data_9E0D
# 
_entry.id   9E0D 
# 
_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   9E0D         pdb_00009e0d 10.2210/pdb9e0d/pdb 
WWPDB D_1000289169 ?            ?                   
# 
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                        9E0D 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-17 
_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    2    ?                ? ? ? 
4  non-polymer syn 'FORMIC ACID'                       46.025     4    ?                ? ? ? 
5  non-polymer syn '(2H-1,3-benzodioxol-5-yl)methanol' 152.147    2    ?                ? ? ? 
6  non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE   663.425    2    ?                ? ? ? 
7  non-polymer syn 'SULFATE ION'                       96.063     6    ?                ? ? ? 
8  non-polymer syn 'MAGNESIUM ION'                     24.305     2    ?                ? ? ? 
9  non-polymer syn 'PENTAETHYLENE GLYCOL'              238.278    1    ?                ? ? ? 
10 non-polymer syn 'DI(HYDROXYETHYL)ETHER'             106.120    2    ?                ? ? ? 
11 water       nat water                               18.015     2387 ?                ? ? ? 
# 
_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  '(2H-1,3-benzodioxol-5-yl)methanol' A1BDV 
6  NICOTINAMIDE-ADENINE-DINUCLEOTIDE   NAD   
7  'SULFATE ION'                       SO4   
8  'MAGNESIUM ION'                     MG    
9  'PENTAETHYLENE GLYCOL'              1PE   
10 'DI(HYDROXYETHYL)ETHER'             PEG   
11 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 
1PE   non-polymer         . 'PENTAETHYLENE GLYCOL'              PEG400              'C10 H22 O6'        238.278 
A1BDV non-polymer         . '(2H-1,3-benzodioxol-5-yl)methanol' 'piperonyl alcohol' 'C8 H8 O3'          152.147 
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 
MG    non-polymer         . 'MAGNESIUM ION'                     ?                   'Mg 2'              24.305  
NAD   non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE   ?                   'C21 H27 N7 O14 P2' 663.425 
PEG   non-polymer         . 'DI(HYDROXYETHYL)ETHER'             ?                   'C4 H10 O3'         106.120 
PGE   non-polymer         . 'TRIETHYLENE GLYCOL'                ?                   'C6 H14 O4'         150.173 
PHE   'L-peptide linking' y PHENYLALANINE                       ?                   'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                             ?                   'C5 H9 N O2'        115.130 
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   79   HIS HIS A . n 
A 1 82   SER 82   80   ?    ?   ?   A . n 
A 1 83   GLY 83   81   ?    ?   ?   A . n 
A 1 84   SER 84   82   82   SER SER A . n 
A 1 85   GLY 85   83   83   GLY GLY A . n 
A 1 86   VAL 86   84   84   VAL VAL A . n 
A 1 87   GLU 87   85   85   GLU GLU A . n 
A 1 88   GLY 88   86   86   GLY GLY A . n 
A 1 89   LEU 89   87   87   LEU LEU A . n 
A 1 90   VAL 90   88   88   VAL VAL A . n 
A 1 91   GLN 91   89   89   GLN GLN A . n 
A 1 92   GLU 92   90   90   GLU GLU A . n 
A 1 93   TYR 93   91   91   TYR TYR A . n 
A 1 94   SER 94   92   92   SER SER A . n 
A 1 95   LEU 95   93   93   LEU LEU A . n 
A 1 96   SER 96   94   94   SER SER A . n 
A 1 97   SER 97   95   95   SER SER A . n 
A 1 98   GLN 98   96   96   GLN GLN A . n 
A 1 99   GLU 99   97   97   GLU GLU A . n 
A 1 100  GLY 100  98   98   GLY GLY A . n 
A 1 101  VAL 101  99   99   VAL VAL A . n 
A 1 102  ALA 102  100  100  ALA ALA A . n 
A 1 103  LEU 103  101  101  LEU LEU A . n 
A 1 104  MET 104  102  102  MET MET A . n 
A 1 105  CYS 105  103  103  CYS CYS A . n 
A 1 106  LEU 106  104  104  LEU LEU A . n 
A 1 107  ALA 107  105  105  ALA ALA A . n 
A 1 108  GLU 108  106  106  GLU GLU A . n 
A 1 109  ALA 109  107  107  ALA ALA A . n 
A 1 110  LEU 110  108  108  LEU LEU A . n 
A 1 111  LEU 111  109  109  LEU LEU A . n 
A 1 112  ARG 112  110  110  ARG ARG A . n 
A 1 113  ILE 113  111  111  ILE ILE A . n 
A 1 114  PRO 114  112  112  PRO PRO A . n 
A 1 115  ASP 115  113  113  ASP ASP A . n 
A 1 116  THR 116  114  114  THR THR A . n 
A 1 117  ALA 117  115  115  ALA ALA A . n 
A 1 118  THR 118  116  116  THR THR A . n 
A 1 119  ARG 119  117  117  ARG ARG A . n 
A 1 120  ASP 120  118  118  ASP ASP A . n 
A 1 121  ALA 121  119  119  ALA ALA A . n 
A 1 122  LEU 122  120  120  LEU LEU A . n 
A 1 123  ILE 123  121  121  ILE ILE A . n 
A 1 124  ARG 124  122  122  ARG ARG A . n 
A 1 125  ASP 125  123  123  ASP ASP A . n 
A 1 126  LYS 126  124  124  LYS LYS A . n 
A 1 127  ILE 127  125  125  ILE ILE A . n 
A 1 128  ALA 128  126  126  ALA ALA A . n 
A 1 129  ASP 129  127  127  ASP ASP A . n 
A 1 130  GLY 130  128  128  GLY GLY A . n 
A 1 131  ASN 131  129  129  ASN ASN A . n 
A 1 132  TRP 132  130  130  TRP TRP A . n 
A 1 133  LYS 133  131  131  LYS LYS A . n 
A 1 134  SER 134  132  132  SER SER A . n 
A 1 135  HIS 135  133  133  HIS HIS A . n 
A 1 136  LEU 136  134  134  LEU LEU A . n 
A 1 137  GLY 137  135  ?    ?   ?   A . n 
A 1 138  GLY 138  136  ?    ?   ?   A . n 
A 1 139  SER 139  137  137  SER SER A . n 
A 1 140  ARG 140  138  138  ARG ARG A . n 
A 1 141  SER 141  139  139  SER SER A . n 
A 1 142  LEU 142  140  140  LEU LEU A . n 
A 1 143  PHE 143  141  141  PHE PHE A . n 
A 1 144  VAL 144  142  142  VAL VAL A . n 
A 1 145  ASN 145  143  143  ASN ASN A . n 
A 1 146  ALA 146  144  144  ALA ALA A . n 
A 1 147  ALA 147  145  145  ALA ALA A . n 
A 1 148  THR 148  146  146  THR THR A . n 
A 1 149  TRP 149  147  147  TRP TRP A . n 
A 1 150  GLY 150  148  148  GLY GLY A . n 
A 1 151  LEU 151  149  149  LEU LEU A . n 
A 1 152  VAL 152  150  150  VAL VAL A . n 
A 1 153  VAL 153  151  151  VAL VAL A . n 
A 1 154  THR 154  152  152  THR THR A . n 
A 1 155  GLY 155  153  153  GLY GLY A . n 
A 1 156  LYS 156  154  154  LYS LYS A . n 
A 1 157  LEU 157  155  155  LEU LEU A . n 
A 1 158  THR 158  156  156  THR THR A . n 
A 1 159  SER 159  157  157  SER SER A . n 
A 1 160  THR 160  158  158  THR THR A . n 
A 1 161  VAL 161  159  159  VAL VAL A . n 
A 1 162  ASN 162  160  160  ASN ASN A . n 
A 1 163  ASP 163  161  161  ASP ASP A . n 
A 1 164  ARG 164  162  162  ARG ARG A . n 
A 1 165  SER 165  163  163  SER SER A . n 
A 1 166  LEU 166  164  164  LEU LEU A . n 
A 1 167  ALA 167  165  165  ALA ALA A . n 
A 1 168  ALA 168  166  166  ALA ALA A . n 
A 1 169  ALA 169  167  167  ALA ALA A . n 
A 1 170  LEU 170  168  168  LEU LEU A . n 
A 1 171  THR 171  169  169  THR THR A . n 
A 1 172  ARG 172  170  170  ARG ARG A . n 
A 1 173  LEU 173  171  171  LEU LEU A . n 
A 1 174  ILE 174  172  172  ILE ILE A . n 
A 1 175  SER 175  173  173  SER SER A . n 
A 1 176  ARG 176  174  174  ARG ARG A . n 
A 1 177  CYS 177  175  175  CYS CYS A . n 
A 1 178  GLY 178  176  176  GLY GLY A . n 
A 1 179  GLU 179  177  177  GLU GLU A . n 
A 1 180  PRO 180  178  178  PRO PRO A . n 
A 1 181  VAL 181  179  179  VAL VAL A . n 
A 1 182  ILE 182  180  180  ILE ILE A . n 
A 1 183  ARG 183  181  181  ARG ARG A . n 
A 1 184  ARG 184  182  182  ARG ARG A . n 
A 1 185  GLY 185  183  183  GLY GLY A . n 
A 1 186  VAL 186  184  184  VAL VAL A . n 
A 1 187  ASP 187  185  185  ASP ASP A . n 
A 1 188  MET 188  186  186  MET MET A . n 
A 1 189  ALA 189  187  187  ALA ALA A . n 
A 1 190  MET 190  188  188  MET MET A . n 
A 1 191  ARG 191  189  189  ARG ARG A . n 
A 1 192  MET 192  190  190  MET MET A . n 
A 1 193  MET 193  191  191  MET MET A . n 
A 1 194  GLY 194  192  192  GLY GLY A . n 
A 1 195  GLU 195  193  193  GLU GLU A . n 
A 1 196  GLN 196  194  194  GLN GLN A . n 
A 1 197  PHE 197  195  195  PHE PHE A . n 
A 1 198  VAL 198  196  196  VAL VAL A . n 
A 1 199  THR 199  197  197  THR THR A . n 
A 1 200  GLY 200  198  198  GLY GLY A . n 
A 1 201  GLU 201  199  199  GLU GLU A . n 
A 1 202  THR 202  200  200  THR THR A . n 
A 1 203  ILE 203  201  201  ILE ILE A . n 
A 1 204  ARG 204  202  202  ARG ARG A . n 
A 1 205  GLU 205  203  203  GLU GLU A . n 
A 1 206  ALA 206  204  204  ALA ALA A . n 
A 1 207  LEU 207  205  205  LEU LEU A . n 
A 1 208  LYS 208  206  206  LYS LYS A . n 
A 1 209  ARG 209  207  207  ARG ARG A . n 
A 1 210  SER 210  208  208  SER SER A . n 
A 1 211  LYS 211  209  209  LYS LYS A . n 
A 1 212  GLU 212  210  210  GLU GLU A . n 
A 1 213  LEU 213  211  211  LEU LEU A . n 
A 1 214  GLU 214  212  212  GLU GLU A . n 
A 1 215  GLU 215  213  213  GLU GLU A . n 
A 1 216  LYS 216  214  214  LYS LYS A . n 
A 1 217  GLY 217  215  215  GLY GLY A . n 
A 1 218  PHE 218  216  216  PHE PHE A . n 
A 1 219  SER 219  217  217  SER SER A . n 
A 1 220  TYR 220  218  218  TYR TYR A . n 
A 1 221  SER 221  219  219  SER SER A . n 
A 1 222  TYR 222  220  220  TYR TYR A . n 
A 1 223  ASP 223  221  221  ASP ASP A . n 
A 1 224  MET 224  222  222  MET MET A . n 
A 1 225  LEU 225  223  223  LEU LEU A . n 
A 1 226  GLY 226  224  224  GLY GLY A . n 
A 1 227  GLU 227  225  225  GLU GLU A . n 
A 1 228  ALA 228  226  226  ALA ALA A . n 
A 1 229  ALA 229  227  227  ALA ALA A . n 
A 1 230  THR 230  228  228  THR THR A . n 
A 1 231  THR 231  229  229  THR THR A . n 
A 1 232  ALA 232  230  230  ALA ALA A . n 
A 1 233  ALA 233  231  231  ALA ALA A . n 
A 1 234  ASP 234  232  232  ASP ASP A . n 
A 1 235  ALA 235  233  233  ALA ALA A . n 
A 1 236  GLU 236  234  234  GLU GLU A . n 
A 1 237  ARG 237  235  235  ARG ARG A . n 
A 1 238  TYR 238  236  236  TYR TYR A . n 
A 1 239  TYR 239  237  237  TYR TYR A . n 
A 1 240  ARG 240  238  238  ARG ARG A . n 
A 1 241  ASP 241  239  239  ASP ASP A . n 
A 1 242  TYR 242  240  240  TYR TYR A . n 
A 1 243  GLU 243  241  241  GLU GLU A . n 
A 1 244  SER 244  242  242  SER SER A . n 
A 1 245  ALA 245  243  243  ALA ALA A . n 
A 1 246  ILE 246  244  244  ILE ILE A . n 
A 1 247  HIS 247  245  245  HIS HIS A . n 
A 1 248  ALA 248  246  246  ALA ALA A . n 
A 1 249  ILE 249  247  247  ILE ILE A . n 
A 1 250  GLY 250  248  248  GLY GLY A . n 
A 1 251  LYS 251  249  249  LYS LYS A . n 
A 1 252  ALA 252  250  250  ALA ALA A . n 
A 1 253  SER 253  251  251  SER SER A . n 
A 1 254  ALA 254  252  252  ALA ALA A . n 
A 1 255  GLY 255  253  253  GLY GLY A . n 
A 1 256  ARG 256  254  254  ARG ARG A . n 
A 1 257  GLY 257  255  255  GLY GLY A . n 
A 1 258  ILE 258  256  256  ILE ILE A . n 
A 1 259  TYR 259  257  257  TYR TYR A . n 
A 1 260  GLU 260  258  258  GLU GLU A . n 
A 1 261  GLY 261  259  259  GLY GLY A . n 
A 1 262  PRO 262  260  260  PRO PRO A . n 
A 1 263  GLY 263  261  261  GLY GLY A . n 
A 1 264  ILE 264  262  262  ILE ILE A . n 
A 1 265  SER 265  263  263  SER SER A . n 
A 1 266  ILE 266  264  264  ILE ILE A . n 
A 1 267  LYS 267  265  265  LYS LYS A . n 
A 1 268  LEU 268  266  266  LEU LEU A . n 
A 1 269  SER 269  267  267  SER SER A . n 
A 1 270  ALA 270  268  268  ALA ALA A . n 
A 1 271  LEU 271  269  269  LEU LEU A . n 
A 1 272  HIS 272  270  270  HIS HIS A . n 
A 1 273  PRO 273  271  271  PRO PRO A . n 
A 1 274  ARG 274  272  272  ARG ARG A . n 
A 1 275  TYR 275  273  273  TYR TYR A . n 
A 1 276  SER 276  274  274  SER SER A . n 
A 1 277  ARG 277  275  275  ARG ARG A . n 
A 1 278  ALA 278  276  276  ALA ALA A . n 
A 1 279  GLN 279  277  277  GLN GLN A . n 
A 1 280  ALA 280  278  278  ALA ALA A . n 
A 1 281  ALA 281  279  279  ALA ALA A . n 
A 1 282  ARG 282  280  280  ARG ARG A . n 
A 1 283  VAL 283  281  281  VAL VAL A . n 
A 1 284  MET 284  282  282  MET MET A . n 
A 1 285  GLY 285  283  283  GLY GLY A . n 
A 1 286  GLU 286  284  284  GLU GLU A . n 
A 1 287  LEU 287  285  285  LEU LEU A . n 
A 1 288  LEU 288  286  286  LEU LEU A . n 
A 1 289  PRO 289  287  287  PRO PRO A . n 
A 1 290  ARG 290  288  288  ARG ARG A . n 
A 1 291  VAL 291  289  289  VAL VAL A . n 
A 1 292  LYS 292  290  290  LYS LYS A . n 
A 1 293  ALA 293  291  291  ALA ALA A . n 
A 1 294  LEU 294  292  292  LEU LEU A . n 
A 1 295  ALA 295  293  293  ALA ALA A . n 
A 1 296  LEU 296  294  294  LEU LEU A . n 
A 1 297  LEU 297  295  295  LEU LEU A . n 
A 1 298  ALA 298  296  296  ALA ALA A . n 
A 1 299  LYS 299  297  297  LYS LYS A . n 
A 1 300  ASN 300  298  298  ASN ASN A . n 
A 1 301  TYR 301  299  299  TYR TYR A . n 
A 1 302  ASP 302  300  300  ASP ASP A . n 
A 1 303  ILE 303  301  301  ILE ILE A . n 
A 1 304  GLY 304  302  302  GLY GLY A . n 
A 1 305  LEU 305  303  303  LEU LEU A . n 
A 1 306  ASN 306  304  304  ASN ASN A . n 
A 1 307  ILE 307  305  305  ILE ILE A . n 
A 1 308  ASP 308  306  306  ASP ASP A . n 
A 1 309  ALA 309  307  307  ALA ALA A . n 
A 1 310  GLU 310  308  308  GLU GLU A . n 
A 1 311  GLU 311  309  309  GLU GLU A . n 
A 1 312  ALA 312  310  310  ALA ALA A . n 
A 1 313  ASP 313  311  311  ASP ASP A . n 
A 1 314  ARG 314  312  312  ARG ARG A . n 
A 1 315  LEU 315  313  313  LEU LEU A . n 
A 1 316  GLU 316  314  314  GLU GLU A . n 
A 1 317  LEU 317  315  315  LEU LEU A . n 
A 1 318  SER 318  316  316  SER SER A . n 
A 1 319  LEU 319  317  317  LEU LEU A . n 
A 1 320  ASP 320  318  318  ASP ASP A . n 
A 1 321  LEU 321  319  319  LEU LEU A . n 
A 1 322  LEU 322  320  320  LEU LEU A . n 
A 1 323  GLU 323  321  321  GLU GLU A . n 
A 1 324  VAL 324  322  322  VAL VAL A . n 
A 1 325  LEU 325  323  323  LEU LEU A . n 
A 1 326  CYS 326  324  324  CYS CYS A . n 
A 1 327  LEU 327  325  325  LEU LEU A . n 
A 1 328  ASP 328  326  326  ASP ASP A . n 
A 1 329  GLY 329  327  327  GLY GLY A . n 
A 1 330  ASP 330  328  328  ASP ASP A . n 
A 1 331  LEU 331  329  329  LEU LEU A . n 
A 1 332  SER 332  330  330  SER SER A . n 
A 1 333  GLY 333  331  331  GLY GLY A . n 
A 1 334  TRP 334  332  332  TRP TRP A . n 
A 1 335  ASN 335  333  333  ASN ASN A . n 
A 1 336  GLY 336  334  334  GLY GLY A . n 
A 1 337  MET 337  335  335  MET MET A . n 
A 1 338  GLY 338  336  336  GLY GLY A . n 
A 1 339  PHE 339  337  337  PHE PHE A . n 
A 1 340  VAL 340  338  338  VAL VAL A . n 
A 1 341  VAL 341  339  339  VAL VAL A . n 
A 1 342  GLN 342  340  340  GLN GLN A . n 
A 1 343  ALA 343  341  341  ALA ALA A . n 
A 1 344  TYR 344  342  342  TYR TYR A . n 
A 1 345  GLY 345  343  343  GLY GLY A . n 
A 1 346  LYS 346  344  344  LYS LYS A . n 
A 1 347  ARG 347  345  345  ARG ARG A . n 
A 1 348  CYS 348  346  346  CYS CYS A . n 
A 1 349  PRO 349  347  347  PRO PRO A . n 
A 1 350  PHE 350  348  348  PHE PHE A . n 
A 1 351  VAL 351  349  349  VAL VAL A . n 
A 1 352  LEU 352  350  350  LEU LEU A . n 
A 1 353  ASP 353  351  351  ASP ASP A . n 
A 1 354  PHE 354  352  352  PHE PHE A . n 
A 1 355  ILE 355  353  353  ILE ILE A . n 
A 1 356  ILE 356  354  354  ILE ILE A . n 
A 1 357  ASP 357  355  355  ASP ASP A . n 
A 1 358  LEU 358  356  356  LEU LEU A . n 
A 1 359  ALA 359  357  357  ALA ALA A . n 
A 1 360  ARG 360  358  358  ARG ARG A . n 
A 1 361  ARG 361  359  359  ARG ARG A . n 
A 1 362  SER 362  360  360  SER SER A . n 
A 1 363  GLY 363  361  361  GLY GLY A . n 
A 1 364  ARG 364  362  362  ARG ARG A . n 
A 1 365  ARG 365  363  363  ARG ARG A . n 
A 1 366  ILE 366  364  364  ILE ILE A . n 
A 1 367  MET 367  365  365  MET MET A . n 
A 1 368  VAL 368  366  366  VAL VAL A . n 
A 1 369  ARG 369  367  367  ARG ARG A . n 
A 1 370  LEU 370  368  368  LEU LEU A . n 
A 1 371  VAL 371  369  369  VAL VAL A . n 
A 1 372  LYS 372  370  370  LYS LYS A . n 
A 1 373  GLY 373  371  371  GLY GLY A . n 
A 1 374  ALA 374  372  372  ALA ALA A . n 
A 1 375  TYR 375  373  373  TYR TYR A . n 
A 1 376  TRP 376  374  374  TRP TRP A . n 
A 1 377  ASP 377  375  375  ASP ASP A . n 
A 1 378  ALA 378  376  376  ALA ALA A . n 
A 1 379  GLU 379  377  377  GLU GLU A . n 
A 1 380  ILE 380  378  378  ILE ILE A . n 
A 1 381  LYS 381  379  379  LYS LYS A . n 
A 1 382  ARG 382  380  380  ARG ARG A . n 
A 1 383  ALA 383  381  381  ALA ALA A . n 
A 1 384  GLN 384  382  382  GLN GLN A . n 
A 1 385  LEU 385  383  383  LEU LEU A . n 
A 1 386  ASP 386  384  384  ASP ASP A . n 
A 1 387  GLY 387  385  385  GLY GLY A . n 
A 1 388  LEU 388  386  386  LEU LEU A . n 
A 1 389  ALA 389  387  387  ALA ALA A . n 
A 1 390  ASP 390  388  388  ASP ASP A . n 
A 1 391  PHE 391  389  389  PHE PHE A . n 
A 1 392  PRO 392  390  390  PRO PRO A . n 
A 1 393  VAL 393  391  391  VAL VAL A . n 
A 1 394  PHE 394  392  392  PHE PHE A . n 
A 1 395  THR 395  393  393  THR THR A . n 
A 1 396  ARG 396  394  394  ARG ARG A . n 
A 1 397  LYS 397  395  395  LYS LYS A . n 
A 1 398  ILE 398  396  396  ILE ILE A . n 
A 1 399  HIS 399  397  397  HIS HIS A . n 
A 1 400  THR 400  398  398  THR THR A . n 
A 1 401  ASP 401  399  399  ASP ASP A . n 
A 1 402  VAL 402  400  400  VAL VAL A . n 
A 1 403  SER 403  401  401  SER SER A . n 
A 1 404  TYR 404  402  402  TYR TYR A . n 
A 1 405  ILE 405  403  403  ILE ILE A . n 
A 1 406  ALA 406  404  404  ALA ALA A . n 
A 1 407  CYS 407  405  405  CYS CYS A . n 
A 1 408  ALA 408  406  406  ALA ALA A . n 
A 1 409  ALA 409  407  407  ALA ALA A . n 
A 1 410  LYS 410  408  408  LYS LYS A . n 
A 1 411  LEU 411  409  409  LEU LEU A . n 
A 1 412  LEU 412  410  410  LEU LEU A . n 
A 1 413  ALA 413  411  411  ALA ALA A . n 
A 1 414  ALA 414  412  412  ALA ALA A . n 
A 1 415  THR 415  413  413  THR THR A . n 
A 1 416  ASP 416  414  414  ASP ASP A . n 
A 1 417  VAL 417  415  415  VAL VAL A . n 
A 1 418  VAL 418  416  416  VAL VAL A . n 
A 1 419  PHE 419  417  417  PHE PHE A . n 
A 1 420  PRO 420  418  418  PRO PRO A . n 
A 1 421  GLN 421  419  419  GLN GLN A . n 
A 1 422  PHE 422  420  420  PHE PHE A . n 
A 1 423  ALA 423  421  421  ALA ALA A . n 
A 1 424  THR 424  422  422  THR THR A . n 
A 1 425  HIS 425  423  423  HIS HIS A . n 
A 1 426  ASN 426  424  424  ASN ASN A . n 
A 1 427  ALA 427  425  425  ALA ALA A . n 
A 1 428  GLN 428  426  426  GLN GLN A . n 
A 1 429  THR 429  427  427  THR THR A . n 
A 1 430  LEU 430  428  428  LEU LEU A . n 
A 1 431  ALA 431  429  429  ALA ALA A . n 
A 1 432  ALA 432  430  430  ALA ALA A . n 
A 1 433  ILE 433  431  431  ILE ILE A . n 
A 1 434  TYR 434  432  432  TYR TYR A . n 
A 1 435  HIS 435  433  433  HIS HIS A . n 
A 1 436  MET 436  434  434  MET MET A . n 
A 1 437  ALA 437  435  435  ALA ALA A . n 
A 1 438  GLY 438  436  436  GLY GLY A . n 
A 1 439  LYS 439  437  437  LYS LYS A . n 
A 1 440  ASP 440  438  438  ASP ASP A . n 
A 1 441  PHE 441  439  439  PHE PHE A . n 
A 1 442  HIS 442  440  440  HIS HIS A . n 
A 1 443  VAL 443  441  441  VAL VAL A . n 
A 1 444  GLY 444  442  442  GLY GLY A . n 
A 1 445  LYS 445  443  443  LYS LYS A . n 
A 1 446  TYR 446  444  444  TYR TYR A . n 
A 1 447  GLU 447  445  445  GLU GLU A . n 
A 1 448  PHE 448  446  446  PHE PHE A . n 
A 1 449  GLN 449  447  447  GLN GLN A . n 
A 1 450  CYS 450  448  448  CYS CYS A . n 
A 1 451  LEU 451  449  449  LEU LEU A . n 
A 1 452  HIS 452  450  450  HIS HIS A . n 
A 1 453  GLY 453  451  451  GLY GLY A . n 
A 1 454  MET 454  452  452  MET MET A . n 
A 1 455  GLY 455  453  453  GLY GLY A . n 
A 1 456  GLU 456  454  454  GLU GLU A . n 
A 1 457  PRO 457  455  455  PRO PRO A . n 
A 1 458  LEU 458  456  456  LEU LEU A . n 
A 1 459  TYR 459  457  457  TYR TYR A . n 
A 1 460  GLU 460  458  458  GLU GLU A . n 
A 1 461  GLU 461  459  459  GLU GLU A . n 
A 1 462  VAL 462  460  460  VAL VAL A . n 
A 1 463  VAL 463  461  461  VAL VAL A . n 
A 1 464  GLY 464  462  462  GLY GLY A . n 
A 1 465  ARG 465  463  463  ARG ARG A . n 
A 1 466  GLY 466  464  464  GLY GLY A . n 
A 1 467  LYS 467  465  465  LYS LYS A . n 
A 1 468  LEU 468  466  466  LEU LEU A . n 
A 1 469  ASP 469  467  467  ASP ASP A . n 
A 1 470  ARG 470  468  468  ARG ARG A . n 
A 1 471  PRO 471  469  469  PRO PRO A . n 
A 1 472  CYS 472  470  470  CYS CYS A . n 
A 1 473  ARG 473  471  471  ARG ARG A . n 
A 1 474  ILE 474  472  472  ILE ILE A . n 
A 1 475  TYR 475  473  473  TYR TYR A . n 
A 1 476  ALA 476  474  474  ALA ALA A . n 
A 1 477  PRO 477  475  475  PRO PRO A . n 
A 1 478  VAL 478  476  476  VAL VAL A . n 
A 1 479  GLY 479  477  477  GLY GLY A . n 
A 1 480  THR 480  478  478  THR THR A . n 
A 1 481  HIS 481  479  479  HIS HIS A . n 
A 1 482  GLU 482  480  480  GLU GLU A . n 
A 1 483  THR 483  481  481  THR THR A . n 
A 1 484  LEU 484  482  482  LEU LEU A . n 
A 1 485  LEU 485  483  483  LEU LEU A . n 
A 1 486  ALA 486  484  484  ALA ALA A . n 
A 1 487  TYR 487  485  485  TYR TYR A . n 
A 1 488  LEU 488  486  486  LEU LEU A . n 
A 1 489  VAL 489  487  487  VAL VAL A . n 
A 1 490  ARG 490  488  488  ARG ARG A . n 
A 1 491  ARG 491  489  489  ARG ARG A . n 
A 1 492  LEU 492  490  490  LEU LEU A . n 
A 1 493  LEU 493  491  491  LEU LEU A . n 
A 1 494  GLU 494  492  ?    ?   ?   A . n 
A 1 495  ASN 495  493  ?    ?   ?   A . n 
A 1 496  GLY 496  494  494  GLY GLY A . n 
A 1 497  ALA 497  495  495  ALA ALA A . n 
A 1 498  ASN 498  496  496  ASN ASN A . n 
A 1 499  SER 499  497  497  SER SER A . n 
A 1 500  SER 500  498  498  SER SER A . n 
A 1 501  PHE 501  499  499  PHE PHE A . n 
A 1 502  VAL 502  500  500  VAL VAL A . n 
A 1 503  HIS 503  501  501  HIS HIS A . n 
A 1 504  ARG 504  502  502  ARG ARG A . n 
A 1 505  ILE 505  503  503  ILE ILE A . n 
A 1 506  ASN 506  504  504  ASN ASN A . n 
A 1 507  ASP 507  505  505  ASP ASP A . n 
A 1 508  PRO 508  506  506  PRO PRO A . n 
A 1 509  LYS 509  507  507  LYS LYS A . n 
A 1 510  VAL 510  508  508  VAL VAL A . n 
A 1 511  SER 511  509  509  SER SER A . n 
A 1 512  ILE 512  510  510  ILE ILE A . n 
A 1 513  ASP 513  511  511  ASP ASP A . n 
A 1 514  GLU 514  512  512  GLU GLU A . n 
A 1 515  LEU 515  513  513  LEU LEU A . n 
A 1 516  ILE 516  514  514  ILE ILE A . n 
A 1 517  ALA 517  515  515  ALA ALA A . n 
A 1 518  ASP 518  516  516  ASP ASP A . n 
A 1 519  PRO 519  517  517  PRO PRO A . n 
A 1 520  VAL 520  518  518  VAL VAL A . n 
A 1 521  GLU 521  519  519  GLU GLU A . n 
A 1 522  VAL 522  520  520  VAL VAL A . n 
A 1 523  VAL 523  521  521  VAL VAL A . n 
A 1 524  ARG 524  522  522  ARG ARG A . n 
A 1 525  ALA 525  523  523  ALA ALA A . n 
A 1 526  MET 526  524  524  MET MET A . n 
A 1 527  PRO 527  525  525  PRO PRO A . n 
A 1 528  VAL 528  526  526  VAL VAL A . n 
A 1 529  VAL 529  527  527  VAL VAL A . n 
A 1 530  GLY 530  528  528  GLY GLY A . n 
A 1 531  ALA 531  529  529  ALA ALA A . n 
A 1 532  LYS 532  530  530  LYS LYS A . n 
A 1 533  HIS 533  531  531  HIS HIS A . n 
A 1 534  ASP 534  532  532  ASP ASP A . n 
A 1 535  ARG 535  533  533  ARG ARG A . n 
A 1 536  ILE 536  534  534  ILE ILE A . n 
A 1 537  ALA 537  535  535  ALA ALA A . n 
A 1 538  LEU 538  536  536  LEU LEU A . n 
A 1 539  PRO 539  537  537  PRO PRO A . n 
A 1 540  ALA 540  538  538  ALA ALA A . n 
A 1 541  GLU 541  539  539  GLU GLU A . n 
A 1 542  LEU 542  540  540  LEU LEU A . n 
A 1 543  PHE 543  541  541  PHE PHE A . n 
A 1 544  GLY 544  542  542  GLY GLY A . n 
A 1 545  ASP 545  543  543  ASP ASP A . n 
A 1 546  ALA 546  544  544  ALA ALA A . n 
A 1 547  ARG 547  545  545  ARG ARG A . n 
A 1 548  THR 548  546  546  THR THR A . n 
A 1 549  ASN 549  547  547  ASN ASN A . n 
A 1 550  SER 550  548  548  SER SER A . n 
A 1 551  ALA 551  549  549  ALA ALA A . n 
A 1 552  GLY 552  550  550  GLY GLY A . n 
A 1 553  LEU 553  551  551  LEU LEU A . n 
A 1 554  ASP 554  552  552  ASP ASP A . n 
A 1 555  LEU 555  553  553  LEU LEU A . n 
A 1 556  SER 556  554  554  SER SER A . n 
A 1 557  ASN 557  555  555  ASN ASN A . n 
A 1 558  GLU 558  556  556  GLU GLU A . n 
A 1 559  GLU 559  557  557  GLU GLU A . n 
A 1 560  THR 560  558  558  THR THR A . n 
A 1 561  LEU 561  559  559  LEU LEU A . n 
A 1 562  ALA 562  560  560  ALA ALA A . n 
A 1 563  SER 563  561  561  SER SER A . n 
A 1 564  LEU 564  562  562  LEU LEU A . n 
A 1 565  THR 565  563  563  THR THR A . n 
A 1 566  GLU 566  564  564  GLU GLU A . n 
A 1 567  ALA 567  565  565  ALA ALA A . n 
A 1 568  LEU 568  566  566  LEU LEU A . n 
A 1 569  ARG 569  567  567  ARG ARG A . n 
A 1 570  GLU 570  568  568  GLU GLU A . n 
A 1 571  SER 571  569  569  SER SER A . n 
A 1 572  ALA 572  570  570  ALA ALA A . n 
A 1 573  ALA 573  571  571  ALA ALA A . n 
A 1 574  MET 574  572  572  MET MET A . n 
A 1 575  LYS 575  573  573  LYS LYS A . n 
A 1 576  TRP 576  574  574  TRP TRP A . n 
A 1 577  THR 577  575  575  THR THR A . n 
A 1 578  ALA 578  576  576  ALA ALA A . n 
A 1 579  LEU 579  577  577  LEU LEU A . n 
A 1 580  PRO 580  578  578  PRO PRO A . n 
A 1 581  GLN 581  579  579  GLN GLN A . n 
A 1 582  LEU 582  580  580  LEU LEU A . n 
A 1 583  ALA 583  581  581  ALA ALA A . n 
A 1 584  THR 584  582  582  THR THR A . n 
A 1 585  GLY 585  583  583  GLY GLY A . n 
A 1 586  PRO 586  584  584  PRO PRO A . n 
A 1 587  ALA 587  585  585  ALA ALA A . n 
A 1 588  ALA 588  586  586  ALA ALA A . n 
A 1 589  GLY 589  587  587  GLY GLY A . n 
A 1 590  GLU 590  588  588  GLU GLU A . n 
A 1 591  THR 591  589  589  THR THR A . n 
A 1 592  ARG 592  590  590  ARG ARG A . n 
A 1 593  THR 593  591  591  THR THR A . n 
A 1 594  VAL 594  592  592  VAL VAL A . n 
A 1 595  LEU 595  593  593  LEU LEU A . n 
A 1 596  ASN 596  594  594  ASN ASN A . n 
A 1 597  PRO 597  595  595  PRO PRO A . n 
A 1 598  GLY 598  596  596  GLY GLY A . n 
A 1 599  ASP 599  597  597  ASP ASP A . n 
A 1 600  HIS 600  598  598  HIS HIS A . n 
A 1 601  ARG 601  599  599  ARG ARG A . n 
A 1 602  ASP 602  600  600  ASP ASP A . n 
A 1 603  VAL 603  601  601  VAL VAL A . n 
A 1 604  VAL 604  602  602  VAL VAL A . n 
A 1 605  GLY 605  603  603  GLY GLY A . n 
A 1 606  SER 606  604  604  SER SER A . n 
A 1 607  VAL 607  605  605  VAL VAL A . n 
A 1 608  THR 608  606  606  THR THR A . n 
A 1 609  GLU 609  607  607  GLU GLU A . n 
A 1 610  THR 610  608  608  THR THR A . n 
A 1 611  SER 611  609  609  SER SER A . n 
A 1 612  GLU 612  610  610  GLU GLU A . n 
A 1 613  GLU 613  611  611  GLU GLU A . n 
A 1 614  ASP 614  612  612  ASP ASP A . n 
A 1 615  ALA 615  613  613  ALA ALA A . n 
A 1 616  ARG 616  614  614  ARG ARG A . n 
A 1 617  ARG 617  615  615  ARG ARG A . n 
A 1 618  ALA 618  616  616  ALA ALA A . n 
A 1 619  VAL 619  617  617  VAL VAL A . n 
A 1 620  ARG 620  618  618  ARG ARG A . n 
A 1 621  LEU 621  619  619  LEU LEU A . n 
A 1 622  ALA 622  620  620  ALA ALA A . n 
A 1 623  ALA 623  621  621  ALA ALA A . n 
A 1 624  ASP 624  622  622  ASP ASP A . n 
A 1 625  ALA 625  623  623  ALA ALA A . n 
A 1 626  ALA 626  624  624  ALA ALA A . n 
A 1 627  PRO 627  625  625  PRO PRO A . n 
A 1 628  ASP 628  626  626  ASP ASP A . n 
A 1 629  TRP 629  627  627  TRP TRP A . n 
A 1 630  ALA 630  628  628  ALA ALA A . n 
A 1 631  ALA 631  629  629  ALA ALA A . n 
A 1 632  VAL 632  630  630  VAL VAL A . n 
A 1 633  PRO 633  631  631  PRO PRO A . n 
A 1 634  PRO 634  632  632  PRO PRO A . n 
A 1 635  SER 635  633  633  SER SER A . n 
A 1 636  GLU 636  634  634  GLU GLU A . n 
A 1 637  ARG 637  635  635  ARG ARG A . n 
A 1 638  ALA 638  636  636  ALA ALA A . n 
A 1 639  ALA 639  637  637  ALA ALA A . n 
A 1 640  CYS 640  638  638  CYS CYS A . n 
A 1 641  LEU 641  639  639  LEU LEU A . n 
A 1 642  ASP 642  640  640  ASP ASP A . n 
A 1 643  ARG 643  641  641  ARG ARG A . n 
A 1 644  ALA 644  642  642  ALA ALA A . n 
A 1 645  ALA 645  643  643  ALA ALA A . n 
A 1 646  GLU 646  644  644  GLU GLU A . n 
A 1 647  LEU 647  645  645  LEU LEU A . n 
A 1 648  MET 648  646  646  MET MET A . n 
A 1 649  GLN 649  647  647  GLN GLN A . n 
A 1 650  ALA 650  648  648  ALA ALA A . n 
A 1 651  ARG 651  649  649  ARG ARG A . n 
A 1 652  MET 652  650  650  MET MET A . n 
A 1 653  PRO 653  651  651  PRO PRO A . n 
A 1 654  THR 654  652  652  THR THR A . n 
A 1 655  LEU 655  653  653  LEU LEU A . n 
A 1 656  LEU 656  654  654  LEU LEU A . n 
A 1 657  GLY 657  655  655  GLY GLY A . n 
A 1 658  LEU 658  656  656  LEU LEU A . n 
A 1 659  ILE 659  657  657  ILE ILE A . n 
A 1 660  ILE 660  658  658  ILE ILE A . n 
A 1 661  ARG 661  659  659  ARG ARG A . n 
A 1 662  GLU 662  660  660  GLU GLU A . n 
A 1 663  ALA 663  661  661  ALA ALA A . n 
A 1 664  GLY 664  662  662  GLY GLY A . n 
A 1 665  LYS 665  663  663  LYS LYS A . n 
A 1 666  SER 666  664  664  SER SER A . n 
A 1 667  ALA 667  665  665  ALA ALA A . n 
A 1 668  LEU 668  666  666  LEU LEU A . n 
A 1 669  ASN 669  667  667  ASN ASN A . n 
A 1 670  ALA 670  668  668  ALA ALA A . n 
A 1 671  ILE 671  669  669  ILE ILE A . n 
A 1 672  ALA 672  670  670  ALA ALA A . n 
A 1 673  GLU 673  671  671  GLU GLU A . n 
A 1 674  VAL 674  672  672  VAL VAL A . n 
A 1 675  ARG 675  673  673  ARG ARG A . n 
A 1 676  GLU 676  674  674  GLU GLU A . n 
A 1 677  ALA 677  675  675  ALA ALA A . n 
A 1 678  ILE 678  676  676  ILE ILE A . n 
A 1 679  ASP 679  677  677  ASP ASP A . n 
A 1 680  PHE 680  678  678  PHE PHE A . n 
A 1 681  LEU 681  679  679  LEU LEU A . n 
A 1 682  ARG 682  680  680  ARG ARG A . n 
A 1 683  TYR 683  681  681  TYR TYR A . n 
A 1 684  TYR 684  682  682  TYR TYR A . n 
A 1 685  ALA 685  683  683  ALA ALA A . n 
A 1 686  GLU 686  684  684  GLU GLU A . n 
A 1 687  GLN 687  685  685  GLN GLN A . n 
A 1 688  THR 688  686  686  THR THR A . n 
A 1 689  ARG 689  687  687  ARG ARG A . n 
A 1 690  ARG 690  688  688  ARG ARG A . n 
A 1 691  THR 691  689  689  THR THR A . n 
A 1 692  LEU 692  690  690  LEU LEU A . n 
A 1 693  GLY 693  691  691  GLY GLY A . n 
A 1 694  PRO 694  692  692  PRO PRO A . n 
A 1 695  GLY 695  693  693  GLY GLY A . n 
A 1 696  HIS 696  694  694  HIS HIS A . n 
A 1 697  GLY 697  695  695  GLY GLY A . n 
A 1 698  PRO 698  696  696  PRO PRO A . n 
A 1 699  LEU 699  697  697  LEU LEU A . n 
A 1 700  GLY 700  698  698  GLY GLY A . n 
A 1 701  PRO 701  699  699  PRO PRO A . n 
A 1 702  ILE 702  700  700  ILE ILE A . n 
A 1 703  VAL 703  701  701  VAL VAL A . n 
A 1 704  CYS 704  702  702  CYS CYS A . n 
A 1 705  ILE 705  703  703  ILE ILE A . n 
A 1 706  SER 706  704  704  SER SER A . n 
A 1 707  PRO 707  705  705  PRO PRO A . n 
A 1 708  TRP 708  706  706  TRP TRP A . n 
A 1 709  ASN 709  707  707  ASN ASN A . n 
A 1 710  PHE 710  708  708  PHE PHE A . n 
A 1 711  PRO 711  709  709  PRO PRO A . n 
A 1 712  LEU 712  710  710  LEU LEU A . n 
A 1 713  ALA 713  711  711  ALA ALA A . n 
A 1 714  ILE 714  712  712  ILE ILE A . n 
A 1 715  PHE 715  713  713  PHE PHE A . n 
A 1 716  THR 716  714  714  THR THR A . n 
A 1 717  GLY 717  715  715  GLY GLY A . n 
A 1 718  GLN 718  716  716  GLN GLN A . n 
A 1 719  ILE 719  717  717  ILE ILE A . n 
A 1 720  ALA 720  718  718  ALA ALA A . n 
A 1 721  ALA 721  719  719  ALA ALA A . n 
A 1 722  ALA 722  720  720  ALA ALA A . n 
A 1 723  LEU 723  721  721  LEU LEU A . n 
A 1 724  VAL 724  722  722  VAL VAL A . n 
A 1 725  ALA 725  723  723  ALA ALA A . n 
A 1 726  GLY 726  724  724  GLY GLY A . n 
A 1 727  ASN 727  725  725  ASN ASN A . n 
A 1 728  PRO 728  726  726  PRO PRO A . n 
A 1 729  VAL 729  727  727  VAL VAL A . n 
A 1 730  LEU 730  728  728  LEU LEU A . n 
A 1 731  ALA 731  729  729  ALA ALA A . n 
A 1 732  LYS 732  730  730  LYS LYS A . n 
A 1 733  PRO 733  731  731  PRO PRO A . n 
A 1 734  ALA 734  732  732  ALA ALA A . n 
A 1 735  GLU 735  733  733  GLU GLU A . n 
A 1 736  GLU 736  734  734  GLU GLU A . n 
A 1 737  THR 737  735  735  THR THR A . n 
A 1 738  PRO 738  736  736  PRO PRO A . n 
A 1 739  LEU 739  737  737  LEU LEU A . n 
A 1 740  ILE 740  738  738  ILE ILE A . n 
A 1 741  ALA 741  739  739  ALA ALA A . n 
A 1 742  ALA 742  740  740  ALA ALA A . n 
A 1 743  GLU 743  741  741  GLU GLU A . n 
A 1 744  GLY 744  742  742  GLY GLY A . n 
A 1 745  VAL 745  743  743  VAL VAL A . n 
A 1 746  ARG 746  744  744  ARG ARG A . n 
A 1 747  ILE 747  745  745  ILE ILE A . n 
A 1 748  LEU 748  746  746  LEU LEU A . n 
A 1 749  ARG 749  747  747  ARG ARG A . n 
A 1 750  GLU 750  748  748  GLU GLU A . n 
A 1 751  ALA 751  749  749  ALA ALA A . n 
A 1 752  GLY 752  750  750  GLY GLY A . n 
A 1 753  ILE 753  751  751  ILE ILE A . n 
A 1 754  PRO 754  752  752  PRO PRO A . n 
A 1 755  ALA 755  753  753  ALA ALA A . n 
A 1 756  SER 756  754  754  SER SER A . n 
A 1 757  ALA 757  755  755  ALA ALA A . n 
A 1 758  LEU 758  756  756  LEU LEU A . n 
A 1 759  GLN 759  757  757  GLN GLN A . n 
A 1 760  LEU 760  758  758  LEU LEU A . n 
A 1 761  LEU 761  759  759  LEU LEU A . n 
A 1 762  PRO 762  760  760  PRO PRO A . n 
A 1 763  GLY 763  761  761  GLY GLY A . n 
A 1 764  ASP 764  762  762  ASP ASP A . n 
A 1 765  GLY 765  763  763  GLY GLY A . n 
A 1 766  ARG 766  764  764  ARG ARG A . n 
A 1 767  VAL 767  765  765  VAL VAL A . n 
A 1 768  GLY 768  766  766  GLY GLY A . n 
A 1 769  ALA 769  767  767  ALA ALA A . n 
A 1 770  ALA 770  768  768  ALA ALA A . n 
A 1 771  LEU 771  769  769  LEU LEU A . n 
A 1 772  VAL 772  770  770  VAL VAL A . n 
A 1 773  ALA 773  771  771  ALA ALA A . n 
A 1 774  ALA 774  772  772  ALA ALA A . n 
A 1 775  ALA 775  773  773  ALA ALA A . n 
A 1 776  GLU 776  774  774  GLU GLU A . n 
A 1 777  THR 777  775  775  THR THR A . n 
A 1 778  ALA 778  776  776  ALA ALA A . n 
A 1 779  GLY 779  777  777  GLY GLY A . n 
A 1 780  VAL 780  778  778  VAL VAL A . n 
A 1 781  MET 781  779  779  MET MET A . n 
A 1 782  PHE 782  780  780  PHE PHE A . n 
A 1 783  THR 783  781  781  THR THR A . n 
A 1 784  GLY 784  782  782  GLY GLY A . n 
A 1 785  SER 785  783  783  SER SER A . n 
A 1 786  THR 786  784  784  THR THR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  VAL 788  786  786  VAL VAL A . n 
A 1 789  ALA 789  787  787  ALA ALA A . n 
A 1 790  ARG 790  788  788  ARG ARG A . n 
A 1 791  LEU 791  789  789  LEU LEU A . n 
A 1 792  ILE 792  790  790  ILE ILE A . n 
A 1 793  GLN 793  791  791  GLN GLN A . n 
A 1 794  ALA 794  792  792  ALA ALA A . n 
A 1 795  GLN 795  793  793  GLN GLN A . n 
A 1 796  LEU 796  794  794  LEU LEU A . n 
A 1 797  ALA 797  795  795  ALA ALA A . n 
A 1 798  ASP 798  796  796  ASP ASP A . n 
A 1 799  ARG 799  797  797  ARG ARG A . n 
A 1 800  LEU 800  798  798  LEU LEU A . n 
A 1 801  SER 801  799  799  SER SER A . n 
A 1 802  PRO 802  800  800  PRO PRO A . n 
A 1 803  ALA 803  801  801  ALA ALA A . n 
A 1 804  GLY 804  802  802  GLY GLY A . n 
A 1 805  ARG 805  803  803  ARG ARG A . n 
A 1 806  PRO 806  804  804  PRO PRO A . n 
A 1 807  ILE 807  805  805  ILE ILE A . n 
A 1 808  PRO 808  806  806  PRO PRO A . n 
A 1 809  LEU 809  807  807  LEU LEU A . n 
A 1 810  ILE 810  808  808  ILE ILE A . n 
A 1 811  ALA 811  809  809  ALA ALA A . n 
A 1 812  GLU 812  810  810  GLU GLU A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  GLY 814  812  812  GLY GLY A . n 
A 1 815  GLY 815  813  813  GLY GLY A . n 
A 1 816  GLN 816  814  814  GLN GLN A . n 
A 1 817  ASN 817  815  815  ASN ASN A . n 
A 1 818  ALA 818  816  816  ALA ALA A . n 
A 1 819  MET 819  817  817  MET MET A . n 
A 1 820  ILE 820  818  818  ILE ILE A . n 
A 1 821  VAL 821  819  819  VAL VAL A . n 
A 1 822  ASP 822  820  820  ASP ASP A . n 
A 1 823  SER 823  821  821  SER SER A . n 
A 1 824  SER 824  822  822  SER SER A . n 
A 1 825  ALA 825  823  823  ALA ALA A . n 
A 1 826  LEU 826  824  824  LEU LEU A . n 
A 1 827  ALA 827  825  825  ALA ALA A . n 
A 1 828  GLU 828  826  826  GLU GLU A . n 
A 1 829  GLN 829  827  827  GLN GLN A . n 
A 1 830  VAL 830  828  828  VAL VAL A . n 
A 1 831  VAL 831  829  829  VAL VAL A . n 
A 1 832  GLY 832  830  830  GLY GLY A . n 
A 1 833  ASP 833  831  831  ASP ASP A . n 
A 1 834  VAL 834  832  832  VAL VAL A . n 
A 1 835  ILE 835  833  833  ILE ILE A . n 
A 1 836  THR 836  834  834  THR THR A . n 
A 1 837  SER 837  835  835  SER SER A . n 
A 1 838  ALA 838  836  836  ALA ALA A . n 
A 1 839  PHE 839  837  837  PHE PHE A . n 
A 1 840  ASP 840  838  838  ASP ASP A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  ALA 842  840  840  ALA ALA A . n 
A 1 843  GLY 843  841  841  GLY GLY A . n 
A 1 844  GLN 844  842  842  GLN GLN A . n 
A 1 845  ARG 845  843  843  ARG ARG A . n 
A 1 846  CYS 846  844  844  CYS CYS A . n 
A 1 847  SER 847  845  845  SER SER A . n 
A 1 848  ALA 848  846  846  ALA ALA A . n 
A 1 849  LEU 849  847  847  LEU LEU A . n 
A 1 850  ARG 850  848  848  ARG ARG A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LEU 852  850  850  LEU LEU A . n 
A 1 853  CYS 853  851  851  CYS CYS A . n 
A 1 854  LEU 854  852  852  LEU LEU A . n 
A 1 855  GLN 855  853  853  GLN GLN A . n 
A 1 856  GLU 856  854  854  GLU GLU A . n 
A 1 857  ASP 857  855  855  ASP ASP A . n 
A 1 858  VAL 858  856  856  VAL VAL A . n 
A 1 859  ALA 859  857  857  ALA ALA A . n 
A 1 860  ASP 860  858  858  ASP ASP A . n 
A 1 861  ARG 861  859  859  ARG ARG A . n 
A 1 862  ILE 862  860  860  ILE ILE A . n 
A 1 863  LEU 863  861  861  LEU LEU A . n 
A 1 864  THR 864  862  862  THR THR A . n 
A 1 865  MET 865  863  863  MET MET A . n 
A 1 866  LEU 866  864  864  LEU LEU A . n 
A 1 867  LYS 867  865  865  LYS LYS A . n 
A 1 868  GLY 868  866  866  GLY GLY A . n 
A 1 869  ALA 869  867  867  ALA ALA A . n 
A 1 870  LEU 870  868  868  LEU LEU A . n 
A 1 871  HIS 871  869  869  HIS HIS A . n 
A 1 872  GLU 872  870  870  GLU GLU A . n 
A 1 873  LEU 873  871  871  LEU LEU A . n 
A 1 874  HIS 874  872  872  HIS HIS A . n 
A 1 875  ILE 875  873  873  ILE ILE A . n 
A 1 876  GLY 876  874  874  GLY GLY A . n 
A 1 877  ARG 877  875  875  ARG ARG A . n 
A 1 878  THR 878  876  876  THR THR A . n 
A 1 879  ASP 879  877  877  ASP ASP A . n 
A 1 880  ARG 880  878  878  ARG ARG A . n 
A 1 881  LEU 881  879  879  LEU LEU A . n 
A 1 882  SER 882  880  880  SER SER A . n 
A 1 883  VAL 883  881  881  VAL VAL A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  VAL 885  883  883  VAL VAL A . n 
A 1 886  GLY 886  884  884  GLY GLY A . n 
A 1 887  PRO 887  885  885  PRO PRO A . n 
A 1 888  VAL 888  886  886  VAL VAL A . n 
A 1 889  ILE 889  887  887  ILE ILE A . n 
A 1 890  THR 890  888  888  THR THR A . n 
A 1 891  SER 891  889  889  SER SER A . n 
A 1 892  GLU 892  890  890  GLU GLU A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  LYS 894  892  892  LYS LYS A . n 
A 1 895  ASP 895  893  893  ASP ASP A . n 
A 1 896  ASN 896  894  894  ASN ASN A . n 
A 1 897  ILE 897  895  895  ILE ILE A . n 
A 1 898  GLU 898  896  896  GLU GLU A . n 
A 1 899  LYS 899  897  897  LYS LYS A . n 
A 1 900  HIS 900  898  898  HIS HIS A . n 
A 1 901  ILE 901  899  899  ILE ILE A . n 
A 1 902  GLU 902  900  900  GLU GLU A . n 
A 1 903  ARG 903  901  901  ARG ARG A . n 
A 1 904  MET 904  902  902  MET MET A . n 
A 1 905  ARG 905  903  903  ARG ARG A . n 
A 1 906  GLY 906  904  904  GLY GLY A . n 
A 1 907  LEU 907  905  905  LEU LEU A . n 
A 1 908  GLY 908  906  906  GLY GLY A . n 
A 1 909  ARG 909  907  907  ARG ARG A . n 
A 1 910  LYS 910  908  908  LYS LYS A . n 
A 1 911  VAL 911  909  909  VAL VAL A . n 
A 1 912  GLU 912  910  910  GLU GLU A . n 
A 1 913  GLN 913  911  911  GLN GLN A . n 
A 1 914  ILE 914  912  912  ILE ILE A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  ALA 917  915  915  ALA ALA A . n 
A 1 918  SER 918  916  916  SER SER A . n 
A 1 919  GLU 919  917  917  GLU GLU A . n 
A 1 920  THR 920  918  918  THR THR A . n 
A 1 921  GLY 921  919  919  GLY GLY A . n 
A 1 922  VAL 922  920  920  VAL VAL A . n 
A 1 923  GLY 923  921  921  GLY GLY A . n 
A 1 924  THR 924  922  922  THR THR A . n 
A 1 925  PHE 925  923  923  PHE PHE A . n 
A 1 926  VAL 926  924  924  VAL VAL A . n 
A 1 927  PRO 927  925  925  PRO PRO A . n 
A 1 928  PRO 928  926  926  PRO PRO A . n 
A 1 929  THR 929  927  927  THR THR A . n 
A 1 930  ILE 930  928  928  ILE ILE A . n 
A 1 931  ILE 931  929  929  ILE ILE A . n 
A 1 932  GLU 932  930  930  GLU GLU A . n 
A 1 933  LEU 933  931  931  LEU LEU A . n 
A 1 934  GLU 934  932  932  GLU GLU A . n 
A 1 935  LYS 935  933  933  LYS LYS A . n 
A 1 936  LEU 936  934  934  LEU LEU A . n 
A 1 937  SER 937  935  935  SER SER A . n 
A 1 938  ASP 938  936  936  ASP ASP A . n 
A 1 939  LEU 939  937  937  LEU LEU A . n 
A 1 940  GLN 940  938  938  GLN GLN A . n 
A 1 941  ARG 941  939  939  ARG ARG A . n 
A 1 942  GLU 942  940  940  GLU GLU A . n 
A 1 943  VAL 943  941  941  VAL VAL A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  GLY 945  943  943  GLY GLY A . n 
A 1 946  PRO 946  944  944  PRO PRO A . n 
A 1 947  VAL 947  945  945  VAL VAL A . n 
A 1 948  LEU 948  946  946  LEU LEU A . n 
A 1 949  HIS 949  947  947  HIS HIS A . n 
A 1 950  VAL 950  948  948  VAL VAL A . n 
A 1 951  ILE 951  949  949  ILE ILE A . n 
A 1 952  ARG 952  950  950  ARG ARG A . n 
A 1 953  TYR 953  951  951  TYR TYR A . n 
A 1 954  ARG 954  952  952  ARG ARG A . n 
A 1 955  ARG 955  953  953  ARG ARG A . n 
A 1 956  ASP 956  954  954  ASP ASP A . n 
A 1 957  ASP 957  955  955  ASP ASP A . n 
A 1 958  LEU 958  956  956  LEU LEU A . n 
A 1 959  ASP 959  957  957  ASP ASP A . n 
A 1 960  ARG 960  958  958  ARG ARG A . n 
A 1 961  LEU 961  959  959  LEU LEU A . n 
A 1 962  VAL 962  960  960  VAL VAL A . n 
A 1 963  ASP 963  961  961  ASP ASP A . n 
A 1 964  ASP 964  962  962  ASP ASP A . n 
A 1 965  VAL 965  963  963  VAL VAL A . n 
A 1 966  ASN 966  964  964  ASN ASN A . n 
A 1 967  ALA 967  965  965  ALA ALA A . n 
A 1 968  THR 968  966  966  THR THR A . n 
A 1 969  GLY 969  967  967  GLY GLY A . n 
A 1 970  TYR 970  968  968  TYR TYR A . n 
A 1 971  GLY 971  969  969  GLY GLY A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  THR 973  971  971  THR THR A . n 
A 1 974  PHE 974  972  972  PHE PHE A . n 
A 1 975  GLY 975  973  973  GLY GLY A . n 
A 1 976  LEU 976  974  974  LEU LEU A . n 
A 1 977  HIS 977  975  975  HIS HIS A . n 
A 1 978  THR 978  976  976  THR THR A . n 
A 1 979  ARG 979  977  977  ARG ARG A . n 
A 1 980  LEU 980  978  978  LEU LEU A . n 
A 1 981  ASP 981  979  979  ASP ASP A . n 
A 1 982  GLU 982  980  980  GLU GLU A . n 
A 1 983  THR 983  981  981  THR THR A . n 
A 1 984  ILE 984  982  982  ILE ILE A . n 
A 1 985  ALA 985  983  983  ALA ALA A . n 
A 1 986  HIS 986  984  984  HIS HIS A . n 
A 1 987  VAL 987  985  985  VAL VAL A . n 
A 1 988  THR 988  986  986  THR THR A . n 
A 1 989  SER 989  987  987  SER SER A . n 
A 1 990  ARG 990  988  988  ARG ARG A . n 
A 1 991  ILE 991  989  989  ILE ILE A . n 
A 1 992  LYS 992  990  990  LYS LYS A . n 
A 1 993  ALA 993  991  991  ALA ALA A . n 
A 1 994  GLY 994  992  992  GLY GLY A . n 
A 1 995  ASN 995  993  993  ASN ASN A . n 
A 1 996  LEU 996  994  994  LEU LEU A . n 
A 1 997  TYR 997  995  995  TYR TYR A . n 
A 1 998  ILE 998  996  996  ILE ILE A . n 
A 1 999  ASN 999  997  997  ASN ASN A . n 
A 1 1000 ARG 1000 998  998  ARG ARG A . n 
A 1 1001 ASN 1001 999  999  ASN ASN A . n 
A 1 1002 ILE 1002 1000 1000 ILE ILE A . n 
A 1 1003 ILE 1003 1001 1001 ILE ILE A . n 
A 1 1004 GLY 1004 1002 1002 GLY GLY A . n 
A 1 1005 ALA 1005 1003 1003 ALA ALA A . n 
A 1 1006 VAL 1006 1004 1004 VAL VAL A . n 
A 1 1007 VAL 1007 1005 1005 VAL VAL A . n 
A 1 1008 GLY 1008 1006 1006 GLY GLY A . n 
A 1 1009 VAL 1009 1007 1007 VAL VAL A . n 
A 1 1010 GLN 1010 1008 1008 GLN GLN A . n 
A 1 1011 PRO 1011 1009 1009 PRO PRO A . n 
A 1 1012 PHE 1012 1010 1010 PHE PHE A . n 
A 1 1013 GLY 1013 1011 1011 GLY GLY A . n 
A 1 1014 GLY 1014 1012 1012 GLY GLY A . n 
A 1 1015 ARG 1015 1013 1013 ARG ARG A . n 
A 1 1016 GLY 1016 1014 1014 GLY GLY A . n 
A 1 1017 LEU 1017 1015 1015 LEU LEU A . n 
A 1 1018 SER 1018 1016 1016 SER SER A . n 
A 1 1019 GLY 1019 1017 1017 GLY GLY A . n 
A 1 1020 THR 1020 1018 1018 THR THR A . n 
A 1 1021 GLY 1021 1019 1019 GLY GLY A . n 
A 1 1022 PRO 1022 1020 1020 PRO PRO A . n 
A 1 1023 LYS 1023 1021 1021 LYS LYS A . n 
A 1 1024 ALA 1024 1022 1022 ALA ALA A . n 
A 1 1025 GLY 1025 1023 1023 GLY GLY A . n 
A 1 1026 GLY 1026 1024 1024 GLY GLY A . n 
A 1 1027 PRO 1027 1025 1025 PRO PRO A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 TYR 1029 1027 1027 TYR TYR A . n 
A 1 1030 LEU 1030 1028 1028 LEU LEU A . n 
A 1 1031 GLY 1031 1029 1029 GLY GLY A . n 
A 1 1032 ARG 1032 1030 1030 ARG ARG A . n 
A 1 1033 LEU 1033 1031 1031 LEU LEU A . n 
A 1 1034 VAL 1034 1032 1032 VAL VAL A . n 
A 1 1035 THR 1035 1033 1033 THR THR A . n 
A 1 1036 THR 1036 1034 1034 THR THR A . n 
A 1 1037 ALA 1037 1035 1035 ALA ALA A . n 
A 1 1038 PRO 1038 1036 1036 PRO PRO A . n 
A 1 1039 VAL 1039 1037 1037 VAL VAL A . n 
A 1 1040 PRO 1040 1038 1038 PRO PRO A . n 
A 1 1041 PRO 1041 1039 1039 PRO PRO A . n 
A 1 1042 GLN 1042 1040 1040 GLN GLN A . n 
A 1 1043 HIS 1043 1041 1041 HIS HIS A . n 
A 1 1044 SER 1044 1042 1042 SER SER A . n 
A 1 1045 SER 1045 1043 1043 SER SER A . n 
A 1 1046 VAL 1046 1044 1044 VAL VAL A . n 
A 1 1047 HIS 1047 1045 1045 HIS HIS A . n 
A 1 1048 THR 1048 1046 1046 THR THR A . n 
A 1 1049 ASP 1049 1047 1047 ASP ASP A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 VAL 1051 1049 1049 VAL VAL A . n 
A 1 1052 LEU 1052 1050 1050 LEU LEU A . n 
A 1 1053 LEU 1053 1051 1051 LEU LEU A . n 
A 1 1054 ASP 1054 1052 1052 ASP ASP A . n 
A 1 1055 PHE 1055 1053 1053 PHE PHE A . n 
A 1 1056 ALA 1056 1054 1054 ALA ALA A . n 
A 1 1057 LYS 1057 1055 1055 LYS LYS A . n 
A 1 1058 TRP 1058 1056 1056 TRP TRP A . n 
A 1 1059 LEU 1059 1057 1057 LEU LEU A . n 
A 1 1060 ASP 1060 1058 1058 ASP ASP A . n 
A 1 1061 GLY 1061 1059 1059 GLY GLY A . n 
A 1 1062 LYS 1062 1060 1060 LYS LYS A . n 
A 1 1063 GLY 1063 1061 1061 GLY GLY A . n 
A 1 1064 ALA 1064 1062 1062 ALA ALA A . n 
A 1 1065 ARG 1065 1063 1063 ARG ARG A . n 
A 1 1066 ALA 1066 1064 1064 ALA ALA A . n 
A 1 1067 GLU 1067 1065 1065 GLU GLU A . n 
A 1 1068 ALA 1068 1066 1066 ALA ALA A . n 
A 1 1069 GLU 1069 1067 1067 GLU GLU A . n 
A 1 1070 ALA 1070 1068 1068 ALA ALA A . n 
A 1 1071 ALA 1071 1069 1069 ALA ALA A . n 
A 1 1072 ARG 1072 1070 1070 ARG ARG A . n 
A 1 1073 ASN 1073 1071 1071 ASN ASN A . n 
A 1 1074 ALA 1074 1072 1072 ALA ALA A . n 
A 1 1075 GLY 1075 1073 1073 GLY GLY A . n 
A 1 1076 SER 1076 1074 1074 SER SER A . n 
A 1 1077 SER 1077 1075 1075 SER SER A . n 
A 1 1078 SER 1078 1076 1076 SER SER A . n 
A 1 1079 ALA 1079 1077 1077 ALA ALA A . n 
A 1 1080 LEU 1080 1078 1078 LEU LEU A . n 
A 1 1081 GLY 1081 1079 1079 GLY GLY A . n 
A 1 1082 LEU 1082 1080 1080 LEU LEU A . n 
A 1 1083 ASP 1083 1081 1081 ASP ASP A . n 
A 1 1084 LEU 1084 1082 1082 LEU LEU A . n 
A 1 1085 GLU 1085 1083 1083 GLU GLU A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 PRO 1087 1085 1085 PRO PRO A . n 
A 1 1088 GLY 1088 1086 1086 GLY GLY A . n 
A 1 1089 PRO 1089 1087 1087 PRO PRO A . n 
A 1 1090 VAL 1090 1088 1088 VAL VAL A . n 
A 1 1091 GLY 1091 1089 1089 GLY GLY A . n 
A 1 1092 GLU 1092 1090 1090 GLU GLU A . n 
A 1 1093 ARG 1093 1091 1091 ARG ARG A . n 
A 1 1094 ASN 1094 1092 1092 ASN ASN A . n 
A 1 1095 LEU 1095 1093 1093 LEU LEU A . n 
A 1 1096 TYR 1096 1094 1094 TYR TYR A . n 
A 1 1097 THR 1097 1095 1095 THR THR A . n 
A 1 1098 LEU 1098 1096 1096 LEU LEU A . n 
A 1 1099 HIS 1099 1097 1097 HIS HIS A . n 
A 1 1100 ALA 1100 1098 1098 ALA ALA A . n 
A 1 1101 ARG 1101 1099 1099 ARG ARG A . n 
A 1 1102 GLY 1102 1100 1100 GLY GLY A . n 
A 1 1103 ARG 1103 1101 1101 ARG ARG A . n 
A 1 1104 ILE 1104 1102 1102 ILE ILE A . n 
A 1 1105 LEU 1105 1103 1103 LEU LEU A . n 
A 1 1106 LEU 1106 1104 1104 LEU LEU A . n 
A 1 1107 VAL 1107 1105 1105 VAL VAL A . n 
A 1 1108 PRO 1108 1106 1106 PRO PRO A . n 
A 1 1109 ALA 1109 1107 1107 ALA ALA A . n 
A 1 1110 THR 1110 1108 1108 THR THR A . n 
A 1 1111 GLU 1111 1109 1109 GLU GLU A . n 
A 1 1112 SER 1112 1110 1110 SER SER A . n 
A 1 1113 GLY 1113 1111 1111 GLY GLY A . n 
A 1 1114 LEU 1114 1112 1112 LEU LEU A . n 
A 1 1115 TYR 1115 1113 1113 TYR TYR A . n 
A 1 1116 HIS 1116 1114 1114 HIS HIS A . n 
A 1 1117 GLN 1117 1115 1115 GLN GLN A . n 
A 1 1118 LEU 1118 1116 1116 LEU LEU A . n 
A 1 1119 ALA 1119 1117 1117 ALA ALA A . n 
A 1 1120 ALA 1120 1118 1118 ALA ALA A . n 
A 1 1121 ALA 1121 1119 1119 ALA ALA A . n 
A 1 1122 LEU 1122 1120 1120 LEU LEU A . n 
A 1 1123 ALA 1123 1121 1121 ALA ALA A . n 
A 1 1124 THR 1124 1122 1122 THR THR A . n 
A 1 1125 GLY 1125 1123 1123 GLY GLY A . n 
A 1 1126 ASN 1126 1124 1124 ASN ASN A . n 
A 1 1127 SER 1127 1125 1125 SER SER A . n 
A 1 1128 VAL 1128 1126 1126 VAL VAL A . n 
A 1 1129 ALA 1129 1127 1127 ALA ALA A . n 
A 1 1130 ILE 1130 1128 1128 ILE ILE A . n 
A 1 1131 ASP 1131 1129 1129 ASP ASP A . n 
A 1 1132 ALA 1132 1130 1130 ALA ALA A . n 
A 1 1133 ALA 1133 1131 1131 ALA ALA A . n 
A 1 1134 SER 1134 1132 1132 SER SER A . n 
A 1 1135 GLY 1135 1133 1133 GLY GLY A . n 
A 1 1136 LEU 1136 1134 1134 LEU LEU A . n 
A 1 1137 GLN 1137 1135 1135 GLN GLN A . n 
A 1 1138 ALA 1138 1136 1136 ALA ALA A . n 
A 1 1139 SER 1139 1137 1137 SER SER A . n 
A 1 1140 LEU 1140 1138 1138 LEU LEU A . n 
A 1 1141 LYS 1141 1139 1139 LYS LYS A . n 
A 1 1142 ASN 1142 1140 1140 ASN ASN A . n 
A 1 1143 LEU 1143 1141 1141 LEU LEU A . n 
A 1 1144 PRO 1144 1142 1142 PRO PRO A . n 
A 1 1145 GLN 1145 1143 1143 GLN GLN A . n 
A 1 1146 THR 1146 1144 1144 THR THR A . n 
A 1 1147 VAL 1147 1145 1145 VAL VAL A . n 
A 1 1148 GLY 1148 1146 1146 GLY GLY A . n 
A 1 1149 LEU 1149 1147 1147 LEU LEU A . n 
A 1 1150 ARG 1150 1148 1148 ARG ARG A . n 
A 1 1151 VAL 1151 1149 1149 VAL VAL A . n 
A 1 1152 SER 1152 1150 1150 SER SER A . n 
A 1 1153 TRP 1153 1151 1151 TRP TRP A . n 
A 1 1154 SER 1154 1152 1152 SER SER A . n 
A 1 1155 LYS 1155 1153 1153 LYS LYS A . n 
A 1 1156 ASP 1156 1154 1154 ASP ASP A . n 
A 1 1157 TRP 1157 1155 1155 TRP TRP A . n 
A 1 1158 ALA 1158 1156 1156 ALA ALA A . n 
A 1 1159 ALA 1159 1157 1157 ALA ALA A . n 
A 1 1160 ASP 1160 1158 1158 ASP ASP A . n 
A 1 1161 GLY 1161 1159 1159 GLY GLY A . n 
A 1 1162 PRO 1162 1160 1160 PRO PRO A . n 
A 1 1163 PHE 1163 1161 1161 PHE PHE A . n 
A 1 1164 ALA 1164 1162 1162 ALA ALA A . n 
A 1 1165 GLY 1165 1163 1163 GLY GLY A . n 
A 1 1166 ALA 1166 1164 1164 ALA ALA A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 VAL 1168 1166 1166 VAL VAL A . n 
A 1 1169 GLU 1169 1167 1167 GLU GLU A . n 
A 1 1170 GLY 1170 1168 1168 GLY GLY A . n 
A 1 1171 ASP 1171 1169 1169 ASP ASP A . n 
A 1 1172 ALA 1172 1170 1170 ALA ALA A . n 
A 1 1173 GLU 1173 1171 1171 GLU GLU A . n 
A 1 1174 ARG 1174 1172 1172 ARG ARG A . n 
A 1 1175 ILE 1175 1173 1173 ILE ILE A . n 
A 1 1176 ARG 1176 1174 1174 ARG ARG A . n 
A 1 1177 ALA 1177 1175 1175 ALA ALA A . n 
A 1 1178 VAL 1178 1176 1176 VAL VAL A . n 
A 1 1179 ASN 1179 1177 1177 ASN ASN A . n 
A 1 1180 LYS 1180 1178 1178 LYS LYS A . n 
A 1 1181 ALA 1181 1179 1179 ALA ALA A . n 
A 1 1182 ILE 1182 1180 1180 ILE ILE A . n 
A 1 1183 ALA 1183 1181 1181 ALA ALA A . n 
A 1 1184 ALA 1184 1182 1182 ALA ALA A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 PRO 1186 1184 1184 PRO PRO A . n 
A 1 1187 GLY 1187 1185 1185 GLY GLY A . n 
A 1 1188 PRO 1188 1186 1186 PRO PRO A . n 
A 1 1189 LEU 1189 1187 1187 LEU LEU A . n 
A 1 1190 LEU 1190 1188 1188 LEU LEU A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 VAL 1192 1190 1190 VAL VAL A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 ALA 1194 1192 1192 ALA ALA A . n 
A 1 1195 ALA 1195 1193 1193 ALA ALA A . n 
A 1 1196 SER 1196 1194 1194 SER SER A . n 
A 1 1197 SER 1197 1195 1195 SER SER A . n 
A 1 1198 GLY 1198 1196 1196 GLY GLY A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 ILE 1200 1198 1198 ILE ILE A . n 
A 1 1201 ALA 1201 1199 1199 ALA ALA A . n 
A 1 1202 ARG 1202 1200 1200 ARG ARG A . n 
A 1 1203 ASN 1203 1201 1201 ASN ASN A . n 
A 1 1204 PRO 1204 1202 1202 PRO PRO A . n 
A 1 1205 ASP 1205 1203 1203 ASP ASP A . n 
A 1 1206 ALA 1206 1204 1204 ALA ALA A . n 
A 1 1207 TYR 1207 1205 1205 TYR TYR A . n 
A 1 1208 CYS 1208 1206 1206 CYS CYS A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 ASN 1210 1208 1208 ASN ASN A . n 
A 1 1211 TRP 1211 1209 1209 TRP TRP A . n 
A 1 1212 LEU 1212 1210 1210 LEU LEU A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 GLU 1214 1212 1212 GLU GLU A . n 
A 1 1215 GLU 1215 1213 1213 GLU GLU A . n 
A 1 1216 VAL 1216 1214 1214 VAL VAL A . n 
A 1 1217 SER 1217 1215 1215 SER SER A . n 
A 1 1218 ALA 1218 1216 1216 ALA ALA A . n 
A 1 1219 SER 1219 1217 1217 SER SER A . n 
A 1 1220 ILE 1220 1218 1218 ILE ILE A . n 
A 1 1221 ASN 1221 1219 1219 ASN ASN A . n 
A 1 1222 THR 1222 1220 1220 THR THR A . n 
A 1 1223 ALA 1223 1221 1221 ALA ALA A . n 
A 1 1224 ALA 1224 1222 1222 ALA ALA A . n 
A 1 1225 ALA 1225 1223 1223 ALA ALA A . n 
A 1 1226 GLY 1226 1224 1224 GLY GLY A . n 
A 1 1227 GLY 1227 1225 1225 GLY GLY A . n 
A 1 1228 ASN 1228 1226 1226 ASN ASN A . n 
A 1 1229 ALA 1229 1227 1227 ALA ALA A . n 
A 1 1230 SER 1230 1228 1228 SER SER A . n 
A 1 1231 LEU 1231 1229 1229 LEU LEU A . n 
A 1 1232 MET 1232 1230 1230 MET MET A . n 
A 1 1233 ALA 1233 1231 1231 ALA ALA A . n 
A 1 1234 ILE 1234 1232 1232 ILE ILE A . n 
A 1 1235 GLY 1235 1233 1233 GLY GLY 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  ?    ?   ?   B . n 
B 1 496  GLY 496  494  ?    ?   ?   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  ?    ?   ?   B . n 
B 1 916  LEU 916  914  ?    ?   ?   B . n 
B 1 917  ALA 917  915  ?    ?   ?   B . n 
B 1 918  SER 918  916  ?    ?   ?   B . n 
B 1 919  GLU 919  917  917  GLU GLU B . n 
B 1 920  THR 920  918  918  THR THR B . n 
B 1 921  GLY 921  919  919  GLY GLY B . n 
B 1 922  VAL 922  920  920  VAL VAL B . n 
B 1 923  GLY 923  921  921  GLY GLY B . n 
B 1 924  THR 924  922  922  THR THR B . n 
B 1 925  PHE 925  923  923  PHE PHE B . n 
B 1 926  VAL 926  924  924  VAL VAL B . n 
B 1 927  PRO 927  925  925  PRO PRO B . n 
B 1 928  PRO 928  926  926  PRO PRO B . n 
B 1 929  THR 929  927  927  THR THR B . n 
B 1 930  ILE 930  928  928  ILE ILE B . n 
B 1 931  ILE 931  929  929  ILE ILE B . n 
B 1 932  GLU 932  930  930  GLU GLU B . n 
B 1 933  LEU 933  931  931  LEU LEU B . n 
B 1 934  GLU 934  932  932  GLU GLU B . n 
B 1 935  LYS 935  933  933  LYS LYS B . n 
B 1 936  LEU 936  934  934  LEU LEU B . n 
B 1 937  SER 937  935  935  SER SER B . n 
B 1 938  ASP 938  936  936  ASP ASP B . n 
B 1 939  LEU 939  937  937  LEU LEU B . n 
B 1 940  GLN 940  938  938  GLN GLN B . n 
B 1 941  ARG 941  939  939  ARG ARG B . n 
B 1 942  GLU 942  940  940  GLU GLU B . n 
B 1 943  VAL 943  941  941  VAL VAL B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  GLY 945  943  943  GLY GLY B . n 
B 1 946  PRO 946  944  944  PRO PRO B . n 
B 1 947  VAL 947  945  945  VAL VAL B . n 
B 1 948  LEU 948  946  946  LEU LEU B . n 
B 1 949  HIS 949  947  947  HIS HIS B . n 
B 1 950  VAL 950  948  948  VAL VAL B . n 
B 1 951  ILE 951  949  949  ILE ILE B . n 
B 1 952  ARG 952  950  950  ARG ARG B . n 
B 1 953  TYR 953  951  951  TYR TYR B . n 
B 1 954  ARG 954  952  952  ARG ARG B . n 
B 1 955  ARG 955  953  953  ARG ARG B . n 
B 1 956  ASP 956  954  954  ASP ASP B . n 
B 1 957  ASP 957  955  955  ASP ASP B . n 
B 1 958  LEU 958  956  956  LEU LEU B . n 
B 1 959  ASP 959  957  957  ASP ASP B . n 
B 1 960  ARG 960  958  958  ARG ARG B . n 
B 1 961  LEU 961  959  959  LEU LEU B . n 
B 1 962  VAL 962  960  960  VAL VAL B . n 
B 1 963  ASP 963  961  961  ASP ASP B . n 
B 1 964  ASP 964  962  962  ASP ASP B . n 
B 1 965  VAL 965  963  963  VAL VAL B . n 
B 1 966  ASN 966  964  964  ASN ASN B . n 
B 1 967  ALA 967  965  965  ALA ALA B . n 
B 1 968  THR 968  966  966  THR THR B . n 
B 1 969  GLY 969  967  967  GLY GLY B . n 
B 1 970  TYR 970  968  968  TYR TYR B . n 
B 1 971  GLY 971  969  969  GLY GLY B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  THR 973  971  971  THR THR B . n 
B 1 974  PHE 974  972  972  PHE PHE B . n 
B 1 975  GLY 975  973  973  GLY GLY B . n 
B 1 976  LEU 976  974  974  LEU LEU B . n 
B 1 977  HIS 977  975  975  HIS HIS B . n 
B 1 978  THR 978  976  976  THR THR B . n 
B 1 979  ARG 979  977  977  ARG ARG B . n 
B 1 980  LEU 980  978  978  LEU LEU B . n 
B 1 981  ASP 981  979  979  ASP ASP B . n 
B 1 982  GLU 982  980  980  GLU GLU B . n 
B 1 983  THR 983  981  981  THR THR B . n 
B 1 984  ILE 984  982  982  ILE ILE B . n 
B 1 985  ALA 985  983  983  ALA ALA B . n 
B 1 986  HIS 986  984  984  HIS HIS B . n 
B 1 987  VAL 987  985  985  VAL VAL B . n 
B 1 988  THR 988  986  986  THR THR B . n 
B 1 989  SER 989  987  987  SER SER B . n 
B 1 990  ARG 990  988  988  ARG ARG B . n 
B 1 991  ILE 991  989  989  ILE ILE B . n 
B 1 992  LYS 992  990  990  LYS LYS B . n 
B 1 993  ALA 993  991  991  ALA ALA B . n 
B 1 994  GLY 994  992  992  GLY GLY B . n 
B 1 995  ASN 995  993  993  ASN ASN B . n 
B 1 996  LEU 996  994  994  LEU LEU B . n 
B 1 997  TYR 997  995  995  TYR TYR B . n 
B 1 998  ILE 998  996  996  ILE ILE B . n 
B 1 999  ASN 999  997  997  ASN ASN B . n 
B 1 1000 ARG 1000 998  998  ARG ARG B . n 
B 1 1001 ASN 1001 999  999  ASN ASN B . n 
B 1 1002 ILE 1002 1000 1000 ILE ILE B . n 
B 1 1003 ILE 1003 1001 1001 ILE ILE B . n 
B 1 1004 GLY 1004 1002 1002 GLY GLY B . n 
B 1 1005 ALA 1005 1003 1003 ALA ALA B . n 
B 1 1006 VAL 1006 1004 1004 VAL VAL B . n 
B 1 1007 VAL 1007 1005 1005 VAL VAL B . n 
B 1 1008 GLY 1008 1006 1006 GLY GLY B . n 
B 1 1009 VAL 1009 1007 1007 VAL VAL B . n 
B 1 1010 GLN 1010 1008 1008 GLN GLN B . n 
B 1 1011 PRO 1011 1009 1009 PRO PRO B . n 
B 1 1012 PHE 1012 1010 1010 PHE PHE B . n 
B 1 1013 GLY 1013 1011 1011 GLY GLY B . n 
B 1 1014 GLY 1014 1012 1012 GLY GLY B . n 
B 1 1015 ARG 1015 1013 1013 ARG ARG B . n 
B 1 1016 GLY 1016 1014 1014 GLY GLY B . n 
B 1 1017 LEU 1017 1015 1015 LEU LEU B . n 
B 1 1018 SER 1018 1016 1016 SER SER B . n 
B 1 1019 GLY 1019 1017 1017 GLY GLY B . n 
B 1 1020 THR 1020 1018 1018 THR THR B . n 
B 1 1021 GLY 1021 1019 1019 GLY GLY B . n 
B 1 1022 PRO 1022 1020 1020 PRO PRO B . n 
B 1 1023 LYS 1023 1021 1021 LYS LYS B . n 
B 1 1024 ALA 1024 1022 1022 ALA ALA B . n 
B 1 1025 GLY 1025 1023 1023 GLY GLY B . n 
B 1 1026 GLY 1026 1024 1024 GLY GLY B . n 
B 1 1027 PRO 1027 1025 1025 PRO PRO B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 TYR 1029 1027 1027 TYR TYR B . n 
B 1 1030 LEU 1030 1028 1028 LEU LEU B . n 
B 1 1031 GLY 1031 1029 1029 GLY GLY B . n 
B 1 1032 ARG 1032 1030 1030 ARG ARG B . n 
B 1 1033 LEU 1033 1031 1031 LEU LEU B . n 
B 1 1034 VAL 1034 1032 1032 VAL VAL B . n 
B 1 1035 THR 1035 1033 1033 THR THR B . n 
B 1 1036 THR 1036 1034 1034 THR THR B . n 
B 1 1037 ALA 1037 1035 1035 ALA ALA B . n 
B 1 1038 PRO 1038 1036 1036 PRO PRO B . n 
B 1 1039 VAL 1039 1037 1037 VAL VAL B . n 
B 1 1040 PRO 1040 1038 1038 PRO PRO B . n 
B 1 1041 PRO 1041 1039 1039 PRO PRO B . n 
B 1 1042 GLN 1042 1040 1040 GLN GLN B . n 
B 1 1043 HIS 1043 1041 1041 HIS HIS B . n 
B 1 1044 SER 1044 1042 1042 SER SER B . n 
B 1 1045 SER 1045 1043 1043 SER SER B . n 
B 1 1046 VAL 1046 1044 1044 VAL VAL B . n 
B 1 1047 HIS 1047 1045 1045 HIS HIS B . n 
B 1 1048 THR 1048 1046 1046 THR THR B . n 
B 1 1049 ASP 1049 1047 1047 ASP ASP B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 VAL 1051 1049 1049 VAL VAL B . n 
B 1 1052 LEU 1052 1050 1050 LEU LEU B . n 
B 1 1053 LEU 1053 1051 1051 LEU LEU B . n 
B 1 1054 ASP 1054 1052 1052 ASP ASP B . n 
B 1 1055 PHE 1055 1053 1053 PHE PHE B . n 
B 1 1056 ALA 1056 1054 1054 ALA ALA B . n 
B 1 1057 LYS 1057 1055 1055 LYS LYS B . n 
B 1 1058 TRP 1058 1056 1056 TRP TRP B . n 
B 1 1059 LEU 1059 1057 1057 LEU LEU B . n 
B 1 1060 ASP 1060 1058 1058 ASP ASP B . n 
B 1 1061 GLY 1061 1059 1059 GLY GLY B . n 
B 1 1062 LYS 1062 1060 1060 LYS LYS B . n 
B 1 1063 GLY 1063 1061 1061 GLY GLY B . n 
B 1 1064 ALA 1064 1062 1062 ALA ALA B . n 
B 1 1065 ARG 1065 1063 1063 ARG ARG B . n 
B 1 1066 ALA 1066 1064 1064 ALA ALA B . n 
B 1 1067 GLU 1067 1065 1065 GLU GLU B . n 
B 1 1068 ALA 1068 1066 1066 ALA ALA B . n 
B 1 1069 GLU 1069 1067 1067 GLU GLU B . n 
B 1 1070 ALA 1070 1068 1068 ALA ALA B . n 
B 1 1071 ALA 1071 1069 1069 ALA ALA B . n 
B 1 1072 ARG 1072 1070 1070 ARG ARG B . n 
B 1 1073 ASN 1073 1071 1071 ASN ASN B . n 
B 1 1074 ALA 1074 1072 1072 ALA ALA B . n 
B 1 1075 GLY 1075 1073 1073 GLY GLY B . n 
B 1 1076 SER 1076 1074 1074 SER SER B . n 
B 1 1077 SER 1077 1075 1075 SER SER B . n 
B 1 1078 SER 1078 1076 1076 SER SER B . n 
B 1 1079 ALA 1079 1077 1077 ALA ALA B . n 
B 1 1080 LEU 1080 1078 1078 LEU LEU B . n 
B 1 1081 GLY 1081 1079 1079 GLY GLY B . n 
B 1 1082 LEU 1082 1080 1080 LEU LEU B . n 
B 1 1083 ASP 1083 1081 1081 ASP ASP B . n 
B 1 1084 LEU 1084 1082 1082 LEU LEU B . n 
B 1 1085 GLU 1085 1083 1083 GLU GLU B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 PRO 1087 1085 1085 PRO PRO B . n 
B 1 1088 GLY 1088 1086 1086 GLY GLY B . n 
B 1 1089 PRO 1089 1087 1087 PRO PRO B . n 
B 1 1090 VAL 1090 1088 1088 VAL VAL B . n 
B 1 1091 GLY 1091 1089 1089 GLY GLY B . n 
B 1 1092 GLU 1092 1090 1090 GLU GLU B . n 
B 1 1093 ARG 1093 1091 1091 ARG ARG B . n 
B 1 1094 ASN 1094 1092 1092 ASN ASN B . n 
B 1 1095 LEU 1095 1093 1093 LEU LEU B . n 
B 1 1096 TYR 1096 1094 1094 TYR TYR B . n 
B 1 1097 THR 1097 1095 1095 THR THR B . n 
B 1 1098 LEU 1098 1096 1096 LEU LEU B . n 
B 1 1099 HIS 1099 1097 1097 HIS HIS B . n 
B 1 1100 ALA 1100 1098 1098 ALA ALA B . n 
B 1 1101 ARG 1101 1099 1099 ARG ARG B . n 
B 1 1102 GLY 1102 1100 1100 GLY GLY B . n 
B 1 1103 ARG 1103 1101 1101 ARG ARG B . n 
B 1 1104 ILE 1104 1102 1102 ILE ILE B . n 
B 1 1105 LEU 1105 1103 1103 LEU LEU B . n 
B 1 1106 LEU 1106 1104 1104 LEU LEU B . n 
B 1 1107 VAL 1107 1105 1105 VAL VAL B . n 
B 1 1108 PRO 1108 1106 1106 PRO PRO B . n 
B 1 1109 ALA 1109 1107 1107 ALA ALA B . n 
B 1 1110 THR 1110 1108 1108 THR THR B . n 
B 1 1111 GLU 1111 1109 1109 GLU GLU B . n 
B 1 1112 SER 1112 1110 1110 SER SER B . n 
B 1 1113 GLY 1113 1111 1111 GLY GLY B . n 
B 1 1114 LEU 1114 1112 1112 LEU LEU B . n 
B 1 1115 TYR 1115 1113 1113 TYR TYR B . n 
B 1 1116 HIS 1116 1114 1114 HIS HIS B . n 
B 1 1117 GLN 1117 1115 1115 GLN GLN B . n 
B 1 1118 LEU 1118 1116 1116 LEU LEU B . n 
B 1 1119 ALA 1119 1117 1117 ALA ALA B . n 
B 1 1120 ALA 1120 1118 1118 ALA ALA B . n 
B 1 1121 ALA 1121 1119 1119 ALA ALA B . n 
B 1 1122 LEU 1122 1120 1120 LEU LEU B . n 
B 1 1123 ALA 1123 1121 1121 ALA ALA B . n 
B 1 1124 THR 1124 1122 1122 THR THR B . n 
B 1 1125 GLY 1125 1123 1123 GLY GLY B . n 
B 1 1126 ASN 1126 1124 1124 ASN ASN B . n 
B 1 1127 SER 1127 1125 1125 SER SER B . n 
B 1 1128 VAL 1128 1126 1126 VAL VAL B . n 
B 1 1129 ALA 1129 1127 1127 ALA ALA B . n 
B 1 1130 ILE 1130 1128 1128 ILE ILE B . n 
B 1 1131 ASP 1131 1129 1129 ASP ASP B . n 
B 1 1132 ALA 1132 1130 1130 ALA ALA B . n 
B 1 1133 ALA 1133 1131 1131 ALA ALA B . n 
B 1 1134 SER 1134 1132 1132 SER SER B . n 
B 1 1135 GLY 1135 1133 1133 GLY GLY B . n 
B 1 1136 LEU 1136 1134 1134 LEU LEU B . n 
B 1 1137 GLN 1137 1135 1135 GLN GLN B . n 
B 1 1138 ALA 1138 1136 1136 ALA ALA B . n 
B 1 1139 SER 1139 1137 1137 SER SER B . n 
B 1 1140 LEU 1140 1138 1138 LEU LEU B . n 
B 1 1141 LYS 1141 1139 1139 LYS LYS B . n 
B 1 1142 ASN 1142 1140 1140 ASN ASN B . n 
B 1 1143 LEU 1143 1141 1141 LEU LEU B . n 
B 1 1144 PRO 1144 1142 1142 PRO PRO B . n 
B 1 1145 GLN 1145 1143 1143 GLN GLN B . n 
B 1 1146 THR 1146 1144 1144 THR THR B . n 
B 1 1147 VAL 1147 1145 1145 VAL VAL B . n 
B 1 1148 GLY 1148 1146 1146 GLY GLY B . n 
B 1 1149 LEU 1149 1147 1147 LEU LEU B . n 
B 1 1150 ARG 1150 1148 1148 ARG ARG B . n 
B 1 1151 VAL 1151 1149 1149 VAL VAL B . n 
B 1 1152 SER 1152 1150 1150 SER SER B . n 
B 1 1153 TRP 1153 1151 1151 TRP TRP B . n 
B 1 1154 SER 1154 1152 1152 SER SER B . n 
B 1 1155 LYS 1155 1153 1153 LYS LYS B . n 
B 1 1156 ASP 1156 1154 1154 ASP ASP B . n 
B 1 1157 TRP 1157 1155 1155 TRP TRP B . n 
B 1 1158 ALA 1158 1156 1156 ALA ALA B . n 
B 1 1159 ALA 1159 1157 1157 ALA ALA B . n 
B 1 1160 ASP 1160 1158 1158 ASP ASP B . n 
B 1 1161 GLY 1161 1159 1159 GLY GLY B . n 
B 1 1162 PRO 1162 1160 1160 PRO PRO B . n 
B 1 1163 PHE 1163 1161 1161 PHE PHE B . n 
B 1 1164 ALA 1164 1162 1162 ALA ALA B . n 
B 1 1165 GLY 1165 1163 1163 GLY GLY B . n 
B 1 1166 ALA 1166 1164 1164 ALA ALA B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 VAL 1168 1166 1166 VAL VAL B . n 
B 1 1169 GLU 1169 1167 1167 GLU GLU B . n 
B 1 1170 GLY 1170 1168 1168 GLY GLY B . n 
B 1 1171 ASP 1171 1169 1169 ASP ASP B . n 
B 1 1172 ALA 1172 1170 1170 ALA ALA B . n 
B 1 1173 GLU 1173 1171 1171 GLU GLU B . n 
B 1 1174 ARG 1174 1172 1172 ARG ARG B . n 
B 1 1175 ILE 1175 1173 1173 ILE ILE B . n 
B 1 1176 ARG 1176 1174 1174 ARG ARG B . n 
B 1 1177 ALA 1177 1175 1175 ALA ALA B . n 
B 1 1178 VAL 1178 1176 1176 VAL VAL B . n 
B 1 1179 ASN 1179 1177 1177 ASN ASN B . n 
B 1 1180 LYS 1180 1178 1178 LYS LYS B . n 
B 1 1181 ALA 1181 1179 1179 ALA ALA B . n 
B 1 1182 ILE 1182 1180 1180 ILE ILE B . n 
B 1 1183 ALA 1183 1181 1181 ALA ALA B . n 
B 1 1184 ALA 1184 1182 1182 ALA ALA B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 PRO 1186 1184 1184 PRO PRO B . n 
B 1 1187 GLY 1187 1185 1185 GLY GLY B . n 
B 1 1188 PRO 1188 1186 1186 PRO PRO B . n 
B 1 1189 LEU 1189 1187 1187 LEU LEU B . n 
B 1 1190 LEU 1190 1188 1188 LEU LEU B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 VAL 1192 1190 1190 VAL VAL B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 ALA 1194 1192 1192 ALA ALA B . n 
B 1 1195 ALA 1195 1193 1193 ALA ALA B . n 
B 1 1196 SER 1196 1194 1194 SER SER B . n 
B 1 1197 SER 1197 1195 1195 SER SER B . n 
B 1 1198 GLY 1198 1196 1196 GLY GLY B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 ILE 1200 1198 1198 ILE ILE B . n 
B 1 1201 ALA 1201 1199 1199 ALA ALA B . n 
B 1 1202 ARG 1202 1200 1200 ARG ARG B . n 
B 1 1203 ASN 1203 1201 1201 ASN ASN B . n 
B 1 1204 PRO 1204 1202 1202 PRO PRO B . n 
B 1 1205 ASP 1205 1203 1203 ASP ASP B . n 
B 1 1206 ALA 1206 1204 1204 ALA ALA B . n 
B 1 1207 TYR 1207 1205 1205 TYR TYR B . n 
B 1 1208 CYS 1208 1206 1206 CYS CYS B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 ASN 1210 1208 1208 ASN ASN B . n 
B 1 1211 TRP 1211 1209 1209 TRP TRP B . n 
B 1 1212 LEU 1212 1210 1210 LEU LEU B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 GLU 1214 1212 1212 GLU GLU B . n 
B 1 1215 GLU 1215 1213 1213 GLU GLU B . n 
B 1 1216 VAL 1216 1214 1214 VAL VAL B . n 
B 1 1217 SER 1217 1215 1215 SER SER B . n 
B 1 1218 ALA 1218 1216 1216 ALA ALA B . n 
B 1 1219 SER 1219 1217 1217 SER SER B . n 
B 1 1220 ILE 1220 1218 1218 ILE ILE B . n 
B 1 1221 ASN 1221 1219 1219 ASN ASN B . n 
B 1 1222 THR 1222 1220 1220 THR THR B . n 
B 1 1223 ALA 1223 1221 1221 ALA ALA B . n 
B 1 1224 ALA 1224 1222 1222 ALA ALA B . n 
B 1 1225 ALA 1225 1223 1223 ALA ALA B . n 
B 1 1226 GLY 1226 1224 1224 GLY GLY B . n 
B 1 1227 GLY 1227 1225 1225 GLY GLY B . n 
B 1 1228 ASN 1228 1226 1226 ASN ASN B . n 
B 1 1229 ALA 1229 1227 1227 ALA ALA B . n 
B 1 1230 SER 1230 1228 1228 SER SER B . n 
B 1 1231 LEU 1231 1229 1229 LEU LEU B . n 
B 1 1232 MET 1232 1230 1230 MET MET B . n 
B 1 1233 ALA 1233 1231 1231 ALA ALA B . n 
B 1 1234 ILE 1234 1232 1232 ILE ILE B . n 
B 1 1235 GLY 1235 1233 1233 GLY GLY 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 A1BDV ? ? A1BDV ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD   ? ? FAD   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NAD   ? ? NAD   ? ? '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    1301 1301 FAD   FAD A . 
D  3  PGE   1    1302 1302 PGE   PGE A . 
E  4  FMT   1    1303 1303 FMT   FMT A . 
F  4  FMT   1    1304 1304 FMT   FMT A . 
G  5  A1BDV 1    1305 1305 A1BDV 217 A . 
H  6  NAD   1    1306 2002 NAD   NAD A . 
I  7  SO4   1    1307 2    SO4   SO4 A . 
J  7  SO4   1    1308 3    SO4   SO4 A . 
K  7  SO4   1    1309 4    SO4   SO4 A . 
L  7  SO4   1    1310 5    SO4   SO4 A . 
M  7  SO4   1    1311 6    SO4   SO4 A . 
N  8  MG    1    1312 1    MG    MG  A . 
O  2  FAD   1    1301 1301 FAD   FAD B . 
P  4  FMT   1    1302 1302 FMT   FMT B . 
Q  3  PGE   1    1303 1303 PGE   PGE B . 
R  9  1PE   1    1304 1304 1PE   1PE B . 
S  10 PEG   1    1305 1305 PEG   PEG B . 
T  4  FMT   1    1306 1306 FMT   FMT B . 
U  5  A1BDV 1    1307 1307 A1BDV 217 B . 
V  6  NAD   1    1308 2002 NAD   NAD B . 
W  7  SO4   1    1309 1    SO4   SO4 B . 
X  8  MG    1    1310 2    MG    MG  B . 
Y  10 PEG   1    1311 1977 PEG   PEG B . 
Z  11 HOH   1    1401 2056 HOH   HOH A . 
Z  11 HOH   2    1402 2007 HOH   HOH A . 
Z  11 HOH   3    1403 2061 HOH   HOH A . 
Z  11 HOH   4    1404 1553 HOH   HOH A . 
Z  11 HOH   5    1405 127  HOH   HOH A . 
Z  11 HOH   6    1406 1975 HOH   HOH A . 
Z  11 HOH   7    1407 2224 HOH   HOH A . 
Z  11 HOH   8    1408 589  HOH   HOH A . 
Z  11 HOH   9    1409 2263 HOH   HOH A . 
Z  11 HOH   10   1410 2377 HOH   HOH A . 
Z  11 HOH   11   1411 734  HOH   HOH A . 
Z  11 HOH   12   1412 732  HOH   HOH A . 
Z  11 HOH   13   1413 2000 HOH   HOH A . 
Z  11 HOH   14   1414 1543 HOH   HOH A . 
Z  11 HOH   15   1415 1440 HOH   HOH A . 
Z  11 HOH   16   1416 1865 HOH   HOH A . 
Z  11 HOH   17   1417 1256 HOH   HOH A . 
Z  11 HOH   18   1418 1461 HOH   HOH A . 
Z  11 HOH   19   1419 2079 HOH   HOH A . 
Z  11 HOH   20   1420 1090 HOH   HOH A . 
Z  11 HOH   21   1421 539  HOH   HOH A . 
Z  11 HOH   22   1422 530  HOH   HOH A . 
Z  11 HOH   23   1423 2091 HOH   HOH A . 
Z  11 HOH   24   1424 714  HOH   HOH A . 
Z  11 HOH   25   1425 1635 HOH   HOH A . 
Z  11 HOH   26   1426 1838 HOH   HOH A . 
Z  11 HOH   27   1427 1582 HOH   HOH A . 
Z  11 HOH   28   1428 169  HOH   HOH A . 
Z  11 HOH   29   1429 756  HOH   HOH A . 
Z  11 HOH   30   1430 2242 HOH   HOH A . 
Z  11 HOH   31   1431 2260 HOH   HOH A . 
Z  11 HOH   32   1432 2292 HOH   HOH A . 
Z  11 HOH   33   1433 1579 HOH   HOH A . 
Z  11 HOH   34   1434 1799 HOH   HOH A . 
Z  11 HOH   35   1435 1616 HOH   HOH A . 
Z  11 HOH   36   1436 1610 HOH   HOH A . 
Z  11 HOH   37   1437 807  HOH   HOH A . 
Z  11 HOH   38   1438 1433 HOH   HOH A . 
Z  11 HOH   39   1439 2393 HOH   HOH A . 
Z  11 HOH   40   1440 1263 HOH   HOH A . 
Z  11 HOH   41   1441 1272 HOH   HOH A . 
Z  11 HOH   42   1442 2113 HOH   HOH A . 
Z  11 HOH   43   1443 1946 HOH   HOH A . 
Z  11 HOH   44   1444 2404 HOH   HOH A . 
Z  11 HOH   45   1445 302  HOH   HOH A . 
Z  11 HOH   46   1446 965  HOH   HOH A . 
Z  11 HOH   47   1447 1571 HOH   HOH A . 
Z  11 HOH   48   1448 1905 HOH   HOH A . 
Z  11 HOH   49   1449 1453 HOH   HOH A . 
Z  11 HOH   50   1450 1331 HOH   HOH A . 
Z  11 HOH   51   1451 1674 HOH   HOH A . 
Z  11 HOH   52   1452 948  HOH   HOH A . 
Z  11 HOH   53   1453 987  HOH   HOH A . 
Z  11 HOH   54   1454 1690 HOH   HOH A . 
Z  11 HOH   55   1455 716  HOH   HOH A . 
Z  11 HOH   56   1456 1777 HOH   HOH A . 
Z  11 HOH   57   1457 2232 HOH   HOH A . 
Z  11 HOH   58   1458 2432 HOH   HOH A . 
Z  11 HOH   59   1459 1289 HOH   HOH A . 
Z  11 HOH   60   1460 1599 HOH   HOH A . 
Z  11 HOH   61   1461 407  HOH   HOH A . 
Z  11 HOH   62   1462 1926 HOH   HOH A . 
Z  11 HOH   63   1463 2309 HOH   HOH A . 
Z  11 HOH   64   1464 1743 HOH   HOH A . 
Z  11 HOH   65   1465 1159 HOH   HOH A . 
Z  11 HOH   66   1466 2011 HOH   HOH A . 
Z  11 HOH   67   1467 1619 HOH   HOH A . 
Z  11 HOH   68   1468 227  HOH   HOH A . 
Z  11 HOH   69   1469 2062 HOH   HOH A . 
Z  11 HOH   70   1470 2054 HOH   HOH A . 
Z  11 HOH   71   1471 1115 HOH   HOH A . 
Z  11 HOH   72   1472 531  HOH   HOH A . 
Z  11 HOH   73   1473 29   HOH   HOH A . 
Z  11 HOH   74   1474 972  HOH   HOH A . 
Z  11 HOH   75   1475 2207 HOH   HOH A . 
Z  11 HOH   76   1476 2192 HOH   HOH A . 
Z  11 HOH   77   1477 623  HOH   HOH A . 
Z  11 HOH   78   1478 680  HOH   HOH A . 
Z  11 HOH   79   1479 1397 HOH   HOH A . 
Z  11 HOH   80   1480 2332 HOH   HOH A . 
Z  11 HOH   81   1481 1195 HOH   HOH A . 
Z  11 HOH   82   1482 356  HOH   HOH A . 
Z  11 HOH   83   1483 2055 HOH   HOH A . 
Z  11 HOH   84   1484 836  HOH   HOH A . 
Z  11 HOH   85   1485 1715 HOH   HOH A . 
Z  11 HOH   86   1486 2350 HOH   HOH A . 
Z  11 HOH   87   1487 654  HOH   HOH A . 
Z  11 HOH   88   1488 737  HOH   HOH A . 
Z  11 HOH   89   1489 280  HOH   HOH A . 
Z  11 HOH   90   1490 2036 HOH   HOH A . 
Z  11 HOH   91   1491 2001 HOH   HOH A . 
Z  11 HOH   92   1492 1333 HOH   HOH A . 
Z  11 HOH   93   1493 1859 HOH   HOH A . 
Z  11 HOH   94   1494 749  HOH   HOH A . 
Z  11 HOH   95   1495 1077 HOH   HOH A . 
Z  11 HOH   96   1496 1974 HOH   HOH A . 
Z  11 HOH   97   1497 831  HOH   HOH A . 
Z  11 HOH   98   1498 2129 HOH   HOH A . 
Z  11 HOH   99   1499 1056 HOH   HOH A . 
Z  11 HOH   100  1500 1717 HOH   HOH A . 
Z  11 HOH   101  1501 1305 HOH   HOH A . 
Z  11 HOH   102  1502 147  HOH   HOH A . 
Z  11 HOH   103  1503 2100 HOH   HOH A . 
Z  11 HOH   104  1504 1163 HOH   HOH A . 
Z  11 HOH   105  1505 87   HOH   HOH A . 
Z  11 HOH   106  1506 524  HOH   HOH A . 
Z  11 HOH   107  1507 201  HOH   HOH A . 
Z  11 HOH   108  1508 581  HOH   HOH A . 
Z  11 HOH   109  1509 226  HOH   HOH A . 
Z  11 HOH   110  1510 2342 HOH   HOH A . 
Z  11 HOH   111  1511 544  HOH   HOH A . 
Z  11 HOH   112  1512 1252 HOH   HOH A . 
Z  11 HOH   113  1513 344  HOH   HOH A . 
Z  11 HOH   114  1514 235  HOH   HOH A . 
Z  11 HOH   115  1515 1388 HOH   HOH A . 
Z  11 HOH   116  1516 1182 HOH   HOH A . 
Z  11 HOH   117  1517 75   HOH   HOH A . 
Z  11 HOH   118  1518 123  HOH   HOH A . 
Z  11 HOH   119  1519 691  HOH   HOH A . 
Z  11 HOH   120  1520 585  HOH   HOH A . 
Z  11 HOH   121  1521 745  HOH   HOH A . 
Z  11 HOH   122  1522 347  HOH   HOH A . 
Z  11 HOH   123  1523 902  HOH   HOH A . 
Z  11 HOH   124  1524 97   HOH   HOH A . 
Z  11 HOH   125  1525 493  HOH   HOH A . 
Z  11 HOH   126  1526 719  HOH   HOH A . 
Z  11 HOH   127  1527 135  HOH   HOH A . 
Z  11 HOH   128  1528 1684 HOH   HOH A . 
Z  11 HOH   129  1529 1698 HOH   HOH A . 
Z  11 HOH   130  1530 1895 HOH   HOH A . 
Z  11 HOH   131  1531 35   HOH   HOH A . 
Z  11 HOH   132  1532 1376 HOH   HOH A . 
Z  11 HOH   133  1533 2218 HOH   HOH A . 
Z  11 HOH   134  1534 191  HOH   HOH A . 
Z  11 HOH   135  1535 55   HOH   HOH A . 
Z  11 HOH   136  1536 2114 HOH   HOH A . 
Z  11 HOH   137  1537 1457 HOH   HOH A . 
Z  11 HOH   138  1538 921  HOH   HOH A . 
Z  11 HOH   139  1539 1450 HOH   HOH A . 
Z  11 HOH   140  1540 2343 HOH   HOH A . 
Z  11 HOH   141  1541 2075 HOH   HOH A . 
Z  11 HOH   142  1542 1484 HOH   HOH A . 
Z  11 HOH   143  1543 952  HOH   HOH A . 
Z  11 HOH   144  1544 823  HOH   HOH A . 
Z  11 HOH   145  1545 1143 HOH   HOH A . 
Z  11 HOH   146  1546 1952 HOH   HOH A . 
Z  11 HOH   147  1547 370  HOH   HOH A . 
Z  11 HOH   148  1548 695  HOH   HOH A . 
Z  11 HOH   149  1549 1105 HOH   HOH A . 
Z  11 HOH   150  1550 457  HOH   HOH A . 
Z  11 HOH   151  1551 2101 HOH   HOH A . 
Z  11 HOH   152  1552 2070 HOH   HOH A . 
Z  11 HOH   153  1553 919  HOH   HOH A . 
Z  11 HOH   154  1554 1567 HOH   HOH A . 
Z  11 HOH   155  1555 982  HOH   HOH A . 
Z  11 HOH   156  1556 1694 HOH   HOH A . 
Z  11 HOH   157  1557 2268 HOH   HOH A . 
Z  11 HOH   158  1558 348  HOH   HOH A . 
Z  11 HOH   159  1559 1320 HOH   HOH A . 
Z  11 HOH   160  1560 2359 HOH   HOH A . 
Z  11 HOH   161  1561 758  HOH   HOH A . 
Z  11 HOH   162  1562 155  HOH   HOH A . 
Z  11 HOH   163  1563 784  HOH   HOH A . 
Z  11 HOH   164  1564 1763 HOH   HOH A . 
Z  11 HOH   165  1565 256  HOH   HOH A . 
Z  11 HOH   166  1566 1364 HOH   HOH A . 
Z  11 HOH   167  1567 360  HOH   HOH A . 
Z  11 HOH   168  1568 502  HOH   HOH A . 
Z  11 HOH   169  1569 20   HOH   HOH A . 
Z  11 HOH   170  1570 970  HOH   HOH A . 
Z  11 HOH   171  1571 136  HOH   HOH A . 
Z  11 HOH   172  1572 41   HOH   HOH A . 
Z  11 HOH   173  1573 1510 HOH   HOH A . 
Z  11 HOH   174  1574 1424 HOH   HOH A . 
Z  11 HOH   175  1575 679  HOH   HOH A . 
Z  11 HOH   176  1576 1330 HOH   HOH A . 
Z  11 HOH   177  1577 78   HOH   HOH A . 
Z  11 HOH   178  1578 2096 HOH   HOH A . 
Z  11 HOH   179  1579 286  HOH   HOH A . 
Z  11 HOH   180  1580 2344 HOH   HOH A . 
Z  11 HOH   181  1581 2065 HOH   HOH A . 
Z  11 HOH   182  1582 499  HOH   HOH A . 
Z  11 HOH   183  1583 1906 HOH   HOH A . 
Z  11 HOH   184  1584 1976 HOH   HOH A . 
Z  11 HOH   185  1585 489  HOH   HOH A . 
Z  11 HOH   186  1586 346  HOH   HOH A . 
Z  11 HOH   187  1587 439  HOH   HOH A . 
Z  11 HOH   188  1588 1170 HOH   HOH A . 
Z  11 HOH   189  1589 449  HOH   HOH A . 
Z  11 HOH   190  1590 107  HOH   HOH A . 
Z  11 HOH   191  1591 2259 HOH   HOH A . 
Z  11 HOH   192  1592 190  HOH   HOH A . 
Z  11 HOH   193  1593 219  HOH   HOH A . 
Z  11 HOH   194  1594 1959 HOH   HOH A . 
Z  11 HOH   195  1595 2431 HOH   HOH A . 
Z  11 HOH   196  1596 2046 HOH   HOH A . 
Z  11 HOH   197  1597 307  HOH   HOH A . 
Z  11 HOH   198  1598 1041 HOH   HOH A . 
Z  11 HOH   199  1599 409  HOH   HOH A . 
Z  11 HOH   200  1600 665  HOH   HOH A . 
Z  11 HOH   201  1601 843  HOH   HOH A . 
Z  11 HOH   202  1602 126  HOH   HOH A . 
Z  11 HOH   203  1603 21   HOH   HOH A . 
Z  11 HOH   204  1604 1370 HOH   HOH A . 
Z  11 HOH   205  1605 853  HOH   HOH A . 
Z  11 HOH   206  1606 938  HOH   HOH A . 
Z  11 HOH   207  1607 214  HOH   HOH A . 
Z  11 HOH   208  1608 2320 HOH   HOH A . 
Z  11 HOH   209  1609 1511 HOH   HOH A . 
Z  11 HOH   210  1610 1206 HOH   HOH A . 
Z  11 HOH   211  1611 1795 HOH   HOH A . 
Z  11 HOH   212  1612 568  HOH   HOH A . 
Z  11 HOH   213  1613 456  HOH   HOH A . 
Z  11 HOH   214  1614 185  HOH   HOH A . 
Z  11 HOH   215  1615 1140 HOH   HOH A . 
Z  11 HOH   216  1616 750  HOH   HOH A . 
Z  11 HOH   217  1617 1850 HOH   HOH A . 
Z  11 HOH   218  1618 971  HOH   HOH A . 
Z  11 HOH   219  1619 2381 HOH   HOH A . 
Z  11 HOH   220  1620 611  HOH   HOH A . 
Z  11 HOH   221  1621 958  HOH   HOH A . 
Z  11 HOH   222  1622 406  HOH   HOH A . 
Z  11 HOH   223  1623 267  HOH   HOH A . 
Z  11 HOH   224  1624 2164 HOH   HOH A . 
Z  11 HOH   225  1625 1133 HOH   HOH A . 
Z  11 HOH   226  1626 1006 HOH   HOH A . 
Z  11 HOH   227  1627 1617 HOH   HOH A . 
Z  11 HOH   228  1628 475  HOH   HOH A . 
Z  11 HOH   229  1629 1079 HOH   HOH A . 
Z  11 HOH   230  1630 2167 HOH   HOH A . 
Z  11 HOH   231  1631 410  HOH   HOH A . 
Z  11 HOH   232  1632 1014 HOH   HOH A . 
Z  11 HOH   233  1633 447  HOH   HOH A . 
Z  11 HOH   234  1634 2085 HOH   HOH A . 
Z  11 HOH   235  1635 582  HOH   HOH A . 
Z  11 HOH   236  1636 569  HOH   HOH A . 
Z  11 HOH   237  1637 2251 HOH   HOH A . 
Z  11 HOH   238  1638 293  HOH   HOH A . 
Z  11 HOH   239  1639 614  HOH   HOH A . 
Z  11 HOH   240  1640 1385 HOH   HOH A . 
Z  11 HOH   241  1641 1787 HOH   HOH A . 
Z  11 HOH   242  1642 199  HOH   HOH A . 
Z  11 HOH   243  1643 600  HOH   HOH A . 
Z  11 HOH   244  1644 1581 HOH   HOH A . 
Z  11 HOH   245  1645 306  HOH   HOH A . 
Z  11 HOH   246  1646 1420 HOH   HOH A . 
Z  11 HOH   247  1647 1733 HOH   HOH A . 
Z  11 HOH   248  1648 104  HOH   HOH A . 
Z  11 HOH   249  1649 1024 HOH   HOH A . 
Z  11 HOH   250  1650 54   HOH   HOH A . 
Z  11 HOH   251  1651 1008 HOH   HOH A . 
Z  11 HOH   252  1652 977  HOH   HOH A . 
Z  11 HOH   253  1653 1064 HOH   HOH A . 
Z  11 HOH   254  1654 84   HOH   HOH A . 
Z  11 HOH   255  1655 132  HOH   HOH A . 
Z  11 HOH   256  1656 795  HOH   HOH A . 
Z  11 HOH   257  1657 818  HOH   HOH A . 
Z  11 HOH   258  1658 1125 HOH   HOH A . 
Z  11 HOH   259  1659 401  HOH   HOH A . 
Z  11 HOH   260  1660 1044 HOH   HOH A . 
Z  11 HOH   261  1661 1954 HOH   HOH A . 
Z  11 HOH   262  1662 533  HOH   HOH A . 
Z  11 HOH   263  1663 395  HOH   HOH A . 
Z  11 HOH   264  1664 31   HOH   HOH A . 
Z  11 HOH   265  1665 683  HOH   HOH A . 
Z  11 HOH   266  1666 124  HOH   HOH A . 
Z  11 HOH   267  1667 742  HOH   HOH A . 
Z  11 HOH   268  1668 868  HOH   HOH A . 
Z  11 HOH   269  1669 156  HOH   HOH A . 
Z  11 HOH   270  1670 1683 HOH   HOH A . 
Z  11 HOH   271  1671 128  HOH   HOH A . 
Z  11 HOH   272  1672 270  HOH   HOH A . 
Z  11 HOH   273  1673 2449 HOH   HOH A . 
Z  11 HOH   274  1674 341  HOH   HOH A . 
Z  11 HOH   275  1675 1435 HOH   HOH A . 
Z  11 HOH   276  1676 343  HOH   HOH A . 
Z  11 HOH   277  1677 424  HOH   HOH A . 
Z  11 HOH   278  1678 891  HOH   HOH A . 
Z  11 HOH   279  1679 805  HOH   HOH A . 
Z  11 HOH   280  1680 563  HOH   HOH A . 
Z  11 HOH   281  1681 594  HOH   HOH A . 
Z  11 HOH   282  1682 534  HOH   HOH A . 
Z  11 HOH   283  1683 740  HOH   HOH A . 
Z  11 HOH   284  1684 1181 HOH   HOH A . 
Z  11 HOH   285  1685 2286 HOH   HOH A . 
Z  11 HOH   286  1686 259  HOH   HOH A . 
Z  11 HOH   287  1687 1606 HOH   HOH A . 
Z  11 HOH   288  1688 783  HOH   HOH A . 
Z  11 HOH   289  1689 1661 HOH   HOH A . 
Z  11 HOH   290  1690 2174 HOH   HOH A . 
Z  11 HOH   291  1691 1074 HOH   HOH A . 
Z  11 HOH   292  1692 709  HOH   HOH A . 
Z  11 HOH   293  1693 1351 HOH   HOH A . 
Z  11 HOH   294  1694 369  HOH   HOH A . 
Z  11 HOH   295  1695 1502 HOH   HOH A . 
Z  11 HOH   296  1696 501  HOH   HOH A . 
Z  11 HOH   297  1697 712  HOH   HOH A . 
Z  11 HOH   298  1698 444  HOH   HOH A . 
Z  11 HOH   299  1699 385  HOH   HOH A . 
Z  11 HOH   300  1700 1620 HOH   HOH A . 
Z  11 HOH   301  1701 781  HOH   HOH A . 
Z  11 HOH   302  1702 40   HOH   HOH A . 
Z  11 HOH   303  1703 362  HOH   HOH A . 
Z  11 HOH   304  1704 1187 HOH   HOH A . 
Z  11 HOH   305  1705 1098 HOH   HOH A . 
Z  11 HOH   306  1706 916  HOH   HOH A . 
Z  11 HOH   307  1707 171  HOH   HOH A . 
Z  11 HOH   308  1708 2219 HOH   HOH A . 
Z  11 HOH   309  1709 269  HOH   HOH A . 
Z  11 HOH   310  1710 1278 HOH   HOH A . 
Z  11 HOH   311  1711 1710 HOH   HOH A . 
Z  11 HOH   312  1712 52   HOH   HOH A . 
Z  11 HOH   313  1713 216  HOH   HOH A . 
Z  11 HOH   314  1714 1508 HOH   HOH A . 
Z  11 HOH   315  1715 1973 HOH   HOH A . 
Z  11 HOH   316  1716 747  HOH   HOH A . 
Z  11 HOH   317  1717 217  HOH   HOH A . 
Z  11 HOH   318  1718 24   HOH   HOH A . 
Z  11 HOH   319  1719 1734 HOH   HOH A . 
Z  11 HOH   320  1720 1604 HOH   HOH A . 
Z  11 HOH   321  1721 560  HOH   HOH A . 
Z  11 HOH   322  1722 1073 HOH   HOH A . 
Z  11 HOH   323  1723 436  HOH   HOH A . 
Z  11 HOH   324  1724 454  HOH   HOH A . 
Z  11 HOH   325  1725 2156 HOH   HOH A . 
Z  11 HOH   326  1726 793  HOH   HOH A . 
Z  11 HOH   327  1727 1860 HOH   HOH A . 
Z  11 HOH   328  1728 617  HOH   HOH A . 
Z  11 HOH   329  1729 1153 HOH   HOH A . 
Z  11 HOH   330  1730 2099 HOH   HOH A . 
Z  11 HOH   331  1731 298  HOH   HOH A . 
Z  11 HOH   332  1732 240  HOH   HOH A . 
Z  11 HOH   333  1733 852  HOH   HOH A . 
Z  11 HOH   334  1734 113  HOH   HOH A . 
Z  11 HOH   335  1735 527  HOH   HOH A . 
Z  11 HOH   336  1736 1770 HOH   HOH A . 
Z  11 HOH   337  1737 976  HOH   HOH A . 
Z  11 HOH   338  1738 258  HOH   HOH A . 
Z  11 HOH   339  1739 1428 HOH   HOH A . 
Z  11 HOH   340  1740 1929 HOH   HOH A . 
Z  11 HOH   341  1741 1288 HOH   HOH A . 
Z  11 HOH   342  1742 804  HOH   HOH A . 
Z  11 HOH   343  1743 241  HOH   HOH A . 
Z  11 HOH   344  1744 646  HOH   HOH A . 
Z  11 HOH   345  1745 1087 HOH   HOH A . 
Z  11 HOH   346  1746 180  HOH   HOH A . 
Z  11 HOH   347  1747 2015 HOH   HOH A . 
Z  11 HOH   348  1748 1650 HOH   HOH A . 
Z  11 HOH   349  1749 857  HOH   HOH A . 
Z  11 HOH   350  1750 1304 HOH   HOH A . 
Z  11 HOH   351  1751 728  HOH   HOH A . 
Z  11 HOH   352  1752 1533 HOH   HOH A . 
Z  11 HOH   353  1753 1092 HOH   HOH A . 
Z  11 HOH   354  1754 923  HOH   HOH A . 
Z  11 HOH   355  1755 2076 HOH   HOH A . 
Z  11 HOH   356  1756 209  HOH   HOH A . 
Z  11 HOH   357  1757 1721 HOH   HOH A . 
Z  11 HOH   358  1758 133  HOH   HOH A . 
Z  11 HOH   359  1759 2185 HOH   HOH A . 
Z  11 HOH   360  1760 1360 HOH   HOH A . 
Z  11 HOH   361  1761 2168 HOH   HOH A . 
Z  11 HOH   362  1762 2457 HOH   HOH A . 
Z  11 HOH   363  1763 1116 HOH   HOH A . 
Z  11 HOH   364  1764 466  HOH   HOH A . 
Z  11 HOH   365  1765 518  HOH   HOH A . 
Z  11 HOH   366  1766 548  HOH   HOH A . 
Z  11 HOH   367  1767 445  HOH   HOH A . 
Z  11 HOH   368  1768 157  HOH   HOH A . 
Z  11 HOH   369  1769 2190 HOH   HOH A . 
Z  11 HOH   370  1770 192  HOH   HOH A . 
Z  11 HOH   371  1771 1729 HOH   HOH A . 
Z  11 HOH   372  1772 352  HOH   HOH A . 
Z  11 HOH   373  1773 275  HOH   HOH A . 
Z  11 HOH   374  1774 1164 HOH   HOH A . 
Z  11 HOH   375  1775 598  HOH   HOH A . 
Z  11 HOH   376  1776 23   HOH   HOH A . 
Z  11 HOH   377  1777 1494 HOH   HOH A . 
Z  11 HOH   378  1778 1419 HOH   HOH A . 
Z  11 HOH   379  1779 541  HOH   HOH A . 
Z  11 HOH   380  1780 1654 HOH   HOH A . 
Z  11 HOH   381  1781 88   HOH   HOH A . 
Z  11 HOH   382  1782 1521 HOH   HOH A . 
Z  11 HOH   383  1783 1093 HOH   HOH A . 
Z  11 HOH   384  1784 1470 HOH   HOH A . 
Z  11 HOH   385  1785 262  HOH   HOH A . 
Z  11 HOH   386  1786 2044 HOH   HOH A . 
Z  11 HOH   387  1787 1807 HOH   HOH A . 
Z  11 HOH   388  1788 473  HOH   HOH A . 
Z  11 HOH   389  1789 995  HOH   HOH A . 
Z  11 HOH   390  1790 1501 HOH   HOH A . 
Z  11 HOH   391  1791 570  HOH   HOH A . 
Z  11 HOH   392  1792 328  HOH   HOH A . 
Z  11 HOH   393  1793 896  HOH   HOH A . 
Z  11 HOH   394  1794 1241 HOH   HOH A . 
Z  11 HOH   395  1795 430  HOH   HOH A . 
Z  11 HOH   396  1796 1352 HOH   HOH A . 
Z  11 HOH   397  1797 1083 HOH   HOH A . 
Z  11 HOH   398  1798 2354 HOH   HOH A . 
Z  11 HOH   399  1799 1144 HOH   HOH A . 
Z  11 HOH   400  1800 1191 HOH   HOH A . 
Z  11 HOH   401  1801 2115 HOH   HOH A . 
Z  11 HOH   402  1802 1526 HOH   HOH A . 
Z  11 HOH   403  1803 1630 HOH   HOH A . 
Z  11 HOH   404  1804 380  HOH   HOH A . 
Z  11 HOH   405  1805 1875 HOH   HOH A . 
Z  11 HOH   406  1806 811  HOH   HOH A . 
Z  11 HOH   407  1807 36   HOH   HOH A . 
Z  11 HOH   408  1808 616  HOH   HOH A . 
Z  11 HOH   409  1809 423  HOH   HOH A . 
Z  11 HOH   410  1810 30   HOH   HOH A . 
Z  11 HOH   411  1811 713  HOH   HOH A . 
Z  11 HOH   412  1812 2084 HOH   HOH A . 
Z  11 HOH   413  1813 25   HOH   HOH A . 
Z  11 HOH   414  1814 698  HOH   HOH A . 
Z  11 HOH   415  1815 272  HOH   HOH A . 
Z  11 HOH   416  1816 2134 HOH   HOH A . 
Z  11 HOH   417  1817 483  HOH   HOH A . 
Z  11 HOH   418  1818 196  HOH   HOH A . 
Z  11 HOH   419  1819 1373 HOH   HOH A . 
Z  11 HOH   420  1820 1806 HOH   HOH A . 
Z  11 HOH   421  1821 271  HOH   HOH A . 
Z  11 HOH   422  1822 1319 HOH   HOH A . 
Z  11 HOH   423  1823 1794 HOH   HOH A . 
Z  11 HOH   424  1824 1139 HOH   HOH A . 
Z  11 HOH   425  1825 1121 HOH   HOH A . 
Z  11 HOH   426  1826 722  HOH   HOH A . 
Z  11 HOH   427  1827 42   HOH   HOH A . 
Z  11 HOH   428  1828 1221 HOH   HOH A . 
Z  11 HOH   429  1829 909  HOH   HOH A . 
Z  11 HOH   430  1830 1279 HOH   HOH A . 
Z  11 HOH   431  1831 160  HOH   HOH A . 
Z  11 HOH   432  1832 1096 HOH   HOH A . 
Z  11 HOH   433  1833 118  HOH   HOH A . 
Z  11 HOH   434  1834 1188 HOH   HOH A . 
Z  11 HOH   435  1835 1516 HOH   HOH A . 
Z  11 HOH   436  1836 1205 HOH   HOH A . 
Z  11 HOH   437  1837 869  HOH   HOH A . 
Z  11 HOH   438  1838 2384 HOH   HOH A . 
Z  11 HOH   439  1839 1632 HOH   HOH A . 
Z  11 HOH   440  1840 480  HOH   HOH A . 
Z  11 HOH   441  1841 417  HOH   HOH A . 
Z  11 HOH   442  1842 1281 HOH   HOH A . 
Z  11 HOH   443  1843 1375 HOH   HOH A . 
Z  11 HOH   444  1844 2057 HOH   HOH A . 
Z  11 HOH   445  1845 944  HOH   HOH A . 
Z  11 HOH   446  1846 517  HOH   HOH A . 
Z  11 HOH   447  1847 516  HOH   HOH A . 
Z  11 HOH   448  1848 73   HOH   HOH A . 
Z  11 HOH   449  1849 203  HOH   HOH A . 
Z  11 HOH   450  1850 1598 HOH   HOH A . 
Z  11 HOH   451  1851 435  HOH   HOH A . 
Z  11 HOH   452  1852 1490 HOH   HOH A . 
Z  11 HOH   453  1853 173  HOH   HOH A . 
Z  11 HOH   454  1854 752  HOH   HOH A . 
Z  11 HOH   455  1855 553  HOH   HOH A . 
Z  11 HOH   456  1856 2267 HOH   HOH A . 
Z  11 HOH   457  1857 738  HOH   HOH A . 
Z  11 HOH   458  1858 375  HOH   HOH A . 
Z  11 HOH   459  1859 890  HOH   HOH A . 
Z  11 HOH   460  1860 731  HOH   HOH A . 
Z  11 HOH   461  1861 2052 HOH   HOH A . 
Z  11 HOH   462  1862 358  HOH   HOH A . 
Z  11 HOH   463  1863 342  HOH   HOH A . 
Z  11 HOH   464  1864 964  HOH   HOH A . 
Z  11 HOH   465  1865 1036 HOH   HOH A . 
Z  11 HOH   466  1866 260  HOH   HOH A . 
Z  11 HOH   467  1867 1640 HOH   HOH A . 
Z  11 HOH   468  1868 1348 HOH   HOH A . 
Z  11 HOH   469  1869 2346 HOH   HOH A . 
Z  11 HOH   470  1870 233  HOH   HOH A . 
Z  11 HOH   471  1871 165  HOH   HOH A . 
Z  11 HOH   472  1872 920  HOH   HOH A . 
Z  11 HOH   473  1873 2433 HOH   HOH A . 
Z  11 HOH   474  1874 172  HOH   HOH A . 
Z  11 HOH   475  1875 44   HOH   HOH A . 
Z  11 HOH   476  1876 876  HOH   HOH A . 
Z  11 HOH   477  1877 82   HOH   HOH A . 
Z  11 HOH   478  1878 813  HOH   HOH A . 
Z  11 HOH   479  1879 193  HOH   HOH A . 
Z  11 HOH   480  1880 1314 HOH   HOH A . 
Z  11 HOH   481  1881 2252 HOH   HOH A . 
Z  11 HOH   482  1882 847  HOH   HOH A . 
Z  11 HOH   483  1883 294  HOH   HOH A . 
Z  11 HOH   484  1884 345  HOH   HOH A . 
Z  11 HOH   485  1885 856  HOH   HOH A . 
Z  11 HOH   486  1886 2331 HOH   HOH A . 
Z  11 HOH   487  1887 655  HOH   HOH A . 
Z  11 HOH   488  1888 71   HOH   HOH A . 
Z  11 HOH   489  1889 168  HOH   HOH A . 
Z  11 HOH   490  1890 990  HOH   HOH A . 
Z  11 HOH   491  1891 1798 HOH   HOH A . 
Z  11 HOH   492  1892 476  HOH   HOH A . 
Z  11 HOH   493  1893 1928 HOH   HOH A . 
Z  11 HOH   494  1894 329  HOH   HOH A . 
Z  11 HOH   495  1895 1704 HOH   HOH A . 
Z  11 HOH   496  1896 672  HOH   HOH A . 
Z  11 HOH   497  1897 2277 HOH   HOH A . 
Z  11 HOH   498  1898 1269 HOH   HOH A . 
Z  11 HOH   499  1899 915  HOH   HOH A . 
Z  11 HOH   500  1900 467  HOH   HOH A . 
Z  11 HOH   501  1901 1840 HOH   HOH A . 
Z  11 HOH   502  1902 34   HOH   HOH A . 
Z  11 HOH   503  1903 743  HOH   HOH A . 
Z  11 HOH   504  1904 2319 HOH   HOH A . 
Z  11 HOH   505  1905 867  HOH   HOH A . 
Z  11 HOH   506  1906 1764 HOH   HOH A . 
Z  11 HOH   507  1907 829  HOH   HOH A . 
Z  11 HOH   508  1908 323  HOH   HOH A . 
Z  11 HOH   509  1909 1386 HOH   HOH A . 
Z  11 HOH   510  1910 651  HOH   HOH A . 
Z  11 HOH   511  1911 619  HOH   HOH A . 
Z  11 HOH   512  1912 1568 HOH   HOH A . 
Z  11 HOH   513  1913 296  HOH   HOH A . 
Z  11 HOH   514  1914 574  HOH   HOH A . 
Z  11 HOH   515  1915 825  HOH   HOH A . 
Z  11 HOH   516  1916 827  HOH   HOH A . 
Z  11 HOH   517  1917 86   HOH   HOH A . 
Z  11 HOH   518  1918 706  HOH   HOH A . 
Z  11 HOH   519  1919 1596 HOH   HOH A . 
Z  11 HOH   520  1920 2395 HOH   HOH A . 
Z  11 HOH   521  1921 762  HOH   HOH A . 
Z  11 HOH   522  1922 1009 HOH   HOH A . 
Z  11 HOH   523  1923 350  HOH   HOH A . 
Z  11 HOH   524  1924 963  HOH   HOH A . 
Z  11 HOH   525  1925 284  HOH   HOH A . 
Z  11 HOH   526  1926 1546 HOH   HOH A . 
Z  11 HOH   527  1927 1035 HOH   HOH A . 
Z  11 HOH   528  1928 1166 HOH   HOH A . 
Z  11 HOH   529  1929 440  HOH   HOH A . 
Z  11 HOH   530  1930 2389 HOH   HOH A . 
Z  11 HOH   531  1931 18   HOH   HOH A . 
Z  11 HOH   532  1932 207  HOH   HOH A . 
Z  11 HOH   533  1933 788  HOH   HOH A . 
Z  11 HOH   534  1934 62   HOH   HOH A . 
Z  11 HOH   535  1935 584  HOH   HOH A . 
Z  11 HOH   536  1936 324  HOH   HOH A . 
Z  11 HOH   537  1937 1935 HOH   HOH A . 
Z  11 HOH   538  1938 610  HOH   HOH A . 
Z  11 HOH   539  1939 814  HOH   HOH A . 
Z  11 HOH   540  1940 1085 HOH   HOH A . 
Z  11 HOH   541  1941 108  HOH   HOH A . 
Z  11 HOH   542  1942 393  HOH   HOH A . 
Z  11 HOH   543  1943 1465 HOH   HOH A . 
Z  11 HOH   544  1944 532  HOH   HOH A . 
Z  11 HOH   545  1945 729  HOH   HOH A . 
Z  11 HOH   546  1946 1531 HOH   HOH A . 
Z  11 HOH   547  1947 246  HOH   HOH A . 
Z  11 HOH   548  1948 1969 HOH   HOH A . 
Z  11 HOH   549  1949 663  HOH   HOH A . 
Z  11 HOH   550  1950 587  HOH   HOH A . 
Z  11 HOH   551  1951 744  HOH   HOH A . 
Z  11 HOH   552  1952 1202 HOH   HOH A . 
Z  11 HOH   553  1953 419  HOH   HOH A . 
Z  11 HOH   554  1954 332  HOH   HOH A . 
Z  11 HOH   555  1955 746  HOH   HOH A . 
Z  11 HOH   556  1956 2186 HOH   HOH A . 
Z  11 HOH   557  1957 238  HOH   HOH A . 
Z  11 HOH   558  1958 1134 HOH   HOH A . 
Z  11 HOH   559  1959 511  HOH   HOH A . 
Z  11 HOH   560  1960 1755 HOH   HOH A . 
Z  11 HOH   561  1961 512  HOH   HOH A . 
Z  11 HOH   562  1962 1226 HOH   HOH A . 
Z  11 HOH   563  1963 1851 HOH   HOH A . 
Z  11 HOH   564  1964 1259 HOH   HOH A . 
Z  11 HOH   565  1965 586  HOH   HOH A . 
Z  11 HOH   566  1966 1812 HOH   HOH A . 
Z  11 HOH   567  1967 1900 HOH   HOH A . 
Z  11 HOH   568  1968 685  HOH   HOH A . 
Z  11 HOH   569  1969 391  HOH   HOH A . 
Z  11 HOH   570  1970 1478 HOH   HOH A . 
Z  11 HOH   571  1971 1034 HOH   HOH A . 
Z  11 HOH   572  1972 906  HOH   HOH A . 
Z  11 HOH   573  1973 1689 HOH   HOH A . 
Z  11 HOH   574  1974 261  HOH   HOH A . 
Z  11 HOH   575  1975 1123 HOH   HOH A . 
Z  11 HOH   576  1976 1071 HOH   HOH A . 
Z  11 HOH   577  1977 791  HOH   HOH A . 
Z  11 HOH   578  1978 887  HOH   HOH A . 
Z  11 HOH   579  1979 500  HOH   HOH A . 
Z  11 HOH   580  1980 588  HOH   HOH A . 
Z  11 HOH   581  1981 274  HOH   HOH A . 
Z  11 HOH   582  1982 325  HOH   HOH A . 
Z  11 HOH   583  1983 1713 HOH   HOH A . 
Z  11 HOH   584  1984 304  HOH   HOH A . 
Z  11 HOH   585  1985 1687 HOH   HOH A . 
Z  11 HOH   586  1986 608  HOH   HOH A . 
Z  11 HOH   587  1987 2278 HOH   HOH A . 
Z  11 HOH   588  1988 433  HOH   HOH A . 
Z  11 HOH   589  1989 1239 HOH   HOH A . 
Z  11 HOH   590  1990 2098 HOH   HOH A . 
Z  11 HOH   591  1991 297  HOH   HOH A . 
Z  11 HOH   592  1992 834  HOH   HOH A . 
Z  11 HOH   593  1993 2095 HOH   HOH A . 
Z  11 HOH   594  1994 1367 HOH   HOH A . 
Z  11 HOH   595  1995 1267 HOH   HOH A . 
Z  11 HOH   596  1996 895  HOH   HOH A . 
Z  11 HOH   597  1997 93   HOH   HOH A . 
Z  11 HOH   598  1998 2429 HOH   HOH A . 
Z  11 HOH   599  1999 1246 HOH   HOH A . 
Z  11 HOH   600  2000 61   HOH   HOH A . 
Z  11 HOH   601  2001 2131 HOH   HOH A . 
Z  11 HOH   602  2002 2315 HOH   HOH A . 
Z  11 HOH   603  2003 1932 HOH   HOH A . 
Z  11 HOH   604  2004 1660 HOH   HOH A . 
Z  11 HOH   605  2005 1158 HOH   HOH A . 
Z  11 HOH   606  2006 2050 HOH   HOH A . 
Z  11 HOH   607  2007 1483 HOH   HOH A . 
Z  11 HOH   608  2008 2077 HOH   HOH A . 
Z  11 HOH   609  2009 528  HOH   HOH A . 
Z  11 HOH   610  2010 552  HOH   HOH A . 
Z  11 HOH   611  2011 255  HOH   HOH A . 
Z  11 HOH   612  2012 364  HOH   HOH A . 
Z  11 HOH   613  2013 72   HOH   HOH A . 
Z  11 HOH   614  2014 779  HOH   HOH A . 
Z  11 HOH   615  2015 367  HOH   HOH A . 
Z  11 HOH   616  2016 1667 HOH   HOH A . 
Z  11 HOH   617  2017 1094 HOH   HOH A . 
Z  11 HOH   618  2018 2023 HOH   HOH A . 
Z  11 HOH   619  2019 1019 HOH   HOH A . 
Z  11 HOH   620  2020 1563 HOH   HOH A . 
Z  11 HOH   621  2021 1021 HOH   HOH A . 
Z  11 HOH   622  2022 787  HOH   HOH A . 
Z  11 HOH   623  2023 922  HOH   HOH A . 
Z  11 HOH   624  2024 1197 HOH   HOH A . 
Z  11 HOH   625  2025 1592 HOH   HOH A . 
Z  11 HOH   626  2026 1658 HOH   HOH A . 
Z  11 HOH   627  2027 1889 HOH   HOH A . 
Z  11 HOH   628  2028 150  HOH   HOH A . 
Z  11 HOH   629  2029 299  HOH   HOH A . 
Z  11 HOH   630  2030 1222 HOH   HOH A . 
Z  11 HOH   631  2031 2010 HOH   HOH A . 
Z  11 HOH   632  2032 1213 HOH   HOH A . 
Z  11 HOH   633  2033 1921 HOH   HOH A . 
Z  11 HOH   634  2034 1626 HOH   HOH A . 
Z  11 HOH   635  2035 593  HOH   HOH A . 
Z  11 HOH   636  2036 1250 HOH   HOH A . 
Z  11 HOH   637  2037 858  HOH   HOH A . 
Z  11 HOH   638  2038 371  HOH   HOH A . 
Z  11 HOH   639  2039 1417 HOH   HOH A . 
Z  11 HOH   640  2040 735  HOH   HOH A . 
Z  11 HOH   641  2041 2353 HOH   HOH A . 
Z  11 HOH   642  2042 1432 HOH   HOH A . 
Z  11 HOH   643  2043 208  HOH   HOH A . 
Z  11 HOH   644  2044 1045 HOH   HOH A . 
Z  11 HOH   645  2045 495  HOH   HOH A . 
Z  11 HOH   646  2046 1075 HOH   HOH A . 
Z  11 HOH   647  2047 1805 HOH   HOH A . 
Z  11 HOH   648  2048 2239 HOH   HOH A . 
Z  11 HOH   649  2049 558  HOH   HOH A . 
Z  11 HOH   650  2050 1216 HOH   HOH A . 
Z  11 HOH   651  2051 2125 HOH   HOH A . 
Z  11 HOH   652  2052 109  HOH   HOH A . 
Z  11 HOH   653  2053 485  HOH   HOH A . 
Z  11 HOH   654  2054 1618 HOH   HOH A . 
Z  11 HOH   655  2055 978  HOH   HOH A . 
Z  11 HOH   656  2056 1441 HOH   HOH A . 
Z  11 HOH   657  2057 416  HOH   HOH A . 
Z  11 HOH   658  2058 1049 HOH   HOH A . 
Z  11 HOH   659  2059 166  HOH   HOH A . 
Z  11 HOH   660  2060 39   HOH   HOH A . 
Z  11 HOH   661  2061 1951 HOH   HOH A . 
Z  11 HOH   662  2062 415  HOH   HOH A . 
Z  11 HOH   663  2063 111  HOH   HOH A . 
Z  11 HOH   664  2064 1504 HOH   HOH A . 
Z  11 HOH   665  2065 851  HOH   HOH A . 
Z  11 HOH   666  2066 601  HOH   HOH A . 
Z  11 HOH   667  2067 540  HOH   HOH A . 
Z  11 HOH   668  2068 1266 HOH   HOH A . 
Z  11 HOH   669  2069 1346 HOH   HOH A . 
Z  11 HOH   670  2070 879  HOH   HOH A . 
Z  11 HOH   671  2071 321  HOH   HOH A . 
Z  11 HOH   672  2072 1716 HOH   HOH A . 
Z  11 HOH   673  2073 69   HOH   HOH A . 
Z  11 HOH   674  2074 633  HOH   HOH A . 
Z  11 HOH   675  2075 1668 HOH   HOH A . 
Z  11 HOH   676  2076 1956 HOH   HOH A . 
Z  11 HOH   677  2077 763  HOH   HOH A . 
Z  11 HOH   678  2078 228  HOH   HOH A . 
Z  11 HOH   679  2079 605  HOH   HOH A . 
Z  11 HOH   680  2080 1249 HOH   HOH A . 
Z  11 HOH   681  2081 2282 HOH   HOH A . 
Z  11 HOH   682  2082 656  HOH   HOH A . 
Z  11 HOH   683  2083 953  HOH   HOH A . 
Z  11 HOH   684  2084 666  HOH   HOH A . 
Z  11 HOH   685  2085 2133 HOH   HOH A . 
Z  11 HOH   686  2086 660  HOH   HOH A . 
Z  11 HOH   687  2087 1459 HOH   HOH A . 
Z  11 HOH   688  2088 572  HOH   HOH A . 
Z  11 HOH   689  2089 854  HOH   HOH A . 
Z  11 HOH   690  2090 1809 HOH   HOH A . 
Z  11 HOH   691  2091 1675 HOH   HOH A . 
Z  11 HOH   692  2092 981  HOH   HOH A . 
Z  11 HOH   693  2093 790  HOH   HOH A . 
Z  11 HOH   694  2094 398  HOH   HOH A . 
Z  11 HOH   695  2095 1802 HOH   HOH A . 
Z  11 HOH   696  2096 1010 HOH   HOH A . 
Z  11 HOH   697  2097 2149 HOH   HOH A . 
Z  11 HOH   698  2098 1325 HOH   HOH A . 
Z  11 HOH   699  2099 636  HOH   HOH A . 
Z  11 HOH   700  2100 1185 HOH   HOH A . 
Z  11 HOH   701  2101 2120 HOH   HOH A . 
Z  11 HOH   702  2102 2043 HOH   HOH A . 
Z  11 HOH   703  2103 1614 HOH   HOH A . 
Z  11 HOH   704  2104 458  HOH   HOH A . 
Z  11 HOH   705  2105 969  HOH   HOH A . 
Z  11 HOH   706  2106 736  HOH   HOH A . 
Z  11 HOH   707  2107 1487 HOH   HOH A . 
Z  11 HOH   708  2108 699  HOH   HOH A . 
Z  11 HOH   709  2109 2072 HOH   HOH A . 
Z  11 HOH   710  2110 1842 HOH   HOH A . 
Z  11 HOH   711  2111 935  HOH   HOH A . 
Z  11 HOH   712  2112 453  HOH   HOH A . 
Z  11 HOH   713  2113 817  HOH   HOH A . 
Z  11 HOH   714  2114 215  HOH   HOH A . 
Z  11 HOH   715  2115 1412 HOH   HOH A . 
Z  11 HOH   716  2116 777  HOH   HOH A . 
Z  11 HOH   717  2117 1498 HOH   HOH A . 
Z  11 HOH   718  2118 1664 HOH   HOH A . 
Z  11 HOH   719  2119 1642 HOH   HOH A . 
Z  11 HOH   720  2120 669  HOH   HOH A . 
Z  11 HOH   721  2121 2170 HOH   HOH A . 
Z  11 HOH   722  2122 327  HOH   HOH A . 
Z  11 HOH   723  2123 1819 HOH   HOH A . 
Z  11 HOH   724  2124 1922 HOH   HOH A . 
Z  11 HOH   725  2125 1651 HOH   HOH A . 
Z  11 HOH   726  2126 1315 HOH   HOH A . 
Z  11 HOH   727  2127 372  HOH   HOH A . 
Z  11 HOH   728  2128 1944 HOH   HOH A . 
Z  11 HOH   729  2129 529  HOH   HOH A . 
Z  11 HOH   730  2130 2337 HOH   HOH A . 
Z  11 HOH   731  2131 1402 HOH   HOH A . 
Z  11 HOH   732  2132 992  HOH   HOH A . 
Z  11 HOH   733  2133 1371 HOH   HOH A . 
Z  11 HOH   734  2134 245  HOH   HOH A . 
Z  11 HOH   735  2135 721  HOH   HOH A . 
Z  11 HOH   736  2136 522  HOH   HOH A . 
Z  11 HOH   737  2137 957  HOH   HOH A . 
Z  11 HOH   738  2138 316  HOH   HOH A . 
Z  11 HOH   739  2139 451  HOH   HOH A . 
Z  11 HOH   740  2140 959  HOH   HOH A . 
Z  11 HOH   741  2141 707  HOH   HOH A . 
Z  11 HOH   742  2142 263  HOH   HOH A . 
Z  11 HOH   743  2143 388  HOH   HOH A . 
Z  11 HOH   744  2144 2058 HOH   HOH A . 
Z  11 HOH   745  2145 955  HOH   HOH A . 
Z  11 HOH   746  2146 479  HOH   HOH A . 
Z  11 HOH   747  2147 1829 HOH   HOH A . 
Z  11 HOH   748  2148 2333 HOH   HOH A . 
Z  11 HOH   749  2149 1757 HOH   HOH A . 
Z  11 HOH   750  2150 1309 HOH   HOH A . 
Z  11 HOH   751  2151 2078 HOH   HOH A . 
Z  11 HOH   752  2152 200  HOH   HOH A . 
Z  11 HOH   753  2153 2208 HOH   HOH A . 
Z  11 HOH   754  2154 2301 HOH   HOH A . 
Z  11 HOH   755  2155 782  HOH   HOH A . 
Z  11 HOH   756  2156 138  HOH   HOH A . 
Z  11 HOH   757  2157 427  HOH   HOH A . 
Z  11 HOH   758  2158 268  HOH   HOH A . 
Z  11 HOH   759  2159 696  HOH   HOH A . 
Z  11 HOH   760  2160 885  HOH   HOH A . 
Z  11 HOH   761  2161 1366 HOH   HOH A . 
Z  11 HOH   762  2162 1473 HOH   HOH A . 
Z  11 HOH   763  2163 2063 HOH   HOH A . 
Z  11 HOH   764  2164 460  HOH   HOH A . 
Z  11 HOH   765  2165 1539 HOH   HOH A . 
Z  11 HOH   766  2166 1403 HOH   HOH A . 
Z  11 HOH   767  2167 991  HOH   HOH A . 
Z  11 HOH   768  2168 1016 HOH   HOH A . 
Z  11 HOH   769  2169 940  HOH   HOH A . 
Z  11 HOH   770  2170 2425 HOH   HOH A . 
Z  11 HOH   771  2171 1631 HOH   HOH A . 
Z  11 HOH   772  2172 904  HOH   HOH A . 
Z  11 HOH   773  2173 1268 HOH   HOH A . 
Z  11 HOH   774  2174 420  HOH   HOH A . 
Z  11 HOH   775  2175 578  HOH   HOH A . 
Z  11 HOH   776  2176 984  HOH   HOH A . 
Z  11 HOH   777  2177 1160 HOH   HOH A . 
Z  11 HOH   778  2178 1242 HOH   HOH A . 
Z  11 HOH   779  2179 1117 HOH   HOH A . 
Z  11 HOH   780  2180 1020 HOH   HOH A . 
Z  11 HOH   781  2181 803  HOH   HOH A . 
Z  11 HOH   782  2182 2094 HOH   HOH A . 
Z  11 HOH   783  2183 221  HOH   HOH A . 
Z  11 HOH   784  2184 2388 HOH   HOH A . 
Z  11 HOH   785  2185 376  HOH   HOH A . 
Z  11 HOH   786  2186 536  HOH   HOH A . 
Z  11 HOH   787  2187 874  HOH   HOH A . 
Z  11 HOH   788  2188 187  HOH   HOH A . 
Z  11 HOH   789  2189 414  HOH   HOH A . 
Z  11 HOH   790  2190 418  HOH   HOH A . 
Z  11 HOH   791  2191 1284 HOH   HOH A . 
Z  11 HOH   792  2192 1570 HOH   HOH A . 
Z  11 HOH   793  2193 492  HOH   HOH A . 
Z  11 HOH   794  2194 1970 HOH   HOH A . 
Z  11 HOH   795  2195 693  HOH   HOH A . 
Z  11 HOH   796  2196 1399 HOH   HOH A . 
Z  11 HOH   797  2197 898  HOH   HOH A . 
Z  11 HOH   798  2198 1574 HOH   HOH A . 
Z  11 HOH   799  2199 37   HOH   HOH A . 
Z  11 HOH   800  2200 1095 HOH   HOH A . 
Z  11 HOH   801  2201 1748 HOH   HOH A . 
Z  11 HOH   802  2202 1381 HOH   HOH A . 
Z  11 HOH   803  2203 702  HOH   HOH A . 
Z  11 HOH   804  2204 2092 HOH   HOH A . 
Z  11 HOH   805  2205 1393 HOH   HOH A . 
Z  11 HOH   806  2206 775  HOH   HOH A . 
Z  11 HOH   807  2207 998  HOH   HOH A . 
Z  11 HOH   808  2208 2373 HOH   HOH A . 
Z  11 HOH   809  2209 1372 HOH   HOH A . 
Z  11 HOH   810  2210 2450 HOH   HOH A . 
Z  11 HOH   811  2211 1744 HOH   HOH A . 
Z  11 HOH   812  2212 1199 HOH   HOH A . 
Z  11 HOH   813  2213 537  HOH   HOH A . 
Z  11 HOH   814  2214 897  HOH   HOH A . 
Z  11 HOH   815  2215 289  HOH   HOH A . 
Z  11 HOH   816  2216 946  HOH   HOH A . 
Z  11 HOH   817  2217 1566 HOH   HOH A . 
Z  11 HOH   818  2218 2272 HOH   HOH A . 
Z  11 HOH   819  2219 1437 HOH   HOH A . 
Z  11 HOH   820  2220 405  HOH   HOH A . 
Z  11 HOH   821  2221 1507 HOH   HOH A . 
Z  11 HOH   822  2222 2176 HOH   HOH A . 
Z  11 HOH   823  2223 1637 HOH   HOH A . 
Z  11 HOH   824  2224 163  HOH   HOH A . 
Z  11 HOH   825  2225 2159 HOH   HOH A . 
Z  11 HOH   826  2226 2327 HOH   HOH A . 
Z  11 HOH   827  2227 2394 HOH   HOH A . 
Z  11 HOH   828  2228 860  HOH   HOH A . 
Z  11 HOH   829  2229 939  HOH   HOH A . 
Z  11 HOH   830  2230 1811 HOH   HOH A . 
Z  11 HOH   831  2231 1633 HOH   HOH A . 
Z  11 HOH   832  2232 2255 HOH   HOH A . 
Z  11 HOH   833  2233 1847 HOH   HOH A . 
Z  11 HOH   834  2234 2347 HOH   HOH A . 
Z  11 HOH   835  2235 664  HOH   HOH A . 
Z  11 HOH   836  2236 842  HOH   HOH A . 
Z  11 HOH   837  2237 2427 HOH   HOH A . 
Z  11 HOH   838  2238 1434 HOH   HOH A . 
Z  11 HOH   839  2239 1270 HOH   HOH A . 
Z  11 HOH   840  2240 2205 HOH   HOH A . 
Z  11 HOH   841  2241 1012 HOH   HOH A . 
Z  11 HOH   842  2242 506  HOH   HOH A . 
Z  11 HOH   843  2243 27   HOH   HOH A . 
Z  11 HOH   844  2244 661  HOH   HOH A . 
Z  11 HOH   845  2245 2117 HOH   HOH A . 
Z  11 HOH   846  2246 1534 HOH   HOH A . 
Z  11 HOH   847  2247 1788 HOH   HOH A . 
Z  11 HOH   848  2248 403  HOH   HOH A . 
Z  11 HOH   849  2249 2340 HOH   HOH A . 
Z  11 HOH   850  2250 1291 HOH   HOH A . 
Z  11 HOH   851  2251 1950 HOH   HOH A . 
Z  11 HOH   852  2252 796  HOH   HOH A . 
Z  11 HOH   853  2253 841  HOH   HOH A . 
Z  11 HOH   854  2254 1046 HOH   HOH A . 
Z  11 HOH   855  2255 1597 HOH   HOH A . 
Z  11 HOH   856  2256 772  HOH   HOH A . 
Z  11 HOH   857  2257 761  HOH   HOH A . 
Z  11 HOH   858  2258 2124 HOH   HOH A . 
Z  11 HOH   859  2259 1030 HOH   HOH A . 
Z  11 HOH   860  2260 753  HOH   HOH A . 
Z  11 HOH   861  2261 936  HOH   HOH A . 
Z  11 HOH   862  2262 2066 HOH   HOH A . 
Z  11 HOH   863  2263 1793 HOH   HOH A . 
Z  11 HOH   864  2264 2116 HOH   HOH A . 
Z  11 HOH   865  2265 1509 HOH   HOH A . 
Z  11 HOH   866  2266 1328 HOH   HOH A . 
Z  11 HOH   867  2267 1778 HOH   HOH A . 
Z  11 HOH   868  2268 684  HOH   HOH A . 
Z  11 HOH   869  2269 1072 HOH   HOH A . 
Z  11 HOH   870  2270 2456 HOH   HOH A . 
Z  11 HOH   871  2271 1912 HOH   HOH A . 
Z  11 HOH   872  2272 1138 HOH   HOH A . 
Z  11 HOH   873  2273 1873 HOH   HOH A . 
Z  11 HOH   874  2274 2045 HOH   HOH A . 
Z  11 HOH   875  2275 785  HOH   HOH A . 
Z  11 HOH   876  2276 1586 HOH   HOH A . 
Z  11 HOH   877  2277 2051 HOH   HOH A . 
Z  11 HOH   878  2278 2428 HOH   HOH A . 
Z  11 HOH   879  2279 2198 HOH   HOH A . 
Z  11 HOH   880  2280 2324 HOH   HOH A . 
Z  11 HOH   881  2281 1078 HOH   HOH A . 
Z  11 HOH   882  2282 1756 HOH   HOH A . 
Z  11 HOH   883  2283 1916 HOH   HOH A . 
Z  11 HOH   884  2284 2144 HOH   HOH A . 
Z  11 HOH   885  2285 2060 HOH   HOH A . 
Z  11 HOH   886  2286 1050 HOH   HOH A . 
Z  11 HOH   887  2287 2179 HOH   HOH A . 
Z  11 HOH   888  2288 794  HOH   HOH A . 
Z  11 HOH   889  2289 2258 HOH   HOH A . 
Z  11 HOH   890  2290 396  HOH   HOH A . 
Z  11 HOH   891  2291 1208 HOH   HOH A . 
Z  11 HOH   892  2292 2024 HOH   HOH A . 
Z  11 HOH   893  2293 1971 HOH   HOH A . 
Z  11 HOH   894  2294 2206 HOH   HOH A . 
Z  11 HOH   895  2295 2341 HOH   HOH A . 
Z  11 HOH   896  2296 2165 HOH   HOH A . 
Z  11 HOH   897  2297 2249 HOH   HOH A . 
Z  11 HOH   898  2298 2230 HOH   HOH A . 
Z  11 HOH   899  2299 2371 HOH   HOH A . 
Z  11 HOH   900  2300 1408 HOH   HOH A . 
Z  11 HOH   901  2301 2018 HOH   HOH A . 
Z  11 HOH   902  2302 1678 HOH   HOH A . 
Z  11 HOH   903  2303 2146 HOH   HOH A . 
Z  11 HOH   904  2304 910  HOH   HOH A . 
Z  11 HOH   905  2305 1882 HOH   HOH A . 
Z  11 HOH   906  2306 677  HOH   HOH A . 
Z  11 HOH   907  2307 934  HOH   HOH A . 
Z  11 HOH   908  2308 2250 HOH   HOH A . 
Z  11 HOH   909  2309 1881 HOH   HOH A . 
Z  11 HOH   910  2310 2231 HOH   HOH A . 
Z  11 HOH   911  2311 1839 HOH   HOH A . 
Z  11 HOH   912  2312 1312 HOH   HOH A . 
Z  11 HOH   913  2313 1416 HOH   HOH A . 
Z  11 HOH   914  2314 2236 HOH   HOH A . 
Z  11 HOH   915  2315 2307 HOH   HOH A . 
Z  11 HOH   916  2316 1754 HOH   HOH A . 
Z  11 HOH   917  2317 2387 HOH   HOH A . 
Z  11 HOH   918  2318 2316 HOH   HOH A . 
Z  11 HOH   919  2319 2390 HOH   HOH A . 
Z  11 HOH   920  2320 1972 HOH   HOH A . 
Z  11 HOH   921  2321 2300 HOH   HOH A . 
Z  11 HOH   922  2322 1290 HOH   HOH A . 
Z  11 HOH   923  2323 1909 HOH   HOH A . 
Z  11 HOH   924  2324 1316 HOH   HOH A . 
Z  11 HOH   925  2325 1624 HOH   HOH A . 
Z  11 HOH   926  2326 1685 HOH   HOH A . 
Z  11 HOH   927  2327 1299 HOH   HOH A . 
Z  11 HOH   928  2328 1254 HOH   HOH A . 
Z  11 HOH   929  2329 2426 HOH   HOH A . 
Z  11 HOH   930  2330 2370 HOH   HOH A . 
Z  11 HOH   931  2331 1380 HOH   HOH A . 
Z  11 HOH   932  2332 986  HOH   HOH A . 
Z  11 HOH   933  2333 1262 HOH   HOH A . 
Z  11 HOH   934  2334 1525 HOH   HOH A . 
Z  11 HOH   935  2335 1695 HOH   HOH A . 
Z  11 HOH   936  2336 2308 HOH   HOH A . 
Z  11 HOH   937  2337 1058 HOH   HOH A . 
Z  11 HOH   938  2338 621  HOH   HOH A . 
Z  11 HOH   939  2339 2411 HOH   HOH A . 
Z  11 HOH   940  2340 927  HOH   HOH A . 
Z  11 HOH   941  2341 2318 HOH   HOH A . 
Z  11 HOH   942  2342 2067 HOH   HOH A . 
Z  11 HOH   943  2343 1240 HOH   HOH A . 
Z  11 HOH   944  2344 562  HOH   HOH A . 
Z  11 HOH   945  2345 1945 HOH   HOH A . 
Z  11 HOH   946  2346 1634 HOH   HOH A . 
Z  11 HOH   947  2347 1340 HOH   HOH A . 
Z  11 HOH   948  2348 2132 HOH   HOH A . 
Z  11 HOH   949  2349 918  HOH   HOH A . 
Z  11 HOH   950  2350 2365 HOH   HOH A . 
Z  11 HOH   951  2351 1527 HOH   HOH A . 
Z  11 HOH   952  2352 1561 HOH   HOH A . 
Z  11 HOH   953  2353 832  HOH   HOH A . 
Z  11 HOH   954  2354 968  HOH   HOH A . 
Z  11 HOH   955  2355 2451 HOH   HOH A . 
Z  11 HOH   956  2356 1104 HOH   HOH A . 
Z  11 HOH   957  2357 2243 HOH   HOH A . 
Z  11 HOH   958  2358 1589 HOH   HOH A . 
Z  11 HOH   959  2359 1623 HOH   HOH A . 
Z  11 HOH   960  2360 1210 HOH   HOH A . 
Z  11 HOH   961  2361 1872 HOH   HOH A . 
Z  11 HOH   962  2362 1679 HOH   HOH A . 
Z  11 HOH   963  2363 1282 HOH   HOH A . 
Z  11 HOH   964  2364 2012 HOH   HOH A . 
Z  11 HOH   965  2365 1101 HOH   HOH A . 
Z  11 HOH   966  2366 2059 HOH   HOH A . 
Z  11 HOH   967  2367 2119 HOH   HOH A . 
Z  11 HOH   968  2368 884  HOH   HOH A . 
Z  11 HOH   969  2369 2071 HOH   HOH A . 
Z  11 HOH   970  2370 2008 HOH   HOH A . 
Z  11 HOH   971  2371 840  HOH   HOH A . 
Z  11 HOH   972  2372 2143 HOH   HOH A . 
Z  11 HOH   973  2373 2097 HOH   HOH A . 
Z  11 HOH   974  2374 1830 HOH   HOH A . 
Z  11 HOH   975  2375 2128 HOH   HOH A . 
Z  11 HOH   976  2376 1627 HOH   HOH A . 
Z  11 HOH   977  2377 2435 HOH   HOH A . 
Z  11 HOH   978  2378 2178 HOH   HOH A . 
Z  11 HOH   979  2379 1469 HOH   HOH A . 
Z  11 HOH   980  2380 1953 HOH   HOH A . 
Z  11 HOH   981  2381 2366 HOH   HOH A . 
Z  11 HOH   982  2382 1460 HOH   HOH A . 
Z  11 HOH   983  2383 2254 HOH   HOH A . 
Z  11 HOH   984  2384 2374 HOH   HOH A . 
Z  11 HOH   985  2385 1513 HOH   HOH A . 
Z  11 HOH   986  2386 1227 HOH   HOH A . 
Z  11 HOH   987  2387 837  HOH   HOH A . 
Z  11 HOH   988  2388 1908 HOH   HOH A . 
Z  11 HOH   989  2389 2321 HOH   HOH A . 
Z  11 HOH   990  2390 2424 HOH   HOH A . 
Z  11 HOH   991  2391 2244 HOH   HOH A . 
Z  11 HOH   992  2392 1173 HOH   HOH A . 
Z  11 HOH   993  2393 1762 HOH   HOH A . 
Z  11 HOH   994  2394 1903 HOH   HOH A . 
Z  11 HOH   995  2395 2372 HOH   HOH A . 
Z  11 HOH   996  2396 1335 HOH   HOH A . 
Z  11 HOH   997  2397 428  HOH   HOH A . 
Z  11 HOH   998  2398 1422 HOH   HOH A . 
Z  11 HOH   999  2399 2130 HOH   HOH A . 
Z  11 HOH   1000 2400 2329 HOH   HOH A . 
Z  11 HOH   1001 2401 2053 HOH   HOH A . 
Z  11 HOH   1002 2402 2442 HOH   HOH A . 
Z  11 HOH   1003 2403 1425 HOH   HOH A . 
Z  11 HOH   1004 2404 609  HOH   HOH A . 
Z  11 HOH   1005 2405 1603 HOH   HOH A . 
Z  11 HOH   1006 2406 1580 HOH   HOH A . 
Z  11 HOH   1007 2407 1670 HOH   HOH A . 
Z  11 HOH   1008 2408 1960 HOH   HOH A . 
Z  11 HOH   1009 2409 164  HOH   HOH A . 
Z  11 HOH   1010 2410 1649 HOH   HOH A . 
Z  11 HOH   1011 2411 1343 HOH   HOH A . 
Z  11 HOH   1012 2412 1706 HOH   HOH A . 
Z  11 HOH   1013 2413 1792 HOH   HOH A . 
Z  11 HOH   1014 2414 1814 HOH   HOH A . 
Z  11 HOH   1015 2415 2245 HOH   HOH A . 
Z  11 HOH   1016 2416 2453 HOH   HOH A . 
Z  11 HOH   1017 2417 1007 HOH   HOH A . 
Z  11 HOH   1018 2418 1818 HOH   HOH A . 
Z  11 HOH   1019 2419 1228 HOH   HOH A . 
Z  11 HOH   1020 2420 1587 HOH   HOH A . 
Z  11 HOH   1021 2421 1773 HOH   HOH A . 
Z  11 HOH   1022 2422 1933 HOH   HOH A . 
Z  11 HOH   1023 2423 1901 HOH   HOH A . 
Z  11 HOH   1024 2424 1843 HOH   HOH A . 
Z  11 HOH   1025 2425 1871 HOH   HOH A . 
Z  11 HOH   1026 2426 389  HOH   HOH A . 
Z  11 HOH   1027 2427 2013 HOH   HOH A . 
Z  11 HOH   1028 2428 2465 HOH   HOH A . 
Z  11 HOH   1029 2429 2304 HOH   HOH A . 
Z  11 HOH   1030 2430 1189 HOH   HOH A . 
Z  11 HOH   1031 2431 2110 HOH   HOH A . 
Z  11 HOH   1032 2432 2225 HOH   HOH A . 
Z  11 HOH   1033 2433 1236 HOH   HOH A . 
Z  11 HOH   1034 2434 2326 HOH   HOH A . 
Z  11 HOH   1035 2435 2073 HOH   HOH A . 
Z  11 HOH   1036 2436 1127 HOH   HOH A . 
Z  11 HOH   1037 2437 1797 HOH   HOH A . 
Z  11 HOH   1038 2438 1947 HOH   HOH A . 
Z  11 HOH   1039 2439 2434 HOH   HOH A . 
Z  11 HOH   1040 2440 550  HOH   HOH A . 
Z  11 HOH   1041 2441 2385 HOH   HOH A . 
Z  11 HOH   1042 2442 1000 HOH   HOH A . 
Z  11 HOH   1043 2443 1145 HOH   HOH A . 
Z  11 HOH   1044 2444 2454 HOH   HOH A . 
Z  11 HOH   1045 2445 1701 HOH   HOH A . 
Z  11 HOH   1046 2446 2064 HOH   HOH A . 
Z  11 HOH   1047 2447 2020 HOH   HOH A . 
Z  11 HOH   1048 2448 2157 HOH   HOH A . 
Z  11 HOH   1049 2449 1326 HOH   HOH A . 
Z  11 HOH   1050 2450 905  HOH   HOH A . 
Z  11 HOH   1051 2451 1031 HOH   HOH A . 
Z  11 HOH   1052 2452 2262 HOH   HOH A . 
Z  11 HOH   1053 2453 2386 HOH   HOH A . 
Z  11 HOH   1054 2454 1431 HOH   HOH A . 
Z  11 HOH   1055 2455 650  HOH   HOH A . 
Z  11 HOH   1056 2456 1931 HOH   HOH A . 
Z  11 HOH   1057 2457 1446 HOH   HOH A . 
Z  11 HOH   1058 2458 2335 HOH   HOH A . 
Z  11 HOH   1059 2459 1696 HOH   HOH A . 
Z  11 HOH   1060 2460 2280 HOH   HOH A . 
Z  11 HOH   1061 2461 1766 HOH   HOH A . 
Z  11 HOH   1062 2462 2212 HOH   HOH A . 
Z  11 HOH   1063 2463 1815 HOH   HOH A . 
Z  11 HOH   1064 2464 1497 HOH   HOH A . 
Z  11 HOH   1065 2465 2402 HOH   HOH A . 
Z  11 HOH   1066 2466 2216 HOH   HOH A . 
Z  11 HOH   1067 2467 819  HOH   HOH A . 
Z  11 HOH   1068 2468 2323 HOH   HOH A . 
Z  11 HOH   1069 2469 1761 HOH   HOH A . 
Z  11 HOH   1070 2470 1602 HOH   HOH A . 
Z  11 HOH   1071 2471 288  HOH   HOH A . 
Z  11 HOH   1072 2472 1955 HOH   HOH A . 
Z  11 HOH   1073 2473 1011 HOH   HOH A . 
Z  11 HOH   1074 2474 2463 HOH   HOH A . 
Z  11 HOH   1075 2475 2464 HOH   HOH A . 
Z  11 HOH   1076 2476 1726 HOH   HOH A . 
Z  11 HOH   1077 2477 2180 HOH   HOH A . 
Z  11 HOH   1078 2478 2452 HOH   HOH A . 
Z  11 HOH   1079 2479 2269 HOH   HOH A . 
Z  11 HOH   1080 2480 1037 HOH   HOH A . 
Z  11 HOH   1081 2481 2166 HOH   HOH A . 
Z  11 HOH   1082 2482 1398 HOH   HOH A . 
Z  11 HOH   1083 2483 2047 HOH   HOH A . 
Z  11 HOH   1084 2484 1018 HOH   HOH A . 
Z  11 HOH   1085 2485 1849 HOH   HOH A . 
Z  11 HOH   1086 2486 1768 HOH   HOH A . 
Z  11 HOH   1087 2487 1827 HOH   HOH A . 
Z  11 HOH   1088 2488 1841 HOH   HOH A . 
Z  11 HOH   1089 2489 1477 HOH   HOH A . 
Z  11 HOH   1090 2490 2135 HOH   HOH A . 
Z  11 HOH   1091 2491 1120 HOH   HOH A . 
Z  11 HOH   1092 2492 1310 HOH   HOH A . 
Z  11 HOH   1093 2493 2376 HOH   HOH A . 
Z  11 HOH   1094 2494 2364 HOH   HOH A . 
Z  11 HOH   1095 2495 1820 HOH   HOH A . 
Z  11 HOH   1096 2496 2401 HOH   HOH A . 
Z  11 HOH   1097 2497 477  HOH   HOH A . 
Z  11 HOH   1098 2498 1183 HOH   HOH A . 
Z  11 HOH   1099 2499 2270 HOH   HOH A . 
Z  11 HOH   1100 2500 2108 HOH   HOH A . 
Z  11 HOH   1101 2501 1130 HOH   HOH A . 
Z  11 HOH   1102 2502 2273 HOH   HOH A . 
Z  11 HOH   1103 2503 1897 HOH   HOH A . 
Z  11 HOH   1104 2504 1027 HOH   HOH A . 
Z  11 HOH   1105 2505 1167 HOH   HOH A . 
Z  11 HOH   1106 2506 1611 HOH   HOH A . 
Z  11 HOH   1107 2507 2378 HOH   HOH A . 
Z  11 HOH   1108 2508 1554 HOH   HOH A . 
Z  11 HOH   1109 2509 2423 HOH   HOH A . 
Z  11 HOH   1110 2510 1835 HOH   HOH A . 
Z  11 HOH   1111 2511 2093 HOH   HOH A . 
Z  11 HOH   1112 2512 2136 HOH   HOH A . 
Z  11 HOH   1113 2513 1463 HOH   HOH A . 
Z  11 HOH   1114 2514 2177 HOH   HOH A . 
Z  11 HOH   1115 2515 1298 HOH   HOH A . 
Z  11 HOH   1116 2516 2274 HOH   HOH A . 
Z  11 HOH   1117 2517 1837 HOH   HOH A . 
Z  11 HOH   1118 2518 1334 HOH   HOH A . 
Z  11 HOH   1119 2519 1641 HOH   HOH A . 
Z  11 HOH   1120 2520 914  HOH   HOH A . 
Z  11 HOH   1121 2521 2217 HOH   HOH A . 
Z  11 HOH   1122 2522 1831 HOH   HOH A . 
Z  11 HOH   1123 2523 1869 HOH   HOH A . 
Z  11 HOH   1124 2524 1383 HOH   HOH A . 
Z  11 HOH   1125 2525 1231 HOH   HOH A . 
Z  11 HOH   1126 2526 878  HOH   HOH A . 
Z  11 HOH   1127 2527 1848 HOH   HOH A . 
Z  11 HOH   1128 2528 1817 HOH   HOH A . 
Z  11 HOH   1129 2529 2375 HOH   HOH A . 
Z  11 HOH   1130 2530 1779 HOH   HOH A . 
Z  11 HOH   1131 2531 1747 HOH   HOH A . 
Z  11 HOH   1132 2532 1666 HOH   HOH A . 
Z  11 HOH   1133 2533 618  HOH   HOH A . 
Z  11 HOH   1134 2534 2406 HOH   HOH A . 
Z  11 HOH   1135 2535 962  HOH   HOH A . 
Z  11 HOH   1136 2536 2107 HOH   HOH A . 
Z  11 HOH   1137 2537 1782 HOH   HOH A . 
Z  11 HOH   1138 2538 1001 HOH   HOH A . 
Z  11 HOH   1139 2539 225  HOH   HOH A . 
Z  11 HOH   1140 2540 2074 HOH   HOH A . 
Z  11 HOH   1141 2541 1100 HOH   HOH A . 
Z  11 HOH   1142 2542 1781 HOH   HOH A . 
Z  11 HOH   1143 2543 1673 HOH   HOH A . 
Z  11 HOH   1144 2544 1585 HOH   HOH A . 
Z  11 HOH   1145 2545 1225 HOH   HOH A . 
Z  11 HOH   1146 2546 1547 HOH   HOH A . 
Z  11 HOH   1147 2547 2363 HOH   HOH A . 
Z  11 HOH   1148 2548 1108 HOH   HOH A . 
Z  11 HOH   1149 2549 1892 HOH   HOH A . 
Z  11 HOH   1150 2550 2145 HOH   HOH A . 
Z  11 HOH   1151 2551 1643 HOH   HOH A . 
Z  11 HOH   1152 2552 697  HOH   HOH A . 
Z  11 HOH   1153 2553 2109 HOH   HOH A . 
Z  11 HOH   1154 2554 1456 HOH   HOH A . 
Z  11 HOH   1155 2555 1147 HOH   HOH A . 
Z  11 HOH   1156 2556 2017 HOH   HOH A . 
Z  11 HOH   1157 2557 1677 HOH   HOH A . 
Z  11 HOH   1158 2558 1347 HOH   HOH A . 
Z  11 HOH   1159 2559 1492 HOH   HOH A . 
Z  11 HOH   1160 2560 979  HOH   HOH A . 
Z  11 HOH   1161 2561 2407 HOH   HOH A . 
Z  11 HOH   1162 2562 1593 HOH   HOH A . 
Z  11 HOH   1163 2563 1142 HOH   HOH A . 
Z  11 HOH   1164 2564 2317 HOH   HOH A . 
Z  11 HOH   1165 2565 1879 HOH   HOH A . 
Z  11 HOH   1166 2566 1745 HOH   HOH A . 
Z  11 HOH   1167 2567 1891 HOH   HOH A . 
Z  11 HOH   1168 2568 850  HOH   HOH A . 
Z  11 HOH   1169 2569 2184 HOH   HOH A . 
Z  11 HOH   1170 2570 2127 HOH   HOH A . 
Z  11 HOH   1171 2571 1785 HOH   HOH A . 
Z  11 HOH   1172 2572 1536 HOH   HOH A . 
Z  11 HOH   1173 2573 1244 HOH   HOH A . 
Z  11 HOH   1174 2574 1106 HOH   HOH A . 
Z  11 HOH   1175 2575 2241 HOH   HOH A . 
Z  11 HOH   1176 2576 1652 HOH   HOH A . 
Z  11 HOH   1177 2577 1800 HOH   HOH A . 
Z  11 HOH   1178 2578 2048 HOH   HOH A . 
Z  11 HOH   1179 2579 1584 HOH   HOH A . 
Z  11 HOH   1180 2580 1752 HOH   HOH A . 
Z  11 HOH   1181 2581 2281 HOH   HOH A . 
Z  11 HOH   1182 2582 2169 HOH   HOH A . 
Z  11 HOH   1183 2583 1874 HOH   HOH A . 
Z  11 HOH   1184 2584 1718 HOH   HOH A . 
Z  11 HOH   1185 2585 1192 HOH   HOH A . 
Z  11 HOH   1186 2586 1223 HOH   HOH A . 
Z  11 HOH   1187 2587 1401 HOH   HOH A . 
Z  11 HOH   1188 2588 1703 HOH   HOH A . 
Z  11 HOH   1189 2589 1590 HOH   HOH A . 
Z  11 HOH   1190 2590 2105 HOH   HOH A . 
Z  11 HOH   1191 2591 1047 HOH   HOH A . 
Z  11 HOH   1192 2592 1559 HOH   HOH A . 
Z  11 HOH   1193 2593 2441 HOH   HOH A . 
Z  11 HOH   1194 2594 2106 HOH   HOH A . 
Z  11 HOH   1195 2595 2175 HOH   HOH A . 
Z  11 HOH   1196 2596 1349 HOH   HOH A . 
Z  11 HOH   1197 2597 1700 HOH   HOH A . 
Z  11 HOH   1198 2598 1341 HOH   HOH A . 
Z  11 HOH   1199 2599 2191 HOH   HOH A . 
Z  11 HOH   1200 2600 1751 HOH   HOH A . 
AA 11 HOH   1    1401 2002 HOH   HOH B . 
AA 11 HOH   2    1402 1576 HOH   HOH B . 
AA 11 HOH   3    1403 1550 HOH   HOH B . 
AA 11 HOH   4    1404 2446 HOH   HOH B . 
AA 11 HOH   5    1405 1738 HOH   HOH B . 
AA 11 HOH   6    1406 1179 HOH   HOH B . 
AA 11 HOH   7    1407 2360 HOH   HOH B . 
AA 11 HOH   8    1408 739  HOH   HOH B . 
AA 11 HOH   9    1409 2264 HOH   HOH B . 
AA 11 HOH   10   1410 2087 HOH   HOH B . 
AA 11 HOH   11   1411 1136 HOH   HOH B . 
AA 11 HOH   12   1412 647  HOH   HOH B . 
AA 11 HOH   13   1413 2080 HOH   HOH B . 
AA 11 HOH   14   1414 1353 HOH   HOH B . 
AA 11 HOH   15   1415 846  HOH   HOH B . 
AA 11 HOH   16   1416 2279 HOH   HOH B . 
AA 11 HOH   17   1417 1784 HOH   HOH B . 
AA 11 HOH   18   1418 1054 HOH   HOH B . 
AA 11 HOH   19   1419 774  HOH   HOH B . 
AA 11 HOH   20   1420 2181 HOH   HOH B . 
AA 11 HOH   21   1421 810  HOH   HOH B . 
AA 11 HOH   22   1422 1451 HOH   HOH B . 
AA 11 HOH   23   1423 2455 HOH   HOH B . 
AA 11 HOH   24   1424 1378 HOH   HOH B . 
AA 11 HOH   25   1425 2209 HOH   HOH B . 
AA 11 HOH   26   1426 1406 HOH   HOH B . 
AA 11 HOH   27   1427 103  HOH   HOH B . 
AA 11 HOH   28   1428 1426 HOH   HOH B . 
AA 11 HOH   29   1429 2069 HOH   HOH B . 
AA 11 HOH   30   1430 2400 HOH   HOH B . 
AA 11 HOH   31   1431 2345 HOH   HOH B . 
AA 11 HOH   32   1432 1057 HOH   HOH B . 
AA 11 HOH   33   1433 1338 HOH   HOH B . 
AA 11 HOH   34   1434 2391 HOH   HOH B . 
AA 11 HOH   35   1435 1496 HOH   HOH B . 
AA 11 HOH   36   1436 1942 HOH   HOH B . 
AA 11 HOH   37   1437 1193 HOH   HOH B . 
AA 11 HOH   38   1438 606  HOH   HOH B . 
AA 11 HOH   39   1439 317  HOH   HOH B . 
AA 11 HOH   40   1440 450  HOH   HOH B . 
AA 11 HOH   41   1441 1155 HOH   HOH B . 
AA 11 HOH   42   1442 542  HOH   HOH B . 
AA 11 HOH   43   1443 975  HOH   HOH B . 
AA 11 HOH   44   1444 1198 HOH   HOH B . 
AA 11 HOH   45   1445 657  HOH   HOH B . 
AA 11 HOH   46   1446 830  HOH   HOH B . 
AA 11 HOH   47   1447 1005 HOH   HOH B . 
AA 11 HOH   48   1448 2183 HOH   HOH B . 
AA 11 HOH   49   1449 47   HOH   HOH B . 
AA 11 HOH   50   1450 1363 HOH   HOH B . 
AA 11 HOH   51   1451 1237 HOH   HOH B . 
AA 11 HOH   52   1452 442  HOH   HOH B . 
AA 11 HOH   53   1453 1400 HOH   HOH B . 
AA 11 HOH   54   1454 1317 HOH   HOH B . 
AA 11 HOH   55   1455 1824 HOH   HOH B . 
AA 11 HOH   56   1456 1091 HOH   HOH B . 
AA 11 HOH   57   1457 1438 HOH   HOH B . 
AA 11 HOH   58   1458 1495 HOH   HOH B . 
AA 11 HOH   59   1459 89   HOH   HOH B . 
AA 11 HOH   60   1460 242  HOH   HOH B . 
AA 11 HOH   61   1461 629  HOH   HOH B . 
AA 11 HOH   62   1462 555  HOH   HOH B . 
AA 11 HOH   63   1463 1749 HOH   HOH B . 
AA 11 HOH   64   1464 1297 HOH   HOH B . 
AA 11 HOH   65   1465 374  HOH   HOH B . 
AA 11 HOH   66   1466 2041 HOH   HOH B . 
AA 11 HOH   67   1467 1783 HOH   HOH B . 
AA 11 HOH   68   1468 45   HOH   HOH B . 
AA 11 HOH   69   1469 408  HOH   HOH B . 
AA 11 HOH   70   1470 2275 HOH   HOH B . 
AA 11 HOH   71   1471 265  HOH   HOH B . 
AA 11 HOH   72   1472 1062 HOH   HOH B . 
AA 11 HOH   73   1473 2194 HOH   HOH B . 
AA 11 HOH   74   1474 2290 HOH   HOH B . 
AA 11 HOH   75   1475 308  HOH   HOH B . 
AA 11 HOH   76   1476 557  HOH   HOH B . 
AA 11 HOH   77   1477 338  HOH   HOH B . 
AA 11 HOH   78   1478 434  HOH   HOH B . 
AA 11 HOH   79   1479 291  HOH   HOH B . 
AA 11 HOH   80   1480 1934 HOH   HOH B . 
AA 11 HOH   81   1481 988  HOH   HOH B . 
AA 11 HOH   82   1482 1517 HOH   HOH B . 
AA 11 HOH   83   1483 1344 HOH   HOH B . 
AA 11 HOH   84   1484 508  HOH   HOH B . 
AA 11 HOH   85   1485 2211 HOH   HOH B . 
AA 11 HOH   86   1486 404  HOH   HOH B . 
AA 11 HOH   87   1487 620  HOH   HOH B . 
AA 11 HOH   88   1488 903  HOH   HOH B . 
AA 11 HOH   89   1489 2193 HOH   HOH B . 
AA 11 HOH   90   1490 2306 HOH   HOH B . 
AA 11 HOH   91   1491 1656 HOH   HOH B . 
AA 11 HOH   92   1492 10   HOH   HOH B . 
AA 11 HOH   93   1493 2152 HOH   HOH B . 
AA 11 HOH   94   1494 2368 HOH   HOH B . 
AA 11 HOH   95   1495 387  HOH   HOH B . 
AA 11 HOH   96   1496 63   HOH   HOH B . 
AA 11 HOH   97   1497 2448 HOH   HOH B . 
AA 11 HOH   98   1498 15   HOH   HOH B . 
AA 11 HOH   99   1499 1941 HOH   HOH B . 
AA 11 HOH   100  1500 392  HOH   HOH B . 
AA 11 HOH   101  1501 723  HOH   HOH B . 
AA 11 HOH   102  1502 925  HOH   HOH B . 
AA 11 HOH   103  1503 526  HOH   HOH B . 
AA 11 HOH   104  1504 510  HOH   HOH B . 
AA 11 HOH   105  1505 102  HOH   HOH B . 
AA 11 HOH   106  1506 828  HOH   HOH B . 
AA 11 HOH   107  1507 1150 HOH   HOH B . 
AA 11 HOH   108  1508 2235 HOH   HOH B . 
AA 11 HOH   109  1509 490  HOH   HOH B . 
AA 11 HOH   110  1510 930  HOH   HOH B . 
AA 11 HOH   111  1511 337  HOH   HOH B . 
AA 11 HOH   112  1512 786  HOH   HOH B . 
AA 11 HOH   113  1513 1405 HOH   HOH B . 
AA 11 HOH   114  1514 152  HOH   HOH B . 
AA 11 HOH   115  1515 1369 HOH   HOH B . 
AA 11 HOH   116  1516 1665 HOH   HOH B . 
AA 11 HOH   117  1517 46   HOH   HOH B . 
AA 11 HOH   118  1518 715  HOH   HOH B . 
AA 11 HOH   119  1519 801  HOH   HOH B . 
AA 11 HOH   120  1520 824  HOH   HOH B . 
AA 11 HOH   121  1521 1472 HOH   HOH B . 
AA 11 HOH   122  1522 730  HOH   HOH B . 
AA 11 HOH   123  1523 800  HOH   HOH B . 
AA 11 HOH   124  1524 397  HOH   HOH B . 
AA 11 HOH   125  1525 114  HOH   HOH B . 
AA 11 HOH   126  1526 319  HOH   HOH B . 
AA 11 HOH   127  1527 864  HOH   HOH B . 
AA 11 HOH   128  1528 281  HOH   HOH B . 
AA 11 HOH   129  1529 875  HOH   HOH B . 
AA 11 HOH   130  1530 1318 HOH   HOH B . 
AA 11 HOH   131  1531 224  HOH   HOH B . 
AA 11 HOH   132  1532 26   HOH   HOH B . 
AA 11 HOH   133  1533 2334 HOH   HOH B . 
AA 11 HOH   134  1534 673  HOH   HOH B . 
AA 11 HOH   135  1535 1285 HOH   HOH B . 
AA 11 HOH   136  1536 252  HOH   HOH B . 
AA 11 HOH   137  1537 320  HOH   HOH B . 
AA 11 HOH   138  1538 1775 HOH   HOH B . 
AA 11 HOH   139  1539 1629 HOH   HOH B . 
AA 11 HOH   140  1540 277  HOH   HOH B . 
AA 11 HOH   141  1541 1867 HOH   HOH B . 
AA 11 HOH   142  1542 292  HOH   HOH B . 
AA 11 HOH   143  1543 143  HOH   HOH B . 
AA 11 HOH   144  1544 283  HOH   HOH B . 
AA 11 HOH   145  1545 1948 HOH   HOH B . 
AA 11 HOH   146  1546 1043 HOH   HOH B . 
AA 11 HOH   147  1547 446  HOH   HOH B . 
AA 11 HOH   148  1548 1137 HOH   HOH B . 
AA 11 HOH   149  1549 1275 HOH   HOH B . 
AA 11 HOH   150  1550 230  HOH   HOH B . 
AA 11 HOH   151  1551 1712 HOH   HOH B . 
AA 11 HOH   152  1552 1302 HOH   HOH B . 
AA 11 HOH   153  1553 326  HOH   HOH B . 
AA 11 HOH   154  1554 1042 HOH   HOH B . 
AA 11 HOH   155  1555 1731 HOH   HOH B . 
AA 11 HOH   156  1556 615  HOH   HOH B . 
AA 11 HOH   157  1557 929  HOH   HOH B . 
AA 11 HOH   158  1558 1109 HOH   HOH B . 
AA 11 HOH   159  1559 383  HOH   HOH B . 
AA 11 HOH   160  1560 2031 HOH   HOH B . 
AA 11 HOH   161  1561 33   HOH   HOH B . 
AA 11 HOH   162  1562 2014 HOH   HOH B . 
AA 11 HOH   163  1563 2154 HOH   HOH B . 
AA 11 HOH   164  1564 1055 HOH   HOH B . 
AA 11 HOH   165  1565 1940 HOH   HOH B . 
AA 11 HOH   166  1566 799  HOH   HOH B . 
AA 11 HOH   167  1567 149  HOH   HOH B . 
AA 11 HOH   168  1568 117  HOH   HOH B . 
AA 11 HOH   169  1569 1436 HOH   HOH B . 
AA 11 HOH   170  1570 120  HOH   HOH B . 
AA 11 HOH   171  1571 379  HOH   HOH B . 
AA 11 HOH   172  1572 1361 HOH   HOH B . 
AA 11 HOH   173  1573 377  HOH   HOH B . 
AA 11 HOH   174  1574 1265 HOH   HOH B . 
AA 11 HOH   175  1575 2035 HOH   HOH B . 
AA 11 HOH   176  1576 300  HOH   HOH B . 
AA 11 HOH   177  1577 421  HOH   HOH B . 
AA 11 HOH   178  1578 1591 HOH   HOH B . 
AA 11 HOH   179  1579 798  HOH   HOH B . 
AA 11 HOH   180  1580 1833 HOH   HOH B . 
AA 11 HOH   181  1581 577  HOH   HOH B . 
AA 11 HOH   182  1582 452  HOH   HOH B . 
AA 11 HOH   183  1583 1963 HOH   HOH B . 
AA 11 HOH   184  1584 318  HOH   HOH B . 
AA 11 HOH   185  1585 1915 HOH   HOH B . 
AA 11 HOH   186  1586 1636 HOH   HOH B . 
AA 11 HOH   187  1587 607  HOH   HOH B . 
AA 11 HOH   188  1588 1377 HOH   HOH B . 
AA 11 HOH   189  1589 197  HOH   HOH B . 
AA 11 HOH   190  1590 1600 HOH   HOH B . 
AA 11 HOH   191  1591 2358 HOH   HOH B . 
AA 11 HOH   192  1592 1925 HOH   HOH B . 
AA 11 HOH   193  1593 989  HOH   HOH B . 
AA 11 HOH   194  1594 815  HOH   HOH B . 
AA 11 HOH   195  1595 463  HOH   HOH B . 
AA 11 HOH   196  1596 19   HOH   HOH B . 
AA 11 HOH   197  1597 881  HOH   HOH B . 
AA 11 HOH   198  1598 2336 HOH   HOH B . 
AA 11 HOH   199  1599 11   HOH   HOH B . 
AA 11 HOH   200  1600 2140 HOH   HOH B . 
AA 11 HOH   201  1601 202  HOH   HOH B . 
AA 11 HOH   202  1602 1885 HOH   HOH B . 
AA 11 HOH   203  1603 2121 HOH   HOH B . 
AA 11 HOH   204  1604 243  HOH   HOH B . 
AA 11 HOH   205  1605 1311 HOH   HOH B . 
AA 11 HOH   206  1606 1549 HOH   HOH B . 
AA 11 HOH   207  1607 1296 HOH   HOH B . 
AA 11 HOH   208  1608 2256 HOH   HOH B . 
AA 11 HOH   209  1609 773  HOH   HOH B . 
AA 11 HOH   210  1610 635  HOH   HOH B . 
AA 11 HOH   211  1611 1577 HOH   HOH B . 
AA 11 HOH   212  1612 248  HOH   HOH B . 
AA 11 HOH   213  1613 551  HOH   HOH B . 
AA 11 HOH   214  1614 1506 HOH   HOH B . 
AA 11 HOH   215  1615 1051 HOH   HOH B . 
AA 11 HOH   216  1616 464  HOH   HOH B . 
AA 11 HOH   217  1617 110  HOH   HOH B . 
AA 11 HOH   218  1618 871  HOH   HOH B . 
AA 11 HOH   219  1619 2408 HOH   HOH B . 
AA 11 HOH   220  1620 488  HOH   HOH B . 
AA 11 HOH   221  1621 330  HOH   HOH B . 
AA 11 HOH   222  1622 81   HOH   HOH B . 
AA 11 HOH   223  1623 662  HOH   HOH B . 
AA 11 HOH   224  1624 340  HOH   HOH B . 
AA 11 HOH   225  1625 2314 HOH   HOH B . 
AA 11 HOH   226  1626 236  HOH   HOH B . 
AA 11 HOH   227  1627 105  HOH   HOH B . 
AA 11 HOH   228  1628 276  HOH   HOH B . 
AA 11 HOH   229  1629 1293 HOH   HOH B . 
AA 11 HOH   230  1630 497  HOH   HOH B . 
AA 11 HOH   231  1631 1190 HOH   HOH B . 
AA 11 HOH   232  1632 366  HOH   HOH B . 
AA 11 HOH   233  1633 820  HOH   HOH B . 
AA 11 HOH   234  1634 287  HOH   HOH B . 
AA 11 HOH   235  1635 234  HOH   HOH B . 
AA 11 HOH   236  1636 1082 HOH   HOH B . 
AA 11 HOH   237  1637 1146 HOH   HOH B . 
AA 11 HOH   238  1638 1097 HOH   HOH B . 
AA 11 HOH   239  1639 9    HOH   HOH B . 
AA 11 HOH   240  1640 545  HOH   HOH B . 
AA 11 HOH   241  1641 359  HOH   HOH B . 
AA 11 HOH   242  1642 637  HOH   HOH B . 
AA 11 HOH   243  1643 1111 HOH   HOH B . 
AA 11 HOH   244  1644 50   HOH   HOH B . 
AA 11 HOH   245  1645 411  HOH   HOH B . 
AA 11 HOH   246  1646 212  HOH   HOH B . 
AA 11 HOH   247  1647 802  HOH   HOH B . 
AA 11 HOH   248  1648 565  HOH   HOH B . 
AA 11 HOH   249  1649 22   HOH   HOH B . 
AA 11 HOH   250  1650 441  HOH   HOH B . 
AA 11 HOH   251  1651 1355 HOH   HOH B . 
AA 11 HOH   252  1652 153  HOH   HOH B . 
AA 11 HOH   253  1653 134  HOH   HOH B . 
AA 11 HOH   254  1654 74   HOH   HOH B . 
AA 11 HOH   255  1655 179  HOH   HOH B . 
AA 11 HOH   256  1656 835  HOH   HOH B . 
AA 11 HOH   257  1657 7    HOH   HOH B . 
AA 11 HOH   258  1658 1936 HOH   HOH B . 
AA 11 HOH   259  1659 1730 HOH   HOH B . 
AA 11 HOH   260  1660 1583 HOH   HOH B . 
AA 11 HOH   261  1661 525  HOH   HOH B . 
AA 11 HOH   262  1662 980  HOH   HOH B . 
AA 11 HOH   263  1663 768  HOH   HOH B . 
AA 11 HOH   264  1664 1968 HOH   HOH B . 
AA 11 HOH   265  1665 239  HOH   HOH B . 
AA 11 HOH   266  1666 438  HOH   HOH B . 
AA 11 HOH   267  1667 1720 HOH   HOH B . 
AA 11 HOH   268  1668 2412 HOH   HOH B . 
AA 11 HOH   269  1669 2122 HOH   HOH B . 
AA 11 HOH   270  1670 643  HOH   HOH B . 
AA 11 HOH   271  1671 229  HOH   HOH B . 
AA 11 HOH   272  1672 183  HOH   HOH B . 
AA 11 HOH   273  1673 1224 HOH   HOH B . 
AA 11 HOH   274  1674 77   HOH   HOH B . 
AA 11 HOH   275  1675 1964 HOH   HOH B . 
AA 11 HOH   276  1676 862  HOH   HOH B . 
AA 11 HOH   277  1677 49   HOH   HOH B . 
AA 11 HOH   278  1678 1253 HOH   HOH B . 
AA 11 HOH   279  1679 652  HOH   HOH B . 
AA 11 HOH   280  1680 295  HOH   HOH B . 
AA 11 HOH   281  1681 1151 HOH   HOH B . 
AA 11 HOH   282  1682 1622 HOH   HOH B . 
AA 11 HOH   283  1683 349  HOH   HOH B . 
AA 11 HOH   284  1684 889  HOH   HOH B . 
AA 11 HOH   285  1685 116  HOH   HOH B . 
AA 11 HOH   286  1686 1039 HOH   HOH B . 
AA 11 HOH   287  1687 1443 HOH   HOH B . 
AA 11 HOH   288  1688 469  HOH   HOH B . 
AA 11 HOH   289  1689 1391 HOH   HOH B . 
AA 11 HOH   290  1690 757  HOH   HOH B . 
AA 11 HOH   291  1691 1647 HOH   HOH B . 
AA 11 HOH   292  1692 17   HOH   HOH B . 
AA 11 HOH   293  1693 1605 HOH   HOH B . 
AA 11 HOH   294  1694 211  HOH   HOH B . 
AA 11 HOH   295  1695 170  HOH   HOH B . 
AA 11 HOH   296  1696 733  HOH   HOH B . 
AA 11 HOH   297  1697 1128 HOH   HOH B . 
AA 11 HOH   298  1698 1612 HOH   HOH B . 
AA 11 HOH   299  1699 1681 HOH   HOH B . 
AA 11 HOH   300  1700 487  HOH   HOH B . 
AA 11 HOH   301  1701 186  HOH   HOH B . 
AA 11 HOH   302  1702 141  HOH   HOH B . 
AA 11 HOH   303  1703 571  HOH   HOH B . 
AA 11 HOH   304  1704 1578 HOH   HOH B . 
AA 11 HOH   305  1705 1243 HOH   HOH B . 
AA 11 HOH   306  1706 140  HOH   HOH B . 
AA 11 HOH   307  1707 1069 HOH   HOH B . 
AA 11 HOH   308  1708 865  HOH   HOH B . 
AA 11 HOH   309  1709 974  HOH   HOH B . 
AA 11 HOH   310  1710 16   HOH   HOH B . 
AA 11 HOH   311  1711 355  HOH   HOH B . 
AA 11 HOH   312  1712 1560 HOH   HOH B . 
AA 11 HOH   313  1713 513  HOH   HOH B . 
AA 11 HOH   314  1714 556  HOH   HOH B . 
AA 11 HOH   315  1715 1707 HOH   HOH B . 
AA 11 HOH   316  1716 232  HOH   HOH B . 
AA 11 HOH   317  1717 521  HOH   HOH B . 
AA 11 HOH   318  1718 1102 HOH   HOH B . 
AA 11 HOH   319  1719 645  HOH   HOH B . 
AA 11 HOH   320  1720 99   HOH   HOH B . 
AA 11 HOH   321  1721 1234 HOH   HOH B . 
AA 11 HOH   322  1722 382  HOH   HOH B . 
AA 11 HOH   323  1723 178  HOH   HOH B . 
AA 11 HOH   324  1724 353  HOH   HOH B . 
AA 11 HOH   325  1725 866  HOH   HOH B . 
AA 11 HOH   326  1726 632  HOH   HOH B . 
AA 11 HOH   327  1727 626  HOH   HOH B . 
AA 11 HOH   328  1728 182  HOH   HOH B . 
AA 11 HOH   329  1729 2253 HOH   HOH B . 
AA 11 HOH   330  1730 994  HOH   HOH B . 
AA 11 HOH   331  1731 567  HOH   HOH B . 
AA 11 HOH   332  1732 575  HOH   HOH B . 
AA 11 HOH   333  1733 158  HOH   HOH B . 
AA 11 HOH   334  1734 129  HOH   HOH B . 
AA 11 HOH   335  1735 220  HOH   HOH B . 
AA 11 HOH   336  1736 2086 HOH   HOH B . 
AA 11 HOH   337  1737 901  HOH   HOH B . 
AA 11 HOH   338  1738 57   HOH   HOH B . 
AA 11 HOH   339  1739 1791 HOH   HOH B . 
AA 11 HOH   340  1740 357  HOH   HOH B . 
AA 11 HOH   341  1741 290  HOH   HOH B . 
AA 11 HOH   342  1742 498  HOH   HOH B . 
AA 11 HOH   343  1743 1    HOH   HOH B . 
AA 11 HOH   344  1744 625  HOH   HOH B . 
AA 11 HOH   345  1745 237  HOH   HOH B . 
AA 11 HOH   346  1746 6    HOH   HOH B . 
AA 11 HOH   347  1747 1404 HOH   HOH B . 
AA 11 HOH   348  1748 754  HOH   HOH B . 
AA 11 HOH   349  1749 95   HOH   HOH B . 
AA 11 HOH   350  1750 58   HOH   HOH B . 
AA 11 HOH   351  1751 1845 HOH   HOH B . 
AA 11 HOH   352  1752 1129 HOH   HOH B . 
AA 11 HOH   353  1753 1065 HOH   HOH B . 
AA 11 HOH   354  1754 2396 HOH   HOH B . 
AA 11 HOH   355  1755 70   HOH   HOH B . 
AA 11 HOH   356  1756 303  HOH   HOH B . 
AA 11 HOH   357  1757 381  HOH   HOH B . 
AA 11 HOH   358  1758 596  HOH   HOH B . 
AA 11 HOH   359  1759 2266 HOH   HOH B . 
AA 11 HOH   360  1760 503  HOH   HOH B . 
AA 11 HOH   361  1761 335  HOH   HOH B . 
AA 11 HOH   362  1762 2276 HOH   HOH B . 
AA 11 HOH   363  1763 1215 HOH   HOH B . 
AA 11 HOH   364  1764 1251 HOH   HOH B . 
AA 11 HOH   365  1765 28   HOH   HOH B . 
AA 11 HOH   366  1766 311  HOH   HOH B . 
AA 11 HOH   367  1767 32   HOH   HOH B . 
AA 11 HOH   368  1768 535  HOH   HOH B . 
AA 11 HOH   369  1769 4    HOH   HOH B . 
AA 11 HOH   370  1770 422  HOH   HOH B . 
AA 11 HOH   371  1771 1026 HOH   HOH B . 
AA 11 HOH   372  1772 1646 HOH   HOH B . 
AA 11 HOH   373  1773 384  HOH   HOH B . 
AA 11 HOH   374  1774 797  HOH   HOH B . 
AA 11 HOH   375  1775 13   HOH   HOH B . 
AA 11 HOH   376  1776 195  HOH   HOH B . 
AA 11 HOH   377  1777 653  HOH   HOH B . 
AA 11 HOH   378  1778 1609 HOH   HOH B . 
AA 11 HOH   379  1779 2    HOH   HOH B . 
AA 11 HOH   380  1780 67   HOH   HOH B . 
AA 11 HOH   381  1781 139  HOH   HOH B . 
AA 11 HOH   382  1782 1308 HOH   HOH B . 
AA 11 HOH   383  1783 928  HOH   HOH B . 
AA 11 HOH   384  1784 2294 HOH   HOH B . 
AA 11 HOH   385  1785 681  HOH   HOH B . 
AA 11 HOH   386  1786 941  HOH   HOH B . 
AA 11 HOH   387  1787 1323 HOH   HOH B . 
AA 11 HOH   388  1788 985  HOH   HOH B . 
AA 11 HOH   389  1789 223  HOH   HOH B . 
AA 11 HOH   390  1790 689  HOH   HOH B . 
AA 11 HOH   391  1791 354  HOH   HOH B . 
AA 11 HOH   392  1792 873  HOH   HOH B . 
AA 11 HOH   393  1793 1486 HOH   HOH B . 
AA 11 HOH   394  1794 250  HOH   HOH B . 
AA 11 HOH   395  1795 48   HOH   HOH B . 
AA 11 HOH   396  1796 1122 HOH   HOH B . 
AA 11 HOH   397  1797 780  HOH   HOH B . 
AA 11 HOH   398  1798 1080 HOH   HOH B . 
AA 11 HOH   399  1799 65   HOH   HOH B . 
AA 11 HOH   400  1800 38   HOH   HOH B . 
AA 11 HOH   401  1801 776  HOH   HOH B . 
AA 11 HOH   402  1802 1255 HOH   HOH B . 
AA 11 HOH   403  1803 85   HOH   HOH B . 
AA 11 HOH   404  1804 659  HOH   HOH B . 
AA 11 HOH   405  1805 2126 HOH   HOH B . 
AA 11 HOH   406  1806 546  HOH   HOH B . 
AA 11 HOH   407  1807 122  HOH   HOH B . 
AA 11 HOH   408  1808 816  HOH   HOH B . 
AA 11 HOH   409  1809 848  HOH   HOH B . 
AA 11 HOH   410  1810 1810 HOH   HOH B . 
AA 11 HOH   411  1811 1565 HOH   HOH B . 
AA 11 HOH   412  1812 1229 HOH   HOH B . 
AA 11 HOH   413  1813 310  HOH   HOH B . 
AA 11 HOH   414  1814 676  HOH   HOH B . 
AA 11 HOH   415  1815 1032 HOH   HOH B . 
AA 11 HOH   416  1816 704  HOH   HOH B . 
AA 11 HOH   417  1817 1518 HOH   HOH B . 
AA 11 HOH   418  1818 639  HOH   HOH B . 
AA 11 HOH   419  1819 101  HOH   HOH B . 
AA 11 HOH   420  1820 482  HOH   HOH B . 
AA 11 HOH   421  1821 844  HOH   HOH B . 
AA 11 HOH   422  1822 494  HOH   HOH B . 
AA 11 HOH   423  1823 336  HOH   HOH B . 
AA 11 HOH   424  1824 667  HOH   HOH B . 
AA 11 HOH   425  1825 8    HOH   HOH B . 
AA 11 HOH   426  1826 2162 HOH   HOH B . 
AA 11 HOH   427  1827 520  HOH   HOH B . 
AA 11 HOH   428  1828 1786 HOH   HOH B . 
AA 11 HOH   429  1829 1339 HOH   HOH B . 
AA 11 HOH   430  1830 1394 HOH   HOH B . 
AA 11 HOH   431  1831 1280 HOH   HOH B . 
AA 11 HOH   432  1832 1260 HOH   HOH B . 
AA 11 HOH   433  1833 83   HOH   HOH B . 
AA 11 HOH   434  1834 426  HOH   HOH B . 
AA 11 HOH   435  1835 92   HOH   HOH B . 
AA 11 HOH   436  1836 145  HOH   HOH B . 
AA 11 HOH   437  1837 1868 HOH   HOH B . 
AA 11 HOH   438  1838 333  HOH   HOH B . 
AA 11 HOH   439  1839 2443 HOH   HOH B . 
AA 11 HOH   440  1840 177  HOH   HOH B . 
AA 11 HOH   441  1841 368  HOH   HOH B . 
AA 11 HOH   442  1842 2088 HOH   HOH B . 
AA 11 HOH   443  1843 613  HOH   HOH B . 
AA 11 HOH   444  1844 162  HOH   HOH B . 
AA 11 HOH   445  1845 470  HOH   HOH B . 
AA 11 HOH   446  1846 112  HOH   HOH B . 
AA 11 HOH   447  1847 266  HOH   HOH B . 
AA 11 HOH   448  1848 932  HOH   HOH B . 
AA 11 HOH   449  1849 622  HOH   HOH B . 
AA 11 HOH   450  1850 12   HOH   HOH B . 
AA 11 HOH   451  1851 1154 HOH   HOH B . 
AA 11 HOH   452  1852 59   HOH   HOH B . 
AA 11 HOH   453  1853 554  HOH   HOH B . 
AA 11 HOH   454  1854 146  HOH   HOH B . 
AA 11 HOH   455  1855 580  HOH   HOH B . 
AA 11 HOH   456  1856 973  HOH   HOH B . 
AA 11 HOH   457  1857 471  HOH   HOH B . 
AA 11 HOH   458  1858 573  HOH   HOH B . 
AA 11 HOH   459  1859 833  HOH   HOH B . 
AA 11 HOH   460  1860 181  HOH   HOH B . 
AA 11 HOH   461  1861 899  HOH   HOH B . 
AA 11 HOH   462  1862 997  HOH   HOH B . 
AA 11 HOH   463  1863 1924 HOH   HOH B . 
AA 11 HOH   464  1864 1938 HOH   HOH B . 
AA 11 HOH   465  1865 628  HOH   HOH B . 
AA 11 HOH   466  1866 2328 HOH   HOH B . 
AA 11 HOH   467  1867 1048 HOH   HOH B . 
AA 11 HOH   468  1868 431  HOH   HOH B . 
AA 11 HOH   469  1869 1669 HOH   HOH B . 
AA 11 HOH   470  1870 188  HOH   HOH B . 
AA 11 HOH   471  1871 872  HOH   HOH B . 
AA 11 HOH   472  1872 68   HOH   HOH B . 
AA 11 HOH   473  1873 755  HOH   HOH B . 
AA 11 HOH   474  1874 1235 HOH   HOH B . 
AA 11 HOH   475  1875 1966 HOH   HOH B . 
AA 11 HOH   476  1876 769  HOH   HOH B . 
AA 11 HOH   477  1877 313  HOH   HOH B . 
AA 11 HOH   478  1878 279  HOH   HOH B . 
AA 11 HOH   479  1879 115  HOH   HOH B . 
AA 11 HOH   480  1880 400  HOH   HOH B . 
AA 11 HOH   481  1881 56   HOH   HOH B . 
AA 11 HOH   482  1882 315  HOH   HOH B . 
AA 11 HOH   483  1883 1813 HOH   HOH B . 
AA 11 HOH   484  1884 849  HOH   HOH B . 
AA 11 HOH   485  1885 254  HOH   HOH B . 
AA 11 HOH   486  1886 855  HOH   HOH B . 
AA 11 HOH   487  1887 121  HOH   HOH B . 
AA 11 HOH   488  1888 210  HOH   HOH B . 
AA 11 HOH   489  1889 1178 HOH   HOH B . 
AA 11 HOH   490  1890 278  HOH   HOH B . 
AA 11 HOH   491  1891 334  HOH   HOH B . 
AA 11 HOH   492  1892 1168 HOH   HOH B . 
AA 11 HOH   493  1893 64   HOH   HOH B . 
AA 11 HOH   494  1894 690  HOH   HOH B . 
AA 11 HOH   495  1895 2415 HOH   HOH B . 
AA 11 HOH   496  1896 1410 HOH   HOH B . 
AA 11 HOH   497  1897 1003 HOH   HOH B . 
AA 11 HOH   498  1898 1741 HOH   HOH B . 
AA 11 HOH   499  1899 2150 HOH   HOH B . 
AA 11 HOH   500  1900 1575 HOH   HOH B . 
AA 11 HOH   501  1901 2022 HOH   HOH B . 
AA 11 HOH   502  1902 339  HOH   HOH B . 
AA 11 HOH   503  1903 942  HOH   HOH B . 
AA 11 HOH   504  1904 1356 HOH   HOH B . 
AA 11 HOH   505  1905 703  HOH   HOH B . 
AA 11 HOH   506  1906 1659 HOH   HOH B . 
AA 11 HOH   507  1907 53   HOH   HOH B . 
AA 11 HOH   508  1908 247  HOH   HOH B . 
AA 11 HOH   509  1909 2419 HOH   HOH B . 
AA 11 HOH   510  1910 1890 HOH   HOH B . 
AA 11 HOH   511  1911 351  HOH   HOH B . 
AA 11 HOH   512  1912 1306 HOH   HOH B . 
AA 11 HOH   513  1913 1059 HOH   HOH B . 
AA 11 HOH   514  1914 98   HOH   HOH B . 
AA 11 HOH   515  1915 412  HOH   HOH B . 
AA 11 HOH   516  1916 1089 HOH   HOH B . 
AA 11 HOH   517  1917 1230 HOH   HOH B . 
AA 11 HOH   518  1918 2201 HOH   HOH B . 
AA 11 HOH   519  1919 504  HOH   HOH B . 
AA 11 HOH   520  1920 861  HOH   HOH B . 
AA 11 HOH   521  1921 882  HOH   HOH B . 
AA 11 HOH   522  1922 812  HOH   HOH B . 
AA 11 HOH   523  1923 2090 HOH   HOH B . 
AA 11 HOH   524  1924 845  HOH   HOH B . 
AA 11 HOH   525  1925 96   HOH   HOH B . 
AA 11 HOH   526  1926 51   HOH   HOH B . 
AA 11 HOH   527  1927 1607 HOH   HOH B . 
AA 11 HOH   528  1928 3    HOH   HOH B . 
AA 11 HOH   529  1929 1962 HOH   HOH B . 
AA 11 HOH   530  1930 764  HOH   HOH B . 
AA 11 HOH   531  1931 583  HOH   HOH B . 
AA 11 HOH   532  1932 1595 HOH   HOH B . 
AA 11 HOH   533  1933 1816 HOH   HOH B . 
AA 11 HOH   534  1934 1052 HOH   HOH B . 
AA 11 HOH   535  1935 131  HOH   HOH B . 
AA 11 HOH   536  1936 638  HOH   HOH B . 
AA 11 HOH   537  1937 1283 HOH   HOH B . 
AA 11 HOH   538  1938 674  HOH   HOH B . 
AA 11 HOH   539  1939 1068 HOH   HOH B . 
AA 11 HOH   540  1940 167  HOH   HOH B . 
AA 11 HOH   541  1941 1877 HOH   HOH B . 
AA 11 HOH   542  1942 711  HOH   HOH B . 
AA 11 HOH   543  1943 1862 HOH   HOH B . 
AA 11 HOH   544  1944 641  HOH   HOH B . 
AA 11 HOH   545  1945 1740 HOH   HOH B . 
AA 11 HOH   546  1946 924  HOH   HOH B . 
AA 11 HOH   547  1947 1724 HOH   HOH B . 
AA 11 HOH   548  1948 462  HOH   HOH B . 
AA 11 HOH   549  1949 253  HOH   HOH B . 
AA 11 HOH   550  1950 687  HOH   HOH B . 
AA 11 HOH   551  1951 312  HOH   HOH B . 
AA 11 HOH   552  1952 60   HOH   HOH B . 
AA 11 HOH   553  1953 675  HOH   HOH B . 
AA 11 HOH   554  1954 950  HOH   HOH B . 
AA 11 HOH   555  1955 1149 HOH   HOH B . 
AA 11 HOH   556  1956 1342 HOH   HOH B . 
AA 11 HOH   557  1957 1692 HOH   HOH B . 
AA 11 HOH   558  1958 1548 HOH   HOH B . 
AA 11 HOH   559  1959 1004 HOH   HOH B . 
AA 11 HOH   560  1960 599  HOH   HOH B . 
AA 11 HOH   561  1961 472  HOH   HOH B . 
AA 11 HOH   562  1962 1737 HOH   HOH B . 
AA 11 HOH   563  1963 1261 HOH   HOH B . 
AA 11 HOH   564  1964 309  HOH   HOH B . 
AA 11 HOH   565  1965 80   HOH   HOH B . 
AA 11 HOH   566  1966 148  HOH   HOH B . 
AA 11 HOH   567  1967 130  HOH   HOH B . 
AA 11 HOH   568  1968 717  HOH   HOH B . 
AA 11 HOH   569  1969 670  HOH   HOH B . 
AA 11 HOH   570  1970 1458 HOH   HOH B . 
AA 11 HOH   571  1971 1711 HOH   HOH B . 
AA 11 HOH   572  1972 877  HOH   HOH B . 
AA 11 HOH   573  1973 759  HOH   HOH B . 
AA 11 HOH   574  1974 443  HOH   HOH B . 
AA 11 HOH   575  1975 1124 HOH   HOH B . 
AA 11 HOH   576  1976 1476 HOH   HOH B . 
AA 11 HOH   577  1977 204  HOH   HOH B . 
AA 11 HOH   578  1978 838  HOH   HOH B . 
AA 11 HOH   579  1979 2138 HOH   HOH B . 
AA 11 HOH   580  1980 1157 HOH   HOH B . 
AA 11 HOH   581  1981 1896 HOH   HOH B . 
AA 11 HOH   582  1982 194  HOH   HOH B . 
AA 11 HOH   583  1983 474  HOH   HOH B . 
AA 11 HOH   584  1984 1540 HOH   HOH B . 
AA 11 HOH   585  1985 1112 HOH   HOH B . 
AA 11 HOH   586  1986 213  HOH   HOH B . 
AA 11 HOH   587  1987 2141 HOH   HOH B . 
AA 11 HOH   588  1988 2223 HOH   HOH B . 
AA 11 HOH   589  1989 1086 HOH   HOH B . 
AA 11 HOH   590  1990 2137 HOH   HOH B . 
AA 11 HOH   591  1991 748  HOH   HOH B . 
AA 11 HOH   592  1992 648  HOH   HOH B . 
AA 11 HOH   593  1993 1676 HOH   HOH B . 
AA 11 HOH   594  1994 119  HOH   HOH B . 
AA 11 HOH   595  1995 2257 HOH   HOH B . 
AA 11 HOH   596  1996 900  HOH   HOH B . 
AA 11 HOH   597  1997 1194 HOH   HOH B . 
AA 11 HOH   598  1998 1832 HOH   HOH B . 
AA 11 HOH   599  1999 251  HOH   HOH B . 
AA 11 HOH   600  2000 2398 HOH   HOH B . 
AA 11 HOH   601  2001 486  HOH   HOH B . 
AA 11 HOH   602  2002 305  HOH   HOH B . 
AA 11 HOH   603  2003 1196 HOH   HOH B . 
AA 11 HOH   604  2004 394  HOH   HOH B . 
AA 11 HOH   605  2005 1449 HOH   HOH B . 
AA 11 HOH   606  2006 725  HOH   HOH B . 
AA 11 HOH   607  2007 2228 HOH   HOH B . 
AA 11 HOH   608  2008 634  HOH   HOH B . 
AA 11 HOH   609  2009 184  HOH   HOH B . 
AA 11 HOH   610  2010 1937 HOH   HOH B . 
AA 11 HOH   611  2011 106  HOH   HOH B . 
AA 11 HOH   612  2012 566  HOH   HOH B . 
AA 11 HOH   613  2013 189  HOH   HOH B . 
AA 11 HOH   614  2014 399  HOH   HOH B . 
AA 11 HOH   615  2015 425  HOH   HOH B . 
AA 11 HOH   616  2016 249  HOH   HOH B . 
AA 11 HOH   617  2017 285  HOH   HOH B . 
AA 11 HOH   618  2018 365  HOH   HOH B . 
AA 11 HOH   619  2019 322  HOH   HOH B . 
AA 11 HOH   620  2020 961  HOH   HOH B . 
AA 11 HOH   621  2021 2042 HOH   HOH B . 
AA 11 HOH   622  2022 892  HOH   HOH B . 
AA 11 HOH   623  2023 912  HOH   HOH B . 
AA 11 HOH   624  2024 390  HOH   HOH B . 
AA 11 HOH   625  2025 244  HOH   HOH B . 
AA 11 HOH   626  2026 198  HOH   HOH B . 
AA 11 HOH   627  2027 1028 HOH   HOH B . 
AA 11 HOH   628  2028 2155 HOH   HOH B . 
AA 11 HOH   629  2029 1362 HOH   HOH B . 
AA 11 HOH   630  2030 1013 HOH   HOH B . 
AA 11 HOH   631  2031 1628 HOH   HOH B . 
AA 11 HOH   632  2032 402  HOH   HOH B . 
AA 11 HOH   633  2033 1407 HOH   HOH B . 
AA 11 HOH   634  2034 5    HOH   HOH B . 
AA 11 HOH   635  2035 1327 HOH   HOH B . 
AA 11 HOH   636  2036 218  HOH   HOH B . 
AA 11 HOH   637  2037 1564 HOH   HOH B . 
AA 11 HOH   638  2038 1746 HOH   HOH B . 
AA 11 HOH   639  2039 1358 HOH   HOH B . 
AA 11 HOH   640  2040 2148 HOH   HOH B . 
AA 11 HOH   641  2041 926  HOH   HOH B . 
AA 11 HOH   642  2042 459  HOH   HOH B . 
AA 11 HOH   643  2043 591  HOH   HOH B . 
AA 11 HOH   644  2044 176  HOH   HOH B . 
AA 11 HOH   645  2045 1169 HOH   HOH B . 
AA 11 HOH   646  2046 1186 HOH   HOH B . 
AA 11 HOH   647  2047 543  HOH   HOH B . 
AA 11 HOH   648  2048 949  HOH   HOH B . 
AA 11 HOH   649  2049 1204 HOH   HOH B . 
AA 11 HOH   650  2050 1514 HOH   HOH B . 
AA 11 HOH   651  2051 91   HOH   HOH B . 
AA 11 HOH   652  2052 144  HOH   HOH B . 
AA 11 HOH   653  2053 644  HOH   HOH B . 
AA 11 HOH   654  2054 154  HOH   HOH B . 
AA 11 HOH   655  2055 465  HOH   HOH B . 
AA 11 HOH   656  2056 1572 HOH   HOH B . 
AA 11 HOH   657  2057 886  HOH   HOH B . 
AA 11 HOH   658  2058 561  HOH   HOH B . 
AA 11 HOH   659  2059 2248 HOH   HOH B . 
AA 11 HOH   660  2060 205  HOH   HOH B . 
AA 11 HOH   661  2061 151  HOH   HOH B . 
AA 11 HOH   662  2062 264  HOH   HOH B . 
AA 11 HOH   663  2063 1834 HOH   HOH B . 
AA 11 HOH   664  2064 2104 HOH   HOH B . 
AA 11 HOH   665  2065 1017 HOH   HOH B . 
AA 11 HOH   666  2066 2444 HOH   HOH B . 
AA 11 HOH   667  2067 1427 HOH   HOH B . 
AA 11 HOH   668  2068 484  HOH   HOH B . 
AA 11 HOH   669  2069 507  HOH   HOH B . 
AA 11 HOH   670  2070 1350 HOH   HOH B . 
AA 11 HOH   671  2071 1171 HOH   HOH B . 
AA 11 HOH   672  2072 1345 HOH   HOH B . 
AA 11 HOH   673  2073 1898 HOH   HOH B . 
AA 11 HOH   674  2074 257  HOH   HOH B . 
AA 11 HOH   675  2075 1232 HOH   HOH B . 
AA 11 HOH   676  2076 175  HOH   HOH B . 
AA 11 HOH   677  2077 822  HOH   HOH B . 
AA 11 HOH   678  2078 523  HOH   HOH B . 
AA 11 HOH   679  2079 701  HOH   HOH B . 
AA 11 HOH   680  2080 1023 HOH   HOH B . 
AA 11 HOH   681  2081 1644 HOH   HOH B . 
AA 11 HOH   682  2082 496  HOH   HOH B . 
AA 11 HOH   683  2083 767  HOH   HOH B . 
AA 11 HOH   684  2084 592  HOH   HOH B . 
AA 11 HOH   685  2085 1750 HOH   HOH B . 
AA 11 HOH   686  2086 2103 HOH   HOH B . 
AA 11 HOH   687  2087 66   HOH   HOH B . 
AA 11 HOH   688  2088 2265 HOH   HOH B . 
AA 11 HOH   689  2089 1902 HOH   HOH B . 
AA 11 HOH   690  2090 2032 HOH   HOH B . 
AA 11 HOH   691  2091 1066 HOH   HOH B . 
AA 11 HOH   692  2092 1861 HOH   HOH B . 
AA 11 HOH   693  2093 1562 HOH   HOH B . 
AA 11 HOH   694  2094 718  HOH   HOH B . 
AA 11 HOH   695  2095 627  HOH   HOH B . 
AA 11 HOH   696  2096 2171 HOH   HOH B . 
AA 11 HOH   697  2097 576  HOH   HOH B . 
AA 11 HOH   698  2098 2271 HOH   HOH B . 
AA 11 HOH   699  2099 174  HOH   HOH B . 
AA 11 HOH   700  2100 1176 HOH   HOH B . 
AA 11 HOH   701  2101 603  HOH   HOH B . 
AA 11 HOH   702  2102 1480 HOH   HOH B . 
AA 11 HOH   703  2103 765  HOH   HOH B . 
AA 11 HOH   704  2104 893  HOH   HOH B . 
AA 11 HOH   705  2105 2414 HOH   HOH B . 
AA 11 HOH   706  2106 1313 HOH   HOH B . 
AA 11 HOH   707  2107 2182 HOH   HOH B . 
AA 11 HOH   708  2108 519  HOH   HOH B . 
AA 11 HOH   709  2109 688  HOH   HOH B . 
AA 11 HOH   710  2110 481  HOH   HOH B . 
AA 11 HOH   711  2111 2284 HOH   HOH B . 
AA 11 HOH   712  2112 564  HOH   HOH B . 
AA 11 HOH   713  2113 658  HOH   HOH B . 
AA 11 HOH   714  2114 809  HOH   HOH B . 
AA 11 HOH   715  2115 100  HOH   HOH B . 
AA 11 HOH   716  2116 2349 HOH   HOH B . 
AA 11 HOH   717  2117 945  HOH   HOH B . 
AA 11 HOH   718  2118 137  HOH   HOH B . 
AA 11 HOH   719  2119 630  HOH   HOH B . 
AA 11 HOH   720  2120 1645 HOH   HOH B . 
AA 11 HOH   721  2121 1961 HOH   HOH B . 
AA 11 HOH   722  2122 1699 HOH   HOH B . 
AA 11 HOH   723  2123 222  HOH   HOH B . 
AA 11 HOH   724  2124 79   HOH   HOH B . 
AA 11 HOH   725  2125 1682 HOH   HOH B . 
AA 11 HOH   726  2126 1939 HOH   HOH B . 
AA 11 HOH   727  2127 1    HOH   HOH B . 
AA 11 HOH   728  2128 771  HOH   HOH B . 
AA 11 HOH   729  2129 1503 HOH   HOH B . 
AA 11 HOH   730  2130 386  HOH   HOH B . 
AA 11 HOH   731  2131 2330 HOH   HOH B . 
AA 11 HOH   732  2132 960  HOH   HOH B . 
AA 11 HOH   733  2133 808  HOH   HOH B . 
AA 11 HOH   734  2134 2293 HOH   HOH B . 
AA 11 HOH   735  2135 43   HOH   HOH B . 
AA 11 HOH   736  2136 1444 HOH   HOH B . 
AA 11 HOH   737  2137 538  HOH   HOH B . 
AA 11 HOH   738  2138 2142 HOH   HOH B . 
AA 11 HOH   739  2139 331  HOH   HOH B . 
AA 11 HOH   740  2140 373  HOH   HOH B . 
AA 11 HOH   741  2141 1653 HOH   HOH B . 
AA 11 HOH   742  2142 314  HOH   HOH B . 
AA 11 HOH   743  2143 378  HOH   HOH B . 
AA 11 HOH   744  2144 159  HOH   HOH B . 
AA 11 HOH   745  2145 1825 HOH   HOH B . 
AA 11 HOH   746  2146 1336 HOH   HOH B . 
AA 11 HOH   747  2147 361  HOH   HOH B . 
AA 11 HOH   748  2148 1002 HOH   HOH B . 
AA 11 HOH   749  2149 1218 HOH   HOH B . 
AA 11 HOH   750  2150 2039 HOH   HOH B . 
AA 11 HOH   751  2151 2302 HOH   HOH B . 
AA 11 HOH   752  2152 2204 HOH   HOH B . 
AA 11 HOH   753  2153 206  HOH   HOH B . 
AA 11 HOH   754  2154 760  HOH   HOH B . 
AA 11 HOH   755  2155 1357 HOH   HOH B . 
AA 11 HOH   756  2156 2009 HOH   HOH B . 
AA 11 HOH   757  2157 2299 HOH   HOH B . 
AA 11 HOH   758  2158 14   HOH   HOH B . 
AA 11 HOH   759  2159 1413 HOH   HOH B . 
AA 11 HOH   760  2160 883  HOH   HOH B . 
AA 11 HOH   761  2161 1771 HOH   HOH B . 
AA 11 HOH   762  2162 1822 HOH   HOH B . 
AA 11 HOH   763  2163 1853 HOH   HOH B . 
AA 11 HOH   764  2164 1110 HOH   HOH B . 
AA 11 HOH   765  2165 1466 HOH   HOH B . 
AA 11 HOH   766  2166 1855 HOH   HOH B . 
AA 11 HOH   767  2167 595  HOH   HOH B . 
AA 11 HOH   768  2168 741  HOH   HOH B . 
AA 11 HOH   769  2169 301  HOH   HOH B . 
AA 11 HOH   770  2170 983  HOH   HOH B . 
AA 11 HOH   771  2171 1141 HOH   HOH B . 
AA 11 HOH   772  2172 2160 HOH   HOH B . 
AA 11 HOH   773  2173 1384 HOH   HOH B . 
AA 11 HOH   774  2174 2379 HOH   HOH B . 
AA 11 HOH   775  2175 2123 HOH   HOH B . 
AA 11 HOH   776  2176 1448 HOH   HOH B . 
AA 11 HOH   777  2177 2203 HOH   HOH B . 
AA 11 HOH   778  2178 1359 HOH   HOH B . 
AA 11 HOH   779  2179 273  HOH   HOH B . 
AA 11 HOH   780  2180 547  HOH   HOH B . 
AA 11 HOH   781  2181 468  HOH   HOH B . 
AA 11 HOH   782  2182 231  HOH   HOH B . 
AA 11 HOH   783  2183 142  HOH   HOH B . 
AA 11 HOH   784  2184 1354 HOH   HOH B . 
AA 11 HOH   785  2185 2200 HOH   HOH B . 
AA 11 HOH   786  2186 1321 HOH   HOH B . 
AA 11 HOH   787  2187 1029 HOH   HOH B . 
AA 11 HOH   788  2188 2382 HOH   HOH B . 
AA 11 HOH   789  2189 478  HOH   HOH B . 
AA 11 HOH   790  2190 907  HOH   HOH B . 
AA 11 HOH   791  2191 2222 HOH   HOH B . 
AA 11 HOH   792  2192 2405 HOH   HOH B . 
AA 11 HOH   793  2193 1823 HOH   HOH B . 
AA 11 HOH   794  2194 1491 HOH   HOH B . 
AA 11 HOH   795  2195 692  HOH   HOH B . 
AA 11 HOH   796  2196 597  HOH   HOH B . 
AA 11 HOH   797  2197 1790 HOH   HOH B . 
AA 11 HOH   798  2198 2034 HOH   HOH B . 
AA 11 HOH   799  2199 559  HOH   HOH B . 
AA 11 HOH   800  2200 1247 HOH   HOH B . 
AA 11 HOH   801  2201 806  HOH   HOH B . 
AA 11 HOH   802  2202 2213 HOH   HOH B . 
AA 11 HOH   803  2203 888  HOH   HOH B . 
AA 11 HOH   804  2204 1759 HOH   HOH B . 
AA 11 HOH   805  2205 1857 HOH   HOH B . 
AA 11 HOH   806  2206 1697 HOH   HOH B . 
AA 11 HOH   807  2207 590  HOH   HOH B . 
AA 11 HOH   808  2208 413  HOH   HOH B . 
AA 11 HOH   809  2209 2214 HOH   HOH B . 
AA 11 HOH   810  2210 76   HOH   HOH B . 
AA 11 HOH   811  2211 2247 HOH   HOH B . 
AA 11 HOH   812  2212 1233 HOH   HOH B . 
AA 11 HOH   813  2213 649  HOH   HOH B . 
AA 11 HOH   814  2214 870  HOH   HOH B . 
AA 11 HOH   815  2215 1040 HOH   HOH B . 
AA 11 HOH   816  2216 821  HOH   HOH B . 
AA 11 HOH   817  2217 999  HOH   HOH B . 
AA 11 HOH   818  2218 1920 HOH   HOH B . 
AA 11 HOH   819  2219 1735 HOH   HOH B . 
AA 11 HOH   820  2220 1542 HOH   HOH B . 
AA 11 HOH   821  2221 1528 HOH   HOH B . 
AA 11 HOH   822  2222 2246 HOH   HOH B . 
AA 11 HOH   823  2223 1725 HOH   HOH B . 
AA 11 HOH   824  2224 2430 HOH   HOH B . 
AA 11 HOH   825  2225 282  HOH   HOH B . 
AA 11 HOH   826  2226 2234 HOH   HOH B . 
AA 11 HOH   827  2227 2420 HOH   HOH B . 
AA 11 HOH   828  2228 778  HOH   HOH B . 
AA 11 HOH   829  2229 1965 HOH   HOH B . 
AA 11 HOH   830  2230 1573 HOH   HOH B . 
AA 11 HOH   831  2231 1530 HOH   HOH B . 
AA 11 HOH   832  2232 2037 HOH   HOH B . 
AA 11 HOH   833  2233 1462 HOH   HOH B . 
AA 11 HOH   834  2234 1545 HOH   HOH B . 
AA 11 HOH   835  2235 2030 HOH   HOH B . 
AA 11 HOH   836  2236 429  HOH   HOH B . 
AA 11 HOH   837  2237 631  HOH   HOH B . 
AA 11 HOH   838  2238 1162 HOH   HOH B . 
AA 11 HOH   839  2239 1601 HOH   HOH B . 
AA 11 HOH   840  2240 724  HOH   HOH B . 
AA 11 HOH   841  2241 2445 HOH   HOH B . 
AA 11 HOH   842  2242 1907 HOH   HOH B . 
AA 11 HOH   843  2243 2238 HOH   HOH B . 
AA 11 HOH   844  2244 2163 HOH   HOH B . 
AA 11 HOH   845  2245 931  HOH   HOH B . 
AA 11 HOH   846  2246 2237 HOH   HOH B . 
AA 11 HOH   847  2247 1727 HOH   HOH B . 
AA 11 HOH   848  2248 2038 HOH   HOH B . 
AA 11 HOH   849  2249 2139 HOH   HOH B . 
AA 11 HOH   850  2250 708  HOH   HOH B . 
AA 11 HOH   851  2251 1828 HOH   HOH B . 
AA 11 HOH   852  2252 727  HOH   HOH B . 
AA 11 HOH   853  2253 2298 HOH   HOH B . 
AA 11 HOH   854  2254 1324 HOH   HOH B . 
AA 11 HOH   855  2255 1541 HOH   HOH B . 
AA 11 HOH   856  2256 505  HOH   HOH B . 
AA 11 HOH   857  2257 461  HOH   HOH B . 
AA 11 HOH   858  2258 2229 HOH   HOH B . 
AA 11 HOH   859  2259 1430 HOH   HOH B . 
AA 11 HOH   860  2260 2210 HOH   HOH B . 
AA 11 HOH   861  2261 947  HOH   HOH B . 
AA 11 HOH   862  2262 2068 HOH   HOH B . 
AA 11 HOH   863  2263 1220 HOH   HOH B . 
AA 11 HOH   864  2264 2215 HOH   HOH B . 
AA 11 HOH   865  2265 1033 HOH   HOH B . 
AA 11 HOH   866  2266 1844 HOH   HOH B . 
AA 11 HOH   867  2267 1705 HOH   HOH B . 
AA 11 HOH   868  2268 602  HOH   HOH B . 
AA 11 HOH   869  2269 2362 HOH   HOH B . 
AA 11 HOH   870  2270 2352 HOH   HOH B . 
AA 11 HOH   871  2271 1387 HOH   HOH B . 
AA 11 HOH   872  2272 1876 HOH   HOH B . 
AA 11 HOH   873  2273 1688 HOH   HOH B . 
AA 11 HOH   874  2274 1429 HOH   HOH B . 
AA 11 HOH   875  2275 1273 HOH   HOH B . 
AA 11 HOH   876  2276 2083 HOH   HOH B . 
AA 11 HOH   877  2277 951  HOH   HOH B . 
AA 11 HOH   878  2278 2025 HOH   HOH B . 
AA 11 HOH   879  2279 1415 HOH   HOH B . 
AA 11 HOH   880  2280 2447 HOH   HOH B . 
AA 11 HOH   881  2281 2082 HOH   HOH B . 
AA 11 HOH   882  2282 859  HOH   HOH B . 
AA 11 HOH   883  2283 2197 HOH   HOH B . 
AA 11 HOH   884  2284 2233 HOH   HOH B . 
AA 11 HOH   885  2285 880  HOH   HOH B . 
AA 11 HOH   886  2286 2151 HOH   HOH B . 
AA 11 HOH   887  2287 1719 HOH   HOH B . 
AA 11 HOH   888  2288 2195 HOH   HOH B . 
AA 11 HOH   889  2289 2289 HOH   HOH B . 
AA 11 HOH   890  2290 1454 HOH   HOH B . 
AA 11 HOH   891  2291 1203 HOH   HOH B . 
AA 11 HOH   892  2292 1923 HOH   HOH B . 
AA 11 HOH   893  2293 2261 HOH   HOH B . 
AA 11 HOH   894  2294 90   HOH   HOH B . 
AA 11 HOH   895  2295 1893 HOH   HOH B . 
AA 11 HOH   896  2296 966  HOH   HOH B . 
AA 11 HOH   897  2297 2081 HOH   HOH B . 
AA 11 HOH   898  2298 894  HOH   HOH B . 
AA 11 HOH   899  2299 1538 HOH   HOH B . 
AA 11 HOH   900  2300 1396 HOH   HOH B . 
AA 11 HOH   901  2301 1471 HOH   HOH B . 
AA 11 HOH   902  2302 2006 HOH   HOH B . 
AA 11 HOH   903  2303 943  HOH   HOH B . 
AA 11 HOH   904  2304 1680 HOH   HOH B . 
AA 11 HOH   905  2305 726  HOH   HOH B . 
AA 11 HOH   906  2306 1625 HOH   HOH B . 
AA 11 HOH   907  2307 1276 HOH   HOH B . 
AA 11 HOH   908  2308 1856 HOH   HOH B . 
AA 11 HOH   909  2309 1512 HOH   HOH B . 
AA 11 HOH   910  2310 2295 HOH   HOH B . 
AA 11 HOH   911  2311 432  HOH   HOH B . 
AA 11 HOH   912  2312 1672 HOH   HOH B . 
AA 11 HOH   913  2313 1489 HOH   HOH B . 
AA 11 HOH   914  2314 1165 HOH   HOH B . 
AA 11 HOH   915  2315 1826 HOH   HOH B . 
AA 11 HOH   916  2316 455  HOH   HOH B . 
AA 11 HOH   917  2317 1615 HOH   HOH B . 
AA 11 HOH   918  2318 911  HOH   HOH B . 
AA 11 HOH   919  2319 720  HOH   HOH B . 
AA 11 HOH   920  2320 1322 HOH   HOH B . 
AA 11 HOH   921  2321 1245 HOH   HOH B . 
AA 11 HOH   922  2322 1088 HOH   HOH B . 
AA 11 HOH   923  2323 1207 HOH   HOH B . 
AA 11 HOH   924  2324 2003 HOH   HOH B . 
AA 11 HOH   925  2325 2147 HOH   HOH B . 
AA 11 HOH   926  2326 1662 HOH   HOH B . 
AA 11 HOH   927  2327 1500 HOH   HOH B . 
AA 11 HOH   928  2328 549  HOH   HOH B . 
AA 11 HOH   929  2329 954  HOH   HOH B . 
AA 11 HOH   930  2330 2227 HOH   HOH B . 
AA 11 HOH   931  2331 2202 HOH   HOH B . 
AA 11 HOH   932  2332 2288 HOH   HOH B . 
AA 11 HOH   933  2333 789  HOH   HOH B . 
AA 11 HOH   934  2334 1638 HOH   HOH B . 
AA 11 HOH   935  2335 1214 HOH   HOH B . 
AA 11 HOH   936  2336 1248 HOH   HOH B . 
AA 11 HOH   937  2337 1303 HOH   HOH B . 
AA 11 HOH   938  2338 491  HOH   HOH B . 
AA 11 HOH   939  2339 1551 HOH   HOH B . 
AA 11 HOH   940  2340 937  HOH   HOH B . 
AA 11 HOH   941  2341 2418 HOH   HOH B . 
AA 11 HOH   942  2342 2187 HOH   HOH B . 
AA 11 HOH   943  2343 1613 HOH   HOH B . 
AA 11 HOH   944  2344 1423 HOH   HOH B . 
AA 11 HOH   945  2345 1911 HOH   HOH B . 
AA 11 HOH   946  2346 2021 HOH   HOH B . 
AA 11 HOH   947  2347 2028 HOH   HOH B . 
AA 11 HOH   948  2348 1522 HOH   HOH B . 
AA 11 HOH   949  2349 1557 HOH   HOH B . 
AA 11 HOH   950  2350 1535 HOH   HOH B . 
AA 11 HOH   951  2351 515  HOH   HOH B . 
AA 11 HOH   952  2352 1025 HOH   HOH B . 
AA 11 HOH   953  2353 2459 HOH   HOH B . 
AA 11 HOH   954  2354 1702 HOH   HOH B . 
AA 11 HOH   955  2355 94   HOH   HOH B . 
AA 11 HOH   956  2356 1854 HOH   HOH B . 
AA 11 HOH   957  2357 2392 HOH   HOH B . 
AA 11 HOH   958  2358 1257 HOH   HOH B . 
AA 11 HOH   959  2359 2027 HOH   HOH B . 
AA 11 HOH   960  2360 1846 HOH   HOH B . 
AA 11 HOH   961  2361 2322 HOH   HOH B . 
AA 11 HOH   962  2362 1780 HOH   HOH B . 
AA 11 HOH   963  2363 1217 HOH   HOH B . 
AA 11 HOH   964  2364 2049 HOH   HOH B . 
AA 11 HOH   965  2365 1411 HOH   HOH B . 
AA 11 HOH   966  2366 2417 HOH   HOH B . 
AA 11 HOH   967  2367 1789 HOH   HOH B . 
AA 11 HOH   968  2368 1482 HOH   HOH B . 
AA 11 HOH   969  2369 2    HOH   HOH B . 
AA 11 HOH   970  2370 2399 HOH   HOH B . 
AA 11 HOH   971  2371 1863 HOH   HOH B . 
AA 11 HOH   972  2372 2380 HOH   HOH B . 
AA 11 HOH   973  2373 1390 HOH   HOH B . 
AA 11 HOH   974  2374 2199 HOH   HOH B . 
AA 11 HOH   975  2375 1294 HOH   HOH B . 
AA 11 HOH   976  2376 1365 HOH   HOH B . 
AA 11 HOH   977  2377 1888 HOH   HOH B . 
AA 11 HOH   978  2378 1212 HOH   HOH B . 
AA 11 HOH   979  2379 1409 HOH   HOH B . 
AA 11 HOH   980  2380 2438 HOH   HOH B . 
AA 11 HOH   981  2381 1022 HOH   HOH B . 
AA 11 HOH   982  2382 1258 HOH   HOH B . 
AA 11 HOH   983  2383 1468 HOH   HOH B . 
AA 11 HOH   984  2384 1329 HOH   HOH B . 
AA 11 HOH   985  2385 1523 HOH   HOH B . 
AA 11 HOH   986  2386 1801 HOH   HOH B . 
AA 11 HOH   987  2387 792  HOH   HOH B . 
AA 11 HOH   988  2388 1760 HOH   HOH B . 
AA 11 HOH   989  2389 682  HOH   HOH B . 
AA 11 HOH   990  2390 2296 HOH   HOH B . 
AA 11 HOH   991  2391 1286 HOH   HOH B . 
AA 11 HOH   992  2392 2439 HOH   HOH B . 
AA 11 HOH   993  2393 1474 HOH   HOH B . 
AA 11 HOH   994  2394 1671 HOH   HOH B . 
AA 11 HOH   995  2395 2409 HOH   HOH B . 
AA 11 HOH   996  2396 2460 HOH   HOH B . 
AA 11 HOH   997  2397 1161 HOH   HOH B . 
AA 11 HOH   998  2398 1374 HOH   HOH B . 
AA 11 HOH   999  2399 1452 HOH   HOH B . 
AA 11 HOH   1000 2400 1172 HOH   HOH B . 
AA 11 HOH   1001 2401 1389 HOH   HOH B . 
AA 11 HOH   1002 2402 1709 HOH   HOH B . 
AA 11 HOH   1003 2403 1126 HOH   HOH B . 
AA 11 HOH   1004 2404 1475 HOH   HOH B . 
AA 11 HOH   1005 2405 1015 HOH   HOH B . 
AA 11 HOH   1006 2406 1753 HOH   HOH B . 
AA 11 HOH   1007 2407 1301 HOH   HOH B . 
AA 11 HOH   1008 2408 1552 HOH   HOH B . 
AA 11 HOH   1009 2409 2421 HOH   HOH B . 
AA 11 HOH   1010 2410 1686 HOH   HOH B . 
AA 11 HOH   1011 2411 2004 HOH   HOH B . 
AA 11 HOH   1012 2412 2410 HOH   HOH B . 
AA 11 HOH   1013 2413 1899 HOH   HOH B . 
AA 11 HOH   1014 2414 1274 HOH   HOH B . 
AA 11 HOH   1015 2415 2040 HOH   HOH B . 
AA 11 HOH   1016 2416 1544 HOH   HOH B . 
AA 11 HOH   1017 2417 1292 HOH   HOH B . 
AA 11 HOH   1018 2418 1063 HOH   HOH B . 
AA 11 HOH   1019 2419 1152 HOH   HOH B . 
AA 11 HOH   1020 2420 640  HOH   HOH B . 
AA 11 HOH   1021 2421 1608 HOH   HOH B . 
AA 11 HOH   1022 2422 2312 HOH   HOH B . 
AA 11 HOH   1023 2423 1156 HOH   HOH B . 
AA 11 HOH   1024 2424 1887 HOH   HOH B . 
AA 11 HOH   1025 2425 1594 HOH   HOH B . 
AA 11 HOH   1026 2426 1858 HOH   HOH B . 
AA 11 HOH   1027 2427 1118 HOH   HOH B . 
AA 11 HOH   1028 2428 2291 HOH   HOH B . 
AA 11 HOH   1029 2429 993  HOH   HOH B . 
AA 11 HOH   1030 2430 1479 HOH   HOH B . 
AA 11 HOH   1031 2431 2436 HOH   HOH B . 
AA 11 HOH   1032 2432 1499 HOH   HOH B . 
AA 11 HOH   1033 2433 1722 HOH   HOH B . 
AA 11 HOH   1034 2434 1914 HOH   HOH B . 
AA 11 HOH   1035 2435 1758 HOH   HOH B . 
AA 11 HOH   1036 2436 1295 HOH   HOH B . 
AA 11 HOH   1037 2437 1418 HOH   HOH B . 
AA 11 HOH   1038 2438 448  HOH   HOH B . 
AA 11 HOH   1039 2439 2111 HOH   HOH B . 
AA 11 HOH   1040 2440 1870 HOH   HOH B . 
AA 11 HOH   1041 2441 1765 HOH   HOH B . 
AA 11 HOH   1042 2442 1878 HOH   HOH B . 
AA 11 HOH   1043 2443 4    HOH   HOH B . 
AA 11 HOH   1044 2444 1300 HOH   HOH B . 
AA 11 HOH   1045 2445 2339 HOH   HOH B . 
AA 11 HOH   1046 2446 125  HOH   HOH B . 
AA 11 HOH   1047 2447 694  HOH   HOH B . 
AA 11 HOH   1048 2448 1184 HOH   HOH B . 
AA 11 HOH   1049 2449 2283 HOH   HOH B . 
AA 11 HOH   1050 2450 2303 HOH   HOH B . 
AA 11 HOH   1051 2451 1774 HOH   HOH B . 
AA 11 HOH   1052 2452 1505 HOH   HOH B . 
AA 11 HOH   1053 2453 1515 HOH   HOH B . 
AA 11 HOH   1054 2454 2033 HOH   HOH B . 
AA 11 HOH   1055 2455 2416 HOH   HOH B . 
AA 11 HOH   1056 2456 686  HOH   HOH B . 
AA 11 HOH   1057 2457 2351 HOH   HOH B . 
AA 11 HOH   1058 2458 1836 HOH   HOH B . 
AA 11 HOH   1059 2459 2305 HOH   HOH B . 
AA 11 HOH   1060 2460 1060 HOH   HOH B . 
AA 11 HOH   1061 2461 1439 HOH   HOH B . 
AA 11 HOH   1062 2462 1917 HOH   HOH B . 
AA 11 HOH   1063 2463 2161 HOH   HOH B . 
AA 11 HOH   1064 2464 826  HOH   HOH B . 
AA 11 HOH   1065 2465 1271 HOH   HOH B . 
AA 11 HOH   1066 2466 839  HOH   HOH B . 
AA 11 HOH   1067 2467 766  HOH   HOH B . 
AA 11 HOH   1068 2468 705  HOH   HOH B . 
AA 11 HOH   1069 2469 2313 HOH   HOH B . 
AA 11 HOH   1070 2470 2383 HOH   HOH B . 
AA 11 HOH   1071 2471 2029 HOH   HOH B . 
AA 11 HOH   1072 2472 437  HOH   HOH B . 
AA 11 HOH   1073 2473 678  HOH   HOH B . 
AA 11 HOH   1074 2474 2287 HOH   HOH B . 
AA 11 HOH   1075 2475 1769 HOH   HOH B . 
AA 11 HOH   1076 2476 2285 HOH   HOH B . 
AA 11 HOH   1077 2477 2369 HOH   HOH B . 
AA 11 HOH   1078 2478 509  HOH   HOH B . 
AA 11 HOH   1079 2479 1919 HOH   HOH B . 
AA 11 HOH   1080 2480 1135 HOH   HOH B . 
AA 11 HOH   1081 2481 1655 HOH   HOH B . 
AA 11 HOH   1082 2482 2118 HOH   HOH B . 
AA 11 HOH   1083 2483 2357 HOH   HOH B . 
AA 11 HOH   1084 2484 1621 HOH   HOH B . 
AA 11 HOH   1085 2485 1174 HOH   HOH B . 
AA 11 HOH   1086 2486 2361 HOH   HOH B . 
AA 11 HOH   1087 2487 1485 HOH   HOH B . 
AA 11 HOH   1088 2488 1103 HOH   HOH B . 
AA 11 HOH   1089 2489 579  HOH   HOH B . 
AA 11 HOH   1090 2490 2173 HOH   HOH B . 
AA 11 HOH   1091 2491 1532 HOH   HOH B . 
AA 11 HOH   1092 2492 1767 HOH   HOH B . 
AA 11 HOH   1093 2493 161  HOH   HOH B . 
AA 11 HOH   1094 2494 1657 HOH   HOH B . 
AA 11 HOH   1095 2495 1886 HOH   HOH B . 
AA 11 HOH   1096 2496 2422 HOH   HOH B . 
AA 11 HOH   1097 2497 1804 HOH   HOH B . 
AA 11 HOH   1098 2498 2016 HOH   HOH B . 
AA 11 HOH   1099 2499 1114 HOH   HOH B . 
AA 11 HOH   1100 2500 1693 HOH   HOH B . 
AA 11 HOH   1101 2501 1379 HOH   HOH B . 
AA 11 HOH   1102 2502 1382 HOH   HOH B . 
AA 11 HOH   1103 2503 2310 HOH   HOH B . 
AA 11 HOH   1104 2504 1332 HOH   HOH B . 
AA 11 HOH   1105 2505 1038 HOH   HOH B . 
AA 11 HOH   1106 2506 1918 HOH   HOH B . 
AA 11 HOH   1107 2507 1884 HOH   HOH B . 
AA 11 HOH   1108 2508 1177 HOH   HOH B . 
AA 11 HOH   1109 2509 1520 HOH   HOH B . 
AA 11 HOH   1110 2510 1442 HOH   HOH B . 
AA 11 HOH   1111 2511 2413 HOH   HOH B . 
AA 11 HOH   1112 2512 1488 HOH   HOH B . 
AA 11 HOH   1113 2513 1455 HOH   HOH B . 
AA 11 HOH   1114 2514 1132 HOH   HOH B . 
AA 11 HOH   1115 2515 604  HOH   HOH B . 
AA 11 HOH   1116 2516 700  HOH   HOH B . 
AA 11 HOH   1117 2517 1852 HOH   HOH B . 
AA 11 HOH   1118 2518 1209 HOH   HOH B . 
AA 11 HOH   1119 2519 908  HOH   HOH B . 
AA 11 HOH   1120 2520 2397 HOH   HOH B . 
AA 11 HOH   1121 2521 2102 HOH   HOH B . 
AA 11 HOH   1122 2522 1648 HOH   HOH B . 
AA 11 HOH   1123 2523 1076 HOH   HOH B . 
AA 11 HOH   1124 2524 1967 HOH   HOH B . 
AA 11 HOH   1125 2525 751  HOH   HOH B . 
AA 11 HOH   1126 2526 2297 HOH   HOH B . 
AA 11 HOH   1127 2527 1148 HOH   HOH B . 
AA 11 HOH   1128 2528 2196 HOH   HOH B . 
AA 11 HOH   1129 2529 1732 HOH   HOH B . 
AA 11 HOH   1130 2530 2188 HOH   HOH B . 
AA 11 HOH   1131 2531 933  HOH   HOH B . 
AA 11 HOH   1132 2532 1880 HOH   HOH B . 
AA 11 HOH   1133 2533 1368 HOH   HOH B . 
AA 11 HOH   1134 2534 1663 HOH   HOH B . 
AA 11 HOH   1135 2535 1081 HOH   HOH B . 
AA 11 HOH   1136 2536 1714 HOH   HOH B . 
AA 11 HOH   1137 2537 1537 HOH   HOH B . 
AA 11 HOH   1138 2538 1739 HOH   HOH B . 
AA 11 HOH   1139 2539 2026 HOH   HOH B . 
AA 11 HOH   1140 2540 1493 HOH   HOH B . 
AA 11 HOH   1141 2541 1736 HOH   HOH B . 
AA 11 HOH   1142 2542 363  HOH   HOH B . 
AA 11 HOH   1143 2543 2158 HOH   HOH B . 
AA 11 HOH   1144 2544 2189 HOH   HOH B . 
AA 11 HOH   1145 2545 1529 HOH   HOH B . 
AA 11 HOH   1146 2546 1821 HOH   HOH B . 
AA 11 HOH   1147 2547 2440 HOH   HOH B . 
AA 11 HOH   1148 2548 668  HOH   HOH B . 
AA 11 HOH   1149 2549 1337 HOH   HOH B . 
AA 11 HOH   1150 2550 1481 HOH   HOH B . 
AA 11 HOH   1151 2551 1447 HOH   HOH B . 
AA 11 HOH   1152 2552 1808 HOH   HOH B . 
AA 11 HOH   1153 2553 1421 HOH   HOH B . 
AA 11 HOH   1154 2554 2019 HOH   HOH B . 
AA 11 HOH   1155 2555 770  HOH   HOH B . 
AA 11 HOH   1156 2556 2172 HOH   HOH B . 
AA 11 HOH   1157 2557 1519 HOH   HOH B . 
AA 11 HOH   1158 2558 2458 HOH   HOH B . 
AA 11 HOH   1159 2559 1211 HOH   HOH B . 
AA 11 HOH   1160 2560 1524 HOH   HOH B . 
AA 11 HOH   1161 2561 1913 HOH   HOH B . 
AA 11 HOH   1162 2562 1691 HOH   HOH B . 
AA 11 HOH   1163 2563 1084 HOH   HOH B . 
AA 11 HOH   1164 2564 1277 HOH   HOH B . 
AA 11 HOH   1165 2565 956  HOH   HOH B . 
AA 11 HOH   1166 2566 514  HOH   HOH B . 
AA 11 HOH   1167 2567 2005 HOH   HOH B . 
AA 11 HOH   1168 2568 1067 HOH   HOH B . 
AA 11 HOH   1169 2569 2338 HOH   HOH B . 
AA 11 HOH   1170 2570 2089 HOH   HOH B . 
AA 11 HOH   1171 2571 2226 HOH   HOH B . 
AA 11 HOH   1172 2572 2403 HOH   HOH B . 
AA 11 HOH   1173 2573 2240 HOH   HOH B . 
AA 11 HOH   1174 2574 1200 HOH   HOH B . 
AA 11 HOH   1175 2575 2311 HOH   HOH B . 
AA 11 HOH   1176 2576 2437 HOH   HOH B . 
AA 11 HOH   1177 2577 1708 HOH   HOH B . 
AA 11 HOH   1178 2578 2356 HOH   HOH B . 
AA 11 HOH   1179 2579 2220 HOH   HOH B . 
AA 11 HOH   1180 2580 1742 HOH   HOH B . 
AA 11 HOH   1181 2581 2153 HOH   HOH B . 
AA 11 HOH   1182 2582 1803 HOH   HOH B . 
AA 11 HOH   1183 2583 1113 HOH   HOH B . 
AA 11 HOH   1184 2584 2348 HOH   HOH B . 
AA 11 HOH   1185 2585 1392 HOH   HOH B . 
AA 11 HOH   1186 2586 2221 HOH   HOH B . 
AA 11 HOH   1187 2587 1180 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 ARG 33   ? NE  ? A ARG 35   NE  
2   1 Y 1 A ARG 33   ? CZ  ? A ARG 35   CZ  
3   1 Y 1 A ARG 33   ? NH1 ? A ARG 35   NH1 
4   1 Y 1 A ARG 33   ? NH2 ? A ARG 35   NH2 
5   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
6   1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
7   1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
8   1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
9   1 Y 1 A HIS 79   ? CG  ? A HIS 81   CG  
10  1 Y 1 A HIS 79   ? ND1 ? A HIS 81   ND1 
11  1 Y 1 A HIS 79   ? CD2 ? A HIS 81   CD2 
12  1 Y 1 A HIS 79   ? CE1 ? A HIS 81   CE1 
13  1 Y 1 A HIS 79   ? NE2 ? A HIS 81   NE2 
14  1 Y 1 A SER 82   ? OG  ? A SER 84   OG  
15  1 Y 1 A GLU 85   ? CG  ? A GLU 87   CG  
16  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
17  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
18  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
19  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
20  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
21  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
22  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
23  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
24  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
25  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
26  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
27  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
28  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
29  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
30  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
31  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
32  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
33  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
34  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
35  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
36  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
37  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
38  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
39  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
40  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
41  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
42  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
43  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
44  1 Y 1 A SER 137  ? OG  ? A SER 139  OG  
45  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
46  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
47  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
48  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
49  1 Y 1 A THR 156  ? OG1 ? A THR 158  OG1 
50  1 Y 1 A THR 156  ? CG2 ? A THR 158  CG2 
51  1 Y 1 A GLU 177  ? CG  ? A GLU 179  CG  
52  1 Y 1 A GLU 177  ? CD  ? A GLU 179  CD  
53  1 Y 1 A GLU 177  ? OE1 ? A GLU 179  OE1 
54  1 Y 1 A GLU 177  ? OE2 ? A GLU 179  OE2 
55  1 Y 1 A ARG 189  ? CG  ? A ARG 191  CG  
56  1 Y 1 A ARG 189  ? CD  ? A ARG 191  CD  
57  1 Y 1 A ARG 189  ? NE  ? A ARG 191  NE  
58  1 Y 1 A ARG 189  ? CZ  ? A ARG 191  CZ  
59  1 Y 1 A ARG 189  ? NH1 ? A ARG 191  NH1 
60  1 Y 1 A ARG 189  ? NH2 ? A ARG 191  NH2 
61  1 Y 1 A GLN 194  ? CG  ? A GLN 196  CG  
62  1 Y 1 A GLN 194  ? CD  ? A GLN 196  CD  
63  1 Y 1 A GLN 194  ? OE1 ? A GLN 196  OE1 
64  1 Y 1 A GLN 194  ? NE2 ? A GLN 196  NE2 
65  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
66  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
67  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
68  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
69  1 Y 1 A LYS 209  ? CG  ? A LYS 211  CG  
70  1 Y 1 A LYS 209  ? CD  ? A LYS 211  CD  
71  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
72  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
73  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
74  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
75  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
76  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
77  1 Y 1 A LYS 214  ? CG  ? A LYS 216  CG  
78  1 Y 1 A LYS 214  ? CD  ? A LYS 216  CD  
79  1 Y 1 A LYS 214  ? CE  ? A LYS 216  CE  
80  1 Y 1 A LYS 214  ? NZ  ? A LYS 216  NZ  
81  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
82  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
83  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
84  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
85  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
86  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
87  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
88  1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
89  1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
90  1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
91  1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
92  1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
93  1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
94  1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
95  1 Y 1 A THR 481  ? OG1 ? A THR 483  OG1 
96  1 Y 1 A THR 481  ? CG2 ? A THR 483  CG2 
97  1 Y 1 A LEU 482  ? CG  ? A LEU 484  CG  
98  1 Y 1 A LEU 482  ? CD1 ? A LEU 484  CD1 
99  1 Y 1 A LEU 482  ? CD2 ? A LEU 484  CD2 
100 1 Y 1 A ARG 489  ? CG  ? A ARG 491  CG  
101 1 Y 1 A ARG 489  ? CD  ? A ARG 491  CD  
102 1 Y 1 A ARG 489  ? NE  ? A ARG 491  NE  
103 1 Y 1 A ARG 489  ? CZ  ? A ARG 491  CZ  
104 1 Y 1 A ARG 489  ? NH1 ? A ARG 491  NH1 
105 1 Y 1 A ARG 489  ? NH2 ? A ARG 491  NH2 
106 1 Y 1 A LEU 490  ? CG  ? A LEU 492  CG  
107 1 Y 1 A LEU 490  ? CD1 ? A LEU 492  CD1 
108 1 Y 1 A LEU 490  ? CD2 ? A LEU 492  CD2 
109 1 Y 1 A ASN 496  ? CG  ? A ASN 498  CG  
110 1 Y 1 A ASN 496  ? OD1 ? A ASN 498  OD1 
111 1 Y 1 A ASN 496  ? ND2 ? A ASN 498  ND2 
112 1 Y 1 A VAL 500  ? CG1 ? A VAL 502  CG1 
113 1 Y 1 A VAL 500  ? CG2 ? A VAL 502  CG2 
114 1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
115 1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
116 1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
117 1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
118 1 Y 1 A ARG 533  ? CG  ? A ARG 535  CG  
119 1 Y 1 A ARG 533  ? CD  ? A ARG 535  CD  
120 1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
121 1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
122 1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
123 1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
124 1 Y 1 A LYS 573  ? CG  ? A LYS 575  CG  
125 1 Y 1 A LYS 573  ? CD  ? A LYS 575  CD  
126 1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
127 1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
128 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
129 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
130 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
131 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
132 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
133 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
134 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
135 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
136 1 Y 1 A GLU 785  ? CG  ? A GLU 787  CG  
137 1 Y 1 A GLU 785  ? CD  ? A GLU 787  CD  
138 1 Y 1 A GLU 785  ? OE1 ? A GLU 787  OE1 
139 1 Y 1 A GLU 785  ? OE2 ? A GLU 787  OE2 
140 1 Y 1 A LEU 824  ? CG  ? A LEU 826  CG  
141 1 Y 1 A LEU 824  ? CD1 ? A LEU 826  CD1 
142 1 Y 1 A LEU 824  ? CD2 ? A LEU 826  CD2 
143 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
144 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
145 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
146 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
147 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
148 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
149 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
150 1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
151 1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
152 1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
153 1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
154 1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
155 1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
156 1 Y 1 A ILE 912  ? CG1 ? A ILE 914  CG1 
157 1 Y 1 A ILE 912  ? CG2 ? A ILE 914  CG2 
158 1 Y 1 A ILE 912  ? CD1 ? A ILE 914  CD1 
159 1 Y 1 A GLU 932  ? CG  ? A GLU 934  CG  
160 1 Y 1 A GLU 932  ? CD  ? A GLU 934  CD  
161 1 Y 1 A GLU 932  ? OE1 ? A GLU 934  OE1 
162 1 Y 1 A GLU 932  ? OE2 ? A GLU 934  OE2 
163 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
164 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
165 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
166 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
167 1 Y 1 A LEU 934  ? CG  ? A LEU 936  CG  
168 1 Y 1 A LEU 934  ? CD1 ? A LEU 936  CD1 
169 1 Y 1 A LEU 934  ? CD2 ? A LEU 936  CD2 
170 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
171 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
172 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
173 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
174 1 Y 1 A ARG 939  ? CG  ? A ARG 941  CG  
175 1 Y 1 A ARG 939  ? CD  ? A ARG 941  CD  
176 1 Y 1 A ARG 939  ? NE  ? A ARG 941  NE  
177 1 Y 1 A ARG 939  ? CZ  ? A ARG 941  CZ  
178 1 Y 1 A ARG 939  ? NH1 ? A ARG 941  NH1 
179 1 Y 1 A ARG 939  ? NH2 ? A ARG 941  NH2 
180 1 Y 1 A ILE 949  ? CG1 ? A ILE 951  CG1 
181 1 Y 1 A ILE 949  ? CG2 ? A ILE 951  CG2 
182 1 Y 1 A ILE 949  ? CD1 ? A ILE 951  CD1 
183 1 Y 1 A ARG 952  ? CG  ? A ARG 954  CG  
184 1 Y 1 A ARG 952  ? CD  ? A ARG 954  CD  
185 1 Y 1 A ARG 952  ? NE  ? A ARG 954  NE  
186 1 Y 1 A ARG 952  ? CZ  ? A ARG 954  CZ  
187 1 Y 1 A ARG 952  ? NH1 ? A ARG 954  NH1 
188 1 Y 1 A ARG 952  ? NH2 ? A ARG 954  NH2 
189 1 Y 1 A ARG 1063 ? CG  ? A ARG 1065 CG  
190 1 Y 1 A ARG 1063 ? CD  ? A ARG 1065 CD  
191 1 Y 1 A ARG 1063 ? NE  ? A ARG 1065 NE  
192 1 Y 1 A ARG 1063 ? CZ  ? A ARG 1065 CZ  
193 1 Y 1 A ARG 1063 ? NH1 ? A ARG 1065 NH1 
194 1 Y 1 A ARG 1063 ? NH2 ? A ARG 1065 NH2 
195 1 Y 1 A ARG 1091 ? CG  ? A ARG 1093 CG  
196 1 Y 1 A ARG 1091 ? CD  ? A ARG 1093 CD  
197 1 Y 1 A ARG 1091 ? NE  ? A ARG 1093 NE  
198 1 Y 1 A ARG 1091 ? CZ  ? A ARG 1093 CZ  
199 1 Y 1 A ARG 1091 ? NH1 ? A ARG 1093 NH1 
200 1 Y 1 A ARG 1091 ? NH2 ? A ARG 1093 NH2 
201 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
202 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
203 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
204 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
205 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
206 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
207 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
208 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
209 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
210 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
211 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
212 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
213 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
214 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
215 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
216 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
217 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
218 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
219 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
220 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
221 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
222 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
223 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
224 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
225 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
226 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
227 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
228 1 Y 1 B SER 66   ? OG  ? B SER 68   OG  
229 1 Y 1 B GLU 73   ? CG  ? B GLU 75   CG  
230 1 Y 1 B GLU 73   ? CD  ? B GLU 75   CD  
231 1 Y 1 B GLU 73   ? OE1 ? B GLU 75   OE1 
232 1 Y 1 B GLU 73   ? OE2 ? B GLU 75   OE2 
233 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
234 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
235 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
236 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
237 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
238 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
239 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
240 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
241 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
242 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
243 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
244 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
245 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
246 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
247 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
248 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
249 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
250 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
251 1 Y 1 B ASP 127  ? CG  ? B ASP 129  CG  
252 1 Y 1 B ASP 127  ? OD1 ? B ASP 129  OD1 
253 1 Y 1 B ASP 127  ? OD2 ? B ASP 129  OD2 
254 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
255 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
256 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
257 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
258 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
259 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
260 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
261 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
262 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
263 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
264 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
265 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
266 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
267 1 Y 1 B ARG 138  ? CG  ? B ARG 140  CG  
268 1 Y 1 B ARG 138  ? CD  ? B ARG 140  CD  
269 1 Y 1 B ARG 138  ? NE  ? B ARG 140  NE  
270 1 Y 1 B ARG 138  ? CZ  ? B ARG 140  CZ  
271 1 Y 1 B ARG 138  ? NH1 ? B ARG 140  NH1 
272 1 Y 1 B ARG 138  ? NH2 ? B ARG 140  NH2 
273 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
274 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
275 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
276 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
277 1 Y 1 B LEU 155  ? CG  ? B LEU 157  CG  
278 1 Y 1 B LEU 155  ? CD1 ? B LEU 157  CD1 
279 1 Y 1 B LEU 155  ? CD2 ? B LEU 157  CD2 
280 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
281 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
282 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
283 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
284 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
285 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
286 1 Y 1 B GLN 194  ? CG  ? B GLN 196  CG  
287 1 Y 1 B GLN 194  ? CD  ? B GLN 196  CD  
288 1 Y 1 B GLN 194  ? OE1 ? B GLN 196  OE1 
289 1 Y 1 B GLN 194  ? NE2 ? B GLN 196  NE2 
290 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
291 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
292 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
293 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
294 1 Y 1 B LYS 209  ? CG  ? B LYS 211  CG  
295 1 Y 1 B LYS 209  ? CD  ? B LYS 211  CD  
296 1 Y 1 B LYS 209  ? CE  ? B LYS 211  CE  
297 1 Y 1 B LYS 209  ? NZ  ? B LYS 211  NZ  
298 1 Y 1 B GLU 210  ? CG  ? B GLU 212  CG  
299 1 Y 1 B GLU 210  ? CD  ? B GLU 212  CD  
300 1 Y 1 B GLU 210  ? OE1 ? B GLU 212  OE1 
301 1 Y 1 B GLU 210  ? OE2 ? B GLU 212  OE2 
302 1 Y 1 B LYS 214  ? CG  ? B LYS 216  CG  
303 1 Y 1 B LYS 214  ? CD  ? B LYS 216  CD  
304 1 Y 1 B LYS 214  ? CE  ? B LYS 216  CE  
305 1 Y 1 B LYS 214  ? NZ  ? B LYS 216  NZ  
306 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
307 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
308 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
309 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
310 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
311 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
312 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
313 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
314 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
315 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
316 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
317 1 Y 1 B GLU 458  ? CG  ? B GLU 460  CG  
318 1 Y 1 B GLU 458  ? CD  ? B GLU 460  CD  
319 1 Y 1 B GLU 458  ? OE1 ? B GLU 460  OE1 
320 1 Y 1 B GLU 458  ? OE2 ? B GLU 460  OE2 
321 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
322 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
323 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
324 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
325 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
326 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
327 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
328 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
329 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
330 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
331 1 Y 1 B THR 481  ? OG1 ? B THR 483  OG1 
332 1 Y 1 B THR 481  ? CG2 ? B THR 483  CG2 
333 1 Y 1 B LEU 482  ? CG  ? B LEU 484  CG  
334 1 Y 1 B LEU 482  ? CD1 ? B LEU 484  CD1 
335 1 Y 1 B LEU 482  ? CD2 ? B LEU 484  CD2 
336 1 Y 1 B TYR 485  ? CG  ? B TYR 487  CG  
337 1 Y 1 B TYR 485  ? CD1 ? B TYR 487  CD1 
338 1 Y 1 B TYR 485  ? CD2 ? B TYR 487  CD2 
339 1 Y 1 B TYR 485  ? CE1 ? B TYR 487  CE1 
340 1 Y 1 B TYR 485  ? CE2 ? B TYR 487  CE2 
341 1 Y 1 B TYR 485  ? CZ  ? B TYR 487  CZ  
342 1 Y 1 B TYR 485  ? OH  ? B TYR 487  OH  
343 1 Y 1 B ARG 489  ? CG  ? B ARG 491  CG  
344 1 Y 1 B ARG 489  ? CD  ? B ARG 491  CD  
345 1 Y 1 B ARG 489  ? NE  ? B ARG 491  NE  
346 1 Y 1 B ARG 489  ? CZ  ? B ARG 491  CZ  
347 1 Y 1 B ARG 489  ? NH1 ? B ARG 491  NH1 
348 1 Y 1 B ARG 489  ? NH2 ? B ARG 491  NH2 
349 1 Y 1 B LEU 490  ? CG  ? B LEU 492  CG  
350 1 Y 1 B LEU 490  ? CD1 ? B LEU 492  CD1 
351 1 Y 1 B LEU 490  ? CD2 ? B LEU 492  CD2 
352 1 Y 1 B GLU 492  ? CG  ? B GLU 494  CG  
353 1 Y 1 B GLU 492  ? CD  ? B GLU 494  CD  
354 1 Y 1 B GLU 492  ? OE1 ? B GLU 494  OE1 
355 1 Y 1 B GLU 492  ? OE2 ? B GLU 494  OE2 
356 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
357 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
358 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
359 1 Y 1 B VAL 500  ? CG1 ? B VAL 502  CG1 
360 1 Y 1 B VAL 500  ? CG2 ? B VAL 502  CG2 
361 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
362 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
363 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
364 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
365 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
366 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
367 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
368 1 Y 1 B ILE 510  ? CG1 ? B ILE 512  CG1 
369 1 Y 1 B ILE 510  ? CG2 ? B ILE 512  CG2 
370 1 Y 1 B ILE 510  ? CD1 ? B ILE 512  CD1 
371 1 Y 1 B ILE 514  ? CG1 ? B ILE 516  CG1 
372 1 Y 1 B ILE 514  ? CG2 ? B ILE 516  CG2 
373 1 Y 1 B ILE 514  ? CD1 ? B ILE 516  CD1 
374 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
375 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
376 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
377 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
378 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
379 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
380 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
381 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
382 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
383 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
384 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
385 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
386 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
387 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
388 1 Y 1 B ASP 796  ? CG  ? B ASP 798  CG  
389 1 Y 1 B ASP 796  ? OD1 ? B ASP 798  OD1 
390 1 Y 1 B ASP 796  ? OD2 ? B ASP 798  OD2 
391 1 Y 1 B ASP 838  ? CG  ? B ASP 840  CG  
392 1 Y 1 B ASP 838  ? OD1 ? B ASP 840  OD1 
393 1 Y 1 B ASP 838  ? OD2 ? B ASP 840  OD2 
394 1 Y 1 B GLU 854  ? CG  ? B GLU 856  CG  
395 1 Y 1 B GLU 854  ? CD  ? B GLU 856  CD  
396 1 Y 1 B GLU 854  ? OE1 ? B GLU 856  OE1 
397 1 Y 1 B GLU 854  ? OE2 ? B GLU 856  OE2 
398 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
399 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
400 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
401 1 Y 1 B GLU 890  ? CG  ? B GLU 892  CG  
402 1 Y 1 B GLU 890  ? CD  ? B GLU 892  CD  
403 1 Y 1 B GLU 890  ? OE1 ? B GLU 892  OE1 
404 1 Y 1 B GLU 890  ? OE2 ? B GLU 892  OE2 
405 1 Y 1 B GLU 917  ? CG  ? B GLU 919  CG  
406 1 Y 1 B GLU 917  ? CD  ? B GLU 919  CD  
407 1 Y 1 B GLU 917  ? OE1 ? B GLU 919  OE1 
408 1 Y 1 B GLU 917  ? OE2 ? B GLU 919  OE2 
409 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
410 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
411 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
412 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
413 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
414 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
415 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
416 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
417 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
418 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
419 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
420 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
421 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
422 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
423 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
424 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
425 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
426 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
427 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
428 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
429 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
430 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
431 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
432 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
433 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
434 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
435 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
436 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
437 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
438 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
439 1 Y 1 B ARG 1091 ? CG  ? B ARG 1093 CG  
440 1 Y 1 B ARG 1091 ? CD  ? B ARG 1093 CD  
441 1 Y 1 B ARG 1091 ? NE  ? B ARG 1093 NE  
442 1 Y 1 B ARG 1091 ? CZ  ? B ARG 1093 CZ  
443 1 Y 1 B ARG 1091 ? NH1 ? B ARG 1093 NH1 
444 1 Y 1 B ARG 1091 ? NH2 ? B ARG 1093 NH2 
445 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
446 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
447 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
448 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
449 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
450 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
451 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
452 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
453 1 Y 1 B LEU 1147 ? CG  ? B LEU 1149 CG  
454 1 Y 1 B LEU 1147 ? CD1 ? B LEU 1149 CD1 
455 1 Y 1 B LEU 1147 ? CD2 ? B LEU 1149 CD2 
456 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
457 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
458 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
459 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
460 1 Y 1 B MET 1230 ? CG  ? B MET 1232 CG  
461 1 Y 1 B MET 1230 ? SD  ? B MET 1232 SD  
462 1 Y 1 B MET 1230 ? CE  ? B MET 1232 CE  
# 
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                   106.38 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9E0D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.286 
_cell.length_a_esd                 ? 
_cell.length_b                     101.515 
_cell.length_b_esd                 ? 
_cell.length_c                     125.584 
_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                         9E0D 
_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                   9E0D 
_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, 0.2 M ammonium sulfate, and 18% (w/v) PEG 3350. Enzyme was incubated with 12 mM piperonyl alcohol. Crystal was soaked in cryobuffer containing 25 mM piperonyl alcohol 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         2023-12-16 
_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   1.00008 
_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        1.00008 
_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                                       9E0D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.33 
_reflns.d_resolution_low                               48.11 
_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                                     1017897 
_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                           93.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.90 
_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                                0.070 
_reflns.pdbx_Rpim_I_all                                0.026 
_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                              0.065 
_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                                    1.33 
_reflns_shell.d_res_low                                     1.35 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           107455 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             17707 
_reflns_shell.percent_possible_obs                          65.2 
_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                               6.1 
_reflns_shell.pdbx_chi_squared                              0.58 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.6 
_reflns_shell.pdbx_Rrim_I_all                               2.299 
_reflns_shell.pdbx_Rpim_I_all                               0.913 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.353 
_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                                  2.102 
_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                                 9E0D 
_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                            1.33 
_refine.ls_d_res_low                             46.78 
_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                     1017897 
_refine.ls_number_reflns_R_free                  50607 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.22 
_refine.ls_percent_reflns_R_free                 4.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1757 
_refine.ls_R_factor_R_free                       0.1930 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1748 
_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                          0.06 
_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                 23.17 
_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                            0.16 
_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        17748 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         310 
_refine_hist.number_atoms_solvent             2387 
_refine_hist.number_atoms_total               20445 
_refine_hist.d_res_high                       1.33 
_refine_hist.d_res_low                        46.78 
# 
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' ? 0.005  ? 18656 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.908  ? 25486 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.038 ? 6919  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.069  ? 2993  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3313  ? 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' 1.33 1.35  . . 1145 21674 63.00  . . . . 0.3482 . . . . . . . . . . . 0.3415 
'X-RAY DIFFRACTION' 1.35 1.36  . . 1245 23618 68.00  . . . . 0.3356 . . . . . . . . . . . 0.3347 
'X-RAY DIFFRACTION' 1.36 1.38  . . 1339 26465 76.00  . . . . 0.3247 . . . . . . . . . . . 0.3337 
'X-RAY DIFFRACTION' 1.38 1.39  . . 1556 30470 88.00  . . . . 0.3148 . . . . . . . . . . . 0.3381 
'X-RAY DIFFRACTION' 1.39 1.41  . . 1661 32218 93.00  . . . . 0.3041 . . . . . . . . . . . 0.3158 
'X-RAY DIFFRACTION' 1.41 1.43  . . 1736 32740 95.00  . . . . 0.2889 . . . . . . . . . . . 0.3169 
'X-RAY DIFFRACTION' 1.43 1.45  . . 1702 33084 96.00  . . . . 0.2748 . . . . . . . . . . . 0.2962 
'X-RAY DIFFRACTION' 1.45 1.47  . . 1720 33163 96.00  . . . . 0.2636 . . . . . . . . . . . 0.2788 
'X-RAY DIFFRACTION' 1.47 1.50  . . 1740 33340 96.00  . . . . 0.2498 . . . . . . . . . . . 0.2710 
'X-RAY DIFFRACTION' 1.50 1.52  . . 1667 33303 96.00  . . . . 0.2405 . . . . . . . . . . . 0.2518 
'X-RAY DIFFRACTION' 1.52 1.55  . . 1698 33436 96.00  . . . . 0.2282 . . . . . . . . . . . 0.2562 
'X-RAY DIFFRACTION' 1.55 1.58  . . 1746 33129 96.00  . . . . 0.2216 . . . . . . . . . . . 0.2376 
'X-RAY DIFFRACTION' 1.58 1.61  . . 1661 33545 97.00  . . . . 0.2130 . . . . . . . . . . . 0.2379 
'X-RAY DIFFRACTION' 1.61 1.64  . . 1799 33427 97.00  . . . . 0.2047 . . . . . . . . . . . 0.2264 
'X-RAY DIFFRACTION' 1.64 1.68  . . 1768 33396 97.00  . . . . 0.2031 . . . . . . . . . . . 0.2292 
'X-RAY DIFFRACTION' 1.68 1.71  . . 1726 33534 97.00  . . . . 0.2108 . . . . . . . . . . . 0.2306 
'X-RAY DIFFRACTION' 1.71 1.76  . . 1743 33470 97.00  . . . . 0.2018 . . . . . . . . . . . 0.2167 
'X-RAY DIFFRACTION' 1.76 1.81  . . 1822 32972 96.00  . . . . 0.1944 . . . . . . . . . . . 0.2289 
'X-RAY DIFFRACTION' 1.81 1.86  . . 1593 30403 88.00  . . . . 0.1844 . . . . . . . . . . . 0.2108 
'X-RAY DIFFRACTION' 1.86 1.92  . . 1784 33451 97.00  . . . . 0.1861 . . . . . . . . . . . 0.2100 
'X-RAY DIFFRACTION' 1.92 1.99  . . 1784 33948 98.00  . . . . 0.1830 . . . . . . . . . . . 0.2023 
'X-RAY DIFFRACTION' 1.99 2.07  . . 1765 33888 98.00  . . . . 0.1757 . . . . . . . . . . . 0.2028 
'X-RAY DIFFRACTION' 2.07 2.16  . . 1767 34090 98.00  . . . . 0.1674 . . . . . . . . . . . 0.1873 
'X-RAY DIFFRACTION' 2.16 2.27  . . 1773 33843 98.00  . . . . 0.1680 . . . . . . . . . . . 0.1988 
'X-RAY DIFFRACTION' 2.27 2.42  . . 1821 33853 98.00  . . . . 0.1662 . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 2.42 2.60  . . 1710 33942 98.00  . . . . 0.1663 . . . . . . . . . . . 0.1884 
'X-RAY DIFFRACTION' 2.60 2.87  . . 1804 33478 97.00  . . . . 0.1672 . . . . . . . . . . . 0.1898 
'X-RAY DIFFRACTION' 2.87 3.28  . . 1796 32819 95.00  . . . . 0.1626 . . . . . . . . . . . 0.1731 
'X-RAY DIFFRACTION' 3.28 4.13  . . 1764 32035 93.00  . . . . 0.1398 . . . . . . . . . . . 0.1515 
'X-RAY DIFFRACTION' 4.13 46.78 . . 1772 34556 100.00 . . . . 0.1403 . . . . . . . . . . . 0.1553 
# 
_struct.entry_id                     9E0D 
_struct.title                        'Structure of proline utilization A complexed with piperonyl alcohol' 
_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        9E0D 
_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 4  ? 
G  N N 5  ? 
H  N N 6  ? 
I  N N 7  ? 
J  N N 7  ? 
K  N N 7  ? 
L  N N 7  ? 
M  N N 7  ? 
N  N N 8  ? 
O  N N 2  ? 
P  N N 4  ? 
Q  N N 3  ? 
R  N N 9  ? 
S  N N 10 ? 
T  N N 4  ? 
U  N N 5  ? 
V  N N 6  ? 
W  N N 7  ? 
X  N N 8  ? 
Y  N N 10 ? 
Z  N N 11 ? 
AA N N 11 ? 
# 
_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 9E0D A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9E0D 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 9E0D SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9E0D MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9E0D SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9E0D 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)' 12020 ? 
1 MORE         -145  ? 
1 'SSA (A^2)'  76750 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,Z                            
3 1 B,O,P,Q,R,S,T,U,V,W,X,Y,AA                             
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 SER A 31   ? ALA A 40   ? SER A 29   ALA A 38   1 ? 10 
HELX_P HELX_P2   AA2 PRO A 44   ? THR A 57   ? PRO A 42   THR A 55   1 ? 14 
HELX_P HELX_P3   AA3 SER A 59   ? GLY A 79   ? SER A 57   GLY A 77   1 ? 21 
HELX_P HELX_P4   AA4 GLY A 85   ? TYR A 93   ? GLY A 83   TYR A 91   1 ? 9  
HELX_P HELX_P5   AA5 SER A 96   ? ARG A 112  ? SER A 94   ARG A 110  1 ? 17 
HELX_P HELX_P6   AA6 ASP A 115  ? LYS A 126  ? ASP A 113  LYS A 124  1 ? 12 
HELX_P HELX_P7   AA7 ASN A 131  ? LEU A 136  ? ASN A 129  LEU A 134  1 ? 6  
HELX_P HELX_P8   AA8 ASN A 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P9   AA9 ASN A 162  ? GLN A 196  ? ASN A 160  GLN A 194  1 ? 35 
HELX_P HELX_P10  AB1 THR A 202  ? GLY A 217  ? THR A 200  GLY A 215  1 ? 16 
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 THR A 480  ? ALA A 486  ? THR A 478  ALA A 484  1 ? 7  
HELX_P HELX_P25  AC7 TYR A 487  ? LEU A 493  ? TYR A 485  LEU A 491  1 ? 7  
HELX_P HELX_P26  AC8 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P27  AC9 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P28  AD1 ASP A 518  ? ALA A 525  ? ASP A 516  ALA A 523  1 ? 8  
HELX_P HELX_P29  AD2 LEU A 538  ? LEU A 542  ? LEU A 536  LEU A 540  5 ? 5  
HELX_P HELX_P30  AD3 ASN A 557  ? ALA A 573  ? ASN A 555  ALA A 571  1 ? 17 
HELX_P HELX_P31  AD4 SER A 611  ? ALA A 631  ? SER A 609  ALA A 629  1 ? 21 
HELX_P HELX_P32  AD5 PRO A 633  ? GLY A 664  ? PRO A 631  GLY A 662  1 ? 32 
HELX_P HELX_P33  AD6 SER A 666  ? LEU A 692  ? SER A 664  LEU A 690  1 ? 27 
HELX_P HELX_P34  AD7 LEU A 712  ? ALA A 725  ? LEU A 710  ALA A 723  1 ? 14 
HELX_P HELX_P35  AD8 THR A 737  ? ALA A 751  ? THR A 735  ALA A 749  1 ? 15 
HELX_P HELX_P36  AD9 ASP A 764  ? ALA A 774  ? ASP A 762  ALA A 772  1 ? 11 
HELX_P HELX_P37  AE1 SER A 785  ? ASP A 798  ? SER A 783  ASP A 796  1 ? 14 
HELX_P HELX_P38  AE2 LEU A 826  ? ASP A 840  ? LEU A 824  ASP A 838  1 ? 15 
HELX_P HELX_P39  AE3 SER A 841  ? GLN A 844  ? SER A 839  GLN A 842  5 ? 4  
HELX_P HELX_P40  AE4 GLU A 856  ? HIS A 871  ? GLU A 854  HIS A 869  1 ? 16 
HELX_P HELX_P41  AE5 THR A 890  ? LEU A 907  ? THR A 888  LEU A 905  1 ? 18 
HELX_P HELX_P42  AE6 ALA A 917  ? GLY A 923  ? ALA A 915  GLY A 921  5 ? 7  
HELX_P HELX_P43  AE7 LYS A 935  ? LEU A 939  ? LYS A 933  LEU A 937  5 ? 5  
HELX_P HELX_P44  AE8 ARG A 954  ? ASP A 956  ? ARG A 952  ASP A 954  5 ? 3  
HELX_P HELX_P45  AE9 ASP A 957  ? THR A 968  ? ASP A 955  THR A 966  1 ? 12 
HELX_P HELX_P46  AF1 LEU A 980  ? ILE A 991  ? LEU A 978  ILE A 989  1 ? 12 
HELX_P HELX_P47  AF2 ARG A 1015 ? GLY A 1019 ? ARG A 1013 GLY A 1017 5 ? 5  
HELX_P HELX_P48  AF3 TYR A 1029 ? VAL A 1034 ? TYR A 1027 VAL A 1032 5 ? 6  
HELX_P HELX_P49  AF4 ASP A 1049 ? LYS A 1062 ? ASP A 1047 LYS A 1060 1 ? 14 
HELX_P HELX_P50  AF5 ALA A 1064 ? SER A 1078 ? ALA A 1062 SER A 1076 1 ? 15 
HELX_P HELX_P51  AF6 THR A 1110 ? THR A 1124 ? THR A 1108 THR A 1122 1 ? 15 
HELX_P HELX_P52  AF7 ALA A 1133 ? GLY A 1135 ? ALA A 1131 GLY A 1133 5 ? 3  
HELX_P HELX_P53  AF8 LEU A 1136 ? LYS A 1141 ? LEU A 1134 LYS A 1139 5 ? 6  
HELX_P HELX_P54  AF9 PRO A 1144 ? LEU A 1149 ? PRO A 1142 LEU A 1147 1 ? 6  
HELX_P HELX_P55  AG1 ASP A 1156 ? GLY A 1161 ? ASP A 1154 GLY A 1159 1 ? 6  
HELX_P HELX_P56  AG2 ASP A 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P57  AG3 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P58  AG4 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
HELX_P HELX_P59  AG5 ALA A 1229 ? ILE A 1234 ? ALA A 1227 ILE A 1232 5 ? 6  
HELX_P HELX_P60  AG6 SER B 31   ? ALA B 40   ? SER B 29   ALA B 38   1 ? 10 
HELX_P HELX_P61  AG7 PRO B 44   ? THR B 57   ? PRO B 42   THR B 55   1 ? 14 
HELX_P HELX_P62  AG8 SER B 59   ? GLY B 79   ? SER B 57   GLY B 77   1 ? 21 
HELX_P HELX_P63  AG9 VAL B 86   ? SER B 94   ? VAL B 84   SER B 92   1 ? 9  
HELX_P HELX_P64  AH1 SER B 96   ? ARG B 112  ? SER B 94   ARG B 110  1 ? 17 
HELX_P HELX_P65  AH2 ASP B 115  ? LYS B 126  ? ASP B 113  LYS B 124  1 ? 12 
HELX_P HELX_P66  AH3 ASN B 145  ? GLY B 155  ? ASN B 143  GLY B 153  1 ? 11 
HELX_P HELX_P67  AH4 ASN B 162  ? GLN B 196  ? ASN B 160  GLN B 194  1 ? 35 
HELX_P HELX_P68  AH5 THR B 202  ? GLY B 217  ? THR B 200  GLY B 215  1 ? 16 
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  ? ASP B 328  ? ARG B 312  ASP B 326  1 ? 15 
HELX_P HELX_P76  AI4 GLY B 329  ? SER B 332  ? GLY B 327  SER B 330  5 ? 4  
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  ? GLY B 387  ? TYR B 373  GLY B 385  1 ? 13 
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  ? ALA B 437  ? ASN B 424  ALA B 435  1 ? 12 
HELX_P HELX_P81  AI9 GLY B 455  ? GLU B 460  ? GLY B 453  GLU B 458  1 ? 6  
HELX_P HELX_P82  AJ1 THR B 480  ? ALA B 486  ? THR B 478  ALA B 484  1 ? 7  
HELX_P HELX_P83  AJ2 LEU B 488  ? GLU B 494  ? LEU B 486  GLU B 492  1 ? 7  
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  ? ASP B 798  ? SER B 783  ASP B 796  1 ? 14 
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 GLU B 919  ? GLY B 923  ? GLU B 917  GLY B 921  5 ? 5  
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  
HELX_P HELX_P120 AN3 ASN B 1228 ? ALA B 1233 ? ASN B 1226 ALA B 1231 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? H NAD . O2A ? ? ? 1_555 N  MG  . MG ? ? A NAD 1306 A MG  1312 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
metalc2  metalc ? ? N MG  . MG  ? ? ? 1_555 Z  HOH . O  ? ? A MG  1312 A HOH 1546 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
metalc3  metalc ? ? N MG  . MG  ? ? ? 1_555 Z  HOH . O  ? ? A MG  1312 A HOH 1628 1_555 ? ? ? ? ? ? ? 2.190 ? ? 
metalc4  metalc ? ? N MG  . MG  ? ? ? 1_555 Z  HOH . O  ? ? A MG  1312 A HOH 2061 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
metalc5  metalc ? ? N MG  . MG  ? ? ? 1_555 Z  HOH . O  ? ? A MG  1312 A HOH 2251 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc6  metalc ? ? N MG  . MG  ? ? ? 1_555 Z  HOH . O  ? ? A MG  1312 A HOH 2380 1_555 ? ? ? ? ? ? ? 1.974 ? ? 
metalc7  metalc ? ? V NAD . O2A ? ? ? 1_555 X  MG  . MG ? ? B NAD 1308 B MG  1310 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc8  metalc ? ? X MG  . MG  ? ? ? 1_555 AA HOH . O  ? ? B MG  1310 B HOH 1583 1_555 ? ? ? ? ? ? ? 1.898 ? ? 
metalc9  metalc ? ? X MG  . MG  ? ? ? 1_555 AA HOH . O  ? ? B MG  1310 B HOH 1929 1_555 ? ? ? ? ? ? ? 1.891 ? ? 
metalc10 metalc ? ? X MG  . MG  ? ? ? 1_555 AA HOH . O  ? ? B MG  1310 B HOH 2037 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc11 metalc ? ? X MG  . MG  ? ? ? 1_555 AA HOH . O  ? ? B MG  1310 B HOH 2121 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc12 metalc ? ? X MG  . MG  ? ? ? 1_555 AA HOH . O  ? ? B MG  1310 B HOH 2339 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? H  NAD . ? A NAD 1306 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 1546 ? 1_555 84.7  ? 
2  O2A ? H  NAD . ? A NAD 1306 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 1628 ? 1_555 89.6  ? 
3  O   ? Z  HOH . ? A HOH 1546 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 1628 ? 1_555 92.5  ? 
4  O2A ? H  NAD . ? A NAD 1306 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2061 ? 1_555 88.2  ? 
5  O   ? Z  HOH . ? A HOH 1546 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2061 ? 1_555 94.2  ? 
6  O   ? Z  HOH . ? A HOH 1628 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2061 ? 1_555 172.7 ? 
7  O2A ? H  NAD . ? A NAD 1306 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2251 ? 1_555 89.8  ? 
8  O   ? Z  HOH . ? A HOH 1546 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2251 ? 1_555 172.4 ? 
9  O   ? Z  HOH . ? A HOH 1628 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2251 ? 1_555 82.3  ? 
10 O   ? Z  HOH . ? A HOH 2061 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2251 ? 1_555 90.7  ? 
11 O2A ? H  NAD . ? A NAD 1306 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2380 ? 1_555 173.9 ? 
12 O   ? Z  HOH . ? A HOH 1546 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2380 ? 1_555 89.5  ? 
13 O   ? Z  HOH . ? A HOH 1628 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2380 ? 1_555 89.0  ? 
14 O   ? Z  HOH . ? A HOH 2061 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2380 ? 1_555 93.9  ? 
15 O   ? Z  HOH . ? A HOH 2251 ? 1_555 MG ? N MG . ? A MG 1312 ? 1_555 O ? Z  HOH . ? A HOH 2380 ? 1_555 95.9  ? 
16 O2A ? V  NAD . ? B NAD 1308 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 1583 ? 1_555 97.4  ? 
17 O2A ? V  NAD . ? B NAD 1308 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 1929 ? 1_555 95.2  ? 
18 O   ? AA HOH . ? B HOH 1583 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 1929 ? 1_555 122.4 ? 
19 O2A ? V  NAD . ? B NAD 1308 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2037 ? 1_555 80.7  ? 
20 O   ? AA HOH . ? B HOH 1583 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2037 ? 1_555 90.2  ? 
21 O   ? AA HOH . ? B HOH 1929 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2037 ? 1_555 147.4 ? 
22 O2A ? V  NAD . ? B NAD 1308 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2121 ? 1_555 86.6  ? 
23 O   ? AA HOH . ? B HOH 1583 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2121 ? 1_555 151.6 ? 
24 O   ? AA HOH . ? B HOH 1929 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2121 ? 1_555 85.0  ? 
25 O   ? AA HOH . ? B HOH 2037 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2121 ? 1_555 62.5  ? 
26 O2A ? V  NAD . ? B NAD 1308 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2339 ? 1_555 165.5 ? 
27 O   ? AA HOH . ? B HOH 1583 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2339 ? 1_555 89.5  ? 
28 O   ? AA HOH . ? B HOH 1929 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2339 ? 1_555 91.8  ? 
29 O   ? AA HOH . ? B HOH 2037 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2339 ? 1_555 86.6  ? 
30 O   ? AA HOH . ? B HOH 2121 ? 1_555 MG ? X MG . ? B MG 1310 ? 1_555 O ? AA HOH . ? B HOH 2339 ? 1_555 81.4  ? 
# 
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 -3.14 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 0.34  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -3.81 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 2.85  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9  ? 
AA2 ? 3  ? 
AA3 ? 2  ? 
AA4 ? 5  ? 
AA5 ? 10 ? 
AA6 ? 5  ? 
AA7 ? 9  ? 
AA8 ? 3  ? 
AA9 ? 2  ? 
AB1 ? 5  ? 
AB2 ? 10 ? 
AB3 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? parallel      
AA1 8 9  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA5 1 2  ? anti-parallel 
AA5 2 3  ? parallel      
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
AA5 6 7  ? parallel      
AA5 7 8  ? parallel      
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? parallel      
AA6 2 3  ? parallel      
AA6 3 4  ? parallel      
AA6 4 5  ? parallel      
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? parallel      
AA7 8 9  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AB1 1 2  ? parallel      
AB1 2 3  ? parallel      
AB1 3 4  ? parallel      
AB1 4 5  ? parallel      
AB2 1 2  ? anti-parallel 
AB2 2 3  ? parallel      
AB2 3 4  ? parallel      
AB2 4 5  ? parallel      
AB2 5 6  ? parallel      
AB2 6 7  ? parallel      
AB2 7 8  ? parallel      
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? parallel      
AB3 2 3  ? parallel      
AB3 3 4  ? parallel      
AB3 4 5  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA1 2  GLY A 263  ? ILE A 266  ? GLY A 261  ILE A 264  
AA1 3  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  ? PRO A 477  ? CYS A 470  PRO A 475  
AA1 9  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA2 1  TRP A 576  ? ALA A 578  ? TRP A 574  ALA A 576  
AA2 2  ASP A 599  ? THR A 608  ? ASP A 597  THR A 606  
AA2 3  THR A 591  ? ASN A 596  ? THR A 589  ASN A 594  
AA3 1  GLN A 581  ? LEU A 582  ? GLN A 579  LEU A 580  
AA3 2  GLY A 585  ? PRO A 586  ? GLY A 583  PRO A 584  
AA4 1  LEU A 758  ? LEU A 760  ? LEU A 756  LEU A 758  
AA4 2  VAL A 729  ? LYS A 732  ? VAL A 727  LYS A 730  
AA4 3  ILE A 702  ? ILE A 705  ? ILE A 700  ILE A 703  
AA4 4  GLY A 779  ? THR A 783  ? GLY A 777  THR A 781  
AA4 5  LEU A 809  ? GLU A 812  ? LEU A 807  GLU A 810  
AA5 1  VAL A 911  ? GLN A 913  ? VAL A 909  GLN A 911  
AA5 2  THR A 929  ? GLU A 932  ? THR A 927  GLU A 930  
AA5 3  VAL A 947  ? TYR A 953  ? VAL A 945  TYR A 951  
AA5 4  LEU A 849  ? GLN A 855  ? LEU A 847  GLN A 853  
AA5 5  ASN A 817  ? VAL A 821  ? ASN A 815  VAL A 819  
AA5 6  THR A 973  ? HIS A 977  ? THR A 971  HIS A 975  
AA5 7  ASN A 995  ? ILE A 998  ? ASN A 993  ILE A 996  
AA5 8  VAL A 1213 ? ASN A 1221 ? VAL A 1211 ASN A 1219 
AA5 9  GLU A 1092 ? ALA A 1100 ? GLU A 1090 ALA A 1098 
AA5 10 ASP A 1083 ? LEU A 1086 ? ASP A 1081 LEU A 1084 
AA6 1  VAL A 1151 ? SER A 1154 ? VAL A 1149 SER A 1152 
AA6 2  SER A 1127 ? ASP A 1131 ? SER A 1125 ASP A 1129 
AA6 3  ARG A 1103 ? VAL A 1107 ? ARG A 1101 VAL A 1105 
AA6 4  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  SER B 219  ? ASP B 223  ? SER B 217  ASP B 221  
AA7 2  GLY B 263  ? ILE B 266  ? GLY B 261  ILE B 264  
AA7 3  LEU B 305  ? ILE B 307  ? LEU B 303  ILE B 305  
AA7 4  MET B 337  ? GLN B 342  ? MET B 335  GLN B 340  
AA7 5  ILE B 366  ? VAL B 371  ? ILE B 364  VAL B 369  
AA7 6  VAL B 418  ? ALA B 423  ? VAL B 416  ALA B 421  
AA7 7  GLU B 447  ? LEU B 451  ? GLU B 445  LEU B 449  
AA7 8  CYS B 472  ? PRO B 477  ? CYS B 470  PRO B 475  
AA7 9  SER B 219  ? ASP B 223  ? SER B 217  ASP B 221  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? GLU B 609  ? ASP B 597  GLU B 607  
AA8 3  GLU B 590  ? ASN B 596  ? GLU B 588  ASN B 594  
AA9 1  GLN B 581  ? LEU B 582  ? GLN B 579  LEU B 580  
AA9 2  GLY B 585  ? PRO B 586  ? GLY B 583  PRO B 584  
AB1 1  LEU B 758  ? LEU B 760  ? LEU B 756  LEU B 758  
AB1 2  VAL B 729  ? LYS B 732  ? VAL B 727  LYS B 730  
AB1 3  ILE B 702  ? ILE B 705  ? ILE B 700  ILE B 703  
AB1 4  GLY B 779  ? THR B 783  ? GLY B 777  THR B 781  
AB1 5  LEU B 809  ? GLU B 812  ? LEU B 807  GLU B 810  
AB2 1  VAL B 911  ? GLN B 913  ? VAL B 909  GLN B 911  
AB2 2  THR B 929  ? GLU B 932  ? THR B 927  GLU B 930  
AB2 3  VAL B 947  ? TYR B 953  ? VAL B 945  TYR B 951  
AB2 4  LEU B 849  ? GLN B 855  ? LEU B 847  GLN B 853  
AB2 5  ASN B 817  ? VAL B 821  ? ASN B 815  VAL B 819  
AB2 6  THR B 973  ? HIS B 977  ? THR B 971  HIS B 975  
AB2 7  ASN B 995  ? ILE B 998  ? ASN B 993  ILE B 996  
AB2 8  VAL B 1213 ? ASN B 1221 ? VAL B 1211 ASN B 1219 
AB2 9  GLU B 1092 ? ALA B 1100 ? GLU B 1090 ALA B 1098 
AB2 10 ASP B 1083 ? LEU B 1086 ? ASP B 1081 LEU B 1084 
AB3 1  VAL B 1151 ? SER B 1154 ? VAL B 1149 SER B 1152 
AB3 2  SER B 1127 ? ASP B 1131 ? SER B 1125 ASP B 1129 
AB3 3  ARG B 1103 ? VAL B 1107 ? ARG B 1101 VAL B 1105 
AB3 4  ALA B 1166 ? GLU B 1169 ? ALA B 1164 GLU B 1167 
AB3 5  VAL B 1192 ? ALA B 1195 ? VAL B 1190 ALA B 1193 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N TYR A 222  ? N TYR A 220  O SER A 265  ? O SER A 263  
AA1 2 3  N ILE A 266  ? N ILE A 264  O ASN A 306  ? O ASN A 304  
AA1 3 4  N LEU A 305  ? N LEU A 303  O GLY A 338  ? O GLY A 336  
AA1 4 5  N PHE A 339  ? N PHE A 337  O MET A 367  ? O MET A 365  
AA1 5 6  N LEU A 370  ? N LEU A 368  O GLN A 421  ? O GLN A 419  
AA1 6 7  N PHE A 422  ? N PHE A 420  O GLU A 447  ? O GLU A 445  
AA1 7 8  N CYS A 450  ? N CYS A 448  O TYR A 475  ? O TYR A 473  
AA1 8 9  O ILE A 474  ? O ILE A 472  N SER A 219  ? N SER A 217  
AA2 1 2  N ALA A 578  ? N ALA A 576  O THR A 608  ? O THR A 606  
AA2 2 3  O GLY A 605  ? O GLY A 603  N VAL A 594  ? N VAL A 592  
AA3 1 2  N LEU A 582  ? N LEU A 580  O GLY A 585  ? O GLY A 583  
AA4 1 2  O GLN A 759  ? O GLN A 757  N ALA A 731  ? N ALA A 729  
AA4 2 3  O LYS A 732  ? O LYS A 730  N CYS A 704  ? N CYS A 702  
AA4 3 4  N ILE A 705  ? N ILE A 703  O MET A 781  ? O MET A 779  
AA4 4 5  N PHE A 782  ? N PHE A 780  O ILE A 810  ? O ILE A 808  
AA5 1 2  N GLU A 912  ? N GLU A 910  O ILE A 930  ? O ILE A 928  
AA5 2 3  N ILE A 931  ? N ILE A 929  O LEU A 948  ? O LEU A 946  
AA5 3 4  O HIS A 949  ? O HIS A 947  N LEU A 852  ? N LEU A 850  
AA5 4 5  O CYS A 853  ? O CYS A 851  N MET A 819  ? N MET A 817  
AA5 5 6  N ILE A 820  ? N ILE A 818  O HIS A 977  ? O HIS A 975  
AA5 6 7  N LEU A 976  ? N LEU A 974  O TYR A 997  ? O TYR A 995  
AA5 7 8  N LEU A 996  ? N LEU A 994  O SER A 1217 ? O SER A 1215 
AA5 8 9  O ALA A 1218 ? O ALA A 1216 N LEU A 1095 ? N LEU A 1093 
AA5 9 10 O TYR A 1096 ? O TYR A 1094 N LEU A 1084 ? N LEU A 1082 
AA6 1 2  O SER A 1152 ? O SER A 1150 N ILE A 1130 ? N ILE A 1128 
AA6 2 3  O ALA A 1129 ? O ALA A 1127 N LEU A 1106 ? N LEU A 1104 
AA6 3 4  N VAL A 1107 ? N VAL A 1105 O LEU A 1167 ? O LEU A 1165 
AA6 4 5  N VAL A 1168 ? N VAL A 1166 O GLN A 1193 ? O GLN A 1191 
AA7 1 2  N TYR B 222  ? N TYR B 220  O SER B 265  ? O SER B 263  
AA7 2 3  N ILE B 266  ? N ILE B 264  O ASN B 306  ? O ASN B 304  
AA7 3 4  N LEU B 305  ? N LEU B 303  O GLY B 338  ? O GLY B 336  
AA7 4 5  N MET B 337  ? N MET B 335  O MET B 367  ? O MET B 365  
AA7 5 6  N VAL B 368  ? N VAL B 366  O GLN B 421  ? O GLN B 419  
AA7 6 7  N PHE B 422  ? N PHE B 420  O GLU B 447  ? O GLU B 445  
AA7 7 8  N CYS B 450  ? N CYS B 448  O TYR B 475  ? O TYR B 473  
AA7 8 9  O ILE B 474  ? O ILE B 472  N SER B 219  ? N SER B 217  
AA8 1 2  N ALA B 578  ? N ALA B 576  O THR B 608  ? O THR B 606  
AA8 2 3  O GLU B 609  ? O GLU B 607  N GLU B 590  ? N GLU B 588  
AA9 1 2  N LEU B 582  ? N LEU B 580  O GLY B 585  ? O GLY B 583  
AB1 1 2  O GLN B 759  ? O GLN B 757  N ALA B 731  ? N ALA B 729  
AB1 2 3  O 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 THR B 929  ? N THR B 927  O LEU B 948  ? O LEU B 946  
AB2 3 4  O HIS B 949  ? O HIS B 947  N LEU B 852  ? N LEU B 850  
AB2 4 5  O CYS B 853  ? O CYS B 851  N MET B 819  ? N MET B 817  
AB2 5 6  N ILE B 820  ? N ILE B 818  O HIS B 977  ? O HIS B 975  
AB2 6 7  N LEU B 976  ? N LEU B 974  O TYR B 997  ? O TYR B 995  
AB2 7 8  N LEU B 996  ? N LEU B 994  O SER B 1217 ? O SER B 1215 
AB2 8 9  O 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                   9E0D 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE1 B GLN 793  ? ? O B HOH 1401 ? ? 2.04 
2  1 O   A HOH 2378 ? ? O A HOH 2514 ? ? 2.05 
3  1 O   A HOH 1822 ? ? O A HOH 2031 ? ? 2.05 
4  1 OD1 A ASP 796  ? ? O A HOH 1401 ? ? 2.08 
5  1 OE1 A GLN 793  ? ? O A HOH 1402 ? ? 2.11 
6  1 OE1 B GLU 674  ? A O B HOH 1402 ? ? 2.12 
7  1 O   A HOH 2051 ? ? O A HOH 2509 ? ? 2.14 
8  1 O   B HOH 1569 ? ? O B HOH 2492 ? ? 2.17 
9  1 O   A HOH 2101 ? ? O A HOH 2367 ? ? 2.18 
10 1 O   A HOH 2163 ? ? O A HOH 2464 ? ? 2.18 
11 1 OE1 A GLU 458  ? ? O A HOH 1403 ? ? 2.18 
12 1 O   B HOH 1493 ? ? O B HOH 1563 ? ? 2.19 
13 1 O   B HOH 1828 ? ? O B HOH 2426 ? ? 2.19 
14 1 O   B HOH 2033 ? ? O B HOH 2263 ? ? 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     1404 
_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     2250 
_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              2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 22   ? ? -157.81 56.66   
2  1 ASN A 129  ? ? -64.08  93.27   
3  1 GLU A 225  ? ? -172.10 145.62  
4  1 GLU A 308  ? ? -119.38 -135.65 
5  1 MET A 452  ? ? -151.05 -48.01  
6  1 LYS A 465  ? ? -117.97 -124.26 
7  1 ASP A 597  ? ? -170.92 98.65   
8  1 HIS A 694  ? ? -103.97 79.00   
9  1 THR A 811  ? ? -124.13 -155.25 
10 1 GLN A 842  ? ? -94.60  51.14   
11 1 GLN A 938  ? ? -102.80 -71.80  
12 1 LEU A 970  ? ? -97.55  -87.08  
13 1 GLN A 1008 ? ? -118.91 77.79   
14 1 ALA B 22   ? ? -156.63 61.32   
15 1 ASP B 127  ? ? -91.31  41.94   
16 1 HIS B 133  ? ? 177.81  159.74  
17 1 GLU B 308  ? ? -116.64 -135.76 
18 1 MET B 452  ? ? -138.29 -44.90  
19 1 VAL B 460  ? ? -121.46 -52.20  
20 1 LYS B 465  ? ? -119.39 -128.54 
21 1 TYR B 485  ? ? -164.36 22.07   
22 1 ASP B 597  ? ? -169.33 99.30   
23 1 THR B 689  ? ? -131.11 -42.39  
24 1 HIS B 694  ? ? -102.53 76.10   
25 1 PHE B 708  ? ? -119.55 74.27   
26 1 THR B 811  ? ? -126.14 -153.70 
27 1 GLN B 842  ? ? -93.01  53.92   
28 1 LEU B 970  ? ? -98.40  -87.41  
29 1 VAL B 1007 ? ? -120.79 -50.50  
30 1 GLN B 1008 ? ? -115.64 78.23   
31 1 ASP B 1154 ? ? -158.47 89.98   
# 
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 -25.6237 66.3226 92.4702 0.1555 ? 0.0187  ? 0.0106  ? 0.1318 ? 0.0034  ? 0.1406 ? 0.6665 ? -0.0247 
? 0.1534 ? 0.1003 ? -0.0030 ? 0.1647 ? -0.0388 ? -0.1073 ? 0.0089  ? 0.0336 ? 0.0370 ? 0.0105  ? -0.0173 ? -0.0066 ? 0.0017  ? 
2 'X-RAY DIFFRACTION' ? refined 5.7445   31.8809 90.8267 0.1075 ? -0.0050 ? -0.0026 ? 0.1466 ? -0.0165 ? 0.1225 ? 0.1750 ? -0.0188 
? 0.0918 ? 0.2265 ? -0.0462 ? 0.4228 ? 0.0136  ? -0.0391 ? -0.0078 ? 0.0484 ? 0.0059 ? -0.0027 ? 0.0463  ? -0.1078 ? -0.0229 ? 
# 
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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2599 ? 5.85 . 
2 1 O ? A HOH 2600 ? 5.86 . 
# 
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 SER 80  ? A SER 82  
17 1 Y 1 A GLY 81  ? A GLY 83  
18 1 Y 1 A GLY 135 ? A GLY 137 
19 1 Y 1 A GLY 136 ? A GLY 138 
20 1 Y 1 A GLU 492 ? A GLU 494 
21 1 Y 1 A ASN 493 ? A ASN 495 
22 1 Y 1 B SER -1  ? B SER 1   
23 1 Y 1 B MET 0   ? B MET 2   
24 1 Y 1 B MET 1   ? B MET 3   
25 1 Y 1 B SER 2   ? B SER 4   
26 1 Y 1 B PRO 3   ? B PRO 5   
27 1 Y 1 B ASN 4   ? B ASN 6   
28 1 Y 1 B PRO 5   ? B PRO 7   
29 1 Y 1 B LEU 6   ? B LEU 8   
30 1 Y 1 B GLN 7   ? B GLN 9   
31 1 Y 1 B LYS 8   ? B LYS 10  
32 1 Y 1 B PRO 9   ? B PRO 11  
33 1 Y 1 B ALA 10  ? B ALA 12  
34 1 Y 1 B ILE 11  ? B ILE 13  
35 1 Y 1 B ASP 12  ? B ASP 14  
36 1 Y 1 B ALA 13  ? B ALA 15  
37 1 Y 1 B HIS 79  ? B HIS 81  
38 1 Y 1 B SER 80  ? B SER 82  
39 1 Y 1 B GLY 81  ? B GLY 83  
40 1 Y 1 B SER 82  ? B SER 84  
41 1 Y 1 B GLY 135 ? B GLY 137 
42 1 Y 1 B GLY 136 ? B GLY 138 
43 1 Y 1 B SER 137 ? B SER 139 
44 1 Y 1 B ASN 493 ? B ASN 495 
45 1 Y 1 B GLY 494 ? B GLY 496 
46 1 Y 1 B GLY 913 ? B GLY 915 
47 1 Y 1 B LEU 914 ? B LEU 916 
48 1 Y 1 B ALA 915 ? B ALA 917 
49 1 Y 1 B SER 916 ? B SER 918 
# 
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 
1PE   OH2    O  N N 1   
1PE   C12    C  N N 2   
1PE   C22    C  N N 3   
1PE   OH3    O  N N 4   
1PE   C13    C  N N 5   
1PE   C23    C  N N 6   
1PE   OH4    O  N N 7   
1PE   C14    C  N N 8   
1PE   C24    C  N N 9   
1PE   OH5    O  N N 10  
1PE   C15    C  N N 11  
1PE   C25    C  N N 12  
1PE   OH6    O  N N 13  
1PE   C16    C  N N 14  
1PE   C26    C  N N 15  
1PE   OH7    O  N N 16  
1PE   HO2    H  N N 17  
1PE   H121   H  N N 18  
1PE   H122   H  N N 19  
1PE   H221   H  N N 20  
1PE   H222   H  N N 21  
1PE   H131   H  N N 22  
1PE   H132   H  N N 23  
1PE   H231   H  N N 24  
1PE   H232   H  N N 25  
1PE   H141   H  N N 26  
1PE   H142   H  N N 27  
1PE   H241   H  N N 28  
1PE   H242   H  N N 29  
1PE   H151   H  N N 30  
1PE   H152   H  N N 31  
1PE   H251   H  N N 32  
1PE   H252   H  N N 33  
1PE   H161   H  N N 34  
1PE   H162   H  N N 35  
1PE   H261   H  N N 36  
1PE   H262   H  N N 37  
1PE   HO7    H  N N 38  
A1BDV C02    C  N N 39  
A1BDV C03    C  Y N 40  
A1BDV C04    C  Y N 41  
A1BDV C05    C  Y N 42  
A1BDV C06    C  Y N 43  
A1BDV C08    C  N N 44  
A1BDV C10    C  Y N 45  
A1BDV C11    C  Y N 46  
A1BDV O01    O  N N 47  
A1BDV O07    O  N N 48  
A1BDV O09    O  N N 49  
A1BDV H1     H  N N 50  
A1BDV H2     H  N N 51  
A1BDV H3     H  N N 52  
A1BDV H4     H  N N 53  
A1BDV H5     H  N N 54  
A1BDV H6     H  N N 55  
A1BDV H7     H  N N 56  
A1BDV H8     H  N N 57  
ALA   N      N  N N 58  
ALA   CA     C  N S 59  
ALA   C      C  N N 60  
ALA   O      O  N N 61  
ALA   CB     C  N N 62  
ALA   OXT    O  N N 63  
ALA   H      H  N N 64  
ALA   H2     H  N N 65  
ALA   HA     H  N N 66  
ALA   HB1    H  N N 67  
ALA   HB2    H  N N 68  
ALA   HB3    H  N N 69  
ALA   HXT    H  N N 70  
ARG   N      N  N N 71  
ARG   CA     C  N S 72  
ARG   C      C  N N 73  
ARG   O      O  N N 74  
ARG   CB     C  N N 75  
ARG   CG     C  N N 76  
ARG   CD     C  N N 77  
ARG   NE     N  N N 78  
ARG   CZ     C  N N 79  
ARG   NH1    N  N N 80  
ARG   NH2    N  N N 81  
ARG   OXT    O  N N 82  
ARG   H      H  N N 83  
ARG   H2     H  N N 84  
ARG   HA     H  N N 85  
ARG   HB2    H  N N 86  
ARG   HB3    H  N N 87  
ARG   HG2    H  N N 88  
ARG   HG3    H  N N 89  
ARG   HD2    H  N N 90  
ARG   HD3    H  N N 91  
ARG   HE     H  N N 92  
ARG   HH11   H  N N 93  
ARG   HH12   H  N N 94  
ARG   HH21   H  N N 95  
ARG   HH22   H  N N 96  
ARG   HXT    H  N N 97  
ASN   N      N  N N 98  
ASN   CA     C  N S 99  
ASN   C      C  N N 100 
ASN   O      O  N N 101 
ASN   CB     C  N N 102 
ASN   CG     C  N N 103 
ASN   OD1    O  N N 104 
ASN   ND2    N  N N 105 
ASN   OXT    O  N N 106 
ASN   H      H  N N 107 
ASN   H2     H  N N 108 
ASN   HA     H  N N 109 
ASN   HB2    H  N N 110 
ASN   HB3    H  N N 111 
ASN   HD21   H  N N 112 
ASN   HD22   H  N N 113 
ASN   HXT    H  N N 114 
ASP   N      N  N N 115 
ASP   CA     C  N S 116 
ASP   C      C  N N 117 
ASP   O      O  N N 118 
ASP   CB     C  N N 119 
ASP   CG     C  N N 120 
ASP   OD1    O  N N 121 
ASP   OD2    O  N N 122 
ASP   OXT    O  N N 123 
ASP   H      H  N N 124 
ASP   H2     H  N N 125 
ASP   HA     H  N N 126 
ASP   HB2    H  N N 127 
ASP   HB3    H  N N 128 
ASP   HD2    H  N N 129 
ASP   HXT    H  N N 130 
CYS   N      N  N N 131 
CYS   CA     C  N R 132 
CYS   C      C  N N 133 
CYS   O      O  N N 134 
CYS   CB     C  N N 135 
CYS   SG     S  N N 136 
CYS   OXT    O  N N 137 
CYS   H      H  N N 138 
CYS   H2     H  N N 139 
CYS   HA     H  N N 140 
CYS   HB2    H  N N 141 
CYS   HB3    H  N N 142 
CYS   HG     H  N N 143 
CYS   HXT    H  N N 144 
FAD   PA     P  N R 145 
FAD   O1A    O  N N 146 
FAD   O2A    O  N N 147 
FAD   O5B    O  N N 148 
FAD   C5B    C  N N 149 
FAD   C4B    C  N R 150 
FAD   O4B    O  N N 151 
FAD   C3B    C  N S 152 
FAD   O3B    O  N N 153 
FAD   C2B    C  N R 154 
FAD   O2B    O  N N 155 
FAD   C1B    C  N R 156 
FAD   N9A    N  Y N 157 
FAD   C8A    C  Y N 158 
FAD   N7A    N  Y N 159 
FAD   C5A    C  Y N 160 
FAD   C6A    C  Y N 161 
FAD   N6A    N  N N 162 
FAD   N1A    N  Y N 163 
FAD   C2A    C  Y N 164 
FAD   N3A    N  Y N 165 
FAD   C4A    C  Y N 166 
FAD   N1     N  N N 167 
FAD   C2     C  N N 168 
FAD   O2     O  N N 169 
FAD   N3     N  N N 170 
FAD   C4     C  N N 171 
FAD   O4     O  N N 172 
FAD   C4X    C  N N 173 
FAD   N5     N  N N 174 
FAD   C5X    C  Y N 175 
FAD   C6     C  Y N 176 
FAD   C7     C  Y N 177 
FAD   C7M    C  N N 178 
FAD   C8     C  Y N 179 
FAD   C8M    C  N N 180 
FAD   C9     C  Y N 181 
FAD   C9A    C  Y N 182 
FAD   N10    N  N N 183 
FAD   C10    C  N N 184 
FAD   "C1'"  C  N N 185 
FAD   "C2'"  C  N S 186 
FAD   "O2'"  O  N N 187 
FAD   "C3'"  C  N S 188 
FAD   "O3'"  O  N N 189 
FAD   "C4'"  C  N R 190 
FAD   "O4'"  O  N N 191 
FAD   "C5'"  C  N N 192 
FAD   "O5'"  O  N N 193 
FAD   P      P  N R 194 
FAD   O1P    O  N N 195 
FAD   O2P    O  N N 196 
FAD   O3P    O  N N 197 
FAD   HOA2   H  N N 198 
FAD   H51A   H  N N 199 
FAD   H52A   H  N N 200 
FAD   H4B    H  N N 201 
FAD   H3B    H  N N 202 
FAD   HO3A   H  N N 203 
FAD   H2B    H  N N 204 
FAD   HO2A   H  N N 205 
FAD   H1B    H  N N 206 
FAD   H8A    H  N N 207 
FAD   H61A   H  N N 208 
FAD   H62A   H  N N 209 
FAD   H2A    H  N N 210 
FAD   HN3    H  N N 211 
FAD   H6     H  N N 212 
FAD   HM71   H  N N 213 
FAD   HM72   H  N N 214 
FAD   HM73   H  N N 215 
FAD   HM81   H  N N 216 
FAD   HM82   H  N N 217 
FAD   HM83   H  N N 218 
FAD   H9     H  N N 219 
FAD   "H1'1" H  N N 220 
FAD   "H1'2" H  N N 221 
FAD   "H2'"  H  N N 222 
FAD   "HO2'" H  N N 223 
FAD   "H3'"  H  N N 224 
FAD   "HO3'" H  N N 225 
FAD   "H4'"  H  N N 226 
FAD   "HO4'" H  N N 227 
FAD   "H5'1" H  N N 228 
FAD   "H5'2" H  N N 229 
FAD   HOP2   H  N N 230 
FMT   C      C  N N 231 
FMT   O1     O  N N 232 
FMT   O2     O  N N 233 
FMT   H      H  N N 234 
FMT   HO2    H  N N 235 
GLN   N      N  N N 236 
GLN   CA     C  N S 237 
GLN   C      C  N N 238 
GLN   O      O  N N 239 
GLN   CB     C  N N 240 
GLN   CG     C  N N 241 
GLN   CD     C  N N 242 
GLN   OE1    O  N N 243 
GLN   NE2    N  N N 244 
GLN   OXT    O  N N 245 
GLN   H      H  N N 246 
GLN   H2     H  N N 247 
GLN   HA     H  N N 248 
GLN   HB2    H  N N 249 
GLN   HB3    H  N N 250 
GLN   HG2    H  N N 251 
GLN   HG3    H  N N 252 
GLN   HE21   H  N N 253 
GLN   HE22   H  N N 254 
GLN   HXT    H  N N 255 
GLU   N      N  N N 256 
GLU   CA     C  N S 257 
GLU   C      C  N N 258 
GLU   O      O  N N 259 
GLU   CB     C  N N 260 
GLU   CG     C  N N 261 
GLU   CD     C  N N 262 
GLU   OE1    O  N N 263 
GLU   OE2    O  N N 264 
GLU   OXT    O  N N 265 
GLU   H      H  N N 266 
GLU   H2     H  N N 267 
GLU   HA     H  N N 268 
GLU   HB2    H  N N 269 
GLU   HB3    H  N N 270 
GLU   HG2    H  N N 271 
GLU   HG3    H  N N 272 
GLU   HE2    H  N N 273 
GLU   HXT    H  N N 274 
GLY   N      N  N N 275 
GLY   CA     C  N N 276 
GLY   C      C  N N 277 
GLY   O      O  N N 278 
GLY   OXT    O  N N 279 
GLY   H      H  N N 280 
GLY   H2     H  N N 281 
GLY   HA2    H  N N 282 
GLY   HA3    H  N N 283 
GLY   HXT    H  N N 284 
HIS   N      N  N N 285 
HIS   CA     C  N S 286 
HIS   C      C  N N 287 
HIS   O      O  N N 288 
HIS   CB     C  N N 289 
HIS   CG     C  Y N 290 
HIS   ND1    N  Y N 291 
HIS   CD2    C  Y N 292 
HIS   CE1    C  Y N 293 
HIS   NE2    N  Y N 294 
HIS   OXT    O  N N 295 
HIS   H      H  N N 296 
HIS   H2     H  N N 297 
HIS   HA     H  N N 298 
HIS   HB2    H  N N 299 
HIS   HB3    H  N N 300 
HIS   HD1    H  N N 301 
HIS   HD2    H  N N 302 
HIS   HE1    H  N N 303 
HIS   HE2    H  N N 304 
HIS   HXT    H  N N 305 
HOH   O      O  N N 306 
HOH   H1     H  N N 307 
HOH   H2     H  N N 308 
ILE   N      N  N N 309 
ILE   CA     C  N S 310 
ILE   C      C  N N 311 
ILE   O      O  N N 312 
ILE   CB     C  N S 313 
ILE   CG1    C  N N 314 
ILE   CG2    C  N N 315 
ILE   CD1    C  N N 316 
ILE   OXT    O  N N 317 
ILE   H      H  N N 318 
ILE   H2     H  N N 319 
ILE   HA     H  N N 320 
ILE   HB     H  N N 321 
ILE   HG12   H  N N 322 
ILE   HG13   H  N N 323 
ILE   HG21   H  N N 324 
ILE   HG22   H  N N 325 
ILE   HG23   H  N N 326 
ILE   HD11   H  N N 327 
ILE   HD12   H  N N 328 
ILE   HD13   H  N N 329 
ILE   HXT    H  N N 330 
LEU   N      N  N N 331 
LEU   CA     C  N S 332 
LEU   C      C  N N 333 
LEU   O      O  N N 334 
LEU   CB     C  N N 335 
LEU   CG     C  N N 336 
LEU   CD1    C  N N 337 
LEU   CD2    C  N N 338 
LEU   OXT    O  N N 339 
LEU   H      H  N N 340 
LEU   H2     H  N N 341 
LEU   HA     H  N N 342 
LEU   HB2    H  N N 343 
LEU   HB3    H  N N 344 
LEU   HG     H  N N 345 
LEU   HD11   H  N N 346 
LEU   HD12   H  N N 347 
LEU   HD13   H  N N 348 
LEU   HD21   H  N N 349 
LEU   HD22   H  N N 350 
LEU   HD23   H  N N 351 
LEU   HXT    H  N N 352 
LYS   N      N  N N 353 
LYS   CA     C  N S 354 
LYS   C      C  N N 355 
LYS   O      O  N N 356 
LYS   CB     C  N N 357 
LYS   CG     C  N N 358 
LYS   CD     C  N N 359 
LYS   CE     C  N N 360 
LYS   NZ     N  N N 361 
LYS   OXT    O  N N 362 
LYS   H      H  N N 363 
LYS   H2     H  N N 364 
LYS   HA     H  N N 365 
LYS   HB2    H  N N 366 
LYS   HB3    H  N N 367 
LYS   HG2    H  N N 368 
LYS   HG3    H  N N 369 
LYS   HD2    H  N N 370 
LYS   HD3    H  N N 371 
LYS   HE2    H  N N 372 
LYS   HE3    H  N N 373 
LYS   HZ1    H  N N 374 
LYS   HZ2    H  N N 375 
LYS   HZ3    H  N N 376 
LYS   HXT    H  N N 377 
MET   N      N  N N 378 
MET   CA     C  N S 379 
MET   C      C  N N 380 
MET   O      O  N N 381 
MET   CB     C  N N 382 
MET   CG     C  N N 383 
MET   SD     S  N N 384 
MET   CE     C  N N 385 
MET   OXT    O  N N 386 
MET   H      H  N N 387 
MET   H2     H  N N 388 
MET   HA     H  N N 389 
MET   HB2    H  N N 390 
MET   HB3    H  N N 391 
MET   HG2    H  N N 392 
MET   HG3    H  N N 393 
MET   HE1    H  N N 394 
MET   HE2    H  N N 395 
MET   HE3    H  N N 396 
MET   HXT    H  N N 397 
MG    MG     MG N N 398 
NAD   PA     P  N S 399 
NAD   O1A    O  N N 400 
NAD   O2A    O  N N 401 
NAD   O5B    O  N N 402 
NAD   C5B    C  N N 403 
NAD   C4B    C  N R 404 
NAD   O4B    O  N N 405 
NAD   C3B    C  N S 406 
NAD   O3B    O  N N 407 
NAD   C2B    C  N R 408 
NAD   O2B    O  N N 409 
NAD   C1B    C  N R 410 
NAD   N9A    N  Y N 411 
NAD   C8A    C  Y N 412 
NAD   N7A    N  Y N 413 
NAD   C5A    C  Y N 414 
NAD   C6A    C  Y N 415 
NAD   N6A    N  N N 416 
NAD   N1A    N  Y N 417 
NAD   C2A    C  Y N 418 
NAD   N3A    N  Y N 419 
NAD   C4A    C  Y N 420 
NAD   O3     O  N N 421 
NAD   PN     P  N N 422 
NAD   O1N    O  N N 423 
NAD   O2N    O  N N 424 
NAD   O5D    O  N N 425 
NAD   C5D    C  N N 426 
NAD   C4D    C  N R 427 
NAD   O4D    O  N N 428 
NAD   C3D    C  N S 429 
NAD   O3D    O  N N 430 
NAD   C2D    C  N R 431 
NAD   O2D    O  N N 432 
NAD   C1D    C  N R 433 
NAD   N1N    N  Y N 434 
NAD   C2N    C  Y N 435 
NAD   C3N    C  Y N 436 
NAD   C7N    C  N N 437 
NAD   O7N    O  N N 438 
NAD   N7N    N  N N 439 
NAD   C4N    C  Y N 440 
NAD   C5N    C  Y N 441 
NAD   C6N    C  Y N 442 
NAD   HOA2   H  N N 443 
NAD   H51A   H  N N 444 
NAD   H52A   H  N N 445 
NAD   H4B    H  N N 446 
NAD   H3B    H  N N 447 
NAD   HO3A   H  N N 448 
NAD   H2B    H  N N 449 
NAD   HO2A   H  N N 450 
NAD   H1B    H  N N 451 
NAD   H8A    H  N N 452 
NAD   H61A   H  N N 453 
NAD   H62A   H  N N 454 
NAD   H2A    H  N N 455 
NAD   H51N   H  N N 456 
NAD   H52N   H  N N 457 
NAD   H4D    H  N N 458 
NAD   H3D    H  N N 459 
NAD   HO3N   H  N N 460 
NAD   H2D    H  N N 461 
NAD   HO2N   H  N N 462 
NAD   H1D    H  N N 463 
NAD   H2N    H  N N 464 
NAD   H71N   H  N N 465 
NAD   H72N   H  N N 466 
NAD   H4N    H  N N 467 
NAD   H5N    H  N N 468 
NAD   H6N    H  N N 469 
PEG   C1     C  N N 470 
PEG   O1     O  N N 471 
PEG   C2     C  N N 472 
PEG   O2     O  N N 473 
PEG   C3     C  N N 474 
PEG   C4     C  N N 475 
PEG   O4     O  N N 476 
PEG   H11    H  N N 477 
PEG   H12    H  N N 478 
PEG   HO1    H  N N 479 
PEG   H21    H  N N 480 
PEG   H22    H  N N 481 
PEG   H31    H  N N 482 
PEG   H32    H  N N 483 
PEG   H41    H  N N 484 
PEG   H42    H  N N 485 
PEG   HO4    H  N N 486 
PGE   C1     C  N N 487 
PGE   O1     O  N N 488 
PGE   C2     C  N N 489 
PGE   O2     O  N N 490 
PGE   C3     C  N N 491 
PGE   C4     C  N N 492 
PGE   O4     O  N N 493 
PGE   C6     C  N N 494 
PGE   C5     C  N N 495 
PGE   O3     O  N N 496 
PGE   H1     H  N N 497 
PGE   H12    H  N N 498 
PGE   HO1    H  N N 499 
PGE   H2     H  N N 500 
PGE   H22    H  N N 501 
PGE   H3     H  N N 502 
PGE   H32    H  N N 503 
PGE   H4     H  N N 504 
PGE   H42    H  N N 505 
PGE   HO4    H  N N 506 
PGE   H6     H  N N 507 
PGE   H62    H  N N 508 
PGE   H5     H  N N 509 
PGE   H52    H  N N 510 
PHE   N      N  N N 511 
PHE   CA     C  N S 512 
PHE   C      C  N N 513 
PHE   O      O  N N 514 
PHE   CB     C  N N 515 
PHE   CG     C  Y N 516 
PHE   CD1    C  Y N 517 
PHE   CD2    C  Y N 518 
PHE   CE1    C  Y N 519 
PHE   CE2    C  Y N 520 
PHE   CZ     C  Y N 521 
PHE   OXT    O  N N 522 
PHE   H      H  N N 523 
PHE   H2     H  N N 524 
PHE   HA     H  N N 525 
PHE   HB2    H  N N 526 
PHE   HB3    H  N N 527 
PHE   HD1    H  N N 528 
PHE   HD2    H  N N 529 
PHE   HE1    H  N N 530 
PHE   HE2    H  N N 531 
PHE   HZ     H  N N 532 
PHE   HXT    H  N N 533 
PRO   N      N  N N 534 
PRO   CA     C  N S 535 
PRO   C      C  N N 536 
PRO   O      O  N N 537 
PRO   CB     C  N N 538 
PRO   CG     C  N N 539 
PRO   CD     C  N N 540 
PRO   OXT    O  N N 541 
PRO   H      H  N N 542 
PRO   HA     H  N N 543 
PRO   HB2    H  N N 544 
PRO   HB3    H  N N 545 
PRO   HG2    H  N N 546 
PRO   HG3    H  N N 547 
PRO   HD2    H  N N 548 
PRO   HD3    H  N N 549 
PRO   HXT    H  N N 550 
SER   N      N  N N 551 
SER   CA     C  N S 552 
SER   C      C  N N 553 
SER   O      O  N N 554 
SER   CB     C  N N 555 
SER   OG     O  N N 556 
SER   OXT    O  N N 557 
SER   H      H  N N 558 
SER   H2     H  N N 559 
SER   HA     H  N N 560 
SER   HB2    H  N N 561 
SER   HB3    H  N N 562 
SER   HG     H  N N 563 
SER   HXT    H  N N 564 
SO4   S      S  N N 565 
SO4   O1     O  N N 566 
SO4   O2     O  N N 567 
SO4   O3     O  N N 568 
SO4   O4     O  N N 569 
THR   N      N  N N 570 
THR   CA     C  N S 571 
THR   C      C  N N 572 
THR   O      O  N N 573 
THR   CB     C  N R 574 
THR   OG1    O  N N 575 
THR   CG2    C  N N 576 
THR   OXT    O  N N 577 
THR   H      H  N N 578 
THR   H2     H  N N 579 
THR   HA     H  N N 580 
THR   HB     H  N N 581 
THR   HG1    H  N N 582 
THR   HG21   H  N N 583 
THR   HG22   H  N N 584 
THR   HG23   H  N N 585 
THR   HXT    H  N N 586 
TRP   N      N  N N 587 
TRP   CA     C  N S 588 
TRP   C      C  N N 589 
TRP   O      O  N N 590 
TRP   CB     C  N N 591 
TRP   CG     C  Y N 592 
TRP   CD1    C  Y N 593 
TRP   CD2    C  Y N 594 
TRP   NE1    N  Y N 595 
TRP   CE2    C  Y N 596 
TRP   CE3    C  Y N 597 
TRP   CZ2    C  Y N 598 
TRP   CZ3    C  Y N 599 
TRP   CH2    C  Y N 600 
TRP   OXT    O  N N 601 
TRP   H      H  N N 602 
TRP   H2     H  N N 603 
TRP   HA     H  N N 604 
TRP   HB2    H  N N 605 
TRP   HB3    H  N N 606 
TRP   HD1    H  N N 607 
TRP   HE1    H  N N 608 
TRP   HE3    H  N N 609 
TRP   HZ2    H  N N 610 
TRP   HZ3    H  N N 611 
TRP   HH2    H  N N 612 
TRP   HXT    H  N N 613 
TYR   N      N  N N 614 
TYR   CA     C  N S 615 
TYR   C      C  N N 616 
TYR   O      O  N N 617 
TYR   CB     C  N N 618 
TYR   CG     C  Y N 619 
TYR   CD1    C  Y N 620 
TYR   CD2    C  Y N 621 
TYR   CE1    C  Y N 622 
TYR   CE2    C  Y N 623 
TYR   CZ     C  Y N 624 
TYR   OH     O  N N 625 
TYR   OXT    O  N N 626 
TYR   H      H  N N 627 
TYR   H2     H  N N 628 
TYR   HA     H  N N 629 
TYR   HB2    H  N N 630 
TYR   HB3    H  N N 631 
TYR   HD1    H  N N 632 
TYR   HD2    H  N N 633 
TYR   HE1    H  N N 634 
TYR   HE2    H  N N 635 
TYR   HH     H  N N 636 
TYR   HXT    H  N N 637 
VAL   N      N  N N 638 
VAL   CA     C  N S 639 
VAL   C      C  N N 640 
VAL   O      O  N N 641 
VAL   CB     C  N N 642 
VAL   CG1    C  N N 643 
VAL   CG2    C  N N 644 
VAL   OXT    O  N N 645 
VAL   H      H  N N 646 
VAL   H2     H  N N 647 
VAL   HA     H  N N 648 
VAL   HB     H  N N 649 
VAL   HG11   H  N N 650 
VAL   HG12   H  N N 651 
VAL   HG13   H  N N 652 
VAL   HG21   H  N N 653 
VAL   HG22   H  N N 654 
VAL   HG23   H  N N 655 
VAL   HXT    H  N N 656 
# 
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 
1PE   OH2   C12    sing N N 1   
1PE   OH2   HO2    sing N N 2   
1PE   C12   C22    sing N N 3   
1PE   C12   H121   sing N N 4   
1PE   C12   H122   sing N N 5   
1PE   C22   OH3    sing N N 6   
1PE   C22   H221   sing N N 7   
1PE   C22   H222   sing N N 8   
1PE   OH3   C23    sing N N 9   
1PE   C13   C23    sing N N 10  
1PE   C13   OH4    sing N N 11  
1PE   C13   H131   sing N N 12  
1PE   C13   H132   sing N N 13  
1PE   C23   H231   sing N N 14  
1PE   C23   H232   sing N N 15  
1PE   OH4   C24    sing N N 16  
1PE   C14   C24    sing N N 17  
1PE   C14   OH5    sing N N 18  
1PE   C14   H141   sing N N 19  
1PE   C14   H142   sing N N 20  
1PE   C24   H241   sing N N 21  
1PE   C24   H242   sing N N 22  
1PE   OH5   C25    sing N N 23  
1PE   C15   C25    sing N N 24  
1PE   C15   OH6    sing N N 25  
1PE   C15   H151   sing N N 26  
1PE   C15   H152   sing N N 27  
1PE   C25   H251   sing N N 28  
1PE   C25   H252   sing N N 29  
1PE   OH6   C26    sing N N 30  
1PE   C16   C26    sing N N 31  
1PE   C16   OH7    sing N N 32  
1PE   C16   H161   sing N N 33  
1PE   C16   H162   sing N N 34  
1PE   C26   H261   sing N N 35  
1PE   C26   H262   sing N N 36  
1PE   OH7   HO7    sing N N 37  
A1BDV O01   C02    sing N N 38  
A1BDV C02   C03    sing N N 39  
A1BDV C04   C03    doub Y N 40  
A1BDV C04   C05    sing Y N 41  
A1BDV C03   C11    sing Y N 42  
A1BDV C05   C06    doub Y N 43  
A1BDV C11   C10    doub Y N 44  
A1BDV C06   C10    sing Y N 45  
A1BDV C06   O07    sing N N 46  
A1BDV C10   O09    sing N N 47  
A1BDV O07   C08    sing N N 48  
A1BDV O09   C08    sing N N 49  
A1BDV C02   H1     sing N N 50  
A1BDV C02   H2     sing N N 51  
A1BDV C04   H3     sing N N 52  
A1BDV C05   H4     sing N N 53  
A1BDV C08   H5     sing N N 54  
A1BDV C08   H6     sing N N 55  
A1BDV C11   H7     sing N N 56  
A1BDV O01   H8     sing N N 57  
ALA   N     CA     sing N N 58  
ALA   N     H      sing N N 59  
ALA   N     H2     sing N N 60  
ALA   CA    C      sing N N 61  
ALA   CA    CB     sing N N 62  
ALA   CA    HA     sing N N 63  
ALA   C     O      doub N N 64  
ALA   C     OXT    sing N N 65  
ALA   CB    HB1    sing N N 66  
ALA   CB    HB2    sing N N 67  
ALA   CB    HB3    sing N N 68  
ALA   OXT   HXT    sing N N 69  
ARG   N     CA     sing N N 70  
ARG   N     H      sing N N 71  
ARG   N     H2     sing N N 72  
ARG   CA    C      sing N N 73  
ARG   CA    CB     sing N N 74  
ARG   CA    HA     sing N N 75  
ARG   C     O      doub N N 76  
ARG   C     OXT    sing N N 77  
ARG   CB    CG     sing N N 78  
ARG   CB    HB2    sing N N 79  
ARG   CB    HB3    sing N N 80  
ARG   CG    CD     sing N N 81  
ARG   CG    HG2    sing N N 82  
ARG   CG    HG3    sing N N 83  
ARG   CD    NE     sing N N 84  
ARG   CD    HD2    sing N N 85  
ARG   CD    HD3    sing N N 86  
ARG   NE    CZ     sing N N 87  
ARG   NE    HE     sing N N 88  
ARG   CZ    NH1    sing N N 89  
ARG   CZ    NH2    doub N N 90  
ARG   NH1   HH11   sing N N 91  
ARG   NH1   HH12   sing N N 92  
ARG   NH2   HH21   sing N N 93  
ARG   NH2   HH22   sing N N 94  
ARG   OXT   HXT    sing N N 95  
ASN   N     CA     sing N N 96  
ASN   N     H      sing N N 97  
ASN   N     H2     sing N N 98  
ASN   CA    C      sing N N 99  
ASN   CA    CB     sing N N 100 
ASN   CA    HA     sing N N 101 
ASN   C     O      doub N N 102 
ASN   C     OXT    sing N N 103 
ASN   CB    CG     sing N N 104 
ASN   CB    HB2    sing N N 105 
ASN   CB    HB3    sing N N 106 
ASN   CG    OD1    doub N N 107 
ASN   CG    ND2    sing N N 108 
ASN   ND2   HD21   sing N N 109 
ASN   ND2   HD22   sing N N 110 
ASN   OXT   HXT    sing N N 111 
ASP   N     CA     sing N N 112 
ASP   N     H      sing N N 113 
ASP   N     H2     sing N N 114 
ASP   CA    C      sing N N 115 
ASP   CA    CB     sing N N 116 
ASP   CA    HA     sing N N 117 
ASP   C     O      doub N N 118 
ASP   C     OXT    sing N N 119 
ASP   CB    CG     sing N N 120 
ASP   CB    HB2    sing N N 121 
ASP   CB    HB3    sing N N 122 
ASP   CG    OD1    doub N N 123 
ASP   CG    OD2    sing N N 124 
ASP   OD2   HD2    sing N N 125 
ASP   OXT   HXT    sing N N 126 
CYS   N     CA     sing N N 127 
CYS   N     H      sing N N 128 
CYS   N     H2     sing N N 129 
CYS   CA    C      sing N N 130 
CYS   CA    CB     sing N N 131 
CYS   CA    HA     sing N N 132 
CYS   C     O      doub N N 133 
CYS   C     OXT    sing N N 134 
CYS   CB    SG     sing N N 135 
CYS   CB    HB2    sing N N 136 
CYS   CB    HB3    sing N N 137 
CYS   SG    HG     sing N N 138 
CYS   OXT   HXT    sing N N 139 
FAD   PA    O1A    doub N N 140 
FAD   PA    O2A    sing N N 141 
FAD   PA    O5B    sing N N 142 
FAD   PA    O3P    sing N N 143 
FAD   O2A   HOA2   sing N N 144 
FAD   O5B   C5B    sing N N 145 
FAD   C5B   C4B    sing N N 146 
FAD   C5B   H51A   sing N N 147 
FAD   C5B   H52A   sing N N 148 
FAD   C4B   O4B    sing N N 149 
FAD   C4B   C3B    sing N N 150 
FAD   C4B   H4B    sing N N 151 
FAD   O4B   C1B    sing N N 152 
FAD   C3B   O3B    sing N N 153 
FAD   C3B   C2B    sing N N 154 
FAD   C3B   H3B    sing N N 155 
FAD   O3B   HO3A   sing N N 156 
FAD   C2B   O2B    sing N N 157 
FAD   C2B   C1B    sing N N 158 
FAD   C2B   H2B    sing N N 159 
FAD   O2B   HO2A   sing N N 160 
FAD   C1B   N9A    sing N N 161 
FAD   C1B   H1B    sing N N 162 
FAD   N9A   C8A    sing Y N 163 
FAD   N9A   C4A    sing Y N 164 
FAD   C8A   N7A    doub Y N 165 
FAD   C8A   H8A    sing N N 166 
FAD   N7A   C5A    sing Y N 167 
FAD   C5A   C6A    sing Y N 168 
FAD   C5A   C4A    doub Y N 169 
FAD   C6A   N6A    sing N N 170 
FAD   C6A   N1A    doub Y N 171 
FAD   N6A   H61A   sing N N 172 
FAD   N6A   H62A   sing N N 173 
FAD   N1A   C2A    sing Y N 174 
FAD   C2A   N3A    doub Y N 175 
FAD   C2A   H2A    sing N N 176 
FAD   N3A   C4A    sing Y N 177 
FAD   N1    C2     sing N N 178 
FAD   N1    C10    doub N N 179 
FAD   C2    O2     doub N N 180 
FAD   C2    N3     sing N N 181 
FAD   N3    C4     sing N N 182 
FAD   N3    HN3    sing N N 183 
FAD   C4    O4     doub N N 184 
FAD   C4    C4X    sing N N 185 
FAD   C4X   N5     doub N N 186 
FAD   C4X   C10    sing N N 187 
FAD   N5    C5X    sing N N 188 
FAD   C5X   C6     doub Y N 189 
FAD   C5X   C9A    sing Y N 190 
FAD   C6    C7     sing Y N 191 
FAD   C6    H6     sing N N 192 
FAD   C7    C7M    sing N N 193 
FAD   C7    C8     doub Y N 194 
FAD   C7M   HM71   sing N N 195 
FAD   C7M   HM72   sing N N 196 
FAD   C7M   HM73   sing N N 197 
FAD   C8    C8M    sing N N 198 
FAD   C8    C9     sing Y N 199 
FAD   C8M   HM81   sing N N 200 
FAD   C8M   HM82   sing N N 201 
FAD   C8M   HM83   sing N N 202 
FAD   C9    C9A    doub Y N 203 
FAD   C9    H9     sing N N 204 
FAD   C9A   N10    sing N N 205 
FAD   N10   C10    sing N N 206 
FAD   N10   "C1'"  sing N N 207 
FAD   "C1'" "C2'"  sing N N 208 
FAD   "C1'" "H1'1" sing N N 209 
FAD   "C1'" "H1'2" sing N N 210 
FAD   "C2'" "O2'"  sing N N 211 
FAD   "C2'" "C3'"  sing N N 212 
FAD   "C2'" "H2'"  sing N N 213 
FAD   "O2'" "HO2'" sing N N 214 
FAD   "C3'" "O3'"  sing N N 215 
FAD   "C3'" "C4'"  sing N N 216 
FAD   "C3'" "H3'"  sing N N 217 
FAD   "O3'" "HO3'" sing N N 218 
FAD   "C4'" "O4'"  sing N N 219 
FAD   "C4'" "C5'"  sing N N 220 
FAD   "C4'" "H4'"  sing N N 221 
FAD   "O4'" "HO4'" sing N N 222 
FAD   "C5'" "O5'"  sing N N 223 
FAD   "C5'" "H5'1" sing N N 224 
FAD   "C5'" "H5'2" sing N N 225 
FAD   "O5'" P      sing N N 226 
FAD   P     O1P    doub N N 227 
FAD   P     O2P    sing N N 228 
FAD   P     O3P    sing N N 229 
FAD   O2P   HOP2   sing N N 230 
FMT   C     O1     doub N N 231 
FMT   C     O2     sing N N 232 
FMT   C     H      sing N N 233 
FMT   O2    HO2    sing N N 234 
GLN   N     CA     sing N N 235 
GLN   N     H      sing N N 236 
GLN   N     H2     sing N N 237 
GLN   CA    C      sing N N 238 
GLN   CA    CB     sing N N 239 
GLN   CA    HA     sing N N 240 
GLN   C     O      doub N N 241 
GLN   C     OXT    sing N N 242 
GLN   CB    CG     sing N N 243 
GLN   CB    HB2    sing N N 244 
GLN   CB    HB3    sing N N 245 
GLN   CG    CD     sing N N 246 
GLN   CG    HG2    sing N N 247 
GLN   CG    HG3    sing N N 248 
GLN   CD    OE1    doub N N 249 
GLN   CD    NE2    sing N N 250 
GLN   NE2   HE21   sing N N 251 
GLN   NE2   HE22   sing N N 252 
GLN   OXT   HXT    sing N N 253 
GLU   N     CA     sing N N 254 
GLU   N     H      sing N N 255 
GLU   N     H2     sing N N 256 
GLU   CA    C      sing N N 257 
GLU   CA    CB     sing N N 258 
GLU   CA    HA     sing N N 259 
GLU   C     O      doub N N 260 
GLU   C     OXT    sing N N 261 
GLU   CB    CG     sing N N 262 
GLU   CB    HB2    sing N N 263 
GLU   CB    HB3    sing N N 264 
GLU   CG    CD     sing N N 265 
GLU   CG    HG2    sing N N 266 
GLU   CG    HG3    sing N N 267 
GLU   CD    OE1    doub N N 268 
GLU   CD    OE2    sing N N 269 
GLU   OE2   HE2    sing N N 270 
GLU   OXT   HXT    sing N N 271 
GLY   N     CA     sing N N 272 
GLY   N     H      sing N N 273 
GLY   N     H2     sing N N 274 
GLY   CA    C      sing N N 275 
GLY   CA    HA2    sing N N 276 
GLY   CA    HA3    sing N N 277 
GLY   C     O      doub N N 278 
GLY   C     OXT    sing N N 279 
GLY   OXT   HXT    sing N N 280 
HIS   N     CA     sing N N 281 
HIS   N     H      sing N N 282 
HIS   N     H2     sing N N 283 
HIS   CA    C      sing N N 284 
HIS   CA    CB     sing N N 285 
HIS   CA    HA     sing N N 286 
HIS   C     O      doub N N 287 
HIS   C     OXT    sing N N 288 
HIS   CB    CG     sing N N 289 
HIS   CB    HB2    sing N N 290 
HIS   CB    HB3    sing N N 291 
HIS   CG    ND1    sing Y N 292 
HIS   CG    CD2    doub Y N 293 
HIS   ND1   CE1    doub Y N 294 
HIS   ND1   HD1    sing N N 295 
HIS   CD2   NE2    sing Y N 296 
HIS   CD2   HD2    sing N N 297 
HIS   CE1   NE2    sing Y N 298 
HIS   CE1   HE1    sing N N 299 
HIS   NE2   HE2    sing N N 300 
HIS   OXT   HXT    sing N N 301 
HOH   O     H1     sing N N 302 
HOH   O     H2     sing N N 303 
ILE   N     CA     sing N N 304 
ILE   N     H      sing N N 305 
ILE   N     H2     sing N N 306 
ILE   CA    C      sing N N 307 
ILE   CA    CB     sing N N 308 
ILE   CA    HA     sing N N 309 
ILE   C     O      doub N N 310 
ILE   C     OXT    sing N N 311 
ILE   CB    CG1    sing N N 312 
ILE   CB    CG2    sing N N 313 
ILE   CB    HB     sing N N 314 
ILE   CG1   CD1    sing N N 315 
ILE   CG1   HG12   sing N N 316 
ILE   CG1   HG13   sing N N 317 
ILE   CG2   HG21   sing N N 318 
ILE   CG2   HG22   sing N N 319 
ILE   CG2   HG23   sing N N 320 
ILE   CD1   HD11   sing N N 321 
ILE   CD1   HD12   sing N N 322 
ILE   CD1   HD13   sing N N 323 
ILE   OXT   HXT    sing N N 324 
LEU   N     CA     sing N N 325 
LEU   N     H      sing N N 326 
LEU   N     H2     sing N N 327 
LEU   CA    C      sing N N 328 
LEU   CA    CB     sing N N 329 
LEU   CA    HA     sing N N 330 
LEU   C     O      doub N N 331 
LEU   C     OXT    sing N N 332 
LEU   CB    CG     sing N N 333 
LEU   CB    HB2    sing N N 334 
LEU   CB    HB3    sing N N 335 
LEU   CG    CD1    sing N N 336 
LEU   CG    CD2    sing N N 337 
LEU   CG    HG     sing N N 338 
LEU   CD1   HD11   sing N N 339 
LEU   CD1   HD12   sing N N 340 
LEU   CD1   HD13   sing N N 341 
LEU   CD2   HD21   sing N N 342 
LEU   CD2   HD22   sing N N 343 
LEU   CD2   HD23   sing N N 344 
LEU   OXT   HXT    sing N N 345 
LYS   N     CA     sing N N 346 
LYS   N     H      sing N N 347 
LYS   N     H2     sing N N 348 
LYS   CA    C      sing N N 349 
LYS   CA    CB     sing N N 350 
LYS   CA    HA     sing N N 351 
LYS   C     O      doub N N 352 
LYS   C     OXT    sing N N 353 
LYS   CB    CG     sing N N 354 
LYS   CB    HB2    sing N N 355 
LYS   CB    HB3    sing N N 356 
LYS   CG    CD     sing N N 357 
LYS   CG    HG2    sing N N 358 
LYS   CG    HG3    sing N N 359 
LYS   CD    CE     sing N N 360 
LYS   CD    HD2    sing N N 361 
LYS   CD    HD3    sing N N 362 
LYS   CE    NZ     sing N N 363 
LYS   CE    HE2    sing N N 364 
LYS   CE    HE3    sing N N 365 
LYS   NZ    HZ1    sing N N 366 
LYS   NZ    HZ2    sing N N 367 
LYS   NZ    HZ3    sing N N 368 
LYS   OXT   HXT    sing N N 369 
MET   N     CA     sing N N 370 
MET   N     H      sing N N 371 
MET   N     H2     sing N N 372 
MET   CA    C      sing N N 373 
MET   CA    CB     sing N N 374 
MET   CA    HA     sing N N 375 
MET   C     O      doub N N 376 
MET   C     OXT    sing N N 377 
MET   CB    CG     sing N N 378 
MET   CB    HB2    sing N N 379 
MET   CB    HB3    sing N N 380 
MET   CG    SD     sing N N 381 
MET   CG    HG2    sing N N 382 
MET   CG    HG3    sing N N 383 
MET   SD    CE     sing N N 384 
MET   CE    HE1    sing N N 385 
MET   CE    HE2    sing N N 386 
MET   CE    HE3    sing N N 387 
MET   OXT   HXT    sing N N 388 
NAD   PA    O1A    doub N N 389 
NAD   PA    O2A    sing N N 390 
NAD   PA    O5B    sing N N 391 
NAD   PA    O3     sing N N 392 
NAD   O2A   HOA2   sing N N 393 
NAD   O5B   C5B    sing N N 394 
NAD   C5B   C4B    sing N N 395 
NAD   C5B   H51A   sing N N 396 
NAD   C5B   H52A   sing N N 397 
NAD   C4B   O4B    sing N N 398 
NAD   C4B   C3B    sing N N 399 
NAD   C4B   H4B    sing N N 400 
NAD   O4B   C1B    sing N N 401 
NAD   C3B   O3B    sing N N 402 
NAD   C3B   C2B    sing N N 403 
NAD   C3B   H3B    sing N N 404 
NAD   O3B   HO3A   sing N N 405 
NAD   C2B   O2B    sing N N 406 
NAD   C2B   C1B    sing N N 407 
NAD   C2B   H2B    sing N N 408 
NAD   O2B   HO2A   sing N N 409 
NAD   C1B   N9A    sing N N 410 
NAD   C1B   H1B    sing N N 411 
NAD   N9A   C8A    sing Y N 412 
NAD   N9A   C4A    sing Y N 413 
NAD   C8A   N7A    doub Y N 414 
NAD   C8A   H8A    sing N N 415 
NAD   N7A   C5A    sing Y N 416 
NAD   C5A   C6A    sing Y N 417 
NAD   C5A   C4A    doub Y N 418 
NAD   C6A   N6A    sing N N 419 
NAD   C6A   N1A    doub Y N 420 
NAD   N6A   H61A   sing N N 421 
NAD   N6A   H62A   sing N N 422 
NAD   N1A   C2A    sing Y N 423 
NAD   C2A   N3A    doub Y N 424 
NAD   C2A   H2A    sing N N 425 
NAD   N3A   C4A    sing Y N 426 
NAD   O3    PN     sing N N 427 
NAD   PN    O1N    doub N N 428 
NAD   PN    O2N    sing N N 429 
NAD   PN    O5D    sing N N 430 
NAD   O5D   C5D    sing N N 431 
NAD   C5D   C4D    sing N N 432 
NAD   C5D   H51N   sing N N 433 
NAD   C5D   H52N   sing N N 434 
NAD   C4D   O4D    sing N N 435 
NAD   C4D   C3D    sing N N 436 
NAD   C4D   H4D    sing N N 437 
NAD   O4D   C1D    sing N N 438 
NAD   C3D   O3D    sing N N 439 
NAD   C3D   C2D    sing N N 440 
NAD   C3D   H3D    sing N N 441 
NAD   O3D   HO3N   sing N N 442 
NAD   C2D   O2D    sing N N 443 
NAD   C2D   C1D    sing N N 444 
NAD   C2D   H2D    sing N N 445 
NAD   O2D   HO2N   sing N N 446 
NAD   C1D   N1N    sing N N 447 
NAD   C1D   H1D    sing N N 448 
NAD   N1N   C2N    sing Y N 449 
NAD   N1N   C6N    doub Y N 450 
NAD   C2N   C3N    doub Y N 451 
NAD   C2N   H2N    sing N N 452 
NAD   C3N   C7N    sing N N 453 
NAD   C3N   C4N    sing Y N 454 
NAD   C7N   O7N    doub N N 455 
NAD   C7N   N7N    sing N N 456 
NAD   N7N   H71N   sing N N 457 
NAD   N7N   H72N   sing N N 458 
NAD   C4N   C5N    doub Y N 459 
NAD   C4N   H4N    sing N N 460 
NAD   C5N   C6N    sing Y N 461 
NAD   C5N   H5N    sing N N 462 
NAD   C6N   H6N    sing N N 463 
PEG   C1    O1     sing N N 464 
PEG   C1    C2     sing N N 465 
PEG   C1    H11    sing N N 466 
PEG   C1    H12    sing N N 467 
PEG   O1    HO1    sing N N 468 
PEG   C2    O2     sing N N 469 
PEG   C2    H21    sing N N 470 
PEG   C2    H22    sing N N 471 
PEG   O2    C3     sing N N 472 
PEG   C3    C4     sing N N 473 
PEG   C3    H31    sing N N 474 
PEG   C3    H32    sing N N 475 
PEG   C4    O4     sing N N 476 
PEG   C4    H41    sing N N 477 
PEG   C4    H42    sing N N 478 
PEG   O4    HO4    sing N N 479 
PGE   C1    O1     sing N N 480 
PGE   C1    C2     sing N N 481 
PGE   C1    H1     sing N N 482 
PGE   C1    H12    sing N N 483 
PGE   O1    HO1    sing N N 484 
PGE   C2    O2     sing N N 485 
PGE   C2    H2     sing N N 486 
PGE   C2    H22    sing N N 487 
PGE   O2    C3     sing N N 488 
PGE   C3    C4     sing N N 489 
PGE   C3    H3     sing N N 490 
PGE   C3    H32    sing N N 491 
PGE   C4    O3     sing N N 492 
PGE   C4    H4     sing N N 493 
PGE   C4    H42    sing N N 494 
PGE   O4    C6     sing N N 495 
PGE   O4    HO4    sing N N 496 
PGE   C6    C5     sing N N 497 
PGE   C6    H6     sing N N 498 
PGE   C6    H62    sing N N 499 
PGE   C5    O3     sing N N 500 
PGE   C5    H5     sing N N 501 
PGE   C5    H52    sing N N 502 
PHE   N     CA     sing N N 503 
PHE   N     H      sing N N 504 
PHE   N     H2     sing N N 505 
PHE   CA    C      sing N N 506 
PHE   CA    CB     sing N N 507 
PHE   CA    HA     sing N N 508 
PHE   C     O      doub N N 509 
PHE   C     OXT    sing N N 510 
PHE   CB    CG     sing N N 511 
PHE   CB    HB2    sing N N 512 
PHE   CB    HB3    sing N N 513 
PHE   CG    CD1    doub Y N 514 
PHE   CG    CD2    sing Y N 515 
PHE   CD1   CE1    sing Y N 516 
PHE   CD1   HD1    sing N N 517 
PHE   CD2   CE2    doub Y N 518 
PHE   CD2   HD2    sing N N 519 
PHE   CE1   CZ     doub Y N 520 
PHE   CE1   HE1    sing N N 521 
PHE   CE2   CZ     sing Y N 522 
PHE   CE2   HE2    sing N N 523 
PHE   CZ    HZ     sing N N 524 
PHE   OXT   HXT    sing N N 525 
PRO   N     CA     sing N N 526 
PRO   N     CD     sing N N 527 
PRO   N     H      sing N N 528 
PRO   CA    C      sing N N 529 
PRO   CA    CB     sing N N 530 
PRO   CA    HA     sing N N 531 
PRO   C     O      doub N N 532 
PRO   C     OXT    sing N N 533 
PRO   CB    CG     sing N N 534 
PRO   CB    HB2    sing N N 535 
PRO   CB    HB3    sing N N 536 
PRO   CG    CD     sing N N 537 
PRO   CG    HG2    sing N N 538 
PRO   CG    HG3    sing N N 539 
PRO   CD    HD2    sing N N 540 
PRO   CD    HD3    sing N N 541 
PRO   OXT   HXT    sing N N 542 
SER   N     CA     sing N N 543 
SER   N     H      sing N N 544 
SER   N     H2     sing N N 545 
SER   CA    C      sing N N 546 
SER   CA    CB     sing N N 547 
SER   CA    HA     sing N N 548 
SER   C     O      doub N N 549 
SER   C     OXT    sing N N 550 
SER   CB    OG     sing N N 551 
SER   CB    HB2    sing N N 552 
SER   CB    HB3    sing N N 553 
SER   OG    HG     sing N N 554 
SER   OXT   HXT    sing N N 555 
SO4   S     O1     doub N N 556 
SO4   S     O2     doub N N 557 
SO4   S     O3     sing N N 558 
SO4   S     O4     sing N N 559 
THR   N     CA     sing N N 560 
THR   N     H      sing N N 561 
THR   N     H2     sing N N 562 
THR   CA    C      sing N N 563 
THR   CA    CB     sing N N 564 
THR   CA    HA     sing N N 565 
THR   C     O      doub N N 566 
THR   C     OXT    sing N N 567 
THR   CB    OG1    sing N N 568 
THR   CB    CG2    sing N N 569 
THR   CB    HB     sing N N 570 
THR   OG1   HG1    sing N N 571 
THR   CG2   HG21   sing N N 572 
THR   CG2   HG22   sing N N 573 
THR   CG2   HG23   sing N N 574 
THR   OXT   HXT    sing N N 575 
TRP   N     CA     sing N N 576 
TRP   N     H      sing N N 577 
TRP   N     H2     sing N N 578 
TRP   CA    C      sing N N 579 
TRP   CA    CB     sing N N 580 
TRP   CA    HA     sing N N 581 
TRP   C     O      doub N N 582 
TRP   C     OXT    sing N N 583 
TRP   CB    CG     sing N N 584 
TRP   CB    HB2    sing N N 585 
TRP   CB    HB3    sing N N 586 
TRP   CG    CD1    doub Y N 587 
TRP   CG    CD2    sing Y N 588 
TRP   CD1   NE1    sing Y N 589 
TRP   CD1   HD1    sing N N 590 
TRP   CD2   CE2    doub Y N 591 
TRP   CD2   CE3    sing Y N 592 
TRP   NE1   CE2    sing Y N 593 
TRP   NE1   HE1    sing N N 594 
TRP   CE2   CZ2    sing Y N 595 
TRP   CE3   CZ3    doub Y N 596 
TRP   CE3   HE3    sing N N 597 
TRP   CZ2   CH2    doub Y N 598 
TRP   CZ2   HZ2    sing N N 599 
TRP   CZ3   CH2    sing Y N 600 
TRP   CZ3   HZ3    sing N N 601 
TRP   CH2   HH2    sing N N 602 
TRP   OXT   HXT    sing N N 603 
TYR   N     CA     sing N N 604 
TYR   N     H      sing N N 605 
TYR   N     H2     sing N N 606 
TYR   CA    C      sing N N 607 
TYR   CA    CB     sing N N 608 
TYR   CA    HA     sing N N 609 
TYR   C     O      doub N N 610 
TYR   C     OXT    sing N N 611 
TYR   CB    CG     sing N N 612 
TYR   CB    HB2    sing N N 613 
TYR   CB    HB3    sing N N 614 
TYR   CG    CD1    doub Y N 615 
TYR   CG    CD2    sing Y N 616 
TYR   CD1   CE1    sing Y N 617 
TYR   CD1   HD1    sing N N 618 
TYR   CD2   CE2    doub Y N 619 
TYR   CD2   HD2    sing N N 620 
TYR   CE1   CZ     doub Y N 621 
TYR   CE1   HE1    sing N N 622 
TYR   CE2   CZ     sing Y N 623 
TYR   CE2   HE2    sing N N 624 
TYR   CZ    OH     sing N N 625 
TYR   OH    HH     sing N N 626 
TYR   OXT   HXT    sing N N 627 
VAL   N     CA     sing N N 628 
VAL   N     H      sing N N 629 
VAL   N     H2     sing N N 630 
VAL   CA    C      sing N N 631 
VAL   CA    CB     sing N N 632 
VAL   CA    HA     sing N N 633 
VAL   C     O      doub N N 634 
VAL   C     OXT    sing N N 635 
VAL   CB    CG1    sing N N 636 
VAL   CB    CG2    sing N N 637 
VAL   CB    HB     sing N N 638 
VAL   CG1   HG11   sing N N 639 
VAL   CG1   HG12   sing N N 640 
VAL   CG1   HG13   sing N N 641 
VAL   CG2   HG21   sing N N 642 
VAL   CG2   HG22   sing N N 643 
VAL   CG2   HG23   sing N N 644 
VAL   OXT   HXT    sing N N 645 
# 
_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                    9E0D 
_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]   0.009971 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002930 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009851 
_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]   0.008299 
_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  
MG 
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   ? -49.211 93.802  103.155 1.00 44.25 ? 14   ALA   A N     1 
ATOM   2     C  CA    . ALA   A  1  16   ? -48.138 92.828  103.350 1.00 48.46 ? 14   ALA   A CA    1 
ATOM   3     C  C     . ALA   A  1  16   ? -48.708 91.424  103.533 1.00 45.09 ? 14   ALA   A C     1 
ATOM   4     O  O     . ALA   A  1  16   ? -49.390 91.154  104.519 1.00 48.11 ? 14   ALA   A O     1 
ATOM   5     C  CB    . ALA   A  1  16   ? -47.283 93.214  104.547 1.00 49.05 ? 14   ALA   A CB    1 
ATOM   6     N  N     . PRO   A  1  17   ? -48.423 90.527  102.588 1.00 43.27 ? 15   PRO   A N     1 
ATOM   7     C  CA    . PRO   A  1  17   ? -49.001 89.179  102.663 1.00 37.41 ? 15   PRO   A CA    1 
ATOM   8     C  C     . PRO   A  1  17   ? -48.462 88.417  103.864 1.00 39.71 ? 15   PRO   A C     1 
ATOM   9     O  O     . PRO   A  1  17   ? -47.287 88.529  104.221 1.00 34.68 ? 15   PRO   A O     1 
ATOM   10    C  CB    . PRO   A  1  17   ? -48.563 88.530  101.347 1.00 37.70 ? 15   PRO   A CB    1 
ATOM   11    C  CG    . PRO   A  1  17   ? -47.338 89.279  100.951 1.00 39.34 ? 15   PRO   A CG    1 
ATOM   12    C  CD    . PRO   A  1  17   ? -47.531 90.689  101.428 1.00 39.36 ? 15   PRO   A CD    1 
ATOM   13    N  N     . ALA   A  1  18   ? -49.343 87.645  104.490 1.00 35.30 ? 16   ALA   A N     1 
ATOM   14    C  CA    . ALA   A  1  18   ? -48.964 86.912  105.684 1.00 31.06 ? 16   ALA   A CA    1 
ATOM   15    C  C     . ALA   A  1  18   ? -47.910 85.868  105.329 1.00 27.98 ? 16   ALA   A C     1 
ATOM   16    O  O     . ALA   A  1  18   ? -47.956 85.284  104.242 1.00 28.21 ? 16   ALA   A O     1 
ATOM   17    C  CB    . ALA   A  1  18   ? -50.192 86.232  106.293 1.00 33.06 ? 16   ALA   A CB    1 
ATOM   18    N  N     . PRO   A  1  19   ? -46.949 85.616  106.212 1.00 27.07 ? 17   PRO   A N     1 
ATOM   19    C  CA    . PRO   A  1  19   ? -45.881 84.663  105.889 1.00 27.15 ? 17   PRO   A CA    1 
ATOM   20    C  C     . PRO   A  1  19   ? -46.442 83.265  105.688 1.00 24.60 ? 17   PRO   A C     1 
ATOM   21    O  O     . PRO   A  1  19   ? -47.238 82.774  106.492 1.00 27.13 ? 17   PRO   A O     1 
ATOM   22    C  CB    . PRO   A  1  19   ? -44.966 84.735  107.118 1.00 29.96 ? 17   PRO   A CB    1 
ATOM   23    C  CG    . PRO   A  1  19   ? -45.255 86.076  107.727 1.00 29.52 ? 17   PRO   A CG    1 
ATOM   24    C  CD    . PRO   A  1  19   ? -46.718 86.298  107.497 1.00 26.74 ? 17   PRO   A CD    1 
ATOM   25    N  N     . PHE   A  1  20   ? -46.043 82.639  104.583 1.00 23.64 ? 18   PHE   A N     1 
ATOM   26    C  CA    . PHE   A  1  20   ? -46.394 81.269  104.225 1.00 23.89 ? 18   PHE   A CA    1 
ATOM   27    C  C     . PHE   A  1  20   ? -47.874 81.078  103.933 1.00 26.61 ? 18   PHE   A C     1 
ATOM   28    O  O     . PHE   A  1  20   ? -48.331 79.933  103.823 1.00 25.50 ? 18   PHE   A O     1 
ATOM   29    C  CB    . PHE   A  1  20   ? -45.913 80.249  105.261 1.00 24.25 ? 18   PHE   A CB    1 
ATOM   30    C  CG    . PHE   A  1  20   ? -44.437 80.310  105.526 1.00 24.03 ? 18   PHE   A CG    1 
ATOM   31    C  CD1   . PHE   A  1  20   ? -43.536 79.783  104.616 1.00 23.36 ? 18   PHE   A CD1   1 
ATOM   32    C  CD2   . PHE   A  1  20   ? -43.955 80.892  106.689 1.00 24.71 ? 18   PHE   A CD2   1 
ATOM   33    C  CE1   . PHE   A  1  20   ? -42.173 79.834  104.862 1.00 23.77 ? 18   PHE   A CE1   1 
ATOM   34    C  CE2   . PHE   A  1  20   ? -42.595 80.943  106.940 1.00 25.62 ? 18   PHE   A CE2   1 
ATOM   35    C  CZ    . PHE   A  1  20   ? -41.706 80.420  106.028 1.00 25.16 ? 18   PHE   A CZ    1 
ATOM   36    N  N     . ALA   A  1  21   ? -48.633 82.161  103.788 1.00 27.40 ? 19   ALA   A N     1 
ATOM   37    C  CA    . ALA   A  1  21   ? -50.054 82.029  103.493 1.00 25.35 ? 19   ALA   A CA    1 
ATOM   38    C  C     . ALA   A  1  21   ? -50.303 81.418  102.125 1.00 30.71 ? 19   ALA   A C     1 
ATOM   39    O  O     . ALA   A  1  21   ? -51.387 80.877  101.885 1.00 29.36 ? 19   ALA   A O     1 
ATOM   40    C  CB    . ALA   A  1  21   ? -50.741 83.391  103.610 1.00 28.11 ? 19   ALA   A CB    1 
ATOM   41    N  N     . ASP   A  1  22   ? -49.327 81.483  101.230 1.00 24.39 ? 20   ASP   A N     1 
ATOM   42    C  CA    . ASP   A  1  22   ? -49.455 80.938  99.886  1.00 26.69 ? 20   ASP   A CA    1 
ATOM   43    C  C     . ASP   A  1  22   ? -48.275 80.036  99.578  1.00 21.70 ? 20   ASP   A C     1 
ATOM   44    O  O     . ASP   A  1  22   ? -47.767 80.002  98.453  1.00 24.98 ? 20   ASP   A O     1 
ATOM   45    C  CB    . ASP   A  1  22   ? -49.569 82.055  98.853  1.00 31.24 ? 20   ASP   A CB    1 
ATOM   46    C  CG    . ASP   A  1  22   ? -50.792 82.926  99.069  1.00 40.85 ? 20   ASP   A CG    1 
ATOM   47    O  OD1   . ASP   A  1  22   ? -51.906 82.373  99.175  1.00 47.55 ? 20   ASP   A OD1   1 
ATOM   48    O  OD2   . ASP   A  1  22   ? -50.636 84.163  99.149  1.00 51.61 ? 20   ASP   A OD2   1 
ATOM   49    N  N     . PHE   A  1  23   ? -47.816 79.299  100.591 1.00 21.64 ? 21   PHE   A N     1 
ATOM   50    C  CA    . PHE   A  1  23   ? -46.561 78.569  100.459 1.00 19.73 ? 21   PHE   A CA    1 
ATOM   51    C  C     . PHE   A  1  23   ? -46.615 77.564  99.315  1.00 19.72 ? 21   PHE   A C     1 
ATOM   52    O  O     . PHE   A  1  23   ? -45.782 77.596  98.403  1.00 19.94 ? 21   PHE   A O     1 
ATOM   53    C  CB    . PHE   A  1  23   ? -46.187 77.876  101.769 1.00 20.68 ? 21   PHE   A CB    1 
ATOM   54    C  CG    . PHE   A  1  23   ? -44.981 77.004  101.640 1.00 19.22 ? 21   PHE   A CG    1 
ATOM   55    C  CD1   . PHE   A  1  23   ? -43.765 77.556  101.278 1.00 21.99 ? 21   PHE   A CD1   1 
ATOM   56    C  CD2   . PHE   A  1  23   ? -45.060 75.634  101.833 1.00 20.14 ? 21   PHE   A CD2   1 
ATOM   57    C  CE1   . PHE   A  1  23   ? -42.634 76.758  101.125 1.00 21.66 ? 21   PHE   A CE1   1 
ATOM   58    C  CE2   . PHE   A  1  23   ? -43.938 74.832  101.686 1.00 22.58 ? 21   PHE   A CE2   1 
ATOM   59    C  CZ    . PHE   A  1  23   ? -42.726 75.396  101.327 1.00 21.57 ? 21   PHE   A CZ    1 
ATOM   60    N  N     . ALA   A  1  24   ? -47.576 76.642  99.359  1.00 21.57 ? 22   ALA   A N     1 
ATOM   61    C  CA    . ALA   A  1  24   ? -47.615 75.583  98.355  1.00 22.61 ? 22   ALA   A CA    1 
ATOM   62    C  C     . ALA   A  1  24   ? -49.013 74.993  98.237  1.00 19.65 ? 22   ALA   A C     1 
ATOM   63    O  O     . ALA   A  1  24   ? -49.187 73.772  98.373  1.00 19.84 ? 22   ALA   A O     1 
ATOM   64    C  CB    . ALA   A  1  24   ? -46.609 74.480  98.693  1.00 24.91 ? 22   ALA   A CB    1 
ATOM   65    N  N     . PRO   A  1  25   ? -50.024 75.808  97.956  1.00 22.07 ? 23   PRO   A N     1 
ATOM   66    C  CA    . PRO   A  1  25   ? -51.381 75.279  97.860  1.00 23.42 ? 23   PRO   A CA    1 
ATOM   67    C  C     . PRO   A  1  25   ? -51.466 74.278  96.724  1.00 21.55 ? 23   PRO   A C     1 
ATOM   68    O  O     . PRO   A  1  25   ? -50.872 74.481  95.655  1.00 21.30 ? 23   PRO   A O     1 
ATOM   69    C  CB    . PRO   A  1  25   ? -52.223 76.527  97.563  1.00 24.50 ? 23   PRO   A CB    1 
ATOM   70    C  CG    . PRO   A  1  25   ? -51.299 77.440  96.866  1.00 25.00 ? 23   PRO   A CG    1 
ATOM   71    C  CD    . PRO   A  1  25   ? -49.954 77.216  97.524  1.00 23.83 ? 23   PRO   A CD    1 
ATOM   72    N  N     . PRO   A  1  26   ? -52.147 73.160  96.934  1.00 22.06 ? 24   PRO   A N     1 
ATOM   73    C  CA    . PRO   A  1  26   ? -52.275 72.173  95.862  1.00 22.24 ? 24   PRO   A CA    1 
ATOM   74    C  C     . PRO   A  1  26   ? -53.101 72.725  94.713  1.00 20.68 ? 24   PRO   A C     1 
ATOM   75    O  O     . PRO   A  1  26   ? -53.885 73.668  94.859  1.00 21.75 ? 24   PRO   A O     1 
ATOM   76    C  CB    . PRO   A  1  26   ? -52.987 70.998  96.540  1.00 22.59 ? 24   PRO   A CB    1 
ATOM   77    C  CG    . PRO   A  1  26   ? -53.738 71.635  97.677  1.00 28.51 ? 24   PRO   A CG    1 
ATOM   78    C  CD    . PRO   A  1  26   ? -52.855 72.755  98.160  1.00 24.35 ? 24   PRO   A CD    1 
ATOM   79    N  N     . VAL   A  1  27   ? -52.891 72.121  93.543  1.00 20.81 ? 25   VAL   A N     1 
ATOM   80    C  CA    . VAL   A  1  27   ? -53.678 72.473  92.364  1.00 19.31 ? 25   VAL   A CA    1 
ATOM   81    C  C     . VAL   A  1  27   ? -55.168 72.348  92.649  1.00 24.11 ? 25   VAL   A C     1 
ATOM   82    O  O     . VAL   A  1  27   ? -55.967 73.214  92.267  1.00 23.10 ? 25   VAL   A O     1 
ATOM   83    C  CB    . VAL   A  1  27   ? -53.253 71.601  91.170  1.00 19.38 ? 25   VAL   A CB    1 
ATOM   84    C  CG1   . VAL   A  1  27   ? -54.212 71.807  90.018  1.00 22.24 ? 25   VAL   A CG1   1 
ATOM   85    C  CG2   . VAL   A  1  27   ? -51.831 71.938  90.761  1.00 21.32 ? 25   VAL   A CG2   1 
ATOM   86    N  N     . ARG   A  1  28   ? -55.564 71.281  93.329  1.00 23.36 ? 26   ARG   A N     1 
ATOM   87    C  CA    . ARG   A  1  28   ? -56.961 71.059  93.666  1.00 23.57 ? 26   ARG   A CA    1 
ATOM   88    C  C     . ARG   A  1  28   ? -57.013 70.368  95.017  1.00 27.65 ? 26   ARG   A C     1 
ATOM   89    O  O     . ARG   A  1  28   ? -56.020 69.774  95.451  1.00 22.64 ? 26   ARG   A O     1 
ATOM   90    C  CB    . ARG   A  1  28   ? -57.632 70.169  92.611  1.00 25.95 ? 26   ARG   A CB    1 
ATOM   91    C  CG    . ARG   A  1  28   ? -57.085 68.744  92.595  1.00 28.69 ? 26   ARG   A CG    1 
ATOM   92    C  CD    . ARG   A  1  28   ? -57.607 67.923  91.419  1.00 32.27 ? 26   ARG   A CD    1 
ATOM   93    N  NE    . ARG   A  1  28   ? -56.955 68.285  90.168  1.00 33.16 ? 26   ARG   A NE    1 
ATOM   94    C  CZ    . ARG   A  1  28   ? -57.469 69.110  89.267  1.00 35.35 ? 26   ARG   A CZ    1 
ATOM   95    N  NH1   . ARG   A  1  28   ? -58.666 69.656  89.430  1.00 35.76 ? 26   ARG   A NH1   1 
ATOM   96    N  NH2   . ARG   A  1  28   ? -56.764 69.399  88.178  1.00 30.86 ? 26   ARG   A NH2   1 
ATOM   97    N  N     . PRO   A  1  29   ? -58.151 70.432  95.714  1.00 24.04 ? 27   PRO   A N     1 
ATOM   98    C  CA    . PRO   A  1  29   ? -58.292 69.645  96.943  1.00 26.44 ? 27   PRO   A CA    1 
ATOM   99    C  C     . PRO   A  1  29   ? -58.075 68.172  96.633  1.00 23.95 ? 27   PRO   A C     1 
ATOM   100   O  O     . PRO   A  1  29   ? -58.502 67.667  95.593  1.00 23.71 ? 27   PRO   A O     1 
ATOM   101   C  CB    . PRO   A  1  29   ? -59.736 69.925  97.380  1.00 26.17 ? 27   PRO   A CB    1 
ATOM   102   C  CG    . PRO   A  1  29   ? -60.074 71.240  96.737  1.00 26.28 ? 27   PRO   A CG    1 
ATOM   103   C  CD    . PRO   A  1  29   ? -59.351 71.235  95.424  1.00 26.38 ? 27   PRO   A CD    1 
ATOM   104   N  N     . GLN   A  1  30   ? -57.382 67.487  97.531  1.00 23.29 ? 28   GLN   A N     1 
ATOM   105   C  CA    . GLN   A  1  30   ? -56.984 66.111  97.268  1.00 24.38 ? 28   GLN   A CA    1 
ATOM   106   C  C     . GLN   A  1  30   ? -58.139 65.173  97.592  1.00 23.16 ? 28   GLN   A C     1 
ATOM   107   O  O     . GLN   A  1  30   ? -58.559 65.077  98.746  1.00 25.65 ? 28   GLN   A O     1 
ATOM   108   C  CB    . GLN   A  1  30   ? -55.760 65.764  98.106  1.00 24.00 ? 28   GLN   A CB    1 
ATOM   109   C  CG    . GLN   A  1  30   ? -54.562 66.652  97.813  1.00 22.61 ? 28   GLN   A CG    1 
ATOM   110   C  CD    . GLN   A  1  30   ? -54.046 66.486  96.396  1.00 22.42 ? 28   GLN   A CD    1 
ATOM   111   O  OE1   . GLN   A  1  30   ? -53.368 65.509  96.077  1.00 20.89 ? 28   GLN   A OE1   1 
ATOM   112   N  NE2   . GLN   A  1  30   ? -54.355 67.443  95.543  1.00 22.09 ? 28   GLN   A NE2   1 
ATOM   113   N  N     . SER   A  1  31   ? -58.642 64.479  96.577  1.00 22.39 ? 29   SER   A N     1 
ATOM   114   C  CA    . SER   A  1  31   ? -59.708 63.511  96.786  1.00 20.27 ? 29   SER   A CA    1 
ATOM   115   C  C     . SER   A  1  31   ? -59.192 62.315  97.584  1.00 24.23 ? 29   SER   A C     1 
ATOM   116   O  O     . SER   A  1  31   ? -57.985 62.128  97.774  1.00 21.92 ? 29   SER   A O     1 
ATOM   117   C  CB    . SER   A  1  31   ? -60.229 63.016  95.444  1.00 21.19 ? 29   SER   A CB    1 
ATOM   118   O  OG    . SER   A  1  31   ? -59.232 62.223  94.813  1.00 20.69 ? 29   SER   A OG    1 
ATOM   119   N  N     . THR   A  1  32   ? -60.133 61.486  98.046  1.00 24.02 ? 30   THR   A N     1 
ATOM   120   C  CA    . THR   A  1  32   ? -59.771 60.239  98.708  1.00 21.78 ? 30   THR   A CA    1 
ATOM   121   C  C     . THR   A  1  32   ? -58.831 59.418  97.839  1.00 22.15 ? 30   THR   A C     1 
ATOM   122   O  O     . THR   A  1  32   ? -57.837 58.873  98.327  1.00 21.62 ? 30   THR   A O     1 
ATOM   123   C  CB    . THR   A  1  32   ? -61.037 59.434  99.029  1.00 24.66 ? 30   THR   A CB    1 
ATOM   124   O  OG1   . THR   A  1  32   ? -61.895 60.224  99.858  1.00 30.25 ? 30   THR   A OG1   1 
ATOM   125   C  CG2   . THR   A  1  32   ? -60.690 58.141  99.752  1.00 28.10 ? 30   THR   A CG2   1 
ATOM   126   N  N     . LEU   A  1  33   ? -59.131 59.323  96.546  1.00 22.53 ? 31   LEU   A N     1 
ATOM   127   C  CA    . LEU   A  1  33   ? -58.280 58.541  95.664  1.00 19.88 ? 31   LEU   A CA    1 
ATOM   128   C  C     . LEU   A  1  33   ? -56.914 59.188  95.500  1.00 20.26 ? 31   LEU   A C     1 
ATOM   129   O  O     . LEU   A  1  33   ? -55.900 58.487  95.456  1.00 19.75 ? 31   LEU   A O     1 
ATOM   130   C  CB    . LEU   A  1  33   ? -58.960 58.336  94.314  1.00 19.79 ? 31   LEU   A CB    1 
ATOM   131   C  CG    . LEU   A  1  33   ? -60.114 57.333  94.359  1.00 23.00 ? 31   LEU   A CG    1 
ATOM   132   C  CD1   . LEU   A  1  33   ? -60.961 57.446  93.115  1.00 22.93 ? 31   LEU   A CD1   1 
ATOM   133   C  CD2   . LEU   A  1  33   ? -59.587 55.909  94.528  1.00 26.86 ? 31   LEU   A CD2   1 
ATOM   134   N  N     . ARG   A  1  34   ? -56.858 60.521  95.402  1.00 18.89 ? 32   ARG   A N     1 
ATOM   135   C  CA    . ARG   A  1  34   ? -55.552 61.169  95.291  1.00 17.64 ? 32   ARG   A CA    1 
ATOM   136   C  C     . ARG   A  1  34   ? -54.762 61.011  96.579  1.00 19.05 ? 32   ARG   A C     1 
ATOM   137   O  O     . ARG   A  1  34   ? -53.548 60.790  96.549  1.00 19.86 ? 32   ARG   A O     1 
ATOM   138   C  CB    . ARG   A  1  34   ? -55.721 62.647  94.948  1.00 20.65 ? 32   ARG   A CB    1 
ATOM   139   C  CG    . ARG   A  1  34   ? -56.161 62.898  93.522  1.00 20.08 ? 32   ARG   A CG    1 
ATOM   140   C  CD    . ARG   A  1  34   ? -55.021 62.615  92.535  1.00 21.60 ? 32   ARG   A CD    1 
ATOM   141   N  NE    . ARG   A  1  34   ? -53.908 63.553  92.668  1.00 19.69 ? 32   ARG   A NE    1 
ATOM   142   C  CZ    . ARG   A  1  34   ? -53.828 64.719  92.037  1.00 22.40 ? 32   ARG   A CZ    1 
ATOM   143   N  NH1   . ARG   A  1  34   ? -54.779 65.126  91.208  1.00 22.44 ? 32   ARG   A NH1   1 
ATOM   144   N  NH2   . ARG   A  1  34   ? -52.766 65.496  92.239  1.00 21.73 ? 32   ARG   A NH2   1 
ATOM   145   N  N     . ARG   A  1  35   ? -55.437 61.095  97.721  1.00 20.10 ? 33   ARG   A N     1 
ATOM   146   C  CA    . ARG   A  1  35   ? -54.742 60.941  98.990  1.00 19.60 ? 33   ARG   A CA    1 
ATOM   147   C  C     . ARG   A  1  35   ? -54.176 59.535  99.153  1.00 20.25 ? 33   ARG   A C     1 
ATOM   148   O  O     . ARG   A  1  35   ? -53.110 59.362  99.762  1.00 20.57 ? 33   ARG   A O     1 
ATOM   149   C  CB    . ARG   A  1  35   ? -55.696 61.300  100.135 1.00 21.80 ? 33   ARG   A CB    1 
ATOM   150   C  CG    . ARG   A  1  35   ? -55.953 62.801  100.246 1.00 23.96 ? 33   ARG   A CG    1 
ATOM   151   C  CD    . ARG   A  1  35   ? -56.943 63.126  101.373 1.00 27.52 ? 33   ARG   A CD    1 
ATOM   152   N  N     . ALA   A  1  36   ? -54.868 58.523  98.622  1.00 20.07 ? 34   ALA   A N     1 
ATOM   153   C  CA    . ALA   A  1  36   ? -54.347 57.162  98.701  1.00 21.17 ? 34   ALA   A CA    1 
ATOM   154   C  C     . ALA   A  1  36   ? -53.082 57.009  97.873  1.00 20.75 ? 34   ALA   A C     1 
ATOM   155   O  O     . ALA   A  1  36   ? -52.172 56.266  98.256  1.00 21.37 ? 34   ALA   A O     1 
ATOM   156   C  CB    . ALA   A  1  36   ? -55.407 56.149  98.267  1.00 22.09 ? 34   ALA   A CB    1 
ATOM   157   N  N     . ILE   A  1  37   ? -53.001 57.719  96.747  1.00 17.35 ? 35   ILE   A N     1 
ATOM   158   C  CA    . ILE   A  1  37   ? -51.765 57.736  95.974  1.00 17.50 ? 35   ILE   A CA    1 
ATOM   159   C  C     . ILE   A  1  37   ? -50.633 58.309  96.810  1.00 17.72 ? 35   ILE   A C     1 
ATOM   160   O  O     . ILE   A  1  37   ? -49.569 57.696  96.960  1.00 17.89 ? 35   ILE   A O     1 
ATOM   161   C  CB    . ILE   A  1  37   ? -51.966 58.534  94.678  1.00 16.58 ? 35   ILE   A CB    1 
ATOM   162   C  CG1   . ILE   A  1  37   ? -52.945 57.807  93.763  1.00 17.06 ? 35   ILE   A CG1   1 
ATOM   163   C  CG2   . ILE   A  1  37   ? -50.620 58.720  93.997  1.00 15.87 ? 35   ILE   A CG2   1 
ATOM   164   C  CD1   . ILE   A  1  37   ? -53.431 58.676  92.626  1.00 18.44 ? 35   ILE   A CD1   1 
ATOM   165   N  N     . THR   A  1  38   ? -50.842 59.506  97.353  1.00 18.13 ? 36   THR   A N     1 
ATOM   166   C  CA    . THR   A  1  38   ? -49.779 60.168  98.096  1.00 18.05 ? 36   THR   A CA    1 
ATOM   167   C  C     . THR   A  1  38   ? -49.338 59.329  99.285  1.00 19.34 ? 36   THR   A C     1 
ATOM   168   O  O     . THR   A  1  38   ? -48.141 59.248  99.586  1.00 19.19 ? 36   THR   A O     1 
ATOM   169   C  CB    . THR   A  1  38   ? -50.264 61.541  98.534  1.00 18.69 ? 36   THR   A CB    1 
ATOM   170   O  OG1   . THR   A  1  38   ? -50.770 62.231  97.389  1.00 19.90 ? 36   THR   A OG1   1 
ATOM   171   C  CG2   . THR   A  1  38   ? -49.133 62.332  99.142  1.00 20.96 ? 36   THR   A CG2   1 
ATOM   172   N  N     . ALA   A  1  39   ? -50.286 58.660  99.944  1.00 18.71 ? 37   ALA   A N     1 
ATOM   173   C  CA    . ALA   A  1  39   ? -49.939 57.846  101.102 1.00 20.31 ? 37   ALA   A CA    1 
ATOM   174   C  C     . ALA   A  1  39   ? -49.002 56.693  100.764 1.00 22.84 ? 37   ALA   A C     1 
ATOM   175   O  O     . ALA   A  1  39   ? -48.272 56.233  101.647 1.00 23.30 ? 37   ALA   A O     1 
ATOM   176   C  CB    . ALA   A  1  39   ? -51.209 57.319  101.774 1.00 21.65 ? 37   ALA   A CB    1 
ATOM   177   N  N     . ALA   A  1  40   ? -48.992 56.225  99.515  1.00 19.35 ? 38   ALA   A N     1 
ATOM   178   C  CA    . ALA   A  1  40   ? -48.156 55.104  99.116  1.00 20.87 ? 38   ALA   A CA    1 
ATOM   179   C  C     . ALA   A  1  40   ? -46.795 55.541  98.604  1.00 19.91 ? 38   ALA   A C     1 
ATOM   180   O  O     . ALA   A  1  40   ? -45.977 54.678  98.277  1.00 20.43 ? 38   ALA   A O     1 
ATOM   181   C  CB    . ALA   A  1  40   ? -48.844 54.291  98.022  1.00 19.32 ? 38   ALA   A CB    1 
ATOM   182   N  N     . TYR   A  1  41   ? -46.548 56.852  98.518  1.00 18.88 ? 39   TYR   A N     1 
ATOM   183   C  CA    . TYR   A  1  41   ? -45.384 57.378  97.803  1.00 17.71 ? 39   TYR   A CA    1 
ATOM   184   C  C     . TYR   A  1  41   ? -44.101 56.645  98.179  1.00 18.78 ? 39   TYR   A C     1 
ATOM   185   O  O     . TYR   A  1  41   ? -43.356 56.180  97.307  1.00 18.55 ? 39   TYR   A O     1 
ATOM   186   C  CB    . TYR   A  1  41   ? -45.275 58.872  98.103  1.00 17.92 ? 39   TYR   A CB    1 
ATOM   187   C  CG    . TYR   A  1  41   ? -44.509 59.743  97.122  1.00 16.90 ? 39   TYR   A CG    1 
ATOM   188   C  CD1   . TYR   A  1  41   ? -43.431 59.260  96.387  1.00 18.10 ? 39   TYR   A CD1   1 
ATOM   189   C  CD2   . TYR   A  1  41   ? -44.855 61.077  96.968  1.00 19.05 ? 39   TYR   A CD2   1 
ATOM   190   C  CE1   . TYR   A  1  41   ? -42.734 60.095  95.516  1.00 17.76 ? 39   TYR   A CE1   1 
ATOM   191   C  CE2   . TYR   A  1  41   ? -44.174 61.904  96.112  1.00 18.12 ? 39   TYR   A CE2   1 
ATOM   192   C  CZ    . TYR   A  1  41   ? -43.107 61.413  95.388  1.00 18.25 ? 39   TYR   A CZ    1 
ATOM   193   O  OH    . TYR   A  1  41   ? -42.416 62.247  94.528  1.00 18.60 ? 39   TYR   A OH    1 
ATOM   194   N  N     . ARG   A  1  42   ? -43.826 56.524  99.469  1.00 19.41 ? 40   ARG   A N     1 
ATOM   195   C  CA    . ARG   A  1  42   ? -42.600 55.881  99.922  1.00 20.60 ? 40   ARG   A CA    1 
ATOM   196   C  C     . ARG   A  1  42   ? -42.902 54.783  100.928 1.00 19.30 ? 40   ARG   A C     1 
ATOM   197   O  O     . ARG   A  1  42   ? -42.129 54.537  101.864 1.00 23.62 ? 40   ARG   A O     1 
ATOM   198   C  CB    . ARG   A  1  42   ? -41.619 56.902  100.474 1.00 22.35 ? 40   ARG   A CB    1 
ATOM   199   C  CG    . ARG   A  1  42   ? -41.173 57.861  99.398  1.00 22.50 ? 40   ARG   A CG    1 
ATOM   200   C  CD    . ARG   A  1  42   ? -40.337 58.974  99.932  1.00 22.70 ? 40   ARG   A CD    1 
ATOM   201   N  NE    . ARG   A  1  42   ? -40.330 60.032  98.936  1.00 20.92 ? 40   ARG   A NE    1 
ATOM   202   C  CZ    . ARG   A  1  42   ? -39.531 60.061  97.881  1.00 20.36 ? 40   ARG   A CZ    1 
ATOM   203   N  NH1   . ARG   A  1  42   ? -38.550 59.180  97.729  1.00 20.95 ? 40   ARG   A NH1   1 
ATOM   204   N  NH2   . ARG   A  1  42   ? -39.723 60.994  96.956  1.00 18.82 ? 40   ARG   A NH2   1 
ATOM   205   N  N     . ARG   A  1  43   ? -44.018 54.102  100.716 1.00 21.20 ? 41   ARG   A N     1 
ATOM   206   C  CA    . ARG   A  1  43   ? -44.454 53.046  101.618 1.00 21.03 ? 41   ARG   A CA    1 
ATOM   207   C  C     . ARG   A  1  43   ? -43.385 51.960  101.691 1.00 24.05 ? 41   ARG   A C     1 
ATOM   208   O  O     . ARG   A  1  43   ? -42.782 51.613  100.670 1.00 22.42 ? 41   ARG   A O     1 
ATOM   209   C  CB    . ARG   A  1  43   ? -45.743 52.440  101.073 1.00 21.30 ? 41   ARG   A CB    1 
ATOM   210   C  CG    . ARG   A  1  43   ? -46.284 51.273  101.885 1.00 23.27 ? 41   ARG   A CG    1 
ATOM   211   C  CD    . ARG   A  1  43   ? -47.701 51.006  101.476 1.00 26.53 ? 41   ARG   A CD    1 
ATOM   212   N  NE    . ARG   A  1  43   ? -48.547 52.131  101.854 1.00 24.17 ? 41   ARG   A NE    1 
ATOM   213   C  CZ    . ARG   A  1  43   ? -49.668 52.472  101.236 1.00 21.25 ? 41   ARG   A CZ    1 
ATOM   214   N  NH1   . ARG   A  1  43   ? -50.102 51.813  100.175 1.00 23.62 ? 41   ARG   A NH1   1 
ATOM   215   N  NH2   . ARG   A  1  43   ? -50.371 53.503  101.697 1.00 24.04 ? 41   ARG   A NH2   1 
ATOM   216   N  N     . PRO   A  1  44   ? -43.115 51.412  102.872 1.00 24.36 ? 42   PRO   A N     1 
ATOM   217   C  CA    . PRO   A  1  44   ? -42.120 50.343  102.968 1.00 23.64 ? 42   PRO   A CA    1 
ATOM   218   C  C     . PRO   A  1  44   ? -42.432 49.210  102.003 1.00 19.13 ? 42   PRO   A C     1 
ATOM   219   O  O     . PRO   A  1  44   ? -43.589 48.867  101.754 1.00 22.82 ? 42   PRO   A O     1 
ATOM   220   C  CB    . PRO   A  1  44   ? -42.231 49.893  104.426 1.00 23.38 ? 42   PRO   A CB    1 
ATOM   221   C  CG    . PRO   A  1  44   ? -42.689 51.123  105.141 1.00 29.94 ? 42   PRO   A CG    1 
ATOM   222   C  CD    . PRO   A  1  44   ? -43.627 51.815  104.190 1.00 27.24 ? 42   PRO   A CD    1 
ATOM   223   N  N     . GLU   A  1  45   ? -41.369 48.671  101.408 1.00 23.47 ? 43   GLU   A N     1 
ATOM   224   C  CA    . GLU   A  1  45   ? -41.521 47.650  100.383 1.00 24.27 ? 43   GLU   A CA    1 
ATOM   225   C  C     . GLU   A  1  45   ? -42.224 46.405  100.914 1.00 22.74 ? 43   GLU   A C     1 
ATOM   226   O  O     . GLU   A  1  45   ? -43.010 45.780  100.191 1.00 24.71 ? 43   GLU   A O     1 
ATOM   227   C  CB    . GLU   A  1  45   ? -40.136 47.326  99.822  1.00 25.33 ? 43   GLU   A CB    1 
ATOM   228   C  CG    . GLU   A  1  45   ? -40.155 46.928  98.373  1.00 27.35 ? 43   GLU   A CG    1 
ATOM   229   C  CD    . GLU   A  1  45   ? -38.832 47.139  97.662  1.00 22.81 ? 43   GLU   A CD    1 
ATOM   230   O  OE1   . GLU   A  1  45   ? -37.919 47.818  98.191  1.00 21.89 ? 43   GLU   A OE1   1 
ATOM   231   O  OE2   . GLU   A  1  45   ? -38.712 46.594  96.557  1.00 21.56 ? 43   GLU   A OE2   1 
ATOM   232   N  N     . THR   A  1  46   ? -41.978 46.041  102.180 1.00 27.18 ? 44   THR   A N     1 
ATOM   233   C  CA    . THR   A  1  46   ? -42.653 44.891  102.779 1.00 27.75 ? 44   THR   A CA    1 
ATOM   234   C  C     . THR   A  1  46   ? -44.153 45.101  102.909 1.00 27.43 ? 44   THR   A C     1 
ATOM   235   O  O     . THR   A  1  46   ? -44.899 44.119  102.991 1.00 29.59 ? 44   THR   A O     1 
ATOM   236   C  CB    . THR   A  1  46   ? -42.072 44.591  104.161 1.00 26.70 ? 44   THR   A CB    1 
ATOM   237   O  OG1   . THR   A  1  46   ? -42.149 45.770  104.968 1.00 29.69 ? 44   THR   A OG1   1 
ATOM   238   C  CG2   . THR   A  1  46   ? -40.623 44.146  104.055 1.00 26.79 ? 44   THR   A CG2   1 
ATOM   239   N  N     . GLU   A  1  47   ? -44.610 46.350  102.945 1.00 25.27 ? 45   GLU   A N     1 
ATOM   240   C  CA    . GLU   A  1  47   ? -46.036 46.635  103.002 1.00 26.83 ? 45   GLU   A CA    1 
ATOM   241   C  C     . GLU   A  1  47   ? -46.673 46.682  101.619 1.00 22.93 ? 45   GLU   A C     1 
ATOM   242   O  O     . GLU   A  1  47   ? -47.871 46.407  101.485 1.00 25.83 ? 45   GLU   A O     1 
ATOM   243   C  CB    . GLU   A  1  47   ? -46.269 47.951  103.746 1.00 28.17 ? 45   GLU   A CB    1 
ATOM   244   C  CG    . GLU   A  1  47   ? -45.948 47.854  105.231 1.00 35.46 ? 45   GLU   A CG    1 
ATOM   245   C  CD    . GLU   A  1  47   ? -45.967 49.199  105.929 1.00 39.62 ? 45   GLU   A CD    1 
ATOM   246   O  OE1   . GLU   A  1  47   ? -46.690 50.105  105.459 1.00 39.24 ? 45   GLU   A OE1   1 
ATOM   247   O  OE2   . GLU   A  1  47   ? -45.256 49.349  106.947 1.00 49.31 ? 45   GLU   A OE2   1 
ATOM   248   N  N     . CYS   A  1  48   ? -45.892 47.004  100.584 1.00 21.80 ? 46   CYS   A N     1 
ATOM   249   C  CA    . CYS   A  1  48   ? -46.444 47.090  99.236  1.00 22.20 ? 46   CYS   A CA    1 
ATOM   250   C  C     . CYS   A  1  48   ? -46.697 45.722  98.627  1.00 20.17 ? 46   CYS   A C     1 
ATOM   251   O  O     . CYS   A  1  48   ? -47.669 45.541  97.890  1.00 22.03 ? 46   CYS   A O     1 
ATOM   252   C  CB    . CYS   A  1  48   ? -45.479 47.834  98.313  1.00 21.82 ? 46   CYS   A CB    1 
ATOM   253   S  SG    . CYS   A  1  48   ? -45.178 49.549  98.732  1.00 23.60 ? 46   CYS   A SG    1 
ATOM   254   N  N     . LEU   A  1  49   ? -45.815 44.755  98.891  1.00 22.45 ? 47   LEU   A N     1 
ATOM   255   C  CA    . LEU   A  1  49   ? -45.825 43.513  98.122  1.00 25.16 ? 47   LEU   A CA    1 
ATOM   256   C  C     . LEU   A  1  49   ? -47.012 42.579  98.366  1.00 24.54 ? 47   LEU   A C     1 
ATOM   257   O  O     . LEU   A  1  49   ? -47.553 42.040  97.389  1.00 24.98 ? 47   LEU   A O     1 
ATOM   258   C  CB    . LEU   A  1  49   ? -44.486 42.773  98.233  1.00 26.32 ? 47   LEU   A CB    1 
ATOM   259   C  CG    . LEU   A  1  49   ? -43.519 43.049  97.079  1.00 24.86 ? 47   LEU   A CG    1 
ATOM   260   C  CD1   . LEU   A  1  49   ? -44.121 42.555  95.771  1.00 25.33 ? 47   LEU   A CD1   1 
ATOM   261   C  CD2   . LEU   A  1  49   ? -43.204 44.531  96.987  1.00 24.26 ? 47   LEU   A CD2   1 
ATOM   262   N  N     . PRO   A  1  50   ? -47.444 42.337  99.606  1.00 25.88 ? 48   PRO   A N     1 
ATOM   263   C  CA    . PRO   A  1  50   ? -48.499 41.327  99.838  1.00 26.47 ? 48   PRO   A CA    1 
ATOM   264   C  C     . PRO   A  1  50   ? -49.768 41.578  99.037  1.00 25.98 ? 48   PRO   A C     1 
ATOM   265   O  O     . PRO   A  1  50   ? -50.273 40.639  98.404  1.00 27.84 ? 48   PRO   A O     1 
ATOM   266   C  CB    . PRO   A  1  50   ? -48.742 41.406  101.356 1.00 28.99 ? 48   PRO   A CB    1 
ATOM   267   C  CG    . PRO   A  1  50   ? -47.411 41.772  101.891 1.00 26.12 ? 48   PRO   A CG    1 
ATOM   268   C  CD    . PRO   A  1  50   ? -46.839 42.766  100.880 1.00 24.82 ? 48   PRO   A CD    1 
ATOM   269   N  N     . PRO   A  1  51   ? -50.327 42.800  99.020  1.00 23.76 ? 49   PRO   A N     1 
ATOM   270   C  CA    . PRO   A  1  51   ? -51.526 42.996  98.188  1.00 28.21 ? 49   PRO   A CA    1 
ATOM   271   C  C     . PRO   A  1  51   ? -51.261 42.792  96.708  1.00 22.92 ? 49   PRO   A C     1 
ATOM   272   O  O     . PRO   A  1  51   ? -52.165 42.362  95.982  1.00 25.68 ? 49   PRO   A O     1 
ATOM   273   C  CB    . PRO   A  1  51   ? -51.981 44.427  98.518  1.00 25.62 ? 49   PRO   A CB    1 
ATOM   274   C  CG    . PRO   A  1  51   ? -50.790 45.095  99.061  1.00 25.75 ? 49   PRO   A CG    1 
ATOM   275   C  CD    . PRO   A  1  51   ? -49.983 44.032  99.757  1.00 26.62 ? 49   PRO   A CD    1 
ATOM   276   N  N     . LEU   A  1  52   ? -50.035 43.070  96.247  1.00 24.86 ? 50   LEU   A N     1 
ATOM   277   C  CA    . LEU   A  1  52   ? -49.688 42.840  94.848  1.00 23.70 ? 50   LEU   A CA    1 
ATOM   278   C  C     . LEU   A  1  52   ? -49.588 41.351  94.554  1.00 22.89 ? 50   LEU   A C     1 
ATOM   279   O  O     . LEU   A  1  52   ? -50.080 40.877  93.524  1.00 23.71 ? 50   LEU   A O     1 
ATOM   280   C  CB    . LEU   A  1  52   ? -48.367 43.540  94.525  1.00 20.95 ? 50   LEU   A CB    1 
ATOM   281   C  CG    . LEU   A  1  52   ? -48.351 45.072  94.663  1.00 22.77 ? 50   LEU   A CG    1 
ATOM   282   C  CD1   . LEU   A  1  52   ? -46.927 45.603  94.516  1.00 21.95 ? 50   LEU   A CD1   1 
ATOM   283   C  CD2   . LEU   A  1  52   ? -49.268 45.744  93.652  1.00 22.48 ? 50   LEU   A CD2   1 
ATOM   284   N  N     . VAL   A  1  53   ? -48.958 40.599  95.456  1.00 23.88 ? 51   VAL   A N     1 
ATOM   285   C  CA    . VAL   A  1  53   ? -48.918 39.145  95.322  1.00 23.96 ? 51   VAL   A CA    1 
ATOM   286   C  C     . VAL   A  1  53   ? -50.329 38.582  95.217  1.00 24.26 ? 51   VAL   A C     1 
ATOM   287   O  O     . VAL   A  1  53   ? -50.627 37.754  94.345  1.00 26.97 ? 51   VAL   A O     1 
ATOM   288   C  CB    . VAL   A  1  53   ? -48.137 38.526  96.494  1.00 22.33 ? 51   VAL   A CB    1 
ATOM   289   C  CG1   . VAL   A  1  53   ? -48.236 37.011  96.460  1.00 28.78 ? 51   VAL   A CG1   1 
ATOM   290   C  CG2   . VAL   A  1  53   ? -46.688 38.973  96.455  1.00 27.17 ? 51   VAL   A CG2   1 
ATOM   291   N  N     . GLU   A  1  54   ? -51.231 39.044  96.088  1.00 25.98 ? 52   GLU   A N     1 
ATOM   292   C  CA    . GLU   A  1  54   ? -52.595 38.530  96.052  1.00 27.63 ? 52   GLU   A CA    1 
ATOM   293   C  C     . GLU   A  1  54   ? -53.280 38.880  94.739  1.00 26.26 ? 52   GLU   A C     1 
ATOM   294   O  O     . GLU   A  1  54   ? -53.900 38.019  94.102  1.00 28.16 ? 52   GLU   A O     1 
ATOM   295   C  CB    . GLU   A  1  54   ? -53.406 39.025  97.250  1.00 29.66 ? 52   GLU   A CB    1 
ATOM   296   C  CG    . GLU   A  1  54   ? -54.853 38.531  97.224  1.00 32.77 ? 52   GLU   A CG    1 
ATOM   297   C  CD    . GLU   A  1  54   ? -54.960 37.011  97.095  1.00 39.13 ? 52   GLU   A CD    1 
ATOM   298   O  OE1   . GLU   A  1  54   ? -54.145 36.292  97.711  1.00 42.53 ? 52   GLU   A OE1   1 
ATOM   299   O  OE2   . GLU   A  1  54   ? -55.867 36.532  96.375  1.00 41.36 ? 52   GLU   A OE2   1 
ATOM   300   N  N     . ALA   A  1  55   ? -53.150 40.135  94.297  1.00 24.60 ? 53   ALA   A N     1 
ATOM   301   C  CA    . ALA   A  1  55   ? -53.833 40.560  93.079  1.00 24.64 ? 53   ALA   A CA    1 
ATOM   302   C  C     . ALA   A  1  55   ? -53.272 39.860  91.850  1.00 23.35 ? 53   ALA   A C     1 
ATOM   303   O  O     . ALA   A  1  55   ? -53.998 39.638  90.874  1.00 26.00 ? 53   ALA   A O     1 
ATOM   304   C  CB    . ALA   A  1  55   ? -53.744 42.078  92.927  1.00 25.94 ? 53   ALA   A CB    1 
ATOM   305   N  N     . ALA   A  1  56   ? -51.996 39.499  91.881  1.00 24.35 ? 54   ALA   A N     1 
ATOM   306   C  CA    . ALA   A  1  56   ? -51.338 38.869  90.749  1.00 25.14 ? 54   ALA   A CA    1 
ATOM   307   C  C     . ALA   A  1  56   ? -51.452 37.353  90.761  1.00 28.68 ? 54   ALA   A C     1 
ATOM   308   O  O     . ALA   A  1  56   ? -50.956 36.702  89.834  1.00 27.32 ? 54   ALA   A O     1 
ATOM   309   C  CB    . ALA   A  1  56   ? -49.861 39.263  90.726  1.00 21.79 ? 54   ALA   A CB    1 
ATOM   310   N  N     . THR   A  1  57   ? -52.077 36.778  91.782  1.00 27.89 ? 55   THR   A N     1 
ATOM   311   C  CA    . THR   A  1  57   ? -52.165 35.331  91.873  1.00 27.51 ? 55   THR   A CA    1 
ATOM   312   C  C     . THR   A  1  57   ? -53.088 34.802  90.785  1.00 28.32 ? 55   THR   A C     1 
ATOM   313   O  O     . THR   A  1  57   ? -54.147 35.372  90.518  1.00 30.49 ? 55   THR   A O     1 
ATOM   314   C  CB    . THR   A  1  57   ? -52.699 34.948  93.251  1.00 30.52 ? 55   THR   A CB    1 
ATOM   315   O  OG1   . THR   A  1  57   ? -51.732 35.320  94.239  1.00 30.51 ? 55   THR   A OG1   1 
ATOM   316   C  CG2   . THR   A  1  57   ? -52.973 33.447  93.343  1.00 32.01 ? 55   THR   A CG2   1 
ATOM   317   N  N     . GLN   A  1  58   ? -52.674 33.713  90.142  1.00 28.04 ? 56   GLN   A N     1 
ATOM   318   C  CA    . GLN   A  1  58   ? -53.498 33.059  89.139  1.00 27.73 ? 56   GLN   A CA    1 
ATOM   319   C  C     . GLN   A  1  58   ? -53.548 31.568  89.439  1.00 26.93 ? 56   GLN   A C     1 
ATOM   320   O  O     . GLN   A  1  58   ? -52.770 31.051  90.241  1.00 30.31 ? 56   GLN   A O     1 
ATOM   321   C  CB    . GLN   A  1  58   ? -52.986 33.324  87.720  1.00 26.88 ? 56   GLN   A CB    1 
ATOM   322   C  CG    . GLN   A  1  58   ? -52.938 34.794  87.351  1.00 27.38 ? 56   GLN   A CG    1 
ATOM   323   C  CD    . GLN   A  1  58   ? -52.775 34.999  85.864  1.00 25.74 ? 56   GLN   A CD    1 
ATOM   324   O  OE1   . GLN   A  1  58   ? -53.745 34.932  85.115  1.00 28.65 ? 56   GLN   A OE1   1 
ATOM   325   N  NE2   . GLN   A  1  58   ? -51.542 35.240  85.423  1.00 28.33 ? 56   GLN   A NE2   1 
ATOM   326   N  N     . SER   A  1  59   ? -54.485 30.884  88.795  1.00 28.73 ? 57   SER   A N     1 
ATOM   327   C  CA    . SER   A  1  59   ? -54.677 29.470  89.060  1.00 28.02 ? 57   SER   A CA    1 
ATOM   328   C  C     . SER   A  1  59   ? -53.465 28.675  88.594  1.00 34.41 ? 57   SER   A C     1 
ATOM   329   O  O     . SER   A  1  59   ? -52.685 29.115  87.742  1.00 31.07 ? 57   SER   A O     1 
ATOM   330   C  CB    . SER   A  1  59   ? -55.906 28.956  88.320  1.00 30.87 ? 57   SER   A CB    1 
ATOM   331   O  OG    . SER   A  1  59   ? -55.686 28.973  86.918  1.00 34.52 ? 57   SER   A OG    1 
ATOM   332   N  N     . LYS   A  1  60   ? -53.311 27.484  89.174  1.00 31.53 ? 58   LYS   A N     1 
ATOM   333   C  CA    . LYS   A  1  60   ? -52.251 26.585  88.735  1.00 33.08 ? 58   LYS   A CA    1 
ATOM   334   C  C     . LYS   A  1  60   ? -52.365 26.290  87.244  1.00 31.84 ? 58   LYS   A C     1 
ATOM   335   O  O     . LYS   A  1  60   ? -51.355 26.263  86.532  1.00 33.37 ? 58   LYS   A O     1 
ATOM   336   C  CB    . LYS   A  1  60   ? -52.294 25.293  89.554  1.00 35.63 ? 58   LYS   A CB    1 
ATOM   337   C  CG    . LYS   A  1  60   ? -51.178 24.315  89.226  1.00 36.80 ? 58   LYS   A CG    1 
ATOM   338   C  CD    . LYS   A  1  60   ? -49.816 24.952  89.442  1.00 44.03 ? 58   LYS   A CD    1 
ATOM   339   C  CE    . LYS   A  1  60   ? -48.728 23.904  89.648  1.00 47.69 ? 58   LYS   A CE    1 
ATOM   340   N  NZ    . LYS   A  1  60   ? -48.559 23.019  88.462  1.00 50.28 ? 58   LYS   A NZ    1 
ATOM   341   N  N     . GLU   A  1  61   ? -53.586 26.076  86.751  1.00 32.84 ? 59   GLU   A N     1 
ATOM   342   C  CA    . GLU   A  1  61   ? -53.775 25.810  85.328  1.00 33.51 ? 59   GLU   A CA    1 
ATOM   343   C  C     . GLU   A  1  61   ? -53.270 26.975  84.487  1.00 34.69 ? 59   GLU   A C     1 
ATOM   344   O  O     . GLU   A  1  61   ? -52.587 26.778  83.477  1.00 34.94 ? 59   GLU   A O     1 
ATOM   345   C  CB    . GLU   A  1  61   ? -55.250 25.527  85.034  1.00 35.66 ? 59   GLU   A CB    1 
ATOM   346   N  N     . ILE   A  1  62   ? -53.594 28.201  84.896  1.00 31.55 ? 60   ILE   A N     1 
ATOM   347   C  CA    . ILE   A  1  62   ? -53.107 29.369  84.170  1.00 32.02 ? 60   ILE   A CA    1 
ATOM   348   C  C     . ILE   A  1  62   ? -51.594 29.474  84.271  1.00 33.54 ? 60   ILE   A C     1 
ATOM   349   O  O     . ILE   A  1  62   ? -50.908 29.757  83.279  1.00 33.05 ? 60   ILE   A O     1 
ATOM   350   C  CB    . ILE   A  1  62   ? -53.802 30.642  84.672  1.00 30.41 ? 60   ILE   A CB    1 
ATOM   351   C  CG1   . ILE   A  1  62   ? -55.214 30.702  84.112  1.00 32.43 ? 60   ILE   A CG1   1 
ATOM   352   C  CG2   . ILE   A  1  62   ? -52.985 31.881  84.297  1.00 30.76 ? 60   ILE   A CG2   1 
ATOM   353   C  CD1   . ILE   A  1  62   ? -55.969 31.855  84.605  1.00 35.54 ? 60   ILE   A CD1   1 
ATOM   354   N  N     . ARG   A  1  63   ? -51.047 29.256  85.467  1.00 30.47 ? 61   ARG   A N     1 
ATOM   355   C  CA    . ARG   A  1  63   ? -49.606 29.389  85.642  1.00 30.15 ? 61   ARG   A CA    1 
ATOM   356   C  C     . ARG   A  1  63   ? -48.843 28.402  84.771  1.00 32.29 ? 61   ARG   A C     1 
ATOM   357   O  O     . ARG   A  1  63   ? -47.813 28.753  84.184  1.00 29.81 ? 61   ARG   A O     1 
ATOM   358   C  CB    . ARG   A  1  63   ? -49.239 29.270  87.119  1.00 31.73 ? 61   ARG   A CB    1 
ATOM   359   C  CG    . ARG   A  1  63   ? -49.690 30.485  87.903  1.00 35.48 ? 61   ARG   A CG    1 
ATOM   360   C  CD    . ARG   A  1  63   ? -49.188 30.491  89.323  1.00 40.07 ? 61   ARG   A CD    1 
ATOM   361   N  NE    . ARG   A  1  63   ? -49.921 29.561  90.166  1.00 39.53 ? 61   ARG   A NE    1 
ATOM   362   C  CZ    . ARG   A  1  63   ? -49.470 28.368  90.519  1.00 44.24 ? 61   ARG   A CZ    1 
ATOM   363   N  NH1   . ARG   A  1  63   ? -48.293 27.928  90.111  1.00 43.81 ? 61   ARG   A NH1   1 
ATOM   364   N  NH2   . ARG   A  1  63   ? -50.220 27.598  91.302  1.00 43.69 ? 61   ARG   A NH2   1 
ATOM   365   N  N     . ASP   A  1  64   ? -49.342 27.170  84.654  1.00 33.66 ? 62   ASP   A N     1 
ATOM   366   C  CA    . ASP   A  1  64   ? -48.708 26.205  83.764  1.00 34.18 ? 62   ASP   A CA    1 
ATOM   367   C  C     . ASP   A  1  64   ? -48.855 26.618  82.304  1.00 31.83 ? 62   ASP   A C     1 
ATOM   368   O  O     . ASP   A  1  64   ? -47.915 26.470  81.516  1.00 33.55 ? 62   ASP   A O     1 
ATOM   369   C  CB    . ASP   A  1  64   ? -49.297 24.815  83.997  1.00 34.82 ? 62   ASP   A CB    1 
ATOM   370   C  CG    . ASP   A  1  64   ? -48.958 24.265  85.367  1.00 36.02 ? 62   ASP   A CG    1 
ATOM   371   O  OD1   . ASP   A  1  64   ? -48.151 24.898  86.079  1.00 37.53 ? 62   ASP   A OD1   1 
ATOM   372   O  OD2   . ASP   A  1  64   ? -49.506 23.199  85.734  1.00 43.91 ? 62   ASP   A OD2   1 
ATOM   373   N  N     . ALA   A  1  65   ? -50.032 27.125  81.925  1.00 30.09 ? 63   ALA   A N     1 
ATOM   374   C  CA    . ALA   A  1  65   ? -50.235 27.575  80.551  1.00 32.05 ? 63   ALA   A CA    1 
ATOM   375   C  C     . ALA   A  1  65   ? -49.350 28.770  80.238  1.00 33.39 ? 63   ALA   A C     1 
ATOM   376   O  O     . ALA   A  1  65   ? -48.764 28.852  79.151  1.00 34.04 ? 63   ALA   A O     1 
ATOM   377   C  CB    . ALA   A  1  65   ? -51.708 27.916  80.319  1.00 32.91 ? 63   ALA   A CB    1 
ATOM   378   N  N     . ALA   A  1  66   ? -49.234 29.703  81.185  1.00 30.22 ? 64   ALA   A N     1 
ATOM   379   C  CA    . ALA   A  1  66   ? -48.358 30.852  80.994  1.00 32.62 ? 64   ALA   A CA    1 
ATOM   380   C  C     . ALA   A  1  66   ? -46.908 30.416  80.852  1.00 31.15 ? 64   ALA   A C     1 
ATOM   381   O  O     . ALA   A  1  66   ? -46.180 30.919  79.986  1.00 30.55 ? 64   ALA   A O     1 
ATOM   382   C  CB    . ALA   A  1  66   ? -48.507 31.822  82.164  1.00 29.49 ? 64   ALA   A CB    1 
ATOM   383   N  N     . ALA   A  1  67   ? -46.468 29.479  81.696  1.00 28.14 ? 65   ALA   A N     1 
ATOM   384   C  CA    . ALA   A  1  67   ? -45.096 28.997  81.601  1.00 32.24 ? 65   ALA   A CA    1 
ATOM   385   C  C     . ALA   A  1  67   ? -44.848 28.326  80.255  1.00 30.77 ? 65   ALA   A C     1 
ATOM   386   O  O     . ALA   A  1  67   ? -43.787 28.512  79.645  1.00 32.67 ? 65   ALA   A O     1 
ATOM   387   C  CB    . ALA   A  1  67   ? -44.794 28.037  82.753  1.00 32.38 ? 65   ALA   A CB    1 
ATOM   388   N  N     . SER   A  1  68   ? -45.820 27.553  79.771  1.00 32.66 ? 66   SER   A N     1 
ATOM   389   C  CA    . SER   A  1  68   ? -45.677 26.922  78.464  1.00 35.10 ? 66   SER   A CA    1 
ATOM   390   C  C     . SER   A  1  68   ? -45.603 27.966  77.357  1.00 35.22 ? 66   SER   A C     1 
ATOM   391   O  O     . SER   A  1  68   ? -44.751 27.883  76.465  1.00 34.07 ? 66   SER   A O     1 
ATOM   392   C  CB    . SER   A  1  68   ? -46.829 25.950  78.219  1.00 35.66 ? 66   SER   A CB    1 
ATOM   393   O  OG    . SER   A  1  68   ? -46.788 25.468  76.890  1.00 42.55 ? 66   SER   A OG    1 
ATOM   394   N  N     . THR   A  1  69   ? -46.489 28.964  77.403  1.00 32.38 ? 67   THR   A N     1 
ATOM   395   C  CA    . THR   A  1  69   ? -46.459 30.025  76.403  1.00 30.60 ? 67   THR   A CA    1 
ATOM   396   C  C     . THR   A  1  69   ? -45.145 30.794  76.449  1.00 29.76 ? 67   THR   A C     1 
ATOM   397   O  O     . THR   A  1  69   ? -44.550 31.078  75.404  1.00 29.09 ? 67   THR   A O     1 
ATOM   398   C  CB    . THR   A  1  69   ? -47.643 30.965  76.612  1.00 30.52 ? 67   THR   A CB    1 
ATOM   399   O  OG1   . THR   A  1  69   ? -48.853 30.277  76.277  1.00 29.89 ? 67   THR   A OG1   1 
ATOM   400   C  CG2   . THR   A  1  69   ? -47.507 32.218  75.740  1.00 27.51 ? 67   THR   A CG2   1 
ATOM   401   N  N     . ALA   A  1  70   ? -44.678 31.142  77.649  1.00 31.13 ? 68   ALA   A N     1 
ATOM   402   C  CA    . ALA   A  1  70   ? -43.417 31.869  77.764  1.00 29.60 ? 68   ALA   A CA    1 
ATOM   403   C  C     . ALA   A  1  70   ? -42.262 31.057  77.197  1.00 31.59 ? 68   ALA   A C     1 
ATOM   404   O  O     . ALA   A  1  70   ? -41.420 31.589  76.464  1.00 30.63 ? 68   ALA   A O     1 
ATOM   405   C  CB    . ALA   A  1  70   ? -43.144 32.247  79.221  1.00 28.88 ? 68   ALA   A CB    1 
ATOM   406   N  N     . ARG   A  1  71   ? -42.209 29.764  77.524  1.00 28.93 ? 69   ARG   A N     1 
ATOM   407   C  CA    . ARG   A  1  71   ? -41.145 28.914  77.000  1.00 31.05 ? 69   ARG   A CA    1 
ATOM   408   C  C     . ARG   A  1  71   ? -41.191 28.864  75.480  1.00 33.38 ? 69   ARG   A C     1 
ATOM   409   O  O     . ARG   A  1  71   ? -40.153 28.969  74.815  1.00 33.08 ? 69   ARG   A O     1 
ATOM   410   C  CB    . ARG   A  1  71   ? -41.269 27.511  77.589  1.00 33.50 ? 69   ARG   A CB    1 
ATOM   411   C  CG    . ARG   A  1  71   ? -40.496 26.454  76.823  1.00 36.37 ? 69   ARG   A CG    1 
ATOM   412   C  CD    . ARG   A  1  71   ? -40.500 25.120  77.556  1.00 35.64 ? 69   ARG   A CD    1 
ATOM   413   N  NE    . ARG   A  1  71   ? -39.695 25.184  78.768  1.00 35.32 ? 69   ARG   A NE    1 
ATOM   414   C  CZ    . ARG   A  1  71   ? -38.372 25.108  78.784  1.00 39.92 ? 69   ARG   A CZ    1 
ATOM   415   N  NH1   . ARG   A  1  71   ? -37.674 24.965  77.668  1.00 42.24 ? 69   ARG   A NH1   1 
ATOM   416   N  NH2   . ARG   A  1  71   ? -37.732 25.193  79.947  1.00 42.93 ? 69   ARG   A NH2   1 
ATOM   417   N  N     . LYS   A  1  72   ? -42.393 28.734  74.915  1.00 31.33 ? 70   LYS   A N     1 
ATOM   418   C  CA    . LYS   A  1  72   ? -42.548 28.718  73.464  1.00 34.43 ? 70   LYS   A CA    1 
ATOM   419   C  C     . LYS   A  1  72   ? -42.069 30.024  72.838  1.00 36.43 ? 70   LYS   A C     1 
ATOM   420   O  O     . LYS   A  1  72   ? -41.374 30.012  71.814  1.00 33.09 ? 70   LYS   A O     1 
ATOM   421   C  CB    . LYS   A  1  72   ? -44.006 28.445  73.106  1.00 33.13 ? 70   LYS   A CB    1 
ATOM   422   C  CG    . LYS   A  1  72   ? -44.329 28.618  71.638  1.00 37.21 ? 70   LYS   A CG    1 
ATOM   423   C  CD    . LYS   A  1  72   ? -45.721 28.100  71.322  1.00 40.71 ? 70   LYS   A CD    1 
ATOM   424   C  CE    . LYS   A  1  72   ? -46.107 28.394  69.881  1.00 45.33 ? 70   LYS   A CE    1 
ATOM   425   N  NZ    . LYS   A  1  72   ? -45.013 28.026  68.937  1.00 56.92 ? 70   LYS   A NZ    1 
ATOM   426   N  N     . LEU   A  1  73   ? -42.422 31.161  73.443  1.00 31.64 ? 71   LEU   A N     1 
ATOM   427   C  CA    . LEU   A  1  73   ? -41.931 32.447  72.956  1.00 30.02 ? 71   LEU   A CA    1 
ATOM   428   C  C     . LEU   A  1  73   ? -40.414 32.531  73.057  1.00 31.92 ? 71   LEU   A C     1 
ATOM   429   O  O     . LEU   A  1  73   ? -39.747 33.006  72.132  1.00 32.05 ? 71   LEU   A O     1 
ATOM   430   C  CB    . LEU   A  1  73   ? -42.556 33.581  73.767  1.00 30.37 ? 71   LEU   A CB    1 
ATOM   431   C  CG    . LEU   A  1  73   ? -44.065 33.750  73.649  1.00 30.22 ? 71   LEU   A CG    1 
ATOM   432   C  CD1   . LEU   A  1  73   ? -44.542 34.765  74.673  1.00 27.80 ? 71   LEU   A CD1   1 
ATOM   433   C  CD2   . LEU   A  1  73   ? -44.435 34.194  72.249  1.00 32.36 ? 71   LEU   A CD2   1 
ATOM   434   N  N     . ILE   A  1  74   ? -39.854 32.086  74.182  1.00 29.67 ? 72   ILE   A N     1 
ATOM   435   C  CA    . ILE   A  1  74   ? -38.417 32.202  74.395  1.00 29.71 ? 72   ILE   A CA    1 
ATOM   436   C  C     . ILE   A  1  74   ? -37.658 31.267  73.464  1.00 30.50 ? 72   ILE   A C     1 
ATOM   437   O  O     . ILE   A  1  74   ? -36.606 31.631  72.924  1.00 31.38 ? 72   ILE   A O     1 
ATOM   438   C  CB    . ILE   A  1  74   ? -38.083 31.971  75.878  1.00 29.76 ? 72   ILE   A CB    1 
ATOM   439   C  CG1   . ILE   A  1  74   ? -38.631 33.134  76.713  1.00 31.51 ? 72   ILE   A CG1   1 
ATOM   440   C  CG2   . ILE   A  1  74   ? -36.578 31.803  76.082  1.00 30.56 ? 72   ILE   A CG2   1 
ATOM   441   C  CD1   . ILE   A  1  74   ? -38.729 32.838  78.190  1.00 33.56 ? 72   ILE   A CD1   1 
ATOM   442   N  N     . GLU   A  1  75   ? -38.178 30.057  73.253  1.00 33.87 ? 73   GLU   A N     1 
ATOM   443   C  CA    . GLU   A  1  75   ? -37.548 29.149  72.300  1.00 35.06 ? 73   GLU   A CA    1 
ATOM   444   C  C     . GLU   A  1  75   ? -37.555 29.742  70.897  1.00 36.93 ? 73   GLU   A C     1 
ATOM   445   O  O     . GLU   A  1  75   ? -36.554 29.662  70.177  1.00 35.62 ? 73   GLU   A O     1 
ATOM   446   C  CB    . GLU   A  1  75   ? -38.230 27.783  72.339  1.00 36.19 ? 73   GLU   A CB    1 
ATOM   447   C  CG    . GLU   A  1  75   ? -37.854 26.970  73.565  1.00 37.64 ? 73   GLU   A CG    1 
ATOM   448   C  CD    . GLU   A  1  75   ? -38.722 25.745  73.766  1.00 43.01 ? 73   GLU   A CD    1 
ATOM   449   O  OE1   . GLU   A  1  75   ? -39.775 25.636  73.099  1.00 44.44 ? 73   GLU   A OE1   1 
ATOM   450   O  OE2   . GLU   A  1  75   ? -38.350 24.892  74.600  1.00 43.94 ? 73   GLU   A OE2   1 
ATOM   451   N  N     . ALA   A  1  76   ? -38.665 30.368  70.503  1.00 36.10 ? 74   ALA   A N     1 
ATOM   452   C  CA    . ALA   A  1  76   ? -38.704 31.051  69.214  1.00 35.04 ? 74   ALA   A CA    1 
ATOM   453   C  C     . ALA   A  1  76   ? -37.687 32.185  69.158  1.00 37.68 ? 74   ALA   A C     1 
ATOM   454   O  O     . ALA   A  1  76   ? -36.985 32.347  68.153  1.00 39.16 ? 74   ALA   A O     1 
ATOM   455   C  CB    . ALA   A  1  76   ? -40.114 31.569  68.934  1.00 35.52 ? 74   ALA   A CB    1 
ATOM   456   N  N     . LEU   A  1  77   ? -37.589 32.978  70.229  1.00 35.67 ? 75   LEU   A N     1 
ATOM   457   C  CA    . LEU   A  1  77   ? -36.626 34.076  70.262  1.00 33.80 ? 75   LEU   A CA    1 
ATOM   458   C  C     . LEU   A  1  77   ? -35.202 33.559  70.111  1.00 38.48 ? 75   LEU   A C     1 
ATOM   459   O  O     . LEU   A  1  77   ? -34.439 34.038  69.263  1.00 40.09 ? 75   LEU   A O     1 
ATOM   460   C  CB    . LEU   A  1  77   ? -36.760 34.857  71.569  1.00 33.93 ? 75   LEU   A CB    1 
ATOM   461   C  CG    . LEU   A  1  77   ? -37.865 35.910  71.643  1.00 34.81 ? 75   LEU   A CG    1 
ATOM   462   C  CD1   . LEU   A  1  77   ? -37.860 36.566  73.006  1.00 32.10 ? 75   LEU   A CD1   1 
ATOM   463   C  CD2   . LEU   A  1  77   ? -37.664 36.941  70.552  1.00 34.74 ? 75   LEU   A CD2   1 
ATOM   464   N  N     . ARG   A  1  78   ? -34.826 32.579  70.933  1.00 34.58 ? 76   ARG   A N     1 
ATOM   465   C  CA    . ARG   A  1  78   ? -33.463 32.067  70.894  1.00 35.79 ? 76   ARG   A CA    1 
ATOM   466   C  C     . ARG   A  1  78   ? -33.180 31.294  69.615  1.00 38.71 ? 76   ARG   A C     1 
ATOM   467   O  O     . ARG   A  1  78   ? -32.025 31.226  69.180  1.00 42.29 ? 76   ARG   A O     1 
ATOM   468   C  CB    . ARG   A  1  78   ? -33.200 31.213  72.131  1.00 31.12 ? 76   ARG   A CB    1 
ATOM   469   C  CG    . ARG   A  1  78   ? -33.054 32.052  73.380  1.00 35.09 ? 76   ARG   A CG    1 
ATOM   470   C  CD    . ARG   A  1  78   ? -32.686 31.227  74.586  1.00 32.82 ? 76   ARG   A CD    1 
ATOM   471   N  NE    . ARG   A  1  78   ? -32.129 32.077  75.629  1.00 32.76 ? 76   ARG   A NE    1 
ATOM   472   C  CZ    . ARG   A  1  78   ? -31.706 31.640  76.806  1.00 32.38 ? 76   ARG   A CZ    1 
ATOM   473   N  NH1   . ARG   A  1  78   ? -31.790 30.362  77.139  1.00 36.39 ? 76   ARG   A NH1   1 
ATOM   474   N  NH2   . ARG   A  1  78   ? -31.178 32.507  77.668  1.00 35.28 ? 76   ARG   A NH2   1 
ATOM   475   N  N     . GLY   A  1  79   ? -34.204 30.715  69.000  1.00 37.61 ? 77   GLY   A N     1 
ATOM   476   C  CA    . GLY   A  1  79   ? -34.027 29.982  67.765  1.00 40.22 ? 77   GLY   A CA    1 
ATOM   477   C  C     . GLY   A  1  79   ? -33.831 30.827  66.529  1.00 45.29 ? 77   GLY   A C     1 
ATOM   478   O  O     . GLY   A  1  79   ? -33.620 30.283  65.443  1.00 47.71 ? 77   GLY   A O     1 
ATOM   479   N  N     . LYS   A  1  80   ? -33.896 32.152  66.655  1.00 46.73 ? 78   LYS   A N     1 
ATOM   480   C  CA    . LYS   A  1  80   ? -33.719 33.044  65.517  1.00 48.07 ? 78   LYS   A CA    1 
ATOM   481   C  C     . LYS   A  1  80   ? -32.782 34.205  65.826  1.00 48.63 ? 78   LYS   A C     1 
ATOM   482   O  O     . LYS   A  1  80   ? -32.723 35.159  65.042  1.00 53.95 ? 78   LYS   A O     1 
ATOM   483   C  CB    . LYS   A  1  80   ? -35.074 33.567  65.020  1.00 48.68 ? 78   LYS   A CB    1 
ATOM   484   C  CG    . LYS   A  1  80   ? -35.798 34.459  66.021  1.00 48.99 ? 78   LYS   A CG    1 
ATOM   485   C  CD    . LYS   A  1  80   ? -37.233 34.741  65.596  1.00 43.28 ? 78   LYS   A CD    1 
ATOM   486   C  CE    . LYS   A  1  80   ? -37.922 35.680  66.577  1.00 38.42 ? 78   LYS   A CE    1 
ATOM   487   N  NZ    . LYS   A  1  80   ? -39.361 35.926  66.237  1.00 33.54 ? 78   LYS   A NZ    1 
ATOM   488   N  N     . HIS   A  1  81   ? -32.051 34.147  66.939  1.00 50.38 ? 79   HIS   A N     1 
ATOM   489   C  CA    . HIS   A  1  81   ? -31.196 35.246  67.391  1.00 54.67 ? 79   HIS   A CA    1 
ATOM   490   C  C     . HIS   A  1  81   ? -30.215 35.733  66.323  1.00 59.00 ? 79   HIS   A C     1 
ATOM   491   O  O     . HIS   A  1  81   ? -29.447 34.952  65.764  1.00 63.60 ? 79   HIS   A O     1 
ATOM   492   C  CB    . HIS   A  1  81   ? -30.430 34.838  68.654  1.00 53.92 ? 79   HIS   A CB    1 
ATOM   493   N  N     . SER   A  1  84   ? -26.181 41.689  66.558  1.00 46.73 ? 82   SER   A N     1 
ATOM   494   C  CA    . SER   A  1  84   ? -25.447 40.772  65.695  1.00 49.89 ? 82   SER   A CA    1 
ATOM   495   C  C     . SER   A  1  84   ? -24.698 41.533  64.606  1.00 45.45 ? 82   SER   A C     1 
ATOM   496   O  O     . SER   A  1  84   ? -23.649 41.089  64.144  1.00 42.03 ? 82   SER   A O     1 
ATOM   497   C  CB    . SER   A  1  84   ? -26.387 39.734  65.071  1.00 51.32 ? 82   SER   A CB    1 
ATOM   498   N  N     . GLY   A  1  85   ? -25.244 42.676  64.194  1.00 43.31 ? 83   GLY   A N     1 
ATOM   499   C  CA    . GLY   A  1  85   ? -24.576 43.517  63.221  1.00 39.73 ? 83   GLY   A CA    1 
ATOM   500   C  C     . GLY   A  1  85   ? -23.214 43.969  63.707  1.00 30.44 ? 83   GLY   A C     1 
ATOM   501   O  O     . GLY   A  1  85   ? -22.194 43.704  63.062  1.00 31.95 ? 83   GLY   A O     1 
ATOM   502   N  N     . VAL   A  1  86   ? -23.190 44.656  64.850  1.00 34.12 ? 84   VAL   A N     1 
ATOM   503   C  CA    . VAL   A  1  86   ? -21.921 45.072  65.442  1.00 33.58 ? 84   VAL   A CA    1 
ATOM   504   C  C     . VAL   A  1  86   ? -21.074 43.857  65.789  1.00 31.43 ? 84   VAL   A C     1 
ATOM   505   O  O     . VAL   A  1  86   ? -19.854 43.849  65.575  1.00 27.81 ? 84   VAL   A O     1 
ATOM   506   C  CB    . VAL   A  1  86   ? -22.174 45.979  66.661  1.00 37.04 ? 84   VAL   A CB    1 
ATOM   507   C  CG1   . VAL   A  1  86   ? -20.901 46.154  67.470  1.00 35.06 ? 84   VAL   A CG1   1 
ATOM   508   C  CG2   . VAL   A  1  86   ? -22.709 47.327  66.205  1.00 35.42 ? 84   VAL   A CG2   1 
ATOM   509   N  N     . GLU   A  1  87   ? -21.710 42.803  66.309  1.00 34.07 ? 85   GLU   A N     1 
ATOM   510   C  CA    . GLU   A  1  87   ? -20.975 41.594  66.669  1.00 34.44 ? 85   GLU   A CA    1 
ATOM   511   C  C     . GLU   A  1  87   ? -20.300 40.972  65.454  1.00 34.70 ? 85   GLU   A C     1 
ATOM   512   O  O     . GLU   A  1  87   ? -19.148 40.528  65.535  1.00 34.79 ? 85   GLU   A O     1 
ATOM   513   C  CB    . GLU   A  1  87   ? -21.910 40.588  67.342  1.00 38.56 ? 85   GLU   A CB    1 
ATOM   514   N  N     . GLY   A  1  88   ? -20.994 40.939  64.316  1.00 33.84 ? 86   GLY   A N     1 
ATOM   515   C  CA    . GLY   A  1  88   ? -20.395 40.381  63.117  1.00 30.12 ? 86   GLY   A CA    1 
ATOM   516   C  C     . GLY   A  1  88   ? -19.269 41.232  62.568  1.00 29.02 ? 86   GLY   A C     1 
ATOM   517   O  O     . GLY   A  1  88   ? -18.301 40.706  62.010  1.00 32.75 ? 86   GLY   A O     1 
ATOM   518   N  N     . LEU   A  1  89   ? -19.383 42.555  62.708  1.00 29.45 ? 87   LEU   A N     1 
ATOM   519   C  CA    . LEU   A  1  89   ? -18.305 43.443  62.291  1.00 30.14 ? 87   LEU   A CA    1 
ATOM   520   C  C     . LEU   A  1  89   ? -17.080 43.228  63.165  1.00 26.98 ? 87   LEU   A C     1 
ATOM   521   O  O     . LEU   A  1  89   ? -15.960 43.074  62.661  1.00 26.15 ? 87   LEU   A O     1 
ATOM   522   C  CB    . LEU   A  1  89   ? -18.785 44.892  62.382  1.00 29.30 ? 87   LEU   A CB    1 
ATOM   523   C  CG    . LEU   A  1  89   ? -18.102 45.985  61.553  1.00 34.10 ? 87   LEU   A CG    1 
ATOM   524   C  CD1   . LEU   A  1  89   ? -18.849 47.292  61.755  1.00 35.53 ? 87   LEU   A CD1   1 
ATOM   525   C  CD2   . LEU   A  1  89   ? -16.649 46.164  61.921  1.00 36.39 ? 87   LEU   A CD2   1 
ATOM   526   N  N     . VAL   A  1  90   ? -17.284 43.213  64.483  1.00 27.19 ? 88   VAL   A N     1 
ATOM   527   C  CA    . VAL   A  1  90   ? -16.188 42.952  65.411  1.00 27.23 ? 88   VAL   A CA    1 
ATOM   528   C  C     . VAL   A  1  90   ? -15.505 41.634  65.080  1.00 27.98 ? 88   VAL   A C     1 
ATOM   529   O  O     . VAL   A  1  90   ? -14.270 41.538  65.079  1.00 27.79 ? 88   VAL   A O     1 
ATOM   530   C  CB    . VAL   A  1  90   ? -16.712 42.988  66.857  1.00 26.06 ? 88   VAL   A CB    1 
ATOM   531   C  CG1   . VAL   A  1  90   ? -15.684 42.415  67.806  1.00 28.36 ? 88   VAL   A CG1   1 
ATOM   532   C  CG2   . VAL   A  1  90   ? -17.080 44.412  67.246  1.00 26.77 ? 88   VAL   A CG2   1 
ATOM   533   N  N     . GLN   A  1  91   ? -16.295 40.601  64.777  1.00 30.38 ? 89   GLN   A N     1 
ATOM   534   C  CA    . GLN   A  1  91   ? -15.731 39.295  64.451  1.00 29.92 ? 89   GLN   A CA    1 
ATOM   535   C  C     . GLN   A  1  91   ? -14.975 39.330  63.128  1.00 31.37 ? 89   GLN   A C     1 
ATOM   536   O  O     . GLN   A  1  91   ? -13.859 38.803  63.025  1.00 33.35 ? 89   GLN   A O     1 
ATOM   537   C  CB    . GLN   A  1  91   ? -16.844 38.244  64.405  1.00 32.01 ? 89   GLN   A CB    1 
ATOM   538   N  N     . GLU   A  1  92   ? -15.564 39.948  62.101  1.00 29.63 ? 90   GLU   A N     1 
ATOM   539   C  CA    . GLU   A  1  92   ? -14.950 39.918  60.775  1.00 29.46 ? 90   GLU   A CA    1 
ATOM   540   C  C     . GLU   A  1  92   ? -13.580 40.584  60.770  1.00 28.57 ? 90   GLU   A C     1 
ATOM   541   O  O     . GLU   A  1  92   ? -12.643 40.093  60.130  1.00 30.27 ? 90   GLU   A O     1 
ATOM   542   C  CB    . GLU   A  1  92   ? -15.874 40.574  59.748  1.00 30.92 ? 90   GLU   A CB    1 
ATOM   543   C  CG    . GLU   A  1  92   ? -15.214 40.809  58.394  1.00 31.98 ? 90   GLU   A CG    1 
ATOM   544   C  CD    . GLU   A  1  92   ? -16.189 41.323  57.349  1.00 36.67 ? 90   GLU   A CD    1 
ATOM   545   O  OE1   . GLU   A  1  92   ? -17.370 41.532  57.694  1.00 39.83 ? 90   GLU   A OE1   1 
ATOM   546   O  OE2   . GLU   A  1  92   ? -15.774 41.514  56.185  1.00 41.44 ? 90   GLU   A OE2   1 
ATOM   547   N  N     . TYR   A  1  93   ? -13.439 41.702  61.477  1.00 26.79 ? 91   TYR   A N     1 
ATOM   548   C  CA    . TYR   A  1  93   ? -12.189 42.448  61.490  1.00 27.25 ? 91   TYR   A CA    1 
ATOM   549   C  C     . TYR   A  1  93   ? -11.363 42.214  62.749  1.00 26.12 ? 91   TYR   A C     1 
ATOM   550   O  O     . TYR   A  1  93   ? -10.374 42.925  62.969  1.00 26.37 ? 91   TYR   A O     1 
ATOM   551   C  CB    . TYR   A  1  93   ? -12.459 43.934  61.267  1.00 27.39 ? 91   TYR   A CB    1 
ATOM   552   C  CG    . TYR   A  1  93   ? -12.940 44.211  59.868  1.00 25.60 ? 91   TYR   A CG    1 
ATOM   553   C  CD1   . TYR   A  1  93   ? -12.031 44.388  58.826  1.00 27.09 ? 91   TYR   A CD1   1 
ATOM   554   C  CD2   . TYR   A  1  93   ? -14.295 44.257  59.575  1.00 27.23 ? 91   TYR   A CD2   1 
ATOM   555   C  CE1   . TYR   A  1  93   ? -12.459 44.618  57.539  1.00 28.04 ? 91   TYR   A CE1   1 
ATOM   556   C  CE2   . TYR   A  1  93   ? -14.733 44.492  58.283  1.00 30.69 ? 91   TYR   A CE2   1 
ATOM   557   C  CZ    . TYR   A  1  93   ? -13.808 44.674  57.274  1.00 27.92 ? 91   TYR   A CZ    1 
ATOM   558   O  OH    . TYR   A  1  93   ? -14.234 44.905  55.989  1.00 36.57 ? 91   TYR   A OH    1 
ATOM   559   N  N     . SER   A  1  94   ? -11.743 41.233  63.568  1.00 25.55 ? 92   SER   A N     1 
ATOM   560   C  CA    . SER   A  1  94   ? -11.018 40.887  64.792  1.00 25.11 ? 92   SER   A CA    1 
ATOM   561   C  C     . SER   A  1  94   ? -10.782 42.116  65.661  1.00 23.11 ? 92   SER   A C     1 
ATOM   562   O  O     . SER   A  1  94   ? -9.675  42.370  66.146  1.00 25.84 ? 92   SER   A O     1 
ATOM   563   C  CB    . SER   A  1  94   ? -9.707  40.174  64.477  1.00 26.96 ? 92   SER   A CB    1 
ATOM   564   O  OG    . SER   A  1  94   ? -9.923  39.136  63.539  1.00 29.08 ? 92   SER   A OG    1 
ATOM   565   N  N     . LEU   A  1  95   ? -11.838 42.897  65.843  1.00 22.22 ? 93   LEU   A N     1 
ATOM   566   C  CA    . LEU   A  1  95   ? -11.736 44.135  66.593  1.00 23.47 ? 93   LEU   A CA    1 
ATOM   567   C  C     . LEU   A  1  95   ? -11.748 43.850  68.081  1.00 22.22 ? 93   LEU   A C     1 
ATOM   568   O  O     . LEU   A  1  95   ? -12.488 42.989  68.561  1.00 22.67 ? 93   LEU   A O     1 
ATOM   569   C  CB    . LEU   A  1  95   ? -12.921 45.043  66.274  1.00 19.78 ? 93   LEU   A CB    1 
ATOM   570   C  CG    . LEU   A  1  95   ? -13.085 45.474  64.820  1.00 21.97 ? 93   LEU   A CG    1 
ATOM   571   C  CD1   . LEU   A  1  95   ? -14.225 46.494  64.719  1.00 22.91 ? 93   LEU   A CD1   1 
ATOM   572   C  CD2   . LEU   A  1  95   ? -11.773 46.022  64.260  1.00 22.34 ? 93   LEU   A CD2   1 
ATOM   573   N  N     . SER   A  1  96   ? -10.931 44.589  68.815  1.00 19.86 ? 94   SER   A N     1 
ATOM   574   C  CA    . SER   A  1  96   ? -11.111 44.627  70.249  1.00 19.87 ? 94   SER   A CA    1 
ATOM   575   C  C     . SER   A  1  96   ? -12.368 45.436  70.563  1.00 19.72 ? 94   SER   A C     1 
ATOM   576   O  O     . SER   A  1  96   ? -12.929 46.113  69.700  1.00 19.55 ? 94   SER   A O     1 
ATOM   577   C  CB    . SER   A  1  96   ? -9.905  45.292  70.899  1.00 19.27 ? 94   SER   A CB    1 
ATOM   578   O  OG    . SER   A  1  96   ? -9.866  46.671  70.570  1.00 19.12 ? 94   SER   A OG    1 
ATOM   579   N  N     . SER   A  1  97   ? -12.809 45.374  71.817  1.00 20.10 ? 95   SER   A N     1 
ATOM   580   C  CA    . SER   A  1  97   ? -13.958 46.181  72.217  1.00 20.27 ? 95   SER   A CA    1 
ATOM   581   C  C     . SER   A  1  97   ? -13.691 47.662  71.995  1.00 18.93 ? 95   SER   A C     1 
ATOM   582   O  O     . SER   A  1  97   ? -14.530 48.383  71.447  1.00 18.15 ? 95   SER   A O     1 
ATOM   583   C  CB    . SER   A  1  97   ? -14.303 45.923  73.684  1.00 23.99 ? 95   SER   A CB    1 
ATOM   584   O  OG    . SER   A  1  97   ? -14.891 44.646  73.826  1.00 30.28 ? 95   SER   A OG    1 
ATOM   585   N  N     . GLN   A  1  98   ? -12.520 48.140  72.406  1.00 16.72 ? 96   GLN   A N     1 
ATOM   586   C  CA    . GLN   A  1  98   ? -12.230 49.551  72.204  1.00 16.06 ? 96   GLN   A CA    1 
ATOM   587   C  C     . GLN   A  1  98   ? -12.179 49.897  70.722  1.00 15.52 ? 96   GLN   A C     1 
ATOM   588   O  O     . GLN   A  1  98   ? -12.589 50.992  70.329  1.00 15.93 ? 96   GLN   A O     1 
ATOM   589   C  CB    . GLN   A  1  98   ? -10.925 49.940  72.895  1.00 15.74 ? 96   GLN   A CB    1 
ATOM   590   C  CG    . GLN   A  1  98   ? -11.060 49.997  74.410  1.00 18.56 ? 96   GLN   A CG    1 
ATOM   591   C  CD    . GLN   A  1  98   ? -12.004 51.093  74.862  1.00 17.08 ? 96   GLN   A CD    1 
ATOM   592   O  OE1   . GLN   A  1  98   ? -13.226 50.913  74.882  1.00 19.76 ? 96   GLN   A OE1   1 
ATOM   593   N  NE2   . GLN   A  1  98   ? -11.447 52.248  75.216  1.00 18.95 ? 96   GLN   A NE2   1 
ATOM   594   N  N     . GLU   A  1  99   ? -11.662 48.989  69.886  1.00 16.30 ? 97   GLU   A N     1 
ATOM   595   C  CA    . GLU   A  1  99   ? -11.678 49.252  68.453  1.00 15.69 ? 97   GLU   A CA    1 
ATOM   596   C  C     . GLU   A  1  99   ? -13.101 49.326  67.927  1.00 16.84 ? 97   GLU   A C     1 
ATOM   597   O  O     . GLU   A  1  99   ? -13.425 50.205  67.125  1.00 17.50 ? 97   GLU   A O     1 
ATOM   598   C  CB    . GLU   A  1  99   ? -10.894 48.178  67.728  1.00 15.66 ? 97   GLU   A CB    1 
ATOM   599   C  CG    . GLU   A  1  99   ? -9.405  48.355  67.960  1.00 16.65 ? 97   GLU   A CG    1 
ATOM   600   C  CD    . GLU   A  1  99   ? -8.606  47.173  67.486  1.00 17.84 ? 97   GLU   A CD    1 
ATOM   601   O  OE1   . GLU   A  1  99   ? -9.202  46.154  67.076  1.00 19.32 ? 97   GLU   A OE1   1 
ATOM   602   O  OE2   . GLU   A  1  99   ? -7.358  47.253  67.540  1.00 18.68 ? 97   GLU   A OE2   1 
ATOM   603   N  N     . GLY   A  1  100  ? -13.969 48.424  68.382  1.00 15.98 ? 98   GLY   A N     1 
ATOM   604   C  CA    . GLY   A  1  100  ? -15.358 48.497  67.970  1.00 16.52 ? 98   GLY   A CA    1 
ATOM   605   C  C     . GLY   A  1  100  ? -15.994 49.818  68.346  1.00 17.60 ? 98   GLY   A C     1 
ATOM   606   O  O     . GLY   A  1  100  ? -16.680 50.445  67.533  1.00 16.98 ? 98   GLY   A O     1 
ATOM   607   N  N     . VAL   A  1  101  ? -15.788 50.252  69.594  1.00 15.76 ? 99   VAL   A N     1 
ATOM   608   C  CA    . VAL   A  1  101  ? -16.350 51.522  70.038  1.00 15.43 ? 99   VAL   A CA    1 
ATOM   609   C  C     . VAL   A  1  101  ? -15.780 52.664  69.218  1.00 16.17 ? 99   VAL   A C     1 
ATOM   610   O  O     . VAL   A  1  101  ? -16.522 53.523  68.721  1.00 16.18 ? 99   VAL   A O     1 
ATOM   611   C  CB    . VAL   A  1  101  ? -16.102 51.727  71.539  1.00 14.78 ? 99   VAL   A CB    1 
ATOM   612   C  CG1   . VAL   A  1  101  ? -16.519 53.137  71.952  1.00 16.44 ? 99   VAL   A CG1   1 
ATOM   613   C  CG2   . VAL   A  1  101  ? -16.854 50.661  72.350  1.00 17.76 ? 99   VAL   A CG2   1 
ATOM   614   N  N     . ALA   A  1  102  ? -14.450 52.691  69.059  1.00 15.55 ? 100  ALA   A N     1 
ATOM   615   C  CA    . ALA   A  1  102  ? -13.817 53.776  68.316  1.00 15.36 ? 100  ALA   A CA    1 
ATOM   616   C  C     . ALA   A  1  102  ? -14.315 53.818  66.882  1.00 16.36 ? 100  ALA   A C     1 
ATOM   617   O  O     . ALA   A  1  102  ? -14.543 54.897  66.328  1.00 17.73 ? 100  ALA   A O     1 
ATOM   618   C  CB    . ALA   A  1  102  ? -12.293 53.617  68.347  1.00 16.48 ? 100  ALA   A CB    1 
ATOM   619   N  N     . LEU   A  1  103  ? -14.463 52.652  66.265  1.00 15.21 ? 101  LEU   A N     1 
ATOM   620   C  CA    . LEU   A  1  103  ? -14.980 52.591  64.903  1.00 15.60 ? 101  LEU   A CA    1 
ATOM   621   C  C     . LEU   A  1  103  ? -16.378 53.182  64.819  1.00 17.75 ? 101  LEU   A C     1 
ATOM   622   O  O     . LEU   A  1  103  ? -16.686 53.924  63.880  1.00 18.94 ? 101  LEU   A O     1 
ATOM   623   C  CB    . LEU   A  1  103  ? -14.995 51.145  64.422  1.00 17.14 ? 101  LEU   A CB    1 
ATOM   624   C  CG    . LEU   A  1  103  ? -15.616 50.954  63.041  1.00 17.23 ? 101  LEU   A CG    1 
ATOM   625   C  CD1   . LEU   A  1  103  ? -14.825 51.719  61.987  1.00 20.49 ? 101  LEU   A CD1   1 
ATOM   626   C  CD2   . LEU   A  1  103  ? -15.694 49.487  62.717  1.00 20.15 ? 101  LEU   A CD2   1 
ATOM   627   N  N     . MET   A  1  104  ? -17.246 52.853  65.774  1.00 16.47 ? 102  MET   A N     1 
ATOM   628   C  CA    . MET   A  1  104  ? -18.593 53.402  65.712  1.00 15.93 ? 102  MET   A CA    1 
ATOM   629   C  C     . MET   A  1  104  ? -18.590 54.905  65.935  1.00 17.19 ? 102  MET   A C     1 
ATOM   630   O  O     . MET   A  1  104  ? -19.405 55.613  65.328  1.00 19.32 ? 102  MET   A O     1 
ATOM   631   C  CB    . MET   A  1  104  ? -19.505 52.675  66.696  1.00 18.45 ? 102  MET   A CB    1 
ATOM   632   C  CG    . MET   A  1  104  ? -19.645 51.194  66.375  1.00 19.79 ? 102  MET   A CG    1 
ATOM   633   S  SD    . MET   A  1  104  ? -20.085 50.841  64.639  1.00 27.05 ? 102  MET   A SD    1 
ATOM   634   C  CE    . MET   A  1  104  ? -21.784 51.397  64.596  1.00 26.98 ? 102  MET   A CE    1 
ATOM   635   N  N     . CYS   A  1  105  ? -17.687 55.412  66.782  1.00 16.57 ? 103  CYS   A N     1 
ATOM   636   C  CA    . CYS   A  1  105  ? -17.587 56.856  66.950  1.00 17.70 ? 103  CYS   A CA    1 
ATOM   637   C  C     . CYS   A  1  105  ? -17.122 57.511  65.664  1.00 20.63 ? 103  CYS   A C     1 
ATOM   638   O  O     . CYS   A  1  105  ? -17.620 58.577  65.287  1.00 21.94 ? 103  CYS   A O     1 
ATOM   639   C  CB    . CYS   A  1  105  ? -16.609 57.193  68.064  1.00 18.47 ? 103  CYS   A CB    1 
ATOM   640   S  SG    . CYS   A  1  105  ? -17.151 56.670  69.676  1.00 19.10 ? 103  CYS   A SG    1 
ATOM   641   N  N     . LEU   A  1  106  ? -16.139 56.907  64.994  1.00 18.10 ? 104  LEU   A N     1 
ATOM   642   C  CA    . LEU   A  1  106  ? -15.708 57.428  63.708  1.00 20.24 ? 104  LEU   A CA    1 
ATOM   643   C  C     . LEU   A  1  106  ? -16.859 57.411  62.717  1.00 21.79 ? 104  LEU   A C     1 
ATOM   644   O  O     . LEU   A  1  106  ? -17.076 58.380  61.981  1.00 21.82 ? 104  LEU   A O     1 
ATOM   645   C  CB    . LEU   A  1  106  ? -14.554 56.586  63.172  1.00 19.18 ? 104  LEU   A CB    1 
ATOM   646   C  CG    . LEU   A  1  106  ? -14.245 56.912  61.711  1.00 21.06 ? 104  LEU   A CG    1 
ATOM   647   C  CD1   . LEU   A  1  106  ? -13.714 58.338  61.623  1.00 23.78 ? 104  LEU   A CD1   1 
ATOM   648   C  CD2   . LEU   A  1  106  ? -13.250 55.915  61.161  1.00 22.51 ? 104  LEU   A CD2   1 
ATOM   649   N  N     . ALA   A  1  107  ? -17.594 56.301  62.664  1.00 19.05 ? 105  ALA   A N     1 
ATOM   650   C  CA    . ALA   A  1  107  ? -18.716 56.221  61.743  1.00 20.60 ? 105  ALA   A CA    1 
ATOM   651   C  C     . ALA   A  1  107  ? -19.736 57.305  62.056  1.00 24.11 ? 105  ALA   A C     1 
ATOM   652   O  O     . ALA   A  1  107  ? -20.226 57.985  61.148  1.00 22.33 ? 105  ALA   A O     1 
ATOM   653   C  CB    . ALA   A  1  107  ? -19.338 54.828  61.799  1.00 18.94 ? 105  ALA   A CB    1 
ATOM   654   N  N     . GLU   A  1  108  ? -20.050 57.495  63.343  1.00 21.01 ? 106  GLU   A N     1 
ATOM   655   C  CA    . GLU   A  1  108  ? -20.958 58.565  63.747  1.00 23.13 ? 106  GLU   A CA    1 
ATOM   656   C  C     . GLU   A  1  108  ? -20.479 59.918  63.225  1.00 26.06 ? 106  GLU   A C     1 
ATOM   657   O  O     . GLU   A  1  108  ? -21.258 60.695  62.659  1.00 26.76 ? 106  GLU   A O     1 
ATOM   658   C  CB    . GLU   A  1  108  ? -21.063 58.583  65.275  1.00 22.19 ? 106  GLU   A CB    1 
ATOM   659   C  CG    . GLU   A  1  108  ? -21.930 59.707  65.827  1.00 24.41 ? 106  GLU   A CG    1 
ATOM   660   C  CD    . GLU   A  1  108  ? -21.654 60.001  67.288  1.00 24.66 ? 106  GLU   A CD    1 
ATOM   661   O  OE1   . GLU   A  1  108  ? -21.185 59.096  68.013  1.00 26.36 ? 106  GLU   A OE1   1 
ATOM   662   O  OE2   . GLU   A  1  108  ? -21.900 61.151  67.713  1.00 26.76 ? 106  GLU   A OE2   1 
ATOM   663   N  N     . ALA   A  1  109  ? -19.188 60.205  63.384  1.00 23.53 ? 107  ALA   A N     1 
ATOM   664   C  CA    . ALA   A  1  109  ? -18.656 61.487  62.936  1.00 24.48 ? 107  ALA   A CA    1 
ATOM   665   C  C     . ALA   A  1  109  ? -18.718 61.610  61.423  1.00 27.99 ? 107  ALA   A C     1 
ATOM   666   O  O     . ALA   A  1  109  ? -19.033 62.681  60.892  1.00 29.87 ? 107  ALA   A O     1 
ATOM   667   C  CB    . ALA   A  1  109  ? -17.216 61.643  63.413  1.00 28.47 ? 107  ALA   A CB    1 
ATOM   668   N  N     . LEU   A  1  110  ? -18.398 60.528  60.714  1.00 25.10 ? 108  LEU   A N     1 
ATOM   669   C  CA    . LEU   A  1  110  ? -18.463 60.545  59.261  1.00 22.93 ? 108  LEU   A CA    1 
ATOM   670   C  C     . LEU   A  1  110  ? -19.882 60.775  58.774  1.00 29.52 ? 108  LEU   A C     1 
ATOM   671   O  O     . LEU   A  1  110  ? -20.086 61.388  57.719  1.00 30.58 ? 108  LEU   A O     1 
ATOM   672   C  CB    . LEU   A  1  110  ? -17.913 59.233  58.699  1.00 24.38 ? 108  LEU   A CB    1 
ATOM   673   C  CG    . LEU   A  1  110  ? -16.394 59.127  58.776  1.00 25.87 ? 108  LEU   A CG    1 
ATOM   674   C  CD1   . LEU   A  1  110  ? -15.943 57.715  58.469  1.00 23.81 ? 108  LEU   A CD1   1 
ATOM   675   C  CD2   . LEU   A  1  110  ? -15.769 60.110  57.785  1.00 27.62 ? 108  LEU   A CD2   1 
ATOM   676   N  N     . LEU   A  1  111  ? -20.872 60.295  59.525  1.00 26.83 ? 109  LEU   A N     1 
ATOM   677   C  CA    . LEU   A  1  111  ? -22.266 60.495  59.155  1.00 30.05 ? 109  LEU   A CA    1 
ATOM   678   C  C     . LEU   A  1  111  ? -22.751 61.909  59.433  1.00 35.19 ? 109  LEU   A C     1 
ATOM   679   O  O     . LEU   A  1  111  ? -23.830 62.279  58.958  1.00 37.60 ? 109  LEU   A O     1 
ATOM   680   C  CB    . LEU   A  1  111  ? -23.146 59.459  59.855  1.00 29.20 ? 109  LEU   A CB    1 
ATOM   681   C  CG    . LEU   A  1  111  ? -22.944 58.040  59.312  1.00 27.09 ? 109  LEU   A CG    1 
ATOM   682   C  CD1   . LEU   A  1  111  ? -23.610 57.018  60.203  1.00 30.17 ? 109  LEU   A CD1   1 
ATOM   683   C  CD2   . LEU   A  1  111  ? -23.436 57.924  57.877  1.00 29.88 ? 109  LEU   A CD2   1 
ATOM   684   N  N     . ARG   A  1  112  ? -21.982 62.705  60.178  1.00 32.43 ? 110  ARG   A N     1 
ATOM   685   C  CA    . ARG   A  1  112  ? -22.290 64.124  60.309  1.00 36.90 ? 110  ARG   A CA    1 
ATOM   686   C  C     . ARG   A  1  112  ? -21.922 64.902  59.052  1.00 42.40 ? 110  ARG   A C     1 
ATOM   687   O  O     . ARG   A  1  112  ? -22.377 66.038  58.885  1.00 46.05 ? 110  ARG   A O     1 
ATOM   688   C  CB    . ARG   A  1  112  ? -21.596 64.709  61.539  1.00 36.28 ? 110  ARG   A CB    1 
ATOM   689   C  CG    . ARG   A  1  112  ? -22.066 64.112  62.863  1.00 35.12 ? 110  ARG   A CG    1 
ATOM   690   C  CD    . ARG   A  1  112  ? -21.062 64.359  63.982  1.00 36.30 ? 110  ARG   A CD    1 
ATOM   691   N  NE    . ARG   A  1  112  ? -20.919 65.773  64.305  1.00 44.64 ? 110  ARG   A NE    1 
ATOM   692   C  CZ    . ARG   A  1  112  ? -21.602 66.402  65.253  1.00 51.31 ? 110  ARG   A CZ    1 
ATOM   693   N  NH1   . ARG   A  1  112  ? -22.496 65.770  65.999  1.00 51.34 ? 110  ARG   A NH1   1 
ATOM   694   N  NH2   . ARG   A  1  112  ? -21.383 67.698  65.459  1.00 56.13 ? 110  ARG   A NH2   1 
ATOM   695   N  N     . ILE   A  1  113  ? -21.110 64.322  58.174  1.00 38.40 ? 111  ILE   A N     1 
ATOM   696   C  CA    . ILE   A  1  113  ? -20.866 64.881  56.845  1.00 39.34 ? 111  ILE   A CA    1 
ATOM   697   C  C     . ILE   A  1  113  ? -22.103 64.627  55.993  1.00 44.89 ? 111  ILE   A C     1 
ATOM   698   O  O     . ILE   A  1  113  ? -22.440 63.466  55.719  1.00 41.92 ? 111  ILE   A O     1 
ATOM   699   C  CB    . ILE   A  1  113  ? -19.611 64.272  56.205  1.00 37.62 ? 111  ILE   A CB    1 
ATOM   700   C  CG1   . ILE   A  1  113  ? -18.371 64.648  57.014  1.00 38.36 ? 111  ILE   A CG1   1 
ATOM   701   C  CG2   . ILE   A  1  113  ? -19.480 64.723  54.756  1.00 42.19 ? 111  ILE   A CG2   1 
ATOM   702   C  CD1   . ILE   A  1  113  ? -17.150 63.897  56.600  1.00 33.95 ? 111  ILE   A CD1   1 
ATOM   703   N  N     . PRO   A  1  114  ? -22.806 65.673  55.549  1.00 49.68 ? 112  PRO   A N     1 
ATOM   704   C  CA    . PRO   A  1  114  ? -24.114 65.445  54.911  1.00 49.25 ? 112  PRO   A CA    1 
ATOM   705   C  C     . PRO   A  1  114  ? -24.042 64.800  53.535  1.00 49.89 ? 112  PRO   A C     1 
ATOM   706   O  O     . PRO   A  1  114  ? -24.867 63.931  53.228  1.00 53.24 ? 112  PRO   A O     1 
ATOM   707   C  CB    . PRO   A  1  114  ? -24.740 66.848  54.871  1.00 52.21 ? 112  PRO   A CB    1 
ATOM   708   C  CG    . PRO   A  1  114  ? -23.957 67.653  55.877  1.00 53.56 ? 112  PRO   A CG    1 
ATOM   709   C  CD    . PRO   A  1  114  ? -22.566 67.099  55.820  1.00 51.25 ? 112  PRO   A CD    1 
ATOM   710   N  N     . ASP   A  1  115  ? -23.092 65.196  52.693  1.00 48.25 ? 113  ASP   A N     1 
ATOM   711   C  CA    . ASP   A  1  115  ? -23.034 64.706  51.321  1.00 50.03 ? 113  ASP   A CA    1 
ATOM   712   C  C     . ASP   A  1  115  ? -22.282 63.383  51.252  1.00 47.97 ? 113  ASP   A C     1 
ATOM   713   O  O     . ASP   A  1  115  ? -21.137 63.287  51.705  1.00 48.27 ? 113  ASP   A O     1 
ATOM   714   C  CB    . ASP   A  1  115  ? -22.369 65.730  50.404  1.00 48.76 ? 113  ASP   A CB    1 
ATOM   715   C  CG    . ASP   A  1  115  ? -22.108 65.178  49.019  1.00 54.81 ? 113  ASP   A CG    1 
ATOM   716   O  OD1   . ASP   A  1  115  ? -23.083 64.769  48.346  1.00 55.69 ? 113  ASP   A OD1   1 
ATOM   717   O  OD2   . ASP   A  1  115  ? -20.930 65.145  48.607  1.00 52.82 ? 113  ASP   A OD2   1 
ATOM   718   N  N     . THR   A  1  116  ? -22.921 62.376  50.649  1.00 47.76 ? 114  THR   A N     1 
ATOM   719   C  CA    . THR   A  1  116  ? -22.354 61.031  50.613  1.00 44.28 ? 114  THR   A CA    1 
ATOM   720   C  C     . THR   A  1  116  ? -21.059 60.980  49.806  1.00 47.99 ? 114  THR   A C     1 
ATOM   721   O  O     . THR   A  1  116  ? -20.110 60.286  50.191  1.00 45.02 ? 114  THR   A O     1 
ATOM   722   C  CB    . THR   A  1  116  ? -23.387 60.052  50.056  1.00 44.67 ? 114  THR   A CB    1 
ATOM   723   O  OG1   . THR   A  1  116  ? -24.569 60.098  50.862  1.00 49.81 ? 114  THR   A OG1   1 
ATOM   724   C  CG2   . THR   A  1  116  ? -22.839 58.634  50.047  1.00 46.18 ? 114  THR   A CG2   1 
ATOM   725   N  N     . ALA   A  1  117  ? -20.998 61.699  48.683  1.00 44.18 ? 115  ALA   A N     1 
ATOM   726   C  CA    . ALA   A  1  117  ? -19.773 61.700  47.889  1.00 46.90 ? 115  ALA   A CA    1 
ATOM   727   C  C     . ALA   A  1  117  ? -18.621 62.348  48.648  1.00 43.58 ? 115  ALA   A C     1 
ATOM   728   O  O     . ALA   A  1  117  ? -17.487 61.859  48.601  1.00 43.49 ? 115  ALA   A O     1 
ATOM   729   C  CB    . ALA   A  1  117  ? -20.008 62.393  46.546  1.00 48.20 ? 115  ALA   A CB    1 
ATOM   730   N  N     . THR   A  1  118  ? -18.891 63.451  49.352  1.00 43.82 ? 116  THR   A N     1 
ATOM   731   C  CA    . THR   A  1  118  ? -17.847 64.093  50.144  1.00 44.41 ? 116  THR   A CA    1 
ATOM   732   C  C     . THR   A  1  118  ? -17.359 63.165  51.247  1.00 39.63 ? 116  THR   A C     1 
ATOM   733   O  O     . THR   A  1  118  ? -16.155 63.080  51.515  1.00 39.21 ? 116  THR   A O     1 
ATOM   734   C  CB    . THR   A  1  118  ? -18.381 65.390  50.751  1.00 43.43 ? 116  THR   A CB    1 
ATOM   735   O  OG1   . THR   A  1  118  ? -18.878 66.237  49.708  1.00 52.51 ? 116  THR   A OG1   1 
ATOM   736   C  CG2   . THR   A  1  118  ? -17.282 66.118  51.510  1.00 43.92 ? 116  THR   A CG2   1 
ATOM   737   N  N     . ARG   A  1  119  ? -18.285 62.457  51.893  1.00 39.66 ? 117  ARG   A N     1 
ATOM   738   C  CA    . ARG   A  1  119  ? -17.911 61.524  52.949  1.00 39.41 ? 117  ARG   A CA    1 
ATOM   739   C  C     . ARG   A  1  119  ? -17.057 60.392  52.394  1.00 37.14 ? 117  ARG   A C     1 
ATOM   740   O  O     . ARG   A  1  119  ? -16.006 60.057  52.953  1.00 37.54 ? 117  ARG   A O     1 
ATOM   741   C  CB    . ARG   A  1  119  ? -19.177 60.968  53.598  1.00 35.29 ? 117  ARG   A CB    1 
ATOM   742   C  CG    . ARG   A  1  119  ? -18.923 60.072  54.797  1.00 32.40 ? 117  ARG   A CG    1 
ATOM   743   C  CD    . ARG   A  1  119  ? -20.197 59.355  55.209  1.00 34.77 ? 117  ARG   A CD    1 
ATOM   744   N  NE    . ARG   A  1  119  ? -21.313 60.279  55.378  1.00 35.43 ? 117  ARG   A NE    1 
ATOM   745   C  CZ    . ARG   A  1  119  ? -22.511 60.119  54.831  1.00 38.17 ? 117  ARG   A CZ    1 
ATOM   746   N  NH1   . ARG   A  1  119  ? -22.808 59.046  54.118  1.00 36.30 ? 117  ARG   A NH1   1 
ATOM   747   N  NH2   . ARG   A  1  119  ? -23.437 61.058  55.011  1.00 44.43 ? 117  ARG   A NH2   1 
ATOM   748   N  N     . ASP   A  1  120  ? -17.499 59.791  51.285  1.00 38.55 ? 118  ASP   A N     1 
ATOM   749   C  CA    . ASP   A  1  120  ? -16.765 58.673  50.704  1.00 39.30 ? 118  ASP   A CA    1 
ATOM   750   C  C     . ASP   A  1  120  ? -15.384 59.107  50.239  1.00 40.35 ? 118  ASP   A C     1 
ATOM   751   O  O     . ASP   A  1  120  ? -14.417 58.346  50.356  1.00 37.89 ? 118  ASP   A O     1 
ATOM   752   C  CB    . ASP   A  1  120  ? -17.561 58.058  49.554  1.00 38.32 ? 118  ASP   A CB    1 
ATOM   753   C  CG    . ASP   A  1  120  ? -18.888 57.494  50.010  1.00 43.29 ? 118  ASP   A CG    1 
ATOM   754   O  OD1   . ASP   A  1  120  ? -19.135 57.483  51.233  1.00 44.54 ? 118  ASP   A OD1   1 
ATOM   755   O  OD2   . ASP   A  1  120  ? -19.688 57.066  49.151  1.00 46.04 ? 118  ASP   A OD2   1 
ATOM   756   N  N     . ALA   A  1  121  ? -15.272 60.331  49.715  1.00 41.74 ? 119  ALA   A N     1 
ATOM   757   C  CA    . ALA   A  1  121  ? -13.970 60.844  49.306  1.00 39.97 ? 119  ALA   A CA    1 
ATOM   758   C  C     . ALA   A  1  121  ? -13.054 61.039  50.505  1.00 40.24 ? 119  ALA   A C     1 
ATOM   759   O  O     . ALA   A  1  121  ? -11.874 60.673  50.460  1.00 41.14 ? 119  ALA   A O     1 
ATOM   760   C  CB    . ALA   A  1  121  ? -14.139 62.158  48.542  1.00 41.89 ? 119  ALA   A CB    1 
ATOM   761   N  N     . LEU   A  1  122  ? -13.584 61.610  51.590  1.00 39.31 ? 120  LEU   A N     1 
ATOM   762   C  CA    . LEU   A  1  122  ? -12.790 61.761  52.803  1.00 37.22 ? 120  LEU   A CA    1 
ATOM   763   C  C     . LEU   A  1  122  ? -12.337 60.405  53.329  1.00 38.08 ? 120  LEU   A C     1 
ATOM   764   O  O     . LEU   A  1  122  ? -11.191 60.253  53.770  1.00 36.96 ? 120  LEU   A O     1 
ATOM   765   C  CB    . LEU   A  1  122  ? -13.594 62.505  53.866  1.00 40.35 ? 120  LEU   A CB    1 
ATOM   766   C  CG    . LEU   A  1  122  ? -12.784 62.948  55.085  1.00 38.26 ? 120  LEU   A CG    1 
ATOM   767   C  CD1   . LEU   A  1  122  ? -11.728 63.963  54.678  1.00 46.00 ? 120  LEU   A CD1   1 
ATOM   768   C  CD2   . LEU   A  1  122  ? -13.690 63.510  56.161  1.00 34.85 ? 120  LEU   A CD2   1 
ATOM   769   N  N     . ILE   A  1  123  ? -13.222 59.406  53.281  1.00 36.98 ? 121  ILE   A N     1 
ATOM   770   C  CA    . ILE   A  1  123  ? -12.862 58.065  53.736  1.00 37.93 ? 121  ILE   A CA    1 
ATOM   771   C  C     . ILE   A  1  123  ? -11.740 57.503  52.878  1.00 37.52 ? 121  ILE   A C     1 
ATOM   772   O  O     . ILE   A  1  123  ? -10.686 57.099  53.382  1.00 36.00 ? 121  ILE   A O     1 
ATOM   773   C  CB    . ILE   A  1  123  ? -14.090 57.140  53.722  1.00 33.84 ? 121  ILE   A CB    1 
ATOM   774   C  CG1   . ILE   A  1  123  ? -15.109 57.562  54.784  1.00 32.96 ? 121  ILE   A CG1   1 
ATOM   775   C  CG2   . ILE   A  1  123  ? -13.662 55.684  53.900  1.00 33.59 ? 121  ILE   A CG2   1 
ATOM   776   C  CD1   . ILE   A  1  123  ? -16.408 56.805  54.683  1.00 31.26 ? 121  ILE   A CD1   1 
ATOM   777   N  N     . ARG   A  1  124  ? -11.951 57.484  51.559  1.00 38.17 ? 122  ARG   A N     1 
ATOM   778   C  CA    . ARG   A  1  124  ? -11.009 56.828  50.657  1.00 39.02 ? 122  ARG   A CA    1 
ATOM   779   C  C     . ARG   A  1  124  ? -9.668  57.545  50.622  1.00 44.40 ? 122  ARG   A C     1 
ATOM   780   O  O     . ARG   A  1  124  ? -8.613  56.898  50.635  1.00 45.59 ? 122  ARG   A O     1 
ATOM   781   C  CB    . ARG   A  1  124  ? -11.601 56.753  49.250  1.00 39.31 ? 122  ARG   A CB    1 
ATOM   782   N  N     . ASP   A  1  125  ? -9.682  58.876  50.587  1.00 43.15 ? 123  ASP   A N     1 
ATOM   783   C  CA    . ASP   A  1  125  ? -8.460  59.627  50.331  1.00 48.15 ? 123  ASP   A CA    1 
ATOM   784   C  C     . ASP   A  1  125  ? -7.732  60.040  51.604  1.00 50.52 ? 123  ASP   A C     1 
ATOM   785   O  O     . ASP   A  1  125  ? -6.497  60.044  51.633  1.00 54.49 ? 123  ASP   A O     1 
ATOM   786   C  CB    . ASP   A  1  125  ? -8.769  60.859  49.472  1.00 55.36 ? 123  ASP   A CB    1 
ATOM   787   C  CG    . ASP   A  1  125  ? -9.457  60.504  48.161  1.00 55.79 ? 123  ASP   A CG    1 
ATOM   788   O  OD1   . ASP   A  1  125  ? -9.061  59.503  47.524  1.00 54.95 ? 123  ASP   A OD1   1 
ATOM   789   O  OD2   . ASP   A  1  125  ? -10.399 61.227  47.768  1.00 54.79 ? 123  ASP   A OD2   1 
ATOM   790   N  N     . LYS   A  1  126  ? -8.464  60.383  52.661  1.00 45.74 ? 124  LYS   A N     1 
ATOM   791   C  CA    . LYS   A  1  126  ? -7.871  60.961  53.860  1.00 44.70 ? 124  LYS   A CA    1 
ATOM   792   C  C     . LYS   A  1  126  ? -7.944  60.054  55.081  1.00 45.86 ? 124  LYS   A C     1 
ATOM   793   O  O     . LYS   A  1  126  ? -6.916  59.794  55.715  1.00 49.96 ? 124  LYS   A O     1 
ATOM   794   C  CB    . LYS   A  1  126  ? -8.523  62.318  54.168  1.00 48.68 ? 124  LYS   A CB    1 
ATOM   795   N  N     . ILE   A  1  127  ? -9.136  59.568  55.438  1.00 41.95 ? 125  ILE   A N     1 
ATOM   796   C  CA    . ILE   A  1  127  ? -9.280  58.770  56.657  1.00 39.68 ? 125  ILE   A CA    1 
ATOM   797   C  C     . ILE   A  1  127  ? -8.514  57.459  56.536  1.00 42.69 ? 125  ILE   A C     1 
ATOM   798   O  O     . ILE   A  1  127  ? -7.704  57.112  57.404  1.00 43.73 ? 125  ILE   A O     1 
ATOM   799   C  CB    . ILE   A  1  127  ? -10.764 58.527  56.983  1.00 36.47 ? 125  ILE   A CB    1 
ATOM   800   C  CG1   . ILE   A  1  127  ? -11.542 59.844  57.021  1.00 41.33 ? 125  ILE   A CG1   1 
ATOM   801   C  CG2   . ILE   A  1  127  ? -10.891 57.806  58.322  1.00 36.22 ? 125  ILE   A CG2   1 
ATOM   802   C  CD1   . ILE   A  1  127  ? -11.008 60.833  58.022  1.00 41.59 ? 125  ILE   A CD1   1 
ATOM   803   N  N     . ALA   A  1  128  ? -8.761  56.709  55.459  1.00 39.49 ? 126  ALA   A N     1 
ATOM   804   C  CA    . ALA   A  1  128  ? -8.207  55.363  55.358  1.00 37.37 ? 126  ALA   A CA    1 
ATOM   805   C  C     . ALA   A  1  128  ? -6.691  55.388  55.242  1.00 43.83 ? 126  ALA   A C     1 
ATOM   806   O  O     . ALA   A  1  128  ? -6.015  54.487  55.750  1.00 41.50 ? 126  ALA   A O     1 
ATOM   807   C  CB    . ALA   A  1  128  ? -8.817  54.624  54.170  1.00 38.09 ? 126  ALA   A CB    1 
ATOM   808   N  N     . ASP   A  1  129  ? -6.143  56.406  54.580  1.00 57.99 ? 127  ASP   A N     1 
ATOM   809   C  CA    . ASP   A  1  129  ? -4.716  56.475  54.286  1.00 59.89 ? 127  ASP   A CA    1 
ATOM   810   C  C     . ASP   A  1  129  ? -3.888  57.032  55.439  1.00 60.19 ? 127  ASP   A C     1 
ATOM   811   O  O     . ASP   A  1  129  ? -2.690  57.275  55.254  1.00 65.86 ? 127  ASP   A O     1 
ATOM   812   C  CB    . ASP   A  1  129  ? -4.469  57.282  53.008  1.00 59.06 ? 127  ASP   A CB    1 
ATOM   813   N  N     . GLY   A  1  130  ? -4.479  57.244  56.611  1.00 56.84 ? 128  GLY   A N     1 
ATOM   814   C  CA    . GLY   A  1  130  ? -3.677  57.617  57.758  1.00 59.54 ? 128  GLY   A CA    1 
ATOM   815   C  C     . GLY   A  1  130  ? -4.361  58.477  58.799  1.00 60.19 ? 128  GLY   A C     1 
ATOM   816   O  O     . GLY   A  1  130  ? -5.301  58.037  59.468  1.00 56.09 ? 128  GLY   A O     1 
ATOM   817   N  N     . ASN   A  1  131  ? -3.881  59.713  58.941  1.00 62.99 ? 129  ASN   A N     1 
ATOM   818   C  CA    . ASN   A  1  131  ? -4.284  60.589  60.033  1.00 57.94 ? 129  ASN   A CA    1 
ATOM   819   C  C     . ASN   A  1  131  ? -5.763  60.946  59.973  1.00 51.45 ? 129  ASN   A C     1 
ATOM   820   O  O     . ASN   A  1  131  ? -6.153  61.904  59.298  1.00 56.78 ? 129  ASN   A O     1 
ATOM   821   C  CB    . ASN   A  1  131  ? -3.427  61.859  60.042  1.00 57.44 ? 129  ASN   A CB    1 
ATOM   822   N  N     . TRP   A  1  132  ? -6.595  60.173  60.674  1.00 49.37 ? 130  TRP   A N     1 
ATOM   823   C  CA    . TRP   A  1  132  ? -7.992  60.556  60.842  1.00 40.97 ? 130  TRP   A CA    1 
ATOM   824   C  C     . TRP   A  1  132  ? -8.121  61.786  61.726  1.00 40.27 ? 130  TRP   A C     1 
ATOM   825   O  O     . TRP   A  1  132  ? -9.100  62.534  61.612  1.00 43.75 ? 130  TRP   A O     1 
ATOM   826   C  CB    . TRP   A  1  132  ? -8.774  59.404  61.471  1.00 37.40 ? 130  TRP   A CB    1 
ATOM   827   C  CG    . TRP   A  1  132  ? -8.201  58.953  62.787  1.00 31.94 ? 130  TRP   A CG    1 
ATOM   828   C  CD1   . TRP   A  1  132  ? -7.289  57.956  62.982  1.00 30.84 ? 130  TRP   A CD1   1 
ATOM   829   C  CD2   . TRP   A  1  132  ? -8.503  59.479  64.088  1.00 25.89 ? 130  TRP   A CD2   1 
ATOM   830   N  NE1   . TRP   A  1  132  ? -7.011  57.823  64.319  1.00 28.39 ? 130  TRP   A NE1   1 
ATOM   831   C  CE2   . TRP   A  1  132  ? -7.734  58.752  65.020  1.00 26.84 ? 130  TRP   A CE2   1 
ATOM   832   C  CE3   . TRP   A  1  132  ? -9.339  60.495  64.554  1.00 30.99 ? 130  TRP   A CE3   1 
ATOM   833   C  CZ2   . TRP   A  1  132  ? -7.784  59.002  66.387  1.00 25.40 ? 130  TRP   A CZ2   1 
ATOM   834   C  CZ3   . TRP   A  1  132  ? -9.387  60.744  65.916  1.00 28.20 ? 130  TRP   A CZ3   1 
ATOM   835   C  CH2   . TRP   A  1  132  ? -8.612  60.003  66.815  1.00 27.85 ? 130  TRP   A CH2   1 
ATOM   836   N  N     . LYS   A  1  133  ? -7.152  61.999  62.622  1.00 41.28 ? 131  LYS   A N     1 
ATOM   837   C  CA    . LYS   A  1  133  ? -7.218  63.132  63.538  1.00 45.28 ? 131  LYS   A CA    1 
ATOM   838   C  C     . LYS   A  1  133  ? -7.161  64.452  62.782  1.00 53.25 ? 131  LYS   A C     1 
ATOM   839   O  O     . LYS   A  1  133  ? -7.811  65.429  63.173  1.00 60.15 ? 131  LYS   A O     1 
ATOM   840   C  CB    . LYS   A  1  133  ? -6.078  63.042  64.552  1.00 40.42 ? 131  LYS   A CB    1 
ATOM   841   N  N     . SER   A  1  134  ? -6.399  64.494  61.685  1.00 56.04 ? 132  SER   A N     1 
ATOM   842   C  CA    . SER   A  1  134  ? -6.229  65.739  60.944  1.00 59.91 ? 132  SER   A CA    1 
ATOM   843   C  C     . SER   A  1  134  ? -7.543  66.232  60.349  1.00 62.53 ? 132  SER   A C     1 
ATOM   844   O  O     . SER   A  1  134  ? -7.764  67.445  60.254  1.00 65.59 ? 132  SER   A O     1 
ATOM   845   C  CB    . SER   A  1  134  ? -5.178  65.555  59.847  1.00 59.44 ? 132  SER   A CB    1 
ATOM   846   N  N     . HIS   A  1  135  ? -8.434  65.318  59.965  1.00 61.35 ? 133  HIS   A N     1 
ATOM   847   C  CA    . HIS   A  1  135  ? -9.631  65.682  59.218  1.00 62.18 ? 133  HIS   A CA    1 
ATOM   848   C  C     . HIS   A  1  135  ? -10.908 65.670  60.049  1.00 62.83 ? 133  HIS   A C     1 
ATOM   849   O  O     . HIS   A  1  135  ? -11.927 66.198  59.591  1.00 63.64 ? 133  HIS   A O     1 
ATOM   850   C  CB    . HIS   A  1  135  ? -9.796  64.764  58.000  1.00 60.20 ? 133  HIS   A CB    1 
ATOM   851   C  CG    . HIS   A  1  135  ? -8.557  64.640  57.169  1.00 62.26 ? 133  HIS   A CG    1 
ATOM   852   N  ND1   . HIS   A  1  135  ? -7.529  63.780  57.490  1.00 59.75 ? 133  HIS   A ND1   1 
ATOM   853   C  CD2   . HIS   A  1  135  ? -8.177  65.274  56.035  1.00 60.43 ? 133  HIS   A CD2   1 
ATOM   854   C  CE1   . HIS   A  1  135  ? -6.571  63.886  56.587  1.00 63.79 ? 133  HIS   A CE1   1 
ATOM   855   N  NE2   . HIS   A  1  135  ? -6.939  64.787  55.693  1.00 66.55 ? 133  HIS   A NE2   1 
ATOM   856   N  N     . LEU   A  1  136  ? -10.887 65.088  61.243  1.00 61.58 ? 134  LEU   A N     1 
ATOM   857   C  CA    . LEU   A  1  136  ? -12.084 65.042  62.078  1.00 61.02 ? 134  LEU   A CA    1 
ATOM   858   C  C     . LEU   A  1  136  ? -11.761 65.289  63.550  1.00 64.79 ? 134  LEU   A C     1 
ATOM   859   O  O     . LEU   A  1  136  ? -12.617 65.735  64.315  1.00 64.76 ? 134  LEU   A O     1 
ATOM   860   C  CB    . LEU   A  1  136  ? -12.808 63.702  61.910  1.00 57.22 ? 134  LEU   A CB    1 
ATOM   861   C  CG    . LEU   A  1  136  ? -13.547 63.465  60.591  1.00 54.61 ? 134  LEU   A CG    1 
ATOM   862   C  CD1   . LEU   A  1  136  ? -13.985 62.016  60.478  1.00 45.89 ? 134  LEU   A CD1   1 
ATOM   863   C  CD2   . LEU   A  1  136  ? -14.743 64.398  60.469  1.00 49.50 ? 134  LEU   A CD2   1 
ATOM   864   N  N     . SER   A  1  139  ? -12.463 70.346  67.002  1.00 41.11 ? 137  SER   A N     1 
ATOM   865   C  CA    . SER   A  1  139  ? -13.268 71.154  67.917  1.00 45.34 ? 137  SER   A CA    1 
ATOM   866   C  C     . SER   A  1  139  ? -14.121 70.279  68.839  1.00 45.17 ? 137  SER   A C     1 
ATOM   867   O  O     . SER   A  1  139  ? -14.488 70.684  69.946  1.00 44.26 ? 137  SER   A O     1 
ATOM   868   C  CB    . SER   A  1  139  ? -14.164 72.118  67.132  1.00 46.88 ? 137  SER   A CB    1 
ATOM   869   N  N     . ARG   A  1  140  ? -14.435 69.075  68.370  1.00 36.08 ? 138  ARG   A N     1 
ATOM   870   C  CA    . ARG   A  1  140  ? -15.258 68.131  69.111  1.00 34.63 ? 138  ARG   A CA    1 
ATOM   871   C  C     . ARG   A  1  140  ? -14.595 66.768  69.015  1.00 32.05 ? 138  ARG   A C     1 
ATOM   872   O  O     . ARG   A  1  140  ? -14.276 66.308  67.914  1.00 30.99 ? 138  ARG   A O     1 
ATOM   873   C  CB    . ARG   A  1  140  ? -16.667 68.084  68.505  1.00 35.77 ? 138  ARG   A CB    1 
ATOM   874   C  CG    . ARG   A  1  140  ? -17.556 66.926  68.942  1.00 36.26 ? 138  ARG   A CG    1 
ATOM   875   C  CD    . ARG   A  1  140  ? -18.759 66.843  68.007  1.00 39.64 ? 138  ARG   A CD    1 
ATOM   876   N  NE    . ARG   A  1  140  ? -19.673 65.744  68.300  1.00 42.21 ? 138  ARG   A NE    1 
ATOM   877   C  CZ    . ARG   A  1  140  ? -19.590 64.534  67.759  1.00 45.53 ? 138  ARG   A CZ    1 
ATOM   878   N  NH1   . ARG   A  1  140  ? -18.588 64.201  66.958  1.00 43.63 ? 138  ARG   A NH1   1 
ATOM   879   N  NH2   . ARG   A  1  140  ? -20.536 63.637  68.026  1.00 42.73 ? 138  ARG   A NH2   1 
ATOM   880   N  N     . SER   A  1  141  ? -14.362 66.139  70.163  1.00 29.12 ? 139  SER   A N     1 
ATOM   881   C  CA    . SER   A  1  141  ? -13.781 64.807  70.164  1.00 26.23 ? 139  SER   A CA    1 
ATOM   882   C  C     . SER   A  1  141  ? -14.660 63.860  69.360  1.00 23.60 ? 139  SER   A C     1 
ATOM   883   O  O     . SER   A  1  141  ? -15.889 63.898  69.442  1.00 23.51 ? 139  SER   A O     1 
ATOM   884   C  CB    . SER   A  1  141  ? -13.678 64.297  71.598  1.00 24.12 ? 139  SER   A CB    1 
ATOM   885   O  OG    . SER   A  1  141  ? -13.311 62.929  71.631  1.00 23.51 ? 139  SER   A OG    1 
ATOM   886   N  N     . LEU   A  1  142  ? -14.020 62.997  68.574  1.00 24.48 ? 140  LEU   A N     1 
ATOM   887   C  CA    . LEU   A  1  142  ? -14.756 61.941  67.902  1.00 21.29 ? 140  LEU   A CA    1 
ATOM   888   C  C     . LEU   A  1  142  ? -15.531 61.072  68.883  1.00 20.83 ? 140  LEU   A C     1 
ATOM   889   O  O     . LEU   A  1  142  ? -16.510 60.419  68.501  1.00 21.73 ? 140  LEU   A O     1 
ATOM   890   C  CB    . LEU   A  1  142  ? -13.746 61.068  67.162  1.00 23.69 ? 140  LEU   A CB    1 
ATOM   891   C  CG    . LEU   A  1  142  ? -14.090 60.658  65.745  1.00 28.65 ? 140  LEU   A CG    1 
ATOM   892   C  CD1   . LEU   A  1  142  ? -13.995 61.855  64.824  1.00 31.31 ? 140  LEU   A CD1   1 
ATOM   893   C  CD2   . LEU   A  1  142  ? -13.117 59.600  65.331  1.00 29.73 ? 140  LEU   A CD2   1 
ATOM   894   N  N     . PHE   A  1  143  ? -15.121 61.068  70.146  1.00 18.51 ? 141  PHE   A N     1 
ATOM   895   C  CA    . PHE   A  1  143  ? -15.545 60.062  71.100  1.00 19.01 ? 141  PHE   A CA    1 
ATOM   896   C  C     . PHE   A  1  143  ? -16.550 60.600  72.112  1.00 18.58 ? 141  PHE   A C     1 
ATOM   897   O  O     . PHE   A  1  143  ? -16.767 59.969  73.146  1.00 18.96 ? 141  PHE   A O     1 
ATOM   898   C  CB    . PHE   A  1  143  ? -14.305 59.483  71.781  1.00 18.80 ? 141  PHE   A CB    1 
ATOM   899   C  CG    . PHE   A  1  143  ? -13.283 59.008  70.799  1.00 17.62 ? 141  PHE   A CG    1 
ATOM   900   C  CD1   . PHE   A  1  143  ? -13.605 58.005  69.905  1.00 17.53 ? 141  PHE   A CD1   1 
ATOM   901   C  CD2   . PHE   A  1  143  ? -12.029 59.589  70.722  1.00 18.20 ? 141  PHE   A CD2   1 
ATOM   902   C  CE1   . PHE   A  1  143  ? -12.696 57.572  68.969  1.00 18.64 ? 141  PHE   A CE1   1 
ATOM   903   C  CE2   . PHE   A  1  143  ? -11.114 59.153  69.790  1.00 19.20 ? 141  PHE   A CE2   1 
ATOM   904   C  CZ    . PHE   A  1  143  ? -11.435 58.151  68.919  1.00 17.81 ? 141  PHE   A CZ    1 
ATOM   905   N  N     . VAL   A  1  144  ? -17.192 61.732  71.811  1.00 19.43 ? 142  VAL   A N     1 
ATOM   906   C  CA    A VAL   A  1  144  ? -18.112 62.333  72.773  0.45 20.55 ? 142  VAL   A CA    1 
ATOM   907   C  CA    B VAL   A  1  144  ? -18.141 62.348  72.744  0.55 20.54 ? 142  VAL   A CA    1 
ATOM   908   C  C     . VAL   A  1  144  ? -19.221 61.362  73.169  1.00 20.55 ? 142  VAL   A C     1 
ATOM   909   O  O     . VAL   A  1  144  ? -19.638 61.329  74.333  1.00 20.99 ? 142  VAL   A O     1 
ATOM   910   C  CB    A VAL   A  1  144  ? -18.656 63.683  72.264  0.45 21.58 ? 142  VAL   A CB    1 
ATOM   911   C  CB    B VAL   A  1  144  ? -18.752 63.617  72.122  0.55 21.58 ? 142  VAL   A CB    1 
ATOM   912   C  CG1   A VAL   A  1  144  ? -17.522 64.670  72.060  0.45 23.63 ? 142  VAL   A CG1   1 
ATOM   913   C  CG1   B VAL   A  1  144  ? -19.926 64.116  72.964  0.55 20.89 ? 142  VAL   A CG1   1 
ATOM   914   C  CG2   A VAL   A  1  144  ? -19.438 63.498  70.988  0.45 22.69 ? 142  VAL   A CG2   1 
ATOM   915   C  CG2   B VAL   A  1  144  ? -17.703 64.696  71.984  0.55 23.56 ? 142  VAL   A CG2   1 
ATOM   916   N  N     . ASN   A  1  145  ? -19.710 60.555  72.231  1.00 18.56 ? 143  ASN   A N     1 
ATOM   917   C  CA    . ASN   A  1  145  ? -20.767 59.602  72.537  1.00 19.89 ? 143  ASN   A CA    1 
ATOM   918   C  C     . ASN   A  1  145  ? -20.241 58.187  72.726  1.00 20.82 ? 143  ASN   A C     1 
ATOM   919   O  O     . ASN   A  1  145  ? -20.997 57.218  72.592  1.00 19.41 ? 143  ASN   A O     1 
ATOM   920   C  CB    . ASN   A  1  145  ? -21.842 59.647  71.453  1.00 21.89 ? 143  ASN   A CB    1 
ATOM   921   C  CG    . ASN   A  1  145  ? -22.580 60.958  71.450  1.00 22.51 ? 143  ASN   A CG    1 
ATOM   922   O  OD1   . ASN   A  1  145  ? -23.092 61.380  72.482  1.00 27.63 ? 143  ASN   A OD1   1 
ATOM   923   N  ND2   . ASN   A  1  145  ? -22.594 61.633  70.314  1.00 25.20 ? 143  ASN   A ND2   1 
ATOM   924   N  N     . ALA   A  1  146  ? -18.954 58.043  73.043  1.00 17.54 ? 144  ALA   A N     1 
ATOM   925   C  CA    . ALA   A  1  146  ? -18.398 56.702  73.141  1.00 19.15 ? 144  ALA   A CA    1 
ATOM   926   C  C     . ALA   A  1  146  ? -19.013 55.884  74.271  1.00 16.96 ? 144  ALA   A C     1 
ATOM   927   O  O     . ALA   A  1  146  ? -19.020 54.652  74.201  1.00 20.30 ? 144  ALA   A O     1 
ATOM   928   C  CB    . ALA   A  1  146  ? -16.885 56.775  73.291  1.00 18.28 ? 144  ALA   A CB    1 
ATOM   929   N  N     . ALA   A  1  147  ? -19.542 56.528  75.317  1.00 19.84 ? 145  ALA   A N     1 
ATOM   930   C  CA    . ALA   A  1  147  ? -20.207 55.748  76.357  1.00 22.78 ? 145  ALA   A CA    1 
ATOM   931   C  C     . ALA   A  1  147  ? -21.416 55.024  75.790  1.00 20.58 ? 145  ALA   A C     1 
ATOM   932   O  O     . ALA   A  1  147  ? -21.684 53.867  76.138  1.00 22.42 ? 145  ALA   A O     1 
ATOM   933   C  CB    . ALA   A  1  147  ? -20.605 56.638  77.535  1.00 26.32 ? 145  ALA   A CB    1 
ATOM   934   N  N     . THR   A  1  148  ? -22.142 55.681  74.888  1.00 19.84 ? 146  THR   A N     1 
ATOM   935   C  CA    . THR   A  1  148  ? -23.279 55.044  74.242  1.00 20.34 ? 146  THR   A CA    1 
ATOM   936   C  C     . THR   A  1  148  ? -22.818 53.914  73.341  1.00 19.24 ? 146  THR   A C     1 
ATOM   937   O  O     . THR   A  1  148  ? -23.326 52.789  73.422  1.00 20.70 ? 146  THR   A O     1 
ATOM   938   C  CB    . THR   A  1  148  ? -24.041 56.094  73.442  1.00 24.31 ? 146  THR   A CB    1 
ATOM   939   O  OG1   . THR   A  1  148  ? -24.446 57.139  74.330  1.00 24.82 ? 146  THR   A OG1   1 
ATOM   940   C  CG2   . THR   A  1  148  ? -25.273 55.488  72.764  1.00 26.53 ? 146  THR   A CG2   1 
ATOM   941   N  N     . TRP   A  1  149  ? -21.836 54.187  72.478  1.00 18.75 ? 147  TRP   A N     1 
ATOM   942   C  CA    . TRP   A  1  149  ? -21.341 53.115  71.629  1.00 19.36 ? 147  TRP   A CA    1 
ATOM   943   C  C     . TRP   A  1  149  ? -20.729 51.993  72.444  1.00 17.29 ? 147  TRP   A C     1 
ATOM   944   O  O     . TRP   A  1  149  ? -20.803 50.830  72.036  1.00 19.10 ? 147  TRP   A O     1 
ATOM   945   C  CB    . TRP   A  1  149  ? -20.342 53.650  70.606  1.00 19.81 ? 147  TRP   A CB    1 
ATOM   946   C  CG    . TRP   A  1  149  ? -21.000 54.527  69.605  1.00 17.86 ? 147  TRP   A CG    1 
ATOM   947   C  CD1   . TRP   A  1  149  ? -20.787 55.855  69.433  1.00 19.51 ? 147  TRP   A CD1   1 
ATOM   948   C  CD2   . TRP   A  1  149  ? -22.018 54.153  68.669  1.00 20.99 ? 147  TRP   A CD2   1 
ATOM   949   N  NE1   . TRP   A  1  149  ? -21.588 56.336  68.423  1.00 20.17 ? 147  TRP   A NE1   1 
ATOM   950   C  CE2   . TRP   A  1  149  ? -22.354 55.309  67.940  1.00 20.00 ? 147  TRP   A CE2   1 
ATOM   951   C  CE3   . TRP   A  1  149  ? -22.662 52.950  68.366  1.00 21.12 ? 147  TRP   A CE3   1 
ATOM   952   C  CZ2   . TRP   A  1  149  ? -23.318 55.303  66.932  1.00 23.40 ? 147  TRP   A CZ2   1 
ATOM   953   C  CZ3   . TRP   A  1  149  ? -23.618 52.943  67.360  1.00 26.36 ? 147  TRP   A CZ3   1 
ATOM   954   C  CH2   . TRP   A  1  149  ? -23.933 54.113  66.654  1.00 27.67 ? 147  TRP   A CH2   1 
ATOM   955   N  N     . GLY   A  1  150  ? -20.113 52.321  73.586  1.00 17.81 ? 148  GLY   A N     1 
ATOM   956   C  CA    . GLY   A  1  150  ? -19.618 51.278  74.467  1.00 20.16 ? 148  GLY   A CA    1 
ATOM   957   C  C     . GLY   A  1  150  ? -20.726 50.364  74.940  1.00 19.74 ? 148  GLY   A C     1 
ATOM   958   O  O     . GLY   A  1  150  ? -20.559 49.145  74.998  1.00 21.34 ? 148  GLY   A O     1 
ATOM   959   N  N     . LEU   A  1  151  ? -21.884 50.941  75.270  1.00 20.58 ? 149  LEU   A N     1 
ATOM   960   C  CA    . LEU   A  1  151  ? -23.028 50.119  75.638  1.00 24.69 ? 149  LEU   A CA    1 
ATOM   961   C  C     . LEU   A  1  151  ? -23.461 49.244  74.469  1.00 20.76 ? 149  LEU   A C     1 
ATOM   962   O  O     . LEU   A  1  151  ? -23.751 48.058  74.646  1.00 25.14 ? 149  LEU   A O     1 
ATOM   963   C  CB    . LEU   A  1  151  ? -24.166 51.023  76.111  1.00 25.79 ? 149  LEU   A CB    1 
ATOM   964   C  CG    . LEU   A  1  151  ? -25.286 50.406  76.935  1.00 31.23 ? 149  LEU   A CG    1 
ATOM   965   C  CD1   . LEU   A  1  151  ? -24.717 49.582  78.081  1.00 27.02 ? 149  LEU   A CD1   1 
ATOM   966   C  CD2   . LEU   A  1  151  ? -26.157 51.531  77.471  1.00 34.66 ? 149  LEU   A CD2   1 
ATOM   967   N  N     . VAL   A  1  152  ? -23.474 49.804  73.258  1.00 21.92 ? 150  VAL   A N     1 
ATOM   968   C  CA    . VAL   A  1  152  ? -23.833 49.035  72.065  1.00 23.86 ? 150  VAL   A CA    1 
ATOM   969   C  C     . VAL   A  1  152  ? -22.861 47.884  71.834  1.00 23.74 ? 150  VAL   A C     1 
ATOM   970   O  O     . VAL   A  1  152  ? -23.267 46.755  71.527  1.00 25.77 ? 150  VAL   A O     1 
ATOM   971   C  CB    . VAL   A  1  152  ? -23.913 49.966  70.840  1.00 23.79 ? 150  VAL   A CB    1 
ATOM   972   C  CG1   . VAL   A  1  152  ? -24.009 49.161  69.546  1.00 26.25 ? 150  VAL   A CG1   1 
ATOM   973   C  CG2   . VAL   A  1  152  ? -25.080 50.929  70.977  1.00 25.00 ? 150  VAL   A CG2   1 
ATOM   974   N  N     . VAL   A  1  153  ? -21.560 48.151  71.958  1.00 21.72 ? 151  VAL   A N     1 
ATOM   975   C  CA    . VAL   A  1  153  ? -20.562 47.154  71.591  1.00 24.36 ? 151  VAL   A CA    1 
ATOM   976   C  C     . VAL   A  1  153  ? -20.373 46.127  72.694  1.00 21.46 ? 151  VAL   A C     1 
ATOM   977   O  O     . VAL   A  1  153  ? -20.265 44.924  72.426  1.00 25.49 ? 151  VAL   A O     1 
ATOM   978   C  CB    . VAL   A  1  153  ? -19.242 47.851  71.220  1.00 21.96 ? 151  VAL   A CB    1 
ATOM   979   C  CG1   . VAL   A  1  153  ? -18.140 46.831  70.983  1.00 24.35 ? 151  VAL   A CG1   1 
ATOM   980   C  CG2   . VAL   A  1  153  ? -19.447 48.713  70.002  1.00 23.35 ? 151  VAL   A CG2   1 
ATOM   981   N  N     . THR   A  1  154  ? -20.294 46.578  73.944  1.00 24.37 ? 152  THR   A N     1 
ATOM   982   C  CA    . THR   A  1  154  ? -19.896 45.712  75.041  1.00 24.44 ? 152  THR   A CA    1 
ATOM   983   C  C     . THR   A  1  154  ? -21.039 45.344  75.970  1.00 28.12 ? 152  THR   A C     1 
ATOM   984   O  O     . THR   A  1  154  ? -20.878 44.423  76.779  1.00 29.53 ? 152  THR   A O     1 
ATOM   985   C  CB    . THR   A  1  154  ? -18.782 46.360  75.878  1.00 26.39 ? 152  THR   A CB    1 
ATOM   986   O  OG1   . THR   A  1  154  ? -19.312 47.462  76.631  1.00 26.60 ? 152  THR   A OG1   1 
ATOM   987   C  CG2   . THR   A  1  154  ? -17.657 46.854  74.992  1.00 26.85 ? 152  THR   A CG2   1 
ATOM   988   N  N     . GLY   A  1  155  ? -22.175 46.033  75.886  1.00 25.22 ? 153  GLY   A N     1 
ATOM   989   C  CA    . GLY   A  1  155  ? -23.234 45.854  76.857  1.00 26.84 ? 153  GLY   A CA    1 
ATOM   990   C  C     . GLY   A  1  155  ? -22.961 46.471  78.207  1.00 29.74 ? 153  GLY   A C     1 
ATOM   991   O  O     . GLY   A  1  155  ? -23.794 46.335  79.114  1.00 29.10 ? 153  GLY   A O     1 
ATOM   992   N  N     . LYS   A  1  156  ? -21.824 47.136  78.371  1.00 26.85 ? 154  LYS   A N     1 
ATOM   993   C  CA    . LYS   A  1  156  ? -21.419 47.735  79.632  1.00 29.15 ? 154  LYS   A CA    1 
ATOM   994   C  C     . LYS   A  1  156  ? -21.415 49.249  79.492  1.00 29.66 ? 154  LYS   A C     1 
ATOM   995   O  O     . LYS   A  1  156  ? -21.040 49.791  78.448  1.00 26.12 ? 154  LYS   A O     1 
ATOM   996   C  CB    . LYS   A  1  156  ? -20.021 47.264  80.040  1.00 33.34 ? 154  LYS   A CB    1 
ATOM   997   N  N     . LEU   A  1  157  ? -21.830 49.926  80.549  1.00 27.63 ? 155  LEU   A N     1 
ATOM   998   C  CA    . LEU   A  1  157  ? -21.881 51.375  80.572  1.00 29.96 ? 155  LEU   A CA    1 
ATOM   999   C  C     . LEU   A  1  157  ? -20.687 51.903  81.350  1.00 36.24 ? 155  LEU   A C     1 
ATOM   1000  O  O     . LEU   A  1  157  ? -20.418 51.451  82.467  1.00 36.03 ? 155  LEU   A O     1 
ATOM   1001  C  CB    . LEU   A  1  157  ? -23.169 51.833  81.246  1.00 28.81 ? 155  LEU   A CB    1 
ATOM   1002  C  CG    . LEU   A  1  157  ? -23.329 53.333  81.442  1.00 37.10 ? 155  LEU   A CG    1 
ATOM   1003  C  CD1   . LEU   A  1  157  ? -23.366 54.056  80.101  1.00 36.29 ? 155  LEU   A CD1   1 
ATOM   1004  C  CD2   . LEU   A  1  157  ? -24.597 53.572  82.226  1.00 34.39 ? 155  LEU   A CD2   1 
ATOM   1005  N  N     . THR   A  1  158  ? -19.962 52.836  80.747  1.00 43.05 ? 156  THR   A N     1 
ATOM   1006  C  CA    . THR   A  1  158  ? -18.947 53.618  81.434  1.00 40.31 ? 156  THR   A CA    1 
ATOM   1007  C  C     . THR   A  1  158  ? -19.415 55.065  81.470  1.00 44.28 ? 156  THR   A C     1 
ATOM   1008  O  O     . THR   A  1  158  ? -20.007 55.559  80.506  1.00 49.57 ? 156  THR   A O     1 
ATOM   1009  C  CB    . THR   A  1  158  ? -17.601 53.517  80.715  1.00 42.13 ? 156  THR   A CB    1 
ATOM   1010  N  N     . SER   A  1  159  ? -19.176 55.739  82.591  1.00 31.79 ? 157  SER   A N     1 
ATOM   1011  C  CA    . SER   A  1  159  ? -19.682 57.100  82.731  1.00 29.64 ? 157  SER   A CA    1 
ATOM   1012  C  C     . SER   A  1  159  ? -18.874 58.096  81.903  1.00 32.86 ? 157  SER   A C     1 
ATOM   1013  O  O     . SER   A  1  159  ? -19.435 59.035  81.330  1.00 33.24 ? 157  SER   A O     1 
ATOM   1014  C  CB    . SER   A  1  159  ? -19.711 57.498  84.207  1.00 35.88 ? 157  SER   A CB    1 
ATOM   1015  O  OG    . SER   A  1  159  ? -18.640 56.903  84.923  1.00 38.81 ? 157  SER   A OG    1 
ATOM   1016  N  N     . THR   A  1  160  ? -17.567 57.911  81.829  1.00 26.95 ? 158  THR   A N     1 
ATOM   1017  C  CA    . THR   A  1  160  ? -16.704 58.768  81.038  1.00 24.48 ? 158  THR   A CA    1 
ATOM   1018  C  C     . THR   A  1  160  ? -15.957 57.908  80.032  1.00 24.22 ? 158  THR   A C     1 
ATOM   1019  O  O     . THR   A  1  160  ? -15.963 56.679  80.101  1.00 26.29 ? 158  THR   A O     1 
ATOM   1020  C  CB    . THR   A  1  160  ? -15.710 59.515  81.930  1.00 24.32 ? 158  THR   A CB    1 
ATOM   1021  O  OG1   . THR   A  1  160  ? -14.906 58.559  82.627  1.00 29.18 ? 158  THR   A OG1   1 
ATOM   1022  C  CG2   . THR   A  1  160  ? -16.445 60.401  82.925  1.00 31.18 ? 158  THR   A CG2   1 
ATOM   1023  N  N     . VAL   A  1  161  ? -15.290 58.587  79.108  1.00 16.74 ? 159  VAL   A N     1 
ATOM   1024  C  CA    . VAL   A  1  161  ? -14.751 57.985  77.898  1.00 18.37 ? 159  VAL   A CA    1 
ATOM   1025  C  C     . VAL   A  1  161  ? -13.236 58.029  78.006  1.00 17.32 ? 159  VAL   A C     1 
ATOM   1026  O  O     . VAL   A  1  161  ? -12.666 59.098  78.234  1.00 16.65 ? 159  VAL   A O     1 
ATOM   1027  C  CB    . VAL   A  1  161  ? -15.221 58.797  76.679  1.00 18.80 ? 159  VAL   A CB    1 
ATOM   1028  C  CG1   . VAL   A  1  161  ? -14.485 58.406  75.448  1.00 23.25 ? 159  VAL   A CG1   1 
ATOM   1029  C  CG2   . VAL   A  1  161  ? -16.746 58.661  76.504  1.00 22.56 ? 159  VAL   A CG2   1 
ATOM   1030  N  N     . ASN   A  1  162  ? -12.581 56.882  77.836  1.00 16.08 ? 160  ASN   A N     1 
ATOM   1031  C  CA    . ASN   A  1  162  ? -11.122 56.897  77.751  1.00 16.34 ? 160  ASN   A CA    1 
ATOM   1032  C  C     . ASN   A  1  162  ? -10.783 57.240  76.311  1.00 14.87 ? 160  ASN   A C     1 
ATOM   1033  O  O     . ASN   A  1  162  ? -10.584 56.368  75.464  1.00 16.46 ? 160  ASN   A O     1 
ATOM   1034  C  CB    . ASN   A  1  162  ? -10.521 55.569  78.179  1.00 16.89 ? 160  ASN   A CB    1 
ATOM   1035  C  CG    . ASN   A  1  162  ? -9.016  55.636  78.257  1.00 17.40 ? 160  ASN   A CG    1 
ATOM   1036  O  OD1   . ASN   A  1  162  ? -8.395  56.465  77.590  1.00 17.10 ? 160  ASN   A OD1   1 
ATOM   1037  N  ND2   . ASN   A  1  162  ? -8.425  54.783  79.073  1.00 23.03 ? 160  ASN   A ND2   1 
ATOM   1038  N  N     . ASP   A  1  163  ? -10.710 58.547  76.045  1.00 14.24 ? 161  ASP   A N     1 
ATOM   1039  C  CA    . ASP   A  1  163  ? -10.539 59.020  74.684  1.00 15.75 ? 161  ASP   A CA    1 
ATOM   1040  C  C     . ASP   A  1  163  ? -9.155  58.711  74.145  1.00 15.08 ? 161  ASP   A C     1 
ATOM   1041  O  O     . ASP   A  1  163  ? -8.985  58.559  72.939  1.00 16.79 ? 161  ASP   A O     1 
ATOM   1042  C  CB    . ASP   A  1  163  ? -10.895 60.508  74.546  1.00 18.00 ? 161  ASP   A CB    1 
ATOM   1043  C  CG    . ASP   A  1  163  ? -10.215 61.410  75.572  1.00 20.27 ? 161  ASP   A CG    1 
ATOM   1044  O  OD1   . ASP   A  1  163  ? -10.089 61.044  76.764  1.00 17.80 ? 161  ASP   A OD1   1 
ATOM   1045  O  OD2   . ASP   A  1  163  ? -9.873  62.541  75.177  1.00 22.50 ? 161  ASP   A OD2   1 
ATOM   1046  N  N     . ARG   A  1  164  ? -8.154  58.600  75.015  1.00 15.88 ? 162  ARG   A N     1 
ATOM   1047  C  CA    A ARG   A  1  164  ? -6.832  58.243  74.523  0.55 14.71 ? 162  ARG   A CA    1 
ATOM   1048  C  CA    B ARG   A  1  164  ? -6.826  58.239  74.535  0.45 14.74 ? 162  ARG   A CA    1 
ATOM   1049  C  C     . ARG   A  1  164  ? -6.768  56.773  74.129  1.00 15.05 ? 162  ARG   A C     1 
ATOM   1050  O  O     . ARG   A  1  164  ? -6.102  56.420  73.147  1.00 15.25 ? 162  ARG   A O     1 
ATOM   1051  C  CB    A ARG   A  1  164  ? -5.770  58.601  75.559  0.55 16.77 ? 162  ARG   A CB    1 
ATOM   1052  C  CB    B ARG   A  1  164  ? -5.781  58.565  75.599  0.45 16.78 ? 162  ARG   A CB    1 
ATOM   1053  C  CG    A ARG   A  1  164  ? -5.674  60.089  75.844  0.55 18.25 ? 162  ARG   A CG    1 
ATOM   1054  C  CG    B ARG   A  1  164  ? -5.593  60.052  75.847  0.45 18.30 ? 162  ARG   A CG    1 
ATOM   1055  C  CD    A ARG   A  1  164  ? -5.734  60.935  74.572  0.55 23.71 ? 162  ARG   A CD    1 
ATOM   1056  C  CD    B ARG   A  1  164  ? -5.471  60.829  74.545  0.45 22.88 ? 162  ARG   A CD    1 
ATOM   1057  N  NE    A ARG   A  1  164  ? -4.786  60.528  73.541  0.55 22.11 ? 162  ARG   A NE    1 
ATOM   1058  N  NE    B ARG   A  1  164  ? -6.760  61.399  74.167  0.45 21.98 ? 162  ARG   A NE    1 
ATOM   1059  C  CZ    A ARG   A  1  164  ? -4.928  60.803  72.250  0.55 25.55 ? 162  ARG   A CZ    1 
ATOM   1060  C  CZ    B ARG   A  1  164  ? -7.080  61.811  72.950  0.45 22.72 ? 162  ARG   A CZ    1 
ATOM   1061  N  NH1   A ARG   A  1  164  ? -5.976  61.471  71.797  0.55 27.49 ? 162  ARG   A NH1   1 
ATOM   1062  N  NH1   B ARG   A  1  164  ? -6.230  61.715  71.942  0.45 27.47 ? 162  ARG   A NH1   1 
ATOM   1063  N  NH2   A ARG   A  1  164  ? -3.998  60.393  71.391  0.55 22.51 ? 162  ARG   A NH2   1 
ATOM   1064  N  NH2   B ARG   A  1  164  ? -8.290  62.323  72.738  0.45 24.98 ? 162  ARG   A NH2   1 
ATOM   1065  N  N     . SER   A  1  165  ? -7.466  55.909  74.869  1.00 14.83 ? 163  SER   A N     1 
ATOM   1066  C  CA    . SER   A  1  165  ? -7.556  54.511  74.469  1.00 13.98 ? 163  SER   A CA    1 
ATOM   1067  C  C     . SER   A  1  165  ? -8.300  54.373  73.151  1.00 15.74 ? 163  SER   A C     1 
ATOM   1068  O  O     . SER   A  1  165  ? -7.902  53.591  72.277  1.00 14.25 ? 163  SER   A O     1 
ATOM   1069  C  CB    . SER   A  1  165  ? -8.257  53.714  75.570  1.00 14.53 ? 163  SER   A CB    1 
ATOM   1070  O  OG    . SER   A  1  165  ? -8.536  52.384  75.148  1.00 17.67 ? 163  SER   A OG    1 
ATOM   1071  N  N     . LEU   A  1  166  ? -9.405  55.109  73.005  1.00 15.60 ? 164  LEU   A N     1 
ATOM   1072  C  CA    . LEU   A  1  166  ? -10.163 55.049  71.764  1.00 15.76 ? 164  LEU   A CA    1 
ATOM   1073  C  C     . LEU   A  1  166  ? -9.365  55.596  70.594  1.00 14.99 ? 164  LEU   A C     1 
ATOM   1074  O  O     . LEU   A  1  166  ? -9.442  55.059  69.489  1.00 15.32 ? 164  LEU   A O     1 
ATOM   1075  C  CB    . LEU   A  1  166  ? -11.462 55.823  71.930  1.00 15.05 ? 164  LEU   A CB    1 
ATOM   1076  C  CG    . LEU   A  1  166  ? -12.406 55.112  72.884  1.00 14.84 ? 164  LEU   A CG    1 
ATOM   1077  C  CD1   . LEU   A  1  166  ? -13.568 56.009  73.188  1.00 17.29 ? 164  LEU   A CD1   1 
ATOM   1078  C  CD2   . LEU   A  1  166  ? -12.886 53.794  72.288  1.00 16.88 ? 164  LEU   A CD2   1 
ATOM   1079  N  N     . ALA   A  1  167  ? -8.617  56.679  70.806  1.00 15.52 ? 165  ALA   A N     1 
ATOM   1080  C  CA    . ALA   A  1  167  ? -7.818  57.216  69.714  1.00 15.57 ? 165  ALA   A CA    1 
ATOM   1081  C  C     . ALA   A  1  167  ? -6.751  56.221  69.289  1.00 16.55 ? 165  ALA   A C     1 
ATOM   1082  O  O     . ALA   A  1  167  ? -6.519  56.027  68.092  1.00 16.85 ? 165  ALA   A O     1 
ATOM   1083  C  CB    . ALA   A  1  167  ? -7.183  58.537  70.132  1.00 17.55 ? 165  ALA   A CB    1 
ATOM   1084  N  N     . ALA   A  1  168  ? -6.085  55.594  70.260  1.00 15.93 ? 166  ALA   A N     1 
ATOM   1085  C  CA    . ALA   A  1  168  ? -5.114  54.557  69.929  1.00 16.23 ? 166  ALA   A CA    1 
ATOM   1086  C  C     . ALA   A  1  168  ? -5.772  53.423  69.163  1.00 14.30 ? 166  ALA   A C     1 
ATOM   1087  O  O     . ALA   A  1  168  ? -5.216  52.921  68.178  1.00 16.80 ? 166  ALA   A O     1 
ATOM   1088  C  CB    . ALA   A  1  168  ? -4.484  54.032  71.224  1.00 16.93 ? 166  ALA   A CB    1 
ATOM   1089  N  N     . ALA   A  1  169  ? -6.971  53.022  69.595  1.00 15.23 ? 167  ALA   A N     1 
ATOM   1090  C  CA    . ALA   A  1  169  ? -7.643  51.899  68.975  1.00 14.04 ? 167  ALA   A CA    1 
ATOM   1091  C  C     . ALA   A  1  169  ? -8.081  52.244  67.559  1.00 15.37 ? 167  ALA   A C     1 
ATOM   1092  O  O     . ALA   A  1  169  ? -8.018  51.400  66.662  1.00 16.48 ? 167  ALA   A O     1 
ATOM   1093  C  CB    . ALA   A  1  169  ? -8.851  51.506  69.823  1.00 15.52 ? 167  ALA   A CB    1 
ATOM   1094  N  N     . LEU   A  1  170  ? -8.530  53.480  67.350  1.00 15.99 ? 168  LEU   A N     1 
ATOM   1095  C  CA    . LEU   A  1  170  ? -8.943  53.901  66.018  1.00 16.05 ? 168  LEU   A CA    1 
ATOM   1096  C  C     . LEU   A  1  170  ? -7.755  53.921  65.066  1.00 16.04 ? 168  LEU   A C     1 
ATOM   1097  O  O     . LEU   A  1  170  ? -7.822  53.386  63.953  1.00 16.75 ? 168  LEU   A O     1 
ATOM   1098  C  CB    . LEU   A  1  170  ? -9.587  55.278  66.115  1.00 17.60 ? 168  LEU   A CB    1 
ATOM   1099  C  CG    . LEU   A  1  170  ? -10.221 55.696  64.794  1.00 18.14 ? 168  LEU   A CG    1 
ATOM   1100  C  CD1   . LEU   A  1  170  ? -11.198 54.640  64.271  1.00 20.96 ? 168  LEU   A CD1   1 
ATOM   1101  C  CD2   . LEU   A  1  170  ? -10.921 57.001  64.974  1.00 20.21 ? 168  LEU   A CD2   1 
ATOM   1102  N  N     . THR   A  1  171  ? -6.638  54.500  65.509  1.00 16.47 ? 169  THR   A N     1 
ATOM   1103  C  CA    . THR   A  1  171  ? -5.433  54.487  64.693  1.00 16.93 ? 169  THR   A CA    1 
ATOM   1104  C  C     . THR   A  1  171  ? -5.035  53.057  64.360  1.00 16.32 ? 169  THR   A C     1 
ATOM   1105  O  O     . THR   A  1  171  ? -4.718  52.728  63.213  1.00 17.82 ? 169  THR   A O     1 
ATOM   1106  C  CB    . THR   A  1  171  ? -4.320  55.190  65.458  1.00 19.16 ? 169  THR   A CB    1 
ATOM   1107  O  OG1   . THR   A  1  171  ? -4.672  56.560  65.667  1.00 22.27 ? 169  THR   A OG1   1 
ATOM   1108  C  CG2   . THR   A  1  171  ? -3.007  55.119  64.706  1.00 19.58 ? 169  THR   A CG2   1 
ATOM   1109  N  N     . ARG   A  1  172  ? -5.062  52.188  65.369  1.00 16.71 ? 170  ARG   A N     1 
ATOM   1110  C  CA    . ARG   A  1  172  ? -4.645  50.807  65.165  1.00 16.39 ? 170  ARG   A CA    1 
ATOM   1111  C  C     . ARG   A  1  172  ? -5.534  50.104  64.157  1.00 17.92 ? 170  ARG   A C     1 
ATOM   1112  O  O     . ARG   A  1  172  ? -5.046  49.427  63.243  1.00 17.93 ? 170  ARG   A O     1 
ATOM   1113  C  CB    . ARG   A  1  172  ? -4.656  50.064  66.503  1.00 16.58 ? 170  ARG   A CB    1 
ATOM   1114  C  CG    . ARG   A  1  172  ? -3.941  48.724  66.435  1.00 16.42 ? 170  ARG   A CG    1 
ATOM   1115  C  CD    . ARG   A  1  172  ? -4.098  47.928  67.719  1.00 18.05 ? 170  ARG   A CD    1 
ATOM   1116  N  NE    . ARG   A  1  172  ? -3.850  48.730  68.909  1.00 16.01 ? 170  ARG   A NE    1 
ATOM   1117  C  CZ    . ARG   A  1  172  ? -4.796  49.176  69.725  1.00 16.37 ? 170  ARG   A CZ    1 
ATOM   1118  N  NH1   . ARG   A  1  172  ? -6.077  48.924  69.512  1.00 16.05 ? 170  ARG   A NH1   1 
ATOM   1119  N  NH2   . ARG   A  1  172  ? -4.452  49.920  70.765  1.00 17.23 ? 170  ARG   A NH2   1 
ATOM   1120  N  N     . LEU   A  1  173  ? -6.848  50.260  64.291  1.00 17.09 ? 171  LEU   A N     1 
ATOM   1121  C  CA    . LEU   A  1  173  ? -7.727  49.490  63.422  1.00 15.94 ? 171  LEU   A CA    1 
ATOM   1122  C  C     . LEU   A  1  173  ? -7.695  50.016  61.992  1.00 17.18 ? 171  LEU   A C     1 
ATOM   1123  O  O     . LEU   A  1  173  ? -7.773  49.237  61.041  1.00 18.48 ? 171  LEU   A O     1 
ATOM   1124  C  CB    . LEU   A  1  173  ? -9.153  49.470  63.988  1.00 18.56 ? 171  LEU   A CB    1 
ATOM   1125  C  CG    . LEU   A  1  173  ? -10.049 50.713  63.922  1.00 19.78 ? 171  LEU   A CG    1 
ATOM   1126  C  CD1   . LEU   A  1  173  ? -10.863 50.743  62.623  1.00 21.51 ? 171  LEU   A CD1   1 
ATOM   1127  C  CD2   . LEU   A  1  173  ? -10.991 50.753  65.106  1.00 18.10 ? 171  LEU   A CD2   1 
ATOM   1128  N  N     . ILE   A  1  174  ? -7.580  51.334  61.826  1.00 18.14 ? 172  ILE   A N     1 
ATOM   1129  C  CA    . ILE   A  1  174  ? -7.479  51.890  60.480  1.00 17.96 ? 172  ILE   A CA    1 
ATOM   1130  C  C     . ILE   A  1  174  ? -6.169  51.468  59.837  1.00 19.39 ? 172  ILE   A C     1 
ATOM   1131  O  O     . ILE   A  1  174  ? -6.143  51.047  58.677  1.00 20.74 ? 172  ILE   A O     1 
ATOM   1132  C  CB    . ILE   A  1  174  ? -7.631  53.420  60.518  1.00 18.14 ? 172  ILE   A CB    1 
ATOM   1133  C  CG1   . ILE   A  1  174  ? -9.063  53.811  60.872  1.00 20.51 ? 172  ILE   A CG1   1 
ATOM   1134  C  CG2   . ILE   A  1  174  ? -7.210  54.033  59.164  1.00 23.75 ? 172  ILE   A CG2   1 
ATOM   1135  C  CD1   . ILE   A  1  174  ? -9.210  55.269  61.215  1.00 21.87 ? 172  ILE   A CD1   1 
ATOM   1136  N  N     . SER   A  1  175  ? -5.071  51.540  60.587  1.00 19.52 ? 173  SER   A N     1 
ATOM   1137  C  CA    . SER   A  1  175  ? -3.787  51.157  60.011  1.00 19.04 ? 173  SER   A CA    1 
ATOM   1138  C  C     . SER   A  1  175  ? -3.734  49.672  59.702  1.00 20.09 ? 173  SER   A C     1 
ATOM   1139  O  O     . SER   A  1  175  ? -2.985  49.251  58.813  1.00 22.32 ? 173  SER   A O     1 
ATOM   1140  C  CB    . SER   A  1  175  ? -2.649  51.536  60.948  1.00 21.69 ? 173  SER   A CB    1 
ATOM   1141  O  OG    . SER   A  1  175  ? -2.544  52.937  61.071  1.00 25.54 ? 173  SER   A OG    1 
ATOM   1142  N  N     . ARG   A  1  176  ? -4.517  48.866  60.409  1.00 19.20 ? 174  ARG   A N     1 
ATOM   1143  C  CA    . ARG   A  1  176  ? -4.503  47.433  60.164  1.00 20.13 ? 174  ARG   A CA    1 
ATOM   1144  C  C     . ARG   A  1  176  ? -5.457  47.033  59.048  1.00 22.25 ? 174  ARG   A C     1 
ATOM   1145  O  O     . ARG   A  1  176  ? -5.096  46.218  58.190  1.00 24.06 ? 174  ARG   A O     1 
ATOM   1146  C  CB    . ARG   A  1  176  ? -4.875  46.714  61.465  1.00 21.47 ? 174  ARG   A CB    1 
ATOM   1147  C  CG    . ARG   A  1  176  ? -4.720  45.202  61.418  1.00 21.58 ? 174  ARG   A CG    1 
ATOM   1148  C  CD    . ARG   A  1  176  ? -4.946  44.617  62.808  1.00 23.41 ? 174  ARG   A CD    1 
ATOM   1149  N  NE    . ARG   A  1  176  ? -6.363  44.612  63.159  1.00 22.10 ? 174  ARG   A NE    1 
ATOM   1150  C  CZ    . ARG   A  1  176  ? -6.928  45.278  64.166  1.00 22.49 ? 174  ARG   A CZ    1 
ATOM   1151  N  NH1   . ARG   A  1  176  ? -6.221  46.026  65.012  1.00 20.32 ? 174  ARG   A NH1   1 
ATOM   1152  N  NH2   . ARG   A  1  176  ? -8.248  45.202  64.329  1.00 27.73 ? 174  ARG   A NH2   1 
ATOM   1153  N  N     . CYS   A  1  177  ? -6.670  47.601  59.030  1.00 20.63 ? 175  CYS   A N     1 
ATOM   1154  C  CA    . CYS   A  1  177  ? -7.728  47.145  58.138  1.00 24.89 ? 175  CYS   A CA    1 
ATOM   1155  C  C     . CYS   A  1  177  ? -8.172  48.155  57.090  1.00 24.02 ? 175  CYS   A C     1 
ATOM   1156  O  O     . CYS   A  1  177  ? -8.859  47.760  56.142  1.00 29.12 ? 175  CYS   A O     1 
ATOM   1157  C  CB    . CYS   A  1  177  ? -8.964  46.716  58.940  1.00 26.38 ? 175  CYS   A CB    1 
ATOM   1158  S  SG    . CYS   A  1  177  ? -8.601  45.556  60.270  1.00 27.43 ? 175  CYS   A SG    1 
ATOM   1159  N  N     . GLY   A  1  178  ? -7.862  49.435  57.256  1.00 23.17 ? 176  GLY   A N     1 
ATOM   1160  C  CA    . GLY   A  1  178  ? -8.037  50.366  56.159  1.00 25.49 ? 176  GLY   A CA    1 
ATOM   1161  C  C     . GLY   A  1  178  ? -9.484  50.702  55.828  1.00 22.95 ? 176  GLY   A C     1 
ATOM   1162  O  O     . GLY   A  1  178  ? -10.411 50.545  56.626  1.00 24.04 ? 176  GLY   A O     1 
ATOM   1163  N  N     . GLU   A  1  179  ? -9.657  51.168  54.596  1.00 23.75 ? 177  GLU   A N     1 
ATOM   1164  C  CA    . GLU   A  1  179  ? -10.980 51.585  54.134  1.00 23.45 ? 177  GLU   A CA    1 
ATOM   1165  C  C     . GLU   A  1  179  ? -12.076 50.542  54.321  1.00 22.29 ? 177  GLU   A C     1 
ATOM   1166  O  O     . GLU   A  1  179  ? -13.198 50.932  54.694  1.00 23.08 ? 177  GLU   A O     1 
ATOM   1167  C  CB    . GLU   A  1  179  ? -10.907 52.077  52.680  1.00 25.00 ? 177  GLU   A CB    1 
ATOM   1168  N  N     . PRO   A  1  180  ? -11.863 49.247  54.057  1.00 22.73 ? 178  PRO   A N     1 
ATOM   1169  C  CA    . PRO   A  1  180  ? -12.974 48.295  54.222  1.00 24.14 ? 178  PRO   A CA    1 
ATOM   1170  C  C     . PRO   A  1  180  ? -13.621 48.332  55.595  1.00 21.61 ? 178  PRO   A C     1 
ATOM   1171  O  O     . PRO   A  1  180  ? -14.855 48.284  55.688  1.00 23.22 ? 178  PRO   A O     1 
ATOM   1172  C  CB    . PRO   A  1  180  ? -12.324 46.944  53.910  1.00 25.29 ? 178  PRO   A CB    1 
ATOM   1173  C  CG    . PRO   A  1  180  ? -11.227 47.284  52.958  1.00 25.21 ? 178  PRO   A CG    1 
ATOM   1174  C  CD    . PRO   A  1  180  ? -10.714 48.626  53.368  1.00 24.38 ? 178  PRO   A CD    1 
ATOM   1175  N  N     . VAL   A  1  181  ? -12.836 48.431  56.668  1.00 22.15 ? 179  VAL   A N     1 
ATOM   1176  C  CA    . VAL   A  1  181  ? -13.448 48.445  57.991  1.00 21.07 ? 179  VAL   A CA    1 
ATOM   1177  C  C     . VAL   A  1  181  ? -14.192 49.753  58.237  1.00 20.80 ? 179  VAL   A C     1 
ATOM   1178  O  O     . VAL   A  1  181  ? -15.235 49.764  58.902  1.00 20.72 ? 179  VAL   A O     1 
ATOM   1179  C  CB    . VAL   A  1  181  ? -12.418 48.110  59.090  1.00 21.32 ? 179  VAL   A CB    1 
ATOM   1180  C  CG1   . VAL   A  1  181  ? -11.444 49.270  59.317  1.00 20.83 ? 179  VAL   A CG1   1 
ATOM   1181  C  CG2   . VAL   A  1  181  ? -13.132 47.737  60.377  1.00 23.32 ? 179  VAL   A CG2   1 
ATOM   1182  N  N     . ILE   A  1  182  ? -13.695 50.863  57.693  1.00 20.57 ? 180  ILE   A N     1 
ATOM   1183  C  CA    . ILE   A  1  182  ? -14.372 52.145  57.848  1.00 21.32 ? 180  ILE   A CA    1 
ATOM   1184  C  C     . ILE   A  1  182  ? -15.705 52.112  57.125  1.00 22.40 ? 180  ILE   A C     1 
ATOM   1185  O  O     . ILE   A  1  182  ? -16.733 52.544  57.656  1.00 22.13 ? 180  ILE   A O     1 
ATOM   1186  C  CB    . ILE   A  1  182  ? -13.493 53.288  57.322  1.00 21.78 ? 180  ILE   A CB    1 
ATOM   1187  C  CG1   . ILE   A  1  182  ? -12.169 53.337  58.081  1.00 21.10 ? 180  ILE   A CG1   1 
ATOM   1188  C  CG2   . ILE   A  1  182  ? -14.232 54.615  57.441  1.00 21.95 ? 180  ILE   A CG2   1 
ATOM   1189  C  CD1   . ILE   A  1  182  ? -11.134 54.236  57.436  1.00 24.50 ? 180  ILE   A CD1   1 
ATOM   1190  N  N     . ARG   A  1  183  ? -15.691 51.605  55.895  1.00 20.48 ? 181  ARG   A N     1 
ATOM   1191  C  CA    A ARG   A  1  183  ? -16.919 51.467  55.121  0.43 24.31 ? 181  ARG   A CA    1 
ATOM   1192  C  CA    B ARG   A  1  183  ? -16.915 51.455  55.114  0.57 24.29 ? 181  ARG   A CA    1 
ATOM   1193  C  C     . ARG   A  1  183  ? -17.951 50.639  55.875  1.00 25.05 ? 181  ARG   A C     1 
ATOM   1194  O  O     . ARG   A  1  183  ? -19.128 51.022  55.963  1.00 23.97 ? 181  ARG   A O     1 
ATOM   1195  C  CB    A ARG   A  1  183  ? -16.591 50.839  53.762  0.43 26.48 ? 181  ARG   A CB    1 
ATOM   1196  C  CB    B ARG   A  1  183  ? -16.565 50.769  53.791  0.57 26.45 ? 181  ARG   A CB    1 
ATOM   1197  C  CG    A ARG   A  1  183  ? -17.789 50.373  52.942  0.43 31.06 ? 181  ARG   A CG    1 
ATOM   1198  C  CG    B ARG   A  1  183  ? -17.734 50.486  52.860  0.57 31.11 ? 181  ARG   A CG    1 
ATOM   1199  C  CD    A ARG   A  1  183  ? -18.828 51.472  52.781  0.43 31.90 ? 181  ARG   A CD    1 
ATOM   1200  C  CD    B ARG   A  1  183  ? -18.172 51.744  52.133  0.57 33.28 ? 181  ARG   A CD    1 
ATOM   1201  N  NE    A ARG   A  1  183  ? -18.238 52.739  52.366  0.43 32.11 ? 181  ARG   A NE    1 
ATOM   1202  N  NE    B ARG   A  1  183  ? -19.135 52.520  52.907  0.57 31.41 ? 181  ARG   A NE    1 
ATOM   1203  C  CZ    A ARG   A  1  183  ? -18.793 53.922  52.592  0.43 34.68 ? 181  ARG   A CZ    1 
ATOM   1204  C  CZ    B ARG   A  1  183  ? -19.282 53.835  52.809  0.57 34.43 ? 181  ARG   A CZ    1 
ATOM   1205  N  NH1   A ARG   A  1  183  ? -19.934 54.034  53.253  0.43 33.53 ? 181  ARG   A NH1   1 
ATOM   1206  N  NH1   B ARG   A  1  183  ? -18.500 54.560  52.025  0.57 35.62 ? 181  ARG   A NH1   1 
ATOM   1207  N  NH2   A ARG   A  1  183  ? -18.185 55.018  52.147  0.43 34.82 ? 181  ARG   A NH2   1 
ATOM   1208  N  NH2   B ARG   A  1  183  ? -20.233 54.435  53.518  0.57 34.14 ? 181  ARG   A NH2   1 
ATOM   1209  N  N     . ARG   A  1  184  ? -17.532 49.502  56.426  1.00 22.90 ? 182  ARG   A N     1 
ATOM   1210  C  CA    . ARG   A  1  184  ? -18.460 48.650  57.154  1.00 23.00 ? 182  ARG   A CA    1 
ATOM   1211  C  C     . ARG   A  1  184  ? -18.977 49.344  58.402  1.00 23.20 ? 182  ARG   A C     1 
ATOM   1212  O  O     . ARG   A  1  184  ? -20.166 49.245  58.725  1.00 24.31 ? 182  ARG   A O     1 
ATOM   1213  C  CB    . ARG   A  1  184  ? -17.777 47.333  57.509  1.00 26.49 ? 182  ARG   A CB    1 
ATOM   1214  C  CG    . ARG   A  1  184  ? -17.694 46.373  56.339  1.00 30.33 ? 182  ARG   A CG    1 
ATOM   1215  C  CD    . ARG   A  1  184  ? -18.913 45.450  56.299  1.00 29.16 ? 182  ARG   A CD    1 
ATOM   1216  N  NE    . ARG   A  1  184  ? -18.754 44.319  57.207  1.00 35.62 ? 182  ARG   A NE    1 
ATOM   1217  C  CZ    . ARG   A  1  184  ? -19.591 44.001  58.185  1.00 34.04 ? 182  ARG   A CZ    1 
ATOM   1218  N  NH1   . ARG   A  1  184  ? -20.696 44.697  58.408  1.00 32.98 ? 182  ARG   A NH1   1 
ATOM   1219  N  NH2   . ARG   A  1  184  ? -19.319 42.948  58.952  1.00 30.84 ? 182  ARG   A NH2   1 
ATOM   1220  N  N     . GLY   A  1  185  ? -18.102 50.058  59.111  1.00 22.08 ? 183  GLY   A N     1 
ATOM   1221  C  CA    . GLY   A  1  185  ? -18.545 50.802  60.277  1.00 22.73 ? 183  GLY   A CA    1 
ATOM   1222  C  C     . GLY   A  1  185  ? -19.561 51.871  59.926  1.00 21.73 ? 183  GLY   A C     1 
ATOM   1223  O  O     . GLY   A  1  185  ? -20.592 52.002  60.586  1.00 21.08 ? 183  GLY   A O     1 
ATOM   1224  N  N     . VAL   A  1  186  ? -19.281 52.646  58.875  1.00 21.29 ? 184  VAL   A N     1 
ATOM   1225  C  CA    . VAL   A  1  186  ? -20.207 53.688  58.434  1.00 24.00 ? 184  VAL   A CA    1 
ATOM   1226  C  C     . VAL   A  1  186  ? -21.563 53.094  58.082  1.00 23.94 ? 184  VAL   A C     1 
ATOM   1227  O  O     . VAL   A  1  186  ? -22.609 53.613  58.489  1.00 22.87 ? 184  VAL   A O     1 
ATOM   1228  C  CB    . VAL   A  1  186  ? -19.611 54.472  57.254  1.00 23.91 ? 184  VAL   A CB    1 
ATOM   1229  C  CG1   . VAL   A  1  186  ? -20.705 55.319  56.575  1.00 25.71 ? 184  VAL   A CG1   1 
ATOM   1230  C  CG2   . VAL   A  1  186  ? -18.462 55.331  57.729  1.00 24.44 ? 184  VAL   A CG2   1 
ATOM   1231  N  N     . ASP   A  1  187  ? -21.568 52.000  57.325  1.00 21.76 ? 185  ASP   A N     1 
ATOM   1232  C  CA    . ASP   A  1  187  ? -22.841 51.415  56.915  1.00 24.87 ? 185  ASP   A CA    1 
ATOM   1233  C  C     . ASP   A  1  187  ? -23.596 50.874  58.121  1.00 27.63 ? 185  ASP   A C     1 
ATOM   1234  O  O     . ASP   A  1  187  ? -24.821 51.022  58.213  1.00 26.39 ? 185  ASP   A O     1 
ATOM   1235  C  CB    . ASP   A  1  187  ? -22.620 50.317  55.873  1.00 27.75 ? 185  ASP   A CB    1 
ATOM   1236  C  CG    . ASP   A  1  187  ? -22.101 50.857  54.546  1.00 29.58 ? 185  ASP   A CG    1 
ATOM   1237  O  OD1   . ASP   A  1  187  ? -22.199 52.082  54.312  1.00 35.51 ? 185  ASP   A OD1   1 
ATOM   1238  O  OD2   . ASP   A  1  187  ? -21.597 50.056  53.735  1.00 33.06 ? 185  ASP   A OD2   1 
ATOM   1239  N  N     . MET   A  1  188  ? -22.878 50.269  59.067  1.00 25.18 ? 186  MET   A N     1 
ATOM   1240  C  CA    . MET   A  1  188  ? -23.512 49.777  60.285  1.00 25.65 ? 186  MET   A CA    1 
ATOM   1241  C  C     . MET   A  1  188  ? -24.104 50.918  61.099  1.00 26.71 ? 186  MET   A C     1 
ATOM   1242  O  O     . MET   A  1  188  ? -25.255 50.848  61.547  1.00 25.47 ? 186  MET   A O     1 
ATOM   1243  C  CB    . MET   A  1  188  ? -22.485 49.021  61.124  1.00 28.26 ? 186  MET   A CB    1 
ATOM   1244  C  CG    . MET   A  1  188  ? -23.051 48.447  62.400  1.00 31.85 ? 186  MET   A CG    1 
ATOM   1245  S  SD    . MET   A  1  188  ? -24.199 47.126  62.009  1.00 40.84 ? 186  MET   A SD    1 
ATOM   1246  C  CE    . MET   A  1  188  ? -23.130 46.106  60.985  1.00 36.17 ? 186  MET   A CE    1 
ATOM   1247  N  N     . ALA   A  1  189  ? -23.323 51.975  61.328  1.00 23.27 ? 187  ALA   A N     1 
ATOM   1248  C  CA    . ALA   A  1  189  ? -23.829 53.098  62.107  1.00 24.26 ? 187  ALA   A CA    1 
ATOM   1249  C  C     . ALA   A  1  189  ? -25.007 53.758  61.413  1.00 24.65 ? 187  ALA   A C     1 
ATOM   1250  O  O     . ALA   A  1  189  ? -25.968 54.175  62.069  1.00 22.73 ? 187  ALA   A O     1 
ATOM   1251  C  CB    . ALA   A  1  189  ? -22.723 54.117  62.358  1.00 27.26 ? 187  ALA   A CB    1 
ATOM   1252  N  N     . MET   A  1  190  ? -24.948 53.872  60.089  1.00 24.00 ? 188  MET   A N     1 
ATOM   1253  C  CA    . MET   A  1  190  ? -26.052 54.483  59.359  1.00 25.41 ? 188  MET   A CA    1 
ATOM   1254  C  C     . MET   A  1  190  ? -27.326 53.678  59.543  1.00 25.28 ? 188  MET   A C     1 
ATOM   1255  O  O     . MET   A  1  190  ? -28.405 54.244  59.757  1.00 26.21 ? 188  MET   A O     1 
ATOM   1256  C  CB    . MET   A  1  190  ? -25.697 54.563  57.880  1.00 26.19 ? 188  MET   A CB    1 
ATOM   1257  C  CG    . MET   A  1  190  ? -26.732 55.270  57.031  1.00 32.59 ? 188  MET   A CG    1 
ATOM   1258  S  SD    . MET   A  1  190  ? -26.340 55.111  55.274  1.00 38.61 ? 188  MET   A SD    1 
ATOM   1259  C  CE    . MET   A  1  190  ? -24.571 55.387  55.299  1.00 34.09 ? 188  MET   A CE    1 
ATOM   1260  N  N     . ARG   A  1  191  ? -27.218 52.353  59.472  1.00 23.37 ? 189  ARG   A N     1 
ATOM   1261  C  CA    . ARG   A  1  191  ? -28.388 51.511  59.685  1.00 25.83 ? 189  ARG   A CA    1 
ATOM   1262  C  C     . ARG   A  1  191  ? -28.883 51.613  61.118  1.00 25.77 ? 189  ARG   A C     1 
ATOM   1263  O  O     . ARG   A  1  191  ? -30.090 51.731  61.362  1.00 25.30 ? 189  ARG   A O     1 
ATOM   1264  C  CB    . ARG   A  1  191  ? -28.057 50.058  59.346  1.00 28.66 ? 189  ARG   A CB    1 
ATOM   1265  N  N     . MET   A  1  192  ? -27.976 51.561  62.087  1.00 22.46 ? 190  MET   A N     1 
ATOM   1266  C  CA    . MET   A  1  192  ? -28.421 51.592  63.473  1.00 22.29 ? 190  MET   A CA    1 
ATOM   1267  C  C     . MET   A  1  192  ? -29.050 52.933  63.813  1.00 25.37 ? 190  MET   A C     1 
ATOM   1268  O  O     . MET   A  1  192  ? -30.121 52.988  64.424  1.00 24.58 ? 190  MET   A O     1 
ATOM   1269  C  CB    . MET   A  1  192  ? -27.255 51.281  64.406  1.00 25.13 ? 190  MET   A CB    1 
ATOM   1270  C  CG    . MET   A  1  192  ? -26.797 49.855  64.311  1.00 22.78 ? 190  MET   A CG    1 
ATOM   1271  S  SD    . MET   A  1  192  ? -25.434 49.549  65.433  1.00 34.47 ? 190  MET   A SD    1 
ATOM   1272  C  CE    . MET   A  1  192  ? -26.354 49.346  66.948  1.00 32.23 ? 190  MET   A CE    1 
ATOM   1273  N  N     . MET   A  1  193  ? -28.410 54.026  63.416  1.00 23.71 ? 191  MET   A N     1 
ATOM   1274  C  CA    . MET   A  1  193  ? -28.900 55.337  63.810  1.00 25.37 ? 191  MET   A CA    1 
ATOM   1275  C  C     . MET   A  1  193  ? -30.107 55.787  63.003  1.00 26.28 ? 191  MET   A C     1 
ATOM   1276  O  O     . MET   A  1  193  ? -30.874 56.624  63.485  1.00 27.05 ? 191  MET   A O     1 
ATOM   1277  C  CB    . MET   A  1  193  ? -27.785 56.369  63.702  1.00 28.13 ? 191  MET   A CB    1 
ATOM   1278  C  CG    . MET   A  1  193  ? -26.562 56.012  64.522  1.00 27.47 ? 191  MET   A CG    1 
ATOM   1279  S  SD    . MET   A  1  193  ? -25.307 57.290  64.356  1.00 37.22 ? 191  MET   A SD    1 
ATOM   1280  C  CE    . MET   A  1  193  ? -25.905 58.392  65.612  1.00 32.63 ? 191  MET   A CE    1 
ATOM   1281  N  N     . GLY   A  1  194  ? -30.294 55.256  61.803  1.00 25.21 ? 192  GLY   A N     1 
ATOM   1282  C  CA    . GLY   A  1  194  ? -31.393 55.699  60.969  1.00 25.99 ? 192  GLY   A CA    1 
ATOM   1283  C  C     . GLY   A  1  194  ? -32.573 54.748  60.938  1.00 27.85 ? 192  GLY   A C     1 
ATOM   1284  O  O     . GLY   A  1  194  ? -33.673 55.147  60.541  1.00 29.28 ? 192  GLY   A O     1 
ATOM   1285  N  N     . GLU   A  1  195  ? -32.366 53.494  61.354  1.00 23.91 ? 193  GLU   A N     1 
ATOM   1286  C  CA    . GLU   A  1  195  ? -33.378 52.454  61.206  1.00 24.00 ? 193  GLU   A CA    1 
ATOM   1287  C  C     . GLU   A  1  195  ? -33.629 51.617  62.447  1.00 22.94 ? 193  GLU   A C     1 
ATOM   1288  O  O     . GLU   A  1  195  ? -34.703 51.013  62.537  1.00 21.65 ? 193  GLU   A O     1 
ATOM   1289  C  CB    . GLU   A  1  195  ? -33.015 51.490  60.067  1.00 27.13 ? 193  GLU   A CB    1 
ATOM   1290  C  CG    . GLU   A  1  195  ? -32.744 52.146  58.738  1.00 33.94 ? 193  GLU   A CG    1 
ATOM   1291  C  CD    . GLU   A  1  195  ? -32.401 51.123  57.677  1.00 41.66 ? 193  GLU   A CD    1 
ATOM   1292  O  OE1   . GLU   A  1  195  ? -32.721 49.932  57.884  1.00 43.80 ? 193  GLU   A OE1   1 
ATOM   1293  O  OE2   . GLU   A  1  195  ? -31.808 51.504  56.646  1.00 50.05 ? 193  GLU   A OE2   1 
ATOM   1294  N  N     . GLN   A  1  196  ? -32.694 51.540  63.392  1.00 25.33 ? 194  GLN   A N     1 
ATOM   1295  C  CA    . GLN   A  1  196  ? -32.877 50.713  64.579  1.00 25.40 ? 194  GLN   A CA    1 
ATOM   1296  C  C     . GLN   A  1  196  ? -33.170 51.540  65.822  1.00 25.62 ? 194  GLN   A C     1 
ATOM   1297  O  O     . GLN   A  1  196  ? -34.167 51.300  66.510  1.00 28.45 ? 194  GLN   A O     1 
ATOM   1298  C  CB    . GLN   A  1  196  ? -31.641 49.837  64.815  1.00 24.80 ? 194  GLN   A CB    1 
ATOM   1299  N  N     . PHE   A  1  197  ? -32.329 52.526  66.114  1.00 24.79 ? 195  PHE   A N     1 
ATOM   1300  C  CA    . PHE   A  1  197  ? -32.567 53.372  67.273  1.00 24.73 ? 195  PHE   A CA    1 
ATOM   1301  C  C     . PHE   A  1  197  ? -33.761 54.280  67.056  1.00 26.44 ? 195  PHE   A C     1 
ATOM   1302  O  O     . PHE   A  1  197  ? -34.357 54.757  68.026  1.00 25.59 ? 195  PHE   A O     1 
ATOM   1303  C  CB    . PHE   A  1  197  ? -31.333 54.219  67.560  1.00 25.84 ? 195  PHE   A CB    1 
ATOM   1304  C  CG    . PHE   A  1  197  ? -30.119 53.419  67.912  1.00 27.70 ? 195  PHE   A CG    1 
ATOM   1305  C  CD1   . PHE   A  1  197  ? -30.230 52.244  68.629  1.00 31.75 ? 195  PHE   A CD1   1 
ATOM   1306  C  CD2   . PHE   A  1  197  ? -28.863 53.846  67.524  1.00 29.10 ? 195  PHE   A CD2   1 
ATOM   1307  C  CE1   . PHE   A  1  197  ? -29.105 51.510  68.960  1.00 33.55 ? 195  PHE   A CE1   1 
ATOM   1308  C  CE2   . PHE   A  1  197  ? -27.737 53.114  67.852  1.00 31.99 ? 195  PHE   A CE2   1 
ATOM   1309  C  CZ    . PHE   A  1  197  ? -27.868 51.945  68.569  1.00 30.85 ? 195  PHE   A CZ    1 
ATOM   1310  N  N     . VAL   A  1  198  ? -34.097 54.553  65.802  1.00 21.74 ? 196  VAL   A N     1 
ATOM   1311  C  CA    . VAL   A  1  198  ? -35.280 55.317  65.449  1.00 21.34 ? 196  VAL   A CA    1 
ATOM   1312  C  C     . VAL   A  1  198  ? -35.969 54.577  64.320  1.00 22.40 ? 196  VAL   A C     1 
ATOM   1313  O  O     . VAL   A  1  198  ? -35.339 53.854  63.542  1.00 25.39 ? 196  VAL   A O     1 
ATOM   1314  C  CB    . VAL   A  1  198  ? -34.968 56.775  65.029  1.00 21.91 ? 196  VAL   A CB    1 
ATOM   1315  C  CG1   . VAL   A  1  198  ? -34.356 57.565  66.182  1.00 24.00 ? 196  VAL   A CG1   1 
ATOM   1316  C  CG2   . VAL   A  1  198  ? -34.069 56.798  63.808  1.00 21.67 ? 196  VAL   A CG2   1 
ATOM   1317  N  N     . THR   A  1  199  ? -37.283 54.737  64.252  1.00 21.02 ? 197  THR   A N     1 
ATOM   1318  C  CA    . THR   A  1  199  ? -38.000 54.218  63.100  1.00 20.70 ? 197  THR   A CA    1 
ATOM   1319  C  C     . THR   A  1  199  ? -37.687 55.042  61.863  1.00 24.74 ? 197  THR   A C     1 
ATOM   1320  O  O     . THR   A  1  199  ? -37.634 54.503  60.754  1.00 28.24 ? 197  THR   A O     1 
ATOM   1321  C  CB    . THR   A  1  199  ? -39.496 54.216  63.405  1.00 22.24 ? 197  THR   A CB    1 
ATOM   1322  O  OG1   . THR   A  1  199  ? -39.704 53.492  64.626  1.00 24.65 ? 197  THR   A OG1   1 
ATOM   1323  C  CG2   . THR   A  1  199  ? -40.275 53.554  62.289  1.00 25.74 ? 197  THR   A CG2   1 
ATOM   1324  N  N     . GLY   A  1  200  ? -37.462 56.334  62.036  1.00 22.25 ? 198  GLY   A N     1 
ATOM   1325  C  CA    . GLY   A  1  200  ? -37.071 57.177  60.926  1.00 23.70 ? 198  GLY   A CA    1 
ATOM   1326  C  C     . GLY   A  1  200  ? -36.520 58.483  61.442  1.00 23.00 ? 198  GLY   A C     1 
ATOM   1327  O  O     . GLY   A  1  200  ? -36.693 58.835  62.614  1.00 20.99 ? 198  GLY   A O     1 
ATOM   1328  N  N     . GLU   A  1  201  ? -35.819 59.187  60.554  1.00 23.75 ? 199  GLU   A N     1 
ATOM   1329  C  CA    . GLU   A  1  201  ? -35.246 60.468  60.941  1.00 24.52 ? 199  GLU   A CA    1 
ATOM   1330  C  C     . GLU   A  1  201  ? -36.324 61.532  61.082  1.00 24.49 ? 199  GLU   A C     1 
ATOM   1331  O  O     . GLU   A  1  201  ? -36.212 62.426  61.929  1.00 24.72 ? 199  GLU   A O     1 
ATOM   1332  C  CB    . GLU   A  1  201  ? -34.202 60.890  59.908  1.00 26.24 ? 199  GLU   A CB    1 
ATOM   1333  C  CG    . GLU   A  1  201  ? -33.493 62.194  60.209  1.00 34.62 ? 199  GLU   A CG    1 
ATOM   1334  C  CD    . GLU   A  1  201  ? -32.497 62.566  59.121  1.00 43.66 ? 199  GLU   A CD    1 
ATOM   1335  O  OE1   . GLU   A  1  201  ? -32.176 61.693  58.283  1.00 47.06 ? 199  GLU   A OE1   1 
ATOM   1336  O  OE2   . GLU   A  1  201  ? -32.040 63.729  59.102  1.00 50.63 ? 199  GLU   A OE2   1 
ATOM   1337  N  N     . THR   A  1  202  ? -37.383 61.432  60.283  1.00 23.23 ? 200  THR   A N     1 
ATOM   1338  C  CA    . THR   A  1  202  ? -38.486 62.371  60.305  1.00 22.84 ? 200  THR   A CA    1 
ATOM   1339  C  C     . THR   A  1  202  ? -39.769 61.572  60.415  1.00 21.29 ? 200  THR   A C     1 
ATOM   1340  O  O     . THR   A  1  202  ? -39.801 60.368  60.142  1.00 20.27 ? 200  THR   A O     1 
ATOM   1341  C  CB    . THR   A  1  202  ? -38.575 63.139  58.994  1.00 21.82 ? 200  THR   A CB    1 
ATOM   1342  O  OG1   . THR   A  1  202  ? -38.865 62.212  57.940  1.00 25.37 ? 200  THR   A OG1   1 
ATOM   1343  C  CG2   . THR   A  1  202  ? -37.260 63.853  58.690  1.00 26.56 ? 200  THR   A CG2   1 
ATOM   1344  N  N     . ILE   A  1  203  ? -40.845 62.260  60.788  1.00 20.89 ? 201  ILE   A N     1 
ATOM   1345  C  CA    . ILE   A  1  203  ? -42.110 61.558  60.951  1.00 20.74 ? 201  ILE   A CA    1 
ATOM   1346  C  C     . ILE   A  1  203  ? -42.566 60.963  59.626  1.00 22.12 ? 201  ILE   A C     1 
ATOM   1347  O  O     . ILE   A  1  203  ? -43.090 59.846  59.584  1.00 21.83 ? 201  ILE   A O     1 
ATOM   1348  C  CB    . ILE   A  1  203  ? -43.169 62.453  61.628  1.00 20.37 ? 201  ILE   A CB    1 
ATOM   1349  C  CG1   . ILE   A  1  203  ? -44.409 61.631  61.998  1.00 19.80 ? 201  ILE   A CG1   1 
ATOM   1350  C  CG2   . ILE   A  1  203  ? -43.560 63.634  60.733  1.00 22.49 ? 201  ILE   A CG2   1 
ATOM   1351  C  CD1   . ILE   A  1  203  ? -44.136 60.482  62.930  1.00 18.03 ? 201  ILE   A CD1   1 
ATOM   1352  N  N     . ARG   A  1  204  ? -42.311 61.662  58.514  1.00 19.79 ? 202  ARG   A N     1 
ATOM   1353  C  CA    . ARG   A  1  204  ? -42.709 61.139  57.212  1.00 22.23 ? 202  ARG   A CA    1 
ATOM   1354  C  C     . ARG   A  1  204  ? -41.973 59.852  56.886  1.00 22.54 ? 202  ARG   A C     1 
ATOM   1355  O  O     . ARG   A  1  204  ? -42.575 58.892  56.396  1.00 22.42 ? 202  ARG   A O     1 
ATOM   1356  C  CB    . ARG   A  1  204  ? -42.455 62.178  56.125  1.00 28.73 ? 202  ARG   A CB    1 
ATOM   1357  C  CG    . ARG   A  1  204  ? -43.618 63.100  55.912  1.00 34.92 ? 202  ARG   A CG    1 
ATOM   1358  C  CD    . ARG   A  1  204  ? -43.179 64.376  55.224  1.00 34.43 ? 202  ARG   A CD    1 
ATOM   1359  N  NE    . ARG   A  1  204  ? -44.285 65.320  55.147  1.00 35.79 ? 202  ARG   A NE    1 
ATOM   1360  C  CZ    . ARG   A  1  204  ? -44.737 66.028  56.173  1.00 32.99 ? 202  ARG   A CZ    1 
ATOM   1361  N  NH1   . ARG   A  1  204  ? -44.196 65.922  57.383  1.00 30.36 ? 202  ARG   A NH1   1 
ATOM   1362  N  NH2   . ARG   A  1  204  ? -45.764 66.855  55.985  1.00 27.99 ? 202  ARG   A NH2   1 
ATOM   1363  N  N     . GLU   A  1  205  ? -40.661 59.826  57.127  1.00 22.54 ? 203  GLU   A N     1 
ATOM   1364  C  CA    . GLU   A  1  205  ? -39.901 58.601  56.920  1.00 24.49 ? 203  GLU   A CA    1 
ATOM   1365  C  C     . GLU   A  1  205  ? -40.392 57.490  57.839  1.00 23.18 ? 203  GLU   A C     1 
ATOM   1366  O  O     . GLU   A  1  205  ? -40.590 56.353  57.397  1.00 23.15 ? 203  GLU   A O     1 
ATOM   1367  C  CB    . GLU   A  1  205  ? -38.420 58.878  57.150  1.00 24.05 ? 203  GLU   A CB    1 
ATOM   1368  C  CG    . GLU   A  1  205  ? -37.520 57.705  56.863  1.00 27.70 ? 203  GLU   A CG    1 
ATOM   1369  C  CD    . GLU   A  1  205  ? -36.058 58.097  56.929  1.00 31.68 ? 203  GLU   A CD    1 
ATOM   1370  O  OE1   . GLU   A  1  205  ? -35.560 58.365  58.043  1.00 31.19 ? 203  GLU   A OE1   1 
ATOM   1371  O  OE2   . GLU   A  1  205  ? -35.408 58.164  55.864  1.00 34.08 ? 203  GLU   A OE2   1 
ATOM   1372  N  N     . ALA   A  1  206  ? -40.623 57.806  59.115  1.00 21.83 ? 204  ALA   A N     1 
ATOM   1373  C  CA    . ALA   A  1  206  ? -41.116 56.795  60.043  1.00 20.82 ? 204  ALA   A CA    1 
ATOM   1374  C  C     . ALA   A  1  206  ? -42.460 56.241  59.592  1.00 21.20 ? 204  ALA   A C     1 
ATOM   1375  O  O     . ALA   A  1  206  ? -42.697 55.027  59.656  1.00 21.31 ? 204  ALA   A O     1 
ATOM   1376  C  CB    . ALA   A  1  206  ? -41.237 57.393  61.444  1.00 22.19 ? 204  ALA   A CB    1 
ATOM   1377  N  N     . LEU   A  1  207  ? -43.350 57.111  59.120  1.00 20.17 ? 205  LEU   A N     1 
ATOM   1378  C  CA    . LEU   A  1  207  ? -44.658 56.640  58.676  1.00 20.68 ? 205  LEU   A CA    1 
ATOM   1379  C  C     . LEU   A  1  207  ? -44.536 55.728  57.464  1.00 22.45 ? 205  LEU   A C     1 
ATOM   1380  O  O     . LEU   A  1  207  ? -45.218 54.702  57.379  1.00 22.56 ? 205  LEU   A O     1 
ATOM   1381  C  CB    . LEU   A  1  207  ? -45.572 57.820  58.365  1.00 20.91 ? 205  LEU   A CB    1 
ATOM   1382  C  CG    . LEU   A  1  207  ? -46.063 58.570  59.597  1.00 22.47 ? 205  LEU   A CG    1 
ATOM   1383  C  CD1   . LEU   A  1  207  ? -46.591 59.921  59.168  1.00 20.66 ? 205  LEU   A CD1   1 
ATOM   1384  C  CD2   . LEU   A  1  207  ? -47.140 57.758  60.329  1.00 20.42 ? 205  LEU   A CD2   1 
ATOM   1385  N  N     . LYS   A  1  208  ? -43.672 56.086  56.513  1.00 21.55 ? 206  LYS   A N     1 
ATOM   1386  C  CA    . LYS   A  1  208  ? -43.467 55.222  55.354  1.00 25.07 ? 206  LYS   A CA    1 
ATOM   1387  C  C     . LYS   A  1  208  ? -42.995 53.841  55.784  1.00 26.09 ? 206  LYS   A C     1 
ATOM   1388  O  O     . LYS   A  1  208  ? -43.487 52.822  55.281  1.00 27.74 ? 206  LYS   A O     1 
ATOM   1389  C  CB    . LYS   A  1  208  ? -42.465 55.857  54.388  1.00 28.93 ? 206  LYS   A CB    1 
ATOM   1390  N  N     . ARG   A  1  209  ? -42.066 53.788  56.734  1.00 24.50 ? 207  ARG   A N     1 
ATOM   1391  C  CA    . ARG   A  1  209  ? -41.507 52.528  57.202  1.00 24.81 ? 207  ARG   A CA    1 
ATOM   1392  C  C     . ARG   A  1  209  ? -42.448 51.743  58.099  1.00 26.68 ? 207  ARG   A C     1 
ATOM   1393  O  O     . ARG   A  1  209  ? -42.156 50.583  58.404  1.00 30.14 ? 207  ARG   A O     1 
ATOM   1394  C  CB    . ARG   A  1  209  ? -40.203 52.786  57.938  1.00 24.10 ? 207  ARG   A CB    1 
ATOM   1395  C  CG    . ARG   A  1  209  ? -39.123 53.290  57.007  1.00 27.07 ? 207  ARG   A CG    1 
ATOM   1396  C  CD    . ARG   A  1  209  ? -37.888 53.622  57.771  1.00 28.47 ? 207  ARG   A CD    1 
ATOM   1397  N  NE    . ARG   A  1  209  ? -36.877 54.208  56.906  1.00 29.87 ? 207  ARG   A NE    1 
ATOM   1398  C  CZ    . ARG   A  1  209  ? -35.722 54.685  57.347  1.00 30.72 ? 207  ARG   A CZ    1 
ATOM   1399  N  NH1   . ARG   A  1  209  ? -35.420 54.672  58.636  1.00 31.70 ? 207  ARG   A NH1   1 
ATOM   1400  N  NH2   . ARG   A  1  209  ? -34.852 55.187  56.475  1.00 39.45 ? 207  ARG   A NH2   1 
ATOM   1401  N  N     . SER   A  1  210  ? -43.556 52.337  58.530  1.00 26.76 ? 208  SER   A N     1 
ATOM   1402  C  CA    . SER   A  1  210  ? -44.457 51.644  59.439  1.00 23.66 ? 208  SER   A CA    1 
ATOM   1403  C  C     . SER   A  1  210  ? -45.446 50.746  58.714  1.00 24.44 ? 208  SER   A C     1 
ATOM   1404  O  O     . SER   A  1  210  ? -46.064 49.884  59.350  1.00 23.93 ? 208  SER   A O     1 
ATOM   1405  C  CB    . SER   A  1  210  ? -45.212 52.667  60.287  1.00 23.56 ? 208  SER   A CB    1 
ATOM   1406  O  OG    . SER   A  1  210  ? -44.317 53.393  61.114  1.00 23.34 ? 208  SER   A OG    1 
ATOM   1407  N  N     . LYS   A  1  211  ? -45.605 50.923  57.400  1.00 25.84 ? 209  LYS   A N     1 
ATOM   1408  C  CA    . LYS   A  1  211  ? -46.642 50.201  56.673  1.00 28.74 ? 209  LYS   A CA    1 
ATOM   1409  C  C     . LYS   A  1  211  ? -46.416 48.695  56.728  1.00 27.56 ? 209  LYS   A C     1 
ATOM   1410  O  O     . LYS   A  1  211  ? -47.374 47.919  56.828  1.00 28.88 ? 209  LYS   A O     1 
ATOM   1411  C  CB    . LYS   A  1  211  ? -46.689 50.691  55.226  1.00 29.82 ? 209  LYS   A CB    1 
ATOM   1412  N  N     . GLU   A  1  212  ? -45.152 48.268  56.699  1.00 26.58 ? 210  GLU   A N     1 
ATOM   1413  C  CA    . GLU   A  1  212  ? -44.842 46.842  56.655  1.00 30.24 ? 210  GLU   A CA    1 
ATOM   1414  C  C     . GLU   A  1  212  ? -45.420 46.110  57.860  1.00 31.12 ? 210  GLU   A C     1 
ATOM   1415  O  O     . GLU   A  1  212  ? -46.137 45.115  57.711  1.00 32.05 ? 210  GLU   A O     1 
ATOM   1416  C  CB    . GLU   A  1  212  ? -43.331 46.639  56.578  1.00 34.05 ? 210  GLU   A CB    1 
ATOM   1417  C  CG    . GLU   A  1  212  ? -42.907 45.184  56.604  1.00 39.46 ? 210  GLU   A CG    1 
ATOM   1418  C  CD    . GLU   A  1  212  ? -41.405 45.021  56.524  1.00 45.53 ? 210  GLU   A CD    1 
ATOM   1419  O  OE1   . GLU   A  1  212  ? -40.700 46.050  56.476  1.00 48.46 ? 210  GLU   A OE1   1 
ATOM   1420  O  OE2   . GLU   A  1  212  ? -40.929 43.866  56.507  1.00 55.62 ? 210  GLU   A OE2   1 
ATOM   1421  N  N     . LEU   A  1  213  ? -45.127 46.598  59.066  1.00 27.25 ? 211  LEU   A N     1 
ATOM   1422  C  CA    . LEU   A  1  213  ? -45.622 45.924  60.260  1.00 26.71 ? 211  LEU   A CA    1 
ATOM   1423  C  C     . LEU   A  1  213  ? -47.085 46.239  60.541  1.00 26.16 ? 211  LEU   A C     1 
ATOM   1424  O  O     . LEU   A  1  213  ? -47.779 45.423  61.153  1.00 25.98 ? 211  LEU   A O     1 
ATOM   1425  C  CB    . LEU   A  1  213  ? -44.736 46.243  61.464  1.00 25.78 ? 211  LEU   A CB    1 
ATOM   1426  C  CG    . LEU   A  1  213  ? -43.348 45.595  61.392  1.00 26.78 ? 211  LEU   A CG    1 
ATOM   1427  C  CD1   . LEU   A  1  213  ? -42.552 45.822  62.668  1.00 28.33 ? 211  LEU   A CD1   1 
ATOM   1428  C  CD2   . LEU   A  1  213  ? -43.476 44.103  61.100  1.00 33.45 ? 211  LEU   A CD2   1 
ATOM   1429  N  N     . GLU   A  1  214  ? -47.584 47.395  60.100  1.00 23.92 ? 212  GLU   A N     1 
ATOM   1430  C  CA    . GLU   A  1  214  ? -49.014 47.644  60.232  1.00 25.20 ? 212  GLU   A CA    1 
ATOM   1431  C  C     . GLU   A  1  214  ? -49.815 46.622  59.441  1.00 28.43 ? 212  GLU   A C     1 
ATOM   1432  O  O     . GLU   A  1  214  ? -50.875 46.171  59.889  1.00 27.87 ? 212  GLU   A O     1 
ATOM   1433  C  CB    . GLU   A  1  214  ? -49.355 49.063  59.793  1.00 23.91 ? 212  GLU   A CB    1 
ATOM   1434  C  CG    . GLU   A  1  214  ? -48.956 50.096  60.822  1.00 22.89 ? 212  GLU   A CG    1 
ATOM   1435  C  CD    . GLU   A  1  214  ? -49.334 51.495  60.425  1.00 25.49 ? 212  GLU   A CD    1 
ATOM   1436  O  OE1   . GLU   A  1  214  ? -49.657 51.716  59.240  1.00 29.35 ? 212  GLU   A OE1   1 
ATOM   1437  O  OE2   . GLU   A  1  214  ? -49.299 52.383  61.306  1.00 28.73 ? 212  GLU   A OE2   1 
ATOM   1438  N  N     . GLU   A  1  215  ? -49.307 46.231  58.268  1.00 26.78 ? 213  GLU   A N     1 
ATOM   1439  C  CA    . GLU   A  1  215  ? -49.992 45.236  57.450  1.00 30.00 ? 213  GLU   A CA    1 
ATOM   1440  C  C     . GLU   A  1  215  ? -50.016 43.870  58.116  1.00 35.53 ? 213  GLU   A C     1 
ATOM   1441  O  O     . GLU   A  1  215  ? -50.872 43.044  57.782  1.00 37.13 ? 213  GLU   A O     1 
ATOM   1442  C  CB    . GLU   A  1  215  ? -49.333 45.138  56.072  1.00 33.41 ? 213  GLU   A CB    1 
ATOM   1443  N  N     . LYS   A  1  216  ? -49.107 43.621  59.052  1.00 31.24 ? 214  LYS   A N     1 
ATOM   1444  C  CA    . LYS   A  1  216  ? -49.069 42.374  59.803  1.00 32.96 ? 214  LYS   A CA    1 
ATOM   1445  C  C     . LYS   A  1  216  ? -49.899 42.419  61.082  1.00 34.97 ? 214  LYS   A C     1 
ATOM   1446  O  O     . LYS   A  1  216  ? -50.076 41.378  61.724  1.00 39.77 ? 214  LYS   A O     1 
ATOM   1447  C  CB    . LYS   A  1  216  ? -47.619 41.996  60.125  1.00 31.39 ? 214  LYS   A CB    1 
ATOM   1448  N  N     . GLY   A  1  217  ? -50.424 43.583  61.461  1.00 28.08 ? 215  GLY   A N     1 
ATOM   1449  C  CA    . GLY   A  1  217  ? -51.254 43.712  62.641  1.00 29.35 ? 215  GLY   A CA    1 
ATOM   1450  C  C     . GLY   A  1  217  ? -50.662 44.545  63.755  1.00 25.70 ? 215  GLY   A C     1 
ATOM   1451  O  O     . GLY   A  1  217  ? -51.292 44.669  64.809  1.00 26.03 ? 215  GLY   A O     1 
ATOM   1452  N  N     . PHE   A  1  218  ? -49.472 45.102  63.576  1.00 24.09 ? 216  PHE   A N     1 
ATOM   1453  C  CA    . PHE   A  1  218  ? -48.944 46.019  64.567  1.00 19.72 ? 216  PHE   A CA    1 
ATOM   1454  C  C     . PHE   A  1  218  ? -49.554 47.399  64.374  1.00 21.52 ? 216  PHE   A C     1 
ATOM   1455  O  O     . PHE   A  1  218  ? -50.097 47.731  63.317  1.00 23.27 ? 216  PHE   A O     1 
ATOM   1456  C  CB    . PHE   A  1  218  ? -47.426 46.155  64.424  1.00 19.54 ? 216  PHE   A CB    1 
ATOM   1457  C  CG    . PHE   A  1  218  ? -46.658 44.941  64.851  1.00 22.15 ? 216  PHE   A CG    1 
ATOM   1458  C  CD1   . PHE   A  1  218  ? -46.525 43.848  64.010  1.00 27.31 ? 216  PHE   A CD1   1 
ATOM   1459  C  CD2   . PHE   A  1  218  ? -46.042 44.908  66.088  1.00 22.16 ? 216  PHE   A CD2   1 
ATOM   1460  C  CE1   . PHE   A  1  218  ? -45.813 42.739  64.409  1.00 25.02 ? 216  PHE   A CE1   1 
ATOM   1461  C  CE2   . PHE   A  1  218  ? -45.323 43.800  66.492  1.00 24.81 ? 216  PHE   A CE2   1 
ATOM   1462  C  CZ    . PHE   A  1  218  ? -45.209 42.717  65.648  1.00 23.40 ? 216  PHE   A CZ    1 
ATOM   1463  N  N     . SER   A  1  219  ? -49.442 48.214  65.410  1.00 19.21 ? 217  SER   A N     1 
ATOM   1464  C  CA    . SER   A  1  219  ? -49.727 49.636  65.322  1.00 19.34 ? 217  SER   A CA    1 
ATOM   1465  C  C     . SER   A  1  219  ? -48.514 50.385  65.846  1.00 18.88 ? 217  SER   A C     1 
ATOM   1466  O  O     . SER   A  1  219  ? -47.519 49.780  66.255  1.00 18.14 ? 217  SER   A O     1 
ATOM   1467  C  CB    . SER   A  1  219  ? -50.980 50.017  66.117  1.00 20.57 ? 217  SER   A CB    1 
ATOM   1468  O  OG    . SER   A  1  219  ? -50.805 49.685  67.479  1.00 22.74 ? 217  SER   A OG    1 
ATOM   1469  N  N     . TYR   A  1  220  ? -48.595 51.712  65.837  1.00 18.61 ? 218  TYR   A N     1 
ATOM   1470  C  CA    . TYR   A  1  220  ? -47.459 52.547  66.194  1.00 17.69 ? 218  TYR   A CA    1 
ATOM   1471  C  C     . TYR   A  1  220  ? -47.877 53.679  67.118  1.00 17.25 ? 218  TYR   A C     1 
ATOM   1472  O  O     . TYR   A  1  220  ? -49.015 54.156  67.077  1.00 18.03 ? 218  TYR   A O     1 
ATOM   1473  C  CB    . TYR   A  1  220  ? -46.820 53.150  64.939  1.00 18.76 ? 218  TYR   A CB    1 
ATOM   1474  C  CG    . TYR   A  1  220  ? -45.902 52.182  64.269  1.00 19.32 ? 218  TYR   A CG    1 
ATOM   1475  C  CD1   . TYR   A  1  220  ? -46.394 51.230  63.391  1.00 20.15 ? 218  TYR   A CD1   1 
ATOM   1476  C  CD2   . TYR   A  1  220  ? -44.542 52.199  64.534  1.00 18.49 ? 218  TYR   A CD2   1 
ATOM   1477  C  CE1   . TYR   A  1  220  ? -45.557 50.328  62.792  1.00 19.96 ? 218  TYR   A CE1   1 
ATOM   1478  C  CE2   . TYR   A  1  220  ? -43.703 51.300  63.937  1.00 18.79 ? 218  TYR   A CE2   1 
ATOM   1479  C  CZ    . TYR   A  1  220  ? -44.215 50.367  63.067  1.00 20.15 ? 218  TYR   A CZ    1 
ATOM   1480  O  OH    . TYR   A  1  220  ? -43.371 49.460  62.466  1.00 22.40 ? 218  TYR   A OH    1 
ATOM   1481  N  N     . SER   A  1  221  ? -46.938 54.090  67.966  1.00 16.96 ? 219  SER   A N     1 
ATOM   1482  C  CA    . SER   A  1  221  ? -47.040 55.333  68.717  1.00 17.10 ? 219  SER   A CA    1 
ATOM   1483  C  C     . SER   A  1  221  ? -45.714 56.051  68.528  1.00 16.51 ? 219  SER   A C     1 
ATOM   1484  O  O     . SER   A  1  221  ? -44.666 55.530  68.923  1.00 20.59 ? 219  SER   A O     1 
ATOM   1485  C  CB    . SER   A  1  221  ? -47.276 55.072  70.206  1.00 18.14 ? 219  SER   A CB    1 
ATOM   1486  O  OG    . SER   A  1  221  ? -47.380 56.313  70.881  1.00 19.38 ? 219  SER   A OG    1 
ATOM   1487  N  N     . TYR   A  1  222  ? -45.745 57.237  67.939  1.00 15.20 ? 220  TYR   A N     1 
ATOM   1488  C  CA    . TYR   A  1  222  ? -44.492 57.889  67.579  1.00 17.47 ? 220  TYR   A CA    1 
ATOM   1489  C  C     . TYR   A  1  222  ? -44.015 58.828  68.673  1.00 18.05 ? 220  TYR   A C     1 
ATOM   1490  O  O     . TYR   A  1  222  ? -44.797 59.570  69.266  1.00 17.47 ? 220  TYR   A O     1 
ATOM   1491  C  CB    . TYR   A  1  222  ? -44.621 58.640  66.255  1.00 16.09 ? 220  TYR   A CB    1 
ATOM   1492  C  CG    . TYR   A  1  222  ? -44.951 57.696  65.135  1.00 16.14 ? 220  TYR   A CG    1 
ATOM   1493  C  CD1   . TYR   A  1  222  ? -43.965 56.940  64.523  1.00 18.05 ? 220  TYR   A CD1   1 
ATOM   1494  C  CD2   . TYR   A  1  222  ? -46.265 57.527  64.722  1.00 17.16 ? 220  TYR   A CD2   1 
ATOM   1495  C  CE1   . TYR   A  1  222  ? -44.287 56.051  63.521  1.00 17.91 ? 220  TYR   A CE1   1 
ATOM   1496  C  CE2   . TYR   A  1  222  ? -46.590 56.650  63.726  1.00 18.10 ? 220  TYR   A CE2   1 
ATOM   1497  C  CZ    . TYR   A  1  222  ? -45.603 55.918  63.133  1.00 17.49 ? 220  TYR   A CZ    1 
ATOM   1498  O  OH    . TYR   A  1  222  ? -45.956 55.045  62.143  1.00 21.00 ? 220  TYR   A OH    1 
ATOM   1499  N  N     . ASP   A  1  223  ? -42.707 58.808  68.902  1.00 19.58 ? 221  ASP   A N     1 
ATOM   1500  C  CA    . ASP   A  1  223  ? -42.043 59.633  69.901  1.00 22.16 ? 221  ASP   A CA    1 
ATOM   1501  C  C     . ASP   A  1  223  ? -41.070 60.552  69.176  1.00 22.90 ? 221  ASP   A C     1 
ATOM   1502  O  O     . ASP   A  1  223  ? -40.050 60.090  68.644  1.00 22.44 ? 221  ASP   A O     1 
ATOM   1503  C  CB    . ASP   A  1  223  ? -41.288 58.725  70.860  1.00 23.72 ? 221  ASP   A CB    1 
ATOM   1504  C  CG    . ASP   A  1  223  ? -40.328 59.485  71.767  1.00 26.44 ? 221  ASP   A CG    1 
ATOM   1505  O  OD1   . ASP   A  1  223  ? -40.532 60.694  72.000  1.00 29.43 ? 221  ASP   A OD1   1 
ATOM   1506  O  OD2   . ASP   A  1  223  ? -39.363 58.854  72.242  1.00 35.35 ? 221  ASP   A OD2   1 
ATOM   1507  N  N     . MET   A  1  224  ? -41.376 61.845  69.162  1.00 21.60 ? 222  MET   A N     1 
ATOM   1508  C  CA    . MET   A  1  224  ? -40.533 62.854  68.532  1.00 23.44 ? 222  MET   A CA    1 
ATOM   1509  C  C     . MET   A  1  224  ? -39.320 63.216  69.377  1.00 25.75 ? 222  MET   A C     1 
ATOM   1510  O  O     . MET   A  1  224  ? -38.574 64.130  69.009  1.00 29.72 ? 222  MET   A O     1 
ATOM   1511  C  CB    . MET   A  1  224  ? -41.353 64.096  68.180  1.00 22.35 ? 222  MET   A CB    1 
ATOM   1512  C  CG    . MET   A  1  224  ? -42.547 63.808  67.264  1.00 24.91 ? 222  MET   A CG    1 
ATOM   1513  S  SD    . MET   A  1  224  ? -42.122 62.867  65.780  1.00 28.77 ? 222  MET   A SD    1 
ATOM   1514  C  CE    . MET   A  1  224  ? -41.000 64.015  64.996  1.00 34.62 ? 222  MET   A CE    1 
ATOM   1515  N  N     . LEU   A  1  225  ? -39.123 62.518  70.490  1.00 25.66 ? 223  LEU   A N     1 
ATOM   1516  C  CA    . LEU   A  1  225  ? -37.910 62.549  71.303  1.00 26.94 ? 223  LEU   A CA    1 
ATOM   1517  C  C     . LEU   A  1  225  ? -37.742 63.836  72.102  1.00 30.54 ? 223  LEU   A C     1 
ATOM   1518  O  O     . LEU   A  1  225  ? -36.688 64.034  72.718  1.00 33.10 ? 223  LEU   A O     1 
ATOM   1519  C  CB    . LEU   A  1  225  ? -36.643 62.190  70.508  1.00 29.85 ? 223  LEU   A CB    1 
ATOM   1520  C  CG    . LEU   A  1  225  ? -36.557 60.738  70.012  1.00 26.72 ? 223  LEU   A CG    1 
ATOM   1521  C  CD1   . LEU   A  1  225  ? -35.401 60.559  69.027  1.00 33.88 ? 223  LEU   A CD1   1 
ATOM   1522  C  CD2   . LEU   A  1  225  ? -36.416 59.756  71.172  1.00 32.23 ? 223  LEU   A CD2   1 
ATOM   1523  N  N     . GLY   A  1  226  ? -38.752 64.702  72.134  1.00 27.53 ? 224  GLY   A N     1 
ATOM   1524  C  CA    . GLY   A  1  226  ? -38.694 65.866  73.000  1.00 27.96 ? 224  GLY   A CA    1 
ATOM   1525  C  C     . GLY   A  1  226  ? -38.760 65.466  74.464  1.00 26.70 ? 224  GLY   A C     1 
ATOM   1526  O  O     . GLY   A  1  226  ? -39.501 64.564  74.855  1.00 24.91 ? 224  GLY   A O     1 
ATOM   1527  N  N     . GLU   A  1  227  ? -37.970 66.154  75.282  1.00 23.60 ? 225  GLU   A N     1 
ATOM   1528  C  CA    . GLU   A  1  227  ? -37.908 65.830  76.697  1.00 21.41 ? 225  GLU   A CA    1 
ATOM   1529  C  C     . GLU   A  1  227  ? -37.084 66.906  77.375  1.00 21.81 ? 225  GLU   A C     1 
ATOM   1530  O  O     . GLU   A  1  227  ? -36.159 67.450  76.766  1.00 20.21 ? 225  GLU   A O     1 
ATOM   1531  C  CB    . GLU   A  1  227  ? -37.218 64.475  76.860  1.00 25.72 ? 225  GLU   A CB    1 
ATOM   1532  C  CG    . GLU   A  1  227  ? -37.075 63.965  78.252  1.00 29.24 ? 225  GLU   A CG    1 
ATOM   1533  C  CD    . GLU   A  1  227  ? -36.361 62.628  78.266  1.00 37.84 ? 225  GLU   A CD    1 
ATOM   1534  O  OE1   . GLU   A  1  227  ? -36.304 61.975  77.197  1.00 31.48 ? 225  GLU   A OE1   1 
ATOM   1535  O  OE2   . GLU   A  1  227  ? -35.842 62.240  79.330  1.00 37.20 ? 225  GLU   A OE2   1 
ATOM   1536  N  N     . ALA   A  1  228  ? -37.447 67.234  78.611  1.00 20.30 ? 226  ALA   A N     1 
ATOM   1537  C  CA    . ALA   A  1  228  ? -36.629 68.081  79.477  1.00 21.08 ? 226  ALA   A CA    1 
ATOM   1538  C  C     . ALA   A  1  228  ? -36.254 69.408  78.805  1.00 18.75 ? 226  ALA   A C     1 
ATOM   1539  O  O     . ALA   A  1  228  ? -35.078 69.766  78.687  1.00 20.82 ? 226  ALA   A O     1 
ATOM   1540  C  CB    . ALA   A  1  228  ? -35.390 67.321  79.955  1.00 24.68 ? 226  ALA   A CB    1 
ATOM   1541  N  N     . ALA   A  1  229  ? -37.275 70.151  78.391  1.00 18.24 ? 227  ALA   A N     1 
ATOM   1542  C  CA    . ALA   A  1  229  ? -37.056 71.504  77.900  1.00 17.96 ? 227  ALA   A CA    1 
ATOM   1543  C  C     . ALA   A  1  229  ? -36.318 72.326  78.951  1.00 18.26 ? 227  ALA   A C     1 
ATOM   1544  O  O     . ALA   A  1  229  ? -36.656 72.296  80.137  1.00 18.46 ? 227  ALA   A O     1 
ATOM   1545  C  CB    . ALA   A  1  229  ? -38.394 72.165  77.570  1.00 17.40 ? 227  ALA   A CB    1 
ATOM   1546  N  N     . THR   A  1  230  ? -35.301 73.053  78.503  1.00 17.61 ? 228  THR   A N     1 
ATOM   1547  C  CA    . THR   A  1  230  ? -34.527 73.931  79.367  1.00 19.18 ? 228  THR   A CA    1 
ATOM   1548  C  C     . THR   A  1  230  ? -34.971 75.377  79.254  1.00 17.65 ? 228  THR   A C     1 
ATOM   1549  O  O     . THR   A  1  230  ? -34.815 76.153  80.201  1.00 17.86 ? 228  THR   A O     1 
ATOM   1550  C  CB    . THR   A  1  230  ? -33.040 73.825  78.996  1.00 21.51 ? 228  THR   A CB    1 
ATOM   1551  O  OG1   . THR   A  1  230  ? -32.646 72.445  79.040  1.00 26.46 ? 228  THR   A OG1   1 
ATOM   1552  C  CG2   . THR   A  1  230  ? -32.182 74.601  79.973  1.00 24.36 ? 228  THR   A CG2   1 
ATOM   1553  N  N     . THR   A  1  231  ? -35.550 75.753  78.122  1.00 17.72 ? 229  THR   A N     1 
ATOM   1554  C  CA    . THR   A  1  231  ? -35.915 77.135  77.870  1.00 17.19 ? 229  THR   A CA    1 
ATOM   1555  C  C     . THR   A  1  231  ? -37.299 77.156  77.258  1.00 17.28 ? 229  THR   A C     1 
ATOM   1556  O  O     . THR   A  1  231  ? -37.803 76.134  76.783  1.00 17.50 ? 229  THR   A O     1 
ATOM   1557  C  CB    . THR   A  1  231  ? -34.948 77.791  76.874  1.00 18.34 ? 229  THR   A CB    1 
ATOM   1558  O  OG1   . THR   A  1  231  ? -35.101 77.181  75.584  1.00 19.29 ? 229  THR   A OG1   1 
ATOM   1559  C  CG2   . THR   A  1  231  ? -33.502 77.620  77.328  1.00 20.43 ? 229  THR   A CG2   1 
ATOM   1560  N  N     . ALA   A  1  232  ? -37.901 78.339  77.283  1.00 17.17 ? 230  ALA   A N     1 
ATOM   1561  C  CA    . ALA   A  1  232  ? -39.158 78.528  76.571  1.00 18.49 ? 230  ALA   A CA    1 
ATOM   1562  C  C     . ALA   A  1  232  ? -39.007 78.169  75.099  1.00 18.99 ? 230  ALA   A C     1 
ATOM   1563  O  O     . ALA   A  1  232  ? -39.890 77.529  74.518  1.00 19.80 ? 230  ALA   A O     1 
ATOM   1564  C  CB    . ALA   A  1  232  ? -39.643 79.967  76.735  1.00 18.38 ? 230  ALA   A CB    1 
ATOM   1565  N  N     . ALA   A  1  233  ? -37.891 78.558  74.480  1.00 19.95 ? 231  ALA   A N     1 
ATOM   1566  C  CA    . ALA   A  1  233  ? -37.699 78.251  73.065  1.00 22.35 ? 231  ALA   A CA    1 
ATOM   1567  C  C     . ALA   A  1  233  ? -37.651 76.748  72.822  1.00 22.18 ? 231  ALA   A C     1 
ATOM   1568  O  O     . ALA   A  1  233  ? -38.211 76.258  71.833  1.00 21.69 ? 231  ALA   A O     1 
ATOM   1569  C  CB    . ALA   A  1  233  ? -36.431 78.923  72.542  1.00 24.84 ? 231  ALA   A CB    1 
ATOM   1570  N  N     . ASP   A  1  234  ? -36.990 75.998  73.709  1.00 19.78 ? 232  ASP   A N     1 
ATOM   1571  C  CA    . ASP   A  1  234  ? -36.979 74.542  73.601  1.00 21.51 ? 232  ASP   A CA    1 
ATOM   1572  C  C     . ASP   A  1  234  ? -38.394 74.006  73.658  1.00 19.03 ? 232  ASP   A C     1 
ATOM   1573  O  O     . ASP   A  1  234  ? -38.772 73.125  72.880  1.00 19.32 ? 232  ASP   A O     1 
ATOM   1574  C  CB    . ASP   A  1  234  ? -36.238 73.915  74.784  1.00 25.84 ? 232  ASP   A CB    1 
ATOM   1575  C  CG    . ASP   A  1  234  ? -34.741 74.038  74.706  1.00 33.92 ? 232  ASP   A CG    1 
ATOM   1576  O  OD1   . ASP   A  1  234  ? -34.189 74.300  73.620  1.00 29.97 ? 232  ASP   A OD1   1 
ATOM   1577  O  OD2   . ASP   A  1  234  ? -34.114 73.834  75.773  1.00 31.21 ? 232  ASP   A OD2   1 
ATOM   1578  N  N     . ALA   A  1  235  ? -39.166 74.472  74.642  1.00 18.53 ? 233  ALA   A N     1 
ATOM   1579  C  CA    . ALA   A  1  235  ? -40.521 73.981  74.814  1.00 16.63 ? 233  ALA   A CA    1 
ATOM   1580  C  C     . ALA   A  1  235  ? -41.364 74.290  73.590  1.00 20.15 ? 233  ALA   A C     1 
ATOM   1581  O  O     . ALA   A  1  235  ? -42.188 73.467  73.169  1.00 18.09 ? 233  ALA   A O     1 
ATOM   1582  C  CB    . ALA   A  1  235  ? -41.127 74.596  76.074  1.00 17.33 ? 233  ALA   A CB    1 
ATOM   1583  N  N     . GLU   A  1  236  ? -41.171 75.473  73.003  1.00 18.92 ? 234  GLU   A N     1 
ATOM   1584  C  CA    . GLU   A  1  236  ? -41.895 75.807  71.784  1.00 18.86 ? 234  GLU   A CA    1 
ATOM   1585  C  C     . GLU   A  1  236  ? -41.468 74.915  70.627  1.00 17.70 ? 234  GLU   A C     1 
ATOM   1586  O  O     . GLU   A  1  236  ? -42.309 74.498  69.824  1.00 18.88 ? 234  GLU   A O     1 
ATOM   1587  C  CB    . GLU   A  1  236  ? -41.695 77.284  71.441  1.00 22.44 ? 234  GLU   A CB    1 
ATOM   1588  C  CG    . GLU   A  1  236  ? -42.446 78.226  72.359  1.00 30.80 ? 234  GLU   A CG    1 
ATOM   1589  C  CD    . GLU   A  1  236  ? -41.741 79.555  72.578  1.00 37.30 ? 234  GLU   A CD    1 
ATOM   1590  O  OE1   . GLU   A  1  236  ? -40.817 79.881  71.801  1.00 43.94 ? 234  GLU   A OE1   1 
ATOM   1591  O  OE2   . GLU   A  1  236  ? -42.113 80.273  73.534  1.00 41.99 ? 234  GLU   A OE2   1 
ATOM   1592  N  N     . ARG   A  1  237  ? -40.175 74.613  70.520  1.00 18.42 ? 235  ARG   A N     1 
ATOM   1593  C  CA    . ARG   A  1  237  ? -39.720 73.725  69.455  1.00 18.45 ? 235  ARG   A CA    1 
ATOM   1594  C  C     . ARG   A  1  237  ? -40.316 72.335  69.620  1.00 19.04 ? 235  ARG   A C     1 
ATOM   1595  O  O     . ARG   A  1  237  ? -40.795 71.734  68.653  1.00 19.81 ? 235  ARG   A O     1 
ATOM   1596  C  CB    . ARG   A  1  237  ? -38.190 73.671  69.408  1.00 21.72 ? 235  ARG   A CB    1 
ATOM   1597  C  CG    . ARG   A  1  237  ? -37.634 72.658  68.415  1.00 29.22 ? 235  ARG   A CG    1 
ATOM   1598  C  CD    . ARG   A  1  237  ? -36.141 72.847  68.224  1.00 33.78 ? 235  ARG   A CD    1 
ATOM   1599  N  NE    . ARG   A  1  237  ? -35.444 72.783  69.502  1.00 36.89 ? 235  ARG   A NE    1 
ATOM   1600  C  CZ    . ARG   A  1  237  ? -34.943 71.674  70.027  1.00 41.57 ? 235  ARG   A CZ    1 
ATOM   1601  N  NH1   . ARG   A  1  237  ? -35.005 70.516  69.387  1.00 43.04 ? 235  ARG   A NH1   1 
ATOM   1602  N  NH2   . ARG   A  1  237  ? -34.365 71.728  71.225  1.00 38.74 ? 235  ARG   A NH2   1 
ATOM   1603  N  N     . TYR   A  1  238  ? -40.321 71.810  70.843  1.00 17.45 ? 236  TYR   A N     1 
ATOM   1604  C  CA    . TYR   A  1  238  ? -40.901 70.491  71.034  1.00 17.10 ? 236  TYR   A CA    1 
ATOM   1605  C  C     . TYR   A  1  238  ? -42.394 70.518  70.766  1.00 16.96 ? 236  TYR   A C     1 
ATOM   1606  O  O     . TYR   A  1  238  ? -42.939 69.564  70.209  1.00 18.91 ? 236  TYR   A O     1 
ATOM   1607  C  CB    . TYR   A  1  238  ? -40.619 69.990  72.447  1.00 17.35 ? 236  TYR   A CB    1 
ATOM   1608  C  CG    . TYR   A  1  238  ? -39.163 69.697  72.713  1.00 15.98 ? 236  TYR   A CG    1 
ATOM   1609  C  CD1   . TYR   A  1  238  ? -38.353 69.119  71.746  1.00 20.96 ? 236  TYR   A CD1   1 
ATOM   1610  C  CD2   . TYR   A  1  238  ? -38.605 69.983  73.945  1.00 17.62 ? 236  TYR   A CD2   1 
ATOM   1611  C  CE1   . TYR   A  1  238  ? -37.008 68.846  72.006  1.00 24.06 ? 236  TYR   A CE1   1 
ATOM   1612  C  CE2   . TYR   A  1  238  ? -37.276 69.717  74.212  1.00 20.13 ? 236  TYR   A CE2   1 
ATOM   1613  C  CZ    . TYR   A  1  238  ? -36.486 69.145  73.248  1.00 22.08 ? 236  TYR   A CZ    1 
ATOM   1614  O  OH    . TYR   A  1  238  ? -35.159 68.885  73.532  1.00 26.08 ? 236  TYR   A OH    1 
ATOM   1615  N  N     . TYR   A  1  239  ? -43.059 71.608  71.137  1.00 15.62 ? 237  TYR   A N     1 
ATOM   1616  C  CA    . TYR   A  1  239  ? -44.478 71.730  70.843  1.00 15.76 ? 237  TYR   A CA    1 
ATOM   1617  C  C     . TYR   A  1  239  ? -44.719 71.651  69.347  1.00 17.90 ? 237  TYR   A C     1 
ATOM   1618  O  O     . TYR   A  1  239  ? -45.583 70.899  68.885  1.00 16.91 ? 237  TYR   A O     1 
ATOM   1619  C  CB    . TYR   A  1  239  ? -45.039 73.034  71.392  1.00 16.54 ? 237  TYR   A CB    1 
ATOM   1620  C  CG    . TYR   A  1  239  ? -46.491 73.166  71.044  1.00 19.30 ? 237  TYR   A CG    1 
ATOM   1621  C  CD1   . TYR   A  1  239  ? -46.888 73.700  69.823  1.00 19.36 ? 237  TYR   A CD1   1 
ATOM   1622  C  CD2   . TYR   A  1  239  ? -47.471 72.700  71.905  1.00 19.64 ? 237  TYR   A CD2   1 
ATOM   1623  C  CE1   . TYR   A  1  239  ? -48.216 73.787  69.478  1.00 21.34 ? 237  TYR   A CE1   1 
ATOM   1624  C  CE2   . TYR   A  1  239  ? -48.803 72.800  71.574  1.00 19.79 ? 237  TYR   A CE2   1 
ATOM   1625  C  CZ    . TYR   A  1  239  ? -49.173 73.343  70.359  1.00 21.29 ? 237  TYR   A CZ    1 
ATOM   1626  O  OH    . TYR   A  1  239  ? -50.492 73.448  69.988  1.00 24.28 ? 237  TYR   A OH    1 
ATOM   1627  N  N     . ARG   A  1  240  ? -43.987 72.456  68.571  1.00 17.28 ? 238  ARG   A N     1 
ATOM   1628  C  CA    . ARG   A  1  240  ? -44.264 72.460  67.142  1.00 17.26 ? 238  ARG   A CA    1 
ATOM   1629  C  C     . ARG   A  1  240  ? -43.874 71.139  66.503  1.00 15.87 ? 238  ARG   A C     1 
ATOM   1630  O  O     . ARG   A  1  240  ? -44.494 70.729  65.519  1.00 17.57 ? 238  ARG   A O     1 
ATOM   1631  C  CB    . ARG   A  1  240  ? -43.649 73.673  66.441  1.00 20.73 ? 238  ARG   A CB    1 
ATOM   1632  C  CG    . ARG   A  1  240  ? -42.169 73.722  66.479  1.00 22.93 ? 238  ARG   A CG    1 
ATOM   1633  C  CD    . ARG   A  1  240  ? -41.668 74.921  65.682  1.00 21.06 ? 238  ARG   A CD    1 
ATOM   1634  N  NE    . ARG   A  1  240  ? -40.232 75.087  65.843  1.00 23.80 ? 238  ARG   A NE    1 
ATOM   1635  C  CZ    . ARG   A  1  240  ? -39.669 75.897  66.734  1.00 23.72 ? 238  ARG   A CZ    1 
ATOM   1636  N  NH1   . ARG   A  1  240  ? -40.395 76.695  67.507  1.00 22.58 ? 238  ARG   A NH1   1 
ATOM   1637  N  NH2   . ARG   A  1  240  ? -38.345 75.907  66.851  1.00 28.52 ? 238  ARG   A NH2   1 
ATOM   1638  N  N     . ASP   A  1  241  ? -42.876 70.445  67.058  1.00 16.56 ? 239  ASP   A N     1 
ATOM   1639  C  CA    . ASP   A  1  241  ? -42.562 69.101  66.588  1.00 17.02 ? 239  ASP   A CA    1 
ATOM   1640  C  C     . ASP   A  1  241  ? -43.728 68.154  66.835  1.00 18.33 ? 239  ASP   A C     1 
ATOM   1641  O  O     . ASP   A  1  241  ? -44.088 67.357  65.966  1.00 17.98 ? 239  ASP   A O     1 
ATOM   1642  C  CB    . ASP   A  1  241  ? -41.306 68.567  67.277  1.00 21.19 ? 239  ASP   A CB    1 
ATOM   1643  C  CG    . ASP   A  1  241  ? -40.029 69.184  66.739  1.00 28.03 ? 239  ASP   A CG    1 
ATOM   1644  O  OD1   . ASP   A  1  241  ? -40.104 69.979  65.775  1.00 34.38 ? 239  ASP   A OD1   1 
ATOM   1645  O  OD2   . ASP   A  1  241  ? -38.958 68.877  67.302  1.00 37.85 ? 239  ASP   A OD2   1 
ATOM   1646  N  N     . TYR   A  1  242  ? -44.325 68.214  68.024  1.00 15.78 ? 240  TYR   A N     1 
ATOM   1647  C  CA    . TYR   A  1  242  ? -45.470 67.354  68.301  1.00 15.69 ? 240  TYR   A CA    1 
ATOM   1648  C  C     . TYR   A  1  242  ? -46.646 67.711  67.409  1.00 14.95 ? 240  TYR   A C     1 
ATOM   1649  O  O     . TYR   A  1  242  ? -47.317 66.827  66.872  1.00 16.19 ? 240  TYR   A O     1 
ATOM   1650  C  CB    . TYR   A  1  242  ? -45.901 67.516  69.749  1.00 15.09 ? 240  TYR   A CB    1 
ATOM   1651  C  CG    . TYR   A  1  242  ? -45.010 66.889  70.784  1.00 14.55 ? 240  TYR   A CG    1 
ATOM   1652  C  CD1   . TYR   A  1  242  ? -44.363 65.679  70.566  1.00 16.28 ? 240  TYR   A CD1   1 
ATOM   1653  C  CD2   . TYR   A  1  242  ? -44.867 67.494  72.008  1.00 16.46 ? 240  TYR   A CD2   1 
ATOM   1654  C  CE1   . TYR   A  1  242  ? -43.571 65.111  71.572  1.00 16.48 ? 240  TYR   A CE1   1 
ATOM   1655  C  CE2   . TYR   A  1  242  ? -44.092 66.955  72.986  1.00 15.14 ? 240  TYR   A CE2   1 
ATOM   1656  C  CZ    . TYR   A  1  242  ? -43.457 65.771  72.769  1.00 15.35 ? 240  TYR   A CZ    1 
ATOM   1657  O  OH    . TYR   A  1  242  ? -42.694 65.264  73.798  1.00 16.78 ? 240  TYR   A OH    1 
ATOM   1658  N  N     . GLU   A  1  243  ? -46.897 69.003  67.235  1.00 13.98 ? 241  GLU   A N     1 
ATOM   1659  C  CA    . GLU   A  1  243  ? -48.028 69.427  66.430  1.00 14.67 ? 241  GLU   A CA    1 
ATOM   1660  C  C     . GLU   A  1  243  ? -47.849 68.979  64.988  1.00 14.68 ? 241  GLU   A C     1 
ATOM   1661  O  O     . GLU   A  1  243  ? -48.769 68.423  64.381  1.00 16.49 ? 241  GLU   A O     1 
ATOM   1662  C  CB    . GLU   A  1  243  ? -48.174 70.945  66.530  1.00 15.93 ? 241  GLU   A CB    1 
ATOM   1663  C  CG    . GLU   A  1  243  ? -49.281 71.535  65.695  1.00 20.24 ? 241  GLU   A CG    1 
ATOM   1664  C  CD    . GLU   A  1  243  ? -49.136 73.046  65.591  1.00 23.90 ? 241  GLU   A CD    1 
ATOM   1665  O  OE1   . GLU   A  1  243  ? -47.991 73.565  65.615  1.00 30.02 ? 241  GLU   A OE1   1 
ATOM   1666  O  OE2   . GLU   A  1  243  ? -50.169 73.704  65.491  1.00 22.33 ? 241  GLU   A OE2   1 
ATOM   1667  N  N     . SER   A  1  244  ? -46.651 69.175  64.438  1.00 15.73 ? 242  SER   A N     1 
ATOM   1668  C  CA    . SER   A  1  244  ? -46.404 68.734  63.069  1.00 16.52 ? 242  SER   A CA    1 
ATOM   1669  C  C     . SER   A  1  244  ? -46.491 67.216  62.953  1.00 17.25 ? 242  SER   A C     1 
ATOM   1670  O  O     . SER   A  1  244  ? -47.031 66.692  61.972  1.00 19.64 ? 242  SER   A O     1 
ATOM   1671  C  CB    . SER   A  1  244  ? -45.047 69.250  62.590  1.00 18.59 ? 242  SER   A CB    1 
ATOM   1672  O  OG    . SER   A  1  244  ? -43.978 68.661  63.303  1.00 22.88 ? 242  SER   A OG    1 
ATOM   1673  N  N     . ALA   A  1  245  ? -46.020 66.487  63.970  1.00 16.50 ? 243  ALA   A N     1 
ATOM   1674  C  CA    . ALA   A  1  245  ? -46.139 65.033  63.927  1.00 15.49 ? 243  ALA   A CA    1 
ATOM   1675  C  C     . ALA   A  1  245  ? -47.599 64.592  63.995  1.00 17.37 ? 243  ALA   A C     1 
ATOM   1676  O  O     . ALA   A  1  245  ? -48.004 63.674  63.280  1.00 16.83 ? 243  ALA   A O     1 
ATOM   1677  C  CB    . ALA   A  1  245  ? -45.308 64.381  65.031  1.00 18.40 ? 243  ALA   A CB    1 
ATOM   1678  N  N     . ILE   A  1  246  ? -48.408 65.231  64.842  1.00 15.73 ? 244  ILE   A N     1 
ATOM   1679  C  CA    . ILE   A  1  246  ? -49.822 64.867  64.907  1.00 16.35 ? 244  ILE   A CA    1 
ATOM   1680  C  C     . ILE   A  1  246  ? -50.475 65.012  63.542  1.00 19.03 ? 244  ILE   A C     1 
ATOM   1681  O  O     . ILE   A  1  246  ? -51.241 64.145  63.115  1.00 16.85 ? 244  ILE   A O     1 
ATOM   1682  C  CB    . ILE   A  1  246  ? -50.553 65.676  65.985  1.00 16.02 ? 244  ILE   A CB    1 
ATOM   1683  C  CG1   . ILE   A  1  246  ? -50.083 65.242  67.372  1.00 15.74 ? 244  ILE   A CG1   1 
ATOM   1684  C  CG2   . ILE   A  1  246  ? -52.056 65.475  65.853  1.00 17.37 ? 244  ILE   A CG2   1 
ATOM   1685  C  CD1   . ILE   A  1  246  ? -50.487 66.219  68.466  1.00 16.88 ? 244  ILE   A CD1   1 
ATOM   1686  N  N     . HIS   A  1  247  ? -50.166 66.092  62.821  1.00 17.27 ? 245  HIS   A N     1 
ATOM   1687  C  CA    . HIS   A  1  247  ? -50.740 66.248  61.489  1.00 17.32 ? 245  HIS   A CA    1 
ATOM   1688  C  C     . HIS   A  1  247  ? -50.320 65.105  60.584  1.00 16.74 ? 245  HIS   A C     1 
ATOM   1689  O  O     . HIS   A  1  247  ? -51.148 64.526  59.876  1.00 17.12 ? 245  HIS   A O     1 
ATOM   1690  C  CB    . HIS   A  1  247  ? -50.310 67.575  60.871  1.00 18.32 ? 245  HIS   A CB    1 
ATOM   1691  C  CG    . HIS   A  1  247  ? -50.983 68.762  61.472  1.00 19.34 ? 245  HIS   A CG    1 
ATOM   1692  N  ND1   . HIS   A  1  247  ? -52.339 68.971  61.382  1.00 19.05 ? 245  HIS   A ND1   1 
ATOM   1693  C  CD2   . HIS   A  1  247  ? -50.481 69.818  62.155  1.00 21.15 ? 245  HIS   A CD2   1 
ATOM   1694  C  CE1   . HIS   A  1  247  ? -52.648 70.101  61.993  1.00 21.71 ? 245  HIS   A CE1   1 
ATOM   1695  N  NE2   . HIS   A  1  247  ? -51.538 70.629  62.475  1.00 20.91 ? 245  HIS   A NE2   1 
ATOM   1696  N  N     . ALA   A  1  248  ? -49.036 64.770  60.583  1.00 16.75 ? 246  ALA   A N     1 
ATOM   1697  C  CA    . ALA   A  1  248  ? -48.571 63.715  59.692  1.00 16.81 ? 246  ALA   A CA    1 
ATOM   1698  C  C     . ALA   A  1  248  ? -49.175 62.375  60.078  1.00 17.53 ? 246  ALA   A C     1 
ATOM   1699  O  O     . ALA   A  1  248  ? -49.639 61.622  59.215  1.00 18.15 ? 246  ALA   A O     1 
ATOM   1700  C  CB    . ALA   A  1  248  ? -47.040 63.659  59.697  1.00 18.03 ? 246  ALA   A CB    1 
ATOM   1701  N  N     . ILE   A  1  249  ? -49.208 62.081  61.378  1.00 17.98 ? 247  ILE   A N     1 
ATOM   1702  C  CA    . ILE   A  1  249  ? -49.771 60.825  61.855  1.00 16.89 ? 247  ILE   A CA    1 
ATOM   1703  C  C     . ILE   A  1  249  ? -51.266 60.779  61.588  1.00 16.59 ? 247  ILE   A C     1 
ATOM   1704  O  O     . ILE   A  1  249  ? -51.804 59.746  61.180  1.00 17.87 ? 247  ILE   A O     1 
ATOM   1705  C  CB    . ILE   A  1  249  ? -49.463 60.666  63.352  1.00 17.11 ? 247  ILE   A CB    1 
ATOM   1706  C  CG1   . ILE   A  1  249  ? -47.963 60.529  63.576  1.00 15.86 ? 247  ILE   A CG1   1 
ATOM   1707  C  CG2   . ILE   A  1  249  ? -50.191 59.454  63.925  1.00 17.08 ? 247  ILE   A CG2   1 
ATOM   1708  C  CD1   . ILE   A  1  249  ? -47.563 60.850  65.009  1.00 18.00 ? 247  ILE   A CD1   1 
ATOM   1709  N  N     . GLY   A  1  250  ? -51.963 61.889  61.830  1.00 15.94 ? 248  GLY   A N     1 
ATOM   1710  C  CA    . GLY   A  1  250  ? -53.390 61.924  61.587  1.00 17.16 ? 248  GLY   A CA    1 
ATOM   1711  C  C     . GLY   A  1  250  ? -53.733 61.792  60.117  1.00 17.78 ? 248  GLY   A C     1 
ATOM   1712  O  O     . GLY   A  1  250  ? -54.709 61.129  59.759  1.00 17.82 ? 248  GLY   A O     1 
ATOM   1713  N  N     . LYS   A  1  251  ? -52.955 62.441  59.249  1.00 17.93 ? 249  LYS   A N     1 
ATOM   1714  C  CA    . LYS   A  1  251  ? -53.170 62.288  57.815  1.00 20.30 ? 249  LYS   A CA    1 
ATOM   1715  C  C     . LYS   A  1  251  ? -52.988 60.841  57.399  1.00 19.98 ? 249  LYS   A C     1 
ATOM   1716  O  O     . LYS   A  1  251  ? -53.749 60.326  56.571  1.00 21.19 ? 249  LYS   A O     1 
ATOM   1717  C  CB    . LYS   A  1  251  ? -52.174 63.143  57.041  1.00 20.15 ? 249  LYS   A CB    1 
ATOM   1718  C  CG    . LYS   A  1  251  ? -52.433 64.631  57.073  1.00 21.32 ? 249  LYS   A CG    1 
ATOM   1719  C  CD    . LYS   A  1  251  ? -51.209 65.310  56.495  1.00 21.91 ? 249  LYS   A CD    1 
ATOM   1720  C  CE    . LYS   A  1  251  ? -51.305 66.821  56.569  1.00 21.20 ? 249  LYS   A CE    1 
ATOM   1721  N  NZ    . LYS   A  1  251  ? -50.050 67.406  56.003  1.00 21.54 ? 249  LYS   A NZ    1 
ATOM   1722  N  N     . ALA   A  1  252  ? -51.973 60.175  57.961  1.00 19.86 ? 250  ALA   A N     1 
ATOM   1723  C  CA    . ALA   A  1  252  ? -51.685 58.790  57.614  1.00 20.93 ? 250  ALA   A CA    1 
ATOM   1724  C  C     . ALA   A  1  252  ? -52.679 57.840  58.253  1.00 21.49 ? 250  ALA   A C     1 
ATOM   1725  O  O     . ALA   A  1  252  ? -53.038 56.820  57.653  1.00 21.39 ? 250  ALA   A O     1 
ATOM   1726  C  CB    . ALA   A  1  252  ? -50.278 58.427  58.075  1.00 21.19 ? 250  ALA   A CB    1 
ATOM   1727  N  N     . SER   A  1  253  ? -53.124 58.146  59.471  1.00 20.62 ? 251  SER   A N     1 
ATOM   1728  C  CA    . SER   A  1  253  ? -54.118 57.298  60.108  1.00 18.43 ? 251  SER   A CA    1 
ATOM   1729  C  C     . SER   A  1  253  ? -55.345 57.171  59.229  1.00 20.99 ? 251  SER   A C     1 
ATOM   1730  O  O     . SER   A  1  253  ? -55.898 56.076  59.074  1.00 21.63 ? 251  SER   A O     1 
ATOM   1731  C  CB    . SER   A  1  253  ? -54.505 57.884  61.457  1.00 19.00 ? 251  SER   A CB    1 
ATOM   1732  O  OG    . SER   A  1  253  ? -55.532 57.109  62.045  1.00 20.31 ? 251  SER   A OG    1 
ATOM   1733  N  N     . ALA   A  1  254  ? -55.766 58.284  58.632  1.00 19.49 ? 252  ALA   A N     1 
ATOM   1734  C  CA    . ALA   A  1  254  ? -56.829 58.309  57.635  1.00 22.04 ? 252  ALA   A CA    1 
ATOM   1735  C  C     . ALA   A  1  254  ? -58.084 57.610  58.144  1.00 22.81 ? 252  ALA   A C     1 
ATOM   1736  O  O     . ALA   A  1  254  ? -58.685 56.772  57.465  1.00 22.61 ? 252  ALA   A O     1 
ATOM   1737  C  CB    . ALA   A  1  254  ? -56.356 57.742  56.295  1.00 23.87 ? 252  ALA   A CB    1 
ATOM   1738  N  N     . GLY   A  1  255  ? -58.471 57.939  59.371  1.00 23.42 ? 253  GLY   A N     1 
ATOM   1739  C  CA    . GLY   A  1  255  ? -59.707 57.417  59.907  1.00 22.16 ? 253  GLY   A CA    1 
ATOM   1740  C  C     . GLY   A  1  255  ? -59.641 56.023  60.487  1.00 20.15 ? 253  GLY   A C     1 
ATOM   1741  O  O     . GLY   A  1  255  ? -60.686 55.466  60.826  1.00 24.52 ? 253  GLY   A O     1 
ATOM   1742  N  N     . ARG   A  1  256  ? -58.449 55.441  60.634  1.00 21.18 ? 254  ARG   A N     1 
ATOM   1743  C  CA    . ARG   A  1  256  ? -58.358 54.123  61.255  1.00 20.96 ? 254  ARG   A CA    1 
ATOM   1744  C  C     . ARG   A  1  256  ? -58.722 54.141  62.731  1.00 21.47 ? 254  ARG   A C     1 
ATOM   1745  O  O     . ARG   A  1  256  ? -59.011 53.084  63.299  1.00 22.70 ? 254  ARG   A O     1 
ATOM   1746  C  CB    . ARG   A  1  256  ? -56.956 53.552  61.079  1.00 20.07 ? 254  ARG   A CB    1 
ATOM   1747  C  CG    . ARG   A  1  256  ? -56.765 52.875  59.738  1.00 23.89 ? 254  ARG   A CG    1 
ATOM   1748  C  CD    . ARG   A  1  256  ? -55.354 52.385  59.598  1.00 26.21 ? 254  ARG   A CD    1 
ATOM   1749  N  NE    . ARG   A  1  256  ? -54.436 53.484  59.344  1.00 21.65 ? 254  ARG   A NE    1 
ATOM   1750  C  CZ    . ARG   A  1  256  ? -53.119 53.352  59.292  1.00 23.65 ? 254  ARG   A CZ    1 
ATOM   1751  N  NH1   . ARG   A  1  256  ? -52.534 52.197  59.565  1.00 26.76 ? 254  ARG   A NH1   1 
ATOM   1752  N  NH2   . ARG   A  1  256  ? -52.374 54.395  58.936  1.00 24.46 ? 254  ARG   A NH2   1 
ATOM   1753  N  N     . GLY   A  1  257  ? -58.709 55.305  63.370  1.00 20.69 ? 255  GLY   A N     1 
ATOM   1754  C  CA    . GLY   A  1  257  ? -59.091 55.386  64.762  1.00 19.51 ? 255  GLY   A CA    1 
ATOM   1755  C  C     . GLY   A  1  257  ? -57.950 55.080  65.711  1.00 17.37 ? 255  GLY   A C     1 
ATOM   1756  O  O     . GLY   A  1  257  ? -56.805 54.816  65.334  1.00 18.60 ? 255  GLY   A O     1 
ATOM   1757  N  N     . ILE   A  1  258  ? -58.287 55.092  66.995  1.00 16.41 ? 256  ILE   A N     1 
ATOM   1758  C  CA    . ILE   A  1  258  ? -57.246 55.116  68.011  1.00 17.98 ? 256  ILE   A CA    1 
ATOM   1759  C  C     . ILE   A  1  258  ? -56.659 53.749  68.309  1.00 19.51 ? 256  ILE   A C     1 
ATOM   1760  O  O     . ILE   A  1  258  ? -55.564 53.678  68.876  1.00 18.21 ? 256  ILE   A O     1 
ATOM   1761  C  CB    . ILE   A  1  258  ? -57.756 55.775  69.296  1.00 18.61 ? 256  ILE   A CB    1 
ATOM   1762  C  CG1   . ILE   A  1  258  ? -58.882 54.938  69.908  1.00 19.94 ? 256  ILE   A CG1   1 
ATOM   1763  C  CG2   . ILE   A  1  258  ? -58.165 57.222  69.015  1.00 17.37 ? 256  ILE   A CG2   1 
ATOM   1764  C  CD1   . ILE   A  1  258  ? -59.452 55.547  71.167  1.00 19.89 ? 256  ILE   A CD1   1 
ATOM   1765  N  N     . TYR   A  1  259  ? -57.345 52.663  67.964  1.00 20.45 ? 257  TYR   A N     1 
ATOM   1766  C  CA    . TYR   A  1  259  ? -56.829 51.337  68.276  1.00 20.67 ? 257  TYR   A CA    1 
ATOM   1767  C  C     . TYR   A  1  259  ? -56.067 50.729  67.110  1.00 21.01 ? 257  TYR   A C     1 
ATOM   1768  O  O     . TYR   A  1  259  ? -54.928 50.283  67.281  1.00 24.33 ? 257  TYR   A O     1 
ATOM   1769  C  CB    . TYR   A  1  259  ? -57.959 50.414  68.736  1.00 22.31 ? 257  TYR   A CB    1 
ATOM   1770  C  CG    . TYR   A  1  259  ? -58.761 51.015  69.858  1.00 20.92 ? 257  TYR   A CG    1 
ATOM   1771  C  CD1   . TYR   A  1  259  ? -58.174 51.293  71.085  1.00 21.94 ? 257  TYR   A CD1   1 
ATOM   1772  C  CD2   . TYR   A  1  259  ? -60.105 51.323  69.691  1.00 20.23 ? 257  TYR   A CD2   1 
ATOM   1773  C  CE1   . TYR   A  1  259  ? -58.904 51.858  72.112  1.00 21.53 ? 257  TYR   A CE1   1 
ATOM   1774  C  CE2   . TYR   A  1  259  ? -60.840 51.888  70.711  1.00 24.04 ? 257  TYR   A CE2   1 
ATOM   1775  C  CZ    . TYR   A  1  259  ? -60.233 52.150  71.920  1.00 20.62 ? 257  TYR   A CZ    1 
ATOM   1776  O  OH    . TYR   A  1  259  ? -60.964 52.727  72.927  1.00 21.65 ? 257  TYR   A OH    1 
ATOM   1777  N  N     . GLU   A  1  260  ? -56.664 50.728  65.916  1.00 20.50 ? 258  GLU   A N     1 
ATOM   1778  C  CA    . GLU   A  1  260  ? -55.954 50.214  64.752  1.00 25.39 ? 258  GLU   A CA    1 
ATOM   1779  C  C     . GLU   A  1  260  ? -54.910 51.196  64.243  1.00 24.05 ? 258  GLU   A C     1 
ATOM   1780  O  O     . GLU   A  1  260  ? -53.853 50.781  63.757  1.00 29.18 ? 258  GLU   A O     1 
ATOM   1781  C  CB    . GLU   A  1  260  ? -56.924 49.902  63.609  1.00 27.03 ? 258  GLU   A CB    1 
ATOM   1782  C  CG    . GLU   A  1  260  ? -56.223 49.200  62.440  1.00 35.08 ? 258  GLU   A CG    1 
ATOM   1783  C  CD    . GLU   A  1  260  ? -57.003 49.234  61.136  1.00 38.42 ? 258  GLU   A CD    1 
ATOM   1784  O  OE1   . GLU   A  1  260  ? -58.251 49.324  61.176  1.00 43.47 ? 258  GLU   A OE1   1 
ATOM   1785  O  OE2   . GLU   A  1  260  ? -56.357 49.165  60.066  1.00 38.98 ? 258  GLU   A OE2   1 
ATOM   1786  N  N     . GLY   A  1  261  ? -55.173 52.490  64.364  1.00 19.87 ? 259  GLY   A N     1 
ATOM   1787  C  CA    . GLY   A  1  261  ? -54.334 53.480  63.749  1.00 17.78 ? 259  GLY   A CA    1 
ATOM   1788  C  C     . GLY   A  1  261  ? -53.252 53.987  64.676  1.00 18.69 ? 259  GLY   A C     1 
ATOM   1789  O  O     . GLY   A  1  261  ? -53.257 53.744  65.886  1.00 18.15 ? 259  GLY   A O     1 
ATOM   1790  N  N     . PRO   A  1  262  ? -52.302 54.709  64.104  1.00 16.69 ? 260  PRO   A N     1 
ATOM   1791  C  CA    . PRO   A  1  262  ? -51.145 55.175  64.872  1.00 16.73 ? 260  PRO   A CA    1 
ATOM   1792  C  C     . PRO   A  1  262  ? -51.523 56.311  65.804  1.00 17.55 ? 260  PRO   A C     1 
ATOM   1793  O  O     . PRO   A  1  262  ? -52.540 56.987  65.639  1.00 19.06 ? 260  PRO   A O     1 
ATOM   1794  C  CB    . PRO   A  1  262  ? -50.192 55.679  63.787  1.00 18.54 ? 260  PRO   A CB    1 
ATOM   1795  C  CG    . PRO   A  1  262  ? -51.129 56.081  62.661  1.00 19.11 ? 260  PRO   A CG    1 
ATOM   1796  C  CD    . PRO   A  1  262  ? -52.206 55.051  62.679  1.00 19.57 ? 260  PRO   A CD    1 
ATOM   1797  N  N     . GLY   A  1  263  ? -50.667 56.518  66.798  1.00 16.05 ? 261  GLY   A N     1 
ATOM   1798  C  CA    . GLY   A  1  263  ? -50.827 57.632  67.701  1.00 16.01 ? 261  GLY   A CA    1 
ATOM   1799  C  C     . GLY   A  1  263  ? -49.491 58.287  67.977  1.00 14.41 ? 261  GLY   A C     1 
ATOM   1800  O  O     . GLY   A  1  263  ? -48.480 57.989  67.323  1.00 15.13 ? 261  GLY   A O     1 
ATOM   1801  N  N     . ILE   A  1  264  ? -49.480 59.194  68.945  1.00 14.49 ? 262  ILE   A N     1 
ATOM   1802  C  CA    . ILE   A  1  264  ? -48.275 59.912  69.317  1.00 15.26 ? 262  ILE   A CA    1 
ATOM   1803  C  C     . ILE   A  1  264  ? -48.112 59.778  70.822  1.00 15.07 ? 262  ILE   A C     1 
ATOM   1804  O  O     . ILE   A  1  264  ? -49.085 59.580  71.557  1.00 16.33 ? 262  ILE   A O     1 
ATOM   1805  C  CB    . ILE   A  1  264  ? -48.340 61.393  68.867  1.00 15.73 ? 262  ILE   A CB    1 
ATOM   1806  C  CG1   . ILE   A  1  264  ? -46.966 62.041  68.932  1.00 17.44 ? 262  ILE   A CG1   1 
ATOM   1807  C  CG2   . ILE   A  1  264  ? -49.357 62.184  69.712  1.00 17.31 ? 262  ILE   A CG2   1 
ATOM   1808  C  CD1   . ILE   A  1  264  ? -46.953 63.443  68.327  1.00 18.60 ? 262  ILE   A CD1   1 
ATOM   1809  N  N     . SER   A  1  265  ? -46.871 59.874  71.272  1.00 14.05 ? 263  SER   A N     1 
ATOM   1810  C  CA    . SER   A  1  265  ? -46.546 59.934  72.686  1.00 16.03 ? 263  SER   A CA    1 
ATOM   1811  C  C     . SER   A  1  265  ? -45.798 61.226  72.937  1.00 16.77 ? 263  SER   A C     1 
ATOM   1812  O  O     . SER   A  1  265  ? -44.922 61.599  72.150  1.00 19.28 ? 263  SER   A O     1 
ATOM   1813  C  CB    . SER   A  1  265  ? -45.650 58.779  73.102  1.00 18.00 ? 263  SER   A CB    1 
ATOM   1814  O  OG    . SER   A  1  265  ? -46.353 57.553  73.103  1.00 19.31 ? 263  SER   A OG    1 
ATOM   1815  N  N     . ILE   A  1  266  ? -46.125 61.893  74.041  1.00 16.04 ? 264  ILE   A N     1 
ATOM   1816  C  CA    . ILE   A  1  266  ? -45.497 63.154  74.410  1.00 17.05 ? 264  ILE   A CA    1 
ATOM   1817  C  C     . ILE   A  1  266  ? -44.952 63.035  75.824  1.00 16.86 ? 264  ILE   A C     1 
ATOM   1818  O  O     . ILE   A  1  266  ? -45.383 62.196  76.618  1.00 16.71 ? 264  ILE   A O     1 
ATOM   1819  C  CB    . ILE   A  1  266  ? -46.456 64.359  74.317  1.00 15.93 ? 264  ILE   A CB    1 
ATOM   1820  C  CG1   . ILE   A  1  266  ? -47.574 64.258  75.365  1.00 17.98 ? 264  ILE   A CG1   1 
ATOM   1821  C  CG2   . ILE   A  1  266  ? -47.060 64.474  72.923  1.00 17.90 ? 264  ILE   A CG2   1 
ATOM   1822  C  CD1   . ILE   A  1  266  ? -48.389 65.529  75.477  1.00 19.52 ? 264  ILE   A CD1   1 
ATOM   1823  N  N     . LYS   A  1  267  ? -43.993 63.895  76.137  1.00 15.68 ? 265  LYS   A N     1 
ATOM   1824  C  CA    . LYS   A  1  267  ? -43.500 64.042  77.497  1.00 14.63 ? 265  LYS   A CA    1 
ATOM   1825  C  C     . LYS   A  1  267  ? -43.824 65.440  77.969  1.00 15.93 ? 265  LYS   A C     1 
ATOM   1826  O  O     . LYS   A  1  267  ? -43.506 66.420  77.283  1.00 16.20 ? 265  LYS   A O     1 
ATOM   1827  C  CB    . LYS   A  1  267  ? -41.993 63.816  77.556  1.00 15.85 ? 265  LYS   A CB    1 
ATOM   1828  C  CG    . LYS   A  1  267  ? -41.649 62.353  77.476  1.00 17.43 ? 265  LYS   A CG    1 
ATOM   1829  C  CD    . LYS   A  1  267  ? -40.145 62.140  77.502  1.00 20.75 ? 265  LYS   A CD    1 
ATOM   1830  C  CE    . LYS   A  1  267  ? -39.824 60.659  77.431  1.00 23.57 ? 265  LYS   A CE    1 
ATOM   1831  N  NZ    . LYS   A  1  267  ? -40.401 60.036  76.210  1.00 29.77 ? 265  LYS   A NZ    1 
ATOM   1832  N  N     . LEU   A  1  268  ? -44.496 65.533  79.111  1.00 14.31 ? 266  LEU   A N     1 
ATOM   1833  C  CA    . LEU   A  1  268  ? -44.840 66.846  79.634  1.00 15.09 ? 266  LEU   A CA    1 
ATOM   1834  C  C     . LEU   A  1  268  ? -43.604 67.698  79.858  1.00 15.46 ? 266  LEU   A C     1 
ATOM   1835  O  O     . LEU   A  1  268  ? -43.660 68.919  79.681  1.00 15.48 ? 266  LEU   A O     1 
ATOM   1836  C  CB    . LEU   A  1  268  ? -45.651 66.710  80.921  1.00 17.08 ? 266  LEU   A CB    1 
ATOM   1837  C  CG    . LEU   A  1  268  ? -47.001 66.012  80.715  1.00 16.63 ? 266  LEU   A CG    1 
ATOM   1838  C  CD1   . LEU   A  1  268  ? -47.760 65.916  82.009  1.00 17.28 ? 266  LEU   A CD1   1 
ATOM   1839  C  CD2   . LEU   A  1  268  ? -47.828 66.727  79.656  1.00 19.19 ? 266  LEU   A CD2   1 
ATOM   1840  N  N     . SER   A  1  269  ? -42.480 67.085  80.221  1.00 15.87 ? 267  SER   A N     1 
ATOM   1841  C  CA    . SER   A  1  269  ? -41.274 67.869  80.454  1.00 16.17 ? 267  SER   A CA    1 
ATOM   1842  C  C     . SER   A  1  269  ? -40.758 68.521  79.184  1.00 18.40 ? 267  SER   A C     1 
ATOM   1843  O  O     . SER   A  1  269  ? -39.954 69.453  79.269  1.00 16.93 ? 267  SER   A O     1 
ATOM   1844  C  CB    . SER   A  1  269  ? -40.173 67.003  81.047  1.00 18.07 ? 267  SER   A CB    1 
ATOM   1845  O  OG    . SER   A  1  269  ? -39.677 66.086  80.093  1.00 16.98 ? 267  SER   A OG    1 
ATOM   1846  N  N     . ALA   A  1  270  ? -41.170 68.029  78.011  1.00 15.56 ? 268  ALA   A N     1 
ATOM   1847  C  CA    . ALA   A  1  270  ? -40.785 68.686  76.768  1.00 16.16 ? 268  ALA   A CA    1 
ATOM   1848  C  C     . ALA   A  1  270  ? -41.539 69.983  76.544  1.00 16.36 ? 268  ALA   A C     1 
ATOM   1849  O  O     . ALA   A  1  270  ? -41.087 70.827  75.760  1.00 17.34 ? 268  ALA   A O     1 
ATOM   1850  C  CB    . ALA   A  1  270  ? -41.063 67.758  75.586  1.00 17.26 ? 268  ALA   A CB    1 
ATOM   1851  N  N     . LEU   A  1  271  ? -42.677 70.159  77.204  1.00 15.34 ? 269  LEU   A N     1 
ATOM   1852  C  CA    . LEU   A  1  271  ? -43.604 71.227  76.859  1.00 16.72 ? 269  LEU   A CA    1 
ATOM   1853  C  C     . LEU   A  1  271  ? -43.521 72.419  77.788  1.00 16.15 ? 269  LEU   A C     1 
ATOM   1854  O  O     . LEU   A  1  271  ? -44.209 73.415  77.560  1.00 17.64 ? 269  LEU   A O     1 
ATOM   1855  C  CB    . LEU   A  1  271  ? -45.029 70.698  76.796  1.00 16.36 ? 269  LEU   A CB    1 
ATOM   1856  C  CG    . LEU   A  1  271  ? -45.234 69.721  75.648  1.00 18.16 ? 269  LEU   A CG    1 
ATOM   1857  C  CD1   . LEU   A  1  271  ? -46.624 69.124  75.753  1.00 21.45 ? 269  LEU   A CD1   1 
ATOM   1858  C  CD2   . LEU   A  1  271  ? -45.081 70.476  74.350  1.00 20.10 ? 269  LEU   A CD2   1 
ATOM   1859  N  N     . HIS   A  1  272  ? -42.675 72.353  78.813  1.00 16.23 ? 270  HIS   A N     1 
ATOM   1860  C  CA    . HIS   A  1  272  ? -42.509 73.530  79.633  1.00 15.85 ? 270  HIS   A CA    1 
ATOM   1861  C  C     . HIS   A  1  272  ? -41.164 73.396  80.311  1.00 16.64 ? 270  HIS   A C     1 
ATOM   1862  O  O     . HIS   A  1  272  ? -40.843 72.306  80.796  1.00 17.39 ? 270  HIS   A O     1 
ATOM   1863  C  CB    . HIS   A  1  272  ? -43.603 73.632  80.693  1.00 18.25 ? 270  HIS   A CB    1 
ATOM   1864  C  CG    . HIS   A  1  272  ? -43.710 74.990  81.292  1.00 19.13 ? 270  HIS   A CG    1 
ATOM   1865  N  ND1   . HIS   A  1  272  ? -42.794 75.481  82.197  1.00 19.40 ? 270  HIS   A ND1   1 
ATOM   1866  C  CD2   . HIS   A  1  272  ? -44.617 75.975  81.098  1.00 21.48 ? 270  HIS   A CD2   1 
ATOM   1867  C  CE1   . HIS   A  1  272  ? -43.124 76.719  82.522  1.00 19.55 ? 270  HIS   A CE1   1 
ATOM   1868  N  NE2   . HIS   A  1  272  ? -44.232 77.038  81.875  1.00 22.44 ? 270  HIS   A NE2   1 
ATOM   1869  N  N     . PRO   A  1  273  ? -40.382 74.471  80.404  1.00 17.30 ? 271  PRO   A N     1 
ATOM   1870  C  CA    . PRO   A  1  273  ? -39.066 74.369  81.037  1.00 16.53 ? 271  PRO   A CA    1 
ATOM   1871  C  C     . PRO   A  1  273  ? -39.116 74.276  82.549  1.00 16.44 ? 271  PRO   A C     1 
ATOM   1872  O  O     . PRO   A  1  273  ? -38.082 74.001  83.156  1.00 17.90 ? 271  PRO   A O     1 
ATOM   1873  C  CB    . PRO   A  1  273  ? -38.372 75.662  80.596  1.00 18.00 ? 271  PRO   A CB    1 
ATOM   1874  C  CG    . PRO   A  1  273  ? -39.489 76.630  80.417  1.00 18.43 ? 271  PRO   A CG    1 
ATOM   1875  C  CD    . PRO   A  1  273  ? -40.623 75.811  79.844  1.00 19.05 ? 271  PRO   A CD    1 
ATOM   1876  N  N     . ARG   A  1  274  ? -40.269 74.492  83.178  1.00 16.10 ? 272  ARG   A N     1 
ATOM   1877  C  CA    . ARG   A  1  274  ? -40.389 74.418  84.632  1.00 16.56 ? 272  ARG   A CA    1 
ATOM   1878  C  C     . ARG   A  1  274  ? -41.510 73.470  85.020  1.00 17.44 ? 272  ARG   A C     1 
ATOM   1879  O  O     . ARG   A  1  274  ? -42.433 73.815  85.765  1.00 19.19 ? 272  ARG   A O     1 
ATOM   1880  C  CB    . ARG   A  1  274  ? -40.632 75.790  85.234  1.00 17.16 ? 272  ARG   A CB    1 
ATOM   1881  C  CG    . ARG   A  1  274  ? -39.497 76.763  84.979  1.00 18.25 ? 272  ARG   A CG    1 
ATOM   1882  C  CD    . ARG   A  1  274  ? -38.148 76.245  85.498  1.00 17.51 ? 272  ARG   A CD    1 
ATOM   1883  N  NE    . ARG   A  1  274  ? -38.195 75.835  86.897  1.00 18.39 ? 272  ARG   A NE    1 
ATOM   1884  C  CZ    . ARG   A  1  274  ? -38.179 76.675  87.925  1.00 16.52 ? 272  ARG   A CZ    1 
ATOM   1885  N  NH1   . ARG   A  1  274  ? -38.142 77.983  87.747  1.00 18.86 ? 272  ARG   A NH1   1 
ATOM   1886  N  NH2   . ARG   A  1  274  ? -38.162 76.188  89.161  1.00 19.96 ? 272  ARG   A NH2   1 
ATOM   1887  N  N     . TYR   A  1  275  ? -41.427 72.248  84.515  1.00 16.31 ? 273  TYR   A N     1 
ATOM   1888  C  CA    . TYR   A  1  275  ? -42.437 71.240  84.795  1.00 15.60 ? 273  TYR   A CA    1 
ATOM   1889  C  C     . TYR   A  1  275  ? -42.043 70.582  86.108  1.00 17.31 ? 273  TYR   A C     1 
ATOM   1890  O  O     . TYR   A  1  275  ? -41.246 69.648  86.151  1.00 16.84 ? 273  TYR   A O     1 
ATOM   1891  C  CB    . TYR   A  1  275  ? -42.512 70.260  83.634  1.00 17.45 ? 273  TYR   A CB    1 
ATOM   1892  C  CG    . TYR   A  1  275  ? -43.415 69.100  83.914  1.00 15.18 ? 273  TYR   A CG    1 
ATOM   1893  C  CD1   . TYR   A  1  275  ? -44.716 69.307  84.361  1.00 16.26 ? 273  TYR   A CD1   1 
ATOM   1894  C  CD2   . TYR   A  1  275  ? -42.977 67.796  83.729  1.00 16.14 ? 273  TYR   A CD2   1 
ATOM   1895  C  CE1   . TYR   A  1  275  ? -45.545 68.242  84.624  1.00 18.91 ? 273  TYR   A CE1   1 
ATOM   1896  C  CE2   . TYR   A  1  275  ? -43.807 66.721  83.991  1.00 16.41 ? 273  TYR   A CE2   1 
ATOM   1897  C  CZ    . TYR   A  1  275  ? -45.089 66.958  84.441  1.00 16.32 ? 273  TYR   A CZ    1 
ATOM   1898  O  OH    . TYR   A  1  275  ? -45.929 65.908  84.709  1.00 17.67 ? 273  TYR   A OH    1 
ATOM   1899  N  N     . SER   A  1  276  ? -42.611 71.094  87.197  1.00 14.99 ? 274  SER   A N     1 
ATOM   1900  C  CA    . SER   A  1  276  ? -42.320 70.567  88.517  1.00 14.04 ? 274  SER   A CA    1 
ATOM   1901  C  C     . SER   A  1  276  ? -43.443 70.980  89.446  1.00 15.90 ? 274  SER   A C     1 
ATOM   1902  O  O     . SER   A  1  276  ? -44.165 71.950  89.186  1.00 17.12 ? 274  SER   A O     1 
ATOM   1903  C  CB    . SER   A  1  276  ? -40.997 71.109  89.055  1.00 19.06 ? 274  SER   A CB    1 
ATOM   1904  O  OG    . SER   A  1  276  ? -41.119 72.485  89.348  1.00 21.73 ? 274  SER   A OG    1 
ATOM   1905  N  N     . ARG   A  1  277  ? -43.573 70.227  90.542  1.00 16.60 ? 275  ARG   A N     1 
ATOM   1906  C  CA    . ARG   A  1  277  ? -44.566 70.559  91.558  1.00 16.58 ? 275  ARG   A CA    1 
ATOM   1907  C  C     . ARG   A  1  277  ? -44.340 71.959  92.117  1.00 16.52 ? 275  ARG   A C     1 
ATOM   1908  O  O     . ARG   A  1  277  ? -45.298 72.671  92.417  1.00 16.54 ? 275  ARG   A O     1 
ATOM   1909  C  CB    . ARG   A  1  277  ? -44.545 69.516  92.675  1.00 16.77 ? 275  ARG   A CB    1 
ATOM   1910  C  CG    . ARG   A  1  277  ? -45.415 69.870  93.885  1.00 16.52 ? 275  ARG   A CG    1 
ATOM   1911  C  CD    . ARG   A  1  277  ? -46.886 70.076  93.498  1.00 16.34 ? 275  ARG   A CD    1 
ATOM   1912  N  NE    . ARG   A  1  277  ? -47.713 70.388  94.656  1.00 15.94 ? 275  ARG   A NE    1 
ATOM   1913  C  CZ    . ARG   A  1  277  ? -47.897 71.611  95.131  1.00 15.90 ? 275  ARG   A CZ    1 
ATOM   1914  N  NH1   . ARG   A  1  277  ? -47.302 72.661  94.589  1.00 17.98 ? 275  ARG   A NH1   1 
ATOM   1915  N  NH2   . ARG   A  1  277  ? -48.711 71.789  96.175  1.00 17.48 ? 275  ARG   A NH2   1 
ATOM   1916  N  N     . ALA   A  1  278  ? -43.075 72.372  92.261  1.00 16.43 ? 276  ALA   A N     1 
ATOM   1917  C  CA    . ALA   A  1  278  ? -42.812 73.703  92.800  1.00 16.16 ? 276  ALA   A CA    1 
ATOM   1918  C  C     . ALA   A  1  278  ? -43.384 74.790  91.915  1.00 18.21 ? 276  ALA   A C     1 
ATOM   1919  O  O     . ALA   A  1  278  ? -43.694 75.880  92.399  1.00 20.03 ? 276  ALA   A O     1 
ATOM   1920  C  CB    . ALA   A  1  278  ? -41.306 73.918  92.944  1.00 18.10 ? 276  ALA   A CB    1 
ATOM   1921  N  N     . GLN   A  1  279  ? -43.514 74.518  90.621  1.00 15.83 ? 277  GLN   A N     1 
ATOM   1922  C  CA    . GLN   A  1  279  ? -44.044 75.473  89.658  1.00 15.88 ? 277  GLN   A CA    1 
ATOM   1923  C  C     . GLN   A  1  279  ? -45.425 75.061  89.173  1.00 17.89 ? 277  GLN   A C     1 
ATOM   1924  O  O     . GLN   A  1  279  ? -45.800 75.352  88.036  1.00 17.62 ? 277  GLN   A O     1 
ATOM   1925  C  CB    . GLN   A  1  279  ? -43.081 75.630  88.481  1.00 17.24 ? 277  GLN   A CB    1 
ATOM   1926  C  CG    . GLN   A  1  279  ? -41.695 76.092  88.896  1.00 18.42 ? 277  GLN   A CG    1 
ATOM   1927  C  CD    . GLN   A  1  279  ? -41.724 77.485  89.453  1.00 21.97 ? 277  GLN   A CD    1 
ATOM   1928  O  OE1   . GLN   A  1  279  ? -42.464 78.343  88.973  1.00 30.11 ? 277  GLN   A OE1   1 
ATOM   1929  N  NE2   . GLN   A  1  279  ? -40.943 77.718  90.497  1.00 19.53 ? 277  GLN   A NE2   1 
ATOM   1930  N  N     . ALA   A  1  280  ? -46.194 74.401  90.042  1.00 17.41 ? 278  ALA   A N     1 
ATOM   1931  C  CA    . ALA   A  1  280  ? -47.476 73.839  89.627  1.00 17.25 ? 278  ALA   A CA    1 
ATOM   1932  C  C     . ALA   A  1  280  ? -48.381 74.887  89.003  1.00 17.87 ? 278  ALA   A C     1 
ATOM   1933  O  O     . ALA   A  1  280  ? -49.100 74.591  88.044  1.00 17.81 ? 278  ALA   A O     1 
ATOM   1934  C  CB    . ALA   A  1  280  ? -48.181 73.182  90.811  1.00 19.26 ? 278  ALA   A CB    1 
ATOM   1935  N  N     . ALA   A  1  281  ? -48.392 76.105  89.541  1.00 17.10 ? 279  ALA   A N     1 
ATOM   1936  C  CA    . ALA   A  1  281  ? -49.269 77.128  88.974  1.00 18.70 ? 279  ALA   A CA    1 
ATOM   1937  C  C     . ALA   A  1  281  ? -48.884 77.453  87.536  1.00 18.60 ? 279  ALA   A C     1 
ATOM   1938  O  O     . ALA   A  1  281  ? -49.754 77.581  86.663  1.00 19.20 ? 279  ALA   A O     1 
ATOM   1939  C  CB    . ALA   A  1  281  ? -49.287 78.387  89.847  1.00 20.15 ? 279  ALA   A CB    1 
ATOM   1940  N  N     . ARG   A  1  282  ? -47.585 77.569  87.259  1.00 17.88 ? 280  ARG   A N     1 
ATOM   1941  C  CA    . ARG   A  1  282  ? -47.174 77.784  85.876  1.00 17.39 ? 280  ARG   A CA    1 
ATOM   1942  C  C     . ARG   A  1  282  ? -47.486 76.569  85.021  1.00 17.29 ? 280  ARG   A C     1 
ATOM   1943  O  O     . ARG   A  1  282  ? -47.837 76.706  83.844  1.00 18.20 ? 280  ARG   A O     1 
ATOM   1944  C  CB    . ARG   A  1  282  ? -45.684 78.119  85.800  1.00 18.04 ? 280  ARG   A CB    1 
ATOM   1945  C  CG    . ARG   A  1  282  ? -45.335 79.450  86.416  1.00 20.88 ? 280  ARG   A CG    1 
ATOM   1946  C  CD    . ARG   A  1  282  ? -43.899 79.807  86.056  1.00 20.43 ? 280  ARG   A CD    1 
ATOM   1947  N  NE    . ARG   A  1  282  ? -43.784 79.960  84.612  1.00 20.26 ? 280  ARG   A NE    1 
ATOM   1948  C  CZ    . ARG   A  1  282  ? -42.647 79.941  83.931  1.00 20.22 ? 280  ARG   A CZ    1 
ATOM   1949  N  NH1   . ARG   A  1  282  ? -41.478 79.797  84.535  1.00 20.27 ? 280  ARG   A NH1   1 
ATOM   1950  N  NH2   . ARG   A  1  282  ? -42.686 80.086  82.610  1.00 21.29 ? 280  ARG   A NH2   1 
ATOM   1951  N  N     . VAL   A  1  283  ? -47.352 75.370  85.583  1.00 16.28 ? 281  VAL   A N     1 
ATOM   1952  C  CA    . VAL   A  1  283  ? -47.672 74.165  84.827  1.00 15.75 ? 281  VAL   A CA    1 
ATOM   1953  C  C     . VAL   A  1  283  ? -49.135 74.173  84.405  1.00 17.61 ? 281  VAL   A C     1 
ATOM   1954  O  O     . VAL   A  1  283  ? -49.462 73.951  83.234  1.00 16.96 ? 281  VAL   A O     1 
ATOM   1955  C  CB    . VAL   A  1  283  ? -47.317 72.917  85.643  1.00 15.73 ? 281  VAL   A CB    1 
ATOM   1956  C  CG1   . VAL   A  1  283  ? -47.891 71.675  84.983  1.00 18.99 ? 281  VAL   A CG1   1 
ATOM   1957  C  CG2   . VAL   A  1  283  ? -45.815 72.815  85.748  1.00 17.09 ? 281  VAL   A CG2   1 
ATOM   1958  N  N     . MET   A  1  284  ? -50.040 74.449  85.346  1.00 16.21 ? 282  MET   A N     1 
ATOM   1959  C  CA    . MET   A  1  284  ? -51.458 74.444  85.002  1.00 16.09 ? 282  MET   A CA    1 
ATOM   1960  C  C     . MET   A  1  284  ? -51.822 75.614  84.106  1.00 18.58 ? 282  MET   A C     1 
ATOM   1961  O  O     . MET   A  1  284  ? -52.733 75.501  83.280  1.00 20.95 ? 282  MET   A O     1 
ATOM   1962  C  CB    . MET   A  1  284  ? -52.297 74.466  86.275  1.00 17.76 ? 282  MET   A CB    1 
ATOM   1963  C  CG    . MET   A  1  284  ? -52.025 73.289  87.186  1.00 18.53 ? 282  MET   A CG    1 
ATOM   1964  S  SD    . MET   A  1  284  ? -52.213 71.671  86.426  1.00 20.67 ? 282  MET   A SD    1 
ATOM   1965  C  CE    . MET   A  1  284  ? -53.963 71.649  86.091  1.00 21.08 ? 282  MET   A CE    1 
ATOM   1966  N  N     . GLY   A  1  285  ? -51.142 76.748  84.255  1.00 17.82 ? 283  GLY   A N     1 
ATOM   1967  C  CA    . GLY   A  1  285  ? -51.494 77.906  83.458  1.00 18.65 ? 283  GLY   A CA    1 
ATOM   1968  C  C     . GLY   A  1  285  ? -50.882 77.909  82.078  1.00 18.24 ? 283  GLY   A C     1 
ATOM   1969  O  O     . GLY   A  1  285  ? -51.454 78.483  81.145  1.00 19.91 ? 283  GLY   A O     1 
ATOM   1970  N  N     . GLU   A  1  286  ? -49.718 77.296  81.922  1.00 17.56 ? 284  GLU   A N     1 
ATOM   1971  C  CA    . GLU   A  1  286  ? -48.935 77.421  80.699  1.00 16.30 ? 284  GLU   A CA    1 
ATOM   1972  C  C     . GLU   A  1  286  ? -48.716 76.101  79.990  1.00 18.75 ? 284  GLU   A C     1 
ATOM   1973  O  O     . GLU   A  1  286  ? -48.723 76.058  78.760  1.00 20.24 ? 284  GLU   A O     1 
ATOM   1974  C  CB    . GLU   A  1  286  ? -47.569 78.045  81.005  1.00 17.18 ? 284  GLU   A CB    1 
ATOM   1975  C  CG    . GLU   A  1  286  ? -47.664 79.403  81.658  1.00 20.27 ? 284  GLU   A CG    1 
ATOM   1976  C  CD    . GLU   A  1  286  ? -46.328 79.877  82.196  1.00 22.30 ? 284  GLU   A CD    1 
ATOM   1977  O  OE1   . GLU   A  1  286  ? -45.299 79.504  81.608  1.00 24.27 ? 284  GLU   A OE1   1 
ATOM   1978  O  OE2   . GLU   A  1  286  ? -46.318 80.636  83.190  1.00 25.18 ? 284  GLU   A OE2   1 
ATOM   1979  N  N     . LEU   A  1  287  ? -48.463 75.024  80.727  1.00 15.75 ? 285  LEU   A N     1 
ATOM   1980  C  CA    A LEU   A  1  287  ? -48.258 73.729  80.095  0.67 16.66 ? 285  LEU   A CA    1 
ATOM   1981  C  CA    B LEU   A  1  287  ? -48.260 73.730  80.096  0.33 16.69 ? 285  LEU   A CA    1 
ATOM   1982  C  C     . LEU   A  1  287  ? -49.589 73.107  79.695  1.00 18.52 ? 285  LEU   A C     1 
ATOM   1983  O  O     . LEU   A  1  287  ? -49.741 72.623  78.567  1.00 17.11 ? 285  LEU   A O     1 
ATOM   1984  C  CB    A LEU   A  1  287  ? -47.482 72.804  81.040  0.67 17.51 ? 285  LEU   A CB    1 
ATOM   1985  C  CB    B LEU   A  1  287  ? -47.485 72.810  81.040  0.33 17.52 ? 285  LEU   A CB    1 
ATOM   1986  C  CG    A LEU   A  1  287  ? -46.653 71.661  80.447  0.67 17.90 ? 285  LEU   A CG    1 
ATOM   1987  C  CG    B LEU   A  1  287  ? -47.563 71.315  80.746  0.33 18.62 ? 285  LEU   A CG    1 
ATOM   1988  C  CD1   A LEU   A  1  287  ? -45.819 71.019  81.523  0.67 16.30 ? 285  LEU   A CD1   1 
ATOM   1989  C  CD1   B LEU   A  1  287  ? -47.071 71.018  79.365  0.33 19.95 ? 285  LEU   A CD1   1 
ATOM   1990  C  CD2   A LEU   A  1  287  ? -47.514 70.613  79.818  0.67 21.61 ? 285  LEU   A CD2   1 
ATOM   1991  C  CD2   B LEU   A  1  287  ? -46.758 70.536  81.765  0.33 17.39 ? 285  LEU   A CD2   1 
ATOM   1992  N  N     . LEU   A  1  288  ? -50.552 73.098  80.607  1.00 18.28 ? 286  LEU   A N     1 
ATOM   1993  C  CA    . LEU   A  1  288  ? -51.858 72.508  80.321  1.00 16.90 ? 286  LEU   A CA    1 
ATOM   1994  C  C     . LEU   A  1  288  ? -52.470 72.991  79.011  1.00 18.12 ? 286  LEU   A C     1 
ATOM   1995  O  O     . LEU   A  1  288  ? -52.882 72.138  78.206  1.00 17.36 ? 286  LEU   A O     1 
ATOM   1996  C  CB    . LEU   A  1  288  ? -52.785 72.685  81.529  1.00 20.32 ? 286  LEU   A CB    1 
ATOM   1997  C  CG    . LEU   A  1  288  ? -54.255 72.328  81.303  1.00 22.91 ? 286  LEU   A CG    1 
ATOM   1998  C  CD1   . LEU   A  1  288  ? -54.417 70.844  81.009  1.00 23.37 ? 286  LEU   A CD1   1 
ATOM   1999  C  CD2   . LEU   A  1  288  ? -55.057 72.754  82.523  1.00 29.29 ? 286  LEU   A CD2   1 
ATOM   2000  N  N     . PRO   A  1  289  ? -52.552 74.294  78.722  1.00 16.88 ? 287  PRO   A N     1 
ATOM   2001  C  CA    . PRO   A  1  289  ? -53.147 74.702  77.437  1.00 16.62 ? 287  PRO   A CA    1 
ATOM   2002  C  C     . PRO   A  1  289  ? -52.416 74.158  76.234  1.00 18.87 ? 287  PRO   A C     1 
ATOM   2003  O  O     . PRO   A  1  289  ? -53.036 73.942  75.184  1.00 17.36 ? 287  PRO   A O     1 
ATOM   2004  C  CB    . PRO   A  1  289  ? -53.088 76.232  77.485  1.00 19.59 ? 287  PRO   A CB    1 
ATOM   2005  C  CG    . PRO   A  1  289  ? -53.070 76.558  78.932  1.00 26.51 ? 287  PRO   A CG    1 
ATOM   2006  C  CD    . PRO   A  1  289  ? -52.258 75.468  79.565  1.00 18.97 ? 287  PRO   A CD    1 
ATOM   2007  N  N     . ARG   A  1  290  ? -51.107 73.960  76.338  1.00 15.92 ? 288  ARG   A N     1 
ATOM   2008  C  CA    . ARG   A  1  290  ? -50.363 73.369  75.237  1.00 16.27 ? 288  ARG   A CA    1 
ATOM   2009  C  C     . ARG   A  1  290  ? -50.751 71.918  75.027  1.00 15.42 ? 288  ARG   A C     1 
ATOM   2010  O  O     . ARG   A  1  290  ? -50.957 71.486  73.888  1.00 16.20 ? 288  ARG   A O     1 
ATOM   2011  C  CB    . ARG   A  1  290  ? -48.865 73.501  75.480  1.00 17.38 ? 288  ARG   A CB    1 
ATOM   2012  C  CG    . ARG   A  1  290  ? -48.445 74.928  75.519  1.00 19.08 ? 288  ARG   A CG    1 
ATOM   2013  C  CD    . ARG   A  1  290  ? -47.017 75.065  75.979  1.00 21.00 ? 288  ARG   A CD    1 
ATOM   2014  N  NE    . ARG   A  1  290  ? -46.679 76.476  76.105  1.00 26.36 ? 288  ARG   A NE    1 
ATOM   2015  C  CZ    . ARG   A  1  290  ? -45.714 76.938  76.887  1.00 26.89 ? 288  ARG   A CZ    1 
ATOM   2016  N  NH1   . ARG   A  1  290  ? -44.941 76.121  77.584  1.00 22.85 ? 288  ARG   A NH1   1 
ATOM   2017  N  NH2   . ARG   A  1  290  ? -45.537 78.252  76.990  1.00 28.97 ? 288  ARG   A NH2   1 
ATOM   2018  N  N     . VAL   A  1  291  ? -50.853 71.145  76.111  1.00 15.40 ? 289  VAL   A N     1 
ATOM   2019  C  CA    . VAL   A  1  291  ? -51.316 69.769  75.964  1.00 15.90 ? 289  VAL   A CA    1 
ATOM   2020  C  C     . VAL   A  1  291  ? -52.723 69.745  75.397  1.00 15.11 ? 289  VAL   A C     1 
ATOM   2021  O  O     . VAL   A  1  291  ? -53.045 68.915  74.539  1.00 15.82 ? 289  VAL   A O     1 
ATOM   2022  C  CB    . VAL   A  1  291  ? -51.251 69.009  77.298  1.00 15.09 ? 289  VAL   A CB    1 
ATOM   2023  C  CG1   . VAL   A  1  291  ? -51.579 67.553  77.067  1.00 17.13 ? 289  VAL   A CG1   1 
ATOM   2024  C  CG2   . VAL   A  1  291  ? -49.892 69.137  77.892  1.00 17.99 ? 289  VAL   A CG2   1 
ATOM   2025  N  N     . LYS   A  1  292  ? -53.578 70.643  75.872  1.00 14.90 ? 290  LYS   A N     1 
ATOM   2026  C  CA    . LYS   A  1  292  ? -54.939 70.680  75.370  1.00 13.42 ? 290  LYS   A CA    1 
ATOM   2027  C  C     . LYS   A  1  292  ? -54.953 70.950  73.873  1.00 16.57 ? 290  LYS   A C     1 
ATOM   2028  O  O     . LYS   A  1  292  ? -55.687 70.296  73.123  1.00 15.11 ? 290  LYS   A O     1 
ATOM   2029  C  CB    . LYS   A  1  292  ? -55.733 71.736  76.123  1.00 15.69 ? 290  LYS   A CB    1 
ATOM   2030  C  CG    . LYS   A  1  292  ? -57.156 71.807  75.602  1.00 16.66 ? 290  LYS   A CG    1 
ATOM   2031  C  CD    . LYS   A  1  292  ? -57.977 72.886  76.226  1.00 17.24 ? 290  LYS   A CD    1 
ATOM   2032  C  CE    . LYS   A  1  292  ? -59.343 72.919  75.556  1.00 19.29 ? 290  LYS   A CE    1 
ATOM   2033  N  NZ    . LYS   A  1  292  ? -60.284 73.728  76.363  1.00 20.22 ? 290  LYS   A NZ    1 
ATOM   2034  N  N     . ALA   A  1  293  ? -54.136 71.902  73.411  1.00 15.14 ? 291  ALA   A N     1 
ATOM   2035  C  CA    . ALA   A  1  293  ? -54.111 72.196  71.986  1.00 15.35 ? 291  ALA   A CA    1 
ATOM   2036  C  C     . ALA   A  1  293  ? -53.670 70.982  71.177  1.00 15.54 ? 291  ALA   A C     1 
ATOM   2037  O  O     . ALA   A  1  293  ? -54.246 70.684  70.126  1.00 16.73 ? 291  ALA   A O     1 
ATOM   2038  C  CB    . ALA   A  1  293  ? -53.221 73.411  71.720  1.00 16.38 ? 291  ALA   A CB    1 
ATOM   2039  N  N     . LEU   A  1  294  ? -52.660 70.257  71.655  1.00 14.02 ? 292  LEU   A N     1 
ATOM   2040  C  CA    . LEU   A  1  294  ? -52.251 69.048  70.956  1.00 14.98 ? 292  LEU   A CA    1 
ATOM   2041  C  C     . LEU   A  1  294  ? -53.342 67.997  71.014  1.00 16.39 ? 292  LEU   A C     1 
ATOM   2042  O  O     . LEU   A  1  294  ? -53.611 67.322  70.015  1.00 15.11 ? 292  LEU   A O     1 
ATOM   2043  C  CB    . LEU   A  1  294  ? -50.961 68.495  71.559  1.00 16.42 ? 292  LEU   A CB    1 
ATOM   2044  C  CG    . LEU   A  1  294  ? -49.755 69.415  71.429  1.00 15.04 ? 292  LEU   A CG    1 
ATOM   2045  C  CD1   . LEU   A  1  294  ? -48.604 68.859  72.227  1.00 16.43 ? 292  LEU   A CD1   1 
ATOM   2046  C  CD2   . LEU   A  1  294  ? -49.353 69.586  69.975  1.00 17.46 ? 292  LEU   A CD2   1 
ATOM   2047  N  N     . ALA   A  1  295  ? -53.984 67.855  72.173  1.00 14.37 ? 293  ALA   A N     1 
ATOM   2048  C  CA    . ALA   A  1  295  ? -55.051 66.871  72.296  1.00 15.45 ? 293  ALA   A CA    1 
ATOM   2049  C  C     . ALA   A  1  295  ? -56.217 67.193  71.377  1.00 15.07 ? 293  ALA   A C     1 
ATOM   2050  O  O     . ALA   A  1  295  ? -56.816 66.286  70.798  1.00 15.23 ? 293  ALA   A O     1 
ATOM   2051  C  CB    . ALA   A  1  295  ? -55.522 66.792  73.742  1.00 15.95 ? 293  ALA   A CB    1 
ATOM   2052  N  N     . LEU   A  1  296  ? -56.533 68.476  71.213  1.00 13.69 ? 294  LEU   A N     1 
ATOM   2053  C  CA    . LEU   A  1  296  ? -57.615 68.853  70.307  1.00 14.11 ? 294  LEU   A CA    1 
ATOM   2054  C  C     . LEU   A  1  296  ? -57.304 68.434  68.882  1.00 14.90 ? 294  LEU   A C     1 
ATOM   2055  O  O     . LEU   A  1  296  ? -58.199 68.022  68.137  1.00 16.43 ? 294  LEU   A O     1 
ATOM   2056  C  CB    . LEU   A  1  296  ? -57.843 70.357  70.361  1.00 15.15 ? 294  LEU   A CB    1 
ATOM   2057  C  CG    . LEU   A  1  296  ? -58.568 70.871  71.596  1.00 17.27 ? 294  LEU   A CG    1 
ATOM   2058  C  CD1   . LEU   A  1  296  ? -58.484 72.390  71.642  1.00 17.36 ? 294  LEU   A CD1   1 
ATOM   2059  C  CD2   . LEU   A  1  296  ? -60.032 70.435  71.576  1.00 19.24 ? 294  LEU   A CD2   1 
ATOM   2060  N  N     . LEU   A  1  297  ? -56.042 68.548  68.478  1.00 14.94 ? 295  LEU   A N     1 
ATOM   2061  C  CA    . LEU   A  1  297  ? -55.661 68.115  67.139  1.00 16.17 ? 295  LEU   A CA    1 
ATOM   2062  C  C     . LEU   A  1  297  ? -55.722 66.596  67.024  1.00 15.93 ? 295  LEU   A C     1 
ATOM   2063  O  O     . LEU   A  1  297  ? -56.217 66.062  66.025  1.00 16.27 ? 295  LEU   A O     1 
ATOM   2064  C  CB    . LEU   A  1  297  ? -54.265 68.649  66.799  1.00 17.19 ? 295  LEU   A CB    1 
ATOM   2065  C  CG    . LEU   A  1  297  ? -53.894 68.561  65.323  1.00 23.02 ? 295  LEU   A CG    1 
ATOM   2066  C  CD1   . LEU   A  1  297  ? -54.866 69.384  64.469  1.00 24.77 ? 295  LEU   A CD1   1 
ATOM   2067  C  CD2   . LEU   A  1  297  ? -52.467 69.040  65.164  1.00 23.06 ? 295  LEU   A CD2   1 
ATOM   2068  N  N     . ALA   A  1  298  ? -55.251 65.880  68.050  1.00 14.29 ? 296  ALA   A N     1 
ATOM   2069  C  CA    . ALA   A  1  298  ? -55.367 64.428  68.039  1.00 14.96 ? 296  ALA   A CA    1 
ATOM   2070  C  C     . ALA   A  1  298  ? -56.825 64.003  67.977  1.00 16.14 ? 296  ALA   A C     1 
ATOM   2071  O  O     . ALA   A  1  298  ? -57.163 63.043  67.274  1.00 16.99 ? 296  ALA   A O     1 
ATOM   2072  C  CB    . ALA   A  1  298  ? -54.675 63.835  69.266  1.00 15.62 ? 296  ALA   A CB    1 
ATOM   2073  N  N     . LYS   A  1  299  ? -57.696 64.708  68.707  1.00 14.61 ? 297  LYS   A N     1 
ATOM   2074  C  CA    A LYS   A  1  299  ? -59.130 64.443  68.634  0.70 14.67 ? 297  LYS   A CA    1 
ATOM   2075  C  CA    B LYS   A  1  299  ? -59.127 64.440  68.633  0.30 14.73 ? 297  LYS   A CA    1 
ATOM   2076  C  C     . LYS   A  1  299  ? -59.644 64.611  67.212  1.00 16.98 ? 297  LYS   A C     1 
ATOM   2077  O  O     . LYS   A  1  299  ? -60.414 63.776  66.718  1.00 18.28 ? 297  LYS   A O     1 
ATOM   2078  C  CB    A LYS   A  1  299  ? -59.883 65.375  69.583  0.70 16.55 ? 297  LYS   A CB    1 
ATOM   2079  C  CB    B LYS   A  1  299  ? -59.873 65.364  69.596  0.30 16.58 ? 297  LYS   A CB    1 
ATOM   2080  C  CG    A LYS   A  1  299  ? -61.376 65.449  69.302  0.70 16.81 ? 297  LYS   A CG    1 
ATOM   2081  C  CG    B LYS   A  1  299  ? -61.372 65.421  69.377  0.30 16.83 ? 297  LYS   A CG    1 
ATOM   2082  C  CD    A LYS   A  1  299  ? -62.082 66.359  70.287  0.70 17.41 ? 297  LYS   A CD    1 
ATOM   2083  C  CD    B LYS   A  1  299  ? -62.042 66.264  70.447  0.30 17.48 ? 297  LYS   A CD    1 
ATOM   2084  C  CE    A LYS   A  1  299  ? -63.434 66.798  69.752  0.70 18.02 ? 297  LYS   A CE    1 
ATOM   2085  C  CE    B LYS   A  1  299  ? -63.470 66.595  70.063  0.30 19.02 ? 297  LYS   A CE    1 
ATOM   2086  N  NZ    A LYS   A  1  299  ? -64.229 67.448  70.821  0.70 19.42 ? 297  LYS   A NZ    1 
ATOM   2087  N  NZ    B LYS   A  1  299  ? -63.529 67.364  68.798  0.30 21.37 ? 297  LYS   A NZ    1 
ATOM   2088  N  N     . ASN   A  1  300  ? -59.229 65.681  66.531  1.00 17.19 ? 298  ASN   A N     1 
ATOM   2089  C  CA    . ASN   A  1  300  ? -59.771 65.901  65.199  1.00 15.68 ? 298  ASN   A CA    1 
ATOM   2090  C  C     . ASN   A  1  300  ? -59.381 64.789  64.237  1.00 17.61 ? 298  ASN   A C     1 
ATOM   2091  O  O     . ASN   A  1  300  ? -60.187 64.379  63.393  1.00 20.98 ? 298  ASN   A O     1 
ATOM   2092  C  CB    . ASN   A  1  300  ? -59.408 67.271  64.649  1.00 18.15 ? 298  ASN   A CB    1 
ATOM   2093  C  CG    . ASN   A  1  300  ? -60.207 67.596  63.412  1.00 26.00 ? 298  ASN   A CG    1 
ATOM   2094  O  OD1   . ASN   A  1  300  ? -61.365 68.017  63.496  1.00 31.89 ? 298  ASN   A OD1   1 
ATOM   2095  N  ND2   . ASN   A  1  300  ? -59.619 67.357  62.264  1.00 24.43 ? 298  ASN   A ND2   1 
ATOM   2096  N  N     . TYR   A  1  301  ? -58.156 64.290  64.342  1.00 17.03 ? 299  TYR   A N     1 
ATOM   2097  C  CA    . TYR   A  1  301  ? -57.732 63.184  63.498  1.00 17.49 ? 299  TYR   A CA    1 
ATOM   2098  C  C     . TYR   A  1  301  ? -58.125 61.831  64.062  1.00 16.53 ? 299  TYR   A C     1 
ATOM   2099  O  O     . TYR   A  1  301  ? -57.957 60.821  63.368  1.00 18.79 ? 299  TYR   A O     1 
ATOM   2100  C  CB    . TYR   A  1  301  ? -56.217 63.202  63.357  1.00 16.86 ? 299  TYR   A CB    1 
ATOM   2101  C  CG    . TYR   A  1  301  ? -55.679 64.284  62.465  1.00 17.16 ? 299  TYR   A CG    1 
ATOM   2102  C  CD1   . TYR   A  1  301  ? -55.888 64.247  61.091  1.00 18.74 ? 299  TYR   A CD1   1 
ATOM   2103  C  CD2   . TYR   A  1  301  ? -54.924 65.319  62.989  1.00 17.78 ? 299  TYR   A CD2   1 
ATOM   2104  C  CE1   . TYR   A  1  301  ? -55.364 65.224  60.269  1.00 18.44 ? 299  TYR   A CE1   1 
ATOM   2105  C  CE2   . TYR   A  1  301  ? -54.388 66.303  62.177  1.00 18.31 ? 299  TYR   A CE2   1 
ATOM   2106  C  CZ    . TYR   A  1  301  ? -54.613 66.254  60.810  1.00 19.52 ? 299  TYR   A CZ    1 
ATOM   2107  O  OH    . TYR   A  1  301  ? -54.073 67.233  59.993  1.00 20.75 ? 299  TYR   A OH    1 
ATOM   2108  N  N     . ASP   A  1  302  ? -58.621 61.799  65.296  1.00 16.08 ? 300  ASP   A N     1 
ATOM   2109  C  CA    . ASP   A  1  302  ? -58.960 60.574  66.007  1.00 16.50 ? 300  ASP   A CA    1 
ATOM   2110  C  C     . ASP   A  1  302  ? -57.766 59.626  66.106  1.00 16.99 ? 300  ASP   A C     1 
ATOM   2111  O  O     . ASP   A  1  302  ? -57.821 58.461  65.702  1.00 17.73 ? 300  ASP   A O     1 
ATOM   2112  C  CB    . ASP   A  1  302  ? -60.194 59.878  65.429  1.00 16.30 ? 300  ASP   A CB    1 
ATOM   2113  C  CG    . ASP   A  1  302  ? -60.853 58.967  66.437  1.00 21.67 ? 300  ASP   A CG    1 
ATOM   2114  O  OD1   . ASP   A  1  302  ? -60.810 59.300  67.645  1.00 19.16 ? 300  ASP   A OD1   1 
ATOM   2115  O  OD2   . ASP   A  1  302  ? -61.403 57.923  66.028  1.00 23.39 ? 300  ASP   A OD2   1 
ATOM   2116  N  N     . ILE   A  1  303  ? -56.683 60.144  66.681  1.00 14.72 ? 301  ILE   A N     1 
ATOM   2117  C  CA    . ILE   A  1  303  ? -55.496 59.348  66.969  1.00 15.77 ? 301  ILE   A CA    1 
ATOM   2118  C  C     . ILE   A  1  303  ? -55.248 59.353  68.467  1.00 15.82 ? 301  ILE   A C     1 
ATOM   2119  O  O     . ILE   A  1  303  ? -55.743 60.206  69.207  1.00 16.10 ? 301  ILE   A O     1 
ATOM   2120  C  CB    . ILE   A  1  303  ? -54.234 59.834  66.219  1.00 15.88 ? 301  ILE   A CB    1 
ATOM   2121  C  CG1   . ILE   A  1  303  ? -53.744 61.171  66.780  1.00 15.59 ? 301  ILE   A CG1   1 
ATOM   2122  C  CG2   . ILE   A  1  303  ? -54.517 59.951  64.718  1.00 16.96 ? 301  ILE   A CG2   1 
ATOM   2123  C  CD1   . ILE   A  1  303  ? -52.381 61.586  66.243  1.00 17.36 ? 301  ILE   A CD1   1 
ATOM   2124  N  N     . GLY   A  1  304  ? -54.451 58.385  68.911  1.00 16.04 ? 302  GLY   A N     1 
ATOM   2125  C  CA    . GLY   A  1  304  ? -54.060 58.353  70.310  1.00 14.71 ? 302  GLY   A CA    1 
ATOM   2126  C  C     . GLY   A  1  304  ? -53.028 59.426  70.613  1.00 15.42 ? 302  GLY   A C     1 
ATOM   2127  O  O     . GLY   A  1  304  ? -52.186 59.764  69.781  1.00 15.60 ? 302  GLY   A O     1 
ATOM   2128  N  N     . LEU   A  1  305  ? -53.119 59.990  71.813  1.00 15.58 ? 303  LEU   A N     1 
ATOM   2129  C  CA    . LEU   A  1  305  ? -52.105 60.899  72.332  1.00 13.74 ? 303  LEU   A CA    1 
ATOM   2130  C  C     . LEU   A  1  305  ? -51.791 60.433  73.740  1.00 15.50 ? 303  LEU   A C     1 
ATOM   2131  O  O     . LEU   A  1  305  ? -52.625 60.562  74.640  1.00 15.99 ? 303  LEU   A O     1 
ATOM   2132  C  CB    . LEU   A  1  305  ? -52.591 62.347  72.320  1.00 16.10 ? 303  LEU   A CB    1 
ATOM   2133  C  CG    . LEU   A  1  305  ? -51.561 63.392  72.768  1.00 18.66 ? 303  LEU   A CG    1 
ATOM   2134  C  CD1   . LEU   A  1  305  ? -51.807 64.709  72.074  1.00 21.44 ? 303  LEU   A CD1   1 
ATOM   2135  C  CD2   . LEU   A  1  305  ? -51.574 63.597  74.271  1.00 23.04 ? 303  LEU   A CD2   1 
ATOM   2136  N  N     . ASN   A  1  306  ? -50.588 59.916  73.935  1.00 14.68 ? 304  ASN   A N     1 
ATOM   2137  C  CA    . ASN   A  1  306  ? -50.194 59.298  75.186  1.00 16.09 ? 304  ASN   A CA    1 
ATOM   2138  C  C     . ASN   A  1  306  ? -49.250 60.230  75.927  1.00 15.18 ? 304  ASN   A C     1 
ATOM   2139  O  O     . ASN   A  1  306  ? -48.303 60.756  75.333  1.00 15.86 ? 304  ASN   A O     1 
ATOM   2140  C  CB    . ASN   A  1  306  ? -49.472 57.987  74.913  1.00 15.55 ? 304  ASN   A CB    1 
ATOM   2141  C  CG    . ASN   A  1  306  ? -48.833 57.441  76.145  1.00 17.75 ? 304  ASN   A CG    1 
ATOM   2142  O  OD1   . ASN   A  1  306  ? -47.624 57.624  76.382  1.00 19.52 ? 304  ASN   A OD1   1 
ATOM   2143  N  ND2   . ASN   A  1  306  ? -49.629 56.787  76.962  1.00 15.39 ? 304  ASN   A ND2   1 
ATOM   2144  N  N     . ILE   A  1  307  ? -49.484 60.401  77.222  1.00 14.33 ? 305  ILE   A N     1 
ATOM   2145  C  CA    . ILE   A  1  307  ? -48.560 61.119  78.096  1.00 14.98 ? 305  ILE   A CA    1 
ATOM   2146  C  C     . ILE   A  1  307  ? -47.599 60.116  78.719  1.00 14.10 ? 305  ILE   A C     1 
ATOM   2147  O  O     . ILE   A  1  307  ? -47.988 59.306  79.572  1.00 14.88 ? 305  ILE   A O     1 
ATOM   2148  C  CB    . ILE   A  1  307  ? -49.303 61.913  79.170  1.00 16.27 ? 305  ILE   A CB    1 
ATOM   2149  C  CG1   . ILE   A  1  307  ? -50.213 62.944  78.488  1.00 17.56 ? 305  ILE   A CG1   1 
ATOM   2150  C  CG2   . ILE   A  1  307  ? -48.279 62.556  80.136  1.00 18.78 ? 305  ILE   A CG2   1 
ATOM   2151  C  CD1   . ILE   A  1  307  ? -51.197 63.611  79.428  1.00 22.72 ? 305  ILE   A CD1   1 
ATOM   2152  N  N     . ASP   A  1  308  ? -46.332 60.182  78.313  1.00 14.17 ? 306  ASP   A N     1 
ATOM   2153  C  CA    . ASP   A  1  308  ? -45.312 59.302  78.868  1.00 14.23 ? 306  ASP   A CA    1 
ATOM   2154  C  C     . ASP   A  1  308  ? -45.075 59.653  80.333  1.00 13.86 ? 306  ASP   A C     1 
ATOM   2155  O  O     . ASP   A  1  308  ? -45.254 60.791  80.755  1.00 15.79 ? 306  ASP   A O     1 
ATOM   2156  C  CB    . ASP   A  1  308  ? -43.983 59.484  78.124  1.00 15.75 ? 306  ASP   A CB    1 
ATOM   2157  C  CG    . ASP   A  1  308  ? -43.989 58.889  76.722  1.00 19.65 ? 306  ASP   A CG    1 
ATOM   2158  O  OD1   . ASP   A  1  308  ? -44.916 58.132  76.368  1.00 18.86 ? 306  ASP   A OD1   1 
ATOM   2159  O  OD2   . ASP   A  1  308  ? -43.033 59.166  75.960  1.00 20.32 ? 306  ASP   A OD2   1 
ATOM   2160  N  N     . ALA   A  1  309  ? -44.688 58.657  81.117  1.00 13.96 ? 307  ALA   A N     1 
ATOM   2161  C  CA    . ALA   A  1  309  ? -44.385 58.885  82.523  1.00 14.06 ? 307  ALA   A CA    1 
ATOM   2162  C  C     . ALA   A  1  309  ? -42.900 59.142  82.723  1.00 14.68 ? 307  ALA   A C     1 
ATOM   2163  O  O     . ALA   A  1  309  ? -42.050 58.492  82.107  1.00 16.57 ? 307  ALA   A O     1 
ATOM   2164  C  CB    . ALA   A  1  309  ? -44.801 57.695  83.376  1.00 15.12 ? 307  ALA   A CB    1 
ATOM   2165  N  N     . GLU   A  1  310  ? -42.607 60.085  83.613  1.00 14.66 ? 308  GLU   A N     1 
ATOM   2166  C  CA    . GLU   A  1  310  ? -41.232 60.513  83.809  1.00 14.93 ? 308  GLU   A CA    1 
ATOM   2167  C  C     . GLU   A  1  310  ? -40.792 60.255  85.240  1.00 15.22 ? 308  GLU   A C     1 
ATOM   2168  O  O     . GLU   A  1  310  ? -41.045 59.171  85.774  1.00 15.29 ? 308  GLU   A O     1 
ATOM   2169  C  CB    . GLU   A  1  310  ? -41.085 61.962  83.350  1.00 15.64 ? 308  GLU   A CB    1 
ATOM   2170  C  CG    . GLU   A  1  310  ? -41.420 62.089  81.854  1.00 17.24 ? 308  GLU   A CG    1 
ATOM   2171  C  CD    . GLU   A  1  310  ? -41.176 63.478  81.298  1.00 17.41 ? 308  GLU   A CD    1 
ATOM   2172  O  OE1   . GLU   A  1  310  ? -39.995 63.797  81.013  1.00 20.31 ? 308  GLU   A OE1   1 
ATOM   2173  O  OE2   . GLU   A  1  310  ? -42.159 64.230  81.131  1.00 17.44 ? 308  GLU   A OE2   1 
ATOM   2174  N  N     . GLU   A  1  311  ? -40.119 61.214  85.863  1.00 15.39 ? 309  GLU   A N     1 
ATOM   2175  C  CA    . GLU   A  1  311  ? -39.597 60.957  87.193  1.00 15.97 ? 309  GLU   A CA    1 
ATOM   2176  C  C     . GLU   A  1  311  ? -40.720 60.858  88.212  1.00 15.24 ? 309  GLU   A C     1 
ATOM   2177  O  O     . GLU   A  1  311  ? -41.836 61.347  88.016  1.00 14.88 ? 309  GLU   A O     1 
ATOM   2178  C  CB    . GLU   A  1  311  ? -38.667 62.082  87.633  1.00 17.75 ? 309  GLU   A CB    1 
ATOM   2179  C  CG    . GLU   A  1  311  ? -37.392 62.207  86.803  1.00 19.09 ? 309  GLU   A CG    1 
ATOM   2180  C  CD    . GLU   A  1  311  ? -37.557 63.072  85.563  1.00 20.92 ? 309  GLU   A CD    1 
ATOM   2181  O  OE1   . GLU   A  1  311  ? -38.692 63.420  85.193  1.00 17.18 ? 309  GLU   A OE1   1 
ATOM   2182  O  OE2   . GLU   A  1  311  ? -36.529 63.421  84.950  1.00 26.92 ? 309  GLU   A OE2   1 
ATOM   2183  N  N     . ALA   A  1  312  ? -40.414 60.202  89.326  1.00 14.89 ? 310  ALA   A N     1 
ATOM   2184  C  CA    . ALA   A  1  312  ? -41.439 59.957  90.333  1.00 15.05 ? 310  ALA   A CA    1 
ATOM   2185  C  C     . ALA   A  1  312  ? -42.017 61.247  90.901  1.00 14.47 ? 310  ALA   A C     1 
ATOM   2186  O  O     . ALA   A  1  312  ? -43.204 61.283  91.252  1.00 16.48 ? 310  ALA   A O     1 
ATOM   2187  C  CB    . ALA   A  1  312  ? -40.859 59.089  91.444  1.00 15.97 ? 310  ALA   A CB    1 
ATOM   2188  N  N     . ASP   A  1  313  ? -41.224 62.323  90.970  1.00 16.27 ? 311  ASP   A N     1 
ATOM   2189  C  CA    . ASP   A  1  313  ? -41.741 63.569  91.526  1.00 15.46 ? 311  ASP   A CA    1 
ATOM   2190  C  C     . ASP   A  1  313  ? -42.624 64.337  90.557  1.00 15.54 ? 311  ASP   A C     1 
ATOM   2191  O  O     . ASP   A  1  313  ? -43.099 65.416  90.911  1.00 16.39 ? 311  ASP   A O     1 
ATOM   2192  C  CB    . ASP   A  1  313  ? -40.632 64.446  92.131  1.00 18.05 ? 311  ASP   A CB    1 
ATOM   2193  C  CG    . ASP   A  1  313  ? -39.656 64.982  91.098  1.00 21.11 ? 311  ASP   A CG    1 
ATOM   2194  O  OD1   . ASP   A  1  313  ? -39.805 64.695  89.889  1.00 19.74 ? 311  ASP   A OD1   1 
ATOM   2195  O  OD2   . ASP   A  1  313  ? -38.722 65.703  91.514  1.00 24.50 ? 311  ASP   A OD2   1 
ATOM   2196  N  N     . ARG   A  1  314  ? -42.843 63.804  89.362  1.00 15.14 ? 312  ARG   A N     1 
ATOM   2197  C  CA    . ARG   A  1  314  ? -43.770 64.396  88.418  1.00 14.94 ? 312  ARG   A CA    1 
ATOM   2198  C  C     . ARG   A  1  314  ? -45.052 63.603  88.274  1.00 16.36 ? 312  ARG   A C     1 
ATOM   2199  O  O     . ARG   A  1  314  ? -45.993 64.095  87.644  1.00 15.71 ? 312  ARG   A O     1 
ATOM   2200  C  CB    . ARG   A  1  314  ? -43.104 64.546  87.047  1.00 16.80 ? 312  ARG   A CB    1 
ATOM   2201  C  CG    . ARG   A  1  314  ? -42.141 65.693  87.054  1.00 17.52 ? 312  ARG   A CG    1 
ATOM   2202  C  CD    . ARG   A  1  314  ? -41.104 65.551  85.978  1.00 19.40 ? 312  ARG   A CD    1 
ATOM   2203  N  NE    . ARG   A  1  314  ? -40.516 66.852  85.705  1.00 18.13 ? 312  ARG   A NE    1 
ATOM   2204  C  CZ    . ARG   A  1  314  ? -39.549 67.056  84.823  1.00 17.37 ? 312  ARG   A CZ    1 
ATOM   2205  N  NH1   . ARG   A  1  314  ? -38.970 66.051  84.195  1.00 17.49 ? 312  ARG   A NH1   1 
ATOM   2206  N  NH2   . ARG   A  1  314  ? -39.174 68.304  84.551  1.00 19.68 ? 312  ARG   A NH2   1 
ATOM   2207  N  N     . LEU   A  1  315  ? -45.129 62.414  88.875  1.00 15.74 ? 313  LEU   A N     1 
ATOM   2208  C  CA    . LEU   A  1  315  ? -46.302 61.563  88.696  1.00 15.90 ? 313  LEU   A CA    1 
ATOM   2209  C  C     . LEU   A  1  315  ? -47.574 62.286  89.124  1.00 15.38 ? 313  LEU   A C     1 
ATOM   2210  O  O     . LEU   A  1  315  ? -48.529 62.428  88.347  1.00 15.10 ? 313  LEU   A O     1 
ATOM   2211  C  CB    . LEU   A  1  315  ? -46.115 60.285  89.510  1.00 16.49 ? 313  LEU   A CB    1 
ATOM   2212  C  CG    . LEU   A  1  315  ? -46.925 59.040  89.110  1.00 16.04 ? 313  LEU   A CG    1 
ATOM   2213  C  CD1   . LEU   A  1  315  ? -46.573 57.875  89.999  1.00 17.29 ? 313  LEU   A CD1   1 
ATOM   2214  C  CD2   . LEU   A  1  315  ? -48.420 59.257  89.169  1.00 19.50 ? 313  LEU   A CD2   1 
ATOM   2215  N  N     . GLU   A  1  316  ? -47.625 62.728  90.372  1.00 15.11 ? 314  GLU   A N     1 
ATOM   2216  C  CA    . GLU   A  1  316  ? -48.891 63.256  90.863  1.00 15.13 ? 314  GLU   A CA    1 
ATOM   2217  C  C     . GLU   A  1  316  ? -49.255 64.569  90.177  1.00 17.54 ? 314  GLU   A C     1 
ATOM   2218  O  O     . GLU   A  1  316  ? -50.432 64.820  89.884  1.00 16.28 ? 314  GLU   A O     1 
ATOM   2219  C  CB    . GLU   A  1  316  ? -48.865 63.348  92.385  1.00 16.37 ? 314  GLU   A CB    1 
ATOM   2220  C  CG    . GLU   A  1  316  ? -48.862 61.954  92.993  1.00 16.75 ? 314  GLU   A CG    1 
ATOM   2221  C  CD    . GLU   A  1  316  ? -48.871 61.948  94.499  1.00 18.37 ? 314  GLU   A CD    1 
ATOM   2222  O  OE1   . GLU   A  1  316  ? -49.622 62.753  95.081  1.00 19.30 ? 314  GLU   A OE1   1 
ATOM   2223  O  OE2   . GLU   A  1  316  ? -48.144 61.126  95.099  1.00 19.02 ? 314  GLU   A OE2   1 
ATOM   2224  N  N     . LEU   A  1  317  ? -48.256 65.398  89.870  1.00 16.89 ? 315  LEU   A N     1 
ATOM   2225  C  CA    . LEU   A  1  317  ? -48.515 66.613  89.110  1.00 17.75 ? 315  LEU   A CA    1 
ATOM   2226  C  C     . LEU   A  1  317  ? -49.158 66.290  87.766  1.00 16.51 ? 315  LEU   A C     1 
ATOM   2227  O  O     . LEU   A  1  317  ? -50.119 66.950  87.345  1.00 16.96 ? 315  LEU   A O     1 
ATOM   2228  C  CB    . LEU   A  1  317  ? -47.198 67.353  88.910  1.00 18.91 ? 315  LEU   A CB    1 
ATOM   2229  C  CG    . LEU   A  1  317  ? -47.297 68.613  88.060  1.00 19.49 ? 315  LEU   A CG    1 
ATOM   2230  C  CD1   . LEU   A  1  317  ? -48.250 69.614  88.696  1.00 22.17 ? 315  LEU   A CD1   1 
ATOM   2231  C  CD2   . LEU   A  1  317  ? -45.889 69.177  87.911  1.00 21.18 ? 315  LEU   A CD2   1 
ATOM   2232  N  N     . SER   A  1  318  ? -48.665 65.248  87.095  1.00 14.15 ? 316  SER   A N     1 
ATOM   2233  C  CA    . SER   A  1  318  ? -49.219 64.888  85.800  1.00 14.03 ? 316  SER   A CA    1 
ATOM   2234  C  C     . SER   A  1  318  ? -50.674 64.476  85.922  1.00 15.78 ? 316  SER   A C     1 
ATOM   2235  O  O     . SER   A  1  318  ? -51.447 64.682  84.981  1.00 15.41 ? 316  SER   A O     1 
ATOM   2236  C  CB    . SER   A  1  318  ? -48.401 63.773  85.137  1.00 14.01 ? 316  SER   A CB    1 
ATOM   2237  O  OG    . SER   A  1  318  ? -48.617 62.513  85.743  1.00 15.32 ? 316  SER   A OG    1 
ATOM   2238  N  N     . LEU   A  1  319  ? -51.060 63.902  87.066  1.00 15.14 ? 317  LEU   A N     1 
ATOM   2239  C  CA    . LEU   A  1  319  ? -52.463 63.559  87.282  1.00 15.32 ? 317  LEU   A CA    1 
ATOM   2240  C  C     . LEU   A  1  319  ? -53.349 64.789  87.288  1.00 16.36 ? 317  LEU   A C     1 
ATOM   2241  O  O     . LEU   A  1  319  ? -54.506 64.718  86.865  1.00 16.83 ? 317  LEU   A O     1 
ATOM   2242  C  CB    . LEU   A  1  319  ? -52.621 62.791  88.594  1.00 16.57 ? 317  LEU   A CB    1 
ATOM   2243  C  CG    . LEU   A  1  319  ? -51.922 61.436  88.635  1.00 17.91 ? 317  LEU   A CG    1 
ATOM   2244  C  CD1   . LEU   A  1  319  ? -52.094 60.794  90.009  1.00 19.05 ? 317  LEU   A CD1   1 
ATOM   2245  C  CD2   . LEU   A  1  319  ? -52.433 60.520  87.548  1.00 18.01 ? 317  LEU   A CD2   1 
ATOM   2246  N  N     . ASP   A  1  320  ? -52.849 65.923  87.759  1.00 16.64 ? 318  ASP   A N     1 
ATOM   2247  C  CA    . ASP   A  1  320  ? -53.673 67.123  87.708  1.00 18.32 ? 318  ASP   A CA    1 
ATOM   2248  C  C     . ASP   A  1  320  ? -53.939 67.553  86.279  1.00 18.35 ? 318  ASP   A C     1 
ATOM   2249  O  O     . ASP   A  1  320  ? -55.033 68.041  85.966  1.00 19.69 ? 318  ASP   A O     1 
ATOM   2250  C  CB    . ASP   A  1  320  ? -53.027 68.230  88.524  1.00 18.00 ? 318  ASP   A CB    1 
ATOM   2251  C  CG    . ASP   A  1  320  ? -53.210 68.011  89.995  1.00 21.78 ? 318  ASP   A CG    1 
ATOM   2252  O  OD1   . ASP   A  1  320  ? -54.383 67.893  90.402  1.00 23.26 ? 318  ASP   A OD1   1 
ATOM   2253  O  OD2   . ASP   A  1  320  ? -52.204 67.918  90.727  1.00 24.39 ? 318  ASP   A OD2   1 
ATOM   2254  N  N     . LEU   A  1  321  ? -52.978 67.342  85.388  1.00 15.89 ? 319  LEU   A N     1 
ATOM   2255  C  CA    . LEU   A  1  321  ? -53.214 67.658  83.990  1.00 16.45 ? 319  LEU   A CA    1 
ATOM   2256  C  C     . LEU   A  1  321  ? -54.162 66.652  83.374  1.00 16.00 ? 319  LEU   A C     1 
ATOM   2257  O  O     . LEU   A  1  321  ? -55.087 67.036  82.648  1.00 18.27 ? 319  LEU   A O     1 
ATOM   2258  C  CB    . LEU   A  1  321  ? -51.894 67.694  83.227  1.00 17.60 ? 319  LEU   A CB    1 
ATOM   2259  C  CG    . LEU   A  1  321  ? -51.104 68.978  83.459  1.00 19.32 ? 319  LEU   A CG    1 
ATOM   2260  C  CD1   . LEU   A  1  321  ? -50.191 68.834  84.637  1.00 23.95 ? 319  LEU   A CD1   1 
ATOM   2261  C  CD2   . LEU   A  1  321  ? -50.309 69.298  82.206  1.00 25.29 ? 319  LEU   A CD2   1 
ATOM   2262  N  N     . LEU   A  1  322  ? -53.964 65.364  83.667  1.00 16.42 ? 320  LEU   A N     1 
ATOM   2263  C  CA    . LEU   A  1  322  ? -54.860 64.344  83.135  1.00 17.68 ? 320  LEU   A CA    1 
ATOM   2264  C  C     . LEU   A  1  322  ? -56.291 64.613  83.559  1.00 17.71 ? 320  LEU   A C     1 
ATOM   2265  O  O     . LEU   A  1  322  ? -57.215 64.507  82.744  1.00 17.99 ? 320  LEU   A O     1 
ATOM   2266  C  CB    . LEU   A  1  322  ? -54.429 62.964  83.622  1.00 17.06 ? 320  LEU   A CB    1 
ATOM   2267  C  CG    . LEU   A  1  322  ? -55.233 61.795  83.056  1.00 18.42 ? 320  LEU   A CG    1 
ATOM   2268  C  CD1   . LEU   A  1  322  ? -55.031 61.630  81.559  1.00 17.72 ? 320  LEU   A CD1   1 
ATOM   2269  C  CD2   . LEU   A  1  322  ? -54.862 60.529  83.778  1.00 16.34 ? 320  LEU   A CD2   1 
ATOM   2270  N  N     . GLU   A  1  323  ? -56.489 64.998  84.818  1.00 16.50 ? 321  GLU   A N     1 
ATOM   2271  C  CA    . GLU   A  1  323  ? -57.832 65.268  85.322  1.00 17.83 ? 321  GLU   A CA    1 
ATOM   2272  C  C     . GLU   A  1  323  ? -58.483 66.404  84.550  1.00 19.57 ? 321  GLU   A C     1 
ATOM   2273  O  O     . GLU   A  1  323  ? -59.619 66.278  84.082  1.00 17.52 ? 321  GLU   A O     1 
ATOM   2274  C  CB    . GLU   A  1  323  ? -57.759 65.616  86.808  1.00 17.66 ? 321  GLU   A CB    1 
ATOM   2275  C  CG    . GLU   A  1  323  ? -59.062 66.189  87.386  1.00 23.59 ? 321  GLU   A CG    1 
ATOM   2276  C  CD    . GLU   A  1  323  ? -59.795 65.215  88.275  1.00 29.52 ? 321  GLU   A CD    1 
ATOM   2277  O  OE1   . GLU   A  1  323  ? -59.231 64.164  88.608  1.00 28.08 ? 321  GLU   A OE1   1 
ATOM   2278  O  OE2   . GLU   A  1  323  ? -60.956 65.502  88.640  1.00 29.14 ? 321  GLU   A OE2   1 
ATOM   2279  N  N     . VAL   A  1  324  ? -57.786 67.533  84.410  1.00 17.87 ? 322  VAL   A N     1 
ATOM   2280  C  CA    . VAL   A  1  324  ? -58.380 68.667  83.712  1.00 19.12 ? 322  VAL   A CA    1 
ATOM   2281  C  C     . VAL   A  1  324  ? -58.686 68.310  82.264  1.00 16.75 ? 322  VAL   A C     1 
ATOM   2282  O  O     . VAL   A  1  324  ? -59.756 68.641  81.738  1.00 17.43 ? 322  VAL   A O     1 
ATOM   2283  C  CB    . VAL   A  1  324  ? -57.483 69.913  83.809  1.00 19.50 ? 322  VAL   A CB    1 
ATOM   2284  C  CG1   . VAL   A  1  324  ? -58.079 71.028  82.955  1.00 22.42 ? 322  VAL   A CG1   1 
ATOM   2285  C  CG2   . VAL   A  1  324  ? -57.359 70.369  85.240  1.00 21.31 ? 322  VAL   A CG2   1 
ATOM   2286  N  N     . LEU   A  1  325  ? -57.763 67.620  81.597  1.00 15.64 ? 323  LEU   A N     1 
ATOM   2287  C  CA    . LEU   A  1  325  ? -57.990 67.285  80.195  1.00 16.48 ? 323  LEU   A CA    1 
ATOM   2288  C  C     . LEU   A  1  325  ? -59.183 66.355  80.043  1.00 16.30 ? 323  LEU   A C     1 
ATOM   2289  O  O     . LEU   A  1  325  ? -60.027 66.544  79.155  1.00 16.53 ? 323  LEU   A O     1 
ATOM   2290  C  CB    . LEU   A  1  325  ? -56.736 66.647  79.602  1.00 17.16 ? 323  LEU   A CB    1 
ATOM   2291  C  CG    . LEU   A  1  325  ? -55.532 67.583  79.509  1.00 18.82 ? 323  LEU   A CG    1 
ATOM   2292  C  CD1   . LEU   A  1  325  ? -54.240 66.789  79.364  1.00 18.28 ? 323  LEU   A CD1   1 
ATOM   2293  C  CD2   . LEU   A  1  325  ? -55.743 68.485  78.315  1.00 17.71 ? 323  LEU   A CD2   1 
ATOM   2294  N  N     . CYS   A  1  326  ? -59.283 65.355  80.912  1.00 16.85 ? 324  CYS   A N     1 
ATOM   2295  C  CA    . CYS   A  1  326  ? -60.371 64.400  80.777  1.00 16.68 ? 324  CYS   A CA    1 
ATOM   2296  C  C     . CYS   A  1  326  ? -61.717 65.004  81.121  1.00 18.37 ? 324  CYS   A C     1 
ATOM   2297  O  O     . CYS   A  1  326  ? -62.739 64.487  80.662  1.00 18.27 ? 324  CYS   A O     1 
ATOM   2298  C  CB    . CYS   A  1  326  ? -60.115 63.168  81.633  1.00 16.84 ? 324  CYS   A CB    1 
ATOM   2299  S  SG    . CYS   A  1  326  ? -58.784 62.158  80.972  1.00 19.68 ? 324  CYS   A SG    1 
ATOM   2300  N  N     . LEU   A  1  327  ? -61.744 66.074  81.908  1.00 16.11 ? 325  LEU   A N     1 
ATOM   2301  C  CA    . LEU   A  1  327  ? -62.980 66.755  82.258  1.00 16.53 ? 325  LEU   A CA    1 
ATOM   2302  C  C     . LEU   A  1  327  ? -63.279 67.918  81.330  1.00 17.86 ? 325  LEU   A C     1 
ATOM   2303  O  O     . LEU   A  1  327  ? -64.322 68.552  81.473  1.00 18.73 ? 325  LEU   A O     1 
ATOM   2304  C  CB    . LEU   A  1  327  ? -62.934 67.247  83.705  1.00 19.28 ? 325  LEU   A CB    1 
ATOM   2305  C  CG    . LEU   A  1  327  ? -62.823 66.128  84.745  1.00 21.92 ? 325  LEU   A CG    1 
ATOM   2306  C  CD1   . LEU   A  1  327  ? -62.660 66.716  86.139  1.00 24.28 ? 325  LEU   A CD1   1 
ATOM   2307  C  CD2   . LEU   A  1  327  ? -64.006 65.187  84.681  1.00 24.02 ? 325  LEU   A CD2   1 
ATOM   2308  N  N     . ASP   A  1  328  ? -62.403 68.203  80.375  1.00 16.90 ? 326  ASP   A N     1 
ATOM   2309  C  CA    . ASP   A  1  328  ? -62.575 69.357  79.505  1.00 16.66 ? 326  ASP   A CA    1 
ATOM   2310  C  C     . ASP   A  1  328  ? -63.507 68.970  78.365  1.00 17.64 ? 326  ASP   A C     1 
ATOM   2311  O  O     . ASP   A  1  328  ? -63.162 68.133  77.527  1.00 17.79 ? 326  ASP   A O     1 
ATOM   2312  C  CB    . ASP   A  1  328  ? -61.216 69.806  78.982  1.00 16.78 ? 326  ASP   A CB    1 
ATOM   2313  C  CG    . ASP   A  1  328  ? -61.284 71.119  78.247  1.00 21.05 ? 326  ASP   A CG    1 
ATOM   2314  O  OD1   . ASP   A  1  328  ? -62.265 71.347  77.516  1.00 20.65 ? 326  ASP   A OD1   1 
ATOM   2315  O  OD2   . ASP   A  1  328  ? -60.368 71.942  78.417  1.00 24.15 ? 326  ASP   A OD2   1 
ATOM   2316  N  N     . GLY   A  1  329  ? -64.684 69.591  78.324  1.00 18.03 ? 327  GLY   A N     1 
ATOM   2317  C  CA    . GLY   A  1  329  ? -65.673 69.230  77.326  1.00 17.50 ? 327  GLY   A CA    1 
ATOM   2318  C  C     . GLY   A  1  329  ? -65.220 69.449  75.903  1.00 18.63 ? 327  GLY   A C     1 
ATOM   2319  O  O     . GLY   A  1  329  ? -65.750 68.810  74.992  1.00 17.36 ? 327  GLY   A O     1 
ATOM   2320  N  N     . ASP   A  1  330  ? -64.235 70.328  75.681  1.00 16.63 ? 328  ASP   A N     1 
ATOM   2321  C  CA    . ASP   A  1  330  ? -63.764 70.549  74.321  1.00 18.33 ? 328  ASP   A CA    1 
ATOM   2322  C  C     . ASP   A  1  330  ? -63.111 69.309  73.737  1.00 15.31 ? 328  ASP   A C     1 
ATOM   2323  O  O     . ASP   A  1  330  ? -62.990 69.207  72.515  1.00 17.62 ? 328  ASP   A O     1 
ATOM   2324  C  CB    . ASP   A  1  330  ? -62.742 71.681  74.261  1.00 19.03 ? 328  ASP   A CB    1 
ATOM   2325  C  CG    . ASP   A  1  330  ? -63.347 73.030  74.536  1.00 25.26 ? 328  ASP   A CG    1 
ATOM   2326  O  OD1   . ASP   A  1  330  ? -64.571 73.193  74.349  1.00 26.18 ? 328  ASP   A OD1   1 
ATOM   2327  O  OD2   . ASP   A  1  330  ? -62.590 73.936  74.925  1.00 21.14 ? 328  ASP   A OD2   1 
ATOM   2328  N  N     . LEU   A  1  331  ? -62.685 68.376  74.583  1.00 15.44 ? 329  LEU   A N     1 
ATOM   2329  C  CA    . LEU   A  1  331  ? -62.058 67.143  74.143  1.00 17.67 ? 329  LEU   A CA    1 
ATOM   2330  C  C     . LEU   A  1  331  ? -63.023 65.977  74.121  1.00 17.12 ? 329  LEU   A C     1 
ATOM   2331  O  O     . LEU   A  1  331  ? -62.613 64.854  73.817  1.00 17.33 ? 329  LEU   A O     1 
ATOM   2332  C  CB    . LEU   A  1  331  ? -60.868 66.810  75.047  1.00 16.97 ? 329  LEU   A CB    1 
ATOM   2333  C  CG    . LEU   A  1  331  ? -59.644 67.710  74.862  1.00 16.09 ? 329  LEU   A CG    1 
ATOM   2334  C  CD1   . LEU   A  1  331  ? -58.614 67.456  75.943  1.00 17.74 ? 329  LEU   A CD1   1 
ATOM   2335  C  CD2   . LEU   A  1  331  ? -59.041 67.492  73.487  1.00 17.61 ? 329  LEU   A CD2   1 
ATOM   2336  N  N     . SER   A  1  332  ? -64.298 66.220  74.410  1.00 17.83 ? 330  SER   A N     1 
ATOM   2337  C  CA    . SER   A  1  332  ? -65.247 65.123  74.502  1.00 19.33 ? 330  SER   A CA    1 
ATOM   2338  C  C     . SER   A  1  332  ? -65.468 64.486  73.132  1.00 17.00 ? 330  SER   A C     1 
ATOM   2339  O  O     . SER   A  1  332  ? -65.297 65.116  72.087  1.00 20.02 ? 330  SER   A O     1 
ATOM   2340  C  CB    . SER   A  1  332  ? -66.577 65.607  75.076  1.00 19.06 ? 330  SER   A CB    1 
ATOM   2341  O  OG    . SER   A  1  332  ? -67.214 66.498  74.188  1.00 22.64 ? 330  SER   A OG    1 
ATOM   2342  N  N     . GLY   A  1  333  ? -65.817 63.207  73.151  1.00 16.35 ? 331  GLY   A N     1 
ATOM   2343  C  CA    . GLY   A  1  333  ? -66.014 62.459  71.932  1.00 18.48 ? 331  GLY   A CA    1 
ATOM   2344  C  C     . GLY   A  1  333  ? -64.788 61.718  71.461  1.00 17.27 ? 331  GLY   A C     1 
ATOM   2345  O  O     . GLY   A  1  333  ? -64.879 60.933  70.509  1.00 20.24 ? 331  GLY   A O     1 
ATOM   2346  N  N     . TRP   A  1  334  ? -63.652 61.920  72.110  1.00 16.83 ? 332  TRP   A N     1 
ATOM   2347  C  CA    . TRP   A  1  334  ? -62.391 61.327  71.706  1.00 17.64 ? 332  TRP   A CA    1 
ATOM   2348  C  C     . TRP   A  1  334  ? -61.869 60.507  72.867  1.00 16.21 ? 332  TRP   A C     1 
ATOM   2349  O  O     . TRP   A  1  334  ? -61.791 61.006  73.991  1.00 17.82 ? 332  TRP   A O     1 
ATOM   2350  C  CB    . TRP   A  1  334  ? -61.426 62.455  71.392  1.00 17.37 ? 332  TRP   A CB    1 
ATOM   2351  C  CG    . TRP   A  1  334  ? -60.003 62.079  71.202  1.00 15.97 ? 332  TRP   A CG    1 
ATOM   2352  C  CD1   . TRP   A  1  334  ? -59.467 61.322  70.200  1.00 15.82 ? 332  TRP   A CD1   1 
ATOM   2353  C  CD2   . TRP   A  1  334  ? -58.917 62.532  71.998  1.00 16.08 ? 332  TRP   A CD2   1 
ATOM   2354  N  NE1   . TRP   A  1  334  ? -58.099 61.255  70.347  1.00 15.82 ? 332  TRP   A NE1   1 
ATOM   2355  C  CE2   . TRP   A  1  334  ? -57.737 61.999  71.439  1.00 14.94 ? 332  TRP   A CE2   1 
ATOM   2356  C  CE3   . TRP   A  1  334  ? -58.824 63.334  73.143  1.00 17.20 ? 332  TRP   A CE3   1 
ATOM   2357  C  CZ2   . TRP   A  1  334  ? -56.482 62.226  71.991  1.00 14.74 ? 332  TRP   A CZ2   1 
ATOM   2358  C  CZ3   . TRP   A  1  334  ? -57.579 63.562  73.692  1.00 16.95 ? 332  TRP   A CZ3   1 
ATOM   2359  C  CH2   . TRP   A  1  334  ? -56.419 63.014  73.110  1.00 16.96 ? 332  TRP   A CH2   1 
ATOM   2360  N  N     . ASN   A  1  335  ? -61.533 59.248  72.594  1.00 16.50 ? 333  ASN   A N     1 
ATOM   2361  C  CA    . ASN   A  1  335  ? -61.019 58.332  73.603  1.00 16.04 ? 333  ASN   A CA    1 
ATOM   2362  C  C     . ASN   A  1  335  ? -59.527 58.088  73.441  1.00 16.43 ? 333  ASN   A C     1 
ATOM   2363  O  O     . ASN   A  1  335  ? -59.000 57.105  73.971  1.00 16.91 ? 333  ASN   A O     1 
ATOM   2364  C  CB    . ASN   A  1  335  ? -61.762 57.000  73.552  1.00 18.98 ? 333  ASN   A CB    1 
ATOM   2365  C  CG    . ASN   A  1  335  ? -63.103 57.058  74.230  1.00 18.82 ? 333  ASN   A CG    1 
ATOM   2366  O  OD1   . ASN   A  1  335  ? -63.335 57.861  75.139  1.00 18.27 ? 333  ASN   A OD1   1 
ATOM   2367  N  ND2   . ASN   A  1  335  ? -64.000 56.184  73.804  1.00 25.56 ? 333  ASN   A ND2   1 
ATOM   2368  N  N     . GLY   A  1  336  ? -58.847 58.958  72.704  1.00 15.88 ? 334  GLY   A N     1 
ATOM   2369  C  CA    . GLY   A  1  336  ? -57.444 58.766  72.421  1.00 15.04 ? 334  GLY   A CA    1 
ATOM   2370  C  C     . GLY   A  1  336  ? -56.484 59.244  73.484  1.00 14.27 ? 334  GLY   A C     1 
ATOM   2371  O  O     . GLY   A  1  336  ? -55.290 58.988  73.347  1.00 15.78 ? 334  GLY   A O     1 
ATOM   2372  N  N     . MET   A  1  337  ? -56.936 59.920  74.534  1.00 15.11 ? 335  MET   A N     1 
ATOM   2373  C  CA    A MET   A  1  337  ? -56.013 60.341  75.579  0.53 16.30 ? 335  MET   A CA    1 
ATOM   2374  C  CA    B MET   A  1  337  ? -55.997 60.337  75.564  0.47 16.30 ? 335  MET   A CA    1 
ATOM   2375  C  C     . MET   A  1  337  ? -55.442 59.125  76.291  1.00 14.70 ? 335  MET   A C     1 
ATOM   2376  O  O     . MET   A  1  337  ? -56.192 58.259  76.766  1.00 16.29 ? 335  MET   A O     1 
ATOM   2377  C  CB    A MET   A  1  337  ? -56.723 61.252  76.577  0.53 16.75 ? 335  MET   A CB    1 
ATOM   2378  C  CB    B MET   A  1  337  ? -56.649 61.302  76.546  0.47 16.70 ? 335  MET   A CB    1 
ATOM   2379  C  CG    A MET   A  1  337  ? -55.795 61.905  77.575  0.53 19.47 ? 335  MET   A CG    1 
ATOM   2380  C  CG    B MET   A  1  337  ? -55.758 61.639  77.725  0.47 19.77 ? 335  MET   A CG    1 
ATOM   2381  S  SD    A MET   A  1  337  ? -54.743 63.114  76.771  0.53 24.53 ? 335  MET   A SD    1 
ATOM   2382  S  SD    B MET   A  1  337  ? -55.858 63.386  78.095  0.47 21.29 ? 335  MET   A SD    1 
ATOM   2383  C  CE    A MET   A  1  337  ? -55.838 64.528  76.660  0.53 22.30 ? 335  MET   A CE    1 
ATOM   2384  C  CE    B MET   A  1  337  ? -55.104 64.053  76.616  0.47 17.99 ? 335  MET   A CE    1 
ATOM   2385  N  N     . GLY   A  1  338  ? -54.115 59.072  76.382  1.00 15.13 ? 336  GLY   A N     1 
ATOM   2386  C  CA    . GLY   A  1  338  ? -53.440 57.956  77.005  1.00 17.11 ? 336  GLY   A CA    1 
ATOM   2387  C  C     . GLY   A  1  338  ? -52.489 58.446  78.078  1.00 16.52 ? 336  GLY   A C     1 
ATOM   2388  O  O     . GLY   A  1  338  ? -52.100 59.614  78.108  1.00 15.69 ? 336  GLY   A O     1 
ATOM   2389  N  N     . PHE   A  1  339  ? -52.163 57.543  78.986  1.00 14.59 ? 337  PHE   A N     1 
ATOM   2390  C  CA    . PHE   A  1  339  ? -51.373 57.914  80.145  1.00 15.21 ? 337  PHE   A CA    1 
ATOM   2391  C  C     . PHE   A  1  339  ? -50.609 56.691  80.623  1.00 15.78 ? 337  PHE   A C     1 
ATOM   2392  O  O     . PHE   A  1  339  ? -51.186 55.612  80.772  1.00 15.74 ? 337  PHE   A O     1 
ATOM   2393  C  CB    . PHE   A  1  339  ? -52.326 58.398  81.240  1.00 15.76 ? 337  PHE   A CB    1 
ATOM   2394  C  CG    . PHE   A  1  339  ? -51.647 59.042  82.408  1.00 15.25 ? 337  PHE   A CG    1 
ATOM   2395  C  CD1   . PHE   A  1  339  ? -51.323 60.396  82.380  1.00 15.84 ? 337  PHE   A CD1   1 
ATOM   2396  C  CD2   . PHE   A  1  339  ? -51.361 58.303  83.542  1.00 15.64 ? 337  PHE   A CD2   1 
ATOM   2397  C  CE1   . PHE   A  1  339  ? -50.715 60.988  83.488  1.00 15.60 ? 337  PHE   A CE1   1 
ATOM   2398  C  CE2   . PHE   A  1  339  ? -50.749 58.887  84.645  1.00 17.33 ? 337  PHE   A CE2   1 
ATOM   2399  C  CZ    . PHE   A  1  339  ? -50.439 60.237  84.609  1.00 16.94 ? 337  PHE   A CZ    1 
ATOM   2400  N  N     . VAL   A  1  340  ? -49.310 56.858  80.849  1.00 15.23 ? 338  VAL   A N     1 
ATOM   2401  C  CA    . VAL   A  1  340  ? -48.453 55.771  81.297  1.00 15.39 ? 338  VAL   A CA    1 
ATOM   2402  C  C     . VAL   A  1  340  ? -48.443 55.722  82.808  1.00 15.07 ? 338  VAL   A C     1 
ATOM   2403  O  O     . VAL   A  1  340  ? -48.425 56.760  83.476  1.00 15.23 ? 338  VAL   A O     1 
ATOM   2404  C  CB    . VAL   A  1  340  ? -47.023 55.997  80.795  1.00 14.45 ? 338  VAL   A CB    1 
ATOM   2405  C  CG1   . VAL   A  1  340  ? -46.091 54.908  81.335  1.00 15.45 ? 338  VAL   A CG1   1 
ATOM   2406  C  CG2   . VAL   A  1  340  ? -47.010 56.049  79.286  1.00 14.92 ? 338  VAL   A CG2   1 
ATOM   2407  N  N     . VAL   A  1  341  ? -48.469 54.510  83.348  1.00 14.03 ? 339  VAL   A N     1 
ATOM   2408  C  CA    A VAL   A  1  341  ? -48.217 54.277  84.764  0.46 15.96 ? 339  VAL   A CA    1 
ATOM   2409  C  CA    B VAL   A  1  341  ? -48.219 54.276  84.764  0.54 15.96 ? 339  VAL   A CA    1 
ATOM   2410  C  C     . VAL   A  1  341  ? -47.075 53.283  84.892  1.00 15.12 ? 339  VAL   A C     1 
ATOM   2411  O  O     . VAL   A  1  341  ? -47.003 52.297  84.145  1.00 16.34 ? 339  VAL   A O     1 
ATOM   2412  C  CB    A VAL   A  1  341  ? -49.464 53.797  85.533  0.46 15.99 ? 339  VAL   A CB    1 
ATOM   2413  C  CB    B VAL   A  1  341  ? -49.458 53.779  85.531  0.54 15.98 ? 339  VAL   A CB    1 
ATOM   2414  C  CG1   A VAL   A  1  341  ? -50.534 54.873  85.514  0.46 17.08 ? 339  VAL   A CG1   1 
ATOM   2415  C  CG1   B VAL   A  1  341  ? -49.243 53.999  87.016  0.54 16.93 ? 339  VAL   A CG1   1 
ATOM   2416  C  CG2   A VAL   A  1  341  ? -49.992 52.506  84.953  0.46 18.26 ? 339  VAL   A CG2   1 
ATOM   2417  C  CG2   B VAL   A  1  341  ? -50.717 54.498  85.058  0.54 17.42 ? 339  VAL   A CG2   1 
ATOM   2418  N  N     . GLN   A  1  342  ? -46.186 53.549  85.836  1.00 15.25 ? 340  GLN   A N     1 
ATOM   2419  C  CA    . GLN   A  1  342  ? -44.951 52.793  86.008  1.00 16.05 ? 340  GLN   A CA    1 
ATOM   2420  C  C     . GLN   A  1  342  ? -45.107 51.801  87.151  1.00 14.97 ? 340  GLN   A C     1 
ATOM   2421  O  O     . GLN   A  1  342  ? -45.204 52.196  88.321  1.00 17.45 ? 340  GLN   A O     1 
ATOM   2422  C  CB    . GLN   A  1  342  ? -43.795 53.749  86.277  1.00 16.16 ? 340  GLN   A CB    1 
ATOM   2423  C  CG    . GLN   A  1  342  ? -43.555 54.735  85.144  1.00 14.47 ? 340  GLN   A CG    1 
ATOM   2424  C  CD    . GLN   A  1  342  ? -42.996 56.035  85.641  1.00 14.93 ? 340  GLN   A CD    1 
ATOM   2425  O  OE1   . GLN   A  1  342  ? -43.511 56.627  86.584  1.00 16.39 ? 340  GLN   A OE1   1 
ATOM   2426  N  NE2   . GLN   A  1  342  ? -41.926 56.502  84.997  1.00 14.68 ? 340  GLN   A NE2   1 
ATOM   2427  N  N     . ALA   A  1  343  ? -45.108 50.513  86.811  1.00 14.82 ? 341  ALA   A N     1 
ATOM   2428  C  CA    . ALA   A  1  343  ? -45.299 49.466  87.805  1.00 16.86 ? 341  ALA   A CA    1 
ATOM   2429  C  C     . ALA   A  1  343  ? -44.123 49.346  88.763  1.00 17.47 ? 341  ALA   A C     1 
ATOM   2430  O  O     . ALA   A  1  343  ? -44.266 48.717  89.820  1.00 17.36 ? 341  ALA   A O     1 
ATOM   2431  C  CB    . ALA   A  1  343  ? -45.557 48.128  87.119  1.00 20.20 ? 341  ALA   A CB    1 
ATOM   2432  N  N     . TYR   A  1  344  ? -42.953 49.896  88.423  1.00 16.44 ? 342  TYR   A N     1 
ATOM   2433  C  CA    . TYR   A  1  344  ? -41.898 49.912  89.424  1.00 16.61 ? 342  TYR   A CA    1 
ATOM   2434  C  C     . TYR   A  1  344  ? -42.178 50.883  90.554  1.00 17.41 ? 342  TYR   A C     1 
ATOM   2435  O  O     . TYR   A  1  344  ? -41.422 50.902  91.522  1.00 18.55 ? 342  TYR   A O     1 
ATOM   2436  C  CB    . TYR   A  1  344  ? -40.496 50.115  88.825  1.00 16.26 ? 342  TYR   A CB    1 
ATOM   2437  C  CG    . TYR   A  1  344  ? -40.080 51.482  88.318  1.00 16.20 ? 342  TYR   A CG    1 
ATOM   2438  C  CD1   . TYR   A  1  344  ? -40.927 52.578  88.297  1.00 16.35 ? 342  TYR   A CD1   1 
ATOM   2439  C  CD2   . TYR   A  1  344  ? -38.775 51.653  87.858  1.00 15.97 ? 342  TYR   A CD2   1 
ATOM   2440  C  CE1   . TYR   A  1  344  ? -40.497 53.805  87.800  1.00 16.53 ? 342  TYR   A CE1   1 
ATOM   2441  C  CE2   . TYR   A  1  344  ? -38.340 52.840  87.368  1.00 16.39 ? 342  TYR   A CE2   1 
ATOM   2442  C  CZ    . TYR   A  1  344  ? -39.180 53.922  87.346  1.00 15.02 ? 342  TYR   A CZ    1 
ATOM   2443  O  OH    . TYR   A  1  344  ? -38.712 55.105  86.845  1.00 15.90 ? 342  TYR   A OH    1 
ATOM   2444  N  N     . GLY   A  1  345  ? -43.234 51.684  90.452  1.00 16.18 ? 343  GLY   A N     1 
ATOM   2445  C  CA    . GLY   A  1  345  ? -43.536 52.669  91.464  1.00 17.61 ? 343  GLY   A CA    1 
ATOM   2446  C  C     . GLY   A  1  345  ? -44.548 52.137  92.465  1.00 17.94 ? 343  GLY   A C     1 
ATOM   2447  O  O     . GLY   A  1  345  ? -45.508 51.456  92.105  1.00 17.31 ? 343  GLY   A O     1 
ATOM   2448  N  N     . LYS   A  1  346  ? -44.332 52.495  93.727  1.00 16.58 ? 344  LYS   A N     1 
ATOM   2449  C  CA    . LYS   A  1  346  ? -45.164 51.994  94.808  1.00 17.56 ? 344  LYS   A CA    1 
ATOM   2450  C  C     . LYS   A  1  346  ? -46.586 52.526  94.741  1.00 19.02 ? 344  LYS   A C     1 
ATOM   2451  O  O     . LYS   A  1  346  ? -47.493 51.938  95.342  1.00 18.26 ? 344  LYS   A O     1 
ATOM   2452  C  CB    . LYS   A  1  346  ? -44.532 52.398  96.129  1.00 17.32 ? 344  LYS   A CB    1 
ATOM   2453  C  CG    . LYS   A  1  346  ? -43.184 51.767  96.323  1.00 19.74 ? 344  LYS   A CG    1 
ATOM   2454  C  CD    . LYS   A  1  346  ? -42.548 52.260  97.582  1.00 19.86 ? 344  LYS   A CD    1 
ATOM   2455  C  CE    . LYS   A  1  346  ? -41.333 51.427  97.883  1.00 19.41 ? 344  LYS   A CE    1 
ATOM   2456  N  NZ    . LYS   A  1  346  ? -40.558 52.025  99.006  1.00 21.44 ? 344  LYS   A NZ    1 
ATOM   2457  N  N     . ARG   A  1  347  ? -46.793 53.638  94.053  1.00 16.44 ? 345  ARG   A N     1 
ATOM   2458  C  CA    . ARG   A  1  347  ? -48.118 54.223  93.929  1.00 17.30 ? 345  ARG   A CA    1 
ATOM   2459  C  C     . ARG   A  1  347  ? -48.932 53.631  92.790  1.00 18.53 ? 345  ARG   A C     1 
ATOM   2460  O  O     . ARG   A  1  347  ? -50.124 53.913  92.708  1.00 17.13 ? 345  ARG   A O     1 
ATOM   2461  C  CB    . ARG   A  1  347  ? -48.006 55.738  93.755  1.00 17.29 ? 345  ARG   A CB    1 
ATOM   2462  C  CG    . ARG   A  1  347  ? -47.481 56.421  95.003  1.00 17.23 ? 345  ARG   A CG    1 
ATOM   2463  C  CD    . ARG   A  1  347  ? -47.103 57.845  94.706  1.00 16.35 ? 345  ARG   A CD    1 
ATOM   2464  N  NE    . ARG   A  1  347  ? -45.888 57.890  93.897  1.00 16.76 ? 345  ARG   A NE    1 
ATOM   2465  C  CZ    . ARG   A  1  347  ? -45.387 58.998  93.366  1.00 16.03 ? 345  ARG   A CZ    1 
ATOM   2466  N  NH1   . ARG   A  1  347  ? -45.973 60.175  93.542  1.00 17.12 ? 345  ARG   A NH1   1 
ATOM   2467  N  NH2   . ARG   A  1  347  ? -44.266 58.926  92.645  1.00 15.08 ? 345  ARG   A NH2   1 
ATOM   2468  N  N     . CYS   A  1  348  ? -48.339 52.803  91.944  1.00 16.77 ? 346  CYS   A N     1 
ATOM   2469  C  CA    . CYS   A  1  348  ? -48.974 52.330  90.715  1.00 18.51 ? 346  CYS   A CA    1 
ATOM   2470  C  C     . CYS   A  1  348  ? -50.418 51.856  90.866  1.00 17.69 ? 346  CYS   A C     1 
ATOM   2471  O  O     . CYS   A  1  348  ? -51.294 52.351  90.147  1.00 17.30 ? 346  CYS   A O     1 
ATOM   2472  C  CB    . CYS   A  1  348  ? -48.121 51.249  90.042  1.00 18.24 ? 346  CYS   A CB    1 
ATOM   2473  S  SG    . CYS   A  1  348  ? -48.596 50.981  88.331  1.00 21.35 ? 346  CYS   A SG    1 
ATOM   2474  N  N     . PRO   A  1  349  ? -50.724 50.896  91.736  1.00 17.87 ? 347  PRO   A N     1 
ATOM   2475  C  CA    . PRO   A  1  349  ? -52.129 50.443  91.805  1.00 18.45 ? 347  PRO   A CA    1 
ATOM   2476  C  C     . PRO   A  1  349  ? -53.085 51.537  92.241  1.00 17.34 ? 347  PRO   A C     1 
ATOM   2477  O  O     . PRO   A  1  349  ? -54.233 51.565  91.785  1.00 18.89 ? 347  PRO   A O     1 
ATOM   2478  C  CB    . PRO   A  1  349  ? -52.083 49.269  92.796  1.00 19.76 ? 347  PRO   A CB    1 
ATOM   2479  C  CG    . PRO   A  1  349  ? -50.855 49.497  93.603  1.00 21.53 ? 347  PRO   A CG    1 
ATOM   2480  C  CD    . PRO   A  1  349  ? -49.876 50.268  92.766  1.00 19.65 ? 347  PRO   A CD    1 
ATOM   2481  N  N     . PHE   A  1  350  ? -52.627 52.454  93.095  1.00 18.53 ? 348  PHE   A N     1 
ATOM   2482  C  CA    . PHE   A  1  350  ? -53.471 53.555  93.544  1.00 18.87 ? 348  PHE   A CA    1 
ATOM   2483  C  C     . PHE   A  1  350  ? -53.643 54.595  92.457  1.00 18.98 ? 348  PHE   A C     1 
ATOM   2484  O  O     . PHE   A  1  350  ? -54.717 55.193  92.331  1.00 18.13 ? 348  PHE   A O     1 
ATOM   2485  C  CB    . PHE   A  1  350  ? -52.875 54.161  94.804  1.00 19.05 ? 348  PHE   A CB    1 
ATOM   2486  C  CG    . PHE   A  1  350  ? -52.555 53.130  95.836  1.00 21.21 ? 348  PHE   A CG    1 
ATOM   2487  C  CD1   . PHE   A  1  350  ? -53.558 52.617  96.633  1.00 20.70 ? 348  PHE   A CD1   1 
ATOM   2488  C  CD2   . PHE   A  1  350  ? -51.274 52.630  95.971  1.00 21.58 ? 348  PHE   A CD2   1 
ATOM   2489  C  CE1   . PHE   A  1  350  ? -53.280 51.635  97.562  1.00 24.68 ? 348  PHE   A CE1   1 
ATOM   2490  C  CE2   . PHE   A  1  350  ? -50.993 51.641  96.895  1.00 22.64 ? 348  PHE   A CE2   1 
ATOM   2491  C  CZ    . PHE   A  1  350  ? -51.992 51.151  97.692  1.00 24.64 ? 348  PHE   A CZ    1 
ATOM   2492  N  N     . VAL   A  1  351  ? -52.609 54.797  91.650  1.00 16.84 ? 349  VAL   A N     1 
ATOM   2493  C  CA    . VAL   A  1  351  ? -52.748 55.644  90.475  1.00 15.40 ? 349  VAL   A CA    1 
ATOM   2494  C  C     . VAL   A  1  351  ? -53.773 55.046  89.526  1.00 17.98 ? 349  VAL   A C     1 
ATOM   2495  O  O     . VAL   A  1  351  ? -54.637 55.751  88.987  1.00 17.83 ? 349  VAL   A O     1 
ATOM   2496  C  CB    . VAL   A  1  351  ? -51.376 55.823  89.805  1.00 15.70 ? 349  VAL   A CB    1 
ATOM   2497  C  CG1   . VAL   A  1  351  ? -51.534 56.604  88.514  1.00 16.43 ? 349  VAL   A CG1   1 
ATOM   2498  C  CG2   . VAL   A  1  351  ? -50.439 56.553  90.752  1.00 18.06 ? 349  VAL   A CG2   1 
ATOM   2499  N  N     . LEU   A  1  352  ? -53.697 53.730  89.315  1.00 17.87 ? 350  LEU   A N     1 
ATOM   2500  C  CA    . LEU   A  1  352  ? -54.663 53.061  88.459  1.00 17.47 ? 350  LEU   A CA    1 
ATOM   2501  C  C     . LEU   A  1  352  ? -56.078 53.198  89.004  1.00 17.60 ? 350  LEU   A C     1 
ATOM   2502  O  O     . LEU   A  1  352  ? -57.015 53.429  88.232  1.00 19.00 ? 350  LEU   A O     1 
ATOM   2503  C  CB    . LEU   A  1  352  ? -54.282 51.596  88.285  1.00 16.79 ? 350  LEU   A CB    1 
ATOM   2504  C  CG    . LEU   A  1  352  ? -53.028 51.396  87.448  1.00 17.79 ? 350  LEU   A CG    1 
ATOM   2505  C  CD1   . LEU   A  1  352  ? -52.657 49.930  87.471  1.00 21.15 ? 350  LEU   A CD1   1 
ATOM   2506  C  CD2   . LEU   A  1  352  ? -53.280 51.870  86.029  1.00 20.40 ? 350  LEU   A CD2   1 
ATOM   2507  N  N     . ASP   A  1  353  ? -56.262 53.064  90.329  1.00 18.46 ? 351  ASP   A N     1 
ATOM   2508  C  CA    . ASP   A  1  353  ? -57.591 53.300  90.897  1.00 19.20 ? 351  ASP   A CA    1 
ATOM   2509  C  C     . ASP   A  1  353  ? -58.077 54.705  90.574  1.00 18.64 ? 351  ASP   A C     1 
ATOM   2510  O  O     . ASP   A  1  353  ? -59.245 54.906  90.220  1.00 18.02 ? 351  ASP   A O     1 
ATOM   2511  C  CB    . ASP   A  1  353  ? -57.577 53.120  92.414  1.00 19.65 ? 351  ASP   A CB    1 
ATOM   2512  C  CG    . ASP   A  1  353  ? -57.369 51.681  92.846  1.00 21.97 ? 351  ASP   A CG    1 
ATOM   2513  O  OD1   . ASP   A  1  353  ? -57.655 50.759  92.057  1.00 24.10 ? 351  ASP   A OD1   1 
ATOM   2514  O  OD2   . ASP   A  1  353  ? -56.924 51.477  93.991  1.00 25.70 ? 351  ASP   A OD2   1 
ATOM   2515  N  N     . PHE   A  1  354  ? -57.203 55.695  90.720  1.00 18.50 ? 352  PHE   A N     1 
ATOM   2516  C  CA    . PHE   A  1  354  ? -57.566 57.065  90.389  1.00 17.09 ? 352  PHE   A CA    1 
ATOM   2517  C  C     . PHE   A  1  354  ? -57.932 57.199  88.917  1.00 17.07 ? 352  PHE   A C     1 
ATOM   2518  O  O     . PHE   A  1  354  ? -58.954 57.804  88.577  1.00 17.59 ? 352  PHE   A O     1 
ATOM   2519  C  CB    . PHE   A  1  354  ? -56.419 58.009  90.747  1.00 17.71 ? 352  PHE   A CB    1 
ATOM   2520  C  CG    . PHE   A  1  354  ? -56.589 59.381  90.189  1.00 17.52 ? 352  PHE   A CG    1 
ATOM   2521  C  CD1   . PHE   A  1  354  ? -57.340 60.328  90.868  1.00 18.94 ? 352  PHE   A CD1   1 
ATOM   2522  C  CD2   . PHE   A  1  354  ? -56.037 59.715  88.964  1.00 19.50 ? 352  PHE   A CD2   1 
ATOM   2523  C  CE1   . PHE   A  1  354  ? -57.521 61.592  90.335  1.00 20.10 ? 352  PHE   A CE1   1 
ATOM   2524  C  CE2   . PHE   A  1  354  ? -56.214 60.967  88.429  1.00 20.03 ? 352  PHE   A CE2   1 
ATOM   2525  C  CZ    . PHE   A  1  354  ? -56.952 61.909  89.106  1.00 20.56 ? 352  PHE   A CZ    1 
ATOM   2526  N  N     . ILE   A  1  355  ? -57.117 56.625  88.030  1.00 15.98 ? 353  ILE   A N     1 
ATOM   2527  C  CA    . ILE   A  1  355  ? -57.365 56.767  86.598  1.00 16.17 ? 353  ILE   A CA    1 
ATOM   2528  C  C     . ILE   A  1  355  ? -58.651 56.072  86.192  1.00 18.17 ? 353  ILE   A C     1 
ATOM   2529  O  O     . ILE   A  1  355  ? -59.417 56.594  85.377  1.00 17.77 ? 353  ILE   A O     1 
ATOM   2530  C  CB    . ILE   A  1  355  ? -56.179 56.225  85.793  1.00 18.49 ? 353  ILE   A CB    1 
ATOM   2531  C  CG1   . ILE   A  1  355  ? -54.965 57.122  86.013  1.00 18.46 ? 353  ILE   A CG1   1 
ATOM   2532  C  CG2   . ILE   A  1  355  ? -56.549 56.113  84.318  1.00 18.50 ? 353  ILE   A CG2   1 
ATOM   2533  C  CD1   . ILE   A  1  355  ? -53.695 56.562  85.431  1.00 18.46 ? 353  ILE   A CD1   1 
ATOM   2534  N  N     . ILE   A  1  356  ? -58.868 54.852  86.686  1.00 17.56 ? 354  ILE   A N     1 
ATOM   2535  C  CA    . ILE   A  1  356  ? -60.095 54.140  86.353  1.00 17.19 ? 354  ILE   A CA    1 
ATOM   2536  C  C     . ILE   A  1  356  ? -61.303 54.934  86.811  1.00 18.33 ? 354  ILE   A C     1 
ATOM   2537  O  O     . ILE   A  1  356  ? -62.282 55.079  86.073  1.00 18.42 ? 354  ILE   A O     1 
ATOM   2538  C  CB    . ILE   A  1  356  ? -60.061 52.712  86.925  1.00 18.02 ? 354  ILE   A CB    1 
ATOM   2539  C  CG1   . ILE   A  1  356  ? -59.008 51.887  86.177  1.00 19.43 ? 354  ILE   A CG1   1 
ATOM   2540  C  CG2   . ILE   A  1  356  ? -61.454 52.072  86.859  1.00 23.01 ? 354  ILE   A CG2   1 
ATOM   2541  C  CD1   . ILE   A  1  356  ? -58.569 50.640  86.941  1.00 21.48 ? 354  ILE   A CD1   1 
ATOM   2542  N  N     . ASP   A  1  357  ? -61.220 55.524  87.999  1.00 17.84 ? 355  ASP   A N     1 
ATOM   2543  C  CA    . ASP   A  1  357  ? -62.320 56.350  88.471  1.00 19.22 ? 355  ASP   A CA    1 
ATOM   2544  C  C     . ASP   A  1  357  ? -62.474 57.608  87.621  1.00 17.61 ? 355  ASP   A C     1 
ATOM   2545  O  O     . ASP   A  1  357  ? -63.598 58.008  87.296  1.00 18.53 ? 355  ASP   A O     1 
ATOM   2546  C  CB    . ASP   A  1  357  ? -62.130 56.690  89.942  1.00 21.26 ? 355  ASP   A CB    1 
ATOM   2547  C  CG    . ASP   A  1  357  ? -63.166 57.655  90.434  1.00 21.30 ? 355  ASP   A CG    1 
ATOM   2548  O  OD1   . ASP   A  1  357  ? -64.286 57.202  90.750  1.00 24.73 ? 355  ASP   A OD1   1 
ATOM   2549  O  OD2   . ASP   A  1  357  ? -62.876 58.868  90.469  1.00 20.32 ? 355  ASP   A OD2   1 
ATOM   2550  N  N     . LEU   A  1  358  ? -61.360 58.234  87.229  1.00 16.63 ? 356  LEU   A N     1 
ATOM   2551  C  CA    . LEU   A  1  358  ? -61.450 59.386  86.338  1.00 15.37 ? 356  LEU   A CA    1 
ATOM   2552  C  C     . LEU   A  1  358  ? -62.087 59.003  85.011  1.00 17.85 ? 356  LEU   A C     1 
ATOM   2553  O  O     . LEU   A  1  358  ? -62.899 59.753  84.459  1.00 18.08 ? 356  LEU   A O     1 
ATOM   2554  C  CB    . LEU   A  1  358  ? -60.057 59.957  86.099  1.00 16.02 ? 356  LEU   A CB    1 
ATOM   2555  C  CG    . LEU   A  1  358  ? -59.967 61.099  85.106  1.00 16.23 ? 356  LEU   A CG    1 
ATOM   2556  C  CD1   . LEU   A  1  358  ? -60.816 62.292  85.546  1.00 19.05 ? 356  LEU   A CD1   1 
ATOM   2557  C  CD2   . LEU   A  1  358  ? -58.495 61.496  84.983  1.00 16.98 ? 356  LEU   A CD2   1 
ATOM   2558  N  N     . ALA   A  1  359  ? -61.737 57.829  84.487  1.00 17.04 ? 357  ALA   A N     1 
ATOM   2559  C  CA    . ALA   A  1  359  ? -62.358 57.358  83.259  1.00 18.22 ? 357  ALA   A CA    1 
ATOM   2560  C  C     . ALA   A  1  359  ? -63.859 57.221  83.440  1.00 18.37 ? 357  ALA   A C     1 
ATOM   2561  O  O     . ALA   A  1  359  ? -64.634 57.608  82.564  1.00 19.21 ? 357  ALA   A O     1 
ATOM   2562  C  CB    . ALA   A  1  359  ? -61.758 56.011  82.870  1.00 18.87 ? 357  ALA   A CB    1 
ATOM   2563  N  N     . ARG   A  1  360  ? -64.285 56.681  84.583  1.00 17.52 ? 358  ARG   A N     1 
ATOM   2564  C  CA    . ARG   A  1  360  ? -65.713 56.543  84.846  1.00 19.12 ? 358  ARG   A CA    1 
ATOM   2565  C  C     . ARG   A  1  360  ? -66.389 57.904  84.933  1.00 21.79 ? 358  ARG   A C     1 
ATOM   2566  O  O     . ARG   A  1  360  ? -67.432 58.132  84.310  1.00 23.33 ? 358  ARG   A O     1 
ATOM   2567  C  CB    . ARG   A  1  360  ? -65.922 55.749  86.132  1.00 21.03 ? 358  ARG   A CB    1 
ATOM   2568  C  CG    . ARG   A  1  360  ? -65.556 54.284  86.013  1.00 22.49 ? 358  ARG   A CG    1 
ATOM   2569  C  CD    . ARG   A  1  360  ? -66.040 53.492  87.232  1.00 26.07 ? 358  ARG   A CD    1 
ATOM   2570  N  NE    . ARG   A  1  360  ? -65.326 52.226  87.346  1.00 32.46 ? 358  ARG   A NE    1 
ATOM   2571  C  CZ    . ARG   A  1  360  ? -65.630 51.135  86.656  1.00 39.50 ? 358  ARG   A CZ    1 
ATOM   2572  N  NH1   . ARG   A  1  360  ? -66.671 51.102  85.837  1.00 38.43 ? 358  ARG   A NH1   1 
ATOM   2573  N  NH2   . ARG   A  1  360  ? -64.867 50.052  86.787  1.00 33.69 ? 358  ARG   A NH2   1 
ATOM   2574  N  N     . ARG   A  1  361  ? -65.807 58.823  85.706  1.00 19.42 ? 359  ARG   A N     1 
ATOM   2575  C  CA    . ARG   A  1  361  ? -66.410 60.143  85.894  1.00 19.25 ? 359  ARG   A CA    1 
ATOM   2576  C  C     . ARG   A  1  361  ? -66.478 60.916  84.589  1.00 19.94 ? 359  ARG   A C     1 
ATOM   2577  O  O     . ARG   A  1  361  ? -67.478 61.583  84.297  1.00 21.85 ? 359  ARG   A O     1 
ATOM   2578  C  CB    . ARG   A  1  361  ? -65.584 60.950  86.896  1.00 23.49 ? 359  ARG   A CB    1 
ATOM   2579  C  CG    . ARG   A  1  361  ? -65.680 60.478  88.325  1.00 23.87 ? 359  ARG   A CG    1 
ATOM   2580  C  CD    . ARG   A  1  361  ? -64.969 61.462  89.231  1.00 23.68 ? 359  ARG   A CD    1 
ATOM   2581  N  NE    . ARG   A  1  361  ? -63.515 61.345  89.187  1.00 23.70 ? 359  ARG   A NE    1 
ATOM   2582  C  CZ    . ARG   A  1  361  ? -62.676 62.337  88.919  1.00 22.05 ? 359  ARG   A CZ    1 
ATOM   2583  N  NH1   . ARG   A  1  361  ? -63.105 63.522  88.521  1.00 22.18 ? 359  ARG   A NH1   1 
ATOM   2584  N  NH2   . ARG   A  1  361  ? -61.370 62.141  89.076  1.00 21.51 ? 359  ARG   A NH2   1 
ATOM   2585  N  N     . SER   A  1  362  ? -65.412 60.865  83.801  1.00 18.80 ? 360  SER   A N     1 
ATOM   2586  C  CA    . SER   A  1  362  ? -65.358 61.642  82.575  1.00 16.32 ? 360  SER   A CA    1 
ATOM   2587  C  C     . SER   A  1  362  ? -66.051 60.955  81.410  1.00 19.63 ? 360  SER   A C     1 
ATOM   2588  O  O     . SER   A  1  362  ? -66.374 61.619  80.420  1.00 20.80 ? 360  SER   A O     1 
ATOM   2589  C  CB    . SER   A  1  362  ? -63.895 61.876  82.194  1.00 18.71 ? 360  SER   A CB    1 
ATOM   2590  O  OG    . SER   A  1  362  ? -63.251 60.645  81.878  1.00 17.57 ? 360  SER   A OG    1 
ATOM   2591  N  N     . GLY   A  1  363  ? -66.263 59.647  81.498  1.00 19.61 ? 361  GLY   A N     1 
ATOM   2592  C  CA    . GLY   A  1  363  ? -66.743 58.905  80.357  1.00 20.63 ? 361  GLY   A CA    1 
ATOM   2593  C  C     . GLY   A  1  363  ? -65.742 58.713  79.247  1.00 21.96 ? 361  GLY   A C     1 
ATOM   2594  O  O     . GLY   A  1  363  ? -66.139 58.314  78.145  1.00 23.62 ? 361  GLY   A O     1 
ATOM   2595  N  N     . ARG   A  1  364  ? -64.463 58.996  79.493  1.00 18.92 ? 362  ARG   A N     1 
ATOM   2596  C  CA    . ARG   A  1  364  ? -63.403 58.811  78.508  1.00 20.19 ? 362  ARG   A CA    1 
ATOM   2597  C  C     . ARG   A  1  364  ? -62.747 57.468  78.773  1.00 20.23 ? 362  ARG   A C     1 
ATOM   2598  O  O     . ARG   A  1  364  ? -62.369 57.176  79.911  1.00 20.23 ? 362  ARG   A O     1 
ATOM   2599  C  CB    . ARG   A  1  364  ? -62.318 59.876  78.656  1.00 22.24 ? 362  ARG   A CB    1 
ATOM   2600  C  CG    . ARG   A  1  364  ? -62.792 61.310  78.753  1.00 25.76 ? 362  ARG   A CG    1 
ATOM   2601  C  CD    . ARG   A  1  364  ? -62.727 62.028  77.430  1.00 20.06 ? 362  ARG   A CD    1 
ATOM   2602  N  NE    . ARG   A  1  364  ? -63.533 63.240  77.487  1.00 18.88 ? 362  ARG   A NE    1 
ATOM   2603  C  CZ    . ARG   A  1  364  ? -63.051 64.466  77.632  1.00 18.88 ? 362  ARG   A CZ    1 
ATOM   2604  N  NH1   . ARG   A  1  364  ? -61.747 64.704  77.618  1.00 17.27 ? 362  ARG   A NH1   1 
ATOM   2605  N  NH2   . ARG   A  1  364  ? -63.895 65.478  77.794  1.00 18.09 ? 362  ARG   A NH2   1 
ATOM   2606  N  N     . ARG   A  1  365  ? -62.584 56.670  77.725  1.00 18.68 ? 363  ARG   A N     1 
ATOM   2607  C  CA    . ARG   A  1  365  ? -61.935 55.374  77.888  1.00 17.57 ? 363  ARG   A CA    1 
ATOM   2608  C  C     . ARG   A  1  365  ? -60.434 55.624  77.830  1.00 18.27 ? 363  ARG   A C     1 
ATOM   2609  O  O     . ARG   A  1  365  ? -59.809 55.573  76.770  1.00 20.29 ? 363  ARG   A O     1 
ATOM   2610  C  CB    . ARG   A  1  365  ? -62.389 54.410  76.806  1.00 18.16 ? 363  ARG   A CB    1 
ATOM   2611  C  CG    . ARG   A  1  365  ? -61.856 53.026  77.033  1.00 19.34 ? 363  ARG   A CG    1 
ATOM   2612  C  CD    . ARG   A  1  365  ? -62.669 51.981  76.336  1.00 24.23 ? 363  ARG   A CD    1 
ATOM   2613  N  NE    . ARG   A  1  365  ? -62.149 50.661  76.661  1.00 21.37 ? 363  ARG   A NE    1 
ATOM   2614  C  CZ    . ARG   A  1  365  ? -61.449 49.917  75.820  1.00 19.72 ? 363  ARG   A CZ    1 
ATOM   2615  N  NH1   . ARG   A  1  365  ? -61.227 50.310  74.579  1.00 22.99 ? 363  ARG   A NH1   1 
ATOM   2616  N  NH2   . ARG   A  1  365  ? -60.980 48.746  76.229  1.00 19.22 ? 363  ARG   A NH2   1 
ATOM   2617  N  N     . ILE   A  1  366  ? -59.846 55.923  78.988  1.00 16.96 ? 364  ILE   A N     1 
ATOM   2618  C  CA    . ILE   A  1  366  ? -58.451 56.332  79.019  1.00 16.27 ? 364  ILE   A CA    1 
ATOM   2619  C  C     . ILE   A  1  366  ? -57.578 55.180  78.567  1.00 15.79 ? 364  ILE   A C     1 
ATOM   2620  O  O     . ILE   A  1  366  ? -57.747 54.038  79.008  1.00 15.70 ? 364  ILE   A O     1 
ATOM   2621  C  CB    . ILE   A  1  366  ? -58.078 56.841  80.414  1.00 16.37 ? 364  ILE   A CB    1 
ATOM   2622  C  CG1   . ILE   A  1  366  ? -58.956 58.051  80.762  1.00 20.59 ? 364  ILE   A CG1   1 
ATOM   2623  C  CG2   . ILE   A  1  366  ? -56.595 57.191  80.469  1.00 17.84 ? 364  ILE   A CG2   1 
ATOM   2624  C  CD1   . ILE   A  1  366  ? -58.756 58.570  82.168  1.00 19.99 ? 364  ILE   A CD1   1 
ATOM   2625  N  N     . MET   A  1  367  ? -56.635 55.472  77.677  1.00 16.90 ? 365  MET   A N     1 
ATOM   2626  C  CA    . MET   A  1  367  ? -55.664 54.472  77.264  1.00 17.02 ? 365  MET   A CA    1 
ATOM   2627  C  C     . MET   A  1  367  ? -54.563 54.453  78.307  1.00 16.93 ? 365  MET   A C     1 
ATOM   2628  O  O     . MET   A  1  367  ? -53.950 55.484  78.585  1.00 20.34 ? 365  MET   A O     1 
ATOM   2629  C  CB    . MET   A  1  367  ? -55.113 54.822  75.886  1.00 16.46 ? 365  MET   A CB    1 
ATOM   2630  C  CG    . MET   A  1  367  ? -56.222 55.075  74.877  1.00 18.20 ? 365  MET   A CG    1 
ATOM   2631  S  SD    . MET   A  1  367  ? -55.626 55.459  73.218  1.00 19.64 ? 365  MET   A SD    1 
ATOM   2632  C  CE    . MET   A  1  367  ? -55.474 53.843  72.459  1.00 23.70 ? 365  MET   A CE    1 
ATOM   2633  N  N     . VAL   A  1  368  ? -54.363 53.319  78.946  1.00 15.05 ? 366  VAL   A N     1 
ATOM   2634  C  CA    . VAL   A  1  368  ? -53.430 53.247  80.054  1.00 15.92 ? 366  VAL   A CA    1 
ATOM   2635  C  C     . VAL   A  1  368  ? -52.298 52.339  79.631  1.00 14.99 ? 366  VAL   A C     1 
ATOM   2636  O  O     . VAL   A  1  368  ? -52.488 51.127  79.468  1.00 15.65 ? 366  VAL   A O     1 
ATOM   2637  C  CB    . VAL   A  1  368  ? -54.089 52.744  81.340  1.00 16.36 ? 366  VAL   A CB    1 
ATOM   2638  C  CG1   . VAL   A  1  368  ? -53.041 52.688  82.443  1.00 17.18 ? 366  VAL   A CG1   1 
ATOM   2639  C  CG2   . VAL   A  1  368  ? -55.248 53.649  81.736  1.00 18.85 ? 366  VAL   A CG2   1 
ATOM   2640  N  N     . ARG   A  1  369  ? -51.109 52.911  79.462  1.00 14.90 ? 367  ARG   A N     1 
ATOM   2641  C  CA    . ARG   A  1  369  ? -49.940 52.112  79.149  1.00 16.30 ? 367  ARG   A CA    1 
ATOM   2642  C  C     . ARG   A  1  369  ? -49.281 51.712  80.457  1.00 16.08 ? 367  ARG   A C     1 
ATOM   2643  O  O     . ARG   A  1  369  ? -48.810 52.569  81.212  1.00 17.29 ? 367  ARG   A O     1 
ATOM   2644  C  CB    . ARG   A  1  369  ? -48.958 52.883  78.280  1.00 17.36 ? 367  ARG   A CB    1 
ATOM   2645  C  CG    . ARG   A  1  369  ? -47.766 52.016  77.909  1.00 17.58 ? 367  ARG   A CG    1 
ATOM   2646  C  CD    . ARG   A  1  369  ? -46.593 52.834  77.451  1.00 17.77 ? 367  ARG   A CD    1 
ATOM   2647  N  NE    . ARG   A  1  369  ? -46.899 53.483  76.192  1.00 15.92 ? 367  ARG   A NE    1 
ATOM   2648  C  CZ    . ARG   A  1  369  ? -46.351 54.626  75.804  1.00 17.77 ? 367  ARG   A CZ    1 
ATOM   2649  N  NH1   . ARG   A  1  369  ? -45.439 55.242  76.547  1.00 18.22 ? 367  ARG   A NH1   1 
ATOM   2650  N  NH2   . ARG   A  1  369  ? -46.725 55.161  74.644  1.00 17.09 ? 367  ARG   A NH2   1 
ATOM   2651  N  N     . LEU   A  1  370  ? -49.255 50.421  80.724  1.00 14.97 ? 368  LEU   A N     1 
ATOM   2652  C  CA    . LEU   A  1  370  ? -48.579 49.903  81.898  1.00 15.75 ? 368  LEU   A CA    1 
ATOM   2653  C  C     . LEU   A  1  370  ? -47.155 49.563  81.490  1.00 16.69 ? 368  LEU   A C     1 
ATOM   2654  O  O     . LEU   A  1  370  ? -46.939 48.766  80.569  1.00 16.63 ? 368  LEU   A O     1 
ATOM   2655  C  CB    . LEU   A  1  370  ? -49.301 48.673  82.441  1.00 17.86 ? 368  LEU   A CB    1 
ATOM   2656  C  CG    . LEU   A  1  370  ? -48.741 48.128  83.747  1.00 18.07 ? 368  LEU   A CG    1 
ATOM   2657  C  CD1   . LEU   A  1  370  ? -48.930 49.118  84.885  1.00 20.66 ? 368  LEU   A CD1   1 
ATOM   2658  C  CD2   . LEU   A  1  370  ? -49.412 46.801  84.067  1.00 19.74 ? 368  LEU   A CD2   1 
ATOM   2659  N  N     . VAL   A  1  371  ? -46.193 50.184  82.157  1.00 15.44 ? 369  VAL   A N     1 
ATOM   2660  C  CA    . VAL   A  1  371  ? -44.781 49.942  81.912  1.00 15.67 ? 369  VAL   A CA    1 
ATOM   2661  C  C     . VAL   A  1  371  ? -44.177 49.562  83.242  1.00 16.13 ? 369  VAL   A C     1 
ATOM   2662  O  O     . VAL   A  1  371  ? -44.795 49.720  84.292  1.00 17.15 ? 369  VAL   A O     1 
ATOM   2663  C  CB    . VAL   A  1  371  ? -44.055 51.175  81.335  1.00 15.50 ? 369  VAL   A CB    1 
ATOM   2664  C  CG1   . VAL   A  1  371  ? -44.753 51.688  80.099  1.00 15.81 ? 369  VAL   A CG1   1 
ATOM   2665  C  CG2   . VAL   A  1  371  ? -43.939 52.267  82.398  1.00 17.02 ? 369  VAL   A CG2   1 
ATOM   2666  N  N     . LYS   A  1  372  ? -42.937 49.088  83.203  1.00 16.04 ? 370  LYS   A N     1 
ATOM   2667  C  CA    . LYS   A  1  372  ? -42.234 48.925  84.469  1.00 16.78 ? 370  LYS   A CA    1 
ATOM   2668  C  C     . LYS   A  1  372  ? -41.637 50.250  84.937  1.00 18.19 ? 370  LYS   A C     1 
ATOM   2669  O  O     . LYS   A  1  372  ? -42.056 50.795  85.964  1.00 19.53 ? 370  LYS   A O     1 
ATOM   2670  C  CB    . LYS   A  1  372  ? -41.276 47.736  84.405  1.00 20.41 ? 370  LYS   A CB    1 
ATOM   2671  C  CG    . LYS   A  1  372  ? -42.092 46.444  84.287  1.00 19.94 ? 370  LYS   A CG    1 
ATOM   2672  C  CD    . LYS   A  1  372  ? -41.266 45.176  84.162  1.00 21.42 ? 370  LYS   A CD    1 
ATOM   2673  C  CE    . LYS   A  1  372  ? -42.194 44.008  83.815  1.00 20.52 ? 370  LYS   A CE    1 
ATOM   2674  N  NZ    . LYS   A  1  372  ? -41.434 42.742  83.579  1.00 21.02 ? 370  LYS   A NZ    1 
ATOM   2675  N  N     . GLY   A  1  373  ? -40.745 50.837  84.159  1.00 16.51 ? 371  GLY   A N     1 
ATOM   2676  C  CA    . GLY   A  1  373  ? -40.287 52.186  84.459  1.00 15.64 ? 371  GLY   A CA    1 
ATOM   2677  C  C     . GLY   A  1  373  ? -38.844 52.368  84.028  1.00 16.03 ? 371  GLY   A C     1 
ATOM   2678  O  O     . GLY   A  1  373  ? -38.020 51.465  84.096  1.00 17.32 ? 371  GLY   A O     1 
ATOM   2679  N  N     . ALA   A  1  374  ? -38.532 53.577  83.578  1.00 15.83 ? 372  ALA   A N     1 
ATOM   2680  C  CA    . ALA   A  1  374  ? -37.283 53.822  82.860  1.00 15.93 ? 372  ALA   A CA    1 
ATOM   2681  C  C     . ALA   A  1  374  ? -36.228 54.551  83.678  1.00 17.16 ? 372  ALA   A C     1 
ATOM   2682  O  O     . ALA   A  1  374  ? -35.106 54.730  83.183  1.00 18.95 ? 372  ALA   A O     1 
ATOM   2683  C  CB    . ALA   A  1  374  ? -37.570 54.618  81.585  1.00 16.72 ? 372  ALA   A CB    1 
ATOM   2684  N  N     . TYR   A  1  375  ? -36.536 54.973  84.902  1.00 16.57 ? 373  TYR   A N     1 
ATOM   2685  C  CA    . TYR   A  1  375  ? -35.661 55.875  85.641  1.00 15.81 ? 373  TYR   A CA    1 
ATOM   2686  C  C     . TYR   A  1  375  ? -35.150 55.252  86.926  1.00 14.89 ? 373  TYR   A C     1 
ATOM   2687  O  O     . TYR   A  1  375  ? -34.873 55.968  87.884  1.00 16.25 ? 373  TYR   A O     1 
ATOM   2688  C  CB    . TYR   A  1  375  ? -36.372 57.181  85.993  1.00 16.64 ? 373  TYR   A CB    1 
ATOM   2689  C  CG    . TYR   A  1  375  ? -36.945 57.925  84.825  1.00 15.74 ? 373  TYR   A CG    1 
ATOM   2690  C  CD1   . TYR   A  1  375  ? -38.143 57.519  84.246  1.00 15.50 ? 373  TYR   A CD1   1 
ATOM   2691  C  CD2   . TYR   A  1  375  ? -36.310 59.049  84.319  1.00 20.78 ? 373  TYR   A CD2   1 
ATOM   2692  C  CE1   . TYR   A  1  375  ? -38.681 58.204  83.176  1.00 17.54 ? 373  TYR   A CE1   1 
ATOM   2693  C  CE2   . TYR   A  1  375  ? -36.839 59.744  83.252  1.00 20.25 ? 373  TYR   A CE2   1 
ATOM   2694  C  CZ    . TYR   A  1  375  ? -38.027 59.319  82.694  1.00 20.81 ? 373  TYR   A CZ    1 
ATOM   2695  O  OH    . TYR   A  1  375  ? -38.556 60.016  81.633  1.00 21.75 ? 373  TYR   A OH    1 
ATOM   2696  N  N     . TRP   A  1  376  ? -35.053 53.929  86.965  1.00 14.06 ? 374  TRP   A N     1 
ATOM   2697  C  CA    . TRP   A  1  376  ? -34.840 53.247  88.236  1.00 15.71 ? 374  TRP   A CA    1 
ATOM   2698  C  C     . TRP   A  1  376  ? -33.587 53.740  88.957  1.00 17.10 ? 374  TRP   A C     1 
ATOM   2699  O  O     . TRP   A  1  376  ? -33.662 54.160  90.119  1.00 16.80 ? 374  TRP   A O     1 
ATOM   2700  C  CB    . TRP   A  1  376  ? -34.823 51.733  88.059  1.00 16.85 ? 374  TRP   A CB    1 
ATOM   2701  C  CG    . TRP   A  1  376  ? -34.668 51.042  89.366  1.00 16.67 ? 374  TRP   A CG    1 
ATOM   2702  C  CD1   . TRP   A  1  376  ? -35.652 50.810  90.284  1.00 17.51 ? 374  TRP   A CD1   1 
ATOM   2703  C  CD2   . TRP   A  1  376  ? -33.456 50.548  89.944  1.00 17.80 ? 374  TRP   A CD2   1 
ATOM   2704  N  NE1   . TRP   A  1  376  ? -35.136 50.174  91.382  1.00 16.49 ? 374  TRP   A NE1   1 
ATOM   2705  C  CE2   . TRP   A  1  376  ? -33.786 50.004  91.201  1.00 17.45 ? 374  TRP   A CE2   1 
ATOM   2706  C  CE3   . TRP   A  1  376  ? -32.129 50.493  89.513  1.00 19.31 ? 374  TRP   A CE3   1 
ATOM   2707  C  CZ2   . TRP   A  1  376  ? -32.836 49.414  92.033  1.00 19.63 ? 374  TRP   A CZ2   1 
ATOM   2708  C  CZ3   . TRP   A  1  376  ? -31.186 49.905  90.341  1.00 22.46 ? 374  TRP   A CZ3   1 
ATOM   2709  C  CH2   . TRP   A  1  376  ? -31.545 49.374  91.582  1.00 20.84 ? 374  TRP   A CH2   1 
ATOM   2710  N  N     . ASP   A  1  377  ? -32.419 53.678  88.295  1.00 16.89 ? 375  ASP   A N     1 
ATOM   2711  C  CA    A ASP   A  1  377  ? -31.162 54.119  88.916  0.53 17.88 ? 375  ASP   A CA    1 
ATOM   2712  C  CA    B ASP   A  1  377  ? -31.209 54.083  88.996  0.47 17.87 ? 375  ASP   A CA    1 
ATOM   2713  C  C     . ASP   A  1  377  ? -31.272 55.540  89.432  1.00 17.45 ? 375  ASP   A C     1 
ATOM   2714  O  O     . ASP   A  1  377  ? -30.781 55.876  90.517  1.00 18.00 ? 375  ASP   A O     1 
ATOM   2715  C  CB    A ASP   A  1  377  ? -30.032 54.127  87.878  0.53 20.13 ? 375  ASP   A CB    1 
ATOM   2716  C  CB    B ASP   A  1  377  ? -29.930 53.733  88.220  0.47 20.51 ? 375  ASP   A CB    1 
ATOM   2717  C  CG    A ASP   A  1  377  ? -29.631 52.753  87.413  0.53 25.59 ? 375  ASP   A CG    1 
ATOM   2718  C  CG    B ASP   A  1  377  ? -29.879 54.348  86.838  0.47 22.67 ? 375  ASP   A CG    1 
ATOM   2719  O  OD1   A ASP   A  1  377  ? -29.776 51.792  88.178  0.53 29.47 ? 375  ASP   A OD1   1 
ATOM   2720  O  OD1   B ASP   A  1  377  ? -30.214 55.538  86.691  0.47 26.72 ? 375  ASP   A OD1   1 
ATOM   2721  O  OD2   A ASP   A  1  377  ? -29.140 52.649  86.269  0.53 29.78 ? 375  ASP   A OD2   1 
ATOM   2722  O  OD2   B ASP   A  1  377  ? -29.456 53.641  85.896  0.47 26.60 ? 375  ASP   A OD2   1 
ATOM   2723  N  N     . ALA   A  1  378  ? -31.889 56.408  88.631  1.00 15.72 ? 376  ALA   A N     1 
ATOM   2724  C  CA    . ALA   A  1  378  ? -31.974 57.805  89.009  1.00 15.83 ? 376  ALA   A CA    1 
ATOM   2725  C  C     . ALA   A  1  378  ? -32.858 57.995  90.223  1.00 17.56 ? 376  ALA   A C     1 
ATOM   2726  O  O     . ALA   A  1  378  ? -32.580 58.870  91.049  1.00 16.19 ? 376  ALA   A O     1 
ATOM   2727  C  CB    . ALA   A  1  378  ? -32.494 58.630  87.835  1.00 16.48 ? 376  ALA   A CB    1 
ATOM   2728  N  N     . GLU   A  1  379  ? -33.920 57.198  90.350  1.00 16.03 ? 377  GLU   A N     1 
ATOM   2729  C  CA    . GLU   A  1  379  ? -34.778 57.336  91.516  1.00 14.83 ? 377  GLU   A CA    1 
ATOM   2730  C  C     . GLU   A  1  379  ? -34.061 56.883  92.771  1.00 16.45 ? 377  GLU   A C     1 
ATOM   2731  O  O     . GLU   A  1  379  ? -34.265 57.459  93.841  1.00 16.45 ? 377  GLU   A O     1 
ATOM   2732  C  CB    . GLU   A  1  379  ? -36.067 56.537  91.340  1.00 16.70 ? 377  GLU   A CB    1 
ATOM   2733  C  CG    . GLU   A  1  379  ? -36.912 56.941  90.148  1.00 16.07 ? 377  GLU   A CG    1 
ATOM   2734  C  CD    . GLU   A  1  379  ? -37.496 58.336  90.250  1.00 17.15 ? 377  GLU   A CD    1 
ATOM   2735  O  OE1   . GLU   A  1  379  ? -37.389 59.008  91.299  1.00 18.23 ? 377  GLU   A OE1   1 
ATOM   2736  O  OE2   . GLU   A  1  379  ? -38.114 58.757  89.253  1.00 17.96 ? 377  GLU   A OE2   1 
ATOM   2737  N  N     . ILE   A  1  380  ? -33.237 55.840  92.667  1.00 16.13 ? 378  ILE   A N     1 
ATOM   2738  C  CA    . ILE   A  1  380  ? -32.475 55.410  93.836  1.00 17.15 ? 378  ILE   A CA    1 
ATOM   2739  C  C     . ILE   A  1  380  ? -31.536 56.524  94.276  1.00 17.77 ? 378  ILE   A C     1 
ATOM   2740  O  O     . ILE   A  1  380  ? -31.488 56.899  95.455  1.00 17.25 ? 378  ILE   A O     1 
ATOM   2741  C  CB    . ILE   A  1  380  ? -31.713 54.107  93.534  1.00 16.23 ? 378  ILE   A CB    1 
ATOM   2742  C  CG1   . ILE   A  1  380  ? -32.658 52.987  93.111  1.00 18.37 ? 378  ILE   A CG1   1 
ATOM   2743  C  CG2   . ILE   A  1  380  ? -30.872 53.680  94.740  1.00 18.00 ? 378  ILE   A CG2   1 
ATOM   2744  C  CD1   . ILE   A  1  380  ? -33.788 52.733  94.103  1.00 18.81 ? 378  ILE   A CD1   1 
ATOM   2745  N  N     . LYS   A  1  381  ? -30.785 57.084  93.324  1.00 15.70 ? 379  LYS   A N     1 
ATOM   2746  C  CA    . LYS   A  1  381  ? -29.848 58.142  93.661  1.00 16.02 ? 379  LYS   A CA    1 
ATOM   2747  C  C     . LYS   A  1  381  ? -30.557 59.349  94.252  1.00 16.89 ? 379  LYS   A C     1 
ATOM   2748  O  O     . LYS   A  1  381  ? -30.100 59.918  95.248  1.00 17.01 ? 379  LYS   A O     1 
ATOM   2749  C  CB    . LYS   A  1  381  ? -29.062 58.545  92.418  1.00 16.67 ? 379  LYS   A CB    1 
ATOM   2750  C  CG    . LYS   A  1  381  ? -28.081 59.661  92.701  1.00 15.90 ? 379  LYS   A CG    1 
ATOM   2751  C  CD    . LYS   A  1  381  ? -27.223 59.943  91.475  1.00 16.44 ? 379  LYS   A CD    1 
ATOM   2752  C  CE    . LYS   A  1  381  ? -26.198 61.038  91.769  1.00 17.93 ? 379  LYS   A CE    1 
ATOM   2753  N  NZ    . LYS   A  1  381  ? -25.321 61.317  90.585  1.00 16.28 ? 379  LYS   A NZ    1 
ATOM   2754  N  N     . ARG   A  1  382  ? -31.687 59.743  93.662  1.00 15.60 ? 380  ARG   A N     1 
ATOM   2755  C  CA    . ARG   A  1  382  ? -32.345 60.963  94.105  1.00 16.86 ? 380  ARG   A CA    1 
ATOM   2756  C  C     . ARG   A  1  382  ? -32.840 60.820  95.530  1.00 16.73 ? 380  ARG   A C     1 
ATOM   2757  O  O     . ARG   A  1  382  ? -32.696 61.744  96.339  1.00 16.73 ? 380  ARG   A O     1 
ATOM   2758  C  CB    . ARG   A  1  382  ? -33.513 61.287  93.176  1.00 17.45 ? 380  ARG   A CB    1 
ATOM   2759  C  CG    . ARG   A  1  382  ? -34.206 62.589  93.480  1.00 23.36 ? 380  ARG   A CG    1 
ATOM   2760  C  CD    . ARG   A  1  382  ? -33.444 63.741  92.866  1.00 34.43 ? 380  ARG   A CD    1 
ATOM   2761  N  NE    . ARG   A  1  382  ? -32.671 64.459  93.868  1.00 35.83 ? 380  ARG   A NE    1 
ATOM   2762  C  CZ    . ARG   A  1  382  ? -31.644 65.254  93.601  1.00 36.58 ? 380  ARG   A CZ    1 
ATOM   2763  N  NH1   . ARG   A  1  382  ? -31.183 65.399  92.368  1.00 39.20 ? 380  ARG   A NH1   1 
ATOM   2764  N  NH2   . ARG   A  1  382  ? -31.069 65.926  94.595  1.00 34.14 ? 380  ARG   A NH2   1 
ATOM   2765  N  N     . ALA   A  1  383  ? -33.434 59.669  95.860  1.00 15.93 ? 381  ALA   A N     1 
ATOM   2766  C  CA    . ALA   A  1  383  ? -33.943 59.484  97.215  1.00 15.89 ? 381  ALA   A CA    1 
ATOM   2767  C  C     . ALA   A  1  383  ? -32.806 59.489  98.219  1.00 17.21 ? 381  ALA   A C     1 
ATOM   2768  O  O     . ALA   A  1  383  ? -32.944 60.033  99.322  1.00 18.06 ? 381  ALA   A O     1 
ATOM   2769  C  CB    . ALA   A  1  383  ? -34.736 58.185  97.314  1.00 17.67 ? 381  ALA   A CB    1 
ATOM   2770  N  N     . GLN   A  1  384  ? -31.667 58.906  97.849  1.00 16.06 ? 382  GLN   A N     1 
ATOM   2771  C  CA    . GLN   A  1  384  ? -30.515 58.918  98.742  1.00 16.43 ? 382  GLN   A CA    1 
ATOM   2772  C  C     . GLN   A  1  384  ? -29.992 60.335  98.922  1.00 16.98 ? 382  GLN   A C     1 
ATOM   2773  O  O     . GLN   A  1  384  ? -29.732 60.772  100.050 1.00 18.84 ? 382  GLN   A O     1 
ATOM   2774  C  CB    . GLN   A  1  384  ? -29.431 57.985  98.198  1.00 16.46 ? 382  GLN   A CB    1 
ATOM   2775  C  CG    . GLN   A  1  384  ? -29.798 56.519  98.302  1.00 16.84 ? 382  GLN   A CG    1 
ATOM   2776  C  CD    . GLN   A  1  384  ? -28.653 55.622  97.915  1.00 18.46 ? 382  GLN   A CD    1 
ATOM   2777  O  OE1   . GLN   A  1  384  ? -27.735 56.054  97.232  1.00 18.73 ? 382  GLN   A OE1   1 
ATOM   2778  N  NE2   . GLN   A  1  384  ? -28.694 54.368  98.360  1.00 19.78 ? 382  GLN   A NE2   1 
ATOM   2779  N  N     . LEU   A  1  385  ? -29.841 61.077  97.820  1.00 16.21 ? 383  LEU   A N     1 
ATOM   2780  C  CA    . LEU   A  1  385  ? -29.349 62.448  97.912  1.00 17.39 ? 383  LEU   A CA    1 
ATOM   2781  C  C     . LEU   A  1  385  ? -30.246 63.293  98.798  1.00 17.49 ? 383  LEU   A C     1 
ATOM   2782  O  O     . LEU   A  1  385  ? -29.761 64.120  99.576  1.00 19.10 ? 383  LEU   A O     1 
ATOM   2783  C  CB    . LEU   A  1  385  ? -29.283 63.083  96.522  1.00 16.78 ? 383  LEU   A CB    1 
ATOM   2784  C  CG    . LEU   A  1  385  ? -28.167 62.663  95.569  1.00 19.64 ? 383  LEU   A CG    1 
ATOM   2785  C  CD1   . LEU   A  1  385  ? -28.353 63.373  94.252  1.00 21.16 ? 383  LEU   A CD1   1 
ATOM   2786  C  CD2   . LEU   A  1  385  ? -26.822 63.007  96.161  1.00 21.63 ? 383  LEU   A CD2   1 
ATOM   2787  N  N     . ASP   A  1  386  ? -31.559 63.110  98.682  1.00 17.35 ? 384  ASP   A N     1 
ATOM   2788  C  CA    . ASP   A  1  386  ? -32.517 63.950  99.378  1.00 18.12 ? 384  ASP   A CA    1 
ATOM   2789  C  C     . ASP   A  1  386  ? -32.803 63.466  100.794 1.00 20.09 ? 384  ASP   A C     1 
ATOM   2790  O  O     . ASP   A  1  386  ? -33.577 64.110  101.514 1.00 20.88 ? 384  ASP   A O     1 
ATOM   2791  C  CB    . ASP   A  1  386  ? -33.808 64.058  98.552  1.00 19.49 ? 384  ASP   A CB    1 
ATOM   2792  C  CG    . ASP   A  1  386  ? -33.614 64.859  97.275  1.00 25.36 ? 384  ASP   A CG    1 
ATOM   2793  O  OD1   . ASP   A  1  386  ? -32.542 65.481  97.111  1.00 25.17 ? 384  ASP   A OD1   1 
ATOM   2794  O  OD2   . ASP   A  1  386  ? -34.525 64.865  96.420  1.00 25.96 ? 384  ASP   A OD2   1 
ATOM   2795  N  N     . GLY   A  1  387  ? -32.186 62.365  101.214 1.00 18.76 ? 385  GLY   A N     1 
ATOM   2796  C  CA    . GLY   A  1  387  ? -32.361 61.878  102.577 1.00 19.17 ? 385  GLY   A CA    1 
ATOM   2797  C  C     . GLY   A  1  387  ? -33.795 61.526  102.901 1.00 19.19 ? 385  GLY   A C     1 
ATOM   2798  O  O     . GLY   A  1  387  ? -34.266 61.806  104.010 1.00 20.43 ? 385  GLY   A O     1 
ATOM   2799  N  N     . LEU   A  1  388  ? -34.503 60.924  101.959 1.00 19.15 ? 386  LEU   A N     1 
ATOM   2800  C  CA    . LEU   A  1  388  ? -35.919 60.697  102.185 1.00 21.02 ? 386  LEU   A CA    1 
ATOM   2801  C  C     . LEU   A  1  388  ? -36.162 59.348  102.846 1.00 21.73 ? 386  LEU   A C     1 
ATOM   2802  O  O     . LEU   A  1  388  ? -35.260 58.525  103.019 1.00 21.48 ? 386  LEU   A O     1 
ATOM   2803  C  CB    . LEU   A  1  388  ? -36.698 60.861  100.882 1.00 19.50 ? 386  LEU   A CB    1 
ATOM   2804  C  CG    . LEU   A  1  388  ? -36.520 62.260  100.298 1.00 20.97 ? 386  LEU   A CG    1 
ATOM   2805  C  CD1   . LEU   A  1  388  ? -37.271 62.396  98.978  1.00 21.93 ? 386  LEU   A CD1   1 
ATOM   2806  C  CD2   . LEU   A  1  388  ? -36.948 63.343  101.275 1.00 21.70 ? 386  LEU   A CD2   1 
ATOM   2807  N  N     . ALA   A  1  389  ? -37.409 59.151  103.277 1.00 22.58 ? 387  ALA   A N     1 
ATOM   2808  C  CA    . ALA   A  1  389  ? -37.709 58.017  104.137 1.00 24.57 ? 387  ALA   A CA    1 
ATOM   2809  C  C     . ALA   A  1  389  ? -37.457 56.694  103.435 1.00 22.30 ? 387  ALA   A C     1 
ATOM   2810  O  O     . ALA   A  1  389  ? -37.019 55.727  104.062 1.00 24.21 ? 387  ALA   A O     1 
ATOM   2811  C  CB    . ALA   A  1  389  ? -39.158 58.100  104.609 1.00 27.57 ? 387  ALA   A CB    1 
ATOM   2812  N  N     . ASP   A  1  390  ? -37.731 56.627  102.143 1.00 20.12 ? 388  ASP   A N     1 
ATOM   2813  C  CA    . ASP   A  1  390  ? -37.655 55.377  101.399 1.00 21.86 ? 388  ASP   A CA    1 
ATOM   2814  C  C     . ASP   A  1  390  ? -37.691 55.756  99.926  1.00 18.59 ? 388  ASP   A C     1 
ATOM   2815  O  O     . ASP   A  1  390  ? -37.737 56.938  99.572  1.00 18.80 ? 388  ASP   A O     1 
ATOM   2816  C  CB    . ASP   A  1  390  ? -38.825 54.468  101.784 1.00 21.63 ? 388  ASP   A CB    1 
ATOM   2817  C  CG    . ASP   A  1  390  ? -38.531 52.993  101.587 1.00 22.67 ? 388  ASP   A CG    1 
ATOM   2818  O  OD1   . ASP   A  1  390  ? -37.863 52.618  100.600 1.00 23.56 ? 388  ASP   A OD1   1 
ATOM   2819  O  OD2   . ASP   A  1  390  ? -38.978 52.187  102.435 1.00 25.92 ? 388  ASP   A OD2   1 
ATOM   2820  N  N     . PHE   A  1  391  ? -37.634 54.767  99.087  1.00 17.81 ? 389  PHE   A N     1 
ATOM   2821  C  CA    . PHE   A  1  391  ? -37.666 54.988  97.654  1.00 18.36 ? 389  PHE   A CA    1 
ATOM   2822  C  C     . PHE   A  1  391  ? -39.097 55.023  97.152  1.00 18.52 ? 389  PHE   A C     1 
ATOM   2823  O  O     . PHE   A  1  391  ? -39.993 54.429  97.759  1.00 19.48 ? 389  PHE   A O     1 
ATOM   2824  C  CB    . PHE   A  1  391  ? -36.912 53.866  96.955  1.00 18.73 ? 389  PHE   A CB    1 
ATOM   2825  C  CG    . PHE   A  1  391  ? -35.506 53.763  97.423  1.00 17.35 ? 389  PHE   A CG    1 
ATOM   2826  C  CD1   . PHE   A  1  391  ? -34.593 54.709  97.029  1.00 17.62 ? 389  PHE   A CD1   1 
ATOM   2827  C  CD2   . PHE   A  1  391  ? -35.128 52.794  98.335  1.00 18.21 ? 389  PHE   A CD2   1 
ATOM   2828  C  CE1   . PHE   A  1  391  ? -33.293 54.667  97.482  1.00 19.54 ? 389  PHE   A CE1   1 
ATOM   2829  C  CE2   . PHE   A  1  391  ? -33.831 52.745  98.805  1.00 19.14 ? 389  PHE   A CE2   1 
ATOM   2830  C  CZ    . PHE   A  1  391  ? -32.916 53.682  98.381  1.00 20.05 ? 389  PHE   A CZ    1 
ATOM   2831  N  N     . PRO   A  1  392  ? -39.332 55.744  96.059  1.00 17.57 ? 390  PRO   A N     1 
ATOM   2832  C  CA    . PRO   A  1  392  ? -40.656 55.723  95.432  1.00 16.75 ? 390  PRO   A CA    1 
ATOM   2833  C  C     . PRO   A  1  392  ? -40.803 54.597  94.425  1.00 17.44 ? 390  PRO   A C     1 
ATOM   2834  O  O     . PRO   A  1  392  ? -41.852 54.493  93.775  1.00 17.56 ? 390  PRO   A O     1 
ATOM   2835  C  CB    . PRO   A  1  392  ? -40.699 57.081  94.729  1.00 16.79 ? 390  PRO   A CB    1 
ATOM   2836  C  CG    . PRO   A  1  392  ? -39.268 57.274  94.281  1.00 16.47 ? 390  PRO   A CG    1 
ATOM   2837  C  CD    . PRO   A  1  392  ? -38.415 56.687  95.393  1.00 16.28 ? 390  PRO   A CD    1 
ATOM   2838  N  N     . VAL   A  1  393  ? -39.775 53.755  94.304  1.00 17.59 ? 391  VAL   A N     1 
ATOM   2839  C  CA    . VAL   A  1  393  ? -39.785 52.601  93.423  1.00 17.22 ? 391  VAL   A CA    1 
ATOM   2840  C  C     . VAL   A  1  393  ? -39.336 51.396  94.229  1.00 17.31 ? 391  VAL   A C     1 
ATOM   2841  O  O     . VAL   A  1  393  ? -38.712 51.523  95.282  1.00 18.77 ? 391  VAL   A O     1 
ATOM   2842  C  CB    . VAL   A  1  393  ? -38.870 52.786  92.199  1.00 15.27 ? 391  VAL   A CB    1 
ATOM   2843  C  CG1   . VAL   A  1  393  ? -39.402 53.888  91.297  1.00 17.82 ? 391  VAL   A CG1   1 
ATOM   2844  C  CG2   . VAL   A  1  393  ? -37.444 53.096  92.645  1.00 17.27 ? 391  VAL   A CG2   1 
ATOM   2845  N  N     . PHE   A  1  394  ? -39.677 50.219  93.725  1.00 17.60 ? 392  PHE   A N     1 
ATOM   2846  C  CA    . PHE   A  1  394  ? -39.175 48.995  94.320  1.00 16.06 ? 392  PHE   A CA    1 
ATOM   2847  C  C     . PHE   A  1  394  ? -37.668 48.912  94.124  1.00 17.51 ? 392  PHE   A C     1 
ATOM   2848  O  O     . PHE   A  1  394  ? -37.084 49.600  93.283  1.00 17.92 ? 392  PHE   A O     1 
ATOM   2849  C  CB    . PHE   A  1  394  ? -39.887 47.801  93.701  1.00 19.18 ? 392  PHE   A CB    1 
ATOM   2850  C  CG    . PHE   A  1  394  ? -41.355 47.843  93.925  1.00 18.23 ? 392  PHE   A CG    1 
ATOM   2851  C  CD1   . PHE   A  1  394  ? -41.858 47.730  95.208  1.00 19.86 ? 392  PHE   A CD1   1 
ATOM   2852  C  CD2   . PHE   A  1  394  ? -42.222 48.048  92.879  1.00 19.12 ? 392  PHE   A CD2   1 
ATOM   2853  C  CE1   . PHE   A  1  394  ? -43.205 47.805  95.439  1.00 18.74 ? 392  PHE   A CE1   1 
ATOM   2854  C  CE2   . PHE   A  1  394  ? -43.578 48.121  93.100  1.00 18.59 ? 392  PHE   A CE2   1 
ATOM   2855  C  CZ    . PHE   A  1  394  ? -44.069 47.993  94.386  1.00 19.18 ? 392  PHE   A CZ    1 
ATOM   2856  N  N     . THR   A  1  395  ? -37.030 48.083  94.946  1.00 18.14 ? 393  THR   A N     1 
ATOM   2857  C  CA    . THR   A  1  395  ? -35.587 47.914  94.866  1.00 19.77 ? 393  THR   A CA    1 
ATOM   2858  C  C     . THR   A  1  395  ? -35.173 46.524  94.432  1.00 20.49 ? 393  THR   A C     1 
ATOM   2859  O  O     . THR   A  1  395  ? -33.988 46.309  94.164  1.00 19.89 ? 393  THR   A O     1 
ATOM   2860  C  CB    . THR   A  1  395  ? -34.903 48.243  96.197  1.00 20.62 ? 393  THR   A CB    1 
ATOM   2861  O  OG1   . THR   A  1  395  ? -35.403 47.366  97.211  1.00 20.62 ? 393  THR   A OG1   1 
ATOM   2862  C  CG2   . THR   A  1  395  ? -35.148 49.690  96.585  1.00 21.83 ? 393  THR   A CG2   1 
ATOM   2863  N  N     . ARG   A  1  396  ? -36.101 45.582  94.358  1.00 20.20 ? 394  ARG   A N     1 
ATOM   2864  C  CA    . ARG   A  1  396  ? -35.838 44.278  93.777  1.00 21.93 ? 394  ARG   A CA    1 
ATOM   2865  C  C     . ARG   A  1  396  ? -36.629 44.170  92.492  1.00 19.81 ? 394  ARG   A C     1 
ATOM   2866  O  O     . ARG   A  1  396  ? -37.825 44.472  92.471  1.00 19.92 ? 394  ARG   A O     1 
ATOM   2867  C  CB    . ARG   A  1  396  ? -36.247 43.154  94.719  1.00 23.33 ? 394  ARG   A CB    1 
ATOM   2868  C  CG    . ARG   A  1  396  ? -35.436 43.105  95.981  1.00 24.47 ? 394  ARG   A CG    1 
ATOM   2869  C  CD    . ARG   A  1  396  ? -35.758 41.850  96.775  1.00 26.78 ? 394  ARG   A CD    1 
ATOM   2870  N  NE    . ARG   A  1  396  ? -35.185 41.922  98.110  1.00 30.53 ? 394  ARG   A NE    1 
ATOM   2871  C  CZ    . ARG   A  1  396  ? -34.347 41.030  98.616  1.00 34.75 ? 394  ARG   A CZ    1 
ATOM   2872  N  NH1   . ARG   A  1  396  ? -34.031 39.928  97.954  1.00 37.03 ? 394  ARG   A NH1   1 
ATOM   2873  N  NH2   . ARG   A  1  396  ? -33.819 41.248  99.816  1.00 30.45 ? 394  ARG   A NH2   1 
ATOM   2874  N  N     . LYS   A  1  397  ? -35.954 43.759  91.425  1.00 20.95 ? 395  LYS   A N     1 
ATOM   2875  C  CA    . LYS   A  1  397  ? -36.594 43.716  90.121  1.00 21.58 ? 395  LYS   A CA    1 
ATOM   2876  C  C     . LYS   A  1  397  ? -37.835 42.833  90.147  1.00 20.79 ? 395  LYS   A C     1 
ATOM   2877  O  O     . LYS   A  1  397  ? -38.842 43.135  89.494  1.00 19.89 ? 395  LYS   A O     1 
ATOM   2878  C  CB    . LYS   A  1  397  ? -35.578 43.243  89.082  1.00 24.10 ? 395  LYS   A CB    1 
ATOM   2879  C  CG    . LYS   A  1  397  ? -35.975 43.514  87.654  1.00 23.42 ? 395  LYS   A CG    1 
ATOM   2880  C  CD    . LYS   A  1  397  ? -36.656 42.320  87.039  1.00 22.71 ? 395  LYS   A CD    1 
ATOM   2881  C  CE    . LYS   A  1  397  ? -37.143 42.668  85.643  1.00 23.07 ? 395  LYS   A CE    1 
ATOM   2882  N  NZ    . LYS   A  1  397  ? -37.759 41.496  84.992  1.00 24.65 ? 395  LYS   A NZ    1 
ATOM   2883  N  N     . ILE   A  1  398  ? -37.792 41.741  90.912  1.00 20.86 ? 396  ILE   A N     1 
ATOM   2884  C  CA    . ILE   A  1  398  ? -38.924 40.828  90.942  1.00 22.87 ? 396  ILE   A CA    1 
ATOM   2885  C  C     . ILE   A  1  398  ? -40.150 41.505  91.545  1.00 19.78 ? 396  ILE   A C     1 
ATOM   2886  O  O     . ILE   A  1  398  ? -41.296 41.149  91.227  1.00 21.80 ? 396  ILE   A O     1 
ATOM   2887  C  CB    . ILE   A  1  398  ? -38.511 39.537  91.676  1.00 24.92 ? 396  ILE   A CB    1 
ATOM   2888  C  CG1   . ILE   A  1  398  ? -39.499 38.419  91.387  1.00 30.60 ? 396  ILE   A CG1   1 
ATOM   2889  C  CG2   . ILE   A  1  398  ? -38.371 39.783  93.168  1.00 25.41 ? 396  ILE   A CG2   1 
ATOM   2890  C  CD1   . ILE   A  1  398  ? -38.917 37.052  91.626  1.00 31.25 ? 396  ILE   A CD1   1 
ATOM   2891  N  N     . HIS   A  1  399  ? -39.936 42.507  92.393  1.00 20.94 ? 397  HIS   A N     1 
ATOM   2892  C  CA    . HIS   A  1  399  ? -41.062 43.237  92.958  1.00 20.97 ? 397  HIS   A CA    1 
ATOM   2893  C  C     . HIS   A  1  399  ? -41.778 44.028  91.883  1.00 20.27 ? 397  HIS   A C     1 
ATOM   2894  O  O     . HIS   A  1  399  ? -43.012 44.054  91.835  1.00 20.84 ? 397  HIS   A O     1 
ATOM   2895  C  CB    . HIS   A  1  399  ? -40.575 44.164  94.065  1.00 21.14 ? 397  HIS   A CB    1 
ATOM   2896  C  CG    . HIS   A  1  399  ? -40.064 43.434  95.264  1.00 21.82 ? 397  HIS   A CG    1 
ATOM   2897  N  ND1   . HIS   A  1  399  ? -39.406 44.063  96.296  1.00 21.93 ? 397  HIS   A ND1   1 
ATOM   2898  C  CD2   . HIS   A  1  399  ? -40.111 42.120  95.589  1.00 24.91 ? 397  HIS   A CD2   1 
ATOM   2899  C  CE1   . HIS   A  1  399  ? -39.075 43.168  97.211  1.00 23.53 ? 397  HIS   A CE1   1 
ATOM   2900  N  NE2   . HIS   A  1  399  ? -39.486 41.982  96.803  1.00 24.74 ? 397  HIS   A NE2   1 
ATOM   2901  N  N     . THR   A  1  400  ? -41.013 44.676  91.009  1.00 19.63 ? 398  THR   A N     1 
ATOM   2902  C  CA    . THR   A  1  400  ? -41.616 45.361  89.876  1.00 17.56 ? 398  THR   A CA    1 
ATOM   2903  C  C     . THR   A  1  400  ? -42.407 44.395  89.002  1.00 18.53 ? 398  THR   A C     1 
ATOM   2904  O  O     . THR   A  1  400  ? -43.502 44.728  88.528  1.00 17.61 ? 398  THR   A O     1 
ATOM   2905  C  CB    . THR   A  1  400  ? -40.515 46.058  89.084  1.00 19.66 ? 398  THR   A CB    1 
ATOM   2906  O  OG1   . THR   A  1  400  ? -39.960 47.096  89.894  1.00 18.54 ? 398  THR   A OG1   1 
ATOM   2907  C  CG2   . THR   A  1  400  ? -41.071 46.669  87.806  1.00 18.82 ? 398  THR   A CG2   1 
ATOM   2908  N  N     . ASP   A  1  401  ? -41.891 43.179  88.801  1.00 18.38 ? 399  ASP   A N     1 
ATOM   2909  C  CA    . ASP   A  1  401  ? -42.608 42.220  87.967  1.00 20.02 ? 399  ASP   A CA    1 
ATOM   2910  C  C     . ASP   A  1  401  ? -43.940 41.843  88.599  1.00 18.83 ? 399  ASP   A C     1 
ATOM   2911  O  O     . ASP   A  1  401  ? -44.963 41.760  87.909  1.00 19.30 ? 399  ASP   A O     1 
ATOM   2912  C  CB    . ASP   A  1  401  ? -41.756 40.970  87.724  1.00 20.10 ? 399  ASP   A CB    1 
ATOM   2913  C  CG    . ASP   A  1  401  ? -40.556 41.242  86.836  1.00 22.30 ? 399  ASP   A CG    1 
ATOM   2914  O  OD1   . ASP   A  1  401  ? -40.615 42.195  86.037  1.00 22.39 ? 399  ASP   A OD1   1 
ATOM   2915  O  OD2   . ASP   A  1  401  ? -39.558 40.503  86.939  1.00 25.44 ? 399  ASP   A OD2   1 
ATOM   2916  N  N     . VAL   A  1  402  ? -43.939 41.596  89.911  1.00 19.37 ? 400  VAL   A N     1 
ATOM   2917  C  CA    . VAL   A  1  402  ? -45.181 41.269  90.604  1.00 19.42 ? 400  VAL   A CA    1 
ATOM   2918  C  C     . VAL   A  1  402  ? -46.132 42.452  90.548  1.00 19.14 ? 400  VAL   A C     1 
ATOM   2919  O  O     . VAL   A  1  402  ? -47.330 42.297  90.274  1.00 18.26 ? 400  VAL   A O     1 
ATOM   2920  C  CB    . VAL   A  1  402  ? -44.892 40.848  92.054  1.00 19.54 ? 400  VAL   A CB    1 
ATOM   2921  C  CG1   . VAL   A  1  402  ? -46.203 40.660  92.814  1.00 20.54 ? 400  VAL   A CG1   1 
ATOM   2922  C  CG2   . VAL   A  1  402  ? -44.080 39.572  92.074  1.00 24.04 ? 400  VAL   A CG2   1 
ATOM   2923  N  N     . SER   A  1  403  ? -45.608 43.652  90.808  1.00 19.68 ? 401  SER   A N     1 
ATOM   2924  C  CA    . SER   A  1  403  ? -46.425 44.854  90.717  1.00 20.34 ? 401  SER   A CA    1 
ATOM   2925  C  C     . SER   A  1  403  ? -47.067 44.974  89.343  1.00 20.17 ? 401  SER   A C     1 
ATOM   2926  O  O     . SER   A  1  403  ? -48.267 45.242  89.227  1.00 18.24 ? 401  SER   A O     1 
ATOM   2927  C  CB    . SER   A  1  403  ? -45.565 46.077  91.016  1.00 21.21 ? 401  SER   A CB    1 
ATOM   2928  O  OG    . SER   A  1  403  ? -46.295 47.263  90.789  1.00 18.73 ? 401  SER   A OG    1 
ATOM   2929  N  N     . TYR   A  1  404  ? -46.290 44.719  88.293  1.00 18.69 ? 402  TYR   A N     1 
ATOM   2930  C  CA    . TYR   A  1  404  ? -46.815 44.817  86.941  1.00 18.78 ? 402  TYR   A CA    1 
ATOM   2931  C  C     . TYR   A  1  404  ? -47.971 43.851  86.735  1.00 19.14 ? 402  TYR   A C     1 
ATOM   2932  O  O     . TYR   A  1  404  ? -49.028 44.230  86.224  1.00 18.10 ? 402  TYR   A O     1 
ATOM   2933  C  CB    . TYR   A  1  404  ? -45.678 44.542  85.962  1.00 17.95 ? 402  TYR   A CB    1 
ATOM   2934  C  CG    . TYR   A  1  404  ? -45.995 44.876  84.534  1.00 18.03 ? 402  TYR   A CG    1 
ATOM   2935  C  CD1   . TYR   A  1  404  ? -46.764 44.022  83.758  1.00 18.20 ? 402  TYR   A CD1   1 
ATOM   2936  C  CD2   . TYR   A  1  404  ? -45.518 46.039  83.956  1.00 17.05 ? 402  TYR   A CD2   1 
ATOM   2937  C  CE1   . TYR   A  1  404  ? -47.050 44.319  82.447  1.00 19.04 ? 402  TYR   A CE1   1 
ATOM   2938  C  CE2   . TYR   A  1  404  ? -45.799 46.345  82.626  1.00 18.11 ? 402  TYR   A CE2   1 
ATOM   2939  C  CZ    . TYR   A  1  404  ? -46.560 45.477  81.883  1.00 17.91 ? 402  TYR   A CZ    1 
ATOM   2940  O  OH    . TYR   A  1  404  ? -46.863 45.751  80.579  1.00 19.50 ? 402  TYR   A OH    1 
ATOM   2941  N  N     . ILE   A  1  405  ? -47.793 42.595  87.147  1.00 20.16 ? 403  ILE   A N     1 
ATOM   2942  C  CA    . ILE   A  1  405  ? -48.841 41.605  86.942  1.00 21.91 ? 403  ILE   A CA    1 
ATOM   2943  C  C     . ILE   A  1  405  ? -50.066 41.933  87.787  1.00 18.50 ? 403  ILE   A C     1 
ATOM   2944  O  O     . ILE   A  1  405  ? -51.202 41.808  87.323  1.00 20.23 ? 403  ILE   A O     1 
ATOM   2945  C  CB    . ILE   A  1  405  ? -48.294 40.190  87.199  1.00 21.12 ? 403  ILE   A CB    1 
ATOM   2946  C  CG1   . ILE   A  1  405  ? -47.188 39.891  86.192  1.00 24.88 ? 403  ILE   A CG1   1 
ATOM   2947  C  CG2   . ILE   A  1  405  ? -49.399 39.164  87.075  1.00 24.29 ? 403  ILE   A CG2   1 
ATOM   2948  C  CD1   . ILE   A  1  405  ? -46.364 38.673  86.520  1.00 31.32 ? 403  ILE   A CD1   1 
ATOM   2949  N  N     . ALA   A  1  406  ? -49.850 42.395  89.020  1.00 20.38 ? 404  ALA   A N     1 
ATOM   2950  C  CA    . ALA   A  1  406  ? -50.972 42.808  89.861  1.00 19.62 ? 404  ALA   A CA    1 
ATOM   2951  C  C     . ALA   A  1  406  ? -51.735 43.956  89.224  1.00 21.19 ? 404  ALA   A C     1 
ATOM   2952  O  O     . ALA   A  1  406  ? -52.972 43.976  89.231  1.00 22.29 ? 404  ALA   A O     1 
ATOM   2953  C  CB    . ALA   A  1  406  ? -50.447 43.257  91.218  1.00 20.32 ? 404  ALA   A CB    1 
ATOM   2954  N  N     . CYS   A  1  407  ? -51.011 44.934  88.681  1.00 20.48 ? 405  CYS   A N     1 
ATOM   2955  C  CA    . CYS   A  1  407  ? -51.662 46.077  88.059  1.00 18.88 ? 405  CYS   A CA    1 
ATOM   2956  C  C     . CYS   A  1  407  ? -52.367 45.682  86.768  1.00 20.29 ? 405  CYS   A C     1 
ATOM   2957  O  O     . CYS   A  1  407  ? -53.414 46.247  86.432  1.00 19.24 ? 405  CYS   A O     1 
ATOM   2958  C  CB    . CYS   A  1  407  ? -50.638 47.191  87.852  1.00 19.48 ? 405  CYS   A CB    1 
ATOM   2959  S  SG    . CYS   A  1  407  ? -50.157 47.936  89.438  1.00 24.22 ? 405  CYS   A SG    1 
ATOM   2960  N  N     . ALA   A  1  408  ? -51.828 44.697  86.050  1.00 19.24 ? 406  ALA   A N     1 
ATOM   2961  C  CA    . ALA   A  1  408  ? -52.519 44.197  84.868  1.00 19.50 ? 406  ALA   A CA    1 
ATOM   2962  C  C     . ALA   A  1  408  ? -53.837 43.543  85.239  1.00 18.22 ? 406  ALA   A C     1 
ATOM   2963  O  O     . ALA   A  1  408  ? -54.820 43.661  84.503  1.00 20.66 ? 406  ALA   A O     1 
ATOM   2964  C  CB    . ALA   A  1  408  ? -51.633 43.210  84.113  1.00 21.00 ? 406  ALA   A CB    1 
ATOM   2965  N  N     . ALA   A  1  409  ? -53.870 42.829  86.365  1.00 20.31 ? 407  ALA   A N     1 
ATOM   2966  C  CA    . ALA   A  1  409  ? -55.128 42.241  86.814  1.00 20.22 ? 407  ALA   A CA    1 
ATOM   2967  C  C     . ALA   A  1  409  ? -56.162 43.321  87.083  1.00 21.32 ? 407  ALA   A C     1 
ATOM   2968  O  O     . ALA   A  1  409  ? -57.335 43.173  86.725  1.00 21.89 ? 407  ALA   A O     1 
ATOM   2969  C  CB    . ALA   A  1  409  ? -54.901 41.391  88.068  1.00 21.70 ? 407  ALA   A CB    1 
ATOM   2970  N  N     . LYS   A  1  410  ? -55.731 44.432  87.683  1.00 21.81 ? 408  LYS   A N     1 
ATOM   2971  C  CA    . LYS   A  1  410  ? -56.641 45.540  87.943  1.00 20.17 ? 408  LYS   A CA    1 
ATOM   2972  C  C     . LYS   A  1  410  ? -57.138 46.155  86.640  1.00 18.01 ? 408  LYS   A C     1 
ATOM   2973  O  O     . LYS   A  1  410  ? -58.332 46.426  86.482  1.00 20.33 ? 408  LYS   A O     1 
ATOM   2974  C  CB    . LYS   A  1  410  ? -55.920 46.579  88.806  1.00 20.23 ? 408  LYS   A CB    1 
ATOM   2975  C  CG    . LYS   A  1  410  ? -56.731 47.829  89.105  1.00 22.30 ? 408  LYS   A CG    1 
ATOM   2976  C  CD    . LYS   A  1  410  ? -55.915 48.818  89.916  1.00 22.39 ? 408  LYS   A CD    1 
ATOM   2977  C  CE    . LYS   A  1  410  ? -55.564 48.295  91.295  1.00 23.74 ? 408  LYS   A CE    1 
ATOM   2978  N  NZ    . LYS   A  1  410  ? -56.749 48.279  92.197  1.00 26.83 ? 408  LYS   A NZ    1 
ATOM   2979  N  N     . LEU   A  1  411  ? -56.224 46.396  85.696  1.00 17.93 ? 409  LEU   A N     1 
ATOM   2980  C  CA    . LEU   A  1  411  ? -56.607 46.938  84.397  1.00 17.87 ? 409  LEU   A CA    1 
ATOM   2981  C  C     . LEU   A  1  411  ? -57.539 46.000  83.639  1.00 19.14 ? 409  LEU   A C     1 
ATOM   2982  O  O     . LEU   A  1  411  ? -58.510 46.449  83.018  1.00 19.13 ? 409  LEU   A O     1 
ATOM   2983  C  CB    . LEU   A  1  411  ? -55.350 47.213  83.570  1.00 18.40 ? 409  LEU   A CB    1 
ATOM   2984  C  CG    . LEU   A  1  411  ? -54.636 48.495  83.980  1.00 18.44 ? 409  LEU   A CG    1 
ATOM   2985  C  CD1   . LEU   A  1  411  ? -53.216 48.551  83.398  1.00 18.63 ? 409  LEU   A CD1   1 
ATOM   2986  C  CD2   . LEU   A  1  411  ? -55.418 49.725  83.558  1.00 18.38 ? 409  LEU   A CD2   1 
ATOM   2987  N  N     . LEU   A  1  412  ? -57.250 44.693  83.659  1.00 19.25 ? 410  LEU   A N     1 
ATOM   2988  C  CA    . LEU   A  1  412  ? -58.068 43.754  82.897  1.00 21.84 ? 410  LEU   A CA    1 
ATOM   2989  C  C     . LEU   A  1  412  ? -59.466 43.614  83.466  1.00 21.86 ? 410  LEU   A C     1 
ATOM   2990  O  O     . LEU   A  1  412  ? -60.360 43.138  82.762  1.00 24.13 ? 410  LEU   A O     1 
ATOM   2991  C  CB    . LEU   A  1  412  ? -57.377 42.396  82.792  1.00 22.52 ? 410  LEU   A CB    1 
ATOM   2992  C  CG    . LEU   A  1  412  ? -56.175 42.400  81.837  1.00 21.64 ? 410  LEU   A CG    1 
ATOM   2993  C  CD1   . LEU   A  1  412  ? -55.428 41.094  81.942  1.00 25.77 ? 410  LEU   A CD1   1 
ATOM   2994  C  CD2   . LEU   A  1  412  ? -56.680 42.619  80.423  1.00 22.98 ? 410  LEU   A CD2   1 
ATOM   2995  N  N     . ALA   A  1  413  ? -59.683 44.039  84.706  1.00 20.28 ? 411  ALA   A N     1 
ATOM   2996  C  CA    . ALA   A  1  413  ? -61.032 44.061  85.261  1.00 21.64 ? 411  ALA   A CA    1 
ATOM   2997  C  C     . ALA   A  1  413  ? -61.819 45.301  84.861  1.00 21.82 ? 411  ALA   A C     1 
ATOM   2998  O  O     . ALA   A  1  413  ? -63.009 45.396  85.179  1.00 23.86 ? 411  ALA   A O     1 
ATOM   2999  C  CB    . ALA   A  1  413  ? -60.960 43.974  86.789  1.00 21.38 ? 411  ALA   A CB    1 
ATOM   3000  N  N     . ALA   A  1  414  ? -61.200 46.242  84.156  1.00 20.61 ? 412  ALA   A N     1 
ATOM   3001  C  CA    . ALA   A  1  414  ? -61.802 47.537  83.886  1.00 21.20 ? 412  ALA   A CA    1 
ATOM   3002  C  C     . ALA   A  1  414  ? -61.730 47.884  82.403  1.00 19.84 ? 412  ALA   A C     1 
ATOM   3003  O  O     . ALA   A  1  414  ? -61.740 49.061  82.040  1.00 19.43 ? 412  ALA   A O     1 
ATOM   3004  C  CB    . ALA   A  1  414  ? -61.151 48.629  84.739  1.00 22.33 ? 412  ALA   A CB    1 
ATOM   3005  N  N     . THR   A  1  415  ? -61.675 46.867  81.533  1.00 20.61 ? 413  THR   A N     1 
ATOM   3006  C  CA    . THR   A  1  415  ? -61.577 47.121  80.095  1.00 21.41 ? 413  THR   A CA    1 
ATOM   3007  C  C     . THR   A  1  415  ? -62.800 47.828  79.534  1.00 22.62 ? 413  THR   A C     1 
ATOM   3008  O  O     . THR   A  1  415  ? -62.733 48.369  78.426  1.00 22.80 ? 413  THR   A O     1 
ATOM   3009  C  CB    . THR   A  1  415  ? -61.298 45.833  79.308  1.00 23.91 ? 413  THR   A CB    1 
ATOM   3010  O  OG1   . THR   A  1  415  ? -62.361 44.896  79.510  1.00 25.24 ? 413  THR   A OG1   1 
ATOM   3011  C  CG2   . THR   A  1  415  ? -60.009 45.201  79.768  1.00 23.18 ? 413  THR   A CG2   1 
ATOM   3012  N  N     . ASP   A  1  416  ? -63.920 47.839  80.260  1.00 21.96 ? 414  ASP   A N     1 
ATOM   3013  C  CA    . ASP   A  1  416  ? -65.053 48.624  79.791  1.00 22.46 ? 414  ASP   A CA    1 
ATOM   3014  C  C     . ASP   A  1  416  ? -64.785 50.117  79.889  1.00 22.25 ? 414  ASP   A C     1 
ATOM   3015  O  O     . ASP   A  1  416  ? -65.330 50.893  79.098  1.00 28.14 ? 414  ASP   A O     1 
ATOM   3016  C  CB    . ASP   A  1  416  ? -66.326 48.240  80.548  1.00 23.42 ? 414  ASP   A CB    1 
ATOM   3017  C  CG    . ASP   A  1  416  ? -66.228 48.510  82.030  1.00 31.81 ? 414  ASP   A CG    1 
ATOM   3018  O  OD1   . ASP   A  1  416  ? -65.164 48.226  82.621  1.00 28.17 ? 414  ASP   A OD1   1 
ATOM   3019  O  OD2   . ASP   A  1  416  ? -67.225 49.011  82.606  1.00 36.50 ? 414  ASP   A OD2   1 
ATOM   3020  N  N     . VAL   A  1  417  ? -63.929 50.547  80.814  1.00 20.64 ? 415  VAL   A N     1 
ATOM   3021  C  CA    . VAL   A  1  417  ? -63.727 51.973  81.027  1.00 22.66 ? 415  VAL   A CA    1 
ATOM   3022  C  C     . VAL   A  1  417  ? -62.314 52.454  80.735  1.00 20.16 ? 415  VAL   A C     1 
ATOM   3023  O  O     . VAL   A  1  417  ? -62.124 53.670  80.590  1.00 21.39 ? 415  VAL   A O     1 
ATOM   3024  C  CB    . VAL   A  1  417  ? -64.179 52.433  82.424  1.00 25.63 ? 415  VAL   A CB    1 
ATOM   3025  C  CG1   . VAL   A  1  417  ? -65.659 52.152  82.604  1.00 26.22 ? 415  VAL   A CG1   1 
ATOM   3026  C  CG2   . VAL   A  1  417  ? -63.376 51.748  83.484  1.00 23.84 ? 415  VAL   A CG2   1 
ATOM   3027  N  N     . VAL   A  1  418  ? -61.310 51.576  80.665  1.00 18.70 ? 416  VAL   A N     1 
ATOM   3028  C  CA    . VAL   A  1  418  ? -59.982 51.953  80.200  1.00 18.03 ? 416  VAL   A CA    1 
ATOM   3029  C  C     . VAL   A  1  418  ? -59.539 50.963  79.137  1.00 16.75 ? 416  VAL   A C     1 
ATOM   3030  O  O     . VAL   A  1  418  ? -60.050 49.847  79.034  1.00 17.98 ? 416  VAL   A O     1 
ATOM   3031  C  CB    . VAL   A  1  418  ? -58.930 52.028  81.324  1.00 18.09 ? 416  VAL   A CB    1 
ATOM   3032  C  CG1   . VAL   A  1  418  ? -59.276 53.144  82.302  1.00 20.88 ? 416  VAL   A CG1   1 
ATOM   3033  C  CG2   . VAL   A  1  418  ? -58.830 50.702  82.038  1.00 18.96 ? 416  VAL   A CG2   1 
ATOM   3034  N  N     . PHE   A  1  419  ? -58.534 51.374  78.374  1.00 16.36 ? 417  PHE   A N     1 
ATOM   3035  C  CA    . PHE   A  1  419  ? -57.932 50.523  77.357  1.00 17.48 ? 417  PHE   A CA    1 
ATOM   3036  C  C     . PHE   A  1  419  ? -56.529 50.173  77.831  1.00 16.02 ? 417  PHE   A C     1 
ATOM   3037  O  O     . PHE   A  1  419  ? -55.610 51.004  77.722  1.00 17.38 ? 417  PHE   A O     1 
ATOM   3038  C  CB    . PHE   A  1  419  ? -57.882 51.279  76.026  1.00 17.51 ? 417  PHE   A CB    1 
ATOM   3039  C  CG    . PHE   A  1  419  ? -57.182 50.532  74.934  1.00 17.90 ? 417  PHE   A CG    1 
ATOM   3040  C  CD1   . PHE   A  1  419  ? -57.630 49.282  74.527  1.00 17.90 ? 417  PHE   A CD1   1 
ATOM   3041  C  CD2   . PHE   A  1  419  ? -56.066 51.067  74.320  1.00 16.83 ? 417  PHE   A CD2   1 
ATOM   3042  C  CE1   . PHE   A  1  419  ? -56.988 48.599  73.505  1.00 16.58 ? 417  PHE   A CE1   1 
ATOM   3043  C  CE2   . PHE   A  1  419  ? -55.423 50.387  73.306  1.00 17.52 ? 417  PHE   A CE2   1 
ATOM   3044  C  CZ    . PHE   A  1  419  ? -55.874 49.154  72.902  1.00 18.29 ? 417  PHE   A CZ    1 
ATOM   3045  N  N     . PRO   A  1  420  ? -56.309 48.986  78.390  1.00 16.28 ? 418  PRO   A N     1 
ATOM   3046  C  CA    . PRO   A  1  420  ? -54.968 48.650  78.879  1.00 16.26 ? 418  PRO   A CA    1 
ATOM   3047  C  C     . PRO   A  1  420  ? -54.010 48.376  77.739  1.00 16.32 ? 418  PRO   A C     1 
ATOM   3048  O  O     . PRO   A  1  420  ? -54.362 47.751  76.736  1.00 17.56 ? 418  PRO   A O     1 
ATOM   3049  C  CB    . PRO   A  1  420  ? -55.198 47.377  79.699  1.00 15.41 ? 418  PRO   A CB    1 
ATOM   3050  C  CG    . PRO   A  1  420  ? -56.688 47.379  80.005  1.00 16.68 ? 418  PRO   A CG    1 
ATOM   3051  C  CD    . PRO   A  1  420  ? -57.283 47.940  78.750  1.00 17.65 ? 418  PRO   A CD    1 
ATOM   3052  N  N     . GLN   A  1  421  ? -52.773 48.824  77.931  1.00 16.41 ? 419  GLN   A N     1 
ATOM   3053  C  CA    . GLN   A  1  421  ? -51.719 48.686  76.938  1.00 15.94 ? 419  GLN   A CA    1 
ATOM   3054  C  C     . GLN   A  1  421  ? -50.509 48.154  77.686  1.00 16.24 ? 419  GLN   A C     1 
ATOM   3055  O  O     . GLN   A  1  421  ? -49.915 48.872  78.498  1.00 18.62 ? 419  GLN   A O     1 
ATOM   3056  C  CB    . GLN   A  1  421  ? -51.419 50.039  76.311  1.00 15.41 ? 419  GLN   A CB    1 
ATOM   3057  C  CG    . GLN   A  1  421  ? -52.638 50.637  75.612  1.00 16.16 ? 419  GLN   A CG    1 
ATOM   3058  C  CD    . GLN   A  1  421  ? -52.443 52.092  75.305  1.00 16.26 ? 419  GLN   A CD    1 
ATOM   3059  O  OE1   . GLN   A  1  421  ? -52.246 52.906  76.206  1.00 17.97 ? 419  GLN   A OE1   1 
ATOM   3060  N  NE2   . GLN   A  1  421  ? -52.529 52.442  74.029  1.00 17.17 ? 419  GLN   A NE2   1 
ATOM   3061  N  N     . PHE   A  1  422  ? -50.171 46.895  77.453  1.00 16.21 ? 420  PHE   A N     1 
ATOM   3062  C  CA    . PHE   A  1  422  ? -49.149 46.233  78.257  1.00 14.26 ? 420  PHE   A CA    1 
ATOM   3063  C  C     . PHE   A  1  422  ? -47.807 46.313  77.551  1.00 15.26 ? 420  PHE   A C     1 
ATOM   3064  O  O     . PHE   A  1  422  ? -47.504 45.504  76.670  1.00 17.48 ? 420  PHE   A O     1 
ATOM   3065  C  CB    . PHE   A  1  422  ? -49.553 44.810  78.590  1.00 17.34 ? 420  PHE   A CB    1 
ATOM   3066  C  CG    . PHE   A  1  422  ? -50.849 44.747  79.330  1.00 17.63 ? 420  PHE   A CG    1 
ATOM   3067  C  CD1   . PHE   A  1  422  ? -50.934 45.278  80.602  1.00 19.11 ? 420  PHE   A CD1   1 
ATOM   3068  C  CD2   . PHE   A  1  422  ? -51.983 44.225  78.738  1.00 18.98 ? 420  PHE   A CD2   1 
ATOM   3069  C  CE1   . PHE   A  1  422  ? -52.119 45.241  81.297  1.00 21.00 ? 420  PHE   A CE1   1 
ATOM   3070  C  CE2   . PHE   A  1  422  ? -53.181 44.185  79.419  1.00 19.96 ? 420  PHE   A CE2   1 
ATOM   3071  C  CZ    . PHE   A  1  422  ? -53.248 44.699  80.705  1.00 19.48 ? 420  PHE   A CZ    1 
ATOM   3072  N  N     . ALA   A  1  423  ? -47.015 47.290  77.956  1.00 15.66 ? 421  ALA   A N     1 
ATOM   3073  C  CA    . ALA   A  1  423  ? -45.708 47.529  77.358  1.00 14.80 ? 421  ALA   A CA    1 
ATOM   3074  C  C     . ALA   A  1  423  ? -44.685 46.681  78.095  1.00 18.20 ? 421  ALA   A C     1 
ATOM   3075  O  O     . ALA   A  1  423  ? -44.415 46.908  79.277  1.00 20.55 ? 421  ALA   A O     1 
ATOM   3076  C  CB    . ALA   A  1  423  ? -45.368 49.009  77.472  1.00 16.18 ? 421  ALA   A CB    1 
ATOM   3077  N  N     . THR   A  1  424  ? -44.130 45.694  77.401  1.00 16.89 ? 422  THR   A N     1 
ATOM   3078  C  CA    . THR   A  1  424  ? -43.091 44.878  78.006  1.00 17.65 ? 422  THR   A CA    1 
ATOM   3079  C  C     . THR   A  1  424  ? -42.396 44.073  76.920  1.00 18.24 ? 422  THR   A C     1 
ATOM   3080  O  O     . THR   A  1  424  ? -43.017 43.675  75.930  1.00 19.82 ? 422  THR   A O     1 
ATOM   3081  C  CB    . THR   A  1  424  ? -43.664 43.924  79.064  1.00 20.25 ? 422  THR   A CB    1 
ATOM   3082  O  OG1   . THR   A  1  424  ? -42.582 43.192  79.664  1.00 20.14 ? 422  THR   A OG1   1 
ATOM   3083  C  CG2   . THR   A  1  424  ? -44.644 42.955  78.430  1.00 20.91 ? 422  THR   A CG2   1 
ATOM   3084  N  N     . HIS   A  1  425  ? -41.104 43.840  77.122  1.00 18.74 ? 423  HIS   A N     1 
ATOM   3085  C  CA    . HIS   A  1  425  ? -40.354 42.918  76.289  1.00 19.71 ? 423  HIS   A CA    1 
ATOM   3086  C  C     . HIS   A  1  425  ? -40.133 41.583  76.964  1.00 21.42 ? 423  HIS   A C     1 
ATOM   3087  O  O     . HIS   A  1  425  ? -39.453 40.722  76.401  1.00 23.46 ? 423  HIS   A O     1 
ATOM   3088  C  CB    . HIS   A  1  425  ? -39.017 43.534  75.904  1.00 18.55 ? 423  HIS   A CB    1 
ATOM   3089  C  CG    . HIS   A  1  425  ? -39.163 44.802  75.139  1.00 20.26 ? 423  HIS   A CG    1 
ATOM   3090  N  ND1   . HIS   A  1  425  ? -38.441 45.935  75.435  1.00 21.67 ? 423  HIS   A ND1   1 
ATOM   3091  C  CD2   . HIS   A  1  425  ? -39.984 45.129  74.115  1.00 19.69 ? 423  HIS   A CD2   1 
ATOM   3092  C  CE1   . HIS   A  1  425  ? -38.797 46.903  74.608  1.00 22.59 ? 423  HIS   A CE1   1 
ATOM   3093  N  NE2   . HIS   A  1  425  ? -39.735 46.441  73.802  1.00 20.45 ? 423  HIS   A NE2   1 
ATOM   3094  N  N     . ASN   A  1  426  ? -40.707 41.387  78.141  1.00 20.86 ? 424  ASN   A N     1 
ATOM   3095  C  CA    . ASN   A  1  426  ? -40.443 40.210  78.960  1.00 21.43 ? 424  ASN   A CA    1 
ATOM   3096  C  C     . ASN   A  1  426  ? -41.480 39.147  78.608  1.00 22.59 ? 424  ASN   A C     1 
ATOM   3097  O  O     . ASN   A  1  426  ? -42.678 39.320  78.867  1.00 21.94 ? 424  ASN   A O     1 
ATOM   3098  C  CB    . ASN   A  1  426  ? -40.502 40.622  80.428  1.00 22.46 ? 424  ASN   A CB    1 
ATOM   3099  C  CG    . ASN   A  1  426  ? -40.167 39.496  81.377  1.00 22.05 ? 424  ASN   A CG    1 
ATOM   3100  O  OD1   . ASN   A  1  426  ? -40.577 38.358  81.178  1.00 25.45 ? 424  ASN   A OD1   1 
ATOM   3101  N  ND2   . ASN   A  1  426  ? -39.428 39.821  82.442  1.00 21.94 ? 424  ASN   A ND2   1 
ATOM   3102  N  N     . ALA   A  1  427  ? -41.016 38.042  78.016  1.00 22.39 ? 425  ALA   A N     1 
ATOM   3103  C  CA    . ALA   A  1  427  ? -41.925 36.999  77.554  1.00 23.46 ? 425  ALA   A CA    1 
ATOM   3104  C  C     . ALA   A  1  427  ? -42.702 36.371  78.702  1.00 20.88 ? 425  ALA   A C     1 
ATOM   3105  O  O     . ALA   A  1  427  ? -43.835 35.916  78.505  1.00 23.09 ? 425  ALA   A O     1 
ATOM   3106  C  CB    . ALA   A  1  427  ? -41.130 35.919  76.817  1.00 25.11 ? 425  ALA   A CB    1 
ATOM   3107  N  N     . GLN   A  1  428  ? -42.107 36.318  79.895  1.00 22.60 ? 426  GLN   A N     1 
ATOM   3108  C  CA    . GLN   A  1  428  ? -42.827 35.786  81.047  1.00 26.50 ? 426  GLN   A CA    1 
ATOM   3109  C  C     . GLN   A  1  428  ? -43.965 36.716  81.428  1.00 22.11 ? 426  GLN   A C     1 
ATOM   3110  O  O     . GLN   A  1  428  ? -45.097 36.271  81.656  1.00 22.96 ? 426  GLN   A O     1 
ATOM   3111  C  CB    . GLN   A  1  428  ? -41.872 35.607  82.228  1.00 23.60 ? 426  GLN   A CB    1 
ATOM   3112  C  CG    . GLN   A  1  428  ? -42.409 34.691  83.328  1.00 24.91 ? 426  GLN   A CG    1 
ATOM   3113  C  CD    . GLN   A  1  428  ? -43.487 35.333  84.193  1.00 30.07 ? 426  GLN   A CD    1 
ATOM   3114  O  OE1   . GLN   A  1  428  ? -43.460 36.539  84.458  1.00 29.00 ? 426  GLN   A OE1   1 
ATOM   3115  N  NE2   . GLN   A  1  428  ? -44.440 34.523  84.644  1.00 26.71 ? 426  GLN   A NE2   1 
ATOM   3116  N  N     . THR   A  1  429  ? -43.674 38.016  81.500  1.00 22.17 ? 427  THR   A N     1 
ATOM   3117  C  CA    . THR   A  1  429  ? -44.710 38.999  81.796  1.00 21.78 ? 427  THR   A CA    1 
ATOM   3118  C  C     . THR   A  1  429  ? -45.819 38.935  80.759  1.00 20.67 ? 427  THR   A C     1 
ATOM   3119  O  O     . THR   A  1  429  ? -47.008 38.902  81.100  1.00 21.58 ? 427  THR   A O     1 
ATOM   3120  C  CB    . THR   A  1  429  ? -44.097 40.397  81.809  1.00 23.17 ? 427  THR   A CB    1 
ATOM   3121  O  OG1   . THR   A  1  429  ? -42.945 40.420  82.661  1.00 22.43 ? 427  THR   A OG1   1 
ATOM   3122  C  CG2   . THR   A  1  429  ? -45.107 41.393  82.336  1.00 23.46 ? 427  THR   A CG2   1 
ATOM   3123  N  N     . LEU   A  1  430  ? -45.439 38.913  79.482  1.00 21.17 ? 428  LEU   A N     1 
ATOM   3124  C  CA    . LEU   A  1  430  ? -46.408 38.845  78.396  1.00 22.75 ? 428  LEU   A CA    1 
ATOM   3125  C  C     . LEU   A  1  430  ? -47.302 37.624  78.543  1.00 22.24 ? 428  LEU   A C     1 
ATOM   3126  O  O     . LEU   A  1  430  ? -48.535 37.726  78.472  1.00 22.64 ? 428  LEU   A O     1 
ATOM   3127  C  CB    . LEU   A  1  430  ? -45.647 38.797  77.067  1.00 20.34 ? 428  LEU   A CB    1 
ATOM   3128  C  CG    . LEU   A  1  430  ? -46.328 39.014  75.712  1.00 24.81 ? 428  LEU   A CG    1 
ATOM   3129  C  CD1   . LEU   A  1  430  ? -45.221 39.183  74.688  1.00 28.32 ? 428  LEU   A CD1   1 
ATOM   3130  C  CD2   . LEU   A  1  430  ? -47.229 37.859  75.312  1.00 26.08 ? 428  LEU   A CD2   1 
ATOM   3131  N  N     . ALA   A  1  431  ? -46.691 36.453  78.737  1.00 23.61 ? 429  ALA   A N     1 
ATOM   3132  C  CA    . ALA   A  1  431  ? -47.455 35.213  78.808  1.00 24.52 ? 429  ALA   A CA    1 
ATOM   3133  C  C     . ALA   A  1  431  ? -48.439 35.237  79.967  1.00 24.07 ? 429  ALA   A C     1 
ATOM   3134  O  O     . ALA   A  1  431  ? -49.596 34.822  79.818  1.00 23.57 ? 429  ALA   A O     1 
ATOM   3135  C  CB    . ALA   A  1  431  ? -46.504 34.030  78.961  1.00 23.43 ? 429  ALA   A CB    1 
ATOM   3136  N  N     . ALA   A  1  432  ? -47.993 35.727  81.129  1.00 23.82 ? 430  ALA   A N     1 
ATOM   3137  C  CA    . ALA   A  1  432  ? -48.869 35.810  82.293  1.00 26.06 ? 430  ALA   A CA    1 
ATOM   3138  C  C     . ALA   A  1  432  ? -50.103 36.647  81.995  1.00 23.22 ? 430  ALA   A C     1 
ATOM   3139  O  O     . ALA   A  1  432  ? -51.221 36.283  82.381  1.00 25.41 ? 430  ALA   A O     1 
ATOM   3140  C  CB    . ALA   A  1  432  ? -48.103 36.400  83.476  1.00 24.78 ? 430  ALA   A CB    1 
ATOM   3141  N  N     . ILE   A  1  433  ? -49.925 37.759  81.286  1.00 22.69 ? 431  ILE   A N     1 
ATOM   3142  C  CA    . ILE   A  1  433  ? -51.043 38.649  81.009  1.00 22.89 ? 431  ILE   A CA    1 
ATOM   3143  C  C     . ILE   A  1  433  ? -51.908 38.096  79.896  1.00 21.82 ? 431  ILE   A C     1 
ATOM   3144  O  O     . ILE   A  1  433  ? -53.138 38.184  79.949  1.00 21.65 ? 431  ILE   A O     1 
ATOM   3145  C  CB    . ILE   A  1  433  ? -50.503 40.050  80.692  1.00 24.46 ? 431  ILE   A CB    1 
ATOM   3146  C  CG1   . ILE   A  1  433  ? -49.882 40.630  81.958  1.00 23.86 ? 431  ILE   A CG1   1 
ATOM   3147  C  CG2   . ILE   A  1  433  ? -51.589 40.944  80.122  1.00 23.70 ? 431  ILE   A CG2   1 
ATOM   3148  C  CD1   . ILE   A  1  433  ? -49.200 41.907  81.732  1.00 25.63 ? 431  ILE   A CD1   1 
ATOM   3149  N  N     . TYR   A  1  434  ? -51.283 37.500  78.881  1.00 23.53 ? 432  TYR   A N     1 
ATOM   3150  C  CA    . TYR   A  1  434  ? -52.040 36.867  77.808  1.00 24.42 ? 432  TYR   A CA    1 
ATOM   3151  C  C     . TYR   A  1  434  ? -53.027 35.845  78.361  1.00 25.90 ? 432  TYR   A C     1 
ATOM   3152  O  O     . TYR   A  1  434  ? -54.202 35.814  77.969  1.00 25.52 ? 432  TYR   A O     1 
ATOM   3153  C  CB    . TYR   A  1  434  ? -51.057 36.216  76.835  1.00 24.01 ? 432  TYR   A CB    1 
ATOM   3154  C  CG    . TYR   A  1  434  ? -51.691 35.298  75.828  1.00 26.62 ? 432  TYR   A CG    1 
ATOM   3155  C  CD1   . TYR   A  1  434  ? -52.482 35.797  74.802  1.00 27.55 ? 432  TYR   A CD1   1 
ATOM   3156  C  CD2   . TYR   A  1  434  ? -51.492 33.925  75.898  1.00 29.19 ? 432  TYR   A CD2   1 
ATOM   3157  C  CE1   . TYR   A  1  434  ? -53.056 34.954  73.875  1.00 27.52 ? 432  TYR   A CE1   1 
ATOM   3158  C  CE2   . TYR   A  1  434  ? -52.058 33.076  74.977  1.00 31.25 ? 432  TYR   A CE2   1 
ATOM   3159  C  CZ    . TYR   A  1  434  ? -52.842 33.589  73.970  1.00 32.07 ? 432  TYR   A CZ    1 
ATOM   3160  O  OH    . TYR   A  1  434  ? -53.400 32.730  73.055  1.00 35.40 ? 432  TYR   A OH    1 
ATOM   3161  N  N     . HIS   A  1  435  ? -52.572 35.007  79.289  1.00 26.52 ? 433  HIS   A N     1 
ATOM   3162  C  CA    . HIS   A  1  435  ? -53.476 34.016  79.861  1.00 27.19 ? 433  HIS   A CA    1 
ATOM   3163  C  C     . HIS   A  1  435  ? -54.410 34.630  80.892  1.00 26.55 ? 433  HIS   A C     1 
ATOM   3164  O  O     . HIS   A  1  435  ? -55.560 34.194  81.018  1.00 26.32 ? 433  HIS   A O     1 
ATOM   3165  C  CB    . HIS   A  1  435  ? -52.691 32.837  80.429  1.00 29.79 ? 433  HIS   A CB    1 
ATOM   3166  C  CG    . HIS   A  1  435  ? -52.075 31.978  79.370  1.00 30.60 ? 433  HIS   A CG    1 
ATOM   3167  N  ND1   . HIS   A  1  435  ? -52.784 31.004  78.701  1.00 31.94 ? 433  HIS   A ND1   1 
ATOM   3168  C  CD2   . HIS   A  1  435  ? -50.835 31.983  78.827  1.00 29.22 ? 433  HIS   A CD2   1 
ATOM   3169  C  CE1   . HIS   A  1  435  ? -51.996 30.424  77.812  1.00 31.12 ? 433  HIS   A CE1   1 
ATOM   3170  N  NE2   . HIS   A  1  435  ? -50.809 31.000  77.867  1.00 28.58 ? 433  HIS   A NE2   1 
ATOM   3171  N  N     . MET   A  1  436  ? -53.954 35.661  81.605  1.00 25.08 ? 434  MET   A N     1 
ATOM   3172  C  CA    . MET   A  1  436  ? -54.845 36.364  82.522  1.00 25.66 ? 434  MET   A CA    1 
ATOM   3173  C  C     . MET   A  1  436  ? -56.022 36.988  81.782  1.00 25.33 ? 434  MET   A C     1 
ATOM   3174  O  O     . MET   A  1  436  ? -57.149 37.000  82.289  1.00 26.45 ? 434  MET   A O     1 
ATOM   3175  C  CB    . MET   A  1  436  ? -54.067 37.445  83.263  1.00 23.63 ? 434  MET   A CB    1 
ATOM   3176  C  CG    . MET   A  1  436  ? -54.897 38.170  84.292  1.00 25.34 ? 434  MET   A CG    1 
ATOM   3177  S  SD    . MET   A  1  436  ? -53.997 39.571  84.939  1.00 25.25 ? 434  MET   A SD    1 
ATOM   3178  C  CE    . MET   A  1  436  ? -52.764 38.762  85.948  1.00 28.14 ? 434  MET   A CE    1 
ATOM   3179  N  N     . ALA   A  1  437  ? -55.775 37.530  80.587  1.00 24.86 ? 435  ALA   A N     1 
ATOM   3180  C  CA    . ALA   A  1  437  ? -56.831 38.214  79.856  1.00 27.25 ? 435  ALA   A CA    1 
ATOM   3181  C  C     . ALA   A  1  437  ? -57.850 37.232  79.297  1.00 29.80 ? 435  ALA   A C     1 
ATOM   3182  O  O     . ALA   A  1  437  ? -59.015 37.594  79.101  1.00 30.60 ? 435  ALA   A O     1 
ATOM   3183  C  CB    . ALA   A  1  437  ? -56.226 39.052  78.734  1.00 26.98 ? 435  ALA   A CB    1 
ATOM   3184  N  N     . GLY   A  1  438  ? -57.436 35.994  79.030  1.00 32.19 ? 436  GLY   A N     1 
ATOM   3185  C  CA    . GLY   A  1  438  ? -58.359 34.968  78.592  1.00 34.99 ? 436  GLY   A CA    1 
ATOM   3186  C  C     . GLY   A  1  438  ? -58.555 34.929  77.094  1.00 36.00 ? 436  GLY   A C     1 
ATOM   3187  O  O     . GLY   A  1  438  ? -57.942 35.668  76.317  1.00 34.96 ? 436  GLY   A O     1 
ATOM   3188  N  N     . LYS   A  1  439  ? -59.471 34.045  76.688  1.00 40.20 ? 437  LYS   A N     1 
ATOM   3189  C  CA    . LYS   A  1  439  ? -59.641 33.720  75.277  1.00 44.29 ? 437  LYS   A CA    1 
ATOM   3190  C  C     . LYS   A  1  439  ? -60.553 34.700  74.556  1.00 38.94 ? 437  LYS   A C     1 
ATOM   3191  O  O     . LYS   A  1  439  ? -60.433 34.863  73.338  1.00 45.99 ? 437  LYS   A O     1 
ATOM   3192  C  CB    . LYS   A  1  439  ? -60.171 32.291  75.123  1.00 48.29 ? 437  LYS   A CB    1 
ATOM   3193  N  N     . ASP   A  1  440  ? -61.468 35.349  75.269  1.00 37.76 ? 438  ASP   A N     1 
ATOM   3194  C  CA    . ASP   A  1  440  ? -62.312 36.362  74.650  1.00 42.27 ? 438  ASP   A CA    1 
ATOM   3195  C  C     . ASP   A  1  440  ? -61.465 37.580  74.323  1.00 39.76 ? 438  ASP   A C     1 
ATOM   3196  O  O     . ASP   A  1  440  ? -60.935 38.237  75.226  1.00 40.53 ? 438  ASP   A O     1 
ATOM   3197  C  CB    . ASP   A  1  440  ? -63.445 36.752  75.593  1.00 44.31 ? 438  ASP   A CB    1 
ATOM   3198  C  CG    . ASP   A  1  440  ? -64.546 35.717  75.636  1.00 49.12 ? 438  ASP   A CG    1 
ATOM   3199  O  OD1   . ASP   A  1  440  ? -64.409 34.676  74.956  1.00 46.96 ? 438  ASP   A OD1   1 
ATOM   3200  O  OD2   . ASP   A  1  440  ? -65.549 35.945  76.345  1.00 53.24 ? 438  ASP   A OD2   1 
ATOM   3201  N  N     . PHE   A  1  441  ? -61.322 37.878  73.035  1.00 30.79 ? 439  PHE   A N     1 
ATOM   3202  C  CA    . PHE   A  1  441  ? -60.577 39.059  72.641  1.00 30.53 ? 439  PHE   A CA    1 
ATOM   3203  C  C     . PHE   A  1  441  ? -61.234 39.733  71.452  1.00 29.67 ? 439  PHE   A C     1 
ATOM   3204  O  O     . PHE   A  1  441  ? -61.776 39.074  70.563  1.00 32.16 ? 439  PHE   A O     1 
ATOM   3205  C  CB    . PHE   A  1  441  ? -59.109 38.760  72.306  1.00 25.86 ? 439  PHE   A CB    1 
ATOM   3206  C  CG    . PHE   A  1  441  ? -58.320 39.998  71.999  1.00 26.08 ? 439  PHE   A CG    1 
ATOM   3207  C  CD1   . PHE   A  1  441  ? -57.817 40.782  73.026  1.00 24.13 ? 439  PHE   A CD1   1 
ATOM   3208  C  CD2   . PHE   A  1  441  ? -58.131 40.414  70.689  1.00 26.80 ? 439  PHE   A CD2   1 
ATOM   3209  C  CE1   . PHE   A  1  441  ? -57.123 41.941  72.757  1.00 23.38 ? 439  PHE   A CE1   1 
ATOM   3210  C  CE2   . PHE   A  1  441  ? -57.437 41.576  70.418  1.00 25.39 ? 439  PHE   A CE2   1 
ATOM   3211  C  CZ    . PHE   A  1  441  ? -56.934 42.338  71.459  1.00 23.15 ? 439  PHE   A CZ    1 
ATOM   3212  N  N     . HIS   A  1  442  ? -61.164 41.059  71.447  1.00 27.27 ? 440  HIS   A N     1 
ATOM   3213  C  CA    . HIS   A  1  442  ? -61.504 41.864  70.291  1.00 28.07 ? 440  HIS   A CA    1 
ATOM   3214  C  C     . HIS   A  1  442  ? -60.546 43.040  70.262  1.00 28.91 ? 440  HIS   A C     1 
ATOM   3215  O  O     . HIS   A  1  442  ? -60.055 43.480  71.307  1.00 23.83 ? 440  HIS   A O     1 
ATOM   3216  C  CB    . HIS   A  1  442  ? -62.952 42.364  70.368  1.00 26.74 ? 440  HIS   A CB    1 
ATOM   3217  C  CG    . HIS   A  1  442  ? -63.232 43.237  71.550  1.00 22.98 ? 440  HIS   A CG    1 
ATOM   3218  N  ND1   . HIS   A  1  442  ? -63.638 42.736  72.769  1.00 27.26 ? 440  HIS   A ND1   1 
ATOM   3219  C  CD2   . HIS   A  1  442  ? -63.176 44.582  71.695  1.00 26.14 ? 440  HIS   A CD2   1 
ATOM   3220  C  CE1   . HIS   A  1  442  ? -63.813 43.736  73.616  1.00 25.40 ? 440  HIS   A CE1   1 
ATOM   3221  N  NE2   . HIS   A  1  442  ? -63.541 44.866  72.988  1.00 26.28 ? 440  HIS   A NE2   1 
ATOM   3222  N  N     . VAL   A  1  443  ? -60.253 43.530  69.056  1.00 29.19 ? 441  VAL   A N     1 
ATOM   3223  C  CA    . VAL   A  1  443  ? -59.413 44.715  68.948  1.00 30.78 ? 441  VAL   A CA    1 
ATOM   3224  C  C     . VAL   A  1  443  ? -60.112 45.870  69.645  1.00 26.40 ? 441  VAL   A C     1 
ATOM   3225  O  O     . VAL   A  1  443  ? -61.306 46.118  69.433  1.00 26.41 ? 441  VAL   A O     1 
ATOM   3226  C  CB    . VAL   A  1  443  ? -59.074 45.022  67.482  1.00 32.51 ? 441  VAL   A CB    1 
ATOM   3227  C  CG1   . VAL   A  1  443  ? -58.529 46.432  67.352  1.00 32.93 ? 441  VAL   A CG1   1 
ATOM   3228  C  CG2   . VAL   A  1  443  ? -58.050 44.024  66.964  1.00 36.83 ? 441  VAL   A CG2   1 
ATOM   3229  N  N     . GLY   A  1  444  ? -59.370 46.568  70.500  1.00 24.97 ? 442  GLY   A N     1 
ATOM   3230  C  CA    . GLY   A  1  444  ? -59.924 47.562  71.386  1.00 21.13 ? 442  GLY   A CA    1 
ATOM   3231  C  C     . GLY   A  1  444  ? -60.082 47.106  72.819  1.00 18.57 ? 442  GLY   A C     1 
ATOM   3232  O  O     . GLY   A  1  444  ? -60.282 47.948  73.694  1.00 19.53 ? 442  GLY   A O     1 
ATOM   3233  N  N     . LYS   A  1  445  ? -60.001 45.806  73.092  1.00 19.47 ? 443  LYS   A N     1 
ATOM   3234  C  CA    . LYS   A  1  445  ? -60.114 45.368  74.475  1.00 18.96 ? 443  LYS   A CA    1 
ATOM   3235  C  C     . LYS   A  1  445  ? -58.862 45.732  75.252  1.00 21.19 ? 443  LYS   A C     1 
ATOM   3236  O  O     . LYS   A  1  445  ? -58.934 46.369  76.309  1.00 20.11 ? 443  LYS   A O     1 
ATOM   3237  C  CB    . LYS   A  1  445  ? -60.378 43.871  74.554  1.00 21.22 ? 443  LYS   A CB    1 
ATOM   3238  C  CG    . LYS   A  1  445  ? -60.700 43.434  75.971  1.00 25.74 ? 443  LYS   A CG    1 
ATOM   3239  C  CD    . LYS   A  1  445  ? -61.033 41.962  76.062  1.00 31.87 ? 443  LYS   A CD    1 
ATOM   3240  C  CE    . LYS   A  1  445  ? -61.932 41.709  77.266  1.00 36.62 ? 443  LYS   A CE    1 
ATOM   3241  N  NZ    . LYS   A  1  445  ? -62.299 40.271  77.379  1.00 39.33 ? 443  LYS   A NZ    1 
ATOM   3242  N  N     . TYR   A  1  446  ? -57.703 45.340  74.735  1.00 20.16 ? 444  TYR   A N     1 
ATOM   3243  C  CA    . TYR   A  1  446  ? -56.412 45.719  75.287  1.00 19.65 ? 444  TYR   A CA    1 
ATOM   3244  C  C     . TYR   A  1  446  ? -55.404 45.484  74.178  1.00 19.37 ? 444  TYR   A C     1 
ATOM   3245  O  O     . TYR   A  1  446  ? -55.734 44.927  73.132  1.00 18.92 ? 444  TYR   A O     1 
ATOM   3246  C  CB    . TYR   A  1  446  ? -56.088 44.911  76.549  1.00 19.15 ? 444  TYR   A CB    1 
ATOM   3247  C  CG    . TYR   A  1  446  ? -55.653 43.479  76.304  1.00 22.31 ? 444  TYR   A CG    1 
ATOM   3248  C  CD1   . TYR   A  1  446  ? -54.312 43.182  76.122  1.00 25.72 ? 444  TYR   A CD1   1 
ATOM   3249  C  CD2   . TYR   A  1  446  ? -56.574 42.428  76.267  1.00 28.65 ? 444  TYR   A CD2   1 
ATOM   3250  C  CE1   . TYR   A  1  446  ? -53.882 41.897  75.907  1.00 29.84 ? 444  TYR   A CE1   1 
ATOM   3251  C  CE2   . TYR   A  1  446  ? -56.139 41.116  76.046  1.00 25.06 ? 444  TYR   A CE2   1 
ATOM   3252  C  CZ    . TYR   A  1  446  ? -54.788 40.875  75.865  1.00 27.95 ? 444  TYR   A CZ    1 
ATOM   3253  O  OH    . TYR   A  1  446  ? -54.306 39.600  75.648  1.00 32.99 ? 444  TYR   A OH    1 
ATOM   3254  N  N     . GLU   A  1  447  ? -54.166 45.905  74.410  1.00 17.10 ? 445  GLU   A N     1 
ATOM   3255  C  CA    . GLU   A  1  447  ? -53.109 45.585  73.464  1.00 18.05 ? 445  GLU   A CA    1 
ATOM   3256  C  C     . GLU   A  1  447  ? -51.815 45.423  74.237  1.00 18.46 ? 445  GLU   A C     1 
ATOM   3257  O  O     . GLU   A  1  447  ? -51.715 45.797  75.406  1.00 18.45 ? 445  GLU   A O     1 
ATOM   3258  C  CB    . GLU   A  1  447  ? -52.936 46.678  72.407  1.00 17.94 ? 445  GLU   A CB    1 
ATOM   3259  C  CG    . GLU   A  1  447  ? -52.457 47.992  72.987  1.00 17.13 ? 445  GLU   A CG    1 
ATOM   3260  C  CD    . GLU   A  1  447  ? -52.388 49.120  71.978  1.00 17.90 ? 445  GLU   A CD    1 
ATOM   3261  O  OE1   . GLU   A  1  447  ? -52.921 48.969  70.856  1.00 20.06 ? 445  GLU   A OE1   1 
ATOM   3262  O  OE2   . GLU   A  1  447  ? -51.818 50.177  72.321  1.00 18.19 ? 445  GLU   A OE2   1 
ATOM   3263  N  N     . PHE   A  1  448  ? -50.818 44.860  73.567  1.00 17.62 ? 446  PHE   A N     1 
ATOM   3264  C  CA    . PHE   A  1  448  ? -49.453 44.907  74.058  1.00 17.69 ? 446  PHE   A CA    1 
ATOM   3265  C  C     . PHE   A  1  448  ? -48.729 46.073  73.403  1.00 16.68 ? 446  PHE   A C     1 
ATOM   3266  O  O     . PHE   A  1  448  ? -49.195 46.655  72.420  1.00 18.65 ? 446  PHE   A O     1 
ATOM   3267  C  CB    . PHE   A  1  448  ? -48.731 43.597  73.745  1.00 19.37 ? 446  PHE   A CB    1 
ATOM   3268  C  CG    . PHE   A  1  448  ? -49.268 42.433  74.492  1.00 20.18 ? 446  PHE   A CG    1 
ATOM   3269  C  CD1   . PHE   A  1  448  ? -48.937 42.246  75.821  1.00 19.90 ? 446  PHE   A CD1   1 
ATOM   3270  C  CD2   . PHE   A  1  448  ? -50.124 41.533  73.875  1.00 20.50 ? 446  PHE   A CD2   1 
ATOM   3271  C  CE1   . PHE   A  1  448  ? -49.446 41.166  76.532  1.00 23.29 ? 446  PHE   A CE1   1 
ATOM   3272  C  CE2   . PHE   A  1  448  ? -50.637 40.460  74.576  1.00 23.75 ? 446  PHE   A CE2   1 
ATOM   3273  C  CZ    . PHE   A  1  448  ? -50.301 40.277  75.905  1.00 23.47 ? 446  PHE   A CZ    1 
ATOM   3274  N  N     . GLN   A  1  449  ? -47.571 46.413  73.958  1.00 16.60 ? 447  GLN   A N     1 
ATOM   3275  C  CA    . GLN   A  1  449  ? -46.726 47.418  73.338  1.00 17.23 ? 447  GLN   A CA    1 
ATOM   3276  C  C     . GLN   A  1  449  ? -45.278 47.008  73.484  1.00 17.81 ? 447  GLN   A C     1 
ATOM   3277  O  O     . GLN   A  1  449  ? -44.904 46.284  74.409  1.00 17.67 ? 447  GLN   A O     1 
ATOM   3278  C  CB    . GLN   A  1  449  ? -46.889 48.813  73.930  1.00 16.49 ? 447  GLN   A CB    1 
ATOM   3279  C  CG    . GLN   A  1  449  ? -48.298 49.330  73.828  1.00 15.98 ? 447  GLN   A CG    1 
ATOM   3280  C  CD    . GLN   A  1  449  ? -48.386 50.821  74.039  1.00 18.02 ? 447  GLN   A CD    1 
ATOM   3281  O  OE1   . GLN   A  1  449  ? -47.439 51.451  74.523  1.00 19.94 ? 447  GLN   A OE1   1 
ATOM   3282  N  NE2   . GLN   A  1  449  ? -49.523 51.403  73.676  1.00 17.19 ? 447  GLN   A NE2   1 
ATOM   3283  N  N     . CYS   A  1  450  ? -44.472 47.485  72.551  1.00 16.80 ? 448  CYS   A N     1 
ATOM   3284  C  CA    . CYS   A  1  450  ? -43.050 47.201  72.572  1.00 16.21 ? 448  CYS   A CA    1 
ATOM   3285  C  C     . CYS   A  1  450  ? -42.304 48.370  71.956  1.00 17.11 ? 448  CYS   A C     1 
ATOM   3286  O  O     . CYS   A  1  450  ? -42.896 49.272  71.361  1.00 18.46 ? 448  CYS   A O     1 
ATOM   3287  C  CB    . CYS   A  1  450  ? -42.726 45.906  71.834  1.00 19.50 ? 448  CYS   A CB    1 
ATOM   3288  S  SG    . CYS   A  1  450  ? -42.827 46.020  70.035  1.00 21.18 ? 448  CYS   A SG    1 
ATOM   3289  N  N     . LEU   A  1  451  ? -40.985 48.346  72.108  1.00 17.28 ? 449  LEU   A N     1 
ATOM   3290  C  CA    . LEU   A  1  451  ? -40.139 49.387  71.549  1.00 20.13 ? 449  LEU   A CA    1 
ATOM   3291  C  C     . LEU   A  1  451  ? -39.656 48.983  70.164  1.00 19.36 ? 449  LEU   A C     1 
ATOM   3292  O  O     . LEU   A  1  451  ? -39.307 47.821  69.927  1.00 20.77 ? 449  LEU   A O     1 
ATOM   3293  C  CB    . LEU   A  1  451  ? -38.939 49.628  72.464  1.00 21.31 ? 449  LEU   A CB    1 
ATOM   3294  C  CG    . LEU   A  1  451  ? -37.917 50.677  72.025  1.00 22.15 ? 449  LEU   A CG    1 
ATOM   3295  C  CD1   . LEU   A  1  451  ? -38.525 52.080  71.927  1.00 22.43 ? 449  LEU   A CD1   1 
ATOM   3296  C  CD2   . LEU   A  1  451  ? -36.735 50.653  73.008  1.00 24.75 ? 449  LEU   A CD2   1 
ATOM   3297  N  N     . HIS   A  1  452  ? -39.657 49.949  69.247  1.00 18.26 ? 450  HIS   A N     1 
ATOM   3298  C  CA    . HIS   A  1  452  ? -39.098 49.734  67.916  1.00 21.51 ? 450  HIS   A CA    1 
ATOM   3299  C  C     . HIS   A  1  452  ? -37.662 49.230  67.994  1.00 22.72 ? 450  HIS   A C     1 
ATOM   3300  O  O     . HIS   A  1  452  ? -36.875 49.676  68.830  1.00 23.57 ? 450  HIS   A O     1 
ATOM   3301  C  CB    . HIS   A  1  452  ? -39.107 51.053  67.148  1.00 20.45 ? 450  HIS   A CB    1 
ATOM   3302  C  CG    . HIS   A  1  452  ? -38.347 50.993  65.863  1.00 20.20 ? 450  HIS   A CG    1 
ATOM   3303  N  ND1   . HIS   A  1  452  ? -38.913 50.561  64.684  1.00 20.64 ? 450  HIS   A ND1   1 
ATOM   3304  C  CD2   . HIS   A  1  452  ? -37.058 51.291  65.582  1.00 23.61 ? 450  HIS   A CD2   1 
ATOM   3305  C  CE1   . HIS   A  1  452  ? -38.003 50.602  63.726  1.00 21.41 ? 450  HIS   A CE1   1 
ATOM   3306  N  NE2   . HIS   A  1  452  ? -36.869 51.036  64.247  1.00 22.13 ? 450  HIS   A NE2   1 
ATOM   3307  N  N     . GLY   A  1  453  ? -37.328 48.298  67.107  1.00 24.64 ? 451  GLY   A N     1 
ATOM   3308  C  CA    . GLY   A  1  453  ? -35.954 47.821  67.040  1.00 27.53 ? 451  GLY   A CA    1 
ATOM   3309  C  C     . GLY   A  1  453  ? -35.500 47.109  68.291  1.00 32.03 ? 451  GLY   A C     1 
ATOM   3310  O  O     . GLY   A  1  453  ? -34.297 47.067  68.584  1.00 35.09 ? 451  GLY   A O     1 
ATOM   3311  N  N     . MET   A  1  454  ? -36.437 46.552  69.048  1.00 25.91 ? 452  MET   A N     1 
ATOM   3312  C  CA    . MET   A  1  454  ? -36.120 45.816  70.259  1.00 23.74 ? 452  MET   A CA    1 
ATOM   3313  C  C     . MET   A  1  454  ? -37.184 44.757  70.489  1.00 25.32 ? 452  MET   A C     1 
ATOM   3314  O  O     . MET   A  1  454  ? -36.872 43.586  70.732  1.00 26.47 ? 452  MET   A O     1 
ATOM   3315  C  CB    . MET   A  1  454  ? -36.051 46.758  71.458  1.00 24.93 ? 452  MET   A CB    1 
ATOM   3316  C  CG    . MET   A  1  454  ? -35.929 46.024  72.770  1.00 26.77 ? 452  MET   A CG    1 
ATOM   3317  S  SD    . MET   A  1  454  ? -34.452 44.994  72.771  1.00 32.39 ? 452  MET   A SD    1 
ATOM   3318  C  CE    . MET   A  1  454  ? -33.196 46.269  72.749  1.00 32.89 ? 452  MET   A CE    1 
ATOM   3319  N  N     . GLY   A  1  455  ? -38.450 45.151  70.394  1.00 21.23 ? 453  GLY   A N     1 
ATOM   3320  C  CA    . GLY   A  1  455  ? -39.510 44.222  70.722  1.00 22.69 ? 453  GLY   A CA    1 
ATOM   3321  C  C     . GLY   A  1  455  ? -40.082 43.419  69.580  1.00 23.81 ? 453  GLY   A C     1 
ATOM   3322  O  O     . GLY   A  1  455  ? -40.863 42.496  69.827  1.00 25.24 ? 453  GLY   A O     1 
ATOM   3323  N  N     . GLU   A  1  456  ? -39.730 43.741  68.335  1.00 25.58 ? 454  GLU   A N     1 
ATOM   3324  C  CA    . GLU   A  1  456  ? -40.322 43.033  67.202  1.00 28.08 ? 454  GLU   A CA    1 
ATOM   3325  C  C     . GLU   A  1  456  ? -40.063 41.532  67.197  1.00 28.82 ? 454  GLU   A C     1 
ATOM   3326  O  O     . GLU   A  1  456  ? -40.997 40.783  66.862  1.00 28.47 ? 454  GLU   A O     1 
ATOM   3327  C  CB    . GLU   A  1  456  ? -39.906 43.663  65.868  1.00 31.51 ? 454  GLU   A CB    1 
ATOM   3328  C  CG    . GLU   A  1  456  ? -40.432 45.058  65.642  1.00 35.07 ? 454  GLU   A CG    1 
ATOM   3329  C  CD    . GLU   A  1  456  ? -39.427 46.101  66.042  1.00 31.13 ? 454  GLU   A CD    1 
ATOM   3330  O  OE1   . GLU   A  1  456  ? -38.550 45.783  66.877  1.00 31.58 ? 454  GLU   A OE1   1 
ATOM   3331  O  OE2   . GLU   A  1  456  ? -39.498 47.234  65.517  1.00 32.83 ? 454  GLU   A OE2   1 
ATOM   3332  N  N     . PRO   A  1  457  ? -38.861 41.028  67.504  1.00 28.33 ? 455  PRO   A N     1 
ATOM   3333  C  CA    . PRO   A  1  457  ? -38.686 39.567  67.517  1.00 29.28 ? 455  PRO   A CA    1 
ATOM   3334  C  C     . PRO   A  1  457  ? -39.670 38.855  68.428  1.00 28.41 ? 455  PRO   A C     1 
ATOM   3335  O  O     . PRO   A  1  457  ? -40.227 37.820  68.042  1.00 29.42 ? 455  PRO   A O     1 
ATOM   3336  C  CB    . PRO   A  1  457  ? -37.231 39.389  67.974  1.00 31.27 ? 455  PRO   A CB    1 
ATOM   3337  C  CG    . PRO   A  1  457  ? -36.555 40.640  67.561  1.00 30.48 ? 455  PRO   A CG    1 
ATOM   3338  C  CD    . PRO   A  1  457  ? -37.584 41.725  67.755  1.00 29.75 ? 455  PRO   A CD    1 
ATOM   3339  N  N     . LEU   A  1  458  ? -39.910 39.394  69.624  1.00 27.60 ? 456  LEU   A N     1 
ATOM   3340  C  CA    . LEU   A  1  458  ? -40.881 38.781  70.524  1.00 24.64 ? 456  LEU   A CA    1 
ATOM   3341  C  C     . LEU   A  1  458  ? -42.292 38.902  69.970  1.00 25.42 ? 456  LEU   A C     1 
ATOM   3342  O  O     . LEU   A  1  458  ? -43.041 37.924  69.932  1.00 25.58 ? 456  LEU   A O     1 
ATOM   3343  C  CB    . LEU   A  1  458  ? -40.796 39.426  71.906  1.00 24.45 ? 456  LEU   A CB    1 
ATOM   3344  C  CG    . LEU   A  1  458  ? -41.889 39.022  72.902  1.00 24.17 ? 456  LEU   A CG    1 
ATOM   3345  C  CD1   . LEU   A  1  458  ? -41.861 37.516  73.131  1.00 25.73 ? 456  LEU   A CD1   1 
ATOM   3346  C  CD2   . LEU   A  1  458  ? -41.676 39.776  74.201  1.00 24.77 ? 456  LEU   A CD2   1 
ATOM   3347  N  N     . TYR   A  1  459  ? -42.673 40.097  69.530  1.00 24.40 ? 457  TYR   A N     1 
ATOM   3348  C  CA    . TYR   A  1  459  ? -44.061 40.308  69.156  1.00 25.50 ? 457  TYR   A CA    1 
ATOM   3349  C  C     . TYR   A  1  459  ? -44.409 39.755  67.787  1.00 25.37 ? 457  TYR   A C     1 
ATOM   3350  O  O     . TYR   A  1  459  ? -45.594 39.551  67.505  1.00 26.38 ? 457  TYR   A O     1 
ATOM   3351  C  CB    . TYR   A  1  459  ? -44.468 41.767  69.356  1.00 23.78 ? 457  TYR   A CB    1 
ATOM   3352  C  CG    . TYR   A  1  459  ? -44.680 42.036  70.817  1.00 22.41 ? 457  TYR   A CG    1 
ATOM   3353  C  CD1   . TYR   A  1  459  ? -45.875 41.692  71.423  1.00 22.83 ? 457  TYR   A CD1   1 
ATOM   3354  C  CD2   . TYR   A  1  459  ? -43.667 42.564  71.603  1.00 21.52 ? 457  TYR   A CD2   1 
ATOM   3355  C  CE1   . TYR   A  1  459  ? -46.076 41.903  72.754  1.00 22.12 ? 457  TYR   A CE1   1 
ATOM   3356  C  CE2   . TYR   A  1  459  ? -43.864 42.791  72.955  1.00 19.99 ? 457  TYR   A CE2   1 
ATOM   3357  C  CZ    . TYR   A  1  459  ? -45.076 42.450  73.520  1.00 22.29 ? 457  TYR   A CZ    1 
ATOM   3358  O  OH    . TYR   A  1  459  ? -45.286 42.653  74.861  1.00 22.50 ? 457  TYR   A OH    1 
ATOM   3359  N  N     . GLU   A  1  460  ? -43.413 39.474  66.947  1.00 25.43 ? 458  GLU   A N     1 
ATOM   3360  C  CA    . GLU   A  1  460  ? -43.705 38.676  65.766  1.00 29.93 ? 458  GLU   A CA    1 
ATOM   3361  C  C     . GLU   A  1  460  ? -44.112 37.251  66.113  1.00 30.81 ? 458  GLU   A C     1 
ATOM   3362  O  O     . GLU   A  1  460  ? -44.634 36.542  65.246  1.00 34.05 ? 458  GLU   A O     1 
ATOM   3363  C  CB    . GLU   A  1  460  ? -42.543 38.722  64.777  1.00 32.37 ? 458  GLU   A CB    1 
ATOM   3364  C  CG    . GLU   A  1  460  ? -42.603 39.952  63.885  1.00 38.22 ? 458  GLU   A CG    1 
ATOM   3365  C  CD    . GLU   A  1  460  ? -41.343 40.157  63.081  1.00 46.61 ? 458  GLU   A CD    1 
ATOM   3366  O  OE1   . GLU   A  1  460  ? -40.388 39.376  63.272  1.00 43.73 ? 458  GLU   A OE1   1 
ATOM   3367  O  OE2   . GLU   A  1  460  ? -41.307 41.103  62.264  1.00 50.75 ? 458  GLU   A OE2   1 
ATOM   3368  N  N     . GLU   A  1  461  ? -43.904 36.827  67.356  1.00 29.27 ? 459  GLU   A N     1 
ATOM   3369  C  CA    . GLU   A  1  461  ? -44.443 35.572  67.859  1.00 29.62 ? 459  GLU   A CA    1 
ATOM   3370  C  C     . GLU   A  1  461  ? -45.783 35.758  68.554  1.00 28.79 ? 459  GLU   A C     1 
ATOM   3371  O  O     . GLU   A  1  461  ? -46.319 34.795  69.111  1.00 30.28 ? 459  GLU   A O     1 
ATOM   3372  C  CB    . GLU   A  1  461  ? -43.454 34.935  68.837  1.00 29.88 ? 459  GLU   A CB    1 
ATOM   3373  C  CG    . GLU   A  1  461  ? -42.064 34.805  68.274  1.00 30.67 ? 459  GLU   A CG    1 
ATOM   3374  C  CD    . GLU   A  1  461  ? -42.016 33.881  67.074  1.00 35.18 ? 459  GLU   A CD    1 
ATOM   3375  O  OE1   . GLU   A  1  461  ? -42.885 32.988  66.973  1.00 37.30 ? 459  GLU   A OE1   1 
ATOM   3376  O  OE2   . GLU   A  1  461  ? -41.104 34.049  66.235  1.00 36.87 ? 459  GLU   A OE2   1 
ATOM   3377  N  N     . VAL   A  1  462  ? -46.325 36.976  68.538  1.00 27.82 ? 460  VAL   A N     1 
ATOM   3378  C  CA    . VAL   A  1  462  ? -47.550 37.325  69.246  1.00 26.01 ? 460  VAL   A CA    1 
ATOM   3379  C  C     . VAL   A  1  462  ? -48.631 37.802  68.284  1.00 26.83 ? 460  VAL   A C     1 
ATOM   3380  O  O     . VAL   A  1  462  ? -49.756 37.289  68.284  1.00 28.61 ? 460  VAL   A O     1 
ATOM   3381  C  CB    . VAL   A  1  462  ? -47.278 38.384  70.336  1.00 25.95 ? 460  VAL   A CB    1 
ATOM   3382  C  CG1   . VAL   A  1  462  ? -48.571 38.797  71.013  1.00 24.83 ? 460  VAL   A CG1   1 
ATOM   3383  C  CG2   . VAL   A  1  462  ? -46.259 37.867  71.350  1.00 27.11 ? 460  VAL   A CG2   1 
ATOM   3384  N  N     . VAL   A  1  463  ? -48.302 38.786  67.445  1.00 26.64 ? 461  VAL   A N     1 
ATOM   3385  C  CA    . VAL   A  1  463  ? -49.280 39.395  66.552  1.00 26.76 ? 461  VAL   A CA    1 
ATOM   3386  C  C     . VAL   A  1  463  ? -49.646 38.424  65.440  1.00 32.26 ? 461  VAL   A C     1 
ATOM   3387  O  O     . VAL   A  1  463  ? -48.793 37.687  64.928  1.00 32.79 ? 461  VAL   A O     1 
ATOM   3388  C  CB    . VAL   A  1  463  ? -48.692 40.693  65.974  1.00 26.41 ? 461  VAL   A CB    1 
ATOM   3389  C  CG1   . VAL   A  1  463  ? -49.659 41.329  64.988  1.00 28.09 ? 461  VAL   A CG1   1 
ATOM   3390  C  CG2   . VAL   A  1  463  ? -48.338 41.663  67.092  1.00 27.15 ? 461  VAL   A CG2   1 
ATOM   3391  N  N     . GLY   A  1  464  ? -50.912 38.425  65.053  1.00 31.97 ? 462  GLY   A N     1 
ATOM   3392  C  CA    . GLY   A  1  464  ? -51.323 37.654  63.898  1.00 37.22 ? 462  GLY   A CA    1 
ATOM   3393  C  C     . GLY   A  1  464  ? -52.066 36.389  64.280  1.00 35.65 ? 462  GLY   A C     1 
ATOM   3394  O  O     . GLY   A  1  464  ? -51.818 35.777  65.325  1.00 33.10 ? 462  GLY   A O     1 
ATOM   3395  N  N     . ARG   A  1  465  ? -52.988 35.975  63.403  1.00 36.73 ? 463  ARG   A N     1 
ATOM   3396  C  CA    . ARG   A  1  465  ? -53.823 34.808  63.678  1.00 36.15 ? 463  ARG   A CA    1 
ATOM   3397  C  C     . ARG   A  1  465  ? -52.998 33.535  63.826  1.00 39.14 ? 463  ARG   A C     1 
ATOM   3398  O  O     . ARG   A  1  465  ? -53.420 32.599  64.515  1.00 43.95 ? 463  ARG   A O     1 
ATOM   3399  C  CB    . ARG   A  1  465  ? -54.872 34.642  62.577  1.00 42.14 ? 463  ARG   A CB    1 
ATOM   3400  N  N     . GLY   A  1  466  ? -51.834 33.476  63.195  1.00 35.88 ? 464  GLY   A N     1 
ATOM   3401  C  CA    . GLY   A  1  466  ? -50.978 32.319  63.343  1.00 37.94 ? 464  GLY   A CA    1 
ATOM   3402  C  C     . GLY   A  1  466  ? -50.151 32.290  64.604  1.00 38.48 ? 464  GLY   A C     1 
ATOM   3403  O  O     . GLY   A  1  466  ? -49.409 31.332  64.833  1.00 40.08 ? 464  GLY   A O     1 
ATOM   3404  N  N     . LYS   A  1  467  ? -50.252 33.329  65.438  1.00 34.50 ? 465  LYS   A N     1 
ATOM   3405  C  CA    . LYS   A  1  467  ? -49.494 33.397  66.682  1.00 31.35 ? 465  LYS   A CA    1 
ATOM   3406  C  C     . LYS   A  1  467  ? -50.495 33.435  67.828  1.00 33.68 ? 465  LYS   A C     1 
ATOM   3407  O  O     . LYS   A  1  467  ? -51.329 32.542  67.930  1.00 35.53 ? 465  LYS   A O     1 
ATOM   3408  C  CB    . LYS   A  1  467  ? -48.486 34.533  66.654  1.00 30.77 ? 465  LYS   A CB    1 
ATOM   3409  C  CG    . LYS   A  1  467  ? -47.459 34.427  65.544  1.00 34.42 ? 465  LYS   A CG    1 
ATOM   3410  C  CD    . LYS   A  1  467  ? -46.589 33.199  65.722  1.00 36.79 ? 465  LYS   A CD    1 
ATOM   3411  C  CE    . LYS   A  1  467  ? -45.410 33.229  64.766  1.00 40.68 ? 465  LYS   A CE    1 
ATOM   3412  N  NZ    . LYS   A  1  467  ? -44.499 32.073  64.978  1.00 37.43 ? 465  LYS   A NZ    1 
ATOM   3413  N  N     . LEU   A  1  468  ? -50.429 34.443  68.692  1.00 30.36 ? 466  LEU   A N     1 
ATOM   3414  C  CA    . LEU   A  1  468  ? -51.389 34.599  69.773  1.00 30.90 ? 466  LEU   A CA    1 
ATOM   3415  C  C     . LEU   A  1  468  ? -52.553 35.495  69.391  1.00 30.64 ? 466  LEU   A C     1 
ATOM   3416  O  O     . LEU   A  1  468  ? -53.491 35.632  70.182  1.00 31.45 ? 466  LEU   A O     1 
ATOM   3417  C  CB    . LEU   A  1  468  ? -50.698 35.151  71.022  1.00 31.23 ? 466  LEU   A CB    1 
ATOM   3418  C  CG    . LEU   A  1  468  ? -49.484 34.356  71.503  1.00 32.26 ? 466  LEU   A CG    1 
ATOM   3419  C  CD1   . LEU   A  1  468  ? -48.954 34.909  72.808  1.00 33.47 ? 466  LEU   A CD1   1 
ATOM   3420  C  CD2   . LEU   A  1  468  ? -49.847 32.883  71.642  1.00 31.93 ? 466  LEU   A CD2   1 
ATOM   3421  N  N     . ASP   A  1  469  ? -52.503 36.101  68.205  1.00 31.21 ? 467  ASP   A N     1 
ATOM   3422  C  CA    . ASP   A  1  469  ? -53.569 36.959  67.696  1.00 28.79 ? 467  ASP   A CA    1 
ATOM   3423  C  C     . ASP   A  1  469  ? -53.907 38.070  68.682  1.00 27.97 ? 467  ASP   A C     1 
ATOM   3424  O  O     . ASP   A  1  469  ? -55.069 38.329  68.996  1.00 26.27 ? 467  ASP   A O     1 
ATOM   3425  C  CB    . ASP   A  1  469  ? -54.808 36.157  67.303  1.00 32.29 ? 467  ASP   A CB    1 
ATOM   3426  C  CG    . ASP   A  1  469  ? -55.711 36.914  66.346  1.00 34.97 ? 467  ASP   A CG    1 
ATOM   3427  O  OD1   . ASP   A  1  469  ? -55.217 37.826  65.651  1.00 35.80 ? 467  ASP   A OD1   1 
ATOM   3428  O  OD2   . ASP   A  1  469  ? -56.917 36.604  66.293  1.00 41.20 ? 467  ASP   A OD2   1 
ATOM   3429  N  N     . ARG   A  1  470  ? -52.864 38.709  69.196  1.00 27.12 ? 468  ARG   A N     1 
ATOM   3430  C  CA    . ARG   A  1  470  ? -53.014 39.893  70.010  1.00 24.41 ? 468  ARG   A CA    1 
ATOM   3431  C  C     . ARG   A  1  470  ? -52.212 41.024  69.391  1.00 24.81 ? 468  ARG   A C     1 
ATOM   3432  O  O     . ARG   A  1  470  ? -51.092 40.806  68.911  1.00 23.61 ? 468  ARG   A O     1 
ATOM   3433  C  CB    . ARG   A  1  470  ? -52.525 39.658  71.447  1.00 24.92 ? 468  ARG   A CB    1 
ATOM   3434  C  CG    . ARG   A  1  470  ? -53.288 38.578  72.194  1.00 22.53 ? 468  ARG   A CG    1 
ATOM   3435  C  CD    . ARG   A  1  470  ? -54.758 38.943  72.360  1.00 22.86 ? 468  ARG   A CD    1 
ATOM   3436  N  NE    . ARG   A  1  470  ? -55.487 37.891  73.063  1.00 25.80 ? 468  ARG   A NE    1 
ATOM   3437  C  CZ    . ARG   A  1  470  ? -56.204 36.952  72.465  1.00 26.85 ? 468  ARG   A CZ    1 
ATOM   3438  N  NH1   . ARG   A  1  470  ? -56.340 36.921  71.148  1.00 28.27 ? 468  ARG   A NH1   1 
ATOM   3439  N  NH2   . ARG   A  1  470  ? -56.813 36.029  73.207  1.00 29.64 ? 468  ARG   A NH2   1 
ATOM   3440  N  N     . PRO   A  1  471  ? -52.753 42.230  69.378  1.00 22.33 ? 469  PRO   A N     1 
ATOM   3441  C  CA    . PRO   A  1  471  ? -52.074 43.347  68.725  1.00 22.57 ? 469  PRO   A CA    1 
ATOM   3442  C  C     . PRO   A  1  471  ? -50.964 43.899  69.599  1.00 22.01 ? 469  PRO   A C     1 
ATOM   3443  O  O     . PRO   A  1  471  ? -50.940 43.737  70.819  1.00 21.49 ? 469  PRO   A O     1 
ATOM   3444  C  CB    . PRO   A  1  471  ? -53.190 44.381  68.572  1.00 22.36 ? 469  PRO   A CB    1 
ATOM   3445  C  CG    . PRO   A  1  471  ? -54.081 44.104  69.748  1.00 22.62 ? 469  PRO   A CG    1 
ATOM   3446  C  CD    . PRO   A  1  471  ? -54.066 42.613  69.917  1.00 21.50 ? 469  PRO   A CD    1 
ATOM   3447  N  N     . CYS   A  1  472  ? -50.028 44.565  68.940  1.00 20.31 ? 470  CYS   A N     1 
ATOM   3448  C  CA    . CYS   A  1  472  ? -48.933 45.202  69.640  1.00 20.08 ? 470  CYS   A CA    1 
ATOM   3449  C  C     . CYS   A  1  472  ? -48.688 46.548  68.995  1.00 19.43 ? 470  CYS   A C     1 
ATOM   3450  O  O     . CYS   A  1  472  ? -48.598 46.641  67.767  1.00 20.57 ? 470  CYS   A O     1 
ATOM   3451  C  CB    . CYS   A  1  472  ? -47.659 44.361  69.538  1.00 20.63 ? 470  CYS   A CB    1 
ATOM   3452  S  SG    . CYS   A  1  472  ? -46.251 45.089  70.395  1.00 22.21 ? 470  CYS   A SG    1 
ATOM   3453  N  N     . ARG   A  1  473  ? -48.567 47.578  69.818  1.00 17.25 ? 471  ARG   A N     1 
ATOM   3454  C  CA    . ARG   A  1  473  ? -48.255 48.916  69.352  1.00 17.83 ? 471  ARG   A CA    1 
ATOM   3455  C  C     . ARG   A  1  473  ? -46.770 49.164  69.557  1.00 18.60 ? 471  ARG   A C     1 
ATOM   3456  O  O     . ARG   A  1  473  ? -46.248 48.997  70.664  1.00 18.61 ? 471  ARG   A O     1 
ATOM   3457  C  CB    . ARG   A  1  473  ? -49.043 49.962  70.125  1.00 17.56 ? 471  ARG   A CB    1 
ATOM   3458  C  CG    . ARG   A  1  473  ? -48.868 51.364  69.553  1.00 18.47 ? 471  ARG   A CG    1 
ATOM   3459  C  CD    . ARG   A  1  473  ? -49.812 52.349  70.217  1.00 18.07 ? 471  ARG   A CD    1 
ATOM   3460  N  NE    . ARG   A  1  473  ? -51.188 51.875  70.160  1.00 17.84 ? 471  ARG   A NE    1 
ATOM   3461  C  CZ    . ARG   A  1  473  ? -52.014 52.050  69.138  1.00 18.93 ? 471  ARG   A CZ    1 
ATOM   3462  N  NH1   . ARG   A  1  473  ? -51.693 52.816  68.106  1.00 18.96 ? 471  ARG   A NH1   1 
ATOM   3463  N  NH2   . ARG   A  1  473  ? -53.203 51.453  69.161  1.00 18.51 ? 471  ARG   A NH2   1 
ATOM   3464  N  N     . ILE   A  1  474  ? -46.107 49.592  68.497  1.00 17.63 ? 472  ILE   A N     1 
ATOM   3465  C  CA    . ILE   A  1  474  ? -44.669 49.801  68.514  1.00 16.58 ? 472  ILE   A CA    1 
ATOM   3466  C  C     . ILE   A  1  474  ? -44.404 51.248  68.881  1.00 18.23 ? 472  ILE   A C     1 
ATOM   3467  O  O     . ILE   A  1  474  ? -44.849 52.165  68.184  1.00 18.69 ? 472  ILE   A O     1 
ATOM   3468  C  CB    . ILE   A  1  474  ? -44.063 49.462  67.150  1.00 17.50 ? 472  ILE   A CB    1 
ATOM   3469  C  CG1   . ILE   A  1  474  ? -44.258 47.980  66.857  1.00 21.51 ? 472  ILE   A CG1   1 
ATOM   3470  C  CG2   . ILE   A  1  474  ? -42.591 49.829  67.140  1.00 19.52 ? 472  ILE   A CG2   1 
ATOM   3471  C  CD1   . ILE   A  1  474  ? -43.927 47.614  65.439  1.00 22.46 ? 472  ILE   A CD1   1 
ATOM   3472  N  N     . TYR   A  1  475  ? -43.685 51.455  69.981  1.00 17.29 ? 473  TYR   A N     1 
ATOM   3473  C  CA    . TYR   A  1  475  ? -43.253 52.790  70.358  1.00 17.33 ? 473  TYR   A CA    1 
ATOM   3474  C  C     . TYR   A  1  475  ? -42.068 53.140  69.470  1.00 18.48 ? 473  TYR   A C     1 
ATOM   3475  O  O     . TYR   A  1  475  ? -41.025 52.474  69.517  1.00 18.76 ? 473  TYR   A O     1 
ATOM   3476  C  CB    . TYR   A  1  475  ? -42.851 52.807  71.831  1.00 18.64 ? 473  TYR   A CB    1 
ATOM   3477  C  CG    . TYR   A  1  475  ? -42.569 54.179  72.410  1.00 20.72 ? 473  TYR   A CG    1 
ATOM   3478  C  CD1   . TYR   A  1  475  ? -41.302 54.756  72.307  1.00 23.23 ? 473  TYR   A CD1   1 
ATOM   3479  C  CD2   . TYR   A  1  475  ? -43.561 54.899  73.057  1.00 19.91 ? 473  TYR   A CD2   1 
ATOM   3480  C  CE1   . TYR   A  1  475  ? -41.040 56.011  72.835  1.00 22.63 ? 473  TYR   A CE1   1 
ATOM   3481  C  CE2   . TYR   A  1  475  ? -43.305 56.151  73.599  1.00 17.85 ? 473  TYR   A CE2   1 
ATOM   3482  C  CZ    . TYR   A  1  475  ? -42.046 56.704  73.482  1.00 22.90 ? 473  TYR   A CZ    1 
ATOM   3483  O  OH    . TYR   A  1  475  ? -41.794 57.953  74.008  1.00 23.48 ? 473  TYR   A OH    1 
ATOM   3484  N  N     . ALA   A  1  476  ? -42.236 54.177  68.659  1.00 17.60 ? 474  ALA   A N     1 
ATOM   3485  C  CA    . ALA   A  1  476  ? -41.357 54.431  67.522  1.00 16.60 ? 474  ALA   A CA    1 
ATOM   3486  C  C     . ALA   A  1  476  ? -40.659 55.764  67.694  1.00 18.36 ? 474  ALA   A C     1 
ATOM   3487  O  O     . ALA   A  1  476  ? -41.240 56.820  67.387  1.00 17.77 ? 474  ALA   A O     1 
ATOM   3488  C  CB    . ALA   A  1  476  ? -42.176 54.419  66.231  1.00 19.43 ? 474  ALA   A CB    1 
ATOM   3489  N  N     . PRO   A  1  477  ? -39.405 55.770  68.141  1.00 18.83 ? 475  PRO   A N     1 
ATOM   3490  C  CA    . PRO   A  1  477  ? -38.666 57.028  68.208  1.00 19.02 ? 475  PRO   A CA    1 
ATOM   3491  C  C     . PRO   A  1  477  ? -38.434 57.565  66.810  1.00 16.63 ? 475  PRO   A C     1 
ATOM   3492  O  O     . PRO   A  1  477  ? -38.237 56.812  65.855  1.00 17.96 ? 475  PRO   A O     1 
ATOM   3493  C  CB    . PRO   A  1  477  ? -37.339 56.632  68.872  1.00 18.37 ? 475  PRO   A CB    1 
ATOM   3494  C  CG    . PRO   A  1  477  ? -37.560 55.254  69.428  1.00 23.06 ? 475  PRO   A CG    1 
ATOM   3495  C  CD    . PRO   A  1  477  ? -38.584 54.620  68.542  1.00 20.72 ? 475  PRO   A CD    1 
ATOM   3496  N  N     . VAL   A  1  478  ? -38.487 58.879  66.695  1.00 16.08 ? 476  VAL   A N     1 
ATOM   3497  C  CA    . VAL   A  1  478  ? -38.327 59.568  65.426  1.00 19.21 ? 476  VAL   A CA    1 
ATOM   3498  C  C     . VAL   A  1  478  ? -37.392 60.735  65.679  1.00 22.22 ? 476  VAL   A C     1 
ATOM   3499  O  O     . VAL   A  1  478  ? -37.663 61.574  66.543  1.00 23.84 ? 476  VAL   A O     1 
ATOM   3500  C  CB    . VAL   A  1  478  ? -39.678 60.089  64.905  1.00 21.79 ? 476  VAL   A CB    1 
ATOM   3501  C  CG1   . VAL   A  1  478  ? -39.484 60.860  63.610  1.00 20.80 ? 476  VAL   A CG1   1 
ATOM   3502  C  CG2   . VAL   A  1  478  ? -40.663 58.939  64.716  1.00 19.99 ? 476  VAL   A CG2   1 
ATOM   3503  N  N     . GLY   A  1  479  ? -36.298 60.796  64.944  1.00 20.38 ? 477  GLY   A N     1 
ATOM   3504  C  CA    . GLY   A  1  479  ? -35.445 61.955  65.085  1.00 24.57 ? 477  GLY   A CA    1 
ATOM   3505  C  C     . GLY   A  1  479  ? -34.078 61.720  64.493  1.00 24.45 ? 477  GLY   A C     1 
ATOM   3506  O  O     . GLY   A  1  479  ? -33.741 60.628  64.037  1.00 22.54 ? 477  GLY   A O     1 
ATOM   3507  N  N     . THR   A  1  480  ? -33.296 62.789  64.520  1.00 25.18 ? 478  THR   A N     1 
ATOM   3508  C  CA    . THR   A  1  480  ? -31.965 62.803  63.942  1.00 29.41 ? 478  THR   A CA    1 
ATOM   3509  C  C     . THR   A  1  480  ? -30.980 62.097  64.864  1.00 32.05 ? 478  THR   A C     1 
ATOM   3510  O  O     . THR   A  1  480  ? -31.296 61.727  65.999  1.00 30.42 ? 478  THR   A O     1 
ATOM   3511  C  CB    . THR   A  1  480  ? -31.512 64.244  63.741  1.00 30.70 ? 478  THR   A CB    1 
ATOM   3512  O  OG1   . THR   A  1  480  ? -31.505 64.909  65.011  1.00 36.67 ? 478  THR   A OG1   1 
ATOM   3513  C  CG2   . THR   A  1  480  ? -32.454 64.967  62.799  1.00 31.40 ? 478  THR   A CG2   1 
ATOM   3514  N  N     . HIS   A  1  481  ? -29.756 61.929  64.356  1.00 31.43 ? 479  HIS   A N     1 
ATOM   3515  C  CA    . HIS   A  1  481  ? -28.688 61.332  65.151  1.00 36.86 ? 479  HIS   A CA    1 
ATOM   3516  C  C     . HIS   A  1  481  ? -28.466 62.108  66.443  1.00 37.57 ? 479  HIS   A C     1 
ATOM   3517  O  O     . HIS   A  1  481  ? -28.349 61.515  67.524  1.00 37.52 ? 479  HIS   A O     1 
ATOM   3518  C  CB    . HIS   A  1  481  ? -27.396 61.297  64.334  1.00 33.62 ? 479  HIS   A CB    1 
ATOM   3519  C  CG    . HIS   A  1  481  ? -27.465 60.424  63.121  1.00 38.28 ? 479  HIS   A CG    1 
ATOM   3520  N  ND1   . HIS   A  1  481  ? -26.385 60.228  62.286  1.00 34.32 ? 479  HIS   A ND1   1 
ATOM   3521  C  CD2   . HIS   A  1  481  ? -28.480 59.692  62.601  1.00 35.75 ? 479  HIS   A CD2   1 
ATOM   3522  C  CE1   . HIS   A  1  481  ? -26.732 59.418  61.302  1.00 38.74 ? 479  HIS   A CE1   1 
ATOM   3523  N  NE2   . HIS   A  1  481  ? -27.998 59.076  61.471  1.00 37.60 ? 479  HIS   A NE2   1 
ATOM   3524  N  N     . GLU   A  1  482  ? -28.400 63.440  66.349  1.00 42.02 ? 480  GLU   A N     1 
ATOM   3525  C  CA    . GLU   A  1  482  ? -28.152 64.261  67.531  1.00 41.81 ? 480  GLU   A CA    1 
ATOM   3526  C  C     . GLU   A  1  482  ? -29.228 64.047  68.586  1.00 40.99 ? 480  GLU   A C     1 
ATOM   3527  O  O     . GLU   A  1  482  ? -28.925 63.929  69.781  1.00 42.24 ? 480  GLU   A O     1 
ATOM   3528  C  CB    . GLU   A  1  482  ? -28.082 65.735  67.134  1.00 45.92 ? 480  GLU   A CB    1 
ATOM   3529  N  N     . THR   A  1  483  ? -30.491 63.979  68.160  1.00 33.84 ? 481  THR   A N     1 
ATOM   3530  C  CA    . THR   A  1  483  ? -31.590 63.831  69.107  1.00 37.30 ? 481  THR   A CA    1 
ATOM   3531  C  C     . THR   A  1  483  ? -31.615 62.434  69.719  1.00 37.16 ? 481  THR   A C     1 
ATOM   3532  O  O     . THR   A  1  483  ? -31.855 62.282  70.924  1.00 36.95 ? 481  THR   A O     1 
ATOM   3533  C  CB    . THR   A  1  483  ? -32.913 64.145  68.409  1.00 35.43 ? 481  THR   A CB    1 
ATOM   3534  N  N     . LEU   A  1  484  ? -31.365 61.402  68.906  1.00 34.37 ? 482  LEU   A N     1 
ATOM   3535  C  CA    . LEU   A  1  484  ? -31.452 60.029  69.396  1.00 33.41 ? 482  LEU   A CA    1 
ATOM   3536  C  C     . LEU   A  1  484  ? -30.360 59.727  70.413  1.00 33.91 ? 482  LEU   A C     1 
ATOM   3537  O  O     . LEU   A  1  484  ? -30.593 59.003  71.390  1.00 34.96 ? 482  LEU   A O     1 
ATOM   3538  C  CB    . LEU   A  1  484  ? -31.377 59.051  68.223  1.00 37.41 ? 482  LEU   A CB    1 
ATOM   3539  N  N     . LEU   A  1  485  ? -29.162 60.275  70.207  1.00 36.66 ? 483  LEU   A N     1 
ATOM   3540  C  CA    . LEU   A  1  485  ? -28.046 59.967  71.090  1.00 35.72 ? 483  LEU   A CA    1 
ATOM   3541  C  C     . LEU   A  1  485  ? -28.207 60.578  72.475  1.00 35.57 ? 483  LEU   A C     1 
ATOM   3542  O  O     . LEU   A  1  485  ? -27.556 60.113  73.418  1.00 35.12 ? 483  LEU   A O     1 
ATOM   3543  C  CB    . LEU   A  1  485  ? -26.735 60.432  70.452  1.00 32.71 ? 483  LEU   A CB    1 
ATOM   3544  C  CG    . LEU   A  1  485  ? -26.298 59.622  69.228  1.00 33.71 ? 483  LEU   A CG    1 
ATOM   3545  C  CD1   . LEU   A  1  485  ? -25.125 60.294  68.535  1.00 35.86 ? 483  LEU   A CD1   1 
ATOM   3546  C  CD2   . LEU   A  1  485  ? -25.954 58.191  69.618  1.00 29.80 ? 483  LEU   A CD2   1 
ATOM   3547  N  N     . ALA   A  1  486  ? -29.076 61.585  72.618  1.00 37.65 ? 484  ALA   A N     1 
ATOM   3548  C  CA    . ALA   A  1  486  ? -29.137 62.364  73.853  1.00 36.57 ? 484  ALA   A CA    1 
ATOM   3549  C  C     . ALA   A  1  486  ? -29.467 61.490  75.058  1.00 38.26 ? 484  ALA   A C     1 
ATOM   3550  O  O     . ALA   A  1  486  ? -28.828 61.603  76.112  1.00 36.52 ? 484  ALA   A O     1 
ATOM   3551  C  CB    . ALA   A  1  486  ? -30.154 63.497  73.705  1.00 35.09 ? 484  ALA   A CB    1 
ATOM   3552  N  N     . TYR   A  1  487  ? -30.470 60.615  74.928  1.00 37.56 ? 485  TYR   A N     1 
ATOM   3553  C  CA    . TYR   A  1  487  ? -30.899 59.761  76.032  1.00 34.03 ? 485  TYR   A CA    1 
ATOM   3554  C  C     . TYR   A  1  487  ? -30.932 58.292  75.631  1.00 33.31 ? 485  TYR   A C     1 
ATOM   3555  O  O     . TYR   A  1  487  ? -31.681 57.500  76.209  1.00 31.87 ? 485  TYR   A O     1 
ATOM   3556  C  CB    . TYR   A  1  487  ? -32.241 60.218  76.609  1.00 38.06 ? 485  TYR   A CB    1 
ATOM   3557  C  CG    . TYR   A  1  487  ? -32.224 61.670  77.036  1.00 40.22 ? 485  TYR   A CG    1 
ATOM   3558  C  CD1   . TYR   A  1  487  ? -31.668 62.049  78.253  1.00 44.22 ? 485  TYR   A CD1   1 
ATOM   3559  C  CD2   . TYR   A  1  487  ? -32.740 62.664  76.211  1.00 39.99 ? 485  TYR   A CD2   1 
ATOM   3560  C  CE1   . TYR   A  1  487  ? -31.636 63.377  78.643  1.00 47.95 ? 485  TYR   A CE1   1 
ATOM   3561  C  CE2   . TYR   A  1  487  ? -32.715 63.994  76.592  1.00 45.62 ? 485  TYR   A CE2   1 
ATOM   3562  C  CZ    . TYR   A  1  487  ? -32.161 64.347  77.809  1.00 49.96 ? 485  TYR   A CZ    1 
ATOM   3563  O  OH    . TYR   A  1  487  ? -32.131 65.672  78.192  1.00 51.55 ? 485  TYR   A OH    1 
ATOM   3564  N  N     . LEU   A  1  488  ? -30.107 57.909  74.653  1.00 35.36 ? 486  LEU   A N     1 
ATOM   3565  C  CA    . LEU   A  1  488  ? -30.048 56.506  74.255  1.00 28.77 ? 486  LEU   A CA    1 
ATOM   3566  C  C     . LEU   A  1  488  ? -29.513 55.625  75.379  1.00 30.32 ? 486  LEU   A C     1 
ATOM   3567  O  O     . LEU   A  1  488  ? -29.855 54.439  75.457  1.00 26.27 ? 486  LEU   A O     1 
ATOM   3568  C  CB    . LEU   A  1  488  ? -29.186 56.352  73.002  1.00 33.29 ? 486  LEU   A CB    1 
ATOM   3569  C  CG    . LEU   A  1  488  ? -29.216 54.953  72.385  1.00 37.16 ? 486  LEU   A CG    1 
ATOM   3570  C  CD1   . LEU   A  1  488  ? -30.658 54.493  72.250  1.00 36.59 ? 486  LEU   A CD1   1 
ATOM   3571  C  CD2   . LEU   A  1  488  ? -28.524 54.938  71.038  1.00 30.07 ? 486  LEU   A CD2   1 
ATOM   3572  N  N     . VAL   A  1  489  ? -28.668 56.181  76.250  1.00 33.29 ? 487  VAL   A N     1 
ATOM   3573  C  CA    . VAL   A  1  489  ? -28.130 55.392  77.354  1.00 30.81 ? 487  VAL   A CA    1 
ATOM   3574  C  C     . VAL   A  1  489  ? -29.257 54.882  78.242  1.00 30.40 ? 487  VAL   A C     1 
ATOM   3575  O  O     . VAL   A  1  489  ? -29.315 53.693  78.576  1.00 29.22 ? 487  VAL   A O     1 
ATOM   3576  C  CB    . VAL   A  1  489  ? -27.080 56.197  78.138  1.00 30.46 ? 487  VAL   A CB    1 
ATOM   3577  C  CG1   . VAL   A  1  489  ? -26.769 55.508  79.457  1.00 30.84 ? 487  VAL   A CG1   1 
ATOM   3578  C  CG2   . VAL   A  1  489  ? -25.807 56.367  77.296  1.00 29.23 ? 487  VAL   A CG2   1 
ATOM   3579  N  N     . ARG   A  1  490  ? -30.182 55.768  78.623  1.00 32.85 ? 488  ARG   A N     1 
ATOM   3580  C  CA    . ARG   A  1  490  ? -31.314 55.337  79.441  1.00 32.99 ? 488  ARG   A CA    1 
ATOM   3581  C  C     . ARG   A  1  490  ? -32.119 54.257  78.724  1.00 34.74 ? 488  ARG   A C     1 
ATOM   3582  O  O     . ARG   A  1  490  ? -32.492 53.241  79.324  1.00 34.19 ? 488  ARG   A O     1 
ATOM   3583  C  CB    . ARG   A  1  490  ? -32.201 56.535  79.801  1.00 34.05 ? 488  ARG   A CB    1 
ATOM   3584  C  CG    . ARG   A  1  490  ? -33.356 56.193  80.749  1.00 33.17 ? 488  ARG   A CG    1 
ATOM   3585  C  CD    . ARG   A  1  490  ? -34.336 57.360  80.962  1.00 32.64 ? 488  ARG   A CD    1 
ATOM   3586  N  NE    . ARG   A  1  490  ? -35.107 57.679  79.762  1.00 35.71 ? 488  ARG   A NE    1 
ATOM   3587  C  CZ    . ARG   A  1  490  ? -35.226 58.895  79.244  1.00 37.54 ? 488  ARG   A CZ    1 
ATOM   3588  N  NH1   . ARG   A  1  490  ? -34.640 59.945  79.799  1.00 35.76 ? 488  ARG   A NH1   1 
ATOM   3589  N  NH2   . ARG   A  1  490  ? -35.950 59.063  78.138  1.00 30.89 ? 488  ARG   A NH2   1 
ATOM   3590  N  N     . ARG   A  1  491  ? -32.362 54.446  77.422  1.00 32.49 ? 489  ARG   A N     1 
ATOM   3591  C  CA    . ARG   A  1  491  ? -33.205 53.516  76.680  1.00 33.76 ? 489  ARG   A CA    1 
ATOM   3592  C  C     . ARG   A  1  491  ? -32.554 52.150  76.556  1.00 39.56 ? 489  ARG   A C     1 
ATOM   3593  O  O     . ARG   A  1  491  ? -33.250 51.130  76.580  1.00 38.63 ? 489  ARG   A O     1 
ATOM   3594  C  CB    . ARG   A  1  491  ? -33.517 54.081  75.294  1.00 38.72 ? 489  ARG   A CB    1 
ATOM   3595  N  N     . LEU   A  1  492  ? -31.223 52.108  76.440  1.00 36.80 ? 490  LEU   A N     1 
ATOM   3596  C  CA    . LEU   A  1  492  ? -30.537 50.832  76.269  1.00 37.23 ? 490  LEU   A CA    1 
ATOM   3597  C  C     . LEU   A  1  492  ? -30.517 50.028  77.567  1.00 40.02 ? 490  LEU   A C     1 
ATOM   3598  O  O     . LEU   A  1  492  ? -30.601 48.793  77.539  1.00 35.44 ? 490  LEU   A O     1 
ATOM   3599  C  CB    . LEU   A  1  492  ? -29.121 51.060  75.736  1.00 37.80 ? 490  LEU   A CB    1 
ATOM   3600  N  N     . LEU   A  1  493  ? -30.399 50.700  78.710  1.00 35.48 ? 491  LEU   A N     1 
ATOM   3601  C  CA    . LEU   A  1  493  ? -30.393 49.999  79.988  1.00 30.07 ? 491  LEU   A CA    1 
ATOM   3602  C  C     . LEU   A  1  493  ? -31.736 49.323  80.240  1.00 37.91 ? 491  LEU   A C     1 
ATOM   3603  O  O     . LEU   A  1  493  ? -31.811 48.343  80.980  1.00 42.96 ? 491  LEU   A O     1 
ATOM   3604  C  CB    . LEU   A  1  493  ? -30.068 50.957  81.135  1.00 37.83 ? 491  LEU   A CB    1 
ATOM   3605  C  CG    . LEU   A  1  493  ? -28.672 51.571  81.097  1.00 37.83 ? 491  LEU   A CG    1 
ATOM   3606  C  CD1   . LEU   A  1  493  ? -28.311 52.169  82.460  1.00 39.42 ? 491  LEU   A CD1   1 
ATOM   3607  C  CD2   . LEU   A  1  493  ? -27.672 50.518  80.657  1.00 40.21 ? 491  LEU   A CD2   1 
ATOM   3608  N  N     . GLY   A  1  496  ? -30.938 46.193  78.944  1.00 46.88 ? 494  GLY   A N     1 
ATOM   3609  C  CA    . GLY   A  1  496  ? -29.531 45.874  78.760  1.00 45.62 ? 494  GLY   A CA    1 
ATOM   3610  C  C     . GLY   A  1  496  ? -28.782 45.605  80.055  1.00 52.02 ? 494  GLY   A C     1 
ATOM   3611  O  O     . GLY   A  1  496  ? -27.659 45.091  80.034  1.00 49.50 ? 494  GLY   A O     1 
ATOM   3612  N  N     . ALA   A  1  497  ? -29.398 45.967  81.182  1.00 43.21 ? 495  ALA   A N     1 
ATOM   3613  C  CA    . ALA   A  1  497  ? -28.842 45.662  82.494  1.00 41.17 ? 495  ALA   A CA    1 
ATOM   3614  C  C     . ALA   A  1  497  ? -28.899 44.159  82.750  1.00 36.12 ? 495  ALA   A C     1 
ATOM   3615  O  O     . ALA   A  1  497  ? -29.700 43.433  82.155  1.00 36.82 ? 495  ALA   A O     1 
ATOM   3616  C  CB    . ALA   A  1  497  ? -29.630 46.390  83.586  1.00 34.52 ? 495  ALA   A CB    1 
ATOM   3617  N  N     . ASN   A  1  498  ? -28.039 43.691  83.661  1.00 36.27 ? 496  ASN   A N     1 
ATOM   3618  C  CA    . ASN   A  1  498  ? -27.961 42.255  83.927  1.00 36.55 ? 496  ASN   A CA    1 
ATOM   3619  C  C     . ASN   A  1  498  ? -29.311 41.679  84.344  1.00 35.31 ? 496  ASN   A C     1 
ATOM   3620  O  O     . ASN   A  1  498  ? -29.591 40.502  84.087  1.00 37.16 ? 496  ASN   A O     1 
ATOM   3621  C  CB    . ASN   A  1  498  ? -26.896 41.964  84.987  1.00 41.71 ? 496  ASN   A CB    1 
ATOM   3622  N  N     . SER   A  1  499  ? -30.158 42.492  84.977  1.00 35.76 ? 497  SER   A N     1 
ATOM   3623  C  CA    . SER   A  1  499  ? -31.496 42.074  85.375  1.00 34.84 ? 497  SER   A CA    1 
ATOM   3624  C  C     . SER   A  1  499  ? -32.510 42.119  84.237  1.00 27.82 ? 497  SER   A C     1 
ATOM   3625  O  O     . SER   A  1  499  ? -33.597 41.549  84.381  1.00 31.73 ? 497  SER   A O     1 
ATOM   3626  C  CB    . SER   A  1  499  ? -31.991 42.943  86.539  1.00 35.56 ? 497  SER   A CB    1 
ATOM   3627  O  OG    . SER   A  1  499  ? -31.714 44.315  86.306  1.00 37.61 ? 497  SER   A OG    1 
ATOM   3628  N  N     . SER   A  1  500  ? -32.187 42.769  83.119  1.00 28.96 ? 498  SER   A N     1 
ATOM   3629  C  CA    . SER   A  1  500  ? -33.163 42.962  82.053  1.00 26.26 ? 498  SER   A CA    1 
ATOM   3630  C  C     . SER   A  1  500  ? -33.412 41.671  81.286  1.00 31.37 ? 498  SER   A C     1 
ATOM   3631  O  O     . SER   A  1  500  ? -32.479 40.927  80.967  1.00 29.90 ? 498  SER   A O     1 
ATOM   3632  C  CB    . SER   A  1  500  ? -32.676 44.029  81.079  1.00 33.41 ? 498  SER   A CB    1 
ATOM   3633  O  OG    . SER   A  1  500  ? -32.609 45.285  81.714  1.00 36.68 ? 498  SER   A OG    1 
ATOM   3634  N  N     . PHE   A  1  501  ? -34.689 41.421  80.970  1.00 26.20 ? 499  PHE   A N     1 
ATOM   3635  C  CA    . PHE   A  1  501  ? -35.049 40.254  80.173  1.00 28.59 ? 499  PHE   A CA    1 
ATOM   3636  C  C     . PHE   A  1  501  ? -34.278 40.208  78.862  1.00 31.14 ? 499  PHE   A C     1 
ATOM   3637  O  O     . PHE   A  1  501  ? -33.835 39.136  78.432  1.00 33.10 ? 499  PHE   A O     1 
ATOM   3638  C  CB    . PHE   A  1  501  ? -36.548 40.249  79.871  1.00 25.98 ? 499  PHE   A CB    1 
ATOM   3639  C  CG    . PHE   A  1  501  ? -36.973 39.094  79.014  1.00 24.33 ? 499  PHE   A CG    1 
ATOM   3640  C  CD1   . PHE   A  1  501  ? -37.289 37.881  79.586  1.00 25.73 ? 499  PHE   A CD1   1 
ATOM   3641  C  CD2   . PHE   A  1  501  ? -37.025 39.213  77.631  1.00 31.26 ? 499  PHE   A CD2   1 
ATOM   3642  C  CE1   . PHE   A  1  501  ? -37.673 36.805  78.809  1.00 30.48 ? 499  PHE   A CE1   1 
ATOM   3643  C  CE2   . PHE   A  1  501  ? -37.398 38.136  76.842  1.00 27.25 ? 499  PHE   A CE2   1 
ATOM   3644  C  CZ    . PHE   A  1  501  ? -37.725 36.930  77.437  1.00 30.23 ? 499  PHE   A CZ    1 
ATOM   3645  N  N     . VAL   A  1  502  ? -34.134 41.357  78.199  1.00 30.47 ? 500  VAL   A N     1 
ATOM   3646  C  CA    . VAL   A  1  502  ? -33.496 41.379  76.888  1.00 33.62 ? 500  VAL   A CA    1 
ATOM   3647  C  C     . VAL   A  1  502  ? -32.018 41.043  77.002  1.00 34.30 ? 500  VAL   A C     1 
ATOM   3648  O  O     . VAL   A  1  502  ? -31.435 40.450  76.088  1.00 42.23 ? 500  VAL   A O     1 
ATOM   3649  C  CB    . VAL   A  1  502  ? -33.734 42.725  76.182  1.00 34.83 ? 500  VAL   A CB    1 
ATOM   3650  N  N     . HIS   A  1  503  ? -31.383 41.418  78.109  1.00 33.49 ? 501  HIS   A N     1 
ATOM   3651  C  CA    . HIS   A  1  503  ? -30.020 40.963  78.350  1.00 32.57 ? 501  HIS   A CA    1 
ATOM   3652  C  C     . HIS   A  1  503  ? -29.996 39.472  78.658  1.00 35.33 ? 501  HIS   A C     1 
ATOM   3653  O  O     . HIS   A  1  503  ? -29.140 38.737  78.149  1.00 34.22 ? 501  HIS   A O     1 
ATOM   3654  C  CB    . HIS   A  1  503  ? -29.413 41.762  79.501  1.00 35.48 ? 501  HIS   A CB    1 
ATOM   3655  C  CG    . HIS   A  1  503  ? -28.045 41.305  79.904  1.00 39.15 ? 501  HIS   A CG    1 
ATOM   3656  N  ND1   . HIS   A  1  503  ? -27.833 40.393  80.916  1.00 37.48 ? 501  HIS   A ND1   1 
ATOM   3657  C  CD2   . HIS   A  1  503  ? -26.820 41.633  79.429  1.00 37.59 ? 501  HIS   A CD2   1 
ATOM   3658  C  CE1   . HIS   A  1  503  ? -26.536 40.181  81.050  1.00 37.21 ? 501  HIS   A CE1   1 
ATOM   3659  N  NE2   . HIS   A  1  503  ? -25.899 40.920  80.158  1.00 41.19 ? 501  HIS   A NE2   1 
ATOM   3660  N  N     . ARG   A  1  504  ? -30.943 39.003  79.469  1.00 30.60 ? 502  ARG   A N     1 
ATOM   3661  C  CA    . ARG   A  1  504  ? -30.922 37.615  79.910  1.00 32.33 ? 502  ARG   A CA    1 
ATOM   3662  C  C     . ARG   A  1  504  ? -31.266 36.657  78.775  1.00 37.28 ? 502  ARG   A C     1 
ATOM   3663  O  O     . ARG   A  1  504  ? -30.695 35.561  78.689  1.00 32.97 ? 502  ARG   A O     1 
ATOM   3664  C  CB    . ARG   A  1  504  ? -31.859 37.441  81.105  1.00 33.73 ? 502  ARG   A CB    1 
ATOM   3665  C  CG    . ARG   A  1  504  ? -31.337 38.116  82.370  1.00 34.69 ? 502  ARG   A CG    1 
ATOM   3666  C  CD    . ARG   A  1  504  ? -32.438 38.364  83.395  1.00 35.50 ? 502  ARG   A CD    1 
ATOM   3667  N  NE    . ARG   A  1  504  ? -33.220 37.169  83.687  1.00 36.44 ? 502  ARG   A NE    1 
ATOM   3668  C  CZ    . ARG   A  1  504  ? -32.824 36.181  84.479  1.00 37.56 ? 502  ARG   A CZ    1 
ATOM   3669  N  NH1   . ARG   A  1  504  ? -31.621 36.174  85.031  1.00 41.01 ? 502  ARG   A NH1   1 
ATOM   3670  N  NH2   . ARG   A  1  504  ? -33.656 35.171  84.722  1.00 39.46 ? 502  ARG   A NH2   1 
ATOM   3671  N  N     . ILE   A  1  505  ? -32.190 37.051  77.892  1.00 35.15 ? 503  ILE   A N     1 
ATOM   3672  C  CA    . ILE   A  1  505  ? -32.540 36.217  76.742  1.00 35.96 ? 503  ILE   A CA    1 
ATOM   3673  C  C     . ILE   A  1  505  ? -31.304 35.907  75.905  1.00 38.85 ? 503  ILE   A C     1 
ATOM   3674  O  O     . ILE   A  1  505  ? -31.187 34.814  75.335  1.00 39.62 ? 503  ILE   A O     1 
ATOM   3675  C  CB    . ILE   A  1  505  ? -33.669 36.870  75.911  1.00 38.14 ? 503  ILE   A CB    1 
ATOM   3676  C  CG1   . ILE   A  1  505  ? -34.185 35.918  74.837  1.00 40.47 ? 503  ILE   A CG1   1 
ATOM   3677  C  CG2   . ILE   A  1  505  ? -33.193 38.118  75.221  1.00 39.87 ? 503  ILE   A CG2   1 
ATOM   3678  C  CD1   . ILE   A  1  505  ? -35.142 34.894  75.350  1.00 33.54 ? 503  ILE   A CD1   1 
ATOM   3679  N  N     . ASN   A  1  506  ? -30.356 36.839  75.842  1.00 37.44 ? 504  ASN   A N     1 
ATOM   3680  C  CA    . ASN   A  1  506  ? -29.129 36.673  75.078  1.00 40.53 ? 504  ASN   A CA    1 
ATOM   3681  C  C     . ASN   A  1  506  ? -27.988 36.076  75.889  1.00 41.49 ? 504  ASN   A C     1 
ATOM   3682  O  O     . ASN   A  1  506  ? -26.904 35.865  75.334  1.00 44.92 ? 504  ASN   A O     1 
ATOM   3683  C  CB    . ASN   A  1  506  ? -28.683 38.015  74.493  1.00 43.91 ? 504  ASN   A CB    1 
ATOM   3684  C  CG    . ASN   A  1  506  ? -29.615 38.513  73.415  1.00 43.07 ? 504  ASN   A CG    1 
ATOM   3685  O  OD1   . ASN   A  1  506  ? -30.203 37.724  72.677  1.00 50.94 ? 504  ASN   A OD1   1 
ATOM   3686  N  ND2   . ASN   A  1  506  ? -29.756 39.829  73.315  1.00 50.90 ? 504  ASN   A ND2   1 
ATOM   3687  N  N     . ASP   A  1  507  ? -28.187 35.812  77.180  1.00 38.74 ? 505  ASP   A N     1 
ATOM   3688  C  CA    . ASP   A  1  507  ? -27.141 35.211  77.996  1.00 40.40 ? 505  ASP   A CA    1 
ATOM   3689  C  C     . ASP   A  1  507  ? -27.271 33.698  77.897  1.00 42.55 ? 505  ASP   A C     1 
ATOM   3690  O  O     . ASP   A  1  507  ? -28.255 33.139  78.405  1.00 38.41 ? 505  ASP   A O     1 
ATOM   3691  C  CB    . ASP   A  1  507  ? -27.265 35.657  79.446  1.00 39.11 ? 505  ASP   A CB    1 
ATOM   3692  C  CG    . ASP   A  1  507  ? -26.068 35.235  80.299  1.00 43.19 ? 505  ASP   A CG    1 
ATOM   3693  O  OD1   . ASP   A  1  507  ? -25.450 34.187  80.003  1.00 44.85 ? 505  ASP   A OD1   1 
ATOM   3694  O  OD2   . ASP   A  1  507  ? -25.744 35.950  81.269  1.00 41.25 ? 505  ASP   A OD2   1 
ATOM   3695  N  N     . PRO   A  1  508  ? -26.316 32.998  77.281  1.00 45.40 ? 506  PRO   A N     1 
ATOM   3696  C  CA    . PRO   A  1  508  ? -26.439 31.535  77.171  1.00 46.88 ? 506  PRO   A CA    1 
ATOM   3697  C  C     . PRO   A  1  508  ? -26.451 30.830  78.513  1.00 43.51 ? 506  PRO   A C     1 
ATOM   3698  O  O     . PRO   A  1  508  ? -26.953 29.702  78.601  1.00 47.63 ? 506  PRO   A O     1 
ATOM   3699  C  CB    . PRO   A  1  508  ? -25.212 31.134  76.338  1.00 49.80 ? 506  PRO   A CB    1 
ATOM   3700  C  CG    . PRO   A  1  508  ? -24.695 32.421  75.735  1.00 51.02 ? 506  PRO   A CG    1 
ATOM   3701  C  CD    . PRO   A  1  508  ? -25.055 33.496  76.710  1.00 44.74 ? 506  PRO   A CD    1 
ATOM   3702  N  N     . LYS   A  1  509  ? -25.924 31.461  79.562  1.00 42.10 ? 507  LYS   A N     1 
ATOM   3703  C  CA    . LYS   A  1  509  ? -25.894 30.864  80.889  1.00 40.42 ? 507  LYS   A CA    1 
ATOM   3704  C  C     . LYS   A  1  509  ? -27.230 30.955  81.617  1.00 42.35 ? 507  LYS   A C     1 
ATOM   3705  O  O     . LYS   A  1  509  ? -27.363 30.380  82.701  1.00 43.30 ? 507  LYS   A O     1 
ATOM   3706  C  CB    . LYS   A  1  509  ? -24.800 31.522  81.736  1.00 45.63 ? 507  LYS   A CB    1 
ATOM   3707  N  N     . VAL   A  1  510  ? -28.211 31.659  81.062  1.00 40.80 ? 508  VAL   A N     1 
ATOM   3708  C  CA    . VAL   A  1  510  ? -29.538 31.773  81.660  1.00 37.49 ? 508  VAL   A CA    1 
ATOM   3709  C  C     . VAL   A  1  510  ? -30.456 30.775  80.967  1.00 37.57 ? 508  VAL   A C     1 
ATOM   3710  O  O     . VAL   A  1  510  ? -30.665 30.850  79.751  1.00 40.63 ? 508  VAL   A O     1 
ATOM   3711  C  CB    . VAL   A  1  510  ? -30.082 33.205  81.545  1.00 39.22 ? 508  VAL   A CB    1 
ATOM   3712  C  CG1   . VAL   A  1  510  ? -31.508 33.272  82.071  1.00 36.91 ? 508  VAL   A CG1   1 
ATOM   3713  C  CG2   . VAL   A  1  510  ? -29.185 34.183  82.295  1.00 37.07 ? 508  VAL   A CG2   1 
ATOM   3714  N  N     . SER   A  1  511  ? -31.000 29.836  81.734  1.00 36.34 ? 509  SER   A N     1 
ATOM   3715  C  CA    . SER   A  1  511  ? -31.855 28.811  81.161  1.00 36.28 ? 509  SER   A CA    1 
ATOM   3716  C  C     . SER   A  1  511  ? -33.252 29.362  80.893  1.00 35.89 ? 509  SER   A C     1 
ATOM   3717  O  O     . SER   A  1  511  ? -33.656 30.399  81.429  1.00 36.62 ? 509  SER   A O     1 
ATOM   3718  C  CB    . SER   A  1  511  ? -31.968 27.616  82.107  1.00 42.32 ? 509  SER   A CB    1 
ATOM   3719  O  OG    . SER   A  1  511  ? -32.706 27.965  83.266  1.00 38.99 ? 509  SER   A OG    1 
ATOM   3720  N  N     . ILE   A  1  512  ? -33.992 28.648  80.045  1.00 34.32 ? 510  ILE   A N     1 
ATOM   3721  C  CA    . ILE   A  1  512  ? -35.377 29.020  79.783  1.00 36.22 ? 510  ILE   A CA    1 
ATOM   3722  C  C     . ILE   A  1  512  ? -36.225 28.838  81.035  1.00 39.66 ? 510  ILE   A C     1 
ATOM   3723  O  O     . ILE   A  1  512  ? -37.111 29.653  81.324  1.00 37.28 ? 510  ILE   A O     1 
ATOM   3724  C  CB    . ILE   A  1  512  ? -35.923 28.246  78.570  1.00 35.70 ? 510  ILE   A CB    1 
ATOM   3725  C  CG1   . ILE   A  1  512  ? -35.127 28.621  77.320  1.00 35.71 ? 510  ILE   A CG1   1 
ATOM   3726  C  CG2   . ILE   A  1  512  ? -37.399 28.539  78.363  1.00 36.45 ? 510  ILE   A CG2   1 
ATOM   3727  C  CD1   . ILE   A  1  512  ? -35.598 27.948  76.065  1.00 39.96 ? 510  ILE   A CD1   1 
ATOM   3728  N  N     . ASP   A  1  513  ? -35.960 27.779  81.807  1.00 38.91 ? 511  ASP   A N     1 
ATOM   3729  C  CA    . ASP   A  1  513  ? -36.636 27.613  83.091  1.00 37.38 ? 511  ASP   A CA    1 
ATOM   3730  C  C     . ASP   A  1  513  ? -36.418 28.827  83.986  1.00 38.30 ? 511  ASP   A C     1 
ATOM   3731  O  O     . ASP   A  1  513  ? -37.343 29.277  84.671  1.00 35.60 ? 511  ASP   A O     1 
ATOM   3732  C  CB    . ASP   A  1  513  ? -36.150 26.343  83.789  1.00 43.48 ? 511  ASP   A CB    1 
ATOM   3733  C  CG    . ASP   A  1  513  ? -36.629 25.081  83.104  1.00 48.74 ? 511  ASP   A CG    1 
ATOM   3734  O  OD1   . ASP   A  1  513  ? -37.778 25.061  82.614  1.00 48.62 ? 511  ASP   A OD1   1 
ATOM   3735  O  OD2   . ASP   A  1  513  ? -35.851 24.103  83.057  1.00 58.51 ? 511  ASP   A OD2   1 
ATOM   3736  N  N     . GLU   A  1  514  ? -35.202 29.375  83.988  1.00 35.76 ? 512  GLU   A N     1 
ATOM   3737  C  CA    . GLU   A  1  514  ? -34.955 30.598  84.742  1.00 36.22 ? 512  GLU   A CA    1 
ATOM   3738  C  C     . GLU   A  1  514  ? -35.768 31.759  84.186  1.00 34.77 ? 512  GLU   A C     1 
ATOM   3739  O  O     . GLU   A  1  514  ? -36.260 32.602  84.945  1.00 34.79 ? 512  GLU   A O     1 
ATOM   3740  C  CB    . GLU   A  1  514  ? -33.461 30.927  84.735  1.00 38.20 ? 512  GLU   A CB    1 
ATOM   3741  C  CG    . GLU   A  1  514  ? -32.640 30.066  85.684  1.00 42.65 ? 512  GLU   A CG    1 
ATOM   3742  C  CD    . GLU   A  1  514  ? -31.138 30.284  85.546  1.00 47.20 ? 512  GLU   A CD    1 
ATOM   3743  O  OE1   . GLU   A  1  514  ? -30.638 30.333  84.403  1.00 47.25 ? 512  GLU   A OE1   1 
ATOM   3744  O  OE2   . GLU   A  1  514  ? -30.454 30.404  86.583  1.00 57.31 ? 512  GLU   A OE2   1 
ATOM   3745  N  N     . LEU   A  1  515  ? -35.930 31.818  82.866  1.00 35.24 ? 513  LEU   A N     1 
ATOM   3746  C  CA    . LEU   A  1  515  ? -36.628 32.955  82.274  1.00 33.32 ? 513  LEU   A CA    1 
ATOM   3747  C  C     . LEU   A  1  515  ? -38.134 32.858  82.463  1.00 30.64 ? 513  LEU   A C     1 
ATOM   3748  O  O     . LEU   A  1  515  ? -38.824 33.881  82.437  1.00 31.55 ? 513  LEU   A O     1 
ATOM   3749  C  CB    . LEU   A  1  515  ? -36.281 33.085  80.791  1.00 32.92 ? 513  LEU   A CB    1 
ATOM   3750  C  CG    . LEU   A  1  515  ? -34.855 33.545  80.494  1.00 32.39 ? 513  LEU   A CG    1 
ATOM   3751  C  CD1   . LEU   A  1  515  ? -34.538 33.441  79.007  1.00 34.88 ? 513  LEU   A CD1   1 
ATOM   3752  C  CD2   . LEU   A  1  515  ? -34.651 34.967  80.992  1.00 32.52 ? 513  LEU   A CD2   1 
ATOM   3753  N  N     . ILE   A  1  516  ? -38.665 31.652  82.649  1.00 29.53 ? 514  ILE   A N     1 
ATOM   3754  C  CA    . ILE   A  1  516  ? -40.108 31.486  82.761  1.00 31.35 ? 514  ILE   A CA    1 
ATOM   3755  C  C     . ILE   A  1  516  ? -40.499 31.365  84.225  1.00 32.36 ? 514  ILE   A C     1 
ATOM   3756  O  O     . ILE   A  1  516  ? -41.655 31.058  84.547  1.00 31.87 ? 514  ILE   A O     1 
ATOM   3757  C  CB    . ILE   A  1  516  ? -40.610 30.280  81.948  1.00 31.26 ? 514  ILE   A CB    1 
ATOM   3758  C  CG1   . ILE   A  1  516  ? -40.055 28.975  82.529  1.00 35.78 ? 514  ILE   A CG1   1 
ATOM   3759  C  CG2   . ILE   A  1  516  ? -40.244 30.444  80.470  1.00 34.10 ? 514  ILE   A CG2   1 
ATOM   3760  C  CD1   . ILE   A  1  516  ? -40.547 27.734  81.823  1.00 36.78 ? 514  ILE   A CD1   1 
ATOM   3761  N  N     . ALA   A  1  517  ? -39.537 31.589  85.117  1.00 29.69 ? 515  ALA   A N     1 
ATOM   3762  C  CA    . ALA   A  1  517  ? -39.832 31.586  86.542  1.00 30.58 ? 515  ALA   A CA    1 
ATOM   3763  C  C     . ALA   A  1  517  ? -40.926 32.602  86.829  1.00 28.89 ? 515  ALA   A C     1 
ATOM   3764  O  O     . ALA   A  1  517  ? -40.906 33.719  86.308  1.00 27.67 ? 515  ALA   A O     1 
ATOM   3765  C  CB    . ALA   A  1  517  ? -38.576 31.937  87.333  1.00 31.12 ? 515  ALA   A CB    1 
ATOM   3766  N  N     . ASP   A  1  518  ? -41.896 32.196  87.628  1.00 28.76 ? 516  ASP   A N     1 
ATOM   3767  C  CA    . ASP   A  1  518  ? -43.040 33.025  87.962  1.00 29.40 ? 516  ASP   A CA    1 
ATOM   3768  C  C     . ASP   A  1  518  ? -42.682 33.963  89.107  1.00 28.28 ? 516  ASP   A C     1 
ATOM   3769  O  O     . ASP   A  1  518  ? -42.548 33.521  90.255  1.00 29.63 ? 516  ASP   A O     1 
ATOM   3770  C  CB    . ASP   A  1  518  ? -44.208 32.128  88.360  1.00 30.24 ? 516  ASP   A CB    1 
ATOM   3771  C  CG    . ASP   A  1  518  ? -45.449 32.914  88.707  1.00 29.93 ? 516  ASP   A CG    1 
ATOM   3772  O  OD1   . ASP   A  1  518  ? -45.437 34.156  88.557  1.00 29.87 ? 516  ASP   A OD1   1 
ATOM   3773  O  OD2   . ASP   A  1  518  ? -46.436 32.284  89.131  1.00 35.11 ? 516  ASP   A OD2   1 
ATOM   3774  N  N     . PRO   A  1  519  ? -42.541 35.263  88.845  1.00 28.46 ? 517  PRO   A N     1 
ATOM   3775  C  CA    . PRO   A  1  519  ? -42.165 36.176  89.933  1.00 26.57 ? 517  PRO   A CA    1 
ATOM   3776  C  C     . PRO   A  1  519  ? -43.178 36.214  91.065  1.00 25.46 ? 517  PRO   A C     1 
ATOM   3777  O  O     . PRO   A  1  519  ? -42.790 36.443  92.216  1.00 27.35 ? 517  PRO   A O     1 
ATOM   3778  C  CB    . PRO   A  1  519  ? -42.025 37.533  89.223  1.00 27.44 ? 517  PRO   A CB    1 
ATOM   3779  C  CG    . PRO   A  1  519  ? -42.869 37.418  88.015  1.00 29.76 ? 517  PRO   A CG    1 
ATOM   3780  C  CD    . PRO   A  1  519  ? -42.798 35.979  87.583  1.00 26.48 ? 517  PRO   A CD    1 
ATOM   3781  N  N     . VAL   A  1  520  ? -44.459 35.972  90.773  1.00 26.07 ? 518  VAL   A N     1 
ATOM   3782  C  CA    . VAL   A  1  520  ? -45.482 36.000  91.818  1.00 25.25 ? 518  VAL   A CA    1 
ATOM   3783  C  C     . VAL   A  1  520  ? -45.226 34.905  92.842  1.00 30.85 ? 518  VAL   A C     1 
ATOM   3784  O  O     . VAL   A  1  520  ? -45.227 35.149  94.053  1.00 29.46 ? 518  VAL   A O     1 
ATOM   3785  C  CB    . VAL   A  1  520  ? -46.885 35.882  91.202  1.00 28.19 ? 518  VAL   A CB    1 
ATOM   3786  C  CG1   . VAL   A  1  520  ? -47.935 35.876  92.298  1.00 29.56 ? 518  VAL   A CG1   1 
ATOM   3787  C  CG2   . VAL   A  1  520  ? -47.127 37.021  90.240  1.00 25.83 ? 518  VAL   A CG2   1 
ATOM   3788  N  N     . GLU   A  1  521  ? -44.989 33.683  92.365  1.00 29.74 ? 519  GLU   A N     1 
ATOM   3789  C  CA    . GLU   A  1  521  ? -44.740 32.572  93.278  1.00 31.23 ? 519  GLU   A CA    1 
ATOM   3790  C  C     . GLU   A  1  521  ? -43.369 32.666  93.935  1.00 32.44 ? 519  GLU   A C     1 
ATOM   3791  O  O     . GLU   A  1  521  ? -43.209 32.238  95.083  1.00 34.52 ? 519  GLU   A O     1 
ATOM   3792  C  CB    . GLU   A  1  521  ? -44.925 31.244  92.547  1.00 34.08 ? 519  GLU   A CB    1 
ATOM   3793  C  CG    . GLU   A  1  521  ? -46.361 31.005  92.118  1.00 35.23 ? 519  GLU   A CG    1 
ATOM   3794  C  CD    . GLU   A  1  521  ? -47.315 31.056  93.292  1.00 40.87 ? 519  GLU   A CD    1 
ATOM   3795  O  OE1   . GLU   A  1  521  ? -46.964 30.513  94.361  1.00 42.65 ? 519  GLU   A OE1   1 
ATOM   3796  O  OE2   . GLU   A  1  521  ? -48.407 31.647  93.157  1.00 43.39 ? 519  GLU   A OE2   1 
ATOM   3797  N  N     . VAL   A  1  522  ? -42.372 33.216  93.236  1.00 32.34 ? 520  VAL   A N     1 
ATOM   3798  C  CA    . VAL   A  1  522  ? -41.053 33.388  93.840  1.00 28.72 ? 520  VAL   A CA    1 
ATOM   3799  C  C     . VAL   A  1  522  ? -41.121 34.377  94.998  1.00 36.37 ? 520  VAL   A C     1 
ATOM   3800  O  O     . VAL   A  1  522  ? -40.588 34.124  96.086  1.00 33.63 ? 520  VAL   A O     1 
ATOM   3801  C  CB    . VAL   A  1  522  ? -40.011 33.800  92.783  1.00 31.48 ? 520  VAL   A CB    1 
ATOM   3802  C  CG1   . VAL   A  1  522  ? -38.678 34.112  93.449  1.00 31.11 ? 520  VAL   A CG1   1 
ATOM   3803  C  CG2   . VAL   A  1  522  ? -39.844 32.700  91.735  1.00 32.76 ? 520  VAL   A CG2   1 
ATOM   3804  N  N     . VAL   A  1  523  ? -41.786 35.514  94.785  1.00 29.26 ? 521  VAL   A N     1 
ATOM   3805  C  CA    . VAL   A  1  523  ? -41.940 36.485  95.863  1.00 30.12 ? 521  VAL   A CA    1 
ATOM   3806  C  C     . VAL   A  1  523  ? -42.751 35.890  97.006  1.00 32.71 ? 521  VAL   A C     1 
ATOM   3807  O  O     . VAL   A  1  523  ? -42.406 36.061  98.180  1.00 31.53 ? 521  VAL   A O     1 
ATOM   3808  C  CB    . VAL   A  1  523  ? -42.549 37.795  95.331  1.00 26.57 ? 521  VAL   A CB    1 
ATOM   3809  C  CG1   . VAL   A  1  523  ? -42.923 38.718  96.483  1.00 30.03 ? 521  VAL   A CG1   1 
ATOM   3810  C  CG2   . VAL   A  1  523  ? -41.572 38.482  94.403  1.00 29.66 ? 521  VAL   A CG2   1 
ATOM   3811  N  N     . ARG   A  1  524  ? -43.833 35.172  96.680  1.00 30.28 ? 522  ARG   A N     1 
ATOM   3812  C  CA    . ARG   A  1  524  ? -44.686 34.600  97.719  1.00 32.13 ? 522  ARG   A CA    1 
ATOM   3813  C  C     . ARG   A  1  524  ? -43.906 33.685  98.653  1.00 37.27 ? 522  ARG   A C     1 
ATOM   3814  O  O     . ARG   A  1  524  ? -44.228 33.597  99.843  1.00 40.24 ? 522  ARG   A O     1 
ATOM   3815  C  CB    . ARG   A  1  524  ? -45.843 33.827  97.086  1.00 35.91 ? 522  ARG   A CB    1 
ATOM   3816  C  CG    . ARG   A  1  524  ? -46.809 33.242  98.110  1.00 37.78 ? 522  ARG   A CG    1 
ATOM   3817  C  CD    . ARG   A  1  524  ? -47.679 32.155  97.523  1.00 40.19 ? 522  ARG   A CD    1 
ATOM   3818  N  NE    . ARG   A  1  524  ? -48.279 32.562  96.260  1.00 39.29 ? 522  ARG   A NE    1 
ATOM   3819  C  CZ    . ARG   A  1  524  ? -49.321 33.374  96.151  1.00 35.66 ? 522  ARG   A CZ    1 
ATOM   3820  N  NH1   . ARG   A  1  524  ? -49.889 33.917  97.216  1.00 38.81 ? 522  ARG   A NH1   1 
ATOM   3821  N  NH2   . ARG   A  1  524  ? -49.807 33.646  94.945  1.00 37.86 ? 522  ARG   A NH2   1 
ATOM   3822  N  N     . ALA   A  1  525  ? -42.871 33.022  98.143  1.00 34.30 ? 523  ALA   A N     1 
ATOM   3823  C  CA    . ALA   A  1  525  ? -42.119 32.032  98.901  1.00 38.60 ? 523  ALA   A CA    1 
ATOM   3824  C  C     . ALA   A  1  525  ? -40.886 32.604  99.591  1.00 37.69 ? 523  ALA   A C     1 
ATOM   3825  O  O     . ALA   A  1  525  ? -40.171 31.855  100.265 1.00 42.69 ? 523  ALA   A O     1 
ATOM   3826  C  CB    . ALA   A  1  525  ? -41.717 30.869  97.989  1.00 37.92 ? 523  ALA   A CB    1 
ATOM   3827  N  N     . MET   A  1  526  ? -40.614 33.897  99.443  1.00 37.31 ? 524  MET   A N     1 
ATOM   3828  C  CA    A MET   A  1  526  ? -39.484 34.510  100.125 0.49 37.78 ? 524  MET   A CA    1 
ATOM   3829  C  CA    B MET   A  1  526  ? -39.475 34.480  100.126 0.51 37.78 ? 524  MET   A CA    1 
ATOM   3830  C  C     . MET   A  1  526  ? -39.737 34.538  101.631 1.00 39.50 ? 524  MET   A C     1 
ATOM   3831  O  O     . MET   A  1  526  ? -40.889 34.604  102.070 1.00 37.77 ? 524  MET   A O     1 
ATOM   3832  C  CB    A MET   A  1  526  ? -39.286 35.941  99.630  0.49 38.77 ? 524  MET   A CB    1 
ATOM   3833  C  CB    B MET   A  1  526  ? -39.185 35.875  99.578  0.51 38.76 ? 524  MET   A CB    1 
ATOM   3834  C  CG    A MET   A  1  526  ? -38.707 36.044  98.234  0.49 38.97 ? 524  MET   A CG    1 
ATOM   3835  C  CG    B MET   A  1  526  ? -38.372 35.853  98.293  0.51 39.23 ? 524  MET   A CG    1 
ATOM   3836  S  SD    A MET   A  1  526  ? -37.043 35.363  98.147  0.49 45.50 ? 524  MET   A SD    1 
ATOM   3837  S  SD    B MET   A  1  526  ? -38.205 37.472  97.525  0.51 39.47 ? 524  MET   A SD    1 
ATOM   3838  C  CE    A MET   A  1  526  ? -36.170 36.438  99.287  0.49 38.48 ? 524  MET   A CE    1 
ATOM   3839  C  CE    B MET   A  1  526  ? -36.870 37.169  96.371  0.51 38.97 ? 524  MET   A CE    1 
ATOM   3840  N  N     . PRO   A  1  527  ? -38.678 34.487  102.449 1.00 43.41 ? 525  PRO   A N     1 
ATOM   3841  C  CA    . PRO   A  1  527  ? -38.897 34.489  103.906 1.00 45.74 ? 525  PRO   A CA    1 
ATOM   3842  C  C     . PRO   A  1  527  ? -39.562 35.755  104.408 1.00 42.50 ? 525  PRO   A C     1 
ATOM   3843  O  O     . PRO   A  1  527  ? -40.461 35.690  105.255 1.00 40.90 ? 525  PRO   A O     1 
ATOM   3844  C  CB    . PRO   A  1  527  ? -37.485 34.296  104.478 1.00 45.52 ? 525  PRO   A CB    1 
ATOM   3845  C  CG    . PRO   A  1  527  ? -36.574 34.767  103.399 1.00 47.13 ? 525  PRO   A CG    1 
ATOM   3846  C  CD    . PRO   A  1  527  ? -37.248 34.396  102.110 1.00 41.80 ? 525  PRO   A CD    1 
ATOM   3847  N  N     . VAL   A  1  528  ? -39.150 36.911  103.899 1.00 40.07 ? 526  VAL   A N     1 
ATOM   3848  C  CA    . VAL   A  1  528  ? -39.816 38.178  104.164 1.00 36.95 ? 526  VAL   A CA    1 
ATOM   3849  C  C     . VAL   A  1  528  ? -40.326 38.679  102.823 1.00 32.65 ? 526  VAL   A C     1 
ATOM   3850  O  O     . VAL   A  1  528  ? -39.532 39.061  101.953 1.00 36.09 ? 526  VAL   A O     1 
ATOM   3851  C  CB    . VAL   A  1  528  ? -38.875 39.199  104.813 1.00 35.11 ? 526  VAL   A CB    1 
ATOM   3852  C  CG1   . VAL   A  1  528  ? -39.633 40.469  105.156 1.00 39.33 ? 526  VAL   A CG1   1 
ATOM   3853  C  CG2   . VAL   A  1  528  ? -38.225 38.603  106.054 1.00 41.73 ? 526  VAL   A CG2   1 
ATOM   3854  N  N     . VAL   A  1  529  ? -41.642 38.662  102.641 1.00 33.17 ? 527  VAL   A N     1 
ATOM   3855  C  CA    . VAL   A  1  529  ? -42.216 39.117  101.383 1.00 30.87 ? 527  VAL   A CA    1 
ATOM   3856  C  C     . VAL   A  1  529  ? -41.970 40.612  101.236 1.00 32.43 ? 527  VAL   A C     1 
ATOM   3857  O  O     . VAL   A  1  529  ? -42.327 41.406  102.114 1.00 32.50 ? 527  VAL   A O     1 
ATOM   3858  C  CB    . VAL   A  1  529  ? -43.711 38.785  101.309 1.00 29.05 ? 527  VAL   A CB    1 
ATOM   3859  C  CG1   . VAL   A  1  529  ? -44.313 39.410  100.073 1.00 29.67 ? 527  VAL   A CG1   1 
ATOM   3860  C  CG2   . VAL   A  1  529  ? -43.904 37.282  101.286 1.00 35.70 ? 527  VAL   A CG2   1 
ATOM   3861  N  N     . GLY   A  1  530  ? -41.336 40.998  100.133 1.00 28.62 ? 528  GLY   A N     1 
ATOM   3862  C  CA    . GLY   A  1  530  ? -41.151 42.405  99.846  1.00 27.89 ? 528  GLY   A CA    1 
ATOM   3863  C  C     . GLY   A  1  530  ? -39.989 43.070  100.541 1.00 24.95 ? 528  GLY   A C     1 
ATOM   3864  O  O     . GLY   A  1  530  ? -39.969 44.296  100.638 1.00 26.28 ? 528  GLY   A O     1 
ATOM   3865  N  N     . ALA   A  1  531  ? -39.013 42.308  101.033 1.00 27.48 ? 529  ALA   A N     1 
ATOM   3866  C  CA    . ALA   A  1  531  ? -37.862 42.928  101.673 1.00 24.92 ? 529  ALA   A CA    1 
ATOM   3867  C  C     . ALA   A  1  531  ? -37.069 43.768  100.675 1.00 26.87 ? 529  ALA   A C     1 
ATOM   3868  O  O     . ALA   A  1  531  ? -36.920 43.396  99.508  1.00 26.43 ? 529  ALA   A O     1 
ATOM   3869  C  CB    . ALA   A  1  531  ? -36.952 41.858  102.275 1.00 28.16 ? 529  ALA   A CB    1 
ATOM   3870  N  N     . LYS   A  1  532  ? -36.555 44.902  101.154 1.00 23.42 ? 530  LYS   A N     1 
ATOM   3871  C  CA    . LYS   A  1  532  ? -35.690 45.764  100.358 1.00 26.87 ? 530  LYS   A CA    1 
ATOM   3872  C  C     . LYS   A  1  532  ? -34.499 44.967  99.840  1.00 26.64 ? 530  LYS   A C     1 
ATOM   3873  O  O     . LYS   A  1  532  ? -34.077 43.973  100.441 1.00 24.87 ? 530  LYS   A O     1 
ATOM   3874  C  CB    . LYS   A  1  532  ? -35.177 46.919  101.231 1.00 28.17 ? 530  LYS   A CB    1 
ATOM   3875  C  CG    . LYS   A  1  532  ? -34.178 47.870  100.556 1.00 32.36 ? 530  LYS   A CG    1 
ATOM   3876  C  CD    . LYS   A  1  532  ? -33.683 48.955  101.504 1.00 27.11 ? 530  LYS   A CD    1 
ATOM   3877  C  CE    . LYS   A  1  532  ? -32.899 48.371  102.669 1.00 29.72 ? 530  LYS   A CE    1 
ATOM   3878  N  NZ    . LYS   A  1  532  ? -31.616 47.757  102.222 1.00 28.93 ? 530  LYS   A NZ    1 
ATOM   3879  N  N     . HIS   A  1  533  ? -33.966 45.401  98.703  1.00 23.49 ? 531  HIS   A N     1 
ATOM   3880  C  CA    . HIS   A  1  533  ? -32.734 44.817  98.201  1.00 23.20 ? 531  HIS   A CA    1 
ATOM   3881  C  C     . HIS   A  1  533  ? -31.630 44.954  99.242  1.00 26.70 ? 531  HIS   A C     1 
ATOM   3882  O  O     . HIS   A  1  533  ? -31.436 46.022  99.827  1.00 26.15 ? 531  HIS   A O     1 
ATOM   3883  C  CB    . HIS   A  1  533  ? -32.312 45.522  96.919  1.00 24.73 ? 531  HIS   A CB    1 
ATOM   3884  C  CG    . HIS   A  1  533  ? -31.333 44.739  96.110  1.00 24.89 ? 531  HIS   A CG    1 
ATOM   3885  N  ND1   . HIS   A  1  533  ? -30.041 44.501  96.532  1.00 27.49 ? 531  HIS   A ND1   1 
ATOM   3886  C  CD2   . HIS   A  1  533  ? -31.461 44.115  94.916  1.00 31.24 ? 531  HIS   A CD2   1 
ATOM   3887  C  CE1   . HIS   A  1  533  ? -29.411 43.778  95.624  1.00 33.48 ? 531  HIS   A CE1   1 
ATOM   3888  N  NE2   . HIS   A  1  533  ? -30.250 43.526  94.635  1.00 34.71 ? 531  HIS   A NE2   1 
ATOM   3889  N  N     . ASP   A  1  534  ? -30.900 43.856  99.467  1.00 27.18 ? 532  ASP   A N     1 
ATOM   3890  C  CA    . ASP   A  1  534  ? -29.840 43.852  100.471 1.00 28.82 ? 532  ASP   A CA    1 
ATOM   3891  C  C     . ASP   A  1  534  ? -28.734 44.846  100.152 1.00 28.08 ? 532  ASP   A C     1 
ATOM   3892  O  O     . ASP   A  1  534  ? -28.072 45.350  101.066 1.00 31.82 ? 532  ASP   A O     1 
ATOM   3893  C  CB    . ASP   A  1  534  ? -29.228 42.456  100.576 1.00 31.90 ? 532  ASP   A CB    1 
ATOM   3894  C  CG    . ASP   A  1  534  ? -30.116 41.485  101.314 1.00 43.33 ? 532  ASP   A CG    1 
ATOM   3895  O  OD1   . ASP   A  1  534  ? -31.160 41.920  101.842 1.00 47.69 ? 532  ASP   A OD1   1 
ATOM   3896  O  OD2   . ASP   A  1  534  ? -29.766 40.285  101.369 1.00 53.29 ? 532  ASP   A OD2   1 
ATOM   3897  N  N     . ARG   A  1  535  ? -28.506 45.137  98.876  1.00 23.89 ? 533  ARG   A N     1 
ATOM   3898  C  CA    . ARG   A  1  535  ? -27.353 45.927  98.474  1.00 24.18 ? 533  ARG   A CA    1 
ATOM   3899  C  C     . ARG   A  1  535  ? -27.700 47.377  98.172  1.00 23.46 ? 533  ARG   A C     1 
ATOM   3900  O  O     . ARG   A  1  535  ? -26.862 48.104  97.628  1.00 28.45 ? 533  ARG   A O     1 
ATOM   3901  C  CB    . ARG   A  1  535  ? -26.647 45.283  97.278  1.00 30.64 ? 533  ARG   A CB    1 
ATOM   3902  N  N     . ILE   A  1  536  ? -28.904 47.821  98.518  1.00 23.20 ? 534  ILE   A N     1 
ATOM   3903  C  CA    . ILE   A  1  536  ? -29.303 49.204  98.316  1.00 23.54 ? 534  ILE   A CA    1 
ATOM   3904  C  C     . ILE   A  1  536  ? -29.623 49.797  99.675  1.00 24.71 ? 534  ILE   A C     1 
ATOM   3905  O  O     . ILE   A  1  536  ? -30.534 49.327  100.367 1.00 26.46 ? 534  ILE   A O     1 
ATOM   3906  C  CB    . ILE   A  1  536  ? -30.498 49.320  97.364  1.00 22.05 ? 534  ILE   A CB    1 
ATOM   3907  C  CG1   . ILE   A  1  536  ? -30.104 48.761  96.000  1.00 25.42 ? 534  ILE   A CG1   1 
ATOM   3908  C  CG2   . ILE   A  1  536  ? -30.961 50.775  97.277  1.00 22.80 ? 534  ILE   A CG2   1 
ATOM   3909  C  CD1   . ILE   A  1  536  ? -31.217 48.817  95.009  1.00 27.32 ? 534  ILE   A CD1   1 
ATOM   3910  N  N     . ALA   A  1  537  ? -28.882 50.826  100.049 1.00 21.96 ? 535  ALA   A N     1 
ATOM   3911  C  CA    . ALA   A  1  537  ? -29.059 51.452  101.344 1.00 21.91 ? 535  ALA   A CA    1 
ATOM   3912  C  C     . ALA   A  1  537  ? -30.260 52.386  101.308 1.00 20.29 ? 535  ALA   A C     1 
ATOM   3913  O  O     . ALA   A  1  537  ? -30.419 53.174  100.374 1.00 20.07 ? 535  ALA   A O     1 
ATOM   3914  C  CB    . ALA   A  1  537  ? -27.800 52.239  101.697 1.00 23.51 ? 535  ALA   A CB    1 
ATOM   3915  N  N     . LEU   A  1  538  ? -31.101 52.307  102.333 1.00 20.87 ? 536  LEU   A N     1 
ATOM   3916  C  CA    . LEU   A  1  538  ? -32.050 53.382  102.549 1.00 21.63 ? 536  LEU   A CA    1 
ATOM   3917  C  C     . LEU   A  1  538  ? -31.270 54.678  102.769 1.00 21.98 ? 536  LEU   A C     1 
ATOM   3918  O  O     . LEU   A  1  538  ? -30.125 54.656  103.238 1.00 21.23 ? 536  LEU   A O     1 
ATOM   3919  C  CB    . LEU   A  1  538  ? -32.921 53.088  103.771 1.00 22.05 ? 536  LEU   A CB    1 
ATOM   3920  C  CG    . LEU   A  1  538  ? -33.987 51.999  103.634 1.00 25.09 ? 536  LEU   A CG    1 
ATOM   3921  C  CD1   . LEU   A  1  538  ? -34.670 51.768  104.974 1.00 28.18 ? 536  LEU   A CD1   1 
ATOM   3922  C  CD2   . LEU   A  1  538  ? -35.007 52.367  102.571 1.00 25.45 ? 536  LEU   A CD2   1 
ATOM   3923  N  N     . PRO   A  1  539  ? -31.847 55.818  102.414 1.00 20.65 ? 537  PRO   A N     1 
ATOM   3924  C  CA    . PRO   A  1  539  ? -31.123 57.084  102.584 1.00 19.38 ? 537  PRO   A CA    1 
ATOM   3925  C  C     . PRO   A  1  539  ? -30.591 57.314  103.986 1.00 20.42 ? 537  PRO   A C     1 
ATOM   3926  O  O     . PRO   A  1  539  ? -29.466 57.804  104.134 1.00 21.51 ? 537  PRO   A O     1 
ATOM   3927  C  CB    . PRO   A  1  539  ? -32.161 58.126  102.154 1.00 19.58 ? 537  PRO   A CB    1 
ATOM   3928  C  CG    . PRO   A  1  539  ? -32.960 57.389  101.107 1.00 19.05 ? 537  PRO   A CG    1 
ATOM   3929  C  CD    . PRO   A  1  539  ? -33.092 55.992  101.645 1.00 18.94 ? 537  PRO   A CD    1 
ATOM   3930  N  N     . ALA   A  1  540  ? -31.344 56.930  105.018 1.00 20.41 ? 538  ALA   A N     1 
ATOM   3931  C  CA    . ALA   A  1  540  ? -30.875 57.112  106.387 1.00 21.99 ? 538  ALA   A CA    1 
ATOM   3932  C  C     . ALA   A  1  540  ? -29.636 56.285  106.685 1.00 24.79 ? 538  ALA   A C     1 
ATOM   3933  O  O     . ALA   A  1  540  ? -28.937 56.574  107.662 1.00 25.38 ? 538  ALA   A O     1 
ATOM   3934  C  CB    . ALA   A  1  540  ? -31.970 56.733  107.384 1.00 26.27 ? 538  ALA   A CB    1 
ATOM   3935  N  N     . GLU   A  1  541  ? -29.353 55.260  105.882 1.00 23.77 ? 539  GLU   A N     1 
ATOM   3936  C  CA    . GLU   A  1  541  ? -28.309 54.296  106.200 1.00 25.17 ? 539  GLU   A CA    1 
ATOM   3937  C  C     . GLU   A  1  541  ? -27.092 54.425  105.293 1.00 24.44 ? 539  GLU   A C     1 
ATOM   3938  O  O     . GLU   A  1  541  ? -26.255 53.519  105.253 1.00 24.35 ? 539  GLU   A O     1 
ATOM   3939  C  CB    . GLU   A  1  541  ? -28.876 52.875  106.193 1.00 27.58 ? 539  GLU   A CB    1 
ATOM   3940  C  CG    . GLU   A  1  541  ? -30.088 52.721  107.116 1.00 32.57 ? 539  GLU   A CG    1 
ATOM   3941  C  CD    . GLU   A  1  541  ? -30.636 51.306  107.161 1.00 39.27 ? 539  GLU   A CD    1 
ATOM   3942  O  OE1   . GLU   A  1  541  ? -29.830 50.353  107.150 1.00 51.56 ? 539  GLU   A OE1   1 
ATOM   3943  O  OE2   . GLU   A  1  541  ? -31.874 51.147  107.200 1.00 48.02 ? 539  GLU   A OE2   1 
ATOM   3944  N  N     . LEU   A  1  542  ? -26.964 55.553  104.583 1.00 22.33 ? 540  LEU   A N     1 
ATOM   3945  C  CA    . LEU   A  1  542  ? -25.865 55.722  103.637 1.00 24.35 ? 540  LEU   A CA    1 
ATOM   3946  C  C     . LEU   A  1  542  ? -24.512 55.523  104.291 1.00 24.46 ? 540  LEU   A C     1 
ATOM   3947  O  O     . LEU   A  1  542  ? -23.563 55.079  103.637 1.00 24.72 ? 540  LEU   A O     1 
ATOM   3948  C  CB    . LEU   A  1  542  ? -25.894 57.126  103.047 1.00 26.79 ? 540  LEU   A CB    1 
ATOM   3949  C  CG    . LEU   A  1  542  ? -26.799 57.409  101.859 1.00 25.74 ? 540  LEU   A CG    1 
ATOM   3950  C  CD1   . LEU   A  1  542  ? -26.366 58.736  101.265 1.00 22.56 ? 540  LEU   A CD1   1 
ATOM   3951  C  CD2   . LEU   A  1  542  ? -26.725 56.284  100.836 1.00 27.41 ? 540  LEU   A CD2   1 
ATOM   3952  N  N     . PHE   A  1  543  ? -24.392 55.860  105.569 1.00 22.12 ? 541  PHE   A N     1 
ATOM   3953  C  CA    . PHE   A  1  543  ? -23.111 55.789  106.253 1.00 24.13 ? 541  PHE   A CA    1 
ATOM   3954  C  C     . PHE   A  1  543  ? -23.017 54.590  107.179 1.00 22.20 ? 541  PHE   A C     1 
ATOM   3955  O  O     . PHE   A  1  543  ? -22.034 54.465  107.914 1.00 24.46 ? 541  PHE   A O     1 
ATOM   3956  C  CB    . PHE   A  1  543  ? -22.824 57.098  106.986 1.00 22.80 ? 541  PHE   A CB    1 
ATOM   3957  C  CG    . PHE   A  1  543  ? -23.053 58.302  106.134 1.00 22.22 ? 541  PHE   A CG    1 
ATOM   3958  C  CD1   . PHE   A  1  543  ? -22.361 58.455  104.947 1.00 25.05 ? 541  PHE   A CD1   1 
ATOM   3959  C  CD2   . PHE   A  1  543  ? -23.997 59.255  106.488 1.00 20.21 ? 541  PHE   A CD2   1 
ATOM   3960  C  CE1   . PHE   A  1  543  ? -22.577 59.545  104.141 1.00 24.52 ? 541  PHE   A CE1   1 
ATOM   3961  C  CE2   . PHE   A  1  543  ? -24.214 60.351  105.683 1.00 20.35 ? 541  PHE   A CE2   1 
ATOM   3962  C  CZ    . PHE   A  1  543  ? -23.514 60.495  104.508 1.00 22.63 ? 541  PHE   A CZ    1 
ATOM   3963  N  N     . GLY   A  1  544  ? -24.011 53.708  107.153 1.00 24.42 ? 542  GLY   A N     1 
ATOM   3964  C  CA    . GLY   A  1  544  ? -23.925 52.480  107.922 1.00 27.46 ? 542  GLY   A CA    1 
ATOM   3965  C  C     . GLY   A  1  544  ? -23.787 52.756  109.404 1.00 23.87 ? 542  GLY   A C     1 
ATOM   3966  O  O     . GLY   A  1  544  ? -24.485 53.605  109.972 1.00 26.21 ? 542  GLY   A O     1 
ATOM   3967  N  N     . ASP   A  1  545  ? -22.855 52.043  110.041 1.00 30.27 ? 543  ASP   A N     1 
ATOM   3968  C  CA    . ASP   A  1  545  ? -22.691 52.115  111.490 1.00 29.39 ? 543  ASP   A CA    1 
ATOM   3969  C  C     . ASP   A  1  545  ? -22.017 53.397  111.953 1.00 29.56 ? 543  ASP   A C     1 
ATOM   3970  O  O     . ASP   A  1  545  ? -22.015 53.667  113.158 1.00 33.55 ? 543  ASP   A O     1 
ATOM   3971  C  CB    . ASP   A  1  545  ? -21.868 50.924  111.992 1.00 35.35 ? 543  ASP   A CB    1 
ATOM   3972  C  CG    . ASP   A  1  545  ? -22.508 49.589  111.664 1.00 46.04 ? 543  ASP   A CG    1 
ATOM   3973  O  OD1   . ASP   A  1  545  ? -23.754 49.530  111.572 1.00 46.28 ? 543  ASP   A OD1   1 
ATOM   3974  O  OD2   . ASP   A  1  545  ? -21.764 48.598  111.500 1.00 56.01 ? 543  ASP   A OD2   1 
ATOM   3975  N  N     . ALA   A  1  546  ? -21.441 54.180  111.042 1.00 25.47 ? 544  ALA   A N     1 
ATOM   3976  C  CA    . ALA   A  1  546  ? -20.692 55.364  111.453 1.00 28.40 ? 544  ALA   A CA    1 
ATOM   3977  C  C     . ALA   A  1  546  ? -21.616 56.416  112.048 1.00 26.64 ? 544  ALA   A C     1 
ATOM   3978  O  O     . ALA   A  1  546  ? -21.321 56.997  113.097 1.00 28.01 ? 544  ALA   A O     1 
ATOM   3979  C  CB    . ALA   A  1  546  ? -19.924 55.939  110.268 1.00 26.18 ? 544  ALA   A CB    1 
ATOM   3980  N  N     . ARG   A  1  547  ? -22.742 56.672  111.391 1.00 23.74 ? 545  ARG   A N     1 
ATOM   3981  C  CA    . ARG   A  1  547  ? -23.689 57.661  111.881 1.00 24.93 ? 545  ARG   A CA    1 
ATOM   3982  C  C     . ARG   A  1  547  ? -24.936 57.573  111.026 1.00 19.89 ? 545  ARG   A C     1 
ATOM   3983  O  O     . ARG   A  1  547  ? -24.936 56.985  109.944 1.00 22.79 ? 545  ARG   A O     1 
ATOM   3984  C  CB    . ARG   A  1  547  ? -23.133 59.083  111.830 1.00 26.96 ? 545  ARG   A CB    1 
ATOM   3985  C  CG    . ARG   A  1  547  ? -22.800 59.536  110.455 1.00 27.50 ? 545  ARG   A CG    1 
ATOM   3986  C  CD    . ARG   A  1  547  ? -22.143 60.898  110.474 1.00 27.69 ? 545  ARG   A CD    1 
ATOM   3987  N  NE    . ARG   A  1  547  ? -21.361 61.077  109.260 1.00 24.20 ? 545  ARG   A NE    1 
ATOM   3988  C  CZ    . ARG   A  1  547  ? -21.771 61.734  108.181 1.00 24.13 ? 545  ARG   A CZ    1 
ATOM   3989  N  NH1   . ARG   A  1  547  ? -22.931 62.370  108.152 1.00 23.71 ? 545  ARG   A NH1   1 
ATOM   3990  N  NH2   . ARG   A  1  547  ? -20.990 61.764  107.108 1.00 23.78 ? 545  ARG   A NH2   1 
ATOM   3991  N  N     . THR   A  1  548  ? -25.999 58.172  111.539 1.00 21.16 ? 546  THR   A N     1 
ATOM   3992  C  CA    . THR   A  1  548  ? -27.275 58.219  110.849 1.00 20.85 ? 546  THR   A CA    1 
ATOM   3993  C  C     . THR   A  1  548  ? -27.290 59.433  109.936 1.00 20.58 ? 546  THR   A C     1 
ATOM   3994  O  O     . THR   A  1  548  ? -27.013 60.554  110.374 1.00 20.41 ? 546  THR   A O     1 
ATOM   3995  C  CB    . THR   A  1  548  ? -28.384 58.346  111.890 1.00 24.63 ? 546  THR   A CB    1 
ATOM   3996  O  OG1   . THR   A  1  548  ? -28.273 57.266  112.820 1.00 28.95 ? 546  THR   A OG1   1 
ATOM   3997  C  CG2   . THR   A  1  548  ? -29.739 58.295  111.232 1.00 25.94 ? 546  THR   A CG2   1 
ATOM   3998  N  N     . ASN   A  1  549  ? -27.616 59.211  108.666 1.00 19.36 ? 547  ASN   A N     1 
ATOM   3999  C  CA    . ASN   A  1  549  ? -27.746 60.323  107.741 1.00 19.59 ? 547  ASN   A CA    1 
ATOM   4000  C  C     . ASN   A  1  549  ? -28.882 61.227  108.196 1.00 20.86 ? 547  ASN   A C     1 
ATOM   4001  O  O     . ASN   A  1  549  ? -29.891 60.760  108.723 1.00 21.03 ? 547  ASN   A O     1 
ATOM   4002  C  CB    . ASN   A  1  549  ? -28.056 59.772  106.348 1.00 17.97 ? 547  ASN   A CB    1 
ATOM   4003  C  CG    . ASN   A  1  549  ? -27.868 60.799  105.255 1.00 19.30 ? 547  ASN   A CG    1 
ATOM   4004  O  OD1   . ASN   A  1  549  ? -27.330 61.881  105.484 1.00 19.53 ? 547  ASN   A OD1   1 
ATOM   4005  N  ND2   . ASN   A  1  549  ? -28.289 60.456  104.051 1.00 19.72 ? 547  ASN   A ND2   1 
ATOM   4006  N  N     . SER   A  1  550  ? -28.716 62.531  108.004 1.00 19.65 ? 548  SER   A N     1 
ATOM   4007  C  CA    . SER   A  1  550  ? -29.835 63.433  108.232 1.00 19.85 ? 548  SER   A CA    1 
ATOM   4008  C  C     . SER   A  1  550  ? -30.934 63.131  107.226 1.00 19.98 ? 548  SER   A C     1 
ATOM   4009  O  O     . SER   A  1  550  ? -30.684 62.620  106.131 1.00 21.11 ? 548  SER   A O     1 
ATOM   4010  C  CB    . SER   A  1  550  ? -29.386 64.875  108.055 1.00 19.00 ? 548  SER   A CB    1 
ATOM   4011  O  OG    . SER   A  1  550  ? -28.872 65.078  106.748 1.00 19.27 ? 548  SER   A OG    1 
ATOM   4012  N  N     . ALA   A  1  551  ? -32.166 63.442  107.614 1.00 22.26 ? 549  ALA   A N     1 
ATOM   4013  C  CA    . ALA   A  1  551  ? -33.336 63.229  106.777 1.00 23.33 ? 549  ALA   A CA    1 
ATOM   4014  C  C     . ALA   A  1  551  ? -33.822 64.560  106.223 1.00 20.05 ? 549  ALA   A C     1 
ATOM   4015  O  O     . ALA   A  1  551  ? -33.839 65.571  106.928 1.00 20.75 ? 549  ALA   A O     1 
ATOM   4016  C  CB    . ALA   A  1  551  ? -34.459 62.575  107.585 1.00 24.51 ? 549  ALA   A CB    1 
ATOM   4017  N  N     . GLY   A  1  552  ? -34.229 64.551  104.959 1.00 19.41 ? 550  GLY   A N     1 
ATOM   4018  C  CA    . GLY   A  1  552  ? -34.829 65.703  104.343 1.00 19.78 ? 550  GLY   A CA    1 
ATOM   4019  C  C     . GLY   A  1  552  ? -36.339 65.606  104.330 1.00 20.56 ? 550  GLY   A C     1 
ATOM   4020  O  O     . GLY   A  1  552  ? -36.951 64.865  105.104 1.00 22.14 ? 550  GLY   A O     1 
ATOM   4021  N  N     . LEU   A  1  553  ? -36.944 66.366  103.425 1.00 20.87 ? 551  LEU   A N     1 
ATOM   4022  C  CA    . LEU   A  1  553  ? -38.390 66.431  103.305 1.00 19.31 ? 551  LEU   A CA    1 
ATOM   4023  C  C     . LEU   A  1  553  ? -38.702 66.424  101.822 1.00 21.11 ? 551  LEU   A C     1 
ATOM   4024  O  O     . LEU   A  1  553  ? -37.963 67.006  101.029 1.00 22.50 ? 551  LEU   A O     1 
ATOM   4025  C  CB    . LEU   A  1  553  ? -38.922 67.713  103.937 1.00 22.61 ? 551  LEU   A CB    1 
ATOM   4026  C  CG    . LEU   A  1  553  ? -38.831 67.776  105.463 1.00 24.02 ? 551  LEU   A CG    1 
ATOM   4027  C  CD1   . LEU   A  1  553  ? -39.263 69.146  105.956 1.00 28.37 ? 551  LEU   A CD1   1 
ATOM   4028  C  CD2   . LEU   A  1  553  ? -39.671 66.678  106.124 1.00 24.63 ? 551  LEU   A CD2   1 
ATOM   4029  N  N     . ASP   A  1  554  ? -39.785 65.756  101.450 1.00 19.76 ? 552  ASP   A N     1 
ATOM   4030  C  CA    . ASP   A  1  554  ? -40.127 65.595  100.040 1.00 22.21 ? 552  ASP   A CA    1 
ATOM   4031  C  C     . ASP   A  1  554  ? -41.090 66.709  99.664  1.00 20.16 ? 552  ASP   A C     1 
ATOM   4032  O  O     . ASP   A  1  554  ? -42.286 66.639  99.969  1.00 19.35 ? 552  ASP   A O     1 
ATOM   4033  C  CB    . ASP   A  1  554  ? -40.756 64.230  99.805  1.00 21.48 ? 552  ASP   A CB    1 
ATOM   4034  C  CG    . ASP   A  1  554  ? -41.071 63.988  98.354  1.00 18.89 ? 552  ASP   A CG    1 
ATOM   4035  O  OD1   . ASP   A  1  554  ? -40.838 64.896  97.523  1.00 20.87 ? 552  ASP   A OD1   1 
ATOM   4036  O  OD2   . ASP   A  1  554  ? -41.546 62.885  98.035  1.00 23.87 ? 552  ASP   A OD2   1 
ATOM   4037  N  N     . LEU   A  1  555  ? -40.578 67.736  98.990  1.00 18.45 ? 553  LEU   A N     1 
ATOM   4038  C  CA    . LEU   A  1  555  ? -41.421 68.864  98.619  1.00 20.65 ? 553  LEU   A CA    1 
ATOM   4039  C  C     . LEU   A  1  555  ? -42.308 68.576  97.421  1.00 19.12 ? 553  LEU   A C     1 
ATOM   4040  O  O     . LEU   A  1  555  ? -42.990 69.489  96.940  1.00 21.11 ? 553  LEU   A O     1 
ATOM   4041  C  CB    . LEU   A  1  555  ? -40.595 70.132  98.416  1.00 20.37 ? 553  LEU   A CB    1 
ATOM   4042  C  CG    . LEU   A  1  555  ? -39.771 70.520  99.645  1.00 22.60 ? 553  LEU   A CG    1 
ATOM   4043  C  CD1   . LEU   A  1  555  ? -39.062 71.836  99.402  1.00 24.40 ? 553  LEU   A CD1   1 
ATOM   4044  C  CD2   . LEU   A  1  555  ? -40.668 70.594  100.880 1.00 25.07 ? 553  LEU   A CD2   1 
ATOM   4045  N  N     . SER   A  1  556  ? -42.314 67.340  96.935  1.00 17.90 ? 554  SER   A N     1 
ATOM   4046  C  CA    . SER   A  1  556  ? -43.309 66.911  95.961  1.00 18.17 ? 554  SER   A CA    1 
ATOM   4047  C  C     . SER   A  1  556  ? -44.452 66.139  96.596  1.00 20.66 ? 554  SER   A C     1 
ATOM   4048  O  O     . SER   A  1  556  ? -45.380 65.744  95.888  1.00 20.49 ? 554  SER   A O     1 
ATOM   4049  C  CB    . SER   A  1  556  ? -42.675 66.045  94.868  1.00 20.28 ? 554  SER   A CB    1 
ATOM   4050  O  OG    . SER   A  1  556  ? -42.372 64.746  95.366  1.00 22.49 ? 554  SER   A OG    1 
ATOM   4051  N  N     . ASN   A  1  557  ? -44.411 65.911  97.902  1.00 18.98 ? 555  ASN   A N     1 
ATOM   4052  C  CA    . ASN   A  1  557  ? -45.422 65.129  98.595  1.00 18.82 ? 555  ASN   A CA    1 
ATOM   4053  C  C     . ASN   A  1  557  ? -46.452 66.094  99.169  1.00 20.03 ? 555  ASN   A C     1 
ATOM   4054  O  O     . ASN   A  1  557  ? -46.102 66.961  99.976  1.00 19.26 ? 555  ASN   A O     1 
ATOM   4055  C  CB    . ASN   A  1  557  ? -44.726 64.336  99.703  1.00 20.16 ? 555  ASN   A CB    1 
ATOM   4056  C  CG    . ASN   A  1  557  ? -45.677 63.454  100.483 1.00 18.78 ? 555  ASN   A CG    1 
ATOM   4057  O  OD1   . ASN   A  1  557  ? -46.690 63.913  100.988 1.00 22.37 ? 555  ASN   A OD1   1 
ATOM   4058  N  ND2   . ASN   A  1  557  ? -45.356 62.169  100.567 1.00 20.45 ? 555  ASN   A ND2   1 
ATOM   4059  N  N     . GLU   A  1  558  ? -47.725 65.941  98.759  1.00 19.63 ? 556  GLU   A N     1 
ATOM   4060  C  CA    . GLU   A  1  558  ? -48.761 66.870  99.211  1.00 20.93 ? 556  GLU   A CA    1 
ATOM   4061  C  C     . GLU   A  1  558  ? -48.968 66.812  100.714 1.00 21.06 ? 556  GLU   A C     1 
ATOM   4062  O  O     . GLU   A  1  558  ? -49.289 67.833  101.333 1.00 22.06 ? 556  GLU   A O     1 
ATOM   4063  C  CB    . GLU   A  1  558  ? -50.098 66.613  98.518  1.00 21.82 ? 556  GLU   A CB    1 
ATOM   4064  C  CG    . GLU   A  1  558  ? -50.110 66.931  97.050  1.00 22.24 ? 556  GLU   A CG    1 
ATOM   4065  C  CD    . GLU   A  1  558  ? -49.832 68.392  96.689  1.00 22.37 ? 556  GLU   A CD    1 
ATOM   4066  O  OE1   . GLU   A  1  558  ? -49.864 69.307  97.532  1.00 20.19 ? 556  GLU   A OE1   1 
ATOM   4067  O  OE2   . GLU   A  1  558  ? -49.585 68.625  95.496  1.00 20.94 ? 556  GLU   A OE2   1 
ATOM   4068  N  N     . GLU   A  1  559  ? -48.834 65.626  101.316 1.00 19.45 ? 557  GLU   A N     1 
ATOM   4069  C  CA    . GLU   A  1  559  ? -48.937 65.544  102.770 1.00 21.31 ? 557  GLU   A CA    1 
ATOM   4070  C  C     . GLU   A  1  559  ? -47.822 66.344  103.420 1.00 21.46 ? 557  GLU   A C     1 
ATOM   4071  O  O     . GLU   A  1  559  ? -48.054 67.103  104.368 1.00 21.91 ? 557  GLU   A O     1 
ATOM   4072  C  CB    . GLU   A  1  559  ? -48.863 64.092  103.246 1.00 23.96 ? 557  GLU   A CB    1 
ATOM   4073  C  CG    . GLU   A  1  559  ? -50.004 63.190  102.831 1.00 26.96 ? 557  GLU   A CG    1 
ATOM   4074  C  CD    . GLU   A  1  559  ? -49.753 61.740  103.224 1.00 32.75 ? 557  GLU   A CD    1 
ATOM   4075  O  OE1   . GLU   A  1  559  ? -48.760 61.480  103.940 1.00 42.56 ? 557  GLU   A OE1   1 
ATOM   4076  O  OE2   . GLU   A  1  559  ? -50.533 60.855  102.813 1.00 38.64 ? 557  GLU   A OE2   1 
ATOM   4077  N  N     . THR   A  1  560  ? -46.597 66.181  102.917 1.00 21.10 ? 558  THR   A N     1 
ATOM   4078  C  CA    . THR   A  1  560  ? -45.482 66.952  103.447 1.00 21.72 ? 558  THR   A CA    1 
ATOM   4079  C  C     . THR   A  1  560  ? -45.709 68.438  103.245 1.00 20.91 ? 558  THR   A C     1 
ATOM   4080  O  O     . THR   A  1  560  ? -45.477 69.238  104.155 1.00 21.23 ? 558  THR   A O     1 
ATOM   4081  C  CB    . THR   A  1  560  ? -44.189 66.519  102.764 1.00 20.25 ? 558  THR   A CB    1 
ATOM   4082  O  OG1   . THR   A  1  560  ? -44.017 65.112  102.962 1.00 22.66 ? 558  THR   A OG1   1 
ATOM   4083  C  CG2   . THR   A  1  560  ? -42.996 67.275  103.345 1.00 23.65 ? 558  THR   A CG2   1 
ATOM   4084  N  N     . LEU   A  1  561  ? -46.191 68.828  102.066 1.00 20.22 ? 559  LEU   A N     1 
ATOM   4085  C  CA    . LEU   A  1  561  ? -46.399 70.247  101.819 1.00 19.24 ? 559  LEU   A CA    1 
ATOM   4086  C  C     . LEU   A  1  561  ? -47.481 70.805  102.724 1.00 21.32 ? 559  LEU   A C     1 
ATOM   4087  O  O     . LEU   A  1  561  ? -47.369 71.939  103.203 1.00 22.04 ? 559  LEU   A O     1 
ATOM   4088  C  CB    . LEU   A  1  561  ? -46.759 70.484  100.355 1.00 18.10 ? 559  LEU   A CB    1 
ATOM   4089  C  CG    . LEU   A  1  561  ? -45.607 70.250  99.392  1.00 17.69 ? 559  LEU   A CG    1 
ATOM   4090  C  CD1   . LEU   A  1  561  ? -46.118 70.405  97.981  1.00 19.37 ? 559  LEU   A CD1   1 
ATOM   4091  C  CD2   . LEU   A  1  561  ? -44.460 71.227  99.688  1.00 19.58 ? 559  LEU   A CD2   1 
ATOM   4092  N  N     . ALA   A  1  562  ? -48.544 70.030  102.961 1.00 20.57 ? 560  ALA   A N     1 
ATOM   4093  C  CA    . ALA   A  1  562  ? -49.621 70.525  103.812 1.00 22.41 ? 560  ALA   A CA    1 
ATOM   4094  C  C     . ALA   A  1  562  ? -49.149 70.659  105.249 1.00 23.28 ? 560  ALA   A C     1 
ATOM   4095  O  O     . ALA   A  1  562  ? -49.434 71.662  105.915 1.00 22.72 ? 560  ALA   A O     1 
ATOM   4096  C  CB    . ALA   A  1  562  ? -50.832 69.594  103.730 1.00 24.26 ? 560  ALA   A CB    1 
ATOM   4097  N  N     . SER   A  1  563  ? -48.420 69.661  105.743 1.00 22.69 ? 561  SER   A N     1 
ATOM   4098  C  CA    A SER   A  1  563  ? -47.905 69.730  107.105 0.44 24.55 ? 561  SER   A CA    1 
ATOM   4099  C  CA    B SER   A  1  563  ? -47.928 69.751  107.111 0.56 24.54 ? 561  SER   A CA    1 
ATOM   4100  C  C     . SER   A  1  563  ? -46.859 70.827  107.234 1.00 23.35 ? 561  SER   A C     1 
ATOM   4101  O  O     . SER   A  1  563  ? -46.838 71.568  108.221 1.00 25.00 ? 561  SER   A O     1 
ATOM   4102  C  CB    A SER   A  1  563  ? -47.315 68.374  107.491 0.44 26.83 ? 561  SER   A CB    1 
ATOM   4103  C  CB    B SER   A  1  563  ? -47.415 68.394  107.593 0.56 26.90 ? 561  SER   A CB    1 
ATOM   4104  O  OG    A SER   A  1  563  ? -46.585 68.462  108.696 0.44 26.51 ? 561  SER   A OG    1 
ATOM   4105  O  OG    B SER   A  1  563  ? -46.246 68.016  106.900 0.56 28.91 ? 561  SER   A OG    1 
ATOM   4106  N  N     . LEU   A  1  564  ? -45.988 70.949  106.232 1.00 23.70 ? 562  LEU   A N     1 
ATOM   4107  C  CA    . LEU   A  1  564  ? -44.969 71.988  106.267 1.00 22.98 ? 562  LEU   A CA    1 
ATOM   4108  C  C     . LEU   A  1  564  ? -45.597 73.373  106.239 1.00 21.95 ? 562  LEU   A C     1 
ATOM   4109  O  O     . LEU   A  1  564  ? -45.174 74.266  106.980 1.00 23.71 ? 562  LEU   A O     1 
ATOM   4110  C  CB    . LEU   A  1  564  ? -44.026 71.809  105.082 1.00 22.21 ? 562  LEU   A CB    1 
ATOM   4111  C  CG    . LEU   A  1  564  ? -42.682 72.516  105.136 1.00 28.14 ? 562  LEU   A CG    1 
ATOM   4112  C  CD1   . LEU   A  1  564  ? -41.963 72.159  106.420 1.00 27.81 ? 562  LEU   A CD1   1 
ATOM   4113  C  CD2   . LEU   A  1  564  ? -41.858 72.103  103.932 1.00 23.00 ? 562  LEU   A CD2   1 
ATOM   4114  N  N     . THR   A  1  565  ? -46.612 73.574  105.393 1.00 22.97 ? 563  THR   A N     1 
ATOM   4115  C  CA    . THR   A  1  565  ? -47.298 74.860  105.368 1.00 23.03 ? 563  THR   A CA    1 
ATOM   4116  C  C     . THR   A  1  565  ? -47.713 75.278  106.770 1.00 22.18 ? 563  THR   A C     1 
ATOM   4117  O  O     . THR   A  1  565  ? -47.467 76.412  107.194 1.00 24.37 ? 563  THR   A O     1 
ATOM   4118  C  CB    . THR   A  1  565  ? -48.528 74.788  104.466 1.00 22.94 ? 563  THR   A CB    1 
ATOM   4119  O  OG1   . THR   A  1  565  ? -48.121 74.522  103.118 1.00 22.81 ? 563  THR   A OG1   1 
ATOM   4120  C  CG2   . THR   A  1  565  ? -49.280 76.110  104.518 1.00 25.97 ? 563  THR   A CG2   1 
ATOM   4121  N  N     . GLU   A  1  566  ? -48.327 74.359  107.514 1.00 23.70 ? 564  GLU   A N     1 
ATOM   4122  C  CA    . GLU   A  1  566  ? -48.789 74.703  108.852 1.00 25.95 ? 564  GLU   A CA    1 
ATOM   4123  C  C     . GLU   A  1  566  ? -47.624 74.974  109.791 1.00 23.39 ? 564  GLU   A C     1 
ATOM   4124  O  O     . GLU   A  1  566  ? -47.651 75.944  110.559 1.00 25.39 ? 564  GLU   A O     1 
ATOM   4125  C  CB    . GLU   A  1  566  ? -49.696 73.602  109.395 1.00 26.39 ? 564  GLU   A CB    1 
ATOM   4126  C  CG    . GLU   A  1  566  ? -50.989 73.454  108.597 1.00 35.08 ? 564  GLU   A CG    1 
ATOM   4127  C  CD    . GLU   A  1  566  ? -51.662 74.793  108.306 1.00 39.20 ? 564  GLU   A CD    1 
ATOM   4128  O  OE1   . GLU   A  1  566  ? -51.898 75.568  109.259 1.00 41.76 ? 564  GLU   A OE1   1 
ATOM   4129  O  OE2   . GLU   A  1  566  ? -51.945 75.074  107.117 1.00 37.70 ? 564  GLU   A OE2   1 
ATOM   4130  N  N     . ALA   A  1  567  ? -46.591 74.135  109.739 1.00 23.29 ? 565  ALA   A N     1 
ATOM   4131  C  CA    . ALA   A  1  567  ? -45.448 74.343  110.620 1.00 23.57 ? 565  ALA   A CA    1 
ATOM   4132  C  C     . ALA   A  1  567  ? -44.729 75.643  110.283 1.00 22.33 ? 565  ALA   A C     1 
ATOM   4133  O  O     . ALA   A  1  567  ? -44.256 76.349  111.182 1.00 25.02 ? 565  ALA   A O     1 
ATOM   4134  C  CB    . ALA   A  1  567  ? -44.493 73.157  110.525 1.00 25.81 ? 565  ALA   A CB    1 
ATOM   4135  N  N     . LEU   A  1  568  ? -44.648 75.978  108.993 1.00 22.88 ? 566  LEU   A N     1 
ATOM   4136  C  CA    . LEU   A  1  568  ? -44.001 77.221  108.592 1.00 21.24 ? 566  LEU   A CA    1 
ATOM   4137  C  C     . LEU   A  1  568  ? -44.794 78.426  109.064 1.00 23.86 ? 566  LEU   A C     1 
ATOM   4138  O  O     . LEU   A  1  568  ? -44.228 79.371  109.624 1.00 24.06 ? 566  LEU   A O     1 
ATOM   4139  C  CB    . LEU   A  1  568  ? -43.828 77.264  107.075 1.00 20.61 ? 566  LEU   A CB    1 
ATOM   4140  C  CG    . LEU   A  1  568  ? -42.877 76.214  106.507 1.00 20.83 ? 566  LEU   A CG    1 
ATOM   4141  C  CD1   . LEU   A  1  568  ? -42.977 76.202  104.988 1.00 21.27 ? 566  LEU   A CD1   1 
ATOM   4142  C  CD2   . LEU   A  1  568  ? -41.427 76.431  106.949 1.00 23.14 ? 566  LEU   A CD2   1 
ATOM   4143  N  N     . ARG   A  1  569  ? -46.114 78.411  108.854 1.00 23.14 ? 567  ARG   A N     1 
ATOM   4144  C  CA    . ARG   A  1  569  ? -46.946 79.484  109.386 1.00 24.93 ? 567  ARG   A CA    1 
ATOM   4145  C  C     . ARG   A  1  569  ? -46.785 79.594  110.892 1.00 25.78 ? 567  ARG   A C     1 
ATOM   4146  O  O     . ARG   A  1  569  ? -46.642 80.700  111.430 1.00 26.73 ? 567  ARG   A O     1 
ATOM   4147  C  CB    . ARG   A  1  569  ? -48.411 79.246  109.026 1.00 25.88 ? 567  ARG   A CB    1 
ATOM   4148  C  CG    . ARG   A  1  569  ? -48.714 79.419  107.553 1.00 29.39 ? 567  ARG   A CG    1 
ATOM   4149  C  CD    . ARG   A  1  569  ? -50.175 79.112  107.262 1.00 31.87 ? 567  ARG   A CD    1 
ATOM   4150  N  NE    . ARG   A  1  569  ? -50.446 79.050  105.830 1.00 34.22 ? 567  ARG   A NE    1 
ATOM   4151  C  CZ    . ARG   A  1  569  ? -51.612 78.687  105.311 1.00 42.46 ? 567  ARG   A CZ    1 
ATOM   4152  N  NH1   . ARG   A  1  569  ? -52.629 78.330  106.079 1.00 45.62 ? 567  ARG   A NH1   1 
ATOM   4153  N  NH2   . ARG   A  1  569  ? -51.763 78.683  103.989 1.00 42.29 ? 567  ARG   A NH2   1 
ATOM   4154  N  N     . GLU   A  1  570  ? -46.781 78.455  111.590 1.00 25.90 ? 568  GLU   A N     1 
ATOM   4155  C  CA    . GLU   A  1  570  ? -46.626 78.494  113.040 1.00 26.01 ? 568  GLU   A CA    1 
ATOM   4156  C  C     . GLU   A  1  570  ? -45.282 79.087  113.421 1.00 30.53 ? 568  GLU   A C     1 
ATOM   4157  O  O     . GLU   A  1  570  ? -45.177 79.831  114.405 1.00 29.03 ? 568  GLU   A O     1 
ATOM   4158  C  CB    . GLU   A  1  570  ? -46.807 77.094  113.630 1.00 28.58 ? 568  GLU   A CB    1 
ATOM   4159  C  CG    . GLU   A  1  570  ? -48.256 76.613  113.584 1.00 33.33 ? 568  GLU   A CG    1 
ATOM   4160  C  CD    . GLU   A  1  570  ? -48.418 75.150  113.956 1.00 41.87 ? 568  GLU   A CD    1 
ATOM   4161  O  OE1   . GLU   A  1  570  ? -47.410 74.410  113.933 1.00 45.62 ? 568  GLU   A OE1   1 
ATOM   4162  O  OE2   . GLU   A  1  570  ? -49.559 74.742  114.274 1.00 52.41 ? 568  GLU   A OE2   1 
ATOM   4163  N  N     . SER   A  1  571  ? -44.249 78.799  112.631 1.00 25.81 ? 569  SER   A N     1 
ATOM   4164  C  CA    . SER   A  1  571  ? -42.929 79.344  112.928 1.00 25.70 ? 569  SER   A CA    1 
ATOM   4165  C  C     . SER   A  1  571  ? -42.910 80.860  112.793 1.00 25.79 ? 569  SER   A C     1 
ATOM   4166  O  O     . SER   A  1  571  ? -42.180 81.535  113.521 1.00 27.75 ? 569  SER   A O     1 
ATOM   4167  C  CB    . SER   A  1  571  ? -41.886 78.722  112.006 1.00 24.97 ? 569  SER   A CB    1 
ATOM   4168  O  OG    . SER   A  1  571  ? -41.882 79.351  110.735 1.00 25.22 ? 569  SER   A OG    1 
ATOM   4169  N  N     . ALA   A  1  572  ? -43.712 81.416  111.886 1.00 27.28 ? 570  ALA   A N     1 
ATOM   4170  C  CA    . ALA   A  1  572  ? -43.747 82.864  111.732 1.00 28.27 ? 570  ALA   A CA    1 
ATOM   4171  C  C     . ALA   A  1  572  ? -44.529 83.558  112.835 1.00 31.82 ? 570  ALA   A C     1 
ATOM   4172  O  O     . ALA   A  1  572  ? -44.443 84.783  112.952 1.00 34.03 ? 570  ALA   A O     1 
ATOM   4173  C  CB    . ALA   A  1  572  ? -44.319 83.251  110.368 1.00 31.32 ? 570  ALA   A CB    1 
ATOM   4174  N  N     . ALA   A  1  573  ? -45.283 82.811  113.637 1.00 29.68 ? 571  ALA   A N     1 
ATOM   4175  C  CA    . ALA   A  1  573  ? -45.992 83.353  114.786 1.00 32.67 ? 571  ALA   A CA    1 
ATOM   4176  C  C     . ALA   A  1  573  ? -45.157 83.292  116.058 1.00 37.23 ? 571  ALA   A C     1 
ATOM   4177  O  O     . ALA   A  1  573  ? -45.662 83.606  117.139 1.00 39.15 ? 571  ALA   A O     1 
ATOM   4178  C  CB    . ALA   A  1  573  ? -47.323 82.617  114.984 1.00 32.42 ? 571  ALA   A CB    1 
ATOM   4179  N  N     . MET   A  1  574  ? -43.894 82.899  115.956 1.00 32.48 ? 572  MET   A N     1 
ATOM   4180  C  CA    . MET   A  1  574  ? -43.043 82.794  117.128 1.00 35.29 ? 572  MET   A CA    1 
ATOM   4181  C  C     . MET   A  1  574  ? -42.277 84.091  117.352 1.00 35.11 ? 572  MET   A C     1 
ATOM   4182  O  O     . MET   A  1  574  ? -41.928 84.804  116.406 1.00 33.14 ? 572  MET   A O     1 
ATOM   4183  C  CB    . MET   A  1  574  ? -42.090 81.606  117.001 1.00 35.87 ? 572  MET   A CB    1 
ATOM   4184  C  CG    . MET   A  1  574  ? -42.813 80.262  117.046 1.00 35.80 ? 572  MET   A CG    1 
ATOM   4185  S  SD    . MET   A  1  574  ? -41.786 78.841  116.663 1.00 37.19 ? 572  MET   A SD    1 
ATOM   4186  C  CE    . MET   A  1  574  ? -43.002 77.523  116.709 1.00 44.98 ? 572  MET   A CE    1 
ATOM   4187  N  N     . LYS   A  1  575  ? -42.054 84.408  118.627 1.00 35.17 ? 573  LYS   A N     1 
ATOM   4188  C  CA    . LYS   A  1  575  ? -41.322 85.610  119.022 1.00 36.46 ? 573  LYS   A CA    1 
ATOM   4189  C  C     . LYS   A  1  575  ? -39.835 85.277  119.137 1.00 32.65 ? 573  LYS   A C     1 
ATOM   4190  O  O     . LYS   A  1  575  ? -39.246 85.225  120.219 1.00 33.66 ? 573  LYS   A O     1 
ATOM   4191  C  CB    . LYS   A  1  575  ? -41.885 86.171  120.323 1.00 35.67 ? 573  LYS   A CB    1 
ATOM   4192  N  N     . TRP   A  1  576  ? -39.237 85.043  117.971 1.00 29.44 ? 574  TRP   A N     1 
ATOM   4193  C  CA    . TRP   A  1  576  ? -37.824 84.699  117.880 1.00 28.54 ? 574  TRP   A CA    1 
ATOM   4194  C  C     . TRP   A  1  576  ? -36.970 85.828  118.433 1.00 26.05 ? 574  TRP   A C     1 
ATOM   4195  O  O     . TRP   A  1  576  ? -37.151 86.995  118.076 1.00 29.25 ? 574  TRP   A O     1 
ATOM   4196  C  CB    . TRP   A  1  576  ? -37.456 84.480  116.416 1.00 25.85 ? 574  TRP   A CB    1 
ATOM   4197  C  CG    . TRP   A  1  576  ? -38.138 83.324  115.782 1.00 27.17 ? 574  TRP   A CG    1 
ATOM   4198  C  CD1   . TRP   A  1  576  ? -39.116 83.369  114.827 1.00 26.43 ? 574  TRP   A CD1   1 
ATOM   4199  C  CD2   . TRP   A  1  576  ? -37.904 81.940  116.054 1.00 25.15 ? 574  TRP   A CD2   1 
ATOM   4200  N  NE1   . TRP   A  1  576  ? -39.493 82.097  114.482 1.00 26.67 ? 574  TRP   A NE1   1 
ATOM   4201  C  CE2   . TRP   A  1  576  ? -38.765 81.201  115.221 1.00 25.00 ? 574  TRP   A CE2   1 
ATOM   4202  C  CE3   . TRP   A  1  576  ? -37.045 81.252  116.918 1.00 25.64 ? 574  TRP   A CE3   1 
ATOM   4203  C  CZ2   . TRP   A  1  576  ? -38.789 79.805  115.219 1.00 25.80 ? 574  TRP   A CZ2   1 
ATOM   4204  C  CZ3   . TRP   A  1  576  ? -37.070 79.866  116.916 1.00 27.00 ? 574  TRP   A CZ3   1 
ATOM   4205  C  CH2   . TRP   A  1  576  ? -37.939 79.158  116.073 1.00 28.97 ? 574  TRP   A CH2   1 
ATOM   4206  N  N     . THR   A  1  577  ? -36.040 85.484  119.317 1.00 26.86 ? 575  THR   A N     1 
ATOM   4207  C  CA    . THR   A  1  577  ? -35.105 86.473  119.820 1.00 25.65 ? 575  THR   A CA    1 
ATOM   4208  C  C     . THR   A  1  577  ? -33.712 85.873  119.869 1.00 29.45 ? 575  THR   A C     1 
ATOM   4209  O  O     . THR   A  1  577  ? -33.526 84.652  119.861 1.00 29.38 ? 575  THR   A O     1 
ATOM   4210  C  CB    . THR   A  1  577  ? -35.460 86.973  121.223 1.00 30.57 ? 575  THR   A CB    1 
ATOM   4211  O  OG1   . THR   A  1  577  ? -35.358 85.880  122.141 1.00 31.92 ? 575  THR   A OG1   1 
ATOM   4212  C  CG2   . THR   A  1  577  ? -36.865 87.555  121.259 1.00 32.36 ? 575  THR   A CG2   1 
ATOM   4213  N  N     . ALA   A  1  578  ? -32.731 86.761  119.923 1.00 28.50 ? 576  ALA   A N     1 
ATOM   4214  C  CA    . ALA   A  1  578  ? -31.344 86.383  120.125 1.00 26.26 ? 576  ALA   A CA    1 
ATOM   4215  C  C     . ALA   A  1  578  ? -30.786 87.357  121.143 1.00 28.68 ? 576  ALA   A C     1 
ATOM   4216  O  O     . ALA   A  1  578  ? -30.901 88.572  120.962 1.00 30.62 ? 576  ALA   A O     1 
ATOM   4217  C  CB    . ALA   A  1  578  ? -30.557 86.499  118.820 1.00 28.34 ? 576  ALA   A CB    1 
ATOM   4218  N  N     . LEU   A  1  579  ? -30.221 86.830  122.216 1.00 29.15 ? 577  LEU   A N     1 
ATOM   4219  C  CA    . LEU   A  1  579  ? -29.718 87.637  123.314 1.00 29.57 ? 577  LEU   A CA    1 
ATOM   4220  C  C     . LEU   A  1  579  ? -28.286 87.232  123.602 1.00 30.11 ? 577  LEU   A C     1 
ATOM   4221  O  O     . LEU   A  1  579  ? -27.871 86.115  123.274 1.00 29.20 ? 577  LEU   A O     1 
ATOM   4222  C  CB    . LEU   A  1  579  ? -30.547 87.404  124.586 1.00 29.41 ? 577  LEU   A CB    1 
ATOM   4223  C  CG    . LEU   A  1  579  ? -32.065 87.371  124.465 1.00 33.69 ? 577  LEU   A CG    1 
ATOM   4224  C  CD1   . LEU   A  1  579  ? -32.663 87.037  125.819 1.00 35.03 ? 577  LEU   A CD1   1 
ATOM   4225  C  CD2   . LEU   A  1  579  ? -32.583 88.706  123.954 1.00 39.00 ? 577  LEU   A CD2   1 
ATOM   4226  N  N     . PRO   A  1  580  ? -27.502 88.113  124.223 1.00 28.11 ? 578  PRO   A N     1 
ATOM   4227  C  CA    . PRO   A  1  580  ? -26.188 87.687  124.708 1.00 27.78 ? 578  PRO   A CA    1 
ATOM   4228  C  C     . PRO   A  1  580  ? -26.390 86.695  125.833 1.00 32.77 ? 578  PRO   A C     1 
ATOM   4229  O  O     . PRO   A  1  580  ? -26.832 87.071  126.919 1.00 34.16 ? 578  PRO   A O     1 
ATOM   4230  C  CB    . PRO   A  1  580  ? -25.560 88.987  125.228 1.00 32.58 ? 578  PRO   A CB    1 
ATOM   4231  C  CG    . PRO   A  1  580  ? -26.387 90.090  124.646 1.00 33.09 ? 578  PRO   A CG    1 
ATOM   4232  C  CD    . PRO   A  1  580  ? -27.761 89.528  124.533 1.00 28.54 ? 578  PRO   A CD    1 
ATOM   4233  N  N     . GLN   A  1  581  ? -26.120 85.426  125.571 1.00 27.56 ? 579  GLN   A N     1 
ATOM   4234  C  CA    . GLN   A  1  581  ? -26.350 84.351  126.529 1.00 28.37 ? 579  GLN   A CA    1 
ATOM   4235  C  C     . GLN   A  1  581  ? -25.004 84.031  127.157 1.00 31.16 ? 579  GLN   A C     1 
ATOM   4236  O  O     . GLN   A  1  581  ? -24.272 83.151  126.700 1.00 32.40 ? 579  GLN   A O     1 
ATOM   4237  C  CB    . GLN   A  1  581  ? -26.955 83.135  125.839 1.00 28.94 ? 579  GLN   A CB    1 
ATOM   4238  C  CG    . GLN   A  1  581  ? -28.328 83.396  125.225 1.00 28.45 ? 579  GLN   A CG    1 
ATOM   4239  C  CD    . GLN   A  1  581  ? -29.420 83.539  126.264 1.00 33.99 ? 579  GLN   A CD    1 
ATOM   4240  O  OE1   . GLN   A  1  581  ? -29.175 83.406  127.463 1.00 34.49 ? 579  GLN   A OE1   1 
ATOM   4241  N  NE2   . GLN   A  1  581  ? -30.640 83.807  125.806 1.00 33.65 ? 579  GLN   A NE2   1 
ATOM   4242  N  N     . LEU   A  1  582  ? -24.673 84.778  128.203 1.00 31.03 ? 580  LEU   A N     1 
ATOM   4243  C  CA    . LEU   A  1  582  ? -23.439 84.552  128.924 1.00 31.24 ? 580  LEU   A CA    1 
ATOM   4244  C  C     . LEU   A  1  582  ? -23.604 83.361  129.863 1.00 32.78 ? 580  LEU   A C     1 
ATOM   4245  O  O     . LEU   A  1  582  ? -24.711 82.850  130.072 1.00 36.54 ? 580  LEU   A O     1 
ATOM   4246  C  CB    . LEU   A  1  582  ? -23.029 85.818  129.678 1.00 33.92 ? 580  LEU   A CB    1 
ATOM   4247  C  CG    . LEU   A  1  582  ? -22.214 86.865  128.903 1.00 39.41 ? 580  LEU   A CG    1 
ATOM   4248  C  CD1   . LEU   A  1  582  ? -22.938 87.365  127.665 1.00 34.94 ? 580  LEU   A CD1   1 
ATOM   4249  C  CD2   . LEU   A  1  582  ? -21.865 88.032  129.806 1.00 43.09 ? 580  LEU   A CD2   1 
ATOM   4250  N  N     . ALA   A  1  583  ? -22.482 82.903  130.423 1.00 31.60 ? 581  ALA   A N     1 
ATOM   4251  C  CA    . ALA   A  1  583  ? -22.541 81.778  131.347 1.00 32.54 ? 581  ALA   A CA    1 
ATOM   4252  C  C     . ALA   A  1  583  ? -23.464 82.084  132.514 1.00 35.96 ? 581  ALA   A C     1 
ATOM   4253  O  O     . ALA   A  1  583  ? -24.131 81.183  133.035 1.00 43.93 ? 581  ALA   A O     1 
ATOM   4254  C  CB    . ALA   A  1  583  ? -21.142 81.439  131.859 1.00 35.10 ? 581  ALA   A CB    1 
ATOM   4255  N  N     . THR   A  1  584  ? -23.535 83.353  132.909 1.00 36.88 ? 582  THR   A N     1 
ATOM   4256  C  CA    . THR   A  1  584  ? -24.318 83.816  134.046 1.00 38.29 ? 582  THR   A CA    1 
ATOM   4257  C  C     . THR   A  1  584  ? -25.766 84.123  133.693 1.00 40.86 ? 582  THR   A C     1 
ATOM   4258  O  O     . THR   A  1  584  ? -26.534 84.508  134.582 1.00 41.92 ? 582  THR   A O     1 
ATOM   4259  C  CB    . THR   A  1  584  ? -23.663 85.073  134.628 1.00 44.19 ? 582  THR   A CB    1 
ATOM   4260  O  OG1   . THR   A  1  584  ? -23.529 86.060  133.596 1.00 43.69 ? 582  THR   A OG1   1 
ATOM   4261  C  CG2   . THR   A  1  584  ? -22.292 84.748  135.190 1.00 42.06 ? 582  THR   A CG2   1 
ATOM   4262  N  N     . GLY   A  1  585  ? -26.156 83.972  132.430 1.00 38.28 ? 583  GLY   A N     1 
ATOM   4263  C  CA    . GLY   A  1  585  ? -27.507 84.260  132.008 1.00 37.64 ? 583  GLY   A CA    1 
ATOM   4264  C  C     . GLY   A  1  585  ? -27.551 85.328  130.934 1.00 40.58 ? 583  GLY   A C     1 
ATOM   4265  O  O     . GLY   A  1  585  ? -26.534 85.950  130.606 1.00 38.67 ? 583  GLY   A O     1 
ATOM   4266  N  N     . PRO   A  1  586  ? -28.737 85.570  130.372 1.00 37.68 ? 584  PRO   A N     1 
ATOM   4267  C  CA    . PRO   A  1  586  ? -28.861 86.589  129.324 1.00 36.80 ? 584  PRO   A CA    1 
ATOM   4268  C  C     . PRO   A  1  586  ? -28.461 87.966  129.835 1.00 40.89 ? 584  PRO   A C     1 
ATOM   4269  O  O     . PRO   A  1  586  ? -28.729 88.326  130.984 1.00 40.14 ? 584  PRO   A O     1 
ATOM   4270  C  CB    . PRO   A  1  586  ? -30.347 86.537  128.954 1.00 37.37 ? 584  PRO   A CB    1 
ATOM   4271  C  CG    . PRO   A  1  586  ? -31.018 86.002  130.175 1.00 42.11 ? 584  PRO   A CG    1 
ATOM   4272  C  CD    . PRO   A  1  586  ? -30.047 85.031  130.781 1.00 42.61 ? 584  PRO   A CD    1 
ATOM   4273  N  N     . ALA   A  1  587  ? -27.802 88.733  128.971 1.00 38.15 ? 585  ALA   A N     1 
ATOM   4274  C  CA    . ALA   A  1  587  ? -27.313 90.061  129.307 1.00 36.03 ? 585  ALA   A CA    1 
ATOM   4275  C  C     . ALA   A  1  587  ? -28.081 91.122  128.529 1.00 40.55 ? 585  ALA   A C     1 
ATOM   4276  O  O     . ALA   A  1  587  ? -28.661 90.855  127.472 1.00 37.46 ? 585  ALA   A O     1 
ATOM   4277  C  CB    . ALA   A  1  587  ? -25.810 90.185  129.031 1.00 38.48 ? 585  ALA   A CB    1 
ATOM   4278  N  N     . ALA   A  1  588  ? -28.100 92.331  129.080 1.00 38.93 ? 586  ALA   A N     1 
ATOM   4279  C  CA    . ALA   A  1  588  ? -28.754 93.436  128.401 1.00 38.59 ? 586  ALA   A CA    1 
ATOM   4280  C  C     . ALA   A  1  588  ? -27.860 93.979  127.291 1.00 36.13 ? 586  ALA   A C     1 
ATOM   4281  O  O     . ALA   A  1  588  ? -26.646 93.762  127.272 1.00 43.16 ? 586  ALA   A O     1 
ATOM   4282  C  CB    . ALA   A  1  588  ? -29.077 94.560  129.385 1.00 36.33 ? 586  ALA   A CB    1 
ATOM   4283  N  N     . GLY   A  1  589  ? -28.477 94.698  126.365 1.00 37.55 ? 587  GLY   A N     1 
ATOM   4284  C  CA    . GLY   A  1  589  ? -27.721 95.329  125.300 1.00 34.84 ? 587  GLY   A CA    1 
ATOM   4285  C  C     . GLY   A  1  589  ? -28.644 96.100  124.388 1.00 40.20 ? 587  GLY   A C     1 
ATOM   4286  O  O     . GLY   A  1  589  ? -29.851 96.216  124.634 1.00 39.95 ? 587  GLY   A O     1 
ATOM   4287  N  N     . GLU   A  1  590  ? -28.051 96.638  123.325 1.00 37.25 ? 588  GLU   A N     1 
ATOM   4288  C  CA    . GLU   A  1  590  ? -28.826 97.350  122.320 1.00 37.65 ? 588  GLU   A CA    1 
ATOM   4289  C  C     . GLU   A  1  590  ? -29.669 96.357  121.530 1.00 34.47 ? 588  GLU   A C     1 
ATOM   4290  O  O     . GLU   A  1  590  ? -29.153 95.367  121.000 1.00 35.92 ? 588  GLU   A O     1 
ATOM   4291  C  CB    . GLU   A  1  590  ? -27.892 98.115  121.382 1.00 44.33 ? 588  GLU   A CB    1 
ATOM   4292  N  N     . THR   A  1  591  ? -30.969 96.623  121.454 1.00 35.19 ? 589  THR   A N     1 
ATOM   4293  C  CA    . THR   A  1  591  ? -31.930 95.712  120.854 1.00 34.09 ? 589  THR   A CA    1 
ATOM   4294  C  C     . THR   A  1  591  ? -32.497 96.323  119.581 1.00 34.55 ? 589  THR   A C     1 
ATOM   4295  O  O     . THR   A  1  591  ? -32.847 97.507  119.550 1.00 36.99 ? 589  THR   A O     1 
ATOM   4296  C  CB    . THR   A  1  591  ? -33.064 95.432  121.847 1.00 38.87 ? 589  THR   A CB    1 
ATOM   4297  O  OG1   . THR   A  1  591  ? -32.547 94.708  122.975 1.00 39.80 ? 589  THR   A OG1   1 
ATOM   4298  C  CG2   . THR   A  1  591  ? -34.171 94.635  121.193 1.00 36.23 ? 589  THR   A CG2   1 
ATOM   4299  N  N     . ARG   A  1  592  ? -32.591 95.509  118.532 1.00 31.37 ? 590  ARG   A N     1 
ATOM   4300  C  CA    . ARG   A  1  592  ? -33.197 95.942  117.285 1.00 35.60 ? 590  ARG   A CA    1 
ATOM   4301  C  C     . ARG   A  1  592  ? -33.945 94.769  116.675 1.00 33.18 ? 590  ARG   A C     1 
ATOM   4302  O  O     . ARG   A  1  592  ? -33.717 93.609  117.033 1.00 31.55 ? 590  ARG   A O     1 
ATOM   4303  C  CB    . ARG   A  1  592  ? -32.158 96.480  116.295 1.00 37.33 ? 590  ARG   A CB    1 
ATOM   4304  C  CG    . ARG   A  1  592  ? -31.204 95.428  115.762 1.00 37.40 ? 590  ARG   A CG    1 
ATOM   4305  C  CD    . ARG   A  1  592  ? -30.477 95.919  114.516 1.00 38.84 ? 590  ARG   A CD    1 
ATOM   4306  N  NE    . ARG   A  1  592  ? -29.401 95.015  114.131 1.00 41.03 ? 590  ARG   A NE    1 
ATOM   4307  C  CZ    . ARG   A  1  592  ? -29.580 93.892  113.451 1.00 38.95 ? 590  ARG   A CZ    1 
ATOM   4308  N  NH1   . ARG   A  1  592  ? -30.783 93.511  113.051 1.00 37.54 ? 590  ARG   A NH1   1 
ATOM   4309  N  NH2   . ARG   A  1  592  ? -28.527 93.127  113.172 1.00 39.72 ? 590  ARG   A NH2   1 
ATOM   4310  N  N     . THR   A  1  593  ? -34.843 95.084  115.747 1.00 31.09 ? 591  THR   A N     1 
ATOM   4311  C  CA    . THR   A  1  593  ? -35.572 94.036  115.058 1.00 31.25 ? 591  THR   A CA    1 
ATOM   4312  C  C     . THR   A  1  593  ? -34.711 93.388  113.976 1.00 32.62 ? 591  THR   A C     1 
ATOM   4313  O  O     . THR   A  1  593  ? -33.744 93.964  113.469 1.00 31.66 ? 591  THR   A O     1 
ATOM   4314  C  CB    . THR   A  1  593  ? -36.839 94.593  114.420 1.00 35.59 ? 591  THR   A CB    1 
ATOM   4315  O  OG1   . THR   A  1  593  ? -36.492 95.688  113.564 1.00 38.21 ? 591  THR   A OG1   1 
ATOM   4316  C  CG2   . THR   A  1  593  ? -37.801 95.067  115.490 1.00 36.53 ? 591  THR   A CG2   1 
ATOM   4317  N  N     . VAL   A  1  594  ? -35.075 92.158  113.639 1.00 26.84 ? 592  VAL   A N     1 
ATOM   4318  C  CA    . VAL   A  1  594  ? -34.500 91.437  112.513 1.00 28.16 ? 592  VAL   A CA    1 
ATOM   4319  C  C     . VAL   A  1  594  ? -35.579 91.373  111.440 1.00 28.98 ? 592  VAL   A C     1 
ATOM   4320  O  O     . VAL   A  1  594  ? -36.678 90.862  111.691 1.00 28.79 ? 592  VAL   A O     1 
ATOM   4321  C  CB    . VAL   A  1  594  ? -34.036 90.032  112.927 1.00 27.05 ? 592  VAL   A CB    1 
ATOM   4322  C  CG1   . VAL   A  1  594  ? -33.530 89.256  111.719 1.00 28.23 ? 592  VAL   A CG1   1 
ATOM   4323  C  CG2   . VAL   A  1  594  ? -32.942 90.127  113.995 1.00 30.48 ? 592  VAL   A CG2   1 
ATOM   4324  N  N     . LEU   A  1  595  ? -35.280 91.904  110.257 1.00 28.69 ? 593  LEU   A N     1 
ATOM   4325  C  CA    . LEU   A  1  595  ? -36.264 92.024  109.189 1.00 27.45 ? 593  LEU   A CA    1 
ATOM   4326  C  C     . LEU   A  1  595  ? -35.997 90.986  108.108 1.00 26.74 ? 593  LEU   A C     1 
ATOM   4327  O  O     . LEU   A  1  595  ? -34.847 90.650  107.821 1.00 27.70 ? 593  LEU   A O     1 
ATOM   4328  C  CB    . LEU   A  1  595  ? -36.228 93.426  108.567 1.00 27.77 ? 593  LEU   A CB    1 
ATOM   4329  C  CG    . LEU   A  1  595  ? -36.467 94.611  109.507 1.00 29.49 ? 593  LEU   A CG    1 
ATOM   4330  C  CD1   . LEU   A  1  595  ? -36.474 95.914  108.724 1.00 34.23 ? 593  LEU   A CD1   1 
ATOM   4331  C  CD2   . LEU   A  1  595  ? -37.769 94.435  110.267 1.00 31.01 ? 593  LEU   A CD2   1 
ATOM   4332  N  N     . ASN   A  1  596  ? -37.072 90.485  107.511 1.00 25.12 ? 594  ASN   A N     1 
ATOM   4333  C  CA    . ASN   A  1  596  ? -36.960 89.548  106.400 1.00 24.93 ? 594  ASN   A CA    1 
ATOM   4334  C  C     . ASN   A  1  596  ? -36.309 90.270  105.227 1.00 23.90 ? 594  ASN   A C     1 
ATOM   4335  O  O     . ASN   A  1  596  ? -36.844 91.291  104.767 1.00 24.95 ? 594  ASN   A O     1 
ATOM   4336  C  CB    . ASN   A  1  596  ? -38.387 89.131  106.042 1.00 23.56 ? 594  ASN   A CB    1 
ATOM   4337  C  CG    . ASN   A  1  596  ? -38.449 88.034  104.996 1.00 24.65 ? 594  ASN   A CG    1 
ATOM   4338  O  OD1   . ASN   A  1  596  ? -37.602 87.943  104.113 1.00 23.65 ? 594  ASN   A OD1   1 
ATOM   4339  N  ND2   . ASN   A  1  596  ? -39.480 87.200  105.087 1.00 26.27 ? 594  ASN   A ND2   1 
ATOM   4340  N  N     . PRO   A  1  597  ? -35.168 89.793  104.719 1.00 23.73 ? 595  PRO   A N     1 
ATOM   4341  C  CA    . PRO   A  1  597  ? -34.505 90.500  103.609 1.00 22.81 ? 595  PRO   A CA    1 
ATOM   4342  C  C     . PRO   A  1  597  ? -35.346 90.569  102.351 1.00 24.60 ? 595  PRO   A C     1 
ATOM   4343  O  O     . PRO   A  1  597  ? -35.114 91.451  101.513 1.00 22.78 ? 595  PRO   A O     1 
ATOM   4344  C  CB    . PRO   A  1  597  ? -33.220 89.687  103.378 1.00 25.40 ? 595  PRO   A CB    1 
ATOM   4345  C  CG    . PRO   A  1  597  ? -33.511 88.341  103.944 1.00 24.15 ? 595  PRO   A CG    1 
ATOM   4346  C  CD    . PRO   A  1  597  ? -34.432 88.582  105.120 1.00 22.64 ? 595  PRO   A CD    1 
ATOM   4347  N  N     . GLY   A  1  598  ? -36.312 89.669  102.192 1.00 22.73 ? 596  GLY   A N     1 
ATOM   4348  C  CA    . GLY   A  1  598  ? -37.200 89.697  101.051 1.00 21.31 ? 596  GLY   A CA    1 
ATOM   4349  C  C     . GLY   A  1  598  ? -38.392 90.608  101.200 1.00 24.17 ? 596  GLY   A C     1 
ATOM   4350  O  O     . GLY   A  1  598  ? -39.122 90.822  100.228 1.00 25.80 ? 596  GLY   A O     1 
ATOM   4351  N  N     . ASP   A  1  599  ? -38.599 91.160  102.391 1.00 22.74 ? 597  ASP   A N     1 
ATOM   4352  C  CA    . ASP   A  1  599  ? -39.724 92.049  102.647 1.00 25.21 ? 597  ASP   A CA    1 
ATOM   4353  C  C     . ASP   A  1  599  ? -39.505 92.650  104.019 1.00 24.72 ? 597  ASP   A C     1 
ATOM   4354  O  O     . ASP   A  1  599  ? -39.803 92.009  105.034 1.00 24.87 ? 597  ASP   A O     1 
ATOM   4355  C  CB    . ASP   A  1  599  ? -41.038 91.272  102.638 1.00 24.11 ? 597  ASP   A CB    1 
ATOM   4356  C  CG    . ASP   A  1  599  ? -42.255 92.171  102.716 1.00 26.20 ? 597  ASP   A CG    1 
ATOM   4357  O  OD1   . ASP   A  1  599  ? -42.135 93.319  103.195 1.00 27.28 ? 597  ASP   A OD1   1 
ATOM   4358  O  OD2   . ASP   A  1  599  ? -43.336 91.715  102.294 1.00 28.70 ? 597  ASP   A OD2   1 
ATOM   4359  N  N     . HIS   A  1  600  ? -38.976 93.873  104.058 1.00 25.26 ? 598  HIS   A N     1 
ATOM   4360  C  CA    . HIS   A  1  600  ? -38.627 94.500  105.328 1.00 29.33 ? 598  HIS   A CA    1 
ATOM   4361  C  C     . HIS   A  1  600  ? -39.832 94.747  106.224 1.00 30.37 ? 598  HIS   A C     1 
ATOM   4362  O  O     . HIS   A  1  600  ? -39.647 95.008  107.418 1.00 32.05 ? 598  HIS   A O     1 
ATOM   4363  C  CB    . HIS   A  1  600  ? -37.846 95.790  105.083 1.00 28.13 ? 598  HIS   A CB    1 
ATOM   4364  C  CG    . HIS   A  1  600  ? -36.450 95.559  104.593 1.00 29.97 ? 598  HIS   A CG    1 
ATOM   4365  N  ND1   . HIS   A  1  600  ? -35.577 96.588  104.310 1.00 32.92 ? 598  HIS   A ND1   1 
ATOM   4366  C  CD2   . HIS   A  1  600  ? -35.775 94.412  104.341 1.00 30.35 ? 598  HIS   A CD2   1 
ATOM   4367  C  CE1   . HIS   A  1  600  ? -34.424 96.084  103.904 1.00 34.42 ? 598  HIS   A CE1   1 
ATOM   4368  N  NE2   . HIS   A  1  600  ? -34.517 94.766  103.916 1.00 33.58 ? 598  HIS   A NE2   1 
ATOM   4369  N  N     . ARG   A  1  601  ? -41.050 94.655  105.690 1.00 26.71 ? 599  ARG   A N     1 
ATOM   4370  C  CA    . ARG   A  1  601  ? -42.243 94.772  106.514 1.00 28.80 ? 599  ARG   A CA    1 
ATOM   4371  C  C     . ARG   A  1  601  ? -42.462 93.542  107.381 1.00 29.89 ? 599  ARG   A C     1 
ATOM   4372  O  O     . ARG   A  1  601  ? -43.227 93.612  108.349 1.00 31.81 ? 599  ARG   A O     1 
ATOM   4373  C  CB    . ARG   A  1  601  ? -43.464 94.981  105.624 1.00 28.10 ? 599  ARG   A CB    1 
ATOM   4374  C  CG    . ARG   A  1  601  ? -43.356 96.168  104.689 1.00 29.28 ? 599  ARG   A CG    1 
ATOM   4375  C  CD    . ARG   A  1  601  ? -44.468 96.146  103.657 1.00 32.56 ? 599  ARG   A CD    1 
ATOM   4376  N  NE    . ARG   A  1  601  ? -44.428 94.928  102.855 1.00 29.99 ? 599  ARG   A NE    1 
ATOM   4377  C  CZ    . ARG   A  1  601  ? -45.329 94.599  101.941 1.00 31.92 ? 599  ARG   A CZ    1 
ATOM   4378  N  NH1   . ARG   A  1  601  ? -46.352 95.395  101.658 1.00 33.41 ? 599  ARG   A NH1   1 
ATOM   4379  N  NH2   . ARG   A  1  601  ? -45.207 93.440  101.300 1.00 29.49 ? 599  ARG   A NH2   1 
ATOM   4380  N  N     . ASP   A  1  602  ? -41.812 92.425  107.054 1.00 26.65 ? 600  ASP   A N     1 
ATOM   4381  C  CA    . ASP   A  1  602  ? -41.970 91.178  107.795 1.00 28.65 ? 600  ASP   A CA    1 
ATOM   4382  C  C     . ASP   A  1  602  ? -40.901 91.155  108.877 1.00 31.16 ? 600  ASP   A C     1 
ATOM   4383  O  O     . ASP   A  1  602  ? -39.738 90.851  108.609 1.00 28.58 ? 600  ASP   A O     1 
ATOM   4384  C  CB    . ASP   A  1  602  ? -41.836 89.983  106.856 1.00 26.55 ? 600  ASP   A CB    1 
ATOM   4385  C  CG    . ASP   A  1  602  ? -41.988 88.656  107.577 1.00 30.17 ? 600  ASP   A CG    1 
ATOM   4386  O  OD1   . ASP   A  1  602  ? -42.533 88.657  108.699 1.00 30.00 ? 600  ASP   A OD1   1 
ATOM   4387  O  OD2   . ASP   A  1  602  ? -41.547 87.615  107.035 1.00 27.30 ? 600  ASP   A OD2   1 
ATOM   4388  N  N     . VAL   A  1  603  ? -41.291 91.481  110.103 1.00 30.55 ? 601  VAL   A N     1 
ATOM   4389  C  CA    . VAL   A  1  603  ? -40.366 91.431  111.227 1.00 28.84 ? 601  VAL   A CA    1 
ATOM   4390  C  C     . VAL   A  1  603  ? -40.261 89.985  111.687 1.00 29.72 ? 601  VAL   A C     1 
ATOM   4391  O  O     . VAL   A  1  603  ? -41.263 89.359  112.047 1.00 30.66 ? 601  VAL   A O     1 
ATOM   4392  C  CB    . VAL   A  1  603  ? -40.823 92.351  112.365 1.00 33.65 ? 601  VAL   A CB    1 
ATOM   4393  C  CG1   . VAL   A  1  603  ? -39.844 92.268  113.523 1.00 30.90 ? 601  VAL   A CG1   1 
ATOM   4394  C  CG2   . VAL   A  1  603  ? -40.933 93.775  111.866 1.00 32.71 ? 601  VAL   A CG2   1 
ATOM   4395  N  N     . VAL   A  1  604  ? -39.045 89.453  111.673 1.00 27.34 ? 602  VAL   A N     1 
ATOM   4396  C  CA    . VAL   A  1  604  ? -38.821 88.057  112.018 1.00 28.43 ? 602  VAL   A CA    1 
ATOM   4397  C  C     . VAL   A  1  604  ? -38.564 87.893  113.505 1.00 27.72 ? 602  VAL   A C     1 
ATOM   4398  O  O     . VAL   A  1  604  ? -38.992 86.914  114.118 1.00 28.77 ? 602  VAL   A O     1 
ATOM   4399  C  CB    . VAL   A  1  604  ? -37.653 87.514  111.177 1.00 26.47 ? 602  VAL   A CB    1 
ATOM   4400  C  CG1   . VAL   A  1  604  ? -37.453 86.041  111.462 1.00 25.17 ? 602  VAL   A CG1   1 
ATOM   4401  C  CG2   . VAL   A  1  604  ? -37.908 87.770  109.701 1.00 26.42 ? 602  VAL   A CG2   1 
ATOM   4402  N  N     . GLY   A  1  605  ? -37.874 88.847  114.107 1.00 26.87 ? 603  GLY   A N     1 
ATOM   4403  C  CA    . GLY   A  1  605  ? -37.587 88.749  115.516 1.00 25.70 ? 603  GLY   A CA    1 
ATOM   4404  C  C     . GLY   A  1  605  ? -36.816 89.951  115.993 1.00 25.97 ? 603  GLY   A C     1 
ATOM   4405  O  O     . GLY   A  1  605  ? -36.786 90.996  115.341 1.00 31.03 ? 603  GLY   A O     1 
ATOM   4406  N  N     . SER   A  1  606  ? -36.185 89.781  117.145 1.00 27.94 ? 604  SER   A N     1 
ATOM   4407  C  CA    A SER   A  1  606  ? -35.428 90.852  117.763 0.51 27.25 ? 604  SER   A CA    1 
ATOM   4408  C  CA    B SER   A  1  606  ? -35.444 90.848  117.792 0.49 27.27 ? 604  SER   A CA    1 
ATOM   4409  C  C     . SER   A  1  606  ? -34.114 90.300  118.279 1.00 30.97 ? 604  SER   A C     1 
ATOM   4410  O  O     . SER   A  1  606  ? -34.054 89.185  118.807 1.00 30.06 ? 604  SER   A O     1 
ATOM   4411  C  CB    A SER   A  1  606  ? -36.206 91.497  118.910 0.51 30.09 ? 604  SER   A CB    1 
ATOM   4412  C  CB    B SER   A  1  606  ? -36.232 91.387  118.987 0.49 30.04 ? 604  SER   A CB    1 
ATOM   4413  O  OG    A SER   A  1  606  ? -37.346 92.169  118.411 0.51 31.10 ? 604  SER   A OG    1 
ATOM   4414  O  OG    B SER   A  1  606  ? -35.471 92.330  119.709 0.49 30.91 ? 604  SER   A OG    1 
ATOM   4415  N  N     . VAL   A  1  607  ? -33.054 91.077  118.099 1.00 28.29 ? 605  VAL   A N     1 
ATOM   4416  C  CA    . VAL   A  1  607  ? -31.730 90.696  118.566 1.00 29.61 ? 605  VAL   A CA    1 
ATOM   4417  C  C     . VAL   A  1  607  ? -31.262 91.736  119.566 1.00 28.78 ? 605  VAL   A C     1 
ATOM   4418  O  O     . VAL   A  1  607  ? -31.397 92.942  119.331 1.00 31.32 ? 605  VAL   A O     1 
ATOM   4419  C  CB    . VAL   A  1  607  ? -30.719 90.530  117.415 1.00 28.96 ? 605  VAL   A CB    1 
ATOM   4420  C  CG1   . VAL   A  1  607  ? -30.627 91.801  116.573 1.00 30.69 ? 605  VAL   A CG1   1 
ATOM   4421  C  CG2   . VAL   A  1  607  ? -29.356 90.142  117.968 1.00 29.29 ? 605  VAL   A CG2   1 
ATOM   4422  N  N     . THR   A  1  608  ? -30.744 91.267  120.687 1.00 28.80 ? 606  THR   A N     1 
ATOM   4423  C  CA    . THR   A  1  608  ? -30.063 92.120  121.642 1.00 29.73 ? 606  THR   A CA    1 
ATOM   4424  C  C     . THR   A  1  608  ? -28.578 91.868  121.443 1.00 30.56 ? 606  THR   A C     1 
ATOM   4425  O  O     . THR   A  1  608  ? -28.112 90.738  121.616 1.00 30.16 ? 606  THR   A O     1 
ATOM   4426  C  CB    . THR   A  1  608  ? -30.486 91.760  123.063 1.00 31.18 ? 606  THR   A CB    1 
ATOM   4427  O  OG1   . THR   A  1  608  ? -31.902 91.949  123.196 1.00 31.88 ? 606  THR   A OG1   1 
ATOM   4428  C  CG2   . THR   A  1  608  ? -29.764 92.637  124.065 1.00 33.14 ? 606  THR   A CG2   1 
ATOM   4429  N  N     . GLU   A  1  609  ? -27.847 92.903  121.057 1.00 29.70 ? 607  GLU   A N     1 
ATOM   4430  C  CA    . GLU   A  1  609  ? -26.446 92.720  120.714 1.00 32.29 ? 607  GLU   A CA    1 
ATOM   4431  C  C     . GLU   A  1  609  ? -25.539 92.877  121.935 1.00 32.48 ? 607  GLU   A C     1 
ATOM   4432  O  O     . GLU   A  1  609  ? -25.901 93.485  122.945 1.00 31.64 ? 607  GLU   A O     1 
ATOM   4433  C  CB    . GLU   A  1  609  ? -26.064 93.632  119.546 1.00 34.99 ? 607  GLU   A CB    1 
ATOM   4434  C  CG    . GLU   A  1  609  ? -26.828 93.222  118.278 1.00 38.54 ? 607  GLU   A CG    1 
ATOM   4435  C  CD    . GLU   A  1  609  ? -26.393 93.949  117.019 1.00 42.14 ? 607  GLU   A CD    1 
ATOM   4436  O  OE1   . GLU   A  1  609  ? -26.081 95.157  117.101 1.00 47.50 ? 607  GLU   A OE1   1 
ATOM   4437  O  OE2   . GLU   A  1  609  ? -26.374 93.304  115.942 1.00 40.30 ? 607  GLU   A OE2   1 
ATOM   4438  N  N     . THR   A  1  610  ? -24.359 92.279  121.839 1.00 31.24 ? 608  THR   A N     1 
ATOM   4439  C  CA    . THR   A  1  610  ? -23.447 92.155  122.966 1.00 30.01 ? 608  THR   A CA    1 
ATOM   4440  C  C     . THR   A  1  610  ? -22.560 93.389  123.036 1.00 35.14 ? 608  THR   A C     1 
ATOM   4441  O  O     . THR   A  1  610  ? -22.003 93.820  122.022 1.00 36.07 ? 608  THR   A O     1 
ATOM   4442  C  CB    . THR   A  1  610  ? -22.570 90.912  122.783 1.00 30.94 ? 608  THR   A CB    1 
ATOM   4443  O  OG1   . THR   A  1  610  ? -23.401 89.765  122.557 1.00 29.97 ? 608  THR   A OG1   1 
ATOM   4444  C  CG2   . THR   A  1  610  ? -21.708 90.669  124.010 1.00 33.22 ? 608  THR   A CG2   1 
ATOM   4445  N  N     . SER   A  1  611  ? -22.434 93.956  124.230 1.00 33.92 ? 609  SER   A N     1 
ATOM   4446  C  CA    . SER   A  1  611  ? -21.449 95.003  124.433 1.00 35.89 ? 609  SER   A CA    1 
ATOM   4447  C  C     . SER   A  1  611  ? -20.055 94.394  124.386 1.00 37.29 ? 609  SER   A C     1 
ATOM   4448  O  O     . SER   A  1  611  ? -19.860 93.208  124.666 1.00 33.45 ? 609  SER   A O     1 
ATOM   4449  C  CB    . SER   A  1  611  ? -21.661 95.669  125.790 1.00 37.94 ? 609  SER   A CB    1 
ATOM   4450  O  OG    . SER   A  1  611  ? -21.255 94.812  126.843 1.00 38.22 ? 609  SER   A OG    1 
ATOM   4451  N  N     . GLU   A  1  612  ? -19.074 95.215  124.014 1.00 38.27 ? 610  GLU   A N     1 
ATOM   4452  C  CA    . GLU   A  1  612  ? -17.706 94.715  123.997 1.00 37.90 ? 610  GLU   A CA    1 
ATOM   4453  C  C     . GLU   A  1  612  ? -17.232 94.347  125.396 1.00 37.28 ? 610  GLU   A C     1 
ATOM   4454  O  O     . GLU   A  1  612  ? -16.409 93.438  125.552 1.00 38.50 ? 610  GLU   A O     1 
ATOM   4455  C  CB    . GLU   A  1  612  ? -16.779 95.719  123.310 1.00 47.54 ? 610  GLU   A CB    1 
ATOM   4456  C  CG    . GLU   A  1  612  ? -16.890 95.666  121.789 1.00 46.29 ? 610  GLU   A CG    1 
ATOM   4457  C  CD    . GLU   A  1  612  ? -16.438 96.944  121.109 1.00 55.18 ? 610  GLU   A CD    1 
ATOM   4458  O  OE1   . GLU   A  1  612  ? -15.297 97.388  121.359 1.00 59.02 ? 610  GLU   A OE1   1 
ATOM   4459  O  OE2   . GLU   A  1  612  ? -17.234 97.506  120.324 1.00 56.28 ? 610  GLU   A OE2   1 
ATOM   4460  N  N     . GLU   A  1  613  ? -17.767 95.012  126.424 1.00 35.39 ? 611  GLU   A N     1 
ATOM   4461  C  CA    . GLU   A  1  613  ? -17.460 94.623  127.796 1.00 40.40 ? 611  GLU   A CA    1 
ATOM   4462  C  C     . GLU   A  1  613  ? -17.973 93.220  128.096 1.00 36.12 ? 611  GLU   A C     1 
ATOM   4463  O  O     . GLU   A  1  613  ? -17.263 92.410  128.705 1.00 33.82 ? 611  GLU   A O     1 
ATOM   4464  C  CB    . GLU   A  1  613  ? -18.046 95.637  128.779 1.00 41.77 ? 611  GLU   A CB    1 
ATOM   4465  N  N     . ASP   A  1  614  ? -19.199 92.906  127.666 1.00 35.47 ? 612  ASP   A N     1 
ATOM   4466  C  CA    . ASP   A  1  614  ? -19.755 91.588  127.957 1.00 33.25 ? 612  ASP   A CA    1 
ATOM   4467  C  C     . ASP   A  1  614  ? -19.096 90.499  127.122 1.00 34.27 ? 612  ASP   A C     1 
ATOM   4468  O  O     . ASP   A  1  614  ? -19.000 89.351  127.570 1.00 31.34 ? 612  ASP   A O     1 
ATOM   4469  C  CB    . ASP   A  1  614  ? -21.269 91.584  127.760 1.00 35.23 ? 612  ASP   A CB    1 
ATOM   4470  C  CG    . ASP   A  1  614  ? -22.001 92.315  128.876 1.00 34.30 ? 612  ASP   A CG    1 
ATOM   4471  O  OD1   . ASP   A  1  614  ? -21.446 92.416  129.992 1.00 38.22 ? 612  ASP   A OD1   1 
ATOM   4472  O  OD2   . ASP   A  1  614  ? -23.130 92.787  128.637 1.00 38.51 ? 612  ASP   A OD2   1 
ATOM   4473  N  N     . ALA   A  1  615  ? -18.637 90.835  125.916 1.00 32.28 ? 613  ALA   A N     1 
ATOM   4474  C  CA    . ALA   A  1  615  ? -17.878 89.867  125.133 1.00 31.43 ? 613  ALA   A CA    1 
ATOM   4475  C  C     . ALA   A  1  615  ? -16.601 89.475  125.860 1.00 30.33 ? 613  ALA   A C     1 
ATOM   4476  O  O     . ALA   A  1  615  ? -16.275 88.287  125.965 1.00 30.26 ? 613  ALA   A O     1 
ATOM   4477  C  CB    . ALA   A  1  615  ? -17.564 90.436  123.752 1.00 31.38 ? 613  ALA   A CB    1 
ATOM   4478  N  N     . ARG   A  1  616  ? -15.882 90.461  126.400 1.00 33.55 ? 614  ARG   A N     1 
ATOM   4479  C  CA    . ARG   A  1  616  ? -14.687 90.155  127.179 1.00 36.06 ? 614  ARG   A CA    1 
ATOM   4480  C  C     . ARG   A  1  616  ? -15.036 89.370  128.435 1.00 32.60 ? 614  ARG   A C     1 
ATOM   4481  O  O     . ARG   A  1  616  ? -14.326 88.431  128.807 1.00 32.84 ? 614  ARG   A O     1 
ATOM   4482  C  CB    . ARG   A  1  616  ? -13.946 91.443  127.525 1.00 40.74 ? 614  ARG   A CB    1 
ATOM   4483  C  CG    . ARG   A  1  616  ? -13.108 91.978  126.380 1.00 39.26 ? 614  ARG   A CG    1 
ATOM   4484  C  CD    . ARG   A  1  616  ? -12.448 93.304  126.735 1.00 49.23 ? 614  ARG   A CD    1 
ATOM   4485  N  NE    . ARG   A  1  616  ? -12.999 94.408  125.957 1.00 53.81 ? 614  ARG   A NE    1 
ATOM   4486  C  CZ    . ARG   A  1  616  ? -13.741 95.388  126.456 1.00 48.33 ? 614  ARG   A CZ    1 
ATOM   4487  N  NH1   . ARG   A  1  616  ? -14.031 95.450  127.747 1.00 54.59 ? 614  ARG   A NH1   1 
ATOM   4488  N  NH2   . ARG   A  1  616  ? -14.194 96.336  125.641 1.00 49.69 ? 614  ARG   A NH2   1 
ATOM   4489  N  N     . ARG   A  1  617  ? -16.145 89.723  129.087 1.00 31.55 ? 615  ARG   A N     1 
ATOM   4490  C  CA    . ARG   A  1  617  ? -16.576 88.957  130.249 1.00 32.72 ? 615  ARG   A CA    1 
ATOM   4491  C  C     . ARG   A  1  617  ? -16.893 87.519  129.862 1.00 35.15 ? 615  ARG   A C     1 
ATOM   4492  O  O     . ARG   A  1  617  ? -16.570 86.582  130.601 1.00 32.14 ? 615  ARG   A O     1 
ATOM   4493  C  CB    . ARG   A  1  617  ? -17.784 89.628  130.901 1.00 35.63 ? 615  ARG   A CB    1 
ATOM   4494  C  CG    . ARG   A  1  617  ? -18.213 88.978  132.201 1.00 40.30 ? 615  ARG   A CG    1 
ATOM   4495  C  CD    . ARG   A  1  617  ? -18.955 89.964  133.089 1.00 44.14 ? 615  ARG   A CD    1 
ATOM   4496  N  NE    . ARG   A  1  617  ? -20.180 90.465  132.476 1.00 44.56 ? 615  ARG   A NE    1 
ATOM   4497  C  CZ    . ARG   A  1  617  ? -21.365 89.881  132.593 1.00 48.72 ? 615  ARG   A CZ    1 
ATOM   4498  N  NH1   . ARG   A  1  617  ? -21.509 88.731  133.234 1.00 48.77 ? 615  ARG   A NH1   1 
ATOM   4499  N  NH2   . ARG   A  1  617  ? -22.434 90.467  132.057 1.00 44.57 ? 615  ARG   A NH2   1 
ATOM   4500  N  N     . ALA   A  1  618  ? -17.513 87.322  128.698 1.00 31.43 ? 616  ALA   A N     1 
ATOM   4501  C  CA    . ALA   A  1  618  ? -17.846 85.969  128.268 1.00 31.78 ? 616  ALA   A CA    1 
ATOM   4502  C  C     . ALA   A  1  618  ? -16.592 85.116  128.106 1.00 29.21 ? 616  ALA   A C     1 
ATOM   4503  O  O     . ALA   A  1  618  ? -16.574 83.942  128.498 1.00 30.00 ? 616  ALA   A O     1 
ATOM   4504  C  CB    . ALA   A  1  618  ? -18.658 86.009  126.972 1.00 30.70 ? 616  ALA   A CB    1 
ATOM   4505  N  N     . VAL   A  1  619  ? -15.525 85.690  127.548 1.00 28.06 ? 617  VAL   A N     1 
ATOM   4506  C  CA    . VAL   A  1  619  ? -14.293 84.921  127.389 1.00 29.44 ? 617  VAL   A CA    1 
ATOM   4507  C  C     . VAL   A  1  619  ? -13.726 84.541  128.750 1.00 30.33 ? 617  VAL   A C     1 
ATOM   4508  O  O     . VAL   A  1  619  ? -13.279 83.408  128.958 1.00 31.92 ? 617  VAL   A O     1 
ATOM   4509  C  CB    . VAL   A  1  619  ? -13.271 85.671  126.512 1.00 29.51 ? 617  VAL   A CB    1 
ATOM   4510  C  CG1   . VAL   A  1  619  ? -11.967 84.874  126.409 1.00 30.36 ? 617  VAL   A CG1   1 
ATOM   4511  C  CG2   . VAL   A  1  619  ? -13.836 85.927  125.119 1.00 27.40 ? 617  VAL   A CG2   1 
ATOM   4512  N  N     . ARG   A  1  620  ? -13.767 85.468  129.710 1.00 29.14 ? 618  ARG   A N     1 
ATOM   4513  C  CA    . ARG   A  1  620  ? -13.277 85.144  131.046 1.00 33.02 ? 618  ARG   A CA    1 
ATOM   4514  C  C     . ARG   A  1  620  ? -14.114 84.044  131.683 1.00 31.61 ? 618  ARG   A C     1 
ATOM   4515  O  O     . ARG   A  1  620  ? -13.572 83.130  132.317 1.00 34.33 ? 618  ARG   A O     1 
ATOM   4516  C  CB    . ARG   A  1  620  ? -13.240 86.399  131.918 1.00 36.55 ? 618  ARG   A CB    1 
ATOM   4517  C  CG    . ARG   A  1  620  ? -12.185 87.401  131.477 1.00 39.12 ? 618  ARG   A CG    1 
ATOM   4518  C  CD    . ARG   A  1  620  ? -12.068 88.584  132.437 1.00 47.42 ? 618  ARG   A CD    1 
ATOM   4519  N  NE    . ARG   A  1  620  ? -12.590 89.808  131.839 1.00 50.89 ? 618  ARG   A NE    1 
ATOM   4520  C  CZ    . ARG   A  1  620  ? -13.730 90.391  132.185 1.00 46.45 ? 618  ARG   A CZ    1 
ATOM   4521  N  NH1   . ARG   A  1  620  ? -14.472 89.927  133.180 1.00 52.91 ? 618  ARG   A NH1   1 
ATOM   4522  N  NH2   . ARG   A  1  620  ? -14.135 91.470  131.520 1.00 49.64 ? 618  ARG   A NH2   1 
ATOM   4523  N  N     . LEU   A  1  621  ? -15.435 84.103  131.506 1.00 29.06 ? 619  LEU   A N     1 
ATOM   4524  C  CA    . LEU   A  1  621  ? -16.296 83.032  131.996 1.00 33.51 ? 619  LEU   A CA    1 
ATOM   4525  C  C     . LEU   A  1  621  ? -15.984 81.714  131.303 1.00 32.80 ? 619  LEU   A C     1 
ATOM   4526  O  O     . LEU   A  1  621  ? -15.970 80.657  131.945 1.00 33.67 ? 619  LEU   A O     1 
ATOM   4527  C  CB    . LEU   A  1  621  ? -17.762 83.403  131.778 1.00 30.86 ? 619  LEU   A CB    1 
ATOM   4528  C  CG    . LEU   A  1  621  ? -18.316 84.571  132.595 1.00 33.34 ? 619  LEU   A CG    1 
ATOM   4529  C  CD1   . LEU   A  1  621  ? -19.728 84.905  132.151 1.00 34.27 ? 619  LEU   A CD1   1 
ATOM   4530  C  CD2   . LEU   A  1  621  ? -18.303 84.227  134.066 1.00 34.55 ? 619  LEU   A CD2   1 
ATOM   4531  N  N     . ALA   A  1  622  ? -15.750 81.753  129.988 1.00 31.11 ? 620  ALA   A N     1 
ATOM   4532  C  CA    . ALA   A  1  622  ? -15.360 80.546  129.269 1.00 32.44 ? 620  ALA   A CA    1 
ATOM   4533  C  C     . ALA   A  1  622  ? -14.057 79.986  129.815 1.00 30.58 ? 620  ALA   A C     1 
ATOM   4534  O  O     . ALA   A  1  622  ? -13.928 78.774  130.015 1.00 30.23 ? 620  ALA   A O     1 
ATOM   4535  C  CB    . ALA   A  1  622  ? -15.217 80.851  127.780 1.00 30.11 ? 620  ALA   A CB    1 
ATOM   4536  N  N     . ALA   A  1  623  ? -13.076 80.858  130.056 1.00 29.79 ? 621  ALA   A N     1 
ATOM   4537  C  CA    . ALA   A  1  623  ? -11.806 80.404  130.608 1.00 30.03 ? 621  ALA   A CA    1 
ATOM   4538  C  C     . ALA   A  1  623  ? -12.003 79.753  131.968 1.00 31.18 ? 621  ALA   A C     1 
ATOM   4539  O  O     . ALA   A  1  623  ? -11.408 78.710  132.256 1.00 33.64 ? 621  ALA   A O     1 
ATOM   4540  C  CB    . ALA   A  1  623  ? -10.830 81.573  130.705 1.00 33.53 ? 621  ALA   A CB    1 
ATOM   4541  N  N     . ASP   A  1  624  ? -12.842 80.353  132.817 1.00 32.24 ? 622  ASP   A N     1 
ATOM   4542  C  CA    . ASP   A  1  624  ? -13.117 79.761  134.123 1.00 36.50 ? 622  ASP   A CA    1 
ATOM   4543  C  C     . ASP   A  1  624  ? -13.804 78.408  133.990 1.00 37.33 ? 622  ASP   A C     1 
ATOM   4544  O  O     . ASP   A  1  624  ? -13.545 77.497  134.786 1.00 40.35 ? 622  ASP   A O     1 
ATOM   4545  C  CB    . ASP   A  1  624  ? -13.985 80.708  134.958 1.00 39.17 ? 622  ASP   A CB    1 
ATOM   4546  C  CG    . ASP   A  1  624  ? -13.294 82.028  135.256 1.00 44.21 ? 622  ASP   A CG    1 
ATOM   4547  O  OD1   . ASP   A  1  624  ? -12.046 82.079  135.198 1.00 46.88 ? 622  ASP   A OD1   1 
ATOM   4548  O  OD2   . ASP   A  1  624  ? -14.005 83.014  135.553 1.00 52.48 ? 622  ASP   A OD2   1 
ATOM   4549  N  N     . ALA   A  1  625  ? -14.664 78.256  132.983 1.00 36.10 ? 623  ALA   A N     1 
ATOM   4550  C  CA    . ALA   A  1  625  ? -15.412 77.028  132.752 1.00 37.51 ? 623  ALA   A CA    1 
ATOM   4551  C  C     . ALA   A  1  625  ? -14.638 75.989  131.960 1.00 38.87 ? 623  ALA   A C     1 
ATOM   4552  O  O     . ALA   A  1  625  ? -15.124 74.862  131.815 1.00 40.76 ? 623  ALA   A O     1 
ATOM   4553  C  CB    . ALA   A  1  625  ? -16.686 77.345  131.973 1.00 40.45 ? 623  ALA   A CB    1 
ATOM   4554  N  N     . ALA   A  1  626  ? -13.470 76.338  131.426 1.00 33.48 ? 624  ALA   A N     1 
ATOM   4555  C  CA    . ALA   A  1  626  ? -12.752 75.401  130.565 1.00 32.47 ? 624  ALA   A CA    1 
ATOM   4556  C  C     . ALA   A  1  626  ? -12.440 74.072  131.242 1.00 36.27 ? 624  ALA   A C     1 
ATOM   4557  O  O     . ALA   A  1  626  ? -12.676 73.022  130.621 1.00 36.70 ? 624  ALA   A O     1 
ATOM   4558  C  CB    . ALA   A  1  626  ? -11.520 76.075  129.952 1.00 35.38 ? 624  ALA   A CB    1 
ATOM   4559  N  N     . PRO   A  1  627  ? -11.922 74.025  132.479 1.00 36.20 ? 625  PRO   A N     1 
ATOM   4560  C  CA    . PRO   A  1  627  ? -11.623 72.709  133.075 1.00 35.89 ? 625  PRO   A CA    1 
ATOM   4561  C  C     . PRO   A  1  627  ? -12.842 71.819  133.229 1.00 36.17 ? 625  PRO   A C     1 
ATOM   4562  O  O     . PRO   A  1  627  ? -12.764 70.611  132.972 1.00 37.61 ? 625  PRO   A O     1 
ATOM   4563  C  CB    . PRO   A  1  627  ? -11.010 73.072  134.436 1.00 36.94 ? 625  PRO   A CB    1 
ATOM   4564  C  CG    . PRO   A  1  627  ? -10.481 74.455  134.249 1.00 38.06 ? 625  PRO   A CG    1 
ATOM   4565  C  CD    . PRO   A  1  627  ? -11.476 75.125  133.354 1.00 38.24 ? 625  PRO   A CD    1 
ATOM   4566  N  N     . ASP   A  1  628  ? -13.973 72.385  133.641 1.00 36.52 ? 626  ASP   A N     1 
ATOM   4567  C  CA    . ASP   A  1  628  ? -15.155 71.564  133.863 1.00 38.78 ? 626  ASP   A CA    1 
ATOM   4568  C  C     . ASP   A  1  628  ? -15.640 70.941  132.561 1.00 37.11 ? 626  ASP   A C     1 
ATOM   4569  O  O     . ASP   A  1  628  ? -16.044 69.773  132.536 1.00 38.84 ? 626  ASP   A O     1 
ATOM   4570  C  CB    . ASP   A  1  628  ? -16.254 72.399  134.519 1.00 36.29 ? 626  ASP   A CB    1 
ATOM   4571  C  CG    . ASP   A  1  628  ? -15.875 72.857  135.915 1.00 43.89 ? 626  ASP   A CG    1 
ATOM   4572  O  OD1   . ASP   A  1  628  ? -15.075 72.156  136.567 1.00 46.70 ? 626  ASP   A OD1   1 
ATOM   4573  O  OD2   . ASP   A  1  628  ? -16.376 73.912  136.357 1.00 50.75 ? 626  ASP   A OD2   1 
ATOM   4574  N  N     . TRP   A  1  629  ? -15.590 71.697  131.465 1.00 32.82 ? 627  TRP   A N     1 
ATOM   4575  C  CA    . TRP   A  1  629  ? -16.062 71.160  130.196 1.00 31.33 ? 627  TRP   A CA    1 
ATOM   4576  C  C     . TRP   A  1  629  ? -15.071 70.157  129.624 1.00 30.06 ? 627  TRP   A C     1 
ATOM   4577  O  O     . TRP   A  1  629  ? -15.473 69.119  129.085 1.00 30.96 ? 627  TRP   A O     1 
ATOM   4578  C  CB    . TRP   A  1  629  ? -16.336 72.292  129.210 1.00 30.84 ? 627  TRP   A CB    1 
ATOM   4579  C  CG    . TRP   A  1  629  ? -16.826 71.792  127.894 1.00 28.42 ? 627  TRP   A CG    1 
ATOM   4580  C  CD1   . TRP   A  1  629  ? -16.237 71.980  126.671 1.00 27.30 ? 627  TRP   A CD1   1 
ATOM   4581  C  CD2   . TRP   A  1  629  ? -17.979 70.976  127.660 1.00 26.59 ? 627  TRP   A CD2   1 
ATOM   4582  N  NE1   . TRP   A  1  629  ? -16.967 71.353  125.698 1.00 26.20 ? 627  TRP   A NE1   1 
ATOM   4583  C  CE2   . TRP   A  1  629  ? -18.046 70.737  126.275 1.00 25.57 ? 627  TRP   A CE2   1 
ATOM   4584  C  CE3   . TRP   A  1  629  ? -18.978 70.447  128.480 1.00 27.85 ? 627  TRP   A CE3   1 
ATOM   4585  C  CZ2   . TRP   A  1  629  ? -19.056 69.978  125.696 1.00 28.49 ? 627  TRP   A CZ2   1 
ATOM   4586  C  CZ3   . TRP   A  1  629  ? -19.979 69.690  127.897 1.00 29.44 ? 627  TRP   A CZ3   1 
ATOM   4587  C  CH2   . TRP   A  1  629  ? -20.010 69.466  126.519 1.00 29.55 ? 627  TRP   A CH2   1 
ATOM   4588  N  N     . ALA   A  1  630  ? -13.774 70.450  129.731 1.00 29.87 ? 628  ALA   A N     1 
ATOM   4589  C  CA    . ALA   A  1  630  ? -12.764 69.490  129.301 1.00 33.54 ? 628  ALA   A CA    1 
ATOM   4590  C  C     . ALA   A  1  630  ? -12.885 68.173  130.055 1.00 32.81 ? 628  ALA   A C     1 
ATOM   4591  O  O     . ALA   A  1  630  ? -12.517 67.117  129.526 1.00 32.97 ? 628  ALA   A O     1 
ATOM   4592  C  CB    . ALA   A  1  630  ? -11.366 70.081  129.481 1.00 31.48 ? 628  ALA   A CB    1 
ATOM   4593  N  N     . ALA   A  1  631  ? -13.401 68.214  131.286 1.00 33.23 ? 629  ALA   A N     1 
ATOM   4594  C  CA    . ALA   A  1  631  ? -13.507 67.008  132.096 1.00 34.73 ? 629  ALA   A CA    1 
ATOM   4595  C  C     . ALA   A  1  631  ? -14.699 66.140  131.719 1.00 33.08 ? 629  ALA   A C     1 
ATOM   4596  O  O     . ALA   A  1  631  ? -14.767 64.983  132.147 1.00 32.99 ? 629  ALA   A O     1 
ATOM   4597  C  CB    . ALA   A  1  631  ? -13.564 67.363  133.584 1.00 35.69 ? 629  ALA   A CB    1 
ATOM   4598  N  N     . VAL   A  1  632  ? -15.640 66.662  130.941 1.00 33.64 ? 630  VAL   A N     1 
ATOM   4599  C  CA    . VAL   A  1  632  ? -16.720 65.836  130.415 1.00 31.13 ? 630  VAL   A CA    1 
ATOM   4600  C  C     . VAL   A  1  632  ? -16.075 64.896  129.406 1.00 31.44 ? 630  VAL   A C     1 
ATOM   4601  O  O     . VAL   A  1  632  ? -15.416 65.370  128.471 1.00 30.39 ? 630  VAL   A O     1 
ATOM   4602  C  CB    . VAL   A  1  632  ? -17.825 66.696  129.785 1.00 30.57 ? 630  VAL   A CB    1 
ATOM   4603  C  CG1   . VAL   A  1  632  ? -18.920 65.820  129.188 1.00 31.15 ? 630  VAL   A CG1   1 
ATOM   4604  C  CG2   . VAL   A  1  632  ? -18.399 67.646  130.836 1.00 31.82 ? 630  VAL   A CG2   1 
ATOM   4605  N  N     . PRO   A  1  633  ? -16.206 63.580  129.571 1.00 28.96 ? 631  PRO   A N     1 
ATOM   4606  C  CA    . PRO   A  1  633  ? -15.509 62.664  128.677 1.00 27.17 ? 631  PRO   A CA    1 
ATOM   4607  C  C     . PRO   A  1  633  ? -15.919 62.897  127.243 1.00 28.06 ? 631  PRO   A C     1 
ATOM   4608  O  O     . PRO   A  1  633  ? -17.066 63.291  126.955 1.00 28.18 ? 631  PRO   A O     1 
ATOM   4609  C  CB    . PRO   A  1  633  ? -15.961 61.283  129.169 1.00 29.93 ? 631  PRO   A CB    1 
ATOM   4610  C  CG    . PRO   A  1  633  ? -16.331 61.497  130.597 1.00 32.52 ? 631  PRO   A CG    1 
ATOM   4611  C  CD    . PRO   A  1  633  ? -16.925 62.871  130.642 1.00 31.43 ? 631  PRO   A CD    1 
ATOM   4612  N  N     . PRO   A  1  634  ? -15.010 62.677  126.295 1.00 26.17 ? 632  PRO   A N     1 
ATOM   4613  C  CA    . PRO   A  1  634  ? -15.345 62.908  124.881 1.00 24.98 ? 632  PRO   A CA    1 
ATOM   4614  C  C     . PRO   A  1  634  ? -16.605 62.189  124.432 1.00 23.70 ? 632  PRO   A C     1 
ATOM   4615  O  O     . PRO   A  1  634  ? -17.386 62.752  123.658 1.00 23.76 ? 632  PRO   A O     1 
ATOM   4616  C  CB    . PRO   A  1  634  ? -14.099 62.406  124.138 1.00 25.99 ? 632  PRO   A CB    1 
ATOM   4617  C  CG    . PRO   A  1  634  ? -12.992 62.484  125.148 1.00 28.03 ? 632  PRO   A CG    1 
ATOM   4618  C  CD    . PRO   A  1  634  ? -13.615 62.246  126.495 1.00 26.95 ? 632  PRO   A CD    1 
ATOM   4619  N  N     . SER   A  1  635  ? -16.826 60.957  124.894 1.00 26.73 ? 633  SER   A N     1 
ATOM   4620  C  CA    . SER   A  1  635  ? -18.023 60.225  124.493 1.00 28.80 ? 633  SER   A CA    1 
ATOM   4621  C  C     . SER   A  1  635  ? -19.284 60.953  124.936 1.00 28.66 ? 633  SER   A C     1 
ATOM   4622  O  O     . SER   A  1  635  ? -20.284 60.978  124.206 1.00 26.41 ? 633  SER   A O     1 
ATOM   4623  C  CB    . SER   A  1  635  ? -17.994 58.822  125.095 1.00 33.98 ? 633  SER   A CB    1 
ATOM   4624  O  OG    . SER   A  1  635  ? -18.037 58.882  126.509 1.00 40.80 ? 633  SER   A OG    1 
ATOM   4625  N  N     . GLU   A  1  636  ? -19.253 61.560  126.124 1.00 27.81 ? 634  GLU   A N     1 
ATOM   4626  C  CA    . GLU   A  1  636  ? -20.424 62.287  126.598 1.00 27.62 ? 634  GLU   A CA    1 
ATOM   4627  C  C     . GLU   A  1  636  ? -20.584 63.614  125.870 1.00 27.60 ? 634  GLU   A C     1 
ATOM   4628  O  O     . GLU   A  1  636  ? -21.709 64.023  125.564 1.00 27.34 ? 634  GLU   A O     1 
ATOM   4629  C  CB    . GLU   A  1  636  ? -20.380 62.484  128.113 1.00 29.76 ? 634  GLU   A CB    1 
ATOM   4630  C  CG    . GLU   A  1  636  ? -21.589 63.252  128.650 1.00 35.60 ? 634  GLU   A CG    1 
ATOM   4631  C  CD    . GLU   A  1  636  ? -22.932 62.687  128.171 1.00 43.69 ? 634  GLU   A CD    1 
ATOM   4632  O  OE1   . GLU   A  1  636  ? -23.129 61.455  128.254 1.00 43.36 ? 634  GLU   A OE1   1 
ATOM   4633  O  OE2   . GLU   A  1  636  ? -23.791 63.474  127.703 1.00 38.36 ? 634  GLU   A OE2   1 
ATOM   4634  N  N     . ARG   A  1  637  ? -19.477 64.295  125.560 1.00 25.42 ? 635  ARG   A N     1 
ATOM   4635  C  CA    . ARG   A  1  637  ? -19.585 65.470  124.706 1.00 25.24 ? 635  ARG   A CA    1 
ATOM   4636  C  C     . ARG   A  1  637  ? -20.193 65.091  123.366 1.00 22.92 ? 635  ARG   A C     1 
ATOM   4637  O  O     . ARG   A  1  637  ? -21.094 65.772  122.865 1.00 24.17 ? 635  ARG   A O     1 
ATOM   4638  C  CB    . ARG   A  1  637  ? -18.219 66.134  124.529 1.00 23.21 ? 635  ARG   A CB    1 
ATOM   4639  C  CG    . ARG   A  1  637  ? -17.559 66.449  125.862 1.00 25.14 ? 635  ARG   A CG    1 
ATOM   4640  C  CD    . ARG   A  1  637  ? -16.396 67.408  125.734 1.00 26.72 ? 635  ARG   A CD    1 
ATOM   4641  N  NE    . ARG   A  1  637  ? -15.341 66.894  124.874 1.00 25.75 ? 635  ARG   A NE    1 
ATOM   4642  C  CZ    . ARG   A  1  637  ? -14.151 66.473  125.286 1.00 27.06 ? 635  ARG   A CZ    1 
ATOM   4643  N  NH1   . ARG   A  1  637  ? -13.838 66.414  126.571 1.00 30.32 ? 635  ARG   A NH1   1 
ATOM   4644  N  NH2   . ARG   A  1  637  ? -13.243 66.125  124.381 1.00 25.59 ? 635  ARG   A NH2   1 
ATOM   4645  N  N     . ALA   A  1  638  ? -19.741 63.974  122.793 1.00 24.02 ? 636  ALA   A N     1 
ATOM   4646  C  CA    . ALA   A  1  638  ? -20.292 63.522  121.522 1.00 23.21 ? 636  ALA   A CA    1 
ATOM   4647  C  C     . ALA   A  1  638  ? -21.772 63.188  121.648 1.00 25.25 ? 636  ALA   A C     1 
ATOM   4648  O  O     . ALA   A  1  638  ? -22.550 63.419  120.713 1.00 22.01 ? 636  ALA   A O     1 
ATOM   4649  C  CB    . ALA   A  1  638  ? -19.510 62.308  121.020 1.00 23.20 ? 636  ALA   A CB    1 
ATOM   4650  N  N     . ALA   A  1  639  ? -22.179 62.638  122.795 1.00 23.15 ? 637  ALA   A N     1 
ATOM   4651  C  CA    . ALA   A  1  639  ? -23.592 62.345  123.012 1.00 22.83 ? 637  ALA   A CA    1 
ATOM   4652  C  C     . ALA   A  1  639  ? -24.429 63.616  123.019 1.00 26.80 ? 637  ALA   A C     1 
ATOM   4653  O  O     . ALA   A  1  639  ? -25.582 63.593  122.580 1.00 25.36 ? 637  ALA   A O     1 
ATOM   4654  C  CB    . ALA   A  1  639  ? -23.784 61.544  124.300 1.00 26.77 ? 637  ALA   A CB    1 
ATOM   4655  N  N     . CYS   A  1  640  ? -23.874 64.731  123.510 1.00 23.58 ? 638  CYS   A N     1 
ATOM   4656  C  CA    . CYS   A  1  640  ? -24.597 65.999  123.441 1.00 24.69 ? 638  CYS   A CA    1 
ATOM   4657  C  C     . CYS   A  1  640  ? -24.818 66.402  121.995 1.00 24.75 ? 638  CYS   A C     1 
ATOM   4658  O  O     . CYS   A  1  640  ? -25.918 66.821  121.611 1.00 23.40 ? 638  CYS   A O     1 
ATOM   4659  C  CB    . CYS   A  1  640  ? -23.822 67.105  124.154 1.00 25.06 ? 638  CYS   A CB    1 
ATOM   4660  S  SG    . CYS   A  1  640  ? -23.655 66.939  125.935 1.00 27.59 ? 638  CYS   A SG    1 
ATOM   4661  N  N     . LEU   A  1  641  ? -23.774 66.285  121.176 1.00 22.94 ? 639  LEU   A N     1 
ATOM   4662  C  CA    . LEU   A  1  641  ? -23.915 66.604  119.765 1.00 22.96 ? 639  LEU   A CA    1 
ATOM   4663  C  C     . LEU   A  1  641  ? -24.971 65.729  119.117 1.00 21.28 ? 639  LEU   A C     1 
ATOM   4664  O  O     . LEU   A  1  641  ? -25.812 66.223  118.359 1.00 21.74 ? 639  LEU   A O     1 
ATOM   4665  C  CB    . LEU   A  1  641  ? -22.578 66.432  119.051 1.00 22.23 ? 639  LEU   A CB    1 
ATOM   4666  C  CG    . LEU   A  1  641  ? -21.667 67.662  119.021 1.00 24.47 ? 639  LEU   A CG    1 
ATOM   4667  C  CD1   . LEU   A  1  641  ? -21.243 68.088  120.406 1.00 26.71 ? 639  LEU   A CD1   1 
ATOM   4668  C  CD2   . LEU   A  1  641  ? -20.452 67.393  118.147 1.00 22.17 ? 639  LEU   A CD2   1 
ATOM   4669  N  N     . ASP   A  1  642  ? -24.955 64.427  119.408 1.00 21.80 ? 640  ASP   A N     1 
ATOM   4670  C  CA    . ASP   A  1  642  ? -25.954 63.545  118.818 1.00 23.66 ? 640  ASP   A CA    1 
ATOM   4671  C  C     . ASP   A  1  642  ? -27.358 63.909  119.276 1.00 23.32 ? 640  ASP   A C     1 
ATOM   4672  O  O     . ASP   A  1  642  ? -28.306 63.864  118.482 1.00 23.38 ? 640  ASP   A O     1 
ATOM   4673  C  CB    . ASP   A  1  642  ? -25.648 62.090  119.148 1.00 22.71 ? 640  ASP   A CB    1 
ATOM   4674  C  CG    . ASP   A  1  642  ? -24.594 61.498  118.232 1.00 23.30 ? 640  ASP   A CG    1 
ATOM   4675  O  OD1   . ASP   A  1  642  ? -24.365 62.050  117.123 1.00 23.71 ? 640  ASP   A OD1   1 
ATOM   4676  O  OD2   . ASP   A  1  642  ? -24.009 60.472  118.633 1.00 25.80 ? 640  ASP   A OD2   1 
ATOM   4677  N  N     . ARG   A  1  643  ? -27.514 64.271  120.551 1.00 22.40 ? 641  ARG   A N     1 
ATOM   4678  C  CA    . ARG   A  1  643  ? -28.824 64.703  121.022 1.00 22.02 ? 641  ARG   A CA    1 
ATOM   4679  C  C     . ARG   A  1  643  ? -29.258 65.981  120.324 1.00 24.50 ? 641  ARG   A C     1 
ATOM   4680  O  O     . ARG   A  1  643  ? -30.431 66.129  119.961 1.00 25.52 ? 641  ARG   A O     1 
ATOM   4681  C  CB    . ARG   A  1  643  ? -28.815 64.884  122.538 1.00 24.63 ? 641  ARG   A CB    1 
ATOM   4682  C  CG    . ARG   A  1  643  ? -28.927 63.574  123.294 1.00 25.78 ? 641  ARG   A CG    1 
ATOM   4683  C  CD    . ARG   A  1  643  ? -29.140 63.796  124.781 1.00 30.18 ? 641  ARG   A CD    1 
ATOM   4684  N  NE    . ARG   A  1  643  ? -28.027 64.509  125.389 1.00 28.11 ? 641  ARG   A NE    1 
ATOM   4685  C  CZ    . ARG   A  1  643  ? -27.003 63.916  125.987 1.00 25.48 ? 641  ARG   A CZ    1 
ATOM   4686  N  NH1   . ARG   A  1  643  ? -26.910 62.599  126.044 1.00 31.43 ? 641  ARG   A NH1   1 
ATOM   4687  N  NH2   . ARG   A  1  643  ? -26.064 64.662  126.560 1.00 32.05 ? 641  ARG   A NH2   1 
ATOM   4688  N  N     . ALA   A  1  644  ? -28.325 66.913  120.114 1.00 21.55 ? 642  ALA   A N     1 
ATOM   4689  C  CA    . ALA   A  1  644  ? -28.669 68.135  119.398 1.00 22.57 ? 642  ALA   A CA    1 
ATOM   4690  C  C     . ALA   A  1  644  ? -29.099 67.819  117.979 1.00 21.73 ? 642  ALA   A C     1 
ATOM   4691  O  O     . ALA   A  1  644  ? -30.034 68.435  117.455 1.00 22.58 ? 642  ALA   A O     1 
ATOM   4692  C  CB    . ALA   A  1  644  ? -27.507 69.126  119.416 1.00 22.86 ? 642  ALA   A CB    1 
ATOM   4693  N  N     . ALA   A  1  645  ? -28.435 66.852  117.340 1.00 21.77 ? 643  ALA   A N     1 
ATOM   4694  C  CA    . ALA   A  1  645  ? -28.823 66.462  115.991 1.00 21.01 ? 643  ALA   A CA    1 
ATOM   4695  C  C     . ALA   A  1  645  ? -30.254 65.939  115.968 1.00 22.27 ? 643  ALA   A C     1 
ATOM   4696  O  O     . ALA   A  1  645  ? -31.043 66.300  115.088 1.00 22.17 ? 643  ALA   A O     1 
ATOM   4697  C  CB    . ALA   A  1  645  ? -27.845 65.417  115.455 1.00 21.66 ? 643  ALA   A CB    1 
ATOM   4698  N  N     . GLU   A  1  646  ? -30.601 65.078  116.927 1.00 22.12 ? 644  GLU   A N     1 
ATOM   4699  C  CA    . GLU   A  1  646  ? -31.972 64.589  117.020 1.00 24.17 ? 644  GLU   A CA    1 
ATOM   4700  C  C     . GLU   A  1  646  ? -32.950 65.738  117.202 1.00 26.23 ? 644  GLU   A C     1 
ATOM   4701  O  O     . GLU   A  1  646  ? -34.023 65.752  116.588 1.00 25.04 ? 644  GLU   A O     1 
ATOM   4702  C  CB    . GLU   A  1  646  ? -32.108 63.615  118.190 1.00 30.74 ? 644  GLU   A CB    1 
ATOM   4703  C  CG    . GLU   A  1  646  ? -31.398 62.287  118.020 1.00 32.65 ? 644  GLU   A CG    1 
ATOM   4704  C  CD    . GLU   A  1  646  ? -31.897 61.501  116.822 1.00 41.22 ? 644  GLU   A CD    1 
ATOM   4705  O  OE1   . GLU   A  1  646  ? -33.110 61.566  116.528 1.00 47.52 ? 644  GLU   A OE1   1 
ATOM   4706  O  OE2   . GLU   A  1  646  ? -31.068 60.828  116.169 1.00 39.42 ? 644  GLU   A OE2   1 
ATOM   4707  N  N     . LEU   A  1  647  ? -32.603 66.702  118.058 1.00 24.10 ? 645  LEU   A N     1 
ATOM   4708  C  CA    . LEU   A  1  647  ? -33.490 67.834  118.298 1.00 25.02 ? 645  LEU   A CA    1 
ATOM   4709  C  C     . LEU   A  1  647  ? -33.666 68.662  117.038 1.00 25.53 ? 645  LEU   A C     1 
ATOM   4710  O  O     . LEU   A  1  647  ? -34.784 69.078  116.718 1.00 25.45 ? 645  LEU   A O     1 
ATOM   4711  C  CB    . LEU   A  1  647  ? -32.950 68.695  119.435 1.00 25.96 ? 645  LEU   A CB    1 
ATOM   4712  C  CG    . LEU   A  1  647  ? -33.025 68.044  120.813 1.00 27.43 ? 645  LEU   A CG    1 
ATOM   4713  C  CD1   . LEU   A  1  647  ? -32.331 68.904  121.850 1.00 26.69 ? 645  LEU   A CD1   1 
ATOM   4714  C  CD2   . LEU   A  1  647  ? -34.480 67.813  121.207 1.00 29.53 ? 645  LEU   A CD2   1 
ATOM   4715  N  N     . MET   A  1  648  ? -32.581 68.899  116.300 1.00 22.53 ? 646  MET   A N     1 
ATOM   4716  C  CA    . MET   A  1  648  ? -32.692 69.661  115.064 1.00 23.68 ? 646  MET   A CA    1 
ATOM   4717  C  C     . MET   A  1  648  ? -33.489 68.900  114.022 1.00 23.15 ? 646  MET   A C     1 
ATOM   4718  O  O     . MET   A  1  648  ? -34.263 69.500  113.271 1.00 23.68 ? 646  MET   A O     1 
ATOM   4719  C  CB    . MET   A  1  648  ? -31.307 70.010  114.525 1.00 20.10 ? 646  MET   A CB    1 
ATOM   4720  C  CG    . MET   A  1  648  ? -30.617 71.073  115.328 1.00 23.52 ? 646  MET   A CG    1 
ATOM   4721  S  SD    . MET   A  1  648  ? -29.243 71.731  114.387 1.00 25.57 ? 646  MET   A SD    1 
ATOM   4722  C  CE    . MET   A  1  648  ? -28.543 72.878  115.564 1.00 28.48 ? 646  MET   A CE    1 
ATOM   4723  N  N     . GLN   A  1  649  ? -33.315 67.579  113.955 1.00 22.20 ? 647  GLN   A N     1 
ATOM   4724  C  CA    . GLN   A  1  649  ? -34.101 66.794  113.011 1.00 23.75 ? 647  GLN   A CA    1 
ATOM   4725  C  C     . GLN   A  1  649  ? -35.588 66.910  113.315 1.00 22.51 ? 647  GLN   A C     1 
ATOM   4726  O  O     . GLN   A  1  649  ? -36.404 67.115  112.407 1.00 25.89 ? 647  GLN   A O     1 
ATOM   4727  C  CB    . GLN   A  1  649  ? -33.671 65.330  113.046 1.00 25.21 ? 647  GLN   A CB    1 
ATOM   4728  C  CG    . GLN   A  1  649  ? -34.384 64.499  111.992 1.00 22.99 ? 647  GLN   A CG    1 
ATOM   4729  C  CD    . GLN   A  1  649  ? -33.831 64.751  110.612 1.00 23.66 ? 647  GLN   A CD    1 
ATOM   4730  O  OE1   . GLN   A  1  649  ? -32.758 64.268  110.271 1.00 22.06 ? 647  GLN   A OE1   1 
ATOM   4731  N  NE2   . GLN   A  1  649  ? -34.554 65.517  109.809 1.00 23.87 ? 647  GLN   A NE2   1 
ATOM   4732  N  N     . ALA   A  1  650  ? -35.957 66.781  114.588 1.00 23.56 ? 648  ALA   A N     1 
ATOM   4733  C  CA    . ALA   A  1  650  ? -37.365 66.855  114.965 1.00 24.34 ? 648  ALA   A CA    1 
ATOM   4734  C  C     . ALA   A  1  650  ? -37.927 68.249  114.748 1.00 30.07 ? 648  ALA   A C     1 
ATOM   4735  O  O     . ALA   A  1  650  ? -39.116 68.398  114.429 1.00 30.15 ? 648  ALA   A O     1 
ATOM   4736  C  CB    . ALA   A  1  650  ? -37.528 66.438  116.425 1.00 27.94 ? 648  ALA   A CB    1 
ATOM   4737  N  N     . ARG   A  1  651  ? -37.101 69.271  114.922 1.00 24.44 ? 649  ARG   A N     1 
ATOM   4738  C  CA    . ARG   A  1  651  ? -37.515 70.660  114.815 1.00 25.38 ? 649  ARG   A CA    1 
ATOM   4739  C  C     . ARG   A  1  651  ? -37.340 71.216  113.411 1.00 21.35 ? 649  ARG   A C     1 
ATOM   4740  O  O     . ARG   A  1  651  ? -37.609 72.402  113.195 1.00 24.58 ? 649  ARG   A O     1 
ATOM   4741  C  CB    . ARG   A  1  651  ? -36.727 71.513  115.819 1.00 30.18 ? 649  ARG   A CB    1 
ATOM   4742  C  CG    . ARG   A  1  651  ? -37.326 72.887  116.116 1.00 34.59 ? 649  ARG   A CG    1 
ATOM   4743  C  CD    . ARG   A  1  651  ? -37.185 73.250  117.594 1.00 32.45 ? 649  ARG   A CD    1 
ATOM   4744  N  NE    . ARG   A  1  651  ? -37.675 74.593  117.894 1.00 36.76 ? 649  ARG   A NE    1 
ATOM   4745  C  CZ    . ARG   A  1  651  ? -38.955 74.920  118.023 1.00 36.51 ? 649  ARG   A CZ    1 
ATOM   4746  N  NH1   . ARG   A  1  651  ? -39.919 74.033  117.834 1.00 35.39 ? 649  ARG   A NH1   1 
ATOM   4747  N  NH2   . ARG   A  1  651  ? -39.277 76.172  118.337 1.00 39.65 ? 649  ARG   A NH2   1 
ATOM   4748  N  N     . MET   A  1  652  ? -36.891 70.395  112.463 1.00 24.71 ? 650  MET   A N     1 
ATOM   4749  C  CA    . MET   A  1  652  ? -36.584 70.899  111.126 1.00 22.87 ? 650  MET   A CA    1 
ATOM   4750  C  C     . MET   A  1  652  ? -37.667 71.791  110.539 1.00 23.58 ? 650  MET   A C     1 
ATOM   4751  O  O     . MET   A  1  652  ? -37.328 72.882  110.058 1.00 23.41 ? 650  MET   A O     1 
ATOM   4752  C  CB    . MET   A  1  652  ? -36.208 69.758  110.170 1.00 24.50 ? 650  MET   A CB    1 
ATOM   4753  C  CG    . MET   A  1  652  ? -36.050 70.225  108.743 1.00 21.52 ? 650  MET   A CG    1 
ATOM   4754  S  SD    . MET   A  1  652  ? -35.584 68.880  107.647 1.00 24.71 ? 650  MET   A SD    1 
ATOM   4755  C  CE    . MET   A  1  652  ? -33.860 68.685  108.053 1.00 23.20 ? 650  MET   A CE    1 
ATOM   4756  N  N     . PRO   A  1  653  ? -38.957 71.418  110.548 1.00 23.44 ? 651  PRO   A N     1 
ATOM   4757  C  CA    . PRO   A  1  653  ? -39.963 72.308  109.939 1.00 25.03 ? 651  PRO   A CA    1 
ATOM   4758  C  C     . PRO   A  1  653  ? -39.944 73.711  110.515 1.00 24.31 ? 651  PRO   A C     1 
ATOM   4759  O  O     . PRO   A  1  653  ? -39.969 74.695  109.768 1.00 23.67 ? 651  PRO   A O     1 
ATOM   4760  C  CB    . PRO   A  1  653  ? -41.285 71.583  110.223 1.00 26.19 ? 651  PRO   A CB    1 
ATOM   4761  C  CG    . PRO   A  1  653  ? -40.895 70.141  110.333 1.00 27.72 ? 651  PRO   A CG    1 
ATOM   4762  C  CD    . PRO   A  1  653  ? -39.565 70.170  111.042 1.00 26.03 ? 651  PRO   A CD    1 
ATOM   4763  N  N     . THR   A  1  654  ? -39.885 73.825  111.838 1.00 23.12 ? 652  THR   A N     1 
ATOM   4764  C  CA    . THR   A  1  654  ? -39.804 75.139  112.459 1.00 22.65 ? 652  THR   A CA    1 
ATOM   4765  C  C     . THR   A  1  654  ? -38.505 75.844  112.094 1.00 23.72 ? 652  THR   A C     1 
ATOM   4766  O  O     . THR   A  1  654  ? -38.507 77.046  111.799 1.00 24.14 ? 652  THR   A O     1 
ATOM   4767  C  CB    . THR   A  1  654  ? -39.947 74.998  113.970 1.00 25.61 ? 652  THR   A CB    1 
ATOM   4768  O  OG1   . THR   A  1  654  ? -41.201 74.371  114.255 1.00 28.64 ? 652  THR   A OG1   1 
ATOM   4769  C  CG2   . THR   A  1  654  ? -39.891 76.360  114.639 1.00 27.43 ? 652  THR   A CG2   1 
ATOM   4770  N  N     . LEU   A  1  655  ? -37.389 75.112  112.095 1.00 24.12 ? 653  LEU   A N     1 
ATOM   4771  C  CA    . LEU   A  1  655  ? -36.119 75.718  111.717 1.00 23.74 ? 653  LEU   A CA    1 
ATOM   4772  C  C     . LEU   A  1  655  ? -36.153 76.227  110.283 1.00 25.37 ? 653  LEU   A C     1 
ATOM   4773  O  O     . LEU   A  1  655  ? -35.616 77.303  109.995 1.00 24.48 ? 653  LEU   A O     1 
ATOM   4774  C  CB    . LEU   A  1  655  ? -34.982 74.715  111.906 1.00 23.45 ? 653  LEU   A CB    1 
ATOM   4775  C  CG    . LEU   A  1  655  ? -34.822 74.258  113.354 1.00 23.68 ? 653  LEU   A CG    1 
ATOM   4776  C  CD1   . LEU   A  1  655  ? -33.737 73.221  113.486 1.00 23.96 ? 653  LEU   A CD1   1 
ATOM   4777  C  CD2   . LEU   A  1  655  ? -34.512 75.436  114.252 1.00 28.05 ? 653  LEU   A CD2   1 
ATOM   4778  N  N     . LEU   A  1  656  ? -36.781 75.469  109.369 1.00 24.15 ? 654  LEU   A N     1 
ATOM   4779  C  CA    . LEU   A  1  656  ? -36.894 75.920  107.984 1.00 24.32 ? 654  LEU   A CA    1 
ATOM   4780  C  C     . LEU   A  1  656  ? -37.557 77.280  107.916 1.00 23.72 ? 654  LEU   A C     1 
ATOM   4781  O  O     . LEU   A  1  656  ? -37.092 78.181  107.208 1.00 25.08 ? 654  LEU   A O     1 
ATOM   4782  C  CB    . LEU   A  1  656  ? -37.728 74.942  107.158 1.00 24.58 ? 654  LEU   A CB    1 
ATOM   4783  C  CG    . LEU   A  1  656  ? -37.324 73.480  107.091 1.00 26.46 ? 654  LEU   A CG    1 
ATOM   4784  C  CD1   . LEU   A  1  656  ? -38.221 72.750  106.117 1.00 26.95 ? 654  LEU   A CD1   1 
ATOM   4785  C  CD2   . LEU   A  1  656  ? -35.874 73.361  106.704 1.00 25.24 ? 654  LEU   A CD2   1 
ATOM   4786  N  N     . GLY   A  1  657  ? -38.673 77.430  108.627 1.00 22.96 ? 655  GLY   A N     1 
ATOM   4787  C  CA    . GLY   A  1  657  ? -39.411 78.672  108.555 1.00 26.72 ? 655  GLY   A CA    1 
ATOM   4788  C  C     . GLY   A  1  657  ? -38.576 79.852  108.991 1.00 23.13 ? 655  GLY   A C     1 
ATOM   4789  O  O     . GLY   A  1  657  ? -38.648 80.929  108.399 1.00 25.53 ? 655  GLY   A O     1 
ATOM   4790  N  N     . LEU   A  1  658  ? -37.773 79.667  110.038 1.00 23.17 ? 656  LEU   A N     1 
ATOM   4791  C  CA    . LEU   A  1  658  ? -36.937 80.761  110.504 1.00 21.21 ? 656  LEU   A CA    1 
ATOM   4792  C  C     . LEU   A  1  658  ? -35.851 81.075  109.482 1.00 20.89 ? 656  LEU   A C     1 
ATOM   4793  O  O     . LEU   A  1  658  ? -35.611 82.242  109.157 1.00 22.54 ? 656  LEU   A O     1 
ATOM   4794  C  CB    . LEU   A  1  658  ? -36.331 80.400  111.858 1.00 22.37 ? 656  LEU   A CB    1 
ATOM   4795  C  CG    . LEU   A  1  658  ? -35.449 81.465  112.504 1.00 23.50 ? 656  LEU   A CG    1 
ATOM   4796  C  CD1   . LEU   A  1  658  ? -36.192 82.788  112.611 1.00 25.77 ? 656  LEU   A CD1   1 
ATOM   4797  C  CD2   . LEU   A  1  658  ? -34.987 80.989  113.872 1.00 25.53 ? 656  LEU   A CD2   1 
ATOM   4798  N  N     . ILE   A  1  659  ? -35.190 80.041  108.964 1.00 21.74 ? 657  ILE   A N     1 
ATOM   4799  C  CA    . ILE   A  1  659  ? -34.137 80.249  107.980 1.00 21.53 ? 657  ILE   A CA    1 
ATOM   4800  C  C     . ILE   A  1  659  ? -34.698 80.912  106.732 1.00 22.15 ? 657  ILE   A C     1 
ATOM   4801  O  O     . ILE   A  1  659  ? -34.087 81.826  106.167 1.00 22.23 ? 657  ILE   A O     1 
ATOM   4802  C  CB    . ILE   A  1  659  ? -33.452 78.912  107.657 1.00 21.02 ? 657  ILE   A CB    1 
ATOM   4803  C  CG1   . ILE   A  1  659  ? -32.691 78.431  108.888 1.00 22.08 ? 657  ILE   A CG1   1 
ATOM   4804  C  CG2   . ILE   A  1  659  ? -32.519 79.073  106.473 1.00 21.06 ? 657  ILE   A CG2   1 
ATOM   4805  C  CD1   . ILE   A  1  659  ? -32.352 76.982  108.844 1.00 23.62 ? 657  ILE   A CD1   1 
ATOM   4806  N  N     . ILE   A  1  660  ? -35.873 80.465  106.290 1.00 21.23 ? 658  ILE   A N     1 
ATOM   4807  C  CA    . ILE   A  1  660  ? -36.497 81.048  105.107 1.00 22.32 ? 658  ILE   A CA    1 
ATOM   4808  C  C     . ILE   A  1  660  ? -36.689 82.549  105.289 1.00 21.15 ? 658  ILE   A C     1 
ATOM   4809  O  O     . ILE   A  1  660  ? -36.361 83.348  104.404 1.00 24.22 ? 658  ILE   A O     1 
ATOM   4810  C  CB    . ILE   A  1  660  ? -37.826 80.334  104.805 1.00 19.35 ? 658  ILE   A CB    1 
ATOM   4811  C  CG1   . ILE   A  1  660  ? -37.578 78.929  104.254 1.00 21.05 ? 658  ILE   A CG1   1 
ATOM   4812  C  CG2   . ILE   A  1  660  ? -38.684 81.174  103.862 1.00 22.68 ? 658  ILE   A CG2   1 
ATOM   4813  C  CD1   . ILE   A  1  660  ? -38.859 78.107  104.177 1.00 25.20 ? 658  ILE   A CD1   1 
ATOM   4814  N  N     . ARG   A  1  661  ? -37.219 82.957  106.442 1.00 20.87 ? 659  ARG   A N     1 
ATOM   4815  C  CA    . ARG   A  1  661  ? -37.567 84.359  106.611 1.00 22.44 ? 659  ARG   A CA    1 
ATOM   4816  C  C     . ARG   A  1  661  ? -36.385 85.206  107.042 1.00 25.09 ? 659  ARG   A C     1 
ATOM   4817  O  O     . ARG   A  1  661  ? -36.312 86.384  106.678 1.00 26.05 ? 659  ARG   A O     1 
ATOM   4818  C  CB    . ARG   A  1  661  ? -38.718 84.499  107.607 1.00 25.16 ? 659  ARG   A CB    1 
ATOM   4819  C  CG    . ARG   A  1  661  ? -40.043 84.056  107.020 1.00 22.82 ? 659  ARG   A CG    1 
ATOM   4820  C  CD    . ARG   A  1  661  ? -41.150 84.028  108.061 1.00 25.16 ? 659  ARG   A CD    1 
ATOM   4821  N  NE    . ARG   A  1  661  ? -41.390 85.328  108.671 1.00 26.16 ? 659  ARG   A NE    1 
ATOM   4822  C  CZ    . ARG   A  1  661  ? -41.361 85.551  109.977 1.00 27.15 ? 659  ARG   A CZ    1 
ATOM   4823  N  NH1   . ARG   A  1  661  ? -41.057 84.591  110.834 1.00 28.15 ? 659  ARG   A NH1   1 
ATOM   4824  N  NH2   . ARG   A  1  661  ? -41.653 86.763  110.436 1.00 27.45 ? 659  ARG   A NH2   1 
ATOM   4825  N  N     . GLU   A  1  662  ? -35.471 84.646  107.836 1.00 23.60 ? 660  GLU   A N     1 
ATOM   4826  C  CA    . GLU   A  1  662  ? -34.348 85.440  108.318 1.00 24.46 ? 660  GLU   A CA    1 
ATOM   4827  C  C     . GLU   A  1  662  ? -33.261 85.590  107.260 1.00 23.66 ? 660  GLU   A C     1 
ATOM   4828  O  O     . GLU   A  1  662  ? -32.653 86.658  107.143 1.00 25.85 ? 660  GLU   A O     1 
ATOM   4829  C  CB    . GLU   A  1  662  ? -33.767 84.824  109.591 1.00 25.59 ? 660  GLU   A CB    1 
ATOM   4830  C  CG    . GLU   A  1  662  ? -32.654 85.661  110.201 1.00 27.03 ? 660  GLU   A CG    1 
ATOM   4831  C  CD    . GLU   A  1  662  ? -32.115 85.093  111.498 1.00 25.91 ? 660  GLU   A CD    1 
ATOM   4832  O  OE1   . GLU   A  1  662  ? -32.149 83.857  111.678 1.00 26.22 ? 660  GLU   A OE1   1 
ATOM   4833  O  OE2   . GLU   A  1  662  ? -31.658 85.892  112.336 1.00 26.74 ? 660  GLU   A OE2   1 
ATOM   4834  N  N     . ALA   A  1  663  ? -33.015 84.550  106.468 1.00 22.20 ? 661  ALA   A N     1 
ATOM   4835  C  CA    . ALA   A  1  663  ? -31.816 84.512  105.639 1.00 21.41 ? 661  ALA   A CA    1 
ATOM   4836  C  C     . ALA   A  1  663  ? -32.099 84.510  104.143 1.00 23.14 ? 661  ALA   A C     1 
ATOM   4837  O  O     . ALA   A  1  663  ? -31.166 84.328  103.352 1.00 27.13 ? 661  ALA   A O     1 
ATOM   4838  C  CB    . ALA   A  1  663  ? -30.927 83.324  106.021 1.00 24.23 ? 661  ALA   A CB    1 
ATOM   4839  N  N     . GLY   A  1  664  ? -33.351 84.696  103.732 1.00 25.95 ? 662  GLY   A N     1 
ATOM   4840  C  CA    . GLY   A  1  664  ? -33.647 84.746  102.309 1.00 26.46 ? 662  GLY   A CA    1 
ATOM   4841  C  C     . GLY   A  1  664  ? -33.541 83.422  101.594 1.00 24.45 ? 662  GLY   A C     1 
ATOM   4842  O  O     . GLY   A  1  664  ? -33.320 83.395  100.381 1.00 26.12 ? 662  GLY   A O     1 
ATOM   4843  N  N     . LYS   A  1  665  ? -33.695 82.315  102.308 1.00 21.82 ? 663  LYS   A N     1 
ATOM   4844  C  CA    . LYS   A  1  665  ? -33.516 81.000  101.717 1.00 21.65 ? 663  LYS   A CA    1 
ATOM   4845  C  C     . LYS   A  1  665  ? -34.840 80.435  101.232 1.00 20.33 ? 663  LYS   A C     1 
ATOM   4846  O  O     . LYS   A  1  665  ? -35.884 80.637  101.854 1.00 20.21 ? 663  LYS   A O     1 
ATOM   4847  C  CB    . LYS   A  1  665  ? -32.934 80.033  102.741 1.00 22.72 ? 663  LYS   A CB    1 
ATOM   4848  C  CG    . LYS   A  1  665  ? -31.631 80.489  103.356 1.00 23.97 ? 663  LYS   A CG    1 
ATOM   4849  C  CD    . LYS   A  1  665  ? -30.562 80.699  102.310 1.00 25.53 ? 663  LYS   A CD    1 
ATOM   4850  C  CE    . LYS   A  1  665  ? -29.203 80.876  102.973 1.00 28.10 ? 663  LYS   A CE    1 
ATOM   4851  N  NZ    . LYS   A  1  665  ? -28.148 81.366  102.022 1.00 29.02 ? 663  LYS   A NZ    1 
ATOM   4852  N  N     . SER   A  1  666  ? -34.777 79.700  100.128 1.00 21.57 ? 664  SER   A N     1 
ATOM   4853  C  CA    . SER   A  1  666  ? -35.914 78.896  99.723  1.00 21.02 ? 664  SER   A CA    1 
ATOM   4854  C  C     . SER   A  1  666  ? -36.055 77.693  100.650 1.00 21.66 ? 664  SER   A C     1 
ATOM   4855  O  O     . SER   A  1  666  ? -35.143 77.350  101.410 1.00 22.53 ? 664  SER   A O     1 
ATOM   4856  C  CB    . SER   A  1  666  ? -35.690 78.369  98.313  1.00 22.84 ? 664  SER   A CB    1 
ATOM   4857  O  OG    . SER   A  1  666  ? -34.684 77.378  98.340  1.00 24.08 ? 664  SER   A OG    1 
ATOM   4858  N  N     . ALA   A  1  667  ? -37.217 77.042  100.584 1.00 23.70 ? 665  ALA   A N     1 
ATOM   4859  C  CA    . ALA   A  1  667  ? -37.445 75.877  101.431 1.00 21.47 ? 665  ALA   A CA    1 
ATOM   4860  C  C     . ALA   A  1  667  ? -36.431 74.774  101.142 1.00 23.74 ? 665  ALA   A C     1 
ATOM   4861  O  O     . ALA   A  1  667  ? -35.888 74.171  102.073 1.00 21.22 ? 665  ALA   A O     1 
ATOM   4862  C  CB    . ALA   A  1  667  ? -38.879 75.369  101.260 1.00 24.91 ? 665  ALA   A CB    1 
ATOM   4863  N  N     . LEU   A  1  668  ? -36.173 74.486  99.865  1.00 21.45 ? 666  LEU   A N     1 
ATOM   4864  C  CA    . LEU   A  1  668  ? -35.175 73.477  99.518  1.00 22.70 ? 666  LEU   A CA    1 
ATOM   4865  C  C     . LEU   A  1  668  ? -33.836 73.804  100.152 1.00 24.13 ? 666  LEU   A C     1 
ATOM   4866  O  O     . LEU   A  1  668  ? -33.163 72.929  100.711 1.00 23.22 ? 666  LEU   A O     1 
ATOM   4867  C  CB    . LEU   A  1  668  ? -34.998 73.409  98.003  1.00 25.17 ? 666  LEU   A CB    1 
ATOM   4868  C  CG    . LEU   A  1  668  ? -35.920 72.489  97.225  1.00 34.21 ? 666  LEU   A CG    1 
ATOM   4869  C  CD1   . LEU   A  1  668  ? -35.512 72.543  95.763  1.00 29.52 ? 666  LEU   A CD1   1 
ATOM   4870  C  CD2   . LEU   A  1  668  ? -35.811 71.082  97.779  1.00 34.42 ? 666  LEU   A CD2   1 
ATOM   4871  N  N     . ASN   A  1  669  ? -33.425 75.065  100.063 1.00 21.77 ? 667  ASN   A N     1 
ATOM   4872  C  CA    . ASN   A  1  669  ? -32.123 75.434  100.599 1.00 23.63 ? 667  ASN   A CA    1 
ATOM   4873  C  C     . ASN   A  1  669  ? -32.124 75.429  102.120 1.00 22.80 ? 667  ASN   A C     1 
ATOM   4874  O  O     . ASN   A  1  669  ? -31.097 75.123  102.735 1.00 22.42 ? 667  ASN   A O     1 
ATOM   4875  C  CB    . ASN   A  1  669  ? -31.698 76.782  100.033 1.00 25.66 ? 667  ASN   A CB    1 
ATOM   4876  C  CG    . ASN   A  1  669  ? -31.413 76.709  98.536  1.00 26.97 ? 667  ASN   A CG    1 
ATOM   4877  O  OD1   . ASN   A  1  669  ? -31.025 75.659  98.021  1.00 37.81 ? 667  ASN   A OD1   1 
ATOM   4878  N  ND2   . ASN   A  1  669  ? -31.603 77.815  97.838  1.00 32.85 ? 667  ASN   A ND2   1 
ATOM   4879  N  N     . ALA   A  1  670  ? -33.262 75.734  102.742 1.00 22.05 ? 668  ALA   A N     1 
ATOM   4880  C  CA    . ALA   A  1  670  ? -33.340 75.651  104.192 1.00 21.84 ? 668  ALA   A CA    1 
ATOM   4881  C  C     . ALA   A  1  670  ? -33.286 74.204  104.659 1.00 20.24 ? 668  ALA   A C     1 
ATOM   4882  O  O     . ALA   A  1  670  ? -32.680 73.901  105.695 1.00 21.39 ? 668  ALA   A O     1 
ATOM   4883  C  CB    . ALA   A  1  670  ? -34.614 76.334  104.679 1.00 22.40 ? 668  ALA   A CB    1 
ATOM   4884  N  N     . ILE   A  1  671  ? -33.919 73.295  103.920 1.00 20.46 ? 669  ILE   A N     1 
ATOM   4885  C  CA    . ILE   A  1  671  ? -33.826 71.878  104.256 1.00 19.58 ? 669  ILE   A CA    1 
ATOM   4886  C  C     . ILE   A  1  671  ? -32.375 71.428  104.221 1.00 22.62 ? 669  ILE   A C     1 
ATOM   4887  O  O     . ILE   A  1  671  ? -31.898 70.754  105.140 1.00 22.36 ? 669  ILE   A O     1 
ATOM   4888  C  CB    . ILE   A  1  671  ? -34.693 71.031  103.310 1.00 21.96 ? 669  ILE   A CB    1 
ATOM   4889  C  CG1   . ILE   A  1  671  ? -36.176 71.307  103.537 1.00 22.22 ? 669  ILE   A CG1   1 
ATOM   4890  C  CG2   . ILE   A  1  671  ? -34.388 69.557  103.513 1.00 25.68 ? 669  ILE   A CG2   1 
ATOM   4891  C  CD1   . ILE   A  1  671  ? -37.065 70.706  102.452 1.00 25.19 ? 669  ILE   A CD1   1 
ATOM   4892  N  N     . ALA   A  1  672  ? -31.659 71.786  103.150 1.00 20.80 ? 670  ALA   A N     1 
ATOM   4893  C  CA    . ALA   A  1  672  ? -30.251 71.431  103.047 1.00 20.25 ? 670  ALA   A CA    1 
ATOM   4894  C  C     . ALA   A  1  672  ? -29.453 72.038  104.187 1.00 20.57 ? 670  ALA   A C     1 
ATOM   4895  O  O     . ALA   A  1  672  ? -28.534 71.405  104.714 1.00 21.20 ? 670  ALA   A O     1 
ATOM   4896  C  CB    . ALA   A  1  672  ? -29.692 71.904  101.707 1.00 21.92 ? 670  ALA   A CB    1 
ATOM   4897  N  N     . GLU   A  1  673  ? -29.790 73.265  104.578 1.00 20.48 ? 671  GLU   A N     1 
ATOM   4898  C  CA    . GLU   A  1  673  ? -29.079 73.935  105.661 1.00 21.36 ? 671  GLU   A CA    1 
ATOM   4899  C  C     . GLU   A  1  673  ? -29.236 73.170  106.969 1.00 20.43 ? 671  GLU   A C     1 
ATOM   4900  O  O     . GLU   A  1  673  ? -28.253 72.905  107.673 1.00 20.79 ? 671  GLU   A O     1 
ATOM   4901  C  CB    . GLU   A  1  673  ? -29.644 75.345  105.810 1.00 22.42 ? 671  GLU   A CB    1 
ATOM   4902  C  CG    . GLU   A  1  673  ? -29.032 76.147  106.938 1.00 25.82 ? 671  GLU   A CG    1 
ATOM   4903  C  CD    . GLU   A  1  673  ? -27.741 76.804  106.529 1.00 26.77 ? 671  GLU   A CD    1 
ATOM   4904  O  OE1   . GLU   A  1  673  ? -27.394 76.768  105.324 1.00 30.17 ? 671  GLU   A OE1   1 
ATOM   4905  O  OE2   . GLU   A  1  673  ? -27.065 77.357  107.415 1.00 24.72 ? 671  GLU   A OE2   1 
ATOM   4906  N  N     . VAL   A  1  674  ? -30.467 72.797  107.308 1.00 19.56 ? 672  VAL   A N     1 
ATOM   4907  C  CA    . VAL   A  1  674  ? -30.703 72.063  108.545 1.00 20.02 ? 672  VAL   A CA    1 
ATOM   4908  C  C     . VAL   A  1  674  ? -30.086 70.671  108.469 1.00 19.96 ? 672  VAL   A C     1 
ATOM   4909  O  O     . VAL   A  1  674  ? -29.483 70.192  109.440 1.00 19.47 ? 672  VAL   A O     1 
ATOM   4910  C  CB    . VAL   A  1  674  ? -32.206 72.032  108.887 1.00 20.53 ? 672  VAL   A CB    1 
ATOM   4911  C  CG1   . VAL   A  1  674  ? -32.443 71.260  110.172 1.00 21.16 ? 672  VAL   A CG1   1 
ATOM   4912  C  CG2   . VAL   A  1  674  ? -32.767 73.452  109.008 1.00 21.54 ? 672  VAL   A CG2   1 
ATOM   4913  N  N     . ARG   A  1  675  ? -30.194 70.010  107.314 1.00 19.02 ? 673  ARG   A N     1 
ATOM   4914  C  CA    . ARG   A  1  675  ? -29.545 68.716  107.172 1.00 17.63 ? 673  ARG   A CA    1 
ATOM   4915  C  C     . ARG   A  1  675  ? -28.053 68.834  107.407 1.00 17.95 ? 673  ARG   A C     1 
ATOM   4916  O  O     . ARG   A  1  675  ? -27.468 67.988  108.082 1.00 19.31 ? 673  ARG   A O     1 
ATOM   4917  C  CB    . ARG   A  1  675  ? -29.786 68.135  105.791 1.00 18.06 ? 673  ARG   A CB    1 
ATOM   4918  C  CG    . ARG   A  1  675  ? -31.200 67.681  105.569 1.00 18.50 ? 673  ARG   A CG    1 
ATOM   4919  C  CD    . ARG   A  1  675  ? -31.247 66.908  104.277 1.00 19.93 ? 673  ARG   A CD    1 
ATOM   4920  N  NE    . ARG   A  1  675  ? -30.509 65.658  104.396 1.00 19.86 ? 673  ARG   A NE    1 
ATOM   4921  C  CZ    . ARG   A  1  675  ? -30.137 64.911  103.367 1.00 20.95 ? 673  ARG   A CZ    1 
ATOM   4922  N  NH1   . ARG   A  1  675  ? -30.395 65.275  102.122 1.00 20.74 ? 673  ARG   A NH1   1 
ATOM   4923  N  NH2   . ARG   A  1  675  ? -29.484 63.773  103.594 1.00 20.11 ? 673  ARG   A NH2   1 
ATOM   4924  N  N     . GLU   A  1  676  ? -27.426 69.882  106.868 1.00 18.06 ? 674  GLU   A N     1 
ATOM   4925  C  CA    . GLU   A  1  676  ? -25.988 70.021  107.053 1.00 18.67 ? 674  GLU   A CA    1 
ATOM   4926  C  C     . GLU   A  1  676  ? -25.641 70.209  108.523 1.00 18.70 ? 674  GLU   A C     1 
ATOM   4927  O  O     . GLU   A  1  676  ? -24.644 69.659  109.006 1.00 18.26 ? 674  GLU   A O     1 
ATOM   4928  C  CB    . GLU   A  1  676  ? -25.445 71.165  106.207 1.00 18.76 ? 674  GLU   A CB    1 
ATOM   4929  C  CG    . GLU   A  1  676  ? -23.939 71.222  106.290 1.00 23.77 ? 674  GLU   A CG    1 
ATOM   4930  C  CD    . GLU   A  1  676  ? -23.295 71.923  105.125 1.00 32.89 ? 674  GLU   A CD    1 
ATOM   4931  O  OE1   . GLU   A  1  676  ? -23.761 73.021  104.750 1.00 46.06 ? 674  GLU   A OE1   1 
ATOM   4932  O  OE2   . GLU   A  1  676  ? -22.314 71.361  104.585 1.00 38.65 ? 674  GLU   A OE2   1 
ATOM   4933  N  N     . ALA   A  1  677  ? -26.449 70.979  109.253 1.00 18.25 ? 675  ALA   A N     1 
ATOM   4934  C  CA    . ALA   A  1  677  ? -26.197 71.149  110.678 1.00 19.55 ? 675  ALA   A CA    1 
ATOM   4935  C  C     . ALA   A  1  677  ? -26.280 69.812  111.400 1.00 19.83 ? 675  ALA   A C     1 
ATOM   4936  O  O     . ALA   A  1  677  ? -25.420 69.481  112.226 1.00 18.93 ? 675  ALA   A O     1 
ATOM   4937  C  CB    . ALA   A  1  677  ? -27.191 72.151  111.263 1.00 18.93 ? 675  ALA   A CB    1 
ATOM   4938  N  N     . ILE   A  1  678  ? -27.321 69.031  111.099 1.00 19.76 ? 676  ILE   A N     1 
ATOM   4939  C  CA    . ILE   A  1  678  ? -27.481 67.710  111.691 1.00 19.33 ? 676  ILE   A CA    1 
ATOM   4940  C  C     . ILE   A  1  678  ? -26.275 66.845  111.374 1.00 19.09 ? 676  ILE   A C     1 
ATOM   4941  O  O     . ILE   A  1  678  ? -25.735 66.153  112.248 1.00 19.72 ? 676  ILE   A O     1 
ATOM   4942  C  CB    . ILE   A  1  678  ? -28.785 67.077  111.178 1.00 20.70 ? 676  ILE   A CB    1 
ATOM   4943  C  CG1   . ILE   A  1  678  ? -29.988 67.857  111.706 1.00 21.10 ? 676  ILE   A CG1   1 
ATOM   4944  C  CG2   . ILE   A  1  678  ? -28.884 65.605  111.556 1.00 19.84 ? 676  ILE   A CG2   1 
ATOM   4945  C  CD1   . ILE   A  1  678  ? -31.267 67.529  110.961 1.00 19.27 ? 676  ILE   A CD1   1 
ATOM   4946  N  N     . ASP   A  1  679  ? -25.832 66.883  110.118 1.00 18.05 ? 677  ASP   A N     1 
ATOM   4947  C  CA    . ASP   A  1  679  ? -24.697 66.076  109.691 1.00 17.78 ? 677  ASP   A CA    1 
ATOM   4948  C  C     . ASP   A  1  679  ? -23.412 66.505  110.381 1.00 19.36 ? 677  ASP   A C     1 
ATOM   4949  O  O     . ASP   A  1  679  ? -22.613 65.652  110.772 1.00 18.95 ? 677  ASP   A O     1 
ATOM   4950  C  CB    . ASP   A  1  679  ? -24.546 66.157  108.174 1.00 16.96 ? 677  ASP   A CB    1 
ATOM   4951  C  CG    . ASP   A  1  679  ? -25.704 65.522  107.432 1.00 21.22 ? 677  ASP   A CG    1 
ATOM   4952  O  OD1   . ASP   A  1  679  ? -26.310 64.584  107.963 1.00 22.21 ? 677  ASP   A OD1   1 
ATOM   4953  O  OD2   . ASP   A  1  679  ? -25.962 65.931  106.285 1.00 23.07 ? 677  ASP   A OD2   1 
ATOM   4954  N  N     . PHE   A  1  680  ? -23.179 67.815  110.531 1.00 17.97 ? 678  PHE   A N     1 
ATOM   4955  C  CA    . PHE   A  1  680  ? -21.994 68.261  111.266 1.00 18.73 ? 678  PHE   A CA    1 
ATOM   4956  C  C     . PHE   A  1  680  ? -22.005 67.705  112.677 1.00 19.15 ? 678  PHE   A C     1 
ATOM   4957  O  O     . PHE   A  1  680  ? -20.996 67.185  113.167 1.00 18.96 ? 678  PHE   A O     1 
ATOM   4958  C  CB    . PHE   A  1  680  ? -21.953 69.785  111.363 1.00 18.70 ? 678  PHE   A CB    1 
ATOM   4959  C  CG    . PHE   A  1  680  ? -21.326 70.462  110.196 1.00 18.25 ? 678  PHE   A CG    1 
ATOM   4960  C  CD1   . PHE   A  1  680  ? -20.094 70.055  109.709 1.00 18.39 ? 678  PHE   A CD1   1 
ATOM   4961  C  CD2   . PHE   A  1  680  ? -21.965 71.532  109.592 1.00 20.32 ? 678  PHE   A CD2   1 
ATOM   4962  C  CE1   . PHE   A  1  680  ? -19.517 70.698  108.647 1.00 18.35 ? 678  PHE   A CE1   1 
ATOM   4963  C  CE2   . PHE   A  1  680  ? -21.399 72.178  108.526 1.00 19.50 ? 678  PHE   A CE2   1 
ATOM   4964  C  CZ    . PHE   A  1  680  ? -20.177 71.764  108.040 1.00 18.94 ? 678  PHE   A CZ    1 
ATOM   4965  N  N     . LEU   A  1  681  ? -23.136 67.851  113.365 1.00 18.67 ? 679  LEU   A N     1 
ATOM   4966  C  CA    . LEU   A  1  681  ? -23.237 67.352  114.730 1.00 18.23 ? 679  LEU   A CA    1 
ATOM   4967  C  C     . LEU   A  1  681  ? -22.915 65.865  114.791 1.00 19.94 ? 679  LEU   A C     1 
ATOM   4968  O  O     . LEU   A  1  681  ? -22.106 65.423  115.616 1.00 20.11 ? 679  LEU   A O     1 
ATOM   4969  C  CB    . LEU   A  1  681  ? -24.641 67.626  115.273 1.00 20.57 ? 679  LEU   A CB    1 
ATOM   4970  C  CG    . LEU   A  1  681  ? -24.955 69.104  115.501 1.00 20.83 ? 679  LEU   A CG    1 
ATOM   4971  C  CD1   . LEU   A  1  681  ? -26.464 69.358  115.513 1.00 21.03 ? 679  LEU   A CD1   1 
ATOM   4972  C  CD2   . LEU   A  1  681  ? -24.326 69.586  116.795 1.00 21.44 ? 679  LEU   A CD2   1 
ATOM   4973  N  N     . ARG   A  1  682  ? -23.529 65.077  113.910 1.00 18.93 ? 680  ARG   A N     1 
ATOM   4974  C  CA    . ARG   A  1  682  ? -23.327 63.635  113.970 1.00 18.26 ? 680  ARG   A CA    1 
ATOM   4975  C  C     . ARG   A  1  682  ? -21.940 63.237  113.487 1.00 19.48 ? 680  ARG   A C     1 
ATOM   4976  O  O     . ARG   A  1  682  ? -21.356 62.287  114.019 1.00 19.75 ? 680  ARG   A O     1 
ATOM   4977  C  CB    . ARG   A  1  682  ? -24.401 62.919  113.163 1.00 17.73 ? 680  ARG   A CB    1 
ATOM   4978  C  CG    . ARG   A  1  682  ? -25.756 63.035  113.781 1.00 19.65 ? 680  ARG   A CG    1 
ATOM   4979  C  CD    . ARG   A  1  682  ? -26.775 62.347  112.929 1.00 20.92 ? 680  ARG   A CD    1 
ATOM   4980  N  NE    . ARG   A  1  682  ? -28.060 62.349  113.604 1.00 22.62 ? 680  ARG   A NE    1 
ATOM   4981  C  CZ    . ARG   A  1  682  ? -29.215 62.181  112.980 1.00 22.81 ? 680  ARG   A CZ    1 
ATOM   4982  N  NH1   . ARG   A  1  682  ? -29.271 61.988  111.676 1.00 22.44 ? 680  ARG   A NH1   1 
ATOM   4983  N  NH2   . ARG   A  1  682  ? -30.341 62.217  113.687 1.00 24.70 ? 680  ARG   A NH2   1 
ATOM   4984  N  N     . TYR   A  1  683  ? -21.397 63.957  112.508 1.00 18.24 ? 681  TYR   A N     1 
ATOM   4985  C  CA    . TYR   A  1  683  ? -20.059 63.650  112.014 1.00 16.60 ? 681  TYR   A CA    1 
ATOM   4986  C  C     . TYR   A  1  683  ? -19.005 63.959  113.065 1.00 20.44 ? 681  TYR   A C     1 
ATOM   4987  O  O     . TYR   A  1  683  ? -18.134 63.127  113.347 1.00 19.10 ? 681  TYR   A O     1 
ATOM   4988  C  CB    . TYR   A  1  683  ? -19.794 64.435  110.730 1.00 17.20 ? 681  TYR   A CB    1 
ATOM   4989  C  CG    . TYR   A  1  683  ? -18.415 64.218  110.182 1.00 17.88 ? 681  TYR   A CG    1 
ATOM   4990  C  CD1   . TYR   A  1  683  ? -18.110 63.063  109.486 1.00 17.88 ? 681  TYR   A CD1   1 
ATOM   4991  C  CD2   . TYR   A  1  683  ? -17.426 65.167  110.364 1.00 18.62 ? 681  TYR   A CD2   1 
ATOM   4992  C  CE1   . TYR   A  1  683  ? -16.838 62.853  108.986 1.00 17.50 ? 681  TYR   A CE1   1 
ATOM   4993  C  CE2   . TYR   A  1  683  ? -16.155 64.972  109.884 1.00 17.95 ? 681  TYR   A CE2   1 
ATOM   4994  C  CZ    . TYR   A  1  683  ? -15.872 63.809  109.195 1.00 17.72 ? 681  TYR   A CZ    1 
ATOM   4995  O  OH    . TYR   A  1  683  ? -14.605 63.592  108.696 1.00 18.87 ? 681  TYR   A OH    1 
ATOM   4996  N  N     . TYR   A  1  684  ? -19.059 65.154  113.659 1.00 18.26 ? 682  TYR   A N     1 
ATOM   4997  C  CA    . TYR   A  1  684  ? -18.049 65.472  114.660 1.00 17.99 ? 682  TYR   A CA    1 
ATOM   4998  C  C     . TYR   A  1  684  ? -18.213 64.606  115.895 1.00 20.22 ? 682  TYR   A C     1 
ATOM   4999  O  O     . TYR   A  1  684  ? -17.222 64.273  116.550 1.00 20.64 ? 682  TYR   A O     1 
ATOM   5000  C  CB    . TYR   A  1  684  ? -18.049 66.954  115.022 1.00 18.26 ? 682  TYR   A CB    1 
ATOM   5001  C  CG    . TYR   A  1  684  ? -17.687 67.850  113.865 1.00 17.58 ? 682  TYR   A CG    1 
ATOM   5002  C  CD1   . TYR   A  1  684  ? -16.633 67.540  113.026 1.00 19.08 ? 682  TYR   A CD1   1 
ATOM   5003  C  CD2   . TYR   A  1  684  ? -18.408 69.004  113.611 1.00 18.22 ? 682  TYR   A CD2   1 
ATOM   5004  C  CE1   . TYR   A  1  684  ? -16.306 68.358  111.964 1.00 18.85 ? 682  TYR   A CE1   1 
ATOM   5005  C  CE2   . TYR   A  1  684  ? -18.089 69.826  112.557 1.00 17.88 ? 682  TYR   A CE2   1 
ATOM   5006  C  CZ    . TYR   A  1  684  ? -17.041 69.501  111.729 1.00 18.87 ? 682  TYR   A CZ    1 
ATOM   5007  O  OH    . TYR   A  1  684  ? -16.721 70.323  110.677 1.00 19.32 ? 682  TYR   A OH    1 
ATOM   5008  N  N     . ALA   A  1  685  ? -19.440 64.203  116.219 1.00 18.40 ? 683  ALA   A N     1 
ATOM   5009  C  CA    . ALA   A  1  685  ? -19.625 63.245  117.302 1.00 19.33 ? 683  ALA   A CA    1 
ATOM   5010  C  C     . ALA   A  1  685  ? -18.925 61.927  116.988 1.00 21.13 ? 683  ALA   A C     1 
ATOM   5011  O  O     . ALA   A  1  685  ? -18.213 61.372  117.832 1.00 19.67 ? 683  ALA   A O     1 
ATOM   5012  C  CB    . ALA   A  1  685  ? -21.115 63.022  117.554 1.00 19.11 ? 683  ALA   A CB    1 
ATOM   5013  N  N     . GLU   A  1  686  ? -19.126 61.405  115.780 1.00 20.84 ? 684  GLU   A N     1 
ATOM   5014  C  CA    . GLU   A  1  686  ? -18.505 60.133  115.432 1.00 20.45 ? 684  GLU   A CA    1 
ATOM   5015  C  C     . GLU   A  1  686  ? -16.991 60.270  115.354 1.00 19.59 ? 684  GLU   A C     1 
ATOM   5016  O  O     . GLU   A  1  686  ? -16.258 59.404  115.849 1.00 20.69 ? 684  GLU   A O     1 
ATOM   5017  C  CB    . GLU   A  1  686  ? -19.076 59.598  114.120 1.00 24.00 ? 684  GLU   A CB    1 
ATOM   5018  C  CG    . GLU   A  1  686  ? -18.373 58.339  113.604 1.00 24.99 ? 684  GLU   A CG    1 
ATOM   5019  C  CD    . GLU   A  1  686  ? -18.453 57.142  114.558 1.00 30.70 ? 684  GLU   A CD    1 
ATOM   5020  O  OE1   . GLU   A  1  686  ? -19.287 57.135  115.493 1.00 28.65 ? 684  GLU   A OE1   1 
ATOM   5021  O  OE2   . GLU   A  1  686  ? -17.670 56.186  114.364 1.00 31.56 ? 684  GLU   A OE2   1 
ATOM   5022  N  N     . GLN   A  1  687  ? -16.505 61.354  114.746 1.00 19.01 ? 685  GLN   A N     1 
ATOM   5023  C  CA    . GLN   A  1  687  ? -15.062 61.558  114.688 1.00 19.16 ? 685  GLN   A CA    1 
ATOM   5024  C  C     . GLN   A  1  687  ? -14.471 61.635  116.088 1.00 20.95 ? 685  GLN   A C     1 
ATOM   5025  O  O     . GLN   A  1  687  ? -13.368 61.133  116.339 1.00 21.59 ? 685  GLN   A O     1 
ATOM   5026  C  CB    . GLN   A  1  687  ? -14.748 62.823  113.898 1.00 19.39 ? 685  GLN   A CB    1 
ATOM   5027  C  CG    . GLN   A  1  687  ? -15.080 62.700  112.420 1.00 18.34 ? 685  GLN   A CG    1 
ATOM   5028  C  CD    . GLN   A  1  687  ? -14.345 61.545  111.772 1.00 23.73 ? 685  GLN   A CD    1 
ATOM   5029  O  OE1   . GLN   A  1  687  ? -13.120 61.472  111.832 1.00 22.16 ? 685  GLN   A OE1   1 
ATOM   5030  N  NE2   . GLN   A  1  687  ? -15.089 60.632  111.161 1.00 26.19 ? 685  GLN   A NE2   1 
ATOM   5031  N  N     . THR   A  1  688  ? -15.197 62.245  117.022 1.00 19.09 ? 686  THR   A N     1 
ATOM   5032  C  CA    . THR   A  1  688  ? -14.729 62.284  118.401 1.00 20.41 ? 686  THR   A CA    1 
ATOM   5033  C  C     . THR   A  1  688  ? -14.626 60.884  118.974 1.00 20.27 ? 686  THR   A C     1 
ATOM   5034  O  O     . THR   A  1  688  ? -13.604 60.517  119.571 1.00 21.65 ? 686  THR   A O     1 
ATOM   5035  C  CB    . THR   A  1  688  ? -15.673 63.138  119.244 1.00 20.69 ? 686  THR   A CB    1 
ATOM   5036  O  OG1   . THR   A  1  688  ? -15.539 64.500  118.843 1.00 21.58 ? 686  THR   A OG1   1 
ATOM   5037  C  CG2   . THR   A  1  688  ? -15.321 63.014  120.732 1.00 22.52 ? 686  THR   A CG2   1 
ATOM   5038  N  N     . ARG   A  1  689  ? -15.675 60.082  118.797 1.00 22.13 ? 687  ARG   A N     1 
ATOM   5039  C  CA    . ARG   A  1  689  ? -15.666 58.720  119.310 1.00 23.86 ? 687  ARG   A CA    1 
ATOM   5040  C  C     . ARG   A  1  689  ? -14.568 57.886  118.677 1.00 23.51 ? 687  ARG   A C     1 
ATOM   5041  O  O     . ARG   A  1  689  ? -14.117 56.917  119.293 1.00 24.27 ? 687  ARG   A O     1 
ATOM   5042  C  CB    . ARG   A  1  689  ? -17.014 58.047  119.074 1.00 23.31 ? 687  ARG   A CB    1 
ATOM   5043  C  CG    . ARG   A  1  689  ? -18.142 58.631  119.909 1.00 25.85 ? 687  ARG   A CG    1 
ATOM   5044  C  CD    . ARG   A  1  689  ? -19.389 57.787  119.772 1.00 27.34 ? 687  ARG   A CD    1 
ATOM   5045  N  NE    . ARG   A  1  689  ? -19.940 57.866  118.428 1.00 27.39 ? 687  ARG   A NE    1 
ATOM   5046  C  CZ    . ARG   A  1  689  ? -20.933 58.675  118.080 1.00 27.74 ? 687  ARG   A CZ    1 
ATOM   5047  N  NH1   . ARG   A  1  689  ? -21.488 59.500  118.953 1.00 29.02 ? 687  ARG   A NH1   1 
ATOM   5048  N  NH2   . ARG   A  1  689  ? -21.383 58.649  116.830 1.00 27.01 ? 687  ARG   A NH2   1 
ATOM   5049  N  N     . ARG   A  1  690  ? -14.132 58.243  117.468 1.00 20.25 ? 688  ARG   A N     1 
ATOM   5050  C  CA    . ARG   A  1  690  ? -13.028 57.541  116.831 1.00 21.75 ? 688  ARG   A CA    1 
ATOM   5051  C  C     . ARG   A  1  690  ? -11.664 57.988  117.333 1.00 23.96 ? 688  ARG   A C     1 
ATOM   5052  O  O     . ARG   A  1  690  ? -10.698 57.237  117.170 1.00 23.11 ? 688  ARG   A O     1 
ATOM   5053  C  CB    . ARG   A  1  690  ? -13.069 57.745  115.316 1.00 21.54 ? 688  ARG   A CB    1 
ATOM   5054  C  CG    . ARG   A  1  690  ? -14.292 57.136  114.659 1.00 23.88 ? 688  ARG   A CG    1 
ATOM   5055  C  CD    . ARG   A  1  690  ? -14.213 55.616  114.584 1.00 24.01 ? 688  ARG   A CD    1 
ATOM   5056  N  NE    . ARG   A  1  690  ? -13.071 55.157  113.794 1.00 26.72 ? 688  ARG   A NE    1 
ATOM   5057  C  CZ    . ARG   A  1  690  ? -12.039 54.489  114.287 1.00 28.79 ? 688  ARG   A CZ    1 
ATOM   5058  N  NH1   . ARG   A  1  690  ? -11.960 54.184  115.576 1.00 27.18 ? 688  ARG   A NH1   1 
ATOM   5059  N  NH2   . ARG   A  1  690  ? -11.063 54.109  113.467 1.00 25.61 ? 688  ARG   A NH2   1 
ATOM   5060  N  N     . THR   A  1  691  ? -11.542 59.189  117.910 1.00 21.50 ? 689  THR   A N     1 
ATOM   5061  C  CA    . THR   A  1  691  ? -10.199 59.737  118.097 1.00 22.52 ? 689  THR   A CA    1 
ATOM   5062  C  C     . THR   A  1  691  ? -9.832  60.221  119.493 1.00 23.91 ? 689  THR   A C     1 
ATOM   5063  O  O     . THR   A  1  691  ? -8.741  59.912  119.978 1.00 26.67 ? 689  THR   A O     1 
ATOM   5064  C  CB    . THR   A  1  691  ? -9.923  60.888  117.129 1.00 20.63 ? 689  THR   A CB    1 
ATOM   5065  O  OG1   . THR   A  1  691  ? -10.922 61.903  117.282 1.00 22.77 ? 689  THR   A OG1   1 
ATOM   5066  C  CG2   . THR   A  1  691  ? -9.925  60.395  115.693 1.00 21.92 ? 689  THR   A CG2   1 
ATOM   5067  N  N     . LEU   A  1  692  ? -10.693 60.997  120.146 1.00 21.93 ? 690  LEU   A N     1 
ATOM   5068  C  CA    . LEU   A  1  692  ? -10.229 61.836  121.245 1.00 23.73 ? 690  LEU   A CA    1 
ATOM   5069  C  C     . LEU   A  1  692  ? -10.019 61.047  122.531 1.00 23.41 ? 690  LEU   A C     1 
ATOM   5070  O  O     . LEU   A  1  692  ? -10.898 60.301  122.973 1.00 26.45 ? 690  LEU   A O     1 
ATOM   5071  C  CB    . LEU   A  1  692  ? -11.186 63.003  121.476 1.00 24.45 ? 690  LEU   A CB    1 
ATOM   5072  C  CG    . LEU   A  1  692  ? -11.202 64.004  120.315 1.00 23.81 ? 690  LEU   A CG    1 
ATOM   5073  C  CD1   . LEU   A  1  692  ? -11.968 65.247  120.717 1.00 26.82 ? 690  LEU   A CD1   1 
ATOM   5074  C  CD2   . LEU   A  1  692  ? -9.793  64.368  119.882 1.00 26.61 ? 690  LEU   A CD2   1 
ATOM   5075  N  N     . GLY   A  1  693  ? -8.843  61.225  123.122 1.00 23.66 ? 691  GLY   A N     1 
ATOM   5076  C  CA    . GLY   A  1  693  ? -8.506  60.617  124.384 1.00 27.20 ? 691  GLY   A CA    1 
ATOM   5077  C  C     . GLY   A  1  693  ? -7.889  61.622  125.336 1.00 29.69 ? 691  GLY   A C     1 
ATOM   5078  O  O     . GLY   A  1  693  ? -7.816  62.822  125.049 1.00 30.28 ? 691  GLY   A O     1 
ATOM   5079  N  N     . PRO   A  1  694  ? -7.418  61.141  126.488 1.00 32.09 ? 692  PRO   A N     1 
ATOM   5080  C  CA    . PRO   A  1  694  ? -6.913  62.063  127.524 1.00 31.69 ? 692  PRO   A CA    1 
ATOM   5081  C  C     . PRO   A  1  694  ? -5.751  62.932  127.072 1.00 35.17 ? 692  PRO   A C     1 
ATOM   5082  O  O     . PRO   A  1  694  ? -5.614  64.066  127.552 1.00 36.40 ? 692  PRO   A O     1 
ATOM   5083  C  CB    . PRO   A  1  694  ? -6.506  61.119  128.665 1.00 36.81 ? 692  PRO   A CB    1 
ATOM   5084  C  CG    . PRO   A  1  694  ? -7.277  59.851  128.416 1.00 32.49 ? 692  PRO   A CG    1 
ATOM   5085  C  CD    . PRO   A  1  694  ? -7.406  59.735  126.926 1.00 30.47 ? 692  PRO   A CD    1 
ATOM   5086  N  N     . GLY   A  1  695  ? -4.907  62.443  126.164 1.00 28.29 ? 693  GLY   A N     1 
ATOM   5087  C  CA    . GLY   A  1  695  ? -3.759  63.206  125.713 1.00 32.23 ? 693  GLY   A CA    1 
ATOM   5088  C  C     . GLY   A  1  695  ? -4.045  64.278  124.688 1.00 31.31 ? 693  GLY   A C     1 
ATOM   5089  O  O     . GLY   A  1  695  ? -3.120  64.995  124.294 1.00 32.92 ? 693  GLY   A O     1 
ATOM   5090  N  N     . HIS   A  1  696  ? -5.293  64.408  124.232 1.00 29.41 ? 694  HIS   A N     1 
ATOM   5091  C  CA    . HIS   A  1  696  ? -5.656  65.439  123.262 1.00 28.68 ? 694  HIS   A CA    1 
ATOM   5092  C  C     . HIS   A  1  696  ? -6.392  66.529  124.028 1.00 29.59 ? 694  HIS   A C     1 
ATOM   5093  O  O     . HIS   A  1  696  ? -7.624  66.610  124.037 1.00 31.83 ? 694  HIS   A O     1 
ATOM   5094  C  CB    . HIS   A  1  696  ? -6.487  64.851  122.133 1.00 27.89 ? 694  HIS   A CB    1 
ATOM   5095  C  CG    . HIS   A  1  696  ? -5.924  63.576  121.590 1.00 24.91 ? 694  HIS   A CG    1 
ATOM   5096  N  ND1   . HIS   A  1  696  ? -6.570  62.366  121.719 1.00 26.73 ? 694  HIS   A ND1   1 
ATOM   5097  C  CD2   . HIS   A  1  696  ? -4.757  63.316  120.953 1.00 26.18 ? 694  HIS   A CD2   1 
ATOM   5098  C  CE1   . HIS   A  1  696  ? -5.840  61.419  121.158 1.00 26.56 ? 694  HIS   A CE1   1 
ATOM   5099  N  NE2   . HIS   A  1  696  ? -4.731  61.967  120.695 1.00 27.80 ? 694  HIS   A NE2   1 
ATOM   5100  N  N     . GLY   A  1  697  ? -5.611  67.359  124.704 1.00 31.14 ? 695  GLY   A N     1 
ATOM   5101  C  CA    . GLY   A  1  697  ? -6.158  68.396  125.539 1.00 29.79 ? 695  GLY   A CA    1 
ATOM   5102  C  C     . GLY   A  1  697  ? -6.763  69.500  124.705 1.00 26.50 ? 695  GLY   A C     1 
ATOM   5103  O  O     . GLY   A  1  697  ? -6.269  69.842  123.627 1.00 26.87 ? 695  GLY   A O     1 
ATOM   5104  N  N     . PRO   A  1  698  ? -7.857  70.080  125.177 1.00 28.16 ? 696  PRO   A N     1 
ATOM   5105  C  CA    . PRO   A  1  698  ? -8.461  71.188  124.439 1.00 29.65 ? 696  PRO   A CA    1 
ATOM   5106  C  C     . PRO   A  1  698  ? -7.549  72.406  124.446 1.00 26.33 ? 696  PRO   A C     1 
ATOM   5107  O  O     . PRO   A  1  698  ? -6.678  72.570  125.303 1.00 29.34 ? 696  PRO   A O     1 
ATOM   5108  C  CB    . PRO   A  1  698  ? -9.757  71.461  125.205 1.00 31.31 ? 696  PRO   A CB    1 
ATOM   5109  C  CG    . PRO   A  1  698  ? -9.492  70.973  126.564 1.00 36.09 ? 696  PRO   A CG    1 
ATOM   5110  C  CD    . PRO   A  1  698  ? -8.593  69.774  126.412 1.00 35.98 ? 696  PRO   A CD    1 
ATOM   5111  N  N     . LEU   A  1  699  ? -7.735  73.249  123.431 1.00 25.51 ? 697  LEU   A N     1 
ATOM   5112  C  CA    . LEU   A  1  699  ? -7.024  74.522  123.390 1.00 24.29 ? 697  LEU   A CA    1 
ATOM   5113  C  C     . LEU   A  1  699  ? -7.437  75.425  124.539 1.00 25.49 ? 697  LEU   A C     1 
ATOM   5114  O  O     . LEU   A  1  699  ? -6.589  76.056  125.179 1.00 28.49 ? 697  LEU   A O     1 
ATOM   5115  C  CB    . LEU   A  1  699  ? -7.305  75.230  122.072 1.00 22.87 ? 697  LEU   A CB    1 
ATOM   5116  C  CG    . LEU   A  1  699  ? -6.834  74.539  120.800 1.00 25.76 ? 697  LEU   A CG    1 
ATOM   5117  C  CD1   . LEU   A  1  699  ? -7.245  75.377  119.606 1.00 25.07 ? 697  LEU   A CD1   1 
ATOM   5118  C  CD2   . LEU   A  1  699  ? -5.332  74.349  120.840 1.00 28.60 ? 697  LEU   A CD2   1 
ATOM   5119  N  N     . GLY   A  1  700  ? -8.737  75.498  124.824 1.00 25.72 ? 698  GLY   A N     1 
ATOM   5120  C  CA    . GLY   A  1  700  ? -9.267  76.481  125.739 1.00 24.22 ? 698  GLY   A CA    1 
ATOM   5121  C  C     . GLY   A  1  700  ? -10.419 77.186  125.068 1.00 25.05 ? 698  GLY   A C     1 
ATOM   5122  O  O     . GLY   A  1  700  ? -10.996 76.664  124.110 1.00 26.33 ? 698  GLY   A O     1 
ATOM   5123  N  N     . PRO   A  1  701  ? -10.773 78.382  125.533 1.00 25.52 ? 699  PRO   A N     1 
ATOM   5124  C  CA    . PRO   A  1  701  ? -11.903 79.093  124.921 1.00 24.69 ? 699  PRO   A CA    1 
ATOM   5125  C  C     . PRO   A  1  701  ? -11.663 79.326  123.438 1.00 24.83 ? 699  PRO   A C     1 
ATOM   5126  O  O     . PRO   A  1  701  ? -10.630 79.854  123.028 1.00 25.03 ? 699  PRO   A O     1 
ATOM   5127  C  CB    . PRO   A  1  701  ? -11.956 80.410  125.700 1.00 27.45 ? 699  PRO   A CB    1 
ATOM   5128  C  CG    . PRO   A  1  701  ? -11.383 80.056  127.048 1.00 28.92 ? 699  PRO   A CG    1 
ATOM   5129  C  CD    . PRO   A  1  701  ? -10.285 79.058  126.748 1.00 26.03 ? 699  PRO   A CD    1 
ATOM   5130  N  N     . ILE   A  1  702  ? -12.616 78.893  122.626 1.00 24.11 ? 700  ILE   A N     1 
ATOM   5131  C  CA    A ILE   A  1  702  ? -12.545 79.066  121.182 0.57 22.29 ? 700  ILE   A CA    1 
ATOM   5132  C  CA    B ILE   A  1  702  ? -12.557 79.049  121.176 0.43 22.30 ? 700  ILE   A CA    1 
ATOM   5133  C  C     . ILE   A  1  702  ? -13.613 80.060  120.764 1.00 22.34 ? 700  ILE   A C     1 
ATOM   5134  O  O     . ILE   A  1  702  ? -14.779 79.941  121.159 1.00 23.39 ? 700  ILE   A O     1 
ATOM   5135  C  CB    A ILE   A  1  702  ? -12.684 77.731  120.435 0.57 22.78 ? 700  ILE   A CB    1 
ATOM   5136  C  CB    B ILE   A  1  702  ? -12.786 77.710  120.456 0.43 22.75 ? 700  ILE   A CB    1 
ATOM   5137  C  CG1   A ILE   A  1  702  ? -11.421 76.895  120.640 0.57 23.21 ? 700  ILE   A CG1   1 
ATOM   5138  C  CG1   B ILE   A  1  702  ? -11.725 76.694  120.873 0.43 23.82 ? 700  ILE   A CG1   1 
ATOM   5139  C  CG2   A ILE   A  1  702  ? -12.936 77.967  118.942 0.57 22.40 ? 700  ILE   A CG2   1 
ATOM   5140  C  CG2   B ILE   A  1  702  ? -12.772 77.905  118.938 0.43 22.42 ? 700  ILE   A CG2   1 
ATOM   5141  C  CD1   A ILE   A  1  702  ? -11.440 75.591  119.907 0.57 21.54 ? 700  ILE   A CD1   1 
ATOM   5142  C  CD1   B ILE   A  1  702  ? -10.332 77.076  120.483 0.43 22.97 ? 700  ILE   A CD1   1 
ATOM   5143  N  N     . VAL   A  1  703  ? -13.209 81.044  119.974 1.00 22.45 ? 701  VAL   A N     1 
ATOM   5144  C  CA    . VAL   A  1  703  ? -14.124 82.030  119.429 1.00 23.60 ? 701  VAL   A CA    1 
ATOM   5145  C  C     . VAL   A  1  703  ? -14.564 81.516  118.066 1.00 22.16 ? 701  VAL   A C     1 
ATOM   5146  O  O     . VAL   A  1  703  ? -13.729 81.281  117.190 1.00 22.52 ? 701  VAL   A O     1 
ATOM   5147  C  CB    . VAL   A  1  703  ? -13.436 83.397  119.326 1.00 23.71 ? 701  VAL   A CB    1 
ATOM   5148  C  CG1   . VAL   A  1  703  ? -14.298 84.363  118.553 1.00 24.66 ? 701  VAL   A CG1   1 
ATOM   5149  C  CG2   . VAL   A  1  703  ? -13.146 83.940  120.733 1.00 26.44 ? 701  VAL   A CG2   1 
ATOM   5150  N  N     . CYS   A  1  704  ? -15.866 81.287  117.905 1.00 20.95 ? 702  CYS   A N     1 
ATOM   5151  C  CA    . CYS   A  1  704  ? -16.439 80.813  116.650 1.00 20.93 ? 702  CYS   A CA    1 
ATOM   5152  C  C     . CYS   A  1  704  ? -17.195 81.972  116.026 1.00 23.58 ? 702  CYS   A C     1 
ATOM   5153  O  O     . CYS   A  1  704  ? -18.197 82.437  116.573 1.00 22.32 ? 702  CYS   A O     1 
ATOM   5154  C  CB    . CYS   A  1  704  ? -17.363 79.620  116.869 1.00 22.34 ? 702  CYS   A CB    1 
ATOM   5155  S  SG    . CYS   A  1  704  ? -16.532 78.212  117.601 1.00 22.39 ? 702  CYS   A SG    1 
ATOM   5156  N  N     . ILE   A  1  705  ? -16.702 82.440  114.889 1.00 20.27 ? 703  ILE   A N     1 
ATOM   5157  C  CA    . ILE   A  1  705  ? -17.289 83.552  114.164 1.00 22.75 ? 703  ILE   A CA    1 
ATOM   5158  C  C     . ILE   A  1  705  ? -17.775 83.006  112.834 1.00 19.74 ? 703  ILE   A C     1 
ATOM   5159  O  O     . ILE   A  1  705  ? -17.014 82.339  112.122 1.00 20.04 ? 703  ILE   A O     1 
ATOM   5160  C  CB    . ILE   A  1  705  ? -16.250 84.669  113.975 1.00 21.10 ? 703  ILE   A CB    1 
ATOM   5161  C  CG1   . ILE   A  1  705  ? -15.883 85.275  115.328 1.00 22.44 ? 703  ILE   A CG1   1 
ATOM   5162  C  CG2   . ILE   A  1  705  ? -16.767 85.730  113.042 1.00 22.16 ? 703  ILE   A CG2   1 
ATOM   5163  C  CD1   . ILE   A  1  705  ? -14.640 86.135  115.270 1.00 25.65 ? 703  ILE   A CD1   1 
ATOM   5164  N  N     . SER   A  1  706  ? -19.036 83.256  112.517 1.00 20.52 ? 704  SER   A N     1 
ATOM   5165  C  CA    . SER   A  1  706  ? -19.676 82.566  111.409 1.00 20.68 ? 704  SER   A CA    1 
ATOM   5166  C  C     . SER   A  1  706  ? -20.317 83.559  110.456 1.00 20.94 ? 704  SER   A C     1 
ATOM   5167  O  O     . SER   A  1  706  ? -20.609 84.699  110.830 1.00 21.96 ? 704  SER   A O     1 
ATOM   5168  C  CB    . SER   A  1  706  ? -20.719 81.567  111.930 1.00 23.13 ? 704  SER   A CB    1 
ATOM   5169  O  OG    . SER   A  1  706  ? -21.584 82.198  112.844 1.00 22.80 ? 704  SER   A OG    1 
ATOM   5170  N  N     . PRO   A  1  707  ? -20.540 83.155  109.210 1.00 20.60 ? 705  PRO   A N     1 
ATOM   5171  C  CA    . PRO   A  1  707  ? -21.089 84.059  108.200 1.00 22.02 ? 705  PRO   A CA    1 
ATOM   5172  C  C     . PRO   A  1  707  ? -22.613 84.003  108.213 1.00 19.27 ? 705  PRO   A C     1 
ATOM   5173  O  O     . PRO   A  1  707  ? -23.225 83.118  108.810 1.00 22.51 ? 705  PRO   A O     1 
ATOM   5174  C  CB    . PRO   A  1  707  ? -20.564 83.437  106.903 1.00 20.97 ? 705  PRO   A CB    1 
ATOM   5175  C  CG    . PRO   A  1  707  ? -20.571 81.984  107.192 1.00 20.31 ? 705  PRO   A CG    1 
ATOM   5176  C  CD    . PRO   A  1  707  ? -20.170 81.849  108.636 1.00 20.38 ? 705  PRO   A CD    1 
ATOM   5177  N  N     . TRP   A  1  708  ? -23.224 84.970  107.529 1.00 20.96 ? 706  TRP   A N     1 
ATOM   5178  C  CA    . TRP   A  1  708  ? -24.684 85.000  107.530 1.00 20.81 ? 706  TRP   A CA    1 
ATOM   5179  C  C     . TRP   A  1  708  ? -25.275 83.948  106.603 1.00 22.52 ? 706  TRP   A C     1 
ATOM   5180  O  O     . TRP   A  1  708  ? -26.413 83.517  106.809 1.00 22.61 ? 706  TRP   A O     1 
ATOM   5181  C  CB    . TRP   A  1  708  ? -25.206 86.388  107.141 1.00 20.16 ? 706  TRP   A CB    1 
ATOM   5182  C  CG    . TRP   A  1  708  ? -25.062 86.629  105.690 1.00 22.17 ? 706  TRP   A CG    1 
ATOM   5183  C  CD1   . TRP   A  1  708  ? -24.025 87.249  105.067 1.00 21.96 ? 706  TRP   A CD1   1 
ATOM   5184  C  CD2   . TRP   A  1  708  ? -25.963 86.209  104.657 1.00 21.64 ? 706  TRP   A CD2   1 
ATOM   5185  N  NE1   . TRP   A  1  708  ? -24.220 87.245  103.708 1.00 22.49 ? 706  TRP   A NE1   1 
ATOM   5186  C  CE2   . TRP   A  1  708  ? -25.402 86.608  103.431 1.00 20.69 ? 706  TRP   A CE2   1 
ATOM   5187  C  CE3   . TRP   A  1  708  ? -27.195 85.543  104.654 1.00 21.36 ? 706  TRP   A CE3   1 
ATOM   5188  C  CZ2   . TRP   A  1  708  ? -26.022 86.363  102.212 1.00 19.86 ? 706  TRP   A CZ2   1 
ATOM   5189  C  CZ3   . TRP   A  1  708  ? -27.797 85.279  103.439 1.00 21.75 ? 706  TRP   A CZ3   1 
ATOM   5190  C  CH2   . TRP   A  1  708  ? -27.216 85.701  102.235 1.00 20.87 ? 706  TRP   A CH2   1 
ATOM   5191  N  N     . ASN   A  1  709  ? -24.534 83.517  105.584 1.00 20.98 ? 707  ASN   A N     1 
ATOM   5192  C  CA    . ASN   A  1  709  ? -25.188 82.889  104.442 1.00 22.80 ? 707  ASN   A CA    1 
ATOM   5193  C  C     . ASN   A  1  709  ? -25.505 81.422  104.657 1.00 22.77 ? 707  ASN   A C     1 
ATOM   5194  O  O     . ASN   A  1  709  ? -26.366 80.881  103.960 1.00 21.72 ? 707  ASN   A O     1 
ATOM   5195  C  CB    . ASN   A  1  709  ? -24.337 83.059  103.192 1.00 21.89 ? 707  ASN   A CB    1 
ATOM   5196  C  CG    . ASN   A  1  709  ? -23.084 82.242  103.251 1.00 22.56 ? 707  ASN   A CG    1 
ATOM   5197  O  OD1   . ASN   A  1  709  ? -22.220 82.478  104.095 1.00 24.11 ? 707  ASN   A OD1   1 
ATOM   5198  N  ND2   . ASN   A  1  709  ? -22.969 81.265  102.357 1.00 23.00 ? 707  ASN   A ND2   1 
ATOM   5199  N  N     . PHE   A  1  710  ? -24.810 80.756  105.570 1.00 21.20 ? 708  PHE   A N     1 
ATOM   5200  C  CA    . PHE   A  1  710  ? -25.187 79.433  106.046 1.00 21.94 ? 708  PHE   A CA    1 
ATOM   5201  C  C     . PHE   A  1  710  ? -25.386 79.609  107.543 1.00 21.66 ? 708  PHE   A C     1 
ATOM   5202  O  O     . PHE   A  1  710  ? -24.563 79.164  108.356 1.00 22.51 ? 708  PHE   A O     1 
ATOM   5203  C  CB    . PHE   A  1  710  ? -24.122 78.386  105.737 1.00 22.62 ? 708  PHE   A CB    1 
ATOM   5204  C  CG    . PHE   A  1  710  ? -23.859 78.197  104.263 1.00 23.81 ? 708  PHE   A CG    1 
ATOM   5205  C  CD1   . PHE   A  1  710  ? -24.893 78.253  103.340 1.00 25.39 ? 708  PHE   A CD1   1 
ATOM   5206  C  CD2   . PHE   A  1  710  ? -22.569 77.958  103.803 1.00 24.88 ? 708  PHE   A CD2   1 
ATOM   5207  C  CE1   . PHE   A  1  710  ? -24.649 78.075  101.989 1.00 26.32 ? 708  PHE   A CE1   1 
ATOM   5208  C  CE2   . PHE   A  1  710  ? -22.315 77.778  102.447 1.00 26.16 ? 708  PHE   A CE2   1 
ATOM   5209  C  CZ    . PHE   A  1  710  ? -23.355 77.840  101.542 1.00 26.28 ? 708  PHE   A CZ    1 
ATOM   5210  N  N     . PRO   A  1  711  ? -26.476 80.277  107.938 1.00 21.54 ? 709  PRO   A N     1 
ATOM   5211  C  CA    . PRO   A  1  711  ? -26.569 80.813  109.302 1.00 22.12 ? 709  PRO   A CA    1 
ATOM   5212  C  C     . PRO   A  1  711  ? -26.786 79.768  110.368 1.00 20.50 ? 709  PRO   A C     1 
ATOM   5213  O  O     . PRO   A  1  711  ? -26.635 80.083  111.555 1.00 22.86 ? 709  PRO   A O     1 
ATOM   5214  C  CB    . PRO   A  1  711  ? -27.777 81.748  109.216 1.00 23.52 ? 709  PRO   A CB    1 
ATOM   5215  C  CG    . PRO   A  1  711  ? -28.647 81.097  108.194 1.00 21.90 ? 709  PRO   A CG    1 
ATOM   5216  C  CD    . PRO   A  1  711  ? -27.685 80.580  107.150 1.00 20.90 ? 709  PRO   A CD    1 
ATOM   5217  N  N     . LEU   A  1  712  ? -27.159 78.552  109.998 1.00 22.13 ? 710  LEU   A N     1 
ATOM   5218  C  CA    . LEU   A  1  712  ? -27.259 77.467  110.958 1.00 19.67 ? 710  LEU   A CA    1 
ATOM   5219  C  C     . LEU   A  1  712  ? -26.188 76.413  110.760 1.00 20.88 ? 710  LEU   A C     1 
ATOM   5220  O  O     . LEU   A  1  712  ? -25.580 75.967  111.733 1.00 20.64 ? 710  LEU   A O     1 
ATOM   5221  C  CB    . LEU   A  1  712  ? -28.643 76.810  110.897 1.00 21.88 ? 710  LEU   A CB    1 
ATOM   5222  C  CG    . LEU   A  1  712  ? -28.820 75.699  111.931 1.00 22.38 ? 710  LEU   A CG    1 
ATOM   5223  C  CD1   . LEU   A  1  712  ? -28.748 76.250  113.345 1.00 20.96 ? 710  LEU   A CD1   1 
ATOM   5224  C  CD2   . LEU   A  1  712  ? -30.127 74.941  111.691 1.00 24.85 ? 710  LEU   A CD2   1 
ATOM   5225  N  N     . ALA   A  1  713  ? -25.905 76.044  109.516 1.00 20.88 ? 711  ALA   A N     1 
ATOM   5226  C  CA    . ALA   A  1  713  ? -25.013 74.918  109.272 1.00 19.39 ? 711  ALA   A CA    1 
ATOM   5227  C  C     . ALA   A  1  713  ? -23.578 75.236  109.674 1.00 20.21 ? 711  ALA   A C     1 
ATOM   5228  O  O     . ALA   A  1  713  ? -22.970 74.511  110.467 1.00 20.55 ? 711  ALA   A O     1 
ATOM   5229  C  CB    . ALA   A  1  713  ? -25.084 74.504  107.805 1.00 19.53 ? 711  ALA   A CB    1 
ATOM   5230  N  N     . ILE   A  1  714  ? -23.006 76.299  109.115 1.00 19.84 ? 712  ILE   A N     1 
ATOM   5231  C  CA    . ILE   A  1  714  ? -21.620 76.618  109.449 1.00 18.17 ? 712  ILE   A CA    1 
ATOM   5232  C  C     . ILE   A  1  714  ? -21.516 77.035  110.902 1.00 19.91 ? 712  ILE   A C     1 
ATOM   5233  O  O     . ILE   A  1  714  ? -20.572 76.661  111.613 1.00 20.63 ? 712  ILE   A O     1 
ATOM   5234  C  CB    . ILE   A  1  714  ? -21.072 77.689  108.498 1.00 21.24 ? 712  ILE   A CB    1 
ATOM   5235  C  CG1   . ILE   A  1  714  ? -20.948 77.064  107.108 1.00 22.33 ? 712  ILE   A CG1   1 
ATOM   5236  C  CG2   . ILE   A  1  714  ? -19.734 78.247  109.011 1.00 21.18 ? 712  ILE   A CG2   1 
ATOM   5237  C  CD1   . ILE   A  1  714  ? -19.992 77.751  106.208 1.00 30.04 ? 712  ILE   A CD1   1 
ATOM   5238  N  N     . PHE   A  1  715  ? -22.488 77.818  111.366 1.00 19.92 ? 713  PHE   A N     1 
ATOM   5239  C  CA    . PHE   A  1  715  ? -22.555 78.189  112.770 1.00 20.86 ? 713  PHE   A CA    1 
ATOM   5240  C  C     . PHE   A  1  715  ? -22.480 76.952  113.654 1.00 20.64 ? 713  PHE   A C     1 
ATOM   5241  O  O     . PHE   A  1  715  ? -21.648 76.871  114.567 1.00 20.54 ? 713  PHE   A O     1 
ATOM   5242  C  CB    . PHE   A  1  715  ? -23.864 78.946  112.994 1.00 19.59 ? 713  PHE   A CB    1 
ATOM   5243  C  CG    . PHE   A  1  715  ? -24.098 79.337  114.408 1.00 21.94 ? 713  PHE   A CG    1 
ATOM   5244  C  CD1   . PHE   A  1  715  ? -23.459 80.438  114.934 1.00 22.64 ? 713  PHE   A CD1   1 
ATOM   5245  C  CD2   . PHE   A  1  715  ? -24.949 78.600  115.216 1.00 24.22 ? 713  PHE   A CD2   1 
ATOM   5246  C  CE1   . PHE   A  1  715  ? -23.673 80.810  116.246 1.00 25.61 ? 713  PHE   A CE1   1 
ATOM   5247  C  CE2   . PHE   A  1  715  ? -25.161 78.955  116.516 1.00 23.83 ? 713  PHE   A CE2   1 
ATOM   5248  C  CZ    . PHE   A  1  715  ? -24.534 80.070  117.041 1.00 26.23 ? 713  PHE   A CZ    1 
ATOM   5249  N  N     . THR   A  1  716  ? -23.330 75.962  113.380 1.00 20.43 ? 714  THR   A N     1 
ATOM   5250  C  CA    . THR   A  1  716  ? -23.370 74.761  114.207 1.00 20.17 ? 714  THR   A CA    1 
ATOM   5251  C  C     . THR   A  1  716  ? -22.101 73.945  114.054 1.00 20.33 ? 714  THR   A C     1 
ATOM   5252  O  O     . THR   A  1  716  ? -21.564 73.433  115.041 1.00 21.13 ? 714  THR   A O     1 
ATOM   5253  C  CB    . THR   A  1  716  ? -24.571 73.909  113.823 1.00 22.66 ? 714  THR   A CB    1 
ATOM   5254  O  OG1   . THR   A  1  716  ? -25.759 74.654  114.094 1.00 21.95 ? 714  THR   A OG1   1 
ATOM   5255  C  CG2   . THR   A  1  716  ? -24.608 72.622  114.631 1.00 22.91 ? 714  THR   A CG2   1 
ATOM   5256  N  N     . GLY   A  1  717  ? -21.612 73.815  112.822 1.00 19.43 ? 715  GLY   A N     1 
ATOM   5257  C  CA    . GLY   A  1  717  ? -20.428 73.005  112.586 1.00 19.90 ? 715  GLY   A CA    1 
ATOM   5258  C  C     . GLY   A  1  717  ? -19.237 73.473  113.399 1.00 19.88 ? 715  GLY   A C     1 
ATOM   5259  O  O     . GLY   A  1  717  ? -18.590 72.680  114.080 1.00 20.29 ? 715  GLY   A O     1 
ATOM   5260  N  N     . GLN   A  1  718  ? -18.938 74.773  113.342 1.00 18.28 ? 716  GLN   A N     1 
ATOM   5261  C  CA    . GLN   A  1  718  ? -17.767 75.274  114.058 1.00 18.75 ? 716  GLN   A CA    1 
ATOM   5262  C  C     . GLN   A  1  718  ? -17.920 75.058  115.549 1.00 20.11 ? 716  GLN   A C     1 
ATOM   5263  O  O     . GLN   A  1  718  ? -17.008 74.574  116.225 1.00 20.39 ? 716  GLN   A O     1 
ATOM   5264  C  CB    . GLN   A  1  718  ? -17.566 76.763  113.778 1.00 19.50 ? 716  GLN   A CB    1 
ATOM   5265  C  CG    . GLN   A  1  718  ? -17.234 77.046  112.335 1.00 19.81 ? 716  GLN   A CG    1 
ATOM   5266  C  CD    . GLN   A  1  718  ? -16.809 78.481  112.082 1.00 21.11 ? 716  GLN   A CD    1 
ATOM   5267  O  OE1   . GLN   A  1  718  ? -15.871 78.725  111.324 1.00 20.73 ? 716  GLN   A OE1   1 
ATOM   5268  N  NE2   . GLN   A  1  718  ? -17.485 79.433  112.709 1.00 21.16 ? 716  GLN   A NE2   1 
ATOM   5269  N  N     . ILE   A  1  719  ? -19.079 75.430  116.083 1.00 19.93 ? 717  ILE   A N     1 
ATOM   5270  C  CA    . ILE   A  1  719  ? -19.304 75.324  117.517 1.00 20.40 ? 717  ILE   A CA    1 
ATOM   5271  C  C     . ILE   A  1  719  ? -19.278 73.872  117.959 1.00 21.18 ? 717  ILE   A C     1 
ATOM   5272  O  O     . ILE   A  1  719  ? -18.681 73.534  118.989 1.00 22.05 ? 717  ILE   A O     1 
ATOM   5273  C  CB    . ILE   A  1  719  ? -20.631 76.002  117.885 1.00 23.36 ? 717  ILE   A CB    1 
ATOM   5274  C  CG1   . ILE   A  1  719  ? -20.517 77.501  117.669 1.00 21.52 ? 717  ILE   A CG1   1 
ATOM   5275  C  CG2   . ILE   A  1  719  ? -21.049 75.649  119.299 1.00 31.01 ? 717  ILE   A CG2   1 
ATOM   5276  C  CD1   . ILE   A  1  719  ? -21.857 78.124  117.546 1.00 29.25 ? 717  ILE   A CD1   1 
ATOM   5277  N  N     . ALA   A  1  720  ? -19.935 72.995  117.200 1.00 21.91 ? 718  ALA   A N     1 
ATOM   5278  C  CA    . ALA   A  1  720  ? -20.002 71.596  117.594 1.00 22.34 ? 718  ALA   A CA    1 
ATOM   5279  C  C     . ALA   A  1  720  ? -18.613 70.986  117.635 1.00 20.64 ? 718  ALA   A C     1 
ATOM   5280  O  O     . ALA   A  1  720  ? -18.286 70.247  118.565 1.00 20.37 ? 718  ALA   A O     1 
ATOM   5281  C  CB    . ALA   A  1  720  ? -20.897 70.819  116.627 1.00 22.32 ? 718  ALA   A CB    1 
ATOM   5282  N  N     . ALA   A  1  721  ? -17.793 71.287  116.632 1.00 20.47 ? 719  ALA   A N     1 
ATOM   5283  C  CA    . ALA   A  1  721  ? -16.432 70.774  116.604 1.00 18.48 ? 719  ALA   A CA    1 
ATOM   5284  C  C     . ALA   A  1  721  ? -15.637 71.255  117.811 1.00 20.79 ? 719  ALA   A C     1 
ATOM   5285  O  O     . ALA   A  1  721  ? -14.997 70.458  118.508 1.00 21.25 ? 719  ALA   A O     1 
ATOM   5286  C  CB    . ALA   A  1  721  ? -15.761 71.228  115.320 1.00 20.13 ? 719  ALA   A CB    1 
ATOM   5287  N  N     . ALA   A  1  722  ? -15.668 72.564  118.076 1.00 19.30 ? 720  ALA   A N     1 
ATOM   5288  C  CA    . ALA   A  1  722  ? -14.914 73.102  119.202 1.00 20.45 ? 720  ALA   A CA    1 
ATOM   5289  C  C     . ALA   A  1  722  ? -15.396 72.499  120.514 1.00 22.63 ? 720  ALA   A C     1 
ATOM   5290  O  O     . ALA   A  1  722  ? -14.588 72.078  121.353 1.00 21.79 ? 720  ALA   A O     1 
ATOM   5291  C  CB    . ALA   A  1  722  ? -15.009 74.626  119.222 1.00 21.71 ? 720  ALA   A CB    1 
ATOM   5292  N  N     . LEU   A  1  723  ? -16.716 72.437  120.702 1.00 20.73 ? 721  LEU   A N     1 
ATOM   5293  C  CA    . LEU   A  1  723  ? -17.271 71.887  121.934 1.00 22.17 ? 721  LEU   A CA    1 
ATOM   5294  C  C     . LEU   A  1  723  ? -16.885 70.430  122.109 1.00 22.25 ? 721  LEU   A C     1 
ATOM   5295  O  O     . LEU   A  1  723  ? -16.480 70.006  123.194 1.00 22.52 ? 721  LEU   A O     1 
ATOM   5296  C  CB    . LEU   A  1  723  ? -18.790 71.998  121.915 1.00 22.92 ? 721  LEU   A CB    1 
ATOM   5297  C  CG    . LEU   A  1  723  ? -19.416 73.361  122.114 1.00 22.31 ? 721  LEU   A CG    1 
ATOM   5298  C  CD1   . LEU   A  1  723  ? -20.902 73.194  121.899 1.00 25.13 ? 721  LEU   A CD1   1 
ATOM   5299  C  CD2   . LEU   A  1  723  ? -19.125 73.852  123.509 1.00 26.06 ? 721  LEU   A CD2   1 
ATOM   5300  N  N     . VAL   A  1  724  ? -17.008 69.638  121.048 1.00 22.62 ? 722  VAL   A N     1 
ATOM   5301  C  CA    . VAL   A  1  724  ? -16.798 68.214  121.240 1.00 21.76 ? 722  VAL   A CA    1 
ATOM   5302  C  C     . VAL   A  1  724  ? -15.323 67.916  121.465 1.00 21.19 ? 722  VAL   A C     1 
ATOM   5303  O  O     . VAL   A  1  724  ? -14.982 66.927  122.117 1.00 22.52 ? 722  VAL   A O     1 
ATOM   5304  C  CB    . VAL   A  1  724  ? -17.416 67.413  120.085 1.00 20.63 ? 722  VAL   A CB    1 
ATOM   5305  C  CG1   . VAL   A  1  724  ? -16.529 67.469  118.830 1.00 22.25 ? 722  VAL   A CG1   1 
ATOM   5306  C  CG2   . VAL   A  1  724  ? -17.733 65.998  120.526 1.00 22.40 ? 722  VAL   A CG2   1 
ATOM   5307  N  N     . ALA   A  1  725  ? -14.438 68.771  120.949 1.00 21.09 ? 723  ALA   A N     1 
ATOM   5308  C  CA    . ALA   A  1  725  ? -13.012 68.692  121.242 1.00 22.89 ? 723  ALA   A CA    1 
ATOM   5309  C  C     . ALA   A  1  725  ? -12.684 69.125  122.663 1.00 24.61 ? 723  ALA   A C     1 
ATOM   5310  O  O     . ALA   A  1  725  ? -11.500 69.099  123.034 1.00 25.34 ? 723  ALA   A O     1 
ATOM   5311  C  CB    . ALA   A  1  725  ? -12.228 69.533  120.235 1.00 21.48 ? 723  ALA   A CB    1 
ATOM   5312  N  N     . GLY   A  1  726  ? -13.678 69.518  123.459 1.00 24.32 ? 724  GLY   A N     1 
ATOM   5313  C  CA    . GLY   A  1  726  ? -13.456 69.867  124.845 1.00 24.03 ? 724  GLY   A CA    1 
ATOM   5314  C  C     . GLY   A  1  726  ? -13.217 71.330  125.124 1.00 24.16 ? 724  GLY   A C     1 
ATOM   5315  O  O     . GLY   A  1  726  ? -12.774 71.666  126.232 1.00 25.79 ? 724  GLY   A O     1 
ATOM   5316  N  N     . ASN   A  1  727  ? -13.492 72.209  124.168 1.00 23.93 ? 725  ASN   A N     1 
ATOM   5317  C  CA    . ASN   A  1  727  ? -13.290 73.635  124.359 1.00 23.29 ? 725  ASN   A CA    1 
ATOM   5318  C  C     . ASN   A  1  727  ? -14.613 74.329  124.645 1.00 24.03 ? 725  ASN   A C     1 
ATOM   5319  O  O     . ASN   A  1  727  ? -15.610 74.081  123.950 1.00 24.39 ? 725  ASN   A O     1 
ATOM   5320  C  CB    . ASN   A  1  727  ? -12.724 74.244  123.078 1.00 23.45 ? 725  ASN   A CB    1 
ATOM   5321  C  CG    . ASN   A  1  727  ? -11.492 73.538  122.596 1.00 24.19 ? 725  ASN   A CG    1 
ATOM   5322  O  OD1   . ASN   A  1  727  ? -10.408 73.744  123.128 1.00 24.61 ? 725  ASN   A OD1   1 
ATOM   5323  N  ND2   . ASN   A  1  727  ? -11.647 72.699  121.585 1.00 22.44 ? 725  ASN   A ND2   1 
ATOM   5324  N  N     . PRO   A  1  728  ? -14.655 75.232  125.613 1.00 24.18 ? 726  PRO   A N     1 
ATOM   5325  C  CA    . PRO   A  1  728  ? -15.810 76.121  125.712 1.00 26.88 ? 726  PRO   A CA    1 
ATOM   5326  C  C     . PRO   A  1  728  ? -15.779 77.105  124.560 1.00 24.07 ? 726  PRO   A C     1 
ATOM   5327  O  O     . PRO   A  1  728  ? -14.716 77.477  124.055 1.00 26.16 ? 726  PRO   A O     1 
ATOM   5328  C  CB    . PRO   A  1  728  ? -15.594 76.836  127.049 1.00 24.03 ? 726  PRO   A CB    1 
ATOM   5329  C  CG    . PRO   A  1  728  ? -14.115 76.842  127.234 1.00 28.15 ? 726  PRO   A CG    1 
ATOM   5330  C  CD    . PRO   A  1  728  ? -13.581 75.604  126.548 1.00 25.59 ? 726  PRO   A CD    1 
ATOM   5331  N  N     . VAL   A  1  729  ? -16.966 77.528  124.141 1.00 23.81 ? 727  VAL   A N     1 
ATOM   5332  C  CA    . VAL   A  1  729  ? -17.135 78.274  122.905 1.00 23.15 ? 727  VAL   A CA    1 
ATOM   5333  C  C     . VAL   A  1  729  ? -17.792 79.615  123.175 1.00 22.66 ? 727  VAL   A C     1 
ATOM   5334  O  O     . VAL   A  1  729  ? -18.773 79.705  123.919 1.00 23.87 ? 727  VAL   A O     1 
ATOM   5335  C  CB    . VAL   A  1  729  ? -17.968 77.453  121.903 1.00 22.53 ? 727  VAL   A CB    1 
ATOM   5336  C  CG1   . VAL   A  1  729  ? -18.433 78.322  120.735 1.00 25.13 ? 727  VAL   A CG1   1 
ATOM   5337  C  CG2   . VAL   A  1  729  ? -17.142 76.288  121.403 1.00 24.30 ? 727  VAL   A CG2   1 
ATOM   5338  N  N     . LEU   A  1  730  ? -17.270 80.649  122.530 1.00 24.46 ? 728  LEU   A N     1 
ATOM   5339  C  CA    . LEU   A  1  730  ? -17.932 81.937  122.405 1.00 25.42 ? 728  LEU   A CA    1 
ATOM   5340  C  C     . LEU   A  1  730  ? -18.430 81.989  120.973 1.00 23.24 ? 728  LEU   A C     1 
ATOM   5341  O  O     . LEU   A  1  730  ? -17.626 82.041  120.037 1.00 23.61 ? 728  LEU   A O     1 
ATOM   5342  C  CB    . LEU   A  1  730  ? -16.966 83.086  122.669 1.00 26.05 ? 728  LEU   A CB    1 
ATOM   5343  C  CG    . LEU   A  1  730  ? -16.291 83.140  124.045 1.00 25.29 ? 728  LEU   A CG    1 
ATOM   5344  C  CD1   . LEU   A  1  730  ? -17.299 82.888  125.144 1.00 26.35 ? 728  LEU   A CD1   1 
ATOM   5345  C  CD2   . LEU   A  1  730  ? -15.136 82.159  124.141 1.00 24.74 ? 728  LEU   A CD2   1 
ATOM   5346  N  N     . ALA   A  1  731  ? -19.747 81.950  120.804 1.00 23.86 ? 729  ALA   A N     1 
ATOM   5347  C  CA    . ALA   A  1  731  ? -20.365 81.859  119.488 1.00 25.69 ? 729  ALA   A CA    1 
ATOM   5348  C  C     . ALA   A  1  731  ? -20.816 83.251  119.072 1.00 24.35 ? 729  ALA   A C     1 
ATOM   5349  O  O     . ALA   A  1  731  ? -21.727 83.825  119.676 1.00 26.29 ? 729  ALA   A O     1 
ATOM   5350  C  CB    . ALA   A  1  731  ? -21.541 80.889  119.518 1.00 25.35 ? 729  ALA   A CB    1 
ATOM   5351  N  N     . LYS   A  1  732  ? -20.177 83.790  118.039 1.00 21.30 ? 730  LYS   A N     1 
ATOM   5352  C  CA    . LYS   A  1  732  ? -20.521 85.112  117.531 1.00 24.57 ? 730  LYS   A CA    1 
ATOM   5353  C  C     . LYS   A  1  732  ? -21.125 84.925  116.145 1.00 24.29 ? 730  LYS   A C     1 
ATOM   5354  O  O     . LYS   A  1  732  ? -20.387 84.807  115.156 1.00 23.06 ? 730  LYS   A O     1 
ATOM   5355  C  CB    . LYS   A  1  732  ? -19.270 85.992  117.468 1.00 25.64 ? 730  LYS   A CB    1 
ATOM   5356  C  CG    . LYS   A  1  732  ? -19.511 87.461  117.755 1.00 26.66 ? 730  LYS   A CG    1 
ATOM   5357  C  CD    . LYS   A  1  732  ? -20.480 88.068  116.752 1.00 23.16 ? 730  LYS   A CD    1 
ATOM   5358  C  CE    . LYS   A  1  732  ? -19.851 88.202  115.382 1.00 22.77 ? 730  LYS   A CE    1 
ATOM   5359  N  NZ    . LYS   A  1  732  ? -20.829 88.793  114.423 1.00 24.52 ? 730  LYS   A NZ    1 
ATOM   5360  N  N     . PRO   A  1  733  ? -22.446 84.869  116.021 1.00 22.32 ? 731  PRO   A N     1 
ATOM   5361  C  CA    . PRO   A  1  733  ? -23.065 84.712  114.703 1.00 22.58 ? 731  PRO   A CA    1 
ATOM   5362  C  C     . PRO   A  1  733  ? -23.041 86.026  113.946 1.00 21.49 ? 731  PRO   A C     1 
ATOM   5363  O  O     . PRO   A  1  733  ? -22.934 87.108  114.522 1.00 23.82 ? 731  PRO   A O     1 
ATOM   5364  C  CB    . PRO   A  1  733  ? -24.506 84.340  115.046 1.00 23.41 ? 731  PRO   A CB    1 
ATOM   5365  C  CG    . PRO   A  1  733  ? -24.768 85.068  116.337 1.00 24.13 ? 731  PRO   A CG    1 
ATOM   5366  C  CD    . PRO   A  1  733  ? -23.448 85.002  117.096 1.00 23.41 ? 731  PRO   A CD    1 
ATOM   5367  N  N     . ALA   A  1  734  ? -23.159 85.912  112.629 1.00 20.34 ? 732  ALA   A N     1 
ATOM   5368  C  CA    . ALA   A  1  734  ? -23.220 87.099  111.794 1.00 23.42 ? 732  ALA   A CA    1 
ATOM   5369  C  C     . ALA   A  1  734  ? -24.351 88.010  112.252 1.00 22.64 ? 732  ALA   A C     1 
ATOM   5370  O  O     . ALA   A  1  734  ? -25.419 87.556  112.683 1.00 25.52 ? 732  ALA   A O     1 
ATOM   5371  C  CB    . ALA   A  1  734  ? -23.455 86.690  110.343 1.00 23.72 ? 732  ALA   A CB    1 
ATOM   5372  N  N     . GLU   A  1  735  ? -24.112 89.314  112.147 1.00 23.95 ? 733  GLU   A N     1 
ATOM   5373  C  CA    . GLU   A  1  735  ? -25.113 90.272  112.596 1.00 27.26 ? 733  GLU   A CA    1 
ATOM   5374  C  C     . GLU   A  1  735  ? -26.416 90.157  111.814 1.00 25.34 ? 733  GLU   A C     1 
ATOM   5375  O  O     . GLU   A  1  735  ? -27.477 90.512  112.337 1.00 26.38 ? 733  GLU   A O     1 
ATOM   5376  C  CB    . GLU   A  1  735  ? -24.562 91.695  112.520 1.00 27.42 ? 733  GLU   A CB    1 
ATOM   5377  C  CG    . GLU   A  1  735  ? -24.065 92.112  111.141 1.00 27.00 ? 733  GLU   A CG    1 
ATOM   5378  C  CD    . GLU   A  1  735  ? -22.577 91.845  110.941 1.00 33.24 ? 733  GLU   A CD    1 
ATOM   5379  O  OE1   . GLU   A  1  735  ? -22.043 90.919  111.585 1.00 30.03 ? 733  GLU   A OE1   1 
ATOM   5380  O  OE2   . GLU   A  1  735  ? -21.943 92.571  110.147 1.00 31.43 ? 733  GLU   A OE2   1 
ATOM   5381  N  N     . GLU   A  1  736  ? -26.368 89.641  110.588 1.00 24.07 ? 734  GLU   A N     1 
ATOM   5382  C  CA    . GLU   A  1  736  ? -27.584 89.568  109.793 1.00 22.84 ? 734  GLU   A CA    1 
ATOM   5383  C  C     . GLU   A  1  736  ? -28.514 88.453  110.247 1.00 26.69 ? 734  GLU   A C     1 
ATOM   5384  O  O     . GLU   A  1  736  ? -29.726 88.557  110.042 1.00 26.68 ? 734  GLU   A O     1 
ATOM   5385  C  CB    . GLU   A  1  736  ? -27.243 89.364  108.317 1.00 24.15 ? 734  GLU   A CB    1 
ATOM   5386  C  CG    . GLU   A  1  736  ? -26.437 90.490  107.687 1.00 26.46 ? 734  GLU   A CG    1 
ATOM   5387  C  CD    . GLU   A  1  736  ? -24.937 90.267  107.773 1.00 29.73 ? 734  GLU   A CD    1 
ATOM   5388  O  OE1   . GLU   A  1  736  ? -24.491 89.465  108.624 1.00 26.88 ? 734  GLU   A OE1   1 
ATOM   5389  O  OE2   . GLU   A  1  736  ? -24.205 90.884  106.970 1.00 30.45 ? 734  GLU   A OE2   1 
ATOM   5390  N  N     . THR   A  1  737  ? -27.987 87.377  110.831 1.00 24.22 ? 735  THR   A N     1 
ATOM   5391  C  CA    . THR   A  1  737  ? -28.765 86.157  111.072 1.00 24.08 ? 735  THR   A CA    1 
ATOM   5392  C  C     . THR   A  1  737  ? -28.589 85.632  112.496 1.00 25.68 ? 735  THR   A C     1 
ATOM   5393  O  O     . THR   A  1  737  ? -28.222 84.472  112.701 1.00 23.69 ? 735  THR   A O     1 
ATOM   5394  C  CB    . THR   A  1  737  ? -28.392 85.086  110.049 1.00 22.76 ? 735  THR   A CB    1 
ATOM   5395  O  OG1   . THR   A  1  737  ? -26.970 84.863  110.095 1.00 24.03 ? 735  THR   A OG1   1 
ATOM   5396  C  CG2   . THR   A  1  737  ? -28.792 85.517  108.643 1.00 23.28 ? 735  THR   A CG2   1 
ATOM   5397  N  N     . PRO   A  1  738  ? -28.892 86.448  113.513 1.00 22.49 ? 736  PRO   A N     1 
ATOM   5398  C  CA    . PRO   A  1  738  ? -28.704 85.982  114.894 1.00 23.60 ? 736  PRO   A CA    1 
ATOM   5399  C  C     . PRO   A  1  738  ? -29.797 85.057  115.391 1.00 25.01 ? 736  PRO   A C     1 
ATOM   5400  O  O     . PRO   A  1  738  ? -29.561 84.316  116.355 1.00 25.05 ? 736  PRO   A O     1 
ATOM   5401  C  CB    . PRO   A  1  738  ? -28.727 87.285  115.703 1.00 27.81 ? 736  PRO   A CB    1 
ATOM   5402  C  CG    . PRO   A  1  738  ? -29.649 88.154  114.922 1.00 26.29 ? 736  PRO   A CG    1 
ATOM   5403  C  CD    . PRO   A  1  738  ? -29.374 87.841  113.476 1.00 24.75 ? 736  PRO   A CD    1 
ATOM   5404  N  N     . LEU   A  1  739  ? -30.991 85.086  114.794 1.00 24.18 ? 737  LEU   A N     1 
ATOM   5405  C  CA    . LEU   A  1  739  ? -32.106 84.351  115.385 1.00 23.66 ? 737  LEU   A CA    1 
ATOM   5406  C  C     . LEU   A  1  739  ? -31.914 82.848  115.247 1.00 21.76 ? 737  LEU   A C     1 
ATOM   5407  O  O     . LEU   A  1  739  ? -32.090 82.099  116.212 1.00 24.37 ? 737  LEU   A O     1 
ATOM   5408  C  CB    . LEU   A  1  739  ? -33.423 84.785  114.747 1.00 23.75 ? 737  LEU   A CB    1 
ATOM   5409  C  CG    . LEU   A  1  739  ? -33.720 86.267  114.887 1.00 23.94 ? 737  LEU   A CG    1 
ATOM   5410  C  CD1   . LEU   A  1  739  ? -34.962 86.571  114.079 1.00 23.07 ? 737  LEU   A CD1   1 
ATOM   5411  C  CD2   . LEU   A  1  739  ? -33.940 86.628  116.346 1.00 25.19 ? 737  LEU   A CD2   1 
ATOM   5412  N  N     . ILE   A  1  740  ? -31.558 82.384  114.052 1.00 21.66 ? 738  ILE   A N     1 
ATOM   5413  C  CA    . ILE   A  1  740  ? -31.370 80.948  113.889 1.00 22.81 ? 738  ILE   A CA    1 
ATOM   5414  C  C     . ILE   A  1  740  ? -30.164 80.489  114.690 1.00 22.07 ? 738  ILE   A C     1 
ATOM   5415  O  O     . ILE   A  1  740  ? -30.139 79.369  115.212 1.00 23.78 ? 738  ILE   A O     1 
ATOM   5416  C  CB    . ILE   A  1  740  ? -31.302 80.567  112.400 1.00 24.46 ? 738  ILE   A CB    1 
ATOM   5417  C  CG1   . ILE   A  1  740  ? -31.245 79.051  112.228 1.00 23.70 ? 738  ILE   A CG1   1 
ATOM   5418  C  CG2   . ILE   A  1  740  ? -30.108 81.214  111.733 1.00 23.82 ? 738  ILE   A CG2   1 
ATOM   5419  C  CD1   . ILE   A  1  740  ? -32.487 78.340  112.717 1.00 25.60 ? 738  ILE   A CD1   1 
ATOM   5420  N  N     . ALA   A  1  741  ? -29.166 81.358  114.833 1.00 22.67 ? 739  ALA   A N     1 
ATOM   5421  C  CA    . ALA   A  1  741  ? -28.022 81.039  115.676 1.00 25.04 ? 739  ALA   A CA    1 
ATOM   5422  C  C     . ALA   A  1  741  ? -28.452 80.869  117.123 1.00 23.92 ? 739  ALA   A C     1 
ATOM   5423  O  O     . ALA   A  1  741  ? -28.036 79.921  117.801 1.00 24.73 ? 739  ALA   A O     1 
ATOM   5424  C  CB    . ALA   A  1  741  ? -26.987 82.149  115.565 1.00 27.41 ? 739  ALA   A CB    1 
ATOM   5425  N  N     . ALA   A  1  742  ? -29.288 81.787  117.616 1.00 23.99 ? 740  ALA   A N     1 
ATOM   5426  C  CA    . ALA   A  1  742  ? -29.758 81.677  118.987 1.00 22.90 ? 740  ALA   A CA    1 
ATOM   5427  C  C     . ALA   A  1  742  ? -30.559 80.403  119.176 1.00 24.35 ? 740  ALA   A C     1 
ATOM   5428  O  O     . ALA   A  1  742  ? -30.483 79.763  120.231 1.00 26.40 ? 740  ALA   A O     1 
ATOM   5429  C  CB    . ALA   A  1  742  ? -30.596 82.900  119.355 1.00 24.18 ? 740  ALA   A CB    1 
ATOM   5430  N  N     . GLU   A  1  743  ? -31.326 80.013  118.158 1.00 23.04 ? 741  GLU   A N     1 
ATOM   5431  C  CA    . GLU   A  1  743  ? -32.077 78.772  118.258 1.00 26.82 ? 741  GLU   A CA    1 
ATOM   5432  C  C     . GLU   A  1  743  ? -31.140 77.567  118.248 1.00 23.92 ? 741  GLU   A C     1 
ATOM   5433  O  O     . GLU   A  1  743  ? -31.353 76.601  118.992 1.00 24.38 ? 741  GLU   A O     1 
ATOM   5434  C  CB    . GLU   A  1  743  ? -33.126 78.716  117.143 1.00 23.90 ? 741  GLU   A CB    1 
ATOM   5435  C  CG    . GLU   A  1  743  ? -33.871 77.409  117.032 1.00 29.07 ? 741  GLU   A CG    1 
ATOM   5436  C  CD    . GLU   A  1  743  ? -34.824 77.143  118.184 1.00 25.25 ? 741  GLU   A CD    1 
ATOM   5437  O  OE1   . GLU   A  1  743  ? -35.002 78.015  119.066 1.00 26.96 ? 741  GLU   A OE1   1 
ATOM   5438  O  OE2   . GLU   A  1  743  ? -35.385 76.029  118.210 1.00 31.53 ? 741  GLU   A OE2   1 
ATOM   5439  N  N     . GLY   A  1  744  ? -30.076 77.620  117.441 1.00 24.70 ? 742  GLY   A N     1 
ATOM   5440  C  CA    . GLY   A  1  744  ? -29.092 76.552  117.471 1.00 24.41 ? 742  GLY   A CA    1 
ATOM   5441  C  C     . GLY   A  1  744  ? -28.421 76.420  118.825 1.00 23.69 ? 742  GLY   A C     1 
ATOM   5442  O  O     . GLY   A  1  744  ? -28.235 75.311  119.331 1.00 24.79 ? 742  GLY   A O     1 
ATOM   5443  N  N     . VAL   A  1  745  ? -28.071 77.552  119.442 1.00 24.19 ? 743  VAL   A N     1 
ATOM   5444  C  CA    . VAL   A  1  745  ? -27.490 77.522  120.783 1.00 24.57 ? 743  VAL   A CA    1 
ATOM   5445  C  C     . VAL   A  1  745  ? -28.490 76.970  121.792 1.00 25.07 ? 743  VAL   A C     1 
ATOM   5446  O  O     . VAL   A  1  745  ? -28.132 76.195  122.690 1.00 26.84 ? 743  VAL   A O     1 
ATOM   5447  C  CB    . VAL   A  1  745  ? -26.986 78.924  121.173 1.00 25.76 ? 743  VAL   A CB    1 
ATOM   5448  C  CG1   . VAL   A  1  745  ? -26.732 79.017  122.679 1.00 28.22 ? 743  VAL   A CG1   1 
ATOM   5449  C  CG2   . VAL   A  1  745  ? -25.717 79.254  120.396 1.00 28.67 ? 743  VAL   A CG2   1 
ATOM   5450  N  N     . ARG   A  1  746  ? -29.758 77.355  121.659 1.00 26.04 ? 744  ARG   A N     1 
ATOM   5451  C  CA    . ARG   A  1  746  ? -30.769 76.841  122.572 1.00 25.46 ? 744  ARG   A CA    1 
ATOM   5452  C  C     . ARG   A  1  746  ? -30.876 75.326  122.451 1.00 25.27 ? 744  ARG   A C     1 
ATOM   5453  O  O     . ARG   A  1  746  ? -30.963 74.615  123.456 1.00 28.09 ? 744  ARG   A O     1 
ATOM   5454  C  CB    . ARG   A  1  746  ? -32.106 77.507  122.258 1.00 27.68 ? 744  ARG   A CB    1 
ATOM   5455  C  CG    . ARG   A  1  746  ? -33.193 77.189  123.253 1.00 28.97 ? 744  ARG   A CG    1 
ATOM   5456  C  CD    . ARG   A  1  746  ? -34.576 77.499  122.699 1.00 28.53 ? 744  ARG   A CD    1 
ATOM   5457  N  NE    . ARG   A  1  746  ? -34.929 76.601  121.607 1.00 30.08 ? 744  ARG   A NE    1 
ATOM   5458  C  CZ    . ARG   A  1  746  ? -35.275 75.331  121.766 1.00 31.03 ? 744  ARG   A CZ    1 
ATOM   5459  N  NH1   . ARG   A  1  746  ? -35.349 74.779  122.968 1.00 35.21 ? 744  ARG   A NH1   1 
ATOM   5460  N  NH2   . ARG   A  1  746  ? -35.554 74.596  120.694 1.00 30.13 ? 744  ARG   A NH2   1 
ATOM   5461  N  N     . ILE   A  1  747  ? -30.826 74.813  121.221 1.00 25.56 ? 745  ILE   A N     1 
ATOM   5462  C  CA    . ILE   A  1  747  ? -30.896 73.371  121.002 1.00 25.91 ? 745  ILE   A CA    1 
ATOM   5463  C  C     . ILE   A  1  747  ? -29.674 72.667  121.580 1.00 24.91 ? 745  ILE   A C     1 
ATOM   5464  O  O     . ILE   A  1  747  ? -29.794 71.626  122.235 1.00 25.12 ? 745  ILE   A O     1 
ATOM   5465  C  CB    . ILE   A  1  747  ? -31.083 73.076  119.507 1.00 24.24 ? 745  ILE   A CB    1 
ATOM   5466  C  CG1   . ILE   A  1  747  ? -32.513 73.446  119.096 1.00 25.17 ? 745  ILE   A CG1   1 
ATOM   5467  C  CG2   . ILE   A  1  747  ? -30.743 71.614  119.207 1.00 27.04 ? 745  ILE   A CG2   1 
ATOM   5468  C  CD1   . ILE   A  1  747  ? -32.725 73.539  117.607 1.00 24.80 ? 745  ILE   A CD1   1 
ATOM   5469  N  N     . LEU   A  1  748  ? -28.476 73.203  121.328 1.00 25.64 ? 746  LEU   A N     1 
ATOM   5470  C  CA    . LEU   A  1  748  ? -27.273 72.616  121.910 1.00 25.46 ? 746  LEU   A CA    1 
ATOM   5471  C  C     . LEU   A  1  748  ? -27.343 72.610  123.433 1.00 28.03 ? 746  LEU   A C     1 
ATOM   5472  O  O     . LEU   A  1  748  ? -26.999 71.611  124.078 1.00 25.70 ? 746  LEU   A O     1 
ATOM   5473  C  CB    . LEU   A  1  748  ? -26.041 73.373  121.418 1.00 23.60 ? 746  LEU   A CB    1 
ATOM   5474  C  CG    . LEU   A  1  748  ? -25.537 72.899  120.063 1.00 27.44 ? 746  LEU   A CG    1 
ATOM   5475  C  CD1   . LEU   A  1  748  ? -24.521 73.879  119.500 1.00 29.61 ? 746  LEU   A CD1   1 
ATOM   5476  C  CD2   . LEU   A  1  748  ? -24.915 71.529  120.235 1.00 27.72 ? 746  LEU   A CD2   1 
ATOM   5477  N  N     . ARG   A  1  749  ? -27.800 73.711  124.023 1.00 25.31 ? 747  ARG   A N     1 
ATOM   5478  C  CA    . ARG   A  1  749  ? -27.946 73.750  125.471 1.00 26.80 ? 747  ARG   A CA    1 
ATOM   5479  C  C     . ARG   A  1  749  ? -28.978 72.737  125.949 1.00 27.60 ? 747  ARG   A C     1 
ATOM   5480  O  O     . ARG   A  1  749  ? -28.771 72.060  126.966 1.00 30.60 ? 747  ARG   A O     1 
ATOM   5481  C  CB    . ARG   A  1  749  ? -28.288 75.171  125.917 1.00 28.57 ? 747  ARG   A CB    1 
ATOM   5482  C  CG    . ARG   A  1  749  ? -27.079 76.103  125.909 1.00 31.97 ? 747  ARG   A CG    1 
ATOM   5483  C  CD    . ARG   A  1  749  ? -27.444 77.497  126.368 1.00 35.30 ? 747  ARG   A CD    1 
ATOM   5484  N  NE    . ARG   A  1  749  ? -26.278 78.354  126.571 1.00 32.68 ? 747  ARG   A NE    1 
ATOM   5485  C  CZ    . ARG   A  1  749  ? -26.306 79.449  127.320 1.00 32.68 ? 747  ARG   A CZ    1 
ATOM   5486  N  NH1   . ARG   A  1  749  ? -27.409 79.826  127.944 1.00 34.31 ? 747  ARG   A NH1   1 
ATOM   5487  N  NH2   . ARG   A  1  749  ? -25.200 80.175  127.464 1.00 33.21 ? 747  ARG   A NH2   1 
ATOM   5488  N  N     . GLU   A  1  750  ? -30.097 72.614  125.230 1.00 26.12 ? 748  GLU   A N     1 
ATOM   5489  C  CA    . GLU   A  1  750  ? -31.079 71.597  125.590 1.00 30.27 ? 748  GLU   A CA    1 
ATOM   5490  C  C     . GLU   A  1  750  ? -30.493 70.194  125.486 1.00 28.84 ? 748  GLU   A C     1 
ATOM   5491  O  O     . GLU   A  1  750  ? -30.833 69.313  126.283 1.00 29.02 ? 748  GLU   A O     1 
ATOM   5492  C  CB    . GLU   A  1  750  ? -32.313 71.722  124.700 1.00 28.79 ? 748  GLU   A CB    1 
ATOM   5493  C  CG    . GLU   A  1  750  ? -33.409 70.746  125.063 1.00 30.09 ? 748  GLU   A CG    1 
ATOM   5494  C  CD    . GLU   A  1  750  ? -34.581 70.813  124.112 1.00 34.36 ? 748  GLU   A CD    1 
ATOM   5495  O  OE1   . GLU   A  1  750  ? -34.802 71.888  123.518 1.00 41.97 ? 748  GLU   A OE1   1 
ATOM   5496  O  OE2   . GLU   A  1  750  ? -35.270 69.785  123.951 1.00 33.88 ? 748  GLU   A OE2   1 
ATOM   5497  N  N     . ALA   A  1  751  ? -29.587 69.978  124.541 1.00 26.04 ? 749  ALA   A N     1 
ATOM   5498  C  CA    . ALA   A  1  751  ? -28.969 68.675  124.367 1.00 28.10 ? 749  ALA   A CA    1 
ATOM   5499  C  C     . ALA   A  1  751  ? -27.937 68.362  125.436 1.00 28.27 ? 749  ALA   A C     1 
ATOM   5500  O  O     . ALA   A  1  751  ? -27.414 67.244  125.458 1.00 30.69 ? 749  ALA   A O     1 
ATOM   5501  C  CB    . ALA   A  1  751  ? -28.321 68.593  122.984 1.00 25.44 ? 749  ALA   A CB    1 
ATOM   5502  N  N     . GLY   A  1  752  ? -27.631 69.314  126.312 1.00 26.92 ? 750  GLY   A N     1 
ATOM   5503  C  CA    . GLY   A  1  752  ? -26.760 69.071  127.447 1.00 29.24 ? 750  GLY   A CA    1 
ATOM   5504  C  C     . GLY   A  1  752  ? -25.492 69.892  127.462 1.00 27.32 ? 750  GLY   A C     1 
ATOM   5505  O  O     . GLY   A  1  752  ? -24.713 69.764  128.413 1.00 29.62 ? 750  GLY   A O     1 
ATOM   5506  N  N     . ILE   A  1  753  ? -25.214 70.714  126.454 1.00 28.69 ? 751  ILE   A N     1 
ATOM   5507  C  CA    . ILE   A  1  753  ? -24.050 71.594  126.519 1.00 28.88 ? 751  ILE   A CA    1 
ATOM   5508  C  C     . ILE   A  1  753  ? -24.299 72.600  127.633 1.00 28.71 ? 751  ILE   A C     1 
ATOM   5509  O  O     . ILE   A  1  753  ? -25.275 73.356  127.561 1.00 29.33 ? 751  ILE   A O     1 
ATOM   5510  C  CB    . ILE   A  1  753  ? -23.820 72.334  125.196 1.00 24.50 ? 751  ILE   A CB    1 
ATOM   5511  C  CG1   . ILE   A  1  753  ? -23.624 71.350  124.043 1.00 25.92 ? 751  ILE   A CG1   1 
ATOM   5512  C  CG2   . ILE   A  1  753  ? -22.602 73.233  125.340 1.00 27.08 ? 751  ILE   A CG2   1 
ATOM   5513  C  CD1   . ILE   A  1  753  ? -22.348 70.534  124.148 1.00 25.37 ? 751  ILE   A CD1   1 
ATOM   5514  N  N     . PRO   A  1  754  ? -23.458 72.655  128.667 1.00 29.16 ? 752  PRO   A N     1 
ATOM   5515  C  CA    . PRO   A  1  754  ? -23.685 73.624  129.744 1.00 28.57 ? 752  PRO   A CA    1 
ATOM   5516  C  C     . PRO   A  1  754  ? -23.594 75.050  129.228 1.00 29.26 ? 752  PRO   A C     1 
ATOM   5517  O  O     . PRO   A  1  754  ? -22.869 75.344  128.274 1.00 26.93 ? 752  PRO   A O     1 
ATOM   5518  C  CB    . PRO   A  1  754  ? -22.548 73.334  130.733 1.00 34.15 ? 752  PRO   A CB    1 
ATOM   5519  C  CG    . PRO   A  1  754  ? -22.003 72.006  130.350 1.00 32.31 ? 752  PRO   A CG    1 
ATOM   5520  C  CD    . PRO   A  1  754  ? -22.232 71.874  128.879 1.00 31.12 ? 752  PRO   A CD    1 
ATOM   5521  N  N     . ALA   A  1  755  ? -24.338 75.943  129.885 1.00 30.81 ? 753  ALA   A N     1 
ATOM   5522  C  CA    . ALA   A  1  755  ? -24.312 77.358  129.524 1.00 28.89 ? 753  ALA   A CA    1 
ATOM   5523  C  C     . ALA   A  1  755  ? -22.901 77.933  129.587 1.00 29.63 ? 753  ALA   A C     1 
ATOM   5524  O  O     . ALA   A  1  755  ? -22.552 78.812  128.790 1.00 30.79 ? 753  ALA   A O     1 
ATOM   5525  C  CB    . ALA   A  1  755  ? -25.243 78.149  130.449 1.00 28.98 ? 753  ALA   A CB    1 
ATOM   5526  N  N     . SER   A  1  756  ? -22.073 77.443  130.510 1.00 30.41 ? 754  SER   A N     1 
ATOM   5527  C  CA    . SER   A  1  756  ? -20.715 77.954  130.624 1.00 30.86 ? 754  SER   A CA    1 
ATOM   5528  C  C     . SER   A  1  756  ? -19.850 77.510  129.453 1.00 29.73 ? 754  SER   A C     1 
ATOM   5529  O  O     . SER   A  1  756  ? -18.860 78.175  129.130 1.00 31.51 ? 754  SER   A O     1 
ATOM   5530  C  CB    . SER   A  1  756  ? -20.107 77.491  131.945 1.00 34.55 ? 754  SER   A CB    1 
ATOM   5531  O  OG    . SER   A  1  756  ? -20.049 76.075  132.003 1.00 34.74 ? 754  SER   A OG    1 
ATOM   5532  N  N     . ALA   A  1  757  ? -20.205 76.396  128.813 1.00 29.25 ? 755  ALA   A N     1 
ATOM   5533  C  CA    . ALA   A  1  757  ? -19.444 75.882  127.684 1.00 25.78 ? 755  ALA   A CA    1 
ATOM   5534  C  C     . ALA   A  1  757  ? -19.871 76.479  126.355 1.00 27.93 ? 755  ALA   A C     1 
ATOM   5535  O  O     . ALA   A  1  757  ? -19.115 76.389  125.387 1.00 25.45 ? 755  ALA   A O     1 
ATOM   5536  C  CB    . ALA   A  1  757  ? -19.593 74.361  127.593 1.00 29.06 ? 755  ALA   A CB    1 
ATOM   5537  N  N     . LEU   A  1  758  ? -21.059 77.071  126.272 1.00 24.77 ? 756  LEU   A N     1 
ATOM   5538  C  CA    . LEU   A  1  758  ? -21.546 77.614  125.005 1.00 23.95 ? 756  LEU   A CA    1 
ATOM   5539  C  C     . LEU   A  1  758  ? -22.266 78.922  125.297 1.00 26.61 ? 756  LEU   A C     1 
ATOM   5540  O  O     . LEU   A  1  758  ? -23.394 78.923  125.799 1.00 29.26 ? 756  LEU   A O     1 
ATOM   5541  C  CB    . LEU   A  1  758  ? -22.449 76.629  124.285 1.00 25.68 ? 756  LEU   A CB    1 
ATOM   5542  C  CG    . LEU   A  1  758  ? -23.062 77.153  122.991 1.00 24.19 ? 756  LEU   A CG    1 
ATOM   5543  C  CD1   . LEU   A  1  758  ? -22.002 77.711  122.043 1.00 23.92 ? 756  LEU   A CD1   1 
ATOM   5544  C  CD2   . LEU   A  1  758  ? -23.839 76.036  122.341 1.00 26.21 ? 756  LEU   A CD2   1 
ATOM   5545  N  N     . GLN   A  1  759  ? -21.603 80.026  124.992 1.00 25.02 ? 757  GLN   A N     1 
ATOM   5546  C  CA    . GLN   A  1  759  ? -22.157 81.357  125.167 1.00 28.47 ? 757  GLN   A CA    1 
ATOM   5547  C  C     . GLN   A  1  759  ? -22.411 81.973  123.802 1.00 27.92 ? 757  GLN   A C     1 
ATOM   5548  O  O     . GLN   A  1  759  ? -21.538 81.942  122.926 1.00 29.31 ? 757  GLN   A O     1 
ATOM   5549  C  CB    . GLN   A  1  759  ? -21.189 82.225  125.962 1.00 28.75 ? 757  GLN   A CB    1 
ATOM   5550  C  CG    . GLN   A  1  759  ? -21.041 81.774  127.384 1.00 31.53 ? 757  GLN   A CG    1 
ATOM   5551  C  CD    . GLN   A  1  759  ? -20.024 82.598  128.118 1.00 29.18 ? 757  GLN   A CD    1 
ATOM   5552  O  OE1   . GLN   A  1  759  ? -20.361 83.591  128.764 1.00 29.03 ? 757  GLN   A OE1   1 
ATOM   5553  N  NE2   . GLN   A  1  759  ? -18.759 82.206  128.008 1.00 28.03 ? 757  GLN   A NE2   1 
ATOM   5554  N  N     . LEU   A  1  760  ? -23.607 82.512  123.619 1.00 28.44 ? 758  LEU   A N     1 
ATOM   5555  C  CA    . LEU   A  1  760  ? -23.980 83.175  122.379 1.00 27.28 ? 758  LEU   A CA    1 
ATOM   5556  C  C     . LEU   A  1  760  ? -23.784 84.672  122.555 1.00 26.97 ? 758  LEU   A C     1 
ATOM   5557  O  O     . LEU   A  1  760  ? -24.265 85.254  123.528 1.00 27.80 ? 758  LEU   A O     1 
ATOM   5558  C  CB    . LEU   A  1  760  ? -25.438 82.887  122.034 1.00 27.66 ? 758  LEU   A CB    1 
ATOM   5559  C  CG    . LEU   A  1  760  ? -25.915 83.596  120.768 1.00 26.61 ? 758  LEU   A CG    1 
ATOM   5560  C  CD1   . LEU   A  1  760  ? -25.495 82.813  119.550 1.00 25.27 ? 758  LEU   A CD1   1 
ATOM   5561  C  CD2   . LEU   A  1  760  ? -27.426 83.813  120.786 1.00 28.05 ? 758  LEU   A CD2   1 
ATOM   5562  N  N     . LEU   A  1  761  ? -23.071 85.290  121.620 1.00 25.53 ? 759  LEU   A N     1 
ATOM   5563  C  CA    A LEU   A  1  761  ? -22.744 86.711  121.681 0.42 27.65 ? 759  LEU   A CA    1 
ATOM   5564  C  CA    B LEU   A  1  761  ? -22.740 86.714  121.680 0.58 27.66 ? 759  LEU   A CA    1 
ATOM   5565  C  C     . LEU   A  1  761  ? -23.167 87.359  120.370 1.00 28.25 ? 759  LEU   A C     1 
ATOM   5566  O  O     . LEU   A  1  761  ? -22.355 87.544  119.457 1.00 26.01 ? 759  LEU   A O     1 
ATOM   5567  C  CB    A LEU   A  1  761  ? -21.259 86.906  121.987 0.42 27.50 ? 759  LEU   A CB    1 
ATOM   5568  C  CB    B LEU   A  1  761  ? -21.248 86.940  121.933 0.58 27.50 ? 759  LEU   A CB    1 
ATOM   5569  C  CG    A LEU   A  1  761  ? -20.888 86.214  123.302 0.42 28.31 ? 759  LEU   A CG    1 
ATOM   5570  C  CG    B LEU   A  1  761  ? -20.584 86.387  123.200 0.58 27.86 ? 759  LEU   A CG    1 
ATOM   5571  C  CD1   A LEU   A  1  761  ? -19.407 85.942  123.421 0.42 26.32 ? 759  LEU   A CD1   1 
ATOM   5572  C  CD1   B LEU   A  1  761  ? -21.473 86.574  124.420 0.58 26.80 ? 759  LEU   A CD1   1 
ATOM   5573  C  CD2   A LEU   A  1  761  ? -21.377 87.039  124.478 0.42 27.64 ? 759  LEU   A CD2   1 
ATOM   5574  C  CD2   B LEU   A  1  761  ? -20.192 84.929  123.026 0.58 27.25 ? 759  LEU   A CD2   1 
ATOM   5575  N  N     . PRO   A  1  762  ? -24.438 87.702  120.235 1.00 26.76 ? 760  PRO   A N     1 
ATOM   5576  C  CA    . PRO   A  1  762  ? -24.885 88.365  119.009 1.00 27.61 ? 760  PRO   A CA    1 
ATOM   5577  C  C     . PRO   A  1  762  ? -24.243 89.735  118.879 1.00 30.08 ? 760  PRO   A C     1 
ATOM   5578  O  O     . PRO   A  1  762  ? -23.886 90.380  119.868 1.00 29.51 ? 760  PRO   A O     1 
ATOM   5579  C  CB    . PRO   A  1  762  ? -26.401 88.489  119.205 1.00 26.40 ? 760  PRO   A CB    1 
ATOM   5580  C  CG    . PRO   A  1  762  ? -26.742 87.493  120.269 1.00 27.06 ? 760  PRO   A CG    1 
ATOM   5581  C  CD    . PRO   A  1  762  ? -25.547 87.455  121.170 1.00 25.23 ? 760  PRO   A CD    1 
ATOM   5582  N  N     . GLY   A  1  763  ? -24.080 90.173  117.648 1.00 27.21 ? 761  GLY   A N     1 
ATOM   5583  C  CA    . GLY   A  1  763  ? -23.519 91.485  117.397 1.00 31.02 ? 761  GLY   A CA    1 
ATOM   5584  C  C     . GLY   A  1  763  ? -22.784 91.490  116.076 1.00 30.48 ? 761  GLY   A C     1 
ATOM   5585  O  O     . GLY   A  1  763  ? -22.756 90.500  115.349 1.00 26.28 ? 761  GLY   A O     1 
ATOM   5586  N  N     . ASP   A  1  764  ? -22.172 92.634  115.787 1.00 30.62 ? 762  ASP   A N     1 
ATOM   5587  C  CA    . ASP   A  1  764  ? -21.485 92.818  114.516 1.00 31.25 ? 762  ASP   A CA    1 
ATOM   5588  C  C     . ASP   A  1  764  ? -20.004 92.453  114.661 1.00 30.85 ? 762  ASP   A C     1 
ATOM   5589  O  O     . ASP   A  1  764  ? -19.604 91.756  115.600 1.00 28.09 ? 762  ASP   A O     1 
ATOM   5590  C  CB    . ASP   A  1  764  ? -21.753 94.225  113.968 1.00 36.00 ? 762  ASP   A CB    1 
ATOM   5591  C  CG    . ASP   A  1  764  ? -21.244 95.320  114.883 1.00 35.44 ? 762  ASP   A CG    1 
ATOM   5592  O  OD1   . ASP   A  1  764  ? -20.339 95.057  115.697 1.00 36.91 ? 762  ASP   A OD1   1 
ATOM   5593  O  OD2   . ASP   A  1  764  ? -21.763 96.452  114.800 1.00 44.57 ? 762  ASP   A OD2   1 
ATOM   5594  N  N     . GLY   A  1  765  ? -19.174 92.928  113.731 1.00 29.95 ? 763  GLY   A N     1 
ATOM   5595  C  CA    . GLY   A  1  765  ? -17.763 92.586  113.740 1.00 29.66 ? 763  GLY   A CA    1 
ATOM   5596  C  C     . GLY   A  1  765  ? -17.021 93.067  114.970 1.00 29.39 ? 763  GLY   A C     1 
ATOM   5597  O  O     . GLY   A  1  765  ? -15.988 92.484  115.325 1.00 31.37 ? 763  GLY   A O     1 
ATOM   5598  N  N     . ARG   A  1  766  ? -17.519 94.123  115.625 1.00 30.96 ? 764  ARG   A N     1 
ATOM   5599  C  CA    . ARG   A  1  766  ? -16.909 94.599  116.863 1.00 31.39 ? 764  ARG   A CA    1 
ATOM   5600  C  C     . ARG   A  1  766  ? -16.948 93.527  117.937 1.00 30.82 ? 764  ARG   A C     1 
ATOM   5601  O  O     . ARG   A  1  766  ? -16.007 93.396  118.730 1.00 31.81 ? 764  ARG   A O     1 
ATOM   5602  C  CB    . ARG   A  1  766  ? -17.662 95.819  117.386 1.00 37.62 ? 764  ARG   A CB    1 
ATOM   5603  C  CG    . ARG   A  1  766  ? -17.646 97.028  116.497 1.00 44.44 ? 764  ARG   A CG    1 
ATOM   5604  C  CD    . ARG   A  1  766  ? -18.528 98.091  117.115 1.00 39.81 ? 764  ARG   A CD    1 
ATOM   5605  N  NE    . ARG   A  1  766  ? -19.939 97.735  117.025 1.00 41.49 ? 764  ARG   A NE    1 
ATOM   5606  C  CZ    . ARG   A  1  766  ? -20.869 98.121  117.889 1.00 46.50 ? 764  ARG   A CZ    1 
ATOM   5607  N  NH1   . ARG   A  1  766  ? -20.561 98.822  118.969 1.00 48.06 ? 764  ARG   A NH1   1 
ATOM   5608  N  NH2   . ARG   A  1  766  ? -22.139 97.795  117.665 1.00 46.15 ? 764  ARG   A NH2   1 
ATOM   5609  N  N     . VAL   A  1  767  ? -18.054 92.786  118.012 1.00 28.61 ? 765  VAL   A N     1 
ATOM   5610  C  CA    . VAL   A  1  767  ? -18.148 91.710  118.989 1.00 32.46 ? 765  VAL   A CA    1 
ATOM   5611  C  C     . VAL   A  1  767  ? -17.182 90.597  118.629 1.00 28.73 ? 765  VAL   A C     1 
ATOM   5612  O  O     . VAL   A  1  767  ? -16.477 90.061  119.493 1.00 28.73 ? 765  VAL   A O     1 
ATOM   5613  C  CB    . VAL   A  1  767  ? -19.601 91.215  119.107 1.00 27.78 ? 765  VAL   A CB    1 
ATOM   5614  C  CG1   . VAL   A  1  767  ? -19.705 90.128  120.166 1.00 29.27 ? 765  VAL   A CG1   1 
ATOM   5615  C  CG2   . VAL   A  1  767  ? -20.533 92.379  119.418 1.00 30.94 ? 765  VAL   A CG2   1 
ATOM   5616  N  N     . GLY   A  1  768  ? -17.125 90.237  117.344 1.00 27.95 ? 766  GLY   A N     1 
ATOM   5617  C  CA    . GLY   A  1  768  ? -16.129 89.278  116.902 1.00 26.45 ? 766  GLY   A CA    1 
ATOM   5618  C  C     . GLY   A  1  768  ? -14.720 89.721  117.233 1.00 25.92 ? 766  GLY   A C     1 
ATOM   5619  O  O     . GLY   A  1  768  ? -13.926 88.949  117.768 1.00 26.89 ? 766  GLY   A O     1 
ATOM   5620  N  N     . ALA   A  1  769  ? -14.395 90.978  116.925 1.00 28.32 ? 767  ALA   A N     1 
ATOM   5621  C  CA    . ALA   A  1  769  ? -13.044 91.474  117.174 1.00 30.99 ? 767  ALA   A CA    1 
ATOM   5622  C  C     . ALA   A  1  769  ? -12.734 91.488  118.665 1.00 28.64 ? 767  ALA   A C     1 
ATOM   5623  O  O     . ALA   A  1  769  ? -11.627 91.124  119.079 1.00 29.74 ? 767  ALA   A O     1 
ATOM   5624  C  CB    . ALA   A  1  769  ? -12.879 92.871  116.575 1.00 29.97 ? 767  ALA   A CB    1 
ATOM   5625  N  N     . ALA   A  1  770  ? -13.705 91.896  119.486 1.00 28.53 ? 768  ALA   A N     1 
ATOM   5626  C  CA    . ALA   A  1  770  ? -13.484 91.931  120.929 1.00 28.49 ? 768  ALA   A CA    1 
ATOM   5627  C  C     . ALA   A  1  770  ? -13.220 90.534  121.464 1.00 28.86 ? 768  ALA   A C     1 
ATOM   5628  O  O     . ALA   A  1  770  ? -12.409 90.351  122.379 1.00 29.78 ? 768  ALA   A O     1 
ATOM   5629  C  CB    . ALA   A  1  770  ? -14.689 92.553  121.632 1.00 31.64 ? 768  ALA   A CB    1 
ATOM   5630  N  N     . LEU   A  1  771  ? -13.892 89.532  120.896 1.00 28.83 ? 769  LEU   A N     1 
ATOM   5631  C  CA    . LEU   A  1  771  ? -13.661 88.156  121.315 1.00 27.24 ? 769  LEU   A CA    1 
ATOM   5632  C  C     . LEU   A  1  771  ? -12.293 87.671  120.867 1.00 29.11 ? 769  LEU   A C     1 
ATOM   5633  O  O     . LEU   A  1  771  ? -11.585 87.002  121.627 1.00 29.97 ? 769  LEU   A O     1 
ATOM   5634  C  CB    . LEU   A  1  771  ? -14.755 87.253  120.743 1.00 26.95 ? 769  LEU   A CB    1 
ATOM   5635  C  CG    . LEU   A  1  771  ? -16.157 87.491  121.303 1.00 26.30 ? 769  LEU   A CG    1 
ATOM   5636  C  CD1   . LEU   A  1  771  ? -17.177 86.712  120.486 1.00 27.82 ? 769  LEU   A CD1   1 
ATOM   5637  C  CD2   . LEU   A  1  771  ? -16.227 87.104  122.765 1.00 27.93 ? 769  LEU   A CD2   1 
ATOM   5638  N  N     . VAL   A  1  772  ? -11.916 87.978  119.625 1.00 28.52 ? 770  VAL   A N     1 
ATOM   5639  C  CA    . VAL   A  1  772  ? -10.612 87.561  119.117 1.00 27.31 ? 770  VAL   A CA    1 
ATOM   5640  C  C     . VAL   A  1  772  ? -9.498  88.156  119.964 1.00 30.15 ? 770  VAL   A C     1 
ATOM   5641  O  O     . VAL   A  1  772  ? -8.523  87.476  120.298 1.00 32.52 ? 770  VAL   A O     1 
ATOM   5642  C  CB    . VAL   A  1  772  ? -10.470 87.929  117.628 1.00 26.33 ? 770  VAL   A CB    1 
ATOM   5643  C  CG1   . VAL   A  1  772  ? -9.033  87.788  117.173 1.00 28.42 ? 770  VAL   A CG1   1 
ATOM   5644  C  CG2   . VAL   A  1  772  ? -11.371 87.045  116.773 1.00 27.14 ? 770  VAL   A CG2   1 
ATOM   5645  N  N     . ALA   A  1  773  ? -9.635  89.428  120.341 1.00 30.95 ? 771  ALA   A N     1 
ATOM   5646  C  CA    . ALA   A  1  773  ? -8.596  90.126  121.089 1.00 28.83 ? 771  ALA   A CA    1 
ATOM   5647  C  C     . ALA   A  1  773  ? -8.560  89.754  122.565 1.00 34.67 ? 771  ALA   A C     1 
ATOM   5648  O  O     . ALA   A  1  773  ? -7.575  90.083  123.241 1.00 38.24 ? 771  ALA   A O     1 
ATOM   5649  C  CB    . ALA   A  1  773  ? -8.790  91.638  120.963 1.00 33.40 ? 771  ALA   A CB    1 
ATOM   5650  N  N     . ALA   A  1  774  ? -9.592  89.088  123.081 1.00 34.28 ? 772  ALA   A N     1 
ATOM   5651  C  CA    . ALA   A  1  774  ? -9.646  88.791  124.510 1.00 34.34 ? 772  ALA   A CA    1 
ATOM   5652  C  C     . ALA   A  1  774  ? -8.478  87.900  124.921 1.00 33.48 ? 772  ALA   A C     1 
ATOM   5653  O  O     . ALA   A  1  774  ? -8.095  86.973  124.204 1.00 32.62 ? 772  ALA   A O     1 
ATOM   5654  C  CB    . ALA   A  1  774  ? -10.978 88.132  124.872 1.00 34.44 ? 772  ALA   A CB    1 
ATOM   5655  N  N     . ALA   A  1  775  ? -7.913  88.187  126.098 1.00 39.78 ? 773  ALA   A N     1 
ATOM   5656  C  CA    . ALA   A  1  775  ? -6.648  87.566  126.476 1.00 38.74 ? 773  ALA   A CA    1 
ATOM   5657  C  C     . ALA   A  1  775  ? -6.740  86.047  126.558 1.00 32.01 ? 773  ALA   A C     1 
ATOM   5658  O  O     . ALA   A  1  775  ? -5.778  85.353  126.218 1.00 33.42 ? 773  ALA   A O     1 
ATOM   5659  C  CB    . ALA   A  1  775  ? -6.147  88.152  127.797 1.00 39.46 ? 773  ALA   A CB    1 
ATOM   5660  N  N     . GLU   A  1  776  ? -7.876  85.511  126.994 1.00 30.98 ? 774  GLU   A N     1 
ATOM   5661  C  CA    . GLU   A  1  776  ? -8.004  84.077  127.219 1.00 29.08 ? 774  GLU   A CA    1 
ATOM   5662  C  C     . GLU   A  1  776  ? -8.442  83.307  125.978 1.00 30.02 ? 774  GLU   A C     1 
ATOM   5663  O  O     . GLU   A  1  776  ? -8.579  82.081  126.042 1.00 30.03 ? 774  GLU   A O     1 
ATOM   5664  C  CB    . GLU   A  1  776  ? -8.968  83.803  128.376 1.00 30.57 ? 774  GLU   A CB    1 
ATOM   5665  C  CG    . GLU   A  1  776  ? -8.583  84.508  129.673 1.00 33.88 ? 774  GLU   A CG    1 
ATOM   5666  C  CD    . GLU   A  1  776  ? -9.188  85.904  129.810 1.00 42.41 ? 774  GLU   A CD    1 
ATOM   5667  O  OE1   . GLU   A  1  776  ? -9.717  86.450  128.816 1.00 36.66 ? 774  GLU   A OE1   1 
ATOM   5668  O  OE2   . GLU   A  1  776  ? -9.136  86.458  130.929 1.00 47.50 ? 774  GLU   A OE2   1 
ATOM   5669  N  N     . THR   A  1  777  ? -8.647  83.980  124.856 1.00 27.98 ? 775  THR   A N     1 
ATOM   5670  C  CA    . THR   A  1  777  ? -9.040  83.284  123.638 1.00 26.63 ? 775  THR   A CA    1 
ATOM   5671  C  C     . THR   A  1  777  ? -7.909  82.376  123.183 1.00 26.93 ? 775  THR   A C     1 
ATOM   5672  O  O     . THR   A  1  777  ? -6.789  82.839  122.941 1.00 29.62 ? 775  THR   A O     1 
ATOM   5673  C  CB    . THR   A  1  777  ? -9.367  84.301  122.558 1.00 26.42 ? 775  THR   A CB    1 
ATOM   5674  O  OG1   . THR   A  1  777  ? -10.567 84.983  122.929 1.00 27.14 ? 775  THR   A OG1   1 
ATOM   5675  C  CG2   . THR   A  1  777  ? -9.547  83.589  121.215 1.00 24.67 ? 775  THR   A CG2   1 
ATOM   5676  N  N     . ALA   A  1  778  ? -8.196  81.080  123.076 1.00 24.35 ? 776  ALA   A N     1 
ATOM   5677  C  CA    . ALA   A  1  778  ? -7.170  80.092  122.779 1.00 24.57 ? 776  ALA   A CA    1 
ATOM   5678  C  C     . ALA   A  1  778  ? -7.211  79.579  121.351 1.00 23.64 ? 776  ALA   A C     1 
ATOM   5679  O  O     . ALA   A  1  778  ? -6.296  78.862  120.943 1.00 24.61 ? 776  ALA   A O     1 
ATOM   5680  C  CB    . ALA   A  1  778  ? -7.265  78.905  123.750 1.00 26.12 ? 776  ALA   A CB    1 
ATOM   5681  N  N     . GLY   A  1  779  ? -8.243  79.912  120.597 1.00 22.85 ? 777  GLY   A N     1 
ATOM   5682  C  CA    . GLY   A  1  779  ? -8.291  79.565  119.198 1.00 21.39 ? 777  GLY   A CA    1 
ATOM   5683  C  C     . GLY   A  1  779  ? -9.470  80.270  118.582 1.00 22.03 ? 777  GLY   A C     1 
ATOM   5684  O  O     . GLY   A  1  779  ? -10.405 80.678  119.279 1.00 22.63 ? 777  GLY   A O     1 
ATOM   5685  N  N     . VAL   A  1  780  ? -9.408  80.425  117.268 1.00 22.27 ? 778  VAL   A N     1 
ATOM   5686  C  CA    . VAL   A  1  780  ? -10.436 81.141  116.534 1.00 21.80 ? 778  VAL   A CA    1 
ATOM   5687  C  C     . VAL   A  1  780  ? -10.841 80.293  115.345 1.00 21.10 ? 778  VAL   A C     1 
ATOM   5688  O  O     . VAL   A  1  780  ? -9.983  79.829  114.585 1.00 20.87 ? 778  VAL   A O     1 
ATOM   5689  C  CB    . VAL   A  1  780  ? -9.964  82.537  116.086 1.00 21.37 ? 778  VAL   A CB    1 
ATOM   5690  C  CG1   . VAL   A  1  780  ? -11.064 83.233  115.295 1.00 21.78 ? 778  VAL   A CG1   1 
ATOM   5691  C  CG2   . VAL   A  1  780  ? -9.578  83.374  117.304 1.00 22.44 ? 778  VAL   A CG2   1 
ATOM   5692  N  N     . MET   A  1  781  ? -12.138 80.062  115.209 1.00 20.44 ? 779  MET   A N     1 
ATOM   5693  C  CA    . MET   A  1  781  ? -12.697 79.432  114.026 1.00 18.43 ? 779  MET   A CA    1 
ATOM   5694  C  C     . MET   A  1  781  ? -13.521 80.487  113.316 1.00 20.96 ? 779  MET   A C     1 
ATOM   5695  O  O     . MET   A  1  781  ? -14.508 80.981  113.870 1.00 20.72 ? 779  MET   A O     1 
ATOM   5696  C  CB    . MET   A  1  781  ? -13.561 78.236  114.410 1.00 22.18 ? 779  MET   A CB    1 
ATOM   5697  C  CG    . MET   A  1  781  ? -12.815 77.246  115.268 1.00 21.05 ? 779  MET   A CG    1 
ATOM   5698  S  SD    . MET   A  1  781  ? -13.888 75.951  115.865 1.00 21.47 ? 779  MET   A SD    1 
ATOM   5699  C  CE    . MET   A  1  781  ? -14.139 75.016  114.369 1.00 21.46 ? 779  MET   A CE    1 
ATOM   5700  N  N     . PHE   A  1  782  ? -13.091 80.853  112.115 1.00 20.42 ? 780  PHE   A N     1 
ATOM   5701  C  CA    . PHE   A  1  782  ? -13.694 81.917  111.340 1.00 21.34 ? 780  PHE   A CA    1 
ATOM   5702  C  C     . PHE   A  1  782  ? -14.116 81.369  109.993 1.00 20.84 ? 780  PHE   A C     1 
ATOM   5703  O  O     . PHE   A  1  782  ? -13.304 80.776  109.273 1.00 19.56 ? 780  PHE   A O     1 
ATOM   5704  C  CB    . PHE   A  1  782  ? -12.701 83.049  111.078 1.00 20.20 ? 780  PHE   A CB    1 
ATOM   5705  C  CG    . PHE   A  1  782  ? -13.249 84.112  110.178 1.00 21.33 ? 780  PHE   A CG    1 
ATOM   5706  C  CD1   . PHE   A  1  782  ? -14.103 85.081  110.678 1.00 21.82 ? 780  PHE   A CD1   1 
ATOM   5707  C  CD2   . PHE   A  1  782  ? -12.954 84.116  108.819 1.00 20.31 ? 780  PHE   A CD2   1 
ATOM   5708  C  CE1   . PHE   A  1  782  ? -14.632 86.048  109.859 1.00 22.20 ? 780  PHE   A CE1   1 
ATOM   5709  C  CE2   . PHE   A  1  782  ? -13.475 85.083  107.996 1.00 20.68 ? 780  PHE   A CE2   1 
ATOM   5710  C  CZ    . PHE   A  1  782  ? -14.314 86.052  108.516 1.00 20.31 ? 780  PHE   A CZ    1 
ATOM   5711  N  N     . THR   A  1  783  ? -15.367 81.616  109.637 1.00 18.13 ? 781  THR   A N     1 
ATOM   5712  C  CA    . THR   A  1  783  ? -15.826 81.442  108.269 1.00 19.87 ? 781  THR   A CA    1 
ATOM   5713  C  C     . THR   A  1  783  ? -16.462 82.755  107.848 1.00 19.90 ? 781  THR   A C     1 
ATOM   5714  O  O     . THR   A  1  783  ? -17.287 83.309  108.577 1.00 20.10 ? 781  THR   A O     1 
ATOM   5715  C  CB    . THR   A  1  783  ? -16.801 80.270  108.168 1.00 22.16 ? 781  THR   A CB    1 
ATOM   5716  O  OG1   . THR   A  1  783  ? -16.156 79.087  108.663 1.00 20.53 ? 781  THR   A OG1   1 
ATOM   5717  C  CG2   . THR   A  1  783  ? -17.201 80.039  106.726 1.00 18.73 ? 781  THR   A CG2   1 
ATOM   5718  N  N     . GLY   A  1  784  ? -16.041 83.273  106.703 1.00 19.95 ? 782  GLY   A N     1 
ATOM   5719  C  CA    . GLY   A  1  784  ? -16.445 84.605  106.306 1.00 20.50 ? 782  GLY   A CA    1 
ATOM   5720  C  C     . GLY   A  1  784  ? -15.576 85.081  105.164 1.00 18.36 ? 782  GLY   A C     1 
ATOM   5721  O  O     . GLY   A  1  784  ? -14.923 84.279  104.497 1.00 20.19 ? 782  GLY   A O     1 
ATOM   5722  N  N     . SER   A  1  785  ? -15.569 86.391  104.958 1.00 20.54 ? 783  SER   A N     1 
ATOM   5723  C  CA    . SER   A  1  785  ? -14.834 86.940  103.829 1.00 21.23 ? 783  SER   A CA    1 
ATOM   5724  C  C     . SER   A  1  785  ? -13.330 86.894  104.073 1.00 22.29 ? 783  SER   A C     1 
ATOM   5725  O  O     . SER   A  1  785  ? -12.857 86.939  105.211 1.00 22.06 ? 783  SER   A O     1 
ATOM   5726  C  CB    . SER   A  1  785  ? -15.263 88.381  103.571 1.00 23.22 ? 783  SER   A CB    1 
ATOM   5727  O  OG    . SER   A  1  785  ? -14.934 89.205  104.669 1.00 24.33 ? 783  SER   A OG    1 
ATOM   5728  N  N     . THR   A  1  786  ? -12.578 86.793  102.976 1.00 20.39 ? 784  THR   A N     1 
ATOM   5729  C  CA    . THR   A  1  786  ? -11.125 86.816  103.070 1.00 21.79 ? 784  THR   A CA    1 
ATOM   5730  C  C     . THR   A  1  786  ? -10.626 88.096  103.728 1.00 21.17 ? 784  THR   A C     1 
ATOM   5731  O  O     . THR   A  1  786  ? -9.682  88.067  104.528 1.00 22.13 ? 784  THR   A O     1 
ATOM   5732  C  CB    . THR   A  1  786  ? -10.533 86.636  101.675 1.00 24.41 ? 784  THR   A CB    1 
ATOM   5733  O  OG1   . THR   A  1  786  ? -11.032 85.417  101.127 1.00 24.09 ? 784  THR   A OG1   1 
ATOM   5734  C  CG2   . THR   A  1  786  ? -9.025  86.581  101.744 1.00 25.05 ? 784  THR   A CG2   1 
ATOM   5735  N  N     . GLU   A  1  787  ? -11.265 89.231  103.425 1.00 26.40 ? 785  GLU   A N     1 
ATOM   5736  C  CA    . GLU   A  1  787  ? -10.804 90.499  103.979 1.00 25.92 ? 785  GLU   A CA    1 
ATOM   5737  C  C     . GLU   A  1  787  ? -10.976 90.537  105.490 1.00 23.45 ? 785  GLU   A C     1 
ATOM   5738  O  O     . GLU   A  1  787  ? -10.105 91.040  106.205 1.00 24.46 ? 785  GLU   A O     1 
ATOM   5739  C  CB    . GLU   A  1  787  ? -11.538 91.670  103.324 1.00 27.96 ? 785  GLU   A CB    1 
ATOM   5740  N  N     . VAL   A  1  788  ? -12.091 90.006  105.995 1.00 23.45 ? 786  VAL   A N     1 
ATOM   5741  C  CA    . VAL   A  1  788  ? -12.272 89.977  107.444 1.00 22.06 ? 786  VAL   A CA    1 
ATOM   5742  C  C     . VAL   A  1  788  ? -11.298 88.997  108.091 1.00 22.64 ? 786  VAL   A C     1 
ATOM   5743  O  O     . VAL   A  1  788  ? -10.686 89.298  109.122 1.00 23.54 ? 786  VAL   A O     1 
ATOM   5744  C  CB    . VAL   A  1  788  ? -13.740 89.697  107.808 1.00 23.79 ? 786  VAL   A CB    1 
ATOM   5745  C  CG1   . VAL   A  1  788  ? -13.860 89.426  109.293 1.00 24.30 ? 786  VAL   A CG1   1 
ATOM   5746  C  CG2   . VAL   A  1  788  ? -14.611 90.886  107.414 1.00 26.45 ? 786  VAL   A CG2   1 
ATOM   5747  N  N     . ALA   A  1  789  ? -11.113 87.820  107.486 1.00 22.10 ? 787  ALA   A N     1 
ATOM   5748  C  CA    . ALA   A  1  789  ? -10.133 86.876  108.014 1.00 22.06 ? 787  ALA   A CA    1 
ATOM   5749  C  C     . ALA   A  1  789  ? -8.759  87.517  108.122 1.00 21.11 ? 787  ALA   A C     1 
ATOM   5750  O  O     . ALA   A  1  789  ? -8.017  87.263  109.073 1.00 21.13 ? 787  ALA   A O     1 
ATOM   5751  C  CB    . ALA   A  1  789  ? -10.063 85.636  107.125 1.00 19.88 ? 787  ALA   A CB    1 
ATOM   5752  N  N     . ARG   A  1  790  ? -8.406  88.362  107.151 1.00 21.12 ? 788  ARG   A N     1 
ATOM   5753  C  CA    . ARG   A  1  790  ? -7.106  89.020  107.172 1.00 21.98 ? 788  ARG   A CA    1 
ATOM   5754  C  C     . ARG   A  1  790  ? -6.980  89.967  108.364 1.00 21.04 ? 788  ARG   A C     1 
ATOM   5755  O  O     . ARG   A  1  790  ? -5.909  90.076  108.971 1.00 23.83 ? 788  ARG   A O     1 
ATOM   5756  C  CB    . ARG   A  1  790  ? -6.911  89.751  105.845 1.00 26.15 ? 788  ARG   A CB    1 
ATOM   5757  C  CG    . ARG   A  1  790  ? -5.548  90.369  105.677 1.00 23.81 ? 788  ARG   A CG    1 
ATOM   5758  C  CD    . ARG   A  1  790  ? -5.340  90.860  104.240 1.00 25.90 ? 788  ARG   A CD    1 
ATOM   5759  N  NE    . ARG   A  1  790  ? -5.264  89.765  103.279 1.00 24.71 ? 788  ARG   A NE    1 
ATOM   5760  C  CZ    . ARG   A  1  790  ? -6.070  89.606  102.236 1.00 24.41 ? 788  ARG   A CZ    1 
ATOM   5761  N  NH1   . ARG   A  1  790  ? -7.046  90.460  101.973 1.00 28.01 ? 788  ARG   A NH1   1 
ATOM   5762  N  NH2   . ARG   A  1  790  ? -5.887  88.565  101.429 1.00 25.87 ? 788  ARG   A NH2   1 
ATOM   5763  N  N     . LEU   A  1  791  ? -8.077  90.648  108.722 1.00 23.76 ? 789  LEU   A N     1 
ATOM   5764  C  CA    . LEU   A  1  791  ? -8.092  91.479  109.921 1.00 25.14 ? 789  LEU   A CA    1 
ATOM   5765  C  C     . LEU   A  1  791  ? -7.910  90.632  111.174 1.00 24.55 ? 789  LEU   A C     1 
ATOM   5766  O  O     . LEU   A  1  791  ? -7.183  91.015  112.094 1.00 25.88 ? 789  LEU   A O     1 
ATOM   5767  C  CB    . LEU   A  1  791  ? -9.419  92.234  109.995 1.00 25.57 ? 789  LEU   A CB    1 
ATOM   5768  C  CG    . LEU   A  1  791  ? -9.687  93.257  108.890 1.00 29.93 ? 789  LEU   A CG    1 
ATOM   5769  C  CD1   . LEU   A  1  791  ? -11.095 93.808  108.989 1.00 31.96 ? 789  LEU   A CD1   1 
ATOM   5770  C  CD2   . LEU   A  1  791  ? -8.670  94.373  108.960 1.00 31.14 ? 789  LEU   A CD2   1 
ATOM   5771  N  N     . ILE   A  1  792  ? -8.564  89.471  111.226 1.00 23.40 ? 790  ILE   A N     1 
ATOM   5772  C  CA    . ILE   A  1  792  ? -8.398  88.585  112.374 1.00 22.98 ? 790  ILE   A CA    1 
ATOM   5773  C  C     . ILE   A  1  792  ? -6.975  88.049  112.442 1.00 24.55 ? 790  ILE   A C     1 
ATOM   5774  O  O     . ILE   A  1  792  ? -6.368  87.993  113.519 1.00 25.82 ? 790  ILE   A O     1 
ATOM   5775  C  CB    . ILE   A  1  792  ? -9.446  87.462  112.329 1.00 23.56 ? 790  ILE   A CB    1 
ATOM   5776  C  CG1   . ILE   A  1  792  ? -10.825 88.047  112.585 1.00 24.87 ? 790  ILE   A CG1   1 
ATOM   5777  C  CG2   . ILE   A  1  792  ? -9.107  86.367  113.337 1.00 25.00 ? 790  ILE   A CG2   1 
ATOM   5778  C  CD1   . ILE   A  1  792  ? -11.959 87.115  112.255 1.00 23.96 ? 790  ILE   A CD1   1 
ATOM   5779  N  N     . GLN   A  1  793  ? -6.422  87.652  111.295 1.00 22.66 ? 791  GLN   A N     1 
ATOM   5780  C  CA    . GLN   A  1  793  ? -5.037  87.208  111.242 1.00 23.16 ? 791  GLN   A CA    1 
ATOM   5781  C  C     . GLN   A  1  793  ? -4.106  88.270  111.806 1.00 23.26 ? 791  GLN   A C     1 
ATOM   5782  O  O     . GLN   A  1  793  ? -3.183  87.960  112.567 1.00 24.75 ? 791  GLN   A O     1 
ATOM   5783  C  CB    . GLN   A  1  793  ? -4.676  86.898  109.790 1.00 22.91 ? 791  GLN   A CB    1 
ATOM   5784  C  CG    . GLN   A  1  793  ? -3.232  86.500  109.553 1.00 25.48 ? 791  GLN   A CG    1 
ATOM   5785  C  CD    . GLN   A  1  793  ? -2.847  86.551  108.075 1.00 26.36 ? 791  GLN   A CD    1 
ATOM   5786  O  OE1   . GLN   A  1  793  ? -3.314  87.416  107.325 1.00 28.39 ? 791  GLN   A OE1   1 
ATOM   5787  N  NE2   . GLN   A  1  793  ? -2.007  85.613  107.646 1.00 28.67 ? 791  GLN   A NE2   1 
ATOM   5788  N  N     . ALA   A  1  794  ? -4.356  89.536  111.466 1.00 24.75 ? 792  ALA   A N     1 
ATOM   5789  C  CA    . ALA   A  1  794  ? -3.522  90.612  111.979 1.00 29.94 ? 792  ALA   A CA    1 
ATOM   5790  C  C     . ALA   A  1  794  ? -3.676  90.752  113.488 1.00 26.77 ? 792  ALA   A C     1 
ATOM   5791  O  O     . ALA   A  1  794  ? -2.680  90.912  114.199 1.00 30.85 ? 792  ALA   A O     1 
ATOM   5792  C  CB    . ALA   A  1  794  ? -3.877  91.919  111.277 1.00 28.70 ? 792  ALA   A CB    1 
ATOM   5793  N  N     . GLN   A  1  795  ? -4.918  90.688  113.985 1.00 27.47 ? 793  GLN   A N     1 
ATOM   5794  C  CA    . GLN   A  1  795  ? -5.168  90.718  115.426 1.00 27.24 ? 793  GLN   A CA    1 
ATOM   5795  C  C     . GLN   A  1  795  ? -4.357  89.646  116.142 1.00 29.22 ? 793  GLN   A C     1 
ATOM   5796  O  O     . GLN   A  1  795  ? -3.698  89.915  117.153 1.00 32.06 ? 793  GLN   A O     1 
ATOM   5797  C  CB    . GLN   A  1  795  ? -6.656  90.468  115.688 1.00 30.89 ? 793  GLN   A CB    1 
ATOM   5798  C  CG    . GLN   A  1  795  ? -7.517  91.675  116.005 1.00 38.52 ? 793  GLN   A CG    1 
ATOM   5799  C  CD    . GLN   A  1  795  ? -8.967  91.279  116.303 1.00 37.43 ? 793  GLN   A CD    1 
ATOM   5800  O  OE1   . GLN   A  1  795  ? -9.605  90.573  115.517 1.00 39.91 ? 793  GLN   A OE1   1 
ATOM   5801  N  NE2   . GLN   A  1  795  ? -9.483  91.720  117.439 1.00 32.74 ? 793  GLN   A NE2   1 
ATOM   5802  N  N     . LEU   A  1  796  ? -4.397  88.414  115.627 1.00 27.56 ? 794  LEU   A N     1 
ATOM   5803  C  CA    . LEU   A  1  796  ? -3.749  87.291  116.289 1.00 27.73 ? 794  LEU   A CA    1 
ATOM   5804  C  C     . LEU   A  1  796  ? -2.237  87.296  116.132 1.00 27.88 ? 794  LEU   A C     1 
ATOM   5805  O  O     . LEU   A  1  796  ? -1.544  86.608  116.891 1.00 31.72 ? 794  LEU   A O     1 
ATOM   5806  C  CB    . LEU   A  1  796  ? -4.320  85.972  115.762 1.00 26.00 ? 794  LEU   A CB    1 
ATOM   5807  C  CG    . LEU   A  1  796  ? -5.790  85.690  116.066 1.00 25.44 ? 794  LEU   A CG    1 
ATOM   5808  C  CD1   . LEU   A  1  796  ? -6.239  84.377  115.441 1.00 27.74 ? 794  LEU   A CD1   1 
ATOM   5809  C  CD2   . LEU   A  1  796  ? -5.995  85.678  117.577 1.00 26.99 ? 794  LEU   A CD2   1 
ATOM   5810  N  N     . ALA   A  1  797  ? -1.704  88.034  115.162 1.00 29.59 ? 795  ALA   A N     1 
ATOM   5811  C  CA    . ALA   A  1  797  ? -0.258  88.077  115.003 1.00 30.27 ? 795  ALA   A CA    1 
ATOM   5812  C  C     . ALA   A  1  797  ? 0.421   88.716  116.209 1.00 34.69 ? 795  ALA   A C     1 
ATOM   5813  O  O     . ALA   A  1  797  ? 1.609   88.475  116.440 1.00 45.51 ? 795  ALA   A O     1 
ATOM   5814  C  CB    . ALA   A  1  797  ? 0.112   88.785  113.696 1.00 30.56 ? 795  ALA   A CB    1 
ATOM   5815  N  N     . ASP   A  1  798  ? -0.321  89.506  116.991 1.00 36.18 ? 796  ASP   A N     1 
ATOM   5816  C  CA    . ASP   A  1  798  ? 0.184   90.069  118.240 1.00 42.65 ? 796  ASP   A CA    1 
ATOM   5817  C  C     . ASP   A  1  798  ? 0.301   89.027  119.337 1.00 41.45 ? 796  ASP   A C     1 
ATOM   5818  O  O     . ASP   A  1  798  ? 1.028   89.249  120.311 1.00 40.69 ? 796  ASP   A O     1 
ATOM   5819  C  CB    . ASP   A  1  798  ? -0.809  91.106  118.767 1.00 36.72 ? 796  ASP   A CB    1 
ATOM   5820  C  CG    . ASP   A  1  798  ? -0.881  92.333  117.905 1.00 51.71 ? 796  ASP   A CG    1 
ATOM   5821  O  OD1   . ASP   A  1  798  ? 0.155   92.680  117.303 1.00 52.11 ? 796  ASP   A OD1   1 
ATOM   5822  O  OD2   . ASP   A  1  798  ? -1.967  92.949  117.831 1.00 52.14 ? 796  ASP   A OD2   1 
ATOM   5823  N  N     . ARG   A  1  799  ? -0.402  87.911  119.205 1.00 35.29 ? 797  ARG   A N     1 
ATOM   5824  C  CA    . ARG   A  1  799  ? -0.802  87.096  120.337 1.00 33.43 ? 797  ARG   A CA    1 
ATOM   5825  C  C     . ARG   A  1  799  ? -0.024  85.790  120.394 1.00 31.48 ? 797  ARG   A C     1 
ATOM   5826  O  O     . ARG   A  1  799  ? 0.322   85.202  119.368 1.00 29.76 ? 797  ARG   A O     1 
ATOM   5827  C  CB    . ARG   A  1  799  ? -2.292  86.783  120.225 1.00 38.23 ? 797  ARG   A CB    1 
ATOM   5828  C  CG    . ARG   A  1  799  ? -3.147  88.024  120.013 1.00 36.98 ? 797  ARG   A CG    1 
ATOM   5829  C  CD    . ARG   A  1  799  ? -3.435  88.664  121.333 1.00 41.60 ? 797  ARG   A CD    1 
ATOM   5830  N  NE    . ARG   A  1  799  ? -4.049  87.687  122.221 1.00 45.58 ? 797  ARG   A NE    1 
ATOM   5831  C  CZ    . ARG   A  1  799  ? -5.316  87.308  122.144 1.00 40.05 ? 797  ARG   A CZ    1 
ATOM   5832  N  NH1   . ARG   A  1  799  ? -6.139  87.833  121.252 1.00 43.59 ? 797  ARG   A NH1   1 
ATOM   5833  N  NH2   . ARG   A  1  799  ? -5.767  86.379  122.981 1.00 44.18 ? 797  ARG   A NH2   1 
ATOM   5834  N  N     . LEU   A  1  800  ? 0.239   85.339  121.617 1.00 29.07 ? 798  LEU   A N     1 
ATOM   5835  C  CA    . LEU   A  1  800  ? 0.772   84.011  121.860 1.00 30.61 ? 798  LEU   A CA    1 
ATOM   5836  C  C     . LEU   A  1  800  ? -0.022  83.365  122.983 1.00 27.95 ? 798  LEU   A C     1 
ATOM   5837  O  O     . LEU   A  1  800  ? -0.558  84.048  123.856 1.00 33.31 ? 798  LEU   A O     1 
ATOM   5838  C  CB    . LEU   A  1  800  ? 2.249   84.056  122.265 1.00 32.18 ? 798  LEU   A CB    1 
ATOM   5839  C  CG    . LEU   A  1  800  ? 3.250   84.459  121.184 1.00 31.83 ? 798  LEU   A CG    1 
ATOM   5840  C  CD1   . LEU   A  1  800  ? 4.639   84.641  121.793 1.00 30.93 ? 798  LEU   A CD1   1 
ATOM   5841  C  CD2   . LEU   A  1  800  ? 3.280   83.433  120.059 1.00 32.67 ? 798  LEU   A CD2   1 
ATOM   5842  N  N     . SER   A  1  801  ? -0.091  82.037  122.943 1.00 30.67 ? 799  SER   A N     1 
ATOM   5843  C  CA    . SER   A  1  801  ? -0.699  81.279  124.018 1.00 34.44 ? 799  SER   A CA    1 
ATOM   5844  C  C     . SER   A  1  801  ? 0.185   81.375  125.259 1.00 35.62 ? 799  SER   A C     1 
ATOM   5845  O  O     . SER   A  1  801  ? 1.340   81.807  125.178 1.00 34.95 ? 799  SER   A O     1 
ATOM   5846  C  CB    . SER   A  1  801  ? -0.835  79.819  123.594 1.00 34.03 ? 799  SER   A CB    1 
ATOM   5847  O  OG    . SER   A  1  801  ? 0.438   79.198  123.558 1.00 35.45 ? 799  SER   A OG    1 
ATOM   5848  N  N     . PRO   A  1  802  ? -0.331  80.985  126.430 1.00 34.55 ? 800  PRO   A N     1 
ATOM   5849  C  CA    . PRO   A  1  802  ? 0.533   80.926  127.624 1.00 39.79 ? 800  PRO   A CA    1 
ATOM   5850  C  C     . PRO   A  1  802  ? 1.787   80.096  127.428 1.00 40.09 ? 800  PRO   A C     1 
ATOM   5851  O  O     . PRO   A  1  802  ? 2.807   80.362  128.075 1.00 43.28 ? 800  PRO   A O     1 
ATOM   5852  C  CB    . PRO   A  1  802  ? -0.391  80.322  128.687 1.00 38.25 ? 800  PRO   A CB    1 
ATOM   5853  C  CG    . PRO   A  1  802  ? -1.759  80.746  128.268 1.00 39.69 ? 800  PRO   A CG    1 
ATOM   5854  C  CD    . PRO   A  1  802  ? -1.748  80.739  126.761 1.00 34.78 ? 800  PRO   A CD    1 
ATOM   5855  N  N     . ALA   A  1  803  ? 1.747   79.098  126.551 1.00 38.67 ? 801  ALA   A N     1 
ATOM   5856  C  CA    . ALA   A  1  803  ? 2.929   78.328  126.196 1.00 41.20 ? 801  ALA   A CA    1 
ATOM   5857  C  C     . ALA   A  1  803  ? 3.817   79.042  125.183 1.00 41.43 ? 801  ALA   A C     1 
ATOM   5858  O  O     . ALA   A  1  803  ? 4.782   78.442  124.700 1.00 39.92 ? 801  ALA   A O     1 
ATOM   5859  C  CB    . ALA   A  1  803  ? 2.520   76.956  125.650 1.00 43.58 ? 801  ALA   A CB    1 
ATOM   5860  N  N     . GLY   A  1  804  ? 3.508   80.290  124.844 1.00 38.57 ? 802  GLY   A N     1 
ATOM   5861  C  CA    . GLY   A  1  804  ? 4.270   81.026  123.845 1.00 35.58 ? 802  GLY   A CA    1 
ATOM   5862  C  C     . GLY   A  1  804  ? 4.178   80.511  122.422 1.00 34.60 ? 802  GLY   A C     1 
ATOM   5863  O  O     . GLY   A  1  804  ? 5.184   80.519  121.704 1.00 33.58 ? 802  GLY   A O     1 
ATOM   5864  N  N     . ARG   A  1  805  ? 2.998   80.092  121.979 1.00 32.66 ? 803  ARG   A N     1 
ATOM   5865  C  CA    . ARG   A  1  805  ? 2.806   79.576  120.633 1.00 32.25 ? 803  ARG   A CA    1 
ATOM   5866  C  C     . ARG   A  1  805  ? 1.628   80.277  119.971 1.00 26.50 ? 803  ARG   A C     1 
ATOM   5867  O  O     . ARG   A  1  805  ? 0.763   80.831  120.656 1.00 28.23 ? 803  ARG   A O     1 
ATOM   5868  C  CB    . ARG   A  1  805  ? 2.577   78.057  120.655 1.00 34.71 ? 803  ARG   A CB    1 
ATOM   5869  C  CG    . ARG   A  1  805  ? 3.760   77.274  121.217 1.00 32.32 ? 803  ARG   A CG    1 
ATOM   5870  C  CD    . ARG   A  1  805  ? 5.045   77.565  120.438 1.00 36.50 ? 803  ARG   A CD    1 
ATOM   5871  N  NE    . ARG   A  1  805  ? 6.197   76.867  121.001 1.00 33.10 ? 803  ARG   A NE    1 
ATOM   5872  C  CZ    . ARG   A  1  805  ? 7.050   77.390  121.873 1.00 37.98 ? 803  ARG   A CZ    1 
ATOM   5873  N  NH1   . ARG   A  1  805  ? 6.926   78.635  122.306 1.00 38.57 ? 803  ARG   A NH1   1 
ATOM   5874  N  NH2   . ARG   A  1  805  ? 8.053   76.642  122.326 1.00 42.98 ? 803  ARG   A NH2   1 
ATOM   5875  N  N     . PRO   A  1  806  ? 1.584   80.301  118.634 1.00 28.31 ? 804  PRO   A N     1 
ATOM   5876  C  CA    . PRO   A  1  806  ? 0.519   81.047  117.951 1.00 27.02 ? 804  PRO   A CA    1 
ATOM   5877  C  C     . PRO   A  1  806  ? -0.856  80.496  118.291 1.00 25.98 ? 804  PRO   A C     1 
ATOM   5878  O  O     . PRO   A  1  806  ? -1.034  79.292  118.485 1.00 26.63 ? 804  PRO   A O     1 
ATOM   5879  C  CB    . PRO   A  1  806  ? 0.838   80.839  116.466 1.00 29.10 ? 804  PRO   A CB    1 
ATOM   5880  C  CG    . PRO   A  1  806  ? 2.297   80.580  116.434 1.00 30.57 ? 804  PRO   A CG    1 
ATOM   5881  C  CD    . PRO   A  1  806  ? 2.585   79.793  117.680 1.00 29.45 ? 804  PRO   A CD    1 
ATOM   5882  N  N     . ILE   A  1  807  ? -1.829  81.399  118.355 1.00 24.18 ? 805  ILE   A N     1 
ATOM   5883  C  CA    . ILE   A  1  807  ? -3.224  81.033  118.587 1.00 23.12 ? 805  ILE   A CA    1 
ATOM   5884  C  C     . ILE   A  1  807  ? -3.766  80.422  117.301 1.00 21.33 ? 805  ILE   A C     1 
ATOM   5885  O  O     . ILE   A  1  807  ? -3.776  81.097  116.262 1.00 25.68 ? 805  ILE   A O     1 
ATOM   5886  C  CB    . ILE   A  1  807  ? -4.047  82.263  118.985 1.00 25.71 ? 805  ILE   A CB    1 
ATOM   5887  C  CG1   . ILE   A  1  807  ? -3.492  82.878  120.272 1.00 30.25 ? 805  ILE   A CG1   1 
ATOM   5888  C  CG2   . ILE   A  1  807  ? -5.525  81.906  119.107 1.00 26.19 ? 805  ILE   A CG2   1 
ATOM   5889  C  CD1   . ILE   A  1  807  ? -3.556  81.969  121.473 1.00 30.25 ? 805  ILE   A CD1   1 
ATOM   5890  N  N     . PRO   A  1  808  ? -4.202  79.160  117.309 1.00 22.28 ? 806  PRO   A N     1 
ATOM   5891  C  CA    . PRO   A  1  808  ? -4.694  78.547  116.069 1.00 21.75 ? 806  PRO   A CA    1 
ATOM   5892  C  C     . PRO   A  1  808  ? -5.876  79.304  115.482 1.00 21.28 ? 806  PRO   A C     1 
ATOM   5893  O  O     . PRO   A  1  808  ? -6.798  79.713  116.191 1.00 21.63 ? 806  PRO   A O     1 
ATOM   5894  C  CB    . PRO   A  1  808  ? -5.108  77.138  116.508 1.00 23.35 ? 806  PRO   A CB    1 
ATOM   5895  C  CG    . PRO   A  1  808  ? -4.304  76.876  117.726 1.00 23.54 ? 806  PRO   A CG    1 
ATOM   5896  C  CD    . PRO   A  1  808  ? -4.220  78.208  118.426 1.00 22.33 ? 806  PRO   A CD    1 
ATOM   5897  N  N     . LEU   A  1  809  ? -5.839  79.468  114.164 1.00 21.16 ? 807  LEU   A N     1 
ATOM   5898  C  CA    . LEU   A  1  809  ? -6.902  80.117  113.409 1.00 21.39 ? 807  LEU   A CA    1 
ATOM   5899  C  C     . LEU   A  1  809  ? -7.287  79.201  112.261 1.00 19.64 ? 807  LEU   A C     1 
ATOM   5900  O  O     . LEU   A  1  809  ? -6.443  78.855  111.429 1.00 21.55 ? 807  LEU   A O     1 
ATOM   5901  C  CB    . LEU   A  1  809  ? -6.413  81.452  112.845 1.00 23.50 ? 807  LEU   A CB    1 
ATOM   5902  C  CG    . LEU   A  1  809  ? -7.381  82.119  111.868 1.00 22.41 ? 807  LEU   A CG    1 
ATOM   5903  C  CD1   . LEU   A  1  809  ? -8.682  82.463  112.581 1.00 22.69 ? 807  LEU   A CD1   1 
ATOM   5904  C  CD2   . LEU   A  1  809  ? -6.754  83.349  111.242 1.00 24.24 ? 807  LEU   A CD2   1 
ATOM   5905  N  N     . ILE   A  1  810  ? -8.549  78.793  112.222 1.00 18.55 ? 808  ILE   A N     1 
ATOM   5906  C  CA    . ILE   A  1  810  ? -9.134  78.206  111.028 1.00 19.86 ? 808  ILE   A CA    1 
ATOM   5907  C  C     . ILE   A  1  810  ? -9.894  79.333  110.371 1.00 20.38 ? 808  ILE   A C     1 
ATOM   5908  O  O     . ILE   A  1  810  ? -10.780 79.924  110.991 1.00 21.39 ? 808  ILE   A O     1 
ATOM   5909  C  CB    . ILE   A  1  810  ? -10.077 77.045  111.370 1.00 19.16 ? 808  ILE   A CB    1 
ATOM   5910  C  CG1   . ILE   A  1  810  ? -9.359  75.984  112.202 1.00 20.84 ? 808  ILE   A CG1   1 
ATOM   5911  C  CG2   . ILE   A  1  810  ? -10.614 76.432  110.082 1.00 21.36 ? 808  ILE   A CG2   1 
ATOM   5912  C  CD1   . ILE   A  1  810  ? -10.216 74.760  112.492 1.00 23.89 ? 808  ILE   A CD1   1 
ATOM   5913  N  N     . ALA   A  1  811  ? -9.530  79.666  109.141 1.00 19.77 ? 809  ALA   A N     1 
ATOM   5914  C  CA    . ALA   A  1  811  ? -10.140 80.790  108.439 1.00 20.36 ? 809  ALA   A CA    1 
ATOM   5915  C  C     . ALA   A  1  811  ? -10.559 80.265  107.080 1.00 18.94 ? 809  ALA   A C     1 
ATOM   5916  O  O     . ALA   A  1  811  ? -9.720  80.049  106.203 1.00 19.21 ? 809  ALA   A O     1 
ATOM   5917  C  CB    . ALA   A  1  811  ? -9.172  81.956  108.316 1.00 22.14 ? 809  ALA   A CB    1 
ATOM   5918  N  N     . GLU   A  1  812  ? -11.851 80.030  106.932 1.00 17.51 ? 810  GLU   A N     1 
ATOM   5919  C  CA    . GLU   A  1  812  ? -12.418 79.475  105.714 1.00 18.97 ? 810  GLU   A CA    1 
ATOM   5920  C  C     . GLU   A  1  812  ? -13.129 80.607  104.997 1.00 17.92 ? 810  GLU   A C     1 
ATOM   5921  O  O     . GLU   A  1  812  ? -14.083 81.181  105.534 1.00 19.10 ? 810  GLU   A O     1 
ATOM   5922  C  CB    . GLU   A  1  812  ? -13.343 78.315  106.068 1.00 21.04 ? 810  GLU   A CB    1 
ATOM   5923  C  CG    . GLU   A  1  812  ? -12.585 77.203  106.799 1.00 20.36 ? 810  GLU   A CG    1 
ATOM   5924  C  CD    . GLU   A  1  812  ? -11.436 76.645  105.969 1.00 22.63 ? 810  GLU   A CD    1 
ATOM   5925  O  OE1   . GLU   A  1  812  ? -11.706 75.823  105.073 1.00 21.91 ? 810  GLU   A OE1   1 
ATOM   5926  O  OE2   . GLU   A  1  812  ? -10.261 77.025  106.203 1.00 22.55 ? 810  GLU   A OE2   1 
ATOM   5927  N  N     . THR   A  1  813  ? -12.628 80.957  103.814 1.00 18.37 ? 811  THR   A N     1 
ATOM   5928  C  CA    . THR   A  1  813  ? -12.938 82.252  103.228 1.00 19.24 ? 811  THR   A CA    1 
ATOM   5929  C  C     . THR   A  1  813  ? -13.548 82.166  101.832 1.00 18.83 ? 811  THR   A C     1 
ATOM   5930  O  O     . THR   A  1  813  ? -14.176 81.160  101.490 1.00 20.33 ? 811  THR   A O     1 
ATOM   5931  C  CB    . THR   A  1  813  ? -11.713 83.174  103.309 1.00 20.31 ? 811  THR   A CB    1 
ATOM   5932  O  OG1   . THR   A  1  813  ? -10.536 82.502  102.831 1.00 20.19 ? 811  THR   A OG1   1 
ATOM   5933  C  CG2   . THR   A  1  813  ? -11.481 83.570  104.760 1.00 21.60 ? 811  THR   A CG2   1 
ATOM   5934  N  N     . GLY   A  1  814  ? -13.400 83.221  101.035 1.00 19.47 ? 812  GLY   A N     1 
ATOM   5935  C  CA    . GLY   A  1  814  ? -14.172 83.355  99.818  1.00 19.92 ? 812  GLY   A CA    1 
ATOM   5936  C  C     . GLY   A  1  814  ? -13.677 82.484  98.683  1.00 20.92 ? 812  GLY   A C     1 
ATOM   5937  O  O     . GLY   A  1  814  ? -12.670 81.787  98.771  1.00 21.78 ? 812  GLY   A O     1 
ATOM   5938  N  N     . GLY   A  1  815  ? -14.411 82.546  97.576  1.00 19.39 ? 813  GLY   A N     1 
ATOM   5939  C  CA    . GLY   A  1  815  ? -14.048 81.798  96.394  1.00 19.37 ? 813  GLY   A CA    1 
ATOM   5940  C  C     . GLY   A  1  815  ? -14.243 82.654  95.160  1.00 19.60 ? 813  GLY   A C     1 
ATOM   5941  O  O     . GLY   A  1  815  ? -14.916 83.684  95.191  1.00 22.23 ? 813  GLY   A O     1 
ATOM   5942  N  N     . GLN   A  1  816  ? -13.603 82.225  94.079  1.00 18.59 ? 814  GLN   A N     1 
ATOM   5943  C  CA    . GLN   A  1  816  ? -13.826 82.779  92.746  1.00 19.77 ? 814  GLN   A CA    1 
ATOM   5944  C  C     . GLN   A  1  816  ? -14.000 81.581  91.827  1.00 18.67 ? 814  GLN   A C     1 
ATOM   5945  O  O     . GLN   A  1  816  ? -13.154 81.280  90.985  1.00 19.50 ? 814  GLN   A O     1 
ATOM   5946  C  CB    . GLN   A  1  816  ? -12.662 83.657  92.307  1.00 20.17 ? 814  GLN   A CB    1 
ATOM   5947  C  CG    . GLN   A  1  816  ? -12.959 84.457  91.054  1.00 22.68 ? 814  GLN   A CG    1 
ATOM   5948  C  CD    . GLN   A  1  816  ? -14.040 85.496  91.290  1.00 25.15 ? 814  GLN   A CD    1 
ATOM   5949  O  OE1   . GLN   A  1  816  ? -15.231 85.192  91.259  1.00 23.78 ? 814  GLN   A OE1   1 
ATOM   5950  N  NE2   . GLN   A  1  816  ? -13.624 86.733  91.540  1.00 26.82 ? 814  GLN   A NE2   1 
ATOM   5951  N  N     . ASN   A  1  817  ? -15.096 80.870  92.031  1.00 16.45 ? 815  ASN   A N     1 
ATOM   5952  C  CA    . ASN   A  1  817  ? -15.182 79.485  91.609  1.00 16.04 ? 815  ASN   A CA    1 
ATOM   5953  C  C     . ASN   A  1  817  ? -15.543 79.386  90.137  1.00 16.87 ? 815  ASN   A C     1 
ATOM   5954  O  O     . ASN   A  1  817  ? -16.482 80.042  89.660  1.00 16.96 ? 815  ASN   A O     1 
ATOM   5955  C  CB    . ASN   A  1  817  ? -16.219 78.771  92.464  1.00 16.82 ? 815  ASN   A CB    1 
ATOM   5956  C  CG    . ASN   A  1  817  ? -15.993 79.017  93.931  1.00 15.40 ? 815  ASN   A CG    1 
ATOM   5957  O  OD1   . ASN   A  1  817  ? -14.894 78.780  94.439  1.00 16.04 ? 815  ASN   A OD1   1 
ATOM   5958  N  ND2   . ASN   A  1  817  ? -17.009 79.523  94.618  1.00 16.67 ? 815  ASN   A ND2   1 
ATOM   5959  N  N     . ALA   A  1  818  ? -14.816 78.531  89.432  1.00 15.94 ? 816  ALA   A N     1 
ATOM   5960  C  CA    . ALA   A  1  818  ? -14.984 78.353  88.004  1.00 15.34 ? 816  ALA   A CA    1 
ATOM   5961  C  C     . ALA   A  1  818  ? -15.565 76.984  87.701  1.00 15.02 ? 816  ALA   A C     1 
ATOM   5962  O  O     . ALA   A  1  818  ? -15.414 76.029  88.470  1.00 15.41 ? 816  ALA   A O     1 
ATOM   5963  C  CB    . ALA   A  1  818  ? -13.629 78.452  87.305  1.00 16.07 ? 816  ALA   A CB    1 
ATOM   5964  N  N     . MET   A  1  819  ? -16.240 76.904  86.555  1.00 15.33 ? 817  MET   A N     1 
ATOM   5965  C  CA    . MET   A  1  819  ? -16.587 75.635  85.951  1.00 14.76 ? 817  MET   A CA    1 
ATOM   5966  C  C     . MET   A  1  819  ? -16.109 75.669  84.511  1.00 16.53 ? 817  MET   A C     1 
ATOM   5967  O  O     . MET   A  1  819  ? -16.357 76.644  83.798  1.00 16.73 ? 817  MET   A O     1 
ATOM   5968  C  CB    . MET   A  1  819  ? -18.090 75.424  85.978  1.00 16.70 ? 817  MET   A CB    1 
ATOM   5969  C  CG    . MET   A  1  819  ? -18.502 74.142  85.294  1.00 16.63 ? 817  MET   A CG    1 
ATOM   5970  S  SD    . MET   A  1  819  ? -20.288 74.021  85.147  1.00 18.47 ? 817  MET   A SD    1 
ATOM   5971  C  CE    . MET   A  1  819  ? -20.718 73.735  86.854  1.00 21.30 ? 817  MET   A CE    1 
ATOM   5972  N  N     . ILE   A  1  820  ? -15.399 74.630  84.093  1.00 15.38 ? 818  ILE   A N     1 
ATOM   5973  C  CA    . ILE   A  1  820  ? -14.938 74.518  82.719  1.00 16.51 ? 818  ILE   A CA    1 
ATOM   5974  C  C     . ILE   A  1  820  ? -15.815 73.497  82.021  1.00 15.83 ? 818  ILE   A C     1 
ATOM   5975  O  O     . ILE   A  1  820  ? -16.072 72.411  82.556  1.00 16.25 ? 818  ILE   A O     1 
ATOM   5976  C  CB    . ILE   A  1  820  ? -13.457 74.117  82.665  1.00 16.46 ? 818  ILE   A CB    1 
ATOM   5977  C  CG1   . ILE   A  1  820  ? -12.590 75.209  83.291  1.00 16.84 ? 818  ILE   A CG1   1 
ATOM   5978  C  CG2   . ILE   A  1  820  ? -13.043 73.820  81.215  1.00 18.60 ? 818  ILE   A CG2   1 
ATOM   5979  C  CD1   . ILE   A  1  820  ? -11.114 74.878  83.294  1.00 16.56 ? 818  ILE   A CD1   1 
ATOM   5980  N  N     . VAL   A  1  821  ? -16.293 73.855  80.836  1.00 16.56 ? 819  VAL   A N     1 
ATOM   5981  C  CA    . VAL   A  1  821  ? -17.203 73.019  80.070  1.00 16.74 ? 819  VAL   A CA    1 
ATOM   5982  C  C     . VAL   A  1  821  ? -16.596 72.862  78.691  1.00 17.63 ? 819  VAL   A C     1 
ATOM   5983  O  O     . VAL   A  1  821  ? -16.293 73.861  78.033  1.00 19.58 ? 819  VAL   A O     1 
ATOM   5984  C  CB    . VAL   A  1  821  ? -18.584 73.684  79.945  1.00 16.94 ? 819  VAL   A CB    1 
ATOM   5985  C  CG1   . VAL   A  1  821  ? -19.496 72.853  79.065  1.00 18.55 ? 819  VAL   A CG1   1 
ATOM   5986  C  CG2   . VAL   A  1  821  ? -19.204 73.899  81.325  1.00 17.16 ? 819  VAL   A CG2   1 
ATOM   5987  N  N     . ASP   A  1  822  ? -16.413 71.626  78.258  1.00 16.29 ? 820  ASP   A N     1 
ATOM   5988  C  CA    . ASP   A  1  822  ? -15.894 71.410  76.921  1.00 17.86 ? 820  ASP   A CA    1 
ATOM   5989  C  C     . ASP   A  1  822  ? -17.016 70.972  75.990  1.00 18.76 ? 820  ASP   A C     1 
ATOM   5990  O  O     . ASP   A  1  822  ? -18.178 70.858  76.381  1.00 18.80 ? 820  ASP   A O     1 
ATOM   5991  C  CB    . ASP   A  1  822  ? -14.665 70.496  76.929  1.00 19.25 ? 820  ASP   A CB    1 
ATOM   5992  C  CG    . ASP   A  1  822  ? -14.993 69.021  77.143  1.00 18.11 ? 820  ASP   A CG    1 
ATOM   5993  O  OD1   . ASP   A  1  822  ? -16.173 68.597  77.104  1.00 19.58 ? 820  ASP   A OD1   1 
ATOM   5994  O  OD2   . ASP   A  1  822  ? -14.016 68.269  77.370  1.00 20.53 ? 820  ASP   A OD2   1 
ATOM   5995  N  N     . SER   A  1  823  ? -16.656 70.721  74.732  1.00 19.29 ? 821  SER   A N     1 
ATOM   5996  C  CA    . SER   A  1  823  ? -17.657 70.416  73.718  1.00 20.32 ? 821  SER   A CA    1 
ATOM   5997  C  C     . SER   A  1  823  ? -18.225 69.012  73.833  1.00 22.42 ? 821  SER   A C     1 
ATOM   5998  O  O     . SER   A  1  823  ? -19.128 68.664  73.063  1.00 24.86 ? 821  SER   A O     1 
ATOM   5999  C  CB    . SER   A  1  823  ? -17.059 70.627  72.327  1.00 22.36 ? 821  SER   A CB    1 
ATOM   6000  O  OG    . SER   A  1  823  ? -15.887 69.850  72.175  1.00 26.50 ? 821  SER   A OG    1 
ATOM   6001  N  N     . SER   A  1  824  ? -17.738 68.202  74.771  1.00 18.17 ? 822  SER   A N     1 
ATOM   6002  C  CA    . SER   A  1  824  ? -18.287 66.878  74.990  1.00 18.27 ? 822  SER   A CA    1 
ATOM   6003  C  C     . SER   A  1  824  ? -19.408 66.875  76.017  1.00 20.05 ? 822  SER   A C     1 
ATOM   6004  O  O     . SER   A  1  824  ? -20.122 65.875  76.133  1.00 21.58 ? 822  SER   A O     1 
ATOM   6005  C  CB    . SER   A  1  824  ? -17.186 65.910  75.431  1.00 19.48 ? 822  SER   A CB    1 
ATOM   6006  O  OG    . SER   A  1  824  ? -16.797 66.136  76.781  1.00 19.28 ? 822  SER   A OG    1 
ATOM   6007  N  N     . ALA   A  1  825  ? -19.577 67.967  76.756  1.00 19.19 ? 823  ALA   A N     1 
ATOM   6008  C  CA    . ALA   A  1  825  ? -20.577 68.015  77.806  1.00 20.19 ? 823  ALA   A CA    1 
ATOM   6009  C  C     . ALA   A  1  825  ? -21.967 68.132  77.200  1.00 20.06 ? 823  ALA   A C     1 
ATOM   6010  O  O     . ALA   A  1  825  ? -22.140 68.632  76.086  1.00 21.42 ? 823  ALA   A O     1 
ATOM   6011  C  CB    . ALA   A  1  825  ? -20.305 69.218  78.704  1.00 19.93 ? 823  ALA   A CB    1 
ATOM   6012  N  N     . LEU   A  1  826  ? -22.961 67.645  77.931  1.00 21.06 ? 824  LEU   A N     1 
ATOM   6013  C  CA    . LEU   A  1  826  ? -24.350 67.731  77.501  1.00 21.18 ? 824  LEU   A CA    1 
ATOM   6014  C  C     . LEU   A  1  826  ? -24.913 69.080  77.940  1.00 21.57 ? 824  LEU   A C     1 
ATOM   6015  O  O     . LEU   A  1  826  ? -24.972 69.371  79.139  1.00 21.39 ? 824  LEU   A O     1 
ATOM   6016  C  CB    . LEU   A  1  826  ? -25.158 66.580  78.094  1.00 25.11 ? 824  LEU   A CB    1 
ATOM   6017  N  N     . ALA   A  1  827  ? -25.325 69.899  76.968  1.00 21.86 ? 825  ALA   A N     1 
ATOM   6018  C  CA    . ALA   A  1  827  ? -25.667 71.286  77.269  1.00 20.18 ? 825  ALA   A CA    1 
ATOM   6019  C  C     . ALA   A  1  827  ? -26.771 71.386  78.314  1.00 20.65 ? 825  ALA   A C     1 
ATOM   6020  O  O     . ALA   A  1  827  ? -26.688 72.217  79.223  1.00 19.79 ? 825  ALA   A O     1 
ATOM   6021  C  CB    . ALA   A  1  827  ? -26.061 72.024  75.991  1.00 22.55 ? 825  ALA   A CB    1 
ATOM   6022  N  N     . GLU   A  1  828  ? -27.806 70.550  78.210  1.00 21.11 ? 826  GLU   A N     1 
ATOM   6023  C  CA    . GLU   A  1  828  ? -28.913 70.636  79.158  1.00 20.80 ? 826  GLU   A CA    1 
ATOM   6024  C  C     . GLU   A  1  828  ? -28.440 70.352  80.576  1.00 21.91 ? 826  GLU   A C     1 
ATOM   6025  O  O     . GLU   A  1  828  ? -28.922 70.964  81.539  1.00 21.09 ? 826  GLU   A O     1 
ATOM   6026  C  CB    . GLU   A  1  828  ? -30.017 69.650  78.776  1.00 26.42 ? 826  GLU   A CB    1 
ATOM   6027  C  CG    . GLU   A  1  828  ? -30.863 70.083  77.591  1.00 29.05 ? 826  GLU   A CG    1 
ATOM   6028  C  CD    . GLU   A  1  828  ? -30.207 69.815  76.244  1.00 35.63 ? 826  GLU   A CD    1 
ATOM   6029  O  OE1   . GLU   A  1  828  ? -29.086 69.256  76.201  1.00 32.45 ? 826  GLU   A OE1   1 
ATOM   6030  O  OE2   . GLU   A  1  828  ? -30.829 70.167  75.217  1.00 41.92 ? 826  GLU   A OE2   1 
ATOM   6031  N  N     . GLN   A  1  829  ? -27.518 69.399  80.721  1.00 21.05 ? 827  GLN   A N     1 
ATOM   6032  C  CA    . GLN   A  1  829  ? -26.954 69.068  82.024  1.00 23.38 ? 827  GLN   A CA    1 
ATOM   6033  C  C     . GLN   A  1  829  ? -26.128 70.229  82.551  1.00 18.66 ? 827  GLN   A C     1 
ATOM   6034  O  O     . GLN   A  1  829  ? -26.245 70.622  83.720  1.00 19.58 ? 827  GLN   A O     1 
ATOM   6035  C  CB    . GLN   A  1  829  ? -26.047 67.859  81.842  1.00 27.17 ? 827  GLN   A CB    1 
ATOM   6036  C  CG    . GLN   A  1  829  ? -26.088 66.830  82.919  1.00 33.78 ? 827  GLN   A CG    1 
ATOM   6037  C  CD    . GLN   A  1  829  ? -25.366 65.576  82.472  1.00 34.60 ? 827  GLN   A CD    1 
ATOM   6038  O  OE1   . GLN   A  1  829  ? -24.275 65.652  81.904  1.00 31.21 ? 827  GLN   A OE1   1 
ATOM   6039  N  NE2   . GLN   A  1  829  ? -25.985 64.420  82.689  1.00 38.70 ? 827  GLN   A NE2   1 
ATOM   6040  N  N     . VAL   A  1  830  ? -25.274 70.783  81.694  1.00 18.39 ? 828  VAL   A N     1 
ATOM   6041  C  CA    . VAL   A  1  830  ? -24.468 71.938  82.065  1.00 17.89 ? 828  VAL   A CA    1 
ATOM   6042  C  C     . VAL   A  1  830  ? -25.355 73.074  82.546  1.00 16.86 ? 828  VAL   A C     1 
ATOM   6043  O  O     . VAL   A  1  830  ? -25.114 73.670  83.600  1.00 17.45 ? 828  VAL   A O     1 
ATOM   6044  C  CB    . VAL   A  1  830  ? -23.603 72.386  80.875  1.00 18.62 ? 828  VAL   A CB    1 
ATOM   6045  C  CG1   . VAL   A  1  830  ? -22.954 73.721  81.164  1.00 19.53 ? 828  VAL   A CG1   1 
ATOM   6046  C  CG2   . VAL   A  1  830  ? -22.549 71.331  80.551  1.00 20.72 ? 828  VAL   A CG2   1 
ATOM   6047  N  N     . VAL   A  1  831  ? -26.390 73.400  81.767  1.00 16.99 ? 829  VAL   A N     1 
ATOM   6048  C  CA    . VAL   A  1  831  ? -27.189 74.573  82.093  1.00 17.58 ? 829  VAL   A CA    1 
ATOM   6049  C  C     . VAL   A  1  831  ? -27.880 74.396  83.435  1.00 16.41 ? 829  VAL   A C     1 
ATOM   6050  O  O     . VAL   A  1  831  ? -27.908 75.323  84.252  1.00 16.89 ? 829  VAL   A O     1 
ATOM   6051  C  CB    . VAL   A  1  831  ? -28.166 74.905  80.956  1.00 17.79 ? 829  VAL   A CB    1 
ATOM   6052  C  CG1   . VAL   A  1  831  ? -29.145 75.973  81.398  1.00 17.87 ? 829  VAL   A CG1   1 
ATOM   6053  C  CG2   . VAL   A  1  831  ? -27.383 75.390  79.755  1.00 19.71 ? 829  VAL   A CG2   1 
ATOM   6054  N  N     . GLY   A  1  832  ? -28.427 73.204  83.694  1.00 17.25 ? 830  GLY   A N     1 
ATOM   6055  C  CA    . GLY   A  1  832  ? -29.032 72.958  84.993  1.00 16.26 ? 830  GLY   A CA    1 
ATOM   6056  C  C     . GLY   A  1  832  ? -28.038 73.129  86.126  1.00 15.89 ? 830  GLY   A C     1 
ATOM   6057  O  O     . GLY   A  1  832  ? -28.328 73.786  87.130  1.00 17.67 ? 830  GLY   A O     1 
ATOM   6058  N  N     . ASP   A  1  833  ? -26.836 72.579  85.962  1.00 16.68 ? 831  ASP   A N     1 
ATOM   6059  C  CA    . ASP   A  1  833  ? -25.843 72.689  87.024  1.00 16.22 ? 831  ASP   A CA    1 
ATOM   6060  C  C     . ASP   A  1  833  ? -25.327 74.111  87.164  1.00 15.82 ? 831  ASP   A C     1 
ATOM   6061  O  O     . ASP   A  1  833  ? -24.959 74.530  88.266  1.00 17.34 ? 831  ASP   A O     1 
ATOM   6062  C  CB    . ASP   A  1  833  ? -24.687 71.735  86.746  1.00 16.99 ? 831  ASP   A CB    1 
ATOM   6063  C  CG    . ASP   A  1  833  ? -25.086 70.304  86.910  1.00 17.75 ? 831  ASP   A CG    1 
ATOM   6064  O  OD1   . ASP   A  1  833  ? -26.161 70.059  87.497  1.00 20.06 ? 831  ASP   A OD1   1 
ATOM   6065  O  OD2   . ASP   A  1  833  ? -24.346 69.422  86.428  1.00 18.69 ? 831  ASP   A OD2   1 
ATOM   6066  N  N     . VAL   A  1  834  ? -25.283 74.863  86.064  1.00 16.05 ? 832  VAL   A N     1 
ATOM   6067  C  CA    . VAL   A  1  834  ? -24.837 76.250  86.121  1.00 16.79 ? 832  VAL   A CA    1 
ATOM   6068  C  C     . VAL   A  1  834  ? -25.881 77.125  86.797  1.00 16.15 ? 832  VAL   A C     1 
ATOM   6069  O  O     . VAL   A  1  834  ? -25.564 77.945  87.664  1.00 16.56 ? 832  VAL   A O     1 
ATOM   6070  C  CB    . VAL   A  1  834  ? -24.520 76.765  84.710  1.00 16.73 ? 832  VAL   A CB    1 
ATOM   6071  C  CG1   . VAL   A  1  834  ? -24.361 78.265  84.723  1.00 18.57 ? 832  VAL   A CG1   1 
ATOM   6072  C  CG2   . VAL   A  1  834  ? -23.257 76.093  84.188  1.00 18.45 ? 832  VAL   A CG2   1 
ATOM   6073  N  N     . ILE   A  1  835  ? -27.146 76.980  86.389  1.00 16.88 ? 833  ILE   A N     1 
ATOM   6074  C  CA    . ILE   A  1  835  ? -28.211 77.770  86.991  1.00 18.48 ? 833  ILE   A CA    1 
ATOM   6075  C  C     . ILE   A  1  835  ? -28.266 77.521  88.490  1.00 17.73 ? 833  ILE   A C     1 
ATOM   6076  O  O     . ILE   A  1  835  ? -28.370 78.458  89.291  1.00 19.64 ? 833  ILE   A O     1 
ATOM   6077  C  CB    . ILE   A  1  835  ? -29.551 77.455  86.303  1.00 18.12 ? 833  ILE   A CB    1 
ATOM   6078  C  CG1   . ILE   A  1  835  ? -29.577 78.007  84.872  1.00 19.91 ? 833  ILE   A CG1   1 
ATOM   6079  C  CG2   . ILE   A  1  835  ? -30.714 77.991  87.137  1.00 22.40 ? 833  ILE   A CG2   1 
ATOM   6080  C  CD1   . ILE   A  1  835  ? -29.681 79.515  84.804  1.00 22.81 ? 833  ILE   A CD1   1 
ATOM   6081  N  N     . THR   A  1  836  ? -28.162 76.259  88.895  1.00 17.74 ? 834  THR   A N     1 
ATOM   6082  C  CA    . THR   A  1  836  ? -28.163 75.940  90.316  1.00 17.33 ? 834  THR   A CA    1 
ATOM   6083  C  C     . THR   A  1  836  ? -26.923 76.505  90.999  1.00 18.77 ? 834  THR   A C     1 
ATOM   6084  O  O     . THR   A  1  836  ? -27.024 77.210  92.006  1.00 19.44 ? 834  THR   A O     1 
ATOM   6085  C  CB    . THR   A  1  836  ? -28.258 74.424  90.496  1.00 21.02 ? 834  THR   A CB    1 
ATOM   6086  O  OG1   . THR   A  1  836  ? -29.517 73.968  89.996  1.00 27.62 ? 834  THR   A OG1   1 
ATOM   6087  C  CG2   . THR   A  1  836  ? -28.151 74.042  91.952  1.00 25.82 ? 834  THR   A CG2   1 
ATOM   6088  N  N     . SER   A  1  837  ? -25.744 76.249  90.437  1.00 17.09 ? 835  SER   A N     1 
ATOM   6089  C  CA    . SER   A  1  837  ? -24.512 76.641  91.116  1.00 16.79 ? 835  SER   A CA    1 
ATOM   6090  C  C     . SER   A  1  837  ? -24.373 78.150  91.211  1.00 15.36 ? 835  SER   A C     1 
ATOM   6091  O  O     . SER   A  1  837  ? -23.835 78.666  92.191  1.00 17.95 ? 835  SER   A O     1 
ATOM   6092  C  CB    . SER   A  1  837  ? -23.288 76.065  90.405  1.00 16.55 ? 835  SER   A CB    1 
ATOM   6093  O  OG    . SER   A  1  837  ? -23.333 74.652  90.398  1.00 17.80 ? 835  SER   A OG    1 
ATOM   6094  N  N     . ALA   A  1  838  ? -24.814 78.878  90.181  1.00 15.46 ? 836  ALA   A N     1 
ATOM   6095  C  CA    . ALA   A  1  838  ? -24.596 80.318  90.151  1.00 15.34 ? 836  ALA   A CA    1 
ATOM   6096  C  C     . ALA   A  1  838  ? -25.670 81.080  90.907  1.00 19.21 ? 836  ALA   A C     1 
ATOM   6097  O  O     . ALA   A  1  838  ? -25.379 82.112  91.516  1.00 18.32 ? 836  ALA   A O     1 
ATOM   6098  C  CB    . ALA   A  1  838  ? -24.534 80.824  88.708  1.00 18.24 ? 836  ALA   A CB    1 
ATOM   6099  N  N     . PHE   A  1  839  ? -26.918 80.624  90.844  1.00 17.04 ? 837  PHE   A N     1 
ATOM   6100  C  CA    . PHE   A  1  839  ? -28.028 81.453  91.288  1.00 17.47 ? 837  PHE   A CA    1 
ATOM   6101  C  C     . PHE   A  1  839  ? -28.832 80.911  92.453  1.00 20.23 ? 837  PHE   A C     1 
ATOM   6102  O  O     . PHE   A  1  839  ? -29.620 81.671  93.034  1.00 19.72 ? 837  PHE   A O     1 
ATOM   6103  C  CB    . PHE   A  1  839  ? -28.960 81.780  90.118  1.00 17.91 ? 837  PHE   A CB    1 
ATOM   6104  C  CG    . PHE   A  1  839  ? -28.239 82.374  88.954  1.00 17.54 ? 837  PHE   A CG    1 
ATOM   6105  C  CD1   . PHE   A  1  839  ? -27.538 83.554  89.097  1.00 20.81 ? 837  PHE   A CD1   1 
ATOM   6106  C  CD2   . PHE   A  1  839  ? -28.233 81.734  87.723  1.00 18.93 ? 837  PHE   A CD2   1 
ATOM   6107  C  CE1   . PHE   A  1  839  ? -26.858 84.109  88.035  1.00 19.24 ? 837  PHE   A CE1   1 
ATOM   6108  C  CE2   . PHE   A  1  839  ? -27.553 82.279  86.658  1.00 21.93 ? 837  PHE   A CE2   1 
ATOM   6109  C  CZ    . PHE   A  1  839  ? -26.869 83.468  86.810  1.00 21.97 ? 837  PHE   A CZ    1 
ATOM   6110  N  N     . ASP   A  1  840  ? -28.674 79.641  92.812  1.00 20.51 ? 838  ASP   A N     1 
ATOM   6111  C  CA    . ASP   A  1  840  ? -29.267 79.154  94.046  1.00 19.45 ? 838  ASP   A CA    1 
ATOM   6112  C  C     . ASP   A  1  840  ? -28.833 80.059  95.191  1.00 21.42 ? 838  ASP   A C     1 
ATOM   6113  O  O     . ASP   A  1  840  ? -27.684 80.507  95.248  1.00 21.00 ? 838  ASP   A O     1 
ATOM   6114  C  CB    . ASP   A  1  840  ? -28.794 77.721  94.284  1.00 23.92 ? 838  ASP   A CB    1 
ATOM   6115  C  CG    . ASP   A  1  840  ? -29.374 77.103  95.521  1.00 31.68 ? 838  ASP   A CG    1 
ATOM   6116  O  OD1   . ASP   A  1  840  ? -28.855 77.385  96.622  1.00 28.66 ? 838  ASP   A OD1   1 
ATOM   6117  O  OD2   . ASP   A  1  840  ? -30.338 76.320  95.378  1.00 35.49 ? 838  ASP   A OD2   1 
ATOM   6118  N  N     . SER   A  1  841  ? -29.775 80.373  96.079  1.00 20.16 ? 839  SER   A N     1 
ATOM   6119  C  CA    . SER   A  1  841  ? -29.512 81.284  97.191  1.00 19.47 ? 839  SER   A CA    1 
ATOM   6120  C  C     . SER   A  1  841  ? -29.017 82.643  96.704  1.00 19.41 ? 839  SER   A C     1 
ATOM   6121  O  O     . SER   A  1  841  ? -28.279 83.337  97.408  1.00 19.15 ? 839  SER   A O     1 
ATOM   6122  C  CB    . SER   A  1  841  ? -28.545 80.674  98.213  1.00 23.93 ? 839  SER   A CB    1 
ATOM   6123  O  OG    . SER   A  1  841  ? -28.951 79.359  98.560  1.00 28.63 ? 839  SER   A OG    1 
ATOM   6124  N  N     . ALA   A  1  842  ? -29.415 83.027  95.490  1.00 19.76 ? 840  ALA   A N     1 
ATOM   6125  C  CA    . ALA   A  1  842  ? -28.971 84.274  94.874  1.00 18.33 ? 840  ALA   A CA    1 
ATOM   6126  C  C     . ALA   A  1  842  ? -27.451 84.372  94.853  1.00 18.34 ? 840  ALA   A C     1 
ATOM   6127  O  O     . ALA   A  1  842  ? -26.877 85.439  95.054  1.00 20.85 ? 840  ALA   A O     1 
ATOM   6128  C  CB    . ALA   A  1  842  ? -29.606 85.507  95.527  1.00 18.64 ? 840  ALA   A CB    1 
ATOM   6129  N  N     . GLY   A  1  843  ? -26.798 83.238  94.606  1.00 18.46 ? 841  GLY   A N     1 
ATOM   6130  C  CA    . GLY   A  1  843  ? -25.346 83.225  94.548  1.00 17.76 ? 841  GLY   A CA    1 
ATOM   6131  C  C     . GLY   A  1  843  ? -24.662 83.451  95.873  1.00 18.21 ? 841  GLY   A C     1 
ATOM   6132  O  O     . GLY   A  1  843  ? -23.443 83.648  95.906  1.00 18.53 ? 841  GLY   A O     1 
ATOM   6133  N  N     . GLN   A  1  844  ? -25.405 83.400  96.969  1.00 17.43 ? 842  GLN   A N     1 
ATOM   6134  C  CA    . GLN   A  1  844  ? -24.849 83.663  98.290  1.00 17.19 ? 842  GLN   A CA    1 
ATOM   6135  C  C     . GLN   A  1  844  ? -24.435 82.370  98.978  1.00 19.44 ? 842  GLN   A C     1 
ATOM   6136  O  O     . GLN   A  1  844  ? -24.803 82.053  100.106 1.00 20.95 ? 842  GLN   A O     1 
ATOM   6137  C  CB    . GLN   A  1  844  ? -25.822 84.491  99.113  1.00 18.16 ? 842  GLN   A CB    1 
ATOM   6138  C  CG    . GLN   A  1  844  ? -26.043 85.864  98.487  1.00 18.74 ? 842  GLN   A CG    1 
ATOM   6139  C  CD    . GLN   A  1  844  ? -27.249 86.579  99.042  1.00 18.10 ? 842  GLN   A CD    1 
ATOM   6140  O  OE1   . GLN   A  1  844  ? -27.142 87.686  99.546  1.00 20.01 ? 842  GLN   A OE1   1 
ATOM   6141  N  NE2   . GLN   A  1  844  ? -28.411 85.955  98.930  1.00 21.01 ? 842  GLN   A NE2   1 
ATOM   6142  N  N     . ARG   A  1  845  ? -23.658 81.596  98.231  1.00 19.85 ? 843  ARG   A N     1 
ATOM   6143  C  CA    . ARG   A  1  845  ? -22.939 80.441  98.727  1.00 19.40 ? 843  ARG   A CA    1 
ATOM   6144  C  C     . ARG   A  1  845  ? -21.475 80.695  98.438  1.00 18.34 ? 843  ARG   A C     1 
ATOM   6145  O  O     . ARG   A  1  845  ? -21.128 81.205  97.371  1.00 18.02 ? 843  ARG   A O     1 
ATOM   6146  C  CB    . ARG   A  1  845  ? -23.349 79.169  97.988  1.00 20.13 ? 843  ARG   A CB    1 
ATOM   6147  C  CG    . ARG   A  1  845  ? -24.790 78.742  98.224  1.00 20.74 ? 843  ARG   A CG    1 
ATOM   6148  C  CD    . ARG   A  1  845  ? -25.093 77.457  97.481  1.00 23.19 ? 843  ARG   A CD    1 
ATOM   6149  N  NE    . ARG   A  1  845  ? -26.448 76.982  97.732  1.00 29.39 ? 843  ARG   A NE    1 
ATOM   6150  C  CZ    . ARG   A  1  845  ? -26.757 76.063  98.637  1.00 33.18 ? 843  ARG   A CZ    1 
ATOM   6151  N  NH1   . ARG   A  1  845  ? -25.828 75.488  99.383  1.00 32.91 ? 843  ARG   A NH1   1 
ATOM   6152  N  NH2   . ARG   A  1  845  ? -28.029 75.708  98.792  1.00 34.99 ? 843  ARG   A NH2   1 
ATOM   6153  N  N     . CYS   A  1  846  ? -20.611 80.361  99.389  1.00 18.26 ? 844  CYS   A N     1 
ATOM   6154  C  CA    . CYS   A  1  846  ? -19.196 80.535  99.117  1.00 19.24 ? 844  CYS   A CA    1 
ATOM   6155  C  C     . CYS   A  1  846  ? -18.756 79.662  97.952  1.00 17.64 ? 844  CYS   A C     1 
ATOM   6156  O  O     . CYS   A  1  846  ? -17.788 79.986  97.260  1.00 16.92 ? 844  CYS   A O     1 
ATOM   6157  C  CB    . CYS   A  1  846  ? -18.393 80.192  100.363 1.00 18.18 ? 844  CYS   A CB    1 
ATOM   6158  S  SG    . CYS   A  1  846  ? -18.797 78.604  101.103 1.00 20.50 ? 844  CYS   A SG    1 
ATOM   6159  N  N     . SER   A  1  847  ? -19.461 78.561  97.725  1.00 16.50 ? 845  SER   A N     1 
ATOM   6160  C  CA    . SER   A  1  847  ? -19.166 77.600  96.676  1.00 15.14 ? 845  SER   A CA    1 
ATOM   6161  C  C     . SER   A  1  847  ? -19.771 77.988  95.341  1.00 16.69 ? 845  SER   A C     1 
ATOM   6162  O  O     . SER   A  1  847  ? -19.562 77.267  94.359  1.00 16.10 ? 845  SER   A O     1 
ATOM   6163  C  CB    . SER   A  1  847  ? -19.746 76.259  97.087  1.00 16.66 ? 845  SER   A CB    1 
ATOM   6164  O  OG    . SER   A  1  847  ? -21.115 76.452  97.434  1.00 19.32 ? 845  SER   A OG    1 
ATOM   6165  N  N     . ALA   A  1  848  ? -20.512 79.093  95.286  1.00 17.04 ? 846  ALA   A N     1 
ATOM   6166  C  CA    . ALA   A  1  848  ? -21.301 79.409  94.102  1.00 15.85 ? 846  ALA   A CA    1 
ATOM   6167  C  C     . ALA   A  1  848  ? -20.417 79.582  92.874  1.00 16.71 ? 846  ALA   A C     1 
ATOM   6168  O  O     . ALA   A  1  848  ? -19.273 80.038  92.948  1.00 17.26 ? 846  ALA   A O     1 
ATOM   6169  C  CB    . ALA   A  1  848  ? -22.101 80.689  94.335  1.00 17.92 ? 846  ALA   A CB    1 
ATOM   6170  N  N     . LEU   A  1  849  ? -20.964 79.205  91.731  1.00 16.58 ? 847  LEU   A N     1 
ATOM   6171  C  CA    . LEU   A  1  849  ? -20.234 79.350  90.486  1.00 16.11 ? 847  LEU   A CA    1 
ATOM   6172  C  C     . LEU   A  1  849  ? -20.155 80.823  90.117  1.00 16.39 ? 847  LEU   A C     1 
ATOM   6173  O  O     . LEU   A  1  849  ? -21.189 81.478  89.953  1.00 17.82 ? 847  LEU   A O     1 
ATOM   6174  C  CB    . LEU   A  1  849  ? -20.974 78.585  89.400  1.00 16.27 ? 847  LEU   A CB    1 
ATOM   6175  C  CG    . LEU   A  1  849  ? -20.384 78.774  88.010  1.00 15.24 ? 847  LEU   A CG    1 
ATOM   6176  C  CD1   . LEU   A  1  849  ? -18.958 78.259  87.974  1.00 16.12 ? 847  LEU   A CD1   1 
ATOM   6177  C  CD2   . LEU   A  1  849  ? -21.245 78.049  86.999  1.00 17.49 ? 847  LEU   A CD2   1 
ATOM   6178  N  N     . ARG   A  1  850  ? -18.933 81.332  89.966  1.00 15.73 ? 848  ARG   A N     1 
ATOM   6179  C  CA    . ARG   A  1  850  ? -18.706 82.721  89.596  1.00 17.95 ? 848  ARG   A CA    1 
ATOM   6180  C  C     . ARG   A  1  850  ? -18.264 82.889  88.158  1.00 17.02 ? 848  ARG   A C     1 
ATOM   6181  O  O     . ARG   A  1  850  ? -18.533 83.932  87.559  1.00 18.74 ? 848  ARG   A O     1 
ATOM   6182  C  CB    . ARG   A  1  850  ? -17.634 83.343  90.500  1.00 18.57 ? 848  ARG   A CB    1 
ATOM   6183  C  CG    . ARG   A  1  850  ? -17.909 83.157  91.973  1.00 18.94 ? 848  ARG   A CG    1 
ATOM   6184  C  CD    . ARG   A  1  850  ? -19.283 83.650  92.338  1.00 20.38 ? 848  ARG   A CD    1 
ATOM   6185  N  NE    . ARG   A  1  850  ? -19.459 83.606  93.781  1.00 19.89 ? 848  ARG   A NE    1 
ATOM   6186  C  CZ    . ARG   A  1  850  ? -20.606 83.847  94.396  1.00 19.81 ? 848  ARG   A CZ    1 
ATOM   6187  N  NH1   . ARG   A  1  850  ? -21.705 84.153  93.719  1.00 17.32 ? 848  ARG   A NH1   1 
ATOM   6188  N  NH2   . ARG   A  1  850  ? -20.654 83.770  95.721  1.00 18.84 ? 848  ARG   A NH2   1 
ATOM   6189  N  N     . VAL   A  1  851  ? -17.555 81.910  87.603  1.00 18.54 ? 849  VAL   A N     1 
ATOM   6190  C  CA    . VAL   A  1  851  ? -16.971 82.054  86.274  1.00 18.48 ? 849  VAL   A CA    1 
ATOM   6191  C  C     . VAL   A  1  851  ? -17.229 80.766  85.518  1.00 17.85 ? 849  VAL   A C     1 
ATOM   6192  O  O     . VAL   A  1  851  ? -16.655 79.724  85.853  1.00 18.30 ? 849  VAL   A O     1 
ATOM   6193  C  CB    . VAL   A  1  851  ? -15.462 82.328  86.314  1.00 21.56 ? 849  VAL   A CB    1 
ATOM   6194  C  CG1   . VAL   A  1  851  ? -14.965 82.603  84.904  1.00 24.74 ? 849  VAL   A CG1   1 
ATOM   6195  C  CG2   . VAL   A  1  851  ? -15.126 83.476  87.243  1.00 23.04 ? 849  VAL   A CG2   1 
ATOM   6196  N  N     . LEU   A  1  852  ? -18.082 80.831  84.502  1.00 16.45 ? 850  LEU   A N     1 
ATOM   6197  C  CA    . LEU   A  1  852  ? -18.325 79.699  83.623  1.00 17.46 ? 850  LEU   A CA    1 
ATOM   6198  C  C     . LEU   A  1  852  ? -17.431 79.846  82.402  1.00 17.17 ? 850  LEU   A C     1 
ATOM   6199  O  O     . LEU   A  1  852  ? -17.411 80.905  81.766  1.00 17.28 ? 850  LEU   A O     1 
ATOM   6200  C  CB    . LEU   A  1  852  ? -19.782 79.711  83.183  1.00 16.01 ? 850  LEU   A CB    1 
ATOM   6201  C  CG    . LEU   A  1  852  ? -20.198 78.645  82.180  1.00 17.89 ? 850  LEU   A CG    1 
ATOM   6202  C  CD1   . LEU   A  1  852  ? -20.012 77.247  82.749  1.00 16.94 ? 850  LEU   A CD1   1 
ATOM   6203  C  CD2   . LEU   A  1  852  ? -21.661 78.890  81.780  1.00 18.00 ? 850  LEU   A CD2   1 
ATOM   6204  N  N     . CYS   A  1  853  ? -16.688 78.793  82.084  1.00 17.57 ? 851  CYS   A N     1 
ATOM   6205  C  CA    . CYS   A  1  853  ? -15.711 78.830  81.003  1.00 16.10 ? 851  CYS   A CA    1 
ATOM   6206  C  C     . CYS   A  1  853  ? -16.165 77.832  79.958  1.00 16.39 ? 851  CYS   A C     1 
ATOM   6207  O  O     . CYS   A  1  853  ? -16.191 76.628  80.218  1.00 17.57 ? 851  CYS   A O     1 
ATOM   6208  C  CB    . CYS   A  1  853  ? -14.327 78.452  81.512  1.00 17.94 ? 851  CYS   A CB    1 
ATOM   6209  S  SG    . CYS   A  1  853  ? -13.767 79.381  82.926  1.00 20.58 ? 851  CYS   A SG    1 
ATOM   6210  N  N     . LEU   A  1  854  ? -16.538 78.336  78.791  1.00 17.85 ? 852  LEU   A N     1 
ATOM   6211  C  CA    . LEU   A  1  854  ? -17.154 77.531  77.750  1.00 17.26 ? 852  LEU   A CA    1 
ATOM   6212  C  C     . LEU   A  1  854  ? -16.195 77.395  76.583  1.00 16.90 ? 852  LEU   A C     1 
ATOM   6213  O  O     . LEU   A  1  854  ? -15.681 78.395  76.074  1.00 19.24 ? 852  LEU   A O     1 
ATOM   6214  C  CB    . LEU   A  1  854  ? -18.423 78.212  77.239  1.00 17.89 ? 852  LEU   A CB    1 
ATOM   6215  C  CG    . LEU   A  1  854  ? -19.523 78.408  78.281  1.00 17.73 ? 852  LEU   A CG    1 
ATOM   6216  C  CD1   . LEU   A  1  854  ? -20.714 79.153  77.671  1.00 17.94 ? 852  LEU   A CD1   1 
ATOM   6217  C  CD2   . LEU   A  1  854  ? -19.939 77.056  78.810  1.00 18.69 ? 852  LEU   A CD2   1 
ATOM   6218  N  N     . GLN   A  1  855  ? -15.999 76.162  76.134  1.00 16.89 ? 853  GLN   A N     1 
ATOM   6219  C  CA    . GLN   A  1  855  ? -15.194 75.964  74.946  1.00 17.67 ? 853  GLN   A CA    1 
ATOM   6220  C  C     . GLN   A  1  855  ? -15.878 76.648  73.771  1.00 19.53 ? 853  GLN   A C     1 
ATOM   6221  O  O     . GLN   A  1  855  ? -17.102 76.589  73.626  1.00 20.17 ? 853  GLN   A O     1 
ATOM   6222  C  CB    . GLN   A  1  855  ? -15.018 74.479  74.677  1.00 17.38 ? 853  GLN   A CB    1 
ATOM   6223  C  CG    . GLN   A  1  855  ? -13.928 74.234  73.663  1.00 18.73 ? 853  GLN   A CG    1 
ATOM   6224  C  CD    . GLN   A  1  855  ? -13.860 72.800  73.224  1.00 21.84 ? 853  GLN   A CD    1 
ATOM   6225  O  OE1   . GLN   A  1  855  ? -13.925 71.885  74.035  1.00 23.68 ? 853  GLN   A OE1   1 
ATOM   6226  N  NE2   . GLN   A  1  855  ? -13.717 72.595  71.919  1.00 25.39 ? 853  GLN   A NE2   1 
ATOM   6227  N  N     . GLU   A  1  856  ? -15.066 77.305  72.942  1.00 20.10 ? 854  GLU   A N     1 
ATOM   6228  C  CA    . GLU   A  1  856  ? -15.582 78.263  71.970  1.00 21.96 ? 854  GLU   A CA    1 
ATOM   6229  C  C     . GLU   A  1  856  ? -16.628 77.634  71.063  1.00 23.63 ? 854  GLU   A C     1 
ATOM   6230  O  O     . GLU   A  1  856  ? -17.638 78.268  70.741  1.00 24.06 ? 854  GLU   A O     1 
ATOM   6231  C  CB    . GLU   A  1  856  ? -14.417 78.829  71.155  1.00 23.74 ? 854  GLU   A CB    1 
ATOM   6232  C  CG    . GLU   A  1  856  ? -14.836 79.753  70.017  1.00 27.39 ? 854  GLU   A CG    1 
ATOM   6233  C  CD    . GLU   A  1  856  ? -15.589 80.974  70.503  1.00 35.58 ? 854  GLU   A CD    1 
ATOM   6234  O  OE1   . GLU   A  1  856  ? -15.222 81.509  71.574  1.00 31.67 ? 854  GLU   A OE1   1 
ATOM   6235  O  OE2   . GLU   A  1  856  ? -16.546 81.396  69.816  1.00 36.03 ? 854  GLU   A OE2   1 
ATOM   6236  N  N     . ASP   A  1  857  ? -16.421 76.374  70.667  1.00 21.83 ? 855  ASP   A N     1 
ATOM   6237  C  CA    . ASP   A  1  857  ? -17.282 75.734  69.677  1.00 26.67 ? 855  ASP   A CA    1 
ATOM   6238  C  C     . ASP   A  1  857  ? -18.694 75.473  70.192  1.00 25.09 ? 855  ASP   A C     1 
ATOM   6239  O  O     . ASP   A  1  857  ? -19.612 75.293  69.382  1.00 27.49 ? 855  ASP   A O     1 
ATOM   6240  C  CB    . ASP   A  1  857  ? -16.650 74.421  69.209  1.00 30.35 ? 855  ASP   A CB    1 
ATOM   6241  N  N     . VAL   A  1  858  ? -18.893 75.441  71.508  1.00 19.81 ? 856  VAL   A N     1 
ATOM   6242  C  CA    . VAL   A  1  858  ? -20.208 75.223  72.090  1.00 21.29 ? 856  VAL   A CA    1 
ATOM   6243  C  C     . VAL   A  1  858  ? -20.701 76.425  72.871  1.00 19.36 ? 856  VAL   A C     1 
ATOM   6244  O  O     . VAL   A  1  858  ? -21.812 76.383  73.417  1.00 19.47 ? 856  VAL   A O     1 
ATOM   6245  C  CB    . VAL   A  1  858  ? -20.257 73.948  72.957  1.00 21.81 ? 856  VAL   A CB    1 
ATOM   6246  C  CG1   . VAL   A  1  858  ? -19.998 72.716  72.098  1.00 24.63 ? 856  VAL   A CG1   1 
ATOM   6247  C  CG2   . VAL   A  1  858  ? -19.243 74.041  74.104  1.00 21.84 ? 856  VAL   A CG2   1 
ATOM   6248  N  N     . ALA   A  1  859  ? -19.924 77.505  72.913  1.00 19.67 ? 857  ALA   A N     1 
ATOM   6249  C  CA    . ALA   A  1  859  ? -20.225 78.608  73.818  1.00 18.73 ? 857  ALA   A CA    1 
ATOM   6250  C  C     . ALA   A  1  859  ? -21.544 79.277  73.462  1.00 20.51 ? 857  ALA   A C     1 
ATOM   6251  O  O     . ALA   A  1  859  ? -22.369 79.537  74.343  1.00 20.91 ? 857  ALA   A O     1 
ATOM   6252  C  CB    . ALA   A  1  859  ? -19.090 79.621  73.809  1.00 20.32 ? 857  ALA   A CB    1 
ATOM   6253  N  N     . ASP   A  1  860  ? -21.768 79.549  72.172  1.00 21.95 ? 858  ASP   A N     1 
ATOM   6254  C  CA    . ASP   A  1  860  ? -22.983 80.253  71.772  1.00 24.57 ? 858  ASP   A CA    1 
ATOM   6255  C  C     . ASP   A  1  860  ? -24.226 79.436  72.097  1.00 22.75 ? 858  ASP   A C     1 
ATOM   6256  O  O     . ASP   A  1  860  ? -25.209 79.966  72.631  1.00 22.62 ? 858  ASP   A O     1 
ATOM   6257  C  CB    . ASP   A  1  860  ? -22.938 80.599  70.283  1.00 24.29 ? 858  ASP   A CB    1 
ATOM   6258  C  CG    . ASP   A  1  860  ? -21.956 81.706  69.969  1.00 30.91 ? 858  ASP   A CG    1 
ATOM   6259  O  OD1   . ASP   A  1  860  ? -21.694 82.551  70.852  1.00 33.49 ? 858  ASP   A OD1   1 
ATOM   6260  O  OD2   . ASP   A  1  860  ? -21.456 81.733  68.826  1.00 47.28 ? 858  ASP   A OD2   1 
ATOM   6261  N  N     . ARG   A  1  861  ? -24.205 78.140  71.785  1.00 20.38 ? 859  ARG   A N     1 
ATOM   6262  C  CA    . ARG   A  1  861  ? -25.368 77.308  72.060  1.00 25.91 ? 859  ARG   A CA    1 
ATOM   6263  C  C     . ARG   A  1  861  ? -25.640 77.217  73.554  1.00 19.84 ? 859  ARG   A C     1 
ATOM   6264  O  O     . ARG   A  1  861  ? -26.790 77.330  73.991  1.00 19.96 ? 859  ARG   A O     1 
ATOM   6265  C  CB    . ARG   A  1  861  ? -25.193 75.917  71.453  1.00 27.85 ? 859  ARG   A CB    1 
ATOM   6266  C  CG    . ARG   A  1  861  ? -26.198 74.915  71.983  1.00 34.47 ? 859  ARG   A CG    1 
ATOM   6267  C  CD    . ARG   A  1  861  ? -26.358 73.715  71.077  1.00 42.24 ? 859  ARG   A CD    1 
ATOM   6268  N  NE    . ARG   A  1  861  ? -27.554 72.963  71.439  1.00 49.37 ? 859  ARG   A NE    1 
ATOM   6269  C  CZ    . ARG   A  1  861  ? -27.558 71.902  72.234  1.00 42.52 ? 859  ARG   A CZ    1 
ATOM   6270  N  NH1   . ARG   A  1  861  ? -26.437 71.409  72.734  1.00 44.23 ? 859  ARG   A NH1   1 
ATOM   6271  N  NH2   . ARG   A  1  861  ? -28.716 71.319  72.531  1.00 44.24 ? 859  ARG   A NH2   1 
ATOM   6272  N  N     . ILE   A  1  862  ? -24.599 77.008  74.355  1.00 18.81 ? 860  ILE   A N     1 
ATOM   6273  C  CA    . ILE   A  1  862  ? -24.814 76.893  75.792  1.00 19.19 ? 860  ILE   A CA    1 
ATOM   6274  C  C     . ILE   A  1  862  ? -25.268 78.223  76.368  1.00 18.80 ? 860  ILE   A C     1 
ATOM   6275  O  O     . ILE   A  1  862  ? -26.172 78.273  77.212  1.00 16.95 ? 860  ILE   A O     1 
ATOM   6276  C  CB    . ILE   A  1  862  ? -23.547 76.366  76.482  1.00 19.21 ? 860  ILE   A CB    1 
ATOM   6277  C  CG1   . ILE   A  1  862  ? -23.343 74.894  76.126  1.00 21.15 ? 860  ILE   A CG1   1 
ATOM   6278  C  CG2   . ILE   A  1  862  ? -23.658 76.551  77.994  1.00 21.18 ? 860  ILE   A CG2   1 
ATOM   6279  C  CD1   . ILE   A  1  862  ? -21.992 74.355  76.558  1.00 23.03 ? 860  ILE   A CD1   1 
ATOM   6280  N  N     . LEU   A  1  863  ? -24.663 79.319  75.913  1.00 18.01 ? 861  LEU   A N     1 
ATOM   6281  C  CA    . LEU   A  1  863  ? -25.032 80.635  76.416  1.00 17.79 ? 861  LEU   A CA    1 
ATOM   6282  C  C     . LEU   A  1  863  ? -26.479 80.963  76.084  1.00 18.80 ? 861  LEU   A C     1 
ATOM   6283  O  O     . LEU   A  1  863  ? -27.211 81.489  76.928  1.00 19.14 ? 861  LEU   A O     1 
ATOM   6284  C  CB    . LEU   A  1  863  ? -24.088 81.689  75.845  1.00 21.67 ? 861  LEU   A CB    1 
ATOM   6285  C  CG    . LEU   A  1  863  ? -24.078 83.059  76.498  1.00 27.88 ? 861  LEU   A CG    1 
ATOM   6286  C  CD1   . LEU   A  1  863  ? -23.971 82.942  78.014  1.00 25.05 ? 861  LEU   A CD1   1 
ATOM   6287  C  CD2   . LEU   A  1  863  ? -22.899 83.828  75.935  1.00 33.53 ? 861  LEU   A CD2   1 
ATOM   6288  N  N     . THR   A  1  864  ? -26.916 80.643  74.866  1.00 17.82 ? 862  THR   A N     1 
ATOM   6289  C  CA    . THR   A  1  864  ? -28.324 80.827  74.524  1.00 19.09 ? 862  THR   A CA    1 
ATOM   6290  C  C     . THR   A  1  864  ? -29.218 80.030  75.463  1.00 18.53 ? 862  THR   A C     1 
ATOM   6291  O  O     . THR   A  1  864  ? -30.210 80.548  75.984  1.00 19.03 ? 862  THR   A O     1 
ATOM   6292  C  CB    . THR   A  1  864  ? -28.563 80.409  73.077  1.00 20.47 ? 862  THR   A CB    1 
ATOM   6293  O  OG1   . THR   A  1  864  ? -27.847 81.299  72.222  1.00 22.81 ? 862  THR   A OG1   1 
ATOM   6294  C  CG2   . THR   A  1  864  ? -30.063 80.441  72.742  1.00 22.03 ? 862  THR   A CG2   1 
ATOM   6295  N  N     . MET   A  1  865  ? -28.879 78.761  75.691  1.00 16.66 ? 863  MET   A N     1 
ATOM   6296  C  CA    . MET   A  1  865  ? -29.690 77.947  76.581  1.00 16.93 ? 863  MET   A CA    1 
ATOM   6297  C  C     . MET   A  1  865  ? -29.645 78.486  78.001  1.00 15.97 ? 863  MET   A C     1 
ATOM   6298  O  O     . MET   A  1  865  ? -30.663 78.506  78.701  1.00 15.96 ? 863  MET   A O     1 
ATOM   6299  C  CB    . MET   A  1  865  ? -29.209 76.503  76.537  1.00 18.32 ? 863  MET   A CB    1 
ATOM   6300  C  CG    . MET   A  1  865  ? -30.068 75.535  77.311  1.00 21.67 ? 863  MET   A CG    1 
ATOM   6301  S  SD    . MET   A  1  865  ? -29.412 73.870  77.132  1.00 25.60 ? 863  MET   A SD    1 
ATOM   6302  C  CE    . MET   A  1  865  ? -28.932 74.019  75.399  1.00 21.86 ? 863  MET   A CE    1 
ATOM   6303  N  N     . LEU   A  1  866  ? -28.476 78.954  78.428  1.00 16.40 ? 864  LEU   A N     1 
ATOM   6304  C  CA    . LEU   A  1  866  ? -28.340 79.474  79.780  1.00 17.25 ? 864  LEU   A CA    1 
ATOM   6305  C  C     . LEU   A  1  866  ? -29.197 80.716  79.988  1.00 15.84 ? 864  LEU   A C     1 
ATOM   6306  O  O     . LEU   A  1  866  ? -29.852 80.857  81.026  1.00 17.52 ? 864  LEU   A O     1 
ATOM   6307  C  CB    . LEU   A  1  866  ? -26.870 79.787  80.030  1.00 17.14 ? 864  LEU   A CB    1 
ATOM   6308  C  CG    . LEU   A  1  866  ? -26.560 80.337  81.412  1.00 21.97 ? 864  LEU   A CG    1 
ATOM   6309  C  CD1   . LEU   A  1  866  ? -26.942 79.318  82.469  1.00 22.16 ? 864  LEU   A CD1   1 
ATOM   6310  C  CD2   . LEU   A  1  866  ? -25.092 80.695  81.497  1.00 21.43 ? 864  LEU   A CD2   1 
ATOM   6311  N  N     . LYS   A  1  867  ? -29.184 81.638  79.021  1.00 16.83 ? 865  LYS   A N     1 
ATOM   6312  C  CA    . LYS   A  1  867  ? -30.004 82.836  79.135  1.00 18.45 ? 865  LYS   A CA    1 
ATOM   6313  C  C     . LYS   A  1  867  ? -31.480 82.480  79.143  1.00 18.19 ? 865  LYS   A C     1 
ATOM   6314  O  O     . LYS   A  1  867  ? -32.267 83.079  79.883  1.00 18.89 ? 865  LYS   A O     1 
ATOM   6315  C  CB    . LYS   A  1  867  ? -29.688 83.797  77.991  1.00 18.05 ? 865  LYS   A CB    1 
ATOM   6316  C  CG    . LYS   A  1  867  ? -28.265 84.336  78.066  1.00 21.26 ? 865  LYS   A CG    1 
ATOM   6317  C  CD    . LYS   A  1  867  ? -27.906 85.193  76.863  1.00 22.69 ? 865  LYS   A CD    1 
ATOM   6318  C  CE    . LYS   A  1  867  ? -26.510 85.761  77.048  1.00 25.82 ? 865  LYS   A CE    1 
ATOM   6319  N  NZ    . LYS   A  1  867  ? -25.946 86.396  75.821  1.00 31.52 ? 865  LYS   A NZ    1 
ATOM   6320  N  N     . GLY   A  1  868  ? -31.878 81.506  78.328  1.00 17.41 ? 866  GLY   A N     1 
ATOM   6321  C  CA    . GLY   A  1  868  ? -33.265 81.087  78.336  1.00 18.25 ? 866  GLY   A CA    1 
ATOM   6322  C  C     . GLY   A  1  868  ? -33.656 80.491  79.670  1.00 16.73 ? 866  GLY   A C     1 
ATOM   6323  O  O     . GLY   A  1  868  ? -34.751 80.747  80.179  1.00 18.42 ? 866  GLY   A O     1 
ATOM   6324  N  N     . ALA   A  1  869  ? -32.758 79.703  80.267  1.00 16.06 ? 867  ALA   A N     1 
ATOM   6325  C  CA    . ALA   A  1  869  ? -33.056 79.121  81.567  1.00 16.88 ? 867  ALA   A CA    1 
ATOM   6326  C  C     . ALA   A  1  869  ? -33.101 80.196  82.638  1.00 16.52 ? 867  ALA   A C     1 
ATOM   6327  O  O     . ALA   A  1  869  ? -33.920 80.127  83.561  1.00 16.83 ? 867  ALA   A O     1 
ATOM   6328  C  CB    . ALA   A  1  869  ? -31.998 78.084  81.926  1.00 17.94 ? 867  ALA   A CB    1 
ATOM   6329  N  N     . LEU   A  1  870  ? -32.235 81.204  82.515  1.00 16.04 ? 868  LEU   A N     1 
ATOM   6330  C  CA    . LEU   A  1  870  ? -32.210 82.292  83.485  1.00 18.33 ? 868  LEU   A CA    1 
ATOM   6331  C  C     . LEU   A  1  870  ? -33.574 82.944  83.593  1.00 19.06 ? 868  LEU   A C     1 
ATOM   6332  O  O     . LEU   A  1  870  ? -34.040 83.264  84.693  1.00 19.86 ? 868  LEU   A O     1 
ATOM   6333  C  CB    . LEU   A  1  870  ? -31.193 83.341  83.041  1.00 19.86 ? 868  LEU   A CB    1 
ATOM   6334  C  CG    . LEU   A  1  870  ? -30.910 84.502  83.993  1.00 22.86 ? 868  LEU   A CG    1 
ATOM   6335  C  CD1   . LEU   A  1  870  ? -29.875 84.078  85.010  1.00 24.98 ? 868  LEU   A CD1   1 
ATOM   6336  C  CD2   . LEU   A  1  870  ? -30.434 85.739  83.240  1.00 25.33 ? 868  LEU   A CD2   1 
ATOM   6337  N  N     . HIS   A  1  871  ? -34.236 83.143  82.458  1.00 17.39 ? 869  HIS   A N     1 
ATOM   6338  C  CA    . HIS   A  1  871  ? -35.490 83.876  82.470  1.00 19.43 ? 869  HIS   A CA    1 
ATOM   6339  C  C     . HIS   A  1  871  ? -36.659 83.063  82.989  1.00 20.75 ? 869  HIS   A C     1 
ATOM   6340  O  O     . HIS   A  1  871  ? -37.753 83.616  83.139  1.00 21.68 ? 869  HIS   A O     1 
ATOM   6341  C  CB    . HIS   A  1  871  ? -35.777 84.433  81.086  1.00 22.06 ? 869  HIS   A CB    1 
ATOM   6342  C  CG    . HIS   A  1  871  ? -34.871 85.562  80.730  1.00 24.30 ? 869  HIS   A CG    1 
ATOM   6343  N  ND1   . HIS   A  1  871  ? -34.975 86.805  81.317  1.00 26.11 ? 869  HIS   A ND1   1 
ATOM   6344  C  CD2   . HIS   A  1  871  ? -33.802 85.621  79.903  1.00 22.07 ? 869  HIS   A CD2   1 
ATOM   6345  C  CE1   . HIS   A  1  871  ? -34.027 87.591  80.840  1.00 27.66 ? 869  HIS   A CE1   1 
ATOM   6346  N  NE2   . HIS   A  1  871  ? -33.299 86.896  79.983  1.00 25.64 ? 869  HIS   A NE2   1 
ATOM   6347  N  N     . GLU   A  1  872  ? -36.457 81.784  83.267  1.00 16.97 ? 870  GLU   A N     1 
ATOM   6348  C  CA    . GLU   A  1  872  ? -37.490 80.954  83.870  1.00 18.76 ? 870  GLU   A CA    1 
ATOM   6349  C  C     . GLU   A  1  872  ? -37.435 80.946  85.389  1.00 19.84 ? 870  GLU   A C     1 
ATOM   6350  O  O     . GLU   A  1  872  ? -38.257 80.272  86.022  1.00 19.43 ? 870  GLU   A O     1 
ATOM   6351  C  CB    . GLU   A  1  872  ? -37.377 79.519  83.352  1.00 17.42 ? 870  GLU   A CB    1 
ATOM   6352  C  CG    . GLU   A  1  872  ? -37.571 79.412  81.852  1.00 19.73 ? 870  GLU   A CG    1 
ATOM   6353  C  CD    . GLU   A  1  872  ? -38.943 79.857  81.406  1.00 22.74 ? 870  GLU   A CD    1 
ATOM   6354  O  OE1   . GLU   A  1  872  ? -39.894 79.784  82.217  1.00 22.54 ? 870  GLU   A OE1   1 
ATOM   6355  O  OE2   . GLU   A  1  872  ? -39.075 80.288  80.239  1.00 22.10 ? 870  GLU   A OE2   1 
ATOM   6356  N  N     . LEU   A  1  873  ? -36.503 81.679  85.989  1.00 18.06 ? 871  LEU   A N     1 
ATOM   6357  C  CA    . LEU   A  1  873  ? -36.387 81.712  87.436  1.00 18.36 ? 871  LEU   A CA    1 
ATOM   6358  C  C     . LEU   A  1  873  ? -37.366 82.715  88.024  1.00 18.69 ? 871  LEU   A C     1 
ATOM   6359  O  O     . LEU   A  1  873  ? -37.569 83.805  87.480  1.00 21.04 ? 871  LEU   A O     1 
ATOM   6360  C  CB    . LEU   A  1  873  ? -34.971 82.113  87.837  1.00 18.80 ? 871  LEU   A CB    1 
ATOM   6361  C  CG    . LEU   A  1  873  ? -33.888 81.165  87.333  1.00 18.53 ? 871  LEU   A CG    1 
ATOM   6362  C  CD1   . LEU   A  1  873  ? -32.506 81.717  87.681  1.00 21.75 ? 871  LEU   A CD1   1 
ATOM   6363  C  CD2   . LEU   A  1  873  ? -34.069 79.786  87.933  1.00 22.27 ? 871  LEU   A CD2   1 
ATOM   6364  N  N     . HIS   A  1  874  ? -37.956 82.335  89.153  1.00 18.39 ? 872  HIS   A N     1 
ATOM   6365  C  CA    . HIS   A  1  874  ? -38.868 83.175  89.911  1.00 18.30 ? 872  HIS   A CA    1 
ATOM   6366  C  C     . HIS   A  1  874  ? -38.105 83.743  91.100  1.00 18.94 ? 872  HIS   A C     1 
ATOM   6367  O  O     . HIS   A  1  874  ? -37.631 82.991  91.959  1.00 19.33 ? 872  HIS   A O     1 
ATOM   6368  C  CB    . HIS   A  1  874  ? -40.046 82.323  90.387  1.00 21.03 ? 872  HIS   A CB    1 
ATOM   6369  C  CG    . HIS   A  1  874  ? -41.094 83.069  91.158  1.00 22.65 ? 872  HIS   A CG    1 
ATOM   6370  N  ND1   . HIS   A  1  874  ? -41.078 84.435  91.342  1.00 28.70 ? 872  HIS   A ND1   1 
ATOM   6371  C  CD2   . HIS   A  1  874  ? -42.206 82.621  91.789  1.00 29.02 ? 872  HIS   A CD2   1 
ATOM   6372  C  CE1   . HIS   A  1  874  ? -42.131 84.796  92.058  1.00 23.31 ? 872  HIS   A CE1   1 
ATOM   6373  N  NE2   . HIS   A  1  874  ? -42.826 83.712  92.347  1.00 30.07 ? 872  HIS   A NE2   1 
ATOM   6374  N  N     . ILE   A  1  875  ? -38.002 85.065  91.143  1.00 19.35 ? 873  ILE   A N     1 
ATOM   6375  C  CA    . ILE   A  1  875  ? -37.305 85.783  92.198  1.00 20.13 ? 873  ILE   A CA    1 
ATOM   6376  C  C     . ILE   A  1  875  ? -38.357 86.433  93.084  1.00 21.45 ? 873  ILE   A C     1 
ATOM   6377  O  O     . ILE   A  1  875  ? -39.271 87.105  92.586  1.00 22.14 ? 873  ILE   A O     1 
ATOM   6378  C  CB    . ILE   A  1  875  ? -36.347 86.835  91.612  1.00 21.13 ? 873  ILE   A CB    1 
ATOM   6379  C  CG1   . ILE   A  1  875  ? -35.078 86.189  91.043  1.00 23.50 ? 873  ILE   A CG1   1 
ATOM   6380  C  CG2   . ILE   A  1  875  ? -35.900 87.805  92.681  1.00 24.15 ? 873  ILE   A CG2   1 
ATOM   6381  C  CD1   . ILE   A  1  875  ? -35.257 85.246  89.863  1.00 25.95 ? 873  ILE   A CD1   1 
ATOM   6382  N  N     . GLY   A  1  876  ? -38.251 86.221  94.389  1.00 20.42 ? 874  GLY   A N     1 
ATOM   6383  C  CA    . GLY   A  1  876  ? -39.185 86.873  95.287  1.00 19.21 ? 874  GLY   A CA    1 
ATOM   6384  C  C     . GLY   A  1  876  ? -38.965 86.461  96.723  1.00 20.22 ? 874  GLY   A C     1 
ATOM   6385  O  O     . GLY   A  1  876  ? -38.005 85.760  97.058  1.00 20.57 ? 874  GLY   A O     1 
ATOM   6386  N  N     . ARG   A  1  877  ? -39.863 86.949  97.579  1.00 21.40 ? 875  ARG   A N     1 
ATOM   6387  C  CA    . ARG   A  1  877  ? -39.872 86.535  98.973  1.00 22.47 ? 875  ARG   A CA    1 
ATOM   6388  C  C     . ARG   A  1  877  ? -40.013 85.020  99.043  1.00 21.22 ? 875  ARG   A C     1 
ATOM   6389  O  O     . ARG   A  1  877  ? -40.847 84.423  98.354  1.00 21.27 ? 875  ARG   A O     1 
ATOM   6390  C  CB    . ARG   A  1  877  ? -41.023 87.222  99.705  1.00 24.37 ? 875  ARG   A CB    1 
ATOM   6391  C  CG    . ARG   A  1  877  ? -40.829 87.240  101.192 1.00 24.52 ? 875  ARG   A CG    1 
ATOM   6392  C  CD    . ARG   A  1  877  ? -41.923 88.035  101.847 1.00 29.02 ? 875  ARG   A CD    1 
ATOM   6393  N  NE    . ARG   A  1  877  ? -43.105 87.225  102.089 1.00 26.06 ? 875  ARG   A NE    1 
ATOM   6394  C  CZ    . ARG   A  1  877  ? -44.176 87.670  102.730 1.00 29.79 ? 875  ARG   A CZ    1 
ATOM   6395  N  NH1   . ARG   A  1  877  ? -44.247 88.918  103.166 1.00 32.61 ? 875  ARG   A NH1   1 
ATOM   6396  N  NH2   . ARG   A  1  877  ? -45.195 86.843  102.944 1.00 33.78 ? 875  ARG   A NH2   1 
ATOM   6397  N  N     . THR   A  1  878  ? -39.184 84.394  99.864  1.00 22.44 ? 876  THR   A N     1 
ATOM   6398  C  CA    . THR   A  1  878  ? -38.961 82.963  99.751  1.00 20.29 ? 876  THR   A CA    1 
ATOM   6399  C  C     . THR   A  1  878  ? -39.959 82.110  100.517 1.00 21.69 ? 876  THR   A C     1 
ATOM   6400  O  O     . THR   A  1  878  ? -39.785 80.887  100.572 1.00 21.36 ? 876  THR   A O     1 
ATOM   6401  C  CB    . THR   A  1  878  ? -37.542 82.633  100.200 1.00 20.59 ? 876  THR   A CB    1 
ATOM   6402  O  OG1   . THR   A  1  878  ? -37.315 83.239  101.471 1.00 24.08 ? 876  THR   A OG1   1 
ATOM   6403  C  CG2   . THR   A  1  878  ? -36.549 83.178  99.210  1.00 24.93 ? 876  THR   A CG2   1 
ATOM   6404  N  N     . ASP   A  1  879  ? -41.002 82.704  101.086 1.00 21.00 ? 877  ASP   A N     1 
ATOM   6405  C  CA    . ASP   A  1  879  ? -42.040 81.920  101.743 1.00 24.61 ? 877  ASP   A CA    1 
ATOM   6406  C  C     . ASP   A  1  879  ? -43.075 81.365  100.759 1.00 21.84 ? 877  ASP   A C     1 
ATOM   6407  O  O     . ASP   A  1  879  ? -44.220 81.091  101.148 1.00 21.47 ? 877  ASP   A O     1 
ATOM   6408  C  CB    . ASP   A  1  879  ? -42.696 82.724  102.870 1.00 21.54 ? 877  ASP   A CB    1 
ATOM   6409  C  CG    . ASP   A  1  879  ? -43.453 83.933  102.364 1.00 29.23 ? 877  ASP   A CG    1 
ATOM   6410  O  OD1   . ASP   A  1  879  ? -43.039 84.522  101.340 1.00 29.49 ? 877  ASP   A OD1   1 
ATOM   6411  O  OD2   . ASP   A  1  879  ? -44.474 84.283  102.987 1.00 28.18 ? 877  ASP   A OD2   1 
ATOM   6412  N  N     . ARG   A  1  880  ? -42.685 81.187  99.499  1.00 22.01 ? 878  ARG   A N     1 
ATOM   6413  C  CA    . ARG   A  1  880  ? -43.501 80.516  98.499  1.00 20.91 ? 878  ARG   A CA    1 
ATOM   6414  C  C     . ARG   A  1  880  ? -42.640 79.452  97.844  1.00 19.88 ? 878  ARG   A C     1 
ATOM   6415  O  O     . ARG   A  1  880  ? -41.505 79.735  97.441  1.00 19.43 ? 878  ARG   A O     1 
ATOM   6416  C  CB    . ARG   A  1  880  ? -43.975 81.488  97.412  1.00 24.79 ? 878  ARG   A CB    1 
ATOM   6417  C  CG    . ARG   A  1  880  ? -45.023 82.494  97.864  1.00 27.98 ? 878  ARG   A CG    1 
ATOM   6418  C  CD    . ARG   A  1  880  ? -45.436 83.380  96.690  1.00 32.29 ? 878  ARG   A CD    1 
ATOM   6419  N  NE    . ARG   A  1  880  ? -46.318 84.461  97.113  1.00 43.78 ? 878  ARG   A NE    1 
ATOM   6420  C  CZ    . ARG   A  1  880  ? -47.587 84.574  96.744  1.00 44.34 ? 878  ARG   A CZ    1 
ATOM   6421  N  NH1   . ARG   A  1  880  ? -48.145 83.705  95.916  1.00 46.65 ? 878  ARG   A NH1   1 
ATOM   6422  N  NH2   . ARG   A  1  880  ? -48.311 85.587  97.212  1.00 49.20 ? 878  ARG   A NH2   1 
ATOM   6423  N  N     . LEU   A  1  881  ? -43.182 78.234  97.731  1.00 19.15 ? 879  LEU   A N     1 
ATOM   6424  C  CA    . LEU   A  1  881  ? -42.453 77.142  97.095  1.00 19.29 ? 879  LEU   A CA    1 
ATOM   6425  C  C     . LEU   A  1  881  ? -42.036 77.485  95.672  1.00 18.55 ? 879  LEU   A C     1 
ATOM   6426  O  O     . LEU   A  1  881  ? -40.992 77.015  95.201  1.00 19.26 ? 879  LEU   A O     1 
ATOM   6427  C  CB    . LEU   A  1  881  ? -43.309 75.879  97.111  1.00 19.25 ? 879  LEU   A CB    1 
ATOM   6428  C  CG    . LEU   A  1  881  ? -42.676 74.593  96.598  1.00 19.72 ? 879  LEU   A CG    1 
ATOM   6429  C  CD1   . LEU   A  1  881  ? -41.486 74.228  97.491  1.00 21.40 ? 879  LEU   A CD1   1 
ATOM   6430  C  CD2   . LEU   A  1  881  ? -43.729 73.488  96.577  1.00 23.52 ? 879  LEU   A CD2   1 
ATOM   6431  N  N     . SER   A  1  882  ? -42.819 78.311  94.978  1.00 18.62 ? 880  SER   A N     1 
ATOM   6432  C  CA    . SER   A  1  882  ? -42.502 78.629  93.593  1.00 17.99 ? 880  SER   A CA    1 
ATOM   6433  C  C     . SER   A  1  882  ? -41.321 79.575  93.444  1.00 21.73 ? 880  SER   A C     1 
ATOM   6434  O  O     . SER   A  1  882  ? -40.898 79.826  92.311  1.00 21.02 ? 880  SER   A O     1 
ATOM   6435  C  CB    . SER   A  1  882  ? -43.717 79.256  92.920  1.00 19.70 ? 880  SER   A CB    1 
ATOM   6436  O  OG    . SER   A  1  882  ? -44.027 80.472  93.566  1.00 23.59 ? 880  SER   A OG    1 
ATOM   6437  N  N     . VAL   A  1  883  ? -40.774 80.106  94.532  1.00 20.08 ? 881  VAL   A N     1 
ATOM   6438  C  CA    . VAL   A  1  883  ? -39.656 81.033  94.408  1.00 19.26 ? 881  VAL   A CA    1 
ATOM   6439  C  C     . VAL   A  1  883  ? -38.357 80.253  94.278  1.00 20.26 ? 881  VAL   A C     1 
ATOM   6440  O  O     . VAL   A  1  883  ? -38.039 79.395  95.109  1.00 22.86 ? 881  VAL   A O     1 
ATOM   6441  C  CB    . VAL   A  1  883  ? -39.613 82.018  95.585  1.00 20.86 ? 881  VAL   A CB    1 
ATOM   6442  C  CG1   . VAL   A  1  883  ? -38.264 82.750  95.602  1.00 19.74 ? 881  VAL   A CG1   1 
ATOM   6443  C  CG2   . VAL   A  1  883  ? -40.748 82.997  95.455  1.00 21.65 ? 881  VAL   A CG2   1 
ATOM   6444  N  N     . ASP   A  1  884  ? -37.601 80.559  93.233  1.00 18.85 ? 882  ASP   A N     1 
ATOM   6445  C  CA    . ASP   A  1  884  ? -36.316 79.921  93.007  1.00 19.25 ? 882  ASP   A CA    1 
ATOM   6446  C  C     . ASP   A  1  884  ? -35.176 80.682  93.646  1.00 21.40 ? 882  ASP   A C     1 
ATOM   6447  O  O     . ASP   A  1  884  ? -34.244 80.069  94.176  1.00 24.08 ? 882  ASP   A O     1 
ATOM   6448  C  CB    . ASP   A  1  884  ? -36.064 79.847  91.512  1.00 19.42 ? 882  ASP   A CB    1 
ATOM   6449  C  CG    . ASP   A  1  884  ? -37.139 79.076  90.809  1.00 19.62 ? 882  ASP   A CG    1 
ATOM   6450  O  OD1   . ASP   A  1  884  ? -37.352 77.912  91.205  1.00 21.49 ? 882  ASP   A OD1   1 
ATOM   6451  O  OD2   . ASP   A  1  884  ? -37.782 79.650  89.915  1.00 19.56 ? 882  ASP   A OD2   1 
ATOM   6452  N  N     . VAL   A  1  885  ? -35.222 82.004  93.566  1.00 19.44 ? 883  VAL   A N     1 
ATOM   6453  C  CA    . VAL   A  1  885  ? -34.111 82.850  93.967  1.00 20.17 ? 883  VAL   A CA    1 
ATOM   6454  C  C     . VAL   A  1  885  ? -34.654 83.892  94.921  1.00 19.72 ? 883  VAL   A C     1 
ATOM   6455  O  O     . VAL   A  1  885  ? -35.588 84.625  94.577  1.00 19.77 ? 883  VAL   A O     1 
ATOM   6456  C  CB    . VAL   A  1  885  ? -33.456 83.524  92.757  1.00 21.54 ? 883  VAL   A CB    1 
ATOM   6457  C  CG1   . VAL   A  1  885  ? -32.335 84.448  93.212  1.00 21.66 ? 883  VAL   A CG1   1 
ATOM   6458  C  CG2   . VAL   A  1  885  ? -32.923 82.470  91.798  1.00 22.31 ? 883  VAL   A CG2   1 
ATOM   6459  N  N     . GLY   A  1  886  ? -34.082 83.951  96.116  1.00 19.72 ? 884  GLY   A N     1 
ATOM   6460  C  CA    . GLY   A  1  886  ? -34.508 84.905  97.101  1.00 19.31 ? 884  GLY   A CA    1 
ATOM   6461  C  C     . GLY   A  1  886  ? -33.723 86.190  97.056  1.00 19.72 ? 884  GLY   A C     1 
ATOM   6462  O  O     . GLY   A  1  886  ? -33.022 86.503  96.087  1.00 19.31 ? 884  GLY   A O     1 
ATOM   6463  N  N     . PRO   A  1  887  ? -33.829 86.964  98.124  1.00 20.30 ? 885  PRO   A N     1 
ATOM   6464  C  CA    . PRO   A  1  887  ? -33.184 88.275  98.162  1.00 19.76 ? 885  PRO   A CA    1 
ATOM   6465  C  C     . PRO   A  1  887  ? -31.709 88.142  98.503  1.00 19.68 ? 885  PRO   A C     1 
ATOM   6466  O  O     . PRO   A  1  887  ? -31.225 87.105  98.958  1.00 18.95 ? 885  PRO   A O     1 
ATOM   6467  C  CB    . PRO   A  1  887  ? -33.920 88.962  99.313  1.00 19.88 ? 885  PRO   A CB    1 
ATOM   6468  C  CG    . PRO   A  1  887  ? -34.231 87.836  100.254 1.00 21.31 ? 885  PRO   A CG    1 
ATOM   6469  C  CD    . PRO   A  1  887  ? -34.575 86.672  99.361  1.00 21.58 ? 885  PRO   A CD    1 
ATOM   6470  N  N     . VAL   A  1  888  ? -31.001 89.237  98.279  1.00 19.77 ? 886  VAL   A N     1 
ATOM   6471  C  CA    . VAL   A  1  888  ? -29.706 89.397  98.907  1.00 19.59 ? 886  VAL   A CA    1 
ATOM   6472  C  C     . VAL   A  1  888  ? -29.907 89.897  100.334 1.00 20.85 ? 886  VAL   A C     1 
ATOM   6473  O  O     . VAL   A  1  888  ? -30.948 90.449  100.693 1.00 21.66 ? 886  VAL   A O     1 
ATOM   6474  C  CB    . VAL   A  1  888  ? -28.757 90.292  98.088  1.00 21.28 ? 886  VAL   A CB    1 
ATOM   6475  C  CG1   . VAL   A  1  888  ? -28.555 89.690  96.691  1.00 21.61 ? 886  VAL   A CG1   1 
ATOM   6476  C  CG2   . VAL   A  1  888  ? -29.273 91.696  97.983  1.00 25.73 ? 886  VAL   A CG2   1 
ATOM   6477  N  N     . ILE   A  1  889  ? -28.903 89.668  101.176 1.00 20.41 ? 887  ILE   A N     1 
ATOM   6478  C  CA    . ILE   A  1  889  ? -29.153 89.729  102.617 1.00 22.40 ? 887  ILE   A CA    1 
ATOM   6479  C  C     . ILE   A  1  889  ? -29.417 91.148  103.110 1.00 24.98 ? 887  ILE   A C     1 
ATOM   6480  O  O     . ILE   A  1  889  ? -30.201 91.344  104.048 1.00 23.58 ? 887  ILE   A O     1 
ATOM   6481  C  CB    . ILE   A  1  889  ? -28.021 89.026  103.390 1.00 22.94 ? 887  ILE   A CB    1 
ATOM   6482  C  CG1   . ILE   A  1  889  ? -28.375 88.909  104.876 1.00 21.40 ? 887  ILE   A CG1   1 
ATOM   6483  C  CG2   . ILE   A  1  889  ? -26.677 89.741  103.169 1.00 21.90 ? 887  ILE   A CG2   1 
ATOM   6484  C  CD1   . ILE   A  1  889  ? -29.654 88.143  105.145 1.00 22.95 ? 887  ILE   A CD1   1 
ATOM   6485  N  N     . THR   A  1  890  ? -28.789 92.155  102.507 1.00 22.32 ? 888  THR   A N     1 
ATOM   6486  C  CA    . THR   A  1  890  ? -28.905 93.528  102.982 1.00 21.14 ? 888  THR   A CA    1 
ATOM   6487  C  C     . THR   A  1  890  ? -28.853 94.482  101.802 1.00 23.81 ? 888  THR   A C     1 
ATOM   6488  O  O     . THR   A  1  890  ? -28.425 94.125  100.701 1.00 24.16 ? 888  THR   A O     1 
ATOM   6489  C  CB    . THR   A  1  890  ? -27.757 93.927  103.921 1.00 25.06 ? 888  THR   A CB    1 
ATOM   6490  O  OG1   . THR   A  1  890  ? -26.512 93.814  103.221 1.00 26.12 ? 888  THR   A OG1   1 
ATOM   6491  C  CG2   . THR   A  1  890  ? -27.727 93.083  105.191 1.00 25.53 ? 888  THR   A CG2   1 
ATOM   6492  N  N     . SER   A  1  891  ? -29.267 95.723  102.061 1.00 25.14 ? 889  SER   A N     1 
ATOM   6493  C  CA    A SER   A  1  891  ? -29.155 96.774  101.053 0.44 28.10 ? 889  SER   A CA    1 
ATOM   6494  C  CA    B SER   A  1  891  ? -29.157 96.756  101.039 0.56 28.09 ? 889  SER   A CA    1 
ATOM   6495  C  C     . SER   A  1  891  ? -27.704 97.038  100.691 1.00 28.54 ? 889  SER   A C     1 
ATOM   6496  O  O     . SER   A  1  891  ? -27.400 97.382  99.544  1.00 28.32 ? 889  SER   A O     1 
ATOM   6497  C  CB    A SER   A  1  891  ? -29.776 98.071  101.574 0.44 29.40 ? 889  SER   A CB    1 
ATOM   6498  C  CB    B SER   A  1  891  ? -29.841 98.040  101.508 0.56 29.42 ? 889  SER   A CB    1 
ATOM   6499  O  OG    A SER   A  1  891  ? -31.157 97.920  101.835 0.44 28.62 ? 889  SER   A OG    1 
ATOM   6500  O  OG    B SER   A  1  891  ? -29.226 98.530  102.683 0.56 33.00 ? 889  SER   A OG    1 
ATOM   6501  N  N     . GLU   A  1  892  ? -26.798 96.903  101.662 1.00 26.17 ? 890  GLU   A N     1 
ATOM   6502  C  CA    . GLU   A  1  892  ? -25.387 97.136  101.382 1.00 27.82 ? 890  GLU   A CA    1 
ATOM   6503  C  C     . GLU   A  1  892  ? -24.849 96.066  100.454 1.00 27.27 ? 890  GLU   A C     1 
ATOM   6504  O  O     . GLU   A  1  892  ? -24.068 96.361  99.542  1.00 28.43 ? 890  GLU   A O     1 
ATOM   6505  C  CB    . GLU   A  1  892  ? -24.580 97.159  102.679 1.00 31.10 ? 890  GLU   A CB    1 
ATOM   6506  C  CG    . GLU   A  1  892  ? -25.080 98.143  103.727 1.00 36.27 ? 890  GLU   A CG    1 
ATOM   6507  C  CD    . GLU   A  1  892  ? -26.059 97.507  104.702 1.00 41.21 ? 890  GLU   A CD    1 
ATOM   6508  O  OE1   . GLU   A  1  892  ? -27.263 97.424  104.382 1.00 36.33 ? 890  GLU   A OE1   1 
ATOM   6509  O  OE2   . GLU   A  1  892  ? -25.616 97.080  105.791 1.00 52.05 ? 890  GLU   A OE2   1 
ATOM   6510  N  N     . ALA   A  1  893  ? -25.237 94.811  100.688 1.00 26.37 ? 891  ALA   A N     1 
ATOM   6511  C  CA    . ALA   A  1  893  ? -24.843 93.744  99.779  1.00 25.70 ? 891  ALA   A CA    1 
ATOM   6512  C  C     . ALA   A  1  893  ? -25.402 94.003  98.389  1.00 28.01 ? 891  ALA   A C     1 
ATOM   6513  O  O     . ALA   A  1  893  ? -24.686 93.884  97.388  1.00 26.87 ? 891  ALA   A O     1 
ATOM   6514  C  CB    . ALA   A  1  893  ? -25.295 92.391  100.328 1.00 24.42 ? 891  ALA   A CB    1 
ATOM   6515  N  N     . LYS   A  1  894  ? -26.673 94.403  98.313  1.00 24.17 ? 892  LYS   A N     1 
ATOM   6516  C  CA    . LYS   A  1  894  ? -27.270 94.754  97.031  1.00 24.55 ? 892  LYS   A CA    1 
ATOM   6517  C  C     . LYS   A  1  894  ? -26.484 95.858  96.337  1.00 28.33 ? 892  LYS   A C     1 
ATOM   6518  O  O     . LYS   A  1  894  ? -26.169 95.756  95.146  1.00 27.31 ? 892  LYS   A O     1 
ATOM   6519  C  CB    . LYS   A  1  894  ? -28.725 95.175  97.237  1.00 23.01 ? 892  LYS   A CB    1 
ATOM   6520  C  CG    . LYS   A  1  894  ? -29.405 95.734  96.005  1.00 25.03 ? 892  LYS   A CG    1 
ATOM   6521  C  CD    . LYS   A  1  894  ? -30.890 95.912  96.255  1.00 27.19 ? 892  LYS   A CD    1 
ATOM   6522  C  CE    . LYS   A  1  894  ? -31.597 96.557  95.067  1.00 30.06 ? 892  LYS   A CE    1 
ATOM   6523  N  NZ    . LYS   A  1  894  ? -33.057 96.669  95.309  1.00 41.91 ? 892  LYS   A NZ    1 
ATOM   6524  N  N     . ASP   A  1  895  ? -26.151 96.923  97.072  1.00 26.35 ? 893  ASP   A N     1 
ATOM   6525  C  CA    . ASP   A  1  895  ? -25.418 98.036  96.477  1.00 30.24 ? 893  ASP   A CA    1 
ATOM   6526  C  C     . ASP   A  1  895  ? -24.057 97.587  95.970  1.00 28.24 ? 893  ASP   A C     1 
ATOM   6527  O  O     . ASP   A  1  895  ? -23.618 97.999  94.890  1.00 30.65 ? 893  ASP   A O     1 
ATOM   6528  C  CB    . ASP   A  1  895  ? -25.236 99.154  97.505  1.00 29.08 ? 893  ASP   A CB    1 
ATOM   6529  C  CG    . ASP   A  1  895  ? -26.534 99.858  97.849  1.00 34.84 ? 893  ASP   A CG    1 
ATOM   6530  O  OD1   . ASP   A  1  895  ? -27.525 99.706  97.100  1.00 40.84 ? 893  ASP   A OD1   1 
ATOM   6531  O  OD2   . ASP   A  1  895  ? -26.556 100.583 98.868  1.00 39.48 ? 893  ASP   A OD2   1 
ATOM   6532  N  N     . ASN   A  1  896  ? -23.370 96.749  96.744  1.00 27.23 ? 894  ASN   A N     1 
ATOM   6533  C  CA    . ASN   A  1  896  ? -22.058 96.273  96.330  1.00 27.70 ? 894  ASN   A CA    1 
ATOM   6534  C  C     . ASN   A  1  896  ? -22.158 95.430  95.070  1.00 28.46 ? 894  ASN   A C     1 
ATOM   6535  O  O     . ASN   A  1  896  ? -21.336 95.565  94.156  1.00 27.32 ? 894  ASN   A O     1 
ATOM   6536  C  CB    . ASN   A  1  896  ? -21.414 95.470  97.458  1.00 30.19 ? 894  ASN   A CB    1 
ATOM   6537  C  CG    . ASN   A  1  896  ? -20.096 94.848  97.048  1.00 36.55 ? 894  ASN   A CG    1 
ATOM   6538  O  OD1   . ASN   A  1  896  ? -20.046 93.691  96.620  1.00 43.46 ? 894  ASN   A OD1   1 
ATOM   6539  N  ND2   . ASN   A  1  896  ? -19.019 95.613  97.173  1.00 39.35 ? 894  ASN   A ND2   1 
ATOM   6540  N  N     . ILE   A  1  897  ? -23.158 94.550  95.004  1.00 25.89 ? 895  ILE   A N     1 
ATOM   6541  C  CA    . ILE   A  1  897  ? -23.305 93.703  93.827  1.00 25.60 ? 895  ILE   A CA    1 
ATOM   6542  C  C     . ILE   A  1  897  ? -23.668 94.545  92.615  1.00 28.42 ? 895  ILE   A C     1 
ATOM   6543  O  O     . ILE   A  1  897  ? -23.127 94.352  91.520  1.00 25.49 ? 895  ILE   A O     1 
ATOM   6544  C  CB    . ILE   A  1  897  ? -24.352 92.609  94.087  1.00 23.64 ? 895  ILE   A CB    1 
ATOM   6545  C  CG1   . ILE   A  1  897  ? -23.909 91.698  95.229  1.00 22.08 ? 895  ILE   A CG1   1 
ATOM   6546  C  CG2   . ILE   A  1  897  ? -24.594 91.804  92.828  1.00 24.63 ? 895  ILE   A CG2   1 
ATOM   6547  C  CD1   . ILE   A  1  897  ? -25.082 90.986  95.903  1.00 22.94 ? 895  ILE   A CD1   1 
ATOM   6548  N  N     . GLU   A  1  898  ? -24.596 95.487  92.786  1.00 25.92 ? 896  GLU   A N     1 
ATOM   6549  C  CA    . GLU   A  1  898  ? -25.017 96.308  91.660  1.00 29.62 ? 896  GLU   A CA    1 
ATOM   6550  C  C     . GLU   A  1  898  ? -23.890 97.197  91.161  1.00 27.95 ? 896  GLU   A C     1 
ATOM   6551  O  O     . GLU   A  1  898  ? -23.789 97.448  89.955  1.00 30.06 ? 896  GLU   A O     1 
ATOM   6552  C  CB    . GLU   A  1  898  ? -26.253 97.121  92.037  1.00 29.59 ? 896  GLU   A CB    1 
ATOM   6553  C  CG    . GLU   A  1  898  ? -27.479 96.251  92.213  1.00 30.38 ? 896  GLU   A CG    1 
ATOM   6554  C  CD    . GLU   A  1  898  ? -28.718 97.028  92.619  1.00 34.64 ? 896  GLU   A CD    1 
ATOM   6555  O  OE1   . GLU   A  1  898  ? -28.576 98.148  93.151  1.00 41.78 ? 896  GLU   A OE1   1 
ATOM   6556  O  OE2   . GLU   A  1  898  ? -29.832 96.509  92.404  1.00 42.74 ? 896  GLU   A OE2   1 
ATOM   6557  N  N     . LYS   A  1  899  ? -23.039 97.681  92.067  1.00 26.66 ? 897  LYS   A N     1 
ATOM   6558  C  CA    . LYS   A  1  899  ? -21.885 98.461  91.645  1.00 27.91 ? 897  LYS   A CA    1 
ATOM   6559  C  C     . LYS   A  1  899  ? -20.997 97.642  90.722  1.00 30.75 ? 897  LYS   A C     1 
ATOM   6560  O  O     . LYS   A  1  899  ? -20.501 98.149  89.710  1.00 30.59 ? 897  LYS   A O     1 
ATOM   6561  C  CB    . LYS   A  1  899  ? -21.096 98.928  92.869  1.00 30.64 ? 897  LYS   A CB    1 
ATOM   6562  N  N     . HIS   A  1  900  ? -20.801 96.365  91.049  1.00 26.59 ? 898  HIS   A N     1 
ATOM   6563  C  CA    . HIS   A  1  900  ? -20.006 95.499  90.189  1.00 27.50 ? 898  HIS   A CA    1 
ATOM   6564  C  C     . HIS   A  1  900  ? -20.666 95.328  88.827  1.00 26.46 ? 898  HIS   A C     1 
ATOM   6565  O  O     . HIS   A  1  900  ? -20.007 95.432  87.788  1.00 28.52 ? 898  HIS   A O     1 
ATOM   6566  C  CB    . HIS   A  1  900  ? -19.818 94.141  90.854  1.00 26.10 ? 898  HIS   A CB    1 
ATOM   6567  C  CG    . HIS   A  1  900  ? -19.196 93.124  89.953  1.00 25.64 ? 898  HIS   A CG    1 
ATOM   6568  N  ND1   . HIS   A  1  900  ? -17.851 93.120  89.655  1.00 27.47 ? 898  HIS   A ND1   1 
ATOM   6569  C  CD2   . HIS   A  1  900  ? -19.741 92.101  89.253  1.00 27.11 ? 898  HIS   A CD2   1 
ATOM   6570  C  CE1   . HIS   A  1  900  ? -17.590 92.125  88.825  1.00 26.97 ? 898  HIS   A CE1   1 
ATOM   6571  N  NE2   . HIS   A  1  900  ? -18.719 91.491  88.568  1.00 25.29 ? 898  HIS   A NE2   1 
ATOM   6572  N  N     . ILE   A  1  901  ? -21.971 95.057  88.817  1.00 25.01 ? 899  ILE   A N     1 
ATOM   6573  C  CA    . ILE   A  1  901  ? -22.677 94.857  87.556  1.00 26.81 ? 899  ILE   A CA    1 
ATOM   6574  C  C     . ILE   A  1  901  ? -22.559 96.089  86.673  1.00 30.08 ? 899  ILE   A C     1 
ATOM   6575  O  O     . ILE   A  1  901  ? -22.345 95.985  85.458  1.00 31.11 ? 899  ILE   A O     1 
ATOM   6576  C  CB    . ILE   A  1  901  ? -24.144 94.490  87.825  1.00 22.85 ? 899  ILE   A CB    1 
ATOM   6577  C  CG1   . ILE   A  1  901  ? -24.226 93.151  88.562  1.00 25.18 ? 899  ILE   A CG1   1 
ATOM   6578  C  CG2   . ILE   A  1  901  ? -24.927 94.466  86.521  1.00 26.90 ? 899  ILE   A CG2   1 
ATOM   6579  C  CD1   . ILE   A  1  901  ? -25.630 92.828  89.074  1.00 23.80 ? 899  ILE   A CD1   1 
ATOM   6580  N  N     . GLU   A  1  902  ? -22.702 97.277  87.264  1.00 30.18 ? 900  GLU   A N     1 
ATOM   6581  C  CA    . GLU   A  1  902  ? -22.654 98.499  86.469  1.00 32.76 ? 900  GLU   A CA    1 
ATOM   6582  C  C     . GLU   A  1  902  ? -21.243 98.796  85.981  1.00 33.05 ? 900  GLU   A C     1 
ATOM   6583  O  O     . GLU   A  1  902  ? -21.064 99.299  84.865  1.00 38.38 ? 900  GLU   A O     1 
ATOM   6584  C  CB    . GLU   A  1  902  ? -23.236 99.669  87.260  1.00 38.45 ? 900  GLU   A CB    1 
ATOM   6585  C  CG    . GLU   A  1  902  ? -24.729 99.536  87.472  1.00 38.84 ? 900  GLU   A CG    1 
ATOM   6586  C  CD    . GLU   A  1  902  ? -25.458 99.204  86.182  1.00 42.53 ? 900  GLU   A CD    1 
ATOM   6587  O  OE1   . GLU   A  1  902  ? -25.236 99.914  85.176  1.00 45.95 ? 900  GLU   A OE1   1 
ATOM   6588  O  OE2   . GLU   A  1  902  ? -26.239 98.225  86.168  1.00 42.07 ? 900  GLU   A OE2   1 
ATOM   6589  N  N     . ARG   A  1  903  ? -20.232 98.502  86.799  1.00 32.52 ? 901  ARG   A N     1 
ATOM   6590  C  CA    . ARG   A  1  903  ? -18.854 98.603  86.328  1.00 35.13 ? 901  ARG   A CA    1 
ATOM   6591  C  C     . ARG   A  1  903  ? -18.646 97.741  85.089  1.00 39.11 ? 901  ARG   A C     1 
ATOM   6592  O  O     . ARG   A  1  903  ? -18.168 98.224  84.056  1.00 41.12 ? 901  ARG   A O     1 
ATOM   6593  C  CB    . ARG   A  1  903  ? -17.883 98.202  87.439  1.00 36.32 ? 901  ARG   A CB    1 
ATOM   6594  N  N     . MET   A  1  904  ? -19.028 96.463  85.169  1.00 34.70 ? 902  MET   A N     1 
ATOM   6595  C  CA    . MET   A  1  904  ? -18.936 95.579  84.010  1.00 32.07 ? 902  MET   A CA    1 
ATOM   6596  C  C     . MET   A  1  904  ? -19.727 96.134  82.836  1.00 35.65 ? 902  MET   A C     1 
ATOM   6597  O  O     . MET   A  1  904  ? -19.241 96.156  81.699  1.00 35.53 ? 902  MET   A O     1 
ATOM   6598  C  CB    . MET   A  1  904  ? -19.461 94.190  84.376  1.00 30.13 ? 902  MET   A CB    1 
ATOM   6599  C  CG    . MET   A  1  904  ? -18.674 93.497  85.452  1.00 28.86 ? 902  MET   A CG    1 
ATOM   6600  S  SD    . MET   A  1  904  ? -17.008 93.133  84.887  1.00 38.98 ? 902  MET   A SD    1 
ATOM   6601  C  CE    . MET   A  1  904  ? -16.051 94.337  85.804  1.00 39.32 ? 902  MET   A CE    1 
ATOM   6602  N  N     . ARG   A  1  905  ? -20.960 96.573  83.091  1.00 33.54 ? 903  ARG   A N     1 
ATOM   6603  C  CA    . ARG   A  1  905  ? -21.779 97.128  82.021  1.00 35.42 ? 903  ARG   A CA    1 
ATOM   6604  C  C     . ARG   A  1  905  ? -21.116 98.357  81.420  1.00 42.04 ? 903  ARG   A C     1 
ATOM   6605  O  O     . ARG   A  1  905  ? -21.180 98.573  80.205  1.00 40.22 ? 903  ARG   A O     1 
ATOM   6606  C  CB    . ARG   A  1  905  ? -23.168 97.470  82.552  1.00 36.53 ? 903  ARG   A CB    1 
ATOM   6607  C  CG    . ARG   A  1  905  ? -24.232 97.563  81.478  1.00 40.67 ? 903  ARG   A CG    1 
ATOM   6608  C  CD    . ARG   A  1  905  ? -25.508 98.176  82.017  1.00 40.70 ? 903  ARG   A CD    1 
ATOM   6609  N  NE    . ARG   A  1  905  ? -26.098 97.403  83.105  1.00 38.63 ? 903  ARG   A NE    1 
ATOM   6610  C  CZ    . ARG   A  1  905  ? -26.969 96.418  82.937  1.00 38.87 ? 903  ARG   A CZ    1 
ATOM   6611  N  NH1   . ARG   A  1  905  ? -27.315 95.998  81.729  1.00 39.38 ? 903  ARG   A NH1   1 
ATOM   6612  N  NH2   . ARG   A  1  905  ? -27.512 95.842  84.007  1.00 39.32 ? 903  ARG   A NH2   1 
ATOM   6613  N  N     . GLY   A  1  906  ? -20.457 99.163  82.256  1.00 38.82 ? 904  GLY   A N     1 
ATOM   6614  C  CA    . GLY   A  1  906  ? -19.776 100.343 81.756  1.00 42.66 ? 904  GLY   A CA    1 
ATOM   6615  C  C     . GLY   A  1  906  ? -18.559 100.019 80.914  1.00 46.81 ? 904  GLY   A C     1 
ATOM   6616  O  O     . GLY   A  1  906  ? -18.178 100.805 80.041  1.00 48.68 ? 904  GLY   A O     1 
ATOM   6617  N  N     . LEU   A  1  907  ? -17.934 98.870  81.157  1.00 41.23 ? 905  LEU   A N     1 
ATOM   6618  C  CA    . LEU   A  1  907  ? -16.804 98.426  80.352  1.00 42.01 ? 905  LEU   A CA    1 
ATOM   6619  C  C     . LEU   A  1  907  ? -17.221 97.877  78.994  1.00 41.15 ? 905  LEU   A C     1 
ATOM   6620  O  O     . LEU   A  1  907  ? -16.348 97.525  78.194  1.00 45.59 ? 905  LEU   A O     1 
ATOM   6621  C  CB    . LEU   A  1  907  ? -15.993 97.373  81.108  1.00 41.00 ? 905  LEU   A CB    1 
ATOM   6622  C  CG    . LEU   A  1  907  ? -15.327 97.842  82.401  1.00 44.58 ? 905  LEU   A CG    1 
ATOM   6623  C  CD1   . LEU   A  1  907  ? -14.459 96.740  82.985  1.00 44.44 ? 905  LEU   A CD1   1 
ATOM   6624  C  CD2   . LEU   A  1  907  ? -14.512 99.102  82.151  1.00 49.57 ? 905  LEU   A CD2   1 
ATOM   6625  N  N     . GLY   A  1  908  ? -18.518 97.791  78.719  1.00 38.80 ? 906  GLY   A N     1 
ATOM   6626  C  CA    . GLY   A  1  908  ? -19.002 97.248  77.470  1.00 40.36 ? 906  GLY   A CA    1 
ATOM   6627  C  C     . GLY   A  1  908  ? -19.301 95.766  77.481  1.00 35.40 ? 906  GLY   A C     1 
ATOM   6628  O  O     . GLY   A  1  908  ? -19.601 95.207  76.421  1.00 36.81 ? 906  GLY   A O     1 
ATOM   6629  N  N     . ARG   A  1  909  ? -19.236 95.113  78.638  1.00 33.50 ? 907  ARG   A N     1 
ATOM   6630  C  CA    . ARG   A  1  909  ? -19.517 93.687  78.704  1.00 28.11 ? 907  ARG   A CA    1 
ATOM   6631  C  C     . ARG   A  1  909  ? -21.015 93.446  78.564  1.00 32.10 ? 907  ARG   A C     1 
ATOM   6632  O  O     . ARG   A  1  909  ? -21.834 94.226  79.058  1.00 33.18 ? 907  ARG   A O     1 
ATOM   6633  C  CB    . ARG   A  1  909  ? -19.021 93.129  80.037  1.00 28.20 ? 907  ARG   A CB    1 
ATOM   6634  C  CG    . ARG   A  1  909  ? -17.577 93.487  80.366  1.00 32.88 ? 907  ARG   A CG    1 
ATOM   6635  C  CD    . ARG   A  1  909  ? -16.595 92.806  79.421  1.00 35.29 ? 907  ARG   A CD    1 
ATOM   6636  N  NE    . ARG   A  1  909  ? -15.216 92.944  79.879  1.00 37.68 ? 907  ARG   A NE    1 
ATOM   6637  C  CZ    . ARG   A  1  909  ? -14.339 93.809  79.384  1.00 45.51 ? 907  ARG   A CZ    1 
ATOM   6638  N  NH1   . ARG   A  1  909  ? -14.660 94.636  78.401  1.00 45.10 ? 907  ARG   A NH1   1 
ATOM   6639  N  NH2   . ARG   A  1  909  ? -13.107 93.844  79.886  1.00 41.52 ? 907  ARG   A NH2   1 
ATOM   6640  N  N     . LYS   A  1  910  ? -21.372 92.365  77.873  1.00 26.10 ? 908  LYS   A N     1 
ATOM   6641  C  CA    . LYS   A  1  910  ? -22.776 92.016  77.709  1.00 27.24 ? 908  LYS   A CA    1 
ATOM   6642  C  C     . LYS   A  1  910  ? -23.350 91.513  79.027  1.00 27.34 ? 908  LYS   A C     1 
ATOM   6643  O  O     . LYS   A  1  910  ? -22.806 90.589  79.642  1.00 25.33 ? 908  LYS   A O     1 
ATOM   6644  C  CB    . LYS   A  1  910  ? -22.937 90.939  76.641  1.00 29.25 ? 908  LYS   A CB    1 
ATOM   6645  C  CG    . LYS   A  1  910  ? -22.815 91.446  75.226  1.00 36.20 ? 908  LYS   A CG    1 
ATOM   6646  C  CD    . LYS   A  1  910  ? -23.149 90.345  74.233  1.00 37.25 ? 908  LYS   A CD    1 
ATOM   6647  C  CE    . LYS   A  1  910  ? -24.529 89.768  74.485  1.00 39.03 ? 908  LYS   A CE    1 
ATOM   6648  N  NZ    . LYS   A  1  910  ? -24.973 88.924  73.338  1.00 47.09 ? 908  LYS   A NZ    1 
ATOM   6649  N  N     . VAL   A  1  911  ? -24.472 92.101  79.437  1.00 26.44 ? 909  VAL   A N     1 
ATOM   6650  C  CA    . VAL   A  1  911  ? -25.112 91.816  80.715  1.00 25.63 ? 909  VAL   A CA    1 
ATOM   6651  C  C     . VAL   A  1  911  ? -26.540 91.371  80.438  1.00 24.81 ? 909  VAL   A C     1 
ATOM   6652  O  O     . VAL   A  1  911  ? -27.309 92.100  79.798  1.00 27.02 ? 909  VAL   A O     1 
ATOM   6653  C  CB    . VAL   A  1  911  ? -25.093 93.045  81.637  1.00 26.68 ? 909  VAL   A CB    1 
ATOM   6654  C  CG1   . VAL   A  1  911  ? -25.781 92.739  82.966  1.00 29.38 ? 909  VAL   A CG1   1 
ATOM   6655  C  CG2   . VAL   A  1  911  ? -23.660 93.530  81.856  1.00 27.71 ? 909  VAL   A CG2   1 
ATOM   6656  N  N     . GLU   A  1  912  ? -26.886 90.173  80.902  1.00 23.13 ? 910  GLU   A N     1 
ATOM   6657  C  CA    . GLU   A  1  912  ? -28.233 89.629  80.810  1.00 23.97 ? 910  GLU   A CA    1 
ATOM   6658  C  C     . GLU   A  1  912  ? -28.807 89.588  82.218  1.00 25.88 ? 910  GLU   A C     1 
ATOM   6659  O  O     . GLU   A  1  912  ? -28.165 89.060  83.131  1.00 22.85 ? 910  GLU   A O     1 
ATOM   6660  C  CB    . GLU   A  1  912  ? -28.187 88.207  80.248  1.00 24.77 ? 910  GLU   A CB    1 
ATOM   6661  C  CG    . GLU   A  1  912  ? -29.548 87.604  79.971  1.00 24.34 ? 910  GLU   A CG    1 
ATOM   6662  C  CD    . GLU   A  1  912  ? -30.151 88.134  78.685  1.00 28.45 ? 910  GLU   A CD    1 
ATOM   6663  O  OE1   . GLU   A  1  912  ? -29.413 88.758  77.896  1.00 28.75 ? 910  GLU   A OE1   1 
ATOM   6664  O  OE2   . GLU   A  1  912  ? -31.362 87.934  78.463  1.00 29.75 ? 910  GLU   A OE2   1 
ATOM   6665  N  N     . GLN   A  1  913  ? -29.995 90.158  82.402  1.00 24.38 ? 911  GLN   A N     1 
ATOM   6666  C  CA    . GLN   A  1  913  ? -30.620 90.175  83.715  1.00 25.83 ? 911  GLN   A CA    1 
ATOM   6667  C  C     . GLN   A  1  913  ? -32.090 89.824  83.602  1.00 29.27 ? 911  GLN   A C     1 
ATOM   6668  O  O     . GLN   A  1  913  ? -32.774 90.256  82.670  1.00 28.31 ? 911  GLN   A O     1 
ATOM   6669  C  CB    . GLN   A  1  913  ? -30.493 91.548  84.382  1.00 26.14 ? 911  GLN   A CB    1 
ATOM   6670  C  CG    . GLN   A  1  913  ? -29.071 91.949  84.686  1.00 28.65 ? 911  GLN   A CG    1 
ATOM   6671  C  CD    . GLN   A  1  913  ? -29.007 93.153  85.589  1.00 29.90 ? 911  GLN   A CD    1 
ATOM   6672  O  OE1   . GLN   A  1  913  ? -29.440 94.246  85.216  1.00 31.12 ? 911  GLN   A OE1   1 
ATOM   6673  N  NE2   . GLN   A  1  913  ? -28.485 92.962  86.792  1.00 27.52 ? 911  GLN   A NE2   1 
ATOM   6674  N  N     . ILE   A  1  914  ? -32.568 89.033  84.562  1.00 26.50 ? 912  ILE   A N     1 
ATOM   6675  C  CA    . ILE   A  1  914  ? -33.996 88.781  84.673  1.00 24.96 ? 912  ILE   A CA    1 
ATOM   6676  C  C     . ILE   A  1  914  ? -34.691 90.053  85.141  1.00 27.60 ? 912  ILE   A C     1 
ATOM   6677  O  O     . ILE   A  1  914  ? -34.130 90.863  85.892  1.00 27.74 ? 912  ILE   A O     1 
ATOM   6678  C  CB    . ILE   A  1  914  ? -34.250 87.611  85.643  1.00 32.35 ? 912  ILE   A CB    1 
ATOM   6679  N  N     . GLY   A  1  915  ? -35.918 90.254  84.672  1.00 29.31 ? 913  GLY   A N     1 
ATOM   6680  C  CA    . GLY   A  1  915  ? -36.710 91.362  85.168  1.00 29.72 ? 913  GLY   A CA    1 
ATOM   6681  C  C     . GLY   A  1  915  ? -37.365 90.966  86.479  1.00 28.55 ? 913  GLY   A C     1 
ATOM   6682  O  O     . GLY   A  1  915  ? -37.894 89.865  86.625  1.00 34.16 ? 913  GLY   A O     1 
ATOM   6683  N  N     . LEU   A  1  916  ? -37.299 91.870  87.448  1.00 28.22 ? 914  LEU   A N     1 
ATOM   6684  C  CA    . LEU   A  1  916  ? -37.831 91.601  88.774  1.00 31.20 ? 914  LEU   A CA    1 
ATOM   6685  C  C     . LEU   A  1  916  ? -39.269 92.085  88.877  1.00 33.23 ? 914  LEU   A C     1 
ATOM   6686  O  O     . LEU   A  1  916  ? -39.635 93.118  88.309  1.00 33.72 ? 914  LEU   A O     1 
ATOM   6687  C  CB    . LEU   A  1  916  ? -36.993 92.304  89.837  1.00 30.26 ? 914  LEU   A CB    1 
ATOM   6688  C  CG    . LEU   A  1  916  ? -35.542 91.841  89.940  1.00 31.21 ? 914  LEU   A CG    1 
ATOM   6689  C  CD1   . LEU   A  1  916  ? -34.853 92.543  91.096  1.00 34.30 ? 914  LEU   A CD1   1 
ATOM   6690  C  CD2   . LEU   A  1  916  ? -35.494 90.336  90.106  1.00 34.58 ? 914  LEU   A CD2   1 
ATOM   6691  N  N     . ALA   A  1  917  ? -40.077 91.333  89.619  1.00 28.07 ? 915  ALA   A N     1 
ATOM   6692  C  CA    . ALA   A  1  917  ? -41.449 91.736  89.875  1.00 29.31 ? 915  ALA   A CA    1 
ATOM   6693  C  C     . ALA   A  1  917  ? -41.475 92.955  90.788  1.00 32.13 ? 915  ALA   A C     1 
ATOM   6694  O  O     . ALA   A  1  917  ? -40.545 93.202  91.561  1.00 32.12 ? 915  ALA   A O     1 
ATOM   6695  C  CB    . ALA   A  1  917  ? -42.209 90.591  90.540  1.00 32.18 ? 915  ALA   A CB    1 
ATOM   6696  N  N     . SER   A  1  918  ? -42.563 93.723  90.696  1.00 32.08 ? 916  SER   A N     1 
ATOM   6697  C  CA    . SER   A  1  918  ? -42.707 94.901  91.546  1.00 34.57 ? 916  SER   A CA    1 
ATOM   6698  C  C     . SER   A  1  918  ? -42.673 94.537  93.024  1.00 30.62 ? 916  SER   A C     1 
ATOM   6699  O  O     . SER   A  1  918  ? -42.238 95.349  93.847  1.00 31.41 ? 916  SER   A O     1 
ATOM   6700  C  CB    . SER   A  1  918  ? -44.018 95.613  91.218  1.00 33.88 ? 916  SER   A CB    1 
ATOM   6701  O  OG    . SER   A  1  918  ? -45.097 94.698  91.296  1.00 41.08 ? 916  SER   A OG    1 
ATOM   6702  N  N     . GLU   A  1  919  ? -43.118 93.324  93.371  1.00 32.58 ? 917  GLU   A N     1 
ATOM   6703  C  CA    . GLU   A  1  919  ? -43.154 92.879  94.760  1.00 32.13 ? 917  GLU   A CA    1 
ATOM   6704  C  C     . GLU   A  1  919  ? -41.773 92.836  95.398  1.00 32.81 ? 917  GLU   A C     1 
ATOM   6705  O  O     . GLU   A  1  919  ? -41.670 92.843  96.630  1.00 30.46 ? 917  GLU   A O     1 
ATOM   6706  C  CB    . GLU   A  1  919  ? -43.785 91.486  94.849  1.00 34.01 ? 917  GLU   A CB    1 
ATOM   6707  C  CG    . GLU   A  1  919  ? -45.299 91.463  94.706  1.00 37.31 ? 917  GLU   A CG    1 
ATOM   6708  C  CD    . GLU   A  1  919  ? -45.768 91.507  93.262  1.00 43.87 ? 917  GLU   A CD    1 
ATOM   6709  O  OE1   . GLU   A  1  919  ? -44.925 91.667  92.353  1.00 40.24 ? 917  GLU   A OE1   1 
ATOM   6710  O  OE2   . GLU   A  1  919  ? -46.989 91.376  93.036  1.00 48.08 ? 917  GLU   A OE2   1 
ATOM   6711  N  N     . THR   A  1  920  ? -40.711 92.787  94.599  1.00 28.81 ? 918  THR   A N     1 
ATOM   6712  C  CA    . THR   A  1  920  ? -39.375 92.774  95.178  1.00 26.04 ? 918  THR   A CA    1 
ATOM   6713  C  C     . THR   A  1  920  ? -38.992 94.111  95.797  1.00 27.91 ? 918  THR   A C     1 
ATOM   6714  O  O     . THR   A  1  920  ? -38.026 94.159  96.567  1.00 26.83 ? 918  THR   A O     1 
ATOM   6715  C  CB    . THR   A  1  920  ? -38.343 92.368  94.124  1.00 27.56 ? 918  THR   A CB    1 
ATOM   6716  O  OG1   . THR   A  1  920  ? -38.331 93.330  93.064  1.00 27.60 ? 918  THR   A OG1   1 
ATOM   6717  C  CG2   . THR   A  1  920  ? -38.672 90.992  93.561  1.00 26.27 ? 918  THR   A CG2   1 
ATOM   6718  N  N     . GLY   A  1  921  ? -39.732 95.183  95.500  1.00 30.67 ? 919  GLY   A N     1 
ATOM   6719  C  CA    . GLY   A  1  921  ? -39.365 96.498  95.997  1.00 29.19 ? 919  GLY   A CA    1 
ATOM   6720  C  C     . GLY   A  1  921  ? -39.323 96.599  97.510  1.00 28.11 ? 919  GLY   A C     1 
ATOM   6721  O  O     . GLY   A  1  921  ? -38.596 97.431  98.057  1.00 32.46 ? 919  GLY   A O     1 
ATOM   6722  N  N     . VAL   A  1  922  ? -40.093 95.758  98.208  1.00 27.50 ? 920  VAL   A N     1 
ATOM   6723  C  CA    . VAL   A  1  922  ? -40.121 95.812  99.670  1.00 26.06 ? 920  VAL   A CA    1 
ATOM   6724  C  C     . VAL   A  1  922  ? -38.943 95.100  100.313 1.00 28.07 ? 920  VAL   A C     1 
ATOM   6725  O  O     . VAL   A  1  922  ? -38.762 95.202  101.533 1.00 28.92 ? 920  VAL   A O     1 
ATOM   6726  C  CB    . VAL   A  1  922  ? -41.436 95.253  100.243 1.00 27.87 ? 920  VAL   A CB    1 
ATOM   6727  C  CG1   . VAL   A  1  922  ? -42.598 96.169  99.890  1.00 28.39 ? 920  VAL   A CG1   1 
ATOM   6728  C  CG2   . VAL   A  1  922  ? -41.679 93.851  99.716  1.00 28.87 ? 920  VAL   A CG2   1 
ATOM   6729  N  N     . GLY   A  1  923  ? -38.143 94.375  99.534  1.00 25.17 ? 921  GLY   A N     1 
ATOM   6730  C  CA    . GLY   A  1  923  ? -36.945 93.749  100.056 1.00 25.67 ? 921  GLY   A CA    1 
ATOM   6731  C  C     . GLY   A  1  923  ? -35.708 94.185  99.298  1.00 23.81 ? 921  GLY   A C     1 
ATOM   6732  O  O     . GLY   A  1  923  ? -35.736 95.183  98.574  1.00 27.39 ? 921  GLY   A O     1 
ATOM   6733  N  N     . THR   A  1  924  ? -34.613 93.453  99.454  1.00 23.27 ? 922  THR   A N     1 
ATOM   6734  C  CA    . THR   A  1  924  ? -33.355 93.779  98.785  1.00 23.59 ? 922  THR   A CA    1 
ATOM   6735  C  C     . THR   A  1  924  ? -33.004 92.651  97.822  1.00 24.34 ? 922  THR   A C     1 
ATOM   6736  O  O     . THR   A  1  924  ? -32.439 91.631  98.223  1.00 23.35 ? 922  THR   A O     1 
ATOM   6737  C  CB    . THR   A  1  924  ? -32.251 94.029  99.802  1.00 23.12 ? 922  THR   A CB    1 
ATOM   6738  O  OG1   . THR   A  1  924  ? -32.171 92.930  100.720 1.00 21.84 ? 922  THR   A OG1   1 
ATOM   6739  C  CG2   . THR   A  1  924  ? -32.553 95.297  100.577 1.00 26.20 ? 922  THR   A CG2   1 
ATOM   6740  N  N     . PHE   A  1  925  ? -33.327 92.843  96.548  1.00 21.76 ? 923  PHE   A N     1 
ATOM   6741  C  CA    . PHE   A  1  925  ? -33.139 91.819  95.539  1.00 20.58 ? 923  PHE   A CA    1 
ATOM   6742  C  C     . PHE   A  1  925  ? -32.177 92.304  94.470  1.00 23.07 ? 923  PHE   A C     1 
ATOM   6743  O  O     . PHE   A  1  925  ? -32.147 93.488  94.111  1.00 24.28 ? 923  PHE   A O     1 
ATOM   6744  C  CB    . PHE   A  1  925  ? -34.468 91.440  94.875  1.00 21.50 ? 923  PHE   A CB    1 
ATOM   6745  C  CG    . PHE   A  1  925  ? -35.413 90.714  95.771  1.00 23.14 ? 923  PHE   A CG    1 
ATOM   6746  C  CD1   . PHE   A  1  925  ? -36.258 91.410  96.620  1.00 22.82 ? 923  PHE   A CD1   1 
ATOM   6747  C  CD2   . PHE   A  1  925  ? -35.463 89.333  95.762  1.00 19.28 ? 923  PHE   A CD2   1 
ATOM   6748  C  CE1   . PHE   A  1  925  ? -37.145 90.739  97.443  1.00 22.90 ? 923  PHE   A CE1   1 
ATOM   6749  C  CE2   . PHE   A  1  925  ? -36.352 88.654  96.591  1.00 21.09 ? 923  PHE   A CE2   1 
ATOM   6750  C  CZ    . PHE   A  1  925  ? -37.192 89.360  97.427  1.00 20.84 ? 923  PHE   A CZ    1 
ATOM   6751  N  N     . VAL   A  1  926  ? -31.393 91.364  93.959  1.00 22.19 ? 924  VAL   A N     1 
ATOM   6752  C  CA    . VAL   A  1  926  ? -30.577 91.564  92.774  1.00 22.30 ? 924  VAL   A CA    1 
ATOM   6753  C  C     . VAL   A  1  926  ? -30.998 90.487  91.782  1.00 21.93 ? 924  VAL   A C     1 
ATOM   6754  O  O     . VAL   A  1  926  ? -31.031 89.306  92.141  1.00 20.56 ? 924  VAL   A O     1 
ATOM   6755  C  CB    . VAL   A  1  926  ? -29.072 91.455  93.077  1.00 23.07 ? 924  VAL   A CB    1 
ATOM   6756  C  CG1   . VAL   A  1  926  ? -28.271 91.549  91.792  1.00 23.56 ? 924  VAL   A CG1   1 
ATOM   6757  C  CG2   . VAL   A  1  926  ? -28.659 92.548  94.045  1.00 24.36 ? 924  VAL   A CG2   1 
ATOM   6758  N  N     . PRO   A  1  927  ? -31.345 90.834  90.551  1.00 22.28 ? 925  PRO   A N     1 
ATOM   6759  C  CA    . PRO   A  1  927  ? -31.752 89.812  89.600  1.00 22.95 ? 925  PRO   A CA    1 
ATOM   6760  C  C     . PRO   A  1  927  ? -30.568 88.948  89.218  1.00 22.36 ? 925  PRO   A C     1 
ATOM   6761  O  O     . PRO   A  1  927  ? -29.447 89.455  89.076  1.00 21.82 ? 925  PRO   A O     1 
ATOM   6762  C  CB    . PRO   A  1  927  ? -32.246 90.629  88.400  1.00 26.81 ? 925  PRO   A CB    1 
ATOM   6763  C  CG    . PRO   A  1  927  ? -31.509 91.916  88.494  1.00 26.87 ? 925  PRO   A CG    1 
ATOM   6764  C  CD    . PRO   A  1  927  ? -31.342 92.185  89.964  1.00 24.70 ? 925  PRO   A CD    1 
ATOM   6765  N  N     . PRO   A  1  928  ? -30.769 87.638  89.100  1.00 22.32 ? 926  PRO   A N     1 
ATOM   6766  C  CA    . PRO   A  1  928  ? -29.752 86.782  88.488  1.00 19.53 ? 926  PRO   A CA    1 
ATOM   6767  C  C     . PRO   A  1  928  ? -29.240 87.417  87.209  1.00 19.26 ? 926  PRO   A C     1 
ATOM   6768  O  O     . PRO   A  1  928  ? -30.011 87.895  86.373  1.00 20.52 ? 926  PRO   A O     1 
ATOM   6769  C  CB    . PRO   A  1  928  ? -30.521 85.486  88.220  1.00 21.43 ? 926  PRO   A CB    1 
ATOM   6770  C  CG    . PRO   A  1  928  ? -31.457 85.428  89.370  1.00 22.20 ? 926  PRO   A CG    1 
ATOM   6771  C  CD    . PRO   A  1  928  ? -31.919 86.854  89.574  1.00 23.55 ? 926  PRO   A CD    1 
ATOM   6772  N  N     . THR   A  1  929  ? -27.925 87.454  87.086  1.00 19.99 ? 927  THR   A N     1 
ATOM   6773  C  CA    . THR   A  1  929  ? -27.241 88.244  86.082  1.00 22.39 ? 927  THR   A CA    1 
ATOM   6774  C  C     . THR   A  1  929  ? -26.159 87.391  85.446  1.00 21.88 ? 927  THR   A C     1 
ATOM   6775  O  O     . THR   A  1  929  ? -25.463 86.651  86.139  1.00 20.80 ? 927  THR   A O     1 
ATOM   6776  C  CB    . THR   A  1  929  ? -26.600 89.456  86.758  1.00 24.55 ? 927  THR   A CB    1 
ATOM   6777  O  OG1   . THR   A  1  929  ? -27.632 90.267  87.334  1.00 23.06 ? 927  THR   A OG1   1 
ATOM   6778  C  CG2   . THR   A  1  929  ? -25.801 90.282  85.761  1.00 22.86 ? 927  THR   A CG2   1 
ATOM   6779  N  N     . ILE   A  1  930  ? -26.049 87.468  84.124  1.00 20.74 ? 928  ILE   A N     1 
ATOM   6780  C  CA    . ILE   A  1  930  ? -24.976 86.820  83.381  1.00 22.42 ? 928  ILE   A CA    1 
ATOM   6781  C  C     . ILE   A  1  930  ? -24.164 87.919  82.721  1.00 22.29 ? 928  ILE   A C     1 
ATOM   6782  O  O     . ILE   A  1  930  ? -24.725 88.765  82.012  1.00 24.10 ? 928  ILE   A O     1 
ATOM   6783  C  CB    . ILE   A  1  930  ? -25.525 85.850  82.319  1.00 19.81 ? 928  ILE   A CB    1 
ATOM   6784  C  CG1   . ILE   A  1  930  ? -26.290 84.699  82.973  1.00 22.51 ? 928  ILE   A CG1   1 
ATOM   6785  C  CG2   . ILE   A  1  930  ? -24.390 85.329  81.434  1.00 24.22 ? 928  ILE   A CG2   1 
ATOM   6786  C  CD1   . ILE   A  1  930  ? -27.119 83.874  81.975  1.00 23.45 ? 928  ILE   A CD1   1 
ATOM   6787  N  N     . ILE   A  1  931  ? -22.857 87.911  82.959  1.00 23.25 ? 929  ILE   A N     1 
ATOM   6788  C  CA    . ILE   A  1  931  ? -21.938 88.905  82.420  1.00 21.31 ? 929  ILE   A CA    1 
ATOM   6789  C  C     . ILE   A  1  931  ? -20.909 88.176  81.573  1.00 23.60 ? 929  ILE   A C     1 
ATOM   6790  O  O     . ILE   A  1  931  ? -20.213 87.282  82.064  1.00 22.70 ? 929  ILE   A O     1 
ATOM   6791  C  CB    . ILE   A  1  931  ? -21.246 89.694  83.539  1.00 25.38 ? 929  ILE   A CB    1 
ATOM   6792  C  CG1   . ILE   A  1  931  ? -22.282 90.423  84.400  1.00 23.87 ? 929  ILE   A CG1   1 
ATOM   6793  C  CG2   . ILE   A  1  931  ? -20.241 90.673  82.953  1.00 25.93 ? 929  ILE   A CG2   1 
ATOM   6794  C  CD1   . ILE   A  1  931  ? -21.665 91.301  85.472  1.00 25.79 ? 929  ILE   A CD1   1 
ATOM   6795  N  N     . GLU   A  1  932  ? -20.800 88.554  80.308  1.00 25.30 ? 930  GLU   A N     1 
ATOM   6796  C  CA    . GLU   A  1  932  ? -19.831 87.925  79.423  1.00 23.76 ? 930  GLU   A CA    1 
ATOM   6797  C  C     . GLU   A  1  932  ? -18.518 88.693  79.486  1.00 23.13 ? 930  GLU   A C     1 
ATOM   6798  O  O     . GLU   A  1  932  ? -18.464 89.883  79.158  1.00 25.38 ? 930  GLU   A O     1 
ATOM   6799  C  CB    . GLU   A  1  932  ? -20.392 87.851  78.007  1.00 24.83 ? 930  GLU   A CB    1 
ATOM   6800  C  CG    . GLU   A  1  932  ? -21.584 86.906  77.921  1.00 24.42 ? 930  GLU   A CG    1 
ATOM   6801  C  CD    . GLU   A  1  932  ? -22.339 87.048  76.631  1.00 30.41 ? 930  GLU   A CD    1 
ATOM   6802  O  OE1   . GLU   A  1  932  ? -21.693 86.968  75.566  1.00 29.37 ? 930  GLU   A OE1   1 
ATOM   6803  O  OE2   . GLU   A  1  932  ? -23.576 87.245  76.680  1.00 28.43 ? 930  GLU   A OE2   1 
ATOM   6804  N  N     . LEU   A  1  933  ? -17.473 88.025  79.945  1.00 25.76 ? 931  LEU   A N     1 
ATOM   6805  C  CA    . LEU   A  1  933  ? -16.171 88.646  80.105  1.00 24.93 ? 931  LEU   A CA    1 
ATOM   6806  C  C     . LEU   A  1  933  ? -15.269 88.310  78.928  1.00 31.86 ? 931  LEU   A C     1 
ATOM   6807  O  O     . LEU   A  1  933  ? -15.466 87.315  78.226  1.00 28.61 ? 931  LEU   A O     1 
ATOM   6808  C  CB    . LEU   A  1  933  ? -15.498 88.180  81.399  1.00 29.17 ? 931  LEU   A CB    1 
ATOM   6809  C  CG    . LEU   A  1  933  ? -16.217 88.504  82.710  1.00 29.29 ? 931  LEU   A CG    1 
ATOM   6810  C  CD1   . LEU   A  1  933  ? -15.350 88.091  83.877  1.00 33.25 ? 931  LEU   A CD1   1 
ATOM   6811  C  CD2   . LEU   A  1  933  ? -16.558 89.981  82.788  1.00 31.77 ? 931  LEU   A CD2   1 
ATOM   6812  N  N     . GLU   A  1  934  ? -14.264 89.164  78.727  1.00 32.06 ? 932  GLU   A N     1 
ATOM   6813  C  CA    . GLU   A  1  934  ? -13.214 88.918  77.748  1.00 38.86 ? 932  GLU   A CA    1 
ATOM   6814  C  C     . GLU   A  1  934  ? -12.095 88.067  78.337  1.00 40.08 ? 932  GLU   A C     1 
ATOM   6815  O  O     . GLU   A  1  934  ? -11.650 87.101  77.711  1.00 44.71 ? 932  GLU   A O     1 
ATOM   6816  C  CB    . GLU   A  1  934  ? -12.664 90.247  77.218  1.00 41.27 ? 932  GLU   A CB    1 
ATOM   6817  N  N     . LYS   A  1  935  ? -11.651 88.400  79.546  1.00 39.94 ? 933  LYS   A N     1 
ATOM   6818  C  CA    . LYS   A  1  935  ? -10.592 87.672  80.227  1.00 41.28 ? 933  LYS   A CA    1 
ATOM   6819  C  C     . LYS   A  1  935  ? -11.001 87.432  81.672  1.00 41.72 ? 933  LYS   A C     1 
ATOM   6820  O  O     . LYS   A  1  935  ? -11.776 88.199  82.248  1.00 41.04 ? 933  LYS   A O     1 
ATOM   6821  C  CB    . LYS   A  1  935  ? -9.277  88.461  80.213  1.00 42.49 ? 933  LYS   A CB    1 
ATOM   6822  N  N     . LEU   A  1  936  ? -10.466 86.355  82.255  1.00 39.94 ? 934  LEU   A N     1 
ATOM   6823  C  CA    . LEU   A  1  936  ? -10.712 86.082  83.668  1.00 39.58 ? 934  LEU   A CA    1 
ATOM   6824  C  C     . LEU   A  1  936  ? -10.160 87.192  84.549  1.00 43.06 ? 934  LEU   A C     1 
ATOM   6825  O  O     . LEU   A  1  936  ? -10.650 87.403  85.664  1.00 43.45 ? 934  LEU   A O     1 
ATOM   6826  C  CB    . LEU   A  1  936  ? -10.111 84.735  84.070  1.00 39.15 ? 934  LEU   A CB    1 
ATOM   6827  N  N     . SER   A  1  937  ? -9.153  87.919  84.061  1.00 46.23 ? 935  SER   A N     1 
ATOM   6828  C  CA    . SER   A  1  937  ? -8.590  89.040  84.800  1.00 42.22 ? 935  SER   A CA    1 
ATOM   6829  C  C     . SER   A  1  937  ? -9.553  90.215  84.919  1.00 41.85 ? 935  SER   A C     1 
ATOM   6830  O  O     . SER   A  1  937  ? -9.277  91.140  85.689  1.00 43.99 ? 935  SER   A O     1 
ATOM   6831  C  CB    . SER   A  1  937  ? -7.273  89.483  84.156  1.00 43.69 ? 935  SER   A CB    1 
ATOM   6832  O  OG    . SER   A  1  937  ? -7.463  89.847  82.798  1.00 46.51 ? 935  SER   A OG    1 
ATOM   6833  N  N     . ASP   A  1  938  ? -10.670 90.205  84.184  1.00 41.82 ? 936  ASP   A N     1 
ATOM   6834  C  CA    . ASP   A  1  938  ? -11.700 91.220  84.381  1.00 42.29 ? 936  ASP   A CA    1 
ATOM   6835  C  C     . ASP   A  1  938  ? -12.268 91.195  85.794  1.00 42.80 ? 936  ASP   A C     1 
ATOM   6836  O  O     . ASP   A  1  938  ? -12.825 92.201  86.244  1.00 40.83 ? 936  ASP   A O     1 
ATOM   6837  C  CB    . ASP   A  1  938  ? -12.842 91.023  83.381  1.00 44.74 ? 936  ASP   A CB    1 
ATOM   6838  C  CG    . ASP   A  1  938  ? -12.391 91.169  81.943  1.00 47.17 ? 936  ASP   A CG    1 
ATOM   6839  O  OD1   . ASP   A  1  938  ? -11.238 91.597  81.721  1.00 49.51 ? 936  ASP   A OD1   1 
ATOM   6840  O  OD2   . ASP   A  1  938  ? -13.188 90.847  81.035  1.00 45.54 ? 936  ASP   A OD2   1 
ATOM   6841  N  N     . LEU   A  1  939  ? -12.147 90.072  86.496  1.00 39.77 ? 937  LEU   A N     1 
ATOM   6842  C  CA    . LEU   A  1  939  ? -12.630 89.963  87.864  1.00 39.22 ? 937  LEU   A CA    1 
ATOM   6843  C  C     . LEU   A  1  939  ? -11.524 90.300  88.850  1.00 43.17 ? 937  LEU   A C     1 
ATOM   6844  O  O     . LEU   A  1  939  ? -10.365 89.916  88.661  1.00 43.93 ? 937  LEU   A O     1 
ATOM   6845  C  CB    . LEU   A  1  939  ? -13.126 88.548  88.141  1.00 34.60 ? 937  LEU   A CB    1 
ATOM   6846  C  CG    . LEU   A  1  939  ? -14.389 88.128  87.401  1.00 35.24 ? 937  LEU   A CG    1 
ATOM   6847  C  CD1   . LEU   A  1  939  ? -14.971 86.900  88.059  1.00 34.51 ? 937  LEU   A CD1   1 
ATOM   6848  C  CD2   . LEU   A  1  939  ? -15.397 89.262  87.390  1.00 35.32 ? 937  LEU   A CD2   1 
ATOM   6849  N  N     . GLN   A  1  940  ? -11.894 91.012  89.914  1.00 38.17 ? 938  GLN   A N     1 
ATOM   6850  C  CA    . GLN   A  1  940  ? -10.940 91.379  90.952  1.00 40.75 ? 938  GLN   A CA    1 
ATOM   6851  C  C     . GLN   A  1  940  ? -11.113 90.487  92.175  1.00 43.44 ? 938  GLN   A C     1 
ATOM   6852  O  O     . GLN   A  1  940  ? -10.269 89.627  92.443  1.00 50.70 ? 938  GLN   A O     1 
ATOM   6853  C  CB    . GLN   A  1  940  ? -11.099 92.852  91.336  1.00 42.27 ? 938  GLN   A CB    1 
ATOM   6854  N  N     . ARG   A  1  941  ? -12.199 90.679  92.918  1.00 38.39 ? 939  ARG   A N     1 
ATOM   6855  C  CA    . ARG   A  1  941  ? -12.479 89.911  94.121  1.00 35.60 ? 939  ARG   A CA    1 
ATOM   6856  C  C     . ARG   A  1  941  ? -13.847 89.248  94.007  1.00 29.24 ? 939  ARG   A C     1 
ATOM   6857  O  O     . ARG   A  1  941  ? -14.640 89.548  93.114  1.00 30.35 ? 939  ARG   A O     1 
ATOM   6858  C  CB    . ARG   A  1  941  ? -12.420 90.797  95.373  1.00 36.52 ? 939  ARG   A CB    1 
ATOM   6859  N  N     . GLU   A  1  942  ? -14.105 88.326  94.932  1.00 25.53 ? 940  GLU   A N     1 
ATOM   6860  C  CA    . GLU   A  1  942  ? -15.391 87.645  95.004  1.00 24.58 ? 940  GLU   A CA    1 
ATOM   6861  C  C     . GLU   A  1  942  ? -16.538 88.646  95.024  1.00 24.59 ? 940  GLU   A C     1 
ATOM   6862  O  O     . GLU   A  1  942  ? -16.515 89.627  95.776  1.00 25.73 ? 940  GLU   A O     1 
ATOM   6863  C  CB    . GLU   A  1  942  ? -15.417 86.818  96.288  1.00 24.20 ? 940  GLU   A CB    1 
ATOM   6864  C  CG    . GLU   A  1  942  ? -16.715 86.089  96.548  1.00 22.18 ? 940  GLU   A CG    1 
ATOM   6865  C  CD    . GLU   A  1  942  ? -16.732 85.508  97.935  1.00 22.93 ? 940  GLU   A CD    1 
ATOM   6866  O  OE1   . GLU   A  1  942  ? -16.573 86.295  98.896  1.00 27.61 ? 940  GLU   A OE1   1 
ATOM   6867  O  OE2   . GLU   A  1  942  ? -16.889 84.282  98.078  1.00 21.07 ? 940  GLU   A OE2   1 
ATOM   6868  N  N     . VAL   A  1  943  ? -17.542 88.395  94.184  1.00 23.13 ? 941  VAL   A N     1 
ATOM   6869  C  CA    . VAL   A  1  943  ? -18.788 89.155  94.171  1.00 22.25 ? 941  VAL   A CA    1 
ATOM   6870  C  C     . VAL   A  1  943  ? -19.867 88.212  94.680  1.00 24.26 ? 941  VAL   A C     1 
ATOM   6871  O  O     . VAL   A  1  943  ? -20.275 87.279  93.977  1.00 21.44 ? 941  VAL   A O     1 
ATOM   6872  C  CB    . VAL   A  1  943  ? -19.122 89.698  92.776  1.00 22.99 ? 941  VAL   A CB    1 
ATOM   6873  C  CG1   . VAL   A  1  943  ? -20.476 90.404  92.775  1.00 23.26 ? 941  VAL   A CG1   1 
ATOM   6874  C  CG2   . VAL   A  1  943  ? -18.025 90.643  92.312  1.00 27.97 ? 941  VAL   A CG2   1 
ATOM   6875  N  N     . PHE   A  1  944  ? -20.306 88.434  95.917  1.00 23.18 ? 942  PHE   A N     1 
ATOM   6876  C  CA    . PHE   A  1  944  ? -21.111 87.455  96.643  1.00 22.15 ? 942  PHE   A CA    1 
ATOM   6877  C  C     . PHE   A  1  944  ? -22.577 87.742  96.356  1.00 22.33 ? 942  PHE   A C     1 
ATOM   6878  O  O     . PHE   A  1  944  ? -23.316 88.296  97.171  1.00 23.22 ? 942  PHE   A O     1 
ATOM   6879  C  CB    . PHE   A  1  944  ? -20.793 87.526  98.132  1.00 19.80 ? 942  PHE   A CB    1 
ATOM   6880  C  CG    . PHE   A  1  944  ? -21.178 86.299  98.897  1.00 19.48 ? 942  PHE   A CG    1 
ATOM   6881  C  CD1   . PHE   A  1  944  ? -20.500 85.106  98.694  1.00 18.14 ? 942  PHE   A CD1   1 
ATOM   6882  C  CD2   . PHE   A  1  944  ? -22.202 86.337  99.836  1.00 19.01 ? 942  PHE   A CD2   1 
ATOM   6883  C  CE1   . PHE   A  1  944  ? -20.852 83.971  99.405  1.00 16.80 ? 942  PHE   A CE1   1 
ATOM   6884  C  CE2   . PHE   A  1  944  ? -22.546 85.198  100.555 1.00 19.89 ? 942  PHE   A CE2   1 
ATOM   6885  C  CZ    . PHE   A  1  944  ? -21.877 84.020  100.335 1.00 19.46 ? 942  PHE   A CZ    1 
ATOM   6886  N  N     . GLY   A  1  945  ? -23.000 87.365  95.153  1.00 20.26 ? 943  GLY   A N     1 
ATOM   6887  C  CA    . GLY   A  1  945  ? -24.343 87.633  94.709  1.00 20.94 ? 943  GLY   A CA    1 
ATOM   6888  C  C     . GLY   A  1  945  ? -24.642 86.838  93.463  1.00 20.70 ? 943  GLY   A C     1 
ATOM   6889  O  O     . GLY   A  1  945  ? -23.839 86.013  93.020  1.00 20.71 ? 943  GLY   A O     1 
ATOM   6890  N  N     . PRO   A  1  946  ? -25.811 87.061  92.879  1.00 18.40 ? 944  PRO   A N     1 
ATOM   6891  C  CA    . PRO   A  1  946  ? -26.272 86.218  91.764  1.00 19.24 ? 944  PRO   A CA    1 
ATOM   6892  C  C     . PRO   A  1  946  ? -25.727 86.698  90.427  1.00 19.34 ? 944  PRO   A C     1 
ATOM   6893  O  O     . PRO   A  1  946  ? -26.470 87.100  89.532  1.00 20.55 ? 944  PRO   A O     1 
ATOM   6894  C  CB    . PRO   A  1  946  ? -27.795 86.358  91.865  1.00 18.03 ? 944  PRO   A CB    1 
ATOM   6895  C  CG    . PRO   A  1  946  ? -27.981 87.790  92.346  1.00 20.89 ? 944  PRO   A CG    1 
ATOM   6896  C  CD    . PRO   A  1  946  ? -26.831 88.035  93.314  1.00 20.19 ? 944  PRO   A CD    1 
ATOM   6897  N  N     . VAL   A  1  947  ? -24.407 86.652  90.291  1.00 19.91 ? 945  VAL   A N     1 
ATOM   6898  C  CA    . VAL   A  1  947  ? -23.719 87.221  89.143  1.00 20.99 ? 945  VAL   A CA    1 
ATOM   6899  C  C     . VAL   A  1  947  ? -22.788 86.162  88.579  1.00 21.10 ? 945  VAL   A C     1 
ATOM   6900  O  O     . VAL   A  1  947  ? -21.745 85.858  89.170  1.00 21.39 ? 945  VAL   A O     1 
ATOM   6901  C  CB    . VAL   A  1  947  ? -22.948 88.499  89.490  1.00 23.34 ? 945  VAL   A CB    1 
ATOM   6902  C  CG1   . VAL   A  1  947  ? -22.359 89.101  88.231  1.00 23.19 ? 945  VAL   A CG1   1 
ATOM   6903  C  CG2   . VAL   A  1  947  ? -23.861 89.495  90.196  1.00 22.61 ? 945  VAL   A CG2   1 
ATOM   6904  N  N     . LEU   A  1  948  ? -23.150 85.623  87.429  1.00 19.45 ? 946  LEU   A N     1 
ATOM   6905  C  CA    . LEU   A  1  948  ? -22.347 84.627  86.750  1.00 19.68 ? 946  LEU   A CA    1 
ATOM   6906  C  C     . LEU   A  1  948  ? -21.571 85.315  85.643  1.00 19.95 ? 946  LEU   A C     1 
ATOM   6907  O  O     . LEU   A  1  948  ? -22.149 86.055  84.839  1.00 22.44 ? 946  LEU   A O     1 
ATOM   6908  C  CB    . LEU   A  1  948  ? -23.262 83.573  86.141  1.00 18.79 ? 946  LEU   A CB    1 
ATOM   6909  C  CG    . LEU   A  1  948  ? -22.505 82.557  85.299  1.00 19.40 ? 946  LEU   A CG    1 
ATOM   6910  C  CD1   . LEU   A  1  948  ? -21.551 81.767  86.190  1.00 19.40 ? 946  LEU   A CD1   1 
ATOM   6911  C  CD2   . LEU   A  1  948  ? -23.498 81.663  84.604  1.00 21.19 ? 946  LEU   A CD2   1 
ATOM   6912  N  N     . HIS   A  1  949  ? -20.271 85.077  85.602  1.00 19.18 ? 947  HIS   A N     1 
ATOM   6913  C  CA    . HIS   A  1  949  ? -19.441 85.578  84.525  1.00 19.26 ? 947  HIS   A CA    1 
ATOM   6914  C  C     . HIS   A  1  949  ? -19.126 84.430  83.586  1.00 21.61 ? 947  HIS   A C     1 
ATOM   6915  O  O     . HIS   A  1  949  ? -18.979 83.287  84.021  1.00 20.66 ? 947  HIS   A O     1 
ATOM   6916  C  CB    . HIS   A  1  949  ? -18.166 86.179  85.085  1.00 19.37 ? 947  HIS   A CB    1 
ATOM   6917  C  CG    . HIS   A  1  949  ? -18.419 87.206  86.139  1.00 21.79 ? 947  HIS   A CG    1 
ATOM   6918  N  ND1   . HIS   A  1  949  ? -18.620 86.877  87.462  1.00 21.90 ? 947  HIS   A ND1   1 
ATOM   6919  C  CD2   . HIS   A  1  949  ? -18.545 88.551  86.058  1.00 23.24 ? 947  HIS   A CD2   1 
ATOM   6920  C  CE1   . HIS   A  1  949  ? -18.839 87.982  88.154  1.00 22.96 ? 947  HIS   A CE1   1 
ATOM   6921  N  NE2   . HIS   A  1  949  ? -18.798 89.010  87.326  1.00 24.59 ? 947  HIS   A NE2   1 
ATOM   6922  N  N     . VAL   A  1  950  ? -19.074 84.729  82.293  1.00 20.14 ? 948  VAL   A N     1 
ATOM   6923  C  CA    . VAL   A  1  950  ? -18.879 83.720  81.263  1.00 21.37 ? 948  VAL   A CA    1 
ATOM   6924  C  C     . VAL   A  1  950  ? -17.658 84.103  80.452  1.00 23.49 ? 948  VAL   A C     1 
ATOM   6925  O  O     . VAL   A  1  950  ? -17.552 85.240  79.981  1.00 23.31 ? 948  VAL   A O     1 
ATOM   6926  C  CB    . VAL   A  1  950  ? -20.116 83.594  80.358  1.00 21.61 ? 948  VAL   A CB    1 
ATOM   6927  C  CG1   . VAL   A  1  950  ? -19.840 82.609  79.224  1.00 23.36 ? 948  VAL   A CG1   1 
ATOM   6928  C  CG2   . VAL   A  1  950  ? -21.328 83.167  81.171  1.00 21.69 ? 948  VAL   A CG2   1 
ATOM   6929  N  N     . ILE   A  1  951  ? -16.725 83.168  80.318  1.00 20.65 ? 949  ILE   A N     1 
ATOM   6930  C  CA    . ILE   A  1  951  ? -15.549 83.344  79.479  1.00 21.89 ? 949  ILE   A CA    1 
ATOM   6931  C  C     . ILE   A  1  951  ? -15.544 82.209  78.471  1.00 24.52 ? 949  ILE   A C     1 
ATOM   6932  O  O     . ILE   A  1  951  ? -16.033 81.111  78.750  1.00 21.74 ? 949  ILE   A O     1 
ATOM   6933  C  CB    . ILE   A  1  951  ? -14.243 83.351  80.298  1.00 25.11 ? 949  ILE   A CB    1 
ATOM   6934  N  N     . ARG   A  1  952  ? -14.998 82.476  77.292  1.00 22.16 ? 950  ARG   A N     1 
ATOM   6935  C  CA    . ARG   A  1  952  ? -14.885 81.471  76.249  1.00 21.63 ? 950  ARG   A CA    1 
ATOM   6936  C  C     . ARG   A  1  952  ? -13.418 81.119  76.068  1.00 20.48 ? 950  ARG   A C     1 
ATOM   6937  O  O     . ARG   A  1  952  ? -12.540 81.964  76.246  1.00 23.33 ? 950  ARG   A O     1 
ATOM   6938  C  CB    . ARG   A  1  952  ? -15.436 82.010  74.931  1.00 24.87 ? 950  ARG   A CB    1 
ATOM   6939  C  CG    . ARG   A  1  952  ? -16.841 82.561  75.059  1.00 25.87 ? 950  ARG   A CG    1 
ATOM   6940  C  CD    . ARG   A  1  952  ? -17.126 83.544  73.951  1.00 29.99 ? 950  ARG   A CD    1 
ATOM   6941  N  NE    . ARG   A  1  952  ? -17.429 82.862  72.702  1.00 31.26 ? 950  ARG   A NE    1 
ATOM   6942  C  CZ    . ARG   A  1  952  ? -18.655 82.712  72.217  1.00 31.26 ? 950  ARG   A CZ    1 
ATOM   6943  N  NH1   . ARG   A  1  952  ? -19.709 83.222  72.832  1.00 30.11 ? 950  ARG   A NH1   1 
ATOM   6944  N  NH2   . ARG   A  1  952  ? -18.826 82.031  71.090  1.00 28.75 ? 950  ARG   A NH2   1 
ATOM   6945  N  N     . TYR   A  1  953  ? -13.150 79.865  75.715  1.00 19.66 ? 951  TYR   A N     1 
ATOM   6946  C  CA    . TYR   A  1  953  ? -11.767 79.468  75.499  1.00 20.37 ? 951  TYR   A CA    1 
ATOM   6947  C  C     . TYR   A  1  953  ? -11.683 78.504  74.326  1.00 19.37 ? 951  TYR   A C     1 
ATOM   6948  O  O     . TYR   A  1  953  ? -12.609 77.731  74.065  1.00 20.28 ? 951  TYR   A O     1 
ATOM   6949  C  CB    . TYR   A  1  953  ? -11.157 78.829  76.762  1.00 21.82 ? 951  TYR   A CB    1 
ATOM   6950  C  CG    . TYR   A  1  953  ? -11.701 77.452  77.057  1.00 18.96 ? 951  TYR   A CG    1 
ATOM   6951  C  CD1   . TYR   A  1  953  ? -12.910 77.281  77.728  1.00 18.46 ? 951  TYR   A CD1   1 
ATOM   6952  C  CD2   . TYR   A  1  953  ? -11.021 76.320  76.627  1.00 20.33 ? 951  TYR   A CD2   1 
ATOM   6953  C  CE1   . TYR   A  1  953  ? -13.400 76.018  77.988  1.00 17.81 ? 951  TYR   A CE1   1 
ATOM   6954  C  CE2   . TYR   A  1  953  ? -11.498 75.062  76.880  1.00 17.47 ? 951  TYR   A CE2   1 
ATOM   6955  C  CZ    . TYR   A  1  953  ? -12.701 74.914  77.553  1.00 18.55 ? 951  TYR   A CZ    1 
ATOM   6956  O  OH    . TYR   A  1  953  ? -13.189 73.661  77.803  1.00 19.62 ? 951  TYR   A OH    1 
ATOM   6957  N  N     . ARG   A  1  954  ? -10.545 78.556  73.633  1.00 22.52 ? 952  ARG   A N     1 
ATOM   6958  C  CA    . ARG   A  1  954  ? -10.231 77.587  72.596  1.00 24.08 ? 952  ARG   A CA    1 
ATOM   6959  C  C     . ARG   A  1  954  ? -9.643  76.339  73.240  1.00 20.43 ? 952  ARG   A C     1 
ATOM   6960  O  O     . ARG   A  1  954  ? -8.891  76.427  74.215  1.00 21.48 ? 952  ARG   A O     1 
ATOM   6961  C  CB    . ARG   A  1  954  ? -9.217  78.185  71.619  1.00 25.51 ? 952  ARG   A CB    1 
ATOM   6962  N  N     . ARG   A  1  955  ? -9.993  75.172  72.685  1.00 22.32 ? 953  ARG   A N     1 
ATOM   6963  C  CA    . ARG   A  1  955  ? -9.587  73.902  73.284  1.00 22.74 ? 953  ARG   A CA    1 
ATOM   6964  C  C     . ARG   A  1  955  ? -8.088  73.851  73.569  1.00 22.28 ? 953  ARG   A C     1 
ATOM   6965  O  O     . ARG   A  1  955  ? -7.667  73.405  74.643  1.00 24.18 ? 953  ARG   A O     1 
ATOM   6966  C  CB    . ARG   A  1  955  ? -9.999  72.733  72.385  1.00 28.65 ? 953  ARG   A CB    1 
ATOM   6967  C  CG    . ARG   A  1  955  ? -9.527  71.359  72.889  1.00 34.85 ? 953  ARG   A CG    1 
ATOM   6968  C  CD    . ARG   A  1  955  ? -9.839  71.228  74.364  1.00 37.45 ? 953  ARG   A CD    1 
ATOM   6969  N  NE    . ARG   A  1  955  ? -9.496  69.953  74.983  1.00 43.10 ? 953  ARG   A NE    1 
ATOM   6970  C  CZ    . ARG   A  1  955  ? -8.357  69.706  75.616  1.00 39.17 ? 953  ARG   A CZ    1 
ATOM   6971  N  NH1   . ARG   A  1  955  ? -7.370  70.591  75.637  1.00 30.59 ? 953  ARG   A NH1   1 
ATOM   6972  N  NH2   . ARG   A  1  955  ? -8.206  68.545  76.250  1.00 37.14 ? 953  ARG   A NH2   1 
ATOM   6973  N  N     . ASP   A  1  956  ? -7.264  74.309  72.629  1.00 22.09 ? 954  ASP   A N     1 
ATOM   6974  C  CA    . ASP   A  1  956  ? -5.823  74.220  72.844  1.00 22.48 ? 954  ASP   A CA    1 
ATOM   6975  C  C     . ASP   A  1  956  ? -5.362  75.081  74.008  1.00 24.00 ? 954  ASP   A C     1 
ATOM   6976  O  O     . ASP   A  1  956  ? -4.263  74.861  74.530  1.00 25.02 ? 954  ASP   A O     1 
ATOM   6977  C  CB    . ASP   A  1  956  ? -5.053  74.606  71.580  1.00 24.01 ? 954  ASP   A CB    1 
ATOM   6978  C  CG    . ASP   A  1  956  ? -5.231  73.603  70.457  1.00 29.68 ? 954  ASP   A CG    1 
ATOM   6979  O  OD1   . ASP   A  1  956  ? -5.607  72.445  70.743  1.00 30.49 ? 954  ASP   A OD1   1 
ATOM   6980  O  OD2   . ASP   A  1  956  ? -4.988  73.974  69.290  1.00 34.48 ? 954  ASP   A OD2   1 
ATOM   6981  N  N     . ASP   A  1  957  ? -6.170  76.053  74.424  1.00 21.99 ? 955  ASP   A N     1 
ATOM   6982  C  CA    . ASP   A  1  957  ? -5.829  76.948  75.518  1.00 23.05 ? 955  ASP   A CA    1 
ATOM   6983  C  C     . ASP   A  1  957  ? -6.369  76.471  76.857  1.00 21.88 ? 955  ASP   A C     1 
ATOM   6984  O  O     . ASP   A  1  957  ? -6.356  77.233  77.829  1.00 22.19 ? 955  ASP   A O     1 
ATOM   6985  C  CB    . ASP   A  1  957  ? -6.322  78.362  75.216  1.00 26.74 ? 955  ASP   A CB    1 
ATOM   6986  C  CG    . ASP   A  1  957  ? -5.630  78.969  74.015  1.00 32.12 ? 955  ASP   A CG    1 
ATOM   6987  O  OD1   . ASP   A  1  957  ? -4.431  78.679  73.807  1.00 30.71 ? 955  ASP   A OD1   1 
ATOM   6988  O  OD2   . ASP   A  1  957  ? -6.287  79.725  73.275  1.00 34.78 ? 955  ASP   A OD2   1 
ATOM   6989  N  N     . LEU   A  1  958  ? -6.815  75.219  76.936  1.00 20.49 ? 956  LEU   A N     1 
ATOM   6990  C  CA    . LEU   A  1  958  ? -7.373  74.718  78.188  1.00 18.93 ? 956  LEU   A CA    1 
ATOM   6991  C  C     . LEU   A  1  958  ? -6.369  74.823  79.327  1.00 21.25 ? 956  LEU   A C     1 
ATOM   6992  O  O     . LEU   A  1  958  ? -6.721  75.231  80.441  1.00 19.11 ? 956  LEU   A O     1 
ATOM   6993  C  CB    . LEU   A  1  958  ? -7.813  73.271  78.011  1.00 20.59 ? 956  LEU   A CB    1 
ATOM   6994  C  CG    . LEU   A  1  958  ? -8.334  72.608  79.284  1.00 19.92 ? 956  LEU   A CG    1 
ATOM   6995  C  CD1   . LEU   A  1  958  ? -9.553  73.343  79.833  1.00 22.25 ? 956  LEU   A CD1   1 
ATOM   6996  C  CD2   . LEU   A  1  958  ? -8.648  71.149  79.011  1.00 23.20 ? 956  LEU   A CD2   1 
ATOM   6997  N  N     . ASP   A  1  959  ? -5.105  74.476  79.071  1.00 18.07 ? 957  ASP   A N     1 
ATOM   6998  C  CA    . ASP   A  1  959  ? -4.137  74.506  80.158  1.00 19.96 ? 957  ASP   A CA    1 
ATOM   6999  C  C     . ASP   A  1  959  ? -3.876  75.933  80.613  1.00 18.83 ? 957  ASP   A C     1 
ATOM   7000  O  O     . ASP   A  1  959  ? -3.743  76.195  81.815  1.00 20.70 ? 957  ASP   A O     1 
ATOM   7001  C  CB    . ASP   A  1  959  ? -2.833  73.839  79.738  1.00 20.83 ? 957  ASP   A CB    1 
ATOM   7002  C  CG    . ASP   A  1  959  ? -1.954  73.537  80.923  1.00 22.59 ? 957  ASP   A CG    1 
ATOM   7003  O  OD1   . ASP   A  1  959  ? -2.419  72.847  81.850  1.00 22.43 ? 957  ASP   A OD1   1 
ATOM   7004  O  OD2   . ASP   A  1  959  ? -0.798  73.996  80.947  1.00 30.15 ? 957  ASP   A OD2   1 
ATOM   7005  N  N     . ARG   A  1  960  ? -3.790  76.865  79.667  1.00 19.53 ? 958  ARG   A N     1 
ATOM   7006  C  CA    . ARG   A  1  960  ? -3.661  78.269  80.034  1.00 20.19 ? 958  ARG   A CA    1 
ATOM   7007  C  C     . ARG   A  1  960  ? -4.869  78.720  80.842  1.00 21.99 ? 958  ARG   A C     1 
ATOM   7008  O  O     . ARG   A  1  960  ? -4.728  79.480  81.810  1.00 22.66 ? 958  ARG   A O     1 
ATOM   7009  C  CB    . ARG   A  1  960  ? -3.499  79.115  78.769  1.00 23.17 ? 958  ARG   A CB    1 
ATOM   7010  C  CG    . ARG   A  1  960  ? -3.214  80.592  78.998  1.00 26.47 ? 958  ARG   A CG    1 
ATOM   7011  C  CD    . ARG   A  1  960  ? -4.495  81.420  79.102  1.00 36.88 ? 958  ARG   A CD    1 
ATOM   7012  N  NE    . ARG   A  1  960  ? -5.513  81.008  78.141  1.00 38.07 ? 958  ARG   A NE    1 
ATOM   7013  C  CZ    . ARG   A  1  960  ? -6.815  81.221  78.292  1.00 37.97 ? 958  ARG   A CZ    1 
ATOM   7014  N  NH1   . ARG   A  1  960  ? -7.295  81.851  79.353  1.00 41.09 ? 958  ARG   A NH1   1 
ATOM   7015  N  NH2   . ARG   A  1  960  ? -7.658  80.778  77.363  1.00 43.51 ? 958  ARG   A NH2   1 
ATOM   7016  N  N     . LEU   A  1  961  ? -6.057  78.249  80.467  1.00 19.51 ? 959  LEU   A N     1 
ATOM   7017  C  CA    . LEU   A  1  961  ? -7.266  78.622  81.192  1.00 20.80 ? 959  LEU   A CA    1 
ATOM   7018  C  C     . LEU   A  1  961  ? -7.201  78.152  82.635  1.00 21.36 ? 959  LEU   A C     1 
ATOM   7019  O  O     . LEU   A  1  961  ? -7.544  78.905  83.554  1.00 20.58 ? 959  LEU   A O     1 
ATOM   7020  C  CB    . LEU   A  1  961  ? -8.487  78.030  80.504  1.00 18.73 ? 959  LEU   A CB    1 
ATOM   7021  C  CG    . LEU   A  1  961  ? -9.803  78.212  81.264  1.00 19.26 ? 959  LEU   A CG    1 
ATOM   7022  C  CD1   . LEU   A  1  961  ? -10.178 79.690  81.354  1.00 24.94 ? 959  LEU   A CD1   1 
ATOM   7023  C  CD2   . LEU   A  1  961  ? -10.912 77.404  80.612  1.00 23.04 ? 959  LEU   A CD2   1 
ATOM   7024  N  N     . VAL   A  1  962  ? -6.771  76.908  82.858  1.00 18.99 ? 960  VAL   A N     1 
ATOM   7025  C  CA    . VAL   A  1  962  ? -6.617  76.425  84.224  1.00 19.28 ? 960  VAL   A CA    1 
ATOM   7026  C  C     . VAL   A  1  962  ? -5.629  77.296  84.989  1.00 22.39 ? 960  VAL   A C     1 
ATOM   7027  O  O     . VAL   A  1  962  ? -5.849  77.616  86.163  1.00 22.11 ? 960  VAL   A O     1 
ATOM   7028  C  CB    . VAL   A  1  962  ? -6.232  74.935  84.238  1.00 19.98 ? 960  VAL   A CB    1 
ATOM   7029  C  CG1   . VAL   A  1  962  ? -5.989  74.455  85.677  1.00 23.36 ? 960  VAL   A CG1   1 
ATOM   7030  C  CG2   . VAL   A  1  962  ? -7.319  74.104  83.554  1.00 20.19 ? 960  VAL   A CG2   1 
ATOM   7031  N  N     . ASP   A  1  963  ? -4.533  77.701  84.337  1.00 22.78 ? 961  ASP   A N     1 
ATOM   7032  C  CA    . ASP   A  1  963  ? -3.620  78.665  84.948  1.00 22.36 ? 961  ASP   A CA    1 
ATOM   7033  C  C     . ASP   A  1  963  ? -4.356  79.941  85.332  1.00 22.81 ? 961  ASP   A C     1 
ATOM   7034  O  O     . ASP   A  1  963  ? -4.171  80.469  86.436  1.00 24.99 ? 961  ASP   A O     1 
ATOM   7035  C  CB    . ASP   A  1  963  ? -2.489  79.021  83.980  1.00 24.23 ? 961  ASP   A CB    1 
ATOM   7036  C  CG    . ASP   A  1  963  ? -1.483  77.913  83.799  1.00 29.21 ? 961  ASP   A CG    1 
ATOM   7037  O  OD1   . ASP   A  1  963  ? -1.467  76.954  84.596  1.00 33.57 ? 961  ASP   A OD1   1 
ATOM   7038  O  OD2   . ASP   A  1  963  ? -0.693  78.014  82.830  1.00 36.33 ? 961  ASP   A OD2   1 
ATOM   7039  N  N     . ASP   A  1  964  ? -5.195  80.454  84.427  1.00 21.35 ? 962  ASP   A N     1 
ATOM   7040  C  CA    . ASP   A  1  964  ? -5.915  81.693  84.706  1.00 25.02 ? 962  ASP   A CA    1 
ATOM   7041  C  C     . ASP   A  1  964  ? -6.848  81.531  85.899  1.00 27.68 ? 962  ASP   A C     1 
ATOM   7042  O  O     . ASP   A  1  964  ? -6.950  82.427  86.745  1.00 28.14 ? 962  ASP   A O     1 
ATOM   7043  C  CB    . ASP   A  1  964  ? -6.696  82.132  83.470  1.00 25.92 ? 962  ASP   A CB    1 
ATOM   7044  C  CG    . ASP   A  1  964  ? -5.790  82.616  82.356  1.00 26.85 ? 962  ASP   A CG    1 
ATOM   7045  O  OD1   . ASP   A  1  964  ? -4.576  82.783  82.604  1.00 34.26 ? 962  ASP   A OD1   1 
ATOM   7046  O  OD2   . ASP   A  1  964  ? -6.303  82.830  81.238  1.00 39.01 ? 962  ASP   A OD2   1 
ATOM   7047  N  N     . VAL   A  1  965  ? -7.536  80.394  85.986  1.00 22.06 ? 963  VAL   A N     1 
ATOM   7048  C  CA    . VAL   A  1  965  ? -8.398  80.144  87.137  1.00 22.42 ? 963  VAL   A CA    1 
ATOM   7049  C  C     . VAL   A  1  965  ? -7.569  80.119  88.410  1.00 24.60 ? 963  VAL   A C     1 
ATOM   7050  O  O     . VAL   A  1  965  ? -7.926  80.741  89.419  1.00 24.94 ? 963  VAL   A O     1 
ATOM   7051  C  CB    . VAL   A  1  965  ? -9.179  78.833  86.950  1.00 20.23 ? 963  VAL   A CB    1 
ATOM   7052  C  CG1   . VAL   A  1  965  ? -9.921  78.477  88.229  1.00 21.91 ? 963  VAL   A CG1   1 
ATOM   7053  C  CG2   . VAL   A  1  965  ? -10.151 78.951  85.780  1.00 22.75 ? 963  VAL   A CG2   1 
ATOM   7054  N  N     . ASN   A  1  966  ? -6.447  79.398  88.382  1.00 21.22 ? 964  ASN   A N     1 
ATOM   7055  C  CA    . ASN   A  1  966  ? -5.586  79.328  89.556  1.00 22.18 ? 964  ASN   A CA    1 
ATOM   7056  C  C     . ASN   A  1  966  ? -5.022  80.693  89.907  1.00 25.80 ? 964  ASN   A C     1 
ATOM   7057  O  O     . ASN   A  1  966  ? -4.772  80.977  91.084  1.00 23.89 ? 964  ASN   A O     1 
ATOM   7058  C  CB    . ASN   A  1  966  ? -4.419  78.363  89.318  1.00 21.23 ? 964  ASN   A CB    1 
ATOM   7059  C  CG    . ASN   A  1  966  ? -4.837  76.902  89.339  1.00 22.78 ? 964  ASN   A CG    1 
ATOM   7060  O  OD1   . ASN   A  1  966  ? -5.871  76.543  89.898  1.00 21.54 ? 964  ASN   A OD1   1 
ATOM   7061  N  ND2   . ASN   A  1  966  ? -4.021  76.048  88.730  1.00 21.13 ? 964  ASN   A ND2   1 
ATOM   7062  N  N     . ALA   A  1  967  ? -4.825  81.552  88.904  1.00 24.98 ? 965  ALA   A N     1 
ATOM   7063  C  CA    . ALA   A  1  967  ? -4.119  82.812  89.108  1.00 27.67 ? 965  ALA   A CA    1 
ATOM   7064  C  C     . ALA   A  1  967  ? -4.908  83.824  89.923  1.00 27.53 ? 965  ALA   A C     1 
ATOM   7065  O  O     . ALA   A  1  967  ? -4.323  84.818  90.367  1.00 28.48 ? 965  ALA   A O     1 
ATOM   7066  C  CB    . ALA   A  1  967  ? -3.705  83.420  87.766  1.00 30.93 ? 965  ALA   A CB    1 
ATOM   7067  N  N     . THR   A  1  968  ? -6.210  83.616  90.126  1.00 23.23 ? 966  THR   A N     1 
ATOM   7068  C  CA    . THR   A  1  968  ? -6.949  84.518  91.001  1.00 23.81 ? 966  THR   A CA    1 
ATOM   7069  C  C     . THR   A  1  968  ? -6.451  84.439  92.433  1.00 24.62 ? 966  THR   A C     1 
ATOM   7070  O  O     . THR   A  1  968  ? -6.650  85.384  93.204  1.00 27.19 ? 966  THR   A O     1 
ATOM   7071  C  CB    . THR   A  1  968  ? -8.432  84.166  91.003  1.00 25.19 ? 966  THR   A CB    1 
ATOM   7072  O  OG1   . THR   A  1  968  ? -8.628  82.945  91.732  1.00 23.31 ? 966  THR   A OG1   1 
ATOM   7073  C  CG2   . THR   A  1  968  ? -8.954  84.005  89.577  1.00 24.24 ? 966  THR   A CG2   1 
ATOM   7074  N  N     . GLY   A  1  969  ? -5.820  83.333  92.805  1.00 21.96 ? 967  GLY   A N     1 
ATOM   7075  C  CA    . GLY   A  1  969  ? -5.410  83.108  94.168  1.00 22.35 ? 967  GLY   A CA    1 
ATOM   7076  C  C     . GLY   A  1  969  ? -6.441  82.406  95.009  1.00 21.87 ? 967  GLY   A C     1 
ATOM   7077  O  O     . GLY   A  1  969  ? -6.110  81.938  96.101  1.00 19.61 ? 967  GLY   A O     1 
ATOM   7078  N  N     . TYR   A  1  970  ? -7.681  82.320  94.538  1.00 20.20 ? 968  TYR   A N     1 
ATOM   7079  C  CA    . TYR   A  1  970  ? -8.686  81.561  95.250  1.00 18.51 ? 968  TYR   A CA    1 
ATOM   7080  C  C     . TYR   A  1  970  ? -8.520  80.081  94.936  1.00 17.63 ? 968  TYR   A C     1 
ATOM   7081  O  O     . TYR   A  1  970  ? -7.720  79.687  94.083  1.00 21.57 ? 968  TYR   A O     1 
ATOM   7082  C  CB    . TYR   A  1  970  ? -10.076 82.043  94.855  1.00 18.34 ? 968  TYR   A CB    1 
ATOM   7083  C  CG    . TYR   A  1  970  ? -10.383 83.448  95.310  1.00 19.29 ? 968  TYR   A CG    1 
ATOM   7084  C  CD1   . TYR   A  1  970  ? -10.904 83.690  96.576  1.00 21.68 ? 968  TYR   A CD1   1 
ATOM   7085  C  CD2   . TYR   A  1  970  ? -10.176 84.533  94.467  1.00 22.46 ? 968  TYR   A CD2   1 
ATOM   7086  C  CE1   . TYR   A  1  970  ? -11.213 84.972  96.986  1.00 22.59 ? 968  TYR   A CE1   1 
ATOM   7087  C  CE2   . TYR   A  1  970  ? -10.480 85.820  94.870  1.00 24.26 ? 968  TYR   A CE2   1 
ATOM   7088  C  CZ    . TYR   A  1  970  ? -10.996 86.033  96.131  1.00 25.06 ? 968  TYR   A CZ    1 
ATOM   7089  O  OH    . TYR   A  1  970  ? -11.303 87.313  96.541  1.00 31.00 ? 968  TYR   A OH    1 
ATOM   7090  N  N     . GLY   A  1  971  ? -9.292  79.255  95.622  1.00 15.65 ? 969  GLY   A N     1 
ATOM   7091  C  CA    . GLY   A  1  971  ? -9.161  77.829  95.430  1.00 16.47 ? 969  GLY   A CA    1 
ATOM   7092  C  C     . GLY   A  1  971  ? -10.184 77.065  96.230  1.00 16.53 ? 969  GLY   A C     1 
ATOM   7093  O  O     . GLY   A  1  971  ? -9.842  76.154  96.988  1.00 17.16 ? 969  GLY   A O     1 
ATOM   7094  N  N     . LEU   A  1  972  ? -11.450 77.435  96.065  1.00 14.78 ? 970  LEU   A N     1 
ATOM   7095  C  CA    . LEU   A  1  972  ? -12.510 76.838  96.869  1.00 16.10 ? 970  LEU   A CA    1 
ATOM   7096  C  C     . LEU   A  1  972  ? -13.189 75.715  96.095  1.00 16.53 ? 970  LEU   A C     1 
ATOM   7097  O  O     . LEU   A  1  972  ? -12.803 74.553  96.230  1.00 16.24 ? 970  LEU   A O     1 
ATOM   7098  C  CB    . LEU   A  1  972  ? -13.497 77.907  97.329  1.00 16.46 ? 970  LEU   A CB    1 
ATOM   7099  C  CG    . LEU   A  1  972  ? -14.507 77.436  98.375  1.00 16.66 ? 970  LEU   A CG    1 
ATOM   7100  C  CD1   . LEU   A  1  972  ? -13.817 76.684  99.518  1.00 16.95 ? 970  LEU   A CD1   1 
ATOM   7101  C  CD2   . LEU   A  1  972  ? -15.273 78.637  98.918  1.00 18.66 ? 970  LEU   A CD2   1 
ATOM   7102  N  N     . THR   A  1  973  ? -14.201 76.028  95.287  1.00 15.31 ? 971  THR   A N     1 
ATOM   7103  C  CA    . THR   A  1  973  ? -14.827 74.997  94.477  1.00 15.01 ? 971  THR   A CA    1 
ATOM   7104  C  C     . THR   A  1  973  ? -14.452 75.163  93.014  1.00 14.98 ? 971  THR   A C     1 
ATOM   7105  O  O     . THR   A  1  973  ? -14.080 76.242  92.557  1.00 15.88 ? 971  THR   A O     1 
ATOM   7106  C  CB    . THR   A  1  973  ? -16.347 74.994  94.631  1.00 14.41 ? 971  THR   A CB    1 
ATOM   7107  O  OG1   . THR   A  1  973  ? -16.851 76.267  94.234  1.00 16.41 ? 971  THR   A OG1   1 
ATOM   7108  C  CG2   . THR   A  1  973  ? -16.749 74.700  96.066  1.00 16.99 ? 971  THR   A CG2   1 
ATOM   7109  N  N     . PHE   A  1  974  ? -14.574 74.063  92.286  1.00 15.65 ? 972  PHE   A N     1 
ATOM   7110  C  CA    . PHE   A  1  974  ? -14.263 74.054  90.870  1.00 15.14 ? 972  PHE   A CA    1 
ATOM   7111  C  C     . PHE   A  1  974  ? -15.044 72.931  90.229  1.00 14.17 ? 972  PHE   A C     1 
ATOM   7112  O  O     . PHE   A  1  974  ? -15.102 71.824  90.763  1.00 16.47 ? 972  PHE   A O     1 
ATOM   7113  C  CB    . PHE   A  1  974  ? -12.771 73.797  90.655  1.00 15.64 ? 972  PHE   A CB    1 
ATOM   7114  C  CG    . PHE   A  1  974  ? -12.424 73.594  89.224  1.00 14.68 ? 972  PHE   A CG    1 
ATOM   7115  C  CD1   . PHE   A  1  974  ? -12.245 74.683  88.392  1.00 14.47 ? 972  PHE   A CD1   1 
ATOM   7116  C  CD2   . PHE   A  1  974  ? -12.352 72.313  88.692  1.00 16.54 ? 972  PHE   A CD2   1 
ATOM   7117  C  CE1   . PHE   A  1  974  ? -11.956 74.500  87.054  1.00 17.12 ? 972  PHE   A CE1   1 
ATOM   7118  C  CE2   . PHE   A  1  974  ? -12.053 72.122  87.352  1.00 15.20 ? 972  PHE   A CE2   1 
ATOM   7119  C  CZ    . PHE   A  1  974  ? -11.861 73.215  86.538  1.00 16.04 ? 972  PHE   A CZ    1 
ATOM   7120  N  N     . GLY   A  1  975  ? -15.627 73.210  89.074  1.00 13.96 ? 973  GLY   A N     1 
ATOM   7121  C  CA    . GLY   A  1  975  ? -16.385 72.221  88.345  1.00 15.30 ? 973  GLY   A CA    1 
ATOM   7122  C  C     . GLY   A  1  975  ? -15.815 71.972  86.966  1.00 14.89 ? 973  GLY   A C     1 
ATOM   7123  O  O     . GLY   A  1  975  ? -15.245 72.864  86.334  1.00 14.20 ? 973  GLY   A O     1 
ATOM   7124  N  N     . LEU   A  1  976  ? -15.991 70.748  86.500  1.00 15.08 ? 974  LEU   A N     1 
ATOM   7125  C  CA    . LEU   A  1  976  ? -15.589 70.393  85.150  1.00 14.56 ? 974  LEU   A CA    1 
ATOM   7126  C  C     . LEU   A  1  976  ? -16.682 69.536  84.547  1.00 14.04 ? 974  LEU   A C     1 
ATOM   7127  O  O     . LEU   A  1  976  ? -17.090 68.537  85.144  1.00 15.60 ? 974  LEU   A O     1 
ATOM   7128  C  CB    . LEU   A  1  976  ? -14.291 69.598  85.195  1.00 15.86 ? 974  LEU   A CB    1 
ATOM   7129  C  CG    . LEU   A  1  976  ? -13.863 68.997  83.866  1.00 15.41 ? 974  LEU   A CG    1 
ATOM   7130  C  CD1   . LEU   A  1  976  ? -13.531 70.082  82.858  1.00 18.49 ? 974  LEU   A CD1   1 
ATOM   7131  C  CD2   . LEU   A  1  976  ? -12.677 68.102  84.125  1.00 18.67 ? 974  LEU   A CD2   1 
ATOM   7132  N  N     . HIS   A  1  977  ? -17.162 69.930  83.374  1.00 14.70 ? 975  HIS   A N     1 
ATOM   7133  C  CA    . HIS   A  1  977  ? -18.135 69.143  82.634  1.00 15.42 ? 975  HIS   A CA    1 
ATOM   7134  C  C     . HIS   A  1  977  ? -17.448 68.659  81.369  1.00 14.77 ? 975  HIS   A C     1 
ATOM   7135  O  O     . HIS   A  1  977  ? -17.145 69.454  80.470  1.00 15.74 ? 975  HIS   A O     1 
ATOM   7136  C  CB    . HIS   A  1  977  ? -19.380 69.960  82.296  1.00 16.99 ? 975  HIS   A CB    1 
ATOM   7137  C  CG    . HIS   A  1  977  ? -20.477 69.814  83.294  1.00 18.51 ? 975  HIS   A CG    1 
ATOM   7138  N  ND1   . HIS   A  1  977  ? -21.590 69.040  83.059  1.00 23.58 ? 975  HIS   A ND1   1 
ATOM   7139  C  CD2   . HIS   A  1  977  ? -20.622 70.319  84.542  1.00 24.62 ? 975  HIS   A CD2   1 
ATOM   7140  C  CE1   . HIS   A  1  977  ? -22.387 69.094  84.111  1.00 22.18 ? 975  HIS   A CE1   1 
ATOM   7141  N  NE2   . HIS   A  1  977  ? -21.824 69.863  85.022  1.00 21.90 ? 975  HIS   A NE2   1 
ATOM   7142  N  N     . THR   A  1  978  ? -17.220 67.356  81.315  1.00 14.73 ? 976  THR   A N     1 
ATOM   7143  C  CA    . THR   A  1  978  ? -16.608 66.722  80.163  1.00 15.69 ? 976  THR   A CA    1 
ATOM   7144  C  C     . THR   A  1  978  ? -16.868 65.241  80.285  1.00 15.51 ? 976  THR   A C     1 
ATOM   7145  O  O     . THR   A  1  978  ? -17.026 64.708  81.385  1.00 17.46 ? 976  THR   A O     1 
ATOM   7146  C  CB    . THR   A  1  978  ? -15.093 66.942  80.117  1.00 17.08 ? 976  THR   A CB    1 
ATOM   7147  O  OG1   . THR   A  1  978  ? -14.556 66.265  78.972  1.00 16.13 ? 976  THR   A OG1   1 
ATOM   7148  C  CG2   . THR   A  1  978  ? -14.435 66.350  81.329  1.00 17.78 ? 976  THR   A CG2   1 
ATOM   7149  N  N     . ARG   A  1  979  ? -16.881 64.576  79.147  1.00 15.83 ? 977  ARG   A N     1 
ATOM   7150  C  CA    . ARG   A  1  979  ? -16.958 63.131  79.131  1.00 18.56 ? 977  ARG   A CA    1 
ATOM   7151  C  C     . ARG   A  1  979  ? -15.598 62.485  78.934  1.00 17.68 ? 977  ARG   A C     1 
ATOM   7152  O  O     . ARG   A  1  979  ? -15.505 61.255  78.955  1.00 19.91 ? 977  ARG   A O     1 
ATOM   7153  C  CB    . ARG   A  1  979  ? -17.895 62.697  78.015  1.00 18.34 ? 977  ARG   A CB    1 
ATOM   7154  C  CG    . ARG   A  1  979  ? -19.321 63.077  78.309  1.00 22.64 ? 977  ARG   A CG    1 
ATOM   7155  C  CD    . ARG   A  1  979  ? -20.184 62.852  77.114  1.00 31.01 ? 977  ARG   A CD    1 
ATOM   7156  N  NE    . ARG   A  1  979  ? -21.585 63.071  77.440  1.00 34.03 ? 977  ARG   A NE    1 
ATOM   7157  C  CZ    . ARG   A  1  979  ? -22.582 62.795  76.615  1.00 37.46 ? 977  ARG   A CZ    1 
ATOM   7158  N  NH1   . ARG   A  1  979  ? -22.357 62.307  75.405  1.00 31.17 ? 977  ARG   A NH1   1 
ATOM   7159  N  NH2   . ARG   A  1  979  ? -23.833 63.000  77.018  1.00 35.86 ? 977  ARG   A NH2   1 
ATOM   7160  N  N     . LEU   A  1  980  ? -14.551 63.275  78.770  1.00 14.94 ? 978  LEU   A N     1 
ATOM   7161  C  CA    . LEU   A  1  980  ? -13.284 62.780  78.251  1.00 15.42 ? 978  LEU   A CA    1 
ATOM   7162  C  C     . LEU   A  1  980  ? -12.285 62.593  79.384  1.00 16.76 ? 978  LEU   A C     1 
ATOM   7163  O  O     . LEU   A  1  980  ? -11.902 63.559  80.046  1.00 16.29 ? 978  LEU   A O     1 
ATOM   7164  C  CB    . LEU   A  1  980  ? -12.724 63.750  77.217  1.00 16.01 ? 978  LEU   A CB    1 
ATOM   7165  C  CG    . LEU   A  1  980  ? -13.699 64.093  76.097  1.00 17.01 ? 978  LEU   A CG    1 
ATOM   7166  C  CD1   . LEU   A  1  980  ? -13.087 65.121  75.161  1.00 19.63 ? 978  LEU   A CD1   1 
ATOM   7167  C  CD2   . LEU   A  1  980  ? -14.085 62.823  75.329  1.00 19.20 ? 978  LEU   A CD2   1 
ATOM   7168  N  N     . ASP   A  1  981  ? -11.840 61.351  79.573  1.00 16.61 ? 979  ASP   A N     1 
ATOM   7169  C  CA    . ASP   A  1  981  ? -10.886 61.057  80.640  1.00 16.20 ? 979  ASP   A CA    1 
ATOM   7170  C  C     . ASP   A  1  981  ? -9.607  61.871  80.513  1.00 17.17 ? 979  ASP   A C     1 
ATOM   7171  O  O     . ASP   A  1  981  ? -9.029  62.265  81.527  1.00 16.07 ? 979  ASP   A O     1 
ATOM   7172  C  CB    . ASP   A  1  981  ? -10.534 59.574  80.644  1.00 19.09 ? 979  ASP   A CB    1 
ATOM   7173  C  CG    . ASP   A  1  981  ? -11.645 58.711  81.148  1.00 19.31 ? 979  ASP   A CG    1 
ATOM   7174  O  OD1   . ASP   A  1  981  ? -12.584 59.243  81.772  1.00 22.56 ? 979  ASP   A OD1   1 
ATOM   7175  O  OD2   . ASP   A  1  981  ? -11.562 57.482  80.921  1.00 23.02 ? 979  ASP   A OD2   1 
ATOM   7176  N  N     . GLU   A  1  982  ? -9.116  62.100  79.293  1.00 15.95 ? 980  GLU   A N     1 
ATOM   7177  C  CA    . GLU   A  1  982  ? -7.878  62.864  79.182  1.00 16.53 ? 980  GLU   A CA    1 
ATOM   7178  C  C     . GLU   A  1  982  ? -8.079  64.270  79.725  1.00 16.07 ? 980  GLU   A C     1 
ATOM   7179  O  O     . GLU   A  1  982  ? -7.210  64.818  80.409  1.00 17.00 ? 980  GLU   A O     1 
ATOM   7180  C  CB    . GLU   A  1  982  ? -7.405  62.931  77.736  1.00 19.06 ? 980  GLU   A CB    1 
ATOM   7181  C  CG    . GLU   A  1  982  ? -6.199  63.847  77.562  1.00 18.99 ? 980  GLU   A CG    1 
ATOM   7182  C  CD    . GLU   A  1  982  ? -5.940  64.213  76.121  1.00 25.55 ? 980  GLU   A CD    1 
ATOM   7183  O  OE1   . GLU   A  1  982  ? -6.870  64.693  75.437  1.00 26.05 ? 980  GLU   A OE1   1 
ATOM   7184  O  OE2   . GLU   A  1  982  ? -4.791  64.031  75.664  1.00 22.97 ? 980  GLU   A OE2   1 
ATOM   7185  N  N     . THR   A  1  983  ? -9.248  64.848  79.466  1.00 14.73 ? 981  THR   A N     1 
ATOM   7186  C  CA    . THR   A  1  983  ? -9.511  66.196  79.944  1.00 15.85 ? 981  THR   A CA    1 
ATOM   7187  C  C     . THR   A  1  983  ? -9.696  66.197  81.454  1.00 16.12 ? 981  THR   A C     1 
ATOM   7188  O  O     . THR   A  1  983  ? -9.191  67.087  82.143  1.00 16.42 ? 981  THR   A O     1 
ATOM   7189  C  CB    . THR   A  1  983  ? -10.741 66.748  79.217  1.00 17.07 ? 981  THR   A CB    1 
ATOM   7190  O  OG1   . THR   A  1  983  ? -10.448 66.851  77.820  1.00 18.51 ? 981  THR   A OG1   1 
ATOM   7191  C  CG2   . THR   A  1  983  ? -11.132 68.123  79.739  1.00 17.75 ? 981  THR   A CG2   1 
ATOM   7192  N  N     . ILE   A  1  984  ? -10.369 65.179  81.991  1.00 15.22 ? 982  ILE   A N     1 
ATOM   7193  C  CA    . ILE   A  1  984  ? -10.525 65.089  83.441  1.00 15.81 ? 982  ILE   A CA    1 
ATOM   7194  C  C     . ILE   A  1  984  ? -9.164  64.996  84.106  1.00 16.42 ? 982  ILE   A C     1 
ATOM   7195  O  O     . ILE   A  1  984  ? -8.882  65.697  85.086  1.00 15.52 ? 982  ILE   A O     1 
ATOM   7196  C  CB    . ILE   A  1  984  ? -11.395 63.883  83.819  1.00 15.46 ? 982  ILE   A CB    1 
ATOM   7197  C  CG1   . ILE   A  1  984  ? -12.819 64.097  83.329  1.00 16.91 ? 982  ILE   A CG1   1 
ATOM   7198  C  CG2   . ILE   A  1  984  ? -11.380 63.667  85.332  1.00 18.16 ? 982  ILE   A CG2   1 
ATOM   7199  C  CD1   . ILE   A  1  984  ? -13.686 62.867  83.435  1.00 18.62 ? 982  ILE   A CD1   1 
ATOM   7200  N  N     . ALA   A  1  985  ? -8.306  64.118  83.584  1.00 15.33 ? 983  ALA   A N     1 
ATOM   7201  C  CA    . ALA   A  1  985  ? -6.999  63.910  84.200  1.00 16.70 ? 983  ALA   A CA    1 
ATOM   7202  C  C     . ALA   A  1  985  ? -6.180  65.187  84.140  1.00 16.65 ? 983  ALA   A C     1 
ATOM   7203  O  O     . ALA   A  1  985  ? -5.559  65.588  85.129  1.00 16.63 ? 983  ALA   A O     1 
ATOM   7204  C  CB    . ALA   A  1  985  ? -6.272  62.763  83.496  1.00 17.22 ? 983  ALA   A CB    1 
ATOM   7205  N  N     . HIS   A  1  986  ? -6.175  65.840  82.984  1.00 16.44 ? 984  HIS   A N     1 
ATOM   7206  C  CA    . HIS   A  1  986  ? -5.428  67.078  82.815  1.00 19.01 ? 984  HIS   A CA    1 
ATOM   7207  C  C     . HIS   A  1  986  ? -5.934  68.144  83.770  1.00 16.71 ? 984  HIS   A C     1 
ATOM   7208  O  O     . HIS   A  1  986  ? -5.180  68.686  84.582  1.00 17.66 ? 984  HIS   A O     1 
ATOM   7209  C  CB    . HIS   A  1  986  ? -5.573  67.534  81.365  1.00 17.41 ? 984  HIS   A CB    1 
ATOM   7210  C  CG    . HIS   A  1  986  ? -5.034  68.902  81.081  1.00 19.50 ? 984  HIS   A CG    1 
ATOM   7211  N  ND1   . HIS   A  1  986  ? -5.245  69.538  79.879  1.00 25.16 ? 984  HIS   A ND1   1 
ATOM   7212  C  CD2   . HIS   A  1  986  ? -4.272  69.743  81.821  1.00 17.70 ? 984  HIS   A CD2   1 
ATOM   7213  C  CE1   . HIS   A  1  986  ? -4.650  70.718  79.896  1.00 26.36 ? 984  HIS   A CE1   1 
ATOM   7214  N  NE2   . HIS   A  1  986  ? -4.065  70.873  81.068  1.00 21.17 ? 984  HIS   A NE2   1 
ATOM   7215  N  N     . VAL   A  1  987  ? -7.226  68.435  83.704  1.00 17.19 ? 985  VAL   A N     1 
ATOM   7216  C  CA    . VAL   A  1  987  ? -7.762  69.557  84.461  1.00 16.52 ? 985  VAL   A CA    1 
ATOM   7217  C  C     . VAL   A  1  987  ? -7.655  69.310  85.958  1.00 18.73 ? 985  VAL   A C     1 
ATOM   7218  O  O     . VAL   A  1  987  ? -7.254  70.201  86.714  1.00 16.54 ? 985  VAL   A O     1 
ATOM   7219  C  CB    . VAL   A  1  987  ? -9.203  69.851  84.030  1.00 14.84 ? 985  VAL   A CB    1 
ATOM   7220  C  CG1   . VAL   A  1  987  ? -9.805  70.890  84.954  1.00 17.09 ? 985  VAL   A CG1   1 
ATOM   7221  C  CG2   . VAL   A  1  987  ? -9.204  70.360  82.611  1.00 18.12 ? 985  VAL   A CG2   1 
ATOM   7222  N  N     . THR   A  1  988  ? -8.012  68.109  86.420  1.00 17.18 ? 986  THR   A N     1 
ATOM   7223  C  CA    . THR   A  1  988  ? -7.992  67.892  87.866  1.00 17.34 ? 986  THR   A CA    1 
ATOM   7224  C  C     . THR   A  1  988  ? -6.572  67.839  88.410  1.00 21.85 ? 986  THR   A C     1 
ATOM   7225  O  O     . THR   A  1  988  ? -6.357  68.111  89.599  1.00 23.09 ? 986  THR   A O     1 
ATOM   7226  C  CB    . THR   A  1  988  ? -8.764  66.637  88.267  1.00 19.26 ? 986  THR   A CB    1 
ATOM   7227  O  OG1   . THR   A  1  988  ? -8.142  65.489  87.688  1.00 20.28 ? 986  THR   A OG1   1 
ATOM   7228  C  CG2   . THR   A  1  988  ? -10.220 66.727  87.808  1.00 19.51 ? 986  THR   A CG2   1 
ATOM   7229  N  N     . SER   A  1  989  ? -5.594  67.493  87.576  1.00 18.17 ? 987  SER   A N     1 
ATOM   7230  C  CA    . SER   A  1  989  ? -4.217  67.483  88.047  1.00 21.77 ? 987  SER   A CA    1 
ATOM   7231  C  C     . SER   A  1  989  ? -3.650  68.894  88.134  1.00 22.08 ? 987  SER   A C     1 
ATOM   7232  O  O     . SER   A  1  989  ? -2.764  69.153  88.956  1.00 28.57 ? 987  SER   A O     1 
ATOM   7233  C  CB    . SER   A  1  989  ? -3.349  66.586  87.158  1.00 24.44 ? 987  SER   A CB    1 
ATOM   7234  O  OG    . SER   A  1  989  ? -3.166  67.136  85.868  1.00 30.86 ? 987  SER   A OG    1 
ATOM   7235  N  N     . ARG   A  1  990  ? -4.160  69.817  87.329  1.00 17.12 ? 988  ARG   A N     1 
ATOM   7236  C  CA    . ARG   A  1  990  ? -3.603  71.160  87.241  1.00 19.98 ? 988  ARG   A CA    1 
ATOM   7237  C  C     . ARG   A  1  990  ? -4.366  72.183  88.061  1.00 19.63 ? 988  ARG   A C     1 
ATOM   7238  O  O     . ARG   A  1  990  ? -3.765  73.164  88.509  1.00 20.16 ? 988  ARG   A O     1 
ATOM   7239  C  CB    . ARG   A  1  990  ? -3.549  71.614  85.782  1.00 22.20 ? 988  ARG   A CB    1 
ATOM   7240  C  CG    . ARG   A  1  990  ? -2.786  70.647  84.893  1.00 28.49 ? 988  ARG   A CG    1 
ATOM   7241  C  CD    . ARG   A  1  990  ? -1.298  70.839  85.006  1.00 30.91 ? 988  ARG   A CD    1 
ATOM   7242  N  NE    . ARG   A  1  990  ? -0.828  71.807  84.027  1.00 28.03 ? 988  ARG   A NE    1 
ATOM   7243  C  CZ    . ARG   A  1  990  ? 0.421   72.243  83.951  1.00 26.95 ? 988  ARG   A CZ    1 
ATOM   7244  N  NH1   . ARG   A  1  990  ? 1.335   71.878  84.836  1.00 31.96 ? 988  ARG   A NH1   1 
ATOM   7245  N  NH2   . ARG   A  1  990  ? 0.758   73.065  82.962  1.00 27.63 ? 988  ARG   A NH2   1 
ATOM   7246  N  N     . ILE   A  1  991  ? -5.672  71.987  88.260  1.00 16.96 ? 989  ILE   A N     1 
ATOM   7247  C  CA    . ILE   A  1  991  ? -6.445  72.915  89.071  1.00 17.46 ? 989  ILE   A CA    1 
ATOM   7248  C  C     . ILE   A  1  991  ? -5.968  72.846  90.514  1.00 17.92 ? 989  ILE   A C     1 
ATOM   7249  O  O     . ILE   A  1  991  ? -5.546  71.795  91.008  1.00 18.32 ? 989  ILE   A O     1 
ATOM   7250  C  CB    . ILE   A  1  991  ? -7.950  72.604  88.950  1.00 16.69 ? 989  ILE   A CB    1 
ATOM   7251  C  CG1   . ILE   A  1  991  ? -8.782  73.752  89.520  1.00 20.32 ? 989  ILE   A CG1   1 
ATOM   7252  C  CG2   . ILE   A  1  991  ? -8.279  71.309  89.655  1.00 17.57 ? 989  ILE   A CG2   1 
ATOM   7253  C  CD1   . ILE   A  1  991  ? -8.715  75.008  88.694  1.00 21.59 ? 989  ILE   A CD1   1 
ATOM   7254  N  N     . LYS   A  1  992  ? -6.035  73.977  91.202  1.00 18.05 ? 990  LYS   A N     1 
ATOM   7255  C  CA    . LYS   A  1  992  ? -5.656  74.058  92.608  1.00 19.00 ? 990  LYS   A CA    1 
ATOM   7256  C  C     . LYS   A  1  992  ? -6.863  74.571  93.386  1.00 16.71 ? 990  LYS   A C     1 
ATOM   7257  O  O     . LYS   A  1  992  ? -6.994  75.772  93.635  1.00 19.81 ? 990  LYS   A O     1 
ATOM   7258  C  CB    . LYS   A  1  992  ? -4.454  74.962  92.792  1.00 20.10 ? 990  LYS   A CB    1 
ATOM   7259  C  CG    . LYS   A  1  992  ? -3.205  74.512  92.047  1.00 22.66 ? 990  LYS   A CG    1 
ATOM   7260  C  CD    . LYS   A  1  992  ? -2.119  75.583  92.178  1.00 31.35 ? 990  LYS   A CD    1 
ATOM   7261  C  CE    . LYS   A  1  992  ? -0.831  75.189  91.463  1.00 39.25 ? 990  LYS   A CE    1 
ATOM   7262  N  NZ    . LYS   A  1  992  ? 0.213   76.257  91.564  1.00 47.28 ? 990  LYS   A NZ    1 
ATOM   7263  N  N     . ALA   A  1  993  ? -7.733  73.653  93.784  1.00 16.96 ? 991  ALA   A N     1 
ATOM   7264  C  CA    . ALA   A  1  993  ? -8.919  74.006  94.552  1.00 15.80 ? 991  ALA   A CA    1 
ATOM   7265  C  C     . ALA   A  1  993  ? -9.256  72.856  95.476  1.00 17.76 ? 991  ALA   A C     1 
ATOM   7266  O  O     . ALA   A  1  993  ? -8.950  71.694  95.197  1.00 18.77 ? 991  ALA   A O     1 
ATOM   7267  C  CB    . ALA   A  1  993  ? -10.129 74.298  93.657  1.00 16.61 ? 991  ALA   A CB    1 
ATOM   7268  N  N     . GLY   A  1  994  ? -9.957  73.185  96.561  1.00 15.63 ? 992  GLY   A N     1 
ATOM   7269  C  CA    . GLY   A  1  994  ? -10.192 72.201  97.596  1.00 16.75 ? 992  GLY   A CA    1 
ATOM   7270  C  C     . GLY   A  1  994  ? -11.338 71.257  97.317  1.00 14.84 ? 992  GLY   A C     1 
ATOM   7271  O  O     . GLY   A  1  994  ? -11.346 70.138  97.823  1.00 15.21 ? 992  GLY   A O     1 
ATOM   7272  N  N     . ASN   A  1  995  ? -12.317 71.678  96.521  1.00 14.88 ? 993  ASN   A N     1 
ATOM   7273  C  CA    . ASN   A  1  995  ? -13.497 70.865  96.259  1.00 15.30 ? 993  ASN   A CA    1 
ATOM   7274  C  C     . ASN   A  1  995  ? -13.726 70.861  94.764  1.00 15.12 ? 993  ASN   A C     1 
ATOM   7275  O  O     . ASN   A  1  995  ? -14.029 71.901  94.176  1.00 15.39 ? 993  ASN   A O     1 
ATOM   7276  C  CB    . ASN   A  1  995  ? -14.715 71.403  96.999  1.00 15.29 ? 993  ASN   A CB    1 
ATOM   7277  C  CG    . ASN   A  1  995  ? -14.727 70.983  98.431  1.00 16.33 ? 993  ASN   A CG    1 
ATOM   7278  O  OD1   . ASN   A  1  995  ? -14.094 71.614  99.273  1.00 16.60 ? 993  ASN   A OD1   1 
ATOM   7279  N  ND2   . ASN   A  1  995  ? -15.409 69.887  98.717  1.00 17.40 ? 993  ASN   A ND2   1 
ATOM   7280  N  N     . LEU   A  1  996  ? -13.555 69.701  94.157  1.00 14.52 ? 994  LEU   A N     1 
ATOM   7281  C  CA    . LEU   A  1  996  ? -13.723 69.546  92.725  1.00 14.97 ? 994  LEU   A CA    1 
ATOM   7282  C  C     . LEU   A  1  996  ? -14.991 68.759  92.464  1.00 14.01 ? 994  LEU   A C     1 
ATOM   7283  O  O     . LEU   A  1  996  ? -15.347 67.862  93.229  1.00 14.51 ? 994  LEU   A O     1 
ATOM   7284  C  CB    . LEU   A  1  996  ? -12.546 68.773  92.120  1.00 15.21 ? 994  LEU   A CB    1 
ATOM   7285  C  CG    . LEU   A  1  996  ? -11.151 69.182  92.589  1.00 15.92 ? 994  LEU   A CG    1 
ATOM   7286  C  CD1   . LEU   A  1  996  ? -10.077 68.352  91.890  1.00 19.89 ? 994  LEU   A CD1   1 
ATOM   7287  C  CD2   . LEU   A  1  996  ? -10.948 70.669  92.345  1.00 17.37 ? 994  LEU   A CD2   1 
ATOM   7288  N  N     . TYR   A  1  997  ? -15.651 69.080  91.353  1.00 14.75 ? 995  TYR   A N     1 
ATOM   7289  C  CA    . TYR   A  1  997  ? -16.918 68.453  91.013  1.00 14.69 ? 995  TYR   A CA    1 
ATOM   7290  C  C     . TYR   A  1  997  ? -16.903 68.171  89.529  1.00 14.10 ? 995  TYR   A C     1 
ATOM   7291  O  O     . TYR   A  1  997  ? -16.614 69.065  88.732  1.00 16.26 ? 995  TYR   A O     1 
ATOM   7292  C  CB    . TYR   A  1  997  ? -18.078 69.383  91.332  1.00 16.03 ? 995  TYR   A CB    1 
ATOM   7293  C  CG    . TYR   A  1  997  ? -18.108 69.795  92.767  1.00 15.50 ? 995  TYR   A CG    1 
ATOM   7294  C  CD1   . TYR   A  1  997  ? -18.774 69.033  93.701  1.00 16.51 ? 995  TYR   A CD1   1 
ATOM   7295  C  CD2   . TYR   A  1  997  ? -17.429 70.931  93.186  1.00 16.28 ? 995  TYR   A CD2   1 
ATOM   7296  C  CE1   . TYR   A  1  997  ? -18.795 69.415  95.029  1.00 17.10 ? 995  TYR   A CE1   1 
ATOM   7297  C  CE2   . TYR   A  1  997  ? -17.442 71.323  94.506  1.00 19.59 ? 995  TYR   A CE2   1 
ATOM   7298  C  CZ    . TYR   A  1  997  ? -18.124 70.557  95.413  1.00 18.78 ? 995  TYR   A CZ    1 
ATOM   7299  O  OH    . TYR   A  1  997  ? -18.144 70.940  96.738  1.00 22.56 ? 995  TYR   A OH    1 
ATOM   7300  N  N     . ILE   A  1  998  ? -17.165 66.927  89.171  1.00 13.55 ? 996  ILE   A N     1 
ATOM   7301  C  CA    A ILE   A  1  998  ? -17.102 66.479  87.786  0.43 14.71 ? 996  ILE   A CA    1 
ATOM   7302  C  CA    B ILE   A  1  998  ? -17.106 66.494  87.783  0.57 14.70 ? 996  ILE   A CA    1 
ATOM   7303  C  C     . ILE   A  1  998  ? -18.511 66.109  87.351  1.00 14.76 ? 996  ILE   A C     1 
ATOM   7304  O  O     . ILE   A  1  998  ? -19.120 65.203  87.925  1.00 14.92 ? 996  ILE   A O     1 
ATOM   7305  C  CB    A ILE   A  1  998  ? -16.151 65.284  87.624  0.43 16.50 ? 996  ILE   A CB    1 
ATOM   7306  C  CB    B ILE   A  1  998  ? -16.112 65.341  87.590  0.57 16.50 ? 996  ILE   A CB    1 
ATOM   7307  C  CG1   A ILE   A  1  998  ? -14.809 65.562  88.302  0.43 17.85 ? 996  ILE   A CG1   1 
ATOM   7308  C  CG1   B ILE   A  1  998  ? -14.691 65.814  87.895  0.57 17.89 ? 996  ILE   A CG1   1 
ATOM   7309  C  CG2   A ILE   A  1  998  ? -15.944 64.973  86.145  0.43 15.87 ? 996  ILE   A CG2   1 
ATOM   7310  C  CG2   B ILE   A  1  998  ? -16.190 64.799  86.167  0.57 15.91 ? 996  ILE   A CG2   1 
ATOM   7311  C  CD1   A ILE   A  1  998  ? -14.037 66.686  87.663  0.43 17.33 ? 996  ILE   A CD1   1 
ATOM   7312  C  CD1   B ILE   A  1  998  ? -13.683 64.701  87.916  0.57 19.75 ? 996  ILE   A CD1   1 
ATOM   7313  N  N     . ASN   A  1  999  ? -19.008 66.805  86.325  1.00 14.00 ? 997  ASN   A N     1 
ATOM   7314  C  CA    . ASN   A  1  999  ? -20.299 66.505  85.700  1.00 14.26 ? 997  ASN   A CA    1 
ATOM   7315  C  C     . ASN   A  1  999  ? -21.472 66.653  86.654  1.00 14.47 ? 997  ASN   A C     1 
ATOM   7316  O  O     . ASN   A  1  999  ? -22.454 65.912  86.575  1.00 15.74 ? 997  ASN   A O     1 
ATOM   7317  C  CB    . ASN   A  1  999  ? -20.275 65.140  85.030  1.00 14.08 ? 997  ASN   A CB    1 
ATOM   7318  C  CG    . ASN   A  1  999  ? -19.334 65.121  83.870  1.00 14.16 ? 997  ASN   A CG    1 
ATOM   7319  O  OD1   . ASN   A  1  999  ? -19.143 66.151  83.222  1.00 15.83 ? 997  ASN   A OD1   1 
ATOM   7320  N  ND2   . ASN   A  1  999  ? -18.727 63.974  83.599  1.00 16.63 ? 997  ASN   A ND2   1 
ATOM   7321  N  N     . ARG   A  1  1000 ? -21.381 67.646  87.529  1.00 14.52 ? 998  ARG   A N     1 
ATOM   7322  C  CA    . ARG   A  1  1000 ? -22.449 67.948  88.474  1.00 14.47 ? 998  ARG   A CA    1 
ATOM   7323  C  C     . ARG   A  1  1000 ? -22.305 69.407  88.881  1.00 16.74 ? 998  ARG   A C     1 
ATOM   7324  O  O     . ARG   A  1  1000 ? -21.405 70.114  88.421  1.00 17.28 ? 998  ARG   A O     1 
ATOM   7325  C  CB    . ARG   A  1  1000 ? -22.401 67.009  89.681  1.00 14.56 ? 998  ARG   A CB    1 
ATOM   7326  C  CG    . ARG   A  1  1000 ? -21.010 66.909  90.297  1.00 15.49 ? 998  ARG   A CG    1 
ATOM   7327  C  CD    . ARG   A  1  1000 ? -21.098 66.548  91.752  1.00 16.42 ? 998  ARG   A CD    1 
ATOM   7328  N  NE    . ARG   A  1  1000 ? -21.692 67.633  92.518  1.00 14.22 ? 998  ARG   A NE    1 
ATOM   7329  C  CZ    . ARG   A  1  1000 ? -22.018 67.544  93.797  1.00 16.33 ? 998  ARG   A CZ    1 
ATOM   7330  N  NH1   . ARG   A  1  1000 ? -21.767 66.447  94.501  1.00 17.25 ? 998  ARG   A NH1   1 
ATOM   7331  N  NH2   . ARG   A  1  1000 ? -22.586 68.587  94.391  1.00 17.17 ? 998  ARG   A NH2   1 
ATOM   7332  N  N     . ASN   A  1  1001 ? -23.212 69.868  89.739  1.00 15.22 ? 999  ASN   A N     1 
ATOM   7333  C  CA    . ASN   A  1  1001 ? -23.061 71.224  90.236  1.00 14.79 ? 999  ASN   A CA    1 
ATOM   7334  C  C     . ASN   A  1  1001 ? -21.881 71.291  91.208  1.00 16.76 ? 999  ASN   A C     1 
ATOM   7335  O  O     . ASN   A  1  1001 ? -21.299 70.279  91.589  1.00 16.64 ? 999  ASN   A O     1 
ATOM   7336  C  CB    . ASN   A  1  1001 ? -24.370 71.729  90.861  1.00 17.29 ? 999  ASN   A CB    1 
ATOM   7337  C  CG    . ASN   A  1  1001 ? -24.724 71.026  92.145  1.00 18.55 ? 999  ASN   A CG    1 
ATOM   7338  O  OD1   . ASN   A  1  1001 ? -23.886 70.815  93.013  1.00 19.02 ? 999  ASN   A OD1   1 
ATOM   7339  N  ND2   . ASN   A  1  1001 ? -26.002 70.703  92.298  1.00 24.31 ? 999  ASN   A ND2   1 
ATOM   7340  N  N     . ILE   A  1  1002 ? -21.541 72.504  91.620  1.00 15.07 ? 1000 ILE   A N     1 
ATOM   7341  C  CA    . ILE   A  1  1002 ? -20.361 72.697  92.448  1.00 16.80 ? 1000 ILE   A CA    1 
ATOM   7342  C  C     . ILE   A  1  1002 ? -20.724 73.151  93.854  1.00 17.34 ? 1000 ILE   A C     1 
ATOM   7343  O  O     . ILE   A  1  1002 ? -19.873 73.684  94.563  1.00 18.42 ? 1000 ILE   A O     1 
ATOM   7344  C  CB    . ILE   A  1  1002 ? -19.343 73.636  91.792  1.00 15.89 ? 1000 ILE   A CB    1 
ATOM   7345  C  CG1   . ILE   A  1  1002 ? -19.871 75.075  91.730  1.00 16.85 ? 1000 ILE   A CG1   1 
ATOM   7346  C  CG2   . ILE   A  1  1002 ? -18.953 73.112  90.418  1.00 15.87 ? 1000 ILE   A CG2   1 
ATOM   7347  C  CD1   . ILE   A  1  1002 ? -18.826 76.064  91.253  1.00 17.28 ? 1000 ILE   A CD1   1 
ATOM   7348  N  N     A ILE   A  1  1003 ? -21.964 72.976  94.275  0.46 17.09 ? 1001 ILE   A N     1 
ATOM   7349  N  N     B ILE   A  1  1003 ? -21.971 72.914  94.278  0.54 17.04 ? 1001 ILE   A N     1 
ATOM   7350  C  CA    A ILE   A  1  1003 ? -22.365 73.468  95.579  0.46 18.75 ? 1001 ILE   A CA    1 
ATOM   7351  C  CA    B ILE   A  1  1003 ? -22.503 73.443  95.530  0.54 18.78 ? 1001 ILE   A CA    1 
ATOM   7352  C  C     A ILE   A  1  1003 ? -22.381 72.356  96.629  0.46 21.19 ? 1001 ILE   A C     1 
ATOM   7353  C  C     B ILE   A  1  1003 ? -23.138 72.321  96.348  0.54 18.19 ? 1001 ILE   A C     1 
ATOM   7354  O  O     A ILE   A  1  1003 ? -22.890 72.555  97.733  0.46 20.54 ? 1001 ILE   A O     1 
ATOM   7355  O  O     B ILE   A  1  1003 ? -23.287 71.188  95.895  0.54 19.18 ? 1001 ILE   A O     1 
ATOM   7356  C  CB    A ILE   A  1  1003 ? -23.674 74.268  95.520  0.46 18.16 ? 1001 ILE   A CB    1 
ATOM   7357  C  CB    B ILE   A  1  1003 ? -23.518 74.585  95.316  0.54 17.98 ? 1001 ILE   A CB    1 
ATOM   7358  C  CG1   A ILE   A  1  1003 ? -24.793 73.432  94.906  0.46 18.51 ? 1001 ILE   A CG1   1 
ATOM   7359  C  CG1   B ILE   A  1  1003 ? -24.764 74.066  94.600  0.54 17.15 ? 1001 ILE   A CG1   1 
ATOM   7360  C  CG2   A ILE   A  1  1003 ? -23.457 75.548  94.719  0.46 18.88 ? 1001 ILE   A CG2   1 
ATOM   7361  C  CG2   B ILE   A  1  1003 ? -22.894 75.734  94.545  0.54 17.41 ? 1001 ILE   A CG2   1 
ATOM   7362  C  CD1   A ILE   A  1  1003 ? -26.145 74.103  94.990  0.46 21.15 ? 1001 ILE   A CD1   1 
ATOM   7363  C  CD1   B ILE   A  1  1003 ? -25.966 74.995  94.717  0.54 20.24 ? 1001 ILE   A CD1   1 
ATOM   7364  N  N     A GLY   A  1  1004 ? -21.791 71.206  96.316  0.46 20.59 ? 1002 GLY   A N     1 
ATOM   7365  N  N     B GLY   A  1  1004 ? -23.509 72.661  97.578  0.54 19.59 ? 1002 GLY   A N     1 
ATOM   7366  C  CA    A GLY   A  1  1004 ? -21.784 70.074  97.219  0.46 18.01 ? 1002 GLY   A CA    1 
ATOM   7367  C  CA    B GLY   A  1  1004 ? -24.109 71.692  98.479  0.54 20.43 ? 1002 GLY   A CA    1 
ATOM   7368  C  C     A GLY   A  1  1004 ? -20.870 70.241  98.410  0.46 17.70 ? 1002 GLY   A C     1 
ATOM   7369  C  C     B GLY   A  1  1004 ? -23.205 70.555  98.913  0.54 18.44 ? 1002 GLY   A C     1 
ATOM   7370  O  O     A GLY   A  1  1004 ? -19.669 70.464  98.270  0.46 19.17 ? 1002 GLY   A O     1 
ATOM   7371  O  O     B GLY   A  1  1004 ? -23.659 69.404  98.978  0.54 20.50 ? 1002 GLY   A O     1 
ATOM   7372  N  N     A ALA   A  1  1005 ? -21.441 70.145  99.602  0.46 16.98 ? 1003 ALA   A N     1 
ATOM   7373  N  N     B ALA   A  1  1005 ? -21.940 70.846  99.218  0.54 18.99 ? 1003 ALA   A N     1 
ATOM   7374  C  CA    A ALA   A  1  1005 ? -20.649 70.178  100.821 0.46 18.47 ? 1003 ALA   A CA    1 
ATOM   7375  C  CA    B ALA   A  1  1005 ? -21.035 69.819  99.716  0.54 17.15 ? 1003 ALA   A CA    1 
ATOM   7376  C  C     A ALA   A  1  1005 ? -21.137 69.126  101.796 0.46 19.50 ? 1003 ALA   A C     1 
ATOM   7377  C  C     B ALA   A  1  1005 ? -21.623 69.145  100.950 0.54 18.82 ? 1003 ALA   A C     1 
ATOM   7378  O  O     A ALA   A  1  1005 ? -21.150 69.359  103.009 0.46 18.31 ? 1003 ALA   A O     1 
ATOM   7379  O  O     B ALA   A  1  1005 ? -22.208 69.798  101.819 0.54 21.17 ? 1003 ALA   A O     1 
ATOM   7380  C  CB    A ALA   A  1  1005 ? -20.678 71.553  101.485 0.46 17.98 ? 1003 ALA   A CB    1 
ATOM   7381  C  CB    B ALA   A  1  1005 ? -19.686 70.440  100.080 0.54 19.18 ? 1003 ALA   A CB    1 
ATOM   7382  N  N     A VAL   A  1  1006 ? -21.563 67.976  101.276 0.46 18.24 ? 1004 VAL   A N     1 
ATOM   7383  N  N     B VAL   A  1  1006 ? -21.456 67.827  101.024 0.54 18.59 ? 1004 VAL   A N     1 
ATOM   7384  C  CA    A VAL   A  1  1006 ? -22.127 66.909  102.092 0.46 17.78 ? 1004 VAL   A CA    1 
ATOM   7385  C  CA    B VAL   A  1  1006 ? -22.057 67.002  102.065 0.54 17.80 ? 1004 VAL   A CA    1 
ATOM   7386  C  C     A VAL   A  1  1006 ? -21.089 66.479  103.113 0.46 17.95 ? 1004 VAL   A C     1 
ATOM   7387  C  C     B VAL   A  1  1006 ? -21.000 66.660  103.104 0.54 18.11 ? 1004 VAL   A C     1 
ATOM   7388  O  O     A VAL   A  1  1006 ? -20.050 65.906  102.767 0.46 16.45 ? 1004 VAL   A O     1 
ATOM   7389  O  O     B VAL   A  1  1006 ? -19.867 66.301  102.765 0.54 17.07 ? 1004 VAL   A O     1 
ATOM   7390  C  CB    A VAL   A  1  1006 ? -22.606 65.726  101.235 0.46 17.64 ? 1004 VAL   A CB    1 
ATOM   7391  C  CB    B VAL   A  1  1006 ? -22.675 65.731  101.452 0.54 17.65 ? 1004 VAL   A CB    1 
ATOM   7392  C  CG1   A VAL   A  1  1006 ? -23.135 64.618  102.131 0.46 19.45 ? 1004 VAL   A CG1   1 
ATOM   7393  C  CG1   B VAL   A  1  1006 ? -23.144 64.781  102.543 0.54 19.28 ? 1004 VAL   A CG1   1 
ATOM   7394  C  CG2   A VAL   A  1  1006 ? -23.678 66.186  100.245 0.46 18.14 ? 1004 VAL   A CG2   1 
ATOM   7395  C  CG2   B VAL   A  1  1006 ? -23.829 66.101  100.520 0.54 18.16 ? 1004 VAL   A CG2   1 
ATOM   7396  N  N     . VAL   A  1  1007 ? -21.369 66.781  104.378 1.00 16.97 ? 1005 VAL   A N     1 
ATOM   7397  C  CA    . VAL   A  1  1007 ? -20.429 66.518  105.457 1.00 17.15 ? 1005 VAL   A CA    1 
ATOM   7398  C  C     . VAL   A  1  1007 ? -19.942 65.078  105.392 1.00 16.93 ? 1005 VAL   A C     1 
ATOM   7399  O  O     . VAL   A  1  1007 ? -20.734 64.143  105.244 1.00 18.62 ? 1005 VAL   A O     1 
ATOM   7400  C  CB    . VAL   A  1  1007 ? -21.126 66.822  106.793 1.00 17.00 ? 1005 VAL   A CB    1 
ATOM   7401  C  CG1   . VAL   A  1  1007 ? -20.246 66.417  107.949 1.00 18.82 ? 1005 VAL   A CG1   1 
ATOM   7402  C  CG2   . VAL   A  1  1007 ? -21.454 68.289  106.873 1.00 19.59 ? 1005 VAL   A CG2   1 
ATOM   7403  N  N     . GLY   A  1  1008 ? -18.621 64.889  105.510 1.00 17.21 ? 1006 GLY   A N     1 
ATOM   7404  C  CA    . GLY   A  1  1008 ? -18.072 63.552  105.501 1.00 17.46 ? 1006 GLY   A CA    1 
ATOM   7405  C  C     . GLY   A  1  1008 ? -18.090 62.868  104.157 1.00 17.80 ? 1006 GLY   A C     1 
ATOM   7406  O  O     . GLY   A  1  1008 ? -17.646 61.719  104.057 1.00 20.29 ? 1006 GLY   A O     1 
ATOM   7407  N  N     . VAL   A  1  1009 ? -18.593 63.533  103.124 1.00 17.13 ? 1007 VAL   A N     1 
ATOM   7408  C  CA    . VAL   A  1  1009 ? -18.681 62.987  101.777 1.00 18.31 ? 1007 VAL   A CA    1 
ATOM   7409  C  C     . VAL   A  1  1009 ? -17.944 63.872  100.790 1.00 17.63 ? 1007 VAL   A C     1 
ATOM   7410  O  O     . VAL   A  1  1009 ? -17.106 63.397  100.018 1.00 17.33 ? 1007 VAL   A O     1 
ATOM   7411  C  CB    . VAL   A  1  1009 ? -20.148 62.780  101.348 1.00 17.72 ? 1007 VAL   A CB    1 
ATOM   7412  C  CG1   . VAL   A  1  1009 ? -20.212 62.168  99.969  1.00 18.42 ? 1007 VAL   A CG1   1 
ATOM   7413  C  CG2   . VAL   A  1  1009 ? -20.851 61.875  102.333 1.00 19.44 ? 1007 VAL   A CG2   1 
ATOM   7414  N  N     . GLN   A  1  1010 ? -18.209 65.175  100.834 1.00 17.38 ? 1008 GLN   A N     1 
ATOM   7415  C  CA    . GLN   A  1  1010 ? -17.330 66.184  100.255 1.00 18.09 ? 1008 GLN   A CA    1 
ATOM   7416  C  C     . GLN   A  1  1010 ? -16.888 67.078  101.405 1.00 16.75 ? 1008 GLN   A C     1 
ATOM   7417  O  O     . GLN   A  1  1010 ? -17.428 68.178  101.583 1.00 19.51 ? 1008 GLN   A O     1 
ATOM   7418  C  CB    . GLN   A  1  1010 ? -18.010 66.997  99.157  1.00 19.19 ? 1008 GLN   A CB    1 
ATOM   7419  C  CG    . GLN   A  1  1010 ? -18.540 66.139  98.020  1.00 16.92 ? 1008 GLN   A CG    1 
ATOM   7420  C  CD    . GLN   A  1  1010 ? -20.040 65.919  98.098  1.00 18.58 ? 1008 GLN   A CD    1 
ATOM   7421  O  OE1   . GLN   A  1  1010 ? -20.783 66.761  98.616  1.00 18.64 ? 1008 GLN   A OE1   1 
ATOM   7422  N  NE2   . GLN   A  1  1010 ? -20.493 64.782  97.581  1.00 18.82 ? 1008 GLN   A NE2   1 
ATOM   7423  N  N     . PRO   A  1  1011 ? -15.934 66.629  102.224 1.00 17.83 ? 1009 PRO   A N     1 
ATOM   7424  C  CA    . PRO   A  1  1011 ? -15.306 67.544  103.185 1.00 16.76 ? 1009 PRO   A CA    1 
ATOM   7425  C  C     . PRO   A  1  1011 ? -14.967 68.831  102.465 1.00 15.89 ? 1009 PRO   A C     1 
ATOM   7426  O  O     . PRO   A  1  1011 ? -14.463 68.816  101.338 1.00 15.73 ? 1009 PRO   A O     1 
ATOM   7427  C  CB    . PRO   A  1  1011 ? -14.043 66.793  103.605 1.00 16.72 ? 1009 PRO   A CB    1 
ATOM   7428  C  CG    . PRO   A  1  1011 ? -14.430 65.359  103.481 1.00 18.22 ? 1009 PRO   A CG    1 
ATOM   7429  C  CD    . PRO   A  1  1011 ? -15.291 65.304  102.234 1.00 16.92 ? 1009 PRO   A CD    1 
ATOM   7430  N  N     . PHE   A  1  1012 ? -15.322 69.949  103.072 1.00 16.32 ? 1010 PHE   A N     1 
ATOM   7431  C  CA    . PHE   A  1  1012 ? -15.415 71.193  102.336 1.00 16.02 ? 1010 PHE   A CA    1 
ATOM   7432  C  C     . PHE   A  1  1012 ? -14.386 72.186  102.836 1.00 17.77 ? 1010 PHE   A C     1 
ATOM   7433  O  O     . PHE   A  1  1012 ? -14.251 72.396  104.045 1.00 18.52 ? 1010 PHE   A O     1 
ATOM   7434  C  CB    . PHE   A  1  1012 ? -16.811 71.810  102.452 1.00 15.53 ? 1010 PHE   A CB    1 
ATOM   7435  C  CG    . PHE   A  1  1012 ? -16.977 73.012  101.593 1.00 16.15 ? 1010 PHE   A CG    1 
ATOM   7436  C  CD1   . PHE   A  1  1012 ? -17.257 72.868  100.247 1.00 17.67 ? 1010 PHE   A CD1   1 
ATOM   7437  C  CD2   . PHE   A  1  1012 ? -16.833 74.291  102.117 1.00 17.28 ? 1010 PHE   A CD2   1 
ATOM   7438  C  CE1   . PHE   A  1  1012 ? -17.386 73.973  99.424  1.00 18.43 ? 1010 PHE   A CE1   1 
ATOM   7439  C  CE2   . PHE   A  1  1012 ? -16.970 75.412  101.296 1.00 18.32 ? 1010 PHE   A CE2   1 
ATOM   7440  C  CZ    . PHE   A  1  1012 ? -17.259 75.251  99.952  1.00 18.15 ? 1010 PHE   A CZ    1 
ATOM   7441  N  N     . GLY   A  1  1013 ? -13.699 72.815  101.910 1.00 18.15 ? 1011 GLY   A N     1 
ATOM   7442  C  CA    . GLY   A  1  1013 ? -12.800 73.894  102.264 1.00 17.38 ? 1011 GLY   A CA    1 
ATOM   7443  C  C     . GLY   A  1  1013 ? -11.709 73.984  101.238 1.00 17.47 ? 1011 GLY   A C     1 
ATOM   7444  O  O     . GLY   A  1  1013 ? -11.303 72.995  100.638 1.00 17.94 ? 1011 GLY   A O     1 
ATOM   7445  N  N     . GLY   A  1  1014 ? -11.242 75.203  101.028 1.00 17.64 ? 1012 GLY   A N     1 
ATOM   7446  C  CA    . GLY   A  1  1014 ? -10.283 75.459  99.990  1.00 19.95 ? 1012 GLY   A CA    1 
ATOM   7447  C  C     . GLY   A  1  1014 ? -8.932  75.941  100.468 1.00 19.36 ? 1012 GLY   A C     1 
ATOM   7448  O  O     . GLY   A  1  1014 ? -8.582  75.868  101.651 1.00 19.97 ? 1012 GLY   A O     1 
ATOM   7449  N  N     . ARG   A  1  1015 ? -8.173  76.469  99.514  1.00 18.02 ? 1013 ARG   A N     1 
ATOM   7450  C  CA    . ARG   A  1  1015 ? -6.790  76.842  99.733  1.00 18.26 ? 1013 ARG   A CA    1 
ATOM   7451  C  C     . ARG   A  1  1015 ? -6.582  78.246  99.198  1.00 17.97 ? 1013 ARG   A C     1 
ATOM   7452  O  O     . ARG   A  1  1015 ? -7.489  78.861  98.640  1.00 18.14 ? 1013 ARG   A O     1 
ATOM   7453  C  CB    . ARG   A  1  1015 ? -5.860  75.880  98.990  1.00 18.47 ? 1013 ARG   A CB    1 
ATOM   7454  C  CG    . ARG   A  1  1015 ? -6.102  75.920  97.488  1.00 20.18 ? 1013 ARG   A CG    1 
ATOM   7455  C  CD    . ARG   A  1  1015 ? -5.010  75.221  96.701  1.00 21.80 ? 1013 ARG   A CD    1 
ATOM   7456  N  NE    . ARG   A  1  1015 ? -3.693  75.421  97.284  1.00 26.76 ? 1013 ARG   A NE    1 
ATOM   7457  C  CZ    . ARG   A  1  1015 ? -2.966  76.521  97.154  1.00 29.73 ? 1013 ARG   A CZ    1 
ATOM   7458  N  NH1   . ARG   A  1  1015 ? -3.385  77.545  96.425  1.00 28.11 ? 1013 ARG   A NH1   1 
ATOM   7459  N  NH2   . ARG   A  1  1015 ? -1.793  76.600  97.780  1.00 26.00 ? 1013 ARG   A NH2   1 
ATOM   7460  N  N     . GLY   A  1  1016 ? -5.355  78.742  99.345  1.00 19.55 ? 1014 GLY   A N     1 
ATOM   7461  C  CA    . GLY   A  1  1016 ? -5.076  80.088  98.887  1.00 20.67 ? 1014 GLY   A CA    1 
ATOM   7462  C  C     . GLY   A  1  1016 ? -5.936  81.092  99.628  1.00 18.25 ? 1014 GLY   A C     1 
ATOM   7463  O  O     . GLY   A  1  1016 ? -6.112  81.018  100.849 1.00 20.14 ? 1014 GLY   A O     1 
ATOM   7464  N  N     . LEU   A  1  1017 ? -6.511  82.031  98.874  1.00 18.72 ? 1015 LEU   A N     1 
ATOM   7465  C  CA    . LEU   A  1  1017 ? -7.388  83.039  99.456  1.00 20.06 ? 1015 LEU   A CA    1 
ATOM   7466  C  C     . LEU   A  1  1017 ? -8.682  82.448  99.988  1.00 18.63 ? 1015 LEU   A C     1 
ATOM   7467  O  O     . LEU   A  1  1017 ? -9.469  83.178  100.594 1.00 19.90 ? 1015 LEU   A O     1 
ATOM   7468  C  CB    . LEU   A  1  1017 ? -7.724  84.105  98.413  1.00 20.53 ? 1015 LEU   A CB    1 
ATOM   7469  C  CG    . LEU   A  1  1017 ? -6.550  84.911  97.875  1.00 22.01 ? 1015 LEU   A CG    1 
ATOM   7470  C  CD1   . LEU   A  1  1017 ? -7.009  85.822  96.746  1.00 22.84 ? 1015 LEU   A CD1   1 
ATOM   7471  C  CD2   . LEU   A  1  1017 ? -5.913  85.719  99.006  1.00 22.48 ? 1015 LEU   A CD2   1 
ATOM   7472  N  N     . SER   A  1  1018 ? -8.920  81.151  99.771  1.00 17.17 ? 1016 SER   A N     1 
ATOM   7473  C  CA    . SER   A  1  1018 ? -10.174 80.521  100.156 1.00 18.41 ? 1016 SER   A CA    1 
ATOM   7474  C  C     . SER   A  1  1018 ? -10.115 79.785  101.484 1.00 15.93 ? 1016 SER   A C     1 
ATOM   7475  O  O     . SER   A  1  1018 ? -11.163 79.354  101.970 1.00 18.41 ? 1016 SER   A O     1 
ATOM   7476  C  CB    . SER   A  1  1018 ? -10.623 79.533  99.074  1.00 18.41 ? 1016 SER   A CB    1 
ATOM   7477  O  OG    . SER   A  1  1018 ? -10.796 80.222  97.855  1.00 17.71 ? 1016 SER   A OG    1 
ATOM   7478  N  N     . GLY   A  1  1019 ? -8.944  79.602  102.075 1.00 17.98 ? 1017 GLY   A N     1 
ATOM   7479  C  CA    . GLY   A  1  1019 ? -8.955  78.885  103.325 1.00 18.33 ? 1017 GLY   A CA    1 
ATOM   7480  C  C     . GLY   A  1  1019 ? -7.585  78.537  103.836 1.00 18.90 ? 1017 GLY   A C     1 
ATOM   7481  O  O     . GLY   A  1  1019 ? -6.630  78.433  103.065 1.00 20.78 ? 1017 GLY   A O     1 
ATOM   7482  N  N     . THR   A  1  1020 ? -7.489  78.378  105.148 1.00 19.90 ? 1018 THR   A N     1 
ATOM   7483  C  CA    . THR   A  1  1020 ? -6.313  77.801  105.774 1.00 19.10 ? 1018 THR   A CA    1 
ATOM   7484  C  C     . THR   A  1  1020 ? -6.439  76.301  105.911 1.00 17.85 ? 1018 THR   A C     1 
ATOM   7485  O  O     . THR   A  1  1020 ? -5.426  75.618  106.081 1.00 19.34 ? 1018 THR   A O     1 
ATOM   7486  C  CB    . THR   A  1  1020 ? -6.161  78.360  107.194 1.00 18.92 ? 1018 THR   A CB    1 
ATOM   7487  O  OG1   . THR   A  1  1020 ? -7.343  78.055  107.965 1.00 19.57 ? 1018 THR   A OG1   1 
ATOM   7488  C  CG2   . THR   A  1  1020 ? -5.952  79.868  107.149 1.00 23.06 ? 1018 THR   A CG2   1 
ATOM   7489  N  N     . GLY   A  1  1021 ? -7.664  75.791  105.895 1.00 19.85 ? 1019 GLY   A N     1 
ATOM   7490  C  CA    . GLY   A  1  1021 ? -7.914  74.453  106.352 1.00 20.45 ? 1019 GLY   A CA    1 
ATOM   7491  C  C     . GLY   A  1  1021 ? -7.681  74.348  107.848 1.00 19.75 ? 1019 GLY   A C     1 
ATOM   7492  O  O     . GLY   A  1  1021 ? -7.369  75.333  108.527 1.00 19.47 ? 1019 GLY   A O     1 
ATOM   7493  N  N     . PRO   A  1  1022 ? -7.885  73.155  108.399 1.00 19.21 ? 1020 PRO   A N     1 
ATOM   7494  C  CA    . PRO   A  1  1022 ? -8.372  71.954  107.718 1.00 18.85 ? 1020 PRO   A CA    1 
ATOM   7495  C  C     . PRO   A  1  1022 ? -9.835  72.072  107.326 1.00 20.13 ? 1020 PRO   A C     1 
ATOM   7496  O  O     . PRO   A  1  1022 ? -10.547 72.988  107.745 1.00 20.90 ? 1020 PRO   A O     1 
ATOM   7497  C  CB    . PRO   A  1  1022 ? -8.166  70.863  108.771 1.00 19.55 ? 1020 PRO   A CB    1 
ATOM   7498  C  CG    . PRO   A  1  1022 ? -8.338  71.584  110.076 1.00 21.69 ? 1020 PRO   A CG    1 
ATOM   7499  C  CD    . PRO   A  1  1022 ? -7.708  72.933  109.846 1.00 19.32 ? 1020 PRO   A CD    1 
ATOM   7500  N  N     . LYS   A  1  1023 ? -10.281 71.138  106.493 1.00 18.59 ? 1021 LYS   A N     1 
ATOM   7501  C  CA    . LYS   A  1  1023 ? -11.637 71.175  105.965 1.00 17.71 ? 1021 LYS   A CA    1 
ATOM   7502  C  C     . LYS   A  1  1023 ? -12.667 70.897  107.045 1.00 18.51 ? 1021 LYS   A C     1 
ATOM   7503  O  O     . LYS   A  1  1023 ? -12.569 69.915  107.785 1.00 18.36 ? 1021 LYS   A O     1 
ATOM   7504  C  CB    . LYS   A  1  1023 ? -11.801 70.104  104.891 1.00 16.96 ? 1021 LYS   A CB    1 
ATOM   7505  C  CG    . LYS   A  1  1023 ? -11.176 70.419  103.559 1.00 16.51 ? 1021 LYS   A CG    1 
ATOM   7506  C  CD    . LYS   A  1  1023 ? -11.347 69.199  102.689 1.00 16.77 ? 1021 LYS   A CD    1 
ATOM   7507  C  CE    . LYS   A  1  1023 ? -10.955 69.459  101.233 1.00 16.87 ? 1021 LYS   A CE    1 
ATOM   7508  N  NZ    . LYS   A  1  1023 ? -12.013 70.245  100.539 1.00 17.54 ? 1021 LYS   A NZ    1 
ATOM   7509  N  N     . ALA   A  1  1024 ? -13.702 71.731  107.079 1.00 19.04 ? 1022 ALA   A N     1 
ATOM   7510  C  CA    . ALA   A  1  1024 ? -14.893 71.397  107.837 1.00 19.65 ? 1022 ALA   A CA    1 
ATOM   7511  C  C     . ALA   A  1  1024 ? -15.534 70.153  107.243 1.00 18.63 ? 1022 ALA   A C     1 
ATOM   7512  O  O     . ALA   A  1  1024 ? -15.497 69.921  106.025 1.00 18.77 ? 1022 ALA   A O     1 
ATOM   7513  C  CB    . ALA   A  1  1024 ? -15.885 72.557  107.779 1.00 20.31 ? 1022 ALA   A CB    1 
ATOM   7514  N  N     . GLY   A  1  1025 ? -16.126 69.344  108.115 1.00 18.55 ? 1023 GLY   A N     1 
ATOM   7515  C  CA    . GLY   A  1  1025 ? -16.762 68.128  107.668 1.00 19.31 ? 1023 GLY   A CA    1 
ATOM   7516  C  C     . GLY   A  1  1025 ? -15.782 67.105  107.172 1.00 18.37 ? 1023 GLY   A C     1 
ATOM   7517  O  O     . GLY   A  1  1025 ? -16.160 66.196  106.426 1.00 18.45 ? 1023 GLY   A O     1 
ATOM   7518  N  N     . GLY   A  1  1026 ? -14.518 67.246  107.565 1.00 17.84 ? 1024 GLY   A N     1 
ATOM   7519  C  CA    . GLY   A  1  1026 ? -13.478 66.314  107.217 1.00 16.64 ? 1024 GLY   A CA    1 
ATOM   7520  C  C     . GLY   A  1  1026 ? -12.754 65.841  108.456 1.00 17.57 ? 1024 GLY   A C     1 
ATOM   7521  O  O     . GLY   A  1  1026 ? -12.953 66.348  109.567 1.00 18.00 ? 1024 GLY   A O     1 
ATOM   7522  N  N     . PRO   A  1  1027 ? -11.878 64.853  108.272 1.00 17.06 ? 1025 PRO   A N     1 
ATOM   7523  C  CA    . PRO   A  1  1027 ? -11.324 64.131  109.415 1.00 17.76 ? 1025 PRO   A CA    1 
ATOM   7524  C  C     . PRO   A  1  1027 ? -10.163 64.835  110.092 1.00 16.88 ? 1025 PRO   A C     1 
ATOM   7525  O  O     . PRO   A  1  1027 ? -9.738  64.377  111.149 1.00 18.00 ? 1025 PRO   A O     1 
ATOM   7526  C  CB    . PRO   A  1  1027 ? -10.879 62.802  108.788 1.00 19.31 ? 1025 PRO   A CB    1 
ATOM   7527  C  CG    . PRO   A  1  1027 ? -10.532 63.177  107.371 1.00 19.08 ? 1025 PRO   A CG    1 
ATOM   7528  C  CD    . PRO   A  1  1027 ? -11.563 64.205  106.987 1.00 16.65 ? 1025 PRO   A CD    1 
ATOM   7529  N  N     . LEU   A  1  1028 ? -9.629  65.913  109.516 1.00 17.37 ? 1026 LEU   A N     1 
ATOM   7530  C  CA    . LEU   A  1  1028 ? -8.533  66.643  110.152 1.00 17.08 ? 1026 LEU   A CA    1 
ATOM   7531  C  C     . LEU   A  1  1028 ? -9.020  67.786  111.021 1.00 18.45 ? 1026 LEU   A C     1 
ATOM   7532  O  O     . LEU   A  1  1028 ? -8.221  68.405  111.731 1.00 20.17 ? 1026 LEU   A O     1 
ATOM   7533  C  CB    . LEU   A  1  1028 ? -7.575  67.190  109.089 1.00 17.65 ? 1026 LEU   A CB    1 
ATOM   7534  C  CG    . LEU   A  1  1028 ? -6.725  66.135  108.382 1.00 20.60 ? 1026 LEU   A CG    1 
ATOM   7535  C  CD1   . LEU   A  1  1028 ? -5.975  66.766  107.215 1.00 20.81 ? 1026 LEU   A CD1   1 
ATOM   7536  C  CD2   . LEU   A  1  1028 ? -5.768  65.522  109.380 1.00 27.49 ? 1026 LEU   A CD2   1 
ATOM   7537  N  N     . TYR   A  1  1029 ? -10.323 68.039  111.016 1.00 17.75 ? 1027 TYR   A N     1 
ATOM   7538  C  CA    . TYR   A  1  1029 ? -10.850 69.256  111.613 1.00 18.65 ? 1027 TYR   A CA    1 
ATOM   7539  C  C     . TYR   A  1  1029 ? -10.691 69.247  113.123 1.00 18.37 ? 1027 TYR   A C     1 
ATOM   7540  O  O     . TYR   A  1  1029 ? -10.176 70.209  113.706 1.00 19.44 ? 1027 TYR   A O     1 
ATOM   7541  C  CB    . TYR   A  1  1029 ? -12.315 69.346  111.244 1.00 19.26 ? 1027 TYR   A CB    1 
ATOM   7542  C  CG    . TYR   A  1  1029 ? -12.964 70.692  111.338 1.00 18.40 ? 1027 TYR   A CG    1 
ATOM   7543  C  CD1   . TYR   A  1  1029 ? -12.585 71.733  110.496 1.00 19.87 ? 1027 TYR   A CD1   1 
ATOM   7544  C  CD2   . TYR   A  1  1029 ? -14.021 70.897  112.215 1.00 18.76 ? 1027 TYR   A CD2   1 
ATOM   7545  C  CE1   . TYR   A  1  1029 ? -13.227 72.955  110.541 1.00 18.70 ? 1027 TYR   A CE1   1 
ATOM   7546  C  CE2   . TYR   A  1  1029 ? -14.670 72.106  112.259 1.00 19.40 ? 1027 TYR   A CE2   1 
ATOM   7547  C  CZ    . TYR   A  1  1029 ? -14.275 73.129  111.428 1.00 18.69 ? 1027 TYR   A CZ    1 
ATOM   7548  O  OH    . TYR   A  1  1029 ? -14.955 74.329  111.480 1.00 21.54 ? 1027 TYR   A OH    1 
ATOM   7549  N  N     . LEU   A  1  1030 ? -11.149 68.180  113.781 1.00 18.35 ? 1028 LEU   A N     1 
ATOM   7550  C  CA    . LEU   A  1  1030 ? -11.123 68.194  115.240 1.00 18.71 ? 1028 LEU   A CA    1 
ATOM   7551  C  C     . LEU   A  1  1030 ? -9.708  68.307  115.763 1.00 20.94 ? 1028 LEU   A C     1 
ATOM   7552  O  O     . LEU   A  1  1030 ? -9.489  68.907  116.820 1.00 20.94 ? 1028 LEU   A O     1 
ATOM   7553  C  CB    . LEU   A  1  1030 ? -11.764 66.939  115.821 1.00 20.15 ? 1028 LEU   A CB    1 
ATOM   7554  C  CG    . LEU   A  1  1030 ? -13.256 66.767  115.574 1.00 21.18 ? 1028 LEU   A CG    1 
ATOM   7555  C  CD1   . LEU   A  1  1030 ? -13.757 65.551  116.324 1.00 26.29 ? 1028 LEU   A CD1   1 
ATOM   7556  C  CD2   . LEU   A  1  1030 ? -14.030 68.012  115.987 1.00 24.31 ? 1028 LEU   A CD2   1 
ATOM   7557  N  N     . GLY   A  1  1031 ? -8.740  67.745  115.037 1.00 18.90 ? 1029 GLY   A N     1 
ATOM   7558  C  CA    . GLY   A  1  1031 ? -7.370  67.749  115.510 1.00 20.49 ? 1029 GLY   A CA    1 
ATOM   7559  C  C     . GLY   A  1  1031 ? -6.763  69.125  115.614 1.00 19.87 ? 1029 GLY   A C     1 
ATOM   7560  O  O     . GLY   A  1  1031 ? -5.767  69.297  116.325 1.00 22.33 ? 1029 GLY   A O     1 
ATOM   7561  N  N     . ARG   A  1  1032 ? -7.318  70.102  114.905 1.00 18.58 ? 1030 ARG   A N     1 
ATOM   7562  C  CA    . ARG   A  1  1032 ? -6.855  71.473  115.015 1.00 18.20 ? 1030 ARG   A CA    1 
ATOM   7563  C  C     . ARG   A  1  1032 ? -7.325  72.136  116.303 1.00 20.82 ? 1030 ARG   A C     1 
ATOM   7564  O  O     . ARG   A  1  1032 ? -6.794  73.186  116.683 1.00 22.10 ? 1030 ARG   A O     1 
ATOM   7565  C  CB    . ARG   A  1  1032 ? -7.354  72.263  113.807 1.00 22.82 ? 1030 ARG   A CB    1 
ATOM   7566  C  CG    . ARG   A  1  1032 ? -6.729  73.630  113.637 1.00 19.56 ? 1030 ARG   A CG    1 
ATOM   7567  C  CD    . ARG   A  1  1032 ? -5.271  73.512  113.229 1.00 20.59 ? 1030 ARG   A CD    1 
ATOM   7568  N  NE    . ARG   A  1  1032 ? -4.761  74.812  112.823 1.00 20.74 ? 1030 ARG   A NE    1 
ATOM   7569  C  CZ    . ARG   A  1  1032 ? -3.691  75.399  113.338 1.00 22.65 ? 1030 ARG   A CZ    1 
ATOM   7570  N  NH1   . ARG   A  1  1032 ? -3.005  74.846  114.326 1.00 26.96 ? 1030 ARG   A NH1   1 
ATOM   7571  N  NH2   . ARG   A  1  1032 ? -3.308  76.577  112.856 1.00 26.37 ? 1030 ARG   A NH2   1 
ATOM   7572  N  N     . LEU   A  1  1033 ? -8.306  71.547  116.976 1.00 19.50 ? 1031 LEU   A N     1 
ATOM   7573  C  CA    . LEU   A  1  1033 ? -8.949  72.168  118.120 1.00 20.36 ? 1031 LEU   A CA    1 
ATOM   7574  C  C     . LEU   A  1  1033 ? -8.469  71.587  119.438 1.00 21.56 ? 1031 LEU   A C     1 
ATOM   7575  O  O     . LEU   A  1  1033 ? -9.070  71.851  120.481 1.00 23.91 ? 1031 LEU   A O     1 
ATOM   7576  C  CB    . LEU   A  1  1033 ? -10.463 72.027  117.987 1.00 20.63 ? 1031 LEU   A CB    1 
ATOM   7577  C  CG    . LEU   A  1  1033 ? -10.960 72.455  116.606 1.00 21.90 ? 1031 LEU   A CG    1 
ATOM   7578  C  CD1   . LEU   A  1  1033 ? -12.457 72.245  116.470 1.00 21.72 ? 1031 LEU   A CD1   1 
ATOM   7579  C  CD2   . LEU   A  1  1033 ? -10.588 73.905  116.327 1.00 24.22 ? 1031 LEU   A CD2   1 
ATOM   7580  N  N     . VAL   A  1  1034 ? -7.394  70.807  119.409 1.00 22.62 ? 1032 VAL   A N     1 
ATOM   7581  C  CA    . VAL   A  1  1034 ? -6.763  70.256  120.592 1.00 22.61 ? 1032 VAL   A CA    1 
ATOM   7582  C  C     . VAL   A  1  1034 ? -5.279  70.576  120.499 1.00 25.11 ? 1032 VAL   A C     1 
ATOM   7583  O  O     . VAL   A  1  1034 ? -4.763  70.912  119.433 1.00 24.83 ? 1032 VAL   A O     1 
ATOM   7584  C  CB    . VAL   A  1  1034 ? -7.005  68.740  120.727 1.00 23.94 ? 1032 VAL   A CB    1 
ATOM   7585  C  CG1   . VAL   A  1  1034 ? -8.479  68.459  121.046 1.00 25.23 ? 1032 VAL   A CG1   1 
ATOM   7586  C  CG2   . VAL   A  1  1034 ? -6.592  68.028  119.442 1.00 21.49 ? 1032 VAL   A CG2   1 
ATOM   7587  N  N     . THR   A  1  1035 ? -4.591  70.486  121.639 1.00 25.48 ? 1033 THR   A N     1 
ATOM   7588  C  CA    . THR   A  1  1035 ? -3.183  70.870  121.651 1.00 26.20 ? 1033 THR   A CA    1 
ATOM   7589  C  C     . THR   A  1  1035 ? -2.295  69.818  121.003 1.00 28.34 ? 1033 THR   A C     1 
ATOM   7590  O  O     . THR   A  1  1035 ? -1.266  70.163  120.413 1.00 33.48 ? 1033 THR   A O     1 
ATOM   7591  C  CB    . THR   A  1  1035 ? -2.725  71.163  123.075 1.00 28.54 ? 1033 THR   A CB    1 
ATOM   7592  O  OG1   . THR   A  1  1035 ? -3.077  70.065  123.920 1.00 36.71 ? 1033 THR   A OG1   1 
ATOM   7593  C  CG2   . THR   A  1  1035 ? -3.387  72.423  123.592 1.00 29.82 ? 1033 THR   A CG2   1 
ATOM   7594  N  N     . THR   A  1  1036 ? -2.670  68.546  121.101 1.00 25.91 ? 1034 THR   A N     1 
ATOM   7595  C  CA    . THR   A  1  1036 ? -1.971  67.454  120.436 1.00 26.88 ? 1034 THR   A CA    1 
ATOM   7596  C  C     . THR   A  1  1036 ? -2.977  66.763  119.529 1.00 25.15 ? 1034 THR   A C     1 
ATOM   7597  O  O     . THR   A  1  1036 ? -3.962  66.200  120.014 1.00 27.25 ? 1034 THR   A O     1 
ATOM   7598  C  CB    . THR   A  1  1036 ? -1.426  66.466  121.468 1.00 33.68 ? 1034 THR   A CB    1 
ATOM   7599  O  OG1   . THR   A  1  1036 ? -0.557  67.157  122.376 1.00 35.40 ? 1034 THR   A OG1   1 
ATOM   7600  C  CG2   . THR   A  1  1036 ? -0.642  65.359  120.778 1.00 31.74 ? 1034 THR   A CG2   1 
ATOM   7601  N  N     . ALA   A  1  1037 ? -2.737  66.816  118.225 1.00 24.43 ? 1035 ALA   A N     1 
ATOM   7602  C  CA    . ALA   A  1  1037 ? -3.703  66.277  117.280 1.00 25.72 ? 1035 ALA   A CA    1 
ATOM   7603  C  C     . ALA   A  1  1037 ? -3.725  64.752  117.353 1.00 24.68 ? 1035 ALA   A C     1 
ATOM   7604  O  O     . ALA   A  1  1037 ? -2.669  64.114  117.404 1.00 25.49 ? 1035 ALA   A O     1 
ATOM   7605  C  CB    . ALA   A  1  1037 ? -3.355  66.714  115.860 1.00 25.41 ? 1035 ALA   A CB    1 
ATOM   7606  N  N     . PRO   A  1  1038 ? -4.904  64.143  117.368 1.00 23.33 ? 1036 PRO   A N     1 
ATOM   7607  C  CA    . PRO   A  1  1038 ? -4.993  62.686  117.287 1.00 21.03 ? 1036 PRO   A CA    1 
ATOM   7608  C  C     . PRO   A  1  1038 ? -4.729  62.248  115.855 1.00 22.49 ? 1036 PRO   A C     1 
ATOM   7609  O  O     . PRO   A  1  1038 ? -4.637  63.057  114.934 1.00 22.58 ? 1036 PRO   A O     1 
ATOM   7610  C  CB    . PRO   A  1  1038 ? -6.454  62.422  117.653 1.00 23.84 ? 1036 PRO   A CB    1 
ATOM   7611  C  CG    . PRO   A  1  1038 ? -7.163  63.609  117.080 1.00 26.04 ? 1036 PRO   A CG    1 
ATOM   7612  C  CD    . PRO   A  1  1038 ? -6.236  64.775  117.351 1.00 23.28 ? 1036 PRO   A CD    1 
ATOM   7613  N  N     . VAL   A  1  1039 ? -4.628  60.939  115.677 1.00 22.73 ? 1037 VAL   A N     1 
ATOM   7614  C  CA    . VAL   A  1  1039 ? -4.521  60.337  114.353 1.00 22.06 ? 1037 VAL   A CA    1 
ATOM   7615  C  C     . VAL   A  1  1039 ? -5.939  60.150  113.822 1.00 21.04 ? 1037 VAL   A C     1 
ATOM   7616  O  O     . VAL   A  1  1039 ? -6.697  59.353  114.391 1.00 21.87 ? 1037 VAL   A O     1 
ATOM   7617  C  CB    . VAL   A  1  1039 ? -3.779  58.999  114.402 1.00 21.57 ? 1037 VAL   A CB    1 
ATOM   7618  C  CG1   . VAL   A  1  1039 ? -3.729  58.370  113.010 1.00 23.07 ? 1037 VAL   A CG1   1 
ATOM   7619  C  CG2   . VAL   A  1  1039 ? -2.369  59.199  114.947 1.00 26.05 ? 1037 VAL   A CG2   1 
ATOM   7620  N  N     . PRO   A  1  1040 ? -6.333  60.845  112.763 1.00 20.95 ? 1038 PRO   A N     1 
ATOM   7621  C  CA    . PRO   A  1  1040 ? -7.698  60.717  112.276 1.00 20.33 ? 1038 PRO   A CA    1 
ATOM   7622  C  C     . PRO   A  1  1040 ? -7.947  59.323  111.733 1.00 18.95 ? 1038 PRO   A C     1 
ATOM   7623  O  O     . PRO   A  1  1040 ? -7.001  58.626  111.334 1.00 19.19 ? 1038 PRO   A O     1 
ATOM   7624  C  CB    . PRO   A  1  1040 ? -7.778  61.769  111.155 1.00 21.21 ? 1038 PRO   A CB    1 
ATOM   7625  C  CG    . PRO   A  1  1040 ? -6.654  62.694  111.415 1.00 22.99 ? 1038 PRO   A CG    1 
ATOM   7626  C  CD    . PRO   A  1  1040 ? -5.567  61.862  112.030 1.00 22.93 ? 1038 PRO   A CD    1 
ATOM   7627  N  N     . PRO   A  1  1041 ? -9.208  58.893  111.671 1.00 18.42 ? 1039 PRO   A N     1 
ATOM   7628  C  CA    . PRO   A  1  1041 ? -9.515  57.614  111.026 1.00 17.78 ? 1039 PRO   A CA    1 
ATOM   7629  C  C     . PRO   A  1  1041 ? -9.000  57.620  109.597 1.00 18.52 ? 1039 PRO   A C     1 
ATOM   7630  O  O     . PRO   A  1  1041 ? -9.049  58.645  108.912 1.00 19.78 ? 1039 PRO   A O     1 
ATOM   7631  C  CB    . PRO   A  1  1041 ? -11.050 57.563  111.045 1.00 20.56 ? 1039 PRO   A CB    1 
ATOM   7632  C  CG    . PRO   A  1  1041 ? -11.443 58.513  112.122 1.00 24.34 ? 1039 PRO   A CG    1 
ATOM   7633  C  CD    . PRO   A  1  1041 ? -10.423 59.595  112.120 1.00 23.18 ? 1039 PRO   A CD    1 
ATOM   7634  N  N     . GLN   A  1  1042 ? -8.477  56.468  109.164 1.00 17.90 ? 1040 GLN   A N     1 
ATOM   7635  C  CA    . GLN   A  1  1042 ? -8.012  56.223  107.800 1.00 19.35 ? 1040 GLN   A CA    1 
ATOM   7636  C  C     . GLN   A  1  1042 ? -6.859  57.117  107.378 1.00 19.42 ? 1040 GLN   A C     1 
ATOM   7637  O  O     . GLN   A  1  1042 ? -6.503  57.138  106.199 1.00 19.50 ? 1040 GLN   A O     1 
ATOM   7638  C  CB    . GLN   A  1  1042 ? -9.141  56.331  106.772 1.00 22.34 ? 1040 GLN   A CB    1 
ATOM   7639  C  CG    . GLN   A  1  1042 ? -10.365 55.507  107.108 1.00 28.18 ? 1040 GLN   A CG    1 
ATOM   7640  C  CD    . GLN   A  1  1042 ? -11.393 55.558  105.997 1.00 35.17 ? 1040 GLN   A CD    1 
ATOM   7641  O  OE1   . GLN   A  1  1042 ? -11.502 54.631  105.199 1.00 42.12 ? 1040 GLN   A OE1   1 
ATOM   7642  N  NE2   . GLN   A  1  1042 ? -12.131 56.656  105.924 1.00 35.61 ? 1040 GLN   A NE2   1 
ATOM   7643  N  N     . HIS   A  1  1043 ? -6.230  57.821  108.309 1.00 17.73 ? 1041 HIS   A N     1 
ATOM   7644  C  CA    . HIS   A  1  1043 ? -5.237  58.836  107.975 1.00 18.44 ? 1041 HIS   A CA    1 
ATOM   7645  C  C     . HIS   A  1  1043 ? -3.853  58.205  108.027 1.00 17.76 ? 1041 HIS   A C     1 
ATOM   7646  O  O     . HIS   A  1  1043 ? -3.248  58.099  109.095 1.00 18.52 ? 1041 HIS   A O     1 
ATOM   7647  C  CB    . HIS   A  1  1043 ? -5.335  59.991  108.961 1.00 20.11 ? 1041 HIS   A CB    1 
ATOM   7648  C  CG    . HIS   A  1  1043 ? -4.377  61.107  108.691 1.00 18.31 ? 1041 HIS   A CG    1 
ATOM   7649  N  ND1   . HIS   A  1  1043 ? -4.660  62.147  107.834 1.00 18.40 ? 1041 HIS   A ND1   1 
ATOM   7650  C  CD2   . HIS   A  1  1043 ? -3.135  61.348  109.176 1.00 17.81 ? 1041 HIS   A CD2   1 
ATOM   7651  C  CE1   . HIS   A  1  1043 ? -3.639  62.985  107.806 1.00 19.89 ? 1041 HIS   A CE1   1 
ATOM   7652  N  NE2   . HIS   A  1  1043 ? -2.697  62.520  108.609 1.00 19.26 ? 1041 HIS   A NE2   1 
ATOM   7653  N  N     . SER   A  1  1044 ? -3.364  57.775  106.870 1.00 17.16 ? 1042 SER   A N     1 
ATOM   7654  C  CA    . SER   A  1  1044 ? -2.010  57.251  106.728 1.00 16.52 ? 1042 SER   A CA    1 
ATOM   7655  C  C     . SER   A  1  1044 ? -1.739  57.179  105.239 1.00 16.86 ? 1042 SER   A C     1 
ATOM   7656  O  O     . SER   A  1  1044 ? -2.640  57.328  104.413 1.00 19.84 ? 1042 SER   A O     1 
ATOM   7657  C  CB    . SER   A  1  1044 ? -1.868  55.861  107.341 1.00 17.22 ? 1042 SER   A CB    1 
ATOM   7658  O  OG    . SER   A  1  1044 ? -2.668  54.934  106.637 1.00 19.33 ? 1042 SER   A OG    1 
ATOM   7659  N  N     . SER   A  1  1045 ? -0.478  56.933  104.903 1.00 16.22 ? 1043 SER   A N     1 
ATOM   7660  C  CA    . SER   A  1  1045 ? -0.109  56.752  103.512 1.00 18.45 ? 1043 SER   A CA    1 
ATOM   7661  C  C     . SER   A  1  1045 ? 1.090   55.832  103.463 1.00 16.46 ? 1043 SER   A C     1 
ATOM   7662  O  O     . SER   A  1  1045 ? 2.026   55.979  104.243 1.00 17.00 ? 1043 SER   A O     1 
ATOM   7663  C  CB    . SER   A  1  1045 ? 0.252   58.086  102.859 1.00 17.96 ? 1043 SER   A CB    1 
ATOM   7664  O  OG    . SER   A  1  1045 ? 0.681   57.862  101.519 1.00 18.75 ? 1043 SER   A OG    1 
ATOM   7665  N  N     . VAL   A  1  1046 ? 1.055   54.883  102.525 1.00 17.10 ? 1044 VAL   A N     1 
ATOM   7666  C  CA    . VAL   A  1  1046 ? 2.210   54.016  102.326 1.00 18.91 ? 1044 VAL   A CA    1 
ATOM   7667  C  C     . VAL   A  1  1046 ? 3.268   54.668  101.466 1.00 18.56 ? 1044 VAL   A C     1 
ATOM   7668  O  O     . VAL   A  1  1046 ? 4.351   54.093  101.301 1.00 19.65 ? 1044 VAL   A O     1 
ATOM   7669  C  CB    . VAL   A  1  1046 ? 1.835   52.642  101.735 1.00 20.43 ? 1044 VAL   A CB    1 
ATOM   7670  C  CG1   . VAL   A  1  1046 ? 0.862   51.921  102.658 1.00 22.18 ? 1044 VAL   A CG1   1 
ATOM   7671  C  CG2   . VAL   A  1  1046 ? 1.254   52.797  100.347 1.00 19.39 ? 1044 VAL   A CG2   1 
ATOM   7672  N  N     . HIS   A  1  1047 ? 3.003   55.850  100.933 1.00 17.04 ? 1045 HIS   A N     1 
ATOM   7673  C  CA    . HIS   A  1  1047 ? 3.918   56.492  100.006 1.00 19.20 ? 1045 HIS   A CA    1 
ATOM   7674  C  C     . HIS   A  1  1047 ? 4.886   57.398  100.743 1.00 17.91 ? 1045 HIS   A C     1 
ATOM   7675  O  O     . HIS   A  1  1047 ? 4.521   58.067  101.714 1.00 20.10 ? 1045 HIS   A O     1 
ATOM   7676  C  CB    . HIS   A  1  1047 ? 3.109   57.247  98.964  1.00 22.21 ? 1045 HIS   A CB    1 
ATOM   7677  C  CG    . HIS   A  1  1047 ? 2.140   56.360  98.253  1.00 26.87 ? 1045 HIS   A CG    1 
ATOM   7678  N  ND1   . HIS   A  1  1047 ? 2.547   55.349  97.407  1.00 27.56 ? 1045 HIS   A ND1   1 
ATOM   7679  C  CD2   . HIS   A  1  1047 ? 0.790   56.279  98.317  1.00 25.63 ? 1045 HIS   A CD2   1 
ATOM   7680  C  CE1   . HIS   A  1  1047 ? 1.484   54.710  96.951  1.00 26.34 ? 1045 HIS   A CE1   1 
ATOM   7681  N  NE2   . HIS   A  1  1047 ? 0.407   55.252  97.493  1.00 28.70 ? 1045 HIS   A NE2   1 
ATOM   7682  N  N     . THR   A  1  1048 ? 6.134   57.390  100.299 1.00 18.41 ? 1046 THR   A N     1 
ATOM   7683  C  CA    . THR   A  1  1048 ? 7.162   58.234  100.879 1.00 18.63 ? 1046 THR   A CA    1 
ATOM   7684  C  C     . THR   A  1  1048 ? 7.643   59.202  99.816  1.00 17.83 ? 1046 THR   A C     1 
ATOM   7685  O  O     . THR   A  1  1048 ? 7.987   58.791  98.704  1.00 19.87 ? 1046 THR   A O     1 
ATOM   7686  C  CB    . THR   A  1  1048 ? 8.319   57.401  101.411 1.00 18.25 ? 1046 THR   A CB    1 
ATOM   7687  O  OG1   . THR   A  1  1048 ? 7.793   56.384  102.267 1.00 19.89 ? 1046 THR   A OG1   1 
ATOM   7688  C  CG2   . THR   A  1  1048 ? 9.272   58.285  102.207 1.00 19.75 ? 1046 THR   A CG2   1 
ATOM   7689  N  N     . ASP   A  1  1049 ? 7.659   60.471  100.161 1.00 17.44 ? 1047 ASP   A N     1 
ATOM   7690  C  CA    . ASP   A  1  1049 ? 8.098   61.474  99.219  1.00 17.40 ? 1047 ASP   A CA    1 
ATOM   7691  C  C     . ASP   A  1  1049 ? 9.556   61.211  98.846  1.00 17.83 ? 1047 ASP   A C     1 
ATOM   7692  O  O     . ASP   A  1  1049 ? 10.397  61.005  99.735  1.00 17.27 ? 1047 ASP   A O     1 
ATOM   7693  C  CB    . ASP   A  1  1049 ? 7.943   62.851  99.846  1.00 17.81 ? 1047 ASP   A CB    1 
ATOM   7694  C  CG    . ASP   A  1  1049 ? 8.350   63.942  98.903  1.00 18.25 ? 1047 ASP   A CG    1 
ATOM   7695  O  OD1   . ASP   A  1  1049 ? 9.566   64.196  98.775  1.00 18.79 ? 1047 ASP   A OD1   1 
ATOM   7696  O  OD2   . ASP   A  1  1049 ? 7.450   64.515  98.252  1.00 18.86 ? 1047 ASP   A OD2   1 
ATOM   7697  N  N     . PRO   A  1  1050 ? 9.887   61.163  97.559  1.00 16.97 ? 1048 PRO   A N     1 
ATOM   7698  C  CA    . PRO   A  1  1050 ? 11.252  60.788  97.172  1.00 18.52 ? 1048 PRO   A CA    1 
ATOM   7699  C  C     . PRO   A  1  1050 ? 12.261  61.887  97.430  1.00 16.42 ? 1048 PRO   A C     1 
ATOM   7700  O  O     . PRO   A  1  1050 ? 13.454  61.602  97.601  1.00 17.80 ? 1048 PRO   A O     1 
ATOM   7701  C  CB    . PRO   A  1  1050 ? 11.114  60.493  95.673  1.00 19.84 ? 1048 PRO   A CB    1 
ATOM   7702  C  CG    . PRO   A  1  1050 ? 9.941   61.369  95.241  1.00 20.37 ? 1048 PRO   A CG    1 
ATOM   7703  C  CD    . PRO   A  1  1050 ? 8.989   61.314  96.401  1.00 18.76 ? 1048 PRO   A CD    1 
ATOM   7704  N  N     . VAL   A  1  1051 ? 11.820  63.143  97.435  1.00 17.68 ? 1049 VAL   A N     1 
ATOM   7705  C  CA    . VAL   A  1  1051 ? 12.726  64.230  97.763  1.00 17.30 ? 1049 VAL   A CA    1 
ATOM   7706  C  C     . VAL   A  1  1051 ? 13.055  64.201  99.245  1.00 16.61 ? 1049 VAL   A C     1 
ATOM   7707  O  O     . VAL   A  1  1051 ? 14.200  64.431  99.638  1.00 17.66 ? 1049 VAL   A O     1 
ATOM   7708  C  CB    . VAL   A  1  1051 ? 12.151  65.581  97.305  1.00 19.23 ? 1049 VAL   A CB    1 
ATOM   7709  C  CG1   . VAL   A  1  1051 ? 13.120  66.695  97.650  1.00 22.27 ? 1049 VAL   A CG1   1 
ATOM   7710  C  CG2   . VAL   A  1  1051 ? 11.896  65.552  95.797  1.00 18.76 ? 1049 VAL   A CG2   1 
ATOM   7711  N  N     . LEU   A  1  1052 ? 12.064  63.895  100.091 1.00 17.02 ? 1050 LEU   A N     1 
ATOM   7712  C  CA    . LEU   A  1  1052 ? 12.352  63.620  101.492 1.00 16.33 ? 1050 LEU   A CA    1 
ATOM   7713  C  C     . LEU   A  1  1052 ? 13.413  62.537  101.625 1.00 18.41 ? 1050 LEU   A C     1 
ATOM   7714  O  O     . LEU   A  1  1052 ? 14.373  62.684  102.386 1.00 16.74 ? 1050 LEU   A O     1 
ATOM   7715  C  CB    . LEU   A  1  1052 ? 11.059  63.223  102.206 1.00 16.79 ? 1050 LEU   A CB    1 
ATOM   7716  C  CG    . LEU   A  1  1052 ? 11.107  62.826  103.691 1.00 17.88 ? 1050 LEU   A CG    1 
ATOM   7717  C  CD1   . LEU   A  1  1052 ? 11.673  61.415  103.942 1.00 18.03 ? 1050 LEU   A CD1   1 
ATOM   7718  C  CD2   . LEU   A  1  1052 ? 11.877  63.874  104.496 1.00 18.39 ? 1050 LEU   A CD2   1 
ATOM   7719  N  N     . LEU   A  1  1053 ? 13.257  61.430  100.889 1.00 17.61 ? 1051 LEU   A N     1 
ATOM   7720  C  CA    . LEU   A  1  1053 ? 14.244  60.361  100.986 1.00 17.77 ? 1051 LEU   A CA    1 
ATOM   7721  C  C     . LEU   A  1  1053 ? 15.616  60.843  100.559 1.00 17.34 ? 1051 LEU   A C     1 
ATOM   7722  O  O     . LEU   A  1  1053 ? 16.613  60.523  101.205 1.00 18.60 ? 1051 LEU   A O     1 
ATOM   7723  C  CB    . LEU   A  1  1053 ? 13.816  59.151  100.157 1.00 20.12 ? 1051 LEU   A CB    1 
ATOM   7724  C  CG    . LEU   A  1  1053 ? 12.595  58.433  100.728 1.00 19.89 ? 1051 LEU   A CG    1 
ATOM   7725  C  CD1   . LEU   A  1  1053 ? 12.065  57.414  99.726  1.00 21.11 ? 1051 LEU   A CD1   1 
ATOM   7726  C  CD2   . LEU   A  1  1053 ? 12.936  57.761  102.030 1.00 20.66 ? 1051 LEU   A CD2   1 
ATOM   7727  N  N     . ASP   A  1  1054 ? 15.688  61.616  99.471  1.00 17.09 ? 1052 ASP   A N     1 
ATOM   7728  C  CA    . ASP   A  1  1054 ? 16.978  62.145  99.040  1.00 18.43 ? 1052 ASP   A CA    1 
ATOM   7729  C  C     . ASP   A  1  1054 ? 17.563  63.051  100.106 1.00 17.19 ? 1052 ASP   A C     1 
ATOM   7730  O  O     . ASP   A  1  1054 ? 18.771  63.030  100.353 1.00 18.45 ? 1052 ASP   A O     1 
ATOM   7731  C  CB    . ASP   A  1  1054 ? 16.821  62.926  97.744  1.00 17.96 ? 1052 ASP   A CB    1 
ATOM   7732  C  CG    . ASP   A  1  1054 ? 16.559  62.036  96.568  1.00 21.07 ? 1052 ASP   A CG    1 
ATOM   7733  O  OD1   . ASP   A  1  1054 ? 16.683  60.799  96.721  1.00 20.87 ? 1052 ASP   A OD1   1 
ATOM   7734  O  OD2   . ASP   A  1  1054 ? 16.220  62.587  95.503  1.00 24.90 ? 1052 ASP   A OD2   1 
ATOM   7735  N  N     . PHE   A  1  1055 ? 16.718  63.848  100.754 1.00 15.79 ? 1053 PHE   A N     1 
ATOM   7736  C  CA    . PHE   A  1  1055 ? 17.188  64.730  101.814 1.00 19.48 ? 1053 PHE   A CA    1 
ATOM   7737  C  C     . PHE   A  1  1055 ? 17.706  63.936  103.005 1.00 17.30 ? 1053 PHE   A C     1 
ATOM   7738  O  O     . PHE   A  1  1055 ? 18.748  64.275  103.579 1.00 18.68 ? 1053 PHE   A O     1 
ATOM   7739  C  CB    . PHE   A  1  1055 ? 16.056  65.666  102.230 1.00 18.40 ? 1053 PHE   A CB    1 
ATOM   7740  C  CG    . PHE   A  1  1055 ? 16.436  66.625  103.309 1.00 18.72 ? 1053 PHE   A CG    1 
ATOM   7741  C  CD1   . PHE   A  1  1055 ? 17.532  67.450  103.155 1.00 20.10 ? 1053 PHE   A CD1   1 
ATOM   7742  C  CD2   . PHE   A  1  1055 ? 15.688  66.711  104.470 1.00 19.09 ? 1053 PHE   A CD2   1 
ATOM   7743  C  CE1   . PHE   A  1  1055 ? 17.885  68.358  104.149 1.00 21.52 ? 1053 PHE   A CE1   1 
ATOM   7744  C  CE2   . PHE   A  1  1055 ? 16.035  67.616  105.472 1.00 20.67 ? 1053 PHE   A CE2   1 
ATOM   7745  C  CZ    . PHE   A  1  1055 ? 17.137  68.434  105.303 1.00 22.30 ? 1053 PHE   A CZ    1 
ATOM   7746  N  N     . ALA   A  1  1056 ? 16.994  62.879  103.399 1.00 18.09 ? 1054 ALA   A N     1 
ATOM   7747  C  CA    . ALA   A  1  1056 ? 17.468  62.042  104.499 1.00 18.48 ? 1054 ALA   A CA    1 
ATOM   7748  C  C     . ALA   A  1  1056 ? 18.840  61.458  104.197 1.00 19.12 ? 1054 ALA   A C     1 
ATOM   7749  O  O     . ALA   A  1  1056 ? 19.714  61.434  105.067 1.00 20.37 ? 1054 ALA   A O     1 
ATOM   7750  C  CB    . ALA   A  1  1056 ? 16.460  60.935  104.796 1.00 21.32 ? 1054 ALA   A CB    1 
ATOM   7751  N  N     . LYS   A  1  1057 ? 19.054  60.988  102.966 1.00 18.74 ? 1055 LYS   A N     1 
ATOM   7752  C  CA    . LYS   A  1  1057 ? 20.366  60.454  102.612 1.00 22.80 ? 1055 LYS   A CA    1 
ATOM   7753  C  C     . LYS   A  1  1057 ? 21.430  61.540  102.641 1.00 20.07 ? 1055 LYS   A C     1 
ATOM   7754  O  O     . LYS   A  1  1057 ? 22.568  61.296  103.069 1.00 20.62 ? 1055 LYS   A O     1 
ATOM   7755  C  CB    . LYS   A  1  1057 ? 20.318  59.808  101.232 1.00 22.52 ? 1055 LYS   A CB    1 
ATOM   7756  C  CG    . LYS   A  1  1057 ? 19.624  58.477  101.236 1.00 24.58 ? 1055 LYS   A CG    1 
ATOM   7757  C  CD    . LYS   A  1  1057 ? 19.805  57.786  99.906  1.00 22.38 ? 1055 LYS   A CD    1 
ATOM   7758  C  CE    . LYS   A  1  1057 ? 19.232  58.617  98.778  1.00 23.81 ? 1055 LYS   A CE    1 
ATOM   7759  N  NZ    . LYS   A  1  1057 ? 19.112  57.816  97.527  1.00 29.47 ? 1055 LYS   A NZ    1 
ATOM   7760  N  N     . TRP   A  1  1058 ? 21.091  62.730  102.150 1.00 19.77 ? 1056 TRP   A N     1 
ATOM   7761  C  CA    . TRP   A  1  1058 ? 22.007  63.860  102.222 1.00 22.30 ? 1056 TRP   A CA    1 
ATOM   7762  C  C     . TRP   A  1  1058 ? 22.369  64.181  103.665 1.00 21.12 ? 1056 TRP   A C     1 
ATOM   7763  O  O     . TRP   A  1  1058 ? 23.538  64.420  103.977 1.00 23.74 ? 1056 TRP   A O     1 
ATOM   7764  C  CB    . TRP   A  1  1058 ? 21.381  65.072  101.531 1.00 24.34 ? 1056 TRP   A CB    1 
ATOM   7765  C  CG    . TRP   A  1  1058 ? 22.209  66.319  101.596 1.00 23.72 ? 1056 TRP   A CG    1 
ATOM   7766  C  CD1   . TRP   A  1  1058 ? 23.202  66.696  100.728 1.00 27.43 ? 1056 TRP   A CD1   1 
ATOM   7767  C  CD2   . TRP   A  1  1058 ? 22.113  67.363  102.573 1.00 25.88 ? 1056 TRP   A CD2   1 
ATOM   7768  N  NE1   . TRP   A  1  1058 ? 23.723  67.909  101.108 1.00 28.66 ? 1056 TRP   A NE1   1 
ATOM   7769  C  CE2   . TRP   A  1  1058 ? 23.077  68.338  102.239 1.00 28.00 ? 1056 TRP   A CE2   1 
ATOM   7770  C  CE3   . TRP   A  1  1058 ? 21.313  67.563  103.700 1.00 25.18 ? 1056 TRP   A CE3   1 
ATOM   7771  C  CZ2   . TRP   A  1  1058 ? 23.260  69.498  102.995 1.00 28.93 ? 1056 TRP   A CZ2   1 
ATOM   7772  C  CZ3   . TRP   A  1  1058 ? 21.491  68.718  104.447 1.00 27.48 ? 1056 TRP   A CZ3   1 
ATOM   7773  C  CH2   . TRP   A  1  1058 ? 22.461  69.666  104.095 1.00 27.87 ? 1056 TRP   A CH2   1 
ATOM   7774  N  N     . LEU   A  1  1059 ? 21.379  64.170  104.558 1.00 19.86 ? 1057 LEU   A N     1 
ATOM   7775  C  CA    . LEU   A  1  1059 ? 21.633  64.451  105.966 1.00 22.44 ? 1057 LEU   A CA    1 
ATOM   7776  C  C     . LEU   A  1  1059 ? 22.608  63.448  106.543 1.00 20.86 ? 1057 LEU   A C     1 
ATOM   7777  O  O     . LEU   A  1  1059 ? 23.546  63.819  107.255 1.00 24.14 ? 1057 LEU   A O     1 
ATOM   7778  C  CB    . LEU   A  1  1059 ? 20.323  64.408  106.743 1.00 19.89 ? 1057 LEU   A CB    1 
ATOM   7779  C  CG    . LEU   A  1  1059 ? 19.459  65.645  106.579 1.00 21.52 ? 1057 LEU   A CG    1 
ATOM   7780  C  CD1   . LEU   A  1  1059 ? 18.086  65.405  107.206 1.00 19.52 ? 1057 LEU   A CD1   1 
ATOM   7781  C  CD2   . LEU   A  1  1059 ? 20.144  66.821  107.256 1.00 23.24 ? 1057 LEU   A CD2   1 
ATOM   7782  N  N     . ASP   A  1  1060 ? 22.404  62.164  106.246 1.00 21.34 ? 1058 ASP   A N     1 
ATOM   7783  C  CA    . ASP   A  1  1060 ? 23.355  61.158  106.693 1.00 27.97 ? 1058 ASP   A CA    1 
ATOM   7784  C  C     . ASP   A  1  1060 ? 24.739  61.421  106.120 1.00 24.61 ? 1058 ASP   A C     1 
ATOM   7785  O  O     . ASP   A  1  1060 ? 25.742  61.304  106.833 1.00 26.31 ? 1058 ASP   A O     1 
ATOM   7786  C  CB    . ASP   A  1  1060 ? 22.863  59.764  106.322 1.00 26.26 ? 1058 ASP   A CB    1 
ATOM   7787  C  CG    . ASP   A  1  1060 ? 22.038  59.135  107.419 1.00 25.71 ? 1058 ASP   A CG    1 
ATOM   7788  O  OD1   . ASP   A  1  1060 ? 22.328  59.390  108.614 1.00 32.89 ? 1058 ASP   A OD1   1 
ATOM   7789  O  OD2   . ASP   A  1  1060 ? 21.108  58.382  107.093 1.00 31.75 ? 1058 ASP   A OD2   1 
ATOM   7790  N  N     . GLY   A  1  1061 ? 24.819  61.809  104.847 1.00 25.47 ? 1059 GLY   A N     1 
ATOM   7791  C  CA    . GLY   A  1  1061 ? 26.118  62.093  104.257 1.00 24.70 ? 1059 GLY   A CA    1 
ATOM   7792  C  C     . GLY   A  1  1061 ? 26.809  63.279  104.896 1.00 26.88 ? 1059 GLY   A C     1 
ATOM   7793  O  O     . GLY   A  1  1061 ? 28.044  63.327  104.957 1.00 28.78 ? 1059 GLY   A O     1 
ATOM   7794  N  N     . LYS   A  1  1062 ? 26.034  64.248  105.382 1.00 26.55 ? 1060 LYS   A N     1 
ATOM   7795  C  CA    . LYS   A  1  1062 ? 26.579  65.395  106.095 1.00 29.29 ? 1060 LYS   A CA    1 
ATOM   7796  C  C     . LYS   A  1  1062 ? 26.908  65.091  107.549 1.00 29.19 ? 1060 LYS   A C     1 
ATOM   7797  O  O     . LYS   A  1  1062 ? 27.467  65.956  108.229 1.00 33.64 ? 1060 LYS   A O     1 
ATOM   7798  C  CB    . LYS   A  1  1062 ? 25.613  66.580  106.017 1.00 30.76 ? 1060 LYS   A CB    1 
ATOM   7799  C  CG    . LYS   A  1  1062 ? 25.524  67.220  104.642 1.00 30.77 ? 1060 LYS   A CG    1 
ATOM   7800  C  CD    . LYS   A  1  1062 ? 26.878  67.774  104.202 1.00 36.29 ? 1060 LYS   A CD    1 
ATOM   7801  C  CE    . LYS   A  1  1062 ? 26.807  68.356  102.799 1.00 38.02 ? 1060 LYS   A CE    1 
ATOM   7802  N  NZ    . LYS   A  1  1062 ? 28.093  68.986  102.400 1.00 41.24 ? 1060 LYS   A NZ    1 
ATOM   7803  N  N     . GLY   A  1  1063 ? 26.598  63.894  108.041 1.00 27.17 ? 1061 GLY   A N     1 
ATOM   7804  C  CA    . GLY   A  1  1063 ? 26.808  63.556  109.433 1.00 30.33 ? 1061 GLY   A CA    1 
ATOM   7805  C  C     . GLY   A  1  1063 ? 25.668  63.908  110.366 1.00 30.91 ? 1061 GLY   A C     1 
ATOM   7806  O  O     . GLY   A  1  1063 ? 25.794  63.695  111.581 1.00 31.93 ? 1061 GLY   A O     1 
ATOM   7807  N  N     . ALA   A  1  1064 ? 24.555  64.429  109.845 1.00 25.52 ? 1062 ALA   A N     1 
ATOM   7808  C  CA    . ALA   A  1  1064 ? 23.418  64.830  110.679 1.00 24.79 ? 1062 ALA   A CA    1 
ATOM   7809  C  C     . ALA   A  1  1064 ? 22.517  63.619  110.920 1.00 26.01 ? 1062 ALA   A C     1 
ATOM   7810  O  O     . ALA   A  1  1064 ? 21.397  63.513  110.420 1.00 22.85 ? 1062 ALA   A O     1 
ATOM   7811  C  CB    . ALA   A  1  1064 ? 22.677  65.998  110.043 1.00 25.07 ? 1062 ALA   A CB    1 
ATOM   7812  N  N     . ARG   A  1  1065 ? 23.039  62.695  111.724 1.00 23.74 ? 1063 ARG   A N     1 
ATOM   7813  C  CA    . ARG   A  1  1065 ? 22.446  61.367  111.824 1.00 23.04 ? 1063 ARG   A CA    1 
ATOM   7814  C  C     . ARG   A  1  1065 ? 21.074  61.418  112.478 1.00 25.03 ? 1063 ARG   A C     1 
ATOM   7815  O  O     . ARG   A  1  1065 ? 20.125  60.786  112.002 1.00 25.92 ? 1063 ARG   A O     1 
ATOM   7816  C  CB    . ARG   A  1  1065 ? 23.381  60.438  112.595 1.00 28.00 ? 1063 ARG   A CB    1 
ATOM   7817  N  N     . ALA   A  1  1066 ? 20.946  62.154  113.585 1.00 25.33 ? 1064 ALA   A N     1 
ATOM   7818  C  CA    . ALA   A  1  1066 ? 19.650  62.243  114.245 1.00 25.07 ? 1064 ALA   A CA    1 
ATOM   7819  C  C     . ALA   A  1  1066 ? 18.626  62.924  113.351 1.00 23.03 ? 1064 ALA   A C     1 
ATOM   7820  O  O     . ALA   A  1  1066 ? 17.450  62.543  113.341 1.00 23.74 ? 1064 ALA   A O     1 
ATOM   7821  C  CB    . ALA   A  1  1066 ? 19.772  63.000  115.564 1.00 26.14 ? 1064 ALA   A CB    1 
ATOM   7822  N  N     . GLU   A  1  1067 ? 19.053  63.939  112.597 1.00 23.35 ? 1065 GLU   A N     1 
ATOM   7823  C  CA    . GLU   A  1  1067 ? 18.123  64.618  111.701 1.00 22.24 ? 1065 GLU   A CA    1 
ATOM   7824  C  C     . GLU   A  1  1067 ? 17.714  63.717  110.544 1.00 22.21 ? 1065 GLU   A C     1 
ATOM   7825  O  O     . GLU   A  1  1067 ? 16.560  63.749  110.113 1.00 20.31 ? 1065 GLU   A O     1 
ATOM   7826  C  CB    . GLU   A  1  1067 ? 18.729  65.926  111.189 1.00 24.36 ? 1065 GLU   A CB    1 
ATOM   7827  C  CG    . GLU   A  1  1067 ? 18.857  67.028  112.251 1.00 22.96 ? 1065 GLU   A CG    1 
ATOM   7828  C  CD    . GLU   A  1  1067 ? 20.061  66.872  113.167 1.00 28.31 ? 1065 GLU   A CD    1 
ATOM   7829  O  OE1   . GLU   A  1  1067 ? 20.912  65.989  112.930 1.00 24.41 ? 1065 GLU   A OE1   1 
ATOM   7830  O  OE2   . GLU   A  1  1067 ? 20.146  67.649  114.144 1.00 32.11 ? 1065 GLU   A OE2   1 
ATOM   7831  N  N     . ALA   A  1  1068 ? 18.647  62.914  110.025 1.00 21.47 ? 1066 ALA   A N     1 
ATOM   7832  C  CA    . ALA   A  1  1068 ? 18.297  61.962  108.975 1.00 21.74 ? 1066 ALA   A CA    1 
ATOM   7833  C  C     . ALA   A  1  1068 ? 17.256  60.970  109.469 1.00 21.83 ? 1066 ALA   A C     1 
ATOM   7834  O  O     . ALA   A  1  1068 ? 16.328  60.613  108.736 1.00 20.31 ? 1066 ALA   A O     1 
ATOM   7835  C  CB    . ALA   A  1  1068 ? 19.544  61.222  108.503 1.00 24.16 ? 1066 ALA   A CB    1 
ATOM   7836  N  N     . GLU   A  1  1069 ? 17.400  60.504  110.709 1.00 22.33 ? 1067 GLU   A N     1 
ATOM   7837  C  CA    . GLU   A  1  1069 ? 16.399  59.614  111.278 1.00 22.17 ? 1067 GLU   A CA    1 
ATOM   7838  C  C     . GLU   A  1  1069 ? 15.067  60.326  111.422 1.00 21.73 ? 1067 GLU   A C     1 
ATOM   7839  O  O     . GLU   A  1  1069 ? 14.012  59.765  111.099 1.00 22.52 ? 1067 GLU   A O     1 
ATOM   7840  C  CB    . GLU   A  1  1069 ? 16.881  59.108  112.637 1.00 23.98 ? 1067 GLU   A CB    1 
ATOM   7841  C  CG    . GLU   A  1  1069 ? 15.857  58.286  113.393 1.00 28.26 ? 1067 GLU   A CG    1 
ATOM   7842  C  CD    . GLU   A  1  1069 ? 15.721  56.872  112.857 1.00 38.42 ? 1067 GLU   A CD    1 
ATOM   7843  O  OE1   . GLU   A  1  1069 ? 16.481  56.506  111.932 1.00 41.12 ? 1067 GLU   A OE1   1 
ATOM   7844  O  OE2   . GLU   A  1  1069 ? 14.853  56.125  113.365 1.00 47.50 ? 1067 GLU   A OE2   1 
ATOM   7845  N  N     . ALA   A  1  1070 ? 15.095  61.568  111.907 1.00 21.84 ? 1068 ALA   A N     1 
ATOM   7846  C  CA    . ALA   A  1  1070 ? 13.863  62.335  112.007 1.00 22.84 ? 1068 ALA   A CA    1 
ATOM   7847  C  C     . ALA   A  1  1070 ? 13.250  62.549  110.636 1.00 18.13 ? 1068 ALA   A C     1 
ATOM   7848  O  O     . ALA   A  1  1070 ? 12.018  62.546  110.499 1.00 20.39 ? 1068 ALA   A O     1 
ATOM   7849  C  CB    . ALA   A  1  1070 ? 14.128  63.678  112.687 1.00 23.38 ? 1068 ALA   A CB    1 
ATOM   7850  N  N     . ALA   A  1  1071 ? 14.089  62.725  109.614 1.00 19.09 ? 1069 ALA   A N     1 
ATOM   7851  C  CA    . ALA   A  1  1071 ? 13.573  62.900  108.262 1.00 17.94 ? 1069 ALA   A CA    1 
ATOM   7852  C  C     . ALA   A  1  1071 ? 12.886  61.630  107.779 1.00 18.22 ? 1069 ALA   A C     1 
ATOM   7853  O  O     . ALA   A  1  1071 ? 11.766  61.682  107.262 1.00 18.27 ? 1069 ALA   A O     1 
ATOM   7854  C  CB    . ALA   A  1  1071 ? 14.692  63.324  107.314 1.00 20.25 ? 1069 ALA   A CB    1 
ATOM   7855  N  N     . ARG   A  1  1072 ? 13.522  60.472  107.984 1.00 18.70 ? 1070 ARG   A N     1 
ATOM   7856  C  CA    . ARG   A  1  1072 ? 12.881  59.218  107.611 1.00 20.64 ? 1070 ARG   A CA    1 
ATOM   7857  C  C     . ARG   A  1  1072 ? 11.571  59.030  108.358 1.00 21.18 ? 1070 ARG   A C     1 
ATOM   7858  O  O     . ARG   A  1  1072 ? 10.576  58.586  107.776 1.00 20.33 ? 1070 ARG   A O     1 
ATOM   7859  C  CB    . ARG   A  1  1072 ? 13.816  58.038  107.864 1.00 22.02 ? 1070 ARG   A CB    1 
ATOM   7860  C  CG    . ARG   A  1  1072 ? 14.966  57.956  106.865 1.00 23.97 ? 1070 ARG   A CG    1 
ATOM   7861  C  CD    . ARG   A  1  1072 ? 15.795  56.695  107.066 1.00 25.13 ? 1070 ARG   A CD    1 
ATOM   7862  N  NE    . ARG   A  1  1072 ? 16.545  56.747  108.313 1.00 26.52 ? 1070 ARG   A NE    1 
ATOM   7863  C  CZ    . ARG   A  1  1072 ? 17.753  57.281  108.432 1.00 27.50 ? 1070 ARG   A CZ    1 
ATOM   7864  N  NH1   . ARG   A  1  1072 ? 18.384  57.802  107.391 1.00 27.66 ? 1070 ARG   A NH1   1 
ATOM   7865  N  NH2   . ARG   A  1  1072 ? 18.334  57.305  109.627 1.00 28.77 ? 1070 ARG   A NH2   1 
ATOM   7866  N  N     . ASN   A  1  1073 ? 11.550  59.366  109.649 1.00 19.52 ? 1071 ASN   A N     1 
ATOM   7867  C  CA    . ASN   A  1  1073 ? 10.322  59.245  110.424 1.00 21.59 ? 1071 ASN   A CA    1 
ATOM   7868  C  C     . ASN   A  1  1073 ? 9.235   60.149  109.868 1.00 19.76 ? 1071 ASN   A C     1 
ATOM   7869  O  O     . ASN   A  1  1073 ? 8.070   59.747  109.787 1.00 21.09 ? 1071 ASN   A O     1 
ATOM   7870  C  CB    . ASN   A  1  1073 ? 10.591  59.565  111.893 1.00 20.89 ? 1071 ASN   A CB    1 
ATOM   7871  C  CG    . ASN   A  1  1073 ? 11.388  58.476  112.576 1.00 28.37 ? 1071 ASN   A CG    1 
ATOM   7872  O  OD1   . ASN   A  1  1073 ? 11.432  57.340  112.100 1.00 31.93 ? 1071 ASN   A OD1   1 
ATOM   7873  N  ND2   . ASN   A  1  1073 ? 12.019  58.812  113.690 1.00 30.45 ? 1071 ASN   A ND2   1 
ATOM   7874  N  N     . ALA   A  1  1074 ? 9.595   61.381  109.491 1.00 18.58 ? 1072 ALA   A N     1 
ATOM   7875  C  CA    . ALA   A  1  1074 ? 8.624   62.273  108.873 1.00 20.46 ? 1072 ALA   A CA    1 
ATOM   7876  C  C     . ALA   A  1  1074 ? 8.127   61.701  107.557 1.00 17.74 ? 1072 ALA   A C     1 
ATOM   7877  O  O     . ALA   A  1  1074 ? 6.935   61.794  107.241 1.00 17.32 ? 1072 ALA   A O     1 
ATOM   7878  C  CB    . ALA   A  1  1074 ? 9.245   63.654  108.652 1.00 21.99 ? 1072 ALA   A CB    1 
ATOM   7879  N  N     . GLY   A  1  1075 ? 9.027   61.099  106.780 1.00 18.37 ? 1073 GLY   A N     1 
ATOM   7880  C  CA    . GLY   A  1  1075 ? 8.603   60.480  105.539 1.00 17.64 ? 1073 GLY   A CA    1 
ATOM   7881  C  C     . GLY   A  1  1075 ? 7.533   59.428  105.755 1.00 16.94 ? 1073 GLY   A C     1 
ATOM   7882  O  O     . GLY   A  1  1075 ? 6.573   59.342  104.984 1.00 18.89 ? 1073 GLY   A O     1 
ATOM   7883  N  N     . SER   A  1  1076 ? 7.692   58.606  106.796 1.00 17.77 ? 1074 SER   A N     1 
ATOM   7884  C  CA    . SER   A  1  1076 ? 6.713   57.567  107.096 1.00 18.91 ? 1074 SER   A CA    1 
ATOM   7885  C  C     . SER   A  1  1076 ? 5.455   58.137  107.726 1.00 19.36 ? 1074 SER   A C     1 
ATOM   7886  O  O     . SER   A  1  1076 ? 4.347   57.682  107.421 1.00 21.75 ? 1074 SER   A O     1 
ATOM   7887  C  CB    . SER   A  1  1076 ? 7.317   56.544  108.055 1.00 22.70 ? 1074 SER   A CB    1 
ATOM   7888  O  OG    . SER   A  1  1076 ? 8.300   55.769  107.414 1.00 30.18 ? 1074 SER   A OG    1 
ATOM   7889  N  N     . SER   A  1  1077 ? 5.608   59.125  108.608 1.00 19.45 ? 1075 SER   A N     1 
ATOM   7890  C  CA    A SER   A  1  1077 ? 4.450   59.655  109.316 0.48 22.12 ? 1075 SER   A CA    1 
ATOM   7891  C  CA    B SER   A  1  1077 ? 4.463   59.676  109.324 0.52 22.12 ? 1075 SER   A CA    1 
ATOM   7892  C  C     . SER   A  1  1077 ? 3.558   60.489  108.409 1.00 18.95 ? 1075 SER   A C     1 
ATOM   7893  O  O     . SER   A  1  1077 ? 2.354   60.609  108.667 1.00 20.39 ? 1075 SER   A O     1 
ATOM   7894  C  CB    A SER   A  1  1077 ? 4.907   60.470  110.522 0.48 23.30 ? 1075 SER   A CB    1 
ATOM   7895  C  CB    B SER   A  1  1077 ? 4.960   60.547  110.477 0.52 23.25 ? 1075 SER   A CB    1 
ATOM   7896  O  OG    A SER   A  1  1077 ? 5.403   59.608  111.524 0.48 24.46 ? 1075 SER   A OG    1 
ATOM   7897  O  OG    B SER   A  1  1077 ? 3.879   61.192  111.128 0.52 23.97 ? 1075 SER   A OG    1 
ATOM   7898  N  N     . SER   A  1  1078 ? 4.121   61.070  107.362 1.00 17.92 ? 1076 SER   A N     1 
ATOM   7899  C  CA    . SER   A  1  1078 ? 3.347   61.885  106.447 1.00 18.30 ? 1076 SER   A CA    1 
ATOM   7900  C  C     . SER   A  1  1078 ? 2.215   61.071  105.838 1.00 18.43 ? 1076 SER   A C     1 
ATOM   7901  O  O     . SER   A  1  1078 ? 2.382   59.902  105.485 1.00 18.53 ? 1076 SER   A O     1 
ATOM   7902  C  CB    . SER   A  1  1078 ? 4.264   62.372  105.335 1.00 17.67 ? 1076 SER   A CB    1 
ATOM   7903  O  OG    . SER   A  1  1078 ? 3.496   63.029  104.346 1.00 17.33 ? 1076 SER   A OG    1 
ATOM   7904  N  N     . ALA   A  1  1079 ? 1.049   61.693  105.718 1.00 16.70 ? 1077 ALA   A N     1 
ATOM   7905  C  CA    . ALA   A  1  1079 ? -0.066  61.068  105.033 1.00 15.92 ? 1077 ALA   A CA    1 
ATOM   7906  C  C     . ALA   A  1  1079 ? -0.216  61.574  103.614 1.00 16.10 ? 1077 ALA   A C     1 
ATOM   7907  O  O     . ALA   A  1  1079 ? -1.230  61.298  102.973 1.00 15.78 ? 1077 ALA   A O     1 
ATOM   7908  C  CB    . ALA   A  1  1079 ? -1.360  61.251  105.825 1.00 16.54 ? 1077 ALA   A CB    1 
ATOM   7909  N  N     . LEU   A  1  1080 ? 0.773   62.303  103.103 1.00 15.73 ? 1078 LEU   A N     1 
ATOM   7910  C  CA    . LEU   A  1  1080 ? 0.793   62.682  101.697 1.00 16.69 ? 1078 LEU   A CA    1 
ATOM   7911  C  C     . LEU   A  1  1080 ? 0.563   61.451  100.836 1.00 15.21 ? 1078 LEU   A C     1 
ATOM   7912  O  O     . LEU   A  1  1080 ? 1.225   60.422  101.009 1.00 16.13 ? 1078 LEU   A O     1 
ATOM   7913  C  CB    . LEU   A  1  1080 ? 2.170   63.256  101.366 1.00 16.32 ? 1078 LEU   A CB    1 
ATOM   7914  C  CG    . LEU   A  1  1080 ? 2.388   63.550  99.887  1.00 15.49 ? 1078 LEU   A CG    1 
ATOM   7915  C  CD1   . LEU   A  1  1080 ? 1.535   64.729  99.467  1.00 18.55 ? 1078 LEU   A CD1   1 
ATOM   7916  C  CD2   . LEU   A  1  1080 ? 3.867   63.825  99.629  1.00 16.75 ? 1078 LEU   A CD2   1 
ATOM   7917  N  N     . GLY   A  1  1081 ? -0.382  61.550  99.904  1.00 15.11 ? 1079 GLY   A N     1 
ATOM   7918  C  CA    . GLY   A  1  1081 ? -0.690  60.421  99.053  1.00 16.71 ? 1079 GLY   A CA    1 
ATOM   7919  C  C     . GLY   A  1  1081 ? -1.895  59.617  99.489  1.00 17.78 ? 1079 GLY   A C     1 
ATOM   7920  O  O     . GLY   A  1  1081 ? -2.315  58.714  98.753  1.00 17.98 ? 1079 GLY   A O     1 
ATOM   7921  N  N     . LEU   A  1  1082 ? -2.435  59.891  100.671 1.00 15.53 ? 1080 LEU   A N     1 
ATOM   7922  C  CA    A LEU   A  1  1082 ? -3.705  59.297  101.058 0.50 16.17 ? 1080 LEU   A CA    1 
ATOM   7923  C  CA    B LEU   A  1  1082 ? -3.707  59.300  101.061 0.50 16.17 ? 1080 LEU   A CA    1 
ATOM   7924  C  C     . LEU   A  1  1082 ? -4.721  59.524  99.950  1.00 18.16 ? 1080 LEU   A C     1 
ATOM   7925  O  O     . LEU   A  1  1082 ? -4.816  60.618  99.393  1.00 17.32 ? 1080 LEU   A O     1 
ATOM   7926  C  CB    A LEU   A  1  1082 ? -4.202  59.953  102.344 0.50 16.57 ? 1080 LEU   A CB    1 
ATOM   7927  C  CB    B LEU   A  1  1082 ? -4.199  59.968  102.346 0.50 16.57 ? 1080 LEU   A CB    1 
ATOM   7928  C  CG    A LEU   A  1  1082 ? -5.546  59.464  102.874 0.50 16.56 ? 1080 LEU   A CG    1 
ATOM   7929  C  CG    B LEU   A  1  1082 ? -5.549  59.558  102.932 0.50 16.58 ? 1080 LEU   A CG    1 
ATOM   7930  C  CD1   A LEU   A  1  1082 ? -5.525  57.967  103.078 0.50 16.26 ? 1080 LEU   A CD1   1 
ATOM   7931  C  CD1   B LEU   A  1  1082 ? -5.509  59.735  104.440 0.50 17.00 ? 1080 LEU   A CD1   1 
ATOM   7932  C  CD2   A LEU   A  1  1082 ? -5.877  60.181  104.168 0.50 18.44 ? 1080 LEU   A CD2   1 
ATOM   7933  C  CD2   B LEU   A  1  1082 ? -6.691  60.383  102.323 0.50 17.38 ? 1080 LEU   A CD2   1 
ATOM   7934  N  N     . ASP   A  1  1083 ? -5.467  58.474  99.623  1.00 17.72 ? 1081 ASP   A N     1 
ATOM   7935  C  CA    . ASP   A  1  1083 ? -6.383  58.526  98.486  1.00 19.49 ? 1081 ASP   A CA    1 
ATOM   7936  C  C     . ASP   A  1  1083 ? -7.541  57.593  98.818  1.00 20.25 ? 1081 ASP   A C     1 
ATOM   7937  O  O     . ASP   A  1  1083 ? -7.408  56.373  98.700  1.00 23.03 ? 1081 ASP   A O     1 
ATOM   7938  C  CB    . ASP   A  1  1083 ? -5.646  58.093  97.220  1.00 21.38 ? 1081 ASP   A CB    1 
ATOM   7939  C  CG    . ASP   A  1  1083 ? -6.503  58.180  95.976  1.00 28.30 ? 1081 ASP   A CG    1 
ATOM   7940  O  OD1   . ASP   A  1  1083 ? -7.627  58.712  96.056  1.00 30.77 ? 1081 ASP   A OD1   1 
ATOM   7941  O  OD2   . ASP   A  1  1083 ? -6.041  57.711  94.909  1.00 33.51 ? 1081 ASP   A OD2   1 
ATOM   7942  N  N     . LEU   A  1  1084 ? -8.665  58.174  99.235  1.00 18.63 ? 1082 LEU   A N     1 
ATOM   7943  C  CA    . LEU   A  1  1084 ? -9.780  57.408  99.756  1.00 18.83 ? 1082 LEU   A CA    1 
ATOM   7944  C  C     . LEU   A  1  1084 ? -11.036 57.705  98.962  1.00 19.39 ? 1082 LEU   A C     1 
ATOM   7945  O  O     . LEU   A  1  1084 ? -11.192 58.787  98.395  1.00 20.64 ? 1082 LEU   A O     1 
ATOM   7946  C  CB    . LEU   A  1  1084 ? -10.070 57.795  101.200 1.00 21.10 ? 1082 LEU   A CB    1 
ATOM   7947  C  CG    . LEU   A  1  1084 ? -8.975  57.563  102.228 1.00 22.77 ? 1082 LEU   A CG    1 
ATOM   7948  C  CD1   . LEU   A  1  1084 ? -9.421  58.191  103.528 1.00 23.37 ? 1082 LEU   A CD1   1 
ATOM   7949  C  CD2   . LEU   A  1  1084 ? -8.741  56.074  102.379 1.00 23.64 ? 1082 LEU   A CD2   1 
ATOM   7950  N  N     . GLU   A  1  1085 ? -11.905 56.714  98.896  1.00 19.01 ? 1083 GLU   A N     1 
ATOM   7951  C  CA    . GLU   A  1  1085 ? -13.269 56.930  98.450  1.00 17.38 ? 1083 GLU   A CA    1 
ATOM   7952  C  C     . GLU   A  1  1085 ? -14.159 56.907  99.679  1.00 19.10 ? 1083 GLU   A C     1 
ATOM   7953  O  O     . GLU   A  1  1085 ? -14.113 55.956  100.469 1.00 21.65 ? 1083 GLU   A O     1 
ATOM   7954  C  CB    . GLU   A  1  1085 ? -13.726 55.872  97.447  1.00 20.53 ? 1083 GLU   A CB    1 
ATOM   7955  C  CG    . GLU   A  1  1085 ? -15.179 56.114  97.058  1.00 20.69 ? 1083 GLU   A CG    1 
ATOM   7956  C  CD    . GLU   A  1  1085 ? -15.686 55.264  95.915  1.00 29.15 ? 1083 GLU   A CD    1 
ATOM   7957  O  OE1   . GLU   A  1  1085 ? -14.872 54.601  95.246  1.00 31.76 ? 1083 GLU   A OE1   1 
ATOM   7958  O  OE2   . GLU   A  1  1085 ? -16.923 55.270  95.691  1.00 27.95 ? 1083 GLU   A OE2   1 
ATOM   7959  N  N     . LEU   A  1  1086 ? -14.941 57.964  99.852  1.00 19.34 ? 1084 LEU   A N     1 
ATOM   7960  C  CA    . LEU   A  1  1086 ? -15.822 58.140  100.997 1.00 17.67 ? 1084 LEU   A CA    1 
ATOM   7961  C  C     . LEU   A  1  1086 ? -17.214 57.612  100.666 1.00 20.97 ? 1084 LEU   A C     1 
ATOM   7962  O  O     . LEU   A  1  1086 ? -17.704 57.809  99.552  1.00 20.51 ? 1084 LEU   A O     1 
ATOM   7963  C  CB    . LEU   A  1  1086 ? -15.924 59.619  101.353 1.00 18.33 ? 1084 LEU   A CB    1 
ATOM   7964  C  CG    . LEU   A  1  1086 ? -14.573 60.271  101.671 1.00 21.17 ? 1084 LEU   A CG    1 
ATOM   7965  C  CD1   . LEU   A  1  1086 ? -14.722 61.720  102.089 1.00 21.31 ? 1084 LEU   A CD1   1 
ATOM   7966  C  CD2   . LEU   A  1  1086 ? -13.808 59.477  102.731 1.00 22.98 ? 1084 LEU   A CD2   1 
ATOM   7967  N  N     . PRO   A  1  1087 ? -17.834 56.923  101.614 1.00 20.08 ? 1085 PRO   A N     1 
ATOM   7968  C  CA    . PRO   A  1  1087 ? -19.192 56.414  101.392 1.00 22.50 ? 1085 PRO   A CA    1 
ATOM   7969  C  C     . PRO   A  1  1087 ? -20.160 57.544  101.104 1.00 19.96 ? 1085 PRO   A C     1 
ATOM   7970  O  O     . PRO   A  1  1087 ? -20.119 58.604  101.728 1.00 23.01 ? 1085 PRO   A O     1 
ATOM   7971  C  CB    . PRO   A  1  1087 ? -19.538 55.730  102.717 1.00 23.46 ? 1085 PRO   A CB    1 
ATOM   7972  C  CG    . PRO   A  1  1087 ? -18.231 55.466  103.373 1.00 26.35 ? 1085 PRO   A CG    1 
ATOM   7973  C  CD    . PRO   A  1  1087 ? -17.269 56.505  102.904 1.00 20.88 ? 1085 PRO   A CD    1 
ATOM   7974  N  N     . GLY   A  1  1088 ? -21.043 57.305  100.144 1.00 20.04 ? 1086 GLY   A N     1 
ATOM   7975  C  CA    . GLY   A  1  1088 ? -22.038 58.280  99.789  1.00 23.02 ? 1086 GLY   A CA    1 
ATOM   7976  C  C     . GLY   A  1  1088 ? -23.142 57.664  98.961  1.00 18.57 ? 1086 GLY   A C     1 
ATOM   7977  O  O     . GLY   A  1  1088 ? -23.341 56.445  98.936  1.00 19.11 ? 1086 GLY   A O     1 
ATOM   7978  N  N     . PRO   A  1  1089 ? -23.868 58.506  98.244  1.00 20.24 ? 1087 PRO   A N     1 
ATOM   7979  C  CA    . PRO   A  1  1089 ? -24.973 58.007  97.428  1.00 20.08 ? 1087 PRO   A CA    1 
ATOM   7980  C  C     . PRO   A  1  1089 ? -24.460 57.219  96.234  1.00 19.46 ? 1087 PRO   A C     1 
ATOM   7981  O  O     . PRO   A  1  1089 ? -23.313 57.362  95.791  1.00 19.71 ? 1087 PRO   A O     1 
ATOM   7982  C  CB    . PRO   A  1  1089 ? -25.670 59.290  96.969  1.00 22.97 ? 1087 PRO   A CB    1 
ATOM   7983  C  CG    . PRO   A  1  1089 ? -24.535 60.293  96.907  1.00 24.32 ? 1087 PRO   A CG    1 
ATOM   7984  C  CD    . PRO   A  1  1089 ? -23.658 59.955  98.084  1.00 20.47 ? 1087 PRO   A CD    1 
ATOM   7985  N  N     . VAL   A  1  1090 ? -25.338 56.357  95.723  1.00 19.35 ? 1088 VAL   A N     1 
ATOM   7986  C  CA    . VAL   A  1  1090 ? -25.066 55.698  94.455  1.00 16.82 ? 1088 VAL   A CA    1 
ATOM   7987  C  C     . VAL   A  1  1090 ? -24.952 56.741  93.348  1.00 16.56 ? 1088 VAL   A C     1 
ATOM   7988  O  O     . VAL   A  1  1090 ? -25.431 57.877  93.461  1.00 18.42 ? 1088 VAL   A O     1 
ATOM   7989  C  CB    . VAL   A  1  1090 ? -26.143 54.660  94.105  1.00 18.81 ? 1088 VAL   A CB    1 
ATOM   7990  C  CG1   . VAL   A  1  1090 ? -26.242 53.601  95.192  1.00 19.79 ? 1088 VAL   A CG1   1 
ATOM   7991  C  CG2   . VAL   A  1  1090 ? -27.486 55.340  93.895  1.00 19.98 ? 1088 VAL   A CG2   1 
ATOM   7992  N  N     . GLY   A  1  1091 ? -24.285 56.350  92.267  1.00 16.82 ? 1089 GLY   A N     1 
ATOM   7993  C  CA    . GLY   A  1  1091 ? -24.194 57.224  91.115  1.00 19.28 ? 1089 GLY   A CA    1 
ATOM   7994  C  C     . GLY   A  1  1091 ? -23.254 58.381  91.312  1.00 17.11 ? 1089 GLY   A C     1 
ATOM   7995  O  O     . GLY   A  1  1091 ? -23.285 59.344  90.547  1.00 16.85 ? 1089 GLY   A O     1 
ATOM   7996  N  N     . GLU   A  1  1092 ? -22.397 58.295  92.322  1.00 17.35 ? 1090 GLU   A N     1 
ATOM   7997  C  CA    . GLU   A  1  1092 ? -21.416 59.327  92.593  1.00 18.53 ? 1090 GLU   A CA    1 
ATOM   7998  C  C     . GLU   A  1  1092 ? -20.198 58.642  93.187  1.00 19.37 ? 1090 GLU   A C     1 
ATOM   7999  O  O     . GLU   A  1  1092 ? -20.326 57.661  93.925  1.00 19.92 ? 1090 GLU   A O     1 
ATOM   8000  C  CB    . GLU   A  1  1092 ? -21.981 60.310  93.618  1.00 21.30 ? 1090 GLU   A CB    1 
ATOM   8001  C  CG    . GLU   A  1  1092 ? -21.512 61.736  93.470  1.00 26.41 ? 1090 GLU   A CG    1 
ATOM   8002  C  CD    . GLU   A  1  1092 ? -22.284 62.661  94.384  1.00 24.44 ? 1090 GLU   A CD    1 
ATOM   8003  O  OE1   . GLU   A  1  1092 ? -22.099 62.553  95.610  1.00 22.20 ? 1090 GLU   A OE1   1 
ATOM   8004  O  OE2   . GLU   A  1  1092 ? -23.093 63.470  93.876  1.00 27.31 ? 1090 GLU   A OE2   1 
ATOM   8005  N  N     . ARG   A  1  1093 ? -19.020 59.145  92.849  1.00 16.82 ? 1091 ARG   A N     1 
ATOM   8006  C  CA    . ARG   A  1  1093 ? -17.782 58.715  93.482  1.00 17.29 ? 1091 ARG   A CA    1 
ATOM   8007  C  C     . ARG   A  1  1093 ? -17.213 59.928  94.194  1.00 16.10 ? 1091 ARG   A C     1 
ATOM   8008  O  O     . ARG   A  1  1093 ? -16.991 60.974  93.577  1.00 17.42 ? 1091 ARG   A O     1 
ATOM   8009  C  CB    . ARG   A  1  1093 ? -16.783 58.164  92.463  1.00 20.11 ? 1091 ARG   A CB    1 
ATOM   8010  N  N     . ASN   A  1  1094 ? -17.019 59.802  95.496  1.00 16.32 ? 1092 ASN   A N     1 
ATOM   8011  C  CA    . ASN   A  1  1094 ? -16.577 60.921  96.307  1.00 14.93 ? 1092 ASN   A CA    1 
ATOM   8012  C  C     . ASN   A  1  1094 ? -15.209 60.586  96.868  1.00 16.18 ? 1092 ASN   A C     1 
ATOM   8013  O  O     . ASN   A  1  1094 ? -15.064 59.643  97.653  1.00 18.17 ? 1092 ASN   A O     1 
ATOM   8014  C  CB    . ASN   A  1  1094 ? -17.614 61.221  97.372  1.00 15.34 ? 1092 ASN   A CB    1 
ATOM   8015  C  CG    . ASN   A  1  1094 ? -18.831 61.866  96.775  1.00 15.90 ? 1092 ASN   A CG    1 
ATOM   8016  O  OD1   . ASN   A  1  1094 ? -18.753 62.997  96.310  1.00 16.89 ? 1092 ASN   A OD1   1 
ATOM   8017  N  ND2   . ASN   A  1  1094 ? -19.959 61.149  96.753  1.00 18.63 ? 1092 ASN   A ND2   1 
ATOM   8018  N  N     . LEU   A  1  1095 ? -14.209 61.331  96.418  1.00 16.39 ? 1093 LEU   A N     1 
ATOM   8019  C  CA    . LEU   A  1  1095 ? -12.821 61.013  96.686  1.00 16.10 ? 1093 LEU   A CA    1 
ATOM   8020  C  C     . LEU   A  1  1095 ? -12.215 62.071  97.585  1.00 16.74 ? 1093 LEU   A C     1 
ATOM   8021  O  O     . LEU   A  1  1095 ? -12.557 63.251  97.521  1.00 17.35 ? 1093 LEU   A O     1 
ATOM   8022  C  CB    . LEU   A  1  1095 ? -12.028 60.955  95.384  1.00 18.31 ? 1093 LEU   A CB    1 
ATOM   8023  C  CG    . LEU   A  1  1095 ? -12.651 60.016  94.346  1.00 22.34 ? 1093 LEU   A CG    1 
ATOM   8024  C  CD1   . LEU   A  1  1095 ? -11.826 60.016  93.076  1.00 25.80 ? 1093 LEU   A CD1   1 
ATOM   8025  C  CD2   . LEU   A  1  1095 ? -12.805 58.602  94.903  1.00 22.41 ? 1093 LEU   A CD2   1 
ATOM   8026  N  N     . TYR   A  1  1096 ? -11.274 61.625  98.401  1.00 16.36 ? 1094 TYR   A N     1 
ATOM   8027  C  CA    . TYR   A  1  1096 ? -10.620 62.482  99.375  1.00 15.73 ? 1094 TYR   A CA    1 
ATOM   8028  C  C     . TYR   A  1  1096 ? -9.148  62.146  99.326  1.00 15.88 ? 1094 TYR   A C     1 
ATOM   8029  O  O     . TYR   A  1  1096 ? -8.776  60.982  99.502  1.00 16.98 ? 1094 TYR   A O     1 
ATOM   8030  C  CB    . TYR   A  1  1096 ? -11.189 62.182  100.753 1.00 16.62 ? 1094 TYR   A CB    1 
ATOM   8031  C  CG    . TYR   A  1  1096 ? -10.492 62.877  101.889 1.00 17.06 ? 1094 TYR   A CG    1 
ATOM   8032  C  CD1   . TYR   A  1  1096 ? -10.838 64.171  102.258 1.00 17.84 ? 1094 TYR   A CD1   1 
ATOM   8033  C  CD2   . TYR   A  1  1096 ? -9.512  62.226  102.620 1.00 18.41 ? 1094 TYR   A CD2   1 
ATOM   8034  C  CE1   . TYR   A  1  1096 ? -10.207 64.802  103.328 1.00 17.41 ? 1094 TYR   A CE1   1 
ATOM   8035  C  CE2   . TYR   A  1  1096 ? -8.881  62.846  103.696 1.00 18.29 ? 1094 TYR   A CE2   1 
ATOM   8036  C  CZ    . TYR   A  1  1096 ? -9.227  64.132  104.035 1.00 16.59 ? 1094 TYR   A CZ    1 
ATOM   8037  O  OH    . TYR   A  1  1096 ? -8.612  64.740  105.102 1.00 17.97 ? 1094 TYR   A OH    1 
ATOM   8038  N  N     . THR   A  1  1097 ? -8.325  63.147  99.062  1.00 16.01 ? 1095 THR   A N     1 
ATOM   8039  C  CA    . THR   A  1  1097 ? -6.910  62.907  98.837  1.00 15.86 ? 1095 THR   A CA    1 
ATOM   8040  C  C     . THR   A  1  1097 ? -6.099  63.966  99.566  1.00 16.91 ? 1095 THR   A C     1 
ATOM   8041  O  O     . THR   A  1  1097 ? -6.550  65.095  99.762  1.00 17.01 ? 1095 THR   A O     1 
ATOM   8042  C  CB    . THR   A  1  1097 ? -6.582  62.954  97.340  1.00 19.39 ? 1095 THR   A CB    1 
ATOM   8043  O  OG1   . THR   A  1  1097 ? -6.957  64.229  96.817  1.00 23.78 ? 1095 THR   A OG1   1 
ATOM   8044  C  CG2   . THR   A  1  1097 ? -7.339  61.891  96.590  1.00 20.67 ? 1095 THR   A CG2   1 
ATOM   8045  N  N     . LEU   A  1  1098 ? -4.891  63.589  99.974  1.00 16.22 ? 1096 LEU   A N     1 
ATOM   8046  C  CA    . LEU   A  1  1098 ? -3.962  64.514  100.609 1.00 16.93 ? 1096 LEU   A CA    1 
ATOM   8047  C  C     . LEU   A  1  1098 ? -2.801  64.796  99.669  1.00 15.30 ? 1096 LEU   A C     1 
ATOM   8048  O  O     . LEU   A  1  1098 ? -2.110  63.871  99.225  1.00 16.09 ? 1096 LEU   A O     1 
ATOM   8049  C  CB    . LEU   A  1  1098 ? -3.459  63.962  101.934 1.00 16.94 ? 1096 LEU   A CB    1 
ATOM   8050  C  CG    . LEU   A  1  1098 ? -4.585  63.742  102.939 1.00 15.35 ? 1096 LEU   A CG    1 
ATOM   8051  C  CD1   . LEU   A  1  1098 ? -3.943  63.245  104.212 1.00 17.81 ? 1096 LEU   A CD1   1 
ATOM   8052  C  CD2   . LEU   A  1  1098 ? -5.393  65.019  103.189 1.00 16.53 ? 1096 LEU   A CD2   1 
ATOM   8053  N  N     . HIS   A  1  1099 ? -2.597  66.072  99.374  1.00 14.98 ? 1097 HIS   A N     1 
ATOM   8054  C  CA    . HIS   A  1  1099 ? -1.566  66.550  98.469  1.00 15.47 ? 1097 HIS   A CA    1 
ATOM   8055  C  C     . HIS   A  1  1099 ? -0.649  67.494  99.226  1.00 17.01 ? 1097 HIS   A C     1 
ATOM   8056  O  O     . HIS   A  1  1099 ? -0.905  67.873  100.366 1.00 16.64 ? 1097 HIS   A O     1 
ATOM   8057  C  CB    . HIS   A  1  1099 ? -2.194  67.334  97.314  1.00 17.96 ? 1097 HIS   A CB    1 
ATOM   8058  C  CG    . HIS   A  1  1099 ? -3.167  66.538  96.511  1.00 19.22 ? 1097 HIS   A CG    1 
ATOM   8059  N  ND1   . HIS   A  1  1099 ? -2.843  65.990  95.292  1.00 24.26 ? 1097 HIS   A ND1   1 
ATOM   8060  C  CD2   . HIS   A  1  1099 ? -4.451  66.190  96.755  1.00 20.51 ? 1097 HIS   A CD2   1 
ATOM   8061  C  CE1   . HIS   A  1  1099 ? -3.892  65.344  94.811  1.00 25.60 ? 1097 HIS   A CE1   1 
ATOM   8062  N  NE2   . HIS   A  1  1099 ? -4.879  65.450  95.679  1.00 24.25 ? 1097 HIS   A NE2   1 
ATOM   8063  N  N     . ALA   A  1  1100 ? 0.424   67.895  98.562  1.00 16.81 ? 1098 ALA   A N     1 
ATOM   8064  C  CA    . ALA   A  1  1100 ? 1.249   68.942  99.127  1.00 17.68 ? 1098 ALA   A CA    1 
ATOM   8065  C  C     . ALA   A  1  1100 ? 0.464   70.245  99.170  1.00 18.88 ? 1098 ALA   A C     1 
ATOM   8066  O  O     . ALA   A  1  1100 ? -0.458  70.467  98.380  1.00 19.62 ? 1098 ALA   A O     1 
ATOM   8067  C  CB    . ALA   A  1  1100 ? 2.491   69.129  98.265  1.00 16.68 ? 1098 ALA   A CB    1 
ATOM   8068  N  N     . ARG   A  1  1101 ? 0.804   71.094  100.140 1.00 18.31 ? 1099 ARG   A N     1 
ATOM   8069  C  CA    A ARG   A  1  1101 ? 0.191   72.415  100.197 0.53 19.83 ? 1099 ARG   A CA    1 
ATOM   8070  C  CA    B ARG   A  1  1101 ? 0.201   72.419  100.208 0.47 19.83 ? 1099 ARG   A CA    1 
ATOM   8071  C  C     . ARG   A  1  1101 ? 0.765   73.340  99.138  1.00 18.27 ? 1099 ARG   A C     1 
ATOM   8072  O  O     . ARG   A  1  1101 ? 0.031   74.136  98.546  1.00 20.79 ? 1099 ARG   A O     1 
ATOM   8073  C  CB    A ARG   A  1  1101 ? 0.378   73.041  101.577 0.53 22.19 ? 1099 ARG   A CB    1 
ATOM   8074  C  CB    B ARG   A  1  1101 ? 0.441   73.021  101.588 0.47 22.19 ? 1099 ARG   A CB    1 
ATOM   8075  C  CG    A ARG   A  1  1101 ? -0.333  72.306  102.684 0.53 20.89 ? 1099 ARG   A CG    1 
ATOM   8076  C  CG    B ARG   A  1  1101 ? -0.425  72.429  102.664 0.47 21.00 ? 1099 ARG   A CG    1 
ATOM   8077  C  CD    A ARG   A  1  1101 ? -0.214  73.043  104.006 0.53 19.76 ? 1099 ARG   A CD    1 
ATOM   8078  C  CD    B ARG   A  1  1101 ? -1.241  73.523  103.306 0.47 22.40 ? 1099 ARG   A CD    1 
ATOM   8079  N  NE    A ARG   A  1  1101 ? -1.077  74.213  104.103 0.53 18.53 ? 1099 ARG   A NE    1 
ATOM   8080  N  NE    B ARG   A  1  1101 ? -2.296  72.999  104.160 0.47 20.18 ? 1099 ARG   A NE    1 
ATOM   8081  C  CZ    A ARG   A  1  1101 ? -2.333  74.177  104.528 0.53 20.05 ? 1099 ARG   A CZ    1 
ATOM   8082  C  CZ    B ARG   A  1  1101 ? -3.046  73.751  104.952 0.47 22.30 ? 1099 ARG   A CZ    1 
ATOM   8083  N  NH1   A ARG   A  1  1101 ? -2.907  73.041  104.890 0.53 22.40 ? 1099 ARG   A NH1   1 
ATOM   8084  N  NH1   B ARG   A  1  1101 ? -2.873  75.063  105.030 0.47 21.02 ? 1099 ARG   A NH1   1 
ATOM   8085  N  NH2   A ARG   A  1  1101 ? -3.030  75.307  104.589 0.53 21.10 ? 1099 ARG   A NH2   1 
ATOM   8086  N  NH2   B ARG   A  1  1101 ? -3.985  73.174  105.691 0.47 18.34 ? 1099 ARG   A NH2   1 
ATOM   8087  N  N     . GLY   A  1  1102 ? 2.061   73.250  98.884  1.00 17.40 ? 1100 GLY   A N     1 
ATOM   8088  C  CA    . GLY   A  1  1102 ? 2.684   74.131  97.923  1.00 20.10 ? 1100 GLY   A CA    1 
ATOM   8089  C  C     . GLY   A  1  1102 ? 4.061   74.524  98.400  1.00 18.86 ? 1100 GLY   A C     1 
ATOM   8090  O  O     . GLY   A  1  1102 ? 4.902   73.665  98.677  1.00 20.61 ? 1100 GLY   A O     1 
ATOM   8091  N  N     . ARG   A  1  1103 ? 4.309   75.818  98.517  1.00 17.53 ? 1101 ARG   A N     1 
ATOM   8092  C  CA    . ARG   A  1  1103 ? 5.598   76.302  98.982  1.00 18.25 ? 1101 ARG   A CA    1 
ATOM   8093  C  C     . ARG   A  1  1103 ? 5.431   76.774  100.417 1.00 19.07 ? 1101 ARG   A C     1 
ATOM   8094  O  O     . ARG   A  1  1103 ? 4.594   77.642  100.702 1.00 20.13 ? 1101 ARG   A O     1 
ATOM   8095  C  CB    . ARG   A  1  1103 ? 6.131   77.428  98.097  1.00 19.00 ? 1101 ARG   A CB    1 
ATOM   8096  C  CG    . ARG   A  1  1103 ? 7.525   77.889  98.522  1.00 25.07 ? 1101 ARG   A CG    1 
ATOM   8097  C  CD    . ARG   A  1  1103 ? 8.207   78.635  97.396  1.00 28.36 ? 1101 ARG   A CD    1 
ATOM   8098  N  NE    . ARG   A  1  1103 ? 8.507   77.703  96.316  1.00 32.62 ? 1101 ARG   A NE    1 
ATOM   8099  C  CZ    . ARG   A  1  1103 ? 8.598   78.022  95.034  1.00 42.78 ? 1101 ARG   A CZ    1 
ATOM   8100  N  NH1   . ARG   A  1  1103 ? 8.355   79.252  94.607  1.00 49.01 ? 1101 ARG   A NH1   1 
ATOM   8101  N  NH2   . ARG   A  1  1103 ? 8.942   77.082  94.157  1.00 35.52 ? 1101 ARG   A NH2   1 
ATOM   8102  N  N     . ILE   A  1  1104 ? 6.200   76.177  101.318 1.00 16.99 ? 1102 ILE   A N     1 
ATOM   8103  C  CA    . ILE   A  1  1104 ? 6.129   76.486  102.740 1.00 18.24 ? 1102 ILE   A CA    1 
ATOM   8104  C  C     . ILE   A  1  1104 ? 7.252   77.454  103.058 1.00 18.38 ? 1102 ILE   A C     1 
ATOM   8105  O  O     . ILE   A  1  1104 ? 8.407   77.215  102.684 1.00 18.46 ? 1102 ILE   A O     1 
ATOM   8106  C  CB    . ILE   A  1  1104 ? 6.277   75.211  103.585 1.00 18.60 ? 1102 ILE   A CB    1 
ATOM   8107  C  CG1   . ILE   A  1  1104 ? 5.260   74.148  103.154 1.00 19.91 ? 1102 ILE   A CG1   1 
ATOM   8108  C  CG2   . ILE   A  1  1104 ? 6.140   75.543  105.077 1.00 18.79 ? 1102 ILE   A CG2   1 
ATOM   8109  C  CD1   . ILE   A  1  1104 ? 3.829   74.543  103.357 1.00 20.85 ? 1102 ILE   A CD1   1 
ATOM   8110  N  N     . LEU   A  1  1105 ? 6.925   78.549  103.736 1.00 17.51 ? 1103 LEU   A N     1 
ATOM   8111  C  CA    . LEU   A  1  1105 ? 7.951   79.460  104.223 1.00 19.57 ? 1103 LEU   A CA    1 
ATOM   8112  C  C     . LEU   A  1  1105 ? 8.599   78.853  105.461 1.00 18.18 ? 1103 LEU   A C     1 
ATOM   8113  O  O     . LEU   A  1  1105 ? 7.907   78.527  106.428 1.00 20.62 ? 1103 LEU   A O     1 
ATOM   8114  C  CB    . LEU   A  1  1105 ? 7.319   80.804  104.568 1.00 21.43 ? 1103 LEU   A CB    1 
ATOM   8115  C  CG    . LEU   A  1  1105 ? 8.244   81.815  105.251 1.00 23.97 ? 1103 LEU   A CG    1 
ATOM   8116  C  CD1   . LEU   A  1  1105 ? 9.355   82.249  104.301 1.00 23.93 ? 1103 LEU   A CD1   1 
ATOM   8117  C  CD2   . LEU   A  1  1105 ? 7.445   83.013  105.728 1.00 24.58 ? 1103 LEU   A CD2   1 
ATOM   8118  N  N     . LEU   A  1  1106 ? 9.911   78.671  105.428 1.00 18.38 ? 1104 LEU   A N     1 
ATOM   8119  C  CA    . LEU   A  1  1106 ? 10.639  78.186  106.590 1.00 20.79 ? 1104 LEU   A CA    1 
ATOM   8120  C  C     . LEU   A  1  1106 ? 11.378  79.350  107.214 1.00 22.42 ? 1104 LEU   A C     1 
ATOM   8121  O  O     . LEU   A  1  1106 ? 12.150  80.035  106.536 1.00 20.99 ? 1104 LEU   A O     1 
ATOM   8122  C  CB    . LEU   A  1  1106 ? 11.657  77.112  106.216 1.00 19.87 ? 1104 LEU   A CB    1 
ATOM   8123  C  CG    . LEU   A  1  1106 ? 11.140  75.873  105.502 1.00 23.68 ? 1104 LEU   A CG    1 
ATOM   8124  C  CD1   . LEU   A  1  1106 ? 12.178  74.768  105.542 1.00 21.82 ? 1104 LEU   A CD1   1 
ATOM   8125  C  CD2   . LEU   A  1  1106 ? 9.812   75.383  106.034 1.00 23.02 ? 1104 LEU   A CD2   1 
ATOM   8126  N  N     . VAL   A  1  1107 ? 11.163  79.548  108.508 1.00 19.39 ? 1105 VAL   A N     1 
ATOM   8127  C  CA    . VAL   A  1  1107 ? 11.873  80.578  109.255 1.00 20.56 ? 1105 VAL   A CA    1 
ATOM   8128  C  C     . VAL   A  1  1107 ? 12.642  79.866  110.360 1.00 20.90 ? 1105 VAL   A C     1 
ATOM   8129  O  O     . VAL   A  1  1107 ? 12.160  79.766  111.494 1.00 21.67 ? 1105 VAL   A O     1 
ATOM   8130  C  CB    . VAL   A  1  1107 ? 10.907  81.647  109.788 1.00 20.98 ? 1105 VAL   A CB    1 
ATOM   8131  C  CG1   . VAL   A  1  1107 ? 11.687  82.828  110.315 1.00 22.91 ? 1105 VAL   A CG1   1 
ATOM   8132  C  CG2   . VAL   A  1  1107 ? 9.955   82.103  108.674 1.00 22.46 ? 1105 VAL   A CG2   1 
ATOM   8133  N  N     . PRO   A  1  1108 ? 13.819  79.330  110.069 1.00 20.25 ? 1106 PRO   A N     1 
ATOM   8134  C  CA    . PRO   A  1  1108 ? 14.574  78.587  111.077 1.00 21.84 ? 1106 PRO   A CA    1 
ATOM   8135  C  C     . PRO   A  1  1108 ? 15.432  79.520  111.918 1.00 23.84 ? 1106 PRO   A C     1 
ATOM   8136  O  O     . PRO   A  1  1108 ? 15.679  80.672  111.564 1.00 24.80 ? 1106 PRO   A O     1 
ATOM   8137  C  CB    . PRO   A  1  1108 ? 15.477  77.691  110.221 1.00 22.92 ? 1106 PRO   A CB    1 
ATOM   8138  C  CG    . PRO   A  1  1108 ? 15.733  78.516  109.004 1.00 22.96 ? 1106 PRO   A CG    1 
ATOM   8139  C  CD    . PRO   A  1  1108 ? 14.446  79.256  108.737 1.00 23.55 ? 1106 PRO   A CD    1 
ATOM   8140  N  N     . ALA   A  1  1109 ? 15.875  78.991  113.053 1.00 21.35 ? 1107 ALA   A N     1 
ATOM   8141  C  CA    . ALA   A  1  1109 ? 16.849  79.662  113.906 1.00 23.78 ? 1107 ALA   A CA    1 
ATOM   8142  C  C     . ALA   A  1  1109 ? 18.171  78.922  113.982 1.00 28.02 ? 1107 ALA   A C     1 
ATOM   8143  O  O     . ALA   A  1  1109 ? 19.227  79.552  114.039 1.00 28.27 ? 1107 ALA   A O     1 
ATOM   8144  C  CB    . ALA   A  1  1109 ? 16.288  79.849  115.325 1.00 24.24 ? 1107 ALA   A CB    1 
ATOM   8145  N  N     . THR   A  1  1110 ? 18.143  77.596  113.983 1.00 22.99 ? 1108 THR   A N     1 
ATOM   8146  C  CA    . THR   A  1  1110 ? 19.343  76.794  114.107 1.00 22.98 ? 1108 THR   A CA    1 
ATOM   8147  C  C     . THR   A  1  1110 ? 19.424  75.843  112.927 1.00 23.31 ? 1108 THR   A C     1 
ATOM   8148  O  O     . THR   A  1  1110 ? 18.439  75.596  112.226 1.00 20.91 ? 1108 THR   A O     1 
ATOM   8149  C  CB    . THR   A  1  1110 ? 19.327  75.964  115.395 1.00 25.50 ? 1108 THR   A CB    1 
ATOM   8150  O  OG1   . THR   A  1  1110 ? 18.227  75.048  115.352 1.00 23.72 ? 1108 THR   A OG1   1 
ATOM   8151  C  CG2   . THR   A  1  1110 ? 19.182  76.864  116.611 1.00 25.16 ? 1108 THR   A CG2   1 
ATOM   8152  N  N     . GLU   A  1  1111 ? 20.616  75.303  112.717 1.00 24.49 ? 1109 GLU   A N     1 
ATOM   8153  C  CA    . GLU   A  1  1111 ? 20.785  74.327  111.649 1.00 21.46 ? 1109 GLU   A CA    1 
ATOM   8154  C  C     . GLU   A  1  1111 ? 19.887  73.116  111.866 1.00 24.19 ? 1109 GLU   A C     1 
ATOM   8155  O  O     . GLU   A  1  1111 ? 19.196  72.672  110.943 1.00 21.14 ? 1109 GLU   A O     1 
ATOM   8156  C  CB    . GLU   A  1  1111 ? 22.250  73.919  111.560 1.00 24.61 ? 1109 GLU   A CB    1 
ATOM   8157  C  CG    . GLU   A  1  1111 ? 22.477  72.724  110.655 1.00 25.64 ? 1109 GLU   A CG    1 
ATOM   8158  C  CD    . GLU   A  1  1111 ? 23.945  72.445  110.444 1.00 29.03 ? 1109 GLU   A CD    1 
ATOM   8159  O  OE1   . GLU   A  1  1111 ? 24.595  73.244  109.741 1.00 29.30 ? 1109 GLU   A OE1   1 
ATOM   8160  O  OE2   . GLU   A  1  1111 ? 24.445  71.442  110.994 1.00 31.94 ? 1109 GLU   A OE2   1 
ATOM   8161  N  N     . SER   A  1  1112 ? 19.866  72.575  113.087 1.00 23.73 ? 1110 SER   A N     1 
ATOM   8162  C  CA    . SER   A  1  1112 ? 19.031  71.408  113.347 1.00 24.98 ? 1110 SER   A CA    1 
ATOM   8163  C  C     . SER   A  1  1112 ? 17.563  71.741  113.153 1.00 21.94 ? 1110 SER   A C     1 
ATOM   8164  O  O     . SER   A  1  1112 ? 16.811  70.943  112.583 1.00 21.94 ? 1110 SER   A O     1 
ATOM   8165  C  CB    . SER   A  1  1112 ? 19.274  70.858  114.751 1.00 26.58 ? 1110 SER   A CB    1 
ATOM   8166  O  OG    . SER   A  1  1112 ? 18.504  69.683  114.958 1.00 25.86 ? 1110 SER   A OG    1 
ATOM   8167  N  N     . GLY   A  1  1113 ? 17.136  72.921  113.609 1.00 21.54 ? 1111 GLY   A N     1 
ATOM   8168  C  CA    . GLY   A  1  1113 ? 15.769  73.339  113.354 1.00 18.33 ? 1111 GLY   A CA    1 
ATOM   8169  C  C     . GLY   A  1  1113 ? 15.466  73.410  111.870 1.00 19.25 ? 1111 GLY   A C     1 
ATOM   8170  O  O     . GLY   A  1  1113 ? 14.393  72.986  111.422 1.00 20.33 ? 1111 GLY   A O     1 
ATOM   8171  N  N     . LEU   A  1  1114 ? 16.406  73.942  111.085 1.00 19.20 ? 1112 LEU   A N     1 
ATOM   8172  C  CA    . LEU   A  1  1114 ? 16.207  73.997  109.640 1.00 20.25 ? 1112 LEU   A CA    1 
ATOM   8173  C  C     . LEU   A  1  1114 ? 16.030  72.600  109.063 1.00 19.82 ? 1112 LEU   A C     1 
ATOM   8174  O  O     . LEU   A  1  1114 ? 15.126  72.360  108.255 1.00 18.85 ? 1112 LEU   A O     1 
ATOM   8175  C  CB    . LEU   A  1  1114 ? 17.380  74.701  108.959 1.00 21.27 ? 1112 LEU   A CB    1 
ATOM   8176  C  CG    . LEU   A  1  1114 ? 17.330  74.655  107.424 1.00 20.61 ? 1112 LEU   A CG    1 
ATOM   8177  C  CD1   . LEU   A  1  1114 ? 16.000  75.192  106.883 1.00 22.52 ? 1112 LEU   A CD1   1 
ATOM   8178  C  CD2   . LEU   A  1  1114 ? 18.494  75.423  106.836 1.00 24.61 ? 1112 LEU   A CD2   1 
ATOM   8179  N  N     . TYR   A  1  1115 ? 16.884  71.664  109.470 1.00 20.16 ? 1113 TYR   A N     1 
ATOM   8180  C  CA    . TYR   A  1  1115 ? 16.779  70.305  108.952 1.00 18.25 ? 1113 TYR   A CA    1 
ATOM   8181  C  C     . TYR   A  1  1115 ? 15.448  69.669  109.329 1.00 19.88 ? 1113 TYR   A C     1 
ATOM   8182  O  O     . TYR   A  1  1115 ? 14.834  68.975  108.512 1.00 19.46 ? 1113 TYR   A O     1 
ATOM   8183  C  CB    . TYR   A  1  1115 ? 17.927  69.454  109.474 1.00 19.45 ? 1113 TYR   A CB    1 
ATOM   8184  C  CG    . TYR   A  1  1115 ? 19.294  69.869  108.975 1.00 18.78 ? 1113 TYR   A CG    1 
ATOM   8185  C  CD1   . TYR   A  1  1115 ? 19.432  70.730  107.892 1.00 19.27 ? 1113 TYR   A CD1   1 
ATOM   8186  C  CD2   . TYR   A  1  1115 ? 20.439  69.395  109.586 1.00 23.96 ? 1113 TYR   A CD2   1 
ATOM   8187  C  CE1   . TYR   A  1  1115 ? 20.690  71.100  107.418 1.00 23.65 ? 1113 TYR   A CE1   1 
ATOM   8188  C  CE2   . TYR   A  1  1115 ? 21.691  69.753  109.126 1.00 21.62 ? 1113 TYR   A CE2   1 
ATOM   8189  C  CZ    . TYR   A  1  1115 ? 21.802  70.610  108.042 1.00 22.75 ? 1113 TYR   A CZ    1 
ATOM   8190  O  OH    . TYR   A  1  1115 ? 23.058  70.973  107.602 1.00 24.95 ? 1113 TYR   A OH    1 
ATOM   8191  N  N     . HIS   A  1  1116 ? 14.990  69.884  110.566 1.00 19.86 ? 1114 HIS   A N     1 
ATOM   8192  C  CA    . HIS   A  1  1116 ? 13.687  69.363  110.966 1.00 18.43 ? 1114 HIS   A CA    1 
ATOM   8193  C  C     . HIS   A  1  1116 ? 12.556  70.021  110.182 1.00 18.29 ? 1114 HIS   A C     1 
ATOM   8194  O  O     . HIS   A  1  1116 ? 11.589  69.349  109.792 1.00 19.09 ? 1114 HIS   A O     1 
ATOM   8195  C  CB    . HIS   A  1  1116 ? 13.479  69.549  112.469 1.00 22.30 ? 1114 HIS   A CB    1 
ATOM   8196  C  CG    . HIS   A  1  1116 ? 14.140  68.502  113.312 1.00 23.09 ? 1114 HIS   A CG    1 
ATOM   8197  N  ND1   . HIS   A  1  1116 ? 15.444  68.609  113.753 1.00 26.05 ? 1114 HIS   A ND1   1 
ATOM   8198  C  CD2   . HIS   A  1  1116 ? 13.672  67.331  113.806 1.00 23.88 ? 1114 HIS   A CD2   1 
ATOM   8199  C  CE1   . HIS   A  1  1116 ? 15.748  67.549  114.481 1.00 24.38 ? 1114 HIS   A CE1   1 
ATOM   8200  N  NE2   . HIS   A  1  1116 ? 14.693  66.756  114.525 1.00 29.26 ? 1114 HIS   A NE2   1 
ATOM   8201  N  N     . GLN   A  1  1117 ? 12.630  71.340  109.972 1.00 18.74 ? 1115 GLN   A N     1 
ATOM   8202  C  CA    . GLN   A  1  1117 ? 11.593  72.011  109.192 1.00 18.73 ? 1115 GLN   A CA    1 
ATOM   8203  C  C     . GLN   A  1  1117 ? 11.573  71.485  107.772 1.00 17.60 ? 1115 GLN   A C     1 
ATOM   8204  O  O     . GLN   A  1  1117 ? 10.506  71.232  107.204 1.00 18.27 ? 1115 GLN   A O     1 
ATOM   8205  C  CB    . GLN   A  1  1117 ? 11.825  73.521  109.160 1.00 19.91 ? 1115 GLN   A CB    1 
ATOM   8206  C  CG    . GLN   A  1  1117 ? 11.656  74.206  110.480 1.00 19.39 ? 1115 GLN   A CG    1 
ATOM   8207  C  CD    . GLN   A  1  1117 ? 11.903  75.690  110.383 1.00 23.74 ? 1115 GLN   A CD    1 
ATOM   8208  O  OE1   . GLN   A  1  1117 ? 12.477  76.173  109.405 1.00 20.80 ? 1115 GLN   A OE1   1 
ATOM   8209  N  NE2   . GLN   A  1  1117 ? 11.472  76.425  111.400 1.00 20.19 ? 1115 GLN   A NE2   1 
ATOM   8210  N  N     . LEU   A  1  1118 ? 12.755  71.366  107.167 1.00 16.77 ? 1116 LEU   A N     1 
ATOM   8211  C  CA    A LEU   A  1  1118 ? 12.837  70.877  105.800 0.49 17.26 ? 1116 LEU   A CA    1 
ATOM   8212  C  CA    B LEU   A  1  1118 ? 12.854  70.863  105.802 0.51 17.27 ? 1116 LEU   A CA    1 
ATOM   8213  C  C     . LEU   A  1  1118 ? 12.317  69.450  105.704 1.00 18.45 ? 1116 LEU   A C     1 
ATOM   8214  O  O     . LEU   A  1  1118 ? 11.592  69.114  104.765 1.00 17.94 ? 1116 LEU   A O     1 
ATOM   8215  C  CB    A LEU   A  1  1118 ? 14.279  70.993  105.298 0.49 19.33 ? 1116 LEU   A CB    1 
ATOM   8216  C  CB    B LEU   A  1  1118 ? 14.312  70.882  105.354 0.51 19.36 ? 1116 LEU   A CB    1 
ATOM   8217  C  CG    A LEU   A  1  1118 ? 14.552  70.787  103.810 0.49 19.09 ? 1116 LEU   A CG    1 
ATOM   8218  C  CG    B LEU   A  1  1118 ? 14.839  72.222  104.875 0.51 19.17 ? 1116 LEU   A CG    1 
ATOM   8219  C  CD1   A LEU   A  1  1118 ? 13.563  71.565  102.949 0.49 19.22 ? 1116 LEU   A CD1   1 
ATOM   8220  C  CD1   B LEU   A  1  1118 ? 16.339  72.142  104.753 0.51 19.94 ? 1116 LEU   A CD1   1 
ATOM   8221  C  CD2   A LEU   A  1  1118 ? 15.970  71.215  103.487 0.49 22.25 ? 1116 LEU   A CD2   1 
ATOM   8222  C  CD2   B LEU   A  1  1118 ? 14.219  72.574  103.545 0.51 18.52 ? 1116 LEU   A CD2   1 
ATOM   8223  N  N     . ALA   A  1  1119 ? 12.653  68.605  106.674 1.00 19.00 ? 1117 ALA   A N     1 
ATOM   8224  C  CA    . ALA   A  1  1119 ? 12.138  67.241  106.639 1.00 20.36 ? 1117 ALA   A CA    1 
ATOM   8225  C  C     . ALA   A  1  1119 ? 10.620  67.238  106.707 1.00 18.91 ? 1117 ALA   A C     1 
ATOM   8226  O  O     . ALA   A  1  1119 ? 9.959   66.529  105.944 1.00 18.53 ? 1117 ALA   A O     1 
ATOM   8227  C  CB    . ALA   A  1  1119 ? 12.723  66.416  107.776 1.00 20.43 ? 1117 ALA   A CB    1 
ATOM   8228  N  N     . ALA   A  1  1120 ? 10.047  68.053  107.585 1.00 17.36 ? 1118 ALA   A N     1 
ATOM   8229  C  CA    . ALA   A  1  1120 ? 8.593   68.095  107.701 1.00 16.60 ? 1118 ALA   A CA    1 
ATOM   8230  C  C     . ALA   A  1  1120 ? 7.973   68.543  106.393 1.00 18.82 ? 1118 ALA   A C     1 
ATOM   8231  O  O     . ALA   A  1  1120 ? 7.000   67.948  105.911 1.00 17.02 ? 1118 ALA   A O     1 
ATOM   8232  C  CB    . ALA   A  1  1120 ? 8.195   69.053  108.819 1.00 18.27 ? 1118 ALA   A CB    1 
ATOM   8233  N  N     . ALA   A  1  1121 ? 8.532   69.591  105.794 1.00 17.14 ? 1119 ALA   A N     1 
ATOM   8234  C  CA    . ALA   A  1  1121 ? 7.951   70.135  104.576 1.00 17.72 ? 1119 ALA   A CA    1 
ATOM   8235  C  C     . ALA   A  1  1121 ? 8.119   69.181  103.404 1.00 16.65 ? 1119 ALA   A C     1 
ATOM   8236  O  O     . ALA   A  1  1121 ? 7.204   69.022  102.591 1.00 17.03 ? 1119 ALA   A O     1 
ATOM   8237  C  CB    . ALA   A  1  1121 ? 8.574   71.493  104.263 1.00 18.87 ? 1119 ALA   A CB    1 
ATOM   8238  N  N     . LEU   A  1  1122 ? 9.296   68.575  103.275 1.00 16.34 ? 1120 LEU   A N     1 
ATOM   8239  C  CA    . LEU   A  1  1122 ? 9.547   67.691  102.139 1.00 15.39 ? 1120 LEU   A CA    1 
ATOM   8240  C  C     . LEU   A  1  1122 ? 8.758   66.401  102.265 1.00 16.69 ? 1120 LEU   A C     1 
ATOM   8241  O  O     . LEU   A  1  1122 ? 8.272   65.870  101.262 1.00 16.55 ? 1120 LEU   A O     1 
ATOM   8242  C  CB    . LEU   A  1  1122 ? 11.039  67.389  102.023 1.00 19.29 ? 1120 LEU   A CB    1 
ATOM   8243  C  CG    . LEU   A  1  1122 ? 11.950  68.564  101.684 1.00 17.98 ? 1120 LEU   A CG    1 
ATOM   8244  C  CD1   . LEU   A  1  1122 ? 13.381  68.102  101.726 1.00 19.92 ? 1120 LEU   A CD1   1 
ATOM   8245  C  CD2   . LEU   A  1  1122 ? 11.601  69.161  100.335 1.00 20.70 ? 1120 LEU   A CD2   1 
ATOM   8246  N  N     . ALA   A  1  1123 ? 8.622   65.886  103.487 1.00 16.54 ? 1121 ALA   A N     1 
ATOM   8247  C  CA    . ALA   A  1  1123 ? 7.872   64.658  103.701 1.00 16.05 ? 1121 ALA   A CA    1 
ATOM   8248  C  C     . ALA   A  1  1123 ? 6.423   64.826  103.302 1.00 16.39 ? 1121 ALA   A C     1 
ATOM   8249  O  O     . ALA   A  1  1123 ? 5.755   63.832  103.018 1.00 17.54 ? 1121 ALA   A O     1 
ATOM   8250  C  CB    . ALA   A  1  1123 ? 7.911   64.262  105.177 1.00 16.72 ? 1121 ALA   A CB    1 
ATOM   8251  N  N     . THR   A  1  1124 ? 5.925   66.059  103.290 1.00 15.43 ? 1122 THR   A N     1 
ATOM   8252  C  CA    . THR   A  1  1124 ? 4.552   66.330  102.905 1.00 14.67 ? 1122 THR   A CA    1 
ATOM   8253  C  C     . THR   A  1  1124 ? 4.457   66.874  101.493 1.00 15.84 ? 1122 THR   A C     1 
ATOM   8254  O  O     . THR   A  1  1124 ? 3.408   67.395  101.096 1.00 16.95 ? 1122 THR   A O     1 
ATOM   8255  C  CB    . THR   A  1  1124 ? 3.896   67.243  103.942 1.00 17.43 ? 1122 THR   A CB    1 
ATOM   8256  O  OG1   . THR   A  1  1124 ? 4.774   68.331  104.252 1.00 17.18 ? 1122 THR   A OG1   1 
ATOM   8257  C  CG2   . THR   A  1  1124 ? 3.642   66.449  105.229 1.00 16.91 ? 1122 THR   A CG2   1 
ATOM   8258  N  N     . GLY   A  1  1125 ? 5.536   66.731  100.724 1.00 15.87 ? 1123 GLY   A N     1 
ATOM   8259  C  CA    . GLY   A  1  1125 ? 5.551   66.979  99.298  1.00 16.77 ? 1123 GLY   A CA    1 
ATOM   8260  C  C     . GLY   A  1  1125 ? 5.746   68.420  98.906  1.00 15.06 ? 1123 GLY   A C     1 
ATOM   8261  O  O     . GLY   A  1  1125 ? 5.629   68.750  97.722  1.00 17.74 ? 1123 GLY   A O     1 
ATOM   8262  N  N     . ASN   A  1  1126 ? 6.042   69.289  99.855  1.00 15.89 ? 1124 ASN   A N     1 
ATOM   8263  C  CA    . ASN   A  1  1126 ? 6.096   70.709  99.579  1.00 15.74 ? 1124 ASN   A CA    1 
ATOM   8264  C  C     . ASN   A  1  1126 ? 7.467   71.131  99.101  1.00 16.76 ? 1124 ASN   A C     1 
ATOM   8265  O  O     . ASN   A  1  1126 ? 8.480   70.472  99.348  1.00 18.56 ? 1124 ASN   A O     1 
ATOM   8266  C  CB    . ASN   A  1  1126 ? 5.799   71.496  100.844 1.00 16.42 ? 1124 ASN   A CB    1 
ATOM   8267  C  CG    . ASN   A  1  1126 ? 4.447   71.203  101.379 1.00 16.78 ? 1124 ASN   A CG    1 
ATOM   8268  O  OD1   . ASN   A  1  1126 ? 3.447   71.593  100.794 1.00 17.83 ? 1124 ASN   A OD1   1 
ATOM   8269  N  ND2   . ASN   A  1  1126 ? 4.397   70.497  102.505 1.00 15.89 ? 1124 ASN   A ND2   1 
ATOM   8270  N  N     . SER   A  1  1127 ? 7.480   72.283  98.445  1.00 17.17 ? 1125 SER   A N     1 
ATOM   8271  C  CA    . SER   A  1  1127 ? 8.711   73.030  98.280  1.00 17.56 ? 1125 SER   A CA    1 
ATOM   8272  C  C     . SER   A  1  1127 ? 8.816   74.031  99.418  1.00 17.59 ? 1125 SER   A C     1 
ATOM   8273  O  O     . SER   A  1  1127 ? 7.885   74.210  100.210 1.00 17.68 ? 1125 SER   A O     1 
ATOM   8274  C  CB    . SER   A  1  1127 ? 8.725   73.762  96.940  1.00 19.35 ? 1125 SER   A CB    1 
ATOM   8275  O  OG    . SER   A  1  1127 ? 7.661   74.691  96.863  1.00 25.35 ? 1125 SER   A OG    1 
ATOM   8276  N  N     . VAL   A  1  1128 ? 9.969   74.677  99.524  1.00 19.03 ? 1126 VAL   A N     1 
ATOM   8277  C  CA    . VAL   A  1  1128 ? 10.194  75.596  100.628 1.00 19.69 ? 1126 VAL   A CA    1 
ATOM   8278  C  C     . VAL   A  1  1128 ? 10.850  76.866  100.125 1.00 20.95 ? 1126 VAL   A C     1 
ATOM   8279  O  O     . VAL   A  1  1128 ? 11.573  76.874  99.123  1.00 20.98 ? 1126 VAL   A O     1 
ATOM   8280  C  CB    . VAL   A  1  1128 ? 11.053  74.982  101.748 1.00 20.75 ? 1126 VAL   A CB    1 
ATOM   8281  C  CG1   . VAL   A  1  1128 ? 10.399  73.742  102.321 1.00 21.35 ? 1126 VAL   A CG1   1 
ATOM   8282  C  CG2   . VAL   A  1  1128 ? 12.456  74.685  101.221 1.00 20.57 ? 1126 VAL   A CG2   1 
ATOM   8283  N  N     . ALA   A  1  1129 ? 10.589  77.946  100.842 1.00 20.77 ? 1127 ALA   A N     1 
ATOM   8284  C  CA    . ALA   A  1  1129 ? 11.379  79.161  100.750 1.00 20.82 ? 1127 ALA   A CA    1 
ATOM   8285  C  C     . ALA   A  1  1129 ? 11.938  79.405  102.141 1.00 18.73 ? 1127 ALA   A C     1 
ATOM   8286  O  O     . ALA   A  1  1129 ? 11.172  79.563  103.099 1.00 21.82 ? 1127 ALA   A O     1 
ATOM   8287  C  CB    . ALA   A  1  1129 ? 10.521  80.336  100.292 1.00 23.82 ? 1127 ALA   A CB    1 
ATOM   8288  N  N     . ILE   A  1  1130 ? 13.261  79.399  102.258 1.00 20.26 ? 1128 ILE   A N     1 
ATOM   8289  C  CA    . ILE   A  1  1130 ? 13.926  79.513  103.550 1.00 21.18 ? 1128 ILE   A CA    1 
ATOM   8290  C  C     . ILE   A  1  1130 ? 14.325  80.960  103.770 1.00 23.78 ? 1128 ILE   A C     1 
ATOM   8291  O  O     . ILE   A  1  1130 ? 14.936  81.586  102.895 1.00 24.37 ? 1128 ILE   A O     1 
ATOM   8292  C  CB    . ILE   A  1  1130 ? 15.156  78.599  103.655 1.00 20.91 ? 1128 ILE   A CB    1 
ATOM   8293  C  CG1   . ILE   A  1  1130 ? 14.804  77.170  103.262 1.00 22.53 ? 1128 ILE   A CG1   1 
ATOM   8294  C  CG2   . ILE   A  1  1130 ? 15.708  78.622  105.078 1.00 23.17 ? 1128 ILE   A CG2   1 
ATOM   8295  C  CD1   . ILE   A  1  1130 ? 16.021  76.323  103.079 1.00 20.94 ? 1128 ILE   A CD1   1 
ATOM   8296  N  N     . ASP   A  1  1131 ? 14.002  81.481  104.950 1.00 22.01 ? 1129 ASP   A N     1 
ATOM   8297  C  CA    . ASP   A  1  1131 ? 14.390  82.831  105.331 1.00 24.17 ? 1129 ASP   A CA    1 
ATOM   8298  C  C     . ASP   A  1  1131 ? 15.896  83.018  105.196 1.00 24.49 ? 1129 ASP   A C     1 
ATOM   8299  O  O     . ASP   A  1  1131 ? 16.672  82.419  105.948 1.00 24.65 ? 1129 ASP   A O     1 
ATOM   8300  C  CB    . ASP   A  1  1131 ? 13.973  83.095  106.774 1.00 22.50 ? 1129 ASP   A CB    1 
ATOM   8301  C  CG    . ASP   A  1  1131 ? 14.344  84.478  107.233 1.00 28.77 ? 1129 ASP   A CG    1 
ATOM   8302  O  OD1   . ASP   A  1  1131 ? 14.404  85.382  106.377 1.00 27.34 ? 1129 ASP   A OD1   1 
ATOM   8303  O  OD2   . ASP   A  1  1131 ? 14.587  84.657  108.444 1.00 28.25 ? 1129 ASP   A OD2   1 
ATOM   8304  N  N     . ALA   A  1  1132 ? 16.316  83.847  104.238 1.00 25.54 ? 1130 ALA   A N     1 
ATOM   8305  C  CA    . ALA   A  1  1132 ? 17.737  84.114  104.057 1.00 29.31 ? 1130 ALA   A CA    1 
ATOM   8306  C  C     . ALA   A  1  1132 ? 18.330  84.884  105.226 1.00 30.22 ? 1130 ALA   A C     1 
ATOM   8307  O  O     . ALA   A  1  1132 ? 19.537  84.785  105.470 1.00 31.08 ? 1130 ALA   A O     1 
ATOM   8308  C  CB    . ALA   A  1  1132 ? 17.968  84.871  102.749 1.00 29.49 ? 1130 ALA   A CB    1 
ATOM   8309  N  N     . ALA   A  1  1133 ? 17.510  85.634  105.965 1.00 26.73 ? 1131 ALA   A N     1 
ATOM   8310  C  CA    . ALA   A  1  1133 ? 18.005  86.348  107.137 1.00 31.84 ? 1131 ALA   A CA    1 
ATOM   8311  C  C     . ALA   A  1  1133 ? 18.418  85.415  108.269 1.00 32.01 ? 1131 ALA   A C     1 
ATOM   8312  O  O     . ALA   A  1  1133 ? 19.059  85.871  109.221 1.00 31.75 ? 1131 ALA   A O     1 
ATOM   8313  C  CB    . ALA   A  1  1133 ? 16.956  87.348  107.627 1.00 33.55 ? 1131 ALA   A CB    1 
ATOM   8314  N  N     . SER   A  1  1134 ? 18.075  84.128  108.189 1.00 29.24 ? 1132 SER   A N     1 
ATOM   8315  C  CA    . SER   A  1  1134 ? 18.515  83.158  109.185 1.00 26.16 ? 1132 SER   A CA    1 
ATOM   8316  C  C     . SER   A  1  1134 ? 20.023  82.960  109.176 1.00 28.17 ? 1132 SER   A C     1 
ATOM   8317  O  O     . SER   A  1  1134 ? 20.573  82.462  110.162 1.00 27.75 ? 1132 SER   A O     1 
ATOM   8318  C  CB    . SER   A  1  1134 ? 17.854  81.801  108.914 1.00 26.11 ? 1132 SER   A CB    1 
ATOM   8319  O  OG    . SER   A  1  1134 ? 18.363  81.204  107.720 1.00 25.45 ? 1132 SER   A OG    1 
ATOM   8320  N  N     . GLY   A  1  1135 ? 20.691  83.305  108.078 1.00 28.32 ? 1133 GLY   A N     1 
ATOM   8321  C  CA    . GLY   A  1  1135 ? 22.119  83.091  107.973 1.00 27.65 ? 1133 GLY   A CA    1 
ATOM   8322  C  C     . GLY   A  1  1135 ? 22.541  81.641  107.916 1.00 29.91 ? 1133 GLY   A C     1 
ATOM   8323  O  O     . GLY   A  1  1135 ? 23.703  81.337  108.177 1.00 30.54 ? 1133 GLY   A O     1 
ATOM   8324  N  N     . LEU   A  1  1136 ? 21.630  80.728  107.578 1.00 25.69 ? 1134 LEU   A N     1 
ATOM   8325  C  CA    . LEU   A  1  1136 ? 21.914  79.301  107.620 1.00 27.68 ? 1134 LEU   A CA    1 
ATOM   8326  C  C     . LEU   A  1  1136 ? 22.236  78.721  106.247 1.00 26.86 ? 1134 LEU   A C     1 
ATOM   8327  O  O     . LEU   A  1  1136 ? 22.197  77.497  106.079 1.00 26.15 ? 1134 LEU   A O     1 
ATOM   8328  C  CB    . LEU   A  1  1136 ? 20.747  78.546  108.261 1.00 25.74 ? 1134 LEU   A CB    1 
ATOM   8329  C  CG    . LEU   A  1  1136 ? 20.531  78.783  109.755 1.00 26.00 ? 1134 LEU   A CG    1 
ATOM   8330  C  CD1   . LEU   A  1  1136 ? 19.220  78.132  110.216 1.00 25.09 ? 1134 LEU   A CD1   1 
ATOM   8331  C  CD2   . LEU   A  1  1136 ? 21.712  78.272  110.563 1.00 27.69 ? 1134 LEU   A CD2   1 
ATOM   8332  N  N     . GLN   A  1  1137 ? 22.565  79.573  105.269 1.00 27.89 ? 1135 GLN   A N     1 
ATOM   8333  C  CA    . GLN   A  1  1137 ? 22.842  79.092  103.916 1.00 29.53 ? 1135 GLN   A CA    1 
ATOM   8334  C  C     . GLN   A  1  1137 ? 23.922  78.015  103.897 1.00 27.56 ? 1135 GLN   A C     1 
ATOM   8335  O  O     . GLN   A  1  1137 ? 23.813  77.032  103.155 1.00 28.15 ? 1135 GLN   A O     1 
ATOM   8336  C  CB    . GLN   A  1  1137 ? 23.230  80.257  102.999 1.00 29.50 ? 1135 GLN   A CB    1 
ATOM   8337  C  CG    . GLN   A  1  1137 ? 22.075  81.160  102.576 1.00 29.41 ? 1135 GLN   A CG    1 
ATOM   8338  C  CD    . GLN   A  1  1137 ? 21.758  82.236  103.604 1.00 28.97 ? 1135 GLN   A CD    1 
ATOM   8339  O  OE1   . GLN   A  1  1137 ? 22.273  82.217  104.724 1.00 32.49 ? 1135 GLN   A OE1   1 
ATOM   8340  N  NE2   . GLN   A  1  1137 ? 20.905  83.181  103.224 1.00 33.53 ? 1135 GLN   A NE2   1 
ATOM   8341  N  N     . ALA   A  1  1138 ? 24.969  78.173  104.709 1.00 27.07 ? 1136 ALA   A N     1 
ATOM   8342  C  CA    . ALA   A  1  1138 ? 26.053  77.195  104.717 1.00 25.90 ? 1136 ALA   A CA    1 
ATOM   8343  C  C     . ALA   A  1  1138 ? 25.636  75.837  105.262 1.00 30.91 ? 1136 ALA   A C     1 
ATOM   8344  O  O     . ALA   A  1  1138 ? 26.424  74.889  105.177 1.00 35.35 ? 1136 ALA   A O     1 
ATOM   8345  C  CB    . ALA   A  1  1138 ? 27.257  77.721  105.505 1.00 28.02 ? 1136 ALA   A CB    1 
ATOM   8346  N  N     . SER   A  1  1139 ? 24.429  75.716  105.817 1.00 28.90 ? 1137 SER   A N     1 
ATOM   8347  C  CA    . SER   A  1  1139 ? 23.957  74.436  106.321 1.00 29.51 ? 1137 SER   A CA    1 
ATOM   8348  C  C     . SER   A  1  1139 ? 23.342  73.563  105.239 1.00 25.61 ? 1137 SER   A C     1 
ATOM   8349  O  O     . SER   A  1  1139 ? 23.051  72.395  105.511 1.00 27.72 ? 1137 SER   A O     1 
ATOM   8350  C  CB    . SER   A  1  1139 ? 22.930  74.645  107.441 1.00 29.74 ? 1137 SER   A CB    1 
ATOM   8351  O  OG    . SER   A  1  1139 ? 23.522  75.253  108.571 1.00 30.49 ? 1137 SER   A OG    1 
ATOM   8352  N  N     . LEU   A  1  1140 ? 23.120  74.096  104.040 1.00 26.29 ? 1138 LEU   A N     1 
ATOM   8353  C  CA    . LEU   A  1  1140 ? 22.505  73.356  102.945 1.00 25.73 ? 1138 LEU   A CA    1 
ATOM   8354  C  C     . LEU   A  1  1140 ? 23.422  73.280  101.734 1.00 30.14 ? 1138 LEU   A C     1 
ATOM   8355  O  O     . LEU   A  1  1140 ? 22.973  73.369  100.588 1.00 34.48 ? 1138 LEU   A O     1 
ATOM   8356  C  CB    . LEU   A  1  1140 ? 21.158  73.952  102.549 1.00 30.43 ? 1138 LEU   A CB    1 
ATOM   8357  C  CG    . LEU   A  1  1140 ? 19.944  73.681  103.431 1.00 31.85 ? 1138 LEU   A CG    1 
ATOM   8358  C  CD1   . LEU   A  1  1140 ? 18.709  74.083  102.659 1.00 32.03 ? 1138 LEU   A CD1   1 
ATOM   8359  C  CD2   . LEU   A  1  1140 ? 19.858  72.222  103.865 1.00 29.05 ? 1138 LEU   A CD2   1 
ATOM   8360  N  N     . LYS   A  1  1141 ? 24.717  73.112  101.970 1.00 30.33 ? 1139 LYS   A N     1 
ATOM   8361  C  CA    . LYS   A  1  1141 ? 25.665  73.022  100.871 1.00 34.00 ? 1139 LYS   A CA    1 
ATOM   8362  C  C     . LYS   A  1  1141 ? 25.552  71.667  100.178 1.00 32.04 ? 1139 LYS   A C     1 
ATOM   8363  O  O     . LYS   A  1  1141 ? 25.364  70.632  100.824 1.00 30.72 ? 1139 LYS   A O     1 
ATOM   8364  C  CB    . LYS   A  1  1141 ? 27.089  73.229  101.391 1.00 35.40 ? 1139 LYS   A CB    1 
ATOM   8365  N  N     . ASN   A  1  1142 ? 25.656  71.682  98.850  1.00 32.60 ? 1140 ASN   A N     1 
ATOM   8366  C  CA    . ASN   A  1  1142 ? 25.775  70.460  98.053  1.00 32.08 ? 1140 ASN   A CA    1 
ATOM   8367  C  C     . ASN   A  1  1142 ? 24.516  69.593  98.115  1.00 29.55 ? 1140 ASN   A C     1 
ATOM   8368  O  O     . ASN   A  1  1142 ? 24.600  68.364  98.148  1.00 27.36 ? 1140 ASN   A O     1 
ATOM   8369  C  CB    . ASN   A  1  1142 ? 27.019  69.650  98.422  1.00 35.12 ? 1140 ASN   A CB    1 
ATOM   8370  C  CG    . ASN   A  1  1142 ? 28.261  70.512  98.534  1.00 41.95 ? 1140 ASN   A CG    1 
ATOM   8371  O  OD1   . ASN   A  1  1142 ? 28.838  70.652  99.616  1.00 46.17 ? 1140 ASN   A OD1   1 
ATOM   8372  N  ND2   . ASN   A  1  1142 ? 28.677  71.098  97.419  1.00 37.41 ? 1140 ASN   A ND2   1 
ATOM   8373  N  N     . LEU   A  1  1143 ? 23.344  70.223  98.132  1.00 31.47 ? 1141 LEU   A N     1 
ATOM   8374  C  CA    . LEU   A  1  1143 ? 22.116  69.450  98.127  1.00 29.73 ? 1141 LEU   A CA    1 
ATOM   8375  C  C     . LEU   A  1  1143 ? 22.022  68.630  96.844  1.00 29.32 ? 1141 LEU   A C     1 
ATOM   8376  O  O     . LEU   A  1  1143 ? 22.475  69.070  95.782  1.00 29.25 ? 1141 LEU   A O     1 
ATOM   8377  C  CB    . LEU   A  1  1143 ? 20.902  70.368  98.177  1.00 29.19 ? 1141 LEU   A CB    1 
ATOM   8378  C  CG    . LEU   A  1  1143 ? 20.477  70.903  99.530  1.00 27.70 ? 1141 LEU   A CG    1 
ATOM   8379  C  CD1   . LEU   A  1  1143 ? 19.275  71.801  99.329  1.00 26.52 ? 1141 LEU   A CD1   1 
ATOM   8380  C  CD2   . LEU   A  1  1143 ? 20.164  69.756  100.495 1.00 27.69 ? 1141 LEU   A CD2   1 
ATOM   8381  N  N     . PRO   A  1  1144 ? 21.423  67.444  96.908  1.00 26.13 ? 1142 PRO   A N     1 
ATOM   8382  C  CA    . PRO   A  1  1144 ? 21.072  66.749  95.667  1.00 27.34 ? 1142 PRO   A CA    1 
ATOM   8383  C  C     . PRO   A  1  1144 ? 20.166  67.641  94.835  1.00 26.12 ? 1142 PRO   A C     1 
ATOM   8384  O  O     . PRO   A  1  1144 ? 19.373  68.427  95.364  1.00 24.72 ? 1142 PRO   A O     1 
ATOM   8385  C  CB    . PRO   A  1  1144 ? 20.319  65.503  96.158  1.00 31.62 ? 1142 PRO   A CB    1 
ATOM   8386  C  CG    . PRO   A  1  1144 ? 20.643  65.385  97.624  1.00 31.55 ? 1142 PRO   A CG    1 
ATOM   8387  C  CD    . PRO   A  1  1144 ? 20.902  66.768  98.108  1.00 30.29 ? 1142 PRO   A CD    1 
ATOM   8388  N  N     . GLN   A  1  1145 ? 20.296  67.522  93.514  1.00 25.70 ? 1143 GLN   A N     1 
ATOM   8389  C  CA    . GLN   A  1  1145 ? 19.491  68.349  92.622  1.00 28.55 ? 1143 GLN   A CA    1 
ATOM   8390  C  C     . GLN   A  1  1145 ? 17.998  68.209  92.905  1.00 25.06 ? 1143 GLN   A C     1 
ATOM   8391  O  O     . GLN   A  1  1145 ? 17.252  69.190  92.814  1.00 23.29 ? 1143 GLN   A O     1 
ATOM   8392  C  CB    . GLN   A  1  1145 ? 19.797  68.003  91.163  1.00 34.15 ? 1143 GLN   A CB    1 
ATOM   8393  N  N     . THR   A  1  1146 ? 17.537  66.997  93.239  1.00 24.95 ? 1144 THR   A N     1 
ATOM   8394  C  CA    . THR   A  1  1146 ? 16.112  66.808  93.516  1.00 25.34 ? 1144 THR   A CA    1 
ATOM   8395  C  C     . THR   A  1  1146 ? 15.656  67.668  94.685  1.00 22.79 ? 1144 THR   A C     1 
ATOM   8396  O  O     . THR   A  1  1146 ? 14.536  68.191  94.682  1.00 23.16 ? 1144 THR   A O     1 
ATOM   8397  C  CB    . THR   A  1  1146 ? 15.822  65.349  93.850  1.00 26.35 ? 1144 THR   A CB    1 
ATOM   8398  O  OG1   . THR   A  1  1146 ? 16.700  64.924  94.898  1.00 26.49 ? 1144 THR   A OG1   1 
ATOM   8399  C  CG2   . THR   A  1  1146 ? 15.984  64.462  92.633  1.00 25.28 ? 1144 THR   A CG2   1 
ATOM   8400  N  N     . VAL   A  1  1147 ? 16.498  67.794  95.708  1.00 22.39 ? 1145 VAL   A N     1 
ATOM   8401  C  CA    . VAL   A  1  1147 ? 16.142  68.620  96.853  1.00 20.49 ? 1145 VAL   A CA    1 
ATOM   8402  C  C     . VAL   A  1  1147 ? 16.323  70.096  96.529  1.00 22.05 ? 1145 VAL   A C     1 
ATOM   8403  O  O     . VAL   A  1  1147 ? 15.475  70.925  96.870  1.00 20.75 ? 1145 VAL   A O     1 
ATOM   8404  C  CB    . VAL   A  1  1147 ? 16.938  68.201  98.100  1.00 21.52 ? 1145 VAL   A CB    1 
ATOM   8405  C  CG1   . VAL   A  1  1147 ? 16.455  68.994  99.303  1.00 22.26 ? 1145 VAL   A CG1   1 
ATOM   8406  C  CG2   . VAL   A  1  1147 ? 16.802  66.699  98.355  1.00 24.72 ? 1145 VAL   A CG2   1 
ATOM   8407  N  N     . GLY   A  1  1148 ? 17.421  70.445  95.855  1.00 22.65 ? 1146 GLY   A N     1 
ATOM   8408  C  CA    . GLY   A  1  1148 ? 17.624  71.830  95.461  1.00 22.93 ? 1146 GLY   A CA    1 
ATOM   8409  C  C     . GLY   A  1  1148 ? 16.474  72.392  94.649  1.00 23.35 ? 1146 GLY   A C     1 
ATOM   8410  O  O     . GLY   A  1  1148 ? 16.125  73.568  94.788  1.00 25.23 ? 1146 GLY   A O     1 
ATOM   8411  N  N     . LEU   A  1  1149 ? 15.859  71.561  93.794  1.00 21.34 ? 1147 LEU   A N     1 
ATOM   8412  C  CA    . LEU   A  1  1149 ? 14.728  72.026  92.996  1.00 25.76 ? 1147 LEU   A CA    1 
ATOM   8413  C  C     . LEU   A  1  1149 ? 13.579  72.489  93.873  1.00 23.64 ? 1147 LEU   A C     1 
ATOM   8414  O  O     . LEU   A  1  1149 ? 12.770  73.321  93.448  1.00 25.98 ? 1147 LEU   A O     1 
ATOM   8415  C  CB    . LEU   A  1  1149 ? 14.234  70.912  92.075  1.00 26.68 ? 1147 LEU   A CB    1 
ATOM   8416  C  CG    . LEU   A  1  1149 ? 15.051  70.667  90.806  1.00 35.29 ? 1147 LEU   A CG    1 
ATOM   8417  C  CD1   . LEU   A  1  1149 ? 14.436  69.529  90.004  1.00 34.81 ? 1147 LEU   A CD1   1 
ATOM   8418  C  CD2   . LEU   A  1  1149 ? 15.126  71.949  89.984  1.00 33.71 ? 1147 LEU   A CD2   1 
ATOM   8419  N  N     . ARG   A  1  1150 ? 13.490  71.955  95.089  1.00 22.11 ? 1148 ARG   A N     1 
ATOM   8420  C  CA    . ARG   A  1  1150 ? 12.414  72.288  96.005  1.00 21.07 ? 1148 ARG   A CA    1 
ATOM   8421  C  C     . ARG   A  1  1150 ? 12.783  73.391  96.977  1.00 20.83 ? 1148 ARG   A C     1 
ATOM   8422  O  O     . ARG   A  1  1150 ? 11.923  73.825  97.745  1.00 22.40 ? 1148 ARG   A O     1 
ATOM   8423  C  CB    . ARG   A  1  1150 ? 12.049  71.057  96.826  1.00 21.50 ? 1148 ARG   A CB    1 
ATOM   8424  C  CG    . ARG   A  1  1150 ? 11.305  70.013  96.030  1.00 22.78 ? 1148 ARG   A CG    1 
ATOM   8425  C  CD    . ARG   A  1  1150 ? 10.132  69.543  96.827  1.00 21.95 ? 1148 ARG   A CD    1 
ATOM   8426  N  NE    . ARG   A  1  1150 ? 9.542   68.332  96.284  1.00 21.84 ? 1148 ARG   A NE    1 
ATOM   8427  C  CZ    . ARG   A  1  1150 ? 9.013   67.387  97.042  1.00 19.93 ? 1148 ARG   A CZ    1 
ATOM   8428  N  NH1   . ARG   A  1  1150 ? 8.944   67.524  98.359  1.00 18.35 ? 1148 ARG   A NH1   1 
ATOM   8429  N  NH2   . ARG   A  1  1150 ? 8.568   66.271  96.472  1.00 19.73 ? 1148 ARG   A NH2   1 
ATOM   8430  N  N     . VAL   A  1  1151 ? 14.031  73.836  96.977  1.00 19.34 ? 1149 VAL   A N     1 
ATOM   8431  C  CA    . VAL   A  1  1151 ? 14.535  74.783  97.961  1.00 20.54 ? 1149 VAL   A CA    1 
ATOM   8432  C  C     . VAL   A  1  1151 ? 14.811  76.117  97.284  1.00 25.60 ? 1149 VAL   A C     1 
ATOM   8433  O  O     . VAL   A  1  1151 ? 15.504  76.178  96.263  1.00 27.82 ? 1149 VAL   A O     1 
ATOM   8434  C  CB    . VAL   A  1  1151 ? 15.794  74.243  98.655  1.00 21.38 ? 1149 VAL   A CB    1 
ATOM   8435  C  CG1   . VAL   A  1  1151 ? 16.402  75.302  99.558  1.00 25.87 ? 1149 VAL   A CG1   1 
ATOM   8436  C  CG2   . VAL   A  1  1151 ? 15.465  72.996  99.454  1.00 22.24 ? 1149 VAL   A CG2   1 
ATOM   8437  N  N     . SER   A  1  1152 ? 14.266  77.181  97.847  1.00 22.74 ? 1150 SER   A N     1 
ATOM   8438  C  CA    . SER   A  1  1152 ? 14.666  78.530  97.497  1.00 25.47 ? 1150 SER   A CA    1 
ATOM   8439  C  C     . SER   A  1  1152 ? 14.965  79.269  98.788  1.00 26.81 ? 1150 SER   A C     1 
ATOM   8440  O  O     . SER   A  1  1152 ? 14.480  78.905  99.863  1.00 25.73 ? 1150 SER   A O     1 
ATOM   8441  C  CB    . SER   A  1  1152 ? 13.588  79.273  96.698  1.00 28.69 ? 1150 SER   A CB    1 
ATOM   8442  O  OG    . SER   A  1  1152 ? 12.397  79.417  97.450  1.00 32.93 ? 1150 SER   A OG    1 
ATOM   8443  N  N     . TRP   A  1  1153 ? 15.797  80.293  98.674  1.00 24.88 ? 1151 TRP   A N     1 
ATOM   8444  C  CA    . TRP   A  1  1153 ? 16.102  81.187  99.776  1.00 26.23 ? 1151 TRP   A CA    1 
ATOM   8445  C  C     . TRP   A  1  1153 ? 15.446  82.533  99.513  1.00 28.81 ? 1151 TRP   A C     1 
ATOM   8446  O  O     . TRP   A  1  1153 ? 15.456  83.029  98.380  1.00 32.52 ? 1151 TRP   A O     1 
ATOM   8447  C  CB    . TRP   A  1  1153 ? 17.609  81.350  99.918  1.00 26.84 ? 1151 TRP   A CB    1 
ATOM   8448  C  CG    . TRP   A  1  1153 ? 18.261  80.120  100.429 1.00 27.22 ? 1151 TRP   A CG    1 
ATOM   8449  C  CD1   . TRP   A  1  1153 ? 18.691  79.053  99.696  1.00 28.61 ? 1151 TRP   A CD1   1 
ATOM   8450  C  CD2   . TRP   A  1  1153 ? 18.542  79.810  101.796 1.00 27.07 ? 1151 TRP   A CD2   1 
ATOM   8451  N  NE1   . TRP   A  1  1153 ? 19.237  78.103  100.524 1.00 30.13 ? 1151 TRP   A NE1   1 
ATOM   8452  C  CE2   . TRP   A  1  1153 ? 19.157  78.542  101.820 1.00 26.92 ? 1151 TRP   A CE2   1 
ATOM   8453  C  CE3   . TRP   A  1  1153 ? 18.347  80.487  103.002 1.00 24.21 ? 1151 TRP   A CE3   1 
ATOM   8454  C  CZ2   . TRP   A  1  1153 ? 19.574  77.934  103.007 1.00 25.78 ? 1151 TRP   A CZ2   1 
ATOM   8455  C  CZ3   . TRP   A  1  1153 ? 18.761  79.883  104.182 1.00 26.11 ? 1151 TRP   A CZ3   1 
ATOM   8456  C  CH2   . TRP   A  1  1153 ? 19.366  78.617  104.175 1.00 27.74 ? 1151 TRP   A CH2   1 
ATOM   8457  N  N     . SER   A  1  1154 ? 14.856  83.114  100.552 1.00 26.51 ? 1152 SER   A N     1 
ATOM   8458  C  CA    . SER   A  1  1154 ? 14.030  84.303  100.401 1.00 28.01 ? 1152 SER   A CA    1 
ATOM   8459  C  C     . SER   A  1  1154 ? 14.545  85.393  101.323 1.00 29.43 ? 1152 SER   A C     1 
ATOM   8460  O  O     . SER   A  1  1154 ? 14.522  85.237  102.549 1.00 29.33 ? 1152 SER   A O     1 
ATOM   8461  C  CB    . SER   A  1  1154 ? 12.563  84.006  100.713 1.00 27.10 ? 1152 SER   A CB    1 
ATOM   8462  O  OG    . SER   A  1  1154 ? 11.785  85.181  100.570 1.00 28.37 ? 1152 SER   A OG    1 
ATOM   8463  N  N     . LYS   A  1  1155 ? 15.003  86.493  100.732 1.00 30.61 ? 1153 LYS   A N     1 
ATOM   8464  C  CA    . LYS   A  1  1155 ? 15.327  87.685  101.502 1.00 31.57 ? 1153 LYS   A CA    1 
ATOM   8465  C  C     . LYS   A  1  1155 ? 14.142  88.630  101.631 1.00 33.45 ? 1153 LYS   A C     1 
ATOM   8466  O  O     . LYS   A  1  1155 ? 14.101  89.429  102.572 1.00 40.94 ? 1153 LYS   A O     1 
ATOM   8467  C  CB    . LYS   A  1  1155 ? 16.514  88.422  100.868 1.00 34.20 ? 1153 LYS   A CB    1 
ATOM   8468  N  N     . ASP   A  1  1156 ? 13.177  88.548  100.717 1.00 31.26 ? 1154 ASP   A N     1 
ATOM   8469  C  CA    . ASP   A  1  1156 ? 11.982  89.387  100.712 1.00 32.64 ? 1154 ASP   A CA    1 
ATOM   8470  C  C     . ASP   A  1  1156 ? 10.811  88.412  100.623 1.00 32.67 ? 1154 ASP   A C     1 
ATOM   8471  O  O     . ASP   A  1  1156 ? 10.408  88.015  99.525  1.00 28.91 ? 1154 ASP   A O     1 
ATOM   8472  C  CB    . ASP   A  1  1156 ? 12.024  90.338  99.519  1.00 35.81 ? 1154 ASP   A CB    1 
ATOM   8473  C  CG    . ASP   A  1  1156 ? 10.820  91.260  99.452  1.00 40.77 ? 1154 ASP   A CG    1 
ATOM   8474  O  OD1   . ASP   A  1  1156 ? 9.914   91.147  100.306 1.00 40.76 ? 1154 ASP   A OD1   1 
ATOM   8475  O  OD2   . ASP   A  1  1156 ? 10.780  92.108  98.536  1.00 44.86 ? 1154 ASP   A OD2   1 
ATOM   8476  N  N     . TRP   A  1  1157 ? 10.264  88.030  101.781 1.00 29.14 ? 1155 TRP   A N     1 
ATOM   8477  C  CA    . TRP   A  1  1157 ? 9.226   87.001  101.793 1.00 25.77 ? 1155 TRP   A CA    1 
ATOM   8478  C  C     . TRP   A  1  1157 ? 8.024   87.411  100.956 1.00 30.12 ? 1155 TRP   A C     1 
ATOM   8479  O  O     . TRP   A  1  1157 ? 7.431   86.577  100.266 1.00 29.00 ? 1155 TRP   A O     1 
ATOM   8480  C  CB    . TRP   A  1  1157 ? 8.771   86.707  103.220 1.00 26.73 ? 1155 TRP   A CB    1 
ATOM   8481  C  CG    . TRP   A  1  1157 ? 9.837   86.299  104.175 1.00 26.19 ? 1155 TRP   A CG    1 
ATOM   8482  C  CD1   . TRP   A  1  1157 ? 11.127  85.955  103.891 1.00 24.78 ? 1155 TRP   A CD1   1 
ATOM   8483  C  CD2   . TRP   A  1  1157 ? 9.703   86.219  105.596 1.00 24.08 ? 1155 TRP   A CD2   1 
ATOM   8484  N  NE1   . TRP   A  1  1157 ? 11.799  85.645  105.049 1.00 26.54 ? 1155 TRP   A NE1   1 
ATOM   8485  C  CE2   . TRP   A  1  1157 ? 10.946  85.805  106.110 1.00 25.26 ? 1155 TRP   A CE2   1 
ATOM   8486  C  CE3   . TRP   A  1  1157 ? 8.644   86.452  106.485 1.00 24.14 ? 1155 TRP   A CE3   1 
ATOM   8487  C  CZ2   . TRP   A  1  1157 ? 11.165  85.623  107.474 1.00 25.67 ? 1155 TRP   A CZ2   1 
ATOM   8488  C  CZ3   . TRP   A  1  1157 ? 8.864   86.272  107.837 1.00 25.12 ? 1155 TRP   A CZ3   1 
ATOM   8489  C  CH2   . TRP   A  1  1157 ? 10.110  85.862  108.318 1.00 27.49 ? 1155 TRP   A CH2   1 
ATOM   8490  N  N     . ALA   A  1  1158 ? 7.640   88.689  101.010 1.00 29.61 ? 1156 ALA   A N     1 
ATOM   8491  C  CA    . ALA   A  1  1158 ? 6.467   89.138  100.266 1.00 30.82 ? 1156 ALA   A CA    1 
ATOM   8492  C  C     . ALA   A  1  1158 ? 6.663   89.038  98.762  1.00 34.65 ? 1156 ALA   A C     1 
ATOM   8493  O  O     . ALA   A  1  1158 ? 5.676   88.963  98.021  1.00 38.80 ? 1156 ALA   A O     1 
ATOM   8494  C  CB    . ALA   A  1  1158 ? 6.107   90.574  100.648 1.00 33.20 ? 1156 ALA   A CB    1 
ATOM   8495  N  N     . ALA   A  1  1159 ? 7.911   89.047  98.297  1.00 31.10 ? 1157 ALA   A N     1 
ATOM   8496  C  CA    . ALA   A  1  1159 ? 8.197   88.930  96.875  1.00 34.91 ? 1157 ALA   A CA    1 
ATOM   8497  C  C     . ALA   A  1  1159 ? 8.162   87.492  96.380  1.00 34.72 ? 1157 ALA   A C     1 
ATOM   8498  O  O     . ALA   A  1  1159 ? 7.972   87.268  95.182  1.00 35.85 ? 1157 ALA   A O     1 
ATOM   8499  C  CB    . ALA   A  1  1159 ? 9.569   89.541  96.569  1.00 35.30 ? 1157 ALA   A CB    1 
ATOM   8500  N  N     . ASP   A  1  1160 ? 8.326   86.514  97.268  1.00 32.89 ? 1158 ASP   A N     1 
ATOM   8501  C  CA    . ASP   A  1  1160 ? 8.505   85.124  96.869  1.00 32.80 ? 1158 ASP   A CA    1 
ATOM   8502  C  C     . ASP   A  1  1160 ? 7.289   84.253  97.152  1.00 28.15 ? 1158 ASP   A C     1 
ATOM   8503  O  O     . ASP   A  1  1160 ? 7.352   83.034  96.966  1.00 29.61 ? 1158 ASP   A O     1 
ATOM   8504  C  CB    . ASP   A  1  1160 ? 9.761   84.558  97.521  1.00 32.71 ? 1158 ASP   A CB    1 
ATOM   8505  C  CG    . ASP   A  1  1160 ? 10.986  85.358  97.167  1.00 35.98 ? 1158 ASP   A CG    1 
ATOM   8506  O  OD1   . ASP   A  1  1160 ? 11.002  85.936  96.059  1.00 39.99 ? 1158 ASP   A OD1   1 
ATOM   8507  O  OD2   . ASP   A  1  1160 ? 11.920  85.429  97.990  1.00 34.10 ? 1158 ASP   A OD2   1 
ATOM   8508  N  N     . GLY   A  1  1161 ? 6.188   84.845  97.589  1.00 30.20 ? 1159 GLY   A N     1 
ATOM   8509  C  CA    . GLY   A  1  1161 ? 4.971   84.107  97.788  1.00 29.48 ? 1159 GLY   A CA    1 
ATOM   8510  C  C     . GLY   A  1  1161 ? 4.208   83.919  96.490  1.00 30.32 ? 1159 GLY   A C     1 
ATOM   8511  O  O     . GLY   A  1  1161 ? 4.715   84.194  95.400  1.00 34.35 ? 1159 GLY   A O     1 
ATOM   8512  N  N     . PRO   A  1  1162 ? 2.963   83.450  96.588  1.00 29.24 ? 1160 PRO   A N     1 
ATOM   8513  C  CA    . PRO   A  1  1162 ? 2.250   83.103  97.818  1.00 24.81 ? 1160 PRO   A CA    1 
ATOM   8514  C  C     . PRO   A  1  1162 ? 2.777   81.807  98.404  1.00 27.34 ? 1160 PRO   A C     1 
ATOM   8515  O  O     . PRO   A  1  1162 ? 3.147   80.865  97.705  1.00 26.91 ? 1160 PRO   A O     1 
ATOM   8516  C  CB    . PRO   A  1  1162 ? 0.803   82.951  97.341  1.00 27.39 ? 1160 PRO   A CB    1 
ATOM   8517  C  CG    . PRO   A  1  1162 ? 0.952   82.410  95.951  1.00 33.51 ? 1160 PRO   A CG    1 
ATOM   8518  C  CD    . PRO   A  1  1162 ? 2.165   83.128  95.391  1.00 32.26 ? 1160 PRO   A CD    1 
ATOM   8519  N  N     . PHE   A  1  1163 ? 2.843   81.758  99.720  1.00 23.65 ? 1161 PHE   A N     1 
ATOM   8520  C  CA    . PHE   A  1  1163 ? 3.175   80.525  100.400 1.00 20.49 ? 1161 PHE   A CA    1 
ATOM   8521  C  C     . PHE   A  1  1163 ? 1.889   79.819  100.787 1.00 20.60 ? 1161 PHE   A C     1 
ATOM   8522  O  O     . PHE   A  1  1163 ? 0.791   80.363  100.663 1.00 23.51 ? 1161 PHE   A O     1 
ATOM   8523  C  CB    . PHE   A  1  1163 ? 4.033   80.828  101.622 1.00 20.08 ? 1161 PHE   A CB    1 
ATOM   8524  C  CG    . PHE   A  1  1163 ? 5.271   81.583  101.282 1.00 20.82 ? 1161 PHE   A CG    1 
ATOM   8525  C  CD1   . PHE   A  1  1163 ? 6.214   81.023  100.439 1.00 22.10 ? 1161 PHE   A CD1   1 
ATOM   8526  C  CD2   . PHE   A  1  1163 ? 5.469   82.871  101.749 1.00 21.24 ? 1161 PHE   A CD2   1 
ATOM   8527  C  CE1   . PHE   A  1  1163 ? 7.366   81.718  100.096 1.00 23.96 ? 1161 PHE   A CE1   1 
ATOM   8528  C  CE2   . PHE   A  1  1163 ? 6.617   83.574  101.412 1.00 25.76 ? 1161 PHE   A CE2   1 
ATOM   8529  C  CZ    . PHE   A  1  1163 ? 7.564   82.999  100.581 1.00 24.73 ? 1161 PHE   A CZ    1 
ATOM   8530  N  N     . ALA   A  1  1164 ? 2.025   78.570  101.221 1.00 20.14 ? 1162 ALA   A N     1 
ATOM   8531  C  CA    . ALA   A  1  1164 ? 0.863   77.777  101.594 1.00 20.15 ? 1162 ALA   A CA    1 
ATOM   8532  C  C     . ALA   A  1  1164 ? 0.921   77.342  103.045 1.00 19.03 ? 1162 ALA   A C     1 
ATOM   8533  O  O     . ALA   A  1  1164 ? 0.105   76.523  103.478 1.00 21.67 ? 1162 ALA   A O     1 
ATOM   8534  C  CB    . ALA   A  1  1164 ? 0.732   76.563  100.673 1.00 20.18 ? 1162 ALA   A CB    1 
ATOM   8535  N  N     . GLY   A  1  1165 ? 1.876   77.865  103.792 1.00 18.40 ? 1163 GLY   A N     1 
ATOM   8536  C  CA    . GLY   A  1  1165 ? 2.030   77.576  105.201 1.00 17.47 ? 1163 GLY   A CA    1 
ATOM   8537  C  C     . GLY   A  1  1165 ? 3.401   78.061  105.609 1.00 19.85 ? 1163 GLY   A C     1 
ATOM   8538  O  O     . GLY   A  1  1165 ? 4.175   78.547  104.788 1.00 19.38 ? 1163 GLY   A O     1 
ATOM   8539  N  N     . ALA   A  1  1166 ? 3.686   77.931  106.898 1.00 19.42 ? 1164 ALA   A N     1 
ATOM   8540  C  CA    . ALA   A  1  1166 ? 4.981   78.378  107.382 1.00 17.50 ? 1164 ALA   A CA    1 
ATOM   8541  C  C     . ALA   A  1  1166 ? 5.383   77.557  108.592 1.00 19.39 ? 1164 ALA   A C     1 
ATOM   8542  O  O     . ALA   A  1  1166 ? 4.535   77.112  109.371 1.00 21.60 ? 1164 ALA   A O     1 
ATOM   8543  C  CB    . ALA   A  1  1166 ? 4.963   79.862  107.755 1.00 19.82 ? 1164 ALA   A CB    1 
ATOM   8544  N  N     . LEU   A  1  1167 ? 6.687   77.364  108.731 1.00 18.48 ? 1165 LEU   A N     1 
ATOM   8545  C  CA    . LEU   A  1  1167 ? 7.275   76.733  109.900 1.00 18.29 ? 1165 LEU   A CA    1 
ATOM   8546  C  C     . LEU   A  1  1167 ? 8.270   77.715  110.488 1.00 20.70 ? 1165 LEU   A C     1 
ATOM   8547  O  O     . LEU   A  1  1167 ? 9.118   78.249  109.768 1.00 20.65 ? 1165 LEU   A O     1 
ATOM   8548  C  CB    . LEU   A  1  1167 ? 7.985   75.435  109.521 1.00 18.70 ? 1165 LEU   A CB    1 
ATOM   8549  C  CG    . LEU   A  1  1167 ? 7.086   74.372  108.890 1.00 19.46 ? 1165 LEU   A CG    1 
ATOM   8550  C  CD1   . LEU   A  1  1167 ? 7.905   73.159  108.488 1.00 20.36 ? 1165 LEU   A CD1   1 
ATOM   8551  C  CD2   . LEU   A  1  1167 ? 5.983   73.976  109.852 1.00 20.81 ? 1165 LEU   A CD2   1 
ATOM   8552  N  N     . VAL   A  1  1168 ? 8.162   77.951  111.786 1.00 19.82 ? 1166 VAL   A N     1 
ATOM   8553  C  CA    . VAL   A  1  1168 ? 8.948   78.966  112.470 1.00 19.64 ? 1166 VAL   A CA    1 
ATOM   8554  C  C     . VAL   A  1  1168 ? 9.650   78.320  113.646 1.00 21.73 ? 1166 VAL   A C     1 
ATOM   8555  O  O     . VAL   A  1  1168 ? 9.051   77.526  114.379 1.00 19.98 ? 1166 VAL   A O     1 
ATOM   8556  C  CB    . VAL   A  1  1168 ? 8.050   80.123  112.957 1.00 20.84 ? 1166 VAL   A CB    1 
ATOM   8557  C  CG1   . VAL   A  1  1168 ? 8.888   81.191  113.633 1.00 22.57 ? 1166 VAL   A CG1   1 
ATOM   8558  C  CG2   . VAL   A  1  1168 ? 7.271   80.710  111.792 1.00 21.73 ? 1166 VAL   A CG2   1 
ATOM   8559  N  N     . GLU   A  1  1169 ? 10.919  78.663  113.830 1.00 19.07 ? 1167 GLU   A N     1 
ATOM   8560  C  CA    . GLU   A  1  1169 ? 11.690  78.230  114.983 1.00 20.64 ? 1167 GLU   A CA    1 
ATOM   8561  C  C     . GLU   A  1  1169 ? 12.160  79.466  115.729 1.00 22.66 ? 1167 GLU   A C     1 
ATOM   8562  O  O     . GLU   A  1  1169 ? 12.690  80.398  115.116 1.00 23.62 ? 1167 GLU   A O     1 
ATOM   8563  C  CB    . GLU   A  1  1169 ? 12.915  77.430  114.550 1.00 20.12 ? 1167 GLU   A CB    1 
ATOM   8564  C  CG    . GLU   A  1  1169 ? 13.792  76.974  115.695 1.00 22.27 ? 1167 GLU   A CG    1 
ATOM   8565  C  CD    . GLU   A  1  1169 ? 15.124  76.436  115.223 1.00 21.12 ? 1167 GLU   A CD    1 
ATOM   8566  O  OE1   . GLU   A  1  1169 ? 15.418  76.533  114.010 1.00 20.43 ? 1167 GLU   A OE1   1 
ATOM   8567  O  OE2   . GLU   A  1  1169 ? 15.878  75.917  116.072 1.00 22.76 ? 1167 GLU   A OE2   1 
ATOM   8568  N  N     . GLY   A  1  1170 ? 11.959  79.483  117.036 1.00 21.56 ? 1168 GLY   A N     1 
ATOM   8569  C  CA    . GLY   A  1  1170 ? 12.497  80.570  117.823 1.00 23.73 ? 1168 GLY   A CA    1 
ATOM   8570  C  C     . GLY   A  1  1170 ? 11.915  80.569  119.215 1.00 26.63 ? 1168 GLY   A C     1 
ATOM   8571  O  O     . GLY   A  1  1170 ? 11.004  79.802  119.539 1.00 25.44 ? 1168 GLY   A O     1 
ATOM   8572  N  N     . ASP   A  1  1171 ? 12.449  81.470  120.031 1.00 25.12 ? 1169 ASP   A N     1 
ATOM   8573  C  CA    . ASP   A  1  1171 ? 11.824  81.711  121.319 1.00 23.83 ? 1169 ASP   A CA    1 
ATOM   8574  C  C     . ASP   A  1  1171 ? 10.523  82.484  121.119 1.00 27.16 ? 1169 ASP   A C     1 
ATOM   8575  O  O     . ASP   A  1  1171 ? 10.148  82.847  119.998 1.00 24.78 ? 1169 ASP   A O     1 
ATOM   8576  C  CB    . ASP   A  1  1171 ? 12.805  82.338  122.318 1.00 26.34 ? 1169 ASP   A CB    1 
ATOM   8577  C  CG    . ASP   A  1  1171 ? 13.305  83.718  121.902 1.00 30.87 ? 1169 ASP   A CG    1 
ATOM   8578  O  OD1   . ASP   A  1  1171 ? 12.675  84.390  121.063 1.00 28.83 ? 1169 ASP   A OD1   1 
ATOM   8579  O  OD2   . ASP   A  1  1171 ? 14.348  84.148  122.449 1.00 37.48 ? 1169 ASP   A OD2   1 
ATOM   8580  N  N     . ALA   A  1  1172 ? 9.817   82.730  122.225 1.00 27.34 ? 1170 ALA   A N     1 
ATOM   8581  C  CA    . ALA   A  1  1172 ? 8.478   83.299  122.137 1.00 26.64 ? 1170 ALA   A CA    1 
ATOM   8582  C  C     . ALA   A  1  1172 ? 8.482   84.635  121.405 1.00 27.00 ? 1170 ALA   A C     1 
ATOM   8583  O  O     . ALA   A  1  1172 ? 7.627   84.890  120.553 1.00 27.76 ? 1170 ALA   A O     1 
ATOM   8584  C  CB    . ALA   A  1  1172 ? 7.880   83.448  123.534 1.00 29.40 ? 1170 ALA   A CB    1 
ATOM   8585  N  N     . GLU   A  1  1173 ? 9.436   85.511  121.724 1.00 29.23 ? 1171 GLU   A N     1 
ATOM   8586  C  CA    . GLU   A  1  1173 ? 9.410   86.824  121.089 1.00 30.26 ? 1171 GLU   A CA    1 
ATOM   8587  C  C     . GLU   A  1  1173 ? 9.821   86.754  119.626 1.00 28.96 ? 1171 GLU   A C     1 
ATOM   8588  O  O     . GLU   A  1  1173 ? 9.302   87.517  118.802 1.00 28.86 ? 1171 GLU   A O     1 
ATOM   8589  C  CB    . GLU   A  1  1173 ? 10.230  87.839  121.881 1.00 34.20 ? 1171 GLU   A CB    1 
ATOM   8590  C  CG    . GLU   A  1  1173 ? 9.588   88.194  123.219 1.00 35.54 ? 1171 GLU   A CG    1 
ATOM   8591  C  CD    . GLU   A  1  1173 ? 8.112   88.576  123.097 1.00 40.24 ? 1171 GLU   A CD    1 
ATOM   8592  O  OE1   . GLU   A  1  1173 ? 7.750   89.327  122.163 1.00 40.20 ? 1171 GLU   A OE1   1 
ATOM   8593  O  OE2   . GLU   A  1  1173 ? 7.309   88.120  123.941 1.00 41.28 ? 1171 GLU   A OE2   1 
ATOM   8594  N  N     . ARG   A  1  1174 ? 10.722  85.834  119.281 1.00 26.50 ? 1172 ARG   A N     1 
ATOM   8595  C  CA    . ARG   A  1  1174 ? 11.034  85.606  117.872 1.00 25.84 ? 1172 ARG   A CA    1 
ATOM   8596  C  C     . ARG   A  1  1174 ? 9.808   85.103  117.124 1.00 25.06 ? 1172 ARG   A C     1 
ATOM   8597  O  O     . ARG   A  1  1174 ? 9.495   85.584  116.027 1.00 24.79 ? 1172 ARG   A O     1 
ATOM   8598  C  CB    . ARG   A  1  1174 ? 12.188  84.610  117.752 1.00 26.29 ? 1172 ARG   A CB    1 
ATOM   8599  C  CG    . ARG   A  1  1174 ? 12.519  84.194  116.323 1.00 25.83 ? 1172 ARG   A CG    1 
ATOM   8600  C  CD    . ARG   A  1  1174 ? 12.925  85.395  115.492 1.00 29.83 ? 1172 ARG   A CD    1 
ATOM   8601  N  NE    . ARG   A  1  1174 ? 13.249  85.025  114.118 1.00 27.30 ? 1172 ARG   A NE    1 
ATOM   8602  C  CZ    . ARG   A  1  1174 ? 13.318  85.884  113.110 1.00 30.88 ? 1172 ARG   A CZ    1 
ATOM   8603  N  NH1   . ARG   A  1  1174 ? 13.076  87.174  113.282 1.00 29.54 ? 1172 ARG   A NH1   1 
ATOM   8604  N  NH2   . ARG   A  1  1174 ? 13.628  85.437  111.898 1.00 27.77 ? 1172 ARG   A NH2   1 
ATOM   8605  N  N     . ILE   A  1  1175 ? 9.089   84.145  117.713 1.00 23.76 ? 1173 ILE   A N     1 
ATOM   8606  C  CA    . ILE   A  1  1175 ? 7.861   83.644  117.104 1.00 23.89 ? 1173 ILE   A CA    1 
ATOM   8607  C  C     . ILE   A  1  1175 ? 6.868   84.778  116.899 1.00 23.84 ? 1173 ILE   A C     1 
ATOM   8608  O  O     . ILE   A  1  1175 ? 6.273   84.921  115.825 1.00 24.37 ? 1173 ILE   A O     1 
ATOM   8609  C  CB    . ILE   A  1  1175 ? 7.262   82.516  117.962 1.00 24.72 ? 1173 ILE   A CB    1 
ATOM   8610  C  CG1   . ILE   A  1  1175 ? 8.162   81.281  117.900 1.00 25.75 ? 1173 ILE   A CG1   1 
ATOM   8611  C  CG2   . ILE   A  1  1175 ? 5.833   82.209  117.521 1.00 24.41 ? 1173 ILE   A CG2   1 
ATOM   8612  C  CD1   . ILE   A  1  1175 ? 7.817   80.216  118.932 1.00 26.75 ? 1173 ILE   A CD1   1 
ATOM   8613  N  N     . ARG   A  1  1176 ? 6.684   85.614  117.924 1.00 25.78 ? 1174 ARG   A N     1 
ATOM   8614  C  CA    . ARG   A  1  1176 ? 5.734   86.713  117.802 1.00 28.04 ? 1174 ARG   A CA    1 
ATOM   8615  C  C     . ARG   A  1  1176 ? 6.136   87.650  116.670 1.00 24.79 ? 1174 ARG   A C     1 
ATOM   8616  O  O     . ARG   A  1  1176 ? 5.304   88.028  115.834 1.00 26.37 ? 1174 ARG   A O     1 
ATOM   8617  C  CB    . ARG   A  1  1176 ? 5.621   87.463  119.131 1.00 25.42 ? 1174 ARG   A CB    1 
ATOM   8618  C  CG    . ARG   A  1  1176 ? 4.348   88.285  119.240 1.00 33.69 ? 1174 ARG   A CG    1 
ATOM   8619  C  CD    . ARG   A  1  1176 ? 4.410   89.260  120.409 1.00 32.91 ? 1174 ARG   A CD    1 
ATOM   8620  N  NE    . ARG   A  1  1176 ? 4.743   88.603  121.668 1.00 33.49 ? 1174 ARG   A NE    1 
ATOM   8621  C  CZ    . ARG   A  1  1176 ? 3.851   88.123  122.526 1.00 38.30 ? 1174 ARG   A CZ    1 
ATOM   8622  N  NH1   . ARG   A  1  1176 ? 2.553   88.148  122.262 1.00 34.07 ? 1174 ARG   A NH1   1 
ATOM   8623  N  NH2   . ARG   A  1  1176 ? 4.269   87.622  123.686 1.00 36.40 ? 1174 ARG   A NH2   1 
ATOM   8624  N  N     . ALA   A  1  1177 ? 7.421   88.000  116.604 1.00 26.68 ? 1175 ALA   A N     1 
ATOM   8625  C  CA    . ALA   A  1  1177 ? 7.903   88.892  115.554 1.00 28.12 ? 1175 ALA   A CA    1 
ATOM   8626  C  C     . ALA   A  1  1177 ? 7.705   88.273  114.180 1.00 24.51 ? 1175 ALA   A C     1 
ATOM   8627  O  O     . ALA   A  1  1177 ? 7.223   88.933  113.253 1.00 26.64 ? 1175 ALA   A O     1 
ATOM   8628  C  CB    . ALA   A  1  1177 ? 9.380   89.203  115.775 1.00 28.78 ? 1175 ALA   A CB    1 
ATOM   8629  N  N     . VAL   A  1  1178 ? 8.063   86.998  114.036 1.00 24.43 ? 1176 VAL   A N     1 
ATOM   8630  C  CA    . VAL   A  1  1178 ? 7.899   86.323  112.754 1.00 23.16 ? 1176 VAL   A CA    1 
ATOM   8631  C  C     . VAL   A  1  1178 ? 6.429   86.247  112.381 1.00 24.22 ? 1176 VAL   A C     1 
ATOM   8632  O  O     . VAL   A  1  1178 ? 6.056   86.463  111.221 1.00 24.36 ? 1176 VAL   A O     1 
ATOM   8633  C  CB    . VAL   A  1  1178 ? 8.556   84.932  112.783 1.00 23.04 ? 1176 VAL   A CB    1 
ATOM   8634  C  CG1   . VAL   A  1  1178 ? 8.184   84.154  111.532 1.00 21.92 ? 1176 VAL   A CG1   1 
ATOM   8635  C  CG2   . VAL   A  1  1178 ? 10.056  85.060  112.866 1.00 24.29 ? 1176 VAL   A CG2   1 
ATOM   8636  N  N     . ASN   A  1  1179 ? 5.572   85.934  113.352 1.00 25.63 ? 1177 ASN   A N     1 
ATOM   8637  C  CA    . ASN   A  1  1179 ? 4.148   85.824  113.072 1.00 23.73 ? 1177 ASN   A CA    1 
ATOM   8638  C  C     . ASN   A  1  1179 ? 3.593   87.148  112.561 1.00 28.23 ? 1177 ASN   A C     1 
ATOM   8639  O  O     . ASN   A  1  1179 ? 2.731   87.170  111.674 1.00 24.73 ? 1177 ASN   A O     1 
ATOM   8640  C  CB    . ASN   A  1  1179 ? 3.416   85.371  114.337 1.00 27.45 ? 1177 ASN   A CB    1 
ATOM   8641  C  CG    . ASN   A  1  1179 ? 2.219   84.495  114.048 1.00 31.42 ? 1177 ASN   A CG    1 
ATOM   8642  O  OD1   . ASN   A  1  1179 ? 2.069   83.959  112.946 1.00 35.73 ? 1177 ASN   A OD1   1 
ATOM   8643  N  ND2   . ASN   A  1  1179 ? 1.349   84.342  115.044 1.00 35.69 ? 1177 ASN   A ND2   1 
ATOM   8644  N  N     . LYS   A  1  1180 ? 4.084   88.267  113.099 1.00 26.79 ? 1178 LYS   A N     1 
ATOM   8645  C  CA    . LYS   A  1  1180 ? 3.644   89.568  112.606 1.00 28.75 ? 1178 LYS   A CA    1 
ATOM   8646  C  C     . LYS   A  1  1180 ? 4.098   89.793  111.171 1.00 26.31 ? 1178 LYS   A C     1 
ATOM   8647  O  O     . LYS   A  1  1180 ? 3.317   90.265  110.336 1.00 25.93 ? 1178 LYS   A O     1 
ATOM   8648  C  CB    . LYS   A  1  1180 ? 4.160   90.682  113.517 1.00 28.71 ? 1178 LYS   A CB    1 
ATOM   8649  C  CG    . LYS   A  1  1180 ? 3.567   90.644  114.923 1.00 30.91 ? 1178 LYS   A CG    1 
ATOM   8650  C  CD    . LYS   A  1  1180 ? 4.312   91.559  115.892 1.00 30.59 ? 1178 LYS   A CD    1 
ATOM   8651  C  CE    . LYS   A  1  1180 ? 4.318   93.010  115.423 1.00 38.13 ? 1178 LYS   A CE    1 
ATOM   8652  N  NZ    . LYS   A  1  1180 ? 4.980   93.907  116.413 1.00 44.01 ? 1178 LYS   A NZ    1 
ATOM   8653  N  N     . ALA   A  1  1181 ? 5.348   89.449  110.865 1.00 24.68 ? 1179 ALA   A N     1 
ATOM   8654  C  CA    . ALA   A  1  1181 ? 5.844   89.595  109.500 1.00 24.96 ? 1179 ALA   A CA    1 
ATOM   8655  C  C     . ALA   A  1  1181 ? 5.080   88.700  108.534 1.00 22.83 ? 1179 ALA   A C     1 
ATOM   8656  O  O     . ALA   A  1  1181 ? 4.766   89.110  107.412 1.00 24.68 ? 1179 ALA   A O     1 
ATOM   8657  C  CB    . ALA   A  1  1181 ? 7.337   89.293  109.448 1.00 23.26 ? 1179 ALA   A CB    1 
ATOM   8658  N  N     . ILE   A  1  1182 ? 4.756   87.478  108.959 1.00 24.04 ? 1180 ILE   A N     1 
ATOM   8659  C  CA    . ILE   A  1  1182 ? 4.016   86.568  108.092 1.00 22.06 ? 1180 ILE   A CA    1 
ATOM   8660  C  C     . ILE   A  1  1182 ? 2.616   87.095  107.837 1.00 25.04 ? 1180 ILE   A C     1 
ATOM   8661  O  O     . ILE   A  1  1182 ? 2.113   87.056  106.705 1.00 23.75 ? 1180 ILE   A O     1 
ATOM   8662  C  CB    . ILE   A  1  1182 ? 3.990   85.151  108.689 1.00 20.70 ? 1180 ILE   A CB    1 
ATOM   8663  C  CG1   . ILE   A  1  1182 ? 5.385   84.534  108.648 1.00 23.27 ? 1180 ILE   A CG1   1 
ATOM   8664  C  CG2   . ILE   A  1  1182 ? 2.968   84.295  107.963 1.00 23.51 ? 1180 ILE   A CG2   1 
ATOM   8665  C  CD1   . ILE   A  1  1182 ? 5.474   83.182  109.341 1.00 25.57 ? 1180 ILE   A CD1   1 
ATOM   8666  N  N     . ALA   A  1  1183 ? 1.959   87.590  108.884 1.00 22.58 ? 1181 ALA   A N     1 
ATOM   8667  C  CA    . ALA   A  1  1183 ? 0.620   88.131  108.712 1.00 22.95 ? 1181 ALA   A CA    1 
ATOM   8668  C  C     . ALA   A  1  1183 ? 0.616   89.281  107.718 1.00 27.01 ? 1181 ALA   A C     1 
ATOM   8669  O  O     . ALA   A  1  1183 ? -0.368  89.476  106.996 1.00 25.46 ? 1181 ALA   A O     1 
ATOM   8670  C  CB    . ALA   A  1  1183 ? 0.060   88.583  110.061 1.00 24.62 ? 1181 ALA   A CB    1 
ATOM   8671  N  N     . ALA   A  1  1184 ? 1.712   90.033  107.646 1.00 23.55 ? 1182 ALA   A N     1 
ATOM   8672  C  CA    . ALA   A  1  1184 ? 1.776   91.180  106.755 1.00 25.48 ? 1182 ALA   A CA    1 
ATOM   8673  C  C     . ALA   A  1  1184 ? 2.004   90.789  105.305 1.00 24.02 ? 1182 ALA   A C     1 
ATOM   8674  O  O     . ALA   A  1  1184 ? 1.940   91.664  104.436 1.00 26.26 ? 1182 ALA   A O     1 
ATOM   8675  C  CB    . ALA   A  1  1184 ? 2.880   92.140  107.210 1.00 25.00 ? 1182 ALA   A CB    1 
ATOM   8676  N  N     . LEU   A  1  1185 ? 2.267   89.514  105.022 1.00 22.85 ? 1183 LEU   A N     1 
ATOM   8677  C  CA    . LEU   A  1  1185 ? 2.509   89.109  103.647 1.00 25.21 ? 1183 LEU   A CA    1 
ATOM   8678  C  C     . LEU   A  1  1185 ? 1.221   89.242  102.843 1.00 25.07 ? 1183 LEU   A C     1 
ATOM   8679  O  O     . LEU   A  1  1185 ? 0.132   88.969  103.360 1.00 25.95 ? 1183 LEU   A O     1 
ATOM   8680  C  CB    . LEU   A  1  1185 ? 2.995   87.663  103.582 1.00 22.36 ? 1183 LEU   A CB    1 
ATOM   8681  C  CG    . LEU   A  1  1185 ? 4.319   87.380  104.293 1.00 24.12 ? 1183 LEU   A CG    1 
ATOM   8682  C  CD1   . LEU   A  1  1185 ? 4.636   85.894  104.268 1.00 23.61 ? 1183 LEU   A CD1   1 
ATOM   8683  C  CD2   . LEU   A  1  1185 ? 5.453   88.185  103.673 1.00 25.23 ? 1183 LEU   A CD2   1 
ATOM   8684  N  N     . PRO   A  1  1186 ? 1.305   89.669  101.587 1.00 26.48 ? 1184 PRO   A N     1 
ATOM   8685  C  CA    . PRO   A  1  1186 ? 0.094   89.772  100.773 1.00 24.67 ? 1184 PRO   A CA    1 
ATOM   8686  C  C     . PRO   A  1  1186 ? -0.495  88.402  100.500 1.00 23.24 ? 1184 PRO   A C     1 
ATOM   8687  O  O     . PRO   A  1  1186 ? 0.202   87.386  100.479 1.00 24.76 ? 1184 PRO   A O     1 
ATOM   8688  C  CB    . PRO   A  1  1186 ? 0.593   90.412  99.471  1.00 27.50 ? 1184 PRO   A CB    1 
ATOM   8689  C  CG    . PRO   A  1  1186 ? 2.030   90.046  99.405  1.00 31.73 ? 1184 PRO   A CG    1 
ATOM   8690  C  CD    . PRO   A  1  1186 ? 2.513   90.046  100.836 1.00 28.26 ? 1184 PRO   A CD    1 
ATOM   8691  N  N     . GLY   A  1  1187 ? -1.804  88.387  100.308 1.00 22.48 ? 1185 GLY   A N     1 
ATOM   8692  C  CA    . GLY   A  1  1187 ? -2.464  87.216  99.796  1.00 27.11 ? 1185 GLY   A CA    1 
ATOM   8693  C  C     . GLY   A  1  1187 ? -3.039  86.322  100.871 1.00 21.05 ? 1185 GLY   A C     1 
ATOM   8694  O  O     . GLY   A  1  1187 ? -3.727  86.774  101.792 1.00 24.26 ? 1185 GLY   A O     1 
ATOM   8695  N  N     . PRO   A  1  1188 ? -2.779  85.024  100.755 1.00 22.21 ? 1186 PRO   A N     1 
ATOM   8696  C  CA    . PRO   A  1  1188 ? -3.509  84.057  101.575 1.00 21.37 ? 1186 PRO   A CA    1 
ATOM   8697  C  C     . PRO   A  1  1188 ? -3.054  84.108  103.019 1.00 20.62 ? 1186 PRO   A C     1 
ATOM   8698  O  O     . PRO   A  1  1188 ? -1.903  84.423  103.330 1.00 21.69 ? 1186 PRO   A O     1 
ATOM   8699  C  CB    . PRO   A  1  1188 ? -3.150  82.711  100.936 1.00 23.03 ? 1186 PRO   A CB    1 
ATOM   8700  C  CG    . PRO   A  1  1188 ? -1.800  82.930  100.343 1.00 23.21 ? 1186 PRO   A CG    1 
ATOM   8701  C  CD    . PRO   A  1  1188 ? -1.786  84.378  99.884  1.00 23.11 ? 1186 PRO   A CD    1 
ATOM   8702  N  N     . LEU   A  1  1189 ? -3.990  83.805  103.906 1.00 21.01 ? 1187 LEU   A N     1 
ATOM   8703  C  CA    . LEU   A  1  1189 ? -3.623  83.545  105.286 1.00 20.60 ? 1187 LEU   A CA    1 
ATOM   8704  C  C     . LEU   A  1  1189 ? -2.768  82.286  105.329 1.00 21.78 ? 1187 LEU   A C     1 
ATOM   8705  O  O     . LEU   A  1  1189 ? -3.037  81.307  104.627 1.00 24.79 ? 1187 LEU   A O     1 
ATOM   8706  C  CB    . LEU   A  1  1189 ? -4.882  83.374  106.135 1.00 21.94 ? 1187 LEU   A CB    1 
ATOM   8707  C  CG    . LEU   A  1  1189 ? -5.587  84.670  106.569 1.00 22.56 ? 1187 LEU   A CG    1 
ATOM   8708  C  CD1   . LEU   A  1  1189 ? -6.276  85.366  105.401 1.00 23.13 ? 1187 LEU   A CD1   1 
ATOM   8709  C  CD2   . LEU   A  1  1189 ? -6.584  84.370  107.671 1.00 26.05 ? 1187 LEU   A CD2   1 
ATOM   8710  N  N     . LEU   A  1  1190 ? -1.692  82.331  106.094 1.00 20.98 ? 1188 LEU   A N     1 
ATOM   8711  C  CA    . LEU   A  1  1190 ? -0.789  81.197  106.173 1.00 22.26 ? 1188 LEU   A CA    1 
ATOM   8712  C  C     . LEU   A  1  1190 ? -1.019  80.453  107.477 1.00 19.36 ? 1188 LEU   A C     1 
ATOM   8713  O  O     . LEU   A  1  1190 ? -1.097  81.068  108.546 1.00 23.12 ? 1188 LEU   A O     1 
ATOM   8714  C  CB    . LEU   A  1  1190 ? 0.669   81.637  106.065 1.00 22.15 ? 1188 LEU   A CB    1 
ATOM   8715  C  CG    . LEU   A  1  1190 ? 1.029   82.373  104.775 1.00 22.15 ? 1188 LEU   A CG    1 
ATOM   8716  C  CD1   . LEU   A  1  1190 ? 2.526   82.561  104.713 1.00 27.77 ? 1188 LEU   A CD1   1 
ATOM   8717  C  CD2   . LEU   A  1  1190 ? 0.530   81.612  103.541 1.00 23.51 ? 1188 LEU   A CD2   1 
ATOM   8718  N  N     . LEU   A  1  1191 ? -1.150  79.138  107.378 1.00 19.83 ? 1189 LEU   A N     1 
ATOM   8719  C  CA    . LEU   A  1  1191 ? -1.187  78.295  108.562 1.00 20.45 ? 1189 LEU   A CA    1 
ATOM   8720  C  C     . LEU   A  1  1191 ? 0.247   78.180  109.051 1.00 19.90 ? 1189 LEU   A C     1 
ATOM   8721  O  O     . LEU   A  1  1191 ? 1.075   77.516  108.418 1.00 21.64 ? 1189 LEU   A O     1 
ATOM   8722  C  CB    . LEU   A  1  1191 ? -1.777  76.932  108.214 1.00 21.43 ? 1189 LEU   A CB    1 
ATOM   8723  C  CG    . LEU   A  1  1191 ? -2.325  76.082  109.364 1.00 18.91 ? 1189 LEU   A CG    1 
ATOM   8724  C  CD1   . LEU   A  1  1191 ? -3.163  74.942  108.811 1.00 20.13 ? 1189 LEU   A CD1   1 
ATOM   8725  C  CD2   . LEU   A  1  1191 ? -1.187  75.517  110.237 1.00 19.95 ? 1189 LEU   A CD2   1 
ATOM   8726  N  N     . VAL   A  1  1192 ? 0.540   78.849  110.163 1.00 19.11 ? 1190 VAL   A N     1 
ATOM   8727  C  CA    . VAL   A  1  1192 ? 1.878   78.919  110.734 1.00 17.79 ? 1190 VAL   A CA    1 
ATOM   8728  C  C     . VAL   A  1  1192 ? 1.967   77.929  111.884 1.00 18.66 ? 1190 VAL   A C     1 
ATOM   8729  O  O     . VAL   A  1  1192 ? 1.071   77.862  112.735 1.00 21.94 ? 1190 VAL   A O     1 
ATOM   8730  C  CB    . VAL   A  1  1192 ? 2.165   80.344  111.237 1.00 21.74 ? 1190 VAL   A CB    1 
ATOM   8731  C  CG1   . VAL   A  1  1192 ? 3.562   80.418  111.837 1.00 24.35 ? 1190 VAL   A CG1   1 
ATOM   8732  C  CG2   . VAL   A  1  1192 ? 2.000   81.344  110.104 1.00 25.31 ? 1190 VAL   A CG2   1 
ATOM   8733  N  N     . GLN   A  1  1193 ? 3.058   77.176  111.928 1.00 20.44 ? 1191 GLN   A N     1 
ATOM   8734  C  CA    . GLN   A  1  1193 ? 3.395   76.375  113.091 1.00 18.22 ? 1191 GLN   A CA    1 
ATOM   8735  C  C     . GLN   A  1  1193 ? 4.727   76.861  113.614 1.00 20.40 ? 1191 GLN   A C     1 
ATOM   8736  O  O     . GLN   A  1  1193 ? 5.665   77.064  112.837 1.00 21.15 ? 1191 GLN   A O     1 
ATOM   8737  C  CB    . GLN   A  1  1193 ? 3.523   74.907  112.732 1.00 19.03 ? 1191 GLN   A CB    1 
ATOM   8738  C  CG    . GLN   A  1  1193 ? 2.279   74.344  112.099 1.00 20.84 ? 1191 GLN   A CG    1 
ATOM   8739  C  CD    . GLN   A  1  1193 ? 2.324   72.838  112.032 1.00 21.35 ? 1191 GLN   A CD    1 
ATOM   8740  O  OE1   . GLN   A  1  1193 ? 2.228   72.158  113.056 1.00 22.68 ? 1191 GLN   A OE1   1 
ATOM   8741  N  NE2   . GLN   A  1  1193 ? 2.470   72.308  110.827 1.00 21.28 ? 1191 GLN   A NE2   1 
ATOM   8742  N  N     . ALA   A  1  1194 ? 4.816   77.031  114.921 1.00 19.80 ? 1192 ALA   A N     1 
ATOM   8743  C  CA    . ALA   A  1  1194 ? 6.037   77.518  115.528 1.00 18.74 ? 1192 ALA   A CA    1 
ATOM   8744  C  C     . ALA   A  1  1194 ? 6.480   76.556  116.614 1.00 19.84 ? 1192 ALA   A C     1 
ATOM   8745  O  O     . ALA   A  1  1194 ? 5.665   75.896  117.260 1.00 21.92 ? 1192 ALA   A O     1 
ATOM   8746  C  CB    . ALA   A  1  1194 ? 5.823   78.901  116.131 1.00 22.53 ? 1192 ALA   A CB    1 
ATOM   8747  N  N     . ALA   A  1  1195 ? 7.788   76.499  116.818 1.00 20.01 ? 1193 ALA   A N     1 
ATOM   8748  C  CA    . ALA   A  1  1195 ? 8.343   75.688  117.880 1.00 21.78 ? 1193 ALA   A CA    1 
ATOM   8749  C  C     . ALA   A  1  1195 ? 9.640   76.335  118.321 1.00 21.67 ? 1193 ALA   A C     1 
ATOM   8750  O  O     . ALA   A  1  1195 ? 10.304  77.018  117.538 1.00 23.39 ? 1193 ALA   A O     1 
ATOM   8751  C  CB    . ALA   A  1  1195 ? 8.603   74.260  117.394 1.00 22.65 ? 1193 ALA   A CB    1 
ATOM   8752  N  N     . SER   A  1  1196 ? 9.988   76.132  119.583 1.00 21.19 ? 1194 SER   A N     1 
ATOM   8753  C  CA    . SER   A  1  1196 ? 11.315  76.516  120.025 1.00 23.09 ? 1194 SER   A CA    1 
ATOM   8754  C  C     . SER   A  1  1196 ? 12.329  75.458  119.602 1.00 22.02 ? 1194 SER   A C     1 
ATOM   8755  O  O     . SER   A  1  1196 ? 11.984  74.327  119.252 1.00 21.38 ? 1194 SER   A O     1 
ATOM   8756  C  CB    . SER   A  1  1196 ? 11.350  76.638  121.544 1.00 25.07 ? 1194 SER   A CB    1 
ATOM   8757  O  OG    . SER   A  1  1196 ? 11.194  75.361  122.133 1.00 26.25 ? 1194 SER   A OG    1 
ATOM   8758  N  N     . SER   A  1  1197 ? 13.606  75.837  119.633 1.00 23.83 ? 1195 SER   A N     1 
ATOM   8759  C  CA    . SER   A  1  1197 ? 14.654  74.860  119.355 1.00 25.33 ? 1195 SER   A CA    1 
ATOM   8760  C  C     . SER   A  1  1197 ? 14.573  73.676  120.315 1.00 22.75 ? 1195 SER   A C     1 
ATOM   8761  O  O     . SER   A  1  1197 ? 14.743  72.520  119.905 1.00 24.81 ? 1195 SER   A O     1 
ATOM   8762  C  CB    . SER   A  1  1197 ? 16.027  75.526  119.451 1.00 25.97 ? 1195 SER   A CB    1 
ATOM   8763  O  OG    . SER   A  1  1197 ? 16.141  76.616  118.551 1.00 25.51 ? 1195 SER   A OG    1 
ATOM   8764  N  N     . GLY   A  1  1198 ? 14.305  73.945  121.593 1.00 25.80 ? 1196 GLY   A N     1 
ATOM   8765  C  CA    . GLY   A  1  1198 ? 14.187  72.861  122.558 1.00 26.83 ? 1196 GLY   A CA    1 
ATOM   8766  C  C     . GLY   A  1  1198 ? 12.997  71.962  122.282 1.00 27.54 ? 1196 GLY   A C     1 
ATOM   8767  O  O     . GLY   A  1  1198 ? 13.077  70.739  122.433 1.00 27.57 ? 1196 GLY   A O     1 
ATOM   8768  N  N     . GLU   A  1  1199 ? 11.880  72.553  121.860 1.00 25.26 ? 1197 GLU   A N     1 
ATOM   8769  C  CA    . GLU   A  1  1199 ? 10.718  71.763  121.479 1.00 26.70 ? 1197 GLU   A CA    1 
ATOM   8770  C  C     . GLU   A  1  1199 ? 11.033  70.868  120.286 1.00 25.26 ? 1197 GLU   A C     1 
ATOM   8771  O  O     . GLU   A  1  1199 ? 10.638  69.697  120.255 1.00 24.53 ? 1197 GLU   A O     1 
ATOM   8772  C  CB    . GLU   A  1  1199 ? 9.575   72.717  121.161 1.00 24.67 ? 1197 GLU   A CB    1 
ATOM   8773  C  CG    . GLU   A  1  1199 ? 8.224   72.096  120.965 1.00 31.05 ? 1197 GLU   A CG    1 
ATOM   8774  C  CD    . GLU   A  1  1199 ? 7.164   73.164  120.749 1.00 38.11 ? 1197 GLU   A CD    1 
ATOM   8775  O  OE1   . GLU   A  1  1199 ? 7.485   74.363  120.948 1.00 34.51 ? 1197 GLU   A OE1   1 
ATOM   8776  O  OE2   . GLU   A  1  1199 ? 6.022   72.811  120.383 1.00 42.37 ? 1197 GLU   A OE2   1 
ATOM   8777  N  N     . ILE   A  1  1200 ? 11.737  71.403  119.285 1.00 23.13 ? 1198 ILE   A N     1 
ATOM   8778  C  CA    . ILE   A  1  1200 ? 12.157  70.578  118.156 1.00 23.90 ? 1198 ILE   A CA    1 
ATOM   8779  C  C     . ILE   A  1  1200 ? 12.992  69.398  118.639 1.00 26.12 ? 1198 ILE   A C     1 
ATOM   8780  O  O     . ILE   A  1  1200 ? 12.828  68.265  118.171 1.00 26.39 ? 1198 ILE   A O     1 
ATOM   8781  C  CB    . ILE   A  1  1200 ? 12.900  71.436  117.116 1.00 22.06 ? 1198 ILE   A CB    1 
ATOM   8782  C  CG1   . ILE   A  1  1200 ? 11.937  72.435  116.474 1.00 22.97 ? 1198 ILE   A CG1   1 
ATOM   8783  C  CG2   . ILE   A  1  1200 ? 13.569  70.556  116.055 1.00 23.14 ? 1198 ILE   A CG2   1 
ATOM   8784  C  CD1   . ILE   A  1  1200 ? 12.607  73.460  115.588 1.00 23.44 ? 1198 ILE   A CD1   1 
ATOM   8785  N  N     . ALA   A  1  1201 ? 13.872  69.636  119.616 1.00 24.62 ? 1199 ALA   A N     1 
ATOM   8786  C  CA    . ALA   A  1  1201 ? 14.714  68.561  120.131 1.00 26.87 ? 1199 ALA   A CA    1 
ATOM   8787  C  C     . ALA   A  1  1201 ? 13.899  67.531  120.904 1.00 27.69 ? 1199 ALA   A C     1 
ATOM   8788  O  O     . ALA   A  1  1201 ? 14.157  66.326  120.803 1.00 28.21 ? 1199 ALA   A O     1 
ATOM   8789  C  CB    . ALA   A  1  1201 ? 15.813  69.147  121.015 1.00 27.34 ? 1199 ALA   A CB    1 
ATOM   8790  N  N     . ARG   A  1  1202 ? 12.911  67.983  121.675 1.00 24.82 ? 1200 ARG   A N     1 
ATOM   8791  C  CA    . ARG   A  1  1202 ? 12.168  67.101  122.569 1.00 25.18 ? 1200 ARG   A CA    1 
ATOM   8792  C  C     . ARG   A  1  1202 ? 11.010  66.384  121.890 1.00 28.54 ? 1200 ARG   A C     1 
ATOM   8793  O  O     . ARG   A  1  1202 ? 10.715  65.235  122.232 1.00 28.72 ? 1200 ARG   A O     1 
ATOM   8794  C  CB    . ARG   A  1  1202 ? 11.616  67.899  123.750 1.00 28.12 ? 1200 ARG   A CB    1 
ATOM   8795  C  CG    . ARG   A  1  1202 ? 12.686  68.372  124.726 1.00 25.69 ? 1200 ARG   A CG    1 
ATOM   8796  C  CD    . ARG   A  1  1202 ? 12.048  69.044  125.930 1.00 28.17 ? 1200 ARG   A CD    1 
ATOM   8797  N  NE    . ARG   A  1  1202 ? 11.235  70.183  125.531 1.00 31.36 ? 1200 ARG   A NE    1 
ATOM   8798  C  CZ    . ARG   A  1  1202 ? 11.639  71.447  125.552 1.00 30.83 ? 1200 ARG   A CZ    1 
ATOM   8799  N  NH1   . ARG   A  1  1202 ? 12.828  71.790  126.027 1.00 27.50 ? 1200 ARG   A NH1   1 
ATOM   8800  N  NH2   . ARG   A  1  1202 ? 10.829  72.392  125.080 1.00 31.34 ? 1200 ARG   A NH2   1 
ATOM   8801  N  N     . ASN   A  1  1203 ? 10.330  67.033  120.958 1.00 25.29 ? 1201 ASN   A N     1 
ATOM   8802  C  CA    . ASN   A  1  1203 ? 9.061   66.519  120.448 1.00 25.05 ? 1201 ASN   A CA    1 
ATOM   8803  C  C     . ASN   A  1  1203 ? 9.165   66.224  118.960 1.00 27.91 ? 1201 ASN   A C     1 
ATOM   8804  O  O     . ASN   A  1  1203 ? 9.263   67.165  118.149 1.00 26.72 ? 1201 ASN   A O     1 
ATOM   8805  C  CB    . ASN   A  1  1203 ? 7.952   67.535  120.718 1.00 27.76 ? 1201 ASN   A CB    1 
ATOM   8806  C  CG    . ASN   A  1  1203 ? 6.589   67.075  120.218 1.00 29.31 ? 1201 ASN   A CG    1 
ATOM   8807  O  OD1   . ASN   A  1  1203 ? 6.416   65.933  119.791 1.00 30.53 ? 1201 ASN   A OD1   1 
ATOM   8808  N  ND2   . ASN   A  1  1203 ? 5.610   67.972  120.279 1.00 30.00 ? 1201 ASN   A ND2   1 
ATOM   8809  N  N     . PRO   A  1  1204 ? 9.127   64.955  118.548 1.00 28.01 ? 1202 PRO   A N     1 
ATOM   8810  C  CA    . PRO   A  1  1204 ? 9.178   64.649  117.112 1.00 30.70 ? 1202 PRO   A CA    1 
ATOM   8811  C  C     . PRO   A  1  1204 ? 8.023   65.243  116.333 1.00 28.17 ? 1202 PRO   A C     1 
ATOM   8812  O  O     . PRO   A  1  1204 ? 8.137   65.408  115.113 1.00 30.27 ? 1202 PRO   A O     1 
ATOM   8813  C  CB    . PRO   A  1  1204 ? 9.158   63.113  117.074 1.00 36.11 ? 1202 PRO   A CB    1 
ATOM   8814  C  CG    . PRO   A  1  1204 ? 9.592   62.688  118.445 1.00 37.01 ? 1202 PRO   A CG    1 
ATOM   8815  C  CD    . PRO   A  1  1204 ? 9.040   63.737  119.370 1.00 31.49 ? 1202 PRO   A CD    1 
ATOM   8816  N  N     . ASP   A  1  1205 ? 6.920   65.578  117.002 1.00 29.73 ? 1203 ASP   A N     1 
ATOM   8817  C  CA    . ASP   A  1  1205 ? 5.768   66.196  116.361 1.00 29.29 ? 1203 ASP   A CA    1 
ATOM   8818  C  C     . ASP   A  1  1205 ? 5.685   67.694  116.630 1.00 29.61 ? 1203 ASP   A C     1 
ATOM   8819  O  O     . ASP   A  1  1205 ? 4.589   68.266  116.574 1.00 31.48 ? 1203 ASP   A O     1 
ATOM   8820  C  CB    . ASP   A  1  1205 ? 4.481   65.501  116.807 1.00 35.11 ? 1203 ASP   A CB    1 
ATOM   8821  C  CG    . ASP   A  1  1205 ? 4.472   64.026  116.471 1.00 39.53 ? 1203 ASP   A CG    1 
ATOM   8822  O  OD1   . ASP   A  1  1205 ? 5.225   63.617  115.560 1.00 35.00 ? 1203 ASP   A OD1   1 
ATOM   8823  O  OD2   . ASP   A  1  1205 ? 3.710   63.279  117.119 1.00 41.38 ? 1203 ASP   A OD2   1 
ATOM   8824  N  N     . ALA   A  1  1206 ? 6.818   68.333  116.945 1.00 25.48 ? 1204 ALA   A N     1 
ATOM   8825  C  CA    . ALA   A  1  1206 ? 6.828   69.778  117.158 1.00 24.64 ? 1204 ALA   A CA    1 
ATOM   8826  C  C     . ALA   A  1  1206 ? 6.123   70.499  116.020 1.00 25.46 ? 1204 ALA   A C     1 
ATOM   8827  O  O     . ALA   A  1  1206 ? 5.320   71.411  116.252 1.00 28.70 ? 1204 ALA   A O     1 
ATOM   8828  C  CB    . ALA   A  1  1206 ? 8.264   70.274  117.291 1.00 23.77 ? 1204 ALA   A CB    1 
ATOM   8829  N  N     . TYR   A  1  1207 ? 6.395   70.091  114.785 1.00 24.09 ? 1205 TYR   A N     1 
ATOM   8830  C  CA    . TYR   A  1  1207 ? 5.638   70.531  113.623 1.00 24.72 ? 1205 TYR   A CA    1 
ATOM   8831  C  C     . TYR   A  1  1207 ? 4.750   69.381  113.190 1.00 24.73 ? 1205 TYR   A C     1 
ATOM   8832  O  O     . TYR   A  1  1207 ? 5.248   68.311  112.825 1.00 29.55 ? 1205 TYR   A O     1 
ATOM   8833  C  CB    . TYR   A  1  1207 ? 6.573   70.916  112.485 1.00 22.68 ? 1205 TYR   A CB    1 
ATOM   8834  C  CG    . TYR   A  1  1207 ? 7.501   72.037  112.844 1.00 20.50 ? 1205 TYR   A CG    1 
ATOM   8835  C  CD1   . TYR   A  1  1207 ? 7.001   73.289  113.195 1.00 22.06 ? 1205 TYR   A CD1   1 
ATOM   8836  C  CD2   . TYR   A  1  1207 ? 8.876   71.854  112.833 1.00 20.56 ? 1205 TYR   A CD2   1 
ATOM   8837  C  CE1   . TYR   A  1  1207 ? 7.848   74.326  113.519 1.00 20.35 ? 1205 TYR   A CE1   1 
ATOM   8838  C  CE2   . TYR   A  1  1207 ? 9.736   72.888  113.154 1.00 21.95 ? 1205 TYR   A CE2   1 
ATOM   8839  C  CZ    . TYR   A  1  1207 ? 9.213   74.121  113.493 1.00 21.78 ? 1205 TYR   A CZ    1 
ATOM   8840  O  OH    . TYR   A  1  1207 ? 10.066  75.143  113.818 1.00 22.87 ? 1205 TYR   A OH    1 
ATOM   8841  N  N     . CYS   A  1  1208 ? 3.448   69.609  113.205 1.00 22.29 ? 1206 CYS   A N     1 
ATOM   8842  C  CA    . CYS   A  1  1208 ? 2.489   68.562  112.915 1.00 21.83 ? 1206 CYS   A CA    1 
ATOM   8843  C  C     . CYS   A  1  1208 ? 2.298   68.463  111.409 1.00 20.26 ? 1206 CYS   A C     1 
ATOM   8844  O  O     . CYS   A  1  1208 ? 2.027   69.464  110.739 1.00 20.15 ? 1206 CYS   A O     1 
ATOM   8845  C  CB    . CYS   A  1  1208 ? 1.168   68.878  113.613 1.00 23.96 ? 1206 CYS   A CB    1 
ATOM   8846  S  SG    . CYS   A  1  1208 ? -0.136  67.691  113.323 1.00 27.38 ? 1206 CYS   A SG    1 
ATOM   8847  N  N     . LEU   A  1  1209 ? 2.452   67.249  110.881 1.00 18.45 ? 1207 LEU   A N     1 
ATOM   8848  C  CA    . LEU   A  1  1209 ? 2.363   67.045  109.447 1.00 17.38 ? 1207 LEU   A CA    1 
ATOM   8849  C  C     . LEU   A  1  1209 ? 0.935   67.146  108.933 1.00 18.81 ? 1207 LEU   A C     1 
ATOM   8850  O  O     . LEU   A  1  1209 ? 0.745   67.311  107.725 1.00 19.43 ? 1207 LEU   A O     1 
ATOM   8851  C  CB    . LEU   A  1  1209 ? 2.971   65.692  109.077 1.00 18.08 ? 1207 LEU   A CB    1 
ATOM   8852  C  CG    . LEU   A  1  1209 ? 4.404   65.497  109.556 1.00 18.72 ? 1207 LEU   A CG    1 
ATOM   8853  C  CD1   . LEU   A  1  1209 ? 4.879   64.129  109.101 1.00 22.45 ? 1207 LEU   A CD1   1 
ATOM   8854  C  CD2   . LEU   A  1  1209 ? 5.306   66.597  108.994 1.00 21.79 ? 1207 LEU   A CD2   1 
ATOM   8855  N  N     . ASN   A  1  1210 ? -0.066  67.049  109.821 1.00 19.91 ? 1208 ASN   A N     1 
ATOM   8856  C  CA    . ASN   A  1  1210 ? -1.456  67.222  109.406 1.00 21.00 ? 1208 ASN   A CA    1 
ATOM   8857  C  C     . ASN   A  1  1210 ? -1.652  68.542  108.673 1.00 19.83 ? 1208 ASN   A C     1 
ATOM   8858  O  O     . ASN   A  1  1210 ? -2.477  68.635  107.763 1.00 21.76 ? 1208 ASN   A O     1 
ATOM   8859  C  CB    . ASN   A  1  1210 ? -2.393  67.222  110.623 1.00 23.76 ? 1208 ASN   A CB    1 
ATOM   8860  C  CG    . ASN   A  1  1210 ? -2.467  65.876  111.337 1.00 23.92 ? 1208 ASN   A CG    1 
ATOM   8861  O  OD1   . ASN   A  1  1210 ? -1.664  64.980  111.103 1.00 33.58 ? 1208 ASN   A OD1   1 
ATOM   8862  N  ND2   . ASN   A  1  1210 ? -3.427  65.753  112.250 1.00 31.12 ? 1208 ASN   A ND2   1 
ATOM   8863  N  N     . TRP   A  1  1211 ? -0.935  69.587  109.091 1.00 19.86 ? 1209 TRP   A N     1 
ATOM   8864  C  CA    . TRP   A  1  1211 ? -1.168  70.931  108.585 1.00 19.65 ? 1209 TRP   A CA    1 
ATOM   8865  C  C     . TRP   A  1  1211 ? -0.228  71.299  107.458 1.00 21.46 ? 1209 TRP   A C     1 
ATOM   8866  O  O     . TRP   A  1  1211 ? -0.229  72.453  107.021 1.00 23.00 ? 1209 TRP   A O     1 
ATOM   8867  C  CB    . TRP   A  1  1211 ? -1.080  71.963  109.712 1.00 20.65 ? 1209 TRP   A CB    1 
ATOM   8868  C  CG    . TRP   A  1  1211 ? -1.646  71.469  110.993 1.00 19.33 ? 1209 TRP   A CG    1 
ATOM   8869  C  CD1   . TRP   A  1  1211 ? -1.014  71.437  112.207 1.00 20.71 ? 1209 TRP   A CD1   1 
ATOM   8870  C  CD2   . TRP   A  1  1211 ? -2.947  70.903  111.206 1.00 18.82 ? 1209 TRP   A CD2   1 
ATOM   8871  N  NE1   . TRP   A  1  1211 ? -1.841  70.890  113.157 1.00 23.34 ? 1209 TRP   A NE1   1 
ATOM   8872  C  CE2   . TRP   A  1  1211 ? -3.030  70.553  112.566 1.00 18.89 ? 1209 TRP   A CE2   1 
ATOM   8873  C  CE3   . TRP   A  1  1211 ? -4.044  70.647  110.375 1.00 19.34 ? 1209 TRP   A CE3   1 
ATOM   8874  C  CZ2   . TRP   A  1  1211 ? -4.165  69.971  113.119 1.00 22.35 ? 1209 TRP   A CZ2   1 
ATOM   8875  C  CZ3   . TRP   A  1  1211 ? -5.177  70.070  110.934 1.00 21.55 ? 1209 TRP   A CZ3   1 
ATOM   8876  C  CH2   . TRP   A  1  1211 ? -5.224  69.736  112.291 1.00 22.73 ? 1209 TRP   A CH2   1 
ATOM   8877  N  N     . LEU   A  1  1212 ? 0.574   70.347  106.990 1.00 18.09 ? 1210 LEU   A N     1 
ATOM   8878  C  CA    . LEU   A  1  1212 ? 1.499   70.554  105.892 1.00 17.64 ? 1210 LEU   A CA    1 
ATOM   8879  C  C     . LEU   A  1  1212 ? 1.044   69.851  104.628 1.00 16.31 ? 1210 LEU   A C     1 
ATOM   8880  O  O     . LEU   A  1  1212 ? 1.739   69.906  103.613 1.00 17.00 ? 1210 LEU   A O     1 
ATOM   8881  C  CB    . LEU   A  1  1212 ? 2.898   70.090  106.298 1.00 16.46 ? 1210 LEU   A CB    1 
ATOM   8882  C  CG    . LEU   A  1  1212 ? 3.567   71.087  107.237 1.00 17.82 ? 1210 LEU   A CG    1 
ATOM   8883  C  CD1   . LEU   A  1  1212 ? 4.736   70.428  107.974 1.00 18.94 ? 1210 LEU   A CD1   1 
ATOM   8884  C  CD2   . LEU   A  1  1212 ? 4.036   72.297  106.434 1.00 20.49 ? 1210 LEU   A CD2   1 
ATOM   8885  N  N     . VAL   A  1  1213 ? -0.108  69.199  104.673 1.00 17.04 ? 1211 VAL   A N     1 
ATOM   8886  C  CA    . VAL   A  1  1213 ? -0.739  68.647  103.491 1.00 17.71 ? 1211 VAL   A CA    1 
ATOM   8887  C  C     . VAL   A  1  1213 ? -2.014  69.426  103.238 1.00 16.84 ? 1211 VAL   A C     1 
ATOM   8888  O  O     . VAL   A  1  1213 ? -2.549  70.113  104.116 1.00 18.18 ? 1211 VAL   A O     1 
ATOM   8889  C  CB    . VAL   A  1  1213 ? -1.025  67.130  103.593 1.00 17.27 ? 1211 VAL   A CB    1 
ATOM   8890  C  CG1   . VAL   A  1  1213 ? 0.271   66.346  103.627 1.00 19.04 ? 1211 VAL   A CG1   1 
ATOM   8891  C  CG2   . VAL   A  1  1213 ? -1.868  66.817  104.824 1.00 17.93 ? 1211 VAL   A CG2   1 
ATOM   8892  N  N     . GLU   A  1  1214 ? -2.496  69.310  102.014 1.00 17.52 ? 1212 GLU   A N     1 
ATOM   8893  C  CA    . GLU   A  1  1214 ? -3.704  69.975  101.568 1.00 19.83 ? 1212 GLU   A CA    1 
ATOM   8894  C  C     . GLU   A  1  1214 ? -4.715  68.898  101.223 1.00 17.11 ? 1212 GLU   A C     1 
ATOM   8895  O  O     . GLU   A  1  1214 ? -4.407  67.968  100.472 1.00 16.64 ? 1212 GLU   A O     1 
ATOM   8896  C  CB    . GLU   A  1  1214 ? -3.375  70.782  100.324 1.00 25.06 ? 1212 GLU   A CB    1 
ATOM   8897  C  CG    . GLU   A  1  1214 ? -4.509  71.558  99.727  1.00 31.93 ? 1212 GLU   A CG    1 
ATOM   8898  C  CD    . GLU   A  1  1214 ? -4.000  72.464  98.636  1.00 35.56 ? 1212 GLU   A CD    1 
ATOM   8899  O  OE1   . GLU   A  1  1214 ? -3.371  73.493  98.971  1.00 35.92 ? 1212 GLU   A OE1   1 
ATOM   8900  O  OE2   . GLU   A  1  1214 ? -4.186  72.124  97.452  1.00 38.44 ? 1212 GLU   A OE2   1 
ATOM   8901  N  N     . GLU   A  1  1215 ? -5.900  69.008  101.797 1.00 17.23 ? 1213 GLU   A N     1 
ATOM   8902  C  CA    . GLU   A  1  1215 ? -6.977  68.086  101.488 1.00 15.91 ? 1213 GLU   A CA    1 
ATOM   8903  C  C     . GLU   A  1  1215 ? -7.670  68.513  100.204 1.00 15.79 ? 1213 GLU   A C     1 
ATOM   8904  O  O     . GLU   A  1  1215 ? -7.904  69.702  99.960  1.00 16.89 ? 1213 GLU   A O     1 
ATOM   8905  C  CB    . GLU   A  1  1215 ? -8.004  68.112  102.607 1.00 15.91 ? 1213 GLU   A CB    1 
ATOM   8906  C  CG    . GLU   A  1  1215 ? -7.482  67.715  103.961 1.00 16.85 ? 1213 GLU   A CG    1 
ATOM   8907  C  CD    . GLU   A  1  1215 ? -8.450  68.106  105.040 1.00 17.14 ? 1213 GLU   A CD    1 
ATOM   8908  O  OE1   . GLU   A  1  1215 ? -8.443  69.297  105.414 1.00 18.77 ? 1213 GLU   A OE1   1 
ATOM   8909  O  OE2   . GLU   A  1  1215 ? -9.222  67.232  105.474 1.00 18.26 ? 1213 GLU   A OE2   1 
ATOM   8910  N  N     . VAL   A  1  1216 ? -7.975  67.540  99.371  1.00 15.58 ? 1214 VAL   A N     1 
ATOM   8911  C  CA    . VAL   A  1  1216 ? -8.740  67.788  98.161  1.00 16.12 ? 1214 VAL   A CA    1 
ATOM   8912  C  C     . VAL   A  1  1216 ? -9.884  66.796  98.117  1.00 16.56 ? 1214 VAL   A C     1 
ATOM   8913  O  O     . VAL   A  1  1216 ? -9.684  65.592  98.297  1.00 17.40 ? 1214 VAL   A O     1 
ATOM   8914  C  CB    . VAL   A  1  1216 ? -7.873  67.672  96.900  1.00 17.30 ? 1214 VAL   A CB    1 
ATOM   8915  C  CG1   . VAL   A  1  1216 ? -8.749  67.853  95.675  1.00 17.73 ? 1214 VAL   A CG1   1 
ATOM   8916  C  CG2   . VAL   A  1  1216 ? -6.778  68.726  96.918  1.00 19.69 ? 1214 VAL   A CG2   1 
ATOM   8917  N  N     . SER   A  1  1217 ? -11.083 67.303  97.930  1.00 16.05 ? 1215 SER   A N     1 
ATOM   8918  C  CA    . SER   A  1  1217 ? -12.261 66.477  97.768  1.00 15.52 ? 1215 SER   A CA    1 
ATOM   8919  C  C     . SER   A  1  1217 ? -12.683 66.577  96.317  1.00 15.34 ? 1215 SER   A C     1 
ATOM   8920  O  O     . SER   A  1  1217 ? -12.649 67.661  95.736  1.00 16.09 ? 1215 SER   A O     1 
ATOM   8921  C  CB    . SER   A  1  1217 ? -13.380 67.019  98.640  1.00 16.33 ? 1215 SER   A CB    1 
ATOM   8922  O  OG    . SER   A  1  1217 ? -14.649 66.608  98.173  1.00 19.00 ? 1215 SER   A OG    1 
ATOM   8923  N  N     . ALA   A  1  1218 ? -13.026 65.445  95.724  1.00 15.13 ? 1216 ALA   A N     1 
ATOM   8924  C  CA    . ALA   A  1  1218 ? -13.522 65.424  94.353  1.00 16.11 ? 1216 ALA   A CA    1 
ATOM   8925  C  C     . ALA   A  1  1218 ? -14.784 64.592  94.320  1.00 17.28 ? 1216 ALA   A C     1 
ATOM   8926  O  O     . ALA   A  1  1218 ? -14.797 63.460  94.804  1.00 17.93 ? 1216 ALA   A O     1 
ATOM   8927  C  CB    . ALA   A  1  1218 ? -12.502 64.831  93.384  1.00 16.97 ? 1216 ALA   A CB    1 
ATOM   8928  N  N     . SER   A  1  1219 ? -15.840 65.154  93.753  1.00 15.76 ? 1217 SER   A N     1 
ATOM   8929  C  CA    . SER   A  1  1219 ? -17.119 64.477  93.648  1.00 16.94 ? 1217 SER   A CA    1 
ATOM   8930  C  C     . SER   A  1  1219 ? -17.431 64.288  92.181  1.00 14.09 ? 1217 SER   A C     1 
ATOM   8931  O  O     . SER   A  1  1219 ? -17.568 65.268  91.443  1.00 16.21 ? 1217 SER   A O     1 
ATOM   8932  C  CB    . SER   A  1  1219 ? -18.221 65.290  94.317  1.00 17.93 ? 1217 SER   A CB    1 
ATOM   8933  O  OG    . SER   A  1  1219 ? -19.455 64.610  94.177  1.00 17.65 ? 1217 SER   A OG    1 
ATOM   8934  N  N     . ILE   A  1  1220 ? -17.541 63.038  91.767  1.00 15.76 ? 1218 ILE   A N     1 
ATOM   8935  C  CA    . ILE   A  1  1220 ? -17.738 62.697  90.367  1.00 16.61 ? 1218 ILE   A CA    1 
ATOM   8936  C  C     . ILE   A  1  1220 ? -19.131 62.113  90.211  1.00 14.87 ? 1218 ILE   A C     1 
ATOM   8937  O  O     . ILE   A  1  1220 ? -19.456 61.097  90.827  1.00 17.19 ? 1218 ILE   A O     1 
ATOM   8938  C  CB    . ILE   A  1  1220 ? -16.679 61.703  89.882  1.00 19.12 ? 1218 ILE   A CB    1 
ATOM   8939  C  CG1   . ILE   A  1  1220 ? -15.284 62.278  90.114  1.00 21.32 ? 1218 ILE   A CG1   1 
ATOM   8940  C  CG2   . ILE   A  1  1220 ? -16.904 61.410  88.413  1.00 19.95 ? 1218 ILE   A CG2   1 
ATOM   8941  C  CD1   . ILE   A  1  1220 ? -14.183 61.234  90.095  1.00 32.18 ? 1218 ILE   A CD1   1 
ATOM   8942  N  N     . ASN   A  1  1221 ? -19.935 62.733  89.360  1.00 15.72 ? 1219 ASN   A N     1 
ATOM   8943  C  CA    . ASN   A  1  1221 ? -21.260 62.204  89.047  1.00 15.95 ? 1219 ASN   A CA    1 
ATOM   8944  C  C     . ASN   A  1  1221 ? -21.082 61.085  88.027  1.00 15.96 ? 1219 ASN   A C     1 
ATOM   8945  O  O     . ASN   A  1  1221 ? -20.859 61.341  86.843  1.00 19.42 ? 1219 ASN   A O     1 
ATOM   8946  C  CB    . ASN   A  1  1221 ? -22.130 63.319  88.491  1.00 18.57 ? 1219 ASN   A CB    1 
ATOM   8947  C  CG    . ASN   A  1  1221 ? -23.450 62.813  87.978  1.00 17.25 ? 1219 ASN   A CG    1 
ATOM   8948  O  OD1   . ASN   A  1  1221 ? -23.834 61.664  88.225  1.00 16.38 ? 1219 ASN   A OD1   1 
ATOM   8949  N  ND2   . ASN   A  1  1221 ? -24.147 63.665  87.238  1.00 19.26 ? 1219 ASN   A ND2   1 
ATOM   8950  N  N     . THR   A  1  1222 ? -21.194 59.843  88.476  1.00 15.63 ? 1220 THR   A N     1 
ATOM   8951  C  CA    . THR   A  1  1222 ? -20.984 58.692  87.609  1.00 18.73 ? 1220 THR   A CA    1 
ATOM   8952  C  C     . THR   A  1  1222 ? -22.263 58.241  86.932  1.00 21.97 ? 1220 THR   A C     1 
ATOM   8953  O  O     . THR   A  1  1222 ? -22.254 57.228  86.226  1.00 25.98 ? 1220 THR   A O     1 
ATOM   8954  C  CB    . THR   A  1  1222 ? -20.369 57.538  88.396  1.00 20.65 ? 1220 THR   A CB    1 
ATOM   8955  O  OG1   . THR   A  1  1222 ? -21.257 57.149  89.449  1.00 20.10 ? 1220 THR   A OG1   1 
ATOM   8956  C  CG2   . THR   A  1  1222 ? -19.033 57.966  88.983  1.00 20.53 ? 1220 THR   A CG2   1 
ATOM   8957  N  N     . ALA   A  1  1223 ? -23.356 58.960  87.139  1.00 19.97 ? 1221 ALA   A N     1 
ATOM   8958  C  CA    . ALA   A  1  1223 ? -24.592 58.735  86.414  1.00 23.57 ? 1221 ALA   A CA    1 
ATOM   8959  C  C     . ALA   A  1  1223 ? -24.750 59.693  85.243  1.00 26.77 ? 1221 ALA   A C     1 
ATOM   8960  O  O     . ALA   A  1  1223 ? -25.765 59.629  84.543  1.00 31.22 ? 1221 ALA   A O     1 
ATOM   8961  C  CB    . ALA   A  1  1223 ? -25.781 58.893  87.363  1.00 21.64 ? 1221 ALA   A CB    1 
ATOM   8962  N  N     . ALA   A  1  1224 ? -23.772 60.579  85.016  1.00 27.22 ? 1222 ALA   A N     1 
ATOM   8963  C  CA    . ALA   A  1  1224 ? -23.958 61.667  84.059  1.00 30.63 ? 1222 ALA   A CA    1 
ATOM   8964  C  C     . ALA   A  1  1224 ? -24.179 61.151  82.643  1.00 33.03 ? 1222 ALA   A C     1 
ATOM   8965  O  O     . ALA   A  1  1224 ? -24.869 61.802  81.851  1.00 35.64 ? 1222 ALA   A O     1 
ATOM   8966  C  CB    . ALA   A  1  1224 ? -22.773 62.635  84.107  1.00 28.53 ? 1222 ALA   A CB    1 
ATOM   8967  N  N     . ALA   A  1  1225 ? -23.618 59.985  82.306  1.00 30.43 ? 1223 ALA   A N     1 
ATOM   8968  C  CA    . ALA   A  1  1225 ? -23.832 59.424  80.976  1.00 32.50 ? 1223 ALA   A CA    1 
ATOM   8969  C  C     . ALA   A  1  1225 ? -25.276 59.006  80.741  1.00 37.14 ? 1223 ALA   A C     1 
ATOM   8970  O  O     . ALA   A  1  1225 ? -25.636 58.693  79.600  1.00 38.04 ? 1223 ALA   A O     1 
ATOM   8971  C  CB    . ALA   A  1  1225 ? -22.884 58.247  80.727  1.00 34.54 ? 1223 ALA   A CB    1 
ATOM   8972  N  N     . GLY   A  1  1226 ? -26.108 59.001  81.780  1.00 33.48 ? 1224 GLY   A N     1 
ATOM   8973  C  CA    . GLY   A  1  1226 ? -27.515 58.653  81.653  1.00 33.04 ? 1224 GLY   A CA    1 
ATOM   8974  C  C     . GLY   A  1  1226 ? -27.917 57.404  82.406  1.00 37.56 ? 1224 GLY   A C     1 
ATOM   8975  O  O     . GLY   A  1  1226 ? -29.098 57.031  82.369  1.00 35.20 ? 1224 GLY   A O     1 
ATOM   8976  N  N     . GLY   A  1  1227 ? -26.992 56.735  83.082  1.00 29.89 ? 1225 GLY   A N     1 
ATOM   8977  C  CA    . GLY   A  1  1227 ? -27.329 55.549  83.846  1.00 34.91 ? 1225 GLY   A CA    1 
ATOM   8978  C  C     . GLY   A  1  1227 ? -26.208 55.226  84.805  1.00 33.15 ? 1225 GLY   A C     1 
ATOM   8979  O  O     . GLY   A  1  1227 ? -25.113 55.794  84.733  1.00 32.06 ? 1225 GLY   A O     1 
ATOM   8980  N  N     . ASN   A  1  1228 ? -26.499 54.290  85.703  1.00 27.92 ? 1226 ASN   A N     1 
ATOM   8981  C  CA    . ASN   A  1  1228 ? -25.578 53.868  86.752  1.00 31.46 ? 1226 ASN   A CA    1 
ATOM   8982  C  C     . ASN   A  1  1228 ? -25.091 52.457  86.425  1.00 35.17 ? 1226 ASN   A C     1 
ATOM   8983  O  O     . ASN   A  1  1228 ? -25.864 51.493  86.492  1.00 33.15 ? 1226 ASN   A O     1 
ATOM   8984  C  CB    . ASN   A  1  1228 ? -26.292 53.912  88.102  1.00 31.83 ? 1226 ASN   A CB    1 
ATOM   8985  C  CG    . ASN   A  1  1228 ? -25.361 53.661  89.276  1.00 35.31 ? 1226 ASN   A CG    1 
ATOM   8986  O  OD1   . ASN   A  1  1228 ? -24.410 52.878  89.189  1.00 34.62 ? 1226 ASN   A OD1   1 
ATOM   8987  N  ND2   . ASN   A  1  1228 ? -25.645 54.317  90.394  1.00 31.63 ? 1226 ASN   A ND2   1 
ATOM   8988  N  N     . ALA   A  1  1229 ? -23.802 52.338  86.088  1.00 33.60 ? 1227 ALA   A N     1 
ATOM   8989  C  CA    . ALA   A  1  1229 ? -23.251 51.039  85.712  1.00 34.21 ? 1227 ALA   A CA    1 
ATOM   8990  C  C     . ALA   A  1  1229 ? -23.306 50.049  86.870  1.00 34.02 ? 1227 ALA   A C     1 
ATOM   8991  O  O     . ALA   A  1  1229 ? -23.666 48.881  86.680  1.00 35.77 ? 1227 ALA   A O     1 
ATOM   8992  C  CB    . ALA   A  1  1229 ? -21.812 51.206  85.221  1.00 31.37 ? 1227 ALA   A CB    1 
ATOM   8993  N  N     . SER   A  1  1230 ? -22.943 50.494  88.076  1.00 34.14 ? 1228 SER   A N     1 
ATOM   8994  C  CA    . SER   A  1  1230 ? -22.925 49.583  89.217  1.00 35.96 ? 1228 SER   A CA    1 
ATOM   8995  C  C     . SER   A  1  1230 ? -24.316 49.038  89.516  1.00 41.96 ? 1228 SER   A C     1 
ATOM   8996  O  O     . SER   A  1  1230 ? -24.473 47.848  89.820  1.00 42.12 ? 1228 SER   A O     1 
ATOM   8997  C  CB    . SER   A  1  1230 ? -22.338 50.284  90.441  1.00 40.89 ? 1228 SER   A CB    1 
ATOM   8998  O  OG    . SER   A  1  1230 ? -20.962 50.563  90.249  1.00 48.97 ? 1228 SER   A OG    1 
ATOM   8999  N  N     . LEU   A  1  1231 ? -25.341 49.887  89.420  1.00 36.49 ? 1229 LEU   A N     1 
ATOM   9000  C  CA    . LEU   A  1  1231 ? -26.700 49.434  89.694  1.00 39.26 ? 1229 LEU   A CA    1 
ATOM   9001  C  C     . LEU   A  1  1231 ? -27.282 48.579  88.574  1.00 40.36 ? 1229 LEU   A C     1 
ATOM   9002  O  O     . LEU   A  1  1231 ? -28.338 47.967  88.775  1.00 39.76 ? 1229 LEU   A O     1 
ATOM   9003  C  CB    . LEU   A  1  1231 ? -27.614 50.617  90.015  1.00 36.79 ? 1229 LEU   A CB    1 
ATOM   9004  C  CG    . LEU   A  1  1231 ? -27.456 51.279  91.389  1.00 34.94 ? 1229 LEU   A CG    1 
ATOM   9005  C  CD1   . LEU   A  1  1231 ? -28.527 52.334  91.580  1.00 30.78 ? 1229 LEU   A CD1   1 
ATOM   9006  C  CD2   . LEU   A  1  1231 ? -27.521 50.262  92.508  1.00 41.91 ? 1229 LEU   A CD2   1 
ATOM   9007  N  N     . MET   A  1  1232 ? -26.628 48.512  87.411  1.00 40.64 ? 1230 MET   A N     1 
ATOM   9008  C  CA    . MET   A  1  1232 ? -27.040 47.546  86.397  1.00 41.14 ? 1230 MET   A CA    1 
ATOM   9009  C  C     . MET   A  1  1232 ? -26.854 46.113  86.876  1.00 40.41 ? 1230 MET   A C     1 
ATOM   9010  O  O     . MET   A  1  1232 ? -27.509 45.203  86.354  1.00 42.77 ? 1230 MET   A O     1 
ATOM   9011  C  CB    . MET   A  1  1232 ? -26.251 47.753  85.103  1.00 40.72 ? 1230 MET   A CB    1 
ATOM   9012  C  CG    . MET   A  1  1232 ? -26.584 49.023  84.342  1.00 36.93 ? 1230 MET   A CG    1 
ATOM   9013  S  SD    . MET   A  1  1232 ? -25.460 49.207  82.932  1.00 46.27 ? 1230 MET   A SD    1 
ATOM   9014  C  CE    . MET   A  1  1232 ? -25.832 47.715  81.997  1.00 43.48 ? 1230 MET   A CE    1 
ATOM   9015  N  N     . ALA   A  1  1233 ? -25.969 45.893  87.849  1.00 46.42 ? 1231 ALA   A N     1 
ATOM   9016  C  CA    . ALA   A  1  1233 ? -25.774 44.585  88.459  1.00 49.35 ? 1231 ALA   A CA    1 
ATOM   9017  C  C     . ALA   A  1  1233 ? -26.702 44.337  89.640  1.00 53.00 ? 1231 ALA   A C     1 
ATOM   9018  O  O     . ALA   A  1  1233 ? -26.704 43.227  90.184  1.00 55.82 ? 1231 ALA   A O     1 
ATOM   9019  C  CB    . ALA   A  1  1233 ? -24.320 44.427  88.919  1.00 48.96 ? 1231 ALA   A CB    1 
ATOM   9020  N  N     . ILE   A  1  1234 ? -27.486 45.331  90.046  1.00 51.03 ? 1232 ILE   A N     1 
ATOM   9021  C  CA    . ILE   A  1  1234 ? -28.370 45.215  91.199  1.00 50.66 ? 1232 ILE   A CA    1 
ATOM   9022  C  C     . ILE   A  1  1234 ? -29.786 44.958  90.699  1.00 48.18 ? 1232 ILE   A C     1 
ATOM   9023  O  O     . ILE   A  1  1234 ? -30.419 45.832  90.094  1.00 44.37 ? 1232 ILE   A O     1 
ATOM   9024  C  CB    . ILE   A  1  1234 ? -28.292 46.447  92.111  1.00 45.83 ? 1232 ILE   A CB    1 
ATOM   9025  C  CG1   . ILE   A  1  1234 ? -26.878 46.574  92.687  1.00 46.83 ? 1232 ILE   A CG1   1 
ATOM   9026  C  CG2   . ILE   A  1  1234 ? -29.333 46.349  93.213  1.00 39.48 ? 1232 ILE   A CG2   1 
ATOM   9027  C  CD1   . ILE   A  1  1234 ? -26.809 47.202  94.065  1.00 41.87 ? 1232 ILE   A CD1   1 
ATOM   9028  N  N     . GLY   A  1  1235 ? -30.275 43.750  90.947  1.00 45.58 ? 1233 GLY   A N     1 
ATOM   9029  C  CA    . GLY   A  1  1235 ? -31.636 43.384  90.618  1.00 40.46 ? 1233 GLY   A CA    1 
ATOM   9030  C  C     . GLY   A  1  1235 ? -32.213 42.562  91.749  1.00 38.00 ? 1233 GLY   A C     1 
ATOM   9031  O  O     . GLY   A  1  1235 ? -31.508 41.782  92.390  1.00 42.47 ? 1233 GLY   A O     1 
ATOM   9032  O  OXT   . GLY   A  1  1235 ? -33.390 42.654  92.060  1.00 26.35 ? 1233 GLY   A OXT   1 
ATOM   9033  N  N     . ALA   B  1  16   ? 30.127  5.159   80.733  1.00 43.10 ? 14   ALA   B N     1 
ATOM   9034  C  CA    . ALA   B  1  16   ? 29.132  6.199   80.988  1.00 43.59 ? 14   ALA   B CA    1 
ATOM   9035  C  C     . ALA   B  1  16   ? 27.724  5.619   80.963  1.00 40.95 ? 14   ALA   B C     1 
ATOM   9036  O  O     . ALA   B  1  16   ? 27.397  4.824   80.084  1.00 46.63 ? 14   ALA   B O     1 
ATOM   9037  C  CB    . ALA   B  1  16   ? 29.257  7.319   79.961  1.00 38.34 ? 14   ALA   B CB    1 
ATOM   9038  N  N     . PRO   B  1  17   ? 26.890  6.022   81.920  1.00 39.03 ? 15   PRO   B N     1 
ATOM   9039  C  CA    . PRO   B  1  17   ? 25.507  5.532   81.939  1.00 37.56 ? 15   PRO   B CA    1 
ATOM   9040  C  C     . PRO   B  1  17   ? 24.750  5.995   80.703  1.00 33.64 ? 15   PRO   B C     1 
ATOM   9041  O  O     . PRO   B  1  17   ? 24.942  7.112   80.217  1.00 33.85 ? 15   PRO   B O     1 
ATOM   9042  C  CB    . PRO   B  1  17   ? 24.929  6.153   83.216  1.00 38.08 ? 15   PRO   B CB    1 
ATOM   9043  C  CG    . PRO   B  1  17   ? 25.776  7.357   83.464  1.00 42.09 ? 15   PRO   B CG    1 
ATOM   9044  C  CD    . PRO   B  1  17   ? 27.155  6.979   83.007  1.00 38.20 ? 15   PRO   B CD    1 
ATOM   9045  N  N     . ALA   B  1  18   ? 23.903  5.111   80.185  1.00 34.40 ? 16   ALA   B N     1 
ATOM   9046  C  CA    . ALA   B  1  18   ? 23.110  5.448   79.015  1.00 28.47 ? 16   ALA   B CA    1 
ATOM   9047  C  C     . ALA   B  1  18   ? 22.184  6.617   79.342  1.00 25.76 ? 16   ALA   B C     1 
ATOM   9048  O  O     . ALA   B  1  18   ? 21.600  6.662   80.428  1.00 26.12 ? 16   ALA   B O     1 
ATOM   9049  C  CB    . ALA   B  1  18   ? 22.272  4.248   78.580  1.00 31.88 ? 16   ALA   B CB    1 
ATOM   9050  N  N     . PRO   B  1  19   ? 22.029  7.574   78.433  1.00 25.60 ? 17   PRO   B N     1 
ATOM   9051  C  CA    . PRO   B  1  19   ? 21.192  8.744   78.727  1.00 23.97 ? 17   PRO   B CA    1 
ATOM   9052  C  C     . PRO   B  1  19   ? 19.766  8.342   79.072  1.00 21.58 ? 17   PRO   B C     1 
ATOM   9053  O  O     . PRO   B  1  19   ? 19.142  7.537   78.378  1.00 23.72 ? 17   PRO   B O     1 
ATOM   9054  C  CB    . PRO   B  1  19   ? 21.250  9.550   77.423  1.00 23.35 ? 17   PRO   B CB    1 
ATOM   9055  C  CG    . PRO   B  1  19   ? 22.559  9.164   76.820  1.00 25.99 ? 17   PRO   B CG    1 
ATOM   9056  C  CD    . PRO   B  1  19   ? 22.734  7.704   77.147  1.00 25.54 ? 17   PRO   B CD    1 
ATOM   9057  N  N     . PHE   B  1  20   ? 19.264  8.893   80.175  1.00 22.94 ? 18   PHE   B N     1 
ATOM   9058  C  CA    . PHE   B  1  20   ? 17.886  8.725   80.627  1.00 21.59 ? 18   PHE   B CA    1 
ATOM   9059  C  C     . PHE   B  1  20   ? 17.566  7.304   81.063  1.00 26.03 ? 18   PHE   B C     1 
ATOM   9060  O  O     . PHE   B  1  20   ? 16.393  6.977   81.250  1.00 25.72 ? 18   PHE   B O     1 
ATOM   9061  C  CB    . PHE   B  1  20   ? 16.868  9.216   79.592  1.00 21.00 ? 18   PHE   B CB    1 
ATOM   9062  C  CG    . PHE   B  1  20   ? 17.062  10.647  79.197  1.00 19.01 ? 18   PHE   B CG    1 
ATOM   9063  C  CD1   . PHE   B  1  20   ? 16.717  11.671  80.059  1.00 19.22 ? 18   PHE   B CD1   1 
ATOM   9064  C  CD2   . PHE   B  1  20   ? 17.588  10.970  77.956  1.00 19.88 ? 18   PHE   B CD2   1 
ATOM   9065  C  CE1   . PHE   B  1  20   ? 16.891  12.997  79.701  1.00 19.67 ? 18   PHE   B CE1   1 
ATOM   9066  C  CE2   . PHE   B  1  20   ? 17.758  12.290  77.593  1.00 19.82 ? 18   PHE   B CE2   1 
ATOM   9067  C  CZ    . PHE   B  1  20   ? 17.414  13.302  78.458  1.00 20.27 ? 18   PHE   B CZ    1 
ATOM   9068  N  N     . ALA   B  1  21   ? 18.578  6.452   81.233  1.00 28.24 ? 19   ALA   B N     1 
ATOM   9069  C  CA    . ALA   B  1  21   ? 18.333  5.067   81.620  1.00 29.10 ? 19   ALA   B CA    1 
ATOM   9070  C  C     . ALA   B  1  21   ? 17.750  4.954   83.021  1.00 29.32 ? 19   ALA   B C     1 
ATOM   9071  O  O     . ALA   B  1  21   ? 17.119  3.941   83.338  1.00 33.75 ? 19   ALA   B O     1 
ATOM   9072  C  CB    . ALA   B  1  21   ? 19.627  4.259   81.522  1.00 30.95 ? 19   ALA   B CB    1 
ATOM   9073  N  N     . ASP   B  1  22   ? 17.935  5.968   83.859  1.00 24.65 ? 20   ASP   B N     1 
ATOM   9074  C  CA    . ASP   B  1  22   ? 17.390  5.983   85.209  1.00 27.27 ? 20   ASP   B CA    1 
ATOM   9075  C  C     . ASP   B  1  22   ? 16.671  7.293   85.463  1.00 22.72 ? 20   ASP   B C     1 
ATOM   9076  O  O     . ASP   B  1  22   ? 16.781  7.886   86.541  1.00 26.43 ? 20   ASP   B O     1 
ATOM   9077  C  CB    . ASP   B  1  22   ? 18.483  5.744   86.248  1.00 30.52 ? 20   ASP   B CB    1 
ATOM   9078  N  N     . PHE   B  1  23   ? 15.920  7.768   84.465  1.00 19.46 ? 21   PHE   B N     1 
ATOM   9079  C  CA    . PHE   B  1  23   ? 15.363  9.113   84.549  1.00 19.45 ? 21   PHE   B CA    1 
ATOM   9080  C  C     . PHE   B  1  23   ? 14.403  9.249   85.724  1.00 19.12 ? 21   PHE   B C     1 
ATOM   9081  O  O     . PHE   B  1  23   ? 14.562  10.136  86.568  1.00 19.26 ? 21   PHE   B O     1 
ATOM   9082  C  CB    . PHE   B  1  23   ? 14.645  9.482   83.254  1.00 17.93 ? 21   PHE   B CB    1 
ATOM   9083  C  CG    . PHE   B  1  23   ? 13.968  10.806  83.330  1.00 19.56 ? 21   PHE   B CG    1 
ATOM   9084  C  CD1   . PHE   B  1  23   ? 14.716  11.957  83.480  1.00 18.83 ? 21   PHE   B CD1   1 
ATOM   9085  C  CD2   . PHE   B  1  23   ? 12.583  10.904  83.283  1.00 18.58 ? 21   PHE   B CD2   1 
ATOM   9086  C  CE1   . PHE   B  1  23   ? 14.094  13.196  83.581  1.00 19.14 ? 21   PHE   B CE1   1 
ATOM   9087  C  CE2   . PHE   B  1  23   ? 11.970  12.134  83.387  1.00 20.07 ? 21   PHE   B CE2   1 
ATOM   9088  C  CZ    . PHE   B  1  23   ? 12.720  13.273  83.530  1.00 19.60 ? 21   PHE   B CZ    1 
ATOM   9089  N  N     . ALA   B  1  24   ? 13.374  8.404   85.768  1.00 19.54 ? 22   ALA   B N     1 
ATOM   9090  C  CA    . ALA   B  1  24   ? 12.395  8.491   86.847  1.00 19.00 ? 22   ALA   B CA    1 
ATOM   9091  C  C     . ALA   B  1  24   ? 11.673  7.167   87.055  1.00 18.57 ? 22   ALA   B C     1 
ATOM   9092  O  O     . ALA   B  1  24   ? 10.445  7.107   86.918  1.00 20.28 ? 22   ALA   B O     1 
ATOM   9093  C  CB    . ALA   B  1  24   ? 11.376  9.589   86.544  1.00 23.20 ? 22   ALA   B CB    1 
ATOM   9094  N  N     . PRO   B  1  25   ? 12.376  6.095   87.400  1.00 21.01 ? 23   PRO   B N     1 
ATOM   9095  C  CA    . PRO   B  1  25   ? 11.709  4.810   87.586  1.00 24.38 ? 23   PRO   B CA    1 
ATOM   9096  C  C     . PRO   B  1  25   ? 10.734  4.895   88.744  1.00 21.92 ? 23   PRO   B C     1 
ATOM   9097  O  O     . PRO   B  1  25   ? 11.040  5.514   89.773  1.00 21.78 ? 23   PRO   B O     1 
ATOM   9098  C  CB    . PRO   B  1  25   ? 12.868  3.853   87.902  1.00 27.19 ? 23   PRO   B CB    1 
ATOM   9099  C  CG    . PRO   B  1  25   ? 13.921  4.713   88.462  1.00 24.85 ? 23   PRO   B CG    1 
ATOM   9100  C  CD    . PRO   B  1  25   ? 13.804  6.035   87.754  1.00 20.78 ? 23   PRO   B CD    1 
ATOM   9101  N  N     . PRO   B  1  26   ? 9.536   4.335   88.597  1.00 22.72 ? 24   PRO   B N     1 
ATOM   9102  C  CA    . PRO   B  1  26   ? 8.564   4.394   89.690  1.00 23.77 ? 24   PRO   B CA    1 
ATOM   9103  C  C     . PRO   B  1  26   ? 9.041   3.572   90.874  1.00 24.25 ? 24   PRO   B C     1 
ATOM   9104  O  O     . PRO   B  1  26   ? 9.863   2.663   90.746  1.00 24.32 ? 24   PRO   B O     1 
ATOM   9105  C  CB    . PRO   B  1  26   ? 7.300   3.785   89.077  1.00 24.89 ? 24   PRO   B CB    1 
ATOM   9106  C  CG    . PRO   B  1  26   ? 7.792   2.904   87.986  1.00 26.48 ? 24   PRO   B CG    1 
ATOM   9107  C  CD    . PRO   B  1  26   ? 9.025   3.582   87.438  1.00 25.75 ? 24   PRO   B CD    1 
ATOM   9108  N  N     . VAL   B  1  27   ? 8.503   3.916   92.046  1.00 23.51 ? 25   VAL   B N     1 
ATOM   9109  C  CA    . VAL   B  1  27   ? 8.836   3.182   93.263  1.00 23.59 ? 25   VAL   B CA    1 
ATOM   9110  C  C     . VAL   B  1  27   ? 8.482   1.711   93.113  1.00 23.52 ? 25   VAL   B C     1 
ATOM   9111  O  O     . VAL   B  1  27   ? 9.221   0.830   93.567  1.00 27.47 ? 25   VAL   B O     1 
ATOM   9112  C  CB    . VAL   B  1  27   ? 8.141   3.819   94.478  1.00 24.34 ? 25   VAL   B CB    1 
ATOM   9113  C  CG1   . VAL   B  1  27   ? 8.279   2.909   95.697  1.00 25.98 ? 25   VAL   B CG1   1 
ATOM   9114  C  CG2   . VAL   B  1  27   ? 8.718   5.195   94.752  1.00 23.78 ? 25   VAL   B CG2   1 
ATOM   9115  N  N     . ARG   B  1  28   ? 7.363   1.419   92.462  1.00 23.52 ? 26   ARG   B N     1 
ATOM   9116  C  CA    . ARG   B  1  28   ? 6.937   0.043   92.267  1.00 22.52 ? 26   ARG   B CA    1 
ATOM   9117  C  C     . ARG   B  1  28   ? 6.166   -0.034  90.960  1.00 27.87 ? 26   ARG   B C     1 
ATOM   9118  O  O     . ARG   B  1  28   ? 5.699   0.991   90.452  1.00 24.22 ? 26   ARG   B O     1 
ATOM   9119  C  CB    . ARG   B  1  28   ? 6.053   -0.426  93.433  1.00 28.08 ? 26   ARG   B CB    1 
ATOM   9120  C  CG    . ARG   B  1  28   ? 4.696   0.265   93.485  1.00 28.38 ? 26   ARG   B CG    1 
ATOM   9121  C  CD    . ARG   B  1  28   ? 3.920   -0.083  94.750  1.00 28.90 ? 26   ARG   B CD    1 
ATOM   9122  N  NE    . ARG   B  1  28   ? 4.533   0.503   95.937  1.00 29.70 ? 26   ARG   B NE    1 
ATOM   9123  C  CZ    . ARG   B  1  28   ? 5.257   -0.173  96.818  1.00 33.62 ? 26   ARG   B CZ    1 
ATOM   9124  N  NH1   . ARG   B  1  28   ? 5.472   -1.474  96.686  1.00 32.09 ? 26   ARG   B NH1   1 
ATOM   9125  N  NH2   . ARG   B  1  28   ? 5.773   0.470   97.861  1.00 32.56 ? 26   ARG   B NH2   1 
ATOM   9126  N  N     . PRO   B  1  29   ? 6.041   -1.224  90.374  1.00 25.44 ? 27   PRO   B N     1 
ATOM   9127  C  CA    . PRO   B  1  29   ? 5.149   -1.370  89.220  1.00 25.98 ? 27   PRO   B CA    1 
ATOM   9128  C  C     . PRO   B  1  29   ? 3.740   -0.945  89.595  1.00 27.05 ? 27   PRO   B C     1 
ATOM   9129  O  O     . PRO   B  1  29   ? 3.240   -1.261  90.676  1.00 26.43 ? 27   PRO   B O     1 
ATOM   9130  C  CB    . PRO   B  1  29   ? 5.218   -2.868  88.904  1.00 28.27 ? 27   PRO   B CB    1 
ATOM   9131  C  CG    . PRO   B  1  29   ? 6.550   -3.292  89.430  1.00 33.45 ? 27   PRO   B CG    1 
ATOM   9132  C  CD    . PRO   B  1  29   ? 6.756   -2.476  90.679  1.00 29.70 ? 27   PRO   B CD    1 
ATOM   9133  N  N     . GLN   B  1  30   ? 3.108   -0.199  88.696  1.00 26.16 ? 28   GLN   B N     1 
ATOM   9134  C  CA    . GLN   B  1  30   ? 1.802   0.380   88.973  1.00 27.33 ? 28   GLN   B CA    1 
ATOM   9135  C  C     . GLN   B  1  30   ? 0.712   -0.655  88.728  1.00 26.60 ? 28   GLN   B C     1 
ATOM   9136  O  O     . GLN   B  1  30   ? 0.542   -1.141  87.602  1.00 27.38 ? 28   GLN   B O     1 
ATOM   9137  C  CB    . GLN   B  1  30   ? 1.588   1.607   88.090  1.00 24.97 ? 28   GLN   B CB    1 
ATOM   9138  C  CG    . GLN   B  1  30   ? 2.688   2.644   88.242  1.00 24.82 ? 28   GLN   B CG    1 
ATOM   9139  C  CD    . GLN   B  1  30   ? 2.655   3.316   89.601  1.00 25.22 ? 28   GLN   B CD    1 
ATOM   9140  O  OE1   . GLN   B  1  30   ? 1.798   4.157   89.857  1.00 24.98 ? 28   GLN   B OE1   1 
ATOM   9141  N  NE2   . GLN   B  1  30   ? 3.578   2.939   90.487  1.00 23.21 ? 28   GLN   B NE2   1 
ATOM   9142  N  N     . SER   B  1  31   ? -0.026  -0.982  89.784  1.00 25.52 ? 29   SER   B N     1 
ATOM   9143  C  CA    . SER   B  1  31   ? -1.116  -1.935  89.700  1.00 26.43 ? 29   SER   B CA    1 
ATOM   9144  C  C     . SER   B  1  31   ? -2.291  -1.324  88.940  1.00 26.50 ? 29   SER   B C     1 
ATOM   9145  O  O     . SER   B  1  31   ? -2.331  -0.123  88.657  1.00 25.71 ? 29   SER   B O     1 
ATOM   9146  C  CB    . SER   B  1  31   ? -1.597  -2.293  91.099  1.00 27.40 ? 29   SER   B CB    1 
ATOM   9147  O  OG    . SER   B  1  31   ? -2.226  -1.172  91.692  1.00 25.67 ? 29   SER   B OG    1 
ATOM   9148  N  N     . THR   B  1  32   ? -3.262  -2.177  88.607  1.00 27.93 ? 30   THR   B N     1 
ATOM   9149  C  CA    . THR   B  1  32   ? -4.479  -1.695  87.965  1.00 26.89 ? 30   THR   B CA    1 
ATOM   9150  C  C     . THR   B  1  32   ? -5.126  -0.583  88.785  1.00 25.22 ? 30   THR   B C     1 
ATOM   9151  O  O     . THR   B  1  32   ? -5.510  0.460   88.246  1.00 26.93 ? 30   THR   B O     1 
ATOM   9152  C  CB    . THR   B  1  32   ? -5.441  -2.864  87.750  1.00 29.79 ? 30   THR   B CB    1 
ATOM   9153  O  OG1   . THR   B  1  32   ? -4.817  -3.824  86.891  1.00 32.50 ? 30   THR   B OG1   1 
ATOM   9154  C  CG2   . THR   B  1  32   ? -6.749  -2.391  87.114  1.00 34.56 ? 30   THR   B CG2   1 
ATOM   9155  N  N     . LEU   B  1  33   ? -5.222  -0.774  90.102  1.00 26.20 ? 31   LEU   B N     1 
ATOM   9156  C  CA    . LEU   B  1  33   ? -5.846  0.241   90.944  1.00 26.48 ? 31   LEU   B CA    1 
ATOM   9157  C  C     . LEU   B  1  33   ? -5.025  1.521   90.981  1.00 23.33 ? 31   LEU   B C     1 
ATOM   9158  O  O     . LEU   B  1  33   ? -5.585  2.621   90.947  1.00 23.33 ? 31   LEU   B O     1 
ATOM   9159  C  CB    . LEU   B  1  33   ? -6.074  -0.309  92.351  1.00 24.87 ? 31   LEU   B CB    1 
ATOM   9160  C  CG    . LEU   B  1  33   ? -7.155  -1.387  92.356  1.00 26.90 ? 31   LEU   B CG    1 
ATOM   9161  C  CD1   . LEU   B  1  33   ? -7.202  -2.097  93.692  1.00 29.06 ? 31   LEU   B CD1   1 
ATOM   9162  C  CD2   . LEU   B  1  33   ? -8.509  -0.791  92.025  1.00 30.01 ? 31   LEU   B CD2   1 
ATOM   9163  N  N     . ARG   B  1  34   ? -3.698  1.403   91.061  1.00 21.91 ? 32   ARG   B N     1 
ATOM   9164  C  CA    . ARG   B  1  34   ? -2.867  2.599   91.037  1.00 22.45 ? 32   ARG   B CA    1 
ATOM   9165  C  C     . ARG   B  1  34   ? -2.988  3.316   89.699  1.00 22.17 ? 32   ARG   B C     1 
ATOM   9166  O  O     . ARG   B  1  34   ? -3.045  4.551   89.647  1.00 21.94 ? 32   ARG   B O     1 
ATOM   9167  C  CB    . ARG   B  1  34   ? -1.412  2.236   91.322  1.00 21.09 ? 32   ARG   B CB    1 
ATOM   9168  C  CG    . ARG   B  1  34   ? -1.116  1.841   92.768  1.00 23.60 ? 32   ARG   B CG    1 
ATOM   9169  C  CD    . ARG   B  1  34   ? -1.181  3.027   93.725  1.00 22.85 ? 32   ARG   B CD    1 
ATOM   9170  N  NE    . ARG   B  1  34   ? -0.140  4.008   93.450  1.00 22.64 ? 32   ARG   B NE    1 
ATOM   9171  C  CZ    . ARG   B  1  34   ? 1.076   3.986   93.980  1.00 23.72 ? 32   ARG   B CZ    1 
ATOM   9172  N  NH1   . ARG   B  1  34   ? 1.445   3.037   94.831  1.00 24.09 ? 32   ARG   B NH1   1 
ATOM   9173  N  NH2   . ARG   B  1  34   ? 1.946   4.932   93.640  1.00 23.76 ? 32   ARG   B NH2   1 
ATOM   9174  N  N     . ARG   B  1  35   ? -3.041  2.556   88.606  1.00 23.26 ? 33   ARG   B N     1 
ATOM   9175  C  CA    . ARG   B  1  35   ? -3.197  3.170   87.291  1.00 24.18 ? 33   ARG   B CA    1 
ATOM   9176  C  C     . ARG   B  1  35   ? -4.525  3.899   87.177  1.00 21.91 ? 33   ARG   B C     1 
ATOM   9177  O  O     . ARG   B  1  35   ? -4.612  4.944   86.526  1.00 22.31 ? 33   ARG   B O     1 
ATOM   9178  C  CB    . ARG   B  1  35   ? -3.096  2.102   86.209  1.00 25.68 ? 33   ARG   B CB    1 
ATOM   9179  C  CG    . ARG   B  1  35   ? -1.684  1.639   86.008  1.00 28.08 ? 33   ARG   B CG    1 
ATOM   9180  C  CD    . ARG   B  1  35   ? -1.578  0.536   84.971  1.00 30.84 ? 33   ARG   B CD    1 
ATOM   9181  N  NE    . ARG   B  1  35   ? -0.200  0.072   84.910  1.00 37.16 ? 33   ARG   B NE    1 
ATOM   9182  C  CZ    . ARG   B  1  35   ? 0.770   0.703   84.262  1.00 44.10 ? 33   ARG   B CZ    1 
ATOM   9183  N  NH1   . ARG   B  1  35   ? 0.528   1.787   83.539  1.00 47.17 ? 33   ARG   B NH1   1 
ATOM   9184  N  NH2   . ARG   B  1  35   ? 2.017   0.244   84.349  1.00 40.41 ? 33   ARG   B NH2   1 
ATOM   9185  N  N     . ALA   B  1  36   ? -5.571  3.361   87.800  1.00 22.03 ? 34   ALA   B N     1 
ATOM   9186  C  CA    . ALA   B  1  36   ? -6.858  4.037   87.742  1.00 26.13 ? 34   ALA   B CA    1 
ATOM   9187  C  C     . ALA   B  1  36   ? -6.807  5.367   88.475  1.00 25.37 ? 34   ALA   B C     1 
ATOM   9188  O  O     . ALA   B  1  36   ? -7.447  6.334   88.051  1.00 23.73 ? 34   ALA   B O     1 
ATOM   9189  C  CB    . ALA   B  1  36   ? -7.967  3.136   88.288  1.00 24.48 ? 34   ALA   B CB    1 
ATOM   9190  N  N     . ILE   B  1  37   ? -6.030  5.440   89.557  1.00 21.93 ? 35   ILE   B N     1 
ATOM   9191  C  CA    . ILE   B  1  37   ? -5.822  6.716   90.229  1.00 20.90 ? 35   ILE   B CA    1 
ATOM   9192  C  C     . ILE   B  1  37   ? -5.158  7.702   89.286  1.00 22.78 ? 35   ILE   B C     1 
ATOM   9193  O  O     . ILE   B  1  37   ? -5.652  8.814   89.068  1.00 20.01 ? 35   ILE   B O     1 
ATOM   9194  C  CB    . ILE   B  1  37   ? -4.991  6.511   91.503  1.00 20.37 ? 35   ILE   B CB    1 
ATOM   9195  C  CG1   . ILE   B  1  37   ? -5.779  5.699   92.526  1.00 20.03 ? 35   ILE   B CG1   1 
ATOM   9196  C  CG2   . ILE   B  1  37   ? -4.565  7.855   92.082  1.00 20.89 ? 35   ILE   B CG2   1 
ATOM   9197  C  CD1   . ILE   B  1  37   ? -4.896  5.117   93.614  1.00 22.58 ? 35   ILE   B CD1   1 
ATOM   9198  N  N     . THR   B  1  38   ? -4.010  7.314   88.725  1.00 20.16 ? 36   THR   B N     1 
ATOM   9199  C  CA    . THR   B  1  38   ? -3.259  8.222   87.870  1.00 21.57 ? 36   THR   B CA    1 
ATOM   9200  C  C     . THR   B  1  38   ? -4.095  8.680   86.686  1.00 20.90 ? 36   THR   B C     1 
ATOM   9201  O  O     . THR   B  1  38   ? -4.025  9.848   86.285  1.00 20.89 ? 36   THR   B O     1 
ATOM   9202  C  CB    . THR   B  1  38   ? -1.982  7.528   87.404  1.00 19.72 ? 36   THR   B CB    1 
ATOM   9203  O  OG1   . THR   B  1  38   ? -1.300  6.999   88.547  1.00 20.61 ? 36   THR   B OG1   1 
ATOM   9204  C  CG2   . THR   B  1  38   ? -1.071  8.496   86.666  1.00 23.22 ? 36   THR   B CG2   1 
ATOM   9205  N  N     . ALA   B  1  39   ? -4.907  7.781   86.131  1.00 20.94 ? 37   ALA   B N     1 
ATOM   9206  C  CA    . ALA   B  1  39   ? -5.709  8.134   84.964  1.00 23.16 ? 37   ALA   B CA    1 
ATOM   9207  C  C     . ALA   B  1  39   ? -6.690  9.252   85.273  1.00 24.52 ? 37   ALA   B C     1 
ATOM   9208  O  O     . ALA   B  1  39   ? -7.084  10.001  84.372  1.00 23.81 ? 37   ALA   B O     1 
ATOM   9209  C  CB    . ALA   B  1  39   ? -6.458  6.903   84.448  1.00 22.95 ? 37   ALA   B CB    1 
ATOM   9210  N  N     . ALA   B  1  40   ? -7.090  9.389   86.533  1.00 20.45 ? 38   ALA   B N     1 
ATOM   9211  C  CA    . ALA   B  1  40   ? -8.079  10.379  86.920  1.00 22.18 ? 38   ALA   B CA    1 
ATOM   9212  C  C     . ALA   B  1  40   ? -7.460  11.715  87.296  1.00 19.14 ? 38   ALA   B C     1 
ATOM   9213  O  O     . ALA   B  1  40   ? -8.201  12.664  87.558  1.00 21.44 ? 38   ALA   B O     1 
ATOM   9214  C  CB    . ALA   B  1  40   ? -8.911  9.850   88.097  1.00 22.45 ? 38   ALA   B CB    1 
ATOM   9215  N  N     . TYR   B  1  41   ? -6.128  11.801  87.325  1.00 18.96 ? 39   TYR   B N     1 
ATOM   9216  C  CA    . TYR   B  1  41   ? -5.440  12.927  87.950  1.00 20.17 ? 39   TYR   B CA    1 
ATOM   9217  C  C     . TYR   B  1  41   ? -6.028  14.268  87.509  1.00 18.62 ? 39   TYR   B C     1 
ATOM   9218  O  O     . TYR   B  1  41   ? -6.343  15.128  88.340  1.00 19.52 ? 39   TYR   B O     1 
ATOM   9219  C  CB    . TYR   B  1  41   ? -3.959  12.821  87.582  1.00 18.41 ? 39   TYR   B CB    1 
ATOM   9220  C  CG    . TYR   B  1  41   ? -2.955  13.524  88.463  1.00 18.85 ? 39   TYR   B CG    1 
ATOM   9221  C  CD1   . TYR   B  1  41   ? -3.275  14.669  89.178  1.00 18.65 ? 39   TYR   B CD1   1 
ATOM   9222  C  CD2   . TYR   B  1  41   ? -1.655  13.053  88.536  1.00 20.60 ? 39   TYR   B CD2   1 
ATOM   9223  C  CE1   . TYR   B  1  41   ? -2.325  15.313  89.959  1.00 18.67 ? 39   TYR   B CE1   1 
ATOM   9224  C  CE2   . TYR   B  1  41   ? -0.698  13.684  89.311  1.00 19.40 ? 39   TYR   B CE2   1 
ATOM   9225  C  CZ    . TYR   B  1  41   ? -1.036  14.817  90.015  1.00 17.57 ? 39   TYR   B CZ    1 
ATOM   9226  O  OH    . TYR   B  1  41   ? -0.088  15.442  90.782  1.00 18.94 ? 39   TYR   B OH    1 
ATOM   9227  N  N     . ARG   B  1  42   ? -6.180  14.467  86.204  1.00 19.59 ? 40   ARG   B N     1 
ATOM   9228  C  CA    . ARG   B  1  42   ? -6.669  15.733  85.673  1.00 19.20 ? 40   ARG   B CA    1 
ATOM   9229  C  C     . ARG   B  1  42   ? -7.864  15.511  84.759  1.00 20.38 ? 40   ARG   B C     1 
ATOM   9230  O  O     . ARG   B  1  42   ? -8.050  16.223  83.770  1.00 21.55 ? 40   ARG   B O     1 
ATOM   9231  C  CB    . ARG   B  1  42   ? -5.555  16.515  84.995  1.00 20.58 ? 40   ARG   B CB    1 
ATOM   9232  C  CG    . ARG   B  1  42   ? -4.475  16.847  86.010  1.00 21.17 ? 40   ARG   B CG    1 
ATOM   9233  C  CD    . ARG   B  1  42   ? -3.297  17.569  85.433  1.00 19.56 ? 40   ARG   B CD    1 
ATOM   9234  N  NE    . ARG   B  1  42   ? -2.205  17.480  86.389  1.00 19.19 ? 40   ARG   B NE    1 
ATOM   9235  C  CZ    . ARG   B  1  42   ? -1.987  18.346  87.370  1.00 19.70 ? 40   ARG   B CZ    1 
ATOM   9236  N  NH1   . ARG   B  1  42   ? -2.693  19.464  87.479  1.00 19.46 ? 40   ARG   B NH1   1 
ATOM   9237  N  NH2   . ARG   B  1  42   ? -1.024  18.093  88.255  1.00 18.53 ? 40   ARG   B NH2   1 
ATOM   9238  N  N     . ARG   B  1  43   ? -8.690  14.532  85.105  1.00 20.02 ? 41   ARG   B N     1 
ATOM   9239  C  CA    . ARG   B  1  43   ? -9.841  14.188  84.284  1.00 20.25 ? 41   ARG   B CA    1 
ATOM   9240  C  C     . ARG   B  1  43   ? -10.773 15.391  84.178  1.00 23.90 ? 41   ARG   B C     1 
ATOM   9241  O  O     . ARG   B  1  43   ? -10.968 16.114  85.160  1.00 21.37 ? 41   ARG   B O     1 
ATOM   9242  C  CB    . ARG   B  1  43   ? -10.579 13.018  84.937  1.00 20.49 ? 41   ARG   B CB    1 
ATOM   9243  C  CG    . ARG   B  1  43   ? -11.858 12.587  84.227  1.00 20.56 ? 41   ARG   B CG    1 
ATOM   9244  C  CD    . ARG   B  1  43   ? -12.259 11.219  84.710  1.00 25.01 ? 41   ARG   B CD    1 
ATOM   9245  N  NE    . ARG   B  1  43   ? -11.278 10.220  84.313  1.00 24.52 ? 41   ARG   B NE    1 
ATOM   9246  C  CZ    . ARG   B  1  43   ? -11.023 9.108   84.989  1.00 27.15 ? 41   ARG   B CZ    1 
ATOM   9247  N  NH1   . ARG   B  1  43   ? -11.663 8.817   86.108  1.00 23.91 ? 41   ARG   B NH1   1 
ATOM   9248  N  NH2   . ARG   B  1  43   ? -10.087 8.276   84.539  1.00 25.39 ? 41   ARG   B NH2   1 
ATOM   9249  N  N     . PRO   B  1  44   ? -11.337 15.658  83.007  1.00 22.06 ? 42   PRO   B N     1 
ATOM   9250  C  CA    . PRO   B  1  44   ? -12.256 16.790  82.881  1.00 22.16 ? 42   PRO   B CA    1 
ATOM   9251  C  C     . PRO   B  1  44   ? -13.369 16.713  83.912  1.00 22.05 ? 42   PRO   B C     1 
ATOM   9252  O  O     . PRO   B  1  44   ? -13.870 15.638  84.246  1.00 21.42 ? 42   PRO   B O     1 
ATOM   9253  C  CB    . PRO   B  1  44   ? -12.785 16.647  81.452  1.00 24.25 ? 42   PRO   B CB    1 
ATOM   9254  C  CG    . PRO   B  1  44   ? -11.603 16.062  80.720  1.00 26.27 ? 42   PRO   B CG    1 
ATOM   9255  C  CD    . PRO   B  1  44   ? -11.029 15.057  81.697  1.00 24.77 ? 42   PRO   B CD    1 
ATOM   9256  N  N     . GLU   B  1  45   ? -13.712 17.882  84.446  1.00 22.47 ? 43   GLU   B N     1 
ATOM   9257  C  CA    . GLU   B  1  45   ? -14.715 17.972  85.493  1.00 21.48 ? 43   GLU   B CA    1 
ATOM   9258  C  C     . GLU   B  1  45   ? -16.049 17.393  85.036  1.00 24.60 ? 43   GLU   B C     1 
ATOM   9259  O  O     . GLU   B  1  45   ? -16.745 16.732  85.813  1.00 25.43 ? 43   GLU   B O     1 
ATOM   9260  C  CB    . GLU   B  1  45   ? -14.833 19.436  85.911  1.00 26.91 ? 43   GLU   B CB    1 
ATOM   9261  C  CG    . GLU   B  1  45   ? -15.324 19.627  87.314  1.00 28.22 ? 43   GLU   B CG    1 
ATOM   9262  C  CD    . GLU   B  1  45   ? -14.760 20.869  87.971  1.00 21.35 ? 43   GLU   B CD    1 
ATOM   9263  O  OE1   . GLU   B  1  45   ? -13.910 21.569  87.374  1.00 21.89 ? 43   GLU   B OE1   1 
ATOM   9264  O  OE2   . GLU   B  1  45   ? -15.187 21.134  89.109  1.00 22.86 ? 43   GLU   B OE2   1 
ATOM   9265  N  N     . THR   B  1  46   ? -16.402 17.587  83.759  1.00 25.53 ? 44   THR   B N     1 
ATOM   9266  C  CA    . THR   B  1  46   ? -17.654 17.044  83.243  1.00 24.61 ? 44   THR   B CA    1 
ATOM   9267  C  C     . THR   B  1  46   ? -17.644 15.527  83.167  1.00 24.71 ? 44   THR   B C     1 
ATOM   9268  O  O     . THR   B  1  46   ? -18.715 14.912  83.160  1.00 27.52 ? 44   THR   B O     1 
ATOM   9269  C  CB    . THR   B  1  46   ? -17.946 17.608  81.856  1.00 26.64 ? 44   THR   B CB    1 
ATOM   9270  O  OG1   . THR   B  1  46   ? -16.802 17.407  81.015  1.00 27.13 ? 44   THR   B OG1   1 
ATOM   9271  C  CG2   . THR   B  1  46   ? -18.269 19.093  81.945  1.00 27.10 ? 44   THR   B CG2   1 
ATOM   9272  N  N     . GLU   B  1  47   ? -16.467 14.909  83.099  1.00 24.13 ? 45   GLU   B N     1 
ATOM   9273  C  CA    . GLU   B  1  47   ? -16.378 13.458  83.175  1.00 25.56 ? 45   GLU   B CA    1 
ATOM   9274  C  C     . GLU   B  1  47   ? -16.369 12.955  84.612  1.00 23.09 ? 45   GLU   B C     1 
ATOM   9275  O  O     . GLU   B  1  47   ? -16.829 11.840  84.876  1.00 27.67 ? 45   GLU   B O     1 
ATOM   9276  C  CB    . GLU   B  1  47   ? -15.125 12.967  82.445  1.00 25.17 ? 45   GLU   B CB    1 
ATOM   9277  C  CG    . GLU   B  1  47   ? -15.118 13.281  80.953  1.00 30.42 ? 45   GLU   B CG    1 
ATOM   9278  C  CD    . GLU   B  1  47   ? -13.803 12.920  80.295  1.00 34.81 ? 45   GLU   B CD    1 
ATOM   9279  O  OE1   . GLU   B  1  47   ? -13.125 11.994  80.793  1.00 39.53 ? 45   GLU   B OE1   1 
ATOM   9280  O  OE2   . GLU   B  1  47   ? -13.446 13.565  79.289  1.00 40.32 ? 45   GLU   B OE2   1 
ATOM   9281  N  N     . CYS   B  1  48   ? -15.854 13.758  85.547  1.00 21.46 ? 46   CYS   B N     1 
ATOM   9282  C  CA    . CYS   B  1  48   ? -15.781 13.315  86.935  1.00 23.09 ? 46   CYS   B CA    1 
ATOM   9283  C  C     . CYS   B  1  48   ? -17.147 13.295  87.598  1.00 23.52 ? 46   CYS   B C     1 
ATOM   9284  O  O     . CYS   B  1  48   ? -17.443 12.398  88.397  1.00 24.04 ? 46   CYS   B O     1 
ATOM   9285  C  CB    . CYS   B  1  48   ? -14.872 14.248  87.730  1.00 22.69 ? 46   CYS   B CB    1 
ATOM   9286  S  SG    . CYS   B  1  48   ? -13.147 14.159  87.284  1.00 22.41 ? 46   CYS   B SG    1 
ATOM   9287  N  N     . LEU   B  1  49   ? -17.979 14.288  87.304  1.00 23.88 ? 47   LEU   B N     1 
ATOM   9288  C  CA    . LEU   B  1  49   ? -19.174 14.489  88.126  1.00 22.96 ? 47   LEU   B CA    1 
ATOM   9289  C  C     . LEU   B  1  49   ? -20.244 13.421  87.974  1.00 26.20 ? 47   LEU   B C     1 
ATOM   9290  O  O     . LEU   B  1  49   ? -20.810 13.006  88.999  1.00 26.01 ? 47   LEU   B O     1 
ATOM   9291  C  CB    . LEU   B  1  49   ? -19.709 15.917  87.977  1.00 25.38 ? 47   LEU   B CB    1 
ATOM   9292  C  CG    . LEU   B  1  49   ? -19.243 16.854  89.096  1.00 24.25 ? 47   LEU   B CG    1 
ATOM   9293  C  CD1   . LEU   B  1  49   ? -19.775 16.379  90.454  1.00 26.33 ? 47   LEU   B CD1   1 
ATOM   9294  C  CD2   . LEU   B  1  49   ? -17.725 16.951  89.112  1.00 23.61 ? 47   LEU   B CD2   1 
ATOM   9295  N  N     . PRO   B  1  50   ? -20.603 12.964  86.775  1.00 27.19 ? 48   PRO   B N     1 
ATOM   9296  C  CA    . PRO   B  1  50   ? -21.762 12.060  86.656  1.00 25.85 ? 48   PRO   B CA    1 
ATOM   9297  C  C     . PRO   B  1  50   ? -21.649 10.822  87.534  1.00 27.16 ? 48   PRO   B C     1 
ATOM   9298  O  O     . PRO   B  1  50   ? -22.615 10.492  88.240  1.00 27.86 ? 48   PRO   B O     1 
ATOM   9299  C  CB    . PRO   B  1  50   ? -21.794 11.717  85.159  1.00 26.12 ? 48   PRO   B CB    1 
ATOM   9300  C  CG    . PRO   B  1  50   ? -21.284 12.954  84.521  1.00 26.74 ? 48   PRO   B CG    1 
ATOM   9301  C  CD    . PRO   B  1  50   ? -20.185 13.462  85.450  1.00 25.16 ? 48   PRO   B CD    1 
ATOM   9302  N  N     . PRO   B  1  51   ? -20.511 10.111  87.562  1.00 28.81 ? 49   PRO   B N     1 
ATOM   9303  C  CA    . PRO   B  1  51   ? -20.451 8.954   88.471  1.00 27.12 ? 49   PRO   B CA    1 
ATOM   9304  C  C     . PRO   B  1  51   ? -20.521 9.331   89.939  1.00 27.43 ? 49   PRO   B C     1 
ATOM   9305  O  O     . PRO   B  1  51   ? -21.059 8.557   90.739  1.00 28.65 ? 49   PRO   B O     1 
ATOM   9306  C  CB    . PRO   B  1  51   ? -19.129 8.265   88.108  1.00 29.41 ? 49   PRO   B CB    1 
ATOM   9307  C  CG    . PRO   B  1  51   ? -18.320 9.311   87.459  1.00 30.68 ? 49   PRO   B CG    1 
ATOM   9308  C  CD    . PRO   B  1  51   ? -19.296 10.186  86.726  1.00 25.98 ? 49   PRO   B CD    1 
ATOM   9309  N  N     . LEU   B  1  52   ? -19.997 10.498  90.319  1.00 26.60 ? 50   LEU   B N     1 
ATOM   9310  C  CA    . LEU   B  1  52   ? -20.145 10.949  91.699  1.00 25.49 ? 50   LEU   B CA    1 
ATOM   9311  C  C     . LEU   B  1  52   ? -21.603 11.247  92.024  1.00 27.18 ? 50   LEU   B C     1 
ATOM   9312  O  O     . LEU   B  1  52   ? -22.099 10.864  93.092  1.00 26.46 ? 50   LEU   B O     1 
ATOM   9313  C  CB    . LEU   B  1  52   ? -19.282 12.186  91.933  1.00 26.14 ? 50   LEU   B CB    1 
ATOM   9314  C  CG    . LEU   B  1  52   ? -17.788 11.987  91.695  1.00 24.89 ? 50   LEU   B CG    1 
ATOM   9315  C  CD1   . LEU   B  1  52   ? -17.067 13.325  91.723  1.00 25.35 ? 50   LEU   B CD1   1 
ATOM   9316  C  CD2   . LEU   B  1  52   ? -17.225 11.028  92.727  1.00 26.66 ? 50   LEU   B CD2   1 
ATOM   9317  N  N     . VAL   B  1  53   ? -22.299 11.936  91.119  1.00 25.61 ? 51   VAL   B N     1 
ATOM   9318  C  CA    . VAL   B  1  53   ? -23.723 12.205  91.318  1.00 25.87 ? 51   VAL   B CA    1 
ATOM   9319  C  C     . VAL   B  1  53   ? -24.482 10.905  91.537  1.00 31.10 ? 51   VAL   B C     1 
ATOM   9320  O  O     . VAL   B  1  53   ? -25.315 10.796  92.445  1.00 29.09 ? 51   VAL   B O     1 
ATOM   9321  C  CB    . VAL   B  1  53   ? -24.285 13.002  90.127  1.00 26.89 ? 51   VAL   B CB    1 
ATOM   9322  C  CG1   . VAL   B  1  53   ? -25.811 12.968  90.127  1.00 29.60 ? 51   VAL   B CG1   1 
ATOM   9323  C  CG2   . VAL   B  1  53   ? -23.794 14.424  90.179  1.00 27.27 ? 51   VAL   B CG2   1 
ATOM   9324  N  N     . GLU   B  1  54   ? -24.189 9.891   90.719  1.00 31.16 ? 52   GLU   B N     1 
ATOM   9325  C  CA    . GLU   B  1  54   ? -24.864 8.606   90.866  1.00 31.22 ? 52   GLU   B CA    1 
ATOM   9326  C  C     . GLU   B  1  54   ? -24.568 7.987   92.225  1.00 32.04 ? 52   GLU   B C     1 
ATOM   9327  O  O     . GLU   B  1  54   ? -25.479 7.528   92.922  1.00 32.73 ? 52   GLU   B O     1 
ATOM   9328  C  CB    . GLU   B  1  54   ? -24.457 7.662   89.734  1.00 35.09 ? 52   GLU   B CB    1 
ATOM   9329  N  N     . ALA   B  1  55   ? -23.295 7.989   92.630  1.00 29.01 ? 53   ALA   B N     1 
ATOM   9330  C  CA    . ALA   B  1  55   ? -22.929 7.410   93.920  1.00 31.48 ? 53   ALA   B CA    1 
ATOM   9331  C  C     . ALA   B  1  55   ? -23.524 8.188   95.089  1.00 27.96 ? 53   ALA   B C     1 
ATOM   9332  O  O     . ALA   B  1  55   ? -23.826 7.599   96.132  1.00 32.86 ? 53   ALA   B O     1 
ATOM   9333  C  CB    . ALA   B  1  55   ? -21.406 7.344   94.050  1.00 31.76 ? 53   ALA   B CB    1 
ATOM   9334  N  N     . ALA   B  1  56   ? -23.690 9.501   94.942  1.00 29.65 ? 54   ALA   B N     1 
ATOM   9335  C  CA    . ALA   B  1  56   ? -24.157 10.344  96.033  1.00 31.62 ? 54   ALA   B CA    1 
ATOM   9336  C  C     . ALA   B  1  56   ? -25.672 10.378  96.158  1.00 32.56 ? 54   ALA   B C     1 
ATOM   9337  O  O     . ALA   B  1  56   ? -26.181 10.923  97.146  1.00 34.29 ? 54   ALA   B O     1 
ATOM   9338  C  CB    . ALA   B  1  56   ? -23.644 11.772  95.840  1.00 30.31 ? 54   ALA   B CB    1 
ATOM   9339  N  N     . THR   B  1  57   ? -26.394 9.812   95.194  1.00 33.74 ? 55   THR   B N     1 
ATOM   9340  C  CA    . THR   B  1  57   ? -27.845 9.922   95.170  1.00 37.08 ? 55   THR   B CA    1 
ATOM   9341  C  C     . THR   B  1  57   ? -28.467 9.177   96.342  1.00 36.72 ? 55   THR   B C     1 
ATOM   9342  O  O     . THR   B  1  57   ? -28.068 8.055   96.668  1.00 36.29 ? 55   THR   B O     1 
ATOM   9343  C  CB    . THR   B  1  57   ? -28.379 9.360   93.853  1.00 38.47 ? 55   THR   B CB    1 
ATOM   9344  O  OG1   . THR   B  1  57   ? -28.004 10.235  92.785  1.00 36.44 ? 55   THR   B OG1   1 
ATOM   9345  C  CG2   . THR   B  1  57   ? -29.902 9.229   93.890  1.00 35.53 ? 55   THR   B CG2   1 
ATOM   9346  N  N     . GLN   B  1  58   ? -29.444 9.817   96.981  1.00 39.75 ? 56   GLN   B N     1 
ATOM   9347  C  CA    . GLN   B  1  58   ? -30.196 9.221   98.072  1.00 36.87 ? 56   GLN   B CA    1 
ATOM   9348  C  C     . GLN   B  1  58   ? -31.686 9.399   97.806  1.00 40.49 ? 56   GLN   B C     1 
ATOM   9349  O  O     . GLN   B  1  58   ? -32.101 10.265  97.030  1.00 38.63 ? 56   GLN   B O     1 
ATOM   9350  C  CB    . GLN   B  1  58   ? -29.809 9.830   99.430  1.00 39.17 ? 56   GLN   B CB    1 
ATOM   9351  C  CG    . GLN   B  1  58   ? -28.298 9.950   99.651  1.00 38.37 ? 56   GLN   B CG    1 
ATOM   9352  C  CD    . GLN   B  1  58   ? -27.916 9.893   101.119 1.00 43.61 ? 56   GLN   B CD    1 
ATOM   9353  O  OE1   . GLN   B  1  58   ? -28.133 8.881   101.786 1.00 44.77 ? 56   GLN   B OE1   1 
ATOM   9354  N  NE2   . GLN   B  1  58   ? -27.347 10.979  101.631 1.00 42.44 ? 56   GLN   B NE2   1 
ATOM   9355  N  N     . SER   B  1  59   ? -32.486 8.562   98.465  1.00 42.49 ? 57   SER   B N     1 
ATOM   9356  C  CA    . SER   B  1  59   ? -33.928 8.572   98.276  1.00 40.79 ? 57   SER   B CA    1 
ATOM   9357  C  C     . SER   B  1  59   ? -34.528 9.888   98.760  1.00 42.96 ? 57   SER   B C     1 
ATOM   9358  O  O     . SER   B  1  59   ? -33.926 10.631  99.539  1.00 40.50 ? 57   SER   B O     1 
ATOM   9359  C  CB    . SER   B  1  59   ? -34.570 7.430   99.060  1.00 44.48 ? 57   SER   B CB    1 
ATOM   9360  O  OG    . SER   B  1  59   ? -34.432 7.637   100.458 1.00 44.03 ? 57   SER   B OG    1 
ATOM   9361  N  N     . LYS   B  1  60   ? -35.747 10.166  98.289  1.00 42.05 ? 58   LYS   B N     1 
ATOM   9362  C  CA    . LYS   B  1  60   ? -36.464 11.352  98.748  1.00 44.36 ? 58   LYS   B CA    1 
ATOM   9363  C  C     . LYS   B  1  60   ? -36.659 11.335  100.258 1.00 44.15 ? 58   LYS   B C     1 
ATOM   9364  O  O     . LYS   B  1  60   ? -36.603 12.389  100.902 1.00 44.04 ? 58   LYS   B O     1 
ATOM   9365  C  CB    . LYS   B  1  60   ? -37.815 11.465  98.038  1.00 42.80 ? 58   LYS   B CB    1 
ATOM   9366  N  N     . GLU   B  1  61   ? -36.879 10.153  100.840 1.00 44.92 ? 59   GLU   B N     1 
ATOM   9367  C  CA    . GLU   B  1  61   ? -37.066 10.059  102.284 1.00 41.27 ? 59   GLU   B CA    1 
ATOM   9368  C  C     . GLU   B  1  61   ? -35.799 10.469  103.022 1.00 44.14 ? 59   GLU   B C     1 
ATOM   9369  O  O     . GLU   B  1  61   ? -35.833 11.321  103.917 1.00 43.30 ? 59   GLU   B O     1 
ATOM   9370  C  CB    . GLU   B  1  61   ? -37.476 8.635   102.666 1.00 50.16 ? 59   GLU   B CB    1 
ATOM   9371  N  N     . ILE   B  1  62   ? -34.664 9.876   102.646 1.00 42.12 ? 60   ILE   B N     1 
ATOM   9372  C  CA    . ILE   B  1  62   ? -33.396 10.219  103.285 1.00 42.65 ? 60   ILE   B CA    1 
ATOM   9373  C  C     . ILE   B  1  62   ? -33.056 11.686  103.056 1.00 40.83 ? 60   ILE   B C     1 
ATOM   9374  O  O     . ILE   B  1  62   ? -32.617 12.389  103.976 1.00 43.91 ? 60   ILE   B O     1 
ATOM   9375  C  CB    . ILE   B  1  62   ? -32.284 9.273   102.795 1.00 42.11 ? 60   ILE   B CB    1 
ATOM   9376  C  CG1   . ILE   B  1  62   ? -32.533 7.858   103.321 1.00 45.77 ? 60   ILE   B CG1   1 
ATOM   9377  C  CG2   . ILE   B  1  62   ? -30.913 9.786   103.210 1.00 42.13 ? 60   ILE   B CG2   1 
ATOM   9378  C  CD1   . ILE   B  1  62   ? -31.478 6.858   102.913 1.00 45.38 ? 60   ILE   B CD1   1 
ATOM   9379  N  N     . ARG   B  1  63   ? -33.264 12.175  101.830 1.00 36.23 ? 61   ARG   B N     1 
ATOM   9380  C  CA    . ARG   B  1  63   ? -32.982 13.573  101.523 1.00 39.18 ? 61   ARG   B CA    1 
ATOM   9381  C  C     . ARG   B  1  63   ? -33.819 14.517  102.375 1.00 41.91 ? 61   ARG   B C     1 
ATOM   9382  O  O     . ARG   B  1  63   ? -33.322 15.550  102.837 1.00 40.51 ? 61   ARG   B O     1 
ATOM   9383  C  CB    . ARG   B  1  63   ? -33.203 13.848  100.035 1.00 39.35 ? 61   ARG   B CB    1 
ATOM   9384  C  CG    . ARG   B  1  63   ? -32.122 13.261  99.151  1.00 39.17 ? 61   ARG   B CG    1 
ATOM   9385  C  CD    . ARG   B  1  63   ? -32.200 13.779  97.727  1.00 45.96 ? 61   ARG   B CD    1 
ATOM   9386  N  NE    . ARG   B  1  63   ? -33.321 13.214  96.986  1.00 45.90 ? 61   ARG   B NE    1 
ATOM   9387  C  CZ    . ARG   B  1  63   ? -34.330 13.923  96.500  1.00 46.37 ? 61   ARG   B CZ    1 
ATOM   9388  N  NH1   . ARG   B  1  63   ? -34.402 15.233  96.676  1.00 47.86 ? 61   ARG   B NH1   1 
ATOM   9389  N  NH2   . ARG   B  1  63   ? -35.283 13.305  95.810  1.00 47.19 ? 61   ARG   B NH2   1 
ATOM   9390  N  N     . ASP   B  1  64   ? -35.098 14.193  102.580 1.00 37.61 ? 62   ASP   B N     1 
ATOM   9391  C  CA    . ASP   B  1  64   ? -35.919 15.024  103.452 1.00 38.67 ? 62   ASP   B CA    1 
ATOM   9392  C  C     . ASP   B  1  64   ? -35.442 14.937  104.894 1.00 37.34 ? 62   ASP   B C     1 
ATOM   9393  O  O     . ASP   B  1  64   ? -35.331 15.960  105.579 1.00 42.00 ? 62   ASP   B O     1 
ATOM   9394  C  CB    . ASP   B  1  64   ? -37.390 14.619  103.344 1.00 43.23 ? 62   ASP   B CB    1 
ATOM   9395  C  CG    . ASP   B  1  64   ? -37.979 14.907  101.975 1.00 48.06 ? 62   ASP   B CG    1 
ATOM   9396  O  OD1   . ASP   B  1  64   ? -37.552 15.888  101.325 1.00 43.98 ? 62   ASP   B OD1   1 
ATOM   9397  O  OD2   . ASP   B  1  64   ? -38.880 14.151  101.551 1.00 53.52 ? 62   ASP   B OD2   1 
ATOM   9398  N  N     . ALA   B  1  65   ? -35.147 13.722  105.366 1.00 35.81 ? 63   ALA   B N     1 
ATOM   9399  C  CA    . ALA   B  1  65   ? -34.645 13.557  106.726 1.00 39.71 ? 63   ALA   B CA    1 
ATOM   9400  C  C     . ALA   B  1  65   ? -33.341 14.322  106.934 1.00 42.38 ? 63   ALA   B C     1 
ATOM   9401  O  O     . ALA   B  1  65   ? -33.159 14.982  107.963 1.00 44.45 ? 63   ALA   B O     1 
ATOM   9402  C  CB    . ALA   B  1  65   ? -34.466 12.071  107.041 1.00 41.07 ? 63   ALA   B CB    1 
ATOM   9403  N  N     . ALA   B  1  66   ? -32.425 14.255  105.961 1.00 41.12 ? 64   ALA   B N     1 
ATOM   9404  C  CA    . ALA   B  1  66   ? -31.151 14.955  106.093 1.00 38.48 ? 64   ALA   B CA    1 
ATOM   9405  C  C     . ALA   B  1  66   ? -31.343 16.467  106.077 1.00 39.61 ? 64   ALA   B C     1 
ATOM   9406  O  O     . ALA   B  1  66   ? -30.668 17.192  106.817 1.00 40.26 ? 64   ALA   B O     1 
ATOM   9407  C  CB    . ALA   B  1  66   ? -30.193 14.515  104.987 1.00 39.83 ? 64   ALA   B CB    1 
ATOM   9408  N  N     . ALA   B  1  67   ? -32.261 16.964  105.248 1.00 37.85 ? 65   ALA   B N     1 
ATOM   9409  C  CA    . ALA   B  1  67   ? -32.500 18.403  105.201 1.00 36.97 ? 65   ALA   B CA    1 
ATOM   9410  C  C     . ALA   B  1  67   ? -33.062 18.906  106.526 1.00 45.28 ? 65   ALA   B C     1 
ATOM   9411  O  O     . ALA   B  1  67   ? -32.744 20.020  106.961 1.00 39.98 ? 65   ALA   B O     1 
ATOM   9412  C  CB    . ALA   B  1  67   ? -33.449 18.741  104.051 1.00 44.36 ? 65   ALA   B CB    1 
ATOM   9413  N  N     . SER   B  1  68   ? -33.907 18.099  107.175 1.00 45.07 ? 66   SER   B N     1 
ATOM   9414  C  CA    . SER   B  1  68   ? -34.427 18.458  108.492 1.00 42.87 ? 66   SER   B CA    1 
ATOM   9415  C  C     . SER   B  1  68   ? -33.323 18.420  109.542 1.00 45.96 ? 66   SER   B C     1 
ATOM   9416  O  O     . SER   B  1  68   ? -33.182 19.353  110.342 1.00 47.75 ? 66   SER   B O     1 
ATOM   9417  C  CB    . SER   B  1  68   ? -35.568 17.517  108.875 1.00 45.92 ? 66   SER   B CB    1 
ATOM   9418  N  N     . THR   B  1  69   ? -32.537 17.339  109.561 1.00 42.86 ? 67   THR   B N     1 
ATOM   9419  C  CA    . THR   B  1  69   ? -31.411 17.242  110.487 1.00 41.95 ? 67   THR   B CA    1 
ATOM   9420  C  C     . THR   B  1  69   ? -30.442 18.400  110.292 1.00 42.34 ? 67   THR   B C     1 
ATOM   9421  O  O     . THR   B  1  69   ? -29.976 19.006  111.264 1.00 39.53 ? 67   THR   B O     1 
ATOM   9422  C  CB    . THR   B  1  69   ? -30.688 15.911  110.289 1.00 38.85 ? 67   THR   B CB    1 
ATOM   9423  O  OG1   . THR   B  1  69   ? -31.550 14.833  110.666 1.00 44.18 ? 67   THR   B OG1   1 
ATOM   9424  C  CG2   . THR   B  1  69   ? -29.424 15.863  111.132 1.00 37.05 ? 67   THR   B CG2   1 
ATOM   9425  N  N     . ALA   B  1  70   ? -30.108 18.706  109.036 1.00 37.14 ? 68   ALA   B N     1 
ATOM   9426  C  CA    . ALA   B  1  70   ? -29.270 19.865  108.757 1.00 42.05 ? 68   ALA   B CA    1 
ATOM   9427  C  C     . ALA   B  1  70   ? -29.909 21.147  109.271 1.00 41.67 ? 68   ALA   B C     1 
ATOM   9428  O  O     . ALA   B  1  70   ? -29.219 22.020  109.812 1.00 41.51 ? 68   ALA   B O     1 
ATOM   9429  C  CB    . ALA   B  1  70   ? -28.989 19.965  107.256 1.00 39.70 ? 68   ALA   B CB    1 
ATOM   9430  N  N     . ARG   B  1  71   ? -31.229 21.282  109.110 1.00 44.62 ? 69   ARG   B N     1 
ATOM   9431  C  CA    . ARG   B  1  71   ? -31.916 22.460  109.631 1.00 45.82 ? 69   ARG   B CA    1 
ATOM   9432  C  C     . ARG   B  1  71   ? -31.764 22.544  111.144 1.00 35.05 ? 69   ARG   B C     1 
ATOM   9433  O  O     . ARG   B  1  71   ? -31.429 23.602  111.688 1.00 39.25 ? 69   ARG   B O     1 
ATOM   9434  C  CB    . ARG   B  1  71   ? -33.393 22.435  109.223 1.00 45.21 ? 69   ARG   B CB    1 
ATOM   9435  C  CG    . ARG   B  1  71   ? -34.172 23.682  109.631 1.00 45.62 ? 69   ARG   B CG    1 
ATOM   9436  C  CD    . ARG   B  1  71   ? -35.503 23.812  108.884 1.00 44.50 ? 69   ARG   B CD    1 
ATOM   9437  N  NE    . ARG   B  1  71   ? -35.406 24.637  107.685 1.00 45.48 ? 69   ARG   B NE    1 
ATOM   9438  C  CZ    . ARG   B  1  71   ? -35.338 25.963  107.692 1.00 49.23 ? 69   ARG   B CZ    1 
ATOM   9439  N  NH1   . ARG   B  1  71   ? -35.338 26.648  108.825 1.00 47.04 ? 69   ARG   B NH1   1 
ATOM   9440  N  NH2   . ARG   B  1  71   ? -35.259 26.617  106.536 1.00 50.22 ? 69   ARG   B NH2   1 
ATOM   9441  N  N     . LYS   B  1  72   ? -31.960 21.415  111.832 1.00 37.27 ? 70   LYS   B N     1 
ATOM   9442  C  CA    . LYS   B  1  72   ? -31.862 21.383  113.288 1.00 37.30 ? 70   LYS   B CA    1 
ATOM   9443  C  C     . LYS   B  1  72   ? -30.465 21.765  113.766 1.00 42.13 ? 70   LYS   B C     1 
ATOM   9444  O  O     . LYS   B  1  72   ? -30.313 22.366  114.836 1.00 41.89 ? 70   LYS   B O     1 
ATOM   9445  C  CB    . LYS   B  1  72   ? -32.242 19.987  113.788 1.00 39.33 ? 70   LYS   B CB    1 
ATOM   9446  C  CG    . LYS   B  1  72   ? -32.173 19.790  115.301 1.00 41.78 ? 70   LYS   B CG    1 
ATOM   9447  C  CD    . LYS   B  1  72   ? -32.574 18.360  115.674 1.00 42.51 ? 70   LYS   B CD    1 
ATOM   9448  C  CE    . LYS   B  1  72   ? -32.304 18.038  117.141 1.00 45.98 ? 70   LYS   B CE    1 
ATOM   9449  N  NZ    . LYS   B  1  72   ? -33.213 18.747  118.078 1.00 39.77 ? 70   LYS   B NZ    1 
ATOM   9450  N  N     . LEU   B  1  73   ? -29.434 21.435  112.989 1.00 42.56 ? 71   LEU   B N     1 
ATOM   9451  C  CA    . LEU   B  1  73   ? -28.075 21.786  113.383 1.00 39.57 ? 71   LEU   B CA    1 
ATOM   9452  C  C     . LEU   B  1  73   ? -27.788 23.264  113.145 1.00 37.74 ? 71   LEU   B C     1 
ATOM   9453  O  O     . LEU   B  1  73   ? -27.140 23.913  113.973 1.00 43.09 ? 71   LEU   B O     1 
ATOM   9454  C  CB    . LEU   B  1  73   ? -27.075 20.919  112.618 1.00 37.44 ? 71   LEU   B CB    1 
ATOM   9455  C  CG    . LEU   B  1  73   ? -27.233 19.408  112.804 1.00 36.12 ? 71   LEU   B CG    1 
ATOM   9456  C  CD1   . LEU   B  1  73   ? -26.386 18.657  111.783 1.00 37.72 ? 71   LEU   B CD1   1 
ATOM   9457  C  CD2   . LEU   B  1  73   ? -26.871 18.991  114.220 1.00 39.76 ? 71   LEU   B CD2   1 
ATOM   9458  N  N     . ILE   B  1  74   ? -28.257 23.807  112.021 1.00 39.15 ? 72   ILE   B N     1 
ATOM   9459  C  CA    . ILE   B  1  74   ? -27.953 25.192  111.673 1.00 40.16 ? 72   ILE   B CA    1 
ATOM   9460  C  C     . ILE   B  1  74   ? -28.703 26.157  112.583 1.00 45.58 ? 72   ILE   B C     1 
ATOM   9461  O  O     . ILE   B  1  74   ? -28.156 27.181  113.015 1.00 41.60 ? 72   ILE   B O     1 
ATOM   9462  C  CB    . ILE   B  1  74   ? -28.243 25.439  110.183 1.00 40.32 ? 72   ILE   B CB    1 
ATOM   9463  C  CG1   . ILE   B  1  74   ? -27.261 24.636  109.326 1.00 39.64 ? 72   ILE   B CG1   1 
ATOM   9464  C  CG2   . ILE   B  1  74   ? -28.157 26.924  109.857 1.00 38.75 ? 72   ILE   B CG2   1 
ATOM   9465  C  CD1   . ILE   B  1  74   ? -27.800 24.263  107.967 1.00 38.87 ? 72   ILE   B CD1   1 
ATOM   9466  N  N     . GLU   B  1  75   ? -29.969 25.857  112.875 1.00 42.63 ? 73   GLU   B N     1 
ATOM   9467  C  CA    . GLU   B  1  75   ? -30.704 26.638  113.863 1.00 43.28 ? 73   GLU   B CA    1 
ATOM   9468  C  C     . GLU   B  1  75   ? -29.984 26.618  115.207 1.00 46.29 ? 73   GLU   B C     1 
ATOM   9469  O  O     . GLU   B  1  75   ? -29.780 27.667  115.831 1.00 47.88 ? 73   GLU   B O     1 
ATOM   9470  C  CB    . GLU   B  1  75   ? -32.129 26.099  113.994 1.00 41.10 ? 73   GLU   B CB    1 
ATOM   9471  N  N     . ALA   B  1  76   ? -29.575 25.426  115.657 1.00 41.24 ? 74   ALA   B N     1 
ATOM   9472  C  CA    . ALA   B  1  76   ? -28.800 25.315  116.888 1.00 43.90 ? 74   ALA   B CA    1 
ATOM   9473  C  C     . ALA   B  1  76   ? -27.523 26.146  116.823 1.00 43.54 ? 74   ALA   B C     1 
ATOM   9474  O  O     . ALA   B  1  76   ? -27.167 26.827  117.793 1.00 46.49 ? 74   ALA   B O     1 
ATOM   9475  C  CB    . ALA   B  1  76   ? -28.475 23.848  117.173 1.00 38.81 ? 74   ALA   B CB    1 
ATOM   9476  N  N     . LEU   B  1  77   ? -26.818 26.105  115.689 1.00 40.57 ? 75   LEU   B N     1 
ATOM   9477  C  CA    . LEU   B  1  77   ? -25.584 26.872  115.553 1.00 45.15 ? 75   LEU   B CA    1 
ATOM   9478  C  C     . LEU   B  1  77   ? -25.858 28.371  115.589 1.00 43.07 ? 75   LEU   B C     1 
ATOM   9479  O  O     . LEU   B  1  77   ? -25.171 29.123  116.291 1.00 44.72 ? 75   LEU   B O     1 
ATOM   9480  C  CB    . LEU   B  1  77   ? -24.875 26.494  114.250 1.00 42.55 ? 75   LEU   B CB    1 
ATOM   9481  C  CG    . LEU   B  1  77   ? -24.144 25.155  114.198 1.00 41.76 ? 75   LEU   B CG    1 
ATOM   9482  C  CD1   . LEU   B  1  77   ? -23.685 24.872  112.776 1.00 37.31 ? 75   LEU   B CD1   1 
ATOM   9483  C  CD2   . LEU   B  1  77   ? -22.958 25.174  115.138 1.00 40.67 ? 75   LEU   B CD2   1 
ATOM   9484  N  N     . ARG   B  1  78   ? -26.850 28.826  114.822 1.00 40.28 ? 76   ARG   B N     1 
ATOM   9485  C  CA    . ARG   B  1  78   ? -27.124 30.255  114.730 1.00 42.96 ? 76   ARG   B CA    1 
ATOM   9486  C  C     . ARG   B  1  78   ? -27.770 30.805  115.992 1.00 44.11 ? 76   ARG   B C     1 
ATOM   9487  O  O     . ARG   B  1  78   ? -27.782 32.024  116.187 1.00 45.45 ? 76   ARG   B O     1 
ATOM   9488  C  CB    . ARG   B  1  78   ? -28.008 30.540  113.519 1.00 48.82 ? 76   ARG   B CB    1 
ATOM   9489  C  CG    . ARG   B  1  78   ? -27.349 30.150  112.216 1.00 47.09 ? 76   ARG   B CG    1 
ATOM   9490  C  CD    . ARG   B  1  78   ? -28.131 30.634  111.018 1.00 50.31 ? 76   ARG   B CD    1 
ATOM   9491  N  NE    . ARG   B  1  78   ? -27.232 31.105  109.972 1.00 49.38 ? 76   ARG   B NE    1 
ATOM   9492  C  CZ    . ARG   B  1  78   ? -27.628 31.533  108.782 1.00 53.17 ? 76   ARG   B CZ    1 
ATOM   9493  N  NH1   . ARG   B  1  78   ? -28.906 31.520  108.434 1.00 54.84 ? 76   ARG   B NH1   1 
ATOM   9494  N  NH2   . ARG   B  1  78   ? -26.721 31.987  107.921 1.00 51.35 ? 76   ARG   B NH2   1 
ATOM   9495  N  N     . GLY   B  1  79   ? -28.292 29.938  116.847 1.00 41.59 ? 77   GLY   B N     1 
ATOM   9496  C  CA    . GLY   B  1  79   ? -28.949 30.358  118.061 1.00 45.79 ? 77   GLY   B CA    1 
ATOM   9497  C  C     . GLY   B  1  79   ? -28.055 30.547  119.260 1.00 47.50 ? 77   GLY   B C     1 
ATOM   9498  O  O     . GLY   B  1  79   ? -28.526 31.021  120.294 1.00 37.61 ? 77   GLY   B O     1 
ATOM   9499  N  N     . LYS   B  1  80   ? -26.773 30.209  119.164 1.00 47.68 ? 78   LYS   B N     1 
ATOM   9500  C  CA    . LYS   B  1  80   ? -25.901 30.269  120.333 1.00 43.89 ? 78   LYS   B CA    1 
ATOM   9501  C  C     . LYS   B  1  80   ? -24.598 31.019  120.064 1.00 38.71 ? 78   LYS   B C     1 
ATOM   9502  O  O     . LYS   B  1  80   ? -24.355 31.490  118.952 1.00 46.23 ? 78   LYS   B O     1 
ATOM   9503  C  CB    . LYS   B  1  80   ? -25.616 28.854  120.846 1.00 46.26 ? 78   LYS   B CB    1 
ATOM   9504  C  CG    . LYS   B  1  80   ? -24.903 27.966  119.842 1.00 41.87 ? 78   LYS   B CG    1 
ATOM   9505  C  CD    . LYS   B  1  80   ? -24.961 26.498  120.256 1.00 43.68 ? 78   LYS   B CD    1 
ATOM   9506  C  CE    . LYS   B  1  80   ? -24.013 25.643  119.409 1.00 40.71 ? 78   LYS   B CE    1 
ATOM   9507  N  NZ    . LYS   B  1  80   ? -24.108 24.188  119.741 1.00 38.03 ? 78   LYS   B NZ    1 
ATOM   9508  N  N     . GLY   B  1  85   ? -15.669 36.410  120.687 1.00 49.28 ? 83   GLY   B N     1 
ATOM   9509  C  CA    . GLY   B  1  85   ? -14.518 36.825  121.468 1.00 44.89 ? 83   GLY   B CA    1 
ATOM   9510  C  C     . GLY   B  1  85   ? -13.917 38.128  120.975 1.00 43.67 ? 83   GLY   B C     1 
ATOM   9511  O  O     . GLY   B  1  85   ? -13.972 39.152  121.662 1.00 42.88 ? 83   GLY   B O     1 
ATOM   9512  N  N     . VAL   B  1  86   ? -13.337 38.084  119.775 1.00 43.43 ? 84   VAL   B N     1 
ATOM   9513  C  CA    . VAL   B  1  86   ? -12.816 39.299  119.158 1.00 42.06 ? 84   VAL   B CA    1 
ATOM   9514  C  C     . VAL   B  1  86   ? -13.945 40.282  118.867 1.00 39.88 ? 84   VAL   B C     1 
ATOM   9515  O  O     . VAL   B  1  86   ? -13.783 41.498  119.028 1.00 40.55 ? 84   VAL   B O     1 
ATOM   9516  C  CB    . VAL   B  1  86   ? -11.995 38.950  117.904 1.00 41.52 ? 84   VAL   B CB    1 
ATOM   9517  C  CG1   . VAL   B  1  86   ? -11.820 40.167  117.012 1.00 47.07 ? 84   VAL   B CG1   1 
ATOM   9518  C  CG2   . VAL   B  1  86   ? -10.640 38.407  118.309 1.00 44.32 ? 84   VAL   B CG2   1 
ATOM   9519  N  N     . GLU   B  1  87   ? -15.108 39.774  118.449 1.00 42.93 ? 85   GLU   B N     1 
ATOM   9520  C  CA    . GLU   B  1  87   ? -16.242 40.649  118.158 1.00 45.28 ? 85   GLU   B CA    1 
ATOM   9521  C  C     . GLU   B  1  87   ? -16.627 41.484  119.374 1.00 41.26 ? 85   GLU   B C     1 
ATOM   9522  O  O     . GLU   B  1  87   ? -16.878 42.689  119.256 1.00 41.42 ? 85   GLU   B O     1 
ATOM   9523  C  CB    . GLU   B  1  87   ? -17.434 39.821  117.677 1.00 47.43 ? 85   GLU   B CB    1 
ATOM   9524  N  N     . GLY   B  1  88   ? -16.671 40.862  120.554 1.00 42.74 ? 86   GLY   B N     1 
ATOM   9525  C  CA    . GLY   B  1  88   ? -17.025 41.603  121.753 1.00 41.55 ? 86   GLY   B CA    1 
ATOM   9526  C  C     . GLY   B  1  88   ? -15.994 42.653  122.119 1.00 38.08 ? 86   GLY   B C     1 
ATOM   9527  O  O     . GLY   B  1  88   ? -16.340 43.734  122.601 1.00 37.29 ? 86   GLY   B O     1 
ATOM   9528  N  N     . LEU   B  1  89   ? -14.712 42.349  121.899 1.00 37.06 ? 87   LEU   B N     1 
ATOM   9529  C  CA    . LEU   B  1  89   ? -13.669 43.334  122.157 1.00 38.16 ? 87   LEU   B CA    1 
ATOM   9530  C  C     . LEU   B  1  89   ? -13.790 44.518  121.206 1.00 33.57 ? 87   LEU   B C     1 
ATOM   9531  O  O     . LEU   B  1  89   ? -13.688 45.677  121.628 1.00 31.15 ? 87   LEU   B O     1 
ATOM   9532  C  CB    . LEU   B  1  89   ? -12.299 42.672  122.020 1.00 37.67 ? 87   LEU   B CB    1 
ATOM   9533  C  CG    . LEU   B  1  89   ? -11.082 43.578  122.180 1.00 39.31 ? 87   LEU   B CG    1 
ATOM   9534  C  CD1   . LEU   B  1  89   ? -11.090 44.216  123.544 1.00 42.72 ? 87   LEU   B CD1   1 
ATOM   9535  C  CD2   . LEU   B  1  89   ? -9.804  42.780  121.954 1.00 41.47 ? 87   LEU   B CD2   1 
ATOM   9536  N  N     . VAL   B  1  90   ? -14.018 44.241  119.921 1.00 34.29 ? 88   VAL   B N     1 
ATOM   9537  C  CA    . VAL   B  1  90   ? -14.202 45.306  118.941 1.00 35.34 ? 88   VAL   B CA    1 
ATOM   9538  C  C     . VAL   B  1  90   ? -15.406 46.164  119.305 1.00 36.31 ? 88   VAL   B C     1 
ATOM   9539  O  O     . VAL   B  1  90   ? -15.357 47.397  119.220 1.00 35.94 ? 88   VAL   B O     1 
ATOM   9540  C  CB    . VAL   B  1  90   ? -14.314 44.713  117.523 1.00 35.37 ? 88   VAL   B CB    1 
ATOM   9541  C  CG1   . VAL   B  1  90   ? -14.776 45.770  116.529 1.00 37.23 ? 88   VAL   B CG1   1 
ATOM   9542  C  CG2   . VAL   B  1  90   ? -12.983 44.115  117.092 1.00 31.68 ? 88   VAL   B CG2   1 
ATOM   9543  N  N     . GLN   B  1  91   ? -16.495 45.529  119.746 1.00 38.20 ? 89   GLN   B N     1 
ATOM   9544  C  CA    . GLN   B  1  91   ? -17.687 46.282  120.121 1.00 39.39 ? 89   GLN   B CA    1 
ATOM   9545  C  C     . GLN   B  1  91   ? -17.443 47.118  121.373 1.00 35.78 ? 89   GLN   B C     1 
ATOM   9546  O  O     . GLN   B  1  91   ? -17.801 48.299  121.420 1.00 40.71 ? 89   GLN   B O     1 
ATOM   9547  C  CB    . GLN   B  1  91   ? -18.870 45.332  120.318 1.00 44.85 ? 89   GLN   B CB    1 
ATOM   9548  N  N     . GLU   B  1  92   ? -16.817 46.526  122.394 1.00 37.01 ? 90   GLU   B N     1 
ATOM   9549  C  CA    . GLU   B  1  92   ? -16.662 47.219  123.669 1.00 38.48 ? 90   GLU   B CA    1 
ATOM   9550  C  C     . GLU   B  1  92   ? -15.818 48.482  123.532 1.00 33.95 ? 90   GLU   B C     1 
ATOM   9551  O  O     . GLU   B  1  92   ? -16.112 49.504  124.162 1.00 36.87 ? 90   GLU   B O     1 
ATOM   9552  C  CB    . GLU   B  1  92   ? -16.067 46.282  124.725 1.00 40.65 ? 90   GLU   B CB    1 
ATOM   9553  C  CG    . GLU   B  1  92   ? -15.997 46.917  126.110 1.00 43.25 ? 90   GLU   B CG    1 
ATOM   9554  C  CD    . GLU   B  1  92   ? -15.237 46.086  127.134 1.00 44.56 ? 90   GLU   B CD    1 
ATOM   9555  O  OE1   . GLU   B  1  92   ? -14.903 44.917  126.843 1.00 48.67 ? 90   GLU   B OE1   1 
ATOM   9556  O  OE2   . GLU   B  1  92   ? -14.976 46.613  128.237 1.00 42.12 ? 90   GLU   B OE2   1 
ATOM   9557  N  N     . TYR   B  1  93   ? -14.768 48.441  122.714 1.00 34.46 ? 91   TYR   B N     1 
ATOM   9558  C  CA    . TYR   B  1  93   ? -13.890 49.592  122.560 1.00 35.15 ? 91   TYR   B CA    1 
ATOM   9559  C  C     . TYR   B  1  93   ? -14.123 50.355  121.266 1.00 34.77 ? 91   TYR   B C     1 
ATOM   9560  O  O     . TYR   B  1  93   ? -13.340 51.255  120.946 1.00 32.15 ? 91   TYR   B O     1 
ATOM   9561  C  CB    . TYR   B  1  93   ? -12.424 49.185  122.715 1.00 31.60 ? 91   TYR   B CB    1 
ATOM   9562  C  CG    . TYR   B  1  93   ? -12.126 48.803  124.138 1.00 30.62 ? 91   TYR   B CG    1 
ATOM   9563  C  CD1   . TYR   B  1  93   ? -11.805 49.772  125.083 1.00 29.83 ? 91   TYR   B CD1   1 
ATOM   9564  C  CD2   . TYR   B  1  93   ? -12.220 47.484  124.555 1.00 34.42 ? 91   TYR   B CD2   1 
ATOM   9565  C  CE1   . TYR   B  1  93   ? -11.554 49.437  126.396 1.00 32.82 ? 91   TYR   B CE1   1 
ATOM   9566  C  CE2   . TYR   B  1  93   ? -11.975 47.138  125.879 1.00 35.47 ? 91   TYR   B CE2   1 
ATOM   9567  C  CZ    . TYR   B  1  93   ? -11.640 48.119  126.789 1.00 35.01 ? 91   TYR   B CZ    1 
ATOM   9568  O  OH    . TYR   B  1  93   ? -11.397 47.784  128.106 1.00 36.40 ? 91   TYR   B OH    1 
ATOM   9569  N  N     . SER   B  1  94   ? -15.186 50.026  120.531 1.00 31.56 ? 92   SER   B N     1 
ATOM   9570  C  CA    . SER   B  1  94   ? -15.547 50.721  119.301 1.00 29.55 ? 92   SER   B CA    1 
ATOM   9571  C  C     . SER   B  1  94   ? -14.366 50.771  118.342 1.00 29.47 ? 92   SER   B C     1 
ATOM   9572  O  O     . SER   B  1  94   ? -14.029 51.817  117.784 1.00 30.66 ? 92   SER   B O     1 
ATOM   9573  C  CB    . SER   B  1  94   ? -16.090 52.118  119.584 1.00 30.95 ? 92   SER   B CB    1 
ATOM   9574  O  OG    . SER   B  1  94   ? -17.216 52.045  120.437 1.00 37.21 ? 92   SER   B OG    1 
ATOM   9575  N  N     . LEU   B  1  95   ? -13.727 49.620  118.167 1.00 26.93 ? 93   LEU   B N     1 
ATOM   9576  C  CA    . LEU   B  1  95   ? -12.549 49.532  117.325 1.00 26.50 ? 93   LEU   B CA    1 
ATOM   9577  C  C     . LEU   B  1  95   ? -12.949 49.427  115.865 1.00 28.48 ? 93   LEU   B C     1 
ATOM   9578  O  O     . LEU   B  1  95   ? -13.906 48.734  115.510 1.00 28.16 ? 93   LEU   B O     1 
ATOM   9579  C  CB    . LEU   B  1  95   ? -11.743 48.287  117.684 1.00 27.98 ? 93   LEU   B CB    1 
ATOM   9580  C  CG    . LEU   B  1  95   ? -11.210 48.206  119.111 1.00 28.74 ? 93   LEU   B CG    1 
ATOM   9581  C  CD1   . LEU   B  1  95   ? -10.265 47.028  119.253 1.00 26.64 ? 93   LEU   B CD1   1 
ATOM   9582  C  CD2   . LEU   B  1  95   ? -10.527 49.508  119.518 1.00 29.31 ? 93   LEU   B CD2   1 
ATOM   9583  N  N     . SER   B  1  96   ? -12.182 50.088  115.009 1.00 25.39 ? 94   SER   B N     1 
ATOM   9584  C  CA    . SER   B  1  96   ? -12.277 49.793  113.599 1.00 25.36 ? 94   SER   B CA    1 
ATOM   9585  C  C     . SER   B  1  96   ? -11.618 48.442  113.336 1.00 26.38 ? 94   SER   B C     1 
ATOM   9586  O  O     . SER   B  1  96   ? -10.949 47.874  114.203 1.00 24.70 ? 94   SER   B O     1 
ATOM   9587  C  CB    . SER   B  1  96   ? -11.545 50.866  112.806 1.00 24.10 ? 94   SER   B CB    1 
ATOM   9588  O  OG    . SER   B  1  96   ? -10.148 50.795  113.054 1.00 23.89 ? 94   SER   B OG    1 
ATOM   9589  N  N     . SER   B  1  97   ? -11.811 47.915  112.126 1.00 24.98 ? 95   SER   B N     1 
ATOM   9590  C  CA    . SER   B  1  97   ? -11.147 46.666  111.773 1.00 23.89 ? 95   SER   B CA    1 
ATOM   9591  C  C     . SER   B  1  97   ? -9.635  46.804  111.888 1.00 23.90 ? 95   SER   B C     1 
ATOM   9592  O  O     . SER   B  1  97   ? -8.966  45.953  112.485 1.00 22.58 ? 95   SER   B O     1 
ATOM   9593  C  CB    . SER   B  1  97   ? -11.550 46.222  110.367 1.00 28.00 ? 95   SER   B CB    1 
ATOM   9594  O  OG    . SER   B  1  97   ? -12.912 45.822  110.372 1.00 32.87 ? 95   SER   B OG    1 
ATOM   9595  N  N     . GLN   B  1  98   ? -9.079  47.884  111.334 1.00 22.94 ? 96   GLN   B N     1 
ATOM   9596  C  CA    . GLN   B  1  98   ? -7.633  48.081  111.402 1.00 22.30 ? 96   GLN   B CA    1 
ATOM   9597  C  C     . GLN   B  1  98   ? -7.162  48.220  112.841 1.00 21.81 ? 96   GLN   B C     1 
ATOM   9598  O  O     . GLN   B  1  98   ? -6.067  47.765  113.192 1.00 21.33 ? 96   GLN   B O     1 
ATOM   9599  C  CB    . GLN   B  1  98   ? -7.228  49.312  110.587 1.00 23.85 ? 96   GLN   B CB    1 
ATOM   9600  C  CG    . GLN   B  1  98   ? -7.269  49.096  109.095 1.00 22.87 ? 96   GLN   B CG    1 
ATOM   9601  C  CD    . GLN   B  1  98   ? -6.270  48.049  108.656 1.00 24.02 ? 96   GLN   B CD    1 
ATOM   9602  O  OE1   . GLN   B  1  98   ? -6.547  46.850  108.702 1.00 26.56 ? 96   GLN   B OE1   1 
ATOM   9603  N  NE2   . GLN   B  1  98   ? -5.092  48.495  108.227 1.00 22.36 ? 96   GLN   B NE2   1 
ATOM   9604  N  N     . GLU   B  1  99   ? -7.968  48.854  113.687 1.00 20.50 ? 97   GLU   B N     1 
ATOM   9605  C  CA    . GLU   B  1  99   ? -7.602  48.943  115.094 1.00 21.23 ? 97   GLU   B CA    1 
ATOM   9606  C  C     . GLU   B  1  99   ? -7.637  47.574  115.754 1.00 24.45 ? 97   GLU   B C     1 
ATOM   9607  O  O     . GLU   B  1  99   ? -6.745  47.237  116.539 1.00 23.30 ? 97   GLU   B O     1 
ATOM   9608  C  CB    . GLU   B  1  99   ? -8.521  49.922  115.813 1.00 22.50 ? 97   GLU   B CB    1 
ATOM   9609  C  CG    . GLU   B  1  99   ? -8.206  51.374  115.504 1.00 22.81 ? 97   GLU   B CG    1 
ATOM   9610  C  CD    . GLU   B  1  99   ? -9.305  52.302  115.961 1.00 24.35 ? 97   GLU   B CD    1 
ATOM   9611  O  OE1   . GLU   B  1  99   ? -10.296 51.808  116.542 1.00 26.30 ? 97   GLU   B OE1   1 
ATOM   9612  O  OE2   . GLU   B  1  99   ? -9.174  53.528  115.781 1.00 24.26 ? 97   GLU   B OE2   1 
ATOM   9613  N  N     . GLY   B  1  100  ? -8.652  46.766  115.437 1.00 21.85 ? 98   GLY   B N     1 
ATOM   9614  C  CA    . GLY   B  1  100  ? -8.689  45.415  115.967 1.00 23.15 ? 98   GLY   B CA    1 
ATOM   9615  C  C     . GLY   B  1  100  ? -7.476  44.610  115.550 1.00 23.31 ? 98   GLY   B C     1 
ATOM   9616  O  O     . GLY   B  1  100  ? -6.864  43.921  116.371 1.00 23.76 ? 98   GLY   B O     1 
ATOM   9617  N  N     . VAL   B  1  101  ? -7.097  44.706  114.275 1.00 20.22 ? 99   VAL   B N     1 
ATOM   9618  C  CA    . VAL   B  1  101  ? -5.920  43.990  113.793 1.00 20.47 ? 99   VAL   B CA    1 
ATOM   9619  C  C     . VAL   B  1  101  ? -4.665  44.495  114.491 1.00 21.96 ? 99   VAL   B C     1 
ATOM   9620  O  O     . VAL   B  1  101  ? -3.839  43.707  114.971 1.00 21.73 ? 99   VAL   B O     1 
ATOM   9621  C  CB    . VAL   B  1  101  ? -5.805  44.115  112.265 1.00 20.09 ? 99   VAL   B CB    1 
ATOM   9622  C  CG1   . VAL   B  1  101  ? -4.518  43.474  111.771 1.00 21.32 ? 99   VAL   B CG1   1 
ATOM   9623  C  CG2   . VAL   B  1  101  ? -7.010  43.482  111.590 1.00 24.85 ? 99   VAL   B CG2   1 
ATOM   9624  N  N     . ALA   B  1  102  ? -4.496  45.820  114.543 1.00 20.10 ? 100  ALA   B N     1 
ATOM   9625  C  CA    . ALA   B  1  102  ? -3.303  46.392  115.156 1.00 20.75 ? 100  ALA   B CA    1 
ATOM   9626  C  C     . ALA   B  1  102  ? -3.209  45.987  116.614 1.00 21.13 ? 100  ALA   B C     1 
ATOM   9627  O  O     . ALA   B  1  102  ? -2.116  45.695  117.116 1.00 22.11 ? 100  ALA   B O     1 
ATOM   9628  C  CB    . ALA   B  1  102  ? -3.336  47.916  115.045 1.00 21.98 ? 100  ALA   B CB    1 
ATOM   9629  N  N     . LEU   B  1  103  ? -4.351  45.963  117.305 1.00 21.14 ? 101  LEU   B N     1 
ATOM   9630  C  CA    . LEU   B  1  103  ? -4.371  45.579  118.710 1.00 23.14 ? 101  LEU   B CA    1 
ATOM   9631  C  C     . LEU   B  1  103  ? -3.931  44.134  118.891 1.00 23.93 ? 101  LEU   B C     1 
ATOM   9632  O  O     . LEU   B  1  103  ? -3.172  43.818  119.819 1.00 23.27 ? 101  LEU   B O     1 
ATOM   9633  C  CB    . LEU   B  1  103  ? -5.774  45.787  119.279 1.00 22.77 ? 101  LEU   B CB    1 
ATOM   9634  C  CG    . LEU   B  1  103  ? -5.936  45.327  120.717 1.00 22.99 ? 101  LEU   B CG    1 
ATOM   9635  C  CD1   . LEU   B  1  103  ? -5.067  46.185  121.619 1.00 26.45 ? 101  LEU   B CD1   1 
ATOM   9636  C  CD2   . LEU   B  1  103  ? -7.398  45.410  121.133 1.00 23.81 ? 101  LEU   B CD2   1 
ATOM   9637  N  N     . MET   B  1  104  ? -4.402  43.240  118.026 1.00 21.63 ? 102  MET   B N     1 
ATOM   9638  C  CA    . MET   B  1  104  ? -4.005  41.846  118.162 1.00 24.30 ? 102  MET   B CA    1 
ATOM   9639  C  C     . MET   B  1  104  ? -2.539  41.655  117.831 1.00 23.34 ? 102  MET   B C     1 
ATOM   9640  O  O     . MET   B  1  104  ? -1.874  40.821  118.452 1.00 24.86 ? 102  MET   B O     1 
ATOM   9641  C  CB    . MET   B  1  104  ? -4.890  40.942  117.308 1.00 24.68 ? 102  MET   B CB    1 
ATOM   9642  C  CG    . MET   B  1  104  ? -6.360  41.016  117.697 1.00 27.52 ? 102  MET   B CG    1 
ATOM   9643  S  SD    . MET   B  1  104  ? -6.647  40.638  119.441 1.00 33.28 ? 102  MET   B SD    1 
ATOM   9644  C  CE    . MET   B  1  104  ? -6.341  38.880  119.426 1.00 35.64 ? 102  MET   B CE    1 
ATOM   9645  N  N     . CYS   B  1  105  ? -2.012  42.423  116.880 1.00 21.02 ? 103  CYS   B N     1 
ATOM   9646  C  CA    . CYS   B  1  105  ? -0.577  42.392  116.634 1.00 22.67 ? 103  CYS   B CA    1 
ATOM   9647  C  C     . CYS   B  1  105  ? 0.186   42.850  117.862 1.00 22.93 ? 103  CYS   B C     1 
ATOM   9648  O  O     . CYS   B  1  105  ? 1.192   42.241  118.245 1.00 23.48 ? 103  CYS   B O     1 
ATOM   9649  C  CB    . CYS   B  1  105  ? -0.228  43.285  115.449 1.00 21.98 ? 103  CYS   B CB    1 
ATOM   9650  S  SG    . CYS   B  1  105  ? -0.832  42.667  113.899 1.00 21.93 ? 103  CYS   B SG    1 
ATOM   9651  N  N     . LEU   B  1  106  ? -0.260  43.948  118.481 1.00 21.62 ? 104  LEU   B N     1 
ATOM   9652  C  CA    . LEU   B  1  106  ? 0.396   44.409  119.693 1.00 21.70 ? 104  LEU   B CA    1 
ATOM   9653  C  C     . LEU   B  1  106  ? 0.321   43.347  120.774 1.00 22.40 ? 104  LEU   B C     1 
ATOM   9654  O  O     . LEU   B  1  106  ? 1.310   43.085  121.473 1.00 24.09 ? 104  LEU   B O     1 
ATOM   9655  C  CB    . LEU   B  1  106  ? -0.246  45.703  120.185 1.00 22.07 ? 104  LEU   B CB    1 
ATOM   9656  C  CG    . LEU   B  1  106  ? 0.281   46.180  121.544 1.00 22.67 ? 104  LEU   B CG    1 
ATOM   9657  C  CD1   . LEU   B  1  106  ? 1.706   46.672  121.420 1.00 28.39 ? 104  LEU   B CD1   1 
ATOM   9658  C  CD2   . LEU   B  1  106  ? -0.615  47.250  122.150 1.00 24.51 ? 104  LEU   B CD2   1 
ATOM   9659  N  N     . ALA   B  1  107  ? -0.849  42.724  120.924 1.00 23.67 ? 105  ALA   B N     1 
ATOM   9660  C  CA    . ALA   B  1  107  ? -1.019  41.707  121.954 1.00 22.69 ? 105  ALA   B CA    1 
ATOM   9661  C  C     . ALA   B  1  107  ? -0.105  40.519  121.693 1.00 26.52 ? 105  ALA   B C     1 
ATOM   9662  O  O     . ALA   B  1  107  ? 0.530   40.003  122.622 1.00 27.98 ? 105  ALA   B O     1 
ATOM   9663  C  CB    . ALA   B  1  107  ? -2.478  41.264  121.993 1.00 24.30 ? 105  ALA   B CB    1 
ATOM   9664  N  N     . GLU   B  1  108  ? -0.021  40.083  120.434 1.00 24.84 ? 106  GLU   B N     1 
ATOM   9665  C  CA    . GLU   B  1  108  ? 0.894   39.013  120.057 1.00 26.69 ? 106  GLU   B CA    1 
ATOM   9666  C  C     . GLU   B  1  108  ? 2.316   39.345  120.481 1.00 28.11 ? 106  GLU   B C     1 
ATOM   9667  O  O     . GLU   B  1  108  ? 3.016   38.510  121.062 1.00 27.82 ? 106  GLU   B O     1 
ATOM   9668  C  CB    . GLU   B  1  108  ? 0.834   38.801  118.545 1.00 26.19 ? 106  GLU   B CB    1 
ATOM   9669  C  CG    . GLU   B  1  108  ? 1.922   37.880  118.000 1.00 27.65 ? 106  GLU   B CG    1 
ATOM   9670  C  CD    . GLU   B  1  108  ? 2.024   37.926  116.484 1.00 32.75 ? 106  GLU   B CD    1 
ATOM   9671  O  OE1   . GLU   B  1  108  ? 1.073   38.407  115.835 1.00 30.14 ? 106  GLU   B OE1   1 
ATOM   9672  O  OE2   . GLU   B  1  108  ? 3.066   37.496  115.936 1.00 35.34 ? 106  GLU   B OE2   1 
ATOM   9673  N  N     . ALA   B  1  109  ? 2.757   40.572  120.202 1.00 25.79 ? 107  ALA   B N     1 
ATOM   9674  C  CA    . ALA   B  1  109  ? 4.117   40.962  120.553 1.00 26.57 ? 107  ALA   B CA    1 
ATOM   9675  C  C     . ALA   B  1  109  ? 4.305   40.995  122.062 1.00 26.33 ? 107  ALA   B C     1 
ATOM   9676  O  O     . ALA   B  1  109  ? 5.337   40.549  122.578 1.00 27.06 ? 107  ALA   B O     1 
ATOM   9677  C  CB    . ALA   B  1  109  ? 4.452   42.316  119.928 1.00 29.41 ? 107  ALA   B CB    1 
ATOM   9678  N  N     . LEU   B  1  110  ? 3.313   41.511  122.791 1.00 24.80 ? 108  LEU   B N     1 
ATOM   9679  C  CA    . LEU   B  1  110  ? 3.420   41.553  124.243 1.00 24.33 ? 108  LEU   B CA    1 
ATOM   9680  C  C     . LEU   B  1  110  ? 3.455   40.157  124.843 1.00 27.93 ? 108  LEU   B C     1 
ATOM   9681  O  O     . LEU   B  1  110  ? 4.090   39.945  125.887 1.00 29.66 ? 108  LEU   B O     1 
ATOM   9682  C  CB    . LEU   B  1  110  ? 2.254   42.353  124.828 1.00 25.81 ? 108  LEU   B CB    1 
ATOM   9683  C  CG    . LEU   B  1  110  ? 2.369   43.858  124.585 1.00 26.05 ? 108  LEU   B CG    1 
ATOM   9684  C  CD1   . LEU   B  1  110  ? 1.055   44.547  124.917 1.00 26.31 ? 108  LEU   B CD1   1 
ATOM   9685  C  CD2   . LEU   B  1  110  ? 3.509   44.437  125.422 1.00 30.61 ? 108  LEU   B CD2   1 
ATOM   9686  N  N     . LEU   B  1  111  ? 2.786   39.196  124.206 1.00 28.12 ? 109  LEU   B N     1 
ATOM   9687  C  CA    . LEU   B  1  111  ? 2.785   37.829  124.708 1.00 31.28 ? 109  LEU   B CA    1 
ATOM   9688  C  C     . LEU   B  1  111  ? 4.108   37.117  124.477 1.00 33.95 ? 109  LEU   B C     1 
ATOM   9689  O  O     . LEU   B  1  111  ? 4.340   36.071  125.092 1.00 34.67 ? 109  LEU   B O     1 
ATOM   9690  C  CB    . LEU   B  1  111  ? 1.644   37.032  124.086 1.00 32.25 ? 109  LEU   B CB    1 
ATOM   9691  C  CG    . LEU   B  1  111  ? 0.268   37.417  124.621 1.00 27.92 ? 109  LEU   B CG    1 
ATOM   9692  C  CD1   . LEU   B  1  111  ? -0.801  36.732  123.805 1.00 33.86 ? 109  LEU   B CD1   1 
ATOM   9693  C  CD2   . LEU   B  1  111  ? 0.133   37.064  126.094 1.00 35.30 ? 109  LEU   B CD2   1 
ATOM   9694  N  N     . ARG   B  1  112  ? 4.971   37.646  123.610 1.00 30.93 ? 110  ARG   B N     1 
ATOM   9695  C  CA    . ARG   B  1  112  ? 6.323   37.115  123.501 1.00 34.84 ? 110  ARG   B CA    1 
ATOM   9696  C  C     . ARG   B  1  112  ? 7.179   37.478  124.704 1.00 35.79 ? 110  ARG   B C     1 
ATOM   9697  O  O     . ARG   B  1  112  ? 8.268   36.919  124.862 1.00 36.27 ? 110  ARG   B O     1 
ATOM   9698  C  CB    . ARG   B  1  112  ? 6.980   37.566  122.195 1.00 32.92 ? 110  ARG   B CB    1 
ATOM   9699  C  CG    . ARG   B  1  112  ? 6.291   37.020  120.955 1.00 37.12 ? 110  ARG   B CG    1 
ATOM   9700  C  CD    . ARG   B  1  112  ? 7.115   37.223  119.692 1.00 43.12 ? 110  ARG   B CD    1 
ATOM   9701  N  NE    . ARG   B  1  112  ? 7.013   38.578  119.164 1.00 41.80 ? 110  ARG   B NE    1 
ATOM   9702  C  CZ    . ARG   B  1  112  ? 6.170   38.951  118.209 1.00 40.94 ? 110  ARG   B CZ    1 
ATOM   9703  N  NH1   . ARG   B  1  112  ? 5.324   38.093  117.660 1.00 44.91 ? 110  ARG   B NH1   1 
ATOM   9704  N  NH2   . ARG   B  1  112  ? 6.177   40.215  117.793 1.00 41.69 ? 110  ARG   B NH2   1 
ATOM   9705  N  N     . ILE   B  1  113  ? 6.719   38.396  125.547 1.00 33.56 ? 111  ILE   B N     1 
ATOM   9706  C  CA    . ILE   B  1  113  ? 7.341   38.627  126.845 1.00 35.37 ? 111  ILE   B CA    1 
ATOM   9707  C  C     . ILE   B  1  113  ? 6.791   37.559  127.781 1.00 36.61 ? 111  ILE   B C     1 
ATOM   9708  O  O     . ILE   B  1  113  ? 5.610   37.608  128.153 1.00 38.61 ? 111  ILE   B O     1 
ATOM   9709  C  CB    . ILE   B  1  113  ? 7.050   40.042  127.364 1.00 34.28 ? 111  ILE   B CB    1 
ATOM   9710  C  CG1   . ILE   B  1  113  ? 7.553   41.086  126.366 1.00 34.27 ? 111  ILE   B CG1   1 
ATOM   9711  C  CG2   . ILE   B  1  113  ? 7.674   40.243  128.747 1.00 37.01 ? 111  ILE   B CG2   1 
ATOM   9712  C  CD1   . ILE   B  1  113  ? 7.110   42.499  126.690 1.00 34.45 ? 111  ILE   B CD1   1 
ATOM   9713  N  N     . PRO   B  1  114  ? 7.600   36.573  128.177 1.00 41.65 ? 112  PRO   B N     1 
ATOM   9714  C  CA    . PRO   B  1  114  ? 7.049   35.449  128.951 1.00 41.35 ? 112  PRO   B CA    1 
ATOM   9715  C  C     . PRO   B  1  114  ? 6.661   35.809  130.374 1.00 37.43 ? 112  PRO   B C     1 
ATOM   9716  O  O     . PRO   B  1  114  ? 5.705   35.233  130.908 1.00 41.29 ? 112  PRO   B O     1 
ATOM   9717  C  CB    . PRO   B  1  114  ? 8.176   34.406  128.907 1.00 37.76 ? 112  PRO   B CB    1 
ATOM   9718  C  CG    . PRO   B  1  114  ? 9.413   35.206  128.692 1.00 39.36 ? 112  PRO   B CG    1 
ATOM   9719  C  CD    . PRO   B  1  114  ? 9.022   36.381  127.844 1.00 38.41 ? 112  PRO   B CD    1 
ATOM   9720  N  N     . ASP   B  1  115  ? 7.363   36.746  131.004 1.00 40.73 ? 113  ASP   B N     1 
ATOM   9721  C  CA    . ASP   B  1  115  ? 7.118   37.079  132.402 1.00 44.30 ? 113  ASP   B CA    1 
ATOM   9722  C  C     . ASP   B  1  115  ? 5.959   38.063  132.503 1.00 42.99 ? 113  ASP   B C     1 
ATOM   9723  O  O     . ASP   B  1  115  ? 6.042   39.182  131.984 1.00 42.80 ? 113  ASP   B O     1 
ATOM   9724  C  CB    . ASP   B  1  115  ? 8.382   37.672  133.020 1.00 42.12 ? 113  ASP   B CB    1 
ATOM   9725  C  CG    . ASP   B  1  115  ? 8.156   38.191  134.425 1.00 47.19 ? 113  ASP   B CG    1 
ATOM   9726  O  OD1   . ASP   B  1  115  ? 7.672   37.418  135.280 1.00 53.15 ? 113  ASP   B OD1   1 
ATOM   9727  O  OD2   . ASP   B  1  115  ? 8.468   39.373  134.677 1.00 48.07 ? 113  ASP   B OD2   1 
ATOM   9728  N  N     . THR   B  1  116  ? 4.885   37.646  133.180 1.00 43.88 ? 114  THR   B N     1 
ATOM   9729  C  CA    . THR   B  1  116  ? 3.707   38.499  133.327 1.00 44.70 ? 114  THR   B CA    1 
ATOM   9730  C  C     . THR   B  1  116  ? 4.067   39.848  133.938 1.00 45.89 ? 114  THR   B C     1 
ATOM   9731  O  O     . THR   B  1  116  ? 3.599   40.894  133.473 1.00 41.61 ? 114  THR   B O     1 
ATOM   9732  C  CB    . THR   B  1  116  ? 2.651   37.788  134.177 1.00 48.82 ? 114  THR   B CB    1 
ATOM   9733  O  OG1   . THR   B  1  116  ? 2.168   36.634  133.478 1.00 54.48 ? 114  THR   B OG1   1 
ATOM   9734  C  CG2   . THR   B  1  116  ? 1.484   38.718  134.482 1.00 49.21 ? 114  THR   B CG2   1 
ATOM   9735  N  N     . ALA   B  1  117  ? 4.902   39.845  134.979 1.00 48.81 ? 115  ALA   B N     1 
ATOM   9736  C  CA    . ALA   B  1  117  ? 5.267   41.092  135.642 1.00 47.26 ? 115  ALA   B CA    1 
ATOM   9737  C  C     . ALA   B  1  117  ? 5.934   42.056  134.670 1.00 41.87 ? 115  ALA   B C     1 
ATOM   9738  O  O     . ALA   B  1  117  ? 5.566   43.234  134.598 1.00 45.47 ? 115  ALA   B O     1 
ATOM   9739  C  CB    . ALA   B  1  117  ? 6.186   40.801  136.828 1.00 45.24 ? 115  ALA   B CB    1 
ATOM   9740  N  N     . THR   B  1  118  ? 6.927   41.572  133.919 1.00 42.64 ? 116  THR   B N     1 
ATOM   9741  C  CA    . THR   B  1  118  ? 7.623   42.430  132.968 1.00 41.45 ? 116  THR   B CA    1 
ATOM   9742  C  C     . THR   B  1  118  ? 6.670   42.939  131.896 1.00 40.75 ? 116  THR   B C     1 
ATOM   9743  O  O     . THR   B  1  118  ? 6.732   44.110  131.504 1.00 40.97 ? 116  THR   B O     1 
ATOM   9744  C  CB    . THR   B  1  118  ? 8.781   41.666  132.327 1.00 41.32 ? 116  THR   B CB    1 
ATOM   9745  O  OG1   . THR   B  1  118  ? 9.681   41.216  133.347 1.00 45.15 ? 116  THR   B OG1   1 
ATOM   9746  C  CG2   . THR   B  1  118  ? 9.535   42.557  131.354 1.00 40.40 ? 116  THR   B CG2   1 
ATOM   9747  N  N     . ARG   B  1  119  ? 5.776   42.070  131.420 1.00 39.16 ? 117  ARG   B N     1 
ATOM   9748  C  CA    . ARG   B  1  119  ? 4.822   42.465  130.389 1.00 37.15 ? 117  ARG   B CA    1 
ATOM   9749  C  C     . ARG   B  1  119  ? 3.860   43.525  130.908 1.00 38.10 ? 117  ARG   B C     1 
ATOM   9750  O  O     . ARG   B  1  119  ? 3.661   44.564  130.268 1.00 35.91 ? 117  ARG   B O     1 
ATOM   9751  C  CB    . ARG   B  1  119  ? 4.049   41.242  129.902 1.00 37.61 ? 117  ARG   B CB    1 
ATOM   9752  C  CG    . ARG   B  1  119  ? 3.120   41.540  128.737 1.00 32.96 ? 117  ARG   B CG    1 
ATOM   9753  C  CD    . ARG   B  1  119  ? 2.175   40.393  128.467 1.00 34.23 ? 117  ARG   B CD    1 
ATOM   9754  N  NE    . ARG   B  1  119  ? 2.872   39.114  128.410 1.00 36.58 ? 117  ARG   B NE    1 
ATOM   9755  C  CZ    . ARG   B  1  119  ? 2.523   38.044  129.112 1.00 41.08 ? 117  ARG   B CZ    1 
ATOM   9756  N  NH1   . ARG   B  1  119  ? 1.451   38.045  129.886 1.00 35.62 ? 117  ARG   B NH1   1 
ATOM   9757  N  NH2   . ARG   B  1  119  ? 3.261   36.941  129.024 1.00 42.75 ? 117  ARG   B NH2   1 
ATOM   9758  N  N     . ASP   B  1  120  ? 3.253   43.279  132.071 1.00 38.06 ? 118  ASP   B N     1 
ATOM   9759  C  CA    . ASP   B  1  120  ? 2.314   44.245  132.633 1.00 37.61 ? 118  ASP   B CA    1 
ATOM   9760  C  C     . ASP   B  1  120  ? 2.996   45.563  132.970 1.00 39.01 ? 118  ASP   B C     1 
ATOM   9761  O  O     . ASP   B  1  120  ? 2.372   46.624  132.866 1.00 39.01 ? 118  ASP   B O     1 
ATOM   9762  C  CB    . ASP   B  1  120  ? 1.611   43.654  133.854 1.00 39.98 ? 118  ASP   B CB    1 
ATOM   9763  C  CG    . ASP   B  1  120  ? 0.670   42.519  133.488 1.00 45.55 ? 118  ASP   B CG    1 
ATOM   9764  O  OD1   . ASP   B  1  120  ? 0.395   42.337  132.281 1.00 47.34 ? 118  ASP   B OD1   1 
ATOM   9765  O  OD2   . ASP   B  1  120  ? 0.212   41.801  134.402 1.00 48.66 ? 118  ASP   B OD2   1 
ATOM   9766  N  N     . ALA   B  1  121  ? 4.273   45.522  133.358 1.00 39.90 ? 119  ALA   B N     1 
ATOM   9767  C  CA    . ALA   B  1  121  ? 5.003   46.760  133.616 1.00 43.39 ? 119  ALA   B CA    1 
ATOM   9768  C  C     . ALA   B  1  121  ? 5.202   47.553  132.332 1.00 39.37 ? 119  ALA   B C     1 
ATOM   9769  O  O     . ALA   B  1  121  ? 4.987   48.770  132.304 1.00 39.84 ? 119  ALA   B O     1 
ATOM   9770  C  CB    . ALA   B  1  121  ? 6.345   46.457  134.284 1.00 42.29 ? 119  ALA   B CB    1 
ATOM   9771  N  N     . LEU   B  1  122  ? 5.611   46.878  131.254 1.00 37.56 ? 120  LEU   B N     1 
ATOM   9772  C  CA    . LEU   B  1  122  ? 5.790   47.565  129.980 1.00 38.67 ? 120  LEU   B CA    1 
ATOM   9773  C  C     . LEU   B  1  122  ? 4.475   48.163  129.495 1.00 35.83 ? 120  LEU   B C     1 
ATOM   9774  O  O     . LEU   B  1  122  ? 4.448   49.277  128.961 1.00 38.57 ? 120  LEU   B O     1 
ATOM   9775  C  CB    . LEU   B  1  122  ? 6.357   46.599  128.941 1.00 36.70 ? 120  LEU   B CB    1 
ATOM   9776  C  CG    . LEU   B  1  122  ? 6.719   47.205  127.586 1.00 39.59 ? 120  LEU   B CG    1 
ATOM   9777  C  CD1   . LEU   B  1  122  ? 7.955   48.088  127.711 1.00 38.86 ? 120  LEU   B CD1   1 
ATOM   9778  C  CD2   . LEU   B  1  122  ? 6.930   46.119  126.549 1.00 36.47 ? 120  LEU   B CD2   1 
ATOM   9779  N  N     . ILE   B  1  123  ? 3.373   47.436  129.688 1.00 34.07 ? 121  ILE   B N     1 
ATOM   9780  C  CA    . ILE   B  1  123  ? 2.058   47.931  129.286 1.00 34.51 ? 121  ILE   B CA    1 
ATOM   9781  C  C     . ILE   B  1  123  ? 1.714   49.207  130.044 1.00 41.93 ? 121  ILE   B C     1 
ATOM   9782  O  O     . ILE   B  1  123  ? 1.375   50.235  129.443 1.00 40.44 ? 121  ILE   B O     1 
ATOM   9783  C  CB    . ILE   B  1  123  ? 0.992   46.839  129.493 1.00 32.89 ? 121  ILE   B CB    1 
ATOM   9784  C  CG1   . ILE   B  1  123  ? 1.216   45.684  128.519 1.00 29.94 ? 121  ILE   B CG1   1 
ATOM   9785  C  CG2   . ILE   B  1  123  ? -0.411  47.413  129.334 1.00 35.06 ? 121  ILE   B CG2   1 
ATOM   9786  C  CD1   . ILE   B  1  123  ? 0.319   44.506  128.773 1.00 28.20 ? 121  ILE   B CD1   1 
ATOM   9787  N  N     . ARG   B  1  124  ? 1.807   49.164  131.376 1.00 38.93 ? 122  ARG   B N     1 
ATOM   9788  C  CA    . ARG   B  1  124  ? 1.370   50.296  132.187 1.00 40.82 ? 122  ARG   B CA    1 
ATOM   9789  C  C     . ARG   B  1  124  ? 2.321   51.481  132.061 1.00 45.07 ? 122  ARG   B C     1 
ATOM   9790  O  O     . ARG   B  1  124  ? 1.879   52.635  132.033 1.00 50.51 ? 122  ARG   B O     1 
ATOM   9791  C  CB    . ARG   B  1  124  ? 1.218   49.871  133.649 1.00 45.52 ? 122  ARG   B CB    1 
ATOM   9792  N  N     . ASP   B  1  125  ? 3.626   51.222  131.974 1.00 45.43 ? 123  ASP   B N     1 
ATOM   9793  C  CA    . ASP   B  1  125  ? 4.620   52.288  132.025 1.00 48.77 ? 123  ASP   B CA    1 
ATOM   9794  C  C     . ASP   B  1  125  ? 5.075   52.782  130.660 1.00 48.87 ? 123  ASP   B C     1 
ATOM   9795  O  O     . ASP   B  1  125  ? 5.479   53.943  130.542 1.00 49.61 ? 123  ASP   B O     1 
ATOM   9796  C  CB    . ASP   B  1  125  ? 5.850   51.839  132.822 1.00 54.06 ? 123  ASP   B CB    1 
ATOM   9797  C  CG    . ASP   B  1  125  ? 5.492   51.284  134.185 1.00 57.23 ? 123  ASP   B CG    1 
ATOM   9798  O  OD1   . ASP   B  1  125  ? 4.434   51.666  134.730 1.00 55.73 ? 123  ASP   B OD1   1 
ATOM   9799  O  OD2   . ASP   B  1  125  ? 6.272   50.460  134.710 1.00 62.41 ? 123  ASP   B OD2   1 
ATOM   9800  N  N     . LYS   B  1  126  ? 5.027   51.948  129.627 1.00 45.43 ? 124  LYS   B N     1 
ATOM   9801  C  CA    . LYS   B  1  126  ? 5.563   52.340  128.329 1.00 43.81 ? 124  LYS   B CA    1 
ATOM   9802  C  C     . LYS   B  1  126  ? 4.548   52.291  127.198 1.00 44.88 ? 124  LYS   B C     1 
ATOM   9803  O  O     . LYS   B  1  126  ? 4.543   53.186  126.351 1.00 48.14 ? 124  LYS   B O     1 
ATOM   9804  C  CB    . LYS   B  1  126  ? 6.783   51.479  127.968 1.00 45.54 ? 124  LYS   B CB    1 
ATOM   9805  N  N     . ILE   B  1  127  ? 3.689   51.272  127.150 1.00 41.29 ? 125  ILE   B N     1 
ATOM   9806  C  CA    . ILE   B  1  127  ? 2.798   51.123  126.002 1.00 39.17 ? 125  ILE   B CA    1 
ATOM   9807  C  C     . ILE   B  1  127  ? 1.561   52.003  126.144 1.00 41.07 ? 125  ILE   B C     1 
ATOM   9808  O  O     . ILE   B  1  127  ? 1.140   52.657  125.183 1.00 41.52 ? 125  ILE   B O     1 
ATOM   9809  C  CB    . ILE   B  1  127  ? 2.429   49.646  125.772 1.00 34.53 ? 125  ILE   B CB    1 
ATOM   9810  C  CG1   . ILE   B  1  127  ? 3.681   48.762  125.767 1.00 37.21 ? 125  ILE   B CG1   1 
ATOM   9811  C  CG2   . ILE   B  1  127  ? 1.662   49.493  124.463 1.00 36.20 ? 125  ILE   B CG2   1 
ATOM   9812  C  CD1   . ILE   B  1  127  ? 4.672   49.122  124.695 1.00 40.16 ? 125  ILE   B CD1   1 
ATOM   9813  N  N     . ALA   B  1  128  ? 0.951   52.025  127.331 1.00 38.25 ? 126  ALA   B N     1 
ATOM   9814  C  CA    . ALA   B  1  128  ? -0.303  52.754  127.499 1.00 38.36 ? 126  ALA   B CA    1 
ATOM   9815  C  C     . ALA   B  1  128  ? -0.120  54.253  127.315 1.00 43.44 ? 126  ALA   B C     1 
ATOM   9816  O  O     . ALA   B  1  128  ? -1.078  54.957  126.981 1.00 43.77 ? 126  ALA   B O     1 
ATOM   9817  C  CB    . ALA   B  1  128  ? -0.914  52.453  128.865 1.00 37.51 ? 126  ALA   B CB    1 
ATOM   9818  N  N     . ASP   B  1  129  ? 1.088   54.759  127.535 1.00 44.31 ? 127  ASP   B N     1 
ATOM   9819  C  CA    . ASP   B  1  129  ? 1.388   56.169  127.301 1.00 52.72 ? 127  ASP   B CA    1 
ATOM   9820  C  C     . ASP   B  1  129  ? 1.902   56.413  125.891 1.00 55.67 ? 127  ASP   B C     1 
ATOM   9821  O  O     . ASP   B  1  129  ? 2.848   57.182  125.692 1.00 62.90 ? 127  ASP   B O     1 
ATOM   9822  C  CB    . ASP   B  1  129  ? 2.379   56.672  128.347 1.00 52.92 ? 127  ASP   B CB    1 
ATOM   9823  N  N     . GLY   B  1  130  ? 1.295   55.770  124.894 1.00 58.48 ? 128  GLY   B N     1 
ATOM   9824  C  CA    . GLY   B  1  130  ? 1.758   55.866  123.526 1.00 59.00 ? 128  GLY   B CA    1 
ATOM   9825  C  C     . GLY   B  1  130  ? 3.196   55.380  123.412 1.00 63.85 ? 128  GLY   B C     1 
ATOM   9826  O  O     . GLY   B  1  130  ? 3.694   54.606  124.233 1.00 65.93 ? 128  GLY   B O     1 
ATOM   9827  N  N     . ASN   B  1  131  ? 3.868   55.859  122.365 1.00 64.31 ? 129  ASN   B N     1 
ATOM   9828  C  CA    . ASN   B  1  131  ? 5.280   55.549  122.130 1.00 62.34 ? 129  ASN   B CA    1 
ATOM   9829  C  C     . ASN   B  1  131  ? 5.543   54.046  122.103 1.00 58.47 ? 129  ASN   B C     1 
ATOM   9830  O  O     . ASN   B  1  131  ? 6.645   53.591  122.420 1.00 58.08 ? 129  ASN   B O     1 
ATOM   9831  C  CB    . ASN   B  1  131  ? 6.200   56.257  123.130 1.00 65.49 ? 129  ASN   B CB    1 
ATOM   9832  N  N     . TRP   B  1  132  ? 4.520   53.267  121.738 1.00 52.27 ? 130  TRP   B N     1 
ATOM   9833  C  CA    . TRP   B  1  132  ? 4.684   51.829  121.568 1.00 43.96 ? 130  TRP   B CA    1 
ATOM   9834  C  C     . TRP   B  1  132  ? 5.744   51.495  120.528 1.00 46.93 ? 130  TRP   B C     1 
ATOM   9835  O  O     . TRP   B  1  132  ? 6.291   50.387  120.549 1.00 50.76 ? 130  TRP   B O     1 
ATOM   9836  C  CB    . TRP   B  1  132  ? 3.347   51.209  121.149 1.00 39.17 ? 130  TRP   B CB    1 
ATOM   9837  C  CG    . TRP   B  1  132  ? 2.812   51.773  119.853 1.00 32.40 ? 130  TRP   B CG    1 
ATOM   9838  C  CD1   . TRP   B  1  132  ? 1.931   52.807  119.708 1.00 32.64 ? 130  TRP   B CD1   1 
ATOM   9839  C  CD2   . TRP   B  1  132  ? 3.141   51.339  118.529 1.00 31.32 ? 130  TRP   B CD2   1 
ATOM   9840  N  NE1   . TRP   B  1  132  ? 1.686   53.038  118.373 1.00 31.35 ? 130  TRP   B NE1   1 
ATOM   9841  C  CE2   . TRP   B  1  132  ? 2.420   52.151  117.630 1.00 28.41 ? 130  TRP   B CE2   1 
ATOM   9842  C  CE3   . TRP   B  1  132  ? 3.973   50.340  118.017 1.00 31.38 ? 130  TRP   B CE3   1 
ATOM   9843  C  CZ2   . TRP   B  1  132  ? 2.511   51.993  116.250 1.00 26.67 ? 130  TRP   B CZ2   1 
ATOM   9844  C  CZ3   . TRP   B  1  132  ? 4.058   50.187  116.649 1.00 27.82 ? 130  TRP   B CZ3   1 
ATOM   9845  C  CH2   . TRP   B  1  132  ? 3.331   51.007  115.782 1.00 28.29 ? 130  TRP   B CH2   1 
ATOM   9846  N  N     . LYS   B  1  133  ? 6.034   52.421  119.610 1.00 47.40 ? 131  LYS   B N     1 
ATOM   9847  C  CA    . LYS   B  1  133  ? 7.020   52.154  118.568 1.00 48.32 ? 131  LYS   B CA    1 
ATOM   9848  C  C     . LYS   B  1  133  ? 8.415   51.995  119.162 1.00 58.20 ? 131  LYS   B C     1 
ATOM   9849  O  O     . LYS   B  1  133  ? 9.143   51.054  118.822 1.00 58.81 ? 131  LYS   B O     1 
ATOM   9850  C  CB    . LYS   B  1  133  ? 6.993   53.273  117.526 1.00 46.97 ? 131  LYS   B CB    1 
ATOM   9851  N  N     . SER   B  1  134  ? 8.799   52.902  120.061 1.00 61.42 ? 132  SER   B N     1 
ATOM   9852  C  CA    . SER   B  1  134  ? 10.093  52.820  120.729 1.00 60.10 ? 132  SER   B CA    1 
ATOM   9853  C  C     . SER   B  1  134  ? 10.067  51.741  121.805 1.00 61.29 ? 132  SER   B C     1 
ATOM   9854  O  O     . SER   B  1  134  ? 10.397  52.000  122.967 1.00 67.29 ? 132  SER   B O     1 
ATOM   9855  C  CB    . SER   B  1  134  ? 10.470  54.175  121.330 1.00 57.06 ? 132  SER   B CB    1 
ATOM   9856  N  N     . HIS   B  1  135  ? 9.674   50.531  121.413 1.00 58.88 ? 133  HIS   B N     1 
ATOM   9857  C  CA    . HIS   B  1  135  ? 9.556   49.344  122.249 1.00 59.88 ? 133  HIS   B CA    1 
ATOM   9858  C  C     . HIS   B  1  135  ? 9.020   48.241  121.349 1.00 62.55 ? 133  HIS   B C     1 
ATOM   9859  O  O     . HIS   B  1  135  ? 8.445   48.515  120.290 1.00 62.51 ? 133  HIS   B O     1 
ATOM   9860  C  CB    . HIS   B  1  135  ? 8.611   49.558  123.438 1.00 55.65 ? 133  HIS   B CB    1 
ATOM   9861  N  N     . LEU   B  1  136  ? 9.224   46.997  121.772 1.00 62.94 ? 134  LEU   B N     1 
ATOM   9862  C  CA    . LEU   B  1  136  ? 8.764   45.834  121.008 1.00 60.02 ? 134  LEU   B CA    1 
ATOM   9863  C  C     . LEU   B  1  136  ? 9.360   45.794  119.601 1.00 58.09 ? 134  LEU   B C     1 
ATOM   9864  O  O     . LEU   B  1  136  ? 8.725   46.214  118.633 1.00 53.26 ? 134  LEU   B O     1 
ATOM   9865  C  CB    . LEU   B  1  136  ? 7.233   45.802  120.942 1.00 50.48 ? 134  LEU   B CB    1 
ATOM   9866  C  CG    . LEU   B  1  136  ? 6.557   45.896  122.308 1.00 47.05 ? 134  LEU   B CG    1 
ATOM   9867  C  CD1   . LEU   B  1  136  ? 5.056   45.944  122.163 1.00 42.81 ? 134  LEU   B CD1   1 
ATOM   9868  C  CD2   . LEU   B  1  136  ? 6.976   44.719  123.172 1.00 47.02 ? 134  LEU   B CD2   1 
ATOM   9869  N  N     . ARG   B  1  140  ? 11.930  44.349  114.071 1.00 41.62 ? 138  ARG   B N     1 
ATOM   9870  C  CA    . ARG   B  1  140  ? 10.869  43.653  113.350 1.00 43.54 ? 138  ARG   B CA    1 
ATOM   9871  C  C     . ARG   B  1  140  ? 9.529   44.349  113.561 1.00 42.32 ? 138  ARG   B C     1 
ATOM   9872  O  O     . ARG   B  1  140  ? 9.166   44.687  114.689 1.00 35.39 ? 138  ARG   B O     1 
ATOM   9873  C  CB    . ARG   B  1  140  ? 10.777  42.187  113.789 1.00 42.52 ? 138  ARG   B CB    1 
ATOM   9874  N  N     . SER   B  1  141  ? 8.802   44.559  112.464 1.00 35.57 ? 139  SER   B N     1 
ATOM   9875  C  CA    . SER   B  1  141  ? 7.522   45.243  112.538 1.00 29.70 ? 139  SER   B CA    1 
ATOM   9876  C  C     . SER   B  1  141  ? 6.593   44.520  113.503 1.00 30.74 ? 139  SER   B C     1 
ATOM   9877  O  O     . SER   B  1  141  ? 6.555   43.288  113.566 1.00 30.75 ? 139  SER   B O     1 
ATOM   9878  C  CB    . SER   B  1  141  ? 6.880   45.295  111.151 1.00 30.24 ? 139  SER   B CB    1 
ATOM   9879  O  OG    . SER   B  1  141  ? 5.560   45.825  111.213 1.00 30.09 ? 139  SER   B OG    1 
ATOM   9880  N  N     . LEU   B  1  142  ? 5.849   45.301  114.276 1.00 27.28 ? 140  LEU   B N     1 
ATOM   9881  C  CA    . LEU   B  1  142  ? 4.799   44.722  115.094 1.00 25.97 ? 140  LEU   B CA    1 
ATOM   9882  C  C     . LEU   B  1  142  ? 3.780   43.983  114.244 1.00 22.23 ? 140  LEU   B C     1 
ATOM   9883  O  O     . LEU   B  1  142  ? 3.066   43.111  114.750 1.00 23.01 ? 140  LEU   B O     1 
ATOM   9884  C  CB    . LEU   B  1  142  ? 4.072   45.856  115.807 1.00 24.54 ? 140  LEU   B CB    1 
ATOM   9885  C  CG    . LEU   B  1  142  ? 3.523   45.501  117.173 1.00 30.05 ? 140  LEU   B CG    1 
ATOM   9886  C  CD1   . LEU   B  1  142  ? 4.673   45.372  118.129 1.00 33.87 ? 140  LEU   B CD1   1 
ATOM   9887  C  CD2   . LEU   B  1  142  ? 2.577   46.572  117.633 1.00 30.13 ? 140  LEU   B CD2   1 
ATOM   9888  N  N     . PHE   B  1  143  ? 3.695   44.316  112.960 1.00 22.46 ? 141  PHE   B N     1 
ATOM   9889  C  CA    . PHE   B  1  143  ? 2.585   43.905  112.121 1.00 21.02 ? 141  PHE   B CA    1 
ATOM   9890  C  C     . PHE   B  1  143  ? 2.950   42.779  111.164 1.00 24.41 ? 141  PHE   B C     1 
ATOM   9891  O  O     . PHE   B  1  143  ? 2.212   42.522  110.209 1.00 22.65 ? 141  PHE   B O     1 
ATOM   9892  C  CB    . PHE   B  1  143  ? 2.037   45.127  111.388 1.00 21.89 ? 141  PHE   B CB    1 
ATOM   9893  C  CG    . PHE   B  1  143  ? 1.726   46.265  112.304 1.00 21.14 ? 141  PHE   B CG    1 
ATOM   9894  C  CD1   . PHE   B  1  143  ? 0.798   46.102  113.319 1.00 21.45 ? 141  PHE   B CD1   1 
ATOM   9895  C  CD2   . PHE   B  1  143  ? 2.353   47.495  112.168 1.00 20.18 ? 141  PHE   B CD2   1 
ATOM   9896  C  CE1   . PHE   B  1  143  ? 0.502   47.131  114.173 1.00 20.81 ? 141  PHE   B CE1   1 
ATOM   9897  C  CE2   . PHE   B  1  143  ? 2.063   48.535  113.034 1.00 20.53 ? 141  PHE   B CE2   1 
ATOM   9898  C  CZ    . PHE   B  1  143  ? 1.127   48.356  114.027 1.00 19.91 ? 141  PHE   B CZ    1 
ATOM   9899  N  N     . VAL   B  1  144  ? 4.058   42.078  111.431 1.00 23.58 ? 142  VAL   B N     1 
ATOM   9900  C  CA    . VAL   B  1  144  ? 4.507   40.980  110.575 1.00 23.97 ? 142  VAL   B CA    1 
ATOM   9901  C  C     . VAL   B  1  144  ? 3.397   39.967  110.321 1.00 24.21 ? 142  VAL   B C     1 
ATOM   9902  O  O     . VAL   B  1  144  ? 3.253   39.459  109.203 1.00 23.10 ? 142  VAL   B O     1 
ATOM   9903  C  CB    . VAL   B  1  144  ? 5.775   40.329  111.162 1.00 24.27 ? 142  VAL   B CB    1 
ATOM   9904  C  CG1   . VAL   B  1  144  ? 6.131   39.053  110.411 1.00 28.45 ? 142  VAL   B CG1   1 
ATOM   9905  C  CG2   . VAL   B  1  144  ? 6.921   41.309  111.109 1.00 28.41 ? 142  VAL   B CG2   1 
ATOM   9906  N  N     . ASN   B  1  145  ? 2.589   39.659  111.340 1.00 24.48 ? 143  ASN   B N     1 
ATOM   9907  C  CA    . ASN   B  1  145  ? 1.530   38.667  111.201 1.00 24.47 ? 143  ASN   B CA    1 
ATOM   9908  C  C     . ASN   B  1  145  ? 0.151   39.291  111.043 1.00 24.23 ? 143  ASN   B C     1 
ATOM   9909  O  O     . ASN   B  1  145  ? -0.858  38.626  111.298 1.00 24.89 ? 143  ASN   B O     1 
ATOM   9910  C  CB    . ASN   B  1  145  ? 1.548   37.687  112.373 1.00 28.54 ? 143  ASN   B CB    1 
ATOM   9911  C  CG    . ASN   B  1  145  ? 2.673   36.685  112.261 1.00 32.88 ? 143  ASN   B CG    1 
ATOM   9912  O  OD1   . ASN   B  1  145  ? 2.913   36.125  111.188 1.00 35.24 ? 143  ASN   B OD1   1 
ATOM   9913  N  ND2   . ASN   B  1  145  ? 3.373   36.454  113.363 1.00 35.85 ? 143  ASN   B ND2   1 
ATOM   9914  N  N     . ALA   B  1  146  ? 0.086   40.550  110.617 1.00 22.07 ? 144  ALA   B N     1 
ATOM   9915  C  CA    . ALA   B  1  146  ? -1.198  41.239  110.564 1.00 23.23 ? 144  ALA   B CA    1 
ATOM   9916  C  C     . ALA   B  1  146  ? -2.153  40.633  109.539 1.00 23.10 ? 144  ALA   B C     1 
ATOM   9917  O  O     . ALA   B  1  146  ? -3.372  40.771  109.684 1.00 26.46 ? 144  ALA   B O     1 
ATOM   9918  C  CB    . ALA   B  1  146  ? -0.985  42.727  110.296 1.00 23.01 ? 144  ALA   B CB    1 
ATOM   9919  N  N     . ALA   B  1  147  ? -1.644  39.982  108.492 1.00 24.88 ? 145  ALA   B N     1 
ATOM   9920  C  CA    . ALA   B  1  147  ? -2.558  39.337  107.553 1.00 22.24 ? 145  ALA   B CA    1 
ATOM   9921  C  C     . ALA   B  1  147  ? -3.349  38.237  108.245 1.00 26.15 ? 145  ALA   B C     1 
ATOM   9922  O  O     . ALA   B  1  147  ? -4.547  38.058  107.989 1.00 27.70 ? 145  ALA   B O     1 
ATOM   9923  C  CB    . ALA   B  1  147  ? -1.789  38.774  106.361 1.00 25.89 ? 145  ALA   B CB    1 
ATOM   9924  N  N     . THR   B  1  148  ? -2.695  37.508  109.144 1.00 24.95 ? 146  THR   B N     1 
ATOM   9925  C  CA    . THR   B  1  148  ? -3.373  36.470  109.904 1.00 24.50 ? 146  THR   B CA    1 
ATOM   9926  C  C     . THR   B  1  148  ? -4.392  37.079  110.861 1.00 25.11 ? 146  THR   B C     1 
ATOM   9927  O  O     . THR   B  1  148  ? -5.539  36.626  110.934 1.00 27.34 ? 146  THR   B O     1 
ATOM   9928  C  CB    . THR   B  1  148  ? -2.335  35.631  110.649 1.00 33.63 ? 146  THR   B CB    1 
ATOM   9929  O  OG1   . THR   B  1  148  ? -1.471  34.999  109.694 1.00 36.13 ? 146  THR   B OG1   1 
ATOM   9930  C  CG2   . THR   B  1  148  ? -3.011  34.571  111.505 1.00 38.41 ? 146  THR   B CG2   1 
ATOM   9931  N  N     . TRP   B  1  149  ? -4.002  38.126  111.590 1.00 24.37 ? 147  TRP   B N     1 
ATOM   9932  C  CA    . TRP   B  1  149  ? -4.961  38.779  112.468 1.00 23.71 ? 147  TRP   B CA    1 
ATOM   9933  C  C     . TRP   B  1  149  ? -6.064  39.464  111.680 1.00 23.35 ? 147  TRP   B C     1 
ATOM   9934  O  O     . TRP   B  1  149  ? -7.199  39.551  112.164 1.00 24.26 ? 147  TRP   B O     1 
ATOM   9935  C  CB    . TRP   B  1  149  ? -4.269  39.769  113.397 1.00 24.99 ? 147  TRP   B CB    1 
ATOM   9936  C  CG    . TRP   B  1  149  ? -3.395  39.094  114.386 1.00 23.67 ? 147  TRP   B CG    1 
ATOM   9937  C  CD1   . TRP   B  1  149  ? -2.041  39.171  114.462 1.00 25.05 ? 147  TRP   B CD1   1 
ATOM   9938  C  CD2   . TRP   B  1  149  ? -3.810  38.202  115.428 1.00 25.78 ? 147  TRP   B CD2   1 
ATOM   9939  N  NE1   . TRP   B  1  149  ? -1.583  38.400  115.503 1.00 27.60 ? 147  TRP   B NE1   1 
ATOM   9940  C  CE2   . TRP   B  1  149  ? -2.647  37.790  116.108 1.00 27.49 ? 147  TRP   B CE2   1 
ATOM   9941  C  CE3   . TRP   B  1  149  ? -5.051  37.718  115.855 1.00 28.72 ? 147  TRP   B CE3   1 
ATOM   9942  C  CZ2   . TRP   B  1  149  ? -2.686  36.921  117.197 1.00 29.63 ? 147  TRP   B CZ2   1 
ATOM   9943  C  CZ3   . TRP   B  1  149  ? -5.090  36.851  116.941 1.00 30.41 ? 147  TRP   B CZ3   1 
ATOM   9944  C  CH2   . TRP   B  1  149  ? -3.913  36.464  117.599 1.00 32.86 ? 147  TRP   B CH2   1 
ATOM   9945  N  N     . GLY   B  1  150  ? -5.749  39.966  110.484 1.00 24.27 ? 148  GLY   B N     1 
ATOM   9946  C  CA    . GLY   B  1  150  ? -6.793  40.503  109.629 1.00 26.27 ? 148  GLY   B CA    1 
ATOM   9947  C  C     . GLY   B  1  150  ? -7.851  39.466  109.318 1.00 24.44 ? 148  GLY   B C     1 
ATOM   9948  O  O     . GLY   B  1  150  ? -9.049  39.753  109.352 1.00 25.84 ? 148  GLY   B O     1 
ATOM   9949  N  N     . LEU   B  1  151  ? -7.423  38.237  109.031 1.00 25.68 ? 149  LEU   B N     1 
ATOM   9950  C  CA    A LEU   B  1  151  ? -8.385  37.161  108.815 0.46 29.36 ? 149  LEU   B CA    1 
ATOM   9951  C  CA    B LEU   B  1  151  ? -8.386  37.165  108.812 0.54 29.36 ? 149  LEU   B CA    1 
ATOM   9952  C  C     . LEU   B  1  151  ? -9.212  36.911  110.068 1.00 28.78 ? 149  LEU   B C     1 
ATOM   9953  O  O     . LEU   B  1  151  ? -10.428 36.701  109.991 1.00 31.64 ? 149  LEU   B O     1 
ATOM   9954  C  CB    A LEU   B  1  151  ? -7.654  35.887  108.395 0.46 30.61 ? 149  LEU   B CB    1 
ATOM   9955  C  CB    B LEU   B  1  151  ? -7.652  35.900  108.371 0.54 30.61 ? 149  LEU   B CB    1 
ATOM   9956  C  CG    A LEU   B  1  151  ? -7.879  35.385  106.969 0.46 32.42 ? 149  LEU   B CG    1 
ATOM   9957  C  CG    B LEU   B  1  151  ? -8.486  34.733  107.850 0.54 32.21 ? 149  LEU   B CG    1 
ATOM   9958  C  CD1   A LEU   B  1  151  ? -7.066  34.125  106.726 0.46 35.92 ? 149  LEU   B CD1   1 
ATOM   9959  C  CD1   B LEU   B  1  151  ? -9.287  35.153  106.625 0.54 32.67 ? 149  LEU   B CD1   1 
ATOM   9960  C  CD2   A LEU   B  1  151  ? -9.358  35.128  106.718 0.46 32.69 ? 149  LEU   B CD2   1 
ATOM   9961  C  CD2   B LEU   B  1  151  ? -7.574  33.563  107.522 0.54 35.98 ? 149  LEU   B CD2   1 
ATOM   9962  N  N     . VAL   B  1  152  ? -8.569  36.944  111.235 1.00 28.31 ? 150  VAL   B N     1 
ATOM   9963  C  CA    . VAL   B  1  152  ? -9.278  36.729  112.491 1.00 28.74 ? 150  VAL   B CA    1 
ATOM   9964  C  C     . VAL   B  1  152  ? -10.311 37.825  112.726 1.00 29.10 ? 150  VAL   B C     1 
ATOM   9965  O  O     . VAL   B  1  152  ? -11.440 37.556  113.154 1.00 31.24 ? 150  VAL   B O     1 
ATOM   9966  C  CB    . VAL   B  1  152  ? -8.271  36.646  113.652 1.00 27.61 ? 150  VAL   B CB    1 
ATOM   9967  C  CG1   . VAL   B  1  152  ? -8.999  36.659  114.984 1.00 32.02 ? 150  VAL   B CG1   1 
ATOM   9968  C  CG2   . VAL   B  1  152  ? -7.403  35.408  113.516 1.00 31.20 ? 150  VAL   B CG2   1 
ATOM   9969  N  N     . VAL   B  1  153  ? -9.943  39.073  112.447 1.00 27.76 ? 151  VAL   B N     1 
ATOM   9970  C  CA    . VAL   B  1  153  ? -10.783 40.209  112.808 1.00 25.71 ? 151  VAL   B CA    1 
ATOM   9971  C  C     . VAL   B  1  153  ? -11.863 40.457  111.762 1.00 30.26 ? 151  VAL   B C     1 
ATOM   9972  O  O     . VAL   B  1  153  ? -13.015 40.742  112.101 1.00 30.78 ? 151  VAL   B O     1 
ATOM   9973  C  CB    . VAL   B  1  153  ? -9.895  41.448  113.022 1.00 27.14 ? 151  VAL   B CB    1 
ATOM   9974  C  CG1   . VAL   B  1  153  ? -10.747 42.701  113.175 1.00 28.19 ? 151  VAL   B CG1   1 
ATOM   9975  C  CG2   . VAL   B  1  153  ? -8.998  41.248  114.222 1.00 24.89 ? 151  VAL   B CG2   1 
ATOM   9976  N  N     . THR   B  1  154  ? -11.507 40.374  110.479 1.00 29.29 ? 152  THR   B N     1 
ATOM   9977  C  CA    . THR   B  1  154  ? -12.403 40.763  109.401 1.00 30.04 ? 152  THR   B CA    1 
ATOM   9978  C  C     . THR   B  1  154  ? -12.906 39.596  108.574 1.00 34.38 ? 152  THR   B C     1 
ATOM   9979  O  O     . THR   B  1  154  ? -13.856 39.773  107.807 1.00 36.50 ? 152  THR   B O     1 
ATOM   9980  C  CB    . THR   B  1  154  ? -11.694 41.728  108.438 1.00 29.54 ? 152  THR   B CB    1 
ATOM   9981  O  OG1   . THR   B  1  154  ? -10.745 40.995  107.656 1.00 30.73 ? 152  THR   B OG1   1 
ATOM   9982  C  CG2   . THR   B  1  154  ? -10.968 42.823  109.205 1.00 31.35 ? 152  THR   B CG2   1 
ATOM   9983  N  N     . GLY   B  1  155  ? -12.285 38.427  108.685 1.00 29.30 ? 153  GLY   B N     1 
ATOM   9984  C  CA    . GLY   B  1  155  ? -12.632 37.324  107.814 1.00 32.46 ? 153  GLY   B CA    1 
ATOM   9985  C  C     . GLY   B  1  155  ? -12.091 37.442  106.413 1.00 34.84 ? 153  GLY   B C     1 
ATOM   9986  O  O     . GLY   B  1  155  ? -12.407 36.594  105.569 1.00 38.84 ? 153  GLY   B O     1 
ATOM   9987  N  N     . LYS   B  1  156  ? -11.291 38.463  106.134 1.00 32.02 ? 154  LYS   B N     1 
ATOM   9988  C  CA    . LYS   B  1  156  ? -10.709 38.678  104.820 1.00 35.10 ? 154  LYS   B CA    1 
ATOM   9989  C  C     . LYS   B  1  156  ? -9.200  38.545  104.923 1.00 31.90 ? 154  LYS   B C     1 
ATOM   9990  O  O     . LYS   B  1  156  ? -8.598  38.966  105.916 1.00 32.64 ? 154  LYS   B O     1 
ATOM   9991  C  CB    . LYS   B  1  156  ? -11.065 40.069  104.284 1.00 40.26 ? 154  LYS   B CB    1 
ATOM   9992  N  N     . LEU   B  1  157  ? -8.595  37.951  103.901 1.00 32.62 ? 155  LEU   B N     1 
ATOM   9993  C  CA    . LEU   B  1  157  ? -7.154  37.776  103.833 1.00 34.28 ? 155  LEU   B CA    1 
ATOM   9994  C  C     . LEU   B  1  157  ? -6.588  38.745  102.808 1.00 38.93 ? 155  LEU   B C     1 
ATOM   9995  O  O     . LEU   B  1  157  ? -7.130  38.880  101.707 1.00 40.98 ? 155  LEU   B O     1 
ATOM   9996  C  CB    . LEU   B  1  157  ? -6.798  36.343  103.434 1.00 35.71 ? 155  LEU   B CB    1 
ATOM   9997  N  N     . THR   B  1  158  ? -5.515  39.432  103.180 1.00 37.94 ? 156  THR   B N     1 
ATOM   9998  C  CA    . THR   B  1  158  ? -4.698  40.169  102.233 1.00 38.60 ? 156  THR   B CA    1 
ATOM   9999  C  C     . THR   B  1  158  ? -3.312  39.547  102.229 1.00 36.80 ? 156  THR   B C     1 
ATOM   10000 O  O     . THR   B  1  158  ? -2.873  38.962  103.224 1.00 38.97 ? 156  THR   B O     1 
ATOM   10001 C  CB    . THR   B  1  158  ? -4.591  41.648  102.604 1.00 42.05 ? 156  THR   B CB    1 
ATOM   10002 O  OG1   . THR   B  1  158  ? -3.804  41.786  103.794 1.00 42.79 ? 156  THR   B OG1   1 
ATOM   10003 C  CG2   . THR   B  1  158  ? -5.972  42.235  102.842 1.00 44.22 ? 156  THR   B CG2   1 
ATOM   10004 N  N     . SER   B  1  159  ? -2.627  39.663  101.097 1.00 33.35 ? 157  SER   B N     1 
ATOM   10005 C  CA    A SER   B  1  159  ? -1.297  39.079  100.981 0.59 32.45 ? 157  SER   B CA    1 
ATOM   10006 C  CA    B SER   B  1  159  ? -1.300  39.072  100.998 0.41 32.45 ? 157  SER   B CA    1 
ATOM   10007 C  C     . SER   B  1  159  ? -0.256  39.898  101.731 1.00 34.66 ? 157  SER   B C     1 
ATOM   10008 O  O     . SER   B  1  159  ? 0.697   39.337  102.281 1.00 32.04 ? 157  SER   B O     1 
ATOM   10009 C  CB    A SER   B  1  159  ? -0.924  38.958  99.504  0.59 33.65 ? 157  SER   B CB    1 
ATOM   10010 C  CB    B SER   B  1  159  ? -0.901  38.900  99.534  0.41 33.57 ? 157  SER   B CB    1 
ATOM   10011 O  OG    A SER   B  1  159  ? -1.685  39.869  98.725  0.59 34.87 ? 157  SER   B OG    1 
ATOM   10012 O  OG    B SER   B  1  159  ? 0.390   38.330  99.436  0.41 29.58 ? 157  SER   B OG    1 
ATOM   10013 N  N     . THR   B  1  160  ? -0.418  41.212  101.757 1.00 28.19 ? 158  THR   B N     1 
ATOM   10014 C  CA    . THR   B  1  160  ? 0.499   42.090  102.455 1.00 24.51 ? 158  THR   B CA    1 
ATOM   10015 C  C     . THR   B  1  160  ? -0.304  43.035  103.331 1.00 23.73 ? 158  THR   B C     1 
ATOM   10016 O  O     . THR   B  1  160  ? -1.533  43.109  103.256 1.00 26.41 ? 158  THR   B O     1 
ATOM   10017 C  CB    . THR   B  1  160  ? 1.388   42.873  101.480 1.00 26.38 ? 158  THR   B CB    1 
ATOM   10018 O  OG1   . THR   B  1  160  ? 0.561   43.580  100.555 1.00 30.02 ? 158  THR   B OG1   1 
ATOM   10019 C  CG2   . THR   B  1  160  ? 2.326   41.935  100.727 1.00 26.34 ? 158  THR   B CG2   1 
ATOM   10020 N  N     . VAL   B  1  161  ? 0.430   43.792  104.131 1.00 20.49 ? 159  VAL   B N     1 
ATOM   10021 C  CA    . VAL   B  1  161  ? -0.079  44.476  105.304 1.00 22.86 ? 159  VAL   B CA    1 
ATOM   10022 C  C     . VAL   B  1  161  ? 0.138   45.964  105.087 1.00 20.84 ? 159  VAL   B C     1 
ATOM   10023 O  O     . VAL   B  1  161  ? 1.238   46.381  104.707 1.00 19.10 ? 159  VAL   B O     1 
ATOM   10024 C  CB    . VAL   B  1  161  ? 0.701   43.983  106.538 1.00 26.59 ? 159  VAL   B CB    1 
ATOM   10025 C  CG1   . VAL   B  1  161  ? 0.663   44.978  107.654 1.00 31.48 ? 159  VAL   B CG1   1 
ATOM   10026 C  CG2   . VAL   B  1  161  ? 0.176   42.617  106.967 1.00 33.89 ? 159  VAL   B CG2   1 
ATOM   10027 N  N     . ASN   B  1  162  ? -0.904  46.760  105.299 1.00 20.93 ? 160  ASN   B N     1 
ATOM   10028 C  CA    . ASN   B  1  162  ? -0.709  48.204  105.255 1.00 19.44 ? 160  ASN   B CA    1 
ATOM   10029 C  C     . ASN   B  1  162  ? -0.223  48.615  106.631 1.00 19.69 ? 160  ASN   B C     1 
ATOM   10030 O  O     . ASN   B  1  162  ? -1.003  48.935  107.524 1.00 20.00 ? 160  ASN   B O     1 
ATOM   10031 C  CB    . ASN   B  1  162  ? -1.971  48.939  104.838 1.00 20.16 ? 160  ASN   B CB    1 
ATOM   10032 C  CG    . ASN   B  1  162  ? -1.745  50.434  104.709 1.00 20.66 ? 160  ASN   B CG    1 
ATOM   10033 O  OD1   . ASN   B  1  162  ? -0.788  50.978  105.272 1.00 20.49 ? 160  ASN   B OD1   1 
ATOM   10034 N  ND2   . ASN   B  1  162  ? -2.619  51.105  103.977 1.00 23.96 ? 160  ASN   B ND2   1 
ATOM   10035 N  N     . ASP   B  1  163  ? 1.101   48.611  106.784 1.00 18.77 ? 161  ASP   B N     1 
ATOM   10036 C  CA    . ASP   B  1  163  ? 1.706   48.872  108.080 1.00 17.03 ? 161  ASP   B CA    1 
ATOM   10037 C  C     . ASP   B  1  163  ? 1.560   50.321  108.511 1.00 18.21 ? 161  ASP   B C     1 
ATOM   10038 O  O     . ASP   B  1  163  ? 1.580   50.605  109.710 1.00 18.51 ? 161  ASP   B O     1 
ATOM   10039 C  CB    . ASP   B  1  163  ? 3.165   48.412  108.112 1.00 19.48 ? 161  ASP   B CB    1 
ATOM   10040 C  CG    . ASP   B  1  163  ? 3.987   48.951  106.965 1.00 20.37 ? 161  ASP   B CG    1 
ATOM   10041 O  OD1   . ASP   B  1  163  ? 3.526   48.915  105.805 1.00 19.57 ? 161  ASP   B OD1   1 
ATOM   10042 O  OD2   . ASP   B  1  163  ? 5.121   49.392  107.241 1.00 23.81 ? 161  ASP   B OD2   1 
ATOM   10043 N  N     . ARG   B  1  164  ? 1.413   51.250  107.567 1.00 17.07 ? 162  ARG   B N     1 
ATOM   10044 C  CA    A ARG   B  1  164  ? 1.168   52.630  107.966 0.49 17.46 ? 162  ARG   B CA    1 
ATOM   10045 C  CA    B ARG   B  1  164  ? 1.162   52.636  107.951 0.51 17.47 ? 162  ARG   B CA    1 
ATOM   10046 C  C     . ARG   B  1  164  ? -0.242  52.800  108.509 1.00 17.54 ? 162  ARG   B C     1 
ATOM   10047 O  O     . ARG   B  1  164  ? -0.448  53.527  109.483 1.00 17.13 ? 162  ARG   B O     1 
ATOM   10048 C  CB    A ARG   B  1  164  ? 1.440   53.581  106.802 0.49 18.53 ? 162  ARG   B CB    1 
ATOM   10049 C  CB    B ARG   B  1  164  ? 1.375   53.563  106.753 0.51 18.51 ? 162  ARG   B CB    1 
ATOM   10050 C  CG    A ARG   B  1  164  ? 2.909   53.636  106.403 0.49 20.10 ? 162  ARG   B CG    1 
ATOM   10051 C  CG    B ARG   B  1  164  ? 2.813   53.617  106.249 0.51 20.03 ? 162  ARG   B CG    1 
ATOM   10052 C  CD    A ARG   B  1  164  ? 3.812   53.771  107.628 0.49 23.30 ? 162  ARG   B CD    1 
ATOM   10053 C  CD    B ARG   B  1  164  ? 3.794   53.873  107.386 0.51 23.01 ? 162  ARG   B CD    1 
ATOM   10054 N  NE    A ARG   B  1  164  ? 3.512   54.963  108.409 0.49 24.20 ? 162  ARG   B NE    1 
ATOM   10055 N  NE    B ARG   B  1  164  ? 4.374   52.626  107.876 0.51 20.83 ? 162  ARG   B NE    1 
ATOM   10056 C  CZ    A ARG   B  1  164  ? 3.895   55.160  109.664 0.49 25.78 ? 162  ARG   B CZ    1 
ATOM   10057 C  CZ    B ARG   B  1  164  ? 4.894   52.459  109.084 0.51 25.28 ? 162  ARG   B CZ    1 
ATOM   10058 N  NH1   A ARG   B  1  164  ? 4.577   54.244  110.332 0.49 27.61 ? 162  ARG   B NH1   1 
ATOM   10059 N  NH1   B ARG   B  1  164  ? 4.892   53.433  109.977 0.51 26.82 ? 162  ARG   B NH1   1 
ATOM   10060 N  NH2   A ARG   B  1  164  ? 3.581   56.302  110.265 0.49 26.15 ? 162  ARG   B NH2   1 
ATOM   10061 N  NH2   B ARG   B  1  164  ? 5.428   51.283  109.402 0.51 25.34 ? 162  ARG   B NH2   1 
ATOM   10062 N  N     . SER   B  1  165  ? -1.220  52.147  107.875 1.00 18.32 ? 163  SER   B N     1 
ATOM   10063 C  CA    . SER   B  1  165  ? -2.581  52.175  108.388 1.00 17.08 ? 163  SER   B CA    1 
ATOM   10064 C  C     . SER   B  1  165  ? -2.655  51.511  109.755 1.00 17.28 ? 163  SER   B C     1 
ATOM   10065 O  O     . SER   B  1  165  ? -3.355  51.992  110.651 1.00 17.91 ? 163  SER   B O     1 
ATOM   10066 C  CB    . SER   B  1  165  ? -3.492  51.448  107.407 1.00 19.38 ? 163  SER   B CB    1 
ATOM   10067 O  OG    . SER   B  1  165  ? -4.754  51.193  107.995 1.00 20.83 ? 163  SER   B OG    1 
ATOM   10068 N  N     . LEU   B  1  166  ? -1.923  50.409  109.932 1.00 18.15 ? 164  LEU   B N     1 
ATOM   10069 C  CA    . LEU   B  1  166  ? -1.955  49.721  111.218 1.00 18.57 ? 164  LEU   B CA    1 
ATOM   10070 C  C     . LEU   B  1  166  ? -1.251  50.526  112.298 1.00 19.11 ? 164  LEU   B C     1 
ATOM   10071 O  O     . LEU   B  1  166  ? -1.696  50.540  113.444 1.00 19.91 ? 164  LEU   B O     1 
ATOM   10072 C  CB    . LEU   B  1  166  ? -1.313  48.347  111.085 1.00 20.04 ? 164  LEU   B CB    1 
ATOM   10073 C  CG    . LEU   B  1  166  ? -2.190  47.395  110.282 1.00 17.19 ? 164  LEU   B CG    1 
ATOM   10074 C  CD1   . LEU   B  1  166  ? -1.473  46.128  109.979 1.00 22.27 ? 164  LEU   B CD1   1 
ATOM   10075 C  CD2   . LEU   B  1  166  ? -3.477  47.096  111.043 1.00 21.30 ? 164  LEU   B CD2   1 
ATOM   10076 N  N     . ALA   B  1  167  ? -0.116  51.148  111.970 1.00 16.85 ? 165  ALA   B N     1 
ATOM   10077 C  CA    . ALA   B  1  167  ? 0.561   51.995  112.947 1.00 17.28 ? 165  ALA   B CA    1 
ATOM   10078 C  C     . ALA   B  1  167  ? -0.330  53.152  113.381 1.00 19.16 ? 165  ALA   B C     1 
ATOM   10079 O  O     . ALA   B  1  167  ? -0.430  53.463  114.573 1.00 19.32 ? 165  ALA   B O     1 
ATOM   10080 C  CB    . ALA   B  1  167  ? 1.870   52.510  112.351 1.00 19.75 ? 165  ALA   B CB    1 
ATOM   10081 N  N     . ALA   B  1  168  ? -0.998  53.791  112.412 1.00 19.08 ? 166  ALA   B N     1 
ATOM   10082 C  CA    . ALA   B  1  168  ? -1.952  54.846  112.730 1.00 17.72 ? 166  ALA   B CA    1 
ATOM   10083 C  C     . ALA   B  1  168  ? -3.078  54.320  113.608 1.00 17.20 ? 166  ALA   B C     1 
ATOM   10084 O  O     . ALA   B  1  168  ? -3.463  54.962  114.583 1.00 20.00 ? 166  ALA   B O     1 
ATOM   10085 C  CB    . ALA   B  1  168  ? -2.523  55.405  111.425 1.00 19.34 ? 166  ALA   B CB    1 
ATOM   10086 N  N     . ALA   B  1  169  ? -3.597  53.134  113.275 1.00 18.51 ? 167  ALA   B N     1 
ATOM   10087 C  CA    . ALA   B  1  169  ? -4.700  52.577  114.048 1.00 17.89 ? 167  ALA   B CA    1 
ATOM   10088 C  C     . ALA   B  1  169  ? -4.265  52.237  115.467 1.00 20.33 ? 167  ALA   B C     1 
ATOM   10089 O  O     . ALA   B  1  169  ? -5.021  52.455  116.421 1.00 20.52 ? 167  ALA   B O     1 
ATOM   10090 C  CB    . ALA   B  1  169  ? -5.225  51.336  113.336 1.00 20.57 ? 167  ALA   B CB    1 
ATOM   10091 N  N     . LEU   B  1  170  ? -3.052  51.704  115.626 1.00 19.38 ? 168  LEU   B N     1 
ATOM   10092 C  CA    . LEU   B  1  170  ? -2.585  51.363  116.965 1.00 18.73 ? 168  LEU   B CA    1 
ATOM   10093 C  C     . LEU   B  1  170  ? -2.375  52.610  117.808 1.00 20.22 ? 168  LEU   B C     1 
ATOM   10094 O  O     . LEU   B  1  170  ? -2.782  52.656  118.972 1.00 21.30 ? 168  LEU   B O     1 
ATOM   10095 C  CB    . LEU   B  1  170  ? -1.299  50.554  116.870 1.00 21.55 ? 168  LEU   B CB    1 
ATOM   10096 C  CG    . LEU   B  1  170  ? -0.817  50.012  118.210 1.00 21.67 ? 168  LEU   B CG    1 
ATOM   10097 C  CD1   . LEU   B  1  170  ? -1.903  49.185  118.876 1.00 23.23 ? 168  LEU   B CD1   1 
ATOM   10098 C  CD2   . LEU   B  1  170  ? 0.399   49.187  117.974 1.00 23.80 ? 168  LEU   B CD2   1 
ATOM   10099 N  N     . THR   B  1  171  ? -1.739  53.630  117.238 1.00 20.57 ? 169  THR   B N     1 
ATOM   10100 C  CA    . THR   B  1  171  ? -1.600  54.889  117.954 1.00 20.00 ? 169  THR   B CA    1 
ATOM   10101 C  C     . THR   B  1  171  ? -2.961  55.449  118.334 1.00 21.45 ? 169  THR   B C     1 
ATOM   10102 O  O     . THR   B  1  171  ? -3.167  55.911  119.462 1.00 21.16 ? 169  THR   B O     1 
ATOM   10103 C  CB    . THR   B  1  171  ? -0.848  55.889  117.081 1.00 22.30 ? 169  THR   B CB    1 
ATOM   10104 O  OG1   . THR   B  1  171  ? 0.485   55.413  116.853 1.00 25.92 ? 169  THR   B OG1   1 
ATOM   10105 C  CG2   . THR   B  1  171  ? -0.793  57.249  117.749 1.00 24.08 ? 169  THR   B CG2   1 
ATOM   10106 N  N     . ARG   B  1  172  ? -3.908  55.411  117.393 1.00 21.61 ? 170  ARG   B N     1 
ATOM   10107 C  CA    . ARG   B  1  172  ? -5.223  55.967  117.664 1.00 20.45 ? 170  ARG   B CA    1 
ATOM   10108 C  C     . ARG   B  1  172  ? -5.914  55.217  118.790 1.00 21.60 ? 170  ARG   B C     1 
ATOM   10109 O  O     . ARG   B  1  172  ? -6.458  55.827  119.713 1.00 22.52 ? 170  ARG   B O     1 
ATOM   10110 C  CB    . ARG   B  1  172  ? -6.069  55.931  116.396 1.00 21.38 ? 170  ARG   B CB    1 
ATOM   10111 C  CG    . ARG   B  1  172  ? -7.340  56.759  116.505 1.00 19.62 ? 170  ARG   B CG    1 
ATOM   10112 C  CD    . ARG   B  1  172  ? -8.235  56.577  115.285 1.00 20.60 ? 170  ARG   B CD    1 
ATOM   10113 N  NE    . ARG   B  1  172  ? -7.501  56.673  114.034 1.00 18.81 ? 170  ARG   B NE    1 
ATOM   10114 C  CZ    . ARG   B  1  172  ? -7.221  55.642  113.254 1.00 18.27 ? 170  ARG   B CZ    1 
ATOM   10115 N  NH1   . ARG   B  1  172  ? -7.569  54.409  113.579 1.00 20.49 ? 170  ARG   B NH1   1 
ATOM   10116 N  NH2   . ARG   B  1  172  ? -6.558  55.849  112.123 1.00 18.48 ? 170  ARG   B NH2   1 
ATOM   10117 N  N     . LEU   B  1  173  ? -5.898  53.883  118.732 1.00 21.23 ? 171  LEU   B N     1 
ATOM   10118 C  CA    . LEU   B  1  173  ? -6.628  53.140  119.755 1.00 20.80 ? 171  LEU   B CA    1 
ATOM   10119 C  C     . LEU   B  1  173  ? -5.986  53.288  121.132 1.00 22.99 ? 171  LEU   B C     1 
ATOM   10120 O  O     . LEU   B  1  173  ? -6.692  53.353  122.141 1.00 23.58 ? 171  LEU   B O     1 
ATOM   10121 C  CB    . LEU   B  1  173  ? -6.789  51.676  119.341 1.00 22.14 ? 171  LEU   B CB    1 
ATOM   10122 C  CG    . LEU   B  1  173  ? -5.619  50.699  119.420 1.00 23.81 ? 171  LEU   B CG    1 
ATOM   10123 C  CD1   . LEU   B  1  173  ? -5.590  50.038  120.802 1.00 23.83 ? 171  LEU   B CD1   1 
ATOM   10124 C  CD2   . LEU   B  1  173  ? -5.753  49.662  118.345 1.00 23.79 ? 171  LEU   B CD2   1 
ATOM   10125 N  N     . ILE   B  1  174  ? -4.651  53.329  121.199 1.00 22.84 ? 172  ILE   B N     1 
ATOM   10126 C  CA    . ILE   B  1  174  ? -4.013  53.480  122.504 1.00 21.15 ? 172  ILE   B CA    1 
ATOM   10127 C  C     . ILE   B  1  174  ? -4.257  54.870  123.063 1.00 23.41 ? 172  ILE   B C     1 
ATOM   10128 O  O     . ILE   B  1  174  ? -4.560  55.031  124.251 1.00 25.20 ? 172  ILE   B O     1 
ATOM   10129 C  CB    . ILE   B  1  174  ? -2.513  53.149  122.417 1.00 21.93 ? 172  ILE   B CB    1 
ATOM   10130 C  CG1   . ILE   B  1  174  ? -2.318  51.681  122.047 1.00 23.63 ? 172  ILE   B CG1   1 
ATOM   10131 C  CG2   . ILE   B  1  174  ? -1.819  53.495  123.734 1.00 26.39 ? 172  ILE   B CG2   1 
ATOM   10132 C  CD1   . ILE   B  1  174  ? -0.877  51.299  121.763 1.00 24.74 ? 172  ILE   B CD1   1 
ATOM   10133 N  N     . SER   B  1  175  ? -4.118  55.898  122.223 1.00 23.27 ? 173  SER   B N     1 
ATOM   10134 C  CA    . SER   B  1  175  ? -4.355  57.248  122.706 1.00 22.39 ? 173  SER   B CA    1 
ATOM   10135 C  C     . SER   B  1  175  ? -5.811  57.447  123.111 1.00 23.86 ? 173  SER   B C     1 
ATOM   10136 O  O     . SER   B  1  175  ? -6.105  58.279  123.970 1.00 28.24 ? 173  SER   B O     1 
ATOM   10137 C  CB    . SER   B  1  175  ? -3.945  58.265  121.644 1.00 25.78 ? 173  SER   B CB    1 
ATOM   10138 O  OG    . SER   B  1  175  ? -2.557  58.173  121.371 1.00 31.41 ? 173  SER   B OG    1 
ATOM   10139 N  N     . ARG   B  1  176  ? -6.725  56.684  122.515 1.00 23.78 ? 174  ARG   B N     1 
ATOM   10140 C  CA    . ARG   B  1  176  ? -8.138  56.830  122.836 1.00 22.52 ? 174  ARG   B CA    1 
ATOM   10141 C  C     . ARG   B  1  176  ? -8.526  56.014  124.069 1.00 25.62 ? 174  ARG   B C     1 
ATOM   10142 O  O     . ARG   B  1  176  ? -9.272  56.495  124.920 1.00 28.08 ? 174  ARG   B O     1 
ATOM   10143 C  CB    . ARG   B  1  176  ? -8.979  56.419  121.622 1.00 24.90 ? 174  ARG   B CB    1 
ATOM   10144 C  CG    . ARG   B  1  176  ? -10.476 56.700  121.758 1.00 24.84 ? 174  ARG   B CG    1 
ATOM   10145 C  CD    . ARG   B  1  176  ? -11.216 56.364  120.460 1.00 24.22 ? 174  ARG   B CD    1 
ATOM   10146 N  NE    . ARG   B  1  176  ? -11.376 54.928  120.243 1.00 26.00 ? 174  ARG   B NE    1 
ATOM   10147 C  CZ    . ARG   B  1  176  ? -10.811 54.214  119.273 1.00 26.43 ? 174  ARG   B CZ    1 
ATOM   10148 N  NH1   . ARG   B  1  176  ? -10.061 54.773  118.321 1.00 24.56 ? 174  ARG   B NH1   1 
ATOM   10149 N  NH2   . ARG   B  1  176  ? -11.009 52.898  119.243 1.00 30.78 ? 174  ARG   B NH2   1 
ATOM   10150 N  N     . CYS   B  1  177  ? -8.029  54.778  124.174 1.00 26.80 ? 175  CYS   B N     1 
ATOM   10151 C  CA    . CYS   B  1  177  ? -8.517  53.849  125.183 1.00 25.42 ? 175  CYS   B CA    1 
ATOM   10152 C  C     . CYS   B  1  177  ? -7.478  53.431  126.208 1.00 27.91 ? 175  CYS   B C     1 
ATOM   10153 O  O     . CYS   B  1  177  ? -7.854  52.859  127.236 1.00 29.61 ? 175  CYS   B O     1 
ATOM   10154 C  CB    . CYS   B  1  177  ? -9.104  52.591  124.528 1.00 27.02 ? 175  CYS   B CB    1 
ATOM   10155 S  SG    . CYS   B  1  177  ? -10.357 52.952  123.261 1.00 34.32 ? 175  CYS   B SG    1 
ATOM   10156 N  N     . GLY   B  1  178  ? -6.193  53.672  125.956 1.00 27.95 ? 176  GLY   B N     1 
ATOM   10157 C  CA    . GLY   B  1  178  ? -5.219  53.504  127.019 1.00 30.50 ? 176  GLY   B CA    1 
ATOM   10158 C  C     . GLY   B  1  178  ? -4.983  52.057  127.423 1.00 27.69 ? 176  GLY   B C     1 
ATOM   10159 O  O     . GLY   B  1  178  ? -5.218  51.109  126.669 1.00 27.91 ? 176  GLY   B O     1 
ATOM   10160 N  N     . GLU   B  1  179  ? -4.512  51.903  128.659 1.00 29.32 ? 177  GLU   B N     1 
ATOM   10161 C  CA    . GLU   B  1  179  ? -4.178  50.577  129.171 1.00 31.29 ? 177  GLU   B CA    1 
ATOM   10162 C  C     . GLU   B  1  179  ? -5.335  49.582  129.127 1.00 25.22 ? 177  GLU   B C     1 
ATOM   10163 O  O     . GLU   B  1  179  ? -5.087  48.412  128.790 1.00 27.26 ? 177  GLU   B O     1 
ATOM   10164 C  CB    . GLU   B  1  179  ? -3.574  50.685  130.577 1.00 32.78 ? 177  GLU   B CB    1 
ATOM   10165 C  CG    . GLU   B  1  179  ? -3.050  49.364  131.106 1.00 33.33 ? 177  GLU   B CG    1 
ATOM   10166 C  CD    . GLU   B  1  179  ? -2.357  49.494  132.447 1.00 42.69 ? 177  GLU   B CD    1 
ATOM   10167 O  OE1   . GLU   B  1  179  ? -2.186  50.634  132.931 1.00 46.54 ? 177  GLU   B OE1   1 
ATOM   10168 O  OE2   . GLU   B  1  179  ? -1.981  48.448  133.018 1.00 50.89 ? 177  GLU   B OE2   1 
ATOM   10169 N  N     . PRO   B  1  180  ? -6.582  49.948  129.446 1.00 26.00 ? 178  PRO   B N     1 
ATOM   10170 C  CA    . PRO   B  1  180  ? -7.646  48.931  129.444 1.00 27.55 ? 178  PRO   B CA    1 
ATOM   10171 C  C     . PRO   B  1  180  ? -7.806  48.179  128.134 1.00 30.20 ? 178  PRO   B C     1 
ATOM   10172 O  O     . PRO   B  1  180  ? -8.052  46.967  128.156 1.00 30.69 ? 178  PRO   B O     1 
ATOM   10173 C  CB    . PRO   B  1  180  ? -8.898  49.733  129.820 1.00 33.27 ? 178  PRO   B CB    1 
ATOM   10174 C  CG    . PRO   B  1  180  ? -8.374  50.837  130.667 1.00 30.10 ? 178  PRO   B CG    1 
ATOM   10175 C  CD    . PRO   B  1  180  ? -7.041  51.205  130.067 1.00 27.95 ? 178  PRO   B CD    1 
ATOM   10176 N  N     . VAL   B  1  181  ? -7.677  48.843  126.984 1.00 25.08 ? 179  VAL   B N     1 
ATOM   10177 C  CA    . VAL   B  1  181  ? -7.840  48.101  125.741 1.00 25.05 ? 179  VAL   B CA    1 
ATOM   10178 C  C     . VAL   B  1  181  ? -6.649  47.187  125.486 1.00 25.52 ? 179  VAL   B C     1 
ATOM   10179 O  O     . VAL   B  1  181  ? -6.807  46.093  124.929 1.00 26.71 ? 179  VAL   B O     1 
ATOM   10180 C  CB    . VAL   B  1  181  ? -8.138  49.033  124.550 1.00 27.50 ? 179  VAL   B CB    1 
ATOM   10181 C  CG1   . VAL   B  1  181  ? -6.907  49.842  124.174 1.00 27.69 ? 179  VAL   B CG1   1 
ATOM   10182 C  CG2   . VAL   B  1  181  ? -8.605  48.220  123.365 1.00 29.53 ? 179  VAL   B CG2   1 
ATOM   10183 N  N     . ILE   B  1  182  ? -5.445  47.608  125.886 1.00 24.76 ? 180  ILE   B N     1 
ATOM   10184 C  CA    . ILE   B  1  182  ? -4.266  46.766  125.718 1.00 27.09 ? 180  ILE   B CA    1 
ATOM   10185 C  C     . ILE   B  1  182  ? -4.400  45.506  126.561 1.00 27.03 ? 180  ILE   B C     1 
ATOM   10186 O  O     . ILE   B  1  182  ? -4.105  44.394  126.102 1.00 28.58 ? 180  ILE   B O     1 
ATOM   10187 C  CB    . ILE   B  1  182  ? -2.990  47.550  126.070 1.00 24.89 ? 180  ILE   B CB    1 
ATOM   10188 C  CG1   . ILE   B  1  182  ? -2.831  48.766  125.160 1.00 25.83 ? 180  ILE   B CG1   1 
ATOM   10189 C  CG2   . ILE   B  1  182  ? -1.762  46.642  125.946 1.00 26.00 ? 180  ILE   B CG2   1 
ATOM   10190 C  CD1   . ILE   B  1  182  ? -1.820  49.770  125.676 1.00 26.96 ? 180  ILE   B CD1   1 
ATOM   10191 N  N     . ARG   B  1  183  ? -4.837  45.669  127.812 1.00 29.06 ? 181  ARG   B N     1 
ATOM   10192 C  CA    . ARG   B  1  183  ? -5.046  44.528  128.693 1.00 31.83 ? 181  ARG   B CA    1 
ATOM   10193 C  C     . ARG   B  1  183  ? -6.058  43.557  128.102 1.00 28.49 ? 181  ARG   B C     1 
ATOM   10194 O  O     . ARG   B  1  183  ? -5.833  42.341  128.082 1.00 31.98 ? 181  ARG   B O     1 
ATOM   10195 C  CB    . ARG   B  1  183  ? -5.510  45.036  130.059 1.00 30.44 ? 181  ARG   B CB    1 
ATOM   10196 C  CG    . ARG   B  1  183  ? -6.292  44.032  130.899 1.00 38.60 ? 181  ARG   B CG    1 
ATOM   10197 C  CD    . ARG   B  1  183  ? -5.389  43.160  131.764 1.00 43.49 ? 181  ARG   B CD    1 
ATOM   10198 N  NE    . ARG   B  1  183  ? -4.649  42.166  130.994 1.00 43.47 ? 181  ARG   B NE    1 
ATOM   10199 C  CZ    . ARG   B  1  183  ? -3.328  42.128  130.891 1.00 42.60 ? 181  ARG   B CZ    1 
ATOM   10200 N  NH1   . ARG   B  1  183  ? -2.561  43.039  131.472 1.00 43.61 ? 181  ARG   B NH1   1 
ATOM   10201 N  NH2   . ARG   B  1  183  ? -2.761  41.143  130.204 1.00 45.33 ? 181  ARG   B NH2   1 
ATOM   10202 N  N     . ARG   B  1  184  ? -7.185  44.076  127.612 1.00 30.37 ? 182  ARG   B N     1 
ATOM   10203 C  CA    . ARG   B  1  184  ? -8.192  43.212  127.007 1.00 31.94 ? 182  ARG   B CA    1 
ATOM   10204 C  C     . ARG   B  1  184  ? -7.651  42.506  125.769 1.00 30.25 ? 182  ARG   B C     1 
ATOM   10205 O  O     . ARG   B  1  184  ? -7.941  41.325  125.546 1.00 31.47 ? 182  ARG   B O     1 
ATOM   10206 C  CB    . ARG   B  1  184  ? -9.445  44.018  126.666 1.00 33.43 ? 182  ARG   B CB    1 
ATOM   10207 C  CG    . ARG   B  1  184  ? -10.357 44.267  127.848 1.00 39.40 ? 182  ARG   B CG    1 
ATOM   10208 C  CD    . ARG   B  1  184  ? -11.357 43.132  128.021 1.00 41.47 ? 182  ARG   B CD    1 
ATOM   10209 N  NE    . ARG   B  1  184  ? -12.533 43.298  127.171 1.00 38.94 ? 182  ARG   B NE    1 
ATOM   10210 C  CZ    . ARG   B  1  184  ? -12.986 42.388  126.318 1.00 39.19 ? 182  ARG   B CZ    1 
ATOM   10211 N  NH1   . ARG   B  1  184  ? -12.375 41.225  126.154 1.00 41.85 ? 182  ARG   B NH1   1 
ATOM   10212 N  NH2   . ARG   B  1  184  ? -14.087 42.649  125.617 1.00 43.05 ? 182  ARG   B NH2   1 
ATOM   10213 N  N     . GLY   B  1  185  ? -6.872  43.213  124.946 1.00 30.62 ? 183  GLY   B N     1 
ATOM   10214 C  CA    . GLY   B  1  185  ? -6.317  42.584  123.760 1.00 27.30 ? 183  GLY   B CA    1 
ATOM   10215 C  C     . GLY   B  1  185  ? -5.320  41.492  124.097 1.00 28.14 ? 183  GLY   B C     1 
ATOM   10216 O  O     . GLY   B  1  185  ? -5.292  40.441  123.449 1.00 29.43 ? 183  GLY   B O     1 
ATOM   10217 N  N     . VAL   B  1  186  ? -4.497  41.722  125.122 1.00 27.27 ? 184  VAL   B N     1 
ATOM   10218 C  CA    . VAL   B  1  186  ? -3.539  40.706  125.551 1.00 28.09 ? 184  VAL   B CA    1 
ATOM   10219 C  C     . VAL   B  1  186  ? -4.269  39.465  126.051 1.00 30.68 ? 184  VAL   B C     1 
ATOM   10220 O  O     . VAL   B  1  186  ? -3.946  38.334  125.668 1.00 30.21 ? 184  VAL   B O     1 
ATOM   10221 C  CB    . VAL   B  1  186  ? -2.587  41.281  126.614 1.00 30.35 ? 184  VAL   B CB    1 
ATOM   10222 C  CG1   . VAL   B  1  186  ? -1.825  40.158  127.300 1.00 31.22 ? 184  VAL   B CG1   1 
ATOM   10223 C  CG2   . VAL   B  1  186  ? -1.624  42.272  125.981 1.00 28.69 ? 184  VAL   B CG2   1 
ATOM   10224 N  N     . ASP   B  1  187  ? -5.273  39.659  126.908 1.00 29.40 ? 185  ASP   B N     1 
ATOM   10225 C  CA    . ASP   B  1  187  ? -6.034  38.523  127.418 1.00 31.36 ? 185  ASP   B CA    1 
ATOM   10226 C  C     . ASP   B  1  187  ? -6.742  37.790  126.291 1.00 34.96 ? 185  ASP   B C     1 
ATOM   10227 O  O     . ASP   B  1  187  ? -6.805  36.555  126.286 1.00 32.83 ? 185  ASP   B O     1 
ATOM   10228 C  CB    . ASP   B  1  187  ? -7.041  38.990  128.468 1.00 33.13 ? 185  ASP   B CB    1 
ATOM   10229 C  CG    . ASP   B  1  187  ? -6.370  39.537  129.710 1.00 38.34 ? 185  ASP   B CG    1 
ATOM   10230 O  OD1   . ASP   B  1  187  ? -5.184  39.209  129.935 1.00 39.72 ? 185  ASP   B OD1   1 
ATOM   10231 O  OD2   . ASP   B  1  187  ? -7.022  40.297  130.455 1.00 37.49 ? 185  ASP   B OD2   1 
ATOM   10232 N  N     . MET   B  1  188  ? -7.270  38.536  125.320 1.00 34.86 ? 186  MET   B N     1 
ATOM   10233 C  CA    . MET   B  1  188  ? -7.950  37.919  124.188 1.00 31.85 ? 186  MET   B CA    1 
ATOM   10234 C  C     . MET   B  1  188  ? -6.982  37.097  123.345 1.00 31.89 ? 186  MET   B C     1 
ATOM   10235 O  O     . MET   B  1  188  ? -7.256  35.935  123.023 1.00 32.96 ? 186  MET   B O     1 
ATOM   10236 C  CB    . MET   B  1  188  ? -8.614  39.004  123.345 1.00 34.39 ? 186  MET   B CB    1 
ATOM   10237 C  CG    . MET   B  1  188  ? -9.393  38.477  122.158 1.00 37.97 ? 186  MET   B CG    1 
ATOM   10238 S  SD    . MET   B  1  188  ? -10.749 37.418  122.684 1.00 53.23 ? 186  MET   B SD    1 
ATOM   10239 C  CE    . MET   B  1  188  ? -11.576 38.476  123.874 1.00 49.19 ? 186  MET   B CE    1 
ATOM   10240 N  N     . ALA   B  1  189  ? -5.841  37.681  122.978 1.00 30.78 ? 187  ALA   B N     1 
ATOM   10241 C  CA    . ALA   B  1  189  ? -4.864  36.943  122.184 1.00 32.34 ? 187  ALA   B CA    1 
ATOM   10242 C  C     . ALA   B  1  189  ? -4.347  35.726  122.943 1.00 32.29 ? 187  ALA   B C     1 
ATOM   10243 O  O     . ALA   B  1  189  ? -4.116  34.665  122.351 1.00 30.44 ? 187  ALA   B O     1 
ATOM   10244 C  CB    . ALA   B  1  189  ? -3.707  37.861  121.795 1.00 33.36 ? 187  ALA   B CB    1 
ATOM   10245 N  N     . MET   B  1  190  ? -4.151  35.867  124.252 1.00 32.28 ? 188  MET   B N     1 
ATOM   10246 C  CA    . MET   B  1  190  ? -3.704  34.738  125.062 1.00 33.76 ? 188  MET   B CA    1 
ATOM   10247 C  C     . MET   B  1  190  ? -4.699  33.586  124.982 1.00 33.64 ? 188  MET   B C     1 
ATOM   10248 O  O     . MET   B  1  190  ? -4.312  32.426  124.798 1.00 33.90 ? 188  MET   B O     1 
ATOM   10249 C  CB    . MET   B  1  190  ? -3.522  35.188  126.510 1.00 34.43 ? 188  MET   B CB    1 
ATOM   10250 C  CG    . MET   B  1  190  ? -2.581  34.316  127.309 1.00 39.05 ? 188  MET   B CG    1 
ATOM   10251 S  SD    . MET   B  1  190  ? -2.584  34.777  129.049 1.00 44.27 ? 188  MET   B SD    1 
ATOM   10252 C  CE    . MET   B  1  190  ? -2.194  36.524  128.963 1.00 38.40 ? 188  MET   B CE    1 
ATOM   10253 N  N     . ARG   B  1  191  ? -5.990  33.889  125.115 1.00 32.60 ? 189  ARG   B N     1 
ATOM   10254 C  CA    . ARG   B  1  191  ? -7.001  32.842  125.033 1.00 36.69 ? 189  ARG   B CA    1 
ATOM   10255 C  C     . ARG   B  1  191  ? -7.025  32.222  123.642 1.00 34.74 ? 189  ARG   B C     1 
ATOM   10256 O  O     . ARG   B  1  191  ? -7.061  30.995  123.492 1.00 34.75 ? 189  ARG   B O     1 
ATOM   10257 C  CB    . ARG   B  1  191  ? -8.373  33.407  125.402 1.00 34.94 ? 189  ARG   B CB    1 
ATOM   10258 N  N     . MET   B  1  192  ? -6.982  33.059  122.607 1.00 30.47 ? 190  MET   B N     1 
ATOM   10259 C  CA    . MET   B  1  192  ? -7.064  32.541  121.250 1.00 30.88 ? 190  MET   B CA    1 
ATOM   10260 C  C     . MET   B  1  192  ? -5.859  31.674  120.921 1.00 33.24 ? 190  MET   B C     1 
ATOM   10261 O  O     . MET   B  1  192  ? -6.001  30.550  120.426 1.00 32.54 ? 190  MET   B O     1 
ATOM   10262 C  CB    . MET   B  1  192  ? -7.167  33.700  120.264 1.00 33.24 ? 190  MET   B CB    1 
ATOM   10263 C  CG    . MET   B  1  192  ? -8.377  34.577  120.483 1.00 36.57 ? 190  MET   B CG    1 
ATOM   10264 S  SD    . MET   B  1  192  ? -8.523  35.743  119.129 1.00 46.28 ? 190  MET   B SD    1 
ATOM   10265 C  CE    . MET   B  1  192  ? -9.177  34.649  117.875 1.00 39.47 ? 190  MET   B CE    1 
ATOM   10266 N  N     . MET   B  1  193  ? -4.660  32.176  121.195 1.00 31.17 ? 191  MET   B N     1 
ATOM   10267 C  CA    A MET   B  1  193  ? -3.444  31.462  120.831 0.50 33.52 ? 191  MET   B CA    1 
ATOM   10268 C  CA    B MET   B  1  193  ? -3.467  31.439  120.813 0.50 33.52 ? 191  MET   B CA    1 
ATOM   10269 C  C     . MET   B  1  193  ? -3.137  30.307  121.772 1.00 35.33 ? 191  MET   B C     1 
ATOM   10270 O  O     . MET   B  1  193  ? -2.386  29.402  121.397 1.00 35.62 ? 191  MET   B O     1 
ATOM   10271 C  CB    A MET   B  1  193  ? -2.256  32.426  120.804 0.50 35.76 ? 191  MET   B CB    1 
ATOM   10272 C  CB    B MET   B  1  193  ? -2.282  32.388  120.659 0.50 35.78 ? 191  MET   B CB    1 
ATOM   10273 C  CG    A MET   B  1  193  ? -2.468  33.654  119.932 0.50 34.14 ? 191  MET   B CG    1 
ATOM   10274 C  CG    B MET   B  1  193  ? -2.424  33.308  119.467 0.50 34.55 ? 191  MET   B CG    1 
ATOM   10275 S  SD    A MET   B  1  193  ? -1.103  34.830  120.026 0.50 31.89 ? 191  MET   B SD    1 
ATOM   10276 S  SD    B MET   B  1  193  ? -0.879  34.111  119.037 0.50 34.85 ? 191  MET   B SD    1 
ATOM   10277 C  CE    A MET   B  1  193  ? -0.081  34.255  118.677 0.50 39.67 ? 191  MET   B CE    1 
ATOM   10278 C  CE    B MET   B  1  193  ? -0.651  35.185  120.452 0.50 34.11 ? 191  MET   B CE    1 
ATOM   10279 N  N     . GLY   B  1  194  ? -3.693  30.322  122.978 1.00 33.02 ? 192  GLY   B N     1 
ATOM   10280 C  CA    . GLY   B  1  194  ? -3.390  29.285  123.941 1.00 34.59 ? 192  GLY   B CA    1 
ATOM   10281 C  C     . GLY   B  1  194  ? -4.456  28.218  124.044 1.00 34.31 ? 192  GLY   B C     1 
ATOM   10282 O  O     . GLY   B  1  194  ? -4.168  27.093  124.465 1.00 34.21 ? 192  GLY   B O     1 
ATOM   10283 N  N     . GLU   B  1  195  ? -5.692  28.552  123.667 1.00 32.69 ? 193  GLU   B N     1 
ATOM   10284 C  CA    . GLU   B  1  195  ? -6.829  27.673  123.920 1.00 33.93 ? 193  GLU   B CA    1 
ATOM   10285 C  C     . GLU   B  1  195  ? -7.726  27.427  122.720 1.00 33.47 ? 193  GLU   B C     1 
ATOM   10286 O  O     . GLU   B  1  195  ? -8.431  26.412  122.712 1.00 29.69 ? 193  GLU   B O     1 
ATOM   10287 C  CB    . GLU   B  1  195  ? -7.697  28.221  125.064 1.00 33.76 ? 193  GLU   B CB    1 
ATOM   10288 C  CG    . GLU   B  1  195  ? -6.939  28.538  126.334 1.00 42.48 ? 193  GLU   B CG    1 
ATOM   10289 C  CD    . GLU   B  1  195  ? -7.777  29.336  127.306 1.00 45.79 ? 193  GLU   B CD    1 
ATOM   10290 O  OE1   . GLU   B  1  195  ? -8.995  29.071  127.387 1.00 51.05 ? 193  GLU   B OE1   1 
ATOM   10291 O  OE2   . GLU   B  1  195  ? -7.222  30.234  127.976 1.00 50.87 ? 193  GLU   B OE2   1 
ATOM   10292 N  N     . GLN   B  1  196  ? -7.743  28.310  121.724 1.00 34.14 ? 194  GLN   B N     1 
ATOM   10293 C  CA    . GLN   B  1  196  ? -8.593  28.147  120.551 1.00 34.37 ? 194  GLN   B CA    1 
ATOM   10294 C  C     . GLN   B  1  196  ? -7.815  27.660  119.336 1.00 33.90 ? 194  GLN   B C     1 
ATOM   10295 O  O     . GLN   B  1  196  ? -8.175  26.644  118.736 1.00 38.53 ? 194  GLN   B O     1 
ATOM   10296 C  CB    . GLN   B  1  196  ? -9.307  29.465  120.227 1.00 36.62 ? 194  GLN   B CB    1 
ATOM   10297 N  N     . PHE   B  1  197  ? -6.748  28.369  118.965 1.00 34.61 ? 195  PHE   B N     1 
ATOM   10298 C  CA    . PHE   B  1  197  ? -5.938  27.957  117.824 1.00 35.64 ? 195  PHE   B CA    1 
ATOM   10299 C  C     . PHE   B  1  197  ? -5.208  26.654  118.100 1.00 34.98 ? 195  PHE   B C     1 
ATOM   10300 O  O     . PHE   B  1  197  ? -4.906  25.901  117.166 1.00 36.79 ? 195  PHE   B O     1 
ATOM   10301 C  CB    . PHE   B  1  197  ? -4.933  29.051  117.479 1.00 35.40 ? 195  PHE   B CB    1 
ATOM   10302 C  CG    . PHE   B  1  197  ? -5.569  30.343  117.064 1.00 35.25 ? 195  PHE   B CG    1 
ATOM   10303 C  CD1   . PHE   B  1  197  ? -6.792  30.349  116.415 1.00 36.31 ? 195  PHE   B CD1   1 
ATOM   10304 C  CD2   . PHE   B  1  197  ? -4.948  31.551  117.330 1.00 36.42 ? 195  PHE   B CD2   1 
ATOM   10305 C  CE1   . PHE   B  1  197  ? -7.382  31.538  116.030 1.00 39.65 ? 195  PHE   B CE1   1 
ATOM   10306 C  CE2   . PHE   B  1  197  ? -5.533  32.744  116.947 1.00 38.61 ? 195  PHE   B CE2   1 
ATOM   10307 C  CZ    . PHE   B  1  197  ? -6.750  32.736  116.298 1.00 37.67 ? 195  PHE   B CZ    1 
ATOM   10308 N  N     . VAL   B  1  198  ? -4.890  26.387  119.363 1.00 33.43 ? 196  VAL   B N     1 
ATOM   10309 C  CA    . VAL   B  1  198  ? -4.291  25.127  119.774 1.00 31.71 ? 196  VAL   B CA    1 
ATOM   10310 C  C     . VAL   B  1  198  ? -5.057  24.618  120.981 1.00 31.68 ? 196  VAL   B C     1 
ATOM   10311 O  O     . VAL   B  1  198  ? -5.669  25.387  121.729 1.00 31.49 ? 196  VAL   B O     1 
ATOM   10312 C  CB    . VAL   B  1  198  ? -2.789  25.258  120.114 1.00 28.12 ? 196  VAL   B CB    1 
ATOM   10313 C  CG1   . VAL   B  1  198  ? -2.013  25.786  118.933 1.00 31.52 ? 196  VAL   B CG1   1 
ATOM   10314 C  CG2   . VAL   B  1  198  ? -2.596  26.149  121.332 1.00 34.07 ? 196  VAL   B CG2   1 
ATOM   10315 N  N     . THR   B  1  199  ? -5.048  23.302  121.154 1.00 29.36 ? 197  THR   B N     1 
ATOM   10316 C  CA    A THR   B  1  199  ? -5.606  22.715  122.363 0.59 28.56 ? 197  THR   B CA    1 
ATOM   10317 C  CA    B THR   B  1  199  ? -5.618  22.742  122.369 0.41 28.59 ? 197  THR   B CA    1 
ATOM   10318 C  C     . THR   B  1  199  ? -4.689  22.928  123.557 1.00 30.88 ? 197  THR   B C     1 
ATOM   10319 O  O     . THR   B  1  199  ? -5.156  22.923  124.695 1.00 32.69 ? 197  THR   B O     1 
ATOM   10320 C  CB    A THR   B  1  199  ? -5.865  21.227  122.127 0.59 29.25 ? 197  THR   B CB    1 
ATOM   10321 C  CB    B THR   B  1  199  ? -5.956  21.266  122.171 0.41 29.22 ? 197  THR   B CB    1 
ATOM   10322 O  OG1   A THR   B  1  199  ? -6.616  21.074  120.918 0.59 28.09 ? 197  THR   B OG1   1 
ATOM   10323 O  OG1   B THR   B  1  199  ? -6.431  20.708  123.401 0.41 31.01 ? 197  THR   B OG1   1 
ATOM   10324 C  CG2   A THR   B  1  199  ? -6.652  20.617  123.272 0.59 31.11 ? 197  THR   B CG2   1 
ATOM   10325 C  CG2   B THR   B  1  199  ? -4.732  20.516  121.734 0.41 25.76 ? 197  THR   B CG2   1 
ATOM   10326 N  N     . GLY   B  1  200  ? -3.403  23.120  123.313 1.00 27.81 ? 198  GLY   B N     1 
ATOM   10327 C  CA    . GLY   B  1  200  ? -2.454  23.384  124.371 1.00 29.28 ? 198  GLY   B CA    1 
ATOM   10328 C  C     . GLY   B  1  200  ? -1.108  23.680  123.749 1.00 27.66 ? 198  GLY   B C     1 
ATOM   10329 O  O     . GLY   B  1  200  ? -0.871  23.396  122.572 1.00 26.79 ? 198  GLY   B O     1 
ATOM   10330 N  N     . GLU   B  1  201  ? -0.233  24.276  124.562 1.00 31.27 ? 199  GLU   B N     1 
ATOM   10331 C  CA    . GLU   B  1  201  ? 1.113   24.589  124.092 1.00 29.84 ? 199  GLU   B CA    1 
ATOM   10332 C  C     . GLU   B  1  201  ? 2.036   23.382  124.145 1.00 30.44 ? 199  GLU   B C     1 
ATOM   10333 O  O     . GLU   B  1  201  ? 3.034   23.337  123.418 1.00 35.76 ? 199  GLU   B O     1 
ATOM   10334 C  CB    . GLU   B  1  201  ? 1.716   25.726  124.920 1.00 36.96 ? 199  GLU   B CB    1 
ATOM   10335 C  CG    . GLU   B  1  201  ? 1.100   27.083  124.647 1.00 41.33 ? 199  GLU   B CG    1 
ATOM   10336 C  CD    . GLU   B  1  201  ? 1.839   28.206  125.349 1.00 50.66 ? 199  GLU   B CD    1 
ATOM   10337 O  OE1   . GLU   B  1  201  ? 2.674   27.914  126.235 1.00 46.24 ? 199  GLU   B OE1   1 
ATOM   10338 O  OE2   . GLU   B  1  201  ? 1.584   29.381  125.008 1.00 52.63 ? 199  GLU   B OE2   1 
ATOM   10339 N  N     . THR   B  1  202  ? 1.748   22.423  125.015 1.00 27.37 ? 200  THR   B N     1 
ATOM   10340 C  CA    . THR   B  1  202  ? 2.505   21.187  125.104 1.00 29.91 ? 200  THR   B CA    1 
ATOM   10341 C  C     . THR   B  1  202  ? 1.524   20.030  125.019 1.00 29.13 ? 200  THR   B C     1 
ATOM   10342 O  O     . THR   B  1  202  ? 0.323   20.196  125.252 1.00 25.66 ? 200  THR   B O     1 
ATOM   10343 C  CB    . THR   B  1  202  ? 3.251   21.079  126.435 1.00 31.30 ? 200  THR   B CB    1 
ATOM   10344 O  OG1   . THR   B  1  202  ? 2.299   20.960  127.496 1.00 28.28 ? 200  THR   B OG1   1 
ATOM   10345 C  CG2   . THR   B  1  202  ? 4.121   22.311  126.675 1.00 30.81 ? 200  THR   B CG2   1 
ATOM   10346 N  N     . ILE   B  1  203  ? 2.047   18.850  124.678 1.00 26.09 ? 201  ILE   B N     1 
ATOM   10347 C  CA    . ILE   B  1  203  ? 1.182   17.676  124.595 1.00 26.06 ? 201  ILE   B CA    1 
ATOM   10348 C  C     . ILE   B  1  203  ? 0.608   17.346  125.966 1.00 28.95 ? 201  ILE   B C     1 
ATOM   10349 O  O     . ILE   B  1  203  ? -0.553  16.935  126.083 1.00 25.51 ? 201  ILE   B O     1 
ATOM   10350 C  CB    . ILE   B  1  203  ? 1.914   16.492  123.930 1.00 25.31 ? 201  ILE   B CB    1 
ATOM   10351 C  CG1   . ILE   B  1  203  ? 0.937   15.350  123.627 1.00 27.09 ? 201  ILE   B CG1   1 
ATOM   10352 C  CG2   . ILE   B  1  203  ? 3.083   16.009  124.784 1.00 28.63 ? 201  ILE   B CG2   1 
ATOM   10353 C  CD1   . ILE   B  1  203  ? -0.188  15.746  122.662 1.00 23.72 ? 201  ILE   B CD1   1 
ATOM   10354 N  N     . ARG   B  1  204  ? 1.394   17.571  127.023 1.00 29.34 ? 202  ARG   B N     1 
ATOM   10355 C  CA    . ARG   B  1  204  ? 0.929   17.423  128.399 1.00 30.33 ? 202  ARG   B CA    1 
ATOM   10356 C  C     . ARG   B  1  204  ? -0.333  18.238  128.641 1.00 27.20 ? 202  ARG   B C     1 
ATOM   10357 O  O     . ARG   B  1  204  ? -1.335  17.734  129.171 1.00 29.71 ? 202  ARG   B O     1 
ATOM   10358 C  CB    . ARG   B  1  204  ? 2.039   17.949  129.314 1.00 34.41 ? 202  ARG   B CB    1 
ATOM   10359 C  CG    . ARG   B  1  204  ? 2.203   17.258  130.614 1.00 44.56 ? 202  ARG   B CG    1 
ATOM   10360 C  CD    . ARG   B  1  204  ? 3.518   17.673  131.274 1.00 37.60 ? 202  ARG   B CD    1 
ATOM   10361 N  NE    . ARG   B  1  204  ? 3.573   19.093  131.612 1.00 30.44 ? 202  ARG   B NE    1 
ATOM   10362 C  CZ    . ARG   B  1  204  ? 2.894   19.646  132.606 1.00 37.29 ? 202  ARG   B CZ    1 
ATOM   10363 N  NH1   . ARG   B  1  204  ? 2.047   18.942  133.339 1.00 35.24 ? 202  ARG   B NH1   1 
ATOM   10364 N  NH2   . ARG   B  1  204  ? 3.068   20.939  132.873 1.00 37.32 ? 202  ARG   B NH2   1 
ATOM   10365 N  N     . GLU   B  1  205  ? -0.288  19.521  128.280 1.00 28.52 ? 203  GLU   B N     1 
ATOM   10366 C  CA    . GLU   B  1  205  ? -1.423  20.406  128.505 1.00 30.21 ? 203  GLU   B CA    1 
ATOM   10367 C  C     . GLU   B  1  205  ? -2.602  20.015  127.625 1.00 27.75 ? 203  GLU   B C     1 
ATOM   10368 O  O     . GLU   B  1  205  ? -3.748  19.988  128.089 1.00 30.10 ? 203  GLU   B O     1 
ATOM   10369 C  CB    . GLU   B  1  205  ? -1.004  21.847  128.220 1.00 33.48 ? 203  GLU   B CB    1 
ATOM   10370 C  CG    . GLU   B  1  205  ? -2.084  22.880  128.486 1.00 32.65 ? 203  GLU   B CG    1 
ATOM   10371 C  CD    . GLU   B  1  205  ? -1.577  24.305  128.337 1.00 42.67 ? 203  GLU   B CD    1 
ATOM   10372 O  OE1   . GLU   B  1  205  ? -1.118  24.668  127.231 1.00 36.21 ? 203  GLU   B OE1   1 
ATOM   10373 O  OE2   . GLU   B  1  205  ? -1.628  25.059  129.334 1.00 51.69 ? 203  GLU   B OE2   1 
ATOM   10374 N  N     . ALA   B  1  206  ? -2.335  19.708  126.358 1.00 24.97 ? 204  ALA   B N     1 
ATOM   10375 C  CA    . ALA   B  1  206  ? -3.395  19.294  125.446 1.00 26.07 ? 204  ALA   B CA    1 
ATOM   10376 C  C     . ALA   B  1  206  ? -4.120  18.067  125.974 1.00 27.65 ? 204  ALA   B C     1 
ATOM   10377 O  O     . ALA   B  1  206  ? -5.358  18.023  125.998 1.00 25.77 ? 204  ALA   B O     1 
ATOM   10378 C  CB    . ALA   B  1  206  ? -2.789  18.995  124.081 1.00 23.85 ? 204  ALA   B CB    1 
ATOM   10379 N  N     . LEU   B  1  207  ? -3.361  17.055  126.402 1.00 25.55 ? 205  LEU   B N     1 
ATOM   10380 C  CA    . LEU   B  1  207  ? -3.971  15.837  126.923 1.00 28.29 ? 205  LEU   B CA    1 
ATOM   10381 C  C     . LEU   B  1  207  ? -4.812  16.128  128.152 1.00 28.77 ? 205  LEU   B C     1 
ATOM   10382 O  O     . LEU   B  1  207  ? -5.899  15.559  128.318 1.00 29.75 ? 205  LEU   B O     1 
ATOM   10383 C  CB    . LEU   B  1  207  ? -2.891  14.806  127.250 1.00 27.36 ? 205  LEU   B CB    1 
ATOM   10384 C  CG    . LEU   B  1  207  ? -2.222  14.183  126.024 1.00 29.36 ? 205  LEU   B CG    1 
ATOM   10385 C  CD1   . LEU   B  1  207  ? -0.951  13.452  126.423 1.00 30.94 ? 205  LEU   B CD1   1 
ATOM   10386 C  CD2   . LEU   B  1  207  ? -3.188  13.237  125.328 1.00 26.57 ? 205  LEU   B CD2   1 
ATOM   10387 N  N     . LYS   B  1  208  ? -4.329  17.007  129.031 1.00 26.01 ? 206  LYS   B N     1 
ATOM   10388 C  CA    . LYS   B  1  208  ? -5.097  17.331  130.227 1.00 27.31 ? 206  LYS   B CA    1 
ATOM   10389 C  C     . LYS   B  1  208  ? -6.398  18.041  129.868 1.00 29.31 ? 206  LYS   B C     1 
ATOM   10390 O  O     . LYS   B  1  208  ? -7.450  17.766  130.460 1.00 31.08 ? 206  LYS   B O     1 
ATOM   10391 C  CB    . LYS   B  1  208  ? -4.253  18.171  131.192 1.00 30.47 ? 206  LYS   B CB    1 
ATOM   10392 N  N     . ARG   B  1  209  ? -6.354  18.938  128.888 1.00 28.33 ? 207  ARG   B N     1 
ATOM   10393 C  CA    . ARG   B  1  209  ? -7.547  19.665  128.485 1.00 29.51 ? 207  ARG   B CA    1 
ATOM   10394 C  C     . ARG   B  1  209  ? -8.506  18.807  127.679 1.00 33.17 ? 207  ARG   B C     1 
ATOM   10395 O  O     . ARG   B  1  209  ? -9.664  19.200  127.496 1.00 32.30 ? 207  ARG   B O     1 
ATOM   10396 C  CB    . ARG   B  1  209  ? -7.150  20.897  127.681 1.00 30.92 ? 207  ARG   B CB    1 
ATOM   10397 C  CG    . ARG   B  1  209  ? -6.362  21.912  128.492 1.00 30.94 ? 207  ARG   B CG    1 
ATOM   10398 C  CD    . ARG   B  1  209  ? -5.979  23.085  127.625 1.00 33.36 ? 207  ARG   B CD    1 
ATOM   10399 N  NE    . ARG   B  1  209  ? -5.415  24.190  128.387 1.00 39.86 ? 207  ARG   B NE    1 
ATOM   10400 C  CZ    . ARG   B  1  209  ? -4.944  25.301  127.838 1.00 42.98 ? 207  ARG   B CZ    1 
ATOM   10401 N  NH1   . ARG   B  1  209  ? -4.928  25.469  126.523 1.00 35.64 ? 207  ARG   B NH1   1 
ATOM   10402 N  NH2   . ARG   B  1  209  ? -4.481  26.268  128.625 1.00 42.70 ? 207  ARG   B NH2   1 
ATOM   10403 N  N     . SER   B  1  210  ? -8.062  17.645  127.211 1.00 28.65 ? 208  SER   B N     1 
ATOM   10404 C  CA    . SER   B  1  210  ? -8.917  16.790  126.404 1.00 30.47 ? 208  SER   B CA    1 
ATOM   10405 C  C     . SER   B  1  210  ? -9.923  16.010  127.234 1.00 29.97 ? 208  SER   B C     1 
ATOM   10406 O  O     . SER   B  1  210  ? -10.918 15.529  126.683 1.00 29.58 ? 208  SER   B O     1 
ATOM   10407 C  CB    . SER   B  1  210  ? -8.048  15.836  125.588 1.00 25.65 ? 208  SER   B CB    1 
ATOM   10408 O  OG    . SER   B  1  210  ? -7.235  16.565  124.676 1.00 30.02 ? 208  SER   B OG    1 
ATOM   10409 N  N     . LYS   B  1  211  ? -9.696  15.885  128.541 1.00 28.17 ? 209  LYS   B N     1 
ATOM   10410 C  CA    . LYS   B  1  211  ? -10.543 15.025  129.362 1.00 28.08 ? 209  LYS   B CA    1 
ATOM   10411 C  C     . LYS   B  1  211  ? -12.006 15.450  129.311 1.00 29.67 ? 209  LYS   B C     1 
ATOM   10412 O  O     . LYS   B  1  211  ? -12.901 14.597  129.283 1.00 33.96 ? 209  LYS   B O     1 
ATOM   10413 C  CB    . LYS   B  1  211  ? -10.040 15.022  130.804 1.00 33.00 ? 209  LYS   B CB    1 
ATOM   10414 N  N     . GLU   B  1  212  ? -12.270 16.761  129.288 1.00 30.99 ? 210  GLU   B N     1 
ATOM   10415 C  CA    . GLU   B  1  212  ? -13.644 17.246  129.398 1.00 32.71 ? 210  GLU   B CA    1 
ATOM   10416 C  C     . GLU   B  1  212  ? -14.500 16.746  128.241 1.00 31.98 ? 210  GLU   B C     1 
ATOM   10417 O  O     . GLU   B  1  212  ? -15.581 16.185  128.452 1.00 34.75 ? 210  GLU   B O     1 
ATOM   10418 C  CB    . GLU   B  1  212  ? -13.663 18.774  129.463 1.00 38.16 ? 210  GLU   B CB    1 
ATOM   10419 N  N     . LEU   B  1  213  ? -14.030 16.932  127.007 1.00 28.88 ? 211  LEU   B N     1 
ATOM   10420 C  CA    . LEU   B  1  213  ? -14.810 16.471  125.861 1.00 31.85 ? 211  LEU   B CA    1 
ATOM   10421 C  C     . LEU   B  1  213  ? -14.736 14.959  125.676 1.00 31.17 ? 211  LEU   B C     1 
ATOM   10422 O  O     . LEU   B  1  213  ? -15.695 14.358  125.180 1.00 30.86 ? 211  LEU   B O     1 
ATOM   10423 C  CB    . LEU   B  1  213  ? -14.444 17.241  124.588 1.00 29.03 ? 211  LEU   B CB    1 
ATOM   10424 C  CG    . LEU   B  1  213  ? -14.847 18.721  124.630 1.00 29.85 ? 211  LEU   B CG    1 
ATOM   10425 C  CD1   . LEU   B  1  213  ? -14.536 19.453  123.336 1.00 30.61 ? 211  LEU   B CD1   1 
ATOM   10426 C  CD2   . LEU   B  1  213  ? -16.325 18.861  124.991 1.00 33.11 ? 211  LEU   B CD2   1 
ATOM   10427 N  N     . GLU   B  1  214  ? -13.630 14.323  126.079 1.00 27.45 ? 212  GLU   B N     1 
ATOM   10428 C  CA    . GLU   B  1  214  ? -13.569 12.865  126.014 1.00 27.01 ? 212  GLU   B CA    1 
ATOM   10429 C  C     . GLU   B  1  214  ? -14.644 12.233  126.882 1.00 32.90 ? 212  GLU   B C     1 
ATOM   10430 O  O     . GLU   B  1  214  ? -15.295 11.268  126.466 1.00 32.01 ? 212  GLU   B O     1 
ATOM   10431 C  CB    . GLU   B  1  214  ? -12.182 12.354  126.404 1.00 29.69 ? 212  GLU   B CB    1 
ATOM   10432 C  CG    . GLU   B  1  214  ? -11.150 12.536  125.297 1.00 27.28 ? 212  GLU   B CG    1 
ATOM   10433 C  CD    . GLU   B  1  214  ? -9.814  11.901  125.624 1.00 29.54 ? 212  GLU   B CD    1 
ATOM   10434 O  OE1   . GLU   B  1  214  ? -9.533  11.678  126.813 1.00 34.94 ? 212  GLU   B OE1   1 
ATOM   10435 O  OE2   . GLU   B  1  214  ? -9.037  11.633  124.684 1.00 29.71 ? 212  GLU   B OE2   1 
ATOM   10436 N  N     . GLU   B  1  215  ? -14.856 12.777  128.084 1.00 32.32 ? 213  GLU   B N     1 
ATOM   10437 C  CA    . GLU   B  1  215  ? -15.919 12.278  128.946 1.00 31.39 ? 213  GLU   B CA    1 
ATOM   10438 C  C     . GLU   B  1  215  ? -17.284 12.400  128.282 1.00 33.02 ? 213  GLU   B C     1 
ATOM   10439 O  O     . GLU   B  1  215  ? -18.196 11.625  128.596 1.00 34.71 ? 213  GLU   B O     1 
ATOM   10440 C  CB    . GLU   B  1  215  ? -15.908 13.029  130.275 1.00 34.65 ? 213  GLU   B CB    1 
ATOM   10441 C  CG    . GLU   B  1  215  ? -14.702 12.727  131.147 1.00 38.56 ? 213  GLU   B CG    1 
ATOM   10442 C  CD    . GLU   B  1  215  ? -14.833 13.307  132.543 1.00 45.39 ? 213  GLU   B CD    1 
ATOM   10443 O  OE1   . GLU   B  1  215  ? -15.932 13.207  133.133 1.00 56.06 ? 213  GLU   B OE1   1 
ATOM   10444 O  OE2   . GLU   B  1  215  ? -13.837 13.868  133.048 1.00 52.38 ? 213  GLU   B OE2   1 
ATOM   10445 N  N     . LYS   B  1  216  ? -17.451 13.374  127.387 1.00 32.66 ? 214  LYS   B N     1 
ATOM   10446 C  CA    . LYS   B  1  216  ? -18.706 13.534  126.666 1.00 33.09 ? 214  LYS   B CA    1 
ATOM   10447 C  C     . LYS   B  1  216  ? -18.803 12.625  125.449 1.00 35.36 ? 214  LYS   B C     1 
ATOM   10448 O  O     . LYS   B  1  216  ? -19.885 12.519  124.863 1.00 35.05 ? 214  LYS   B O     1 
ATOM   10449 C  CB    . LYS   B  1  216  ? -18.898 14.995  126.244 1.00 34.35 ? 214  LYS   B CB    1 
ATOM   10450 N  N     . GLY   B  1  217  ? -17.714 11.963  125.061 1.00 29.64 ? 215  GLY   B N     1 
ATOM   10451 C  CA    . GLY   B  1  217  ? -17.737 11.035  123.949 1.00 28.78 ? 215  GLY   B CA    1 
ATOM   10452 C  C     . GLY   B  1  217  ? -16.924 11.464  122.747 1.00 34.22 ? 215  GLY   B C     1 
ATOM   10453 O  O     . GLY   B  1  217  ? -16.913 10.744  121.740 1.00 32.48 ? 215  GLY   B O     1 
ATOM   10454 N  N     . PHE   B  1  218  ? -16.266 12.618  122.802 1.00 29.24 ? 216  PHE   B N     1 
ATOM   10455 C  CA    . PHE   B  1  218  ? -15.320 12.975  121.760 1.00 27.19 ? 216  PHE   B CA    1 
ATOM   10456 C  C     . PHE   B  1  218  ? -14.042 12.164  121.924 1.00 28.09 ? 216  PHE   B C     1 
ATOM   10457 O  O     . PHE   B  1  218  ? -13.765 11.583  122.977 1.00 28.25 ? 216  PHE   B O     1 
ATOM   10458 C  CB    . PHE   B  1  218  ? -14.953 14.456  121.849 1.00 25.99 ? 216  PHE   B CB    1 
ATOM   10459 C  CG    . PHE   B  1  218  ? -16.066 15.385  121.471 1.00 30.99 ? 216  PHE   B CG    1 
ATOM   10460 C  CD1   . PHE   B  1  218  ? -17.043 15.730  122.397 1.00 30.19 ? 216  PHE   B CD1   1 
ATOM   10461 C  CD2   . PHE   B  1  218  ? -16.124 15.933  120.201 1.00 31.51 ? 216  PHE   B CD2   1 
ATOM   10462 C  CE1   . PHE   B  1  218  ? -18.061 16.592  122.054 1.00 33.25 ? 216  PHE   B CE1   1 
ATOM   10463 C  CE2   . PHE   B  1  218  ? -17.140 16.794  119.851 1.00 31.07 ? 216  PHE   B CE2   1 
ATOM   10464 C  CZ    . PHE   B  1  218  ? -18.109 17.126  120.779 1.00 31.61 ? 216  PHE   B CZ    1 
ATOM   10465 N  N     . SER   B  1  219  ? -13.266 12.117  120.853 1.00 27.34 ? 217  SER   B N     1 
ATOM   10466 C  CA    . SER   B  1  219  ? -11.899 11.629  120.904 1.00 26.74 ? 217  SER   B CA    1 
ATOM   10467 C  C     . SER   B  1  219  ? -11.000 12.689  120.292 1.00 25.53 ? 217  SER   B C     1 
ATOM   10468 O  O     . SER   B  1  219  ? -11.458 13.756  119.875 1.00 23.69 ? 217  SER   B O     1 
ATOM   10469 C  CB    . SER   B  1  219  ? -11.747 10.291  120.176 1.00 26.53 ? 217  SER   B CB    1 
ATOM   10470 O  OG    . SER   B  1  219  ? -12.162 10.424  118.830 1.00 29.30 ? 217  SER   B OG    1 
ATOM   10471 N  N     . TYR   B  1  220  ? -9.703  12.397  120.235 1.00 25.47 ? 218  TYR   B N     1 
ATOM   10472 C  CA    . TYR   B  1  220  ? -8.737  13.387  119.797 1.00 24.00 ? 218  TYR   B CA    1 
ATOM   10473 C  C     . TYR   B  1  220  ? -7.716  12.773  118.857 1.00 21.54 ? 218  TYR   B C     1 
ATOM   10474 O  O     . TYR   B  1  220  ? -7.387  11.588  118.945 1.00 23.67 ? 218  TYR   B O     1 
ATOM   10475 C  CB    . TYR   B  1  220  ? -7.995  14.011  120.988 1.00 22.35 ? 218  TYR   B CB    1 
ATOM   10476 C  CG    . TYR   B  1  220  ? -8.791  15.102  121.659 1.00 23.01 ? 218  TYR   B CG    1 
ATOM   10477 C  CD1   . TYR   B  1  220  ? -9.755  14.802  122.610 1.00 24.99 ? 218  TYR   B CD1   1 
ATOM   10478 C  CD2   . TYR   B  1  220  ? -8.609  16.431  121.299 1.00 22.50 ? 218  TYR   B CD2   1 
ATOM   10479 C  CE1   . TYR   B  1  220  ? -10.495 15.799  123.213 1.00 25.11 ? 218  TYR   B CE1   1 
ATOM   10480 C  CE2   . TYR   B  1  220  ? -9.341  17.437  121.898 1.00 26.11 ? 218  TYR   B CE2   1 
ATOM   10481 C  CZ    . TYR   B  1  220  ? -10.286 17.112  122.843 1.00 24.71 ? 218  TYR   B CZ    1 
ATOM   10482 O  OH    . TYR   B  1  220  ? -11.018 18.106  123.446 1.00 30.34 ? 218  TYR   B OH    1 
ATOM   10483 N  N     . SER   B  1  221  ? -7.211  13.615  117.971 1.00 21.37 ? 219  SER   B N     1 
ATOM   10484 C  CA    . SER   B  1  221  ? -6.035  13.320  117.169 1.00 20.58 ? 219  SER   B CA    1 
ATOM   10485 C  C     . SER   B  1  221  ? -5.151  14.554  117.242 1.00 22.40 ? 219  SER   B C     1 
ATOM   10486 O  O     . SER   B  1  221  ? -5.568  15.639  116.826 1.00 23.02 ? 219  SER   B O     1 
ATOM   10487 C  CB    . SER   B  1  221  ? -6.427  13.032  115.721 1.00 21.89 ? 219  SER   B CB    1 
ATOM   10488 O  OG    . SER   B  1  221  ? -5.272  12.772  114.944 1.00 21.91 ? 219  SER   B OG    1 
ATOM   10489 N  N     . TYR   B  1  222  ? -3.947  14.397  117.786 1.00 21.92 ? 220  TYR   B N     1 
ATOM   10490 C  CA    . TYR   B  1  222  ? -3.084  15.541  118.056 1.00 20.33 ? 220  TYR   B CA    1 
ATOM   10491 C  C     . TYR   B  1  222  ? -2.156  15.842  116.894 1.00 21.36 ? 220  TYR   B C     1 
ATOM   10492 O  O     . TYR   B  1  222  ? -1.592  14.936  116.276 1.00 21.94 ? 220  TYR   B O     1 
ATOM   10493 C  CB    . TYR   B  1  222  ? -2.266  15.309  119.322 1.00 19.52 ? 220  TYR   B CB    1 
ATOM   10494 C  CG    . TYR   B  1  222  ? -3.188  15.196  120.485 1.00 19.85 ? 220  TYR   B CG    1 
ATOM   10495 C  CD1   . TYR   B  1  222  ? -3.755  16.329  121.054 1.00 20.76 ? 220  TYR   B CD1   1 
ATOM   10496 C  CD2   . TYR   B  1  222  ? -3.535  13.954  121.004 1.00 20.93 ? 220  TYR   B CD2   1 
ATOM   10497 C  CE1   . TYR   B  1  222  ? -4.638  16.232  122.104 1.00 20.64 ? 220  TYR   B CE1   1 
ATOM   10498 C  CE2   . TYR   B  1  222  ? -4.412  13.846  122.071 1.00 21.38 ? 220  TYR   B CE2   1 
ATOM   10499 C  CZ    . TYR   B  1  222  ? -4.950  14.992  122.621 1.00 20.24 ? 220  TYR   B CZ    1 
ATOM   10500 O  OH    . TYR   B  1  222  ? -5.835  14.901  123.652 1.00 22.36 ? 220  TYR   B OH    1 
ATOM   10501 N  N     . ASP   B  1  223  ? -1.996  17.135  116.617 1.00 20.09 ? 221  ASP   B N     1 
ATOM   10502 C  CA    . ASP   B  1  223  ? -1.155  17.649  115.544 1.00 22.58 ? 221  ASP   B CA    1 
ATOM   10503 C  C     . ASP   B  1  223  ? -0.053  18.476  116.194 1.00 24.02 ? 221  ASP   B C     1 
ATOM   10504 O  O     . ASP   B  1  223  ? -0.320  19.554  116.734 1.00 23.48 ? 221  ASP   B O     1 
ATOM   10505 C  CB    . ASP   B  1  223  ? -2.005  18.519  114.628 1.00 25.00 ? 221  ASP   B CB    1 
ATOM   10506 C  CG    . ASP   B  1  223  ? -1.179  19.355  113.673 1.00 28.61 ? 221  ASP   B CG    1 
ATOM   10507 O  OD1   . ASP   B  1  223  ? -0.018  18.994  113.398 1.00 26.94 ? 221  ASP   B OD1   1 
ATOM   10508 O  OD2   . ASP   B  1  223  ? -1.701  20.387  113.207 1.00 31.00 ? 221  ASP   B OD2   1 
ATOM   10509 N  N     . MET   B  1  224  ? 1.183   17.985  116.130 1.00 21.60 ? 222  MET   B N     1 
ATOM   10510 C  CA    . MET   B  1  224  ? 2.297   18.694  116.740 1.00 24.96 ? 222  MET   B CA    1 
ATOM   10511 C  C     . MET   B  1  224  ? 2.856   19.795  115.852 1.00 24.25 ? 222  MET   B C     1 
ATOM   10512 O  O     . MET   B  1  224  ? 3.928   20.330  116.155 1.00 25.68 ? 222  MET   B O     1 
ATOM   10513 C  CB    . MET   B  1  224  ? 3.399   17.716  117.157 1.00 26.08 ? 222  MET   B CB    1 
ATOM   10514 C  CG    . MET   B  1  224  ? 2.927   16.622  118.099 1.00 21.90 ? 222  MET   B CG    1 
ATOM   10515 S  SD    . MET   B  1  224  ? 2.034   17.273  119.518 1.00 28.80 ? 222  MET   B SD    1 
ATOM   10516 C  CE    . MET   B  1  224  ? 3.312   18.284  120.262 1.00 31.21 ? 222  MET   B CE    1 
ATOM   10517 N  N     . LEU   B  1  225  ? 2.164   20.121  114.766 1.00 25.89 ? 223  LEU   B N     1 
ATOM   10518 C  CA    . LEU   B  1  225  ? 2.380   21.272  113.891 1.00 24.14 ? 223  LEU   B CA    1 
ATOM   10519 C  C     . LEU   B  1  225  ? 3.533   21.101  112.904 1.00 31.36 ? 223  LEU   B C     1 
ATOM   10520 O  O     . LEU   B  1  225  ? 3.782   22.023  112.115 1.00 31.16 ? 223  LEU   B O     1 
ATOM   10521 C  CB    . LEU   B  1  225  ? 2.529   22.606  114.639 1.00 29.08 ? 223  LEU   B CB    1 
ATOM   10522 C  CG    . LEU   B  1  225  ? 1.406   22.919  115.626 1.00 30.39 ? 223  LEU   B CG    1 
ATOM   10523 C  CD1   . LEU   B  1  225  ? 1.691   24.213  116.354 1.00 37.94 ? 223  LEU   B CD1   1 
ATOM   10524 C  CD2   . LEU   B  1  225  ? 0.066   22.980  114.922 1.00 30.64 ? 223  LEU   B CD2   1 
ATOM   10525 N  N     . GLY   B  1  226  ? 4.231   19.970  112.904 1.00 25.01 ? 224  GLY   B N     1 
ATOM   10526 C  CA    . GLY   B  1  226  ? 5.315   19.785  111.955 1.00 26.81 ? 224  GLY   B CA    1 
ATOM   10527 C  C     . GLY   B  1  226  ? 4.793   19.750  110.531 1.00 23.09 ? 224  GLY   B C     1 
ATOM   10528 O  O     . GLY   B  1  226  ? 3.771   19.130  110.233 1.00 23.19 ? 224  GLY   B O     1 
ATOM   10529 N  N     . GLU   B  1  227  ? 5.512   20.425  109.639 1.00 22.28 ? 225  GLU   B N     1 
ATOM   10530 C  CA    . GLU   B  1  227  ? 5.091   20.466  108.250 1.00 23.17 ? 225  GLU   B CA    1 
ATOM   10531 C  C     . GLU   B  1  227  ? 6.227   21.056  107.438 1.00 19.21 ? 225  GLU   B C     1 
ATOM   10532 O  O     . GLU   B  1  227  ? 6.958   21.914  107.932 1.00 21.12 ? 225  GLU   B O     1 
ATOM   10533 C  CB    . GLU   B  1  227  ? 3.847   21.352  108.114 1.00 24.90 ? 225  GLU   B CB    1 
ATOM   10534 C  CG    . GLU   B  1  227  ? 3.249   21.400  106.742 1.00 25.20 ? 225  GLU   B CG    1 
ATOM   10535 C  CD    . GLU   B  1  227  ? 1.919   22.119  106.735 1.00 28.31 ? 225  GLU   B CD    1 
ATOM   10536 O  OE1   . GLU   B  1  227  ? 1.397   22.421  107.832 1.00 27.70 ? 225  GLU   B OE1   1 
ATOM   10537 O  OE2   . GLU   B  1  227  ? 1.397   22.378  105.635 1.00 32.34 ? 225  GLU   B OE2   1 
ATOM   10538 N  N     . ALA   B  1  228  ? 6.376   20.580  106.202 1.00 18.15 ? 226  ALA   B N     1 
ATOM   10539 C  CA    . ALA   B  1  228  ? 7.222   21.237  105.209 1.00 19.35 ? 226  ALA   B CA    1 
ATOM   10540 C  C     . ALA   B  1  228  ? 8.618   21.530  105.755 1.00 19.31 ? 226  ALA   B C     1 
ATOM   10541 O  O     . ALA   B  1  228  ? 9.076   22.672  105.784 1.00 20.38 ? 226  ALA   B O     1 
ATOM   10542 C  CB    . ALA   B  1  228  ? 6.557   22.514  104.702 1.00 21.62 ? 226  ALA   B CB    1 
ATOM   10543 N  N     . ALA   B  1  229  ? 9.280   20.474  106.214 1.00 17.53 ? 227  ALA   B N     1 
ATOM   10544 C  CA    . ALA   B  1  229  ? 10.676  20.594  106.613 1.00 17.48 ? 227  ALA   B CA    1 
ATOM   10545 C  C     . ALA   B  1  229  ? 11.487  21.211  105.480 1.00 16.49 ? 227  ALA   B C     1 
ATOM   10546 O  O     . ALA   B  1  229  ? 11.337  20.834  104.319 1.00 18.41 ? 227  ALA   B O     1 
ATOM   10547 C  CB    . ALA   B  1  229  ? 11.226  19.207  106.940 1.00 18.05 ? 227  ALA   B CB    1 
ATOM   10548 N  N     . THR   B  1  230  ? 12.323  22.184  105.825 1.00 17.41 ? 228  THR   B N     1 
ATOM   10549 C  CA    . THR   B  1  230  ? 13.204  22.820  104.857 1.00 16.49 ? 228  THR   B CA    1 
ATOM   10550 C  C     . THR   B  1  230  ? 14.610  22.254  104.912 1.00 17.72 ? 228  THR   B C     1 
ATOM   10551 O  O     . THR   B  1  230  ? 15.298  22.208  103.887 1.00 17.97 ? 228  THR   B O     1 
ATOM   10552 C  CB    . THR   B  1  230  ? 13.260  24.327  105.135 1.00 18.58 ? 228  THR   B CB    1 
ATOM   10553 O  OG1   . THR   B  1  230  ? 11.922  24.842  105.174 1.00 23.89 ? 228  THR   B OG1   1 
ATOM   10554 C  CG2   . THR   B  1  230  ? 14.042  25.063  104.051 1.00 18.44 ? 228  THR   B CG2   1 
ATOM   10555 N  N     . THR   B  1  231  ? 15.036  21.807  106.084 1.00 17.38 ? 229  THR   B N     1 
ATOM   10556 C  CA    . THR   B  1  231  ? 16.379  21.294  106.287 1.00 16.81 ? 229  THR   B CA    1 
ATOM   10557 C  C     . THR   B  1  231  ? 16.281  19.936  106.960 1.00 17.07 ? 229  THR   B C     1 
ATOM   10558 O  O     . THR   B  1  231  ? 15.247  19.566  107.518 1.00 16.66 ? 229  THR   B O     1 
ATOM   10559 C  CB    . THR   B  1  231  ? 17.185  22.223  107.190 1.00 17.78 ? 229  THR   B CB    1 
ATOM   10560 O  OG1   . THR   B  1  231  ? 16.649  22.146  108.518 1.00 18.48 ? 229  THR   B OG1   1 
ATOM   10561 C  CG2   . THR   B  1  231  ? 17.135  23.660  106.691 1.00 18.84 ? 229  THR   B CG2   1 
ATOM   10562 N  N     . ALA   B  1  232  ? 17.394  19.212  106.941 1.00 16.67 ? 230  ALA   B N     1 
ATOM   10563 C  CA    . ALA   B  1  232  ? 17.453  17.952  107.671 1.00 17.13 ? 230  ALA   B CA    1 
ATOM   10564 C  C     . ALA   B  1  232  ? 17.181  18.164  109.153 1.00 18.82 ? 230  ALA   B C     1 
ATOM   10565 O  O     . ALA   B  1  232  ? 16.525  17.336  109.794 1.00 19.34 ? 230  ALA   B O     1 
ATOM   10566 C  CB    . ALA   B  1  232  ? 18.823  17.309  107.466 1.00 18.94 ? 230  ALA   B CB    1 
ATOM   10567 N  N     . ALA   B  1  233  ? 17.687  19.262  109.722 1.00 17.99 ? 231  ALA   B N     1 
ATOM   10568 C  CA    . ALA   B  1  233  ? 17.445  19.530  111.134 1.00 18.75 ? 231  ALA   B CA    1 
ATOM   10569 C  C     . ALA   B  1  233  ? 15.963  19.725  111.414 1.00 17.49 ? 231  ALA   B C     1 
ATOM   10570 O  O     . ALA   B  1  233  ? 15.467  19.296  112.464 1.00 18.89 ? 231  ALA   B O     1 
ATOM   10571 C  CB    . ALA   B  1  233  ? 18.256  20.740  111.601 1.00 21.61 ? 231  ALA   B CB    1 
ATOM   10572 N  N     . ASP   B  1  234  ? 15.242  20.380  110.499 1.00 17.20 ? 232  ASP   B N     1 
ATOM   10573 C  CA    . ASP   B  1  234  ? 13.803  20.524  110.684 1.00 18.40 ? 232  ASP   B CA    1 
ATOM   10574 C  C     . ASP   B  1  234  ? 13.151  19.159  110.765 1.00 17.97 ? 232  ASP   B C     1 
ATOM   10575 O  O     . ASP   B  1  234  ? 12.346  18.891  111.668 1.00 17.99 ? 232  ASP   B O     1 
ATOM   10576 C  CB    . ASP   B  1  234  ? 13.178  21.246  109.494 1.00 19.32 ? 232  ASP   B CB    1 
ATOM   10577 C  CG    . ASP   B  1  234  ? 13.501  22.702  109.443 1.00 23.34 ? 232  ASP   B CG    1 
ATOM   10578 O  OD1   . ASP   B  1  234  ? 13.833  23.304  110.485 1.00 22.78 ? 232  ASP   B OD1   1 
ATOM   10579 O  OD2   . ASP   B  1  234  ? 13.390  23.242  108.328 1.00 23.28 ? 232  ASP   B OD2   1 
ATOM   10580 N  N     . ALA   B  1  235  ? 13.481  18.294  109.804 1.00 17.77 ? 233  ALA   B N     1 
ATOM   10581 C  CA    . ALA   B  1  235  ? 12.843  16.994  109.714 1.00 17.96 ? 233  ALA   B CA    1 
ATOM   10582 C  C     . ALA   B  1  235  ? 13.164  16.152  110.931 1.00 17.87 ? 233  ALA   B C     1 
ATOM   10583 O  O     . ALA   B  1  235  ? 12.288  15.461  111.460 1.00 18.62 ? 233  ALA   B O     1 
ATOM   10584 C  CB    . ALA   B  1  235  ? 13.258  16.279  108.425 1.00 18.65 ? 233  ALA   B CB    1 
ATOM   10585 N  N     . GLU   B  1  236  ? 14.410  16.207  111.398 1.00 18.29 ? 234  GLU   B N     1 
ATOM   10586 C  CA    . GLU   B  1  236  ? 14.772  15.451  112.586 1.00 18.18 ? 234  GLU   B CA    1 
ATOM   10587 C  C     . GLU   B  1  236  ? 14.029  15.971  113.803 1.00 18.75 ? 234  GLU   B C     1 
ATOM   10588 O  O     . GLU   B  1  236  ? 13.549  15.183  114.630 1.00 19.28 ? 234  GLU   B O     1 
ATOM   10589 C  CB    . GLU   B  1  236  ? 16.280  15.520  112.791 1.00 20.63 ? 234  GLU   B CB    1 
ATOM   10590 C  CG    . GLU   B  1  236  ? 16.793  14.538  113.815 1.00 24.74 ? 234  GLU   B CG    1 
ATOM   10591 C  CD    . GLU   B  1  236  ? 18.297  14.636  113.977 1.00 31.92 ? 234  GLU   B CD    1 
ATOM   10592 O  OE1   . GLU   B  1  236  ? 18.884  15.589  113.421 1.00 35.50 ? 234  GLU   B OE1   1 
ATOM   10593 O  OE2   . GLU   B  1  236  ? 18.886  13.766  114.654 1.00 36.26 ? 234  GLU   B OE2   1 
ATOM   10594 N  N     . ARG   B  1  237  ? 13.915  17.294  113.928 1.00 17.84 ? 235  ARG   B N     1 
ATOM   10595 C  CA    . ARG   B  1  237  ? 13.183  17.867  115.046 1.00 19.67 ? 235  ARG   B CA    1 
ATOM   10596 C  C     . ARG   B  1  237  ? 11.720  17.440  115.014 1.00 19.27 ? 235  ARG   B C     1 
ATOM   10597 O  O     . ARG   B  1  237  ? 11.165  17.017  116.035 1.00 19.82 ? 235  ARG   B O     1 
ATOM   10598 C  CB    . ARG   B  1  237  ? 13.296  19.393  115.044 1.00 20.18 ? 235  ARG   B CB    1 
ATOM   10599 C  CG    . ARG   B  1  237  ? 12.530  19.997  116.202 1.00 24.16 ? 235  ARG   B CG    1 
ATOM   10600 C  CD    . ARG   B  1  237  ? 12.441  21.500  116.194 1.00 30.40 ? 235  ARG   B CD    1 
ATOM   10601 N  NE    . ARG   B  1  237  ? 11.737  21.908  117.406 1.00 34.79 ? 235  ARG   B NE    1 
ATOM   10602 C  CZ    . ARG   B  1  237  ? 11.748  23.129  117.922 1.00 36.89 ? 235  ARG   B CZ    1 
ATOM   10603 N  NH1   . ARG   B  1  237  ? 12.431  24.113  117.359 1.00 41.12 ? 235  ARG   B NH1   1 
ATOM   10604 N  NH2   . ARG   B  1  237  ? 11.059  23.366  119.036 1.00 36.02 ? 235  ARG   B NH2   1 
ATOM   10605 N  N     . TYR   B  1  238  ? 11.075  17.553  113.852 1.00 18.85 ? 236  TYR   B N     1 
ATOM   10606 C  CA    . TYR   B  1  238  ? 9.668   17.170  113.780 1.00 17.79 ? 236  TYR   B CA    1 
ATOM   10607 C  C     . TYR   B  1  238  ? 9.490   15.690  114.075 1.00 18.27 ? 236  TYR   B C     1 
ATOM   10608 O  O     . TYR   B  1  238  ? 8.516   15.295  114.728 1.00 18.05 ? 236  TYR   B O     1 
ATOM   10609 C  CB    . TYR   B  1  238  ? 9.080   17.492  112.412 1.00 17.29 ? 236  TYR   B CB    1 
ATOM   10610 C  CG    . TYR   B  1  238  ? 8.993   18.954  112.074 1.00 18.64 ? 236  TYR   B CG    1 
ATOM   10611 C  CD1   . TYR   B  1  238  ? 8.734   19.914  113.038 1.00 22.49 ? 236  TYR   B CD1   1 
ATOM   10612 C  CD2   . TYR   B  1  238  ? 9.171   19.370  110.769 1.00 20.28 ? 236  TYR   B CD2   1 
ATOM   10613 C  CE1   . TYR   B  1  238  ? 8.654   21.258  112.703 1.00 28.16 ? 236  TYR   B CE1   1 
ATOM   10614 C  CE2   . TYR   B  1  238  ? 9.096   20.694  110.424 1.00 20.32 ? 236  TYR   B CE2   1 
ATOM   10615 C  CZ    . TYR   B  1  238  ? 8.836   21.637  111.386 1.00 27.97 ? 236  TYR   B CZ    1 
ATOM   10616 O  OH    . TYR   B  1  238  ? 8.776   22.961  111.021 1.00 26.47 ? 236  TYR   B OH    1 
ATOM   10617 N  N     . TYR   B  1  239  ? 10.421  14.858  113.616 1.00 17.54 ? 237  TYR   B N     1 
ATOM   10618 C  CA    . TYR   B  1  239  ? 10.356  13.444  113.950 1.00 17.21 ? 237  TYR   B CA    1 
ATOM   10619 C  C     . TYR   B  1  239  ? 10.400  13.256  115.455 1.00 19.85 ? 237  TYR   B C     1 
ATOM   10620 O  O     . TYR   B  1  239  ? 9.573   12.539  116.033 1.00 19.12 ? 237  TYR   B O     1 
ATOM   10621 C  CB    . TYR   B  1  239  ? 11.513  12.688  113.301 1.00 17.74 ? 237  TYR   B CB    1 
ATOM   10622 C  CG    . TYR   B  1  239  ? 11.591  11.261  113.769 1.00 21.28 ? 237  TYR   B CG    1 
ATOM   10623 C  CD1   . TYR   B  1  239  ? 10.882  10.272  113.126 1.00 23.36 ? 237  TYR   B CD1   1 
ATOM   10624 C  CD2   . TYR   B  1  239  ? 12.353  10.902  114.879 1.00 28.46 ? 237  TYR   B CD2   1 
ATOM   10625 C  CE1   . TYR   B  1  239  ? 10.934  8.971   113.551 1.00 21.13 ? 237  TYR   B CE1   1 
ATOM   10626 C  CE2   . TYR   B  1  239  ? 12.400  9.590   115.317 1.00 27.66 ? 237  TYR   B CE2   1 
ATOM   10627 C  CZ    . TYR   B  1  239  ? 11.688  8.632   114.640 1.00 26.93 ? 237  TYR   B CZ    1 
ATOM   10628 O  OH    . TYR   B  1  239  ? 11.718  7.319   115.044 1.00 32.61 ? 237  TYR   B OH    1 
ATOM   10629 N  N     . ARG   B  1  240  ? 11.371  13.891  116.110 1.00 19.68 ? 238  ARG   B N     1 
ATOM   10630 C  CA    . ARG   B  1  240  ? 11.499  13.729  117.549 1.00 20.28 ? 238  ARG   B CA    1 
ATOM   10631 C  C     . ARG   B  1  240  ? 10.272  14.255  118.276 1.00 20.68 ? 238  ARG   B C     1 
ATOM   10632 O  O     . ARG   B  1  240  ? 9.852   13.688  119.292 1.00 21.26 ? 238  ARG   B O     1 
ATOM   10633 C  CB    . ARG   B  1  240  ? 12.759  14.439  118.039 1.00 20.46 ? 238  ARG   B CB    1 
ATOM   10634 C  CG    . ARG   B  1  240  ? 14.035  13.793  117.571 1.00 23.16 ? 238  ARG   B CG    1 
ATOM   10635 C  CD    . ARG   B  1  240  ? 14.139  12.358  118.048 1.00 28.65 ? 238  ARG   B CD    1 
ATOM   10636 N  NE    . ARG   B  1  240  ? 15.325  11.716  117.500 1.00 30.09 ? 238  ARG   B NE    1 
ATOM   10637 C  CZ    . ARG   B  1  240  ? 15.550  10.410  117.532 1.00 35.62 ? 238  ARG   B CZ    1 
ATOM   10638 N  NH1   . ARG   B  1  240  ? 14.688  9.573   118.087 1.00 32.51 ? 238  ARG   B NH1   1 
ATOM   10639 N  NH2   . ARG   B  1  240  ? 16.668  9.931   116.992 1.00 39.02 ? 238  ARG   B NH2   1 
ATOM   10640 N  N     . ASP   B  1  241  ? 9.687   15.343  117.773 1.00 21.29 ? 239  ASP   B N     1 
ATOM   10641 C  CA    . ASP   B  1  241  ? 8.475   15.872  118.383 1.00 23.72 ? 239  ASP   B CA    1 
ATOM   10642 C  C     . ASP   B  1  241  ? 7.318   14.894  118.241 1.00 21.15 ? 239  ASP   B C     1 
ATOM   10643 O  O     . ASP   B  1  241  ? 6.551   14.702  119.184 1.00 21.03 ? 239  ASP   B O     1 
ATOM   10644 C  CB    . ASP   B  1  241  ? 8.120   17.226  117.778 1.00 24.53 ? 239  ASP   B CB    1 
ATOM   10645 C  CG    . ASP   B  1  241  ? 9.088   18.333  118.194 1.00 29.99 ? 239  ASP   B CG    1 
ATOM   10646 O  OD1   . ASP   B  1  241  ? 9.913   18.123  119.118 1.00 31.63 ? 239  ASP   B OD1   1 
ATOM   10647 O  OD2   . ASP   B  1  241  ? 9.021   19.418  117.582 1.00 37.64 ? 239  ASP   B OD2   1 
ATOM   10648 N  N     . TYR   B  1  242  ? 7.178   14.261  117.074 1.00 19.11 ? 240  TYR   B N     1 
ATOM   10649 C  CA    . TYR   B  1  242  ? 6.148   13.240  116.922 1.00 19.67 ? 240  TYR   B CA    1 
ATOM   10650 C  C     . TYR   B  1  242  ? 6.405   12.071  117.854 1.00 19.47 ? 240  TYR   B C     1 
ATOM   10651 O  O     . TYR   B  1  242  ? 5.477   11.543  118.471 1.00 19.10 ? 240  TYR   B O     1 
ATOM   10652 C  CB    . TYR   B  1  242  ? 6.154   12.714  115.496 1.00 19.28 ? 240  TYR   B CB    1 
ATOM   10653 C  CG    . TYR   B  1  242  ? 5.566   13.619  114.443 1.00 18.17 ? 240  TYR   B CG    1 
ATOM   10654 C  CD1   . TYR   B  1  242  ? 4.487   14.456  114.711 1.00 20.05 ? 240  TYR   B CD1   1 
ATOM   10655 C  CD2   . TYR   B  1  242  ? 6.075   13.605  113.166 1.00 18.47 ? 240  TYR   B CD2   1 
ATOM   10656 C  CE1   . TYR   B  1  242  ? 3.938   15.262  113.707 1.00 20.91 ? 240  TYR   B CE1   1 
ATOM   10657 C  CE2   . TYR   B  1  242  ? 5.540   14.396  112.175 1.00 19.00 ? 240  TYR   B CE2   1 
ATOM   10658 C  CZ    . TYR   B  1  242  ? 4.483   15.221  112.447 1.00 21.36 ? 240  TYR   B CZ    1 
ATOM   10659 O  OH    . TYR   B  1  242  ? 3.970   16.001  111.428 1.00 20.57 ? 240  TYR   B OH    1 
ATOM   10660 N  N     . GLU   B  1  243  ? 7.662   11.637  117.941 1.00 19.93 ? 241  GLU   B N     1 
ATOM   10661 C  CA    . GLU   B  1  243  ? 8.004   10.505  118.792 1.00 18.85 ? 241  GLU   B CA    1 
ATOM   10662 C  C     . GLU   B  1  243  ? 7.661   10.801  120.246 1.00 21.49 ? 241  GLU   B C     1 
ATOM   10663 O  O     . GLU   B  1  243  ? 7.047   9.981   120.939 1.00 19.21 ? 241  GLU   B O     1 
ATOM   10664 C  CB    . GLU   B  1  243  ? 9.502   10.244  118.640 1.00 19.87 ? 241  GLU   B CB    1 
ATOM   10665 C  CG    . GLU   B  1  243  ? 10.026  9.126   119.506 1.00 23.33 ? 241  GLU   B CG    1 
ATOM   10666 C  CD    . GLU   B  1  243  ? 11.543  9.028   119.460 1.00 28.18 ? 241  GLU   B CD    1 
ATOM   10667 O  OE1   . GLU   B  1  243  ? 12.210  10.075  119.334 1.00 30.92 ? 241  GLU   B OE1   1 
ATOM   10668 O  OE2   . GLU   B  1  243  ? 12.067  7.900   119.544 1.00 31.51 ? 241  GLU   B OE2   1 
ATOM   10669 N  N     . SER   B  1  244  ? 8.054   11.982  120.724 1.00 19.61 ? 242  SER   B N     1 
ATOM   10670 C  CA    A SER   B  1  244  ? 7.749   12.373  122.094 0.56 19.67 ? 242  SER   B CA    1 
ATOM   10671 C  CA    B SER   B  1  244  ? 7.748   12.363  122.097 0.44 19.69 ? 242  SER   B CA    1 
ATOM   10672 C  C     . SER   B  1  244  ? 6.245   12.443  122.320 1.00 18.58 ? 242  SER   B C     1 
ATOM   10673 O  O     . SER   B  1  244  ? 5.739   12.022  123.367 1.00 19.48 ? 242  SER   B O     1 
ATOM   10674 C  CB    A SER   B  1  244  ? 8.391   13.730  122.372 0.56 20.66 ? 242  SER   B CB    1 
ATOM   10675 C  CB    B SER   B  1  244  ? 8.408   13.702  122.421 0.44 20.70 ? 242  SER   B CB    1 
ATOM   10676 O  OG    A SER   B  1  244  ? 8.061   14.210  123.657 0.56 24.44 ? 242  SER   B OG    1 
ATOM   10677 O  OG    B SER   B  1  244  ? 9.822   13.605  122.363 0.44 21.03 ? 242  SER   B OG    1 
ATOM   10678 N  N     . ALA   B  1  245  ? 5.515   12.977  121.343 1.00 20.14 ? 243  ALA   B N     1 
ATOM   10679 C  CA    . ALA   B  1  245  ? 4.071   13.080  121.480 1.00 20.18 ? 243  ALA   B CA    1 
ATOM   10680 C  C     . ALA   B  1  245  ? 3.425   11.704  121.512 1.00 21.28 ? 243  ALA   B C     1 
ATOM   10681 O  O     . ALA   B  1  245  ? 2.476   11.482  122.265 1.00 21.53 ? 243  ALA   B O     1 
ATOM   10682 C  CB    . ALA   B  1  245  ? 3.509   13.903  120.328 1.00 21.07 ? 243  ALA   B CB    1 
ATOM   10683 N  N     . ILE   B  1  246  ? 3.921   10.771  120.699 1.00 20.00 ? 244  ILE   B N     1 
ATOM   10684 C  CA    . ILE   B  1  246  ? 3.362   9.421   120.709 1.00 20.57 ? 244  ILE   B CA    1 
ATOM   10685 C  C     . ILE   B  1  246  ? 3.492   8.790   122.082 1.00 21.93 ? 244  ILE   B C     1 
ATOM   10686 O  O     . ILE   B  1  246  ? 2.547   8.172   122.580 1.00 22.65 ? 244  ILE   B O     1 
ATOM   10687 C  CB    . ILE   B  1  246  ? 3.989   8.552   119.609 1.00 21.40 ? 244  ILE   B CB    1 
ATOM   10688 C  CG1   . ILE   B  1  246  ? 3.509   9.044   118.248 1.00 21.63 ? 244  ILE   B CG1   1 
ATOM   10689 C  CG2   . ILE   B  1  246  ? 3.623   7.089   119.827 1.00 23.07 ? 244  ILE   B CG2   1 
ATOM   10690 C  CD1   . ILE   B  1  246  ? 4.194   8.385   117.069 1.00 22.40 ? 244  ILE   B CD1   1 
ATOM   10691 N  N     . HIS   B  1  247  ? 4.655   8.932   122.721 1.00 22.14 ? 245  HIS   B N     1 
ATOM   10692 C  CA    . HIS   B  1  247  ? 4.796   8.406   124.075 1.00 21.48 ? 245  HIS   B CA    1 
ATOM   10693 C  C     . HIS   B  1  247  ? 3.782   9.027   125.024 1.00 22.20 ? 245  HIS   B C     1 
ATOM   10694 O  O     . HIS   B  1  247  ? 3.158   8.318   125.814 1.00 23.21 ? 245  HIS   B O     1 
ATOM   10695 C  CB    . HIS   B  1  247  ? 6.222   8.592   124.593 1.00 22.80 ? 245  HIS   B CB    1 
ATOM   10696 C  CG    . HIS   B  1  247  ? 7.212   7.681   123.941 1.00 24.34 ? 245  HIS   B CG    1 
ATOM   10697 N  ND1   . HIS   B  1  247  ? 7.186   6.314   124.116 1.00 23.36 ? 245  HIS   B ND1   1 
ATOM   10698 C  CD2   . HIS   B  1  247  ? 8.252   7.937   123.115 1.00 26.91 ? 245  HIS   B CD2   1 
ATOM   10699 C  CE1   . HIS   B  1  247  ? 8.162   5.766   123.415 1.00 26.27 ? 245  HIS   B CE1   1 
ATOM   10700 N  NE2   . HIS   B  1  247  ? 8.825   6.729   122.801 1.00 28.84 ? 245  HIS   B NE2   1 
ATOM   10701 N  N     . ALA   B  1  248  ? 3.576   10.341  124.942 1.00 20.81 ? 246  ALA   B N     1 
ATOM   10702 C  CA    . ALA   B  1  248  ? 2.634   10.974  125.857 1.00 22.21 ? 246  ALA   B CA    1 
ATOM   10703 C  C     . ALA   B  1  248  ? 1.202   10.569  125.533 1.00 22.13 ? 246  ALA   B C     1 
ATOM   10704 O  O     . ALA   B  1  248  ? 0.417   10.239  126.428 1.00 22.02 ? 246  ALA   B O     1 
ATOM   10705 C  CB    . ALA   B  1  248  ? 2.780   12.494  125.782 1.00 23.73 ? 246  ALA   B CB    1 
ATOM   10706 N  N     . ILE   B  1  249  ? 0.842   10.604  124.254 1.00 23.02 ? 247  ILE   B N     1 
ATOM   10707 C  CA    . ILE   B  1  249  ? -0.508  10.223  123.850 1.00 23.28 ? 247  ILE   B CA    1 
ATOM   10708 C  C     . ILE   B  1  249  ? -0.754  8.754   124.153 1.00 21.40 ? 247  ILE   B C     1 
ATOM   10709 O  O     . ILE   B  1  249  ? -1.834  8.373   124.624 1.00 24.06 ? 247  ILE   B O     1 
ATOM   10710 C  CB    . ILE   B  1  249  ? -0.707  10.527  122.357 1.00 21.35 ? 247  ILE   B CB    1 
ATOM   10711 C  CG1   . ILE   B  1  249  ? -0.626  12.025  122.089 1.00 19.78 ? 247  ILE   B CG1   1 
ATOM   10712 C  CG2   . ILE   B  1  249  ? -2.040  9.938   121.868 1.00 22.89 ? 247  ILE   B CG2   1 
ATOM   10713 C  CD1   . ILE   B  1  249  ? -0.266  12.352  120.658 1.00 22.08 ? 247  ILE   B CD1   1 
ATOM   10714 N  N     . GLY   B  1  250  ? 0.241   7.910   123.876 1.00 23.81 ? 248  GLY   B N     1 
ATOM   10715 C  CA    . GLY   B  1  250  ? 0.089   6.490   124.114 1.00 23.96 ? 248  GLY   B CA    1 
ATOM   10716 C  C     . GLY   B  1  250  ? -0.097  6.165   125.580 1.00 26.38 ? 248  GLY   B C     1 
ATOM   10717 O  O     . GLY   B  1  250  ? -0.956  5.359   125.944 1.00 25.89 ? 248  GLY   B O     1 
ATOM   10718 N  N     . LYS   B  1  251  ? 0.700   6.793   126.446 1.00 24.00 ? 249  LYS   B N     1 
ATOM   10719 C  CA    . LYS   B  1  251  ? 0.513   6.579   127.876 1.00 26.92 ? 249  LYS   B CA    1 
ATOM   10720 C  C     . LYS   B  1  251  ? -0.840  7.108   128.338 1.00 23.43 ? 249  LYS   B C     1 
ATOM   10721 O  O     . LYS   B  1  251  ? -1.520  6.464   129.144 1.00 28.39 ? 249  LYS   B O     1 
ATOM   10722 C  CB    . LYS   B  1  251  ? 1.656   7.225   128.660 1.00 28.70 ? 249  LYS   B CB    1 
ATOM   10723 N  N     . ALA   B  1  252  ? -1.261  8.261   127.809 1.00 26.24 ? 250  ALA   B N     1 
ATOM   10724 C  CA    . ALA   B  1  252  ? -2.562  8.814   128.184 1.00 24.69 ? 250  ALA   B CA    1 
ATOM   10725 C  C     . ALA   B  1  252  ? -3.706  7.952   127.667 1.00 26.78 ? 250  ALA   B C     1 
ATOM   10726 O  O     . ALA   B  1  252  ? -4.737  7.818   128.334 1.00 28.19 ? 250  ALA   B O     1 
ATOM   10727 C  CB    . ALA   B  1  252  ? -2.699  10.246  127.673 1.00 26.94 ? 250  ALA   B CB    1 
ATOM   10728 N  N     . SER   B  1  253  ? -3.552  7.373   126.476 1.00 26.12 ? 251  SER   B N     1 
ATOM   10729 C  CA    . SER   B  1  253  ? -4.582  6.480   125.958 1.00 27.56 ? 251  SER   B CA    1 
ATOM   10730 C  C     . SER   B  1  253  ? -4.856  5.350   126.934 1.00 26.91 ? 251  SER   B C     1 
ATOM   10731 O  O     . SER   B  1  253  ? -6.018  5.017   127.201 1.00 29.41 ? 251  SER   B O     1 
ATOM   10732 C  CB    . SER   B  1  253  ? -4.141  5.902   124.623 1.00 25.65 ? 251  SER   B CB    1 
ATOM   10733 O  OG    . SER   B  1  253  ? -5.118  4.995   124.136 1.00 27.57 ? 251  SER   B OG    1 
ATOM   10734 N  N     . ALA   B  1  254  ? -3.797  4.749   127.477 1.00 27.45 ? 252  ALA   B N     1 
ATOM   10735 C  CA    . ALA   B  1  254  ? -3.905  3.749   128.537 1.00 29.35 ? 252  ALA   B CA    1 
ATOM   10736 C  C     . ALA   B  1  254  ? -4.810  2.588   128.128 1.00 33.36 ? 252  ALA   B C     1 
ATOM   10737 O  O     . ALA   B  1  254  ? -5.697  2.161   128.870 1.00 35.70 ? 252  ALA   B O     1 
ATOM   10738 C  CB    . ALA   B  1  254  ? -4.349  4.377   129.858 1.00 31.04 ? 252  ALA   B CB    1 
ATOM   10739 N  N     . GLY   B  1  255  ? -4.582  2.082   126.918 1.00 33.14 ? 253  GLY   B N     1 
ATOM   10740 C  CA    . GLY   B  1  255  ? -5.303  0.924   126.440 1.00 32.40 ? 253  GLY   B CA    1 
ATOM   10741 C  C     . GLY   B  1  255  ? -6.717  1.177   125.973 1.00 32.54 ? 253  GLY   B C     1 
ATOM   10742 O  O     . GLY   B  1  255  ? -7.453  0.213   125.747 1.00 36.33 ? 253  GLY   B O     1 
ATOM   10743 N  N     . ARG   B  1  256  ? -7.128  2.438   125.819 1.00 29.92 ? 254  ARG   B N     1 
ATOM   10744 C  CA    . ARG   B  1  256  ? -8.475  2.713   125.331 1.00 32.28 ? 254  ARG   B CA    1 
ATOM   10745 C  C     . ARG   B  1  256  ? -8.671  2.311   123.878 1.00 31.91 ? 254  ARG   B C     1 
ATOM   10746 O  O     . ARG   B  1  256  ? -9.818  2.238   123.422 1.00 31.48 ? 254  ARG   B O     1 
ATOM   10747 C  CB    . ARG   B  1  256  ? -8.838  4.185   125.519 1.00 30.61 ? 254  ARG   B CB    1 
ATOM   10748 C  CG    . ARG   B  1  256  ? -9.303  4.519   126.927 1.00 27.93 ? 254  ARG   B CG    1 
ATOM   10749 C  CD    . ARG   B  1  256  ? -9.592  5.991   127.033 1.00 28.04 ? 254  ARG   B CD    1 
ATOM   10750 N  NE    . ARG   B  1  256  ? -8.353  6.758   127.066 1.00 28.99 ? 254  ARG   B NE    1 
ATOM   10751 C  CZ    . ARG   B  1  256  ? -8.283  8.073   126.934 1.00 29.44 ? 254  ARG   B CZ    1 
ATOM   10752 N  NH1   . ARG   B  1  256  ? -9.353  8.796   126.646 1.00 33.11 ? 254  ARG   B NH1   1 
ATOM   10753 N  NH2   . ARG   B  1  256  ? -7.108  8.679   127.099 1.00 31.04 ? 254  ARG   B NH2   1 
ATOM   10754 N  N     . GLY   B  1  257  ? -7.596  2.043   123.149 1.00 31.71 ? 255  GLY   B N     1 
ATOM   10755 C  CA    . GLY   B  1  257  ? -7.718  1.603   121.776 1.00 28.95 ? 255  GLY   B CA    1 
ATOM   10756 C  C     . GLY   B  1  257  ? -7.867  2.754   120.803 1.00 28.58 ? 255  GLY   B C     1 
ATOM   10757 O  O     . GLY   B  1  257  ? -7.940  3.928   121.167 1.00 28.49 ? 255  GLY   B O     1 
ATOM   10758 N  N     . ILE   B  1  258  ? -7.938  2.397   119.523 1.00 29.31 ? 256  ILE   B N     1 
ATOM   10759 C  CA    . ILE   B  1  258  ? -7.831  3.408   118.478 1.00 26.93 ? 256  ILE   B CA    1 
ATOM   10760 C  C     . ILE   B  1  258  ? -9.109  4.217   118.273 1.00 24.91 ? 256  ILE   B C     1 
ATOM   10761 O  O     . ILE   B  1  258  ? -9.055  5.290   117.660 1.00 26.71 ? 256  ILE   B O     1 
ATOM   10762 C  CB    . ILE   B  1  258  ? -7.381  2.769   117.158 1.00 30.93 ? 256  ILE   B CB    1 
ATOM   10763 C  CG1   . ILE   B  1  258  ? -8.403  1.723   116.717 1.00 29.76 ? 256  ILE   B CG1   1 
ATOM   10764 C  CG2   . ILE   B  1  258  ? -6.004  2.135   117.318 1.00 29.24 ? 256  ILE   B CG2   1 
ATOM   10765 C  CD1   . ILE   B  1  258  ? -8.081  1.094   115.391 1.00 29.72 ? 256  ILE   B CD1   1 
ATOM   10766 N  N     . TYR   B  1  259  ? -10.255 3.745   118.768 1.00 28.02 ? 257  TYR   B N     1 
ATOM   10767 C  CA    . TYR   B  1  259  ? -11.524 4.434   118.539 1.00 28.56 ? 257  TYR   B CA    1 
ATOM   10768 C  C     . TYR   B  1  259  ? -11.868 5.382   119.684 1.00 29.46 ? 257  TYR   B C     1 
ATOM   10769 O  O     . TYR   B  1  259  ? -12.064 6.583   119.467 1.00 27.89 ? 257  TYR   B O     1 
ATOM   10770 C  CB    . TYR   B  1  259  ? -12.644 3.410   118.293 1.00 30.41 ? 257  TYR   B CB    1 
ATOM   10771 C  CG    . TYR   B  1  259  ? -12.275 2.450   117.191 1.00 29.37 ? 257  TYR   B CG    1 
ATOM   10772 C  CD1   . TYR   B  1  259  ? -12.155 2.891   115.882 1.00 30.29 ? 257  TYR   B CD1   1 
ATOM   10773 C  CD2   . TYR   B  1  259  ? -12.006 1.116   117.460 1.00 32.80 ? 257  TYR   B CD2   1 
ATOM   10774 C  CE1   . TYR   B  1  259  ? -11.789 2.030   114.865 1.00 30.95 ? 257  TYR   B CE1   1 
ATOM   10775 C  CE2   . TYR   B  1  259  ? -11.641 0.244   116.447 1.00 29.23 ? 257  TYR   B CE2   1 
ATOM   10776 C  CZ    . TYR   B  1  259  ? -11.537 0.708   115.156 1.00 33.97 ? 257  TYR   B CZ    1 
ATOM   10777 O  OH    . TYR   B  1  259  ? -11.172 -0.154  114.151 1.00 32.09 ? 257  TYR   B OH    1 
ATOM   10778 N  N     . GLU   B  1  260  ? -11.933 4.857   120.908 1.00 28.17 ? 258  GLU   B N     1 
ATOM   10779 C  CA    . GLU   B  1  260  ? -12.185 5.718   122.056 1.00 31.12 ? 258  GLU   B CA    1 
ATOM   10780 C  C     . GLU   B  1  260  ? -10.966 6.570   122.377 1.00 32.47 ? 258  GLU   B C     1 
ATOM   10781 O  O     . GLU   B  1  260  ? -11.097 7.747   122.742 1.00 32.22 ? 258  GLU   B O     1 
ATOM   10782 C  CB    . GLU   B  1  260  ? -12.569 4.879   123.274 1.00 30.17 ? 258  GLU   B CB    1 
ATOM   10783 C  CG    . GLU   B  1  260  ? -12.755 5.706   124.535 1.00 37.83 ? 258  GLU   B CG    1 
ATOM   10784 C  CD    . GLU   B  1  260  ? -13.016 4.858   125.760 1.00 38.71 ? 258  GLU   B CD    1 
ATOM   10785 O  OE1   . GLU   B  1  260  ? -13.157 3.625   125.607 1.00 46.64 ? 258  GLU   B OE1   1 
ATOM   10786 O  OE2   . GLU   B  1  260  ? -13.079 5.425   126.875 1.00 42.84 ? 258  GLU   B OE2   1 
ATOM   10787 N  N     . GLY   B  1  261  ? -9.778  5.998   122.234 1.00 29.71 ? 259  GLY   B N     1 
ATOM   10788 C  CA    . GLY   B  1  261  ? -8.569  6.640   122.679 1.00 26.93 ? 259  GLY   B CA    1 
ATOM   10789 C  C     . GLY   B  1  261  ? -8.002  7.606   121.664 1.00 24.94 ? 259  GLY   B C     1 
ATOM   10790 O  O     . GLY   B  1  261  ? -8.347  7.589   120.478 1.00 25.72 ? 259  GLY   B O     1 
ATOM   10791 N  N     . PRO   B  1  262  ? -7.107  8.470   122.126 1.00 24.65 ? 260  PRO   B N     1 
ATOM   10792 C  CA    . PRO   B  1  262  ? -6.552  9.508   121.256 1.00 24.74 ? 260  PRO   B CA    1 
ATOM   10793 C  C     . PRO   B  1  262  ? -5.551  8.938   120.267 1.00 24.48 ? 260  PRO   B C     1 
ATOM   10794 O  O     . PRO   B  1  262  ? -4.989  7.855   120.444 1.00 26.53 ? 260  PRO   B O     1 
ATOM   10795 C  CB    . PRO   B  1  262  ? -5.848  10.446  122.248 1.00 24.86 ? 260  PRO   B CB    1 
ATOM   10796 C  CG    . PRO   B  1  262  ? -5.482  9.559   123.390 1.00 25.07 ? 260  PRO   B CG    1 
ATOM   10797 C  CD    . PRO   B  1  262  ? -6.622  8.582   123.509 1.00 24.75 ? 260  PRO   B CD    1 
ATOM   10798 N  N     . GLY   B  1  263  ? -5.327  9.706   119.214 1.00 21.90 ? 261  GLY   B N     1 
ATOM   10799 C  CA    . GLY   B  1  263  ? -4.321  9.356   118.236 1.00 22.19 ? 261  GLY   B CA    1 
ATOM   10800 C  C     . GLY   B  1  263  ? -3.450  10.539  117.878 1.00 21.14 ? 261  GLY   B C     1 
ATOM   10801 O  O     . GLY   B  1  263  ? -3.532  11.614  118.486 1.00 21.45 ? 261  GLY   B O     1 
ATOM   10802 N  N     . ILE   B  1  264  ? -2.622  10.353  116.868 1.00 21.13 ? 262  ILE   B N     1 
ATOM   10803 C  CA    . ILE   B  1  264  ? -1.752  11.413  116.393 1.00 20.49 ? 262  ILE   B CA    1 
ATOM   10804 C  C     . ILE   B  1  264  ? -1.905  11.528  114.885 1.00 21.12 ? 262  ILE   B C     1 
ATOM   10805 O  O     . ILE   B  1  264  ? -2.245  10.558  114.201 1.00 21.45 ? 262  ILE   B O     1 
ATOM   10806 C  CB    . ILE   B  1  264  ? -0.289  11.142  116.805 1.00 21.90 ? 262  ILE   B CB    1 
ATOM   10807 C  CG1   . ILE   B  1  264  ? 0.558   12.396  116.607 1.00 20.21 ? 262  ILE   B CG1   1 
ATOM   10808 C  CG2   . ILE   B  1  264  ? 0.268   9.977   116.005 1.00 21.19 ? 262  ILE   B CG2   1 
ATOM   10809 C  CD1   . ILE   B  1  264  ? 1.978   12.275  117.142 1.00 21.98 ? 262  ILE   B CD1   1 
ATOM   10810 N  N     . SER   B  1  265  ? -1.691  12.735  114.372 1.00 17.95 ? 263  SER   B N     1 
ATOM   10811 C  CA    . SER   B  1  265  ? -1.700  13.001  112.941 1.00 18.52 ? 263  SER   B CA    1 
ATOM   10812 C  C     . SER   B  1  265  ? -0.337  13.555  112.572 1.00 20.58 ? 263  SER   B C     1 
ATOM   10813 O  O     . SER   B  1  265  ? 0.199   14.409  113.286 1.00 22.36 ? 263  SER   B O     1 
ATOM   10814 C  CB    . SER   B  1  265  ? -2.762  14.035  112.568 1.00 22.56 ? 263  SER   B CB    1 
ATOM   10815 O  OG    . SER   B  1  265  ? -4.060  13.462  112.566 1.00 21.90 ? 263  SER   B OG    1 
ATOM   10816 N  N     . ILE   B  1  266  ? 0.232   13.053  111.480 1.00 18.09 ? 264  ILE   B N     1 
ATOM   10817 C  CA    . ILE   B  1  266  ? 1.538   13.498  111.017 1.00 19.52 ? 264  ILE   B CA    1 
ATOM   10818 C  C     . ILE   B  1  266  ? 1.427   13.963  109.576 1.00 18.90 ? 264  ILE   B C     1 
ATOM   10819 O  O     . ILE   B  1  266  ? 0.507   13.597  108.843 1.00 18.60 ? 264  ILE   B O     1 
ATOM   10820 C  CB    . ILE   B  1  266  ? 2.620   12.406  111.138 1.00 19.99 ? 264  ILE   B CB    1 
ATOM   10821 C  CG1   . ILE   B  1  266  ? 2.313   11.241  110.192 1.00 23.73 ? 264  ILE   B CG1   1 
ATOM   10822 C  CG2   . ILE   B  1  266  ? 2.714   11.917  112.565 1.00 20.55 ? 264  ILE   B CG2   1 
ATOM   10823 C  CD1   . ILE   B  1  266  ? 3.444   10.232  110.067 1.00 23.76 ? 264  ILE   B CD1   1 
ATOM   10824 N  N     . LYS   B  1  267  ? 2.405   14.753  109.161 1.00 17.29 ? 265  LYS   B N     1 
ATOM   10825 C  CA    . LYS   B  1  267  ? 2.541   15.137  107.769 1.00 16.92 ? 265  LYS   B CA    1 
ATOM   10826 C  C     . LYS   B  1  267  ? 3.859   14.585  107.253 1.00 16.54 ? 265  LYS   B C     1 
ATOM   10827 O  O     . LYS   B  1  267  ? 4.901   14.769  107.887 1.00 17.81 ? 265  LYS   B O     1 
ATOM   10828 C  CB    . LYS   B  1  267  ? 2.489   16.654  107.618 1.00 17.60 ? 265  LYS   B CB    1 
ATOM   10829 C  CG    . LYS   B  1  267  ? 1.073   17.209  107.729 1.00 21.89 ? 265  LYS   B CG    1 
ATOM   10830 C  CD    . LYS   B  1  267  ? 1.068   18.724  107.728 1.00 25.77 ? 265  LYS   B CD    1 
ATOM   10831 C  CE    . LYS   B  1  267  ? -0.334  19.274  107.962 1.00 27.92 ? 265  LYS   B CE    1 
ATOM   10832 N  NZ    . LYS   B  1  267  ? -0.923  18.812  109.249 1.00 27.96 ? 265  LYS   B NZ    1 
ATOM   10833 N  N     . LEU   B  1  268  ? 3.805   13.867  106.134 1.00 16.33 ? 266  LEU   B N     1 
ATOM   10834 C  CA    . LEU   B  1  268  ? 5.040   13.347  105.556 1.00 18.19 ? 266  LEU   B CA    1 
ATOM   10835 C  C     . LEU   B  1  268  ? 6.023   14.456  105.213 1.00 18.28 ? 266  LEU   B C     1 
ATOM   10836 O  O     . LEU   B  1  268  ? 7.236   14.269  105.351 1.00 17.32 ? 266  LEU   B O     1 
ATOM   10837 C  CB    . LEU   B  1  268  ? 4.735   12.481  104.338 1.00 17.20 ? 266  LEU   B CB    1 
ATOM   10838 C  CG    . LEU   B  1  268  ? 3.858   11.265  104.656 1.00 19.80 ? 266  LEU   B CG    1 
ATOM   10839 C  CD1   . LEU   B  1  268  ? 3.705   10.373  103.435 1.00 20.20 ? 266  LEU   B CD1   1 
ATOM   10840 C  CD2   . LEU   B  1  268  ? 4.424   10.474  105.821 1.00 22.68 ? 266  LEU   B CD2   1 
ATOM   10841 N  N     . SER   B  1  269  ? 5.533   15.628  104.806 1.00 17.78 ? 267  SER   B N     1 
ATOM   10842 C  CA    . SER   B  1  269  ? 6.441   16.724  104.492 1.00 19.07 ? 267  SER   B CA    1 
ATOM   10843 C  C     . SER   B  1  269  ? 7.211   17.204  105.713 1.00 17.14 ? 267  SER   B C     1 
ATOM   10844 O  O     . SER   B  1  269  ? 8.256   17.848  105.556 1.00 17.70 ? 267  SER   B O     1 
ATOM   10845 C  CB    . SER   B  1  269  ? 5.681   17.910  103.903 1.00 18.59 ? 267  SER   B CB    1 
ATOM   10846 O  OG    . SER   B  1  269  ? 4.884   18.529  104.907 1.00 19.19 ? 267  SER   B OG    1 
ATOM   10847 N  N     . ALA   B  1  270  ? 6.719   16.924  106.924 1.00 15.94 ? 268  ALA   B N     1 
ATOM   10848 C  CA    . ALA   B  1  270  ? 7.475   17.254  108.123 1.00 18.11 ? 268  ALA   B CA    1 
ATOM   10849 C  C     . ALA   B  1  270  ? 8.700   16.370  108.276 1.00 18.38 ? 268  ALA   B C     1 
ATOM   10850 O  O     . ALA   B  1  270  ? 9.648   16.747  108.979 1.00 18.11 ? 268  ALA   B O     1 
ATOM   10851 C  CB    . ALA   B  1  270  ? 6.597   17.051  109.362 1.00 17.53 ? 268  ALA   B CB    1 
ATOM   10852 N  N     . LEU   B  1  271  ? 8.695   15.194  107.658 1.00 17.38 ? 269  LEU   B N     1 
ATOM   10853 C  CA    . LEU   B  1  271  ? 9.669   14.173  107.996 1.00 19.32 ? 269  LEU   B CA    1 
ATOM   10854 C  C     . LEU   B  1  271  ? 10.834  14.106  107.030 1.00 17.58 ? 269  LEU   B C     1 
ATOM   10855 O  O     . LEU   B  1  271  ? 11.759  13.323  107.257 1.00 19.54 ? 269  LEU   B O     1 
ATOM   10856 C  CB    . LEU   B  1  271  ? 9.000   12.813  108.131 1.00 18.84 ? 269  LEU   B CB    1 
ATOM   10857 C  CG    . LEU   B  1  271  ? 8.033   12.746  109.310 1.00 20.05 ? 269  LEU   B CG    1 
ATOM   10858 C  CD1   . LEU   B  1  271  ? 7.292   11.420  109.272 1.00 22.48 ? 269  LEU   B CD1   1 
ATOM   10859 C  CD2   . LEU   B  1  271  ? 8.796   12.918  110.621 1.00 19.52 ? 269  LEU   B CD2   1 
ATOM   10860 N  N     . HIS   B  1  272  ? 10.826  14.918  105.975 1.00 16.11 ? 270  HIS   B N     1 
ATOM   10861 C  CA    . HIS   B  1  272  ? 11.961  14.907  105.075 1.00 17.49 ? 270  HIS   B CA    1 
ATOM   10862 C  C     . HIS   B  1  272  ? 11.931  16.222  104.326 1.00 15.98 ? 270  HIS   B C     1 
ATOM   10863 O  O     . HIS   B  1  272  ? 10.850  16.656  103.916 1.00 18.38 ? 270  HIS   B O     1 
ATOM   10864 C  CB    . HIS   B  1  272  ? 11.858  13.744  104.089 1.00 19.50 ? 270  HIS   B CB    1 
ATOM   10865 C  CG    . HIS   B  1  272  ? 13.161  13.427  103.436 1.00 17.95 ? 270  HIS   B CG    1 
ATOM   10866 N  ND1   . HIS   B  1  272  ? 13.669  14.175  102.395 1.00 21.82 ? 270  HIS   B ND1   1 
ATOM   10867 C  CD2   . HIS   B  1  272  ? 14.097  12.492  103.724 1.00 23.43 ? 270  HIS   B CD2   1 
ATOM   10868 C  CE1   . HIS   B  1  272  ? 14.853  13.698  102.054 1.00 23.44 ? 270  HIS   B CE1   1 
ATOM   10869 N  NE2   . HIS   B  1  272  ? 15.135  12.673  102.841 1.00 22.96 ? 270  HIS   B NE2   1 
ATOM   10870 N  N     . PRO   B  1  273  ? 13.080  16.867  104.111 1.00 16.25 ? 271  PRO   B N     1 
ATOM   10871 C  CA    . PRO   B  1  273  ? 13.089  18.145  103.386 1.00 16.78 ? 271  PRO   B CA    1 
ATOM   10872 C  C     . PRO   B  1  273  ? 12.889  18.005  101.888 1.00 16.74 ? 271  PRO   B C     1 
ATOM   10873 O  O     . PRO   B  1  273  ? 12.678  19.020  101.221 1.00 18.41 ? 271  PRO   B O     1 
ATOM   10874 C  CB    . PRO   B  1  273  ? 14.480  18.708  103.697 1.00 19.31 ? 271  PRO   B CB    1 
ATOM   10875 C  CG    . PRO   B  1  273  ? 15.309  17.500  103.949 1.00 19.55 ? 271  PRO   B CG    1 
ATOM   10876 C  CD    . PRO   B  1  273  ? 14.403  16.521  104.649 1.00 17.79 ? 271  PRO   B CD    1 
ATOM   10877 N  N     . ARG   B  1  274  ? 12.924  16.797  101.343 1.00 16.57 ? 272  ARG   B N     1 
ATOM   10878 C  CA    . ARG   B  1  274  ? 12.733  16.584  99.916  1.00 18.80 ? 272  ARG   B CA    1 
ATOM   10879 C  C     . ARG   B  1  274  ? 11.633  15.571  99.685  1.00 18.18 ? 272  ARG   B C     1 
ATOM   10880 O  O     . ARG   B  1  274  ? 11.790  14.584  98.966  1.00 18.99 ? 272  ARG   B O     1 
ATOM   10881 C  CB    . ARG   B  1  274  ? 14.027  16.157  99.228  1.00 17.79 ? 272  ARG   B CB    1 
ATOM   10882 C  CG    . ARG   B  1  274  ? 15.159  17.187  99.285  1.00 18.87 ? 272  ARG   B CG    1 
ATOM   10883 C  CD    . ARG   B  1  274  ? 14.764  18.526  98.690  1.00 20.38 ? 272  ARG   B CD    1 
ATOM   10884 N  NE    . ARG   B  1  274  ? 14.291  18.417  97.315  1.00 18.96 ? 272  ARG   B NE    1 
ATOM   10885 C  CZ    . ARG   B  1  274  ? 15.079  18.301  96.255  1.00 17.97 ? 272  ARG   B CZ    1 
ATOM   10886 N  NH1   . ARG   B  1  274  ? 16.394  18.203  96.379  1.00 18.57 ? 272  ARG   B NH1   1 
ATOM   10887 N  NH2   . ARG   B  1  274  ? 14.538  18.289  95.044  1.00 19.68 ? 272  ARG   B NH2   1 
ATOM   10888 N  N     . TYR   B  1  275  ? 10.485  15.800  100.314 1.00 17.09 ? 273  TYR   B N     1 
ATOM   10889 C  CA    . TYR   B  1  275  ? 9.329   14.933  100.125 1.00 18.44 ? 273  TYR   B CA    1 
ATOM   10890 C  C     . TYR   B  1  275  ? 8.671   15.287  98.793  1.00 19.10 ? 273  TYR   B C     1 
ATOM   10891 O  O     . TYR   B  1  275  ? 7.836   16.186  98.698  1.00 18.11 ? 273  TYR   B O     1 
ATOM   10892 C  CB    . TYR   B  1  275  ? 8.371   15.079  101.299 1.00 16.20 ? 273  TYR   B CB    1 
ATOM   10893 C  CG    . TYR   B  1  275  ? 7.118   14.288  101.128 1.00 16.33 ? 273  TYR   B CG    1 
ATOM   10894 C  CD1   . TYR   B  1  275  ? 7.169   12.957  100.748 1.00 17.28 ? 273  TYR   B CD1   1 
ATOM   10895 C  CD2   . TYR   B  1  275  ? 5.881   14.868  101.348 1.00 17.45 ? 273  TYR   B CD2   1 
ATOM   10896 C  CE1   . TYR   B  1  275  ? 6.016   12.226  100.580 1.00 18.64 ? 273  TYR   B CE1   1 
ATOM   10897 C  CE2   . TYR   B  1  275  ? 4.730   14.150  101.194 1.00 16.11 ? 273  TYR   B CE2   1 
ATOM   10898 C  CZ    . TYR   B  1  275  ? 4.802   12.824  100.805 1.00 18.48 ? 273  TYR   B CZ    1 
ATOM   10899 O  OH    . TYR   B  1  275  ? 3.668   12.080  100.625 1.00 19.92 ? 273  TYR   B OH    1 
ATOM   10900 N  N     . SER   B  1  276  ? 9.054   14.573  97.740  1.00 17.44 ? 274  SER   B N     1 
ATOM   10901 C  CA    . SER   B  1  276  ? 8.504   14.866  96.425  1.00 17.10 ? 274  SER   B CA    1 
ATOM   10902 C  C     . SER   B  1  276  ? 8.758   13.676  95.521  1.00 17.55 ? 274  SER   B C     1 
ATOM   10903 O  O     . SER   B  1  276  ? 9.660   12.873  95.764  1.00 17.30 ? 274  SER   B O     1 
ATOM   10904 C  CB    . SER   B  1  276  ? 9.137   16.111  95.812  1.00 21.64 ? 274  SER   B CB    1 
ATOM   10905 O  OG    . SER   B  1  276  ? 10.462  15.838  95.424  1.00 23.88 ? 274  SER   B OG    1 
ATOM   10906 N  N     . ARG   B  1  277  ? 7.945   13.577  94.471  1.00 16.27 ? 275  ARG   B N     1 
ATOM   10907 C  CA    . ARG   B  1  277  ? 8.118   12.491  93.523  1.00 16.08 ? 275  ARG   B CA    1 
ATOM   10908 C  C     . ARG   B  1  277  ? 9.491   12.537  92.878  1.00 17.45 ? 275  ARG   B C     1 
ATOM   10909 O  O     . ARG   B  1  277  ? 10.070  11.484  92.594  1.00 17.46 ? 275  ARG   B O     1 
ATOM   10910 C  CB    . ARG   B  1  277  ? 7.015   12.550  92.468  1.00 17.26 ? 275  ARG   B CB    1 
ATOM   10911 C  CG    . ARG   B  1  277  ? 7.190   11.576  91.308  1.00 18.55 ? 275  ARG   B CG    1 
ATOM   10912 C  CD    . ARG   B  1  277  ? 7.247   10.141  91.805  1.00 17.46 ? 275  ARG   B CD    1 
ATOM   10913 N  NE    . ARG   B  1  277  ? 7.391   9.205   90.700  1.00 19.10 ? 275  ARG   B NE    1 
ATOM   10914 C  CZ    . ARG   B  1  277  ? 8.553   8.843   90.176  1.00 17.66 ? 275  ARG   B CZ    1 
ATOM   10915 N  NH1   . ARG   B  1  277  ? 9.699   9.343   90.616  1.00 20.54 ? 275  ARG   B NH1   1 
ATOM   10916 N  NH2   . ARG   B  1  277  ? 8.561   7.947   89.192  1.00 18.87 ? 275  ARG   B NH2   1 
ATOM   10917 N  N     . ALA   B  1  278  ? 10.027  13.739  92.655  1.00 17.01 ? 276  ALA   B N     1 
ATOM   10918 C  CA    . ALA   B  1  278  ? 11.344  13.856  92.044  1.00 16.05 ? 276  ALA   B CA    1 
ATOM   10919 C  C     . ALA   B  1  278  ? 12.409  13.219  92.913  1.00 17.48 ? 276  ALA   B C     1 
ATOM   10920 O  O     . ALA   B  1  278  ? 13.460  12.813  92.405  1.00 18.86 ? 276  ALA   B O     1 
ATOM   10921 C  CB    . ALA   B  1  278  ? 11.685  15.322  91.781  1.00 20.33 ? 276  ALA   B CB    1 
ATOM   10922 N  N     . GLN   B  1  279  ? 12.175  13.137  94.221  1.00 18.03 ? 277  GLN   B N     1 
ATOM   10923 C  CA    . GLN   B  1  279  ? 13.117  12.515  95.142  1.00 16.83 ? 277  GLN   B CA    1 
ATOM   10924 C  C     . GLN   B  1  279  ? 12.563  11.221  95.726  1.00 17.73 ? 277  GLN   B C     1 
ATOM   10925 O  O     . GLN   B  1  279  ? 12.823  10.898  96.887  1.00 17.70 ? 277  GLN   B O     1 
ATOM   10926 C  CB    . GLN   B  1  279  ? 13.528  13.487  96.247  1.00 18.70 ? 277  GLN   B CB    1 
ATOM   10927 C  CG    . GLN   B  1  279  ? 14.143  14.758  95.699  1.00 18.80 ? 277  GLN   B CG    1 
ATOM   10928 C  CD    . GLN   B  1  279  ? 15.443  14.486  94.969  1.00 21.66 ? 277  GLN   B CD    1 
ATOM   10929 O  OE1   . GLN   B  1  279  ? 16.130  13.498  95.244  1.00 25.53 ? 277  GLN   B OE1   1 
ATOM   10930 N  NE2   . GLN   B  1  279  ? 15.778  15.350  94.017  1.00 20.13 ? 277  GLN   B NE2   1 
ATOM   10931 N  N     . ALA   B  1  280  ? 11.800  10.470  94.931  1.00 18.40 ? 278  ALA   B N     1 
ATOM   10932 C  CA    . ALA   B  1  280  ? 11.112  9.301   95.462  1.00 19.62 ? 278  ALA   B CA    1 
ATOM   10933 C  C     . ALA   B  1  280  ? 12.074  8.313   96.110  1.00 19.76 ? 278  ALA   B C     1 
ATOM   10934 O  O     . ALA   B  1  280  ? 11.746  7.716   97.139  1.00 19.96 ? 278  ALA   B O     1 
ATOM   10935 C  CB    . ALA   B  1  280  ? 10.302  8.623   94.359  1.00 20.21 ? 278  ALA   B CB    1 
ATOM   10936 N  N     . ALA   B  1  281  ? 13.262  8.120   95.528  1.00 20.30 ? 279  ALA   B N     1 
ATOM   10937 C  CA    . ALA   B  1  281  ? 14.201  7.175   96.125  1.00 20.04 ? 279  ALA   B CA    1 
ATOM   10938 C  C     . ALA   B  1  281  ? 14.588  7.604   97.535  1.00 19.38 ? 279  ALA   B C     1 
ATOM   10939 O  O     . ALA   B  1  281  ? 14.651  6.774   98.452  1.00 21.84 ? 279  ALA   B O     1 
ATOM   10940 C  CB    . ALA   B  1  281  ? 15.446  7.031   95.248  1.00 23.19 ? 279  ALA   B CB    1 
ATOM   10941 N  N     . ARG   B  1  282  ? 14.848  8.896   97.729  1.00 17.70 ? 280  ARG   B N     1 
ATOM   10942 C  CA    . ARG   B  1  282  ? 15.190  9.376   99.061  1.00 17.95 ? 280  ARG   B CA    1 
ATOM   10943 C  C     . ARG   B  1  282  ? 13.998  9.284   99.992  1.00 18.31 ? 280  ARG   B C     1 
ATOM   10944 O  O     . ARG   B  1  282  ? 14.159  9.015   101.185 1.00 19.10 ? 280  ARG   B O     1 
ATOM   10945 C  CB    . ARG   B  1  282  ? 15.688  10.816  98.988  1.00 20.21 ? 280  ARG   B CB    1 
ATOM   10946 C  CG    . ARG   B  1  282  ? 17.051  10.952  98.318  1.00 21.56 ? 280  ARG   B CG    1 
ATOM   10947 C  CD    . ARG   B  1  282  ? 17.597  12.345  98.551  1.00 21.61 ? 280  ARG   B CD    1 
ATOM   10948 N  NE    . ARG   B  1  282  ? 17.919  12.533  99.962  1.00 20.82 ? 280  ARG   B NE    1 
ATOM   10949 C  CZ    . ARG   B  1  282  ? 18.090  13.710  100.546 1.00 20.42 ? 280  ARG   B CZ    1 
ATOM   10950 N  NH1   . ARG   B  1  282  ? 17.972  14.843  99.870  1.00 21.14 ? 280  ARG   B NH1   1 
ATOM   10951 N  NH2   . ARG   B  1  282  ? 18.381  13.753  101.841 1.00 21.53 ? 280  ARG   B NH2   1 
ATOM   10952 N  N     . VAL   B  1  283  ? 12.797  9.517   99.465  1.00 17.79 ? 281  VAL   B N     1 
ATOM   10953 C  CA    . VAL   B  1  283  ? 11.595  9.393   100.283 1.00 18.79 ? 281  VAL   B CA    1 
ATOM   10954 C  C     . VAL   B  1  283  ? 11.462  7.972   100.808 1.00 19.13 ? 281  VAL   B C     1 
ATOM   10955 O  O     . VAL   B  1  283  ? 11.294  7.746   102.015 1.00 19.18 ? 281  VAL   B O     1 
ATOM   10956 C  CB    . VAL   B  1  283  ? 10.364  9.840   99.476  1.00 18.36 ? 281  VAL   B CB    1 
ATOM   10957 C  CG1   . VAL   B  1  283  ? 9.083   9.441   100.181 1.00 20.53 ? 281  VAL   B CG1   1 
ATOM   10958 C  CG2   . VAL   B  1  283  ? 10.414  11.344  99.264  1.00 18.73 ? 281  VAL   B CG2   1 
ATOM   10959 N  N     . MET   B  1  284  ? 11.584  6.991   99.915  1.00 18.37 ? 282  MET   B N     1 
ATOM   10960 C  CA    . MET   B  1  284  ? 11.452  5.601   100.325 1.00 17.92 ? 282  MET   B CA    1 
ATOM   10961 C  C     . MET   B  1  284  ? 12.613  5.175   101.210 1.00 21.17 ? 282  MET   B C     1 
ATOM   10962 O  O     . MET   B  1  284  ? 12.430  4.370   102.128 1.00 22.91 ? 282  MET   B O     1 
ATOM   10963 C  CB    . MET   B  1  284  ? 11.337  4.690   99.107  1.00 20.30 ? 282  MET   B CB    1 
ATOM   10964 C  CG    . MET   B  1  284  ? 10.135  4.991   98.239  1.00 18.69 ? 282  MET   B CG    1 
ATOM   10965 S  SD    . MET   B  1  284  ? 8.562   4.953   99.117  1.00 23.80 ? 282  MET   B SD    1 
ATOM   10966 C  CE    . MET   B  1  284  ? 8.411   3.193   99.413  1.00 24.71 ? 282  MET   B CE    1 
ATOM   10967 N  N     . GLY   B  1  285  ? 13.810  5.700   100.950 1.00 20.25 ? 283  GLY   B N     1 
ATOM   10968 C  CA    . GLY   B  1  285  ? 14.977  5.278   101.705 1.00 21.89 ? 283  GLY   B CA    1 
ATOM   10969 C  C     . GLY   B  1  285  ? 15.125  5.944   103.053 1.00 21.64 ? 283  GLY   B C     1 
ATOM   10970 O  O     . GLY   B  1  285  ? 15.671  5.342   103.984 1.00 24.77 ? 283  GLY   B O     1 
ATOM   10971 N  N     . GLU   B  1  286  ? 14.660  7.183   103.183 1.00 19.97 ? 284  GLU   B N     1 
ATOM   10972 C  CA    . GLU   B  1  286  ? 14.920  7.998   104.362 1.00 19.94 ? 284  GLU   B CA    1 
ATOM   10973 C  C     . GLU   B  1  286  ? 13.663  8.424   105.094 1.00 21.61 ? 284  GLU   B C     1 
ATOM   10974 O  O     . GLU   B  1  286  ? 13.650  8.445   106.330 1.00 24.30 ? 284  GLU   B O     1 
ATOM   10975 C  CB    . GLU   B  1  286  ? 15.707  9.257   103.967 1.00 20.41 ? 284  GLU   B CB    1 
ATOM   10976 C  CG    . GLU   B  1  286  ? 16.969  8.960   103.158 1.00 21.90 ? 284  GLU   B CG    1 
ATOM   10977 C  CD    . GLU   B  1  286  ? 17.593  10.198  102.536 1.00 25.47 ? 284  GLU   B CD    1 
ATOM   10978 O  OE1   . GLU   B  1  286  ? 17.414  11.316  103.067 1.00 25.04 ? 284  GLU   B OE1   1 
ATOM   10979 O  OE2   . GLU   B  1  286  ? 18.270  10.044  101.501 1.00 25.13 ? 284  GLU   B OE2   1 
ATOM   10980 N  N     . LEU   B  1  287  ? 12.610  8.788   104.367 1.00 19.93 ? 285  LEU   B N     1 
ATOM   10981 C  CA    . LEU   B  1  287  ? 11.388  9.228   105.025 1.00 20.65 ? 285  LEU   B CA    1 
ATOM   10982 C  C     . LEU   B  1  287  ? 10.613  8.031   105.550 1.00 22.86 ? 285  LEU   B C     1 
ATOM   10983 O  O     . LEU   B  1  287  ? 10.192  8.017   106.710 1.00 19.63 ? 285  LEU   B O     1 
ATOM   10984 C  CB    . LEU   B  1  287  ? 10.540  10.053  104.052 1.00 19.94 ? 285  LEU   B CB    1 
ATOM   10985 C  CG    . LEU   B  1  287  ? 9.492   11.017  104.624 1.00 21.71 ? 285  LEU   B CG    1 
ATOM   10986 C  CD1   . LEU   B  1  287  ? 8.926   11.831  103.491 1.00 19.90 ? 285  LEU   B CD1   1 
ATOM   10987 C  CD2   . LEU   B  1  287  ? 8.360   10.318  105.337 1.00 22.82 ? 285  LEU   B CD2   1 
ATOM   10988 N  N     . LEU   B  1  288  ? 10.440  7.013   104.710 1.00 21.32 ? 286  LEU   B N     1 
ATOM   10989 C  CA    . LEU   B  1  288  ? 9.673   5.829   105.089 1.00 20.25 ? 286  LEU   B CA    1 
ATOM   10990 C  C     . LEU   B  1  288  ? 10.136  5.193   106.393 1.00 21.61 ? 286  LEU   B C     1 
ATOM   10991 O  O     . LEU   B  1  288  ? 9.283   4.926   107.252 1.00 20.87 ? 286  LEU   B O     1 
ATOM   10992 C  CB    . LEU   B  1  288  ? 9.637   4.841   103.918 1.00 23.91 ? 286  LEU   B CB    1 
ATOM   10993 C  CG    . LEU   B  1  288  ? 9.035   3.485   104.263 1.00 25.85 ? 286  LEU   B CG    1 
ATOM   10994 C  CD1   . LEU   B  1  288  ? 7.571   3.634   104.674 1.00 25.52 ? 286  LEU   B CD1   1 
ATOM   10995 C  CD2   . LEU   B  1  288  ? 9.176   2.546   103.079 1.00 29.14 ? 286  LEU   B CD2   1 
ATOM   10996 N  N     . PRO   B  1  289  ? 11.430  4.934   106.617 1.00 20.97 ? 287  PRO   B N     1 
ATOM   10997 C  CA    . PRO   B  1  289  ? 11.834  4.359   107.910 1.00 22.37 ? 287  PRO   B CA    1 
ATOM   10998 C  C     . PRO   B  1  289  ? 11.411  5.194   109.099 1.00 20.78 ? 287  PRO   B C     1 
ATOM   10999 O  O     . PRO   B  1  289  ? 11.113  4.634   110.160 1.00 22.84 ? 287  PRO   B O     1 
ATOM   11000 C  CB    . PRO   B  1  289  ? 13.361  4.269   107.792 1.00 25.33 ? 287  PRO   B CB    1 
ATOM   11001 C  CG    . PRO   B  1  289  ? 13.591  4.110   106.323 1.00 26.19 ? 287  PRO   B CG    1 
ATOM   11002 C  CD    . PRO   B  1  289  ? 12.568  5.004   105.680 1.00 23.62 ? 287  PRO   B CD    1 
ATOM   11003 N  N     . ARG   B  1  290  ? 11.368  6.519   108.949 1.00 19.21 ? 288  ARG   B N     1 
ATOM   11004 C  CA    A ARG   B  1  290  ? 10.909  7.369   110.041 0.51 21.06 ? 288  ARG   B CA    1 
ATOM   11005 C  CA    B ARG   B  1  290  ? 10.909  7.374   110.037 0.49 21.06 ? 288  ARG   B CA    1 
ATOM   11006 C  C     . ARG   B  1  290  ? 9.425   7.171   110.308 1.00 18.67 ? 288  ARG   B C     1 
ATOM   11007 O  O     . ARG   B  1  290  ? 9.009   7.071   111.467 1.00 20.76 ? 288  ARG   B O     1 
ATOM   11008 C  CB    A ARG   B  1  290  ? 11.227  8.831   109.741 0.51 22.10 ? 288  ARG   B CB    1 
ATOM   11009 C  CB    B ARG   B  1  290  ? 11.212  8.836   109.709 0.49 22.09 ? 288  ARG   B CB    1 
ATOM   11010 C  CG    A ARG   B  1  290  ? 12.719  9.115   109.763 0.51 23.69 ? 288  ARG   B CG    1 
ATOM   11011 C  CG    B ARG   B  1  290  ? 12.707  9.125   109.609 0.49 23.65 ? 288  ARG   B CG    1 
ATOM   11012 C  CD    A ARG   B  1  290  ? 13.071  10.337  108.948 0.51 23.88 ? 288  ARG   B CD    1 
ATOM   11013 C  CD    B ARG   B  1  290  ? 12.973  10.544  109.145 0.49 24.11 ? 288  ARG   B CD    1 
ATOM   11014 N  NE    A ARG   B  1  290  ? 14.510  10.434  108.736 0.51 25.27 ? 288  ARG   B NE    1 
ATOM   11015 N  NE    B ARG   B  1  290  ? 14.036  11.178  109.918 0.49 22.49 ? 288  ARG   B NE    1 
ATOM   11016 C  CZ    A ARG   B  1  290  ? 15.079  11.256  107.867 0.51 24.49 ? 288  ARG   B CZ    1 
ATOM   11017 C  CZ    B ARG   B  1  290  ? 14.615  12.326  109.591 0.49 25.04 ? 288  ARG   B CZ    1 
ATOM   11018 N  NH1   A ARG   B  1  290  ? 14.359  12.083  107.125 0.51 22.03 ? 288  ARG   B NH1   1 
ATOM   11019 N  NH1   B ARG   B  1  290  ? 14.286  12.977  108.486 0.49 24.61 ? 288  ARG   B NH1   1 
ATOM   11020 N  NH2   A ARG   B  1  290  ? 16.402  11.243  107.733 0.51 24.71 ? 288  ARG   B NH2   1 
ATOM   11021 N  NH2   B ARG   B  1  290  ? 15.545  12.834  110.394 0.49 24.06 ? 288  ARG   B NH2   1 
ATOM   11022 N  N     . VAL   B  1  291  ? 8.611   7.091   109.253 1.00 20.62 ? 289  VAL   B N     1 
ATOM   11023 C  CA    . VAL   B  1  291  ? 7.194   6.834   109.487 1.00 19.63 ? 289  VAL   B CA    1 
ATOM   11024 C  C     . VAL   B  1  291  ? 7.009   5.469   110.114 1.00 19.31 ? 289  VAL   B C     1 
ATOM   11025 O  O     . VAL   B  1  291  ? 6.185   5.293   111.020 1.00 20.86 ? 289  VAL   B O     1 
ATOM   11026 C  CB    . VAL   B  1  291  ? 6.378   6.967   108.192 1.00 22.18 ? 289  VAL   B CB    1 
ATOM   11027 C  CG1   . VAL   B  1  291  ? 4.895   6.806   108.510 1.00 22.61 ? 289  VAL   B CG1   1 
ATOM   11028 C  CG2   . VAL   B  1  291  ? 6.639   8.296   107.551 1.00 24.45 ? 289  VAL   B CG2   1 
ATOM   11029 N  N     . LYS   B  1  292  ? 7.755   4.474   109.631 1.00 20.03 ? 290  LYS   B N     1 
ATOM   11030 C  CA    . LYS   B  1  292  ? 7.614   3.137   110.188 1.00 20.96 ? 290  LYS   B CA    1 
ATOM   11031 C  C     . LYS   B  1  292  ? 7.922   3.140   111.676 1.00 22.79 ? 290  LYS   B C     1 
ATOM   11032 O  O     . LYS   B  1  292  ? 7.213   2.502   112.463 1.00 23.42 ? 290  LYS   B O     1 
ATOM   11033 C  CB    . LYS   B  1  292  ? 8.510   2.147   109.446 1.00 23.68 ? 290  LYS   B CB    1 
ATOM   11034 C  CG    . LYS   B  1  292  ? 8.326   0.702   109.899 1.00 28.02 ? 290  LYS   B CG    1 
ATOM   11035 C  CD    . LYS   B  1  292  ? 9.295   0.315   110.997 1.00 31.30 ? 290  LYS   B CD    1 
ATOM   11036 C  CE    . LYS   B  1  292  ? 9.033   -1.105  111.497 1.00 30.31 ? 290  LYS   B CE    1 
ATOM   11037 N  NZ    . LYS   B  1  292  ? 9.331   -2.113  110.446 1.00 30.68 ? 290  LYS   B NZ    1 
ATOM   11038 N  N     . ALA   B  1  293  ? 8.970   3.864   112.081 1.00 22.15 ? 291  ALA   B N     1 
ATOM   11039 C  CA    . ALA   B  1  293  ? 9.328   3.911   113.492 1.00 22.70 ? 291  ALA   B CA    1 
ATOM   11040 C  C     . ALA   B  1  293  ? 8.218   4.546   114.313 1.00 23.34 ? 291  ALA   B C     1 
ATOM   11041 O  O     . ALA   B  1  293  ? 7.886   4.065   115.402 1.00 22.12 ? 291  ALA   B O     1 
ATOM   11042 C  CB    . ALA   B  1  293  ? 10.628  4.689   113.669 1.00 22.07 ? 291  ALA   B CB    1 
ATOM   11043 N  N     . LEU   B  1  294  ? 7.639   5.637   113.809 1.00 21.19 ? 292  LEU   B N     1 
ATOM   11044 C  CA    . LEU   B  1  294  ? 6.529   6.265   114.513 1.00 22.99 ? 292  LEU   B CA    1 
ATOM   11045 C  C     . LEU   B  1  294  ? 5.321   5.347   114.548 1.00 22.66 ? 292  LEU   B C     1 
ATOM   11046 O  O     . LEU   B  1  294  ? 4.643   5.238   115.575 1.00 21.57 ? 292  LEU   B O     1 
ATOM   11047 C  CB    . LEU   B  1  294  ? 6.173   7.592   113.848 1.00 22.07 ? 292  LEU   B CB    1 
ATOM   11048 C  CG    . LEU   B  1  294  ? 7.270   8.656   113.861 1.00 20.79 ? 292  LEU   B CG    1 
ATOM   11049 C  CD1   . LEU   B  1  294  ? 6.827   9.830   113.023 1.00 20.67 ? 292  LEU   B CD1   1 
ATOM   11050 C  CD2   . LEU   B  1  294  ? 7.596   9.091   115.288 1.00 23.46 ? 292  LEU   B CD2   1 
ATOM   11051 N  N     . ALA   B  1  295  ? 5.032   4.680   113.430 1.00 21.11 ? 293  ALA   B N     1 
ATOM   11052 C  CA    . ALA   B  1  295  ? 3.903   3.757   113.398 1.00 23.66 ? 293  ALA   B CA    1 
ATOM   11053 C  C     . ALA   B  1  295  ? 4.118   2.597   114.361 1.00 24.24 ? 293  ALA   B C     1 
ATOM   11054 O  O     . ALA   B  1  295  ? 3.181   2.160   115.038 1.00 23.00 ? 293  ALA   B O     1 
ATOM   11055 C  CB    . ALA   B  1  295  ? 3.692   3.253   111.970 1.00 23.47 ? 293  ALA   B CB    1 
ATOM   11056 N  N     . LEU   B  1  296  ? 5.353   2.106   114.463 1.00 23.07 ? 294  LEU   B N     1 
ATOM   11057 C  CA    . LEU   B  1  296  ? 5.638   1.040   115.416 1.00 23.94 ? 294  LEU   B CA    1 
ATOM   11058 C  C     . LEU   B  1  296  ? 5.370   1.494   116.845 1.00 23.96 ? 294  LEU   B C     1 
ATOM   11059 O  O     . LEU   B  1  296  ? 4.809   0.739   117.651 1.00 25.00 ? 294  LEU   B O     1 
ATOM   11060 C  CB    . LEU   B  1  296  ? 7.082   0.573   115.251 1.00 25.87 ? 294  LEU   B CB    1 
ATOM   11061 C  CG    . LEU   B  1  296  ? 7.513   -0.615  116.113 1.00 30.28 ? 294  LEU   B CG    1 
ATOM   11062 C  CD1   . LEU   B  1  296  ? 6.522   -1.762  115.973 1.00 32.63 ? 294  LEU   B CD1   1 
ATOM   11063 C  CD2   . LEU   B  1  296  ? 8.917   -1.067  115.730 1.00 34.64 ? 294  LEU   B CD2   1 
ATOM   11064 N  N     . LEU   B  1  297  ? 5.752   2.730   117.177 1.00 23.60 ? 295  LEU   B N     1 
ATOM   11065 C  CA    . LEU   B  1  297  ? 5.438   3.250   118.505 1.00 24.62 ? 295  LEU   B CA    1 
ATOM   11066 C  C     . LEU   B  1  297  ? 3.933   3.361   118.706 1.00 24.75 ? 295  LEU   B C     1 
ATOM   11067 O  O     . LEU   B  1  297  ? 3.407   2.984   119.760 1.00 24.48 ? 295  LEU   B O     1 
ATOM   11068 C  CB    . LEU   B  1  297  ? 6.101   4.613   118.711 1.00 24.39 ? 295  LEU   B CB    1 
ATOM   11069 C  CG    . LEU   B  1  297  ? 7.616   4.664   118.889 1.00 29.43 ? 295  LEU   B CG    1 
ATOM   11070 C  CD1   . LEU   B  1  297  ? 8.098   6.118   118.851 1.00 27.70 ? 295  LEU   B CD1   1 
ATOM   11071 C  CD2   . LEU   B  1  297  ? 8.021   3.995   120.190 1.00 32.01 ? 295  LEU   B CD2   1 
ATOM   11072 N  N     . ALA   B  1  298  ? 3.218   3.874   117.706 1.00 23.79 ? 296  ALA   B N     1 
ATOM   11073 C  CA    . ALA   B  1  298  ? 1.772   3.985   117.828 1.00 25.08 ? 296  ALA   B CA    1 
ATOM   11074 C  C     . ALA   B  1  298  ? 1.143   2.613   117.988 1.00 25.98 ? 296  ALA   B C     1 
ATOM   11075 O  O     . ALA   B  1  298  ? 0.210   2.434   118.782 1.00 26.37 ? 296  ALA   B O     1 
ATOM   11076 C  CB    . ALA   B  1  298  ? 1.201   4.701   116.604 1.00 23.89 ? 296  ALA   B CB    1 
ATOM   11077 N  N     . LYS   B  1  299  ? 1.652   1.626   117.249 1.00 25.04 ? 297  LYS   B N     1 
ATOM   11078 C  CA    . LYS   B  1  299  ? 1.145   0.266   117.389 1.00 27.78 ? 297  LYS   B CA    1 
ATOM   11079 C  C     . LYS   B  1  299  ? 1.365   -0.261  118.798 1.00 29.97 ? 297  LYS   B C     1 
ATOM   11080 O  O     . LYS   B  1  299  ? 0.472   -0.893  119.380 1.00 30.32 ? 297  LYS   B O     1 
ATOM   11081 C  CB    . LYS   B  1  299  ? 1.826   -0.653  116.377 1.00 29.00 ? 297  LYS   B CB    1 
ATOM   11082 C  CG    . LYS   B  1  299  ? 1.459   -2.117  116.563 1.00 32.27 ? 297  LYS   B CG    1 
ATOM   11083 C  CD    . LYS   B  1  299  ? 2.634   -3.025  116.272 1.00 36.58 ? 297  LYS   B CD    1 
ATOM   11084 C  CE    . LYS   B  1  299  ? 2.222   -4.489  116.319 1.00 37.02 ? 297  LYS   B CE    1 
ATOM   11085 N  NZ    . LYS   B  1  299  ? 1.900   -4.961  117.690 1.00 44.58 ? 297  LYS   B NZ    1 
ATOM   11086 N  N     . ASN   B  1  300  ? 2.547   -0.015  119.367 1.00 26.74 ? 298  ASN   B N     1 
ATOM   11087 C  CA    . ASN   B  1  300  ? 2.844   -0.544  120.695 1.00 26.13 ? 298  ASN   B CA    1 
ATOM   11088 C  C     . ASN   B  1  300  ? 1.918   0.038   121.753 1.00 28.88 ? 298  ASN   B C     1 
ATOM   11089 O  O     . ASN   B  1  300  ? 1.582   -0.646  122.724 1.00 31.18 ? 298  ASN   B O     1 
ATOM   11090 C  CB    . ASN   B  1  300  ? 4.314   -0.305  121.043 1.00 27.69 ? 298  ASN   B CB    1 
ATOM   11091 C  CG    . ASN   B  1  300  ? 5.250   -1.172  120.212 1.00 31.62 ? 298  ASN   B CG    1 
ATOM   11092 O  OD1   . ASN   B  1  300  ? 4.850   -2.216  119.700 1.00 41.50 ? 298  ASN   B OD1   1 
ATOM   11093 N  ND2   . ASN   B  1  300  ? 6.502   -0.747  120.084 1.00 39.35 ? 298  ASN   B ND2   1 
ATOM   11094 N  N     . TYR   B  1  301  ? 1.489   1.284   121.581 1.00 25.54 ? 299  TYR   B N     1 
ATOM   11095 C  CA    . TYR   B  1  301  ? 0.512   1.882   122.480 1.00 25.63 ? 299  TYR   B CA    1 
ATOM   11096 C  C     . TYR   B  1  301  ? -0.917  1.657   122.024 1.00 24.85 ? 299  TYR   B C     1 
ATOM   11097 O  O     . TYR   B  1  301  ? -1.845  2.063   122.731 1.00 26.82 ? 299  TYR   B O     1 
ATOM   11098 C  CB    . TYR   B  1  301  ? 0.743   3.390   122.592 1.00 23.22 ? 299  TYR   B CB    1 
ATOM   11099 C  CG    . TYR   B  1  301  ? 1.988   3.779   123.347 1.00 26.02 ? 299  TYR   B CG    1 
ATOM   11100 C  CD1   . TYR   B  1  301  ? 2.056   3.634   124.727 1.00 25.39 ? 299  TYR   B CD1   1 
ATOM   11101 C  CD2   . TYR   B  1  301  ? 3.086   4.303   122.681 1.00 24.78 ? 299  TYR   B CD2   1 
ATOM   11102 C  CE1   . TYR   B  1  301  ? 3.191   3.993   125.423 1.00 25.34 ? 299  TYR   B CE1   1 
ATOM   11103 C  CE2   . TYR   B  1  301  ? 4.222   4.676   123.367 1.00 27.61 ? 299  TYR   B CE2   1 
ATOM   11104 C  CZ    . TYR   B  1  301  ? 4.267   4.514   124.735 1.00 25.35 ? 299  TYR   B CZ    1 
ATOM   11105 O  OH    . TYR   B  1  301  ? 5.392   4.871   125.430 1.00 27.17 ? 299  TYR   B OH    1 
ATOM   11106 N  N     . ASP   B  1  302  ? -1.109  1.029   120.867 1.00 25.69 ? 300  ASP   B N     1 
ATOM   11107 C  CA    . ASP   B  1  302  ? -2.414  0.855   120.235 1.00 28.59 ? 300  ASP   B CA    1 
ATOM   11108 C  C     . ASP   B  1  302  ? -3.178  2.177   120.135 1.00 24.74 ? 300  ASP   B C     1 
ATOM   11109 O  O     . ASP   B  1  302  ? -4.302  2.322   120.622 1.00 27.08 ? 300  ASP   B O     1 
ATOM   11110 C  CB    . ASP   B  1  302  ? -3.249  -0.235  120.910 1.00 28.60 ? 300  ASP   B CB    1 
ATOM   11111 C  CG    . ASP   B  1  302  ? -4.372  -0.732  120.017 1.00 29.78 ? 300  ASP   B CG    1 
ATOM   11112 O  OD1   . ASP   B  1  302  ? -4.213  -0.673  118.773 1.00 33.45 ? 300  ASP   B OD1   1 
ATOM   11113 O  OD2   . ASP   B  1  302  ? -5.411  -1.166  120.554 1.00 35.80 ? 300  ASP   B OD2   1 
ATOM   11114 N  N     . ILE   B  1  303  ? -2.534  3.154   119.503 1.00 24.27 ? 301  ILE   B N     1 
ATOM   11115 C  CA    . ILE   B  1  303  ? -3.172  4.419   119.170 1.00 23.87 ? 301  ILE   B CA    1 
ATOM   11116 C  C     . ILE   B  1  303  ? -3.218  4.559   117.655 1.00 25.55 ? 301  ILE   B C     1 
ATOM   11117 O  O     . ILE   B  1  303  ? -2.494  3.885   116.918 1.00 24.37 ? 301  ILE   B O     1 
ATOM   11118 C  CB    . ILE   B  1  303  ? -2.474  5.636   119.813 1.00 22.00 ? 301  ILE   B CB    1 
ATOM   11119 C  CG1   . ILE   B  1  303  ? -1.101  5.879   119.178 1.00 24.29 ? 301  ILE   B CG1   1 
ATOM   11120 C  CG2   . ILE   B  1  303  ? -2.323  5.432   121.319 1.00 24.66 ? 301  ILE   B CG2   1 
ATOM   11121 C  CD1   . ILE   B  1  303  ? -0.479  7.219   119.563 1.00 25.62 ? 301  ILE   B CD1   1 
ATOM   11122 N  N     . GLY   B  1  304  ? -4.076  5.467   117.194 1.00 22.58 ? 302  GLY   B N     1 
ATOM   11123 C  CA    . GLY   B  1  304  ? -4.127  5.774   115.774 1.00 22.21 ? 302  GLY   B CA    1 
ATOM   11124 C  C     . GLY   B  1  304  ? -2.984  6.696   115.371 1.00 21.98 ? 302  GLY   B C     1 
ATOM   11125 O  O     . GLY   B  1  304  ? -2.582  7.590   116.116 1.00 22.88 ? 302  GLY   B O     1 
ATOM   11126 N  N     . LEU   B  1  305  ? -2.443  6.454   114.181 1.00 20.10 ? 303  LEU   B N     1 
ATOM   11127 C  CA    . LEU   B  1  305  ? -1.452  7.339   113.583 1.00 21.61 ? 303  LEU   B CA    1 
ATOM   11128 C  C     . LEU   B  1  305  ? -1.937  7.634   112.178 1.00 20.81 ? 303  LEU   B C     1 
ATOM   11129 O  O     . LEU   B  1  305  ? -1.983  6.731   111.339 1.00 21.62 ? 303  LEU   B O     1 
ATOM   11130 C  CB    . LEU   B  1  305  ? -0.059  6.709   113.563 1.00 23.61 ? 303  LEU   B CB    1 
ATOM   11131 C  CG    . LEU   B  1  305  ? 1.022   7.612   112.952 1.00 22.92 ? 303  LEU   B CG    1 
ATOM   11132 C  CD1   . LEU   B  1  305  ? 2.311   7.555   113.743 1.00 25.25 ? 303  LEU   B CD1   1 
ATOM   11133 C  CD2   . LEU   B  1  305  ? 1.280   7.250   111.502 1.00 26.60 ? 303  LEU   B CD2   1 
ATOM   11134 N  N     . ASN   B  1  306  ? -2.278  8.891   111.927 1.00 19.77 ? 304  ASN   B N     1 
ATOM   11135 C  CA    . ASN   B  1  306  ? -2.896  9.312   110.683 1.00 20.36 ? 304  ASN   B CA    1 
ATOM   11136 C  C     . ASN   B  1  306  ? -1.899  10.104  109.856 1.00 19.46 ? 304  ASN   B C     1 
ATOM   11137 O  O     . ASN   B  1  306  ? -1.189  10.966  110.385 1.00 19.64 ? 304  ASN   B O     1 
ATOM   11138 C  CB    . ASN   B  1  306  ? -4.088  10.217  110.965 1.00 22.94 ? 304  ASN   B CB    1 
ATOM   11139 C  CG    . ASN   B  1  306  ? -4.666  10.786  109.709 1.00 20.90 ? 304  ASN   B CG    1 
ATOM   11140 O  OD1   . ASN   B  1  306  ? -5.403  10.105  108.990 1.00 23.45 ? 304  ASN   B OD1   1 
ATOM   11141 N  ND2   . ASN   B  1  306  ? -4.336  12.038  109.418 1.00 21.75 ? 304  ASN   B ND2   1 
ATOM   11142 N  N     . ILE   B  1  307  ? -1.868  9.825   108.560 1.00 20.25 ? 305  ILE   B N     1 
ATOM   11143 C  CA    . ILE   B  1  307  ? -1.075  10.594  107.609 1.00 19.05 ? 305  ILE   B CA    1 
ATOM   11144 C  C     . ILE   B  1  307  ? -1.982  11.635  106.969 1.00 19.23 ? 305  ILE   B C     1 
ATOM   11145 O  O     . ILE   B  1  307  ? -2.891  11.296  106.197 1.00 18.62 ? 305  ILE   B O     1 
ATOM   11146 C  CB    . ILE   B  1  307  ? -0.422  9.694   106.555 1.00 20.49 ? 305  ILE   B CB    1 
ATOM   11147 C  CG1   . ILE   B  1  307  ? 0.526   8.712   107.248 1.00 22.50 ? 305  ILE   B CG1   1 
ATOM   11148 C  CG2   . ILE   B  1  307  ? 0.287   10.549  105.485 1.00 21.61 ? 305  ILE   B CG2   1 
ATOM   11149 C  CD1   . ILE   B  1  307  ? 1.159   7.722   106.299 1.00 25.70 ? 305  ILE   B CD1   1 
ATOM   11150 N  N     . ASP   B  1  308  ? -1.748  12.899  107.304 1.00 19.47 ? 306  ASP   B N     1 
ATOM   11151 C  CA    . ASP   B  1  308  ? -2.499  13.989  106.708 1.00 20.09 ? 306  ASP   B CA    1 
ATOM   11152 C  C     . ASP   B  1  308  ? -2.188  14.072  105.224 1.00 18.82 ? 306  ASP   B C     1 
ATOM   11153 O  O     . ASP   B  1  308  ? -1.095  13.730  104.771 1.00 20.21 ? 306  ASP   B O     1 
ATOM   11154 C  CB    . ASP   B  1  308  ? -2.117  15.319  107.355 1.00 19.82 ? 306  ASP   B CB    1 
ATOM   11155 C  CG    . ASP   B  1  308  ? -2.590  15.445  108.800 1.00 21.66 ? 306  ASP   B CG    1 
ATOM   11156 O  OD1   . ASP   B  1  308  ? -3.398  14.618  109.269 1.00 21.44 ? 306  ASP   B OD1   1 
ATOM   11157 O  OD2   . ASP   B  1  308  ? -2.140  16.399  109.473 1.00 21.47 ? 306  ASP   B OD2   1 
ATOM   11158 N  N     . ALA   B  1  309  ? -3.158  14.540  104.463 1.00 17.17 ? 307  ALA   B N     1 
ATOM   11159 C  CA    . ALA   B  1  309  ? -2.989  14.668  103.029 1.00 17.02 ? 307  ALA   B CA    1 
ATOM   11160 C  C     . ALA   B  1  309  ? -2.584  16.088  102.685 1.00 17.47 ? 307  ALA   B C     1 
ATOM   11161 O  O     . ALA   B  1  309  ? -3.108  17.053  103.254 1.00 18.98 ? 307  ALA   B O     1 
ATOM   11162 C  CB    . ALA   B  1  309  ? -4.294  14.330  102.323 1.00 18.09 ? 307  ALA   B CB    1 
ATOM   11163 N  N     . GLU   B  1  310  ? -1.622  16.209  101.774 1.00 17.26 ? 308  GLU   B N     1 
ATOM   11164 C  CA    . GLU   B  1  310  ? -1.051  17.512  101.466 1.00 17.33 ? 308  GLU   B CA    1 
ATOM   11165 C  C     . GLU   B  1  310  ? -1.336  17.885  100.015 1.00 16.78 ? 308  GLU   B C     1 
ATOM   11166 O  O     . GLU   B  1  310  ? -2.463  17.696  99.543  1.00 16.87 ? 308  GLU   B O     1 
ATOM   11167 C  CB    . GLU   B  1  310  ? 0.439   17.526  101.833 1.00 16.55 ? 308  GLU   B CB    1 
ATOM   11168 C  CG    . GLU   B  1  310  ? 0.625   17.177  103.310 1.00 18.25 ? 308  GLU   B CG    1 
ATOM   11169 C  CD    . GLU   B  1  310  ? 2.059   17.262  103.777 1.00 20.38 ? 308  GLU   B CD    1 
ATOM   11170 O  OE1   . GLU   B  1  310  ? 2.548   18.389  103.963 1.00 19.90 ? 308  GLU   B OE1   1 
ATOM   11171 O  OE2   . GLU   B  1  310  ? 2.679   16.201  103.987 1.00 18.89 ? 308  GLU   B OE2   1 
ATOM   11172 N  N     . GLU   B  1  311  ? -0.342  18.403  99.302  1.00 16.94 ? 309  GLU   B N     1 
ATOM   11173 C  CA    . GLU   B  1  311  ? -0.571  18.866  97.943  1.00 16.30 ? 309  GLU   B CA    1 
ATOM   11174 C  C     . GLU   B  1  311  ? -0.888  17.699  97.018  1.00 17.45 ? 309  GLU   B C     1 
ATOM   11175 O  O     . GLU   B  1  311  ? -0.514  16.551  97.270  1.00 17.14 ? 309  GLU   B O     1 
ATOM   11176 C  CB    . GLU   B  1  311  ? 0.670   19.579  97.423  1.00 16.79 ? 309  GLU   B CB    1 
ATOM   11177 C  CG    . GLU   B  1  311  ? 0.956   20.886  98.143  1.00 19.42 ? 309  GLU   B CG    1 
ATOM   11178 C  CD    . GLU   B  1  311  ? 1.884   20.726  99.334  1.00 20.58 ? 309  GLU   B CD    1 
ATOM   11179 O  OE1   . GLU   B  1  311  ? 2.044   19.592  99.849  1.00 19.19 ? 309  GLU   B OE1   1 
ATOM   11180 O  OE2   . GLU   B  1  311  ? 2.450   21.756  99.762  1.00 26.47 ? 309  GLU   B OE2   1 
ATOM   11181 N  N     . ALA   B  1  312  ? -1.587  18.012  95.920  1.00 16.39 ? 310  ALA   B N     1 
ATOM   11182 C  CA    . ALA   B  1  312  ? -2.000  16.971  94.989  1.00 17.29 ? 310  ALA   B CA    1 
ATOM   11183 C  C     . ALA   B  1  312  ? -0.821  16.188  94.436  1.00 15.35 ? 310  ALA   B C     1 
ATOM   11184 O  O     . ALA   B  1  312  ? -0.950  14.982  94.196  1.00 16.41 ? 310  ALA   B O     1 
ATOM   11185 C  CB    . ALA   B  1  312  ? -2.799  17.576  93.831  1.00 16.12 ? 310  ALA   B CB    1 
ATOM   11186 N  N     . ASP   B  1  313  ? 0.339   16.836  94.251  1.00 16.39 ? 311  ASP   B N     1 
ATOM   11187 C  CA    . ASP   B  1  313  ? 1.481   16.126  93.682  1.00 16.47 ? 311  ASP   B CA    1 
ATOM   11188 C  C     . ASP   B  1  313  ? 2.185   15.225  94.681  1.00 19.29 ? 311  ASP   B C     1 
ATOM   11189 O  O     . ASP   B  1  313  ? 3.197   14.612  94.334  1.00 18.09 ? 311  ASP   B O     1 
ATOM   11190 C  CB    . ASP   B  1  313  ? 2.446   17.064  92.942  1.00 17.35 ? 311  ASP   B CB    1 
ATOM   11191 C  CG    . ASP   B  1  313  ? 3.155   18.048  93.846  1.00 19.65 ? 311  ASP   B CG    1 
ATOM   11192 O  OD1   . ASP   B  1  313  ? 3.000   17.991  95.082  1.00 20.30 ? 311  ASP   B OD1   1 
ATOM   11193 O  OD2   . ASP   B  1  313  ? 3.914   18.884  93.297  1.00 22.70 ? 311  ASP   B OD2   1 
ATOM   11194 N  N     . ARG   B  1  314  ? 1.674   15.128  95.901  1.00 16.45 ? 312  ARG   B N     1 
ATOM   11195 C  CA    . ARG   B  1  314  ? 2.198   14.207  96.893  1.00 17.65 ? 312  ARG   B CA    1 
ATOM   11196 C  C     . ARG   B  1  314  ? 1.264   13.046  97.158  1.00 17.38 ? 312  ARG   B C     1 
ATOM   11197 O  O     . ARG   B  1  314  ? 1.649   12.108  97.863  1.00 19.04 ? 312  ARG   B O     1 
ATOM   11198 C  CB    . ARG   B  1  314  ? 2.470   14.950  98.203  1.00 16.64 ? 312  ARG   B CB    1 
ATOM   11199 C  CG    . ARG   B  1  314  ? 3.747   15.750  98.105  1.00 17.38 ? 312  ARG   B CG    1 
ATOM   11200 C  CD    . ARG   B  1  314  ? 3.820   16.838  99.145  1.00 16.84 ? 312  ARG   B CD    1 
ATOM   11201 N  NE    . ARG   B  1  314  ? 5.192   17.305  99.280  1.00 16.65 ? 312  ARG   B NE    1 
ATOM   11202 C  CZ    . ARG   B  1  314  ? 5.556   18.303  100.069 1.00 16.17 ? 312  ARG   B CZ    1 
ATOM   11203 N  NH1   . ARG   B  1  314  ? 4.665   19.045  100.701 1.00 18.08 ? 312  ARG   B NH1   1 
ATOM   11204 N  NH2   . ARG   B  1  314  ? 6.849   18.550  100.245 1.00 18.21 ? 312  ARG   B NH2   1 
ATOM   11205 N  N     . LEU   B  1  315  ? 0.054   13.081  96.605  1.00 17.11 ? 313  LEU   B N     1 
ATOM   11206 C  CA    . LEU   B  1  315  ? -0.927  12.052  96.904  1.00 18.21 ? 313  LEU   B CA    1 
ATOM   11207 C  C     . LEU   B  1  315  ? -0.393  10.672  96.549  1.00 18.53 ? 313  LEU   B C     1 
ATOM   11208 O  O     . LEU   B  1  315  ? -0.337  9.775   97.399  1.00 19.11 ? 313  LEU   B O     1 
ATOM   11209 C  CB    . LEU   B  1  315  ? -2.211  12.343  96.132  1.00 16.65 ? 313  LEU   B CB    1 
ATOM   11210 C  CG    . LEU   B  1  315  ? -3.517  11.722  96.632  1.00 18.62 ? 313  LEU   B CG    1 
ATOM   11211 C  CD1   . LEU   B  1  315  ? -4.659  12.176  95.746  1.00 21.08 ? 313  LEU   B CD1   1 
ATOM   11212 C  CD2   . LEU   B  1  315  ? -3.478  10.203  96.666  1.00 21.96 ? 313  LEU   B CD2   1 
ATOM   11213 N  N     . GLU   B  1  316  ? -0.032  10.465  95.281  1.00 17.78 ? 314  GLU   B N     1 
ATOM   11214 C  CA    . GLU   B  1  316  ? 0.305   9.109   94.876  1.00 18.53 ? 314  GLU   B CA    1 
ATOM   11215 C  C     . GLU   B  1  316  ? 1.606   8.645   95.511  1.00 19.35 ? 314  GLU   B C     1 
ATOM   11216 O  O     . GLU   B  1  316  ? 1.727   7.473   95.879  1.00 20.33 ? 314  GLU   B O     1 
ATOM   11217 C  CB    . GLU   B  1  316  ? 0.302   8.989   93.355  1.00 20.48 ? 314  GLU   B CB    1 
ATOM   11218 C  CG    . GLU   B  1  316  ? -1.105  9.184   92.800  1.00 18.23 ? 314  GLU   B CG    1 
ATOM   11219 C  CD    . GLU   B  1  316  ? -1.179  9.079   91.286  1.00 22.83 ? 314  GLU   B CD    1 
ATOM   11220 O  OE1   . GLU   B  1  316  ? -0.548  8.165   90.719  1.00 22.42 ? 314  GLU   B OE1   1 
ATOM   11221 O  OE2   . GLU   B  1  316  ? -1.890  9.899   90.665  1.00 23.02 ? 314  GLU   B OE2   1 
ATOM   11222 N  N     . LEU   B  1  317  ? 2.568   9.550   95.686  1.00 19.79 ? 315  LEU   B N     1 
ATOM   11223 C  CA    . LEU   B  1  317  ? 3.771   9.194   96.421  1.00 20.20 ? 315  LEU   B CA    1 
ATOM   11224 C  C     . LEU   B  1  317  ? 3.428   8.667   97.805  1.00 20.70 ? 315  LEU   B C     1 
ATOM   11225 O  O     . LEU   B  1  317  ? 3.973   7.646   98.239  1.00 21.37 ? 315  LEU   B O     1 
ATOM   11226 C  CB    . LEU   B  1  317  ? 4.678   10.411  96.517  1.00 19.02 ? 315  LEU   B CB    1 
ATOM   11227 C  CG    . LEU   B  1  317  ? 5.972   10.166  97.277  1.00 20.86 ? 315  LEU   B CG    1 
ATOM   11228 C  CD1   . LEU   B  1  317  ? 6.704   8.968   96.681  1.00 24.99 ? 315  LEU   B CD1   1 
ATOM   11229 C  CD2   . LEU   B  1  317  ? 6.810   11.413  97.187  1.00 22.26 ? 315  LEU   B CD2   1 
ATOM   11230 N  N     . SER   B  1  318  ? 2.492   9.323   98.499  1.00 18.27 ? 316  SER   B N     1 
ATOM   11231 C  CA    . SER   B  1  318  ? 2.154   8.878   99.846  1.00 19.21 ? 316  SER   B CA    1 
ATOM   11232 C  C     . SER   B  1  318  ? 1.578   7.467   99.840  1.00 18.94 ? 316  SER   B C     1 
ATOM   11233 O  O     . SER   B  1  318  ? 1.738   6.729   100.818 1.00 20.65 ? 316  SER   B O     1 
ATOM   11234 C  CB    . SER   B  1  318  ? 1.201   9.869   100.522 1.00 19.25 ? 316  SER   B CB    1 
ATOM   11235 O  OG    . SER   B  1  318  ? -0.107  9.763   99.992  1.00 18.75 ? 316  SER   B OG    1 
ATOM   11236 N  N     . LEU   B  1  319  ? 0.922   7.065   98.748  1.00 18.79 ? 317  LEU   B N     1 
ATOM   11237 C  CA    . LEU   B  1  319  ? 0.368   5.717   98.683  1.00 20.71 ? 317  LEU   B CA    1 
ATOM   11238 C  C     . LEU   B  1  319  ? 1.463   4.660   98.679  1.00 20.99 ? 317  LEU   B C     1 
ATOM   11239 O  O     . LEU   B  1  319  ? 1.258   3.551   99.190  1.00 20.75 ? 317  LEU   B O     1 
ATOM   11240 C  CB    . LEU   B  1  319  ? -0.504  5.575   97.437  1.00 21.09 ? 317  LEU   B CB    1 
ATOM   11241 C  CG    . LEU   B  1  319  ? -1.728  6.484   97.343  1.00 21.26 ? 317  LEU   B CG    1 
ATOM   11242 C  CD1   . LEU   B  1  319  ? -2.363  6.347   95.960  1.00 21.43 ? 317  LEU   B CD1   1 
ATOM   11243 C  CD2   . LEU   B  1  319  ? -2.717  6.165   98.447  1.00 22.62 ? 317  LEU   B CD2   1 
ATOM   11244 N  N     . ASP   B  1  320  ? 2.625   4.974   98.109  1.00 20.98 ? 318  ASP   B N     1 
ATOM   11245 C  CA    . ASP   B  1  320  ? 3.726   4.024   98.157  1.00 22.58 ? 318  ASP   B CA    1 
ATOM   11246 C  C     . ASP   B  1  320  ? 4.199   3.779   99.580  1.00 20.00 ? 318  ASP   B C     1 
ATOM   11247 O  O     . ASP   B  1  320  ? 4.603   2.662   99.916  1.00 24.02 ? 318  ASP   B O     1 
ATOM   11248 C  CB    . ASP   B  1  320  ? 4.858   4.504   97.269  1.00 22.43 ? 318  ASP   B CB    1 
ATOM   11249 C  CG    . ASP   B  1  320  ? 4.540   4.307   95.813  1.00 20.94 ? 318  ASP   B CG    1 
ATOM   11250 O  OD1   . ASP   B  1  320  ? 4.202   3.162   95.446  1.00 23.41 ? 318  ASP   B OD1   1 
ATOM   11251 O  OD2   . ASP   B  1  320  ? 4.583   5.285   95.050  1.00 24.42 ? 318  ASP   B OD2   1 
ATOM   11252 N  N     . LEU   B  1  321  ? 4.133   4.794   100.435 1.00 18.98 ? 319  LEU   B N     1 
ATOM   11253 C  CA    . LEU   B  1  321  ? 4.471   4.567   101.835 1.00 21.71 ? 319  LEU   B CA    1 
ATOM   11254 C  C     . LEU   B  1  321  ? 3.364   3.802   102.545 1.00 20.65 ? 319  LEU   B C     1 
ATOM   11255 O  O     . LEU   B  1  321  ? 3.637   2.879   103.322 1.00 22.06 ? 319  LEU   B O     1 
ATOM   11256 C  CB    . LEU   B  1  321  ? 4.749   5.894   102.540 1.00 22.69 ? 319  LEU   B CB    1 
ATOM   11257 C  CG    . LEU   B  1  321  ? 6.091   6.546   102.214 1.00 22.20 ? 319  LEU   B CG    1 
ATOM   11258 C  CD1   . LEU   B  1  321  ? 6.016   7.386   100.952 1.00 22.85 ? 319  LEU   B CD1   1 
ATOM   11259 C  CD2   . LEU   B  1  321  ? 6.540   7.383   103.395 1.00 23.37 ? 319  LEU   B CD2   1 
ATOM   11260 N  N     . LEU   B  1  322  ? 2.106   4.158   102.277 1.00 21.10 ? 320  LEU   B N     1 
ATOM   11261 C  CA    . LEU   B  1  322  ? 0.995   3.438   102.884 1.00 21.39 ? 320  LEU   B CA    1 
ATOM   11262 C  C     . LEU   B  1  322  ? 1.069   1.960   102.548 1.00 21.23 ? 320  LEU   B C     1 
ATOM   11263 O  O     . LEU   B  1  322  ? 0.821   1.108   103.410 1.00 22.74 ? 320  LEU   B O     1 
ATOM   11264 C  CB    . LEU   B  1  322  ? -0.325  4.017   102.383 1.00 23.52 ? 320  LEU   B CB    1 
ATOM   11265 C  CG    . LEU   B  1  322  ? -1.563  3.379   103.014 1.00 23.80 ? 320  LEU   B CG    1 
ATOM   11266 C  CD1   . LEU   B  1  322  ? -1.611  3.680   104.501 1.00 23.19 ? 320  LEU   B CD1   1 
ATOM   11267 C  CD2   . LEU   B  1  322  ? -2.813  3.880   102.325 1.00 23.84 ? 320  LEU   B CD2   1 
ATOM   11268 N  N     . GLU   B  1  323  ? 1.427   1.643   101.299 1.00 21.59 ? 321  GLU   B N     1 
ATOM   11269 C  CA    . GLU   B  1  323  ? 1.531   0.254   100.862 1.00 24.19 ? 321  GLU   B CA    1 
ATOM   11270 C  C     . GLU   B  1  323  ? 2.541   -0.508  101.704 1.00 22.38 ? 321  GLU   B C     1 
ATOM   11271 O  O     . GLU   B  1  323  ? 2.253   -1.603  102.197 1.00 25.87 ? 321  GLU   B O     1 
ATOM   11272 C  CB    . GLU   B  1  323  ? 1.936   0.207   99.388  1.00 25.70 ? 321  GLU   B CB    1 
ATOM   11273 C  CG    . GLU   B  1  323  ? 2.251   -1.193  98.865  1.00 30.27 ? 321  GLU   B CG    1 
ATOM   11274 C  CD    . GLU   B  1  323  ? 1.043   -1.881  98.246  1.00 30.55 ? 321  GLU   B CD    1 
ATOM   11275 O  OE1   . GLU   B  1  323  ? 0.025   -1.201  98.002  1.00 29.13 ? 321  GLU   B OE1   1 
ATOM   11276 O  OE2   . GLU   B  1  323  ? 1.110   -3.104  98.008  1.00 30.76 ? 321  GLU   B OE2   1 
ATOM   11277 N  N     . VAL   B  1  324  ? 3.741   0.054   101.872 1.00 21.54 ? 322  VAL   B N     1 
ATOM   11278 C  CA    . VAL   B  1  324  ? 4.772   -0.625  102.652 1.00 24.85 ? 322  VAL   B CA    1 
ATOM   11279 C  C     . VAL   B  1  324  ? 4.312   -0.808  104.092 1.00 24.27 ? 322  VAL   B C     1 
ATOM   11280 O  O     . VAL   B  1  324  ? 4.431   -1.895  104.669 1.00 25.61 ? 322  VAL   B O     1 
ATOM   11281 C  CB    . VAL   B  1  324  ? 6.111   0.129   102.557 1.00 25.54 ? 322  VAL   B CB    1 
ATOM   11282 C  CG1   . VAL   B  1  324  ? 7.143   -0.493  103.492 1.00 26.25 ? 322  VAL   B CG1   1 
ATOM   11283 C  CG2   . VAL   B  1  324  ? 6.609   0.127   101.122 1.00 27.16 ? 322  VAL   B CG2   1 
ATOM   11284 N  N     . LEU   B  1  325  ? 3.755   0.245   104.687 1.00 21.82 ? 323  LEU   B N     1 
ATOM   11285 C  CA    . LEU   B  1  325  ? 3.357   0.173   106.086 1.00 24.46 ? 323  LEU   B CA    1 
ATOM   11286 C  C     . LEU   B  1  325  ? 2.294   -0.893  106.313 1.00 23.93 ? 323  LEU   B C     1 
ATOM   11287 O  O     . LEU   B  1  325  ? 2.348   -1.632  107.303 1.00 23.53 ? 323  LEU   B O     1 
ATOM   11288 C  CB    . LEU   B  1  325  ? 2.876   1.543   106.547 1.00 23.89 ? 323  LEU   B CB    1 
ATOM   11289 C  CG    . LEU   B  1  325  ? 3.983   2.594   106.550 1.00 24.47 ? 323  LEU   B CG    1 
ATOM   11290 C  CD1   . LEU   B  1  325  ? 3.392   3.983   106.665 1.00 28.62 ? 323  LEU   B CD1   1 
ATOM   11291 C  CD2   . LEU   B  1  325  ? 4.941   2.322   107.688 1.00 24.78 ? 323  LEU   B CD2   1 
ATOM   11292 N  N     . CYS   B  1  326  ? 1.325   -0.999  105.401 1.00 25.36 ? 324  CYS   B N     1 
ATOM   11293 C  CA    . CYS   B  1  326  ? 0.275   -1.994  105.570 1.00 25.66 ? 324  CYS   B CA    1 
ATOM   11294 C  C     . CYS   B  1  326  ? 0.779   -3.419  105.379 1.00 25.68 ? 324  CYS   B C     1 
ATOM   11295 O  O     . CYS   B  1  326  ? 0.167   -4.351  105.911 1.00 25.47 ? 324  CYS   B O     1 
ATOM   11296 C  CB    . CYS   B  1  326  ? -0.903  -1.691  104.644 1.00 25.84 ? 324  CYS   B CB    1 
ATOM   11297 S  SG    . CYS   B  1  326  ? -1.806  -0.202  105.106 1.00 27.45 ? 324  CYS   B SG    1 
ATOM   11298 N  N     . LEU   B  1  327  ? 1.885   -3.606  104.655 1.00 24.90 ? 325  LEU   B N     1 
ATOM   11299 C  CA    . LEU   B  1  327  ? 2.478   -4.923  104.456 1.00 28.31 ? 325  LEU   B CA    1 
ATOM   11300 C  C     . LEU   B  1  327  ? 3.598   -5.224  105.440 1.00 29.57 ? 325  LEU   B C     1 
ATOM   11301 O  O     . LEU   B  1  327  ? 4.190   -6.307  105.373 1.00 29.45 ? 325  LEU   B O     1 
ATOM   11302 C  CB    . LEU   B  1  327  ? 2.990   -5.073  103.018 1.00 25.79 ? 325  LEU   B CB    1 
ATOM   11303 C  CG    . LEU   B  1  327  ? 1.924   -4.936  101.928 1.00 29.18 ? 325  LEU   B CG    1 
ATOM   11304 C  CD1   . LEU   B  1  327  ? 2.536   -5.128  100.550 1.00 35.45 ? 325  LEU   B CD1   1 
ATOM   11305 C  CD2   . LEU   B  1  327  ? 0.779   -5.895  102.145 1.00 35.84 ? 325  LEU   B CD2   1 
ATOM   11306 N  N     . ASP   B  1  328  ? 3.898   -4.304  106.353 1.00 26.22 ? 326  ASP   B N     1 
ATOM   11307 C  CA    . ASP   B  1  328  ? 4.995   -4.483  107.298 1.00 27.90 ? 326  ASP   B CA    1 
ATOM   11308 C  C     . ASP   B  1  328  ? 4.516   -5.330  108.470 1.00 27.30 ? 326  ASP   B C     1 
ATOM   11309 O  O     . ASP   B  1  328  ? 3.682   -4.887  109.268 1.00 27.65 ? 326  ASP   B O     1 
ATOM   11310 C  CB    . ASP   B  1  328  ? 5.471   -3.119  107.780 1.00 25.82 ? 326  ASP   B CB    1 
ATOM   11311 C  CG    . ASP   B  1  328  ? 6.765   -3.197  108.570 1.00 32.01 ? 326  ASP   B CG    1 
ATOM   11312 O  OD1   . ASP   B  1  328  ? 7.036   -4.250  109.180 1.00 29.68 ? 326  ASP   B OD1   1 
ATOM   11313 O  OD2   . ASP   B  1  328  ? 7.510   -2.198  108.587 1.00 32.83 ? 326  ASP   B OD2   1 
ATOM   11314 N  N     . GLY   B  1  329  ? 5.056   -6.546  108.588 1.00 30.58 ? 327  GLY   B N     1 
ATOM   11315 C  CA    . GLY   B  1  329  ? 4.654   -7.448  109.656 1.00 28.56 ? 327  GLY   B CA    1 
ATOM   11316 C  C     . GLY   B  1  329  ? 4.948   -6.945  111.055 1.00 28.91 ? 327  GLY   B C     1 
ATOM   11317 O  O     . GLY   B  1  329  ? 4.334   -7.421  112.013 1.00 29.97 ? 327  GLY   B O     1 
ATOM   11318 N  N     . ASP   B  1  330  ? 5.876   -5.993  111.201 1.00 27.56 ? 328  ASP   B N     1 
ATOM   11319 C  CA    . ASP   B  1  330  ? 6.099   -5.386  112.509 1.00 26.40 ? 328  ASP   B CA    1 
ATOM   11320 C  C     . ASP   B  1  330  ? 4.845   -4.693  113.023 1.00 29.66 ? 328  ASP   B C     1 
ATOM   11321 O  O     . ASP   B  1  330  ? 4.679   -4.531  114.236 1.00 33.59 ? 328  ASP   B O     1 
ATOM   11322 C  CB    . ASP   B  1  330  ? 7.263   -4.394  112.450 1.00 29.59 ? 328  ASP   B CB    1 
ATOM   11323 C  CG    . ASP   B  1  330  ? 8.606   -5.078  112.253 1.00 35.03 ? 328  ASP   B CG    1 
ATOM   11324 O  OD1   . ASP   B  1  330  ? 8.682   -6.317  112.400 1.00 37.28 ? 328  ASP   B OD1   1 
ATOM   11325 O  OD2   . ASP   B  1  330  ? 9.592   -4.378  111.949 1.00 36.05 ? 328  ASP   B OD2   1 
ATOM   11326 N  N     . LEU   B  1  331  ? 3.955   -4.272  112.123 1.00 26.01 ? 329  LEU   B N     1 
ATOM   11327 C  CA    . LEU   B  1  331  ? 2.722   -3.596  112.492 1.00 27.05 ? 329  LEU   B CA    1 
ATOM   11328 C  C     . LEU   B  1  331  ? 1.531   -4.545  112.510 1.00 25.11 ? 329  LEU   B C     1 
ATOM   11329 O  O     . LEU   B  1  331  ? 0.382   -4.091  112.485 1.00 30.64 ? 329  LEU   B O     1 
ATOM   11330 C  CB    . LEU   B  1  331  ? 2.472   -2.420  111.549 1.00 25.65 ? 329  LEU   B CB    1 
ATOM   11331 C  CG    . LEU   B  1  331  ? 3.647   -1.443  111.425 1.00 25.17 ? 329  LEU   B CG    1 
ATOM   11332 C  CD1   . LEU   B  1  331  ? 3.341   -0.337  110.432 1.00 25.03 ? 329  LEU   B CD1   1 
ATOM   11333 C  CD2   . LEU   B  1  331  ? 3.987   -0.857  112.787 1.00 26.83 ? 329  LEU   B CD2   1 
ATOM   11334 N  N     . SER   B  1  332  ? 1.795   -5.849  112.559 1.00 30.70 ? 330  SER   B N     1 
ATOM   11335 C  CA    . SER   B  1  332  ? 0.763   -6.878  112.483 1.00 30.26 ? 330  SER   B CA    1 
ATOM   11336 C  C     . SER   B  1  332  ? -0.399  -6.603  113.431 1.00 32.09 ? 330  SER   B C     1 
ATOM   11337 O  O     . SER   B  1  332  ? -0.202  -6.324  114.617 1.00 34.52 ? 330  SER   B O     1 
ATOM   11338 C  CB    . SER   B  1  332  ? 1.391   -8.222  112.843 1.00 34.05 ? 330  SER   B CB    1 
ATOM   11339 O  OG    . SER   B  1  332  ? 0.398   -9.225  112.943 1.00 39.95 ? 330  SER   B OG    1 
ATOM   11340 N  N     . GLY   B  1  333  ? -1.615  -6.690  112.898 1.00 29.32 ? 331  GLY   B N     1 
ATOM   11341 C  CA    . GLY   B  1  333  ? -2.814  -6.595  113.705 1.00 32.34 ? 331  GLY   B CA    1 
ATOM   11342 C  C     . GLY   B  1  333  ? -3.182  -5.204  114.173 1.00 32.91 ? 331  GLY   B C     1 
ATOM   11343 O  O     . GLY   B  1  333  ? -4.185  -5.053  114.884 1.00 32.52 ? 331  GLY   B O     1 
ATOM   11344 N  N     . TRP   B  1  334  ? -2.420  -4.185  113.796 1.00 30.68 ? 332  TRP   B N     1 
ATOM   11345 C  CA    . TRP   B  1  334  ? -2.682  -2.817  114.229 1.00 29.48 ? 332  TRP   B CA    1 
ATOM   11346 C  C     . TRP   B  1  334  ? -3.627  -2.149  113.241 1.00 27.39 ? 332  TRP   B C     1 
ATOM   11347 O  O     . TRP   B  1  334  ? -3.305  -2.003  112.058 1.00 27.16 ? 332  TRP   B O     1 
ATOM   11348 C  CB    . TRP   B  1  334  ? -1.364  -2.057  114.334 1.00 31.09 ? 332  TRP   B CB    1 
ATOM   11349 C  CG    . TRP   B  1  334  ? -1.483  -0.600  114.648 1.00 28.38 ? 332  TRP   B CG    1 
ATOM   11350 C  CD1   . TRP   B  1  334  ? -2.071  -0.030  115.746 1.00 29.34 ? 332  TRP   B CD1   1 
ATOM   11351 C  CD2   . TRP   B  1  334  ? -0.950  0.474   113.875 1.00 28.18 ? 332  TRP   B CD2   1 
ATOM   11352 N  NE1   . TRP   B  1  334  ? -1.952  1.341   115.686 1.00 27.82 ? 332  TRP   B NE1   1 
ATOM   11353 C  CE2   . TRP   B  1  334  ? -1.266  1.674   114.548 1.00 25.70 ? 332  TRP   B CE2   1 
ATOM   11354 C  CE3   . TRP   B  1  334  ? -0.249  0.542   112.669 1.00 27.17 ? 332  TRP   B CE3   1 
ATOM   11355 C  CZ2   . TRP   B  1  334  ? -0.900  2.925   114.049 1.00 24.72 ? 332  TRP   B CZ2   1 
ATOM   11356 C  CZ3   . TRP   B  1  334  ? 0.119   1.778   112.188 1.00 29.49 ? 332  TRP   B CZ3   1 
ATOM   11357 C  CH2   . TRP   B  1  334  ? -0.206  2.953   112.875 1.00 27.55 ? 332  TRP   B CH2   1 
ATOM   11358 N  N     . ASN   B  1  335  ? -4.803  -1.763  113.718 1.00 27.90 ? 333  ASN   B N     1 
ATOM   11359 C  CA    . ASN   B  1  335  ? -5.795  -1.125  112.870 1.00 27.26 ? 333  ASN   B CA    1 
ATOM   11360 C  C     . ASN   B  1  335  ? -5.750  0.388   112.982 1.00 24.91 ? 333  ASN   B C     1 
ATOM   11361 O  O     . ASN   B  1  335  ? -6.678  1.073   112.539 1.00 27.00 ? 333  ASN   B O     1 
ATOM   11362 C  CB    . ASN   B  1  335  ? -7.180  -1.691  113.164 1.00 29.92 ? 333  ASN   B CB    1 
ATOM   11363 C  CG    . ASN   B  1  335  ? -7.287  -3.146  112.761 1.00 33.71 ? 333  ASN   B CG    1 
ATOM   11364 O  OD1   . ASN   B  1  335  ? -6.606  -3.579  111.828 1.00 30.16 ? 333  ASN   B OD1   1 
ATOM   11365 N  ND2   . ASN   B  1  335  ? -8.125  -3.908  113.460 1.00 31.95 ? 333  ASN   B ND2   1 
ATOM   11366 N  N     . GLY   B  1  336  ? -4.673  0.920   113.551 1.00 25.94 ? 334  GLY   B N     1 
ATOM   11367 C  CA    . GLY   B  1  336  ? -4.549  2.336   113.792 1.00 26.47 ? 334  GLY   B CA    1 
ATOM   11368 C  C     . GLY   B  1  336  ? -3.940  3.151   112.686 1.00 24.60 ? 334  GLY   B C     1 
ATOM   11369 O  O     . GLY   B  1  336  ? -3.896  4.379   112.804 1.00 23.01 ? 334  GLY   B O     1 
ATOM   11370 N  N     . MET   B  1  337  ? -3.460  2.536   111.610 1.00 25.62 ? 335  MET   B N     1 
ATOM   11371 C  CA    A MET   B  1  337  ? -2.939  3.307   110.489 0.55 24.13 ? 335  MET   B CA    1 
ATOM   11372 C  CA    B MET   B  1  337  ? -2.933  3.317   110.501 0.45 24.14 ? 335  MET   B CA    1 
ATOM   11373 C  C     . MET   B  1  337  ? -4.063  4.125   109.874 1.00 23.48 ? 335  MET   B C     1 
ATOM   11374 O  O     . MET   B  1  337  ? -5.086  3.565   109.460 1.00 24.53 ? 335  MET   B O     1 
ATOM   11375 C  CB    A MET   B  1  337  ? -2.373  2.361   109.436 0.55 26.70 ? 335  MET   B CB    1 
ATOM   11376 C  CB    B MET   B  1  337  ? -2.275  2.416   109.462 0.45 26.69 ? 335  MET   B CB    1 
ATOM   11377 C  CG    A MET   B  1  337  ? -1.939  3.054   108.160 0.55 24.38 ? 335  MET   B CG    1 
ATOM   11378 C  CG    B MET   B  1  337  ? -1.449  3.181   108.443 0.45 25.98 ? 335  MET   B CG    1 
ATOM   11379 S  SD    A MET   B  1  337  ? -0.236  3.605   108.285 0.55 28.50 ? 335  MET   B SD    1 
ATOM   11380 S  SD    B MET   B  1  337  ? -0.125  4.129   109.226 0.45 26.95 ? 335  MET   B SD    1 
ATOM   11381 C  CE    A MET   B  1  337  ? -0.444  5.367   108.543 0.55 24.03 ? 335  MET   B CE    1 
ATOM   11382 C  CE    B MET   B  1  337  ? 1.199   2.938   109.272 0.45 26.65 ? 335  MET   B CE    1 
ATOM   11383 N  N     . GLY   B  1  338  ? -3.871  5.438   109.820 1.00 22.52 ? 336  GLY   B N     1 
ATOM   11384 C  CA    . GLY   B  1  338  ? -4.857  6.344   109.272 1.00 25.19 ? 336  GLY   B CA    1 
ATOM   11385 C  C     . GLY   B  1  338  ? -4.327  7.066   108.050 1.00 22.20 ? 336  GLY   B C     1 
ATOM   11386 O  O     . GLY   B  1  338  ? -3.128  7.310   107.920 1.00 20.89 ? 336  GLY   B O     1 
ATOM   11387 N  N     . PHE   B  1  339  ? -5.232  7.394   107.139 1.00 21.70 ? 337  PHE   B N     1 
ATOM   11388 C  CA    . PHE   B  1  339  ? -4.809  7.992   105.887 1.00 21.23 ? 337  PHE   B CA    1 
ATOM   11389 C  C     . PHE   B  1  339  ? -5.916  8.914   105.412 1.00 20.47 ? 337  PHE   B C     1 
ATOM   11390 O  O     . PHE   B  1  339  ? -7.083  8.511   105.366 1.00 21.32 ? 337  PHE   B O     1 
ATOM   11391 C  CB    . PHE   B  1  339  ? -4.530  6.896   104.858 1.00 21.49 ? 337  PHE   B CB    1 
ATOM   11392 C  CG    . PHE   B  1  339  ? -3.810  7.377   103.641 1.00 21.42 ? 337  PHE   B CG    1 
ATOM   11393 C  CD1   . PHE   B  1  339  ? -2.426  7.455   103.615 1.00 20.83 ? 337  PHE   B CD1   1 
ATOM   11394 C  CD2   . PHE   B  1  339  ? -4.520  7.750   102.515 1.00 21.32 ? 337  PHE   B CD2   1 
ATOM   11395 C  CE1   . PHE   B  1  339  ? -1.764  7.904   102.466 1.00 23.00 ? 337  PHE   B CE1   1 
ATOM   11396 C  CE2   . PHE   B  1  339  ? -3.872  8.187   101.369 1.00 21.34 ? 337  PHE   B CE2   1 
ATOM   11397 C  CZ    . PHE   B  1  339  ? -2.491  8.266   101.350 1.00 22.30 ? 337  PHE   B CZ    1 
ATOM   11398 N  N     . VAL   B  1  340  ? -5.560  10.140  105.094 1.00 20.29 ? 338  VAL   B N     1 
ATOM   11399 C  CA    . VAL   B  1  340  ? -6.526  11.137  104.654 1.00 20.22 ? 338  VAL   B CA    1 
ATOM   11400 C  C     . VAL   B  1  340  ? -6.683  11.039  103.150 1.00 19.34 ? 338  VAL   B C     1 
ATOM   11401 O  O     . VAL   B  1  340  ? -5.702  10.878  102.421 1.00 20.02 ? 338  VAL   B O     1 
ATOM   11402 C  CB    . VAL   B  1  340  ? -6.070  12.549  105.055 1.00 21.16 ? 338  VAL   B CB    1 
ATOM   11403 C  CG1   . VAL   B  1  340  ? -7.057  13.584  104.531 1.00 21.56 ? 338  VAL   B CG1   1 
ATOM   11404 C  CG2   . VAL   B  1  340  ? -5.929  12.635  106.565 1.00 20.82 ? 338  VAL   B CG2   1 
ATOM   11405 N  N     . VAL   B  1  341  ? -7.915  11.168  102.681 1.00 20.47 ? 339  VAL   B N     1 
ATOM   11406 C  CA    . VAL   B  1  341  ? -8.197  11.330  101.263 1.00 21.43 ? 339  VAL   B CA    1 
ATOM   11407 C  C     . VAL   B  1  341  ? -9.042  12.580  101.091 1.00 19.37 ? 339  VAL   B C     1 
ATOM   11408 O  O     . VAL   B  1  341  ? -9.986  12.815  101.861 1.00 20.45 ? 339  VAL   B O     1 
ATOM   11409 C  CB    . VAL   B  1  341  ? -8.881  10.088  100.663 1.00 23.76 ? 339  VAL   B CB    1 
ATOM   11410 C  CG1   . VAL   B  1  341  ? -8.008  8.875   100.836 1.00 24.80 ? 339  VAL   B CG1   1 
ATOM   11411 C  CG2   . VAL   B  1  341  ? -10.236 9.851   101.304 1.00 28.45 ? 339  VAL   B CG2   1 
ATOM   11412 N  N     . GLN   B  1  342  ? -8.692  13.383  100.088 1.00 18.79 ? 340  GLN   B N     1 
ATOM   11413 C  CA    . GLN   B  1  342  ? -9.272  14.705  99.874  1.00 19.43 ? 340  GLN   B CA    1 
ATOM   11414 C  C     . GLN   B  1  342  ? -10.323 14.611  98.777  1.00 19.08 ? 340  GLN   B C     1 
ATOM   11415 O  O     . GLN   B  1  342  ? -10.000 14.363  97.609  1.00 20.19 ? 340  GLN   B O     1 
ATOM   11416 C  CB    . GLN   B  1  342  ? -8.182  15.702  99.494  1.00 19.59 ? 340  GLN   B CB    1 
ATOM   11417 C  CG    . GLN   B  1  342  ? -7.134  15.898  100.570 1.00 18.44 ? 340  GLN   B CG    1 
ATOM   11418 C  CD    . GLN   B  1  342  ? -5.766  16.238  99.974  1.00 18.40 ? 340  GLN   B CD    1 
ATOM   11419 O  OE1   . GLN   B  1  342  ? -5.324  15.621  99.002  1.00 17.69 ? 340  GLN   B OE1   1 
ATOM   11420 N  NE2   . GLN   B  1  342  ? -5.097  17.225  100.552 1.00 17.59 ? 340  GLN   B NE2   1 
ATOM   11421 N  N     . ALA   B  1  343  ? -11.578 14.836  99.153  1.00 18.96 ? 341  ALA   B N     1 
ATOM   11422 C  CA    . ALA   B  1  343  ? -12.679 14.712  98.213  1.00 19.60 ? 341  ALA   B CA    1 
ATOM   11423 C  C     . ALA   B  1  343  ? -12.715 15.847  97.207  1.00 19.83 ? 341  ALA   B C     1 
ATOM   11424 O  O     . ALA   B  1  343  ? -13.405 15.718  96.187  1.00 20.24 ? 341  ALA   B O     1 
ATOM   11425 C  CB    . ALA   B  1  343  ? -14.001 14.645  98.969  1.00 22.17 ? 341  ALA   B CB    1 
ATOM   11426 N  N     . TYR   B  1  344  ? -11.998 16.954  97.447  1.00 19.90 ? 342  TYR   B N     1 
ATOM   11427 C  CA    . TYR   B  1  344  ? -11.909 17.936  96.380  1.00 19.77 ? 342  TYR   B CA    1 
ATOM   11428 C  C     . TYR   B  1  344  ? -11.044 17.456  95.233  1.00 18.25 ? 342  TYR   B C     1 
ATOM   11429 O  O     . TYR   B  1  344  ? -10.973 18.139  94.211  1.00 19.35 ? 342  TYR   B O     1 
ATOM   11430 C  CB    . TYR   B  1  344  ? -11.491 19.338  96.863  1.00 20.00 ? 342  TYR   B CB    1 
ATOM   11431 C  CG    . TYR   B  1  344  ? -10.043 19.603  97.281  1.00 18.64 ? 342  TYR   B CG    1 
ATOM   11432 C  CD1   . TYR   B  1  344  ? -9.084  18.602  97.347  1.00 19.05 ? 342  TYR   B CD1   1 
ATOM   11433 C  CD2   . TYR   B  1  344  ? -9.669  20.887  97.646  1.00 17.23 ? 342  TYR   B CD2   1 
ATOM   11434 C  CE1   . TYR   B  1  344  ? -7.774  18.889  97.743  1.00 16.54 ? 342  TYR   B CE1   1 
ATOM   11435 C  CE2   . TYR   B  1  344  ? -8.396  21.175  98.056  1.00 18.48 ? 342  TYR   B CE2   1 
ATOM   11436 C  CZ    . TYR   B  1  344  ? -7.455  20.187  98.095  1.00 17.48 ? 342  TYR   B CZ    1 
ATOM   11437 O  OH    . TYR   B  1  344  ? -6.196  20.525  98.530  1.00 17.16 ? 342  TYR   B OH    1 
ATOM   11438 N  N     . GLY   B  1  345  ? -10.394 16.306  95.392  1.00 18.46 ? 343  GLY   B N     1 
ATOM   11439 C  CA    . GLY   B  1  345  ? -9.513  15.784  94.370  1.00 19.04 ? 343  GLY   B CA    1 
ATOM   11440 C  C     . GLY   B  1  345  ? -10.246 14.808  93.464  1.00 20.26 ? 343  GLY   B C     1 
ATOM   11441 O  O     . GLY   B  1  345  ? -11.042 13.988  93.920  1.00 19.91 ? 343  GLY   B O     1 
ATOM   11442 N  N     . LYS   B  1  346  ? -9.926  14.889  92.173  1.00 19.17 ? 344  LYS   B N     1 
ATOM   11443 C  CA    . LYS   B  1  346  ? -10.573 14.050  91.178  1.00 19.90 ? 344  LYS   B CA    1 
ATOM   11444 C  C     . LYS   B  1  346  ? -10.213 12.584  91.329  1.00 19.40 ? 344  LYS   B C     1 
ATOM   11445 O  O     . LYS   B  1  346  ? -10.943 11.727  90.827  1.00 21.35 ? 344  LYS   B O     1 
ATOM   11446 C  CB    . LYS   B  1  346  ? -10.181 14.531  89.786  1.00 19.85 ? 344  LYS   B CB    1 
ATOM   11447 C  CG    . LYS   B  1  346  ? -10.606 15.954  89.531  1.00 20.31 ? 344  LYS   B CG    1 
ATOM   11448 C  CD    . LYS   B  1  346  ? -10.102 16.446  88.210  1.00 20.99 ? 344  LYS   B CD    1 
ATOM   11449 C  CE    . LYS   B  1  346  ? -10.771 17.758  87.874  1.00 20.97 ? 344  LYS   B CE    1 
ATOM   11450 N  NZ    . LYS   B  1  346  ? -10.207 18.341  86.631  1.00 20.04 ? 344  LYS   B NZ    1 
ATOM   11451 N  N     . ARG   B  1  347  ? -9.093  12.277  91.981  1.00 19.02 ? 345  ARG   B N     1 
ATOM   11452 C  CA    . ARG   B  1  347  ? -8.697  10.889  92.155  1.00 20.83 ? 345  ARG   B CA    1 
ATOM   11453 C  C     . ARG   B  1  347  ? -9.336  10.240  93.369  1.00 19.28 ? 345  ARG   B C     1 
ATOM   11454 O  O     . ARG   B  1  347  ? -9.209  9.022   93.535  1.00 21.36 ? 345  ARG   B O     1 
ATOM   11455 C  CB    . ARG   B  1  347  ? -7.177  10.784  92.241  1.00 19.87 ? 345  ARG   B CB    1 
ATOM   11456 C  CG    . ARG   B  1  347  ? -6.514  11.165  90.937  1.00 17.81 ? 345  ARG   B CG    1 
ATOM   11457 C  CD    . ARG   B  1  347  ? -5.043  11.435  91.125  1.00 18.17 ? 345  ARG   B CD    1 
ATOM   11458 N  NE    . ARG   B  1  347  ? -4.811  12.677  91.852  1.00 17.78 ? 345  ARG   B NE    1 
ATOM   11459 C  CZ    . ARG   B  1  347  ? -3.626  13.031  92.318  1.00 19.46 ? 345  ARG   B CZ    1 
ATOM   11460 N  NH1   . ARG   B  1  347  ? -2.563  12.267  92.137  1.00 19.65 ? 345  ARG   B NH1   1 
ATOM   11461 N  NH2   . ARG   B  1  347  ? -3.501  14.184  92.969  1.00 16.88 ? 345  ARG   B NH2   1 
ATOM   11462 N  N     . CYS   B  1  348  ? -10.049 11.019  94.182  1.00 20.54 ? 346  CYS   B N     1 
ATOM   11463 C  CA    . CYS   B  1  348  ? -10.542 10.550  95.477  1.00 20.56 ? 346  CYS   B CA    1 
ATOM   11464 C  C     . CYS   B  1  348  ? -11.223 9.189   95.441  1.00 22.40 ? 346  CYS   B C     1 
ATOM   11465 O  O     . CYS   B  1  348  ? -10.816 8.305   96.209  1.00 23.22 ? 346  CYS   B O     1 
ATOM   11466 C  CB    . CYS   B  1  348  ? -11.424 11.616  96.138  1.00 20.91 ? 346  CYS   B CB    1 
ATOM   11467 S  SG    . CYS   B  1  348  ? -11.713 11.250  97.890  1.00 26.89 ? 346  CYS   B SG    1 
ATOM   11468 N  N     . PRO   B  1  349  ? -12.246 8.945   94.617  1.00 22.20 ? 347  PRO   B N     1 
ATOM   11469 C  CA    . PRO   B  1  349  ? -12.869 7.613   94.650  1.00 24.22 ? 347  PRO   B CA    1 
ATOM   11470 C  C     . PRO   B  1  349  ? -11.923 6.500   94.238  1.00 20.74 ? 347  PRO   B C     1 
ATOM   11471 O  O     . PRO   B  1  349  ? -12.027 5.386   94.768  1.00 22.95 ? 347  PRO   B O     1 
ATOM   11472 C  CB    . PRO   B  1  349  ? -14.075 7.745   93.709  1.00 24.00 ? 347  PRO   B CB    1 
ATOM   11473 C  CG    . PRO   B  1  349  ? -13.768 8.883   92.838  1.00 25.32 ? 347  PRO   B CG    1 
ATOM   11474 C  CD    . PRO   B  1  349  ? -12.843 9.811   93.585  1.00 23.56 ? 347  PRO   B CD    1 
ATOM   11475 N  N     . PHE   B  1  350  ? -10.980 6.782   93.339  1.00 21.55 ? 348  PHE   B N     1 
ATOM   11476 C  CA    . PHE   B  1  350  ? -10.034 5.762   92.904  1.00 23.21 ? 348  PHE   B CA    1 
ATOM   11477 C  C     . PHE   B  1  350  ? -8.980  5.498   93.966  1.00 20.25 ? 348  PHE   B C     1 
ATOM   11478 O  O     . PHE   B  1  350  ? -8.567  4.348   94.166  1.00 23.20 ? 348  PHE   B O     1 
ATOM   11479 C  CB    . PHE   B  1  350  ? -9.431  6.187   91.571  1.00 20.58 ? 348  PHE   B CB    1 
ATOM   11480 C  CG    . PHE   B  1  350  ? -10.479 6.568   90.586  1.00 21.62 ? 348  PHE   B CG    1 
ATOM   11481 C  CD1   . PHE   B  1  350  ? -11.191 5.590   89.909  1.00 25.16 ? 348  PHE   B CD1   1 
ATOM   11482 C  CD2   . PHE   B  1  350  ? -10.810 7.898   90.387  1.00 22.98 ? 348  PHE   B CD2   1 
ATOM   11483 C  CE1   . PHE   B  1  350  ? -12.197 5.937   89.024  1.00 27.84 ? 348  PHE   B CE1   1 
ATOM   11484 C  CE2   . PHE   B  1  350  ? -11.813 8.252   89.503  1.00 23.21 ? 348  PHE   B CE2   1 
ATOM   11485 C  CZ    . PHE   B  1  350  ? -12.506 7.273   88.822  1.00 23.85 ? 348  PHE   B CZ    1 
ATOM   11486 N  N     . VAL   B  1  351  ? -8.582  6.540   94.695  1.00 20.27 ? 349  VAL   B N     1 
ATOM   11487 C  CA    . VAL   B  1  351  ? -7.716  6.342   95.855  1.00 20.29 ? 349  VAL   B CA    1 
ATOM   11488 C  C     . VAL   B  1  351  ? -8.427  5.495   96.901  1.00 22.85 ? 349  VAL   B C     1 
ATOM   11489 O  O     . VAL   B  1  351  ? -7.832  4.598   97.509  1.00 23.23 ? 349  VAL   B O     1 
ATOM   11490 C  CB    . VAL   B  1  351  ? -7.283  7.701   96.425  1.00 19.78 ? 349  VAL   B CB    1 
ATOM   11491 C  CG1   . VAL   B  1  351  ? -6.438  7.502   97.693  1.00 19.94 ? 349  VAL   B CG1   1 
ATOM   11492 C  CG2   . VAL   B  1  351  ? -6.519  8.475   95.371  1.00 20.79 ? 349  VAL   B CG2   1 
ATOM   11493 N  N     . LEU   B  1  352  ? -9.717  5.759   97.119  1.00 20.67 ? 350  LEU   B N     1 
ATOM   11494 C  CA    . LEU   B  1  352  ? -10.469 4.962   98.078  1.00 21.64 ? 350  LEU   B CA    1 
ATOM   11495 C  C     . LEU   B  1  352  ? -10.533 3.503   97.653  1.00 23.20 ? 350  LEU   B C     1 
ATOM   11496 O  O     . LEU   B  1  352  ? -10.363 2.605   98.483  1.00 24.28 ? 350  LEU   B O     1 
ATOM   11497 C  CB    . LEU   B  1  352  ? -11.864 5.539   98.273  1.00 23.33 ? 350  LEU   B CB    1 
ATOM   11498 C  CG    . LEU   B  1  352  ? -11.908 6.845   99.059  1.00 24.51 ? 350  LEU   B CG    1 
ATOM   11499 C  CD1   . LEU   B  1  352  ? -13.334 7.341   99.087  1.00 27.32 ? 350  LEU   B CD1   1 
ATOM   11500 C  CD2   . LEU   B  1  352  ? -11.392 6.615   100.481 1.00 28.85 ? 350  LEU   B CD2   1 
ATOM   11501 N  N     . ASP   B  1  353  ? -10.774 3.249   96.360  1.00 23.10 ? 351  ASP   B N     1 
ATOM   11502 C  CA    . ASP   B  1  353  ? -10.740 1.879   95.851  1.00 25.21 ? 351  ASP   B CA    1 
ATOM   11503 C  C     . ASP   B  1  353  ? -9.399  1.225   96.152  1.00 21.71 ? 351  ASP   B C     1 
ATOM   11504 O  O     . ASP   B  1  353  ? -9.340  0.066   96.578  1.00 24.77 ? 351  ASP   B O     1 
ATOM   11505 C  CB    . ASP   B  1  353  ? -10.969 1.862   94.338  1.00 26.90 ? 351  ASP   B CB    1 
ATOM   11506 C  CG    . ASP   B  1  353  ? -12.386 2.220   93.942  1.00 29.28 ? 351  ASP   B CG    1 
ATOM   11507 O  OD1   . ASP   B  1  353  ? -13.301 2.103   94.780  1.00 30.42 ? 351  ASP   B OD1   1 
ATOM   11508 O  OD2   . ASP   B  1  353  ? -12.573 2.624   92.771  1.00 33.39 ? 351  ASP   B OD2   1 
ATOM   11509 N  N     . PHE   B  1  354  ? -8.309  1.948   95.905  1.00 24.02 ? 352  PHE   B N     1 
ATOM   11510 C  CA    . PHE   B  1  354  ? -6.982  1.422   96.205  1.00 22.92 ? 352  PHE   B CA    1 
ATOM   11511 C  C     . PHE   B  1  354  ? -6.830  1.112   97.689  1.00 22.91 ? 352  PHE   B C     1 
ATOM   11512 O  O     . PHE   B  1  354  ? -6.354  0.035   98.060  1.00 24.82 ? 352  PHE   B O     1 
ATOM   11513 C  CB    . PHE   B  1  354  ? -5.907  2.412   95.761  1.00 23.78 ? 352  PHE   B CB    1 
ATOM   11514 C  CG    . PHE   B  1  354  ? -4.533  2.057   96.261  1.00 23.15 ? 352  PHE   B CG    1 
ATOM   11515 C  CD1   . PHE   B  1  354  ? -3.752  1.145   95.579  1.00 24.37 ? 352  PHE   B CD1   1 
ATOM   11516 C  CD2   . PHE   B  1  354  ? -4.040  2.610   97.437  1.00 23.23 ? 352  PHE   B CD2   1 
ATOM   11517 C  CE1   . PHE   B  1  354  ? -2.494  0.794   96.053  1.00 24.60 ? 352  PHE   B CE1   1 
ATOM   11518 C  CE2   . PHE   B  1  354  ? -2.791  2.260   97.915  1.00 24.47 ? 352  PHE   B CE2   1 
ATOM   11519 C  CZ    . PHE   B  1  354  ? -2.021  1.356   97.225  1.00 25.69 ? 352  PHE   B CZ    1 
ATOM   11520 N  N     . ILE   B  1  355  ? -7.232  2.050   98.553  1.00 22.19 ? 353  ILE   B N     1 
ATOM   11521 C  CA    . ILE   B  1  355  ? -7.073  1.857   99.995  1.00 22.78 ? 353  ILE   B CA    1 
ATOM   11522 C  C     . ILE   B  1  355  ? -7.930  0.701   100.478 1.00 23.38 ? 353  ILE   B C     1 
ATOM   11523 O  O     . ILE   B  1  355  ? -7.484  -0.126  101.283 1.00 24.29 ? 353  ILE   B O     1 
ATOM   11524 C  CB    . ILE   B  1  355  ? -7.395  3.150   100.763 1.00 23.89 ? 353  ILE   B CB    1 
ATOM   11525 C  CG1   . ILE   B  1  355  ? -6.387  4.238   100.423 1.00 25.85 ? 353  ILE   B CG1   1 
ATOM   11526 C  CG2   . ILE   B  1  355  ? -7.443  2.889   102.275 1.00 25.91 ? 353  ILE   B CG2   1 
ATOM   11527 C  CD1   . ILE   B  1  355  ? -6.761  5.568   100.992 1.00 24.15 ? 353  ILE   B CD1   1 
ATOM   11528 N  N     . ILE   B  1  356  ? -9.178  0.634   100.013 1.00 24.11 ? 354  ILE   B N     1 
ATOM   11529 C  CA    . ILE   B  1  356  ? -10.064 -0.442  100.441 1.00 25.96 ? 354  ILE   B CA    1 
ATOM   11530 C  C     . ILE   B  1  356  ? -9.485  -1.789  100.041 1.00 25.26 ? 354  ILE   B C     1 
ATOM   11531 O  O     . ILE   B  1  356  ? -9.523  -2.756  100.812 1.00 26.40 ? 354  ILE   B O     1 
ATOM   11532 C  CB    . ILE   B  1  356  ? -11.479 -0.224  99.876  1.00 25.60 ? 354  ILE   B CB    1 
ATOM   11533 C  CG1   . ILE   B  1  356  ? -12.137 0.971   100.577 1.00 29.33 ? 354  ILE   B CG1   1 
ATOM   11534 C  CG2   . ILE   B  1  356  ? -12.314 -1.488  100.033 1.00 27.63 ? 354  ILE   B CG2   1 
ATOM   11535 C  CD1   . ILE   B  1  356  ? -13.404 1.481   99.906  1.00 27.43 ? 354  ILE   B CD1   1 
ATOM   11536 N  N     . ASP   B  1  357  ? -8.934  -1.871  98.828  1.00 25.51 ? 355  ASP   B N     1 
ATOM   11537 C  CA    . ASP   B  1  357  ? -8.319  -3.115  98.393  1.00 26.55 ? 355  ASP   B CA    1 
ATOM   11538 C  C     . ASP   B  1  357  ? -7.066  -3.421  99.199  1.00 23.36 ? 355  ASP   B C     1 
ATOM   11539 O  O     . ASP   B  1  357  ? -6.839  -4.575  99.580  1.00 24.98 ? 355  ASP   B O     1 
ATOM   11540 C  CB    . ASP   B  1  357  ? -7.991  -3.051  96.907  1.00 26.75 ? 355  ASP   B CB    1 
ATOM   11541 C  CG    . ASP   B  1  357  ? -7.134  -4.214  96.458  1.00 27.51 ? 355  ASP   B CG    1 
ATOM   11542 O  OD1   . ASP   B  1  357  ? -7.681  -5.328  96.297  1.00 29.49 ? 355  ASP   B OD1   1 
ATOM   11543 O  OD2   . ASP   B  1  357  ? -5.914  -4.018  96.284  1.00 25.88 ? 355  ASP   B OD2   1 
ATOM   11544 N  N     . LEU   B  1  358  ? -6.241  -2.405  99.465  1.00 24.36 ? 356  LEU   B N     1 
ATOM   11545 C  CA    . LEU   B  1  358  ? -5.055  -2.623  100.282 1.00 23.48 ? 356  LEU   B CA    1 
ATOM   11546 C  C     . LEU   B  1  358  ? -5.443  -3.141  101.657 1.00 22.67 ? 356  LEU   B C     1 
ATOM   11547 O  O     . LEU   B  1  358  ? -4.817  -4.072  102.179 1.00 25.03 ? 356  LEU   B O     1 
ATOM   11548 C  CB    . LEU   B  1  358  ? -4.276  -1.321  100.418 1.00 22.17 ? 356  LEU   B CB    1 
ATOM   11549 C  CG    . LEU   B  1  358  ? -3.052  -1.339  101.340 1.00 24.39 ? 356  LEU   B CG    1 
ATOM   11550 C  CD1   . LEU   B  1  358  ? -2.038  -2.379  100.904 1.00 26.33 ? 356  LEU   B CD1   1 
ATOM   11551 C  CD2   . LEU   B  1  358  ? -2.429  0.036   101.336 1.00 22.81 ? 356  LEU   B CD2   1 
ATOM   11552 N  N     . ALA   B  1  359  ? -6.490  -2.561  102.250 1.00 24.55 ? 357  ALA   B N     1 
ATOM   11553 C  CA    . ALA   B  1  359  ? -6.963  -3.024  103.547 1.00 24.46 ? 357  ALA   B CA    1 
ATOM   11554 C  C     . ALA   B  1  359  ? -7.365  -4.488  103.479 1.00 25.85 ? 357  ALA   B C     1 
ATOM   11555 O  O     . ALA   B  1  359  ? -6.977  -5.294  104.332 1.00 27.17 ? 357  ALA   B O     1 
ATOM   11556 C  CB    . ALA   B  1  359  ? -8.145  -2.167  104.002 1.00 28.37 ? 357  ALA   B CB    1 
ATOM   11557 N  N     . ARG   B  1  360  ? -8.119  -4.853  102.438 1.00 25.46 ? 358  ARG   B N     1 
ATOM   11558 C  CA    . ARG   B  1  360  ? -8.577  -6.228  102.289 1.00 28.65 ? 358  ARG   B CA    1 
ATOM   11559 C  C     . ARG   B  1  360  ? -7.414  -7.198  102.137 1.00 23.39 ? 358  ARG   B C     1 
ATOM   11560 O  O     . ARG   B  1  360  ? -7.398  -8.260  102.768 1.00 26.69 ? 358  ARG   B O     1 
ATOM   11561 C  CB    . ARG   B  1  360  ? -9.543  -6.340  101.110 1.00 27.57 ? 358  ARG   B CB    1 
ATOM   11562 C  CG    . ARG   B  1  360  ? -10.980 -6.365  101.546 1.00 36.11 ? 358  ARG   B CG    1 
ATOM   11563 C  CD    . ARG   B  1  360  ? -11.892 -6.788  100.412 1.00 37.28 ? 358  ARG   B CD    1 
ATOM   11564 N  NE    . ARG   B  1  360  ? -12.438 -5.640  99.701  1.00 40.87 ? 358  ARG   B NE    1 
ATOM   11565 C  CZ    . ARG   B  1  360  ? -13.651 -5.149  99.907  1.00 38.71 ? 358  ARG   B CZ    1 
ATOM   11566 N  NH1   . ARG   B  1  360  ? -14.460 -5.665  100.818 1.00 46.18 ? 358  ARG   B NH1   1 
ATOM   11567 N  NH2   . ARG   B  1  360  ? -14.068 -4.122  99.171  1.00 45.98 ? 358  ARG   B NH2   1 
ATOM   11568 N  N     . ARG   B  1  361  ? -6.426  -6.858  101.309 1.00 26.57 ? 359  ARG   B N     1 
ATOM   11569 C  CA    . ARG   B  1  361  ? -5.370  -7.827  101.053 1.00 28.10 ? 359  ARG   B CA    1 
ATOM   11570 C  C     . ARG   B  1  361  ? -4.295  -7.853  102.130 1.00 24.50 ? 359  ARG   B C     1 
ATOM   11571 O  O     . ARG   B  1  361  ? -3.578  -8.850  102.237 1.00 27.09 ? 359  ARG   B O     1 
ATOM   11572 C  CB    . ARG   B  1  361  ? -4.767  -7.639  99.661  1.00 33.03 ? 359  ARG   B CB    1 
ATOM   11573 C  CG    . ARG   B  1  361  ? -4.111  -6.308  99.442  1.00 32.94 ? 359  ARG   B CG    1 
ATOM   11574 C  CD    . ARG   B  1  361  ? -3.690  -6.164  97.984  1.00 28.71 ? 359  ARG   B CD    1 
ATOM   11575 N  NE    . ARG   B  1  361  ? -3.466  -4.766  97.651  1.00 25.91 ? 359  ARG   B NE    1 
ATOM   11576 C  CZ    . ARG   B  1  361  ? -2.297  -4.150  97.754  1.00 26.35 ? 359  ARG   B CZ    1 
ATOM   11577 N  NH1   . ARG   B  1  361  ? -1.213  -4.788  98.161  1.00 27.12 ? 359  ARG   B NH1   1 
ATOM   11578 N  NH2   . ARG   B  1  361  ? -2.214  -2.860  97.438  1.00 23.44 ? 359  ARG   B NH2   1 
ATOM   11579 N  N     . SER   B  1  362  ? -4.182  -6.802  102.945 1.00 25.78 ? 360  SER   B N     1 
ATOM   11580 C  CA    . SER   B  1  362  ? -3.176  -6.754  103.997 1.00 27.16 ? 360  SER   B CA    1 
ATOM   11581 C  C     . SER   B  1  362  ? -3.701  -7.185  105.360 1.00 26.72 ? 360  SER   B C     1 
ATOM   11582 O  O     . SER   B  1  362  ? -2.900  -7.358  106.286 1.00 28.87 ? 360  SER   B O     1 
ATOM   11583 C  CB    . SER   B  1  362  ? -2.595  -5.340  104.104 1.00 29.28 ? 360  SER   B CB    1 
ATOM   11584 O  OG    . SER   B  1  362  ? -3.571  -4.432  104.583 1.00 26.71 ? 360  SER   B OG    1 
ATOM   11585 N  N     . GLY   B  1  363  ? -5.010  -7.333  105.522 1.00 26.38 ? 361  GLY   B N     1 
ATOM   11586 C  CA    . GLY   B  1  363  ? -5.538  -7.685  106.824 1.00 27.24 ? 361  GLY   B CA    1 
ATOM   11587 C  C     . GLY   B  1  363  ? -5.420  -6.566  107.830 1.00 28.13 ? 361  GLY   B C     1 
ATOM   11588 O  O     . GLY   B  1  363  ? -5.215  -6.824  109.017 1.00 29.97 ? 361  GLY   B O     1 
ATOM   11589 N  N     . ARG   B  1  364  ? -5.548  -5.326  107.378 1.00 28.95 ? 362  ARG   B N     1 
ATOM   11590 C  CA    . ARG   B  1  364  ? -5.493  -4.147  108.229 1.00 29.39 ? 362  ARG   B CA    1 
ATOM   11591 C  C     . ARG   B  1  364  ? -6.775  -3.374  107.990 1.00 29.93 ? 362  ARG   B C     1 
ATOM   11592 O  O     . ARG   B  1  364  ? -7.123  -3.098  106.839 1.00 32.73 ? 362  ARG   B O     1 
ATOM   11593 C  CB    . ARG   B  1  364  ? -4.344  -3.235  107.795 1.00 30.68 ? 362  ARG   B CB    1 
ATOM   11594 C  CG    . ARG   B  1  364  ? -2.963  -3.846  107.850 1.00 26.14 ? 362  ARG   B CG    1 
ATOM   11595 C  CD    . ARG   B  1  364  ? -2.434  -3.872  109.272 1.00 27.53 ? 362  ARG   B CD    1 
ATOM   11596 N  NE    . ARG   B  1  364  ? -1.167  -4.586  109.326 1.00 26.10 ? 362  ARG   B NE    1 
ATOM   11597 C  CZ    . ARG   B  1  364  ? 0.022   -4.032  109.132 1.00 26.19 ? 362  ARG   B CZ    1 
ATOM   11598 N  NH1   . ARG   B  1  364  ? 0.159   -2.730  108.926 1.00 26.21 ? 362  ARG   B NH1   1 
ATOM   11599 N  NH2   . ARG   B  1  364  ? 1.103   -4.804  109.153 1.00 29.75 ? 362  ARG   B NH2   1 
ATOM   11600 N  N     . ARG   B  1  365  ? -7.484  -3.030  109.053 1.00 27.40 ? 363  ARG   B N     1 
ATOM   11601 C  CA    . ARG   B  1  365  ? -8.511  -2.014  108.906 1.00 28.05 ? 363  ARG   B CA    1 
ATOM   11602 C  C     . ARG   B  1  365  ? -7.800  -0.676  108.891 1.00 24.86 ? 363  ARG   B C     1 
ATOM   11603 O  O     . ARG   B  1  365  ? -7.108  -0.326  109.850 1.00 27.21 ? 363  ARG   B O     1 
ATOM   11604 C  CB    . ARG   B  1  365  ? -9.529  -2.075  110.037 1.00 28.34 ? 363  ARG   B CB    1 
ATOM   11605 C  CG    . ARG   B  1  365  ? -10.769 -1.235  109.774 1.00 29.95 ? 363  ARG   B CG    1 
ATOM   11606 C  CD    . ARG   B  1  365  ? -11.874 -1.600  110.753 1.00 31.36 ? 363  ARG   B CD    1 
ATOM   11607 N  NE    . ARG   B  1  365  ? -13.151 -0.974  110.427 1.00 35.68 ? 363  ARG   B NE    1 
ATOM   11608 C  CZ    . ARG   B  1  365  ? -13.840 -0.203  111.260 1.00 33.26 ? 363  ARG   B CZ    1 
ATOM   11609 N  NH1   . ARG   B  1  365  ? -13.409 0.046   112.486 1.00 32.70 ? 363  ARG   B NH1   1 
ATOM   11610 N  NH2   . ARG   B  1  365  ? -14.989 0.330   110.853 1.00 29.21 ? 363  ARG   B NH2   1 
ATOM   11611 N  N     . ILE   B  1  366  ? -7.901  0.035   107.790 1.00 25.35 ? 364  ILE   B N     1 
ATOM   11612 C  CA    . ILE   B  1  366  ? -7.252  1.329   107.657 1.00 24.78 ? 364  ILE   B CA    1 
ATOM   11613 C  C     . ILE   B  1  366  ? -8.266  2.394   108.037 1.00 26.38 ? 364  ILE   B C     1 
ATOM   11614 O  O     . ILE   B  1  366  ? -9.428  2.335   107.613 1.00 25.94 ? 364  ILE   B O     1 
ATOM   11615 C  CB    . ILE   B  1  366  ? -6.740  1.525   106.220 1.00 23.92 ? 364  ILE   B CB    1 
ATOM   11616 C  CG1   . ILE   B  1  366  ? -5.682  0.469   105.882 1.00 27.25 ? 364  ILE   B CG1   1 
ATOM   11617 C  CG2   . ILE   B  1  366  ? -6.232  2.950   106.010 1.00 23.53 ? 364  ILE   B CG2   1 
ATOM   11618 C  CD1   . ILE   B  1  366  ? -5.257  0.446   104.419 1.00 26.07 ? 364  ILE   B CD1   1 
ATOM   11619 N  N     . MET   B  1  367  ? -7.847  3.344   108.871 1.00 24.68 ? 365  MET   B N     1 
ATOM   11620 C  CA    . MET   B  1  367  ? -8.706  4.466   109.218 1.00 25.65 ? 365  MET   B CA    1 
ATOM   11621 C  C     . MET   B  1  367  ? -8.593  5.483   108.099 1.00 23.93 ? 365  MET   B C     1 
ATOM   11622 O  O     . MET   B  1  367  ? -7.487  5.899   107.747 1.00 26.27 ? 365  MET   B O     1 
ATOM   11623 C  CB    . MET   B  1  367  ? -8.278  5.071   110.553 1.00 24.22 ? 365  MET   B CB    1 
ATOM   11624 C  CG    . MET   B  1  367  ? -8.123  4.049   111.647 1.00 26.37 ? 365  MET   B CG    1 
ATOM   11625 S  SD    . MET   B  1  367  ? -7.585  4.775   113.211 1.00 26.23 ? 365  MET   B SD    1 
ATOM   11626 C  CE    . MET   B  1  367  ? -9.102  5.037   114.120 1.00 31.47 ? 365  MET   B CE    1 
ATOM   11627 N  N     . VAL   B  1  368  ? -9.720  5.854   107.503 1.00 22.30 ? 366  VAL   B N     1 
ATOM   11628 C  CA    . VAL   B  1  368  ? -9.699  6.732   106.345 1.00 21.98 ? 366  VAL   B CA    1 
ATOM   11629 C  C     . VAL   B  1  368  ? -10.422 8.015   106.706 1.00 24.79 ? 366  VAL   B C     1 
ATOM   11630 O  O     . VAL   B  1  368  ? -11.644 8.015   106.906 1.00 23.98 ? 366  VAL   B O     1 
ATOM   11631 C  CB    . VAL   B  1  368  ? -10.317 6.077   105.107 1.00 24.46 ? 366  VAL   B CB    1 
ATOM   11632 C  CG1   . VAL   B  1  368  ? -10.210 7.021   103.946 1.00 23.54 ? 366  VAL   B CG1   1 
ATOM   11633 C  CG2   . VAL   B  1  368  ? -9.608  4.775   104.800 1.00 25.31 ? 366  VAL   B CG2   1 
ATOM   11634 N  N     . ARG   B  1  369  ? -9.676  9.107   106.796 1.00 21.86 ? 367  ARG   B N     1 
ATOM   11635 C  CA    . ARG   B  1  369  ? -10.270 10.405  107.053 1.00 21.78 ? 367  ARG   B CA    1 
ATOM   11636 C  C     . ARG   B  1  369  ? -10.645 11.002  105.712 1.00 22.15 ? 367  ARG   B C     1 
ATOM   11637 O  O     . ARG   B  1  369  ? -9.773  11.312  104.894 1.00 21.93 ? 367  ARG   B O     1 
ATOM   11638 C  CB    . ARG   B  1  369  ? -9.327  11.339  107.809 1.00 21.20 ? 367  ARG   B CB    1 
ATOM   11639 C  CG    . ARG   B  1  369  ? -10.005 12.674  108.121 1.00 25.29 ? 367  ARG   B CG    1 
ATOM   11640 C  CD    . ARG   B  1  369  ? -9.011  13.733  108.516 1.00 21.85 ? 367  ARG   B CD    1 
ATOM   11641 N  NE    . ARG   B  1  369  ? -8.308  13.371  109.735 1.00 21.60 ? 367  ARG   B NE    1 
ATOM   11642 C  CZ    . ARG   B  1  369  ? -7.083  13.773  110.039 1.00 21.50 ? 367  ARG   B CZ    1 
ATOM   11643 N  NH1   . ARG   B  1  369  ? -6.385  14.546  109.220 1.00 21.96 ? 367  ARG   B NH1   1 
ATOM   11644 N  NH2   . ARG   B  1  369  ? -6.546  13.379  111.192 1.00 22.83 ? 367  ARG   B NH2   1 
ATOM   11645 N  N     . LEU   B  1  370  ? -11.937 11.155  105.483 1.00 22.00 ? 368  LEU   B N     1 
ATOM   11646 C  CA    . LEU   B  1  370  ? -12.418 11.840  104.301 1.00 21.50 ? 368  LEU   B CA    1 
ATOM   11647 C  C     . LEU   B  1  370  ? -12.543 13.320  104.631 1.00 20.58 ? 368  LEU   B C     1 
ATOM   11648 O  O     . LEU   B  1  370  ? -13.266 13.697  105.563 1.00 22.34 ? 368  LEU   B O     1 
ATOM   11649 C  CB    . LEU   B  1  370  ? -13.761 11.259  103.872 1.00 22.00 ? 368  LEU   B CB    1 
ATOM   11650 C  CG    . LEU   B  1  370  ? -14.301 11.803  102.552 1.00 23.43 ? 368  LEU   B CG    1 
ATOM   11651 C  CD1   . LEU   B  1  370  ? -13.420 11.422  101.372 1.00 23.99 ? 368  LEU   B CD1   1 
ATOM   11652 C  CD2   . LEU   B  1  370  ? -15.715 11.301  102.329 1.00 24.57 ? 368  LEU   B CD2   1 
ATOM   11653 N  N     . VAL   B  1  371  ? -11.814 14.145  103.894 1.00 20.02 ? 369  VAL   B N     1 
ATOM   11654 C  CA    . VAL   B  1  371  ? -11.869 15.588  104.029 1.00 20.47 ? 369  VAL   B CA    1 
ATOM   11655 C  C     . VAL   B  1  371  ? -12.246 16.140  102.677 1.00 20.83 ? 369  VAL   B C     1 
ATOM   11656 O  O     . VAL   B  1  371  ? -12.217 15.436  101.671 1.00 21.15 ? 369  VAL   B O     1 
ATOM   11657 C  CB    . VAL   B  1  371  ? -10.527 16.186  104.483 1.00 18.24 ? 369  VAL   B CB    1 
ATOM   11658 C  CG1   . VAL   B  1  371  ? -10.048 15.510  105.746 1.00 21.21 ? 369  VAL   B CG1   1 
ATOM   11659 C  CG2   . VAL   B  1  371  ? -9.488  16.066  103.373 1.00 20.95 ? 369  VAL   B CG2   1 
ATOM   11660 N  N     . LYS   B  1  372  ? -12.567 17.426  102.649 1.00 20.85 ? 370  LYS   B N     1 
ATOM   11661 C  CA    . LYS   B  1  372  ? -12.679 18.078  101.353 1.00 22.24 ? 370  LYS   B CA    1 
ATOM   11662 C  C     . LYS   B  1  372  ? -11.293 18.425  100.817 1.00 19.47 ? 370  LYS   B C     1 
ATOM   11663 O  O     . LYS   B  1  372  ? -10.839 17.836  99.831  1.00 20.38 ? 370  LYS   B O     1 
ATOM   11664 C  CB    . LYS   B  1  372  ? -13.684 19.236  101.412 1.00 22.56 ? 370  LYS   B CB    1 
ATOM   11665 C  CG    . LYS   B  1  372  ? -15.085 18.672  101.630 1.00 24.04 ? 370  LYS   B CG    1 
ATOM   11666 C  CD    . LYS   B  1  372  ? -16.176 19.701  101.778 1.00 24.05 ? 370  LYS   B CD    1 
ATOM   11667 C  CE    . LYS   B  1  372  ? -17.456 19.012  102.239 1.00 27.95 ? 370  LYS   B CE    1 
ATOM   11668 N  NZ    . LYS   B  1  372  ? -18.531 20.007  102.509 1.00 27.86 ? 370  LYS   B NZ    1 
ATOM   11669 N  N     . GLY   B  1  373  ? -10.587 19.319  101.480 1.00 19.49 ? 371  GLY   B N     1 
ATOM   11670 C  CA    . GLY   B  1  373  ? -9.190  19.551  101.141 1.00 17.84 ? 371  GLY   B CA    1 
ATOM   11671 C  C     . GLY   B  1  373  ? -8.779  20.972  101.464 1.00 19.42 ? 371  GLY   B C     1 
ATOM   11672 O  O     . GLY   B  1  373  ? -9.535  21.927  101.322 1.00 22.15 ? 371  GLY   B O     1 
ATOM   11673 N  N     . ALA   B  1  374  ? -7.517  21.128  101.873 1.00 18.09 ? 372  ALA   B N     1 
ATOM   11674 C  CA    . ALA   B  1  374  ? -7.049  22.371  102.470 1.00 19.86 ? 372  ALA   B CA    1 
ATOM   11675 C  C     . ALA   B  1  374  ? -6.208  23.226  101.536 1.00 18.19 ? 372  ALA   B C     1 
ATOM   11676 O  O     . ALA   B  1  374  ? -5.800  24.320  101.932 1.00 21.15 ? 372  ALA   B O     1 
ATOM   11677 C  CB    . ALA   B  1  374  ? -6.239  22.070  103.732 1.00 19.78 ? 372  ALA   B CB    1 
ATOM   11678 N  N     . TYR   B  1  375  ? -5.934  22.771  100.318 1.00 17.91 ? 373  TYR   B N     1 
ATOM   11679 C  CA    . TYR   B  1  375  ? -4.997  23.467  99.444  1.00 17.28 ? 373  TYR   B CA    1 
ATOM   11680 C  C     . TYR   B  1  375  ? -5.648  23.991  98.172  1.00 18.81 ? 373  TYR   B C     1 
ATOM   11681 O  O     . TYR   B  1  375  ? -4.974  24.160  97.165  1.00 17.39 ? 373  TYR   B O     1 
ATOM   11682 C  CB    . TYR   B  1  375  ? -3.820  22.576  99.059  1.00 18.80 ? 373  TYR   B CB    1 
ATOM   11683 C  CG    . TYR   B  1  375  ? -3.073  21.990  100.224 1.00 19.34 ? 373  TYR   B CG    1 
ATOM   11684 C  CD1   . TYR   B  1  375  ? -3.582  20.912  100.926 1.00 19.06 ? 373  TYR   B CD1   1 
ATOM   11685 C  CD2   . TYR   B  1  375  ? -1.830  22.491  100.598 1.00 20.95 ? 373  TYR   B CD2   1 
ATOM   11686 C  CE1   . TYR   B  1  375  ? -2.893  20.374  101.996 1.00 20.36 ? 373  TYR   B CE1   1 
ATOM   11687 C  CE2   . TYR   B  1  375  ? -1.132  21.949  101.653 1.00 23.93 ? 373  TYR   B CE2   1 
ATOM   11688 C  CZ    . TYR   B  1  375  ? -1.667  20.893  102.344 1.00 21.14 ? 373  TYR   B CZ    1 
ATOM   11689 O  OH    . TYR   B  1  375  ? -0.983  20.333  103.386 1.00 23.37 ? 373  TYR   B OH    1 
ATOM   11690 N  N     . TRP   B  1  376  ? -6.949  24.270  98.205  1.00 17.19 ? 374  TRP   B N     1 
ATOM   11691 C  CA    . TRP   B  1  376  ? -7.669  24.504  96.961  1.00 17.46 ? 374  TRP   B CA    1 
ATOM   11692 C  C     . TRP   B  1  376  ? -7.069  25.651  96.157  1.00 16.85 ? 374  TRP   B C     1 
ATOM   11693 O  O     . TRP   B  1  376  ? -6.739  25.479  94.980  1.00 17.37 ? 374  TRP   B O     1 
ATOM   11694 C  CB    . TRP   B  1  376  ? -9.146  24.742  97.223  1.00 16.80 ? 374  TRP   B CB    1 
ATOM   11695 C  CG    . TRP   B  1  376  ? -9.882  24.907  95.940  1.00 18.37 ? 374  TRP   B CG    1 
ATOM   11696 C  CD1   . TRP   B  1  376  ? -10.271 23.919  95.089  1.00 18.54 ? 374  TRP   B CD1   1 
ATOM   11697 C  CD2   . TRP   B  1  376  ? -10.302 26.138  95.354  1.00 20.02 ? 374  TRP   B CD2   1 
ATOM   11698 N  NE1   . TRP   B  1  376  ? -10.924 24.461  94.005  1.00 17.95 ? 374  TRP   B NE1   1 
ATOM   11699 C  CE2   . TRP   B  1  376  ? -10.946 25.825  94.141  1.00 19.78 ? 374  TRP   B CE2   1 
ATOM   11700 C  CE3   . TRP   B  1  376  ? -10.203 27.480  95.744  1.00 22.04 ? 374  TRP   B CE3   1 
ATOM   11701 C  CZ2   . TRP   B  1  376  ? -11.473 26.801  93.304  1.00 19.42 ? 374  TRP   B CZ2   1 
ATOM   11702 C  CZ3   . TRP   B  1  376  ? -10.738 28.448  94.925  1.00 23.18 ? 374  TRP   B CZ3   1 
ATOM   11703 C  CH2   . TRP   B  1  376  ? -11.372 28.106  93.716  1.00 21.75 ? 374  TRP   B CH2   1 
ATOM   11704 N  N     . ASP   B  1  377  ? -6.948  26.839  96.760  1.00 18.02 ? 375  ASP   B N     1 
ATOM   11705 C  CA    . ASP   B  1  377  ? -6.445  27.990  96.012  1.00 20.37 ? 375  ASP   B CA    1 
ATOM   11706 C  C     . ASP   B  1  377  ? -5.083  27.688  95.421  1.00 17.47 ? 375  ASP   B C     1 
ATOM   11707 O  O     . ASP   B  1  377  ? -4.779  28.089  94.293  1.00 18.31 ? 375  ASP   B O     1 
ATOM   11708 C  CB    . ASP   B  1  377  ? -6.290  29.209  96.924  1.00 24.01 ? 375  ASP   B CB    1 
ATOM   11709 C  CG    . ASP   B  1  377  ? -7.588  29.718  97.462  1.00 35.98 ? 375  ASP   B CG    1 
ATOM   11710 O  OD1   . ASP   B  1  377  ? -8.543  29.827  96.681  1.00 44.01 ? 375  ASP   B OD1   1 
ATOM   11711 O  OD2   . ASP   B  1  377  ? -7.642  30.031  98.668  1.00 50.00 ? 375  ASP   B OD2   1 
ATOM   11712 N  N     . ALA   B  1  378  ? -4.231  27.016  96.195  1.00 16.94 ? 376  ALA   B N     1 
ATOM   11713 C  CA    . ALA   B  1  378  ? -2.880  26.743  95.737  1.00 16.58 ? 376  ALA   B CA    1 
ATOM   11714 C  C     . ALA   B  1  378  ? -2.875  25.749  94.588  1.00 17.76 ? 376  ALA   B C     1 
ATOM   11715 O  O     . ALA   B  1  378  ? -2.019  25.838  93.702  1.00 17.17 ? 376  ALA   B O     1 
ATOM   11716 C  CB    . ALA   B  1  378  ? -2.031  26.226  96.898  1.00 19.69 ? 376  ALA   B CB    1 
ATOM   11717 N  N     . GLU   B  1  379  ? -3.811  24.803  94.589  1.00 16.63 ? 377  GLU   B N     1 
ATOM   11718 C  CA    . GLU   B  1  379  ? -3.861  23.837  93.501  1.00 15.77 ? 377  GLU   B CA    1 
ATOM   11719 C  C     . GLU   B  1  379  ? -4.308  24.503  92.214  1.00 18.24 ? 377  GLU   B C     1 
ATOM   11720 O  O     . GLU   B  1  379  ? -3.819  24.161  91.132  1.00 17.16 ? 377  GLU   B O     1 
ATOM   11721 C  CB    . GLU   B  1  379  ? -4.792  22.668  93.848  1.00 16.79 ? 377  GLU   B CB    1 
ATOM   11722 C  CG    . GLU   B  1  379  ? -4.383  21.824  95.062  1.00 18.40 ? 377  GLU   B CG    1 
ATOM   11723 C  CD    . GLU   B  1  379  ? -3.079  21.053  94.919  1.00 19.16 ? 377  GLU   B CD    1 
ATOM   11724 O  OE1   . GLU   B  1  379  ? -2.450  21.052  93.832  1.00 20.89 ? 377  GLU   B OE1   1 
ATOM   11725 O  OE2   . GLU   B  1  379  ? -2.692  20.425  95.931  1.00 19.16 ? 377  GLU   B OE2   1 
ATOM   11726 N  N     . ILE   B  1  380  ? -5.240  25.457  92.303  1.00 17.22 ? 378  ILE   B N     1 
ATOM   11727 C  CA    . ILE   B  1  380  ? -5.648  26.192  91.105  1.00 16.12 ? 378  ILE   B CA    1 
ATOM   11728 C  C     . ILE   B  1  380  ? -4.460  26.946  90.533  1.00 16.62 ? 378  ILE   B C     1 
ATOM   11729 O  O     . ILE   B  1  380  ? -4.156  26.859  89.336  1.00 16.13 ? 378  ILE   B O     1 
ATOM   11730 C  CB    . ILE   B  1  380  ? -6.811  27.147  91.415  1.00 17.14 ? 378  ILE   B CB    1 
ATOM   11731 C  CG1   . ILE   B  1  380  ? -7.990  26.378  92.000  1.00 17.00 ? 378  ILE   B CG1   1 
ATOM   11732 C  CG2   . ILE   B  1  380  ? -7.210  27.914  90.165  1.00 17.99 ? 378  ILE   B CG2   1 
ATOM   11733 C  CD1   . ILE   B  1  380  ? -8.542  25.316  91.070  1.00 19.30 ? 378  ILE   B CD1   1 
ATOM   11734 N  N     . LYS   B  1  381  ? -3.770  27.699  91.390  1.00 15.89 ? 379  LYS   B N     1 
ATOM   11735 C  CA    . LYS   B  1  381  ? -2.634  28.481  90.931  1.00 16.15 ? 379  LYS   B CA    1 
ATOM   11736 C  C     . LYS   B  1  381  ? -1.561  27.587  90.331  1.00 16.22 ? 379  LYS   B C     1 
ATOM   11737 O  O     . LYS   B  1  381  ? -1.046  27.875  89.247  1.00 16.16 ? 379  LYS   B O     1 
ATOM   11738 C  CB    . LYS   B  1  381  ? -2.060  29.312  92.071  1.00 16.86 ? 379  LYS   B CB    1 
ATOM   11739 C  CG    . LYS   B  1  381  ? -0.801  30.049  91.681  1.00 17.23 ? 379  LYS   B CG    1 
ATOM   11740 C  CD    . LYS   B  1  381  ? -0.371  30.974  92.806  1.00 15.63 ? 379  LYS   B CD    1 
ATOM   11741 C  CE    . LYS   B  1  381  ? 0.758   31.881  92.366  1.00 18.61 ? 379  LYS   B CE    1 
ATOM   11742 N  NZ    . LYS   B  1  381  ? 1.200   32.754  93.491  1.00 16.33 ? 379  LYS   B NZ    1 
ATOM   11743 N  N     . ARG   B  1  382  ? -1.269  26.464  90.990  1.00 16.23 ? 380  ARG   B N     1 
ATOM   11744 C  CA    . ARG   B  1  382  ? -0.156  25.628  90.551  1.00 16.00 ? 380  ARG   B CA    1 
ATOM   11745 C  C     . ARG   B  1  382  ? -0.441  25.039  89.183  1.00 15.78 ? 380  ARG   B C     1 
ATOM   11746 O  O     . ARG   B  1  382  ? 0.430   25.023  88.311  1.00 16.07 ? 380  ARG   B O     1 
ATOM   11747 C  CB    . ARG   B  1  382  ? 0.055   24.504  91.564  1.00 18.83 ? 380  ARG   B CB    1 
ATOM   11748 C  CG    . ARG   B  1  382  ? 1.251   23.633  91.273  1.00 23.64 ? 380  ARG   B CG    1 
ATOM   11749 C  CD    . ARG   B  1  382  ? 2.518   24.355  91.684  1.00 32.43 ? 380  ARG   B CD    1 
ATOM   11750 N  NE    . ARG   B  1  382  ? 3.309   24.775  90.539  1.00 35.18 ? 380  ARG   B NE    1 
ATOM   11751 C  CZ    . ARG   B  1  382  ? 4.247   25.716  90.572  1.00 35.74 ? 380  ARG   B CZ    1 
ATOM   11752 N  NH1   . ARG   B  1  382  ? 4.503   26.405  91.677  1.00 34.42 ? 380  ARG   B NH1   1 
ATOM   11753 N  NH2   . ARG   B  1  382  ? 4.947   25.974  89.468  1.00 33.91 ? 380  ARG   B NH2   1 
ATOM   11754 N  N     . ALA   B  1  383  ? -1.662  24.581  88.958  1.00 15.23 ? 381  ALA   B N     1 
ATOM   11755 C  CA    . ALA   B  1  383  ? -1.971  23.976  87.670  1.00 15.15 ? 381  ALA   B CA    1 
ATOM   11756 C  C     . ALA   B  1  383  ? -1.931  25.021  86.567  1.00 16.39 ? 381  ALA   B C     1 
ATOM   11757 O  O     . ALA   B  1  383  ? -1.480  24.739  85.447  1.00 16.92 ? 381  ALA   B O     1 
ATOM   11758 C  CB    . ALA   B  1  383  ? -3.346  23.323  87.744  1.00 16.95 ? 381  ALA   B CB    1 
ATOM   11759 N  N     . GLN   B  1  384  ? -2.367  26.241  86.876  1.00 14.87 ? 382  GLN   B N     1 
ATOM   11760 C  CA    . GLN   B  1  384  ? -2.271  27.324  85.905  1.00 16.33 ? 382  GLN   B CA    1 
ATOM   11761 C  C     . GLN   B  1  384  ? -0.825  27.670  85.607  1.00 15.22 ? 382  GLN   B C     1 
ATOM   11762 O  O     . GLN   B  1  384  ? -0.446  27.808  84.439  1.00 16.17 ? 382  GLN   B O     1 
ATOM   11763 C  CB    . GLN   B  1  384  ? -3.037  28.549  86.397  1.00 16.78 ? 382  GLN   B CB    1 
ATOM   11764 C  CG    . GLN   B  1  384  ? -4.535  28.363  86.313  1.00 16.08 ? 382  GLN   B CG    1 
ATOM   11765 C  CD    . GLN   B  1  384  ? -5.264  29.585  86.736  1.00 17.54 ? 382  GLN   B CD    1 
ATOM   11766 O  OE1   . GLN   B  1  384  ? -4.700  30.452  87.390  1.00 18.95 ? 382  GLN   B OE1   1 
ATOM   11767 N  NE2   . GLN   B  1  384  ? -6.540  29.663  86.392  1.00 17.25 ? 382  GLN   B NE2   1 
ATOM   11768 N  N     . LEU   B  1  385  ? -0.012  27.837  86.652  1.00 16.14 ? 383  LEU   B N     1 
ATOM   11769 C  CA    . LEU   B  1  385  ? 1.399   28.134  86.450  1.00 15.86 ? 383  LEU   B CA    1 
ATOM   11770 C  C     . LEU   B  1  385  ? 2.066   27.082  85.592  1.00 15.42 ? 383  LEU   B C     1 
ATOM   11771 O  O     . LEU   B  1  385  ? 2.908   27.408  84.744  1.00 15.80 ? 383  LEU   B O     1 
ATOM   11772 C  CB    . LEU   B  1  385  ? 2.120   28.227  87.792  1.00 17.76 ? 383  LEU   B CB    1 
ATOM   11773 C  CG    . LEU   B  1  385  ? 1.819   29.421  88.686  1.00 19.95 ? 383  LEU   B CG    1 
ATOM   11774 C  CD1   . LEU   B  1  385  ? 2.602   29.268  89.965  1.00 20.79 ? 383  LEU   B CD1   1 
ATOM   11775 C  CD2   . LEU   B  1  385  ? 2.217   30.694  87.971  1.00 21.05 ? 383  LEU   B CD2   1 
ATOM   11776 N  N     . ASP   B  1  386  ? 1.744   25.816  85.820  1.00 17.21 ? 384  ASP   B N     1 
ATOM   11777 C  CA    . ASP   B  1  386  ? 2.441   24.727  85.156  1.00 16.88 ? 384  ASP   B CA    1 
ATOM   11778 C  C     . ASP   B  1  386  ? 1.849   24.386  83.804  1.00 17.74 ? 384  ASP   B C     1 
ATOM   11779 O  O     . ASP   B  1  386  ? 2.381   23.511  83.113  1.00 17.34 ? 384  ASP   B O     1 
ATOM   11780 C  CB    . ASP   B  1  386  ? 2.501   23.495  86.061  1.00 18.26 ? 384  ASP   B CB    1 
ATOM   11781 C  CG    . ASP   B  1  386  ? 3.391   23.707  87.280  1.00 22.22 ? 384  ASP   B CG    1 
ATOM   11782 O  OD1   . ASP   B  1  386  ? 4.116   24.726  87.341  1.00 23.75 ? 384  ASP   B OD1   1 
ATOM   11783 O  OD2   . ASP   B  1  386  ? 3.357   22.850  88.188  1.00 23.62 ? 384  ASP   B OD2   1 
ATOM   11784 N  N     . GLY   B  1  387  ? 0.766   25.049  83.412  1.00 15.90 ? 385  GLY   B N     1 
ATOM   11785 C  CA    . GLY   B  1  387  ? 0.175   24.815  82.108  1.00 17.81 ? 385  GLY   B CA    1 
ATOM   11786 C  C     . GLY   B  1  387  ? -0.304  23.396  81.925  1.00 18.85 ? 385  GLY   B C     1 
ATOM   11787 O  O     . GLY   B  1  387  ? -0.178  22.831  80.831  1.00 18.82 ? 385  GLY   B O     1 
ATOM   11788 N  N     . LEU   B  1  388  ? -0.872  22.805  82.969  1.00 17.82 ? 386  LEU   B N     1 
ATOM   11789 C  CA    . LEU   B  1  388  ? -1.241  21.406  82.879  1.00 17.45 ? 386  LEU   B CA    1 
ATOM   11790 C  C     . LEU   B  1  388  ? -2.643  21.255  82.302  1.00 16.60 ? 386  LEU   B C     1 
ATOM   11791 O  O     . LEU   B  1  388  ? -3.385  22.223  82.125  1.00 18.23 ? 386  LEU   B O     1 
ATOM   11792 C  CB    . LEU   B  1  388  ? -1.069  20.720  84.229  1.00 17.68 ? 386  LEU   B CB    1 
ATOM   11793 C  CG    . LEU   B  1  388  ? 0.388   20.788  84.669  1.00 17.83 ? 386  LEU   B CG    1 
ATOM   11794 C  CD1   . LEU   B  1  388  ? 0.603   20.124  86.029  1.00 20.85 ? 386  LEU   B CD1   1 
ATOM   11795 C  CD2   . LEU   B  1  388  ? 1.337   20.204  83.607  1.00 20.54 ? 386  LEU   B CD2   1 
ATOM   11796 N  N     . ALA   B  1  389  ? -3.001  20.008  81.995  1.00 17.86 ? 387  ALA   B N     1 
ATOM   11797 C  CA    . ALA   B  1  389  ? -4.183  19.776  81.172  1.00 17.27 ? 387  ALA   B CA    1 
ATOM   11798 C  C     . ALA   B  1  389  ? -5.454  20.233  81.873  1.00 19.16 ? 387  ALA   B C     1 
ATOM   11799 O  O     . ALA   B  1  389  ? -6.387  20.730  81.234  1.00 21.91 ? 387  ALA   B O     1 
ATOM   11800 C  CB    . ALA   B  1  389  ? -4.286  18.298  80.797  1.00 21.52 ? 387  ALA   B CB    1 
ATOM   11801 N  N     . ASP   B  1  390  ? -5.512  20.066  83.184  1.00 18.41 ? 388  ASP   B N     1 
ATOM   11802 C  CA    . ASP   B  1  390  ? -6.685  20.437  83.959  1.00 18.67 ? 388  ASP   B CA    1 
ATOM   11803 C  C     . ASP   B  1  390  ? -6.225  20.544  85.400  1.00 16.68 ? 388  ASP   B C     1 
ATOM   11804 O  O     . ASP   B  1  390  ? -5.051  20.338  85.714  1.00 17.33 ? 388  ASP   B O     1 
ATOM   11805 C  CB    . ASP   B  1  390  ? -7.811  19.405  83.777  1.00 19.12 ? 388  ASP   B CB    1 
ATOM   11806 C  CG    . ASP   B  1  390  ? -9.207  20.005  83.925  1.00 21.05 ? 388  ASP   B CG    1 
ATOM   11807 O  OD1   . ASP   B  1  390  ? -9.445  20.742  84.900  1.00 21.36 ? 388  ASP   B OD1   1 
ATOM   11808 O  OD2   . ASP   B  1  390  ? -10.063 19.735  83.056  1.00 24.98 ? 388  ASP   B OD2   1 
ATOM   11809 N  N     . PHE   B  1  391  ? -7.137  20.888  86.256  1.00 17.21 ? 389  PHE   B N     1 
ATOM   11810 C  CA    . PHE   B  1  391  ? -6.851  20.910  87.672  1.00 18.13 ? 389  PHE   B CA    1 
ATOM   11811 C  C     . PHE   B  1  391  ? -6.941  19.506  88.253  1.00 17.44 ? 389  PHE   B C     1 
ATOM   11812 O  O     . PHE   B  1  391  ? -7.659  18.652  87.729  1.00 18.84 ? 389  PHE   B O     1 
ATOM   11813 C  CB    . PHE   B  1  391  ? -7.855  21.820  88.362  1.00 18.99 ? 389  PHE   B CB    1 
ATOM   11814 C  CG    . PHE   B  1  391  ? -7.833  23.205  87.819  1.00 16.84 ? 389  PHE   B CG    1 
ATOM   11815 C  CD1   . PHE   B  1  391  ? -6.793  24.054  88.150  1.00 17.26 ? 389  PHE   B CD1   1 
ATOM   11816 C  CD2   . PHE   B  1  391  ? -8.797  23.639  86.917  1.00 17.43 ? 389  PHE   B CD2   1 
ATOM   11817 C  CE1   . PHE   B  1  391  ? -6.724  25.331  87.631  1.00 18.59 ? 389  PHE   B CE1   1 
ATOM   11818 C  CE2   . PHE   B  1  391  ? -8.736  24.923  86.398  1.00 18.32 ? 389  PHE   B CE2   1 
ATOM   11819 C  CZ    . PHE   B  1  391  ? -7.697  25.766  86.750  1.00 17.70 ? 389  PHE   B CZ    1 
ATOM   11820 N  N     . PRO   B  1  392  ? -6.228  19.250  89.348  1.00 16.67 ? 390  PRO   B N     1 
ATOM   11821 C  CA    . PRO   B  1  392  ? -6.365  17.975  90.056  1.00 14.98 ? 390  PRO   B CA    1 
ATOM   11822 C  C     . PRO   B  1  392  ? -7.427  18.027  91.139  1.00 17.86 ? 390  PRO   B C     1 
ATOM   11823 O  O     . PRO   B  1  392  ? -7.576  17.067  91.905  1.00 18.15 ? 390  PRO   B O     1 
ATOM   11824 C  CB    . PRO   B  1  392  ? -4.980  17.831  90.689  1.00 17.46 ? 390  PRO   B CB    1 
ATOM   11825 C  CG    . PRO   B  1  392  ? -4.621  19.251  91.042  1.00 17.98 ? 390  PRO   B CG    1 
ATOM   11826 C  CD    . PRO   B  1  392  ? -5.171  20.098  89.933  1.00 17.22 ? 390  PRO   B CD    1 
ATOM   11827 N  N     . VAL   B  1  393  ? -8.125  19.153  91.215  1.00 18.18 ? 391  VAL   B N     1 
ATOM   11828 C  CA    . VAL   B  1  393  ? -9.231  19.359  92.132  1.00 18.15 ? 391  VAL   B CA    1 
ATOM   11829 C  C     . VAL   B  1  393  ? -10.396 19.915  91.330  1.00 18.63 ? 391  VAL   B C     1 
ATOM   11830 O  O     . VAL   B  1  393  ? -10.233 20.394  90.202  1.00 18.84 ? 391  VAL   B O     1 
ATOM   11831 C  CB    . VAL   B  1  393  ? -8.853  20.329  93.277  1.00 18.66 ? 391  VAL   B CB    1 
ATOM   11832 C  CG1   . VAL   B  1  393  ? -7.704  19.763  94.106  1.00 18.21 ? 391  VAL   B CG1   1 
ATOM   11833 C  CG2   . VAL   B  1  393  ? -8.472  21.695  92.717  1.00 18.66 ? 391  VAL   B CG2   1 
ATOM   11834 N  N     . PHE   B  1  394  ? -11.578 19.843  91.930  1.00 19.15 ? 392  PHE   B N     1 
ATOM   11835 C  CA    . PHE   B  1  394  ? -12.753 20.469  91.352  1.00 17.69 ? 392  PHE   B CA    1 
ATOM   11836 C  C     . PHE   B  1  394  ? -12.634 21.987  91.435  1.00 18.41 ? 392  PHE   B C     1 
ATOM   11837 O  O     . PHE   B  1  394  ? -11.831 22.535  92.199  1.00 19.69 ? 392  PHE   B O     1 
ATOM   11838 C  CB    . PHE   B  1  394  ? -14.011 19.956  92.050  1.00 19.35 ? 392  PHE   B CB    1 
ATOM   11839 C  CG    . PHE   B  1  394  ? -14.161 18.477  91.934  1.00 19.60 ? 392  PHE   B CG    1 
ATOM   11840 C  CD1   . PHE   B  1  394  ? -14.415 17.908  90.698  1.00 19.60 ? 392  PHE   B CD1   1 
ATOM   11841 C  CD2   . PHE   B  1  394  ? -13.962 17.647  93.017  1.00 19.40 ? 392  PHE   B CD2   1 
ATOM   11842 C  CE1   . PHE   B  1  394  ? -14.504 16.549  90.562  1.00 20.79 ? 392  PHE   B CE1   1 
ATOM   11843 C  CE2   . PHE   B  1  394  ? -14.051 16.291  92.887  1.00 20.16 ? 392  PHE   B CE2   1 
ATOM   11844 C  CZ    . PHE   B  1  394  ? -14.329 15.735  91.653  1.00 21.56 ? 392  PHE   B CZ    1 
ATOM   11845 N  N     . THR   B  1  395  ? -13.421 22.669  90.602  1.00 19.60 ? 393  THR   B N     1 
ATOM   11846 C  CA    . THR   B  1  395  ? -13.401 24.122  90.537  1.00 19.31 ? 393  THR   B CA    1 
ATOM   11847 C  C     . THR   B  1  395  ? -14.697 24.757  91.014  1.00 18.11 ? 393  THR   B C     1 
ATOM   11848 O  O     . THR   B  1  395  ? -14.724 25.977  91.209  1.00 22.42 ? 393  THR   B O     1 
ATOM   11849 C  CB    . THR   B  1  395  ? -13.088 24.611  89.117  1.00 20.86 ? 393  THR   B CB    1 
ATOM   11850 O  OG1   . THR   B  1  395  ? -14.096 24.142  88.215  1.00 21.21 ? 393  THR   B OG1   1 
ATOM   11851 C  CG2   . THR   B  1  395  ? -11.728 24.103  88.660  1.00 19.98 ? 393  THR   B CG2   1 
ATOM   11852 N  N     . ARG   B  1  396  ? -15.750 23.974  91.197  1.00 21.95 ? 394  ARG   B N     1 
ATOM   11853 C  CA    . ARG   B  1  396  ? -16.982 24.439  91.818  1.00 22.30 ? 394  ARG   B CA    1 
ATOM   11854 C  C     . ARG   B  1  396  ? -17.106 23.765  93.169  1.00 21.28 ? 394  ARG   B C     1 
ATOM   11855 O  O     . ARG   B  1  396  ? -16.977 22.539  93.272  1.00 20.89 ? 394  ARG   B O     1 
ATOM   11856 C  CB    . ARG   B  1  396  ? -18.210 24.096  90.977  1.00 22.37 ? 394  ARG   B CB    1 
ATOM   11857 C  CG    . ARG   B  1  396  ? -18.226 24.786  89.646  1.00 23.46 ? 394  ARG   B CG    1 
ATOM   11858 C  CD    . ARG   B  1  396  ? -19.590 24.613  88.981  1.00 26.59 ? 394  ARG   B CD    1 
ATOM   11859 N  NE    . ARG   B  1  396  ? -19.537 25.090  87.606  1.00 27.88 ? 394  ARG   B NE    1 
ATOM   11860 C  CZ    . ARG   B  1  396  ? -20.364 25.980  87.078  1.00 31.08 ? 394  ARG   B CZ    1 
ATOM   11861 N  NH1   . ARG   B  1  396  ? -21.395 26.457  87.758  1.00 31.73 ? 394  ARG   B NH1   1 
ATOM   11862 N  NH2   . ARG   B  1  396  ? -20.158 26.394  85.830  1.00 29.78 ? 394  ARG   B NH2   1 
ATOM   11863 N  N     . LYS   B  1  397  ? -17.399 24.563  94.196  1.00 23.41 ? 395  LYS   B N     1 
ATOM   11864 C  CA    . LYS   B  1  397  ? -17.416 24.030  95.547  1.00 26.29 ? 395  LYS   B CA    1 
ATOM   11865 C  C     . LYS   B  1  397  ? -18.473 22.943  95.685  1.00 22.36 ? 395  LYS   B C     1 
ATOM   11866 O  O     . LYS   B  1  397  ? -18.263 21.932  96.363  1.00 23.99 ? 395  LYS   B O     1 
ATOM   11867 C  CB    . LYS   B  1  397  ? -17.636 25.177  96.531  1.00 27.13 ? 395  LYS   B CB    1 
ATOM   11868 C  CG    . LYS   B  1  397  ? -17.289 24.851  97.957  1.00 25.34 ? 395  LYS   B CG    1 
ATOM   11869 C  CD    . LYS   B  1  397  ? -18.497 24.345  98.687  1.00 26.86 ? 395  LYS   B CD    1 
ATOM   11870 C  CE    . LYS   B  1  397  ? -18.178 24.064  100.140 1.00 26.74 ? 395  LYS   B CE    1 
ATOM   11871 N  NZ    . LYS   B  1  397  ? -19.365 23.495  100.828 1.00 25.61 ? 395  LYS   B NZ    1 
ATOM   11872 N  N     . ILE   B  1  398  ? -19.605 23.112  95.003  1.00 22.94 ? 396  ILE   B N     1 
ATOM   11873 C  CA    . ILE   B  1  398  ? -20.654 22.105  95.054  1.00 26.99 ? 396  ILE   B CA    1 
ATOM   11874 C  C     . ILE   B  1  398  ? -20.166 20.765  94.510  1.00 20.92 ? 396  ILE   B C     1 
ATOM   11875 O  O     . ILE   B  1  398  ? -20.654 19.704  94.918  1.00 23.53 ? 396  ILE   B O     1 
ATOM   11876 C  CB    . ILE   B  1  398  ? -21.904 22.635  94.327  1.00 28.24 ? 396  ILE   B CB    1 
ATOM   11877 C  CG1   . ILE   B  1  398  ? -23.099 21.766  94.647  1.00 35.26 ? 396  ILE   B CG1   1 
ATOM   11878 C  CG2   . ILE   B  1  398  ? -21.662 22.720  92.824  1.00 27.67 ? 396  ILE   B CG2   1 
ATOM   11879 C  CD1   . ILE   B  1  398  ? -24.376 22.386  94.230  1.00 34.15 ? 396  ILE   B CD1   1 
ATOM   11880 N  N     . HIS   B  1  399  ? -19.180 20.784  93.604  1.00 23.33 ? 397  HIS   B N     1 
ATOM   11881 C  CA    . HIS   B  1  399  ? -18.647 19.531  93.074  1.00 24.35 ? 397  HIS   B CA    1 
ATOM   11882 C  C     . HIS   B  1  399  ? -17.860 18.781  94.133  1.00 20.49 ? 397  HIS   B C     1 
ATOM   11883 O  O     . HIS   B  1  399  ? -17.963 17.554  94.246  1.00 22.56 ? 397  HIS   B O     1 
ATOM   11884 C  CB    . HIS   B  1  399  ? -17.750 19.821  91.878  1.00 23.01 ? 397  HIS   B CB    1 
ATOM   11885 C  CG    . HIS   B  1  399  ? -18.495 20.322  90.685  1.00 23.81 ? 397  HIS   B CG    1 
ATOM   11886 N  ND1   . HIS   B  1  399  ? -17.856 20.852  89.587  1.00 23.64 ? 397  HIS   B ND1   1 
ATOM   11887 C  CD2   . HIS   B  1  399  ? -19.821 20.376  90.414  1.00 26.88 ? 397  HIS   B CD2   1 
ATOM   11888 C  CE1   . HIS   B  1  399  ? -18.756 21.205  88.685  1.00 24.68 ? 397  HIS   B CE1   1 
ATOM   11889 N  NE2   . HIS   B  1  399  ? -19.956 20.931  89.165  1.00 25.72 ? 397  HIS   B NE2   1 
ATOM   11890 N  N     . THR   B  1  400  ? -17.067 19.506  94.918  1.00 22.16 ? 398  THR   B N     1 
ATOM   11891 C  CA    . THR   B  1  400  ? -16.393 18.884  96.047  1.00 22.66 ? 398  THR   B CA    1 
ATOM   11892 C  C     . THR   B  1  400  ? -17.403 18.318  97.032  1.00 20.21 ? 398  THR   B C     1 
ATOM   11893 O  O     . THR   B  1  400  ? -17.208 17.221  97.566  1.00 23.66 ? 398  THR   B O     1 
ATOM   11894 C  CB    . THR   B  1  400  ? -15.497 19.914  96.722  1.00 20.22 ? 398  THR   B CB    1 
ATOM   11895 O  OG1   . THR   B  1  400  ? -14.421 20.226  95.837  1.00 19.04 ? 398  THR   B OG1   1 
ATOM   11896 C  CG2   . THR   B  1  400  ? -14.945 19.369  98.018  1.00 23.72 ? 398  THR   B CG2   1 
ATOM   11897 N  N     . ASP   B  1  401  ? -18.515 19.030  97.248  1.00 23.65 ? 399  ASP   B N     1 
ATOM   11898 C  CA    . ASP   B  1  401  ? -19.534 18.531  98.163  1.00 28.17 ? 399  ASP   B CA    1 
ATOM   11899 C  C     . ASP   B  1  401  ? -20.138 17.235  97.652  1.00 21.50 ? 399  ASP   B C     1 
ATOM   11900 O  O     . ASP   B  1  401  ? -20.341 16.290  98.421  1.00 25.20 ? 399  ASP   B O     1 
ATOM   11901 C  CB    . ASP   B  1  401  ? -20.623 19.584  98.377  1.00 28.04 ? 399  ASP   B CB    1 
ATOM   11902 C  CG    . ASP   B  1  401  ? -20.146 20.746  99.216  1.00 30.41 ? 399  ASP   B CG    1 
ATOM   11903 O  OD1   . ASP   B  1  401  ? -19.173 20.562  99.986  1.00 28.52 ? 399  ASP   B OD1   1 
ATOM   11904 O  OD2   . ASP   B  1  401  ? -20.739 21.839  99.113  1.00 30.55 ? 399  ASP   B OD2   1 
ATOM   11905 N  N     . VAL   B  1  402  ? -20.422 17.170  96.350  1.00 23.67 ? 400  VAL   B N     1 
ATOM   11906 C  CA    . VAL   B  1  402  ? -20.960 15.946  95.775  1.00 26.27 ? 400  VAL   B CA    1 
ATOM   11907 C  C     . VAL   B  1  402  ? -19.923 14.843  95.834  1.00 22.20 ? 400  VAL   B C     1 
ATOM   11908 O  O     . VAL   B  1  402  ? -20.237 13.688  96.141  1.00 23.58 ? 400  VAL   B O     1 
ATOM   11909 C  CB    . VAL   B  1  402  ? -21.423 16.199  94.331  1.00 25.37 ? 400  VAL   B CB    1 
ATOM   11910 C  CG1   . VAL   B  1  402  ? -21.805 14.878  93.660  1.00 28.08 ? 400  VAL   B CG1   1 
ATOM   11911 C  CG2   . VAL   B  1  402  ? -22.574 17.197  94.314  1.00 27.08 ? 400  VAL   B CG2   1 
ATOM   11912 N  N     . SER   B  1  403  ? -18.669 15.182  95.515  1.00 23.58 ? 401  SER   B N     1 
ATOM   11913 C  CA    . SER   B  1  403  ? -17.589 14.205  95.588  1.00 26.13 ? 401  SER   B CA    1 
ATOM   11914 C  C     . SER   B  1  403  ? -17.456 13.637  96.992  1.00 20.27 ? 401  SER   B C     1 
ATOM   11915 O  O     . SER   B  1  403  ? -17.304 12.423  97.169  1.00 22.73 ? 401  SER   B O     1 
ATOM   11916 C  CB    . SER   B  1  403  ? -16.276 14.856  95.168  1.00 21.68 ? 401  SER   B CB    1 
ATOM   11917 O  OG    . SER   B  1  403  ? -15.199 13.960  95.372  1.00 22.83 ? 401  SER   B OG    1 
ATOM   11918 N  N     . TYR   B  1  404  ? -17.541 14.501  98.001  1.00 23.02 ? 402  TYR   B N     1 
ATOM   11919 C  CA    . TYR   B  1  404  ? -17.459 14.051  99.385  1.00 24.78 ? 402  TYR   B CA    1 
ATOM   11920 C  C     . TYR   B  1  404  ? -18.585 13.077  99.705  1.00 22.86 ? 402  TYR   B C     1 
ATOM   11921 O  O     . TYR   B  1  404  ? -18.359 12.008  100.289 1.00 24.36 ? 402  TYR   B O     1 
ATOM   11922 C  CB    . TYR   B  1  404  ? -17.534 15.267  100.304 1.00 25.07 ? 402  TYR   B CB    1 
ATOM   11923 C  CG    . TYR   B  1  404  ? -17.180 14.969  101.741 1.00 24.98 ? 402  TYR   B CG    1 
ATOM   11924 C  CD1   . TYR   B  1  404  ? -18.102 14.389  102.603 1.00 26.27 ? 402  TYR   B CD1   1 
ATOM   11925 C  CD2   . TYR   B  1  404  ? -15.919 15.269  102.235 1.00 23.83 ? 402  TYR   B CD2   1 
ATOM   11926 C  CE1   . TYR   B  1  404  ? -17.777 14.125  103.917 1.00 28.26 ? 402  TYR   B CE1   1 
ATOM   11927 C  CE2   . TYR   B  1  404  ? -15.586 15.003  103.554 1.00 23.22 ? 402  TYR   B CE2   1 
ATOM   11928 C  CZ    . TYR   B  1  404  ? -16.520 14.426  104.382 1.00 25.55 ? 402  TYR   B CZ    1 
ATOM   11929 O  OH    . TYR   B  1  404  ? -16.203 14.158  105.692 1.00 26.96 ? 402  TYR   B OH    1 
ATOM   11930 N  N     . ILE   B  1  405  ? -19.814 13.431  99.326  1.00 26.24 ? 403  ILE   B N     1 
ATOM   11931 C  CA    . ILE   B  1  405  ? -20.958 12.577  99.622  1.00 30.06 ? 403  ILE   B CA    1 
ATOM   11932 C  C     . ILE   B  1  405  ? -20.856 11.259  98.864  1.00 23.77 ? 403  ILE   B C     1 
ATOM   11933 O  O     . ILE   B  1  405  ? -21.144 10.190  99.410  1.00 27.93 ? 403  ILE   B O     1 
ATOM   11934 C  CB    . ILE   B  1  405  ? -22.269 13.336  99.353  1.00 31.28 ? 403  ILE   B CB    1 
ATOM   11935 C  CG1   . ILE   B  1  405  ? -22.406 14.504  100.337 1.00 31.93 ? 403  ILE   B CG1   1 
ATOM   11936 C  CG2   . ILE   B  1  405  ? -23.459 12.408  99.463  1.00 27.40 ? 403  ILE   B CG2   1 
ATOM   11937 C  CD1   . ILE   B  1  405  ? -23.502 15.485  99.986  1.00 36.40 ? 403  ILE   B CD1   1 
ATOM   11938 N  N     . ALA   B  1  406  ? -20.397 11.310  97.607  1.00 25.28 ? 404  ALA   B N     1 
ATOM   11939 C  CA    . ALA   B  1  406  ? -20.209 10.082  96.836  1.00 27.25 ? 404  ALA   B CA    1 
ATOM   11940 C  C     . ALA   B  1  406  ? -19.144 9.194   97.465  1.00 26.17 ? 404  ALA   B C     1 
ATOM   11941 O  O     . ALA   B  1  406  ? -19.296 7.968   97.527  1.00 27.87 ? 404  ALA   B O     1 
ATOM   11942 C  CB    . ALA   B  1  406  ? -19.822 10.429  95.396  1.00 27.40 ? 404  ALA   B CB    1 
ATOM   11943 N  N     . CYS   B  1  407  ? -18.046 9.797   97.926  1.00 25.90 ? 405  CYS   B N     1 
ATOM   11944 C  CA    . CYS   B  1  407  ? -16.978 9.031   98.554  1.00 25.95 ? 405  CYS   B CA    1 
ATOM   11945 C  C     . CYS   B  1  407  ? -17.389 8.525   99.931  1.00 23.16 ? 405  CYS   B C     1 
ATOM   11946 O  O     . CYS   B  1  407  ? -17.000 7.420   100.324 1.00 28.39 ? 405  CYS   B O     1 
ATOM   11947 C  CB    . CYS   B  1  407  ? -15.711 9.879   98.618  1.00 22.26 ? 405  CYS   B CB    1 
ATOM   11948 S  SG    . CYS   B  1  407  ? -14.966 10.143  96.978  1.00 28.98 ? 405  CYS   B SG    1 
ATOM   11949 N  N     . ALA   B  1  408  ? -18.187 9.311   100.662 1.00 26.29 ? 406  ALA   B N     1 
ATOM   11950 C  CA    . ALA   B  1  408  ? -18.785 8.827   101.902 1.00 28.83 ? 406  ALA   B CA    1 
ATOM   11951 C  C     . ALA   B  1  408  ? -19.645 7.597   101.653 1.00 27.01 ? 406  ALA   B C     1 
ATOM   11952 O  O     . ALA   B  1  408  ? -19.610 6.639   102.429 1.00 31.58 ? 406  ALA   B O     1 
ATOM   11953 C  CB    . ALA   B  1  408  ? -19.625 9.932   102.530 1.00 32.41 ? 406  ALA   B CB    1 
ATOM   11954 N  N     . ALA   B  1  409  ? -20.403 7.595   100.553 1.00 28.53 ? 407  ALA   B N     1 
ATOM   11955 C  CA    . ALA   B  1  409  ? -21.206 6.422   100.228 1.00 31.59 ? 407  ALA   B CA    1 
ATOM   11956 C  C     . ALA   B  1  409  ? -20.326 5.203   100.006 1.00 27.92 ? 407  ALA   B C     1 
ATOM   11957 O  O     . ALA   B  1  409  ? -20.639 4.106   100.479 1.00 31.08 ? 407  ALA   B O     1 
ATOM   11958 C  CB    . ALA   B  1  409  ? -22.075 6.698   99.002  1.00 29.44 ? 407  ALA   B CB    1 
ATOM   11959 N  N     . LYS   B  1  410  ? -19.205 5.384   99.305  1.00 30.19 ? 408  LYS   B N     1 
ATOM   11960 C  CA    . LYS   B  1  410  ? -18.270 4.285   99.105  1.00 27.26 ? 408  LYS   B CA    1 
ATOM   11961 C  C     . LYS   B  1  410  ? -17.677 3.827   100.428 1.00 31.24 ? 408  LYS   B C     1 
ATOM   11962 O  O     . LYS   B  1  410  ? -17.559 2.623   100.681 1.00 32.75 ? 408  LYS   B O     1 
ATOM   11963 C  CB    . LYS   B  1  410  ? -17.159 4.720   98.148  1.00 28.03 ? 408  LYS   B CB    1 
ATOM   11964 C  CG    . LYS   B  1  410  ? -16.131 3.634   97.862  1.00 29.17 ? 408  LYS   B CG    1 
ATOM   11965 C  CD    . LYS   B  1  410  ? -14.968 4.161   97.038  1.00 31.21 ? 408  LYS   B CD    1 
ATOM   11966 C  CE    . LYS   B  1  410  ? -15.399 4.602   95.641  1.00 31.82 ? 408  LYS   B CE    1 
ATOM   11967 N  NZ    . LYS   B  1  410  ? -15.627 3.451   94.710  1.00 34.02 ? 408  LYS   B NZ    1 
ATOM   11968 N  N     . LEU   B  1  411  ? -17.287 4.775   101.283 1.00 30.38 ? 409  LEU   B N     1 
ATOM   11969 C  CA    . LEU   B  1  411  ? -16.730 4.401   102.576 1.00 31.41 ? 409  LEU   B CA    1 
ATOM   11970 C  C     . LEU   B  1  411  ? -17.766 3.711   103.450 1.00 29.71 ? 409  LEU   B C     1 
ATOM   11971 O  O     . LEU   B  1  411  ? -17.452 2.719   104.114 1.00 30.99 ? 409  LEU   B O     1 
ATOM   11972 C  CB    . LEU   B  1  411  ? -16.161 5.625   103.285 1.00 27.42 ? 409  LEU   B CB    1 
ATOM   11973 C  CG    . LEU   B  1  411  ? -14.822 6.093   102.729 1.00 28.90 ? 409  LEU   B CG    1 
ATOM   11974 C  CD1   . LEU   B  1  411  ? -14.542 7.502   103.190 1.00 27.34 ? 409  LEU   B CD1   1 
ATOM   11975 C  CD2   . LEU   B  1  411  ? -13.712 5.151   103.161 1.00 28.51 ? 409  LEU   B CD2   1 
ATOM   11976 N  N     . LEU   B  1  412  ? -19.003 4.225   103.468 1.00 29.98 ? 410  LEU   B N     1 
ATOM   11977 C  CA    . LEU   B  1  412  ? -20.017 3.655   104.352 1.00 31.58 ? 410  LEU   B CA    1 
ATOM   11978 C  C     . LEU   B  1  412  ? -20.402 2.250   103.922 1.00 32.72 ? 410  LEU   B C     1 
ATOM   11979 O  O     . LEU   B  1  412  ? -20.835 1.446   104.754 1.00 36.63 ? 410  LEU   B O     1 
ATOM   11980 C  CB    . LEU   B  1  412  ? -21.249 4.560   104.421 1.00 34.73 ? 410  LEU   B CB    1 
ATOM   11981 C  CG    . LEU   B  1  412  ? -21.082 5.826   105.264 1.00 33.64 ? 410  LEU   B CG    1 
ATOM   11982 C  CD1   . LEU   B  1  412  ? -22.202 6.810   104.982 1.00 38.56 ? 410  LEU   B CD1   1 
ATOM   11983 C  CD2   . LEU   B  1  412  ? -21.033 5.474   106.742 1.00 36.63 ? 410  LEU   B CD2   1 
ATOM   11984 N  N     . ALA   B  1  413  ? -20.250 1.937   102.638 1.00 32.82 ? 411  ALA   B N     1 
ATOM   11985 C  CA    . ALA   B  1  413  ? -20.450 0.577   102.162 1.00 37.87 ? 411  ALA   B CA    1 
ATOM   11986 C  C     . ALA   B  1  413  ? -19.255 -0.321  102.445 1.00 33.85 ? 411  ALA   B C     1 
ATOM   11987 O  O     . ALA   B  1  413  ? -19.312 -1.516  102.144 1.00 38.54 ? 411  ALA   B O     1 
ATOM   11988 C  CB    . ALA   B  1  413  ? -20.748 0.582   100.663 1.00 38.53 ? 411  ALA   B CB    1 
ATOM   11989 N  N     . ALA   B  1  414  ? -18.181 0.216   103.028 1.00 35.77 ? 412  ALA   B N     1 
ATOM   11990 C  CA    . ALA   B  1  414  ? -16.986 -0.572  103.297 1.00 29.95 ? 412  ALA   B CA    1 
ATOM   11991 C  C     . ALA   B  1  414  ? -16.561 -0.500  104.762 1.00 34.50 ? 412  ALA   B C     1 
ATOM   11992 O  O     . ALA   B  1  414  ? -15.381 -0.708  105.064 1.00 32.29 ? 412  ALA   B O     1 
ATOM   11993 C  CB    . ALA   B  1  414  ? -15.833 -0.148  102.383 1.00 33.78 ? 412  ALA   B CB    1 
ATOM   11994 N  N     . THR   B  1  415  ? -17.494 -0.217  105.681 1.00 33.15 ? 413  THR   B N     1 
ATOM   11995 C  CA    . THR   B  1  415  ? -17.132 -0.075  107.091 1.00 32.17 ? 413  THR   B CA    1 
ATOM   11996 C  C     . THR   B  1  415  ? -16.607 -1.369  107.686 1.00 31.53 ? 413  THR   B C     1 
ATOM   11997 O  O     . THR   B  1  415  ? -15.932 -1.334  108.721 1.00 35.06 ? 413  THR   B O     1 
ATOM   11998 C  CB    . THR   B  1  415  ? -18.311 0.432   107.921 1.00 34.13 ? 413  THR   B CB    1 
ATOM   11999 O  OG1   . THR   B  1  415  ? -19.399 -0.494  107.821 1.00 37.29 ? 413  THR   B OG1   1 
ATOM   12000 C  CG2   . THR   B  1  415  ? -18.761 1.799   107.440 1.00 34.56 ? 413  THR   B CG2   1 
ATOM   12001 N  N     . ASP   B  1  416  ? -16.892 -2.508  107.057 1.00 35.87 ? 414  ASP   B N     1 
ATOM   12002 C  CA    . ASP   B  1  416  ? -16.291 -3.762  107.482 1.00 36.18 ? 414  ASP   B CA    1 
ATOM   12003 C  C     . ASP   B  1  416  ? -14.806 -3.838  107.156 1.00 30.57 ? 414  ASP   B C     1 
ATOM   12004 O  O     . ASP   B  1  416  ? -14.112 -4.701  107.702 1.00 37.19 ? 414  ASP   B O     1 
ATOM   12005 C  CB    . ASP   B  1  416  ? -17.047 -4.946  106.860 1.00 30.76 ? 414  ASP   B CB    1 
ATOM   12006 C  CG    . ASP   B  1  416  ? -17.057 -4.906  105.329 1.00 43.65 ? 414  ASP   B CG    1 
ATOM   12007 O  OD1   . ASP   B  1  416  ? -16.970 -3.804  104.746 1.00 44.17 ? 414  ASP   B OD1   1 
ATOM   12008 O  OD2   . ASP   B  1  416  ? -17.160 -5.986  104.707 1.00 47.58 ? 414  ASP   B OD2   1 
ATOM   12009 N  N     . VAL   B  1  417  ? -14.295 -2.941  106.310 1.00 32.88 ? 415  VAL   B N     1 
ATOM   12010 C  CA    . VAL   B  1  417  ? -12.951 -3.063  105.752 1.00 30.97 ? 415  VAL   B CA    1 
ATOM   12011 C  C     . VAL   B  1  417  ? -12.091 -1.860  106.130 1.00 30.82 ? 415  VAL   B C     1 
ATOM   12012 O  O     . VAL   B  1  417  ? -10.872 -1.976  106.287 1.00 29.26 ? 415  VAL   B O     1 
ATOM   12013 C  CB    . VAL   B  1  417  ? -13.042 -3.235  104.223 1.00 35.84 ? 415  VAL   B CB    1 
ATOM   12014 C  CG1   . VAL   B  1  417  ? -11.667 -3.336  103.600 1.00 28.95 ? 415  VAL   B CG1   1 
ATOM   12015 C  CG2   . VAL   B  1  417  ? -13.867 -4.467  103.889 1.00 36.44 ? 415  VAL   B CG2   1 
ATOM   12016 N  N     . VAL   B  1  418  ? -12.714 -0.690  106.249 1.00 29.89 ? 416  VAL   B N     1 
ATOM   12017 C  CA    . VAL   B  1  418  ? -12.020 0.527   106.643 1.00 27.57 ? 416  VAL   B CA    1 
ATOM   12018 C  C     . VAL   B  1  418  ? -12.853 1.220   107.706 1.00 32.50 ? 416  VAL   B C     1 
ATOM   12019 O  O     . VAL   B  1  418  ? -14.039 0.937   107.884 1.00 29.49 ? 416  VAL   B O     1 
ATOM   12020 C  CB    . VAL   B  1  418  ? -11.762 1.484   105.460 1.00 28.33 ? 416  VAL   B CB    1 
ATOM   12021 C  CG1   . VAL   B  1  418  ? -10.737 0.887   104.507 1.00 25.30 ? 416  VAL   B CG1   1 
ATOM   12022 C  CG2   . VAL   B  1  418  ? -13.075 1.783   104.729 1.00 27.50 ? 416  VAL   B CG2   1 
ATOM   12023 N  N     . PHE   B  1  419  ? -12.206 2.134   108.424 1.00 27.45 ? 417  PHE   B N     1 
ATOM   12024 C  CA    . PHE   B  1  419  ? -12.881 2.915   109.452 1.00 27.29 ? 417  PHE   B CA    1 
ATOM   12025 C  C     . PHE   B  1  419  ? -13.059 4.325   108.912 1.00 24.77 ? 417  PHE   B C     1 
ATOM   12026 O  O     . PHE   B  1  419  ? -12.108 5.124   108.929 1.00 25.60 ? 417  PHE   B O     1 
ATOM   12027 C  CB    . PHE   B  1  419  ? -12.056 2.930   110.739 1.00 28.88 ? 417  PHE   B CB    1 
ATOM   12028 C  CG    . PHE   B  1  419  ? -12.662 3.751   111.836 1.00 26.74 ? 417  PHE   B CG    1 
ATOM   12029 C  CD1   . PHE   B  1  419  ? -13.917 3.448   112.340 1.00 30.53 ? 417  PHE   B CD1   1 
ATOM   12030 C  CD2   . PHE   B  1  419  ? -11.972 4.828   112.368 1.00 27.78 ? 417  PHE   B CD2   1 
ATOM   12031 C  CE1   . PHE   B  1  419  ? -14.471 4.208   113.362 1.00 30.37 ? 417  PHE   B CE1   1 
ATOM   12032 C  CE2   . PHE   B  1  419  ? -12.521 5.588   113.388 1.00 27.63 ? 417  PHE   B CE2   1 
ATOM   12033 C  CZ    . PHE   B  1  419  ? -13.772 5.283   113.878 1.00 28.36 ? 417  PHE   B CZ    1 
ATOM   12034 N  N     . PRO   B  1  420  ? -14.240 4.673   108.413 1.00 24.50 ? 418  PRO   B N     1 
ATOM   12035 C  CA    . PRO   B  1  420  ? -14.425 5.994   107.810 1.00 24.72 ? 418  PRO   B CA    1 
ATOM   12036 C  C     . PRO   B  1  420  ? -14.499 7.070   108.877 1.00 24.35 ? 418  PRO   B C     1 
ATOM   12037 O  O     . PRO   B  1  420  ? -15.134 6.896   109.917 1.00 24.58 ? 418  PRO   B O     1 
ATOM   12038 C  CB    . PRO   B  1  420  ? -15.764 5.858   107.075 1.00 28.12 ? 418  PRO   B CB    1 
ATOM   12039 C  CG    . PRO   B  1  420  ? -15.985 4.387   106.945 1.00 28.57 ? 418  PRO   B CG    1 
ATOM   12040 C  CD    . PRO   B  1  420  ? -15.408 3.807   108.194 1.00 27.69 ? 418  PRO   B CD    1 
ATOM   12041 N  N     . GLN   B  1  421  ? -13.837 8.188   108.607 1.00 24.90 ? 419  GLN   B N     1 
ATOM   12042 C  CA    . GLN   B  1  421  ? -13.778 9.312   109.533 1.00 24.30 ? 419  GLN   B CA    1 
ATOM   12043 C  C     . GLN   B  1  421  ? -14.147 10.541  108.726 1.00 22.79 ? 419  GLN   B C     1 
ATOM   12044 O  O     . GLN   B  1  421  ? -13.376 10.981  107.871 1.00 22.31 ? 419  GLN   B O     1 
ATOM   12045 C  CB    . GLN   B  1  421  ? -12.379 9.445   110.133 1.00 22.19 ? 419  GLN   B CB    1 
ATOM   12046 C  CG    . GLN   B  1  421  ? -11.933 8.185   110.813 1.00 23.09 ? 419  GLN   B CG    1 
ATOM   12047 C  CD    . GLN   B  1  421  ? -10.450 8.150   111.037 1.00 23.72 ? 419  GLN   B CD    1 
ATOM   12048 O  OE1   . GLN   B  1  421  ? -9.674  8.210   110.093 1.00 24.61 ? 419  GLN   B OE1   1 
ATOM   12049 N  NE2   . GLN   B  1  421  ? -10.043 8.055   112.295 1.00 24.22 ? 419  GLN   B NE2   1 
ATOM   12050 N  N     . PHE   B  1  422  ? -15.344 11.065  108.956 1.00 24.77 ? 420  PHE   B N     1 
ATOM   12051 C  CA    . PHE   B  1  422  ? -15.891 12.110  108.102 1.00 23.82 ? 420  PHE   B CA    1 
ATOM   12052 C  C     . PHE   B  1  422  ? -15.590 13.462  108.733 1.00 25.38 ? 420  PHE   B C     1 
ATOM   12053 O  O     . PHE   B  1  422  ? -16.301 13.935  109.622 1.00 24.50 ? 420  PHE   B O     1 
ATOM   12054 C  CB    . PHE   B  1  422  ? -17.375 11.872  107.864 1.00 25.05 ? 420  PHE   B CB    1 
ATOM   12055 C  CG    . PHE   B  1  422  ? -17.666 10.545  107.223 1.00 26.97 ? 420  PHE   B CG    1 
ATOM   12056 C  CD1   . PHE   B  1  422  ? -17.280 10.299  105.918 1.00 27.90 ? 420  PHE   B CD1   1 
ATOM   12057 C  CD2   . PHE   B  1  422  ? -18.322 9.543   107.916 1.00 28.83 ? 420  PHE   B CD2   1 
ATOM   12058 C  CE1   . PHE   B  1  422  ? -17.544 9.083   105.318 1.00 30.52 ? 420  PHE   B CE1   1 
ATOM   12059 C  CE2   . PHE   B  1  422  ? -18.583 8.320   107.313 1.00 31.72 ? 420  PHE   B CE2   1 
ATOM   12060 C  CZ    . PHE   B  1  422  ? -18.192 8.098   106.007 1.00 32.24 ? 420  PHE   B CZ    1 
ATOM   12061 N  N     . ALA   B  1  423  ? -14.494 14.069  108.281 1.00 23.56 ? 421  ALA   B N     1 
ATOM   12062 C  CA    . ALA   B  1  423  ? -14.081 15.378  108.762 1.00 21.96 ? 421  ALA   B CA    1 
ATOM   12063 C  C     . ALA   B  1  423  ? -14.823 16.442  107.972 1.00 26.23 ? 421  ALA   B C     1 
ATOM   12064 O  O     . ALA   B  1  423  ? -14.590 16.605  106.773 1.00 27.12 ? 421  ALA   B O     1 
ATOM   12065 C  CB    . ALA   B  1  423  ? -12.577 15.538  108.561 1.00 22.51 ? 421  ALA   B CB    1 
ATOM   12066 N  N     . THR   B  1  424  ? -15.707 17.179  108.640 1.00 27.34 ? 422  THR   B N     1 
ATOM   12067 C  CA    . THR   B  1  424  ? -16.405 18.281  107.995 1.00 24.27 ? 422  THR   B CA    1 
ATOM   12068 C  C     . THR   B  1  424  ? -17.003 19.168  109.074 1.00 23.83 ? 422  THR   B C     1 
ATOM   12069 O  O     . THR   B  1  424  ? -17.387 18.689  110.140 1.00 28.00 ? 422  THR   B O     1 
ATOM   12070 C  CB    . THR   B  1  424  ? -17.510 17.780  107.049 1.00 26.18 ? 422  THR   B CB    1 
ATOM   12071 O  OG1   . THR   B  1  424  ? -18.142 18.906  106.430 1.00 27.10 ? 422  THR   B OG1   1 
ATOM   12072 C  CG2   . THR   B  1  424  ? -18.550 16.952  107.813 1.00 27.53 ? 422  THR   B CG2   1 
ATOM   12073 N  N     . HIS   B  1  425  ? -17.037 20.468  108.801 1.00 26.17 ? 423  HIS   B N     1 
ATOM   12074 C  CA    . HIS   B  1  425  ? -17.769 21.407  109.643 1.00 26.37 ? 423  HIS   B CA    1 
ATOM   12075 C  C     . HIS   B  1  425  ? -19.103 21.803  109.033 1.00 32.40 ? 423  HIS   B C     1 
ATOM   12076 O  O     . HIS   B  1  425  ? -19.815 22.629  109.608 1.00 30.58 ? 423  HIS   B O     1 
ATOM   12077 C  CB    . HIS   B  1  425  ? -16.923 22.653  109.899 1.00 26.77 ? 423  HIS   B CB    1 
ATOM   12078 C  CG    . HIS   B  1  425  ? -15.653 22.369  110.637 1.00 24.03 ? 423  HIS   B CG    1 
ATOM   12079 N  ND1   . HIS   B  1  425  ? -14.440 22.890  110.251 1.00 29.11 ? 423  HIS   B ND1   1 
ATOM   12080 C  CD2   . HIS   B  1  425  ? -15.406 21.601  111.725 1.00 26.23 ? 423  HIS   B CD2   1 
ATOM   12081 C  CE1   . HIS   B  1  425  ? -13.499 22.468  111.079 1.00 26.94 ? 423  HIS   B CE1   1 
ATOM   12082 N  NE2   . HIS   B  1  425  ? -14.060 21.687  111.983 1.00 25.99 ? 423  HIS   B NE2   1 
ATOM   12083 N  N     . ASN   B  1  426  ? -19.454 21.225  107.891 1.00 28.34 ? 424  ASN   B N     1 
ATOM   12084 C  CA    . ASN   B  1  426  ? -20.650 21.594  107.154 1.00 28.70 ? 424  ASN   B CA    1 
ATOM   12085 C  C     . ASN   B  1  426  ? -21.814 20.735  107.635 1.00 31.09 ? 424  ASN   B C     1 
ATOM   12086 O  O     . ASN   B  1  426  ? -21.803 19.510  107.463 1.00 28.79 ? 424  ASN   B O     1 
ATOM   12087 C  CB    . ASN   B  1  426  ? -20.381 21.365  105.669 1.00 29.06 ? 424  ASN   B CB    1 
ATOM   12088 C  CG    . ASN   B  1  426  ? -21.481 21.892  104.786 1.00 29.47 ? 424  ASN   B CG    1 
ATOM   12089 O  OD1   . ASN   B  1  426  ? -22.664 21.658  105.041 1.00 30.44 ? 424  ASN   B OD1   1 
ATOM   12090 N  ND2   . ASN   B  1  426  ? -21.098 22.595  103.721 1.00 29.11 ? 424  ASN   B ND2   1 
ATOM   12091 N  N     . ALA   B  1  427  ? -22.818 21.382  108.247 1.00 32.00 ? 425  ALA   B N     1 
ATOM   12092 C  CA    . ALA   B  1  427  ? -23.955 20.654  108.801 1.00 36.44 ? 425  ALA   B CA    1 
ATOM   12093 C  C     . ALA   B  1  427  ? -24.760 19.941  107.721 1.00 30.12 ? 425  ALA   B C     1 
ATOM   12094 O  O     . ALA   B  1  427  ? -25.344 18.881  107.983 1.00 32.45 ? 425  ALA   B O     1 
ATOM   12095 C  CB    . ALA   B  1  427  ? -24.850 21.603  109.600 1.00 37.84 ? 425  ALA   B CB    1 
ATOM   12096 N  N     . GLN   B  1  428  ? -24.791 20.489  106.502 1.00 31.22 ? 426  GLN   B N     1 
ATOM   12097 C  CA    . GLN   B  1  428  ? -25.479 19.792  105.421 1.00 32.07 ? 426  GLN   B CA    1 
ATOM   12098 C  C     . GLN   B  1  428  ? -24.751 18.505  105.064 1.00 30.00 ? 426  GLN   B C     1 
ATOM   12099 O  O     . GLN   B  1  428  ? -25.367 17.438  104.952 1.00 30.67 ? 426  GLN   B O     1 
ATOM   12100 C  CB    . GLN   B  1  428  ? -25.632 20.703  104.203 1.00 33.93 ? 426  GLN   B CB    1 
ATOM   12101 C  CG    . GLN   B  1  428  ? -26.643 20.196  103.175 1.00 35.42 ? 426  GLN   B CG    1 
ATOM   12102 C  CD    . GLN   B  1  428  ? -26.125 19.025  102.354 1.00 32.67 ? 426  GLN   B CD    1 
ATOM   12103 O  OE1   . GLN   B  1  428  ? -24.947 18.981  101.990 1.00 35.09 ? 426  GLN   B OE1   1 
ATOM   12104 N  NE2   . GLN   B  1  428  ? -26.998 18.065  102.069 1.00 36.76 ? 426  GLN   B NE2   1 
ATOM   12105 N  N     . THR   B  1  429  ? -23.425 18.585  104.900 1.00 30.65 ? 427  THR   B N     1 
ATOM   12106 C  CA    . THR   B  1  429  ? -22.637 17.390  104.614 1.00 32.63 ? 427  THR   B CA    1 
ATOM   12107 C  C     . THR   B  1  429  ? -22.803 16.347  105.710 1.00 27.43 ? 427  THR   B C     1 
ATOM   12108 O  O     . THR   B  1  429  ? -23.012 15.158  105.432 1.00 28.40 ? 427  THR   B O     1 
ATOM   12109 C  CB    . THR   B  1  429  ? -21.164 17.771  104.485 1.00 28.65 ? 427  THR   B CB    1 
ATOM   12110 O  OG1   . THR   B  1  429  ? -21.030 18.892  103.606 1.00 28.27 ? 427  THR   B OG1   1 
ATOM   12111 C  CG2   . THR   B  1  429  ? -20.376 16.596  103.952 1.00 31.62 ? 427  THR   B CG2   1 
ATOM   12112 N  N     . LEU   B  1  430  ? -22.687 16.776  106.972 1.00 32.03 ? 428  LEU   B N     1 
ATOM   12113 C  CA    . LEU   B  1  430  ? -22.819 15.855  108.096 1.00 29.72 ? 428  LEU   B CA    1 
ATOM   12114 C  C     . LEU   B  1  430  ? -24.183 15.186  108.084 1.00 28.44 ? 428  LEU   B C     1 
ATOM   12115 O  O     . LEU   B  1  430  ? -24.288 13.964  108.234 1.00 30.81 ? 428  LEU   B O     1 
ATOM   12116 C  CB    . LEU   B  1  430  ? -22.619 16.619  109.406 1.00 32.05 ? 428  LEU   B CB    1 
ATOM   12117 C  CG    . LEU   B  1  430  ? -22.508 15.901  110.761 1.00 33.53 ? 428  LEU   B CG    1 
ATOM   12118 C  CD1   . LEU   B  1  430  ? -22.095 16.924  111.786 1.00 32.97 ? 428  LEU   B CD1   1 
ATOM   12119 C  CD2   . LEU   B  1  430  ? -23.783 15.215  111.227 1.00 38.60 ? 428  LEU   B CD2   1 
ATOM   12120 N  N     . ALA   B  1  431  ? -25.243 15.981  107.912 1.00 33.96 ? 429  ALA   B N     1 
ATOM   12121 C  CA    . ALA   B  1  431  ? -26.595 15.434  107.943 1.00 34.94 ? 429  ALA   B CA    1 
ATOM   12122 C  C     . ALA   B  1  431  ? -26.793 14.409  106.837 1.00 34.23 ? 429  ALA   B C     1 
ATOM   12123 O  O     . ALA   B  1  431  ? -27.409 13.361  107.056 1.00 36.50 ? 429  ALA   B O     1 
ATOM   12124 C  CB    . ALA   B  1  431  ? -27.614 16.566  107.825 1.00 36.87 ? 429  ALA   B CB    1 
ATOM   12125 N  N     . ALA   B  1  432  ? -26.240 14.679  105.648 1.00 34.27 ? 430  ALA   B N     1 
ATOM   12126 C  CA    . ALA   B  1  432  ? -26.360 13.733  104.544 1.00 30.18 ? 430  ALA   B CA    1 
ATOM   12127 C  C     . ALA   B  1  432  ? -25.703 12.403  104.885 1.00 34.17 ? 430  ALA   B C     1 
ATOM   12128 O  O     . ALA   B  1  432  ? -26.252 11.338  104.589 1.00 35.39 ? 430  ALA   B O     1 
ATOM   12129 C  CB    . ALA   B  1  432  ? -25.755 14.325  103.269 1.00 31.73 ? 430  ALA   B CB    1 
ATOM   12130 N  N     . ILE   B  1  433  ? -24.518 12.443  105.499 1.00 33.20 ? 431  ILE   B N     1 
ATOM   12131 C  CA    . ILE   B  1  433  ? -23.820 11.202  105.826 1.00 35.41 ? 431  ILE   B CA    1 
ATOM   12132 C  C     . ILE   B  1  433  ? -24.468 10.509  107.013 1.00 32.92 ? 431  ILE   B C     1 
ATOM   12133 O  O     . ILE   B  1  433  ? -24.557 9.276   107.059 1.00 31.93 ? 431  ILE   B O     1 
ATOM   12134 C  CB    . ILE   B  1  433  ? -22.333 11.486  106.081 1.00 30.85 ? 431  ILE   B CB    1 
ATOM   12135 C  CG1   . ILE   B  1  433  ? -21.666 11.952  104.794 1.00 35.54 ? 431  ILE   B CG1   1 
ATOM   12136 C  CG2   . ILE   B  1  433  ? -21.638 10.251  106.648 1.00 36.37 ? 431  ILE   B CG2   1 
ATOM   12137 C  CD1   . ILE   B  1  433  ? -20.263 12.337  105.013 1.00 36.35 ? 431  ILE   B CD1   1 
ATOM   12138 N  N     . TYR   B  1  434  ? -24.893 11.286  108.007 1.00 35.13 ? 432  TYR   B N     1 
ATOM   12139 C  CA    . TYR   B  1  434  ? -25.562 10.709  109.166 1.00 34.94 ? 432  TYR   B CA    1 
ATOM   12140 C  C     . TYR   B  1  434  ? -26.757 9.867   108.742 1.00 37.10 ? 432  TYR   B C     1 
ATOM   12141 O  O     . TYR   B  1  434  ? -26.938 8.741   109.218 1.00 36.61 ? 432  TYR   B O     1 
ATOM   12142 C  CB    . TYR   B  1  434  ? -25.972 11.837  110.111 1.00 37.13 ? 432  TYR   B CB    1 
ATOM   12143 C  CG    . TYR   B  1  434  ? -26.904 11.428  111.220 1.00 34.80 ? 432  TYR   B CG    1 
ATOM   12144 C  CD1   . TYR   B  1  434  ? -26.447 10.697  112.308 1.00 36.17 ? 432  TYR   B CD1   1 
ATOM   12145 C  CD2   . TYR   B  1  434  ? -28.244 11.785  111.181 1.00 37.26 ? 432  TYR   B CD2   1 
ATOM   12146 C  CE1   . TYR   B  1  434  ? -27.307 10.332  113.331 1.00 37.88 ? 432  TYR   B CE1   1 
ATOM   12147 C  CE2   . TYR   B  1  434  ? -29.103 11.430  112.190 1.00 38.80 ? 432  TYR   B CE2   1 
ATOM   12148 C  CZ    . TYR   B  1  434  ? -28.632 10.701  113.260 1.00 39.98 ? 432  TYR   B CZ    1 
ATOM   12149 O  OH    . TYR   B  1  434  ? -29.496 10.342  114.265 1.00 37.88 ? 432  TYR   B OH    1 
ATOM   12150 N  N     . HIS   B  1  435  ? -27.548 10.369  107.798 1.00 38.63 ? 433  HIS   B N     1 
ATOM   12151 C  CA    . HIS   B  1  435  ? -28.704 9.605   107.348 1.00 39.56 ? 433  HIS   B CA    1 
ATOM   12152 C  C     . HIS   B  1  435  ? -28.317 8.535   106.339 1.00 39.05 ? 433  HIS   B C     1 
ATOM   12153 O  O     . HIS   B  1  435  ? -28.886 7.439   106.347 1.00 39.05 ? 433  HIS   B O     1 
ATOM   12154 C  CB    . HIS   B  1  435  ? -29.771 10.545  106.805 1.00 41.48 ? 433  HIS   B CB    1 
ATOM   12155 C  CG    . HIS   B  1  435  ? -30.489 11.293  107.878 1.00 41.10 ? 433  HIS   B CG    1 
ATOM   12156 N  ND1   . HIS   B  1  435  ? -31.484 10.720  108.639 1.00 39.14 ? 433  HIS   B ND1   1 
ATOM   12157 C  CD2   . HIS   B  1  435  ? -30.337 12.555  108.342 1.00 39.06 ? 433  HIS   B CD2   1 
ATOM   12158 C  CE1   . HIS   B  1  435  ? -31.927 11.603  109.516 1.00 45.37 ? 433  HIS   B CE1   1 
ATOM   12159 N  NE2   . HIS   B  1  435  ? -31.250 12.725  109.356 1.00 39.77 ? 433  HIS   B NE2   1 
ATOM   12160 N  N     . MET   B  1  436  ? -27.341 8.829   105.479 1.00 34.74 ? 434  MET   B N     1 
ATOM   12161 C  CA    . MET   B  1  436  ? -26.850 7.816   104.556 1.00 35.93 ? 434  MET   B CA    1 
ATOM   12162 C  C     . MET   B  1  436  ? -26.345 6.588   105.295 1.00 33.13 ? 434  MET   B C     1 
ATOM   12163 O  O     . MET   B  1  436  ? -26.467 5.465   104.792 1.00 38.15 ? 434  MET   B O     1 
ATOM   12164 C  CB    . MET   B  1  436  ? -25.732 8.411   103.706 1.00 36.76 ? 434  MET   B CB    1 
ATOM   12165 C  CG    . MET   B  1  436  ? -25.039 7.418   102.806 1.00 40.01 ? 434  MET   B CG    1 
ATOM   12166 S  SD    . MET   B  1  436  ? -23.628 8.197   102.005 1.00 39.70 ? 434  MET   B SD    1 
ATOM   12167 C  CE    . MET   B  1  436  ? -24.461 9.359   100.937 1.00 37.61 ? 434  MET   B CE    1 
ATOM   12168 N  N     . ALA   B  1  437  ? -25.780 6.779   106.492 1.00 35.44 ? 435  ALA   B N     1 
ATOM   12169 C  CA    . ALA   B  1  437  ? -25.232 5.664   107.255 1.00 36.88 ? 435  ALA   B CA    1 
ATOM   12170 C  C     . ALA   B  1  437  ? -26.316 4.768   107.833 1.00 40.15 ? 435  ALA   B C     1 
ATOM   12171 O  O     . ALA   B  1  437  ? -26.031 3.618   108.185 1.00 39.77 ? 435  ALA   B O     1 
ATOM   12172 C  CB    . ALA   B  1  437  ? -24.344 6.190   108.383 1.00 38.99 ? 435  ALA   B CB    1 
ATOM   12173 N  N     . GLY   B  1  438  ? -27.542 5.264   107.942 1.00 42.68 ? 436  GLY   B N     1 
ATOM   12174 C  CA    . GLY   B  1  438  ? -28.639 4.451   108.420 1.00 41.64 ? 436  GLY   B CA    1 
ATOM   12175 C  C     . GLY   B  1  438  ? -28.725 4.415   109.932 1.00 44.83 ? 436  GLY   B C     1 
ATOM   12176 O  O     . GLY   B  1  438  ? -27.984 5.081   110.660 1.00 47.16 ? 436  GLY   B O     1 
ATOM   12177 N  N     . LYS   B  1  439  ? -29.657 3.587   110.408 1.00 44.89 ? 437  LYS   B N     1 
ATOM   12178 C  CA    . LYS   B  1  439  ? -29.977 3.544   111.830 1.00 43.84 ? 437  LYS   B CA    1 
ATOM   12179 C  C     . LYS   B  1  439  ? -28.978 2.723   112.637 1.00 44.90 ? 437  LYS   B C     1 
ATOM   12180 O  O     . LYS   B  1  439  ? -28.802 2.982   113.833 1.00 47.46 ? 437  LYS   B O     1 
ATOM   12181 C  CB    . LYS   B  1  439  ? -31.386 2.983   112.033 1.00 40.21 ? 437  LYS   B CB    1 
ATOM   12182 N  N     . ASP   B  1  440  ? -28.330 1.736   112.022 1.00 42.22 ? 438  ASP   B N     1 
ATOM   12183 C  CA    . ASP   B  1  440  ? -27.456 0.831   112.759 1.00 45.67 ? 438  ASP   B CA    1 
ATOM   12184 C  C     . ASP   B  1  440  ? -26.108 1.503   112.974 1.00 43.47 ? 438  ASP   B C     1 
ATOM   12185 O  O     . ASP   B  1  440  ? -25.394 1.796   112.008 1.00 46.21 ? 438  ASP   B O     1 
ATOM   12186 C  CB    . ASP   B  1  440  ? -27.281 -0.478  111.992 1.00 47.38 ? 438  ASP   B CB    1 
ATOM   12187 N  N     . PHE   B  1  441  ? -25.762 1.756   114.234 1.00 41.28 ? 439  PHE   B N     1 
ATOM   12188 C  CA    . PHE   B  1  441  ? -24.492 2.395   114.543 1.00 38.42 ? 439  PHE   B CA    1 
ATOM   12189 C  C     . PHE   B  1  441  ? -23.897 1.829   115.822 1.00 39.13 ? 439  PHE   B C     1 
ATOM   12190 O  O     . PHE   B  1  441  ? -24.608 1.464   116.764 1.00 36.94 ? 439  PHE   B O     1 
ATOM   12191 C  CB    . PHE   B  1  441  ? -24.604 3.915   114.690 1.00 37.68 ? 439  PHE   B CB    1 
ATOM   12192 C  CG    . PHE   B  1  441  ? -23.283 4.573   114.950 1.00 39.77 ? 439  PHE   B CG    1 
ATOM   12193 C  CD1   . PHE   B  1  441  ? -22.440 4.864   113.899 1.00 33.00 ? 439  PHE   B CD1   1 
ATOM   12194 C  CD2   . PHE   B  1  441  ? -22.863 4.850   116.245 1.00 35.40 ? 439  PHE   B CD2   1 
ATOM   12195 C  CE1   . PHE   B  1  441  ? -21.209 5.445   114.117 1.00 36.98 ? 439  PHE   B CE1   1 
ATOM   12196 C  CE2   . PHE   B  1  441  ? -21.633 5.427   116.474 1.00 36.44 ? 439  PHE   B CE2   1 
ATOM   12197 C  CZ    . PHE   B  1  441  ? -20.805 5.720   115.402 1.00 36.77 ? 439  PHE   B CZ    1 
ATOM   12198 N  N     . HIS   B  1  442  ? -22.569 1.779   115.842 1.00 39.85 ? 440  HIS   B N     1 
ATOM   12199 C  CA    . HIS   B  1  442  ? -21.808 1.486   117.043 1.00 38.03 ? 440  HIS   B CA    1 
ATOM   12200 C  C     . HIS   B  1  442  ? -20.485 2.227   116.937 1.00 35.52 ? 440  HIS   B C     1 
ATOM   12201 O  O     . HIS   B  1  442  ? -20.041 2.586   115.842 1.00 34.91 ? 440  HIS   B O     1 
ATOM   12202 C  CB    . HIS   B  1  442  ? -21.554 -0.015  117.178 1.00 37.94 ? 440  HIS   B CB    1 
ATOM   12203 C  CG    . HIS   B  1  442  ? -20.935 -0.625  115.961 1.00 40.57 ? 440  HIS   B CG    1 
ATOM   12204 N  ND1   . HIS   B  1  442  ? -19.576 -0.602  115.726 1.00 43.88 ? 440  HIS   B ND1   1 
ATOM   12205 C  CD2   . HIS   B  1  442  ? -21.492 -1.256  114.899 1.00 39.30 ? 440  HIS   B CD2   1 
ATOM   12206 C  CE1   . HIS   B  1  442  ? -19.321 -1.204  114.576 1.00 38.01 ? 440  HIS   B CE1   1 
ATOM   12207 N  NE2   . HIS   B  1  442  ? -20.466 -1.609  114.055 1.00 44.36 ? 440  HIS   B NE2   1 
ATOM   12208 N  N     . VAL   B  1  443  ? -19.860 2.468   118.089 1.00 36.57 ? 441  VAL   B N     1 
ATOM   12209 C  CA    . VAL   B  1  443  ? -18.511 3.018   118.071 1.00 37.13 ? 441  VAL   B CA    1 
ATOM   12210 C  C     . VAL   B  1  443  ? -17.581 2.014   117.413 1.00 33.23 ? 441  VAL   B C     1 
ATOM   12211 O  O     . VAL   B  1  443  ? -17.596 0.821   117.736 1.00 36.31 ? 441  VAL   B O     1 
ATOM   12212 C  CB    . VAL   B  1  443  ? -18.049 3.386   119.486 1.00 38.63 ? 441  VAL   B CB    1 
ATOM   12213 C  CG1   . VAL   B  1  443  ? -16.560 3.701   119.477 1.00 34.46 ? 441  VAL   B CG1   1 
ATOM   12214 C  CG2   . VAL   B  1  443  ? -18.835 4.580   119.996 1.00 40.34 ? 441  VAL   B CG2   1 
ATOM   12215 N  N     . GLY   B  1  444  ? -16.784 2.491   116.459 1.00 34.86 ? 442  GLY   B N     1 
ATOM   12216 C  CA    . GLY   B  1  444  ? -15.914 1.653   115.665 1.00 34.60 ? 442  GLY   B CA    1 
ATOM   12217 C  C     . GLY   B  1  444  ? -16.404 1.435   114.249 1.00 31.97 ? 442  GLY   B C     1 
ATOM   12218 O  O     . GLY   B  1  444  ? -15.623 0.986   113.400 1.00 31.83 ? 442  GLY   B O     1 
ATOM   12219 N  N     . LYS   B  1  445  ? -17.675 1.733   113.974 1.00 32.54 ? 443  LYS   B N     1 
ATOM   12220 C  CA    . LYS   B  1  445  ? -18.186 1.624   112.612 1.00 30.78 ? 443  LYS   B CA    1 
ATOM   12221 C  C     . LYS   B  1  445  ? -17.663 2.769   111.753 1.00 31.65 ? 443  LYS   B C     1 
ATOM   12222 O  O     . LYS   B  1  445  ? -17.070 2.552   110.692 1.00 32.45 ? 443  LYS   B O     1 
ATOM   12223 C  CB    . LYS   B  1  445  ? -19.716 1.612   112.625 1.00 30.22 ? 443  LYS   B CB    1 
ATOM   12224 C  CG    . LYS   B  1  445  ? -20.328 1.344   111.258 1.00 35.84 ? 443  LYS   B CG    1 
ATOM   12225 C  CD    . LYS   B  1  445  ? -21.837 1.201   111.348 1.00 40.17 ? 443  LYS   B CD    1 
ATOM   12226 C  CE    . LYS   B  1  445  ? -22.434 0.814   110.007 1.00 41.14 ? 443  LYS   B CE    1 
ATOM   12227 N  NZ    . LYS   B  1  445  ? -23.895 0.567   110.147 1.00 45.09 ? 443  LYS   B NZ    1 
ATOM   12228 N  N     . TYR   B  1  446  ? -17.894 3.999   112.195 1.00 30.79 ? 444  TYR   B N     1 
ATOM   12229 C  CA    . TYR   B  1  446  ? -17.337 5.193   111.578 1.00 29.11 ? 444  TYR   B CA    1 
ATOM   12230 C  C     . TYR   B  1  446  ? -17.405 6.293   112.625 1.00 31.47 ? 444  TYR   B C     1 
ATOM   12231 O  O     . TYR   B  1  446  ? -18.018 6.128   113.684 1.00 29.37 ? 444  TYR   B O     1 
ATOM   12232 C  CB    . TYR   B  1  446  ? -18.102 5.582   110.305 1.00 29.85 ? 444  TYR   B CB    1 
ATOM   12233 C  CG    . TYR   B  1  446  ? -19.520 6.045   110.557 1.00 35.28 ? 444  TYR   B CG    1 
ATOM   12234 C  CD1   . TYR   B  1  446  ? -19.804 7.384   110.812 1.00 29.02 ? 444  TYR   B CD1   1 
ATOM   12235 C  CD2   . TYR   B  1  446  ? -20.578 5.148   110.516 1.00 33.84 ? 444  TYR   B CD2   1 
ATOM   12236 C  CE1   . TYR   B  1  446  ? -21.101 7.806   111.046 1.00 38.00 ? 444  TYR   B CE1   1 
ATOM   12237 C  CE2   . TYR   B  1  446  ? -21.876 5.562   110.744 1.00 37.53 ? 444  TYR   B CE2   1 
ATOM   12238 C  CZ    . TYR   B  1  446  ? -22.131 6.894   111.005 1.00 35.93 ? 444  TYR   B CZ    1 
ATOM   12239 O  OH    . TYR   B  1  446  ? -23.425 7.308   111.234 1.00 43.19 ? 444  TYR   B OH    1 
ATOM   12240 N  N     . GLU   B  1  447  ? -16.772 7.418   112.327 1.00 29.30 ? 445  GLU   B N     1 
ATOM   12241 C  CA    . GLU   B  1  447  ? -16.862 8.574   113.199 1.00 27.06 ? 445  GLU   B CA    1 
ATOM   12242 C  C     . GLU   B  1  447  ? -16.874 9.833   112.354 1.00 24.86 ? 445  GLU   B C     1 
ATOM   12243 O  O     . GLU   B  1  447  ? -16.546 9.817   111.164 1.00 25.62 ? 445  GLU   B O     1 
ATOM   12244 C  CB    . GLU   B  1  447  ? -15.700 8.622   114.198 1.00 26.04 ? 445  GLU   B CB    1 
ATOM   12245 C  CG    . GLU   B  1  447  ? -14.383 8.887   113.512 1.00 25.61 ? 445  GLU   B CG    1 
ATOM   12246 C  CD    . GLU   B  1  447  ? -13.213 8.835   114.460 1.00 26.22 ? 445  GLU   B CD    1 
ATOM   12247 O  OE1   . GLU   B  1  447  ? -13.396 8.395   115.613 1.00 26.43 ? 445  GLU   B OE1   1 
ATOM   12248 O  OE2   . GLU   B  1  447  ? -12.111 9.239   114.026 1.00 25.16 ? 445  GLU   B OE2   1 
ATOM   12249 N  N     . PHE   B  1  448  ? -17.268 10.930  112.974 1.00 25.93 ? 446  PHE   B N     1 
ATOM   12250 C  CA    . PHE   B  1  448  ? -17.019 12.236  112.402 1.00 24.16 ? 446  PHE   B CA    1 
ATOM   12251 C  C     . PHE   B  1  448  ? -15.721 12.799  112.975 1.00 22.79 ? 446  PHE   B C     1 
ATOM   12252 O  O     . PHE   B  1  448  ? -15.159 12.271  113.934 1.00 25.53 ? 446  PHE   B O     1 
ATOM   12253 C  CB    . PHE   B  1  448  ? -18.184 13.172  112.679 1.00 29.36 ? 446  PHE   B CB    1 
ATOM   12254 C  CG    . PHE   B  1  448  ? -19.452 12.734  112.034 1.00 29.15 ? 446  PHE   B CG    1 
ATOM   12255 C  CD1   . PHE   B  1  448  ? -19.719 13.071  110.719 1.00 31.37 ? 446  PHE   B CD1   1 
ATOM   12256 C  CD2   . PHE   B  1  448  ? -20.372 11.967  112.734 1.00 31.22 ? 446  PHE   B CD2   1 
ATOM   12257 C  CE1   . PHE   B  1  448  ? -20.885 12.658  110.109 1.00 30.48 ? 446  PHE   B CE1   1 
ATOM   12258 C  CE2   . PHE   B  1  448  ? -21.546 11.550  112.130 1.00 32.88 ? 446  PHE   B CE2   1 
ATOM   12259 C  CZ    . PHE   B  1  448  ? -21.800 11.899  110.818 1.00 30.29 ? 446  PHE   B CZ    1 
ATOM   12260 N  N     . GLN   B  1  449  ? -15.234 13.866  112.356 1.00 25.04 ? 447  GLN   B N     1 
ATOM   12261 C  CA    . GLN   B  1  449  ? -14.071 14.576  112.864 1.00 21.12 ? 447  GLN   B CA    1 
ATOM   12262 C  C     . GLN   B  1  449  ? -14.275 16.064  112.653 1.00 23.55 ? 447  GLN   B C     1 
ATOM   12263 O  O     . GLN   B  1  449  ? -15.003 16.490  111.751 1.00 23.66 ? 447  GLN   B O     1 
ATOM   12264 C  CB    . GLN   B  1  449  ? -12.754 14.137  112.201 1.00 21.53 ? 447  GLN   B CB    1 
ATOM   12265 C  CG    . GLN   B  1  449  ? -12.471 12.663  112.321 1.00 23.96 ? 447  GLN   B CG    1 
ATOM   12266 C  CD    . GLN   B  1  449  ? -11.014 12.357  112.144 1.00 21.87 ? 447  GLN   B CD    1 
ATOM   12267 O  OE1   . GLN   B  1  449  ? -10.275 13.187  111.647 1.00 25.23 ? 447  GLN   B OE1   1 
ATOM   12268 N  NE2   . GLN   B  1  449  ? -10.593 11.166  112.556 1.00 22.47 ? 447  GLN   B NE2   1 
ATOM   12269 N  N     . CYS   B  1  450  ? -13.624 16.853  113.497 1.00 24.52 ? 448  CYS   B N     1 
ATOM   12270 C  CA    . CYS   B  1  450  ? -13.677 18.297  113.368 1.00 21.94 ? 448  CYS   B CA    1 
ATOM   12271 C  C     . CYS   B  1  450  ? -12.377 18.875  113.898 1.00 20.30 ? 448  CYS   B C     1 
ATOM   12272 O  O     . CYS   B  1  450  ? -11.567 18.179  114.511 1.00 23.23 ? 448  CYS   B O     1 
ATOM   12273 C  CB    . CYS   B  1  450  ? -14.858 18.882  114.154 1.00 23.81 ? 448  CYS   B CB    1 
ATOM   12274 S  SG    . CYS   B  1  450  ? -14.696 18.815  115.963 1.00 26.87 ? 448  CYS   B SG    1 
ATOM   12275 N  N     . LEU   B  1  451  ? -12.214 20.169  113.681 1.00 24.10 ? 449  LEU   B N     1 
ATOM   12276 C  CA    . LEU   B  1  451  ? -11.045 20.891  114.147 1.00 24.91 ? 449  LEU   B CA    1 
ATOM   12277 C  C     . LEU   B  1  451  ? -11.327 21.470  115.523 1.00 27.01 ? 449  LEU   B C     1 
ATOM   12278 O  O     . LEU   B  1  451  ? -12.417 21.986  115.786 1.00 27.79 ? 449  LEU   B O     1 
ATOM   12279 C  CB    . LEU   B  1  451  ? -10.733 22.025  113.177 1.00 26.29 ? 449  LEU   B CB    1 
ATOM   12280 C  CG    . LEU   B  1  451  ? -9.428  22.797  113.342 1.00 31.32 ? 449  LEU   B CG    1 
ATOM   12281 C  CD1   . LEU   B  1  451  ? -8.222  21.857  113.436 1.00 27.25 ? 449  LEU   B CD1   1 
ATOM   12282 C  CD2   . LEU   B  1  451  ? -9.263  23.772  112.188 1.00 33.93 ? 449  LEU   B CD2   1 
ATOM   12283 N  N     . HIS   B  1  452  ? -10.344 21.356  116.409 1.00 24.22 ? 450  HIS   B N     1 
ATOM   12284 C  CA    . HIS   B  1  452  ? -10.428 21.995  117.710 1.00 28.03 ? 450  HIS   B CA    1 
ATOM   12285 C  C     . HIS   B  1  452  ? -10.721 23.478  117.548 1.00 27.71 ? 450  HIS   B C     1 
ATOM   12286 O  O     . HIS   B  1  452  ? -10.145 24.148  116.689 1.00 29.93 ? 450  HIS   B O     1 
ATOM   12287 C  CB    . HIS   B  1  452  ? -9.086  21.844  118.418 1.00 25.73 ? 450  HIS   B CB    1 
ATOM   12288 C  CG    . HIS   B  1  452  ? -8.983  22.669  119.657 1.00 26.37 ? 450  HIS   B CG    1 
ATOM   12289 N  ND1   . HIS   B  1  452  ? -9.473  22.245  120.872 1.00 28.78 ? 450  HIS   B ND1   1 
ATOM   12290 C  CD2   . HIS   B  1  452  ? -8.479  23.907  119.862 1.00 29.48 ? 450  HIS   B CD2   1 
ATOM   12291 C  CE1   . HIS   B  1  452  ? -9.260  23.181  121.780 1.00 31.18 ? 450  HIS   B CE1   1 
ATOM   12292 N  NE2   . HIS   B  1  452  ? -8.661  24.201  121.191 1.00 28.79 ? 450  HIS   B NE2   1 
ATOM   12293 N  N     . GLY   B  1  453  ? -11.621 23.990  118.389 1.00 31.40 ? 451  GLY   B N     1 
ATOM   12294 C  CA    . GLY   B  1  453  ? -11.891 25.415  118.394 1.00 40.61 ? 451  GLY   B CA    1 
ATOM   12295 C  C     . GLY   B  1  453  ? -12.594 25.924  117.161 1.00 43.88 ? 451  GLY   B C     1 
ATOM   12296 O  O     . GLY   B  1  453  ? -12.607 27.134  116.913 1.00 44.30 ? 451  GLY   B O     1 
ATOM   12297 N  N     . MET   B  1  454  ? -13.158 25.025  116.362 1.00 35.40 ? 452  MET   B N     1 
ATOM   12298 C  CA    . MET   B  1  454  ? -13.970 25.401  115.217 1.00 34.25 ? 452  MET   B CA    1 
ATOM   12299 C  C     . MET   B  1  454  ? -15.181 24.485  115.163 1.00 35.86 ? 452  MET   B C     1 
ATOM   12300 O  O     . MET   B  1  454  ? -16.313 24.943  114.972 1.00 37.29 ? 452  MET   B O     1 
ATOM   12301 C  CB    . MET   B  1  454  ? -13.167 25.253  113.926 1.00 33.17 ? 452  MET   B CB    1 
ATOM   12302 C  CG    . MET   B  1  454  ? -14.002 25.468  112.677 1.00 34.13 ? 452  MET   B CG    1 
ATOM   12303 S  SD    . MET   B  1  454  ? -14.814 27.072  112.723 1.00 41.58 ? 452  MET   B SD    1 
ATOM   12304 C  CE    . MET   B  1  454  ? -13.381 28.147  112.675 1.00 41.38 ? 452  MET   B CE    1 
ATOM   12305 N  N     . GLY   B  1  455  ? -14.947 23.189  115.352 1.00 27.24 ? 453  GLY   B N     1 
ATOM   12306 C  CA    . GLY   B  1  455  ? -15.972 22.191  115.153 1.00 28.66 ? 453  GLY   B CA    1 
ATOM   12307 C  C     . GLY   B  1  455  ? -16.850 21.894  116.342 1.00 33.54 ? 453  GLY   B C     1 
ATOM   12308 O  O     . GLY   B  1  455  ? -17.892 21.256  116.173 1.00 32.32 ? 453  GLY   B O     1 
ATOM   12309 N  N     . GLU   B  1  456  ? -16.463 22.327  117.545 1.00 36.38 ? 454  GLU   B N     1 
ATOM   12310 C  CA    . GLU   B  1  456  ? -17.232 21.966  118.737 1.00 36.77 ? 454  GLU   B CA    1 
ATOM   12311 C  C     . GLU   B  1  456  ? -18.676 22.446  118.710 1.00 35.94 ? 454  GLU   B C     1 
ATOM   12312 O  O     . GLU   B  1  456  ? -19.565 21.646  119.047 1.00 37.38 ? 454  GLU   B O     1 
ATOM   12313 C  CB    . GLU   B  1  456  ? -16.497 22.372  120.019 1.00 39.47 ? 454  GLU   B CB    1 
ATOM   12314 C  CG    . GLU   B  1  456  ? -15.217 21.600  120.272 1.00 40.28 ? 454  GLU   B CG    1 
ATOM   12315 C  CD    . GLU   B  1  456  ? -14.018 22.267  119.647 1.00 38.76 ? 454  GLU   B CD    1 
ATOM   12316 O  OE1   . GLU   B  1  456  ? -14.179 22.876  118.567 1.00 41.82 ? 454  GLU   B OE1   1 
ATOM   12317 O  OE2   . GLU   B  1  456  ? -12.920 22.199  120.243 1.00 36.91 ? 454  GLU   B OE2   1 
ATOM   12318 N  N     . PRO   B  1  457  ? -18.988 23.702  118.353 1.00 35.15 ? 455  PRO   B N     1 
ATOM   12319 C  CA    . PRO   B  1  457  ? -20.405 24.109  118.312 1.00 36.88 ? 455  PRO   B CA    1 
ATOM   12320 C  C     . PRO   B  1  457  ? -21.286 23.174  117.502 1.00 37.56 ? 455  PRO   B C     1 
ATOM   12321 O  O     . PRO   B  1  457  ? -22.383 22.809  117.948 1.00 39.97 ? 455  PRO   B O     1 
ATOM   12322 C  CB    . PRO   B  1  457  ? -20.336 25.517  117.710 1.00 34.48 ? 455  PRO   B CB    1 
ATOM   12323 C  CG    . PRO   B  1  457  ? -19.020 26.029  118.147 1.00 40.97 ? 455  PRO   B CG    1 
ATOM   12324 C  CD    . PRO   B  1  457  ? -18.094 24.845  118.095 1.00 40.02 ? 455  PRO   B CD    1 
ATOM   12325 N  N     . LEU   B  1  458  ? -20.830 22.771  116.317 1.00 35.69 ? 456  LEU   B N     1 
ATOM   12326 C  CA    . LEU   B  1  458  ? -21.595 21.809  115.534 1.00 35.68 ? 456  LEU   B CA    1 
ATOM   12327 C  C     . LEU   B  1  458  ? -21.643 20.460  116.234 1.00 33.11 ? 456  LEU   B C     1 
ATOM   12328 O  O     . LEU   B  1  458  ? -22.716 19.873  116.416 1.00 34.35 ? 456  LEU   B O     1 
ATOM   12329 C  CB    . LEU   B  1  458  ? -20.985 21.668  114.140 1.00 32.79 ? 456  LEU   B CB    1 
ATOM   12330 C  CG    . LEU   B  1  458  ? -21.690 20.672  113.219 1.00 32.58 ? 456  LEU   B CG    1 
ATOM   12331 C  CD1   . LEU   B  1  458  ? -23.156 21.044  113.058 1.00 35.59 ? 456  LEU   B CD1   1 
ATOM   12332 C  CD2   . LEU   B  1  458  ? -21.012 20.623  111.861 1.00 33.80 ? 456  LEU   B CD2   1 
ATOM   12333 N  N     . TYR   B  1  459  ? -20.490 19.958  116.657 1.00 30.48 ? 457  TYR   B N     1 
ATOM   12334 C  CA    . TYR   B  1  459  ? -20.446 18.594  117.154 1.00 29.48 ? 457  TYR   B CA    1 
ATOM   12335 C  C     . TYR   B  1  459  ? -20.931 18.450  118.589 1.00 31.68 ? 457  TYR   B C     1 
ATOM   12336 O  O     . TYR   B  1  459  ? -21.185 17.324  119.020 1.00 30.44 ? 457  TYR   B O     1 
ATOM   12337 C  CB    . TYR   B  1  459  ? -19.067 17.982  116.925 1.00 32.71 ? 457  TYR   B CB    1 
ATOM   12338 C  CG    . TYR   B  1  459  ? -18.919 17.617  115.479 1.00 29.15 ? 457  TYR   B CG    1 
ATOM   12339 C  CD1   . TYR   B  1  459  ? -19.460 16.435  114.992 1.00 28.00 ? 457  TYR   B CD1   1 
ATOM   12340 C  CD2   . TYR   B  1  459  ? -18.300 18.478  114.581 1.00 29.19 ? 457  TYR   B CD2   1 
ATOM   12341 C  CE1   . TYR   B  1  459  ? -19.359 16.106  113.655 1.00 28.01 ? 457  TYR   B CE1   1 
ATOM   12342 C  CE2   . TYR   B  1  459  ? -18.192 18.153  113.234 1.00 30.69 ? 457  TYR   B CE2   1 
ATOM   12343 C  CZ    . TYR   B  1  459  ? -18.725 16.963  112.781 1.00 26.03 ? 457  TYR   B CZ    1 
ATOM   12344 O  OH    . TYR   B  1  459  ? -18.624 16.628  111.445 1.00 28.33 ? 457  TYR   B OH    1 
ATOM   12345 N  N     . GLU   B  1  460  ? -21.079 19.554  119.323 1.00 33.79 ? 458  GLU   B N     1 
ATOM   12346 C  CA    . GLU   B  1  460  ? -21.846 19.505  120.560 1.00 36.92 ? 458  GLU   B CA    1 
ATOM   12347 C  C     . GLU   B  1  460  ? -23.296 19.134  120.293 1.00 40.86 ? 458  GLU   B C     1 
ATOM   12348 O  O     . GLU   B  1  460  ? -23.991 18.681  121.212 1.00 37.99 ? 458  GLU   B O     1 
ATOM   12349 C  CB    . GLU   B  1  460  ? -21.760 20.847  121.289 1.00 37.36 ? 458  GLU   B CB    1 
ATOM   12350 N  N     . GLU   B  1  461  ? -23.765 19.318  119.058 1.00 37.36 ? 459  GLU   B N     1 
ATOM   12351 C  CA    . GLU   B  1  461  ? -25.104 18.916  118.653 1.00 39.35 ? 459  GLU   B CA    1 
ATOM   12352 C  C     . GLU   B  1  461  ? -25.145 17.515  118.060 1.00 40.82 ? 459  GLU   B C     1 
ATOM   12353 O  O     . GLU   B  1  461  ? -26.199 17.089  117.576 1.00 37.00 ? 459  GLU   B O     1 
ATOM   12354 C  CB    . GLU   B  1  461  ? -25.683 19.922  117.656 1.00 38.41 ? 459  GLU   B CB    1 
ATOM   12355 C  CG    . GLU   B  1  461  ? -25.527 21.371  118.073 1.00 36.04 ? 459  GLU   B CG    1 
ATOM   12356 C  CD    . GLU   B  1  461  ? -26.242 21.684  119.375 1.00 47.04 ? 459  GLU   B CD    1 
ATOM   12357 O  OE1   . GLU   B  1  461  ? -27.142 20.910  119.763 1.00 48.49 ? 459  GLU   B OE1   1 
ATOM   12358 O  OE2   . GLU   B  1  461  ? -25.903 22.706  120.008 1.00 51.03 ? 459  GLU   B OE2   1 
ATOM   12359 N  N     . VAL   B  1  462  ? -24.028 16.792  118.088 1.00 37.73 ? 460  VAL   B N     1 
ATOM   12360 C  CA    . VAL   B  1  462  ? -23.905 15.486  117.452 1.00 34.36 ? 460  VAL   B CA    1 
ATOM   12361 C  C     . VAL   B  1  462  ? -23.527 14.411  118.459 1.00 36.00 ? 460  VAL   B C     1 
ATOM   12362 O  O     . VAL   B  1  462  ? -24.177 13.365  118.545 1.00 36.72 ? 460  VAL   B O     1 
ATOM   12363 C  CB    . VAL   B  1  462  ? -22.892 15.523  116.282 1.00 34.18 ? 460  VAL   B CB    1 
ATOM   12364 C  CG1   . VAL   B  1  462  ? -22.702 14.133  115.694 1.00 32.74 ? 460  VAL   B CG1   1 
ATOM   12365 C  CG2   . VAL   B  1  462  ? -23.353 16.508  115.230 1.00 32.72 ? 460  VAL   B CG2   1 
ATOM   12366 N  N     . VAL   B  1  463  ? -22.462 14.648  119.226 1.00 33.26 ? 461  VAL   B N     1 
ATOM   12367 C  CA    . VAL   B  1  463  ? -21.990 13.673  120.192 1.00 31.32 ? 461  VAL   B CA    1 
ATOM   12368 C  C     . VAL   B  1  463  ? -22.958 13.608  121.366 1.00 34.91 ? 461  VAL   B C     1 
ATOM   12369 O  O     . VAL   B  1  463  ? -23.466 14.634  121.837 1.00 39.18 ? 461  VAL   B O     1 
ATOM   12370 C  CB    . VAL   B  1  463  ? -20.570 14.045  120.653 1.00 31.21 ? 461  VAL   B CB    1 
ATOM   12371 C  CG1   . VAL   B  1  463  ? -20.039 13.009  121.619 1.00 32.71 ? 461  VAL   B CG1   1 
ATOM   12372 C  CG2   . VAL   B  1  463  ? -19.640 14.174  119.447 1.00 32.61 ? 461  VAL   B CG2   1 
ATOM   12373 N  N     . GLY   B  1  464  ? -23.220 12.403  121.837 1.00 36.73 ? 462  GLY   B N     1 
ATOM   12374 C  CA    . GLY   B  1  464  ? -24.027 12.253  123.035 1.00 37.45 ? 462  GLY   B CA    1 
ATOM   12375 C  C     . GLY   B  1  464  ? -25.361 11.599  122.739 1.00 43.41 ? 462  GLY   B C     1 
ATOM   12376 O  O     . GLY   B  1  464  ? -25.965 11.822  121.684 1.00 39.75 ? 462  GLY   B O     1 
ATOM   12377 N  N     . ARG   B  1  465  ? -25.824 10.779  123.684 1.00 44.09 ? 463  ARG   B N     1 
ATOM   12378 C  CA    . ARG   B  1  465  ? -27.129 10.146  123.547 1.00 45.13 ? 463  ARG   B CA    1 
ATOM   12379 C  C     . ARG   B  1  465  ? -28.241 11.176  123.373 1.00 46.81 ? 463  ARG   B C     1 
ATOM   12380 O  O     . ARG   B  1  465  ? -29.230 10.913  122.677 1.00 50.36 ? 463  ARG   B O     1 
ATOM   12381 C  CB    . ARG   B  1  465  ? -27.405 9.258   124.759 1.00 49.09 ? 463  ARG   B CB    1 
ATOM   12382 N  N     . GLY   B  1  466  ? -28.091 12.355  123.979 1.00 44.14 ? 464  GLY   B N     1 
ATOM   12383 C  CA    . GLY   B  1  466  ? -29.075 13.414  123.856 1.00 46.01 ? 464  GLY   B CA    1 
ATOM   12384 C  C     . GLY   B  1  466  ? -29.079 14.138  122.533 1.00 48.23 ? 464  GLY   B C     1 
ATOM   12385 O  O     . GLY   B  1  466  ? -29.952 14.984  122.303 1.00 44.92 ? 464  GLY   B O     1 
ATOM   12386 N  N     . LYS   B  1  467  ? -28.120 13.834  121.663 1.00 43.09 ? 465  LYS   B N     1 
ATOM   12387 C  CA    . LYS   B  1  467  ? -28.041 14.453  120.348 1.00 40.34 ? 465  LYS   B CA    1 
ATOM   12388 C  C     . LYS   B  1  467  ? -28.154 13.376  119.276 1.00 45.93 ? 465  LYS   B C     1 
ATOM   12389 O  O     . LYS   B  1  467  ? -29.082 12.559  119.306 1.00 41.81 ? 465  LYS   B O     1 
ATOM   12390 C  CB    . LYS   B  1  467  ? -26.728 15.224  120.211 1.00 42.40 ? 465  LYS   B CB    1 
ATOM   12391 C  CG    . LYS   B  1  467  ? -26.486 16.231  121.325 1.00 44.89 ? 465  LYS   B CG    1 
ATOM   12392 C  CD    . LYS   B  1  467  ? -27.444 17.407  121.238 1.00 48.58 ? 465  LYS   B CD    1 
ATOM   12393 C  CE    . LYS   B  1  467  ? -27.212 18.388  122.379 1.00 50.67 ? 465  LYS   B CE    1 
ATOM   12394 N  NZ    . LYS   B  1  467  ? -27.885 19.696  122.141 1.00 52.37 ? 465  LYS   B NZ    1 
ATOM   12395 N  N     . LEU   B  1  468  ? -27.214 13.358  118.327 1.00 40.31 ? 466  LEU   B N     1 
ATOM   12396 C  CA    . LEU   B  1  468  ? -27.245 12.341  117.282 1.00 39.33 ? 466  LEU   B CA    1 
ATOM   12397 C  C     . LEU   B  1  468  ? -26.572 11.044  117.704 1.00 33.60 ? 466  LEU   B C     1 
ATOM   12398 O  O     . LEU   B  1  468  ? -26.662 10.050  116.975 1.00 36.03 ? 466  LEU   B O     1 
ATOM   12399 C  CB    . LEU   B  1  468  ? -26.628 12.872  115.986 1.00 40.79 ? 466  LEU   B CB    1 
ATOM   12400 C  CG    . LEU   B  1  468  ? -27.266 14.161  115.461 1.00 41.38 ? 466  LEU   B CG    1 
ATOM   12401 C  CD1   . LEU   B  1  468  ? -26.719 14.537  114.097 1.00 42.69 ? 466  LEU   B CD1   1 
ATOM   12402 C  CD2   . LEU   B  1  468  ? -28.790 14.030  115.426 1.00 40.94 ? 466  LEU   B CD2   1 
ATOM   12403 N  N     . ASP   B  1  469  ? -25.903 11.031  118.855 1.00 36.04 ? 467  ASP   B N     1 
ATOM   12404 C  CA    . ASP   B  1  469  ? -25.250 9.831   119.373 1.00 39.81 ? 467  ASP   B CA    1 
ATOM   12405 C  C     . ASP   B  1  469  ? -24.194 9.305   118.408 1.00 36.32 ? 467  ASP   B C     1 
ATOM   12406 O  O     . ASP   B  1  469  ? -24.085 8.099   118.173 1.00 35.32 ? 467  ASP   B O     1 
ATOM   12407 C  CB    . ASP   B  1  469  ? -26.255 8.744   119.758 1.00 42.30 ? 467  ASP   B CB    1 
ATOM   12408 C  CG    . ASP   B  1  469  ? -25.696 7.776   120.770 1.00 44.19 ? 467  ASP   B CG    1 
ATOM   12409 O  OD1   . ASP   B  1  469  ? -24.666 8.110   121.395 1.00 44.01 ? 467  ASP   B OD1   1 
ATOM   12410 O  OD2   . ASP   B  1  469  ? -26.280 6.685   120.940 1.00 52.03 ? 467  ASP   B OD2   1 
ATOM   12411 N  N     . ARG   B  1  470  ? -23.412 10.224  117.849 1.00 39.90 ? 468  ARG   B N     1 
ATOM   12412 C  CA    . ARG   B  1  470  ? -22.336 9.895   116.932 1.00 32.46 ? 468  ARG   B CA    1 
ATOM   12413 C  C     . ARG   B  1  470  ? -21.035 10.498  117.441 1.00 33.58 ? 468  ARG   B C     1 
ATOM   12414 O  O     . ARG   B  1  470  ? -21.004 11.670  117.842 1.00 32.57 ? 468  ARG   B O     1 
ATOM   12415 C  CB    . ARG   B  1  470  ? -22.624 10.435  115.522 1.00 34.03 ? 468  ARG   B CB    1 
ATOM   12416 C  CG    . ARG   B  1  470  ? -23.837 9.796   114.864 1.00 32.58 ? 468  ARG   B CG    1 
ATOM   12417 C  CD    . ARG   B  1  470  ? -23.663 8.294   114.746 1.00 30.64 ? 468  ARG   B CD    1 
ATOM   12418 N  NE    . ARG   B  1  470  ? -24.818 7.650   114.127 1.00 36.24 ? 468  ARG   B NE    1 
ATOM   12419 C  CZ    . ARG   B  1  470  ? -25.841 7.139   114.800 1.00 37.66 ? 468  ARG   B CZ    1 
ATOM   12420 N  NH1   . ARG   B  1  470  ? -25.899 7.195   116.122 1.00 34.99 ? 468  ARG   B NH1   1 
ATOM   12421 N  NH2   . ARG   B  1  470  ? -26.830 6.551   114.130 1.00 40.02 ? 468  ARG   B NH2   1 
ATOM   12422 N  N     . PRO   B  1  471  ? -19.950 9.737   117.423 1.00 30.46 ? 469  PRO   B N     1 
ATOM   12423 C  CA    . PRO   B  1  471  ? -18.684 10.240  117.953 1.00 31.78 ? 469  PRO   B CA    1 
ATOM   12424 C  C     . PRO   B  1  471  ? -18.018 11.204  116.988 1.00 29.22 ? 469  PRO   B C     1 
ATOM   12425 O  O     . PRO   B  1  471  ? -18.242 11.188  115.775 1.00 26.57 ? 469  PRO   B O     1 
ATOM   12426 C  CB    . PRO   B  1  471  ? -17.845 8.968   118.097 1.00 29.69 ? 469  PRO   B CB    1 
ATOM   12427 C  CG    . PRO   B  1  471  ? -18.347 8.096   117.024 1.00 32.24 ? 469  PRO   B CG    1 
ATOM   12428 C  CD    . PRO   B  1  471  ? -19.828 8.350   116.962 1.00 32.45 ? 469  PRO   B CD    1 
ATOM   12429 N  N     . CYS   B  1  472  ? -17.172 12.050  117.560 1.00 29.28 ? 470  CYS   B N     1 
ATOM   12430 C  CA    . CYS   B  1  472  ? -16.393 12.994  116.783 1.00 25.99 ? 470  CYS   B CA    1 
ATOM   12431 C  C     . CYS   B  1  472  ? -14.980 13.022  117.343 1.00 23.37 ? 470  CYS   B C     1 
ATOM   12432 O  O     . CYS   B  1  472  ? -14.796 13.131  118.562 1.00 27.62 ? 470  CYS   B O     1 
ATOM   12433 C  CB    . CYS   B  1  472  ? -17.004 14.395  116.835 1.00 29.23 ? 470  CYS   B CB    1 
ATOM   12434 S  SG    . CYS   B  1  472  ? -16.133 15.570  115.798 1.00 30.04 ? 470  CYS   B SG    1 
ATOM   12435 N  N     . ARG   B  1  473  ? -13.993 12.886  116.460 1.00 24.57 ? 471  ARG   B N     1 
ATOM   12436 C  CA    . ARG   B  1  473  ? -12.593 13.011  116.836 1.00 24.72 ? 471  ARG   B CA    1 
ATOM   12437 C  C     . ARG   B  1  473  ? -12.136 14.426  116.529 1.00 24.07 ? 471  ARG   B C     1 
ATOM   12438 O  O     . ARG   B  1  473  ? -12.287 14.906  115.400 1.00 24.54 ? 471  ARG   B O     1 
ATOM   12439 C  CB    . ARG   B  1  473  ? -11.719 12.011  116.085 1.00 23.12 ? 471  ARG   B CB    1 
ATOM   12440 C  CG    . ARG   B  1  473  ? -10.252 12.033  116.554 1.00 23.39 ? 471  ARG   B CG    1 
ATOM   12441 C  CD    . ARG   B  1  473  ? -9.457  10.909  115.911 1.00 23.83 ? 471  ARG   B CD    1 
ATOM   12442 N  NE    . ARG   B  1  473  ? -10.142 9.630   116.062 1.00 25.14 ? 471  ARG   B NE    1 
ATOM   12443 C  CZ    . ARG   B  1  473  ? -10.062 8.857   117.136 1.00 27.43 ? 471  ARG   B CZ    1 
ATOM   12444 N  NH1   . ARG   B  1  473  ? -9.260  9.157   118.146 1.00 24.43 ? 471  ARG   B NH1   1 
ATOM   12445 N  NH2   . ARG   B  1  473  ? -10.812 7.761   117.205 1.00 27.59 ? 471  ARG   B NH2   1 
ATOM   12446 N  N     . ILE   B  1  474  ? -11.574 15.084  117.533 1.00 24.92 ? 472  ILE   B N     1 
ATOM   12447 C  CA    . ILE   B  1  474  ? -11.149 16.469  117.406 1.00 23.20 ? 472  ILE   B CA    1 
ATOM   12448 C  C     . ILE   B  1  474  ? -9.695  16.487  116.965 1.00 24.70 ? 472  ILE   B C     1 
ATOM   12449 O  O     . ILE   B  1  474  ? -8.826  15.918  117.638 1.00 23.68 ? 472  ILE   B O     1 
ATOM   12450 C  CB    . ILE   B  1  474  ? -11.327 17.217  118.732 1.00 22.55 ? 472  ILE   B CB    1 
ATOM   12451 C  CG1   . ILE   B  1  474  ? -12.806 17.240  119.116 1.00 24.48 ? 472  ILE   B CG1   1 
ATOM   12452 C  CG2   . ILE   B  1  474  ? -10.777 18.612  118.614 1.00 24.73 ? 472  ILE   B CG2   1 
ATOM   12453 C  CD1   . ILE   B  1  474  ? -13.058 17.783  120.494 1.00 28.42 ? 472  ILE   B CD1   1 
ATOM   12454 N  N     . TYR   B  1  475  ? -9.438  17.123  115.831 1.00 22.43 ? 473  TYR   B N     1 
ATOM   12455 C  CA    . TYR   B  1  475  ? -8.079  17.363  115.370 1.00 22.38 ? 473  TYR   B CA    1 
ATOM   12456 C  C     . TYR   B  1  475  ? -7.517  18.500  116.203 1.00 23.71 ? 473  TYR   B C     1 
ATOM   12457 O  O     . TYR   B  1  475  ? -8.016  19.628  116.149 1.00 23.37 ? 473  TYR   B O     1 
ATOM   12458 C  CB    . TYR   B  1  475  ? -8.098  17.727  113.889 1.00 21.40 ? 473  TYR   B CB    1 
ATOM   12459 C  CG    . TYR   B  1  475  ? -6.743  17.757  113.233 1.00 22.60 ? 473  TYR   B CG    1 
ATOM   12460 C  CD1   . TYR   B  1  475  ? -5.975  18.915  113.240 1.00 23.21 ? 473  TYR   B CD1   1 
ATOM   12461 C  CD2   . TYR   B  1  475  ? -6.232  16.633  112.600 1.00 21.28 ? 473  TYR   B CD2   1 
ATOM   12462 C  CE1   . TYR   B  1  475  ? -4.731  18.957  112.629 1.00 23.45 ? 473  TYR   B CE1   1 
ATOM   12463 C  CE2   . TYR   B  1  475  ? -4.990  16.663  111.985 1.00 20.30 ? 473  TYR   B CE2   1 
ATOM   12464 C  CZ    . TYR   B  1  475  ? -4.247  17.827  112.011 1.00 21.50 ? 473  TYR   B CZ    1 
ATOM   12465 O  OH    . TYR   B  1  475  ? -3.011  17.881  111.411 1.00 24.34 ? 473  TYR   B OH    1 
ATOM   12466 N  N     . ALA   B  1  476  ? -6.495  18.203  116.991 1.00 22.01 ? 474  ALA   B N     1 
ATOM   12467 C  CA    . ALA   B  1  476  ? -6.065  19.102  118.058 1.00 25.90 ? 474  ALA   B CA    1 
ATOM   12468 C  C     . ALA   B  1  476  ? -4.648  19.597  117.818 1.00 23.33 ? 474  ALA   B C     1 
ATOM   12469 O  O     . ALA   B  1  476  ? -3.677  18.866  118.089 1.00 23.00 ? 474  ALA   B O     1 
ATOM   12470 C  CB    . ALA   B  1  476  ? -6.157  18.376  119.394 1.00 25.21 ? 474  ALA   B CB    1 
ATOM   12471 N  N     . PRO   B  1  477  ? -4.473  20.822  117.322 1.00 23.38 ? 475  PRO   B N     1 
ATOM   12472 C  CA    . PRO   B  1  477  ? -3.124  21.375  117.195 1.00 23.40 ? 475  PRO   B CA    1 
ATOM   12473 C  C     . PRO   B  1  477  ? -2.525  21.597  118.565 1.00 23.49 ? 475  PRO   B C     1 
ATOM   12474 O  O     . PRO   B  1  477  ? -3.210  22.004  119.504 1.00 23.82 ? 475  PRO   B O     1 
ATOM   12475 C  CB    . PRO   B  1  477  ? -3.353  22.713  116.486 1.00 26.38 ? 475  PRO   B CB    1 
ATOM   12476 C  CG    . PRO   B  1  477  ? -4.679  22.577  115.827 1.00 27.55 ? 475  PRO   B CG    1 
ATOM   12477 C  CD    . PRO   B  1  477  ? -5.490  21.702  116.725 1.00 25.63 ? 475  PRO   B CD    1 
ATOM   12478 N  N     . VAL   B  1  478  ? -1.232  21.330  118.669 1.00 22.28 ? 476  VAL   B N     1 
ATOM   12479 C  CA    . VAL   B  1  478  ? -0.496  21.461  119.913 1.00 23.29 ? 476  VAL   B CA    1 
ATOM   12480 C  C     . VAL   B  1  478  ? 0.786   22.198  119.593 1.00 26.19 ? 476  VAL   B C     1 
ATOM   12481 O  O     . VAL   B  1  478  ? 1.553   21.754  118.735 1.00 25.44 ? 476  VAL   B O     1 
ATOM   12482 C  CB    . VAL   B  1  478  ? -0.177  20.091  120.534 1.00 24.17 ? 476  VAL   B CB    1 
ATOM   12483 C  CG1   . VAL   B  1  478  ? 0.576   20.269  121.835 1.00 26.84 ? 476  VAL   B CG1   1 
ATOM   12484 C  CG2   . VAL   B  1  478  ? -1.460  19.286  120.759 1.00 23.10 ? 476  VAL   B CG2   1 
ATOM   12485 N  N     . GLY   B  1  479  ? 1.021   23.312  120.264 1.00 27.62 ? 477  GLY   B N     1 
ATOM   12486 C  CA    . GLY   B  1  479  ? 2.279   24.002  120.078 1.00 34.40 ? 477  GLY   B CA    1 
ATOM   12487 C  C     . GLY   B  1  479  ? 2.193   25.461  120.463 1.00 34.52 ? 477  GLY   B C     1 
ATOM   12488 O  O     . GLY   B  1  479  ? 1.167   25.955  120.929 1.00 30.44 ? 477  GLY   B O     1 
ATOM   12489 N  N     . THR   B  1  480  ? 3.308   26.145  120.221 1.00 38.19 ? 478  THR   B N     1 
ATOM   12490 C  CA    . THR   B  1  480  ? 3.528   27.504  120.685 1.00 43.03 ? 478  THR   B CA    1 
ATOM   12491 C  C     . THR   B  1  480  ? 2.827   28.505  119.770 1.00 47.29 ? 478  THR   B C     1 
ATOM   12492 O  O     . THR   B  1  480  ? 2.208   28.149  118.761 1.00 45.77 ? 478  THR   B O     1 
ATOM   12493 C  CB    . THR   B  1  480  ? 5.026   27.794  120.721 1.00 41.76 ? 478  THR   B CB    1 
ATOM   12494 O  OG1   . THR   B  1  480  ? 5.555   27.667  119.394 1.00 49.48 ? 478  THR   B OG1   1 
ATOM   12495 C  CG2   . THR   B  1  480  ? 5.736   26.813  121.633 1.00 41.16 ? 478  THR   B CG2   1 
ATOM   12496 N  N     . HIS   B  1  481  ? 2.947   29.786  120.122 1.00 50.16 ? 479  HIS   B N     1 
ATOM   12497 C  CA    . HIS   B  1  481  ? 2.337   30.844  119.322 1.00 49.70 ? 479  HIS   B CA    1 
ATOM   12498 C  C     . HIS   B  1  481  ? 3.002   30.958  117.956 1.00 53.71 ? 479  HIS   B C     1 
ATOM   12499 O  O     . HIS   B  1  481  ? 2.317   31.039  116.929 1.00 51.83 ? 479  HIS   B O     1 
ATOM   12500 C  CB    . HIS   B  1  481  ? 2.420   32.173  120.072 1.00 47.35 ? 479  HIS   B CB    1 
ATOM   12501 C  CG    . HIS   B  1  481  ? 1.644   32.192  121.350 1.00 47.39 ? 479  HIS   B CG    1 
ATOM   12502 N  ND1   . HIS   B  1  481  ? 1.631   33.279  122.199 1.00 51.86 ? 479  HIS   B ND1   1 
ATOM   12503 C  CD2   . HIS   B  1  481  ? 0.852   31.256  121.926 1.00 46.54 ? 479  HIS   B CD2   1 
ATOM   12504 C  CE1   . HIS   B  1  481  ? 0.866   33.012  123.243 1.00 52.10 ? 479  HIS   B CE1   1 
ATOM   12505 N  NE2   . HIS   B  1  481  ? 0.380   31.791  123.101 1.00 53.09 ? 479  HIS   B NE2   1 
ATOM   12506 N  N     . GLU   B  1  482  ? 4.339   30.973  117.925 1.00 49.74 ? 480  GLU   B N     1 
ATOM   12507 C  CA    . GLU   B  1  482  ? 5.049   31.141  116.661 1.00 47.74 ? 480  GLU   B CA    1 
ATOM   12508 C  C     . GLU   B  1  482  ? 4.742   30.002  115.700 1.00 49.08 ? 480  GLU   B C     1 
ATOM   12509 O  O     . GLU   B  1  482  ? 4.599   30.218  114.490 1.00 51.28 ? 480  GLU   B O     1 
ATOM   12510 C  CB    . GLU   B  1  482  ? 6.554   31.246  116.913 1.00 48.66 ? 480  GLU   B CB    1 
ATOM   12511 N  N     . THR   B  1  483  ? 4.626   28.780  116.223 1.00 50.51 ? 481  THR   B N     1 
ATOM   12512 C  CA    . THR   B  1  483  ? 4.318   27.637  115.372 1.00 49.60 ? 481  THR   B CA    1 
ATOM   12513 C  C     . THR   B  1  483  ? 2.875   27.692  114.878 1.00 45.90 ? 481  THR   B C     1 
ATOM   12514 O  O     . THR   B  1  483  ? 2.610   27.498  113.685 1.00 49.81 ? 481  THR   B O     1 
ATOM   12515 C  CB    . THR   B  1  483  ? 4.593   26.336  116.130 1.00 49.87 ? 481  THR   B CB    1 
ATOM   12516 N  N     . LEU   B  1  484  ? 1.928   27.963  115.783 1.00 47.74 ? 482  LEU   B N     1 
ATOM   12517 C  CA    . LEU   B  1  484  ? 0.519   28.011  115.397 1.00 46.13 ? 482  LEU   B CA    1 
ATOM   12518 C  C     . LEU   B  1  484  ? 0.272   29.054  114.312 1.00 44.95 ? 482  LEU   B C     1 
ATOM   12519 O  O     . LEU   B  1  484  ? -0.499  28.818  113.373 1.00 47.97 ? 482  LEU   B O     1 
ATOM   12520 C  CB    . LEU   B  1  484  ? -0.349  28.293  116.624 1.00 43.37 ? 482  LEU   B CB    1 
ATOM   12521 N  N     . LEU   B  1  485  ? 0.933   30.210  114.413 1.00 45.19 ? 483  LEU   B N     1 
ATOM   12522 C  CA    . LEU   B  1  485  ? 0.684   31.295  113.469 1.00 49.41 ? 483  LEU   B CA    1 
ATOM   12523 C  C     . LEU   B  1  485  ? 1.093   30.929  112.049 1.00 47.46 ? 483  LEU   B C     1 
ATOM   12524 O  O     . LEU   B  1  485  ? 0.557   31.492  111.087 1.00 45.71 ? 483  LEU   B O     1 
ATOM   12525 C  CB    . LEU   B  1  485  ? 1.430   32.553  113.919 1.00 47.11 ? 483  LEU   B CB    1 
ATOM   12526 C  CG    . LEU   B  1  485  ? 0.808   33.348  115.065 1.00 42.95 ? 483  LEU   B CG    1 
ATOM   12527 C  CD1   . LEU   B  1  485  ? 1.828   34.316  115.633 1.00 45.15 ? 483  LEU   B CD1   1 
ATOM   12528 C  CD2   . LEU   B  1  485  ? -0.429  34.092  114.584 1.00 41.09 ? 483  LEU   B CD2   1 
ATOM   12529 N  N     . ALA   B  1  486  ? 2.027   29.989  111.894 1.00 45.74 ? 484  ALA   B N     1 
ATOM   12530 C  CA    . ALA   B  1  486  ? 2.659   29.722  110.604 1.00 40.93 ? 484  ALA   B CA    1 
ATOM   12531 C  C     . ALA   B  1  486  ? 1.716   29.131  109.555 1.00 46.42 ? 484  ALA   B C     1 
ATOM   12532 O  O     . ALA   B  1  486  ? 2.147   28.959  108.408 1.00 48.74 ? 484  ALA   B O     1 
ATOM   12533 C  CB    . ALA   B  1  486  ? 3.883   28.824  110.792 1.00 44.06 ? 484  ALA   B CB    1 
ATOM   12534 N  N     . TYR   B  1  487  ? 0.463   28.822  109.895 1.00 49.85 ? 485  TYR   B N     1 
ATOM   12535 C  CA    . TYR   B  1  487  ? -0.476  28.283  108.916 1.00 45.03 ? 485  TYR   B CA    1 
ATOM   12536 C  C     . TYR   B  1  487  ? -1.909  28.372  109.424 1.00 47.29 ? 485  TYR   B C     1 
ATOM   12537 O  O     . TYR   B  1  487  ? -2.788  27.648  108.943 1.00 43.14 ? 485  TYR   B O     1 
ATOM   12538 C  CB    . TYR   B  1  487  ? -0.122  26.835  108.567 1.00 39.89 ? 485  TYR   B CB    1 
ATOM   12539 N  N     . LEU   B  1  488  ? -2.149  29.279  110.378 1.00 55.50 ? 486  LEU   B N     1 
ATOM   12540 C  CA    . LEU   B  1  488  ? -3.450  29.491  111.014 1.00 56.01 ? 486  LEU   B CA    1 
ATOM   12541 C  C     . LEU   B  1  488  ? -4.568  29.784  110.019 1.00 57.90 ? 486  LEU   B C     1 
ATOM   12542 O  O     . LEU   B  1  488  ? -5.743  29.797  110.408 1.00 61.37 ? 486  LEU   B O     1 
ATOM   12543 C  CB    . LEU   B  1  488  ? -3.312  30.670  111.977 1.00 53.64 ? 486  LEU   B CB    1 
ATOM   12544 C  CG    . LEU   B  1  488  ? -4.378  30.977  113.019 1.00 49.74 ? 486  LEU   B CG    1 
ATOM   12545 C  CD1   . LEU   B  1  488  ? -3.669  31.474  114.243 1.00 52.24 ? 486  LEU   B CD1   1 
ATOM   12546 C  CD2   . LEU   B  1  488  ? -5.356  32.026  112.522 1.00 52.54 ? 486  LEU   B CD2   1 
ATOM   12547 N  N     . VAL   B  1  489  ? -4.228  30.024  108.755 1.00 56.18 ? 487  VAL   B N     1 
ATOM   12548 C  CA    . VAL   B  1  489  ? -5.206  30.305  107.718 1.00 55.59 ? 487  VAL   B CA    1 
ATOM   12549 C  C     . VAL   B  1  489  ? -6.176  29.143  107.508 1.00 54.07 ? 487  VAL   B C     1 
ATOM   12550 O  O     . VAL   B  1  489  ? -7.284  29.346  106.997 1.00 51.61 ? 487  VAL   B O     1 
ATOM   12551 C  CB    . VAL   B  1  489  ? -4.405  30.675  106.454 1.00 50.14 ? 487  VAL   B CB    1 
ATOM   12552 C  CG1   . VAL   B  1  489  ? -5.307  30.973  105.293 1.00 58.25 ? 487  VAL   B CG1   1 
ATOM   12553 C  CG2   . VAL   B  1  489  ? -3.503  31.870  106.743 1.00 49.85 ? 487  VAL   B CG2   1 
ATOM   12554 N  N     . ARG   B  1  490  ? -5.802  27.930  107.920 1.00 39.28 ? 488  ARG   B N     1 
ATOM   12555 C  CA    . ARG   B  1  490  ? -6.658  26.773  107.685 1.00 43.58 ? 488  ARG   B CA    1 
ATOM   12556 C  C     . ARG   B  1  490  ? -7.906  26.797  108.560 1.00 42.24 ? 488  ARG   B C     1 
ATOM   12557 O  O     . ARG   B  1  490  ? -9.004  26.486  108.084 1.00 39.99 ? 488  ARG   B O     1 
ATOM   12558 C  CB    . ARG   B  1  490  ? -5.862  25.485  107.881 1.00 41.43 ? 488  ARG   B CB    1 
ATOM   12559 C  CG    . ARG   B  1  490  ? -4.791  25.318  106.826 1.00 37.52 ? 488  ARG   B CG    1 
ATOM   12560 C  CD    . ARG   B  1  490  ? -3.936  24.097  107.056 1.00 36.43 ? 488  ARG   B CD    1 
ATOM   12561 N  NE    . ARG   B  1  490  ? -2.945  23.984  105.992 1.00 34.56 ? 488  ARG   B NE    1 
ATOM   12562 C  CZ    . ARG   B  1  490  ? -1.746  23.436  106.142 1.00 31.90 ? 488  ARG   B CZ    1 
ATOM   12563 N  NH1   . ARG   B  1  490  ? -1.361  22.929  107.300 1.00 31.88 ? 488  ARG   B NH1   1 
ATOM   12564 N  NH2   . ARG   B  1  490  ? -0.911  23.410  105.107 1.00 33.34 ? 488  ARG   B NH2   1 
ATOM   12565 N  N     . ARG   B  1  491  ? -7.765  27.158  109.838 1.00 42.73 ? 489  ARG   B N     1 
ATOM   12566 C  CA    . ARG   B  1  491  ? -8.935  27.213  110.710 1.00 41.06 ? 489  ARG   B CA    1 
ATOM   12567 C  C     . ARG   B  1  491  ? -10.003 28.152  110.162 1.00 44.86 ? 489  ARG   B C     1 
ATOM   12568 O  O     . ARG   B  1  491  ? -11.200 27.892  110.335 1.00 44.36 ? 489  ARG   B O     1 
ATOM   12569 C  CB    . ARG   B  1  491  ? -8.530  27.633  112.125 1.00 40.36 ? 489  ARG   B CB    1 
ATOM   12570 N  N     . LEU   B  1  492  ? -9.596  29.226  109.479 1.00 47.57 ? 490  LEU   B N     1 
ATOM   12571 C  CA    . LEU   B  1  492  ? -10.512 30.271  109.033 1.00 47.85 ? 490  LEU   B CA    1 
ATOM   12572 C  C     . LEU   B  1  492  ? -10.769 30.241  107.531 1.00 42.15 ? 490  LEU   B C     1 
ATOM   12573 O  O     . LEU   B  1  492  ? -11.925 30.134  107.114 1.00 55.26 ? 490  LEU   B O     1 
ATOM   12574 C  CB    . LEU   B  1  492  ? -10.002 31.654  109.468 1.00 45.45 ? 490  LEU   B CB    1 
ATOM   12575 N  N     . LEU   B  1  493  ? -9.725  30.353  106.699 1.00 54.69 ? 491  LEU   B N     1 
ATOM   12576 C  CA    . LEU   B  1  493  ? -9.949  30.408  105.254 1.00 47.75 ? 491  LEU   B CA    1 
ATOM   12577 C  C     . LEU   B  1  493  ? -10.705 29.184  104.762 1.00 50.65 ? 491  LEU   B C     1 
ATOM   12578 O  O     . LEU   B  1  493  ? -11.420 29.258  103.756 1.00 50.54 ? 491  LEU   B O     1 
ATOM   12579 C  CB    . LEU   B  1  493  ? -8.635  30.587  104.495 1.00 49.98 ? 491  LEU   B CB    1 
ATOM   12580 C  CG    . LEU   B  1  493  ? -8.750  31.391  103.200 1.00 46.72 ? 491  LEU   B CG    1 
ATOM   12581 C  CD1   . LEU   B  1  493  ? -9.376  32.760  103.483 1.00 41.47 ? 491  LEU   B CD1   1 
ATOM   12582 C  CD2   . LEU   B  1  493  ? -7.403  31.533  102.508 1.00 49.92 ? 491  LEU   B CD2   1 
ATOM   12583 N  N     . GLU   B  1  494  ? -10.569 28.061  105.459 1.00 50.82 ? 492  GLU   B N     1 
ATOM   12584 C  CA    . GLU   B  1  494  ? -11.487 26.945  105.292 1.00 52.09 ? 492  GLU   B CA    1 
ATOM   12585 C  C     . GLU   B  1  494  ? -12.601 27.110  106.314 1.00 45.59 ? 492  GLU   B C     1 
ATOM   12586 O  O     . GLU   B  1  494  ? -13.625 26.435  106.246 1.00 58.32 ? 492  GLU   B O     1 
ATOM   12587 C  CB    . GLU   B  1  494  ? -10.773 25.612  105.514 1.00 33.54 ? 492  GLU   B CB    1 
ATOM   12588 N  N     . ALA   B  1  497  ? -13.182 31.835  103.724 1.00 55.72 ? 495  ALA   B N     1 
ATOM   12589 C  CA    . ALA   B  1  497  ? -13.628 32.023  102.347 1.00 49.61 ? 495  ALA   B CA    1 
ATOM   12590 C  C     . ALA   B  1  497  ? -15.139 32.183  102.294 1.00 40.86 ? 495  ALA   B C     1 
ATOM   12591 O  O     . ALA   B  1  497  ? -15.859 31.533  103.049 1.00 46.39 ? 495  ALA   B O     1 
ATOM   12592 C  CB    . ALA   B  1  497  ? -13.193 30.852  101.481 1.00 42.00 ? 495  ALA   B CB    1 
ATOM   12593 N  N     . ASN   B  1  498  ? -15.610 33.042  101.385 1.00 44.34 ? 496  ASN   B N     1 
ATOM   12594 C  CA    . ASN   B  1  498  ? -17.040 33.324  101.289 1.00 46.23 ? 496  ASN   B CA    1 
ATOM   12595 C  C     . ASN   B  1  498  ? -17.850 32.056  101.045 1.00 45.74 ? 496  ASN   B C     1 
ATOM   12596 O  O     . ASN   B  1  498  ? -18.977 31.926  101.535 1.00 43.09 ? 496  ASN   B O     1 
ATOM   12597 C  CB    . ASN   B  1  498  ? -17.298 34.348  100.183 1.00 47.62 ? 496  ASN   B CB    1 
ATOM   12598 N  N     . SER   B  1  499  ? -17.293 31.109  100.294 1.00 40.57 ? 497  SER   B N     1 
ATOM   12599 C  CA    . SER   B  1  499  ? -17.993 29.876  99.959  1.00 37.68 ? 497  SER   B CA    1 
ATOM   12600 C  C     . SER   B  1  499  ? -17.985 28.859  101.090 1.00 37.13 ? 497  SER   B C     1 
ATOM   12601 O  O     . SER   B  1  499  ? -18.657 27.828  100.979 1.00 34.51 ? 497  SER   B O     1 
ATOM   12602 C  CB    . SER   B  1  499  ? -17.330 29.241  98.739  1.00 39.74 ? 497  SER   B CB    1 
ATOM   12603 O  OG    . SER   B  1  499  ? -15.936 29.107  98.964  1.00 38.89 ? 497  SER   B OG    1 
ATOM   12604 N  N     . SER   B  1  500  ? -17.234 29.105  102.158 1.00 37.56 ? 498  SER   B N     1 
ATOM   12605 C  CA    . SER   B  1  500  ? -17.105 28.122  103.220 1.00 35.87 ? 498  SER   B CA    1 
ATOM   12606 C  C     . SER   B  1  500  ? -18.280 28.213  104.184 1.00 40.23 ? 498  SER   B C     1 
ATOM   12607 O  O     . SER   B  1  500  ? -18.778 29.303  104.480 1.00 42.27 ? 498  SER   B O     1 
ATOM   12608 C  CB    . SER   B  1  500  ? -15.786 28.315  103.968 1.00 40.50 ? 498  SER   B CB    1 
ATOM   12609 O  OG    . SER   B  1  500  ? -15.682 29.630  104.487 1.00 46.76 ? 498  SER   B OG    1 
ATOM   12610 N  N     . PHE   B  1  501  ? -18.731 27.047  104.652 1.00 33.84 ? 499  PHE   B N     1 
ATOM   12611 C  CA    . PHE   B  1  501  ? -19.798 26.982  105.644 1.00 37.11 ? 499  PHE   B CA    1 
ATOM   12612 C  C     . PHE   B  1  501  ? -19.463 27.819  106.875 1.00 44.62 ? 499  PHE   B C     1 
ATOM   12613 O  O     . PHE   B  1  501  ? -20.335 28.497  107.429 1.00 47.47 ? 499  PHE   B O     1 
ATOM   12614 C  CB    . PHE   B  1  501  ? -20.032 25.519  106.031 1.00 36.54 ? 499  PHE   B CB    1 
ATOM   12615 C  CG    . PHE   B  1  501  ? -21.224 25.299  106.926 1.00 37.55 ? 499  PHE   B CG    1 
ATOM   12616 C  CD1   . PHE   B  1  501  ? -21.117 25.440  108.301 1.00 39.32 ? 499  PHE   B CD1   1 
ATOM   12617 C  CD2   . PHE   B  1  501  ? -22.445 24.924  106.390 1.00 35.98 ? 499  PHE   B CD2   1 
ATOM   12618 C  CE1   . PHE   B  1  501  ? -22.218 25.232  109.123 1.00 41.39 ? 499  PHE   B CE1   1 
ATOM   12619 C  CE2   . PHE   B  1  501  ? -23.549 24.714  107.205 1.00 38.47 ? 499  PHE   B CE2   1 
ATOM   12620 C  CZ    . PHE   B  1  501  ? -23.431 24.867  108.574 1.00 38.90 ? 499  PHE   B CZ    1 
ATOM   12621 N  N     . VAL   B  1  502  ? -18.198 27.798  107.307 1.00 48.48 ? 500  VAL   B N     1 
ATOM   12622 C  CA    . VAL   B  1  502  ? -17.812 28.511  108.522 1.00 53.44 ? 500  VAL   B CA    1 
ATOM   12623 C  C     . VAL   B  1  502  ? -17.920 30.026  108.369 1.00 54.10 ? 500  VAL   B C     1 
ATOM   12624 O  O     . VAL   B  1  502  ? -18.009 30.740  109.374 1.00 57.05 ? 500  VAL   B O     1 
ATOM   12625 C  CB    . VAL   B  1  502  ? -16.424 28.063  109.016 1.00 52.64 ? 500  VAL   B CB    1 
ATOM   12626 N  N     . HIS   B  1  503  ? -17.908 30.541  107.140 1.00 47.49 ? 501  HIS   B N     1 
ATOM   12627 C  CA    . HIS   B  1  503  ? -18.233 31.945  106.918 1.00 50.11 ? 501  HIS   B CA    1 
ATOM   12628 C  C     . HIS   B  1  503  ? -19.720 32.146  106.654 1.00 51.70 ? 501  HIS   B C     1 
ATOM   12629 O  O     . HIS   B  1  503  ? -20.295 33.154  107.081 1.00 49.47 ? 501  HIS   B O     1 
ATOM   12630 C  CB    . HIS   B  1  503  ? -17.420 32.507  105.749 1.00 51.33 ? 501  HIS   B CB    1 
ATOM   12631 C  CG    . HIS   B  1  503  ? -17.929 33.820  105.237 1.00 52.10 ? 501  HIS   B CG    1 
ATOM   12632 N  ND1   . HIS   B  1  503  ? -18.914 33.913  104.276 1.00 51.27 ? 501  HIS   B ND1   1 
ATOM   12633 C  CD2   . HIS   B  1  503  ? -17.593 35.093  105.554 1.00 53.86 ? 501  HIS   B CD2   1 
ATOM   12634 C  CE1   . HIS   B  1  503  ? -19.162 35.186  104.023 1.00 53.20 ? 501  HIS   B CE1   1 
ATOM   12635 N  NE2   . HIS   B  1  503  ? -18.372 35.923  104.785 1.00 54.18 ? 501  HIS   B NE2   1 
ATOM   12636 N  N     . ARG   B  1  504  ? -20.353 31.191  105.966 1.00 46.40 ? 502  ARG   B N     1 
ATOM   12637 C  CA    . ARG   B  1  504  ? -21.753 31.342  105.585 1.00 43.41 ? 502  ARG   B CA    1 
ATOM   12638 C  C     . ARG   B  1  504  ? -22.694 31.164  106.769 1.00 46.90 ? 502  ARG   B C     1 
ATOM   12639 O  O     . ARG   B  1  504  ? -23.766 31.777  106.799 1.00 48.14 ? 502  ARG   B O     1 
ATOM   12640 C  CB    . ARG   B  1  504  ? -22.096 30.354  104.475 1.00 42.58 ? 502  ARG   B CB    1 
ATOM   12641 C  CG    . ARG   B  1  504  ? -21.452 30.698  103.150 1.00 43.84 ? 502  ARG   B CG    1 
ATOM   12642 C  CD    . ARG   B  1  504  ? -21.388 29.494  102.230 1.00 40.80 ? 502  ARG   B CD    1 
ATOM   12643 N  NE    . ARG   B  1  504  ? -22.689 28.871  102.020 1.00 38.36 ? 502  ARG   B NE    1 
ATOM   12644 C  CZ    . ARG   B  1  504  ? -23.644 29.368  101.247 1.00 37.28 ? 502  ARG   B CZ    1 
ATOM   12645 N  NH1   . ARG   B  1  504  ? -23.518 30.551  100.665 1.00 40.84 ? 502  ARG   B NH1   1 
ATOM   12646 N  NH2   . ARG   B  1  504  ? -24.751 28.659  101.046 1.00 37.67 ? 502  ARG   B NH2   1 
ATOM   12647 N  N     . ILE   B  1  505  ? -22.323 30.327  107.741 1.00 42.65 ? 503  ILE   B N     1 
ATOM   12648 C  CA    . ILE   B  1  505  ? -23.151 30.142  108.928 1.00 48.21 ? 503  ILE   B CA    1 
ATOM   12649 C  C     . ILE   B  1  505  ? -23.328 31.445  109.695 1.00 48.65 ? 503  ILE   B C     1 
ATOM   12650 O  O     . ILE   B  1  505  ? -24.320 31.613  110.414 1.00 46.39 ? 503  ILE   B O     1 
ATOM   12651 C  CB    . ILE   B  1  505  ? -22.575 29.023  109.821 1.00 42.04 ? 503  ILE   B CB    1 
ATOM   12652 N  N     . ASN   B  1  506  ? -22.396 32.386  109.543 1.00 45.23 ? 504  ASN   B N     1 
ATOM   12653 C  CA    . ASN   B  1  506  ? -22.428 33.652  110.261 1.00 50.47 ? 504  ASN   B CA    1 
ATOM   12654 C  C     . ASN   B  1  506  ? -22.817 34.832  109.381 1.00 53.49 ? 504  ASN   B C     1 
ATOM   12655 O  O     . ASN   B  1  506  ? -22.770 35.975  109.844 1.00 55.29 ? 504  ASN   B O     1 
ATOM   12656 C  CB    . ASN   B  1  506  ? -21.085 33.912  110.945 1.00 53.73 ? 504  ASN   B CB    1 
ATOM   12657 C  CG    . ASN   B  1  506  ? -20.802 32.924  112.054 1.00 52.73 ? 504  ASN   B CG    1 
ATOM   12658 O  OD1   . ASN   B  1  506  ? -21.695 32.565  112.822 1.00 54.18 ? 504  ASN   B OD1   1 
ATOM   12659 N  ND2   . ASN   B  1  506  ? -19.558 32.469  112.139 1.00 54.86 ? 504  ASN   B ND2   1 
ATOM   12660 N  N     . ASP   B  1  507  ? -23.196 34.590  108.127 1.00 49.89 ? 505  ASP   B N     1 
ATOM   12661 C  CA    . ASP   B  1  507  ? -23.639 35.670  107.260 1.00 55.57 ? 505  ASP   B CA    1 
ATOM   12662 C  C     . ASP   B  1  507  ? -25.159 35.695  107.267 1.00 57.72 ? 505  ASP   B C     1 
ATOM   12663 O  O     . ASP   B  1  507  ? -25.786 34.785  106.703 1.00 57.27 ? 505  ASP   B O     1 
ATOM   12664 C  CB    . ASP   B  1  507  ? -23.116 35.464  105.840 1.00 53.92 ? 505  ASP   B CB    1 
ATOM   12665 C  CG    . ASP   B  1  507  ? -23.182 36.729  105.006 1.00 59.47 ? 505  ASP   B CG    1 
ATOM   12666 O  OD1   . ASP   B  1  507  ? -23.714 37.747  105.500 1.00 63.09 ? 505  ASP   B OD1   1 
ATOM   12667 O  OD2   . ASP   B  1  507  ? -22.697 36.708  103.855 1.00 66.34 ? 505  ASP   B OD2   1 
ATOM   12668 N  N     . PRO   B  1  508  ? -25.795 36.694  107.887 1.00 60.65 ? 506  PRO   B N     1 
ATOM   12669 C  CA    . PRO   B  1  508  ? -27.265 36.694  107.968 1.00 58.07 ? 506  PRO   B CA    1 
ATOM   12670 C  C     . PRO   B  1  508  ? -27.955 36.799  106.620 1.00 61.32 ? 506  PRO   B C     1 
ATOM   12671 O  O     . PRO   B  1  508  ? -29.146 36.476  106.525 1.00 64.80 ? 506  PRO   B O     1 
ATOM   12672 C  CB    . PRO   B  1  508  ? -27.576 37.910  108.855 1.00 63.60 ? 506  PRO   B CB    1 
ATOM   12673 C  CG    . PRO   B  1  508  ? -26.282 38.239  109.542 1.00 62.65 ? 506  PRO   B CG    1 
ATOM   12674 C  CD    . PRO   B  1  508  ? -25.203 37.849  108.581 1.00 59.26 ? 506  PRO   B CD    1 
ATOM   12675 N  N     . LYS   B  1  509  ? -27.252 37.244  105.578 1.00 62.31 ? 507  LYS   B N     1 
ATOM   12676 C  CA    . LYS   B  1  509  ? -27.818 37.254  104.235 1.00 62.56 ? 507  LYS   B CA    1 
ATOM   12677 C  C     . LYS   B  1  509  ? -28.006 35.853  103.670 1.00 64.62 ? 507  LYS   B C     1 
ATOM   12678 O  O     . LYS   B  1  509  ? -28.665 35.704  102.635 1.00 67.82 ? 507  LYS   B O     1 
ATOM   12679 C  CB    . LYS   B  1  509  ? -26.933 38.079  103.299 1.00 58.20 ? 507  LYS   B CB    1 
ATOM   12680 N  N     . VAL   B  1  510  ? -27.453 34.834  104.320 1.00 63.22 ? 508  VAL   B N     1 
ATOM   12681 C  CA    . VAL   B  1  510  ? -27.545 33.453  103.864 1.00 60.79 ? 508  VAL   B CA    1 
ATOM   12682 C  C     . VAL   B  1  510  ? -28.557 32.734  104.744 1.00 57.96 ? 508  VAL   B C     1 
ATOM   12683 O  O     . VAL   B  1  510  ? -28.338 32.575  105.950 1.00 59.10 ? 508  VAL   B O     1 
ATOM   12684 C  CB    . VAL   B  1  510  ? -26.175 32.760  103.922 1.00 55.42 ? 508  VAL   B CB    1 
ATOM   12685 C  CG1   . VAL   B  1  510  ? -26.256 31.380  103.292 1.00 54.39 ? 508  VAL   B CG1   1 
ATOM   12686 C  CG2   . VAL   B  1  510  ? -25.118 33.615  103.239 1.00 52.93 ? 508  VAL   B CG2   1 
ATOM   12687 N  N     . SER   B  1  511  ? -29.660 32.294  104.145 1.00 55.92 ? 509  SER   B N     1 
ATOM   12688 C  CA    . SER   B  1  511  ? -30.720 31.641  104.894 1.00 55.50 ? 509  SER   B CA    1 
ATOM   12689 C  C     . SER   B  1  511  ? -30.337 30.203  105.221 1.00 55.30 ? 509  SER   B C     1 
ATOM   12690 O  O     . SER   B  1  511  ? -29.409 29.630  104.641 1.00 53.44 ? 509  SER   B O     1 
ATOM   12691 C  CB    . SER   B  1  511  ? -32.012 31.622  104.080 1.00 58.15 ? 509  SER   B CB    1 
ATOM   12692 O  OG    . SER   B  1  511  ? -31.984 30.579  103.120 1.00 57.20 ? 509  SER   B OG    1 
ATOM   12693 N  N     . ILE   B  1  512  ? -31.081 29.615  106.161 1.00 48.92 ? 510  ILE   B N     1 
ATOM   12694 C  CA    . ILE   B  1  512  ? -30.893 28.200  106.468 1.00 49.85 ? 510  ILE   B CA    1 
ATOM   12695 C  C     . ILE   B  1  512  ? -31.333 27.331  105.296 1.00 54.60 ? 510  ILE   B C     1 
ATOM   12696 O  O     . ILE   B  1  512  ? -30.811 26.225  105.105 1.00 50.52 ? 510  ILE   B O     1 
ATOM   12697 C  CB    . ILE   B  1  512  ? -31.589 27.814  107.787 1.00 42.37 ? 510  ILE   B CB    1 
ATOM   12698 N  N     . ASP   B  1  513  ? -32.289 27.809  104.493 1.00 51.82 ? 511  ASP   B N     1 
ATOM   12699 C  CA    . ASP   B  1  513  ? -32.695 27.070  103.300 1.00 51.42 ? 511  ASP   B CA    1 
ATOM   12700 C  C     . ASP   B  1  513  ? -31.527 26.911  102.334 1.00 46.94 ? 511  ASP   B C     1 
ATOM   12701 O  O     . ASP   B  1  513  ? -31.292 25.821  101.800 1.00 47.42 ? 511  ASP   B O     1 
ATOM   12702 C  CB    . ASP   B  1  513  ? -33.871 27.770  102.615 1.00 54.53 ? 511  ASP   B CB    1 
ATOM   12703 C  CG    . ASP   B  1  513  ? -35.205 27.462  103.276 1.00 56.77 ? 511  ASP   B CG    1 
ATOM   12704 O  OD1   . ASP   B  1  513  ? -35.421 26.303  103.693 1.00 55.49 ? 511  ASP   B OD1   1 
ATOM   12705 O  OD2   . ASP   B  1  513  ? -36.044 28.381  103.374 1.00 65.50 ? 511  ASP   B OD2   1 
ATOM   12706 N  N     . GLU   B  1  514  ? -30.785 27.994  102.095 1.00 44.61 ? 512  GLU   B N     1 
ATOM   12707 C  CA    . GLU   B  1  514  ? -29.605 27.913  101.241 1.00 48.49 ? 512  GLU   B CA    1 
ATOM   12708 C  C     . GLU   B  1  514  ? -28.582 26.939  101.815 1.00 46.08 ? 512  GLU   B C     1 
ATOM   12709 O  O     . GLU   B  1  514  ? -28.021 26.111  101.089 1.00 45.33 ? 512  GLU   B O     1 
ATOM   12710 C  CB    . GLU   B  1  514  ? -28.987 29.301  101.075 1.00 45.14 ? 512  GLU   B CB    1 
ATOM   12711 C  CG    . GLU   B  1  514  ? -29.967 30.376  100.630 1.00 56.75 ? 512  GLU   B CG    1 
ATOM   12712 C  CD    . GLU   B  1  514  ? -29.323 31.746  100.534 1.00 59.71 ? 512  GLU   B CD    1 
ATOM   12713 O  OE1   . GLU   B  1  514  ? -28.214 31.840  99.968  1.00 64.26 ? 512  GLU   B OE1   1 
ATOM   12714 O  OE2   . GLU   B  1  514  ? -29.922 32.726  101.031 1.00 61.08 ? 512  GLU   B OE2   1 
ATOM   12715 N  N     . LEU   B  1  515  ? -28.339 27.014  103.126 1.00 44.85 ? 513  LEU   B N     1 
ATOM   12716 C  CA    . LEU   B  1  515  ? -27.347 26.142  103.749 1.00 39.76 ? 513  LEU   B CA    1 
ATOM   12717 C  C     . LEU   B  1  515  ? -27.758 24.677  103.688 1.00 42.58 ? 513  LEU   B C     1 
ATOM   12718 O  O     . LEU   B  1  515  ? -26.894 23.793  103.688 1.00 41.13 ? 513  LEU   B O     1 
ATOM   12719 C  CB    . LEU   B  1  515  ? -27.116 26.562  105.202 1.00 41.04 ? 513  LEU   B CB    1 
ATOM   12720 C  CG    . LEU   B  1  515  ? -26.478 27.927  105.453 1.00 42.57 ? 513  LEU   B CG    1 
ATOM   12721 C  CD1   . LEU   B  1  515  ? -26.486 28.235  106.941 1.00 45.93 ? 513  LEU   B CD1   1 
ATOM   12722 C  CD2   . LEU   B  1  515  ? -25.056 27.969  104.911 1.00 42.71 ? 513  LEU   B CD2   1 
ATOM   12723 N  N     . ILE   B  1  516  ? -29.065 24.395  103.639 1.00 38.87 ? 514  ILE   B N     1 
ATOM   12724 C  CA    . ILE   B  1  516  ? -29.547 23.017  103.601 1.00 37.40 ? 514  ILE   B CA    1 
ATOM   12725 C  C     . ILE   B  1  516  ? -29.690 22.483  102.182 1.00 36.79 ? 514  ILE   B C     1 
ATOM   12726 O  O     . ILE   B  1  516  ? -30.050 21.309  102.008 1.00 39.91 ? 514  ILE   B O     1 
ATOM   12727 C  CB    . ILE   B  1  516  ? -30.869 22.848  104.381 1.00 43.34 ? 514  ILE   B CB    1 
ATOM   12728 N  N     . ALA   B  1  517  ? -29.424 23.304  101.168 1.00 41.80 ? 515  ALA   B N     1 
ATOM   12729 C  CA    . ALA   B  1  517  ? -29.542 22.865  99.783  1.00 40.76 ? 515  ALA   B CA    1 
ATOM   12730 C  C     . ALA   B  1  517  ? -28.704 21.618  99.542  1.00 37.61 ? 515  ALA   B C     1 
ATOM   12731 O  O     . ALA   B  1  517  ? -27.547 21.538  99.968  1.00 37.86 ? 515  ALA   B O     1 
ATOM   12732 C  CB    . ALA   B  1  517  ? -29.093 23.985  98.846  1.00 38.97 ? 515  ALA   B CB    1 
ATOM   12733 N  N     . ASP   B  1  518  ? -29.307 20.634  98.874  1.00 40.42 ? 516  ASP   B N     1 
ATOM   12734 C  CA    . ASP   B  1  518  ? -28.649 19.372  98.575  1.00 38.09 ? 516  ASP   B CA    1 
ATOM   12735 C  C     . ASP   B  1  518  ? -27.714 19.578  97.390  1.00 34.09 ? 516  ASP   B C     1 
ATOM   12736 O  O     . ASP   B  1  518  ? -28.174 19.839  96.272  1.00 33.93 ? 516  ASP   B O     1 
ATOM   12737 C  CB    . ASP   B  1  518  ? -29.693 18.295  98.273  1.00 35.47 ? 516  ASP   B CB    1 
ATOM   12738 C  CG    . ASP   B  1  518  ? -29.085 16.907  98.122  1.00 39.15 ? 516  ASP   B CG    1 
ATOM   12739 O  OD1   . ASP   B  1  518  ? -27.841 16.785  98.085  1.00 36.59 ? 516  ASP   B OD1   1 
ATOM   12740 O  OD2   . ASP   B  1  518  ? -29.861 15.929  98.037  1.00 41.00 ? 516  ASP   B OD2   1 
ATOM   12741 N  N     . PRO   B  1  519  ? -26.399 19.481  97.592  1.00 30.55 ? 517  PRO   B N     1 
ATOM   12742 C  CA    . PRO   B  1  519  ? -25.478 19.648  96.459  1.00 34.89 ? 517  PRO   B CA    1 
ATOM   12743 C  C     . PRO   B  1  519  ? -25.701 18.626  95.363  1.00 29.06 ? 517  PRO   B C     1 
ATOM   12744 O  O     . PRO   B  1  519  ? -25.533 18.952  94.182  1.00 31.12 ? 517  PRO   B O     1 
ATOM   12745 C  CB    . PRO   B  1  519  ? -24.092 19.503  97.105  1.00 31.68 ? 517  PRO   B CB    1 
ATOM   12746 C  CG    . PRO   B  1  519  ? -24.337 18.747  98.359  1.00 32.43 ? 517  PRO   B CG    1 
ATOM   12747 C  CD    . PRO   B  1  519  ? -25.694 19.165  98.844  1.00 28.54 ? 517  PRO   B CD    1 
ATOM   12748 N  N     . VAL   B  1  520  ? -26.080 17.400  95.726  1.00 30.31 ? 518  VAL   B N     1 
ATOM   12749 C  CA    . VAL   B  1  520  ? -26.259 16.346  94.732  1.00 30.46 ? 518  VAL   B CA    1 
ATOM   12750 C  C     . VAL   B  1  520  ? -27.373 16.715  93.763  1.00 30.65 ? 518  VAL   B C     1 
ATOM   12751 O  O     . VAL   B  1  520  ? -27.207 16.644  92.540  1.00 30.71 ? 518  VAL   B O     1 
ATOM   12752 C  CB    . VAL   B  1  520  ? -26.522 14.996  95.418  1.00 33.11 ? 518  VAL   B CB    1 
ATOM   12753 C  CG1   . VAL   B  1  520  ? -26.520 13.868  94.392  1.00 35.41 ? 518  VAL   B CG1   1 
ATOM   12754 C  CG2   . VAL   B  1  520  ? -25.501 14.744  96.519  1.00 32.44 ? 518  VAL   B CG2   1 
ATOM   12755 N  N     . GLU   B  1  521  ? -28.519 17.137  94.296  1.00 33.36 ? 519  GLU   B N     1 
ATOM   12756 C  CA    . GLU   B  1  521  ? -29.639 17.473  93.429  1.00 34.61 ? 519  GLU   B CA    1 
ATOM   12757 C  C     . GLU   B  1  521  ? -29.403 18.770  92.670  1.00 33.68 ? 519  GLU   B C     1 
ATOM   12758 O  O     . GLU   B  1  521  ? -29.883 18.915  91.540  1.00 35.52 ? 519  GLU   B O     1 
ATOM   12759 C  CB    . GLU   B  1  521  ? -30.937 17.515  94.232  1.00 36.97 ? 519  GLU   B CB    1 
ATOM   12760 C  CG    . GLU   B  1  521  ? -31.276 16.184  94.878  1.00 36.73 ? 519  GLU   B CG    1 
ATOM   12761 C  CD    . GLU   B  1  521  ? -31.304 15.031  93.884  1.00 40.59 ? 519  GLU   B CD    1 
ATOM   12762 O  OE1   . GLU   B  1  521  ? -31.668 15.255  92.712  1.00 40.15 ? 519  GLU   B OE1   1 
ATOM   12763 O  OE2   . GLU   B  1  521  ? -30.962 13.894  94.280  1.00 47.41 ? 519  GLU   B OE2   1 
ATOM   12764 N  N     . VAL   B  1  522  ? -28.672 19.717  93.253  1.00 33.61 ? 520  VAL   B N     1 
ATOM   12765 C  CA    . VAL   B  1  522  ? -28.362 20.938  92.519  1.00 33.72 ? 520  VAL   B CA    1 
ATOM   12766 C  C     . VAL   B  1  522  ? -27.447 20.631  91.337  1.00 36.63 ? 520  VAL   B C     1 
ATOM   12767 O  O     . VAL   B  1  522  ? -27.677 21.105  90.217  1.00 35.79 ? 520  VAL   B O     1 
ATOM   12768 C  CB    . VAL   B  1  522  ? -27.788 22.020  93.451  1.00 37.68 ? 520  VAL   B CB    1 
ATOM   12769 C  CG1   . VAL   B  1  522  ? -27.343 23.232  92.643  1.00 36.19 ? 520  VAL   B CG1   1 
ATOM   12770 C  CG2   . VAL   B  1  522  ? -28.824 22.423  94.490  1.00 40.42 ? 520  VAL   B CG2   1 
ATOM   12771 N  N     . VAL   B  1  523  ? -26.405 19.823  91.563  1.00 30.48 ? 521  VAL   B N     1 
ATOM   12772 C  CA    . VAL   B  1  523  ? -25.524 19.426  90.465  1.00 30.49 ? 521  VAL   B CA    1 
ATOM   12773 C  C     . VAL   B  1  523  ? -26.292 18.651  89.400  1.00 31.87 ? 521  VAL   B C     1 
ATOM   12774 O  O     . VAL   B  1  523  ? -26.122 18.891  88.199  1.00 30.49 ? 521  VAL   B O     1 
ATOM   12775 C  CB    . VAL   B  1  523  ? -24.309 18.641  90.989  1.00 32.44 ? 521  VAL   B CB    1 
ATOM   12776 C  CG1   . VAL   B  1  523  ? -23.596 17.961  89.842  1.00 33.21 ? 521  VAL   B CG1   1 
ATOM   12777 C  CG2   . VAL   B  1  523  ? -23.356 19.573  91.711  1.00 33.14 ? 521  VAL   B CG2   1 
ATOM   12778 N  N     . ARG   B  1  524  ? -27.136 17.704  89.819  1.00 33.07 ? 522  ARG   B N     1 
ATOM   12779 C  CA    . ARG   B  1  524  ? -27.860 16.880  88.855  1.00 35.42 ? 522  ARG   B CA    1 
ATOM   12780 C  C     . ARG   B  1  524  ? -28.708 17.727  87.916  1.00 36.12 ? 522  ARG   B C     1 
ATOM   12781 O  O     . ARG   B  1  524  ? -28.909 17.355  86.753  1.00 36.51 ? 522  ARG   B O     1 
ATOM   12782 C  CB    . ARG   B  1  524  ? -28.740 15.868  89.588  1.00 36.76 ? 522  ARG   B CB    1 
ATOM   12783 C  CG    . ARG   B  1  524  ? -29.474 14.902  88.670  1.00 35.67 ? 522  ARG   B CG    1 
ATOM   12784 C  CD    . ARG   B  1  524  ? -30.662 14.264  89.376  1.00 39.07 ? 522  ARG   B CD    1 
ATOM   12785 N  NE    . ARG   B  1  524  ? -30.308 13.782  90.705  1.00 39.37 ? 522  ARG   B NE    1 
ATOM   12786 C  CZ    . ARG   B  1  524  ? -29.669 12.645  90.945  1.00 41.16 ? 522  ARG   B CZ    1 
ATOM   12787 N  NH1   . ARG   B  1  524  ? -29.270 11.853  89.962  1.00 39.85 ? 522  ARG   B NH1   1 
ATOM   12788 N  NH2   . ARG   B  1  524  ? -29.421 12.295  92.205  1.00 41.14 ? 522  ARG   B NH2   1 
ATOM   12789 N  N     . ALA   B  1  525  ? -29.182 18.878  88.384  1.00 34.60 ? 523  ALA   B N     1 
ATOM   12790 C  CA    . ALA   B  1  525  ? -30.113 19.699  87.624  1.00 40.47 ? 523  ALA   B CA    1 
ATOM   12791 C  C     . ALA   B  1  525  ? -29.433 20.759  86.772  1.00 40.50 ? 523  ALA   B C     1 
ATOM   12792 O  O     . ALA   B  1  525  ? -30.123 21.483  86.050  1.00 40.37 ? 523  ALA   B O     1 
ATOM   12793 C  CB    . ALA   B  1  525  ? -31.134 20.356  88.559  1.00 37.69 ? 523  ALA   B CB    1 
ATOM   12794 N  N     . MET   B  1  526  ? -28.112 20.876  86.837  1.00 37.30 ? 524  MET   B N     1 
ATOM   12795 C  CA    A MET   B  1  526  ? -27.410 21.852  86.022  0.47 39.81 ? 524  MET   B CA    1 
ATOM   12796 C  CA    B MET   B  1  526  ? -27.421 21.857  86.021  0.53 39.81 ? 524  MET   B CA    1 
ATOM   12797 C  C     . MET   B  1  526  ? -27.474 21.446  84.550  1.00 37.59 ? 524  MET   B C     1 
ATOM   12798 O  O     . MET   B  1  526  ? -27.498 20.254  84.230  1.00 36.30 ? 524  MET   B O     1 
ATOM   12799 C  CB    A MET   B  1  526  ? -25.952 21.947  86.456  0.47 38.74 ? 524  MET   B CB    1 
ATOM   12800 C  CB    B MET   B  1  526  ? -25.972 21.991  86.473  0.53 38.74 ? 524  MET   B CB    1 
ATOM   12801 C  CG    A MET   B  1  526  ? -25.771 22.531  87.842  0.47 42.37 ? 524  MET   B CG    1 
ATOM   12802 C  CG    B MET   B  1  526  ? -25.817 22.743  87.783  0.53 42.45 ? 524  MET   B CG    1 
ATOM   12803 S  SD    A MET   B  1  526  ? -26.450 24.197  87.964  0.47 46.40 ? 524  MET   B SD    1 
ATOM   12804 S  SD    B MET   B  1  526  ? -24.167 22.576  88.484  0.53 42.92 ? 524  MET   B SD    1 
ATOM   12805 C  CE    A MET   B  1  526  ? -25.455 25.065  86.753  0.47 41.22 ? 524  MET   B CE    1 
ATOM   12806 C  CE    B MET   B  1  526  ? -23.703 24.291  88.712  0.53 42.05 ? 524  MET   B CE    1 
ATOM   12807 N  N     . PRO   B  1  527  ? -27.509 22.420  83.634  1.00 40.37 ? 525  PRO   B N     1 
ATOM   12808 C  CA    . PRO   B  1  527  ? -27.626 22.063  82.209  1.00 45.61 ? 525  PRO   B CA    1 
ATOM   12809 C  C     . PRO   B  1  527  ? -26.482 21.199  81.712  1.00 40.43 ? 525  PRO   B C     1 
ATOM   12810 O  O     . PRO   B  1  527  ? -26.695 20.311  80.877  1.00 40.28 ? 525  PRO   B O     1 
ATOM   12811 C  CB    . PRO   B  1  527  ? -27.683 23.428  81.506  1.00 45.85 ? 525  PRO   B CB    1 
ATOM   12812 C  CG    . PRO   B  1  527  ? -27.006 24.363  82.452  1.00 47.22 ? 525  PRO   B CG    1 
ATOM   12813 C  CD    . PRO   B  1  527  ? -27.364 23.873  83.826  1.00 45.23 ? 525  PRO   B CD    1 
ATOM   12814 N  N     . VAL   B  1  528  ? -25.273 21.422  82.215  1.00 41.77 ? 526  VAL   B N     1 
ATOM   12815 C  CA    . VAL   B  1  528  ? -24.127 20.577  81.915  1.00 35.18 ? 526  VAL   B CA    1 
ATOM   12816 C  C     . VAL   B  1  528  ? -23.570 20.102  83.247  1.00 32.60 ? 526  VAL   B C     1 
ATOM   12817 O  O     . VAL   B  1  528  ? -22.917 20.875  83.960  1.00 34.57 ? 526  VAL   B O     1 
ATOM   12818 C  CB    . VAL   B  1  528  ? -23.057 21.320  81.106  1.00 35.22 ? 526  VAL   B CB    1 
ATOM   12819 C  CG1   . VAL   B  1  528  ? -21.824 20.449  80.935  1.00 33.20 ? 526  VAL   B CG1   1 
ATOM   12820 C  CG2   . VAL   B  1  528  ? -23.608 21.730  79.755  1.00 38.99 ? 526  VAL   B CG2   1 
ATOM   12821 N  N     . VAL   B  1  529  ? -23.809 18.834  83.578  1.00 28.15 ? 527  VAL   B N     1 
ATOM   12822 C  CA    . VAL   B  1  529  ? -23.355 18.302  84.859  1.00 28.42 ? 527  VAL   B CA    1 
ATOM   12823 C  C     . VAL   B  1  529  ? -21.835 18.358  84.918  1.00 29.63 ? 527  VAL   B C     1 
ATOM   12824 O  O     . VAL   B  1  529  ? -21.136 17.829  84.044  1.00 29.92 ? 527  VAL   B O     1 
ATOM   12825 C  CB    . VAL   B  1  529  ? -23.869 16.879  85.075  1.00 27.46 ? 527  VAL   B CB    1 
ATOM   12826 C  CG1   . VAL   B  1  529  ? -23.218 16.270  86.315  1.00 29.74 ? 527  VAL   B CG1   1 
ATOM   12827 C  CG2   . VAL   B  1  529  ? -25.388 16.878  85.214  1.00 30.02 ? 527  VAL   B CG2   1 
ATOM   12828 N  N     . GLY   B  1  530  ? -21.315 19.023  85.944  1.00 26.16 ? 528  GLY   B N     1 
ATOM   12829 C  CA    . GLY   B  1  530  ? -19.890 19.023  86.163  1.00 27.05 ? 528  GLY   B CA    1 
ATOM   12830 C  C     . GLY   B  1  530  ? -19.112 20.045  85.373  1.00 24.76 ? 528  GLY   B C     1 
ATOM   12831 O  O     . GLY   B  1  530  ? -17.891 19.920  85.270  1.00 23.03 ? 528  GLY   B O     1 
ATOM   12832 N  N     . ALA   B  1  531  ? -19.772 21.059  84.820  1.00 23.76 ? 529  ALA   B N     1 
ATOM   12833 C  CA    . ALA   B  1  531  ? -19.051 22.103  84.105  1.00 22.53 ? 529  ALA   B CA    1 
ATOM   12834 C  C     . ALA   B  1  531  ? -18.092 22.827  85.043  1.00 23.60 ? 529  ALA   B C     1 
ATOM   12835 O  O     . ALA   B  1  531  ? -18.402 23.059  86.218  1.00 25.85 ? 529  ALA   B O     1 
ATOM   12836 C  CB    . ALA   B  1  531  ? -20.030 23.104  83.497  1.00 28.88 ? 529  ALA   B CB    1 
ATOM   12837 N  N     . LYS   B  1  532  ? -16.914 23.152  84.517  1.00 22.67 ? 530  LYS   B N     1 
ATOM   12838 C  CA    . LYS   B  1  532  ? -15.933 23.955  85.234  1.00 24.92 ? 530  LYS   B CA    1 
ATOM   12839 C  C     . LYS   B  1  532  ? -16.564 25.263  85.687  1.00 25.24 ? 530  LYS   B C     1 
ATOM   12840 O  O     . LYS   B  1  532  ? -17.503 25.773  85.069  1.00 24.01 ? 530  LYS   B O     1 
ATOM   12841 C  CB    . LYS   B  1  532  ? -14.773 24.263  84.279  1.00 22.92 ? 530  LYS   B CB    1 
ATOM   12842 C  CG    . LYS   B  1  532  ? -13.643 25.108  84.840  1.00 27.26 ? 530  LYS   B CG    1 
ATOM   12843 C  CD    . LYS   B  1  532  ? -12.613 25.380  83.754  1.00 23.93 ? 530  LYS   B CD    1 
ATOM   12844 C  CE    . LYS   B  1  532  ? -13.184 26.194  82.606  1.00 26.65 ? 530  LYS   B CE    1 
ATOM   12845 N  NZ    . LYS   B  1  532  ? -13.525 27.599  83.003  1.00 26.78 ? 530  LYS   B NZ    1 
ATOM   12846 N  N     . HIS   B  1  533  ? -16.055 25.791  86.792  1.00 22.20 ? 531  HIS   B N     1 
ATOM   12847 C  CA    . HIS   B  1  533  ? -16.421 27.130  87.225  1.00 22.92 ? 531  HIS   B CA    1 
ATOM   12848 C  C     . HIS   B  1  533  ? -16.223 28.122  86.085  1.00 22.69 ? 531  HIS   B C     1 
ATOM   12849 O  O     . HIS   B  1  533  ? -15.185 28.127  85.423  1.00 24.08 ? 531  HIS   B O     1 
ATOM   12850 C  CB    . HIS   B  1  533  ? -15.531 27.515  88.400  1.00 23.69 ? 531  HIS   B CB    1 
ATOM   12851 C  CG    . HIS   B  1  533  ? -16.062 28.652  89.206  1.00 25.82 ? 531  HIS   B CG    1 
ATOM   12852 N  ND1   . HIS   B  1  533  ? -16.186 29.927  88.699  1.00 26.44 ? 531  HIS   B ND1   1 
ATOM   12853 C  CD2   . HIS   B  1  533  ? -16.510 28.707  90.481  1.00 32.37 ? 531  HIS   B CD2   1 
ATOM   12854 C  CE1   . HIS   B  1  533  ? -16.688 30.719  89.629  1.00 33.53 ? 531  HIS   B CE1   1 
ATOM   12855 N  NE2   . HIS   B  1  533  ? -16.896 30.003  90.719  1.00 38.70 ? 531  HIS   B NE2   1 
ATOM   12856 N  N     . ASP   B  1  534  ? -17.234 28.960  85.855  1.00 24.33 ? 532  ASP   B N     1 
ATOM   12857 C  CA    . ASP   B  1  534  ? -17.195 29.920  84.757  1.00 26.38 ? 532  ASP   B CA    1 
ATOM   12858 C  C     . ASP   B  1  534  ? -16.091 30.954  84.917  1.00 27.28 ? 532  ASP   B C     1 
ATOM   12859 O  O     . ASP   B  1  534  ? -15.682 31.564  83.922  1.00 28.96 ? 532  ASP   B O     1 
ATOM   12860 C  CB    . ASP   B  1  534  ? -18.532 30.662  84.662  1.00 28.27 ? 532  ASP   B CB    1 
ATOM   12861 C  CG    . ASP   B  1  534  ? -19.672 29.762  84.252  1.00 40.82 ? 532  ASP   B CG    1 
ATOM   12862 O  OD1   . ASP   B  1  534  ? -19.443 28.865  83.411  1.00 46.87 ? 532  ASP   B OD1   1 
ATOM   12863 O  OD2   . ASP   B  1  534  ? -20.798 29.955  84.766  1.00 49.77 ? 532  ASP   B OD2   1 
ATOM   12864 N  N     . ARG   B  1  535  ? -15.606 31.175  86.136  1.00 23.37 ? 533  ARG   B N     1 
ATOM   12865 C  CA    . ARG   B  1  535  ? -14.668 32.256  86.397  1.00 24.22 ? 533  ARG   B CA    1 
ATOM   12866 C  C     . ARG   B  1  535  ? -13.273 31.757  86.745  1.00 24.40 ? 533  ARG   B C     1 
ATOM   12867 O  O     . ARG   B  1  535  ? -12.461 32.534  87.246  1.00 26.42 ? 533  ARG   B O     1 
ATOM   12868 C  CB    . ARG   B  1  535  ? -15.196 33.178  87.498  1.00 28.62 ? 533  ARG   B CB    1 
ATOM   12869 N  N     . ILE   B  1  536  ? -12.992 30.478  86.525  1.00 21.15 ? 534  ILE   B N     1 
ATOM   12870 C  CA    . ILE   B  1  536  ? -11.667 29.911  86.734  1.00 19.52 ? 534  ILE   B CA    1 
ATOM   12871 C  C     . ILE   B  1  536  ? -11.211 29.368  85.397  1.00 19.07 ? 534  ILE   B C     1 
ATOM   12872 O  O     . ILE   B  1  536  ? -11.848 28.468  84.835  1.00 22.17 ? 534  ILE   B O     1 
ATOM   12873 C  CB    . ILE   B  1  536  ? -11.683 28.795  87.783  1.00 20.18 ? 534  ILE   B CB    1 
ATOM   12874 C  CG1   . ILE   B  1  536  ? -12.148 29.357  89.124  1.00 21.37 ? 534  ILE   B CG1   1 
ATOM   12875 C  CG2   . ILE   B  1  536  ? -10.279 28.195  87.925  1.00 21.11 ? 534  ILE   B CG2   1 
ATOM   12876 C  CD1   . ILE   B  1  536  ? -12.321 28.305  90.185  1.00 27.56 ? 534  ILE   B CD1   1 
ATOM   12877 N  N     . ALA   B  1  537  ? -10.116 29.908  84.890  1.00 19.44 ? 535  ALA   B N     1 
ATOM   12878 C  CA    . ALA   B  1  537  ? -9.648  29.513  83.572  1.00 20.75 ? 535  ALA   B CA    1 
ATOM   12879 C  C     . ALA   B  1  537  ? -8.883  28.205  83.675  1.00 17.92 ? 535  ALA   B C     1 
ATOM   12880 O  O     . ALA   B  1  537  ? -8.067  28.019  84.581  1.00 18.05 ? 535  ALA   B O     1 
ATOM   12881 C  CB    . ALA   B  1  537  ? -8.737  30.596  83.002  1.00 21.40 ? 535  ALA   B CB    1 
ATOM   12882 N  N     . LEU   B  1  538  ? -9.158  27.287  82.756  1.00 18.98 ? 536  LEU   B N     1 
ATOM   12883 C  CA    . LEU   B  1  538  ? -8.231  26.186  82.567  1.00 18.51 ? 536  LEU   B CA    1 
ATOM   12884 C  C     . LEU   B  1  538  ? -6.855  26.760  82.251  1.00 18.12 ? 536  LEU   B C     1 
ATOM   12885 O  O     . LEU   B  1  538  ? -6.746  27.853  81.683  1.00 18.93 ? 536  LEU   B O     1 
ATOM   12886 C  CB    . LEU   B  1  538  ? -8.657  25.325  81.384  1.00 20.26 ? 536  LEU   B CB    1 
ATOM   12887 C  CG    . LEU   B  1  538  ? -9.831  24.378  81.587  1.00 25.28 ? 536  LEU   B CG    1 
ATOM   12888 C  CD1   . LEU   B  1  538  ? -10.173 23.745  80.254  1.00 26.29 ? 536  LEU   B CD1   1 
ATOM   12889 C  CD2   . LEU   B  1  538  ? -9.501  23.316  82.624  1.00 22.59 ? 536  LEU   B CD2   1 
ATOM   12890 N  N     . PRO   B  1  539  ? -5.786  26.049  82.610  1.00 17.09 ? 537  PRO   B N     1 
ATOM   12891 C  CA    . PRO   B  1  539  ? -4.444  26.552  82.285  1.00 17.06 ? 537  PRO   B CA    1 
ATOM   12892 C  C     . PRO   B  1  539  ? -4.289  26.912  80.824  1.00 16.63 ? 537  PRO   B C     1 
ATOM   12893 O  O     . PRO   B  1  539  ? -3.717  27.963  80.528  1.00 16.38 ? 537  PRO   B O     1 
ATOM   12894 C  CB    . PRO   B  1  539  ? -3.522  25.422  82.754  1.00 18.33 ? 537  PRO   B CB    1 
ATOM   12895 C  CG    . PRO   B  1  539  ? -4.313  24.769  83.868  1.00 16.28 ? 537  PRO   B CG    1 
ATOM   12896 C  CD    . PRO   B  1  539  ? -5.741  24.818  83.417  1.00 19.10 ? 537  PRO   B CD    1 
ATOM   12897 N  N     . ALA   B  1  540  ? -4.857  26.118  79.915  1.00 16.69 ? 538  ALA   B N     1 
ATOM   12898 C  CA    . ALA   B  1  540  ? -4.726  26.430  78.499  1.00 18.12 ? 538  ALA   B CA    1 
ATOM   12899 C  C     . ALA   B  1  540  ? -5.421  27.731  78.124  1.00 18.86 ? 538  ALA   B C     1 
ATOM   12900 O  O     . ALA   B  1  540  ? -5.074  28.334  77.099  1.00 18.46 ? 538  ALA   B O     1 
ATOM   12901 C  CB    . ALA   B  1  540  ? -5.292  25.288  77.658  1.00 19.52 ? 538  ALA   B CB    1 
ATOM   12902 N  N     . GLU   B  1  541  ? -6.373  28.183  78.944  1.00 20.17 ? 539  GLU   B N     1 
ATOM   12903 C  CA    . GLU   B  1  541  ? -7.241  29.301  78.600  1.00 19.44 ? 539  GLU   B CA    1 
ATOM   12904 C  C     . GLU   B  1  541  ? -6.917  30.569  79.389  1.00 18.36 ? 539  GLU   B C     1 
ATOM   12905 O  O     . GLU   B  1  541  ? -7.730  31.495  79.423  1.00 19.45 ? 539  GLU   B O     1 
ATOM   12906 C  CB    . GLU   B  1  541  ? -8.712  28.873  78.709  1.00 22.33 ? 539  GLU   B CB    1 
ATOM   12907 C  CG    . GLU   B  1  541  ? -8.983  27.678  77.761  1.00 23.85 ? 539  GLU   B CG    1 
ATOM   12908 C  CD    . GLU   B  1  541  ? -10.362 27.025  77.853  1.00 33.16 ? 539  GLU   B CD    1 
ATOM   12909 O  OE1   . GLU   B  1  541  ? -11.219 27.461  78.644  1.00 32.77 ? 539  GLU   B OE1   1 
ATOM   12910 O  OE2   . GLU   B  1  541  ? -10.582 26.046  77.104  1.00 36.40 ? 539  GLU   B OE2   1 
ATOM   12911 N  N     . LEU   B  1  542  ? -5.718  30.661  79.974  1.00 16.80 ? 540  LEU   B N     1 
ATOM   12912 C  CA    . LEU   B  1  542  ? -5.393  31.821  80.802  1.00 18.19 ? 540  LEU   B CA    1 
ATOM   12913 C  C     . LEU   B  1  542  ? -5.519  33.122  80.037  1.00 18.70 ? 540  LEU   B C     1 
ATOM   12914 O  O     . LEU   B  1  542  ? -5.806  34.166  80.631  1.00 20.56 ? 540  LEU   B O     1 
ATOM   12915 C  CB    . LEU   B  1  542  ? -3.959  31.735  81.307  1.00 19.83 ? 540  LEU   B CB    1 
ATOM   12916 C  CG    . LEU   B  1  542  ? -3.624  30.835  82.474  1.00 20.17 ? 540  LEU   B CG    1 
ATOM   12917 C  CD1   . LEU   B  1  542  ? -2.225  31.192  82.944  1.00 18.79 ? 540  LEU   B CD1   1 
ATOM   12918 C  CD2   . LEU   B  1  542  ? -4.644  30.977  83.603  1.00 20.60 ? 540  LEU   B CD2   1 
ATOM   12919 N  N     . PHE   B  1  543  ? -5.278  33.091  78.732  1.00 18.87 ? 541  PHE   B N     1 
ATOM   12920 C  CA    . PHE   B  1  543  ? -5.288  34.294  77.917  1.00 19.53 ? 541  PHE   B CA    1 
ATOM   12921 C  C     . PHE   B  1  543  ? -6.559  34.428  77.101  1.00 19.83 ? 541  PHE   B C     1 
ATOM   12922 O  O     . PHE   B  1  543  ? -6.639  35.306  76.236  1.00 20.64 ? 541  PHE   B O     1 
ATOM   12923 C  CB    . PHE   B  1  543  ? -4.035  34.332  77.049  1.00 17.55 ? 541  PHE   B CB    1 
ATOM   12924 C  CG    . PHE   B  1  543  ? -2.803  34.091  77.843  1.00 18.84 ? 541  PHE   B CG    1 
ATOM   12925 C  CD1   . PHE   B  1  543  ? -2.525  34.907  78.922  1.00 19.77 ? 541  PHE   B CD1   1 
ATOM   12926 C  CD2   . PHE   B  1  543  ? -1.977  33.014  77.590  1.00 17.11 ? 541  PHE   B CD2   1 
ATOM   12927 C  CE1   . PHE   B  1  543  ? -1.411  34.700  79.698  1.00 21.36 ? 541  PHE   B CE1   1 
ATOM   12928 C  CE2   . PHE   B  1  543  ? -0.844  32.799  78.366  1.00 18.05 ? 541  PHE   B CE2   1 
ATOM   12929 C  CZ    . PHE   B  1  543  ? -0.569  33.644  79.426  1.00 21.63 ? 541  PHE   B CZ    1 
ATOM   12930 N  N     . GLY   B  1  544  ? -7.553  33.583  77.367  1.00 19.73 ? 542  GLY   B N     1 
ATOM   12931 C  CA    . GLY   B  1  544  ? -8.829  33.706  76.692  1.00 19.23 ? 542  GLY   B CA    1 
ATOM   12932 C  C     . GLY   B  1  544  ? -8.681  33.594  75.189  1.00 21.08 ? 542  GLY   B C     1 
ATOM   12933 O  O     . GLY   B  1  544  ? -7.942  32.751  74.667  1.00 22.40 ? 542  GLY   B O     1 
ATOM   12934 N  N     . ASP   B  1  545  ? -9.394  34.465  74.473  1.00 23.17 ? 543  ASP   B N     1 
ATOM   12935 C  CA    . ASP   B  1  545  ? -9.421  34.393  73.021  1.00 25.71 ? 543  ASP   B CA    1 
ATOM   12936 C  C     . ASP   B  1  545  ? -8.132  34.874  72.374  1.00 23.89 ? 543  ASP   B C     1 
ATOM   12937 O  O     . ASP   B  1  545  ? -7.964  34.678  71.167  1.00 24.47 ? 543  ASP   B O     1 
ATOM   12938 C  CB    . ASP   B  1  545  ? -10.583 35.228  72.472  1.00 26.93 ? 543  ASP   B CB    1 
ATOM   12939 C  CG    . ASP   B  1  545  ? -11.936 34.764  72.982  1.00 41.25 ? 543  ASP   B CG    1 
ATOM   12940 O  OD1   . ASP   B  1  545  ? -12.063 33.586  73.387  1.00 43.60 ? 543  ASP   B OD1   1 
ATOM   12941 O  OD2   . ASP   B  1  545  ? -12.880 35.582  72.962  1.00 47.08 ? 543  ASP   B OD2   1 
ATOM   12942 N  N     . ALA   B  1  546  ? -7.235  35.509  73.129  1.00 21.49 ? 544  ALA   B N     1 
ATOM   12943 C  CA    . ALA   B  1  546  ? -6.021  36.051  72.517  1.00 19.81 ? 544  ALA   B CA    1 
ATOM   12944 C  C     . ALA   B  1  546  ? -5.111  34.953  71.979  1.00 19.49 ? 544  ALA   B C     1 
ATOM   12945 O  O     . ALA   B  1  546  ? -4.581  35.072  70.868  1.00 20.06 ? 544  ALA   B O     1 
ATOM   12946 C  CB    . ALA   B  1  546  ? -5.265  36.945  73.499  1.00 21.98 ? 544  ALA   B CB    1 
ATOM   12947 N  N     . ARG   B  1  547  ? -4.893  33.896  72.754  1.00 19.23 ? 545  ARG   B N     1 
ATOM   12948 C  CA    . ARG   B  1  547  ? -3.987  32.835  72.337  1.00 17.60 ? 545  ARG   B CA    1 
ATOM   12949 C  C     . ARG   B  1  547  ? -4.133  31.701  73.329  1.00 18.38 ? 545  ARG   B C     1 
ATOM   12950 O  O     . ARG   B  1  547  ? -4.678  31.872  74.424  1.00 18.80 ? 545  ARG   B O     1 
ATOM   12951 C  CB    . ARG   B  1  547  ? -2.525  33.294  72.283  1.00 22.20 ? 545  ARG   B CB    1 
ATOM   12952 C  CG    . ARG   B  1  547  ? -2.022  33.786  73.606  1.00 18.37 ? 545  ARG   B CG    1 
ATOM   12953 C  CD    . ARG   B  1  547  ? -0.587  34.276  73.470  1.00 19.10 ? 545  ARG   B CD    1 
ATOM   12954 N  NE    . ARG   B  1  547  ? -0.268  35.148  74.586  1.00 17.55 ? 545  ARG   B NE    1 
ATOM   12955 C  CZ    . ARG   B  1  547  ? 0.521   34.815  75.597  1.00 17.40 ? 545  ARG   B CZ    1 
ATOM   12956 N  NH1   . ARG   B  1  547  ? 1.148   33.651  75.634  1.00 17.88 ? 545  ARG   B NH1   1 
ATOM   12957 N  NH2   . ARG   B  1  547  ? 0.674   35.670  76.603  1.00 19.39 ? 545  ARG   B NH2   1 
ATOM   12958 N  N     . THR   B  1  548  ? -3.672  30.535  72.913  1.00 16.94 ? 546  THR   B N     1 
ATOM   12959 C  CA    . THR   B  1  548  ? -3.664  29.365  73.772  1.00 16.80 ? 546  THR   B CA    1 
ATOM   12960 C  C     . THR   B  1  548  ? -2.368  29.343  74.568  1.00 16.10 ? 546  THR   B C     1 
ATOM   12961 O  O     . THR   B  1  548  ? -1.283  29.482  74.005  1.00 15.64 ? 546  THR   B O     1 
ATOM   12962 C  CB    . THR   B  1  548  ? -3.744  28.124  72.901  1.00 16.88 ? 546  THR   B CB    1 
ATOM   12963 O  OG1   . THR   B  1  548  ? -4.945  28.194  72.116  1.00 20.84 ? 546  THR   B OG1   1 
ATOM   12964 C  CG2   . THR   B  1  548  ? -3.735  26.877  73.750  1.00 19.10 ? 546  THR   B CG2   1 
ATOM   12965 N  N     . ASN   B  1  549  ? -2.482  29.167  75.878  1.00 15.77 ? 547  ASN   B N     1 
ATOM   12966 C  CA    . ASN   B  1  549  ? -1.307  29.082  76.723  1.00 16.48 ? 547  ASN   B CA    1 
ATOM   12967 C  C     . ASN   B  1  549  ? -0.526  27.824  76.376  1.00 15.90 ? 547  ASN   B C     1 
ATOM   12968 O  O     . ASN   B  1  549  ? -1.103  26.793  76.027  1.00 16.84 ? 547  ASN   B O     1 
ATOM   12969 C  CB    . ASN   B  1  549  ? -1.780  29.028  78.167  1.00 15.51 ? 547  ASN   B CB    1 
ATOM   12970 C  CG    . ASN   B  1  549  ? -0.665  29.182  79.145  1.00 14.02 ? 547  ASN   B CG    1 
ATOM   12971 O  OD1   . ASN   B  1  549  ? 0.436   29.626  78.795  1.00 15.58 ? 547  ASN   B OD1   1 
ATOM   12972 N  ND2   . ASN   B  1  549  ? -0.939  28.829  80.393  1.00 15.54 ? 547  ASN   B ND2   1 
ATOM   12973 N  N     . SER   B  1  550  ? 0.800   27.917  76.425  1.00 15.25 ? 548  SER   B N     1 
ATOM   12974 C  CA    . SER   B  1  550  ? 1.594   26.708  76.276  1.00 16.99 ? 548  SER   B CA    1 
ATOM   12975 C  C     . SER   B  1  550  ? 1.253   25.725  77.388  1.00 15.20 ? 548  SER   B C     1 
ATOM   12976 O  O     . SER   B  1  550  ? 0.868   26.111  78.498  1.00 16.61 ? 548  SER   B O     1 
ATOM   12977 C  CB    . SER   B  1  550  ? 3.077   27.037  76.351  1.00 14.59 ? 548  SER   B CB    1 
ATOM   12978 O  OG    . SER   B  1  550  ? 3.390   27.574  77.621  1.00 15.37 ? 548  SER   B OG    1 
ATOM   12979 N  N     . ALA   B  1  551  ? 1.402   24.445  77.077  1.00 16.64 ? 549  ALA   B N     1 
ATOM   12980 C  CA    . ALA   B  1  551  ? 1.159   23.379  78.035  1.00 17.68 ? 549  ALA   B CA    1 
ATOM   12981 C  C     . ALA   B  1  551  ? 2.470   22.777  78.505  1.00 16.92 ? 549  ALA   B C     1 
ATOM   12982 O  O     . ALA   B  1  551  ? 3.423   22.634  77.730  1.00 17.63 ? 549  ALA   B O     1 
ATOM   12983 C  CB    . ALA   B  1  551  ? 0.283   22.282  77.437  1.00 19.72 ? 549  ALA   B CB    1 
ATOM   12984 N  N     . GLY   B  1  552  ? 2.518   22.436  79.781  1.00 17.75 ? 550  GLY   B N     1 
ATOM   12985 C  CA    . GLY   B  1  552  ? 3.647   21.767  80.359  1.00 18.74 ? 550  GLY   B CA    1 
ATOM   12986 C  C     . GLY   B  1  552  ? 3.424   20.276  80.420  1.00 16.45 ? 550  GLY   B C     1 
ATOM   12987 O  O     . GLY   B  1  552  ? 2.580   19.709  79.718  1.00 19.30 ? 550  GLY   B O     1 
ATOM   12988 N  N     . LEU   B  1  553  ? 4.209   19.630  81.264  1.00 18.24 ? 551  LEU   B N     1 
ATOM   12989 C  CA    . LEU   B  1  553  ? 4.112   18.201  81.478  1.00 18.14 ? 551  LEU   B CA    1 
ATOM   12990 C  C     . LEU   B  1  553  ? 4.152   17.986  82.977  1.00 18.28 ? 551  LEU   B C     1 
ATOM   12991 O  O     . LEU   B  1  553  ? 4.893   18.668  83.685  1.00 20.42 ? 551  LEU   B O     1 
ATOM   12992 C  CB    . LEU   B  1  553  ? 5.294   17.466  80.813  1.00 19.59 ? 551  LEU   B CB    1 
ATOM   12993 C  CG    . LEU   B  1  553  ? 5.274   17.452  79.285  1.00 20.83 ? 551  LEU   B CG    1 
ATOM   12994 C  CD1   . LEU   B  1  553  ? 6.590   16.939  78.742  1.00 24.93 ? 551  LEU   B CD1   1 
ATOM   12995 C  CD2   . LEU   B  1  553  ? 4.129   16.590  78.797  1.00 24.16 ? 551  LEU   B CD2   1 
ATOM   12996 N  N     . ASP   B  1  554  ? 3.342   17.057  83.458  1.00 17.94 ? 552  ASP   B N     1 
ATOM   12997 C  CA    . ASP   B  1  554  ? 3.207   16.848  84.895  1.00 18.43 ? 552  ASP   B CA    1 
ATOM   12998 C  C     . ASP   B  1  554  ? 4.211   15.786  85.323  1.00 17.49 ? 552  ASP   B C     1 
ATOM   12999 O  O     . ASP   B  1  554  ? 3.990   14.590  85.126  1.00 18.59 ? 552  ASP   B O     1 
ATOM   13000 C  CB    . ASP   B  1  554  ? 1.782   16.428  85.217  1.00 19.89 ? 552  ASP   B CB    1 
ATOM   13001 C  CG    . ASP   B  1  554  ? 1.557   16.211  86.701  1.00 19.55 ? 552  ASP   B CG    1 
ATOM   13002 O  OD1   . ASP   B  1  554  ? 2.508   16.380  87.501  1.00 20.74 ? 552  ASP   B OD1   1 
ATOM   13003 O  OD2   . ASP   B  1  554  ? 0.419   15.876  87.065  1.00 22.03 ? 552  ASP   B OD2   1 
ATOM   13004 N  N     . LEU   B  1  555  ? 5.305   16.221  85.932  1.00 18.61 ? 553  LEU   B N     1 
ATOM   13005 C  CA    . LEU   B  1  555  ? 6.348   15.293  86.334  1.00 19.98 ? 553  LEU   B CA    1 
ATOM   13006 C  C     . LEU   B  1  555  ? 6.018   14.558  87.622  1.00 19.63 ? 553  LEU   B C     1 
ATOM   13007 O  O     . LEU   B  1  555  ? 6.881   13.857  88.151  1.00 20.36 ? 553  LEU   B O     1 
ATOM   13008 C  CB    . LEU   B  1  555  ? 7.690   16.010  86.441  1.00 19.24 ? 553  LEU   B CB    1 
ATOM   13009 C  CG    . LEU   B  1  555  ? 8.139   16.718  85.164  1.00 18.69 ? 553  LEU   B CG    1 
ATOM   13010 C  CD1   . LEU   B  1  555  ? 9.532   17.290  85.384  1.00 22.79 ? 553  LEU   B CD1   1 
ATOM   13011 C  CD2   . LEU   B  1  555  ? 8.116   15.763  83.972  1.00 23.10 ? 553  LEU   B CD2   1 
ATOM   13012 N  N     . SER   B  1  556  ? 4.798   14.701  88.138  1.00 19.35 ? 554  SER   B N     1 
ATOM   13013 C  CA    . SER   B  1  556  ? 4.319   13.854  89.218  1.00 19.54 ? 554  SER   B CA    1 
ATOM   13014 C  C     . SER   B  1  556  ? 3.369   12.779  88.723  1.00 21.05 ? 554  SER   B C     1 
ATOM   13015 O  O     . SER   B  1  556  ? 2.904   11.958  89.517  1.00 20.73 ? 554  SER   B O     1 
ATOM   13016 C  CB    . SER   B  1  556  ? 3.624   14.706  90.288  1.00 19.92 ? 554  SER   B CB    1 
ATOM   13017 O  OG    . SER   B  1  556  ? 2.345   15.112  89.823  1.00 21.19 ? 554  SER   B OG    1 
ATOM   13018 N  N     . ASN   B  1  557  ? 3.081   12.754  87.429  1.00 19.30 ? 555  ASN   B N     1 
ATOM   13019 C  CA    . ASN   B  1  557  ? 2.156   11.803  86.842  1.00 18.71 ? 555  ASN   B CA    1 
ATOM   13020 C  C     . ASN   B  1  557  ? 2.953   10.614  86.314  1.00 20.08 ? 555  ASN   B C     1 
ATOM   13021 O  O     . ASN   B  1  557  ? 3.805   10.780  85.434  1.00 19.90 ? 555  ASN   B O     1 
ATOM   13022 C  CB    . ASN   B  1  557  ? 1.380   12.509  85.729  1.00 20.29 ? 555  ASN   B CB    1 
ATOM   13023 C  CG    . ASN   B  1  557  ? 0.374   11.614  85.055  1.00 21.55 ? 555  ASN   B CG    1 
ATOM   13024 O  OD1   . ASN   B  1  557  ? 0.694   10.506  84.640  1.00 21.76 ? 555  ASN   B OD1   1 
ATOM   13025 N  ND2   . ASN   B  1  557  ? -0.871  12.081  84.960  1.00 21.06 ? 555  ASN   B ND2   1 
ATOM   13026 N  N     . GLU   B  1  558  ? 2.696   9.423   86.863  1.00 20.70 ? 556  GLU   B N     1 
ATOM   13027 C  CA    . GLU   B  1  558  ? 3.483   8.251   86.474  1.00 22.21 ? 556  GLU   B CA    1 
ATOM   13028 C  C     . GLU   B  1  558  ? 3.326   7.926   84.999  1.00 22.29 ? 556  GLU   B C     1 
ATOM   13029 O  O     . GLU   B  1  558  ? 4.273   7.444   84.371  1.00 23.38 ? 556  GLU   B O     1 
ATOM   13030 C  CB    . GLU   B  1  558  ? 3.114   7.015   87.291  1.00 25.35 ? 556  GLU   B CB    1 
ATOM   13031 C  CG    . GLU   B  1  558  ? 3.540   7.039   88.723  1.00 24.64 ? 556  GLU   B CG    1 
ATOM   13032 C  CD    . GLU   B  1  558  ? 5.045   7.187   88.966  1.00 24.84 ? 556  GLU   B CD    1 
ATOM   13033 O  OE1   . GLU   B  1  558  ? 5.903   6.932   88.086  1.00 23.47 ? 556  GLU   B OE1   1 
ATOM   13034 O  OE2   . GLU   B  1  558  ? 5.370   7.571   90.091  1.00 23.50 ? 556  GLU   B OE2   1 
ATOM   13035 N  N     . GLU   B  1  559  ? 2.129   8.122   84.439  1.00 21.28 ? 557  GLU   B N     1 
ATOM   13036 C  CA    . GLU   B  1  559  ? 1.959   7.916   83.005  1.00 21.48 ? 557  GLU   B CA    1 
ATOM   13037 C  C     . GLU   B  1  559  ? 2.858   8.866   82.242  1.00 20.55 ? 557  GLU   B C     1 
ATOM   13038 O  O     . GLU   B  1  559  ? 3.545   8.472   81.292  1.00 22.48 ? 557  GLU   B O     1 
ATOM   13039 C  CB    . GLU   B  1  559  ? 0.511   8.167   82.583  1.00 26.02 ? 557  GLU   B CB    1 
ATOM   13040 C  CG    . GLU   B  1  559  ? -0.508  7.159   83.026  1.00 31.50 ? 557  GLU   B CG    1 
ATOM   13041 C  CD    . GLU   B  1  559  ? -1.859  7.419   82.378  1.00 39.45 ? 557  GLU   B CD    1 
ATOM   13042 O  OE1   . GLU   B  1  559  ? -1.883  7.723   81.165  1.00 39.88 ? 557  GLU   B OE1   1 
ATOM   13043 O  OE2   . GLU   B  1  559  ? -2.891  7.340   83.081  1.00 36.88 ? 557  GLU   B OE2   1 
ATOM   13044 N  N     . THR   B  1  560  ? 2.861   10.133  82.645  1.00 19.66 ? 558  THR   B N     1 
ATOM   13045 C  CA    . THR   B  1  560  ? 3.716   11.101  81.978  1.00 19.01 ? 558  THR   B CA    1 
ATOM   13046 C  C     . THR   B  1  560  ? 5.177   10.726  82.129  1.00 19.77 ? 558  THR   B C     1 
ATOM   13047 O  O     . THR   B  1  560  ? 5.943   10.792  81.160  1.00 19.62 ? 558  THR   B O     1 
ATOM   13048 C  CB    . THR   B  1  560  ? 3.461   12.493  82.534  1.00 18.82 ? 558  THR   B CB    1 
ATOM   13049 O  OG1   . THR   B  1  560  ? 2.073   12.803  82.384  1.00 20.79 ? 558  THR   B OG1   1 
ATOM   13050 C  CG2   . THR   B  1  560  ? 4.291   13.516  81.776  1.00 20.54 ? 558  THR   B CG2   1 
ATOM   13051 N  N     . LEU   B  1  561  ? 5.586   10.324  83.331  1.00 19.09 ? 559  LEU   B N     1 
ATOM   13052 C  CA    . LEU   B  1  561  ? 6.986   9.979   83.529  1.00 17.14 ? 559  LEU   B CA    1 
ATOM   13053 C  C     . LEU   B  1  561  ? 7.380   8.781   82.680  1.00 20.26 ? 559  LEU   B C     1 
ATOM   13054 O  O     . LEU   B  1  561  ? 8.478   8.755   82.113  1.00 18.56 ? 559  LEU   B O     1 
ATOM   13055 C  CB    . LEU   B  1  561  ? 7.276   9.725   85.004  1.00 18.86 ? 559  LEU   B CB    1 
ATOM   13056 C  CG    . LEU   B  1  561  ? 7.198   10.981  85.873  1.00 18.04 ? 559  LEU   B CG    1 
ATOM   13057 C  CD1   . LEU   B  1  561  ? 7.334   10.591  87.333  1.00 19.21 ? 559  LEU   B CD1   1 
ATOM   13058 C  CD2   . LEU   B  1  561  ? 8.268   11.994  85.489  1.00 19.27 ? 559  LEU   B CD2   1 
ATOM   13059 N  N     . ALA   B  1  562  ? 6.506   7.784   82.584  1.00 19.96 ? 560  ALA   B N     1 
ATOM   13060 C  CA    . ALA   B  1  562  ? 6.835   6.611   81.790  1.00 20.16 ? 560  ALA   B CA    1 
ATOM   13061 C  C     . ALA   B  1  562  ? 6.924   6.956   80.313  1.00 22.66 ? 560  ALA   B C     1 
ATOM   13062 O  O     . ALA   B  1  562  ? 7.844   6.505   79.620  1.00 21.61 ? 560  ALA   B O     1 
ATOM   13063 C  CB    . ALA   B  1  562  ? 5.802   5.510   82.021  1.00 22.79 ? 560  ALA   B CB    1 
ATOM   13064 N  N     . SER   B  1  563  ? 5.974   7.741   79.803  1.00 20.15 ? 561  SER   B N     1 
ATOM   13065 C  CA    . SER   B  1  563  ? 6.036   8.088   78.389  1.00 19.98 ? 561  SER   B CA    1 
ATOM   13066 C  C     . SER   B  1  563  ? 7.194   9.033   78.115  1.00 21.47 ? 561  SER   B C     1 
ATOM   13067 O  O     . SER   B  1  563  ? 7.888   8.899   77.098  1.00 21.61 ? 561  SER   B O     1 
ATOM   13068 C  CB    . SER   B  1  563  ? 4.700   8.663   77.905  1.00 21.97 ? 561  SER   B CB    1 
ATOM   13069 O  OG    . SER   B  1  563  ? 4.415   9.903   78.520  1.00 25.45 ? 561  SER   B OG    1 
ATOM   13070 N  N     . LEU   B  1  564  ? 7.433   9.981   79.020  1.00 19.54 ? 562  LEU   B N     1 
ATOM   13071 C  CA    . LEU   B  1  564  ? 8.551   10.893  78.843  1.00 18.80 ? 562  LEU   B CA    1 
ATOM   13072 C  C     . LEU   B  1  564  ? 9.876   10.144  78.863  1.00 20.16 ? 562  LEU   B C     1 
ATOM   13073 O  O     . LEU   B  1  564  ? 10.758  10.419  78.042  1.00 20.91 ? 562  LEU   B O     1 
ATOM   13074 C  CB    . LEU   B  1  564  ? 8.502   11.978  79.918  1.00 20.38 ? 562  LEU   B CB    1 
ATOM   13075 C  CG    . LEU   B  1  564  ? 9.594   13.033  79.881  1.00 21.86 ? 562  LEU   B CG    1 
ATOM   13076 C  CD1   . LEU   B  1  564  ? 9.576   13.776  78.546  1.00 21.80 ? 562  LEU   B CD1   1 
ATOM   13077 C  CD2   . LEU   B  1  564  ? 9.429   13.994  81.049  1.00 24.39 ? 562  LEU   B CD2   1 
ATOM   13078 N  N     . THR   B  1  565  ? 10.025  9.178   79.776  1.00 19.59 ? 563  THR   B N     1 
ATOM   13079 C  CA    . THR   B  1  565  ? 11.245  8.374   79.817  1.00 19.30 ? 563  THR   B CA    1 
ATOM   13080 C  C     . THR   B  1  565  ? 11.539  7.769   78.454  1.00 23.24 ? 563  THR   B C     1 
ATOM   13081 O  O     . THR   B  1  565  ? 12.673  7.821   77.970  1.00 21.10 ? 563  THR   B O     1 
ATOM   13082 C  CB    . THR   B  1  565  ? 11.097  7.251   80.846  1.00 21.32 ? 563  THR   B CB    1 
ATOM   13083 O  OG1   . THR   B  1  565  ? 10.980  7.810   82.159  1.00 20.88 ? 563  THR   B OG1   1 
ATOM   13084 C  CG2   . THR   B  1  565  ? 12.315  6.333   80.820  1.00 22.88 ? 563  THR   B CG2   1 
ATOM   13085 N  N     . GLU   B  1  566  ? 10.524  7.189   77.819  1.00 20.16 ? 564  GLU   B N     1 
ATOM   13086 C  CA    . GLU   B  1  566  ? 10.739  6.577   76.516  1.00 20.03 ? 564  GLU   B CA    1 
ATOM   13087 C  C     . GLU   B  1  566  ? 11.092  7.626   75.474  1.00 22.47 ? 564  GLU   B C     1 
ATOM   13088 O  O     . GLU   B  1  566  ? 12.002  7.417   74.665  1.00 21.59 ? 564  GLU   B O     1 
ATOM   13089 C  CB    . GLU   B  1  566  ? 9.514   5.761   76.109  1.00 23.99 ? 564  GLU   B CB    1 
ATOM   13090 C  CG    . GLU   B  1  566  ? 9.282   4.562   77.027  1.00 30.82 ? 564  GLU   B CG    1 
ATOM   13091 C  CD    . GLU   B  1  566  ? 10.576  3.843   77.398  1.00 38.45 ? 564  GLU   B CD    1 
ATOM   13092 O  OE1   . GLU   B  1  566  ? 11.318  3.426   76.478  1.00 43.41 ? 564  GLU   B OE1   1 
ATOM   13093 O  OE2   . GLU   B  1  566  ? 10.853  3.693   78.613  1.00 38.86 ? 564  GLU   B OE2   1 
ATOM   13094 N  N     . ALA   B  1  567  ? 10.408  8.768   75.496  1.00 19.34 ? 565  ALA   B N     1 
ATOM   13095 C  CA    . ALA   B  1  567  ? 10.705  9.818   74.525  1.00 20.55 ? 565  ALA   B CA    1 
ATOM   13096 C  C     . ALA   B  1  567  ? 12.100  10.383  74.739  1.00 20.75 ? 565  ALA   B C     1 
ATOM   13097 O  O     . ALA   B  1  567  ? 12.809  10.695  73.775  1.00 18.84 ? 565  ALA   B O     1 
ATOM   13098 C  CB    . ALA   B  1  567  ? 9.663   10.930  74.625  1.00 20.14 ? 565  ALA   B CB    1 
ATOM   13099 N  N     . LEU   B  1  568  ? 12.513  10.510  75.994  1.00 17.59 ? 566  LEU   B N     1 
ATOM   13100 C  CA    . LEU   B  1  568  ? 13.847  11.013  76.286  1.00 17.19 ? 566  LEU   B CA    1 
ATOM   13101 C  C     . LEU   B  1  568  ? 14.907  10.027  75.822  1.00 17.70 ? 566  LEU   B C     1 
ATOM   13102 O  O     . LEU   B  1  568  ? 15.884  10.414  75.167  1.00 18.61 ? 566  LEU   B O     1 
ATOM   13103 C  CB    . LEU   B  1  568  ? 13.983  11.307  77.781  1.00 17.12 ? 566  LEU   B CB    1 
ATOM   13104 C  CG    . LEU   B  1  568  ? 13.062  12.417  78.297  1.00 17.45 ? 566  LEU   B CG    1 
ATOM   13105 C  CD1   . LEU   B  1  568  ? 13.112  12.506  79.809  1.00 19.05 ? 566  LEU   B CD1   1 
ATOM   13106 C  CD2   . LEU   B  1  568  ? 13.415  13.745  77.659  1.00 19.21 ? 566  LEU   B CD2   1 
ATOM   13107 N  N     . ARG   B  1  569  ? 14.727  8.743   76.145  1.00 18.77 ? 567  ARG   B N     1 
ATOM   13108 C  CA    . ARG   B  1  569  ? 15.651  7.727   75.659  1.00 20.20 ? 567  ARG   B CA    1 
ATOM   13109 C  C     . ARG   B  1  569  ? 15.734  7.760   74.143  1.00 21.91 ? 567  ARG   B C     1 
ATOM   13110 O  O     . ARG   B  1  569  ? 16.831  7.745   73.569  1.00 21.71 ? 567  ARG   B O     1 
ATOM   13111 C  CB    . ARG   B  1  569  ? 15.219  6.343   76.138  1.00 22.63 ? 567  ARG   B CB    1 
ATOM   13112 C  CG    . ARG   B  1  569  ? 15.523  6.111   77.595  1.00 28.18 ? 567  ARG   B CG    1 
ATOM   13113 C  CD    . ARG   B  1  569  ? 15.019  4.767   78.074  1.00 28.94 ? 567  ARG   B CD    1 
ATOM   13114 N  NE    . ARG   B  1  569  ? 15.141  4.678   79.526  1.00 34.02 ? 567  ARG   B NE    1 
ATOM   13115 C  CZ    . ARG   B  1  569  ? 14.550  3.760   80.280  1.00 36.46 ? 567  ARG   B CZ    1 
ATOM   13116 N  NH1   . ARG   B  1  569  ? 13.783  2.821   79.751  1.00 38.25 ? 567  ARG   B NH1   1 
ATOM   13117 N  NH2   . ARG   B  1  569  ? 14.728  3.793   81.599  1.00 38.68 ? 567  ARG   B NH2   1 
ATOM   13118 N  N     . GLU   B  1  570  ? 14.582  7.828   73.477  1.00 20.16 ? 568  GLU   B N     1 
ATOM   13119 C  CA    . GLU   B  1  570  ? 14.578  7.859   72.022  1.00 20.83 ? 568  GLU   B CA    1 
ATOM   13120 C  C     . GLU   B  1  570  ? 15.266  9.103   71.493  1.00 21.97 ? 568  GLU   B C     1 
ATOM   13121 O  O     . GLU   B  1  570  ? 15.907  9.050   70.439  1.00 22.70 ? 568  GLU   B O     1 
ATOM   13122 C  CB    . GLU   B  1  570  ? 13.146  7.780   71.503  1.00 22.23 ? 568  GLU   B CB    1 
ATOM   13123 C  CG    . GLU   B  1  570  ? 12.485  6.432   71.753  1.00 25.52 ? 568  GLU   B CG    1 
ATOM   13124 C  CD    . GLU   B  1  570  ? 10.959  6.494   71.735  1.00 35.39 ? 568  GLU   B CD    1 
ATOM   13125 O  OE1   . GLU   B  1  570  ? 10.396  7.587   71.507  1.00 32.24 ? 568  GLU   B OE1   1 
ATOM   13126 O  OE2   . GLU   B  1  570  ? 10.320  5.444   71.960  1.00 41.70 ? 568  GLU   B OE2   1 
ATOM   13127 N  N     . SER   B  1  571  ? 15.158  10.225  72.208  1.00 19.89 ? 569  SER   B N     1 
ATOM   13128 C  CA    . SER   B  1  571  ? 15.794  11.445  71.727  1.00 20.24 ? 569  SER   B CA    1 
ATOM   13129 C  C     . SER   B  1  571  ? 17.300  11.292  71.726  1.00 22.76 ? 569  SER   B C     1 
ATOM   13130 O  O     . SER   B  1  571  ? 17.988  11.858  70.866  1.00 21.81 ? 569  SER   B O     1 
ATOM   13131 C  CB    . SER   B  1  571  ? 15.387  12.646  72.582  1.00 20.54 ? 569  SER   B CB    1 
ATOM   13132 O  OG    . SER   B  1  571  ? 16.101  12.686  73.817  1.00 21.10 ? 569  SER   B OG    1 
ATOM   13133 N  N     . ALA   B  1  572  ? 17.829  10.509  72.659  1.00 20.57 ? 570  ALA   B N     1 
ATOM   13134 C  CA    . ALA   B  1  572  ? 19.270  10.350  72.724  1.00 20.96 ? 570  ALA   B CA    1 
ATOM   13135 C  C     . ALA   B  1  572  ? 19.792  9.436   71.628  1.00 24.51 ? 570  ALA   B C     1 
ATOM   13136 O  O     . ALA   B  1  572  ? 20.994  9.456   71.343  1.00 27.51 ? 570  ALA   B O     1 
ATOM   13137 C  CB    . ALA   B  1  572  ? 19.687  9.865   74.112  1.00 21.99 ? 570  ALA   B CB    1 
ATOM   13138 N  N     . ALA   B  1  573  ? 18.919  8.651   71.000  1.00 22.88 ? 571  ALA   B N     1 
ATOM   13139 C  CA    . ALA   B  1  573  ? 19.322  7.784   69.902  1.00 25.63 ? 571  ALA   B CA    1 
ATOM   13140 C  C     . ALA   B  1  573  ? 19.265  8.478   68.547  1.00 24.96 ? 571  ALA   B C     1 
ATOM   13141 O  O     . ALA   B  1  573  ? 19.702  7.892   67.549  1.00 26.07 ? 571  ALA   B O     1 
ATOM   13142 C  CB    . ALA   B  1  573  ? 18.446  6.527   69.874  1.00 26.43 ? 571  ALA   B CB    1 
ATOM   13143 N  N     . MET   B  1  574  ? 18.751  9.701   68.485  1.00 22.58 ? 572  MET   B N     1 
ATOM   13144 C  CA    . MET   B  1  574  ? 18.659  10.410  67.219  1.00 20.32 ? 572  MET   B CA    1 
ATOM   13145 C  C     . MET   B  1  574  ? 19.995  11.042  66.871  1.00 22.38 ? 572  MET   B C     1 
ATOM   13146 O  O     . MET   B  1  574  ? 20.781  11.407  67.747  1.00 22.75 ? 572  MET   B O     1 
ATOM   13147 C  CB    . MET   B  1  574  ? 17.608  11.508  67.322  1.00 23.99 ? 572  MET   B CB    1 
ATOM   13148 C  CG    . MET   B  1  574  ? 16.213  10.955  67.488  1.00 24.09 ? 572  MET   B CG    1 
ATOM   13149 S  SD    . MET   B  1  574  ? 15.060  12.224  68.019  1.00 25.41 ? 572  MET   B SD    1 
ATOM   13150 C  CE    . MET   B  1  574  ? 13.539  11.271  68.082  1.00 26.04 ? 572  MET   B CE    1 
ATOM   13151 N  N     . LYS   B  1  575  ? 20.245  11.176  65.571  1.00 21.06 ? 573  LYS   B N     1 
ATOM   13152 C  CA    . LYS   B  1  575  ? 21.423  11.893  65.085  1.00 21.73 ? 573  LYS   B CA    1 
ATOM   13153 C  C     . LYS   B  1  575  ? 21.063  13.368  65.028  1.00 19.80 ? 573  LYS   B C     1 
ATOM   13154 O  O     . LYS   B  1  575  ? 20.362  13.812  64.116  1.00 21.02 ? 573  LYS   B O     1 
ATOM   13155 C  CB    . LYS   B  1  575  ? 21.842  11.375  63.714  1.00 21.77 ? 573  LYS   B CB    1 
ATOM   13156 C  CG    . LYS   B  1  575  ? 23.067  12.067  63.120  1.00 23.95 ? 573  LYS   B CG    1 
ATOM   13157 C  CD    . LYS   B  1  575  ? 23.475  11.402  61.811  1.00 29.53 ? 573  LYS   B CD    1 
ATOM   13158 C  CE    . LYS   B  1  575  ? 24.879  11.808  61.369  1.00 41.92 ? 573  LYS   B CE    1 
ATOM   13159 N  NZ    . LYS   B  1  575  ? 24.954  13.205  60.858  1.00 44.48 ? 573  LYS   B NZ    1 
ATOM   13160 N  N     . TRP   B  1  576  ? 21.538  14.125  66.010  1.00 19.51 ? 574  TRP   B N     1 
ATOM   13161 C  CA    . TRP   B  1  576  ? 21.302  15.554  66.088  1.00 18.20 ? 574  TRP   B CA    1 
ATOM   13162 C  C     . TRP   B  1  576  ? 22.437  16.298  65.411  1.00 17.61 ? 574  TRP   B C     1 
ATOM   13163 O  O     . TRP   B  1  576  ? 23.611  16.103  65.745  1.00 19.60 ? 574  TRP   B O     1 
ATOM   13164 C  CB    . TRP   B  1  576  ? 21.225  15.997  67.540  1.00 17.58 ? 574  TRP   B CB    1 
ATOM   13165 C  CG    . TRP   B  1  576  ? 20.047  15.453  68.267  1.00 18.10 ? 574  TRP   B CG    1 
ATOM   13166 C  CD1   . TRP   B  1  576  ? 20.053  14.467  69.201  1.00 20.16 ? 574  TRP   B CD1   1 
ATOM   13167 C  CD2   . TRP   B  1  576  ? 18.689  15.846  68.093  1.00 17.62 ? 574  TRP   B CD2   1 
ATOM   13168 N  NE1   . TRP   B  1  576  ? 18.773  14.246  69.659  1.00 19.34 ? 574  TRP   B NE1   1 
ATOM   13169 C  CE2   . TRP   B  1  576  ? 17.917  15.077  68.984  1.00 18.94 ? 574  TRP   B CE2   1 
ATOM   13170 C  CE3   . TRP   B  1  576  ? 18.056  16.794  67.292  1.00 17.46 ? 574  TRP   B CE3   1 
ATOM   13171 C  CZ2   . TRP   B  1  576  ? 16.540  15.217  69.088  1.00 20.21 ? 574  TRP   B CZ2   1 
ATOM   13172 C  CZ3   . TRP   B  1  576  ? 16.687  16.940  67.399  1.00 18.43 ? 574  TRP   B CZ3   1 
ATOM   13173 C  CH2   . TRP   B  1  576  ? 15.945  16.159  68.296  1.00 19.69 ? 574  TRP   B CH2   1 
ATOM   13174 N  N     . THR   B  1  577  ? 22.082  17.154  64.468  1.00 19.45 ? 575  THR   B N     1 
ATOM   13175 C  CA    . THR   B  1  577  ? 23.062  17.928  63.738  1.00 16.90 ? 575  THR   B CA    1 
ATOM   13176 C  C     . THR   B  1  577  ? 22.615  19.375  63.700  1.00 17.10 ? 575  THR   B C     1 
ATOM   13177 O  O     . THR   B  1  577  ? 21.450  19.700  63.903  1.00 17.29 ? 575  THR   B O     1 
ATOM   13178 C  CB    . THR   B  1  577  ? 23.225  17.417  62.308  1.00 20.65 ? 575  THR   B CB    1 
ATOM   13179 O  OG1   . THR   B  1  577  ? 21.982  17.572  61.615  1.00 23.82 ? 575  THR   B OG1   1 
ATOM   13180 C  CG2   . THR   B  1  577  ? 23.623  15.949  62.313  1.00 21.20 ? 575  THR   B CG2   1 
ATOM   13181 N  N     . ALA   B  1  578  ? 23.568  20.248  63.423  1.00 16.34 ? 576  ALA   B N     1 
ATOM   13182 C  CA    . ALA   B  1  578  ? 23.279  21.644  63.155  1.00 16.69 ? 576  ALA   B CA    1 
ATOM   13183 C  C     . ALA   B  1  578  ? 24.216  22.066  62.049  1.00 16.24 ? 576  ALA   B C     1 
ATOM   13184 O  O     . ALA   B  1  578  ? 25.427  21.894  62.174  1.00 18.19 ? 576  ALA   B O     1 
ATOM   13185 C  CB    . ALA   B  1  578  ? 23.497  22.501  64.403  1.00 17.40 ? 576  ALA   B CB    1 
ATOM   13186 N  N     . LEU   B  1  579  ? 23.658  22.569  60.968  1.00 16.84 ? 577  LEU   B N     1 
ATOM   13187 C  CA    . LEU   B  1  579  ? 24.394  22.898  59.765  1.00 18.33 ? 577  LEU   B CA    1 
ATOM   13188 C  C     . LEU   B  1  579  ? 24.154  24.350  59.404  1.00 17.56 ? 577  LEU   B C     1 
ATOM   13189 O  O     . LEU   B  1  579  ? 23.136  24.935  59.796  1.00 16.14 ? 577  LEU   B O     1 
ATOM   13190 C  CB    . LEU   B  1  579  ? 23.874  22.040  58.606  1.00 20.42 ? 577  LEU   B CB    1 
ATOM   13191 C  CG    . LEU   B  1  579  ? 23.755  20.546  58.872  1.00 22.76 ? 577  LEU   B CG    1 
ATOM   13192 C  CD1   . LEU   B  1  579  ? 23.189  19.834  57.645  1.00 23.97 ? 577  LEU   B CD1   1 
ATOM   13193 C  CD2   . LEU   B  1  579  ? 25.134  20.019  59.229  1.00 22.73 ? 577  LEU   B CD2   1 
ATOM   13194 N  N     . PRO   B  1  580  ? 25.053  24.956  58.624  1.00 16.52 ? 578  PRO   B N     1 
ATOM   13195 C  CA    . PRO   B  1  580  ? 24.733  26.252  58.022  1.00 16.74 ? 578  PRO   B CA    1 
ATOM   13196 C  C     . PRO   B  1  580  ? 23.649  26.031  56.991  1.00 16.71 ? 578  PRO   B C     1 
ATOM   13197 O  O     . PRO   B  1  580  ? 23.901  25.505  55.909  1.00 18.97 ? 578  PRO   B O     1 
ATOM   13198 C  CB    . PRO   B  1  580  ? 26.053  26.686  57.375  1.00 19.70 ? 578  PRO   B CB    1 
ATOM   13199 C  CG    . PRO   B  1  580  ? 27.107  25.814  58.048  1.00 19.75 ? 578  PRO   B CG    1 
ATOM   13200 C  CD    . PRO   B  1  580  ? 26.410  24.511  58.265  1.00 19.58 ? 578  PRO   B CD    1 
ATOM   13201 N  N     . GLN   B  1  581  ? 22.426  26.360  57.359  1.00 15.85 ? 579  GLN   B N     1 
ATOM   13202 C  CA    . GLN   B  1  581  ? 21.264  26.112  56.520  1.00 17.86 ? 579  GLN   B CA    1 
ATOM   13203 C  C     . GLN   B  1  581  ? 20.975  27.395  55.765  1.00 19.62 ? 579  GLN   B C     1 
ATOM   13204 O  O     . GLN   B  1  581  ? 20.259  28.275  56.245  1.00 18.71 ? 579  GLN   B O     1 
ATOM   13205 C  CB    . GLN   B  1  581  ? 20.087  25.707  57.383  1.00 17.30 ? 579  GLN   B CB    1 
ATOM   13206 C  CG    . GLN   B  1  581  ? 20.273  24.403  58.075  1.00 17.99 ? 579  GLN   B CG    1 
ATOM   13207 C  CD    . GLN   B  1  581  ? 20.198  23.203  57.152  1.00 23.18 ? 579  GLN   B CD    1 
ATOM   13208 O  OE1   . GLN   B  1  581  ? 20.015  23.325  55.931  1.00 22.49 ? 579  GLN   B OE1   1 
ATOM   13209 N  NE2   . GLN   B  1  581  ? 20.323  22.022  57.738  1.00 26.92 ? 579  GLN   B NE2   1 
ATOM   13210 N  N     . LEU   B  1  582  ? 21.562  27.506  54.580  1.00 18.07 ? 580  LEU   B N     1 
ATOM   13211 C  CA    . LEU   B  1  582  ? 21.298  28.651  53.733  1.00 17.84 ? 580  LEU   B CA    1 
ATOM   13212 C  C     . LEU   B  1  582  ? 20.034  28.391  52.917  1.00 19.61 ? 580  LEU   B C     1 
ATOM   13213 O  O     . LEU   B  1  582  ? 19.478  27.289  52.919  1.00 20.55 ? 580  LEU   B O     1 
ATOM   13214 C  CB    . LEU   B  1  582  ? 22.509  28.956  52.852  1.00 19.23 ? 580  LEU   B CB    1 
ATOM   13215 C  CG    . LEU   B  1  582  ? 23.584  29.813  53.556  1.00 24.18 ? 580  LEU   B CG    1 
ATOM   13216 C  CD1   . LEU   B  1  582  ? 24.265  29.098  54.734  1.00 21.74 ? 580  LEU   B CD1   1 
ATOM   13217 C  CD2   . LEU   B  1  582  ? 24.622  30.332  52.570  1.00 29.02 ? 580  LEU   B CD2   1 
ATOM   13218 N  N     . ALA   B  1  583  ? 19.567  29.428  52.226  1.00 18.75 ? 581  ALA   B N     1 
ATOM   13219 C  CA    . ALA   B  1  583  ? 18.337  29.285  51.453  1.00 18.93 ? 581  ALA   B CA    1 
ATOM   13220 C  C     . ALA   B  1  583  ? 18.481  28.208  50.395  1.00 23.28 ? 581  ALA   B C     1 
ATOM   13221 O  O     . ALA   B  1  583  ? 17.509  27.516  50.071  1.00 24.15 ? 581  ALA   B O     1 
ATOM   13222 C  CB    . ALA   B  1  583  ? 17.987  30.616  50.798  1.00 21.97 ? 581  ALA   B CB    1 
ATOM   13223 N  N     . THR   B  1  584  ? 19.683  28.044  49.860  1.00 20.33 ? 582  THR   B N     1 
ATOM   13224 C  CA    . THR   B  1  584  ? 19.947  27.093  48.794  1.00 20.54 ? 582  THR   B CA    1 
ATOM   13225 C  C     . THR   B  1  584  ? 20.314  25.711  49.312  1.00 18.93 ? 582  THR   B C     1 
ATOM   13226 O  O     . THR   B  1  584  ? 20.619  24.823  48.508  1.00 20.54 ? 582  THR   B O     1 
ATOM   13227 C  CB    . THR   B  1  584  ? 21.073  27.628  47.907  1.00 25.04 ? 582  THR   B CB    1 
ATOM   13228 O  OG1   . THR   B  1  584  ? 22.120  28.129  48.747  1.00 24.72 ? 582  THR   B OG1   1 
ATOM   13229 C  CG2   . THR   B  1  584  ? 20.561  28.757  47.046  1.00 31.11 ? 582  THR   B CG2   1 
ATOM   13230 N  N     . GLY   B  1  585  ? 20.294  25.506  50.624  1.00 20.95 ? 583  GLY   B N     1 
ATOM   13231 C  CA    . GLY   B  1  585  ? 20.612  24.224  51.204  1.00 20.11 ? 583  GLY   B CA    1 
ATOM   13232 C  C     . GLY   B  1  585  ? 21.736  24.355  52.205  1.00 19.25 ? 583  GLY   B C     1 
ATOM   13233 O  O     . GLY   B  1  585  ? 22.300  25.440  52.388  1.00 21.96 ? 583  GLY   B O     1 
ATOM   13234 N  N     . PRO   B  1  586  ? 22.071  23.260  52.887  1.00 18.99 ? 584  PRO   B N     1 
ATOM   13235 C  CA    . PRO   B  1  586  ? 23.152  23.321  53.872  1.00 18.02 ? 584  PRO   B CA    1 
ATOM   13236 C  C     . PRO   B  1  586  ? 24.490  23.496  53.190  1.00 19.55 ? 584  PRO   B C     1 
ATOM   13237 O  O     . PRO   B  1  586  ? 24.755  22.914  52.136  1.00 21.48 ? 584  PRO   B O     1 
ATOM   13238 C  CB    . PRO   B  1  586  ? 23.072  21.963  54.571  1.00 20.00 ? 584  PRO   B CB    1 
ATOM   13239 C  CG    . PRO   B  1  586  ? 22.486  21.068  53.537  1.00 23.82 ? 584  PRO   B CG    1 
ATOM   13240 C  CD    . PRO   B  1  586  ? 21.472  21.919  52.826  1.00 22.52 ? 584  PRO   B CD    1 
ATOM   13241 N  N     . ALA   B  1  587  ? 25.341  24.287  53.821  1.00 18.47 ? 585  ALA   B N     1 
ATOM   13242 C  CA    . ALA   B  1  587  ? 26.679  24.544  53.323  1.00 19.14 ? 585  ALA   B CA    1 
ATOM   13243 C  C     . ALA   B  1  587  ? 27.684  23.711  54.096  1.00 20.01 ? 585  ALA   B C     1 
ATOM   13244 O  O     . ALA   B  1  587  ? 27.448  23.297  55.234  1.00 20.99 ? 585  ALA   B O     1 
ATOM   13245 C  CB    . ALA   B  1  587  ? 27.016  26.029  53.464  1.00 21.27 ? 585  ALA   B CB    1 
ATOM   13246 N  N     . ALA   B  1  588  ? 28.820  23.467  53.454  1.00 20.53 ? 586  ALA   B N     1 
ATOM   13247 C  CA    . ALA   B  1  588  ? 29.916  22.790  54.121  1.00 20.73 ? 586  ALA   B CA    1 
ATOM   13248 C  C     . ALA   B  1  588  ? 30.580  23.734  55.114  1.00 20.43 ? 586  ALA   B C     1 
ATOM   13249 O  O     . ALA   B  1  588  ? 30.508  24.959  54.994  1.00 22.51 ? 586  ALA   B O     1 
ATOM   13250 C  CB    . ALA   B  1  588  ? 30.952  22.341  53.097  1.00 20.69 ? 586  ALA   B CB    1 
ATOM   13251 N  N     . GLY   B  1  589  ? 31.233  23.148  56.106  1.00 21.04 ? 587  GLY   B N     1 
ATOM   13252 C  CA    . GLY   B  1  589  ? 31.984  23.949  57.050  1.00 21.87 ? 587  GLY   B CA    1 
ATOM   13253 C  C     . GLY   B  1  589  ? 32.785  23.066  57.977  1.00 22.08 ? 587  GLY   B C     1 
ATOM   13254 O  O     . GLY   B  1  589  ? 32.840  21.848  57.809  1.00 23.49 ? 587  GLY   B O     1 
ATOM   13255 N  N     . GLU   B  1  590  ? 33.404  23.704  58.968  1.00 25.49 ? 588  GLU   B N     1 
ATOM   13256 C  CA    . GLU   B  1  590  ? 34.139  22.972  59.991  1.00 24.03 ? 588  GLU   B CA    1 
ATOM   13257 C  C     . GLU   B  1  590  ? 33.165  22.317  60.962  1.00 21.18 ? 588  GLU   B C     1 
ATOM   13258 O  O     . GLU   B  1  590  ? 32.284  22.977  61.513  1.00 21.88 ? 588  GLU   B O     1 
ATOM   13259 C  CB    . GLU   B  1  590  ? 35.046  23.933  60.756  1.00 26.98 ? 588  GLU   B CB    1 
ATOM   13260 C  CG    . GLU   B  1  590  ? 36.128  24.574  59.897  1.00 32.11 ? 588  GLU   B CG    1 
ATOM   13261 C  CD    . GLU   B  1  590  ? 37.099  23.557  59.319  1.00 40.87 ? 588  GLU   B CD    1 
ATOM   13262 O  OE1   . GLU   B  1  590  ? 37.420  22.568  60.014  1.00 48.49 ? 588  GLU   B OE1   1 
ATOM   13263 O  OE2   . GLU   B  1  590  ? 37.540  23.746  58.164  1.00 51.54 ? 588  GLU   B OE2   1 
ATOM   13264 N  N     . THR   B  1  591  ? 33.345  21.028  61.203  1.00 23.29 ? 589  THR   B N     1 
ATOM   13265 C  CA    . THR   B  1  591  ? 32.422  20.253  62.012  1.00 24.43 ? 589  THR   B CA    1 
ATOM   13266 C  C     . THR   B  1  591  ? 33.095  19.802  63.298  1.00 22.78 ? 589  THR   B C     1 
ATOM   13267 O  O     . THR   B  1  591  ? 34.271  19.424  63.298  1.00 24.26 ? 589  THR   B O     1 
ATOM   13268 C  CB    . THR   B  1  591  ? 31.932  19.039  61.228  1.00 23.00 ? 589  THR   B CB    1 
ATOM   13269 O  OG1   . THR   B  1  591  ? 31.278  19.494  60.041  1.00 25.97 ? 589  THR   B OG1   1 
ATOM   13270 C  CG2   . THR   B  1  591  ? 30.952  18.236  62.046  1.00 25.35 ? 589  THR   B CG2   1 
ATOM   13271 N  N     . ARG   B  1  592  ? 32.349  19.853  64.395  1.00 21.93 ? 590  ARG   B N     1 
ATOM   13272 C  CA    . ARG   B  1  592  ? 32.831  19.328  65.658  1.00 25.58 ? 590  ARG   B CA    1 
ATOM   13273 C  C     . ARG   B  1  592  ? 31.665  18.705  66.412  1.00 23.85 ? 590  ARG   B C     1 
ATOM   13274 O  O     . ARG   B  1  592  ? 30.490  18.936  66.097  1.00 21.18 ? 590  ARG   B O     1 
ATOM   13275 C  CB    . ARG   B  1  592  ? 33.485  20.423  66.500  1.00 24.69 ? 590  ARG   B CB    1 
ATOM   13276 C  CG    . ARG   B  1  592  ? 32.516  21.499  66.925  1.00 26.42 ? 590  ARG   B CG    1 
ATOM   13277 C  CD    . ARG   B  1  592  ? 33.111  22.371  68.006  1.00 32.87 ? 590  ARG   B CD    1 
ATOM   13278 N  NE    . ARG   B  1  592  ? 32.256  23.513  68.289  1.00 31.04 ? 590  ARG   B NE    1 
ATOM   13279 C  CZ    . ARG   B  1  592  ? 31.237  23.487  69.135  1.00 31.90 ? 590  ARG   B CZ    1 
ATOM   13280 N  NH1   . ARG   B  1  592  ? 30.921  22.388  69.805  1.00 30.62 ? 590  ARG   B NH1   1 
ATOM   13281 N  NH2   . ARG   B  1  592  ? 30.521  24.592  69.318  1.00 30.74 ? 590  ARG   B NH2   1 
ATOM   13282 N  N     . THR   B  1  593  ? 32.001  17.908  67.421  1.00 23.47 ? 591  THR   B N     1 
ATOM   13283 C  CA    . THR   B  1  593  ? 30.980  17.297  68.252  1.00 22.02 ? 591  THR   B CA    1 
ATOM   13284 C  C     . THR   B  1  593  ? 30.467  18.280  69.292  1.00 22.46 ? 591  THR   B C     1 
ATOM   13285 O  O     . THR   B  1  593  ? 31.153  19.224  69.694  1.00 23.58 ? 591  THR   B O     1 
ATOM   13286 C  CB    . THR   B  1  593  ? 31.517  16.052  68.950  1.00 25.24 ? 591  THR   B CB    1 
ATOM   13287 O  OG1   . THR   B  1  593  ? 32.613  16.425  69.789  1.00 27.58 ? 591  THR   B OG1   1 
ATOM   13288 C  CG2   . THR   B  1  593  ? 31.977  15.033  67.922  1.00 29.78 ? 591  THR   B CG2   1 
ATOM   13289 N  N     . VAL   B  1  594  ? 29.225  18.062  69.697  1.00 19.34 ? 592  VAL   B N     1 
ATOM   13290 C  CA    . VAL   B  1  594  ? 28.601  18.766  70.805  1.00 19.35 ? 592  VAL   B CA    1 
ATOM   13291 C  C     . VAL   B  1  594  ? 28.493  17.762  71.938  1.00 20.85 ? 592  VAL   B C     1 
ATOM   13292 O  O     . VAL   B  1  594  ? 27.904  16.688  71.764  1.00 21.82 ? 592  VAL   B O     1 
ATOM   13293 C  CB    . VAL   B  1  594  ? 27.219  19.294  70.399  1.00 19.72 ? 592  VAL   B CB    1 
ATOM   13294 C  CG1   . VAL   B  1  594  ? 26.551  19.999  71.573  1.00 19.86 ? 592  VAL   B CG1   1 
ATOM   13295 C  CG2   . VAL   B  1  594  ? 27.364  20.233  69.215  1.00 21.62 ? 592  VAL   B CG2   1 
ATOM   13296 N  N     . LEU   B  1  595  ? 29.088  18.091  73.084  1.00 20.95 ? 593  LEU   B N     1 
ATOM   13297 C  CA    . LEU   B  1  595  ? 29.189  17.186  74.219  1.00 20.03 ? 593  LEU   B CA    1 
ATOM   13298 C  C     . LEU   B  1  595  ? 28.273  17.660  75.334  1.00 18.85 ? 593  LEU   B C     1 
ATOM   13299 O  O     . LEU   B  1  595  ? 28.052  18.859  75.513  1.00 21.07 ? 593  LEU   B O     1 
ATOM   13300 C  CB    . LEU   B  1  595  ? 30.625  17.141  74.744  1.00 20.32 ? 593  LEU   B CB    1 
ATOM   13301 C  CG    . LEU   B  1  595  ? 31.666  16.771  73.690  1.00 22.31 ? 593  LEU   B CG    1 
ATOM   13302 C  CD1   . LEU   B  1  595  ? 33.039  16.753  74.348  1.00 25.79 ? 593  LEU   B CD1   1 
ATOM   13303 C  CD2   . LEU   B  1  595  ? 31.350  15.427  73.031  1.00 23.28 ? 593  LEU   B CD2   1 
ATOM   13304 N  N     . ASN   B  1  596  ? 27.738  16.706  76.073  1.00 17.32 ? 594  ASN   B N     1 
ATOM   13305 C  CA    . ASN   B  1  596  ? 26.919  17.023  77.231  1.00 18.32 ? 594  ASN   B CA    1 
ATOM   13306 C  C     . ASN   B  1  596  ? 27.781  17.740  78.263  1.00 18.13 ? 594  ASN   B C     1 
ATOM   13307 O  O     . ASN   B  1  596  ? 28.778  17.165  78.728  1.00 17.52 ? 594  ASN   B O     1 
ATOM   13308 C  CB    . ASN   B  1  596  ? 26.423  15.700  77.799  1.00 16.78 ? 594  ASN   B CB    1 
ATOM   13309 C  CG    . ASN   B  1  596  ? 25.381  15.877  78.878  1.00 17.58 ? 594  ASN   B CG    1 
ATOM   13310 O  OD1   . ASN   B  1  596  ? 25.393  16.850  79.634  1.00 18.56 ? 594  ASN   B OD1   1 
ATOM   13311 N  ND2   . ASN   B  1  596  ? 24.470  14.923  78.961  1.00 20.83 ? 594  ASN   B ND2   1 
ATOM   13312 N  N     . PRO   B  1  597  ? 27.450  18.973  78.653  1.00 17.17 ? 595  PRO   B N     1 
ATOM   13313 C  CA    . PRO   B  1  597  ? 28.271  19.661  79.661  1.00 18.67 ? 595  PRO   B CA    1 
ATOM   13314 C  C     . PRO   B  1  597  ? 28.332  18.933  80.979  1.00 18.25 ? 595  PRO   B C     1 
ATOM   13315 O  O     . PRO   B  1  597  ? 29.289  19.137  81.733  1.00 16.57 ? 595  PRO   B O     1 
ATOM   13316 C  CB    . PRO   B  1  597  ? 27.600  21.036  79.803  1.00 17.15 ? 595  PRO   B CB    1 
ATOM   13317 C  CG    . PRO   B  1  597  ? 26.179  20.820  79.317  1.00 17.58 ? 595  PRO   B CG    1 
ATOM   13318 C  CD    . PRO   B  1  597  ? 26.306  19.793  78.216  1.00 16.51 ? 595  PRO   B CD    1 
ATOM   13319 N  N     . GLY   B  1  598  ? 27.349  18.095  81.286  1.00 17.40 ? 596  GLY   B N     1 
ATOM   13320 C  CA    . GLY   B  1  598  ? 27.388  17.343  82.523  1.00 18.57 ? 596  GLY   B CA    1 
ATOM   13321 C  C     . GLY   B  1  598  ? 28.174  16.061  82.444  1.00 19.43 ? 596  GLY   B C     1 
ATOM   13322 O  O     . GLY   B  1  598  ? 28.415  15.426  83.473  1.00 19.93 ? 596  GLY   B O     1 
ATOM   13323 N  N     . ASP   B  1  599  ? 28.589  15.671  81.245  1.00 17.78 ? 597  ASP   B N     1 
ATOM   13324 C  CA    . ASP   B  1  599  ? 29.355  14.451  81.054  1.00 19.91 ? 597  ASP   B CA    1 
ATOM   13325 C  C     . ASP   B  1  599  ? 29.881  14.453  79.633  1.00 19.93 ? 597  ASP   B C     1 
ATOM   13326 O  O     . ASP   B  1  599  ? 29.162  14.101  78.693  1.00 19.18 ? 597  ASP   B O     1 
ATOM   13327 C  CB    . ASP   B  1  599  ? 28.473  13.228  81.284  1.00 21.28 ? 597  ASP   B CB    1 
ATOM   13328 C  CG    . ASP   B  1  599  ? 29.251  11.935  81.288  1.00 24.05 ? 597  ASP   B CG    1 
ATOM   13329 O  OD1   . ASP   B  1  599  ? 30.399  11.916  80.779  1.00 22.57 ? 597  ASP   B OD1   1 
ATOM   13330 O  OD2   . ASP   B  1  599  ? 28.704  10.933  81.797  1.00 25.23 ? 597  ASP   B OD2   1 
ATOM   13331 N  N     . HIS   B  1  600  ? 31.142  14.837  79.466  1.00 19.29 ? 598  HIS   B N     1 
ATOM   13332 C  CA    . HIS   B  1  600  ? 31.689  14.958  78.125  1.00 20.53 ? 598  HIS   B CA    1 
ATOM   13333 C  C     . HIS   B  1  600  ? 31.764  13.630  77.386  1.00 20.26 ? 598  HIS   B C     1 
ATOM   13334 O  O     . HIS   B  1  600  ? 31.986  13.635  76.173  1.00 24.18 ? 598  HIS   B O     1 
ATOM   13335 C  CB    . HIS   B  1  600  ? 33.047  15.665  78.164  1.00 21.87 ? 598  HIS   B CB    1 
ATOM   13336 C  CG    . HIS   B  1  600  ? 32.947  17.122  78.499  1.00 22.86 ? 598  HIS   B CG    1 
ATOM   13337 N  ND1   . HIS   B  1  600  ? 34.049  17.943  78.606  1.00 26.85 ? 598  HIS   B ND1   1 
ATOM   13338 C  CD2   . HIS   B  1  600  ? 31.870  17.903  78.752  1.00 22.24 ? 598  HIS   B CD2   1 
ATOM   13339 C  CE1   . HIS   B  1  600  ? 33.656  19.167  78.913  1.00 27.35 ? 598  HIS   B CE1   1 
ATOM   13340 N  NE2   . HIS   B  1  600  ? 32.337  19.171  79.007  1.00 23.90 ? 598  HIS   B NE2   1 
ATOM   13341 N  N     . ARG   B  1  601  ? 31.595  12.497  78.075  1.00 20.97 ? 599  ARG   B N     1 
ATOM   13342 C  CA    . ARG   B  1  601  ? 31.526  11.223  77.372  1.00 20.89 ? 599  ARG   B CA    1 
ATOM   13343 C  C     . ARG   B  1  601  ? 30.230  11.073  76.588  1.00 21.48 ? 599  ARG   B C     1 
ATOM   13344 O  O     . ARG   B  1  601  ? 30.149  10.220  75.698  1.00 24.39 ? 599  ARG   B O     1 
ATOM   13345 C  CB    . ARG   B  1  601  ? 31.654  10.077  78.367  1.00 24.10 ? 599  ARG   B CB    1 
ATOM   13346 C  CG    . ARG   B  1  601  ? 32.948  10.119  79.164  1.00 24.74 ? 599  ARG   B CG    1 
ATOM   13347 C  CD    . ARG   B  1  601  ? 32.893  9.173   80.336  1.00 27.75 ? 599  ARG   B CD    1 
ATOM   13348 N  NE    . ARG   B  1  601  ? 31.808  9.488   81.256  1.00 25.47 ? 599  ARG   B NE    1 
ATOM   13349 C  CZ    . ARG   B  1  601  ? 31.443  8.716   82.268  1.00 29.54 ? 599  ARG   B CZ    1 
ATOM   13350 N  NH1   . ARG   B  1  601  ? 32.084  7.590   82.544  1.00 30.83 ? 599  ARG   B NH1   1 
ATOM   13351 N  NH2   . ARG   B  1  601  ? 30.404  9.076   83.018  1.00 28.01 ? 599  ARG   B NH2   1 
ATOM   13352 N  N     . ASP   B  1  602  ? 29.215  11.869  76.910  1.00 20.48 ? 600  ASP   B N     1 
ATOM   13353 C  CA    . ASP   B  1  602  ? 27.915  11.804  76.251  1.00 20.96 ? 600  ASP   B CA    1 
ATOM   13354 C  C     . ASP   B  1  602  ? 27.957  12.745  75.052  1.00 20.97 ? 600  ASP   B C     1 
ATOM   13355 O  O     . ASP   B  1  602  ? 27.864  13.967  75.195  1.00 19.31 ? 600  ASP   B O     1 
ATOM   13356 C  CB    . ASP   B  1  602  ? 26.820  12.189  77.236  1.00 22.33 ? 600  ASP   B CB    1 
ATOM   13357 C  CG    . ASP   B  1  602  ? 25.441  12.067  76.642  1.00 23.60 ? 600  ASP   B CG    1 
ATOM   13358 O  OD1   . ASP   B  1  602  ? 25.292  11.346  75.631  1.00 23.75 ? 600  ASP   B OD1   1 
ATOM   13359 O  OD2   . ASP   B  1  602  ? 24.513  12.694  77.191  1.00 23.46 ? 600  ASP   B OD2   1 
ATOM   13360 N  N     . VAL   B  1  603  ? 28.117  12.179  73.862  1.00 21.70 ? 601  VAL   B N     1 
ATOM   13361 C  CA    . VAL   B  1  603  ? 28.098  12.968  72.637  1.00 21.65 ? 601  VAL   B CA    1 
ATOM   13362 C  C     . VAL   B  1  603  ? 26.647  13.213  72.250  1.00 21.49 ? 601  VAL   B C     1 
ATOM   13363 O  O     . VAL   B  1  603  ? 25.883  12.270  72.018  1.00 21.58 ? 601  VAL   B O     1 
ATOM   13364 C  CB    . VAL   B  1  603  ? 28.855  12.259  71.510  1.00 21.38 ? 601  VAL   B CB    1 
ATOM   13365 C  CG1   . VAL   B  1  603  ? 28.805  13.101  70.229  1.00 21.93 ? 601  VAL   B CG1   1 
ATOM   13366 C  CG2   . VAL   B  1  603  ? 30.298  11.991  71.939  1.00 21.66 ? 601  VAL   B CG2   1 
ATOM   13367 N  N     . VAL   B  1  604  ? 26.260  14.480  72.204  1.00 18.79 ? 602  VAL   B N     1 
ATOM   13368 C  CA    . VAL   B  1  604  ? 24.881  14.823  71.886  1.00 17.60 ? 602  VAL   B CA    1 
ATOM   13369 C  C     . VAL   B  1  604  ? 24.665  14.916  70.391  1.00 19.10 ? 602  VAL   B C     1 
ATOM   13370 O  O     . VAL   B  1  604  ? 23.631  14.484  69.885  1.00 19.30 ? 602  VAL   B O     1 
ATOM   13371 C  CB    . VAL   B  1  604  ? 24.504  16.130  72.591  1.00 18.46 ? 602  VAL   B CB    1 
ATOM   13372 C  CG1   . VAL   B  1  604  ? 23.025  16.403  72.403  1.00 18.06 ? 602  VAL   B CG1   1 
ATOM   13373 C  CG2   . VAL   B  1  604  ? 24.864  16.036  74.064  1.00 18.67 ? 602  VAL   B CG2   1 
ATOM   13374 N  N     . GLY   B  1  605  ? 25.629  15.449  69.660  1.00 18.34 ? 603  GLY   B N     1 
ATOM   13375 C  CA    . GLY   B  1  605  ? 25.429  15.644  68.244  1.00 19.38 ? 603  GLY   B CA    1 
ATOM   13376 C  C     . GLY   B  1  605  ? 26.639  16.286  67.626  1.00 19.38 ? 603  GLY   B C     1 
ATOM   13377 O  O     . GLY   B  1  605  ? 27.730  16.269  68.199  1.00 19.38 ? 603  GLY   B O     1 
ATOM   13378 N  N     . SER   B  1  606  ? 26.436  16.857  66.450  1.00 18.10 ? 604  SER   B N     1 
ATOM   13379 C  CA    A SER   B  1  606  ? 27.527  17.459  65.705  0.30 19.73 ? 604  SER   B CA    1 
ATOM   13380 C  CA    B SER   B  1  606  ? 27.520  17.444  65.678  0.33 19.72 ? 604  SER   B CA    1 
ATOM   13381 C  CA    C SER   B  1  606  ? 27.511  17.427  65.653  0.37 19.72 ? 604  SER   B CA    1 
ATOM   13382 C  C     . SER   B  1  606  ? 27.062  18.773  65.108  1.00 18.88 ? 604  SER   B C     1 
ATOM   13383 O  O     . SER   B  1  606  ? 25.909  18.917  64.696  1.00 20.17 ? 604  SER   B O     1 
ATOM   13384 C  CB    A SER   B  1  606  ? 28.036  16.536  64.596  0.30 22.33 ? 604  SER   B CB    1 
ATOM   13385 C  CB    B SER   B  1  606  ? 27.946  16.523  64.529  0.33 22.30 ? 604  SER   B CB    1 
ATOM   13386 C  CB    C SER   B  1  606  ? 27.825  16.485  64.487  0.37 22.25 ? 604  SER   B CB    1 
ATOM   13387 O  OG    A SER   B  1  606  ? 27.020  16.275  63.651  0.30 22.87 ? 604  SER   B OG    1 
ATOM   13388 O  OG    B SER   B  1  606  ? 28.472  15.303  65.024  0.33 25.30 ? 604  SER   B OG    1 
ATOM   13389 O  OG    C SER   B  1  606  ? 28.643  17.108  63.525  0.37 24.41 ? 604  SER   B OG    1 
ATOM   13390 N  N     . VAL   B  1  607  ? 27.962  19.746  65.093  1.00 17.77 ? 605  VAL   B N     1 
ATOM   13391 C  CA    . VAL   B  1  607  ? 27.669  21.056  64.534  1.00 16.91 ? 605  VAL   B CA    1 
ATOM   13392 C  C     . VAL   B  1  607  ? 28.675  21.356  63.437  1.00 17.80 ? 605  VAL   B C     1 
ATOM   13393 O  O     . VAL   B  1  607  ? 29.883  21.175  63.618  1.00 18.79 ? 605  VAL   B O     1 
ATOM   13394 C  CB    . VAL   B  1  607  ? 27.633  22.173  65.594  1.00 17.07 ? 605  VAL   B CB    1 
ATOM   13395 C  CG1   . VAL   B  1  607  ? 28.957  22.248  66.381  1.00 18.13 ? 605  VAL   B CG1   1 
ATOM   13396 C  CG2   . VAL   B  1  607  ? 27.330  23.504  64.925  1.00 18.58 ? 605  VAL   B CG2   1 
ATOM   13397 N  N     . THR   B  1  608  ? 28.173  21.797  62.301  1.00 17.27 ? 606  THR   B N     1 
ATOM   13398 C  CA    . THR   B  1  608  ? 29.002  22.305  61.226  1.00 17.69 ? 606  THR   B CA    1 
ATOM   13399 C  C     . THR   B  1  608  ? 28.873  23.818  61.252  1.00 17.55 ? 606  THR   B C     1 
ATOM   13400 O  O     . THR   B  1  608  ? 27.773  24.355  61.108  1.00 19.23 ? 606  THR   B O     1 
ATOM   13401 C  CB    . THR   B  1  608  ? 28.520  21.731  59.900  1.00 18.83 ? 606  THR   B CB    1 
ATOM   13402 O  OG1   . THR   B  1  608  ? 28.665  20.307  59.938  1.00 20.29 ? 606  THR   B OG1   1 
ATOM   13403 C  CG2   . THR   B  1  608  ? 29.321  22.296  58.748  1.00 20.42 ? 606  THR   B CG2   1 
ATOM   13404 N  N     . GLU   B  1  609  ? 29.990  24.496  61.446  1.00 18.74 ? 607  GLU   B N     1 
ATOM   13405 C  CA    . GLU   B  1  609  ? 29.933  25.925  61.658  1.00 19.47 ? 607  GLU   B CA    1 
ATOM   13406 C  C     . GLU   B  1  609  ? 30.111  26.681  60.346  1.00 18.37 ? 607  GLU   B C     1 
ATOM   13407 O  O     . GLU   B  1  609  ? 30.645  26.165  59.359  1.00 20.60 ? 607  GLU   B O     1 
ATOM   13408 C  CB    . GLU   B  1  609  ? 30.908  26.342  62.761  1.00 22.32 ? 607  GLU   B CB    1 
ATOM   13409 C  CG    . GLU   B  1  609  ? 30.457  25.746  64.099  1.00 24.28 ? 607  GLU   B CG    1 
ATOM   13410 C  CD    . GLU   B  1  609  ? 31.306  26.153  65.285  1.00 29.63 ? 607  GLU   B CD    1 
ATOM   13411 O  OE1   . GLU   B  1  609  ? 32.512  26.442  65.102  1.00 32.36 ? 607  GLU   B OE1   1 
ATOM   13412 O  OE2   . GLU   B  1  609  ? 30.762  26.168  66.407  1.00 26.18 ? 607  GLU   B OE2   1 
ATOM   13413 N  N     . THR   B  1  610  ? 29.605  27.905  60.340  1.00 17.82 ? 608  THR   B N     1 
ATOM   13414 C  CA    . THR   B  1  610  ? 29.451  28.688  59.123  1.00 18.23 ? 608  THR   B CA    1 
ATOM   13415 C  C     . THR   B  1  610  ? 30.725  29.465  58.836  1.00 20.57 ? 608  THR   B C     1 
ATOM   13416 O  O     . THR   B  1  610  ? 31.269  30.123  59.724  1.00 19.87 ? 608  THR   B O     1 
ATOM   13417 C  CB    . THR   B  1  610  ? 28.304  29.680  59.311  1.00 17.74 ? 608  THR   B CB    1 
ATOM   13418 O  OG1   . THR   B  1  610  ? 27.146  28.997  59.807  1.00 18.67 ? 608  THR   B OG1   1 
ATOM   13419 C  CG2   . THR   B  1  610  ? 27.976  30.345  57.993  1.00 18.90 ? 608  THR   B CG2   1 
ATOM   13420 N  N     . SER   B  1  611  ? 31.180  29.422  57.594  1.00 18.84 ? 609  SER   B N     1 
ATOM   13421 C  CA    . SER   B  1  611  ? 32.277  30.301  57.210  1.00 20.87 ? 609  SER   B CA    1 
ATOM   13422 C  C     . SER   B  1  611  ? 31.780  31.739  57.123  1.00 23.05 ? 609  SER   B C     1 
ATOM   13423 O  O     . SER   B  1  611  ? 30.598  31.999  56.883  1.00 19.23 ? 609  SER   B O     1 
ATOM   13424 C  CB    . SER   B  1  611  ? 32.851  29.881  55.859  1.00 21.15 ? 609  SER   B CB    1 
ATOM   13425 O  OG    . SER   B  1  611  ? 31.942  30.205  54.821  1.00 22.36 ? 609  SER   B OG    1 
ATOM   13426 N  N     . GLU   B  1  612  ? 32.688  32.689  57.336  1.00 21.77 ? 610  GLU   B N     1 
ATOM   13427 C  CA    . GLU   B  1  612  ? 32.301  34.088  57.197  1.00 21.97 ? 610  GLU   B CA    1 
ATOM   13428 C  C     . GLU   B  1  612  ? 31.794  34.384  55.789  1.00 23.61 ? 610  GLU   B C     1 
ATOM   13429 O  O     . GLU   B  1  612  ? 30.855  35.171  55.615  1.00 22.98 ? 610  GLU   B O     1 
ATOM   13430 C  CB    . GLU   B  1  612  ? 33.447  35.013  57.613  1.00 26.42 ? 610  GLU   B CB    1 
ATOM   13431 C  CG    . GLU   B  1  612  ? 33.826  34.847  59.087  1.00 30.79 ? 610  GLU   B CG    1 
ATOM   13432 C  CD    . GLU   B  1  612  ? 34.929  35.794  59.531  1.00 34.74 ? 610  GLU   B CD    1 
ATOM   13433 O  OE1   . GLU   B  1  612  ? 35.141  36.821  58.852  1.00 48.38 ? 610  GLU   B OE1   1 
ATOM   13434 O  OE2   . GLU   B  1  612  ? 35.578  35.506  60.558  1.00 37.66 ? 610  GLU   B OE2   1 
ATOM   13435 N  N     . GLU   B  1  613  ? 32.369  33.730  54.778  1.00 23.48 ? 611  GLU   B N     1 
ATOM   13436 C  CA    . GLU   B  1  613  ? 31.877  33.913  53.416  1.00 23.13 ? 611  GLU   B CA    1 
ATOM   13437 C  C     . GLU   B  1  613  ? 30.433  33.441  53.289  1.00 22.04 ? 611  GLU   B C     1 
ATOM   13438 O  O     . GLU   B  1  613  ? 29.607  34.108  52.661  1.00 22.99 ? 611  GLU   B O     1 
ATOM   13439 C  CB    . GLU   B  1  613  ? 32.786  33.196  52.414  1.00 25.92 ? 611  GLU   B CB    1 
ATOM   13440 N  N     . ASP   B  1  614  ? 30.105  32.298  53.895  1.00 20.39 ? 612  ASP   B N     1 
ATOM   13441 C  CA    . ASP   B  1  614  ? 28.734  31.813  53.810  1.00 20.14 ? 612  ASP   B CA    1 
ATOM   13442 C  C     . ASP   B  1  614  ? 27.787  32.649  54.651  1.00 20.33 ? 612  ASP   B C     1 
ATOM   13443 O  O     . ASP   B  1  614  ? 26.604  32.769  54.309  1.00 18.72 ? 612  ASP   B O     1 
ATOM   13444 C  CB    . ASP   B  1  614  ? 28.665  30.334  54.174  1.00 20.63 ? 612  ASP   B CB    1 
ATOM   13445 C  CG    . ASP   B  1  614  ? 29.127  29.448  53.033  1.00 23.26 ? 612  ASP   B CG    1 
ATOM   13446 O  OD1   . ASP   B  1  614  ? 29.027  29.898  51.865  1.00 29.22 ? 612  ASP   B OD1   1 
ATOM   13447 O  OD2   . ASP   B  1  614  ? 29.585  28.321  53.291  1.00 24.43 ? 612  ASP   B OD2   1 
ATOM   13448 N  N     . ALA   B  1  615  ? 28.276  33.242  55.738  1.00 19.62 ? 613  ALA   B N     1 
ATOM   13449 C  CA    . ALA   B  1  615  ? 27.432  34.162  56.492  1.00 19.04 ? 613  ALA   B CA    1 
ATOM   13450 C  C     . ALA   B  1  615  ? 27.037  35.351  55.629  1.00 18.99 ? 613  ALA   B C     1 
ATOM   13451 O  O     . ALA   B  1  615  ? 25.866  35.725  55.570  1.00 17.96 ? 613  ALA   B O     1 
ATOM   13452 C  CB    . ALA   B  1  615  ? 28.150  34.607  57.765  1.00 20.60 ? 613  ALA   B CB    1 
ATOM   13453 N  N     . ARG   B  1  616  ? 27.997  35.927  54.909  1.00 21.23 ? 614  ARG   B N     1 
ATOM   13454 C  CA    . ARG   B  1  616  ? 27.666  37.033  54.020  1.00 19.31 ? 614  ARG   B CA    1 
ATOM   13455 C  C     . ARG   B  1  616  ? 26.752  36.581  52.888  1.00 18.73 ? 614  ARG   B C     1 
ATOM   13456 O  O     . ARG   B  1  616  ? 25.814  37.297  52.515  1.00 19.63 ? 614  ARG   B O     1 
ATOM   13457 C  CB    . ARG   B  1  616  ? 28.944  37.669  53.483  1.00 23.28 ? 614  ARG   B CB    1 
ATOM   13458 C  CG    . ARG   B  1  616  ? 29.613  38.564  54.509  1.00 24.46 ? 614  ARG   B CG    1 
ATOM   13459 C  CD    . ARG   B  1  616  ? 30.789  39.316  53.911  1.00 28.89 ? 614  ARG   B CD    1 
ATOM   13460 N  NE    . ARG   B  1  616  ? 31.911  38.422  53.667  1.00 32.96 ? 614  ARG   B NE    1 
ATOM   13461 C  CZ    . ARG   B  1  616  ? 32.757  38.018  54.603  1.00 33.39 ? 614  ARG   B CZ    1 
ATOM   13462 N  NH1   . ARG   B  1  616  ? 32.636  38.414  55.862  1.00 31.89 ? 614  ARG   B NH1   1 
ATOM   13463 N  NH2   . ARG   B  1  616  ? 33.746  37.197  54.268  1.00 32.27 ? 614  ARG   B NH2   1 
ATOM   13464 N  N     . ARG   B  1  617  ? 27.011  35.396  52.331  1.00 18.33 ? 615  ARG   B N     1 
ATOM   13465 C  CA    . ARG   B  1  617  ? 26.133  34.864  51.297  1.00 20.28 ? 615  ARG   B CA    1 
ATOM   13466 C  C     . ARG   B  1  617  ? 24.711  34.713  51.822  1.00 18.78 ? 615  ARG   B C     1 
ATOM   13467 O  O     . ARG   B  1  617  ? 23.742  35.017  51.118  1.00 19.95 ? 615  ARG   B O     1 
ATOM   13468 C  CB    . ARG   B  1  617  ? 26.672  33.523  50.794  1.00 23.61 ? 615  ARG   B CB    1 
ATOM   13469 C  CG    . ARG   B  1  617  ? 25.843  32.919  49.673  1.00 22.11 ? 615  ARG   B CG    1 
ATOM   13470 C  CD    . ARG   B  1  617  ? 26.638  31.887  48.895  1.00 27.87 ? 615  ARG   B CD    1 
ATOM   13471 N  NE    . ARG   B  1  617  ? 26.799  30.634  49.619  1.00 33.47 ? 615  ARG   B NE    1 
ATOM   13472 C  CZ    . ARG   B  1  617  ? 25.951  29.617  49.536  1.00 38.56 ? 615  ARG   B CZ    1 
ATOM   13473 N  NH1   . ARG   B  1  617  ? 24.860  29.685  48.785  1.00 36.49 ? 615  ARG   B NH1   1 
ATOM   13474 N  NH2   . ARG   B  1  617  ? 26.197  28.508  50.230  1.00 41.96 ? 615  ARG   B NH2   1 
ATOM   13475 N  N     . ALA   B  1  618  ? 24.565  34.253  53.063  1.00 17.74 ? 616  ALA   B N     1 
ATOM   13476 C  CA    . ALA   B  1  618  ? 23.230  34.103  53.626  1.00 16.29 ? 616  ALA   B CA    1 
ATOM   13477 C  C     . ALA   B  1  618  ? 22.506  35.441  53.683  1.00 16.27 ? 616  ALA   B C     1 
ATOM   13478 O  O     . ALA   B  1  618  ? 21.309  35.522  53.388  1.00 16.89 ? 616  ALA   B O     1 
ATOM   13479 C  CB    . ALA   B  1  618  ? 23.328  33.484  55.019  1.00 16.94 ? 616  ALA   B CB    1 
ATOM   13480 N  N     . VAL   B  1  619  ? 23.206  36.506  54.071  1.00 18.12 ? 617  VAL   B N     1 
ATOM   13481 C  CA    . VAL   B  1  619  ? 22.547  37.806  54.141  1.00 17.39 ? 617  VAL   B CA    1 
ATOM   13482 C  C     . VAL   B  1  619  ? 22.109  38.251  52.759  1.00 18.54 ? 617  VAL   B C     1 
ATOM   13483 O  O     . VAL   B  1  619  ? 21.019  38.797  52.588  1.00 19.13 ? 617  VAL   B O     1 
ATOM   13484 C  CB    . VAL   B  1  619  ? 23.427  38.855  54.844  1.00 17.77 ? 617  VAL   B CB    1 
ATOM   13485 C  CG1   . VAL   B  1  619  ? 22.729  40.207  54.883  1.00 21.27 ? 617  VAL   B CG1   1 
ATOM   13486 C  CG2   . VAL   B  1  619  ? 23.738  38.401  56.243  1.00 18.85 ? 617  VAL   B CG2   1 
ATOM   13487 N  N     . ARG   B  1  620  ? 22.942  37.998  51.747  1.00 19.30 ? 618  ARG   B N     1 
ATOM   13488 C  CA    . ARG   B  1  620  ? 22.549  38.326  50.383  1.00 20.31 ? 618  ARG   B CA    1 
ATOM   13489 C  C     . ARG   B  1  620  ? 21.321  37.535  49.953  1.00 17.85 ? 618  ARG   B C     1 
ATOM   13490 O  O     . ARG   B  1  620  ? 20.409  38.086  49.327  1.00 19.71 ? 618  ARG   B O     1 
ATOM   13491 C  CB    . ARG   B  1  620  ? 23.722  38.107  49.424  1.00 22.42 ? 618  ARG   B CB    1 
ATOM   13492 C  CG    . ARG   B  1  620  ? 24.739  39.226  49.504  1.00 30.62 ? 618  ARG   B CG    1 
ATOM   13493 C  CD    . ARG   B  1  620  ? 25.822  39.122  48.441  1.00 36.98 ? 618  ARG   B CD    1 
ATOM   13494 N  NE    . ARG   B  1  620  ? 27.006  38.460  48.972  1.00 42.88 ? 618  ARG   B NE    1 
ATOM   13495 C  CZ    . ARG   B  1  620  ? 27.333  37.200  48.724  1.00 35.11 ? 618  ARG   B CZ    1 
ATOM   13496 N  NH1   . ARG   B  1  620  ? 26.616  36.447  47.903  1.00 41.06 ? 618  ARG   B NH1   1 
ATOM   13497 N  NH2   . ARG   B  1  620  ? 28.404  36.683  49.311  1.00 38.27 ? 618  ARG   B NH2   1 
ATOM   13498 N  N     . LEU   B  1  621  ? 21.276  36.241  50.283  1.00 19.00 ? 619  LEU   B N     1 
ATOM   13499 C  CA    . LEU   B  1  621  ? 20.103  35.435  49.957  1.00 19.09 ? 619  LEU   B CA    1 
ATOM   13500 C  C     . LEU   B  1  621  ? 18.869  35.955  50.679  1.00 19.35 ? 619  LEU   B C     1 
ATOM   13501 O  O     . LEU   B  1  621  ? 17.767  35.957  50.118  1.00 19.54 ? 619  LEU   B O     1 
ATOM   13502 C  CB    . LEU   B  1  621  ? 20.354  33.971  50.324  1.00 20.27 ? 619  LEU   B CB    1 
ATOM   13503 C  CG    . LEU   B  1  621  ? 21.412  33.250  49.479  1.00 21.04 ? 619  LEU   B CG    1 
ATOM   13504 C  CD1   . LEU   B  1  621  ? 21.739  31.882  50.075  1.00 23.54 ? 619  LEU   B CD1   1 
ATOM   13505 C  CD2   . LEU   B  1  621  ? 20.924  33.111  48.039  1.00 26.96 ? 619  LEU   B CD2   1 
ATOM   13506 N  N     . ALA   B  1  622  ? 19.033  36.381  51.932  1.00 17.47 ? 620  ALA   B N     1 
ATOM   13507 C  CA    . ALA   B  1  622  ? 17.912  36.941  52.676  1.00 18.23 ? 620  ALA   B CA    1 
ATOM   13508 C  C     . ALA   B  1  622  ? 17.430  38.238  52.038  1.00 18.87 ? 620  ALA   B C     1 
ATOM   13509 O  O     . ALA   B  1  622  ? 16.219  38.461  51.915  1.00 16.91 ? 620  ALA   B O     1 
ATOM   13510 C  CB    . ALA   B  1  622  ? 18.305  37.156  54.141  1.00 19.23 ? 620  ALA   B CB    1 
ATOM   13511 N  N     . ALA   B  1  623  ? 18.359  39.093  51.609  1.00 18.29 ? 621  ALA   B N     1 
ATOM   13512 C  CA    . ALA   B  1  623  ? 17.970  40.339  50.960  1.00 18.94 ? 621  ALA   B CA    1 
ATOM   13513 C  C     . ALA   B  1  623  ? 17.206  40.064  49.677  1.00 19.35 ? 621  ALA   B C     1 
ATOM   13514 O  O     . ALA   B  1  623  ? 16.181  40.703  49.406  1.00 20.60 ? 621  ALA   B O     1 
ATOM   13515 C  CB    . ALA   B  1  623  ? 19.213  41.177  50.671  1.00 19.09 ? 621  ALA   B CB    1 
ATOM   13516 N  N     . ASP   B  1  624  ? 17.661  39.081  48.897  1.00 20.09 ? 622  ASP   B N     1 
ATOM   13517 C  CA    . ASP   B  1  624  ? 16.971  38.747  47.655  1.00 20.72 ? 622  ASP   B CA    1 
ATOM   13518 C  C     . ASP   B  1  624  ? 15.535  38.324  47.917  1.00 22.83 ? 622  ASP   B C     1 
ATOM   13519 O  O     . ASP   B  1  624  ? 14.628  38.680  47.156  1.00 28.03 ? 622  ASP   B O     1 
ATOM   13520 C  CB    . ASP   B  1  624  ? 17.707  37.613  46.937  1.00 27.95 ? 622  ASP   B CB    1 
ATOM   13521 C  CG    . ASP   B  1  624  ? 19.096  38.005  46.468  1.00 34.15 ? 622  ASP   B CG    1 
ATOM   13522 O  OD1   . ASP   B  1  624  ? 19.395  39.217  46.355  1.00 37.33 ? 622  ASP   B OD1   1 
ATOM   13523 O  OD2   . ASP   B  1  624  ? 19.891  37.077  46.194  1.00 36.97 ? 622  ASP   B OD2   1 
ATOM   13524 N  N     . ALA   B  1  625  ? 15.313  37.562  48.978  1.00 24.18 ? 623  ALA   B N     1 
ATOM   13525 C  CA    . ALA   B  1  625  ? 14.002  37.023  49.295  1.00 27.87 ? 623  ALA   B CA    1 
ATOM   13526 C  C     . ALA   B  1  625  ? 13.170  37.959  50.148  1.00 24.24 ? 623  ALA   B C     1 
ATOM   13527 O  O     . ALA   B  1  625  ? 12.006  37.646  50.433  1.00 24.82 ? 623  ALA   B O     1 
ATOM   13528 C  CB    . ALA   B  1  625  ? 14.161  35.712  50.049  1.00 33.36 ? 623  ALA   B CB    1 
ATOM   13529 N  N     . ALA   B  1  626  ? 13.740  39.075  50.592  1.00 21.57 ? 624  ALA   B N     1 
ATOM   13530 C  CA    . ALA   B  1  626  ? 13.011  39.950  51.505  1.00 20.03 ? 624  ALA   B CA    1 
ATOM   13531 C  C     . ALA   B  1  626  ? 11.667  40.390  50.949  1.00 19.88 ? 624  ALA   B C     1 
ATOM   13532 O  O     . ALA   B  1  626  ? 10.669  40.310  51.683  1.00 20.22 ? 624  ALA   B O     1 
ATOM   13533 C  CB    . ALA   B  1  626  ? 13.890  41.118  51.963  1.00 19.56 ? 624  ALA   B CB    1 
ATOM   13534 N  N     . PRO   B  1  627  ? 11.544  40.823  49.690  1.00 20.71 ? 625  PRO   B N     1 
ATOM   13535 C  CA    . PRO   B  1  627  ? 10.216  41.250  49.222  1.00 20.70 ? 625  PRO   B CA    1 
ATOM   13536 C  C     . PRO   B  1  627  ? 9.184   40.138  49.235  1.00 21.02 ? 625  PRO   B C     1 
ATOM   13537 O  O     . PRO   B  1  627  ? 8.011   40.395  49.548  1.00 21.15 ? 625  PRO   B O     1 
ATOM   13538 C  CB    . PRO   B  1  627  ? 10.485  41.763  47.797  1.00 23.87 ? 625  PRO   B CB    1 
ATOM   13539 C  CG    . PRO   B  1  627  ? 11.942  42.050  47.755  1.00 26.22 ? 625  PRO   B CG    1 
ATOM   13540 C  CD    . PRO   B  1  627  ? 12.590  41.076  48.683  1.00 22.41 ? 625  PRO   B CD    1 
ATOM   13541 N  N     . ASP   B  1  628  ? 9.579   38.905  48.903  1.00 19.66 ? 626  ASP   B N     1 
ATOM   13542 C  CA    . ASP   B  1  628  ? 8.609   37.819  48.847  1.00 21.79 ? 626  ASP   B CA    1 
ATOM   13543 C  C     . ASP   B  1  628  ? 8.070   37.497  50.230  1.00 21.51 ? 626  ASP   B C     1 
ATOM   13544 O  O     . ASP   B  1  628  ? 6.888   37.171  50.383  1.00 22.50 ? 626  ASP   B O     1 
ATOM   13545 C  CB    . ASP   B  1  628  ? 9.221   36.564  48.233  1.00 24.06 ? 626  ASP   B CB    1 
ATOM   13546 C  CG    . ASP   B  1  628  ? 9.497   36.712  46.754  1.00 29.87 ? 626  ASP   B CG    1 
ATOM   13547 O  OD1   . ASP   B  1  628  ? 8.821   37.532  46.099  1.00 31.79 ? 626  ASP   B OD1   1 
ATOM   13548 O  OD2   . ASP   B  1  628  ? 10.394  36.005  46.264  1.00 35.91 ? 626  ASP   B OD2   1 
ATOM   13549 N  N     . TRP   B  1  629  ? 8.916   37.575  51.250  1.00 19.05 ? 627  TRP   B N     1 
ATOM   13550 C  CA    . TRP   B  1  629  ? 8.415   37.294  52.583  1.00 18.44 ? 627  TRP   B CA    1 
ATOM   13551 C  C     . TRP   B  1  629  ? 7.593   38.455  53.108  1.00 17.77 ? 627  TRP   B C     1 
ATOM   13552 O  O     . TRP   B  1  629  ? 6.566   38.243  53.755  1.00 17.63 ? 627  TRP   B O     1 
ATOM   13553 C  CB    . TRP   B  1  629  ? 9.583   36.954  53.506  1.00 17.00 ? 627  TRP   B CB    1 
ATOM   13554 C  CG    . TRP   B  1  629  ? 9.145   36.666  54.894  1.00 15.18 ? 627  TRP   B CG    1 
ATOM   13555 C  CD1   . TRP   B  1  629  ? 9.512   37.341  56.029  1.00 17.38 ? 627  TRP   B CD1   1 
ATOM   13556 C  CD2   . TRP   B  1  629  ? 8.241   35.644  55.309  1.00 17.81 ? 627  TRP   B CD2   1 
ATOM   13557 N  NE1   . TRP   B  1  629  ? 8.896   36.789  57.120  1.00 16.25 ? 627  TRP   B NE1   1 
ATOM   13558 C  CE2   . TRP   B  1  629  ? 8.102   35.751  56.706  1.00 16.62 ? 627  TRP   B CE2   1 
ATOM   13559 C  CE3   . TRP   B  1  629  ? 7.520   34.656  54.636  1.00 18.59 ? 627  TRP   B CE3   1 
ATOM   13560 C  CZ2   . TRP   B  1  629  ? 7.278   34.899  57.438  1.00 16.24 ? 627  TRP   B CZ2   1 
ATOM   13561 C  CZ3   . TRP   B  1  629  ? 6.706   33.818  55.367  1.00 18.30 ? 627  TRP   B CZ3   1 
ATOM   13562 C  CH2   . TRP   B  1  629  ? 6.588   33.945  56.746  1.00 18.43 ? 627  TRP   B CH2   1 
ATOM   13563 N  N     . ALA   B  1  630  ? 7.999   39.686  52.803  1.00 18.04 ? 628  ALA   B N     1 
ATOM   13564 C  CA    . ALA   B  1  630  ? 7.222   40.835  53.238  1.00 18.62 ? 628  ALA   B CA    1 
ATOM   13565 C  C     . ALA   B  1  630  ? 5.833   40.801  52.627  1.00 19.92 ? 628  ALA   B C     1 
ATOM   13566 O  O     . ALA   B  1  630  ? 4.880   41.308  53.226  1.00 21.63 ? 628  ALA   B O     1 
ATOM   13567 C  CB    . ALA   B  1  630  ? 7.939   42.121  52.844  1.00 21.81 ? 628  ALA   B CB    1 
ATOM   13568 N  N     . ALA   B  1  631  ? 5.702   40.192  51.448  1.00 18.60 ? 629  ALA   B N     1 
ATOM   13569 C  CA    . ALA   B  1  631  ? 4.426   40.137  50.756  1.00 18.53 ? 629  ALA   B CA    1 
ATOM   13570 C  C     . ALA   B  1  631  ? 3.493   39.074  51.312  1.00 21.31 ? 629  ALA   B C     1 
ATOM   13571 O  O     . ALA   B  1  631  ? 2.305   39.086  50.980  1.00 22.45 ? 629  ALA   B O     1 
ATOM   13572 C  CB    . ALA   B  1  631  ? 4.661   39.903  49.259  1.00 21.43 ? 629  ALA   B CB    1 
ATOM   13573 N  N     . VAL   B  1  632  ? 3.984   38.163  52.141  1.00 19.53 ? 630  VAL   B N     1 
ATOM   13574 C  CA    . VAL   B  1  632  ? 3.084   37.228  52.817  1.00 18.83 ? 630  VAL   B CA    1 
ATOM   13575 C  C     . VAL   B  1  632  ? 2.277   38.010  53.842  1.00 19.20 ? 630  VAL   B C     1 
ATOM   13576 O  O     . VAL   B  1  632  ? 2.872   38.701  54.693  1.00 19.16 ? 630  VAL   B O     1 
ATOM   13577 C  CB    . VAL   B  1  632  ? 3.878   36.115  53.491  1.00 18.83 ? 630  VAL   B CB    1 
ATOM   13578 C  CG1   . VAL   B  1  632  ? 2.921   35.193  54.251  1.00 20.33 ? 630  VAL   B CG1   1 
ATOM   13579 C  CG2   . VAL   B  1  632  ? 4.672   35.343  52.463  1.00 20.04 ? 630  VAL   B CG2   1 
ATOM   13580 N  N     . PRO   B  1  633  ? 0.948   37.961  53.800  1.00 18.58 ? 631  PRO   B N     1 
ATOM   13581 C  CA    . PRO   B  1  633  ? 0.164   38.804  54.689  1.00 18.51 ? 631  PRO   B CA    1 
ATOM   13582 C  C     . PRO   B  1  633  ? 0.520   38.530  56.137  1.00 18.09 ? 631  PRO   B C     1 
ATOM   13583 O  O     . PRO   B  1  633  ? 0.804   37.380  56.519  1.00 17.97 ? 631  PRO   B O     1 
ATOM   13584 C  CB    . PRO   B  1  633  ? -1.277  38.374  54.392  1.00 19.71 ? 631  PRO   B CB    1 
ATOM   13585 C  CG    . PRO   B  1  633  ? -1.237  37.866  52.993  1.00 22.72 ? 631  PRO   B CG    1 
ATOM   13586 C  CD    . PRO   B  1  633  ? 0.110   37.192  52.867  1.00 19.15 ? 631  PRO   B CD    1 
ATOM   13587 N  N     . PRO   B  1  634  ? 0.481   39.558  56.984  1.00 17.63 ? 632  PRO   B N     1 
ATOM   13588 C  CA    . PRO   B  1  634  ? 0.770   39.346  58.409  1.00 17.83 ? 632  PRO   B CA    1 
ATOM   13589 C  C     . PRO   B  1  634  ? -0.015  38.209  59.036  1.00 17.45 ? 632  PRO   B C     1 
ATOM   13590 O  O     . PRO   B  1  634  ? 0.566   37.444  59.809  1.00 17.43 ? 632  PRO   B O     1 
ATOM   13591 C  CB    . PRO   B  1  634  ? 0.424   40.703  59.040  1.00 19.58 ? 632  PRO   B CB    1 
ATOM   13592 C  CG    . PRO   B  1  634  ? 0.666   41.686  57.946  1.00 23.23 ? 632  PRO   B CG    1 
ATOM   13593 C  CD    . PRO   B  1  634  ? 0.366   40.986  56.642  1.00 18.41 ? 632  PRO   B CD    1 
ATOM   13594 N  N     . SER   B  1  635  ? -1.303  38.058  58.732  1.00 19.18 ? 633  SER   B N     1 
ATOM   13595 C  CA    . SER   B  1  635  ? -2.044  36.967  59.354  1.00 19.67 ? 633  SER   B CA    1 
ATOM   13596 C  C     . SER   B  1  635  ? -1.499  35.611  58.931  1.00 17.68 ? 633  SER   B C     1 
ATOM   13597 O  O     . SER   B  1  635  ? -1.540  34.655  59.713  1.00 18.27 ? 633  SER   B O     1 
ATOM   13598 C  CB    . SER   B  1  635  ? -3.530  37.065  59.004  1.00 22.49 ? 633  SER   B CB    1 
ATOM   13599 O  OG    . SER   B  1  635  ? -3.715  36.946  57.610  1.00 31.31 ? 633  SER   B OG    1 
ATOM   13600 N  N     . GLU   B  1  636  ? -0.997  35.501  57.698  1.00 18.27 ? 634  GLU   B N     1 
ATOM   13601 C  CA    . GLU   B  1  636  ? -0.421  34.233  57.265  1.00 17.56 ? 634  GLU   B CA    1 
ATOM   13602 C  C     . GLU   B  1  636  ? 0.962   34.016  57.865  1.00 17.93 ? 634  GLU   B C     1 
ATOM   13603 O  O     . GLU   B  1  636  ? 1.325   32.883  58.194  1.00 17.63 ? 634  GLU   B O     1 
ATOM   13604 C  CB    . GLU   B  1  636  ? -0.358  34.153  55.740  1.00 19.63 ? 634  GLU   B CB    1 
ATOM   13605 C  CG    . GLU   B  1  636  ? 0.228   32.829  55.235  1.00 29.00 ? 634  GLU   B CG    1 
ATOM   13606 C  CD    . GLU   B  1  636  ? -0.339  31.602  55.961  1.00 36.24 ? 634  GLU   B CD    1 
ATOM   13607 O  OE1   . GLU   B  1  636  ? -1.587  31.488  56.066  1.00 34.00 ? 634  GLU   B OE1   1 
ATOM   13608 O  OE2   . GLU   B  1  636  ? 0.466   30.758  56.438  1.00 30.96 ? 634  GLU   B OE2   1 
ATOM   13609 N  N     . ARG   B  1  637  ? 1.744   35.081  58.031  1.00 15.80 ? 635  ARG   B N     1 
ATOM   13610 C  CA    . ARG   B  1  637  ? 3.002   34.922  58.749  1.00 16.49 ? 635  ARG   B CA    1 
ATOM   13611 C  C     . ARG   B  1  637  ? 2.729   34.487  60.179  1.00 16.02 ? 635  ARG   B C     1 
ATOM   13612 O  O     . ARG   B  1  637  ? 3.396   33.586  60.708  1.00 16.35 ? 635  ARG   B O     1 
ATOM   13613 C  CB    . ARG   B  1  637  ? 3.792   36.223  58.717  1.00 15.38 ? 635  ARG   B CB    1 
ATOM   13614 C  CG    . ARG   B  1  637  ? 4.021   36.751  57.305  1.00 16.75 ? 635  ARG   B CG    1 
ATOM   13615 C  CD    . ARG   B  1  637  ? 5.094   37.809  57.289  1.00 16.80 ? 635  ARG   B CD    1 
ATOM   13616 N  NE    . ARG   B  1  637  ? 4.733   38.974  58.086  1.00 17.30 ? 635  ARG   B NE    1 
ATOM   13617 C  CZ    . ARG   B  1  637  ? 4.517   40.189  57.606  1.00 17.98 ? 635  ARG   B CZ    1 
ATOM   13618 N  NH1   . ARG   B  1  637  ? 4.453   40.422  56.302  1.00 23.07 ? 635  ARG   B NH1   1 
ATOM   13619 N  NH2   . ARG   B  1  637  ? 4.374   41.201  58.453  1.00 17.77 ? 635  ARG   B NH2   1 
ATOM   13620 N  N     . ALA   B  1  638  ? 1.711   35.087  60.799  1.00 14.59 ? 636  ALA   B N     1 
ATOM   13621 C  CA    . ALA   B  1  638  ? 1.328   34.700  62.149  1.00 15.36 ? 636  ALA   B CA    1 
ATOM   13622 C  C     . ALA   B  1  638  ? 0.876   33.249  62.199  1.00 15.24 ? 636  ALA   B C     1 
ATOM   13623 O  O     . ALA   B  1  638  ? 1.162   32.543  63.173  1.00 14.81 ? 636  ALA   B O     1 
ATOM   13624 C  CB    . ALA   B  1  638  ? 0.231   35.634  62.671  1.00 17.22 ? 636  ALA   B CB    1 
ATOM   13625 N  N     . ALA   B  1  639  ? 0.166   32.781  61.163  1.00 16.26 ? 637  ALA   B N     1 
ATOM   13626 C  CA    . ALA   B  1  639  ? -0.265  31.387  61.147  1.00 16.61 ? 637  ALA   B CA    1 
ATOM   13627 C  C     . ALA   B  1  639  ? 0.922   30.434  61.125  1.00 15.18 ? 637  ALA   B C     1 
ATOM   13628 O  O     . ALA   B  1  639  ? 0.842   29.336  61.683  1.00 15.63 ? 637  ALA   B O     1 
ATOM   13629 C  CB    . ALA   B  1  639  ? -1.182  31.131  59.950  1.00 17.03 ? 637  ALA   B CB    1 
ATOM   13630 N  N     . CYS   B  1  640  ? 2.017   30.823  60.472  1.00 15.05 ? 638  CYS   B N     1 
ATOM   13631 C  CA    . CYS   B  1  640  ? 3.235   30.022  60.530  1.00 15.17 ? 638  CYS   B CA    1 
ATOM   13632 C  C     . CYS   B  1  640  ? 3.741   29.906  61.953  1.00 14.58 ? 638  CYS   B C     1 
ATOM   13633 O  O     . CYS   B  1  640  ? 4.123   28.822  62.395  1.00 15.10 ? 638  CYS   B O     1 
ATOM   13634 C  CB    . CYS   B  1  640  ? 4.338   30.646  59.671  1.00 14.39 ? 638  CYS   B CB    1 
ATOM   13635 S  SG    . CYS   B  1  640  ? 4.032   30.622  57.918  1.00 17.28 ? 638  CYS   B SG    1 
ATOM   13636 N  N     . LEU   B  1  641  ? 3.769   31.024  62.680  1.00 14.01 ? 639  LEU   B N     1 
ATOM   13637 C  CA    . LEU   B  1  641  ? 4.215   30.971  64.067  1.00 15.11 ? 639  LEU   B CA    1 
ATOM   13638 C  C     . LEU   B  1  641  ? 3.320   30.057  64.881  1.00 14.58 ? 639  LEU   B C     1 
ATOM   13639 O  O     . LEU   B  1  641  ? 3.809   29.243  65.672  1.00 14.69 ? 639  LEU   B O     1 
ATOM   13640 C  CB    . LEU   B  1  641  ? 4.214   32.370  64.674  1.00 14.52 ? 639  LEU   B CB    1 
ATOM   13641 C  CG    . LEU   B  1  641  ? 5.480   33.203  64.500  1.00 15.22 ? 639  LEU   B CG    1 
ATOM   13642 C  CD1   . LEU   B  1  641  ? 5.895   33.405  63.046  1.00 17.79 ? 639  LEU   B CD1   1 
ATOM   13643 C  CD2   . LEU   B  1  641  ? 5.284   34.528  65.224  1.00 14.76 ? 639  LEU   B CD2   1 
ATOM   13644 N  N     . ASP   B  1  642  ? 2.003   30.181  64.704  1.00 13.47 ? 640  ASP   B N     1 
ATOM   13645 C  CA    . ASP   B  1  642  ? 1.083   29.322  65.440  1.00 14.24 ? 640  ASP   B CA    1 
ATOM   13646 C  C     . ASP   B  1  642  ? 1.280   27.856  65.081  1.00 13.36 ? 640  ASP   B C     1 
ATOM   13647 O  O     . ASP   B  1  642  ? 1.213   26.983  65.952  1.00 15.70 ? 640  ASP   B O     1 
ATOM   13648 C  CB    . ASP   B  1  642  ? -0.362  29.737  65.173  1.00 15.48 ? 640  ASP   B CB    1 
ATOM   13649 C  CG    . ASP   B  1  642  ? -0.779  30.939  65.980  1.00 18.23 ? 640  ASP   B CG    1 
ATOM   13650 O  OD1   . ASP   B  1  642  ? -0.132  31.224  67.004  1.00 17.14 ? 640  ASP   B OD1   1 
ATOM   13651 O  OD2   . ASP   B  1  642  ? -1.777  31.586  65.598  1.00 19.06 ? 640  ASP   B OD2   1 
ATOM   13652 N  N     . ARG   B  1  643  ? 1.511   27.556  63.801  1.00 14.57 ? 641  ARG   B N     1 
ATOM   13653 C  CA    . ARG   B  1  643  ? 1.773   26.170  63.440  1.00 15.54 ? 641  ARG   B CA    1 
ATOM   13654 C  C     . ARG   B  1  643  ? 3.066   25.683  64.079  1.00 15.14 ? 641  ARG   B C     1 
ATOM   13655 O  O     . ARG   B  1  643  ? 3.150   24.541  64.549  1.00 16.34 ? 641  ARG   B O     1 
ATOM   13656 C  CB    . ARG   B  1  643  ? 1.834   26.014  61.923  1.00 15.81 ? 641  ARG   B CB    1 
ATOM   13657 C  CG    . ARG   B  1  643  ? 0.462   25.885  61.311  1.00 18.06 ? 641  ARG   B CG    1 
ATOM   13658 C  CD    . ARG   B  1  643  ? 0.535   25.521  59.836  1.00 21.23 ? 641  ARG   B CD    1 
ATOM   13659 N  NE    . ARG   B  1  643  ? 1.249   26.523  59.053  1.00 20.75 ? 641  ARG   B NE    1 
ATOM   13660 C  CZ    . ARG   B  1  643  ? 0.681   27.554  58.446  1.00 20.20 ? 641  ARG   B CZ    1 
ATOM   13661 N  NH1   . ARG   B  1  643  ? -0.630  27.749  58.492  1.00 21.04 ? 641  ARG   B NH1   1 
ATOM   13662 N  NH2   . ARG   B  1  643  ? 1.444   28.405  57.766  1.00 21.42 ? 641  ARG   B NH2   1 
ATOM   13663 N  N     . ALA   B  1  644  ? 4.082   26.535  64.115  1.00 13.86 ? 642  ALA   B N     1 
ATOM   13664 C  CA    . ALA   B  1  644  ? 5.328   26.137  64.746  1.00 15.17 ? 642  ALA   B CA    1 
ATOM   13665 C  C     . ALA   B  1  644  ? 5.110   25.857  66.220  1.00 15.46 ? 642  ALA   B C     1 
ATOM   13666 O  O     . ALA   B  1  644  ? 5.707   24.931  66.783  1.00 14.89 ? 642  ALA   B O     1 
ATOM   13667 C  CB    . ALA   B  1  644  ? 6.370   27.233  64.554  1.00 14.81 ? 642  ALA   B CB    1 
ATOM   13668 N  N     . ALA   B  1  645  ? 4.257   26.659  66.870  1.00 14.73 ? 643  ALA   B N     1 
ATOM   13669 C  CA    . ALA   B  1  645  ? 4.000   26.437  68.284  1.00 16.17 ? 643  ALA   B CA    1 
ATOM   13670 C  C     . ALA   B  1  645  ? 3.322   25.096  68.498  1.00 14.17 ? 643  ALA   B C     1 
ATOM   13671 O  O     . ALA   B  1  645  ? 3.631   24.387  69.462  1.00 15.92 ? 643  ALA   B O     1 
ATOM   13672 C  CB    . ALA   B  1  645  ? 3.155   27.575  68.849  1.00 15.18 ? 643  ALA   B CB    1 
ATOM   13673 N  N     . GLU   B  1  646  ? 2.388   24.736  67.610  1.00 15.16 ? 644  GLU   B N     1 
ATOM   13674 C  CA    . GLU   B  1  646  ? 1.735   23.436  67.713  1.00 16.60 ? 644  GLU   B CA    1 
ATOM   13675 C  C     . GLU   B  1  646  ? 2.745   22.309  67.601  1.00 16.04 ? 644  GLU   B C     1 
ATOM   13676 O  O     . GLU   B  1  646  ? 2.654   21.308  68.320  1.00 17.36 ? 644  GLU   B O     1 
ATOM   13677 C  CB    . GLU   B  1  646  ? 0.686   23.277  66.615  1.00 19.90 ? 644  GLU   B CB    1 
ATOM   13678 C  CG    . GLU   B  1  646  ? -0.505  24.195  66.748  1.00 25.17 ? 644  GLU   B CG    1 
ATOM   13679 C  CD    . GLU   B  1  646  ? -1.250  23.994  68.049  1.00 31.00 ? 644  GLU   B CD    1 
ATOM   13680 O  OE1   . GLU   B  1  646  ? -1.541  22.832  68.403  1.00 37.34 ? 644  GLU   B OE1   1 
ATOM   13681 O  OE2   . GLU   B  1  646  ? -1.536  25.004  68.726  1.00 33.49 ? 644  GLU   B OE2   1 
ATOM   13682 N  N     . LEU   B  1  647  ? 3.705   22.449  66.683  1.00 16.68 ? 645  LEU   B N     1 
ATOM   13683 C  CA    . LEU   B  1  647  ? 4.703   21.407  66.494  1.00 17.75 ? 645  LEU   B CA    1 
ATOM   13684 C  C     . LEU   B  1  647  ? 5.613   21.300  67.703  1.00 17.20 ? 645  LEU   B C     1 
ATOM   13685 O  O     . LEU   B  1  647  ? 5.891   20.195  68.178  1.00 17.67 ? 645  LEU   B O     1 
ATOM   13686 C  CB    . LEU   B  1  647  ? 5.515   21.702  65.237  1.00 16.55 ? 645  LEU   B CB    1 
ATOM   13687 C  CG    . LEU   B  1  647  ? 4.755   21.624  63.921  1.00 18.75 ? 645  LEU   B CG    1 
ATOM   13688 C  CD1   . LEU   B  1  647  ? 5.713   21.919  62.776  1.00 18.44 ? 645  LEU   B CD1   1 
ATOM   13689 C  CD2   . LEU   B  1  647  ? 4.102   20.248  63.768  1.00 21.78 ? 645  LEU   B CD2   1 
ATOM   13690 N  N     . MET   B  1  648  ? 6.048   22.433  68.244  1.00 14.30 ? 646  MET   B N     1 
ATOM   13691 C  CA    . MET   B  1  648  ? 6.882   22.392  69.439  1.00 15.16 ? 646  MET   B CA    1 
ATOM   13692 C  C     . MET   B  1  648  ? 6.123   21.789  70.607  1.00 15.90 ? 646  MET   B C     1 
ATOM   13693 O  O     . MET   B  1  648  ? 6.700   21.072  71.433  1.00 17.61 ? 646  MET   B O     1 
ATOM   13694 C  CB    . MET   B  1  648  ? 7.338   23.798  69.804  1.00 15.93 ? 646  MET   B CB    1 
ATOM   13695 C  CG    . MET   B  1  648  ? 8.393   24.335  68.889  1.00 18.65 ? 646  MET   B CG    1 
ATOM   13696 S  SD    . MET   B  1  648  ? 9.212   25.712  69.692  1.00 18.86 ? 646  MET   B SD    1 
ATOM   13697 C  CE    . MET   B  1  648  ? 10.247  26.239  68.338  1.00 20.68 ? 646  MET   B CE    1 
ATOM   13698 N  N     . GLN   B  1  649  ? 4.830   22.100  70.720  1.00 14.92 ? 647  GLN   B N     1 
ATOM   13699 C  CA    . GLN   B  1  649  ? 4.048   21.532  71.807  1.00 15.20 ? 647  GLN   B CA    1 
ATOM   13700 C  C     . GLN   B  1  649  ? 3.971   20.018  71.675  1.00 16.79 ? 647  GLN   B C     1 
ATOM   13701 O  O     . GLN   B  1  649  ? 4.174   19.290  72.655  1.00 18.63 ? 647  GLN   B O     1 
ATOM   13702 C  CB    . GLN   B  1  649  ? 2.652   22.138  71.791  1.00 15.68 ? 647  GLN   B CB    1 
ATOM   13703 C  CG    . GLN   B  1  649  ? 1.801   21.694  72.960  1.00 17.52 ? 647  GLN   B CG    1 
ATOM   13704 C  CD    . GLN   B  1  649  ? 2.236   22.365  74.248  1.00 15.99 ? 647  GLN   B CD    1 
ATOM   13705 O  OE1   . GLN   B  1  649  ? 1.931   23.540  74.486  1.00 17.92 ? 647  GLN   B OE1   1 
ATOM   13706 N  NE2   . GLN   B  1  649  ? 3.008   21.647  75.062  1.00 17.95 ? 647  GLN   B NE2   1 
ATOM   13707 N  N     . ALA   B  1  650  ? 3.682   19.527  70.467  1.00 16.99 ? 648  ALA   B N     1 
ATOM   13708 C  CA    . ALA   B  1  650  ? 3.553   18.085  70.270  1.00 17.61 ? 648  ALA   B CA    1 
ATOM   13709 C  C     . ALA   B  1  650  ? 4.885   17.369  70.439  1.00 19.34 ? 648  ALA   B C     1 
ATOM   13710 O  O     . ALA   B  1  650  ? 4.919   16.209  70.866  1.00 21.61 ? 648  ALA   B O     1 
ATOM   13711 C  CB    . ALA   B  1  650  ? 2.969   17.790  68.890  1.00 20.61 ? 648  ALA   B CB    1 
ATOM   13712 N  N     . ARG   B  1  651  ? 5.987   18.034  70.115  1.00 17.63 ? 649  ARG   B N     1 
ATOM   13713 C  CA    . ARG   B  1  651  ? 7.299   17.419  70.169  1.00 17.40 ? 649  ARG   B CA    1 
ATOM   13714 C  C     . ARG   B  1  651  ? 8.060   17.787  71.422  1.00 17.30 ? 649  ARG   B C     1 
ATOM   13715 O  O     . ARG   B  1  651  ? 9.254   17.487  71.527  1.00 17.87 ? 649  ARG   B O     1 
ATOM   13716 C  CB    . ARG   B  1  651  ? 8.081   17.816  68.929  1.00 18.88 ? 649  ARG   B CB    1 
ATOM   13717 C  CG    . ARG   B  1  651  ? 7.352   17.347  67.706  1.00 20.40 ? 649  ARG   B CG    1 
ATOM   13718 C  CD    . ARG   B  1  651  ? 7.950   17.901  66.450  1.00 19.47 ? 649  ARG   B CD    1 
ATOM   13719 N  NE    . ARG   B  1  651  ? 7.078   17.574  65.335  1.00 22.08 ? 649  ARG   B NE    1 
ATOM   13720 C  CZ    . ARG   B  1  651  ? 7.287   17.978  64.094  1.00 20.86 ? 649  ARG   B CZ    1 
ATOM   13721 N  NH1   . ARG   B  1  651  ? 8.361   18.687  63.775  1.00 19.97 ? 649  ARG   B NH1   1 
ATOM   13722 N  NH2   . ARG   B  1  651  ? 6.408   17.647  63.147  1.00 20.59 ? 649  ARG   B NH2   1 
ATOM   13723 N  N     . MET   B  1  652  ? 7.400   18.434  72.377  1.00 17.31 ? 650  MET   B N     1 
ATOM   13724 C  CA    . MET   B  1  652  ? 8.070   18.829  73.607  1.00 16.72 ? 650  MET   B CA    1 
ATOM   13725 C  C     . MET   B  1  652  ? 8.876   17.712  74.255  1.00 17.63 ? 650  MET   B C     1 
ATOM   13726 O  O     . MET   B  1  652  ? 10.014  17.985  74.658  1.00 17.97 ? 650  MET   B O     1 
ATOM   13727 C  CB    . MET   B  1  652  ? 7.063   19.434  74.595  1.00 16.66 ? 650  MET   B CB    1 
ATOM   13728 C  CG    . MET   B  1  652  ? 7.709   19.846  75.904  1.00 16.44 ? 650  MET   B CG    1 
ATOM   13729 S  SD    . MET   B  1  652  ? 6.496   20.535  77.033  1.00 20.10 ? 650  MET   B SD    1 
ATOM   13730 C  CE    . MET   B  1  652  ? 6.283   22.138  76.299  1.00 17.45 ? 650  MET   B CE    1 
ATOM   13731 N  N     . PRO   B  1  653  ? 8.392   16.470  74.370  1.00 16.96 ? 651  PRO   B N     1 
ATOM   13732 C  CA    . PRO   B  1  653  ? 9.217   15.443  75.031  1.00 19.36 ? 651  PRO   B CA    1 
ATOM   13733 C  C     . PRO   B  1  653  ? 10.568  15.240  74.367  1.00 19.05 ? 651  PRO   B C     1 
ATOM   13734 O  O     . PRO   B  1  653  ? 11.583  15.130  75.063  1.00 19.75 ? 651  PRO   B O     1 
ATOM   13735 C  CB    . PRO   B  1  653  ? 8.325   14.195  74.981  1.00 19.10 ? 651  PRO   B CB    1 
ATOM   13736 C  CG    . PRO   B  1  653  ? 6.917   14.748  75.001  1.00 19.23 ? 651  PRO   B CG    1 
ATOM   13737 C  CD    . PRO   B  1  653  ? 7.017   15.990  74.123  1.00 17.98 ? 651  PRO   B CD    1 
ATOM   13738 N  N     . THR   B  1  654  ? 10.604  15.215  73.032  1.00 17.89 ? 652  THR   B N     1 
ATOM   13739 C  CA    . THR   B  1  654  ? 11.867  15.071  72.315  1.00 18.08 ? 652  THR   B CA    1 
ATOM   13740 C  C     . THR   B  1  654  ? 12.740  16.309  72.492  1.00 19.95 ? 652  THR   B C     1 
ATOM   13741 O  O     . THR   B  1  654  ? 13.943  16.204  72.758  1.00 18.93 ? 652  THR   B O     1 
ATOM   13742 C  CB    . THR   B  1  654  ? 11.582  14.818  70.834  1.00 19.43 ? 652  THR   B CB    1 
ATOM   13743 O  OG1   . THR   B  1  654  ? 10.826  13.608  70.698  1.00 21.91 ? 652  THR   B OG1   1 
ATOM   13744 C  CG2   . THR   B  1  654  ? 12.888  14.692  70.046  1.00 21.10 ? 652  THR   B CG2   1 
ATOM   13745 N  N     . LEU   B  1  655  ? 12.150  17.496  72.353  1.00 17.72 ? 653  LEU   B N     1 
ATOM   13746 C  CA    . LEU   B  1  655  ? 12.900  18.731  72.556  1.00 17.58 ? 653  LEU   B CA    1 
ATOM   13747 C  C     . LEU   B  1  655  ? 13.510  18.788  73.949  1.00 18.74 ? 653  LEU   B C     1 
ATOM   13748 O  O     . LEU   B  1  655  ? 14.658  19.223  74.113  1.00 17.79 ? 653  LEU   B O     1 
ATOM   13749 C  CB    . LEU   B  1  655  ? 11.993  19.938  72.337  1.00 17.71 ? 653  LEU   B CB    1 
ATOM   13750 C  CG    . LEU   B  1  655  ? 11.375  20.012  70.942  1.00 19.20 ? 653  LEU   B CG    1 
ATOM   13751 C  CD1   . LEU   B  1  655  ? 10.426  21.196  70.837  1.00 19.66 ? 653  LEU   B CD1   1 
ATOM   13752 C  CD2   . LEU   B  1  655  ? 12.480  20.118  69.930  1.00 20.97 ? 653  LEU   B CD2   1 
ATOM   13753 N  N     . LEU   B  1  656  ? 12.763  18.344  74.964  1.00 19.18 ? 654  LEU   B N     1 
ATOM   13754 C  CA    . LEU   B  1  656  ? 13.289  18.314  76.330  1.00 18.97 ? 654  LEU   B CA    1 
ATOM   13755 C  C     . LEU   B  1  656  ? 14.557  17.491  76.402  1.00 18.15 ? 654  LEU   B C     1 
ATOM   13756 O  O     . LEU   B  1  656  ? 15.532  17.883  77.055  1.00 19.99 ? 654  LEU   B O     1 
ATOM   13757 C  CB    . LEU   B  1  656  ? 12.279  17.669  77.282  1.00 22.22 ? 654  LEU   B CB    1 
ATOM   13758 C  CG    . LEU   B  1  656  ? 10.907  18.278  77.442  1.00 23.72 ? 654  LEU   B CG    1 
ATOM   13759 C  CD1   . LEU   B  1  656  ? 10.168  17.623  78.592  1.00 23.66 ? 654  LEU   B CD1   1 
ATOM   13760 C  CD2   . LEU   B  1  656  ? 11.038  19.754  77.642  1.00 22.31 ? 654  LEU   B CD2   1 
ATOM   13761 N  N     . GLY   B  1  657  ? 14.536  16.312  75.792  1.00 19.40 ? 655  GLY   B N     1 
ATOM   13762 C  CA    . GLY   B  1  657  ? 15.699  15.455  75.831  1.00 20.42 ? 655  GLY   B CA    1 
ATOM   13763 C  C     . GLY   B  1  657  ? 16.918  16.136  75.262  1.00 20.59 ? 655  GLY   B C     1 
ATOM   13764 O  O     . GLY   B  1  657  ? 18.013  16.035  75.816  1.00 20.86 ? 655  GLY   B O     1 
ATOM   13765 N  N     . LEU   B  1  658  ? 16.745  16.850  74.151  1.00 18.31 ? 656  LEU   B N     1 
ATOM   13766 C  CA    . LEU   B  1  658  ? 17.878  17.547  73.573  1.00 17.54 ? 656  LEU   B CA    1 
ATOM   13767 C  C     . LEU   B  1  658  ? 18.350  18.672  74.480  1.00 18.05 ? 656  LEU   B C     1 
ATOM   13768 O  O     . LEU   B  1  658  ? 19.551  18.830  74.709  1.00 17.65 ? 656  LEU   B O     1 
ATOM   13769 C  CB    . LEU   B  1  658  ? 17.496  18.076  72.198  1.00 18.27 ? 656  LEU   B CB    1 
ATOM   13770 C  CG    . LEU   B  1  658  ? 18.645  18.734  71.446  1.00 16.99 ? 656  LEU   B CG    1 
ATOM   13771 C  CD1   . LEU   B  1  658  ? 19.838  17.794  71.308  1.00 17.12 ? 656  LEU   B CD1   1 
ATOM   13772 C  CD2   . LEU   B  1  658  ? 18.147  19.174  70.078  1.00 18.16 ? 656  LEU   B CD2   1 
ATOM   13773 N  N     . ILE   B  1  659  ? 17.421  19.448  75.029  1.00 15.61 ? 657  ILE   B N     1 
ATOM   13774 C  CA    . ILE   B  1  659  ? 17.799  20.579  75.864  1.00 15.78 ? 657  ILE   B CA    1 
ATOM   13775 C  C     . ILE   B  1  659  ? 18.480  20.101  77.134  1.00 15.60 ? 657  ILE   B C     1 
ATOM   13776 O  O     . ILE   B  1  659  ? 19.465  20.693  77.598  1.00 16.50 ? 657  ILE   B O     1 
ATOM   13777 C  CB    . ILE   B  1  659  ? 16.546  21.412  76.170  1.00 15.78 ? 657  ILE   B CB    1 
ATOM   13778 C  CG1   . ILE   B  1  659  ? 16.076  22.093  74.897  1.00 15.79 ? 657  ILE   B CG1   1 
ATOM   13779 C  CG2   . ILE   B  1  659  ? 16.827  22.443  77.233  1.00 18.02 ? 657  ILE   B CG2   1 
ATOM   13780 C  CD1   . ILE   B  1  659  ? 14.657  22.596  74.996  1.00 17.10 ? 657  ILE   B CD1   1 
ATOM   13781 N  N     . ILE   B  1  660  ? 17.970  19.016  77.713  1.00 16.15 ? 658  ILE   B N     1 
ATOM   13782 C  CA    . ILE   B  1  660  ? 18.566  18.465  78.922  1.00 16.16 ? 658  ILE   B CA    1 
ATOM   13783 C  C     . ILE   B  1  660  ? 20.029  18.117  78.675  1.00 16.12 ? 658  ILE   B C     1 
ATOM   13784 O  O     . ILE   B  1  660  ? 20.914  18.438  79.485  1.00 18.55 ? 658  ILE   B O     1 
ATOM   13785 C  CB    . ILE   B  1  660  ? 17.760  17.241  79.389  1.00 16.78 ? 658  ILE   B CB    1 
ATOM   13786 C  CG1   . ILE   B  1  660  ? 16.438  17.678  80.023  1.00 18.95 ? 658  ILE   B CG1   1 
ATOM   13787 C  CG2   . ILE   B  1  660  ? 18.577  16.388  80.354  1.00 17.51 ? 658  ILE   B CG2   1 
ATOM   13788 C  CD1   . ILE   B  1  660  ? 15.532  16.510  80.356  1.00 19.46 ? 658  ILE   B CD1   1 
ATOM   13789 N  N     . ARG   B  1  661  ? 20.308  17.464  77.548  1.00 15.47 ? 659  ARG   B N     1 
ATOM   13790 C  CA    . ARG   B  1  661  ? 21.649  16.951  77.303  1.00 16.25 ? 659  ARG   B CA    1 
ATOM   13791 C  C     . ARG   B  1  661  ? 22.581  17.990  76.696  1.00 18.14 ? 659  ARG   B C     1 
ATOM   13792 O  O     . ARG   B  1  661  ? 23.790  17.946  76.947  1.00 18.67 ? 659  ARG   B O     1 
ATOM   13793 C  CB    . ARG   B  1  661  ? 21.580  15.691  76.441  1.00 17.38 ? 659  ARG   B CB    1 
ATOM   13794 C  CG    . ARG   B  1  661  ? 21.101  14.494  77.237  1.00 20.55 ? 659  ARG   B CG    1 
ATOM   13795 C  CD    . ARG   B  1  661  ? 20.893  13.256  76.385  1.00 21.90 ? 659  ARG   B CD    1 
ATOM   13796 N  NE    . ARG   B  1  661  ? 22.114  12.812  75.718  1.00 20.66 ? 659  ARG   B NE    1 
ATOM   13797 C  CZ    . ARG   B  1  661  ? 22.265  12.737  74.404  1.00 22.86 ? 659  ARG   B CZ    1 
ATOM   13798 N  NH1   . ARG   B  1  661  ? 21.295  13.083  73.573  1.00 24.04 ? 659  ARG   B NH1   1 
ATOM   13799 N  NH2   . ARG   B  1  661  ? 23.417  12.290  73.906  1.00 22.41 ? 659  ARG   B NH2   1 
ATOM   13800 N  N     . GLU   B  1  662  ? 22.063  18.923  75.904  1.00 17.28 ? 660  GLU   B N     1 
ATOM   13801 C  CA    . GLU   B  1  662  ? 22.939  19.894  75.260  1.00 17.72 ? 660  GLU   B CA    1 
ATOM   13802 C  C     . GLU   B  1  662  ? 23.243  21.080  76.161  1.00 16.78 ? 660  GLU   B C     1 
ATOM   13803 O  O     . GLU   B  1  662  ? 24.374  21.575  76.168  1.00 17.62 ? 660  GLU   B O     1 
ATOM   13804 C  CB    . GLU   B  1  662  ? 22.310  20.400  73.960  1.00 18.63 ? 660  GLU   B CB    1 
ATOM   13805 C  CG    . GLU   B  1  662  ? 23.198  21.403  73.225  1.00 19.44 ? 660  GLU   B CG    1 
ATOM   13806 C  CD    . GLU   B  1  662  ? 22.609  21.910  71.912  1.00 17.70 ? 660  GLU   B CD    1 
ATOM   13807 O  OE1   . GLU   B  1  662  ? 21.377  22.047  71.803  1.00 18.41 ? 660  GLU   B OE1   1 
ATOM   13808 O  OE2   . GLU   B  1  662  ? 23.406  22.183  71.000  1.00 19.45 ? 660  GLU   B OE2   1 
ATOM   13809 N  N     . ALA   B  1  663  ? 22.267  21.528  76.945  1.00 15.85 ? 661  ALA   B N     1 
ATOM   13810 C  CA    . ALA   B  1  663  ? 22.389  22.774  77.681  1.00 16.98 ? 661  ALA   B CA    1 
ATOM   13811 C  C     . ALA   B  1  663  ? 22.457  22.580  79.187  1.00 16.99 ? 661  ALA   B C     1 
ATOM   13812 O  O     . ALA   B  1  663  ? 22.437  23.573  79.922  1.00 21.59 ? 661  ALA   B O     1 
ATOM   13813 C  CB    . ALA   B  1  663  ? 21.255  23.734  77.312  1.00 17.69 ? 661  ALA   B CB    1 
ATOM   13814 N  N     . GLY   B  1  664  ? 22.520  21.342  79.666  1.00 17.71 ? 662  GLY   B N     1 
ATOM   13815 C  CA    . GLY   B  1  664  ? 22.637  21.119  81.101  1.00 19.96 ? 662  GLY   B CA    1 
ATOM   13816 C  C     . GLY   B  1  664  ? 21.411  21.470  81.915  1.00 22.02 ? 662  GLY   B C     1 
ATOM   13817 O  O     . GLY   B  1  664  ? 21.525  21.760  83.110  1.00 20.54 ? 662  GLY   B O     1 
ATOM   13818 N  N     . LYS   B  1  665  ? 20.239  21.457  81.300  1.00 16.68 ? 663  LYS   B N     1 
ATOM   13819 C  CA    . LYS   B  1  665  ? 19.016  21.819  81.995  1.00 17.33 ? 663  LYS   B CA    1 
ATOM   13820 C  C     . LYS   B  1  665  ? 18.387  20.602  82.642  1.00 16.50 ? 663  LYS   B C     1 
ATOM   13821 O  O     . LYS   B  1  665  ? 18.456  19.486  82.124  1.00 16.98 ? 663  LYS   B O     1 
ATOM   13822 C  CB    . LYS   B  1  665  ? 17.997  22.391  81.013  1.00 16.92 ? 663  LYS   B CB    1 
ATOM   13823 C  CG    . LYS   B  1  665  ? 18.482  23.574  80.221  1.00 22.02 ? 663  LYS   B CG    1 
ATOM   13824 C  CD    . LYS   B  1  665  ? 18.853  24.724  81.117  1.00 23.72 ? 663  LYS   B CD    1 
ATOM   13825 C  CE    . LYS   B  1  665  ? 19.324  25.920  80.288  1.00 23.36 ? 663  LYS   B CE    1 
ATOM   13826 N  NZ    . LYS   B  1  665  ? 19.868  27.005  81.161  1.00 26.01 ? 663  LYS   B NZ    1 
ATOM   13827 N  N     . SER   B  1  666  ? 17.725  20.840  83.765  1.00 18.79 ? 664  SER   B N     1 
ATOM   13828 C  CA    . SER   B  1  666  ? 16.862  19.826  84.335  1.00 18.86 ? 664  SER   B CA    1 
ATOM   13829 C  C     . SER   B  1  666  ? 15.577  19.724  83.518  1.00 18.42 ? 664  SER   B C     1 
ATOM   13830 O  O     . SER   B  1  666  ? 15.252  20.594  82.704  1.00 18.69 ? 664  SER   B O     1 
ATOM   13831 C  CB    . SER   B  1  666  ? 16.467  20.217  85.746  1.00 20.61 ? 664  SER   B CB    1 
ATOM   13832 O  OG    . SER   B  1  666  ? 15.566  21.309  85.684  1.00 23.01 ? 664  SER   B OG    1 
ATOM   13833 N  N     . ALA   B  1  667  ? 14.844  18.634  83.740  1.00 18.53 ? 665  ALA   B N     1 
ATOM   13834 C  CA    . ALA   B  1  667  ? 13.595  18.425  83.013  1.00 16.49 ? 665  ALA   B CA    1 
ATOM   13835 C  C     . ALA   B  1  667  ? 12.620  19.577  83.223  1.00 18.35 ? 665  ALA   B C     1 
ATOM   13836 O  O     . ALA   B  1  667  ? 12.007  20.051  82.259  1.00 17.31 ? 665  ALA   B O     1 
ATOM   13837 C  CB    . ALA   B  1  667  ? 12.959  17.094  83.417  1.00 19.73 ? 665  ALA   B CB    1 
ATOM   13838 N  N     . LEU   B  1  668  ? 12.457  20.044  84.468  1.00 18.10 ? 666  LEU   B N     1 
ATOM   13839 C  CA    . LEU   B  1  668  ? 11.533  21.151  84.702  1.00 21.01 ? 666  LEU   B CA    1 
ATOM   13840 C  C     . LEU   B  1  668  ? 11.964  22.393  83.943  1.00 18.20 ? 666  LEU   B C     1 
ATOM   13841 O  O     . LEU   B  1  668  ? 11.129  23.100  83.365  1.00 18.59 ? 666  LEU   B O     1 
ATOM   13842 C  CB    . LEU   B  1  668  ? 11.403  21.464  86.192  1.00 21.01 ? 666  LEU   B CB    1 
ATOM   13843 C  CG    . LEU   B  1  668  ? 10.430  20.578  86.963  1.00 25.80 ? 666  LEU   B CG    1 
ATOM   13844 C  CD1   . LEU   B  1  668  ? 10.451  20.956  88.438  1.00 32.02 ? 666  LEU   B CD1   1 
ATOM   13845 C  CD2   . LEU   B  1  668  ? 9.019   20.691  86.381  1.00 29.86 ? 666  LEU   B CD2   1 
ATOM   13846 N  N     . ASN   B  1  669  ? 13.261  22.671  83.922  1.00 17.56 ? 667  ASN   B N     1 
ATOM   13847 C  CA    . ASN   B  1  669  ? 13.715  23.871  83.240  1.00 17.84 ? 667  ASN   B CA    1 
ATOM   13848 C  C     . ASN   B  1  669  ? 13.671  23.709  81.734  1.00 16.96 ? 667  ASN   B C     1 
ATOM   13849 O  O     . ASN   B  1  669  ? 13.475  24.700  81.021  1.00 18.71 ? 667  ASN   B O     1 
ATOM   13850 C  CB    . ASN   B  1  669  ? 15.093  24.264  83.760  1.00 22.31 ? 667  ASN   B CB    1 
ATOM   13851 C  CG    . ASN   B  1  669  ? 15.022  24.795  85.169  1.00 27.95 ? 667  ASN   B CG    1 
ATOM   13852 O  OD1   . ASN   B  1  669  ? 14.014  25.395  85.556  1.00 34.12 ? 667  ASN   B OD1   1 
ATOM   13853 N  ND2   . ASN   B  1  669  ? 16.063  24.567  85.951  1.00 31.11 ? 667  ASN   B ND2   1 
ATOM   13854 N  N     . ALA   B  1  670  ? 13.828  22.480  81.238  1.00 16.20 ? 668  ALA   B N     1 
ATOM   13855 C  CA    . ALA   B  1  670  ? 13.659  22.235  79.811  1.00 16.53 ? 668  ALA   B CA    1 
ATOM   13856 C  C     . ALA   B  1  670  ? 12.206  22.404  79.396  1.00 16.01 ? 668  ALA   B C     1 
ATOM   13857 O  O     . ALA   B  1  670  ? 11.923  22.923  78.311  1.00 16.02 ? 668  ALA   B O     1 
ATOM   13858 C  CB    . ALA   B  1  670  ? 14.149  20.833  79.450  1.00 17.15 ? 668  ALA   B CB    1 
ATOM   13859 N  N     . ILE   B  1  671  ? 11.270  21.937  80.229  1.00 16.07 ? 669  ILE   B N     1 
ATOM   13860 C  CA    . ILE   B  1  671  ? 9.853   22.182  79.970  1.00 15.93 ? 669  ILE   B CA    1 
ATOM   13861 C  C     . ILE   B  1  671  ? 9.584   23.679  79.892  1.00 16.32 ? 669  ILE   B C     1 
ATOM   13862 O  O     . ILE   B  1  671  ? 8.913   24.160  78.970  1.00 16.87 ? 669  ILE   B O     1 
ATOM   13863 C  CB    . ILE   B  1  671  ? 8.983   21.513  81.046  1.00 14.94 ? 669  ILE   B CB    1 
ATOM   13864 C  CG1   . ILE   B  1  671  ? 9.002   20.003  80.880  1.00 16.18 ? 669  ILE   B CG1   1 
ATOM   13865 C  CG2   . ILE   B  1  671  ? 7.556   22.020  80.931  1.00 18.55 ? 669  ILE   B CG2   1 
ATOM   13866 C  CD1   . ILE   B  1  671  ? 8.495   19.243  82.108  1.00 19.78 ? 669  ILE   B CD1   1 
ATOM   13867 N  N     . ALA   B  1  672  ? 10.091  24.434  80.865  1.00 16.34 ? 670  ALA   B N     1 
ATOM   13868 C  CA    . ALA   B  1  672  ? 9.874   25.874  80.862  1.00 17.21 ? 670  ALA   B CA    1 
ATOM   13869 C  C     . ALA   B  1  672  ? 10.456  26.502  79.606  1.00 17.18 ? 670  ALA   B C     1 
ATOM   13870 O  O     . ALA   B  1  672  ? 9.864   27.422  79.025  1.00 18.04 ? 670  ALA   B O     1 
ATOM   13871 C  CB    . ALA   B  1  672  ? 10.484  26.495  82.122  1.00 19.46 ? 670  ALA   B CB    1 
ATOM   13872 N  N     . GLU   B  1  673  ? 11.604  25.997  79.161  1.00 16.33 ? 671  GLU   B N     1 
ATOM   13873 C  CA    . GLU   B  1  673  ? 12.246  26.503  77.958  1.00 17.23 ? 671  GLU   B CA    1 
ATOM   13874 C  C     . GLU   B  1  673  ? 11.361  26.309  76.737  1.00 16.50 ? 671  GLU   B C     1 
ATOM   13875 O  O     . GLU   B  1  673  ? 11.159  27.242  75.950  1.00 16.06 ? 671  GLU   B O     1 
ATOM   13876 C  CB    . GLU   B  1  673  ? 13.564  25.758  77.770  1.00 18.38 ? 671  GLU   B CB    1 
ATOM   13877 C  CG    . GLU   B  1  673  ? 14.387  26.235  76.604  1.00 18.35 ? 671  GLU   B CG    1 
ATOM   13878 C  CD    . GLU   B  1  673  ? 15.151  27.502  76.898  1.00 19.13 ? 671  GLU   B CD    1 
ATOM   13879 O  OE1   . GLU   B  1  673  ? 15.315  27.880  78.081  1.00 21.50 ? 671  GLU   B OE1   1 
ATOM   13880 O  OE2   . GLU   B  1  673  ? 15.610  28.125  75.931  1.00 17.16 ? 671  GLU   B OE2   1 
ATOM   13881 N  N     . VAL   B  1  674  ? 10.854  25.091  76.541  1.00 14.45 ? 672  VAL   B N     1 
ATOM   13882 C  CA    . VAL   B  1  674  ? 9.999   24.834  75.388  1.00 15.11 ? 672  VAL   B CA    1 
ATOM   13883 C  C     . VAL   B  1  674  ? 8.696   25.612  75.497  1.00 14.43 ? 672  VAL   B C     1 
ATOM   13884 O  O     . VAL   B  1  674  ? 8.224   26.188  74.512  1.00 15.39 ? 672  VAL   B O     1 
ATOM   13885 C  CB    . VAL   B  1  674  ? 9.763   23.326  75.216  1.00 15.00 ? 672  VAL   B CB    1 
ATOM   13886 C  CG1   . VAL   B  1  674  ? 8.897   23.070  74.002  1.00 15.91 ? 672  VAL   B CG1   1 
ATOM   13887 C  CG2   . VAL   B  1  674  ? 11.092  22.610  75.080  1.00 17.32 ? 672  VAL   B CG2   1 
ATOM   13888 N  N     . ARG   B  1  675  ? 8.114   25.667  76.694  1.00 14.57 ? 673  ARG   B N     1 
ATOM   13889 C  CA    . ARG   B  1  675  ? 6.881   26.432  76.862  1.00 14.53 ? 673  ARG   B CA    1 
ATOM   13890 C  C     . ARG   B  1  675  ? 7.093   27.885  76.490  1.00 13.63 ? 673  ARG   B C     1 
ATOM   13891 O  O     . ARG   B  1  675  ? 6.250   28.488  75.818  1.00 15.02 ? 673  ARG   B O     1 
ATOM   13892 C  CB    . ARG   B  1  675  ? 6.398   26.361  78.305  1.00 15.51 ? 673  ARG   B CB    1 
ATOM   13893 C  CG    . ARG   B  1  675  ? 5.810   25.030  78.708  1.00 16.64 ? 673  ARG   B CG    1 
ATOM   13894 C  CD    . ARG   B  1  675  ? 5.166   25.175  80.072  1.00 16.63 ? 673  ARG   B CD    1 
ATOM   13895 N  NE    . ARG   B  1  675  ? 3.989   26.025  79.966  1.00 15.38 ? 673  ARG   B NE    1 
ATOM   13896 C  CZ    . ARG   B  1  675  ? 3.402   26.613  81.002  1.00 16.25 ? 673  ARG   B CZ    1 
ATOM   13897 N  NH1   . ARG   B  1  675  ? 3.877   26.481  82.227  1.00 16.68 ? 673  ARG   B NH1   1 
ATOM   13898 N  NH2   . ARG   B  1  675  ? 2.311   27.343  80.796  1.00 17.13 ? 673  ARG   B NH2   1 
ATOM   13899 N  N     . GLU   B  1  676  ? 8.224   28.457  76.894  1.00 13.68 ? 674  GLU   B N     1 
ATOM   13900 C  CA    A GLU   B  1  676  ? 8.492   29.854  76.579  0.46 14.82 ? 674  GLU   B CA    1 
ATOM   13901 C  CA    B GLU   B  1  676  ? 8.473   29.854  76.578  0.54 14.81 ? 674  GLU   B CA    1 
ATOM   13902 C  C     . GLU   B  1  676  ? 8.598   30.066  75.076  1.00 14.10 ? 674  GLU   B C     1 
ATOM   13903 O  O     . GLU   B  1  676  ? 8.113   31.068  74.548  1.00 13.89 ? 674  GLU   B O     1 
ATOM   13904 C  CB    A GLU   B  1  676  ? 9.780   30.297  77.269  0.46 15.34 ? 674  GLU   B CB    1 
ATOM   13905 C  CB    B GLU   B  1  676  ? 9.717   30.348  77.310  0.54 15.33 ? 674  GLU   B CB    1 
ATOM   13906 C  CG    A GLU   B  1  676  ? 10.103  31.770  77.103  0.46 17.19 ? 674  GLU   B CG    1 
ATOM   13907 C  CG    B GLU   B  1  676  ? 9.857   31.853  77.275  0.54 16.48 ? 674  GLU   B CG    1 
ATOM   13908 C  CD    A GLU   B  1  676  ? 9.503   32.637  78.189  0.46 19.30 ? 674  GLU   B CD    1 
ATOM   13909 C  CD    B GLU   B  1  676  ? 10.932  32.368  78.203  0.54 21.28 ? 674  GLU   B CD    1 
ATOM   13910 O  OE1   A GLU   B  1  676  ? 8.611   32.152  78.913  0.46 22.39 ? 674  GLU   B OE1   1 
ATOM   13911 O  OE1   B GLU   B  1  676  ? 10.976  31.922  79.370  0.54 23.17 ? 674  GLU   B OE1   1 
ATOM   13912 O  OE2   A GLU   B  1  676  ? 9.930   33.803  78.318  0.46 19.73 ? 674  GLU   B OE2   1 
ATOM   13913 O  OE2   B GLU   B  1  676  ? 11.731  33.220  77.763  0.54 24.99 ? 674  GLU   B OE2   1 
ATOM   13914 N  N     . ALA   B  1  677  ? 9.248   29.137  74.368  1.00 14.42 ? 675  ALA   B N     1 
ATOM   13915 C  CA    . ALA   B  1  677  ? 9.315   29.259  72.915  1.00 13.84 ? 675  ALA   B CA    1 
ATOM   13916 C  C     . ALA   B  1  677  ? 7.923   29.226  72.304  1.00 14.22 ? 675  ALA   B C     1 
ATOM   13917 O  O     . ALA   B  1  677  ? 7.600   30.039  71.433  1.00 14.35 ? 675  ALA   B O     1 
ATOM   13918 C  CB    . ALA   B  1  677  ? 10.178  28.137  72.341  1.00 14.87 ? 675  ALA   B CB    1 
ATOM   13919 N  N     . ILE   B  1  678  ? 7.081   28.302  72.773  1.00 12.75 ? 676  ILE   B N     1 
ATOM   13920 C  CA    . ILE   B  1  678  ? 5.705   28.209  72.296  1.00 12.41 ? 676  ILE   B CA    1 
ATOM   13921 C  C     . ILE   B  1  678  ? 4.979   29.516  72.553  1.00 12.90 ? 676  ILE   B C     1 
ATOM   13922 O  O     . ILE   B  1  678  ? 4.270   30.034  71.680  1.00 13.98 ? 676  ILE   B O     1 
ATOM   13923 C  CB    . ILE   B  1  678  ? 5.001   27.024  72.975  1.00 13.34 ? 676  ILE   B CB    1 
ATOM   13924 C  CG1   . ILE   B  1  678  ? 5.586   25.710  72.465  1.00 14.84 ? 676  ILE   B CG1   1 
ATOM   13925 C  CG2   . ILE   B  1  678  ? 3.478   27.086  72.747  1.00 13.58 ? 676  ILE   B CG2   1 
ATOM   13926 C  CD1   . ILE   B  1  678  ? 5.355   24.547  73.436  1.00 14.86 ? 676  ILE   B CD1   1 
ATOM   13927 N  N     . ASP   B  1  679  ? 5.143   30.064  73.758  1.00 13.57 ? 677  ASP   B N     1 
ATOM   13928 C  CA    . ASP   B  1  679  ? 4.464   31.299  74.123  1.00 14.14 ? 677  ASP   B CA    1 
ATOM   13929 C  C     . ASP   B  1  679  ? 4.948   32.473  73.289  1.00 14.33 ? 677  ASP   B C     1 
ATOM   13930 O  O     . ASP   B  1  679  ? 4.136   33.296  72.867  1.00 14.22 ? 677  ASP   B O     1 
ATOM   13931 C  CB    . ASP   B  1  679  ? 4.638   31.574  75.612  1.00 14.04 ? 677  ASP   B CB    1 
ATOM   13932 C  CG    . ASP   B  1  679  ? 3.874   30.594  76.483  1.00 15.41 ? 677  ASP   B CG    1 
ATOM   13933 O  OD1   . ASP   B  1  679  ? 2.797   30.125  76.048  1.00 16.99 ? 677  ASP   B OD1   1 
ATOM   13934 O  OD2   . ASP   B  1  679  ? 4.346   30.326  77.613  1.00 18.33 ? 677  ASP   B OD2   1 
ATOM   13935 N  N     . PHE   B  1  680  ? 6.255   32.565  73.020  1.00 13.11 ? 678  PHE   B N     1 
ATOM   13936 C  CA    . PHE   B  1  680  ? 6.720   33.620  72.119  1.00 13.42 ? 678  PHE   B CA    1 
ATOM   13937 C  C     . PHE   B  1  680  ? 6.045   33.502  70.765  1.00 13.91 ? 678  PHE   B C     1 
ATOM   13938 O  O     . PHE   B  1  680  ? 5.585   34.497  70.194  1.00 13.31 ? 678  PHE   B O     1 
ATOM   13939 C  CB    . PHE   B  1  680  ? 8.227   33.528  71.913  1.00 13.47 ? 678  PHE   B CB    1 
ATOM   13940 C  CG    . PHE   B  1  680  ? 9.042   34.188  72.977  1.00 13.38 ? 678  PHE   B CG    1 
ATOM   13941 C  CD1   . PHE   B  1  680  ? 8.806   35.502  73.365  1.00 14.30 ? 678  PHE   B CD1   1 
ATOM   13942 C  CD2   . PHE   B  1  680  ? 10.091  33.492  73.558  1.00 14.46 ? 678  PHE   B CD2   1 
ATOM   13943 C  CE1   . PHE   B  1  680  ? 9.610   36.096  74.343  1.00 15.13 ? 678  PHE   B CE1   1 
ATOM   13944 C  CE2   . PHE   B  1  680  ? 10.875  34.070  74.540  1.00 15.79 ? 678  PHE   B CE2   1 
ATOM   13945 C  CZ    . PHE   B  1  680  ? 10.638  35.370  74.927  1.00 15.50 ? 678  PHE   B CZ    1 
ATOM   13946 N  N     . LEU   B  1  681  ? 6.004   32.289  70.221  1.00 12.74 ? 679  LEU   B N     1 
ATOM   13947 C  CA    . LEU   B  1  681  ? 5.414   32.095  68.907  1.00 13.09 ? 679  LEU   B CA    1 
ATOM   13948 C  C     . LEU   B  1  681  ? 3.980   32.575  68.906  1.00 13.18 ? 679  LEU   B C     1 
ATOM   13949 O  O     . LEU   B  1  681  ? 3.573   33.352  68.034  1.00 13.73 ? 679  LEU   B O     1 
ATOM   13950 C  CB    . LEU   B  1  681  ? 5.506   30.619  68.518  1.00 13.55 ? 679  LEU   B CB    1 
ATOM   13951 C  CG    . LEU   B  1  681  ? 6.934   30.177  68.201  1.00 12.69 ? 679  LEU   B CG    1 
ATOM   13952 C  CD1   . LEU   B  1  681  ? 7.024   28.673  68.264  1.00 13.39 ? 679  LEU   B CD1   1 
ATOM   13953 C  CD2   . LEU   B  1  681  ? 7.324   30.688  66.836  1.00 14.87 ? 679  LEU   B CD2   1 
ATOM   13954 N  N     . ARG   B  1  682  ? 3.200   32.136  69.891  1.00 13.01 ? 680  ARG   B N     1 
ATOM   13955 C  CA    . ARG   B  1  682  ? 1.784   32.461  69.887  1.00 12.17 ? 680  ARG   B CA    1 
ATOM   13956 C  C     . ARG   B  1  682  ? 1.552   33.914  70.250  1.00 12.79 ? 680  ARG   B C     1 
ATOM   13957 O  O     . ARG   B  1  682  ? 0.586   34.518  69.769  1.00 14.49 ? 680  ARG   B O     1 
ATOM   13958 C  CB    . ARG   B  1  682  ? 1.042   31.546  70.850  1.00 13.18 ? 680  ARG   B CB    1 
ATOM   13959 C  CG    . ARG   B  1  682  ? 1.013   30.114  70.362  1.00 13.68 ? 680  ARG   B CG    1 
ATOM   13960 C  CD    . ARG   B  1  682  ? 0.356   29.245  71.404  1.00 15.53 ? 680  ARG   B CD    1 
ATOM   13961 N  NE    . ARG   B  1  682  ? 0.147   27.909  70.873  1.00 15.80 ? 680  ARG   B NE    1 
ATOM   13962 C  CZ    . ARG   B  1  682  ? -0.074  26.838  71.614  1.00 16.02 ? 680  ARG   B CZ    1 
ATOM   13963 N  NH1   . ARG   B  1  682  ? -0.116  26.907  72.932  1.00 17.24 ? 680  ARG   B NH1   1 
ATOM   13964 N  NH2   . ARG   B  1  682  ? -0.214  25.662  71.015  1.00 19.75 ? 680  ARG   B NH2   1 
ATOM   13965 N  N     . TYR   B  1  683  ? 2.393   34.471  71.113  1.00 12.82 ? 681  TYR   B N     1 
ATOM   13966 C  CA    . TYR   B  1  683  ? 2.223   35.863  71.498  1.00 13.34 ? 681  TYR   B CA    1 
ATOM   13967 C  C     . TYR   B  1  683  ? 2.537   36.788  70.334  1.00 13.27 ? 681  TYR   B C     1 
ATOM   13968 O  O     . TYR   B  1  683  ? 1.751   37.691  70.021  1.00 14.14 ? 681  TYR   B O     1 
ATOM   13969 C  CB    . TYR   B  1  683  ? 3.113   36.167  72.697  1.00 13.64 ? 681  TYR   B CB    1 
ATOM   13970 C  CG    . TYR   B  1  683  ? 3.060   37.606  73.117  1.00 13.06 ? 681  TYR   B CG    1 
ATOM   13971 C  CD1   . TYR   B  1  683  ? 1.993   38.087  73.871  1.00 14.99 ? 681  TYR   B CD1   1 
ATOM   13972 C  CD2   . TYR   B  1  683  ? 4.068   38.475  72.759  1.00 14.76 ? 681  TYR   B CD2   1 
ATOM   13973 C  CE1   . TYR   B  1  683  ? 1.936   39.416  74.238  1.00 15.81 ? 681  TYR   B CE1   1 
ATOM   13974 C  CE2   . TYR   B  1  683  ? 4.029   39.803  73.127  1.00 14.12 ? 681  TYR   B CE2   1 
ATOM   13975 C  CZ    . TYR   B  1  683  ? 2.964   40.260  73.869  1.00 13.56 ? 681  TYR   B CZ    1 
ATOM   13976 O  OH    . TYR   B  1  683  ? 2.929   41.590  74.213  1.00 16.20 ? 681  TYR   B OH    1 
ATOM   13977 N  N     . TYR   B  1  684  ? 3.685   36.588  69.679  1.00 12.52 ? 682  TYR   B N     1 
ATOM   13978 C  CA    . TYR   B  1  684  ? 3.988   37.449  68.541  1.00 12.98 ? 682  TYR   B CA    1 
ATOM   13979 C  C     . TYR   B  1  684  ? 2.990   37.257  67.406  1.00 13.95 ? 682  TYR   B C     1 
ATOM   13980 O  O     . TYR   B  1  684  ? 2.693   38.211  66.687  1.00 14.87 ? 682  TYR   B O     1 
ATOM   13981 C  CB    . TYR   B  1  684  ? 5.437   37.265  68.092  1.00 13.50 ? 682  TYR   B CB    1 
ATOM   13982 C  CG    . TYR   B  1  684  ? 6.429   37.657  69.151  1.00 12.85 ? 682  TYR   B CG    1 
ATOM   13983 C  CD1   . TYR   B  1  684  ? 6.251   38.802  69.916  1.00 13.79 ? 682  TYR   B CD1   1 
ATOM   13984 C  CD2   . TYR   B  1  684  ? 7.550   36.881  69.384  1.00 13.44 ? 682  TYR   B CD2   1 
ATOM   13985 C  CE1   . TYR   B  1  684  ? 7.157   39.153  70.905  1.00 14.01 ? 682  TYR   B CE1   1 
ATOM   13986 C  CE2   . TYR   B  1  684  ? 8.469   37.220  70.352  1.00 13.22 ? 682  TYR   B CE2   1 
ATOM   13987 C  CZ    . TYR   B  1  684  ? 8.276   38.360  71.108  1.00 13.77 ? 682  TYR   B CZ    1 
ATOM   13988 O  OH    . TYR   B  1  684  ? 9.178   38.682  72.086  1.00 14.71 ? 682  TYR   B OH    1 
ATOM   13989 N  N     . ALA   B  1  685  ? 2.452   36.046  67.245  1.00 13.05 ? 683  ALA   B N     1 
ATOM   13990 C  CA    . ALA   B  1  685  ? 1.401   35.828  66.260  1.00 13.42 ? 683  ALA   B CA    1 
ATOM   13991 C  C     . ALA   B  1  685  ? 0.188   36.671  66.599  1.00 15.38 ? 683  ALA   B C     1 
ATOM   13992 O  O     . ALA   B  1  685  ? -0.334  37.406  65.748  1.00 14.55 ? 683  ALA   B O     1 
ATOM   13993 C  CB    . ALA   B  1  685  ? 1.053   34.343  66.206  1.00 14.00 ? 683  ALA   B CB    1 
ATOM   13994 N  N     . GLU   B  1  686  ? -0.250  36.616  67.855  1.00 14.59 ? 684  GLU   B N     1 
ATOM   13995 C  CA    . GLU   B  1  686  ? -1.425  37.393  68.216  1.00 15.06 ? 684  GLU   B CA    1 
ATOM   13996 C  C     . GLU   B  1  686  ? -1.144  38.886  68.140  1.00 15.77 ? 684  GLU   B C     1 
ATOM   13997 O  O     . GLU   B  1  686  ? -1.964  39.643  67.623  1.00 15.83 ? 684  GLU   B O     1 
ATOM   13998 C  CB    . GLU   B  1  686  ? -1.900  37.016  69.607  1.00 16.33 ? 684  GLU   B CB    1 
ATOM   13999 C  CG    . GLU   B  1  686  ? -3.042  37.912  70.111  1.00 18.77 ? 684  GLU   B CG    1 
ATOM   14000 C  CD    . GLU   B  1  686  ? -4.326  37.837  69.285  1.00 22.45 ? 684  GLU   B CD    1 
ATOM   14001 O  OE1   . GLU   B  1  686  ? -4.479  36.970  68.390  1.00 21.69 ? 684  GLU   B OE1   1 
ATOM   14002 O  OE2   . GLU   B  1  686  ? -5.219  38.666  69.566  1.00 24.56 ? 684  GLU   B OE2   1 
ATOM   14003 N  N     . GLN   B  1  687  ? 0.019   39.332  68.624  1.00 14.03 ? 685  GLN   B N     1 
ATOM   14004 C  CA    . GLN   B  1  687  ? 0.314   40.759  68.533  1.00 14.55 ? 685  GLN   B CA    1 
ATOM   14005 C  C     . GLN   B  1  687  ? 0.319   41.216  67.080  1.00 15.01 ? 685  GLN   B C     1 
ATOM   14006 O  O     . GLN   B  1  687  ? -0.138  42.323  66.763  1.00 16.13 ? 685  GLN   B O     1 
ATOM   14007 C  CB    . GLN   B  1  687  ? 1.647   41.074  69.199  1.00 15.20 ? 685  GLN   B CB    1 
ATOM   14008 C  CG    . GLN   B  1  687  ? 1.596   40.860  70.693  1.00 17.20 ? 685  GLN   B CG    1 
ATOM   14009 C  CD    . GLN   B  1  687  ? 0.571   41.750  71.350  1.00 18.68 ? 685  GLN   B CD    1 
ATOM   14010 O  OE1   . GLN   B  1  687  ? 0.609   42.971  71.202  1.00 18.24 ? 685  GLN   B OE1   1 
ATOM   14011 N  NE2   . GLN   B  1  687  ? -0.356  41.144  72.082  1.00 20.95 ? 685  GLN   B NE2   1 
ATOM   14012 N  N     . THR   B  1  688  ? 0.818   40.366  66.181  1.00 14.48 ? 686  THR   B N     1 
ATOM   14013 C  CA    . THR   B  1  688  ? 0.759   40.682  64.759  1.00 14.61 ? 686  THR   B CA    1 
ATOM   14014 C  C     . THR   B  1  688  ? -0.677  40.841  64.295  1.00 14.76 ? 686  THR   B C     1 
ATOM   14015 O  O     . THR   B  1  688  ? -1.007  41.800  63.595  1.00 16.50 ? 686  THR   B O     1 
ATOM   14016 C  CB    . THR   B  1  688  ? 1.432   39.573  63.969  1.00 13.35 ? 686  THR   B CB    1 
ATOM   14017 O  OG1   . THR   B  1  688  ? 2.819   39.605  64.277  1.00 15.36 ? 686  THR   B OG1   1 
ATOM   14018 C  CG2   . THR   B  1  688  ? 1.246   39.805  62.477  1.00 15.32 ? 686  THR   B CG2   1 
ATOM   14019 N  N     . ARG   B  1  689  ? -1.535  39.888  64.650  1.00 13.87 ? 687  ARG   B N     1 
ATOM   14020 C  CA    . ARG   B  1  689  ? -2.933  39.966  64.243  1.00 15.74 ? 687  ARG   B CA    1 
ATOM   14021 C  C     . ARG   B  1  689  ? -3.609  41.212  64.787  1.00 15.33 ? 687  ARG   B C     1 
ATOM   14022 O  O     . ARG   B  1  689  ? -4.556  41.716  64.175  1.00 17.63 ? 687  ARG   B O     1 
ATOM   14023 C  CB    . ARG   B  1  689  ? -3.673  38.712  64.684  1.00 15.79 ? 687  ARG   B CB    1 
ATOM   14024 C  CG    . ARG   B  1  689  ? -3.304  37.496  63.846  1.00 17.30 ? 687  ARG   B CG    1 
ATOM   14025 C  CD    . ARG   B  1  689  ? -4.172  36.320  64.217  1.00 18.66 ? 687  ARG   B CD    1 
ATOM   14026 N  NE    . ARG   B  1  689  ? -4.020  35.917  65.608  1.00 19.48 ? 687  ARG   B NE    1 
ATOM   14027 C  CZ    . ARG   B  1  689  ? -3.266  34.906  66.021  1.00 19.65 ? 687  ARG   B CZ    1 
ATOM   14028 N  NH1   . ARG   B  1  689  ? -2.585  34.163  65.167  1.00 18.86 ? 687  ARG   B NH1   1 
ATOM   14029 N  NH2   . ARG   B  1  689  ? -3.212  34.621  67.319  1.00 18.57 ? 687  ARG   B NH2   1 
ATOM   14030 N  N     . ARG   B  1  690  ? -3.152  41.715  65.928  1.00 15.70 ? 688  ARG   B N     1 
ATOM   14031 C  CA    . ARG   B  1  690  ? -3.711  42.926  66.501  1.00 15.34 ? 688  ARG   B CA    1 
ATOM   14032 C  C     . ARG   B  1  690  ? -3.199  44.204  65.855  1.00 15.94 ? 688  ARG   B C     1 
ATOM   14033 O  O     . ARG   B  1  690  ? -3.832  45.248  66.033  1.00 17.12 ? 688  ARG   B O     1 
ATOM   14034 C  CB    . ARG   B  1  690  ? -3.387  42.982  67.994  1.00 16.74 ? 688  ARG   B CB    1 
ATOM   14035 C  CG    . ARG   B  1  690  ? -4.030  41.860  68.795  1.00 18.28 ? 688  ARG   B CG    1 
ATOM   14036 C  CD    . ARG   B  1  690  ? -5.537  42.078  69.000  1.00 21.77 ? 688  ARG   B CD    1 
ATOM   14037 N  NE    . ARG   B  1  690  ? -5.799  43.325  69.714  1.00 26.18 ? 688  ARG   B NE    1 
ATOM   14038 C  CZ    . ARG   B  1  690  ? -6.394  44.382  69.184  1.00 24.72 ? 688  ARG   B CZ    1 
ATOM   14039 N  NH1   . ARG   B  1  690  ? -6.889  44.351  67.958  1.00 23.96 ? 688  ARG   B NH1   1 
ATOM   14040 N  NH2   . ARG   B  1  690  ? -6.523  45.490  69.912  1.00 20.41 ? 688  ARG   B NH2   1 
ATOM   14041 N  N     . THR   B  1  691  ? -2.051  44.172  65.155  1.00 16.36 ? 689  THR   B N     1 
ATOM   14042 C  CA    . THR   B  1  691  ? -1.415  45.446  64.816  1.00 16.74 ? 689  THR   B CA    1 
ATOM   14043 C  C     . THR   B  1  691  ? -1.001  45.614  63.363  1.00 16.79 ? 689  THR   B C     1 
ATOM   14044 O  O     . THR   B  1  691  ? -1.147  46.709  62.829  1.00 20.14 ? 689  THR   B O     1 
ATOM   14045 C  CB    . THR   B  1  691  ? -0.168  45.681  65.683  1.00 16.72 ? 689  THR   B CB    1 
ATOM   14046 O  OG1   . THR   B  1  691  ? 0.746   44.581  65.532  1.00 17.44 ? 689  THR   B OG1   1 
ATOM   14047 C  CG2   . THR   B  1  691  ? -0.533  45.860  67.132  1.00 16.84 ? 689  THR   B CG2   1 
ATOM   14048 N  N     . LEU   B  1  692  ? -0.425  44.600  62.730  1.00 16.51 ? 690  LEU   B N     1 
ATOM   14049 C  CA    . LEU   B  1  692  ? 0.345   44.875  61.522  1.00 17.75 ? 690  LEU   B CA    1 
ATOM   14050 C  C     . LEU   B  1  692  ? -0.541  45.038  60.293  1.00 18.44 ? 690  LEU   B C     1 
ATOM   14051 O  O     . LEU   B  1  692  ? -1.379  44.188  59.992  1.00 20.13 ? 690  LEU   B O     1 
ATOM   14052 C  CB    . LEU   B  1  692  ? 1.418   43.817  61.278  1.00 16.89 ? 690  LEU   B CB    1 
ATOM   14053 C  CG    . LEU   B  1  692  ? 2.495   43.776  62.360  1.00 18.73 ? 690  LEU   B CG    1 
ATOM   14054 C  CD1   . LEU   B  1  692  ? 3.634   42.900  61.861  1.00 20.36 ? 690  LEU   B CD1   1 
ATOM   14055 C  CD2   . LEU   B  1  692  ? 2.998   45.171  62.721  1.00 20.60 ? 690  LEU   B CD2   1 
ATOM   14056 N  N     . GLY   B  1  693  ? -0.320  46.133  59.580  1.00 17.65 ? 691  GLY   B N     1 
ATOM   14057 C  CA    . GLY   B  1  693  ? -1.028  46.424  58.366  1.00 19.37 ? 691  GLY   B CA    1 
ATOM   14058 C  C     . GLY   B  1  693  ? -0.055  46.817  57.283  1.00 19.95 ? 691  GLY   B C     1 
ATOM   14059 O  O     . GLY   B  1  693  ? 1.168   46.757  57.457  1.00 20.52 ? 691  GLY   B O     1 
ATOM   14060 N  N     . PRO   B  1  694  ? -0.588  47.247  56.143  1.00 21.42 ? 692  PRO   B N     1 
ATOM   14061 C  CA    . PRO   B  1  694  ? 0.278   47.470  54.974  1.00 22.93 ? 692  PRO   B CA    1 
ATOM   14062 C  C     . PRO   B  1  694  ? 1.326   48.546  55.179  1.00 22.97 ? 692  PRO   B C     1 
ATOM   14063 O  O     . PRO   B  1  694  ? 2.406   48.463  54.577  1.00 26.66 ? 692  PRO   B O     1 
ATOM   14064 C  CB    . PRO   B  1  694  ? -0.713  47.816  53.851  1.00 26.38 ? 692  PRO   B CB    1 
ATOM   14065 C  CG    . PRO   B  1  694  ? -2.007  48.114  54.527  1.00 30.11 ? 692  PRO   B CG    1 
ATOM   14066 C  CD    . PRO   B  1  694  ? -2.020  47.372  55.829  1.00 24.39 ? 692  PRO   B CD    1 
ATOM   14067 N  N     . GLY   B  1  695  ? 1.058   49.543  56.016  1.00 23.29 ? 693  GLY   B N     1 
ATOM   14068 C  CA    . GLY   B  1  695  ? 1.993   50.615  56.265  1.00 22.80 ? 693  GLY   B CA    1 
ATOM   14069 C  C     . GLY   B  1  695  ? 3.089   50.300  57.254  1.00 22.25 ? 693  GLY   B C     1 
ATOM   14070 O  O     . GLY   B  1  695  ? 3.925   51.162  57.533  1.00 27.59 ? 693  GLY   B O     1 
ATOM   14071 N  N     . HIS   B  1  696  ? 3.101   49.095  57.821  1.00 20.57 ? 694  HIS   B N     1 
ATOM   14072 C  CA    . HIS   B  1  696  ? 4.158   48.693  58.742  1.00 19.97 ? 694  HIS   B CA    1 
ATOM   14073 C  C     . HIS   B  1  696  ? 5.124   47.777  57.997  1.00 19.49 ? 694  HIS   B C     1 
ATOM   14074 O  O     . HIS   B  1  696  ? 5.115   46.554  58.131  1.00 24.68 ? 694  HIS   B O     1 
ATOM   14075 C  CB    . HIS   B  1  696  ? 3.557   48.029  59.972  1.00 20.17 ? 694  HIS   B CB    1 
ATOM   14076 C  CG    . HIS   B  1  696  ? 2.441   48.811  60.584  1.00 18.87 ? 694  HIS   B CG    1 
ATOM   14077 N  ND1   . HIS   B  1  696  ? 1.151   48.333  60.648  1.00 19.70 ? 694  HIS   B ND1   1 
ATOM   14078 C  CD2   . HIS   B  1  696  ? 2.411   50.050  61.129  1.00 19.54 ? 694  HIS   B CD2   1 
ATOM   14079 C  CE1   . HIS   B  1  696  ? 0.381   49.233  61.229  1.00 21.05 ? 694  HIS   B CE1   1 
ATOM   14080 N  NE2   . HIS   B  1  696  ? 1.116   50.290  61.516  1.00 21.11 ? 694  HIS   B NE2   1 
ATOM   14081 N  N     . GLY   B  1  697  ? 5.942   48.407  57.170  1.00 22.17 ? 695  GLY   B N     1 
ATOM   14082 C  CA    . GLY   B  1  697  ? 6.867   47.685  56.331  1.00 20.47 ? 695  GLY   B CA    1 
ATOM   14083 C  C     . GLY   B  1  697  ? 8.005   47.085  57.124  1.00 20.24 ? 695  GLY   B C     1 
ATOM   14084 O  O     . GLY   B  1  697  ? 8.437   47.627  58.138  1.00 19.85 ? 695  GLY   B O     1 
ATOM   14085 N  N     . PRO   B  1  698  ? 8.529   45.960  56.662  1.00 20.80 ? 696  PRO   B N     1 
ATOM   14086 C  CA    . PRO   B  1  698  ? 9.649   45.334  57.367  1.00 19.64 ? 696  PRO   B CA    1 
ATOM   14087 C  C     . PRO   B  1  698  ? 10.925  46.131  57.178  1.00 18.79 ? 696  PRO   B C     1 
ATOM   14088 O  O     . PRO   B  1  698  ? 11.056  46.952  56.271  1.00 19.38 ? 696  PRO   B O     1 
ATOM   14089 C  CB    . PRO   B  1  698  ? 9.773   43.967  56.692  1.00 23.29 ? 696  PRO   B CB    1 
ATOM   14090 C  CG    . PRO   B  1  698  ? 9.276   44.214  55.316  1.00 28.35 ? 696  PRO   B CG    1 
ATOM   14091 C  CD    . PRO   B  1  698  ? 8.120   45.184  55.482  1.00 23.68 ? 696  PRO   B CD    1 
ATOM   14092 N  N     . LEU   B  1  699  ? 11.869  45.880  58.082  1.00 18.17 ? 697  LEU   B N     1 
ATOM   14093 C  CA    . LEU   B  1  699  ? 13.194  46.473  57.941  1.00 16.04 ? 697  LEU   B CA    1 
ATOM   14094 C  C     . LEU   B  1  699  ? 13.961  45.841  56.790  1.00 16.44 ? 697  LEU   B C     1 
ATOM   14095 O  O     . LEU   B  1  699  ? 14.671  46.533  56.054  1.00 19.81 ? 697  LEU   B O     1 
ATOM   14096 C  CB    . LEU   B  1  699  ? 13.972  46.262  59.232  1.00 16.45 ? 697  LEU   B CB    1 
ATOM   14097 C  CG    . LEU   B  1  699  ? 13.375  46.889  60.486  1.00 18.58 ? 697  LEU   B CG    1 
ATOM   14098 C  CD1   . LEU   B  1  699  ? 14.207  46.484  61.680  1.00 17.96 ? 697  LEU   B CD1   1 
ATOM   14099 C  CD2   . LEU   B  1  699  ? 13.329  48.403  60.336  1.00 23.94 ? 697  LEU   B CD2   1 
ATOM   14100 N  N     . GLY   B  1  700  ? 13.849  44.526  56.637  1.00 15.60 ? 698  GLY   B N     1 
ATOM   14101 C  CA    . GLY   B  1  700  ? 14.719  43.774  55.766  1.00 16.54 ? 698  GLY   B CA    1 
ATOM   14102 C  C     . GLY   B  1  700  ? 15.377  42.669  56.561  1.00 16.41 ? 698  GLY   B C     1 
ATOM   14103 O  O     . GLY   B  1  700  ? 14.921  42.307  57.645  1.00 16.58 ? 698  GLY   B O     1 
ATOM   14104 N  N     . PRO   B  1  701  ? 16.471  42.122  56.046  1.00 15.93 ? 699  PRO   B N     1 
ATOM   14105 C  CA    . PRO   B  1  701  ? 17.129  40.997  56.720  1.00 15.20 ? 699  PRO   B CA    1 
ATOM   14106 C  C     . PRO   B  1  701  ? 17.515  41.376  58.139  1.00 15.51 ? 699  PRO   B C     1 
ATOM   14107 O  O     . PRO   B  1  701  ? 18.152  42.403  58.377  1.00 16.16 ? 699  PRO   B O     1 
ATOM   14108 C  CB    . PRO   B  1  701  ? 18.371  40.751  55.856  1.00 16.48 ? 699  PRO   B CB    1 
ATOM   14109 C  CG    . PRO   B  1  701  ? 17.937  41.244  54.505  1.00 18.18 ? 699  PRO   B CG    1 
ATOM   14110 C  CD    . PRO   B  1  701  ? 17.165  42.486  54.804  1.00 18.51 ? 699  PRO   B CD    1 
ATOM   14111 N  N     . ILE   B  1  702  ? 17.088  40.559  59.092  1.00 15.44 ? 700  ILE   B N     1 
ATOM   14112 C  CA    A ILE   B  1  702  ? 17.405  40.780  60.494  0.64 15.05 ? 700  ILE   B CA    1 
ATOM   14113 C  CA    B ILE   B  1  702  ? 17.385  40.771  60.504  0.36 15.04 ? 700  ILE   B CA    1 
ATOM   14114 C  C     . ILE   B  1  702  ? 18.327  39.672  60.961  1.00 15.43 ? 700  ILE   B C     1 
ATOM   14115 O  O     . ILE   B  1  702  ? 18.060  38.486  60.738  1.00 15.29 ? 700  ILE   B O     1 
ATOM   14116 C  CB    A ILE   B  1  702  ? 16.143  40.877  61.362  0.64 14.54 ? 700  ILE   B CB    1 
ATOM   14117 C  CB    B ILE   B  1  702  ? 16.108  40.768  61.359  0.36 14.54 ? 700  ILE   B CB    1 
ATOM   14118 C  CG1   A ILE   B  1  702  ? 15.499  42.242  61.135  0.64 14.83 ? 700  ILE   B CG1   1 
ATOM   14119 C  CG1   B ILE   B  1  702  ? 15.149  41.848  60.872  0.36 15.01 ? 700  ILE   B CG1   1 
ATOM   14120 C  CG2   A ILE   B  1  702  ? 16.507  40.665  62.828  0.64 15.64 ? 700  ILE   B CG2   1 
ATOM   14121 C  CG2   B ILE   B  1  702  ? 16.459  40.986  62.821  0.36 15.67 ? 700  ILE   B CG2   1 
ATOM   14122 C  CD1   A ILE   B  1  702  ? 14.190  42.437  61.867  0.64 14.90 ? 700  ILE   B CD1   1 
ATOM   14123 C  CD1   B ILE   B  1  702  ? 15.700  43.238  60.970  0.36 16.19 ? 700  ILE   B CD1   1 
ATOM   14124 N  N     . VAL   B  1  703  ? 19.417  40.063  61.598  1.00 14.75 ? 701  VAL   B N     1 
ATOM   14125 C  CA    . VAL   B  1  703  ? 20.339  39.118  62.199  1.00 14.43 ? 701  VAL   B CA    1 
ATOM   14126 C  C     . VAL   B  1  703  ? 19.929  38.921  63.648  1.00 13.52 ? 701  VAL   B C     1 
ATOM   14127 O  O     . VAL   B  1  703  ? 19.836  39.890  64.408  1.00 14.72 ? 701  VAL   B O     1 
ATOM   14128 C  CB    . VAL   B  1  703  ? 21.768  39.650  62.089  1.00 14.18 ? 701  VAL   B CB    1 
ATOM   14129 C  CG1   . VAL   B  1  703  ? 22.712  38.780  62.899  1.00 15.60 ? 701  VAL   B CG1   1 
ATOM   14130 C  CG2   . VAL   B  1  703  ? 22.169  39.689  60.626  1.00 15.86 ? 701  VAL   B CG2   1 
ATOM   14131 N  N     . CYS   B  1  704  ? 19.657  37.676  64.020  1.00 13.20 ? 702  CYS   B N     1 
ATOM   14132 C  CA    . CYS   B  1  704  ? 19.225  37.335  65.365  1.00 13.07 ? 702  CYS   B CA    1 
ATOM   14133 C  C     . CYS   B  1  704  ? 20.332  36.532  66.007  1.00 14.69 ? 702  CYS   B C     1 
ATOM   14134 O  O     . CYS   B  1  704  ? 20.646  35.424  65.559  1.00 14.37 ? 702  CYS   B O     1 
ATOM   14135 C  CB    . CYS   B  1  704  ? 17.948  36.509  65.325  1.00 13.80 ? 702  CYS   B CB    1 
ATOM   14136 S  SG    . CYS   B  1  704  ? 16.544  37.362  64.611  1.00 15.16 ? 702  CYS   B SG    1 
ATOM   14137 N  N     . ILE   B  1  705  ? 20.912  37.094  67.054  1.00 13.14 ? 703  ILE   B N     1 
ATOM   14138 C  CA    . ILE   B  1  705  ? 22.049  36.497  67.727  1.00 14.25 ? 703  ILE   B CA    1 
ATOM   14139 C  C     . ILE   B  1  705  ? 21.609  36.221  69.149  1.00 13.87 ? 703  ILE   B C     1 
ATOM   14140 O  O     . ILE   B  1  705  ? 21.110  37.122  69.831  1.00 14.10 ? 703  ILE   B O     1 
ATOM   14141 C  CB    . ILE   B  1  705  ? 23.262  37.432  67.695  1.00 14.09 ? 703  ILE   B CB    1 
ATOM   14142 C  CG1   . ILE   B  1  705  ? 23.816  37.513  66.281  1.00 16.89 ? 703  ILE   B CG1   1 
ATOM   14143 C  CG2   . ILE   B  1  705  ? 24.319  36.939  68.652  1.00 15.10 ? 703  ILE   B CG2   1 
ATOM   14144 C  CD1   . ILE   B  1  705  ? 24.789  38.659  66.109  1.00 17.37 ? 703  ILE   B CD1   1 
ATOM   14145 N  N     . SER   B  1  706  ? 21.784  34.982  69.580  1.00 14.41 ? 704  SER   B N     1 
ATOM   14146 C  CA    . SER   B  1  706  ? 21.151  34.520  70.795  1.00 14.52 ? 704  SER   B CA    1 
ATOM   14147 C  C     . SER   B  1  706  ? 22.154  33.886  71.743  1.00 15.19 ? 704  SER   B C     1 
ATOM   14148 O  O     . SER   B  1  706  ? 23.232  33.451  71.330  1.00 15.12 ? 704  SER   B O     1 
ATOM   14149 C  CB    . SER   B  1  706  ? 20.035  33.516  70.462  1.00 15.07 ? 704  SER   B CB    1 
ATOM   14150 O  OG    . SER   B  1  706  ? 20.511  32.485  69.623  1.00 13.92 ? 704  SER   B OG    1 
ATOM   14151 N  N     . PRO   B  1  707  ? 21.834  33.871  73.028  1.00 14.58 ? 705  PRO   B N     1 
ATOM   14152 C  CA    . PRO   B  1  707  ? 22.741  33.335  74.040  1.00 15.08 ? 705  PRO   B CA    1 
ATOM   14153 C  C     . PRO   B  1  707  ? 22.534  31.834  74.187  1.00 15.70 ? 705  PRO   B C     1 
ATOM   14154 O  O     . PRO   B  1  707  ? 21.541  31.264  73.737  1.00 16.98 ? 705  PRO   B O     1 
ATOM   14155 C  CB    . PRO   B  1  707  ? 22.257  34.044  75.310  1.00 15.21 ? 705  PRO   B CB    1 
ATOM   14156 C  CG    . PRO   B  1  707  ? 20.791  34.163  75.113  1.00 14.89 ? 705  PRO   B CG    1 
ATOM   14157 C  CD    . PRO   B  1  707  ? 20.629  34.466  73.629  1.00 15.08 ? 705  PRO   B CD    1 
ATOM   14158 N  N     . TRP   B  1  708  ? 23.485  31.201  74.866  1.00 14.56 ? 706  TRP   B N     1 
ATOM   14159 C  CA    . TRP   B  1  708  ? 23.371  29.756  75.016  1.00 14.54 ? 706  TRP   B CA    1 
ATOM   14160 C  C     . TRP   B  1  708  ? 22.352  29.362  76.073  1.00 13.77 ? 706  TRP   B C     1 
ATOM   14161 O  O     . TRP   B  1  708  ? 21.855  28.234  76.044  1.00 15.68 ? 706  TRP   B O     1 
ATOM   14162 C  CB    . TRP   B  1  708  ? 24.736  29.127  75.354  1.00 15.22 ? 706  TRP   B CB    1 
ATOM   14163 C  CG    . TRP   B  1  708  ? 25.123  29.374  76.766  1.00 15.32 ? 706  TRP   B CG    1 
ATOM   14164 C  CD1   . TRP   B  1  708  ? 25.893  30.393  77.237  1.00 19.01 ? 706  TRP   B CD1   1 
ATOM   14165 C  CD2   . TRP   B  1  708  ? 24.709  28.611  77.905  1.00 16.79 ? 706  TRP   B CD2   1 
ATOM   14166 N  NE1   . TRP   B  1  708  ? 25.981  30.313  78.605  1.00 18.20 ? 706  TRP   B NE1   1 
ATOM   14167 C  CE2   . TRP   B  1  708  ? 25.263  29.227  79.036  1.00 15.37 ? 706  TRP   B CE2   1 
ATOM   14168 C  CE3   . TRP   B  1  708  ? 23.938  27.456  78.072  1.00 16.72 ? 706  TRP   B CE3   1 
ATOM   14169 C  CZ2   . TRP   B  1  708  ? 25.054  28.739  80.321  1.00 16.42 ? 706  TRP   B CZ2   1 
ATOM   14170 C  CZ3   . TRP   B  1  708  ? 23.730  26.971  79.343  1.00 15.99 ? 706  TRP   B CZ3   1 
ATOM   14171 C  CH2   . TRP   B  1  708  ? 24.291  27.609  80.455  1.00 17.33 ? 706  TRP   B CH2   1 
ATOM   14172 N  N     . ASN   B  1  709  ? 22.062  30.244  77.028  1.00 15.07 ? 707  ASN   B N     1 
ATOM   14173 C  CA    . ASN   B  1  709  ? 21.499  29.756  78.284  1.00 15.20 ? 707  ASN   B CA    1 
ATOM   14174 C  C     . ASN   B  1  709  ? 20.003  29.541  78.235  1.00 16.56 ? 707  ASN   B C     1 
ATOM   14175 O  O     . ASN   B  1  709  ? 19.481  28.784  79.056  1.00 17.82 ? 707  ASN   B O     1 
ATOM   14176 C  CB    . ASN   B  1  709  ? 21.845  30.708  79.421  1.00 15.43 ? 707  ASN   B CB    1 
ATOM   14177 C  CG    . ASN   B  1  709  ? 21.111  32.007  79.309  1.00 16.76 ? 707  ASN   B CG    1 
ATOM   14178 O  OD1   . ASN   B  1  709  ? 21.369  32.797  78.412  1.00 20.51 ? 707  ASN   B OD1   1 
ATOM   14179 N  ND2   . ASN   B  1  709  ? 20.155  32.223  80.202  1.00 18.99 ? 707  ASN   B ND2   1 
ATOM   14180 N  N     . PHE   B  1  710  ? 19.313  30.205  77.315  1.00 15.48 ? 708  PHE   B N     1 
ATOM   14181 C  CA    . PHE   B  1  710  ? 17.924  29.914  76.984  1.00 17.55 ? 708  PHE   B CA    1 
ATOM   14182 C  C     . PHE   B  1  710  ? 17.964  29.538  75.512  1.00 16.52 ? 708  PHE   B C     1 
ATOM   14183 O  O     . PHE   B  1  710  ? 17.561  30.315  74.637  1.00 15.79 ? 708  PHE   B O     1 
ATOM   14184 C  CB    . PHE   B  1  710  ? 17.008  31.111  77.237  1.00 16.02 ? 708  PHE   B CB    1 
ATOM   14185 C  CG    . PHE   B  1  710  ? 16.935  31.534  78.692  1.00 18.51 ? 708  PHE   B CG    1 
ATOM   14186 C  CD1   . PHE   B  1  710  ? 16.857  30.592  79.710  1.00 20.01 ? 708  PHE   B CD1   1 
ATOM   14187 C  CD2   . PHE   B  1  710  ? 16.947  32.875  79.033  1.00 19.46 ? 708  PHE   B CD2   1 
ATOM   14188 C  CE1   . PHE   B  1  710  ? 16.782  30.991  81.040  1.00 19.89 ? 708  PHE   B CE1   1 
ATOM   14189 C  CE2   . PHE   B  1  710  ? 16.870  33.287  80.358  1.00 20.02 ? 708  PHE   B CE2   1 
ATOM   14190 C  CZ    . PHE   B  1  710  ? 16.796  32.346  81.361  1.00 21.04 ? 708  PHE   B CZ    1 
ATOM   14191 N  N     . PRO   B  1  711  ? 18.461  28.338  75.208  1.00 16.29 ? 709  PRO   B N     1 
ATOM   14192 C  CA    . PRO   B  1  711  ? 18.903  28.040  73.838  1.00 16.28 ? 709  PRO   B CA    1 
ATOM   14193 C  C     . PRO   B  1  711  ? 17.780  27.823  72.848  1.00 15.86 ? 709  PRO   B C     1 
ATOM   14194 O  O     . PRO   B  1  711  ? 18.044  27.825  71.640  1.00 16.15 ? 709  PRO   B O     1 
ATOM   14195 C  CB    . PRO   B  1  711  ? 19.737  26.766  74.017  1.00 16.66 ? 709  PRO   B CB    1 
ATOM   14196 C  CG    . PRO   B  1  711  ? 19.067  26.095  75.202  1.00 16.58 ? 709  PRO   B CG    1 
ATOM   14197 C  CD    . PRO   B  1  711  ? 18.723  27.222  76.134  1.00 15.53 ? 709  PRO   B CD    1 
ATOM   14198 N  N     . LEU   B  1  712  ? 16.553  27.597  73.304  1.00 13.79 ? 710  LEU   B N     1 
ATOM   14199 C  CA    . LEU   B  1  712  ? 15.412  27.550  72.405  1.00 14.80 ? 710  LEU   B CA    1 
ATOM   14200 C  C     . LEU   B  1  712  ? 14.478  28.728  72.587  1.00 15.48 ? 710  LEU   B C     1 
ATOM   14201 O  O     . LEU   B  1  712  ? 13.957  29.249  71.604  1.00 16.61 ? 710  LEU   B O     1 
ATOM   14202 C  CB    . LEU   B  1  712  ? 14.636  26.243  72.595  1.00 14.79 ? 710  LEU   B CB    1 
ATOM   14203 C  CG    . LEU   B  1  712  ? 13.438  26.057  71.660  1.00 13.84 ? 710  LEU   B CG    1 
ATOM   14204 C  CD1   . LEU   B  1  712  ? 13.860  25.991  70.197  1.00 15.22 ? 710  LEU   B CD1   1 
ATOM   14205 C  CD2   . LEU   B  1  712  ? 12.667  24.811  72.052  1.00 18.94 ? 710  LEU   B CD2   1 
ATOM   14206 N  N     . ALA   B  1  713  ? 14.299  29.203  73.814  1.00 14.36 ? 711  ALA   B N     1 
ATOM   14207 C  CA    . ALA   B  1  713  ? 13.266  30.201  74.057  1.00 15.13 ? 711  ALA   B CA    1 
ATOM   14208 C  C     . ALA   B  1  713  ? 13.645  31.562  73.485  1.00 14.65 ? 711  ALA   B C     1 
ATOM   14209 O  O     . ALA   B  1  713  ? 12.901  32.132  72.683  1.00 15.12 ? 711  ALA   B O     1 
ATOM   14210 C  CB    . ALA   B  1  713  ? 12.970  30.288  75.551  1.00 16.51 ? 711  ALA   B CB    1 
ATOM   14211 N  N     . ILE   B  1  714  ? 14.797  32.108  73.885  1.00 15.21 ? 712  ILE   B N     1 
ATOM   14212 C  CA    . ILE   B  1  714  ? 15.185  33.412  73.358  1.00 15.23 ? 712  ILE   B CA    1 
ATOM   14213 C  C     . ILE   B  1  714  ? 15.504  33.296  71.880  1.00 15.32 ? 712  ILE   B C     1 
ATOM   14214 O  O     . ILE   B  1  714  ? 15.141  34.164  71.074  1.00 14.67 ? 712  ILE   B O     1 
ATOM   14215 C  CB    . ILE   B  1  714  ? 16.356  33.990  74.168  1.00 15.00 ? 712  ILE   B CB    1 
ATOM   14216 C  CG1   . ILE   B  1  714  ? 15.815  34.409  75.536  1.00 17.88 ? 712  ILE   B CG1   1 
ATOM   14217 C  CG2   . ILE   B  1  714  ? 17.000  35.149  73.391  1.00 16.13 ? 712  ILE   B CG2   1 
ATOM   14218 C  CD1   . ILE   B  1  714  ? 16.784  35.156  76.368  1.00 25.66 ? 712  ILE   B CD1   1 
ATOM   14219 N  N     . PHE   B  1  715  ? 16.145  32.192  71.499  1.00 14.20 ? 713  PHE   B N     1 
ATOM   14220 C  CA    . PHE   B  1  715  ? 16.405  31.908  70.094  1.00 13.04 ? 713  PHE   B CA    1 
ATOM   14221 C  C     . PHE   B  1  715  ? 15.129  32.025  69.271  1.00 13.80 ? 713  PHE   B C     1 
ATOM   14222 O  O     . PHE   B  1  715  ? 15.082  32.765  68.282  1.00 14.48 ? 713  PHE   B O     1 
ATOM   14223 C  CB    . PHE   B  1  715  ? 16.968  30.498  69.973  1.00 13.63 ? 713  PHE   B CB    1 
ATOM   14224 C  CG    . PHE   B  1  715  ? 17.222  30.084  68.560  1.00 14.31 ? 713  PHE   B CG    1 
ATOM   14225 C  CD1   . PHE   B  1  715  ? 18.352  30.524  67.905  1.00 14.01 ? 713  PHE   B CD1   1 
ATOM   14226 C  CD2   . PHE   B  1  715  ? 16.322  29.271  67.882  1.00 14.79 ? 713  PHE   B CD2   1 
ATOM   14227 C  CE1   . PHE   B  1  715  ? 18.585  30.164  66.600  1.00 15.36 ? 713  PHE   B CE1   1 
ATOM   14228 C  CE2   . PHE   B  1  715  ? 16.545  28.908  66.578  1.00 15.24 ? 713  PHE   B CE2   1 
ATOM   14229 C  CZ    . PHE   B  1  715  ? 17.677  29.347  65.935  1.00 14.46 ? 713  PHE   B CZ    1 
ATOM   14230 N  N     . THR   B  1  716  ? 14.076  31.310  69.686  1.00 13.15 ? 714  THR   B N     1 
ATOM   14231 C  CA    . THR   B  1  716  ? 12.812  31.313  68.957  1.00 13.42 ? 714  THR   B CA    1 
ATOM   14232 C  C     . THR   B  1  716  ? 12.130  32.667  69.045  1.00 13.73 ? 714  THR   B C     1 
ATOM   14233 O  O     . THR   B  1  716  ? 11.557  33.139  68.057  1.00 14.23 ? 714  THR   B O     1 
ATOM   14234 C  CB    . THR   B  1  716  ? 11.897  30.228  69.525  1.00 14.32 ? 714  THR   B CB    1 
ATOM   14235 O  OG1   . THR   B  1  716  ? 12.493  28.941  69.337  1.00 15.99 ? 714  THR   B OG1   1 
ATOM   14236 C  CG2   . THR   B  1  716  ? 10.543  30.248  68.830  1.00 15.78 ? 714  THR   B CG2   1 
ATOM   14237 N  N     . GLY   B  1  717  ? 12.159  33.299  70.219  1.00 14.11 ? 715  GLY   B N     1 
ATOM   14238 C  CA    . GLY   B  1  717  ? 11.471  34.571  70.382  1.00 15.00 ? 715  GLY   B CA    1 
ATOM   14239 C  C     . GLY   B  1  717  ? 11.955  35.634  69.414  1.00 14.44 ? 715  GLY   B C     1 
ATOM   14240 O  O     . GLY   B  1  717  ? 11.159  36.284  68.731  1.00 14.33 ? 715  GLY   B O     1 
ATOM   14241 N  N     . GLN   B  1  718  ? 13.269  35.816  69.330  1.00 13.41 ? 716  GLN   B N     1 
ATOM   14242 C  CA    . GLN   B  1  718  ? 13.779  36.855  68.450  1.00 12.94 ? 716  GLN   B CA    1 
ATOM   14243 C  C     . GLN   B  1  718  ? 13.437  36.548  67.007  1.00 13.56 ? 716  GLN   B C     1 
ATOM   14244 O  O     . GLN   B  1  718  ? 12.996  37.424  66.265  1.00 14.26 ? 716  GLN   B O     1 
ATOM   14245 C  CB    . GLN   B  1  718  ? 15.290  36.990  68.610  1.00 13.15 ? 716  GLN   B CB    1 
ATOM   14246 C  CG    . GLN   B  1  718  ? 15.713  37.389  70.028  1.00 13.12 ? 716  GLN   B CG    1 
ATOM   14247 C  CD    . GLN   B  1  718  ? 17.188  37.669  70.133  1.00 14.74 ? 716  GLN   B CD    1 
ATOM   14248 O  OE1   . GLN   B  1  718  ? 17.581  38.667  70.730  1.00 15.03 ? 716  GLN   B OE1   1 
ATOM   14249 N  NE2   . GLN   B  1  718  ? 18.020  36.800  69.551  1.00 15.29 ? 716  GLN   B NE2   1 
ATOM   14250 N  N     . ILE   B  1  719  ? 13.639  35.300  66.602  1.00 12.92 ? 717  ILE   B N     1 
ATOM   14251 C  CA    . ILE   B  1  719  ? 13.422  34.916  65.216  1.00 13.73 ? 717  ILE   B CA    1 
ATOM   14252 C  C     . ILE   B  1  719  ? 11.954  35.056  64.870  1.00 14.36 ? 717  ILE   B C     1 
ATOM   14253 O  O     . ILE   B  1  719  ? 11.594  35.574  63.811  1.00 14.42 ? 717  ILE   B O     1 
ATOM   14254 C  CB    . ILE   B  1  719  ? 13.899  33.474  65.008  1.00 15.17 ? 717  ILE   B CB    1 
ATOM   14255 C  CG1   . ILE   B  1  719  ? 15.417  33.417  65.085  1.00 14.73 ? 717  ILE   B CG1   1 
ATOM   14256 C  CG2   . ILE   B  1  719  ? 13.384  32.910  63.699  1.00 18.48 ? 717  ILE   B CG2   1 
ATOM   14257 C  CD1   . ILE   B  1  719  ? 15.889  32.019  65.230  1.00 19.54 ? 717  ILE   B CD1   1 
ATOM   14258 N  N     . ALA   B  1  720  ? 11.089  34.590  65.763  1.00 13.50 ? 718  ALA   B N     1 
ATOM   14259 C  CA    . ALA   B  1  720  ? 9.664   34.620  65.494  1.00 13.77 ? 718  ALA   B CA    1 
ATOM   14260 C  C     . ALA   B  1  720  ? 9.196   36.050  65.304  1.00 13.73 ? 718  ALA   B C     1 
ATOM   14261 O  O     . ALA   B  1  720  ? 8.399   36.339  64.398  1.00 13.77 ? 718  ALA   B O     1 
ATOM   14262 C  CB    . ALA   B  1  720  ? 8.912   33.940  66.640  1.00 14.37 ? 718  ALA   B CB    1 
ATOM   14263 N  N     . ALA   B  1  721  ? 9.622   36.948  66.198  1.00 13.64 ? 719  ALA   B N     1 
ATOM   14264 C  CA    . ALA   B  1  721  ? 9.211   38.342  66.088  1.00 13.33 ? 719  ALA   B CA    1 
ATOM   14265 C  C     . ALA   B  1  721  ? 9.680   38.947  64.779  1.00 12.74 ? 719  ALA   B C     1 
ATOM   14266 O  O     . ALA   B  1  721  ? 8.915   39.605  64.066  1.00 13.79 ? 719  ALA   B O     1 
ATOM   14267 C  CB    . ALA   B  1  721  ? 9.765   39.139  67.268  1.00 14.07 ? 719  ALA   B CB    1 
ATOM   14268 N  N     . ALA   B  1  722  ? 10.945  38.744  64.455  1.00 13.02 ? 720  ALA   B N     1 
ATOM   14269 C  CA    . ALA   B  1  722  ? 11.469  39.308  63.221  1.00 12.51 ? 720  ALA   B CA    1 
ATOM   14270 C  C     . ALA   B  1  722  ? 10.721  38.767  62.012  1.00 13.54 ? 720  ALA   B C     1 
ATOM   14271 O  O     . ALA   B  1  722  ? 10.321  39.529  61.130  1.00 13.99 ? 720  ALA   B O     1 
ATOM   14272 C  CB    . ALA   B  1  722  ? 12.964  39.015  63.121  1.00 13.90 ? 720  ALA   B CB    1 
ATOM   14273 N  N     . LEU   B  1  723  ? 10.506  37.454  61.975  1.00 14.07 ? 721  LEU   B N     1 
ATOM   14274 C  CA    . LEU   B  1  723  ? 9.799   36.841  60.854  1.00 14.19 ? 721  LEU   B CA    1 
ATOM   14275 C  C     . LEU   B  1  723  ? 8.379   37.364  60.741  1.00 14.34 ? 721  LEU   B C     1 
ATOM   14276 O  O     . LEU   B  1  723  ? 7.903   37.672  59.643  1.00 15.08 ? 721  LEU   B O     1 
ATOM   14277 C  CB    . LEU   B  1  723  ? 9.740   35.332  61.057  1.00 14.89 ? 721  LEU   B CB    1 
ATOM   14278 C  CG    . LEU   B  1  723  ? 11.030  34.564  60.814  1.00 14.79 ? 721  LEU   B CG    1 
ATOM   14279 C  CD1   . LEU   B  1  723  ? 10.820  33.147  61.275  1.00 15.51 ? 721  LEU   B CD1   1 
ATOM   14280 C  CD2   . LEU   B  1  723  ? 11.408  34.625  59.339  1.00 15.95 ? 721  LEU   B CD2   1 
ATOM   14281 N  N     . VAL   B  1  724  ? 7.656   37.406  61.858  1.00 12.91 ? 722  VAL   B N     1 
ATOM   14282 C  CA    . VAL   B  1  724  ? 6.250   37.755  61.756  1.00 13.31 ? 722  VAL   B CA    1 
ATOM   14283 C  C     . VAL   B  1  724  ? 6.085   39.219  61.395  1.00 13.79 ? 722  VAL   B C     1 
ATOM   14284 O  O     . VAL   B  1  724  ? 5.078   39.604  60.784  1.00 15.48 ? 722  VAL   B O     1 
ATOM   14285 C  CB    . VAL   B  1  724  ? 5.496   37.331  63.026  1.00 13.61 ? 722  VAL   B CB    1 
ATOM   14286 C  CG1   . VAL   B  1  724  ? 5.663   38.357  64.157  1.00 15.76 ? 722  VAL   B CG1   1 
ATOM   14287 C  CG2   . VAL   B  1  724  ? 4.036   37.099  62.713  1.00 14.28 ? 722  VAL   B CG2   1 
ATOM   14288 N  N     . ALA   B  1  725  ? 7.069   40.049  61.740  1.00 14.98 ? 723  ALA   B N     1 
ATOM   14289 C  CA    . ALA   B  1  725  ? 7.089   41.437  61.307  1.00 15.39 ? 723  ALA   B CA    1 
ATOM   14290 C  C     . ALA   B  1  725  ? 7.429   41.581  59.831  1.00 15.86 ? 723  ALA   B C     1 
ATOM   14291 O  O     . ALA   B  1  725  ? 7.439   42.709  59.322  1.00 17.99 ? 723  ALA   B O     1 
ATOM   14292 C  CB    . ALA   B  1  725  ? 8.056   42.239  62.186  1.00 15.96 ? 723  ALA   B CB    1 
ATOM   14293 N  N     . GLY   B  1  726  ? 7.695   40.481  59.136  1.00 14.49 ? 724  GLY   B N     1 
ATOM   14294 C  CA    . GLY   B  1  726  ? 7.910   40.519  57.706  1.00 15.34 ? 724  GLY   B CA    1 
ATOM   14295 C  C     . GLY   B  1  726  ? 9.352   40.535  57.272  1.00 16.63 ? 724  GLY   B C     1 
ATOM   14296 O  O     . GLY   B  1  726  ? 9.622   40.848  56.104  1.00 17.47 ? 724  GLY   B O     1 
ATOM   14297 N  N     . ASN   B  1  727  ? 10.284  40.201  58.163  1.00 15.08 ? 725  ASN   B N     1 
ATOM   14298 C  CA    . ASN   B  1  727  ? 11.705  40.256  57.889  1.00 14.76 ? 725  ASN   B CA    1 
ATOM   14299 C  C     . ASN   B  1  727  ? 12.248  38.853  57.734  1.00 14.39 ? 725  ASN   B C     1 
ATOM   14300 O  O     . ASN   B  1  727  ? 11.957  37.986  58.566  1.00 16.51 ? 725  ASN   B O     1 
ATOM   14301 C  CB    . ASN   B  1  727  ? 12.441  40.920  59.048  1.00 15.36 ? 725  ASN   B CB    1 
ATOM   14302 C  CG    . ASN   B  1  727  ? 11.890  42.274  59.399  1.00 16.66 ? 725  ASN   B CG    1 
ATOM   14303 O  OD1   . ASN   B  1  727  ? 12.179  43.271  58.728  1.00 16.72 ? 725  ASN   B OD1   1 
ATOM   14304 N  ND2   . ASN   B  1  727  ? 11.101  42.329  60.472  1.00 15.43 ? 725  ASN   B ND2   1 
ATOM   14305 N  N     . PRO   B  1  728  ? 13.053  38.592  56.718  1.00 14.85 ? 726  PRO   B N     1 
ATOM   14306 C  CA    . PRO   B  1  728  ? 13.795  37.337  56.700  1.00 15.58 ? 726  PRO   B CA    1 
ATOM   14307 C  C     . PRO   B  1  728  ? 14.872  37.408  57.759  1.00 16.75 ? 726  PRO   B C     1 
ATOM   14308 O  O     . PRO   B  1  728  ? 15.353  38.488  58.107  1.00 16.29 ? 726  PRO   B O     1 
ATOM   14309 C  CB    . PRO   B  1  728  ? 14.412  37.312  55.305  1.00 16.06 ? 726  PRO   B CB    1 
ATOM   14310 C  CG    . PRO   B  1  728  ? 14.575  38.764  54.947  1.00 17.39 ? 726  PRO   B CG    1 
ATOM   14311 C  CD    . PRO   B  1  728  ? 13.445  39.507  55.634  1.00 15.50 ? 726  PRO   B CD    1 
ATOM   14312 N  N     . VAL   B  1  729  ? 15.242  36.243  58.270  1.00 14.35 ? 727  VAL   B N     1 
ATOM   14313 C  CA    . VAL   B  1  729  ? 16.083  36.146  59.454  1.00 15.10 ? 727  VAL   B CA    1 
ATOM   14314 C  C     . VAL   B  1  729  ? 17.323  35.333  59.149  1.00 16.76 ? 727  VAL   B C     1 
ATOM   14315 O  O     . VAL   B  1  729  ? 17.264  34.283  58.490  1.00 15.53 ? 727  VAL   B O     1 
ATOM   14316 C  CB    . VAL   B  1  729  ? 15.306  35.495  60.608  1.00 14.38 ? 727  VAL   B CB    1 
ATOM   14317 C  CG1   . VAL   B  1  729  ? 16.264  35.103  61.743  1.00 14.38 ? 727  VAL   B CG1   1 
ATOM   14318 C  CG2   . VAL   B  1  729  ? 14.278  36.459  61.117  1.00 16.25 ? 727  VAL   B CG2   1 
ATOM   14319 N  N     . LEU   B  1  730  ? 18.444  35.818  59.660  1.00 14.49 ? 728  LEU   B N     1 
ATOM   14320 C  CA    . LEU   B  1  730  ? 19.685  35.067  59.764  1.00 15.32 ? 728  LEU   B CA    1 
ATOM   14321 C  C     . LEU   B  1  730  ? 19.833  34.729  61.240  1.00 13.25 ? 728  LEU   B C     1 
ATOM   14322 O  O     . LEU   B  1  730  ? 20.042  35.620  62.066  1.00 15.73 ? 728  LEU   B O     1 
ATOM   14323 C  CB    . LEU   B  1  730  ? 20.872  35.902  59.291  1.00 15.79 ? 728  LEU   B CB    1 
ATOM   14324 C  CG    . LEU   B  1  730  ? 20.890  36.403  57.845  1.00 16.07 ? 728  LEU   B CG    1 
ATOM   14325 C  CD1   . LEU   B  1  730  ? 20.506  35.283  56.870  1.00 16.66 ? 728  LEU   B CD1   1 
ATOM   14326 C  CD2   . LEU   B  1  730  ? 20.041  37.643  57.630  1.00 16.49 ? 728  LEU   B CD2   1 
ATOM   14327 N  N     . ALA   B  1  731  ? 19.699  33.463  61.575  1.00 14.16 ? 729  ALA   B N     1 
ATOM   14328 C  CA    . ALA   B  1  731  ? 19.681  33.020  62.959  1.00 13.42 ? 729  ALA   B CA    1 
ATOM   14329 C  C     . ALA   B  1  731  ? 21.060  32.488  63.309  1.00 14.72 ? 729  ALA   B C     1 
ATOM   14330 O  O     . ALA   B  1  731  ? 21.493  31.476  62.755  1.00 14.29 ? 729  ALA   B O     1 
ATOM   14331 C  CB    . ALA   B  1  731  ? 18.614  31.944  63.133  1.00 15.93 ? 729  ALA   B CB    1 
ATOM   14332 N  N     . LYS   B  1  732  ? 21.735  33.167  64.232  1.00 13.78 ? 730  LYS   B N     1 
ATOM   14333 C  CA    . LYS   B  1  732  ? 23.071  32.794  64.682  1.00 14.80 ? 730  LYS   B CA    1 
ATOM   14334 C  C     . LYS   B  1  732  ? 22.984  32.367  66.137  1.00 14.39 ? 730  LYS   B C     1 
ATOM   14335 O  O     . LYS   B  1  732  ? 23.004  33.221  67.042  1.00 15.36 ? 730  LYS   B O     1 
ATOM   14336 C  CB    . LYS   B  1  732  ? 24.043  33.965  64.516  1.00 17.05 ? 730  LYS   B CB    1 
ATOM   14337 C  CG    . LYS   B  1  732  ? 25.474  33.571  64.179  1.00 16.47 ? 730  LYS   B CG    1 
ATOM   14338 C  CD    . LYS   B  1  732  ? 26.097  32.680  65.224  1.00 16.73 ? 730  LYS   B CD    1 
ATOM   14339 C  CE    . LYS   B  1  732  ? 26.434  33.450  66.482  1.00 15.99 ? 730  LYS   B CE    1 
ATOM   14340 N  NZ    . LYS   B  1  732  ? 27.030  32.531  67.485  1.00 15.72 ? 730  LYS   B NZ    1 
ATOM   14341 N  N     . PRO   B  1  733  ? 22.871  31.078  66.410  1.00 13.91 ? 731  PRO   B N     1 
ATOM   14342 C  CA    . PRO   B  1  733  ? 22.734  30.616  67.790  1.00 14.84 ? 731  PRO   B CA    1 
ATOM   14343 C  C     . PRO   B  1  733  ? 24.097  30.602  68.448  1.00 14.05 ? 731  PRO   B C     1 
ATOM   14344 O  O     . PRO   B  1  733  ? 25.140  30.579  67.795  1.00 14.76 ? 731  PRO   B O     1 
ATOM   14345 C  CB    . PRO   B  1  733  ? 22.242  29.182  67.620  1.00 15.95 ? 731  PRO   B CB    1 
ATOM   14346 C  CG    . PRO   B  1  733  ? 22.851  28.747  66.313  1.00 16.07 ? 731  PRO   B CG    1 
ATOM   14347 C  CD    . PRO   B  1  733  ? 22.802  29.979  65.433  1.00 15.04 ? 731  PRO   B CD    1 
ATOM   14348 N  N     . ALA   B  1  734  ? 24.072  30.613  69.773  1.00 14.86 ? 732  ALA   B N     1 
ATOM   14349 C  CA    . ALA   B  1  734  ? 25.318  30.543  70.525  1.00 14.35 ? 732  ALA   B CA    1 
ATOM   14350 C  C     . ALA   B  1  734  ? 26.093  29.288  70.152  1.00 15.74 ? 732  ALA   B C     1 
ATOM   14351 O  O     . ALA   B  1  734  ? 25.531  28.244  69.819  1.00 16.53 ? 732  ALA   B O     1 
ATOM   14352 C  CB    . ALA   B  1  734  ? 25.001  30.498  72.017  1.00 16.59 ? 732  ALA   B CB    1 
ATOM   14353 N  N     . GLU   B  1  735  ? 27.417  29.391  70.227  1.00 15.31 ? 733  GLU   B N     1 
ATOM   14354 C  CA    . GLU   B  1  735  ? 28.241  28.265  69.807  1.00 16.68 ? 733  GLU   B CA    1 
ATOM   14355 C  C     . GLU   B  1  735  ? 28.058  27.053  70.708  1.00 14.94 ? 733  GLU   B C     1 
ATOM   14356 O  O     . GLU   B  1  735  ? 28.265  25.918  70.268  1.00 15.97 ? 733  GLU   B O     1 
ATOM   14357 C  CB    . GLU   B  1  735  ? 29.717  28.666  69.733  1.00 17.78 ? 733  GLU   B CB    1 
ATOM   14358 C  CG    . GLU   B  1  735  ? 30.273  29.294  70.997  1.00 22.09 ? 733  GLU   B CG    1 
ATOM   14359 C  CD    . GLU   B  1  735  ? 30.166  30.815  71.010  1.00 23.62 ? 733  GLU   B CD    1 
ATOM   14360 O  OE1   . GLU   B  1  735  ? 29.189  31.369  70.463  1.00 22.29 ? 733  GLU   B OE1   1 
ATOM   14361 O  OE2   . GLU   B  1  735  ? 31.073  31.467  71.576  1.00 24.28 ? 733  GLU   B OE2   1 
ATOM   14362 N  N     . GLU   B  1  736  ? 27.648  27.270  71.959  1.00 15.65 ? 734  GLU   B N     1 
ATOM   14363 C  CA    . GLU   B  1  736  ? 27.515  26.163  72.895  1.00 17.43 ? 734  GLU   B CA    1 
ATOM   14364 C  C     . GLU   B  1  736  ? 26.286  25.308  72.606  1.00 16.69 ? 734  GLU   B C     1 
ATOM   14365 O  O     . GLU   B  1  736  ? 26.265  24.121  72.957  1.00 18.40 ? 734  GLU   B O     1 
ATOM   14366 C  CB    . GLU   B  1  736  ? 27.414  26.700  74.322  1.00 16.43 ? 734  GLU   B CB    1 
ATOM   14367 C  CG    . GLU   B  1  736  ? 28.673  27.414  74.794  1.00 18.63 ? 734  GLU   B CG    1 
ATOM   14368 C  CD    . GLU   B  1  736  ? 28.640  28.914  74.571  1.00 18.12 ? 734  GLU   B CD    1 
ATOM   14369 O  OE1   . GLU   B  1  736  ? 27.854  29.392  73.730  1.00 18.33 ? 734  GLU   B OE1   1 
ATOM   14370 O  OE2   . GLU   B  1  736  ? 29.423  29.619  75.241  1.00 25.25 ? 734  GLU   B OE2   1 
ATOM   14371 N  N     . THR   B  1  737  ? 25.241  25.884  72.006  1.00 16.08 ? 735  THR   B N     1 
ATOM   14372 C  CA    . THR   B  1  737  ? 23.931  25.224  71.940  1.00 16.43 ? 735  THR   B CA    1 
ATOM   14373 C  C     . THR   B  1  737  ? 23.324  25.274  70.542  1.00 15.32 ? 735  THR   B C     1 
ATOM   14374 O  O     . THR   B  1  737  ? 22.178  25.682  70.364  1.00 16.72 ? 735  THR   B O     1 
ATOM   14375 C  CB    . THR   B  1  737  ? 22.971  25.816  72.969  1.00 15.95 ? 735  THR   B CB    1 
ATOM   14376 O  OG1   . THR   B  1  737  ? 22.900  27.239  72.802  1.00 16.22 ? 735  THR   B OG1   1 
ATOM   14377 C  CG2   . THR   B  1  737  ? 23.445  25.481  74.370  1.00 17.61 ? 735  THR   B CG2   1 
ATOM   14378 N  N     . PRO   B  1  738  ? 24.052  24.823  69.527  1.00 15.12 ? 736  PRO   B N     1 
ATOM   14379 C  CA    . PRO   B  1  738  ? 23.513  24.895  68.163  1.00 15.57 ? 736  PRO   B CA    1 
ATOM   14380 C  C     . PRO   B  1  738  ? 22.458  23.855  67.864  1.00 16.11 ? 736  PRO   B C     1 
ATOM   14381 O  O     . PRO   B  1  738  ? 21.679  24.068  66.932  1.00 15.28 ? 736  PRO   B O     1 
ATOM   14382 C  CB    . PRO   B  1  738  ? 24.752  24.639  67.298  1.00 15.92 ? 736  PRO   B CB    1 
ATOM   14383 C  CG    . PRO   B  1  738  ? 25.564  23.700  68.140  1.00 17.26 ? 736  PRO   B CG    1 
ATOM   14384 C  CD    . PRO   B  1  738  ? 25.389  24.204  69.553  1.00 16.52 ? 736  PRO   B CD    1 
ATOM   14385 N  N     . LEU   B  1  739  ? 22.413  22.732  68.588  1.00 15.43 ? 737  LEU   B N     1 
ATOM   14386 C  CA    . LEU   B  1  739  ? 21.549  21.641  68.147  1.00 16.12 ? 737  LEU   B CA    1 
ATOM   14387 C  C     . LEU   B  1  739  ? 20.083  21.978  68.360  1.00 14.92 ? 737  LEU   B C     1 
ATOM   14388 O  O     . LEU   B  1  739  ? 19.256  21.766  67.467  1.00 15.28 ? 737  LEU   B O     1 
ATOM   14389 C  CB    . LEU   B  1  739  ? 21.901  20.355  68.874  1.00 14.70 ? 737  LEU   B CB    1 
ATOM   14390 C  CG    . LEU   B  1  739  ? 23.341  19.904  68.670  1.00 15.10 ? 737  LEU   B CG    1 
ATOM   14391 C  CD1   . LEU   B  1  739  ? 23.554  18.656  69.492  1.00 18.19 ? 737  LEU   B CD1   1 
ATOM   14392 C  CD2   . LEU   B  1  739  ? 23.627  19.640  67.198  1.00 16.90 ? 737  LEU   B CD2   1 
ATOM   14393 N  N     . ILE   B  1  740  ? 19.740  22.511  69.532  1.00 14.67 ? 738  ILE   B N     1 
ATOM   14394 C  CA    . ILE   B  1  740  ? 18.336  22.838  69.749  1.00 13.91 ? 738  ILE   B CA    1 
ATOM   14395 C  C     . ILE   B  1  740  ? 17.929  23.996  68.854  1.00 14.89 ? 738  ILE   B C     1 
ATOM   14396 O  O     . ILE   B  1  740  ? 16.775  24.088  68.429  1.00 15.17 ? 738  ILE   B O     1 
ATOM   14397 C  CB    . ILE   B  1  740  ? 18.039  23.096  71.242  1.00 17.17 ? 738  ILE   B CB    1 
ATOM   14398 C  CG1   . ILE   B  1  740  ? 16.532  23.247  71.486  1.00 15.48 ? 738  ILE   B CG1   1 
ATOM   14399 C  CG2   . ILE   B  1  740  ? 18.791  24.313  71.723  1.00 18.77 ? 738  ILE   B CG2   1 
ATOM   14400 C  CD1   . ILE   B  1  740  ? 15.748  22.013  71.181  1.00 18.71 ? 738  ILE   B CD1   1 
ATOM   14401 N  N     . ALA   B  1  741  ? 18.858  24.903  68.554  1.00 14.34 ? 739  ALA   B N     1 
ATOM   14402 C  CA    . ALA   B  1  741  ? 18.554  25.989  67.634  1.00 14.78 ? 739  ALA   B CA    1 
ATOM   14403 C  C     . ALA   B  1  741  ? 18.254  25.443  66.250  1.00 14.77 ? 739  ALA   B C     1 
ATOM   14404 O  O     . ALA   B  1  741  ? 17.294  25.874  65.596  1.00 14.71 ? 739  ALA   B O     1 
ATOM   14405 C  CB    . ALA   B  1  741  ? 19.745  26.937  67.553  1.00 16.05 ? 739  ALA   B CB    1 
ATOM   14406 N  N     . ALA   B  1  742  ? 19.048  24.472  65.802  1.00 14.37 ? 740  ALA   B N     1 
ATOM   14407 C  CA    . ALA   B  1  742  ? 18.796  23.846  64.514  1.00 15.27 ? 740  ALA   B CA    1 
ATOM   14408 C  C     . ALA   B  1  742  ? 17.416  23.218  64.502  1.00 14.56 ? 740  ALA   B C     1 
ATOM   14409 O  O     . ALA   B  1  742  ? 16.680  23.314  63.510  1.00 15.03 ? 740  ALA   B O     1 
ATOM   14410 C  CB    . ALA   B  1  742  ? 19.867  22.794  64.217  1.00 15.90 ? 740  ALA   B CB    1 
ATOM   14411 N  N     . GLU   B  1  743  ? 17.034  22.602  65.620  1.00 15.33 ? 741  GLU   B N     1 
ATOM   14412 C  CA    . GLU   B  1  743  ? 15.712  22.004  65.700  1.00 15.90 ? 741  GLU   B CA    1 
ATOM   14413 C  C     . GLU   B  1  743  ? 14.626  23.065  65.655  1.00 14.32 ? 741  GLU   B C     1 
ATOM   14414 O  O     . GLU   B  1  743  ? 13.606  22.879  64.990  1.00 15.35 ? 741  GLU   B O     1 
ATOM   14415 C  CB    . GLU   B  1  743  ? 15.617  21.134  66.946  1.00 16.52 ? 741  GLU   B CB    1 
ATOM   14416 C  CG    . GLU   B  1  743  ? 14.272  20.489  67.094  1.00 16.08 ? 741  GLU   B CG    1 
ATOM   14417 C  CD    . GLU   B  1  743  ? 13.984  19.410  66.082  1.00 20.23 ? 741  GLU   B CD    1 
ATOM   14418 O  OE1   . GLU   B  1  743  ? 14.858  19.041  65.270  1.00 19.16 ? 741  GLU   B OE1   1 
ATOM   14419 O  OE2   . GLU   B  1  743  ? 12.843  18.913  66.103  1.00 21.62 ? 741  GLU   B OE2   1 
ATOM   14420 N  N     . GLY   B  1  744  ? 14.839  24.202  66.316  1.00 15.45 ? 742  GLY   B N     1 
ATOM   14421 C  CA    . GLY   B  1  744  ? 13.889  25.292  66.206  1.00 16.44 ? 742  GLY   B CA    1 
ATOM   14422 C  C     . GLY   B  1  744  ? 13.697  25.742  64.772  1.00 14.27 ? 742  GLY   B C     1 
ATOM   14423 O  O     . GLY   B  1  744  ? 12.571  25.980  64.331  1.00 15.29 ? 742  GLY   B O     1 
ATOM   14424 N  N     . VAL   B  1  745  ? 14.790  25.862  64.026  1.00 15.07 ? 743  VAL   B N     1 
ATOM   14425 C  CA    . VAL   B  1  745  ? 14.680  26.275  62.635  1.00 13.79 ? 743  VAL   B CA    1 
ATOM   14426 C  C     . VAL   B  1  745  ? 13.967  25.211  61.813  1.00 15.36 ? 743  VAL   B C     1 
ATOM   14427 O  O     . VAL   B  1  745  ? 13.146  25.536  60.942  1.00 15.30 ? 743  VAL   B O     1 
ATOM   14428 C  CB    . VAL   B  1  745  ? 16.065  26.636  62.073  1.00 14.94 ? 743  VAL   B CB    1 
ATOM   14429 C  CG1   . VAL   B  1  745  ? 16.004  26.772  60.543  1.00 14.43 ? 743  VAL   B CG1   1 
ATOM   14430 C  CG2   . VAL   B  1  745  ? 16.528  27.930  62.721  1.00 16.72 ? 743  VAL   B CG2   1 
ATOM   14431 N  N     . ARG   B  1  746  ? 14.246  23.930  62.077  1.00 14.79 ? 744  ARG   B N     1 
ATOM   14432 C  CA    . ARG   B  1  746  ? 13.529  22.874  61.365  1.00 15.39 ? 744  ARG   B CA    1 
ATOM   14433 C  C     . ARG   B  1  746  ? 12.033  23.012  61.587  1.00 14.10 ? 744  ARG   B C     1 
ATOM   14434 O  O     . ARG   B  1  746  ? 11.238  22.866  60.654  1.00 15.74 ? 744  ARG   B O     1 
ATOM   14435 C  CB    . ARG   B  1  746  ? 13.939  21.497  61.882  1.00 15.75 ? 744  ARG   B CB    1 
ATOM   14436 C  CG    . ARG   B  1  746  ? 15.327  21.039  61.512  1.00 17.03 ? 744  ARG   B CG    1 
ATOM   14437 C  CD    . ARG   B  1  746  ? 15.530  19.621  62.037  1.00 16.13 ? 744  ARG   B CD    1 
ATOM   14438 N  NE    . ARG   B  1  746  ? 16.929  19.254  61.912  1.00 19.08 ? 744  ARG   B NE    1 
ATOM   14439 C  CZ    . ARG   B  1  746  ? 17.821  19.323  62.886  1.00 17.27 ? 744  ARG   B CZ    1 
ATOM   14440 N  NH1   . ARG   B  1  746  ? 17.463  19.495  64.144  1.00 17.93 ? 744  ARG   B NH1   1 
ATOM   14441 N  NH2   . ARG   B  1  746  ? 19.108  19.231  62.582  1.00 18.84 ? 744  ARG   B NH2   1 
ATOM   14442 N  N     . ILE   B  1  747  ? 11.638  23.290  62.824  1.00 13.47 ? 745  ILE   B N     1 
ATOM   14443 C  CA    . ILE   B  1  747  ? 10.225  23.361  63.136  1.00 13.46 ? 745  ILE   B CA    1 
ATOM   14444 C  C     . ILE   B  1  747  ? 9.600   24.584  62.490  1.00 15.21 ? 745  ILE   B C     1 
ATOM   14445 O  O     . ILE   B  1  747  ? 8.502   24.506  61.931  1.00 14.23 ? 745  ILE   B O     1 
ATOM   14446 C  CB    . ILE   B  1  747  ? 10.037  23.351  64.660  1.00 14.86 ? 745  ILE   B CB    1 
ATOM   14447 C  CG1   . ILE   B  1  747  ? 10.283  21.940  65.178  1.00 16.15 ? 745  ILE   B CG1   1 
ATOM   14448 C  CG2   . ILE   B  1  747  ? 8.625   23.803  65.011  1.00 15.05 ? 745  ILE   B CG2   1 
ATOM   14449 C  CD1   . ILE   B  1  747  ? 10.360  21.850  66.676  1.00 18.55 ? 745  ILE   B CD1   1 
ATOM   14450 N  N     . LEU   B  1  748  ? 10.274  25.733  62.550  1.00 14.91 ? 746  LEU   B N     1 
ATOM   14451 C  CA    . LEU   B  1  748  ? 9.725   26.915  61.893  1.00 15.86 ? 746  LEU   B CA    1 
ATOM   14452 C  C     . LEU   B  1  748  ? 9.604   26.715  60.389  1.00 14.34 ? 746  LEU   B C     1 
ATOM   14453 O  O     . LEU   B  1  748  ? 8.605   27.107  59.782  1.00 14.87 ? 746  LEU   B O     1 
ATOM   14454 C  CB    . LEU   B  1  748  ? 10.561  28.146  62.214  1.00 14.61 ? 746  LEU   B CB    1 
ATOM   14455 C  CG    . LEU   B  1  748  ? 10.219  28.810  63.551  1.00 18.48 ? 746  LEU   B CG    1 
ATOM   14456 C  CD1   . LEU   B  1  748  ? 11.375  29.684  64.020  1.00 19.69 ? 746  LEU   B CD1   1 
ATOM   14457 C  CD2   . LEU   B  1  748  ? 8.958   29.620  63.393  1.00 20.70 ? 746  LEU   B CD2   1 
ATOM   14458 N  N     . ARG   B  1  749  ? 10.613  26.115  59.760  1.00 14.03 ? 747  ARG   B N     1 
ATOM   14459 C  CA    . ARG   B  1  749  ? 10.487  25.841  58.332  1.00 14.55 ? 747  ARG   B CA    1 
ATOM   14460 C  C     . ARG   B  1  749  ? 9.350   24.863  58.065  1.00 14.98 ? 747  ARG   B C     1 
ATOM   14461 O  O     . ARG   B  1  749  ? 8.564   25.047  57.123  1.00 15.16 ? 747  ARG   B O     1 
ATOM   14462 C  CB    . ARG   B  1  749  ? 11.804  25.302  57.795  1.00 15.66 ? 747  ARG   B CB    1 
ATOM   14463 C  CG    . ARG   B  1  749  ? 12.857  26.366  57.625  1.00 16.58 ? 747  ARG   B CG    1 
ATOM   14464 C  CD    . ARG   B  1  749  ? 14.053  25.774  56.950  1.00 17.86 ? 747  ARG   B CD    1 
ATOM   14465 N  NE    . ARG   B  1  749  ? 15.067  26.772  56.663  1.00 17.02 ? 747  ARG   B NE    1 
ATOM   14466 C  CZ    . ARG   B  1  749  ? 16.122  26.531  55.900  1.00 21.87 ? 747  ARG   B CZ    1 
ATOM   14467 N  NH1   . ARG   B  1  749  ? 16.284  25.359  55.304  1.00 23.25 ? 747  ARG   B NH1   1 
ATOM   14468 N  NH2   . ARG   B  1  749  ? 17.027  27.488  55.722  1.00 21.92 ? 747  ARG   B NH2   1 
ATOM   14469 N  N     . GLU   B  1  750  ? 9.227   23.827  58.902  1.00 14.91 ? 748  GLU   B N     1 
ATOM   14470 C  CA    . GLU   B  1  750  ? 8.148   22.866  58.704  1.00 15.90 ? 748  GLU   B CA    1 
ATOM   14471 C  C     . GLU   B  1  750  ? 6.798   23.544  58.824  1.00 14.60 ? 748  GLU   B C     1 
ATOM   14472 O  O     . GLU   B  1  750  ? 5.856   23.193  58.110  1.00 16.56 ? 748  GLU   B O     1 
ATOM   14473 C  CB    . GLU   B  1  750  ? 8.256   21.747  59.733  1.00 15.95 ? 748  GLU   B CB    1 
ATOM   14474 C  CG    . GLU   B  1  750  ? 7.223   20.664  59.522  1.00 18.63 ? 748  GLU   B CG    1 
ATOM   14475 C  CD    . GLU   B  1  750  ? 7.403   19.501  60.465  1.00 18.03 ? 748  GLU   B CD    1 
ATOM   14476 O  OE1   . GLU   B  1  750  ? 8.455   19.437  61.135  1.00 20.20 ? 748  GLU   B OE1   1 
ATOM   14477 O  OE2   . GLU   B  1  750  ? 6.483   18.662  60.537  1.00 22.35 ? 748  GLU   B OE2   1 
ATOM   14478 N  N     . ALA   B  1  751  ? 6.713   24.562  59.672  1.00 15.01 ? 749  ALA   B N     1 
ATOM   14479 C  CA    . ALA   B  1  751  ? 5.474   25.289  59.902  1.00 15.42 ? 749  ALA   B CA    1 
ATOM   14480 C  C     . ALA   B  1  751  ? 5.148   26.273  58.791  1.00 16.78 ? 749  ALA   B C     1 
ATOM   14481 O  O     . ALA   B  1  751  ? 4.063   26.857  58.799  1.00 17.14 ? 749  ALA   B O     1 
ATOM   14482 C  CB    . ALA   B  1  751  ? 5.566   26.024  61.234  1.00 15.89 ? 749  ALA   B CB    1 
ATOM   14483 N  N     . GLY   B  1  752  ? 6.039   26.464  57.827  1.00 15.87 ? 750  GLY   B N     1 
ATOM   14484 C  CA    . GLY   B  1  752  ? 5.748   27.294  56.679  1.00 16.67 ? 750  GLY   B CA    1 
ATOM   14485 C  C     . GLY   B  1  752  ? 6.705   28.437  56.455  1.00 15.73 ? 750  GLY   B C     1 
ATOM   14486 O  O     . GLY   B  1  752  ? 6.535   29.162  55.468  1.00 18.67 ? 750  GLY   B O     1 
ATOM   14487 N  N     . ILE   B  1  753  ? 7.696   28.670  57.314  1.00 15.25 ? 751  ILE   B N     1 
ATOM   14488 C  CA    . ILE   B  1  753  ? 8.640   29.753  57.056  1.00 16.89 ? 751  ILE   B CA    1 
ATOM   14489 C  C     . ILE   B  1  753  ? 9.540   29.324  55.904  1.00 17.64 ? 751  ILE   B C     1 
ATOM   14490 O  O     . ILE   B  1  753  ? 10.207  28.287  56.000  1.00 17.97 ? 751  ILE   B O     1 
ATOM   14491 C  CB    . ILE   B  1  753  ? 9.493   30.066  58.291  1.00 15.15 ? 751  ILE   B CB    1 
ATOM   14492 C  CG1   . ILE   B  1  753  ? 8.612   30.424  59.494  1.00 16.62 ? 751  ILE   B CG1   1 
ATOM   14493 C  CG2   . ILE   B  1  753  ? 10.457  31.173  57.939  1.00 17.26 ? 751  ILE   B CG2   1 
ATOM   14494 C  CD1   . ILE   B  1  753  ? 7.746   31.661  59.261  1.00 16.94 ? 751  ILE   B CD1   1 
ATOM   14495 N  N     . PRO   B  1  754  ? 9.573   30.069  54.801  1.00 16.15 ? 752  PRO   B N     1 
ATOM   14496 C  CA    . PRO   B  1  754  ? 10.393  29.661  53.654  1.00 16.72 ? 752  PRO   B CA    1 
ATOM   14497 C  C     . PRO   B  1  754  ? 11.860  29.594  54.028  1.00 16.80 ? 752  PRO   B C     1 
ATOM   14498 O  O     . PRO   B  1  754  ? 12.339  30.331  54.890  1.00 17.12 ? 752  PRO   B O     1 
ATOM   14499 C  CB    . PRO   B  1  754  ? 10.152  30.777  52.634  1.00 19.81 ? 752  PRO   B CB    1 
ATOM   14500 C  CG    . PRO   B  1  754  ? 8.878   31.423  53.047  1.00 21.92 ? 752  PRO   B CG    1 
ATOM   14501 C  CD    . PRO   B  1  754  ? 8.799   31.292  54.536  1.00 17.07 ? 752  PRO   B CD    1 
ATOM   14502 N  N     . ALA   B  1  755  ? 12.583  28.690  53.361  1.00 18.71 ? 753  ALA   B N     1 
ATOM   14503 C  CA    . ALA   B  1  755  ? 14.001  28.552  53.656  1.00 20.51 ? 753  ALA   B CA    1 
ATOM   14504 C  C     . ALA   B  1  755  ? 14.747  29.858  53.435  1.00 18.09 ? 753  ALA   B C     1 
ATOM   14505 O  O     . ALA   B  1  755  ? 15.684  30.171  54.174  1.00 19.29 ? 753  ALA   B O     1 
ATOM   14506 C  CB    . ALA   B  1  755  ? 14.615  27.426  52.826  1.00 24.06 ? 753  ALA   B CB    1 
ATOM   14507 N  N     . SER   B  1  756  ? 14.338  30.647  52.452  1.00 17.66 ? 754  SER   B N     1 
ATOM   14508 C  CA    . SER   B  1  756  ? 15.011  31.917  52.231  1.00 17.48 ? 754  SER   B CA    1 
ATOM   14509 C  C     . SER   B  1  756  ? 14.696  32.940  53.308  1.00 17.44 ? 754  SER   B C     1 
ATOM   14510 O  O     . SER   B  1  756  ? 15.462  33.894  53.476  1.00 18.42 ? 754  SER   B O     1 
ATOM   14511 C  CB    . SER   B  1  756  ? 14.655  32.466  50.859  1.00 21.06 ? 754  SER   B CB    1 
ATOM   14512 O  OG    . SER   B  1  756  ? 13.258  32.636  50.756  1.00 25.06 ? 754  SER   B OG    1 
ATOM   14513 N  N     . ALA   B  1  757  ? 13.592  32.769  54.040  1.00 15.41 ? 755  ALA   B N     1 
ATOM   14514 C  CA    . ALA   B  1  757  ? 13.253  33.675  55.122  1.00 14.67 ? 755  ALA   B CA    1 
ATOM   14515 C  C     . ALA   B  1  757  ? 13.890  33.291  56.448  1.00 15.18 ? 755  ALA   B C     1 
ATOM   14516 O  O     . ALA   B  1  757  ? 13.858  34.093  57.383  1.00 15.50 ? 755  ALA   B O     1 
ATOM   14517 C  CB    . ALA   B  1  757  ? 11.732  33.754  55.278  1.00 15.60 ? 755  ALA   B CB    1 
ATOM   14518 N  N     . LEU   B  1  758  ? 14.450  32.088  56.565  1.00 16.01 ? 756  LEU   B N     1 
ATOM   14519 C  CA    . LEU   B  1  758  ? 14.996  31.661  57.854  1.00 15.56 ? 756  LEU   B CA    1 
ATOM   14520 C  C     . LEU   B  1  758  ? 16.189  30.755  57.585  1.00 14.74 ? 756  LEU   B C     1 
ATOM   14521 O  O     . LEU   B  1  758  ? 16.031  29.582  57.231  1.00 17.06 ? 756  LEU   B O     1 
ATOM   14522 C  CB    . LEU   B  1  758  ? 13.950  30.967  58.710  1.00 14.92 ? 756  LEU   B CB    1 
ATOM   14523 C  CG    . LEU   B  1  758  ? 14.522  30.432  60.021  1.00 15.11 ? 756  LEU   B CG    1 
ATOM   14524 C  CD1   . LEU   B  1  758  ? 15.141  31.536  60.890  1.00 16.03 ? 756  LEU   B CD1   1 
ATOM   14525 C  CD2   . LEU   B  1  758  ? 13.421  29.717  60.799  1.00 16.02 ? 756  LEU   B CD2   1 
ATOM   14526 N  N     . GLN   B  1  759  ? 17.376  31.309  57.765  1.00 14.67 ? 757  GLN   B N     1 
ATOM   14527 C  CA    . GLN   B  1  759  ? 18.621  30.599  57.558  1.00 15.06 ? 757  GLN   B CA    1 
ATOM   14528 C  C     . GLN   B  1  759  ? 19.324  30.479  58.897  1.00 15.60 ? 757  GLN   B C     1 
ATOM   14529 O  O     . GLN   B  1  759  ? 19.293  31.411  59.706  1.00 17.44 ? 757  GLN   B O     1 
ATOM   14530 C  CB    . GLN   B  1  759  ? 19.477  31.363  56.560  1.00 15.05 ? 757  GLN   B CB    1 
ATOM   14531 C  CG    . GLN   B  1  759  ? 18.886  31.336  55.157  1.00 15.52 ? 757  GLN   B CG    1 
ATOM   14532 C  CD    . GLN   B  1  759  ? 19.643  32.217  54.208  1.00 16.19 ? 757  GLN   B CD    1 
ATOM   14533 O  OE1   . GLN   B  1  759  ? 20.486  31.749  53.443  1.00 17.96 ? 757  GLN   B OE1   1 
ATOM   14534 N  NE2   . GLN   B  1  759  ? 19.359  33.505  54.251  1.00 17.11 ? 757  GLN   B NE2   1 
ATOM   14535 N  N     . LEU   B  1  760  ? 19.901  29.312  59.146  1.00 15.80 ? 758  LEU   B N     1 
ATOM   14536 C  CA    . LEU   B  1  760  ? 20.614  29.034  60.386  1.00 15.20 ? 758  LEU   B CA    1 
ATOM   14537 C  C     . LEU   B  1  760  ? 22.105  29.081  60.104  1.00 17.24 ? 758  LEU   B C     1 
ATOM   14538 O  O     . LEU   B  1  760  ? 22.580  28.391  59.205  1.00 16.71 ? 758  LEU   B O     1 
ATOM   14539 C  CB    . LEU   B  1  760  ? 20.270  27.635  60.892  1.00 15.75 ? 758  LEU   B CB    1 
ATOM   14540 C  CG    . LEU   B  1  760  ? 20.955  27.281  62.207  1.00 15.47 ? 758  LEU   B CG    1 
ATOM   14541 C  CD1   . LEU   B  1  760  ? 20.263  27.968  63.366  1.00 16.88 ? 758  LEU   B CD1   1 
ATOM   14542 C  CD2   . LEU   B  1  760  ? 21.005  25.779  62.405  1.00 17.89 ? 758  LEU   B CD2   1 
ATOM   14543 N  N     . LEU   B  1  761  ? 22.843  29.879  60.879  1.00 15.68 ? 759  LEU   B N     1 
ATOM   14544 C  CA    . LEU   B  1  761  ? 24.289  30.020  60.713  1.00 15.66 ? 759  LEU   B CA    1 
ATOM   14545 C  C     . LEU   B  1  761  ? 24.965  29.675  62.031  1.00 15.88 ? 759  LEU   B C     1 
ATOM   14546 O  O     . LEU   B  1  761  ? 25.253  30.569  62.840  1.00 16.54 ? 759  LEU   B O     1 
ATOM   14547 C  CB    . LEU   B  1  761  ? 24.670  31.432  60.284  1.00 16.88 ? 759  LEU   B CB    1 
ATOM   14548 C  CG    . LEU   B  1  761  ? 24.166  31.974  58.943  1.00 19.48 ? 759  LEU   B CG    1 
ATOM   14549 C  CD1   . LEU   B  1  761  ? 24.248  30.943  57.809  1.00 18.65 ? 759  LEU   B CD1   1 
ATOM   14550 C  CD2   . LEU   B  1  761  ? 22.767  32.531  59.064  1.00 19.53 ? 759  LEU   B CD2   1 
ATOM   14551 N  N     . PRO   B  1  762  ? 25.222  28.403  62.294  1.00 15.26 ? 760  PRO   B N     1 
ATOM   14552 C  CA    . PRO   B  1  762  ? 25.935  28.054  63.524  1.00 15.02 ? 760  PRO   B CA    1 
ATOM   14553 C  C     . PRO   B  1  762  ? 27.348  28.586  63.489  1.00 16.57 ? 760  PRO   B C     1 
ATOM   14554 O  O     . PRO   B  1  762  ? 27.946  28.771  62.424  1.00 16.85 ? 760  PRO   B O     1 
ATOM   14555 C  CB    . PRO   B  1  762  ? 25.941  26.520  63.515  1.00 15.32 ? 760  PRO   B CB    1 
ATOM   14556 C  CG    . PRO   B  1  762  ? 24.882  26.124  62.531  1.00 15.99 ? 760  PRO   B CG    1 
ATOM   14557 C  CD    . PRO   B  1  762  ? 24.895  27.211  61.500  1.00 15.34 ? 760  PRO   B CD    1 
ATOM   14558 N  N     . GLY   B  1  763  ? 27.885  28.806  64.673  1.00 16.33 ? 761  GLY   B N     1 
ATOM   14559 C  CA    . GLY   B  1  763  ? 29.279  29.167  64.817  1.00 15.59 ? 761  GLY   B CA    1 
ATOM   14560 C  C     . GLY   B  1  763  ? 29.445  30.106  65.991  1.00 15.62 ? 761  GLY   B C     1 
ATOM   14561 O  O     . GLY   B  1  763  ? 28.529  30.327  66.779  1.00 16.87 ? 761  GLY   B O     1 
ATOM   14562 N  N     . ASP   B  1  764  ? 30.653  30.636  66.107  1.00 19.03 ? 762  ASP   B N     1 
ATOM   14563 C  CA    . ASP   B  1  764  ? 30.976  31.445  67.270  1.00 18.43 ? 762  ASP   B CA    1 
ATOM   14564 C  C     . ASP   B  1  764  ? 30.733  32.920  66.961  1.00 19.59 ? 762  ASP   B C     1 
ATOM   14565 O  O     . ASP   B  1  764  ? 30.009  33.274  66.022  1.00 18.54 ? 762  ASP   B O     1 
ATOM   14566 C  CB    . ASP   B  1  764  ? 32.382  31.117  67.786  1.00 19.88 ? 762  ASP   B CB    1 
ATOM   14567 C  CG    . ASP   B  1  764  ? 33.486  31.517  66.814  1.00 24.47 ? 762  ASP   B CG    1 
ATOM   14568 O  OD1   . ASP   B  1  764  ? 33.239  32.236  65.826  1.00 20.73 ? 762  ASP   B OD1   1 
ATOM   14569 O  OD2   . ASP   B  1  764  ? 34.641  31.096  67.048  1.00 31.46 ? 762  ASP   B OD2   1 
ATOM   14570 N  N     . GLY   B  1  765  ? 31.330  33.798  67.763  1.00 18.90 ? 763  GLY   B N     1 
ATOM   14571 C  CA    . GLY   B  1  765  ? 31.063  35.211  67.617  1.00 17.22 ? 763  GLY   B CA    1 
ATOM   14572 C  C     . GLY   B  1  765  ? 31.549  35.791  66.311  1.00 19.08 ? 763  GLY   B C     1 
ATOM   14573 O  O     . GLY   B  1  765  ? 31.052  36.837  65.888  1.00 19.64 ? 763  GLY   B O     1 
ATOM   14574 N  N     . ARG   B  1  766  ? 32.515  35.139  65.661  1.00 18.13 ? 764  ARG   B N     1 
ATOM   14575 C  CA    . ARG   B  1  766  ? 32.966  35.622  64.361  1.00 19.36 ? 764  ARG   B CA    1 
ATOM   14576 C  C     . ARG   B  1  766  ? 31.867  35.497  63.323  1.00 19.16 ? 764  ARG   B C     1 
ATOM   14577 O  O     . ARG   B  1  766  ? 31.766  36.334  62.419  1.00 18.95 ? 764  ARG   B O     1 
ATOM   14578 C  CB    . ARG   B  1  766  ? 34.187  34.836  63.894  1.00 20.53 ? 764  ARG   B CB    1 
ATOM   14579 C  CG    . ARG   B  1  766  ? 35.363  34.878  64.849  1.00 23.96 ? 764  ARG   B CG    1 
ATOM   14580 C  CD    . ARG   B  1  766  ? 36.410  33.845  64.442  1.00 30.89 ? 764  ARG   B CD    1 
ATOM   14581 N  NE    . ARG   B  1  766  ? 35.895  32.487  64.582  1.00 32.76 ? 764  ARG   B NE    1 
ATOM   14582 C  CZ    . ARG   B  1  766  ? 36.525  31.398  64.161  1.00 39.27 ? 764  ARG   B CZ    1 
ATOM   14583 N  NH1   . ARG   B  1  766  ? 37.697  31.471  63.552  1.00 39.87 ? 764  ARG   B NH1   1 
ATOM   14584 N  NH2   . ARG   B  1  766  ? 35.963  30.208  64.353  1.00 42.52 ? 764  ARG   B NH2   1 
ATOM   14585 N  N     . VAL   B  1  767  ? 31.034  34.467  63.449  1.00 17.78 ? 765  VAL   B N     1 
ATOM   14586 C  CA    . VAL   B  1  767  ? 29.899  34.325  62.553  1.00 18.41 ? 765  VAL   B CA    1 
ATOM   14587 C  C     . VAL   B  1  767  ? 28.875  35.408  62.843  1.00 17.86 ? 765  VAL   B C     1 
ATOM   14588 O  O     . VAL   B  1  767  ? 28.345  36.044  61.925  1.00 17.23 ? 765  VAL   B O     1 
ATOM   14589 C  CB    . VAL   B  1  767  ? 29.313  32.909  62.673  1.00 16.15 ? 765  VAL   B CB    1 
ATOM   14590 C  CG1   . VAL   B  1  767  ? 28.121  32.772  61.754  1.00 17.58 ? 765  VAL   B CG1   1 
ATOM   14591 C  CG2   . VAL   B  1  767  ? 30.363  31.870  62.326  1.00 20.18 ? 765  VAL   B CG2   1 
ATOM   14592 N  N     . GLY   B  1  768  ? 28.595  35.655  64.124  1.00 15.93 ? 766  GLY   B N     1 
ATOM   14593 C  CA    . GLY   B  1  768  ? 27.713  36.759  64.458  1.00 17.65 ? 766  GLY   B CA    1 
ATOM   14594 C  C     . GLY   B  1  768  ? 28.234  38.077  63.918  1.00 15.94 ? 766  GLY   B C     1 
ATOM   14595 O  O     . GLY   B  1  768  ? 27.487  38.868  63.337  1.00 17.05 ? 766  GLY   B O     1 
ATOM   14596 N  N     . ALA   B  1  769  ? 29.536  38.320  64.082  1.00 17.43 ? 767  ALA   B N     1 
ATOM   14597 C  CA    . ALA   B  1  769  ? 30.091  39.592  63.632  1.00 17.70 ? 767  ALA   B CA    1 
ATOM   14598 C  C     . ALA   B  1  769  ? 30.000  39.724  62.117  1.00 18.07 ? 767  ALA   B C     1 
ATOM   14599 O  O     . ALA   B  1  769  ? 29.700  40.807  61.599  1.00 18.90 ? 767  ALA   B O     1 
ATOM   14600 C  CB    . ALA   B  1  769  ? 31.539  39.720  64.109  1.00 18.48 ? 767  ALA   B CB    1 
ATOM   14601 N  N     . ALA   B  1  770  ? 30.232  38.628  61.392  1.00 16.55 ? 768  ALA   B N     1 
ATOM   14602 C  CA    . ALA   B  1  770  ? 30.155  38.681  59.937  1.00 17.34 ? 768  ALA   B CA    1 
ATOM   14603 C  C     . ALA   B  1  770  ? 28.736  38.992  59.482  1.00 17.26 ? 768  ALA   B C     1 
ATOM   14604 O  O     . ALA   B  1  770  ? 28.533  39.726  58.507  1.00 19.30 ? 768  ALA   B O     1 
ATOM   14605 C  CB    . ALA   B  1  770  ? 30.616  37.360  59.334  1.00 17.46 ? 768  ALA   B CB    1 
ATOM   14606 N  N     . LEU   B  1  771  ? 27.740  38.437  60.173  1.00 16.15 ? 769  LEU   B N     1 
ATOM   14607 C  CA    . LEU   B  1  771  ? 26.355  38.731  59.829  1.00 17.37 ? 769  LEU   B CA    1 
ATOM   14608 C  C     . LEU   B  1  771  ? 26.030  40.189  60.111  1.00 17.53 ? 769  LEU   B C     1 
ATOM   14609 O  O     . LEU   B  1  771  ? 25.402  40.865  59.289  1.00 18.81 ? 769  LEU   B O     1 
ATOM   14610 C  CB    . LEU   B  1  771  ? 25.425  37.816  60.625  1.00 16.38 ? 769  LEU   B CB    1 
ATOM   14611 C  CG    . LEU   B  1  771  ? 25.482  36.348  60.203  1.00 16.72 ? 769  LEU   B CG    1 
ATOM   14612 C  CD1   . LEU   B  1  771  ? 24.757  35.501  61.230  1.00 17.46 ? 769  LEU   B CD1   1 
ATOM   14613 C  CD2   . LEU   B  1  771  ? 24.898  36.143  58.795  1.00 17.38 ? 769  LEU   B CD2   1 
ATOM   14614 N  N     . VAL   B  1  772  ? 26.441  40.684  61.280  1.00 16.30 ? 770  VAL   B N     1 
ATOM   14615 C  CA    . VAL   B  1  772  ? 26.138  42.059  61.672  1.00 16.08 ? 770  VAL   B CA    1 
ATOM   14616 C  C     . VAL   B  1  772  ? 26.733  43.047  60.682  1.00 19.89 ? 770  VAL   B C     1 
ATOM   14617 O  O     . VAL   B  1  772  ? 26.109  44.063  60.342  1.00 20.17 ? 770  VAL   B O     1 
ATOM   14618 C  CB    . VAL   B  1  772  ? 26.663  42.318  63.092  1.00 17.74 ? 770  VAL   B CB    1 
ATOM   14619 C  CG1   . VAL   B  1  772  ? 26.694  43.812  63.381  1.00 19.39 ? 770  VAL   B CG1   1 
ATOM   14620 C  CG2   . VAL   B  1  772  ? 25.821  41.572  64.109  1.00 18.82 ? 770  VAL   B CG2   1 
ATOM   14621 N  N     . ALA   B  1  773  ? 27.952  42.773  60.216  1.00 19.33 ? 771  ALA   B N     1 
ATOM   14622 C  CA    . ALA   B  1  773  ? 28.643  43.698  59.332  1.00 20.33 ? 771  ALA   B CA    1 
ATOM   14623 C  C     . ALA   B  1  773  ? 28.168  43.630  57.893  1.00 23.85 ? 771  ALA   B C     1 
ATOM   14624 O  O     . ALA   B  1  773  ? 28.535  44.508  57.102  1.00 24.13 ? 771  ALA   B O     1 
ATOM   14625 C  CB    . ALA   B  1  773  ? 30.140  43.408  59.354  1.00 20.66 ? 771  ALA   B CB    1 
ATOM   14626 N  N     . ALA   B  1  774  ? 27.392  42.614  57.531  1.00 18.75 ? 772  ALA   B N     1 
ATOM   14627 C  CA    . ALA   B  1  774  ? 27.023  42.414  56.136  1.00 20.51 ? 772  ALA   B CA    1 
ATOM   14628 C  C     . ALA   B  1  774  ? 26.188  43.577  55.623  1.00 21.91 ? 772  ALA   B C     1 
ATOM   14629 O  O     . ALA   B  1  774  ? 25.366  44.155  56.339  1.00 21.43 ? 772  ALA   B O     1 
ATOM   14630 C  CB    . ALA   B  1  774  ? 26.257  41.101  55.962  1.00 22.57 ? 772  ALA   B CB    1 
ATOM   14631 N  N     . ALA   B  1  775  ? 26.395  43.898  54.345  1.00 24.53 ? 773  ALA   B N     1 
ATOM   14632 C  CA    . ALA   B  1  775  ? 25.865  45.134  53.786  1.00 24.24 ? 773  ALA   B CA    1 
ATOM   14633 C  C     . ALA   B  1  775  ? 24.344  45.196  53.871  1.00 21.88 ? 773  ALA   B C     1 
ATOM   14634 O  O     . ALA   B  1  775  ? 23.773  46.266  54.106  1.00 24.74 ? 773  ALA   B O     1 
ATOM   14635 C  CB    . ALA   B  1  775  ? 26.321  45.261  52.333  1.00 26.66 ? 773  ALA   B CB    1 
ATOM   14636 N  N     . GLU   B  1  776  ? 23.673  44.069  53.677  1.00 21.32 ? 774  GLU   B N     1 
ATOM   14637 C  CA    . GLU   B  1  776  ? 22.222  44.064  53.591  1.00 19.97 ? 774  GLU   B CA    1 
ATOM   14638 C  C     . GLU   B  1  776  ? 21.524  43.864  54.932  1.00 18.48 ? 774  GLU   B C     1 
ATOM   14639 O  O     . GLU   B  1  776  ? 20.294  43.880  54.971  1.00 19.46 ? 774  GLU   B O     1 
ATOM   14640 C  CB    . GLU   B  1  776  ? 21.749  43.001  52.599  1.00 19.47 ? 774  GLU   B CB    1 
ATOM   14641 C  CG    . GLU   B  1  776  ? 22.320  43.151  51.190  1.00 24.59 ? 774  GLU   B CG    1 
ATOM   14642 C  CD    . GLU   B  1  776  ? 23.652  42.431  50.991  1.00 31.81 ? 774  GLU   B CD    1 
ATOM   14643 O  OE1   . GLU   B  1  776  ? 24.231  41.876  51.965  1.00 26.22 ? 774  GLU   B OE1   1 
ATOM   14644 O  OE2   . GLU   B  1  776  ? 24.136  42.426  49.837  1.00 35.34 ? 774  GLU   B OE2   1 
ATOM   14645 N  N     . THR   B  1  777  ? 22.262  43.671  56.017  1.00 17.25 ? 775  THR   B N     1 
ATOM   14646 C  CA    . THR   B  1  777  ? 21.639  43.543  57.325  1.00 16.75 ? 775  THR   B CA    1 
ATOM   14647 C  C     . THR   B  1  777  ? 20.926  44.833  57.685  1.00 16.88 ? 775  THR   B C     1 
ATOM   14648 O  O     . THR   B  1  777  ? 21.526  45.912  57.674  1.00 18.97 ? 775  THR   B O     1 
ATOM   14649 C  CB    . THR   B  1  777  ? 22.731  43.222  58.333  1.00 18.49 ? 775  THR   B CB    1 
ATOM   14650 O  OG1   . THR   B  1  777  ? 23.227  41.914  58.034  1.00 19.67 ? 775  THR   B OG1   1 
ATOM   14651 C  CG2   . THR   B  1  777  ? 22.174  43.265  59.750  1.00 16.88 ? 775  THR   B CG2   1 
ATOM   14652 N  N     . ALA   B  1  778  ? 19.626  44.715  57.976  1.00 14.69 ? 776  ALA   B N     1 
ATOM   14653 C  CA    . ALA   B  1  778  ? 18.769  45.860  58.214  1.00 15.89 ? 776  ALA   B CA    1 
ATOM   14654 C  C     . ALA   B  1  778  ? 18.373  46.009  59.669  1.00 15.77 ? 776  ALA   B C     1 
ATOM   14655 O  O     . ALA   B  1  778  ? 17.725  47.000  60.022  1.00 17.61 ? 776  ALA   B O     1 
ATOM   14656 C  CB    . ALA   B  1  778  ? 17.493  45.735  57.371  1.00 16.08 ? 776  ALA   B CB    1 
ATOM   14657 N  N     . GLY   B  1  779  ? 18.715  45.045  60.507  1.00 14.72 ? 777  GLY   B N     1 
ATOM   14658 C  CA    . GLY   B  1  779  ? 18.452  45.165  61.926  1.00 15.85 ? 777  GLY   B CA    1 
ATOM   14659 C  C     . GLY   B  1  779  ? 19.104  43.998  62.620  1.00 15.19 ? 777  GLY   B C     1 
ATOM   14660 O  O     . GLY   B  1  779  ? 19.393  42.969  62.004  1.00 15.75 ? 777  GLY   B O     1 
ATOM   14661 N  N     . VAL   B  1  780  ? 19.351  44.176  63.911  1.00 14.67 ? 778  VAL   B N     1 
ATOM   14662 C  CA    . VAL   B  1  780  ? 19.993  43.140  64.697  1.00 14.50 ? 778  VAL   B CA    1 
ATOM   14663 C  C     . VAL   B  1  780  ? 19.219  42.976  65.987  1.00 13.75 ? 778  VAL   B C     1 
ATOM   14664 O  O     . VAL   B  1  780  ? 18.909  43.965  66.660  1.00 14.36 ? 778  VAL   B O     1 
ATOM   14665 C  CB    . VAL   B  1  780  ? 21.473  43.456  64.984  1.00 15.08 ? 778  VAL   B CB    1 
ATOM   14666 C  CG1   . VAL   B  1  780  ? 22.063  42.372  65.869  1.00 16.66 ? 778  VAL   B CG1   1 
ATOM   14667 C  CG2   . VAL   B  1  780  ? 22.250  43.553  63.676  1.00 15.34 ? 778  VAL   B CG2   1 
ATOM   14668 N  N     . MET   B  1  781  ? 18.924  41.736  66.328  1.00 13.90 ? 779  MET   B N     1 
ATOM   14669 C  CA    . MET   B  1  781  ? 18.333  41.395  67.614  1.00 13.87 ? 779  MET   B CA    1 
ATOM   14670 C  C     . MET   B  1  781  ? 19.377  40.578  68.342  1.00 15.00 ? 779  MET   B C     1 
ATOM   14671 O  O     . MET   B  1  781  ? 19.756  39.496  67.883  1.00 14.94 ? 779  MET   B O     1 
ATOM   14672 C  CB    . MET   B  1  781  ? 17.050  40.599  67.425  1.00 14.88 ? 779  MET   B CB    1 
ATOM   14673 C  CG    . MET   B  1  781  ? 16.078  41.338  66.533  1.00 15.33 ? 779  MET   B CG    1 
ATOM   14674 S  SD    . MET   B  1  781  ? 14.605  40.400  66.184  1.00 14.81 ? 779  MET   B SD    1 
ATOM   14675 C  CE    . MET   B  1  781  ? 13.774  40.504  67.753  1.00 16.03 ? 779  MET   B CE    1 
ATOM   14676 N  N     . PHE   B  1  782  ? 19.882  41.119  69.436  1.00 14.92 ? 780  PHE   B N     1 
ATOM   14677 C  CA    . PHE   B  1  782  ? 20.952  40.494  70.178  1.00 14.92 ? 780  PHE   B CA    1 
ATOM   14678 C  C     . PHE   B  1  782  ? 20.490  40.278  71.604  1.00 13.40 ? 780  PHE   B C     1 
ATOM   14679 O  O     . PHE   B  1  782  ? 19.957  41.192  72.232  1.00 14.49 ? 780  PHE   B O     1 
ATOM   14680 C  CB    . PHE   B  1  782  ? 22.176  41.403  70.227  1.00 13.59 ? 780  PHE   B CB    1 
ATOM   14681 C  CG    . PHE   B  1  782  ? 23.256  40.875  71.098  1.00 13.59 ? 780  PHE   B CG    1 
ATOM   14682 C  CD1   . PHE   B  1  782  ? 24.037  39.822  70.660  1.00 15.60 ? 780  PHE   B CD1   1 
ATOM   14683 C  CD2   . PHE   B  1  782  ? 23.455  41.385  72.375  1.00 14.35 ? 780  PHE   B CD2   1 
ATOM   14684 C  CE1   . PHE   B  1  782  ? 25.029  39.311  71.456  1.00 15.79 ? 780  PHE   B CE1   1 
ATOM   14685 C  CE2   . PHE   B  1  782  ? 24.452  40.863  73.188  1.00 16.32 ? 780  PHE   B CE2   1 
ATOM   14686 C  CZ    . PHE   B  1  782  ? 25.239  39.844  72.725  1.00 15.99 ? 780  PHE   B CZ    1 
ATOM   14687 N  N     . THR   B  1  783  ? 20.735  39.083  72.114  1.00 13.69 ? 781  THR   B N     1 
ATOM   14688 C  CA    . THR   B  1  783  ? 20.634  38.825  73.537  1.00 14.70 ? 781  THR   B CA    1 
ATOM   14689 C  C     . THR   B  1  783  ? 21.908  38.119  73.949  1.00 14.82 ? 781  THR   B C     1 
ATOM   14690 O  O     . THR   B  1  783  ? 22.319  37.145  73.311  1.00 14.74 ? 781  THR   B O     1 
ATOM   14691 C  CB    . THR   B  1  783  ? 19.404  37.978  73.852  1.00 14.47 ? 781  THR   B CB    1 
ATOM   14692 O  OG1   . THR   B  1  783  ? 18.231  38.651  73.392  1.00 15.20 ? 781  THR   B OG1   1 
ATOM   14693 C  CG2   . THR   B  1  783  ? 19.275  37.797  75.355  1.00 14.71 ? 781  THR   B CG2   1 
ATOM   14694 N  N     . GLY   B  1  784  ? 22.555  38.632  74.990  1.00 15.28 ? 782  GLY   B N     1 
ATOM   14695 C  CA    . GLY   B  1  784  ? 23.846  38.112  75.384  1.00 15.24 ? 782  GLY   B CA    1 
ATOM   14696 C  C     . GLY   B  1  784  ? 24.518  39.088  76.321  1.00 17.25 ? 782  GLY   B C     1 
ATOM   14697 O  O     . GLY   B  1  784  ? 23.858  39.916  76.941  1.00 16.65 ? 782  GLY   B O     1 
ATOM   14698 N  N     . SER   B  1  785  ? 25.830  38.988  76.401  1.00 17.20 ? 783  SER   B N     1 
ATOM   14699 C  CA    . SER   B  1  785  ? 26.547  39.839  77.337  1.00 17.96 ? 783  SER   B CA    1 
ATOM   14700 C  C     . SER   B  1  785  ? 26.575  41.286  76.865  1.00 17.14 ? 783  SER   B C     1 
ATOM   14701 O  O     . SER   B  1  785  ? 26.595  41.583  75.666  1.00 18.24 ? 783  SER   B O     1 
ATOM   14702 C  CB    . SER   B  1  785  ? 27.973  39.335  77.522  1.00 18.69 ? 783  SER   B CB    1 
ATOM   14703 O  OG    . SER   B  1  785  ? 28.704  39.398  76.312  1.00 19.10 ? 783  SER   B OG    1 
ATOM   14704 N  N     . THR   B  1  786  ? 26.644  42.201  77.837  1.00 19.83 ? 784  THR   B N     1 
ATOM   14705 C  CA    . THR   B  1  786  ? 26.749  43.614  77.504  1.00 19.54 ? 784  THR   B CA    1 
ATOM   14706 C  C     . THR   B  1  786  ? 28.011  43.889  76.696  1.00 19.05 ? 784  THR   B C     1 
ATOM   14707 O  O     . THR   B  1  786  ? 28.005  44.721  75.782  1.00 20.85 ? 784  THR   B O     1 
ATOM   14708 C  CB    . THR   B  1  786  ? 26.698  44.452  78.788  1.00 19.29 ? 784  THR   B CB    1 
ATOM   14709 O  OG1   . THR   B  1  786  ? 25.535  44.088  79.542  1.00 21.24 ? 784  THR   B OG1   1 
ATOM   14710 C  CG2   . THR   B  1  786  ? 26.627  45.927  78.446  1.00 22.75 ? 784  THR   B CG2   1 
ATOM   14711 N  N     . GLU   B  1  787  ? 29.104  43.191  77.017  1.00 21.06 ? 785  GLU   B N     1 
ATOM   14712 C  CA    . GLU   B  1  787  ? 30.367  43.405  76.319  1.00 19.53 ? 785  GLU   B CA    1 
ATOM   14713 C  C     . GLU   B  1  787  ? 30.227  43.118  74.829  1.00 19.63 ? 785  GLU   B C     1 
ATOM   14714 O  O     . GLU   B  1  787  ? 30.702  43.893  73.986  1.00 20.59 ? 785  GLU   B O     1 
ATOM   14715 C  CB    . GLU   B  1  787  ? 31.456  42.520  76.936  1.00 24.49 ? 785  GLU   B CB    1 
ATOM   14716 N  N     . VAL   B  1  788  ? 29.573  42.003  74.484  1.00 18.11 ? 786  VAL   B N     1 
ATOM   14717 C  CA    . VAL   B  1  788  ? 29.400  41.661  73.075  1.00 18.32 ? 786  VAL   B CA    1 
ATOM   14718 C  C     . VAL   B  1  788  ? 28.433  42.634  72.407  1.00 16.06 ? 786  VAL   B C     1 
ATOM   14719 O  O     . VAL   B  1  788  ? 28.632  43.046  71.256  1.00 17.71 ? 786  VAL   B O     1 
ATOM   14720 C  CB    . VAL   B  1  788  ? 28.942  40.195  72.946  1.00 19.06 ? 786  VAL   B CB    1 
ATOM   14721 C  CG1   . VAL   B  1  788  ? 28.492  39.895  71.526  1.00 18.94 ? 786  VAL   B CG1   1 
ATOM   14722 C  CG2   . VAL   B  1  788  ? 30.082  39.248  73.344  1.00 19.72 ? 786  VAL   B CG2   1 
ATOM   14723 N  N     . ALA   B  1  789  ? 27.391  43.048  73.135  1.00 16.76 ? 787  ALA   B N     1 
ATOM   14724 C  CA    . ALA   B  1  789  ? 26.436  43.990  72.571  1.00 15.55 ? 787  ALA   B CA    1 
ATOM   14725 C  C     . ALA   B  1  789  ? 27.128  45.272  72.147  1.00 17.04 ? 787  ALA   B C     1 
ATOM   14726 O  O     . ALA   B  1  789  ? 26.805  45.843  71.106  1.00 17.84 ? 787  ALA   B O     1 
ATOM   14727 C  CB    . ALA   B  1  789  ? 25.329  44.298  73.577  1.00 15.72 ? 787  ALA   B CB    1 
ATOM   14728 N  N     . ARG   B  1  790  ? 28.096  45.738  72.941  1.00 17.38 ? 788  ARG   B N     1 
ATOM   14729 C  CA    . ARG   B  1  790  ? 28.799  46.963  72.576  1.00 17.88 ? 788  ARG   B CA    1 
ATOM   14730 C  C     . ARG   B  1  790  ? 29.580  46.794  71.287  1.00 19.46 ? 788  ARG   B C     1 
ATOM   14731 O  O     . ARG   B  1  790  ? 29.716  47.744  70.512  1.00 21.70 ? 788  ARG   B O     1 
ATOM   14732 C  CB    . ARG   B  1  790  ? 29.806  47.327  73.653  1.00 21.25 ? 788  ARG   B CB    1 
ATOM   14733 C  CG    . ARG   B  1  790  ? 29.234  47.744  74.924  1.00 23.28 ? 788  ARG   B CG    1 
ATOM   14734 C  CD    . ARG   B  1  790  ? 30.352  48.343  75.759  1.00 29.61 ? 788  ARG   B CD    1 
ATOM   14735 N  NE    . ARG   B  1  790  ? 29.846  48.612  77.090  1.00 33.49 ? 788  ARG   B NE    1 
ATOM   14736 C  CZ    . ARG   B  1  790  ? 29.051  49.628  77.388  1.00 32.97 ? 788  ARG   B CZ    1 
ATOM   14737 N  NH1   . ARG   B  1  790  ? 28.718  50.539  76.480  1.00 29.11 ? 788  ARG   B NH1   1 
ATOM   14738 N  NH2   . ARG   B  1  790  ? 28.570  49.728  78.622  1.00 37.88 ? 788  ARG   B NH2   1 
ATOM   14739 N  N     . LEU   B  1  791  ? 30.140  45.607  71.061  1.00 18.79 ? 789  LEU   B N     1 
ATOM   14740 C  CA    . LEU   B  1  791  ? 30.873  45.374  69.819  1.00 20.19 ? 789  LEU   B CA    1 
ATOM   14741 C  C     . LEU   B  1  791  ? 29.937  45.431  68.624  1.00 19.54 ? 789  LEU   B C     1 
ATOM   14742 O  O     . LEU   B  1  791  ? 30.252  46.045  67.600  1.00 21.01 ? 789  LEU   B O     1 
ATOM   14743 C  CB    . LEU   B  1  791  ? 31.577  44.020  69.868  1.00 20.76 ? 789  LEU   B CB    1 
ATOM   14744 C  CG    . LEU   B  1  791  ? 32.587  43.815  70.992  1.00 22.02 ? 789  LEU   B CG    1 
ATOM   14745 C  CD1   . LEU   B  1  791  ? 33.178  42.416  70.906  1.00 22.87 ? 789  LEU   B CD1   1 
ATOM   14746 C  CD2   . LEU   B  1  791  ? 33.677  44.877  70.905  1.00 24.41 ? 789  LEU   B CD2   1 
ATOM   14747 N  N     . ILE   B  1  792  ? 28.755  44.825  68.760  1.00 18.79 ? 790  ILE   B N     1 
ATOM   14748 C  CA    . ILE   B  1  792  ? 27.769  44.857  67.690  1.00 19.22 ? 790  ILE   B CA    1 
ATOM   14749 C  C     . ILE   B  1  792  ? 27.303  46.279  67.447  1.00 17.88 ? 790  ILE   B C     1 
ATOM   14750 O  O     . ILE   B  1  792  ? 27.176  46.724  66.298  1.00 19.41 ? 790  ILE   B O     1 
ATOM   14751 C  CB    . ILE   B  1  792  ? 26.605  43.940  68.080  1.00 16.34 ? 790  ILE   B CB    1 
ATOM   14752 C  CG1   . ILE   B  1  792  ? 27.080  42.497  68.072  1.00 16.78 ? 790  ILE   B CG1   1 
ATOM   14753 C  CG2   . ILE   B  1  792  ? 25.403  44.167  67.165  1.00 16.82 ? 790  ILE   B CG2   1 
ATOM   14754 C  CD1   . ILE   B  1  792  ? 26.107  41.521  68.641  1.00 17.53 ? 790  ILE   B CD1   1 
ATOM   14755 N  N     . GLN   B  1  793  ? 27.031  47.006  68.529  1.00 17.70 ? 791  GLN   B N     1 
ATOM   14756 C  CA    . GLN   B  1  793  ? 26.606  48.390  68.424  1.00 19.60 ? 791  GLN   B CA    1 
ATOM   14757 C  C     . GLN   B  1  793  ? 27.626  49.215  67.662  1.00 20.53 ? 791  GLN   B C     1 
ATOM   14758 O  O     . GLN   B  1  793  ? 27.261  50.030  66.808  1.00 19.77 ? 791  GLN   B O     1 
ATOM   14759 C  CB    . GLN   B  1  793  ? 26.408  48.947  69.828  1.00 19.81 ? 791  GLN   B CB    1 
ATOM   14760 C  CG    . GLN   B  1  793  ? 26.041  50.390  69.880  1.00 21.31 ? 791  GLN   B CG    1 
ATOM   14761 C  CD    . GLN   B  1  793  ? 26.314  50.970  71.241  1.00 23.90 ? 791  GLN   B CD    1 
ATOM   14762 O  OE1   . GLN   B  1  793  ? 27.350  50.690  71.852  1.00 24.91 ? 791  GLN   B OE1   1 
ATOM   14763 N  NE2   . GLN   B  1  793  ? 25.384  51.764  71.740  1.00 27.35 ? 791  GLN   B NE2   1 
ATOM   14764 N  N     . ALA   B  1  794  ? 28.911  48.996  67.942  1.00 19.80 ? 792  ALA   B N     1 
ATOM   14765 C  CA    . ALA   B  1  794  ? 29.949  49.724  67.225  1.00 20.39 ? 792  ALA   B CA    1 
ATOM   14766 C  C     . ALA   B  1  794  ? 29.964  49.366  65.742  1.00 21.00 ? 792  ALA   B C     1 
ATOM   14767 O  O     . ALA   B  1  794  ? 30.096  50.258  64.891  1.00 23.47 ? 792  ALA   B O     1 
ATOM   14768 C  CB    . ALA   B  1  794  ? 31.310  49.482  67.877  1.00 23.80 ? 792  ALA   B CB    1 
ATOM   14769 N  N     . GLN   B  1  795  ? 29.838  48.075  65.406  1.00 20.07 ? 793  GLN   B N     1 
ATOM   14770 C  CA    . GLN   B  1  795  ? 29.787  47.688  63.994  1.00 20.25 ? 793  GLN   B CA    1 
ATOM   14771 C  C     . GLN   B  1  795  ? 28.642  48.400  63.289  1.00 21.75 ? 793  GLN   B C     1 
ATOM   14772 O  O     . GLN   B  1  795  ? 28.789  48.903  62.168  1.00 21.60 ? 793  GLN   B O     1 
ATOM   14773 C  CB    . GLN   B  1  795  ? 29.561  46.176  63.845  1.00 25.36 ? 793  GLN   B CB    1 
ATOM   14774 C  CG    . GLN   B  1  795  ? 30.684  45.224  64.190  1.00 27.47 ? 793  GLN   B CG    1 
ATOM   14775 C  CD    . GLN   B  1  795  ? 30.274  43.758  63.958  1.00 31.49 ? 793  GLN   B CD    1 
ATOM   14776 O  OE1   . GLN   B  1  795  ? 29.676  43.123  64.829  1.00 31.95 ? 793  GLN   B OE1   1 
ATOM   14777 N  NE2   . GLN   B  1  795  ? 30.590  43.228  62.786  1.00 27.40 ? 793  GLN   B NE2   1 
ATOM   14778 N  N     . LEU   B  1  796  ? 27.476  48.433  63.929  1.00 19.06 ? 794  LEU   B N     1 
ATOM   14779 C  CA    . LEU   B  1  796  ? 26.293  48.948  63.254  1.00 18.49 ? 794  LEU   B CA    1 
ATOM   14780 C  C     . LEU   B  1  796  ? 26.367  50.448  63.051  1.00 20.99 ? 794  LEU   B C     1 
ATOM   14781 O  O     . LEU   B  1  796  ? 25.832  50.963  62.064  1.00 23.19 ? 794  LEU   B O     1 
ATOM   14782 C  CB    . LEU   B  1  796  ? 25.044  48.613  64.064  1.00 18.61 ? 794  LEU   B CB    1 
ATOM   14783 C  CG    . LEU   B  1  796  ? 24.652  47.141  64.050  1.00 19.30 ? 794  LEU   B CG    1 
ATOM   14784 C  CD1   . LEU   B  1  796  ? 23.409  46.978  64.892  1.00 19.12 ? 794  LEU   B CD1   1 
ATOM   14785 C  CD2   . LEU   B  1  796  ? 24.366  46.728  62.624  1.00 19.43 ? 794  LEU   B CD2   1 
ATOM   14786 N  N     . ALA   B  1  797  ? 27.009  51.164  63.976  1.00 21.28 ? 795  ALA   B N     1 
ATOM   14787 C  CA    . ALA   B  1  797  ? 27.066  52.615  63.876  1.00 23.77 ? 795  ALA   B CA    1 
ATOM   14788 C  C     . ALA   B  1  797  ? 27.889  53.069  62.684  1.00 25.89 ? 795  ALA   B C     1 
ATOM   14789 O  O     . ALA   B  1  797  ? 27.764  54.220  62.263  1.00 28.02 ? 795  ALA   B O     1 
ATOM   14790 C  CB    . ALA   B  1  797  ? 27.626  53.214  65.165  1.00 25.24 ? 795  ALA   B CB    1 
ATOM   14791 N  N     . ASP   B  1  798  ? 28.718  52.192  62.124  1.00 25.43 ? 796  ASP   B N     1 
ATOM   14792 C  CA    . ASP   B  1  798  ? 29.431  52.544  60.904  1.00 29.12 ? 796  ASP   B CA    1 
ATOM   14793 C  C     . ASP   B  1  798  ? 28.513  52.576  59.692  1.00 29.33 ? 796  ASP   B C     1 
ATOM   14794 O  O     . ASP   B  1  798  ? 28.885  53.155  58.667  1.00 31.64 ? 796  ASP   B O     1 
ATOM   14795 C  CB    . ASP   B  1  798  ? 30.552  51.543  60.650  1.00 24.52 ? 796  ASP   B CB    1 
ATOM   14796 N  N     . ARG   B  1  799  ? 27.330  51.973  59.782  1.00 25.67 ? 797  ARG   B N     1 
ATOM   14797 C  CA    . ARG   B  1  799  ? 26.458  51.767  58.639  1.00 30.04 ? 797  ARG   B CA    1 
ATOM   14798 C  C     . ARG   B  1  799  ? 25.183  52.582  58.786  1.00 28.20 ? 797  ARG   B C     1 
ATOM   14799 O  O     . ARG   B  1  799  ? 24.810  53.018  59.877  1.00 22.57 ? 797  ARG   B O     1 
ATOM   14800 C  CB    . ARG   B  1  799  ? 26.075  50.285  58.497  1.00 29.90 ? 797  ARG   B CB    1 
ATOM   14801 C  CG    . ARG   B  1  799  ? 27.259  49.331  58.360  1.00 36.15 ? 797  ARG   B CG    1 
ATOM   14802 C  CD    . ARG   B  1  799  ? 26.882  48.027  57.644  1.00 34.42 ? 797  ARG   B CD    1 
ATOM   14803 N  NE    . ARG   B  1  799  ? 26.128  47.099  58.481  1.00 33.04 ? 797  ARG   B NE    1 
ATOM   14804 C  CZ    . ARG   B  1  799  ? 24.838  46.821  58.331  1.00 34.41 ? 797  ARG   B CZ    1 
ATOM   14805 N  NH1   . ARG   B  1  799  ? 24.116  47.363  57.364  1.00 29.94 ? 797  ARG   B NH1   1 
ATOM   14806 N  NH2   . ARG   B  1  799  ? 24.256  45.970  59.171  1.00 27.90 ? 797  ARG   B NH2   1 
ATOM   14807 N  N     . LEU   B  1  800  ? 24.519  52.782  57.658  1.00 24.44 ? 798  LEU   B N     1 
ATOM   14808 C  CA    . LEU   B  1  800  ? 23.174  53.316  57.618  1.00 24.25 ? 798  LEU   B CA    1 
ATOM   14809 C  C     . LEU   B  1  800  ? 22.351  52.436  56.696  1.00 26.06 ? 798  LEU   B C     1 
ATOM   14810 O  O     . LEU   B  1  800  ? 22.888  51.735  55.836  1.00 26.25 ? 798  LEU   B O     1 
ATOM   14811 C  CB    . LEU   B  1  800  ? 23.145  54.746  57.071  1.00 27.72 ? 798  LEU   B CB    1 
ATOM   14812 C  CG    . LEU   B  1  800  ? 23.795  55.824  57.928  1.00 30.16 ? 798  LEU   B CG    1 
ATOM   14813 C  CD1   . LEU   B  1  800  ? 23.793  57.125  57.145  1.00 31.03 ? 798  LEU   B CD1   1 
ATOM   14814 C  CD2   . LEU   B  1  800  ? 23.035  55.959  59.239  1.00 24.01 ? 798  LEU   B CD2   1 
ATOM   14815 N  N     . SER   B  1  801  ? 21.042  52.473  56.890  1.00 25.68 ? 799  SER   B N     1 
ATOM   14816 C  CA    . SER   B  1  801  ? 20.131  51.821  55.978  1.00 25.04 ? 799  SER   B CA    1 
ATOM   14817 C  C     . SER   B  1  801  ? 20.208  52.529  54.631  1.00 29.50 ? 799  SER   B C     1 
ATOM   14818 O  O     . SER   B  1  801  ? 20.761  53.627  54.526  1.00 29.91 ? 799  SER   B O     1 
ATOM   14819 C  CB    . SER   B  1  801  ? 18.711  51.933  56.522  1.00 26.92 ? 799  SER   B CB    1 
ATOM   14820 O  OG    . SER   B  1  801  ? 18.264  53.273  56.409  1.00 27.86 ? 799  SER   B OG    1 
ATOM   14821 N  N     . PRO   B  1  802  ? 19.671  51.917  53.571  1.00 33.38 ? 800  PRO   B N     1 
ATOM   14822 C  CA    . PRO   B  1  802  ? 19.578  52.644  52.294  1.00 32.60 ? 800  PRO   B CA    1 
ATOM   14823 C  C     . PRO   B  1  802  ? 18.787  53.933  52.401  1.00 31.39 ? 800  PRO   B C     1 
ATOM   14824 O  O     . PRO   B  1  802  ? 19.024  54.864  51.622  1.00 34.58 ? 800  PRO   B O     1 
ATOM   14825 C  CB    . PRO   B  1  802  ? 18.902  51.632  51.361  1.00 30.72 ? 800  PRO   B CB    1 
ATOM   14826 C  CG    . PRO   B  1  802  ? 19.251  50.304  51.945  1.00 33.30 ? 800  PRO   B CG    1 
ATOM   14827 C  CD    . PRO   B  1  802  ? 19.239  50.514  53.437  1.00 31.53 ? 800  PRO   B CD    1 
ATOM   14828 N  N     . ALA   B  1  803  ? 17.857  54.015  53.351  1.00 32.83 ? 801  ALA   B N     1 
ATOM   14829 C  CA    . ALA   B  1  803  ? 17.145  55.249  53.648  1.00 32.14 ? 801  ALA   B CA    1 
ATOM   14830 C  C     . ALA   B  1  803  ? 17.994  56.258  54.416  1.00 30.85 ? 801  ALA   B C     1 
ATOM   14831 O  O     . ALA   B  1  803  ? 17.524  57.372  54.668  1.00 35.63 ? 801  ALA   B O     1 
ATOM   14832 C  CB    . ALA   B  1  803  ? 15.866  54.939  54.429  1.00 32.93 ? 801  ALA   B CB    1 
ATOM   14833 N  N     . GLY   B  1  804  ? 19.221  55.910  54.790  1.00 28.36 ? 802  GLY   B N     1 
ATOM   14834 C  CA    . GLY   B  1  804  ? 20.066  56.841  55.510  1.00 30.00 ? 802  GLY   B CA    1 
ATOM   14835 C  C     . GLY   B  1  804  ? 19.779  56.952  56.991  1.00 28.75 ? 802  GLY   B C     1 
ATOM   14836 O  O     . GLY   B  1  804  ? 19.960  58.028  57.570  1.00 29.34 ? 802  GLY   B O     1 
ATOM   14837 N  N     . ARG   B  1  805  ? 19.341  55.875  57.627  1.00 28.01 ? 803  ARG   B N     1 
ATOM   14838 C  CA    . ARG   B  1  805  ? 18.947  55.895  59.026  1.00 24.21 ? 803  ARG   B CA    1 
ATOM   14839 C  C     . ARG   B  1  805  ? 19.651  54.784  59.785  1.00 24.75 ? 803  ARG   B C     1 
ATOM   14840 O  O     . ARG   B  1  805  ? 20.094  53.798  59.190  1.00 23.58 ? 803  ARG   B O     1 
ATOM   14841 C  CB    . ARG   B  1  805  ? 17.428  55.728  59.162  1.00 27.16 ? 803  ARG   B CB    1 
ATOM   14842 C  CG    . ARG   B  1  805  ? 16.643  56.854  58.520  1.00 30.77 ? 803  ARG   B CG    1 
ATOM   14843 C  CD    . ARG   B  1  805  ? 17.026  58.201  59.117  1.00 33.44 ? 803  ARG   B CD    1 
ATOM   14844 N  NE    . ARG   B  1  805  ? 16.265  59.286  58.508  1.00 36.32 ? 803  ARG   B NE    1 
ATOM   14845 C  CZ    . ARG   B  1  805  ? 16.719  60.069  57.538  1.00 32.53 ? 803  ARG   B CZ    1 
ATOM   14846 N  NH1   . ARG   B  1  805  ? 17.957  59.960  57.080  1.00 33.16 ? 803  ARG   B NH1   1 
ATOM   14847 N  NH2   . ARG   B  1  805  ? 15.907  60.980  57.009  1.00 38.23 ? 803  ARG   B NH2   1 
ATOM   14848 N  N     . PRO   B  1  806  ? 19.772  54.914  61.106  1.00 22.55 ? 804  PRO   B N     1 
ATOM   14849 C  CA    . PRO   B  1  806  ? 20.502  53.899  61.871  1.00 21.42 ? 804  PRO   B CA    1 
ATOM   14850 C  C     . PRO   B  1  806  ? 19.838  52.540  61.766  1.00 20.84 ? 804  PRO   B C     1 
ATOM   14851 O  O     . PRO   B  1  806  ? 18.610  52.423  61.710  1.00 20.08 ? 804  PRO   B O     1 
ATOM   14852 C  CB    . PRO   B  1  806  ? 20.453  54.434  63.305  1.00 22.22 ? 804  PRO   B CB    1 
ATOM   14853 C  CG    . PRO   B  1  806  ? 20.286  55.910  63.130  1.00 24.50 ? 804  PRO   B CG    1 
ATOM   14854 C  CD    . PRO   B  1  806  ? 19.381  56.053  61.953  1.00 23.73 ? 804  PRO   B CD    1 
ATOM   14855 N  N     . ILE   B  1  807  ? 20.674  51.511  61.735  1.00 18.88 ? 805  ILE   B N     1 
ATOM   14856 C  CA    . ILE   B  1  807  ? 20.214  50.127  61.736  1.00 17.94 ? 805  ILE   B CA    1 
ATOM   14857 C  C     . ILE   B  1  807  ? 19.737  49.810  63.147  1.00 17.02 ? 805  ILE   B C     1 
ATOM   14858 O  O     . ILE   B  1  807  ? 20.518  49.947  64.099  1.00 18.87 ? 805  ILE   B O     1 
ATOM   14859 C  CB    . ILE   B  1  807  ? 21.354  49.181  61.340  1.00 17.90 ? 805  ILE   B CB    1 
ATOM   14860 C  CG1   . ILE   B  1  807  ? 21.946  49.547  59.968  1.00 22.15 ? 805  ILE   B CG1   1 
ATOM   14861 C  CG2   . ILE   B  1  807  ? 20.882  47.732  61.408  1.00 19.31 ? 805  ILE   B CG2   1 
ATOM   14862 C  CD1   . ILE   B  1  807  ? 21.023  49.272  58.816  1.00 25.06 ? 805  ILE   B CD1   1 
ATOM   14863 N  N     . PRO   B  1  808  ? 18.485  49.401  63.331  1.00 16.48 ? 806  PRO   B N     1 
ATOM   14864 C  CA    . PRO   B  1  808  ? 17.986  49.150  64.690  1.00 16.04 ? 806  PRO   B CA    1 
ATOM   14865 C  C     . PRO   B  1  808  ? 18.693  47.979  65.347  1.00 17.61 ? 806  PRO   B C     1 
ATOM   14866 O  O     . PRO   B  1  808  ? 18.962  46.949  64.723  1.00 16.68 ? 806  PRO   B O     1 
ATOM   14867 C  CB    . PRO   B  1  808  ? 16.504  48.831  64.476  1.00 18.40 ? 806  PRO   B CB    1 
ATOM   14868 C  CG    . PRO   B  1  808  ? 16.160  49.442  63.152  1.00 21.85 ? 806  PRO   B CG    1 
ATOM   14869 C  CD    . PRO   B  1  808  ? 17.418  49.326  62.326  1.00 16.50 ? 806  PRO   B CD    1 
ATOM   14870 N  N     . LEU   B  1  809  ? 18.976  48.144  66.635  1.00 15.44 ? 807  LEU   B N     1 
ATOM   14871 C  CA    . LEU   B  1  809  ? 19.563  47.087  67.442  1.00 15.49 ? 807  LEU   B CA    1 
ATOM   14872 C  C     . LEU   B  1  809  ? 18.713  46.948  68.684  1.00 14.21 ? 807  LEU   B C     1 
ATOM   14873 O  O     . LEU   B  1  809  ? 18.504  47.929  69.400  1.00 16.38 ? 807  LEU   B O     1 
ATOM   14874 C  CB    . LEU   B  1  809  ? 20.989  47.458  67.846  1.00 16.57 ? 807  LEU   B CB    1 
ATOM   14875 C  CG    . LEU   B  1  809  ? 21.671  46.591  68.898  1.00 17.30 ? 807  LEU   B CG    1 
ATOM   14876 C  CD1   . LEU   B  1  809  ? 21.848  45.174  68.383  1.00 16.02 ? 807  LEU   B CD1   1 
ATOM   14877 C  CD2   . LEU   B  1  809  ? 23.013  47.210  69.279  1.00 17.92 ? 807  LEU   B CD2   1 
ATOM   14878 N  N     . ILE   B  1  810  ? 18.217  45.745  68.932  1.00 14.03 ? 808  ILE   B N     1 
ATOM   14879 C  CA    . ILE   B  1  810  ? 17.675  45.390  70.235  1.00 14.24 ? 808  ILE   B CA    1 
ATOM   14880 C  C     . ILE   B  1  810  ? 18.780  44.608  70.903  1.00 15.22 ? 808  ILE   B C     1 
ATOM   14881 O  O     . ILE   B  1  810  ? 19.223  43.591  70.367  1.00 16.56 ? 808  ILE   B O     1 
ATOM   14882 C  CB    . ILE   B  1  810  ? 16.405  44.539  70.120  1.00 15.20 ? 808  ILE   B CB    1 
ATOM   14883 C  CG1   . ILE   B  1  810  ? 15.388  45.230  69.229  1.00 16.12 ? 808  ILE   B CG1   1 
ATOM   14884 C  CG2   . ILE   B  1  810  ? 15.814  44.305  71.513  1.00 17.10 ? 808  ILE   B CG2   1 
ATOM   14885 C  CD1   . ILE   B  1  810  ? 14.030  44.510  69.198  1.00 17.07 ? 808  ILE   B CD1   1 
ATOM   14886 N  N     . ALA   B  1  811  ? 19.245  45.084  72.049  1.00 15.68 ? 809  ALA   B N     1 
ATOM   14887 C  CA    . ALA   B  1  811  ? 20.372  44.455  72.729  1.00 14.81 ? 809  ALA   B CA    1 
ATOM   14888 C  C     . ALA   B  1  811  ? 19.939  44.241  74.172  1.00 15.08 ? 809  ALA   B C     1 
ATOM   14889 O  O     . ALA   B  1  811  ? 19.889  45.194  74.960  1.00 16.74 ? 809  ALA   B O     1 
ATOM   14890 C  CB    . ALA   B  1  811  ? 21.638  45.296  72.636  1.00 17.46 ? 809  ALA   B CB    1 
ATOM   14891 N  N     . GLU   B  1  812  ? 19.618  43.003  74.493  1.00 14.53 ? 810  GLU   B N     1 
ATOM   14892 C  CA    . GLU   B  1  812  ? 19.122  42.614  75.807  1.00 14.29 ? 810  GLU   B CA    1 
ATOM   14893 C  C     . GLU   B  1  812  ? 20.252  41.866  76.485  1.00 16.35 ? 810  GLU   B C     1 
ATOM   14894 O  O     . GLU   B  1  812  ? 20.714  40.832  75.987  1.00 16.42 ? 810  GLU   B O     1 
ATOM   14895 C  CB    . GLU   B  1  812  ? 17.855  41.774  75.661  1.00 16.99 ? 810  GLU   B CB    1 
ATOM   14896 C  CG    . GLU   B  1  812  ? 16.780  42.560  74.915  1.00 16.59 ? 810  GLU   B CG    1 
ATOM   14897 C  CD    . GLU   B  1  812  ? 16.396  43.838  75.662  1.00 19.46 ? 810  GLU   B CD    1 
ATOM   14898 O  OE1   . GLU   B  1  812  ? 15.687  43.734  76.684  1.00 18.68 ? 810  GLU   B OE1   1 
ATOM   14899 O  OE2   . GLU   B  1  812  ? 16.787  44.950  75.244  1.00 18.77 ? 810  GLU   B OE2   1 
ATOM   14900 N  N     . THR   B  1  813  ? 20.740  42.429  77.582  1.00 15.73 ? 811  THR   B N     1 
ATOM   14901 C  CA    . THR   B  1  813  ? 22.063  42.088  78.058  1.00 15.60 ? 811  THR   B CA    1 
ATOM   14902 C  C     . THR   B  1  813  ? 22.030  41.640  79.517  1.00 15.24 ? 811  THR   B C     1 
ATOM   14903 O  O     . THR   B  1  813  ? 21.017  41.118  79.984  1.00 16.36 ? 811  THR   B O     1 
ATOM   14904 C  CB    . THR   B  1  813  ? 23.011  43.247  77.756  1.00 16.08 ? 811  THR   B CB    1 
ATOM   14905 O  OG1   . THR   B  1  813  ? 22.429  44.482  78.189  1.00 16.47 ? 811  THR   B OG1   1 
ATOM   14906 C  CG2   . THR   B  1  813  ? 23.227  43.340  76.243  1.00 17.80 ? 811  THR   B CG2   1 
ATOM   14907 N  N     . GLY   B  1  814  ? 23.128  41.805  80.236  1.00 16.84 ? 812  GLY   B N     1 
ATOM   14908 C  CA    . GLY   B  1  814  ? 23.275  41.121  81.504  1.00 17.11 ? 812  GLY   B CA    1 
ATOM   14909 C  C     . GLY   B  1  814  ? 22.538  41.780  82.656  1.00 16.99 ? 812  GLY   B C     1 
ATOM   14910 O  O     . GLY   B  1  814  ? 21.863  42.796  82.517  1.00 19.32 ? 812  GLY   B O     1 
ATOM   14911 N  N     . GLY   B  1  815  ? 22.655  41.151  83.818  1.00 15.75 ? 813  GLY   B N     1 
ATOM   14912 C  CA    . GLY   B  1  815  ? 22.052  41.682  85.022  1.00 15.64 ? 813  GLY   B CA    1 
ATOM   14913 C  C     . GLY   B  1  815  ? 23.001  41.503  86.186  1.00 16.20 ? 813  GLY   B C     1 
ATOM   14914 O  O     . GLY   B  1  815  ? 23.967  40.749  86.118  1.00 19.38 ? 813  GLY   B O     1 
ATOM   14915 N  N     . GLN   B  1  816  ? 22.728  42.248  87.245  1.00 15.65 ? 814  GLN   B N     1 
ATOM   14916 C  CA    . GLN   B  1  816  ? 23.394  42.068  88.533  1.00 16.52 ? 814  GLN   B CA    1 
ATOM   14917 C  C     . GLN   B  1  816  ? 22.285  42.104  89.570  1.00 15.64 ? 814  GLN   B C     1 
ATOM   14918 O  O     . GLN   B  1  816  ? 22.120  43.069  90.312  1.00 17.03 ? 814  GLN   B O     1 
ATOM   14919 C  CB    . GLN   B  1  816  ? 24.447  43.143  88.782  1.00 16.93 ? 814  GLN   B CB    1 
ATOM   14920 C  CG    . GLN   B  1  816  ? 25.376  42.831  89.948  1.00 17.06 ? 814  GLN   B CG    1 
ATOM   14921 C  CD    . GLN   B  1  816  ? 26.221  41.611  89.687  1.00 17.01 ? 814  GLN   B CD    1 
ATOM   14922 O  OE1   . GLN   B  1  816  ? 25.766  40.475  89.839  1.00 18.39 ? 814  GLN   B OE1   1 
ATOM   14923 N  NE2   . GLN   B  1  816  ? 27.477  41.839  89.287  1.00 17.17 ? 814  GLN   B NE2   1 
ATOM   14924 N  N     . ASN   B  1  817  ? 21.493  41.047  89.589  1.00 13.88 ? 815  ASN   B N     1 
ATOM   14925 C  CA    . ASN   B  1  817  ? 20.143  41.120  90.124  1.00 14.24 ? 815  ASN   B CA    1 
ATOM   14926 C  C     . ASN   B  1  817  ? 20.149  40.894  91.623  1.00 15.37 ? 815  ASN   B C     1 
ATOM   14927 O  O     . ASN   B  1  817  ? 20.794  39.960  92.116  1.00 15.85 ? 815  ASN   B O     1 
ATOM   14928 C  CB    . ASN   B  1  817  ? 19.274  40.076  89.434  1.00 15.23 ? 815  ASN   B CB    1 
ATOM   14929 C  CG    . ASN   B  1  817  ? 19.416  40.135  87.935  1.00 13.98 ? 815  ASN   B CG    1 
ATOM   14930 O  OD1   . ASN   B  1  817  ? 19.234  41.193  87.324  1.00 14.39 ? 815  ASN   B OD1   1 
ATOM   14931 N  ND2   . ASN   B  1  817  ? 19.788  39.016  87.341  1.00 14.42 ? 815  ASN   B ND2   1 
ATOM   14932 N  N     . ALA   B  1  818  ? 19.418  41.745  92.337  1.00 13.86 ? 816  ALA   B N     1 
ATOM   14933 C  CA    . ALA   B  1  818  ? 19.340  41.660  93.785  1.00 14.58 ? 816  ALA   B CA    1 
ATOM   14934 C  C     . ALA   B  1  818  ? 17.951  41.230  94.225  1.00 13.55 ? 816  ALA   B C     1 
ATOM   14935 O  O     . ALA   B  1  818  ? 16.957  41.393  93.517  1.00 14.87 ? 816  ALA   B O     1 
ATOM   14936 C  CB    . ALA   B  1  818  ? 19.657  43.017  94.422  1.00 15.62 ? 816  ALA   B CB    1 
ATOM   14937 N  N     . MET   B  1  819  ? 17.893  40.687  95.434  1.00 14.21 ? 817  MET   B N     1 
ATOM   14938 C  CA    . MET   B  1  819  ? 16.648  40.470  96.140  1.00 13.69 ? 817  MET   B CA    1 
ATOM   14939 C  C     . MET   B  1  819  ? 16.843  41.058  97.518  1.00 15.30 ? 817  MET   B C     1 
ATOM   14940 O  O     . MET   B  1  819  ? 17.827  40.735  98.184  1.00 15.71 ? 817  MET   B O     1 
ATOM   14941 C  CB    . MET   B  1  819  ? 16.333  38.984  96.285  1.00 14.65 ? 817  MET   B CB    1 
ATOM   14942 C  CG    . MET   B  1  819  ? 15.080  38.732  97.139  1.00 15.80 ? 817  MET   B CG    1 
ATOM   14943 S  SD    . MET   B  1  819  ? 14.814  36.981  97.433  1.00 18.30 ? 817  MET   B SD    1 
ATOM   14944 C  CE    . MET   B  1  819  ? 14.196  36.475  95.838  1.00 20.49 ? 817  MET   B CE    1 
ATOM   14945 N  N     . ILE   B  1  820  ? 15.935  41.931  97.924  1.00 15.52 ? 818  ILE   B N     1 
ATOM   14946 C  CA    . ILE   B  1  820  ? 15.966  42.521  99.255  1.00 14.02 ? 818  ILE   B CA    1 
ATOM   14947 C  C     . ILE   B  1  820  ? 14.945  41.806  100.112 1.00 15.50 ? 818  ILE   B C     1 
ATOM   14948 O  O     . ILE   B  1  820  ? 13.794  41.632  99.698  1.00 15.50 ? 818  ILE   B O     1 
ATOM   14949 C  CB    . ILE   B  1  820  ? 15.698  44.032  99.209  1.00 15.51 ? 818  ILE   B CB    1 
ATOM   14950 C  CG1   . ILE   B  1  820  ? 16.809  44.716  98.416  1.00 16.51 ? 818  ILE   B CG1   1 
ATOM   14951 C  CG2   . ILE   B  1  820  ? 15.599  44.598  100.642 1.00 17.54 ? 818  ILE   B CG2   1 
ATOM   14952 C  CD1   . ILE   B  1  820  ? 16.632  46.211  98.341  1.00 18.29 ? 818  ILE   B CD1   1 
ATOM   14953 N  N     . VAL   B  1  821  ? 15.370  41.378  101.298 1.00 16.22 ? 819  VAL   B N     1 
ATOM   14954 C  CA    . VAL   B  1  821  ? 14.532  40.624  102.216 1.00 15.70 ? 819  VAL   B CA    1 
ATOM   14955 C  C     . VAL   B  1  821  ? 14.535  41.364  103.537 1.00 17.06 ? 819  VAL   B C     1 
ATOM   14956 O  O     . VAL   B  1  821  ? 15.606  41.598  104.108 1.00 17.43 ? 819  VAL   B O     1 
ATOM   14957 C  CB    . VAL   B  1  821  ? 15.078  39.202  102.421 1.00 14.99 ? 819  VAL   B CB    1 
ATOM   14958 C  CG1   . VAL   B  1  821  ? 14.185  38.421  103.365 1.00 18.23 ? 819  VAL   B CG1   1 
ATOM   14959 C  CG2   . VAL   B  1  821  ? 15.227  38.502  101.075 1.00 15.94 ? 819  VAL   B CG2   1 
ATOM   14960 N  N     . ASP   B  1  822  ? 13.358  41.717  104.030 1.00 16.49 ? 820  ASP   B N     1 
ATOM   14961 C  CA    . ASP   B  1  822  ? 13.299  42.370  105.327 1.00 17.93 ? 820  ASP   B CA    1 
ATOM   14962 C  C     . ASP   B  1  822  ? 12.892  41.367  106.403 1.00 19.81 ? 820  ASP   B C     1 
ATOM   14963 O  O     . ASP   B  1  822  ? 12.669  40.186  106.139 1.00 18.95 ? 820  ASP   B O     1 
ATOM   14964 C  CB    . ASP   B  1  822  ? 12.479  43.666  105.278 1.00 19.23 ? 820  ASP   B CB    1 
ATOM   14965 C  CG    . ASP   B  1  822  ? 10.974  43.443  105.238 1.00 19.72 ? 820  ASP   B CG    1 
ATOM   14966 O  OD1   . ASP   B  1  822  ? 10.488  42.313  105.452 1.00 18.74 ? 820  ASP   B OD1   1 
ATOM   14967 O  OD2   . ASP   B  1  822  ? 10.271  44.443  104.982 1.00 20.45 ? 820  ASP   B OD2   1 
ATOM   14968 N  N     . SER   B  1  823  ? 12.797  41.850  107.642 1.00 20.33 ? 821  SER   B N     1 
ATOM   14969 C  CA    . SER   B  1  823  ? 12.516  40.953  108.755 1.00 20.54 ? 821  SER   B CA    1 
ATOM   14970 C  C     . SER   B  1  823  ? 11.070  40.483  108.794 1.00 22.84 ? 821  SER   B C     1 
ATOM   14971 O  O     . SER   B  1  823  ? 10.731  39.632  109.625 1.00 24.41 ? 821  SER   B O     1 
ATOM   14972 C  CB    . SER   B  1  823  ? 12.892  41.614  110.079 1.00 21.69 ? 821  SER   B CB    1 
ATOM   14973 O  OG    . SER   B  1  823  ? 12.161  42.810  110.258 1.00 25.04 ? 821  SER   B OG    1 
ATOM   14974 N  N     . SER   B  1  824  ? 10.209  41.002  107.929 1.00 18.86 ? 822  SER   B N     1 
ATOM   14975 C  CA    . SER   B  1  824  ? 8.835   40.532  107.888 1.00 19.35 ? 822  SER   B CA    1 
ATOM   14976 C  C     . SER   B  1  824  ? 8.647   39.356  106.942 1.00 21.26 ? 822  SER   B C     1 
ATOM   14977 O  O     . SER   B  1  824  ? 7.588   38.721  106.961 1.00 21.51 ? 822  SER   B O     1 
ATOM   14978 C  CB    . SER   B  1  824  ? 7.879   41.667  107.497 1.00 20.76 ? 822  SER   B CB    1 
ATOM   14979 O  OG    . SER   B  1  824  ? 7.954   41.945  106.104 1.00 19.63 ? 822  SER   B OG    1 
ATOM   14980 N  N     . ALA   B  1  825  ? 9.648   39.049  106.125 1.00 19.07 ? 823  ALA   B N     1 
ATOM   14981 C  CA    . ALA   B  1  825  ? 9.516   37.986  105.147 1.00 19.44 ? 823  ALA   B CA    1 
ATOM   14982 C  C     . ALA   B  1  825  ? 9.504   36.625  105.832 1.00 20.51 ? 823  ALA   B C     1 
ATOM   14983 O  O     . ALA   B  1  825  ? 10.081  36.438  106.906 1.00 23.34 ? 823  ALA   B O     1 
ATOM   14984 C  CB    . ALA   B  1  825  ? 10.694  38.053  104.185 1.00 19.08 ? 823  ALA   B CB    1 
ATOM   14985 N  N     . LEU   B  1  826  ? 8.850   35.665  105.194 1.00 21.10 ? 824  LEU   B N     1 
ATOM   14986 C  CA    . LEU   B  1  826  ? 8.824   34.304  105.713 1.00 20.37 ? 824  LEU   B CA    1 
ATOM   14987 C  C     . LEU   B  1  826  ? 10.068  33.571  105.228 1.00 22.49 ? 824  LEU   B C     1 
ATOM   14988 O  O     . LEU   B  1  826  ? 10.265  33.412  104.019 1.00 20.25 ? 824  LEU   B O     1 
ATOM   14989 C  CB    . LEU   B  1  826  ? 7.563   33.590  105.240 1.00 25.56 ? 824  LEU   B CB    1 
ATOM   14990 C  CG    . LEU   B  1  826  ? 7.346   32.175  105.770 1.00 28.53 ? 824  LEU   B CG    1 
ATOM   14991 C  CD1   . LEU   B  1  826  ? 7.362   32.159  107.285 1.00 31.26 ? 824  LEU   B CD1   1 
ATOM   14992 C  CD2   . LEU   B  1  826  ? 6.023   31.640  105.240 1.00 35.92 ? 824  LEU   B CD2   1 
ATOM   14993 N  N     . ALA   B  1  827  ? 10.911  33.140  106.171 1.00 22.13 ? 825  ALA   B N     1 
ATOM   14994 C  CA    . ALA   B  1  827  ? 12.208  32.568  105.822 1.00 19.74 ? 825  ALA   B CA    1 
ATOM   14995 C  C     . ALA   B  1  827  ? 12.076  31.401  104.849 1.00 19.88 ? 825  ALA   B C     1 
ATOM   14996 O  O     . ALA   B  1  827  ? 12.847  31.305  103.887 1.00 19.21 ? 825  ALA   B O     1 
ATOM   14997 C  CB    . ALA   B  1  827  ? 12.929  32.119  107.089 1.00 21.17 ? 825  ALA   B CB    1 
ATOM   14998 N  N     . GLU   B  1  828  ? 11.123  30.496  105.089 1.00 20.72 ? 826  GLU   B N     1 
ATOM   14999 C  CA    . GLU   B  1  828  ? 10.979  29.343  104.204 1.00 21.29 ? 826  GLU   B CA    1 
ATOM   15000 C  C     . GLU   B  1  828  ? 10.689  29.780  102.773 1.00 21.18 ? 826  GLU   B C     1 
ATOM   15001 O  O     . GLU   B  1  828  ? 11.201  29.185  101.812 1.00 19.87 ? 826  GLU   B O     1 
ATOM   15002 C  CB    . GLU   B  1  828  ? 9.865   28.423  104.708 1.00 22.84 ? 826  GLU   B CB    1 
ATOM   15003 C  CG    . GLU   B  1  828  ? 10.227  27.595  105.936 1.00 26.02 ? 826  GLU   B CG    1 
ATOM   15004 C  CD    . GLU   B  1  828  ? 10.129  28.351  107.256 1.00 28.00 ? 826  GLU   B CD    1 
ATOM   15005 O  OE1   . GLU   B  1  828  ? 9.792   29.558  107.260 1.00 27.03 ? 826  GLU   B OE1   1 
ATOM   15006 O  OE2   . GLU   B  1  828  ? 10.392  27.721  108.306 1.00 28.83 ? 826  GLU   B OE2   1 
ATOM   15007 N  N     . GLN   B  1  829  ? 9.861   30.815  102.605 1.00 19.14 ? 827  GLN   B N     1 
ATOM   15008 C  CA    . GLN   B  1  829  ? 9.531   31.277  101.260 1.00 19.94 ? 827  GLN   B CA    1 
ATOM   15009 C  C     . GLN   B  1  829  ? 10.740  31.916  100.613 1.00 19.24 ? 827  GLN   B C     1 
ATOM   15010 O  O     . GLN   B  1  829  ? 11.040  31.672  99.439  1.00 18.59 ? 827  GLN   B O     1 
ATOM   15011 C  CB    . GLN   B  1  829  ? 8.407   32.303  101.323 1.00 25.57 ? 827  GLN   B CB    1 
ATOM   15012 C  CG    . GLN   B  1  829  ? 7.037   31.743  101.561 1.00 28.85 ? 827  GLN   B CG    1 
ATOM   15013 C  CD    . GLN   B  1  829  ? 5.983   32.825  101.445 1.00 35.70 ? 827  GLN   B CD    1 
ATOM   15014 O  OE1   . GLN   B  1  829  ? 6.267   34.009  101.664 1.00 30.58 ? 827  GLN   B OE1   1 
ATOM   15015 N  NE2   . GLN   B  1  829  ? 4.767   32.434  101.085 1.00 39.89 ? 827  GLN   B NE2   1 
ATOM   15016 N  N     . VAL   B  1  830  ? 11.433  32.762  101.364 1.00 17.85 ? 828  VAL   B N     1 
ATOM   15017 C  CA    . VAL   B  1  830  ? 12.668  33.359  100.881 1.00 16.62 ? 828  VAL   B CA    1 
ATOM   15018 C  C     . VAL   B  1  830  ? 13.625  32.277  100.414 1.00 18.91 ? 828  VAL   B C     1 
ATOM   15019 O  O     . VAL   B  1  830  ? 14.188  32.350  99.318  1.00 17.56 ? 828  VAL   B O     1 
ATOM   15020 C  CB    . VAL   B  1  830  ? 13.312  34.218  101.980 1.00 17.55 ? 828  VAL   B CB    1 
ATOM   15021 C  CG1   . VAL   B  1  830  ? 14.710  34.638  101.550 1.00 18.08 ? 828  VAL   B CG1   1 
ATOM   15022 C  CG2   . VAL   B  1  830  ? 12.440  35.412  102.301 1.00 19.86 ? 828  VAL   B CG2   1 
ATOM   15023 N  N     . VAL   B  1  831  ? 13.838  31.262  101.253 1.00 17.53 ? 829  VAL   B N     1 
ATOM   15024 C  CA    . VAL   B  1  831  ? 14.832  30.250  100.933 1.00 17.51 ? 829  VAL   B CA    1 
ATOM   15025 C  C     . VAL   B  1  831  ? 14.471  29.513  99.651  1.00 17.76 ? 829  VAL   B C     1 
ATOM   15026 O  O     . VAL   B  1  831  ? 15.326  29.311  98.781  1.00 17.64 ? 829  VAL   B O     1 
ATOM   15027 C  CB    . VAL   B  1  831  ? 15.070  29.311  102.128 1.00 18.09 ? 829  VAL   B CB    1 
ATOM   15028 C  CG1   . VAL   B  1  831  ? 15.824  28.071  101.674 1.00 18.84 ? 829  VAL   B CG1   1 
ATOM   15029 C  CG2   . VAL   B  1  831  ? 15.855  30.045  103.199 1.00 18.62 ? 829  VAL   B CG2   1 
ATOM   15030 N  N     . GLY   B  1  832  ? 13.206  29.125  99.493  1.00 16.62 ? 830  GLY   B N     1 
ATOM   15031 C  CA    . GLY   B  1  832  ? 12.819  28.457  98.266  1.00 17.73 ? 830  GLY   B CA    1 
ATOM   15032 C  C     . GLY   B  1  832  ? 13.021  29.344  97.056  1.00 17.85 ? 830  GLY   B C     1 
ATOM   15033 O  O     . GLY   B  1  832  ? 13.498  28.892  96.013  1.00 18.41 ? 830  GLY   B O     1 
ATOM   15034 N  N     . ASP   B  1  833  ? 12.706  30.628  97.197  1.00 15.76 ? 831  ASP   B N     1 
ATOM   15035 C  CA    . ASP   B  1  833  ? 12.823  31.538  96.066  1.00 17.61 ? 831  ASP   B CA    1 
ATOM   15036 C  C     . ASP   B  1  833  ? 14.267  31.876  95.778  1.00 16.18 ? 831  ASP   B C     1 
ATOM   15037 O  O     . ASP   B  1  833  ? 14.621  32.106  94.623  1.00 16.14 ? 831  ASP   B O     1 
ATOM   15038 C  CB    . ASP   B  1  833  ? 12.009  32.805  96.316  1.00 17.20 ? 831  ASP   B CB    1 
ATOM   15039 C  CG    . ASP   B  1  833  ? 10.523  32.539  96.299  1.00 17.53 ? 831  ASP   B CG    1 
ATOM   15040 O  OD1   . ASP   B  1  833  ? 10.111  31.483  95.775  1.00 20.41 ? 831  ASP   B OD1   1 
ATOM   15041 O  OD2   . ASP   B  1  833  ? 9.756   33.375  96.816  1.00 19.41 ? 831  ASP   B OD2   1 
ATOM   15042 N  N     . VAL   B  1  834  ? 15.113  31.908  96.803  1.00 16.03 ? 832  VAL   B N     1 
ATOM   15043 C  CA    . VAL   B  1  834  ? 16.531  32.117  96.581  1.00 17.14 ? 832  VAL   B CA    1 
ATOM   15044 C  C     . VAL   B  1  834  ? 17.134  30.926  95.859  1.00 16.79 ? 832  VAL   B C     1 
ATOM   15045 O  O     . VAL   B  1  834  ? 17.930  31.082  94.927  1.00 17.02 ? 832  VAL   B O     1 
ATOM   15046 C  CB    . VAL   B  1  834  ? 17.231  32.393  97.919  1.00 16.06 ? 832  VAL   B CB    1 
ATOM   15047 C  CG1   . VAL   B  1  834  ? 18.719  32.205  97.785  1.00 17.74 ? 832  VAL   B CG1   1 
ATOM   15048 C  CG2   . VAL   B  1  834  ? 16.926  33.804  98.361  1.00 16.67 ? 832  VAL   B CG2   1 
ATOM   15049 N  N     . ILE   B  1  835  ? 16.797  29.718  96.296  1.00 16.31 ? 833  ILE   B N     1 
ATOM   15050 C  CA    . ILE   B  1  835  ? 17.360  28.539  95.648  1.00 19.14 ? 833  ILE   B CA    1 
ATOM   15051 C  C     . ILE   B  1  835  ? 16.976  28.503  94.178  1.00 18.46 ? 833  ILE   B C     1 
ATOM   15052 O  O     . ILE   B  1  835  ? 17.829  28.334  93.296  1.00 20.39 ? 833  ILE   B O     1 
ATOM   15053 C  CB    . ILE   B  1  835  ? 16.955  27.264  96.394  1.00 20.80 ? 833  ILE   B CB    1 
ATOM   15054 C  CG1   . ILE   B  1  835  ? 17.688  27.225  97.726  1.00 23.49 ? 833  ILE   B CG1   1 
ATOM   15055 C  CG2   . ILE   B  1  835  ? 17.262  26.026  95.540  1.00 24.06 ? 833  ILE   B CG2   1 
ATOM   15056 C  CD1   . ILE   B  1  835  ? 17.443  25.976  98.469  1.00 27.23 ? 833  ILE   B CD1   1 
ATOM   15057 N  N     . THR   B  1  836  ? 15.696  28.709  93.894  1.00 17.07 ? 834  THR   B N     1 
ATOM   15058 C  CA    . THR   B  1  836  ? 15.232  28.758  92.514  1.00 17.16 ? 834  THR   B CA    1 
ATOM   15059 C  C     . THR   B  1  836  ? 15.962  29.843  91.734  1.00 20.53 ? 834  THR   B C     1 
ATOM   15060 O  O     . THR   B  1  836  ? 16.464  29.607  90.626  1.00 22.68 ? 834  THR   B O     1 
ATOM   15061 C  CB    . THR   B  1  836  ? 13.725  29.028  92.530  1.00 19.57 ? 834  THR   B CB    1 
ATOM   15062 O  OG1   . THR   B  1  836  ? 13.046  27.902  93.101  1.00 25.88 ? 834  THR   B OG1   1 
ATOM   15063 C  CG2   . THR   B  1  836  ? 13.192  29.265  91.135  1.00 22.90 ? 834  THR   B CG2   1 
ATOM   15064 N  N     . SER   B  1  837  ? 16.039  31.043  92.303  1.00 15.80 ? 835  SER   B N     1 
ATOM   15065 C  CA    . SER   B  1  837  ? 16.527  32.184  91.546  1.00 16.15 ? 835  SER   B CA    1 
ATOM   15066 C  C     . SER   B  1  837  ? 18.038  32.161  91.397  1.00 15.39 ? 835  SER   B C     1 
ATOM   15067 O  O     . SER   B  1  837  ? 18.567  32.591  90.368  1.00 16.19 ? 835  SER   B O     1 
ATOM   15068 C  CB    . SER   B  1  837  ? 16.134  33.482  92.239  1.00 14.95 ? 835  SER   B CB    1 
ATOM   15069 O  OG    . SER   B  1  837  ? 14.723  33.570  92.380  1.00 15.07 ? 835  SER   B OG    1 
ATOM   15070 N  N     . ALA   B  1  838  ? 18.756  31.706  92.417  1.00 15.84 ? 836  ALA   B N     1 
ATOM   15071 C  CA    . ALA   B  1  838  ? 20.208  31.791  92.396  1.00 15.97 ? 836  ALA   B CA    1 
ATOM   15072 C  C     . ALA   B  1  838  ? 20.858  30.541  91.840  1.00 16.62 ? 836  ALA   B C     1 
ATOM   15073 O  O     . ALA   B  1  838  ? 21.913  30.637  91.204  1.00 18.66 ? 836  ALA   B O     1 
ATOM   15074 C  CB    . ALA   B  1  838  ? 20.740  32.015  93.816  1.00 15.99 ? 836  ALA   B CB    1 
ATOM   15075 N  N     . PHE   B  1  839  ? 20.283  29.370  92.085  1.00 17.55 ? 837  PHE   B N     1 
ATOM   15076 C  CA    . PHE   B  1  839  ? 21.017  28.139  91.864  1.00 19.04 ? 837  PHE   B CA    1 
ATOM   15077 C  C     . PHE   B  1  839  ? 20.382  27.200  90.863  1.00 21.70 ? 837  PHE   B C     1 
ATOM   15078 O  O     . PHE   B  1  839  ? 21.095  26.359  90.303  1.00 21.79 ? 837  PHE   B O     1 
ATOM   15079 C  CB    . PHE   B  1  839  ? 21.259  27.405  93.188  1.00 18.75 ? 837  PHE   B CB    1 
ATOM   15080 C  CG    . PHE   B  1  839  ? 21.972  28.242  94.205  1.00 17.35 ? 837  PHE   B CG    1 
ATOM   15081 C  CD1   . PHE   B  1  839  ? 23.260  28.710  93.956  1.00 17.57 ? 837  PHE   B CD1   1 
ATOM   15082 C  CD2   . PHE   B  1  839  ? 21.370  28.572  95.403  1.00 19.79 ? 837  PHE   B CD2   1 
ATOM   15083 C  CE1   . PHE   B  1  839  ? 23.923  29.490  94.882  1.00 17.10 ? 837  PHE   B CE1   1 
ATOM   15084 C  CE2   . PHE   B  1  839  ? 22.034  29.351  96.337  1.00 20.14 ? 837  PHE   B CE2   1 
ATOM   15085 C  CZ    . PHE   B  1  839  ? 23.320  29.803  96.078  1.00 19.96 ? 837  PHE   B CZ    1 
ATOM   15086 N  N     . ASP   B  1  840  ? 19.088  27.307  90.611  1.00 20.30 ? 838  ASP   B N     1 
ATOM   15087 C  CA    . ASP   B  1  840  ? 18.541  26.562  89.491  1.00 20.61 ? 838  ASP   B CA    1 
ATOM   15088 C  C     . ASP   B  1  840  ? 19.272  26.958  88.213  1.00 20.74 ? 838  ASP   B C     1 
ATOM   15089 O  O     . ASP   B  1  840  ? 19.696  28.106  88.034  1.00 20.81 ? 838  ASP   B O     1 
ATOM   15090 C  CB    . ASP   B  1  840  ? 17.039  26.806  89.348  1.00 27.28 ? 838  ASP   B CB    1 
ATOM   15091 N  N     . SER   B  1  841  ? 19.427  25.986  87.324  1.00 19.66 ? 839  SER   B N     1 
ATOM   15092 C  CA    . SER   B  1  841  ? 20.228  26.135  86.113  1.00 18.17 ? 839  SER   B CA    1 
ATOM   15093 C  C     . SER   B  1  841  ? 21.648  26.546  86.427  1.00 18.78 ? 839  SER   B C     1 
ATOM   15094 O  O     . SER   B  1  841  ? 22.318  27.163  85.599  1.00 17.25 ? 839  SER   B O     1 
ATOM   15095 C  CB    . SER   B  1  841  ? 19.596  27.091  85.096  1.00 22.19 ? 839  SER   B CB    1 
ATOM   15096 O  OG    . SER   B  1  841  ? 18.259  26.694  84.846  1.00 24.12 ? 839  SER   B OG    1 
ATOM   15097 N  N     . ALA   B  1  842  ? 22.106  26.213  87.630  1.00 17.66 ? 840  ALA   B N     1 
ATOM   15098 C  CA    . ALA   B  1  842  ? 23.420  26.623  88.108  1.00 16.25 ? 840  ALA   B CA    1 
ATOM   15099 C  C     . ALA   B  1  842  ? 23.618  28.127  87.940  1.00 14.60 ? 840  ALA   B C     1 
ATOM   15100 O  O     . ALA   B  1  842  ? 24.703  28.595  87.605  1.00 16.08 ? 840  ALA   B O     1 
ATOM   15101 C  CB    . ALA   B  1  842  ? 24.544  25.812  87.459  1.00 17.77 ? 840  ALA   B CB    1 
ATOM   15102 N  N     . GLY   B  1  843  ? 22.550  28.885  88.177  1.00 15.71 ? 841  GLY   B N     1 
ATOM   15103 C  CA    . GLY   B  1  843  ? 22.642  30.326  88.100  1.00 16.00 ? 841  GLY   B CA    1 
ATOM   15104 C  C     . GLY   B  1  843  ? 22.837  30.855  86.706  1.00 15.29 ? 841  GLY   B C     1 
ATOM   15105 O  O     . GLY   B  1  843  ? 23.173  32.029  86.542  1.00 15.73 ? 841  GLY   B O     1 
ATOM   15106 N  N     . GLN   B  1  844  ? 22.635  30.020  85.697  1.00 14.44 ? 842  GLN   B N     1 
ATOM   15107 C  CA    . GLN   B  1  844  ? 22.870  30.421  84.311  1.00 14.45 ? 842  GLN   B CA    1 
ATOM   15108 C  C     . GLN   B  1  844  ? 21.603  30.950  83.657  1.00 16.49 ? 842  GLN   B C     1 
ATOM   15109 O  O     . GLN   B  1  844  ? 21.157  30.486  82.610  1.00 16.95 ? 842  GLN   B O     1 
ATOM   15110 C  CB    . GLN   B  1  844  ? 23.476  29.261  83.543  1.00 14.80 ? 842  GLN   B CB    1 
ATOM   15111 C  CG    . GLN   B  1  844  ? 24.859  28.947  84.091  1.00 15.18 ? 842  GLN   B CG    1 
ATOM   15112 C  CD    . GLN   B  1  844  ? 25.414  27.643  83.586  1.00 15.56 ? 842  GLN   B CD    1 
ATOM   15113 O  OE1   . GLN   B  1  844  ? 26.497  27.612  83.012  1.00 15.55 ? 842  GLN   B OE1   1 
ATOM   15114 N  NE2   . GLN   B  1  844  ? 24.692  26.554  83.824  1.00 17.35 ? 842  GLN   B NE2   1 
ATOM   15115 N  N     . ARG   B  1  845  ? 21.002  31.935  84.320  1.00 16.53 ? 843  ARG   B N     1 
ATOM   15116 C  CA    . ARG   B  1  845  ? 19.905  32.720  83.780  1.00 15.82 ? 843  ARG   B CA    1 
ATOM   15117 C  C     . ARG   B  1  845  ? 20.306  34.179  83.903  1.00 14.66 ? 843  ARG   B C     1 
ATOM   15118 O  O     . ARG   B  1  845  ? 20.877  34.587  84.914  1.00 15.76 ? 843  ARG   B O     1 
ATOM   15119 C  CB    . ARG   B  1  845  ? 18.646  32.527  84.604  1.00 16.08 ? 843  ARG   B CB    1 
ATOM   15120 C  CG    . ARG   B  1  845  ? 18.107  31.107  84.619  1.00 17.39 ? 843  ARG   B CG    1 
ATOM   15121 C  CD    . ARG   B  1  845  ? 16.755  31.141  85.317  1.00 24.12 ? 843  ARG   B CD    1 
ATOM   15122 N  NE    . ARG   B  1  845  ? 16.023  29.885  85.227  1.00 28.17 ? 843  ARG   B NE    1 
ATOM   15123 C  CZ    . ARG   B  1  845  ? 15.858  29.056  86.245  1.00 31.51 ? 843  ARG   B CZ    1 
ATOM   15124 N  NH1   . ARG   B  1  845  ? 16.410  29.296  87.425  1.00 29.95 ? 843  ARG   B NH1   1 
ATOM   15125 N  NH2   . ARG   B  1  845  ? 15.106  27.970  86.081  1.00 36.91 ? 843  ARG   B NH2   1 
ATOM   15126 N  N     . CYS   B  1  846  ? 20.007  34.975  82.883  1.00 14.94 ? 844  CYS   B N     1 
ATOM   15127 C  CA    . CYS   B  1  846  ? 20.283  36.400  83.006  1.00 15.44 ? 844  CYS   B CA    1 
ATOM   15128 C  C     . CYS   B  1  846  ? 19.539  37.000  84.188  1.00 13.74 ? 844  CYS   B C     1 
ATOM   15129 O  O     . CYS   B  1  846  ? 19.979  37.999  84.763  1.00 15.89 ? 844  CYS   B O     1 
ATOM   15130 C  CB    . CYS   B  1  846  ? 19.861  37.110  81.722  1.00 16.45 ? 844  CYS   B CB    1 
ATOM   15131 S  SG    . CYS   B  1  846  ? 18.199  36.743  81.178  1.00 16.48 ? 844  CYS   B SG    1 
ATOM   15132 N  N     . SER   B  1  847  ? 18.373  36.443  84.505  1.00 13.62 ? 845  SER   B N     1 
ATOM   15133 C  CA    . SER   B  1  847  ? 17.513  36.881  85.592  1.00 13.36 ? 845  SER   B CA    1 
ATOM   15134 C  C     . SER   B  1  847  ? 17.950  36.359  86.954  1.00 14.52 ? 845  SER   B C     1 
ATOM   15135 O  O     . SER   B  1  847  ? 17.321  36.710  87.960  1.00 14.67 ? 845  SER   B O     1 
ATOM   15136 C  CB    . SER   B  1  847  ? 16.125  36.324  85.316  1.00 15.09 ? 845  SER   B CB    1 
ATOM   15137 O  OG    . SER   B  1  847  ? 16.249  34.932  85.074  1.00 15.99 ? 845  SER   B OG    1 
ATOM   15138 N  N     . ALA   B  1  848  ? 19.011  35.559  87.018  1.00 13.86 ? 846  ALA   B N     1 
ATOM   15139 C  CA    . ALA   B  1  848  ? 19.316  34.843  88.244  1.00 13.93 ? 846  ALA   B CA    1 
ATOM   15140 C  C     . ALA   B  1  848  ? 19.669  35.804  89.362  1.00 14.22 ? 846  ALA   B C     1 
ATOM   15141 O  O     . ALA   B  1  848  ? 20.223  36.884  89.146  1.00 14.40 ? 846  ALA   B O     1 
ATOM   15142 C  CB    . ALA   B  1  848  ? 20.508  33.921  88.017  1.00 14.33 ? 846  ALA   B CB    1 
ATOM   15143 N  N     . LEU   B  1  849  ? 19.346  35.380  90.582  1.00 14.39 ? 847  LEU   B N     1 
ATOM   15144 C  CA    . LEU   B  1  849  ? 19.675  36.158  91.764  1.00 14.43 ? 847  LEU   B CA    1 
ATOM   15145 C  C     . LEU   B  1  849  ? 21.176  36.139  92.014  1.00 14.73 ? 847  LEU   B C     1 
ATOM   15146 O  O     . LEU   B  1  849  ? 21.758  35.074  92.217  1.00 16.24 ? 847  LEU   B O     1 
ATOM   15147 C  CB    . LEU   B  1  849  ? 18.932  35.571  92.953  1.00 16.36 ? 847  LEU   B CB    1 
ATOM   15148 C  CG    . LEU   B  1  849  ? 19.299  36.212  94.285  1.00 15.22 ? 847  LEU   B CG    1 
ATOM   15149 C  CD1   . LEU   B  1  849  ? 18.971  37.696  94.286  1.00 16.94 ? 847  LEU   B CD1   1 
ATOM   15150 C  CD2   . LEU   B  1  849  ? 18.582  35.474  95.398  1.00 16.27 ? 847  LEU   B CD2   1 
ATOM   15151 N  N     . ARG   B  1  850  ? 21.782  37.321  92.017  1.00 13.25 ? 848  ARG   B N     1 
ATOM   15152 C  CA    . ARG   B  1  850  ? 23.210  37.467  92.234  1.00 14.53 ? 848  ARG   B CA    1 
ATOM   15153 C  C     . ARG   B  1  850  ? 23.540  38.029  93.602  1.00 14.62 ? 848  ARG   B C     1 
ATOM   15154 O  O     . ARG   B  1  850  ? 24.606  37.724  94.143  1.00 15.34 ? 848  ARG   B O     1 
ATOM   15155 C  CB    . ARG   B  1  850  ? 23.820  38.405  91.182  1.00 16.07 ? 848  ARG   B CB    1 
ATOM   15156 C  CG    . ARG   B  1  850  ? 23.528  38.015  89.759  1.00 15.65 ? 848  ARG   B CG    1 
ATOM   15157 C  CD    . ARG   B  1  850  ? 23.880  36.589  89.502  1.00 15.54 ? 848  ARG   B CD    1 
ATOM   15158 N  NE    . ARG   B  1  850  ? 23.708  36.263  88.094  1.00 15.71 ? 848  ARG   B NE    1 
ATOM   15159 C  CZ    . ARG   B  1  850  ? 23.848  35.044  87.597  1.00 16.00 ? 848  ARG   B CZ    1 
ATOM   15160 N  NH1   . ARG   B  1  850  ? 24.132  34.013  88.371  1.00 15.62 ? 848  ARG   B NH1   1 
ATOM   15161 N  NH2   . ARG   B  1  850  ? 23.664  34.854  86.289  1.00 15.85 ? 848  ARG   B NH2   1 
ATOM   15162 N  N     . VAL   B  1  851  ? 22.678  38.868  94.160  1.00 16.39 ? 849  VAL   B N     1 
ATOM   15163 C  CA    . VAL   B  1  851  ? 22.955  39.535  95.428  1.00 15.45 ? 849  VAL   B CA    1 
ATOM   15164 C  C     . VAL   B  1  851  ? 21.723  39.435  96.312  1.00 15.80 ? 849  VAL   B C     1 
ATOM   15165 O  O     . VAL   B  1  851  ? 20.686  40.041  96.020  1.00 15.47 ? 849  VAL   B O     1 
ATOM   15166 C  CB    . VAL   B  1  851  ? 23.364  41.000  95.243  1.00 16.26 ? 849  VAL   B CB    1 
ATOM   15167 C  CG1   . VAL   B  1  851  ? 23.749  41.576  96.601  1.00 19.53 ? 849  VAL   B CG1   1 
ATOM   15168 C  CG2   . VAL   B  1  851  ? 24.520  41.117  94.257  1.00 19.57 ? 849  VAL   B CG2   1 
ATOM   15169 N  N     . LEU   B  1  852  ? 21.828  38.661  97.380  1.00 16.23 ? 850  LEU   B N     1 
ATOM   15170 C  CA    . LEU   B  1  852  ? 20.760  38.509  98.350  1.00 14.92 ? 850  LEU   B CA    1 
ATOM   15171 C  C     . LEU   B  1  852  ? 21.039  39.479  99.483  1.00 16.02 ? 850  LEU   B C     1 
ATOM   15172 O  O     . LEU   B  1  852  ? 22.098  39.400  100.110 1.00 15.45 ? 850  LEU   B O     1 
ATOM   15173 C  CB    . LEU   B  1  852  ? 20.748  37.080  98.875  1.00 14.80 ? 850  LEU   B CB    1 
ATOM   15174 C  CG    . LEU   B  1  852  ? 19.726  36.817  99.977  1.00 15.01 ? 850  LEU   B CG    1 
ATOM   15175 C  CD1   . LEU   B  1  852  ? 18.300  37.132  99.530  1.00 16.49 ? 850  LEU   B CD1   1 
ATOM   15176 C  CD2   . LEU   B  1  852  ? 19.823  35.367  100.428 1.00 16.58 ? 850  LEU   B CD2   1 
ATOM   15177 N  N     . CYS   B  1  853  ? 20.118  40.404  99.724  1.00 15.88 ? 851  CYS   B N     1 
ATOM   15178 C  CA    . CYS   B  1  853  ? 20.288  41.442  100.733 1.00 16.33 ? 851  CYS   B CA    1 
ATOM   15179 C  C     . CYS   B  1  853  ? 19.348  41.131  101.882 1.00 14.92 ? 851  CYS   B C     1 
ATOM   15180 O  O     . CYS   B  1  853  ? 18.127  41.185  101.729 1.00 16.53 ? 851  CYS   B O     1 
ATOM   15181 C  CB    . CYS   B  1  853  ? 20.009  42.822  100.155 1.00 16.57 ? 851  CYS   B CB    1 
ATOM   15182 S  SG    . CYS   B  1  853  ? 20.940  43.169  98.664  1.00 18.96 ? 851  CYS   B SG    1 
ATOM   15183 N  N     . LEU   B  1  854  ? 19.912  40.813  103.035 1.00 17.30 ? 852  LEU   B N     1 
ATOM   15184 C  CA    . LEU   B  1  854  ? 19.133  40.346  104.165 1.00 17.05 ? 852  LEU   B CA    1 
ATOM   15185 C  C     . LEU   B  1  854  ? 19.197  41.376  105.273 1.00 16.74 ? 852  LEU   B C     1 
ATOM   15186 O  O     . LEU   B  1  854  ? 20.287  41.795  105.671 1.00 18.10 ? 852  LEU   B O     1 
ATOM   15187 C  CB    . LEU   B  1  854  ? 19.703  39.030  104.681 1.00 17.02 ? 852  LEU   B CB    1 
ATOM   15188 C  CG    . LEU   B  1  854  ? 19.737  37.908  103.654 1.00 16.69 ? 852  LEU   B CG    1 
ATOM   15189 C  CD1   . LEU   B  1  854  ? 20.441  36.717  104.277 1.00 17.06 ? 852  LEU   B CD1   1 
ATOM   15190 C  CD2   . LEU   B  1  854  ? 18.315  37.555  103.267 1.00 17.38 ? 852  LEU   B CD2   1 
ATOM   15191 N  N     . GLN   B  1  855  ? 18.036  41.760  105.784 1.00 16.60 ? 853  GLN   B N     1 
ATOM   15192 C  CA    . GLN   B  1  855  ? 18.030  42.635  106.940 1.00 17.22 ? 853  GLN   B CA    1 
ATOM   15193 C  C     . GLN   B  1  855  ? 18.800  41.951  108.057 1.00 19.19 ? 853  GLN   B C     1 
ATOM   15194 O  O     . GLN   B  1  855  ? 18.691  40.736  108.253 1.00 19.17 ? 853  GLN   B O     1 
ATOM   15195 C  CB    . GLN   B  1  855  ? 16.604  42.906  107.382 1.00 17.79 ? 853  GLN   B CB    1 
ATOM   15196 C  CG    . GLN   B  1  855  ? 16.520  44.060  108.366 1.00 21.07 ? 853  GLN   B CG    1 
ATOM   15197 C  CD    . GLN   B  1  855  ? 15.111  44.349  108.811 1.00 23.75 ? 853  GLN   B CD    1 
ATOM   15198 O  OE1   . GLN   B  1  855  ? 14.176  44.322  108.018 1.00 27.20 ? 853  GLN   B OE1   1 
ATOM   15199 N  NE2   . GLN   B  1  855  ? 14.949  44.641  110.093 1.00 25.99 ? 853  GLN   B NE2   1 
ATOM   15200 N  N     . GLU   B  1  856  ? 19.609  42.739  108.766 1.00 19.26 ? 854  GLU   B N     1 
ATOM   15201 C  CA    . GLU   B  1  856  ? 20.630  42.166  109.637 1.00 20.17 ? 854  GLU   B CA    1 
ATOM   15202 C  C     . GLU   B  1  856  ? 20.023  41.247  110.688 1.00 20.67 ? 854  GLU   B C     1 
ATOM   15203 O  O     . GLU   B  1  856  ? 20.620  40.226  111.047 1.00 23.57 ? 854  GLU   B O     1 
ATOM   15204 C  CB    . GLU   B  1  856  ? 21.428  43.292  110.298 1.00 24.55 ? 854  GLU   B CB    1 
ATOM   15205 N  N     . ASP   B  1  857  ? 18.831  41.588  111.184 1.00 22.23 ? 855  ASP   B N     1 
ATOM   15206 C  CA    . ASP   B  1  857  ? 18.234  40.850  112.295 1.00 23.84 ? 855  ASP   B CA    1 
ATOM   15207 C  C     . ASP   B  1  857  ? 17.748  39.461  111.901 1.00 22.89 ? 855  ASP   B C     1 
ATOM   15208 O  O     . ASP   B  1  857  ? 17.546  38.617  112.779 1.00 25.92 ? 855  ASP   B O     1 
ATOM   15209 C  CB    . ASP   B  1  857  ? 17.071  41.645  112.893 1.00 29.89 ? 855  ASP   B CB    1 
ATOM   15210 N  N     . VAL   B  1  858  ? 17.527  39.205  110.614 1.00 18.28 ? 856  VAL   B N     1 
ATOM   15211 C  CA    . VAL   B  1  858  ? 17.086  37.895  110.156 1.00 19.73 ? 856  VAL   B CA    1 
ATOM   15212 C  C     . VAL   B  1  858  ? 18.136  37.187  109.333 1.00 17.64 ? 856  VAL   B C     1 
ATOM   15213 O  O     . VAL   B  1  858  ? 17.910  36.039  108.922 1.00 19.46 ? 856  VAL   B O     1 
ATOM   15214 C  CB    . VAL   B  1  858  ? 15.751  37.961  109.391 1.00 20.28 ? 856  VAL   B CB    1 
ATOM   15215 C  CG1   . VAL   B  1  858  ? 14.625  38.388  110.322 1.00 24.52 ? 856  VAL   B CG1   1 
ATOM   15216 C  CG2   . VAL   B  1  858  ? 15.865  38.900  108.209 1.00 21.08 ? 856  VAL   B CG2   1 
ATOM   15217 N  N     . ALA   B  1  859  ? 19.286  37.820  109.096 1.00 18.26 ? 857  ALA   B N     1 
ATOM   15218 C  CA    . ALA   B  1  859  ? 20.258  37.281  108.149 1.00 20.32 ? 857  ALA   B CA    1 
ATOM   15219 C  C     . ALA   B  1  859  ? 20.753  35.905  108.572 1.00 18.95 ? 857  ALA   B C     1 
ATOM   15220 O  O     . ALA   B  1  859  ? 20.769  34.971  107.767 1.00 19.11 ? 857  ALA   B O     1 
ATOM   15221 C  CB    . ALA   B  1  859  ? 21.417  38.259  107.974 1.00 19.73 ? 857  ALA   B CB    1 
ATOM   15222 N  N     . ASP   B  1  860  ? 21.144  35.753  109.840 1.00 21.09 ? 858  ASP   B N     1 
ATOM   15223 C  CA    . ASP   B  1  860  ? 21.720  34.484  110.275 1.00 21.11 ? 858  ASP   B CA    1 
ATOM   15224 C  C     . ASP   B  1  860  ? 20.717  33.349  110.172 1.00 19.36 ? 858  ASP   B C     1 
ATOM   15225 O  O     . ASP   B  1  860  ? 21.059  32.256  109.704 1.00 19.60 ? 858  ASP   B O     1 
ATOM   15226 C  CB    . ASP   B  1  860  ? 22.252  34.591  111.704 1.00 19.11 ? 858  ASP   B CB    1 
ATOM   15227 C  CG    . ASP   B  1  860  ? 23.459  35.477  111.804 1.00 27.02 ? 858  ASP   B CG    1 
ATOM   15228 O  OD1   . ASP   B  1  860  ? 24.202  35.578  110.809 1.00 29.08 ? 858  ASP   B OD1   1 
ATOM   15229 O  OD2   . ASP   B  1  860  ? 23.664  36.074  112.878 1.00 32.46 ? 858  ASP   B OD2   1 
ATOM   15230 N  N     . ARG   B  1  861  ? 19.470  33.582  110.595 1.00 19.38 ? 859  ARG   B N     1 
ATOM   15231 C  CA    . ARG   B  1  861  ? 18.474  32.523  110.518 1.00 21.16 ? 859  ARG   B CA    1 
ATOM   15232 C  C     . ARG   B  1  861  ? 18.176  32.153  109.071 1.00 19.27 ? 859  ARG   B C     1 
ATOM   15233 O  O     . ARG   B  1  861  ? 18.051  30.971  108.738 1.00 19.62 ? 859  ARG   B O     1 
ATOM   15234 C  CB    . ARG   B  1  861  ? 17.193  32.919  111.255 1.00 25.84 ? 859  ARG   B CB    1 
ATOM   15235 C  CG    . ARG   B  1  861  ? 16.074  31.925  111.026 1.00 34.38 ? 859  ARG   B CG    1 
ATOM   15236 C  CD    . ARG   B  1  861  ? 15.076  31.881  112.161 1.00 40.16 ? 859  ARG   B CD    1 
ATOM   15237 N  NE    . ARG   B  1  861  ? 14.025  30.915  111.862 1.00 45.43 ? 859  ARG   B NE    1 
ATOM   15238 C  CZ    . ARG   B  1  861  ? 12.977  31.173  111.090 1.00 42.34 ? 859  ARG   B CZ    1 
ATOM   15239 N  NH1   . ARG   B  1  861  ? 12.794  32.369  110.551 1.00 40.18 ? 859  ARG   B NH1   1 
ATOM   15240 N  NH2   . ARG   B  1  861  ? 12.094  30.206  110.850 1.00 43.83 ? 859  ARG   B NH2   1 
ATOM   15241 N  N     . ILE   B  1  862  ? 18.078  33.146  108.191 1.00 16.34 ? 860  ILE   B N     1 
ATOM   15242 C  CA    . ILE   B  1  862  ? 17.831  32.829  106.786 1.00 17.89 ? 860  ILE   B CA    1 
ATOM   15243 C  C     . ILE   B  1  862  ? 19.010  32.084  106.170 1.00 16.14 ? 860  ILE   B C     1 
ATOM   15244 O  O     . ILE   B  1  862  ? 18.817  31.106  105.439 1.00 18.48 ? 860  ILE   B O     1 
ATOM   15245 C  CB    . ILE   B  1  862  ? 17.451  34.090  105.999 1.00 17.90 ? 860  ILE   B CB    1 
ATOM   15246 C  CG1   . ILE   B  1  862  ? 16.046  34.535  106.415 1.00 19.81 ? 860  ILE   B CG1   1 
ATOM   15247 C  CG2   . ILE   B  1  862  ? 17.526  33.829  104.490 1.00 17.94 ? 860  ILE   B CG2   1 
ATOM   15248 C  CD1   . ILE   B  1  862  ? 15.681  35.933  105.937 1.00 22.82 ? 860  ILE   B CD1   1 
ATOM   15249 N  N     . LEU   B  1  863  ? 20.239  32.509  106.466 1.00 17.28 ? 861  LEU   B N     1 
ATOM   15250 C  CA    . LEU   B  1  863  ? 21.396  31.843  105.875 1.00 18.65 ? 861  LEU   B CA    1 
ATOM   15251 C  C     . LEU   B  1  863  ? 21.542  30.423  106.402 1.00 19.24 ? 861  LEU   B C     1 
ATOM   15252 O  O     . LEU   B  1  863  ? 21.920  29.513  105.655 1.00 18.40 ? 861  LEU   B O     1 
ATOM   15253 C  CB    . LEU   B  1  863  ? 22.660  32.647  106.140 1.00 18.71 ? 861  LEU   B CB    1 
ATOM   15254 C  CG    . LEU   B  1  863  ? 22.726  33.967  105.396 1.00 20.93 ? 861  LEU   B CG    1 
ATOM   15255 C  CD1   . LEU   B  1  863  ? 23.844  34.813  105.979 1.00 24.69 ? 861  LEU   B CD1   1 
ATOM   15256 C  CD2   . LEU   B  1  863  ? 22.933  33.705  103.908 1.00 23.26 ? 861  LEU   B CD2   1 
ATOM   15257 N  N     . THR   B  1  864  ? 21.245  30.208  107.680 1.00 18.14 ? 862  THR   B N     1 
ATOM   15258 C  CA    . THR   B  1  864  ? 21.287  28.847  108.194 1.00 19.45 ? 862  THR   B CA    1 
ATOM   15259 C  C     . THR   B  1  864  ? 20.293  27.973  107.458 1.00 19.55 ? 862  THR   B C     1 
ATOM   15260 O  O     . THR   B  1  864  ? 20.600  26.835  107.085 1.00 19.81 ? 862  THR   B O     1 
ATOM   15261 C  CB    . THR   B  1  864  ? 20.993  28.852  109.691 1.00 23.58 ? 862  THR   B CB    1 
ATOM   15262 O  OG1   . THR   B  1  864  ? 22.068  29.494  110.378 1.00 24.77 ? 862  THR   B OG1   1 
ATOM   15263 C  CG2   . THR   B  1  864  ? 20.831  27.424  110.208 1.00 27.17 ? 862  THR   B CG2   1 
ATOM   15264 N  N     . MET   B  1  865  ? 19.092  28.498  107.221 1.00 18.20 ? 863  MET   B N     1 
ATOM   15265 C  CA    . MET   B  1  865  ? 18.070  27.716  106.550 1.00 17.48 ? 863  MET   B CA    1 
ATOM   15266 C  C     . MET   B  1  865  ? 18.438  27.485  105.092 1.00 17.26 ? 863  MET   B C     1 
ATOM   15267 O  O     . MET   B  1  865  ? 18.286  26.373  104.572 1.00 17.71 ? 863  MET   B O     1 
ATOM   15268 C  CB    . MET   B  1  865  ? 16.731  28.434  106.666 1.00 18.34 ? 863  MET   B CB    1 
ATOM   15269 C  CG    . MET   B  1  865  ? 15.586  27.658  106.085 1.00 20.40 ? 863  MET   B CG    1 
ATOM   15270 S  SD    . MET   B  1  865  ? 14.030  28.535  106.213 1.00 21.41 ? 863  MET   B SD    1 
ATOM   15271 C  CE    . MET   B  1  865  ? 13.878  28.669  107.997 1.00 24.96 ? 863  MET   B CE    1 
ATOM   15272 N  N     . LEU   B  1  866  ? 18.936  28.530  104.429 1.00 18.24 ? 864  LEU   B N     1 
ATOM   15273 C  CA    . LEU   B  1  866  ? 19.372  28.408  103.044 1.00 17.14 ? 864  LEU   B CA    1 
ATOM   15274 C  C     . LEU   B  1  866  ? 20.447  27.343  102.909 1.00 17.54 ? 864  LEU   B C     1 
ATOM   15275 O  O     . LEU   B  1  866  ? 20.377  26.486  102.025 1.00 17.37 ? 864  LEU   B O     1 
ATOM   15276 C  CB    . LEU   B  1  866  ? 19.904  29.757  102.573 1.00 17.96 ? 864  LEU   B CB    1 
ATOM   15277 C  CG    . LEU   B  1  866  ? 20.552  29.751  101.195 1.00 17.37 ? 864  LEU   B CG    1 
ATOM   15278 C  CD1   . LEU   B  1  866  ? 19.545  29.305  100.151 1.00 18.80 ? 864  LEU   B CD1   1 
ATOM   15279 C  CD2   . LEU   B  1  866  ? 21.064  31.152  100.903 1.00 20.42 ? 864  LEU   B CD2   1 
ATOM   15280 N  N     . LYS   B  1  867  ? 21.441  27.368  103.800 1.00 17.72 ? 865  LYS   B N     1 
ATOM   15281 C  CA    . LYS   B  1  867  ? 22.509  26.384  103.710 1.00 18.50 ? 865  LYS   B CA    1 
ATOM   15282 C  C     . LYS   B  1  867  ? 21.985  24.980  103.971 1.00 18.09 ? 865  LYS   B C     1 
ATOM   15283 O  O     . LYS   B  1  867  ? 22.387  24.029  103.294 1.00 18.11 ? 865  LYS   B O     1 
ATOM   15284 C  CB    . LYS   B  1  867  ? 23.653  26.760  104.653 1.00 18.52 ? 865  LYS   B CB    1 
ATOM   15285 C  CG    . LYS   B  1  867  ? 24.339  28.037  104.196 1.00 21.39 ? 865  LYS   B CG    1 
ATOM   15286 C  CD    . LYS   B  1  867  ? 25.255  28.618  105.243 1.00 25.82 ? 865  LYS   B CD    1 
ATOM   15287 C  CE    . LYS   B  1  867  ? 25.759  29.978  104.789 1.00 29.62 ? 865  LYS   B CE    1 
ATOM   15288 N  NZ    . LYS   B  1  867  ? 26.635  30.609  105.820 1.00 36.72 ? 865  LYS   B NZ    1 
ATOM   15289 N  N     . GLY   B  1  868  ? 21.057  24.835  104.920 1.00 18.84 ? 866  GLY   B N     1 
ATOM   15290 C  CA    . GLY   B  1  868  ? 20.463  23.529  105.143 1.00 19.00 ? 866  GLY   B CA    1 
ATOM   15291 C  C     . GLY   B  1  868  ? 19.701  23.041  103.929 1.00 17.78 ? 866  GLY   B C     1 
ATOM   15292 O  O     . GLY   B  1  868  ? 19.753  21.859  103.576 1.00 18.93 ? 866  GLY   B O     1 
ATOM   15293 N  N     . ALA   B  1  869  ? 18.984  23.947  103.267 1.00 18.59 ? 867  ALA   B N     1 
ATOM   15294 C  CA    . ALA   B  1  869  ? 18.269  23.578  102.055 1.00 19.10 ? 867  ALA   B CA    1 
ATOM   15295 C  C     . ALA   B  1  869  ? 19.240  23.238  100.931 1.00 17.18 ? 867  ALA   B C     1 
ATOM   15296 O  O     . ALA   B  1  869  ? 18.987  22.313  100.154 1.00 18.07 ? 867  ALA   B O     1 
ATOM   15297 C  CB    . ALA   B  1  869  ? 17.338  24.715  101.639 1.00 19.91 ? 867  ALA   B CB    1 
ATOM   15298 N  N     . LEU   B  1  870  ? 20.364  23.959  100.840 1.00 17.12 ? 868  LEU   B N     1 
ATOM   15299 C  CA    . LEU   B  1  870  ? 21.330  23.672  99.780  1.00 18.67 ? 868  LEU   B CA    1 
ATOM   15300 C  C     . LEU   B  1  870  ? 21.942  22.296  99.948  1.00 18.02 ? 868  LEU   B C     1 
ATOM   15301 O  O     . LEU   B  1  870  ? 22.275  21.642  98.958  1.00 18.91 ? 868  LEU   B O     1 
ATOM   15302 C  CB    . LEU   B  1  870  ? 22.438  24.721  99.759  1.00 18.38 ? 868  LEU   B CB    1 
ATOM   15303 C  CG    . LEU   B  1  870  ? 21.992  26.060  99.190  1.00 20.49 ? 868  LEU   B CG    1 
ATOM   15304 C  CD1   . LEU   B  1  870  ? 23.085  27.098  99.325  1.00 21.42 ? 868  LEU   B CD1   1 
ATOM   15305 C  CD2   . LEU   B  1  870  ? 21.585  25.886  97.722  1.00 22.07 ? 868  LEU   B CD2   1 
ATOM   15306 N  N     . HIS   B  1  871  ? 22.080  21.841  101.187 1.00 16.83 ? 869  HIS   B N     1 
ATOM   15307 C  CA    A HIS   B  1  871  ? 22.643  20.520  101.416 0.52 19.97 ? 869  HIS   B CA    1 
ATOM   15308 C  CA    B HIS   B  1  871  ? 22.621  20.519  101.465 0.48 19.97 ? 869  HIS   B CA    1 
ATOM   15309 C  C     . HIS   B  1  871  ? 21.749  19.406  100.902 1.00 19.85 ? 869  HIS   B C     1 
ATOM   15310 O  O     . HIS   B  1  871  ? 22.218  18.272  100.764 1.00 22.07 ? 869  HIS   B O     1 
ATOM   15311 C  CB    A HIS   B  1  871  ? 22.966  20.325  102.897 0.52 20.66 ? 869  HIS   B CB    1 
ATOM   15312 C  CB    B HIS   B  1  871  ? 22.762  20.349  102.978 0.48 20.39 ? 869  HIS   B CB    1 
ATOM   15313 C  CG    A HIS   B  1  871  ? 24.307  20.860  103.296 0.52 21.98 ? 869  HIS   B CG    1 
ATOM   15314 C  CG    B HIS   B  1  871  ? 23.362  19.041  103.382 0.48 21.15 ? 869  HIS   B CG    1 
ATOM   15315 N  ND1   A HIS   B  1  871  ? 24.471  22.101  103.874 0.52 23.17 ? 869  HIS   B ND1   1 
ATOM   15316 N  ND1   B HIS   B  1  871  ? 24.714  18.786  103.293 0.48 25.74 ? 869  HIS   B ND1   1 
ATOM   15317 C  CD2   A HIS   B  1  871  ? 25.549  20.330  103.185 0.52 24.39 ? 869  HIS   B CD2   1 
ATOM   15318 C  CD2   B HIS   B  1  871  ? 22.795  17.910  103.862 0.48 25.82 ? 869  HIS   B CD2   1 
ATOM   15319 C  CE1   A HIS   B  1  871  ? 25.753  22.305  104.115 0.52 24.98 ? 869  HIS   B CE1   1 
ATOM   15320 C  CE1   B HIS   B  1  871  ? 24.953  17.555  103.706 0.48 23.43 ? 869  HIS   B CE1   1 
ATOM   15321 N  NE2   A HIS   B  1  871  ? 26.428  21.249  103.701 0.52 23.91 ? 869  HIS   B NE2   1 
ATOM   15322 N  NE2   B HIS   B  1  871  ? 23.806  17.001  104.056 0.48 26.21 ? 869  HIS   B NE2   1 
ATOM   15323 N  N     . GLU   B  1  872  ? 20.494  19.698  100.591 1.00 18.13 ? 870  GLU   B N     1 
ATOM   15324 C  CA    . GLU   B  1  872  ? 19.573  18.695  100.090 1.00 17.02 ? 870  GLU   B CA    1 
ATOM   15325 C  C     . GLU   B  1  872  ? 19.505  18.648  98.575  1.00 17.59 ? 870  GLU   B C     1 
ATOM   15326 O  O     . GLU   B  1  872  ? 18.742  17.844  98.033  1.00 19.90 ? 870  GLU   B O     1 
ATOM   15327 C  CB    . GLU   B  1  872  ? 18.178  18.934  100.671 1.00 18.32 ? 870  GLU   B CB    1 
ATOM   15328 C  CG    . GLU   B  1  872  ? 18.193  18.940  102.182 1.00 19.84 ? 870  GLU   B CG    1 
ATOM   15329 C  CD    . GLU   B  1  872  ? 18.570  17.599  102.769 1.00 20.30 ? 870  GLU   B CD    1 
ATOM   15330 O  OE1   . GLU   B  1  872  ? 18.358  16.567  102.098 1.00 23.08 ? 870  GLU   B OE1   1 
ATOM   15331 O  OE2   . GLU   B  1  872  ? 19.072  17.567  103.908 1.00 21.92 ? 870  GLU   B OE2   1 
ATOM   15332 N  N     . LEU   B  1  873  ? 20.261  19.493  97.882  1.00 18.17 ? 871  LEU   B N     1 
ATOM   15333 C  CA    . LEU   B  1  873  ? 20.202  19.506  96.430  1.00 19.05 ? 871  LEU   B CA    1 
ATOM   15334 C  C     . LEU   B  1  873  ? 21.097  18.427  95.852  1.00 19.03 ? 871  LEU   B C     1 
ATOM   15335 O  O     . LEU   B  1  873  ? 22.164  18.114  96.387  1.00 19.93 ? 871  LEU   B O     1 
ATOM   15336 C  CB    . LEU   B  1  873  ? 20.658  20.855  95.887  1.00 18.11 ? 871  LEU   B CB    1 
ATOM   15337 C  CG    . LEU   B  1  873  ? 19.788  22.031  96.305  1.00 20.98 ? 871  LEU   B CG    1 
ATOM   15338 C  CD1   . LEU   B  1  873  ? 20.249  23.271  95.555  1.00 21.61 ? 871  LEU   B CD1   1 
ATOM   15339 C  CD2   . LEU   B  1  873  ? 18.316  21.746  96.047  1.00 20.75 ? 871  LEU   B CD2   1 
ATOM   15340 N  N     . HIS   B  1  874  ? 20.658  17.877  94.732  1.00 19.22 ? 872  HIS   B N     1 
ATOM   15341 C  CA    . HIS   B  1  874  ? 21.425  16.910  93.975  1.00 19.99 ? 872  HIS   B CA    1 
ATOM   15342 C  C     . HIS   B  1  874  ? 22.016  17.633  92.766  1.00 18.08 ? 872  HIS   B C     1 
ATOM   15343 O  O     . HIS   B  1  874  ? 21.276  18.175  91.942  1.00 17.43 ? 872  HIS   B O     1 
ATOM   15344 C  CB    . HIS   B  1  874  ? 20.492  15.778  93.553  1.00 20.49 ? 872  HIS   B CB    1 
ATOM   15345 C  CG    . HIS   B  1  874  ? 21.162  14.690  92.784  1.00 19.81 ? 872  HIS   B CG    1 
ATOM   15346 N  ND1   . HIS   B  1  874  ? 20.497  13.552  92.384  1.00 26.99 ? 872  HIS   B ND1   1 
ATOM   15347 C  CD2   . HIS   B  1  874  ? 22.430  14.569  92.324  1.00 21.72 ? 872  HIS   B CD2   1 
ATOM   15348 C  CE1   . HIS   B  1  874  ? 21.331  12.770  91.719  1.00 25.72 ? 872  HIS   B CE1   1 
ATOM   15349 N  NE2   . HIS   B  1  874  ? 22.509  13.364  91.669  1.00 26.57 ? 872  HIS   B NE2   1 
ATOM   15350 N  N     . ILE   B  1  875  ? 23.341  17.666  92.691  1.00 17.53 ? 873  ILE   B N     1 
ATOM   15351 C  CA    . ILE   B  1  875  ? 24.069  18.258  91.574  1.00 19.29 ? 873  ILE   B CA    1 
ATOM   15352 C  C     . ILE   B  1  875  ? 24.570  17.121  90.704  1.00 19.15 ? 873  ILE   B C     1 
ATOM   15353 O  O     . ILE   B  1  875  ? 25.209  16.192  91.205  1.00 19.79 ? 873  ILE   B O     1 
ATOM   15354 C  CB    . ILE   B  1  875  ? 25.268  19.073  92.075  1.00 21.66 ? 873  ILE   B CB    1 
ATOM   15355 C  CG1   . ILE   B  1  875  ? 24.832  20.156  93.056  1.00 24.35 ? 873  ILE   B CG1   1 
ATOM   15356 C  CG2   . ILE   B  1  875  ? 26.012  19.664  90.892  1.00 21.25 ? 873  ILE   B CG2   1 
ATOM   15357 C  CD1   . ILE   B  1  875  ? 25.978  20.658  93.903  1.00 27.66 ? 873  ILE   B CD1   1 
ATOM   15358 N  N     . GLY   B  1  876  ? 24.305  17.185  89.406  1.00 16.81 ? 874  GLY   B N     1 
ATOM   15359 C  CA    . GLY   B  1  876  ? 24.810  16.141  88.542  1.00 19.07 ? 874  GLY   B CA    1 
ATOM   15360 C  C     . GLY   B  1  876  ? 24.282  16.277  87.131  1.00 17.04 ? 874  GLY   B C     1 
ATOM   15361 O  O     . GLY   B  1  876  ? 23.667  17.279  86.762  1.00 17.39 ? 874  GLY   B O     1 
ATOM   15362 N  N     . ARG   B  1  877  ? 24.563  15.236  86.351  1.00 19.13 ? 875  ARG   B N     1 
ATOM   15363 C  CA    . ARG   B  1  877  ? 24.085  15.182  84.980  1.00 16.90 ? 875  ARG   B CA    1 
ATOM   15364 C  C     . ARG   B  1  877  ? 22.566  15.154  84.998  1.00 19.66 ? 875  ARG   B C     1 
ATOM   15365 O  O     . ARG   B  1  877  ? 21.960  14.422  85.781  1.00 20.09 ? 875  ARG   B O     1 
ATOM   15366 C  CB    . ARG   B  1  877  ? 24.637  13.932  84.307  1.00 20.69 ? 875  ARG   B CB    1 
ATOM   15367 C  CG    . ARG   B  1  877  ? 24.566  13.996  82.802  1.00 22.17 ? 875  ARG   B CG    1 
ATOM   15368 C  CD    . ARG   B  1  877  ? 25.224  12.792  82.197  1.00 28.31 ? 875  ARG   B CD    1 
ATOM   15369 N  NE    . ARG   B  1  877  ? 24.354  11.629  82.168  1.00 25.46 ? 875  ARG   B NE    1 
ATOM   15370 C  CZ    . ARG   B  1  877  ? 24.683  10.490  81.577  1.00 29.83 ? 875  ARG   B CZ    1 
ATOM   15371 N  NH1   . ARG   B  1  877  ? 25.884  10.313  81.048  1.00 28.58 ? 875  ARG   B NH1   1 
ATOM   15372 N  NH2   . ARG   B  1  877  ? 23.783  9.513   81.499  1.00 33.16 ? 875  ARG   B NH2   1 
ATOM   15373 N  N     . THR   B  1  878  ? 21.951  15.960  84.137  1.00 16.77 ? 876  THR   B N     1 
ATOM   15374 C  CA    . THR   B  1  878  ? 20.554  16.341  84.304  1.00 18.30 ? 876  THR   B CA    1 
ATOM   15375 C  C     . THR   B  1  878  ? 19.556  15.355  83.710  1.00 16.13 ? 876  THR   B C     1 
ATOM   15376 O  O     . THR   B  1  878  ? 18.350  15.633  83.724  1.00 18.40 ? 876  THR   B O     1 
ATOM   15377 C  CB    . THR   B  1  878  ? 20.326  17.735  83.729  1.00 18.44 ? 876  THR   B CB    1 
ATOM   15378 O  OG1   . THR   B  1  878  ? 20.869  17.799  82.405  1.00 20.40 ? 876  THR   B OG1   1 
ATOM   15379 C  CG2   . THR   B  1  878  ? 21.009  18.770  84.591  1.00 20.66 ? 876  THR   B CG2   1 
ATOM   15380 N  N     . ASP   B  1  879  ? 20.007  14.202  83.234  1.00 17.02 ? 877  ASP   B N     1 
ATOM   15381 C  CA    . ASP   B  1  879  ? 19.097  13.204  82.684  1.00 17.51 ? 877  ASP   B CA    1 
ATOM   15382 C  C     . ASP   B  1  879  ? 18.511  12.290  83.756  1.00 17.74 ? 877  ASP   B C     1 
ATOM   15383 O  O     . ASP   B  1  879  ? 18.166  11.141  83.476  1.00 20.04 ? 877  ASP   B O     1 
ATOM   15384 C  CB    . ASP   B  1  879  ? 19.770  12.404  81.569  1.00 21.28 ? 877  ASP   B CB    1 
ATOM   15385 C  CG    . ASP   B  1  879  ? 20.955  11.586  82.062  1.00 22.06 ? 877  ASP   B CG    1 
ATOM   15386 O  OD1   . ASP   B  1  879  ? 21.632  11.997  83.029  1.00 23.97 ? 877  ASP   B OD1   1 
ATOM   15387 O  OD2   . ASP   B  1  879  ? 21.200  10.514  81.481  1.00 23.86 ? 877  ASP   B OD2   1 
ATOM   15388 N  N     . ARG   B  1  880  ? 18.412  12.788  84.982  1.00 19.56 ? 878  ARG   B N     1 
ATOM   15389 C  CA    . ARG   B  1  880  ? 17.703  12.110  86.059  1.00 19.34 ? 878  ARG   B CA    1 
ATOM   15390 C  C     . ARG   B  1  880  ? 16.779  13.133  86.686  1.00 18.60 ? 878  ARG   B C     1 
ATOM   15391 O  O     . ARG   B  1  880  ? 17.202  14.259  86.969  1.00 18.40 ? 878  ARG   B O     1 
ATOM   15392 C  CB    . ARG   B  1  880  ? 18.666  11.612  87.144  1.00 21.29 ? 878  ARG   B CB    1 
ATOM   15393 C  CG    . ARG   B  1  880  ? 19.539  10.431  86.759  1.00 26.80 ? 878  ARG   B CG    1 
ATOM   15394 C  CD    . ARG   B  1  880  ? 20.427  10.015  87.937  1.00 31.30 ? 878  ARG   B CD    1 
ATOM   15395 N  NE    . ARG   B  1  880  ? 21.370  8.968   87.563  1.00 45.73 ? 878  ARG   B NE    1 
ATOM   15396 C  CZ    . ARG   B  1  880  ? 21.230  7.686   87.871  1.00 47.83 ? 878  ARG   B CZ    1 
ATOM   15397 N  NH1   . ARG   B  1  880  ? 20.208  7.256   88.596  1.00 50.07 ? 878  ARG   B NH1   1 
ATOM   15398 N  NH2   . ARG   B  1  880  ? 22.137  6.812   87.440  1.00 48.83 ? 878  ARG   B NH2   1 
ATOM   15399 N  N     . LEU   B  1  881  ? 15.518  12.740  86.890  1.00 18.24 ? 879  LEU   B N     1 
ATOM   15400 C  CA    . LEU   B  1  881  ? 14.548  13.628  87.523  1.00 19.12 ? 879  LEU   B CA    1 
ATOM   15401 C  C     . LEU   B  1  881  ? 15.020  14.113  88.887  1.00 16.17 ? 879  LEU   B C     1 
ATOM   15402 O  O     . LEU   B  1  881  ? 14.713  15.242  89.292  1.00 17.26 ? 879  LEU   B O     1 
ATOM   15403 C  CB    . LEU   B  1  881  ? 13.222  12.897  87.664  1.00 18.40 ? 879  LEU   B CB    1 
ATOM   15404 C  CG    . LEU   B  1  881  ? 12.058  13.708  88.226  1.00 20.29 ? 879  LEU   B CG    1 
ATOM   15405 C  CD1   . LEU   B  1  881  ? 11.694  14.852  87.292  1.00 22.39 ? 879  LEU   B CD1   1 
ATOM   15406 C  CD2   . LEU   B  1  881  ? 10.871  12.789  88.457  1.00 20.03 ? 879  LEU   B CD2   1 
ATOM   15407 N  N     . SER   B  1  882  ? 15.799  13.299  89.596  1.00 16.20 ? 880  SER   B N     1 
ATOM   15408 C  CA    . SER   B  1  882  ? 16.249  13.672  90.926  1.00 16.71 ? 880  SER   B CA    1 
ATOM   15409 C  C     . SER   B  1  882  ? 17.323  14.752  90.927  1.00 19.05 ? 880  SER   B C     1 
ATOM   15410 O  O     . SER   B  1  882  ? 17.714  15.192  92.008  1.00 19.85 ? 880  SER   B O     1 
ATOM   15411 C  CB    . SER   B  1  882  ? 16.789  12.442  91.652  1.00 19.78 ? 880  SER   B CB    1 
ATOM   15412 O  OG    . SER   B  1  882  ? 17.990  12.012  91.031  1.00 24.50 ? 880  SER   B OG    1 
ATOM   15413 N  N     . VAL   B  1  883  ? 17.809  15.202  89.775  1.00 17.65 ? 881  VAL   B N     1 
ATOM   15414 C  CA    . VAL   B  1  883  ? 18.885  16.189  89.751  1.00 19.78 ? 881  VAL   B CA    1 
ATOM   15415 C  C     . VAL   B  1  883  ? 18.298  17.588  89.811  1.00 18.00 ? 881  VAL   B C     1 
ATOM   15416 O  O     . VAL   B  1  883  ? 17.399  17.933  89.033  1.00 19.94 ? 881  VAL   B O     1 
ATOM   15417 C  CB    . VAL   B  1  883  ? 19.778  16.006  88.520  1.00 20.04 ? 881  VAL   B CB    1 
ATOM   15418 C  CG1   . VAL   B  1  883  ? 20.676  17.224  88.353  1.00 20.50 ? 881  VAL   B CG1   1 
ATOM   15419 C  CG2   . VAL   B  1  883  ? 20.594  14.756  88.694  1.00 20.29 ? 881  VAL   B CG2   1 
ATOM   15420 N  N     . ASP   B  1  884  ? 18.787  18.384  90.752  1.00 18.01 ? 882  ASP   B N     1 
ATOM   15421 C  CA    . ASP   B  1  884  ? 18.318  19.742  90.969  1.00 19.20 ? 882  ASP   B CA    1 
ATOM   15422 C  C     . ASP   B  1  884  ? 19.162  20.777  90.248  1.00 20.76 ? 882  ASP   B C     1 
ATOM   15423 O  O     . ASP   B  1  884  ? 18.607  21.716  89.668  1.00 24.67 ? 882  ASP   B O     1 
ATOM   15424 C  CB    . ASP   B  1  884  ? 18.327  20.042  92.465  1.00 19.84 ? 882  ASP   B CB    1 
ATOM   15425 C  CG    . ASP   B  1  884  ? 17.474  19.073  93.236  1.00 20.23 ? 882  ASP   B CG    1 
ATOM   15426 O  OD1   . ASP   B  1  884  ? 16.273  18.960  92.899  1.00 19.99 ? 882  ASP   B OD1   1 
ATOM   15427 O  OD2   . ASP   B  1  884  ? 18.008  18.404  94.146  1.00 19.28 ? 882  ASP   B OD2   1 
ATOM   15428 N  N     . VAL   B  1  885  ? 20.482  20.611  90.258  1.00 18.35 ? 883  VAL   B N     1 
ATOM   15429 C  CA    . VAL   B  1  885  ? 21.424  21.595  89.740  1.00 18.27 ? 883  VAL   B CA    1 
ATOM   15430 C  C     . VAL   B  1  885  ? 22.301  20.881  88.725  1.00 18.12 ? 883  VAL   B C     1 
ATOM   15431 O  O     . VAL   B  1  885  ? 22.956  19.883  89.055  1.00 17.83 ? 883  VAL   B O     1 
ATOM   15432 C  CB    . VAL   B  1  885  ? 22.291  22.194  90.859  1.00 18.91 ? 883  VAL   B CB    1 
ATOM   15433 C  CG1   . VAL   B  1  885  ? 23.274  23.197  90.285  1.00 20.76 ? 883  VAL   B CG1   1 
ATOM   15434 C  CG2   . VAL   B  1  885  ? 21.421  22.844  91.936  1.00 24.17 ? 883  VAL   B CG2   1 
ATOM   15435 N  N     . GLY   B  1  886  ? 22.303  21.382  87.497  1.00 17.32 ? 884  GLY   B N     1 
ATOM   15436 C  CA    . GLY   B  1  886  ? 23.120  20.823  86.457  1.00 17.02 ? 884  GLY   B CA    1 
ATOM   15437 C  C     . GLY   B  1  886  ? 24.466  21.498  86.342  1.00 16.75 ? 884  GLY   B C     1 
ATOM   15438 O  O     . GLY   B  1  886  ? 24.884  22.289  87.192  1.00 17.31 ? 884  GLY   B O     1 
ATOM   15439 N  N     . PRO   B  1  887  ? 25.163  21.182  85.263  1.00 15.54 ? 885  PRO   B N     1 
ATOM   15440 C  CA    . PRO   B  1  887  ? 26.524  21.679  85.057  1.00 13.93 ? 885  PRO   B CA    1 
ATOM   15441 C  C     . PRO   B  1  887  ? 26.534  23.123  84.580  1.00 15.08 ? 885  PRO   B C     1 
ATOM   15442 O  O     . PRO   B  1  887  ? 25.542  23.672  84.099  1.00 16.00 ? 885  PRO   B O     1 
ATOM   15443 C  CB    . PRO   B  1  887  ? 27.022  20.775  83.932  1.00 16.31 ? 885  PRO   B CB    1 
ATOM   15444 C  CG    . PRO   B  1  887  ? 25.773  20.452  83.153  1.00 16.35 ? 885  PRO   B CG    1 
ATOM   15445 C  CD    . PRO   B  1  887  ? 24.725  20.269  84.196  1.00 15.94 ? 885  PRO   B CD    1 
ATOM   15446 N  N     . VAL   B  1  888  ? 27.707  23.718  84.663  1.00 16.09 ? 886  VAL   B N     1 
ATOM   15447 C  CA    . VAL   B  1  888  ? 27.945  24.933  83.905  1.00 16.80 ? 886  VAL   B CA    1 
ATOM   15448 C  C     . VAL   B  1  888  ? 28.322  24.552  82.479  1.00 15.72 ? 886  VAL   B C     1 
ATOM   15449 O  O     . VAL   B  1  888  ? 28.735  23.423  82.198  1.00 15.96 ? 886  VAL   B O     1 
ATOM   15450 C  CB    . VAL   B  1  888  ? 28.987  25.857  84.563  1.00 18.58 ? 886  VAL   B CB    1 
ATOM   15451 C  CG1   . VAL   B  1  888  ? 28.505  26.264  85.959  1.00 17.51 ? 886  VAL   B CG1   1 
ATOM   15452 C  CG2   . VAL   B  1  888  ? 30.334  25.204  84.646  1.00 23.44 ? 886  VAL   B CG2   1 
ATOM   15453 N  N     . ILE   B  1  889  ? 28.112  25.490  81.559  1.00 15.99 ? 887  ILE   B N     1 
ATOM   15454 C  CA    . ILE   B  1  889  ? 28.026  25.109  80.148  1.00 15.83 ? 887  ILE   B CA    1 
ATOM   15455 C  C     . ILE   B  1  889  ? 29.367  24.667  79.565  1.00 16.38 ? 887  ILE   B C     1 
ATOM   15456 O  O     . ILE   B  1  889  ? 29.408  23.779  78.709  1.00 16.17 ? 887  ILE   B O     1 
ATOM   15457 C  CB    . ILE   B  1  889  ? 27.379  26.235  79.335  1.00 16.72 ? 887  ILE   B CB    1 
ATOM   15458 C  CG1   . ILE   B  1  889  ? 27.150  25.788  77.890  1.00 18.41 ? 887  ILE   B CG1   1 
ATOM   15459 C  CG2   . ILE   B  1  889  ? 28.231  27.500  79.399  1.00 18.84 ? 887  ILE   B CG2   1 
ATOM   15460 C  CD1   . ILE   B  1  889  ? 26.241  24.588  77.756  1.00 17.70 ? 887  ILE   B CD1   1 
ATOM   15461 N  N     . THR   B  1  890  ? 30.479  25.257  79.998  1.00 15.84 ? 888  THR   B N     1 
ATOM   15462 C  CA    . THR   B  1  890  ? 31.771  24.922  79.418  1.00 16.92 ? 888  THR   B CA    1 
ATOM   15463 C  C     . THR   B  1  890  ? 32.833  25.004  80.492  1.00 17.60 ? 888  THR   B C     1 
ATOM   15464 O  O     . THR   B  1  890  ? 32.637  25.610  81.547  1.00 16.93 ? 888  THR   B O     1 
ATOM   15465 C  CB    . THR   B  1  890  ? 32.220  25.913  78.329  1.00 18.06 ? 888  THR   B CB    1 
ATOM   15466 O  OG1   . THR   B  1  890  ? 32.221  27.246  78.856  1.00 19.57 ? 888  THR   B OG1   1 
ATOM   15467 C  CG2   . THR   B  1  890  ? 31.319  25.842  77.095  1.00 20.42 ? 888  THR   B CG2   1 
ATOM   15468 N  N     . SER   B  1  891  ? 33.983  24.418  80.182  1.00 18.56 ? 889  SER   B N     1 
ATOM   15469 C  CA    A SER   B  1  891  ? 35.143  24.564  81.057  0.41 17.93 ? 889  SER   B CA    1 
ATOM   15470 C  CA    B SER   B  1  891  ? 35.128  24.564  81.070  0.35 17.93 ? 889  SER   B CA    1 
ATOM   15471 C  CA    C SER   B  1  891  ? 35.131  24.564  81.068  0.24 17.96 ? 889  SER   B CA    1 
ATOM   15472 C  C     . SER   B  1  891  ? 35.547  26.025  81.181  1.00 17.50 ? 889  SER   B C     1 
ATOM   15473 O  O     . SER   B  1  891  ? 35.970  26.474  82.252  1.00 19.23 ? 889  SER   B O     1 
ATOM   15474 C  CB    A SER   B  1  891  ? 36.317  23.743  80.519  0.41 20.84 ? 889  SER   B CB    1 
ATOM   15475 C  CB    B SER   B  1  891  ? 36.289  23.694  80.587  0.35 20.85 ? 889  SER   B CB    1 
ATOM   15476 C  CB    C SER   B  1  891  ? 36.295  23.705  80.574  0.24 20.85 ? 889  SER   B CB    1 
ATOM   15477 O  OG    A SER   B  1  891  ? 36.042  22.357  80.559  0.41 20.70 ? 889  SER   B OG    1 
ATOM   15478 O  OG    B SER   B  1  891  ? 36.742  24.115  79.316  0.35 20.35 ? 889  SER   B OG    1 
ATOM   15479 O  OG    C SER   B  1  891  ? 37.387  23.768  81.476  0.24 22.87 ? 889  SER   B OG    1 
ATOM   15480 N  N     . GLU   B  1  892  ? 35.428  26.783  80.086  1.00 16.99 ? 890  GLU   B N     1 
ATOM   15481 C  CA    . GLU   B  1  892  ? 35.753  28.203  80.129  1.00 19.07 ? 890  GLU   B CA    1 
ATOM   15482 C  C     . GLU   B  1  892  ? 34.842  28.942  81.096  1.00 18.95 ? 890  GLU   B C     1 
ATOM   15483 O  O     . GLU   B  1  892  ? 35.310  29.767  81.889  1.00 19.52 ? 890  GLU   B O     1 
ATOM   15484 C  CB    . GLU   B  1  892  ? 35.641  28.816  78.732  1.00 23.16 ? 890  GLU   B CB    1 
ATOM   15485 N  N     . ALA   B  1  893  ? 33.538  28.662  81.046  1.00 18.48 ? 891  ALA   B N     1 
ATOM   15486 C  CA    . ALA   B  1  893  ? 32.618  29.278  81.994  1.00 17.48 ? 891  ALA   B CA    1 
ATOM   15487 C  C     . ALA   B  1  893  ? 32.991  28.897  83.418  1.00 17.54 ? 891  ALA   B C     1 
ATOM   15488 O  O     . ALA   B  1  893  ? 33.029  29.749  84.314  1.00 18.11 ? 891  ALA   B O     1 
ATOM   15489 C  CB    . ALA   B  1  893  ? 31.183  28.855  81.676  1.00 18.53 ? 891  ALA   B CB    1 
ATOM   15490 N  N     . LYS   B  1  894  ? 33.270  27.613  83.641  1.00 17.14 ? 892  LYS   B N     1 
ATOM   15491 C  CA    . LYS   B  1  894  ? 33.657  27.153  84.969  1.00 16.91 ? 892  LYS   B CA    1 
ATOM   15492 C  C     . LYS   B  1  894  ? 34.881  27.906  85.471  1.00 17.27 ? 892  LYS   B C     1 
ATOM   15493 O  O     . LYS   B  1  894  ? 34.909  28.387  86.608  1.00 19.85 ? 892  LYS   B O     1 
ATOM   15494 C  CB    . LYS   B  1  894  ? 33.918  25.649  84.933  1.00 18.82 ? 892  LYS   B CB    1 
ATOM   15495 C  CG    . LYS   B  1  894  ? 34.384  25.044  86.234  1.00 18.68 ? 892  LYS   B CG    1 
ATOM   15496 C  CD    . LYS   B  1  894  ? 34.513  23.543  86.041  1.00 23.37 ? 892  LYS   B CD    1 
ATOM   15497 C  CE    . LYS   B  1  894  ? 35.447  22.915  87.053  1.00 30.99 ? 892  LYS   B CE    1 
ATOM   15498 N  NZ    . LYS   B  1  894  ? 34.811  22.745  88.372  1.00 34.31 ? 892  LYS   B NZ    1 
ATOM   15499 N  N     . ASP   B  1  895  ? 35.896  28.049  84.618  1.00 17.92 ? 893  ASP   B N     1 
ATOM   15500 C  CA    . ASP   B  1  895  ? 37.097  28.771  85.022  1.00 19.38 ? 893  ASP   B CA    1 
ATOM   15501 C  C     . ASP   B  1  895  ? 36.788  30.228  85.331  1.00 18.05 ? 893  ASP   B C     1 
ATOM   15502 O  O     . ASP   B  1  895  ? 37.351  30.805  86.269  1.00 20.17 ? 893  ASP   B O     1 
ATOM   15503 C  CB    . ASP   B  1  895  ? 38.152  28.688  83.921  1.00 21.56 ? 893  ASP   B CB    1 
ATOM   15504 C  CG    . ASP   B  1  895  ? 38.686  27.296  83.735  1.00 23.73 ? 893  ASP   B CG    1 
ATOM   15505 O  OD1   . ASP   B  1  895  ? 38.526  26.458  84.648  1.00 25.10 ? 893  ASP   B OD1   1 
ATOM   15506 O  OD2   . ASP   B  1  895  ? 39.284  27.048  82.671  1.00 27.87 ? 893  ASP   B OD2   1 
ATOM   15507 N  N     . ASN   B  1  896  ? 35.912  30.840  84.539  1.00 18.74 ? 894  ASN   B N     1 
ATOM   15508 C  CA    . ASN   B  1  896  ? 35.541  32.230  84.755  1.00 19.48 ? 894  ASN   B CA    1 
ATOM   15509 C  C     . ASN   B  1  896  ? 34.873  32.388  86.118  1.00 20.70 ? 894  ASN   B C     1 
ATOM   15510 O  O     . ASN   B  1  896  ? 35.233  33.267  86.914  1.00 20.34 ? 894  ASN   B O     1 
ATOM   15511 C  CB    . ASN   B  1  896  ? 34.608  32.620  83.604  1.00 19.68 ? 894  ASN   B CB    1 
ATOM   15512 C  CG    . ASN   B  1  896  ? 34.132  34.049  83.666  1.00 27.19 ? 894  ASN   B CG    1 
ATOM   15513 O  OD1   . ASN   B  1  896  ? 33.617  34.511  84.679  1.00 28.47 ? 894  ASN   B OD1   1 
ATOM   15514 N  ND2   . ASN   B  1  896  ? 34.261  34.752  82.546  1.00 32.06 ? 894  ASN   B ND2   1 
ATOM   15515 N  N     . ILE   B  1  897  ? 33.919  31.509  86.415  1.00 17.39 ? 895  ILE   B N     1 
ATOM   15516 C  CA    . ILE   B  1  897  ? 33.227  31.558  87.695  1.00 17.76 ? 895  ILE   B CA    1 
ATOM   15517 C  C     . ILE   B  1  897  ? 34.206  31.302  88.831  1.00 17.71 ? 895  ILE   B C     1 
ATOM   15518 O  O     . ILE   B  1  897  ? 34.210  32.008  89.848  1.00 17.10 ? 895  ILE   B O     1 
ATOM   15519 C  CB    . ILE   B  1  897  ? 32.093  30.521  87.701  1.00 16.90 ? 895  ILE   B CB    1 
ATOM   15520 C  CG1   . ILE   B  1  897  ? 31.035  30.855  86.653  1.00 17.94 ? 895  ILE   B CG1   1 
ATOM   15521 C  CG2   . ILE   B  1  897  ? 31.479  30.437  89.088  1.00 17.11 ? 895  ILE   B CG2   1 
ATOM   15522 C  CD1   . ILE   B  1  897  ? 30.226  29.639  86.227  1.00 17.70 ? 895  ILE   B CD1   1 
ATOM   15523 N  N     . GLU   B  1  898  ? 35.042  30.279  88.677  1.00 17.86 ? 896  GLU   B N     1 
ATOM   15524 C  CA    . GLU   B  1  898  ? 35.988  29.941  89.728  1.00 17.86 ? 896  GLU   B CA    1 
ATOM   15525 C  C     . GLU   B  1  898  ? 37.014  31.040  89.948  1.00 20.06 ? 896  GLU   B C     1 
ATOM   15526 O  O     . GLU   B  1  898  ? 37.464  31.240  91.079  1.00 19.15 ? 896  GLU   B O     1 
ATOM   15527 C  CB    . GLU   B  1  898  ? 36.636  28.593  89.434  1.00 20.14 ? 896  GLU   B CB    1 
ATOM   15528 C  CG    . GLU   B  1  898  ? 35.634  27.457  89.618  1.00 22.32 ? 896  GLU   B CG    1 
ATOM   15529 C  CD    . GLU   B  1  898  ? 36.210  26.099  89.293  1.00 29.37 ? 896  GLU   B CD    1 
ATOM   15530 O  OE1   . GLU   B  1  898  ? 37.310  26.037  88.711  1.00 31.56 ? 896  GLU   B OE1   1 
ATOM   15531 O  OE2   . GLU   B  1  898  ? 35.554  25.090  89.624  1.00 35.80 ? 896  GLU   B OE2   1 
ATOM   15532 N  N     . LYS   B  1  899  ? 37.373  31.782  88.898  1.00 17.90 ? 897  LYS   B N     1 
ATOM   15533 C  CA    . LYS   B  1  899  ? 38.302  32.887  89.087  1.00 20.22 ? 897  LYS   B CA    1 
ATOM   15534 C  C     . LYS   B  1  899  ? 37.689  33.935  89.998  1.00 19.04 ? 897  LYS   B C     1 
ATOM   15535 O  O     . LYS   B  1  899  ? 38.365  34.487  90.875  1.00 18.87 ? 897  LYS   B O     1 
ATOM   15536 C  CB    . LYS   B  1  899  ? 38.658  33.516  87.744  1.00 21.85 ? 897  LYS   B CB    1 
ATOM   15537 C  CG    . LYS   B  1  899  ? 39.640  34.660  87.908  1.00 23.02 ? 897  LYS   B CG    1 
ATOM   15538 C  CD    . LYS   B  1  899  ? 40.237  35.105  86.589  1.00 30.88 ? 897  LYS   B CD    1 
ATOM   15539 C  CE    . LYS   B  1  899  ? 39.244  35.900  85.773  1.00 29.40 ? 897  LYS   B CE    1 
ATOM   15540 N  NZ    . LYS   B  1  899  ? 39.940  36.726  84.737  1.00 29.03 ? 897  LYS   B NZ    1 
ATOM   15541 N  N     . HIS   B  1  900  ? 36.401  34.200  89.822  1.00 17.37 ? 898  HIS   B N     1 
ATOM   15542 C  CA    . HIS   B  1  900  ? 35.735  35.157  90.687  1.00 17.38 ? 898  HIS   B CA    1 
ATOM   15543 C  C     . HIS   B  1  900  ? 35.698  34.650  92.119  1.00 17.86 ? 898  HIS   B C     1 
ATOM   15544 O  O     . HIS   B  1  900  ? 35.997  35.392  93.060  1.00 19.39 ? 898  HIS   B O     1 
ATOM   15545 C  CB    . HIS   B  1  900  ? 34.320  35.389  90.188  1.00 16.80 ? 898  HIS   B CB    1 
ATOM   15546 C  CG    . HIS   B  1  900  ? 33.485  36.146  91.156  1.00 17.63 ? 898  HIS   B CG    1 
ATOM   15547 N  ND1   . HIS   B  1  900  ? 33.677  37.486  91.403  1.00 22.14 ? 898  HIS   B ND1   1 
ATOM   15548 C  CD2   . HIS   B  1  900  ? 32.457  35.754  91.947  1.00 18.59 ? 898  HIS   B CD2   1 
ATOM   15549 C  CE1   . HIS   B  1  900  ? 32.793  37.892  92.299  1.00 19.55 ? 898  HIS   B CE1   1 
ATOM   15550 N  NE2   . HIS   B  1  900  ? 32.053  36.859  92.654  1.00 19.04 ? 898  HIS   B NE2   1 
ATOM   15551 N  N     . ILE   B  1  901  ? 35.316  33.386  92.297  1.00 17.52 ? 899  ILE   B N     1 
ATOM   15552 C  CA    . ILE   B  1  901  ? 35.230  32.814  93.635  1.00 17.84 ? 899  ILE   B CA    1 
ATOM   15553 C  C     . ILE   B  1  901  ? 36.571  32.921  94.333  1.00 18.90 ? 899  ILE   B C     1 
ATOM   15554 O  O     . ILE   B  1  901  ? 36.662  33.362  95.485  1.00 19.45 ? 899  ILE   B O     1 
ATOM   15555 C  CB    . ILE   B  1  901  ? 34.756  31.357  93.557  1.00 16.55 ? 899  ILE   B CB    1 
ATOM   15556 C  CG1   . ILE   B  1  901  ? 33.329  31.300  93.012  1.00 16.51 ? 899  ILE   B CG1   1 
ATOM   15557 C  CG2   . ILE   B  1  901  ? 34.815  30.720  94.927  1.00 20.08 ? 899  ILE   B CG2   1 
ATOM   15558 C  CD1   . ILE   B  1  901  ? 32.863  29.888  92.745  1.00 19.53 ? 899  ILE   B CD1   1 
ATOM   15559 N  N     . GLU   B  1  902  ? 37.636  32.549  93.627  1.00 18.60 ? 900  GLU   B N     1 
ATOM   15560 C  CA    . GLU   B  1  902  ? 38.965  32.599  94.215  1.00 20.02 ? 900  GLU   B CA    1 
ATOM   15561 C  C     . GLU   B  1  902  ? 39.401  34.028  94.474  1.00 19.83 ? 900  GLU   B C     1 
ATOM   15562 O  O     . GLU   B  1  902  ? 40.117  34.280  95.446  1.00 21.22 ? 900  GLU   B O     1 
ATOM   15563 C  CB    . GLU   B  1  902  ? 39.961  31.859  93.320  1.00 20.90 ? 900  GLU   B CB    1 
ATOM   15564 C  CG    . GLU   B  1  902  ? 39.749  30.343  93.306  1.00 26.68 ? 900  GLU   B CG    1 
ATOM   15565 C  CD    . GLU   B  1  902  ? 39.533  29.756  94.703  1.00 33.71 ? 900  GLU   B CD    1 
ATOM   15566 O  OE1   . GLU   B  1  902  ? 40.346  30.037  95.613  1.00 33.09 ? 900  GLU   B OE1   1 
ATOM   15567 O  OE2   . GLU   B  1  902  ? 38.545  29.012  94.888  1.00 36.20 ? 900  GLU   B OE2   1 
ATOM   15568 N  N     . ARG   B  1  903  ? 39.001  34.976  93.625  1.00 20.77 ? 901  ARG   B N     1 
ATOM   15569 C  CA    A ARG   B  1  903  ? 39.329  36.372  93.896  0.41 22.43 ? 901  ARG   B CA    1 
ATOM   15570 C  CA    B ARG   B  1  903  ? 39.331  36.370  93.898  0.59 22.42 ? 901  ARG   B CA    1 
ATOM   15571 C  C     . ARG   B  1  903  ? 38.656  36.848  95.175  1.00 24.83 ? 901  ARG   B C     1 
ATOM   15572 O  O     . ARG   B  1  903  ? 39.285  37.505  96.012  1.00 24.48 ? 901  ARG   B O     1 
ATOM   15573 C  CB    A ARG   B  1  903  ? 38.925  37.256  92.717  0.41 24.91 ? 901  ARG   B CB    1 
ATOM   15574 C  CB    B ARG   B  1  903  ? 38.938  37.254  92.719  0.59 24.90 ? 901  ARG   B CB    1 
ATOM   15575 C  CG    A ARG   B  1  903  ? 39.398  38.695  92.855  0.41 30.39 ? 901  ARG   B CG    1 
ATOM   15576 C  CG    B ARG   B  1  903  ? 39.058  38.727  93.039  0.59 30.30 ? 901  ARG   B CG    1 
ATOM   15577 C  CD    A ARG   B  1  903  ? 39.020  39.526  91.639  0.41 32.66 ? 901  ARG   B CD    1 
ATOM   15578 C  CD    B ARG   B  1  903  ? 39.273  39.563  91.794  0.59 33.01 ? 901  ARG   B CD    1 
ATOM   15579 N  NE    A ARG   B  1  903  ? 37.644  40.005  91.689  0.41 33.05 ? 901  ARG   B NE    1 
ATOM   15580 N  NE    B ARG   B  1  903  ? 39.628  40.929  92.154  0.59 33.19 ? 901  ARG   B NE    1 
ATOM   15581 C  CZ    A ARG   B  1  903  ? 37.276  41.171  92.202  0.41 31.99 ? 901  ARG   B CZ    1 
ATOM   15582 C  CZ    B ARG   B  1  903  ? 38.759  41.834  92.580  0.59 33.76 ? 901  ARG   B CZ    1 
ATOM   15583 N  NH1   A ARG   B  1  903  ? 38.153  41.986  92.764  0.41 35.86 ? 901  ARG   B NH1   1 
ATOM   15584 N  NH1   B ARG   B  1  903  ? 37.468  41.557  92.690  0.59 32.97 ? 901  ARG   B NH1   1 
ATOM   15585 N  NH2   A ARG   B  1  903  ? 35.994  41.528  92.151  0.41 32.65 ? 901  ARG   B NH2   1 
ATOM   15586 N  NH2   B ARG   B  1  903  ? 39.194  43.047  92.905  0.59 30.85 ? 901  ARG   B NH2   1 
ATOM   15587 N  N     . MET   B  1  904  ? 37.376  36.518  95.346  1.00 21.45 ? 902  MET   B N     1 
ATOM   15588 C  CA    . MET   B  1  904  ? 36.692  36.856  96.587  1.00 20.37 ? 902  MET   B CA    1 
ATOM   15589 C  C     . MET   B  1  904  ? 37.355  36.175  97.775  1.00 22.72 ? 902  MET   B C     1 
ATOM   15590 O  O     . MET   B  1  904  ? 37.556  36.798  98.825  1.00 22.48 ? 902  MET   B O     1 
ATOM   15591 C  CB    . MET   B  1  904  ? 35.231  36.438  96.494  1.00 21.24 ? 902  MET   B CB    1 
ATOM   15592 C  CG    . MET   B  1  904  ? 34.459  37.127  95.384  1.00 21.66 ? 902  MET   B CG    1 
ATOM   15593 S  SD    . MET   B  1  904  ? 34.336  38.898  95.708  1.00 30.06 ? 902  MET   B SD    1 
ATOM   15594 C  CE    . MET   B  1  904  ? 35.531  39.538  94.561  1.00 30.96 ? 902  MET   B CE    1 
ATOM   15595 N  N     . ARG   B  1  905  ? 37.702  34.898  97.631  1.00 20.65 ? 903  ARG   B N     1 
ATOM   15596 C  CA    . ARG   B  1  905  ? 38.354  34.198  98.730  1.00 23.22 ? 903  ARG   B CA    1 
ATOM   15597 C  C     . ARG   B  1  905  ? 39.672  34.865  99.085  1.00 24.70 ? 903  ARG   B C     1 
ATOM   15598 O  O     . ARG   B  1  905  ? 39.973  35.085  100.267 1.00 24.70 ? 903  ARG   B O     1 
ATOM   15599 C  CB    . ARG   B  1  905  ? 38.593  32.740  98.350  1.00 25.77 ? 903  ARG   B CB    1 
ATOM   15600 C  CG    . ARG   B  1  905  ? 38.695  31.810  99.541  1.00 34.50 ? 903  ARG   B CG    1 
ATOM   15601 C  CD    . ARG   B  1  905  ? 39.166  30.438  99.104  1.00 33.84 ? 903  ARG   B CD    1 
ATOM   15602 N  NE    . ARG   B  1  905  ? 38.316  29.860  98.070  1.00 31.01 ? 903  ARG   B NE    1 
ATOM   15603 C  CZ    . ARG   B  1  905  ? 37.225  29.144  98.310  1.00 28.54 ? 903  ARG   B CZ    1 
ATOM   15604 N  NH1   . ARG   B  1  905  ? 36.773  28.965  99.542  1.00 32.32 ? 903  ARG   B NH1   1 
ATOM   15605 N  NH2   . ARG   B  1  905  ? 36.582  28.581  97.291  1.00 31.98 ? 903  ARG   B NH2   1 
ATOM   15606 N  N     . GLY   B  1  906  ? 40.456  35.226  98.071  1.00 23.47 ? 904  GLY   B N     1 
ATOM   15607 C  CA    . GLY   B  1  906  ? 41.752  35.830  98.325  1.00 23.70 ? 904  GLY   B CA    1 
ATOM   15608 C  C     . GLY   B  1  906  ? 41.664  37.209  98.930  1.00 24.40 ? 904  GLY   B C     1 
ATOM   15609 O  O     . GLY   B  1  906  ? 42.629  37.663  99.557  1.00 27.12 ? 904  GLY   B O     1 
ATOM   15610 N  N     . LEU   B  1  907  ? 40.536  37.885  98.767  1.00 28.49 ? 905  LEU   B N     1 
ATOM   15611 C  CA    . LEU   B  1  907  ? 40.303  39.172  99.402  1.00 27.38 ? 905  LEU   B CA    1 
ATOM   15612 C  C     . LEU   B  1  907  ? 39.744  39.037  100.809 1.00 25.27 ? 905  LEU   B C     1 
ATOM   15613 O  O     . LEU   B  1  907  ? 39.474  40.057  101.451 1.00 27.78 ? 905  LEU   B O     1 
ATOM   15614 C  CB    . LEU   B  1  907  ? 39.365  40.024  98.552  1.00 30.49 ? 905  LEU   B CB    1 
ATOM   15615 C  CG    . LEU   B  1  907  ? 39.983  40.481  97.231  1.00 35.17 ? 905  LEU   B CG    1 
ATOM   15616 C  CD1   . LEU   B  1  907  ? 38.960  41.245  96.408  1.00 36.68 ? 905  LEU   B CD1   1 
ATOM   15617 C  CD2   . LEU   B  1  907  ? 41.216  41.326  97.493  1.00 34.44 ? 905  LEU   B CD2   1 
ATOM   15618 N  N     . GLY   B  1  908  ? 39.579  37.813  101.302 1.00 24.59 ? 906  GLY   B N     1 
ATOM   15619 C  CA    . GLY   B  1  908  ? 39.140  37.590  102.661 1.00 25.22 ? 906  GLY   B CA    1 
ATOM   15620 C  C     . GLY   B  1  908  ? 37.646  37.478  102.846 1.00 28.66 ? 906  GLY   B C     1 
ATOM   15621 O  O     . GLY   B  1  908  ? 37.190  37.367  103.991 1.00 26.53 ? 906  GLY   B O     1 
ATOM   15622 N  N     . ARG   B  1  909  ? 36.871  37.503  101.765 1.00 23.53 ? 907  ARG   B N     1 
ATOM   15623 C  CA    . ARG   B  1  909  ? 35.431  37.350  101.872 1.00 22.63 ? 907  ARG   B CA    1 
ATOM   15624 C  C     . ARG   B  1  909  ? 35.102  35.920  102.270 1.00 23.05 ? 907  ARG   B C     1 
ATOM   15625 O  O     . ARG   B  1  909  ? 35.763  34.971  101.844 1.00 24.65 ? 907  ARG   B O     1 
ATOM   15626 C  CB    . ARG   B  1  909  ? 34.771  37.650  100.526 1.00 23.96 ? 907  ARG   B CB    1 
ATOM   15627 C  CG    . ARG   B  1  909  ? 34.948  39.079  100.045 1.00 26.31 ? 907  ARG   B CG    1 
ATOM   15628 C  CD    . ARG   B  1  909  ? 34.353  40.080  101.026 1.00 32.37 ? 907  ARG   B CD    1 
ATOM   15629 N  NE    . ARG   B  1  909  ? 34.506  41.451  100.548 1.00 38.97 ? 907  ARG   B NE    1 
ATOM   15630 C  CZ    . ARG   B  1  909  ? 35.556  42.220  100.799 1.00 41.25 ? 907  ARG   B CZ    1 
ATOM   15631 N  NH1   . ARG   B  1  909  ? 36.563  41.793  101.546 1.00 45.08 ? 907  ARG   B NH1   1 
ATOM   15632 N  NH2   . ARG   B  1  909  ? 35.597  43.449  100.292 1.00 48.30 ? 907  ARG   B NH2   1 
ATOM   15633 N  N     . LYS   B  1  910  ? 34.064  35.765  103.081 1.00 21.46 ? 908  LYS   B N     1 
ATOM   15634 C  CA    . LYS   B  1  910  ? 33.636  34.431  103.467 1.00 23.22 ? 908  LYS   B CA    1 
ATOM   15635 C  C     . LYS   B  1  910  ? 32.996  33.746  102.262 1.00 20.99 ? 908  LYS   B C     1 
ATOM   15636 O  O     . LYS   B  1  910  ? 32.043  34.267  101.668 1.00 21.67 ? 908  LYS   B O     1 
ATOM   15637 C  CB    . LYS   B  1  910  ? 32.648  34.507  104.624 1.00 23.74 ? 908  LYS   B CB    1 
ATOM   15638 C  CG    . LYS   B  1  910  ? 32.305  33.136  105.190 1.00 30.01 ? 908  LYS   B CG    1 
ATOM   15639 C  CD    . LYS   B  1  910  ? 31.228  33.212  106.262 1.00 35.71 ? 908  LYS   B CD    1 
ATOM   15640 C  CE    . LYS   B  1  910  ? 31.011  31.847  106.908 1.00 46.54 ? 908  LYS   B CE    1 
ATOM   15641 N  NZ    . LYS   B  1  910  ? 29.775  31.794  107.748 1.00 44.25 ? 908  LYS   B NZ    1 
ATOM   15642 N  N     . VAL   B  1  911  ? 33.525  32.583  101.896 1.00 20.13 ? 909  VAL   B N     1 
ATOM   15643 C  CA    . VAL   B  1  911  ? 33.061  31.816  100.749 1.00 19.06 ? 909  VAL   B CA    1 
ATOM   15644 C  C     . VAL   B  1  911  ? 32.698  30.422  101.235 1.00 21.44 ? 909  VAL   B C     1 
ATOM   15645 O  O     . VAL   B  1  911  ? 33.522  29.746  101.861 1.00 22.50 ? 909  VAL   B O     1 
ATOM   15646 C  CB    . VAL   B  1  911  ? 34.158  31.729  99.672  1.00 19.71 ? 909  VAL   B CB    1 
ATOM   15647 C  CG1   . VAL   B  1  911  ? 33.739  30.773  98.555  1.00 19.87 ? 909  VAL   B CG1   1 
ATOM   15648 C  CG2   . VAL   B  1  911  ? 34.500  33.123  99.143  1.00 20.82 ? 909  VAL   B CG2   1 
ATOM   15649 N  N     . GLU   B  1  912  ? 31.475  29.996  100.959 1.00 19.85 ? 910  GLU   B N     1 
ATOM   15650 C  CA    . GLU   B  1  912  ? 31.039  28.656  101.314 1.00 20.03 ? 910  GLU   B CA    1 
ATOM   15651 C  C     . GLU   B  1  912  ? 30.487  27.981  100.076 1.00 19.82 ? 910  GLU   B C     1 
ATOM   15652 O  O     . GLU   B  1  912  ? 29.758  28.599  99.296  1.00 21.08 ? 910  GLU   B O     1 
ATOM   15653 C  CB    . GLU   B  1  912  ? 29.958  28.690  102.390 1.00 21.93 ? 910  GLU   B CB    1 
ATOM   15654 C  CG    . GLU   B  1  912  ? 30.439  29.299  103.697 1.00 30.16 ? 910  GLU   B CG    1 
ATOM   15655 C  CD    . GLU   B  1  912  ? 29.310  29.502  104.687 1.00 39.03 ? 910  GLU   B CD    1 
ATOM   15656 O  OE1   . GLU   B  1  912  ? 28.800  28.496  105.227 1.00 41.50 ? 910  GLU   B OE1   1 
ATOM   15657 O  OE2   . GLU   B  1  912  ? 28.925  30.669  104.910 1.00 45.33 ? 910  GLU   B OE2   1 
ATOM   15658 N  N     . GLN   B  1  913  ? 30.837  26.713  99.890  1.00 18.87 ? 911  GLN   B N     1 
ATOM   15659 C  CA    . GLN   B  1  913  ? 30.327  25.933  98.775  1.00 19.39 ? 911  GLN   B CA    1 
ATOM   15660 C  C     . GLN   B  1  913  ? 29.713  24.660  99.311  1.00 23.13 ? 911  GLN   B C     1 
ATOM   15661 O  O     . GLN   B  1  913  ? 30.270  24.020  100.207 1.00 25.08 ? 911  GLN   B O     1 
ATOM   15662 C  CB    . GLN   B  1  913  ? 31.428  25.597  97.775  1.00 21.48 ? 911  GLN   B CB    1 
ATOM   15663 C  CG    . GLN   B  1  913  ? 32.034  26.846  97.177  1.00 22.54 ? 911  GLN   B CG    1 
ATOM   15664 C  CD    . GLN   B  1  913  ? 33.032  26.536  96.095  1.00 25.23 ? 911  GLN   B CD    1 
ATOM   15665 O  OE1   . GLN   B  1  913  ? 34.082  25.955  96.357  1.00 33.24 ? 911  GLN   B OE1   1 
ATOM   15666 N  NE2   . GLN   B  1  913  ? 32.714  26.922  94.870  1.00 23.59 ? 911  GLN   B NE2   1 
ATOM   15667 N  N     . ILE   B  1  914  ? 28.557  24.311  98.769  1.00 22.83 ? 912  ILE   B N     1 
ATOM   15668 C  CA    . ILE   B  1  914  ? 27.771  23.215  99.297  1.00 29.18 ? 912  ILE   B CA    1 
ATOM   15669 C  C     . ILE   B  1  914  ? 27.388  22.279  98.168  1.00 26.33 ? 912  ILE   B C     1 
ATOM   15670 O  O     . ILE   B  1  914  ? 26.722  22.700  97.217  1.00 25.61 ? 912  ILE   B O     1 
ATOM   15671 C  CB    . ILE   B  1  914  ? 26.523  23.749  100.035 1.00 28.68 ? 912  ILE   B CB    1 
ATOM   15672 C  CG1   . ILE   B  1  914  ? 26.939  24.596  101.248 1.00 29.94 ? 912  ILE   B CG1   1 
ATOM   15673 C  CG2   . ILE   B  1  914  ? 25.635  22.598  100.453 1.00 26.97 ? 912  ILE   B CG2   1 
ATOM   15674 C  CD1   . ILE   B  1  914  ? 25.840  25.483  101.809 1.00 27.17 ? 912  ILE   B CD1   1 
ATOM   15675 N  N     . GLU   B  1  919  ? 31.155  11.939  90.547  1.00 35.33 ? 917  GLU   B N     1 
ATOM   15676 C  CA    . GLU   B  1  919  ? 30.383  11.777  89.319  1.00 34.03 ? 917  GLU   B CA    1 
ATOM   15677 C  C     . GLU   B  1  919  ? 30.474  13.031  88.468  1.00 35.25 ? 917  GLU   B C     1 
ATOM   15678 O  O     . GLU   B  1  919  ? 30.368  12.971  87.243  1.00 36.75 ? 917  GLU   B O     1 
ATOM   15679 C  CB    . GLU   B  1  919  ? 28.917  11.481  89.638  1.00 35.01 ? 917  GLU   B CB    1 
ATOM   15680 N  N     . THR   B  1  920  ? 30.665  14.174  89.126  1.00 32.01 ? 918  THR   B N     1 
ATOM   15681 C  CA    . THR   B  1  920  ? 30.704  15.440  88.404  1.00 30.98 ? 918  THR   B CA    1 
ATOM   15682 C  C     . THR   B  1  920  ? 32.004  15.638  87.630  1.00 31.59 ? 918  THR   B C     1 
ATOM   15683 O  O     . THR   B  1  920  ? 32.049  16.494  86.739  1.00 27.78 ? 918  THR   B O     1 
ATOM   15684 C  CB    . THR   B  1  920  ? 30.463  16.614  89.362  1.00 29.94 ? 918  THR   B CB    1 
ATOM   15685 O  OG1   . THR   B  1  920  ? 31.432  16.588  90.418  1.00 30.50 ? 918  THR   B OG1   1 
ATOM   15686 C  CG2   . THR   B  1  920  ? 29.063  16.557  89.955  1.00 25.87 ? 918  THR   B CG2   1 
ATOM   15687 N  N     . GLY   B  1  921  ? 33.054  14.867  87.942  1.00 31.77 ? 919  GLY   B N     1 
ATOM   15688 C  CA    . GLY   B  1  921  ? 34.355  15.069  87.322  1.00 31.94 ? 919  GLY   B CA    1 
ATOM   15689 C  C     . GLY   B  1  921  ? 34.366  14.903  85.815  1.00 32.46 ? 919  GLY   B C     1 
ATOM   15690 O  O     . GLY   B  1  921  ? 35.254  15.445  85.147  1.00 33.25 ? 919  GLY   B O     1 
ATOM   15691 N  N     . VAL   B  1  922  ? 33.397  14.169  85.262  1.00 24.57 ? 920  VAL   B N     1 
ATOM   15692 C  CA    . VAL   B  1  922  ? 33.319  13.969  83.816  1.00 23.59 ? 920  VAL   B CA    1 
ATOM   15693 C  C     . VAL   B  1  922  ? 32.658  15.131  83.091  1.00 21.44 ? 920  VAL   B C     1 
ATOM   15694 O  O     . VAL   B  1  922  ? 32.678  15.167  81.855  1.00 20.83 ? 920  VAL   B O     1 
ATOM   15695 C  CB    . VAL   B  1  922  ? 32.576  12.659  83.494  1.00 23.73 ? 920  VAL   B CB    1 
ATOM   15696 C  CG1   . VAL   B  1  922  ? 33.379  11.461  83.989  1.00 28.19 ? 920  VAL   B CG1   1 
ATOM   15697 C  CG2   . VAL   B  1  922  ? 31.179  12.667  84.118  1.00 24.96 ? 920  VAL   B CG2   1 
ATOM   15698 N  N     . GLY   B  1  923  ? 32.073  16.075  83.819  1.00 20.67 ? 921  GLY   B N     1 
ATOM   15699 C  CA    . GLY   B  1  923  ? 31.505  17.260  83.210  1.00 19.91 ? 921  GLY   B CA    1 
ATOM   15700 C  C     . GLY   B  1  923  ? 32.054  18.507  83.869  1.00 21.72 ? 921  GLY   B C     1 
ATOM   15701 O  O     . GLY   B  1  923  ? 33.038  18.432  84.609  1.00 22.85 ? 921  GLY   B O     1 
ATOM   15702 N  N     . THR   B  1  924  ? 31.439  19.652  83.634  1.00 17.73 ? 922  THR   B N     1 
ATOM   15703 C  CA    . THR   B  1  924  ? 31.909  20.923  84.174  1.00 17.10 ? 922  THR   B CA    1 
ATOM   15704 C  C     . THR   B  1  924  ? 30.871  21.439  85.164  1.00 17.96 ? 922  THR   B C     1 
ATOM   15705 O  O     . THR   B  1  924  ? 29.824  21.957  84.771  1.00 19.37 ? 922  THR   B O     1 
ATOM   15706 C  CB    . THR   B  1  924  ? 32.164  21.927  83.057  1.00 18.32 ? 922  THR   B CB    1 
ATOM   15707 O  OG1   . THR   B  1  924  ? 31.016  21.995  82.211  1.00 18.84 ? 922  THR   B OG1   1 
ATOM   15708 C  CG2   . THR   B  1  924  ? 33.358  21.490  82.224  1.00 19.97 ? 922  THR   B CG2   1 
ATOM   15709 N  N     . PHE   B  1  925  ? 31.156  21.289  86.450  1.00 17.70 ? 923  PHE   B N     1 
ATOM   15710 C  CA    . PHE   B  1  925  ? 30.226  21.688  87.491  1.00 17.27 ? 923  PHE   B CA    1 
ATOM   15711 C  C     . PHE   B  1  925  ? 30.881  22.682  88.431  1.00 18.30 ? 923  PHE   B C     1 
ATOM   15712 O  O     . PHE   B  1  925  ? 32.073  22.583  88.739  1.00 18.05 ? 923  PHE   B O     1 
ATOM   15713 C  CB    . PHE   B  1  925  ? 29.767  20.489  88.319  1.00 17.94 ? 923  PHE   B CB    1 
ATOM   15714 C  CG    . PHE   B  1  925  ? 28.903  19.528  87.570  1.00 17.48 ? 923  PHE   B CG    1 
ATOM   15715 C  CD1   . PHE   B  1  925  ? 29.478  18.559  86.763  1.00 17.77 ? 923  PHE   B CD1   1 
ATOM   15716 C  CD2   . PHE   B  1  925  ? 27.515  19.584  87.671  1.00 17.45 ? 923  PHE   B CD2   1 
ATOM   15717 C  CE1   . PHE   B  1  925  ? 28.700  17.660  86.071  1.00 18.37 ? 923  PHE   B CE1   1 
ATOM   15718 C  CE2   . PHE   B  1  925  ? 26.731  18.691  86.971  1.00 18.27 ? 923  PHE   B CE2   1 
ATOM   15719 C  CZ    . PHE   B  1  925  ? 27.319  17.721  86.184  1.00 18.43 ? 923  PHE   B CZ    1 
ATOM   15720 N  N     . VAL   B  1  926  ? 30.084  23.634  88.897  1.00 16.43 ? 924  VAL   B N     1 
ATOM   15721 C  CA    . VAL   B  1  926  ? 30.429  24.499  90.014  1.00 16.67 ? 924  VAL   B CA    1 
ATOM   15722 C  C     . VAL   B  1  926  ? 29.311  24.329  91.033  1.00 17.00 ? 924  VAL   B C     1 
ATOM   15723 O  O     . VAL   B  1  926  ? 28.140  24.432  90.667  1.00 17.98 ? 924  VAL   B O     1 
ATOM   15724 C  CB    . VAL   B  1  926  ? 30.527  25.974  89.587  1.00 17.33 ? 924  VAL   B CB    1 
ATOM   15725 C  CG1   . VAL   B  1  926  ? 30.789  26.852  90.786  1.00 19.05 ? 924  VAL   B CG1   1 
ATOM   15726 C  CG2   . VAL   B  1  926  ? 31.617  26.149  88.538  1.00 18.79 ? 924  VAL   B CG2   1 
ATOM   15727 N  N     . PRO   B  1  927  ? 29.602  24.046  92.295  1.00 19.67 ? 925  PRO   B N     1 
ATOM   15728 C  CA    . PRO   B  1  927  ? 28.528  23.865  93.256  1.00 19.42 ? 925  PRO   B CA    1 
ATOM   15729 C  C     . PRO   B  1  927  ? 27.971  25.204  93.692  1.00 18.69 ? 925  PRO   B C     1 
ATOM   15730 O  O     . PRO   B  1  927  ? 28.649  26.239  93.581  1.00 18.71 ? 925  PRO   B O     1 
ATOM   15731 C  CB    . PRO   B  1  927  ? 29.229  23.174  94.428  1.00 24.24 ? 925  PRO   B CB    1 
ATOM   15732 C  CG    . PRO   B  1  927  ? 30.594  23.723  94.382  1.00 21.36 ? 925  PRO   B CG    1 
ATOM   15733 C  CD    . PRO   B  1  927  ? 30.925  23.923  92.920  1.00 20.90 ? 925  PRO   B CD    1 
ATOM   15734 N  N     . PRO   B  1  928  ? 26.743  25.216  94.201  1.00 18.22 ? 926  PRO   B N     1 
ATOM   15735 C  CA    . PRO   B  1  928  ? 26.200  26.433  94.801  1.00 17.57 ? 926  PRO   B CA    1 
ATOM   15736 C  C     . PRO   B  1  928  ? 27.191  27.039  95.775  1.00 18.21 ? 926  PRO   B C     1 
ATOM   15737 O  O     . PRO   B  1  928  ? 27.749  26.355  96.645  1.00 18.82 ? 926  PRO   B O     1 
ATOM   15738 C  CB    . PRO   B  1  928  ? 24.945  25.934  95.520  1.00 17.24 ? 926  PRO   B CB    1 
ATOM   15739 C  CG    . PRO   B  1  928  ? 24.484  24.805  94.648  1.00 21.60 ? 926  PRO   B CG    1 
ATOM   15740 C  CD    . PRO   B  1  928  ? 25.749  24.132  94.170  1.00 20.75 ? 926  PRO   B CD    1 
ATOM   15741 N  N     . THR   B  1  929  ? 27.413  28.332  95.607  1.00 18.09 ? 927  THR   B N     1 
ATOM   15742 C  CA    . THR   B  1  929  ? 28.449  29.055  96.311  1.00 17.72 ? 927  THR   B CA    1 
ATOM   15743 C  C     . THR   B  1  929  ? 27.818  30.298  96.902  1.00 17.12 ? 927  THR   B C     1 
ATOM   15744 O  O     . THR   B  1  929  ? 27.031  30.979  96.236  1.00 17.40 ? 927  THR   B O     1 
ATOM   15745 C  CB    . THR   B  1  929  ? 29.562  29.445  95.335  1.00 17.91 ? 927  THR   B CB    1 
ATOM   15746 O  OG1   . THR   B  1  929  ? 30.141  28.255  94.783  1.00 18.19 ? 927  THR   B OG1   1 
ATOM   15747 C  CG2   . THR   B  1  929  ? 30.632  30.254  96.045  1.00 19.37 ? 927  THR   B CG2   1 
ATOM   15748 N  N     . ILE   B  1  930  ? 28.126  30.567  98.163  1.00 17.61 ? 928  ILE   B N     1 
ATOM   15749 C  CA    . ILE   B  1  930  ? 27.634  31.745  98.858  1.00 18.08 ? 928  ILE   B CA    1 
ATOM   15750 C  C     . ILE   B  1  930  ? 28.835  32.557  99.294  1.00 18.04 ? 928  ILE   B C     1 
ATOM   15751 O  O     . ILE   B  1  930  ? 29.735  32.035  99.965  1.00 18.45 ? 928  ILE   B O     1 
ATOM   15752 C  CB    . ILE   B  1  930  ? 26.765  31.376  100.070 1.00 17.01 ? 928  ILE   B CB    1 
ATOM   15753 C  CG1   . ILE   B  1  930  ? 25.529  30.609  99.611  1.00 19.73 ? 928  ILE   B CG1   1 
ATOM   15754 C  CG2   . ILE   B  1  930  ? 26.369  32.643  100.823 1.00 19.16 ? 928  ILE   B CG2   1 
ATOM   15755 C  CD1   . ILE   B  1  930  ? 24.740  29.989  100.744 1.00 23.94 ? 928  ILE   B CD1   1 
ATOM   15756 N  N     . ILE   B  1  931  ? 28.854  33.828  98.913  1.00 18.61 ? 929  ILE   B N     1 
ATOM   15757 C  CA    . ILE   B  1  931  ? 29.961  34.721  99.228  1.00 17.36 ? 929  ILE   B CA    1 
ATOM   15758 C  C     . ILE   B  1  931  ? 29.391  35.918  99.971  1.00 19.06 ? 929  ILE   B C     1 
ATOM   15759 O  O     . ILE   B  1  931  ? 28.482  36.584  99.466  1.00 18.49 ? 929  ILE   B O     1 
ATOM   15760 C  CB    . ILE   B  1  931  ? 30.681  35.176  97.955  1.00 17.18 ? 929  ILE   B CB    1 
ATOM   15761 C  CG1   . ILE   B  1  931  ? 31.162  33.961  97.155  1.00 19.57 ? 929  ILE   B CG1   1 
ATOM   15762 C  CG2   . ILE   B  1  931  ? 31.827  36.126  98.301  1.00 17.97 ? 929  ILE   B CG2   1 
ATOM   15763 C  CD1   . ILE   B  1  931  ? 31.949  34.343  95.931  1.00 19.94 ? 929  ILE   B CD1   1 
ATOM   15764 N  N     . GLU   B  1  932  ? 29.908  36.189  101.167 1.00 19.09 ? 930  GLU   B N     1 
ATOM   15765 C  CA    . GLU   B  1  932  ? 29.460  37.348  101.927 1.00 18.67 ? 930  GLU   B CA    1 
ATOM   15766 C  C     . GLU   B  1  932  ? 30.256  38.566  101.490 1.00 19.88 ? 930  GLU   B C     1 
ATOM   15767 O  O     . GLU   B  1  932  ? 31.492  38.539  101.480 1.00 19.65 ? 930  GLU   B O     1 
ATOM   15768 C  CB    . GLU   B  1  932  ? 29.623  37.113  103.429 1.00 24.25 ? 930  GLU   B CB    1 
ATOM   15769 C  CG    . GLU   B  1  932  ? 28.888  35.883  103.919 1.00 26.49 ? 930  GLU   B CG    1 
ATOM   15770 C  CD    . GLU   B  1  932  ? 27.966  36.160  105.082 1.00 39.47 ? 930  GLU   B CD    1 
ATOM   15771 O  OE1   . GLU   B  1  932  ? 27.491  37.311  105.212 1.00 39.21 ? 930  GLU   B OE1   1 
ATOM   15772 O  OE2   . GLU   B  1  932  ? 27.716  35.219  105.867 1.00 34.82 ? 930  GLU   B OE2   1 
ATOM   15773 N  N     . LEU   B  1  933  ? 29.557  39.618  101.109 1.00 20.83 ? 931  LEU   B N     1 
ATOM   15774 C  CA    . LEU   B  1  933  ? 30.205  40.857  100.727 1.00 20.97 ? 931  LEU   B CA    1 
ATOM   15775 C  C     . LEU   B  1  933  ? 30.049  41.884  101.836 1.00 24.75 ? 931  LEU   B C     1 
ATOM   15776 O  O     . LEU   B  1  933  ? 29.078  41.865  102.597 1.00 28.76 ? 931  LEU   B O     1 
ATOM   15777 C  CB    . LEU   B  1  933  ? 29.579  41.421  99.457  1.00 21.61 ? 931  LEU   B CB    1 
ATOM   15778 C  CG    . LEU   B  1  933  ? 29.581  40.524  98.223  1.00 24.28 ? 931  LEU   B CG    1 
ATOM   15779 C  CD1   . LEU   B  1  933  ? 28.873  41.255  97.098  1.00 28.04 ? 931  LEU   B CD1   1 
ATOM   15780 C  CD2   . LEU   B  1  933  ? 31.009  40.160  97.840  1.00 29.84 ? 931  LEU   B CD2   1 
ATOM   15781 N  N     . GLU   B  1  934  ? 31.014  42.794  101.909 1.00 27.33 ? 932  GLU   B N     1 
ATOM   15782 C  CA    . GLU   B  1  934  ? 30.860  43.945  102.786 1.00 28.68 ? 932  GLU   B CA    1 
ATOM   15783 C  C     . GLU   B  1  934  ? 30.000  45.012  102.130 1.00 29.89 ? 932  GLU   B C     1 
ATOM   15784 O  O     . GLU   B  1  934  ? 29.203  45.674  102.800 1.00 33.60 ? 932  GLU   B O     1 
ATOM   15785 C  CB    . GLU   B  1  934  ? 32.231  44.520  103.144 1.00 31.39 ? 932  GLU   B CB    1 
ATOM   15786 N  N     . LYS   B  1  935  ? 30.140  45.176  100.818 1.00 26.71 ? 933  LYS   B N     1 
ATOM   15787 C  CA    . LYS   B  1  935  ? 29.419  46.198  100.083 1.00 28.38 ? 933  LYS   B CA    1 
ATOM   15788 C  C     . LYS   B  1  935  ? 29.139  45.646  98.699  1.00 23.99 ? 933  LYS   B C     1 
ATOM   15789 O  O     . LYS   B  1  935  ? 29.907  44.834  98.177  1.00 24.79 ? 933  LYS   B O     1 
ATOM   15790 C  CB    . LYS   B  1  935  ? 30.244  47.486  99.976  1.00 32.02 ? 933  LYS   B CB    1 
ATOM   15791 N  N     . LEU   B  1  936  ? 28.016  46.072  98.118  1.00 22.77 ? 934  LEU   B N     1 
ATOM   15792 C  CA    . LEU   B  1  936  ? 27.685  45.604  96.781  1.00 25.43 ? 934  LEU   B CA    1 
ATOM   15793 C  C     . LEU   B  1  936  ? 28.776  45.966  95.786  1.00 24.85 ? 934  LEU   B C     1 
ATOM   15794 O  O     . LEU   B  1  936  ? 29.023  45.212  94.841  1.00 24.43 ? 934  LEU   B O     1 
ATOM   15795 C  CB    . LEU   B  1  936  ? 26.339  46.169  96.342  1.00 27.52 ? 934  LEU   B CB    1 
ATOM   15796 C  CG    . LEU   B  1  936  ? 25.430  45.181  95.611  1.00 28.04 ? 934  LEU   B CG    1 
ATOM   15797 C  CD1   . LEU   B  1  936  ? 23.973  45.613  95.733  1.00 27.66 ? 934  LEU   B CD1   1 
ATOM   15798 C  CD2   . LEU   B  1  936  ? 25.837  45.074  94.165  1.00 29.35 ? 934  LEU   B CD2   1 
ATOM   15799 N  N     . SER   B  1  937  ? 29.458  47.093  95.994  1.00 23.83 ? 935  SER   B N     1 
ATOM   15800 C  CA    . SER   B  1  937  ? 30.515  47.503  95.079  1.00 25.75 ? 935  SER   B CA    1 
ATOM   15801 C  C     . SER   B  1  937  ? 31.699  46.544  95.068  1.00 26.11 ? 935  SER   B C     1 
ATOM   15802 O  O     . SER   B  1  937  ? 32.566  46.684  94.201  1.00 26.37 ? 935  SER   B O     1 
ATOM   15803 C  CB    . SER   B  1  937  ? 30.975  48.928  95.395  1.00 26.87 ? 935  SER   B CB    1 
ATOM   15804 O  OG    . SER   B  1  937  ? 31.438  49.026  96.729  1.00 29.87 ? 935  SER   B OG    1 
ATOM   15805 N  N     . ASP   B  1  938  ? 31.756  45.580  95.996  1.00 25.07 ? 936  ASP   B N     1 
ATOM   15806 C  CA    . ASP   B  1  938  ? 32.758  44.522  95.906  1.00 25.75 ? 936  ASP   B CA    1 
ATOM   15807 C  C     . ASP   B  1  938  ? 32.590  43.695  94.644  1.00 23.38 ? 936  ASP   B C     1 
ATOM   15808 O  O     . ASP   B  1  938  ? 33.541  43.051  94.198  1.00 26.97 ? 936  ASP   B O     1 
ATOM   15809 C  CB    . ASP   B  1  938  ? 32.645  43.557  97.090  1.00 29.57 ? 936  ASP   B CB    1 
ATOM   15810 C  CG    . ASP   B  1  938  ? 32.966  44.209  98.420  1.00 37.04 ? 936  ASP   B CG    1 
ATOM   15811 O  OD1   . ASP   B  1  938  ? 33.585  45.294  98.426  1.00 36.95 ? 936  ASP   B OD1   1 
ATOM   15812 O  OD2   . ASP   B  1  938  ? 32.595  43.624  99.464  1.00 40.48 ? 936  ASP   B OD2   1 
ATOM   15813 N  N     . LEU   B  1  939  ? 31.397  43.681  94.076  1.00 22.02 ? 937  LEU   B N     1 
ATOM   15814 C  CA    . LEU   B  1  939  ? 31.085  42.872  92.915  1.00 25.78 ? 937  LEU   B CA    1 
ATOM   15815 C  C     . LEU   B  1  939  ? 31.120  43.801  91.714  1.00 24.21 ? 937  LEU   B C     1 
ATOM   15816 O  O     . LEU   B  1  939  ? 30.367  44.783  91.671  1.00 32.28 ? 937  LEU   B O     1 
ATOM   15817 C  CB    . LEU   B  1  939  ? 29.684  42.301  93.113  1.00 22.37 ? 937  LEU   B CB    1 
ATOM   15818 C  CG    . LEU   B  1  939  ? 29.107  41.308  92.117  1.00 29.50 ? 937  LEU   B CG    1 
ATOM   15819 C  CD1   . LEU   B  1  939  ? 30.060  40.140  91.917  1.00 28.19 ? 937  LEU   B CD1   1 
ATOM   15820 C  CD2   . LEU   B  1  939  ? 27.785  40.840  92.683  1.00 25.06 ? 937  LEU   B CD2   1 
ATOM   15821 N  N     . GLN   B  1  940  ? 31.984  43.499  90.742  1.00 22.47 ? 938  GLN   B N     1 
ATOM   15822 C  CA    . GLN   B  1  940  ? 32.223  44.409  89.630  1.00 28.03 ? 938  GLN   B CA    1 
ATOM   15823 C  C     . GLN   B  1  940  ? 31.814  43.863  88.271  1.00 25.36 ? 938  GLN   B C     1 
ATOM   15824 O  O     . GLN   B  1  940  ? 31.905  44.596  87.279  1.00 26.77 ? 938  GLN   B O     1 
ATOM   15825 C  CB    . GLN   B  1  940  ? 33.701  44.827  89.574  1.00 34.82 ? 938  GLN   B CB    1 
ATOM   15826 N  N     . ARG   B  1  941  ? 31.379  42.610  88.185  1.00 19.16 ? 939  ARG   B N     1 
ATOM   15827 C  CA    . ARG   B  1  941  ? 30.989  42.048  86.903  1.00 21.81 ? 939  ARG   B CA    1 
ATOM   15828 C  C     . ARG   B  1  941  ? 29.905  41.011  87.145  1.00 18.09 ? 939  ARG   B C     1 
ATOM   15829 O  O     . ARG   B  1  941  ? 29.783  40.459  88.236  1.00 18.18 ? 939  ARG   B O     1 
ATOM   15830 C  CB    . ARG   B  1  941  ? 32.189  41.434  86.162  1.00 22.04 ? 939  ARG   B CB    1 
ATOM   15831 C  CG    . ARG   B  1  941  ? 32.807  40.223  86.850  1.00 21.47 ? 939  ARG   B CG    1 
ATOM   15832 C  CD    . ARG   B  1  941  ? 34.098  39.806  86.145  1.00 22.18 ? 939  ARG   B CD    1 
ATOM   15833 N  NE    . ARG   B  1  941  ? 34.698  38.597  86.704  1.00 22.56 ? 939  ARG   B NE    1 
ATOM   15834 C  CZ    . ARG   B  1  941  ? 34.425  37.364  86.295  1.00 23.58 ? 939  ARG   B CZ    1 
ATOM   15835 N  NH1   . ARG   B  1  941  ? 33.506  37.130  85.370  1.00 24.77 ? 939  ARG   B NH1   1 
ATOM   15836 N  NH2   . ARG   B  1  941  ? 35.097  36.340  86.819  1.00 24.01 ? 939  ARG   B NH2   1 
ATOM   15837 N  N     . GLU   B  1  942  ? 29.122  40.752  86.106  1.00 19.97 ? 940  GLU   B N     1 
ATOM   15838 C  CA    . GLU   B  1  942  ? 28.136  39.686  86.164  1.00 19.19 ? 940  GLU   B CA    1 
ATOM   15839 C  C     . GLU   B  1  942  ? 28.870  38.358  86.117  1.00 20.07 ? 940  GLU   B C     1 
ATOM   15840 O  O     . GLU   B  1  942  ? 29.623  38.093  85.173  1.00 21.30 ? 940  GLU   B O     1 
ATOM   15841 C  CB    . GLU   B  1  942  ? 27.199  39.805  84.967  1.00 21.09 ? 940  GLU   B CB    1 
ATOM   15842 C  CG    . GLU   B  1  942  ? 26.215  38.660  84.844  1.00 19.09 ? 940  GLU   B CG    1 
ATOM   15843 C  CD    . GLU   B  1  942  ? 25.488  38.656  83.502  1.00 18.85 ? 940  GLU   B CD    1 
ATOM   15844 O  OE1   . GLU   B  1  942  ? 26.172  38.846  82.480  1.00 21.67 ? 940  GLU   B OE1   1 
ATOM   15845 O  OE2   . GLU   B  1  942  ? 24.250  38.472  83.458  1.00 16.61 ? 940  GLU   B OE2   1 
ATOM   15846 N  N     . VAL   B  1  943  ? 28.698  37.544  87.151  1.00 17.53 ? 941  VAL   B N     1 
ATOM   15847 C  CA    . VAL   B  1  943  ? 29.325  36.232  87.244  1.00 17.36 ? 941  VAL   B CA    1 
ATOM   15848 C  C     . VAL   B  1  943  ? 28.226  35.221  86.972  1.00 17.42 ? 941  VAL   B C     1 
ATOM   15849 O  O     . VAL   B  1  943  ? 27.294  35.056  87.766  1.00 16.23 ? 941  VAL   B O     1 
ATOM   15850 C  CB    . VAL   B  1  943  ? 30.004  36.025  88.606  1.00 19.24 ? 941  VAL   B CB    1 
ATOM   15851 C  CG1   . VAL   B  1  943  ? 30.621  34.633  88.692  1.00 18.91 ? 941  VAL   B CG1   1 
ATOM   15852 C  CG2   . VAL   B  1  943  ? 31.060  37.109  88.837  1.00 21.32 ? 941  VAL   B CG2   1 
ATOM   15853 N  N     . PHE   B  1  944  ? 28.314  34.579  85.814  1.00 15.88 ? 942  PHE   B N     1 
ATOM   15854 C  CA    . PHE   B  1  944  ? 27.191  33.843  85.255  1.00 16.33 ? 942  PHE   B CA    1 
ATOM   15855 C  C     . PHE   B  1  944  ? 27.287  32.383  85.689  1.00 16.27 ? 942  PHE   B C     1 
ATOM   15856 O  O     . PHE   B  1  944  ? 27.611  31.475  84.928  1.00 17.39 ? 942  PHE   B O     1 
ATOM   15857 C  CB    . PHE   B  1  944  ? 27.193  34.000  83.740  1.00 16.05 ? 942  PHE   B CB    1 
ATOM   15858 C  CG    . PHE   B  1  944  ? 25.861  33.765  83.112  1.00 16.02 ? 942  PHE   B CG    1 
ATOM   15859 C  CD1   . PHE   B  1  944  ? 24.847  34.697  83.247  1.00 15.73 ? 942  PHE   B CD1   1 
ATOM   15860 C  CD2   . PHE   B  1  944  ? 25.621  32.623  82.361  1.00 16.17 ? 942  PHE   B CD2   1 
ATOM   15861 C  CE1   . PHE   B  1  944  ? 23.622  34.489  82.666  1.00 15.96 ? 942  PHE   B CE1   1 
ATOM   15862 C  CE2   . PHE   B  1  944  ? 24.381  32.411  81.763  1.00 16.74 ? 942  PHE   B CE2   1 
ATOM   15863 C  CZ    . PHE   B  1  944  ? 23.380  33.347  81.924  1.00 18.01 ? 942  PHE   B CZ    1 
ATOM   15864 N  N     . GLY   B  1  945  ? 27.011  32.173  86.960  1.00 15.17 ? 943  GLY   B N     1 
ATOM   15865 C  CA    . GLY   B  1  945  ? 27.128  30.864  87.538  1.00 16.39 ? 943  GLY   B CA    1 
ATOM   15866 C  C     . GLY   B  1  945  ? 26.436  30.833  88.878  1.00 16.76 ? 943  GLY   B C     1 
ATOM   15867 O  O     . GLY   B  1  945  ? 25.770  31.787  89.279  1.00 16.94 ? 943  GLY   B O     1 
ATOM   15868 N  N     . PRO   B  1  946  ? 26.586  29.729  89.598  1.00 16.87 ? 944  PRO   B N     1 
ATOM   15869 C  CA    . PRO   B  1  946  ? 25.790  29.515  90.819  1.00 17.15 ? 944  PRO   B CA    1 
ATOM   15870 C  C     . PRO   B  1  946  ? 26.456  30.161  92.028  1.00 16.42 ? 944  PRO   B C     1 
ATOM   15871 O  O     . PRO   B  1  946  ? 26.809  29.501  92.996  1.00 18.31 ? 944  PRO   B O     1 
ATOM   15872 C  CB    . PRO   B  1  946  ? 25.756  27.987  90.919  1.00 15.71 ? 944  PRO   B CB    1 
ATOM   15873 C  CG    . PRO   B  1  946  ? 27.099  27.586  90.389  1.00 17.30 ? 944  PRO   B CG    1 
ATOM   15874 C  CD    . PRO   B  1  946  ? 27.385  28.545  89.241  1.00 17.76 ? 944  PRO   B CD    1 
ATOM   15875 N  N     . VAL   B  1  947  ? 26.632  31.472  91.956  1.00 16.53 ? 945  VAL   B N     1 
ATOM   15876 C  CA    . VAL   B  1  947  ? 27.379  32.213  92.955  1.00 16.72 ? 945  VAL   B CA    1 
ATOM   15877 C  C     . VAL   B  1  947  ? 26.464  33.292  93.502  1.00 19.00 ? 945  VAL   B C     1 
ATOM   15878 O  O     . VAL   B  1  947  ? 26.177  34.285  92.820  1.00 17.94 ? 945  VAL   B O     1 
ATOM   15879 C  CB    . VAL   B  1  947  ? 28.668  32.806  92.387  1.00 17.91 ? 945  VAL   B CB    1 
ATOM   15880 C  CG1   . VAL   B  1  947  ? 29.440  33.471  93.500  1.00 18.32 ? 945  VAL   B CG1   1 
ATOM   15881 C  CG2   . VAL   B  1  947  ? 29.503  31.715  91.729  1.00 19.52 ? 945  VAL   B CG2   1 
ATOM   15882 N  N     . LEU   B  1  948  ? 25.998  33.092  94.729  1.00 16.10 ? 946  LEU   B N     1 
ATOM   15883 C  CA    . LEU   B  1  948  ? 25.125  34.038  95.398  1.00 16.62 ? 946  LEU   B CA    1 
ATOM   15884 C  C     . LEU   B  1  948  ? 25.954  34.884  96.343  1.00 16.70 ? 946  LEU   B C     1 
ATOM   15885 O  O     . LEU   B  1  948  ? 26.699  34.351  97.174  1.00 18.55 ? 946  LEU   B O     1 
ATOM   15886 C  CB    . LEU   B  1  948  ? 24.077  33.290  96.209  1.00 16.60 ? 946  LEU   B CB    1 
ATOM   15887 C  CG    . LEU   B  1  948  ? 23.128  34.212  96.963  1.00 15.95 ? 946  LEU   B CG    1 
ATOM   15888 C  CD1   . LEU   B  1  948  ? 22.309  35.038  95.980  1.00 16.09 ? 946  LEU   B CD1   1 
ATOM   15889 C  CD2   . LEU   B  1  948  ? 22.237  33.377  97.871  1.00 20.46 ? 946  LEU   B CD2   1 
ATOM   15890 N  N     . HIS   B  1  949  ? 25.831  36.193  96.216  1.00 15.64 ? 947  HIS   B N     1 
ATOM   15891 C  CA    . HIS   B  1  949  ? 26.505  37.119  97.104  1.00 16.15 ? 947  HIS   B CA    1 
ATOM   15892 C  C     . HIS   B  1  949  ? 25.511  37.588  98.139  1.00 17.19 ? 947  HIS   B C     1 
ATOM   15893 O  O     . HIS   B  1  949  ? 24.328  37.753  97.841  1.00 18.48 ? 947  HIS   B O     1 
ATOM   15894 C  CB    . HIS   B  1  949  ? 27.036  38.286  96.290  1.00 18.50 ? 947  HIS   B CB    1 
ATOM   15895 C  CG    . HIS   B  1  949  ? 27.944  37.834  95.197  1.00 16.59 ? 947  HIS   B CG    1 
ATOM   15896 N  ND1   . HIS   B  1  949  ? 27.488  37.454  93.951  1.00 16.91 ? 947  HIS   B ND1   1 
ATOM   15897 C  CD2   . HIS   B  1  949  ? 29.278  37.612  95.194  1.00 16.86 ? 947  HIS   B CD2   1 
ATOM   15898 C  CE1   . HIS   B  1  949  ? 28.514  37.052  93.219  1.00 16.34 ? 947  HIS   B CE1   1 
ATOM   15899 N  NE2   . HIS   B  1  949  ? 29.608  37.133  93.950  1.00 17.31 ? 947  HIS   B NE2   1 
ATOM   15900 N  N     . VAL   B  1  950  ? 25.977  37.754  99.369  1.00 17.44 ? 948  VAL   B N     1 
ATOM   15901 C  CA    . VAL   B  1  950  ? 25.098  38.092  100.475 1.00 18.73 ? 948  VAL   B CA    1 
ATOM   15902 C  C     . VAL   B  1  950  ? 25.547  39.402  101.085 1.00 18.22 ? 948  VAL   B C     1 
ATOM   15903 O  O     . VAL   B  1  950  ? 26.728  39.576  101.412 1.00 18.28 ? 948  VAL   B O     1 
ATOM   15904 C  CB    . VAL   B  1  950  ? 25.061  36.979  101.530 1.00 19.24 ? 948  VAL   B CB    1 
ATOM   15905 C  CG1   . VAL   B  1  950  ? 24.266  37.452  102.743 1.00 22.10 ? 948  VAL   B CG1   1 
ATOM   15906 C  CG2   . VAL   B  1  950  ? 24.452  35.725  100.940 1.00 20.94 ? 948  VAL   B CG2   1 
ATOM   15907 N  N     . ILE   B  1  951  ? 24.601  40.306  101.248 1.00 17.11 ? 949  ILE   B N     1 
ATOM   15908 C  CA    . ILE   B  1  951  ? 24.806  41.579  101.915 1.00 17.71 ? 949  ILE   B CA    1 
ATOM   15909 C  C     . ILE   B  1  951  ? 23.837  41.630  103.081 1.00 18.15 ? 949  ILE   B C     1 
ATOM   15910 O  O     . ILE   B  1  951  ? 22.668  41.263  102.935 1.00 18.65 ? 949  ILE   B O     1 
ATOM   15911 C  CB    . ILE   B  1  951  ? 24.489  42.721  100.937 1.00 21.03 ? 949  ILE   B CB    1 
ATOM   15912 C  CG1   . ILE   B  1  951  ? 25.548  42.783  99.843  1.00 25.36 ? 949  ILE   B CG1   1 
ATOM   15913 C  CG2   . ILE   B  1  951  ? 24.342  44.058  101.683 1.00 27.90 ? 949  ILE   B CG2   1 
ATOM   15914 C  CD1   . ILE   B  1  951  ? 25.316  43.915  98.899  1.00 33.67 ? 949  ILE   B CD1   1 
ATOM   15915 N  N     . ARG   B  1  952  ? 24.317  42.070  104.231 1.00 17.63 ? 950  ARG   B N     1 
ATOM   15916 C  CA    A ARG   B  1  952  ? 23.464  42.337  105.375 0.71 19.98 ? 950  ARG   B CA    1 
ATOM   15917 C  CA    B ARG   B  1  952  ? 23.480  42.339  105.391 0.29 19.99 ? 950  ARG   B CA    1 
ATOM   15918 C  C     . ARG   B  1  952  ? 23.247  43.840  105.477 1.00 19.08 ? 950  ARG   B C     1 
ATOM   15919 O  O     . ARG   B  1  952  ? 24.161  44.628  105.237 1.00 23.30 ? 950  ARG   B O     1 
ATOM   15920 C  CB    A ARG   B  1  952  ? 24.127  41.815  106.650 0.71 19.37 ? 950  ARG   B CB    1 
ATOM   15921 C  CB    B ARG   B  1  952  ? 24.182  41.887  106.673 0.29 19.41 ? 950  ARG   B CB    1 
ATOM   15922 C  CG    A ARG   B  1  952  ? 24.411  40.328  106.584 0.71 21.57 ? 950  ARG   B CG    1 
ATOM   15923 C  CG    B ARG   B  1  952  ? 24.167  40.395  106.927 0.29 22.51 ? 950  ARG   B CG    1 
ATOM   15924 C  CD    A ARG   B  1  952  ? 25.481  39.933  107.579 0.71 24.01 ? 950  ARG   B CD    1 
ATOM   15925 C  CD    B ARG   B  1  952  ? 25.010  40.069  108.151 0.29 24.19 ? 950  ARG   B CD    1 
ATOM   15926 N  NE    A ARG   B  1  952  ? 25.827  38.525  107.444 0.71 27.61 ? 950  ARG   B NE    1 
ATOM   15927 N  NE    B ARG   B  1  952  ? 24.765  38.727  108.664 0.29 25.07 ? 950  ARG   B NE    1 
ATOM   15928 C  CZ    A ARG   B  1  952  ? 25.442  37.571  108.283 0.71 26.87 ? 950  ARG   B CZ    1 
ATOM   15929 C  CZ    B ARG   B  1  952  ? 25.219  37.613  108.103 0.29 26.90 ? 950  ARG   B CZ    1 
ATOM   15930 N  NH1   A ARG   B  1  952  ? 24.670  37.833  109.325 0.71 22.74 ? 950  ARG   B NH1   1 
ATOM   15931 N  NH1   B ARG   B  1  952  ? 25.909  37.637  106.973 0.29 28.32 ? 950  ARG   B NH1   1 
ATOM   15932 N  NH2   A ARG   B  1  952  ? 25.849  36.322  108.073 0.71 27.79 ? 950  ARG   B NH2   1 
ATOM   15933 N  NH2   B ARG   B  1  952  ? 24.970  36.446  108.689 0.29 27.32 ? 950  ARG   B NH2   1 
ATOM   15934 N  N     . TYR   B  1  953  ? 22.027  44.243  105.817 1.00 18.44 ? 951  TYR   B N     1 
ATOM   15935 C  CA    . TYR   B  1  953  ? 21.774  45.674  105.895 1.00 18.05 ? 951  TYR   B CA    1 
ATOM   15936 C  C     . TYR   B  1  953  ? 20.902  45.992  107.098 1.00 19.16 ? 951  TYR   B C     1 
ATOM   15937 O  O     . TYR   B  1  953  ? 20.119  45.155  107.553 1.00 20.07 ? 951  TYR   B O     1 
ATOM   15938 C  CB    . TYR   B  1  953  ? 21.112  46.204  104.606 1.00 20.28 ? 951  TYR   B CB    1 
ATOM   15939 C  CG    . TYR   B  1  953  ? 19.676  45.784  104.454 1.00 17.37 ? 951  TYR   B CG    1 
ATOM   15940 C  CD1   . TYR   B  1  953  ? 19.340  44.548  103.903 1.00 16.67 ? 951  TYR   B CD1   1 
ATOM   15941 C  CD2   . TYR   B  1  953  ? 18.649  46.615  104.871 1.00 18.29 ? 951  TYR   B CD2   1 
ATOM   15942 C  CE1   . TYR   B  1  953  ? 18.021  44.172  103.776 1.00 17.68 ? 951  TYR   B CE1   1 
ATOM   15943 C  CE2   . TYR   B  1  953  ? 17.339  46.240  104.743 1.00 18.68 ? 951  TYR   B CE2   1 
ATOM   15944 C  CZ    . TYR   B  1  953  ? 17.032  45.015  104.200 1.00 18.36 ? 951  TYR   B CZ    1 
ATOM   15945 O  OH    . TYR   B  1  953  ? 15.715  44.644  104.094 1.00 18.08 ? 951  TYR   B OH    1 
ATOM   15946 N  N     . ARG   B  1  954  ? 21.049  47.215  107.606 1.00 21.25 ? 952  ARG   B N     1 
ATOM   15947 C  CA    . ARG   B  1  954  ? 20.162  47.736  108.634 1.00 25.04 ? 952  ARG   B CA    1 
ATOM   15948 C  C     . ARG   B  1  954  ? 18.966  48.381  107.952 1.00 22.92 ? 952  ARG   B C     1 
ATOM   15949 O  O     . ARG   B  1  954  ? 19.116  49.046  106.925 1.00 22.75 ? 952  ARG   B O     1 
ATOM   15950 C  CB    . ARG   B  1  954  ? 20.889  48.781  109.485 1.00 26.71 ? 952  ARG   B CB    1 
ATOM   15951 N  N     . ARG   B  1  955  ? 17.777  48.200  108.540 1.00 24.32 ? 953  ARG   B N     1 
ATOM   15952 C  CA    . ARG   B  1  955  ? 16.562  48.706  107.909 1.00 26.32 ? 953  ARG   B CA    1 
ATOM   15953 C  C     . ARG   B  1  955  ? 16.648  50.203  107.628 1.00 23.83 ? 953  ARG   B C     1 
ATOM   15954 O  O     . ARG   B  1  955  ? 16.128  50.681  106.612 1.00 24.49 ? 953  ARG   B O     1 
ATOM   15955 C  CB    . ARG   B  1  955  ? 15.335  48.371  108.758 1.00 29.30 ? 953  ARG   B CB    1 
ATOM   15956 C  CG    . ARG   B  1  955  ? 14.008  48.824  108.146 1.00 33.97 ? 953  ARG   B CG    1 
ATOM   15957 C  CD    . ARG   B  1  955  ? 13.851  48.362  106.691 1.00 31.52 ? 953  ARG   B CD    1 
ATOM   15958 N  NE    . ARG   B  1  955  ? 12.557  48.748  106.134 1.00 31.40 ? 953  ARG   B NE    1 
ATOM   15959 C  CZ    . ARG   B  1  955  ? 12.239  49.978  105.750 1.00 32.79 ? 953  ARG   B CZ    1 
ATOM   15960 N  NH1   . ARG   B  1  955  ? 13.104  50.977  105.840 1.00 34.25 ? 953  ARG   B NH1   1 
ATOM   15961 N  NH2   . ARG   B  1  955  ? 11.020  50.212  105.264 1.00 30.58 ? 953  ARG   B NH2   1 
ATOM   15962 N  N     . ASP   B  1  956  ? 17.301  50.966  108.507 1.00 23.62 ? 954  ASP   B N     1 
ATOM   15963 C  CA    A ASP   B  1  956  ? 17.433  52.402  108.282 0.50 26.43 ? 954  ASP   B CA    1 
ATOM   15964 C  CA    B ASP   B  1  956  ? 17.401  52.399  108.257 0.50 26.42 ? 954  ASP   B CA    1 
ATOM   15965 C  C     . ASP   B  1  956  ? 18.282  52.729  107.062 1.00 26.21 ? 954  ASP   B C     1 
ATOM   15966 O  O     . ASP   B  1  956  ? 18.248  53.869  106.585 1.00 29.83 ? 954  ASP   B O     1 
ATOM   15967 C  CB    A ASP   B  1  956  ? 18.015  53.081  109.520 0.50 27.12 ? 954  ASP   B CB    1 
ATOM   15968 C  CB    B ASP   B  1  956  ? 17.810  53.186  109.514 0.50 27.32 ? 954  ASP   B CB    1 
ATOM   15969 C  CG    A ASP   B  1  956  ? 17.062  53.051  110.694 0.50 31.82 ? 954  ASP   B CG    1 
ATOM   15970 C  CG    B ASP   B  1  956  ? 19.151  52.751  110.096 0.50 26.66 ? 954  ASP   B CG    1 
ATOM   15971 O  OD1   A ASP   B  1  956  ? 15.840  52.958  110.456 0.50 31.56 ? 954  ASP   B OD1   1 
ATOM   15972 O  OD1   B ASP   B  1  956  ? 19.967  52.126  109.389 0.50 30.48 ? 954  ASP   B OD1   1 
ATOM   15973 O  OD2   A ASP   B  1  956  ? 17.533  53.121  111.848 0.50 34.24 ? 954  ASP   B OD2   1 
ATOM   15974 O  OD2   B ASP   B  1  956  ? 19.388  53.051  111.290 0.50 32.73 ? 954  ASP   B OD2   1 
ATOM   15975 N  N     . ASP   B  1  957  ? 19.040  51.762  106.559 1.00 22.86 ? 955  ASP   B N     1 
ATOM   15976 C  CA    . ASP   B  1  957  ? 19.873  51.943  105.385 1.00 25.28 ? 955  ASP   B CA    1 
ATOM   15977 C  C     . ASP   B  1  957  ? 19.209  51.417  104.123 1.00 20.63 ? 955  ASP   B C     1 
ATOM   15978 O  O     . ASP   B  1  957  ? 19.875  51.303  103.102 1.00 21.82 ? 955  ASP   B O     1 
ATOM   15979 C  CB    . ASP   B  1  957  ? 21.216  51.232  105.563 1.00 26.41 ? 955  ASP   B CB    1 
ATOM   15980 C  CG    . ASP   B  1  957  ? 22.103  51.896  106.594 1.00 34.53 ? 955  ASP   B CG    1 
ATOM   15981 O  OD1   . ASP   B  1  957  ? 21.981  53.124  106.801 1.00 36.18 ? 955  ASP   B OD1   1 
ATOM   15982 O  OD2   . ASP   B  1  957  ? 22.940  51.181  107.187 1.00 37.11 ? 955  ASP   B OD2   1 
ATOM   15983 N  N     . LEU   B  1  958  ? 17.918  51.086  104.179 1.00 20.43 ? 956  LEU   B N     1 
ATOM   15984 C  CA    . LEU   B  1  958  ? 17.262  50.474  103.025 1.00 18.92 ? 956  LEU   B CA    1 
ATOM   15985 C  C     . LEU   B  1  958  ? 17.356  51.359  101.787 1.00 18.52 ? 956  LEU   B C     1 
ATOM   15986 O  O     . LEU   B  1  958  ? 17.659  50.872  100.692 1.00 18.31 ? 956  LEU   B O     1 
ATOM   15987 C  CB    . LEU   B  1  958  ? 15.802  50.182  103.350 1.00 19.48 ? 956  LEU   B CB    1 
ATOM   15988 C  CG    . LEU   B  1  958  ? 14.983  49.618  102.192 1.00 18.43 ? 956  LEU   B CG    1 
ATOM   15989 C  CD1   . LEU   B  1  958  ? 15.591  48.319  101.677 1.00 21.35 ? 956  LEU   B CD1   1 
ATOM   15990 C  CD2   . LEU   B  1  958  ? 13.578  49.402  102.680 1.00 22.02 ? 956  LEU   B CD2   1 
ATOM   15991 N  N     . ASP   B  1  959  ? 17.127  52.661  101.935 1.00 18.85 ? 957  ASP   B N     1 
ATOM   15992 C  CA    . ASP   B  1  959  ? 17.167  53.523  100.761 1.00 18.30 ? 957  ASP   B CA    1 
ATOM   15993 C  C     . ASP   B  1  959  ? 18.559  53.540  100.146 1.00 18.68 ? 957  ASP   B C     1 
ATOM   15994 O  O     . ASP   B  1  959  ? 18.704  53.469  98.920  1.00 18.94 ? 957  ASP   B O     1 
ATOM   15995 C  CB    . ASP   B  1  959  ? 16.698  54.931  101.115 1.00 19.18 ? 957  ASP   B CB    1 
ATOM   15996 C  CG    . ASP   B  1  959  ? 16.270  55.707  99.897  1.00 20.47 ? 957  ASP   B CG    1 
ATOM   15997 O  OD1   . ASP   B  1  959  ? 15.503  55.149  99.083  1.00 19.98 ? 957  ASP   B OD1   1 
ATOM   15998 O  OD2   . ASP   B  1  959  ? 16.684  56.871  99.746  1.00 21.97 ? 957  ASP   B OD2   1 
ATOM   15999 N  N     . ARG   B  1  960  ? 19.593  53.609  100.980 1.00 18.20 ? 958  ARG   B N     1 
ATOM   16000 C  CA    . ARG   B  1  960  ? 20.956  53.549  100.477 1.00 17.82 ? 958  ARG   B CA    1 
ATOM   16001 C  C     . ARG   B  1  960  ? 21.239  52.202  99.824  1.00 18.77 ? 958  ARG   B C     1 
ATOM   16002 O  O     . ARG   B  1  960  ? 21.976  52.127  98.834  1.00 18.85 ? 958  ARG   B O     1 
ATOM   16003 C  CB    . ARG   B  1  960  ? 21.933  53.810  101.625 1.00 21.33 ? 958  ARG   B CB    1 
ATOM   16004 N  N     . LEU   B  1  961  ? 20.692  51.122  100.383 1.00 16.47 ? 959  LEU   B N     1 
ATOM   16005 C  CA    . LEU   B  1  961  ? 20.863  49.815  99.763  1.00 16.79 ? 959  LEU   B CA    1 
ATOM   16006 C  C     . LEU   B  1  961  ? 20.271  49.791  98.362  1.00 17.66 ? 959  LEU   B C     1 
ATOM   16007 O  O     . LEU   B  1  961  ? 20.880  49.250  97.429  1.00 17.04 ? 959  LEU   B O     1 
ATOM   16008 C  CB    . LEU   B  1  961  ? 20.224  48.736  100.631 1.00 17.01 ? 959  LEU   B CB    1 
ATOM   16009 C  CG    . LEU   B  1  961  ? 20.238  47.328  100.032 1.00 17.50 ? 959  LEU   B CG    1 
ATOM   16010 C  CD1   . LEU   B  1  961  ? 21.684  46.824  99.867  1.00 22.93 ? 959  LEU   B CD1   1 
ATOM   16011 C  CD2   . LEU   B  1  961  ? 19.429  46.386  100.888 1.00 19.57 ? 959  LEU   B CD2   1 
ATOM   16012 N  N     . VAL   B  1  962  ? 19.086  50.374  98.190  1.00 16.43 ? 960  VAL   B N     1 
ATOM   16013 C  CA    . VAL   B  1  962  ? 18.504  50.456  96.860  1.00 16.82 ? 960  VAL   B CA    1 
ATOM   16014 C  C     . VAL   B  1  962  ? 19.434  51.217  95.925  1.00 17.76 ? 960  VAL   B C     1 
ATOM   16015 O  O     . VAL   B  1  962  ? 19.643  50.811  94.775  1.00 18.18 ? 960  VAL   B O     1 
ATOM   16016 C  CB    . VAL   B  1  962  ? 17.097  51.067  96.920  1.00 17.67 ? 960  VAL   B CB    1 
ATOM   16017 C  CG1   . VAL   B  1  962  ? 16.589  51.306  95.519  1.00 19.37 ? 960  VAL   B CG1   1 
ATOM   16018 C  CG2   . VAL   B  1  962  ? 16.165  50.139  97.699  1.00 19.87 ? 960  VAL   B CG2   1 
ATOM   16019 N  N     . ASP   B  1  963  ? 20.024  52.319  96.405  1.00 17.19 ? 961  ASP   B N     1 
ATOM   16020 C  CA    . ASP   B  1  963  ? 21.021  53.025  95.606  1.00 19.55 ? 961  ASP   B CA    1 
ATOM   16021 C  C     . ASP   B  1  963  ? 22.158  52.102  95.220  1.00 19.02 ? 961  ASP   B C     1 
ATOM   16022 O  O     . ASP   B  1  963  ? 22.635  52.136  94.079  1.00 19.40 ? 961  ASP   B O     1 
ATOM   16023 C  CB    . ASP   B  1  963  ? 21.615  54.180  96.399  1.00 21.50 ? 961  ASP   B CB    1 
ATOM   16024 C  CG    . ASP   B  1  963  ? 20.702  55.342  96.499  1.00 26.88 ? 961  ASP   B CG    1 
ATOM   16025 O  OD1   . ASP   B  1  963  ? 19.720  55.391  95.732  1.00 25.54 ? 961  ASP   B OD1   1 
ATOM   16026 O  OD2   . ASP   B  1  963  ? 20.985  56.215  97.349  1.00 26.94 ? 961  ASP   B OD2   1 
ATOM   16027 N  N     . ASP   B  1  964  ? 22.625  51.286  96.166  1.00 17.58 ? 962  ASP   B N     1 
ATOM   16028 C  CA    . ASP   B  1  964  ? 23.743  50.395  95.882  1.00 19.16 ? 962  ASP   B CA    1 
ATOM   16029 C  C     . ASP   B  1  964  ? 23.380  49.387  94.805  1.00 18.39 ? 962  ASP   B C     1 
ATOM   16030 O  O     . ASP   B  1  964  ? 24.197  49.090  93.929  1.00 18.98 ? 962  ASP   B O     1 
ATOM   16031 C  CB    . ASP   B  1  964  ? 24.169  49.661  97.146  1.00 18.75 ? 962  ASP   B CB    1 
ATOM   16032 C  CG    . ASP   B  1  964  ? 24.816  50.573  98.158  1.00 21.67 ? 962  ASP   B CG    1 
ATOM   16033 O  OD1   . ASP   B  1  964  ? 25.118  51.739  97.817  1.00 24.57 ? 962  ASP   B OD1   1 
ATOM   16034 O  OD2   . ASP   B  1  964  ? 25.000  50.112  99.306  1.00 29.11 ? 962  ASP   B OD2   1 
ATOM   16035 N  N     . VAL   B  1  965  ? 22.154  48.864  94.848  1.00 16.49 ? 963  VAL   B N     1 
ATOM   16036 C  CA    . VAL   B  1  965  ? 21.707  47.956  93.798  1.00 15.14 ? 963  VAL   B CA    1 
ATOM   16037 C  C     . VAL   B  1  965  ? 21.690  48.681  92.458  1.00 16.74 ? 963  VAL   B C     1 
ATOM   16038 O  O     . VAL   B  1  965  ? 22.200  48.171  91.450  1.00 17.02 ? 963  VAL   B O     1 
ATOM   16039 C  CB    . VAL   B  1  965  ? 20.328  47.364  94.139  1.00 15.85 ? 963  VAL   B CB    1 
ATOM   16040 C  CG1   . VAL   B  1  965  ? 19.842  46.510  92.986  1.00 16.72 ? 963  VAL   B CG1   1 
ATOM   16041 C  CG2   . VAL   B  1  965  ? 20.408  46.528  95.413  1.00 18.42 ? 963  VAL   B CG2   1 
ATOM   16042 N  N     . ASN   B  1  966  ? 21.140  49.898  92.434  1.00 16.63 ? 964  ASN   B N     1 
ATOM   16043 C  CA    . ASN   B  1  966  ? 21.070  50.640  91.177  1.00 17.07 ? 964  ASN   B CA    1 
ATOM   16044 C  C     . ASN   B  1  966  ? 22.454  51.028  90.684  1.00 16.95 ? 964  ASN   B C     1 
ATOM   16045 O  O     . ASN   B  1  966  ? 22.662  51.176  89.473  1.00 18.97 ? 964  ASN   B O     1 
ATOM   16046 C  CB    . ASN   B  1  966  ? 20.233  51.905  91.345  1.00 17.74 ? 964  ASN   B CB    1 
ATOM   16047 C  CG    . ASN   B  1  966  ? 18.757  51.621  91.535  1.00 17.36 ? 964  ASN   B CG    1 
ATOM   16048 O  OD1   . ASN   B  1  966  ? 18.253  50.587  91.107  1.00 18.14 ? 964  ASN   B OD1   1 
ATOM   16049 N  ND2   . ASN   B  1  966  ? 18.054  52.557  92.159  1.00 18.33 ? 964  ASN   B ND2   1 
ATOM   16050 N  N     . ALA   B  1  967  ? 23.406  51.187  91.601  1.00 16.51 ? 965  ALA   B N     1 
ATOM   16051 C  CA    . ALA   B  1  967  ? 24.712  51.732  91.264  1.00 18.92 ? 965  ALA   B CA    1 
ATOM   16052 C  C     . ALA   B  1  967  ? 25.540  50.796  90.401  1.00 18.20 ? 965  ALA   B C     1 
ATOM   16053 O  O     . ALA   B  1  967  ? 26.571  51.227  89.872  1.00 20.30 ? 965  ALA   B O     1 
ATOM   16054 C  CB    . ALA   B  1  967  ? 25.487  52.057  92.543  1.00 19.79 ? 965  ALA   B CB    1 
ATOM   16055 N  N     . THR   B  1  968  ? 25.151  49.523  90.273  1.00 17.24 ? 966  THR   B N     1 
ATOM   16056 C  CA    . THR   B  1  968  ? 25.901  48.635  89.396  1.00 17.99 ? 966  THR   B CA    1 
ATOM   16057 C  C     . THR   B  1  968  ? 25.760  49.046  87.944  1.00 18.71 ? 966  THR   B C     1 
ATOM   16058 O  O     . THR   B  1  968  ? 26.597  48.663  87.119  1.00 20.02 ? 966  THR   B O     1 
ATOM   16059 C  CB    . THR   B  1  968  ? 25.421  47.191  89.513  1.00 16.73 ? 966  THR   B CB    1 
ATOM   16060 O  OG1   . THR   B  1  968  ? 24.125  47.079  88.917  1.00 17.37 ? 966  THR   B OG1   1 
ATOM   16061 C  CG2   . THR   B  1  968  ? 25.348  46.756  90.973  1.00 19.20 ? 966  THR   B CG2   1 
ATOM   16062 N  N     . GLY   B  1  969  ? 24.714  49.805  87.618  1.00 17.23 ? 967  GLY   B N     1 
ATOM   16063 C  CA    . GLY   B  1  969  ? 24.418  50.170  86.257  1.00 17.88 ? 967  GLY   B CA    1 
ATOM   16064 C  C     . GLY   B  1  969  ? 23.514  49.196  85.554  1.00 17.89 ? 967  GLY   B C     1 
ATOM   16065 O  O     . GLY   B  1  969  ? 22.994  49.521  84.483  1.00 17.73 ? 967  GLY   B O     1 
ATOM   16066 N  N     . TYR   B  1  970  ? 23.309  48.016  86.129  1.00 16.83 ? 968  TYR   B N     1 
ATOM   16067 C  CA    . TYR   B  1  970  ? 22.375  47.050  85.584  1.00 15.98 ? 968  TYR   B CA    1 
ATOM   16068 C  C     . TYR   B  1  970  ? 20.969  47.348  86.084  1.00 15.72 ? 968  TYR   B C     1 
ATOM   16069 O  O     . TYR   B  1  970  ? 20.753  48.173  86.976  1.00 18.00 ? 968  TYR   B O     1 
ATOM   16070 C  CB    . TYR   B  1  970  ? 22.792  45.654  86.024  1.00 16.43 ? 968  TYR   B CB    1 
ATOM   16071 C  CG    . TYR   B  1  970  ? 24.024  45.153  85.300  1.00 18.46 ? 968  TYR   B CG    1 
ATOM   16072 C  CD1   . TYR   B  1  970  ? 23.919  44.698  83.998  1.00 19.75 ? 968  TYR   B CD1   1 
ATOM   16073 C  CD2   . TYR   B  1  970  ? 25.276  45.128  85.907  1.00 20.10 ? 968  TYR   B CD2   1 
ATOM   16074 C  CE1   . TYR   B  1  970  ? 25.014  44.220  83.299  1.00 22.77 ? 968  TYR   B CE1   1 
ATOM   16075 C  CE2   . TYR   B  1  970  ? 26.393  44.640  85.208  1.00 23.19 ? 968  TYR   B CE2   1 
ATOM   16076 C  CZ    . TYR   B  1  970  ? 26.235  44.189  83.903  1.00 24.47 ? 968  TYR   B CZ    1 
ATOM   16077 O  OH    . TYR   B  1  970  ? 27.298  43.706  83.167  1.00 32.16 ? 968  TYR   B OH    1 
ATOM   16078 N  N     . GLY   B  1  971  ? 19.993  46.678  85.486  1.00 15.24 ? 969  GLY   B N     1 
ATOM   16079 C  CA    . GLY   B  1  971  ? 18.624  46.882  85.891  1.00 15.92 ? 969  GLY   B CA    1 
ATOM   16080 C  C     . GLY   B  1  971  ? 17.728  45.875  85.220  1.00 13.61 ? 969  GLY   B C     1 
ATOM   16081 O  O     . GLY   B  1  971  ? 16.790  46.255  84.511  1.00 14.22 ? 969  GLY   B O     1 
ATOM   16082 N  N     . LEU   B  1  972  ? 17.985  44.595  85.466  1.00 12.93 ? 970  LEU   B N     1 
ATOM   16083 C  CA    . LEU   B  1  972  ? 17.233  43.533  84.824  1.00 13.90 ? 970  LEU   B CA    1 
ATOM   16084 C  C     . LEU   B  1  972  ? 16.149  43.038  85.772  1.00 12.93 ? 970  LEU   B C     1 
ATOM   16085 O  O     . LEU   B  1  972  ? 15.021  43.532  85.702  1.00 14.76 ? 970  LEU   B O     1 
ATOM   16086 C  CB    . LEU   B  1  972  ? 18.190  42.448  84.311  1.00 15.05 ? 970  LEU   B CB    1 
ATOM   16087 C  CG    . LEU   B  1  972  ? 17.519  41.369  83.476  1.00 14.29 ? 970  LEU   B CG    1 
ATOM   16088 C  CD1   . LEU   B  1  972  ? 16.790  41.976  82.303  1.00 16.91 ? 970  LEU   B CD1   1 
ATOM   16089 C  CD2   . LEU   B  1  972  ? 18.582  40.407  82.994  1.00 17.37 ? 970  LEU   B CD2   1 
ATOM   16090 N  N     . THR   B  1  973  ? 16.458  42.076  86.640  1.00 13.42 ? 971  THR   B N     1 
ATOM   16091 C  CA    . THR   B  1  973  ? 15.458  41.588  87.571  1.00 13.26 ? 971  THR   B CA    1 
ATOM   16092 C  C     . THR   B  1  973  ? 15.773  42.066  88.979  1.00 12.29 ? 971  THR   B C     1 
ATOM   16093 O  O     . THR   B  1  973  ? 16.920  42.349  89.327  1.00 13.86 ? 971  THR   B O     1 
ATOM   16094 C  CB    . THR   B  1  973  ? 15.350  40.057  87.551  1.00 13.22 ? 971  THR   B CB    1 
ATOM   16095 O  OG1   . THR   B  1  973  ? 16.607  39.478  87.909  1.00 13.49 ? 971  THR   B OG1   1 
ATOM   16096 C  CG2   . THR   B  1  973  ? 14.881  39.563  86.167  1.00 15.86 ? 971  THR   B CG2   1 
ATOM   16097 N  N     . PHE   B  1  974  ? 14.725  42.120  89.793  1.00 13.42 ? 972  PHE   B N     1 
ATOM   16098 C  CA    . PHE   B  1  974  ? 14.862  42.549  91.171  1.00 13.51 ? 972  PHE   B CA    1 
ATOM   16099 C  C     . PHE   B  1  974  ? 13.732  41.940  91.976  1.00 13.02 ? 972  PHE   B C     1 
ATOM   16100 O  O     . PHE   B  1  974  ? 12.576  41.998  91.560  1.00 13.62 ? 972  PHE   B O     1 
ATOM   16101 C  CB    . PHE   B  1  974  ? 14.766  44.070  91.276  1.00 12.96 ? 972  PHE   B CB    1 
ATOM   16102 C  CG    . PHE   B  1  974  ? 14.706  44.546  92.700  1.00 13.04 ? 972  PHE   B CG    1 
ATOM   16103 C  CD1   . PHE   B  1  974  ? 15.870  44.646  93.450  1.00 15.66 ? 972  PHE   B CD1   1 
ATOM   16104 C  CD2   . PHE   B  1  974  ? 13.487  44.826  93.292  1.00 13.85 ? 972  PHE   B CD2   1 
ATOM   16105 C  CE1   . PHE   B  1  974  ? 15.824  45.046  94.771  1.00 15.07 ? 972  PHE   B CE1   1 
ATOM   16106 C  CE2   . PHE   B  1  974  ? 13.438  45.229  94.610  1.00 15.88 ? 972  PHE   B CE2   1 
ATOM   16107 C  CZ    . PHE   B  1  974  ? 14.597  45.332  95.348  1.00 15.71 ? 972  PHE   B CZ    1 
ATOM   16108 N  N     . GLY   B  1  975  ? 14.058  41.406  93.147  1.00 14.05 ? 973  GLY   B N     1 
ATOM   16109 C  CA    . GLY   B  1  975  ? 13.063  40.832  94.033  1.00 13.26 ? 973  GLY   B CA    1 
ATOM   16110 C  C     . GLY   B  1  975  ? 12.988  41.539  95.372  1.00 14.45 ? 973  GLY   B C     1 
ATOM   16111 O  O     . GLY   B  1  975  ? 13.984  42.051  95.879  1.00 15.33 ? 973  GLY   B O     1 
ATOM   16112 N  N     . LEU   B  1  976  ? 11.802  41.529  95.954  1.00 14.27 ? 974  LEU   B N     1 
ATOM   16113 C  CA    . LEU   B  1  976  ? 11.610  42.074  97.283  1.00 15.90 ? 974  LEU   B CA    1 
ATOM   16114 C  C     . LEU   B  1  976  ? 10.721  41.100  98.030  1.00 15.99 ? 974  LEU   B C     1 
ATOM   16115 O  O     . LEU   B  1  976  ? 9.645   40.741  97.544  1.00 15.60 ? 974  LEU   B O     1 
ATOM   16116 C  CB    . LEU   B  1  976  ? 10.942  43.444  97.197  1.00 16.94 ? 974  LEU   B CB    1 
ATOM   16117 C  CG    . LEU   B  1  976  ? 10.551  44.061  98.539  1.00 17.80 ? 974  LEU   B CG    1 
ATOM   16118 C  CD1   . LEU   B  1  976  ? 11.789  44.365  99.370  1.00 19.95 ? 974  LEU   B CD1   1 
ATOM   16119 C  CD2   . LEU   B  1  976  ? 9.749   45.314  98.284  1.00 18.81 ? 974  LEU   B CD2   1 
ATOM   16120 N  N     . HIS   B  1  977  ? 11.184  40.655  99.194  1.00 15.22 ? 975  HIS   B N     1 
ATOM   16121 C  CA    . HIS   B  1  977  ? 10.376  39.839  100.090 1.00 16.13 ? 975  HIS   B CA    1 
ATOM   16122 C  C     . HIS   B  1  977  ? 10.077  40.664  101.328 1.00 15.66 ? 975  HIS   B C     1 
ATOM   16123 O  O     . HIS   B  1  977  ? 10.977  40.979  102.112 1.00 16.49 ? 975  HIS   B O     1 
ATOM   16124 C  CB    . HIS   B  1  977  ? 11.072  38.537  100.471 1.00 17.06 ? 975  HIS   B CB    1 
ATOM   16125 C  CG    . HIS   B  1  977  ? 10.772  37.402  99.550  1.00 18.38 ? 975  HIS   B CG    1 
ATOM   16126 N  ND1   . HIS   B  1  977  ? 9.976   36.339  99.918  1.00 25.39 ? 975  HIS   B ND1   1 
ATOM   16127 C  CD2   . HIS   B  1  977  ? 11.164  37.161  98.278  1.00 23.12 ? 975  HIS   B CD2   1 
ATOM   16128 C  CE1   . HIS   B  1  977  ? 9.903   35.483  98.915  1.00 22.66 ? 975  HIS   B CE1   1 
ATOM   16129 N  NE2   . HIS   B  1  977  ? 10.608  35.960  97.908  1.00 22.65 ? 975  HIS   B NE2   1 
ATOM   16130 N  N     . THR   B  1  978  ? 8.811   40.994  101.493 1.00 15.53 ? 976  THR   B N     1 
ATOM   16131 C  CA    . THR   B  1  978  ? 8.344   41.754  102.641 1.00 15.99 ? 976  THR   B CA    1 
ATOM   16132 C  C     . THR   B  1  978  ? 6.839   41.609  102.697 1.00 17.02 ? 976  THR   B C     1 
ATOM   16133 O  O     . THR   B  1  978  ? 6.186   41.400  101.674 1.00 18.54 ? 976  THR   B O     1 
ATOM   16134 C  CB    . THR   B  1  978  ? 8.683   43.240  102.514 1.00 17.96 ? 976  THR   B CB    1 
ATOM   16135 O  OG1   . THR   B  1  978  ? 8.158   43.935  103.651 1.00 17.45 ? 976  THR   B OG1   1 
ATOM   16136 C  CG2   . THR   B  1  978  ? 8.047   43.828  101.274 1.00 18.93 ? 976  THR   B CG2   1 
ATOM   16137 N  N     . ARG   B  1  979  ? 6.294   41.719  103.896 1.00 18.22 ? 977  ARG   B N     1 
ATOM   16138 C  CA    . ARG   B  1  979  ? 4.852   41.762  104.030 1.00 19.44 ? 977  ARG   B CA    1 
ATOM   16139 C  C     . ARG   B  1  979  ? 4.321   43.177  104.144 1.00 20.86 ? 977  ARG   B C     1 
ATOM   16140 O  O     . ARG   B  1  979  ? 3.108   43.357  104.257 1.00 20.23 ? 977  ARG   B O     1 
ATOM   16141 C  CB    . ARG   B  1  979  ? 4.425   40.933  105.232 1.00 22.69 ? 977  ARG   B CB    1 
ATOM   16142 C  CG    . ARG   B  1  979  ? 4.656   39.458  105.011 1.00 29.23 ? 977  ARG   B CG    1 
ATOM   16143 C  CD    . ARG   B  1  979  ? 4.490   38.699  106.300 1.00 35.10 ? 977  ARG   B CD    1 
ATOM   16144 N  NE    . ARG   B  1  979  ? 4.573   37.258  106.104 1.00 41.39 ? 977  ARG   B NE    1 
ATOM   16145 C  CZ    . ARG   B  1  979  ? 4.328   36.367  107.055 1.00 41.71 ? 977  ARG   B CZ    1 
ATOM   16146 N  NH1   . ARG   B  1  979  ? 3.982   36.740  108.277 1.00 37.37 ? 977  ARG   B NH1   1 
ATOM   16147 N  NH2   . ARG   B  1  979  ? 4.430   35.071  106.772 1.00 42.36 ? 977  ARG   B NH2   1 
ATOM   16148 N  N     . LEU   B  1  980  ? 5.183   44.184  104.087 1.00 17.98 ? 978  LEU   B N     1 
ATOM   16149 C  CA    . LEU   B  1  980  ? 4.834   45.530  104.522 1.00 18.55 ? 978  LEU   B CA    1 
ATOM   16150 C  C     . LEU   B  1  980  ? 4.647   46.435  103.319 1.00 17.78 ? 978  LEU   B C     1 
ATOM   16151 O  O     . LEU   B  1  980  ? 5.593   46.663  102.556 1.00 17.51 ? 978  LEU   B O     1 
ATOM   16152 C  CB    . LEU   B  1  980  ? 5.922   46.097  105.422 1.00 19.25 ? 978  LEU   B CB    1 
ATOM   16153 C  CG    . LEU   B  1  980  ? 6.276   45.193  106.594 1.00 20.47 ? 978  LEU   B CG    1 
ATOM   16154 C  CD1   . LEU   B  1  980  ? 7.423   45.806  107.411 1.00 20.17 ? 978  LEU   B CD1   1 
ATOM   16155 C  CD2   . LEU   B  1  980  ? 5.068   44.918  107.458 1.00 19.31 ? 978  LEU   B CD2   1 
ATOM   16156 N  N     . ASP   B  1  981  ? 3.437   46.976  103.174 1.00 17.23 ? 979  ASP   B N     1 
ATOM   16157 C  CA    . ASP   B  1  981  ? 3.138   47.799  102.006 1.00 16.92 ? 979  ASP   B CA    1 
ATOM   16158 C  C     . ASP   B  1  981  ? 4.026   49.028  101.914 1.00 18.17 ? 979  ASP   B C     1 
ATOM   16159 O  O     . ASP   B  1  981  ? 4.342   49.464  100.806 1.00 17.21 ? 979  ASP   B O     1 
ATOM   16160 C  CB    . ASP   B  1  981  ? 1.682   48.256  102.030 1.00 18.68 ? 979  ASP   B CB    1 
ATOM   16161 C  CG    . ASP   B  1  981  ? 0.711   47.145  101.740 1.00 22.23 ? 979  ASP   B CG    1 
ATOM   16162 O  OD1   . ASP   B  1  981  ? 1.118   46.105  101.187 1.00 21.67 ? 979  ASP   B OD1   1 
ATOM   16163 O  OD2   . ASP   B  1  981  ? -0.484  47.339  102.080 1.00 23.60 ? 979  ASP   B OD2   1 
ATOM   16164 N  N     . GLU   B  1  982  ? 4.418   49.622  103.041 1.00 18.31 ? 980  GLU   B N     1 
ATOM   16165 C  CA    . GLU   B  1  982  ? 5.268   50.803  102.953 1.00 18.23 ? 980  GLU   B CA    1 
ATOM   16166 C  C     . GLU   B  1  982  ? 6.613   50.440  102.357 1.00 18.77 ? 980  GLU   B C     1 
ATOM   16167 O  O     . GLU   B  1  982  ? 7.173   51.192  101.552 1.00 18.71 ? 980  GLU   B O     1 
ATOM   16168 C  CB    . GLU   B  1  982  ? 5.482   51.428  104.330 1.00 19.06 ? 980  GLU   B CB    1 
ATOM   16169 C  CG    . GLU   B  1  982  ? 6.439   52.619  104.288 1.00 24.14 ? 980  GLU   B CG    1 
ATOM   16170 C  CD    . GLU   B  1  982  ? 6.978   53.019  105.645 1.00 27.15 ? 980  GLU   B CD    1 
ATOM   16171 O  OE1   . GLU   B  1  982  ? 7.389   52.129  106.425 1.00 30.36 ? 980  GLU   B OE1   1 
ATOM   16172 O  OE2   . GLU   B  1  982  ? 6.992   54.231  105.927 1.00 25.99 ? 980  GLU   B OE2   1 
ATOM   16173 N  N     . THR   B  1  983  ? 7.149   49.289  102.751 1.00 17.34 ? 981  THR   B N     1 
ATOM   16174 C  CA    . THR   B  1  983  ? 8.423   48.849  102.199 1.00 16.46 ? 981  THR   B CA    1 
ATOM   16175 C  C     . THR   B  1  983  ? 8.291   48.540  100.714 1.00 17.18 ? 981  THR   B C     1 
ATOM   16176 O  O     . THR   B  1  983  ? 9.178   48.881  99.919  1.00 17.36 ? 981  THR   B O     1 
ATOM   16177 C  CB    . THR   B  1  983  ? 8.916   47.642  102.991 1.00 19.12 ? 981  THR   B CB    1 
ATOM   16178 O  OG1   . THR   B  1  983  ? 9.159   48.047  104.343 1.00 19.45 ? 981  THR   B OG1   1 
ATOM   16179 C  CG2   . THR   B  1  983  ? 10.201  47.109  102.390 1.00 18.61 ? 981  THR   B CG2   1 
ATOM   16180 N  N     . ILE   B  1  984  ? 7.170   47.933  100.316 1.00 15.62 ? 982  ILE   B N     1 
ATOM   16181 C  CA    . ILE   B  1  984  ? 6.935   47.659  98.901  1.00 15.98 ? 982  ILE   B CA    1 
ATOM   16182 C  C     . ILE   B  1  984  ? 6.892   48.959  98.119  1.00 16.95 ? 982  ILE   B C     1 
ATOM   16183 O  O     . ILE   B  1  984  ? 7.530   49.094  97.065  1.00 16.67 ? 982  ILE   B O     1 
ATOM   16184 C  CB    . ILE   B  1  984  ? 5.642   46.850  98.709  1.00 16.61 ? 982  ILE   B CB    1 
ATOM   16185 C  CG1   . ILE   B  1  984  ? 5.793   45.468  99.327  1.00 20.32 ? 982  ILE   B CG1   1 
ATOM   16186 C  CG2   . ILE   B  1  984  ? 5.321   46.712  97.220  1.00 20.08 ? 982  ILE   B CG2   1 
ATOM   16187 C  CD1   . ILE   B  1  984  ? 4.504   44.694  99.412  1.00 20.28 ? 982  ILE   B CD1   1 
ATOM   16188 N  N     . ALA   B  1  985  ? 6.139   49.938  98.621  1.00 16.87 ? 983  ALA   B N     1 
ATOM   16189 C  CA    . ALA   B  1  985  ? 6.023   51.201  97.898  1.00 17.37 ? 983  ALA   B CA    1 
ATOM   16190 C  C     . ALA   B  1  985  ? 7.371   51.894  97.811  1.00 17.57 ? 983  ALA   B C     1 
ATOM   16191 O  O     . ALA   B  1  985  ? 7.758   52.383  96.743  1.00 17.99 ? 983  ALA   B O     1 
ATOM   16192 C  CB    . ALA   B  1  985  ? 4.990   52.108  98.561  1.00 16.61 ? 983  ALA   B CB    1 
ATOM   16193 N  N     . HIS   B  1  986  ? 8.105   51.921  98.921  1.00 16.91 ? 984  HIS   B N     1 
ATOM   16194 C  CA    . HIS   B  1  986  ? 9.405   52.575  98.937  1.00 18.38 ? 984  HIS   B CA    1 
ATOM   16195 C  C     . HIS   B  1  986  ? 10.335  51.903  97.945  1.00 16.30 ? 984  HIS   B C     1 
ATOM   16196 O  O     . HIS   B  1  986  ? 10.876  52.545  97.039  1.00 17.84 ? 984  HIS   B O     1 
ATOM   16197 C  CB    . HIS   B  1  986  ? 9.982   52.496  100.349 1.00 19.60 ? 984  HIS   B CB    1 
ATOM   16198 C  CG    . HIS   B  1  986  ? 11.370  53.039  100.483 1.00 19.47 ? 984  HIS   B CG    1 
ATOM   16199 N  ND1   . HIS   B  1  986  ? 11.990  53.158  101.706 1.00 25.19 ? 984  HIS   B ND1   1 
ATOM   16200 C  CD2   . HIS   B  1  986  ? 12.260  53.490  99.566  1.00 21.58 ? 984  HIS   B CD2   1 
ATOM   16201 C  CE1   . HIS   B  1  986  ? 13.205  53.652  101.539 1.00 24.92 ? 984  HIS   B CE1   1 
ATOM   16202 N  NE2   . HIS   B  1  986  ? 13.392  53.865  100.250 1.00 20.77 ? 984  HIS   B NE2   1 
ATOM   16203 N  N     . VAL   B  1  987  ? 10.515  50.596  98.093  1.00 15.48 ? 985  VAL   B N     1 
ATOM   16204 C  CA    . VAL   B  1  987  ? 11.523  49.906  97.296  1.00 15.61 ? 985  VAL   B CA    1 
ATOM   16205 C  C     . VAL   B  1  987  ? 11.162  49.930  95.821  1.00 16.69 ? 985  VAL   B C     1 
ATOM   16206 O  O     . VAL   B  1  987  ? 12.015  50.204  94.973  1.00 18.52 ? 985  VAL   B O     1 
ATOM   16207 C  CB    . VAL   B  1  987  ? 11.729  48.476  97.808  1.00 16.35 ? 985  VAL   B CB    1 
ATOM   16208 C  CG1   . VAL   B  1  987  ? 12.644  47.720  96.858  1.00 17.86 ? 985  VAL   B CG1   1 
ATOM   16209 C  CG2   . VAL   B  1  987  ? 12.349  48.510  99.182  1.00 17.62 ? 985  VAL   B CG2   1 
ATOM   16210 N  N     . THR   B  1  988  ? 9.904   49.654  95.487  1.00 16.67 ? 986  THR   B N     1 
ATOM   16211 C  CA    . THR   B  1  988  ? 9.551   49.653  94.071  1.00 18.38 ? 986  THR   B CA    1 
ATOM   16212 C  C     . THR   B  1  988  ? 9.576   51.053  93.466  1.00 19.13 ? 986  THR   B C     1 
ATOM   16213 O  O     . THR   B  1  988  ? 9.787   51.174  92.256  1.00 23.96 ? 986  THR   B O     1 
ATOM   16214 C  CB    . THR   B  1  988  ? 8.209   48.960  93.812  1.00 20.76 ? 986  THR   B CB    1 
ATOM   16215 O  OG1   . THR   B  1  988  ? 7.172   49.666  94.482  1.00 21.37 ? 986  THR   B OG1   1 
ATOM   16216 C  CG2   . THR   B  1  988  ? 8.234   47.511  94.278  1.00 21.14 ? 986  THR   B CG2   1 
ATOM   16217 N  N     . SER   B  1  989  ? 9.390   52.108  94.263  1.00 18.50 ? 987  SER   B N     1 
ATOM   16218 C  CA    . SER   B  1  989  ? 9.490   53.460  93.716  1.00 21.09 ? 987  SER   B CA    1 
ATOM   16219 C  C     . SER   B  1  989  ? 10.928  53.879  93.454  1.00 22.13 ? 987  SER   B C     1 
ATOM   16220 O  O     . SER   B  1  989  ? 11.155  54.805  92.670  1.00 25.45 ? 987  SER   B O     1 
ATOM   16221 C  CB    . SER   B  1  989  ? 8.812   54.494  94.624  1.00 23.50 ? 987  SER   B CB    1 
ATOM   16222 O  OG    . SER   B  1  989  ? 9.513   54.690  95.841  1.00 28.37 ? 987  SER   B OG    1 
ATOM   16223 N  N     . ARG   B  1  990  ? 11.898  53.226  94.086  1.00 18.06 ? 988  ARG   B N     1 
ATOM   16224 C  CA    . ARG   B  1  990  ? 13.290  53.651  94.033  1.00 16.88 ? 988  ARG   B CA    1 
ATOM   16225 C  C     . ARG   B  1  990  ? 14.186  52.730  93.217  1.00 17.81 ? 988  ARG   B C     1 
ATOM   16226 O  O     . ARG   B  1  990  ? 15.219  53.179  92.712  1.00 18.91 ? 988  ARG   B O     1 
ATOM   16227 C  CB    . ARG   B  1  990  ? 13.851  53.778  95.456  1.00 18.66 ? 988  ARG   B CB    1 
ATOM   16228 C  CG    . ARG   B  1  990  ? 13.028  54.673  96.373  1.00 25.35 ? 988  ARG   B CG    1 
ATOM   16229 C  CD    . ARG   B  1  990  ? 13.230  56.136  96.071  1.00 24.90 ? 988  ARG   B CD    1 
ATOM   16230 N  NE    . ARG   B  1  990  ? 14.360  56.679  96.820  1.00 20.03 ? 988  ARG   B NE    1 
ATOM   16231 C  CZ    . ARG   B  1  990  ? 14.757  57.940  96.745  1.00 19.29 ? 988  ARG   B CZ    1 
ATOM   16232 N  NH1   . ARG   B  1  990  ? 14.189  58.792  95.909  1.00 23.58 ? 988  ARG   B NH1   1 
ATOM   16233 N  NH2   . ARG   B  1  990  ? 15.762  58.350  97.513  1.00 22.74 ? 988  ARG   B NH2   1 
ATOM   16234 N  N     . ILE   B  1  991  ? 13.841  51.449  93.098  1.00 16.92 ? 989  ILE   B N     1 
ATOM   16235 C  CA    . ILE   B  1  991  ? 14.637  50.525  92.307  1.00 17.02 ? 989  ILE   B CA    1 
ATOM   16236 C  C     . ILE   B  1  991  ? 14.472  50.861  90.831  1.00 17.70 ? 989  ILE   B C     1 
ATOM   16237 O  O     . ILE   B  1  991  ? 13.426  51.353  90.388  1.00 18.58 ? 989  ILE   B O     1 
ATOM   16238 C  CB    . ILE   B  1  991  ? 14.191  49.082  92.608  1.00 16.94 ? 989  ILE   B CB    1 
ATOM   16239 C  CG1   . ILE   B  1  991  ? 15.225  48.071  92.112  1.00 20.83 ? 989  ILE   B CG1   1 
ATOM   16240 C  CG2   . ILE   B  1  991  ? 12.837  48.804  91.987  1.00 18.57 ? 989  ILE   B CG2   1 
ATOM   16241 C  CD1   . ILE   B  1  991  ? 16.529  48.164  92.861  1.00 22.55 ? 989  ILE   B CD1   1 
ATOM   16242 N  N     . LYS   B  1  992  ? 15.518  50.621  90.062  1.00 15.50 ? 990  LYS   B N     1 
ATOM   16243 C  CA    . LYS   B  1  992  ? 15.490  50.903  88.628  1.00 16.68 ? 990  LYS   B CA    1 
ATOM   16244 C  C     . LYS   B  1  992  ? 15.802  49.603  87.905  1.00 18.00 ? 990  LYS   B C     1 
ATOM   16245 O  O     . LYS   B  1  992  ? 16.919  49.379  87.458  1.00 20.92 ? 990  LYS   B O     1 
ATOM   16246 C  CB    . LYS   B  1  992  ? 16.491  51.986  88.296  1.00 17.80 ? 990  LYS   B CB    1 
ATOM   16247 C  CG    . LYS   B  1  992  ? 16.159  53.324  88.942  1.00 20.66 ? 990  LYS   B CG    1 
ATOM   16248 C  CD    . LYS   B  1  992  ? 17.250  54.351  88.677  1.00 27.14 ? 990  LYS   B CD    1 
ATOM   16249 C  CE    . LYS   B  1  992  ? 17.418  54.613  87.186  1.00 34.59 ? 990  LYS   B CE    1 
ATOM   16250 N  NZ    . LYS   B  1  992  ? 18.570  55.517  86.899  1.00 43.31 ? 990  LYS   B NZ    1 
ATOM   16251 N  N     . ALA   B  1  993  ? 14.805  48.741  87.796  1.00 15.73 ? 991  ALA   B N     1 
ATOM   16252 C  CA    . ALA   B  1  993  ? 14.959  47.476  87.101  1.00 14.81 ? 991  ALA   B CA    1 
ATOM   16253 C  C     . ALA   B  1  993  ? 13.717  47.229  86.269  1.00 14.99 ? 991  ALA   B C     1 
ATOM   16254 O  O     . ALA   B  1  993  ? 12.626  47.704  86.594  1.00 16.25 ? 991  ALA   B O     1 
ATOM   16255 C  CB    . ALA   B  1  993  ? 15.160  46.301  88.066  1.00 17.32 ? 991  ALA   B CB    1 
ATOM   16256 N  N     . GLY   B  1  994  ? 13.893  46.472  85.187  1.00 13.88 ? 992  GLY   B N     1 
ATOM   16257 C  CA    . GLY   B  1  994  ? 12.783  46.274  84.283  1.00 14.71 ? 992  GLY   B CA    1 
ATOM   16258 C  C     . GLY   B  1  994  ? 11.793  45.223  84.715  1.00 14.04 ? 992  GLY   B C     1 
ATOM   16259 O  O     . GLY   B  1  994  ? 10.648  45.267  84.274  1.00 13.22 ? 992  GLY   B O     1 
ATOM   16260 N  N     . ASN   B  1  995  ? 12.196  44.286  85.565  1.00 14.33 ? 993  ASN   B N     1 
ATOM   16261 C  CA    . ASN   B  1  995  ? 11.327  43.206  86.005  1.00 14.64 ? 993  ASN   B CA    1 
ATOM   16262 C  C     . ASN   B  1  995  ? 11.433  43.110  87.510  1.00 12.89 ? 993  ASN   B C     1 
ATOM   16263 O  O     . ASN   B  1  995  ? 12.496  42.765  88.031  1.00 14.26 ? 993  ASN   B O     1 
ATOM   16264 C  CB    . ASN   B  1  995  ? 11.705  41.889  85.344  1.00 15.26 ? 993  ASN   B CB    1 
ATOM   16265 C  CG    . ASN   B  1  995  ? 11.167  41.791  83.941  1.00 15.22 ? 993  ASN   B CG    1 
ATOM   16266 O  OD1   . ASN   B  1  995  ? 11.778  42.282  82.987  1.00 14.35 ? 993  ASN   B OD1   1 
ATOM   16267 N  ND2   . ASN   B  1  995  ? 9.987   41.201  83.810  1.00 14.65 ? 993  ASN   B ND2   1 
ATOM   16268 N  N     . LEU   B  1  996  ? 10.338  43.406  88.182  1.00 13.36 ? 994  LEU   B N     1 
ATOM   16269 C  CA    . LEU   B  1  996  ? 10.268  43.394  89.630  1.00 13.87 ? 994  LEU   B CA    1 
ATOM   16270 C  C     . LEU   B  1  996  ? 9.413   42.225  90.056  1.00 14.43 ? 994  LEU   B C     1 
ATOM   16271 O  O     . LEU   B  1  996  ? 8.455   41.869  89.373  1.00 13.50 ? 994  LEU   B O     1 
ATOM   16272 C  CB    . LEU   B  1  996  ? 9.641   44.680  90.152  1.00 14.25 ? 994  LEU   B CB    1 
ATOM   16273 C  CG    . LEU   B  1  996  ? 10.193  45.973  89.563  1.00 14.67 ? 994  LEU   B CG    1 
ATOM   16274 C  CD1   . LEU   B  1  996  ? 9.472   47.166  90.204  1.00 18.26 ? 994  LEU   B CD1   1 
ATOM   16275 C  CD2   . LEU   B  1  996  ? 11.697  46.061  89.738  1.00 15.92 ? 994  LEU   B CD2   1 
ATOM   16276 N  N     . TYR   B  1  997  ? 9.738   41.650  91.207  1.00 13.98 ? 995  TYR   B N     1 
ATOM   16277 C  CA    . TYR   B  1  997  ? 9.040   40.477  91.707  1.00 14.41 ? 995  TYR   B CA    1 
ATOM   16278 C  C     . TYR   B  1  997  ? 8.884   40.648  93.198  1.00 14.10 ? 995  TYR   B C     1 
ATOM   16279 O  O     . TYR   B  1  997  ? 9.862   40.915  93.902  1.00 15.32 ? 995  TYR   B O     1 
ATOM   16280 C  CB    . TYR   B  1  997  ? 9.816   39.196  91.425  1.00 16.09 ? 995  TYR   B CB    1 
ATOM   16281 C  CG    . TYR   B  1  997  ? 10.179  39.038  89.977  1.00 14.88 ? 995  TYR   B CG    1 
ATOM   16282 C  CD1   . TYR   B  1  997  ? 11.328  39.625  89.476  1.00 14.08 ? 995  TYR   B CD1   1 
ATOM   16283 C  CD2   . TYR   B  1  997  ? 9.379   38.315  89.111  1.00 16.01 ? 995  TYR   B CD2   1 
ATOM   16284 C  CE1   . TYR   B  1  997  ? 11.672  39.501  88.157  1.00 16.41 ? 995  TYR   B CE1   1 
ATOM   16285 C  CE2   . TYR   B  1  997  ? 9.737   38.179  87.771  1.00 15.24 ? 995  TYR   B CE2   1 
ATOM   16286 C  CZ    . TYR   B  1  997  ? 10.885  38.778  87.324  1.00 15.89 ? 995  TYR   B CZ    1 
ATOM   16287 O  OH    . TYR   B  1  997  ? 11.254  38.660  85.997  1.00 18.60 ? 995  TYR   B OH    1 
ATOM   16288 N  N     . ILE   B  1  998  ? 7.663   40.504  93.673  1.00 14.50 ? 996  ILE   B N     1 
ATOM   16289 C  CA    . ILE   B  1  998  ? 7.355   40.724  95.074  1.00 14.70 ? 996  ILE   B CA    1 
ATOM   16290 C  C     . ILE   B  1  998  ? 6.910   39.396  95.670  1.00 15.93 ? 996  ILE   B C     1 
ATOM   16291 O  O     . ILE   B  1  998  ? 5.903   38.821  95.236  1.00 15.54 ? 996  ILE   B O     1 
ATOM   16292 C  CB    . ILE   B  1  998  ? 6.262   41.788  95.245  1.00 16.88 ? 996  ILE   B CB    1 
ATOM   16293 C  CG1   . ILE   B  1  998  ? 6.659   43.100  94.556  1.00 20.86 ? 996  ILE   B CG1   1 
ATOM   16294 C  CG2   . ILE   B  1  998  ? 5.958   41.983  96.727  1.00 16.99 ? 996  ILE   B CG2   1 
ATOM   16295 C  CD1   . ILE   B  1  998  ? 7.876   43.744  95.084  1.00 25.67 ? 996  ILE   B CD1   1 
ATOM   16296 N  N     . ASN   B  1  999  ? 7.660   38.925  96.672  1.00 14.89 ? 997  ASN   B N     1 
ATOM   16297 C  CA    . ASN   B  1  999  ? 7.307   37.729  97.435  1.00 16.12 ? 997  ASN   B CA    1 
ATOM   16298 C  C     . ASN   B  1  999  ? 7.264   36.478  96.564  1.00 15.71 ? 997  ASN   B C     1 
ATOM   16299 O  O     . ASN   B  1  999  ? 6.429   35.594  96.755  1.00 16.11 ? 997  ASN   B O     1 
ATOM   16300 C  CB    . ASN   B  1  999  ? 6.015   37.933  98.217  1.00 15.04 ? 997  ASN   B CB    1 
ATOM   16301 C  CG    . ASN   B  1  999  ? 6.178   38.967  99.275  1.00 16.34 ? 997  ASN   B CG    1 
ATOM   16302 O  OD1   . ASN   B  1  999  ? 7.264   39.087  99.842  1.00 16.43 ? 997  ASN   B OD1   1 
ATOM   16303 N  ND2   . ASN   B  1  999  ? 5.125   39.726  99.553  1.00 17.63 ? 997  ASN   B ND2   1 
ATOM   16304 N  N     . ARG   B  1  1000 ? 8.187   36.397  95.614  1.00 15.09 ? 998  ARG   B N     1 
ATOM   16305 C  CA    . ARG   B  1  1000 ? 8.307   35.237  94.746  1.00 13.92 ? 998  ARG   B CA    1 
ATOM   16306 C  C     . ARG   B  1  1000 ? 9.731   35.209  94.211  1.00 15.28 ? 998  ARG   B C     1 
ATOM   16307 O  O     . ARG   B  1  1000 ? 10.554  36.064  94.546  1.00 16.63 ? 998  ARG   B O     1 
ATOM   16308 C  CB    . ARG   B  1  1000 ? 7.290   35.305  93.607  1.00 15.26 ? 998  ARG   B CB    1 
ATOM   16309 C  CG    . ARG   B  1  1000 ? 7.304   36.640  92.881  1.00 15.92 ? 998  ARG   B CG    1 
ATOM   16310 C  CD    . ARG   B  1  1000 ? 6.783   36.492  91.458  1.00 15.30 ? 998  ARG   B CD    1 
ATOM   16311 N  NE    . ARG   B  1  1000 ? 7.693   35.672  90.673  1.00 14.30 ? 998  ARG   B NE    1 
ATOM   16312 C  CZ    . ARG   B  1  1000 ? 7.409   35.219  89.463  1.00 14.94 ? 998  ARG   B CZ    1 
ATOM   16313 N  NH1   . ARG   B  1  1000 ? 6.278   35.543  88.857  1.00 15.89 ? 998  ARG   B NH1   1 
ATOM   16314 N  NH2   . ARG   B  1  1000 ? 8.282   34.431  88.846  1.00 16.20 ? 998  ARG   B NH2   1 
ATOM   16315 N  N     . ASN   B  1  1001 ? 10.023  34.208  93.378  1.00 14.12 ? 999  ASN   B N     1 
ATOM   16316 C  CA    . ASN   B  1  1001 ? 11.336  34.166  92.754  1.00 14.13 ? 999  ASN   B CA    1 
ATOM   16317 C  C     . ASN   B  1  1001 ? 11.452  35.285  91.714  1.00 13.89 ? 999  ASN   B C     1 
ATOM   16318 O  O     . ASN   B  1  1001 ? 10.469  35.940  91.352  1.00 15.27 ? 999  ASN   B O     1 
ATOM   16319 C  CB    . ASN   B  1  1001 ? 11.618  32.774  92.178  1.00 16.07 ? 999  ASN   B CB    1 
ATOM   16320 C  CG    . ASN   B  1  1001 ? 10.782  32.447  90.958  1.00 17.24 ? 999  ASN   B CG    1 
ATOM   16321 O  OD1   . ASN   B  1  1001 ? 10.638  33.254  90.044  1.00 16.61 ? 999  ASN   B OD1   1 
ATOM   16322 N  ND2   . ASN   B  1  1001 ? 10.241  31.234  90.927  1.00 26.87 ? 999  ASN   B ND2   1 
ATOM   16323 N  N     . ILE   B  1  1002 ? 12.664  35.505  91.227  1.00 14.25 ? 1000 ILE   B N     1 
ATOM   16324 C  CA    . ILE   B  1  1002 ? 12.906  36.618  90.319  1.00 15.75 ? 1000 ILE   B CA    1 
ATOM   16325 C  C     . ILE   B  1  1002 ? 13.206  36.149  88.903  1.00 15.96 ? 1000 ILE   B C     1 
ATOM   16326 O  O     . ILE   B  1  1002 ? 13.813  36.881  88.125  1.00 17.32 ? 1000 ILE   B O     1 
ATOM   16327 C  CB    . ILE   B  1  1002 ? 13.990  37.574  90.838  1.00 14.35 ? 1000 ILE   B CB    1 
ATOM   16328 C  CG1   . ILE   B  1  1002 ? 15.375  36.912  90.869  1.00 15.18 ? 1000 ILE   B CG1   1 
ATOM   16329 C  CG2   . ILE   B  1  1002 ? 13.598  38.107  92.197  1.00 14.67 ? 1000 ILE   B CG2   1 
ATOM   16330 C  CD1   . ILE   B  1  1002 ? 16.475  37.913  91.085  1.00 15.49 ? 1000 ILE   B CD1   1 
ATOM   16331 N  N     . ILE   B  1  1003 ? 12.799  34.941  88.550  1.00 15.71 ? 1001 ILE   B N     1 
ATOM   16332 C  CA    . ILE   B  1  1003 ? 13.163  34.414  87.244  1.00 17.65 ? 1001 ILE   B CA    1 
ATOM   16333 C  C     . ILE   B  1  1003 ? 11.974  34.346  86.291  1.00 22.27 ? 1001 ILE   B C     1 
ATOM   16334 O  O     . ILE   B  1  1003 ? 12.089  33.774  85.201  1.00 21.89 ? 1001 ILE   B O     1 
ATOM   16335 C  CB    . ILE   B  1  1003 ? 13.933  33.095  87.366  1.00 19.21 ? 1001 ILE   B CB    1 
ATOM   16336 C  CG1   . ILE   B  1  1003 ? 13.122  32.086  88.152  1.00 24.81 ? 1001 ILE   B CG1   1 
ATOM   16337 C  CG2   . ILE   B  1  1003 ? 15.287  33.360  88.052  1.00 17.96 ? 1001 ILE   B CG2   1 
ATOM   16338 C  CD1   . ILE   B  1  1003 ? 13.717  30.734  88.106  1.00 30.65 ? 1001 ILE   B CD1   1 
ATOM   16339 N  N     . GLY   B  1  1004 ? 10.849  34.962  86.652  1.00 19.05 ? 1002 GLY   B N     1 
ATOM   16340 C  CA    . GLY   B  1  1004 ? 9.660   34.908  85.816  1.00 18.94 ? 1002 GLY   B CA    1 
ATOM   16341 C  C     . GLY   B  1  1004 ? 9.798   35.752  84.564  1.00 19.18 ? 1002 GLY   B C     1 
ATOM   16342 O  O     . GLY   B  1  1004 ? 10.094  36.951  84.618  1.00 20.29 ? 1002 GLY   B O     1 
ATOM   16343 N  N     . ALA   B  1  1005 ? 9.566   35.123  83.429  1.00 18.23 ? 1003 ALA   B N     1 
ATOM   16344 C  CA    . ALA   B  1  1005 ? 9.591   35.812  82.161  1.00 18.66 ? 1003 ALA   B CA    1 
ATOM   16345 C  C     . ALA   B  1  1005 ? 8.430   35.320  81.324  1.00 19.91 ? 1003 ALA   B C     1 
ATOM   16346 O  O     . ALA   B  1  1005 ? 8.551   35.129  80.108  1.00 21.28 ? 1003 ALA   B O     1 
ATOM   16347 C  CB    . ALA   B  1  1005 ? 10.920  35.595  81.435  1.00 20.30 ? 1003 ALA   B CB    1 
ATOM   16348 N  N     . VAL   B  1  1006 ? 7.289   35.073  81.967  1.00 15.55 ? 1004 VAL   B N     1 
ATOM   16349 C  CA    . VAL   B  1  1006 ? 6.172   34.500  81.234  1.00 16.99 ? 1004 VAL   B CA    1 
ATOM   16350 C  C     . VAL   B  1  1006 ? 5.741   35.484  80.165  1.00 15.77 ? 1004 VAL   B C     1 
ATOM   16351 O  O     . VAL   B  1  1006 ? 5.428   36.646  80.451  1.00 15.63 ? 1004 VAL   B O     1 
ATOM   16352 C  CB    . VAL   B  1  1006 ? 5.030   34.123  82.170  1.00 16.96 ? 1004 VAL   B CB    1 
ATOM   16353 C  CG1   . VAL   B  1  1006 ? 3.839   33.619  81.347  1.00 17.32 ? 1004 VAL   B CG1   1 
ATOM   16354 C  CG2   . VAL   B  1  1006 ? 5.490   33.043  83.137  1.00 17.62 ? 1004 VAL   B CG2   1 
ATOM   16355 N  N     . VAL   B  1  1007 ? 5.775   35.022  78.918  1.00 16.10 ? 1005 VAL   B N     1 
ATOM   16356 C  CA    . VAL   B  1  1007 ? 5.511   35.883  77.780  1.00 15.11 ? 1005 VAL   B CA    1 
ATOM   16357 C  C     . VAL   B  1  1007 ? 4.144   36.534  77.924  1.00 16.06 ? 1005 VAL   B C     1 
ATOM   16358 O  O     . VAL   B  1  1007 ? 3.145   35.874  78.230  1.00 15.42 ? 1005 VAL   B O     1 
ATOM   16359 C  CB    . VAL   B  1  1007 ? 5.613   35.037  76.508  1.00 15.04 ? 1005 VAL   B CB    1 
ATOM   16360 C  CG1   . VAL   B  1  1007 ? 5.217   35.859  75.320  1.00 16.81 ? 1005 VAL   B CG1   1 
ATOM   16361 C  CG2   . VAL   B  1  1007 ? 7.032   34.535  76.360  1.00 16.00 ? 1005 VAL   B CG2   1 
ATOM   16362 N  N     . GLY   B  1  1008 ? 4.096   37.850  77.719  1.00 15.06 ? 1006 GLY   B N     1 
ATOM   16363 C  CA    . GLY   B  1  1008 ? 2.853   38.581  77.814  1.00 15.38 ? 1006 GLY   B CA    1 
ATOM   16364 C  C     . GLY   B  1  1008 ? 2.289   38.710  79.211  1.00 15.85 ? 1006 GLY   B C     1 
ATOM   16365 O  O     . GLY   B  1  1008 ? 1.187   39.259  79.371  1.00 17.94 ? 1006 GLY   B O     1 
ATOM   16366 N  N     . VAL   B  1  1009 ? 2.989   38.199  80.218  1.00 15.72 ? 1007 VAL   B N     1 
ATOM   16367 C  CA    . VAL   B  1  1009 ? 2.565   38.274  81.610  1.00 14.99 ? 1007 VAL   B CA    1 
ATOM   16368 C  C     . VAL   B  1  1009 ? 3.605   39.002  82.449  1.00 15.99 ? 1007 VAL   B C     1 
ATOM   16369 O  O     . VAL   B  1  1009 ? 3.287   39.962  83.158  1.00 16.08 ? 1007 VAL   B O     1 
ATOM   16370 C  CB    . VAL   B  1  1009 ? 2.277   36.871  82.179  1.00 15.82 ? 1007 VAL   B CB    1 
ATOM   16371 C  CG1   . VAL   B  1  1009 ? 1.830   36.965  83.626  1.00 15.42 ? 1007 VAL   B CG1   1 
ATOM   16372 C  CG2   . VAL   B  1  1009 ? 1.216   36.184  81.334  1.00 16.83 ? 1007 VAL   B CG2   1 
ATOM   16373 N  N     . GLN   B  1  1010 ? 4.869   38.587  82.337  1.00 15.72 ? 1008 GLN   B N     1 
ATOM   16374 C  CA    . GLN   B  1  1010 ? 6.023   39.399  82.724  1.00 15.52 ? 1008 GLN   B CA    1 
ATOM   16375 C  C     . GLN   B  1  1010 ? 6.830   39.688  81.463  1.00 16.41 ? 1008 GLN   B C     1 
ATOM   16376 O  O     . GLN   B  1  1010 ? 7.865   39.055  81.233  1.00 16.57 ? 1008 GLN   B O     1 
ATOM   16377 C  CB    . GLN   B  1  1010 ? 6.907   38.712  83.765  1.00 17.24 ? 1008 GLN   B CB    1 
ATOM   16378 C  CG    . GLN   B  1  1010 ? 6.188   38.357  85.048  1.00 16.81 ? 1008 GLN   B CG    1 
ATOM   16379 C  CD    . GLN   B  1  1010 ? 5.778   36.908  85.095  1.00 17.08 ? 1008 GLN   B CD    1 
ATOM   16380 O  OE1   . GLN   B  1  1010 ? 6.475   36.033  84.602  1.00 17.31 ? 1008 GLN   B OE1   1 
ATOM   16381 N  NE2   . GLN   B  1  1010 ? 4.638   36.647  85.708  1.00 16.23 ? 1008 GLN   B NE2   1 
ATOM   16382 N  N     . PRO   B  1  1011 ? 6.397   40.639  80.631  1.00 14.93 ? 1009 PRO   B N     1 
ATOM   16383 C  CA    . PRO   B  1  1011 ? 7.260   41.099  79.536  1.00 15.95 ? 1009 PRO   B CA    1 
ATOM   16384 C  C     . PRO   B  1  1011 ? 8.629   41.382  80.116  1.00 13.66 ? 1009 PRO   B C     1 
ATOM   16385 O  O     . PRO   B  1  1011 ? 8.752   42.005  81.171  1.00 13.54 ? 1009 PRO   B O     1 
ATOM   16386 C  CB    . PRO   B  1  1011 ? 6.584   42.393  79.083  1.00 15.45 ? 1009 PRO   B CB    1 
ATOM   16387 C  CG    . PRO   B  1  1011 ? 5.140   42.153  79.375  1.00 15.68 ? 1009 PRO   B CG    1 
ATOM   16388 C  CD    . PRO   B  1  1011 ? 5.154   41.425  80.710  1.00 16.40 ? 1009 PRO   B CD    1 
ATOM   16389 N  N     . PHE   B  1  1012 ? 9.654   40.877  79.458  1.00 13.46 ? 1010 PHE   B N     1 
ATOM   16390 C  CA    . PHE   B  1  1012 ? 10.941  40.712  80.102  1.00 13.44 ? 1010 PHE   B CA    1 
ATOM   16391 C  C     . PHE   B  1  1012 ? 11.985  41.585  79.432  1.00 13.77 ? 1010 PHE   B C     1 
ATOM   16392 O  O     . PHE   B  1  1012 ? 12.124  41.578  78.208  1.00 14.89 ? 1010 PHE   B O     1 
ATOM   16393 C  CB    . PHE   B  1  1012 ? 11.378  39.253  80.096  1.00 12.95 ? 1010 PHE   B CB    1 
ATOM   16394 C  CG    . PHE   B  1  1012 ? 12.613  39.032  80.887  1.00 13.52 ? 1010 PHE   B CG    1 
ATOM   16395 C  CD1   . PHE   B  1  1012 ? 12.532  38.853  82.254  1.00 15.17 ? 1010 PHE   B CD1   1 
ATOM   16396 C  CD2   . PHE   B  1  1012 ? 13.863  39.051  80.293  1.00 15.58 ? 1010 PHE   B CD2   1 
ATOM   16397 C  CE1   . PHE   B  1  1012 ? 13.673  38.672  83.010  1.00 14.67 ? 1010 PHE   B CE1   1 
ATOM   16398 C  CE2   . PHE   B  1  1012 ? 15.008  38.879  81.054  1.00 15.65 ? 1010 PHE   B CE2   1 
ATOM   16399 C  CZ    . PHE   B  1  1012 ? 14.906  38.690  82.413  1.00 15.65 ? 1010 PHE   B CZ    1 
ATOM   16400 N  N     . GLY   B  1  1013 ? 12.728  42.309  80.233  1.00 13.82 ? 1011 GLY   B N     1 
ATOM   16401 C  CA    . GLY   B  1  1013 ? 13.858  43.061  79.727  1.00 13.33 ? 1011 GLY   B CA    1 
ATOM   16402 C  C     . GLY   B  1  1013 ? 14.116  44.226  80.642  1.00 13.60 ? 1011 GLY   B C     1 
ATOM   16403 O  O     . GLY   B  1  1013 ? 13.212  44.737  81.309  1.00 14.93 ? 1011 GLY   B O     1 
ATOM   16404 N  N     . GLY   B  1  1014 ? 15.374  44.645  80.675  1.00 15.30 ? 1012 GLY   B N     1 
ATOM   16405 C  CA    . GLY   B  1  1014 ? 15.744  45.689  81.592  1.00 17.13 ? 1012 GLY   B CA    1 
ATOM   16406 C  C     . GLY   B  1  1014 ? 16.302  46.934  80.956  1.00 17.44 ? 1012 GLY   B C     1 
ATOM   16407 O  O     . GLY   B  1  1014 ? 16.189  47.150  79.747  1.00 18.05 ? 1012 GLY   B O     1 
ATOM   16408 N  N     . ARG   B  1  1015 ? 16.938  47.749  81.786  1.00 16.20 ? 1013 ARG   B N     1 
ATOM   16409 C  CA    . ARG   B  1  1015 ? 17.420  49.063  81.417  1.00 16.35 ? 1013 ARG   B CA    1 
ATOM   16410 C  C     . ARG   B  1  1015 ? 18.881  49.168  81.821  1.00 15.73 ? 1013 ARG   B C     1 
ATOM   16411 O  O     . ARG   B  1  1015 ? 19.458  48.240  82.391  1.00 15.42 ? 1013 ARG   B O     1 
ATOM   16412 C  CB    . ARG   B  1  1015 ? 16.601  50.149  82.125  1.00 16.78 ? 1013 ARG   B CB    1 
ATOM   16413 C  CG    . ARG   B  1  1015 ? 16.615  50.004  83.642  1.00 17.39 ? 1013 ARG   B CG    1 
ATOM   16414 C  CD    . ARG   B  1  1015 ? 16.546  51.362  84.331  1.00 19.76 ? 1013 ARG   B CD    1 
ATOM   16415 N  NE    . ARG   B  1  1015 ? 17.851  52.019  84.331  1.00 23.36 ? 1013 ARG   B NE    1 
ATOM   16416 C  CZ    . ARG   B  1  1015 ? 18.872  51.674  85.107  1.00 23.10 ? 1013 ARG   B CZ    1 
ATOM   16417 N  NH1   . ARG   B  1  1015 ? 18.774  50.689  85.989  1.00 21.97 ? 1013 ARG   B NH1   1 
ATOM   16418 N  NH2   . ARG   B  1  1015 ? 20.026  52.325  84.989  1.00 26.13 ? 1013 ARG   B NH2   1 
ATOM   16419 N  N     . GLY   B  1  1016 ? 19.467  50.330  81.550  1.00 16.45 ? 1014 GLY   B N     1 
ATOM   16420 C  CA    . GLY   B  1  1016 ? 20.869  50.529  81.874  1.00 15.90 ? 1014 GLY   B CA    1 
ATOM   16421 C  C     . GLY   B  1  1016 ? 21.718  49.549  81.101  1.00 17.37 ? 1014 GLY   B C     1 
ATOM   16422 O  O     . GLY   B  1  1016 ? 21.502  49.325  79.907  1.00 17.86 ? 1014 GLY   B O     1 
ATOM   16423 N  N     . LEU   B  1  1017 ? 22.678  48.933  81.791  1.00 16.01 ? 1015 LEU   B N     1 
ATOM   16424 C  CA    . LEU   B  1  1017 ? 23.520  47.927  81.168  1.00 17.15 ? 1015 LEU   B CA    1 
ATOM   16425 C  C     . LEU   B  1  1017 ? 22.779  46.653  80.830  1.00 16.46 ? 1015 LEU   B C     1 
ATOM   16426 O  O     . LEU   B  1  1017 ? 23.384  45.762  80.225  1.00 16.63 ? 1015 LEU   B O     1 
ATOM   16427 C  CB    . LEU   B  1  1017 ? 24.701  47.583  82.073  1.00 17.04 ? 1015 LEU   B CB    1 
ATOM   16428 C  CG    . LEU   B  1  1017 ? 25.636  48.740  82.438  1.00 19.57 ? 1015 LEU   B CG    1 
ATOM   16429 C  CD1   . LEU   B  1  1017 ? 26.694  48.282  83.430  1.00 20.24 ? 1015 LEU   B CD1   1 
ATOM   16430 C  CD2   . LEU   B  1  1017 ? 26.277  49.279  81.184  1.00 19.96 ? 1015 LEU   B CD2   1 
ATOM   16431 N  N     . SER   B  1  1018 ? 21.494  46.544  81.179  1.00 14.25 ? 1016 SER   B N     1 
ATOM   16432 C  CA    . SER   B  1  1018 ? 20.731  45.327  80.964  1.00 14.61 ? 1016 SER   B CA    1 
ATOM   16433 C  C     . SER   B  1  1018 ? 19.900  45.335  79.696  1.00 13.50 ? 1016 SER   B C     1 
ATOM   16434 O  O     . SER   B  1  1018 ? 19.410  44.279  79.312  1.00 15.05 ? 1016 SER   B O     1 
ATOM   16435 C  CB    . SER   B  1  1018 ? 19.796  45.070  82.143  1.00 15.23 ? 1016 SER   B CB    1 
ATOM   16436 O  OG    . SER   B  1  1018 ? 20.576  44.887  83.303  1.00 15.39 ? 1016 SER   B OG    1 
ATOM   16437 N  N     . GLY   B  1  1019 ? 19.735  46.457  79.021  1.00 14.44 ? 1017 GLY   B N     1 
ATOM   16438 C  CA    . GLY   B  1  1019 ? 18.932  46.389  77.813  1.00 15.24 ? 1017 GLY   B CA    1 
ATOM   16439 C  C     . GLY   B  1  1019 ? 18.718  47.730  77.166  1.00 14.70 ? 1017 GLY   B C     1 
ATOM   16440 O  O     . GLY   B  1  1019 ? 18.764  48.776  77.815  1.00 17.31 ? 1017 GLY   B O     1 
ATOM   16441 N  N     . THR   B  1  1020 ? 18.445  47.669  75.862  1.00 15.17 ? 1018 THR   B N     1 
ATOM   16442 C  CA    . THR   B  1  1020 ? 17.901  48.800  75.135  1.00 15.81 ? 1018 THR   B CA    1 
ATOM   16443 C  C     . THR   B  1  1020 ? 16.389  48.821  75.166  1.00 15.94 ? 1018 THR   B C     1 
ATOM   16444 O  O     . THR   B  1  1020 ? 15.793  49.883  74.974  1.00 16.28 ? 1018 THR   B O     1 
ATOM   16445 C  CB    . THR   B  1  1020 ? 18.295  48.712  73.656  1.00 14.88 ? 1018 THR   B CB    1 
ATOM   16446 O  OG1   . THR   B  1  1020 ? 17.885  47.441  73.121  1.00 14.86 ? 1018 THR   B OG1   1 
ATOM   16447 C  CG2   . THR   B  1  1020 ? 19.816  48.844  73.490  1.00 14.66 ? 1018 THR   B CG2   1 
ATOM   16448 N  N     . GLY   B  1  1021 ? 15.769  47.672  75.364  1.00 15.47 ? 1019 GLY   B N     1 
ATOM   16449 C  CA    . GLY   B  1  1021 ? 14.371  47.535  75.073  1.00 14.80 ? 1019 GLY   B CA    1 
ATOM   16450 C  C     . GLY   B  1  1021 ? 14.163  47.563  73.572  1.00 15.04 ? 1019 GLY   B C     1 
ATOM   16451 O  O     . GLY   B  1  1021 ? 15.109  47.709  72.793  1.00 15.26 ? 1019 GLY   B O     1 
ATOM   16452 N  N     . PRO   B  1  1022 ? 12.925  47.405  73.143  1.00 14.83 ? 1020 PRO   B N     1 
ATOM   16453 C  CA    . PRO   B  1  1022 ? 11.736  47.128  73.955  1.00 14.43 ? 1020 PRO   B CA    1 
ATOM   16454 C  C     . PRO   B  1  1022 ? 11.788  45.711  74.514  1.00 16.02 ? 1020 PRO   B C     1 
ATOM   16455 O  O     . PRO   B  1  1022 ? 12.581  44.877  74.084  1.00 16.86 ? 1020 PRO   B O     1 
ATOM   16456 C  CB    . PRO   B  1  1022 ? 10.596  47.286  72.947  1.00 17.03 ? 1020 PRO   B CB    1 
ATOM   16457 C  CG    . PRO   B  1  1022 ? 11.209  46.857  71.639  1.00 16.00 ? 1020 PRO   B CG    1 
ATOM   16458 C  CD    . PRO   B  1  1022 ? 12.619  47.414  71.702  1.00 15.63 ? 1020 PRO   B CD    1 
ATOM   16459 N  N     . LYS   B  1  1023 ? 10.948  45.432  75.503  1.00 14.26 ? 1021 LYS   B N     1 
ATOM   16460 C  CA    . LYS   B  1  1023 ? 10.960  44.131  76.144  1.00 14.13 ? 1021 LYS   B CA    1 
ATOM   16461 C  C     . LYS   B  1  1023 ? 10.478  43.042  75.210  1.00 14.03 ? 1021 LYS   B C     1 
ATOM   16462 O  O     . LYS   B  1  1023 ? 9.424   43.165  74.578  1.00 14.35 ? 1021 LYS   B O     1 
ATOM   16463 C  CB    . LYS   B  1  1023 ? 10.004  44.132  77.323  1.00 14.50 ? 1021 LYS   B CB    1 
ATOM   16464 C  CG    . LYS   B  1  1023 ? 10.452  44.935  78.532  1.00 14.38 ? 1021 LYS   B CG    1 
ATOM   16465 C  CD    . LYS   B  1  1023 ? 9.325   44.876  79.538  1.00 13.27 ? 1021 LYS   B CD    1 
ATOM   16466 C  CE    . LYS   B  1  1023 ? 9.695   45.405  80.902  1.00 15.39 ? 1021 LYS   B CE    1 
ATOM   16467 N  NZ    . LYS   B  1  1023 ? 10.442  44.355  81.628  1.00 14.77 ? 1021 LYS   B NZ    1 
ATOM   16468 N  N     . ALA   B  1  1024 ? 11.198  41.932  75.214  1.00 16.01 ? 1022 ALA   B N     1 
ATOM   16469 C  CA    . ALA   B  1  1024 ? 10.710  40.708  74.609  1.00 15.35 ? 1022 ALA   B CA    1 
ATOM   16470 C  C     . ALA   B  1  1024 ? 9.466   40.237  75.354  1.00 15.23 ? 1022 ALA   B C     1 
ATOM   16471 O  O     . ALA   B  1  1024 ? 9.308   40.459  76.559  1.00 14.67 ? 1022 ALA   B O     1 
ATOM   16472 C  CB    . ALA   B  1  1024 ? 11.805  39.645  74.685  1.00 16.81 ? 1022 ALA   B CB    1 
ATOM   16473 N  N     . GLY   B  1  1025 ? 8.543   39.627  74.617  1.00 13.79 ? 1023 GLY   B N     1 
ATOM   16474 C  CA    . GLY   B  1  1025 ? 7.332   39.141  75.242  1.00 15.78 ? 1023 GLY   B CA    1 
ATOM   16475 C  C     . GLY   B  1  1025 ? 6.428   40.246  75.706  1.00 14.59 ? 1023 GLY   B C     1 
ATOM   16476 O  O     . GLY   B  1  1025 ? 5.554   40.015  76.537  1.00 14.77 ? 1023 GLY   B O     1 
ATOM   16477 N  N     . GLY   B  1  1026 ? 6.614   41.444  75.168  1.00 15.18 ? 1024 GLY   B N     1 
ATOM   16478 C  CA    . GLY   B  1  1026 ? 5.793   42.583  75.484  1.00 15.43 ? 1024 GLY   B CA    1 
ATOM   16479 C  C     . GLY   B  1  1026 ? 5.284   43.239  74.213  1.00 15.01 ? 1024 GLY   B C     1 
ATOM   16480 O  O     . GLY   B  1  1026 ? 5.717   42.935  73.096  1.00 14.60 ? 1024 GLY   B O     1 
ATOM   16481 N  N     . PRO   B  1  1027 ? 4.382   44.200  74.381  1.00 15.08 ? 1025 PRO   B N     1 
ATOM   16482 C  CA    . PRO   B  1  1027 ? 3.625   44.722  73.243  1.00 13.60 ? 1025 PRO   B CA    1 
ATOM   16483 C  C     . PRO   B  1  1027 ? 4.376   45.742  72.409  1.00 13.94 ? 1025 PRO   B C     1 
ATOM   16484 O  O     . PRO   B  1  1027 ? 3.883   46.100  71.337  1.00 14.38 ? 1025 PRO   B O     1 
ATOM   16485 C  CB    . PRO   B  1  1027 ? 2.409   45.364  73.912  1.00 15.42 ? 1025 PRO   B CB    1 
ATOM   16486 C  CG    . PRO   B  1  1027 ? 2.919   45.765  75.256  1.00 16.93 ? 1025 PRO   B CG    1 
ATOM   16487 C  CD    . PRO   B  1  1027 ? 3.885   44.705  75.670  1.00 15.34 ? 1025 PRO   B CD    1 
ATOM   16488 N  N     . LEU   B  1  1028 ? 5.535   46.226  72.854  1.00 14.65 ? 1026 LEU   B N     1 
ATOM   16489 C  CA    . LEU   B  1  1028 ? 6.287   47.191  72.059  1.00 14.41 ? 1026 LEU   B CA    1 
ATOM   16490 C  C     . LEU   B  1  1028 ? 7.281   46.528  71.129  1.00 14.30 ? 1026 LEU   B C     1 
ATOM   16491 O  O     . LEU   B  1  1028 ? 7.864   47.206  70.280  1.00 17.28 ? 1026 LEU   B O     1 
ATOM   16492 C  CB    . LEU   B  1  1028 ? 7.059   48.154  72.960  1.00 14.97 ? 1026 LEU   B CB    1 
ATOM   16493 C  CG    . LEU   B  1  1028 ? 6.211   48.973  73.916  1.00 18.91 ? 1026 LEU   B CG    1 
ATOM   16494 C  CD1   . LEU   B  1  1028 ? 7.085   49.996  74.613  1.00 20.25 ? 1026 LEU   B CD1   1 
ATOM   16495 C  CD2   . LEU   B  1  1028 ? 5.116   49.643  73.159  1.00 21.42 ? 1026 LEU   B CD2   1 
ATOM   16496 N  N     . TYR   B  1  1029 ? 7.457   45.215  71.254  1.00 13.82 ? 1027 TYR   B N     1 
ATOM   16497 C  CA    . TYR   B  1  1029 ? 8.582   44.531  70.629  1.00 14.20 ? 1027 TYR   B CA    1 
ATOM   16498 C  C     . TYR   B  1  1029 ? 8.470   44.537  69.113  1.00 13.91 ? 1027 TYR   B C     1 
ATOM   16499 O  O     . TYR   B  1  1029 ? 9.434   44.881  68.420  1.00 13.65 ? 1027 TYR   B O     1 
ATOM   16500 C  CB    . TYR   B  1  1029 ? 8.594   43.101  71.123  1.00 14.93 ? 1027 TYR   B CB    1 
ATOM   16501 C  CG    . TYR   B  1  1029 ? 9.870   42.327  70.985  1.00 13.81 ? 1027 TYR   B CG    1 
ATOM   16502 C  CD1   . TYR   B  1  1029 ? 11.011  42.678  71.694  1.00 14.73 ? 1027 TYR   B CD1   1 
ATOM   16503 C  CD2   . TYR   B  1  1029 ? 9.903   41.160  70.227  1.00 15.74 ? 1027 TYR   B CD2   1 
ATOM   16504 C  CE1   . TYR   B  1  1029 ? 12.160  41.906  71.611  1.00 14.08 ? 1027 TYR   B CE1   1 
ATOM   16505 C  CE2   . TYR   B  1  1029 ? 11.044  40.386  70.152  1.00 14.82 ? 1027 TYR   B CE2   1 
ATOM   16506 C  CZ    . TYR   B  1  1029 ? 12.153  40.755  70.846  1.00 14.17 ? 1027 TYR   B CZ    1 
ATOM   16507 O  OH    . TYR   B  1  1029 ? 13.245  39.955  70.777  1.00 15.95 ? 1027 TYR   B OH    1 
ATOM   16508 N  N     . LEU   B  1  1030 ? 7.321   44.113  68.577  1.00 13.93 ? 1028 LEU   B N     1 
ATOM   16509 C  CA    . LEU   B  1  1030 ? 7.231   43.968  67.127  1.00 14.22 ? 1028 LEU   B CA    1 
ATOM   16510 C  C     . LEU   B  1  1030 ? 7.412   45.299  66.428  1.00 15.38 ? 1028 LEU   B C     1 
ATOM   16511 O  O     . LEU   B  1  1030 ? 7.948   45.348  65.318  1.00 14.78 ? 1028 LEU   B O     1 
ATOM   16512 C  CB    . LEU   B  1  1030 ? 5.889   43.355  66.745  1.00 14.41 ? 1028 LEU   B CB    1 
ATOM   16513 C  CG    . LEU   B  1  1030 ? 5.668   41.897  67.146  1.00 15.76 ? 1028 LEU   B CG    1 
ATOM   16514 C  CD1   . LEU   B  1  1030 ? 4.325   41.427  66.639  1.00 18.19 ? 1028 LEU   B CD1   1 
ATOM   16515 C  CD2   . LEU   B  1  1030 ? 6.793   41.008  66.602  1.00 17.56 ? 1028 LEU   B CD2   1 
ATOM   16516 N  N     . GLY   B  1  1031 ? 7.007   46.392  67.066  1.00 14.63 ? 1029 GLY   B N     1 
ATOM   16517 C  CA    . GLY   B  1  1031 ? 7.089   47.691  66.431  1.00 15.90 ? 1029 GLY   B CA    1 
ATOM   16518 C  C     . GLY   B  1  1031 ? 8.501   48.153  66.181  1.00 14.90 ? 1029 GLY   B C     1 
ATOM   16519 O  O     . GLY   B  1  1031 ? 8.709   49.073  65.383  1.00 16.80 ? 1029 GLY   B O     1 
ATOM   16520 N  N     . ARG   B  1  1032 ? 9.473   47.539  66.840  1.00 13.65 ? 1030 ARG   B N     1 
ATOM   16521 C  CA    . ARG   B  1  1032 ? 10.863  47.859  66.574  1.00 14.48 ? 1030 ARG   B CA    1 
ATOM   16522 C  C     . ARG   B  1  1032 ? 11.368  47.200  65.301  1.00 15.18 ? 1030 ARG   B C     1 
ATOM   16523 O  O     . ARG   B  1  1032 ? 12.448  47.560  64.815  1.00 16.25 ? 1030 ARG   B O     1 
ATOM   16524 C  CB    . ARG   B  1  1032 ? 11.716  47.410  67.771  1.00 16.03 ? 1030 ARG   B CB    1 
ATOM   16525 C  CG    . ARG   B  1  1032 ? 13.144  47.924  67.771  1.00 16.04 ? 1030 ARG   B CG    1 
ATOM   16526 C  CD    . ARG   B  1  1032 ? 13.196  49.415  68.026  1.00 16.82 ? 1030 ARG   B CD    1 
ATOM   16527 N  NE    . ARG   B  1  1032 ? 14.574  49.842  68.217  1.00 17.22 ? 1030 ARG   B NE    1 
ATOM   16528 C  CZ    . ARG   B  1  1032 ? 15.171  50.806  67.529  1.00 20.42 ? 1030 ARG   B CZ    1 
ATOM   16529 N  NH1   . ARG   B  1  1032 ? 14.544  51.461  66.562  1.00 21.40 ? 1030 ARG   B NH1   1 
ATOM   16530 N  NH2   . ARG   B  1  1032 ? 16.428  51.120  67.825  1.00 20.15 ? 1030 ARG   B NH2   1 
ATOM   16531 N  N     . LEU   B  1  1033 ? 10.623  46.239  64.762  1.00 15.18 ? 1031 LEU   B N     1 
ATOM   16532 C  CA    . LEU   B  1  1033 ? 11.089  45.408  63.665  1.00 14.39 ? 1031 LEU   B CA    1 
ATOM   16533 C  C     . LEU   B  1  1033 ? 10.409  45.782  62.362  1.00 15.74 ? 1031 LEU   B C     1 
ATOM   16534 O  O     . LEU   B  1  1033 ? 10.462  45.012  61.393  1.00 16.30 ? 1031 LEU   B O     1 
ATOM   16535 C  CB    . LEU   B  1  1033 ? 10.844  43.938  63.999  1.00 15.75 ? 1031 LEU   B CB    1 
ATOM   16536 C  CG    . LEU   B  1  1033 ? 11.375  43.557  65.385  1.00 14.65 ? 1031 LEU   B CG    1 
ATOM   16537 C  CD1   . LEU   B  1  1033 ? 11.050  42.116  65.701  1.00 16.38 ? 1031 LEU   B CD1   1 
ATOM   16538 C  CD2   . LEU   B  1  1033 ? 12.873  43.791  65.514  1.00 17.22 ? 1031 LEU   B CD2   1 
ATOM   16539 N  N     . VAL   B  1  1034 ? 9.748   46.936  62.337  1.00 15.36 ? 1032 VAL   B N     1 
ATOM   16540 C  CA    . VAL   B  1  1034 ? 9.130   47.491  61.145  1.00 16.80 ? 1032 VAL   B CA    1 
ATOM   16541 C  C     . VAL   B  1  1034 ? 9.561   48.945  61.062  1.00 16.89 ? 1032 VAL   B C     1 
ATOM   16542 O  O     . VAL   B  1  1034 ? 10.045  49.524  62.034  1.00 19.62 ? 1032 VAL   B O     1 
ATOM   16543 C  CB    . VAL   B  1  1034 ? 7.596   47.365  61.165  1.00 16.18 ? 1032 VAL   B CB    1 
ATOM   16544 C  CG1   . VAL   B  1  1034 ? 7.186   45.904  61.054  1.00 17.84 ? 1032 VAL   B CG1   1 
ATOM   16545 C  CG2   . VAL   B  1  1034 ? 7.037   47.965  62.448  1.00 17.12 ? 1032 VAL   B CG2   1 
ATOM   16546 N  N     . THR   B  1  1035 ? 9.429   49.526  59.869  1.00 19.05 ? 1033 THR   B N     1 
ATOM   16547 C  CA    . THR   B  1  1035 ? 9.945   50.874  59.676  1.00 20.43 ? 1033 THR   B CA    1 
ATOM   16548 C  C     . THR   B  1  1035 ? 9.031   51.940  60.247  1.00 22.31 ? 1033 THR   B C     1 
ATOM   16549 O  O     . THR   B  1  1035 ? 9.490   53.058  60.503  1.00 26.49 ? 1033 THR   B O     1 
ATOM   16550 C  CB    . THR   B  1  1035 ? 10.221  51.142  58.196  1.00 25.42 ? 1033 THR   B CB    1 
ATOM   16551 O  OG1   . THR   B  1  1035 ? 9.088   50.751  57.417  1.00 29.53 ? 1033 THR   B OG1   1 
ATOM   16552 C  CG2   . THR   B  1  1035 ? 11.446  50.358  57.741  1.00 27.35 ? 1033 THR   B CG2   1 
ATOM   16553 N  N     . THR   B  1  1036 ? 7.755   51.623  60.440  1.00 18.99 ? 1034 THR   B N     1 
ATOM   16554 C  CA    . THR   B  1  1036 ? 6.806   52.503  61.106  1.00 22.94 ? 1034 THR   B CA    1 
ATOM   16555 C  C     . THR   B  1  1036 ? 6.123   51.669  62.175  1.00 20.78 ? 1034 THR   B C     1 
ATOM   16556 O  O     . THR   B  1  1036 ? 5.476   50.670  61.855  1.00 20.22 ? 1034 THR   B O     1 
ATOM   16557 C  CB    . THR   B  1  1036 ? 5.765   53.010  60.111  1.00 27.44 ? 1034 THR   B CB    1 
ATOM   16558 O  OG1   . THR   B  1  1036 ? 6.423   53.606  58.986  1.00 33.90 ? 1034 THR   B OG1   1 
ATOM   16559 C  CG2   . THR   B  1  1036 ? 4.861   54.039  60.774  1.00 31.17 ? 1034 THR   B CG2   1 
ATOM   16560 N  N     . ALA   B  1  1037 ? 6.273   52.066  63.436  1.00 20.81 ? 1035 ALA   B N     1 
ATOM   16561 C  CA    . ALA   B  1  1037 ? 5.710   51.271  64.518  1.00 17.68 ? 1035 ALA   B CA    1 
ATOM   16562 C  C     . ALA   B  1  1037 ? 4.189   51.391  64.529  1.00 18.03 ? 1035 ALA   B C     1 
ATOM   16563 O  O     . ALA   B  1  1037 ? 3.647   52.489  64.359  1.00 19.38 ? 1035 ALA   B O     1 
ATOM   16564 C  CB    . ALA   B  1  1037 ? 6.263   51.727  65.864  1.00 21.29 ? 1035 ALA   B CB    1 
ATOM   16565 N  N     . PRO   B  1  1038 ? 3.480   50.292  64.745  1.00 15.84 ? 1036 PRO   B N     1 
ATOM   16566 C  CA    . PRO   B  1  1038 ? 2.040   50.372  64.987  1.00 15.84 ? 1036 PRO   B CA    1 
ATOM   16567 C  C     . PRO   B  1  1038 ? 1.771   50.837  66.408  1.00 16.24 ? 1036 PRO   B C     1 
ATOM   16568 O  O     . PRO   B  1  1038 ? 2.658   50.941  67.248  1.00 16.88 ? 1036 PRO   B O     1 
ATOM   16569 C  CB    . PRO   B  1  1038 ? 1.589   48.922  64.820  1.00 19.43 ? 1036 PRO   B CB    1 
ATOM   16570 C  CG    . PRO   B  1  1038 ? 2.757   48.129  65.281  1.00 20.82 ? 1036 PRO   B CG    1 
ATOM   16571 C  CD    . PRO   B  1  1038 ? 3.974   48.909  64.821  1.00 18.39 ? 1036 PRO   B CD    1 
ATOM   16572 N  N     . VAL   B  1  1039 ? 0.498   51.096  66.671  1.00 18.29 ? 1037 VAL   B N     1 
ATOM   16573 C  CA    . VAL   B  1  1039 ? 0.022   51.390  68.017  1.00 18.48 ? 1037 VAL   B CA    1 
ATOM   16574 C  C     . VAL   B  1  1039 ? -0.261  50.052  68.691  1.00 17.23 ? 1037 VAL   B C     1 
ATOM   16575 O  O     . VAL   B  1  1039 ? -1.155  49.329  68.240  1.00 17.40 ? 1037 VAL   B O     1 
ATOM   16576 C  CB    . VAL   B  1  1039 ? -1.236  52.257  67.973  1.00 17.57 ? 1037 VAL   B CB    1 
ATOM   16577 C  CG1   . VAL   B  1  1039 ? -1.721  52.494  69.394  1.00 20.35 ? 1037 VAL   B CG1   1 
ATOM   16578 C  CG2   . VAL   B  1  1039 ? -0.929  53.565  67.273  1.00 20.08 ? 1037 VAL   B CG2   1 
ATOM   16579 N  N     . PRO   B  1  1040 ? 0.489   49.667  69.709  1.00 16.41 ? 1038 PRO   B N     1 
ATOM   16580 C  CA    . PRO   B  1  1040 ? 0.279   48.358  70.306  1.00 16.58 ? 1038 PRO   B CA    1 
ATOM   16581 C  C     . PRO   B  1  1040 ? -1.078  48.270  70.981  1.00 16.56 ? 1038 PRO   B C     1 
ATOM   16582 O  O     . PRO   B  1  1040 ? -1.677  49.295  71.343  1.00 17.13 ? 1038 PRO   B O     1 
ATOM   16583 C  CB    . PRO   B  1  1040 ? 1.420   48.259  71.332  1.00 18.97 ? 1038 PRO   B CB    1 
ATOM   16584 C  CG    . PRO   B  1  1040 ? 2.455   49.223  70.836  1.00 20.48 ? 1038 PRO   B CG    1 
ATOM   16585 C  CD    . PRO   B  1  1040 ? 1.690   50.346  70.226  1.00 17.73 ? 1038 PRO   B CD    1 
ATOM   16586 N  N     . PRO   B  1  1041 ? -1.593  47.056  71.182  1.00 17.58 ? 1039 PRO   B N     1 
ATOM   16587 C  CA    . PRO   B  1  1041 ? -2.817  46.898  71.970  1.00 17.23 ? 1039 PRO   B CA    1 
ATOM   16588 C  C     . PRO   B  1  1041 ? -2.644  47.536  73.334  1.00 16.94 ? 1039 PRO   B C     1 
ATOM   16589 O  O     . PRO   B  1  1041 ? -1.573  47.452  73.946  1.00 18.17 ? 1039 PRO   B O     1 
ATOM   16590 C  CB    . PRO   B  1  1041 ? -2.978  45.379  72.086  1.00 19.19 ? 1039 PRO   B CB    1 
ATOM   16591 C  CG    . PRO   B  1  1041 ? -2.182  44.824  70.937  1.00 22.36 ? 1039 PRO   B CG    1 
ATOM   16592 C  CD    . PRO   B  1  1041 ? -1.031  45.755  70.773  1.00 19.43 ? 1039 PRO   B CD    1 
ATOM   16593 N  N     . GLN   B  1  1042 ? -3.696  48.211  73.783  1.00 18.39 ? 1040 GLN   B N     1 
ATOM   16594 C  CA    . GLN   B  1  1042 ? -3.779  48.806  75.111  1.00 18.82 ? 1040 GLN   B CA    1 
ATOM   16595 C  C     . GLN   B  1  1042 ? -2.779  49.926  75.334  1.00 17.50 ? 1040 GLN   B C     1 
ATOM   16596 O  O     . GLN   B  1  1042 ? -2.601  50.371  76.470  1.00 18.71 ? 1040 GLN   B O     1 
ATOM   16597 C  CB    . GLN   B  1  1042 ? -3.619  47.761  76.221  1.00 20.97 ? 1040 GLN   B CB    1 
ATOM   16598 C  CG    . GLN   B  1  1042 ? -4.652  46.657  76.167  1.00 27.23 ? 1040 GLN   B CG    1 
ATOM   16599 C  CD    . GLN   B  1  1042 ? -4.465  45.672  77.303  1.00 30.26 ? 1040 GLN   B CD    1 
ATOM   16600 O  OE1   . GLN   B  1  1042 ? -3.427  45.018  77.407  1.00 40.61 ? 1040 GLN   B OE1   1 
ATOM   16601 N  NE2   . GLN   B  1  1042 ? -5.453  45.591  78.180  1.00 42.46 ? 1040 GLN   B NE2   1 
ATOM   16602 N  N     . HIS   B  1  1043 ? -2.112  50.398  74.293  1.00 17.28 ? 1041 HIS   B N     1 
ATOM   16603 C  CA    . HIS   B  1  1043 ? -1.006  51.330  74.472  1.00 16.90 ? 1041 HIS   B CA    1 
ATOM   16604 C  C     . HIS   B  1  1043 ? -1.532  52.753  74.383  1.00 16.26 ? 1041 HIS   B C     1 
ATOM   16605 O  O     . HIS   B  1  1043 ? -1.622  53.343  73.307  1.00 18.56 ? 1041 HIS   B O     1 
ATOM   16606 C  CB    . HIS   B  1  1043 ? 0.053   51.059  73.417  1.00 16.73 ? 1041 HIS   B CB    1 
ATOM   16607 C  CG    . HIS   B  1  1043 ? 1.240   51.959  73.500  1.00 17.22 ? 1041 HIS   B CG    1 
ATOM   16608 N  ND1   . HIS   B  1  1043 ? 2.318   51.697  74.316  1.00 18.03 ? 1041 HIS   B ND1   1 
ATOM   16609 C  CD2   . HIS   B  1  1043 ? 1.535   53.105  72.841  1.00 19.43 ? 1041 HIS   B CD2   1 
ATOM   16610 C  CE1   . HIS   B  1  1043 ? 3.227   52.643  74.158  1.00 17.99 ? 1041 HIS   B CE1   1 
ATOM   16611 N  NE2   . HIS   B  1  1043 ? 2.779   53.507  73.266  1.00 16.86 ? 1041 HIS   B NE2   1 
ATOM   16612 N  N     . SER   B  1  1044 ? -1.908  53.306  75.530  1.00 14.68 ? 1042 SER   B N     1 
ATOM   16613 C  CA    . SER   B  1  1044 ? -2.341  54.693  75.616  1.00 15.30 ? 1042 SER   B CA    1 
ATOM   16614 C  C     . SER   B  1  1044 ? -2.275  55.083  77.077  1.00 15.72 ? 1042 SER   B C     1 
ATOM   16615 O  O     . SER   B  1  1044 ? -2.129  54.235  77.957  1.00 17.06 ? 1042 SER   B O     1 
ATOM   16616 C  CB    . SER   B  1  1044 ? -3.777  54.872  75.120  1.00 16.76 ? 1042 SER   B CB    1 
ATOM   16617 O  OG    . SER   B  1  1044 ? -4.678  54.206  75.981  1.00 17.53 ? 1042 SER   B OG    1 
ATOM   16618 N  N     . SER   B  1  1045 ? -2.420  56.374  77.327  1.00 15.27 ? 1043 SER   B N     1 
ATOM   16619 C  CA    . SER   B  1  1045 ? -2.500  56.860  78.692  1.00 15.50 ? 1043 SER   B CA    1 
ATOM   16620 C  C     . SER   B  1  1045 ? -3.344  58.115  78.697  1.00 17.02 ? 1043 SER   B C     1 
ATOM   16621 O  O     . SER   B  1  1045 ? -3.278  58.913  77.760  1.00 17.84 ? 1043 SER   B O     1 
ATOM   16622 C  CB    . SER   B  1  1045 ? -1.095  57.218  79.160  1.00 17.05 ? 1043 SER   B CB    1 
ATOM   16623 O  OG    . SER   B  1  1045 ? -1.134  57.817  80.438  1.00 18.14 ? 1043 SER   B OG    1 
ATOM   16624 N  N     . VAL   B  1  1046 ? -4.140  58.296  79.757  1.00 15.90 ? 1044 VAL   B N     1 
ATOM   16625 C  CA    . VAL   B  1  1046 ? -4.907  59.532  79.881  1.00 17.59 ? 1044 VAL   B CA    1 
ATOM   16626 C  C     . VAL   B  1  1046 ? -4.105  60.650  80.513  1.00 18.35 ? 1044 VAL   B C     1 
ATOM   16627 O  O     . VAL   B  1  1046 ? -4.586  61.790  80.574  1.00 18.74 ? 1044 VAL   B O     1 
ATOM   16628 C  CB    . VAL   B  1  1046 ? -6.212  59.314  80.668  1.00 19.36 ? 1044 VAL   B CB    1 
ATOM   16629 C  CG1   . VAL   B  1  1046 ? -7.055  58.273  79.941  1.00 22.11 ? 1044 VAL   B CG1   1 
ATOM   16630 C  CG2   . VAL   B  1  1046 ? -5.912  58.877  82.085  1.00 20.70 ? 1044 VAL   B CG2   1 
ATOM   16631 N  N     . HIS   B  1  1047 ? -2.884  60.366  80.942  1.00 17.57 ? 1045 HIS   B N     1 
ATOM   16632 C  CA    A HIS   B  1  1047 ? -2.086  61.375  81.602  0.51 19.42 ? 1045 HIS   B CA    1 
ATOM   16633 C  CA    B HIS   B  1  1047 ? -2.027  61.335  81.615  0.49 19.42 ? 1045 HIS   B CA    1 
ATOM   16634 C  C     . HIS   B  1  1047 ? -1.282  62.168  80.587  1.00 16.53 ? 1045 HIS   B C     1 
ATOM   16635 O  O     . HIS   B  1  1047 ? -0.796  61.632  79.588  1.00 19.07 ? 1045 HIS   B O     1 
ATOM   16636 C  CB    A HIS   B  1  1047 ? -1.197  60.702  82.635  0.51 19.16 ? 1045 HIS   B CB    1 
ATOM   16637 C  CB    B HIS   B  1  1047 ? -0.984  60.576  82.435  0.49 18.77 ? 1045 HIS   B CB    1 
ATOM   16638 C  CG    A HIS   B  1  1047 ? -1.971  59.829  83.566  0.51 19.00 ? 1045 HIS   B CG    1 
ATOM   16639 C  CG    B HIS   B  1  1047 ? 0.199   61.403  82.848  0.49 17.65 ? 1045 HIS   B CG    1 
ATOM   16640 N  ND1   A HIS   B  1  1047 ? -2.788  60.343  84.548  0.51 20.09 ? 1045 HIS   B ND1   1 
ATOM   16641 N  ND1   B HIS   B  1  1047 ? 0.138   62.330  83.866  0.49 21.28 ? 1045 HIS   B ND1   1 
ATOM   16642 C  CD2   A HIS   B  1  1047 ? -2.108  58.484  83.625  0.51 22.58 ? 1045 HIS   B CD2   1 
ATOM   16643 C  CD2   B HIS   B  1  1047 ? 1.478   61.420  82.398  0.49 18.12 ? 1045 HIS   B CD2   1 
ATOM   16644 C  CE1   A HIS   B  1  1047 ? -3.373  59.349  85.193  0.51 24.29 ? 1045 HIS   B CE1   1 
ATOM   16645 C  CE1   B HIS   B  1  1047 ? 1.324   62.893  84.018  0.49 20.65 ? 1045 HIS   B CE1   1 
ATOM   16646 N  NE2   A HIS   B  1  1047 ? -2.981  58.211  84.649  0.51 20.70 ? 1045 HIS   B NE2   1 
ATOM   16647 N  NE2   B HIS   B  1  1047 ? 2.155   62.359  83.139  0.49 21.36 ? 1045 HIS   B NE2   1 
ATOM   16648 N  N     . THR   B  1  1048 ? -1.177  63.461  80.842  1.00 17.24 ? 1046 THR   B N     1 
ATOM   16649 C  CA    . THR   B  1  1048 ? -0.375  64.342  80.013  1.00 19.49 ? 1046 THR   B CA    1 
ATOM   16650 C  C     . THR   B  1  1048 ? 0.745   64.903  80.871  1.00 16.88 ? 1046 THR   B C     1 
ATOM   16651 O  O     . THR   B  1  1048 ? 0.501   65.419  81.966  1.00 18.81 ? 1046 THR   B O     1 
ATOM   16652 C  CB    . THR   B  1  1048 ? -1.205  65.486  79.448  1.00 20.62 ? 1046 THR   B CB    1 
ATOM   16653 O  OG1   . THR   B  1  1048 ? -2.393  64.967  78.837  1.00 19.18 ? 1046 THR   B OG1   1 
ATOM   16654 C  CG2   . THR   B  1  1048 ? -0.393  66.230  78.399  1.00 21.61 ? 1046 THR   B CG2   1 
ATOM   16655 N  N     . ASP   B  1  1049 ? 1.964   64.790  80.381  1.00 17.07 ? 1047 ASP   B N     1 
ATOM   16656 C  CA    . ASP   B  1  1049 ? 3.085   65.294  81.145  1.00 17.84 ? 1047 ASP   B CA    1 
ATOM   16657 C  C     . ASP   B  1  1049 ? 2.920   66.796  81.351  1.00 16.39 ? 1047 ASP   B C     1 
ATOM   16658 O  O     . ASP   B  1  1049 ? 2.636   67.523  80.393  1.00 17.94 ? 1047 ASP   B O     1 
ATOM   16659 C  CB    . ASP   B  1  1049 ? 4.374   64.997  80.396  1.00 15.75 ? 1047 ASP   B CB    1 
ATOM   16660 C  CG    . ASP   B  1  1049 ? 5.588   65.429  81.169  1.00 17.84 ? 1047 ASP   B CG    1 
ATOM   16661 O  OD1   . ASP   B  1  1049 ? 5.922   66.622  81.075  1.00 18.41 ? 1047 ASP   B OD1   1 
ATOM   16662 O  OD2   . ASP   B  1  1049 ? 6.136   64.599  81.914  1.00 18.79 ? 1047 ASP   B OD2   1 
ATOM   16663 N  N     . PRO   B  1  1050 ? 3.046   67.294  82.581  1.00 18.13 ? 1048 PRO   B N     1 
ATOM   16664 C  CA    . PRO   B  1  1050 ? 2.767   68.715  82.813  1.00 20.45 ? 1048 PRO   B CA    1 
ATOM   16665 C  C     . PRO   B  1  1050 ? 3.845   69.617  82.265  1.00 19.42 ? 1048 PRO   B C     1 
ATOM   16666 O  O     . PRO   B  1  1050 ? 3.560   70.768  81.921  1.00 20.61 ? 1048 PRO   B O     1 
ATOM   16667 C  CB    . PRO   B  1  1050 ? 2.665   68.809  84.342  1.00 23.44 ? 1048 PRO   B CB    1 
ATOM   16668 C  CG    . PRO   B  1  1050 ? 3.486   67.666  84.838  1.00 22.77 ? 1048 PRO   B CG    1 
ATOM   16669 C  CD    . PRO   B  1  1050 ? 3.292   66.556  83.827  1.00 20.10 ? 1048 PRO   B CD    1 
ATOM   16670 N  N     . VAL   B  1  1051 ? 5.081   69.126  82.180  1.00 20.28 ? 1049 VAL   B N     1 
ATOM   16671 C  CA    . VAL   B  1  1051 ? 6.147   69.933  81.600  1.00 19.43 ? 1049 VAL   B CA    1 
ATOM   16672 C  C     . VAL   B  1  1051 ? 5.954   70.054  80.100  1.00 18.64 ? 1049 VAL   B C     1 
ATOM   16673 O  O     . VAL   B  1  1051 ? 6.156   71.124  79.516  1.00 20.35 ? 1049 VAL   B O     1 
ATOM   16674 C  CB    . VAL   B  1  1051 ? 7.515   69.354  81.980  1.00 21.29 ? 1049 VAL   B CB    1 
ATOM   16675 C  CG1   . VAL   B  1  1051 ? 8.621   70.148  81.300  1.00 24.67 ? 1049 VAL   B CG1   1 
ATOM   16676 C  CG2   . VAL   B  1  1051 ? 7.676   69.365  83.502  1.00 23.59 ? 1049 VAL   B CG2   1 
ATOM   16677 N  N     . LEU   B  1  1052 ? 5.529   68.966  79.458  1.00 17.09 ? 1050 LEU   B N     1 
ATOM   16678 C  CA    . LEU   B  1  1052 ? 5.093   69.051  78.069  1.00 17.54 ? 1050 LEU   B CA    1 
ATOM   16679 C  C     . LEU   B  1  1052 ? 4.045   70.146  77.895  1.00 20.56 ? 1050 LEU   B C     1 
ATOM   16680 O  O     . LEU   B  1  1052 ? 4.134   70.973  76.981  1.00 19.60 ? 1050 LEU   B O     1 
ATOM   16681 C  CB    . LEU   B  1  1052 ? 4.554   67.691  77.614  1.00 17.45 ? 1050 LEU   B CB    1 
ATOM   16682 C  CG    . LEU   B  1  1052 ? 4.038   67.557  76.171  1.00 16.84 ? 1050 LEU   B CG    1 
ATOM   16683 C  CD1   . LEU   B  1  1052 ? 2.635   68.118  75.919  1.00 20.39 ? 1050 LEU   B CD1   1 
ATOM   16684 C  CD2   . LEU   B  1  1052 ? 5.032   68.137  75.159  1.00 18.56 ? 1050 LEU   B CD2   1 
ATOM   16685 N  N     . LEU   B  1  1053 ? 3.040   70.169  78.771  1.00 20.48 ? 1051 LEU   B N     1 
ATOM   16686 C  CA    . LEU   B  1  1053 ? 2.005   71.190  78.661  1.00 22.61 ? 1051 LEU   B CA    1 
ATOM   16687 C  C     . LEU   B  1  1053 ? 2.591   72.591  78.783  1.00 20.67 ? 1051 LEU   B C     1 
ATOM   16688 O  O     . LEU   B  1  1053 ? 2.225   73.492  78.021  1.00 22.74 ? 1051 LEU   B O     1 
ATOM   16689 C  CB    . LEU   B  1  1053 ? 0.921   70.966  79.717  1.00 26.43 ? 1051 LEU   B CB    1 
ATOM   16690 C  CG    . LEU   B  1  1053 ? -0.009  69.778  79.447  1.00 25.34 ? 1051 LEU   B CG    1 
ATOM   16691 C  CD1   . LEU   B  1  1053 ? -0.888  69.526  80.665  1.00 26.01 ? 1051 LEU   B CD1   1 
ATOM   16692 C  CD2   . LEU   B  1  1053 ? -0.852  70.009  78.204  1.00 26.99 ? 1051 LEU   B CD2   1 
ATOM   16693 N  N     . ASP   B  1  1054 ? 3.518   72.790  79.724  1.00 20.92 ? 1052 ASP   B N     1 
ATOM   16694 C  CA    . ASP   B  1  1054 ? 4.133   74.107  79.856  1.00 23.26 ? 1052 ASP   B CA    1 
ATOM   16695 C  C     . ASP   B  1  1054 ? 4.965   74.450  78.629  1.00 20.35 ? 1052 ASP   B C     1 
ATOM   16696 O  O     . ASP   B  1  1054 ? 5.019   75.615  78.222  1.00 22.70 ? 1052 ASP   B O     1 
ATOM   16697 C  CB    . ASP   B  1  1054 ? 4.999   74.162  81.112  1.00 22.70 ? 1052 ASP   B CB    1 
ATOM   16698 C  CG    . ASP   B  1  1054 ? 4.179   74.116  82.381  1.00 27.98 ? 1052 ASP   B CG    1 
ATOM   16699 O  OD1   . ASP   B  1  1054 ? 2.960   74.354  82.295  1.00 28.43 ? 1052 ASP   B OD1   1 
ATOM   16700 O  OD2   . ASP   B  1  1054 ? 4.751   73.850  83.461  1.00 31.47 ? 1052 ASP   B OD2   1 
ATOM   16701 N  N     . PHE   B  1  1055 ? 5.608   73.450  78.034  1.00 20.25 ? 1053 PHE   B N     1 
ATOM   16702 C  CA    . PHE   B  1  1055 ? 6.381   73.682  76.825  1.00 21.28 ? 1053 PHE   B CA    1 
ATOM   16703 C  C     . PHE   B  1  1055 ? 5.473   74.093  75.676  1.00 21.96 ? 1053 PHE   B C     1 
ATOM   16704 O  O     . PHE   B  1  1055 ? 5.785   75.025  74.925  1.00 22.15 ? 1053 PHE   B O     1 
ATOM   16705 C  CB    . PHE   B  1  1055 ? 7.159   72.412  76.497  1.00 19.74 ? 1053 PHE   B CB    1 
ATOM   16706 C  CG    . PHE   B  1  1055 ? 8.085   72.548  75.328  1.00 21.39 ? 1053 PHE   B CG    1 
ATOM   16707 C  CD1   . PHE   B  1  1055 ? 9.071   73.526  75.322  1.00 21.96 ? 1053 PHE   B CD1   1 
ATOM   16708 C  CD2   . PHE   B  1  1055 ? 7.971   71.697  74.233  1.00 19.61 ? 1053 PHE   B CD2   1 
ATOM   16709 C  CE1   . PHE   B  1  1055 ? 9.931   73.657  74.238  1.00 23.31 ? 1053 PHE   B CE1   1 
ATOM   16710 C  CE2   . PHE   B  1  1055 ? 8.826   71.824  73.146  1.00 21.45 ? 1053 PHE   B CE2   1 
ATOM   16711 C  CZ    . PHE   B  1  1055 ? 9.803   72.805  73.152  1.00 21.32 ? 1053 PHE   B CZ    1 
ATOM   16712 N  N     . ALA   B  1  1056 ? 4.322   73.431  75.541  1.00 20.72 ? 1054 ALA   B N     1 
ATOM   16713 C  CA    . ALA   B  1  1056 ? 3.389   73.786  74.480  1.00 22.75 ? 1054 ALA   B CA    1 
ATOM   16714 C  C     . ALA   B  1  1056 ? 2.919   75.228  74.620  1.00 20.90 ? 1054 ALA   B C     1 
ATOM   16715 O  O     . ALA   B  1  1056 ? 2.826   75.956  73.625  1.00 22.42 ? 1054 ALA   B O     1 
ATOM   16716 C  CB    . ALA   B  1  1056 ? 2.197   72.829  74.487  1.00 23.86 ? 1054 ALA   B CB    1 
ATOM   16717 N  N     . LYS   B  1  1057 ? 2.610   75.656  75.845  1.00 23.43 ? 1055 LYS   B N     1 
ATOM   16718 C  CA    . LYS   B  1  1057 ? 2.183   77.037  76.050  1.00 24.98 ? 1055 LYS   B CA    1 
ATOM   16719 C  C     . LYS   B  1  1057 ? 3.293   78.009  75.684  1.00 27.43 ? 1055 LYS   B C     1 
ATOM   16720 O  O     . LYS   B  1  1057 ? 3.039   79.054  75.073  1.00 26.93 ? 1055 LYS   B O     1 
ATOM   16721 C  CB    . LYS   B  1  1057 ? 1.762   77.246  77.501  1.00 27.80 ? 1055 LYS   B CB    1 
ATOM   16722 C  CG    . LYS   B  1  1057 ? 0.414   76.644  77.831  1.00 31.57 ? 1055 LYS   B CG    1 
ATOM   16723 C  CD    . LYS   B  1  1057 ? 0.037   76.946  79.261  1.00 26.81 ? 1055 LYS   B CD    1 
ATOM   16724 C  CE    . LYS   B  1  1057 ? 1.075   76.401  80.217  1.00 29.22 ? 1055 LYS   B CE    1 
ATOM   16725 N  NZ    . LYS   B  1  1057 ? 0.573   76.433  81.615  1.00 31.81 ? 1055 LYS   B NZ    1 
ATOM   16726 N  N     . TRP   B  1  1058 ? 4.530   77.682  76.062  1.00 25.94 ? 1056 TRP   B N     1 
ATOM   16727 C  CA    . TRP   B  1  1058 ? 5.671   78.509  75.685  1.00 27.16 ? 1056 TRP   B CA    1 
ATOM   16728 C  C     . TRP   B  1  1058 ? 5.811   78.594  74.171  1.00 24.10 ? 1056 TRP   B C     1 
ATOM   16729 O  O     . TRP   B  1  1058 ? 5.997   79.686  73.621  1.00 26.63 ? 1056 TRP   B O     1 
ATOM   16730 C  CB    . TRP   B  1  1058 ? 6.932   77.953  76.344  1.00 26.03 ? 1056 TRP   B CB    1 
ATOM   16731 C  CG    . TRP   B  1  1058 ? 8.203   78.693  76.030  1.00 27.06 ? 1056 TRP   B CG    1 
ATOM   16732 C  CD1   . TRP   B  1  1058 ? 8.636   79.864  76.590  1.00 33.61 ? 1056 TRP   B CD1   1 
ATOM   16733 C  CD2   . TRP   B  1  1058 ? 9.211   78.294  75.102  1.00 27.59 ? 1056 TRP   B CD2   1 
ATOM   16734 N  NE1   . TRP   B  1  1058 ? 9.851   80.221  76.054  1.00 31.59 ? 1056 TRP   B NE1   1 
ATOM   16735 C  CE2   . TRP   B  1  1058 ? 10.227  79.274  75.139  1.00 30.68 ? 1056 TRP   B CE2   1 
ATOM   16736 C  CE3   . TRP   B  1  1058 ? 9.353   77.206  74.239  1.00 26.22 ? 1056 TRP   B CE3   1 
ATOM   16737 C  CZ2   . TRP   B  1  1058 ? 11.372  79.191  74.347  1.00 30.62 ? 1056 TRP   B CZ2   1 
ATOM   16738 C  CZ3   . TRP   B  1  1058 ? 10.488  77.128  73.446  1.00 31.72 ? 1056 TRP   B CZ3   1 
ATOM   16739 C  CH2   . TRP   B  1  1058 ? 11.482  78.115  73.509  1.00 29.16 ? 1056 TRP   B CH2   1 
ATOM   16740 N  N     . LEU   B  1  1059 ? 5.704   77.460  73.475  1.00 22.46 ? 1057 LEU   B N     1 
ATOM   16741 C  CA    . LEU   B  1  1059 ? 5.724   77.486  72.017  1.00 26.05 ? 1057 LEU   B CA    1 
ATOM   16742 C  C     . LEU   B  1  1059 ? 4.601   78.355  71.474  1.00 29.02 ? 1057 LEU   B C     1 
ATOM   16743 O  O     . LEU   B  1  1059 ? 4.817   79.159  70.559  1.00 29.89 ? 1057 LEU   B O     1 
ATOM   16744 C  CB    . LEU   B  1  1059 ? 5.630   76.069  71.459  1.00 23.44 ? 1057 LEU   B CB    1 
ATOM   16745 C  CG    . LEU   B  1  1059 ? 6.842   75.172  71.722  1.00 22.33 ? 1057 LEU   B CG    1 
ATOM   16746 C  CD1   . LEU   B  1  1059 ? 6.535   73.762  71.297  1.00 22.50 ? 1057 LEU   B CD1   1 
ATOM   16747 C  CD2   . LEU   B  1  1059 ? 8.094   75.684  71.000  1.00 26.90 ? 1057 LEU   B CD2   1 
ATOM   16748 N  N     . ASP   B  1  1060 ? 3.388   78.197  72.024  1.00 28.69 ? 1058 ASP   B N     1 
ATOM   16749 C  CA    . ASP   B  1  1060 ? 2.260   79.049  71.645  1.00 28.73 ? 1058 ASP   B CA    1 
ATOM   16750 C  C     . ASP   B  1  1060 ? 2.646   80.520  71.723  1.00 31.34 ? 1058 ASP   B C     1 
ATOM   16751 O  O     . ASP   B  1  1060 ? 2.440   81.284  70.772  1.00 34.99 ? 1058 ASP   B O     1 
ATOM   16752 C  CB    . ASP   B  1  1060 ? 1.078   78.814  72.598  1.00 31.67 ? 1058 ASP   B CB    1 
ATOM   16753 C  CG    . ASP   B  1  1060 ? 0.285   77.545  72.296  1.00 35.28 ? 1058 ASP   B CG    1 
ATOM   16754 O  OD1   . ASP   B  1  1060 ? 0.224   77.112  71.127  1.00 33.16 ? 1058 ASP   B OD1   1 
ATOM   16755 O  OD2   . ASP   B  1  1060 ? -0.317  76.999  73.256  1.00 36.00 ? 1058 ASP   B OD2   1 
ATOM   16756 N  N     . GLY   B  1  1061 ? 3.198   80.934  72.867  1.00 30.11 ? 1059 GLY   B N     1 
ATOM   16757 C  CA    . GLY   B  1  1061 ? 3.534   82.333  73.065  1.00 34.62 ? 1059 GLY   B CA    1 
ATOM   16758 C  C     . GLY   B  1  1061 ? 4.563   82.853  72.082  1.00 34.95 ? 1059 GLY   B C     1 
ATOM   16759 O  O     . GLY   B  1  1061 ? 4.567   84.042  71.757  1.00 36.32 ? 1059 GLY   B O     1 
ATOM   16760 N  N     . LYS   B  1  1062 ? 5.447   81.978  71.598  1.00 32.48 ? 1060 LYS   B N     1 
ATOM   16761 C  CA    . LYS   B  1  1062 ? 6.439   82.354  70.599  1.00 33.82 ? 1060 LYS   B CA    1 
ATOM   16762 C  C     . LYS   B  1  1062 ? 5.889   82.339  69.185  1.00 36.33 ? 1060 LYS   B C     1 
ATOM   16763 O  O     . LYS   B  1  1062 ? 6.625   82.679  68.252  1.00 42.28 ? 1060 LYS   B O     1 
ATOM   16764 C  CB    . LYS   B  1  1062 ? 7.627   81.394  70.641  1.00 34.14 ? 1060 LYS   B CB    1 
ATOM   16765 C  CG    . LYS   B  1  1062 ? 8.394   81.406  71.924  1.00 35.85 ? 1060 LYS   B CG    1 
ATOM   16766 C  CD    . LYS   B  1  1062 ? 9.630   80.536  71.790  1.00 37.51 ? 1060 LYS   B CD    1 
ATOM   16767 C  CE    . LYS   B  1  1062 ? 10.517  81.004  70.645  1.00 35.37 ? 1060 LYS   B CE    1 
ATOM   16768 N  NZ    . LYS   B  1  1062 ? 11.917  80.548  70.824  1.00 42.02 ? 1060 LYS   B NZ    1 
ATOM   16769 N  N     . GLY   B  1  1063 ? 4.636   81.935  68.996  1.00 33.96 ? 1061 GLY   B N     1 
ATOM   16770 C  CA    . GLY   B  1  1063 ? 4.119   81.785  67.655  1.00 35.93 ? 1061 GLY   B CA    1 
ATOM   16771 C  C     . GLY   B  1  1063 ? 4.627   80.573  66.913  1.00 36.75 ? 1061 GLY   B C     1 
ATOM   16772 O  O     . GLY   B  1  1063 ? 4.385   80.458  65.707  1.00 34.53 ? 1061 GLY   B O     1 
ATOM   16773 N  N     . ALA   B  1  1064 ? 5.330   79.663  67.593  1.00 32.82 ? 1062 ALA   B N     1 
ATOM   16774 C  CA    . ALA   B  1  1064 ? 5.792   78.420  66.977  1.00 30.37 ? 1062 ALA   B CA    1 
ATOM   16775 C  C     . ALA   B  1  1064 ? 4.604   77.462  66.887  1.00 30.81 ? 1062 ALA   B C     1 
ATOM   16776 O  O     . ALA   B  1  1064 ? 4.492   76.474  67.618  1.00 27.02 ? 1062 ALA   B O     1 
ATOM   16777 C  CB    . ALA   B  1  1064 ? 6.950   77.828  67.769  1.00 31.83 ? 1062 ALA   B CB    1 
ATOM   16778 N  N     . ARG   B  1  1065 ? 3.703   77.778  65.952  1.00 30.69 ? 1063 ARG   B N     1 
ATOM   16779 C  CA    . ARG   B  1  1065 ? 2.385   77.148  65.932  1.00 30.82 ? 1063 ARG   B CA    1 
ATOM   16780 C  C     . ARG   B  1  1065 ? 2.478   75.669  65.584  1.00 28.95 ? 1063 ARG   B C     1 
ATOM   16781 O  O     . ARG   B  1  1065 ? 1.869   74.824  66.252  1.00 27.47 ? 1063 ARG   B O     1 
ATOM   16782 C  CB    . ARG   B  1  1065 ? 1.465   77.882  64.952  1.00 33.34 ? 1063 ARG   B CB    1 
ATOM   16783 N  N     . ALA   B  1  1066 ? 3.234   75.334  64.538  1.00 24.28 ? 1064 ALA   B N     1 
ATOM   16784 C  CA    . ALA   B  1  1066 ? 3.379   73.933  64.169  1.00 27.16 ? 1064 ALA   B CA    1 
ATOM   16785 C  C     . ALA   B  1  1066 ? 4.013   73.140  65.301  1.00 26.13 ? 1064 ALA   B C     1 
ATOM   16786 O  O     . ALA   B  1  1066 ? 3.596   72.012  65.590  1.00 26.81 ? 1064 ALA   B O     1 
ATOM   16787 C  CB    . ALA   B  1  1066 ? 4.221   73.809  62.902  1.00 29.07 ? 1064 ALA   B CB    1 
ATOM   16788 N  N     . GLU   B  1  1067 ? 5.022   73.716  65.956  1.00 25.62 ? 1065 GLU   B N     1 
ATOM   16789 C  CA    . GLU   B  1  1067 ? 5.709   73.003  67.026  1.00 25.08 ? 1065 GLU   B CA    1 
ATOM   16790 C  C     . GLU   B  1  1067 ? 4.806   72.821  68.239  1.00 22.21 ? 1065 GLU   B C     1 
ATOM   16791 O  O     . GLU   B  1  1067 ? 4.815   71.756  68.869  1.00 21.52 ? 1065 GLU   B O     1 
ATOM   16792 C  CB    . GLU   B  1  1067 ? 6.995   73.740  67.406  1.00 25.44 ? 1065 GLU   B CB    1 
ATOM   16793 C  CG    . GLU   B  1  1067 ? 8.070   73.695  66.324  1.00 24.99 ? 1065 GLU   B CG    1 
ATOM   16794 C  CD    . GLU   B  1  1067 ? 7.854   74.710  65.214  1.00 28.90 ? 1065 GLU   B CD    1 
ATOM   16795 O  OE1   . GLU   B  1  1067 ? 6.961   75.572  65.341  1.00 28.52 ? 1065 GLU   B OE1   1 
ATOM   16796 O  OE2   . GLU   B  1  1067 ? 8.588   74.641  64.205  1.00 28.02 ? 1065 GLU   B OE2   1 
ATOM   16797 N  N     . ALA   B  1  1068 ? 4.039   73.855  68.589  1.00 22.95 ? 1066 ALA   B N     1 
ATOM   16798 C  CA    . ALA   B  1  1068 ? 3.088   73.728  69.688  1.00 23.71 ? 1066 ALA   B CA    1 
ATOM   16799 C  C     . ALA   B  1  1068 ? 2.072   72.634  69.401  1.00 23.13 ? 1066 ALA   B C     1 
ATOM   16800 O  O     . ALA   B  1  1068 ? 1.730   71.848  70.293  1.00 22.16 ? 1066 ALA   B O     1 
ATOM   16801 C  CB    . ALA   B  1  1068 ? 2.382   75.060  69.925  1.00 23.66 ? 1066 ALA   B CB    1 
ATOM   16802 N  N     . GLU   B  1  1069 ? 1.587   72.561  68.161  1.00 22.05 ? 1067 GLU   B N     1 
ATOM   16803 C  CA    . GLU   B  1  1069 ? 0.672   71.491  67.782  1.00 25.59 ? 1067 GLU   B CA    1 
ATOM   16804 C  C     . GLU   B  1  1069 ? 1.338   70.127  67.910  1.00 24.63 ? 1067 GLU   B C     1 
ATOM   16805 O  O     . GLU   B  1  1069 ? 0.747   69.180  68.445  1.00 23.79 ? 1067 GLU   B O     1 
ATOM   16806 C  CB    . GLU   B  1  1069 ? 0.163   71.723  66.357  1.00 26.88 ? 1067 GLU   B CB    1 
ATOM   16807 C  CG    . GLU   B  1  1069 ? -0.690  70.591  65.796  1.00 28.57 ? 1067 GLU   B CG    1 
ATOM   16808 C  CD    . GLU   B  1  1069 ? -2.069  70.500  66.440  1.00 37.64 ? 1067 GLU   B CD    1 
ATOM   16809 O  OE1   . GLU   B  1  1069 ? -2.447  71.414  67.205  1.00 37.99 ? 1067 GLU   B OE1   1 
ATOM   16810 O  OE2   . GLU   B  1  1069 ? -2.779  69.507  66.176  1.00 46.98 ? 1067 GLU   B OE2   1 
ATOM   16811 N  N     . ALA   B  1  1070 ? 2.572   70.000  67.413  1.00 22.65 ? 1068 ALA   B N     1 
ATOM   16812 C  CA    . ALA   B  1  1070 ? 3.294   68.745  67.574  1.00 21.09 ? 1068 ALA   B CA    1 
ATOM   16813 C  C     . ALA   B  1  1070 ? 3.474   68.407  69.048  1.00 18.93 ? 1068 ALA   B C     1 
ATOM   16814 O  O     . ALA   B  1  1070 ? 3.360   67.241  69.441  1.00 21.86 ? 1068 ALA   B O     1 
ATOM   16815 C  CB    . ALA   B  1  1070 ? 4.651   68.824  66.868  1.00 25.49 ? 1068 ALA   B CB    1 
ATOM   16816 N  N     . ALA   B  1  1071 ? 3.716   69.419  69.881  1.00 20.87 ? 1069 ALA   B N     1 
ATOM   16817 C  CA    . ALA   B  1  1071 ? 3.881   69.163  71.307  1.00 20.36 ? 1069 ALA   B CA    1 
ATOM   16818 C  C     . ALA   B  1  1071 ? 2.589   68.642  71.922  1.00 20.07 ? 1069 ALA   B C     1 
ATOM   16819 O  O     . ALA   B  1  1071 ? 2.602   67.652  72.664  1.00 19.14 ? 1069 ALA   B O     1 
ATOM   16820 C  CB    . ALA   B  1  1071 ? 4.368   70.416  72.032  1.00 21.07 ? 1069 ALA   B CB    1 
ATOM   16821 N  N     . ARG   B  1  1072 ? 1.461   69.292  71.625  1.00 20.15 ? 1070 ARG   B N     1 
ATOM   16822 C  CA    A ARG   B  1  1072 ? 0.185   68.818  72.155  0.57 20.69 ? 1070 ARG   B CA    1 
ATOM   16823 C  CA    B ARG   B  1  1072 ? 0.191   68.815  72.162  0.43 20.71 ? 1070 ARG   B CA    1 
ATOM   16824 C  C     . ARG   B  1  1072 ? -0.119  67.410  71.668  1.00 21.80 ? 1070 ARG   B C     1 
ATOM   16825 O  O     . ARG   B  1  1072 ? -0.568  66.558  72.446  1.00 20.10 ? 1070 ARG   B O     1 
ATOM   16826 C  CB    A ARG   B  1  1072 ? -0.941  69.775  71.767  0.57 22.50 ? 1070 ARG   B CB    1 
ATOM   16827 C  CB    B ARG   B  1  1072 ? -0.935  69.788  71.815  0.43 22.52 ? 1070 ARG   B CB    1 
ATOM   16828 C  CG    A ARG   B  1  1072 ? -0.931  71.080  72.535  0.57 24.70 ? 1070 ARG   B CG    1 
ATOM   16829 C  CG    B ARG   B  1  1072 ? -0.669  71.186  72.327  0.43 24.29 ? 1070 ARG   B CG    1 
ATOM   16830 C  CD    A ARG   B  1  1072 ? -2.152  71.915  72.186  0.57 25.08 ? 1070 ARG   B CD    1 
ATOM   16831 C  CD    B ARG   B  1  1072 ? -1.922  72.038  72.381  0.43 25.06 ? 1070 ARG   B CD    1 
ATOM   16832 N  NE    A ARG   B  1  1072 ? -2.146  72.320  70.786  0.57 26.46 ? 1070 ARG   B NE    1 
ATOM   16833 N  NE    B ARG   B  1  1072 ? -1.605  73.367  72.886  0.43 25.46 ? 1070 ARG   B NE    1 
ATOM   16834 C  CZ    A ARG   B  1  1072 ? -1.675  73.480  70.350  0.57 27.42 ? 1070 ARG   B CZ    1 
ATOM   16835 C  CZ    B ARG   B  1  1072 ? -1.455  73.663  74.169  0.43 23.32 ? 1070 ARG   B CZ    1 
ATOM   16836 N  NH1   A ARG   B  1  1072 ? -1.198  74.389  71.186  0.57 23.92 ? 1070 ARG   B NH1   1 
ATOM   16837 N  NH1   B ARG   B  1  1072 ? -1.657  72.760  75.118  0.43 25.27 ? 1070 ARG   B NH1   1 
ATOM   16838 N  NH2   A ARG   B  1  1072 ? -1.676  73.730  69.044  0.57 23.06 ? 1070 ARG   B NH2   1 
ATOM   16839 N  NH2   B ARG   B  1  1072 ? -1.093  74.895  74.510  0.43 25.47 ? 1070 ARG   B NH2   1 
ATOM   16840 N  N     . ASN   B  1  1073 ? 0.134   67.141  70.385  1.00 19.45 ? 1071 ASN   B N     1 
ATOM   16841 C  CA    . ASN   B  1  1073 ? -0.113  65.807  69.856  1.00 21.18 ? 1071 ASN   B CA    1 
ATOM   16842 C  C     . ASN   B  1  1073 ? 0.758   64.772  70.547  1.00 20.46 ? 1071 ASN   B C     1 
ATOM   16843 O  O     . ASN   B  1  1073 ? 0.291   63.670  70.861  1.00 22.24 ? 1071 ASN   B O     1 
ATOM   16844 C  CB    . ASN   B  1  1073 ? 0.103   65.792  68.343  1.00 24.47 ? 1071 ASN   B CB    1 
ATOM   16845 C  CG    . ASN   B  1  1073 ? -0.985  66.534  67.607  1.00 27.68 ? 1071 ASN   B CG    1 
ATOM   16846 O  OD1   . ASN   B  1  1073 ? -2.086  66.711  68.131  1.00 29.92 ? 1071 ASN   B OD1   1 
ATOM   16847 N  ND2   . ASN   B  1  1073 ? -0.688  66.980  66.393  1.00 32.32 ? 1071 ASN   B ND2   1 
ATOM   16848 N  N     . ALA   B  1  1074 ? 2.034   65.098  70.776  1.00 18.31 ? 1072 ALA   B N     1 
ATOM   16849 C  CA    . ALA   B  1  1074 ? 2.907   64.180  71.499  1.00 19.07 ? 1072 ALA   B CA    1 
ATOM   16850 C  C     . ALA   B  1  1074 ? 2.397   63.955  72.910  1.00 16.03 ? 1072 ALA   B C     1 
ATOM   16851 O  O     . ALA   B  1  1074 ? 2.399   62.821  73.402  1.00 17.40 ? 1072 ALA   B O     1 
ATOM   16852 C  CB    . ALA   B  1  1074 ? 4.332   64.727  71.550  1.00 20.08 ? 1072 ALA   B CB    1 
ATOM   16853 N  N     . GLY   B  1  1075 ? 1.988   65.030  73.582  1.00 16.78 ? 1073 GLY   B N     1 
ATOM   16854 C  CA    . GLY   B  1  1075 ? 1.446   64.887  74.923  1.00 19.09 ? 1073 GLY   B CA    1 
ATOM   16855 C  C     . GLY   B  1  1075 ? 0.290   63.907  74.972  1.00 20.02 ? 1073 GLY   B C     1 
ATOM   16856 O  O     . GLY   B  1  1075 ? 0.186   63.095  75.899  1.00 18.99 ? 1073 GLY   B O     1 
ATOM   16857 N  N     . SER   B  1  1076 ? -0.565  63.940  73.954  1.00 20.66 ? 1074 SER   B N     1 
ATOM   16858 C  CA    . SER   B  1  1076 ? -1.727  63.061  73.938  1.00 19.54 ? 1074 SER   B CA    1 
ATOM   16859 C  C     . SER   B  1  1076 ? -1.360  61.641  73.533  1.00 21.27 ? 1074 SER   B C     1 
ATOM   16860 O  O     . SER   B  1  1076 ? -1.836  60.680  74.144  1.00 21.59 ? 1074 SER   B O     1 
ATOM   16861 C  CB    . SER   B  1  1076 ? -2.784  63.611  72.982  1.00 22.80 ? 1074 SER   B CB    1 
ATOM   16862 O  OG    . SER   B  1  1076 ? -3.358  64.795  73.504  1.00 23.76 ? 1074 SER   B OG    1 
ATOM   16863 N  N     . SER   B  1  1077 ? -0.501  61.478  72.529  1.00 18.69 ? 1075 SER   B N     1 
ATOM   16864 C  CA    A SER   B  1  1077 ? -0.171  60.152  72.010  0.33 20.81 ? 1075 SER   B CA    1 
ATOM   16865 C  CA    B SER   B  1  1077 ? -0.235  60.127  72.057  0.67 20.76 ? 1075 SER   B CA    1 
ATOM   16866 C  C     . SER   B  1  1077 ? 0.751   59.378  72.941  1.00 19.77 ? 1075 SER   B C     1 
ATOM   16867 O  O     . SER   B  1  1077 ? 0.752   58.139  72.924  1.00 22.32 ? 1075 SER   B O     1 
ATOM   16868 C  CB    A SER   B  1  1077 ? 0.501   60.281  70.643  0.33 23.10 ? 1075 SER   B CB    1 
ATOM   16869 C  CB    B SER   B  1  1077 ? 0.238   60.138  70.606  0.67 23.50 ? 1075 SER   B CB    1 
ATOM   16870 O  OG    A SER   B  1  1077 ? -0.364  60.888  69.701  0.33 24.43 ? 1075 SER   B OG    1 
ATOM   16871 O  OG    B SER   B  1  1077 ? 1.520   60.707  70.513  0.67 23.36 ? 1075 SER   B OG    1 
ATOM   16872 N  N     . SER   B  1  1078 ? 1.559   60.089  73.722  1.00 17.51 ? 1076 SER   B N     1 
ATOM   16873 C  CA    . SER   B  1  1078 ? 2.448   59.448  74.677  1.00 18.26 ? 1076 SER   B CA    1 
ATOM   16874 C  C     . SER   B  1  1078 ? 1.664   58.492  75.556  1.00 17.03 ? 1076 SER   B C     1 
ATOM   16875 O  O     . SER   B  1  1078 ? 0.546   58.794  75.989  1.00 16.53 ? 1076 SER   B O     1 
ATOM   16876 C  CB    . SER   B  1  1078 ? 3.064   60.509  75.578  1.00 18.12 ? 1076 SER   B CB    1 
ATOM   16877 O  OG    . SER   B  1  1078 ? 3.759   59.876  76.638  1.00 16.23 ? 1076 SER   B OG    1 
ATOM   16878 N  N     . ALA   B  1  1079 ? 2.249   57.333  75.819  1.00 15.33 ? 1077 ALA   B N     1 
ATOM   16879 C  CA    . ALA   B  1  1079 ? 1.638   56.360  76.706  1.00 16.60 ? 1077 ALA   B CA    1 
ATOM   16880 C  C     . ALA   B  1  1079 ? 2.273   56.382  78.076  1.00 16.43 ? 1077 ALA   B C     1 
ATOM   16881 O  O     . ALA   B  1  1079 ? 2.033   55.476  78.880  1.00 15.36 ? 1077 ALA   B O     1 
ATOM   16882 C  CB    . ALA   B  1  1079 ? 1.698   54.962  76.095  1.00 18.26 ? 1077 ALA   B CB    1 
ATOM   16883 N  N     . LEU   B  1  1080 ? 3.076   57.404  78.361  1.00 15.22 ? 1078 LEU   B N     1 
ATOM   16884 C  CA    . LEU   B  1  1080 ? 3.624   57.580  79.699  1.00 13.41 ? 1078 LEU   B CA    1 
ATOM   16885 C  C     . LEU   B  1  1080 ? 2.498   57.537  80.716  1.00 15.36 ? 1078 LEU   B C     1 
ATOM   16886 O  O     . LEU   B  1  1080 ? 1.490   58.235  80.574  1.00 15.89 ? 1078 LEU   B O     1 
ATOM   16887 C  CB    . LEU   B  1  1080 ? 4.304   58.943  79.771  1.00 14.51 ? 1078 LEU   B CB    1 
ATOM   16888 C  CG    . LEU   B  1  1080 ? 4.735   59.351  81.171  1.00 15.52 ? 1078 LEU   B CG    1 
ATOM   16889 C  CD1   . LEU   B  1  1080 ? 5.910   58.489  81.647  1.00 16.15 ? 1078 LEU   B CD1   1 
ATOM   16890 C  CD2   . LEU   B  1  1080 ? 5.078   60.832  81.174  1.00 16.52 ? 1078 LEU   B CD2   1 
ATOM   16891 N  N     . GLY   B  1  1081 ? 2.666   56.697  81.733  1.00 14.55 ? 1079 GLY   B N     1 
ATOM   16892 C  CA    . GLY   B  1  1081 ? 1.663   56.565  82.764  1.00 16.97 ? 1079 GLY   B CA    1 
ATOM   16893 C  C     . GLY   B  1  1081 ? 0.728   55.396  82.567  1.00 16.84 ? 1079 GLY   B C     1 
ATOM   16894 O  O     . GLY   B  1  1081 ? -0.116  55.148  83.436  1.00 18.21 ? 1079 GLY   B O     1 
ATOM   16895 N  N     . LEU   B  1  1082 ? 0.826   54.694  81.444  1.00 16.53 ? 1080 LEU   B N     1 
ATOM   16896 C  CA    A LEU   B  1  1082 ? 0.080   53.458  81.279  0.47 17.57 ? 1080 LEU   B CA    1 
ATOM   16897 C  CA    B LEU   B  1  1082 ? 0.077   53.458  81.281  0.53 17.57 ? 1080 LEU   B CA    1 
ATOM   16898 C  C     . LEU   B  1  1082 ? 0.351   52.553  82.467  1.00 16.91 ? 1080 LEU   B C     1 
ATOM   16899 O  O     . LEU   B  1  1082 ? 1.489   52.418  82.911  1.00 17.14 ? 1080 LEU   B O     1 
ATOM   16900 C  CB    A LEU   B  1  1082 ? 0.533   52.771  79.993  0.47 16.45 ? 1080 LEU   B CB    1 
ATOM   16901 C  CB    B LEU   B  1  1082 ? 0.517   52.769  79.991  0.53 16.44 ? 1080 LEU   B CB    1 
ATOM   16902 C  CG    A LEU   B  1  1082 ? -0.092  51.417  79.656  0.47 16.97 ? 1080 LEU   B CG    1 
ATOM   16903 C  CG    B LEU   B  1  1082 ? -0.065  51.398  79.626  0.53 16.97 ? 1080 LEU   B CG    1 
ATOM   16904 C  CD1   A LEU   B  1  1082 ? -1.585  51.532  79.667  0.47 22.14 ? 1080 LEU   B CD1   1 
ATOM   16905 C  CD1   B LEU   B  1  1082 ? 0.006   51.219  78.132  0.53 16.87 ? 1080 LEU   B CD1   1 
ATOM   16906 C  CD2   A LEU   B  1  1082 ? 0.381   50.932  78.299  0.47 16.57 ? 1080 LEU   B CD2   1 
ATOM   16907 C  CD2   B LEU   B  1  1082 ? 0.694   50.265  80.308  0.53 17.49 ? 1080 LEU   B CD2   1 
ATOM   16908 N  N     . ASP   B  1  1083 ? -0.699  51.934  82.987  1.00 17.96 ? 1081 ASP   B N     1 
ATOM   16909 C  CA    . ASP   B  1  1083 ? -0.570  51.150  84.209  1.00 20.87 ? 1081 ASP   B CA    1 
ATOM   16910 C  C     . ASP   B  1  1083 ? -1.628  50.057  84.131  1.00 19.24 ? 1081 ASP   B C     1 
ATOM   16911 O  O     . ASP   B  1  1083 ? -2.794  50.293  84.465  1.00 23.35 ? 1081 ASP   B O     1 
ATOM   16912 C  CB    . ASP   B  1  1083 ? -0.770  52.061  85.411  1.00 21.49 ? 1081 ASP   B CB    1 
ATOM   16913 C  CG    . ASP   B  1  1083 ? -0.607  51.344  86.734  1.00 32.18 ? 1081 ASP   B CG    1 
ATOM   16914 O  OD1   . ASP   B  1  1083 ? -0.136  50.193  86.748  1.00 37.31 ? 1081 ASP   B OD1   1 
ATOM   16915 O  OD2   . ASP   B  1  1083 ? -0.953  51.948  87.771  1.00 37.93 ? 1081 ASP   B OD2   1 
ATOM   16916 N  N     . LEU   B  1  1084 ? -1.219  48.878  83.678  1.00 19.79 ? 1082 LEU   B N     1 
ATOM   16917 C  CA    . LEU   B  1  1084 ? -2.123  47.798  83.325  1.00 20.95 ? 1082 LEU   B CA    1 
ATOM   16918 C  C     . LEU   B  1  1084 ? -1.851  46.585  84.196  1.00 19.19 ? 1082 LEU   B C     1 
ATOM   16919 O  O     . LEU   B  1  1084 ? -0.708  46.320  84.582  1.00 19.35 ? 1082 LEU   B O     1 
ATOM   16920 C  CB    . LEU   B  1  1084 ? -1.895  47.354  81.884  1.00 24.01 ? 1082 LEU   B CB    1 
ATOM   16921 C  CG    . LEU   B  1  1084 ? -2.303  48.338  80.797  1.00 28.31 ? 1082 LEU   B CG    1 
ATOM   16922 C  CD1   . LEU   B  1  1084 ? -1.916  47.781  79.454  1.00 27.44 ? 1082 LEU   B CD1   1 
ATOM   16923 C  CD2   . LEU   B  1  1084 ? -3.795  48.653  80.868  1.00 29.79 ? 1082 LEU   B CD2   1 
ATOM   16924 N  N     . GLU   B  1  1085 ? -2.902  45.829  84.475  1.00 19.73 ? 1083 GLU   B N     1 
ATOM   16925 C  CA    . GLU   B  1  1085 ? -2.751  44.477  84.974  1.00 18.58 ? 1083 GLU   B CA    1 
ATOM   16926 C  C     . GLU   B  1  1085 ? -2.942  43.507  83.819  1.00 19.64 ? 1083 GLU   B C     1 
ATOM   16927 O  O     . GLU   B  1  1085 ? -3.948  43.570  83.106  1.00 21.04 ? 1083 GLU   B O     1 
ATOM   16928 C  CB    . GLU   B  1  1085 ? -3.734  44.164  86.102  1.00 19.21 ? 1083 GLU   B CB    1 
ATOM   16929 C  CG    . GLU   B  1  1085 ? -3.539  42.729  86.557  1.00 22.60 ? 1083 GLU   B CG    1 
ATOM   16930 C  CD    . GLU   B  1  1085 ? -4.284  42.369  87.814  1.00 27.19 ? 1083 GLU   B CD    1 
ATOM   16931 O  OE1   . GLU   B  1  1085 ? -4.893  43.266  88.441  1.00 28.69 ? 1083 GLU   B OE1   1 
ATOM   16932 O  OE2   . GLU   B  1  1085 ? -4.256  41.171  88.166  1.00 27.32 ? 1083 GLU   B OE2   1 
ATOM   16933 N  N     . LEU   B  1  1086 ? -1.984  42.636  83.632  1.00 17.54 ? 1084 LEU   B N     1 
ATOM   16934 C  CA    . LEU   B  1  1086 ? -1.980  41.683  82.531  1.00 17.72 ? 1084 LEU   B CA    1 
ATOM   16935 C  C     . LEU   B  1  1086 ? -2.628  40.376  82.976  1.00 20.92 ? 1084 LEU   B C     1 
ATOM   16936 O  O     . LEU   B  1  1086 ? -2.466  39.966  84.125  1.00 21.80 ? 1084 LEU   B O     1 
ATOM   16937 C  CB    . LEU   B  1  1086 ? -0.555  41.404  82.083  1.00 20.34 ? 1084 LEU   B CB    1 
ATOM   16938 C  CG    . LEU   B  1  1086 ? 0.184   42.645  81.595  1.00 20.74 ? 1084 LEU   B CG    1 
ATOM   16939 C  CD1   . LEU   B  1  1086 ? 1.569   42.262  81.138  1.00 20.39 ? 1084 LEU   B CD1   1 
ATOM   16940 C  CD2   . LEU   B  1  1086 ? -0.579  43.311  80.467  1.00 23.85 ? 1084 LEU   B CD2   1 
ATOM   16941 N  N     . PRO   B  1  1087 ? -3.385  39.739  82.088  1.00 18.27 ? 1085 PRO   B N     1 
ATOM   16942 C  CA    . PRO   B  1  1087 ? -3.984  38.438  82.416  1.00 21.51 ? 1085 PRO   B CA    1 
ATOM   16943 C  C     . PRO   B  1  1087 ? -2.917  37.407  82.738  1.00 19.55 ? 1085 PRO   B C     1 
ATOM   16944 O  O     . PRO   B  1  1087 ? -1.881  37.325  82.078  1.00 20.85 ? 1085 PRO   B O     1 
ATOM   16945 C  CB    . PRO   B  1  1087 ? -4.726  38.061  81.128  1.00 22.05 ? 1085 PRO   B CB    1 
ATOM   16946 C  CG    . PRO   B  1  1087 ? -5.002  39.349  80.455  1.00 25.79 ? 1085 PRO   B CG    1 
ATOM   16947 C  CD    . PRO   B  1  1087 ? -3.860  40.263  80.794  1.00 21.79 ? 1085 PRO   B CD    1 
ATOM   16948 N  N     . GLY   B  1  1088 ? -3.184  36.601  83.747  1.00 19.55 ? 1086 GLY   B N     1 
ATOM   16949 C  CA    . GLY   B  1  1088 ? -2.245  35.595  84.158  1.00 21.25 ? 1086 GLY   B CA    1 
ATOM   16950 C  C     . GLY   B  1  1088 ? -2.887  34.653  85.143  1.00 18.44 ? 1086 GLY   B C     1 
ATOM   16951 O  O     . GLY   B  1  1088 ? -4.111  34.581  85.266  1.00 19.77 ? 1086 GLY   B O     1 
ATOM   16952 N  N     . PRO   B  1  1089 ? -2.062  33.915  85.871  1.00 17.58 ? 1087 PRO   B N     1 
ATOM   16953 C  CA    . PRO   B  1  1089 ? -2.589  32.946  86.829  1.00 17.96 ? 1087 PRO   B CA    1 
ATOM   16954 C  C     . PRO   B  1  1089 ? -3.215  33.636  88.028  1.00 18.84 ? 1087 PRO   B C     1 
ATOM   16955 O  O     . PRO   B  1  1089 ? -2.920  34.789  88.355  1.00 18.77 ? 1087 PRO   B O     1 
ATOM   16956 C  CB    . PRO   B  1  1089 ? -1.343  32.164  87.253  1.00 22.02 ? 1087 PRO   B CB    1 
ATOM   16957 C  CG    . PRO   B  1  1089 ? -0.226  33.159  87.085  1.00 22.83 ? 1087 PRO   B CG    1 
ATOM   16958 C  CD    . PRO   B  1  1089 ? -0.589  33.931  85.846  1.00 19.18 ? 1087 PRO   B CD    1 
ATOM   16959 N  N     . VAL   B  1  1090 ? -4.110  32.898  88.686  1.00 17.77 ? 1088 VAL   B N     1 
ATOM   16960 C  CA    . VAL   B  1  1090 ? -4.622  33.359  89.957  1.00 17.21 ? 1088 VAL   B CA    1 
ATOM   16961 C  C     . VAL   B  1  1090 ? -3.486  33.406  90.970  1.00 17.64 ? 1088 VAL   B C     1 
ATOM   16962 O  O     . VAL   B  1  1090 ? -2.428  32.790  90.796  1.00 18.16 ? 1088 VAL   B O     1 
ATOM   16963 C  CB    . VAL   B  1  1090 ? -5.758  32.462  90.464  1.00 19.28 ? 1088 VAL   B CB    1 
ATOM   16964 C  CG1   . VAL   B  1  1090 ? -6.908  32.450  89.476  1.00 20.51 ? 1088 VAL   B CG1   1 
ATOM   16965 C  CG2   . VAL   B  1  1090 ? -5.259  31.048  90.728  1.00 21.60 ? 1088 VAL   B CG2   1 
ATOM   16966 N  N     . GLY   B  1  1091 ? -3.715  34.153  92.043  1.00 19.10 ? 1089 GLY   B N     1 
ATOM   16967 C  CA    . GLY   B  1  1091 ? -2.715  34.242  93.087  1.00 18.05 ? 1089 GLY   B CA    1 
ATOM   16968 C  C     . GLY   B  1  1091 ? -1.508  35.061  92.719  1.00 17.88 ? 1089 GLY   B C     1 
ATOM   16969 O  O     . GLY   B  1  1091 ? -0.481  34.978  93.396  1.00 16.86 ? 1089 GLY   B O     1 
ATOM   16970 N  N     . GLU   B  1  1092 ? -1.601  35.848  91.655  1.00 18.27 ? 1090 GLU   B N     1 
ATOM   16971 C  CA    . GLU   B  1  1092 ? -0.513  36.692  91.215  1.00 17.68 ? 1090 GLU   B CA    1 
ATOM   16972 C  C     . GLU   B  1  1092 ? -1.137  37.917  90.583  1.00 18.49 ? 1090 GLU   B C     1 
ATOM   16973 O  O     . GLU   B  1  1092 ? -2.201  37.823  89.964  1.00 19.14 ? 1090 GLU   B O     1 
ATOM   16974 C  CB    . GLU   B  1  1092 ? 0.310   35.963  90.149  1.00 19.28 ? 1090 GLU   B CB    1 
ATOM   16975 C  CG    . GLU   B  1  1092 ? 1.795   36.008  90.362  1.00 27.67 ? 1090 GLU   B CG    1 
ATOM   16976 C  CD    . GLU   B  1  1092 ? 2.544   35.132  89.372  1.00 26.06 ? 1090 GLU   B CD    1 
ATOM   16977 O  OE1   . GLU   B  1  1092 ? 2.379   35.339  88.153  1.00 20.97 ? 1090 GLU   B OE1   1 
ATOM   16978 O  OE2   . GLU   B  1  1092 ? 3.285   34.229  89.816  1.00 25.49 ? 1090 GLU   B OE2   1 
ATOM   16979 N  N     . ARG   B  1  1093 ? -0.504  39.063  90.766  1.00 17.23 ? 1091 ARG   B N     1 
ATOM   16980 C  CA    . ARG   B  1  1093 ? -0.874  40.282  90.062  1.00 18.03 ? 1091 ARG   B CA    1 
ATOM   16981 C  C     . ARG   B  1  1093 ? 0.323   40.656  89.216  1.00 16.54 ? 1091 ARG   B C     1 
ATOM   16982 O  O     . ARG   B  1  1093 ? 1.421   40.855  89.743  1.00 16.89 ? 1091 ARG   B O     1 
ATOM   16983 C  CB    . ARG   B  1  1093 ? -1.215  41.417  91.033  1.00 19.31 ? 1091 ARG   B CB    1 
ATOM   16984 N  N     . ASN   B  1  1094 ? 0.124   40.716  87.915  1.00 14.86 ? 1092 ASN   B N     1 
ATOM   16985 C  CA    . ASN   B  1  1094 ? 1.198   40.971  86.974  1.00 14.51 ? 1092 ASN   B CA    1 
ATOM   16986 C  C     . ASN   B  1  1094 ? 0.907   42.305  86.317  1.00 17.64 ? 1092 ASN   B C     1 
ATOM   16987 O  O     . ASN   B  1  1094 ? -0.085  42.453  85.590  1.00 17.31 ? 1092 ASN   B O     1 
ATOM   16988 C  CB    . ASN   B  1  1094 ? 1.304   39.821  85.989  1.00 15.57 ? 1092 ASN   B CB    1 
ATOM   16989 C  CG    . ASN   B  1  1094 ? 1.896   38.610  86.635  1.00 15.47 ? 1092 ASN   B CG    1 
ATOM   16990 O  OD1   . ASN   B  1  1094 ? 3.078   38.611  86.931  1.00 16.15 ? 1092 ASN   B OD1   1 
ATOM   16991 N  ND2   . ASN   B  1  1094 ? 1.086   37.594  86.899  1.00 16.95 ? 1092 ASN   B ND2   1 
ATOM   16992 N  N     . LEU   B  1  1095 ? 1.728   43.286  86.641  1.00 15.80 ? 1093 LEU   B N     1 
ATOM   16993 C  CA    . LEU   B  1  1095 ? 1.502   44.667  86.278  1.00 15.65 ? 1093 LEU   B CA    1 
ATOM   16994 C  C     . LEU   B  1  1095 ? 2.515   45.099  85.238  1.00 14.06 ? 1093 LEU   B C     1 
ATOM   16995 O  O     . LEU   B  1  1095 ? 3.658   44.635  85.215  1.00 15.57 ? 1093 LEU   B O     1 
ATOM   16996 C  CB    . LEU   B  1  1095 ? 1.626   45.576  87.487  1.00 16.98 ? 1093 LEU   B CB    1 
ATOM   16997 C  CG    . LEU   B  1  1095 ? 0.790   45.105  88.677  1.00 20.84 ? 1093 LEU   B CG    1 
ATOM   16998 C  CD1   . LEU   B  1  1095 ? 0.994   46.021  89.874  1.00 25.27 ? 1093 LEU   B CD1   1 
ATOM   16999 C  CD2   . LEU   B  1  1095 ? -0.679  45.013  88.288  1.00 21.22 ? 1093 LEU   B CD2   1 
ATOM   17000 N  N     . TYR   B  1  1096 ? 2.087   46.027  84.396  1.00 14.44 ? 1094 TYR   B N     1 
ATOM   17001 C  CA    . TYR   B  1  1096 ? 2.905   46.517  83.303  1.00 14.05 ? 1094 TYR   B CA    1 
ATOM   17002 C  C     . TYR   B  1  1096 ? 2.683   48.011  83.239  1.00 15.07 ? 1094 TYR   B C     1 
ATOM   17003 O  O     . TYR   B  1  1096 ? 1.541   48.463  83.148  1.00 15.00 ? 1094 TYR   B O     1 
ATOM   17004 C  CB    . TYR   B  1  1096 ? 2.487   45.835  82.005  1.00 15.10 ? 1094 TYR   B CB    1 
ATOM   17005 C  CG    . TYR   B  1  1096 ? 3.143   46.361  80.752  1.00 14.52 ? 1094 TYR   B CG    1 
ATOM   17006 C  CD1   . TYR   B  1  1096 ? 4.402   45.929  80.353  1.00 16.07 ? 1094 TYR   B CD1   1 
ATOM   17007 C  CD2   . TYR   B  1  1096 ? 2.483   47.268  79.958  1.00 18.20 ? 1094 TYR   B CD2   1 
ATOM   17008 C  CE1   . TYR   B  1  1096 ? 4.983   46.405  79.183  1.00 15.81 ? 1094 TYR   B CE1   1 
ATOM   17009 C  CE2   . TYR   B  1  1096 ? 3.047   47.742  78.786  1.00 15.93 ? 1094 TYR   B CE2   1 
ATOM   17010 C  CZ    . TYR   B  1  1096 ? 4.289   47.306  78.410  1.00 15.37 ? 1094 TYR   B CZ    1 
ATOM   17011 O  OH    . TYR   B  1  1096 ? 4.855   47.794  77.255  1.00 16.06 ? 1094 TYR   B OH    1 
ATOM   17012 N  N     . THR   B  1  1097 ? 3.765   48.771  83.332  1.00 15.54 ? 1095 THR   B N     1 
ATOM   17013 C  CA    . THR   B  1  1097 ? 3.662   50.209  83.467  1.00 14.99 ? 1095 THR   B CA    1 
ATOM   17014 C  C     . THR   B  1  1097 ? 4.693   50.866  82.569  1.00 14.18 ? 1095 THR   B C     1 
ATOM   17015 O  O     . THR   B  1  1097 ? 5.785   50.332  82.353  1.00 15.69 ? 1095 THR   B O     1 
ATOM   17016 C  CB    . THR   B  1  1097 ? 3.904   50.631  84.914  1.00 17.54 ? 1095 THR   B CB    1 
ATOM   17017 O  OG1   . THR   B  1  1097 ? 5.192   50.181  85.341  1.00 21.81 ? 1095 THR   B OG1   1 
ATOM   17018 C  CG2   . THR   B  1  1097 ? 2.884   50.016  85.818  1.00 18.86 ? 1095 THR   B CG2   1 
ATOM   17019 N  N     . LEU   B  1  1098 ? 4.358   52.056  82.084  1.00 15.51 ? 1096 LEU   B N     1 
ATOM   17020 C  CA    . LEU   B  1  1098 ? 5.262   52.820  81.236  1.00 14.76 ? 1096 LEU   B CA    1 
ATOM   17021 C  C     . LEU   B  1  1098 ? 5.688   54.074  81.974  1.00 14.48 ? 1096 LEU   B C     1 
ATOM   17022 O  O     . LEU   B  1  1098 ? 4.854   54.890  82.373  1.00 15.82 ? 1096 LEU   B O     1 
ATOM   17023 C  CB    . LEU   B  1  1098 ? 4.632   53.177  79.898  1.00 14.72 ? 1096 LEU   B CB    1 
ATOM   17024 C  CG    . LEU   B  1  1098 ? 4.295   51.972  79.034  1.00 14.37 ? 1096 LEU   B CG    1 
ATOM   17025 C  CD1   . LEU   B  1  1098 ? 3.688   52.486  77.747  1.00 15.53 ? 1096 LEU   B CD1   1 
ATOM   17026 C  CD2   . LEU   B  1  1098 ? 5.497   51.108  78.741  1.00 15.88 ? 1096 LEU   B CD2   1 
ATOM   17027 N  N     . HIS   B  1  1099 ? 6.992   54.205  82.147  1.00 15.03 ? 1097 HIS   B N     1 
ATOM   17028 C  CA    . HIS   B  1  1099 ? 7.623   55.295  82.861  1.00 16.01 ? 1097 HIS   B CA    1 
ATOM   17029 C  C     . HIS   B  1  1099 ? 8.484   56.062  81.875  1.00 15.38 ? 1097 HIS   B C     1 
ATOM   17030 O  O     . HIS   B  1  1099 ? 8.729   55.612  80.753  1.00 15.59 ? 1097 HIS   B O     1 
ATOM   17031 C  CB    . HIS   B  1  1099 ? 8.525   54.727  83.949  1.00 16.44 ? 1097 HIS   B CB    1 
ATOM   17032 C  CG    . HIS   B  1  1099 ? 7.787   53.909  84.953  1.00 18.04 ? 1097 HIS   B CG    1 
ATOM   17033 N  ND1   . HIS   B  1  1099 ? 7.430   54.400  86.190  1.00 21.66 ? 1097 HIS   B ND1   1 
ATOM   17034 C  CD2   . HIS   B  1  1099 ? 7.336   52.633  84.906  1.00 20.46 ? 1097 HIS   B CD2   1 
ATOM   17035 C  CE1   . HIS   B  1  1099 ? 6.799   53.455  86.867  1.00 23.09 ? 1097 HIS   B CE1   1 
ATOM   17036 N  NE2   . HIS   B  1  1099 ? 6.728   52.375  86.110  1.00 21.45 ? 1097 HIS   B NE2   1 
ATOM   17037 N  N     . ALA   B  1  1100 ? 8.948   57.229  82.309  1.00 16.63 ? 1098 ALA   B N     1 
ATOM   17038 C  CA    . ALA   B  1  1100 ? 9.952   57.928  81.520  1.00 16.75 ? 1098 ALA   B CA    1 
ATOM   17039 C  C     . ALA   B  1  1100 ? 11.198  57.063  81.396  1.00 16.32 ? 1098 ALA   B C     1 
ATOM   17040 O  O     . ALA   B  1  1100 ? 11.517  56.263  82.282  1.00 17.38 ? 1098 ALA   B O     1 
ATOM   17041 C  CB    . ALA   B  1  1100 ? 10.331  59.245  82.194  1.00 17.59 ? 1098 ALA   B CB    1 
ATOM   17042 N  N     . ARG   B  1  1101 ? 11.897  57.218  80.271  1.00 16.45 ? 1099 ARG   B N     1 
ATOM   17043 C  CA    . ARG   B  1  1101 ? 13.192  56.568  80.102  1.00 16.24 ? 1099 ARG   B CA    1 
ATOM   17044 C  C     . ARG   B  1  1101 ? 14.238  57.149  81.038  1.00 15.58 ? 1099 ARG   B C     1 
ATOM   17045 O  O     . ARG   B  1  1101 ? 15.058  56.411  81.589  1.00 18.08 ? 1099 ARG   B O     1 
ATOM   17046 C  CB    . ARG   B  1  1101 ? 13.651  56.691  78.649  1.00 17.92 ? 1099 ARG   B CB    1 
ATOM   17047 C  CG    . ARG   B  1  1101 ? 13.072  55.649  77.724  1.00 21.20 ? 1099 ARG   B CG    1 
ATOM   17048 C  CD    . ARG   B  1  1101 ? 13.904  54.384  77.739  1.00 20.42 ? 1099 ARG   B CD    1 
ATOM   17049 N  NE    . ARG   B  1  1101 ? 13.345  53.378  76.844  1.00 20.93 ? 1099 ARG   B NE    1 
ATOM   17050 C  CZ    . ARG   B  1  1101 ? 14.064  52.478  76.191  1.00 19.16 ? 1099 ARG   B CZ    1 
ATOM   17051 N  NH1   . ARG   B  1  1101 ? 15.377  52.392  76.345  1.00 18.14 ? 1099 ARG   B NH1   1 
ATOM   17052 N  NH2   . ARG   B  1  1101 ? 13.462  51.663  75.335  1.00 20.76 ? 1099 ARG   B NH2   1 
ATOM   17053 N  N     . GLY   B  1  1102 ? 14.205  58.455  81.255  1.00 15.08 ? 1100 GLY   B N     1 
ATOM   17054 C  CA    . GLY   B  1  1102 ? 15.222  59.106  82.048  1.00 17.67 ? 1100 GLY   B CA    1 
ATOM   17055 C  C     . GLY   B  1  1102 ? 15.658  60.390  81.377  1.00 18.17 ? 1100 GLY   B C     1 
ATOM   17056 O  O     . GLY   B  1  1102 ? 14.839  61.264  81.092  1.00 18.69 ? 1100 GLY   B O     1 
ATOM   17057 N  N     . ARG   B  1  1103 ? 16.950  60.516  81.106  1.00 16.58 ? 1101 ARG   B N     1 
ATOM   17058 C  CA    . ARG   B  1  1103 ? 17.468  61.676  80.403  1.00 17.83 ? 1101 ARG   B CA    1 
ATOM   17059 C  C     . ARG   B  1  1103 ? 17.820  61.274  78.979  1.00 18.37 ? 1101 ARG   B C     1 
ATOM   17060 O  O     . ARG   B  1  1103 ? 18.556  60.304  78.761  1.00 18.34 ? 1101 ARG   B O     1 
ATOM   17061 C  CB    . ARG   B  1  1103 ? 18.697  62.255  81.106  1.00 18.75 ? 1101 ARG   B CB    1 
ATOM   17062 C  CG    . ARG   B  1  1103 ? 19.158  63.564  80.461  1.00 21.05 ? 1101 ARG   B CG    1 
ATOM   17063 C  CD    . ARG   B  1  1103 ? 20.179  64.310  81.305  1.00 26.02 ? 1101 ARG   B CD    1 
ATOM   17064 N  NE    . ARG   B  1  1103 ? 19.549  65.087  82.364  1.00 31.08 ? 1101 ARG   B NE    1 
ATOM   17065 C  CZ    . ARG   B  1  1103 ? 19.626  64.798  83.652  1.00 34.99 ? 1101 ARG   B CZ    1 
ATOM   17066 N  NH1   . ARG   B  1  1103 ? 20.305  63.746  84.084  1.00 43.87 ? 1101 ARG   B NH1   1 
ATOM   17067 N  NH2   . ARG   B  1  1103 ? 19.018  65.592  84.532  1.00 32.30 ? 1101 ARG   B NH2   1 
ATOM   17068 N  N     . ILE   B  1  1104 ? 17.282  62.011  78.020  1.00 15.56 ? 1102 ILE   B N     1 
ATOM   17069 C  CA    . ILE   B  1  1104 ? 17.465  61.716  76.608  1.00 16.31 ? 1102 ILE   B CA    1 
ATOM   17070 C  C     . ILE   B  1  1104 ? 18.485  62.696  76.047  1.00 15.59 ? 1102 ILE   B C     1 
ATOM   17071 O  O     . ILE   B  1  1104 ? 18.384  63.911  76.265  1.00 16.43 ? 1102 ILE   B O     1 
ATOM   17072 C  CB    . ILE   B  1  1104 ? 16.130  61.822  75.855  1.00 15.32 ? 1102 ILE   B CB    1 
ATOM   17073 C  CG1   . ILE   B  1  1104 ? 15.041  60.963  76.528  1.00 16.15 ? 1102 ILE   B CG1   1 
ATOM   17074 C  CG2   . ILE   B  1  1104 ? 16.303  61.466  74.382  1.00 16.79 ? 1102 ILE   B CG2   1 
ATOM   17075 C  CD1   . ILE   B  1  1104 ? 15.347  59.503  76.574  1.00 16.80 ? 1102 ILE   B CD1   1 
ATOM   17076 N  N     . LEU   B  1  1105 ? 19.457  62.171  75.316  1.00 15.21 ? 1103 LEU   B N     1 
ATOM   17077 C  CA    . LEU   B  1  1105 ? 20.408  63.017  74.609  1.00 17.60 ? 1103 LEU   B CA    1 
ATOM   17078 C  C     . LEU   B  1  1105 ? 19.739  63.558  73.351  1.00 15.51 ? 1103 LEU   B C     1 
ATOM   17079 O  O     . LEU   B  1  1105 ? 19.242  62.788  72.524  1.00 16.80 ? 1103 LEU   B O     1 
ATOM   17080 C  CB    . LEU   B  1  1105 ? 21.636  62.189  74.250  1.00 16.38 ? 1103 LEU   B CB    1 
ATOM   17081 C  CG    . LEU   B  1  1105 ? 22.679  62.874  73.377  1.00 19.14 ? 1103 LEU   B CG    1 
ATOM   17082 C  CD1   . LEU   B  1  1105 ? 23.257  64.065  74.108  1.00 18.03 ? 1103 LEU   B CD1   1 
ATOM   17083 C  CD2   . LEU   B  1  1105 ? 23.747  61.871  73.010  1.00 19.51 ? 1103 LEU   B CD2   1 
ATOM   17084 N  N     . LEU   B  1  1106 ? 19.691  64.873  73.219  1.00 16.41 ? 1104 LEU   B N     1 
ATOM   17085 C  CA    . LEU   B  1  1106 ? 19.107  65.510  72.053  1.00 17.70 ? 1104 LEU   B CA    1 
ATOM   17086 C  C     . LEU   B  1  1106 ? 20.239  66.060  71.208  1.00 18.34 ? 1104 LEU   B C     1 
ATOM   17087 O  O     . LEU   B  1  1106 ? 21.079  66.814  71.709  1.00 18.74 ? 1104 LEU   B O     1 
ATOM   17088 C  CB    . LEU   B  1  1106 ? 18.175  66.649  72.469  1.00 18.21 ? 1104 LEU   B CB    1 
ATOM   17089 C  CG    . LEU   B  1  1106 ? 16.697  66.300  72.627  1.00 22.46 ? 1104 LEU   B CG    1 
ATOM   17090 C  CD1   . LEU   B  1  1106 ? 16.483  64.973  73.327  1.00 24.02 ? 1104 LEU   B CD1   1 
ATOM   17091 C  CD2   . LEU   B  1  1106 ? 15.946  67.433  73.309  1.00 17.97 ? 1104 LEU   B CD2   1 
ATOM   17092 N  N     . VAL   B  1  1107 ? 20.266  65.665  69.945  1.00 16.12 ? 1105 VAL   B N     1 
ATOM   17093 C  CA    . VAL   B  1  1107 ? 21.281  66.168  69.032  1.00 19.19 ? 1105 VAL   B CA    1 
ATOM   17094 C  C     . VAL   B  1  1107 ? 20.522  66.848  67.904  1.00 17.18 ? 1105 VAL   B C     1 
ATOM   17095 O  O     . VAL   B  1  1107 ? 20.313  66.250  66.841  1.00 18.50 ? 1105 VAL   B O     1 
ATOM   17096 C  CB    . VAL   B  1  1107 ? 22.187  65.035  68.535  1.00 16.85 ? 1105 VAL   B CB    1 
ATOM   17097 C  CG1   . VAL   B  1  1107 ? 23.381  65.609  67.792  1.00 17.86 ? 1105 VAL   B CG1   1 
ATOM   17098 C  CG2   . VAL   B  1  1107 ? 22.650  64.170  69.703  1.00 18.86 ? 1105 VAL   B CG2   1 
ATOM   17099 N  N     . PRO   B  1  1108 ? 20.076  68.080  68.096  1.00 17.26 ? 1106 PRO   B N     1 
ATOM   17100 C  CA    . PRO   B  1  1108 ? 19.335  68.773  67.047  1.00 19.72 ? 1106 PRO   B CA    1 
ATOM   17101 C  C     . PRO   B  1  1108 ? 20.282  69.396  66.040  1.00 20.24 ? 1106 PRO   B C     1 
ATOM   17102 O  O     . PRO   B  1  1108 ? 21.478  69.573  66.283  1.00 22.31 ? 1106 PRO   B O     1 
ATOM   17103 C  CB    . PRO   B  1  1108 ? 18.613  69.877  67.827  1.00 20.30 ? 1106 PRO   B CB    1 
ATOM   17104 C  CG    . PRO   B  1  1108 ? 19.563  70.195  68.919  1.00 20.01 ? 1106 PRO   B CG    1 
ATOM   17105 C  CD    . PRO   B  1  1108 ? 20.147  68.873  69.335  1.00 20.11 ? 1106 PRO   B CD    1 
ATOM   17106 N  N     . ALA   B  1  1109 ? 19.707  69.746  64.902  1.00 19.48 ? 1107 ALA   B N     1 
ATOM   17107 C  CA    . ALA   B  1  1109 ? 20.368  70.578  63.907  1.00 20.70 ? 1107 ALA   B CA    1 
ATOM   17108 C  C     . ALA   B  1  1109 ? 19.735  71.949  63.785  1.00 23.64 ? 1107 ALA   B C     1 
ATOM   17109 O  O     . ALA   B  1  1109 ? 20.440  72.944  63.607  1.00 24.82 ? 1107 ALA   B O     1 
ATOM   17110 C  CB    . ALA   B  1  1109 ? 20.332  69.890  62.539  1.00 21.79 ? 1107 ALA   B CB    1 
ATOM   17111 N  N     . THR   B  1  1110 ? 18.413  72.023  63.891  1.00 21.73 ? 1108 THR   B N     1 
ATOM   17112 C  CA    . THR   B  1  1110 ? 17.681  73.257  63.680  1.00 20.86 ? 1108 THR   B CA    1 
ATOM   17113 C  C     . THR   B  1  1110 ? 16.817  73.548  64.895  1.00 20.24 ? 1108 THR   B C     1 
ATOM   17114 O  O     . THR   B  1  1110 ? 16.523  72.665  65.709  1.00 20.67 ? 1108 THR   B O     1 
ATOM   17115 C  CB    . THR   B  1  1110 ? 16.767  73.170  62.450  1.00 23.50 ? 1108 THR   B CB    1 
ATOM   17116 O  OG1   . THR   B  1  1110 ? 15.753  72.176  62.662  1.00 22.43 ? 1108 THR   B OG1   1 
ATOM   17117 C  CG2   . THR   B  1  1110 ? 17.562  72.822  61.196  1.00 25.97 ? 1108 THR   B CG2   1 
ATOM   17118 N  N     . GLU   B  1  1111 ? 16.403  74.810  64.995  1.00 21.37 ? 1109 GLU   B N     1 
ATOM   17119 C  CA    . GLU   B  1  1111 ? 15.536  75.212  66.094  1.00 22.27 ? 1109 GLU   B CA    1 
ATOM   17120 C  C     . GLU   B  1  1111 ? 14.240  74.412  66.095  1.00 22.65 ? 1109 GLU   B C     1 
ATOM   17121 O  O     . GLU   B  1  1111 ? 13.820  73.895  67.138  1.00 22.32 ? 1109 GLU   B O     1 
ATOM   17122 C  CB    . GLU   B  1  1111 ? 15.251  76.702  65.998  1.00 22.20 ? 1109 GLU   B CB    1 
ATOM   17123 C  CG    . GLU   B  1  1111 ? 14.203  77.161  66.980  1.00 25.54 ? 1109 GLU   B CG    1 
ATOM   17124 C  CD    . GLU   B  1  1111 ? 14.014  78.654  66.937  1.00 29.50 ? 1109 GLU   B CD    1 
ATOM   17125 O  OE1   . GLU   B  1  1111 ? 14.852  79.367  67.517  1.00 27.91 ? 1109 GLU   B OE1   1 
ATOM   17126 O  OE2   . GLU   B  1  1111 ? 13.043  79.108  66.302  1.00 31.86 ? 1109 GLU   B OE2   1 
ATOM   17127 N  N     . SER   B  1  1112 ? 13.590  74.301  64.938  1.00 22.50 ? 1110 SER   B N     1 
ATOM   17128 C  CA    . SER   B  1  1112 ? 12.350  73.539  64.879  1.00 22.20 ? 1110 SER   B CA    1 
ATOM   17129 C  C     . SER   B  1  1112 ? 12.599  72.084  65.231  1.00 21.88 ? 1110 SER   B C     1 
ATOM   17130 O  O     . SER   B  1  1112 ? 11.804  71.466  65.952  1.00 21.79 ? 1110 SER   B O     1 
ATOM   17131 C  CB    . SER   B  1  1112 ? 11.730  73.638  63.489  1.00 25.41 ? 1110 SER   B CB    1 
ATOM   17132 O  OG    . SER   B  1  1112 ? 10.531  72.877  63.426  1.00 26.54 ? 1110 SER   B OG    1 
ATOM   17133 N  N     . GLY   B  1  1113 ? 13.699  71.518  64.732  1.00 20.72 ? 1111 GLY   B N     1 
ATOM   17134 C  CA    . GLY   B  1  1113 ? 14.028  70.150  65.087  1.00 18.60 ? 1111 GLY   B CA    1 
ATOM   17135 C  C     . GLY   B  1  1113 ? 14.182  69.994  66.583  1.00 19.78 ? 1111 GLY   B C     1 
ATOM   17136 O  O     . GLY   B  1  1113 ? 13.675  69.036  67.173  1.00 19.33 ? 1111 GLY   B O     1 
ATOM   17137 N  N     . LEU   B  1  1114 ? 14.869  70.944  67.219  1.00 20.22 ? 1112 LEU   B N     1 
ATOM   17138 C  CA    . LEU   B  1  1114 ? 15.021  70.901  68.668  1.00 18.80 ? 1112 LEU   B CA    1 
ATOM   17139 C  C     . LEU   B  1  1114 ? 13.668  70.975  69.362  1.00 18.56 ? 1112 LEU   B C     1 
ATOM   17140 O  O     . LEU   B  1  1114 ? 13.420  70.235  70.319  1.00 17.62 ? 1112 LEU   B O     1 
ATOM   17141 C  CB    . LEU   B  1  1114 ? 15.911  72.050  69.139  1.00 20.62 ? 1112 LEU   B CB    1 
ATOM   17142 C  CG    . LEU   B  1  1114 ? 15.964  72.244  70.652  1.00 21.07 ? 1112 LEU   B CG    1 
ATOM   17143 C  CD1   . LEU   B  1  1114 ? 16.465  70.989  71.345  1.00 19.95 ? 1112 LEU   B CD1   1 
ATOM   17144 C  CD2   . LEU   B  1  1114 ? 16.823  73.449  71.022  1.00 24.11 ? 1112 LEU   B CD2   1 
ATOM   17145 N  N     . TYR   B  1  1115 ? 12.781  71.852  68.891  1.00 19.26 ? 1113 TYR   B N     1 
ATOM   17146 C  CA    . TYR   B  1  1115 ? 11.465  71.939  69.518  1.00 19.84 ? 1113 TYR   B CA    1 
ATOM   17147 C  C     . TYR   B  1  1115 ? 10.708  70.624  69.384  1.00 20.27 ? 1113 TYR   B C     1 
ATOM   17148 O  O     . TYR   B  1  1115 ? 10.053  70.182  70.335  1.00 18.51 ? 1113 TYR   B O     1 
ATOM   17149 C  CB    . TYR   B  1  1115 ? 10.657  73.076  68.909  1.00 21.99 ? 1113 TYR   B CB    1 
ATOM   17150 C  CG    . TYR   B  1  1115 ? 11.169  74.465  69.211  1.00 20.21 ? 1113 TYR   B CG    1 
ATOM   17151 C  CD1   . TYR   B  1  1115 ? 12.093  74.700  70.217  1.00 21.42 ? 1113 TYR   B CD1   1 
ATOM   17152 C  CD2   . TYR   B  1  1115 ? 10.722  75.542  68.469  1.00 24.91 ? 1113 TYR   B CD2   1 
ATOM   17153 C  CE1   . TYR   B  1  1115 ? 12.553  75.989  70.477  1.00 24.57 ? 1113 TYR   B CE1   1 
ATOM   17154 C  CE2   . TYR   B  1  1115 ? 11.167  76.818  68.719  1.00 26.64 ? 1113 TYR   B CE2   1 
ATOM   17155 C  CZ    . TYR   B  1  1115 ? 12.084  77.037  69.720  1.00 28.11 ? 1113 TYR   B CZ    1 
ATOM   17156 O  OH    . TYR   B  1  1115 ? 12.525  78.320  69.951  1.00 28.78 ? 1113 TYR   B OH    1 
ATOM   17157 N  N     . HIS   B  1  1116 ? 10.786  69.984  68.214  1.00 17.77 ? 1114 HIS   B N     1 
ATOM   17158 C  CA    . HIS   B  1  1116 ? 10.138  68.689  68.034  1.00 18.88 ? 1114 HIS   B CA    1 
ATOM   17159 C  C     . HIS   B  1  1116 ? 10.771  67.627  68.918  1.00 19.25 ? 1114 HIS   B C     1 
ATOM   17160 O  O     . HIS   B  1  1116 ? 10.065  66.795  69.497  1.00 20.22 ? 1114 HIS   B O     1 
ATOM   17161 C  CB    . HIS   B  1  1116 ? 10.183  68.257  66.571  1.00 19.18 ? 1114 HIS   B CB    1 
ATOM   17162 C  CG    . HIS   B  1  1116 ? 9.149   68.914  65.713  1.00 21.85 ? 1114 HIS   B CG    1 
ATOM   17163 N  ND1   . HIS   B  1  1116 ? 9.362   70.115  65.071  1.00 22.87 ? 1114 HIS   B ND1   1 
ATOM   17164 C  CD2   . HIS   B  1  1116 ? 7.891   68.531  65.386  1.00 23.66 ? 1114 HIS   B CD2   1 
ATOM   17165 C  CE1   . HIS   B  1  1116 ? 8.281   70.446  64.389  1.00 25.94 ? 1114 HIS   B CE1   1 
ATOM   17166 N  NE2   . HIS   B  1  1116 ? 7.375   69.502  64.562  1.00 26.64 ? 1114 HIS   B NE2   1 
ATOM   17167 N  N     . GLN   B  1  1117 ? 12.104  67.623  69.025  1.00 16.10 ? 1115 GLN   B N     1 
ATOM   17168 C  CA    . GLN   B  1  1117 ? 12.755  66.646  69.890  1.00 16.07 ? 1115 GLN   B CA    1 
ATOM   17169 C  C     . GLN   B  1  1117 ? 12.355  66.856  71.337  1.00 16.30 ? 1115 GLN   B C     1 
ATOM   17170 O  O     . GLN   B  1  1117 ? 12.089  65.889  72.060  1.00 16.93 ? 1115 GLN   B O     1 
ATOM   17171 C  CB    . GLN   B  1  1117 ? 14.275  66.766  69.763  1.00 17.23 ? 1115 GLN   B CB    1 
ATOM   17172 C  CG    . GLN   B  1  1117 ? 14.814  66.287  68.441  1.00 16.95 ? 1115 GLN   B CG    1 
ATOM   17173 C  CD    . GLN   B  1  1117 ? 16.306  66.476  68.339  1.00 17.15 ? 1115 GLN   B CD    1 
ATOM   17174 O  OE1   . GLN   B  1  1117 ? 16.916  67.145  69.170  1.00 19.17 ? 1115 GLN   B OE1   1 
ATOM   17175 N  NE2   . GLN   B  1  1117 ? 16.904  65.876  67.318  1.00 18.76 ? 1115 GLN   B NE2   1 
ATOM   17176 N  N     . LEU   B  1  1118 ? 12.350  68.109  71.781  1.00 16.05 ? 1116 LEU   B N     1 
ATOM   17177 C  CA    . LEU   B  1  1118 ? 11.928  68.424  73.140  1.00 17.26 ? 1116 LEU   B CA    1 
ATOM   17178 C  C     . LEU   B  1  1118 ? 10.507  67.964  73.381  1.00 17.18 ? 1116 LEU   B C     1 
ATOM   17179 O  O     . LEU   B  1  1118 ? 10.207  67.384  74.428  1.00 19.03 ? 1116 LEU   B O     1 
ATOM   17180 C  CB    . LEU   B  1  1118 ? 12.016  69.926  73.369  1.00 20.26 ? 1116 LEU   B CB    1 
ATOM   17181 C  CG    . LEU   B  1  1118 ? 13.420  70.431  73.652  1.00 21.45 ? 1116 LEU   B CG    1 
ATOM   17182 C  CD1   . LEU   B  1  1118 ? 13.441  71.951  73.578  1.00 23.21 ? 1116 LEU   B CD1   1 
ATOM   17183 C  CD2   . LEU   B  1  1118 ? 13.865  69.950  75.023  1.00 22.86 ? 1116 LEU   B CD2   1 
ATOM   17184 N  N     . ALA   B  1  1119 ? 9.623   68.204  72.416  1.00 18.60 ? 1117 ALA   B N     1 
ATOM   17185 C  CA    . ALA   B  1  1119 ? 8.231   67.802  72.580  1.00 18.28 ? 1117 ALA   B CA    1 
ATOM   17186 C  C     . ALA   B  1  1119 ? 8.138   66.301  72.788  1.00 18.12 ? 1117 ALA   B C     1 
ATOM   17187 O  O     . ALA   B  1  1119 ? 7.464   65.834  73.714  1.00 18.19 ? 1117 ALA   B O     1 
ATOM   17188 C  CB    . ALA   B  1  1119 ? 7.415   68.237  71.364  1.00 18.76 ? 1117 ALA   B CB    1 
ATOM   17189 N  N     . ALA   B  1  1120 ? 8.835   65.530  71.953  1.00 15.85 ? 1118 ALA   B N     1 
ATOM   17190 C  CA    . ALA   B  1  1120 ? 8.790   64.080  72.083  1.00 14.94 ? 1118 ALA   B CA    1 
ATOM   17191 C  C     . ALA   B  1  1120 ? 9.310   63.644  73.440  1.00 16.38 ? 1118 ALA   B C     1 
ATOM   17192 O  O     . ALA   B  1  1120 ? 8.686   62.820  74.122  1.00 17.39 ? 1118 ALA   B O     1 
ATOM   17193 C  CB    . ALA   B  1  1120 ? 9.593   63.416  70.964  1.00 16.99 ? 1118 ALA   B CB    1 
ATOM   17194 N  N     . ALA   B  1  1121 ? 10.457  64.186  73.859  1.00 15.24 ? 1119 ALA   B N     1 
ATOM   17195 C  CA    . ALA   B  1  1121 ? 11.061  63.736  75.103  1.00 15.63 ? 1119 ALA   B CA    1 
ATOM   17196 C  C     . ALA   B  1  1121 ? 10.259  64.182  76.317  1.00 14.36 ? 1119 ALA   B C     1 
ATOM   17197 O  O     . ALA   B  1  1121 ? 10.109  63.409  77.271  1.00 15.21 ? 1119 ALA   B O     1 
ATOM   17198 C  CB    . ALA   B  1  1121 ? 12.503  64.231  75.195  1.00 16.44 ? 1119 ALA   B CB    1 
ATOM   17199 N  N     . LEU   B  1  1122 ? 9.768   65.426  76.315  1.00 15.45 ? 1120 LEU   B N     1 
ATOM   17200 C  CA    . LEU   B  1  1122 ? 8.994   65.898  77.459  1.00 14.36 ? 1120 LEU   B CA    1 
ATOM   17201 C  C     . LEU   B  1  1122 ? 7.673   65.163  77.570  1.00 16.89 ? 1120 LEU   B C     1 
ATOM   17202 O  O     . LEU   B  1  1122 ? 7.237   64.836  78.681  1.00 16.63 ? 1120 LEU   B O     1 
ATOM   17203 C  CB    . LEU   B  1  1122 ? 8.752   67.400  77.379  1.00 16.77 ? 1120 LEU   B CB    1 
ATOM   17204 C  CG    . LEU   B  1  1122 ? 9.995   68.284  77.439  1.00 19.81 ? 1120 LEU   B CG    1 
ATOM   17205 C  CD1   . LEU   B  1  1122 ? 9.626   69.724  77.155  1.00 19.90 ? 1120 LEU   B CD1   1 
ATOM   17206 C  CD2   . LEU   B  1  1122 ? 10.702  68.161  78.783  1.00 19.26 ? 1120 LEU   B CD2   1 
ATOM   17207 N  N     . ALA   B  1  1123 ? 7.029   64.893  76.435  1.00 15.22 ? 1121 ALA   B N     1 
ATOM   17208 C  CA    . ALA   B  1  1123 ? 5.736   64.221  76.445  1.00 16.67 ? 1121 ALA   B CA    1 
ATOM   17209 C  C     . ALA   B  1  1123 ? 5.840   62.838  77.048  1.00 18.85 ? 1121 ALA   B C     1 
ATOM   17210 O  O     . ALA   B  1  1123 ? 4.837   62.310  77.546  1.00 16.19 ? 1121 ALA   B O     1 
ATOM   17211 C  CB    . ALA   B  1  1123 ? 5.215   64.092  75.022  1.00 16.74 ? 1121 ALA   B CB    1 
ATOM   17212 N  N     . THR   B  1  1124 ? 7.026   62.248  77.022  1.00 14.84 ? 1122 THR   B N     1 
ATOM   17213 C  CA    . THR   B  1  1124 ? 7.246   60.932  77.583  1.00 14.47 ? 1122 THR   B CA    1 
ATOM   17214 C  C     . THR   B  1  1124 ? 7.938   61.002  78.942  1.00 13.47 ? 1122 THR   B C     1 
ATOM   17215 O  O     . THR   B  1  1124 ? 8.441   59.989  79.428  1.00 16.23 ? 1122 THR   B O     1 
ATOM   17216 C  CB    . THR   B  1  1124 ? 8.003   60.054  76.583  1.00 15.85 ? 1122 THR   B CB    1 
ATOM   17217 O  OG1   . THR   B  1  1124 ? 9.085   60.800  76.008  1.00 15.16 ? 1122 THR   B OG1   1 
ATOM   17218 C  CG2   . THR   B  1  1124 ? 7.063   59.619  75.445  1.00 14.81 ? 1122 THR   B CG2   1 
ATOM   17219 N  N     . GLY   B  1  1125 ? 7.933   62.175  79.566  1.00 14.07 ? 1123 GLY   B N     1 
ATOM   17220 C  CA    . GLY   B  1  1125 ? 8.332   62.339  80.953  1.00 15.29 ? 1123 GLY   B CA    1 
ATOM   17221 C  C     . GLY   B  1  1125 ? 9.813   62.498  81.171  1.00 15.58 ? 1123 GLY   B C     1 
ATOM   17222 O  O     . GLY   B  1  1125 ? 10.266  62.483  82.321  1.00 16.81 ? 1123 GLY   B O     1 
ATOM   17223 N  N     . ASN   B  1  1126 ? 10.578  62.645  80.108  1.00 15.75 ? 1124 ASN   B N     1 
ATOM   17224 C  CA    . ASN   B  1  1126 ? 12.021  62.623  80.209  1.00 14.02 ? 1124 ASN   B CA    1 
ATOM   17225 C  C     . ASN   B  1  1126 ? 12.563  64.015  80.459  1.00 14.54 ? 1124 ASN   B C     1 
ATOM   17226 O  O     . ASN   B  1  1126 ? 11.943  65.030  80.148  1.00 16.63 ? 1124 ASN   B O     1 
ATOM   17227 C  CB    . ASN   B  1  1126 ? 12.620  62.072  78.924  1.00 16.18 ? 1124 ASN   B CB    1 
ATOM   17228 C  CG    . ASN   B  1  1126 ? 12.177  60.672  78.644  1.00 15.03 ? 1124 ASN   B CG    1 
ATOM   17229 O  OD1   . ASN   B  1  1126 ? 12.535  59.744  79.358  1.00 15.87 ? 1124 ASN   B OD1   1 
ATOM   17230 N  ND2   . ASN   B  1  1126 ? 11.377  60.505  77.595  1.00 14.77 ? 1124 ASN   B ND2   1 
ATOM   17231 N  N     . SER   B  1  1127 ? 13.769  64.032  81.021  1.00 16.36 ? 1125 SER   B N     1 
ATOM   17232 C  CA    . SER   B  1  1127 ? 14.628  65.199  80.951  1.00 16.69 ? 1125 SER   B CA    1 
ATOM   17233 C  C     . SER   B  1  1127 ? 15.513  65.044  79.723  1.00 17.33 ? 1125 SER   B C     1 
ATOM   17234 O  O     . SER   B  1  1127 ? 15.548  63.988  79.091  1.00 16.63 ? 1125 SER   B O     1 
ATOM   17235 C  CB    . SER   B  1  1127 ? 15.487  65.323  82.207  1.00 18.86 ? 1125 SER   B CB    1 
ATOM   17236 O  OG    . SER   B  1  1127 ? 16.291  64.172  82.402  1.00 22.48 ? 1125 SER   B OG    1 
ATOM   17237 N  N     . VAL   B  1  1128 ? 16.216  66.116  79.375  1.00 17.48 ? 1126 VAL   B N     1 
ATOM   17238 C  CA    . VAL   B  1  1128 ? 17.056  66.091  78.187  1.00 17.45 ? 1126 VAL   B CA    1 
ATOM   17239 C  C     . VAL   B  1  1128 ? 18.398  66.729  78.477  1.00 19.72 ? 1126 VAL   B C     1 
ATOM   17240 O  O     . VAL   B  1  1128 ? 18.528  67.621  79.323  1.00 19.94 ? 1126 VAL   B O     1 
ATOM   17241 C  CB    . VAL   B  1  1128 ? 16.411  66.790  76.972  1.00 17.45 ? 1126 VAL   B CB    1 
ATOM   17242 C  CG1   . VAL   B  1  1128 ? 15.064  66.150  76.626  1.00 17.47 ? 1126 VAL   B CG1   1 
ATOM   17243 C  CG2   . VAL   B  1  1128 ? 16.242  68.283  77.240  1.00 19.66 ? 1126 VAL   B CG2   1 
ATOM   17244 N  N     . ALA   B  1  1129 ? 19.397  66.253  77.750  1.00 17.08 ? 1127 ALA   B N     1 
ATOM   17245 C  CA    . ALA   B  1  1129 ? 20.670  66.939  77.600  1.00 17.76 ? 1127 ALA   B CA    1 
ATOM   17246 C  C     . ALA   B  1  1129 ? 20.792  67.272  76.125  1.00 17.02 ? 1127 ALA   B C     1 
ATOM   17247 O  O     . ALA   B  1  1129 ? 20.776  66.369  75.281  1.00 17.10 ? 1127 ALA   B O     1 
ATOM   17248 C  CB    . ALA   B  1  1129 ? 21.823  66.046  78.051  1.00 19.74 ? 1127 ALA   B CB    1 
ATOM   17249 N  N     . ILE   B  1  1130 ? 20.860  68.554  75.814  1.00 16.55 ? 1128 ILE   B N     1 
ATOM   17250 C  CA    . ILE   B  1  1130 ? 20.911  69.022  74.436  1.00 16.79 ? 1128 ILE   B CA    1 
ATOM   17251 C  C     . ILE   B  1  1130 ? 22.366  69.241  74.055  1.00 16.82 ? 1128 ILE   B C     1 
ATOM   17252 O  O     . ILE   B  1  1130 ? 23.129  69.876  74.799  1.00 18.37 ? 1128 ILE   B O     1 
ATOM   17253 C  CB    . ILE   B  1  1130 ? 20.109  70.319  74.252  1.00 18.04 ? 1128 ILE   B CB    1 
ATOM   17254 C  CG1   . ILE   B  1  1130 ? 18.700  70.182  74.851  1.00 19.14 ? 1128 ILE   B CG1   1 
ATOM   17255 C  CG2   . ILE   B  1  1130 ? 19.999  70.657  72.779  1.00 19.51 ? 1128 ILE   B CG2   1 
ATOM   17256 C  CD1   . ILE   B  1  1130 ? 17.992  71.502  74.962  1.00 19.69 ? 1128 ILE   B CD1   1 
ATOM   17257 N  N     . ASP   B  1  1131 ? 22.741  68.742  72.888  1.00 17.60 ? 1129 ASP   B N     1 
ATOM   17258 C  CA    . ASP   B  1  1131 ? 24.093  68.938  72.386  1.00 17.92 ? 1129 ASP   B CA    1 
ATOM   17259 C  C     . ASP   B  1  1131 ? 24.422  70.419  72.237  1.00 18.44 ? 1129 ASP   B C     1 
ATOM   17260 O  O     . ASP   B  1  1131 ? 23.835  71.116  71.402  1.00 19.44 ? 1129 ASP   B O     1 
ATOM   17261 C  CB    . ASP   B  1  1131 ? 24.209  68.242  71.039  1.00 16.72 ? 1129 ASP   B CB    1 
ATOM   17262 C  CG    . ASP   B  1  1131 ? 25.556  68.441  70.408  1.00 18.07 ? 1129 ASP   B CG    1 
ATOM   17263 O  OD1   . ASP   B  1  1131 ? 26.536  68.579  71.163  1.00 20.30 ? 1129 ASP   B OD1   1 
ATOM   17264 O  OD2   . ASP   B  1  1131 ? 25.602  68.484  69.170  1.00 21.32 ? 1129 ASP   B OD2   1 
ATOM   17265 N  N     . ALA   B  1  1132 ? 25.384  70.900  73.033  1.00 19.62 ? 1130 ALA   B N     1 
ATOM   17266 C  CA    . ALA   B  1  1132 ? 25.754  72.311  72.975  1.00 19.65 ? 1130 ALA   B CA    1 
ATOM   17267 C  C     . ALA   B  1  1132 ? 26.361  72.679  71.632  1.00 21.86 ? 1130 ALA   B C     1 
ATOM   17268 O  O     . ALA   B  1  1132 ? 26.256  73.831  71.198  1.00 22.56 ? 1130 ALA   B O     1 
ATOM   17269 C  CB    . ALA   B  1  1132 ? 26.729  72.648  74.103  1.00 20.54 ? 1130 ALA   B CB    1 
ATOM   17270 N  N     . ALA   B  1  1133 ? 26.983  71.716  70.952  1.00 21.38 ? 1131 ALA   B N     1 
ATOM   17271 C  CA    . ALA   B  1  1133 ? 27.588  72.012  69.662  1.00 25.38 ? 1131 ALA   B CA    1 
ATOM   17272 C  C     . ALA   B  1  1133 ? 26.556  72.362  68.601  1.00 25.13 ? 1131 ALA   B C     1 
ATOM   17273 O  O     . ALA   B  1  1133 ? 26.933  72.842  67.530  1.00 26.28 ? 1131 ALA   B O     1 
ATOM   17274 C  CB    . ALA   B  1  1133 ? 28.462  70.842  69.200  1.00 23.46 ? 1131 ALA   B CB    1 
ATOM   17275 N  N     . SER   B  1  1134 ? 25.265  72.135  68.873  1.00 22.66 ? 1132 SER   B N     1 
ATOM   17276 C  CA    . SER   B  1  1134 ? 24.216  72.561  67.956  1.00 23.46 ? 1132 SER   B CA    1 
ATOM   17277 C  C     . SER   B  1  1134 ? 24.148  74.073  67.833  1.00 21.16 ? 1132 SER   B C     1 
ATOM   17278 O  O     . SER   B  1  1134 ? 23.630  74.576  66.836  1.00 23.75 ? 1132 SER   B O     1 
ATOM   17279 C  CB    . SER   B  1  1134 ? 22.850  72.054  68.439  1.00 22.13 ? 1132 SER   B CB    1 
ATOM   17280 O  OG    . SER   B  1  1134 ? 22.472  72.691  69.653  1.00 21.79 ? 1132 SER   B OG    1 
ATOM   17281 N  N     . GLY   B  1  1135 ? 24.648  74.800  68.829  1.00 22.10 ? 1133 GLY   B N     1 
ATOM   17282 C  CA    . GLY   B  1  1135 ? 24.596  76.247  68.802  1.00 22.67 ? 1133 GLY   B CA    1 
ATOM   17283 C  C     . GLY   B  1  1135 ? 23.209  76.831  68.947  1.00 24.90 ? 1133 GLY   B C     1 
ATOM   17284 O  O     . GLY   B  1  1135 ? 23.009  78.006  68.634  1.00 24.89 ? 1133 GLY   B O     1 
ATOM   17285 N  N     . LEU   B  1  1136 ? 22.248  76.051  69.448  1.00 24.30 ? 1134 LEU   B N     1 
ATOM   17286 C  CA    . LEU   B  1  1136 ? 20.846  76.445  69.484  1.00 24.02 ? 1134 LEU   B CA    1 
ATOM   17287 C  C     . LEU   B  1  1136 ? 20.422  77.025  70.828  1.00 25.23 ? 1134 LEU   B C     1 
ATOM   17288 O  O     . LEU   B  1  1136 ? 19.218  77.136  71.090  1.00 24.02 ? 1134 LEU   B O     1 
ATOM   17289 C  CB    . LEU   B  1  1136 ? 19.966  75.251  69.112  1.00 21.28 ? 1134 LEU   B CB    1 
ATOM   17290 C  CG    . LEU   B  1  1136 ? 20.136  74.775  67.672  1.00 21.77 ? 1134 LEU   B CG    1 
ATOM   17291 C  CD1   . LEU   B  1  1136 ? 19.331  73.513  67.425  1.00 22.25 ? 1134 LEU   B CD1   1 
ATOM   17292 C  CD2   . LEU   B  1  1136 ? 19.731  75.869  66.698  1.00 26.41 ? 1134 LEU   B CD2   1 
ATOM   17293 N  N     . GLN   B  1  1137 ? 21.379  77.400  71.680  1.00 24.71 ? 1135 GLN   B N     1 
ATOM   17294 C  CA    . GLN   B  1  1137 ? 21.054  77.870  73.025  1.00 25.76 ? 1135 GLN   B CA    1 
ATOM   17295 C  C     . GLN   B  1  1137 ? 20.053  79.020  73.007  1.00 28.65 ? 1135 GLN   B C     1 
ATOM   17296 O  O     . GLN   B  1  1137 ? 19.140  79.071  73.842  1.00 28.13 ? 1135 GLN   B O     1 
ATOM   17297 C  CB    . GLN   B  1  1137 ? 22.329  78.285  73.762  1.00 31.08 ? 1135 GLN   B CB    1 
ATOM   17298 C  CG    . GLN   B  1  1137 ? 23.222  77.119  74.179  1.00 26.60 ? 1135 GLN   B CG    1 
ATOM   17299 C  CD    . GLN   B  1  1137 ? 24.153  76.632  73.073  1.00 26.25 ? 1135 GLN   B CD    1 
ATOM   17300 O  OE1   . GLN   B  1  1137 ? 24.003  76.984  71.905  1.00 26.99 ? 1135 GLN   B OE1   1 
ATOM   17301 N  NE2   . GLN   B  1  1137 ? 25.117  75.801  73.449  1.00 25.63 ? 1135 GLN   B NE2   1 
ATOM   17302 N  N     . ALA   B  1  1138 ? 20.193  79.940  72.049  1.00 25.89 ? 1136 ALA   B N     1 
ATOM   17303 C  CA    . ALA   B  1  1138 ? 19.298  81.091  71.978  1.00 28.95 ? 1136 ALA   B CA    1 
ATOM   17304 C  C     . ALA   B  1  1138 ? 17.856  80.690  71.704  1.00 29.84 ? 1136 ALA   B C     1 
ATOM   17305 O  O     . ALA   B  1  1138 ? 16.942  81.477  71.970  1.00 30.87 ? 1136 ALA   B O     1 
ATOM   17306 C  CB    . ALA   B  1  1138 ? 19.778  82.063  70.900  1.00 29.55 ? 1136 ALA   B CB    1 
ATOM   17307 N  N     . SER   B  1  1139 ? 17.629  79.487  71.180  1.00 27.67 ? 1137 SER   B N     1 
ATOM   17308 C  CA    . SER   B  1  1139 ? 16.276  79.053  70.857  1.00 26.81 ? 1137 SER   B CA    1 
ATOM   17309 C  C     . SER   B  1  1139 ? 15.448  78.753  72.098  1.00 28.86 ? 1137 SER   B C     1 
ATOM   17310 O  O     . SER   B  1  1139 ? 14.219  78.658  71.996  1.00 27.15 ? 1137 SER   B O     1 
ATOM   17311 C  CB    . SER   B  1  1139 ? 16.330  77.811  69.974  1.00 27.89 ? 1137 SER   B CB    1 
ATOM   17312 O  OG    . SER   B  1  1139 ? 16.871  78.124  68.707  1.00 29.30 ? 1137 SER   B OG    1 
ATOM   17313 N  N     . LEU   B  1  1140 ? 16.085  78.586  73.255  1.00 28.33 ? 1138 LEU   B N     1 
ATOM   17314 C  CA    . LEU   B  1  1140 ? 15.386  78.327  74.506  1.00 29.31 ? 1138 LEU   B CA    1 
ATOM   17315 C  C     . LEU   B  1  1140 ? 15.415  79.532  75.437  1.00 30.88 ? 1138 LEU   B C     1 
ATOM   17316 O  O     . LEU   B  1  1140 ? 15.371  79.379  76.660  1.00 33.93 ? 1138 LEU   B O     1 
ATOM   17317 C  CB    . LEU   B  1  1140 ? 15.936  77.086  75.203  1.00 30.26 ? 1138 LEU   B CB    1 
ATOM   17318 C  CG    . LEU   B  1  1140 ? 15.759  75.793  74.414  1.00 29.23 ? 1138 LEU   B CG    1 
ATOM   17319 C  CD1   . LEU   B  1  1140 ? 16.163  74.587  75.254  1.00 27.51 ? 1138 LEU   B CD1   1 
ATOM   17320 C  CD2   . LEU   B  1  1140 ? 14.329  75.661  73.872  1.00 30.02 ? 1138 LEU   B CD2   1 
ATOM   17321 N  N     . LYS   B  1  1141 ? 15.497  80.732  74.875  1.00 33.33 ? 1139 LYS   B N     1 
ATOM   17322 C  CA    . LYS   B  1  1141 ? 15.452  81.935  75.692  1.00 37.45 ? 1139 LYS   B CA    1 
ATOM   17323 C  C     . LYS   B  1  1141 ? 14.077  82.063  76.336  1.00 37.40 ? 1139 LYS   B C     1 
ATOM   17324 O  O     . LYS   B  1  1141 ? 13.050  81.827  75.692  1.00 38.24 ? 1139 LYS   B O     1 
ATOM   17325 C  CB    . LYS   B  1  1141 ? 15.737  83.165  74.831  1.00 36.56 ? 1139 LYS   B CB    1 
ATOM   17326 N  N     . ASN   B  1  1142 ? 14.065  82.412  77.625  1.00 39.93 ? 1140 ASN   B N     1 
ATOM   17327 C  CA    . ASN   B  1  1142 ? 12.834  82.664  78.374  1.00 38.67 ? 1140 ASN   B CA    1 
ATOM   17328 C  C     . ASN   B  1  1142 ? 11.985  81.407  78.546  1.00 36.90 ? 1140 ASN   B C     1 
ATOM   17329 O  O     . ASN   B  1  1142 ? 10.765  81.487  78.699  1.00 35.78 ? 1140 ASN   B O     1 
ATOM   17330 C  CB    . ASN   B  1  1142 ? 12.017  83.810  77.770  1.00 43.78 ? 1140 ASN   B CB    1 
ATOM   17331 C  CG    . ASN   B  1  1142 ? 12.840  85.069  77.577  1.00 47.73 ? 1140 ASN   B CG    1 
ATOM   17332 O  OD1   . ASN   B  1  1142 ? 13.592  85.472  78.465  1.00 50.01 ? 1140 ASN   B OD1   1 
ATOM   17333 N  ND2   . ASN   B  1  1142 ? 12.715  85.687  76.409  1.00 50.47 ? 1140 ASN   B ND2   1 
ATOM   17334 N  N     . LEU   B  1  1143 ? 12.621  80.243  78.520  1.00 35.02 ? 1141 LEU   B N     1 
ATOM   17335 C  CA    . LEU   B  1  1143 ? 11.907  79.003  78.763  1.00 33.62 ? 1141 LEU   B CA    1 
ATOM   17336 C  C     . LEU   B  1  1143 ? 11.338  79.019  80.182  1.00 30.18 ? 1141 LEU   B C     1 
ATOM   17337 O  O     . LEU   B  1  1143 ? 12.008  79.483  81.111  1.00 36.33 ? 1141 LEU   B O     1 
ATOM   17338 C  CB    . LEU   B  1  1143 ? 12.885  77.837  78.609  1.00 31.77 ? 1141 LEU   B CB    1 
ATOM   17339 C  CG    . LEU   B  1  1143 ? 12.356  76.423  78.418  1.00 31.74 ? 1141 LEU   B CG    1 
ATOM   17340 C  CD1   . LEU   B  1  1143 ? 11.652  76.301  77.083  1.00 28.50 ? 1141 LEU   B CD1   1 
ATOM   17341 C  CD2   . LEU   B  1  1143 ? 13.500  75.429  78.526  1.00 27.08 ? 1141 LEU   B CD2   1 
ATOM   17342 N  N     . PRO   B  1  1144 ? 10.109  78.541  80.385  1.00 30.84 ? 1142 PRO   B N     1 
ATOM   17343 C  CA    . PRO   B  1  1144 ? 9.568   78.455  81.748  1.00 34.59 ? 1142 PRO   B CA    1 
ATOM   17344 C  C     . PRO   B  1  1144 ? 10.448  77.576  82.622  1.00 31.69 ? 1142 PRO   B C     1 
ATOM   17345 O  O     . PRO   B  1  1144 ? 11.030  76.594  82.159  1.00 27.40 ? 1142 PRO   B O     1 
ATOM   17346 C  CB    . PRO   B  1  1144 ? 8.192   77.804  81.545  1.00 35.18 ? 1142 PRO   B CB    1 
ATOM   17347 C  CG    . PRO   B  1  1144 ? 7.876   77.979  80.102  1.00 33.73 ? 1142 PRO   B CG    1 
ATOM   17348 C  CD    . PRO   B  1  1144 ? 9.184   77.992  79.380  1.00 32.73 ? 1142 PRO   B CD    1 
ATOM   17349 N  N     . GLN   B  1  1145 ? 10.529  77.936  83.908  1.00 33.63 ? 1143 GLN   B N     1 
ATOM   17350 C  CA    . GLN   B  1  1145 ? 11.378  77.196  84.837  1.00 30.22 ? 1143 GLN   B CA    1 
ATOM   17351 C  C     . GLN   B  1  1145 ? 10.983  75.728  84.907  1.00 30.23 ? 1143 GLN   B C     1 
ATOM   17352 O  O     . GLN   B  1  1145 ? 11.844  74.853  85.050  1.00 27.12 ? 1143 GLN   B O     1 
ATOM   17353 C  CB    . GLN   B  1  1145 ? 11.329  77.832  86.229  1.00 33.79 ? 1143 GLN   B CB    1 
ATOM   17354 N  N     . THR   B  1  1146 ? 9.683   75.436  84.810  1.00 30.04 ? 1144 THR   B N     1 
ATOM   17355 C  CA    . THR   B  1  1146 ? 9.248   74.043  84.823  1.00 30.56 ? 1144 THR   B CA    1 
ATOM   17356 C  C     . THR   B  1  1146 ? 9.902   73.269  83.697  1.00 28.49 ? 1144 THR   B C     1 
ATOM   17357 O  O     . THR   B  1  1146 ? 10.330  72.123  83.880  1.00 31.29 ? 1144 THR   B O     1 
ATOM   17358 C  CB    . THR   B  1  1146 ? 7.733   73.969  84.670  1.00 30.49 ? 1144 THR   B CB    1 
ATOM   17359 O  OG1   . THR   B  1  1146 ? 7.306   74.964  83.731  1.00 37.95 ? 1144 THR   B OG1   1 
ATOM   17360 C  CG2   . THR   B  1  1146 ? 7.046   74.193  86.003  1.00 34.45 ? 1144 THR   B CG2   1 
ATOM   17361 N  N     . VAL   B  1  1147 ? 10.000  73.884  82.525  1.00 24.93 ? 1145 VAL   B N     1 
ATOM   17362 C  CA    . VAL   B  1  1147 ? 10.654  73.205  81.418  1.00 22.77 ? 1145 VAL   B CA    1 
ATOM   17363 C  C     . VAL   B  1  1147 ? 12.163  73.240  81.588  1.00 25.60 ? 1145 VAL   B C     1 
ATOM   17364 O  O     . VAL   B  1  1147 ? 12.841  72.229  81.387  1.00 24.94 ? 1145 VAL   B O     1 
ATOM   17365 C  CB    . VAL   B  1  1147 ? 10.208  73.792  80.070  1.00 21.95 ? 1145 VAL   B CB    1 
ATOM   17366 C  CG1   . VAL   B  1  1147 ? 10.798  72.973  78.930  1.00 26.69 ? 1145 VAL   B CG1   1 
ATOM   17367 C  CG2   . VAL   B  1  1147 ? 8.687   73.834  79.990  1.00 23.22 ? 1145 VAL   B CG2   1 
ATOM   17368 N  N     . GLY   B  1  1148 ? 12.707  74.394  81.980  1.00 24.79 ? 1146 GLY   B N     1 
ATOM   17369 C  CA    . GLY   B  1  1148 ? 14.146  74.502  82.151  1.00 24.45 ? 1146 GLY   B CA    1 
ATOM   17370 C  C     . GLY   B  1  1148 ? 14.717  73.501  83.133  1.00 25.52 ? 1146 GLY   B C     1 
ATOM   17371 O  O     . GLY   B  1  1148 ? 15.845  73.032  82.958  1.00 26.12 ? 1146 GLY   B O     1 
ATOM   17372 N  N     . LEU   B  1  1149 ? 13.954  73.156  84.174  1.00 25.12 ? 1147 LEU   B N     1 
ATOM   17373 C  CA    . LEU   B  1  1149 ? 14.421  72.187  85.159  1.00 26.75 ? 1147 LEU   B CA    1 
ATOM   17374 C  C     . LEU   B  1  1149 ? 14.721  70.839  84.522  1.00 26.18 ? 1147 LEU   B C     1 
ATOM   17375 O  O     . LEU   B  1  1149 ? 15.535  70.071  85.050  1.00 27.48 ? 1147 LEU   B O     1 
ATOM   17376 C  CB    . LEU   B  1  1149 ? 13.374  72.019  86.265  1.00 33.24 ? 1147 LEU   B CB    1 
ATOM   17377 N  N     . ARG   B  1  1150 ? 14.073  70.534  83.398  1.00 23.28 ? 1148 ARG   B N     1 
ATOM   17378 C  CA    . ARG   B  1  1150 ? 14.274  69.280  82.680  1.00 23.21 ? 1148 ARG   B CA    1 
ATOM   17379 C  C     . ARG   B  1  1150 ? 15.335  69.383  81.599  1.00 19.87 ? 1148 ARG   B C     1 
ATOM   17380 O  O     . ARG   B  1  1150 ? 15.624  68.378  80.942  1.00 20.21 ? 1148 ARG   B O     1 
ATOM   17381 C  CB    . ARG   B  1  1150 ? 12.981  68.859  81.989  1.00 21.43 ? 1148 ARG   B CB    1 
ATOM   17382 C  CG    . ARG   B  1  1150 ? 11.874  68.400  82.911  1.00 23.07 ? 1148 ARG   B CG    1 
ATOM   17383 C  CD    . ARG   B  1  1150 ? 11.557  66.942  82.679  1.00 24.97 ? 1148 ARG   B CD    1 
ATOM   17384 N  NE    . ARG   B  1  1150 ? 10.290  66.580  83.297  1.00 21.70 ? 1148 ARG   B NE    1 
ATOM   17385 C  CZ    . ARG   B  1  1150 ? 9.236   66.121  82.639  1.00 22.95 ? 1148 ARG   B CZ    1 
ATOM   17386 N  NH1   . ARG   B  1  1150 ? 9.279   65.884  81.335  1.00 20.36 ? 1148 ARG   B NH1   1 
ATOM   17387 N  NH2   . ARG   B  1  1150 ? 8.113   65.887  83.309  1.00 20.62 ? 1148 ARG   B NH2   1 
ATOM   17388 N  N     . VAL   B  1  1151 ? 15.883  70.568  81.366  1.00 21.66 ? 1149 VAL   B N     1 
ATOM   17389 C  CA    . VAL   B  1  1151 ? 16.762  70.822  80.233  1.00 19.98 ? 1149 VAL   B CA    1 
ATOM   17390 C  C     . VAL   B  1  1151 ? 18.165  71.091  80.745  1.00 23.14 ? 1149 VAL   B C     1 
ATOM   17391 O  O     . VAL   B  1  1151 ? 18.362  71.930  81.630  1.00 24.77 ? 1149 VAL   B O     1 
ATOM   17392 C  CB    . VAL   B  1  1151 ? 16.270  72.011  79.396  1.00 22.81 ? 1149 VAL   B CB    1 
ATOM   17393 C  CG1   . VAL   B  1  1151 ? 17.336  72.421  78.368  1.00 26.05 ? 1149 VAL   B CG1   1 
ATOM   17394 C  CG2   . VAL   B  1  1151 ? 14.973  71.662  78.712  1.00 24.35 ? 1149 VAL   B CG2   1 
ATOM   17395 N  N     . SER   B  1  1152 ? 19.136  70.387  80.186  1.00 21.13 ? 1150 SER   B N     1 
ATOM   17396 C  CA    . SER   B  1  1152 ? 20.528  70.750  80.360  1.00 21.58 ? 1150 SER   B CA    1 
ATOM   17397 C  C     . SER   B  1  1152 ? 21.185  70.765  78.991  1.00 22.57 ? 1150 SER   B C     1 
ATOM   17398 O  O     . SER   B  1  1152 ? 20.668  70.205  78.019  1.00 21.64 ? 1150 SER   B O     1 
ATOM   17399 C  CB    . SER   B  1  1152 ? 21.249  69.802  81.323  1.00 24.14 ? 1150 SER   B CB    1 
ATOM   17400 O  OG    . SER   B  1  1152 ? 21.280  68.487  80.821  1.00 27.94 ? 1150 SER   B OG    1 
ATOM   17401 N  N     . TRP   B  1  1153 ? 22.313  71.452  78.912  1.00 20.64 ? 1151 TRP   B N     1 
ATOM   17402 C  CA    . TRP   B  1  1153 ? 23.092  71.535  77.692  1.00 20.24 ? 1151 TRP   B CA    1 
ATOM   17403 C  C     . TRP   B  1  1153 ? 24.388  70.789  77.941  1.00 23.05 ? 1151 TRP   B C     1 
ATOM   17404 O  O     . TRP   B  1  1153 ? 25.003  70.949  78.997  1.00 25.44 ? 1151 TRP   B O     1 
ATOM   17405 C  CB    . TRP   B  1  1153 ? 23.379  72.992  77.342  1.00 22.39 ? 1151 TRP   B CB    1 
ATOM   17406 C  CG    . TRP   B  1  1153 ? 22.151  73.694  76.876  1.00 21.97 ? 1151 TRP   B CG    1 
ATOM   17407 C  CD1   . TRP   B  1  1153 ? 21.222  74.334  77.650  1.00 24.56 ? 1151 TRP   B CD1   1 
ATOM   17408 C  CD2   . TRP   B  1  1153 ? 21.712  73.824  75.524  1.00 22.55 ? 1151 TRP   B CD2   1 
ATOM   17409 N  NE1   . TRP   B  1  1153 ? 20.234  74.860  76.855  1.00 24.13 ? 1151 TRP   B NE1   1 
ATOM   17410 C  CE2   . TRP   B  1  1153 ? 20.504  74.552  75.546  1.00 23.03 ? 1151 TRP   B CE2   1 
ATOM   17411 C  CE3   . TRP   B  1  1153 ? 22.217  73.393  74.294  1.00 21.99 ? 1151 TRP   B CE3   1 
ATOM   17412 C  CZ2   . TRP   B  1  1153 ? 19.807  74.868  74.384  1.00 25.04 ? 1151 TRP   B CZ2   1 
ATOM   17413 C  CZ3   . TRP   B  1  1153 ? 21.525  73.700  73.152  1.00 22.80 ? 1151 TRP   B CZ3   1 
ATOM   17414 C  CH2   . TRP   B  1  1153 ? 20.326  74.428  73.201  1.00 24.23 ? 1151 TRP   B CH2   1 
ATOM   17415 N  N     . SER   B  1  1154 ? 24.780  69.947  76.993  1.00 19.46 ? 1152 SER   B N     1 
ATOM   17416 C  CA    . SER   B  1  1154 ? 25.955  69.109  77.182  1.00 19.65 ? 1152 SER   B CA    1 
ATOM   17417 C  C     . SER   B  1  1154 ? 27.005  69.463  76.149  1.00 19.34 ? 1152 SER   B C     1 
ATOM   17418 O  O     . SER   B  1  1154 ? 26.737  69.418  74.944  1.00 20.33 ? 1152 SER   B O     1 
ATOM   17419 C  CB    . SER   B  1  1154 ? 25.604  67.630  77.065  1.00 21.94 ? 1152 SER   B CB    1 
ATOM   17420 O  OG    . SER   B  1  1154 ? 26.788  66.876  77.216  1.00 20.50 ? 1152 SER   B OG    1 
ATOM   17421 N  N     . LYS   B  1  1155 ? 28.198  69.806  76.633  1.00 20.11 ? 1153 LYS   B N     1 
ATOM   17422 C  CA    . LYS   B  1  1155 ? 29.398  69.923  75.819  1.00 24.07 ? 1153 LYS   B CA    1 
ATOM   17423 C  C     . LYS   B  1  1155 ? 30.279  68.693  75.957  1.00 23.91 ? 1153 LYS   B C     1 
ATOM   17424 O  O     . LYS   B  1  1155 ? 31.428  68.704  75.503  1.00 24.54 ? 1153 LYS   B O     1 
ATOM   17425 C  CB    . LYS   B  1  1155 ? 30.186  71.170  76.225  1.00 26.25 ? 1153 LYS   B CB    1 
ATOM   17426 N  N     . ASP   B  1  1156 ? 29.778  67.646  76.600  1.00 19.54 ? 1154 ASP   B N     1 
ATOM   17427 C  CA    . ASP   B  1  1156 ? 30.573  66.447  76.858  1.00 18.14 ? 1154 ASP   B CA    1 
ATOM   17428 C  C     . ASP   B  1  1156 ? 29.564  65.319  77.093  1.00 18.86 ? 1154 ASP   B C     1 
ATOM   17429 O  O     . ASP   B  1  1156 ? 29.161  65.065  78.228  1.00 18.52 ? 1154 ASP   B O     1 
ATOM   17430 C  CB    . ASP   B  1  1156 ? 31.470  66.643  78.059  1.00 19.96 ? 1154 ASP   B CB    1 
ATOM   17431 C  CG    . ASP   B  1  1156 ? 32.476  65.528  78.221  1.00 18.88 ? 1154 ASP   B CG    1 
ATOM   17432 O  OD1   . ASP   B  1  1156 ? 32.201  64.387  77.800  1.00 17.92 ? 1154 ASP   B OD1   1 
ATOM   17433 O  OD2   . ASP   B  1  1156 ? 33.560  65.812  78.765  1.00 19.62 ? 1154 ASP   B OD2   1 
ATOM   17434 N  N     . TRP   B  1  1157 ? 29.187  64.644  76.011  1.00 16.51 ? 1155 TRP   B N     1 
ATOM   17435 C  CA    . TRP   B  1  1157 ? 28.100  63.676  76.123  1.00 16.66 ? 1155 TRP   B CA    1 
ATOM   17436 C  C     . TRP   B  1  1157 ? 28.479  62.534  77.045  1.00 19.04 ? 1155 TRP   B C     1 
ATOM   17437 O  O     . TRP   B  1  1157 ? 27.667  62.085  77.860  1.00 19.56 ? 1155 TRP   B O     1 
ATOM   17438 C  CB    . TRP   B  1  1157 ? 27.715  63.109  74.763  1.00 19.02 ? 1155 TRP   B CB    1 
ATOM   17439 C  CG    . TRP   B  1  1157 ? 27.275  64.091  73.748  1.00 16.45 ? 1155 TRP   B CG    1 
ATOM   17440 C  CD1   . TRP   B  1  1157 ? 27.036  65.422  73.921  1.00 16.91 ? 1155 TRP   B CD1   1 
ATOM   17441 C  CD2   . TRP   B  1  1157 ? 27.050  63.816  72.369  1.00 16.65 ? 1155 TRP   B CD2   1 
ATOM   17442 N  NE1   . TRP   B  1  1157 ? 26.671  65.988  72.729  1.00 17.56 ? 1155 TRP   B NE1   1 
ATOM   17443 C  CE2   . TRP   B  1  1157 ? 26.684  65.022  71.756  1.00 16.45 ? 1155 TRP   B CE2   1 
ATOM   17444 C  CE3   . TRP   B  1  1157 ? 27.140  62.658  71.586  1.00 18.52 ? 1155 TRP   B CE3   1 
ATOM   17445 C  CZ2   . TRP   B  1  1157 ? 26.384  65.108  70.404  1.00 18.96 ? 1155 TRP   B CZ2   1 
ATOM   17446 C  CZ3   . TRP   B  1  1157 ? 26.840  62.746  70.237  1.00 18.93 ? 1155 TRP   B CZ3   1 
ATOM   17447 C  CH2   . TRP   B  1  1157 ? 26.470  63.962  69.663  1.00 19.50 ? 1155 TRP   B CH2   1 
ATOM   17448 N  N     . ALA   B  1  1158 ? 29.719  62.061  76.942  1.00 17.38 ? 1156 ALA   B N     1 
ATOM   17449 C  CA    . ALA   B  1  1158 ? 30.118  60.906  77.728  1.00 18.29 ? 1156 ALA   B CA    1 
ATOM   17450 C  C     . ALA   B  1  1158 ? 30.185  61.233  79.210  1.00 19.62 ? 1156 ALA   B C     1 
ATOM   17451 O  O     . ALA   B  1  1158 ? 29.914  60.363  80.042  1.00 24.47 ? 1156 ALA   B O     1 
ATOM   17452 C  CB    . ALA   B  1  1158 ? 31.468  60.390  77.232  1.00 16.88 ? 1156 ALA   B CB    1 
ATOM   17453 N  N     . ALA   B  1  1159 ? 30.547  62.469  79.564  1.00 17.76 ? 1157 ALA   B N     1 
ATOM   17454 C  CA    . ALA   B  1  1159 ? 30.620  62.839  80.970  1.00 20.74 ? 1157 ALA   B CA    1 
ATOM   17455 C  C     . ALA   B  1  1159 ? 29.251  63.129  81.564  1.00 21.82 ? 1157 ALA   B C     1 
ATOM   17456 O  O     . ALA   B  1  1159 ? 29.075  62.990  82.779  1.00 22.73 ? 1157 ALA   B O     1 
ATOM   17457 C  CB    . ALA   B  1  1159 ? 31.535  64.052  81.154  1.00 21.35 ? 1157 ALA   B CB    1 
ATOM   17458 N  N     . ASP   B  1  1160 ? 28.284  63.503  80.735  1.00 20.56 ? 1158 ASP   B N     1 
ATOM   17459 C  CA    . ASP   B  1  1160 ? 26.995  63.989  81.199  1.00 22.06 ? 1158 ASP   B CA    1 
ATOM   17460 C  C     . ASP   B  1  1160 ? 25.926  62.912  81.220  1.00 21.01 ? 1158 ASP   B C     1 
ATOM   17461 O  O     . ASP   B  1  1160 ? 24.789  63.195  81.618  1.00 24.86 ? 1158 ASP   B O     1 
ATOM   17462 C  CB    . ASP   B  1  1160 ? 26.558  65.169  80.338  1.00 19.81 ? 1158 ASP   B CB    1 
ATOM   17463 C  CG    . ASP   B  1  1160 ? 27.454  66.371  80.534  1.00 21.37 ? 1158 ASP   B CG    1 
ATOM   17464 O  OD1   . ASP   B  1  1160 ? 28.257  66.351  81.495  1.00 26.46 ? 1158 ASP   B OD1   1 
ATOM   17465 O  OD2   . ASP   B  1  1160 ? 27.389  67.321  79.730  1.00 23.81 ? 1158 ASP   B OD2   1 
ATOM   17466 N  N     . GLY   B  1  1161 ? 26.257  61.694  80.807  1.00 19.02 ? 1159 GLY   B N     1 
ATOM   17467 C  CA    . GLY   B  1  1161 ? 25.350  60.577  80.907  1.00 22.10 ? 1159 GLY   B CA    1 
ATOM   17468 C  C     . GLY   B  1  1161 ? 25.313  60.009  82.312  1.00 26.15 ? 1159 GLY   B C     1 
ATOM   17469 O  O     . GLY   B  1  1161 ? 25.838  60.602  83.259  1.00 27.19 ? 1159 GLY   B O     1 
ATOM   17470 N  N     . PRO   B  1  1162 ? 24.711  58.829  82.472  1.00 27.20 ? 1160 PRO   B N     1 
ATOM   17471 C  CA    . PRO   B  1  1162 ? 24.128  57.989  81.422  1.00 23.00 ? 1160 PRO   B CA    1 
ATOM   17472 C  C     . PRO   B  1  1162 ? 22.816  58.548  80.924  1.00 21.53 ? 1160 PRO   B C     1 
ATOM   17473 O  O     . PRO   B  1  1162 ? 22.002  59.117  81.652  1.00 22.60 ? 1160 PRO   B O     1 
ATOM   17474 C  CB    . PRO   B  1  1162 ? 23.904  56.652  82.142  1.00 27.34 ? 1160 PRO   B CB    1 
ATOM   17475 C  CG    . PRO   B  1  1162 ? 23.606  57.054  83.553  1.00 28.96 ? 1160 PRO   B CG    1 
ATOM   17476 C  CD    . PRO   B  1  1162 ? 24.522  58.235  83.810  1.00 27.46 ? 1160 PRO   B CD    1 
ATOM   17477 N  N     . PHE   B  1  1163 ? 22.614  58.395  79.632  1.00 16.80 ? 1161 PHE   B N     1 
ATOM   17478 C  CA    . PHE   B  1  1163 ? 21.341  58.708  79.017  1.00 16.80 ? 1161 PHE   B CA    1 
ATOM   17479 C  C     . PHE   B  1  1163 ? 20.557  57.423  78.854  1.00 16.68 ? 1161 PHE   B C     1 
ATOM   17480 O  O     . PHE   B  1  1163 ? 21.045  56.330  79.124  1.00 16.76 ? 1161 PHE   B O     1 
ATOM   17481 C  CB    . PHE   B  1  1163 ? 21.574  59.419  77.686  1.00 19.51 ? 1161 PHE   B CB    1 
ATOM   17482 C  CG    . PHE   B  1  1163 ? 22.411  60.640  77.830  1.00 18.82 ? 1161 PHE   B CG    1 
ATOM   17483 C  CD1   . PHE   B  1  1163 ? 21.989  61.691  78.619  1.00 22.23 ? 1161 PHE   B CD1   1 
ATOM   17484 C  CD2   . PHE   B  1  1163 ? 23.652  60.717  77.221  1.00 20.44 ? 1161 PHE   B CD2   1 
ATOM   17485 C  CE1   . PHE   B  1  1163 ? 22.768  62.813  78.780  1.00 22.39 ? 1161 PHE   B CE1   1 
ATOM   17486 C  CE2   . PHE   B  1  1163 ? 24.440  61.844  77.374  1.00 20.86 ? 1161 PHE   B CE2   1 
ATOM   17487 C  CZ    . PHE   B  1  1163 ? 23.998  62.895  78.153  1.00 20.90 ? 1161 PHE   B CZ    1 
ATOM   17488 N  N     . ALA   B  1  1164 ? 19.302  57.570  78.441  1.00 16.60 ? 1162 ALA   B N     1 
ATOM   17489 C  CA    . ALA   B  1  1164 ? 18.431  56.423  78.228  1.00 19.36 ? 1162 ALA   B CA    1 
ATOM   17490 C  C     . ALA   B  1  1164 ? 17.851  56.409  76.824  1.00 18.32 ? 1162 ALA   B C     1 
ATOM   17491 O  O     . ALA   B  1  1164 ? 16.898  55.665  76.552  1.00 18.87 ? 1162 ALA   B O     1 
ATOM   17492 C  CB    . ALA   B  1  1164 ? 17.329  56.383  79.292  1.00 18.83 ? 1162 ALA   B CB    1 
ATOM   17493 N  N     . GLY   B  1  1165 ? 18.405  57.219  75.932  1.00 16.60 ? 1163 GLY   B N     1 
ATOM   17494 C  CA    . GLY   B  1  1165 ? 17.976  57.283  74.552  1.00 16.97 ? 1163 GLY   B CA    1 
ATOM   17495 C  C     . GLY   B  1  1165 ? 18.571  58.521  73.926  1.00 16.70 ? 1163 GLY   B C     1 
ATOM   17496 O  O     . GLY   B  1  1165 ? 19.180  59.353  74.597  1.00 16.60 ? 1163 GLY   B O     1 
ATOM   17497 N  N     . ALA   B  1  1166 ? 18.386  58.633  72.618  1.00 16.02 ? 1164 ALA   B N     1 
ATOM   17498 C  CA    . ALA   B  1  1166 ? 18.896  59.798  71.919  1.00 15.00 ? 1164 ALA   B CA    1 
ATOM   17499 C  C     . ALA   B  1  1166 ? 18.005  60.098  70.738  1.00 17.10 ? 1164 ALA   B C     1 
ATOM   17500 O  O     . ALA   B  1  1166 ? 17.526  59.182  70.068  1.00 17.82 ? 1164 ALA   B O     1 
ATOM   17501 C  CB    . ALA   B  1  1166 ? 20.331  59.586  71.435  1.00 17.14 ? 1164 ALA   B CB    1 
ATOM   17502 N  N     . LEU   B  1  1167 ? 17.781  61.384  70.499  1.00 15.98 ? 1165 LEU   B N     1 
ATOM   17503 C  CA    . LEU   B  1  1167 ? 17.085  61.857  69.315  1.00 16.21 ? 1165 LEU   B CA    1 
ATOM   17504 C  C     . LEU   B  1  1167 ? 18.066  62.696  68.522  1.00 19.09 ? 1165 LEU   B C     1 
ATOM   17505 O  O     . LEU   B  1  1167 ? 18.709  63.588  69.077  1.00 17.77 ? 1165 LEU   B O     1 
ATOM   17506 C  CB    . LEU   B  1  1167 ? 15.872  62.708  69.684  1.00 16.00 ? 1165 LEU   B CB    1 
ATOM   17507 C  CG    . LEU   B  1  1167 ? 14.863  62.024  70.610  1.00 16.33 ? 1165 LEU   B CG    1 
ATOM   17508 C  CD1   . LEU   B  1  1167 ? 13.740  62.990  70.939  1.00 18.98 ? 1165 LEU   B CD1   1 
ATOM   17509 C  CD2   . LEU   B  1  1167 ? 14.298  60.748  69.982  1.00 19.26 ? 1165 LEU   B CD2   1 
ATOM   17510 N  N     . VAL   B  1  1168 ? 18.181  62.404  67.239  1.00 17.68 ? 1166 VAL   B N     1 
ATOM   17511 C  CA    . VAL   B  1  1168 ? 19.197  63.006  66.393  1.00 18.65 ? 1166 VAL   B CA    1 
ATOM   17512 C  C     . VAL   B  1  1168 ? 18.497  63.594  65.184  1.00 17.76 ? 1166 VAL   B C     1 
ATOM   17513 O  O     . VAL   B  1  1168 ? 17.601  62.968  64.607  1.00 18.84 ? 1166 VAL   B O     1 
ATOM   17514 C  CB    . VAL   B  1  1168 ? 20.235  61.955  65.955  1.00 18.49 ? 1166 VAL   B CB    1 
ATOM   17515 C  CG1   . VAL   B  1  1168 ? 21.307  62.594  65.065  1.00 18.54 ? 1166 VAL   B CG1   1 
ATOM   17516 C  CG2   . VAL   B  1  1168 ? 20.865  61.287  67.177  1.00 18.27 ? 1166 VAL   B CG2   1 
ATOM   17517 N  N     . GLU   B  1  1169 ? 18.896  64.800  64.804  1.00 18.21 ? 1167 GLU   B N     1 
ATOM   17518 C  CA    . GLU   B  1  1169 ? 18.418  65.455  63.599  1.00 19.16 ? 1167 GLU   B CA    1 
ATOM   17519 C  C     . GLU   B  1  1169 ? 19.619  65.729  62.705  1.00 19.01 ? 1167 GLU   B C     1 
ATOM   17520 O  O     . GLU   B  1  1169 ? 20.649  66.209  63.187  1.00 20.93 ? 1167 GLU   B O     1 
ATOM   17521 C  CB    . GLU   B  1  1169 ? 17.750  66.783  63.949  1.00 18.91 ? 1167 GLU   B CB    1 
ATOM   17522 C  CG    . GLU   B  1  1169 ? 17.271  67.567  62.736  1.00 20.43 ? 1167 GLU   B CG    1 
ATOM   17523 C  CD    . GLU   B  1  1169 ? 16.872  68.997  63.075  1.00 21.73 ? 1167 GLU   B CD    1 
ATOM   17524 O  OE1   . GLU   B  1  1169 ? 17.103  69.441  64.219  1.00 20.57 ? 1167 GLU   B OE1   1 
ATOM   17525 O  OE2   . GLU   B  1  1169 ? 16.313  69.677  62.195  1.00 22.85 ? 1167 GLU   B OE2   1 
ATOM   17526 N  N     . GLY   B  1  1170 ? 19.499  65.411  61.427  1.00 20.50 ? 1168 GLY   B N     1 
ATOM   17527 C  CA    . GLY   B  1  1170 ? 20.581  65.720  60.508  1.00 21.80 ? 1168 GLY   B CA    1 
ATOM   17528 C  C     . GLY   B  1  1170 ? 20.440  64.963  59.212  1.00 23.97 ? 1168 GLY   B C     1 
ATOM   17529 O  O     . GLY   B  1  1170 ? 19.559  64.122  59.044  1.00 22.70 ? 1168 GLY   B O     1 
ATOM   17530 N  N     . ASP   B  1  1171 ? 21.330  65.291  58.274  1.00 24.98 ? 1169 ASP   B N     1 
ATOM   17531 C  CA    . ASP   B  1  1171 ? 21.396  64.526  57.042  1.00 26.25 ? 1169 ASP   B CA    1 
ATOM   17532 C  C     . ASP   B  1  1171 ? 22.073  63.187  57.311  1.00 24.48 ? 1169 ASP   B C     1 
ATOM   17533 O  O     . ASP   B  1  1171 ? 22.538  62.914  58.418  1.00 22.38 ? 1169 ASP   B O     1 
ATOM   17534 C  CB    . ASP   B  1  1171 ? 22.040  65.330  55.909  1.00 26.39 ? 1169 ASP   B CB    1 
ATOM   17535 C  CG    . ASP   B  1  1171 ? 23.503  65.666  56.159  1.00 26.92 ? 1169 ASP   B CG    1 
ATOM   17536 O  OD1   . ASP   B  1  1171 ? 24.126  65.178  57.127  1.00 27.11 ? 1169 ASP   B OD1   1 
ATOM   17537 O  OD2   . ASP   B  1  1171 ? 24.048  66.450  55.348  1.00 33.76 ? 1169 ASP   B OD2   1 
ATOM   17538 N  N     . ALA   B  1  1172 ? 22.131  62.339  56.283  1.00 24.17 ? 1170 ALA   B N     1 
ATOM   17539 C  CA    . ALA   B  1  1172 ? 22.618  60.981  56.488  1.00 24.61 ? 1170 ALA   B CA    1 
ATOM   17540 C  C     . ALA   B  1  1172 ? 24.013  60.977  57.103  1.00 25.33 ? 1170 ALA   B C     1 
ATOM   17541 O  O     . ALA   B  1  1172 ? 24.278  60.241  58.060  1.00 26.32 ? 1170 ALA   B O     1 
ATOM   17542 C  CB    . ALA   B  1  1172 ? 22.595  60.208  55.170  1.00 27.59 ? 1170 ALA   B CB    1 
ATOM   17543 N  N     . GLU   B  1  1173 ? 24.919  61.807  56.585  1.00 23.83 ? 1171 GLU   B N     1 
ATOM   17544 C  CA    . GLU   B  1  1173 ? 26.277  61.748  57.113  1.00 25.55 ? 1171 GLU   B CA    1 
ATOM   17545 C  C     . GLU   B  1  1173 ? 26.373  62.311  58.528  1.00 24.28 ? 1171 GLU   B C     1 
ATOM   17546 O  O     . GLU   B  1  1173 ? 27.167  61.814  59.333  1.00 24.24 ? 1171 GLU   B O     1 
ATOM   17547 C  CB    . GLU   B  1  1173 ? 27.275  62.379  56.142  1.00 34.23 ? 1171 GLU   B CB    1 
ATOM   17548 C  CG    . GLU   B  1  1173 ? 27.479  61.540  54.877  1.00 34.37 ? 1171 GLU   B CG    1 
ATOM   17549 C  CD    . GLU   B  1  1173 ? 27.815  60.076  55.171  1.00 37.29 ? 1171 GLU   B CD    1 
ATOM   17550 O  OE1   . GLU   B  1  1173 ? 28.686  59.807  56.029  1.00 37.51 ? 1171 GLU   B OE1   1 
ATOM   17551 O  OE2   . GLU   B  1  1173 ? 27.200  59.187  54.540  1.00 40.75 ? 1171 GLU   B OE2   1 
ATOM   17552 N  N     . ARG   B  1  1174 ? 25.563  63.324  58.855  1.00 23.94 ? 1172 ARG   B N     1 
ATOM   17553 C  CA    . ARG   B  1  1174 ? 25.484  63.781  60.239  1.00 22.98 ? 1172 ARG   B CA    1 
ATOM   17554 C  C     . ARG   B  1  1174 ? 24.963  62.669  61.138  1.00 20.48 ? 1172 ARG   B C     1 
ATOM   17555 O  O     . ARG   B  1  1174 ? 25.524  62.409  62.207  1.00 21.26 ? 1172 ARG   B O     1 
ATOM   17556 C  CB    . ARG   B  1  1174 ? 24.580  65.013  60.328  1.00 22.89 ? 1172 ARG   B CB    1 
ATOM   17557 C  CG    . ARG   B  1  1174 ? 24.313  65.517  61.741  1.00 22.45 ? 1172 ARG   B CG    1 
ATOM   17558 C  CD    . ARG   B  1  1174 ? 25.604  65.906  62.431  1.00 24.13 ? 1172 ARG   B CD    1 
ATOM   17559 N  NE    . ARG   B  1  1174 ? 25.344  66.445  63.759  1.00 24.42 ? 1172 ARG   B NE    1 
ATOM   17560 C  CZ    . ARG   B  1  1174 ? 26.252  66.552  64.718  1.00 23.58 ? 1172 ARG   B CZ    1 
ATOM   17561 N  NH1   . ARG   B  1  1174 ? 27.510  66.186  64.525  1.00 23.96 ? 1172 ARG   B NH1   1 
ATOM   17562 N  NH2   . ARG   B  1  1174 ? 25.889  67.027  65.905  1.00 24.31 ? 1172 ARG   B NH2   1 
ATOM   17563 N  N     . ILE   B  1  1175 ? 23.907  61.984  60.698  1.00 20.11 ? 1173 ILE   B N     1 
ATOM   17564 C  CA    . ILE   B  1  1175 ? 23.359  60.876  61.476  1.00 19.80 ? 1173 ILE   B CA    1 
ATOM   17565 C  C     . ILE   B  1  1175 ? 24.414  59.804  61.713  1.00 20.43 ? 1173 ILE   B C     1 
ATOM   17566 O  O     . ILE   B  1  1175 ? 24.568  59.299  62.830  1.00 19.67 ? 1173 ILE   B O     1 
ATOM   17567 C  CB    . ILE   B  1  1175 ? 22.105  60.318  60.787  1.00 20.61 ? 1173 ILE   B CB    1 
ATOM   17568 C  CG1   . ILE   B  1  1175 ? 20.963  61.327  60.893  1.00 21.39 ? 1173 ILE   B CG1   1 
ATOM   17569 C  CG2   . ILE   B  1  1175 ? 21.722  58.979  61.377  1.00 19.82 ? 1173 ILE   B CG2   1 
ATOM   17570 C  CD1   . ILE   B  1  1175 ? 19.786  61.004  60.000  1.00 21.85 ? 1173 ILE   B CD1   1 
ATOM   17571 N  N     . ARG   B  1  1176 ? 25.164  59.437  60.671  1.00 22.53 ? 1174 ARG   B N     1 
ATOM   17572 C  CA    . ARG   B  1  1176 ? 26.173  58.399  60.854  1.00 21.47 ? 1174 ARG   B CA    1 
ATOM   17573 C  C     . ARG   B  1  1176 ? 27.233  58.837  61.854  1.00 20.14 ? 1174 ARG   B C     1 
ATOM   17574 O  O     . ARG   B  1  1176 ? 27.630  58.063  62.728  1.00 20.07 ? 1174 ARG   B O     1 
ATOM   17575 C  CB    . ARG   B  1  1176 ? 26.824  58.042  59.518  1.00 22.64 ? 1174 ARG   B CB    1 
ATOM   17576 C  CG    . ARG   B  1  1176 ? 27.741  56.835  59.599  1.00 26.37 ? 1174 ARG   B CG    1 
ATOM   17577 C  CD    . ARG   B  1  1176 ? 28.719  56.753  58.414  1.00 29.63 ? 1174 ARG   B CD    1 
ATOM   17578 N  NE    . ARG   B  1  1176 ? 28.071  56.984  57.127  1.00 33.05 ? 1174 ARG   B NE    1 
ATOM   17579 C  CZ    . ARG   B  1  1176 ? 27.546  56.034  56.363  1.00 35.32 ? 1174 ARG   B CZ    1 
ATOM   17580 N  NH1   . ARG   B  1  1176 ? 27.566  54.763  56.727  1.00 32.95 ? 1174 ARG   B NH1   1 
ATOM   17581 N  NH2   . ARG   B  1  1176 ? 26.994  56.368  55.199  1.00 36.07 ? 1174 ARG   B NH2   1 
ATOM   17582 N  N     . ALA   B  1  1177 ? 27.688  60.086  61.747  1.00 21.12 ? 1175 ALA   B N     1 
ATOM   17583 C  CA    . ALA   B  1  1177 ? 28.715  60.574  62.658  1.00 21.50 ? 1175 ALA   B CA    1 
ATOM   17584 C  C     . ALA   B  1  1177 ? 28.210  60.601  64.092  1.00 19.51 ? 1175 ALA   B C     1 
ATOM   17585 O  O     . ALA   B  1  1177 ? 28.930  60.225  65.022  1.00 20.66 ? 1175 ALA   B O     1 
ATOM   17586 C  CB    . ALA   B  1  1177 ? 29.155  61.971  62.230  1.00 22.89 ? 1175 ALA   B CB    1 
ATOM   17587 N  N     . VAL   B  1  1178 ? 26.965  61.031  64.285  1.00 19.94 ? 1176 VAL   B N     1 
ATOM   17588 C  CA    . VAL   B  1  1178 ? 26.411  61.083  65.632  1.00 19.11 ? 1176 VAL   B CA    1 
ATOM   17589 C  C     . VAL   B  1  1178 ? 26.207  59.678  66.167  1.00 19.78 ? 1176 VAL   B C     1 
ATOM   17590 O  O     . VAL   B  1  1178 ? 26.496  59.388  67.331  1.00 20.38 ? 1176 VAL   B O     1 
ATOM   17591 C  CB    . VAL   B  1  1178 ? 25.113  61.899  65.627  1.00 22.22 ? 1176 VAL   B CB    1 
ATOM   17592 C  CG1   . VAL   B  1  1178 ? 24.420  61.769  66.965  1.00 21.02 ? 1176 VAL   B CG1   1 
ATOM   17593 C  CG2   . VAL   B  1  1178 ? 25.419  63.356  65.329  1.00 21.40 ? 1176 VAL   B CG2   1 
ATOM   17594 N  N     . ASN   B  1  1179 ? 25.716  58.780  65.316  1.00 18.70 ? 1177 ASN   B N     1 
ATOM   17595 C  CA    . ASN   B  1  1179 ? 25.492  57.410  65.744  1.00 19.72 ? 1177 ASN   B CA    1 
ATOM   17596 C  C     . ASN   B  1  1179 ? 26.799  56.755  66.162  1.00 20.54 ? 1177 ASN   B C     1 
ATOM   17597 O  O     . ASN   B  1  1179 ? 26.853  56.028  67.158  1.00 20.32 ? 1177 ASN   B O     1 
ATOM   17598 C  CB    . ASN   B  1  1179 ? 24.809  56.649  64.607  1.00 19.66 ? 1177 ASN   B CB    1 
ATOM   17599 C  CG    . ASN   B  1  1179 ? 24.084  55.412  65.080  1.00 22.78 ? 1177 ASN   B CG    1 
ATOM   17600 O  OD1   . ASN   B  1  1179 ? 23.650  55.331  66.231  1.00 22.96 ? 1177 ASN   B OD1   1 
ATOM   17601 N  ND2   . ASN   B  1  1179 ? 23.939  54.439  64.184  1.00 20.98 ? 1177 ASN   B ND2   1 
ATOM   17602 N  N     . LYS   B  1  1180 ? 27.878  57.016  65.421  1.00 19.53 ? 1178 LYS   B N     1 
ATOM   17603 C  CA    . LYS   B  1  1180 ? 29.177  56.493  65.827  1.00 21.75 ? 1178 LYS   B CA    1 
ATOM   17604 C  C     . LYS   B  1  1180 ? 29.599  57.058  67.175  1.00 18.36 ? 1178 LYS   B C     1 
ATOM   17605 O  O     . LYS   B  1  1180 ? 30.086  56.323  68.039  1.00 20.43 ? 1178 LYS   B O     1 
ATOM   17606 C  CB    . LYS   B  1  1180 ? 30.229  56.797  64.763  1.00 23.38 ? 1178 LYS   B CB    1 
ATOM   17607 C  CG    . LYS   B  1  1180 ? 30.015  56.073  63.451  1.00 27.94 ? 1178 LYS   B CG    1 
ATOM   17608 C  CD    . LYS   B  1  1180 ? 31.143  56.375  62.461  1.00 30.55 ? 1178 LYS   B CD    1 
ATOM   17609 C  CE    . LYS   B  1  1180 ? 32.367  55.527  62.751  1.00 41.02 ? 1178 LYS   B CE    1 
ATOM   17610 N  NZ    . LYS   B  1  1180 ? 32.106  54.079  62.499  1.00 41.24 ? 1178 LYS   B NZ    1 
ATOM   17611 N  N     . ALA   B  1  1181 ? 29.418  58.368  67.373  1.00 20.21 ? 1179 ALA   B N     1 
ATOM   17612 C  CA    . ALA   B  1  1181 ? 29.785  58.958  68.655  1.00 18.84 ? 1179 ALA   B CA    1 
ATOM   17613 C  C     . ALA   B  1  1181 ? 28.947  58.371  69.785  1.00 18.00 ? 1179 ALA   B C     1 
ATOM   17614 O  O     . ALA   B  1  1181 ? 29.458  58.095  70.871  1.00 19.47 ? 1179 ALA   B O     1 
ATOM   17615 C  CB    . ALA   B  1  1181 ? 29.620  60.475  68.595  1.00 19.05 ? 1179 ALA   B CB    1 
ATOM   17616 N  N     . ILE   B  1  1182 ? 27.656  58.148  69.531  1.00 18.64 ? 1180 ILE   B N     1 
ATOM   17617 C  CA    . ILE   B  1  1182 ? 26.796  57.579  70.558  1.00 18.71 ? 1180 ILE   B CA    1 
ATOM   17618 C  C     . ILE   B  1  1182 ? 27.206  56.151  70.877  1.00 18.27 ? 1180 ILE   B C     1 
ATOM   17619 O  O     . ILE   B  1  1182 ? 27.233  55.744  72.043  1.00 19.59 ? 1180 ILE   B O     1 
ATOM   17620 C  CB    . ILE   B  1  1182 ? 25.327  57.679  70.132  1.00 18.35 ? 1180 ILE   B CB    1 
ATOM   17621 C  CG1   . ILE   B  1  1182 ? 24.877  59.136  70.219  1.00 19.43 ? 1180 ILE   B CG1   1 
ATOM   17622 C  CG2   . ILE   B  1  1182 ? 24.473  56.784  71.014  1.00 21.62 ? 1180 ILE   B CG2   1 
ATOM   17623 C  CD1   . ILE   B  1  1182 ? 23.499  59.397  69.624  1.00 19.27 ? 1180 ILE   B CD1   1 
ATOM   17624 N  N     . ALA   B  1  1183 ? 27.559  55.369  69.850  1.00 20.07 ? 1181 ALA   B N     1 
ATOM   17625 C  CA    . ALA   B  1  1183 ? 27.983  53.996  70.097  1.00 20.72 ? 1181 ALA   B CA    1 
ATOM   17626 C  C     . ALA   B  1  1183 ? 29.237  53.940  70.949  1.00 22.40 ? 1181 ALA   B C     1 
ATOM   17627 O  O     . ALA   B  1  1183 ? 29.476  52.943  71.638  1.00 25.72 ? 1181 ALA   B O     1 
ATOM   17628 C  CB    . ALA   B  1  1183 ? 28.213  53.256  68.780  1.00 22.55 ? 1181 ALA   B CB    1 
ATOM   17629 N  N     . ALA   B  1  1184 ? 30.041  54.994  70.926  1.00 20.61 ? 1182 ALA   B N     1 
ATOM   17630 C  CA    . ALA   B  1  1184 ? 31.267  55.045  71.707  1.00 22.18 ? 1182 ALA   B CA    1 
ATOM   17631 C  C     . ALA   B  1  1184 ? 31.053  55.560  73.122  1.00 21.18 ? 1182 ALA   B C     1 
ATOM   17632 O  O     . ALA   B  1  1184 ? 32.011  55.623  73.897  1.00 21.65 ? 1182 ALA   B O     1 
ATOM   17633 C  CB    . ALA   B  1  1184 ? 32.311  55.906  70.990  1.00 23.62 ? 1182 ALA   B CB    1 
ATOM   17634 N  N     . LEU   B  1  1185 ? 29.836  55.948  73.484  1.00 19.65 ? 1183 LEU   B N     1 
ATOM   17635 C  CA    . LEU   B  1  1185 ? 29.625  56.446  74.833  1.00 18.68 ? 1183 LEU   B CA    1 
ATOM   17636 C  C     . LEU   B  1  1185 ? 29.724  55.293  75.827  1.00 22.53 ? 1183 LEU   B C     1 
ATOM   17637 O  O     . LEU   B  1  1185 ? 29.317  54.167  75.523  1.00 24.07 ? 1183 LEU   B O     1 
ATOM   17638 C  CB    . LEU   B  1  1185 ? 28.247  57.093  74.963  1.00 18.26 ? 1183 LEU   B CB    1 
ATOM   17639 C  CG    . LEU   B  1  1185 ? 28.043  58.332  74.103  1.00 18.30 ? 1183 LEU   B CG    1 
ATOM   17640 C  CD1   . LEU   B  1  1185 ? 26.597  58.770  74.212  1.00 19.17 ? 1183 LEU   B CD1   1 
ATOM   17641 C  CD2   . LEU   B  1  1185 ? 28.975  59.442  74.546  1.00 19.82 ? 1183 LEU   B CD2   1 
ATOM   17642 N  N     . PRO   B  1  1186 ? 30.276  55.530  77.007  1.00 21.89 ? 1184 PRO   B N     1 
ATOM   17643 C  CA    . PRO   B  1  1186 ? 30.287  54.486  78.028  1.00 20.68 ? 1184 PRO   B CA    1 
ATOM   17644 C  C     . PRO   B  1  1186 ? 28.889  54.297  78.583  1.00 19.96 ? 1184 PRO   B C     1 
ATOM   17645 O  O     . PRO   B  1  1186 ? 28.001  55.133  78.414  1.00 24.32 ? 1184 PRO   B O     1 
ATOM   17646 C  CB    . PRO   B  1  1186 ? 31.206  55.069  79.103  1.00 26.01 ? 1184 PRO   B CB    1 
ATOM   17647 C  CG    . PRO   B  1  1186 ? 30.954  56.543  79.005  1.00 28.50 ? 1184 PRO   B CG    1 
ATOM   17648 C  CD    . PRO   B  1  1186 ? 30.777  56.816  77.525  1.00 24.82 ? 1184 PRO   B CD    1 
ATOM   17649 N  N     . GLY   B  1  1187 ? 28.717  53.182  79.279  1.00 20.48 ? 1185 GLY   B N     1 
ATOM   17650 C  CA    . GLY   B  1  1187 ? 27.480  52.912  79.966  1.00 20.86 ? 1185 GLY   B CA    1 
ATOM   17651 C  C     . GLY   B  1  1187 ? 26.470  52.221  79.075  1.00 21.58 ? 1185 GLY   B C     1 
ATOM   17652 O  O     . GLY   B  1  1187 ? 26.805  51.388  78.233  1.00 22.65 ? 1185 GLY   B O     1 
ATOM   17653 N  N     . PRO   B  1  1188 ? 25.203  52.543  79.265  1.00 19.10 ? 1186 PRO   B N     1 
ATOM   17654 C  CA    . PRO   B  1  1188 ? 24.148  51.821  78.545  1.00 19.51 ? 1186 PRO   B CA    1 
ATOM   17655 C  C     . PRO   B  1  1188 ? 24.223  52.050  77.047  1.00 18.81 ? 1186 PRO   B C     1 
ATOM   17656 O  O     . PRO   B  1  1188 ? 24.641  53.107  76.573  1.00 19.80 ? 1186 PRO   B O     1 
ATOM   17657 C  CB    . PRO   B  1  1188 ? 22.854  52.409  79.112  1.00 23.02 ? 1186 PRO   B CB    1 
ATOM   17658 C  CG    . PRO   B  1  1188 ? 23.244  53.697  79.754  1.00 25.03 ? 1186 PRO   B CG    1 
ATOM   17659 C  CD    . PRO   B  1  1188 ? 24.689  53.595  80.153  1.00 22.00 ? 1186 PRO   B CD    1 
ATOM   17660 N  N     . LEU   B  1  1189 ? 23.793  51.041  76.302  1.00 17.54 ? 1187 LEU   B N     1 
ATOM   17661 C  CA    . LEU   B  1  1189 ? 23.626  51.191  74.862  1.00 17.24 ? 1187 LEU   B CA    1 
ATOM   17662 C  C     . LEU   B  1  1189 ? 22.379  52.010  74.600  1.00 17.53 ? 1187 LEU   B C     1 
ATOM   17663 O  O     . LEU   B  1  1189 ? 21.281  51.633  75.029  1.00 21.04 ? 1187 LEU   B O     1 
ATOM   17664 C  CB    . LEU   B  1  1189 ? 23.470  49.826  74.211  1.00 18.23 ? 1187 LEU   B CB    1 
ATOM   17665 C  CG    . LEU   B  1  1189 ? 24.737  49.028  73.958  1.00 20.25 ? 1187 LEU   B CG    1 
ATOM   17666 C  CD1   . LEU   B  1  1189 ? 25.275  48.449  75.252  1.00 24.19 ? 1187 LEU   B CD1   1 
ATOM   17667 C  CD2   . LEU   B  1  1189 ? 24.420  47.939  72.953  1.00 21.44 ? 1187 LEU   B CD2   1 
ATOM   17668 N  N     . LEU   B  1  1190 ? 22.529  53.134  73.920  1.00 16.47 ? 1188 LEU   B N     1 
ATOM   17669 C  CA    . LEU   B  1  1190 ? 21.402  54.035  73.758  1.00 18.39 ? 1188 LEU   B CA    1 
ATOM   17670 C  C     . LEU   B  1  1190 ? 20.551  53.645  72.564  1.00 19.07 ? 1188 LEU   B C     1 
ATOM   17671 O  O     . LEU   B  1  1190 ? 21.058  53.347  71.478  1.00 17.34 ? 1188 LEU   B O     1 
ATOM   17672 C  CB    . LEU   B  1  1190 ? 21.865  55.476  73.582  1.00 17.88 ? 1188 LEU   B CB    1 
ATOM   17673 C  CG    . LEU   B  1  1190 ? 22.699  56.050  74.714  1.00 16.40 ? 1188 LEU   B CG    1 
ATOM   17674 C  CD1   . LEU   B  1  1190 ? 22.803  57.532  74.472  1.00 17.57 ? 1188 LEU   B CD1   1 
ATOM   17675 C  CD2   . LEU   B  1  1190 ? 22.058  55.757  76.069  1.00 19.07 ? 1188 LEU   B CD2   1 
ATOM   17676 N  N     . LEU   B  1  1191 ? 19.244  53.670  72.773  1.00 17.87 ? 1189 LEU   B N     1 
ATOM   17677 C  CA    . LEU   B  1  1191 ? 18.286  53.534  71.687  1.00 15.86 ? 1189 LEU   B CA    1 
ATOM   17678 C  C     . LEU   B  1  1191 ? 18.205  54.874  70.958  1.00 15.45 ? 1189 LEU   B C     1 
ATOM   17679 O  O     . LEU   B  1  1191 ? 17.680  55.857  71.492  1.00 18.99 ? 1189 LEU   B O     1 
ATOM   17680 C  CB    . LEU   B  1  1191 ? 16.930  53.102  72.239  1.00 16.54 ? 1189 LEU   B CB    1 
ATOM   17681 C  CG    . LEU   B  1  1191 ? 15.982  52.483  71.207  1.00 16.42 ? 1189 LEU   B CG    1 
ATOM   17682 C  CD1   . LEU   B  1  1191 ? 14.844  51.818  71.960  1.00 18.11 ? 1189 LEU   B CD1   1 
ATOM   17683 C  CD2   . LEU   B  1  1191 ? 15.439  53.513  70.216  1.00 16.61 ? 1189 LEU   B CD2   1 
ATOM   17684 N  N     . VAL   B  1  1192 ? 18.752  54.912  69.748  1.00 17.01 ? 1190 VAL   B N     1 
ATOM   17685 C  CA    . VAL   B  1  1192 ? 18.897  56.132  68.963  1.00 17.23 ? 1190 VAL   B CA    1 
ATOM   17686 C  C     . VAL   B  1  1192 ? 17.778  56.212  67.940  1.00 16.85 ? 1190 VAL   B C     1 
ATOM   17687 O  O     . VAL   B  1  1192 ? 17.500  55.238  67.225  1.00 19.32 ? 1190 VAL   B O     1 
ATOM   17688 C  CB    . VAL   B  1  1192 ? 20.257  56.157  68.245  1.00 16.55 ? 1190 VAL   B CB    1 
ATOM   17689 C  CG1   . VAL   B  1  1192 ? 20.392  57.420  67.409  1.00 18.42 ? 1190 VAL   B CG1   1 
ATOM   17690 C  CG2   . VAL   B  1  1192 ? 21.400  56.040  69.250  1.00 17.73 ? 1190 VAL   B CG2   1 
ATOM   17691 N  N     . GLN   B  1  1193 ? 17.183  57.388  67.824  1.00 16.50 ? 1191 GLN   B N     1 
ATOM   17692 C  CA    . GLN   B  1  1193 ? 16.232  57.679  66.767  1.00 15.88 ? 1191 GLN   B CA    1 
ATOM   17693 C  C     . GLN   B  1  1193 ? 16.736  58.884  66.005  1.00 17.67 ? 1191 GLN   B C     1 
ATOM   17694 O  O     . GLN   B  1  1193 ? 17.053  59.914  66.605  1.00 18.79 ? 1191 GLN   B O     1 
ATOM   17695 C  CB    . GLN   B  1  1193 ? 14.873  58.023  67.345  1.00 17.74 ? 1191 GLN   B CB    1 
ATOM   17696 C  CG    . GLN   B  1  1193 ? 14.337  56.962  68.250  1.00 18.24 ? 1191 GLN   B CG    1 
ATOM   17697 C  CD    . GLN   B  1  1193 ? 12.871  57.160  68.485  1.00 19.27 ? 1191 GLN   B CD    1 
ATOM   17698 O  OE1   . GLN   B  1  1193 ? 12.065  57.113  67.557  1.00 19.42 ? 1191 GLN   B OE1   1 
ATOM   17699 N  NE2   . GLN   B  1  1193 ? 12.515  57.427  69.728  1.00 17.95 ? 1191 GLN   B NE2   1 
ATOM   17700 N  N     . ALA   B  1  1194 ? 16.804  58.757  64.690  1.00 17.50 ? 1192 ALA   B N     1 
ATOM   17701 C  CA    . ALA   B  1  1194 ? 17.316  59.825  63.856  1.00 18.22 ? 1192 ALA   B CA    1 
ATOM   17702 C  C     . ALA   B  1  1194 ? 16.287  60.199  62.804  1.00 19.59 ? 1192 ALA   B C     1 
ATOM   17703 O  O     . ALA   B  1  1194 ? 15.474  59.374  62.369  1.00 22.15 ? 1192 ALA   B O     1 
ATOM   17704 C  CB    . ALA   B  1  1194 ? 18.606  59.398  63.170  1.00 19.29 ? 1192 ALA   B CB    1 
ATOM   17705 N  N     . ALA   B  1  1195 ? 16.334  61.460  62.397  1.00 18.82 ? 1193 ALA   B N     1 
ATOM   17706 C  CA    . ALA   B  1  1195 ? 15.453  61.966  61.363  1.00 21.26 ? 1193 ALA   B CA    1 
ATOM   17707 C  C     . ALA   B  1  1195 ? 16.151  63.152  60.727  1.00 22.23 ? 1193 ALA   B C     1 
ATOM   17708 O  O     . ALA   B  1  1195 ? 16.933  63.844  61.376  1.00 21.70 ? 1193 ALA   B O     1 
ATOM   17709 C  CB    . ALA   B  1  1195 ? 14.102  62.413  61.942  1.00 20.93 ? 1193 ALA   B CB    1 
ATOM   17710 N  N     . SER   B  1  1196 ? 15.889  63.358  59.445  1.00 22.23 ? 1194 SER   B N     1 
ATOM   17711 C  CA    . SER   B  1  1196 ? 16.327  64.588  58.816  1.00 21.79 ? 1194 SER   B CA    1 
ATOM   17712 C  C     . SER   B  1  1196 ? 15.382  65.719  59.197  1.00 23.62 ? 1194 SER   B C     1 
ATOM   17713 O  O     . SER   B  1  1196 ? 14.265  65.499  59.676  1.00 24.14 ? 1194 SER   B O     1 
ATOM   17714 C  CB    . SER   B  1  1196 ? 16.294  64.432  57.301  1.00 25.22 ? 1194 SER   B CB    1 
ATOM   17715 O  OG    . SER   B  1  1196 ? 14.961  64.270  56.877  1.00 25.89 ? 1194 SER   B OG    1 
ATOM   17716 N  N     . SER   B  1  1197 ? 15.841  66.948  58.970  1.00 22.36 ? 1195 SER   B N     1 
ATOM   17717 C  CA    . SER   B  1  1197 ? 14.988  68.108  59.198  1.00 24.07 ? 1195 SER   B CA    1 
ATOM   17718 C  C     . SER   B  1  1197 ? 13.722  68.028  58.360  1.00 24.65 ? 1195 SER   B C     1 
ATOM   17719 O  O     . SER   B  1  1197 ? 12.629  68.356  58.836  1.00 24.52 ? 1195 SER   B O     1 
ATOM   17720 C  CB    . SER   B  1  1197 ? 15.754  69.384  58.867  1.00 25.21 ? 1195 SER   B CB    1 
ATOM   17721 O  OG    . SER   B  1  1197 ? 16.909  69.490  59.671  1.00 24.75 ? 1195 SER   B OG    1 
ATOM   17722 N  N     . GLY   B  1  1198 ? 13.849  67.594  57.107  1.00 24.04 ? 1196 GLY   B N     1 
ATOM   17723 C  CA    . GLY   B  1  1198 ? 12.673  67.466  56.265  1.00 29.20 ? 1196 GLY   B CA    1 
ATOM   17724 C  C     . GLY   B  1  1198 ? 11.708  66.418  56.781  1.00 29.15 ? 1196 GLY   B C     1 
ATOM   17725 O  O     . GLY   B  1  1198 ? 10.490  66.597  56.722  1.00 28.21 ? 1196 GLY   B O     1 
ATOM   17726 N  N     . GLU   B  1  1199 ? 12.243  65.311  57.296  1.00 26.32 ? 1197 GLU   B N     1 
ATOM   17727 C  CA    . GLU   B  1  1199 ? 11.401  64.263  57.854  1.00 29.04 ? 1197 GLU   B CA    1 
ATOM   17728 C  C     . GLU   B  1  1199 ? 10.636  64.774  59.068  1.00 27.05 ? 1197 GLU   B C     1 
ATOM   17729 O  O     . GLU   B  1  1199 ? 9.439   64.505  59.219  1.00 27.87 ? 1197 GLU   B O     1 
ATOM   17730 C  CB    . GLU   B  1  1199 ? 12.294  63.078  58.218  1.00 30.81 ? 1197 GLU   B CB    1 
ATOM   17731 C  CG    . GLU   B  1  1199 ? 11.583  61.818  58.645  1.00 35.98 ? 1197 GLU   B CG    1 
ATOM   17732 C  CD    . GLU   B  1  1199 ? 12.567  60.696  58.927  1.00 36.94 ? 1197 GLU   B CD    1 
ATOM   17733 O  OE1   . GLU   B  1  1199 ? 13.774  60.861  58.616  1.00 37.41 ? 1197 GLU   B OE1   1 
ATOM   17734 O  OE2   . GLU   B  1  1199 ? 12.140  59.654  59.462  1.00 44.31 ? 1197 GLU   B OE2   1 
ATOM   17735 N  N     . ILE   B  1  1200 ? 11.308  65.539  59.932  1.00 23.73 ? 1198 ILE   B N     1 
ATOM   17736 C  CA    . ILE   B  1  1200 ? 10.641  66.124  61.092  1.00 22.81 ? 1198 ILE   B CA    1 
ATOM   17737 C  C     . ILE   B  1  1200 ? 9.485   67.016  60.655  1.00 28.08 ? 1198 ILE   B C     1 
ATOM   17738 O  O     . ILE   B  1  1200 ? 8.403   66.999  61.258  1.00 27.21 ? 1198 ILE   B O     1 
ATOM   17739 C  CB    . ILE   B  1  1200 ? 11.657  66.877  61.970  1.00 22.08 ? 1198 ILE   B CB    1 
ATOM   17740 C  CG1   . ILE   B  1  1200 ? 12.656  65.903  62.595  1.00 24.20 ? 1198 ILE   B CG1   1 
ATOM   17741 C  CG2   . ILE   B  1  1200 ? 10.938  67.678  63.045  1.00 21.84 ? 1198 ILE   B CG2   1 
ATOM   17742 C  CD1   . ILE   B  1  1200 ? 13.790  66.609  63.330  1.00 23.10 ? 1198 ILE   B CD1   1 
ATOM   17743 N  N     . ALA   B  1  1201 ? 9.689   67.804  59.594  1.00 27.87 ? 1199 ALA   B N     1 
ATOM   17744 C  CA    . ALA   B  1  1201 ? 8.637   68.706  59.135  1.00 30.95 ? 1199 ALA   B CA    1 
ATOM   17745 C  C     . ALA   B  1  1201 ? 7.487   67.956  58.475  1.00 29.58 ? 1199 ALA   B C     1 
ATOM   17746 O  O     . ALA   B  1  1201 ? 6.333   68.387  58.580  1.00 34.48 ? 1199 ALA   B O     1 
ATOM   17747 C  CB    . ALA   B  1  1201 ? 9.207   69.734  58.160  1.00 29.49 ? 1199 ALA   B CB    1 
ATOM   17748 N  N     . ARG   B  1  1202 ? 7.776   66.844  57.798  1.00 29.69 ? 1200 ARG   B N     1 
ATOM   17749 C  CA    . ARG   B  1  1202 ? 6.772   66.132  57.013  1.00 31.25 ? 1200 ARG   B CA    1 
ATOM   17750 C  C     . ARG   B  1  1202 ? 6.044   65.055  57.802  1.00 33.84 ? 1200 ARG   B C     1 
ATOM   17751 O  O     . ARG   B  1  1202 ? 4.862   64.804  57.540  1.00 35.06 ? 1200 ARG   B O     1 
ATOM   17752 C  CB    . ARG   B  1  1202 ? 7.430   65.461  55.805  1.00 33.35 ? 1200 ARG   B CB    1 
ATOM   17753 C  CG    . ARG   B  1  1202 ? 8.047   66.423  54.803  1.00 41.52 ? 1200 ARG   B CG    1 
ATOM   17754 C  CD    . ARG   B  1  1202 ? 8.558   65.673  53.585  1.00 43.01 ? 1200 ARG   B CD    1 
ATOM   17755 N  NE    . ARG   B  1  1202 ? 9.305   64.481  53.969  1.00 40.41 ? 1200 ARG   B NE    1 
ATOM   17756 C  CZ    . ARG   B  1  1202 ? 10.628  64.404  53.999  1.00 42.04 ? 1200 ARG   B CZ    1 
ATOM   17757 N  NH1   . ARG   B  1  1202 ? 11.388  65.427  53.637  1.00 40.77 ? 1200 ARG   B NH1   1 
ATOM   17758 N  NH2   . ARG   B  1  1202 ? 11.203  63.271  54.396  1.00 40.08 ? 1200 ARG   B NH2   1 
ATOM   17759 N  N     . ASN   B  1  1203 ? 6.712   64.420  58.756  1.00 29.66 ? 1201 ASN   B N     1 
ATOM   17760 C  CA    . ASN   B  1  1203 ? 6.207   63.201  59.387  1.00 28.75 ? 1201 ASN   B CA    1 
ATOM   17761 C  C     . ASN   B  1  1203 ? 5.971   63.443  60.866  1.00 29.78 ? 1201 ASN   B C     1 
ATOM   17762 O  O     . ASN   B  1  1203 ? 6.947   63.595  61.628  1.00 26.56 ? 1201 ASN   B O     1 
ATOM   17763 C  CB    . ASN   B  1  1203 ? 7.207   62.062  59.185  1.00 30.91 ? 1201 ASN   B CB    1 
ATOM   17764 C  CG    . ASN   B  1  1203 ? 6.748   60.749  59.806  1.00 32.35 ? 1201 ASN   B CG    1 
ATOM   17765 O  OD1   . ASN   B  1  1203 ? 5.612   60.621  60.271  1.00 34.44 ? 1201 ASN   B OD1   1 
ATOM   17766 N  ND2   . ASN   B  1  1203 ? 7.635   59.759  59.805  1.00 35.01 ? 1201 ASN   B ND2   1 
ATOM   17767 N  N     . PRO   B  1  1204 ? 4.715   63.467  61.318  1.00 30.33 ? 1202 PRO   B N     1 
ATOM   17768 C  CA    . PRO   B  1  1204 ? 4.448   63.634  62.755  1.00 31.10 ? 1202 PRO   B CA    1 
ATOM   17769 C  C     . PRO   B  1  1204 ? 5.073   62.553  63.612  1.00 29.41 ? 1202 PRO   B C     1 
ATOM   17770 O  O     . PRO   B  1  1204 ? 5.304   62.782  64.804  1.00 29.84 ? 1202 PRO   B O     1 
ATOM   17771 C  CB    . PRO   B  1  1204 ? 2.915   63.582  62.839  1.00 33.39 ? 1202 PRO   B CB    1 
ATOM   17772 C  CG    . PRO   B  1  1204 ? 2.435   63.875  61.463  1.00 34.41 ? 1202 PRO   B CG    1 
ATOM   17773 C  CD    . PRO   B  1  1204 ? 3.475   63.337  60.532  1.00 31.69 ? 1202 PRO   B CD    1 
ATOM   17774 N  N     . ASP   B  1  1205 ? 5.344   61.381  63.049  1.00 28.60 ? 1203 ASP   B N     1 
ATOM   17775 C  CA    . ASP   B  1  1205 ? 5.928   60.275  63.789  1.00 29.87 ? 1203 ASP   B CA    1 
ATOM   17776 C  C     . ASP   B  1  1205 ? 7.398   60.073  63.439  1.00 30.32 ? 1203 ASP   B C     1 
ATOM   17777 O  O     . ASP   B  1  1205 ? 7.920   58.960  63.539  1.00 27.89 ? 1203 ASP   B O     1 
ATOM   17778 C  CB    . ASP   B  1  1205 ? 5.122   58.994  63.585  1.00 33.53 ? 1203 ASP   B CB    1 
ATOM   17779 C  CG    . ASP   B  1  1205 ? 3.739   59.065  64.222  1.00 35.63 ? 1203 ASP   B CG    1 
ATOM   17780 O  OD1   . ASP   B  1  1205 ? 3.514   59.939  65.091  1.00 33.14 ? 1203 ASP   B OD1   1 
ATOM   17781 O  OD2   . ASP   B  1  1205 ? 2.877   58.238  63.857  1.00 40.71 ? 1203 ASP   B OD2   1 
ATOM   17782 N  N     . ALA   B  1  1206 ? 8.073   61.147  63.018  1.00 25.45 ? 1204 ALA   B N     1 
ATOM   17783 C  CA    . ALA   B  1  1206 ? 9.501   61.060  62.737  1.00 24.79 ? 1204 ALA   B CA    1 
ATOM   17784 C  C     . ALA   B  1  1206 ? 10.257  60.474  63.921  1.00 24.05 ? 1204 ALA   B C     1 
ATOM   17785 O  O     . ALA   B  1  1206 ? 11.158  59.647  63.746  1.00 26.30 ? 1204 ALA   B O     1 
ATOM   17786 C  CB    . ALA   B  1  1206 ? 10.043  62.441  62.368  1.00 24.86 ? 1204 ALA   B CB    1 
ATOM   17787 N  N     . TYR   B  1  1207 ? 9.903   60.887  65.133  1.00 21.11 ? 1205 TYR   B N     1 
ATOM   17788 C  CA    . TYR   B  1  1207 ? 10.410  60.268  66.347  1.00 21.03 ? 1205 TYR   B CA    1 
ATOM   17789 C  C     . TYR   B  1  1207 ? 9.273   59.504  67.003  1.00 20.84 ? 1205 TYR   B C     1 
ATOM   17790 O  O     . TYR   B  1  1207 ? 8.174   60.039  67.164  1.00 27.17 ? 1205 TYR   B O     1 
ATOM   17791 C  CB    . TYR   B  1  1207 ? 10.954  61.309  67.324  1.00 20.77 ? 1205 TYR   B CB    1 
ATOM   17792 C  CG    . TYR   B  1  1207 ? 12.127  62.074  66.778  1.00 18.45 ? 1205 TYR   B CG    1 
ATOM   17793 C  CD1   . TYR   B  1  1207 ? 13.302  61.427  66.447  1.00 18.63 ? 1205 TYR   B CD1   1 
ATOM   17794 C  CD2   . TYR   B  1  1207 ? 12.058  63.451  66.604  1.00 19.17 ? 1205 TYR   B CD2   1 
ATOM   17795 C  CE1   . TYR   B  1  1207 ? 14.376  62.123  65.946  1.00 18.42 ? 1205 TYR   B CE1   1 
ATOM   17796 C  CE2   . TYR   B  1  1207 ? 13.134  64.157  66.102  1.00 21.19 ? 1205 TYR   B CE2   1 
ATOM   17797 C  CZ    . TYR   B  1  1207 ? 14.285  63.489  65.780  1.00 20.84 ? 1205 TYR   B CZ    1 
ATOM   17798 O  OH    . TYR   B  1  1207 ? 15.350  64.204  65.287  1.00 19.80 ? 1205 TYR   B OH    1 
ATOM   17799 N  N     . CYS   B  1  1208 ? 9.542   58.263  67.369  1.00 17.02 ? 1206 CYS   B N     1 
ATOM   17800 C  CA    . CYS   B  1  1208 ? 8.522   57.363  67.872  1.00 17.97 ? 1206 CYS   B CA    1 
ATOM   17801 C  C     . CYS   B  1  1208 ? 8.533   57.420  69.392  1.00 15.53 ? 1206 CYS   B C     1 
ATOM   17802 O  O     . CYS   B  1  1208 ? 9.565   57.183  70.023  1.00 17.01 ? 1206 CYS   B O     1 
ATOM   17803 C  CB    . CYS   B  1  1208 ? 8.814   55.947  67.385  1.00 19.97 ? 1206 CYS   B CB    1 
ATOM   17804 S  SG    . CYS   B  1  1208 ? 7.597   54.756  67.961  1.00 22.36 ? 1206 CYS   B SG    1 
ATOM   17805 N  N     . LEU   B  1  1209 ? 7.372   57.718  69.982  1.00 15.63 ? 1207 LEU   B N     1 
ATOM   17806 C  CA    . LEU   B  1  1209 ? 7.298   57.828  71.433  1.00 15.93 ? 1207 LEU   B CA    1 
ATOM   17807 C  C     . LEU   B  1  1209 ? 7.341   56.473  72.116  1.00 15.43 ? 1207 LEU   B C     1 
ATOM   17808 O  O     . LEU   B  1  1209 ? 7.573   56.422  73.325  1.00 15.71 ? 1207 LEU   B O     1 
ATOM   17809 C  CB    . LEU   B  1  1209 ? 6.046   58.584  71.851  1.00 15.47 ? 1207 LEU   B CB    1 
ATOM   17810 C  CG    . LEU   B  1  1209 ? 5.849   59.953  71.215  1.00 17.62 ? 1207 LEU   B CG    1 
ATOM   17811 C  CD1   . LEU   B  1  1209 ? 4.611   60.590  71.823  1.00 19.99 ? 1207 LEU   B CD1   1 
ATOM   17812 C  CD2   . LEU   B  1  1209 ? 7.068   60.827  71.428  1.00 19.85 ? 1207 LEU   B CD2   1 
ATOM   17813 N  N     . ASN   B  1  1210 ? 7.132   55.383  71.372  1.00 16.06 ? 1208 ASN   B N     1 
ATOM   17814 C  CA    . ASN   B  1  1210 ? 7.196   54.058  71.972  1.00 17.86 ? 1208 ASN   B CA    1 
ATOM   17815 C  C     . ASN   B  1  1210 ? 8.558   53.820  72.601  1.00 15.65 ? 1208 ASN   B C     1 
ATOM   17816 O  O     . ASN   B  1  1210 ? 8.662   53.118  73.609  1.00 18.15 ? 1208 ASN   B O     1 
ATOM   17817 C  CB    . ASN   B  1  1210 ? 6.944   52.973  70.913  1.00 21.02 ? 1208 ASN   B CB    1 
ATOM   17818 C  CG    . ASN   B  1  1210 ? 5.547   53.056  70.287  1.00 21.01 ? 1208 ASN   B CG    1 
ATOM   17819 O  OD1   . ASN   B  1  1210 ? 4.832   54.029  70.471  1.00 25.66 ? 1208 ASN   B OD1   1 
ATOM   17820 N  ND2   . ASN   B  1  1210 ? 5.194   52.049  69.491  1.00 26.33 ? 1208 ASN   B ND2   1 
ATOM   17821 N  N     . TRP   B  1  1211 ? 9.613   54.396  72.024  1.00 15.74 ? 1209 TRP   B N     1 
ATOM   17822 C  CA    . TRP   B  1  1211 ? 10.968  54.123  72.482  1.00 15.22 ? 1209 TRP   B CA    1 
ATOM   17823 C  C     . TRP   B  1  1211 ? 11.431  55.092  73.552  1.00 17.06 ? 1209 TRP   B C     1 
ATOM   17824 O  O     . TRP   B  1  1211 ? 12.533  54.920  74.086  1.00 18.17 ? 1209 TRP   B O     1 
ATOM   17825 C  CB    . TRP   B  1  1211 ? 11.951  54.131  71.303  1.00 16.95 ? 1209 TRP   B CB    1 
ATOM   17826 C  CG    . TRP   B  1  1211 ? 11.378  53.463  70.091  1.00 18.12 ? 1209 TRP   B CG    1 
ATOM   17827 C  CD1   . TRP   B  1  1211 ? 11.346  53.959  68.825  1.00 19.92 ? 1209 TRP   B CD1   1 
ATOM   17828 C  CD2   . TRP   B  1  1211 ? 10.739  52.186  70.040  1.00 16.93 ? 1209 TRP   B CD2   1 
ATOM   17829 N  NE1   . TRP   B  1  1211 ? 10.725  53.067  67.984  1.00 21.48 ? 1209 TRP   B NE1   1 
ATOM   17830 C  CE2   . TRP   B  1  1211 ? 10.345  51.968  68.711  1.00 18.93 ? 1209 TRP   B CE2   1 
ATOM   17831 C  CE3   . TRP   B  1  1211 ? 10.460  51.201  70.997  1.00 17.55 ? 1209 TRP   B CE3   1 
ATOM   17832 C  CZ2   . TRP   B  1  1211 ? 9.668   50.815  68.311  1.00 19.78 ? 1209 TRP   B CZ2   1 
ATOM   17833 C  CZ3   . TRP   B  1  1211 ? 9.798   50.054  70.598  1.00 19.33 ? 1209 TRP   B CZ3   1 
ATOM   17834 C  CH2   . TRP   B  1  1211 ? 9.409   49.871  69.269  1.00 18.38 ? 1209 TRP   B CH2   1 
ATOM   17835 N  N     . LEU   B  1  1212 ? 10.624  56.094  73.866  1.00 16.08 ? 1210 LEU   B N     1 
ATOM   17836 C  CA    . LEU   B  1  1212 ? 10.995  57.126  74.813  1.00 14.09 ? 1210 LEU   B CA    1 
ATOM   17837 C  C     . LEU   B  1  1212 ? 10.388  56.901  76.180  1.00 15.46 ? 1210 LEU   B C     1 
ATOM   17838 O  O     . LEU   B  1  1212 ? 10.557  57.740  77.066  1.00 14.91 ? 1210 LEU   B O     1 
ATOM   17839 C  CB    . LEU   B  1  1212 ? 10.609  58.491  74.263  1.00 14.27 ? 1210 LEU   B CB    1 
ATOM   17840 C  CG    . LEU   B  1  1212 ? 11.540  58.917  73.124  1.00 13.48 ? 1210 LEU   B CG    1 
ATOM   17841 C  CD1   . LEU   B  1  1212 ? 10.933  60.048  72.349  1.00 17.28 ? 1210 LEU   B CD1   1 
ATOM   17842 C  CD2   . LEU   B  1  1212 ? 12.892  59.316  73.657  1.00 16.48 ? 1210 LEU   B CD2   1 
ATOM   17843 N  N     . VAL   B  1  1213 ? 9.700   55.786  76.366  1.00 15.14 ? 1211 VAL   B N     1 
ATOM   17844 C  CA    . VAL   B  1  1213 ? 9.239   55.366  77.676  1.00 14.55 ? 1211 VAL   B CA    1 
ATOM   17845 C  C     . VAL   B  1  1213 ? 9.972   54.086  78.025  1.00 14.48 ? 1211 VAL   B C     1 
ATOM   17846 O  O     . VAL   B  1  1213 ? 10.473  53.370  77.152  1.00 16.48 ? 1211 VAL   B O     1 
ATOM   17847 C  CB    . VAL   B  1  1213 ? 7.714   55.151  77.709  1.00 15.00 ? 1211 VAL   B CB    1 
ATOM   17848 C  CG1   . VAL   B  1  1213 ? 7.012   56.492  77.547  1.00 17.90 ? 1211 VAL   B CG1   1 
ATOM   17849 C  CG2   . VAL   B  1  1213 ? 7.291   54.167  76.614  1.00 16.38 ? 1211 VAL   B CG2   1 
ATOM   17850 N  N     . GLU   B  1  1214 ? 10.071  53.819  79.326  1.00 15.54 ? 1212 GLU   B N     1 
ATOM   17851 C  CA    . GLU   B  1  1214 ? 10.614  52.572  79.842  1.00 16.68 ? 1212 GLU   B CA    1 
ATOM   17852 C  C     . GLU   B  1  1214 ? 9.479   51.690  80.338  1.00 14.06 ? 1212 GLU   B C     1 
ATOM   17853 O  O     . GLU   B  1  1214 ? 8.639   52.129  81.119  1.00 15.77 ? 1212 GLU   B O     1 
ATOM   17854 C  CB    . GLU   B  1  1214 ? 11.594  52.821  80.994  1.00 17.67 ? 1212 GLU   B CB    1 
ATOM   17855 C  CG    . GLU   B  1  1214 ? 12.271  51.528  81.467  1.00 23.70 ? 1212 GLU   B CG    1 
ATOM   17856 C  CD    . GLU   B  1  1214 ? 13.113  51.671  82.730  1.00 25.54 ? 1212 GLU   B CD    1 
ATOM   17857 O  OE1   . GLU   B  1  1214 ? 13.548  52.795  83.052  1.00 24.37 ? 1212 GLU   B OE1   1 
ATOM   17858 O  OE2   . GLU   B  1  1214 ? 13.318  50.640  83.414  1.00 26.69 ? 1212 GLU   B OE2   1 
ATOM   17859 N  N     . GLU   B  1  1215 ? 9.482   50.444  79.900  1.00 14.61 ? 1213 GLU   B N     1 
ATOM   17860 C  CA    . GLU   B  1  1215 ? 8.541   49.460  80.401  1.00 14.57 ? 1213 GLU   B CA    1 
ATOM   17861 C  C     . GLU   B  1  1215 ? 9.050   48.867  81.700  1.00 13.32 ? 1213 GLU   B C     1 
ATOM   17862 O  O     . GLU   B  1  1215 ? 10.233  48.536  81.824  1.00 14.92 ? 1213 GLU   B O     1 
ATOM   17863 C  CB    . GLU   B  1  1215 ? 8.442   48.323  79.398  1.00 16.12 ? 1213 GLU   B CB    1 
ATOM   17864 C  CG    . GLU   B  1  1215 ? 7.980   48.729  78.018  1.00 17.63 ? 1213 GLU   B CG    1 
ATOM   17865 C  CD    . GLU   B  1  1215 ? 8.191   47.620  77.037  1.00 14.88 ? 1213 GLU   B CD    1 
ATOM   17866 O  OE1   . GLU   B  1  1215 ? 9.318   47.512  76.535  1.00 15.20 ? 1213 GLU   B OE1   1 
ATOM   17867 O  OE2   . GLU   B  1  1215 ? 7.242   46.862  76.783  1.00 16.20 ? 1213 GLU   B OE2   1 
ATOM   17868 N  N     . VAL   B  1  1216 ? 8.153   48.729  82.672  1.00 14.71 ? 1214 VAL   B N     1 
ATOM   17869 C  CA    . VAL   B  1  1216 ? 8.459   48.031  83.907  1.00 15.37 ? 1214 VAL   B CA    1 
ATOM   17870 C  C     . VAL   B  1  1216 ? 7.380   46.994  84.141  1.00 14.08 ? 1214 VAL   B C     1 
ATOM   17871 O  O     . VAL   B  1  1216 ? 6.183   47.296  84.061  1.00 15.21 ? 1214 VAL   B O     1 
ATOM   17872 C  CB    . VAL   B  1  1216 ? 8.566   48.992  85.099  1.00 16.16 ? 1214 VAL   B CB    1 
ATOM   17873 C  CG1   . VAL   B  1  1216 ? 8.762   48.196  86.398  1.00 16.78 ? 1214 VAL   B CG1   1 
ATOM   17874 C  CG2   . VAL   B  1  1216 ? 9.713   49.975  84.879  1.00 18.88 ? 1214 VAL   B CG2   1 
ATOM   17875 N  N     . SER   B  1  1217 ? 7.804   45.762  84.381  1.00 13.48 ? 1215 SER   B N     1 
ATOM   17876 C  CA    . SER   B  1  1217 ? 6.919   44.669  84.740  1.00 13.86 ? 1215 SER   B CA    1 
ATOM   17877 C  C     . SER   B  1  1217 ? 7.092   44.390  86.219  1.00 13.12 ? 1215 SER   B C     1 
ATOM   17878 O  O     . SER   B  1  1217 ? 8.218   44.360  86.710  1.00 14.75 ? 1215 SER   B O     1 
ATOM   17879 C  CB    . SER   B  1  1217 ? 7.327   43.434  83.945  1.00 15.96 ? 1215 SER   B CB    1 
ATOM   17880 O  OG    . SER   B  1  1217 ? 6.858   42.240  84.530  1.00 17.75 ? 1215 SER   B OG    1 
ATOM   17881 N  N     . ALA   B  1  1218 ? 5.993   44.196  86.928  1.00 13.94 ? 1216 ALA   B N     1 
ATOM   17882 C  CA    . ALA   B  1  1218 ? 6.059   43.827  88.333  1.00 16.02 ? 1216 ALA   B CA    1 
ATOM   17883 C  C     . ALA   B  1  1218 ? 5.141   42.640  88.535  1.00 15.26 ? 1216 ALA   B C     1 
ATOM   17884 O  O     . ALA   B  1  1218 ? 3.968   42.693  88.156  1.00 16.29 ? 1216 ALA   B O     1 
ATOM   17885 C  CB    . ALA   B  1  1218 ? 5.640   44.987  89.239  1.00 17.41 ? 1216 ALA   B CB    1 
ATOM   17886 N  N     . SER   B  1  1219 ? 5.660   41.571  89.121  1.00 14.32 ? 1217 SER   B N     1 
ATOM   17887 C  CA    . SER   B  1  1219 ? 4.881   40.376  89.394  1.00 14.47 ? 1217 SER   B CA    1 
ATOM   17888 C  C     . SER   B  1  1219 ? 4.802   40.206  90.897  1.00 14.28 ? 1217 SER   B C     1 
ATOM   17889 O  O     . SER   B  1  1219 ? 5.826   40.022  91.561  1.00 14.81 ? 1217 SER   B O     1 
ATOM   17890 C  CB    . SER   B  1  1219 ? 5.525   39.156  88.755  1.00 15.99 ? 1217 SER   B CB    1 
ATOM   17891 O  OG    . SER   B  1  1219 ? 4.757   37.994  89.019  1.00 17.02 ? 1217 SER   B OG    1 
ATOM   17892 N  N     . ILE   B  1  1220 ? 3.593   40.279  91.429  1.00 14.94 ? 1218 ILE   B N     1 
ATOM   17893 C  CA    . ILE   B  1  1220 ? 3.362   40.216  92.863  1.00 15.04 ? 1218 ILE   B CA    1 
ATOM   17894 C  C     . ILE   B  1  1220 ? 2.667   38.900  93.154  1.00 16.54 ? 1218 ILE   B C     1 
ATOM   17895 O  O     . ILE   B  1  1220 ? 1.585   38.637  92.623  1.00 16.32 ? 1218 ILE   B O     1 
ATOM   17896 C  CB    . ILE   B  1  1220 ? 2.495   41.391  93.324  1.00 18.60 ? 1218 ILE   B CB    1 
ATOM   17897 C  CG1   . ILE   B  1  1220 ? 3.127   42.709  92.883  1.00 21.75 ? 1218 ILE   B CG1   1 
ATOM   17898 C  CG2   . ILE   B  1  1220 ? 2.283   41.325  94.839  1.00 20.37 ? 1218 ILE   B CG2   1 
ATOM   17899 C  CD1   . ILE   B  1  1220 ? 2.184   43.872  92.908  1.00 31.44 ? 1218 ILE   B CD1   1 
ATOM   17900 N  N     . ASN   B  1  1221 ? 3.259   38.093  94.019  1.00 16.26 ? 1219 ASN   B N     1 
ATOM   17901 C  CA    . ASN   B  1  1221 ? 2.624   36.869  94.492  1.00 15.84 ? 1219 ASN   B CA    1 
ATOM   17902 C  C     . ASN   B  1  1221 ? 1.607   37.246  95.561  1.00 18.08 ? 1219 ASN   B C     1 
ATOM   17903 O  O     . ASN   B  1  1221 ? 1.978   37.578  96.689  1.00 20.00 ? 1219 ASN   B O     1 
ATOM   17904 C  CB    . ASN   B  1  1221 ? 3.696   35.961  95.082  1.00 17.04 ? 1219 ASN   B CB    1 
ATOM   17905 C  CG    . ASN   B  1  1221 ? 3.120   34.715  95.716  1.00 17.85 ? 1219 ASN   B CG    1 
ATOM   17906 O  OD1   . ASN   B  1  1221 ? 1.923   34.445  95.612  1.00 17.88 ? 1219 ASN   B OD1   1 
ATOM   17907 N  ND2   . ASN   B  1  1221 ? 3.975   33.940  96.373  1.00 21.11 ? 1219 ASN   B ND2   1 
ATOM   17908 N  N     . THR   B  1  1222 ? 0.325   37.187  95.223  1.00 16.29 ? 1220 THR   B N     1 
ATOM   17909 C  CA    . THR   B  1  1222 ? -0.731  37.573  96.151  1.00 19.39 ? 1220 THR   B CA    1 
ATOM   17910 C  C     . THR   B  1  1222 ? -1.251  36.398  96.961  1.00 24.39 ? 1220 THR   B C     1 
ATOM   17911 O  O     . THR   B  1  1222 ? -2.234  36.550  97.701  1.00 26.85 ? 1220 THR   B O     1 
ATOM   17912 C  CB    . THR   B  1  1222 ? -1.869  38.252  95.402  1.00 20.12 ? 1220 THR   B CB    1 
ATOM   17913 O  OG1   . THR   B  1  1222 ? -2.344  37.370  94.378  1.00 22.25 ? 1220 THR   B OG1   1 
ATOM   17914 C  CG2   . THR   B  1  1222 ? -1.374  39.541  94.761  1.00 21.18 ? 1220 THR   B CG2   1 
ATOM   17915 N  N     . ALA   B  1  1223 ? -0.634  35.233  96.824  1.00 20.35 ? 1221 ALA   B N     1 
ATOM   17916 C  CA    . ALA   B  1  1223 ? -0.919  34.088  97.668  1.00 24.48 ? 1221 ALA   B CA    1 
ATOM   17917 C  C     . ALA   B  1  1223 ? 0.105   33.929  98.781  1.00 32.21 ? 1221 ALA   B C     1 
ATOM   17918 O  O     . ALA   B  1  1223 ? 0.044   32.945  99.523  1.00 35.24 ? 1221 ALA   B O     1 
ATOM   17919 C  CB    . ALA   B  1  1223 ? -0.951  32.812  96.822  1.00 27.18 ? 1221 ALA   B CB    1 
ATOM   17920 N  N     . ALA   B  1  1224 ? 1.040   34.877  98.917  1.00 30.12 ? 1222 ALA   B N     1 
ATOM   17921 C  CA    . ALA   B  1  1224 ? 2.196   34.670  99.786  1.00 34.55 ? 1222 ALA   B CA    1 
ATOM   17922 C  C     . ALA   B  1  1224 ? 1.831   34.611  101.265 1.00 38.09 ? 1222 ALA   B C     1 
ATOM   17923 O  O     . ALA   B  1  1224 ? 2.617   34.080  102.057 1.00 35.28 ? 1222 ALA   B O     1 
ATOM   17924 C  CB    . ALA   B  1  1224 ? 3.262   35.740  99.547  1.00 31.63 ? 1222 ALA   B CB    1 
ATOM   17925 N  N     . ALA   B  1  1225 ? 0.668   35.140  101.656 1.00 33.69 ? 1223 ALA   B N     1 
ATOM   17926 C  CA    . ALA   B  1  1225 ? 0.237   35.083  103.048 1.00 37.50 ? 1223 ALA   B CA    1 
ATOM   17927 C  C     . ALA   B  1  1225 ? -0.391  33.747  103.428 1.00 44.82 ? 1223 ALA   B C     1 
ATOM   17928 O  O     . ALA   B  1  1225 ? -0.764  33.566  104.593 1.00 41.91 ? 1223 ALA   B O     1 
ATOM   17929 C  CB    . ALA   B  1  1225 ? -0.729  36.232  103.362 1.00 38.71 ? 1223 ALA   B CB    1 
ATOM   17930 N  N     . GLY   B  1  1226 ? -0.513  32.812  102.489 1.00 42.00 ? 1224 GLY   B N     1 
ATOM   17931 C  CA    . GLY   B  1  1226 ? -1.065  31.497  102.775 1.00 41.92 ? 1224 GLY   B CA    1 
ATOM   17932 C  C     . GLY   B  1  1226 ? -2.343  31.163  102.032 1.00 44.96 ? 1224 GLY   B C     1 
ATOM   17933 O  O     . GLY   B  1  1226 ? -2.861  30.050  102.205 1.00 41.46 ? 1224 GLY   B O     1 
ATOM   17934 N  N     . GLY   B  1  1227 ? -2.879  32.065  101.217 1.00 38.62 ? 1225 GLY   B N     1 
ATOM   17935 C  CA    . GLY   B  1  1227 ? -4.090  31.784  100.468 1.00 39.09 ? 1225 GLY   B CA    1 
ATOM   17936 C  C     . GLY   B  1  1227 ? -4.382  32.918  99.510  1.00 41.82 ? 1225 GLY   B C     1 
ATOM   17937 O  O     . GLY   B  1  1227 ? -3.644  33.904  99.433  1.00 38.09 ? 1225 GLY   B O     1 
ATOM   17938 N  N     . ASN   B  1  1228 ? -5.488  32.770  98.786  1.00 35.30 ? 1226 ASN   B N     1 
ATOM   17939 C  CA    . ASN   B  1  1228 ? -5.890  33.720  97.753  1.00 41.97 ? 1226 ASN   B CA    1 
ATOM   17940 C  C     . ASN   B  1  1228 ? -7.148  34.450  98.210  1.00 47.42 ? 1226 ASN   B C     1 
ATOM   17941 O  O     . ASN   B  1  1228 ? -8.158  33.814  98.532  1.00 53.39 ? 1226 ASN   B O     1 
ATOM   17942 C  CB    . ASN   B  1  1228 ? -6.143  32.993  96.431  1.00 44.60 ? 1226 ASN   B CB    1 
ATOM   17943 C  CG    . ASN   B  1  1228 ? -6.205  33.938  95.242  1.00 45.81 ? 1226 ASN   B CG    1 
ATOM   17944 O  OD1   . ASN   B  1  1228 ? -6.524  35.119  95.380  1.00 48.85 ? 1226 ASN   B OD1   1 
ATOM   17945 N  ND2   . ASN   B  1  1228 ? -5.899  33.414  94.062  1.00 38.70 ? 1226 ASN   B ND2   1 
ATOM   17946 N  N     . ALA   B  1  1229 ? -7.083  35.785  98.230  1.00 47.56 ? 1227 ALA   B N     1 
ATOM   17947 C  CA    . ALA   B  1  1229 ? -8.248  36.582  98.601  1.00 48.88 ? 1227 ALA   B CA    1 
ATOM   17948 C  C     . ALA   B  1  1229 ? -9.342  36.484  97.545  1.00 53.29 ? 1227 ALA   B C     1 
ATOM   17949 O  O     . ALA   B  1  1229 ? -10.519 36.286  97.872  1.00 53.76 ? 1227 ALA   B O     1 
ATOM   17950 C  CB    . ALA   B  1  1229 ? -7.838  38.040  98.809  1.00 42.43 ? 1227 ALA   B CB    1 
ATOM   17951 N  N     . SER   B  1  1230 ? -8.971  36.621  96.269  1.00 51.79 ? 1228 SER   B N     1 
ATOM   17952 C  CA    . SER   B  1  1230 ? -9.969  36.632  95.202  1.00 52.68 ? 1228 SER   B CA    1 
ATOM   17953 C  C     . SER   B  1  1230 ? -10.705 35.301  95.109  1.00 56.59 ? 1228 SER   B C     1 
ATOM   17954 O  O     . SER   B  1  1230 ? -11.927 35.271  94.918  1.00 56.59 ? 1228 SER   B O     1 
ATOM   17955 C  CB    . SER   B  1  1230 ? -9.313  36.978  93.864  1.00 54.01 ? 1228 SER   B CB    1 
ATOM   17956 O  OG    . SER   B  1  1230 ? -8.996  38.357  93.783  1.00 55.91 ? 1228 SER   B OG    1 
ATOM   17957 N  N     . LEU   B  1  1231 ? -9.982  34.188  95.242  1.00 51.75 ? 1229 LEU   B N     1 
ATOM   17958 C  CA    . LEU   B  1  1231 ? -10.599 32.879  95.079  1.00 50.98 ? 1229 LEU   B CA    1 
ATOM   17959 C  C     . LEU   B  1  1231 ? -11.430 32.449  96.281  1.00 56.08 ? 1229 LEU   B C     1 
ATOM   17960 O  O     . LEU   B  1  1231 ? -12.161 31.455  96.181  1.00 57.80 ? 1229 LEU   B O     1 
ATOM   17961 C  CB    . LEU   B  1  1231 ? -9.547  31.820  94.750  1.00 49.53 ? 1229 LEU   B CB    1 
ATOM   17962 C  CG    . LEU   B  1  1231 ? -8.950  31.756  93.345  1.00 39.41 ? 1229 LEU   B CG    1 
ATOM   17963 C  CD1   . LEU   B  1  1231 ? -8.121  30.492  93.230  1.00 31.27 ? 1229 LEU   B CD1   1 
ATOM   17964 C  CD2   . LEU   B  1  1231 ? -10.023 31.778  92.279  1.00 43.07 ? 1229 LEU   B CD2   1 
ATOM   17965 N  N     . MET   B  1  1232 ? -11.341 33.162  97.406  1.00 54.97 ? 1230 MET   B N     1 
ATOM   17966 C  CA    . MET   B  1  1232 ? -12.275 32.916  98.500  1.00 55.14 ? 1230 MET   B CA    1 
ATOM   17967 C  C     . MET   B  1  1232 ? -13.712 33.194  98.072  1.00 57.54 ? 1230 MET   B C     1 
ATOM   17968 O  O     . MET   B  1  1232 ? -14.636 32.488  98.497  1.00 49.17 ? 1230 MET   B O     1 
ATOM   17969 C  CB    . MET   B  1  1232 ? -11.894 33.766  99.714  1.00 53.44 ? 1230 MET   B CB    1 
ATOM   17970 N  N     . ALA   B  1  1233 ? -13.915 34.203  97.220  1.00 61.32 ? 1231 ALA   B N     1 
ATOM   17971 C  CA    . ALA   B  1  1233 ? -15.232 34.534  96.686  1.00 67.46 ? 1231 ALA   B CA    1 
ATOM   17972 C  C     . ALA   B  1  1233 ? -15.619 33.692  95.477  1.00 69.33 ? 1231 ALA   B C     1 
ATOM   17973 O  O     . ALA   B  1  1233 ? -16.698 33.907  94.911  1.00 71.31 ? 1231 ALA   B O     1 
ATOM   17974 C  CB    . ALA   B  1  1233 ? -15.297 36.021  96.319  1.00 64.34 ? 1231 ALA   B CB    1 
ATOM   17975 N  N     . ILE   B  1  1234 ? -14.776 32.747  95.070  1.00 63.54 ? 1232 ILE   B N     1 
ATOM   17976 C  CA    . ILE   B  1  1234 ? -15.032 31.900  93.910  1.00 60.91 ? 1232 ILE   B CA    1 
ATOM   17977 C  C     . ILE   B  1  1234 ? -15.461 30.527  94.414  1.00 57.25 ? 1232 ILE   B C     1 
ATOM   17978 O  O     . ILE   B  1  1234 ? -14.637 29.739  94.893  1.00 54.78 ? 1232 ILE   B O     1 
ATOM   17979 C  CB    . ILE   B  1  1234 ? -13.809 31.819  92.991  1.00 55.44 ? 1232 ILE   B CB    1 
ATOM   17980 C  CG1   . ILE   B  1  1234 ? -13.509 33.199  92.391  1.00 59.79 ? 1232 ILE   B CG1   1 
ATOM   17981 C  CG2   . ILE   B  1  1234 ? -14.033 30.788  91.909  1.00 51.84 ? 1232 ILE   B CG2   1 
ATOM   17982 C  CD1   . ILE   B  1  1234 ? -13.018 33.179  90.959  1.00 46.09 ? 1232 ILE   B CD1   1 
ATOM   17983 N  N     . GLY   B  1  1235 ? -16.757 30.242  94.311  1.00 51.42 ? 1233 GLY   B N     1 
ATOM   17984 C  CA    . GLY   B  1  1235 ? -17.301 28.959  94.715  1.00 43.62 ? 1233 GLY   B CA    1 
ATOM   17985 C  C     . GLY   B  1  1235 ? -18.133 28.318  93.617  1.00 35.54 ? 1233 GLY   B C     1 
ATOM   17986 O  O     . GLY   B  1  1235 ? -18.923 28.976  92.940  1.00 53.13 ? 1233 GLY   B O     1 
ATOM   17987 O  OXT   . GLY   B  1  1235 ? -18.049 27.119  93.376  1.00 29.50 ? 1233 GLY   B OXT   1 
HETATM 17988 P  PA    . FAD   C  2  .    ? -37.776 43.653  82.195  1.00 20.39 ? 1301 FAD   A PA    1 
HETATM 17989 O  O1A   . FAD   C  2  .    ? -36.319 43.203  81.943  1.00 22.01 ? 1301 FAD   A O1A   1 
HETATM 17990 O  O2A   . FAD   C  2  .    ? -38.811 42.686  82.524  1.00 23.66 ? 1301 FAD   A O2A   1 
HETATM 17991 O  O5B   . FAD   C  2  .    ? -37.910 44.688  83.229  1.00 20.47 ? 1301 FAD   A O5B   1 
HETATM 17992 C  C5B   . FAD   C  2  .    ? -36.845 45.611  83.449  1.00 20.41 ? 1301 FAD   A C5B   1 
HETATM 17993 C  C4B   . FAD   C  2  .    ? -37.355 46.702  84.378  1.00 18.85 ? 1301 FAD   A C4B   1 
HETATM 17994 O  O4B   . FAD   C  2  .    ? -37.355 46.268  85.699  1.00 18.18 ? 1301 FAD   A O4B   1 
HETATM 17995 C  C3B   . FAD   C  2  .    ? -36.572 47.973  84.407  1.00 19.60 ? 1301 FAD   A C3B   1 
HETATM 17996 O  O3B   . FAD   C  2  .    ? -36.805 48.785  83.303  1.00 19.38 ? 1301 FAD   A O3B   1 
HETATM 17997 C  C2B   . FAD   C  2  .    ? -37.048 48.582  85.676  1.00 18.84 ? 1301 FAD   A C2B   1 
HETATM 17998 O  O2B   . FAD   C  2  .    ? -38.290 49.189  85.550  1.00 18.26 ? 1301 FAD   A O2B   1 
HETATM 17999 C  C1B   . FAD   C  2  .    ? -37.239 47.384  86.534  1.00 16.92 ? 1301 FAD   A C1B   1 
HETATM 18000 N  N9A   . FAD   C  2  .    ? -36.147 47.125  87.436  1.00 17.90 ? 1301 FAD   A N9A   1 
HETATM 18001 C  C8A   . FAD   C  2  .    ? -34.846 46.786  87.094  1.00 20.60 ? 1301 FAD   A C8A   1 
HETATM 18002 N  N7A   . FAD   C  2  .    ? -34.139 46.615  88.210  1.00 20.06 ? 1301 FAD   A N7A   1 
HETATM 18003 C  C5A   . FAD   C  2  .    ? -34.947 46.816  89.320  1.00 19.36 ? 1301 FAD   A C5A   1 
HETATM 18004 C  C6A   . FAD   C  2  .    ? -34.761 46.762  90.688  1.00 20.14 ? 1301 FAD   A C6A   1 
HETATM 18005 N  N6A   . FAD   C  2  .    ? -33.491 46.429  91.275  1.00 20.28 ? 1301 FAD   A N6A   1 
HETATM 18006 N  N1A   . FAD   C  2  .    ? -35.793 47.024  91.490  1.00 19.88 ? 1301 FAD   A N1A   1 
HETATM 18007 C  C2A   . FAD   C  2  .    ? -37.021 47.333  91.015  1.00 19.78 ? 1301 FAD   A C2A   1 
HETATM 18008 N  N3A   . FAD   C  2  .    ? -37.246 47.394  89.680  1.00 19.10 ? 1301 FAD   A N3A   1 
HETATM 18009 C  C4A   . FAD   C  2  .    ? -36.236 47.140  88.831  1.00 19.04 ? 1301 FAD   A C4A   1 
HETATM 18010 N  N1    . FAD   C  2  .    ? -40.951 53.741  81.077  1.00 16.38 ? 1301 FAD   A N1    1 
HETATM 18011 C  C2    . FAD   C  2  .    ? -41.259 54.965  81.717  1.00 16.51 ? 1301 FAD   A C2    1 
HETATM 18012 O  O2    . FAD   C  2  .    ? -40.722 55.259  82.878  1.00 15.98 ? 1301 FAD   A O2    1 
HETATM 18013 N  N3    . FAD   C  2  .    ? -42.121 55.864  81.143  1.00 15.66 ? 1301 FAD   A N3    1 
HETATM 18014 C  C4    . FAD   C  2  .    ? -42.698 55.603  79.941  1.00 18.25 ? 1301 FAD   A C4    1 
HETATM 18015 O  O4    . FAD   C  2  .    ? -43.559 56.511  79.427  1.00 17.63 ? 1301 FAD   A O4    1 
HETATM 18016 C  C4X   . FAD   C  2  .    ? -42.436 54.332  79.234  1.00 16.81 ? 1301 FAD   A C4X   1 
HETATM 18017 N  N5    . FAD   C  2  .    ? -43.020 53.997  78.033  1.00 16.88 ? 1301 FAD   A N5    1 
HETATM 18018 C  C5X   . FAD   C  2  .    ? -42.738 52.757  77.454  1.00 18.31 ? 1301 FAD   A C5X   1 
HETATM 18019 C  C6    . FAD   C  2  .    ? -43.314 52.378  76.242  1.00 15.92 ? 1301 FAD   A C6    1 
HETATM 18020 C  C7    . FAD   C  2  .    ? -43.026 51.138  75.681  1.00 18.25 ? 1301 FAD   A C7    1 
HETATM 18021 C  C7M   . FAD   C  2  .    ? -43.681 50.749  74.388  1.00 19.35 ? 1301 FAD   A C7M   1 
HETATM 18022 C  C8    . FAD   C  2  .    ? -42.160 50.251  76.303  1.00 17.11 ? 1301 FAD   A C8    1 
HETATM 18023 C  C8M   . FAD   C  2  .    ? -41.853 48.915  75.690  1.00 20.87 ? 1301 FAD   A C8M   1 
HETATM 18024 C  C9    . FAD   C  2  .    ? -41.568 50.620  77.511  1.00 19.86 ? 1301 FAD   A C9    1 
HETATM 18025 C  C9A   . FAD   C  2  .    ? -41.865 51.859  78.073  1.00 19.86 ? 1301 FAD   A C9A   1 
HETATM 18026 N  N10   . FAD   C  2  .    ? -41.243 52.205  79.292  1.00 21.34 ? 1301 FAD   A N10   1 
HETATM 18027 C  C10   . FAD   C  2  .    ? -41.530 53.427  79.885  1.00 17.07 ? 1301 FAD   A C10   1 
HETATM 18028 C  "C1'" . FAD   C  2  .    ? -40.413 51.215  79.997  1.00 27.35 ? 1301 FAD   A "C1'" 1 
HETATM 18029 C  "C2'" . FAD   C  2  .    ? -38.940 51.357  80.141  1.00 29.34 ? 1301 FAD   A "C2'" 1 
HETATM 18030 O  "O2'" . FAD   C  2  .    ? -38.475 52.146  79.129  1.00 29.28 ? 1301 FAD   A "O2'" 1 
HETATM 18031 C  "C3'" . FAD   C  2  .    ? -38.457 49.903  80.025  1.00 27.15 ? 1301 FAD   A "C3'" 1 
HETATM 18032 O  "O3'" . FAD   C  2  .    ? -38.651 49.507  78.727  1.00 28.91 ? 1301 FAD   A "O3'" 1 
HETATM 18033 C  "C4'" . FAD   C  2  .    ? -39.194 48.886  80.880  1.00 20.30 ? 1301 FAD   A "C4'" 1 
HETATM 18034 O  "O4'" . FAD   C  2  .    ? -39.252 49.270  82.207  1.00 24.82 ? 1301 FAD   A "O4'" 1 
HETATM 18035 C  "C5'" . FAD   C  2  .    ? -38.510 47.528  80.715  1.00 23.03 ? 1301 FAD   A "C5'" 1 
HETATM 18036 O  "O5'" . FAD   C  2  .    ? -39.365 46.537  81.228  1.00 23.42 ? 1301 FAD   A "O5'" 1 
HETATM 18037 P  P     . FAD   C  2  .    ? -39.558 45.164  80.439  1.00 20.90 ? 1301 FAD   A P     1 
HETATM 18038 O  O1P   . FAD   C  2  .    ? -39.625 45.287  78.894  1.00 21.44 ? 1301 FAD   A O1P   1 
HETATM 18039 O  O2P   . FAD   C  2  .    ? -40.780 44.532  81.192  1.00 24.30 ? 1301 FAD   A O2P   1 
HETATM 18040 O  O3P   . FAD   C  2  .    ? -38.289 44.285  80.962  1.00 19.84 ? 1301 FAD   A O3P   1 
HETATM 18041 C  C1    . PGE   D  3  .    ? -3.104  61.581  94.854  1.00 36.77 ? 1302 PGE   A C1    1 
HETATM 18042 O  O1    . PGE   D  3  .    ? -3.130  60.181  95.038  1.00 40.36 ? 1302 PGE   A O1    1 
HETATM 18043 C  C2    . PGE   D  3  .    ? -2.492  62.255  96.059  1.00 34.31 ? 1302 PGE   A C2    1 
HETATM 18044 O  O2    . PGE   D  3  .    ? -1.124  61.930  96.138  1.00 32.09 ? 1302 PGE   A O2    1 
HETATM 18045 C  C3    . PGE   D  3  .    ? -0.252  63.025  96.263  1.00 28.98 ? 1302 PGE   A C3    1 
HETATM 18046 C  C4    . PGE   D  3  .    ? 1.214   62.654  96.294  1.00 28.19 ? 1302 PGE   A C4    1 
HETATM 18047 O  O4    . PGE   D  3  .    ? 1.865   58.316  95.018  1.00 45.22 ? 1302 PGE   A O4    1 
HETATM 18048 C  C6    . PGE   D  3  .    ? 2.453   59.571  94.744  1.00 45.08 ? 1302 PGE   A C6    1 
HETATM 18049 C  C5    . PGE   D  3  .    ? 2.092   60.519  95.873  1.00 40.76 ? 1302 PGE   A C5    1 
HETATM 18050 O  O3    . PGE   D  3  .    ? 1.512   61.681  95.326  1.00 43.03 ? 1302 PGE   A O3    1 
HETATM 18051 C  C     . FMT   E  4  .    ? -45.327 89.790  108.747 0.73 34.05 ? 1303 FMT   A C     1 
HETATM 18052 O  O1    . FMT   E  4  .    ? -44.894 89.399  109.848 0.73 35.33 ? 1303 FMT   A O1    1 
HETATM 18053 O  O2    . FMT   E  4  .    ? -46.443 89.597  108.229 0.73 38.80 ? 1303 FMT   A O2    1 
HETATM 18054 C  C     . FMT   F  4  .    ? -40.301 61.569  102.360 1.00 22.88 ? 1304 FMT   A C     1 
HETATM 18055 O  O1    . FMT   F  4  .    ? -39.518 61.081  103.191 1.00 35.26 ? 1304 FMT   A O1    1 
HETATM 18056 O  O2    . FMT   F  4  .    ? -41.558 61.608  102.365 1.00 33.12 ? 1304 FMT   A O2    1 
HETATM 18057 C  C02   . A1BDV G  5  .    ? -39.219 53.273  75.963  0.68 22.53 ? 1305 A1BDV A C02   1 
HETATM 18058 C  C03   . A1BDV G  5  .    ? -39.677 54.549  76.665  0.68 20.73 ? 1305 A1BDV A C03   1 
HETATM 18059 C  C04   . A1BDV G  5  .    ? -40.796 55.226  76.187  0.68 18.66 ? 1305 A1BDV A C04   1 
HETATM 18060 C  C05   . A1BDV G  5  .    ? -41.230 56.385  76.813  0.68 19.18 ? 1305 A1BDV A C05   1 
HETATM 18061 C  C06   . A1BDV G  5  .    ? -40.537 56.884  77.941  0.68 18.17 ? 1305 A1BDV A C06   1 
HETATM 18062 C  C08   . A1BDV G  5  .    ? -39.906 57.933  79.841  0.68 22.78 ? 1305 A1BDV A C08   1 
HETATM 18063 C  C10   . A1BDV G  5  .    ? -39.441 56.224  78.416  0.68 22.01 ? 1305 A1BDV A C10   1 
HETATM 18064 C  C11   . A1BDV G  5  .    ? -38.998 55.034  77.778  0.68 23.45 ? 1305 A1BDV A C11   1 
HETATM 18065 O  O01   . A1BDV G  5  .    ? -37.829 53.360  75.815  0.68 26.03 ? 1305 A1BDV A O01   1 
HETATM 18066 O  O07   . A1BDV G  5  .    ? -40.772 58.023  78.747  0.68 20.64 ? 1305 A1BDV A O07   1 
HETATM 18067 O  O09   . A1BDV G  5  .    ? -38.955 56.944  79.539  0.68 23.30 ? 1305 A1BDV A O09   1 
HETATM 18068 P  PA    . NAD   H  6  .    ? -18.183 88.482  106.726 1.00 21.78 ? 1306 NAD   A PA    1 
HETATM 18069 O  O1A   . NAD   H  6  .    ? -16.658 88.446  106.487 1.00 21.72 ? 1306 NAD   A O1A   1 
HETATM 18070 O  O2A   . NAD   H  6  .    ? -18.883 89.701  106.348 1.00 24.09 ? 1306 NAD   A O2A   1 
HETATM 18071 O  O5B   . NAD   H  6  .    ? -18.636 88.257  108.131 1.00 22.49 ? 1306 NAD   A O5B   1 
HETATM 18072 C  C5B   . NAD   H  6  .    ? -18.392 87.025  108.774 1.00 22.06 ? 1306 NAD   A C5B   1 
HETATM 18073 C  C4B   . NAD   H  6  .    ? -18.314 87.120  110.297 1.00 19.52 ? 1306 NAD   A C4B   1 
HETATM 18074 O  O4B   . NAD   H  6  .    ? -17.180 87.863  110.709 1.00 20.89 ? 1306 NAD   A O4B   1 
HETATM 18075 C  C3B   . NAD   H  6  .    ? -19.521 87.724  110.959 1.00 20.50 ? 1306 NAD   A C3B   1 
HETATM 18076 O  O3B   . NAD   H  6  .    ? -19.897 87.019  112.090 1.00 21.52 ? 1306 NAD   A O3B   1 
HETATM 18077 C  C2B   . NAD   H  6  .    ? -19.075 89.110  111.203 1.00 24.38 ? 1306 NAD   A C2B   1 
HETATM 18078 O  O2B   . NAD   H  6  .    ? -19.797 89.744  112.198 1.00 23.17 ? 1306 NAD   A O2B   1 
HETATM 18079 C  C1B   . NAD   H  6  .    ? -17.668 88.861  111.583 1.00 24.42 ? 1306 NAD   A C1B   1 
HETATM 18080 N  N9A   . NAD   H  6  .    ? -16.774 89.994  111.506 1.00 21.61 ? 1306 NAD   A N9A   1 
HETATM 18081 C  C8A   . NAD   H  6  .    ? -16.806 91.092  110.669 1.00 23.94 ? 1306 NAD   A C8A   1 
HETATM 18082 N  N7A   . NAD   H  6  .    ? -15.750 91.871  110.913 1.00 24.78 ? 1306 NAD   A N7A   1 
HETATM 18083 C  C5A   . NAD   H  6  .    ? -14.984 91.302  111.920 1.00 22.91 ? 1306 NAD   A C5A   1 
HETATM 18084 C  C6A   . NAD   H  6  .    ? -13.817 91.637  112.578 1.00 25.13 ? 1306 NAD   A C6A   1 
HETATM 18085 N  N6A   . NAD   H  6  .    ? -13.112 92.839  112.246 1.00 27.23 ? 1306 NAD   A N6A   1 
HETATM 18086 N  N1A   . NAD   H  6  .    ? -13.345 90.825  113.527 1.00 24.94 ? 1306 NAD   A N1A   1 
HETATM 18087 C  C2A   . NAD   H  6  .    ? -13.958 89.671  113.890 1.00 25.47 ? 1306 NAD   A C2A   1 
HETATM 18088 N  N3A   . NAD   H  6  .    ? -15.114 89.313  113.274 1.00 21.65 ? 1306 NAD   A N3A   1 
HETATM 18089 C  C4A   . NAD   H  6  .    ? -15.621 90.096  112.305 1.00 23.11 ? 1306 NAD   A C4A   1 
HETATM 18090 O  O3    . NAD   H  6  .    ? -18.897 87.436  105.905 1.00 20.68 ? 1306 NAD   A O3    1 
HETATM 18091 P  PN    . NAD   H  6  .    ? -20.437 87.134  105.623 1.00 21.79 ? 1306 NAD   A PN    1 
HETATM 18092 O  O1N   . NAD   H  6  .    ? -20.944 88.197  104.699 1.00 24.94 ? 1306 NAD   A O1N   1 
HETATM 18093 O  O2N   . NAD   H  6  .    ? -21.218 86.924  106.875 1.00 22.99 ? 1306 NAD   A O2N   1 
HETATM 18094 O  O5D   . NAD   H  6  .    ? -20.354 85.768  104.816 1.00 22.58 ? 1306 NAD   A O5D   1 
HETATM 18095 C  C5D   . NAD   H  6  .    ? -20.030 85.756  103.450 1.00 24.16 ? 1306 NAD   A C5D   1 
HETATM 18096 C  C4D   . NAD   H  6  .    ? -18.586 85.355  103.191 1.00 20.62 ? 1306 NAD   A C4D   1 
HETATM 18097 O  O4D   . NAD   H  6  .    ? -18.265 84.149  103.827 1.00 19.79 ? 1306 NAD   A O4D   1 
HETATM 18098 C  C3D   . NAD   H  6  .    ? -18.295 85.196  101.738 1.00 22.51 ? 1306 NAD   A C3D   1 
HETATM 18099 O  O3D   . NAD   H  6  .    ? -17.107 85.800  101.434 1.00 23.67 ? 1306 NAD   A O3D   1 
HETATM 18100 C  C2D   . NAD   H  6  .    ? -18.188 83.737  101.585 1.00 18.52 ? 1306 NAD   A C2D   1 
HETATM 18101 O  O2D   . NAD   H  6  .    ? -17.422 83.331  100.492 1.00 20.37 ? 1306 NAD   A O2D   1 
HETATM 18102 C  C1D   . NAD   H  6  .    ? -17.584 83.367  102.889 1.00 19.47 ? 1306 NAD   A C1D   1 
HETATM 18103 N  N1N   . NAD   H  6  .    ? -17.859 82.002  103.197 1.00 18.10 ? 1306 NAD   A N1N   1 
HETATM 18104 C  C2N   . NAD   H  6  .    ? -16.841 81.022  103.115 1.00 20.09 ? 1306 NAD   A C2N   1 
HETATM 18105 C  C3N   . NAD   H  6  .    ? -17.192 79.714  103.410 1.00 20.98 ? 1306 NAD   A C3N   1 
HETATM 18106 C  C7N   . NAD   H  6  .    ? -16.202 78.608  103.348 1.00 17.67 ? 1306 NAD   A C7N   1 
HETATM 18107 O  O7N   . NAD   H  6  .    ? -16.523 77.486  103.713 1.00 20.49 ? 1306 NAD   A O7N   1 
HETATM 18108 N  N7N   . NAD   H  6  .    ? -14.909 78.879  102.831 1.00 18.11 ? 1306 NAD   A N7N   1 
HETATM 18109 C  C4N   . NAD   H  6  .    ? -18.512 79.401  103.806 1.00 32.11 ? 1306 NAD   A C4N   1 
HETATM 18110 C  C5N   . NAD   H  6  .    ? -19.524 80.379  103.850 1.00 27.86 ? 1306 NAD   A C5N   1 
HETATM 18111 C  C6N   . NAD   H  6  .    ? -19.183 81.679  103.542 1.00 21.12 ? 1306 NAD   A C6N   1 
HETATM 18112 S  S     . SO4   I  7  .    ? -9.176  53.148  110.554 1.00 19.87 ? 1307 SO4   A S     1 
HETATM 18113 O  O1    . SO4   I  7  .    ? -8.080  53.366  109.562 1.00 20.68 ? 1307 SO4   A O1    1 
HETATM 18114 O  O2    . SO4   I  7  .    ? -10.241 52.327  109.913 1.00 24.57 ? 1307 SO4   A O2    1 
HETATM 18115 O  O3    . SO4   I  7  .    ? -8.641  52.402  111.749 1.00 20.67 ? 1307 SO4   A O3    1 
HETATM 18116 O  O4    . SO4   I  7  .    ? -9.659  54.500  110.967 1.00 24.68 ? 1307 SO4   A O4    1 
HETATM 18117 S  S     . SO4   J  7  .    ? 12.840  75.479  125.231 0.71 36.15 ? 1308 SO4   A S     1 
HETATM 18118 O  O1    . SO4   J  7  .    ? 13.625  75.986  124.058 0.71 36.73 ? 1308 SO4   A O1    1 
HETATM 18119 O  O2    . SO4   J  7  .    ? 11.424  75.215  124.823 0.71 34.26 ? 1308 SO4   A O2    1 
HETATM 18120 O  O3    . SO4   J  7  .    ? 13.459  74.206  125.729 0.71 40.35 ? 1308 SO4   A O3    1 
HETATM 18121 O  O4    . SO4   J  7  .    ? 12.858  76.509  126.320 0.71 46.74 ? 1308 SO4   A O4    1 
HETATM 18122 S  S     . SO4   K  7  .    ? 29.334  71.370  105.202 0.76 42.26 ? 1309 SO4   A S     1 
HETATM 18123 O  O1    . SO4   K  7  .    ? 29.394  70.910  103.778 0.76 43.48 ? 1309 SO4   A O1    1 
HETATM 18124 O  O2    . SO4   K  7  .    ? 27.934  71.780  105.548 0.76 45.60 ? 1309 SO4   A O2    1 
HETATM 18125 O  O3    . SO4   K  7  .    ? 29.780  70.256  106.099 0.76 43.51 ? 1309 SO4   A O3    1 
HETATM 18126 O  O4    . SO4   K  7  .    ? 30.234  72.555  105.381 0.76 43.44 ? 1309 SO4   A O4    1 
HETATM 18127 S  S     . SO4   L  7  .    ? -12.452 75.303  69.756  0.56 28.02 ? 1310 SO4   A S     1 
HETATM 18128 O  O1    . SO4   L  7  .    ? -11.242 75.321  70.630  0.56 29.16 ? 1310 SO4   A O1    1 
HETATM 18129 O  O2    . SO4   L  7  .    ? -12.316 74.171  68.786  0.56 34.67 ? 1310 SO4   A O2    1 
HETATM 18130 O  O3    . SO4   L  7  .    ? -13.699 75.111  70.558  0.56 23.76 ? 1310 SO4   A O3    1 
HETATM 18131 O  O4    . SO4   L  7  .    ? -12.532 76.598  69.004  0.56 35.78 ? 1310 SO4   A O4    1 
HETATM 18132 S  S     . SO4   M  7  .    ? -34.029 25.055  79.407  0.73 45.20 ? 1311 SO4   A S     1 
HETATM 18133 O  O1    . SO4   M  7  .    ? -33.115 26.132  78.902  0.73 42.06 ? 1311 SO4   A O1    1 
HETATM 18134 O  O2    . SO4   M  7  .    ? -34.969 24.653  78.314  0.73 42.35 ? 1311 SO4   A O2    1 
HETATM 18135 O  O3    . SO4   M  7  .    ? -33.215 23.865  79.813  0.73 55.98 ? 1311 SO4   A O3    1 
HETATM 18136 O  O4    . SO4   M  7  .    ? -34.785 25.543  80.607  0.73 41.69 ? 1311 SO4   A O4    1 
HETATM 18137 MG MG    . MG    N  8  .    ? -19.946 91.528  106.563 0.73 22.46 ? 1312 MG    A MG    1 
HETATM 18138 P  PA    . FAD   O  2  .    ? -17.098 23.527  103.524 1.00 23.21 ? 1301 FAD   B PA    1 
HETATM 18139 O  O1A   . FAD   O  2  .    ? -17.314 25.049  103.575 1.00 22.88 ? 1301 FAD   B O1A   1 
HETATM 18140 O  O2A   . FAD   O  2  .    ? -18.216 22.618  103.326 1.00 27.49 ? 1301 FAD   B O2A   1 
HETATM 18141 O  O5B   . FAD   O  2  .    ? -16.170 23.059  102.436 1.00 23.77 ? 1301 FAD   B O5B   1 
HETATM 18142 C  C5B   . FAD   O  2  .    ? -15.051 23.880  102.130 1.00 25.10 ? 1301 FAD   B C5B   1 
HETATM 18143 C  C4B   . FAD   O  2  .    ? -14.122 23.164  101.160 1.00 22.39 ? 1301 FAD   B C4B   1 
HETATM 18144 O  O4B   . FAD   O  2  .    ? -14.619 23.145  99.854  1.00 20.89 ? 1301 FAD   B O4B   1 
HETATM 18145 C  C3B   . FAD   O  2  .    ? -12.794 23.839  101.031 1.00 19.89 ? 1301 FAD   B C3B   1 
HETATM 18146 O  O3B   . FAD   O  2  .    ? -11.941 23.638  102.109 1.00 20.95 ? 1301 FAD   B O3B   1 
HETATM 18147 C  C2B   . FAD   O  2  .    ? -12.283 23.222  99.780  1.00 18.75 ? 1301 FAD   B C2B   1 
HETATM 18148 O  O2B   . FAD   O  2  .    ? -11.903 21.919  99.956  1.00 20.18 ? 1301 FAD   B O2B   1 
HETATM 18149 C  C1B   . FAD   O  2  .    ? -13.521 23.162  98.967  1.00 20.69 ? 1301 FAD   B C1B   1 
HETATM 18150 N  N9A   . FAD   O  2  .    ? -13.725 24.227  98.021  1.00 19.72 ? 1301 FAD   B N9A   1 
HETATM 18151 C  C8A   . FAD   O  2  .    ? -13.850 25.576  98.269  1.00 21.88 ? 1301 FAD   B C8A   1 
HETATM 18152 N  N7A   . FAD   O  2  .    ? -14.059 26.241  97.133  1.00 21.99 ? 1301 FAD   B N7A   1 
HETATM 18153 C  C5A   . FAD   O  2  .    ? -14.073 25.331  96.085  1.00 18.68 ? 1301 FAD   B C5A   1 
HETATM 18154 C  C6A   . FAD   O  2  .    ? -14.266 25.424  94.714  1.00 18.99 ? 1301 FAD   B C6A   1 
HETATM 18155 N  N6A   . FAD   O  2  .    ? -14.496 26.697  94.088  1.00 20.53 ? 1301 FAD   B N6A   1 
HETATM 18156 N  N1A   . FAD   O  2  .    ? -14.215 24.301  93.983  1.00 18.66 ? 1301 FAD   B N1A   1 
HETATM 18157 C  C2A   . FAD   O  2  .    ? -14.026 23.077  94.521  1.00 16.59 ? 1301 FAD   B C2A   1 
HETATM 18158 N  N3A   . FAD   O  2  .    ? -13.847 22.947  95.864  1.00 18.67 ? 1301 FAD   B N3A   1 
HETATM 18159 C  C4A   . FAD   O  2  .    ? -13.875 24.041  96.633  1.00 20.02 ? 1301 FAD   B C4A   1 
HETATM 18160 N  N1    . FAD   O  2  .    ? -7.554  18.871  104.406 1.00 18.32 ? 1301 FAD   B N1    1 
HETATM 18161 C  C2    . FAD   O  2  .    ? -6.398  18.343  103.785 1.00 19.49 ? 1301 FAD   B C2    1 
HETATM 18162 O  O2    . FAD   O  2  .    ? -6.111  18.792  102.567 1.00 17.58 ? 1301 FAD   B O2    1 
HETATM 18163 N  N3    . FAD   O  2  .    ? -5.598  17.405  104.375 1.00 17.67 ? 1301 FAD   B N3    1 
HETATM 18164 C  C4    . FAD   O  2  .    ? -5.867  16.948  105.627 1.00 18.34 ? 1301 FAD   B C4    1 
HETATM 18165 O  O4    . FAD   O  2  .    ? -5.074  16.001  106.165 1.00 19.33 ? 1301 FAD   B O4    1 
HETATM 18166 C  C4X   . FAD   O  2  .    ? -7.057  17.466  106.337 1.00 20.10 ? 1301 FAD   B C4X   1 
HETATM 18167 N  N5    . FAD   O  2  .    ? -7.393  17.017  107.600 1.00 18.70 ? 1301 FAD   B N5    1 
HETATM 18168 C  C5X   . FAD   O  2  .    ? -8.538  17.527  108.193 1.00 19.37 ? 1301 FAD   B C5X   1 
HETATM 18169 C  C6    . FAD   O  2  .    ? -8.886  17.079  109.473 1.00 18.48 ? 1301 FAD   B C6    1 
HETATM 18170 C  C7    . FAD   O  2  .    ? -10.038 17.581  110.060 1.00 21.24 ? 1301 FAD   B C7    1 
HETATM 18171 C  C7M   . FAD   O  2  .    ? -10.444 17.119  111.437 1.00 22.66 ? 1301 FAD   B C7M   1 
HETATM 18172 C  C8    . FAD   O  2  .    ? -10.823 18.506  109.405 1.00 20.44 ? 1301 FAD   B C8    1 
HETATM 18173 C  C8M   . FAD   O  2  .    ? -12.060 19.042  110.051 1.00 21.76 ? 1301 FAD   B C8M   1 
HETATM 18174 C  C9    . FAD   O  2  .    ? -10.488 18.952  108.132 1.00 22.55 ? 1301 FAD   B C9    1 
HETATM 18175 C  C9A   . FAD   O  2  .    ? -9.344  18.456  107.540 1.00 19.78 ? 1301 FAD   B C9A   1 
HETATM 18176 N  N10   . FAD   O  2  .    ? -8.990  18.941  106.253 1.00 20.05 ? 1301 FAD   B N10   1 
HETATM 18177 C  C10   . FAD   O  2  .    ? -7.864  18.427  105.650 1.00 19.80 ? 1301 FAD   B C10   1 
HETATM 18178 C  "C1'" . FAD   O  2  .    ? -9.898  19.851  105.507 1.00 22.90 ? 1301 FAD   B "C1'" 1 
HETATM 18179 C  "C2'" . FAD   O  2  .    ? -9.610  21.309  105.308 1.00 26.80 ? 1301 FAD   B "C2'" 1 
HETATM 18180 O  "O2'" . FAD   O  2  .    ? -8.723  21.745  106.257 1.00 24.44 ? 1301 FAD   B "O2'" 1 
HETATM 18181 C  "C3'" . FAD   O  2  .    ? -10.960 22.038  105.431 1.00 27.45 ? 1301 FAD   B "C3'" 1 
HETATM 18182 O  "O3'" . FAD   O  2  .    ? -11.347 22.068  106.752 1.00 27.21 ? 1301 FAD   B "O3'" 1 
HETATM 18183 C  "C4'" . FAD   O  2  .    ? -12.107 21.406  104.664 1.00 25.40 ? 1301 FAD   B "C4'" 1 
HETATM 18184 O  "O4'" . FAD   O  2  .    ? -11.804 21.350  103.311 1.00 23.55 ? 1301 FAD   B "O4'" 1 
HETATM 18185 C  "C5'" . FAD   O  2  .    ? -13.379 22.206  104.913 1.00 24.66 ? 1301 FAD   B "C5'" 1 
HETATM 18186 O  "O5'" . FAD   O  2  .    ? -14.501 21.466  104.481 1.00 21.57 ? 1301 FAD   B "O5'" 1 
HETATM 18187 P  P     . FAD   O  2  .    ? -15.865 21.660  105.310 1.00 22.19 ? 1301 FAD   B P     1 
HETATM 18188 O  O1P   . FAD   O  2  .    ? -15.643 21.681  106.872 1.00 22.59 ? 1301 FAD   B O1P   1 
HETATM 18189 O  O2P   . FAD   O  2  .    ? -16.822 20.591  104.684 1.00 28.23 ? 1301 FAD   B O2P   1 
HETATM 18190 O  O3P   . FAD   O  2  .    ? -16.444 23.044  104.752 1.00 25.83 ? 1301 FAD   B O3P   1 
HETATM 18191 C  C     . FMT   P  4  .    ? 11.104  49.606  77.484  0.58 16.43 ? 1302 FMT   B C     1 
HETATM 18192 O  O1    . FMT   P  4  .    ? 11.221  49.464  76.244  0.58 21.85 ? 1302 FMT   B O1    1 
HETATM 18193 O  O2    . FMT   P  4  .    ? 11.947  49.788  78.397  0.58 20.99 ? 1302 FMT   B O2    1 
HETATM 18194 C  C1    . PGE   Q  3  .    ? 1.487   60.513  87.004  1.00 37.51 ? 1303 PGE   B C1    1 
HETATM 18195 O  O1    . PGE   Q  3  .    ? 0.280   59.797  86.849  1.00 40.46 ? 1303 PGE   B O1    1 
HETATM 18196 C  C2    . PGE   Q  3  .    ? 2.395   60.240  85.830  1.00 35.65 ? 1303 PGE   B C2    1 
HETATM 18197 O  O2    . PGE   Q  3  .    ? 3.258   59.165  86.120  1.00 38.18 ? 1303 PGE   B O2    1 
HETATM 18198 C  C3    . PGE   Q  3  .    ? 3.980   58.664  85.018  1.00 29.42 ? 1303 PGE   B C3    1 
HETATM 18199 C  C4    . PGE   Q  3  .    ? 4.460   57.236  85.179  1.00 30.29 ? 1303 PGE   B C4    1 
HETATM 18200 O  O4    . PGE   Q  3  .    ? 1.795   54.690  87.000  1.00 41.15 ? 1303 PGE   B O4    1 
HETATM 18201 C  C6    . PGE   Q  3  .    ? 3.183   54.455  86.956  1.00 38.76 ? 1303 PGE   B C6    1 
HETATM 18202 C  C5    . PGE   Q  3  .    ? 3.740   55.073  85.688  1.00 35.05 ? 1303 PGE   B C5    1 
HETATM 18203 O  O3    . PGE   Q  3  .    ? 3.413   56.439  85.671  1.00 35.09 ? 1303 PGE   B O3    1 
HETATM 18204 O  OH2   . 1PE   R  9  .    ? 42.323  35.271  83.997  1.00 27.53 ? 1304 1PE   B OH2   1 
HETATM 18205 C  C12   . 1PE   R  9  .    ? 42.157  34.099  83.238  1.00 30.30 ? 1304 1PE   B C12   1 
HETATM 18206 C  C22   . 1PE   R  9  .    ? 41.291  34.359  82.032  1.00 32.62 ? 1304 1PE   B C22   1 
HETATM 18207 O  OH3   . 1PE   R  9  .    ? 39.988  34.733  82.409  1.00 34.51 ? 1304 1PE   B OH3   1 
HETATM 18208 C  C13   . 1PE   R  9  .    ? 37.881  35.624  81.763  1.00 35.63 ? 1304 1PE   B C13   1 
HETATM 18209 C  C23   . 1PE   R  9  .    ? 39.292  35.317  81.336  1.00 35.05 ? 1304 1PE   B C23   1 
HETATM 18210 O  OH4   . 1PE   R  9  .    ? 37.856  36.710  82.655  1.00 40.74 ? 1304 1PE   B OH4   1 
HETATM 18211 C  C14   . 1PE   R  9  .    ? 36.509  38.437  83.661  1.00 35.96 ? 1304 1PE   B C14   1 
HETATM 18212 C  C24   . 1PE   R  9  .    ? 36.549  37.217  82.781  1.00 34.99 ? 1304 1PE   B C24   1 
HETATM 18213 O  OH5   . 1PE   R  9  .    ? 37.705  38.599  84.378  1.00 34.34 ? 1304 1PE   B OH5   1 
HETATM 18214 C  C15   . 1PE   R  9  .    ? 39.018  40.521  84.904  1.00 35.17 ? 1304 1PE   B C15   1 
HETATM 18215 C  C25   . 1PE   R  9  .    ? 37.702  39.818  85.081  1.00 36.02 ? 1304 1PE   B C25   1 
HETATM 18216 O  OH6   . 1PE   R  9  .    ? 40.072  39.689  85.305  1.00 34.71 ? 1304 1PE   B OH6   1 
HETATM 18217 C  C16   . 1PE   R  9  .    ? 42.291  39.531  86.123  1.00 30.94 ? 1304 1PE   B C16   1 
HETATM 18218 C  C26   . 1PE   R  9  .    ? 41.256  40.421  85.495  1.00 31.89 ? 1304 1PE   B C26   1 
HETATM 18219 O  OH7   . 1PE   R  9  .    ? 42.201  38.244  85.553  1.00 29.53 ? 1304 1PE   B OH7   1 
HETATM 18220 C  C1    . PEG   S  10 .    ? 15.979  66.467  54.149  1.00 43.34 ? 1305 PEG   B C1    1 
HETATM 18221 O  O1    . PEG   S  10 .    ? 15.878  67.381  55.222  1.00 32.36 ? 1305 PEG   B O1    1 
HETATM 18222 C  C2    . PEG   S  10 .    ? 14.645  66.163  53.512  1.00 37.84 ? 1305 PEG   B C2    1 
HETATM 18223 O  O2    . PEG   S  10 .    ? 14.335  64.792  53.613  1.00 45.70 ? 1305 PEG   B O2    1 
HETATM 18224 C  C3    . PEG   S  10 .    ? 15.440  63.937  53.433  1.00 45.70 ? 1305 PEG   B C3    1 
HETATM 18225 C  C4    . PEG   S  10 .    ? 15.077  62.527  53.816  1.00 37.07 ? 1305 PEG   B C4    1 
HETATM 18226 O  O4    . PEG   S  10 .    ? 16.176  61.917  54.450  1.00 45.99 ? 1305 PEG   B O4    1 
HETATM 18227 C  C     . FMT   T  4  .    ? -0.920  17.179  82.648  1.00 11.54 ? 1306 FMT   B C     1 
HETATM 18228 O  O1    . FMT   T  4  .    ? -1.130  15.955  82.775  1.00 33.67 ? 1306 FMT   B O1    1 
HETATM 18229 O  O2    . FMT   T  4  .    ? -1.288  17.955  81.766  1.00 31.20 ? 1306 FMT   B O2    1 
HETATM 18230 C  C02   . A1BDV U  5  .    ? -7.476  20.964  109.461 0.80 25.45 ? 1307 A1BDV B C02   1 
HETATM 18231 C  C03   . A1BDV U  5  .    ? -6.315  20.300  108.725 0.80 20.77 ? 1307 A1BDV B C03   1 
HETATM 18232 C  C04   . A1BDV U  5  .    ? -5.731  19.162  109.272 0.80 21.58 ? 1307 A1BDV B C04   1 
HETATM 18233 C  C05   . A1BDV U  5  .    ? -4.678  18.531  108.628 0.80 21.77 ? 1307 A1BDV B C05   1 
HETATM 18234 C  C06   . A1BDV U  5  .    ? -4.191  19.051  107.407 0.80 20.73 ? 1307 A1BDV B C06   1 
HETATM 18235 C  C08   . A1BDV U  5  .    ? -3.097  19.483  105.476 0.80 21.46 ? 1307 A1BDV B C08   1 
HETATM 18236 C  C10   . A1BDV U  5  .    ? -4.761  20.170  106.868 0.80 20.91 ? 1307 A1BDV B C10   1 
HETATM 18237 C  C11   . A1BDV U  5  .    ? -5.841  20.815  107.525 0.80 23.09 ? 1307 A1BDV B C11   1 
HETATM 18238 O  O01   . A1BDV U  5  .    ? -7.246  22.345  109.489 0.80 30.65 ? 1307 A1BDV B O01   1 
HETATM 18239 O  O07   . A1BDV U  5  .    ? -3.149  18.603  106.570 0.80 23.42 ? 1307 A1BDV B O07   1 
HETATM 18240 O  O09   . A1BDV U  5  .    ? -4.085  20.464  105.659 0.80 23.97 ? 1307 A1BDV B O09   1 
HETATM 18241 P  PA    . NAD   V  6  .    ? 27.532  35.959  74.862  1.00 15.94 ? 1308 NAD   B PA    1 
HETATM 18242 O  O1A   . NAD   V  6  .    ? 27.596  37.493  74.839  1.00 15.74 ? 1308 NAD   B O1A   1 
HETATM 18243 O  O2A   . NAD   V  6  .    ? 28.757  35.215  75.183  1.00 18.91 ? 1308 NAD   B O2A   1 
HETATM 18244 O  O5B   . NAD   V  6  .    ? 27.172  35.409  73.511  1.00 16.03 ? 1308 NAD   B O5B   1 
HETATM 18245 C  C5B   . NAD   V  6  .    ? 25.907  35.707  72.962  1.00 17.24 ? 1308 NAD   B C5B   1 
HETATM 18246 C  C4B   . NAD   V  6  .    ? 25.904  35.562  71.451  1.00 17.04 ? 1308 NAD   B C4B   1 
HETATM 18247 O  O4B   . NAD   V  6  .    ? 26.678  36.572  70.827  1.00 15.67 ? 1308 NAD   B O4B   1 
HETATM 18248 C  C3B   . NAD   V  6  .    ? 26.369  34.224  70.952  1.00 15.82 ? 1308 NAD   B C3B   1 
HETATM 18249 O  O3B   . NAD   V  6  .    ? 25.598  33.801  69.874  1.00 15.67 ? 1308 NAD   B O3B   1 
HETATM 18250 C  C2B   . NAD   V  6  .    ? 27.754  34.534  70.538  1.00 15.94 ? 1308 NAD   B C2B   1 
HETATM 18251 O  O2B   . NAD   V  6  .    ? 28.287  33.667  69.595  1.00 16.13 ? 1308 NAD   B O2B   1 
HETATM 18252 C  C1B   . NAD   V  6  .    ? 27.559  35.880  69.962  1.00 15.52 ? 1308 NAD   B C1B   1 
HETATM 18253 N  N9A   . NAD   V  6  .    ? 28.766  36.658  69.838  1.00 16.25 ? 1308 NAD   B N9A   1 
HETATM 18254 C  C8A   . NAD   V  6  .    ? 29.918  36.599  70.612  1.00 17.79 ? 1308 NAD   B C8A   1 
HETATM 18255 N  N7A   . NAD   V  6  .    ? 30.769  37.531  70.168  1.00 19.61 ? 1308 NAD   B N7A   1 
HETATM 18256 C  C5A   . NAD   V  6  .    ? 30.208  38.227  69.113  1.00 18.73 ? 1308 NAD   B C5A   1 
HETATM 18257 C  C6A   . NAD   V  6  .    ? 30.578  39.274  68.300  1.00 18.15 ? 1308 NAD   B C6A   1 
HETATM 18258 N  N6A   . NAD   V  6  .    ? 31.875  39.873  68.465  1.00 21.84 ? 1308 NAD   B N6A   1 
HETATM 18259 N  N1A   . NAD   V  6  .    ? 29.771  39.743  67.358  1.00 18.50 ? 1308 NAD   B N1A   1 
HETATM 18260 C  C2A   . NAD   V  6  .    ? 28.535  39.215  67.148  1.00 17.17 ? 1308 NAD   B C2A   1 
HETATM 18261 N  N3A   . NAD   V  6  .    ? 28.137  38.189  67.929  1.00 15.63 ? 1308 NAD   B N3A   1 
HETATM 18262 C  C4A   . NAD   V  6  .    ? 28.913  37.690  68.903  1.00 15.45 ? 1308 NAD   B C4A   1 
HETATM 18263 O  O3    . NAD   V  6  .    ? 26.456  35.441  75.781  1.00 15.49 ? 1308 NAD   B O3    1 
HETATM 18264 P  PN    . NAD   V  6  .    ? 26.112  34.007  76.350  1.00 16.13 ? 1308 NAD   B PN    1 
HETATM 18265 O  O1N   . NAD   V  6  .    ? 27.271  33.528  77.189  1.00 18.77 ? 1308 NAD   B O1N   1 
HETATM 18266 O  O2N   . NAD   V  6  .    ? 25.754  33.092  75.212  1.00 16.89 ? 1308 NAD   B O2N   1 
HETATM 18267 O  O5D   . NAD   V  6  .    ? 24.830  34.251  77.231  1.00 16.94 ? 1308 NAD   B O5D   1 
HETATM 18268 C  C5D   . NAD   V  6  .    ? 24.932  34.765  78.540  1.00 17.39 ? 1308 NAD   B C5D   1 
HETATM 18269 C  C4D   . NAD   V  6  .    ? 24.725  36.269  78.591  1.00 16.59 ? 1308 NAD   B C4D   1 
HETATM 18270 O  O4D   . NAD   V  6  .    ? 23.483  36.590  78.010  1.00 16.31 ? 1308 NAD   B O4D   1 
HETATM 18271 C  C3D   . NAD   V  6  .    ? 24.725  36.791  79.997  1.00 16.04 ? 1308 NAD   B C3D   1 
HETATM 18272 O  O3D   . NAD   V  6  .    ? 25.389  37.998  80.053  1.00 17.80 ? 1308 NAD   B O3D   1 
HETATM 18273 C  C2D   . NAD   V  6  .    ? 23.275  36.962  80.235  1.00 15.16 ? 1308 NAD   B C2D   1 
HETATM 18274 O  O2D   . NAD   V  6  .    ? 22.909  37.843  81.243  1.00 16.47 ? 1308 NAD   B O2D   1 
HETATM 18275 C  C1D   . NAD   V  6  .    ? 22.806  37.425  78.897  1.00 15.53 ? 1308 NAD   B C1D   1 
HETATM 18276 N  N1N   . NAD   V  6  .    ? 21.402  37.208  78.747  1.00 15.68 ? 1308 NAD   B N1N   1 
HETATM 18277 C  C2N   . NAD   V  6  .    ? 20.521  38.304  78.747  1.00 15.04 ? 1308 NAD   B C2N   1 
HETATM 18278 C  C3N   . NAD   V  6  .    ? 19.171  38.025  78.648  1.00 16.90 ? 1308 NAD   B C3N   1 
HETATM 18279 C  C7N   . NAD   V  6  .    ? 18.170  39.108  78.661  1.00 14.47 ? 1308 NAD   B C7N   1 
HETATM 18280 O  O7N   . NAD   V  6  .    ? 17.005  38.835  78.394  1.00 16.64 ? 1308 NAD   B O7N   1 
HETATM 18281 N  N7N   . NAD   V  6  .    ? 18.536  40.428  79.007  1.00 15.99 ? 1308 NAD   B N7N   1 
HETATM 18282 C  C4N   . NAD   V  6  .    ? 18.737  36.696  78.454  1.00 29.35 ? 1308 NAD   B C4N   1 
HETATM 18283 C  C5N   . NAD   V  6  .    ? 19.632  35.605  78.489  1.00 21.00 ? 1308 NAD   B C5N   1 
HETATM 18284 C  C6N   . NAD   V  6  .    ? 20.980  35.884  78.613  1.00 15.19 ? 1308 NAD   B C6N   1 
HETATM 18285 S  S     . SO4   W  7  .    ? -7.219  47.650  72.766  1.00 18.11 ? 1309 SO4   B S     1 
HETATM 18286 O  O1    . SO4   W  7  .    ? -6.001  46.924  72.287  1.00 21.21 ? 1309 SO4   B O1    1 
HETATM 18287 O  O2    . SO4   W  7  .    ? -7.971  48.150  71.575  1.00 17.74 ? 1309 SO4   B O2    1 
HETATM 18288 O  O3    . SO4   W  7  .    ? -8.076  46.743  73.572  1.00 21.30 ? 1309 SO4   B O3    1 
HETATM 18289 O  O4    . SO4   W  7  .    ? -6.757  48.810  73.568  1.00 21.92 ? 1309 SO4   B O4    1 
HETATM 18290 MG MG    . MG    X  8  .    ? 30.193  33.710  74.923  0.69 22.63 ? 1310 MG    B MG    1 
HETATM 18291 C  C1    . PEG   Y  10 .    ? 16.877  27.538  46.340  1.00 36.93 ? 1311 PEG   B C1    1 
HETATM 18292 O  O1    . PEG   Y  10 .    ? 16.211  27.822  45.131  1.00 41.48 ? 1311 PEG   B O1    1 
HETATM 18293 C  C2    . PEG   Y  10 .    ? 16.504  26.153  46.814  1.00 32.03 ? 1311 PEG   B C2    1 
HETATM 18294 O  O2    . PEG   Y  10 .    ? 15.869  26.222  48.072  1.00 40.30 ? 1311 PEG   B O2    1 
HETATM 18295 C  C3    . PEG   Y  10 .    ? 14.648  25.522  48.114  1.00 35.15 ? 1311 PEG   B C3    1 
HETATM 18296 C  C4    . PEG   Y  10 .    ? 13.608  26.259  48.924  1.00 34.49 ? 1311 PEG   B C4    1 
HETATM 18297 O  O4    . PEG   Y  10 .    ? 12.340  25.729  48.617  1.00 36.59 ? 1311 PEG   B O4    1 
HETATM 18298 O  O     . HOH   Z  11 .    ? 1.477   94.107  116.565 1.00 40.73 ? 1401 HOH   A O     1 
HETATM 18299 O  O     . HOH   Z  11 .    ? -10.629 91.452  113.893 1.00 34.08 ? 1402 HOH   A O     1 
HETATM 18300 O  O     . HOH   Z  11 .    ? -39.237 37.804  64.260  1.00 41.51 ? 1403 HOH   A O     1 
HETATM 18301 O  O     . HOH   Z  11 .    ? -51.311 74.032  68.030  1.00 31.02 ? 1404 HOH   A O     1 
HETATM 18302 O  O     . HOH   Z  11 .    ? -1.318  88.887  105.022 1.00 20.96 ? 1405 HOH   A O     1 
HETATM 18303 O  O     . HOH   Z  11 .    ? -32.116 79.739  98.803  1.00 30.05 ? 1406 HOH   A O     1 
HETATM 18304 O  O     . HOH   Z  11 .    ? -48.804 50.200  104.750 1.00 43.44 ? 1407 HOH   A O     1 
HETATM 18305 O  O     . HOH   Z  11 .    ? -19.399 72.779  97.108  1.00 25.09 ? 1408 HOH   A O     1 
HETATM 18306 O  O     . HOH   Z  11 .    ? -10.486 63.431  48.261  1.00 45.87 ? 1409 HOH   A O     1 
HETATM 18307 O  O     . HOH   Z  11 .    ? 4.723   81.155  128.976 1.00 41.39 ? 1410 HOH   A O     1 
HETATM 18308 O  O     . HOH   Z  11 .    ? -52.403 61.326  101.610 1.00 28.71 ? 1411 HOH   A O     1 
HETATM 18309 O  O     . HOH   Z  11 .    ? -0.794  91.929  114.998 1.00 41.16 ? 1412 HOH   A O     1 
HETATM 18310 O  O     . HOH   Z  11 .    ? -32.176 56.137  85.661  1.00 27.31 ? 1413 HOH   A O     1 
HETATM 18311 O  O     . HOH   Z  11 .    ? -57.462 67.481  61.480  1.00 31.70 ? 1414 HOH   A O     1 
HETATM 18312 O  O     . HOH   Z  11 .    ? -3.022  82.002  114.280 1.00 34.80 ? 1415 HOH   A O     1 
HETATM 18313 O  O     . HOH   Z  11 .    ? -46.206 26.154  86.155  1.00 41.77 ? 1416 HOH   A O     1 
HETATM 18314 O  O     . HOH   Z  11 .    ? -33.480 71.722  76.500  1.00 38.18 ? 1417 HOH   A O     1 
HETATM 18315 O  O     . HOH   Z  11 .    ? -21.826 95.451  120.351 1.00 38.11 ? 1418 HOH   A O     1 
HETATM 18316 O  O     . HOH   Z  11 .    ? -40.378 96.590  108.998 1.00 40.11 ? 1419 HOH   A O     1 
HETATM 18317 O  O     . HOH   Z  11 .    ? -0.561  79.838  81.346  1.00 36.62 ? 1420 HOH   A O     1 
HETATM 18318 O  O     . HOH   Z  11 .    ? -25.302 60.883  127.524 1.00 37.43 ? 1421 HOH   A O     1 
HETATM 18319 O  O     . HOH   Z  11 .    ? -35.951 85.618  103.890 1.00 29.68 ? 1422 HOH   A O     1 
HETATM 18320 O  O     . HOH   Z  11 .    ? 25.982  72.168  104.249 1.00 36.62 ? 1423 HOH   A O     1 
HETATM 18321 O  O     . HOH   Z  11 .    ? -38.715 67.271  69.042  1.00 33.36 ? 1424 HOH   A O     1 
HETATM 18322 O  O     . HOH   Z  11 .    ? -31.289 58.604  115.306 1.00 44.94 ? 1425 HOH   A O     1 
HETATM 18323 O  O     . HOH   Z  11 .    ? -5.024  72.093  95.186  1.00 36.01 ? 1426 HOH   A O     1 
HETATM 18324 O  O     . HOH   Z  11 .    ? -43.069 33.525  101.974 1.00 38.50 ? 1427 HOH   A O     1 
HETATM 18325 O  O     . HOH   Z  11 .    ? -0.396  63.838  109.372 1.00 23.24 ? 1428 HOH   A O     1 
HETATM 18326 O  O     . HOH   Z  11 .    ? -43.082 80.649  89.430  1.00 31.70 ? 1429 HOH   A O     1 
HETATM 18327 O  O     . HOH   Z  11 .    ? -52.222 24.665  82.304  1.00 39.65 ? 1430 HOH   A O     1 
HETATM 18328 O  O     . HOH   Z  11 .    ? -21.524 66.256  69.818  1.00 43.23 ? 1431 HOH   A O     1 
HETATM 18329 O  O     . HOH   Z  11 .    ? -42.011 80.387  69.720  1.00 39.34 ? 1432 HOH   A O     1 
HETATM 18330 O  O     . HOH   Z  11 .    ? 15.012  55.408  110.296 1.00 35.93 ? 1433 HOH   A O     1 
HETATM 18331 O  O     . HOH   Z  11 .    ? -27.384 99.984  94.275  1.00 42.87 ? 1434 HOH   A O     1 
HETATM 18332 O  O     . HOH   Z  11 .    ? -23.224 56.955  83.661  1.00 35.31 ? 1435 HOH   A O     1 
HETATM 18333 O  O     . HOH   Z  11 .    ? 0.067   82.523  113.021 1.00 36.20 ? 1436 HOH   A O     1 
HETATM 18334 O  O     . HOH   Z  11 .    ? -66.828 72.585  75.134  1.00 30.28 ? 1437 HOH   A O     1 
HETATM 18335 O  O     . HOH   Z  11 .    ? -32.074 87.015  76.287  1.00 36.96 ? 1438 HOH   A O     1 
HETATM 18336 O  O     . HOH   Z  11 .    ? -28.879 94.093  81.837  1.00 40.00 ? 1439 HOH   A O     1 
HETATM 18337 O  O     . HOH   Z  11 .    ? -14.301 64.590  50.903  1.00 41.70 ? 1440 HOH   A O     1 
HETATM 18338 O  O     . HOH   Z  11 .    ? -36.508 64.509  82.731  1.00 33.71 ? 1441 HOH   A O     1 
HETATM 18339 O  O     . HOH   Z  11 .    ? 9.098   81.316  95.746  1.00 43.64 ? 1442 HOH   A O     1 
HETATM 18340 O  O     . HOH   Z  11 .    ? -20.535 55.003  115.409 1.00 38.94 ? 1443 HOH   A O     1 
HETATM 18341 O  O     . HOH   Z  11 .    ? -2.395  67.739  124.433 1.00 38.32 ? 1444 HOH   A O     1 
HETATM 18342 O  O     . HOH   Z  11 .    ? -11.866 68.746  76.218  1.00 25.75 ? 1445 HOH   A O     1 
HETATM 18343 O  O     . HOH   Z  11 .    ? -12.505 87.880  98.647  1.00 35.36 ? 1446 HOH   A O     1 
HETATM 18344 O  O     . HOH   Z  11 .    ? -7.105  80.820  127.612 1.00 33.72 ? 1447 HOH   A O     1 
HETATM 18345 O  O     . HOH   Z  11 .    ? -28.795 38.183  84.555  1.00 46.26 ? 1448 HOH   A O     1 
HETATM 18346 O  O     . HOH   Z  11 .    ? 4.012   87.109  97.854  1.00 36.57 ? 1449 HOH   A O     1 
HETATM 18347 O  O     . HOH   Z  11 .    ? -57.639 28.333  85.491  1.00 37.55 ? 1450 HOH   A O     1 
HETATM 18348 O  O     . HOH   Z  11 .    ? -26.551 85.786  136.734 1.00 39.23 ? 1451 HOH   A O     1 
HETATM 18349 O  O     . HOH   Z  11 .    ? -24.998 67.064  85.894  1.00 30.54 ? 1452 HOH   A O     1 
HETATM 18350 O  O     . HOH   Z  11 .    ? -54.801 33.636  70.943  1.00 35.66 ? 1453 HOH   A O     1 
HETATM 18351 O  O     . HOH   Z  11 .    ? -33.669 93.331  85.877  1.00 39.48 ? 1454 HOH   A O     1 
HETATM 18352 O  O     . HOH   Z  11 .    ? -24.821 65.228  94.356  1.00 33.46 ? 1455 HOH   A O     1 
HETATM 18353 O  O     . HOH   Z  11 .    ? -25.154 59.210  73.094  1.00 35.00 ? 1456 HOH   A O     1 
HETATM 18354 O  O     . HOH   Z  11 .    ? -46.211 52.404  106.380 1.00 42.66 ? 1457 HOH   A O     1 
HETATM 18355 O  O     . HOH   Z  11 .    ? 8.710   90.634  102.464 1.00 42.45 ? 1458 HOH   A O     1 
HETATM 18356 O  O     . HOH   Z  11 .    ? -29.181 57.753  115.124 1.00 37.40 ? 1459 HOH   A O     1 
HETATM 18357 O  O     . HOH   Z  11 .    ? 0.154   59.431  108.280 1.00 31.34 ? 1460 HOH   A O     1 
HETATM 18358 O  O     . HOH   Z  11 .    ? -14.174 61.580  107.231 1.00 25.21 ? 1461 HOH   A O     1 
HETATM 18359 O  O     . HOH   Z  11 .    ? -58.560 37.655  64.687  1.00 44.08 ? 1462 HOH   A O     1 
HETATM 18360 O  O     . HOH   Z  11 .    ? -37.067 67.304  90.473  1.00 40.88 ? 1463 HOH   A O     1 
HETATM 18361 O  O     . HOH   Z  11 .    ? -55.154 76.221  83.404  1.00 36.28 ? 1464 HOH   A O     1 
HETATM 18362 O  O     . HOH   Z  11 .    ? 5.966   96.235  116.347 1.00 38.75 ? 1465 HOH   A O     1 
HETATM 18363 O  O     . HOH   Z  11 .    ? -6.320  68.627  92.075  1.00 28.61 ? 1466 HOH   A O     1 
HETATM 18364 O  O     . HOH   Z  11 .    ? -33.452 61.339  114.032 1.00 41.39 ? 1467 HOH   A O     1 
HETATM 18365 O  O     . HOH   Z  11 .    ? -6.596  58.622  119.601 1.00 23.13 ? 1468 HOH   A O     1 
HETATM 18366 O  O     . HOH   Z  11 .    ? -38.416 38.296  87.429  1.00 36.04 ? 1469 HOH   A O     1 
HETATM 18367 O  O     . HOH   Z  11 .    ? -65.236 48.063  85.262  1.00 36.17 ? 1470 HOH   A O     1 
HETATM 18368 O  O     . HOH   Z  11 .    ? 21.021  57.626  104.676 1.00 34.39 ? 1471 HOH   A O     1 
HETATM 18369 O  O     . HOH   Z  11 .    ? -24.191 92.890  126.335 1.00 33.23 ? 1472 HOH   A O     1 
HETATM 18370 O  O     . HOH   Z  11 .    ? -54.969 56.611  64.469  1.00 18.38 ? 1473 HOH   A O     1 
HETATM 18371 O  O     . HOH   Z  11 .    ? 14.518  61.301  94.128  1.00 29.65 ? 1474 HOH   A O     1 
HETATM 18372 O  O     . HOH   Z  11 .    ? 21.375  68.094  116.323 1.00 40.18 ? 1475 HOH   A O     1 
HETATM 18373 O  O     . HOH   Z  11 .    ? -30.912 67.027  98.300  1.00 37.35 ? 1476 HOH   A O     1 
HETATM 18374 O  O     . HOH   Z  11 .    ? -37.751 62.655  81.384  1.00 27.48 ? 1477 HOH   A O     1 
HETATM 18375 O  O     . HOH   Z  11 .    ? -42.385 38.913  84.640  1.00 28.91 ? 1478 HOH   A O     1 
HETATM 18376 O  O     . HOH   Z  11 .    ? -34.571 67.532  124.927 1.00 35.67 ? 1479 HOH   A O     1 
HETATM 18377 O  O     . HOH   Z  11 .    ? -35.645 56.256  77.709  1.00 38.33 ? 1480 HOH   A O     1 
HETATM 18378 O  O     . HOH   Z  11 .    ? -21.585 47.362  57.740  1.00 32.70 ? 1481 HOH   A O     1 
HETATM 18379 O  O     . HOH   Z  11 .    ? -10.516 49.800  109.648 1.00 23.12 ? 1482 HOH   A O     1 
HETATM 18380 O  O     . HOH   Z  11 .    ? -47.058 75.629  66.799  1.00 32.87 ? 1483 HOH   A O     1 
HETATM 18381 O  O     . HOH   Z  11 .    ? -41.263 63.190  73.367  1.00 27.95 ? 1484 HOH   A O     1 
HETATM 18382 O  O     . HOH   Z  11 .    ? -4.705  43.758  57.608  1.00 35.52 ? 1485 HOH   A O     1 
HETATM 18383 O  O     . HOH   Z  11 .    ? -44.183 91.587  110.967 1.00 37.88 ? 1486 HOH   A O     1 
HETATM 18384 O  O     . HOH   Z  11 .    ? -1.198  50.504  57.472  1.00 28.15 ? 1487 HOH   A O     1 
HETATM 18385 O  O     . HOH   Z  11 .    ? -22.980 80.530  109.839 1.00 26.75 ? 1488 HOH   A O     1 
HETATM 18386 O  O     . HOH   Z  11 .    ? -48.452 54.772  60.908  1.00 25.55 ? 1489 HOH   A O     1 
HETATM 18387 O  O     . HOH   Z  11 .    ? 25.455  79.993  106.869 1.00 35.89 ? 1490 HOH   A O     1 
HETATM 18388 O  O     . HOH   Z  11 .    ? -27.764 61.157  84.035  1.00 37.04 ? 1491 HOH   A O     1 
HETATM 18389 O  O     . HOH   Z  11 .    ? -51.818 47.625  68.630  1.00 29.48 ? 1492 HOH   A O     1 
HETATM 18390 O  O     . HOH   Z  11 .    ? -5.996  70.721  72.611  1.00 38.40 ? 1493 HOH   A O     1 
HETATM 18391 O  O     . HOH   Z  11 .    ? -61.951 57.576  63.537  1.00 29.56 ? 1494 HOH   A O     1 
HETATM 18392 O  O     . HOH   Z  11 .    ? -44.678 30.283  95.888  1.00 42.69 ? 1495 HOH   A O     1 
HETATM 18393 O  O     . HOH   Z  11 .    ? 12.416  74.234  91.067  1.00 35.75 ? 1496 HOH   A O     1 
HETATM 18394 O  O     . HOH   Z  11 .    ? -32.429 79.432  96.012  1.00 31.01 ? 1497 HOH   A O     1 
HETATM 18395 O  O     . HOH   Z  11 .    ? -55.152 75.622  91.833  1.00 40.07 ? 1498 HOH   A O     1 
HETATM 18396 O  O     . HOH   Z  11 .    ? -62.698 43.938  82.019  1.00 31.22 ? 1499 HOH   A O     1 
HETATM 18397 O  O     . HOH   Z  11 .    ? -50.705 50.675  57.123  1.00 36.87 ? 1500 HOH   A O     1 
HETATM 18398 O  O     . HOH   Z  11 .    ? -46.526 38.206  63.807  1.00 40.60 ? 1501 HOH   A O     1 
HETATM 18399 O  O     . HOH   Z  11 .    ? -23.271 63.834  97.521  1.00 20.55 ? 1502 HOH   A O     1 
HETATM 18400 O  O     . HOH   Z  11 .    ? -45.232 73.058  114.261 1.00 40.77 ? 1503 HOH   A O     1 
HETATM 18401 O  O     . HOH   Z  11 .    ? -2.430  74.647  83.936  1.00 32.20 ? 1504 HOH   A O     1 
HETATM 18402 O  O     . HOH   Z  11 .    ? -11.581 63.296  112.834 1.00 20.45 ? 1505 HOH   A O     1 
HETATM 18403 O  O     . HOH   Z  11 .    ? -49.229 66.774  93.722  1.00 21.65 ? 1506 HOH   A O     1 
HETATM 18404 O  O     . HOH   Z  11 .    ? -13.840 74.453  105.592 1.00 21.75 ? 1507 HOH   A O     1 
HETATM 18405 O  O     . HOH   Z  11 .    ? -35.028 95.076  95.842  1.00 29.49 ? 1508 HOH   A O     1 
HETATM 18406 O  O     . HOH   Z  11 .    ? -38.895 77.672  96.843  1.00 22.50 ? 1509 HOH   A O     1 
HETATM 18407 O  O     . HOH   Z  11 .    ? -32.625 92.253  125.667 1.00 39.89 ? 1510 HOH   A O     1 
HETATM 18408 O  O     . HOH   Z  11 .    ? -7.140  50.546  76.334  1.00 27.47 ? 1511 HOH   A O     1 
HETATM 18409 O  O     . HOH   Z  11 .    ? -20.519 55.110  90.876  1.00 36.48 ? 1512 HOH   A O     1 
HETATM 18410 O  O     . HOH   Z  11 .    ? -16.543 76.571  108.148 1.00 21.58 ? 1513 HOH   A O     1 
HETATM 18411 O  O     . HOH   Z  11 .    ? -14.297 75.876  109.500 1.00 21.76 ? 1514 HOH   A O     1 
HETATM 18412 O  O     . HOH   Z  11 .    ? 16.165  61.709  115.439 1.00 34.43 ? 1515 HOH   A O     1 
HETATM 18413 O  O     . HOH   Z  11 .    ? -58.430 38.373  75.905  1.00 33.18 ? 1516 HOH   A O     1 
HETATM 18414 O  O     . HOH   Z  11 .    ? 6.932   54.203  100.981 1.00 20.69 ? 1517 HOH   A O     1 
HETATM 18415 O  O     . HOH   Z  11 .    ? -37.021 80.604  78.668  1.00 20.67 ? 1518 HOH   A O     1 
HETATM 18416 O  O     . HOH   Z  11 .    ? -3.589  70.508  117.086 1.00 25.68 ? 1519 HOH   A O     1 
HETATM 18417 O  O     . HOH   Z  11 .    ? -0.287  93.009  104.264 1.00 28.37 ? 1520 HOH   A O     1 
HETATM 18418 O  O     . HOH   Z  11 .    ? -36.537 95.154  93.582  1.00 32.77 ? 1521 HOH   A O     1 
HETATM 18419 O  O     . HOH   Z  11 .    ? -10.346 81.228  90.774  1.00 23.96 ? 1522 HOH   A O     1 
HETATM 18420 O  O     . HOH   Z  11 .    ? -37.482 64.192  66.638  1.00 29.24 ? 1523 HOH   A O     1 
HETATM 18421 O  O     . HOH   Z  11 .    ? -44.850 63.645  83.978  1.00 18.27 ? 1524 HOH   A O     1 
HETATM 18422 O  O     . HOH   Z  11 .    ? -3.977  79.214  103.376 1.00 22.96 ? 1525 HOH   A O     1 
HETATM 18423 O  O     . HOH   Z  11 .    ? -4.829  70.297  76.173  1.00 32.96 ? 1526 HOH   A O     1 
HETATM 18424 O  O     . HOH   Z  11 .    ? -60.420 59.712  90.170  1.00 19.98 ? 1527 HOH   A O     1 
HETATM 18425 O  O     . HOH   Z  11 .    ? 17.647  78.627  119.275 1.00 37.57 ? 1528 HOH   A O     1 
HETATM 18426 O  O     . HOH   Z  11 .    ? -35.963 52.098  69.204  1.00 34.20 ? 1529 HOH   A O     1 
HETATM 18427 O  O     . HOH   Z  11 .    ? 23.292  69.779  112.652 1.00 36.40 ? 1530 HOH   A O     1 
HETATM 18428 O  O     . HOH   Z  11 .    ? -17.557 72.795  110.866 1.00 19.59 ? 1531 HOH   A O     1 
HETATM 18429 O  O     . HOH   Z  11 .    ? -39.204 35.419  85.279  1.00 34.75 ? 1532 HOH   A O     1 
HETATM 18430 O  O     . HOH   Z  11 .    ? -50.866 58.966  104.594 1.00 39.18 ? 1533 HOH   A O     1 
HETATM 18431 O  O     . HOH   Z  11 .    ? -18.759 59.189  103.887 1.00 24.53 ? 1534 HOH   A O     1 
HETATM 18432 O  O     . HOH   Z  11 .    ? -5.608  53.710  110.354 1.00 17.94 ? 1535 HOH   A O     1 
HETATM 18433 O  O     . HOH   Z  11 .    ? 10.952  76.770  96.426  1.00 27.39 ? 1536 HOH   A O     1 
HETATM 18434 O  O     . HOH   Z  11 .    ? -25.300 87.648  132.498 1.00 38.74 ? 1537 HOH   A O     1 
HETATM 18435 O  O     . HOH   Z  11 .    ? -27.734 78.821  100.817 1.00 30.70 ? 1538 HOH   A O     1 
HETATM 18436 O  O     . HOH   Z  11 .    ? -28.700 42.295  92.454  1.00 47.15 ? 1539 HOH   A O     1 
HETATM 18437 O  O     . HOH   Z  11 .    ? -32.450 96.314  125.046 1.00 43.45 ? 1540 HOH   A O     1 
HETATM 18438 O  O     . HOH   Z  11 .    ? -42.618 66.418  63.295  1.00 35.03 ? 1541 HOH   A O     1 
HETATM 18439 O  O     . HOH   Z  11 .    ? -45.377 89.466  105.756 1.00 35.17 ? 1542 HOH   A O     1 
HETATM 18440 O  O     . HOH   Z  11 .    ? -22.327 67.627  80.974  1.00 28.23 ? 1543 HOH   A O     1 
HETATM 18441 O  O     . HOH   Z  11 .    ? 14.295  86.961  109.666 1.00 32.05 ? 1544 HOH   A O     1 
HETATM 18442 O  O     . HOH   Z  11 .    ? -63.719 73.445  78.144  1.00 33.84 ? 1545 HOH   A O     1 
HETATM 18443 O  O     . HOH   Z  11 .    ? -21.572 90.433  105.932 1.00 28.46 ? 1546 HOH   A O     1 
HETATM 18444 O  O     . HOH   Z  11 .    ? -23.030 60.554  115.419 1.00 22.19 ? 1547 HOH   A O     1 
HETATM 18445 O  O     . HOH   Z  11 .    ? -43.002 48.511  59.788  1.00 26.94 ? 1548 HOH   A O     1 
HETATM 18446 O  O     . HOH   Z  11 .    ? -68.556 56.735  82.384  1.00 30.59 ? 1549 HOH   A O     1 
HETATM 18447 O  O     . HOH   Z  11 .    ? -11.653 73.155  128.090 1.00 29.40 ? 1550 HOH   A O     1 
HETATM 18448 O  O     . HOH   Z  11 .    ? -37.491 78.016  119.929 1.00 36.58 ? 1551 HOH   A O     1 
HETATM 18449 O  O     . HOH   Z  11 .    ? -25.735 70.321  130.777 1.00 38.71 ? 1552 HOH   A O     1 
HETATM 18450 O  O     . HOH   Z  11 .    ? -13.430 55.636  81.143  1.00 32.44 ? 1553 HOH   A O     1 
HETATM 18451 O  O     . HOH   Z  11 .    ? -41.373 71.491  64.027  1.00 27.70 ? 1554 HOH   A O     1 
HETATM 18452 O  O     . HOH   Z  11 .    ? -43.482 75.564  113.682 1.00 28.16 ? 1555 HOH   A O     1 
HETATM 18453 O  O     . HOH   Z  11 .    ? 9.361   79.371  121.610 1.00 35.14 ? 1556 HOH   A O     1 
HETATM 18454 O  O     . HOH   Z  11 .    ? -15.294 56.494  84.221  1.00 41.75 ? 1557 HOH   A O     1 
HETATM 18455 O  O     . HOH   Z  11 .    ? -46.712 59.862  101.716 1.00 23.91 ? 1558 HOH   A O     1 
HETATM 18456 O  O     . HOH   Z  11 .    ? 0.280   76.686  122.770 1.00 34.71 ? 1559 HOH   A O     1 
HETATM 18457 O  O     . HOH   Z  11 .    ? -9.077  77.722  131.516 1.00 39.77 ? 1560 HOH   A O     1 
HETATM 18458 O  O     . HOH   Z  11 .    ? -28.829 75.252  101.394 1.00 33.02 ? 1561 HOH   A O     1 
HETATM 18459 O  O     . HOH   Z  11 .    ? -9.560  64.997  76.090  1.00 21.83 ? 1562 HOH   A O     1 
HETATM 18460 O  O     . HOH   Z  11 .    ? 8.354   89.936  119.667 1.00 31.92 ? 1563 HOH   A O     1 
HETATM 18461 O  O     . HOH   Z  11 .    ? -46.453 81.365  93.028  1.00 38.66 ? 1564 HOH   A O     1 
HETATM 18462 O  O     . HOH   Z  11 .    ? -26.276 82.630  112.153 1.00 22.15 ? 1565 HOH   A O     1 
HETATM 18463 O  O     . HOH   Z  11 .    ? -33.712 52.759  81.616  1.00 37.53 ? 1566 HOH   A O     1 
HETATM 18464 O  O     . HOH   Z  11 .    ? -6.375  82.775  102.804 1.00 22.72 ? 1567 HOH   A O     1 
HETATM 18465 O  O     . HOH   Z  11 .    ? -46.910 35.234  86.647  1.00 28.79 ? 1568 HOH   A O     1 
HETATM 18466 O  O     . HOH   Z  11 .    ? -39.857 57.334  87.683  1.00 16.52 ? 1569 HOH   A O     1 
HETATM 18467 O  O     . HOH   Z  11 .    ? 0.544   85.241  111.209 1.00 29.89 ? 1570 HOH   A O     1 
HETATM 18468 O  O     . HOH   Z  11 .    ? -59.469 54.347  74.452  1.00 19.85 ? 1571 HOH   A O     1 
HETATM 18469 O  O     . HOH   Z  11 .    ? -51.398 55.332  75.577  1.00 19.03 ? 1572 HOH   A O     1 
HETATM 18470 O  O     . HOH   Z  11 .    ? 4.331   73.834  115.863 1.00 30.49 ? 1573 HOH   A O     1 
HETATM 18471 O  O     . HOH   Z  11 .    ? -38.074 62.356  105.005 1.00 34.70 ? 1574 HOH   A O     1 
HETATM 18472 O  O     . HOH   Z  11 .    ? -1.186  77.975  114.112 1.00 26.90 ? 1575 HOH   A O     1 
HETATM 18473 O  O     . HOH   Z  11 .    ? 25.052  77.393  108.859 1.00 36.08 ? 1576 HOH   A O     1 
HETATM 18474 O  O     . HOH   Z  11 .    ? -12.385 77.129  102.720 1.00 19.02 ? 1577 HOH   A O     1 
HETATM 18475 O  O     . HOH   Z  11 .    ? -44.067 31.319  68.655  1.00 39.19 ? 1578 HOH   A O     1 
HETATM 18476 O  O     . HOH   Z  11 .    ? -50.555 69.866  100.027 1.00 22.17 ? 1579 HOH   A O     1 
HETATM 18477 O  O     . HOH   Z  11 .    ? -30.678 81.627  128.725 1.00 42.32 ? 1580 HOH   A O     1 
HETATM 18478 O  O     . HOH   Z  11 .    ? -25.234 96.034  123.231 1.00 34.12 ? 1581 HOH   A O     1 
HETATM 18479 O  O     . HOH   Z  11 .    ? 0.357   85.601  102.600 1.00 25.33 ? 1582 HOH   A O     1 
HETATM 18480 O  O     . HOH   Z  11 .    ? -22.123 54.663  85.567  1.00 37.52 ? 1583 HOH   A O     1 
HETATM 18481 O  O     . HOH   Z  11 .    ? -38.944 27.799  86.182  1.00 43.01 ? 1584 HOH   A O     1 
HETATM 18482 O  O     . HOH   Z  11 .    ? -1.153  83.832  117.546 1.00 27.95 ? 1585 HOH   A O     1 
HETATM 18483 O  O     . HOH   Z  11 .    ? -17.246 86.842  91.760  1.00 22.53 ? 1586 HOH   A O     1 
HETATM 18484 O  O     . HOH   Z  11 .    ? -13.402 77.964  110.723 1.00 21.41 ? 1587 HOH   A O     1 
HETATM 18485 O  O     . HOH   Z  11 .    ? -20.116 52.542  77.818  1.00 28.76 ? 1588 HOH   A O     1 
HETATM 18486 O  O     . HOH   Z  11 .    ? 2.252   85.797  117.648 1.00 28.36 ? 1589 HOH   A O     1 
HETATM 18487 O  O     . HOH   Z  11 .    ? -61.161 55.611  67.307  1.00 20.97 ? 1590 HOH   A O     1 
HETATM 18488 O  O     . HOH   Z  11 .    ? -15.424 44.015  76.348  1.00 43.63 ? 1591 HOH   A O     1 
HETATM 18489 O  O     . HOH   Z  11 .    ? -56.227 34.687  86.024  1.00 24.77 ? 1592 HOH   A O     1 
HETATM 18490 O  O     . HOH   Z  11 .    ? -61.802 58.305  69.898  1.00 21.07 ? 1593 HOH   A O     1 
HETATM 18491 O  O     . HOH   Z  11 .    ? -18.755 96.081  93.794  1.00 40.80 ? 1594 HOH   A O     1 
HETATM 18492 O  O     . HOH   Z  11 .    ? 13.816  87.291  98.014  1.00 37.01 ? 1595 HOH   A O     1 
HETATM 18493 O  O     . HOH   Z  11 .    ? -27.405 73.689  129.115 1.00 34.08 ? 1596 HOH   A O     1 
HETATM 18494 O  O     . HOH   Z  11 .    ? -20.090 59.282  75.967  1.00 22.56 ? 1597 HOH   A O     1 
HETATM 18495 O  O     . HOH   Z  11 .    ? -10.444 69.320  133.101 1.00 34.84 ? 1598 HOH   A O     1 
HETATM 18496 O  O     . HOH   Z  11 .    ? -42.702 61.300  99.829  1.00 25.43 ? 1599 HOH   A O     1 
HETATM 18497 O  O     . HOH   Z  11 .    ? -38.617 65.397  96.149  1.00 28.98 ? 1600 HOH   A O     1 
HETATM 18498 O  O     . HOH   Z  11 .    ? -14.589 48.705  75.466  1.00 32.12 ? 1601 HOH   A O     1 
HETATM 18499 O  O     . HOH   Z  11 .    ? -52.935 63.746  98.021  1.00 20.56 ? 1602 HOH   A O     1 
HETATM 18500 O  O     . HOH   Z  11 .    ? -44.699 63.440  81.121  1.00 17.09 ? 1603 HOH   A O     1 
HETATM 18501 O  O     . HOH   Z  11 .    ? -56.819 32.077  80.009  1.00 32.95 ? 1604 HOH   A O     1 
HETATM 18502 O  O     . HOH   Z  11 .    ? -36.645 63.431  95.688  1.00 27.14 ? 1605 HOH   A O     1 
HETATM 18503 O  O     . HOH   Z  11 .    ? -67.252 60.189  69.558  1.00 29.53 ? 1606 HOH   A O     1 
HETATM 18504 O  O     . HOH   Z  11 .    ? 4.012   58.064  104.458 1.00 20.97 ? 1607 HOH   A O     1 
HETATM 18505 O  O     . HOH   Z  11 .    ? -30.633 73.033  98.229  1.00 38.25 ? 1608 HOH   A O     1 
HETATM 18506 O  O     . HOH   Z  11 .    ? -34.340 76.670  95.795  1.00 32.00 ? 1609 HOH   A O     1 
HETATM 18507 O  O     . HOH   Z  11 .    ? -35.215 76.399  91.699  1.00 32.51 ? 1610 HOH   A O     1 
HETATM 18508 O  O     . HOH   Z  11 .    ? -48.412 81.282  84.707  1.00 35.85 ? 1611 HOH   A O     1 
HETATM 18509 O  O     . HOH   Z  11 .    ? -26.926 89.439  77.219  1.00 29.15 ? 1612 HOH   A O     1 
HETATM 18510 O  O     . HOH   Z  11 .    ? -40.927 49.141  63.665  1.00 26.75 ? 1613 HOH   A O     1 
HETATM 18511 O  O     . HOH   Z  11 .    ? -23.729 83.163  111.585 1.00 22.07 ? 1614 HOH   A O     1 
HETATM 18512 O  O     . HOH   Z  11 .    ? -16.236 91.447  104.039 1.00 36.53 ? 1615 HOH   A O     1 
HETATM 18513 O  O     . HOH   Z  11 .    ? 18.103  59.113  95.216  1.00 31.56 ? 1616 HOH   A O     1 
HETATM 18514 O  O     . HOH   Z  11 .    ? -59.540 40.118  78.407  1.00 40.93 ? 1617 HOH   A O     1 
HETATM 18515 O  O     . HOH   Z  11 .    ? -16.666 55.912  111.905 1.00 32.91 ? 1618 HOH   A O     1 
HETATM 18516 O  O     . HOH   Z  11 .    ? -11.860 71.897  76.302  1.00 31.84 ? 1619 HOH   A O     1 
HETATM 18517 O  O     . HOH   Z  11 .    ? -14.725 64.066  98.988  1.00 25.31 ? 1620 HOH   A O     1 
HETATM 18518 O  O     . HOH   Z  11 .    ? -44.366 41.536  103.834 1.00 34.62 ? 1621 HOH   A O     1 
HETATM 18519 O  O     . HOH   Z  11 .    ? -44.355 73.862  74.680  1.00 26.61 ? 1622 HOH   A O     1 
HETATM 18520 O  O     . HOH   Z  11 .    ? -50.594 52.212  63.637  1.00 23.61 ? 1623 HOH   A O     1 
HETATM 18521 O  O     . HOH   Z  11 .    ? -70.057 61.159  84.854  1.00 35.57 ? 1624 HOH   A O     1 
HETATM 18522 O  O     . HOH   Z  11 .    ? -34.157 69.447  75.945  1.00 29.29 ? 1625 HOH   A O     1 
HETATM 18523 O  O     . HOH   Z  11 .    ? 10.934  67.678  116.127 1.00 30.12 ? 1626 HOH   A O     1 
HETATM 18524 O  O     . HOH   Z  11 .    ? -30.060 63.119  91.538  1.00 34.63 ? 1627 HOH   A O     1 
HETATM 18525 O  O     . HOH   Z  11 .    ? -20.318 91.048  108.667 1.00 27.18 ? 1628 HOH   A O     1 
HETATM 18526 O  O     . HOH   Z  11 .    ? -60.272 51.152  61.945  1.00 35.36 ? 1629 HOH   A O     1 
HETATM 18527 O  O     . HOH   Z  11 .    ? -52.301 49.014  62.481  1.00 35.26 ? 1630 HOH   A O     1 
HETATM 18528 O  O     . HOH   Z  11 .    ? -5.503  77.805  94.532  1.00 24.92 ? 1631 HOH   A O     1 
HETATM 18529 O  O     . HOH   Z  11 .    ? -21.997 43.009  60.485  1.00 36.82 ? 1632 HOH   A O     1 
HETATM 18530 O  O     . HOH   Z  11 .    ? -49.947 56.822  71.442  1.00 25.01 ? 1633 HOH   A O     1 
HETATM 18531 O  O     . HOH   Z  11 .    ? -10.762 63.286  72.366  1.00 30.87 ? 1634 HOH   A O     1 
HETATM 18532 O  O     . HOH   Z  11 .    ? -55.586 36.889  75.945  1.00 30.77 ? 1635 HOH   A O     1 
HETATM 18533 O  O     . HOH   Z  11 .    ? -57.526 57.961  100.825 1.00 25.77 ? 1636 HOH   A O     1 
HETATM 18534 O  O     . HOH   Z  11 .    ? -37.440 30.783  66.027  1.00 45.03 ? 1637 HOH   A O     1 
HETATM 18535 O  O     . HOH   Z  11 .    ? -5.062  54.698  107.815 1.00 20.96 ? 1638 HOH   A O     1 
HETATM 18536 O  O     . HOH   Z  11 .    ? -18.277 79.513  126.884 1.00 27.39 ? 1639 HOH   A O     1 
HETATM 18537 O  O     . HOH   Z  11 .    ? -21.927 52.983  103.967 1.00 36.40 ? 1640 HOH   A O     1 
HETATM 18538 O  O     . HOH   Z  11 .    ? -54.010 76.184  93.946  1.00 38.24 ? 1641 HOH   A O     1 
HETATM 18539 O  O     . HOH   Z  11 .    ? -22.932 67.195  97.075  1.00 23.01 ? 1642 HOH   A O     1 
HETATM 18540 O  O     . HOH   Z  11 .    ? -21.837 88.857  108.625 1.00 25.62 ? 1643 HOH   A O     1 
HETATM 18541 O  O     . HOH   Z  11 .    ? -31.390 71.863  82.072  1.00 33.51 ? 1644 HOH   A O     1 
HETATM 18542 O  O     . HOH   Z  11 .    ? 5.685   63.117  96.798  1.00 21.45 ? 1645 HOH   A O     1 
HETATM 18543 O  O     . HOH   Z  11 .    ? -44.770 59.289  54.910  1.00 32.71 ? 1646 HOH   A O     1 
HETATM 18544 O  O     . HOH   Z  11 .    ? -58.181 72.286  79.931  1.00 35.18 ? 1647 HOH   A O     1 
HETATM 18545 O  O     . HOH   Z  11 .    ? -36.491 58.997  93.827  1.00 17.72 ? 1648 HOH   A O     1 
HETATM 18546 O  O     . HOH   Z  11 .    ? -6.287  54.822  104.861 1.00 32.06 ? 1649 HOH   A O     1 
HETATM 18547 O  O     . HOH   Z  11 .    ? -45.717 65.288  91.487  1.00 17.61 ? 1650 HOH   A O     1 
HETATM 18548 O  O     . HOH   Z  11 .    ? -1.268  83.836  114.724 1.00 32.13 ? 1651 HOH   A O     1 
HETATM 18549 O  O     . HOH   Z  11 .    ? -24.236 59.640  121.176 1.00 35.65 ? 1652 HOH   A O     1 
HETATM 18550 O  O     . HOH   Z  11 .    ? 20.622  58.568  110.572 1.00 30.95 ? 1653 HOH   A O     1 
HETATM 18551 O  O     . HOH   Z  11 .    ? -28.159 62.103  101.777 1.00 18.83 ? 1654 HOH   A O     1 
HETATM 18552 O  O     . HOH   Z  11 .    ? -17.987 82.675  96.223  1.00 20.65 ? 1655 HOH   A O     1 
HETATM 18553 O  O     . HOH   Z  11 .    ? -43.021 85.344  97.065  1.00 26.81 ? 1656 HOH   A O     1 
HETATM 18554 O  O     . HOH   Z  11 .    ? -4.155  70.187  106.344 1.00 29.68 ? 1657 HOH   A O     1 
HETATM 18555 O  O     . HOH   Z  11 .    ? -27.063 53.875  109.251 1.00 29.18 ? 1658 HOH   A O     1 
HETATM 18556 O  O     . HOH   Z  11 .    ? -34.670 80.535  119.949 1.00 26.43 ? 1659 HOH   A O     1 
HETATM 18557 O  O     . HOH   Z  11 .    ? 9.273   57.195  96.960  1.00 30.04 ? 1660 HOH   A O     1 
HETATM 18558 O  O     . HOH   Z  11 .    ? -24.472 92.958  104.756 1.00 37.08 ? 1661 HOH   A O     1 
HETATM 18559 O  O     . HOH   Z  11 .    ? -41.328 85.826  113.333 1.00 28.64 ? 1662 HOH   A O     1 
HETATM 18560 O  O     . HOH   Z  11 .    ? -38.777 49.527  102.055 1.00 29.51 ? 1663 HOH   A O     1 
HETATM 18561 O  O     . HOH   Z  11 .    ? -35.517 51.877  85.005  1.00 20.44 ? 1664 HOH   A O     1 
HETATM 18562 O  O     . HOH   Z  11 .    ? -8.629  80.587  74.292  1.00 30.49 ? 1665 HOH   A O     1 
HETATM 18563 O  O     . HOH   Z  11 .    ? -12.299 79.439  94.128  1.00 18.65 ? 1666 HOH   A O     1 
HETATM 18564 O  O     . HOH   Z  11 .    ? -18.940 70.152  87.331  1.00 26.29 ? 1667 HOH   A O     1 
HETATM 18565 O  O     . HOH   Z  11 .    ? -21.215 56.929  53.230  1.00 36.77 ? 1668 HOH   A O     1 
HETATM 18566 O  O     . HOH   Z  11 .    ? -42.340 47.702  80.805  1.00 21.61 ? 1669 HOH   A O     1 
HETATM 18567 O  O     . HOH   Z  11 .    ? -45.232 65.530  52.630  1.00 36.29 ? 1670 HOH   A O     1 
HETATM 18568 O  O     . HOH   Z  11 .    ? -23.930 63.556  91.312  1.00 22.18 ? 1671 HOH   A O     1 
HETATM 18569 O  O     . HOH   Z  11 .    ? -65.740 59.042  75.577  1.00 21.80 ? 1672 HOH   A O     1 
HETATM 18570 O  O     . HOH   Z  11 .    ? -35.649 39.817  84.110  1.00 38.88 ? 1673 HOH   A O     1 
HETATM 18571 O  O     . HOH   Z  11 .    ? -3.873  57.786  72.476  1.00 23.09 ? 1674 HOH   A O     1 
HETATM 18572 O  O     . HOH   Z  11 .    ? -32.897 70.372  99.887  1.00 38.71 ? 1675 HOH   A O     1 
HETATM 18573 O  O     . HOH   Z  11 .    ? -16.243 75.576  105.601 1.00 21.42 ? 1676 HOH   A O     1 
HETATM 18574 O  O     . HOH   Z  11 .    ? -23.392 54.504  101.004 1.00 27.14 ? 1677 HOH   A O     1 
HETATM 18575 O  O     . HOH   Z  11 .    ? 23.228  65.990  114.319 1.00 28.22 ? 1678 HOH   A O     1 
HETATM 18576 O  O     . HOH   Z  11 .    ? -26.391 50.375  96.243  1.00 30.10 ? 1679 HOH   A O     1 
HETATM 18577 O  O     . HOH   Z  11 .    ? -60.173 47.180  88.310  1.00 27.30 ? 1680 HOH   A O     1 
HETATM 18578 O  O     . HOH   Z  11 .    ? -46.519 67.427  59.423  1.00 25.73 ? 1681 HOH   A O     1 
HETATM 18579 O  O     . HOH   Z  11 .    ? -20.136 78.731  69.821  1.00 25.30 ? 1682 HOH   A O     1 
HETATM 18580 O  O     . HOH   Z  11 .    ? -16.404 60.366  106.039 1.00 25.81 ? 1683 HOH   A O     1 
HETATM 18581 O  O     . HOH   Z  11 .    ? -0.915  58.530  110.389 1.00 34.16 ? 1684 HOH   A O     1 
HETATM 18582 O  O     . HOH   Z  11 .    ? -46.045 43.610  55.468  1.00 39.74 ? 1685 HOH   A O     1 
HETATM 18583 O  O     . HOH   Z  11 .    ? -56.721 46.103  70.774  1.00 22.02 ? 1686 HOH   A O     1 
HETATM 18584 O  O     . HOH   Z  11 .    ? -28.619 57.266  59.561  1.00 34.78 ? 1687 HOH   A O     1 
HETATM 18585 O  O     . HOH   Z  11 .    ? -4.100  73.191  116.445 1.00 26.24 ? 1688 HOH   A O     1 
HETATM 18586 O  O     . HOH   Z  11 .    ? -21.093 55.164  94.629  1.00 35.22 ? 1689 HOH   A O     1 
HETATM 18587 O  O     . HOH   Z  11 .    ? -38.911 52.687  105.093 1.00 37.16 ? 1690 HOH   A O     1 
HETATM 18588 O  O     . HOH   Z  11 .    ? -35.843 37.561  83.152  1.00 36.37 ? 1691 HOH   A O     1 
HETATM 18589 O  O     . HOH   Z  11 .    ? -46.263 30.773  85.099  1.00 29.50 ? 1692 HOH   A O     1 
HETATM 18590 O  O     . HOH   Z  11 .    ? -15.147 90.217  98.035  1.00 38.94 ? 1693 HOH   A O     1 
HETATM 18591 O  O     . HOH   Z  11 .    ? -44.041 62.411  69.723  1.00 22.50 ? 1694 HOH   A O     1 
HETATM 18592 O  O     . HOH   Z  11 .    ? -19.897 93.971  111.235 1.00 33.11 ? 1695 HOH   A O     1 
HETATM 18593 O  O     . HOH   Z  11 .    ? -49.788 68.651  91.705  1.00 22.27 ? 1696 HOH   A O     1 
HETATM 18594 O  O     . HOH   Z  11 .    ? -51.664 73.057  105.270 1.00 29.77 ? 1697 HOH   A O     1 
HETATM 18595 O  O     . HOH   Z  11 .    ? -18.834 61.506  85.052  1.00 23.27 ? 1698 HOH   A O     1 
HETATM 18596 O  O     . HOH   Z  11 .    ? -25.813 63.849  104.406 1.00 22.33 ? 1699 HOH   A O     1 
HETATM 18597 O  O     . HOH   Z  11 .    ? -36.954 85.572  85.520  1.00 34.22 ? 1700 HOH   A O     1 
HETATM 18598 O  O     . HOH   Z  11 .    ? -45.809 76.133  94.074  1.00 26.37 ? 1701 HOH   A O     1 
HETATM 18599 O  O     . HOH   Z  11 .    ? -59.624 60.901  75.615  1.00 17.72 ? 1702 HOH   A O     1 
HETATM 18600 O  O     . HOH   Z  11 .    ? -34.639 66.590  101.256 1.00 24.18 ? 1703 HOH   A O     1 
HETATM 18601 O  O     . HOH   Z  11 .    ? -39.225 61.493  74.250  1.00 34.27 ? 1704 HOH   A O     1 
HETATM 18602 O  O     . HOH   Z  11 .    ? -13.270 55.346  102.972 1.00 34.85 ? 1705 HOH   A O     1 
HETATM 18603 O  O     . HOH   Z  11 .    ? 0.964   91.611  110.346 1.00 31.82 ? 1706 HOH   A O     1 
HETATM 18604 O  O     . HOH   Z  11 .    ? -18.098 57.492  96.888  1.00 21.03 ? 1707 HOH   A O     1 
HETATM 18605 O  O     . HOH   Z  11 .    ? -45.262 63.574  104.816 1.00 37.89 ? 1708 HOH   A O     1 
HETATM 18606 O  O     . HOH   Z  11 .    ? -35.132 40.600  91.739  1.00 25.65 ? 1709 HOH   A O     1 
HETATM 18607 O  O     . HOH   Z  11 .    ? -42.529 60.912  73.823  1.00 32.02 ? 1710 HOH   A O     1 
HETATM 18608 O  O     . HOH   Z  11 .    ? -9.259  45.148  55.528  1.00 33.12 ? 1711 HOH   A O     1 
HETATM 18609 O  O     . HOH   Z  11 .    ? -12.538 77.346  90.617  1.00 17.69 ? 1712 HOH   A O     1 
HETATM 18610 O  O     . HOH   Z  11 .    ? -32.055 61.817  111.199 1.00 24.42 ? 1713 HOH   A O     1 
HETATM 18611 O  O     . HOH   Z  11 .    ? -0.467  66.207  93.999  1.00 35.88 ? 1714 HOH   A O     1 
HETATM 18612 O  O     . HOH   Z  11 .    ? 15.004  76.091  93.597  1.00 37.84 ? 1715 HOH   A O     1 
HETATM 18613 O  O     . HOH   Z  11 .    ? -19.686 55.078  106.697 1.00 31.37 ? 1716 HOH   A O     1 
HETATM 18614 O  O     . HOH   Z  11 .    ? -26.224 56.603  107.566 1.00 22.06 ? 1717 HOH   A O     1 
HETATM 18615 O  O     . HOH   Z  11 .    ? -47.225 60.362  84.845  1.00 16.13 ? 1718 HOH   A O     1 
HETATM 18616 O  O     . HOH   Z  11 .    ? -8.075  87.639  92.693  1.00 41.40 ? 1719 HOH   A O     1 
HETATM 18617 O  O     . HOH   Z  11 .    ? -48.939 83.370  108.524 1.00 33.46 ? 1720 HOH   A O     1 
HETATM 18618 O  O     . HOH   Z  11 .    ? -6.982  42.107  65.905  1.00 25.69 ? 1721 HOH   A O     1 
HETATM 18619 O  O     . HOH   Z  11 .    ? -36.703 61.754  74.519  1.00 33.89 ? 1722 HOH   A O     1 
HETATM 18620 O  O     . HOH   Z  11 .    ? 15.111  83.177  110.661 1.00 26.19 ? 1723 HOH   A O     1 
HETATM 18621 O  O     . HOH   Z  11 .    ? -35.462 73.291  83.268  1.00 26.02 ? 1724 HOH   A O     1 
HETATM 18622 O  O     . HOH   Z  11 .    ? -11.365 58.750  125.155 1.00 38.13 ? 1725 HOH   A O     1 
HETATM 18623 O  O     . HOH   Z  11 .    ? -22.812 59.007  75.437  1.00 29.23 ? 1726 HOH   A O     1 
HETATM 18624 O  O     . HOH   Z  11 .    ? -6.607  66.784  73.720  1.00 42.63 ? 1727 HOH   A O     1 
HETATM 18625 O  O     . HOH   Z  11 .    ? -31.392 60.206  105.101 1.00 26.29 ? 1728 HOH   A O     1 
HETATM 18626 O  O     . HOH   Z  11 .    ? 17.002  71.629  118.683 1.00 31.46 ? 1729 HOH   A O     1 
HETATM 18627 O  O     . HOH   Z  11 .    ? -44.020 69.361  108.633 1.00 36.47 ? 1730 HOH   A O     1 
HETATM 18628 O  O     . HOH   Z  11 .    ? -31.024 60.928  90.191  1.00 22.13 ? 1731 HOH   A O     1 
HETATM 18629 O  O     . HOH   Z  11 .    ? -3.894  78.382  122.125 1.00 25.27 ? 1732 HOH   A O     1 
HETATM 18630 O  O     . HOH   Z  11 .    ? -19.695 85.159  75.201  1.00 31.73 ? 1733 HOH   A O     1 
HETATM 18631 O  O     . HOH   Z  11 .    ? -23.383 63.848  105.788 1.00 18.41 ? 1734 HOH   A O     1 
HETATM 18632 O  O     . HOH   Z  11 .    ? 5.082   55.311  96.419  1.00 26.43 ? 1735 HOH   A O     1 
HETATM 18633 O  O     . HOH   Z  11 .    ? -13.181 94.337  130.080 1.00 48.17 ? 1736 HOH   A O     1 
HETATM 18634 O  O     . HOH   Z  11 .    ? -0.644  70.320  95.669  1.00 35.32 ? 1737 HOH   A O     1 
HETATM 18635 O  O     . HOH   Z  11 .    ? -45.732 78.348  95.788  1.00 21.12 ? 1738 HOH   A O     1 
HETATM 18636 O  O     . HOH   Z  11 .    ? -66.665 68.150  71.811  1.00 34.35 ? 1739 HOH   A O     1 
HETATM 18637 O  O     . HOH   Z  11 .    ? -18.927 54.054  94.308  1.00 40.04 ? 1740 HOH   A O     1 
HETATM 18638 O  O     . HOH   Z  11 .    ? 7.267   57.654  111.864 1.00 32.70 ? 1741 HOH   A O     1 
HETATM 18639 O  O     . HOH   Z  11 .    ? -52.281 78.332  87.341  1.00 29.51 ? 1742 HOH   A O     1 
HETATM 18640 O  O     . HOH   Z  11 .    ? -31.890 88.630  94.820  1.00 22.69 ? 1743 HOH   A O     1 
HETATM 18641 O  O     . HOH   Z  11 .    ? -33.276 49.018  74.862  1.00 29.97 ? 1744 HOH   A O     1 
HETATM 18642 O  O     . HOH   Z  11 .    ? -32.519 82.288  97.601  1.00 29.93 ? 1745 HOH   A O     1 
HETATM 18643 O  O     . HOH   Z  11 .    ? 16.601  58.036  102.314 1.00 22.84 ? 1746 HOH   A O     1 
HETATM 18644 O  O     . HOH   Z  11 .    ? -3.483  56.787  95.047  1.00 38.88 ? 1747 HOH   A O     1 
HETATM 18645 O  O     . HOH   Z  11 .    ? -26.566 97.186  88.664  1.00 36.48 ? 1748 HOH   A O     1 
HETATM 18646 O  O     . HOH   Z  11 .    ? -57.494 64.757  90.620  1.00 30.06 ? 1749 HOH   A O     1 
HETATM 18647 O  O     . HOH   Z  11 .    ? -33.843 97.663  97.720  1.00 41.51 ? 1750 HOH   A O     1 
HETATM 18648 O  O     . HOH   Z  11 .    ? -63.062 54.110  71.875  1.00 27.02 ? 1751 HOH   A O     1 
HETATM 18649 O  O     . HOH   Z  11 .    ? -62.230 54.972  63.016  1.00 34.43 ? 1752 HOH   A O     1 
HETATM 18650 O  O     . HOH   Z  11 .    ? -1.423  58.317  96.208  1.00 33.73 ? 1753 HOH   A O     1 
HETATM 18651 O  O     . HOH   Z  11 .    ? 10.767  57.437  105.311 1.00 28.04 ? 1754 HOH   A O     1 
HETATM 18652 O  O     . HOH   Z  11 .    ? -43.914 89.086  112.622 1.00 42.73 ? 1755 HOH   A O     1 
HETATM 18653 O  O     . HOH   Z  11 .    ? -9.770  74.422  103.760 1.00 20.47 ? 1756 HOH   A O     1 
HETATM 18654 O  O     . HOH   Z  11 .    ? -53.339 39.802  65.745  1.00 37.86 ? 1757 HOH   A O     1 
HETATM 18655 O  O     . HOH   Z  11 .    ? -61.583 70.438  82.673  1.00 21.39 ? 1758 HOH   A O     1 
HETATM 18656 O  O     . HOH   Z  11 .    ? -9.745  40.086  60.988  1.00 38.98 ? 1759 HOH   A O     1 
HETATM 18657 O  O     . HOH   Z  11 .    ? -12.341 64.400  129.353 1.00 34.11 ? 1760 HOH   A O     1 
HETATM 18658 O  O     . HOH   Z  11 .    ? -53.602 43.274  65.219  1.00 37.42 ? 1761 HOH   A O     1 
HETATM 18659 O  O     . HOH   Z  11 .    ? -16.140 94.746  91.028  1.00 38.80 ? 1762 HOH   A O     1 
HETATM 18660 O  O     . HOH   Z  11 .    ? -65.072 54.591  90.598  1.00 34.90 ? 1763 HOH   A O     1 
HETATM 18661 O  O     . HOH   Z  11 .    ? -61.981 61.908  67.949  1.00 25.10 ? 1764 HOH   A O     1 
HETATM 18662 O  O     . HOH   Z  11 .    ? -1.459  79.403  99.448  1.00 27.43 ? 1765 HOH   A O     1 
HETATM 18663 O  O     . HOH   Z  11 .    ? -34.235 75.599  82.812  1.00 27.45 ? 1766 HOH   A O     1 
HETATM 18664 O  O     . HOH   Z  11 .    ? -3.020  62.662  77.230  1.00 22.50 ? 1767 HOH   A O     1 
HETATM 18665 O  O     . HOH   Z  11 .    ? -31.886 82.497  75.058  1.00 23.32 ? 1768 HOH   A O     1 
HETATM 18666 O  O     . HOH   Z  11 .    ? 18.510  62.237  94.053  1.00 36.58 ? 1769 HOH   A O     1 
HETATM 18667 O  O     . HOH   Z  11 .    ? -47.523 49.211  95.525  1.00 20.58 ? 1770 HOH   A O     1 
HETATM 18668 O  O     . HOH   Z  11 .    ? -38.537 32.367  96.510  1.00 37.70 ? 1771 HOH   A O     1 
HETATM 18669 O  O     . HOH   Z  11 .    ? -39.382 78.399  99.513  1.00 22.43 ? 1772 HOH   A O     1 
HETATM 18670 O  O     . HOH   Z  11 .    ? -51.141 64.960  94.537  1.00 20.71 ? 1773 HOH   A O     1 
HETATM 18671 O  O     . HOH   Z  11 .    ? -33.917 90.795  121.753 1.00 32.08 ? 1774 HOH   A O     1 
HETATM 18672 O  O     . HOH   Z  11 .    ? -2.541  54.014  104.065 1.00 28.68 ? 1775 HOH   A O     1 
HETATM 18673 O  O     . HOH   Z  11 .    ? -10.659 67.900  107.703 1.00 18.01 ? 1776 HOH   A O     1 
HETATM 18674 O  O     . HOH   Z  11 .    ? -17.067 88.985  98.935  1.00 36.35 ? 1777 HOH   A O     1 
HETATM 18675 O  O     . HOH   Z  11 .    ? -25.737 50.886  104.723 1.00 38.51 ? 1778 HOH   A O     1 
HETATM 18676 O  O     . HOH   Z  11 .    ? -7.634  42.625  61.772  1.00 26.54 ? 1779 HOH   A O     1 
HETATM 18677 O  O     . HOH   Z  11 .    ? 7.969   91.501  112.669 1.00 35.67 ? 1780 HOH   A O     1 
HETATM 18678 O  O     . HOH   Z  11 .    ? -46.455 54.406  89.343  1.00 18.33 ? 1781 HOH   A O     1 
HETATM 18679 O  O     . HOH   Z  11 .    ? -50.186 38.092  99.406  1.00 35.82 ? 1782 HOH   A O     1 
HETATM 18680 O  O     . HOH   Z  11 .    ? -47.285 70.788  110.809 1.00 33.77 ? 1783 HOH   A O     1 
HETATM 18681 O  O     . HOH   Z  11 .    ? -60.551 68.143  93.836  1.00 39.74 ? 1784 HOH   A O     1 
HETATM 18682 O  O     . HOH   Z  11 .    ? -31.247 84.346  98.861  1.00 23.30 ? 1785 HOH   A O     1 
HETATM 18683 O  O     . HOH   Z  11 .    ? -23.740 65.574  129.464 1.00 42.60 ? 1786 HOH   A O     1 
HETATM 18684 O  O     . HOH   Z  11 .    ? -1.811  80.193  87.803  1.00 39.34 ? 1787 HOH   A O     1 
HETATM 18685 O  O     . HOH   Z  11 .    ? -3.252  90.077  108.295 1.00 26.14 ? 1788 HOH   A O     1 
HETATM 18686 O  O     . HOH   Z  11 .    ? -32.552 60.769  73.102  1.00 35.52 ? 1789 HOH   A O     1 
HETATM 18687 O  O     . HOH   Z  11 .    ? -22.428 96.863  78.462  1.00 41.71 ? 1790 HOH   A O     1 
HETATM 18688 O  O     . HOH   Z  11 .    ? -12.766 89.905  101.231 1.00 33.36 ? 1791 HOH   A O     1 
HETATM 18689 O  O     . HOH   Z  11 .    ? -51.050 69.962  93.602  1.00 21.15 ? 1792 HOH   A O     1 
HETATM 18690 O  O     . HOH   Z  11 .    ? 22.837  73.030  97.869  1.00 35.68 ? 1793 HOH   A O     1 
HETATM 18691 O  O     . HOH   Z  11 .    ? 1.681   73.266  115.506 1.00 31.18 ? 1794 HOH   A O     1 
HETATM 18692 O  O     . HOH   Z  11 .    ? -32.279 93.138  103.454 1.00 26.91 ? 1795 HOH   A O     1 
HETATM 18693 O  O     . HOH   Z  11 .    ? -19.853 59.728  78.708  1.00 32.06 ? 1796 HOH   A O     1 
HETATM 18694 O  O     . HOH   Z  11 .    ? 11.723  75.669  94.408  1.00 36.99 ? 1797 HOH   A O     1 
HETATM 18695 O  O     . HOH   Z  11 .    ? -11.192 92.446  123.669 1.00 37.63 ? 1798 HOH   A O     1 
HETATM 18696 O  O     . HOH   Z  11 .    ? -4.488  71.318  126.385 1.00 39.93 ? 1799 HOH   A O     1 
HETATM 18697 O  O     . HOH   Z  11 .    ? -27.811 55.994  90.217  1.00 30.08 ? 1800 HOH   A O     1 
HETATM 18698 O  O     . HOH   Z  11 .    ? 5.545   74.132  95.205  1.00 41.51 ? 1801 HOH   A O     1 
HETATM 18699 O  O     . HOH   Z  11 .    ? -27.444 58.855  75.856  1.00 37.56 ? 1802 HOH   A O     1 
HETATM 18700 O  O     . HOH   Z  11 .    ? -46.297 32.183  69.959  1.00 35.69 ? 1803 HOH   A O     1 
HETATM 18701 O  O     . HOH   Z  11 .    ? -8.703  60.248  106.709 1.00 21.11 ? 1804 HOH   A O     1 
HETATM 18702 O  O     . HOH   Z  11 .    ? -30.180 71.471  89.064  1.00 40.64 ? 1805 HOH   A O     1 
HETATM 18703 O  O     . HOH   Z  11 .    ? -13.280 59.287  122.054 1.00 27.83 ? 1806 HOH   A O     1 
HETATM 18704 O  O     . HOH   Z  11 .    ? -15.973 68.153  96.327  1.00 16.76 ? 1807 HOH   A O     1 
HETATM 18705 O  O     . HOH   Z  11 .    ? -0.331  52.950  62.700  1.00 27.33 ? 1808 HOH   A O     1 
HETATM 18706 O  O     . HOH   Z  11 .    ? 4.912   67.305  95.497  1.00 28.04 ? 1809 HOH   A O     1 
HETATM 18707 O  O     . HOH   Z  11 .    ? -44.138 55.803  94.699  1.00 17.05 ? 1810 HOH   A O     1 
HETATM 18708 O  O     . HOH   Z  11 .    ? -0.548  83.801  109.110 1.00 28.12 ? 1811 HOH   A O     1 
HETATM 18709 O  O     . HOH   Z  11 .    ? 10.781  54.907  108.225 1.00 38.37 ? 1812 HOH   A O     1 
HETATM 18710 O  O     . HOH   Z  11 .    ? -47.870 57.792  85.963  1.00 16.24 ? 1813 HOH   A O     1 
HETATM 18711 O  O     . HOH   Z  11 .    ? -41.095 71.633  114.026 1.00 29.72 ? 1814 HOH   A O     1 
HETATM 18712 O  O     . HOH   Z  11 .    ? -60.303 61.478  92.392  1.00 23.35 ? 1815 HOH   A O     1 
HETATM 18713 O  O     . HOH   Z  11 .    ? -60.162 63.889  100.639 1.00 39.63 ? 1816 HOH   A O     1 
HETATM 18714 O  O     . HOH   Z  11 .    ? -18.381 60.938  66.553  1.00 26.58 ? 1817 HOH   A O     1 
HETATM 18715 O  O     . HOH   Z  11 .    ? -56.060 55.846  94.704  1.00 20.97 ? 1818 HOH   A O     1 
HETATM 18716 O  O     . HOH   Z  11 .    ? -50.070 32.794  91.290  1.00 36.00 ? 1819 HOH   A O     1 
HETATM 18717 O  O     . HOH   Z  11 .    ? -22.883 55.270  88.269  1.00 36.75 ? 1820 HOH   A O     1 
HETATM 18718 O  O     . HOH   Z  11 .    ? -8.432  93.071  105.403 1.00 25.02 ? 1821 HOH   A O     1 
HETATM 18719 O  O     . HOH   Z  11 .    ? -6.270  70.947  105.771 1.00 29.92 ? 1822 HOH   A O     1 
HETATM 18720 O  O     . HOH   Z  11 .    ? -20.570 100.851 89.193  1.00 38.42 ? 1823 HOH   A O     1 
HETATM 18721 O  O     . HOH   Z  11 .    ? -55.116 29.821  79.561  1.00 34.08 ? 1824 HOH   A O     1 
HETATM 18722 O  O     . HOH   Z  11 .    ? -41.322 28.074  69.859  1.00 38.91 ? 1825 HOH   A O     1 
HETATM 18723 O  O     . HOH   Z  11 .    ? -61.156 53.029  90.857  1.00 26.49 ? 1826 HOH   A O     1 
HETATM 18724 O  O     . HOH   Z  11 .    ? -45.340 62.689  92.273  1.00 17.76 ? 1827 HOH   A O     1 
HETATM 18725 O  O     . HOH   Z  11 .    ? -47.638 85.122  101.511 1.00 34.99 ? 1828 HOH   A O     1 
HETATM 18726 O  O     . HOH   Z  11 .    ? -0.349  77.416  116.588 1.00 28.46 ? 1829 HOH   A O     1 
HETATM 18727 O  O     . HOH   Z  11 .    ? 10.578  67.360  111.408 1.00 35.89 ? 1830 HOH   A O     1 
HETATM 18728 O  O     . HOH   Z  11 .    ? -25.319 62.666  109.675 1.00 22.04 ? 1831 HOH   A O     1 
HETATM 18729 O  O     . HOH   Z  11 .    ? -64.481 44.998  77.753  1.00 35.94 ? 1832 HOH   A O     1 
HETATM 18730 O  O     . HOH   Z  11 .    ? -46.943 49.017  92.813  1.00 19.09 ? 1833 HOH   A O     1 
HETATM 18731 O  O     . HOH   Z  11 .    ? 10.200  63.201  112.464 1.00 32.94 ? 1834 HOH   A O     1 
HETATM 18732 O  O     . HOH   Z  11 .    ? -4.548  82.752  124.543 1.00 38.41 ? 1835 HOH   A O     1 
HETATM 18733 O  O     . HOH   Z  11 .    ? -31.711 59.297  62.731  1.00 33.07 ? 1836 HOH   A O     1 
HETATM 18734 O  O     . HOH   Z  11 .    ? -54.267 47.618  67.037  1.00 28.26 ? 1837 HOH   A O     1 
HETATM 18735 O  O     . HOH   Z  11 .    ? -19.828 76.573  66.950  1.00 39.51 ? 1838 HOH   A O     1 
HETATM 18736 O  O     . HOH   Z  11 .    ? -28.464 77.380  102.858 1.00 35.46 ? 1839 HOH   A O     1 
HETATM 18737 O  O     . HOH   Z  11 .    ? -24.893 88.301  78.860  1.00 26.11 ? 1840 HOH   A O     1 
HETATM 18738 O  O     . HOH   Z  11 .    ? -41.096 90.723  98.297  1.00 25.43 ? 1841 HOH   A O     1 
HETATM 18739 O  O     . HOH   Z  11 .    ? -20.660 47.579  54.503  1.00 34.17 ? 1842 HOH   A O     1 
HETATM 18740 O  O     . HOH   Z  11 .    ? -11.602 88.625  128.418 1.00 35.43 ? 1843 HOH   A O     1 
HETATM 18741 O  O     . HOH   Z  11 .    ? -65.521 69.263  68.987  1.00 31.86 ? 1844 HOH   A O     1 
HETATM 18742 O  O     . HOH   Z  11 .    ? -3.952  79.511  110.441 1.00 29.34 ? 1845 HOH   A O     1 
HETATM 18743 O  O     . HOH   Z  11 .    ? -58.199 65.458  93.968  1.00 27.17 ? 1846 HOH   A O     1 
HETATM 18744 O  O     . HOH   Z  11 .    ? -38.365 50.533  97.986  1.00 26.58 ? 1847 HOH   A O     1 
HETATM 18745 O  O     . HOH   Z  11 .    ? -57.190 60.312  60.767  1.00 20.50 ? 1848 HOH   A O     1 
HETATM 18746 O  O     . HOH   Z  11 .    ? -59.252 52.026  65.836  1.00 21.27 ? 1849 HOH   A O     1 
HETATM 18747 O  O     . HOH   Z  11 .    ? -46.052 29.552  89.080  1.00 37.32 ? 1850 HOH   A O     1 
HETATM 18748 O  O     . HOH   Z  11 .    ? -20.844 70.941  75.307  1.00 23.91 ? 1851 HOH   A O     1 
HETATM 18749 O  O     . HOH   Z  11 .    ? -53.177 56.889  54.897  1.00 32.67 ? 1852 HOH   A O     1 
HETATM 18750 O  O     . HOH   Z  11 .    ? -38.330 61.599  91.449  1.00 19.36 ? 1853 HOH   A O     1 
HETATM 18751 O  O     . HOH   Z  11 .    ? -14.994 67.299  72.739  1.00 23.90 ? 1854 HOH   A O     1 
HETATM 18752 O  O     . HOH   Z  11 .    ? -37.981 41.102  71.205  1.00 28.94 ? 1855 HOH   A O     1 
HETATM 18753 O  O     . HOH   Z  11 .    ? -17.693 59.287  85.946  1.00 32.39 ? 1856 HOH   A O     1 
HETATM 18754 O  O     . HOH   Z  11 .    ? -31.822 89.043  108.261 1.00 30.78 ? 1857 HOH   A O     1 
HETATM 18755 O  O     . HOH   Z  11 .    ? -28.519 62.049  116.410 1.00 24.38 ? 1858 HOH   A O     1 
HETATM 18756 O  O     . HOH   Z  11 .    ? -50.258 66.581  105.950 1.00 30.76 ? 1859 HOH   A O     1 
HETATM 18757 O  O     . HOH   Z  11 .    ? 6.287   90.960  106.034 1.00 32.11 ? 1860 HOH   A O     1 
HETATM 18758 O  O     . HOH   Z  11 .    ? 13.699  86.856  120.352 1.00 37.70 ? 1861 HOH   A O     1 
HETATM 18759 O  O     . HOH   Z  11 .    ? -55.066 47.795  69.569  1.00 23.97 ? 1862 HOH   A O     1 
HETATM 18760 O  O     . HOH   Z  11 .    ? -47.809 64.322  96.455  1.00 22.70 ? 1863 HOH   A O     1 
HETATM 18761 O  O     . HOH   Z  11 .    ? -32.441 59.747  109.053 1.00 31.20 ? 1864 HOH   A O     1 
HETATM 18762 O  O     . HOH   Z  11 .    ? 9.191   55.427  104.453 1.00 28.80 ? 1865 HOH   A O     1 
HETATM 18763 O  O     . HOH   Z  11 .    ? -24.686 88.958  99.550  1.00 22.59 ? 1866 HOH   A O     1 
HETATM 18764 O  O     . HOH   Z  11 .    ? -19.898 88.890  74.708  1.00 35.69 ? 1867 HOH   A O     1 
HETATM 18765 O  O     . HOH   Z  11 .    ? -23.877 61.294  63.324  1.00 31.15 ? 1868 HOH   A O     1 
HETATM 18766 O  O     . HOH   Z  11 .    ? -22.261 95.858  129.200 1.00 42.52 ? 1869 HOH   A O     1 
HETATM 18767 O  O     . HOH   Z  11 .    ? -20.553 81.549  115.421 1.00 20.63 ? 1870 HOH   A O     1 
HETATM 18768 O  O     . HOH   Z  11 .    ? -45.870 72.617  64.032  1.00 19.32 ? 1871 HOH   A O     1 
HETATM 18769 O  O     . HOH   Z  11 .    ? -27.619 70.941  89.680  1.00 28.61 ? 1872 HOH   A O     1 
HETATM 18770 O  O     . HOH   Z  11 .    ? 8.153   92.746  97.934  1.00 42.88 ? 1873 HOH   A O     1 
HETATM 18771 O  O     . HOH   Z  11 .    ? -46.552 66.691  93.564  1.00 19.71 ? 1874 HOH   A O     1 
HETATM 18772 O  O     . HOH   Z  11 .    ? -41.924 67.919  90.746  1.00 19.64 ? 1875 HOH   A O     1 
HETATM 18773 O  O     . HOH   Z  11 .    ? -58.067 37.948  95.464  1.00 32.29 ? 1876 HOH   A O     1 
HETATM 18774 O  O     . HOH   Z  11 .    ? -53.760 55.659  68.171  1.00 18.56 ? 1877 HOH   A O     1 
HETATM 18775 O  O     . HOH   Z  11 .    ? -42.439 77.998  75.497  1.00 27.94 ? 1878 HOH   A O     1 
HETATM 18776 O  O     . HOH   Z  11 .    ? -18.966 59.794  69.623  1.00 23.71 ? 1879 HOH   A O     1 
HETATM 18777 O  O     . HOH   Z  11 .    ? -38.266 36.589  82.239  1.00 35.50 ? 1880 HOH   A O     1 
HETATM 18778 O  O     . HOH   Z  11 .    ? -18.425 39.663  68.069  1.00 40.74 ? 1881 HOH   A O     1 
HETATM 18779 O  O     . HOH   Z  11 .    ? -3.222  77.974  100.943 1.00 24.02 ? 1882 HOH   A O     1 
HETATM 18780 O  O     . HOH   Z  11 .    ? -60.873 68.735  68.326  1.00 23.08 ? 1883 HOH   A O     1 
HETATM 18781 O  O     . HOH   Z  11 .    ? -20.014 86.790  91.127  1.00 23.28 ? 1884 HOH   A O     1 
HETATM 18782 O  O     . HOH   Z  11 .    ? -25.607 94.193  78.011  1.00 36.00 ? 1885 HOH   A O     1 
HETATM 18783 O  O     . HOH   Z  11 .    ? -28.128 64.953  64.039  1.00 45.20 ? 1886 HOH   A O     1 
HETATM 18784 O  O     . HOH   Z  11 .    ? -48.097 66.293  57.630  1.00 26.00 ? 1887 HOH   A O     1 
HETATM 18785 O  O     . HOH   Z  11 .    ? -5.889  76.226  110.718 1.00 20.60 ? 1888 HOH   A O     1 
HETATM 18786 O  O     . HOH   Z  11 .    ? -48.240 75.250  95.226  1.00 22.80 ? 1889 HOH   A O     1 
HETATM 18787 O  O     . HOH   Z  11 .    ? -27.374 82.340  129.286 1.00 32.03 ? 1890 HOH   A O     1 
HETATM 18788 O  O     . HOH   Z  11 .    ? -2.199  62.998  112.972 1.00 35.06 ? 1891 HOH   A O     1 
HETATM 18789 O  O     . HOH   Z  11 .    ? 14.053  82.243  113.552 1.00 26.70 ? 1892 HOH   A O     1 
HETATM 18790 O  O     . HOH   Z  11 .    ? -12.574 81.831  72.344  1.00 38.45 ? 1893 HOH   A O     1 
HETATM 18791 O  O     . HOH   Z  11 .    ? -49.547 75.989  101.203 1.00 23.52 ? 1894 HOH   A O     1 
HETATM 18792 O  O     . HOH   Z  11 .    ? 2.516   84.079  126.259 1.00 37.41 ? 1895 HOH   A O     1 
HETATM 18793 O  O     . HOH   Z  11 .    ? -1.626  77.886  120.807 1.00 29.34 ? 1896 HOH   A O     1 
HETATM 18794 O  O     . HOH   Z  11 .    ? -30.971 59.775  59.892  1.00 42.02 ? 1897 HOH   A O     1 
HETATM 18795 O  O     . HOH   Z  11 .    ? -64.547 59.700  92.527  1.00 34.45 ? 1898 HOH   A O     1 
HETATM 18796 O  O     . HOH   Z  11 .    ? -14.029 42.099  70.696  1.00 32.34 ? 1899 HOH   A O     1 
HETATM 18797 O  O     . HOH   Z  11 .    ? -5.861  65.269  113.778 1.00 22.44 ? 1900 HOH   A O     1 
HETATM 18798 O  O     . HOH   Z  11 .    ? -38.539 62.910  55.269  1.00 39.73 ? 1901 HOH   A O     1 
HETATM 18799 O  O     . HOH   Z  11 .    ? -46.192 56.095  87.100  1.00 16.66 ? 1902 HOH   A O     1 
HETATM 18800 O  O     . HOH   Z  11 .    ? -54.309 37.634  88.907  1.00 28.44 ? 1903 HOH   A O     1 
HETATM 18801 O  O     . HOH   Z  11 .    ? -29.023 67.027  96.125  1.00 41.47 ? 1904 HOH   A O     1 
HETATM 18802 O  O     . HOH   Z  11 .    ? -30.205 81.338  122.508 1.00 31.93 ? 1905 HOH   A O     1 
HETATM 18803 O  O     . HOH   Z  11 .    ? -0.992  73.393  88.479  1.00 37.08 ? 1906 HOH   A O     1 
HETATM 18804 O  O     . HOH   Z  11 .    ? -4.007  76.411  124.204 1.00 30.88 ? 1907 HOH   A O     1 
HETATM 18805 O  O     . HOH   Z  11 .    ? -41.392 64.233  103.274 1.00 22.93 ? 1908 HOH   A O     1 
HETATM 18806 O  O     . HOH   Z  11 .    ? -63.717 52.985  89.486  1.00 32.99 ? 1909 HOH   A O     1 
HETATM 18807 O  O     . HOH   Z  11 .    ? -41.648 70.899  94.951  1.00 25.99 ? 1910 HOH   A O     1 
HETATM 18808 O  O     . HOH   Z  11 .    ? -34.630 77.660  84.639  1.00 25.07 ? 1911 HOH   A O     1 
HETATM 18809 O  O     . HOH   Z  11 .    ? -37.858 65.568  88.099  1.00 34.49 ? 1912 HOH   A O     1 
HETATM 18810 O  O     . HOH   Z  11 .    ? -49.734 49.154  99.432  1.00 24.73 ? 1913 HOH   A O     1 
HETATM 18811 O  O     . HOH   Z  11 .    ? -6.881  70.666  93.641  1.00 23.94 ? 1914 HOH   A O     1 
HETATM 18812 O  O     . HOH   Z  11 .    ? -31.034 91.516  80.203  1.00 32.68 ? 1915 HOH   A O     1 
HETATM 18813 O  O     . HOH   Z  11 .    ? 20.578  62.165  98.417  1.00 27.07 ? 1916 HOH   A O     1 
HETATM 18814 O  O     . HOH   Z  11 .    ? -8.615  65.218  113.556 1.00 19.39 ? 1917 HOH   A O     1 
HETATM 18815 O  O     . HOH   Z  11 .    ? -30.721 91.105  106.775 1.00 27.40 ? 1918 HOH   A O     1 
HETATM 18816 O  O     . HOH   Z  11 .    ? -48.835 33.698  89.025  1.00 37.46 ? 1919 HOH   A O     1 
HETATM 18817 O  O     . HOH   Z  11 .    ? -6.948  85.161  86.201  1.00 37.86 ? 1920 HOH   A O     1 
HETATM 18818 O  O     . HOH   Z  11 .    ? -5.444  68.054  77.527  1.00 32.14 ? 1921 HOH   A O     1 
HETATM 18819 O  O     . HOH   Z  11 .    ? -32.572 92.480  109.927 1.00 32.88 ? 1922 HOH   A O     1 
HETATM 18820 O  O     . HOH   Z  11 .    ? -52.509 54.078  100.002 1.00 28.02 ? 1923 HOH   A O     1 
HETATM 18821 O  O     . HOH   Z  11 .    ? -3.376  57.687  67.865  1.00 34.09 ? 1924 HOH   A O     1 
HETATM 18822 O  O     . HOH   Z  11 .    ? -46.700 82.420  101.149 1.00 24.33 ? 1925 HOH   A O     1 
HETATM 18823 O  O     . HOH   Z  11 .    ? -33.098 78.090  73.865  1.00 26.62 ? 1926 HOH   A O     1 
HETATM 18824 O  O     . HOH   Z  11 .    ? 1.180   74.860  106.900 1.00 27.63 ? 1927 HOH   A O     1 
HETATM 18825 O  O     . HOH   Z  11 .    ? -9.521  56.138  82.271  1.00 32.37 ? 1928 HOH   A O     1 
HETATM 18826 O  O     . HOH   Z  11 .    ? -1.926  85.467  112.606 1.00 26.08 ? 1929 HOH   A O     1 
HETATM 18827 O  O     . HOH   Z  11 .    ? -22.441 98.600  99.913  1.00 37.43 ? 1930 HOH   A O     1 
HETATM 18828 O  O     . HOH   Z  11 .    ? -47.792 59.281  82.451  1.00 15.71 ? 1931 HOH   A O     1 
HETATM 18829 O  O     . HOH   Z  11 .    ? -52.282 62.021  94.382  1.00 20.26 ? 1932 HOH   A O     1 
HETATM 18830 O  O     . HOH   Z  11 .    ? -49.405 78.303  77.240  1.00 31.46 ? 1933 HOH   A O     1 
HETATM 18831 O  O     . HOH   Z  11 .    ? -58.102 57.971  62.786  1.00 19.83 ? 1934 HOH   A O     1 
HETATM 18832 O  O     . HOH   Z  11 .    ? 17.019  69.246  117.287 1.00 28.25 ? 1935 HOH   A O     1 
HETATM 18833 O  O     . HOH   Z  11 .    ? -34.098 82.531  118.130 1.00 23.28 ? 1936 HOH   A O     1 
HETATM 18834 O  O     . HOH   Z  11 .    ? -30.667 87.027  101.698 1.00 31.78 ? 1937 HOH   A O     1 
HETATM 18835 O  O     . HOH   Z  11 .    ? -37.189 45.588  103.791 1.00 31.75 ? 1938 HOH   A O     1 
HETATM 18836 O  O     . HOH   Z  11 .    ? -20.391 66.162  80.718  1.00 27.17 ? 1939 HOH   A O     1 
HETATM 18837 O  O     . HOH   Z  11 .    ? -20.875 73.702  99.299  1.00 28.85 ? 1940 HOH   A O     1 
HETATM 18838 O  O     . HOH   Z  11 .    ? -66.217 61.727  75.492  1.00 18.78 ? 1941 HOH   A O     1 
HETATM 18839 O  O     . HOH   Z  11 .    ? -27.075 64.880  99.792  1.00 25.10 ? 1942 HOH   A O     1 
HETATM 18840 O  O     . HOH   Z  11 .    ? -48.884 29.702  73.537  1.00 37.89 ? 1943 HOH   A O     1 
HETATM 18841 O  O     . HOH   Z  11 .    ? -11.743 59.891  84.363  1.00 27.14 ? 1944 HOH   A O     1 
HETATM 18842 O  O     . HOH   Z  11 .    ? -14.176 85.075  76.650  1.00 32.93 ? 1945 HOH   A O     1 
HETATM 18843 O  O     . HOH   Z  11 .    ? -9.258  87.374  88.265  1.00 43.34 ? 1946 HOH   A O     1 
HETATM 18844 O  O     . HOH   Z  11 .    ? -24.062 67.431  104.874 1.00 22.47 ? 1947 HOH   A O     1 
HETATM 18845 O  O     . HOH   Z  11 .    ? 32.171  72.234  107.380 1.00 46.29 ? 1948 HOH   A O     1 
HETATM 18846 O  O     . HOH   Z  11 .    ? -40.475 81.825  110.326 1.00 29.22 ? 1949 HOH   A O     1 
HETATM 18847 O  O     . HOH   Z  11 .    ? -3.349  87.748  104.393 1.00 27.13 ? 1950 HOH   A O     1 
HETATM 18848 O  O     . HOH   Z  11 .    ? -44.199 31.783  83.617  1.00 29.29 ? 1951 HOH   A O     1 
HETATM 18849 O  O     . HOH   Z  11 .    ? -2.689  56.045  99.528  1.00 33.26 ? 1952 HOH   A O     1 
HETATM 18850 O  O     . HOH   Z  11 .    ? -4.489  59.297  117.947 1.00 22.73 ? 1953 HOH   A O     1 
HETATM 18851 O  O     . HOH   Z  11 .    ? -57.102 53.568  95.853  1.00 24.17 ? 1954 HOH   A O     1 
HETATM 18852 O  O     . HOH   Z  11 .    ? -29.029 76.620  72.455  1.00 29.01 ? 1955 HOH   A O     1 
HETATM 18853 O  O     . HOH   Z  11 .    ? -7.376  37.971  63.352  1.00 35.61 ? 1956 HOH   A O     1 
HETATM 18854 O  O     . HOH   Z  11 .    ? -48.745 61.756  56.557  1.00 22.55 ? 1957 HOH   A O     1 
HETATM 18855 O  O     . HOH   Z  11 .    ? -62.609 67.645  66.160  1.00 29.69 ? 1958 HOH   A O     1 
HETATM 18856 O  O     . HOH   Z  11 .    ? -4.310  73.055  76.680  1.00 29.25 ? 1959 HOH   A O     1 
HETATM 18857 O  O     . HOH   Z  11 .    ? -45.798 33.533  82.393  1.00 34.03 ? 1960 HOH   A O     1 
HETATM 18858 O  O     . HOH   Z  11 .    ? -8.189  77.288  91.594  1.00 23.07 ? 1961 HOH   A O     1 
HETATM 18859 O  O     . HOH   Z  11 .    ? -21.357 59.573  122.022 1.00 30.65 ? 1962 HOH   A O     1 
HETATM 18860 O  O     . HOH   Z  11 .    ? -38.679 58.109  75.107  1.00 37.30 ? 1963 HOH   A O     1 
HETATM 18861 O  O     . HOH   Z  11 .    ? -33.447 45.869  84.332  1.00 27.04 ? 1964 HOH   A O     1 
HETATM 18862 O  O     . HOH   Z  11 .    ? -36.814 51.817  60.650  1.00 29.97 ? 1965 HOH   A O     1 
HETATM 18863 O  O     . HOH   Z  11 .    ? -67.799 37.231  75.257  1.00 40.90 ? 1966 HOH   A O     1 
HETATM 18864 O  O     . HOH   Z  11 .    ? -40.225 97.089  103.016 1.00 37.27 ? 1967 HOH   A O     1 
HETATM 18865 O  O     . HOH   Z  11 .    ? -1.554  77.005  87.405  1.00 27.10 ? 1968 HOH   A O     1 
HETATM 18866 O  O     . HOH   Z  11 .    ? -49.203 47.727  97.013  1.00 23.23 ? 1969 HOH   A O     1 
HETATM 18867 O  O     . HOH   Z  11 .    ? -35.248 63.413  115.623 1.00 35.78 ? 1970 HOH   A O     1 
HETATM 18868 O  O     . HOH   Z  11 .    ? -8.003  75.053  70.020  1.00 30.07 ? 1971 HOH   A O     1 
HETATM 18869 O  O     . HOH   Z  11 .    ? -48.150 83.024  110.947 1.00 32.61 ? 1972 HOH   A O     1 
HETATM 18870 O  O     . HOH   Z  11 .    ? 20.580  83.446  100.442 1.00 39.55 ? 1973 HOH   A O     1 
HETATM 18871 O  O     . HOH   Z  11 .    ? -25.173 79.369  94.685  1.00 22.64 ? 1974 HOH   A O     1 
HETATM 18872 O  O     . HOH   Z  11 .    ? -7.568  50.889  52.728  1.00 30.06 ? 1975 HOH   A O     1 
HETATM 18873 O  O     . HOH   Z  11 .    ? 19.222  82.109  112.609 1.00 32.15 ? 1976 HOH   A O     1 
HETATM 18874 O  O     . HOH   Z  11 .    ? -41.781 79.893  79.561  1.00 30.27 ? 1977 HOH   A O     1 
HETATM 18875 O  O     . HOH   Z  11 .    ? 18.244  57.541  104.589 1.00 29.08 ? 1978 HOH   A O     1 
HETATM 18876 O  O     . HOH   Z  11 .    ? -65.384 71.522  80.253  1.00 27.08 ? 1979 HOH   A O     1 
HETATM 18877 O  O     . HOH   Z  11 .    ? -39.047 66.903  94.043  1.00 27.55 ? 1980 HOH   A O     1 
HETATM 18878 O  O     . HOH   Z  11 .    ? -7.195  62.536  106.666 1.00 20.38 ? 1981 HOH   A O     1 
HETATM 18879 O  O     . HOH   Z  11 .    ? -8.359  81.992  104.552 1.00 21.36 ? 1982 HOH   A O     1 
HETATM 18880 O  O     . HOH   Z  11 .    ? -6.565  53.881  99.723  1.00 40.92 ? 1983 HOH   A O     1 
HETATM 18881 O  O     . HOH   Z  11 .    ? -59.453 63.091  77.297  1.00 21.65 ? 1984 HOH   A O     1 
HETATM 18882 O  O     . HOH   Z  11 .    ? -44.009 40.946  85.380  1.00 34.69 ? 1985 HOH   A O     1 
HETATM 18883 O  O     . HOH   Z  11 .    ? -38.988 88.832  90.371  1.00 32.58 ? 1986 HOH   A O     1 
HETATM 18884 O  O     . HOH   Z  11 .    ? -34.220 55.025  70.834  1.00 36.70 ? 1987 HOH   A O     1 
HETATM 18885 O  O     . HOH   Z  11 .    ? 2.366   84.108  101.212 1.00 25.58 ? 1988 HOH   A O     1 
HETATM 18886 O  O     . HOH   Z  11 .    ? -10.133 82.278  77.690  1.00 35.60 ? 1989 HOH   A O     1 
HETATM 18887 O  O     . HOH   Z  11 .    ? -46.177 65.214  106.546 1.00 36.62 ? 1990 HOH   A O     1 
HETATM 18888 O  O     . HOH   Z  11 .    ? -40.775 80.239  87.308  1.00 21.19 ? 1991 HOH   A O     1 
HETATM 18889 O  O     . HOH   Z  11 .    ? 12.587  67.371  92.804  1.00 31.24 ? 1992 HOH   A O     1 
HETATM 18890 O  O     . HOH   Z  11 .    ? -43.728 25.351  75.729  1.00 39.97 ? 1993 HOH   A O     1 
HETATM 18891 O  O     . HOH   Z  11 .    ? -16.058 47.182  53.377  1.00 31.13 ? 1994 HOH   A O     1 
HETATM 18892 O  O     . HOH   Z  11 .    ? -36.632 69.340  118.844 1.00 30.58 ? 1995 HOH   A O     1 
HETATM 18893 O  O     . HOH   Z  11 .    ? -36.846 68.433  82.948  1.00 27.83 ? 1996 HOH   A O     1 
HETATM 18894 O  O     . HOH   Z  11 .    ? -44.702 61.160  85.182  1.00 17.16 ? 1997 HOH   A O     1 
HETATM 18895 O  O     . HOH   Z  11 .    ? 28.435  74.477  107.126 1.00 42.81 ? 1998 HOH   A O     1 
HETATM 18896 O  O     . HOH   Z  11 .    ? -32.323 48.493  83.760  1.00 33.68 ? 1999 HOH   A O     1 
HETATM 18897 O  O     . HOH   Z  11 .    ? -43.845 59.525  87.201  1.00 16.06 ? 2000 HOH   A O     1 
HETATM 18898 O  O     . HOH   Z  11 .    ? -58.425 73.303  90.862  1.00 42.38 ? 2001 HOH   A O     1 
HETATM 18899 O  O     . HOH   Z  11 .    ? -67.636 51.116  77.466  1.00 42.11 ? 2002 HOH   A O     1 
HETATM 18900 O  O     . HOH   Z  11 .    ? -30.234 54.368  57.595  1.00 39.30 ? 2003 HOH   A O     1 
HETATM 18901 O  O     . HOH   Z  11 .    ? -41.658 55.282  104.559 1.00 36.18 ? 2004 HOH   A O     1 
HETATM 18902 O  O     . HOH   Z  11 .    ? -52.463 72.784  64.069  1.00 28.57 ? 2005 HOH   A O     1 
HETATM 18903 O  O     . HOH   Z  11 .    ? -38.499 73.387  89.951  1.00 33.84 ? 2006 HOH   A O     1 
HETATM 18904 O  O     . HOH   Z  11 .    ? -12.410 40.213  67.987  1.00 39.78 ? 2007 HOH   A O     1 
HETATM 18905 O  O     . HOH   Z  11 .    ? -39.384 88.604  118.760 1.00 33.57 ? 2008 HOH   A O     1 
HETATM 18906 O  O     . HOH   Z  11 .    ? -64.483 43.066  85.844  1.00 28.55 ? 2009 HOH   A O     1 
HETATM 18907 O  O     . HOH   Z  11 .    ? -37.989 67.717  97.831  1.00 27.09 ? 2010 HOH   A O     1 
HETATM 18908 O  O     . HOH   Z  11 .    ? -1.866  78.031  104.853 1.00 22.25 ? 2011 HOH   A O     1 
HETATM 18909 O  O     . HOH   Z  11 .    ? 2.847   74.385  108.931 1.00 26.10 ? 2012 HOH   A O     1 
HETATM 18910 O  O     . HOH   Z  11 .    ? -59.017 58.489  76.630  1.00 18.70 ? 2013 HOH   A O     1 
HETATM 18911 O  O     . HOH   Z  11 .    ? -32.147 52.363  85.795  1.00 27.46 ? 2014 HOH   A O     1 
HETATM 18912 O  O     . HOH   Z  11 .    ? -39.341 76.706  92.913  1.00 24.49 ? 2015 HOH   A O     1 
HETATM 18913 O  O     . HOH   Z  11 .    ? -60.004 50.546  90.478  1.00 33.68 ? 2016 HOH   A O     1 
HETATM 18914 O  O     . HOH   Z  11 .    ? -8.240  60.195  93.714  1.00 36.66 ? 2017 HOH   A O     1 
HETATM 18915 O  O     . HOH   Z  11 .    ? -63.601 71.154  70.541  1.00 28.75 ? 2018 HOH   A O     1 
HETATM 18916 O  O     . HOH   Z  11 .    ? -32.049 75.261  125.999 1.00 30.27 ? 2019 HOH   A O     1 
HETATM 18917 O  O     . HOH   Z  11 .    ? -55.014 26.753  91.327  1.00 35.95 ? 2020 HOH   A O     1 
HETATM 18918 O  O     . HOH   Z  11 .    ? 1.327   62.396  110.795 1.00 28.56 ? 2021 HOH   A O     1 
HETATM 18919 O  O     . HOH   Z  11 .    ? -25.072 82.767  72.174  1.00 30.92 ? 2022 HOH   A O     1 
HETATM 18920 O  O     . HOH   Z  11 .    ? -33.494 83.871  122.894 1.00 28.41 ? 2023 HOH   A O     1 
HETATM 18921 O  O     . HOH   Z  11 .    ? -51.758 87.359  103.019 1.00 44.26 ? 2024 HOH   A O     1 
HETATM 18922 O  O     . HOH   Z  11 .    ? 14.271  78.506  120.352 1.00 32.30 ? 2025 HOH   A O     1 
HETATM 18923 O  O     . HOH   Z  11 .    ? -68.600 52.902  84.777  1.00 35.20 ? 2026 HOH   A O     1 
HETATM 18924 O  O     . HOH   Z  11 .    ? -36.947 88.136  83.078  1.00 35.74 ? 2027 HOH   A O     1 
HETATM 18925 O  O     . HOH   Z  11 .    ? 6.736   61.175  102.759 1.00 18.77 ? 2028 HOH   A O     1 
HETATM 18926 O  O     . HOH   Z  11 .    ? -25.368 88.470  115.769 1.00 23.78 ? 2029 HOH   A O     1 
HETATM 18927 O  O     . HOH   Z  11 .    ? -33.094 92.394  106.415 1.00 36.75 ? 2030 HOH   A O     1 
HETATM 18928 O  O     . HOH   Z  11 .    ? -6.536  70.991  103.735 1.00 29.32 ? 2031 HOH   A O     1 
HETATM 18929 O  O     . HOH   Z  11 .    ? -14.058 95.419  119.179 1.00 35.53 ? 2032 HOH   A O     1 
HETATM 18930 O  O     . HOH   Z  11 .    ? -60.630 70.098  87.420  1.00 42.83 ? 2033 HOH   A O     1 
HETATM 18931 O  O     . HOH   Z  11 .    ? -64.400 48.033  76.144  1.00 35.31 ? 2034 HOH   A O     1 
HETATM 18932 O  O     . HOH   Z  11 .    ? -29.632 83.545  100.950 1.00 25.47 ? 2035 HOH   A O     1 
HETATM 18933 O  O     . HOH   Z  11 .    ? 23.712  58.702  102.816 1.00 36.93 ? 2036 HOH   A O     1 
HETATM 18934 O  O     . HOH   Z  11 .    ? -1.376  80.524  111.439 1.00 29.86 ? 2037 HOH   A O     1 
HETATM 18935 O  O     . HOH   Z  11 .    ? -49.784 72.457  100.827 1.00 22.64 ? 2038 HOH   A O     1 
HETATM 18936 O  O     . HOH   Z  11 .    ? -47.951 55.076  58.087  1.00 34.05 ? 2039 HOH   A O     1 
HETATM 18937 O  O     . HOH   Z  11 .    ? -17.734 85.588  77.160  1.00 27.40 ? 2040 HOH   A O     1 
HETATM 18938 O  O     . HOH   Z  11 .    ? -18.704 97.701  126.336 1.00 44.00 ? 2041 HOH   A O     1 
HETATM 18939 O  O     . HOH   Z  11 .    ? -28.040 60.465  124.532 1.00 38.04 ? 2042 HOH   A O     1 
HETATM 18940 O  O     . HOH   Z  11 .    ? -27.325 61.959  88.663  1.00 21.03 ? 2043 HOH   A O     1 
HETATM 18941 O  O     . HOH   Z  11 .    ? -0.321  74.082  95.718  1.00 36.48 ? 2044 HOH   A O     1 
HETATM 18942 O  O     . HOH   Z  11 .    ? -19.230 90.965  76.617  1.00 31.06 ? 2045 HOH   A O     1 
HETATM 18943 O  O     . HOH   Z  11 .    ? -17.088 53.456  75.923  1.00 32.58 ? 2046 HOH   A O     1 
HETATM 18944 O  O     . HOH   Z  11 .    ? -61.908 68.161  89.031  1.00 36.20 ? 2047 HOH   A O     1 
HETATM 18945 O  O     . HOH   Z  11 .    ? -55.990 25.434  88.144  1.00 38.41 ? 2048 HOH   A O     1 
HETATM 18946 O  O     . HOH   Z  11 .    ? -30.486 50.322  104.375 1.00 30.30 ? 2049 HOH   A O     1 
HETATM 18947 O  O     . HOH   Z  11 .    ? -4.400  55.100  61.179  1.00 33.86 ? 2050 HOH   A O     1 
HETATM 18948 O  O     . HOH   Z  11 .    ? 8.543   68.325  114.148 1.00 31.05 ? 2051 HOH   A O     1 
HETATM 18949 O  O     . HOH   Z  11 .    ? -12.595 65.973  112.373 1.00 19.24 ? 2052 HOH   A O     1 
HETATM 18950 O  O     . HOH   Z  11 .    ? -43.124 77.495  67.742  1.00 28.67 ? 2053 HOH   A O     1 
HETATM 18951 O  O     . HOH   Z  11 .    ? -16.156 53.980  100.214 1.00 35.45 ? 2054 HOH   A O     1 
HETATM 18952 O  O     . HOH   Z  11 .    ? -30.761 96.120  104.462 1.00 33.95 ? 2055 HOH   A O     1 
HETATM 18953 O  O     . HOH   Z  11 .    ? 9.473   68.090  93.439  1.00 37.08 ? 2056 HOH   A O     1 
HETATM 18954 O  O     . HOH   Z  11 .    ? -38.436 70.496  81.461  1.00 22.86 ? 2057 HOH   A O     1 
HETATM 18955 O  O     . HOH   Z  11 .    ? -22.405 54.586  96.978  1.00 32.53 ? 2058 HOH   A O     1 
HETATM 18956 O  O     . HOH   Z  11 .    ? -36.821 60.622  95.969  1.00 19.17 ? 2059 HOH   A O     1 
HETATM 18957 O  O     . HOH   Z  11 .    ? -22.807 83.533  91.105  1.00 19.47 ? 2060 HOH   A O     1 
HETATM 18958 O  O     . HOH   Z  11 .    ? -19.372 92.006  104.729 1.00 31.19 ? 2061 HOH   A O     1 
HETATM 18959 O  O     . HOH   Z  11 .    ? -18.332 68.961  104.181 1.00 23.72 ? 2062 HOH   A O     1 
HETATM 18960 O  O     . HOH   Z  11 .    ? -26.933 52.012  98.324  1.00 22.66 ? 2063 HOH   A O     1 
HETATM 18961 O  O     . HOH   Z  11 .    ? -14.758 55.530  50.730  1.00 41.45 ? 2064 HOH   A O     1 
HETATM 18962 O  O     . HOH   Z  11 .    ? -54.215 79.238  81.129  1.00 33.51 ? 2065 HOH   A O     1 
HETATM 18963 O  O     . HOH   Z  11 .    ? -3.445  82.462  97.007  1.00 25.15 ? 2066 HOH   A O     1 
HETATM 18964 O  O     . HOH   Z  11 .    ? -53.470 49.552  60.145  1.00 30.31 ? 2067 HOH   A O     1 
HETATM 18965 O  O     . HOH   Z  11 .    ? 4.103   60.669  100.589 1.00 25.95 ? 2068 HOH   A O     1 
HETATM 18966 O  O     . HOH   Z  11 .    ? -30.664 91.422  111.092 1.00 35.68 ? 2069 HOH   A O     1 
HETATM 18967 O  O     . HOH   Z  11 .    ? -45.085 57.578  101.819 1.00 26.73 ? 2070 HOH   A O     1 
HETATM 18968 O  O     . HOH   Z  11 .    ? -39.653 61.586  94.144  1.00 21.87 ? 2071 HOH   A O     1 
HETATM 18969 O  O     . HOH   Z  11 .    ? -43.667 85.363  94.535  1.00 37.99 ? 2072 HOH   A O     1 
HETATM 18970 O  O     . HOH   Z  11 .    ? -42.205 56.802  89.131  1.00 17.80 ? 2073 HOH   A O     1 
HETATM 18971 O  O     . HOH   Z  11 .    ? -38.773 71.287  84.006  1.00 24.14 ? 2074 HOH   A O     1 
HETATM 18972 O  O     . HOH   Z  11 .    ? -42.605 28.948  86.242  1.00 35.94 ? 2075 HOH   A O     1 
HETATM 18973 O  O     . HOH   Z  11 .    ? -19.567 90.827  97.318  1.00 36.85 ? 2076 HOH   A O     1 
HETATM 18974 O  O     . HOH   Z  11 .    ? 25.578  64.634  101.969 1.00 28.22 ? 2077 HOH   A O     1 
HETATM 18975 O  O     . HOH   Z  11 .    ? -34.200 56.656  105.114 1.00 24.01 ? 2078 HOH   A O     1 
HETATM 18976 O  O     . HOH   Z  11 .    ? -22.916 53.827  92.310  1.00 29.30 ? 2079 HOH   A O     1 
HETATM 18977 O  O     . HOH   Z  11 .    ? -54.974 42.070  96.506  1.00 31.63 ? 2080 HOH   A O     1 
HETATM 18978 O  O     . HOH   Z  11 .    ? 28.563  64.353  111.978 1.00 34.65 ? 2081 HOH   A O     1 
HETATM 18979 O  O     . HOH   Z  11 .    ? -0.332  86.652  105.250 1.00 24.94 ? 2082 HOH   A O     1 
HETATM 18980 O  O     . HOH   Z  11 .    ? 17.325  80.447  96.245  1.00 32.58 ? 2083 HOH   A O     1 
HETATM 18981 O  O     . HOH   Z  11 .    ? -38.087 72.986  87.261  1.00 31.72 ? 2084 HOH   A O     1 
HETATM 18982 O  O     . HOH   Z  11 .    ? -46.638 34.890  100.728 1.00 41.89 ? 2085 HOH   A O     1 
HETATM 18983 O  O     . HOH   Z  11 .    ? -41.720 88.812  96.418  1.00 26.22 ? 2086 HOH   A O     1 
HETATM 18984 O  O     . HOH   Z  11 .    ? -36.831 49.942  100.396 1.00 27.78 ? 2087 HOH   A O     1 
HETATM 18985 O  O     . HOH   Z  11 .    ? -8.027  72.560  100.254 1.00 28.99 ? 2088 HOH   A O     1 
HETATM 18986 O  O     . HOH   Z  11 .    ? 22.887  76.325  114.155 1.00 28.05 ? 2089 HOH   A O     1 
HETATM 18987 O  O     . HOH   Z  11 .    ? -69.805 49.830  81.634  1.00 40.28 ? 2090 HOH   A O     1 
HETATM 18988 O  O     . HOH   Z  11 .    ? -63.929 47.637  73.656  1.00 36.96 ? 2091 HOH   A O     1 
HETATM 18989 O  O     . HOH   Z  11 .    ? -32.289 64.647  121.582 1.00 29.51 ? 2092 HOH   A O     1 
HETATM 18990 O  O     . HOH   Z  11 .    ? -43.563 90.571  99.664  1.00 31.05 ? 2093 HOH   A O     1 
HETATM 18991 O  O     . HOH   Z  11 .    ? -9.608  64.034  95.715  1.00 21.07 ? 2094 HOH   A O     1 
HETATM 18992 O  O     . HOH   Z  11 .    ? -22.433 48.239  82.801  1.00 33.58 ? 2095 HOH   A O     1 
HETATM 18993 O  O     . HOH   Z  11 .    ? -28.227 69.468  85.580  1.00 30.57 ? 2096 HOH   A O     1 
HETATM 18994 O  O     . HOH   Z  11 .    ? -15.475 55.215  121.178 1.00 34.77 ? 2097 HOH   A O     1 
HETATM 18995 O  O     . HOH   Z  11 .    ? -59.547 38.595  82.323  1.00 33.92 ? 2098 HOH   A O     1 
HETATM 18996 O  O     . HOH   Z  11 .    ? -25.564 68.229  90.063  1.00 28.94 ? 2099 HOH   A O     1 
HETATM 18997 O  O     . HOH   Z  11 .    ? -7.053  93.808  112.816 1.00 34.42 ? 2100 HOH   A O     1 
HETATM 18998 O  O     . HOH   Z  11 .    ? -7.170  64.805  93.995  1.00 38.98 ? 2101 HOH   A O     1 
HETATM 18999 O  O     . HOH   Z  11 .    ? -18.214 73.881  131.600 1.00 38.14 ? 2102 HOH   A O     1 
HETATM 19000 O  O     . HOH   Z  11 .    ? -39.767 39.461  98.257  1.00 36.04 ? 2103 HOH   A O     1 
HETATM 19001 O  O     . HOH   Z  11 .    ? -20.838 58.317  96.934  1.00 23.41 ? 2104 HOH   A O     1 
HETATM 19002 O  O     . HOH   Z  11 .    ? 16.426  65.349  119.305 1.00 32.00 ? 2105 HOH   A O     1 
HETATM 19003 O  O     . HOH   Z  11 .    ? -49.539 35.574  87.583  1.00 29.65 ? 2106 HOH   A O     1 
HETATM 19004 O  O     . HOH   Z  11 .    ? -13.050 69.173  73.554  1.00 33.78 ? 2107 HOH   A O     1 
HETATM 19005 O  O     . HOH   Z  11 .    ? -24.833 69.346  74.174  1.00 29.09 ? 2108 HOH   A O     1 
HETATM 19006 O  O     . HOH   Z  11 .    ? -30.839 66.424  126.379 1.00 37.18 ? 2109 HOH   A O     1 
HETATM 19007 O  O     . HOH   Z  11 .    ? -18.144 88.495  101.291 1.00 39.63 ? 2110 HOH   A O     1 
HETATM 19008 O  O     . HOH   Z  11 .    ? -47.826 80.080  95.563  1.00 34.52 ? 2111 HOH   A O     1 
HETATM 19009 O  O     . HOH   Z  11 .    ? -27.192 90.493  115.215 1.00 27.38 ? 2112 HOH   A O     1 
HETATM 19010 O  O     . HOH   Z  11 .    ? -2.086  78.055  75.381  1.00 26.79 ? 2113 HOH   A O     1 
HETATM 19011 O  O     . HOH   Z  11 .    ? -19.810 79.104  114.516 1.00 20.17 ? 2114 HOH   A O     1 
HETATM 19012 O  O     . HOH   Z  11 .    ? -45.848 24.551  82.158  1.00 39.72 ? 2115 HOH   A O     1 
HETATM 19013 O  O     . HOH   Z  11 .    ? -14.987 59.160  126.223 1.00 29.94 ? 2116 HOH   A O     1 
HETATM 19014 O  O     . HOH   Z  11 .    ? -31.173 74.164  87.506  1.00 32.34 ? 2117 HOH   A O     1 
HETATM 19015 O  O     . HOH   Z  11 .    ? -56.331 68.941  99.803  1.00 37.46 ? 2118 HOH   A O     1 
HETATM 19016 O  O     . HOH   Z  11 .    ? -44.745 85.800  99.380  1.00 36.90 ? 2119 HOH   A O     1 
HETATM 19017 O  O     . HOH   Z  11 .    ? -58.956 42.692  89.076  1.00 31.26 ? 2120 HOH   A O     1 
HETATM 19018 O  O     . HOH   Z  11 .    ? -52.786 37.320  60.846  1.00 48.17 ? 2121 HOH   A O     1 
HETATM 19019 O  O     . HOH   Z  11 .    ? -22.931 75.215  99.324  1.00 24.29 ? 2122 HOH   A O     1 
HETATM 19020 O  O     . HOH   Z  11 .    ? -27.137 80.009  69.725  1.00 37.45 ? 2123 HOH   A O     1 
HETATM 19021 O  O     . HOH   Z  11 .    ? 2.581   86.450  125.731 1.00 39.43 ? 2124 HOH   A O     1 
HETATM 19022 O  O     . HOH   Z  11 .    ? -28.650 84.042  72.708  1.00 40.40 ? 2125 HOH   A O     1 
HETATM 19023 O  O     . HOH   Z  11 .    ? -41.432 29.809  89.207  1.00 35.17 ? 2126 HOH   A O     1 
HETATM 19024 O  O     . HOH   Z  11 .    ? -23.270 89.192  101.781 1.00 28.54 ? 2127 HOH   A O     1 
HETATM 19025 O  O     . HOH   Z  11 .    ? -16.793 54.858  116.788 1.00 35.67 ? 2128 HOH   A O     1 
HETATM 19026 O  O     . HOH   Z  11 .    ? 2.604   78.016  97.662  1.00 25.87 ? 2129 HOH   A O     1 
HETATM 19027 O  O     . HOH   Z  11 .    ? -43.588 37.678  104.555 1.00 40.18 ? 2130 HOH   A O     1 
HETATM 19028 O  O     . HOH   Z  11 .    ? -58.289 45.847  91.831  1.00 37.54 ? 2131 HOH   A O     1 
HETATM 19029 O  O     . HOH   Z  11 .    ? 10.378  81.403  124.745 1.00 32.96 ? 2132 HOH   A O     1 
HETATM 19030 O  O     . HOH   Z  11 .    ? -34.288 42.493  69.983  1.00 36.10 ? 2133 HOH   A O     1 
HETATM 19031 O  O     . HOH   Z  11 .    ? 1.225   66.506  96.140  1.00 24.23 ? 2134 HOH   A O     1 
HETATM 19032 O  O     . HOH   Z  11 .    ? -53.596 68.932  93.167  1.00 23.72 ? 2135 HOH   A O     1 
HETATM 19033 O  O     . HOH   Z  11 .    ? -1.202  70.267  115.922 1.00 26.34 ? 2136 HOH   A O     1 
HETATM 19034 O  O     . HOH   Z  11 .    ? -26.474 84.339  73.838  1.00 32.32 ? 2137 HOH   A O     1 
HETATM 19035 O  O     . HOH   Z  11 .    ? -42.592 77.748  78.114  1.00 25.97 ? 2138 HOH   A O     1 
HETATM 19036 O  O     . HOH   Z  11 .    ? 18.838  73.304  117.600 1.00 27.13 ? 2139 HOH   A O     1 
HETATM 19037 O  O     . HOH   Z  11 .    ? -32.837 57.427  72.367  1.00 37.74 ? 2140 HOH   A O     1 
HETATM 19038 O  O     . HOH   Z  11 .    ? -14.118 58.378  109.595 1.00 36.05 ? 2141 HOH   A O     1 
HETATM 19039 O  O     . HOH   Z  11 .    ? -2.870  76.070  77.020  1.00 23.39 ? 2142 HOH   A O     1 
HETATM 19040 O  O     . HOH   Z  11 .    ? 2.372   76.566  116.439 1.00 24.82 ? 2143 HOH   A O     1 
HETATM 19041 O  O     . HOH   Z  11 .    ? -32.707 40.797  94.858  1.00 39.02 ? 2144 HOH   A O     1 
HETATM 19042 O  O     . HOH   Z  11 .    ? -40.416 64.944  61.844  1.00 29.76 ? 2145 HOH   A O     1 
HETATM 19043 O  O     . HOH   Z  11 .    ? -25.357 59.475  114.072 1.00 27.21 ? 2146 HOH   A O     1 
HETATM 19044 O  O     . HOH   Z  11 .    ? -61.326 41.952  66.845  1.00 42.08 ? 2147 HOH   A O     1 
HETATM 19045 O  O     . HOH   Z  11 .    ? -26.570 39.508  76.994  1.00 43.11 ? 2148 HOH   A O     1 
HETATM 19046 O  O     . HOH   Z  11 .    ? -36.187 71.745  120.774 1.00 39.04 ? 2149 HOH   A O     1 
HETATM 19047 O  O     . HOH   Z  11 .    ? -14.034 55.947  111.151 1.00 33.50 ? 2150 HOH   A O     1 
HETATM 19048 O  O     . HOH   Z  11 .    ? -35.290 97.972  115.678 1.00 36.67 ? 2151 HOH   A O     1 
HETATM 19049 O  O     . HOH   Z  11 .    ? 7.070   55.378  98.396  1.00 20.67 ? 2152 HOH   A O     1 
HETATM 19050 O  O     . HOH   Z  11 .    ? -48.649 94.701  99.988  1.00 48.40 ? 2153 HOH   A O     1 
HETATM 19051 O  O     . HOH   Z  11 .    ? -40.919 69.018  63.137  1.00 36.95 ? 2154 HOH   A O     1 
HETATM 19052 O  O     . HOH   Z  11 .    ? -11.466 43.632  73.743  1.00 28.70 ? 2155 HOH   A O     1 
HETATM 19053 O  O     . HOH   Z  11 .    ? 0.478   64.347  106.804 1.00 19.39 ? 2156 HOH   A O     1 
HETATM 19054 O  O     . HOH   Z  11 .    ? -13.987 86.729  100.414 1.00 25.46 ? 2157 HOH   A O     1 
HETATM 19055 O  O     . HOH   Z  11 .    ? -1.627  54.567  101.400 1.00 26.00 ? 2158 HOH   A O     1 
HETATM 19056 O  O     . HOH   Z  11 .    ? -41.532 88.632  93.645  1.00 29.91 ? 2159 HOH   A O     1 
HETATM 19057 O  O     . HOH   Z  11 .    ? -10.619 87.088  91.027  1.00 34.11 ? 2160 HOH   A O     1 
HETATM 19058 O  O     . HOH   Z  11 .    ? -14.946 53.253  75.271  1.00 32.40 ? 2161 HOH   A O     1 
HETATM 19059 O  O     . HOH   Z  11 .    ? -39.568 84.835  103.359 1.00 28.86 ? 2162 HOH   A O     1 
HETATM 19060 O  O     . HOH   Z  11 .    ? -40.802 70.542  92.534  1.00 28.77 ? 2163 HOH   A O     1 
HETATM 19061 O  O     . HOH   Z  11 .    ? -22.358 76.901  69.876  1.00 24.33 ? 2164 HOH   A O     1 
HETATM 19062 O  O     . HOH   Z  11 .    ? -29.011 55.083  111.008 1.00 36.01 ? 2165 HOH   A O     1 
HETATM 19063 O  O     . HOH   Z  11 .    ? -56.902 39.253  90.985  1.00 36.47 ? 2166 HOH   A O     1 
HETATM 19064 O  O     . HOH   Z  11 .    ? -22.784 94.656  117.820 1.00 33.73 ? 2167 HOH   A O     1 
HETATM 19065 O  O     . HOH   Z  11 .    ? -67.580 64.413  85.061  1.00 31.74 ? 2168 HOH   A O     1 
HETATM 19066 O  O     . HOH   Z  11 .    ? -0.212  67.922  117.222 1.00 33.44 ? 2169 HOH   A O     1 
HETATM 19067 O  O     . HOH   Z  11 .    ? 14.441  88.171  105.201 1.00 39.91 ? 2170 HOH   A O     1 
HETATM 19068 O  O     . HOH   Z  11 .    ? -37.260 66.259  108.948 1.00 36.25 ? 2171 HOH   A O     1 
HETATM 19069 O  O     . HOH   Z  11 .    ? -37.769 40.580  74.001  1.00 32.12 ? 2172 HOH   A O     1 
HETATM 19070 O  O     . HOH   Z  11 .    ? -31.284 41.518  97.734  1.00 37.72 ? 2173 HOH   A O     1 
HETATM 19071 O  O     . HOH   Z  11 .    ? -36.105 80.700  75.398  1.00 26.22 ? 2174 HOH   A O     1 
HETATM 19072 O  O     . HOH   Z  11 .    ? 2.934   64.956  112.651 1.00 32.49 ? 2175 HOH   A O     1 
HETATM 19073 O  O     . HOH   Z  11 .    ? 8.709   65.013  93.822  1.00 31.08 ? 2176 HOH   A O     1 
HETATM 19074 O  O     . HOH   Z  11 .    ? 11.571  74.825  128.355 1.00 37.60 ? 2177 HOH   A O     1 
HETATM 19075 O  O     . HOH   Z  11 .    ? -17.890 54.124  98.218  1.00 33.48 ? 2178 HOH   A O     1 
HETATM 19076 O  O     . HOH   Z  11 .    ? -50.003 27.506  76.851  1.00 35.83 ? 2179 HOH   A O     1 
HETATM 19077 O  O     . HOH   Z  11 .    ? -42.982 49.928  55.373  1.00 33.08 ? 2180 HOH   A O     1 
HETATM 19078 O  O     . HOH   Z  11 .    ? -5.055  55.835  100.850 1.00 30.85 ? 2181 HOH   A O     1 
HETATM 19079 O  O     . HOH   Z  11 .    ? -41.423 24.376  81.005  1.00 46.44 ? 2182 HOH   A O     1 
HETATM 19080 O  O     . HOH   Z  11 .    ? -10.268 63.868  115.195 1.00 21.91 ? 2183 HOH   A O     1 
HETATM 19081 O  O     . HOH   Z  11 .    ? -33.819 98.853  101.000 1.00 46.40 ? 2184 HOH   A O     1 
HETATM 19082 O  O     . HOH   Z  11 .    ? -46.906 77.244  91.811  1.00 25.52 ? 2185 HOH   A O     1 
HETATM 19083 O  O     . HOH   Z  11 .    ? -53.459 72.427  67.888  1.00 26.16 ? 2186 HOH   A O     1 
HETATM 19084 O  O     . HOH   Z  11 .    ? -39.273 86.541  88.935  1.00 30.33 ? 2187 HOH   A O     1 
HETATM 19085 O  O     . HOH   Z  11 .    ? -49.851 73.040  62.640  1.00 22.60 ? 2188 HOH   A O     1 
HETATM 19086 O  O     . HOH   Z  11 .    ? -13.560 54.283  76.857  1.00 25.51 ? 2189 HOH   A O     1 
HETATM 19087 O  O     . HOH   Z  11 .    ? -11.090 54.108  100.003 1.00 27.68 ? 2190 HOH   A O     1 
HETATM 19088 O  O     . HOH   Z  11 .    ? -3.619  82.182  109.586 1.00 31.95 ? 2191 HOH   A O     1 
HETATM 19089 O  O     . HOH   Z  11 .    ? -64.569 55.316  80.533  1.00 29.61 ? 2192 HOH   A O     1 
HETATM 19090 O  O     . HOH   Z  11 .    ? -56.710 32.378  87.568  1.00 24.28 ? 2193 HOH   A O     1 
HETATM 19091 O  O     . HOH   Z  11 .    ? 26.271  74.276  97.589  1.00 38.81 ? 2194 HOH   A O     1 
HETATM 19092 O  O     . HOH   Z  11 .    ? -62.936 62.318  97.651  1.00 30.68 ? 2195 HOH   A O     1 
HETATM 19093 O  O     . HOH   Z  11 .    ? -12.748 53.876  110.069 1.00 34.49 ? 2196 HOH   A O     1 
HETATM 19094 O  O     . HOH   Z  11 .    ? 21.732  73.153  115.299 1.00 29.80 ? 2197 HOH   A O     1 
HETATM 19095 O  O     . HOH   Z  11 .    ? -53.951 45.240  91.712  1.00 30.86 ? 2198 HOH   A O     1 
HETATM 19096 O  O     . HOH   Z  11 .    ? -45.526 55.090  91.815  1.00 17.65 ? 2199 HOH   A O     1 
HETATM 19097 O  O     . HOH   Z  11 .    ? -34.306 50.340  83.052  1.00 30.07 ? 2200 HOH   A O     1 
HETATM 19098 O  O     . HOH   Z  11 .    ? -0.743  75.015  116.219 1.00 33.14 ? 2201 HOH   A O     1 
HETATM 19099 O  O     . HOH   Z  11 .    ? -3.128  85.709  124.213 1.00 38.99 ? 2202 HOH   A O     1 
HETATM 19100 O  O     . HOH   Z  11 .    ? -35.601 43.786  79.136  1.00 27.37 ? 2203 HOH   A O     1 
HETATM 19101 O  O     . HOH   Z  11 .    ? -33.231 60.407  82.357  1.00 41.70 ? 2204 HOH   A O     1 
HETATM 19102 O  O     . HOH   Z  11 .    ? -50.994 79.707  78.491  1.00 38.59 ? 2205 HOH   A O     1 
HETATM 19103 O  O     . HOH   Z  11 .    ? 5.607   58.742  96.946  1.00 31.61 ? 2206 HOH   A O     1 
HETATM 19104 O  O     . HOH   Z  11 .    ? -8.979  52.078  107.053 1.00 30.72 ? 2207 HOH   A O     1 
HETATM 19105 O  O     . HOH   Z  11 .    ? -7.852  89.120  99.285  1.00 40.08 ? 2208 HOH   A O     1 
HETATM 19106 O  O     . HOH   Z  11 .    ? -51.953 30.176  72.665  1.00 41.37 ? 2209 HOH   A O     1 
HETATM 19107 O  O     . HOH   Z  11 .    ? -34.696 75.885  125.637 1.00 33.68 ? 2210 HOH   A O     1 
HETATM 19108 O  O     . HOH   Z  11 .    ? -61.158 61.788  62.336  1.00 33.49 ? 2211 HOH   A O     1 
HETATM 19109 O  O     . HOH   Z  11 .    ? -28.631 57.550  88.188  1.00 31.20 ? 2212 HOH   A O     1 
HETATM 19110 O  O     . HOH   Z  11 .    ? -41.596 64.747  58.195  1.00 27.76 ? 2213 HOH   A O     1 
HETATM 19111 O  O     . HOH   Z  11 .    ? -30.926 83.962  122.856 1.00 27.86 ? 2214 HOH   A O     1 
HETATM 19112 O  O     . HOH   Z  11 .    ? 1.336   57.377  107.210 1.00 20.35 ? 2215 HOH   A O     1 
HETATM 19113 O  O     . HOH   Z  11 .    ? -66.192 68.845  83.760  1.00 31.21 ? 2216 HOH   A O     1 
HETATM 19114 O  O     . HOH   Z  11 .    ? -56.658 73.502  95.908  1.00 32.46 ? 2217 HOH   A O     1 
HETATM 19115 O  O     . HOH   Z  11 .    ? -3.911  58.105  63.248  1.00 42.12 ? 2218 HOH   A O     1 
HETATM 19116 O  O     . HOH   Z  11 .    ? -4.595  50.728  56.162  1.00 34.29 ? 2219 HOH   A O     1 
HETATM 19117 O  O     . HOH   Z  11 .    ? -9.279  60.615  83.985  1.00 24.17 ? 2220 HOH   A O     1 
HETATM 19118 O  O     . HOH   Z  11 .    ? -64.400 71.170  82.881  1.00 36.70 ? 2221 HOH   A O     1 
HETATM 19119 O  O     . HOH   Z  11 .    ? -8.923  53.369  104.416 1.00 38.03 ? 2222 HOH   A O     1 
HETATM 19120 O  O     . HOH   Z  11 .    ? 22.294  65.513  92.603  1.00 41.02 ? 2223 HOH   A O     1 
HETATM 19121 O  O     . HOH   Z  11 .    ? -49.475 54.490  73.724  1.00 21.28 ? 2224 HOH   A O     1 
HETATM 19122 O  O     . HOH   Z  11 .    ? -17.202 55.006  77.972  1.00 33.84 ? 2225 HOH   A O     1 
HETATM 19123 O  O     . HOH   Z  11 .    ? -57.646 33.630  71.652  1.00 44.63 ? 2226 HOH   A O     1 
HETATM 19124 O  O     . HOH   Z  11 .    ? -44.259 93.087  88.330  1.00 42.56 ? 2227 HOH   A O     1 
HETATM 19125 O  O     . HOH   Z  11 .    ? -28.503 95.188  88.774  1.00 34.68 ? 2228 HOH   A O     1 
HETATM 19126 O  O     . HOH   Z  11 .    ? -48.957 65.573  53.922  1.00 28.60 ? 2229 HOH   A O     1 
HETATM 19127 O  O     . HOH   Z  11 .    ? -46.439 78.719  116.866 1.00 35.32 ? 2230 HOH   A O     1 
HETATM 19128 O  O     . HOH   Z  11 .    ? -16.212 43.442  71.437  1.00 35.45 ? 2231 HOH   A O     1 
HETATM 19129 O  O     . HOH   Z  11 .    ? -5.440  47.000  55.331  1.00 36.66 ? 2232 HOH   A O     1 
HETATM 19130 O  O     . HOH   Z  11 .    ? -21.950 67.389  73.378  1.00 36.36 ? 2233 HOH   A O     1 
HETATM 19131 O  O     . HOH   Z  11 .    ? -21.962 95.018  131.366 1.00 45.04 ? 2234 HOH   A O     1 
HETATM 19132 O  O     . HOH   Z  11 .    ? -36.507 82.748  120.423 1.00 32.13 ? 2235 HOH   A O     1 
HETATM 19133 O  O     . HOH   Z  11 .    ? -1.932  80.105  96.959  1.00 30.34 ? 2236 HOH   A O     1 
HETATM 19134 O  O     . HOH   Z  11 .    ? 18.366  75.361  95.953  1.00 36.06 ? 2237 HOH   A O     1 
HETATM 19135 O  O     . HOH   Z  11 .    ? -3.514  79.067  93.018  1.00 32.74 ? 2238 HOH   A O     1 
HETATM 19136 O  O     . HOH   Z  11 .    ? -48.576 78.311  74.688  1.00 30.45 ? 2239 HOH   A O     1 
HETATM 19137 O  O     . HOH   Z  11 .    ? -35.882 44.570  66.248  1.00 38.29 ? 2240 HOH   A O     1 
HETATM 19138 O  O     . HOH   Z  11 .    ? -39.832 38.064  84.840  1.00 31.06 ? 2241 HOH   A O     1 
HETATM 19139 O  O     . HOH   Z  11 .    ? -37.435 86.235  101.575 1.00 25.53 ? 2242 HOH   A O     1 
HETATM 19140 O  O     . HOH   Z  11 .    ? -43.001 56.380  91.685  1.00 17.09 ? 2243 HOH   A O     1 
HETATM 19141 O  O     . HOH   Z  11 .    ? 11.232  85.227  124.111 1.00 29.69 ? 2244 HOH   A O     1 
HETATM 19142 O  O     . HOH   Z  11 .    ? 10.196  77.290  127.472 1.00 44.13 ? 2245 HOH   A O     1 
HETATM 19143 O  O     . HOH   Z  11 .    ? -0.827  77.598  126.147 1.00 39.95 ? 2246 HOH   A O     1 
HETATM 19144 O  O     . HOH   Z  11 .    ? -49.363 33.545  100.155 1.00 46.51 ? 2247 HOH   A O     1 
HETATM 19145 O  O     . HOH   Z  11 .    ? -26.846 62.971  86.102  1.00 23.19 ? 2248 HOH   A O     1 
HETATM 19146 O  O     . HOH   Z  11 .    ? -20.892 50.524  108.336 1.00 43.00 ? 2249 HOH   A O     1 
HETATM 19147 O  O     . HOH   Z  11 .    ? 11.268  61.543  114.730 1.00 34.92 ? 2250 HOH   A O     1 
HETATM 19148 O  O     . HOH   Z  11 .    ? -18.181 92.448  107.385 1.00 34.36 ? 2251 HOH   A O     1 
HETATM 19149 O  O     . HOH   Z  11 .    ? -39.563 47.181  103.592 1.00 33.30 ? 2252 HOH   A O     1 
HETATM 19150 O  O     . HOH   Z  11 .    ? 4.458   86.119  100.552 1.00 28.43 ? 2253 HOH   A O     1 
HETATM 19151 O  O     . HOH   Z  11 .    ? 12.984  88.936  115.750 1.00 36.13 ? 2254 HOH   A O     1 
HETATM 19152 O  O     . HOH   Z  11 .    ? -39.978 47.502  106.192 1.00 36.96 ? 2255 HOH   A O     1 
HETATM 19153 O  O     . HOH   Z  11 .    ? 19.334  64.630  92.623  1.00 33.25 ? 2256 HOH   A O     1 
HETATM 19154 O  O     . HOH   Z  11 .    ? -37.263 75.506  97.217  1.00 29.44 ? 2257 HOH   A O     1 
HETATM 19155 O  O     . HOH   Z  11 .    ? 4.443   93.157  119.310 1.00 48.30 ? 2258 HOH   A O     1 
HETATM 19156 O  O     . HOH   Z  11 .    ? -20.373 54.785  98.574  1.00 30.08 ? 2259 HOH   A O     1 
HETATM 19157 O  O     . HOH   Z  11 .    ? -25.941 69.788  95.361  1.00 31.45 ? 2260 HOH   A O     1 
HETATM 19158 O  O     . HOH   Z  11 .    ? -2.200  91.139  105.213 1.00 29.88 ? 2261 HOH   A O     1 
HETATM 19159 O  O     . HOH   Z  11 .    ? 12.508  65.231  118.133 1.00 37.03 ? 2262 HOH   A O     1 
HETATM 19160 O  O     . HOH   Z  11 .    ? -5.560  90.712  119.436 1.00 38.11 ? 2263 HOH   A O     1 
HETATM 19161 O  O     . HOH   Z  11 .    ? -30.885 70.526  129.084 1.00 42.00 ? 2264 HOH   A O     1 
HETATM 19162 O  O     . HOH   Z  11 .    ? -56.589 40.324  67.254  1.00 36.91 ? 2265 HOH   A O     1 
HETATM 19163 O  O     . HOH   Z  11 .    ? -29.617 58.764  78.871  1.00 36.77 ? 2266 HOH   A O     1 
HETATM 19164 O  O     . HOH   Z  11 .    ? -56.388 33.742  95.234  1.00 44.47 ? 2267 HOH   A O     1 
HETATM 19165 O  O     . HOH   Z  11 .    ? -34.125 59.216  105.784 1.00 27.86 ? 2268 HOH   A O     1 
HETATM 19166 O  O     . HOH   Z  11 .    ? -3.335  75.300  101.536 1.00 29.19 ? 2269 HOH   A O     1 
HETATM 19167 O  O     . HOH   Z  11 .    ? -17.414 92.753  95.351  1.00 44.73 ? 2270 HOH   A O     1 
HETATM 19168 O  O     . HOH   Z  11 .    ? -17.212 67.838  134.619 1.00 46.43 ? 2271 HOH   A O     1 
HETATM 19169 O  O     . HOH   Z  11 .    ? -10.739 66.890  127.025 1.00 36.12 ? 2272 HOH   A O     1 
HETATM 19170 O  O     . HOH   Z  11 .    ? -45.322 92.731  98.308  1.00 42.13 ? 2273 HOH   A O     1 
HETATM 19171 O  O     . HOH   Z  11 .    ? -22.686 67.682  129.434 1.00 37.39 ? 2274 HOH   A O     1 
HETATM 19172 O  O     . HOH   Z  11 .    ? -61.952 59.922  95.461  1.00 25.26 ? 2275 HOH   A O     1 
HETATM 19173 O  O     . HOH   Z  11 .    ? 0.923   69.914  87.176  1.00 34.24 ? 2276 HOH   A O     1 
HETATM 19174 O  O     . HOH   Z  11 .    ? 15.019  82.573  118.724 1.00 31.41 ? 2277 HOH   A O     1 
HETATM 19175 O  O     . HOH   Z  11 .    ? 20.452  75.505  99.373  1.00 42.77 ? 2278 HOH   A O     1 
HETATM 19176 O  O     . HOH   Z  11 .    ? -42.364 85.408  104.946 1.00 34.28 ? 2279 HOH   A O     1 
HETATM 19177 O  O     . HOH   Z  11 .    ? -60.477 40.885  80.648  1.00 41.81 ? 2280 HOH   A O     1 
HETATM 19178 O  O     . HOH   Z  11 .    ? -18.697 59.826  107.847 1.00 32.65 ? 2281 HOH   A O     1 
HETATM 19179 O  O     . HOH   Z  11 .    ? -31.575 94.557  126.594 1.00 37.45 ? 2282 HOH   A O     1 
HETATM 19180 O  O     . HOH   Z  11 .    ? -9.099  73.439  131.347 1.00 41.06 ? 2283 HOH   A O     1 
HETATM 19181 O  O     . HOH   Z  11 .    ? -64.245 58.415  67.162  1.00 37.77 ? 2284 HOH   A O     1 
HETATM 19182 O  O     . HOH   Z  11 .    ? -31.572 38.516  99.207  1.00 44.13 ? 2285 HOH   A O     1 
HETATM 19183 O  O     . HOH   Z  11 .    ? -26.848 60.779  122.262 1.00 31.52 ? 2286 HOH   A O     1 
HETATM 19184 O  O     . HOH   Z  11 .    ? -35.018 70.800  82.317  1.00 38.43 ? 2287 HOH   A O     1 
HETATM 19185 O  O     . HOH   Z  11 .    ? -5.736  75.175  102.697 1.00 28.57 ? 2288 HOH   A O     1 
HETATM 19186 O  O     . HOH   Z  11 .    ? -9.022  41.357  69.014  1.00 37.70 ? 2289 HOH   A O     1 
HETATM 19187 O  O     . HOH   Z  11 .    ? -45.790 78.447  89.644  1.00 24.50 ? 2290 HOH   A O     1 
HETATM 19188 O  O     . HOH   Z  11 .    ? -44.173 76.395  74.260  1.00 32.67 ? 2291 HOH   A O     1 
HETATM 19189 O  O     . HOH   Z  11 .    ? -65.520 72.571  71.450  1.00 38.65 ? 2292 HOH   A O     1 
HETATM 19190 O  O     . HOH   Z  11 .    ? 21.050  71.479  94.418  1.00 38.62 ? 2293 HOH   A O     1 
HETATM 19191 O  O     . HOH   Z  11 .    ? -50.255 54.746  104.550 1.00 37.04 ? 2294 HOH   A O     1 
HETATM 19192 O  O     . HOH   Z  11 .    ? -41.975 89.375  115.088 1.00 41.86 ? 2295 HOH   A O     1 
HETATM 19193 O  O     . HOH   Z  11 .    ? -65.996 64.429  87.756  1.00 31.24 ? 2296 HOH   A O     1 
HETATM 19194 O  O     . HOH   Z  11 .    ? -41.855 75.676  120.048 1.00 46.30 ? 2297 HOH   A O     1 
HETATM 19195 O  O     . HOH   Z  11 .    ? -32.516 44.761  103.047 1.00 39.76 ? 2298 HOH   A O     1 
HETATM 19196 O  O     . HOH   Z  11 .    ? -25.962 74.669  132.249 1.00 35.43 ? 2299 HOH   A O     1 
HETATM 19197 O  O     . HOH   Z  11 .    ? -0.491  52.799  58.695  1.00 37.11 ? 2300 HOH   A O     1 
HETATM 19198 O  O     . HOH   Z  11 .    ? -0.023  67.098  86.030  1.00 36.08 ? 2301 HOH   A O     1 
HETATM 19199 O  O     . HOH   Z  11 .    ? -46.113 63.311  53.542  1.00 37.69 ? 2302 HOH   A O     1 
HETATM 19200 O  O     . HOH   Z  11 .    ? 8.232   69.693  124.696 1.00 43.41 ? 2303 HOH   A O     1 
HETATM 19201 O  O     . HOH   Z  11 .    ? -40.668 46.994  59.489  1.00 36.78 ? 2304 HOH   A O     1 
HETATM 19202 O  O     . HOH   Z  11 .    ? -21.054 53.071  88.324  1.00 39.80 ? 2305 HOH   A O     1 
HETATM 19203 O  O     . HOH   Z  11 .    ? -34.908 65.102  65.955  1.00 29.53 ? 2306 HOH   A O     1 
HETATM 19204 O  O     . HOH   Z  11 .    ? -62.124 67.300  60.329  1.00 38.10 ? 2307 HOH   A O     1 
HETATM 19205 O  O     . HOH   Z  11 .    ? -28.879 32.813  74.492  1.00 42.74 ? 2308 HOH   A O     1 
HETATM 19206 O  O     . HOH   Z  11 .    ? -54.489 41.395  66.845  1.00 40.97 ? 2309 HOH   A O     1 
HETATM 19207 O  O     . HOH   Z  11 .    ? -26.669 48.140  101.703 1.00 42.93 ? 2310 HOH   A O     1 
HETATM 19208 O  O     . HOH   Z  11 .    ? -20.926 74.303  104.012 1.00 38.50 ? 2311 HOH   A O     1 
HETATM 19209 O  O     . HOH   Z  11 .    ? -31.278 78.369  90.620  1.00 30.96 ? 2312 HOH   A O     1 
HETATM 19210 O  O     . HOH   Z  11 .    ? -60.848 68.883  91.642  1.00 38.94 ? 2313 HOH   A O     1 
HETATM 19211 O  O     . HOH   Z  11 .    ? -52.392 41.752  101.234 1.00 36.04 ? 2314 HOH   A O     1 
HETATM 19212 O  O     . HOH   Z  11 .    ? -35.388 60.247  88.465  1.00 33.19 ? 2315 HOH   A O     1 
HETATM 19213 O  O     . HOH   Z  11 .    ? -60.564 59.721  61.862  1.00 32.95 ? 2316 HOH   A O     1 
HETATM 19214 O  O     . HOH   Z  11 .    ? -32.077 98.665  98.853  1.00 43.43 ? 2317 HOH   A O     1 
HETATM 19215 O  O     . HOH   Z  11 .    ? -55.447 48.866  95.130  1.00 44.34 ? 2318 HOH   A O     1 
HETATM 19216 O  O     . HOH   Z  11 .    ? -23.869 100.588 100.632 1.00 40.87 ? 2319 HOH   A O     1 
HETATM 19217 O  O     . HOH   Z  11 .    ? 19.187  71.339  91.376  1.00 45.53 ? 2320 HOH   A O     1 
HETATM 19218 O  O     . HOH   Z  11 .    ? -36.938 74.866  64.133  1.00 39.87 ? 2321 HOH   A O     1 
HETATM 19219 O  O     . HOH   Z  11 .    ? -47.294 33.166  85.379  1.00 39.30 ? 2322 HOH   A O     1 
HETATM 19220 O  O     . HOH   Z  11 .    ? -17.405 65.153  134.034 1.00 44.01 ? 2323 HOH   A O     1 
HETATM 19221 O  O     . HOH   Z  11 .    ? -30.497 49.390  86.113  1.00 36.34 ? 2324 HOH   A O     1 
HETATM 19222 O  O     . HOH   Z  11 .    ? 5.142   71.319  95.781  1.00 36.06 ? 2325 HOH   A O     1 
HETATM 19223 O  O     . HOH   Z  11 .    ? -11.394 59.823  106.126 1.00 33.57 ? 2326 HOH   A O     1 
HETATM 19224 O  O     . HOH   Z  11 .    ? -7.563  73.124  103.099 1.00 31.66 ? 2327 HOH   A O     1 
HETATM 19225 O  O     . HOH   Z  11 .    ? -63.968 65.324  66.279  1.00 31.85 ? 2328 HOH   A O     1 
HETATM 19226 O  O     . HOH   Z  11 .    ? 13.468  83.253  95.790  1.00 45.07 ? 2329 HOH   A O     1 
HETATM 19227 O  O     . HOH   Z  11 .    ? -23.428 75.859  133.039 1.00 34.85 ? 2330 HOH   A O     1 
HETATM 19228 O  O     . HOH   Z  11 .    ? -10.055 66.862  74.037  1.00 33.94 ? 2331 HOH   A O     1 
HETATM 19229 O  O     . HOH   Z  11 .    ? -31.730 68.082  101.059 1.00 33.55 ? 2332 HOH   A O     1 
HETATM 19230 O  O     . HOH   Z  11 .    ? -64.419 63.286  68.263  1.00 33.12 ? 2333 HOH   A O     1 
HETATM 19231 O  O     . HOH   Z  11 .    ? -52.630 57.046  73.464  1.00 29.00 ? 2334 HOH   A O     1 
HETATM 19232 O  O     . HOH   Z  11 .    ? -55.751 31.561  75.047  1.00 42.58 ? 2335 HOH   A O     1 
HETATM 19233 O  O     . HOH   Z  11 .    ? -34.018 61.570  86.018  1.00 39.33 ? 2336 HOH   A O     1 
HETATM 19234 O  O     . HOH   Z  11 .    ? -22.692 74.118  69.494  1.00 32.98 ? 2337 HOH   A O     1 
HETATM 19235 O  O     . HOH   Z  11 .    ? -18.662 59.749  110.621 1.00 27.24 ? 2338 HOH   A O     1 
HETATM 19236 O  O     . HOH   Z  11 .    ? -9.296  55.113  96.297  1.00 43.99 ? 2339 HOH   A O     1 
HETATM 19237 O  O     . HOH   Z  11 .    ? -15.244 57.784  105.820 1.00 36.11 ? 2340 HOH   A O     1 
HETATM 19238 O  O     . HOH   Z  11 .    ? -28.532 67.315  92.912  1.00 44.60 ? 2341 HOH   A O     1 
HETATM 19239 O  O     . HOH   Z  11 .    ? 12.550  63.544  119.950 1.00 39.28 ? 2342 HOH   A O     1 
HETATM 19240 O  O     . HOH   Z  11 .    ? -39.958 67.896  88.816  1.00 30.55 ? 2343 HOH   A O     1 
HETATM 19241 O  O     . HOH   Z  11 .    ? -51.815 55.361  70.252  1.00 25.35 ? 2344 HOH   A O     1 
HETATM 19242 O  O     . HOH   Z  11 .    ? -19.053 54.665  118.005 1.00 41.47 ? 2345 HOH   A O     1 
HETATM 19243 O  O     . HOH   Z  11 .    ? -64.006 51.227  72.941  1.00 34.69 ? 2346 HOH   A O     1 
HETATM 19244 O  O     . HOH   Z  11 .    ? -60.889 72.767  81.628  1.00 36.59 ? 2347 HOH   A O     1 
HETATM 19245 O  O     . HOH   Z  11 .    ? -57.812 72.584  88.018  1.00 39.54 ? 2348 HOH   A O     1 
HETATM 19246 O  O     . HOH   Z  11 .    ? -26.060 67.666  93.745  1.00 35.76 ? 2349 HOH   A O     1 
HETATM 19247 O  O     . HOH   Z  11 .    ? -19.173 71.003  132.374 1.00 39.86 ? 2350 HOH   A O     1 
HETATM 19248 O  O     . HOH   Z  11 .    ? 12.485  88.564  118.343 1.00 39.91 ? 2351 HOH   A O     1 
HETATM 19249 O  O     . HOH   Z  11 .    ? -55.094 57.783  102.014 1.00 29.26 ? 2352 HOH   A O     1 
HETATM 19250 O  O     . HOH   Z  11 .    ? -26.837 65.553  102.442 1.00 26.04 ? 2353 HOH   A O     1 
HETATM 19251 O  O     . HOH   Z  11 .    ? -47.569 63.972  55.808  1.00 29.65 ? 2354 HOH   A O     1 
HETATM 19252 O  O     . HOH   Z  11 .    ? -31.170 73.946  128.479 1.00 43.50 ? 2355 HOH   A O     1 
HETATM 19253 O  O     . HOH   Z  11 .    ? -44.825 88.233  99.316  1.00 37.06 ? 2356 HOH   A O     1 
HETATM 19254 O  O     . HOH   Z  11 .    ? -50.032 24.044  80.365  1.00 46.76 ? 2357 HOH   A O     1 
HETATM 19255 O  O     . HOH   Z  11 .    ? -27.421 51.493  109.305 1.00 37.84 ? 2358 HOH   A O     1 
HETATM 19256 O  O     . HOH   Z  11 .    ? -40.969 66.754  70.505  1.00 30.32 ? 2359 HOH   A O     1 
HETATM 19257 O  O     . HOH   Z  11 .    ? -59.736 64.345  92.001  1.00 30.48 ? 2360 HOH   A O     1 
HETATM 19258 O  O     . HOH   Z  11 .    ? -51.187 68.626  107.512 1.00 38.52 ? 2361 HOH   A O     1 
HETATM 19259 O  O     . HOH   Z  11 .    ? -46.204 56.759  54.276  1.00 36.03 ? 2362 HOH   A O     1 
HETATM 19260 O  O     . HOH   Z  11 .    ? 7.660   62.695  112.038 1.00 34.34 ? 2363 HOH   A O     1 
HETATM 19261 O  O     . HOH   Z  11 .    ? -3.598  68.549  92.264  1.00 37.96 ? 2364 HOH   A O     1 
HETATM 19262 O  O     . HOH   Z  11 .    ? -23.126 71.346  73.756  1.00 33.78 ? 2365 HOH   A O     1 
HETATM 19263 O  O     . HOH   Z  11 .    ? -34.647 39.258  94.607  1.00 36.81 ? 2366 HOH   A O     1 
HETATM 19264 O  O     . HOH   Z  11 .    ? -7.254  65.894  92.113  1.00 38.83 ? 2367 HOH   A O     1 
HETATM 19265 O  O     . HOH   Z  11 .    ? -58.582 30.761  86.234  1.00 31.13 ? 2368 HOH   A O     1 
HETATM 19266 O  O     . HOH   Z  11 .    ? -28.645 65.636  128.682 1.00 43.75 ? 2369 HOH   A O     1 
HETATM 19267 O  O     . HOH   Z  11 .    ? -10.025 93.900  113.498 1.00 35.32 ? 2370 HOH   A O     1 
HETATM 19268 O  O     . HOH   Z  11 .    ? -33.033 84.342  76.641  1.00 29.65 ? 2371 HOH   A O     1 
HETATM 19269 O  O     . HOH   Z  11 .    ? -67.174 62.340  68.264  1.00 39.20 ? 2372 HOH   A O     1 
HETATM 19270 O  O     . HOH   Z  11 .    ? -48.368 30.902  68.848  1.00 44.63 ? 2373 HOH   A O     1 
HETATM 19271 O  O     . HOH   Z  11 .    ? 23.088  62.762  99.263  1.00 39.27 ? 2374 HOH   A O     1 
HETATM 19272 O  O     . HOH   Z  11 .    ? -50.676 81.161  83.290  1.00 37.06 ? 2375 HOH   A O     1 
HETATM 19273 O  O     . HOH   Z  11 .    ? -31.544 76.559  74.175  1.00 35.76 ? 2376 HOH   A O     1 
HETATM 19274 O  O     . HOH   Z  11 .    ? 15.945  83.540  115.839 1.00 39.54 ? 2377 HOH   A O     1 
HETATM 19275 O  O     . HOH   Z  11 .    ? -31.743 74.363  83.354  1.00 30.59 ? 2378 HOH   A O     1 
HETATM 19276 O  O     . HOH   Z  11 .    ? -62.897 61.201  93.121  1.00 32.70 ? 2379 HOH   A O     1 
HETATM 19277 O  O     . HOH   Z  11 .    ? -21.109 93.111  106.756 1.00 29.89 ? 2380 HOH   A O     1 
HETATM 19278 O  O     . HOH   Z  11 .    ? -15.393 68.640  136.766 1.00 46.52 ? 2381 HOH   A O     1 
HETATM 19279 O  O     . HOH   Z  11 .    ? -28.923 61.024  120.530 1.00 37.28 ? 2382 HOH   A O     1 
HETATM 19280 O  O     . HOH   Z  11 .    ? -10.950 41.234  57.225  1.00 44.77 ? 2383 HOH   A O     1 
HETATM 19281 O  O     . HOH   Z  11 .    ? -5.668  89.902  98.142  1.00 44.29 ? 2384 HOH   A O     1 
HETATM 19282 O  O     . HOH   Z  11 .    ? 0.519   63.913  92.723  1.00 42.53 ? 2385 HOH   A O     1 
HETATM 19283 O  O     . HOH   Z  11 .    ? -39.015 35.846  88.465  1.00 33.33 ? 2386 HOH   A O     1 
HETATM 19284 O  O     . HOH   Z  11 .    ? -27.640 64.026  90.297  1.00 35.13 ? 2387 HOH   A O     1 
HETATM 19285 O  O     . HOH   Z  11 .    ? -8.974  67.409  129.064 1.00 37.14 ? 2388 HOH   A O     1 
HETATM 19286 O  O     . HOH   Z  11 .    ? -43.952 61.780  105.029 1.00 45.08 ? 2389 HOH   A O     1 
HETATM 19287 O  O     . HOH   Z  11 .    ? 7.943   66.430  111.389 1.00 40.89 ? 2390 HOH   A O     1 
HETATM 19288 O  O     . HOH   Z  11 .    ? -44.078 23.430  78.088  1.00 43.73 ? 2391 HOH   A O     1 
HETATM 19289 O  O     . HOH   Z  11 .    ? -16.814 57.725  109.884 1.00 39.68 ? 2392 HOH   A O     1 
HETATM 19290 O  O     . HOH   Z  11 .    ? -21.385 63.140  81.053  1.00 39.00 ? 2393 HOH   A O     1 
HETATM 19291 O  O     . HOH   Z  11 .    ? -47.816 85.455  111.804 1.00 40.26 ? 2394 HOH   A O     1 
HETATM 19292 O  O     . HOH   Z  11 .    ? -28.545 80.481  131.336 1.00 43.50 ? 2395 HOH   A O     1 
HETATM 19293 O  O     . HOH   Z  11 .    ? -6.852  55.192  82.327  1.00 32.14 ? 2396 HOH   A O     1 
HETATM 19294 O  O     . HOH   Z  11 .    ? 4.873   60.698  97.833  1.00 25.87 ? 2397 HOH   A O     1 
HETATM 19295 O  O     . HOH   Z  11 .    ? -35.006 55.177  107.043 1.00 34.11 ? 2398 HOH   A O     1 
HETATM 19296 O  O     . HOH   Z  11 .    ? -58.262 74.679  94.683  1.00 39.32 ? 2399 HOH   A O     1 
HETATM 19297 O  O     . HOH   Z  11 .    ? -46.796 31.166  72.536  1.00 40.91 ? 2400 HOH   A O     1 
HETATM 19298 O  O     . HOH   Z  11 .    ? 7.440   91.640  117.871 1.00 41.66 ? 2401 HOH   A O     1 
HETATM 19299 O  O     . HOH   Z  11 .    ? 12.503  64.302  116.111 1.00 39.36 ? 2402 HOH   A O     1 
HETATM 19300 O  O     . HOH   Z  11 .    ? -35.321 73.670  86.274  1.00 30.55 ? 2403 HOH   A O     1 
HETATM 19301 O  O     . HOH   Z  11 .    ? -34.585 76.380  87.023  1.00 28.33 ? 2404 HOH   A O     1 
HETATM 19302 O  O     . HOH   Z  11 .    ? -2.716  57.017  70.258  1.00 32.86 ? 2405 HOH   A O     1 
HETATM 19303 O  O     . HOH   Z  11 .    ? -24.724 65.870  96.584  1.00 33.91 ? 2406 HOH   A O     1 
HETATM 19304 O  O     . HOH   Z  11 .    ? -45.232 28.972  86.776  1.00 37.25 ? 2407 HOH   A O     1 
HETATM 19305 O  O     . HOH   Z  11 .    ? -17.262 96.990  91.772  1.00 34.08 ? 2408 HOH   A O     1 
HETATM 19306 O  O     . HOH   Z  11 .    ? -10.600 78.726  91.971  1.00 19.96 ? 2409 HOH   A O     1 
HETATM 19307 O  O     . HOH   Z  11 .    ? -65.675 54.473  78.234  1.00 33.48 ? 2410 HOH   A O     1 
HETATM 19308 O  O     . HOH   Z  11 .    ? -9.738  66.981  131.969 1.00 37.25 ? 2411 HOH   A O     1 
HETATM 19309 O  O     . HOH   Z  11 .    ? -55.908 32.641  76.969  1.00 41.09 ? 2412 HOH   A O     1 
HETATM 19310 O  O     . HOH   Z  11 .    ? -52.502 48.610  57.591  1.00 41.50 ? 2413 HOH   A O     1 
HETATM 19311 O  O     . HOH   Z  11 .    ? -66.400 72.844  77.729  1.00 41.12 ? 2414 HOH   A O     1 
HETATM 19312 O  O     . HOH   Z  11 .    ? -43.487 24.655  80.113  1.00 44.12 ? 2415 HOH   A O     1 
HETATM 19313 O  O     . HOH   Z  11 .    ? -44.414 83.466  85.767  1.00 44.31 ? 2416 HOH   A O     1 
HETATM 19314 O  O     . HOH   Z  11 .    ? -24.383 97.141  120.603 1.00 39.99 ? 2417 HOH   A O     1 
HETATM 19315 O  O     . HOH   Z  11 .    ? 6.563   67.075  93.379  1.00 34.76 ? 2418 HOH   A O     1 
HETATM 19316 O  O     . HOH   Z  11 .    ? 17.124  84.106  112.395 1.00 36.17 ? 2419 HOH   A O     1 
HETATM 19317 O  O     . HOH   Z  11 .    ? -29.951 79.816  125.153 1.00 35.78 ? 2420 HOH   A O     1 
HETATM 19318 O  O     . HOH   Z  11 .    ? -24.186 77.672  68.036  1.00 41.00 ? 2421 HOH   A O     1 
HETATM 19319 O  O     . HOH   Z  11 .    ? 11.063  90.856  119.029 1.00 43.72 ? 2422 HOH   A O     1 
HETATM 19320 O  O     . HOH   Z  11 .    ? -54.391 78.159  85.599  1.00 37.33 ? 2423 HOH   A O     1 
HETATM 19321 O  O     . HOH   Z  11 .    ? -63.374 48.961  71.750  1.00 39.24 ? 2424 HOH   A O     1 
HETATM 19322 O  O     . HOH   Z  11 .    ? -55.891 32.284  92.025  1.00 39.83 ? 2425 HOH   A O     1 
HETATM 19323 O  O     . HOH   Z  11 .    ? -52.216 74.291  61.727  1.00 23.07 ? 2426 HOH   A O     1 
HETATM 19324 O  O     . HOH   Z  11 .    ? -8.350  61.659  86.481  1.00 38.15 ? 2427 HOH   A O     1 
HETATM 19325 O  O     . HOH   Z  11 .    ? -3.604  69.651  94.614  1.00 43.34 ? 2428 HOH   A O     1 
HETATM 19326 O  O     . HOH   Z  11 .    ? -37.821 74.554  92.930  1.00 34.27 ? 2429 HOH   A O     1 
HETATM 19327 O  O     . HOH   Z  11 .    ? -53.102 45.665  94.342  1.00 33.21 ? 2430 HOH   A O     1 
HETATM 19328 O  O     . HOH   Z  11 .    ? -36.016 87.766  77.465  1.00 45.00 ? 2431 HOH   A O     1 
HETATM 19329 O  O     . HOH   Z  11 .    ? -41.590 48.869  107.897 1.00 44.81 ? 2432 HOH   A O     1 
HETATM 19330 O  O     . HOH   Z  11 .    ? -41.791 64.180  105.921 1.00 36.80 ? 2433 HOH   A O     1 
HETATM 19331 O  O     . HOH   Z  11 .    ? -56.673 30.737  73.082  1.00 48.48 ? 2434 HOH   A O     1 
HETATM 19332 O  O     . HOH   Z  11 .    ? -56.351 74.686  79.112  1.00 31.64 ? 2435 HOH   A O     1 
HETATM 19333 O  O     . HOH   Z  11 .    ? -52.931 66.658  101.656 1.00 34.49 ? 2436 HOH   A O     1 
HETATM 19334 O  O     . HOH   Z  11 .    ? -27.376 65.475  86.114  1.00 41.16 ? 2437 HOH   A O     1 
HETATM 19335 O  O     . HOH   Z  11 .    ? -27.015 59.499  116.003 1.00 37.37 ? 2438 HOH   A O     1 
HETATM 19336 O  O     . HOH   Z  11 .    ? -0.648  79.536  94.578  1.00 44.63 ? 2439 HOH   A O     1 
HETATM 19337 O  O     . HOH   Z  11 .    ? -66.883 66.117  83.027  1.00 25.76 ? 2440 HOH   A O     1 
HETATM 19338 O  O     . HOH   Z  11 .    ? -25.919 83.284  69.517  1.00 41.68 ? 2441 HOH   A O     1 
HETATM 19339 O  O     . HOH   Z  11 .    ? -33.484 81.241  122.195 1.00 32.90 ? 2442 HOH   A O     1 
HETATM 19340 O  O     . HOH   Z  11 .    ? -52.314 64.153  100.430 1.00 30.56 ? 2443 HOH   A O     1 
HETATM 19341 O  O     . HOH   Z  11 .    ? -11.318 96.220  111.570 1.00 39.30 ? 2444 HOH   A O     1 
HETATM 19342 O  O     . HOH   Z  11 .    ? 16.083  66.596  89.653  1.00 38.17 ? 2445 HOH   A O     1 
HETATM 19343 O  O     . HOH   Z  11 .    ? -36.051 63.289  90.038  1.00 34.07 ? 2446 HOH   A O     1 
HETATM 19344 O  O     . HOH   Z  11 .    ? 3.062   74.374  87.277  1.00 42.02 ? 2447 HOH   A O     1 
HETATM 19345 O  O     . HOH   Z  11 .    ? -14.654 57.979  123.633 1.00 38.56 ? 2448 HOH   A O     1 
HETATM 19346 O  O     . HOH   Z  11 .    ? 2.339   75.102  119.128 1.00 40.62 ? 2449 HOH   A O     1 
HETATM 19347 O  O     . HOH   Z  11 .    ? -33.674 80.807  74.214  1.00 30.23 ? 2450 HOH   A O     1 
HETATM 19348 O  O     . HOH   Z  11 .    ? -35.244 39.162  89.449  1.00 38.44 ? 2451 HOH   A O     1 
HETATM 19349 O  O     . HOH   Z  11 .    ? 18.618  89.462  110.704 1.00 42.57 ? 2452 HOH   A O     1 
HETATM 19350 O  O     . HOH   Z  11 .    ? -26.975 93.593  109.613 1.00 40.30 ? 2453 HOH   A O     1 
HETATM 19351 O  O     . HOH   Z  11 .    ? 20.328  61.891  95.798  1.00 31.23 ? 2454 HOH   A O     1 
HETATM 19352 O  O     . HOH   Z  11 .    ? -57.844 32.504  90.001  1.00 27.46 ? 2455 HOH   A O     1 
HETATM 19353 O  O     . HOH   Z  11 .    ? -8.821  58.207  92.181  1.00 43.17 ? 2456 HOH   A O     1 
HETATM 19354 O  O     . HOH   Z  11 .    ? -25.608 65.187  91.385  1.00 36.83 ? 2457 HOH   A O     1 
HETATM 19355 O  O     . HOH   Z  11 .    ? -45.050 29.778  98.630  1.00 41.61 ? 2458 HOH   A O     1 
HETATM 19356 O  O     . HOH   Z  11 .    ? -36.009 90.520  123.167 1.00 37.94 ? 2459 HOH   A O     1 
HETATM 19357 O  O     . HOH   Z  11 .    ? 20.796  70.853  117.944 1.00 42.63 ? 2460 HOH   A O     1 
HETATM 19358 O  O     . HOH   Z  11 .    ? -37.266 63.142  113.714 1.00 36.13 ? 2461 HOH   A O     1 
HETATM 19359 O  O     . HOH   Z  11 .    ? -48.624 81.402  87.367  1.00 39.68 ? 2462 HOH   A O     1 
HETATM 19360 O  O     . HOH   Z  11 .    ? -24.828 97.343  125.545 1.00 41.37 ? 2463 HOH   A O     1 
HETATM 19361 O  O     . HOH   Z  11 .    ? -40.952 68.496  93.277  1.00 31.31 ? 2464 HOH   A O     1 
HETATM 19362 O  O     . HOH   Z  11 .    ? -4.217  65.197  91.282  1.00 43.67 ? 2465 HOH   A O     1 
HETATM 19363 O  O     . HOH   Z  11 .    ? -52.530 55.257  104.556 1.00 44.23 ? 2466 HOH   A O     1 
HETATM 19364 O  O     . HOH   Z  11 .    ? 3.742   64.947  95.876  1.00 26.16 ? 2467 HOH   A O     1 
HETATM 19365 O  O     . HOH   Z  11 .    ? -36.072 38.088  86.354  1.00 39.92 ? 2468 HOH   A O     1 
HETATM 19366 O  O     . HOH   Z  11 .    ? -10.797 66.125  72.018  1.00 41.51 ? 2469 HOH   A O     1 
HETATM 19367 O  O     . HOH   Z  11 .    ? -56.654 44.263  92.073  1.00 36.57 ? 2470 HOH   A O     1 
HETATM 19368 O  O     . HOH   Z  11 .    ? -18.477 74.650  108.829 1.00 22.23 ? 2471 HOH   A O     1 
HETATM 19369 O  O     . HOH   Z  11 .    ? -22.685 91.555  103.290 1.00 35.25 ? 2472 HOH   A O     1 
HETATM 19370 O  O     . HOH   Z  11 .    ? -25.400 62.240  101.832 1.00 30.11 ? 2473 HOH   A O     1 
HETATM 19371 O  O     . HOH   Z  11 .    ? -9.410  63.966  91.236  1.00 43.19 ? 2474 HOH   A O     1 
HETATM 19372 O  O     . HOH   Z  11 .    ? -10.257 62.389  89.259  1.00 43.00 ? 2475 HOH   A O     1 
HETATM 19373 O  O     . HOH   Z  11 .    ? -38.354 91.133  122.320 1.00 43.50 ? 2476 HOH   A O     1 
HETATM 19374 O  O     . HOH   Z  11 .    ? -30.901 70.629  87.063  1.00 39.39 ? 2477 HOH   A O     1 
HETATM 19375 O  O     . HOH   Z  11 .    ? -52.273 76.262  90.830  1.00 40.23 ? 2478 HOH   A O     1 
HETATM 19376 O  O     . HOH   Z  11 .    ? -8.844  57.670  83.978  1.00 38.88 ? 2479 HOH   A O     1 
HETATM 19377 O  O     . HOH   Z  11 .    ? -62.442 53.893  65.392  1.00 35.88 ? 2480 HOH   A O     1 
HETATM 19378 O  O     . HOH   Z  11 .    ? -64.509 67.542  89.087  1.00 46.00 ? 2481 HOH   A O     1 
HETATM 19379 O  O     . HOH   Z  11 .    ? -48.359 56.833  55.761  1.00 32.76 ? 2482 HOH   A O     1 
HETATM 19380 O  O     . HOH   Z  11 .    ? -28.613 76.198  129.498 1.00 38.34 ? 2483 HOH   A O     1 
HETATM 19381 O  O     . HOH   Z  11 .    ? -53.111 69.149  100.503 1.00 30.80 ? 2484 HOH   A O     1 
HETATM 19382 O  O     . HOH   Z  11 .    ? -2.028  74.127  118.272 1.00 39.67 ? 2485 HOH   A O     1 
HETATM 19383 O  O     . HOH   Z  11 .    ? -9.048  73.833  128.812 1.00 40.80 ? 2486 HOH   A O     1 
HETATM 19384 O  O     . HOH   Z  11 .    ? 1.028   71.438  116.951 1.00 40.53 ? 2487 HOH   A O     1 
HETATM 19385 O  O     . HOH   Z  11 .    ? -45.226 94.836  97.350  1.00 42.28 ? 2488 HOH   A O     1 
HETATM 19386 O  O     . HOH   Z  11 .    ? 18.280  64.602  89.931  1.00 38.47 ? 2489 HOH   A O     1 
HETATM 19387 O  O     . HOH   Z  11 .    ? -58.639 55.463  100.571 1.00 38.98 ? 2490 HOH   A O     1 
HETATM 19388 O  O     . HOH   Z  11 .    ? -46.631 80.974  89.451  1.00 35.92 ? 2491 HOH   A O     1 
HETATM 19389 O  O     . HOH   Z  11 .    ? -40.940 82.611  68.661  1.00 34.31 ? 2492 HOH   A O     1 
HETATM 19390 O  O     . HOH   Z  11 .    ? -0.418  86.250  96.522  1.00 40.23 ? 2493 HOH   A O     1 
HETATM 19391 O  O     . HOH   Z  11 .    ? -8.176  76.847  128.947 1.00 43.00 ? 2494 HOH   A O     1 
HETATM 19392 O  O     . HOH   Z  11 .    ? -56.729 72.886  98.776  1.00 41.33 ? 2495 HOH   A O     1 
HETATM 19393 O  O     . HOH   Z  11 .    ? -5.957  62.367  92.879  1.00 43.01 ? 2496 HOH   A O     1 
HETATM 19394 O  O     . HOH   Z  11 .    ? -52.032 73.266  102.354 1.00 27.43 ? 2497 HOH   A O     1 
HETATM 19395 O  O     . HOH   Z  11 .    ? 23.101  70.378  115.298 1.00 34.17 ? 2498 HOH   A O     1 
HETATM 19396 O  O     . HOH   Z  11 .    ? 1.489   58.916  113.722 1.00 44.99 ? 2499 HOH   A O     1 
HETATM 19397 O  O     . HOH   Z  11 .    ? -36.705 82.470  76.864  1.00 35.64 ? 2500 HOH   A O     1 
HETATM 19398 O  O     . HOH   Z  11 .    ? -3.965  79.995  124.532 1.00 36.15 ? 2501 HOH   A O     1 
HETATM 19399 O  O     . HOH   Z  11 .    ? -14.820 48.585  51.123  1.00 38.47 ? 2502 HOH   A O     1 
HETATM 19400 O  O     . HOH   Z  11 .    ? -54.103 59.049  104.150 1.00 46.80 ? 2503 HOH   A O     1 
HETATM 19401 O  O     . HOH   Z  11 .    ? -66.544 47.821  73.217  1.00 30.45 ? 2504 HOH   A O     1 
HETATM 19402 O  O     . HOH   Z  11 .    ? -29.383 92.504  108.588 1.00 32.44 ? 2505 HOH   A O     1 
HETATM 19403 O  O     . HOH   Z  11 .    ? -0.625  60.940  111.932 1.00 35.88 ? 2506 HOH   A O     1 
HETATM 19404 O  O     . HOH   Z  11 .    ? 7.436   76.663  127.465 1.00 42.88 ? 2507 HOH   A O     1 
HETATM 19405 O  O     . HOH   Z  11 .    ? -2.255  91.868  97.932  1.00 31.88 ? 2508 HOH   A O     1 
HETATM 19406 O  O     . HOH   Z  11 .    ? 10.648  68.612  113.927 1.00 35.00 ? 2509 HOH   A O     1 
HETATM 19407 O  O     . HOH   Z  11 .    ? -26.742 66.731  97.825  1.00 36.29 ? 2510 HOH   A O     1 
HETATM 19408 O  O     . HOH   Z  11 .    ? -32.518 58.648  84.315  1.00 38.62 ? 2511 HOH   A O     1 
HETATM 19409 O  O     . HOH   Z  11 .    ? -56.462 49.587  97.786  1.00 43.82 ? 2512 HOH   A O     1 
HETATM 19410 O  O     . HOH   Z  11 .    ? -49.115 77.764  93.525  1.00 34.89 ? 2513 HOH   A O     1 
HETATM 19411 O  O     . HOH   Z  11 .    ? -32.135 75.481  85.026  1.00 33.14 ? 2514 HOH   A O     1 
HETATM 19412 O  O     . HOH   Z  11 .    ? -33.142 58.548  113.165 1.00 40.47 ? 2515 HOH   A O     1 
HETATM 19413 O  O     . HOH   Z  11 .    ? -18.826 46.909  52.753  1.00 39.36 ? 2516 HOH   A O     1 
HETATM 19414 O  O     . HOH   Z  11 .    ? -44.043 28.938  90.458  1.00 40.83 ? 2517 HOH   A O     1 
HETATM 19415 O  O     . HOH   Z  11 .    ? -28.657 77.713  69.943  1.00 35.32 ? 2518 HOH   A O     1 
HETATM 19416 O  O     . HOH   Z  11 .    ? -30.926 84.239  72.994  1.00 39.06 ? 2519 HOH   A O     1 
HETATM 19417 O  O     . HOH   Z  11 .    ? -68.693 69.826  79.944  1.00 31.49 ? 2520 HOH   A O     1 
HETATM 19418 O  O     . HOH   Z  11 .    ? -54.344 55.165  102.172 1.00 36.95 ? 2521 HOH   A O     1 
HETATM 19419 O  O     . HOH   Z  11 .    ? -47.777 37.609  100.244 1.00 36.84 ? 2522 HOH   A O     1 
HETATM 19420 O  O     . HOH   Z  11 .    ? -38.999 30.170  95.202  1.00 45.28 ? 2523 HOH   A O     1 
HETATM 19421 O  O     . HOH   Z  11 .    ? -55.329 46.311  64.994  1.00 36.96 ? 2524 HOH   A O     1 
HETATM 19422 O  O     . HOH   Z  11 .    ? -9.385  62.362  93.708  1.00 31.78 ? 2525 HOH   A O     1 
HETATM 19423 O  O     . HOH   Z  11 .    ? 6.710   62.816  94.298  1.00 29.42 ? 2526 HOH   A O     1 
HETATM 19424 O  O     . HOH   Z  11 .    ? -54.572 80.114  83.741  1.00 41.41 ? 2527 HOH   A O     1 
HETATM 19425 O  O     . HOH   Z  11 .    ? -8.684  52.828  100.927 1.00 39.79 ? 2528 HOH   A O     1 
HETATM 19426 O  O     . HOH   Z  11 .    ? -4.035  88.181  96.541  1.00 38.34 ? 2529 HOH   A O     1 
HETATM 19427 O  O     . HOH   Z  11 .    ? -31.712 54.776  110.544 1.00 41.32 ? 2530 HOH   A O     1 
HETATM 19428 O  O     . HOH   Z  11 .    ? 23.848  58.209  100.210 1.00 35.74 ? 2531 HOH   A O     1 
HETATM 19429 O  O     . HOH   Z  11 .    ? -44.586 82.694  88.447  1.00 39.08 ? 2532 HOH   A O     1 
HETATM 19430 O  O     . HOH   Z  11 .    ? -62.631 55.536  69.654  1.00 30.22 ? 2533 HOH   A O     1 
HETATM 19431 O  O     . HOH   Z  11 .    ? 5.701   56.282  94.189  1.00 44.87 ? 2534 HOH   A O     1 
HETATM 19432 O  O     . HOH   Z  11 .    ? -30.022 60.266  85.561  1.00 32.00 ? 2535 HOH   A O     1 
HETATM 19433 O  O     . HOH   Z  11 .    ? -30.705 86.840  74.123  1.00 45.48 ? 2536 HOH   A O     1 
HETATM 19434 O  O     . HOH   Z  11 .    ? -58.341 59.754  102.636 1.00 38.39 ? 2537 HOH   A O     1 
HETATM 19435 O  O     . HOH   Z  11 .    ? -3.355  83.584  111.847 1.00 33.43 ? 2538 HOH   A O     1 
HETATM 19436 O  O     . HOH   Z  11 .    ? -29.278 60.065  88.305  1.00 22.24 ? 2539 HOH   A O     1 
HETATM 19437 O  O     . HOH   Z  11 .    ? -56.220 76.415  80.653  1.00 38.81 ? 2540 HOH   A O     1 
HETATM 19438 O  O     . HOH   Z  11 .    ? -24.577 52.234  99.755  1.00 31.50 ? 2541 HOH   A O     1 
HETATM 19439 O  O     . HOH   Z  11 .    ? -9.844  49.283  106.632 1.00 39.60 ? 2542 HOH   A O     1 
HETATM 19440 O  O     . HOH   Z  11 .    ? -65.099 56.681  69.069  1.00 37.28 ? 2543 HOH   A O     1 
HETATM 19441 O  O     . HOH   Z  11 .    ? -32.353 65.631  124.199 1.00 33.51 ? 2544 HOH   A O     1 
HETATM 19442 O  O     . HOH   Z  11 .    ? -51.703 47.246  96.247  1.00 29.28 ? 2545 HOH   A O     1 
HETATM 19443 O  O     . HOH   Z  11 .    ? -56.564 76.350  76.610  1.00 30.12 ? 2546 HOH   A O     1 
HETATM 19444 O  O     . HOH   Z  11 .    ? -7.188  69.601  129.609 1.00 42.80 ? 2547 HOH   A O     1 
HETATM 19445 O  O     . HOH   Z  11 .    ? -2.677  85.123  96.241  1.00 31.86 ? 2548 HOH   A O     1 
HETATM 19446 O  O     . HOH   Z  11 .    ? -1.761  75.289  120.458 1.00 39.44 ? 2549 HOH   A O     1 
HETATM 19447 O  O     . HOH   Z  11 .    ? -61.694 50.938  66.240  1.00 39.44 ? 2550 HOH   A O     1 
HETATM 19448 O  O     . HOH   Z  11 .    ? -52.541 66.434  104.439 1.00 36.08 ? 2551 HOH   A O     1 
HETATM 19449 O  O     . HOH   Z  11 .    ? -18.521 74.011  105.846 1.00 25.40 ? 2552 HOH   A O     1 
HETATM 19450 O  O     . HOH   Z  11 .    ? -35.432 84.823  76.552  1.00 42.82 ? 2553 HOH   A O     1 
HETATM 19451 O  O     . HOH   Z  11 .    ? -33.294 76.641  89.586  1.00 38.48 ? 2554 HOH   A O     1 
HETATM 19452 O  O     . HOH   Z  11 .    ? 12.606  62.758  92.742  1.00 33.93 ? 2555 HOH   A O     1 
HETATM 19453 O  O     . HOH   Z  11 .    ? 3.674   69.484  87.921  1.00 36.35 ? 2556 HOH   A O     1 
HETATM 19454 O  O     . HOH   Z  11 .    ? -15.118 39.597  70.111  1.00 43.78 ? 2557 HOH   A O     1 
HETATM 19455 O  O     . HOH   Z  11 .    ? -19.141 57.602  106.273 1.00 31.92 ? 2558 HOH   A O     1 
HETATM 19456 O  O     . HOH   Z  11 .    ? -24.029 50.564  95.013  1.00 36.73 ? 2559 HOH   A O     1 
HETATM 19457 O  O     . HOH   Z  11 .    ? -61.484 70.781  85.396  1.00 33.81 ? 2560 HOH   A O     1 
HETATM 19458 O  O     . HOH   Z  11 .    ? 5.294   70.464  86.646  1.00 40.54 ? 2561 HOH   A O     1 
HETATM 19459 O  O     . HOH   Z  11 .    ? -63.357 57.627  96.071  1.00 37.57 ? 2562 HOH   A O     1 
HETATM 19460 O  O     . HOH   Z  11 .    ? -56.801 52.675  98.427  1.00 32.55 ? 2563 HOH   A O     1 
HETATM 19461 O  O     . HOH   Z  11 .    ? -61.669 52.987  93.627  1.00 40.54 ? 2564 HOH   A O     1 
HETATM 19462 O  O     . HOH   Z  11 .    ? -12.358 61.910  104.759 1.00 31.16 ? 2565 HOH   A O     1 
HETATM 19463 O  O     . HOH   Z  11 .    ? 2.762   71.182  94.801  1.00 40.59 ? 2566 HOH   A O     1 
HETATM 19464 O  O     . HOH   Z  11 .    ? -8.293  71.119  131.880 1.00 43.38 ? 2567 HOH   A O     1 
HETATM 19465 O  O     . HOH   Z  11 .    ? -54.848 53.068  100.292 1.00 32.44 ? 2568 HOH   A O     1 
HETATM 19466 O  O     . HOH   Z  11 .    ? -8.923  43.303  57.507  1.00 36.27 ? 2569 HOH   A O     1 
HETATM 19467 O  O     . HOH   Z  11 .    ? -21.641 68.893  131.813 1.00 42.68 ? 2570 HOH   A O     1 
HETATM 19468 O  O     . HOH   Z  11 .    ? -34.839 64.149  121.276 1.00 39.89 ? 2571 HOH   A O     1 
HETATM 19469 O  O     . HOH   Z  11 .    ? 20.710  73.771  95.879  1.00 39.43 ? 2572 HOH   A O     1 
HETATM 19470 O  O     . HOH   Z  11 .    ? -25.065 62.885  99.438  1.00 29.47 ? 2573 HOH   A O     1 
HETATM 19471 O  O     . HOH   Z  11 .    ? -44.879 61.057  52.918  1.00 35.47 ? 2574 HOH   A O     1 
HETATM 19472 O  O     . HOH   Z  11 .    ? -57.025 28.289  91.946  1.00 36.38 ? 2575 HOH   A O     1 
HETATM 19473 O  O     . HOH   Z  11 .    ? -37.897 69.351  95.413  1.00 34.83 ? 2576 HOH   A O     1 
HETATM 19474 O  O     . HOH   Z  11 .    ? -31.654 61.748  121.375 1.00 38.45 ? 2577 HOH   A O     1 
HETATM 19475 O  O     . HOH   Z  11 .    ? -46.190 39.074  104.090 1.00 34.33 ? 2578 HOH   A O     1 
HETATM 19476 O  O     . HOH   Z  11 .    ? 11.123  64.820  92.683  1.00 34.05 ? 2579 HOH   A O     1 
HETATM 19477 O  O     . HOH   Z  11 .    ? 22.603  63.314  94.775  1.00 40.27 ? 2580 HOH   A O     1 
HETATM 19478 O  O     . HOH   Z  11 .    ? -42.050 61.973  52.496  1.00 43.84 ? 2581 HOH   A O     1 
HETATM 19479 O  O     . HOH   Z  11 .    ? -55.012 42.476  62.620  1.00 44.01 ? 2582 HOH   A O     1 
HETATM 19480 O  O     . HOH   Z  11 .    ? -49.748 86.632  110.169 1.00 44.52 ? 2583 HOH   A O     1 
HETATM 19481 O  O     . HOH   Z  11 .    ? -47.808 59.460  55.267  1.00 39.46 ? 2584 HOH   A O     1 
HETATM 19482 O  O     . HOH   Z  11 .    ? -39.117 71.985  95.352  1.00 34.74 ? 2585 HOH   A O     1 
HETATM 19483 O  O     . HOH   Z  11 .    ? -32.977 57.491  110.618 1.00 33.71 ? 2586 HOH   A O     1 
HETATM 19484 O  O     . HOH   Z  11 .    ? 6.697   59.959  93.962  1.00 39.24 ? 2587 HOH   A O     1 
HETATM 19485 O  O     . HOH   Z  11 .    ? -35.470 39.509  73.255  1.00 42.62 ? 2588 HOH   A O     1 
HETATM 19486 O  O     . HOH   Z  11 .    ? 13.715  66.089  90.124  1.00 35.71 ? 2589 HOH   A O     1 
HETATM 19487 O  O     . HOH   Z  11 .    ? -33.238 78.408  70.845  1.00 38.68 ? 2590 HOH   A O     1 
HETATM 19488 O  O     . HOH   Z  11 .    ? -37.113 34.465  89.623  1.00 37.87 ? 2591 HOH   A O     1 
HETATM 19489 O  O     . HOH   Z  11 .    ? -34.405 78.951  126.227 1.00 38.09 ? 2592 HOH   A O     1 
HETATM 19490 O  O     . HOH   Z  11 .    ? -68.182 70.291  68.890  1.00 34.21 ? 2593 HOH   A O     1 
HETATM 19491 O  O     . HOH   Z  11 .    ? -36.144 81.232  69.768  1.00 45.38 ? 2594 HOH   A O     1 
HETATM 19492 O  O     . HOH   Z  11 .    ? -35.444 56.902  109.041 1.00 41.35 ? 2595 HOH   A O     1 
HETATM 19493 O  O     . HOH   Z  11 .    ? -36.531 32.285  90.421  1.00 37.29 ? 2596 HOH   A O     1 
HETATM 19494 O  O     . HOH   Z  11 .    ? -53.961 71.329  102.108 1.00 35.01 ? 2597 HOH   A O     1 
HETATM 19495 O  O     . HOH   Z  11 .    ? -53.656 47.737  98.243  1.00 34.27 ? 2598 HOH   A O     1 
HETATM 19496 O  O     . HOH   Z  11 .    ? 13.576  63.430  90.186  1.00 37.49 ? 2599 HOH   A O     1 
HETATM 19497 O  O     . HOH   Z  11 .    ? -33.884 81.438  71.316  1.00 38.94 ? 2600 HOH   A O     1 
HETATM 19498 O  O     . HOH   AA 11 .    ? 30.428  42.281  66.525  1.00 27.86 ? 1401 HOH   B O     1 
HETATM 19499 O  O     . HOH   AA 11 .    ? 8.491   31.567  80.944  1.00 32.84 ? 1402 HOH   B O     1 
HETATM 19500 O  O     . HOH   AA 11 .    ? -11.171 27.998  80.784  1.00 28.66 ? 1403 HOH   B O     1 
HETATM 19501 O  O     . HOH   AA 11 .    ? 0.470   77.878  69.050  1.00 33.95 ? 1404 HOH   B O     1 
HETATM 19502 O  O     . HOH   AA 11 .    ? -0.741  48.018  87.059  1.00 37.49 ? 1405 HOH   B O     1 
HETATM 19503 O  O     . HOH   AA 11 .    ? 3.889   72.568  85.155  1.00 36.48 ? 1406 HOH   B O     1 
HETATM 19504 O  O     . HOH   AA 11 .    ? 21.086  40.256  47.516  1.00 38.14 ? 1407 HOH   B O     1 
HETATM 19505 O  O     . HOH   AA 11 .    ? -0.011  18.886  80.080  1.00 26.41 ? 1408 HOH   B O     1 
HETATM 19506 O  O     . HOH   AA 11 .    ? -0.890  46.425  132.643 1.00 45.84 ? 1409 HOH   B O     1 
HETATM 19507 O  O     . HOH   AA 11 .    ? -2.420  29.592  57.156  1.00 36.73 ? 1410 HOH   B O     1 
HETATM 19508 O  O     . HOH   AA 11 .    ? 6.894   51.553  57.142  1.00 32.19 ? 1411 HOH   B O     1 
HETATM 19509 O  O     . HOH   AA 11 .    ? 30.146  35.540  50.409  1.00 29.33 ? 1412 HOH   B O     1 
HETATM 19510 O  O     . HOH   AA 11 .    ? 12.166  45.410  108.596 1.00 38.35 ? 1413 HOH   B O     1 
HETATM 19511 O  O     . HOH   AA 11 .    ? -19.746 28.318  90.824  1.00 37.28 ? 1414 HOH   B O     1 
HETATM 19512 O  O     . HOH   AA 11 .    ? 2.157   17.434  111.931 1.00 32.20 ? 1415 HOH   B O     1 
HETATM 19513 O  O     . HOH   AA 11 .    ? 6.406   15.895  123.944 1.00 36.77 ? 1416 HOH   B O     1 
HETATM 19514 O  O     . HOH   AA 11 .    ? -14.576 -7.013  107.328 1.00 40.31 ? 1417 HOH   B O     1 
HETATM 19515 O  O     . HOH   AA 11 .    ? 34.173  41.580  90.601  1.00 32.26 ? 1418 HOH   B O     1 
HETATM 19516 O  O     . HOH   AA 11 .    ? 4.046   55.616  72.090  1.00 25.29 ? 1419 HOH   B O     1 
HETATM 19517 O  O     . HOH   AA 11 .    ? 12.120  6.675   117.322 1.00 38.33 ? 1420 HOH   B O     1 
HETATM 19518 O  O     . HOH   AA 11 .    ? -16.476 -8.058  105.754 1.00 30.93 ? 1421 HOH   B O     1 
HETATM 19519 O  O     . HOH   AA 11 .    ? -2.075  62.547  69.227  1.00 33.50 ? 1422 HOH   B O     1 
HETATM 19520 O  O     . HOH   AA 11 .    ? 3.544   56.345  62.487  1.00 43.08 ? 1423 HOH   B O     1 
HETATM 19521 O  O     . HOH   AA 11 .    ? -14.153 54.255  117.623 1.00 29.95 ? 1424 HOH   B O     1 
HETATM 19522 O  O     . HOH   AA 11 .    ? 25.664  9.047   74.861  1.00 37.98 ? 1425 HOH   B O     1 
HETATM 19523 O  O     . HOH   AA 11 .    ? -17.710 0.804   99.036  1.00 38.37 ? 1426 HOH   B O     1 
HETATM 19524 O  O     . HOH   AA 11 .    ? 6.162   32.109  78.712  1.00 21.24 ? 1427 HOH   B O     1 
HETATM 19525 O  O     . HOH   AA 11 .    ? -22.605 19.660  101.648 1.00 31.19 ? 1428 HOH   B O     1 
HETATM 19526 O  O     . HOH   AA 11 .    ? -22.691 10.049  121.341 1.00 40.43 ? 1429 HOH   B O     1 
HETATM 19527 O  O     . HOH   AA 11 .    ? 25.536  53.453  96.093  1.00 38.10 ? 1430 HOH   B O     1 
HETATM 19528 O  O     . HOH   AA 11 .    ? 30.581  26.270  52.338  1.00 37.02 ? 1431 HOH   B O     1 
HETATM 19529 O  O     . HOH   AA 11 .    ? 27.466  13.413  66.259  1.00 33.46 ? 1432 HOH   B O     1 
HETATM 19530 O  O     . HOH   AA 11 .    ? -10.341 -2.256  115.160 1.00 34.08 ? 1433 HOH   B O     1 
HETATM 19531 O  O     . HOH   AA 11 .    ? 33.813  47.591  97.508  1.00 41.75 ? 1434 HOH   B O     1 
HETATM 19532 O  O     . HOH   AA 11 .    ? -4.702  7.189   81.380  1.00 41.02 ? 1435 HOH   B O     1 
HETATM 19533 O  O     . HOH   AA 11 .    ? -5.631  39.768  89.698  1.00 40.94 ? 1436 HOH   B O     1 
HETATM 19534 O  O     . HOH   AA 11 .    ? 13.977  58.245  60.387  1.00 36.18 ? 1437 HOH   B O     1 
HETATM 19535 O  O     . HOH   AA 11 .    ? 22.736  35.134  114.999 1.00 30.91 ? 1438 HOH   B O     1 
HETATM 19536 O  O     . HOH   AA 11 .    ? 9.568   26.161  54.849  1.00 22.05 ? 1439 HOH   B O     1 
HETATM 19537 O  O     . HOH   AA 11 .    ? 29.417  42.584  83.883  1.00 26.65 ? 1440 HOH   B O     1 
HETATM 19538 O  O     . HOH   AA 11 .    ? 15.131  21.861  88.092  1.00 34.94 ? 1441 HOH   B O     1 
HETATM 19539 O  O     . HOH   AA 11 .    ? 32.988  30.009  61.548  1.00 27.11 ? 1442 HOH   B O     1 
HETATM 19540 O  O     . HOH   AA 11 .    ? 3.626   21.772  101.980 1.00 30.26 ? 1443 HOH   B O     1 
HETATM 19541 O  O     . HOH   AA 11 .    ? -8.710  24.437  76.584  1.00 36.32 ? 1444 HOH   B O     1 
HETATM 19542 O  O     . HOH   AA 11 .    ? 23.388  18.545  79.975  1.00 27.14 ? 1445 HOH   B O     1 
HETATM 19543 O  O     . HOH   AA 11 .    ? 8.325   -0.709  106.712 1.00 32.71 ? 1446 HOH   B O     1 
HETATM 19544 O  O     . HOH   AA 11 .    ? -14.486 9.935   117.954 1.00 31.45 ? 1447 HOH   B O     1 
HETATM 19545 O  O     . HOH   AA 11 .    ? 25.203  58.802  53.031  1.00 42.60 ? 1448 HOH   B O     1 
HETATM 19546 O  O     . HOH   AA 11 .    ? 13.988  41.671  76.493  1.00 17.30 ? 1449 HOH   B O     1 
HETATM 19547 O  O     . HOH   AA 11 .    ? 4.924   32.541  88.873  1.00 33.42 ? 1450 HOH   B O     1 
HETATM 19548 O  O     . HOH   AA 11 .    ? 39.202  27.018  87.335  1.00 33.31 ? 1451 HOH   B O     1 
HETATM 19549 O  O     . HOH   AA 11 .    ? 16.591  14.694  109.017 1.00 27.84 ? 1452 HOH   B O     1 
HETATM 19550 O  O     . HOH   AA 11 .    ? 33.221  18.062  89.367  1.00 35.21 ? 1453 HOH   B O     1 
HETATM 19551 O  O     . HOH   AA 11 .    ? 7.045   19.733  116.008 1.00 30.10 ? 1454 HOH   B O     1 
HETATM 19552 O  O     . HOH   AA 11 .    ? 25.858  8.803   78.545  1.00 35.19 ? 1455 HOH   B O     1 
HETATM 19553 O  O     . HOH   AA 11 .    ? -9.936  -4.314  106.680 1.00 29.84 ? 1456 HOH   B O     1 
HETATM 19554 O  O     . HOH   AA 11 .    ? -4.610  27.115  69.831  1.00 33.86 ? 1457 HOH   B O     1 
HETATM 19555 O  O     . HOH   AA 11 .    ? -31.352 16.680  101.672 1.00 39.40 ? 1458 HOH   B O     1 
HETATM 19556 O  O     . HOH   AA 11 .    ? 34.095  62.684  77.967  1.00 18.73 ? 1459 HOH   B O     1 
HETATM 19557 O  O     . HOH   AA 11 .    ? 3.608   8.202   91.828  1.00 22.95 ? 1460 HOH   B O     1 
HETATM 19558 O  O     . HOH   AA 11 .    ? -1.137  22.568  70.912  1.00 33.10 ? 1461 HOH   B O     1 
HETATM 19559 O  O     . HOH   AA 11 .    ? 18.743  67.502  82.110  1.00 27.13 ? 1462 HOH   B O     1 
HETATM 19560 O  O     . HOH   AA 11 .    ? -5.444  -1.295  123.110 1.00 37.58 ? 1463 HOH   B O     1 
HETATM 19561 O  O     . HOH   AA 11 .    ? 3.837   14.453  72.382  1.00 32.82 ? 1464 HOH   B O     1 
HETATM 19562 O  O     . HOH   AA 11 .    ? -12.537 20.308  83.378  1.00 25.25 ? 1465 HOH   B O     1 
HETATM 19563 O  O     . HOH   AA 11 .    ? 32.622  19.297  57.745  1.00 31.22 ? 1466 HOH   B O     1 
HETATM 19564 O  O     . HOH   AA 11 .    ? 10.923  80.050  67.389  1.00 41.33 ? 1467 HOH   B O     1 
HETATM 19565 O  O     . HOH   AA 11 .    ? -0.423  27.239  68.150  1.00 17.61 ? 1468 HOH   B O     1 
HETATM 19566 O  O     . HOH   AA 11 .    ? 1.618   13.411  101.396 1.00 22.22 ? 1469 HOH   B O     1 
HETATM 19567 O  O     . HOH   AA 11 .    ? -10.239 39.956  126.791 1.00 40.68 ? 1470 HOH   B O     1 
HETATM 19568 O  O     . HOH   AA 11 .    ? 18.906  31.601  72.871  1.00 21.16 ? 1471 HOH   B O     1 
HETATM 19569 O  O     . HOH   AA 11 .    ? 35.720  39.030  90.300  1.00 33.59 ? 1472 HOH   B O     1 
HETATM 19570 O  O     . HOH   AA 11 .    ? 23.333  65.292  81.881  1.00 34.95 ? 1473 HOH   B O     1 
HETATM 19571 O  O     . HOH   AA 11 .    ? -12.308 4.403   129.100 1.00 42.62 ? 1474 HOH   B O     1 
HETATM 19572 O  O     . HOH   AA 11 .    ? 10.483  51.582  74.994  1.00 21.18 ? 1475 HOH   B O     1 
HETATM 19573 O  O     . HOH   AA 11 .    ? 10.940  46.590  106.224 1.00 31.10 ? 1476 HOH   B O     1 
HETATM 19574 O  O     . HOH   AA 11 .    ? 17.642  13.061  116.791 1.00 28.58 ? 1477 HOH   B O     1 
HETATM 19575 O  O     . HOH   AA 11 .    ? -17.045 5.352   115.934 1.00 27.86 ? 1478 HOH   B O     1 
HETATM 19576 O  O     . HOH   AA 11 .    ? -1.326  14.880  85.460  1.00 24.18 ? 1479 HOH   B O     1 
HETATM 19577 O  O     . HOH   AA 11 .    ? -4.599  65.896  71.536  1.00 37.10 ? 1480 HOH   B O     1 
HETATM 19578 O  O     . HOH   AA 11 .    ? 30.083  50.226  71.099  1.00 29.18 ? 1481 HOH   B O     1 
HETATM 19579 O  O     . HOH   AA 11 .    ? 32.417  26.857  68.258  1.00 36.60 ? 1482 HOH   B O     1 
HETATM 19580 O  O     . HOH   AA 11 .    ? 18.246  38.666  115.260 1.00 33.31 ? 1483 HOH   B O     1 
HETATM 19581 O  O     . HOH   AA 11 .    ? 5.659   44.017  57.987  1.00 33.00 ? 1484 HOH   B O     1 
HETATM 19582 O  O     . HOH   AA 11 .    ? 10.215  0.343   89.670  1.00 43.20 ? 1485 HOH   B O     1 
HETATM 19583 O  O     . HOH   AA 11 .    ? -0.456  73.491  77.284  1.00 29.43 ? 1486 HOH   B O     1 
HETATM 19584 O  O     . HOH   AA 11 .    ? 7.349   32.923  97.638  1.00 29.34 ? 1487 HOH   B O     1 
HETATM 19585 O  O     . HOH   AA 11 .    ? -11.848 -4.232  108.856 1.00 29.50 ? 1488 HOH   B O     1 
HETATM 19586 O  O     . HOH   AA 11 .    ? 25.471  69.624  81.166  1.00 36.38 ? 1489 HOH   B O     1 
HETATM 19587 O  O     . HOH   AA 11 .    ? 11.718  -1.824  109.496 1.00 42.03 ? 1490 HOH   B O     1 
HETATM 19588 O  O     . HOH   AA 11 .    ? -12.063 27.751  101.755 1.00 41.44 ? 1491 HOH   B O     1 
HETATM 19589 O  O     . HOH   AA 11 .    ? -4.358  64.367  80.613  1.00 18.06 ? 1492 HOH   B O     1 
HETATM 19590 O  O     . HOH   AA 11 .    ? -7.825  20.415  79.106  1.00 35.43 ? 1493 HOH   B O     1 
HETATM 19591 O  O     . HOH   AA 11 .    ? -4.867  34.861  56.592  1.00 43.22 ? 1494 HOH   B O     1 
HETATM 19592 O  O     . HOH   AA 11 .    ? 7.752   65.441  63.259  1.00 28.93 ? 1495 HOH   B O     1 
HETATM 19593 O  O     . HOH   AA 11 .    ? 14.995  40.652  72.559  1.00 18.13 ? 1496 HOH   B O     1 
HETATM 19594 O  O     . HOH   AA 11 .    ? -3.125  24.534  103.464 1.00 35.75 ? 1497 HOH   B O     1 
HETATM 19595 O  O     . HOH   AA 11 .    ? -2.294  49.013  63.152  1.00 18.32 ? 1498 HOH   B O     1 
HETATM 19596 O  O     . HOH   AA 11 .    ? -4.507  38.158  93.182  1.00 40.46 ? 1499 HOH   B O     1 
HETATM 19597 O  O     . HOH   AA 11 .    ? 11.096  18.565  64.217  1.00 26.66 ? 1500 HOH   B O     1 
HETATM 19598 O  O     . HOH   AA 11 .    ? -6.607  12.536  124.804 1.00 29.68 ? 1501 HOH   B O     1 
HETATM 19599 O  O     . HOH   AA 11 .    ? 21.173  5.759   67.701  1.00 36.98 ? 1502 HOH   B O     1 
HETATM 19600 O  O     . HOH   AA 11 .    ? 14.832  56.079  74.421  1.00 24.15 ? 1503 HOH   B O     1 
HETATM 19601 O  O     . HOH   AA 11 .    ? 1.100   39.036  107.810 1.00 27.01 ? 1504 HOH   B O     1 
HETATM 19602 O  O     . HOH   AA 11 .    ? 3.456   34.007  86.198  1.00 21.58 ? 1505 HOH   B O     1 
HETATM 19603 O  O     . HOH   AA 11 .    ? 8.925   23.591  108.503 1.00 30.30 ? 1506 HOH   B O     1 
HETATM 19604 O  O     . HOH   AA 11 .    ? 18.554  7.800   100.219 1.00 34.81 ? 1507 HOH   B O     1 
HETATM 19605 O  O     . HOH   AA 11 .    ? -27.591 10.235  88.808  1.00 43.58 ? 1508 HOH   B O     1 
HETATM 19606 O  O     . HOH   AA 11 .    ? 17.435  27.680  82.583  1.00 25.51 ? 1509 HOH   B O     1 
HETATM 19607 O  O     . HOH   AA 11 .    ? 10.355  24.848  103.095 1.00 29.75 ? 1510 HOH   B O     1 
HETATM 19608 O  O     . HOH   AA 11 .    ? 1.644   20.786  103.496 1.00 27.22 ? 1511 HOH   B O     1 
HETATM 19609 O  O     . HOH   AA 11 .    ? 2.479   22.137  129.812 1.00 30.34 ? 1512 HOH   B O     1 
HETATM 19610 O  O     . HOH   AA 11 .    ? 26.531  20.866  55.421  1.00 31.03 ? 1513 HOH   B O     1 
HETATM 19611 O  O     . HOH   AA 11 .    ? 15.332  53.839  81.277  1.00 21.34 ? 1514 HOH   B O     1 
HETATM 19612 O  O     . HOH   AA 11 .    ? -10.448 25.744  102.461 1.00 37.47 ? 1515 HOH   B O     1 
HETATM 19613 O  O     . HOH   AA 11 .    ? 8.052   8.302   72.393  1.00 38.44 ? 1516 HOH   B O     1 
HETATM 19614 O  O     . HOH   AA 11 .    ? 22.267  45.749  90.172  1.00 17.15 ? 1517 HOH   B O     1 
HETATM 19615 O  O     . HOH   AA 11 .    ? 18.720  13.293  95.027  1.00 29.47 ? 1518 HOH   B O     1 
HETATM 19616 O  O     . HOH   AA 11 .    ? 1.025   55.823  110.074 1.00 28.35 ? 1519 HOH   B O     1 
HETATM 19617 O  O     . HOH   AA 11 .    ? -5.815  39.553  106.267 1.00 31.22 ? 1520 HOH   B O     1 
HETATM 19618 O  O     . HOH   AA 11 .    ? -6.101  40.526  62.441  1.00 31.55 ? 1521 HOH   B O     1 
HETATM 19619 O  O     . HOH   AA 11 .    ? 3.281   18.633  88.570  1.00 27.00 ? 1522 HOH   B O     1 
HETATM 19620 O  O     . HOH   AA 11 .    ? 4.151   21.544  118.556 1.00 30.94 ? 1523 HOH   B O     1 
HETATM 19621 O  O     . HOH   AA 11 .    ? -4.837  2.469   123.526 1.00 26.43 ? 1524 HOH   B O     1 
HETATM 19622 O  O     . HOH   AA 11 .    ? 1.568   13.849  104.243 1.00 18.56 ? 1525 HOH   B O     1 
HETATM 19623 O  O     . HOH   AA 11 .    ? -9.421  10.370  122.428 1.00 26.46 ? 1526 HOH   B O     1 
HETATM 19624 O  O     . HOH   AA 11 .    ? 15.135  4.253   97.959  1.00 31.45 ? 1527 HOH   B O     1 
HETATM 19625 O  O     . HOH   AA 11 .    ? 25.351  55.064  61.713  1.00 22.84 ? 1528 HOH   B O     1 
HETATM 19626 O  O     . HOH   AA 11 .    ? 23.182  48.687  106.438 1.00 31.95 ? 1529 HOH   B O     1 
HETATM 19627 O  O     . HOH   AA 11 .    ? -8.778  45.506  108.451 1.00 31.94 ? 1530 HOH   B O     1 
HETATM 19628 O  O     . HOH   AA 11 .    ? 10.095  51.012  64.186  1.00 23.92 ? 1531 HOH   B O     1 
HETATM 19629 O  O     . HOH   AA 11 .    ? -6.338  51.200  72.588  1.00 16.46 ? 1532 HOH   B O     1 
HETATM 19630 O  O     . HOH   AA 11 .    ? -32.140 17.707  90.993  1.00 39.62 ? 1533 HOH   B O     1 
HETATM 19631 O  O     . HOH   AA 11 .    ? -4.489  60.064  124.998 1.00 31.56 ? 1534 HOH   B O     1 
HETATM 19632 O  O     . HOH   AA 11 .    ? 33.604  12.490  74.462  1.00 33.76 ? 1535 HOH   B O     1 
HETATM 19633 O  O     . HOH   AA 11 .    ? 25.734  55.439  77.046  1.00 24.05 ? 1536 HOH   B O     1 
HETATM 19634 O  O     . HOH   AA 11 .    ? 4.313   42.370  83.921  1.00 22.84 ? 1537 HOH   B O     1 
HETATM 19635 O  O     . HOH   AA 11 .    ? 7.763   74.770  61.721  1.00 39.65 ? 1538 HOH   B O     1 
HETATM 19636 O  O     . HOH   AA 11 .    ? 18.776  62.449  57.030  1.00 34.24 ? 1539 HOH   B O     1 
HETATM 19637 O  O     . HOH   AA 11 .    ? 28.766  69.532  79.432  1.00 25.14 ? 1540 HOH   B O     1 
HETATM 19638 O  O     . HOH   AA 11 .    ? -37.293 14.198  94.383  1.00 50.61 ? 1541 HOH   B O     1 
HETATM 19639 O  O     . HOH   AA 11 .    ? -1.312  38.555  79.740  1.00 25.19 ? 1542 HOH   B O     1 
HETATM 19640 O  O     . HOH   AA 11 .    ? -10.651 46.663  74.062  1.00 19.96 ? 1543 HOH   B O     1 
HETATM 19641 O  O     . HOH   AA 11 .    ? 21.383  50.716  87.230  1.00 23.25 ? 1544 HOH   B O     1 
HETATM 19642 O  O     . HOH   AA 11 .    ? 2.554   44.189  69.932  1.00 16.27 ? 1545 HOH   B O     1 
HETATM 19643 O  O     . HOH   AA 11 .    ? 38.496  32.838  83.440  1.00 31.04 ? 1546 HOH   B O     1 
HETATM 19644 O  O     . HOH   AA 11 .    ? 31.792  38.630  83.799  1.00 27.32 ? 1547 HOH   B O     1 
HETATM 19645 O  O     . HOH   AA 11 .    ? 6.166   50.119  87.776  1.00 33.12 ? 1548 HOH   B O     1 
HETATM 19646 O  O     . HOH   AA 11 .    ? 1.477   57.404  87.157  1.00 36.03 ? 1549 HOH   B O     1 
HETATM 19647 O  O     . HOH   AA 11 .    ? -8.869  24.263  100.328 1.00 20.56 ? 1550 HOH   B O     1 
HETATM 19648 O  O     . HOH   AA 11 .    ? 5.891   25.975  85.865  1.00 33.03 ? 1551 HOH   B O     1 
HETATM 19649 O  O     . HOH   AA 11 .    ? -5.750  -6.056  111.665 1.00 32.09 ? 1552 HOH   B O     1 
HETATM 19650 O  O     . HOH   AA 11 .    ? -4.753  -1.670  96.468  1.00 25.05 ? 1553 HOH   B O     1 
HETATM 19651 O  O     . HOH   AA 11 .    ? 10.836  38.572  95.274  1.00 27.93 ? 1554 HOH   B O     1 
HETATM 19652 O  O     . HOH   AA 11 .    ? 6.730   77.630  63.718  1.00 38.54 ? 1555 HOH   B O     1 
HETATM 19653 O  O     . HOH   AA 11 .    ? -0.249  -6.894  106.445 1.00 30.68 ? 1556 HOH   B O     1 
HETATM 19654 O  O     . HOH   AA 11 .    ? 18.679  50.546  69.625  1.00 26.07 ? 1557 HOH   B O     1 
HETATM 19655 O  O     . HOH   AA 11 .    ? 15.733  55.742  92.400  1.00 32.31 ? 1558 HOH   B O     1 
HETATM 19656 O  O     . HOH   AA 11 .    ? -2.722  62.928  85.048  1.00 26.11 ? 1559 HOH   B O     1 
HETATM 19657 O  O     . HOH   AA 11 .    ? 14.919  21.072  92.097  1.00 30.92 ? 1560 HOH   B O     1 
HETATM 19658 O  O     . HOH   AA 11 .    ? 18.272  23.735  84.782  1.00 18.17 ? 1561 HOH   B O     1 
HETATM 19659 O  O     . HOH   AA 11 .    ? 9.637   30.947  109.493 1.00 36.99 ? 1562 HOH   B O     1 
HETATM 19660 O  O     . HOH   AA 11 .    ? -9.172  19.534  80.584  1.00 35.37 ? 1563 HOH   B O     1 
HETATM 19661 O  O     . HOH   AA 11 .    ? 24.069  19.253  97.808  1.00 31.37 ? 1564 HOH   B O     1 
HETATM 19662 O  O     . HOH   AA 11 .    ? -4.754  44.265  80.694  1.00 33.39 ? 1565 HOH   B O     1 
HETATM 19663 O  O     . HOH   AA 11 .    ? -2.522  5.170   84.532  1.00 31.00 ? 1566 HOH   B O     1 
HETATM 19664 O  O     . HOH   AA 11 .    ? -5.211  51.805  75.025  1.00 21.66 ? 1567 HOH   B O     1 
HETATM 19665 O  O     . HOH   AA 11 .    ? -2.291  39.742  86.749  1.00 19.11 ? 1568 HOH   B O     1 
HETATM 19666 O  O     . HOH   AA 11 .    ? 8.332   25.125  105.154 1.00 36.69 ? 1569 HOH   B O     1 
HETATM 19667 O  O     . HOH   AA 11 .    ? 2.595   30.887  79.642  1.00 18.58 ? 1570 HOH   B O     1 
HETATM 19668 O  O     . HOH   AA 11 .    ? 9.084   4.263   80.488  1.00 27.11 ? 1571 HOH   B O     1 
HETATM 19669 O  O     . HOH   AA 11 .    ? 37.529  24.036  84.313  1.00 36.36 ? 1572 HOH   B O     1 
HETATM 19670 O  O     . HOH   AA 11 .    ? 29.838  27.557  55.806  1.00 23.60 ? 1573 HOH   B O     1 
HETATM 19671 O  O     . HOH   AA 11 .    ? 1.280   22.405  110.471 1.00 34.76 ? 1574 HOH   B O     1 
HETATM 19672 O  O     . HOH   AA 11 .    ? 16.037  69.991  54.841  1.00 44.89 ? 1575 HOH   B O     1 
HETATM 19673 O  O     . HOH   AA 11 .    ? 12.042  11.314  71.191  1.00 24.40 ? 1576 HOH   B O     1 
HETATM 19674 O  O     . HOH   AA 11 .    ? 17.297  55.180  96.770  1.00 25.35 ? 1577 HOH   B O     1 
HETATM 19675 O  O     . HOH   AA 11 .    ? 19.027  70.735  58.691  1.00 33.46 ? 1578 HOH   B O     1 
HETATM 19676 O  O     . HOH   AA 11 .    ? -5.794  37.556  77.342  1.00 29.81 ? 1579 HOH   B O     1 
HETATM 19677 O  O     . HOH   AA 11 .    ? -13.899 0.095   96.399  1.00 36.99 ? 1580 HOH   B O     1 
HETATM 19678 O  O     . HOH   AA 11 .    ? -5.739  5.605   121.622 1.00 26.42 ? 1581 HOH   B O     1 
HETATM 19679 O  O     . HOH   AA 11 .    ? 13.517  10.603  90.947  1.00 26.94 ? 1582 HOH   B O     1 
HETATM 19680 O  O     . HOH   AA 11 .    ? 29.447  32.451  76.131  1.00 24.30 ? 1583 HOH   B O     1 
HETATM 19681 O  O     . HOH   AA 11 .    ? 31.582  59.427  71.727  1.00 23.22 ? 1584 HOH   B O     1 
HETATM 19682 O  O     . HOH   AA 11 .    ? -4.374  45.763  89.159  1.00 40.74 ? 1585 HOH   B O     1 
HETATM 19683 O  O     . HOH   AA 11 .    ? -7.299  15.956  81.243  1.00 32.27 ? 1586 HOH   B O     1 
HETATM 19684 O  O     . HOH   AA 11 .    ? 11.253  25.102  107.725 1.00 27.68 ? 1587 HOH   B O     1 
HETATM 19685 O  O     . HOH   AA 11 .    ? 2.727   46.062  53.501  1.00 37.90 ? 1588 HOH   B O     1 
HETATM 19686 O  O     . HOH   AA 11 .    ? 7.528   49.371  106.129 1.00 22.51 ? 1589 HOH   B O     1 
HETATM 19687 O  O     . HOH   AA 11 .    ? -13.075 9.140   123.828 1.00 33.25 ? 1590 HOH   B O     1 
HETATM 19688 O  O     . HOH   AA 11 .    ? 24.171  31.373  46.858  1.00 42.53 ? 1591 HOH   B O     1 
HETATM 19689 O  O     . HOH   AA 11 .    ? -1.445  31.691  125.024 1.00 42.60 ? 1592 HOH   B O     1 
HETATM 19690 O  O     . HOH   AA 11 .    ? 0.794   19.936  111.054 1.00 32.76 ? 1593 HOH   B O     1 
HETATM 19691 O  O     . HOH   AA 11 .    ? 31.581  60.336  65.079  1.00 26.58 ? 1594 HOH   B O     1 
HETATM 19692 O  O     . HOH   AA 11 .    ? 12.164  21.610  100.953 1.00 25.09 ? 1595 HOH   B O     1 
HETATM 19693 O  O     . HOH   AA 11 .    ? 19.660  19.771  105.265 1.00 19.25 ? 1596 HOH   B O     1 
HETATM 19694 O  O     . HOH   AA 11 .    ? 10.981  6.206   121.343 1.00 30.94 ? 1597 HOH   B O     1 
HETATM 19695 O  O     . HOH   AA 11 .    ? -30.785 21.115  83.505  1.00 43.02 ? 1598 HOH   B O     1 
HETATM 19696 O  O     . HOH   AA 11 .    ? 0.946   29.075  82.566  1.00 16.67 ? 1599 HOH   B O     1 
HETATM 19697 O  O     . HOH   AA 11 .    ? 36.464  20.996  78.318  1.00 38.46 ? 1600 HOH   B O     1 
HETATM 19698 O  O     . HOH   AA 11 .    ? 17.154  41.267  71.062  1.00 17.78 ? 1601 HOH   B O     1 
HETATM 19699 O  O     . HOH   AA 11 .    ? 11.865  0.948   93.787  1.00 38.74 ? 1602 HOH   B O     1 
HETATM 19700 O  O     . HOH   AA 11 .    ? -2.136  35.827  100.473 1.00 36.63 ? 1603 HOH   B O     1 
HETATM 19701 O  O     . HOH   AA 11 .    ? 22.819  48.783  77.663  1.00 20.85 ? 1604 HOH   B O     1 
HETATM 19702 O  O     . HOH   AA 11 .    ? 27.339  39.768  104.208 1.00 28.81 ? 1605 HOH   B O     1 
HETATM 19703 O  O     . HOH   AA 11 .    ? 4.715   49.532  68.171  1.00 23.44 ? 1606 HOH   B O     1 
HETATM 19704 O  O     . HOH   AA 11 .    ? 27.045  33.117  104.383 1.00 37.47 ? 1607 HOH   B O     1 
HETATM 19705 O  O     . HOH   AA 11 .    ? -12.494 49.431  129.883 1.00 40.78 ? 1608 HOH   B O     1 
HETATM 19706 O  O     . HOH   AA 11 .    ? -15.141 47.412  113.560 1.00 32.79 ? 1609 HOH   B O     1 
HETATM 19707 O  O     . HOH   AA 11 .    ? 6.966   42.817  49.204  1.00 27.31 ? 1610 HOH   B O     1 
HETATM 19708 O  O     . HOH   AA 11 .    ? -2.426  45.522  102.140 1.00 34.30 ? 1611 HOH   B O     1 
HETATM 19709 O  O     . HOH   AA 11 .    ? 22.692  67.555  64.235  1.00 24.13 ? 1612 HOH   B O     1 
HETATM 19710 O  O     . HOH   AA 11 .    ? 11.112  19.594  61.153  1.00 28.73 ? 1613 HOH   B O     1 
HETATM 19711 O  O     . HOH   AA 11 .    ? 17.687  68.761  84.191  1.00 36.56 ? 1614 HOH   B O     1 
HETATM 19712 O  O     . HOH   AA 11 .    ? 4.186   -8.480  103.835 1.00 33.92 ? 1615 HOH   B O     1 
HETATM 19713 O  O     . HOH   AA 11 .    ? -5.340  40.099  71.807  1.00 27.38 ? 1616 HOH   B O     1 
HETATM 19714 O  O     . HOH   AA 11 .    ? 15.014  39.142  76.652  1.00 16.77 ? 1617 HOH   B O     1 
HETATM 19715 O  O     . HOH   AA 11 .    ? 9.903   71.427  61.282  1.00 29.40 ? 1618 HOH   B O     1 
HETATM 19716 O  O     . HOH   AA 11 .    ? 13.904  81.499  69.324  1.00 38.86 ? 1619 HOH   B O     1 
HETATM 19717 O  O     . HOH   AA 11 .    ? 15.814  53.053  57.436  1.00 30.22 ? 1620 HOH   B O     1 
HETATM 19718 O  O     . HOH   AA 11 .    ? 18.840  24.989  54.106  1.00 23.95 ? 1621 HOH   B O     1 
HETATM 19719 O  O     . HOH   AA 11 .    ? -4.909  31.027  76.942  1.00 18.06 ? 1622 HOH   B O     1 
HETATM 19720 O  O     . HOH   AA 11 .    ? -21.089 15.942  82.161  1.00 30.19 ? 1623 HOH   B O     1 
HETATM 19721 O  O     . HOH   AA 11 .    ? 9.962   50.825  89.616  1.00 26.58 ? 1624 HOH   B O     1 
HETATM 19722 O  O     . HOH   AA 11 .    ? 34.097  54.806  75.348  1.00 36.57 ? 1625 HOH   B O     1 
HETATM 19723 O  O     . HOH   AA 11 .    ? 4.866   63.114  83.734  1.00 22.26 ? 1626 HOH   B O     1 
HETATM 19724 O  O     . HOH   AA 11 .    ? -0.562  24.245  73.835  1.00 21.22 ? 1627 HOH   B O     1 
HETATM 19725 O  O     . HOH   AA 11 .    ? 18.129  52.833  66.247  1.00 23.06 ? 1628 HOH   B O     1 
HETATM 19726 O  O     . HOH   AA 11 .    ? 29.035  68.591  72.107  1.00 36.39 ? 1629 HOH   B O     1 
HETATM 19727 O  O     . HOH   AA 11 .    ? 6.633   6.064   91.900  1.00 22.87 ? 1630 HOH   B O     1 
HETATM 19728 O  O     . HOH   AA 11 .    ? 28.421  19.215  57.511  1.00 32.68 ? 1631 HOH   B O     1 
HETATM 19729 O  O     . HOH   AA 11 .    ? -7.125  8.834   110.599 1.00 22.68 ? 1632 HOH   B O     1 
HETATM 19730 O  O     . HOH   AA 11 .    ? -0.354  56.264  85.853  1.00 30.83 ? 1633 HOH   B O     1 
HETATM 19731 O  O     . HOH   AA 11 .    ? 26.623  22.290  74.913  1.00 21.95 ? 1634 HOH   B O     1 
HETATM 19732 O  O     . HOH   AA 11 .    ? 33.535  68.014  80.282  1.00 24.56 ? 1635 HOH   B O     1 
HETATM 19733 O  O     . HOH   AA 11 .    ? -18.912 24.468  114.559 1.00 33.83 ? 1636 HOH   B O     1 
HETATM 19734 O  O     . HOH   AA 11 .    ? 15.915  43.315  49.916  1.00 32.55 ? 1637 HOH   B O     1 
HETATM 19735 O  O     . HOH   AA 11 .    ? -14.827 6.611   117.000 1.00 28.29 ? 1638 HOH   B O     1 
HETATM 19736 O  O     . HOH   AA 11 .    ? 20.054  43.739  87.332  1.00 14.43 ? 1639 HOH   B O     1 
HETATM 19737 O  O     . HOH   AA 11 .    ? -0.993  -8.533  101.626 1.00 31.01 ? 1640 HOH   B O     1 
HETATM 19738 O  O     . HOH   AA 11 .    ? -2.362  42.024  61.220  1.00 23.48 ? 1641 HOH   B O     1 
HETATM 19739 O  O     . HOH   AA 11 .    ? -11.068 20.490  122.233 1.00 30.78 ? 1642 HOH   B O     1 
HETATM 19740 O  O     . HOH   AA 11 .    ? -7.446  25.804  103.431 1.00 38.64 ? 1643 HOH   B O     1 
HETATM 19741 O  O     . HOH   AA 11 .    ? 21.541  30.483  71.070  1.00 14.69 ? 1644 HOH   B O     1 
HETATM 19742 O  O     . HOH   AA 11 .    ? 14.305  33.920  83.536  1.00 22.49 ? 1645 HOH   B O     1 
HETATM 19743 O  O     . HOH   AA 11 .    ? 19.593  51.257  77.076  1.00 18.86 ? 1646 HOH   B O     1 
HETATM 19744 O  O     . HOH   AA 11 .    ? -6.625  52.708  106.816 1.00 30.06 ? 1647 HOH   B O     1 
HETATM 19745 O  O     . HOH   AA 11 .    ? 19.602  5.671   76.509  1.00 30.12 ? 1648 HOH   B O     1 
HETATM 19746 O  O     . HOH   AA 11 .    ? -4.149  19.001  97.674  1.00 18.13 ? 1649 HOH   B O     1 
HETATM 19747 O  O     . HOH   AA 11 .    ? 18.794  45.433  53.381  1.00 27.29 ? 1650 HOH   B O     1 
HETATM 19748 O  O     . HOH   AA 11 .    ? 33.021  28.880  52.754  1.00 34.32 ? 1651 HOH   B O     1 
HETATM 19749 O  O     . HOH   AA 11 .    ? 15.344  17.135  87.500  1.00 20.92 ? 1652 HOH   B O     1 
HETATM 19750 O  O     . HOH   AA 11 .    ? 17.334  49.223  58.571  1.00 22.07 ? 1653 HOH   B O     1 
HETATM 19751 O  O     . HOH   AA 11 .    ? 17.032  43.096  78.929  1.00 15.83 ? 1654 HOH   B O     1 
HETATM 19752 O  O     . HOH   AA 11 .    ? 3.594   33.920  92.464  1.00 20.59 ? 1655 HOH   B O     1 
HETATM 19753 O  O     . HOH   AA 11 .    ? -6.448  0.702   85.743  1.00 30.84 ? 1656 HOH   B O     1 
HETATM 19754 O  O     . HOH   AA 11 .    ? -1.422  32.857  68.699  1.00 15.45 ? 1657 HOH   B O     1 
HETATM 19755 O  O     . HOH   AA 11 .    ? 4.445   65.139  65.760  1.00 38.33 ? 1658 HOH   B O     1 
HETATM 19756 O  O     . HOH   AA 11 .    ? 0.088   28.298  121.674 1.00 40.91 ? 1659 HOH   B O     1 
HETATM 19757 O  O     . HOH   AA 11 .    ? 4.198   19.613  96.855  1.00 32.19 ? 1660 HOH   B O     1 
HETATM 19758 O  O     . HOH   AA 11 .    ? 21.768  53.495  66.776  1.00 25.05 ? 1661 HOH   B O     1 
HETATM 19759 O  O     . HOH   AA 11 .    ? -4.753  50.665  78.049  1.00 27.28 ? 1662 HOH   B O     1 
HETATM 19760 O  O     . HOH   AA 11 .    ? 4.506   77.784  79.720  1.00 30.72 ? 1663 HOH   B O     1 
HETATM 19761 O  O     . HOH   AA 11 .    ? 1.399   49.509  88.843  1.00 36.82 ? 1664 HOH   B O     1 
HETATM 19762 O  O     . HOH   AA 11 .    ? 20.812  37.725  112.010 1.00 23.61 ? 1665 HOH   B O     1 
HETATM 19763 O  O     . HOH   AA 11 .    ? -5.560  55.393  78.225  1.00 23.33 ? 1666 HOH   B O     1 
HETATM 19764 O  O     . HOH   AA 11 .    ? -20.292 25.904  101.901 1.00 38.78 ? 1667 HOH   B O     1 
HETATM 19765 O  O     . HOH   AA 11 .    ? 15.288  62.325  84.078  1.00 34.56 ? 1668 HOH   B O     1 
HETATM 19766 O  O     . HOH   AA 11 .    ? -5.117  42.841  72.269  1.00 32.25 ? 1669 HOH   B O     1 
HETATM 19767 O  O     . HOH   AA 11 .    ? -5.990  -7.016  115.230 1.00 34.36 ? 1670 HOH   B O     1 
HETATM 19768 O  O     . HOH   AA 11 .    ? 18.554  13.757  74.077  1.00 23.52 ? 1671 HOH   B O     1 
HETATM 19769 O  O     . HOH   AA 11 .    ? 27.304  38.295  89.500  1.00 20.08 ? 1672 HOH   B O     1 
HETATM 19770 O  O     . HOH   AA 11 .    ? 22.966  54.645  53.369  1.00 36.82 ? 1673 HOH   B O     1 
HETATM 19771 O  O     . HOH   AA 11 .    ? 6.286   6.031   85.580  1.00 21.68 ? 1674 HOH   B O     1 
HETATM 19772 O  O     . HOH   AA 11 .    ? 31.006  38.222  77.059  1.00 36.19 ? 1675 HOH   B O     1 
HETATM 19773 O  O     . HOH   AA 11 .    ? -7.760  -0.550  119.395 1.00 31.81 ? 1676 HOH   B O     1 
HETATM 19774 O  O     . HOH   AA 11 .    ? 0.931   31.077  74.359  1.00 17.26 ? 1677 HOH   B O     1 
HETATM 19775 O  O     . HOH   AA 11 .    ? 9.423   -5.341  108.578 1.00 38.85 ? 1678 HOH   B O     1 
HETATM 19776 O  O     . HOH   AA 11 .    ? -11.893 18.686  126.074 1.00 29.64 ? 1679 HOH   B O     1 
HETATM 19777 O  O     . HOH   AA 11 .    ? -1.989  11.474  100.881 1.00 19.45 ? 1680 HOH   B O     1 
HETATM 19778 O  O     . HOH   AA 11 .    ? 25.107  23.945  81.454  1.00 27.31 ? 1681 HOH   B O     1 
HETATM 19779 O  O     . HOH   AA 11 .    ? 10.548  16.674  121.300 1.00 34.91 ? 1682 HOH   B O     1 
HETATM 19780 O  O     . HOH   AA 11 .    ? 0.347   20.492  69.452  1.00 25.43 ? 1683 HOH   B O     1 
HETATM 19781 O  O     . HOH   AA 11 .    ? 23.374  56.236  98.600  1.00 31.29 ? 1684 HOH   B O     1 
HETATM 19782 O  O     . HOH   AA 11 .    ? 24.043  68.989  67.028  1.00 23.50 ? 1685 HOH   B O     1 
HETATM 19783 O  O     . HOH   AA 11 .    ? 14.010  25.996  110.490 1.00 32.30 ? 1686 HOH   B O     1 
HETATM 19784 O  O     . HOH   AA 11 .    ? 23.499  2.830   81.568  1.00 44.53 ? 1687 HOH   B O     1 
HETATM 19785 O  O     . HOH   AA 11 .    ? 38.286  34.159  102.349 1.00 28.22 ? 1688 HOH   B O     1 
HETATM 19786 O  O     . HOH   AA 11 .    ? 5.415   69.692  62.717  1.00 35.54 ? 1689 HOH   B O     1 
HETATM 19787 O  O     . HOH   AA 11 .    ? 12.375  2.354   110.862 1.00 30.28 ? 1690 HOH   B O     1 
HETATM 19788 O  O     . HOH   AA 11 .    ? -7.827  35.923  80.289  1.00 37.28 ? 1691 HOH   B O     1 
HETATM 19789 O  O     . HOH   AA 11 .    ? 15.632  38.482  74.103  1.00 16.26 ? 1692 HOH   B O     1 
HETATM 19790 O  O     . HOH   AA 11 .    ? 4.776   30.826  54.273  1.00 36.08 ? 1693 HOH   B O     1 
HETATM 19791 O  O     . HOH   AA 11 .    ? -13.610 12.143  90.743  1.00 21.89 ? 1694 HOH   B O     1 
HETATM 19792 O  O     . HOH   AA 11 .    ? -0.143  4.620   88.003  1.00 25.13 ? 1695 HOH   B O     1 
HETATM 19793 O  O     . HOH   AA 11 .    ? 33.765  37.970  61.630  1.00 27.48 ? 1696 HOH   B O     1 
HETATM 19794 O  O     . HOH   AA 11 .    ? 31.255  29.122  77.163  1.00 29.28 ? 1697 HOH   B O     1 
HETATM 19795 O  O     . HOH   AA 11 .    ? -4.745  37.475  98.078  1.00 36.67 ? 1698 HOH   B O     1 
HETATM 19796 O  O     . HOH   AA 11 .    ? 3.532   -3.348  92.368  1.00 38.53 ? 1699 HOH   B O     1 
HETATM 19797 O  O     . HOH   AA 11 .    ? -13.635 18.513  105.113 1.00 25.03 ? 1700 HOH   B O     1 
HETATM 19798 O  O     . HOH   AA 11 .    ? 11.256  41.590  54.081  1.00 19.55 ? 1701 HOH   B O     1 
HETATM 19799 O  O     . HOH   AA 11 .    ? 15.527  10.316  89.089  1.00 20.13 ? 1702 HOH   B O     1 
HETATM 19800 O  O     . HOH   AA 11 .    ? 8.570   35.965  102.199 1.00 28.17 ? 1703 HOH   B O     1 
HETATM 19801 O  O     . HOH   AA 11 .    ? 5.119   36.039  48.677  1.00 34.14 ? 1704 HOH   B O     1 
HETATM 19802 O  O     . HOH   AA 11 .    ? -10.473 52.693  127.899 1.00 35.71 ? 1705 HOH   B O     1 
HETATM 19803 O  O     . HOH   AA 11 .    ? -11.349 20.757  87.705  1.00 23.69 ? 1706 HOH   B O     1 
HETATM 19804 O  O     . HOH   AA 11 .    ? 18.944  6.116   74.028  1.00 27.17 ? 1707 HOH   B O     1 
HETATM 19805 O  O     . HOH   AA 11 .    ? 27.855  67.756  67.856  1.00 29.03 ? 1708 HOH   B O     1 
HETATM 19806 O  O     . HOH   AA 11 .    ? 9.742   43.871  109.661 1.00 27.33 ? 1709 HOH   B O     1 
HETATM 19807 O  O     . HOH   AA 11 .    ? 11.657  37.620  71.839  1.00 15.42 ? 1710 HOH   B O     1 
HETATM 19808 O  O     . HOH   AA 11 .    ? 14.599  22.755  101.328 1.00 21.90 ? 1711 HOH   B O     1 
HETATM 19809 O  O     . HOH   AA 11 .    ? -2.381  43.006  57.770  1.00 29.54 ? 1712 HOH   B O     1 
HETATM 19810 O  O     . HOH   AA 11 .    ? 13.543  58.429  64.157  1.00 27.12 ? 1713 HOH   B O     1 
HETATM 19811 O  O     . HOH   AA 11 .    ? -10.110 32.714  88.581  1.00 24.41 ? 1714 HOH   B O     1 
HETATM 19812 O  O     . HOH   AA 11 .    ? 5.885   48.340  110.258 1.00 38.57 ? 1715 HOH   B O     1 
HETATM 19813 O  O     . HOH   AA 11 .    ? 3.898   29.879  84.237  1.00 21.76 ? 1716 HOH   B O     1 
HETATM 19814 O  O     . HOH   AA 11 .    ? -2.154  3.006   125.334 1.00 26.85 ? 1717 HOH   B O     1 
HETATM 19815 O  O     . HOH   AA 11 .    ? 22.970  73.003  64.577  1.00 33.79 ? 1718 HOH   B O     1 
HETATM 19816 O  O     . HOH   AA 11 .    ? -11.199 2.200   121.088 1.00 27.51 ? 1719 HOH   B O     1 
HETATM 19817 O  O     . HOH   AA 11 .    ? 28.967  23.022  76.142  1.00 20.57 ? 1720 HOH   B O     1 
HETATM 19818 O  O     . HOH   AA 11 .    ? -18.310 8.421   121.642 1.00 32.92 ? 1721 HOH   B O     1 
HETATM 19819 O  O     . HOH   AA 11 .    ? 12.506  37.565  107.361 1.00 25.24 ? 1722 HOH   B O     1 
HETATM 19820 O  O     . HOH   AA 11 .    ? -4.662  11.160  99.931  1.00 19.40 ? 1723 HOH   B O     1 
HETATM 19821 O  O     . HOH   AA 11 .    ? 5.481   7.519   93.797  1.00 22.71 ? 1724 HOH   B O     1 
HETATM 19822 O  O     . HOH   AA 11 .    ? 2.243   41.822  53.613  1.00 26.76 ? 1725 HOH   B O     1 
HETATM 19823 O  O     . HOH   AA 11 .    ? 5.739   55.913  104.204 1.00 24.44 ? 1726 HOH   B O     1 
HETATM 19824 O  O     . HOH   AA 11 .    ? -22.328 20.746  87.781  1.00 33.79 ? 1727 HOH   B O     1 
HETATM 19825 O  O     . HOH   AA 11 .    ? 34.788  64.846  80.985  1.00 21.66 ? 1728 HOH   B O     1 
HETATM 19826 O  O     . HOH   AA 11 .    ? -18.480 43.994  124.252 1.00 41.73 ? 1729 HOH   B O     1 
HETATM 19827 O  O     . HOH   AA 11 .    ? 19.205  79.417  68.203  1.00 31.03 ? 1730 HOH   B O     1 
HETATM 19828 O  O     . HOH   AA 11 .    ? -1.492  67.338  74.878  1.00 27.58 ? 1731 HOH   B O     1 
HETATM 19829 O  O     . HOH   AA 11 .    ? 15.228  54.292  66.076  1.00 26.99 ? 1732 HOH   B O     1 
HETATM 19830 O  O     . HOH   AA 11 .    ? 27.672  32.163  73.528  1.00 21.02 ? 1733 HOH   B O     1 
HETATM 19831 O  O     . HOH   AA 11 .    ? -8.053  12.753  96.611  1.00 20.70 ? 1734 HOH   B O     1 
HETATM 19832 O  O     . HOH   AA 11 .    ? 19.875  24.599  45.905  1.00 22.30 ? 1735 HOH   B O     1 
HETATM 19833 O  O     . HOH   AA 11 .    ? 12.146  70.267  60.707  1.00 36.20 ? 1736 HOH   B O     1 
HETATM 19834 O  O     . HOH   AA 11 .    ? -10.349 32.137  79.766  1.00 30.76 ? 1737 HOH   B O     1 
HETATM 19835 O  O     . HOH   AA 11 .    ? 6.593   33.961  86.358  1.00 19.13 ? 1738 HOH   B O     1 
HETATM 19836 O  O     . HOH   AA 11 .    ? 25.126  30.340  108.066 1.00 37.71 ? 1739 HOH   B O     1 
HETATM 19837 O  O     . HOH   AA 11 .    ? 1.680   20.957  89.188  1.00 22.34 ? 1740 HOH   B O     1 
HETATM 19838 O  O     . HOH   AA 11 .    ? 0.810   42.390  75.719  1.00 23.49 ? 1741 HOH   B O     1 
HETATM 19839 O  O     . HOH   AA 11 .    ? -3.416  11.040  83.917  1.00 24.89 ? 1742 HOH   B O     1 
HETATM 19840 O  O     . HOH   AA 11 .    ? 2.710   33.196  78.032  1.00 15.58 ? 1743 HOH   B O     1 
HETATM 19841 O  O     . HOH   AA 11 .    ? 31.567  54.102  67.514  1.00 26.25 ? 1744 HOH   B O     1 
HETATM 19842 O  O     . HOH   AA 11 .    ? 1.276   15.309  115.646 1.00 22.36 ? 1745 HOH   B O     1 
HETATM 19843 O  O     . HOH   AA 11 .    ? 18.283  43.969  91.037  1.00 14.45 ? 1746 HOH   B O     1 
HETATM 19844 O  O     . HOH   AA 11 .    ? 18.138  11.903  105.624 1.00 35.77 ? 1747 HOH   B O     1 
HETATM 19845 O  O     . HOH   AA 11 .    ? 37.391  31.417  81.291  1.00 26.97 ? 1748 HOH   B O     1 
HETATM 19846 O  O     . HOH   AA 11 .    ? 5.797   15.422  94.278  1.00 19.05 ? 1749 HOH   B O     1 
HETATM 19847 O  O     . HOH   AA 11 .    ? 31.146  21.592  79.520  1.00 20.28 ? 1750 HOH   B O     1 
HETATM 19848 O  O     . HOH   AA 11 .    ? 18.661  9.485   91.800  1.00 37.79 ? 1751 HOH   B O     1 
HETATM 19849 O  O     . HOH   AA 11 .    ? 2.642   70.236  63.756  1.00 32.83 ? 1752 HOH   B O     1 
HETATM 19850 O  O     . HOH   AA 11 .    ? 11.927  38.321  47.070  1.00 32.47 ? 1753 HOH   B O     1 
HETATM 19851 O  O     . HOH   AA 11 .    ? 28.596  46.809  92.110  1.00 36.05 ? 1754 HOH   B O     1 
HETATM 19852 O  O     . HOH   AA 11 .    ? 1.502   6.465   91.304  1.00 21.52 ? 1755 HOH   B O     1 
HETATM 19853 O  O     . HOH   AA 11 .    ? 2.556   39.713  98.284  1.00 21.89 ? 1756 HOH   B O     1 
HETATM 19854 O  O     . HOH   AA 11 .    ? -7.773  30.151  75.472  1.00 24.43 ? 1757 HOH   B O     1 
HETATM 19855 O  O     . HOH   AA 11 .    ? 19.426  54.960  93.055  1.00 24.86 ? 1758 HOH   B O     1 
HETATM 19856 O  O     . HOH   AA 11 .    ? -0.774  56.113  121.245 1.00 35.80 ? 1759 HOH   B O     1 
HETATM 19857 O  O     . HOH   AA 11 .    ? 23.748  26.288  50.237  1.00 28.45 ? 1760 HOH   B O     1 
HETATM 19858 O  O     . HOH   AA 11 .    ? 33.259  26.695  58.780  1.00 23.54 ? 1761 HOH   B O     1 
HETATM 19859 O  O     . HOH   AA 11 .    ? -7.067  35.087  128.572 1.00 40.11 ? 1762 HOH   B O     1 
HETATM 19860 O  O     . HOH   AA 11 .    ? 36.805  21.984  83.458  1.00 32.42 ? 1763 HOH   B O     1 
HETATM 19861 O  O     . HOH   AA 11 .    ? 1.723   10.324  78.682  1.00 31.66 ? 1764 HOH   B O     1 
HETATM 19862 O  O     . HOH   AA 11 .    ? -2.577  21.711  91.185  1.00 17.98 ? 1765 HOH   B O     1 
HETATM 19863 O  O     . HOH   AA 11 .    ? 5.154   3.728   92.573  1.00 24.85 ? 1766 HOH   B O     1 
HETATM 19864 O  O     . HOH   AA 11 .    ? 22.768  37.560  85.564  1.00 16.33 ? 1767 HOH   B O     1 
HETATM 19865 O  O     . HOH   AA 11 .    ? 26.910  49.132  94.251  1.00 27.64 ? 1768 HOH   B O     1 
HETATM 19866 O  O     . HOH   AA 11 .    ? 7.532   45.197  74.636  1.00 15.34 ? 1769 HOH   B O     1 
HETATM 19867 O  O     . HOH   AA 11 .    ? 22.344  12.412  71.117  1.00 25.32 ? 1770 HOH   B O     1 
HETATM 19868 O  O     . HOH   AA 11 .    ? 6.306   -3.794  104.081 1.00 32.11 ? 1771 HOH   B O     1 
HETATM 19869 O  O     . HOH   AA 11 .    ? -15.027 18.956  79.630  1.00 36.32 ? 1772 HOH   B O     1 
HETATM 19870 O  O     . HOH   AA 11 .    ? 4.820   22.299  83.344  1.00 23.00 ? 1773 HOH   B O     1 
HETATM 19871 O  O     . HOH   AA 11 .    ? 13.997  72.516  60.595  1.00 28.16 ? 1774 HOH   B O     1 
HETATM 19872 O  O     . HOH   AA 11 .    ? 15.970  48.774  70.311  1.00 16.63 ? 1775 HOH   B O     1 
HETATM 19873 O  O     . HOH   AA 11 .    ? 2.642   11.960  93.964  1.00 20.25 ? 1776 HOH   B O     1 
HETATM 19874 O  O     . HOH   AA 11 .    ? 12.807  50.260  64.558  1.00 24.59 ? 1777 HOH   B O     1 
HETATM 19875 O  O     . HOH   AA 11 .    ? -10.507 11.328  129.346 1.00 41.76 ? 1778 HOH   B O     1 
HETATM 19876 O  O     . HOH   AA 11 .    ? 19.758  33.314  67.058  1.00 14.48 ? 1779 HOH   B O     1 
HETATM 19877 O  O     . HOH   AA 11 .    ? 20.670  27.924  70.874  1.00 16.99 ? 1780 HOH   B O     1 
HETATM 19878 O  O     . HOH   AA 11 .    ? 23.515  33.279  91.129  1.00 18.30 ? 1781 HOH   B O     1 
HETATM 19879 O  O     . HOH   AA 11 .    ? 12.266  53.830  90.271  1.00 34.69 ? 1782 HOH   B O     1 
HETATM 19880 O  O     . HOH   AA 11 .    ? 10.921  9.399   69.523  1.00 30.18 ? 1783 HOH   B O     1 
HETATM 19881 O  O     . HOH   AA 11 .    ? 15.768  7.422   107.731 1.00 35.19 ? 1784 HOH   B O     1 
HETATM 19882 O  O     . HOH   AA 11 .    ? -0.249  40.421  77.350  1.00 24.91 ? 1785 HOH   B O     1 
HETATM 19883 O  O     . HOH   AA 11 .    ? -0.398  75.763  67.728  1.00 33.02 ? 1786 HOH   B O     1 
HETATM 19884 O  O     . HOH   AA 11 .    ? 7.826   56.982  87.014  1.00 33.42 ? 1787 HOH   B O     1 
HETATM 19885 O  O     . HOH   AA 11 .    ? 10.847  53.081  104.194 1.00 32.12 ? 1788 HOH   B O     1 
HETATM 19886 O  O     . HOH   AA 11 .    ? 11.926  49.888  88.092  1.00 20.43 ? 1789 HOH   B O     1 
HETATM 19887 O  O     . HOH   AA 11 .    ? -2.384  24.374  76.139  1.00 24.09 ? 1790 HOH   B O     1 
HETATM 19888 O  O     . HOH   AA 11 .    ? 17.834  24.068  110.070 1.00 24.49 ? 1791 HOH   B O     1 
HETATM 19889 O  O     . HOH   AA 11 .    ? -7.141  28.082  73.753  1.00 28.53 ? 1792 HOH   B O     1 
HETATM 19890 O  O     . HOH   AA 11 .    ? -17.154 16.495  130.676 1.00 40.85 ? 1793 HOH   B O     1 
HETATM 19891 O  O     . HOH   AA 11 .    ? 8.183   14.084  71.254  1.00 23.53 ? 1794 HOH   B O     1 
HETATM 19892 O  O     . HOH   AA 11 .    ? 8.395   40.932  86.387  1.00 16.45 ? 1795 HOH   B O     1 
HETATM 19893 O  O     . HOH   AA 11 .    ? 9.272   32.404  83.221  1.00 31.92 ? 1796 HOH   B O     1 
HETATM 19894 O  O     . HOH   AA 11 .    ? 17.310  28.921  110.403 1.00 27.32 ? 1797 HOH   B O     1 
HETATM 19895 O  O     . HOH   AA 11 .    ? 26.129  47.636  99.658  1.00 31.43 ? 1798 HOH   B O     1 
HETATM 19896 O  O     . HOH   AA 11 .    ? 0.089   12.622  93.256  1.00 18.19 ? 1799 HOH   B O     1 
HETATM 19897 O  O     . HOH   AA 11 .    ? 28.027  29.886  82.729  1.00 17.94 ? 1800 HOH   B O     1 
HETATM 19898 O  O     . HOH   AA 11 .    ? 3.998   17.763  74.929  1.00 26.34 ? 1801 HOH   B O     1 
HETATM 19899 O  O     . HOH   AA 11 .    ? 31.212  52.752  65.157  1.00 30.32 ? 1802 HOH   B O     1 
HETATM 19900 O  O     . HOH   AA 11 .    ? 23.319  52.211  62.037  1.00 21.64 ? 1803 HOH   B O     1 
HETATM 19901 O  O     . HOH   AA 11 .    ? 6.754   8.305   74.667  1.00 26.49 ? 1804 HOH   B O     1 
HETATM 19902 O  O     . HOH   AA 11 .    ? -29.796 18.781  103.055 1.00 31.78 ? 1805 HOH   B O     1 
HETATM 19903 O  O     . HOH   AA 11 .    ? -2.971  31.265  63.143  1.00 25.01 ? 1806 HOH   B O     1 
HETATM 19904 O  O     . HOH   AA 11 .    ? 12.010  21.206  58.603  1.00 18.62 ? 1807 HOH   B O     1 
HETATM 19905 O  O     . HOH   AA 11 .    ? 16.839  53.198  63.665  1.00 26.07 ? 1808 HOH   B O     1 
HETATM 19906 O  O     . HOH   AA 11 .    ? 11.775  12.265  120.939 1.00 28.82 ? 1809 HOH   B O     1 
HETATM 19907 O  O     . HOH   AA 11 .    ? 26.861  62.832  84.504  1.00 36.80 ? 1810 HOH   B O     1 
HETATM 19908 O  O     . HOH   AA 11 .    ? 25.234  14.097  64.790  1.00 31.34 ? 1811 HOH   B O     1 
HETATM 19909 O  O     . HOH   AA 11 .    ? 24.069  21.960  96.896  1.00 27.46 ? 1812 HOH   B O     1 
HETATM 19910 O  O     . HOH   AA 11 .    ? 39.606  29.769  87.458  1.00 22.73 ? 1813 HOH   B O     1 
HETATM 19911 O  O     . HOH   AA 11 .    ? 20.136  50.880  66.660  1.00 27.56 ? 1814 HOH   B O     1 
HETATM 19912 O  O     . HOH   AA 11 .    ? 14.991  7.286   68.535  1.00 29.83 ? 1815 HOH   B O     1 
HETATM 19913 O  O     . HOH   AA 11 .    ? 23.366  52.745  70.104  1.00 29.21 ? 1816 HOH   B O     1 
HETATM 19914 O  O     . HOH   AA 11 .    ? -25.084 10.780  87.057  1.00 34.34 ? 1817 HOH   B O     1 
HETATM 19915 O  O     . HOH   AA 11 .    ? -8.012  27.409  99.421  1.00 29.47 ? 1818 HOH   B O     1 
HETATM 19916 O  O     . HOH   AA 11 .    ? -0.020  19.781  93.579  1.00 20.90 ? 1819 HOH   B O     1 
HETATM 19917 O  O     . HOH   AA 11 .    ? 9.363   19.232  103.259 1.00 23.72 ? 1820 HOH   B O     1 
HETATM 19918 O  O     . HOH   AA 11 .    ? 32.985  58.197  73.782  1.00 31.03 ? 1821 HOH   B O     1 
HETATM 19919 O  O     . HOH   AA 11 .    ? 21.243  54.017  83.188  1.00 27.95 ? 1822 HOH   B O     1 
HETATM 19920 O  O     . HOH   AA 11 .    ? 30.646  40.538  56.937  1.00 26.70 ? 1823 HOH   B O     1 
HETATM 19921 O  O     . HOH   AA 11 .    ? -3.056  -1.939  94.205  1.00 29.34 ? 1824 HOH   B O     1 
HETATM 19922 O  O     . HOH   AA 11 .    ? 17.076  34.469  55.634  1.00 16.16 ? 1825 HOH   B O     1 
HETATM 19923 O  O     . HOH   AA 11 .    ? 29.547  58.381  81.921  1.00 38.17 ? 1826 HOH   B O     1 
HETATM 19924 O  O     . HOH   AA 11 .    ? 22.514  54.455  92.595  1.00 25.96 ? 1827 HOH   B O     1 
HETATM 19925 O  O     . HOH   AA 11 .    ? 13.874  3.754   84.219  1.00 40.32 ? 1828 HOH   B O     1 
HETATM 19926 O  O     . HOH   AA 11 .    ? -6.815  35.547  68.728  1.00 30.17 ? 1829 HOH   B O     1 
HETATM 19927 O  O     . HOH   AA 11 .    ? 8.555   23.435  84.292  1.00 33.22 ? 1830 HOH   B O     1 
HETATM 19928 O  O     . HOH   AA 11 .    ? 2.524   53.830  68.977  1.00 30.43 ? 1831 HOH   B O     1 
HETATM 19929 O  O     . HOH   AA 11 .    ? 11.585  34.674  51.562  1.00 29.31 ? 1832 HOH   B O     1 
HETATM 19930 O  O     . HOH   AA 11 .    ? -13.599 12.895  93.395  1.00 19.85 ? 1833 HOH   B O     1 
HETATM 19931 O  O     . HOH   AA 11 .    ? 28.253  13.668  85.592  1.00 27.47 ? 1834 HOH   B O     1 
HETATM 19932 O  O     . HOH   AA 11 .    ? 3.815   10.857  91.876  1.00 20.01 ? 1835 HOH   B O     1 
HETATM 19933 O  O     . HOH   AA 11 .    ? -6.721  14.588  91.050  1.00 19.00 ? 1836 HOH   B O     1 
HETATM 19934 O  O     . HOH   AA 11 .    ? 26.474  23.054  49.983  1.00 35.90 ? 1837 HOH   B O     1 
HETATM 19935 O  O     . HOH   AA 11 .    ? -3.464  -10.792 100.280 1.00 25.82 ? 1838 HOH   B O     1 
HETATM 19936 O  O     . HOH   AA 11 .    ? 34.698  27.169  99.837  1.00 39.17 ? 1839 HOH   B O     1 
HETATM 19937 O  O     . HOH   AA 11 .    ? 1.503   15.445  81.824  1.00 21.36 ? 1840 HOH   B O     1 
HETATM 19938 O  O     . HOH   AA 11 .    ? 20.053  54.405  80.836  1.00 20.62 ? 1841 HOH   B O     1 
HETATM 19939 O  O     . HOH   AA 11 .    ? -2.752  26.960  60.072  1.00 34.84 ? 1842 HOH   B O     1 
HETATM 19940 O  O     . HOH   AA 11 .    ? -10.659 2.072   90.859  1.00 26.46 ? 1843 HOH   B O     1 
HETATM 19941 O  O     . HOH   AA 11 .    ? -1.222  51.112  64.510  1.00 18.99 ? 1844 HOH   B O     1 
HETATM 19942 O  O     . HOH   AA 11 .    ? 22.152  24.782  108.088 1.00 25.72 ? 1845 HOH   B O     1 
HETATM 19943 O  O     . HOH   AA 11 .    ? -8.207  2.813   91.898  1.00 23.93 ? 1846 HOH   B O     1 
HETATM 19944 O  O     . HOH   AA 11 .    ? 12.130  8.182   90.005  1.00 22.79 ? 1847 HOH   B O     1 
HETATM 19945 O  O     . HOH   AA 11 .    ? 6.801   -7.946  106.967 1.00 36.56 ? 1848 HOH   B O     1 
HETATM 19946 O  O     . HOH   AA 11 .    ? 9.032   62.133  84.770  1.00 25.70 ? 1849 HOH   B O     1 
HETATM 19947 O  O     . HOH   AA 11 .    ? 19.673  19.450  66.016  1.00 16.15 ? 1850 HOH   B O     1 
HETATM 19948 O  O     . HOH   AA 11 .    ? 7.253   38.083  102.418 1.00 28.37 ? 1851 HOH   B O     1 
HETATM 19949 O  O     . HOH   AA 11 .    ? -1.107  21.077  89.071  1.00 19.49 ? 1852 HOH   B O     1 
HETATM 19950 O  O     . HOH   AA 11 .    ? -6.212  34.729  83.309  1.00 27.05 ? 1853 HOH   B O     1 
HETATM 19951 O  O     . HOH   AA 11 .    ? 0.308   27.211  94.298  1.00 20.59 ? 1854 HOH   B O     1 
HETATM 19952 O  O     . HOH   AA 11 .    ? 17.059  34.174  48.124  1.00 32.22 ? 1855 HOH   B O     1 
HETATM 19953 O  O     . HOH   AA 11 .    ? 32.935  46.310  66.977  1.00 29.50 ? 1856 HOH   B O     1 
HETATM 19954 O  O     . HOH   AA 11 .    ? 1.145   9.737   89.196  1.00 23.07 ? 1857 HOH   B O     1 
HETATM 19955 O  O     . HOH   AA 11 .    ? -1.300  66.899  83.460  1.00 26.36 ? 1858 HOH   B O     1 
HETATM 19956 O  O     . HOH   AA 11 .    ? -9.780  6.354   86.560  1.00 28.04 ? 1859 HOH   B O     1 
HETATM 19957 O  O     . HOH   AA 11 .    ? 15.945  16.333  84.904  1.00 19.68 ? 1860 HOH   B O     1 
HETATM 19958 O  O     . HOH   AA 11 .    ? -3.442  66.423  76.728  1.00 26.73 ? 1861 HOH   B O     1 
HETATM 19959 O  O     . HOH   AA 11 .    ? 6.161   16.453  121.294 1.00 31.37 ? 1862 HOH   B O     1 
HETATM 19960 O  O     . HOH   AA 11 .    ? 23.255  76.698  65.096  1.00 43.68 ? 1863 HOH   B O     1 
HETATM 19961 O  O     . HOH   AA 11 .    ? -6.168  48.255  78.435  1.00 36.25 ? 1864 HOH   B O     1 
HETATM 19962 O  O     . HOH   AA 11 .    ? 18.381  15.257  97.108  1.00 27.46 ? 1865 HOH   B O     1 
HETATM 19963 O  O     . HOH   AA 11 .    ? -24.170 -1.541  111.925 1.00 48.00 ? 1866 HOH   B O     1 
HETATM 19964 O  O     . HOH   AA 11 .    ? 13.065  56.086  65.185  1.00 27.64 ? 1867 HOH   B O     1 
HETATM 19965 O  O     . HOH   AA 11 .    ? -6.758  6.788   118.066 1.00 24.36 ? 1868 HOH   B O     1 
HETATM 19966 O  O     . HOH   AA 11 .    ? 2.127   20.623  92.085  1.00 33.88 ? 1869 HOH   B O     1 
HETATM 19967 O  O     . HOH   AA 11 .    ? 20.275  52.756  68.883  1.00 21.16 ? 1870 HOH   B O     1 
HETATM 19968 O  O     . HOH   AA 11 .    ? 43.629  37.006  87.584  1.00 26.90 ? 1871 HOH   B O     1 
HETATM 19969 O  O     . HOH   AA 11 .    ? -5.134  16.634  96.426  1.00 18.10 ? 1872 HOH   B O     1 
HETATM 19970 O  O     . HOH   AA 11 .    ? 1.141   -0.474  92.312  1.00 29.37 ? 1873 HOH   B O     1 
HETATM 19971 O  O     . HOH   AA 11 .    ? -4.834  37.161  89.386  1.00 30.59 ? 1874 HOH   B O     1 
HETATM 19972 O  O     . HOH   AA 11 .    ? 4.893   47.751  86.649  1.00 19.89 ? 1875 HOH   B O     1 
HETATM 19973 O  O     . HOH   AA 11 .    ? 29.521  60.544  58.590  1.00 30.27 ? 1876 HOH   B O     1 
HETATM 19974 O  O     . HOH   AA 11 .    ? 25.377  54.032  73.343  1.00 22.58 ? 1877 HOH   B O     1 
HETATM 19975 O  O     . HOH   AA 11 .    ? 8.482   15.179  89.996  1.00 23.73 ? 1878 HOH   B O     1 
HETATM 19976 O  O     . HOH   AA 11 .    ? 0.201   47.989  76.016  1.00 18.99 ? 1879 HOH   B O     1 
HETATM 19977 O  O     . HOH   AA 11 .    ? -1.671  25.651  79.529  1.00 22.90 ? 1880 HOH   B O     1 
HETATM 19978 O  O     . HOH   AA 11 .    ? 4.653   46.859  68.776  1.00 15.78 ? 1881 HOH   B O     1 
HETATM 19979 O  O     . HOH   AA 11 .    ? 19.090  8.491   83.688  1.00 26.91 ? 1882 HOH   B O     1 
HETATM 19980 O  O     . HOH   AA 11 .    ? 20.509  55.912  84.945  1.00 38.93 ? 1883 HOH   B O     1 
HETATM 19981 O  O     . HOH   AA 11 .    ? 26.905  52.897  74.969  1.00 25.74 ? 1884 HOH   B O     1 
HETATM 19982 O  O     . HOH   AA 11 .    ? -1.220  60.707  76.969  1.00 21.24 ? 1885 HOH   B O     1 
HETATM 19983 O  O     . HOH   AA 11 .    ? 3.100   23.236  58.488  1.00 31.75 ? 1886 HOH   B O     1 
HETATM 19984 O  O     . HOH   AA 11 .    ? 2.319   63.436  77.911  1.00 18.07 ? 1887 HOH   B O     1 
HETATM 19985 O  O     . HOH   AA 11 .    ? -1.506  5.739   91.688  1.00 21.32 ? 1888 HOH   B O     1 
HETATM 19986 O  O     . HOH   AA 11 .    ? 2.121   62.307  68.316  1.00 33.36 ? 1889 HOH   B O     1 
HETATM 19987 O  O     . HOH   AA 11 .    ? 26.283  40.041  52.574  1.00 25.97 ? 1890 HOH   B O     1 
HETATM 19988 O  O     . HOH   AA 11 .    ? 12.436  6.347   84.142  1.00 24.43 ? 1891 HOH   B O     1 
HETATM 19989 O  O     . HOH   AA 11 .    ? 13.033  51.513  86.043  1.00 28.45 ? 1892 HOH   B O     1 
HETATM 19990 O  O     . HOH   AA 11 .    ? -6.224  12.995  98.772  1.00 18.24 ? 1893 HOH   B O     1 
HETATM 19991 O  O     . HOH   AA 11 .    ? 17.842  54.114  82.495  1.00 25.18 ? 1894 HOH   B O     1 
HETATM 19992 O  O     . HOH   AA 11 .    ? 40.294  23.420  57.901  1.00 44.46 ? 1895 HOH   B O     1 
HETATM 19993 O  O     . HOH   AA 11 .    ? 26.747  66.070  57.450  1.00 36.99 ? 1896 HOH   B O     1 
HETATM 19994 O  O     . HOH   AA 11 .    ? -14.640 7.608   119.761 1.00 29.15 ? 1897 HOH   B O     1 
HETATM 19995 O  O     . HOH   AA 11 .    ? -0.354  39.908  130.909 1.00 40.42 ? 1898 HOH   B O     1 
HETATM 19996 O  O     . HOH   AA 11 .    ? -17.685 54.767  120.821 1.00 38.63 ? 1899 HOH   B O     1 
HETATM 19997 O  O     . HOH   AA 11 .    ? 4.824   60.748  67.417  1.00 36.91 ? 1900 HOH   B O     1 
HETATM 19998 O  O     . HOH   AA 11 .    ? 32.603  47.553  91.550  1.00 39.11 ? 1901 HOH   B O     1 
HETATM 19999 O  O     . HOH   AA 11 .    ? 23.313  12.763  67.712  1.00 24.68 ? 1902 HOH   B O     1 
HETATM 20000 O  O     . HOH   AA 11 .    ? 30.004  20.619  76.450  1.00 29.94 ? 1903 HOH   B O     1 
HETATM 20001 O  O     . HOH   AA 11 .    ? 11.648  16.720  67.351  1.00 31.01 ? 1904 HOH   B O     1 
HETATM 20002 O  O     . HOH   AA 11 .    ? 23.817  31.837  109.826 1.00 29.69 ? 1905 HOH   B O     1 
HETATM 20003 O  O     . HOH   AA 11 .    ? 28.470  37.260  82.422  1.00 30.95 ? 1906 HOH   B O     1 
HETATM 20004 O  O     . HOH   AA 11 .    ? 27.041  35.657  90.546  1.00 17.48 ? 1907 HOH   B O     1 
HETATM 20005 O  O     . HOH   AA 11 .    ? -4.351  0.028   110.123 1.00 25.17 ? 1908 HOH   B O     1 
HETATM 20006 O  O     . HOH   AA 11 .    ? 20.440  75.530  62.551  1.00 37.92 ? 1909 HOH   B O     1 
HETATM 20007 O  O     . HOH   AA 11 .    ? -3.523  68.091  70.089  1.00 38.50 ? 1910 HOH   B O     1 
HETATM 20008 O  O     . HOH   AA 11 .    ? 23.470  52.086  83.484  1.00 24.81 ? 1911 HOH   B O     1 
HETATM 20009 O  O     . HOH   AA 11 .    ? 15.787  10.688  112.166 1.00 41.24 ? 1912 HOH   B O     1 
HETATM 20010 O  O     . HOH   AA 11 .    ? -16.320 25.698  106.271 1.00 35.02 ? 1913 HOH   B O     1 
HETATM 20011 O  O     . HOH   AA 11 .    ? 14.460  45.927  77.908  1.00 16.74 ? 1914 HOH   B O     1 
HETATM 20012 O  O     . HOH   AA 11 .    ? -5.229  10.019  114.462 1.00 27.29 ? 1915 HOH   B O     1 
HETATM 20013 O  O     . HOH   AA 11 .    ? 2.724   6.231   79.836  1.00 31.43 ? 1916 HOH   B O     1 
HETATM 20014 O  O     . HOH   AA 11 .    ? 10.249  66.673  86.093  1.00 36.67 ? 1917 HOH   B O     1 
HETATM 20015 O  O     . HOH   AA 11 .    ? 21.562  7.270   83.159  1.00 34.23 ? 1918 HOH   B O     1 
HETATM 20016 O  O     . HOH   AA 11 .    ? 27.217  18.692  61.706  1.00 24.18 ? 1919 HOH   B O     1 
HETATM 20017 O  O     . HOH   AA 11 .    ? 27.107  42.792  104.355 1.00 29.37 ? 1920 HOH   B O     1 
HETATM 20018 O  O     . HOH   AA 11 .    ? 27.818  11.046  84.450  1.00 27.40 ? 1921 HOH   B O     1 
HETATM 20019 O  O     . HOH   AA 11 .    ? 0.908   10.879  129.109 1.00 25.46 ? 1922 HOH   B O     1 
HETATM 20020 O  O     . HOH   AA 11 .    ? -10.878 36.404  75.844  1.00 39.36 ? 1923 HOH   B O     1 
HETATM 20021 O  O     . HOH   AA 11 .    ? 7.397   20.787  101.838 1.00 27.29 ? 1924 HOH   B O     1 
HETATM 20022 O  O     . HOH   AA 11 .    ? 22.768  23.941  84.382  1.00 18.47 ? 1925 HOH   B O     1 
HETATM 20023 O  O     . HOH   AA 11 .    ? 18.923  30.797  88.127  1.00 19.81 ? 1926 HOH   B O     1 
HETATM 20024 O  O     . HOH   AA 11 .    ? -2.908  55.104  83.205  1.00 32.07 ? 1927 HOH   B O     1 
HETATM 20025 O  O     . HOH   AA 11 .    ? 5.155   42.947  70.351  1.00 14.84 ? 1928 HOH   B O     1 
HETATM 20026 O  O     . HOH   AA 11 .    ? 29.963  33.576  73.051  1.00 26.42 ? 1929 HOH   B O     1 
HETATM 20027 O  O     . HOH   AA 11 .    ? 0.689   -7.573  109.023 1.00 30.20 ? 1930 HOH   B O     1 
HETATM 20028 O  O     . HOH   AA 11 .    ? 2.032   40.539  113.943 1.00 28.28 ? 1931 HOH   B O     1 
HETATM 20029 O  O     . HOH   AA 11 .    ? 6.389   82.060  75.060  1.00 36.12 ? 1932 HOH   B O     1 
HETATM 20030 O  O     . HOH   AA 11 .    ? 1.688   66.081  65.205  1.00 39.48 ? 1933 HOH   B O     1 
HETATM 20031 O  O     . HOH   AA 11 .    ? 36.939  28.218  92.730  1.00 32.38 ? 1934 HOH   B O     1 
HETATM 20032 O  O     . HOH   AA 11 .    ? 27.291  23.256  88.263  1.00 18.60 ? 1935 HOH   B O     1 
HETATM 20033 O  O     . HOH   AA 11 .    ? -5.508  -1.822  116.564 1.00 29.20 ? 1936 HOH   B O     1 
HETATM 20034 O  O     . HOH   AA 11 .    ? 18.585  34.633  45.746  1.00 36.10 ? 1937 HOH   B O     1 
HETATM 20035 O  O     . HOH   AA 11 .    ? -4.461  55.913  81.214  1.00 28.31 ? 1938 HOH   B O     1 
HETATM 20036 O  O     . HOH   AA 11 .    ? 28.619  46.729  87.397  1.00 29.62 ? 1939 HOH   B O     1 
HETATM 20037 O  O     . HOH   AA 11 .    ? 24.668  51.115  66.698  1.00 22.67 ? 1940 HOH   B O     1 
HETATM 20038 O  O     . HOH   AA 11 .    ? -18.545 10.316  83.249  1.00 38.66 ? 1941 HOH   B O     1 
HETATM 20039 O  O     . HOH   AA 11 .    ? -2.561  60.334  119.569 1.00 29.01 ? 1942 HOH   B O     1 
HETATM 20040 O  O     . HOH   AA 11 .    ? -12.042 35.049  86.051  1.00 40.60 ? 1943 HOH   B O     1 
HETATM 20041 O  O     . HOH   AA 11 .    ? 18.505  67.152  58.081  1.00 31.29 ? 1944 HOH   B O     1 
HETATM 20042 O  O     . HOH   AA 11 .    ? 19.558  78.385  76.541  1.00 39.93 ? 1945 HOH   B O     1 
HETATM 20043 O  O     . HOH   AA 11 .    ? 30.449  20.550  73.277  1.00 31.24 ? 1946 HOH   B O     1 
HETATM 20044 O  O     . HOH   AA 11 .    ? 12.473  2.457   91.787  1.00 35.99 ? 1947 HOH   B O     1 
HETATM 20045 O  O     . HOH   AA 11 .    ? 15.184  49.206  56.784  1.00 25.87 ? 1948 HOH   B O     1 
HETATM 20046 O  O     . HOH   AA 11 .    ? 4.890   18.187  90.746  1.00 22.99 ? 1949 HOH   B O     1 
HETATM 20047 O  O     . HOH   AA 11 .    ? 13.116  26.134  95.572  1.00 29.71 ? 1950 HOH   B O     1 
HETATM 20048 O  O     . HOH   AA 11 .    ? -2.962  33.980  62.053  1.00 22.06 ? 1951 HOH   B O     1 
HETATM 20049 O  O     . HOH   AA 11 .    ? 28.130  25.896  67.384  1.00 19.32 ? 1952 HOH   B O     1 
HETATM 20050 O  O     . HOH   AA 11 .    ? -5.580  12.822  83.992  1.00 27.68 ? 1953 HOH   B O     1 
HETATM 20051 O  O     . HOH   AA 11 .    ? 3.028   35.699  120.821 1.00 35.15 ? 1954 HOH   B O     1 
HETATM 20052 O  O     . HOH   AA 11 .    ? -16.148 52.257  123.040 1.00 37.98 ? 1955 HOH   B O     1 
HETATM 20053 O  O     . HOH   AA 11 .    ? 15.555  26.978  80.744  1.00 30.84 ? 1956 HOH   B O     1 
HETATM 20054 O  O     . HOH   AA 11 .    ? -11.309 -4.581  97.341  1.00 39.48 ? 1957 HOH   B O     1 
HETATM 20055 O  O     . HOH   AA 11 .    ? 32.627  33.426  70.242  1.00 29.77 ? 1958 HOH   B O     1 
HETATM 20056 O  O     . HOH   AA 11 .    ? -6.160  41.915  83.686  1.00 32.80 ? 1959 HOH   B O     1 
HETATM 20057 O  O     . HOH   AA 11 .    ? -1.054  55.775  71.991  1.00 27.99 ? 1960 HOH   B O     1 
HETATM 20058 O  O     . HOH   AA 11 .    ? 22.752  12.125  87.219  1.00 29.98 ? 1961 HOH   B O     1 
HETATM 20059 O  O     . HOH   AA 11 .    ? 6.022   31.560  120.115 1.00 49.71 ? 1962 HOH   B O     1 
HETATM 20060 O  O     . HOH   AA 11 .    ? -1.711  49.517  100.767 1.00 31.11 ? 1963 HOH   B O     1 
HETATM 20061 O  O     . HOH   AA 11 .    ? 24.747  57.695  77.919  1.00 22.95 ? 1964 HOH   B O     1 
HETATM 20062 O  O     . HOH   AA 11 .    ? 21.991  46.532  76.289  1.00 18.37 ? 1965 HOH   B O     1 
HETATM 20063 O  O     . HOH   AA 11 .    ? 19.505  16.378  63.304  1.00 20.60 ? 1966 HOH   B O     1 
HETATM 20064 O  O     . HOH   AA 11 .    ? -3.057  11.250  103.342 1.00 18.30 ? 1967 HOH   B O     1 
HETATM 20065 O  O     . HOH   AA 11 .    ? 11.551  26.437  101.256 1.00 27.13 ? 1968 HOH   B O     1 
HETATM 20066 O  O     . HOH   AA 11 .    ? 29.010  24.311  50.764  1.00 30.29 ? 1969 HOH   B O     1 
HETATM 20067 O  O     . HOH   AA 11 .    ? 0.346   36.737  108.403 1.00 33.30 ? 1970 HOH   B O     1 
HETATM 20068 O  O     . HOH   AA 11 .    ? -24.112 24.288  103.763 1.00 40.42 ? 1971 HOH   B O     1 
HETATM 20069 O  O     . HOH   AA 11 .    ? 4.697   19.001  123.704 1.00 29.45 ? 1972 HOH   B O     1 
HETATM 20070 O  O     . HOH   AA 11 .    ? 32.892  45.582  74.582  1.00 27.28 ? 1973 HOH   B O     1 
HETATM 20071 O  O     . HOH   AA 11 .    ? 41.176  34.788  90.984  1.00 23.20 ? 1974 HOH   B O     1 
HETATM 20072 O  O     . HOH   AA 11 .    ? 8.092   62.956  65.802  1.00 32.49 ? 1975 HOH   B O     1 
HETATM 20073 O  O     . HOH   AA 11 .    ? 32.441  70.300  73.397  1.00 33.24 ? 1976 HOH   B O     1 
HETATM 20074 O  O     . HOH   AA 11 .    ? 6.253   12.531  126.103 1.00 21.68 ? 1977 HOH   B O     1 
HETATM 20075 O  O     . HOH   AA 11 .    ? 1.585   46.653  98.450  1.00 27.84 ? 1978 HOH   B O     1 
HETATM 20076 O  O     . HOH   AA 11 .    ? 36.198  20.690  89.739  1.00 42.18 ? 1979 HOH   B O     1 
HETATM 20077 O  O     . HOH   AA 11 .    ? -1.793  28.452  62.223  1.00 27.99 ? 1980 HOH   B O     1 
HETATM 20078 O  O     . HOH   AA 11 .    ? 31.372  54.476  58.968  1.00 44.74 ? 1981 HOH   B O     1 
HETATM 20079 O  O     . HOH   AA 11 .    ? 16.315  21.783  99.379  1.00 21.63 ? 1982 HOH   B O     1 
HETATM 20080 O  O     . HOH   AA 11 .    ? -3.426  46.201  106.461 1.00 24.60 ? 1983 HOH   B O     1 
HETATM 20081 O  O     . HOH   AA 11 .    ? 10.117  70.384  86.107  1.00 39.26 ? 1984 HOH   B O     1 
HETATM 20082 O  O     . HOH   AA 11 .    ? -6.634  11.471  127.205 1.00 35.73 ? 1985 HOH   B O     1 
HETATM 20083 O  O     . HOH   AA 11 .    ? 26.922  59.371  78.206  1.00 21.54 ? 1986 HOH   B O     1 
HETATM 20084 O  O     . HOH   AA 11 .    ? 38.869  25.844  80.043  1.00 37.88 ? 1987 HOH   B O     1 
HETATM 20085 O  O     . HOH   AA 11 .    ? -18.249 2.402   94.975  1.00 43.90 ? 1988 HOH   B O     1 
HETATM 20086 O  O     . HOH   AA 11 .    ? 9.894   2.680   116.851 1.00 30.76 ? 1989 HOH   B O     1 
HETATM 20087 O  O     . HOH   AA 11 .    ? 37.732  23.335  90.101  1.00 46.63 ? 1990 HOH   B O     1 
HETATM 20088 O  O     . HOH   AA 11 .    ? 0.637   0.471   95.736  1.00 26.98 ? 1991 HOH   B O     1 
HETATM 20089 O  O     . HOH   AA 11 .    ? -0.527  18.253  91.045  1.00 24.51 ? 1992 HOH   B O     1 
HETATM 20090 O  O     . HOH   AA 11 .    ? -23.001 26.154  102.782 1.00 38.72 ? 1993 HOH   B O     1 
HETATM 20091 O  O     . HOH   AA 11 .    ? 26.229  27.853  66.773  1.00 16.59 ? 1994 HOH   B O     1 
HETATM 20092 O  O     . HOH   AA 11 .    ? -9.261  45.866  130.479 1.00 35.88 ? 1995 HOH   B O     1 
HETATM 20093 O  O     . HOH   AA 11 .    ? -11.488 -1.717  96.045  1.00 30.09 ? 1996 HOH   B O     1 
HETATM 20094 O  O     . HOH   AA 11 .    ? -14.575 40.140  124.259 1.00 37.70 ? 1997 HOH   B O     1 
HETATM 20095 O  O     . HOH   AA 11 .    ? 22.815  10.080  84.764  1.00 36.97 ? 1998 HOH   B O     1 
HETATM 20096 O  O     . HOH   AA 11 .    ? 22.030  25.434  82.132  1.00 21.89 ? 1999 HOH   B O     1 
HETATM 20097 O  O     . HOH   AA 11 .    ? 1.139   81.127  75.496  1.00 44.73 ? 2000 HOH   B O     1 
HETATM 20098 O  O     . HOH   AA 11 .    ? 24.860  16.298  94.669  1.00 24.25 ? 2001 HOH   B O     1 
HETATM 20099 O  O     . HOH   AA 11 .    ? 10.531  33.719  108.930 1.00 26.49 ? 2002 HOH   B O     1 
HETATM 20100 O  O     . HOH   AA 11 .    ? -5.682  35.809  87.295  1.00 31.78 ? 2003 HOH   B O     1 
HETATM 20101 O  O     . HOH   AA 11 .    ? 5.617   18.854  86.966  1.00 25.28 ? 2004 HOH   B O     1 
HETATM 20102 O  O     . HOH   AA 11 .    ? 19.983  22.849  74.151  1.00 29.29 ? 2005 HOH   B O     1 
HETATM 20103 O  O     . HOH   AA 11 .    ? -20.464 25.629  93.987  1.00 30.28 ? 2006 HOH   B O     1 
HETATM 20104 O  O     . HOH   AA 11 .    ? -14.406 16.034  78.244  1.00 38.71 ? 2007 HOH   B O     1 
HETATM 20105 O  O     . HOH   AA 11 .    ? 30.930  51.447  79.732  1.00 32.41 ? 2008 HOH   B O     1 
HETATM 20106 O  O     . HOH   AA 11 .    ? 31.470  62.592  74.759  1.00 21.95 ? 2009 HOH   B O     1 
HETATM 20107 O  O     . HOH   AA 11 .    ? -7.001  44.107  73.458  1.00 30.24 ? 2010 HOH   B O     1 
HETATM 20108 O  O     . HOH   AA 11 .    ? 2.566   49.221  75.705  1.00 19.10 ? 2011 HOH   B O     1 
HETATM 20109 O  O     . HOH   AA 11 .    ? 9.998   53.429  65.252  1.00 25.22 ? 2012 HOH   B O     1 
HETATM 20110 O  O     . HOH   AA 11 .    ? 18.409  53.470  75.539  1.00 18.55 ? 2013 HOH   B O     1 
HETATM 20111 O  O     . HOH   AA 11 .    ? 13.076  48.327  81.754  1.00 24.45 ? 2014 HOH   B O     1 
HETATM 20112 O  O     . HOH   AA 11 .    ? 7.950   58.373  84.723  1.00 23.64 ? 2015 HOH   B O     1 
HETATM 20113 O  O     . HOH   AA 11 .    ? 10.773  29.639  93.702  1.00 26.48 ? 2016 HOH   B O     1 
HETATM 20114 O  O     . HOH   AA 11 .    ? 8.884   6.345   84.655  1.00 23.20 ? 2017 HOH   B O     1 
HETATM 20115 O  O     . HOH   AA 11 .    ? 18.162  23.606  61.089  1.00 21.62 ? 2018 HOH   B O     1 
HETATM 20116 O  O     . HOH   AA 11 .    ? 14.684  17.022  91.534  1.00 22.85 ? 2019 HOH   B O     1 
HETATM 20117 O  O     . HOH   AA 11 .    ? 31.201  46.415  78.310  1.00 34.37 ? 2020 HOH   B O     1 
HETATM 20118 O  O     . HOH   AA 11 .    ? 35.115  19.588  59.486  1.00 39.54 ? 2021 HOH   B O     1 
HETATM 20119 O  O     . HOH   AA 11 .    ? 32.973  38.259  103.950 1.00 30.93 ? 2022 HOH   B O     1 
HETATM 20120 O  O     . HOH   AA 11 .    ? 28.162  9.343   73.512  1.00 33.45 ? 2023 HOH   B O     1 
HETATM 20121 O  O     . HOH   AA 11 .    ? -14.238 9.755   86.922  1.00 24.89 ? 2024 HOH   B O     1 
HETATM 20122 O  O     . HOH   AA 11 .    ? 33.402  19.674  87.175  1.00 23.10 ? 2025 HOH   B O     1 
HETATM 20123 O  O     . HOH   AA 11 .    ? 18.923  52.293  79.542  1.00 20.42 ? 2026 HOH   B O     1 
HETATM 20124 O  O     . HOH   AA 11 .    ? 9.465   29.715  97.930  1.00 29.78 ? 2027 HOH   B O     1 
HETATM 20125 O  O     . HOH   AA 11 .    ? -10.718 12.804  78.880  1.00 42.04 ? 2028 HOH   B O     1 
HETATM 20126 O  O     . HOH   AA 11 .    ? 34.428  13.307  80.558  1.00 32.67 ? 2029 HOH   B O     1 
HETATM 20127 O  O     . HOH   AA 11 .    ? -24.911 17.053  81.623  1.00 35.15 ? 2030 HOH   B O     1 
HETATM 20128 O  O     . HOH   AA 11 .    ? -4.340  54.196  130.369 1.00 37.49 ? 2031 HOH   B O     1 
HETATM 20129 O  O     . HOH   AA 11 .    ? 32.462  29.423  64.242  1.00 22.82 ? 2032 HOH   B O     1 
HETATM 20130 O  O     . HOH   AA 11 .    ? 27.953  75.921  70.211  1.00 44.73 ? 2033 HOH   B O     1 
HETATM 20131 O  O     . HOH   AA 11 .    ? 17.423  34.400  68.019  1.00 14.39 ? 2034 HOH   B O     1 
HETATM 20132 O  O     . HOH   AA 11 .    ? 21.052  47.885  55.647  1.00 30.71 ? 2035 HOH   B O     1 
HETATM 20133 O  O     . HOH   AA 11 .    ? -1.774  37.014  86.954  1.00 20.70 ? 2036 HOH   B O     1 
HETATM 20134 O  O     . HOH   AA 11 .    ? 31.164  34.856  76.702  1.00 31.55 ? 2037 HOH   B O     1 
HETATM 20135 O  O     . HOH   AA 11 .    ? -4.356  42.661  107.762 1.00 35.26 ? 2038 HOH   B O     1 
HETATM 20136 O  O     . HOH   AA 11 .    ? 25.643  33.564  109.359 1.00 38.16 ? 2039 HOH   B O     1 
HETATM 20137 O  O     . HOH   AA 11 .    ? -2.439  14.910  80.444  1.00 41.75 ? 2040 HOH   B O     1 
HETATM 20138 O  O     . HOH   AA 11 .    ? 26.221  20.498  52.640  1.00 28.14 ? 2041 HOH   B O     1 
HETATM 20139 O  O     . HOH   AA 11 .    ? 34.062  22.727  77.863  1.00 27.24 ? 2042 HOH   B O     1 
HETATM 20140 O  O     . HOH   AA 11 .    ? 30.630  34.553  84.117  1.00 25.61 ? 2043 HOH   B O     1 
HETATM 20141 O  O     . HOH   AA 11 .    ? 8.310   37.707  78.737  1.00 18.88 ? 2044 HOH   B O     1 
HETATM 20142 O  O     . HOH   AA 11 .    ? 10.086  22.348  102.222 1.00 33.35 ? 2045 HOH   B O     1 
HETATM 20143 O  O     . HOH   AA 11 .    ? 17.726  50.046  111.196 1.00 34.52 ? 2046 HOH   B O     1 
HETATM 20144 O  O     . HOH   AA 11 .    ? 16.201  53.778  104.417 1.00 27.23 ? 2047 HOH   B O     1 
HETATM 20145 O  O     . HOH   AA 11 .    ? 0.224   11.359  80.719  1.00 34.56 ? 2048 HOH   B O     1 
HETATM 20146 O  O     . HOH   AA 11 .    ? 3.454   41.157  116.836 1.00 29.55 ? 2049 HOH   B O     1 
HETATM 20147 O  O     . HOH   AA 11 .    ? 0.542   21.447  131.593 1.00 35.78 ? 2050 HOH   B O     1 
HETATM 20148 O  O     . HOH   AA 11 .    ? -2.593  14.830  98.267  1.00 17.75 ? 2051 HOH   B O     1 
HETATM 20149 O  O     . HOH   AA 11 .    ? 1.904   30.833  95.514  1.00 22.71 ? 2052 HOH   B O     1 
HETATM 20150 O  O     . HOH   AA 11 .    ? 33.045  25.764  101.472 1.00 28.62 ? 2053 HOH   B O     1 
HETATM 20151 O  O     . HOH   AA 11 .    ? -0.951  13.841  100.283 1.00 18.63 ? 2054 HOH   B O     1 
HETATM 20152 O  O     . HOH   AA 11 .    ? -2.962  40.051  57.478  1.00 24.43 ? 2055 HOH   B O     1 
HETATM 20153 O  O     . HOH   AA 11 .    ? -13.397 54.116  122.130 1.00 31.21 ? 2056 HOH   B O     1 
HETATM 20154 O  O     . HOH   AA 11 .    ? 34.769  17.131  67.207  1.00 31.92 ? 2057 HOH   B O     1 
HETATM 20155 O  O     . HOH   AA 11 .    ? 35.549  25.805  77.308  1.00 26.22 ? 2058 HOH   B O     1 
HETATM 20156 O  O     . HOH   AA 11 .    ? -29.230 26.837  119.808 1.00 47.66 ? 2059 HOH   B O     1 
HETATM 20157 O  O     . HOH   AA 11 .    ? 2.556   49.176  98.560  1.00 23.44 ? 2060 HOH   B O     1 
HETATM 20158 O  O     . HOH   AA 11 .    ? -5.425  23.302  80.170  1.00 22.53 ? 2061 HOH   B O     1 
HETATM 20159 O  O     . HOH   AA 11 .    ? 18.521  48.178  89.535  1.00 20.65 ? 2062 HOH   B O     1 
HETATM 20160 O  O     . HOH   AA 11 .    ? 1.382   38.839  105.040 1.00 34.46 ? 2063 HOH   B O     1 
HETATM 20161 O  O     . HOH   AA 11 .    ? 2.316   30.168  54.302  1.00 36.16 ? 2064 HOH   B O     1 
HETATM 20162 O  O     . HOH   AA 11 .    ? 5.609   12.251  77.328  1.00 30.56 ? 2065 HOH   B O     1 
HETATM 20163 O  O     . HOH   AA 11 .    ? 33.610  12.042  87.670  1.00 40.12 ? 2066 HOH   B O     1 
HETATM 20164 O  O     . HOH   AA 11 .    ? -19.438 -2.275  105.089 1.00 40.62 ? 2067 HOH   B O     1 
HETATM 20165 O  O     . HOH   AA 11 .    ? 28.297  44.611  89.393  1.00 24.94 ? 2068 HOH   B O     1 
HETATM 20166 O  O     . HOH   AA 11 .    ? -9.634  1.082   112.035 1.00 27.45 ? 2069 HOH   B O     1 
HETATM 20167 O  O     . HOH   AA 11 .    ? 7.673   66.053  68.048  1.00 32.62 ? 2070 HOH   B O     1 
HETATM 20168 O  O     . HOH   AA 11 .    ? 22.437  62.026  82.832  1.00 35.76 ? 2071 HOH   B O     1 
HETATM 20169 O  O     . HOH   AA 11 .    ? 6.024   52.064  93.333  1.00 39.79 ? 2072 HOH   B O     1 
HETATM 20170 O  O     . HOH   AA 11 .    ? -23.426 3.643   101.121 1.00 39.56 ? 2073 HOH   B O     1 
HETATM 20171 O  O     . HOH   AA 11 .    ? -15.375 10.600  89.340  1.00 22.33 ? 2074 HOH   B O     1 
HETATM 20172 O  O     . HOH   AA 11 .    ? -3.933  46.363  132.526 1.00 43.46 ? 2075 HOH   B O     1 
HETATM 20173 O  O     . HOH   AA 11 .    ? -8.576  31.849  86.395  1.00 20.59 ? 2076 HOH   B O     1 
HETATM 20174 O  O     . HOH   AA 11 .    ? 35.855  31.700  103.378 1.00 33.57 ? 2077 HOH   B O     1 
HETATM 20175 O  O     . HOH   AA 11 .    ? 8.116   32.024  93.382  1.00 26.45 ? 2078 HOH   B O     1 
HETATM 20176 O  O     . HOH   AA 11 .    ? 1.355   22.746  63.144  1.00 26.78 ? 2079 HOH   B O     1 
HETATM 20177 O  O     . HOH   AA 11 .    ? 30.880  67.478  82.015  1.00 32.12 ? 2080 HOH   B O     1 
HETATM 20178 O  O     . HOH   AA 11 .    ? 17.160  8.134   89.409  1.00 37.89 ? 2081 HOH   B O     1 
HETATM 20179 O  O     . HOH   AA 11 .    ? -0.692  -7.484  99.108  1.00 29.73 ? 2082 HOH   B O     1 
HETATM 20180 O  O     . HOH   AA 11 .    ? 19.036  58.633  81.844  1.00 26.11 ? 2083 HOH   B O     1 
HETATM 20181 O  O     . HOH   AA 11 .    ? -11.917 22.258  85.102  1.00 24.95 ? 2084 HOH   B O     1 
HETATM 20182 O  O     . HOH   AA 11 .    ? -2.646  20.893  110.323 1.00 35.57 ? 2085 HOH   B O     1 
HETATM 20183 O  O     . HOH   AA 11 .    ? 11.321  26.709  51.646  1.00 30.91 ? 2086 HOH   B O     1 
HETATM 20184 O  O     . HOH   AA 11 .    ? 4.724   56.424  74.588  1.00 17.14 ? 2087 HOH   B O     1 
HETATM 20185 O  O     . HOH   AA 11 .    ? -4.624  56.746  126.601 1.00 38.60 ? 2088 HOH   B O     1 
HETATM 20186 O  O     . HOH   AA 11 .    ? 21.759  55.357  104.947 1.00 41.96 ? 2089 HOH   B O     1 
HETATM 20187 O  O     . HOH   AA 11 .    ? 11.388  18.631  97.332  1.00 30.61 ? 2090 HOH   B O     1 
HETATM 20188 O  O     . HOH   AA 11 .    ? 33.363  23.406  64.183  1.00 33.27 ? 2091 HOH   B O     1 
HETATM 20189 O  O     . HOH   AA 11 .    ? 24.090  67.847  80.406  1.00 34.86 ? 2092 HOH   B O     1 
HETATM 20190 O  O     . HOH   AA 11 .    ? 11.534  18.370  94.466  1.00 33.74 ? 2093 HOH   B O     1 
HETATM 20191 O  O     . HOH   AA 11 .    ? 22.891  73.129  81.223  1.00 30.51 ? 2094 HOH   B O     1 
HETATM 20192 O  O     . HOH   AA 11 .    ? 29.311  32.687  102.844 1.00 27.01 ? 2095 HOH   B O     1 
HETATM 20193 O  O     . HOH   AA 11 .    ? -21.401 1.871   120.489 1.00 38.98 ? 2096 HOH   B O     1 
HETATM 20194 O  O     . HOH   AA 11 .    ? -5.563  46.771  83.751  1.00 26.99 ? 2097 HOH   B O     1 
HETATM 20195 O  O     . HOH   AA 11 .    ? 1.466   56.422  114.301 1.00 42.10 ? 2098 HOH   B O     1 
HETATM 20196 O  O     . HOH   AA 11 .    ? 2.893   45.185  67.408  1.00 16.85 ? 2099 HOH   B O     1 
HETATM 20197 O  O     . HOH   AA 11 .    ? 33.066  37.350  81.983  1.00 41.67 ? 2100 HOH   B O     1 
HETATM 20198 O  O     . HOH   AA 11 .    ? 22.147  15.285  80.684  1.00 23.19 ? 2101 HOH   B O     1 
HETATM 20199 O  O     . HOH   AA 11 .    ? 28.153  49.287  97.401  1.00 35.57 ? 2102 HOH   B O     1 
HETATM 20200 O  O     . HOH   AA 11 .    ? 26.320  13.281  87.612  1.00 29.10 ? 2103 HOH   B O     1 
HETATM 20201 O  O     . HOH   AA 11 .    ? 2.433   19.136  76.863  1.00 29.27 ? 2104 HOH   B O     1 
HETATM 20202 O  O     . HOH   AA 11 .    ? 12.583  62.381  84.089  1.00 33.03 ? 2105 HOH   B O     1 
HETATM 20203 O  O     . HOH   AA 11 .    ? -4.493  44.826  108.265 1.00 31.92 ? 2106 HOH   B O     1 
HETATM 20204 O  O     . HOH   AA 11 .    ? 25.497  54.077  54.185  1.00 44.37 ? 2107 HOH   B O     1 
HETATM 20205 O  O     . HOH   AA 11 .    ? 3.194   31.544  97.846  1.00 26.60 ? 2108 HOH   B O     1 
HETATM 20206 O  O     . HOH   AA 11 .    ? -6.093  35.846  92.073  1.00 29.31 ? 2109 HOH   B O     1 
HETATM 20207 O  O     . HOH   AA 11 .    ? -2.352  -7.162  110.024 1.00 26.93 ? 2110 HOH   B O     1 
HETATM 20208 O  O     . HOH   AA 11 .    ? -1.192  15.120  130.466 1.00 37.45 ? 2111 HOH   B O     1 
HETATM 20209 O  O     . HOH   AA 11 .    ? 24.987  53.576  68.146  1.00 23.75 ? 2112 HOH   B O     1 
HETATM 20210 O  O     . HOH   AA 11 .    ? -4.224  31.034  94.319  1.00 29.17 ? 2113 HOH   B O     1 
HETATM 20211 O  O     . HOH   AA 11 .    ? 15.459  49.716  78.555  1.00 26.27 ? 2114 HOH   B O     1 
HETATM 20212 O  O     . HOH   AA 11 .    ? -2.821  64.674  82.932  1.00 17.83 ? 2115 HOH   B O     1 
HETATM 20213 O  O     . HOH   AA 11 .    ? 36.338  17.100  76.996  1.00 42.19 ? 2116 HOH   B O     1 
HETATM 20214 O  O     . HOH   AA 11 .    ? -16.380 22.230  81.791  1.00 26.26 ? 2117 HOH   B O     1 
HETATM 20215 O  O     . HOH   AA 11 .    ? -2.567  30.694  70.207  1.00 18.81 ? 2118 HOH   B O     1 
HETATM 20216 O  O     . HOH   AA 11 .    ? -3.407  52.616  82.108  1.00 27.13 ? 2119 HOH   B O     1 
HETATM 20217 O  O     . HOH   AA 11 .    ? -7.982  48.385  76.194  1.00 30.88 ? 2120 HOH   B O     1 
HETATM 20218 O  O     . HOH   AA 11 .    ? 31.590  35.304  74.445  1.00 38.36 ? 2121 HOH   B O     1 
HETATM 20219 O  O     . HOH   AA 11 .    ? 29.856  9.174   85.894  1.00 36.65 ? 2122 HOH   B O     1 
HETATM 20220 O  O     . HOH   AA 11 .    ? 4.902   58.008  68.433  1.00 24.00 ? 2123 HOH   B O     1 
HETATM 20221 O  O     . HOH   AA 11 .    ? -2.112  57.791  74.781  1.00 18.58 ? 2124 HOH   B O     1 
HETATM 20222 O  O     . HOH   AA 11 .    ? -10.249 18.615  130.643 1.00 36.60 ? 2125 HOH   B O     1 
HETATM 20223 O  O     . HOH   AA 11 .    ? -5.336  50.943  83.159  1.00 40.23 ? 2126 HOH   B O     1 
HETATM 20224 O  O     A HOH   AA 11 .    ? 0.441   63.569  84.241  0.51 23.77 ? 2127 HOH   B O     1 
HETATM 20225 O  O     . HOH   AA 11 .    ? 16.824  51.664  59.510  1.00 26.19 ? 2128 HOH   B O     1 
HETATM 20226 O  O     . HOH   AA 11 .    ? 24.991  18.275  99.804  1.00 32.87 ? 2129 HOH   B O     1 
HETATM 20227 O  O     . HOH   AA 11 .    ? 9.811   18.691  100.664 1.00 23.75 ? 2130 HOH   B O     1 
HETATM 20228 O  O     . HOH   AA 11 .    ? 5.236   24.336  118.937 1.00 40.54 ? 2131 HOH   B O     1 
HETATM 20229 O  O     . HOH   AA 11 .    ? -1.869  -0.633  108.567 1.00 29.41 ? 2132 HOH   B O     1 
HETATM 20230 O  O     . HOH   AA 11 .    ? 17.842  76.676  63.238  1.00 31.92 ? 2133 HOH   B O     1 
HETATM 20231 O  O     . HOH   AA 11 .    ? 18.426  14.844  104.808 1.00 36.37 ? 2134 HOH   B O     1 
HETATM 20232 O  O     . HOH   AA 11 .    ? -7.427  13.522  94.060  1.00 18.55 ? 2135 HOH   B O     1 
HETATM 20233 O  O     . HOH   AA 11 .    ? 2.896   44.439  58.003  1.00 30.60 ? 2136 HOH   B O     1 
HETATM 20234 O  O     . HOH   AA 11 .    ? 29.455  41.907  79.641  1.00 26.84 ? 2137 HOH   B O     1 
HETATM 20235 O  O     . HOH   AA 11 .    ? -4.204  52.904  79.566  1.00 34.46 ? 2138 HOH   B O     1 
HETATM 20236 O  O     . HOH   AA 11 .    ? 20.239  19.278  59.864  1.00 25.39 ? 2139 HOH   B O     1 
HETATM 20237 O  O     . HOH   AA 11 .    ? 14.492  9.406   93.181  1.00 22.98 ? 2140 HOH   B O     1 
HETATM 20238 O  O     . HOH   AA 11 .    ? 14.163  34.801  111.493 1.00 41.00 ? 2141 HOH   B O     1 
HETATM 20239 O  O     . HOH   AA 11 .    ? 15.860  10.565  95.174  1.00 24.59 ? 2142 HOH   B O     1 
HETATM 20240 O  O     . HOH   AA 11 .    ? 18.759  35.770  112.436 1.00 21.88 ? 2143 HOH   B O     1 
HETATM 20241 O  O     . HOH   AA 11 .    ? 22.924  51.528  64.727  1.00 21.25 ? 2144 HOH   B O     1 
HETATM 20242 O  O     . HOH   AA 11 .    ? 4.548   -3.463  94.718  1.00 38.33 ? 2145 HOH   B O     1 
HETATM 20243 O  O     . HOH   AA 11 .    ? -22.963 22.234  101.468 1.00 33.42 ? 2146 HOH   B O     1 
HETATM 20244 O  O     . HOH   AA 11 .    ? 28.265  31.083  80.301  1.00 22.93 ? 2147 HOH   B O     1 
HETATM 20245 O  O     . HOH   AA 11 .    ? 4.650   0.539   86.295  1.00 32.70 ? 2148 HOH   B O     1 
HETATM 20246 O  O     . HOH   AA 11 .    ? 18.016  76.118  78.336  1.00 35.46 ? 2149 HOH   B O     1 
HETATM 20247 O  O     . HOH   AA 11 .    ? 35.042  32.491  54.652  1.00 29.41 ? 2150 HOH   B O     1 
HETATM 20248 O  O     . HOH   AA 11 .    ? -0.653  3.861   130.227 1.00 41.06 ? 2151 HOH   B O     1 
HETATM 20249 O  O     . HOH   AA 11 .    ? 5.681   70.479  60.556  1.00 39.33 ? 2152 HOH   B O     1 
HETATM 20250 O  O     . HOH   AA 11 .    ? 20.111  20.683  108.816 1.00 21.72 ? 2153 HOH   B O     1 
HETATM 20251 O  O     . HOH   AA 11 .    ? -13.514 49.255  110.120 1.00 32.60 ? 2154 HOH   B O     1 
HETATM 20252 O  O     . HOH   AA 11 .    ? -12.817 31.756  83.230  1.00 36.33 ? 2155 HOH   B O     1 
HETATM 20253 O  O     . HOH   AA 11 .    ? 10.544  37.851  77.194  1.00 23.60 ? 2156 HOH   B O     1 
HETATM 20254 O  O     . HOH   AA 11 .    ? 23.669  23.229  106.486 1.00 37.22 ? 2157 HOH   B O     1 
HETATM 20255 O  O     . HOH   AA 11 .    ? 20.611  22.196  60.676  1.00 17.20 ? 2158 HOH   B O     1 
HETATM 20256 O  O     . HOH   AA 11 .    ? 16.941  47.270  54.304  1.00 32.37 ? 2159 HOH   B O     1 
HETATM 20257 O  O     . HOH   AA 11 .    ? 7.225   66.496  86.066  1.00 33.46 ? 2160 HOH   B O     1 
HETATM 20258 O  O     . HOH   AA 11 .    ? 9.060   45.932  131.659 1.00 42.18 ? 2161 HOH   B O     1 
HETATM 20259 O  O     . HOH   AA 11 .    ? -28.970 23.623  89.347  1.00 45.50 ? 2162 HOH   B O     1 
HETATM 20260 O  O     . HOH   AA 11 .    ? 22.593  12.265  79.405  1.00 33.02 ? 2163 HOH   B O     1 
HETATM 20261 O  O     . HOH   AA 11 .    ? -18.156 6.520   95.205  1.00 37.95 ? 2164 HOH   B O     1 
HETATM 20262 O  O     . HOH   AA 11 .    ? 12.200  77.769  63.792  1.00 33.97 ? 2165 HOH   B O     1 
HETATM 20263 O  O     . HOH   AA 11 .    ? 32.903  47.385  87.101  1.00 42.12 ? 2166 HOH   B O     1 
HETATM 20264 O  O     . HOH   AA 11 .    ? -19.540 29.141  87.716  1.00 32.03 ? 2167 HOH   B O     1 
HETATM 20265 O  O     . HOH   AA 11 .    ? 16.231  14.281  106.428 1.00 27.63 ? 2168 HOH   B O     1 
HETATM 20266 O  O     . HOH   AA 11 .    ? 16.136  56.159  63.415  1.00 25.28 ? 2169 HOH   B O     1 
HETATM 20267 O  O     . HOH   AA 11 .    ? 7.632   54.631  64.079  1.00 28.38 ? 2170 HOH   B O     1 
HETATM 20268 O  O     . HOH   AA 11 .    ? -5.031  -3.494  91.288  1.00 30.17 ? 2171 HOH   B O     1 
HETATM 20269 O  O     . HOH   AA 11 .    ? 12.544  58.250  93.492  1.00 33.20 ? 2172 HOH   B O     1 
HETATM 20270 O  O     . HOH   AA 11 .    ? -7.819  24.274  124.687 1.00 34.94 ? 2173 HOH   B O     1 
HETATM 20271 O  O     . HOH   AA 11 .    ? 14.928  58.724  54.135  1.00 48.71 ? 2174 HOH   B O     1 
HETATM 20272 O  O     . HOH   AA 11 .    ? 4.358   17.490  127.278 1.00 35.37 ? 2175 HOH   B O     1 
HETATM 20273 O  O     . HOH   AA 11 .    ? -12.294 8.274   126.523 1.00 33.18 ? 2176 HOH   B O     1 
HETATM 20274 O  O     . HOH   AA 11 .    ? 4.010   67.000  59.824  1.00 43.75 ? 2177 HOH   B O     1 
HETATM 20275 O  O     . HOH   AA 11 .    ? 2.947   54.570  66.377  1.00 33.24 ? 2178 HOH   B O     1 
HETATM 20276 O  O     . HOH   AA 11 .    ? 23.829  17.450  82.262  1.00 24.70 ? 2179 HOH   B O     1 
HETATM 20277 O  O     . HOH   AA 11 .    ? -1.066  37.992  75.901  1.00 28.97 ? 2180 HOH   B O     1 
HETATM 20278 O  O     . HOH   AA 11 .    ? 14.054  75.928  62.478  1.00 27.29 ? 2181 HOH   B O     1 
HETATM 20279 O  O     . HOH   AA 11 .    ? -7.594  10.838  112.360 1.00 23.42 ? 2182 HOH   B O     1 
HETATM 20280 O  O     . HOH   AA 11 .    ? -5.797  15.828  93.960  1.00 19.01 ? 2183 HOH   B O     1 
HETATM 20281 O  O     . HOH   AA 11 .    ? -6.221  9.372   81.581  1.00 34.83 ? 2184 HOH   B O     1 
HETATM 20282 O  O     . HOH   AA 11 .    ? -24.337 10.881  126.275 1.00 44.63 ? 2185 HOH   B O     1 
HETATM 20283 O  O     . HOH   AA 11 .    ? 24.876  63.435  54.078  1.00 33.00 ? 2186 HOH   B O     1 
HETATM 20284 O  O     . HOH   AA 11 .    ? 28.885  22.903  71.933  1.00 31.36 ? 2187 HOH   B O     1 
HETATM 20285 O  O     . HOH   AA 11 .    ? 4.644   36.318  103.265 1.00 42.87 ? 2188 HOH   B O     1 
HETATM 20286 O  O     . HOH   AA 11 .    ? 13.402  19.051  87.128  1.00 24.23 ? 2189 HOH   B O     1 
HETATM 20287 O  O     . HOH   AA 11 .    ? 29.096  65.606  62.054  1.00 31.55 ? 2190 HOH   B O     1 
HETATM 20288 O  O     . HOH   AA 11 .    ? -16.017 4.912   92.127  1.00 41.83 ? 2191 HOH   B O     1 
HETATM 20289 O  O     . HOH   AA 11 .    ? 3.223   54.058  57.237  1.00 41.04 ? 2192 HOH   B O     1 
HETATM 20290 O  O     . HOH   AA 11 .    ? -9.384  14.557  114.157 1.00 31.65 ? 2193 HOH   B O     1 
HETATM 20291 O  O     . HOH   AA 11 .    ? -14.167 44.789  112.894 1.00 39.65 ? 2194 HOH   B O     1 
HETATM 20292 O  O     . HOH   AA 11 .    ? 4.990   43.266  55.510  1.00 29.80 ? 2195 HOH   B O     1 
HETATM 20293 O  O     . HOH   AA 11 .    ? 19.175  54.785  103.711 1.00 25.36 ? 2196 HOH   B O     1 
HETATM 20294 O  O     . HOH   AA 11 .    ? 30.540  47.087  60.539  1.00 39.36 ? 2197 HOH   B O     1 
HETATM 20295 O  O     . HOH   AA 11 .    ? 8.446   16.271  92.325  1.00 31.85 ? 2198 HOH   B O     1 
HETATM 20296 O  O     . HOH   AA 11 .    ? 16.243  52.310  79.220  1.00 22.22 ? 2199 HOH   B O     1 
HETATM 20297 O  O     . HOH   AA 11 .    ? 42.336  32.442  96.303  1.00 39.16 ? 2200 HOH   B O     1 
HETATM 20298 O  O     . HOH   AA 11 .    ? 4.271   77.434  62.651  1.00 32.92 ? 2201 HOH   B O     1 
HETATM 20299 O  O     . HOH   AA 11 .    ? 8.597   -0.551  98.082  1.00 40.46 ? 2202 HOH   B O     1 
HETATM 20300 O  O     . HOH   AA 11 .    ? 17.627  44.420  111.455 1.00 33.56 ? 2203 HOH   B O     1 
HETATM 20301 O  O     . HOH   AA 11 .    ? 20.748  30.868  112.714 1.00 36.35 ? 2204 HOH   B O     1 
HETATM 20302 O  O     . HOH   AA 11 .    ? -12.667 35.291  118.858 1.00 47.49 ? 2205 HOH   B O     1 
HETATM 20303 O  O     . HOH   AA 11 .    ? 29.145  35.769  78.122  1.00 34.26 ? 2206 HOH   B O     1 
HETATM 20304 O  O     . HOH   AA 11 .    ? 12.748  29.675  50.078  1.00 27.22 ? 2207 HOH   B O     1 
HETATM 20305 O  O     . HOH   AA 11 .    ? 30.880  20.155  55.897  1.00 29.64 ? 2208 HOH   B O     1 
HETATM 20306 O  O     . HOH   AA 11 .    ? 5.794   -3.109  99.208  1.00 41.81 ? 2209 HOH   B O     1 
HETATM 20307 O  O     . HOH   AA 11 .    ? 37.133  37.728  88.586  1.00 20.60 ? 2210 HOH   B O     1 
HETATM 20308 O  O     . HOH   AA 11 .    ? -29.038 17.962  116.965 1.00 39.39 ? 2211 HOH   B O     1 
HETATM 20309 O  O     . HOH   AA 11 .    ? 35.646  33.306  80.268  1.00 34.17 ? 2212 HOH   B O     1 
HETATM 20310 O  O     . HOH   AA 11 .    ? 25.613  75.553  76.434  1.00 31.15 ? 2213 HOH   B O     1 
HETATM 20311 O  O     . HOH   AA 11 .    ? -6.754  39.173  66.994  1.00 31.09 ? 2214 HOH   B O     1 
HETATM 20312 O  O     . HOH   AA 11 .    ? 23.465  24.800  47.444  1.00 31.35 ? 2215 HOH   B O     1 
HETATM 20313 O  O     . HOH   AA 11 .    ? 35.474  31.632  57.939  1.00 30.34 ? 2216 HOH   B O     1 
HETATM 20314 O  O     . HOH   AA 11 .    ? 11.936  23.082  112.851 1.00 38.46 ? 2217 HOH   B O     1 
HETATM 20315 O  O     . HOH   AA 11 .    ? -8.196  38.161  69.945  1.00 41.19 ? 2218 HOH   B O     1 
HETATM 20316 O  O     . HOH   AA 11 .    ? -23.754 23.801  83.979  1.00 39.76 ? 2219 HOH   B O     1 
HETATM 20317 O  O     . HOH   AA 11 .    ? 7.883   28.937  80.773  1.00 27.11 ? 2220 HOH   B O     1 
HETATM 20318 O  O     . HOH   AA 11 .    ? 16.037  8.400   110.414 1.00 35.55 ? 2221 HOH   B O     1 
HETATM 20319 O  O     . HOH   AA 11 .    ? -34.548 14.044  110.508 1.00 43.64 ? 2222 HOH   B O     1 
HETATM 20320 O  O     . HOH   AA 11 .    ? -9.212  8.375   81.613  1.00 39.68 ? 2223 HOH   B O     1 
HETATM 20321 O  O     . HOH   AA 11 .    ? 16.595  82.127  79.316  1.00 50.00 ? 2224 HOH   B O     1 
HETATM 20322 O  O     . HOH   AA 11 .    ? 14.861  57.105  71.670  1.00 23.09 ? 2225 HOH   B O     1 
HETATM 20323 O  O     . HOH   AA 11 .    ? -29.556 12.141  86.926  1.00 47.44 ? 2226 HOH   B O     1 
HETATM 20324 O  O     . HOH   AA 11 .    ? 24.954  79.470  66.768  1.00 45.55 ? 2227 HOH   B O     1 
HETATM 20325 O  O     . HOH   AA 11 .    ? -14.924 19.668  82.057  1.00 26.92 ? 2228 HOH   B O     1 
HETATM 20326 O  O     . HOH   AA 11 .    ? 28.234  34.132  80.055  1.00 35.14 ? 2229 HOH   B O     1 
HETATM 20327 O  O     . HOH   AA 11 .    ? 26.366  52.172  55.264  1.00 35.44 ? 2230 HOH   B O     1 
HETATM 20328 O  O     . HOH   AA 11 .    ? 1.198   42.294  97.821  1.00 33.53 ? 2231 HOH   B O     1 
HETATM 20329 O  O     . HOH   AA 11 .    ? -0.389  45.548  77.237  1.00 34.20 ? 2232 HOH   B O     1 
HETATM 20330 O  O     . HOH   AA 11 .    ? 2.521   4.056   84.205  1.00 35.74 ? 2233 HOH   B O     1 
HETATM 20331 O  O     . HOH   AA 11 .    ? 8.932   30.980  88.136  1.00 32.28 ? 2234 HOH   B O     1 
HETATM 20332 O  O     . HOH   AA 11 .    ? 6.212   21.863  88.854  1.00 37.17 ? 2235 HOH   B O     1 
HETATM 20333 O  O     . HOH   AA 11 .    ? -4.292  27.013  99.289  1.00 26.84 ? 2236 HOH   B O     1 
HETATM 20334 O  O     . HOH   AA 11 .    ? 26.670  41.421  80.835  1.00 26.63 ? 2237 HOH   B O     1 
HETATM 20335 O  O     . HOH   AA 11 .    ? 27.138  56.874  80.825  1.00 31.73 ? 2238 HOH   B O     1 
HETATM 20336 O  O     . HOH   AA 11 .    ? -2.546  42.464  73.830  1.00 31.13 ? 2239 HOH   B O     1 
HETATM 20337 O  O     . HOH   AA 11 .    ? 18.733  66.180  55.420  1.00 34.29 ? 2240 HOH   B O     1 
HETATM 20338 O  O     . HOH   AA 11 .    ? 26.427  13.379  90.662  1.00 41.35 ? 2241 HOH   B O     1 
HETATM 20339 O  O     . HOH   AA 11 .    ? 32.847  20.421  72.016  1.00 37.08 ? 2242 HOH   B O     1 
HETATM 20340 O  O     . HOH   AA 11 .    ? -30.721 6.165   99.390  1.00 44.15 ? 2243 HOH   B O     1 
HETATM 20341 O  O     . HOH   AA 11 .    ? 28.696  59.499  83.881  1.00 43.52 ? 2244 HOH   B O     1 
HETATM 20342 O  O     . HOH   AA 11 .    ? -0.729  44.183  55.514  1.00 32.26 ? 2245 HOH   B O     1 
HETATM 20343 O  O     . HOH   AA 11 .    ? -27.112 13.082  99.219  1.00 41.90 ? 2246 HOH   B O     1 
HETATM 20344 O  O     . HOH   AA 11 .    ? 32.120  45.515  61.284  1.00 40.39 ? 2247 HOH   B O     1 
HETATM 20345 O  O     . HOH   AA 11 .    ? -0.980  44.565  75.048  1.00 30.53 ? 2248 HOH   B O     1 
HETATM 20346 O  O     . HOH   AA 11 .    ? 35.597  20.187  85.161  1.00 35.52 ? 2249 HOH   B O     1 
HETATM 20347 O  O     . HOH   AA 11 .    ? 17.085  25.058  52.000  1.00 28.55 ? 2250 HOH   B O     1 
HETATM 20348 O  O     . HOH   AA 11 .    ? 23.319  8.401   73.198  1.00 39.87 ? 2251 HOH   B O     1 
HETATM 20349 O  O     . HOH   AA 11 .    ? -5.486  37.785  85.555  1.00 29.59 ? 2252 HOH   B O     1 
HETATM 20350 O  O     . HOH   AA 11 .    ? 23.991  21.067  106.822 1.00 35.73 ? 2253 HOH   B O     1 
HETATM 20351 O  O     . HOH   AA 11 .    ? -19.598 24.578  112.091 1.00 36.43 ? 2254 HOH   B O     1 
HETATM 20352 O  O     . HOH   AA 11 .    ? -14.454 27.166  100.983 1.00 33.83 ? 2255 HOH   B O     1 
HETATM 20353 O  O     . HOH   AA 11 .    ? -2.758  23.148  79.019  1.00 24.65 ? 2256 HOH   B O     1 
HETATM 20354 O  O     . HOH   AA 11 .    ? 6.472   25.015  83.307  1.00 26.56 ? 2257 HOH   B O     1 
HETATM 20355 O  O     . HOH   AA 11 .    ? -19.425 12.809  80.896  1.00 41.28 ? 2258 HOH   B O     1 
HETATM 20356 O  O     . HOH   AA 11 .    ? -4.013  -4.411  93.760  1.00 38.21 ? 2259 HOH   B O     1 
HETATM 20357 O  O     . HOH   AA 11 .    ? 34.841  6.549   81.336  1.00 39.52 ? 2260 HOH   B O     1 
HETATM 20358 O  O     . HOH   AA 11 .    ? -2.285  60.481  123.549 1.00 38.57 ? 2261 HOH   B O     1 
HETATM 20359 O  O     . HOH   AA 11 .    ? 9.203   23.974  121.553 1.00 37.41 ? 2262 HOH   B O     1 
HETATM 20360 O  O     . HOH   AA 11 .    ? 28.443  75.861  72.346  1.00 41.01 ? 2263 HOH   B O     1 
HETATM 20361 O  O     . HOH   AA 11 .    ? -2.568  -5.232  89.246  1.00 34.63 ? 2264 HOH   B O     1 
HETATM 20362 O  O     . HOH   AA 11 .    ? 15.127  29.278  48.863  1.00 29.85 ? 2265 HOH   B O     1 
HETATM 20363 O  O     . HOH   AA 11 .    ? -21.137 8.692   120.206 1.00 39.92 ? 2266 HOH   B O     1 
HETATM 20364 O  O     . HOH   AA 11 .    ? -1.059  23.117  96.520  1.00 29.74 ? 2267 HOH   B O     1 
HETATM 20365 O  O     . HOH   AA 11 .    ? 22.920  67.874  59.304  1.00 28.82 ? 2268 HOH   B O     1 
HETATM 20366 O  O     . HOH   AA 11 .    ? 24.137  45.548  49.105  1.00 43.57 ? 2269 HOH   B O     1 
HETATM 20367 O  O     . HOH   AA 11 .    ? 35.486  32.352  61.140  1.00 41.47 ? 2270 HOH   B O     1 
HETATM 20368 O  O     . HOH   AA 11 .    ? -21.987 8.231   85.416  1.00 39.27 ? 2271 HOH   B O     1 
HETATM 20369 O  O     . HOH   AA 11 .    ? 26.521  47.391  102.337 1.00 37.66 ? 2272 HOH   B O     1 
HETATM 20370 O  O     . HOH   AA 11 .    ? 39.521  29.550  80.652  1.00 34.73 ? 2273 HOH   B O     1 
HETATM 20371 O  O     . HOH   AA 11 .    ? -2.739  69.707  75.060  1.00 34.08 ? 2274 HOH   B O     1 
HETATM 20372 O  O     . HOH   AA 11 .    ? 0.999   56.010  65.286  1.00 38.94 ? 2275 HOH   B O     1 
HETATM 20373 O  O     . HOH   AA 11 .    ? 10.318  51.546  108.142 1.00 47.04 ? 2276 HOH   B O     1 
HETATM 20374 O  O     . HOH   AA 11 .    ? 28.525  41.888  52.926  1.00 33.69 ? 2277 HOH   B O     1 
HETATM 20375 O  O     . HOH   AA 11 .    ? -3.109  -2.312  84.559  1.00 44.22 ? 2278 HOH   B O     1 
HETATM 20376 O  O     . HOH   AA 11 .    ? -1.646  -9.310  108.581 1.00 33.14 ? 2279 HOH   B O     1 
HETATM 20377 O  O     . HOH   AA 11 .    ? -4.771  40.710  98.075  1.00 38.07 ? 2280 HOH   B O     1 
HETATM 20378 O  O     . HOH   AA 11 .    ? 18.047  46.602  111.375 1.00 35.39 ? 2281 HOH   B O     1 
HETATM 20379 O  O     . HOH   AA 11 .    ? 6.136   17.720  95.954  1.00 31.83 ? 2282 HOH   B O     1 
HETATM 20380 O  O     . HOH   AA 11 .    ? 17.719  75.079  81.047  1.00 37.66 ? 2283 HOH   B O     1 
HETATM 20381 O  O     . HOH   AA 11 .    ? -27.753 14.478  85.712  1.00 41.51 ? 2284 HOH   B O     1 
HETATM 20382 O  O     . HOH   AA 11 .    ? 2.739   57.677  70.252  1.00 27.56 ? 2285 HOH   B O     1 
HETATM 20383 O  O     . HOH   AA 11 .    ? -16.797 50.043  116.325 1.00 42.76 ? 2286 HOH   B O     1 
HETATM 20384 O  O     . HOH   AA 11 .    ? 11.384  43.952  50.676  1.00 37.13 ? 2287 HOH   B O     1 
HETATM 20385 O  O     . HOH   AA 11 .    ? 27.733  71.903  80.585  1.00 41.84 ? 2288 HOH   B O     1 
HETATM 20386 O  O     . HOH   AA 11 .    ? -16.317 8.195   127.109 1.00 43.98 ? 2289 HOH   B O     1 
HETATM 20387 O  O     . HOH   AA 11 .    ? 10.703  10.427  122.737 1.00 31.19 ? 2290 HOH   B O     1 
HETATM 20388 O  O     . HOH   AA 11 .    ? 7.362   33.926  50.929  1.00 31.93 ? 2291 HOH   B O     1 
HETATM 20389 O  O     . HOH   AA 11 .    ? 7.698   24.191  88.897  1.00 40.05 ? 2292 HOH   B O     1 
HETATM 20390 O  O     . HOH   AA 11 .    ? 12.461  40.116  131.883 1.00 45.16 ? 2293 HOH   B O     1 
HETATM 20391 O  O     . HOH   AA 11 .    ? -1.424  37.916  73.133  1.00 19.62 ? 2294 HOH   B O     1 
HETATM 20392 O  O     . HOH   AA 11 .    ? 13.007  35.341  109.029 1.00 34.91 ? 2295 HOH   B O     1 
HETATM 20393 O  O     . HOH   AA 11 .    ? -6.107  39.984  85.644  1.00 33.84 ? 2296 HOH   B O     1 
HETATM 20394 O  O     . HOH   AA 11 .    ? 12.565  46.843  110.924 1.00 37.51 ? 2297 HOH   B O     1 
HETATM 20395 O  O     . HOH   AA 11 .    ? 39.727  38.419  88.387  1.00 30.60 ? 2298 HOH   B O     1 
HETATM 20396 O  O     . HOH   AA 11 .    ? 16.000  35.633  113.007 1.00 34.10 ? 2299 HOH   B O     1 
HETATM 20397 O  O     . HOH   AA 11 .    ? 6.050   17.625  114.508 1.00 28.55 ? 2300 HOH   B O     1 
HETATM 20398 O  O     . HOH   AA 11 .    ? 16.735  56.404  94.435  1.00 34.03 ? 2301 HOH   B O     1 
HETATM 20399 O  O     . HOH   AA 11 .    ? 34.269  38.614  66.430  1.00 41.11 ? 2302 HOH   B O     1 
HETATM 20400 O  O     . HOH   AA 11 .    ? 4.364   29.925  81.566  1.00 25.58 ? 2303 HOH   B O     1 
HETATM 20401 O  O     . HOH   AA 11 .    ? 9.248   0.891   118.957 1.00 36.34 ? 2304 HOH   B O     1 
HETATM 20402 O  O     . HOH   AA 11 .    ? -6.800  8.518   115.894 1.00 27.94 ? 2305 HOH   B O     1 
HETATM 20403 O  O     . HOH   AA 11 .    ? -22.044 26.157  91.080  1.00 40.49 ? 2306 HOH   B O     1 
HETATM 20404 O  O     . HOH   AA 11 .    ? -7.131  37.284  65.879  1.00 35.69 ? 2307 HOH   B O     1 
HETATM 20405 O  O     . HOH   AA 11 .    ? -33.159 16.832  120.906 1.00 38.34 ? 2308 HOH   B O     1 
HETATM 20406 O  O     . HOH   AA 11 .    ? 21.426  6.528   73.059  1.00 38.86 ? 2309 HOH   B O     1 
HETATM 20407 O  O     . HOH   AA 11 .    ? 18.386  8.706   106.577 1.00 44.00 ? 2310 HOH   B O     1 
HETATM 20408 O  O     . HOH   AA 11 .    ? 40.594  30.431  89.952  1.00 27.38 ? 2311 HOH   B O     1 
HETATM 20409 O  O     . HOH   AA 11 .    ? 21.747  14.896  100.442 1.00 40.51 ? 2312 HOH   B O     1 
HETATM 20410 O  O     . HOH   AA 11 .    ? 19.316  60.588  53.998  1.00 41.25 ? 2313 HOH   B O     1 
HETATM 20411 O  O     . HOH   AA 11 .    ? 30.100  71.259  72.317  1.00 34.48 ? 2314 HOH   B O     1 
HETATM 20412 O  O     . HOH   AA 11 .    ? -7.717  12.640  82.261  1.00 38.40 ? 2315 HOH   B O     1 
HETATM 20413 O  O     . HOH   AA 11 .    ? 4.807   43.587  50.651  1.00 28.37 ? 2316 HOH   B O     1 
HETATM 20414 O  O     . HOH   AA 11 .    ? 38.938  41.025  88.665  1.00 33.19 ? 2317 HOH   B O     1 
HETATM 20415 O  O     . HOH   AA 11 .    ? 33.084  40.519  60.979  1.00 37.05 ? 2318 HOH   B O     1 
HETATM 20416 O  O     . HOH   AA 11 .    ? -0.074  -1.728  94.349  1.00 30.97 ? 2319 HOH   B O     1 
HETATM 20417 O  O     . HOH   AA 11 .    ? 4.927   4.785   78.331  1.00 35.13 ? 2320 HOH   B O     1 
HETATM 20418 O  O     . HOH   AA 11 .    ? -6.717  3.087   84.485  1.00 34.07 ? 2321 HOH   B O     1 
HETATM 20419 O  O     . HOH   AA 11 .    ? -2.598  41.644  77.542  1.00 32.84 ? 2322 HOH   B O     1 
HETATM 20420 O  O     . HOH   AA 11 .    ? 4.393   25.797  128.400 1.00 36.04 ? 2323 HOH   B O     1 
HETATM 20421 O  O     . HOH   AA 11 .    ? 32.905  42.519  66.448  1.00 30.08 ? 2324 HOH   B O     1 
HETATM 20422 O  O     . HOH   AA 11 .    ? 9.576   19.516  98.289  1.00 35.42 ? 2325 HOH   B O     1 
HETATM 20423 O  O     . HOH   AA 11 .    ? 6.213   24.196  124.585 1.00 39.64 ? 2326 HOH   B O     1 
HETATM 20424 O  O     . HOH   AA 11 .    ? 30.690  42.553  55.147  1.00 32.80 ? 2327 HOH   B O     1 
HETATM 20425 O  O     . HOH   AA 11 .    ? 5.343   44.785  53.172  1.00 29.95 ? 2328 HOH   B O     1 
HETATM 20426 O  O     . HOH   AA 11 .    ? 32.855  58.897  66.898  1.00 31.14 ? 2329 HOH   B O     1 
HETATM 20427 O  O     . HOH   AA 11 .    ? -18.524 17.726  77.963  1.00 47.18 ? 2330 HOH   B O     1 
HETATM 20428 O  O     . HOH   AA 11 .    ? 4.903   67.235  63.495  1.00 41.98 ? 2331 HOH   B O     1 
HETATM 20429 O  O     . HOH   AA 11 .    ? -13.366 9.693   128.958 1.00 39.27 ? 2332 HOH   B O     1 
HETATM 20430 O  O     . HOH   AA 11 .    ? -2.598  30.143  96.288  1.00 31.66 ? 2333 HOH   B O     1 
HETATM 20431 O  O     . HOH   AA 11 .    ? 28.578  65.136  59.210  1.00 38.64 ? 2334 HOH   B O     1 
HETATM 20432 O  O     . HOH   AA 11 .    ? 23.664  68.954  61.904  1.00 31.12 ? 2335 HOH   B O     1 
HETATM 20433 O  O     . HOH   AA 11 .    ? 9.519   48.920  108.216 1.00 35.11 ? 2336 HOH   B O     1 
HETATM 20434 O  O     . HOH   AA 11 .    ? 2.412   4.010   81.502  1.00 37.46 ? 2337 HOH   B O     1 
HETATM 20435 O  O     . HOH   AA 11 .    ? -2.400  52.077  100.555 1.00 30.52 ? 2338 HOH   B O     1 
HETATM 20436 O  O     . HOH   AA 11 .    ? 31.944  32.581  74.854  1.00 32.88 ? 2339 HOH   B O     1 
HETATM 20437 O  O     . HOH   AA 11 .    ? 14.069  52.275  63.115  1.00 30.94 ? 2340 HOH   B O     1 
HETATM 20438 O  O     . HOH   AA 11 .    ? 34.228  16.207  61.741  1.00 42.50 ? 2341 HOH   B O     1 
HETATM 20439 O  O     . HOH   AA 11 .    ? -7.244  34.456  66.132  1.00 41.97 ? 2342 HOH   B O     1 
HETATM 20440 O  O     . HOH   AA 11 .    ? 29.757  73.635  72.167  1.00 35.29 ? 2343 HOH   B O     1 
HETATM 20441 O  O     . HOH   AA 11 .    ? 7.291   50.157  89.887  1.00 37.55 ? 2344 HOH   B O     1 
HETATM 20442 O  O     . HOH   AA 11 .    ? 33.440  56.064  66.780  1.00 40.46 ? 2345 HOH   B O     1 
HETATM 20443 O  O     . HOH   AA 11 .    ? 29.714  45.924  84.635  1.00 38.54 ? 2346 HOH   B O     1 
HETATM 20444 O  O     . HOH   AA 11 .    ? 0.558   24.588  98.606  1.00 38.81 ? 2347 HOH   B O     1 
HETATM 20445 O  O     . HOH   AA 11 .    ? -0.511  3.960   80.855  1.00 42.85 ? 2348 HOH   B O     1 
HETATM 20446 O  O     . HOH   AA 11 .    ? 32.939  35.274  71.960  1.00 33.99 ? 2349 HOH   B O     1 
HETATM 20447 O  O     . HOH   AA 11 .    ? -4.284  64.211  69.526  1.00 38.98 ? 2350 HOH   B O     1 
HETATM 20448 O  O     . HOH   AA 11 .    ? 0.331   18.616  71.461  1.00 32.54 ? 2351 HOH   B O     1 
HETATM 20449 O  O     . HOH   AA 11 .    ? -1.922  26.507  64.211  1.00 30.20 ? 2352 HOH   B O     1 
HETATM 20450 O  O     . HOH   AA 11 .    ? -1.343  -4.611  86.265  1.00 44.61 ? 2353 HOH   B O     1 
HETATM 20451 O  O     . HOH   AA 11 .    ? -37.650 16.195  95.408  1.00 50.10 ? 2354 HOH   B O     1 
HETATM 20452 O  O     . HOH   AA 11 .    ? 19.659  45.663  89.355  1.00 16.46 ? 2355 HOH   B O     1 
HETATM 20453 O  O     . HOH   AA 11 .    ? 42.641  35.287  93.035  1.00 33.41 ? 2356 HOH   B O     1 
HETATM 20454 O  O     . HOH   AA 11 .    ? 39.179  34.643  105.346 1.00 44.38 ? 2357 HOH   B O     1 
HETATM 20455 O  O     . HOH   AA 11 .    ? 21.211  18.826  110.509 1.00 36.06 ? 2358 HOH   B O     1 
HETATM 20456 O  O     . HOH   AA 11 .    ? 7.278   19.638  96.800  1.00 40.75 ? 2359 HOH   B O     1 
HETATM 20457 O  O     . HOH   AA 11 .    ? 39.079  26.628  91.839  1.00 39.59 ? 2360 HOH   B O     1 
HETATM 20458 O  O     . HOH   AA 11 .    ? 0.162   19.369  75.147  1.00 40.59 ? 2361 HOH   B O     1 
HETATM 20459 O  O     . HOH   AA 11 .    ? 6.210   60.807  87.496  1.00 36.60 ? 2362 HOH   B O     1 
HETATM 20460 O  O     . HOH   AA 11 .    ? 40.114  45.131  90.048  1.00 33.88 ? 2363 HOH   B O     1 
HETATM 20461 O  O     . HOH   AA 11 .    ? 6.387   13.680  68.671  1.00 38.85 ? 2364 HOH   B O     1 
HETATM 20462 O  O     . HOH   AA 11 .    ? 32.728  20.939  75.822  1.00 38.24 ? 2365 HOH   B O     1 
HETATM 20463 O  O     . HOH   AA 11 .    ? 20.658  68.887  58.067  1.00 38.56 ? 2366 HOH   B O     1 
HETATM 20464 O  O     . HOH   AA 11 .    ? 31.196  26.121  72.581  1.00 32.58 ? 2367 HOH   B O     1 
HETATM 20465 O  O     . HOH   AA 11 .    ? 2.042   24.553  129.087 1.00 41.42 ? 2368 HOH   B O     1 
HETATM 20466 O  O     A HOH   AA 11 .    ? 2.297   62.422  83.162  0.51 21.43 ? 2369 HOH   B O     1 
HETATM 20467 O  O     . HOH   AA 11 .    ? 5.330   80.202  78.607  1.00 41.70 ? 2370 HOH   B O     1 
HETATM 20468 O  O     . HOH   AA 11 .    ? 13.155  23.891  88.793  1.00 38.95 ? 2371 HOH   B O     1 
HETATM 20469 O  O     . HOH   AA 11 .    ? 14.587  55.921  61.483  1.00 38.60 ? 2372 HOH   B O     1 
HETATM 20470 O  O     . HOH   AA 11 .    ? 18.212  7.318   97.715  1.00 34.29 ? 2373 HOH   B O     1 
HETATM 20471 O  O     . HOH   AA 11 .    ? 42.469  32.294  99.017  1.00 41.61 ? 2374 HOH   B O     1 
HETATM 20472 O  O     . HOH   AA 11 .    ? -5.185  52.028  101.496 1.00 39.72 ? 2375 HOH   B O     1 
HETATM 20473 O  O     . HOH   AA 11 .    ? 0.407   4.912   85.502  1.00 31.62 ? 2376 HOH   B O     1 
HETATM 20474 O  O     . HOH   AA 11 .    ? 32.587  28.057  74.129  1.00 39.77 ? 2377 HOH   B O     1 
HETATM 20475 O  O     . HOH   AA 11 .    ? 27.710  51.026  95.273  1.00 33.92 ? 2378 HOH   B O     1 
HETATM 20476 O  O     . HOH   AA 11 .    ? 1.944   43.744  55.446  1.00 34.80 ? 2379 HOH   B O     1 
HETATM 20477 O  O     . HOH   AA 11 .    ? 33.197  16.045  64.438  1.00 39.31 ? 2380 HOH   B O     1 
HETATM 20478 O  O     . HOH   AA 11 .    ? 8.944   58.106  94.489  1.00 36.91 ? 2381 HOH   B O     1 
HETATM 20479 O  O     . HOH   AA 11 .    ? 5.052   31.964  92.187  1.00 37.19 ? 2382 HOH   B O     1 
HETATM 20480 O  O     . HOH   AA 11 .    ? 20.550  58.570  52.540  1.00 39.64 ? 2383 HOH   B O     1 
HETATM 20481 O  O     . HOH   AA 11 .    ? -10.502 30.238  75.688  1.00 35.32 ? 2384 HOH   B O     1 
HETATM 20482 O  O     . HOH   AA 11 .    ? -32.880 18.416  100.486 1.00 42.26 ? 2385 HOH   B O     1 
HETATM 20483 O  O     . HOH   AA 11 .    ? 25.872  17.673  96.579  1.00 38.21 ? 2386 HOH   B O     1 
HETATM 20484 O  O     . HOH   AA 11 .    ? 30.966  59.124  60.219  1.00 34.55 ? 2387 HOH   B O     1 
HETATM 20485 O  O     . HOH   AA 11 .    ? -11.937 30.372  81.037  1.00 39.24 ? 2388 HOH   B O     1 
HETATM 20486 O  O     . HOH   AA 11 .    ? 30.364  31.047  78.582  1.00 30.56 ? 2389 HOH   B O     1 
HETATM 20487 O  O     . HOH   AA 11 .    ? 21.334  11.763  98.606  1.00 43.42 ? 2390 HOH   B O     1 
HETATM 20488 O  O     . HOH   AA 11 .    ? 5.832   11.257  75.022  1.00 37.36 ? 2391 HOH   B O     1 
HETATM 20489 O  O     . HOH   AA 11 .    ? 28.613  69.610  65.769  1.00 39.93 ? 2392 HOH   B O     1 
HETATM 20490 O  O     . HOH   AA 11 .    ? 1.723   11.612  76.531  1.00 38.25 ? 2393 HOH   B O     1 
HETATM 20491 O  O     . HOH   AA 11 .    ? 40.683  31.459  84.119  1.00 38.17 ? 2394 HOH   B O     1 
HETATM 20492 O  O     . HOH   AA 11 .    ? -3.538  48.148  87.472  1.00 41.86 ? 2395 HOH   B O     1 
HETATM 20493 O  O     . HOH   AA 11 .    ? 9.251   64.289  86.531  1.00 39.00 ? 2396 HOH   B O     1 
HETATM 20494 O  O     . HOH   AA 11 .    ? -7.354  22.666  78.144  1.00 33.75 ? 2397 HOH   B O     1 
HETATM 20495 O  O     . HOH   AA 11 .    ? -16.222 7.032   121.875 1.00 37.11 ? 2398 HOH   B O     1 
HETATM 20496 O  O     . HOH   AA 11 .    ? 3.896   30.121  93.818  1.00 34.50 ? 2399 HOH   B O     1 
HETATM 20497 O  O     . HOH   AA 11 .    ? 1.424   14.791  79.232  1.00 29.06 ? 2400 HOH   B O     1 
HETATM 20498 O  O     . HOH   AA 11 .    ? 8.639   -3.083  105.076 1.00 38.26 ? 2401 HOH   B O     1 
HETATM 20499 O  O     . HOH   AA 11 .    ? 10.385  28.913  49.284  1.00 35.92 ? 2402 HOH   B O     1 
HETATM 20500 O  O     . HOH   AA 11 .    ? -2.746  28.601  68.505  1.00 27.39 ? 2403 HOH   B O     1 
HETATM 20501 O  O     . HOH   AA 11 .    ? 12.183  21.456  98.198  1.00 31.94 ? 2404 HOH   B O     1 
HETATM 20502 O  O     . HOH   AA 11 .    ? 16.655  26.425  109.276 1.00 27.61 ? 2405 HOH   B O     1 
HETATM 20503 O  O     . HOH   AA 11 .    ? 32.851  41.142  58.509  1.00 36.64 ? 2406 HOH   B O     1 
HETATM 20504 O  O     . HOH   AA 11 .    ? 24.978  70.744  65.018  1.00 33.99 ? 2407 HOH   B O     1 
HETATM 20505 O  O     . HOH   AA 11 .    ? 21.934  78.209  77.546  1.00 40.43 ? 2408 HOH   B O     1 
HETATM 20506 O  O     . HOH   AA 11 .    ? 10.560  74.554  59.989  1.00 44.27 ? 2409 HOH   B O     1 
HETATM 20507 O  O     . HOH   AA 11 .    ? -8.002  37.727  78.884  1.00 37.26 ? 2410 HOH   B O     1 
HETATM 20508 O  O     . HOH   AA 11 .    ? 33.522  47.557  64.444  1.00 38.60 ? 2411 HOH   B O     1 
HETATM 20509 O  O     . HOH   AA 11 .    ? -4.629  50.983  88.388  1.00 47.34 ? 2412 HOH   B O     1 
HETATM 20510 O  O     . HOH   AA 11 .    ? -12.892 -7.640  105.531 1.00 35.62 ? 2413 HOH   B O     1 
HETATM 20511 O  O     . HOH   AA 11 .    ? 4.909   56.202  66.423  1.00 34.86 ? 2414 HOH   B O     1 
HETATM 20512 O  O     . HOH   AA 11 .    ? 35.606  29.875  53.657  1.00 42.94 ? 2415 HOH   B O     1 
HETATM 20513 O  O     . HOH   AA 11 .    ? 23.996  32.784  114.884 1.00 35.78 ? 2416 HOH   B O     1 
HETATM 20514 O  O     . HOH   AA 11 .    ? 7.108   2.709   79.482  1.00 39.13 ? 2417 HOH   B O     1 
HETATM 20515 O  O     . HOH   AA 11 .    ? 20.265  23.234  109.375 1.00 32.77 ? 2418 HOH   B O     1 
HETATM 20516 O  O     . HOH   AA 11 .    ? -17.835 7.225   92.451  1.00 33.23 ? 2419 HOH   B O     1 
HETATM 20517 O  O     . HOH   AA 11 .    ? 14.810  22.282  97.187  1.00 26.33 ? 2420 HOH   B O     1 
HETATM 20518 O  O     . HOH   AA 11 .    ? 14.921  51.372  55.680  1.00 35.83 ? 2421 HOH   B O     1 
HETATM 20519 O  O     . HOH   AA 11 .    ? -2.342  26.456  100.731 1.00 40.45 ? 2422 HOH   B O     1 
HETATM 20520 O  O     . HOH   AA 11 .    ? 12.649  18.615  91.430  1.00 34.51 ? 2423 HOH   B O     1 
HETATM 20521 O  O     . HOH   AA 11 .    ? 35.496  12.957  78.076  1.00 39.73 ? 2424 HOH   B O     1 
HETATM 20522 O  O     . HOH   AA 11 .    ? 10.256  53.429  88.741  1.00 38.52 ? 2425 HOH   B O     1 
HETATM 20523 O  O     . HOH   AA 11 .    ? 11.813  3.031   84.125  1.00 39.01 ? 2426 HOH   B O     1 
HETATM 20524 O  O     . HOH   AA 11 .    ? -4.128  40.384  60.173  1.00 28.56 ? 2427 HOH   B O     1 
HETATM 20525 O  O     . HOH   AA 11 .    ? -16.151 4.011   123.082 1.00 43.15 ? 2428 HOH   B O     1 
HETATM 20526 O  O     . HOH   AA 11 .    ? -10.706 -6.240  105.162 1.00 31.66 ? 2429 HOH   B O     1 
HETATM 20527 O  O     . HOH   AA 11 .    ? 0.812   55.878  69.698  1.00 32.78 ? 2430 HOH   B O     1 
HETATM 20528 O  O     . HOH   AA 11 .    ? 30.671  63.354  58.387  1.00 40.57 ? 2431 HOH   B O     1 
HETATM 20529 O  O     . HOH   AA 11 .    ? 11.683  17.759  89.051  1.00 34.25 ? 2432 HOH   B O     1 
HETATM 20530 O  O     . HOH   AA 11 .    ? 22.062  14.508  98.007  1.00 40.10 ? 2433 HOH   B O     1 
HETATM 20531 O  O     . HOH   AA 11 .    ? 4.073   55.373  114.091 1.00 44.20 ? 2434 HOH   B O     1 
HETATM 20532 O  O     . HOH   AA 11 .    ? 31.654  32.554  80.538  1.00 36.45 ? 2435 HOH   B O     1 
HETATM 20533 O  O     . HOH   AA 11 .    ? 1.078   31.778  82.100  1.00 25.61 ? 2436 HOH   B O     1 
HETATM 20534 O  O     . HOH   AA 11 .    ? 25.690  68.394  58.829  1.00 42.86 ? 2437 HOH   B O     1 
HETATM 20535 O  O     . HOH   AA 11 .    ? 13.953  25.307  100.241 1.00 23.24 ? 2438 HOH   B O     1 
HETATM 20536 O  O     . HOH   AA 11 .    ? -1.614  -5.382  94.188  1.00 48.12 ? 2439 HOH   B O     1 
HETATM 20537 O  O     . HOH   AA 11 .    ? 11.318  53.703  86.650  1.00 42.99 ? 2440 HOH   B O     1 
HETATM 20538 O  O     . HOH   AA 11 .    ? -4.141  68.695  73.571  1.00 38.34 ? 2441 HOH   B O     1 
HETATM 20539 O  O     . HOH   AA 11 .    ? -24.237 17.690  79.152  1.00 45.25 ? 2442 HOH   B O     1 
HETATM 20540 O  O     B HOH   AA 11 .    ? -3.761  60.182  84.846  0.49 23.54 ? 2443 HOH   B O     1 
HETATM 20541 O  O     . HOH   AA 11 .    ? 22.720  57.072  53.214  1.00 41.94 ? 2444 HOH   B O     1 
HETATM 20542 O  O     . HOH   AA 11 .    ? -10.995 33.695  83.693  1.00 43.41 ? 2445 HOH   B O     1 
HETATM 20543 O  O     . HOH   AA 11 .    ? 13.508  36.698  73.733  1.00 18.16 ? 2446 HOH   B O     1 
HETATM 20544 O  O     . HOH   AA 11 .    ? 3.261   13.516  77.188  1.00 33.59 ? 2447 HOH   B O     1 
HETATM 20545 O  O     . HOH   AA 11 .    ? 34.590  26.626  56.459  1.00 28.88 ? 2448 HOH   B O     1 
HETATM 20546 O  O     . HOH   AA 11 .    ? -1.367  10.651  131.052 1.00 45.11 ? 2449 HOH   B O     1 
HETATM 20547 O  O     . HOH   AA 11 .    ? 14.855  22.384  94.488  1.00 41.74 ? 2450 HOH   B O     1 
HETATM 20548 O  O     . HOH   AA 11 .    ? 11.474  0.931   113.263 1.00 39.37 ? 2451 HOH   B O     1 
HETATM 20549 O  O     . HOH   AA 11 .    ? -8.354  -2.189  117.103 1.00 36.70 ? 2452 HOH   B O     1 
HETATM 20550 O  O     . HOH   AA 11 .    ? 31.355  37.961  106.177 1.00 35.75 ? 2453 HOH   B O     1 
HETATM 20551 O  O     . HOH   AA 11 .    ? 6.345   16.107  91.665  1.00 28.55 ? 2454 HOH   B O     1 
HETATM 20552 O  O     . HOH   AA 11 .    ? 23.456  71.621  61.240  1.00 43.48 ? 2455 HOH   B O     1 
HETATM 20553 O  O     . HOH   AA 11 .    ? 19.937  34.404  114.540 1.00 27.18 ? 2456 HOH   B O     1 
HETATM 20554 O  O     . HOH   AA 11 .    ? 25.691  11.540  67.990  1.00 41.91 ? 2457 HOH   B O     1 
HETATM 20555 O  O     . HOH   AA 11 .    ? -13.502 5.243   85.503  1.00 44.80 ? 2458 HOH   B O     1 
HETATM 20556 O  O     . HOH   AA 11 .    ? 14.795  1.942   99.746  1.00 43.73 ? 2459 HOH   B O     1 
HETATM 20557 O  O     . HOH   AA 11 .    ? 10.481  0.976   106.663 1.00 36.95 ? 2460 HOH   B O     1 
HETATM 20558 O  O     . HOH   AA 11 .    ? -21.654 26.401  96.286  1.00 42.79 ? 2461 HOH   B O     1 
HETATM 20559 O  O     . HOH   AA 11 .    ? 7.360   72.371  60.894  1.00 45.81 ? 2462 HOH   B O     1 
HETATM 20560 O  O     . HOH   AA 11 .    ? 15.739  59.970  92.307  1.00 40.11 ? 2463 HOH   B O     1 
HETATM 20561 O  O     . HOH   AA 11 .    ? 6.591   61.138  84.741  1.00 25.96 ? 2464 HOH   B O     1 
HETATM 20562 O  O     . HOH   AA 11 .    ? 18.198  3.905   73.009  1.00 36.37 ? 2465 HOH   B O     1 
HETATM 20563 O  O     . HOH   AA 11 .    ? 12.032  43.981  52.949  1.00 27.87 ? 2466 HOH   B O     1 
HETATM 20564 O  O     . HOH   AA 11 .    ? 41.758  37.233  89.531  1.00 30.19 ? 2467 HOH   B O     1 
HETATM 20565 O  O     . HOH   AA 11 .    ? 34.509  27.859  60.932  1.00 28.38 ? 2468 HOH   B O     1 
HETATM 20566 O  O     . HOH   AA 11 .    ? 2.033   -7.348  98.109  1.00 41.64 ? 2469 HOH   B O     1 
HETATM 20567 O  O     . HOH   AA 11 .    ? 6.163   30.593  97.648  1.00 39.70 ? 2470 HOH   B O     1 
HETATM 20568 O  O     . HOH   AA 11 .    ? 2.064   25.126  94.772  1.00 38.22 ? 2471 HOH   B O     1 
HETATM 20569 O  O     . HOH   AA 11 .    ? 30.609  61.807  72.327  1.00 25.84 ? 2472 HOH   B O     1 
HETATM 20570 O  O     . HOH   AA 11 .    ? 9.386   4.134   83.244  1.00 30.53 ? 2473 HOH   B O     1 
HETATM 20571 O  O     . HOH   AA 11 .    ? -19.120 15.072  131.235 1.00 47.83 ? 2474 HOH   B O     1 
HETATM 20572 O  O     . HOH   AA 11 .    ? 5.553   30.376  85.992  1.00 37.77 ? 2475 HOH   B O     1 
HETATM 20573 O  O     . HOH   AA 11 .    ? -3.384  13.095  130.557 1.00 36.88 ? 2476 HOH   B O     1 
HETATM 20574 O  O     . HOH   AA 11 .    ? -0.862  18.729  67.979  1.00 44.90 ? 2477 HOH   B O     1 
HETATM 20575 O  O     . HOH   AA 11 .    ? 21.710  19.989  106.766 1.00 26.07 ? 2478 HOH   B O     1 
HETATM 20576 O  O     . HOH   AA 11 .    ? 9.129   -4.766  116.261 1.00 44.40 ? 2479 HOH   B O     1 
HETATM 20577 O  O     . HOH   AA 11 .    ? 18.743  48.662  56.187  1.00 29.90 ? 2480 HOH   B O     1 
HETATM 20578 O  O     . HOH   AA 11 .    ? 14.530  44.450  52.411  1.00 36.43 ? 2481 HOH   B O     1 
HETATM 20579 O  O     . HOH   AA 11 .    ? 18.652  29.038  112.778 1.00 35.35 ? 2482 HOH   B O     1 
HETATM 20580 O  O     . HOH   AA 11 .    ? 32.586  45.620  57.169  1.00 43.62 ? 2483 HOH   B O     1 
HETATM 20581 O  O     . HOH   AA 11 .    ? 16.221  77.174  61.523  1.00 43.12 ? 2484 HOH   B O     1 
HETATM 20582 O  O     . HOH   AA 11 .    ? 5.313   3.498   85.397  1.00 33.12 ? 2485 HOH   B O     1 
HETATM 20583 O  O     . HOH   AA 11 .    ? 20.443  46.760  51.571  1.00 41.36 ? 2486 HOH   B O     1 
HETATM 20584 O  O     . HOH   AA 11 .    ? -4.793  3.376   82.609  1.00 41.12 ? 2487 HOH   B O     1 
HETATM 20585 O  O     . HOH   AA 11 .    ? -0.411  57.234  67.580  1.00 37.03 ? 2488 HOH   B O     1 
HETATM 20586 O  O     . HOH   AA 11 .    ? 30.365  24.201  74.001  1.00 26.06 ? 2489 HOH   B O     1 
HETATM 20587 O  O     . HOH   AA 11 .    ? -9.563  -1.486  121.319 1.00 42.92 ? 2490 HOH   B O     1 
HETATM 20588 O  O     . HOH   AA 11 .    ? -9.816  35.302  89.062  1.00 44.14 ? 2491 HOH   B O     1 
HETATM 20589 O  O     . HOH   AA 11 .    ? 7.599   25.674  103.182 1.00 37.06 ? 2492 HOH   B O     1 
HETATM 20590 O  O     . HOH   AA 11 .    ? 13.174  37.074  76.736  1.00 19.13 ? 2493 HOH   B O     1 
HETATM 20591 O  O     . HOH   AA 11 .    ? -15.843 -0.403  98.146  1.00 43.46 ? 2494 HOH   B O     1 
HETATM 20592 O  O     . HOH   AA 11 .    ? 16.774  44.035  51.987  1.00 38.86 ? 2495 HOH   B O     1 
HETATM 20593 O  O     . HOH   AA 11 .    ? 8.808   65.040  65.684  1.00 33.20 ? 2496 HOH   B O     1 
HETATM 20594 O  O     . HOH   AA 11 .    ? 18.701  79.009  64.957  1.00 40.13 ? 2497 HOH   B O     1 
HETATM 20595 O  O     . HOH   AA 11 .    ? 4.538   64.300  86.097  1.00 33.82 ? 2498 HOH   B O     1 
HETATM 20596 O  O     . HOH   AA 11 .    ? 12.675  55.746  105.031 1.00 33.26 ? 2499 HOH   B O     1 
HETATM 20597 O  O     . HOH   AA 11 .    ? 15.342  73.138  58.070  1.00 37.03 ? 2500 HOH   B O     1 
HETATM 20598 O  O     . HOH   AA 11 .    ? 12.993  74.906  60.570  1.00 37.88 ? 2501 HOH   B O     1 
HETATM 20599 O  O     . HOH   AA 11 .    ? 18.308  9.384   95.252  1.00 35.37 ? 2502 HOH   B O     1 
HETATM 20600 O  O     . HOH   AA 11 .    ? 1.499   22.342  94.889  1.00 38.39 ? 2503 HOH   B O     1 
HETATM 20601 O  O     . HOH   AA 11 .    ? 18.500  3.266   77.233  1.00 41.70 ? 2504 HOH   B O     1 
HETATM 20602 O  O     . HOH   AA 11 .    ? 26.388  52.463  83.405  1.00 30.91 ? 2505 HOH   B O     1 
HETATM 20603 O  O     . HOH   AA 11 .    ? 41.674  30.547  81.888  1.00 39.36 ? 2506 HOH   B O     1 
HETATM 20604 O  O     . HOH   AA 11 .    ? 9.004   24.883  86.663  1.00 38.36 ? 2507 HOH   B O     1 
HETATM 20605 O  O     . HOH   AA 11 .    ? -7.122  25.286  74.447  1.00 33.32 ? 2508 HOH   B O     1 
HETATM 20606 O  O     . HOH   AA 11 .    ? 12.328  0.777   108.642 1.00 38.14 ? 2509 HOH   B O     1 
HETATM 20607 O  O     . HOH   AA 11 .    ? 20.025  11.217  95.992  1.00 39.04 ? 2510 HOH   B O     1 
HETATM 20608 O  O     . HOH   AA 11 .    ? 10.518  59.945  85.819  1.00 38.93 ? 2511 HOH   B O     1 
HETATM 20609 O  O     . HOH   AA 11 .    ? 31.191  64.859  62.624  1.00 44.26 ? 2512 HOH   B O     1 
HETATM 20610 O  O     . HOH   AA 11 .    ? -8.866  4.104   84.324  1.00 37.02 ? 2513 HOH   B O     1 
HETATM 20611 O  O     . HOH   AA 11 .    ? -8.493  33.945  84.764  1.00 33.22 ? 2514 HOH   B O     1 
HETATM 20612 O  O     . HOH   AA 11 .    ? 13.769  24.894  97.714  1.00 28.52 ? 2515 HOH   B O     1 
HETATM 20613 O  O     . HOH   AA 11 .    ? 14.328  35.524  81.205  1.00 26.67 ? 2516 HOH   B O     1 
HETATM 20614 O  O     . HOH   AA 11 .    ? -9.200  -0.020  85.973  1.00 40.89 ? 2517 HOH   B O     1 
HETATM 20615 O  O     . HOH   AA 11 .    ? 14.717  7.195   91.418  1.00 34.86 ? 2518 HOH   B O     1 
HETATM 20616 O  O     . HOH   AA 11 .    ? -10.958 47.295  76.819  1.00 34.49 ? 2519 HOH   B O     1 
HETATM 20617 O  O     . HOH   AA 11 .    ? -0.701  80.527  76.808  1.00 41.97 ? 2520 HOH   B O     1 
HETATM 20618 O  O     . HOH   AA 11 .    ? 7.675   28.347  83.384  1.00 39.16 ? 2521 HOH   B O     1 
HETATM 20619 O  O     . HOH   AA 11 .    ? 7.970   31.532  85.551  1.00 35.74 ? 2522 HOH   B O     1 
HETATM 20620 O  O     . HOH   AA 11 .    ? 32.425  60.319  62.350  1.00 34.63 ? 2523 HOH   B O     1 
HETATM 20621 O  O     . HOH   AA 11 .    ? 3.478   48.167  88.875  1.00 34.55 ? 2524 HOH   B O     1 
HETATM 20622 O  O     . HOH   AA 11 .    ? 22.464  50.636  68.283  1.00 25.92 ? 2525 HOH   B O     1 
HETATM 20623 O  O     . HOH   AA 11 .    ? 23.602  13.939  96.077  1.00 45.24 ? 2526 HOH   B O     1 
HETATM 20624 O  O     . HOH   AA 11 .    ? -16.236 8.165   90.416  1.00 29.93 ? 2527 HOH   B O     1 
HETATM 20625 O  O     . HOH   AA 11 .    ? 24.043  76.657  78.236  1.00 42.92 ? 2528 HOH   B O     1 
HETATM 20626 O  O     . HOH   AA 11 .    ? -19.573 1.243   96.974  1.00 40.61 ? 2529 HOH   B O     1 
HETATM 20627 O  O     . HOH   AA 11 .    ? -5.663  38.496  61.288  1.00 38.40 ? 2530 HOH   B O     1 
HETATM 20628 O  O     . HOH   AA 11 .    ? 15.013  56.044  103.888 1.00 30.37 ? 2531 HOH   B O     1 
HETATM 20629 O  O     . HOH   AA 11 .    ? 5.350   82.093  77.346  1.00 40.50 ? 2532 HOH   B O     1 
HETATM 20630 O  O     . HOH   AA 11 .    ? -11.667 2.288   88.430  1.00 35.07 ? 2533 HOH   B O     1 
HETATM 20631 O  O     . HOH   AA 11 .    ? -25.391 13.360  86.264  1.00 36.61 ? 2534 HOH   B O     1 
HETATM 20632 O  O     . HOH   AA 11 .    ? -10.984 4.118   86.481  1.00 34.83 ? 2535 HOH   B O     1 
HETATM 20633 O  O     . HOH   AA 11 .    ? 11.762  1.857   115.562 1.00 38.82 ? 2536 HOH   B O     1 
HETATM 20634 O  O     . HOH   AA 11 .    ? 2.085   44.754  96.513  1.00 29.63 ? 2537 HOH   B O     1 
HETATM 20635 O  O     . HOH   AA 11 .    ? 6.274   12.267  72.500  1.00 37.09 ? 2538 HOH   B O     1 
HETATM 20636 O  O     . HOH   AA 11 .    ? -5.176  -0.388  83.862  1.00 40.86 ? 2539 HOH   B O     1 
HETATM 20637 O  O     . HOH   AA 11 .    ? 2.762   10.411  74.389  1.00 39.92 ? 2540 HOH   B O     1 
HETATM 20638 O  O     . HOH   AA 11 .    ? 35.003  38.953  64.078  1.00 36.80 ? 2541 HOH   B O     1 
HETATM 20639 O  O     . HOH   AA 11 .    ? -0.121  29.104  96.140  1.00 25.50 ? 2542 HOH   B O     1 
HETATM 20640 O  O     . HOH   AA 11 .    ? -12.383 53.396  125.906 1.00 42.28 ? 2543 HOH   B O     1 
HETATM 20641 O  O     . HOH   AA 11 .    ? -6.334  36.307  61.221  1.00 42.43 ? 2544 HOH   B O     1 
HETATM 20642 O  O     . HOH   AA 11 .    ? 27.358  55.240  83.153  1.00 38.70 ? 2545 HOH   B O     1 
HETATM 20643 O  O     . HOH   AA 11 .    ? 18.492  4.904   96.967  1.00 43.42 ? 2546 HOH   B O     1 
HETATM 20644 O  O     . HOH   AA 11 .    ? 33.463  19.735  53.851  1.00 33.45 ? 2547 HOH   B O     1 
HETATM 20645 O  O     . HOH   AA 11 .    ? 9.415   17.389  89.478  1.00 32.23 ? 2548 HOH   B O     1 
HETATM 20646 O  O     . HOH   AA 11 .    ? 6.295   -4.497  101.427 1.00 37.86 ? 2549 HOH   B O     1 
HETATM 20647 O  O     . HOH   AA 11 .    ? 22.101  5.137   70.382  1.00 41.68 ? 2550 HOH   B O     1 
HETATM 20648 O  O     . HOH   AA 11 .    ? -7.733  37.189  83.451  1.00 35.99 ? 2551 HOH   B O     1 
HETATM 20649 O  O     . HOH   AA 11 .    ? -21.106 16.734  79.614  1.00 41.57 ? 2552 HOH   B O     1 
HETATM 20650 O  O     . HOH   AA 11 .    ? 13.869  44.723  49.105  1.00 37.01 ? 2553 HOH   B O     1 
HETATM 20651 O  O     . HOH   AA 11 .    ? 2.351   64.956  86.912  1.00 43.25 ? 2554 HOH   B O     1 
HETATM 20652 O  O     . HOH   AA 11 .    ? 20.426  28.090  43.313  1.00 34.02 ? 2555 HOH   B O     1 
HETATM 20653 O  O     . HOH   AA 11 .    ? -12.760 -0.247  120.908 1.00 39.98 ? 2556 HOH   B O     1 
HETATM 20654 O  O     . HOH   AA 11 .    ? -3.105  38.143  77.482  1.00 31.21 ? 2557 HOH   B O     1 
HETATM 20655 O  O     . HOH   AA 11 .    ? -7.447  -4.710  91.017  1.00 43.27 ? 2558 HOH   B O     1 
HETATM 20656 O  O     . HOH   AA 11 .    ? -1.255  23.501  63.646  1.00 32.24 ? 2559 HOH   B O     1 
HETATM 20657 O  O     . HOH   AA 11 .    ? -8.388  35.479  86.785  1.00 40.49 ? 2560 HOH   B O     1 
HETATM 20658 O  O     . HOH   AA 11 .    ? -4.349  23.428  72.060  1.00 40.34 ? 2561 HOH   B O     1 
HETATM 20659 O  O     . HOH   AA 11 .    ? 1.748   44.475  78.205  1.00 27.51 ? 2562 HOH   B O     1 
HETATM 20660 O  O     . HOH   AA 11 .    ? 2.113   22.098  60.736  1.00 33.52 ? 2563 HOH   B O     1 
HETATM 20661 O  O     . HOH   AA 11 .    ? 3.253   15.256  75.100  1.00 31.83 ? 2564 HOH   B O     1 
HETATM 20662 O  O     . HOH   AA 11 .    ? -23.351 14.413  81.793  1.00 34.77 ? 2565 HOH   B O     1 
HETATM 20663 O  O     . HOH   AA 11 .    ? 2.225   32.056  84.577  1.00 22.93 ? 2566 HOH   B O     1 
HETATM 20664 O  O     . HOH   AA 11 .    ? 34.566  47.701  68.581  1.00 39.26 ? 2567 HOH   B O     1 
HETATM 20665 O  O     . HOH   AA 11 .    ? 6.936   19.106  89.332  1.00 31.03 ? 2568 HOH   B O     1 
HETATM 20666 O  O     . HOH   AA 11 .    ? -14.205 23.541  80.592  1.00 44.69 ? 2569 HOH   B O     1 
HETATM 20667 O  O     . HOH   AA 11 .    ? -0.801  22.209  59.042  1.00 47.16 ? 2570 HOH   B O     1 
HETATM 20668 O  O     . HOH   AA 11 .    ? -19.331 20.483  78.340  1.00 41.81 ? 2571 HOH   B O     1 
HETATM 20669 O  O     . HOH   AA 11 .    ? 10.510  28.815  84.867  1.00 42.41 ? 2572 HOH   B O     1 
HETATM 20670 O  O     . HOH   AA 11 .    ? 41.195  28.074  90.900  1.00 40.94 ? 2573 HOH   B O     1 
HETATM 20671 O  O     . HOH   AA 11 .    ? -4.796  23.808  74.709  1.00 31.87 ? 2574 HOH   B O     1 
HETATM 20672 O  O     . HOH   AA 11 .    ? 0.640   28.094  98.668  1.00 39.76 ? 2575 HOH   B O     1 
HETATM 20673 O  O     . HOH   AA 11 .    ? 29.455  64.665  55.059  1.00 47.32 ? 2576 HOH   B O     1 
HETATM 20674 O  O     . HOH   AA 11 .    ? 22.114  31.528  44.956  1.00 38.82 ? 2577 HOH   B O     1 
HETATM 20675 O  O     . HOH   AA 11 .    ? 33.564  44.191  58.783  1.00 44.47 ? 2578 HOH   B O     1 
HETATM 20676 O  O     . HOH   AA 11 .    ? 6.144   1.722   81.657  1.00 42.60 ? 2579 HOH   B O     1 
HETATM 20677 O  O     . HOH   AA 11 .    ? -2.602  23.766  61.182  1.00 41.11 ? 2580 HOH   B O     1 
HETATM 20678 O  O     . HOH   AA 11 .    ? -5.245  21.432  76.200  1.00 37.88 ? 2581 HOH   B O     1 
HETATM 20679 O  O     . HOH   AA 11 .    ? 19.452  31.899  44.945  1.00 44.01 ? 2582 HOH   B O     1 
HETATM 20680 O  O     . HOH   AA 11 .    ? -24.773 12.881  83.379  1.00 37.99 ? 2583 HOH   B O     1 
HETATM 20681 O  O     . HOH   AA 11 .    ? 33.043  23.369  74.658  1.00 39.63 ? 2584 HOH   B O     1 
HETATM 20682 O  O     . HOH   AA 11 .    ? 22.931  29.644  43.585  1.00 45.28 ? 2585 HOH   B O     1 
HETATM 20683 O  O     . HOH   AA 11 .    ? -15.994 6.270   88.429  1.00 39.29 ? 2586 HOH   B O     1 
HETATM 20684 O  O     . HOH   AA 11 .    ? 7.284   2.252   83.681  1.00 35.02 ? 2587 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   ? 0.5214 0.5467 0.6132 0.0905  -0.0224 -0.1228 14   ALA A N   
2     C CA  . ALA A 16   ? 0.5774 0.6038 0.6600 0.0875  -0.0200 -0.1183 14   ALA A CA  
3     C C   . ALA A 16   ? 0.5353 0.5697 0.6081 0.0864  -0.0149 -0.1123 14   ALA A C   
4     O O   . ALA A 16   ? 0.5705 0.6169 0.6405 0.0896  -0.0127 -0.1161 14   ALA A O   
5     C CB  . ALA A 16   ? 0.5831 0.6155 0.6651 0.0901  -0.0213 -0.1264 14   ALA A CB  
6     N N   . PRO A 17   ? 0.5159 0.5443 0.5840 0.0819  -0.0131 -0.1029 15   PRO A N   
7     C CA  . PRO A 17   ? 0.4422 0.4773 0.5021 0.0806  -0.0085 -0.0967 15   PRO A CA  
8     C C   . PRO A 17   ? 0.4703 0.5158 0.5225 0.0815  -0.0059 -0.0981 15   PRO A C   
9     O O   . PRO A 17   ? 0.4077 0.4517 0.4582 0.0810  -0.0071 -0.0999 15   PRO A O   
10    C CB  . PRO A 17   ? 0.4499 0.4748 0.5075 0.0755  -0.0080 -0.0874 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.4726 0.4883 0.5339 0.0739  -0.0114 -0.0887 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.4699 0.4857 0.5399 0.0777  -0.0151 -0.0976 15   PRO A CD  
13    N N   . ALA A 18   ? 0.4125 0.4687 0.4601 0.0829  -0.0025 -0.0969 16   ALA A N   
14    C CA  . ALA A 18   ? 0.3574 0.4251 0.3979 0.0840  0.0001  -0.0978 16   ALA A CA  
15    C C   . ALA A 18   ? 0.3220 0.3853 0.3559 0.0798  0.0015  -0.0904 16   ALA A C   
16    O O   . ALA A 18   ? 0.3279 0.3831 0.3610 0.0762  0.0023  -0.0830 16   ALA A O   
17    C CB  . ALA A 18   ? 0.3796 0.4596 0.4170 0.0859  0.0036  -0.0966 16   ALA A CB  
18    N N   . PRO A 19   ? 0.3102 0.3786 0.3396 0.0803  0.0018  -0.0923 17   PRO A N   
19    C CA  . PRO A 19   ? 0.3145 0.3786 0.3384 0.0764  0.0030  -0.0856 17   PRO A CA  
20    C C   . PRO A 19   ? 0.2830 0.3506 0.3013 0.0742  0.0068  -0.0772 17   PRO A C   
21    O O   . PRO A 19   ? 0.3121 0.3911 0.3277 0.0761  0.0093  -0.0771 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3486 0.4206 0.3690 0.0784  0.0026  -0.0905 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.3399 0.4153 0.3664 0.0827  -0.0001 -0.1007 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.3026 0.3806 0.3327 0.0844  0.0007  -0.1013 17   PRO A CD  
25    N N   . PHE A 20   ? 0.2744 0.3322 0.2915 0.0701  0.0071  -0.0700 18   PHE A N   
26    C CA  . PHE A 20   ? 0.2787 0.3377 0.2914 0.0673  0.0103  -0.0617 18   PHE A CA  
27    C C   . PHE A 20   ? 0.3115 0.3735 0.3261 0.0679  0.0119  -0.0597 18   PHE A C   
28    O O   . PHE A 20   ? 0.2975 0.3625 0.3088 0.0661  0.0146  -0.0534 18   PHE A O   
29    C CB  . PHE A 20   ? 0.2823 0.3508 0.2884 0.0673  0.0127  -0.0593 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.2812 0.3469 0.2850 0.0665  0.0113  -0.0605 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2764 0.3324 0.2789 0.0628  0.0109  -0.0553 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.2875 0.3608 0.2905 0.0696  0.0103  -0.0672 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.2830 0.3367 0.2836 0.0620  0.0096  -0.0564 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.3004 0.3714 0.3014 0.0688  0.0089  -0.0683 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.2983 0.3594 0.2982 0.0650  0.0086  -0.0628 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.3198 0.3810 0.3402 0.0703  0.0101  -0.0649 19   ALA A N   
37    C CA  . ALA A 21   ? 0.2922 0.3563 0.3148 0.0710  0.0115  -0.0633 19   ALA A CA  
38    C C   . ALA A 21   ? 0.3630 0.4178 0.3861 0.0671  0.0120  -0.0559 19   ALA A C   
39    O O   . ALA A 21   ? 0.3447 0.4027 0.3680 0.0667  0.0139  -0.0525 19   ALA A O   
40    C CB  . ALA A 21   ? 0.3246 0.3892 0.3540 0.0746  0.0091  -0.0709 19   ALA A CB  
41    N N   . ASP A 22   ? 0.2864 0.3305 0.3098 0.0642  0.0102  -0.0536 20   ASP A N   
42    C CA  . ASP A 22   ? 0.3183 0.3538 0.3420 0.0605  0.0105  -0.0470 20   ASP A CA  
43    C C   . ASP A 22   ? 0.2580 0.2894 0.2771 0.0572  0.0111  -0.0422 20   ASP A C   
44    O O   . ASP A 22   ? 0.3024 0.3244 0.3223 0.0543  0.0099  -0.0390 20   ASP A O   
45    C CB  . ASP A 22   ? 0.3769 0.4031 0.4069 0.0602  0.0073  -0.0487 20   ASP A CB  
46    C CG  . ASP A 22   ? 0.4956 0.5254 0.5310 0.0635  0.0065  -0.0533 20   ASP A CG  
47    O OD1 . ASP A 22   ? 0.5788 0.6144 0.6135 0.0641  0.0087  -0.0513 20   ASP A OD1 
48    O OD2 . ASP A 22   ? 0.6311 0.6580 0.6717 0.0656  0.0035  -0.0590 20   ASP A OD2 
49    N N   . PHE A 23   ? 0.2565 0.2952 0.2706 0.0577  0.0130  -0.0417 21   PHE A N   
50    C CA  . PHE A 23   ? 0.2349 0.2700 0.2450 0.0551  0.0132  -0.0382 21   PHE A CA  
51    C C   . PHE A 23   ? 0.2370 0.2661 0.2461 0.0513  0.0143  -0.0311 21   PHE A C   
52    O O   . PHE A 23   ? 0.2425 0.2630 0.2519 0.0489  0.0129  -0.0293 21   PHE A O   
53    C CB  . PHE A 23   ? 0.2452 0.2902 0.2504 0.0563  0.0152  -0.0382 21   PHE A CB  
54    C CG  . PHE A 23   ? 0.2291 0.2709 0.2304 0.0537  0.0156  -0.0341 21   PHE A CG  
55    C CD1 . PHE A 23   ? 0.2663 0.3009 0.2681 0.0527  0.0133  -0.0360 21   PHE A CD1 
56    C CD2 . PHE A 23   ? 0.2406 0.2863 0.2383 0.0520  0.0181  -0.0281 21   PHE A CD2 
57    C CE1 . PHE A 23   ? 0.2643 0.2960 0.2628 0.0503  0.0136  -0.0324 21   PHE A CE1 
58    C CE2 . PHE A 23   ? 0.2735 0.3160 0.2683 0.0497  0.0183  -0.0244 21   PHE A CE2 
59    C CZ  . PHE A 23   ? 0.2630 0.2986 0.2580 0.0489  0.0161  -0.0267 21   PHE A CZ  
60    N N   . ALA A 24   ? 0.2592 0.2930 0.2672 0.0508  0.0167  -0.0270 22   ALA A N   
61    C CA  . ALA A 24   ? 0.2744 0.3032 0.2816 0.0473  0.0177  -0.0206 22   ALA A CA  
62    C C   . ALA A 24   ? 0.2350 0.2682 0.2434 0.0473  0.0196  -0.0176 22   ALA A C   
63    O O   . ALA A 24   ? 0.2371 0.2734 0.2433 0.0457  0.0217  -0.0127 22   ALA A O   
64    C CB  . ALA A 24   ? 0.3047 0.3344 0.3075 0.0456  0.0189  -0.0170 22   ALA A CB  
65    N N   . PRO A 25   ? 0.2643 0.2975 0.2766 0.0488  0.0189  -0.0201 23   PRO A N   
66    C CA  . PRO A 25   ? 0.2794 0.3172 0.2931 0.0488  0.0207  -0.0174 23   PRO A CA  
67    C C   . PRO A 25   ? 0.2577 0.2897 0.2713 0.0452  0.0212  -0.0114 23   PRO A C   
68    O O   . PRO A 25   ? 0.2572 0.2804 0.2716 0.0432  0.0195  -0.0107 23   PRO A O   
69    C CB  . PRO A 25   ? 0.2920 0.3286 0.3104 0.0510  0.0190  -0.0218 23   PRO A CB  
70    C CG  . PRO A 25   ? 0.3008 0.3282 0.3209 0.0504  0.0161  -0.0242 23   PRO A CG  
71    C CD  . PRO A 25   ? 0.2871 0.3150 0.3034 0.0502  0.0161  -0.0250 23   PRO A CD  
72    N N   . PRO A 26   ? 0.2628 0.2999 0.2756 0.0442  0.0235  -0.0070 24   PRO A N   
73    C CA  . PRO A 26   ? 0.2666 0.2985 0.2799 0.0408  0.0238  -0.0018 24   PRO A CA  
74    C C   . PRO A 26   ? 0.2473 0.2742 0.2644 0.0403  0.0226  -0.0021 24   PRO A C   
75    O O   . PRO A 26   ? 0.2592 0.2883 0.2790 0.0426  0.0220  -0.0055 24   PRO A O   
76    C CB  . PRO A 26   ? 0.2686 0.3085 0.2813 0.0404  0.0264  0.0024  24   PRO A CB  
77    C CG  . PRO A 26   ? 0.3403 0.3897 0.3533 0.0438  0.0273  -0.0010 24   PRO A CG  
78    C CD  . PRO A 26   ? 0.2883 0.3367 0.3001 0.0461  0.0257  -0.0067 24   PRO A CD  
79    N N   . VAL A 27   ? 0.2510 0.2713 0.2685 0.0373  0.0221  0.0013  25   VAL A N   
80    C CA  . VAL A 27   ? 0.2323 0.2483 0.2532 0.0364  0.0210  0.0018  25   VAL A CA  
81    C C   . VAL A 27   ? 0.2901 0.3124 0.3135 0.0375  0.0223  0.0024  25   VAL A C   
82    O O   . VAL A 27   ? 0.2765 0.2983 0.3031 0.0388  0.0212  0.0004  25   VAL A O   
83    C CB  . VAL A 27   ? 0.2353 0.2452 0.2558 0.0329  0.0206  0.0056  25   VAL A CB  
84    C CG1 . VAL A 27   ? 0.2713 0.2785 0.2952 0.0320  0.0197  0.0066  25   VAL A CG1 
85    C CG2 . VAL A 27   ? 0.2626 0.2663 0.2812 0.0319  0.0190  0.0045  25   VAL A CG2 
86    N N   . ARG A 28   ? 0.2788 0.3074 0.3012 0.0371  0.0245  0.0055  26   ARG A N   
87    C CA  . ARG A 28   ? 0.2784 0.3139 0.3033 0.0381  0.0260  0.0066  26   ARG A CA  
88    C C   . ARG A 28   ? 0.3276 0.3724 0.3505 0.0390  0.0283  0.0081  26   ARG A C   
89    O O   . ARG A 28   ? 0.2653 0.3098 0.2851 0.0381  0.0287  0.0096  26   ARG A O   
90    C CB  . ARG A 28   ? 0.3087 0.3414 0.3359 0.0352  0.0262  0.0108  26   ARG A CB  
91    C CG  . ARG A 28   ? 0.3441 0.3761 0.3698 0.0325  0.0273  0.0154  26   ARG A CG  
92    C CD  . ARG A 28   ? 0.3899 0.4181 0.4183 0.0296  0.0269  0.0187  26   ARG A CD  
93    N NE  . ARG A 28   ? 0.4040 0.4236 0.4322 0.0282  0.0249  0.0176  26   ARG A NE  
94    C CZ  . ARG A 28   ? 0.4322 0.4485 0.4624 0.0284  0.0234  0.0159  26   ARG A CZ  
95    N NH1 . ARG A 28   ? 0.4351 0.4555 0.4680 0.0301  0.0236  0.0150  26   ARG A NH1 
96    N NH2 . ARG A 28   ? 0.3778 0.3872 0.4075 0.0270  0.0216  0.0154  26   ARG A NH2 
97    N N   . PRO A 29   ? 0.2785 0.3320 0.3030 0.0408  0.0298  0.0079  27   PRO A N   
98    C CA  . PRO A 29   ? 0.3062 0.3695 0.3290 0.0413  0.0321  0.0104  27   PRO A CA  
99    C C   . PRO A 29   ? 0.2752 0.3367 0.2980 0.0379  0.0330  0.0167  27   PRO A C   
100   O O   . PRO A 29   ? 0.2730 0.3295 0.2984 0.0355  0.0326  0.0193  27   PRO A O   
101   C CB  . PRO A 29   ? 0.2989 0.3709 0.3245 0.0432  0.0334  0.0097  27   PRO A CB  
102   C CG  . PRO A 29   ? 0.3010 0.3684 0.3291 0.0451  0.0314  0.0046  27   PRO A CG  
103   C CD  . PRO A 29   ? 0.3062 0.3615 0.3344 0.0425  0.0294  0.0054  27   PRO A CD  
104   N N   . GLN A 30   ? 0.2663 0.3321 0.2864 0.0376  0.0342  0.0190  28   GLN A N   
105   C CA  . GLN A 30   ? 0.2809 0.3442 0.3013 0.0344  0.0346  0.0247  28   GLN A CA  
106   C C   . GLN A 30   ? 0.2620 0.3326 0.2855 0.0334  0.0365  0.0298  28   GLN A C   
107   O O   . GLN A 30   ? 0.2902 0.3714 0.3131 0.0349  0.0382  0.0309  28   GLN A O   
108   C CB  . GLN A 30   ? 0.2767 0.3416 0.2935 0.0346  0.0349  0.0255  28   GLN A CB  
109   C CG  . GLN A 30   ? 0.2624 0.3202 0.2763 0.0355  0.0330  0.0207  28   GLN A CG  
110   C CD  . GLN A 30   ? 0.2636 0.3099 0.2785 0.0330  0.0313  0.0211  28   GLN A CD  
111   O OE1 . GLN A 30   ? 0.2454 0.2880 0.2602 0.0307  0.0311  0.0244  28   GLN A OE1 
112   N NE2 . GLN A 30   ? 0.2606 0.3019 0.2769 0.0335  0.0299  0.0176  28   GLN A NE2 
113   N N   . SER A 31   ? 0.2527 0.3183 0.2798 0.0307  0.0360  0.0328  29   SER A N   
114   C CA  . SER A 31   ? 0.2225 0.2943 0.2534 0.0293  0.0375  0.0379  29   SER A CA  
115   C C   . SER A 31   ? 0.2713 0.3471 0.3020 0.0278  0.0386  0.0434  29   SER A C   
116   O O   . SER A 31   ? 0.2442 0.3167 0.2721 0.0275  0.0380  0.0433  29   SER A O   
117   C CB  . SER A 31   ? 0.2352 0.2998 0.2702 0.0267  0.0364  0.0395  29   SER A CB  
118   O OG  . SER A 31   ? 0.2315 0.2881 0.2663 0.0242  0.0352  0.0412  29   SER A OG  
119   N N   . THR A 32   ? 0.2651 0.3485 0.2992 0.0267  0.0401  0.0485  30   THR A N   
120   C CA  . THR A 32   ? 0.2351 0.3222 0.2704 0.0249  0.0410  0.0548  30   THR A CA  
121   C C   . THR A 32   ? 0.2428 0.3193 0.2794 0.0222  0.0392  0.0564  30   THR A C   
122   O O   . THR A 32   ? 0.2368 0.3129 0.2718 0.0217  0.0391  0.0585  30   THR A O   
123   C CB  . THR A 32   ? 0.2672 0.3623 0.3075 0.0235  0.0425  0.0604  30   THR A CB  
124   O OG1 . THR A 32   ? 0.3347 0.4407 0.3738 0.0262  0.0441  0.0585  30   THR A OG1 
125   C CG2 . THR A 32   ? 0.3087 0.4081 0.3511 0.0214  0.0432  0.0676  30   THR A CG2 
126   N N   . LEU A 33   ? 0.2495 0.3177 0.2890 0.0206  0.0378  0.0551  31   LEU A N   
127   C CA  . LEU A 33   ? 0.2186 0.2773 0.2596 0.0182  0.0362  0.0561  31   LEU A CA  
128   C C   . LEU A 33   ? 0.2271 0.2797 0.2630 0.0193  0.0350  0.0518  31   LEU A C   
129   O O   . LEU A 33   ? 0.2220 0.2706 0.2577 0.0181  0.0343  0.0534  31   LEU A O   
130   C CB  . LEU A 33   ? 0.2182 0.2706 0.2633 0.0163  0.0349  0.0553  31   LEU A CB  
131   C CG  . LEU A 33   ? 0.2552 0.3120 0.3066 0.0143  0.0356  0.0605  31   LEU A CG  
132   C CD1 . LEU A 33   ? 0.2548 0.3071 0.3096 0.0132  0.0345  0.0586  31   LEU A CD1 
133   C CD2 . LEU A 33   ? 0.3034 0.3587 0.3586 0.0118  0.0352  0.0658  31   LEU A CD2 
134   N N   . ARG A 34   ? 0.2112 0.2630 0.2434 0.0216  0.0348  0.0464  32   ARG A N   
135   C CA  . ARG A 34   ? 0.1988 0.2451 0.2265 0.0226  0.0336  0.0425  32   ARG A CA  
136   C C   . ARG A 34   ? 0.2157 0.2678 0.2403 0.0238  0.0346  0.0438  32   ARG A C   
137   O O   . ARG A 34   ? 0.2281 0.2758 0.2506 0.0233  0.0337  0.0435  32   ARG A O   
138   C CB  . ARG A 34   ? 0.2382 0.2828 0.2637 0.0248  0.0329  0.0367  32   ARG A CB  
139   C CG  . ARG A 34   ? 0.2326 0.2700 0.2604 0.0236  0.0315  0.0350  32   ARG A CG  
140   C CD  . ARG A 34   ? 0.2551 0.2834 0.2821 0.0218  0.0298  0.0342  32   ARG A CD  
141   N NE  . ARG A 34   ? 0.2334 0.2586 0.2562 0.0232  0.0289  0.0304  32   ARG A NE  
142   C CZ  . ARG A 34   ? 0.2694 0.2906 0.2911 0.0242  0.0277  0.0263  32   ARG A CZ  
143   N NH1 . ARG A 34   ? 0.2696 0.2894 0.2938 0.0240  0.0271  0.0255  32   ARG A NH1 
144   N NH2 . ARG A 34   ? 0.2628 0.2816 0.2813 0.0254  0.0268  0.0232  32   ARG A NH2 
145   N N   . ARG A 35   ? 0.2256 0.2880 0.2499 0.0253  0.0363  0.0454  33   ARG A N   
146   C CA  . ARG A 35   ? 0.2182 0.2873 0.2393 0.0265  0.0373  0.0469  33   ARG A CA  
147   C C   . ARG A 35   ? 0.2260 0.2943 0.2493 0.0241  0.0372  0.0529  33   ARG A C   
148   O O   . ARG A 35   ? 0.2308 0.2997 0.2512 0.0245  0.0371  0.0535  33   ARG A O   
149   C CB  . ARG A 35   ? 0.2420 0.3237 0.2626 0.0286  0.0392  0.0474  33   ARG A CB  
150   C CG  . ARG A 35   ? 0.2696 0.3530 0.2875 0.0318  0.0390  0.0405  33   ARG A CG  
151   C CD  . ARG A 35   ? 0.3104 0.4071 0.3281 0.0341  0.0410  0.0406  33   ARG A CD  
152   N N   . ALA A 36   ? 0.2224 0.2892 0.2511 0.0215  0.0372  0.0574  34   ALA A N   
153   C CA  . ALA A 36   ? 0.2357 0.3008 0.2676 0.0192  0.0368  0.0631  34   ALA A CA  
154   C C   . ALA A 36   ? 0.2343 0.2888 0.2652 0.0183  0.0349  0.0607  34   ALA A C   
155   O O   . ALA A 36   ? 0.2423 0.2961 0.2734 0.0175  0.0345  0.0636  34   ALA A O   
156   C CB  . ALA A 36   ? 0.2450 0.3105 0.2837 0.0167  0.0370  0.0680  34   ALA A CB  
157   N N   . ILE A 37   ? 0.1942 0.2409 0.2241 0.0184  0.0337  0.0556  35   ILE A N   
158   C CA  . ILE A 37   ? 0.1996 0.2374 0.2279 0.0178  0.0320  0.0528  35   ILE A CA  
159   C C   . ILE A 37   ? 0.2036 0.2431 0.2265 0.0196  0.0321  0.0508  35   ILE A C   
160   O O   . ILE A 37   ? 0.2067 0.2438 0.2293 0.0190  0.0315  0.0523  35   ILE A O   
161   C CB  . ILE A 37   ? 0.1905 0.2212 0.2183 0.0177  0.0309  0.0479  35   ILE A CB  
162   C CG1 . ILE A 37   ? 0.1955 0.2239 0.2289 0.0156  0.0305  0.0499  35   ILE A CG1 
163   C CG2 . ILE A 37   ? 0.1848 0.2078 0.2102 0.0174  0.0293  0.0447  35   ILE A CG2 
164   C CD1 . ILE A 37   ? 0.2145 0.2384 0.2476 0.0157  0.0296  0.0456  35   ILE A CD1 
165   N N   . THR A 38   ? 0.2086 0.2525 0.2276 0.0221  0.0328  0.0471  36   THR A N   
166   C CA  . THR A 38   ? 0.2087 0.2543 0.2228 0.0240  0.0327  0.0443  36   THR A CA  
167   C C   . THR A 38   ? 0.2229 0.2753 0.2366 0.0240  0.0336  0.0491  36   THR A C   
168   O O   . THR A 38   ? 0.2225 0.2732 0.2336 0.0243  0.0329  0.0486  36   THR A O   
169   C CB  . THR A 38   ? 0.2164 0.2664 0.2275 0.0268  0.0332  0.0395  36   THR A CB  
170   O OG1 . THR A 38   ? 0.2333 0.2771 0.2458 0.0265  0.0322  0.0360  36   THR A OG1 
171   C CG2 . THR A 38   ? 0.2465 0.2970 0.2529 0.0287  0.0326  0.0357  36   THR A CG2 
172   N N   . ALA A 39   ? 0.2114 0.2716 0.2278 0.0236  0.0350  0.0540  37   ALA A N   
173   C CA  . ALA A 39   ? 0.2291 0.2969 0.2455 0.0235  0.0359  0.0594  37   ALA A CA  
174   C C   . ALA A 39   ? 0.2624 0.3240 0.2814 0.0213  0.0347  0.0631  37   ALA A C   
175   O O   . ALA A 39   ? 0.2672 0.3330 0.2850 0.0216  0.0348  0.0662  37   ALA A O   
176   C CB  . ALA A 39   ? 0.2419 0.3194 0.2614 0.0231  0.0376  0.0646  37   ALA A CB  
177   N N   . ALA A 40   ? 0.2200 0.2722 0.2428 0.0193  0.0334  0.0627  38   ALA A N   
178   C CA  . ALA A 40   ? 0.2402 0.2864 0.2664 0.0173  0.0320  0.0657  38   ALA A CA  
179   C C   . ALA A 40   ? 0.2316 0.2704 0.2543 0.0178  0.0306  0.0610  38   ALA A C   
180   O O   . ALA A 40   ? 0.2391 0.2730 0.2643 0.0165  0.0294  0.0628  38   ALA A O   
181   C CB  . ALA A 40   ? 0.2204 0.2608 0.2530 0.0149  0.0312  0.0673  38   ALA A CB  
182   N N   . TYR A 41   ? 0.2206 0.2586 0.2381 0.0197  0.0306  0.0552  39   TYR A N   
183   C CA  . TYR A 41   ? 0.2093 0.2396 0.2241 0.0199  0.0292  0.0505  39   TYR A CA  
184   C C   . TYR A 41   ? 0.2233 0.2523 0.2378 0.0195  0.0285  0.0526  39   TYR A C   
185   O O   . TYR A 41   ? 0.2223 0.2440 0.2386 0.0182  0.0271  0.0518  39   TYR A O   
186   C CB  . TYR A 41   ? 0.2131 0.2453 0.2226 0.0223  0.0294  0.0450  39   TYR A CB  
187   C CG  . TYR A 41   ? 0.2036 0.2278 0.2108 0.0224  0.0280  0.0395  39   TYR A CG  
188   C CD1 . TYR A 41   ? 0.2209 0.2381 0.2287 0.0210  0.0267  0.0392  39   TYR A CD1 
189   C CD2 . TYR A 41   ? 0.2315 0.2557 0.2364 0.0239  0.0279  0.0347  39   TYR A CD2 
190   C CE1 . TYR A 41   ? 0.2193 0.2303 0.2251 0.0211  0.0254  0.0345  39   TYR A CE1 
191   C CE2 . TYR A 41   ? 0.2226 0.2400 0.2259 0.0239  0.0265  0.0303  39   TYR A CE2 
192   C CZ  . TYR A 41   ? 0.2262 0.2373 0.2298 0.0224  0.0253  0.0304  39   TYR A CZ  
193   O OH  . TYR A 41   ? 0.2331 0.2382 0.2352 0.0223  0.0240  0.0264  39   TYR A OH  
194   N N   . ARG A 42   ? 0.2294 0.2660 0.2419 0.0207  0.0293  0.0553  40   ARG A N   
195   C CA  . ARG A 42   ? 0.2448 0.2809 0.2570 0.0205  0.0285  0.0574  40   ARG A CA  
196   C C   . ARG A 42   ? 0.2248 0.2682 0.2402 0.0199  0.0293  0.0647  40   ARG A C   
197   O O   . ARG A 42   ? 0.2787 0.3266 0.2922 0.0206  0.0293  0.0671  40   ARG A O   
198   C CB  . ARG A 42   ? 0.2684 0.3061 0.2746 0.0226  0.0283  0.0531  40   ARG A CB  
199   C CG  . ARG A 42   ? 0.2737 0.3034 0.2778 0.0227  0.0273  0.0467  40   ARG A CG  
200   C CD  . ARG A 42   ? 0.2774 0.3088 0.2762 0.0247  0.0270  0.0422  40   ARG A CD  
201   N NE  . ARG A 42   ? 0.2573 0.2824 0.2549 0.0249  0.0262  0.0366  40   ARG A NE  
202   C CZ  . ARG A 42   ? 0.2529 0.2699 0.2509 0.0237  0.0248  0.0344  40   ARG A CZ  
203   N NH1 . ARG A 42   ? 0.2609 0.2749 0.2601 0.0226  0.0241  0.0364  40   ARG A NH1 
204   N NH2 . ARG A 42   ? 0.2352 0.2474 0.2327 0.0236  0.0242  0.0303  40   ARG A NH2 
205   N N   . ARG A 43   ? 0.2469 0.2914 0.2672 0.0184  0.0298  0.0686  41   ARG A N   
206   C CA  . ARG A 43   ? 0.2409 0.2927 0.2653 0.0175  0.0305  0.0763  41   ARG A CA  
207   C C   . ARG A 43   ? 0.2793 0.3277 0.3069 0.0164  0.0290  0.0800  41   ARG A C   
208   O O   . ARG A 43   ? 0.2610 0.3000 0.2911 0.0154  0.0275  0.0777  41   ARG A O   
209   C CB  . ARG A 43   ? 0.2425 0.2937 0.2729 0.0157  0.0308  0.0793  41   ARG A CB  
210   C CG  . ARG A 43   ? 0.2634 0.3214 0.2993 0.0143  0.0313  0.0879  41   ARG A CG  
211   C CD  . ARG A 43   ? 0.3028 0.3620 0.3435 0.0129  0.0319  0.0899  41   ARG A CD  
212   N NE  . ARG A 43   ? 0.2722 0.3382 0.3081 0.0147  0.0337  0.0868  41   ARG A NE  
213   C CZ  . ARG A 43   ? 0.2349 0.3001 0.2724 0.0144  0.0342  0.0850  41   ARG A CZ  
214   N NH1 . ARG A 43   ? 0.2654 0.3234 0.3089 0.0122  0.0331  0.0856  41   ARG A NH1 
215   N NH2 . ARG A 43   ? 0.2694 0.3415 0.3027 0.0163  0.0358  0.0822  41   ARG A NH2 
216   N N   . PRO A 44   ? 0.2805 0.3366 0.3084 0.0167  0.0295  0.0857  42   PRO A N   
217   C CA  . PRO A 44   ? 0.2712 0.3241 0.3029 0.0157  0.0279  0.0897  42   PRO A CA  
218   C C   . PRO A 44   ? 0.2137 0.2590 0.2540 0.0132  0.0265  0.0922  42   PRO A C   
219   O O   . PRO A 44   ? 0.2587 0.3051 0.3034 0.0119  0.0270  0.0947  42   PRO A O   
220   C CB  . PRO A 44   ? 0.2640 0.3286 0.2958 0.0161  0.0289  0.0968  42   PRO A CB  
221   C CG  . PRO A 44   ? 0.3467 0.4198 0.3712 0.0183  0.0307  0.0934  42   PRO A CG  
222   C CD  . PRO A 44   ? 0.3140 0.3826 0.3383 0.0182  0.0313  0.0883  42   PRO A CD  
223   N N   . GLU A 45   ? 0.2705 0.3080 0.3133 0.0127  0.0247  0.0910  43   GLU A N   
224   C CA  . GLU A 45   ? 0.2806 0.3101 0.3316 0.0106  0.0230  0.0919  43   GLU A CA  
225   C C   . GLU A 45   ? 0.2572 0.2906 0.3164 0.0088  0.0227  0.1004  43   GLU A C   
226   O O   . GLU A 45   ? 0.2811 0.3107 0.3471 0.0071  0.0221  0.1014  43   GLU A O   
227   C CB  . GLU A 45   ? 0.2963 0.3182 0.3480 0.0108  0.0212  0.0889  43   GLU A CB  
228   C CG  . GLU A 45   ? 0.3235 0.3359 0.3800 0.0095  0.0196  0.0849  43   GLU A CG  
229   C CD  . GLU A 45   ? 0.2689 0.2746 0.3231 0.0103  0.0183  0.0793  43   GLU A CD  
230   O OE1 . GLU A 45   ? 0.2587 0.2664 0.3066 0.0118  0.0187  0.0774  43   GLU A OE1 
231   O OE2 . GLU A 45   ? 0.2538 0.2526 0.3130 0.0093  0.0169  0.0767  43   GLU A OE2 
232   N N   . THR A 46   ? 0.3106 0.3521 0.3698 0.0092  0.0232  0.1068  44   THR A N   
233   C CA  . THR A 46   ? 0.3136 0.3598 0.3808 0.0074  0.0229  0.1158  44   THR A CA  
234   C C   . THR A 46   ? 0.3073 0.3594 0.3755 0.0066  0.0246  0.1179  44   THR A C   
235   O O   . THR A 46   ? 0.3315 0.3850 0.4080 0.0045  0.0241  0.1244  44   THR A O   
236   C CB  . THR A 46   ? 0.2978 0.3529 0.3637 0.0081  0.0232  0.1223  44   THR A CB  
237   O OG1 . THR A 46   ? 0.3361 0.3998 0.3923 0.0102  0.0254  0.1198  44   THR A OG1 
238   C CG2 . THR A 46   ? 0.3005 0.3498 0.3674 0.0085  0.0212  0.1215  44   THR A CG2 
239   N N   . GLU A 47   ? 0.2814 0.3370 0.3418 0.0082  0.0265  0.1128  45   GLU A N   
240   C CA  . GLU A 47   ? 0.2991 0.3601 0.3601 0.0077  0.0281  0.1140  45   GLU A CA  
241   C C   . GLU A 47   ? 0.2516 0.3036 0.3159 0.0066  0.0274  0.1093  45   GLU A C   
242   O O   . GLU A 47   ? 0.2861 0.3406 0.3548 0.0052  0.0280  0.1120  45   GLU A O   
243   C CB  . GLU A 47   ? 0.3164 0.3860 0.3680 0.0102  0.0304  0.1106  45   GLU A CB  
244   C CG  . GLU A 47   ? 0.4058 0.4870 0.4547 0.0112  0.0314  0.1161  45   GLU A CG  
245   C CD  . GLU A 47   ? 0.4589 0.5481 0.4983 0.0141  0.0332  0.1113  45   GLU A CD  
246   O OE1 . GLU A 47   ? 0.4554 0.5437 0.4918 0.0149  0.0342  0.1058  45   GLU A OE1 
247   O OE2 . GLU A 47   ? 0.5807 0.6769 0.6158 0.0155  0.0336  0.1129  45   GLU A OE2 
248   N N   . CYS A 48   ? 0.2411 0.2834 0.3036 0.0070  0.0261  0.1024  46   CYS A N   
249   C CA  . CYS A 48   ? 0.2480 0.2825 0.3130 0.0060  0.0254  0.0977  46   CYS A CA  
250   C C   . CYS A 48   ? 0.2204 0.2496 0.2961 0.0036  0.0234  0.1013  46   CYS A C   
251   O O   . CYS A 48   ? 0.2434 0.2703 0.3233 0.0022  0.0232  0.1005  46   CYS A O   
252   C CB  . CYS A 48   ? 0.2475 0.2741 0.3075 0.0072  0.0245  0.0895  46   CYS A CB  
253   S SG  . CYS A 48   ? 0.2727 0.3031 0.3211 0.0100  0.0262  0.0837  46   CYS A SG  
254   N N   . LEU A 49   ? 0.2486 0.2756 0.3290 0.0029  0.0218  0.1049  47   LEU A N   
255   C CA  . LEU A 49   ? 0.2818 0.3017 0.3725 0.0009  0.0194  0.1065  47   LEU A CA  
256   C C   . LEU A 49   ? 0.2697 0.2930 0.3696 -0.0014 0.0192  0.1135  47   LEU A C   
257   O O   . LEU A 49   ? 0.2749 0.2925 0.3817 -0.0030 0.0178  0.1119  47   LEU A O   
258   C CB  . LEU A 49   ? 0.2968 0.3126 0.3905 0.0011  0.0175  0.1076  47   LEU A CB  
259   C CG  . LEU A 49   ? 0.2821 0.2888 0.3736 0.0019  0.0161  0.0993  47   LEU A CG  
260   C CD1 . LEU A 49   ? 0.2881 0.2879 0.3863 0.0004  0.0146  0.0959  47   LEU A CD1 
261   C CD2 . LEU A 49   ? 0.2780 0.2858 0.3579 0.0039  0.0179  0.0930  47   LEU A CD2 
262   N N   . PRO A 50   ? 0.2833 0.3160 0.3841 -0.0017 0.0204  0.1213  48   PRO A N   
263   C CA  . PRO A 50   ? 0.2863 0.3222 0.3972 -0.0042 0.0200  0.1289  48   PRO A CA  
264   C C   . PRO A 50   ? 0.2799 0.3146 0.3928 -0.0052 0.0205  0.1261  48   PRO A C   
265   O O   . PRO A 50   ? 0.3016 0.3317 0.4244 -0.0074 0.0186  0.1278  48   PRO A O   
266   C CB  . PRO A 50   ? 0.3150 0.3633 0.4233 -0.0039 0.0219  0.1367  48   PRO A CB  
267   C CG  . PRO A 50   ? 0.2806 0.3294 0.3823 -0.0019 0.0219  0.1351  48   PRO A CG  
268   C CD  . PRO A 50   ? 0.2693 0.3102 0.3635 -0.0001 0.0219  0.1245  48   PRO A CD  
269   N N   . PRO A 51   ? 0.2533 0.2919 0.3576 -0.0037 0.0227  0.1217  49   PRO A N   
270   C CA  . PRO A 51   ? 0.3093 0.3464 0.4160 -0.0047 0.0230  0.1190  49   PRO A CA  
271   C C   . PRO A 51   ? 0.2451 0.2709 0.3549 -0.0053 0.0208  0.1123  49   PRO A C   
272   O O   . PRO A 51   ? 0.2787 0.3020 0.3951 -0.0070 0.0199  0.1121  49   PRO A O   
273   C CB  . PRO A 51   ? 0.2779 0.3212 0.3743 -0.0026 0.0257  0.1152  49   PRO A CB  
274   C CG  . PRO A 51   ? 0.2821 0.3263 0.3701 -0.0003 0.0262  0.1127  49   PRO A CG  
275   C CD  . PRO A 51   ? 0.2912 0.3361 0.3842 -0.0011 0.0250  0.1191  49   PRO A CD  
276   N N   . LEU A 52   ? 0.2732 0.2928 0.3787 -0.0040 0.0198  0.1068  50   LEU A N   
277   C CA  . LEU A 52   ? 0.2608 0.2706 0.3692 -0.0044 0.0177  0.1004  50   LEU A CA  
278   C C   . LEU A 52   ? 0.2480 0.2531 0.3685 -0.0065 0.0150  0.1039  50   LEU A C   
279   O O   . LEU A 52   ? 0.2580 0.2581 0.3849 -0.0079 0.0134  0.1011  50   LEU A O   
280   C CB  . LEU A 52   ? 0.2299 0.2355 0.3305 -0.0024 0.0176  0.0942  50   LEU A CB  
281   C CG  . LEU A 52   ? 0.2558 0.2645 0.3448 -0.0003 0.0198  0.0896  50   LEU A CG  
282   C CD1 . LEU A 52   ? 0.2488 0.2537 0.3314 0.0014  0.0194  0.0848  50   LEU A CD1 
283   C CD2 . LEU A 52   ? 0.2533 0.2601 0.3408 -0.0005 0.0201  0.0846  50   LEU A CD2 
284   N N   . VAL A 53   ? 0.2586 0.2657 0.3830 -0.0068 0.0144  0.1100  51   VAL A N   
285   C CA  . VAL A 53   ? 0.2567 0.2599 0.3938 -0.0089 0.0116  0.1144  51   VAL A CA  
286   C C   . VAL A 53   ? 0.2570 0.2625 0.4025 -0.0112 0.0114  0.1186  51   VAL A C   
287   O O   . VAL A 53   ? 0.2900 0.2896 0.4451 -0.0128 0.0090  0.1170  51   VAL A O   
288   C CB  . VAL A 53   ? 0.2341 0.2408 0.3736 -0.0088 0.0112  0.1217  51   VAL A CB  
289   C CG1 . VAL A 53   ? 0.3121 0.3154 0.4660 -0.0111 0.0083  0.1273  51   VAL A CG1 
290   C CG2 . VAL A 53   ? 0.2989 0.3022 0.4313 -0.0066 0.0110  0.1169  51   VAL A CG2 
291   N N   . GLU A 54   ? 0.2768 0.2913 0.4191 -0.0114 0.0138  0.1235  52   GLU A N   
292   C CA  . GLU A 54   ? 0.2940 0.3115 0.4443 -0.0137 0.0138  0.1280  52   GLU A CA  
293   C C   . GLU A 54   ? 0.2783 0.2908 0.4288 -0.0140 0.0132  0.1206  52   GLU A C   
294   O O   . GLU A 54   ? 0.3001 0.3089 0.4609 -0.0161 0.0112  0.1213  52   GLU A O   
295   C CB  . GLU A 54   ? 0.3172 0.3465 0.4633 -0.0136 0.0167  0.1344  52   GLU A CB  
296   C CG  . GLU A 54   ? 0.3526 0.3857 0.5069 -0.0160 0.0168  0.1391  52   GLU A CG  
297   C CD  . GLU A 54   ? 0.4294 0.4587 0.5986 -0.0189 0.0137  0.1450  52   GLU A CD  
298   O OE1 . GLU A 54   ? 0.4712 0.5002 0.6445 -0.0192 0.0125  0.1501  52   GLU A OE1 
299   O OE2 . GLU A 54   ? 0.4559 0.4823 0.6331 -0.0208 0.0124  0.1445  52   GLU A OE2 
300   N N   . ALA A 55   ? 0.2611 0.2731 0.4006 -0.0119 0.0149  0.1134  53   ALA A N   
301   C CA  . ALA A 55   ? 0.2630 0.2711 0.4020 -0.0121 0.0145  0.1068  53   ALA A CA  
302   C C   . ALA A 55   ? 0.2479 0.2464 0.3929 -0.0128 0.0115  0.1013  53   ALA A C   
303   O O   . ALA A 55   ? 0.2809 0.2764 0.4307 -0.0139 0.0103  0.0981  53   ALA A O   
304   C CB  . ALA A 55   ? 0.2832 0.2931 0.4094 -0.0097 0.0168  0.1008  53   ALA A CB  
305   N N   . ALA A 56   ? 0.2619 0.2563 0.4071 -0.0120 0.0102  0.1002  54   ALA A N   
306   C CA  . ALA A 56   ? 0.2729 0.2588 0.4234 -0.0122 0.0073  0.0944  54   ALA A CA  
307   C C   . ALA A 56   ? 0.3140 0.2969 0.4788 -0.0143 0.0044  0.0989  54   ALA A C   
308   O O   . ALA A 56   ? 0.2970 0.2731 0.4678 -0.0145 0.0017  0.0940  54   ALA A O   
309   C CB  . ALA A 56   ? 0.2339 0.2167 0.3774 -0.0101 0.0073  0.0904  54   ALA A CB  
310   N N   . THR A 57   ? 0.3003 0.2883 0.4711 -0.0159 0.0048  0.1079  55   THR A N   
311   C CA  . THR A 57   ? 0.2916 0.2768 0.4769 -0.0180 0.0018  0.1129  55   THR A CA  
312   C C   . THR A 57   ? 0.3002 0.2815 0.4944 -0.0198 -0.0002 0.1094  55   THR A C   
313   O O   . THR A 57   ? 0.3276 0.3121 0.5189 -0.0203 0.0013  0.1084  55   THR A O   
314   C CB  . THR A 57   ? 0.3259 0.3188 0.5149 -0.0194 0.0030  0.1240  55   THR A CB  
315   O OG1 . THR A 57   ? 0.3271 0.3235 0.5087 -0.0177 0.0045  0.1270  55   THR A OG1 
316   C CG2 . THR A 57   ? 0.3402 0.3305 0.5455 -0.0221 -0.0002 0.1302  55   THR A CG2 
317   N N   . GLN A 58   ? 0.2953 0.2697 0.5004 -0.0207 -0.0038 0.1073  56   GLN A N   
318   C CA  . GLN A 58   ? 0.2893 0.2599 0.5045 -0.0224 -0.0062 0.1040  56   GLN A CA  
319   C C   . GLN A 58   ? 0.2746 0.2431 0.5054 -0.0244 -0.0096 0.1094  56   GLN A C   
320   O O   . GLN A 58   ? 0.3166 0.2863 0.5488 -0.0237 -0.0103 0.1133  56   GLN A O   
321   C CB  . GLN A 58   ? 0.2814 0.2460 0.4937 -0.0210 -0.0076 0.0927  56   GLN A CB  
322   C CG  . GLN A 58   ? 0.2921 0.2591 0.4890 -0.0190 -0.0046 0.0870  56   GLN A CG  
323   C CD  . GLN A 58   ? 0.2733 0.2358 0.4688 -0.0183 -0.0061 0.0767  56   GLN A CD  
324   O OE1 . GLN A 58   ? 0.3089 0.2714 0.5081 -0.0194 -0.0068 0.0740  56   GLN A OE1 
325   N NE2 . GLN A 58   ? 0.3090 0.2682 0.4994 -0.0163 -0.0065 0.0709  56   GLN A NE2 
326   N N   . SER A 59   ? 0.2946 0.2622 0.5348 -0.0260 -0.0118 0.1076  57   SER A N   
327   C CA  . SER A 59   ? 0.2812 0.2493 0.5342 -0.0271 -0.0152 0.1108  57   SER A CA  
328   C C   . SER A 59   ? 0.3625 0.3243 0.6209 -0.0258 -0.0185 0.1058  57   SER A C   
329   O O   . SER A 59   ? 0.3234 0.2797 0.5774 -0.0244 -0.0186 0.0980  57   SER A O   
330   C CB  . SER A 59   ? 0.3144 0.2822 0.5762 -0.0289 -0.0171 0.1089  57   SER A CB  
331   O OG  . SER A 59   ? 0.3623 0.3233 0.6259 -0.0284 -0.0190 0.0989  57   SER A OG  
332   N N   . LYS A 60   ? 0.3222 0.2853 0.5906 -0.0263 -0.0211 0.1103  58   LYS A N   
333   C CA  . LYS A 60   ? 0.3412 0.2989 0.6169 -0.0252 -0.0246 0.1057  58   LYS A CA  
334   C C   . LYS A 60   ? 0.3258 0.2773 0.6068 -0.0250 -0.0272 0.0956  58   LYS A C   
335   O O   . LYS A 60   ? 0.3471 0.2935 0.6272 -0.0234 -0.0285 0.0882  58   LYS A O   
336   C CB  . LYS A 60   ? 0.3686 0.3291 0.6560 -0.0262 -0.0272 0.1126  58   LYS A CB  
337   C CG  . LYS A 60   ? 0.3824 0.3380 0.6779 -0.0251 -0.0309 0.1086  58   LYS A CG  
338   C CD  . LYS A 60   ? 0.4779 0.4314 0.7637 -0.0230 -0.0293 0.1066  58   LYS A CD  
339   C CE  . LYS A 60   ? 0.5221 0.4735 0.8164 -0.0221 -0.0324 0.1065  58   LYS A CE  
340   N NZ  . LYS A 60   ? 0.5533 0.4990 0.8581 -0.0217 -0.0364 0.0981  58   LYS A NZ  
341   N N   . GLU A 61   ? 0.3362 0.2887 0.6228 -0.0266 -0.0280 0.0948  59   GLU A N   
342   C CA  . GLU A 61   ? 0.3446 0.2923 0.6363 -0.0265 -0.0305 0.0851  59   GLU A CA  
343   C C   . GLU A 61   ? 0.3645 0.3089 0.6449 -0.0251 -0.0285 0.0773  59   GLU A C   
344   O O   . GLU A 61   ? 0.3686 0.3084 0.6507 -0.0238 -0.0305 0.0685  59   GLU A O   
345   C CB  . GLU A 61   ? 0.3689 0.3190 0.6671 -0.0285 -0.0313 0.0864  59   GLU A CB  
346   N N   . ILE A 62   ? 0.3275 0.2748 0.5965 -0.0253 -0.0245 0.0806  60   ILE A N   
347   C CA  . ILE A 62   ? 0.3380 0.2824 0.5963 -0.0240 -0.0224 0.0740  60   ILE A CA  
348   C C   . ILE A 62   ? 0.3598 0.3010 0.6136 -0.0218 -0.0225 0.0714  60   ILE A C   
349   O O   . ILE A 62   ? 0.3559 0.2936 0.6064 -0.0203 -0.0232 0.0625  60   ILE A O   
350   C CB  . ILE A 62   ? 0.3197 0.2693 0.5664 -0.0244 -0.0181 0.0782  60   ILE A CB  
351   C CG1 . ILE A 62   ? 0.3435 0.2951 0.5935 -0.0262 -0.0183 0.0772  60   ILE A CG1 
352   C CG2 . ILE A 62   ? 0.3292 0.2797 0.5599 -0.0216 -0.0156 0.0717  60   ILE A CG2 
353   C CD1 . ILE A 62   ? 0.3845 0.3427 0.6231 -0.0261 -0.0143 0.0805  60   ILE A CD1 
354   N N   . ARG A 63   ? 0.3204 0.2641 0.5732 -0.0214 -0.0217 0.0787  61   ARG A N   
355   C CA  . ARG A 63   ? 0.3187 0.2598 0.5669 -0.0193 -0.0216 0.0768  61   ARG A CA  
356   C C   . ARG A 63   ? 0.3445 0.2808 0.6015 -0.0183 -0.0256 0.0691  61   ARG A C   
357   O O   . ARG A 63   ? 0.3158 0.2486 0.5683 -0.0164 -0.0257 0.0625  61   ARG A O   
358   C CB  . ARG A 63   ? 0.3380 0.2833 0.5843 -0.0193 -0.0203 0.0863  61   ARG A CB  
359   C CG  . ARG A 63   ? 0.3877 0.3379 0.6225 -0.0195 -0.0160 0.0920  61   ARG A CG  
360   C CD  . ARG A 63   ? 0.4454 0.4004 0.6768 -0.0191 -0.0145 0.1005  61   ARG A CD  
361   N NE  . ARG A 63   ? 0.4340 0.3941 0.6739 -0.0208 -0.0156 0.1082  61   ARG A NE  
362   C CZ  . ARG A 63   ? 0.4905 0.4503 0.7402 -0.0210 -0.0186 0.1106  61   ARG A CZ  
363   N NH1 . ARG A 63   ? 0.4859 0.4405 0.7381 -0.0195 -0.0208 0.1057  61   ARG A NH1 
364   N NH2 . ARG A 63   ? 0.4792 0.4443 0.7366 -0.0227 -0.0195 0.1182  61   ARG A NH2 
365   N N   . ASP A 64   ? 0.3575 0.2940 0.6273 -0.0194 -0.0289 0.0697  62   ASP A N   
366   C CA  . ASP A 64   ? 0.3625 0.2950 0.6414 -0.0183 -0.0328 0.0619  62   ASP A CA  
367   C C   . ASP A 64   ? 0.3343 0.2640 0.6113 -0.0177 -0.0334 0.0512  62   ASP A C   
368   O O   . ASP A 64   ? 0.3569 0.2836 0.6343 -0.0159 -0.0349 0.0431  62   ASP A O   
369   C CB  . ASP A 64   ? 0.3652 0.2989 0.6587 -0.0197 -0.0362 0.0653  62   ASP A CB  
370   C CG  . ASP A 64   ? 0.3785 0.3151 0.6752 -0.0201 -0.0362 0.0751  62   ASP A CG  
371   O OD1 . ASP A 64   ? 0.4003 0.3377 0.6881 -0.0191 -0.0339 0.0783  62   ASP A OD1 
372   O OD2 . ASP A 64   ? 0.4738 0.4122 0.7822 -0.0214 -0.0388 0.0796  62   ASP A OD2 
373   N N   . ALA A 65   ? 0.3123 0.2435 0.5875 -0.0192 -0.0322 0.0511  63   ALA A N   
374   C CA  . ALA A 65   ? 0.3385 0.2677 0.6115 -0.0188 -0.0327 0.0412  63   ALA A CA  
375   C C   . ALA A 65   ? 0.3601 0.2883 0.6200 -0.0170 -0.0300 0.0368  63   ALA A C   
376   O O   . ALA A 65   ? 0.3694 0.2966 0.6273 -0.0154 -0.0312 0.0271  63   ALA A O   
377   C CB  . ALA A 65   ? 0.3485 0.2801 0.6220 -0.0209 -0.0318 0.0428  63   ALA A CB  
378   N N   . ALA A 66   ? 0.3227 0.2545 0.5709 -0.0166 -0.0263 0.0431  64   ALA A N   
379   C CA  . ALA A 66   ? 0.3576 0.2913 0.5903 -0.0144 -0.0235 0.0390  64   ALA A CA  
380   C C   . ALA A 66   ? 0.3396 0.2699 0.5742 -0.0124 -0.0251 0.0350  64   ALA A C   
381   O O   . ALA A 66   ? 0.3342 0.2648 0.5617 -0.0106 -0.0248 0.0269  64   ALA A O   
382   C CB  . ALA A 66   ? 0.3203 0.2582 0.5419 -0.0144 -0.0196 0.0469  64   ALA A CB  
383   N N   . ALA A 67   ? 0.2991 0.2266 0.5433 -0.0128 -0.0269 0.0408  65   ALA A N   
384   C CA  . ALA A 67   ? 0.3512 0.2755 0.5983 -0.0109 -0.0287 0.0372  65   ALA A CA  
385   C C   . ALA A 67   ? 0.3309 0.2521 0.5861 -0.0101 -0.0321 0.0266  65   ALA A C   
386   O O   . ALA A 67   ? 0.3566 0.2774 0.6075 -0.0079 -0.0324 0.0194  65   ALA A O   
387   C CB  . ALA A 67   ? 0.3503 0.2746 0.6053 -0.0114 -0.0301 0.0453  65   ALA A CB  
388   N N   . SER A 68   ? 0.3515 0.2732 0.6162 -0.0115 -0.0345 0.0250  66   SER A N   
389   C CA  . SER A 68   ? 0.3804 0.3012 0.6520 -0.0105 -0.0377 0.0144  66   SER A CA  
390   C C   . SER A 68   ? 0.3849 0.3063 0.6469 -0.0096 -0.0362 0.0059  66   SER A C   
391   O O   . SER A 68   ? 0.3707 0.2920 0.6320 -0.0076 -0.0375 -0.0030 66   SER A O   
392   C CB  . SER A 68   ? 0.3832 0.3051 0.6666 -0.0122 -0.0405 0.0150  66   SER A CB  
393   O OG  . SER A 68   ? 0.4687 0.3905 0.7577 -0.0112 -0.0433 0.0042  66   SER A OG  
394   N N   . THR A 69   ? 0.3510 0.2764 0.6028 -0.0106 -0.0331 0.0086  67   THR A N   
395   C CA  . THR A 69   ? 0.3313 0.2607 0.5706 -0.0095 -0.0312 0.0014  67   THR A CA  
396   C C   . THR A 69   ? 0.3241 0.2548 0.5517 -0.0072 -0.0291 -0.0009 67   THR A C   
397   O O   . THR A 69   ? 0.3165 0.2491 0.5398 -0.0057 -0.0294 -0.0095 67   THR A O   
398   C CB  . THR A 69   ? 0.3318 0.2649 0.5629 -0.0110 -0.0283 0.0058  67   THR A CB  
399   O OG1 . THR A 69   ? 0.3204 0.2530 0.5622 -0.0129 -0.0305 0.0058  67   THR A OG1 
400   C CG2 . THR A 69   ? 0.2970 0.2345 0.5138 -0.0097 -0.0259 -0.0001 67   THR A CG2 
401   N N   . ALA A 70   ? 0.3433 0.2736 0.5658 -0.0071 -0.0269 0.0068  68   ALA A N   
402   C CA  . ALA A 70   ? 0.3272 0.2587 0.5390 -0.0050 -0.0250 0.0051  68   ALA A CA  
403   C C   . ALA A 70   ? 0.3508 0.2798 0.5695 -0.0033 -0.0278 -0.0017 68   ALA A C   
404   O O   . ALA A 70   ? 0.3404 0.2716 0.5517 -0.0015 -0.0271 -0.0084 68   ALA A O   
405   C CB  . ALA A 70   ? 0.3196 0.2512 0.5263 -0.0052 -0.0226 0.0147  68   ALA A CB  
406   N N   . ARG A 71   ? 0.3137 0.2384 0.5471 -0.0037 -0.0311 0.0001  69   ARG A N   
407   C CA  . ARG A 71   ? 0.3387 0.2609 0.5802 -0.0019 -0.0341 -0.0067 69   ARG A CA  
408   C C   . ARG A 71   ? 0.3671 0.2915 0.6095 -0.0010 -0.0357 -0.0181 69   ARG A C   
409   O O   . ARG A 71   ? 0.3639 0.2898 0.6032 0.0012  -0.0360 -0.0254 69   ARG A O   
410   C CB  . ARG A 71   ? 0.3657 0.2832 0.6240 -0.0027 -0.0377 -0.0025 69   ARG A CB  
411   C CG  . ARG A 71   ? 0.3989 0.3167 0.6662 -0.0010 -0.0413 -0.0108 69   ARG A CG  
412   C CD  . ARG A 71   ? 0.3858 0.3030 0.6655 -0.0016 -0.0441 -0.0054 69   ARG A CD  
413   N NE  . ARG A 71   ? 0.3830 0.2993 0.6598 -0.0012 -0.0429 0.0023  69   ARG A NE  
414   C CZ  . ARG A 71   ? 0.4419 0.3576 0.7172 0.0009  -0.0432 -0.0007 69   ARG A CZ  
415   N NH1 . ARG A 71   ? 0.4708 0.3871 0.7471 0.0029  -0.0447 -0.0112 69   ARG A NH1 
416   N NH2 . ARG A 71   ? 0.4811 0.3963 0.7538 0.0010  -0.0420 0.0070  69   ARG A NH2 
417   N N   . LYS A 72   ? 0.3396 0.2648 0.5859 -0.0025 -0.0366 -0.0198 70   LYS A N   
418   C CA  . LYS A 72   ? 0.3777 0.3060 0.6245 -0.0017 -0.0381 -0.0305 70   LYS A CA  
419   C C   . LYS A 72   ? 0.4067 0.3405 0.6370 -0.0005 -0.0349 -0.0346 70   LYS A C   
420   O O   . LYS A 72   ? 0.3638 0.3005 0.5928 0.0012  -0.0358 -0.0436 70   LYS A O   
421   C CB  . LYS A 72   ? 0.3591 0.2877 0.6121 -0.0039 -0.0393 -0.0302 70   LYS A CB  
422   C CG  . LYS A 72   ? 0.4098 0.3428 0.6612 -0.0033 -0.0403 -0.0405 70   LYS A CG  
423   C CD  . LYS A 72   ? 0.4513 0.3837 0.7119 -0.0054 -0.0423 -0.0406 70   LYS A CD  
424   C CE  . LYS A 72   ? 0.5090 0.4468 0.7665 -0.0049 -0.0431 -0.0504 70   LYS A CE  
425   N NZ  . LYS A 72   ? 0.6546 0.5944 0.9139 -0.0024 -0.0450 -0.0608 70   LYS A NZ  
426   N N   . LEU A 73   ? 0.3495 0.2853 0.5676 -0.0014 -0.0311 -0.0280 71   LEU A N   
427   C CA  . LEU A 73   ? 0.3323 0.2730 0.5352 -0.0003 -0.0281 -0.0308 71   LEU A CA  
428   C C   . LEU A 73   ? 0.3576 0.2984 0.5569 0.0018  -0.0278 -0.0331 71   LEU A C   
429   O O   . LEU A 73   ? 0.3600 0.3049 0.5529 0.0032  -0.0273 -0.0400 71   LEU A O   
430   C CB  . LEU A 73   ? 0.3400 0.2820 0.5320 -0.0015 -0.0245 -0.0226 71   LEU A CB  
431   C CG  . LEU A 73   ? 0.3374 0.2805 0.5305 -0.0035 -0.0242 -0.0202 71   LEU A CG  
432   C CD1 . LEU A 73   ? 0.3096 0.2536 0.4932 -0.0044 -0.0207 -0.0116 71   LEU A CD1 
433   C CD2 . LEU A 73   ? 0.3642 0.3119 0.5534 -0.0033 -0.0245 -0.0281 71   LEU A CD2 
434   N N   . ILE A 74   ? 0.3291 0.2658 0.5322 0.0020  -0.0279 -0.0271 72   ILE A N   
435   C CA  . ILE A 74   ? 0.3310 0.2676 0.5304 0.0039  -0.0274 -0.0285 72   ILE A CA  
436   C C   . ILE A 74   ? 0.3380 0.2746 0.5465 0.0057  -0.0307 -0.0379 72   ILE A C   
437   O O   . ILE A 74   ? 0.3500 0.2897 0.5527 0.0074  -0.0301 -0.0433 72   ILE A O   
438   C CB  . ILE A 74   ? 0.3322 0.2650 0.5335 0.0036  -0.0268 -0.0193 72   ILE A CB  
439   C CG1 . ILE A 74   ? 0.3577 0.2924 0.5473 0.0024  -0.0231 -0.0115 72   ILE A CG1 
440   C CG2 . ILE A 74   ? 0.3427 0.2749 0.5434 0.0057  -0.0272 -0.0212 72   ILE A CG2 
441   C CD1 . ILE A 74   ? 0.3836 0.3154 0.5762 0.0016  -0.0226 -0.0015 72   ILE A CD1 
442   N N   . GLU A 75   ? 0.3769 0.3102 0.5999 0.0052  -0.0343 -0.0400 73   GLU A N   
443   C CA  . GLU A 75   ? 0.3886 0.3223 0.6211 0.0070  -0.0376 -0.0498 73   GLU A CA  
444   C C   . GLU A 75   ? 0.4125 0.3528 0.6378 0.0078  -0.0371 -0.0592 73   GLU A C   
445   O O   . GLU A 75   ? 0.3951 0.3386 0.6195 0.0099  -0.0378 -0.0668 73   GLU A O   
446   C CB  . GLU A 75   ? 0.3988 0.3276 0.6488 0.0062  -0.0417 -0.0502 73   GLU A CB  
447   C CG  . GLU A 75   ? 0.4160 0.3394 0.6749 0.0060  -0.0430 -0.0425 73   GLU A CG  
448   C CD  . GLU A 75   ? 0.4798 0.4025 0.7518 0.0044  -0.0461 -0.0396 73   GLU A CD  
449   O OE1 . GLU A 75   ? 0.4964 0.4205 0.7715 0.0033  -0.0470 -0.0426 73   GLU A OE1 
450   O OE2 . GLU A 75   ? 0.4898 0.4107 0.7692 0.0044  -0.0476 -0.0342 73   GLU A OE2 
451   N N   . ALA A 76   ? 0.4029 0.3460 0.6227 0.0062  -0.0357 -0.0584 74   ALA A N   
452   C CA  . ALA A 76   ? 0.3898 0.3400 0.6016 0.0068  -0.0349 -0.0661 74   ALA A CA  
453   C C   . ALA A 76   ? 0.4265 0.3810 0.6241 0.0080  -0.0317 -0.0661 74   ALA A C   
454   O O   . ALA A 76   ? 0.4445 0.4045 0.6389 0.0095  -0.0320 -0.0740 74   ALA A O   
455   C CB  . ALA A 76   ? 0.3964 0.3485 0.6048 0.0048  -0.0340 -0.0640 74   ALA A CB  
456   N N   . LEU A 77   ? 0.4046 0.3570 0.5938 0.0072  -0.0288 -0.0572 75   LEU A N   
457   C CA  . LEU A 77   ? 0.3841 0.3400 0.5603 0.0081  -0.0258 -0.0566 75   LEU A CA  
458   C C   . LEU A 77   ? 0.4421 0.3984 0.6215 0.0103  -0.0271 -0.0616 75   LEU A C   
459   O O   . LEU A 77   ? 0.4626 0.4247 0.6358 0.0116  -0.0264 -0.0675 75   LEU A O   
460   C CB  . LEU A 77   ? 0.3891 0.3421 0.5579 0.0070  -0.0230 -0.0465 75   LEU A CB  
461   C CG  . LEU A 77   ? 0.4026 0.3574 0.5627 0.0053  -0.0205 -0.0420 75   LEU A CG  
462   C CD1 . LEU A 77   ? 0.3712 0.3233 0.5252 0.0047  -0.0180 -0.0327 75   LEU A CD1 
463   C CD2 . LEU A 77   ? 0.4030 0.3643 0.5527 0.0057  -0.0190 -0.0469 75   LEU A CD2 
464   N N   . ARG A 78   ? 0.3913 0.3419 0.5807 0.0108  -0.0290 -0.0590 76   ARG A N   
465   C CA  . ARG A 78   ? 0.4055 0.3560 0.5985 0.0130  -0.0302 -0.0631 76   ARG A CA  
466   C C   . ARG A 78   ? 0.4386 0.3927 0.6395 0.0146  -0.0331 -0.0743 76   ARG A C   
467   O O   . ARG A 78   ? 0.4832 0.4406 0.6832 0.0167  -0.0334 -0.0800 76   ARG A O   
468   C CB  . ARG A 78   ? 0.3455 0.2890 0.5478 0.0131  -0.0316 -0.0568 76   ARG A CB  
469   C CG  . ARG A 78   ? 0.3995 0.3413 0.5925 0.0122  -0.0285 -0.0469 76   ARG A CG  
470   C CD  . ARG A 78   ? 0.3698 0.3058 0.5714 0.0123  -0.0299 -0.0406 76   ARG A CD  
471   N NE  . ARG A 78   ? 0.3724 0.3084 0.5639 0.0123  -0.0270 -0.0334 76   ARG A NE  
472   C CZ  . ARG A 78   ? 0.3675 0.2996 0.5630 0.0124  -0.0274 -0.0267 76   ARG A CZ  
473   N NH1 . ARG A 78   ? 0.4150 0.3426 0.6249 0.0125  -0.0307 -0.0254 76   ARG A NH1 
474   N NH2 . ARG A 78   ? 0.4073 0.3405 0.5926 0.0125  -0.0247 -0.0211 76   ARG A NH2 
475   N N   . GLY A 79   ? 0.4222 0.3762 0.6307 0.0139  -0.0353 -0.0779 77   GLY A N   
476   C CA  . GLY A 79   ? 0.4513 0.4094 0.6675 0.0154  -0.0382 -0.0891 77   GLY A CA  
477   C C   . GLY A 79   ? 0.5159 0.4833 0.7216 0.0161  -0.0367 -0.0960 77   GLY A C   
478   O O   . GLY A 79   ? 0.5431 0.5154 0.7541 0.0176  -0.0389 -0.1060 77   GLY A O   
479   N N   . LYS A 80   ? 0.5379 0.5085 0.7292 0.0150  -0.0330 -0.0910 78   LYS A N   
480   C CA  . LYS A 80   ? 0.5552 0.5350 0.7361 0.0154  -0.0313 -0.0963 78   LYS A CA  
481   C C   . LYS A 80   ? 0.5658 0.5484 0.7336 0.0156  -0.0279 -0.0924 78   LYS A C   
482   O O   . LYS A 80   ? 0.6340 0.6239 0.7918 0.0153  -0.0261 -0.0943 78   LYS A O   
483   C CB  . LYS A 80   ? 0.5634 0.5457 0.7405 0.0134  -0.0307 -0.0952 78   LYS A CB  
484   C CG  . LYS A 80   ? 0.5713 0.5493 0.7409 0.0113  -0.0279 -0.0846 78   LYS A CG  
485   C CD  . LYS A 80   ? 0.4989 0.4783 0.6675 0.0095  -0.0279 -0.0837 78   LYS A CD  
486   C CE  . LYS A 80   ? 0.4411 0.4169 0.6019 0.0076  -0.0251 -0.0735 78   LYS A CE  
487   N NZ  . LYS A 80   ? 0.3790 0.3559 0.5396 0.0058  -0.0251 -0.0722 78   LYS A NZ  
488   N N   . HIS A 81   ? 0.5896 0.5668 0.7577 0.0160  -0.0272 -0.0868 79   HIS A N   
489   C CA  . HIS A 81   ? 0.6474 0.6262 0.8036 0.0160  -0.0240 -0.0823 79   HIS A CA  
490   C C   . HIS A 81   ? 0.7014 0.6892 0.8513 0.0174  -0.0233 -0.0892 79   HIS A C   
491   O O   . HIS A 81   ? 0.7565 0.7472 0.9129 0.0193  -0.0253 -0.0967 79   HIS A O   
492   C CB  . HIS A 81   ? 0.6388 0.6111 0.7987 0.0167  -0.0242 -0.0771 79   HIS A CB  
493   N N   . SER A 84   ? 0.5580 0.5654 0.6522 0.0160  -0.0099 -0.0752 82   SER A N   
494   C CA  . SER A 84   ? 0.5941 0.6069 0.6946 0.0179  -0.0117 -0.0838 82   SER A CA  
495   C C   . SER A 84   ? 0.5367 0.5603 0.6300 0.0180  -0.0105 -0.0876 82   SER A C   
496   O O   . SER A 84   ? 0.4908 0.5195 0.5867 0.0198  -0.0112 -0.0932 82   SER A O   
497   C CB  . SER A 84   ? 0.6093 0.6220 0.7187 0.0183  -0.0142 -0.0893 82   SER A CB  
498   N N   . GLY A 85   ? 0.5112 0.5385 0.5960 0.0162  -0.0088 -0.0843 83   GLY A N   
499   C CA  . GLY A 85   ? 0.4647 0.5024 0.5423 0.0159  -0.0075 -0.0864 83   GLY A CA  
500   C C   . GLY A 85   ? 0.3482 0.3865 0.4220 0.0164  -0.0062 -0.0843 83   GLY A C   
501   O O   . GLY A 85   ? 0.3645 0.4103 0.4393 0.0178  -0.0065 -0.0897 83   GLY A O   
502   N N   . VAL A 86   ? 0.3985 0.4297 0.4682 0.0154  -0.0048 -0.0767 84   VAL A N   
503   C CA  . VAL A 86   ? 0.3928 0.4238 0.4594 0.0158  -0.0037 -0.0745 84   VAL A CA  
504   C C   . VAL A 86   ? 0.3635 0.3923 0.4382 0.0181  -0.0053 -0.0788 84   VAL A C   
505   O O   . VAL A 86   ? 0.3163 0.3500 0.3905 0.0192  -0.0050 -0.0815 84   VAL A O   
506   C CB  . VAL A 86   ? 0.4409 0.4643 0.5022 0.0144  -0.0022 -0.0659 84   VAL A CB  
507   C CG1 . VAL A 86   ? 0.4168 0.4384 0.4768 0.0151  -0.0015 -0.0638 84   VAL A CG1 
508   C CG2 . VAL A 86   ? 0.4219 0.4489 0.4749 0.0123  -0.0006 -0.0621 84   VAL A CG2 
509   N N   . GLU A 87   ? 0.3966 0.4183 0.4795 0.0189  -0.0070 -0.0794 85   GLU A N   
510   C CA  . GLU A 87   ? 0.3992 0.4182 0.4911 0.0211  -0.0089 -0.0832 85   GLU A CA  
511   C C   . GLU A 87   ? 0.3982 0.4263 0.4940 0.0229  -0.0101 -0.0925 85   GLU A C   
512   O O   . GLU A 87   ? 0.3977 0.4276 0.4966 0.0246  -0.0106 -0.0957 85   GLU A O   
513   C CB  . GLU A 87   ? 0.4514 0.4616 0.5520 0.0213  -0.0108 -0.0819 85   GLU A CB  
514   N N   . GLY A 88   ? 0.3852 0.4196 0.4810 0.0225  -0.0106 -0.0972 86   GLY A N   
515   C CA  . GLY A 88   ? 0.3336 0.3780 0.4328 0.0244  -0.0118 -0.1065 86   GLY A CA  
516   C C   . GLY A 88   ? 0.3190 0.3730 0.4106 0.0243  -0.0099 -0.1072 86   GLY A C   
517   O O   . GLY A 88   ? 0.3629 0.4237 0.4579 0.0263  -0.0106 -0.1139 86   GLY A O   
518   N N   . LEU A 89   ? 0.3274 0.3824 0.4091 0.0221  -0.0075 -0.1005 87   LEU A N   
519   C CA  . LEU A 89   ? 0.3356 0.3992 0.4102 0.0217  -0.0057 -0.0999 87   LEU A CA  
520   C C   . LEU A 89   ? 0.2962 0.3562 0.3726 0.0229  -0.0055 -0.0988 87   LEU A C   
521   O O   . LEU A 89   ? 0.2829 0.3507 0.3599 0.0243  -0.0055 -0.1034 87   LEU A O   
522   C CB  . LEU A 89   ? 0.3282 0.3919 0.3930 0.0189  -0.0036 -0.0922 87   LEU A CB  
523   C CG  . LEU A 89   ? 0.3880 0.4627 0.4448 0.0177  -0.0018 -0.0914 87   LEU A CG  
524   C CD1 . LEU A 89   ? 0.4095 0.4819 0.4587 0.0149  -0.0003 -0.0835 87   LEU A CD1 
525   C CD2 . LEU A 89   ? 0.4166 0.4935 0.4724 0.0184  -0.0010 -0.0910 87   LEU A CD2 
526   N N   . VAL A 90   ? 0.3024 0.3511 0.3798 0.0225  -0.0055 -0.0926 88   VAL A N   
527   C CA  . VAL A 90   ? 0.3034 0.3480 0.3831 0.0238  -0.0055 -0.0912 88   VAL A CA  
528   C C   . VAL A 90   ? 0.3090 0.3560 0.3982 0.0266  -0.0077 -0.0992 88   VAL A C   
529   O O   . VAL A 90   ? 0.3051 0.3561 0.3949 0.0280  -0.0075 -0.1015 88   VAL A O   
530   C CB  . VAL A 90   ? 0.2925 0.3250 0.3727 0.0230  -0.0055 -0.0837 88   VAL A CB  
531   C CG1 . VAL A 90   ? 0.3217 0.3497 0.4063 0.0246  -0.0062 -0.0830 88   VAL A CG1 
532   C CG2 . VAL A 90   ? 0.3052 0.3363 0.3756 0.0205  -0.0033 -0.0762 88   VAL A CG2 
533   N N   . GLN A 91   ? 0.3374 0.3821 0.4346 0.0277  -0.0098 -0.1037 89   GLN A N   
534   C CA  . GLN A 91   ? 0.3276 0.3739 0.4351 0.0305  -0.0122 -0.1118 89   GLN A CA  
535   C C   . GLN A 91   ? 0.3418 0.4018 0.4481 0.0318  -0.0120 -0.1199 89   GLN A C   
536   O O   . GLN A 91   ? 0.3642 0.4280 0.4748 0.0340  -0.0127 -0.1247 89   GLN A O   
537   C CB  . GLN A 91   ? 0.3529 0.3936 0.4696 0.0311  -0.0147 -0.1147 89   GLN A CB  
538   N N   . GLU A 92   ? 0.3191 0.3871 0.4196 0.0304  -0.0111 -0.1213 90   GLU A N   
539   C CA  . GLU A 92   ? 0.3125 0.3947 0.4122 0.0317  -0.0110 -0.1293 90   GLU A CA  
540   C C   . GLU A 92   ? 0.3008 0.3898 0.3951 0.0318  -0.0091 -0.1280 90   GLU A C   
541   O O   . GLU A 92   ? 0.3182 0.4161 0.4159 0.0340  -0.0097 -0.1353 90   GLU A O   
542   C CB  . GLU A 92   ? 0.3305 0.4203 0.4242 0.0299  -0.0101 -0.1296 90   GLU A CB  
543   C CG  . GLU A 92   ? 0.3395 0.4457 0.4300 0.0306  -0.0095 -0.1361 90   GLU A CG  
544   C CD  . GLU A 92   ? 0.3979 0.5120 0.4836 0.0290  -0.0091 -0.1369 90   GLU A CD  
545   O OE1 . GLU A 92   ? 0.4408 0.5471 0.5254 0.0273  -0.0092 -0.1323 90   GLU A OE1 
546   O OE2 . GLU A 92   ? 0.4545 0.5829 0.5373 0.0295  -0.0086 -0.1420 90   GLU A OE2 
547   N N   . TYR A 93   ? 0.2821 0.3673 0.3683 0.0295  -0.0070 -0.1192 91   TYR A N   
548   C CA  . TYR A 93   ? 0.2878 0.3792 0.3685 0.0292  -0.0052 -0.1172 91   TYR A CA  
549   C C   . TYR A 93   ? 0.2755 0.3582 0.3589 0.0301  -0.0054 -0.1138 91   TYR A C   
550   O O   . TYR A 93   ? 0.2792 0.3652 0.3577 0.0295  -0.0038 -0.1108 91   TYR A O   
551   C CB  . TYR A 93   ? 0.2919 0.3869 0.3618 0.0260  -0.0028 -0.1103 91   TYR A CB  
552   C CG  . TYR A 93   ? 0.2663 0.3733 0.3331 0.0254  -0.0025 -0.1142 91   TYR A CG  
553   C CD1 . TYR A 93   ? 0.2810 0.4025 0.3458 0.0260  -0.0017 -0.1188 91   TYR A CD1 
554   C CD2 . TYR A 93   ? 0.2880 0.3925 0.3543 0.0242  -0.0030 -0.1133 91   TYR A CD2 
555   C CE1 . TYR A 93   ? 0.2899 0.4235 0.3519 0.0254  -0.0015 -0.1223 91   TYR A CE1 
556   C CE2 . TYR A 93   ? 0.3289 0.4449 0.3923 0.0237  -0.0028 -0.1169 91   TYR A CE2 
557   C CZ  . TYR A 93   ? 0.2896 0.4203 0.3509 0.0243  -0.0021 -0.1213 91   TYR A CZ  
558   O OH  . TYR A 93   ? 0.3960 0.5392 0.4544 0.0237  -0.0019 -0.1247 91   TYR A OH  
559   N N   . SER A 94   ? 0.2691 0.3413 0.3604 0.0314  -0.0073 -0.1140 92   SER A N   
560   C CA  . SER A 94   ? 0.2651 0.3290 0.3599 0.0325  -0.0078 -0.1107 92   SER A CA  
561   C C   . SER A 94   ? 0.2441 0.3041 0.3300 0.0301  -0.0056 -0.1016 92   SER A C   
562   O O   . SER A 94   ? 0.2788 0.3397 0.3634 0.0306  -0.0049 -0.1000 92   SER A O   
563   C CB  . SER A 94   ? 0.2845 0.3547 0.3850 0.0353  -0.0087 -0.1176 92   SER A CB  
564   O OG  . SER A 94   ? 0.3071 0.3823 0.4155 0.0375  -0.0108 -0.1269 92   SER A OG  
565   N N   . LEU A 95   ? 0.2359 0.2921 0.3161 0.0277  -0.0045 -0.0959 93   LEU A N   
566   C CA  . LEU A 95   ? 0.2556 0.3085 0.3275 0.0254  -0.0026 -0.0877 93   LEU A CA  
567   C C   . LEU A 95   ? 0.2428 0.2842 0.3172 0.0257  -0.0031 -0.0824 93   LEU A C   
568   O O   . LEU A 95   ? 0.2490 0.2830 0.3296 0.0265  -0.0047 -0.0824 93   LEU A O   
569   C CB  . LEU A 95   ? 0.2112 0.2637 0.2767 0.0229  -0.0015 -0.0837 93   LEU A CB  
570   C CG  . LEU A 95   ? 0.2363 0.3004 0.2983 0.0221  -0.0008 -0.0875 93   LEU A CG  
571   C CD1 . LEU A 95   ? 0.2509 0.3133 0.3064 0.0194  0.0003  -0.0820 93   LEU A CD1 
572   C CD2 . LEU A 95   ? 0.2387 0.3131 0.2970 0.0221  0.0004  -0.0890 93   LEU A CD2 
573   N N   . SER A 96   ? 0.2148 0.2551 0.2846 0.0251  -0.0019 -0.0778 94   SER A N   
574   C CA  . SER A 96   ? 0.2183 0.2485 0.2882 0.0248  -0.0020 -0.0714 94   SER A CA  
575   C C   . SER A 96   ? 0.2198 0.2453 0.2843 0.0225  -0.0010 -0.0657 94   SER A C   
576   O O   . SER A 96   ? 0.2176 0.2477 0.2775 0.0210  -0.0001 -0.0661 94   SER A O   
577   C CB  . SER A 96   ? 0.2117 0.2428 0.2777 0.0246  -0.0010 -0.0683 94   SER A CB  
578   O OG  . SER A 96   ? 0.2113 0.2466 0.2686 0.0223  0.0009  -0.0651 94   SER A OG  
579   N N   . SER A 97   ? 0.2273 0.2439 0.2924 0.0223  -0.0012 -0.0603 95   SER A N   
580   C CA  . SER A 97   ? 0.2327 0.2449 0.2926 0.0203  -0.0002 -0.0548 95   SER A CA  
581   C C   . SER A 97   ? 0.2174 0.2336 0.2683 0.0183  0.0016  -0.0518 95   SER A C   
582   O O   . SER A 97   ? 0.2084 0.2262 0.2551 0.0167  0.0024  -0.0506 95   SER A O   
583   C CB  . SER A 97   ? 0.2823 0.2855 0.3439 0.0205  -0.0006 -0.0493 95   SER A CB  
584   O OG  . SER A 97   ? 0.3605 0.3595 0.4304 0.0217  -0.0024 -0.0511 95   SER A OG  
585   N N   . GLN A 98   ? 0.1897 0.2076 0.2381 0.0184  0.0022  -0.0506 96   GLN A N   
586   C CA  . GLN A 98   ? 0.1826 0.2042 0.2235 0.0164  0.0038  -0.0476 96   GLN A CA  
587   C C   . GLN A 98   ? 0.1733 0.2041 0.2121 0.0156  0.0043  -0.0512 96   GLN A C   
588   O O   . GLN A 98   ? 0.1795 0.2127 0.2129 0.0136  0.0053  -0.0484 96   GLN A O   
589   C CB  . GLN A 98   ? 0.1789 0.2010 0.2181 0.0167  0.0041  -0.0459 96   GLN A CB  
590   C CG  . GLN A 98   ? 0.2175 0.2313 0.2564 0.0170  0.0039  -0.0410 96   GLN A CG  
591   C CD  . GLN A 98   ? 0.2019 0.2119 0.2351 0.0151  0.0049  -0.0359 96   GLN A CD  
592   O OE1 . GLN A 98   ? 0.2368 0.2432 0.2707 0.0147  0.0048  -0.0348 96   GLN A OE1 
593   N NE2 . GLN A 98   ? 0.2270 0.2379 0.2551 0.0138  0.0057  -0.0329 96   GLN A NE2 
594   N N   . GLU A 99   ? 0.1796 0.2164 0.2231 0.0172  0.0035  -0.0575 97   GLU A N   
595   C CA  . GLU A 99   ? 0.1693 0.2160 0.2110 0.0165  0.0039  -0.0612 97   GLU A CA  
596   C C   . GLU A 99   ? 0.1844 0.2301 0.2253 0.0155  0.0038  -0.0609 97   GLU A C   
597   O O   . GLU A 99   ? 0.1925 0.2438 0.2285 0.0137  0.0047  -0.0597 97   GLU A O   
598   C CB  . GLU A 99   ? 0.1647 0.2180 0.2122 0.0188  0.0030  -0.0685 97   GLU A CB  
599   C CG  . GLU A 99   ? 0.1761 0.2333 0.2231 0.0194  0.0034  -0.0689 97   GLU A CG  
600   C CD  . GLU A 99   ? 0.1873 0.2495 0.2412 0.0221  0.0022  -0.0762 97   GLU A CD  
601   O OE1 . GLU A 99   ? 0.2043 0.2659 0.2639 0.0236  0.0008  -0.0811 97   GLU A OE1 
602   O OE2 . GLU A 99   ? 0.1964 0.2632 0.2503 0.0228  0.0025  -0.0773 97   GLU A OE2 
603   N N   . GLY A 100  ? 0.1743 0.2129 0.2201 0.0165  0.0026  -0.0616 98   GLY A N   
604   C CA  . GLY A 100  ? 0.1817 0.2189 0.2269 0.0155  0.0025  -0.0610 98   GLY A CA  
605   C C   . GLY A 100  ? 0.1987 0.2330 0.2370 0.0132  0.0038  -0.0543 98   GLY A C   
606   O O   . GLY A 100  ? 0.1906 0.2289 0.2255 0.0117  0.0043  -0.0538 98   GLY A O   
607   N N   . VAL A 101  ? 0.1784 0.2057 0.2148 0.0129  0.0043  -0.0493 99   VAL A N   
608   C CA  . VAL A 101  ? 0.1772 0.2014 0.2076 0.0109  0.0053  -0.0433 99   VAL A CA  
609   C C   . VAL A 101  ? 0.1858 0.2177 0.2109 0.0093  0.0063  -0.0424 99   VAL A C   
610   O O   . VAL A 101  ? 0.1866 0.2202 0.2080 0.0076  0.0068  -0.0400 99   VAL A O   
611   C CB  . VAL A 101  ? 0.1718 0.1883 0.2016 0.0112  0.0055  -0.0388 99   VAL A CB  
612   C CG1 . VAL A 101  ? 0.1955 0.2098 0.2192 0.0093  0.0065  -0.0334 99   VAL A CG1 
613   C CG2 . VAL A 101  ? 0.2103 0.2194 0.2452 0.0125  0.0046  -0.0386 99   VAL A CG2 
614   N N   . ALA A 102  ? 0.1763 0.2132 0.2013 0.0097  0.0065  -0.0442 100  ALA A N   
615   C CA  . ALA A 102  ? 0.1728 0.2176 0.1933 0.0080  0.0074  -0.0428 100  ALA A CA  
616   C C   . ALA A 102  ? 0.1829 0.2362 0.2026 0.0073  0.0074  -0.0455 100  ALA A C   
617   O O   . ALA A 102  ? 0.2002 0.2576 0.2157 0.0052  0.0081  -0.0423 100  ALA A O   
618   C CB  . ALA A 102  ? 0.1851 0.2345 0.2065 0.0088  0.0075  -0.0448 100  ALA A CB  
619   N N   . LEU A 103  ? 0.1658 0.2223 0.1900 0.0090  0.0066  -0.0514 101  LEU A N   
620   C CA  . LEU A 103  ? 0.1680 0.2331 0.1917 0.0085  0.0065  -0.0546 101  LEU A CA  
621   C C   . LEU A 103  ? 0.1971 0.2588 0.2183 0.0069  0.0066  -0.0509 101  LEU A C   
622   O O   . LEU A 103  ? 0.2111 0.2797 0.2288 0.0053  0.0070  -0.0496 101  LEU A O   
623   C CB  . LEU A 103  ? 0.1845 0.2521 0.2145 0.0109  0.0053  -0.0620 101  LEU A CB  
624   C CG  . LEU A 103  ? 0.1826 0.2593 0.2126 0.0107  0.0050  -0.0661 101  LEU A CG  
625   C CD1 . LEU A 103  ? 0.2211 0.3106 0.2469 0.0095  0.0060  -0.0664 101  LEU A CD1 
626   C CD2 . LEU A 103  ? 0.2169 0.2946 0.2541 0.0132  0.0035  -0.0738 101  LEU A CD2 
627   N N   . MET A 104  ? 0.1837 0.2351 0.2068 0.0074  0.0061  -0.0489 102  MET A N   
628   C CA  . MET A 104  ? 0.1788 0.2269 0.1996 0.0060  0.0062  -0.0456 102  MET A CA  
629   C C   . MET A 104  ? 0.1968 0.2443 0.2120 0.0039  0.0071  -0.0393 102  MET A C   
630   O O   . MET A 104  ? 0.2239 0.2739 0.2364 0.0023  0.0073  -0.0370 102  MET A O   
631   C CB  . MET A 104  ? 0.2128 0.2508 0.2373 0.0070  0.0055  -0.0449 102  MET A CB  
632   C CG  . MET A 104  ? 0.2274 0.2659 0.2585 0.0089  0.0043  -0.0511 102  MET A CG  
633   S SD  . MET A 104  ? 0.3154 0.3649 0.3475 0.0089  0.0036  -0.0570 102  MET A SD  
634   C CE  . MET A 104  ? 0.3166 0.3620 0.3465 0.0072  0.0036  -0.0531 102  MET A CE  
635   N N   . CYS A 105  ? 0.1905 0.2350 0.2042 0.0037  0.0076  -0.0365 103  CYS A N   
636   C CA  . CYS A 105  ? 0.2065 0.2507 0.2155 0.0017  0.0083  -0.0309 103  CYS A CA  
637   C C   . CYS A 105  ? 0.2406 0.2958 0.2472 0.0001  0.0086  -0.0309 103  CYS A C   
638   O O   . CYS A 105  ? 0.2578 0.3145 0.2613 -0.0018 0.0088  -0.0268 103  CYS A O   
639   C CB  . CYS A 105  ? 0.2179 0.2576 0.2264 0.0019  0.0086  -0.0286 103  CYS A CB  
640   S SG  . CYS A 105  ? 0.2291 0.2568 0.2396 0.0034  0.0083  -0.0272 103  CYS A SG  
641   N N   . LEU A 106  ? 0.2055 0.2687 0.2135 0.0009  0.0087  -0.0352 104  LEU A N   
642   C CA  . LEU A 106  ? 0.2294 0.3045 0.2352 -0.0005 0.0090  -0.0354 104  LEU A CA  
643   C C   . LEU A 106  ? 0.2477 0.3272 0.2529 -0.0011 0.0087  -0.0362 104  LEU A C   
644   O O   . LEU A 106  ? 0.2472 0.3326 0.2493 -0.0031 0.0089  -0.0326 104  LEU A O   
645   C CB  . LEU A 106  ? 0.2124 0.2958 0.2205 0.0010  0.0091  -0.0411 104  LEU A CB  
646   C CG  . LEU A 106  ? 0.2321 0.3297 0.2383 -0.0001 0.0095  -0.0422 104  LEU A CG  
647   C CD1 . LEU A 106  ? 0.2668 0.3676 0.2692 -0.0028 0.0101  -0.0358 104  LEU A CD1 
648   C CD2 . LEU A 106  ? 0.2467 0.3527 0.2558 0.0018  0.0095  -0.0490 104  LEU A CD2 
649   N N   . ALA A 107  ? 0.2128 0.2898 0.2213 0.0006  0.0080  -0.0407 105  ALA A N   
650   C CA  . ALA A 107  ? 0.2311 0.3122 0.2393 0.0002  0.0076  -0.0418 105  ALA A CA  
651   C C   . ALA A 107  ? 0.2785 0.3540 0.2837 -0.0017 0.0077  -0.0354 105  ALA A C   
652   O O   . ALA A 107  ? 0.2546 0.3366 0.2573 -0.0033 0.0076  -0.0333 105  ALA A O   
653   C CB  . ALA A 107  ? 0.2096 0.2874 0.2227 0.0023  0.0066  -0.0477 105  ALA A CB  
654   N N   . GLU A 108  ? 0.2430 0.3070 0.2485 -0.0015 0.0077  -0.0323 106  GLU A N   
655   C CA  . GLU A 108  ? 0.2724 0.3308 0.2755 -0.0030 0.0078  -0.0264 106  GLU A CA  
656   C C   . GLU A 108  ? 0.3089 0.3730 0.3084 -0.0053 0.0081  -0.0217 106  GLU A C   
657   O O   . GLU A 108  ? 0.3175 0.3840 0.3152 -0.0068 0.0079  -0.0184 106  GLU A O   
658   C CB  . GLU A 108  ? 0.2642 0.3109 0.2681 -0.0022 0.0079  -0.0242 106  GLU A CB  
659   C CG  . GLU A 108  ? 0.2950 0.3356 0.2967 -0.0035 0.0079  -0.0186 106  GLU A CG  
660   C CD  . GLU A 108  ? 0.3013 0.3329 0.3029 -0.0029 0.0082  -0.0161 106  GLU A CD  
661   O OE1 . GLU A 108  ? 0.3232 0.3512 0.3270 -0.0013 0.0082  -0.0186 106  GLU A OE1 
662   O OE2 . GLU A 108  ? 0.3296 0.3579 0.3292 -0.0041 0.0082  -0.0116 106  GLU A OE2 
663   N N   . ALA A 109  ? 0.2761 0.3430 0.2750 -0.0056 0.0085  -0.0211 107  ALA A N   
664   C CA  . ALA A 109  ? 0.2873 0.3595 0.2835 -0.0079 0.0087  -0.0163 107  ALA A CA  
665   C C   . ALA A 109  ? 0.3278 0.4128 0.3229 -0.0090 0.0087  -0.0168 107  ALA A C   
666   O O   . ALA A 109  ? 0.3511 0.4396 0.3443 -0.0112 0.0085  -0.0118 107  ALA A O   
667   C CB  . ALA A 109  ? 0.3375 0.4105 0.3338 -0.0079 0.0091  -0.0161 107  ALA A CB  
668   N N   . LEU A 110  ? 0.2883 0.3807 0.2847 -0.0076 0.0088  -0.0228 108  LEU A N   
669   C CA  . LEU A 110  ? 0.2568 0.3625 0.2520 -0.0085 0.0087  -0.0241 108  LEU A CA  
670   C C   . LEU A 110  ? 0.3406 0.4459 0.3350 -0.0091 0.0081  -0.0225 108  LEU A C   
671   O O   . LEU A 110  ? 0.3516 0.4664 0.3439 -0.0108 0.0080  -0.0200 108  LEU A O   
672   C CB  . LEU A 110  ? 0.2720 0.3849 0.2694 -0.0063 0.0088  -0.0320 108  LEU A CB  
673   C CG  . LEU A 110  ? 0.2891 0.4070 0.2868 -0.0060 0.0095  -0.0335 108  LEU A CG  
674   C CD1 . LEU A 110  ? 0.2604 0.3828 0.2615 -0.0033 0.0093  -0.0419 108  LEU A CD1 
675   C CD2 . LEU A 110  ? 0.3080 0.4385 0.3028 -0.0083 0.0100  -0.0296 108  LEU A CD2 
676   N N   . LEU A 111  ? 0.3095 0.4043 0.3055 -0.0079 0.0077  -0.0236 109  LEU A N   
677   C CA  . LEU A 111  ? 0.3508 0.4445 0.3464 -0.0085 0.0071  -0.0221 109  LEU A CA  
678   C C   . LEU A 111  ? 0.4179 0.5075 0.4115 -0.0106 0.0069  -0.0145 109  LEU A C   
679   O O   . LEU A 111  ? 0.4484 0.5389 0.4413 -0.0114 0.0064  -0.0124 109  LEU A O   
680   C CB  . LEU A 111  ? 0.3420 0.4265 0.3407 -0.0065 0.0067  -0.0259 109  LEU A CB  
681   C CG  . LEU A 111  ? 0.3126 0.4023 0.3143 -0.0046 0.0063  -0.0338 109  LEU A CG  
682   C CD1 . LEU A 111  ? 0.3538 0.4331 0.3595 -0.0028 0.0058  -0.0368 109  LEU A CD1 
683   C CD2 . LEU A 111  ? 0.3443 0.4458 0.3452 -0.0051 0.0058  -0.0362 109  LEU A CD2 
684   N N   . ARG A 112  ? 0.3847 0.4699 0.3776 -0.0114 0.0073  -0.0105 110  ARG A N   
685   C CA  . ARG A 112  ? 0.4426 0.5253 0.4341 -0.0135 0.0069  -0.0035 110  ARG A CA  
686   C C   . ARG A 112  ? 0.5087 0.6037 0.4985 -0.0157 0.0067  0.0000  110  ARG A C   
687   O O   . ARG A 112  ? 0.5553 0.6498 0.5445 -0.0176 0.0060  0.0059  110  ARG A O   
688   C CB  . ARG A 112  ? 0.4375 0.5115 0.4294 -0.0136 0.0071  -0.0008 110  ARG A CB  
689   C CG  . ARG A 112  ? 0.4264 0.4883 0.4197 -0.0116 0.0072  -0.0030 110  ARG A CG  
690   C CD  . ARG A 112  ? 0.4433 0.4992 0.4369 -0.0113 0.0075  -0.0021 110  ARG A CD  
691   N NE  . ARG A 112  ? 0.5499 0.6032 0.5429 -0.0131 0.0070  0.0036  110  ARG A NE  
692   C CZ  . ARG A 112  ? 0.6373 0.6814 0.6307 -0.0129 0.0066  0.0063  110  ARG A CZ  
693   N NH1 . ARG A 112  ? 0.6399 0.6767 0.6340 -0.0112 0.0067  0.0042  110  ARG A NH1 
694   N NH2 . ARG A 112  ? 0.6989 0.7412 0.6924 -0.0145 0.0059  0.0111  110  ARG A NH2 
695   N N   . ILE A 113  ? 0.4545 0.5608 0.4439 -0.0156 0.0071  -0.0035 111  ILE A N   
696   C CA  . ILE A 113  ? 0.4623 0.5824 0.4499 -0.0175 0.0070  -0.0008 111  ILE A CA  
697   C C   . ILE A 113  ? 0.5313 0.6558 0.5184 -0.0174 0.0064  -0.0018 111  ILE A C   
698   O O   . ILE A 113  ? 0.4928 0.6193 0.4806 -0.0155 0.0065  -0.0084 111  ILE A O   
699   C CB  . ILE A 113  ? 0.4368 0.5683 0.4241 -0.0171 0.0078  -0.0049 111  ILE A CB  
700   C CG1 . ILE A 113  ? 0.4473 0.5749 0.4352 -0.0175 0.0084  -0.0031 111  ILE A CG1 
701   C CG2 . ILE A 113  ? 0.4901 0.6375 0.4755 -0.0190 0.0078  -0.0025 111  ILE A CG2 
702   C CD1 . ILE A 113  ? 0.3883 0.5253 0.3764 -0.0165 0.0092  -0.0080 111  ILE A CD1 
703   N N   . PRO A 114  ? 0.5918 0.7180 0.5779 -0.0195 0.0056  0.0044  112  PRO A N   
704   C CA  . PRO A 114  ? 0.5857 0.7141 0.5715 -0.0192 0.0049  0.0036  112  PRO A CA  
705   C C   . PRO A 114  ? 0.5891 0.7329 0.5737 -0.0191 0.0050  -0.0004 112  PRO A C   
706   O O   . PRO A 114  ? 0.6310 0.7756 0.6162 -0.0176 0.0046  -0.0055 112  PRO A O   
707   C CB  . PRO A 114  ? 0.6240 0.7500 0.6097 -0.0215 0.0040  0.0119  112  PRO A CB  
708   C CG  . PRO A 114  ? 0.6436 0.7613 0.6302 -0.0223 0.0041  0.0160  112  PRO A CG  
709   C CD  . PRO A 114  ? 0.6126 0.7360 0.5987 -0.0218 0.0052  0.0124  112  PRO A CD  
710   N N   . ASP A 115  ? 0.5646 0.7211 0.5477 -0.0205 0.0053  0.0016  113  ASP A N   
711   C CA  . ASP A 115  ? 0.5821 0.7550 0.5637 -0.0205 0.0054  -0.0017 113  ASP A CA  
712   C C   . ASP A 115  ? 0.5543 0.7314 0.5368 -0.0181 0.0061  -0.0108 113  ASP A C   
713   O O   . ASP A 115  ? 0.5583 0.7345 0.5413 -0.0177 0.0069  -0.0118 113  ASP A O   
714   C CB  . ASP A 115  ? 0.5623 0.7484 0.5420 -0.0232 0.0054  0.0049  113  ASP A CB  
715   C CG  . ASP A 115  ? 0.6333 0.8381 0.6112 -0.0230 0.0057  0.0010  113  ASP A CG  
716   O OD1 . ASP A 115  ? 0.6431 0.8526 0.6204 -0.0224 0.0050  -0.0017 113  ASP A OD1 
717   O OD2 . ASP A 115  ? 0.6049 0.8200 0.5820 -0.0235 0.0065  0.0003  113  ASP A OD2 
718   N N   . THR A 116  ? 0.5499 0.7318 0.5329 -0.0163 0.0057  -0.0176 114  THR A N   
719   C CA  . THR A 116  ? 0.5043 0.6890 0.4892 -0.0137 0.0060  -0.0270 114  THR A CA  
720   C C   . THR A 116  ? 0.5465 0.7466 0.5302 -0.0139 0.0069  -0.0288 114  THR A C   
721   O O   . THR A 116  ? 0.5087 0.7079 0.4941 -0.0123 0.0075  -0.0338 114  THR A O   
722   C CB  . THR A 116  ? 0.5078 0.6952 0.4942 -0.0120 0.0051  -0.0336 114  THR A CB  
723   O OG1 . THR A 116  ? 0.5772 0.7503 0.5650 -0.0118 0.0044  -0.0318 114  THR A OG1 
724   C CG2 . THR A 116  ? 0.5252 0.7146 0.5147 -0.0091 0.0051  -0.0437 114  THR A CG2 
725   N N   . ALA A 117  ? 0.4945 0.7091 0.4753 -0.0160 0.0069  -0.0246 115  ALA A N   
726   C CA  . ALA A 117  ? 0.5240 0.7545 0.5034 -0.0163 0.0078  -0.0258 115  ALA A CA  
727   C C   . ALA A 117  ? 0.4835 0.7091 0.4631 -0.0175 0.0087  -0.0210 115  ALA A C   
728   O O   . ALA A 117  ? 0.4802 0.7117 0.4605 -0.0165 0.0095  -0.0252 115  ALA A O   
729   C CB  . ALA A 117  ? 0.5359 0.7834 0.5122 -0.0185 0.0075  -0.0213 115  ALA A CB  
730   N N   . THR A 118  ? 0.4902 0.7051 0.4696 -0.0196 0.0084  -0.0125 116  THR A N   
731   C CA  . THR A 118  ? 0.4994 0.7087 0.4794 -0.0208 0.0090  -0.0081 116  THR A CA  
732   C C   . THR A 118  ? 0.4418 0.6396 0.4242 -0.0181 0.0095  -0.0144 116  THR A C   
733   O O   . THR A 118  ? 0.4356 0.6355 0.4186 -0.0179 0.0103  -0.0154 116  THR A O   
734   C CB  . THR A 118  ? 0.4904 0.6892 0.4705 -0.0232 0.0083  0.0012  116  THR A CB  
735   O OG1 . THR A 118  ? 0.6025 0.8118 0.5808 -0.0256 0.0077  0.0075  116  THR A OG1 
736   C CG2 . THR A 118  ? 0.4980 0.6919 0.4790 -0.0246 0.0087  0.0058  116  THR A CG2 
737   N N   . ARG A 119  ? 0.4457 0.6317 0.4297 -0.0162 0.0089  -0.0185 117  ARG A N   
738   C CA  . ARG A 119  ? 0.4452 0.6203 0.4320 -0.0137 0.0091  -0.0241 117  ARG A CA  
739   C C   . ARG A 119  ? 0.4126 0.5979 0.4007 -0.0115 0.0096  -0.0326 117  ARG A C   
740   O O   . ARG A 119  ? 0.4178 0.6011 0.4074 -0.0105 0.0102  -0.0348 117  ARG A O   
741   C CB  . ARG A 119  ? 0.3967 0.5590 0.3852 -0.0122 0.0083  -0.0265 117  ARG A CB  
742   C CG  . ARG A 119  ? 0.3632 0.5130 0.3548 -0.0098 0.0084  -0.0310 117  ARG A CG  
743   C CD  . ARG A 119  ? 0.3957 0.5360 0.3894 -0.0083 0.0076  -0.0341 117  ARG A CD  
744   N NE  . ARG A 119  ? 0.4066 0.5410 0.3987 -0.0100 0.0071  -0.0277 117  ARG A NE  
745   C CZ  . ARG A 119  ? 0.4407 0.5766 0.4328 -0.0101 0.0064  -0.0285 117  ARG A CZ  
746   N NH1 . ARG A 119  ? 0.4144 0.5568 0.4082 -0.0084 0.0059  -0.0356 117  ARG A NH1 
747   N NH2 . ARG A 119  ? 0.5222 0.6529 0.5130 -0.0116 0.0060  -0.0223 117  ARG A NH2 
748   N N   . ASP A 120  ? 0.4266 0.6235 0.4144 -0.0106 0.0092  -0.0375 118  ASP A N   
749   C CA  . ASP A 120  ? 0.4321 0.6393 0.4216 -0.0083 0.0094  -0.0465 118  ASP A CA  
750   C C   . ASP A 120  ? 0.4418 0.6615 0.4298 -0.0093 0.0106  -0.0448 118  ASP A C   
751   O O   . ASP A 120  ? 0.4089 0.6316 0.3991 -0.0073 0.0110  -0.0508 118  ASP A O   
752   C CB  . ASP A 120  ? 0.4161 0.6343 0.4055 -0.0073 0.0087  -0.0519 118  ASP A CB  
753   C CG  . ASP A 120  ? 0.4824 0.6885 0.4740 -0.0061 0.0075  -0.0544 118  ASP A CG  
754   O OD1 . ASP A 120  ? 0.5031 0.6929 0.4965 -0.0058 0.0074  -0.0523 118  ASP A OD1 
755   O OD2 . ASP A 120  ? 0.5147 0.7282 0.5065 -0.0056 0.0067  -0.0583 118  ASP A OD2 
756   N N   . ALA A 121  ? 0.4580 0.6852 0.4427 -0.0124 0.0109  -0.0366 119  ALA A N   
757   C CA  . ALA A 121  ? 0.4320 0.6711 0.4156 -0.0138 0.0120  -0.0339 119  ALA A CA  
758   C C   . ALA A 121  ? 0.4386 0.6664 0.4238 -0.0137 0.0125  -0.0320 119  ALA A C   
759   O O   . ALA A 121  ? 0.4476 0.6818 0.4337 -0.0128 0.0133  -0.0353 119  ALA A O   
760   C CB  . ALA A 121  ? 0.4543 0.7028 0.4347 -0.0174 0.0121  -0.0245 119  ALA A CB  
761   N N   . LEU A 122  ? 0.4323 0.6435 0.4179 -0.0146 0.0120  -0.0268 120  LEU A N   
762   C CA  . LEU A 122  ? 0.4091 0.6090 0.3963 -0.0144 0.0123  -0.0253 120  LEU A CA  
763   C C   . LEU A 122  ? 0.4204 0.6160 0.4106 -0.0109 0.0124  -0.0343 120  LEU A C   
764   O O   . LEU A 122  ? 0.4057 0.6014 0.3972 -0.0103 0.0130  -0.0355 120  LEU A O   
765   C CB  . LEU A 122  ? 0.4542 0.6373 0.4415 -0.0156 0.0116  -0.0193 120  LEU A CB  
766   C CG  . LEU A 122  ? 0.4309 0.6034 0.4193 -0.0159 0.0119  -0.0163 120  LEU A CG  
767   C CD1 . LEU A 122  ? 0.5261 0.7080 0.5136 -0.0187 0.0124  -0.0104 120  LEU A CD1 
768   C CD2 . LEU A 122  ? 0.3930 0.5492 0.3817 -0.0164 0.0111  -0.0120 120  LEU A CD2 
769   N N   . ILE A 123  ? 0.4070 0.5989 0.3989 -0.0087 0.0117  -0.0405 121  ILE A N   
770   C CA  . ILE A 123  ? 0.4193 0.6070 0.4149 -0.0053 0.0115  -0.0490 121  ILE A CA  
771   C C   . ILE A 123  ? 0.4086 0.6120 0.4051 -0.0041 0.0121  -0.0548 121  ILE A C   
772   O O   . ILE A 123  ? 0.3890 0.5912 0.3877 -0.0027 0.0125  -0.0575 121  ILE A O   
773   C CB  . ILE A 123  ? 0.3687 0.5506 0.3665 -0.0034 0.0104  -0.0542 121  ILE A CB  
774   C CG1 . ILE A 123  ? 0.3630 0.5283 0.3608 -0.0042 0.0099  -0.0491 121  ILE A CG1 
775   C CG2 . ILE A 123  ? 0.3641 0.5452 0.3668 0.0001  0.0099  -0.0637 121  ILE A CG2 
776   C CD1 . ILE A 123  ? 0.3425 0.5030 0.3422 -0.0028 0.0088  -0.0530 121  ILE A CD1 
777   N N   . ARG A 124  ? 0.4122 0.6311 0.4069 -0.0045 0.0122  -0.0568 122  ARG A N   
778   C CA  . ARG A 124  ? 0.4173 0.6524 0.4129 -0.0028 0.0127  -0.0636 122  ARG A CA  
779   C C   . ARG A 124  ? 0.4833 0.7262 0.4775 -0.0045 0.0140  -0.0594 122  ARG A C   
780   O O   . ARG A 124  ? 0.4959 0.7440 0.4924 -0.0025 0.0144  -0.0649 122  ARG A O   
781   C CB  . ARG A 124  ? 0.4163 0.6672 0.4099 -0.0031 0.0125  -0.0661 122  ARG A CB  
782   N N   . ASP A 125  ? 0.4683 0.7120 0.4592 -0.0080 0.0145  -0.0496 123  ASP A N   
783   C CA  . ASP A 125  ? 0.5287 0.7825 0.5183 -0.0100 0.0156  -0.0450 123  ASP A CA  
784   C C   . ASP A 125  ? 0.5625 0.8033 0.5535 -0.0106 0.0158  -0.0411 123  ASP A C   
785   O O   . ASP A 125  ? 0.6105 0.8576 0.6023 -0.0105 0.0166  -0.0417 123  ASP A O   
786   C CB  . ASP A 125  ? 0.6179 0.8819 0.6038 -0.0137 0.0158  -0.0364 123  ASP A CB  
787   C CG  . ASP A 125  ? 0.6190 0.8976 0.6032 -0.0132 0.0156  -0.0399 123  ASP A CG  
788   O OD1 . ASP A 125  ? 0.6043 0.8941 0.5896 -0.0106 0.0159  -0.0487 123  ASP A OD1 
789   O OD2 . ASP A 125  ? 0.6070 0.8860 0.5889 -0.0154 0.0151  -0.0340 123  ASP A OD2 
790   N N   . LYS A 126  ? 0.5078 0.7310 0.4990 -0.0111 0.0150  -0.0372 124  LYS A N   
791   C CA  . LYS A 126  ? 0.4983 0.7095 0.4905 -0.0120 0.0151  -0.0325 124  LYS A CA  
792   C C   . LYS A 126  ? 0.5171 0.7130 0.5122 -0.0091 0.0146  -0.0374 124  LYS A C   
793   O O   . LYS A 126  ? 0.5692 0.7628 0.5662 -0.0081 0.0149  -0.0391 124  LYS A O   
794   C CB  . LYS A 126  ? 0.5518 0.7558 0.5420 -0.0153 0.0146  -0.0228 124  LYS A CB  
795   N N   . ILE A 127  ? 0.4708 0.6565 0.4666 -0.0078 0.0137  -0.0395 125  ILE A N   
796   C CA  . ILE A 127  ? 0.4460 0.6169 0.4447 -0.0054 0.0131  -0.0430 125  ILE A CA  
797   C C   . ILE A 127  ? 0.4814 0.6569 0.4836 -0.0022 0.0132  -0.0518 125  ILE A C   
798   O O   . ILE A 127  ? 0.4958 0.6654 0.5004 -0.0009 0.0132  -0.0532 125  ILE A O   
799   C CB  . ILE A 127  ? 0.4089 0.5691 0.4078 -0.0049 0.0122  -0.0431 125  ILE A CB  
800   C CG1 . ILE A 127  ? 0.4728 0.6293 0.4685 -0.0079 0.0121  -0.0346 125  ILE A CG1 
801   C CG2 . ILE A 127  ? 0.4097 0.5547 0.4117 -0.0027 0.0117  -0.0454 125  ILE A CG2 
802   C CD1 . ILE A 127  ? 0.4790 0.6272 0.4741 -0.0096 0.0123  -0.0281 125  ILE A CD1 
803   N N   . ALA A 128  ? 0.4369 0.6234 0.4400 -0.0008 0.0130  -0.0581 126  ALA A N   
804   C CA  . ALA A 128  ? 0.4076 0.5974 0.4150 0.0027  0.0126  -0.0674 126  ALA A CA  
805   C C   . ALA A 128  ? 0.4861 0.6850 0.4942 0.0030  0.0135  -0.0687 126  ALA A C   
806   O O   . ALA A 128  ? 0.4563 0.6520 0.4685 0.0056  0.0132  -0.0741 126  ALA A O   
807   C CB  . ALA A 128  ? 0.4128 0.6133 0.4210 0.0041  0.0121  -0.0741 126  ALA A CB  
808   N N   . ASP A 129  ? 0.6628 0.8731 0.6673 0.0003  0.0146  -0.0635 127  ASP A N   
809   C CA  . ASP A 129  ? 0.6830 0.9045 0.6879 0.0004  0.0156  -0.0646 127  ASP A CA  
810   C C   . ASP A 129  ? 0.6898 0.9018 0.6952 -0.0006 0.0158  -0.0596 127  ASP A C   
811   O O   . ASP A 129  ? 0.7586 0.9796 0.7642 -0.0011 0.0167  -0.0591 127  ASP A O   
812   C CB  . ASP A 129  ? 0.6676 0.9073 0.6690 -0.0021 0.0166  -0.0612 127  ASP A CB  
813   N N   . GLY A 130  ? 0.6531 0.8480 0.6587 -0.0009 0.0151  -0.0560 128  GLY A N   
814   C CA  . GLY A 130  ? 0.6900 0.8759 0.6964 -0.0013 0.0152  -0.0525 128  GLY A CA  
815   C C   . GLY A 130  ? 0.7038 0.8748 0.7085 -0.0032 0.0147  -0.0454 128  GLY A C   
816   O O   . GLY A 130  ? 0.6555 0.8145 0.6612 -0.0020 0.0139  -0.0464 128  GLY A O   
817   N N   . ASN A 131  ? 0.7395 0.9116 0.7422 -0.0062 0.0151  -0.0382 129  ASN A N   
818   C CA  . ASN A 131  ? 0.6804 0.8388 0.6821 -0.0079 0.0146  -0.0318 129  ASN A CA  
819   C C   . ASN A 131  ? 0.6011 0.7529 0.6009 -0.0088 0.0140  -0.0289 129  ASN A C   
820   O O   . ASN A 131  ? 0.6675 0.8245 0.6651 -0.0115 0.0141  -0.0237 129  ASN A O   
821   C CB  . ASN A 131  ? 0.6731 0.8356 0.6737 -0.0111 0.0149  -0.0250 129  ASN A CB  
822   N N   . TRP A 132  ? 0.5780 0.7186 0.5791 -0.0066 0.0134  -0.0321 130  TRP A N   
823   C CA  . TRP A 132  ? 0.4749 0.6074 0.4745 -0.0074 0.0128  -0.0290 130  TRP A CA  
824   C C   . TRP A 132  ? 0.4696 0.5928 0.4678 -0.0096 0.0124  -0.0218 130  TRP A C   
825   O O   . TRP A 132  ? 0.5153 0.6353 0.5119 -0.0113 0.0121  -0.0175 130  TRP A O   
826   C CB  . TRP A 132  ? 0.4321 0.5549 0.4340 -0.0046 0.0122  -0.0340 130  TRP A CB  
827   C CG  . TRP A 132  ? 0.3656 0.4783 0.3697 -0.0029 0.0119  -0.0352 130  TRP A CG  
828   C CD1 . TRP A 132  ? 0.3500 0.4646 0.3571 -0.0005 0.0119  -0.0405 130  TRP A CD1 
829   C CD2 . TRP A 132  ? 0.2935 0.3933 0.2970 -0.0033 0.0115  -0.0309 130  TRP A CD2 
830   N NE1 . TRP A 132  ? 0.3222 0.4258 0.3306 0.0005  0.0116  -0.0395 130  TRP A NE1 
831   C CE2 . TRP A 132  ? 0.3063 0.4010 0.3124 -0.0012 0.0114  -0.0337 130  TRP A CE2 
832   C CE3 . TRP A 132  ? 0.3612 0.4536 0.3626 -0.0051 0.0113  -0.0252 130  TRP A CE3 
833   C CZ2 . TRP A 132  ? 0.2920 0.3751 0.2981 -0.0010 0.0110  -0.0309 130  TRP A CZ2 
834   C CZ3 . TRP A 132  ? 0.3297 0.4105 0.3312 -0.0048 0.0109  -0.0228 130  TRP A CZ3 
835   C CH2 . TRP A 132  ? 0.3259 0.4025 0.3296 -0.0027 0.0108  -0.0256 130  TRP A CH2 
836   N N   . LYS A 133  ? 0.4834 0.6024 0.4827 -0.0096 0.0125  -0.0207 131  LYS A N   
837   C CA  . LYS A 133  ? 0.5373 0.6472 0.5358 -0.0114 0.0119  -0.0146 131  LYS A CA  
838   C C   . LYS A 133  ? 0.6365 0.7533 0.6336 -0.0149 0.0119  -0.0083 131  LYS A C   
839   O O   . LYS A 133  ? 0.7264 0.8363 0.7229 -0.0165 0.0112  -0.0032 131  LYS A O   
840   C CB  . LYS A 133  ? 0.4767 0.5825 0.4768 -0.0106 0.0119  -0.0153 131  LYS A CB  
841   N N   . SER A 134  ? 0.6672 0.7979 0.6641 -0.0159 0.0125  -0.0085 132  SER A N   
842   C CA  . SER A 134  ? 0.7140 0.8524 0.7101 -0.0194 0.0124  -0.0019 132  SER A CA  
843   C C   . SER A 134  ? 0.7477 0.8859 0.7424 -0.0207 0.0119  0.0014  132  SER A C   
844   O O   . SER A 134  ? 0.7867 0.9240 0.7813 -0.0235 0.0112  0.0082  132  SER A O   
845   C CB  . SER A 134  ? 0.7024 0.8573 0.6986 -0.0201 0.0134  -0.0031 132  SER A CB  
846   N N   . HIS A 135  ? 0.7329 0.8714 0.7268 -0.0187 0.0121  -0.0032 133  HIS A N   
847   C CA  . HIS A 135  ? 0.7433 0.8838 0.7356 -0.0198 0.0117  -0.0007 133  HIS A CA  
848   C C   . HIS A 135  ? 0.7561 0.8826 0.7484 -0.0188 0.0109  -0.0004 133  HIS A C   
849   O O   . HIS A 135  ? 0.7667 0.8932 0.7581 -0.0201 0.0104  0.0029  133  HIS A O   
850   C CB  . HIS A 135  ? 0.7142 0.8673 0.7057 -0.0186 0.0123  -0.0058 133  HIS A CB  
851   C CG  . HIS A 135  ? 0.7353 0.9034 0.7268 -0.0191 0.0132  -0.0071 133  HIS A CG  
852   N ND1 . HIS A 135  ? 0.7025 0.8722 0.6955 -0.0170 0.0138  -0.0127 133  HIS A ND1 
853   C CD2 . HIS A 135  ? 0.7076 0.8903 0.6980 -0.0216 0.0136  -0.0033 133  HIS A CD2 
854   C CE1 . HIS A 135  ? 0.7487 0.9334 0.7414 -0.0180 0.0146  -0.0126 133  HIS A CE1 
855   N NE2 . HIS A 135  ? 0.7815 0.9745 0.7725 -0.0208 0.0145  -0.0068 133  HIS A NE2 
856   N N   . LEU A 136  ? 0.7437 0.8589 0.7372 -0.0167 0.0108  -0.0035 134  LEU A N   
857   C CA  . LEU A 136  ? 0.7409 0.8434 0.7343 -0.0157 0.0102  -0.0033 134  LEU A CA  
858   C C   . LEU A 136  ? 0.7922 0.8827 0.7867 -0.0150 0.0099  -0.0023 134  LEU A C   
859   O O   . LEU A 136  ? 0.7952 0.8758 0.7896 -0.0150 0.0093  0.0001  134  LEU A O   
860   C CB  . LEU A 136  ? 0.6928 0.7945 0.6867 -0.0130 0.0104  -0.0096 134  LEU A CB  
861   C CG  . LEU A 136  ? 0.6569 0.7681 0.6498 -0.0134 0.0105  -0.0108 134  LEU A CG  
862   C CD1 . LEU A 136  ? 0.5462 0.6570 0.5405 -0.0106 0.0105  -0.0181 134  LEU A CD1 
863   C CD2 . LEU A 136  ? 0.5939 0.7012 0.5856 -0.0151 0.0098  -0.0055 134  LEU A CD2 
864   N N   . SER A 139  ? 0.5025 0.5590 0.5004 -0.0207 0.0056  0.0177  137  SER A N   
865   C CA  . SER A 139  ? 0.5592 0.6055 0.5581 -0.0206 0.0045  0.0198  137  SER A CA  
866   C C   . SER A 139  ? 0.5602 0.5983 0.5579 -0.0177 0.0050  0.0158  137  SER A C   
867   O O   . SER A 139  ? 0.5514 0.5808 0.5496 -0.0169 0.0043  0.0161  137  SER A O   
868   C CB  . SER A 139  ? 0.5779 0.6259 0.5776 -0.0227 0.0035  0.0246  137  SER A CB  
869   N N   . ARG A 140  ? 0.4445 0.4858 0.4407 -0.0162 0.0060  0.0121  138  ARG A N   
870   C CA  . ARG A 140  ? 0.4285 0.4632 0.4242 -0.0137 0.0065  0.0086  138  ARG A CA  
871   C C   . ARG A 140  ? 0.3946 0.4329 0.3901 -0.0119 0.0075  0.0038  138  ARG A C   
872   O O   . ARG A 140  ? 0.3784 0.4254 0.3737 -0.0124 0.0080  0.0024  138  ARG A O   
873   C CB  . ARG A 140  ? 0.4431 0.4776 0.4382 -0.0137 0.0064  0.0093  138  ARG A CB  
874   C CG  . ARG A 140  ? 0.4509 0.4809 0.4457 -0.0113 0.0070  0.0055  138  ARG A CG  
875   C CD  . ARG A 140  ? 0.4930 0.5257 0.4874 -0.0117 0.0069  0.0060  138  ARG A CD  
876   N NE  . ARG A 140  ? 0.5267 0.5557 0.5214 -0.0097 0.0074  0.0027  138  ARG A NE  
877   C CZ  . ARG A 140  ? 0.5673 0.6005 0.5624 -0.0086 0.0079  -0.0015 138  ARG A CZ  
878   N NH1 . ARG A 140  ? 0.5404 0.5819 0.5355 -0.0090 0.0082  -0.0033 138  ARG A NH1 
879   N NH2 . ARG A 140  ? 0.5327 0.5620 0.5287 -0.0071 0.0080  -0.0040 138  ARG A NH2 
880   N N   . SER A 141  ? 0.3595 0.3915 0.3553 -0.0099 0.0077  0.0013  139  SER A N   
881   C CA  . SER A 141  ? 0.3220 0.3564 0.3184 -0.0080 0.0084  -0.0032 139  SER A CA  
882   C C   . SER A 141  ? 0.2876 0.3247 0.2843 -0.0072 0.0088  -0.0060 139  SER A C   
883   O O   . SER A 141  ? 0.2880 0.3210 0.2844 -0.0069 0.0086  -0.0052 139  SER A O   
884   C CB  . SER A 141  ? 0.2977 0.3240 0.2947 -0.0060 0.0084  -0.0046 139  SER A CB  
885   O OG  . SER A 141  ? 0.2891 0.3167 0.2875 -0.0040 0.0088  -0.0088 139  SER A OG  
886   N N   . LEU A 142  ? 0.2960 0.3406 0.2935 -0.0066 0.0092  -0.0095 140  LEU A N   
887   C CA  . LEU A 142  ? 0.2545 0.3014 0.2529 -0.0053 0.0093  -0.0133 140  LEU A CA  
888   C C   . LEU A 142  ? 0.2511 0.2892 0.2510 -0.0033 0.0092  -0.0151 140  LEU A C   
889   O O   . LEU A 142  ? 0.2624 0.3001 0.2632 -0.0026 0.0091  -0.0170 140  LEU A O   
890   C CB  . LEU A 142  ? 0.2815 0.3371 0.2813 -0.0045 0.0097  -0.0177 140  LEU A CB  
891   C CG  . LEU A 142  ? 0.3413 0.4063 0.3411 -0.0047 0.0098  -0.0203 140  LEU A CG  
892   C CD1 . LEU A 142  ? 0.3732 0.4457 0.3706 -0.0074 0.0099  -0.0161 140  LEU A CD1 
893   C CD2 . LEU A 142  ? 0.3521 0.4237 0.3540 -0.0031 0.0100  -0.0258 140  LEU A CD2 
894   N N   . PHE A 143  ? 0.2238 0.2552 0.2241 -0.0024 0.0091  -0.0143 141  PHE A N   
895   C CA  . PHE A 143  ? 0.2319 0.2564 0.2342 -0.0002 0.0090  -0.0162 141  PHE A CA  
896   C C   . PHE A 143  ? 0.2295 0.2457 0.2307 -0.0003 0.0089  -0.0129 141  PHE A C   
897   O O   . PHE A 143  ? 0.2358 0.2462 0.2383 0.0013  0.0089  -0.0134 141  PHE A O   
898   C CB  . PHE A 143  ? 0.2288 0.2529 0.2326 0.0011  0.0090  -0.0180 141  PHE A CB  
899   C CG  . PHE A 143  ? 0.2105 0.2433 0.2155 0.0012  0.0092  -0.0214 141  PHE A CG  
900   C CD1 . PHE A 143  ? 0.2073 0.2443 0.2145 0.0022  0.0091  -0.0255 141  PHE A CD1 
901   C CD2 . PHE A 143  ? 0.2167 0.2539 0.2208 0.0004  0.0093  -0.0206 141  PHE A CD2 
902   C CE1 . PHE A 143  ? 0.2181 0.2639 0.2264 0.0025  0.0092  -0.0291 141  PHE A CE1 
903   C CE2 . PHE A 143  ? 0.2260 0.2721 0.2313 0.0005  0.0096  -0.0238 141  PHE A CE2 
904   C CZ  . PHE A 143  ? 0.2063 0.2569 0.2135 0.0017  0.0095  -0.0282 141  PHE A CZ  
905   N N   . VAL A 144  ? 0.2410 0.2571 0.2402 -0.0019 0.0088  -0.0097 142  VAL A N   
906   C CA  A VAL A 144  ? 0.2579 0.2667 0.2562 -0.0018 0.0086  -0.0069 142  VAL A CA  
907   C CA  B VAL A 144  ? 0.2577 0.2666 0.2560 -0.0019 0.0086  -0.0069 142  VAL A CA  
908   C C   . VAL A 144  ? 0.2587 0.2633 0.2586 -0.0003 0.0088  -0.0082 142  VAL A C   
909   O O   . VAL A 144  ? 0.2664 0.2649 0.2663 0.0007  0.0088  -0.0071 142  VAL A O   
910   C CB  A VAL A 144  ? 0.2712 0.2810 0.2679 -0.0038 0.0083  -0.0034 142  VAL A CB  
911   C CB  B VAL A 144  ? 0.2709 0.2812 0.2677 -0.0038 0.0083  -0.0036 142  VAL A CB  
912   C CG1 A VAL A 144  ? 0.2962 0.3095 0.2922 -0.0054 0.0080  -0.0015 142  VAL A CG1 
913   C CG1 B VAL A 144  ? 0.2646 0.2680 0.2610 -0.0034 0.0081  -0.0014 142  VAL A CG1 
914   C CG2 A VAL A 144  ? 0.2835 0.2982 0.2803 -0.0046 0.0083  -0.0039 142  VAL A CG2 
915   C CG2 B VAL A 144  ? 0.2953 0.3085 0.2913 -0.0054 0.0080  -0.0014 142  VAL A CG2 
916   N N   . ASN A 145  ? 0.2320 0.2400 0.2333 -0.0001 0.0088  -0.0107 143  ASN A N   
917   C CA  . ASN A 145  ? 0.2493 0.2535 0.2528 0.0011  0.0088  -0.0119 143  ASN A CA  
918   C C   . ASN A 145  ? 0.2600 0.2641 0.2668 0.0028  0.0086  -0.0155 143  ASN A C   
919   O O   . ASN A 145  ? 0.2416 0.2445 0.2513 0.0036  0.0083  -0.0174 143  ASN A O   
920   C CB  . ASN A 145  ? 0.2737 0.2808 0.2771 0.0002  0.0086  -0.0123 143  ASN A CB  
921   C CG  . ASN A 145  ? 0.2829 0.2886 0.2838 -0.0011 0.0086  -0.0084 143  ASN A CG  
922   O OD1 . ASN A 145  ? 0.3498 0.3496 0.3503 -0.0007 0.0087  -0.0061 143  ASN A OD1 
923   N ND2 . ASN A 145  ? 0.3154 0.3269 0.3150 -0.0027 0.0084  -0.0075 143  ASN A ND2 
924   N N   . ALA A 146  ? 0.2180 0.2234 0.2251 0.0033  0.0086  -0.0164 144  ALA A N   
925   C CA  . ALA A 146  ? 0.2370 0.2428 0.2479 0.0050  0.0083  -0.0200 144  ALA A CA  
926   C C   . ALA A 146  ? 0.2106 0.2096 0.2242 0.0064  0.0080  -0.0192 144  ALA A C   
927   O O   . ALA A 146  ? 0.2516 0.2502 0.2696 0.0077  0.0075  -0.0219 144  ALA A O   
928   C CB  . ALA A 146  ? 0.2251 0.2337 0.2357 0.0053  0.0083  -0.0209 144  ALA A CB  
929   N N   . ALA A 147  ? 0.2496 0.2434 0.2610 0.0062  0.0084  -0.0154 145  ALA A N   
930   C CA  . ALA A 147  ? 0.2878 0.2762 0.3018 0.0074  0.0082  -0.0143 145  ALA A CA  
931   C C   . ALA A 147  ? 0.2590 0.2468 0.2759 0.0074  0.0079  -0.0154 145  ALA A C   
932   O O   . ALA A 147  ? 0.2817 0.2671 0.3031 0.0085  0.0074  -0.0163 145  ALA A O   
933   C CB  . ALA A 147  ? 0.3350 0.3192 0.3459 0.0073  0.0087  -0.0103 145  ALA A CB  
934   N N   . THR A 148  ? 0.2496 0.2398 0.2645 0.0062  0.0081  -0.0154 146  THR A N   
935   C CA  . THR A 148  ? 0.2550 0.2454 0.2726 0.0061  0.0078  -0.0168 146  THR A CA  
936   C C   . THR A 148  ? 0.2384 0.2326 0.2602 0.0068  0.0070  -0.0216 146  THR A C   
937   O O   . THR A 148  ? 0.2559 0.2480 0.2826 0.0077  0.0063  -0.0232 146  THR A O   
938   C CB  . THR A 148  ? 0.3055 0.2984 0.3198 0.0046  0.0080  -0.0156 146  THR A CB  
939   O OG1 . THR A 148  ? 0.3143 0.3034 0.3254 0.0041  0.0086  -0.0115 146  THR A OG1 
940   C CG2 . THR A 148  ? 0.3326 0.3259 0.3495 0.0044  0.0076  -0.0170 146  THR A CG2 
941   N N   . TRP A 149  ? 0.2306 0.2308 0.2510 0.0065  0.0070  -0.0240 147  TRP A N   
942   C CA  . TRP A 149  ? 0.2355 0.2400 0.2600 0.0074  0.0062  -0.0291 147  TRP A CA  
943   C C   . TRP A 149  ? 0.2089 0.2098 0.2382 0.0092  0.0056  -0.0305 147  TRP A C   
944   O O   . TRP A 149  ? 0.2298 0.2315 0.2646 0.0102  0.0045  -0.0344 147  TRP A O   
945   C CB  . TRP A 149  ? 0.2394 0.2519 0.2613 0.0068  0.0065  -0.0312 147  TRP A CB  
946   C CG  . TRP A 149  ? 0.2144 0.2315 0.2328 0.0051  0.0068  -0.0303 147  TRP A CG  
947   C CD1 . TRP A 149  ? 0.2361 0.2555 0.2496 0.0035  0.0075  -0.0269 147  TRP A CD1 
948   C CD2 . TRP A 149  ? 0.2526 0.2725 0.2724 0.0048  0.0063  -0.0326 147  TRP A CD2 
949   N NE1 . TRP A 149  ? 0.2436 0.2672 0.2554 0.0022  0.0075  -0.0266 147  TRP A NE1 
950   C CE2 . TRP A 149  ? 0.2400 0.2643 0.2554 0.0031  0.0068  -0.0301 147  TRP A CE2 
951   C CE3 . TRP A 149  ? 0.2527 0.2721 0.2776 0.0059  0.0054  -0.0364 147  TRP A CE3 
952   C CZ2 . TRP A 149  ? 0.2818 0.3101 0.2971 0.0024  0.0064  -0.0313 147  TRP A CZ2 
953   C CZ3 . TRP A 149  ? 0.3178 0.3411 0.3428 0.0052  0.0050  -0.0380 147  TRP A CZ3 
954   C CH2 . TRP A 149  ? 0.3345 0.3624 0.3545 0.0035  0.0056  -0.0355 147  TRP A CH2 
955   N N   . GLY A 150  ? 0.2172 0.2145 0.2449 0.0095  0.0060  -0.0274 148  GLY A N   
956   C CA  . GLY A 150  ? 0.2467 0.2403 0.2791 0.0111  0.0053  -0.0277 148  GLY A CA  
957   C C   . GLY A 150  ? 0.2415 0.2301 0.2786 0.0116  0.0046  -0.0268 148  GLY A C   
958   O O   . GLY A 150  ? 0.2600 0.2474 0.3035 0.0129  0.0034  -0.0292 148  GLY A O   
959   N N   . LEU A 151  ? 0.2539 0.2397 0.2885 0.0106  0.0052  -0.0234 149  LEU A N   
960   C CA  . LEU A 151  ? 0.3057 0.2874 0.3449 0.0108  0.0046  -0.0223 149  LEU A CA  
961   C C   . LEU A 151  ? 0.2534 0.2377 0.2976 0.0110  0.0035  -0.0270 149  LEU A C   
962   O O   . LEU A 151  ? 0.3075 0.2892 0.3585 0.0118  0.0022  -0.0283 149  LEU A O   
963   C CB  . LEU A 151  ? 0.3218 0.3012 0.3570 0.0097  0.0056  -0.0180 149  LEU A CB  
964   C CG  . LEU A 151  ? 0.3910 0.3657 0.4297 0.0099  0.0053  -0.0151 149  LEU A CG  
965   C CD1 . LEU A 151  ? 0.3375 0.3091 0.3799 0.0111  0.0048  -0.0131 149  LEU A CD1 
966   C CD2 . LEU A 151  ? 0.4367 0.4101 0.4702 0.0090  0.0065  -0.0110 149  LEU A CD2 
967   N N   . VAL A 152  ? 0.2674 0.2571 0.3085 0.0102  0.0037  -0.0298 150  VAL A N   
968   C CA  . VAL A 152  ? 0.2892 0.2827 0.3346 0.0104  0.0026  -0.0350 150  VAL A CA  
969   C C   . VAL A 152  ? 0.2852 0.2802 0.3366 0.0121  0.0014  -0.0398 150  VAL A C   
970   O O   . VAL A 152  ? 0.3088 0.3030 0.3672 0.0129  -0.0001 -0.0432 150  VAL A O   
971   C CB  . VAL A 152  ? 0.2877 0.2880 0.3280 0.0092  0.0033  -0.0366 150  VAL A CB  
972   C CG1 . VAL A 152  ? 0.3157 0.3216 0.3600 0.0097  0.0021  -0.0428 150  VAL A CG1 
973   C CG2 . VAL A 152  ? 0.3051 0.3035 0.3411 0.0077  0.0041  -0.0323 150  VAL A CG2 
974   N N   . VAL A 153  ? 0.2596 0.2570 0.3089 0.0126  0.0018  -0.0404 151  VAL A N   
975   C CA  . VAL A 153  ? 0.2903 0.2904 0.3451 0.0143  0.0006  -0.0456 151  VAL A CA  
976   C C   . VAL A 153  ? 0.2535 0.2471 0.3147 0.0157  -0.0005 -0.0442 151  VAL A C   
977   O O   . VAL A 153  ? 0.3021 0.2954 0.3711 0.0171  -0.0022 -0.0484 151  VAL A O   
978   C CB  . VAL A 153  ? 0.2594 0.2654 0.3097 0.0143  0.0015  -0.0468 151  VAL A CB  
979   C CG1 . VAL A 153  ? 0.2868 0.2955 0.3429 0.0163  0.0003  -0.0520 151  VAL A CG1 
980   C CG2 . VAL A 153  ? 0.2763 0.2896 0.3214 0.0130  0.0023  -0.0483 151  VAL A CG2 
981   N N   . THR A 154  ? 0.2929 0.2817 0.3513 0.0154  0.0003  -0.0385 152  THR A N   
982   C CA  . THR A 154  ? 0.2937 0.2776 0.3574 0.0167  -0.0007 -0.0365 152  THR A CA  
983   C C   . THR A 154  ? 0.3415 0.3192 0.4079 0.0162  -0.0010 -0.0318 152  THR A C   
984   O O   . THR A 154  ? 0.3586 0.3324 0.4311 0.0172  -0.0021 -0.0302 152  THR A O   
985   C CB  . THR A 154  ? 0.3199 0.3037 0.3791 0.0169  0.0002  -0.0336 152  THR A CB  
986   O OG1 . THR A 154  ? 0.3255 0.3072 0.3780 0.0156  0.0017  -0.0282 152  THR A OG1 
987   C CG2 . THR A 154  ? 0.3246 0.3150 0.3806 0.0171  0.0007  -0.0376 152  THR A CG2 
988   N N   . GLY A 155  ? 0.3062 0.2833 0.3686 0.0148  0.0000  -0.0293 153  GLY A N   
989   C CA  . GLY A 155  ? 0.3279 0.3000 0.3919 0.0143  0.0001  -0.0242 153  GLY A CA  
990   C C   . GLY A 155  ? 0.3669 0.3365 0.4266 0.0142  0.0012  -0.0186 153  GLY A C   
991   O O   . GLY A 155  ? 0.3597 0.3259 0.4203 0.0139  0.0014  -0.0140 153  GLY A O   
992   N N   . LYS A 156  ? 0.3311 0.3028 0.3861 0.0146  0.0019  -0.0188 154  LYS A N   
993   C CA  . LYS A 156  ? 0.3623 0.3323 0.4131 0.0147  0.0028  -0.0141 154  LYS A CA  
994   C C   . LYS A 156  ? 0.3709 0.3431 0.4132 0.0136  0.0043  -0.0132 154  LYS A C   
995   O O   . LYS A 156  ? 0.3257 0.3016 0.3652 0.0131  0.0046  -0.0164 154  LYS A O   
996   C CB  . LYS A 156  ? 0.4144 0.3850 0.4674 0.0161  0.0021  -0.0150 154  LYS A CB  
997   N N   . LEU A 157  ? 0.3471 0.3173 0.3855 0.0133  0.0053  -0.0087 155  LEU A N   
998   C CA  . LEU A 157  ? 0.3785 0.3500 0.4097 0.0124  0.0065  -0.0075 155  LEU A CA  
999   C C   . LEU A 157  ? 0.4590 0.4311 0.4869 0.0129  0.0067  -0.0064 155  LEU A C   
1000  O O   . LEU A 157  ? 0.4564 0.4268 0.4859 0.0139  0.0065  -0.0038 155  LEU A O   
1001  C CB  . LEU A 157  ? 0.3653 0.3346 0.3946 0.0118  0.0072  -0.0037 155  LEU A CB  
1002  C CG  . LEU A 157  ? 0.4723 0.4424 0.4949 0.0111  0.0083  -0.0023 155  LEU A CG  
1003  C CD1 . LEU A 157  ? 0.4620 0.4347 0.4822 0.0099  0.0084  -0.0050 155  LEU A CD1 
1004  C CD2 . LEU A 157  ? 0.4390 0.4071 0.4607 0.0110  0.0089  0.0011  155  LEU A CD2 
1005  N N   . THR A 158  ? 0.5456 0.5206 0.5695 0.0123  0.0071  -0.0082 156  THR A N   
1006  C CA  . THR A 158  ? 0.5119 0.4876 0.5320 0.0124  0.0074  -0.0071 156  THR A CA  
1007  C C   . THR A 158  ? 0.5639 0.5398 0.5786 0.0113  0.0082  -0.0055 156  THR A C   
1008  O O   . THR A 158  ? 0.6309 0.6081 0.6443 0.0102  0.0085  -0.0065 156  THR A O   
1009  C CB  . THR A 158  ? 0.5336 0.5128 0.5543 0.0126  0.0070  -0.0104 156  THR A CB  
1010  N N   . SER A 159  ? 0.4071 0.3819 0.4188 0.0116  0.0085  -0.0031 157  SER A N   
1011  C CA  . SER A 159  ? 0.3815 0.3560 0.3888 0.0107  0.0091  -0.0018 157  SER A CA  
1012  C C   . SER A 159  ? 0.4223 0.3994 0.4270 0.0095  0.0090  -0.0034 157  SER A C   
1013  O O   . SER A 159  ? 0.4276 0.4051 0.4303 0.0083  0.0092  -0.0031 157  SER A O   
1014  C CB  . SER A 159  ? 0.4617 0.4347 0.4669 0.0116  0.0092  0.0007  157  SER A CB  
1015  O OG  . SER A 159  ? 0.4983 0.4718 0.5047 0.0127  0.0088  0.0008  157  SER A OG  
1016  N N   . THR A 160  ? 0.3465 0.3257 0.3518 0.0098  0.0086  -0.0048 158  THR A N   
1017  C CA  . THR A 160  ? 0.3148 0.2972 0.3183 0.0085  0.0085  -0.0060 158  THR A CA  
1018  C C   . THR A 160  ? 0.3093 0.2953 0.3155 0.0086  0.0083  -0.0089 158  THR A C   
1019  O O   . THR A 160  ? 0.3346 0.3199 0.3443 0.0099  0.0080  -0.0102 158  THR A O   
1020  C CB  . THR A 160  ? 0.3134 0.2958 0.3148 0.0087  0.0082  -0.0052 158  THR A CB  
1021  O OG1 . THR A 160  ? 0.3744 0.3567 0.3778 0.0102  0.0079  -0.0056 158  THR A OG1 
1022  C CG2 . THR A 160  ? 0.4021 0.3815 0.4011 0.0088  0.0083  -0.0030 158  THR A CG2 
1023  N N   . VAL A 161  ? 0.2138 0.2038 0.2186 0.0074  0.0083  -0.0100 159  VAL A N   
1024  C CA  . VAL A 161  ? 0.2321 0.2270 0.2389 0.0072  0.0082  -0.0130 159  VAL A CA  
1025  C C   . VAL A 161  ? 0.2177 0.2157 0.2247 0.0074  0.0080  -0.0141 159  VAL A C   
1026  O O   . VAL A 161  ? 0.2097 0.2085 0.2143 0.0064  0.0080  -0.0126 159  VAL A O   
1027  C CB  . VAL A 161  ? 0.2370 0.2355 0.2420 0.0054  0.0085  -0.0129 159  VAL A CB  
1028  C CG1 . VAL A 161  ? 0.2907 0.2958 0.2969 0.0050  0.0085  -0.0159 159  VAL A CG1 
1029  C CG2 . VAL A 161  ? 0.2854 0.2811 0.2906 0.0052  0.0087  -0.0121 159  VAL A CG2 
1030  N N   . ASN A 162  ? 0.2003 0.2001 0.2107 0.0088  0.0077  -0.0169 160  ASN A N   
1031  C CA  . ASN A 162  ? 0.2021 0.2059 0.2130 0.0090  0.0076  -0.0183 160  ASN A CA  
1032  C C   . ASN A 162  ? 0.1813 0.1921 0.1916 0.0076  0.0079  -0.0203 160  ASN A C   
1033  O O   . ASN A 162  ? 0.1992 0.2140 0.2123 0.0084  0.0078  -0.0238 160  ASN A O   
1034  C CB  . ASN A 162  ? 0.2077 0.2109 0.2229 0.0111  0.0070  -0.0205 160  ASN A CB  
1035  C CG  . ASN A 162  ? 0.2128 0.2198 0.2284 0.0114  0.0068  -0.0217 160  ASN A CG  
1036  O OD1 . ASN A 162  ? 0.2081 0.2199 0.2216 0.0100  0.0071  -0.0219 160  ASN A OD1 
1037  N ND2 . ASN A 162  ? 0.2837 0.2889 0.3023 0.0132  0.0061  -0.0221 160  ASN A ND2 
1038  N N   . ASP A 163  ? 0.1739 0.1864 0.1809 0.0057  0.0082  -0.0180 161  ASP A N   
1039  C CA  . ASP A 163  ? 0.1910 0.2105 0.1971 0.0040  0.0085  -0.0187 161  ASP A CA  
1040  C C   . ASP A 163  ? 0.1797 0.2062 0.1873 0.0043  0.0086  -0.0213 161  ASP A C   
1041  O O   . ASP A 163  ? 0.1988 0.2324 0.2068 0.0037  0.0089  -0.0234 161  ASP A O   
1042  C CB  . ASP A 163  ? 0.2205 0.2398 0.2234 0.0017  0.0086  -0.0150 161  ASP A CB  
1043  C CG  . ASP A 163  ? 0.2507 0.2670 0.2524 0.0012  0.0082  -0.0125 161  ASP A CG  
1044  O OD1 . ASP A 163  ? 0.2210 0.2323 0.2231 0.0027  0.0080  -0.0124 161  ASP A OD1 
1045  O OD2 . ASP A 163  ? 0.2785 0.2975 0.2788 -0.0008 0.0081  -0.0103 161  ASP A OD2 
1046  N N   . ARG A 164  ? 0.1899 0.2150 0.1982 0.0051  0.0083  -0.0213 162  ARG A N   
1047  C CA  A ARG A 164  ? 0.1723 0.2042 0.1824 0.0055  0.0083  -0.0239 162  ARG A CA  
1048  C CA  B ARG A 164  ? 0.1728 0.2046 0.1828 0.0055  0.0083  -0.0239 162  ARG A CA  
1049  C C   . ARG A 164  ? 0.1747 0.2084 0.1887 0.0078  0.0081  -0.0285 162  ARG A C   
1050  O O   . ARG A 164  ? 0.1741 0.2156 0.1896 0.0079  0.0083  -0.0318 162  ARG A O   
1051  C CB  A ARG A 164  ? 0.1991 0.2291 0.2089 0.0057  0.0080  -0.0225 162  ARG A CB  
1052  C CB  B ARG A 164  ? 0.1993 0.2291 0.2092 0.0058  0.0080  -0.0225 162  ARG A CB  
1053  C CG  A ARG A 164  ? 0.2192 0.2483 0.2260 0.0035  0.0079  -0.0186 162  ARG A CG  
1054  C CG  B ARG A 164  ? 0.2197 0.2490 0.2265 0.0035  0.0079  -0.0188 162  ARG A CG  
1055  C CD  A ARG A 164  ? 0.2866 0.3222 0.2919 0.0011  0.0084  -0.0175 162  ARG A CD  
1056  C CD  B ARG A 164  ? 0.2757 0.3123 0.2814 0.0012  0.0084  -0.0180 162  ARG A CD  
1057  N NE  A ARG A 164  ? 0.2628 0.3076 0.2696 0.0010  0.0088  -0.0202 162  ARG A NE  
1058  N NE  B ARG A 164  ? 0.2656 0.2999 0.2695 0.0000  0.0085  -0.0159 162  ARG A NE  
1059  C CZ  A ARG A 164  ? 0.3042 0.3563 0.3104 -0.0005 0.0093  -0.0203 162  ARG A CZ  
1060  C CZ  B ARG A 164  ? 0.2733 0.3134 0.2764 -0.0017 0.0089  -0.0153 162  ARG A CZ  
1061  N NH1 A ARG A 164  ? 0.3297 0.3808 0.3340 -0.0020 0.0094  -0.0178 162  ARG A NH1 
1062  N NH1 B ARG A 164  ? 0.3303 0.3795 0.3340 -0.0024 0.0093  -0.0168 162  ARG A NH1 
1063  N NH2 A ARG A 164  ? 0.2622 0.3235 0.2698 -0.0003 0.0097  -0.0230 162  ARG A NH2 
1064  N NH2 B ARG A 164  ? 0.3034 0.3405 0.3050 -0.0026 0.0088  -0.0131 162  ARG A NH2 
1065  N N   . SER A 165  ? 0.1734 0.2005 0.1895 0.0095  0.0076  -0.0289 163  SER A N   
1066  C CA  . SER A 165  ? 0.1608 0.1889 0.1816 0.0115  0.0071  -0.0332 163  SER A CA  
1067  C C   . SER A 165  ? 0.1814 0.2143 0.2024 0.0109  0.0074  -0.0356 163  SER A C   
1068  O O   . SER A 165  ? 0.1595 0.1983 0.1836 0.0119  0.0072  -0.0403 163  SER A O   
1069  C CB  . SER A 165  ? 0.1697 0.1895 0.1931 0.0131  0.0064  -0.0321 163  SER A CB  
1070  O OG  . SER A 165  ? 0.2075 0.2275 0.2362 0.0148  0.0057  -0.0360 163  SER A OG  
1071  N N   . LEU A 166  ? 0.1814 0.2119 0.1993 0.0093  0.0078  -0.0328 164  LEU A N   
1072  C CA  . LEU A 166  ? 0.1820 0.2172 0.1996 0.0086  0.0080  -0.0347 164  LEU A CA  
1073  C C   . LEU A 166  ? 0.1693 0.2148 0.1853 0.0073  0.0086  -0.0360 164  LEU A C   
1074  O O   . LEU A 166  ? 0.1708 0.2231 0.1882 0.0077  0.0086  -0.0399 164  LEU A O   
1075  C CB  . LEU A 166  ? 0.1756 0.2062 0.1902 0.0071  0.0083  -0.0308 164  LEU A CB  
1076  C CG  . LEU A 166  ? 0.1751 0.1970 0.1918 0.0084  0.0078  -0.0301 164  LEU A CG  
1077  C CD1 . LEU A 166  ? 0.2087 0.2262 0.2222 0.0069  0.0081  -0.0260 164  LEU A CD1 
1078  C CD2 . LEU A 166  ? 0.1990 0.2220 0.2204 0.0099  0.0071  -0.0346 164  LEU A CD2 
1079  N N   . ALA A 167  ? 0.1765 0.2237 0.1895 0.0057  0.0090  -0.0327 165  ALA A N   
1080  C CA  . ALA A 167  ? 0.1741 0.2317 0.1858 0.0043  0.0096  -0.0333 165  ALA A CA  
1081  C C   . ALA A 167  ? 0.1832 0.2474 0.1983 0.0062  0.0095  -0.0385 165  ALA A C   
1082  O O   . ALA A 167  ? 0.1836 0.2575 0.1991 0.0060  0.0098  -0.0416 165  ALA A O   
1083  C CB  . ALA A 167  ? 0.2002 0.2577 0.2090 0.0022  0.0098  -0.0285 165  ALA A CB  
1084  N N   . ALA A 168  ? 0.1760 0.2356 0.1938 0.0080  0.0090  -0.0396 166  ALA A N   
1085  C CA  . ALA A 168  ? 0.1766 0.2417 0.1984 0.0101  0.0087  -0.0449 166  ALA A CA  
1086  C C   . ALA A 168  ? 0.1503 0.2175 0.1757 0.0118  0.0082  -0.0502 166  ALA A C   
1087  O O   . ALA A 168  ? 0.1781 0.2546 0.2056 0.0127  0.0083  -0.0550 166  ALA A O   
1088  C CB  . ALA A 168  ? 0.1868 0.2451 0.2113 0.0119  0.0080  -0.0447 166  ALA A CB  
1089  N N   . ALA A 169  ? 0.1644 0.2236 0.1908 0.0123  0.0076  -0.0495 167  ALA A N   
1090  C CA  . ALA A 169  ? 0.1476 0.2078 0.1782 0.0140  0.0069  -0.0545 167  ALA A CA  
1091  C C   . ALA A 169  ? 0.1621 0.2314 0.1905 0.0127  0.0074  -0.0563 167  ALA A C   
1092  O O   . ALA A 169  ? 0.1729 0.2487 0.2047 0.0142  0.0070  -0.0622 167  ALA A O   
1093  C CB  . ALA A 169  ? 0.1694 0.2189 0.2014 0.0144  0.0062  -0.0523 167  ALA A CB  
1094  N N   . LEU A 170  ? 0.1714 0.2416 0.1945 0.0101  0.0083  -0.0514 168  LEU A N   
1095  C CA  . LEU A 170  ? 0.1700 0.2493 0.1906 0.0087  0.0088  -0.0523 168  LEU A CA  
1096  C C   . LEU A 170  ? 0.1655 0.2576 0.1862 0.0088  0.0093  -0.0555 168  LEU A C   
1097  O O   . LEU A 170  ? 0.1710 0.2721 0.1931 0.0095  0.0093  -0.0605 168  LEU A O   
1098  C CB  . LEU A 170  ? 0.1920 0.2690 0.2075 0.0059  0.0094  -0.0457 168  LEU A CB  
1099  C CG  . LEU A 170  ? 0.1968 0.2824 0.2100 0.0044  0.0097  -0.0458 168  LEU A CG  
1100  C CD1 . LEU A 170  ? 0.2316 0.3171 0.2477 0.0059  0.0090  -0.0507 168  LEU A CD1 
1101  C CD2 . LEU A 170  ? 0.2257 0.3076 0.2347 0.0018  0.0101  -0.0391 168  LEU A CD2 
1102  N N   . THR A 171  ? 0.1711 0.2644 0.1905 0.0081  0.0099  -0.0530 169  THR A N   
1103  C CA  . THR A 171  ? 0.1727 0.2782 0.1925 0.0082  0.0104  -0.0559 169  THR A CA  
1104  C C   . THR A 171  ? 0.1619 0.2712 0.1872 0.0114  0.0097  -0.0638 169  THR A C   
1105  O O   . THR A 171  ? 0.1766 0.2977 0.2028 0.0120  0.0100  -0.0685 169  THR A O   
1106  C CB  . THR A 171  ? 0.2017 0.3058 0.2203 0.0073  0.0108  -0.0520 169  THR A CB  
1107  O OG1 . THR A 171  ? 0.2435 0.3449 0.2577 0.0042  0.0113  -0.0451 169  THR A OG1 
1108  C CG2 . THR A 171  ? 0.2025 0.3193 0.2221 0.0075  0.0114  -0.0550 169  THR A CG2 
1109  N N   . ARG A 172  ? 0.1686 0.2682 0.1981 0.0136  0.0087  -0.0653 170  ARG A N   
1110  C CA  . ARG A 172  ? 0.1616 0.2635 0.1974 0.0168  0.0077  -0.0727 170  ARG A CA  
1111  C C   . ARG A 172  ? 0.1789 0.2851 0.2170 0.0177  0.0071  -0.0780 170  ARG A C   
1112  O O   . ARG A 172  ? 0.1747 0.2908 0.2159 0.0194  0.0068  -0.0847 170  ARG A O   
1113  C CB  . ARG A 172  ? 0.1668 0.2564 0.2068 0.0186  0.0065  -0.0722 170  ARG A CB  
1114  C CG  . ARG A 172  ? 0.1616 0.2534 0.2089 0.0219  0.0053  -0.0791 170  ARG A CG  
1115  C CD  . ARG A 172  ? 0.1847 0.2643 0.2367 0.0236  0.0039  -0.0781 170  ARG A CD  
1116  N NE  . ARG A 172  ? 0.1625 0.2349 0.2108 0.0222  0.0045  -0.0711 170  ARG A NE  
1117  C CZ  . ARG A 172  ? 0.1712 0.2342 0.2167 0.0209  0.0045  -0.0657 170  ARG A CZ  
1118  N NH1 . ARG A 172  ? 0.1681 0.2274 0.2141 0.0206  0.0042  -0.0657 170  ARG A NH1 
1119  N NH2 . ARG A 172  ? 0.1849 0.2428 0.2271 0.0198  0.0050  -0.0602 170  ARG A NH2 
1120  N N   . LEU A 173  ? 0.1711 0.2705 0.2077 0.0167  0.0068  -0.0754 171  LEU A N   
1121  C CA  . LEU A 173  ? 0.1545 0.2571 0.1940 0.0178  0.0060  -0.0807 171  LEU A CA  
1122  C C   . LEU A 173  ? 0.1668 0.2835 0.2026 0.0165  0.0069  -0.0825 171  LEU A C   
1123  O O   . LEU A 173  ? 0.1794 0.3042 0.2185 0.0181  0.0063  -0.0895 171  LEU A O   
1124  C CB  . LEU A 173  ? 0.1914 0.2830 0.2307 0.0170  0.0054  -0.0774 171  LEU A CB  
1125  C CG  . LEU A 173  ? 0.2096 0.2995 0.2424 0.0140  0.0064  -0.0708 171  LEU A CG  
1126  C CD1 . LEU A 173  ? 0.2292 0.3274 0.2607 0.0134  0.0064  -0.0735 171  LEU A CD1 
1127  C CD2 . LEU A 173  ? 0.1928 0.2690 0.2258 0.0137  0.0060  -0.0661 171  LEU A CD2 
1128  N N   . ILE A 174  ? 0.1799 0.3000 0.2094 0.0136  0.0083  -0.0763 172  ILE A N   
1129  C CA  . ILE A 174  ? 0.1739 0.3083 0.2000 0.0122  0.0091  -0.0771 172  ILE A CA  
1130  C C   . ILE A 174  ? 0.1873 0.3341 0.2155 0.0137  0.0095  -0.0825 172  ILE A C   
1131  O O   . ILE A 174  ? 0.2000 0.3589 0.2291 0.0146  0.0095  -0.0881 172  ILE A O   
1132  C CB  . ILE A 174  ? 0.1784 0.3130 0.1980 0.0087  0.0103  -0.0685 172  ILE A CB  
1133  C CG1 . ILE A 174  ? 0.2121 0.3371 0.2299 0.0074  0.0099  -0.0642 172  ILE A CG1 
1134  C CG2 . ILE A 174  ? 0.2450 0.3960 0.2614 0.0071  0.0113  -0.0685 172  ILE A CG2 
1135  C CD1 . ILE A 174  ? 0.2321 0.3540 0.2449 0.0042  0.0106  -0.0557 172  ILE A CD1 
1136  N N   . SER A 175  ? 0.1894 0.3337 0.2185 0.0142  0.0098  -0.0812 173  SER A N   
1137  C CA  . SER A 175  ? 0.1786 0.3349 0.2099 0.0157  0.0101  -0.0862 173  SER A CA  
1138  C C   . SER A 175  ? 0.1890 0.3473 0.2271 0.0194  0.0088  -0.0958 173  SER A C   
1139  O O   . SER A 175  ? 0.2123 0.3836 0.2523 0.0209  0.0090  -0.1018 173  SER A O   
1140  C CB  . SER A 175  ? 0.2135 0.3660 0.2448 0.0154  0.0106  -0.0827 173  SER A CB  
1141  O OG  . SER A 175  ? 0.2640 0.4169 0.2895 0.0119  0.0117  -0.0747 173  SER A OG  
1142  N N   . ARG A 176  ? 0.1805 0.3264 0.2228 0.0209  0.0073  -0.0973 174  ARG A N   
1143  C CA  . ARG A 176  ? 0.1893 0.3361 0.2393 0.0245  0.0057  -0.1062 174  ARG A CA  
1144  C C   . ARG A 176  ? 0.2138 0.3672 0.2645 0.0249  0.0051  -0.1113 174  ARG A C   
1145  O O   . ARG A 176  ? 0.2319 0.3954 0.2869 0.0273  0.0044  -0.1198 174  ARG A O   
1146  C CB  . ARG A 176  ? 0.2101 0.3407 0.2650 0.0258  0.0042  -0.1050 174  ARG A CB  
1147  C CG  . ARG A 176  ? 0.2086 0.3382 0.2730 0.0296  0.0021  -0.1136 174  ARG A CG  
1148  C CD  . ARG A 176  ? 0.2355 0.3495 0.3045 0.0305  0.0008  -0.1107 174  ARG A CD  
1149  N NE  . ARG A 176  ? 0.2223 0.3265 0.2908 0.0293  0.0002  -0.1074 174  ARG A NE  
1150  C CZ  . ARG A 176  ? 0.2321 0.3258 0.2967 0.0273  0.0008  -0.0993 174  ARG A CZ  
1151  N NH1 . ARG A 176  ? 0.2069 0.2973 0.2676 0.0262  0.0018  -0.0935 174  ARG A NH1 
1152  N NH2 . ARG A 176  ? 0.3009 0.3874 0.3654 0.0264  0.0002  -0.0972 174  ARG A NH2 
1153  N N   . CYS A 177  ? 0.1961 0.3447 0.2429 0.0227  0.0053  -0.1066 175  CYS A N   
1154  C CA  . CYS A 177  ? 0.2483 0.4008 0.2964 0.0231  0.0044  -0.1112 175  CYS A CA  
1155  C C   . CYS A 177  ? 0.2361 0.3994 0.2772 0.0205  0.0057  -0.1082 175  CYS A C   
1156  O O   . CYS A 177  ? 0.2981 0.4683 0.3401 0.0211  0.0050  -0.1131 175  CYS A O   
1157  C CB  . CYS A 177  ? 0.2713 0.4088 0.3222 0.0232  0.0031  -0.1092 175  CYS A CB  
1158  S SG  . CYS A 177  ? 0.2864 0.4102 0.3457 0.0259  0.0014  -0.1111 175  CYS A SG  
1159  N N   . GLY A 178  ? 0.2271 0.3916 0.2617 0.0176  0.0073  -0.1002 176  GLY A N   
1160  C CA  . GLY A 178  ? 0.2542 0.4314 0.2830 0.0152  0.0085  -0.0976 176  GLY A CA  
1161  C C   . GLY A 178  ? 0.2238 0.3981 0.2500 0.0136  0.0081  -0.0949 176  GLY A C   
1162  O O   . GLY A 178  ? 0.2418 0.4025 0.2693 0.0136  0.0073  -0.0926 176  GLY A O   
1163  N N   . GLU A 179  ? 0.2305 0.4189 0.2530 0.0124  0.0087  -0.0952 177  GLU A N   
1164  C CA  . GLU A 179  ? 0.2278 0.4157 0.2474 0.0107  0.0084  -0.0924 177  GLU A CA  
1165  C C   . GLU A 179  ? 0.2144 0.3938 0.2388 0.0127  0.0067  -0.0976 177  GLU A C   
1166  O O   . GLU A 179  ? 0.2280 0.3983 0.2508 0.0112  0.0064  -0.0929 177  GLU A O   
1167  C CB  . GLU A 179  ? 0.2426 0.4492 0.2583 0.0095  0.0092  -0.0931 177  GLU A CB  
1168  N N   . PRO A 180  ? 0.2169 0.3991 0.2476 0.0158  0.0054  -0.1071 178  PRO A N   
1169  C CA  . PRO A 180  ? 0.2359 0.4097 0.2717 0.0174  0.0036  -0.1116 178  PRO A CA  
1170  C C   . PRO A 180  ? 0.2096 0.3647 0.2467 0.0167  0.0032  -0.1059 178  PRO A C   
1171  O O   . PRO A 180  ? 0.2321 0.3808 0.2695 0.0160  0.0025  -0.1045 178  PRO A O   
1172  C CB  . PRO A 180  ? 0.2463 0.4251 0.2896 0.0210  0.0023  -0.1223 178  PRO A CB  
1173  C CG  . PRO A 180  ? 0.2405 0.4365 0.2808 0.0211  0.0035  -0.1248 178  PRO A CG  
1174  C CD  . PRO A 180  ? 0.2326 0.4279 0.2660 0.0181  0.0055  -0.1148 178  PRO A CD  
1175  N N   . VAL A 181  ? 0.2190 0.3658 0.2568 0.0169  0.0037  -0.1026 179  VAL A N   
1176  C CA  . VAL A 181  ? 0.2106 0.3406 0.2496 0.0164  0.0033  -0.0973 179  VAL A CA  
1177  C C   . VAL A 181  ? 0.2107 0.3367 0.2429 0.0133  0.0044  -0.0883 179  VAL A C   
1178  O O   . VAL A 181  ? 0.2131 0.3282 0.2459 0.0127  0.0040  -0.0850 179  VAL A O   
1179  C CB  . VAL A 181  ? 0.2151 0.3378 0.2571 0.0178  0.0033  -0.0967 179  VAL A CB  
1180  C CG1 . VAL A 181  ? 0.2098 0.3357 0.2459 0.0159  0.0051  -0.0906 179  VAL A CG1 
1181  C CG2 . VAL A 181  ? 0.2447 0.3513 0.2899 0.0180  0.0024  -0.0933 179  VAL A CG2 
1182  N N   . ILE A 182  ? 0.2068 0.3417 0.2331 0.0112  0.0059  -0.0841 180  ILE A N   
1183  C CA  . ILE A 182  ? 0.2193 0.3509 0.2397 0.0082  0.0067  -0.0757 180  ILE A CA  
1184  C C   . ILE A 182  ? 0.2325 0.3662 0.2523 0.0076  0.0060  -0.0765 180  ILE A C   
1185  O O   . ILE A 182  ? 0.2327 0.3572 0.2511 0.0064  0.0059  -0.0716 180  ILE A O   
1186  C CB  . ILE A 182  ? 0.2235 0.3654 0.2388 0.0061  0.0081  -0.0713 180  ILE A CB  
1187  C CG1 . ILE A 182  ? 0.2154 0.3549 0.2315 0.0067  0.0087  -0.0704 180  ILE A CG1 
1188  C CG2 . ILE A 182  ? 0.2285 0.3669 0.2387 0.0031  0.0087  -0.0626 180  ILE A CG2 
1189  C CD1 . ILE A 182  ? 0.2557 0.4073 0.2680 0.0049  0.0099  -0.0676 180  ILE A CD1 
1190  N N   . ARG A 183  ? 0.2036 0.3501 0.2244 0.0086  0.0056  -0.0828 181  ARG A N   
1191  C CA  A ARG A 183  ? 0.2511 0.4010 0.2717 0.0082  0.0048  -0.0846 181  ARG A CA  
1192  C CA  B ARG A 183  ? 0.2508 0.4007 0.2714 0.0082  0.0048  -0.0847 181  ARG A CA  
1193  C C   . ARG A 183  ? 0.2632 0.3998 0.2887 0.0094  0.0034  -0.0863 181  ARG A C   
1194  O O   . ARG A 183  ? 0.2518 0.3832 0.2757 0.0081  0.0032  -0.0825 181  ARG A O   
1195  C CB  A ARG A 183  ? 0.2727 0.4387 0.2946 0.0096  0.0043  -0.0927 181  ARG A CB  
1196  C CB  B ARG A 183  ? 0.2723 0.4380 0.2946 0.0098  0.0043  -0.0931 181  ARG A CB  
1197  C CG  A ARG A 183  ? 0.3290 0.4990 0.3523 0.0100  0.0031  -0.0969 181  ARG A CG  
1198  C CG  B ARG A 183  ? 0.3294 0.5007 0.3520 0.0098  0.0032  -0.0965 181  ARG A CG  
1199  C CD  A ARG A 183  ? 0.3419 0.5105 0.3598 0.0072  0.0035  -0.0892 181  ARG A CD  
1200  C CD  B ARG A 183  ? 0.3565 0.5358 0.3722 0.0069  0.0041  -0.0898 181  ARG A CD  
1201  N NE  A ARG A 183  ? 0.3437 0.5208 0.3554 0.0048  0.0050  -0.0825 181  ARG A NE  
1202  N NE  B ARG A 183  ? 0.3377 0.5046 0.3512 0.0049  0.0043  -0.0817 181  ARG A NE  
1203  C CZ  A ARG A 183  ? 0.3792 0.5523 0.3864 0.0021  0.0056  -0.0737 181  ARG A CZ  
1204  C CZ  B ARG A 183  ? 0.3773 0.5457 0.3852 0.0021  0.0053  -0.0733 181  ARG A CZ  
1205  N NH1 A ARG A 183  ? 0.3685 0.5293 0.3763 0.0015  0.0050  -0.0704 181  ARG A NH1 
1206  N NH1 B ARG A 183  ? 0.3893 0.5708 0.3933 0.0007  0.0062  -0.0710 181  ARG A NH1 
1207  N NH2 A ARG A 183  ? 0.3796 0.5613 0.3821 -0.0001 0.0067  -0.0680 181  ARG A NH2 
1208  N NH2 B ARG A 183  ? 0.3779 0.5347 0.3845 0.0007  0.0052  -0.0671 181  ARG A NH2 
1209  N N   . ARG A 184  ? 0.2358 0.3669 0.2675 0.0119  0.0025  -0.0917 182  ARG A N   
1210  C CA  . ARG A 184  ? 0.2393 0.3582 0.2765 0.0130  0.0011  -0.0932 182  ARG A CA  
1211  C C   . ARG A 184  ? 0.2471 0.3524 0.2819 0.0113  0.0017  -0.0846 182  ARG A C   
1212  O O   . ARG A 184  ? 0.2632 0.3611 0.2992 0.0108  0.0011  -0.0827 182  ARG A O   
1213  C CB  . ARG A 184  ? 0.2817 0.3979 0.3268 0.0159  -0.0002 -0.1001 182  ARG A CB  
1214  C CG  . ARG A 184  ? 0.3251 0.4524 0.3748 0.0180  -0.0016 -0.1101 182  ARG A CG  
1215  C CD  . ARG A 184  ? 0.3102 0.4318 0.3659 0.0188  -0.0036 -0.1140 182  ARG A CD  
1216  N NE  . ARG A 184  ? 0.3927 0.5037 0.4569 0.0209  -0.0052 -0.1169 182  ARG A NE  
1217  C CZ  . ARG A 184  ? 0.3761 0.4737 0.4437 0.0205  -0.0059 -0.1133 182  ARG A CZ  
1218  N NH1 . ARG A 184  ? 0.3657 0.4584 0.4291 0.0184  -0.0053 -0.1071 182  ARG A NH1 
1219  N NH2 . ARG A 184  ? 0.3355 0.4249 0.4113 0.0225  -0.0074 -0.1159 182  ARG A NH2 
1220  N N   . GLY A 185  ? 0.2350 0.3374 0.2666 0.0106  0.0030  -0.0796 183  GLY A N   
1221  C CA  . GLY A 185  ? 0.2479 0.3387 0.2769 0.0091  0.0036  -0.0717 183  GLY A CA  
1222  C C   . GLY A 185  ? 0.2368 0.3282 0.2606 0.0067  0.0042  -0.0663 183  GLY A C   
1223  O O   . GLY A 185  ? 0.2316 0.3138 0.2556 0.0061  0.0039  -0.0628 183  GLY A O   
1224  N N   . VAL A 186  ? 0.2288 0.3318 0.2482 0.0053  0.0049  -0.0654 184  VAL A N   
1225  C CA  . VAL A 186  ? 0.2641 0.3689 0.2790 0.0030  0.0052  -0.0601 184  VAL A CA  
1226  C C   . VAL A 186  ? 0.2630 0.3661 0.2804 0.0035  0.0041  -0.0628 184  VAL A C   
1227  O O   . VAL A 186  ? 0.2523 0.3484 0.2682 0.0023  0.0040  -0.0581 184  VAL A O   
1228  C CB  . VAL A 186  ? 0.2595 0.3787 0.2701 0.0016  0.0059  -0.0591 184  VAL A CB  
1229  C CG1 . VAL A 186  ? 0.2825 0.4050 0.2895 -0.0005 0.0058  -0.0549 184  VAL A CG1 
1230  C CG2 . VAL A 186  ? 0.2673 0.3864 0.2750 0.0005  0.0070  -0.0544 184  VAL A CG2 
1231  N N   . ASP A 187  ? 0.2320 0.3415 0.2533 0.0052  0.0030  -0.0707 185  ASP A N   
1232  C CA  . ASP A 187  ? 0.2707 0.3794 0.2949 0.0056  0.0018  -0.0737 185  ASP A CA  
1233  C C   . ASP A 187  ? 0.3092 0.4032 0.3375 0.0062  0.0011  -0.0723 185  ASP A C   
1234  O O   . ASP A 187  ? 0.2949 0.3844 0.3232 0.0054  0.0007  -0.0700 185  ASP A O   
1235  C CB  . ASP A 187  ? 0.3024 0.4213 0.3308 0.0075  0.0006  -0.0832 185  ASP A CB  
1236  C CG  . ASP A 187  ? 0.3215 0.4568 0.3455 0.0068  0.0011  -0.0846 185  ASP A CG  
1237  O OD1 . ASP A 187  ? 0.3976 0.5362 0.4155 0.0045  0.0022  -0.0778 185  ASP A OD1 
1238  O OD2 . ASP A 187  ? 0.3613 0.5066 0.3881 0.0086  0.0004  -0.0925 185  ASP A OD2 
1239  N N   . MET A 188  ? 0.2793 0.3662 0.3112 0.0076  0.0011  -0.0733 186  MET A N   
1240  C CA  . MET A 188  ? 0.2884 0.3619 0.3242 0.0081  0.0005  -0.0712 186  MET A CA  
1241  C C   . MET A 188  ? 0.3059 0.3719 0.3368 0.0062  0.0017  -0.0627 186  MET A C   
1242  O O   . MET A 188  ? 0.2922 0.3512 0.3244 0.0058  0.0013  -0.0604 186  MET A O   
1243  C CB  . MET A 188  ? 0.3218 0.3902 0.3618 0.0099  0.0003  -0.0732 186  MET A CB  
1244  C CG  . MET A 188  ? 0.3700 0.4256 0.4144 0.0104  -0.0003 -0.0708 186  MET A CG  
1245  S SD  . MET A 188  ? 0.4818 0.5356 0.5343 0.0115  -0.0024 -0.0765 186  MET A SD  
1246  C CE  . MET A 188  ? 0.4177 0.4815 0.4752 0.0138  -0.0037 -0.0864 186  MET A CE  
1247  N N   . ALA A 189  ? 0.2636 0.3310 0.2893 0.0051  0.0030  -0.0581 187  ALA A N   
1248  C CA  . ALA A 189  ? 0.2799 0.3403 0.3014 0.0035  0.0039  -0.0505 187  ALA A CA  
1249  C C   . ALA A 189  ? 0.2848 0.3481 0.3036 0.0019  0.0038  -0.0481 187  ALA A C   
1250  O O   . ALA A 189  ? 0.2633 0.3191 0.2814 0.0012  0.0039  -0.0438 187  ALA A O   
1251  C CB  . ALA A 189  ? 0.3189 0.3812 0.3359 0.0025  0.0050  -0.0465 187  ALA A CB  
1252  N N   . MET A 190  ? 0.2733 0.3480 0.2906 0.0014  0.0035  -0.0508 188  MET A N   
1253  C CA  . MET A 190  ? 0.2908 0.3691 0.3056 0.0000  0.0033  -0.0486 188  MET A CA  
1254  C C   . MET A 190  ? 0.2896 0.3623 0.3086 0.0007  0.0022  -0.0508 188  MET A C   
1255  O O   . MET A 190  ? 0.3032 0.3716 0.3209 -0.0003 0.0022  -0.0466 188  MET A O   
1256  C CB  . MET A 190  ? 0.2964 0.3893 0.3095 -0.0004 0.0031  -0.0518 188  MET A CB  
1257  C CG  . MET A 190  ? 0.3767 0.4749 0.3868 -0.0020 0.0028  -0.0490 188  MET A CG  
1258  S SD  . MET A 190  ? 0.4472 0.5638 0.4558 -0.0021 0.0024  -0.0539 188  MET A SD  
1259  C CE  . MET A 190  ? 0.3887 0.5110 0.3954 -0.0020 0.0035  -0.0538 188  MET A CE  
1260  N N   . ARG A 191  ? 0.2636 0.3361 0.2882 0.0025  0.0012  -0.0573 189  ARG A N   
1261  C CA  . ARG A 191  ? 0.2949 0.3618 0.3245 0.0031  0.0000  -0.0595 189  ARG A CA  
1262  C C   . ARG A 191  ? 0.2982 0.3522 0.3288 0.0030  0.0005  -0.0544 189  ARG A C   
1263  O O   . ARG A 191  ? 0.2935 0.3429 0.3247 0.0024  0.0002  -0.0519 189  ARG A O   
1264  C CB  . ARG A 191  ? 0.3278 0.3969 0.3641 0.0052  -0.0014 -0.0677 189  ARG A CB  
1265  N N   . MET A 192  ? 0.2579 0.3065 0.2888 0.0037  0.0011  -0.0528 190  MET A N   
1266  C CA  . MET A 192  ? 0.2591 0.2965 0.2912 0.0037  0.0015  -0.0483 190  MET A CA  
1267  C C   . MET A 192  ? 0.3008 0.3356 0.3274 0.0020  0.0026  -0.0415 190  MET A C   
1268  O O   . MET A 192  ? 0.2926 0.3211 0.3201 0.0017  0.0026  -0.0386 190  MET A O   
1269  C CB  . MET A 192  ? 0.2961 0.3292 0.3294 0.0048  0.0020  -0.0480 190  MET A CB  
1270  C CG  . MET A 192  ? 0.2640 0.2973 0.3041 0.0066  0.0007  -0.0542 190  MET A CG  
1271  S SD  . MET A 192  ? 0.4133 0.4417 0.4548 0.0078  0.0011  -0.0534 190  MET A SD  
1272  C CE  . MET A 192  ? 0.3882 0.4046 0.4320 0.0077  0.0011  -0.0480 190  MET A CE  
1273  N N   . MET A 193  ? 0.2799 0.3197 0.3012 0.0010  0.0034  -0.0390 191  MET A N   
1274  C CA  . MET A 193  ? 0.3035 0.3402 0.3203 -0.0004 0.0042  -0.0326 191  MET A CA  
1275  C C   . MET A 193  ? 0.3142 0.3543 0.3298 -0.0016 0.0037  -0.0314 191  MET A C   
1276  O O   . MET A 193  ? 0.3262 0.3617 0.3398 -0.0024 0.0041  -0.0266 191  MET A O   
1277  C CB  . MET A 193  ? 0.3387 0.3791 0.3510 -0.0013 0.0050  -0.0298 191  MET A CB  
1278  C CG  . MET A 193  ? 0.3311 0.3683 0.3444 -0.0003 0.0054  -0.0307 191  MET A CG  
1279  S SD  . MET A 193  ? 0.4547 0.4966 0.4631 -0.0016 0.0063  -0.0272 191  MET A SD  
1280  C CE  . MET A 193  ? 0.4004 0.4326 0.4067 -0.0024 0.0067  -0.0207 191  MET A CE  
1281  N N   . GLY A 194  ? 0.2977 0.3459 0.3145 -0.0015 0.0029  -0.0359 192  GLY A N   
1282  C CA  . GLY A 194  ? 0.3065 0.3590 0.3220 -0.0025 0.0024  -0.0348 192  GLY A CA  
1283  C C   . GLY A 194  ? 0.3294 0.3792 0.3496 -0.0019 0.0014  -0.0378 192  GLY A C   
1284  O O   . GLY A 194  ? 0.3474 0.3982 0.3668 -0.0028 0.0010  -0.0360 192  GLY A O   
1285  N N   . GLU A 195  ? 0.2790 0.3252 0.3044 -0.0005 0.0008  -0.0422 193  GLU A N   
1286  C CA  . GLU A 195  ? 0.2789 0.3234 0.3098 0.0001  -0.0005 -0.0459 193  GLU A CA  
1287  C C   . GLU A 195  ? 0.2671 0.3014 0.3031 0.0010  -0.0006 -0.0455 193  GLU A C   
1288  O O   . GLU A 195  ? 0.2503 0.2816 0.2906 0.0011  -0.0015 -0.0463 193  GLU A O   
1289  C CB  . GLU A 195  ? 0.3145 0.3676 0.3487 0.0010  -0.0018 -0.0535 193  GLU A CB  
1290  C CG  . GLU A 195  ? 0.3983 0.4633 0.4279 0.0003  -0.0017 -0.0547 193  GLU A CG  
1291  C CD  . GLU A 195  ? 0.4919 0.5658 0.5250 0.0014  -0.0030 -0.0629 193  GLU A CD  
1292  O OE1 . GLU A 195  ? 0.5181 0.5883 0.5579 0.0027  -0.0043 -0.0677 193  GLU A OE1 
1293  O OE2 . GLU A 195  ? 0.5956 0.6807 0.6253 0.0012  -0.0029 -0.0647 193  GLU A OE2 
1294  N N   . GLN A 196  ? 0.2990 0.3283 0.3350 0.0017  0.0001  -0.0440 194  GLN A N   
1295  C CA  . GLN A 196  ? 0.3012 0.3217 0.3423 0.0026  -0.0001 -0.0432 194  GLN A CA  
1296  C C   . GLN A 196  ? 0.3074 0.3206 0.3453 0.0020  0.0012  -0.0365 194  GLN A C   
1297  O O   . GLN A 196  ? 0.3443 0.3519 0.3848 0.0019  0.0012  -0.0341 194  GLN A O   
1298  C CB  . GLN A 196  ? 0.2925 0.3126 0.3370 0.0040  -0.0005 -0.0470 194  GLN A CB  
1299  N N   . PHE A 197  ? 0.2986 0.3122 0.3311 0.0017  0.0024  -0.0334 195  PHE A N   
1300  C CA  . PHE A 197  ? 0.3009 0.3083 0.3303 0.0014  0.0036  -0.0276 195  PHE A CA  
1301  C C   . PHE A 197  ? 0.3234 0.3310 0.3502 0.0002  0.0038  -0.0242 195  PHE A C   
1302  O O   . PHE A 197  ? 0.3149 0.3169 0.3407 0.0001  0.0045  -0.0201 195  PHE A O   
1303  C CB  . PHE A 197  ? 0.3162 0.3245 0.3411 0.0013  0.0045  -0.0257 195  PHE A CB  
1304  C CG  . PHE A 197  ? 0.3392 0.3469 0.3665 0.0025  0.0043  -0.0284 195  PHE A CG  
1305  C CD1 . PHE A 197  ? 0.3902 0.3930 0.4231 0.0036  0.0038  -0.0297 195  PHE A CD1 
1306  C CD2 . PHE A 197  ? 0.3564 0.3686 0.3807 0.0024  0.0047  -0.0293 195  PHE A CD2 
1307  C CE1 . PHE A 197  ? 0.4124 0.4146 0.4479 0.0047  0.0035  -0.0320 195  PHE A CE1 
1308  C CE2 . PHE A 197  ? 0.3922 0.4041 0.4190 0.0036  0.0045  -0.0319 195  PHE A CE2 
1309  C CZ  . PHE A 197  ? 0.3777 0.3844 0.4100 0.0048  0.0039  -0.0333 195  PHE A CZ  
1310  N N   . VAL A 198  ? 0.2621 0.2764 0.2876 -0.0005 0.0032  -0.0260 196  VAL A N   
1311  C CA  . VAL A 198  ? 0.2573 0.2725 0.2810 -0.0015 0.0032  -0.0232 196  VAL A CA  
1312  C C   . VAL A 198  ? 0.2680 0.2886 0.2947 -0.0017 0.0019  -0.0275 196  VAL A C   
1313  O O   . VAL A 198  ? 0.3035 0.3294 0.3320 -0.0012 0.0012  -0.0325 196  VAL A O   
1314  C CB  . VAL A 198  ? 0.2653 0.2841 0.2832 -0.0026 0.0037  -0.0197 196  VAL A CB  
1315  C CG1 . VAL A 198  ? 0.2944 0.3076 0.3098 -0.0025 0.0047  -0.0157 196  VAL A CG1 
1316  C CG2 . VAL A 198  ? 0.2598 0.2876 0.2761 -0.0030 0.0033  -0.0226 196  VAL A CG2 
1317  N N   . THR A 199  ? 0.2505 0.2699 0.2782 -0.0022 0.0016  -0.0259 197  THR A N   
1318  C CA  . THR A 199  ? 0.2437 0.2691 0.2737 -0.0025 0.0003  -0.0296 197  THR A CA  
1319  C C   . THR A 199  ? 0.2934 0.3279 0.3189 -0.0034 0.0002  -0.0298 197  THR A C   
1320  O O   . THR A 199  ? 0.3348 0.3768 0.3615 -0.0033 -0.0009 -0.0345 197  THR A O   
1321  C CB  . THR A 199  ? 0.2637 0.2854 0.2959 -0.0029 0.0001  -0.0274 197  THR A CB  
1322  O OG1 . THR A 199  ? 0.2956 0.3093 0.3318 -0.0022 0.0004  -0.0266 197  THR A OG1 
1323  C CG2 . THR A 199  ? 0.3051 0.3325 0.3405 -0.0032 -0.0014 -0.0317 197  THR A CG2 
1324  N N   . GLY A 200  ? 0.2635 0.2978 0.2840 -0.0042 0.0010  -0.0248 198  GLY A N   
1325  C CA  . GLY A 200  ? 0.2804 0.3233 0.2968 -0.0052 0.0008  -0.0239 198  GLY A CA  
1326  C C   . GLY A 200  ? 0.2737 0.3143 0.2859 -0.0059 0.0018  -0.0183 198  GLY A C   
1327  O O   . GLY A 200  ? 0.2509 0.2832 0.2632 -0.0056 0.0025  -0.0151 198  GLY A O   
1328  N N   . GLU A 201  ? 0.2817 0.3301 0.2906 -0.0069 0.0017  -0.0173 199  GLU A N   
1329  C CA  . GLU A 201  ? 0.2931 0.3397 0.2987 -0.0077 0.0023  -0.0120 199  GLU A CA  
1330  C C   . GLU A 201  ? 0.2941 0.3378 0.2987 -0.0085 0.0020  -0.0068 199  GLU A C   
1331  O O   . GLU A 201  ? 0.2993 0.3371 0.3029 -0.0087 0.0025  -0.0027 199  GLU A O   
1332  C CB  . GLU A 201  ? 0.3126 0.3690 0.3153 -0.0087 0.0023  -0.0120 199  GLU A CB  
1333  C CG  . GLU A 201  ? 0.4201 0.4754 0.4200 -0.0098 0.0027  -0.0065 199  GLU A CG  
1334  C CD  . GLU A 201  ? 0.5316 0.5978 0.5293 -0.0110 0.0026  -0.0062 199  GLU A CD  
1335  O OE1 . GLU A 201  ? 0.5721 0.6461 0.5701 -0.0106 0.0024  -0.0110 199  GLU A OE1 
1336  O OE2 . GLU A 201  ? 0.6204 0.6874 0.6161 -0.0124 0.0026  -0.0011 199  GLU A OE2 
1337  N N   . THR A 202  ? 0.2765 0.3244 0.2819 -0.0089 0.0012  -0.0073 200  THR A N   
1338  C CA  . THR A 202  ? 0.2722 0.3182 0.2773 -0.0096 0.0007  -0.0028 200  THR A CA  
1339  C C   . THR A 202  ? 0.2525 0.2959 0.2607 -0.0089 0.0003  -0.0051 200  THR A C   
1340  O O   . THR A 202  ? 0.2381 0.2835 0.2486 -0.0082 0.0001  -0.0102 200  THR A O   
1341  C CB  . THR A 202  ? 0.2569 0.3124 0.2598 -0.0111 -0.0002 -0.0004 200  THR A CB  
1342  O OG1 . THR A 202  ? 0.2989 0.3624 0.3026 -0.0110 -0.0009 -0.0051 200  THR A OG1 
1343  C CG2 . THR A 202  ? 0.3163 0.3762 0.3165 -0.0120 0.0001  0.0019  200  THR A CG2 
1344  N N   . ILE A 203  ? 0.2486 0.2879 0.2572 -0.0090 0.0001  -0.0015 201  ILE A N   
1345  C CA  . ILE A 203  ? 0.2464 0.2832 0.2582 -0.0085 -0.0002 -0.0032 201  ILE A CA  
1346  C C   . ILE A 203  ? 0.2608 0.3064 0.2734 -0.0089 -0.0014 -0.0066 201  ILE A C   
1347  O O   . ILE A 203  ? 0.2560 0.3013 0.2720 -0.0083 -0.0018 -0.0107 201  ILE A O   
1348  C CB  . ILE A 203  ? 0.2434 0.2747 0.2557 -0.0084 -0.0002 0.0013  201  ILE A CB  
1349  C CG1 . ILE A 203  ? 0.2361 0.2642 0.2521 -0.0077 -0.0003 -0.0005 201  ILE A CG1 
1350  C CG2 . ILE A 203  ? 0.2692 0.3057 0.2796 -0.0095 -0.0012 0.0052  201  ILE A CG2 
1351  C CD1 . ILE A 203  ? 0.2146 0.2372 0.2332 -0.0067 0.0005  -0.0036 201  ILE A CD1 
1352  N N   . ARG A 204  ? 0.2293 0.2834 0.2392 -0.0100 -0.0021 -0.0050 202  ARG A N   
1353  C CA  . ARG A 204  ? 0.2569 0.3206 0.2671 -0.0104 -0.0032 -0.0083 202  ARG A CA  
1354  C C   . ARG A 204  ? 0.2591 0.3264 0.2709 -0.0097 -0.0033 -0.0150 202  ARG A C   
1355  O O   . ARG A 204  ? 0.2557 0.3260 0.2703 -0.0093 -0.0042 -0.0197 202  ARG A O   
1356  C CB  . ARG A 204  ? 0.3373 0.4102 0.3441 -0.0118 -0.0039 -0.0046 202  ARG A CB  
1357  C CG  . ARG A 204  ? 0.4158 0.4886 0.4226 -0.0125 -0.0048 0.0002  202  ARG A CG  
1358  C CD  . ARG A 204  ? 0.4085 0.4875 0.4123 -0.0139 -0.0052 0.0057  202  ARG A CD  
1359  N NE  . ARG A 204  ? 0.4260 0.5036 0.4304 -0.0145 -0.0062 0.0108  202  ARG A NE  
1360  C CZ  . ARG A 204  ? 0.3931 0.4613 0.3989 -0.0140 -0.0059 0.0144  202  ARG A CZ  
1361  N NH1 . ARG A 204  ? 0.3627 0.4220 0.3689 -0.0132 -0.0047 0.0138  202  ARG A NH1 
1362  N NH2 . ARG A 204  ? 0.3296 0.3976 0.3363 -0.0144 -0.0069 0.0186  202  ARG A NH2 
1363  N N   . GLU A 205  ? 0.2596 0.3269 0.2698 -0.0095 -0.0024 -0.0157 203  GLU A N   
1364  C CA  . GLU A 205  ? 0.2828 0.3528 0.2950 -0.0085 -0.0025 -0.0222 203  GLU A CA  
1365  C C   . GLU A 205  ? 0.2674 0.3288 0.2844 -0.0073 -0.0025 -0.0254 203  GLU A C   
1366  O O   . GLU A 205  ? 0.2649 0.3291 0.2856 -0.0067 -0.0034 -0.0312 203  GLU A O   
1367  C CB  . GLU A 205  ? 0.2778 0.3485 0.2875 -0.0085 -0.0015 -0.0216 203  GLU A CB  
1368  C CG  . GLU A 205  ? 0.3221 0.3966 0.3337 -0.0074 -0.0016 -0.0283 203  GLU A CG  
1369  C CD  . GLU A 205  ? 0.3726 0.4495 0.3814 -0.0076 -0.0007 -0.0274 203  GLU A CD  
1370  O OE1 . GLU A 205  ? 0.3693 0.4379 0.3780 -0.0073 0.0003  -0.0247 203  GLU A OE1 
1371  O OE2 . GLU A 205  ? 0.4001 0.4880 0.4070 -0.0080 -0.0009 -0.0292 203  GLU A OE2 
1372  N N   . ALA A 206  ? 0.2535 0.3048 0.2710 -0.0071 -0.0016 -0.0216 204  ALA A N   
1373  C CA  . ALA A 206  ? 0.2417 0.2852 0.2640 -0.0061 -0.0015 -0.0237 204  ALA A CA  
1374  C C   . ALA A 206  ? 0.2449 0.2898 0.2708 -0.0062 -0.0027 -0.0257 204  ALA A C   
1375  O O   . ALA A 206  ? 0.2451 0.2885 0.2759 -0.0056 -0.0034 -0.0302 204  ALA A O   
1376  C CB  . ALA A 206  ? 0.2625 0.2964 0.2842 -0.0059 -0.0003 -0.0187 204  ALA A CB  
1377  N N   . LEU A 207  ? 0.2317 0.2793 0.2556 -0.0071 -0.0030 -0.0223 205  LEU A N   
1378  C CA  . LEU A 207  ? 0.2364 0.2857 0.2636 -0.0073 -0.0042 -0.0240 205  LEU A CA  
1379  C C   . LEU A 207  ? 0.2553 0.3134 0.2844 -0.0072 -0.0056 -0.0304 205  LEU A C   
1380  O O   . LEU A 207  ? 0.2551 0.3125 0.2894 -0.0068 -0.0066 -0.0344 205  LEU A O   
1381  C CB  . LEU A 207  ? 0.2397 0.2907 0.2642 -0.0082 -0.0044 -0.0190 205  LEU A CB  
1382  C CG  . LEU A 207  ? 0.2625 0.3046 0.2867 -0.0080 -0.0033 -0.0136 205  LEU A CG  
1383  C CD1 . LEU A 207  ? 0.2396 0.2845 0.2607 -0.0088 -0.0036 -0.0085 205  LEU A CD1 
1384  C CD2 . LEU A 207  ? 0.2368 0.2730 0.2660 -0.0075 -0.0034 -0.0145 205  LEU A CD2 
1385  N N   . LYS A 208  ? 0.2422 0.3091 0.2677 -0.0075 -0.0058 -0.0316 206  LYS A N   
1386  C CA  . LYS A 208  ? 0.2830 0.3593 0.3101 -0.0072 -0.0071 -0.0383 206  LYS A CA  
1387  C C   . LYS A 208  ? 0.2955 0.3680 0.3280 -0.0059 -0.0074 -0.0443 206  LYS A C   
1388  O O   . LYS A 208  ? 0.3139 0.3891 0.3512 -0.0055 -0.0089 -0.0501 206  LYS A O   
1389  C CB  . LYS A 208  ? 0.3301 0.4168 0.3521 -0.0076 -0.0069 -0.0381 206  LYS A CB  
1390  N N   . ARG A 209  ? 0.2776 0.3435 0.3099 -0.0053 -0.0062 -0.0431 207  ARG A N   
1391  C CA  . ARG A 209  ? 0.2811 0.3430 0.3186 -0.0041 -0.0066 -0.0482 207  ARG A CA  
1392  C C   . ARG A 209  ? 0.3058 0.3586 0.3495 -0.0039 -0.0070 -0.0481 207  ARG A C   
1393  O O   . ARG A 209  ? 0.3487 0.3985 0.3982 -0.0029 -0.0078 -0.0525 207  ARG A O   
1394  C CB  . ARG A 209  ? 0.2741 0.3323 0.3092 -0.0036 -0.0052 -0.0463 207  ARG A CB  
1395  C CG  . ARG A 209  ? 0.3100 0.3780 0.3404 -0.0038 -0.0049 -0.0476 207  ARG A CG  
1396  C CD  . ARG A 209  ? 0.3299 0.3939 0.3579 -0.0035 -0.0035 -0.0453 207  ARG A CD  
1397  N NE  . ARG A 209  ? 0.3460 0.4196 0.3694 -0.0039 -0.0031 -0.0456 207  ARG A NE  
1398  C CZ  . ARG A 209  ? 0.3581 0.4305 0.3787 -0.0039 -0.0020 -0.0433 207  ARG A CZ  
1399  N NH1 . ARG A 209  ? 0.3735 0.4358 0.3950 -0.0034 -0.0011 -0.0407 207  ARG A NH1 
1400  N NH2 . ARG A 209  ? 0.4666 0.5489 0.4834 -0.0044 -0.0017 -0.0436 207  ARG A NH2 
1401  N N   . SER A 210  ? 0.3083 0.3571 0.3513 -0.0046 -0.0067 -0.0432 208  SER A N   
1402  C CA  . SER A 210  ? 0.2698 0.3104 0.3186 -0.0045 -0.0069 -0.0424 208  SER A CA  
1403  C C   . SER A 210  ? 0.2767 0.3207 0.3312 -0.0047 -0.0089 -0.0471 208  SER A C   
1404  O O   . SER A 210  ? 0.2701 0.3081 0.3310 -0.0046 -0.0095 -0.0478 208  SER A O   
1405  C CB  . SER A 210  ? 0.2714 0.3065 0.3172 -0.0052 -0.0056 -0.0352 208  SER A CB  
1406  O OG  . SER A 210  ? 0.2714 0.3023 0.3130 -0.0049 -0.0040 -0.0313 208  SER A OG  
1407  N N   . LYS A 211  ? 0.2918 0.3455 0.3444 -0.0050 -0.0100 -0.0503 209  LYS A N   
1408  C CA  . LYS A 211  ? 0.3256 0.3831 0.3832 -0.0052 -0.0119 -0.0547 209  LYS A CA  
1409  C C   . LYS A 211  ? 0.3086 0.3641 0.3744 -0.0043 -0.0135 -0.0614 209  LYS A C   
1410  O O   . LYS A 211  ? 0.3240 0.3769 0.3965 -0.0045 -0.0149 -0.0632 209  LYS A O   
1411  C CB  . LYS A 211  ? 0.3366 0.4062 0.3901 -0.0056 -0.0128 -0.0570 209  LYS A CB  
1412  N N   . GLU A 212  ? 0.2958 0.3524 0.3618 -0.0033 -0.0134 -0.0649 210  GLU A N   
1413  C CA  . GLU A 212  ? 0.3398 0.3952 0.4141 -0.0022 -0.0152 -0.0719 210  GLU A CA  
1414  C C   . GLU A 212  ? 0.3522 0.3966 0.4337 -0.0024 -0.0154 -0.0695 210  GLU A C   
1415  O O   . GLU A 212  ? 0.3617 0.4050 0.4512 -0.0024 -0.0174 -0.0733 210  GLU A O   
1416  C CB  . GLU A 212  ? 0.3877 0.4454 0.4606 -0.0010 -0.0147 -0.0751 210  GLU A CB  
1417  C CG  . GLU A 212  ? 0.4538 0.5096 0.5357 0.0003  -0.0166 -0.0822 210  GLU A CG  
1418  C CD  . GLU A 212  ? 0.5304 0.5888 0.6108 0.0016  -0.0162 -0.0853 210  GLU A CD  
1419  O OE1 . GLU A 212  ? 0.5692 0.6307 0.6414 0.0014  -0.0143 -0.0816 210  GLU A OE1 
1420  O OE2 . GLU A 212  ? 0.6560 0.7134 0.7439 0.0029  -0.0178 -0.0915 210  GLU A OE2 
1421  N N   . LEU A 213  ? 0.3067 0.3433 0.3855 -0.0025 -0.0134 -0.0630 211  LEU A N   
1422  C CA  . LEU A 213  ? 0.3008 0.3279 0.3861 -0.0027 -0.0135 -0.0601 211  LEU A CA  
1423  C C   . LEU A 213  ? 0.2944 0.3190 0.3806 -0.0040 -0.0134 -0.0558 211  LEU A C   
1424  O O   . LEU A 213  ? 0.2914 0.3106 0.3851 -0.0043 -0.0142 -0.0551 211  LEU A O   
1425  C CB  . LEU A 213  ? 0.2922 0.3126 0.3746 -0.0023 -0.0116 -0.0552 211  LEU A CB  
1426  C CG  . LEU A 213  ? 0.3041 0.3251 0.3883 -0.0010 -0.0120 -0.0597 211  LEU A CG  
1427  C CD1 . LEU A 213  ? 0.3267 0.3408 0.4089 -0.0006 -0.0103 -0.0547 211  LEU A CD1 
1428  C CD2 . LEU A 213  ? 0.3852 0.4056 0.4800 -0.0004 -0.0147 -0.0662 211  LEU A CD2 
1429  N N   . GLU A 214  ? 0.2670 0.2958 0.3462 -0.0046 -0.0124 -0.0526 212  GLU A N   
1430  C CA  . GLU A 214  ? 0.2831 0.3107 0.3638 -0.0057 -0.0126 -0.0494 212  GLU A CA  
1431  C C   . GLU A 214  ? 0.3204 0.3513 0.4087 -0.0059 -0.0151 -0.0552 212  GLU A C   
1432  O O   . GLU A 214  ? 0.3127 0.3397 0.4067 -0.0067 -0.0157 -0.0536 212  GLU A O   
1433  C CB  . GLU A 214  ? 0.2680 0.3001 0.3405 -0.0062 -0.0114 -0.0455 212  GLU A CB  
1434  C CG  . GLU A 214  ? 0.2587 0.2856 0.3253 -0.0061 -0.0090 -0.0387 212  GLU A CG  
1435  C CD  . GLU A 214  ? 0.2927 0.3234 0.3523 -0.0066 -0.0082 -0.0347 212  GLU A CD  
1436  O OE1 . GLU A 214  ? 0.3396 0.3780 0.3977 -0.0070 -0.0093 -0.0371 212  GLU A OE1 
1437  O OE2 . GLU A 214  ? 0.3367 0.3627 0.3924 -0.0066 -0.0065 -0.0291 212  GLU A OE2 
1438  N N   . GLU A 215  ? 0.2968 0.3353 0.3856 -0.0054 -0.0167 -0.0621 213  GLU A N   
1439  C CA  . GLU A 215  ? 0.3337 0.3761 0.4300 -0.0055 -0.0194 -0.0686 213  GLU A CA  
1440  C C   . GLU A 215  ? 0.4026 0.4380 0.5095 -0.0053 -0.0209 -0.0711 213  GLU A C   
1441  O O   . GLU A 215  ? 0.4200 0.4559 0.5348 -0.0057 -0.0231 -0.0747 213  GLU A O   
1442  C CB  . GLU A 215  ? 0.3741 0.4271 0.4682 -0.0047 -0.0207 -0.0759 213  GLU A CB  
1443  N N   . LYS A 216  ? 0.3501 0.3792 0.4578 -0.0046 -0.0198 -0.0691 214  LYS A N   
1444  C CA  . LYS A 216  ? 0.3709 0.3928 0.4888 -0.0044 -0.0212 -0.0703 214  LYS A CA  
1445  C C   . LYS A 216  ? 0.3981 0.4119 0.5186 -0.0055 -0.0201 -0.0626 214  LYS A C   
1446  O O   . LYS A 216  ? 0.4578 0.4658 0.5875 -0.0058 -0.0213 -0.0626 214  LYS A O   
1447  C CB  . LYS A 216  ? 0.3516 0.3715 0.4697 -0.0031 -0.0209 -0.0723 214  LYS A CB  
1448  N N   . GLY A 217  ? 0.3135 0.3270 0.4264 -0.0062 -0.0178 -0.0561 215  GLY A N   
1449  C CA  . GLY A 217  ? 0.3311 0.3383 0.4458 -0.0072 -0.0166 -0.0490 215  GLY A CA  
1450  C C   . GLY A 217  ? 0.2886 0.2915 0.3965 -0.0068 -0.0138 -0.0424 215  GLY A C   
1451  O O   . GLY A 217  ? 0.2940 0.2921 0.4030 -0.0074 -0.0126 -0.0365 215  GLY A O   
1452  N N   . PHE A 218  ? 0.2699 0.2745 0.3710 -0.0058 -0.0128 -0.0434 216  PHE A N   
1453  C CA  . PHE A 218  ? 0.2179 0.2191 0.3122 -0.0055 -0.0102 -0.0373 216  PHE A CA  
1454  C C   . PHE A 218  ? 0.2425 0.2465 0.3288 -0.0059 -0.0087 -0.0336 216  PHE A C   
1455  O O   . PHE A 218  ? 0.2632 0.2730 0.3480 -0.0063 -0.0096 -0.0360 216  PHE A O   
1456  C CB  . PHE A 218  ? 0.2167 0.2189 0.3068 -0.0044 -0.0097 -0.0397 216  PHE A CB  
1457  C CG  . PHE A 218  ? 0.2486 0.2470 0.3459 -0.0037 -0.0109 -0.0423 216  PHE A CG  
1458  C CD1 . PHE A 218  ? 0.3108 0.3117 0.4152 -0.0033 -0.0134 -0.0494 216  PHE A CD1 
1459  C CD2 . PHE A 218  ? 0.2508 0.2434 0.3477 -0.0033 -0.0096 -0.0379 216  PHE A CD2 
1460  C CE1 . PHE A 218  ? 0.2807 0.2778 0.3924 -0.0026 -0.0146 -0.0518 216  PHE A CE1 
1461  C CE2 . PHE A 218  ? 0.2833 0.2723 0.3870 -0.0026 -0.0107 -0.0400 216  PHE A CE2 
1462  C CZ  . PHE A 218  ? 0.2622 0.2533 0.3735 -0.0022 -0.0133 -0.0469 216  PHE A CZ  
1463  N N   . SER A 219  ? 0.2161 0.2163 0.2976 -0.0058 -0.0066 -0.0276 217  SER A N   
1464  C CA  . SER A 219  ? 0.2196 0.2220 0.2933 -0.0059 -0.0051 -0.0240 217  SER A CA  
1465  C C   . SER A 219  ? 0.2165 0.2172 0.2837 -0.0051 -0.0035 -0.0219 217  SER A C   
1466  O O   . SER A 219  ? 0.2073 0.2056 0.2762 -0.0045 -0.0035 -0.0232 217  SER A O   
1467  C CB  . SER A 219  ? 0.2358 0.2354 0.3104 -0.0064 -0.0042 -0.0189 217  SER A CB  
1468  O OG  . SER A 219  ? 0.2645 0.2583 0.3411 -0.0061 -0.0030 -0.0152 217  SER A OG  
1469  N N   . TYR A 220  ? 0.2148 0.2169 0.2753 -0.0051 -0.0023 -0.0186 218  TYR A N   
1470  C CA  . TYR A 220  ? 0.2055 0.2067 0.2598 -0.0045 -0.0010 -0.0167 218  TYR A CA  
1471  C C   . TYR A 220  ? 0.2023 0.2004 0.2525 -0.0044 0.0006  -0.0112 218  TYR A C   
1472  O O   . TYR A 220  ? 0.2119 0.2107 0.2623 -0.0047 0.0007  -0.0090 218  TYR A O   
1473  C CB  . TYR A 220  ? 0.2185 0.2261 0.2681 -0.0047 -0.0016 -0.0193 218  TYR A CB  
1474  C CG  . TYR A 220  ? 0.2239 0.2344 0.2760 -0.0044 -0.0027 -0.0249 218  TYR A CG  
1475  C CD1 . TYR A 220  ? 0.2314 0.2456 0.2887 -0.0046 -0.0045 -0.0298 218  TYR A CD1 
1476  C CD2 . TYR A 220  ? 0.2144 0.2241 0.2642 -0.0037 -0.0020 -0.0256 218  TYR A CD2 
1477  C CE1 . TYR A 220  ? 0.2271 0.2441 0.2872 -0.0041 -0.0056 -0.0355 218  TYR A CE1 
1478  C CE2 . TYR A 220  ? 0.2163 0.2289 0.2688 -0.0032 -0.0031 -0.0310 218  TYR A CE2 
1479  C CZ  . TYR A 220  ? 0.2306 0.2468 0.2883 -0.0033 -0.0049 -0.0360 218  TYR A CZ  
1480  O OH  . TYR A 220  ? 0.2569 0.2763 0.3178 -0.0026 -0.0061 -0.0420 218  TYR A OH  
1481  N N   . SER A 221  ? 0.2008 0.1958 0.2478 -0.0037 0.0019  -0.0091 219  SER A N   
1482  C CA  . SER A 221  ? 0.2048 0.1977 0.2471 -0.0033 0.0033  -0.0047 219  SER A CA  
1483  C C   . SER A 221  ? 0.1987 0.1926 0.2358 -0.0030 0.0036  -0.0050 219  SER A C   
1484  O O   . SER A 221  ? 0.2509 0.2431 0.2883 -0.0026 0.0039  -0.0062 219  SER A O   
1485  C CB  . SER A 221  ? 0.2191 0.2070 0.2633 -0.0027 0.0045  -0.0016 219  SER A CB  
1486  O OG  . SER A 221  ? 0.2367 0.2232 0.2764 -0.0022 0.0057  0.0019  219  SER A OG  
1487  N N   . TYR A 222  ? 0.1827 0.1794 0.2156 -0.0034 0.0036  -0.0036 220  TYR A N   
1488  C CA  . TYR A 222  ? 0.2123 0.2108 0.2408 -0.0034 0.0037  -0.0039 220  TYR A CA  
1489  C C   . TYR A 222  ? 0.2220 0.2164 0.2473 -0.0028 0.0049  -0.0004 220  TYR A C   
1490  O O   . TYR A 222  ? 0.2156 0.2078 0.2403 -0.0025 0.0054  0.0025  220  TYR A O   
1491  C CB  . TYR A 222  ? 0.1936 0.1982 0.2195 -0.0043 0.0028  -0.0041 220  TYR A CB  
1492  C CG  . TYR A 222  ? 0.1916 0.2013 0.2204 -0.0048 0.0015  -0.0082 220  TYR A CG  
1493  C CD1 . TYR A 222  ? 0.2145 0.2275 0.2438 -0.0048 0.0010  -0.0123 220  TYR A CD1 
1494  C CD2 . TYR A 222  ? 0.2031 0.2144 0.2345 -0.0052 0.0008  -0.0082 220  TYR A CD2 
1495  C CE1 . TYR A 222  ? 0.2100 0.2280 0.2424 -0.0050 -0.0003 -0.0167 220  TYR A CE1 
1496  C CE2 . TYR A 222  ? 0.2125 0.2285 0.2468 -0.0056 -0.0005 -0.0124 220  TYR A CE2 
1497  C CZ  . TYR A 222  ? 0.2034 0.2228 0.2383 -0.0055 -0.0011 -0.0167 220  TYR A CZ  
1498  O OH  . TYR A 222  ? 0.2451 0.2696 0.2833 -0.0057 -0.0026 -0.0214 220  TYR A OH  
1499  N N   . ASP A 223  ? 0.2423 0.2361 0.2657 -0.0025 0.0053  -0.0012 221  ASP A N   
1500  C CA  . ASP A 223  ? 0.2771 0.2673 0.2975 -0.0019 0.0062  0.0014  221  ASP A CA  
1501  C C   . ASP A 223  ? 0.2867 0.2800 0.3033 -0.0025 0.0059  0.0016  221  ASP A C   
1502  O O   . ASP A 223  ? 0.2801 0.2761 0.2963 -0.0028 0.0056  -0.0008 221  ASP A O   
1503  C CB  . ASP A 223  ? 0.2974 0.2843 0.3194 -0.0011 0.0069  0.0004  221  ASP A CB  
1504  C CG  . ASP A 223  ? 0.3339 0.3181 0.3526 -0.0005 0.0077  0.0022  221  ASP A CG  
1505  O OD1 . ASP A 223  ? 0.3729 0.3564 0.3890 -0.0004 0.0079  0.0046  221  ASP A OD1 
1506  O OD2 . ASP A 223  ? 0.4470 0.4299 0.4661 0.0000  0.0079  0.0011  221  ASP A OD2 
1507  N N   . MET A 224  ? 0.2710 0.2643 0.2855 -0.0028 0.0058  0.0046  222  MET A N   
1508  C CA  . MET A 224  ? 0.2943 0.2904 0.3057 -0.0036 0.0053  0.0058  222  MET A CA  
1509  C C   . MET A 224  ? 0.3252 0.3183 0.3347 -0.0031 0.0059  0.0063  222  MET A C   
1510  O O   . MET A 224  ? 0.3757 0.3705 0.3830 -0.0038 0.0056  0.0078  222  MET A O   
1511  C CB  . MET A 224  ? 0.2805 0.2773 0.2912 -0.0040 0.0046  0.0089  222  MET A CB  
1512  C CG  . MET A 224  ? 0.3112 0.3117 0.3236 -0.0046 0.0039  0.0085  222  MET A CG  
1513  S SD  . MET A 224  ? 0.3576 0.3656 0.3701 -0.0056 0.0031  0.0049  222  MET A SD  
1514  C CE  . MET A 224  ? 0.4312 0.4439 0.4403 -0.0068 0.0026  0.0072  222  MET A CE  
1515  N N   . LEU A 225  ? 0.3252 0.3142 0.3358 -0.0020 0.0068  0.0055  223  LEU A N   
1516  C CA  . LEU A 225  ? 0.3426 0.3292 0.3518 -0.0015 0.0074  0.0053  223  LEU A CA  
1517  C C   . LEU A 225  ? 0.3899 0.3735 0.3972 -0.0011 0.0075  0.0080  223  LEU A C   
1518  O O   . LEU A 225  ? 0.4233 0.4053 0.4292 -0.0007 0.0078  0.0079  223  LEU A O   
1519  C CB  . LEU A 225  ? 0.3785 0.3690 0.3867 -0.0021 0.0071  0.0032  223  LEU A CB  
1520  C CG  . LEU A 225  ? 0.3373 0.3299 0.3481 -0.0019 0.0069  -0.0004 223  LEU A CG  
1521  C CD1 . LEU A 225  ? 0.4265 0.4244 0.4362 -0.0026 0.0065  -0.0027 223  LEU A CD1 
1522  C CD2 . LEU A 225  ? 0.4079 0.3959 0.4209 -0.0008 0.0076  -0.0012 223  LEU A CD2 
1523  N N   . GLY A 226  ? 0.3519 0.3347 0.3594 -0.0011 0.0072  0.0100  224  GLY A N   
1524  C CA  . GLY A 226  ? 0.3587 0.3383 0.3653 -0.0004 0.0072  0.0119  224  GLY A CA  
1525  C C   . GLY A 226  ? 0.3439 0.3197 0.3508 0.0012  0.0082  0.0116  224  GLY A C   
1526  O O   . GLY A 226  ? 0.3209 0.2962 0.3294 0.0017  0.0089  0.0111  224  GLY A O   
1527  N N   . GLU A 227  ? 0.3058 0.2796 0.3113 0.0018  0.0083  0.0119  225  GLU A N   
1528  C CA  . GLU A 227  ? 0.2790 0.2501 0.2843 0.0033  0.0093  0.0116  225  GLU A CA  
1529  C C   . GLU A 227  ? 0.2852 0.2546 0.2890 0.0038  0.0089  0.0119  225  GLU A C   
1530  O O   . GLU A 227  ? 0.2649 0.2351 0.2679 0.0027  0.0081  0.0120  225  GLU A O   
1531  C CB  . GLU A 227  ? 0.3334 0.3049 0.3391 0.0033  0.0099  0.0102  225  GLU A CB  
1532  C CG  . GLU A 227  ? 0.3786 0.3482 0.3842 0.0047  0.0109  0.0103  225  GLU A CG  
1533  C CD  . GLU A 227  ? 0.4870 0.4569 0.4937 0.0046  0.0112  0.0092  225  GLU A CD  
1534  O OE1 . GLU A 227  ? 0.4054 0.3771 0.4134 0.0036  0.0108  0.0080  225  GLU A OE1 
1535  O OE2 . GLU A 227  ? 0.4794 0.4482 0.4859 0.0056  0.0118  0.0094  225  GLU A OE2 
1536  N N   . ALA A 228  ? 0.2667 0.2342 0.2705 0.0053  0.0094  0.0120  226  ALA A N   
1537  C CA  . ALA A 228  ? 0.2774 0.2434 0.2800 0.0061  0.0091  0.0116  226  ALA A CA  
1538  C C   . ALA A 228  ? 0.2479 0.2135 0.2508 0.0052  0.0076  0.0122  226  ALA A C   
1539  O O   . ALA A 228  ? 0.2745 0.2400 0.2766 0.0045  0.0070  0.0120  226  ALA A O   
1540  C CB  . ALA A 228  ? 0.3234 0.2895 0.3247 0.0062  0.0097  0.0107  226  ALA A CB  
1541  N N   . ALA A 229  ? 0.2411 0.2065 0.2456 0.0051  0.0069  0.0132  227  ALA A N   
1542  C CA  . ALA A 229  ? 0.2373 0.2020 0.2430 0.0044  0.0052  0.0143  227  ALA A CA  
1543  C C   . ALA A 229  ? 0.2418 0.2042 0.2475 0.0054  0.0047  0.0132  227  ALA A C   
1544  O O   . ALA A 229  ? 0.2448 0.2062 0.2503 0.0073  0.0054  0.0118  227  ALA A O   
1545  C CB  . ALA A 229  ? 0.2295 0.1940 0.2375 0.0047  0.0045  0.0154  227  ALA A CB  
1546  N N   . THR A 230  ? 0.2336 0.1957 0.2397 0.0042  0.0035  0.0140  228  THR A N   
1547  C CA  . THR A 230  ? 0.2540 0.2140 0.2607 0.0049  0.0026  0.0129  228  THR A CA  
1548  C C   . THR A 230  ? 0.2341 0.1921 0.2443 0.0050  0.0006  0.0137  228  THR A C   
1549  O O   . THR A 230  ? 0.2370 0.1929 0.2486 0.0063  -0.0002 0.0120  228  THR A O   
1550  C CB  . THR A 230  ? 0.2837 0.2445 0.2892 0.0034  0.0023  0.0132  228  THR A CB  
1551  O OG1 . THR A 230  ? 0.3466 0.3093 0.3495 0.0034  0.0039  0.0123  228  THR A OG1 
1552  C CG2 . THR A 230  ? 0.3202 0.2790 0.3263 0.0041  0.0014  0.0117  228  THR A CG2 
1553  N N   . THR A 231  ? 0.2342 0.1930 0.2461 0.0036  -0.0003 0.0161  229  THR A N   
1554  C CA  . THR A 231  ? 0.2267 0.1837 0.2427 0.0034  -0.0025 0.0175  229  THR A CA  
1555  C C   . THR A 231  ? 0.2271 0.1849 0.2446 0.0036  -0.0026 0.0189  229  THR A C   
1556  O O   . THR A 231  ? 0.2298 0.1901 0.2451 0.0033  -0.0012 0.0192  229  THR A O   
1557  C CB  . THR A 231  ? 0.2405 0.1983 0.2580 0.0009  -0.0041 0.0203  229  THR A CB  
1558  O OG1 . THR A 231  ? 0.2518 0.2134 0.2678 -0.0009 -0.0036 0.0227  229  THR A OG1 
1559  C CG2 . THR A 231  ? 0.2676 0.2253 0.2834 0.0005  -0.0038 0.0191  229  THR A CG2 
1560  N N   . ALA A 232  ? 0.2251 0.1808 0.2467 0.0042  -0.0044 0.0196  230  ALA A N   
1561  C CA  . ALA A 232  ? 0.2408 0.1974 0.2644 0.0041  -0.0050 0.0215  230  ALA A CA  
1562  C C   . ALA A 232  ? 0.2463 0.2064 0.2689 0.0016  -0.0051 0.0248  230  ALA A C   
1563  O O   . ALA A 232  ? 0.2560 0.2185 0.2776 0.0014  -0.0043 0.0255  230  ALA A O   
1564  C CB  . ALA A 232  ? 0.2386 0.1923 0.2676 0.0049  -0.0074 0.0220  230  ALA A CB  
1565  N N   . ALA A 233  ? 0.2580 0.2191 0.2809 -0.0005 -0.0061 0.0269  231  ALA A N   
1566  C CA  . ALA A 233  ? 0.2873 0.2528 0.3090 -0.0029 -0.0063 0.0301  231  ALA A CA  
1567  C C   . ALA A 233  ? 0.2856 0.2544 0.3028 -0.0030 -0.0040 0.0283  231  ALA A C   
1568  O O   . ALA A 233  ? 0.2783 0.2509 0.2947 -0.0040 -0.0037 0.0296  231  ALA A O   
1569  C CB  . ALA A 233  ? 0.3182 0.2848 0.3410 -0.0050 -0.0076 0.0326  231  ALA A CB  
1570  N N   . ASP A 234  ? 0.2565 0.2242 0.2711 -0.0021 -0.0025 0.0253  232  ASP A N   
1571  C CA  . ASP A 234  ? 0.2787 0.2488 0.2899 -0.0019 -0.0005 0.0235  232  ASP A CA  
1572  C C   . ASP A 234  ? 0.2471 0.2173 0.2587 -0.0008 0.0003  0.0228  232  ASP A C   
1573  O O   . ASP A 234  ? 0.2500 0.2235 0.2604 -0.0015 0.0010  0.0228  232  ASP A O   
1574  C CB  . ASP A 234  ? 0.3349 0.3029 0.3441 -0.0006 0.0009  0.0206  232  ASP A CB  
1575  C CG  . ASP A 234  ? 0.4373 0.4060 0.4455 -0.0018 0.0006  0.0206  232  ASP A CG  
1576  O OD1 . ASP A 234  ? 0.3862 0.3580 0.3945 -0.0038 -0.0002 0.0228  232  ASP A OD1 
1577  O OD2 . ASP A 234  ? 0.4041 0.3706 0.4112 -0.0006 0.0012  0.0186  232  ASP A OD2 
1578  N N   . ALA A 235  ? 0.2412 0.2082 0.2545 0.0011  0.0002  0.0218  233  ALA A N   
1579  C CA  . ALA A 235  ? 0.2169 0.1842 0.2307 0.0023  0.0010  0.0212  233  ALA A CA  
1580  C C   . ALA A 235  ? 0.2601 0.2298 0.2756 0.0011  -0.0001 0.0237  233  ALA A C   
1581  O O   . ALA A 235  ? 0.2335 0.2054 0.2484 0.0010  0.0007  0.0234  233  ALA A O   
1582  C CB  . ALA A 235  ? 0.2263 0.1904 0.2417 0.0046  0.0010  0.0197  233  ALA A CB  
1583  N N   . GLU A 236  ? 0.2439 0.2135 0.2616 0.0001  -0.0020 0.0262  234  GLU A N   
1584  C CA  . GLU A 236  ? 0.2415 0.2141 0.2608 -0.0011 -0.0032 0.0291  234  GLU A CA  
1585  C C   . GLU A 236  ? 0.2261 0.2038 0.2427 -0.0031 -0.0027 0.0297  234  GLU A C   
1586  O O   . GLU A 236  ? 0.2399 0.2209 0.2566 -0.0035 -0.0027 0.0304  234  GLU A O   
1587  C CB  . GLU A 236  ? 0.2861 0.2574 0.3091 -0.0019 -0.0056 0.0322  234  GLU A CB  
1588  C CG  . GLU A 236  ? 0.3922 0.3591 0.4190 0.0002  -0.0066 0.0314  234  GLU A CG  
1589  C CD  . GLU A 236  ? 0.4744 0.4382 0.5047 -0.0001 -0.0088 0.0328  234  GLU A CD  
1590  O OE1 . GLU A 236  ? 0.5579 0.5235 0.5883 -0.0023 -0.0098 0.0356  234  GLU A OE1 
1591  O OE2 . GLU A 236  ? 0.5341 0.4940 0.5674 0.0019  -0.0095 0.0310  234  GLU A OE2 
1592  N N   . ARG A 237  ? 0.2355 0.2144 0.2500 -0.0041 -0.0023 0.0292  235  ARG A N   
1593  C CA  . ARG A 237  ? 0.2349 0.2193 0.2470 -0.0056 -0.0017 0.0291  235  ARG A CA  
1594  C C   . ARG A 237  ? 0.2426 0.2278 0.2532 -0.0047 -0.0001 0.0261  235  ARG A C   
1595  O O   . ARG A 237  ? 0.2510 0.2406 0.2611 -0.0055 -0.0001 0.0260  235  ARG A O   
1596  C CB  . ARG A 237  ? 0.2764 0.2620 0.2868 -0.0067 -0.0015 0.0289  235  ARG A CB  
1597  C CG  . ARG A 237  ? 0.3702 0.3618 0.3781 -0.0079 -0.0007 0.0279  235  ARG A CG  
1598  C CD  . ARG A 237  ? 0.4277 0.4213 0.4344 -0.0092 -0.0008 0.0284  235  ARG A CD  
1599  N NE  . ARG A 237  ? 0.4690 0.4575 0.4753 -0.0079 -0.0001 0.0264  235  ARG A NE  
1600  C CZ  . ARG A 237  ? 0.5290 0.5169 0.5334 -0.0070 0.0014  0.0231  235  ARG A CZ  
1601  N NH1 . ARG A 237  ? 0.5468 0.5387 0.5499 -0.0072 0.0022  0.0211  235  ARG A NH1 
1602  N NH2 . ARG A 237  ? 0.4948 0.4782 0.4989 -0.0059 0.0019  0.0217  235  ARG A NH2 
1603  N N   . TYR A 238  ? 0.2239 0.2051 0.2341 -0.0031 0.0012  0.0236  236  TYR A N   
1604  C CA  . TYR A 238  ? 0.2195 0.2012 0.2290 -0.0024 0.0026  0.0211  236  TYR A CA  
1605  C C   . TYR A 238  ? 0.2169 0.1992 0.2283 -0.0019 0.0023  0.0218  236  TYR A C   
1606  O O   . TYR A 238  ? 0.2407 0.2258 0.2522 -0.0023 0.0027  0.0207  236  TYR A O   
1607  C CB  . TYR A 238  ? 0.2242 0.2020 0.2332 -0.0007 0.0039  0.0190  236  TYR A CB  
1608  C CG  . TYR A 238  ? 0.2075 0.1850 0.2145 -0.0011 0.0044  0.0179  236  TYR A CG  
1609  C CD1 . TYR A 238  ? 0.2696 0.2511 0.2755 -0.0024 0.0043  0.0174  236  TYR A CD1 
1610  C CD2 . TYR A 238  ? 0.2297 0.2037 0.2363 0.0001  0.0048  0.0172  236  TYR A CD2 
1611  C CE1 . TYR A 238  ? 0.3095 0.2910 0.3138 -0.0026 0.0047  0.0163  236  TYR A CE1 
1612  C CE2 . TYR A 238  ? 0.2620 0.2359 0.2670 -0.0001 0.0052  0.0162  236  TYR A CE2 
1613  C CZ  . TYR A 238  ? 0.2858 0.2633 0.2898 -0.0015 0.0051  0.0158  236  TYR A CZ  
1614  O OH  . TYR A 238  ? 0.3369 0.3144 0.3395 -0.0017 0.0055  0.0148  236  TYR A OH  
1615  N N   . TYR A 239  ? 0.2000 0.1800 0.2134 -0.0012 0.0014  0.0235  237  TYR A N   
1616  C CA  . TYR A 239  ? 0.2009 0.1817 0.2164 -0.0008 0.0010  0.0244  237  TYR A CA  
1617  C C   . TYR A 239  ? 0.2262 0.2122 0.2417 -0.0025 0.0000  0.0259  237  TYR A C   
1618  O O   . TYR A 239  ? 0.2127 0.2012 0.2286 -0.0026 0.0003  0.0251  237  TYR A O   
1619  C CB  . TYR A 239  ? 0.2109 0.1887 0.2290 0.0004  -0.0001 0.0258  237  TYR A CB  
1620  C CG  . TYR A 239  ? 0.2447 0.2236 0.2651 0.0008  -0.0006 0.0268  237  TYR A CG  
1621  C CD1 . TYR A 239  ? 0.2440 0.2261 0.2657 -0.0005 -0.0022 0.0294  237  TYR A CD1 
1622  C CD2 . TYR A 239  ? 0.2490 0.2267 0.2704 0.0025  0.0006  0.0251  237  TYR A CD2 
1623  C CE1 . TYR A 239  ? 0.2678 0.2513 0.2916 -0.0001 -0.0027 0.0303  237  TYR A CE1 
1624  C CE2 . TYR A 239  ? 0.2498 0.2289 0.2734 0.0029  0.0002  0.0260  237  TYR A CE2 
1625  C CZ  . TYR A 239  ? 0.2674 0.2492 0.2923 0.0016  -0.0015 0.0284  237  TYR A CZ  
1626  O OH  . TYR A 239  ? 0.3039 0.2874 0.3312 0.0020  -0.0021 0.0293  237  TYR A OH  
1627  N N   . ARG A 240  ? 0.2177 0.2058 0.2329 -0.0039 -0.0013 0.0283  238  ARG A N   
1628  C CA  . ARG A 240  ? 0.2155 0.2096 0.2307 -0.0056 -0.0024 0.0302  238  ARG A CA  
1629  C C   . ARG A 240  ? 0.1972 0.1957 0.2100 -0.0063 -0.0014 0.0275  238  ARG A C   
1630  O O   . ARG A 240  ? 0.2170 0.2205 0.2299 -0.0071 -0.0019 0.0275  238  ARG A O   
1631  C CB  . ARG A 240  ? 0.2586 0.2546 0.2745 -0.0070 -0.0041 0.0341  238  ARG A CB  
1632  C CG  . ARG A 240  ? 0.2869 0.2833 0.3009 -0.0080 -0.0038 0.0340  238  ARG A CG  
1633  C CD  . ARG A 240  ? 0.2619 0.2610 0.2774 -0.0097 -0.0057 0.0385  238  ARG A CD  
1634  N NE  . ARG A 240  ? 0.2970 0.2961 0.3112 -0.0106 -0.0055 0.0387  238  ARG A NE  
1635  C CZ  . ARG A 240  ? 0.2973 0.2910 0.3131 -0.0101 -0.0060 0.0392  238  ARG A CZ  
1636  N NH1 . ARG A 240  ? 0.2836 0.2718 0.3026 -0.0087 -0.0069 0.0397  238  ARG A NH1 
1637  N NH2 . ARG A 240  ? 0.3583 0.3525 0.3728 -0.0109 -0.0057 0.0390  238  ARG A NH2 
1638  N N   . ASP A 241  ? 0.2071 0.2041 0.2182 -0.0061 -0.0002 0.0250  239  ASP A N   
1639  C CA  . ASP A 241  ? 0.2121 0.2127 0.2219 -0.0064 0.0007  0.0219  239  ASP A CA  
1640  C C   . ASP A 241  ? 0.2286 0.2283 0.2398 -0.0055 0.0013  0.0198  239  ASP A C   
1641  O O   . ASP A 241  ? 0.2225 0.2267 0.2340 -0.0061 0.0011  0.0181  239  ASP A O   
1642  C CB  . ASP A 241  ? 0.2661 0.2646 0.2743 -0.0061 0.0018  0.0197  239  ASP A CB  
1643  C CG  . ASP A 241  ? 0.3524 0.3537 0.3590 -0.0074 0.0012  0.0212  239  ASP A CG  
1644  O OD1 . ASP A 241  ? 0.4313 0.4369 0.4380 -0.0087 0.0000  0.0241  239  ASP A OD1 
1645  O OD2 . ASP A 241  ? 0.4777 0.4773 0.4831 -0.0071 0.0020  0.0197  239  ASP A OD2 
1646  N N   . TYR A 242  ? 0.1976 0.1919 0.2102 -0.0040 0.0020  0.0197  240  TYR A N   
1647  C CA  . TYR A 242  ? 0.1960 0.1897 0.2105 -0.0033 0.0026  0.0182  240  TYR A CA  
1648  C C   . TYR A 242  ? 0.1850 0.1820 0.2010 -0.0038 0.0015  0.0196  240  TYR A C   
1649  O O   . TYR A 242  ? 0.1994 0.1992 0.2165 -0.0042 0.0014  0.0180  240  TYR A O   
1650  C CB  . TYR A 242  ? 0.1898 0.1782 0.2053 -0.0017 0.0036  0.0183  240  TYR A CB  
1651  C CG  . TYR A 242  ? 0.1844 0.1696 0.1989 -0.0009 0.0049  0.0167  240  TYR A CG  
1652  C CD1 . TYR A 242  ? 0.2060 0.1925 0.2201 -0.0014 0.0054  0.0143  240  TYR A CD1 
1653  C CD2 . TYR A 242  ? 0.2100 0.1912 0.2242 0.0004  0.0054  0.0173  240  TYR A CD2 
1654  C CE1 . TYR A 242  ? 0.2097 0.1933 0.2232 -0.0006 0.0064  0.0132  240  TYR A CE1 
1655  C CE2 . TYR A 242  ? 0.1944 0.1733 0.2076 0.0011  0.0065  0.0160  240  TYR A CE2 
1656  C CZ  . TYR A 242  ? 0.1968 0.1768 0.2097 0.0006  0.0070  0.0142  240  TYR A CZ  
1657  O OH  . TYR A 242  ? 0.2159 0.1935 0.2281 0.0014  0.0080  0.0134  240  TYR A OH  
1658  N N   . GLU A 243  ? 0.1727 0.1695 0.1891 -0.0039 0.0004  0.0227  241  GLU A N   
1659  C CA  . GLU A 243  ? 0.1798 0.1796 0.1979 -0.0043 -0.0008 0.0245  241  GLU A CA  
1660  C C   . GLU A 243  ? 0.1780 0.1848 0.1950 -0.0059 -0.0017 0.0242  241  GLU A C   
1661  O O   . GLU A 243  ? 0.1994 0.2095 0.2175 -0.0062 -0.0020 0.0232  241  GLU A O   
1662  C CB  . GLU A 243  ? 0.1960 0.1940 0.2153 -0.0041 -0.0021 0.0280  241  GLU A CB  
1663  C CG  . GLU A 243  ? 0.2488 0.2499 0.2702 -0.0045 -0.0036 0.0305  241  GLU A CG  
1664  C CD  . GLU A 243  ? 0.2952 0.2950 0.3181 -0.0046 -0.0052 0.0344  241  GLU A CD  
1665  O OE1 . GLU A 243  ? 0.3732 0.3723 0.3951 -0.0053 -0.0055 0.0355  241  GLU A OE1 
1666  O OE2 . GLU A 243  ? 0.2744 0.2739 0.3001 -0.0040 -0.0063 0.0363  241  GLU A OE2 
1667  N N   . SER A 244  ? 0.1910 0.2007 0.2058 -0.0070 -0.0019 0.0246  242  SER A N   
1668  C CA  . SER A 244  ? 0.1989 0.2163 0.2124 -0.0085 -0.0027 0.0240  242  SER A CA  
1669  C C   . SER A 244  ? 0.2075 0.2266 0.2211 -0.0082 -0.0018 0.0193  242  SER A C   
1670  O O   . SER A 244  ? 0.2357 0.2607 0.2498 -0.0088 -0.0025 0.0179  242  SER A O   
1671  C CB  . SER A 244  ? 0.2248 0.2453 0.2360 -0.0096 -0.0030 0.0255  242  SER A CB  
1672  O OG  . SER A 244  ? 0.2807 0.2982 0.2906 -0.0092 -0.0017 0.0228  242  SER A OG  
1673  N N   . ALA A 245  ? 0.1996 0.2138 0.2134 -0.0073 -0.0005 0.0167  243  ALA A N   
1674  C CA  . ALA A 245  ? 0.1861 0.2012 0.2011 -0.0070 0.0001  0.0125  243  ALA A CA  
1675  C C   . ALA A 245  ? 0.2092 0.2236 0.2271 -0.0066 -0.0001 0.0120  243  ALA A C   
1676  O O   . ALA A 245  ? 0.2006 0.2191 0.2200 -0.0070 -0.0006 0.0091  243  ALA A O   
1677  C CB  . ALA A 245  ? 0.2247 0.2346 0.2396 -0.0061 0.0014  0.0105  243  ALA A CB  
1678  N N   . ILE A 246  ? 0.1896 0.1994 0.2088 -0.0057 0.0002  0.0144  244  ILE A N   
1679  C CA  . ILE A 246  ? 0.1965 0.2062 0.2186 -0.0054 0.0000  0.0142  244  ILE A CA  
1680  C C   . ILE A 246  ? 0.2281 0.2444 0.2506 -0.0064 -0.0015 0.0145  244  ILE A C   
1681  O O   . ILE A 246  ? 0.1989 0.2178 0.2236 -0.0066 -0.0019 0.0122  244  ILE A O   
1682  C CB  . ILE A 246  ? 0.1936 0.1983 0.2169 -0.0042 0.0005  0.0168  244  ILE A CB  
1683  C CG1 . ILE A 246  ? 0.1918 0.1910 0.2152 -0.0031 0.0021  0.0159  244  ILE A CG1 
1684  C CG2 . ILE A 246  ? 0.2093 0.2151 0.2357 -0.0040 0.0001  0.0170  244  ILE A CG2 
1685  C CD1 . ILE A 246  ? 0.2076 0.2025 0.2313 -0.0018 0.0026  0.0182  244  ILE A CD1 
1686  N N   . HIS A 247  ? 0.2054 0.2250 0.2259 -0.0071 -0.0025 0.0173  245  HIS A N   
1687  C CA  . HIS A 247  ? 0.2036 0.2304 0.2242 -0.0081 -0.0041 0.0180  245  HIS A CA  
1688  C C   . HIS A 247  ? 0.1944 0.2272 0.2144 -0.0089 -0.0043 0.0138  245  HIS A C   
1689  O O   . HIS A 247  ? 0.1972 0.2345 0.2189 -0.0092 -0.0052 0.0120  245  HIS A O   
1690  C CB  . HIS A 247  ? 0.2158 0.2456 0.2346 -0.0090 -0.0052 0.0223  245  HIS A CB  
1691  C CG  . HIS A 247  ? 0.2298 0.2550 0.2502 -0.0083 -0.0056 0.0262  245  HIS A CG  
1692  N ND1 . HIS A 247  ? 0.2251 0.2506 0.2480 -0.0078 -0.0063 0.0274  245  HIS A ND1 
1693  C CD2 . HIS A 247  ? 0.2543 0.2749 0.2746 -0.0078 -0.0056 0.0291  245  HIS A CD2 
1694  C CE1 . HIS A 247  ? 0.2597 0.2809 0.2841 -0.0070 -0.0067 0.0306  245  HIS A CE1 
1695  N NE2 . HIS A 247  ? 0.2512 0.2692 0.2741 -0.0070 -0.0063 0.0316  245  HIS A NE2 
1696  N N   . ALA A 248  ? 0.1950 0.2284 0.2130 -0.0091 -0.0037 0.0120  246  ALA A N   
1697  C CA  . ALA A 248  ? 0.1937 0.2334 0.2114 -0.0096 -0.0041 0.0076  246  ALA A CA  
1698  C C   . ALA A 248  ? 0.2025 0.2397 0.2238 -0.0089 -0.0038 0.0033  246  ALA A C   
1699  O O   . ALA A 248  ? 0.2081 0.2508 0.2309 -0.0093 -0.0048 0.0000  246  ALA A O   
1700  C CB  . ALA A 248  ? 0.2097 0.2504 0.2249 -0.0098 -0.0034 0.0066  246  ALA A CB  
1701  N N   . ILE A 249  ? 0.2103 0.2396 0.2332 -0.0080 -0.0026 0.0034  247  ILE A N   
1702  C CA  . ILE A 249  ? 0.1961 0.2225 0.2230 -0.0075 -0.0023 0.0002  247  ILE A CA  
1703  C C   . ILE A 249  ? 0.1910 0.2187 0.2208 -0.0077 -0.0031 0.0007  247  ILE A C   
1704  O O   . ILE A 249  ? 0.2053 0.2353 0.2385 -0.0079 -0.0038 -0.0027 247  ILE A O   
1705  C CB  . ILE A 249  ? 0.2014 0.2196 0.2291 -0.0066 -0.0008 0.0012  247  ILE A CB  
1706  C CG1 . ILE A 249  ? 0.1867 0.2040 0.2121 -0.0064 -0.0001 0.0000  247  ILE A CG1 
1707  C CG2 . ILE A 249  ? 0.2004 0.2156 0.2329 -0.0062 -0.0006 -0.0010 247  ILE A CG2 
1708  C CD1 . ILE A 249  ? 0.2164 0.2265 0.2411 -0.0055 0.0013  0.0023  247  ILE A CD1 
1709  N N   . GLY A 250  ? 0.1834 0.2097 0.2124 -0.0075 -0.0031 0.0049  248  GLY A N   
1710  C CA  . GLY A 250  ? 0.1976 0.2253 0.2293 -0.0076 -0.0039 0.0057  248  GLY A CA  
1711  C C   . GLY A 250  ? 0.2026 0.2387 0.2342 -0.0086 -0.0056 0.0041  248  GLY A C   
1712  O O   . GLY A 250  ? 0.2013 0.2396 0.2361 -0.0088 -0.0064 0.0021  248  GLY A O   
1713  N N   . LYS A 251  ? 0.2039 0.2453 0.2319 -0.0092 -0.0062 0.0051  249  LYS A N   
1714  C CA  . LYS A 251  ? 0.2310 0.2818 0.2584 -0.0101 -0.0078 0.0034  249  LYS A CA  
1715  C C   . LYS A 251  ? 0.2252 0.2790 0.2549 -0.0102 -0.0082 -0.0028 249  LYS A C   
1716  O O   . LYS A 251  ? 0.2380 0.2975 0.2697 -0.0106 -0.0095 -0.0054 249  LYS A O   
1717  C CB  . LYS A 251  ? 0.2287 0.2850 0.2517 -0.0109 -0.0082 0.0057  249  LYS A CB  
1718  C CG  . LYS A 251  ? 0.2442 0.2999 0.2658 -0.0111 -0.0086 0.0119  249  LYS A CG  
1719  C CD  . LYS A 251  ? 0.2515 0.3116 0.2693 -0.0119 -0.0087 0.0140  249  LYS A CD  
1720  C CE  . LYS A 251  ? 0.2433 0.3020 0.2604 -0.0123 -0.0093 0.0204  249  LYS A CE  
1721  N NZ  . LYS A 251  ? 0.2470 0.3105 0.2609 -0.0133 -0.0094 0.0225  249  LYS A NZ  
1722  N N   . ALA A 252  ? 0.2249 0.2752 0.2546 -0.0097 -0.0072 -0.0054 250  ALA A N   
1723  C CA  . ALA A 252  ? 0.2367 0.2892 0.2692 -0.0096 -0.0077 -0.0116 250  ALA A CA  
1724  C C   . ALA A 252  ? 0.2436 0.2912 0.2817 -0.0093 -0.0078 -0.0134 250  ALA A C   
1725  O O   . ALA A 252  ? 0.2400 0.2911 0.2817 -0.0095 -0.0090 -0.0182 250  ALA A O   
1726  C CB  . ALA A 252  ? 0.2414 0.2913 0.2726 -0.0092 -0.0066 -0.0133 250  ALA A CB  
1727  N N   . SER A 253  ? 0.2348 0.2746 0.2740 -0.0089 -0.0066 -0.0098 251  SER A N   
1728  C CA  . SER A 253  ? 0.2066 0.2422 0.2513 -0.0087 -0.0066 -0.0108 251  SER A CA  
1729  C C   . SER A 253  ? 0.2365 0.2775 0.2837 -0.0093 -0.0082 -0.0119 251  SER A C   
1730  O O   . SER A 253  ? 0.2427 0.2842 0.2950 -0.0096 -0.0091 -0.0155 251  SER A O   
1731  C CB  . SER A 253  ? 0.2164 0.2446 0.2611 -0.0081 -0.0050 -0.0061 251  SER A CB  
1732  O OG  . SER A 253  ? 0.2321 0.2573 0.2822 -0.0081 -0.0050 -0.0065 251  SER A OG  
1733  N N   . ALA A 254  ? 0.2172 0.2622 0.2611 -0.0096 -0.0086 -0.0087 252  ALA A N   
1734  C CA  . ALA A 254  ? 0.2468 0.2983 0.2922 -0.0102 -0.0103 -0.0095 252  ALA A CA  
1735  C C   . ALA A 254  ? 0.2557 0.3040 0.3070 -0.0102 -0.0105 -0.0101 252  ALA A C   
1736  O O   . ALA A 254  ? 0.2505 0.3030 0.3056 -0.0107 -0.0120 -0.0140 252  ALA A O   
1737  C CB  . ALA A 254  ? 0.2673 0.3277 0.3121 -0.0107 -0.0119 -0.0144 252  ALA A CB  
1738  N N   . GLY A 255  ? 0.2654 0.3066 0.3177 -0.0097 -0.0091 -0.0064 253  GLY A N   
1739  C CA  . GLY A 255  ? 0.2485 0.2872 0.3061 -0.0098 -0.0091 -0.0061 253  GLY A CA  
1740  C C   . GLY A 255  ? 0.2226 0.2575 0.2856 -0.0100 -0.0090 -0.0092 253  GLY A C   
1741  O O   . GLY A 255  ? 0.2766 0.3103 0.3449 -0.0103 -0.0092 -0.0092 253  GLY A O   
1742  N N   . ARG A 256  ? 0.2364 0.2696 0.2989 -0.0098 -0.0086 -0.0118 254  ARG A N   
1743  C CA  . ARG A 256  ? 0.2331 0.2621 0.3014 -0.0099 -0.0086 -0.0143 254  ARG A CA  
1744  C C   . ARG A 256  ? 0.2411 0.2632 0.3113 -0.0096 -0.0069 -0.0101 254  ARG A C   
1745  O O   . ARG A 256  ? 0.2557 0.2748 0.3319 -0.0099 -0.0070 -0.0110 254  ARG A O   
1746  C CB  . ARG A 256  ? 0.2222 0.2510 0.2894 -0.0096 -0.0087 -0.0179 254  ARG A CB  
1747  C CG  . ARG A 256  ? 0.2678 0.3034 0.3366 -0.0100 -0.0108 -0.0239 254  ARG A CG  
1748  C CD  . ARG A 256  ? 0.2975 0.3333 0.3652 -0.0095 -0.0108 -0.0275 254  ARG A CD  
1749  N NE  . ARG A 256  ? 0.2415 0.2796 0.3016 -0.0092 -0.0098 -0.0253 254  ARG A NE  
1750  C CZ  . ARG A 256  ? 0.2675 0.3059 0.3252 -0.0087 -0.0094 -0.0273 254  ARG A CZ  
1751  N NH1 . ARG A 256  ? 0.3063 0.3421 0.3684 -0.0083 -0.0098 -0.0313 254  ARG A NH1 
1752  N NH2 . ARG A 256  ? 0.2790 0.3205 0.3300 -0.0086 -0.0087 -0.0252 254  ARG A NH2 
1753  N N   . GLY A 257  ? 0.2336 0.2535 0.2991 -0.0089 -0.0053 -0.0056 255  GLY A N   
1754  C CA  . GLY A 257  ? 0.2199 0.2346 0.2869 -0.0084 -0.0036 -0.0018 255  GLY A CA  
1755  C C   . GLY A 257  ? 0.1947 0.2045 0.2606 -0.0078 -0.0023 -0.0013 255  GLY A C   
1756  O O   . GLY A 257  ? 0.2109 0.2209 0.2749 -0.0077 -0.0026 -0.0039 255  GLY A O   
1757  N N   . ILE A 258  ? 0.1835 0.1893 0.2507 -0.0073 -0.0007 0.0021  256  ILE A N   
1758  C CA  . ILE A 258  ? 0.2055 0.2071 0.2704 -0.0065 0.0008  0.0035  256  ILE A CA  
1759  C C   . ILE A 258  ? 0.2242 0.2234 0.2937 -0.0070 0.0004  0.0014  256  ILE A C   
1760  O O   . ILE A 258  ? 0.2094 0.2058 0.2768 -0.0064 0.0012  0.0016  256  ILE A O   
1761  C CB  . ILE A 258  ? 0.2146 0.2138 0.2785 -0.0057 0.0026  0.0079  256  ILE A CB  
1762  C CG1 . ILE A 258  ? 0.2294 0.2284 0.2998 -0.0062 0.0028  0.0094  256  ILE A CG1 
1763  C CG2 . ILE A 258  ? 0.1998 0.2008 0.2592 -0.0050 0.0028  0.0096  256  ILE A CG2 
1764  C CD1 . ILE A 258  ? 0.2294 0.2272 0.2989 -0.0053 0.0047  0.0136  256  ILE A CD1 
1765  N N   . TYR A 259  ? 0.2336 0.2337 0.3098 -0.0080 -0.0009 -0.0005 257  TYR A N   
1766  C CA  . TYR A 259  ? 0.2353 0.2328 0.3171 -0.0084 -0.0016 -0.0023 257  TYR A CA  
1767  C C   . TYR A 259  ? 0.2385 0.2383 0.3213 -0.0086 -0.0034 -0.0080 257  TYR A C   
1768  O O   . TYR A 259  ? 0.2814 0.2791 0.3639 -0.0082 -0.0035 -0.0096 257  TYR A O   
1769  C CB  . TYR A 259  ? 0.2537 0.2504 0.3436 -0.0094 -0.0020 -0.0009 257  TYR A CB  
1770  C CG  . TYR A 259  ? 0.2367 0.2325 0.3257 -0.0091 -0.0001 0.0046  257  TYR A CG  
1771  C CD1 . TYR A 259  ? 0.2515 0.2443 0.3377 -0.0082 0.0018  0.0080  257  TYR A CD1 
1772  C CD2 . TYR A 259  ? 0.2264 0.2249 0.3173 -0.0095 -0.0002 0.0060  257  TYR A CD2 
1773  C CE1 . TYR A 259  ? 0.2466 0.2396 0.3318 -0.0077 0.0036  0.0126  257  TYR A CE1 
1774  C CE2 . TYR A 259  ? 0.2750 0.2733 0.3651 -0.0091 0.0016  0.0106  257  TYR A CE2 
1775  C CZ  . TYR A 259  ? 0.2335 0.2292 0.3207 -0.0081 0.0035  0.0138  257  TYR A CZ  
1776  O OH  . TYR A 259  ? 0.2465 0.2430 0.3329 -0.0075 0.0052  0.0179  257  TYR A OH  
1777  N N   . GLU A 260  ? 0.2302 0.2346 0.3139 -0.0092 -0.0051 -0.0111 258  GLU A N   
1778  C CA  . GLU A 260  ? 0.2908 0.2987 0.3751 -0.0093 -0.0068 -0.0170 258  GLU A CA  
1779  C C   . GLU A 260  ? 0.2758 0.2862 0.3519 -0.0085 -0.0062 -0.0175 258  GLU A C   
1780  O O   . GLU A 260  ? 0.3404 0.3522 0.4159 -0.0082 -0.0068 -0.0213 258  GLU A O   
1781  C CB  . GLU A 260  ? 0.3088 0.3219 0.3965 -0.0101 -0.0089 -0.0204 258  GLU A CB  
1782  C CG  . GLU A 260  ? 0.4087 0.4261 0.4981 -0.0100 -0.0109 -0.0272 258  GLU A CG  
1783  C CD  . GLU A 260  ? 0.4484 0.4728 0.5385 -0.0106 -0.0128 -0.0308 258  GLU A CD  
1784  O OE1 . GLU A 260  ? 0.5113 0.5363 0.6042 -0.0113 -0.0131 -0.0288 258  GLU A OE1 
1785  O OE2 . GLU A 260  ? 0.4543 0.4843 0.5424 -0.0103 -0.0139 -0.0356 258  GLU A OE2 
1786  N N   . GLY A 261  ? 0.2246 0.2358 0.2947 -0.0083 -0.0050 -0.0136 259  GLY A N   
1787  C CA  . GLY A 261  ? 0.1993 0.2137 0.2624 -0.0079 -0.0047 -0.0137 259  GLY A CA  
1788  C C   . GLY A 261  ? 0.2138 0.2238 0.2727 -0.0071 -0.0030 -0.0111 259  GLY A C   
1789  O O   . GLY A 261  ? 0.2081 0.2129 0.2687 -0.0067 -0.0018 -0.0086 259  GLY A O   
1790  N N   . PRO A 262  ? 0.1893 0.2021 0.2427 -0.0069 -0.0029 -0.0116 260  PRO A N   
1791  C CA  . PRO A 262  ? 0.1923 0.2016 0.2417 -0.0062 -0.0014 -0.0098 260  PRO A CA  
1792  C C   . PRO A 262  ? 0.2049 0.2107 0.2511 -0.0057 0.0000  -0.0046 260  PRO A C   
1793  O O   . PRO A 262  ? 0.2237 0.2309 0.2696 -0.0059 -0.0001 -0.0024 260  PRO A O   
1794  C CB  . PRO A 262  ? 0.2150 0.2297 0.2599 -0.0063 -0.0020 -0.0118 260  PRO A CB  
1795  C CG  . PRO A 262  ? 0.2203 0.2410 0.2648 -0.0070 -0.0033 -0.0122 260  PRO A CG  
1796  C CD  . PRO A 262  ? 0.2242 0.2442 0.2750 -0.0073 -0.0042 -0.0142 260  PRO A CD  
1797  N N   . GLY A 263  ? 0.1880 0.1897 0.2322 -0.0050 0.0013  -0.0029 261  GLY A N   
1798  C CA  . GLY A 263  ? 0.1895 0.1882 0.2305 -0.0043 0.0026  0.0013  261  GLY A CA  
1799  C C   . GLY A 263  ? 0.1713 0.1687 0.2077 -0.0038 0.0033  0.0019  261  GLY A C   
1800  O O   . GLY A 263  ? 0.1801 0.1796 0.2152 -0.0041 0.0028  -0.0007 261  GLY A O   
1801  N N   . ILE A 264  ? 0.1741 0.1683 0.2081 -0.0031 0.0044  0.0051  262  ILE A N   
1802  C CA  . ILE A 264  ? 0.1858 0.1784 0.2157 -0.0026 0.0050  0.0060  262  ILE A CA  
1803  C C   . ILE A 264  ? 0.1848 0.1728 0.2151 -0.0016 0.0064  0.0076  262  ILE A C   
1804  O O   . ILE A 264  ? 0.2004 0.1869 0.2331 -0.0011 0.0070  0.0091  262  ILE A O   
1805  C CB  . ILE A 264  ? 0.1923 0.1865 0.2188 -0.0027 0.0046  0.0082  262  ILE A CB  
1806  C CG1 . ILE A 264  ? 0.2155 0.2090 0.2382 -0.0026 0.0048  0.0085  262  ILE A CG1 
1807  C CG2 . ILE A 264  ? 0.2129 0.2047 0.2399 -0.0018 0.0052  0.0111  262  ILE A CG2 
1808  C CD1 . ILE A 264  ? 0.2304 0.2258 0.2506 -0.0030 0.0040  0.0108  262  ILE A CD1 
1809  N N   . SER A 265  ? 0.1733 0.1595 0.2011 -0.0012 0.0069  0.0074  263  SER A N   
1810  C CA  . SER A 265  ? 0.1997 0.1822 0.2270 -0.0001 0.0082  0.0090  263  SER A CA  
1811  C C   . SER A 265  ? 0.2109 0.1925 0.2339 0.0004  0.0084  0.0103  263  SER A C   
1812  O O   . SER A 265  ? 0.2429 0.2261 0.2636 -0.0002 0.0077  0.0093  263  SER A O   
1813  C CB  . SER A 265  ? 0.2246 0.2057 0.2535 0.0000  0.0084  0.0076  263  SER A CB  
1814  O OG  . SER A 265  ? 0.2396 0.2206 0.2734 -0.0004 0.0082  0.0068  263  SER A OG  
1815  N N   . ILE A 266  ? 0.2026 0.1820 0.2248 0.0015  0.0093  0.0123  264  ILE A N   
1816  C CA  . ILE A 266  ? 0.2169 0.1951 0.2359 0.0021  0.0093  0.0132  264  ILE A CA  
1817  C C   . ILE A 266  ? 0.2156 0.1913 0.2337 0.0033  0.0104  0.0137  264  ILE A C   
1818  O O   . ILE A 266  ? 0.2132 0.1884 0.2333 0.0038  0.0113  0.0142  264  ILE A O   
1819  C CB  . ILE A 266  ? 0.2027 0.1812 0.2216 0.0025  0.0089  0.0148  264  ILE A CB  
1820  C CG1 . ILE A 266  ? 0.2281 0.2059 0.2490 0.0037  0.0098  0.0159  264  ILE A CG1 
1821  C CG2 . ILE A 266  ? 0.2263 0.2078 0.2461 0.0013  0.0076  0.0147  264  ILE A CG2 
1822  C CD1 . ILE A 266  ? 0.2477 0.2255 0.2686 0.0046  0.0094  0.0171  264  ILE A CD1 
1823  N N   . LYS A 267  ? 0.2021 0.1765 0.2174 0.0037  0.0103  0.0138  265  LYS A N   
1824  C CA  . LYS A 267  ? 0.1898 0.1623 0.2039 0.0050  0.0113  0.0141  265  LYS A CA  
1825  C C   . LYS A 267  ? 0.2068 0.1786 0.2199 0.0061  0.0110  0.0149  265  LYS A C   
1826  O O   . LYS A 267  ? 0.2106 0.1823 0.2227 0.0056  0.0100  0.0149  265  LYS A O   
1827  C CB  . LYS A 267  ? 0.2061 0.1778 0.2183 0.0048  0.0112  0.0131  265  LYS A CB  
1828  C CG  . LYS A 267  ? 0.2255 0.1975 0.2394 0.0043  0.0115  0.0122  265  LYS A CG  
1829  C CD  . LYS A 267  ? 0.2683 0.2398 0.2805 0.0042  0.0114  0.0111  265  LYS A CD  
1830  C CE  . LYS A 267  ? 0.3030 0.2747 0.3178 0.0039  0.0115  0.0100  265  LYS A CE  
1831  N NZ  . LYS A 267  ? 0.3801 0.3536 0.3973 0.0028  0.0107  0.0087  265  LYS A NZ  
1832  N N   . LEU A 268  ? 0.1861 0.1578 0.1997 0.0075  0.0120  0.0154  266  LEU A N   
1833  C CA  . LEU A 268  ? 0.1964 0.1676 0.2095 0.0088  0.0117  0.0155  266  LEU A CA  
1834  C C   . LEU A 268  ? 0.2023 0.1718 0.2133 0.0090  0.0110  0.0147  266  LEU A C   
1835  O O   . LEU A 268  ? 0.2027 0.1714 0.2140 0.0094  0.0099  0.0146  266  LEU A O   
1836  C CB  . LEU A 268  ? 0.2209 0.1933 0.2348 0.0105  0.0129  0.0158  266  LEU A CB  
1837  C CG  . LEU A 268  ? 0.2136 0.1880 0.2303 0.0102  0.0135  0.0169  266  LEU A CG  
1838  C CD1 . LEU A 268  ? 0.2210 0.1974 0.2383 0.0119  0.0148  0.0175  266  LEU A CD1 
1839  C CD2 . LEU A 268  ? 0.2454 0.2200 0.2635 0.0097  0.0123  0.0171  266  LEU A CD2 
1840  N N   . SER A 269  ? 0.2082 0.1771 0.2176 0.0088  0.0115  0.0141  267  SER A N   
1841  C CA  . SER A 269  ? 0.2131 0.1806 0.2207 0.0090  0.0108  0.0133  267  SER A CA  
1842  C C   . SER A 269  ? 0.2414 0.2086 0.2489 0.0074  0.0094  0.0136  267  SER A C   
1843  O O   . SER A 269  ? 0.2236 0.1895 0.2303 0.0074  0.0085  0.0134  267  SER A O   
1844  C CB  . SER A 269  ? 0.2377 0.2051 0.2437 0.0090  0.0115  0.0128  267  SER A CB  
1845  O OG  . SER A 269  ? 0.2236 0.1915 0.2299 0.0075  0.0114  0.0127  267  SER A OG  
1846  N N   . ALA A 270  ? 0.2048 0.1734 0.2131 0.0060  0.0091  0.0142  268  ALA A N   
1847  C CA  . ALA A 270  ? 0.2121 0.1816 0.2203 0.0045  0.0077  0.0149  268  ALA A CA  
1848  C C   . ALA A 270  ? 0.2143 0.1833 0.2241 0.0048  0.0065  0.0161  268  ALA A C   
1849  O O   . ALA A 270  ? 0.2265 0.1957 0.2365 0.0037  0.0052  0.0173  268  ALA A O   
1850  C CB  . ALA A 270  ? 0.2250 0.1972 0.2337 0.0031  0.0077  0.0149  268  ALA A CB  
1851  N N   . LEU A 271  ? 0.2011 0.1695 0.2123 0.0062  0.0069  0.0161  269  LEU A N   
1852  C CA  . LEU A 271  ? 0.2179 0.1861 0.2314 0.0065  0.0058  0.0172  269  LEU A CA  
1853  C C   . LEU A 271  ? 0.2111 0.1770 0.2256 0.0081  0.0051  0.0166  269  LEU A C   
1854  O O   . LEU A 271  ? 0.2293 0.1946 0.2463 0.0085  0.0038  0.0173  269  LEU A O   
1855  C CB  . LEU A 271  ? 0.2123 0.1821 0.2274 0.0070  0.0064  0.0175  269  LEU A CB  
1856  C CG  . LEU A 271  ? 0.2343 0.2065 0.2493 0.0053  0.0065  0.0180  269  LEU A CG  
1857  C CD1 . LEU A 271  ? 0.2749 0.2485 0.2918 0.0058  0.0072  0.0181  269  LEU A CD1 
1858  C CD2 . LEU A 271  ? 0.2583 0.2318 0.2736 0.0038  0.0048  0.0195  269  LEU A CD2 
1859  N N   . HIS A 272  ? 0.2130 0.1777 0.2259 0.0090  0.0057  0.0150  270  HIS A N   
1860  C CA  . HIS A 272  ? 0.2084 0.1712 0.2226 0.0105  0.0048  0.0139  270  HIS A CA  
1861  C C   . HIS A 272  ? 0.2195 0.1814 0.2315 0.0106  0.0051  0.0126  270  HIS A C   
1862  O O   . HIS A 272  ? 0.2293 0.1922 0.2390 0.0107  0.0066  0.0121  270  HIS A O   
1863  C CB  . HIS A 272  ? 0.2382 0.2017 0.2535 0.0128  0.0056  0.0125  270  HIS A CB  
1864  C CG  . HIS A 272  ? 0.2490 0.2109 0.2668 0.0145  0.0042  0.0111  270  HIS A CG  
1865  N ND1 . HIS A 272  ? 0.2531 0.2138 0.2702 0.0155  0.0038  0.0090  270  HIS A ND1 
1866  C CD2 . HIS A 272  ? 0.2779 0.2392 0.2992 0.0154  0.0028  0.0111  270  HIS A CD2 
1867  C CE1 . HIS A 272  ? 0.2544 0.2137 0.2748 0.0169  0.0022  0.0076  270  HIS A CE1 
1868  N NE2 . HIS A 272  ? 0.2900 0.2496 0.3131 0.0169  0.0016  0.0089  270  HIS A NE2 
1869  N N   . PRO A 273  ? 0.2281 0.1881 0.2411 0.0105  0.0036  0.0122  271  PRO A N   
1870  C CA  . PRO A 273  ? 0.2193 0.1785 0.2303 0.0106  0.0037  0.0109  271  PRO A CA  
1871  C C   . PRO A 273  ? 0.2184 0.1780 0.2285 0.0129  0.0047  0.0084  271  PRO A C   
1872  O O   . PRO A 273  ? 0.2375 0.1971 0.2456 0.0131  0.0051  0.0074  271  PRO A O   
1873  C CB  . PRO A 273  ? 0.2378 0.1950 0.2512 0.0097  0.0015  0.0115  271  PRO A CB  
1874  C CG  . PRO A 273  ? 0.2424 0.1986 0.2594 0.0105  0.0002  0.0119  271  PRO A CG  
1875  C CD  . PRO A 273  ? 0.2496 0.2079 0.2661 0.0102  0.0014  0.0132  271  PRO A CD  
1876  N N   . ARG A 274  ? 0.2133 0.1738 0.2247 0.0148  0.0051  0.0075  272  ARG A N   
1877  C CA  . ARG A 274  ? 0.2189 0.1810 0.2293 0.0171  0.0061  0.0051  272  ARG A CA  
1878  C C   . ARG A 274  ? 0.2292 0.1943 0.2390 0.0180  0.0080  0.0057  272  ARG A C   
1879  O O   . ARG A 274  ? 0.2504 0.2174 0.2613 0.0200  0.0083  0.0044  272  ARG A O   
1880  C CB  . ARG A 274  ? 0.2259 0.1871 0.2391 0.0190  0.0045  0.0026  272  ARG A CB  
1881  C CG  . ARG A 274  ? 0.2402 0.1983 0.2549 0.0181  0.0024  0.0020  272  ARG A CG  
1882  C CD  . ARG A 274  ? 0.2317 0.1902 0.2433 0.0177  0.0030  0.0012  272  ARG A CD  
1883  N NE  . ARG A 274  ? 0.2427 0.2040 0.2521 0.0199  0.0043  -0.0011 272  ARG A NE  
1884  C CZ  . ARG A 274  ? 0.2184 0.1804 0.2291 0.0221  0.0035  -0.0044 272  ARG A CZ  
1885  N NH1 . ARG A 274  ? 0.2476 0.2070 0.2622 0.0225  0.0012  -0.0060 272  ARG A NH1 
1886  N NH2 . ARG A 274  ? 0.2615 0.2273 0.2698 0.0240  0.0049  -0.0062 272  ARG A NH2 
1887  N N   . TYR A 275  ? 0.2152 0.1811 0.2234 0.0165  0.0092  0.0076  273  TYR A N   
1888  C CA  . TYR A 275  ? 0.2054 0.1739 0.2135 0.0169  0.0109  0.0087  273  TYR A CA  
1889  C C   . TYR A 275  ? 0.2268 0.1978 0.2329 0.0182  0.0123  0.0081  273  TYR A C   
1890  O O   . TYR A 275  ? 0.2215 0.1925 0.2260 0.0173  0.0129  0.0090  273  TYR A O   
1891  C CB  . TYR A 275  ? 0.2288 0.1970 0.2371 0.0147  0.0111  0.0108  273  TYR A CB  
1892  C CG  . TYR A 275  ? 0.1992 0.1698 0.2079 0.0149  0.0127  0.0120  273  TYR A CG  
1893  C CD1 . TYR A 275  ? 0.2115 0.1842 0.2219 0.0162  0.0133  0.0121  273  TYR A CD1 
1894  C CD2 . TYR A 275  ? 0.2114 0.1823 0.2195 0.0137  0.0135  0.0131  273  TYR A CD2 
1895  C CE1 . TYR A 275  ? 0.2440 0.2192 0.2553 0.0161  0.0147  0.0136  273  TYR A CE1 
1896  C CE2 . TYR A 275  ? 0.2138 0.1867 0.2232 0.0136  0.0147  0.0145  273  TYR A CE2 
1897  C CZ  . TYR A 275  ? 0.2114 0.1865 0.2223 0.0148  0.0154  0.0149  273  TYR A CZ  
1898  O OH  . TYR A 275  ? 0.2270 0.2046 0.2397 0.0146  0.0165  0.0167  273  TYR A OH  
1899  N N   . SER A 276  ? 0.1966 0.1701 0.2029 0.0204  0.0127  0.0065  274  SER A N   
1900  C CA  . SER A 276  ? 0.1840 0.1610 0.1884 0.0219  0.0140  0.0061  274  SER A CA  
1901  C C   . SER A 276  ? 0.2058 0.1870 0.2111 0.0242  0.0147  0.0049  274  SER A C   
1902  O O   . SER A 276  ? 0.2208 0.2013 0.2283 0.0250  0.0138  0.0034  274  SER A O   
1903  C CB  . SER A 276  ? 0.2485 0.2244 0.2511 0.0224  0.0131  0.0040  274  SER A CB  
1904  O OG  . SER A 276  ? 0.2820 0.2574 0.2861 0.0239  0.0117  0.0011  274  SER A OG  
1905  N N   . ARG A 277  ? 0.2137 0.1996 0.2175 0.0252  0.0163  0.0056  275  ARG A N   
1906  C CA  . ARG A 277  ? 0.2115 0.2028 0.2158 0.0276  0.0173  0.0044  275  ARG A CA  
1907  C C   . ARG A 277  ? 0.2105 0.2021 0.2152 0.0297  0.0159  0.0001  275  ARG A C   
1908  O O   . ARG A 277  ? 0.2093 0.2034 0.2159 0.0316  0.0158  -0.0019 275  ARG A O   
1909  C CB  . ARG A 277  ? 0.2126 0.2096 0.2150 0.0281  0.0192  0.0063  275  ARG A CB  
1910  C CG  . ARG A 277  ? 0.2070 0.2113 0.2094 0.0308  0.0202  0.0049  275  ARG A CG  
1911  C CD  . ARG A 277  ? 0.2032 0.2089 0.2085 0.0311  0.0206  0.0052  275  ARG A CD  
1912  N NE  . ARG A 277  ? 0.1956 0.2091 0.2010 0.0337  0.0218  0.0037  275  ARG A NE  
1913  C CZ  . ARG A 277  ? 0.1944 0.2096 0.2003 0.0362  0.0209  -0.0008 275  ARG A CZ  
1914  N NH1 . ARG A 277  ? 0.2223 0.2317 0.2292 0.0364  0.0187  -0.0039 275  ARG A NH1 
1915  N NH2 . ARG A 277  ? 0.2116 0.2349 0.2177 0.0387  0.0221  -0.0022 275  ARG A NH2 
1916  N N   . ALA A 278  ? 0.2106 0.1998 0.2139 0.0296  0.0148  -0.0017 276  ALA A N   
1917  C CA  . ALA A 278  ? 0.2068 0.1960 0.2111 0.0317  0.0132  -0.0061 276  ALA A CA  
1918  C C   . ALA A 278  ? 0.2329 0.2181 0.2410 0.0316  0.0114  -0.0074 276  ALA A C   
1919  O O   . ALA A 278  ? 0.2548 0.2410 0.2651 0.0338  0.0102  -0.0111 276  ALA A O   
1920  C CB  . ALA A 278  ? 0.2328 0.2194 0.2353 0.0311  0.0121  -0.0074 276  ALA A CB  
1921  N N   . GLN A 279  ? 0.2038 0.1846 0.2129 0.0293  0.0110  -0.0045 277  GLN A N   
1922  C CA  . GLN A 279  ? 0.2045 0.1816 0.2174 0.0289  0.0092  -0.0048 277  GLN A CA  
1923  C C   . GLN A 279  ? 0.2289 0.2076 0.2433 0.0287  0.0102  -0.0027 277  GLN A C   
1924  O O   . GLN A 279  ? 0.2257 0.2012 0.2424 0.0273  0.0091  -0.0012 277  GLN A O   
1925  C CB  . GLN A 279  ? 0.2235 0.1951 0.2366 0.0263  0.0077  -0.0031 277  GLN A CB  
1926  C CG  . GLN A 279  ? 0.2393 0.2092 0.2514 0.0263  0.0066  -0.0050 277  GLN A CG  
1927  C CD  . GLN A 279  ? 0.2833 0.2526 0.2986 0.0283  0.0047  -0.0089 277  GLN A CD  
1928  O OE1 . GLN A 279  ? 0.3857 0.3532 0.4049 0.0288  0.0032  -0.0094 277  GLN A OE1 
1929  N NE2 . GLN A 279  ? 0.2523 0.2233 0.2663 0.0298  0.0045  -0.0119 277  GLN A NE2 
1930  N N   . ALA A 280  ? 0.2213 0.2055 0.2347 0.0301  0.0122  -0.0026 278  ALA A N   
1931  C CA  . ALA A 280  ? 0.2182 0.2044 0.2329 0.0297  0.0133  -0.0003 278  ALA A CA  
1932  C C   . ALA A 280  ? 0.2253 0.2097 0.2440 0.0304  0.0118  -0.0014 278  ALA A C   
1933  O O   . ALA A 280  ? 0.2245 0.2077 0.2447 0.0290  0.0118  0.0010  278  ALA A O   
1934  C CB  . ALA A 280  ? 0.2417 0.2349 0.2553 0.0313  0.0155  -0.0002 278  ALA A CB  
1935  N N   . ALA A 281  ? 0.2147 0.1993 0.2356 0.0327  0.0104  -0.0052 279  ALA A N   
1936  C CA  . ALA A 281  ? 0.2340 0.2168 0.2595 0.0335  0.0087  -0.0062 279  ALA A CA  
1937  C C   . ALA A 281  ? 0.2343 0.2110 0.2613 0.0310  0.0068  -0.0038 279  ALA A C   
1938  O O   . ALA A 281  ? 0.2414 0.2171 0.2710 0.0303  0.0062  -0.0020 279  ALA A O   
1939  C CB  . ALA A 281  ? 0.2512 0.2351 0.2794 0.0366  0.0072  -0.0112 279  ALA A CB  
1940  N N   . ARG A 282  ? 0.2269 0.2000 0.2525 0.0295  0.0058  -0.0035 280  ARG A N   
1941  C CA  . ARG A 282  ? 0.2219 0.1903 0.2486 0.0269  0.0042  -0.0007 280  ARG A CA  
1942  C C   . ARG A 282  ? 0.2211 0.1903 0.2457 0.0246  0.0057  0.0029  280  ARG A C   
1943  O O   . ARG A 282  ? 0.2326 0.1999 0.2588 0.0230  0.0047  0.0053  280  ARG A O   
1944  C CB  . ARG A 282  ? 0.2316 0.1967 0.2572 0.0257  0.0030  -0.0011 280  ARG A CB  
1945  C CG  . ARG A 282  ? 0.2670 0.2304 0.2959 0.0276  0.0009  -0.0047 280  ARG A CG  
1946  C CD  . ARG A 282  ? 0.2627 0.2224 0.2912 0.0258  -0.0006 -0.0042 280  ARG A CD  
1947  N NE  . ARG A 282  ? 0.2610 0.2177 0.2910 0.0231  -0.0019 -0.0004 280  ARG A NE  
1948  C CZ  . ARG A 282  ? 0.2616 0.2160 0.2907 0.0207  -0.0027 0.0015  280  ARG A CZ  
1949  N NH1 . ARG A 282  ? 0.2631 0.2173 0.2898 0.0206  -0.0025 0.0001  280  ARG A NH1 
1950  N NH2 . ARG A 282  ? 0.2752 0.2281 0.3057 0.0184  -0.0037 0.0051  280  ARG A NH2 
1951  N N   . VAL A 283  ? 0.2086 0.1805 0.2297 0.0244  0.0079  0.0035  281  VAL A N   
1952  C CA  . VAL A 283  ? 0.2019 0.1746 0.2217 0.0223  0.0091  0.0066  281  VAL A CA  
1953  C C   . VAL A 283  ? 0.2240 0.1984 0.2465 0.0227  0.0093  0.0076  281  VAL A C   
1954  O O   . VAL A 283  ? 0.2160 0.1892 0.2394 0.0208  0.0087  0.0098  281  VAL A O   
1955  C CB  . VAL A 283  ? 0.2018 0.1772 0.2185 0.0223  0.0113  0.0071  281  VAL A CB  
1956  C CG1 . VAL A 283  ? 0.2428 0.2193 0.2594 0.0205  0.0125  0.0099  281  VAL A CG1 
1957  C CG2 . VAL A 283  ? 0.2206 0.1938 0.2347 0.0214  0.0109  0.0067  281  VAL A CG2 
1958  N N   . MET A 284  ? 0.2047 0.1825 0.2285 0.0251  0.0101  0.0059  282  MET A N   
1959  C CA  . MET A 284  ? 0.2015 0.1815 0.2282 0.0255  0.0103  0.0068  282  MET A CA  
1960  C C   . MET A 284  ? 0.2329 0.2099 0.2632 0.0255  0.0079  0.0067  282  MET A C   
1961  O O   . MET A 284  ? 0.2621 0.2395 0.2944 0.0248  0.0076  0.0085  282  MET A O   
1962  C CB  . MET A 284  ? 0.2208 0.2059 0.2480 0.0282  0.0118  0.0049  282  MET A CB  
1963  C CG  . MET A 284  ? 0.2304 0.2193 0.2545 0.0281  0.0141  0.0058  282  MET A CG  
1964  S SD  . MET A 284  ? 0.2578 0.2467 0.2809 0.0251  0.0154  0.0099  282  MET A SD  
1965  C CE  . MET A 284  ? 0.2606 0.2528 0.2874 0.0256  0.0158  0.0109  282  MET A CE  
1966  N N   . GLY A 285  ? 0.2238 0.1979 0.2554 0.0264  0.0061  0.0047  283  GLY A N   
1967  C CA  . GLY A 285  ? 0.2339 0.2051 0.2697 0.0265  0.0036  0.0049  283  GLY A CA  
1968  C C   . GLY A 285  ? 0.2298 0.1977 0.2655 0.0236  0.0022  0.0081  283  GLY A C   
1969  O O   . GLY A 285  ? 0.2502 0.2170 0.2891 0.0230  0.0005  0.0098  283  GLY A O   
1970  N N   . GLU A 286  ? 0.2227 0.1895 0.2548 0.0218  0.0027  0.0090  284  GLU A N   
1971  C CA  . GLU A 286  ? 0.2078 0.1720 0.2395 0.0191  0.0013  0.0115  284  GLU A CA  
1972  C C   . GLU A 286  ? 0.2394 0.2051 0.2677 0.0168  0.0028  0.0137  284  GLU A C   
1973  O O   . GLU A 286  ? 0.2583 0.2238 0.2870 0.0149  0.0018  0.0161  284  GLU A O   
1974  C CB  . GLU A 286  ? 0.2200 0.1814 0.2512 0.0189  0.0002  0.0104  284  GLU A CB  
1975  C CG  . GLU A 286  ? 0.2584 0.2179 0.2937 0.0211  -0.0017 0.0079  284  GLU A CG  
1976  C CD  . GLU A 286  ? 0.2851 0.2423 0.3198 0.0211  -0.0025 0.0062  284  GLU A CD  
1977  O OE1 . GLU A 286  ? 0.3112 0.2674 0.3435 0.0188  -0.0025 0.0081  284  GLU A OE1 
1978  O OE2 . GLU A 286  ? 0.3210 0.2779 0.3579 0.0235  -0.0033 0.0027  284  GLU A OE2 
1979  N N   . LEU A 287  ? 0.2020 0.1693 0.2272 0.0171  0.0049  0.0128  285  LEU A N   
1980  C CA  A LEU A 287  ? 0.2139 0.1824 0.2366 0.0151  0.0061  0.0144  285  LEU A CA  
1981  C CA  B LEU A 287  ? 0.2143 0.1828 0.2370 0.0151  0.0061  0.0144  285  LEU A CA  
1982  C C   . LEU A 287  ? 0.2361 0.2071 0.2603 0.0149  0.0068  0.0155  285  LEU A C   
1983  O O   . LEU A 287  ? 0.2181 0.1897 0.2423 0.0130  0.0064  0.0172  285  LEU A O   
1984  C CB  A LEU A 287  ? 0.2255 0.1947 0.2452 0.0153  0.0078  0.0133  285  LEU A CB  
1985  C CB  B LEU A 287  ? 0.2257 0.1948 0.2453 0.0154  0.0078  0.0133  285  LEU A CB  
1986  C CG  A LEU A 287  ? 0.2312 0.2003 0.2484 0.0133  0.0085  0.0144  285  LEU A CG  
1987  C CG  B LEU A 287  ? 0.2395 0.2103 0.2577 0.0140  0.0093  0.0145  285  LEU A CG  
1988  C CD1 A LEU A 287  ? 0.2118 0.1811 0.2265 0.0139  0.0098  0.0133  285  LEU A CD1 
1989  C CD1 B LEU A 287  ? 0.2567 0.2268 0.2744 0.0116  0.0084  0.0158  285  LEU A CD1 
1990  C CD2 A LEU A 287  ? 0.2773 0.2484 0.2953 0.0122  0.0093  0.0157  285  LEU A CD2 
1991  C CD2 B LEU A 287  ? 0.2246 0.1958 0.2403 0.0144  0.0107  0.0138  285  LEU A CD2 
1992  N N   . LEU A 288  ? 0.2320 0.2051 0.2575 0.0168  0.0078  0.0145  286  LEU A N   
1993  C CA  . LEU A 288  ? 0.2131 0.1888 0.2403 0.0167  0.0086  0.0156  286  LEU A CA  
1994  C C   . LEU A 288  ? 0.2278 0.2032 0.2573 0.0156  0.0069  0.0172  286  LEU A C   
1995  O O   . LEU A 288  ? 0.2177 0.1945 0.2472 0.0140  0.0072  0.0185  286  LEU A O   
1996  C CB  . LEU A 288  ? 0.2550 0.2335 0.2836 0.0192  0.0097  0.0143  286  LEU A CB  
1997  C CG  . LEU A 288  ? 0.2859 0.2674 0.3171 0.0194  0.0103  0.0153  286  LEU A CG  
1998  C CD1 . LEU A 288  ? 0.2914 0.2746 0.3218 0.0176  0.0116  0.0170  286  LEU A CD1 
1999  C CD2 . LEU A 288  ? 0.3652 0.3499 0.3978 0.0222  0.0112  0.0136  286  LEU A CD2 
2000  N N   . PRO A 289  ? 0.2120 0.1856 0.2438 0.0163  0.0050  0.0171  287  PRO A N   
2001  C CA  . PRO A 289  ? 0.2079 0.1817 0.2419 0.0151  0.0033  0.0192  287  PRO A CA  
2002  C C   . PRO A 289  ? 0.2371 0.2110 0.2690 0.0124  0.0028  0.0210  287  PRO A C   
2003  O O   . PRO A 289  ? 0.2169 0.1927 0.2499 0.0111  0.0021  0.0226  287  PRO A O   
2004  C CB  . PRO A 289  ? 0.2452 0.2167 0.2824 0.0164  0.0011  0.0189  287  PRO A CB  
2005  C CG  . PRO A 289  ? 0.3329 0.3041 0.3703 0.0189  0.0020  0.0160  287  PRO A CG  
2006  C CD  . PRO A 289  ? 0.2386 0.2104 0.2717 0.0184  0.0041  0.0152  287  PRO A CD  
2007  N N   . ARG A 290  ? 0.2011 0.1734 0.2302 0.0115  0.0030  0.0206  288  ARG A N   
2008  C CA  . ARG A 290  ? 0.2059 0.1791 0.2330 0.0091  0.0027  0.0218  288  ARG A CA  
2009  C C   . ARG A 290  ? 0.1948 0.1704 0.2208 0.0083  0.0042  0.0215  288  ARG A C   
2010  O O   . ARG A 290  ? 0.2039 0.1816 0.2298 0.0066  0.0036  0.0225  288  ARG A O   
2011  C CB  . ARG A 290  ? 0.2216 0.1927 0.2462 0.0086  0.0026  0.0213  288  ARG A CB  
2012  C CG  . ARG A 290  ? 0.2432 0.2120 0.2698 0.0090  0.0008  0.0218  288  ARG A CG  
2013  C CD  . ARG A 290  ? 0.2688 0.2356 0.2933 0.0087  0.0008  0.0209  288  ARG A CD  
2014  N NE  . ARG A 290  ? 0.3367 0.3009 0.3639 0.0093  -0.0012 0.0213  288  ARG A NE  
2015  C CZ  . ARG A 290  ? 0.3443 0.3063 0.3712 0.0099  -0.0014 0.0198  288  ARG A CZ  
2016  N NH1 . ARG A 290  ? 0.2942 0.2562 0.3177 0.0101  0.0002  0.0181  288  ARG A NH1 
2017  N NH2 . ARG A 290  ? 0.3703 0.3298 0.4007 0.0104  -0.0035 0.0200  288  ARG A NH2 
2018  N N   . VAL A 291  ? 0.1948 0.1703 0.2200 0.0093  0.0060  0.0201  289  VAL A N   
2019  C CA  . VAL A 291  ? 0.2004 0.1780 0.2257 0.0085  0.0072  0.0200  289  VAL A CA  
2020  C C   . VAL A 291  ? 0.1887 0.1686 0.2167 0.0084  0.0068  0.0209  289  VAL A C   
2021  O O   . VAL A 291  ? 0.1970 0.1788 0.2255 0.0069  0.0066  0.0212  289  VAL A O   
2022  C CB  . VAL A 291  ? 0.1904 0.1680 0.2151 0.0096  0.0091  0.0191  289  VAL A CB  
2023  C CG1 . VAL A 291  ? 0.2154 0.1946 0.2408 0.0085  0.0100  0.0193  289  VAL A CG1 
2024  C CG2 . VAL A 291  ? 0.2287 0.2042 0.2507 0.0099  0.0094  0.0182  289  VAL A CG2 
2025  N N   . LYS A 292  ? 0.1853 0.1652 0.2154 0.0101  0.0065  0.0211  290  LYS A N   
2026  C CA  . LYS A 292  ? 0.1649 0.1472 0.1979 0.0101  0.0060  0.0220  290  LYS A CA  
2027  C C   . LYS A 292  ? 0.2043 0.1876 0.2376 0.0084  0.0042  0.0233  290  LYS A C   
2028  O O   . LYS A 292  ? 0.1846 0.1705 0.2191 0.0073  0.0041  0.0238  290  LYS A O   
2029  C CB  . LYS A 292  ? 0.1929 0.1750 0.2283 0.0124  0.0058  0.0216  290  LYS A CB  
2030  C CG  . LYS A 292  ? 0.2032 0.1879 0.2418 0.0126  0.0053  0.0226  290  LYS A CG  
2031  C CD  . LYS A 292  ? 0.2095 0.1944 0.2510 0.0149  0.0049  0.0221  290  LYS A CD  
2032  C CE  . LYS A 292  ? 0.2335 0.2211 0.2783 0.0149  0.0042  0.0233  290  LYS A CE  
2033  N NZ  . LYS A 292  ? 0.2439 0.2325 0.2919 0.0175  0.0042  0.0223  290  LYS A NZ  
2034  N N   . ALA A 293  ? 0.1870 0.1687 0.2195 0.0080  0.0028  0.0241  291  ALA A N   
2035  C CA  . ALA A 293  ? 0.1889 0.1725 0.2217 0.0063  0.0010  0.0259  291  ALA A CA  
2036  C C   . ALA A 293  ? 0.1912 0.1773 0.2219 0.0043  0.0015  0.0253  291  ALA A C   
2037  O O   . ALA A 293  ? 0.2049 0.1943 0.2364 0.0032  0.0006  0.0260  291  ALA A O   
2038  C CB  . ALA A 293  ? 0.2027 0.1843 0.2352 0.0061  -0.0006 0.0273  291  ALA A CB  
2039  N N   . LEU A 294  ? 0.1733 0.1580 0.2015 0.0041  0.0027  0.0238  292  LEU A N   
2040  C CA  . LEU A 294  ? 0.1851 0.1721 0.2121 0.0025  0.0030  0.0227  292  LEU A CA  
2041  C C   . LEU A 294  ? 0.2016 0.1903 0.2307 0.0025  0.0038  0.0218  292  LEU A C   
2042  O O   . LEU A 294  ? 0.1842 0.1760 0.2138 0.0012  0.0032  0.0213  292  LEU A O   
2043  C CB  . LEU A 294  ? 0.2048 0.1897 0.2293 0.0024  0.0041  0.0213  292  LEU A CB  
2044  C CG  . LEU A 294  ? 0.1885 0.1721 0.2109 0.0021  0.0033  0.0220  292  LEU A CG  
2045  C CD1 . LEU A 294  ? 0.2075 0.1889 0.2278 0.0024  0.0045  0.0205  292  LEU A CD1 
2046  C CD2 . LEU A 294  ? 0.2182 0.2053 0.2398 0.0003  0.0019  0.0230  292  LEU A CD2 
2047  N N   . ALA A 295  ? 0.1761 0.1632 0.2066 0.0039  0.0050  0.0217  293  ALA A N   
2048  C CA  . ALA A 295  ? 0.1883 0.1773 0.2215 0.0038  0.0057  0.0213  293  ALA A CA  
2049  C C   . ALA A 295  ? 0.1817 0.1736 0.2172 0.0034  0.0045  0.0222  293  ALA A C   
2050  O O   . ALA A 295  ? 0.1824 0.1767 0.2197 0.0024  0.0043  0.0216  293  ALA A O   
2051  C CB  . ALA A 295  ? 0.1946 0.1823 0.2289 0.0054  0.0073  0.0214  293  ALA A CB  
2052  N N   . LEU A 296  ? 0.1642 0.1559 0.2001 0.0042  0.0034  0.0236  294  LEU A N   
2053  C CA  . LEU A 296  ? 0.1677 0.1624 0.2059 0.0038  0.0021  0.0248  294  LEU A CA  
2054  C C   . LEU A 296  ? 0.1771 0.1750 0.2142 0.0019  0.0008  0.0247  294  LEU A C   
2055  O O   . LEU A 296  ? 0.1946 0.1959 0.2336 0.0011  0.0001  0.0247  294  LEU A O   
2056  C CB  . LEU A 296  ? 0.1810 0.1745 0.2201 0.0050  0.0009  0.0266  294  LEU A CB  
2057  C CG  . LEU A 296  ? 0.2077 0.1995 0.2489 0.0073  0.0018  0.0263  294  LEU A CG  
2058  C CD1 . LEU A 296  ? 0.2091 0.1991 0.2514 0.0085  0.0003  0.0275  294  LEU A CD1 
2059  C CD2 . LEU A 296  ? 0.2306 0.2254 0.2750 0.0077  0.0021  0.0264  294  LEU A CD2 
2060  N N   . LEU A 297  ? 0.1786 0.1762 0.2128 0.0010  0.0004  0.0245  295  LEU A N   
2061  C CA  . LEU A 297  ? 0.1933 0.1950 0.2263 -0.0008 -0.0007 0.0241  295  LEU A CA  
2062  C C   . LEU A 297  ? 0.1895 0.1926 0.2232 -0.0016 0.0001  0.0213  295  LEU A C   
2063  O O   . LEU A 297  ? 0.1920 0.1994 0.2267 -0.0026 -0.0009 0.0204  295  LEU A O   
2064  C CB  . LEU A 297  ? 0.2073 0.2086 0.2371 -0.0015 -0.0011 0.0247  295  LEU A CB  
2065  C CG  . LEU A 297  ? 0.2798 0.2867 0.3083 -0.0032 -0.0025 0.0250  295  LEU A CG  
2066  C CD1 . LEU A 297  ? 0.3002 0.3106 0.3303 -0.0035 -0.0043 0.0277  295  LEU A CD1 
2067  C CD2 . LEU A 297  ? 0.2814 0.2880 0.3069 -0.0038 -0.0027 0.0257  295  LEU A CD2 
2068  N N   . ALA A 298  ? 0.1699 0.1697 0.2034 -0.0010 0.0016  0.0199  296  ALA A N   
2069  C CA  . ALA A 298  ? 0.1776 0.1781 0.2129 -0.0017 0.0022  0.0175  296  ALA A CA  
2070  C C   . ALA A 298  ? 0.1907 0.1930 0.2298 -0.0017 0.0020  0.0176  296  ALA A C   
2071  O O   . ALA A 298  ? 0.1998 0.2049 0.2409 -0.0027 0.0013  0.0157  296  ALA A O   
2072  C CB  . ALA A 298  ? 0.1873 0.1838 0.2222 -0.0010 0.0038  0.0167  296  ALA A CB  
2073  N N   . LYS A 299  ? 0.1713 0.1723 0.2117 -0.0005 0.0025  0.0195  297  LYS A N   
2074  C CA  A LYS A 299  ? 0.1699 0.1731 0.2141 -0.0004 0.0023  0.0199  297  LYS A CA  
2075  C CA  B LYS A 299  ? 0.1707 0.1739 0.2149 -0.0004 0.0023  0.0199  297  LYS A CA  
2076  C C   . LYS A 299  ? 0.1976 0.2053 0.2423 -0.0015 0.0004  0.0198  297  LYS A C   
2077  O O   . LYS A 299  ? 0.2121 0.2226 0.2598 -0.0023 -0.0001 0.0186  297  LYS A O   
2078  C CB  A LYS A 299  ? 0.1940 0.1957 0.2392 0.0013  0.0030  0.0219  297  LYS A CB  
2079  C CB  B LYS A 299  ? 0.1943 0.1960 0.2395 0.0013  0.0030  0.0219  297  LYS A CB  
2080  C CG  A LYS A 299  ? 0.1950 0.1997 0.2438 0.0014  0.0024  0.0227  297  LYS A CG  
2081  C CG  B LYS A 299  ? 0.1954 0.1999 0.2443 0.0015  0.0025  0.0227  297  LYS A CG  
2082  C CD  A LYS A 299  ? 0.2027 0.2062 0.2527 0.0034  0.0032  0.0242  297  LYS A CD  
2083  C CD  B LYS A 299  ? 0.2037 0.2069 0.2536 0.0034  0.0035  0.0242  297  LYS A CD  
2084  C CE  A LYS A 299  ? 0.2083 0.2150 0.2614 0.0036  0.0021  0.0253  297  LYS A CE  
2085  C CE  B LYS A 299  ? 0.2209 0.2273 0.2743 0.0038  0.0027  0.0251  297  LYS A CE  
2086  N NZ  A LYS A 299  ? 0.2255 0.2318 0.2806 0.0057  0.0031  0.0262  297  LYS A NZ  
2087  N NZ  B LYS A 299  ? 0.2503 0.2586 0.3030 0.0032  0.0005  0.0260  297  LYS A NZ  
2088  N N   . ASN A 300  ? 0.2007 0.2095 0.2430 -0.0016 -0.0008 0.0212  298  ASN A N   
2089  C CA  . ASN A 300  ? 0.1797 0.1937 0.2225 -0.0025 -0.0026 0.0216  298  ASN A CA  
2090  C C   . ASN A 300  ? 0.2030 0.2207 0.2455 -0.0041 -0.0033 0.0187  298  ASN A C   
2091  O O   . ASN A 300  ? 0.2434 0.2656 0.2880 -0.0048 -0.0044 0.0178  298  ASN A O   
2092  C CB  . ASN A 300  ? 0.2114 0.2262 0.2521 -0.0024 -0.0039 0.0244  298  ASN A CB  
2093  C CG  . ASN A 300  ? 0.3086 0.3290 0.3504 -0.0032 -0.0058 0.0256  298  ASN A CG  
2094  O OD1 . ASN A 300  ? 0.3820 0.4030 0.4266 -0.0025 -0.0063 0.0270  298  ASN A OD1 
2095  N ND2 . ASN A 300  ? 0.2878 0.3130 0.3276 -0.0046 -0.0069 0.0249  298  ASN A ND2 
2096  N N   . TYR A 301  ? 0.1968 0.2132 0.2371 -0.0044 -0.0026 0.0170  299  TYR A N   
2097  C CA  . TYR A 301  ? 0.2013 0.2213 0.2418 -0.0056 -0.0033 0.0135  299  TYR A CA  
2098  C C   . TYR A 301  ? 0.1885 0.2066 0.2328 -0.0057 -0.0026 0.0110  299  TYR A C   
2099  O O   . TYR A 301  ? 0.2158 0.2367 0.2615 -0.0066 -0.0034 0.0076  299  TYR A O   
2100  C CB  . TYR A 301  ? 0.1948 0.2143 0.2316 -0.0059 -0.0030 0.0126  299  TYR A CB  
2101  C CG  . TYR A 301  ? 0.1984 0.2216 0.2318 -0.0064 -0.0041 0.0147  299  TYR A CG  
2102  C CD1 . TYR A 301  ? 0.2162 0.2466 0.2491 -0.0074 -0.0057 0.0140  299  TYR A CD1 
2103  C CD2 . TYR A 301  ? 0.2082 0.2281 0.2391 -0.0059 -0.0036 0.0174  299  TYR A CD2 
2104  C CE1 . TYR A 301  ? 0.2120 0.2465 0.2420 -0.0081 -0.0067 0.0165  299  TYR A CE1 
2105  C CE2 . TYR A 301  ? 0.2147 0.2380 0.2431 -0.0065 -0.0047 0.0198  299  TYR A CE2 
2106  C CZ  . TYR A 301  ? 0.2276 0.2584 0.2556 -0.0077 -0.0062 0.0196  299  TYR A CZ  
2107  O OH  . TYR A 301  ? 0.2426 0.2775 0.2682 -0.0085 -0.0073 0.0227  299  TYR A OH  
2108  N N   . ASP A 302  ? 0.1837 0.1973 0.2299 -0.0048 -0.0012 0.0125  300  ASP A N   
2109  C CA  . ASP A 302  ? 0.1884 0.1999 0.2386 -0.0049 -0.0004 0.0110  300  ASP A CA  
2110  C C   . ASP A 302  ? 0.1953 0.2051 0.2451 -0.0053 -0.0001 0.0084  300  ASP A C   
2111  O O   . ASP A 302  ? 0.2031 0.2142 0.2563 -0.0061 -0.0008 0.0055  300  ASP A O   
2112  C CB  . ASP A 302  ? 0.1832 0.1980 0.2381 -0.0057 -0.0015 0.0098  300  ASP A CB  
2113  C CG  . ASP A 302  ? 0.2504 0.2627 0.3101 -0.0057 -0.0005 0.0102  300  ASP A CG  
2114  O OD1 . ASP A 302  ? 0.2200 0.2287 0.2791 -0.0047 0.0012  0.0126  300  ASP A OD1 
2115  O OD2 . ASP A 302  ? 0.2702 0.2842 0.3345 -0.0067 -0.0014 0.0081  300  ASP A OD2 
2116  N N   . ILE A 303  ? 0.1687 0.1756 0.2148 -0.0046 0.0009  0.0094  301  ILE A N   
2117  C CA  . ILE A 303  ? 0.1829 0.1876 0.2285 -0.0047 0.0013  0.0073  301  ILE A CA  
2118  C C   . ILE A 303  ? 0.1853 0.1850 0.2309 -0.0037 0.0031  0.0094  301  ILE A C   
2119  O O   . ILE A 303  ? 0.1896 0.1878 0.2342 -0.0028 0.0040  0.0121  301  ILE A O   
2120  C CB  . ILE A 303  ? 0.1852 0.1918 0.2264 -0.0050 0.0008  0.0063  301  ILE A CB  
2121  C CG1 . ILE A 303  ? 0.1837 0.1879 0.2207 -0.0041 0.0016  0.0094  301  ILE A CG1 
2122  C CG2 . ILE A 303  ? 0.1970 0.2098 0.2377 -0.0059 -0.0009 0.0047  301  ILE A CG2 
2123  C CD1 . ILE A 303  ? 0.2071 0.2125 0.2401 -0.0045 0.0013  0.0087  301  ILE A CD1 
2124  N N   . GLY A 304  ? 0.1884 0.1859 0.2351 -0.0038 0.0035  0.0079  302  GLY A N   
2125  C CA  . GLY A 304  ? 0.1731 0.1665 0.2194 -0.0029 0.0051  0.0098  302  GLY A CA  
2126  C C   . GLY A 304  ? 0.1843 0.1762 0.2253 -0.0021 0.0058  0.0108  302  GLY A C   
2127  O O   . GLY A 304  ? 0.1871 0.1805 0.2252 -0.0025 0.0050  0.0094  302  GLY A O   
2128  N N   . LEU A 305  ? 0.1876 0.1771 0.2274 -0.0010 0.0071  0.0132  303  LEU A N   
2129  C CA  . LEU A 305  ? 0.1664 0.1538 0.2019 -0.0001 0.0077  0.0140  303  LEU A CA  
2130  C C   . LEU A 305  ? 0.1893 0.1741 0.2253 0.0008  0.0091  0.0150  303  LEU A C   
2131  O O   . LEU A 305  ? 0.1952 0.1799 0.2326 0.0016  0.0101  0.0169  303  LEU A O   
2132  C CB  . LEU A 305  ? 0.1969 0.1847 0.2303 0.0007  0.0075  0.0157  303  LEU A CB  
2133  C CG  . LEU A 305  ? 0.2312 0.2169 0.2608 0.0015  0.0078  0.0164  303  LEU A CG  
2134  C CD1 . LEU A 305  ? 0.2665 0.2533 0.2947 0.0015  0.0067  0.0175  303  LEU A CD1 
2135  C CD2 . LEU A 305  ? 0.2876 0.2709 0.3169 0.0030  0.0092  0.0174  303  LEU A CD2 
2136  N N   . ASN A 306  ? 0.1799 0.1631 0.2148 0.0007  0.0093  0.0139  304  ASN A N   
2137  C CA  . ASN A 306  ? 0.1982 0.1793 0.2338 0.0013  0.0105  0.0150  304  ASN A CA  
2138  C C   . ASN A 306  ? 0.1887 0.1682 0.2200 0.0025  0.0112  0.0156  304  ASN A C   
2139  O O   . ASN A 306  ? 0.1983 0.1775 0.2267 0.0022  0.0106  0.0144  304  ASN A O   
2140  C CB  . ASN A 306  ? 0.1907 0.1711 0.2289 0.0005  0.0100  0.0132  304  ASN A CB  
2141  C CG  . ASN A 306  ? 0.2192 0.1975 0.2577 0.0012  0.0110  0.0145  304  ASN A CG  
2142  O OD1 . ASN A 306  ? 0.2431 0.2200 0.2787 0.0016  0.0112  0.0139  304  ASN A OD1 
2143  N ND2 . ASN A 306  ? 0.1881 0.1665 0.2303 0.0013  0.0117  0.0167  304  ASN A ND2 
2144  N N   . ILE A 307  ? 0.1781 0.1570 0.2092 0.0036  0.0125  0.0175  305  ILE A N   
2145  C CA  . ILE A 307  ? 0.1881 0.1655 0.2156 0.0048  0.0131  0.0177  305  ILE A CA  
2146  C C   . ILE A 307  ? 0.1772 0.1534 0.2050 0.0047  0.0136  0.0178  305  ILE A C   
2147  O O   . ILE A 307  ? 0.1861 0.1627 0.2165 0.0049  0.0144  0.0194  305  ILE A O   
2148  C CB  . ILE A 307  ? 0.2044 0.1827 0.2312 0.0063  0.0141  0.0193  305  ILE A CB  
2149  C CG1 . ILE A 307  ? 0.2203 0.1995 0.2472 0.0065  0.0134  0.0191  305  ILE A CG1 
2150  C CG2 . ILE A 307  ? 0.2377 0.2147 0.2610 0.0076  0.0147  0.0191  305  ILE A CG2 
2151  C CD1 . ILE A 307  ? 0.2850 0.2657 0.3124 0.0080  0.0143  0.0202  305  ILE A CD1 
2152  N N   . ASP A 308  ? 0.1793 0.1543 0.2049 0.0045  0.0130  0.0162  306  ASP A N   
2153  C CA  . ASP A 308  ? 0.1804 0.1541 0.2063 0.0045  0.0133  0.0161  306  ASP A CA  
2154  C C   . ASP A 308  ? 0.1764 0.1498 0.2005 0.0059  0.0145  0.0178  306  ASP A C   
2155  O O   . ASP A 308  ? 0.2016 0.1754 0.2230 0.0069  0.0149  0.0181  306  ASP A O   
2156  C CB  . ASP A 308  ? 0.2006 0.1736 0.2241 0.0041  0.0125  0.0139  306  ASP A CB  
2157  C CG  . ASP A 308  ? 0.2490 0.2232 0.2745 0.0028  0.0114  0.0117  306  ASP A CG  
2158  O OD1 . ASP A 308  ? 0.2374 0.2123 0.2667 0.0022  0.0110  0.0116  306  ASP A OD1 
2159  O OD2 . ASP A 308  ? 0.2580 0.2327 0.2814 0.0024  0.0107  0.0099  306  ASP A OD2 
2160  N N   . ALA A 309  ? 0.1772 0.1504 0.2030 0.0061  0.0150  0.0190  307  ALA A N   
2161  C CA  . ALA A 309  ? 0.1788 0.1526 0.2027 0.0074  0.0161  0.0207  307  ALA A CA  
2162  C C   . ALA A 309  ? 0.1882 0.1605 0.2090 0.0078  0.0159  0.0195  307  ALA A C   
2163  O O   . ALA A 309  ? 0.2123 0.1833 0.2340 0.0071  0.0151  0.0182  307  ALA A O   
2164  C CB  . ALA A 309  ? 0.1906 0.1656 0.2183 0.0073  0.0168  0.0235  307  ALA A CB  
2165  N N   . GLU A 310  ? 0.1888 0.1618 0.2062 0.0091  0.0164  0.0197  308  GLU A N   
2166  C CA  . GLU A 310  ? 0.1938 0.1656 0.2081 0.0096  0.0161  0.0184  308  GLU A CA  
2167  C C   . GLU A 310  ? 0.1973 0.1704 0.2105 0.0108  0.0170  0.0199  308  GLU A C   
2168  O O   . GLU A 310  ? 0.1969 0.1712 0.2129 0.0106  0.0175  0.0221  308  GLU A O   
2169  C CB  . GLU A 310  ? 0.2040 0.1751 0.2153 0.0098  0.0155  0.0166  308  GLU A CB  
2170  C CG  . GLU A 310  ? 0.2241 0.1945 0.2365 0.0084  0.0146  0.0156  308  GLU A CG  
2171  C CD  . GLU A 310  ? 0.2272 0.1969 0.2373 0.0084  0.0137  0.0145  308  GLU A CD  
2172  O OE1 . GLU A 310  ? 0.2649 0.2337 0.2732 0.0080  0.0132  0.0134  308  GLU A OE1 
2173  O OE2 . GLU A 310  ? 0.2273 0.1975 0.2379 0.0086  0.0136  0.0148  308  GLU A OE2 
2174  N N   . GLU A 311  ? 0.2005 0.1739 0.2103 0.0119  0.0171  0.0189  309  GLU A N   
2175  C CA  . GLU A 311  ? 0.2076 0.1830 0.2162 0.0130  0.0178  0.0201  309  GLU A CA  
2176  C C   . GLU A 311  ? 0.1969 0.1760 0.2063 0.0140  0.0190  0.0223  309  GLU A C   
2177  O O   . GLU A 311  ? 0.1917 0.1718 0.2018 0.0142  0.0192  0.0223  309  GLU A O   
2178  C CB  . GLU A 311  ? 0.2315 0.2066 0.2363 0.0141  0.0174  0.0181  309  GLU A CB  
2179  C CG  . GLU A 311  ? 0.2498 0.2220 0.2536 0.0131  0.0163  0.0163  309  GLU A CG  
2180  C CD  . GLU A 311  ? 0.2737 0.2440 0.2773 0.0122  0.0154  0.0146  309  GLU A CD  
2181  O OE1 . GLU A 311  ? 0.2258 0.1964 0.2305 0.0121  0.0155  0.0148  309  GLU A OE1 
2182  O OE2 . GLU A 311  ? 0.3506 0.3194 0.3530 0.0115  0.0146  0.0132  309  GLU A OE2 
2183  N N   . ALA A 312  ? 0.1915 0.1732 0.2009 0.0147  0.0197  0.0245  310  ALA A N   
2184  C CA  . ALA A 312  ? 0.1917 0.1780 0.2021 0.0155  0.0209  0.0272  310  ALA A CA  
2185  C C   . ALA A 312  ? 0.1843 0.1735 0.1920 0.0172  0.0214  0.0255  310  ALA A C   
2186  O O   . ALA A 312  ? 0.2082 0.2008 0.2172 0.0177  0.0223  0.0268  310  ALA A O   
2187  C CB  . ALA A 312  ? 0.2023 0.1915 0.2130 0.0159  0.0214  0.0301  310  ALA A CB  
2188  N N   . ASP A 313  ? 0.2086 0.1966 0.2131 0.0181  0.0208  0.0224  311  ASP A N   
2189  C CA  . ASP A 313  ? 0.1981 0.1886 0.2007 0.0199  0.0210  0.0202  311  ASP A CA  
2190  C C   . ASP A 313  ? 0.1994 0.1877 0.2034 0.0196  0.0204  0.0186  311  ASP A C   
2191  O O   . ASP A 313  ? 0.2099 0.1998 0.2131 0.0211  0.0203  0.0165  311  ASP A O   
2192  C CB  . ASP A 313  ? 0.2320 0.2226 0.2314 0.0212  0.0203  0.0175  311  ASP A CB  
2193  C CG  . ASP A 313  ? 0.2728 0.2578 0.2715 0.0201  0.0188  0.0152  311  ASP A CG  
2194  O OD1 . ASP A 313  ? 0.2560 0.2375 0.2565 0.0185  0.0183  0.0156  311  ASP A OD1 
2195  O OD2 . ASP A 313  ? 0.3165 0.3013 0.3131 0.0210  0.0181  0.0130  311  ASP A OD2 
2196  N N   . ARG A 314  ? 0.1947 0.1796 0.2009 0.0177  0.0199  0.0194  312  ARG A N   
2197  C CA  . ARG A 314  ? 0.1922 0.1757 0.1999 0.0173  0.0194  0.0185  312  ARG A CA  
2198  C C   . ARG A 314  ? 0.2084 0.1939 0.2192 0.0167  0.0202  0.0209  312  ARG A C   
2199  O O   . ARG A 314  ? 0.1998 0.1850 0.2120 0.0165  0.0199  0.0203  312  ARG A O   
2200  C CB  . ARG A 314  ? 0.2173 0.1960 0.2250 0.0156  0.0180  0.0173  312  ARG A CB  
2201  C CG  . ARG A 314  ? 0.2279 0.2047 0.2332 0.0162  0.0170  0.0149  312  ARG A CG  
2202  C CD  . ARG A 314  ? 0.2530 0.2264 0.2579 0.0146  0.0159  0.0143  312  ARG A CD  
2203  N NE  . ARG A 314  ? 0.2378 0.2094 0.2415 0.0148  0.0147  0.0123  312  ARG A NE  
2204  C CZ  . ARG A 314  ? 0.2293 0.1984 0.2323 0.0135  0.0136  0.0117  312  ARG A CZ  
2205  N NH1 . ARG A 314  ? 0.2309 0.1995 0.2341 0.0121  0.0137  0.0124  312  ARG A NH1 
2206  N NH2 . ARG A 314  ? 0.2592 0.2268 0.2619 0.0136  0.0124  0.0105  312  ARG A NH2 
2207  N N   . LEU A 315  ? 0.1993 0.1871 0.2116 0.0163  0.0211  0.0237  313  LEU A N   
2208  C CA  . LEU A 315  ? 0.1995 0.1891 0.2155 0.0154  0.0218  0.0263  313  LEU A CA  
2209  C C   . LEU A 315  ? 0.1915 0.1850 0.2079 0.0167  0.0225  0.0262  313  LEU A C   
2210  O O   . LEU A 315  ? 0.1875 0.1804 0.2061 0.0160  0.0223  0.0260  313  LEU A O   
2211  C CB  . LEU A 315  ? 0.2055 0.1976 0.2233 0.0149  0.0226  0.0297  313  LEU A CB  
2212  C CG  . LEU A 315  ? 0.1982 0.1904 0.2210 0.0132  0.0227  0.0327  313  LEU A CG  
2213  C CD1 . LEU A 315  ? 0.2126 0.2070 0.2375 0.0129  0.0232  0.0364  313  LEU A CD1 
2214  C CD2 . LEU A 315  ? 0.2401 0.2357 0.2650 0.0134  0.0234  0.0337  313  LEU A CD2 
2215  N N   . GLU A 316  ? 0.1871 0.1853 0.2016 0.0185  0.0235  0.0261  314  GLU A N   
2216  C CA  . GLU A 316  ? 0.1855 0.1885 0.2009 0.0199  0.0244  0.0261  314  GLU A CA  
2217  C C   . GLU A 316  ? 0.2170 0.2175 0.2319 0.0207  0.0234  0.0227  314  GLU A C   
2218  O O   . GLU A 316  ? 0.1998 0.2019 0.2169 0.0209  0.0236  0.0228  314  GLU A O   
2219  C CB  . GLU A 316  ? 0.1996 0.2093 0.2131 0.0218  0.0258  0.0268  314  GLU A CB  
2220  C CG  . GLU A 316  ? 0.2027 0.2156 0.2179 0.0207  0.0268  0.0315  314  GLU A CG  
2221  C CD  . GLU A 316  ? 0.2214 0.2421 0.2347 0.0225  0.0282  0.0329  314  GLU A CD  
2222  O OE1 . GLU A 316  ? 0.2317 0.2576 0.2442 0.0244  0.0290  0.0312  314  GLU A OE1 
2223  O OE2 . GLU A 316  ? 0.2291 0.2513 0.2421 0.0220  0.0285  0.0356  314  GLU A OE2 
2224  N N   . LEU A 317  ? 0.2109 0.2075 0.2234 0.0211  0.0222  0.0199  315  LEU A N   
2225  C CA  . LEU A 317  ? 0.2225 0.2163 0.2354 0.0215  0.0209  0.0171  315  LEU A CA  
2226  C C   . LEU A 317  ? 0.2070 0.1978 0.2224 0.0196  0.0202  0.0182  315  LEU A C   
2227  O O   . LEU A 317  ? 0.2120 0.2032 0.2293 0.0201  0.0198  0.0175  315  LEU A O   
2228  C CB  . LEU A 317  ? 0.2395 0.2292 0.2500 0.0216  0.0195  0.0147  315  LEU A CB  
2229  C CG  . LEU A 317  ? 0.2477 0.2339 0.2590 0.0218  0.0178  0.0125  315  LEU A CG  
2230  C CD1 . LEU A 317  ? 0.2801 0.2695 0.2927 0.0241  0.0179  0.0105  315  LEU A CD1 
2231  C CD2 . LEU A 317  ? 0.2710 0.2536 0.2803 0.0215  0.0166  0.0107  315  LEU A CD2 
2232  N N   . SER A 318  ? 0.1777 0.1660 0.1937 0.0176  0.0200  0.0198  316  SER A N   
2233  C CA  . SER A 318  ? 0.1762 0.1623 0.1946 0.0158  0.0192  0.0205  316  SER A CA  
2234  C C   . SER A 318  ? 0.1961 0.1857 0.2177 0.0158  0.0201  0.0222  316  SER A C   
2235  O O   . SER A 318  ? 0.1910 0.1798 0.2145 0.0151  0.0194  0.0220  316  SER A O   
2236  C CB  . SER A 318  ? 0.1767 0.1602 0.1955 0.0138  0.0188  0.0213  316  SER A CB  
2237  O OG  . SER A 318  ? 0.1918 0.1775 0.2126 0.0133  0.0199  0.0238  316  SER A OG  
2238  N N   . LEU A 319  ? 0.1863 0.1803 0.2084 0.0166  0.0216  0.0241  317  LEU A N   
2239  C CA  . LEU A 319  ? 0.1863 0.1843 0.2115 0.0167  0.0226  0.0259  317  LEU A CA  
2240  C C   . LEU A 319  ? 0.1988 0.1986 0.2242 0.0184  0.0224  0.0240  317  LEU A C   
2241  O O   . LEU A 319  ? 0.2032 0.2046 0.2315 0.0180  0.0225  0.0248  317  LEU A O   
2242  C CB  . LEU A 319  ? 0.2002 0.2035 0.2259 0.0172  0.0243  0.0286  317  LEU A CB  
2243  C CG  . LEU A 319  ? 0.2173 0.2192 0.2441 0.0155  0.0243  0.0313  317  LEU A CG  
2244  C CD1 . LEU A 319  ? 0.2295 0.2374 0.2568 0.0161  0.0259  0.0345  317  LEU A CD1 
2245  C CD2 . LEU A 319  ? 0.2180 0.2174 0.2490 0.0132  0.0236  0.0325  317  LEU A CD2 
2246  N N   . ASP A 320  ? 0.2033 0.2029 0.2261 0.0202  0.0220  0.0213  318  ASP A N   
2247  C CA  . ASP A 320  ? 0.2238 0.2247 0.2476 0.0220  0.0215  0.0192  318  ASP A CA  
2248  C C   . ASP A 320  ? 0.2251 0.2216 0.2505 0.0207  0.0199  0.0187  318  ASP A C   
2249  O O   . ASP A 320  ? 0.2408 0.2387 0.2686 0.0213  0.0196  0.0184  318  ASP A O   
2250  C CB  . ASP A 320  ? 0.2204 0.2217 0.2419 0.0243  0.0212  0.0161  318  ASP A CB  
2251  C CG  . ASP A 320  ? 0.2664 0.2743 0.2868 0.0261  0.0230  0.0163  318  ASP A CG  
2252  O OD1 . ASP A 320  ? 0.2827 0.2959 0.3052 0.0269  0.0241  0.0172  318  ASP A OD1 
2253  O OD2 . ASP A 320  ? 0.3003 0.3087 0.3179 0.0266  0.0233  0.0158  318  ASP A OD2 
2254  N N   . LEU A 321  ? 0.1960 0.1877 0.2201 0.0190  0.0187  0.0187  319  LEU A N   
2255  C CA  . LEU A 321  ? 0.2036 0.1922 0.2291 0.0176  0.0172  0.0186  319  LEU A CA  
2256  C C   . LEU A 321  ? 0.1965 0.1865 0.2248 0.0161  0.0175  0.0206  319  LEU A C   
2257  O O   . LEU A 321  ? 0.2244 0.2149 0.2549 0.0159  0.0168  0.0206  319  LEU A O   
2258  C CB  . LEU A 321  ? 0.2203 0.2046 0.2437 0.0162  0.0160  0.0180  319  LEU A CB  
2259  C CG  . LEU A 321  ? 0.2434 0.2255 0.2651 0.0175  0.0149  0.0159  319  LEU A CG  
2260  C CD1 . LEU A 321  ? 0.3026 0.2855 0.3218 0.0185  0.0158  0.0151  319  LEU A CD1 
2261  C CD2 . LEU A 321  ? 0.3206 0.2990 0.3415 0.0158  0.0132  0.0159  319  LEU A CD2 
2262  N N   . LEU A 322  ? 0.2014 0.1924 0.2302 0.0149  0.0185  0.0223  320  LEU A N   
2263  C CA  . LEU A 322  ? 0.2157 0.2080 0.2479 0.0133  0.0187  0.0241  320  LEU A CA  
2264  C C   . LEU A 322  ? 0.2139 0.2104 0.2486 0.0144  0.0195  0.0249  320  LEU A C   
2265  O O   . LEU A 322  ? 0.2163 0.2134 0.2539 0.0136  0.0189  0.0253  320  LEU A O   
2266  C CB  . LEU A 322  ? 0.2075 0.2003 0.2405 0.0122  0.0196  0.0260  320  LEU A CB  
2267  C CG  . LEU A 322  ? 0.2230 0.2166 0.2604 0.0104  0.0195  0.0277  320  LEU A CG  
2268  C CD1 . LEU A 322  ? 0.2148 0.2053 0.2530 0.0087  0.0178  0.0262  320  LEU A CD1 
2269  C CD2 . LEU A 322  ? 0.1958 0.1903 0.2349 0.0096  0.0204  0.0300  320  LEU A CD2 
2270  N N   . GLU A 323  ? 0.1976 0.1977 0.2315 0.0164  0.0208  0.0248  321  GLU A N   
2271  C CA  . GLU A 323  ? 0.2120 0.2171 0.2483 0.0177  0.0218  0.0254  321  GLU A CA  
2272  C C   . GLU A 323  ? 0.2341 0.2381 0.2715 0.0185  0.0204  0.0236  321  GLU A C   
2273  O O   . GLU A 323  ? 0.2064 0.2123 0.2469 0.0181  0.0203  0.0244  321  GLU A O   
2274  C CB  . GLU A 323  ? 0.2089 0.2187 0.2436 0.0200  0.0233  0.0250  321  GLU A CB  
2275  C CG  . GLU A 323  ? 0.2813 0.2969 0.3180 0.0219  0.0242  0.0247  321  GLU A CG  
2276  C CD  . GLU A 323  ? 0.3536 0.3757 0.3923 0.0217  0.0262  0.0278  321  GLU A CD  
2277  O OE1 . GLU A 323  ? 0.3355 0.3577 0.3739 0.0202  0.0268  0.0303  321  GLU A OE1 
2278  O OE2 . GLU A 323  ? 0.3462 0.3737 0.3872 0.0229  0.0270  0.0279  321  GLU A OE2 
2279  N N   . VAL A 324  ? 0.2143 0.2153 0.2495 0.0197  0.0192  0.0212  322  VAL A N   
2280  C CA  . VAL A 324  ? 0.2300 0.2298 0.2668 0.0205  0.0177  0.0198  322  VAL A CA  
2281  C C   . VAL A 324  ? 0.2002 0.1977 0.2386 0.0182  0.0164  0.0209  322  VAL A C   
2282  O O   . VAL A 324  ? 0.2073 0.2063 0.2486 0.0184  0.0158  0.0212  322  VAL A O   
2283  C CB  . VAL A 324  ? 0.2365 0.2331 0.2714 0.0219  0.0165  0.0173  322  VAL A CB  
2284  C CG1 . VAL A 324  ? 0.2732 0.2682 0.3105 0.0224  0.0146  0.0165  322  VAL A CG1 
2285  C CG2 . VAL A 324  ? 0.2586 0.2585 0.2924 0.0245  0.0176  0.0154  322  VAL A CG2 
2286  N N   . LEU A 325  ? 0.1877 0.1821 0.2245 0.0162  0.0159  0.0215  323  LEU A N   
2287  C CA  . LEU A 325  ? 0.1984 0.1913 0.2365 0.0141  0.0146  0.0222  323  LEU A CA  
2288  C C   . LEU A 325  ? 0.1938 0.1899 0.2354 0.0132  0.0153  0.0237  323  LEU A C   
2289  O O   . LEU A 325  ? 0.1957 0.1926 0.2396 0.0127  0.0142  0.0239  323  LEU A O   
2290  C CB  . LEU A 325  ? 0.2088 0.1986 0.2447 0.0123  0.0141  0.0220  323  LEU A CB  
2291  C CG  . LEU A 325  ? 0.2320 0.2186 0.2647 0.0128  0.0131  0.0208  323  LEU A CG  
2292  C CD1 . LEU A 325  ? 0.2265 0.2110 0.2569 0.0114  0.0132  0.0206  323  LEU A CD1 
2293  C CD2 . LEU A 325  ? 0.2180 0.2035 0.2515 0.0123  0.0112  0.0207  323  LEU A CD2 
2294  N N   . CYS A 326  ? 0.1998 0.1981 0.2422 0.0130  0.0169  0.0249  324  CYS A N   
2295  C CA  . CYS A 326  ? 0.1954 0.1967 0.2417 0.0119  0.0174  0.0266  324  CYS A CA  
2296  C C   . CYS A 326  ? 0.2147 0.2200 0.2634 0.0134  0.0179  0.0270  324  CYS A C   
2297  O O   . CYS A 326  ? 0.2115 0.2190 0.2638 0.0123  0.0177  0.0281  324  CYS A O   
2298  C CB  . CYS A 326  ? 0.1967 0.1993 0.2439 0.0111  0.0188  0.0285  324  CYS A CB  
2299  S SG  . CYS A 326  ? 0.2344 0.2326 0.2805 0.0090  0.0180  0.0281  324  CYS A SG  
2300  N N   . LEU A 327  ? 0.1860 0.1926 0.2334 0.0158  0.0183  0.0258  325  LEU A N   
2301  C CA  . LEU A 327  ? 0.1892 0.1998 0.2390 0.0176  0.0187  0.0255  325  LEU A CA  
2302  C C   . LEU A 327  ? 0.2065 0.2151 0.2570 0.0183  0.0168  0.0241  325  LEU A C   
2303  O O   . LEU A 327  ? 0.2157 0.2272 0.2688 0.0198  0.0167  0.0237  325  LEU A O   
2304  C CB  . LEU A 327  ? 0.2233 0.2375 0.2718 0.0201  0.0203  0.0246  325  LEU A CB  
2305  C CG  . LEU A 327  ? 0.2555 0.2734 0.3039 0.0196  0.0223  0.0268  325  LEU A CG  
2306  C CD1 . LEU A 327  ? 0.2847 0.3068 0.3311 0.0223  0.0237  0.0256  325  LEU A CD1 
2307  C CD2 . LEU A 327  ? 0.2793 0.3013 0.3318 0.0183  0.0232  0.0295  325  LEU A CD2 
2308  N N   . ASP A 328  ? 0.1966 0.2004 0.2452 0.0171  0.0151  0.0235  326  ASP A N   
2309  C CA  . ASP A 328  ? 0.1939 0.1958 0.2432 0.0177  0.0131  0.0227  326  ASP A CA  
2310  C C   . ASP A 328  ? 0.2051 0.2082 0.2571 0.0161  0.0121  0.0239  326  ASP A C   
2311  O O   . ASP A 328  ? 0.2075 0.2095 0.2590 0.0138  0.0116  0.0246  326  ASP A O   
2312  C CB  . ASP A 328  ? 0.1980 0.1952 0.2441 0.0170  0.0118  0.0220  326  ASP A CB  
2313  C CG  . ASP A 328  ? 0.2524 0.2477 0.2996 0.0177  0.0096  0.0216  326  ASP A CG  
2314  O OD1 . ASP A 328  ? 0.2459 0.2427 0.2959 0.0175  0.0086  0.0224  326  ASP A OD1 
2315  O OD2 . ASP A 328  ? 0.2932 0.2855 0.3387 0.0184  0.0088  0.0206  326  ASP A OD2 
2316  N N   . GLY A 329  ? 0.2079 0.2138 0.2632 0.0174  0.0117  0.0240  327  GLY A N   
2317  C CA  . GLY A 329  ? 0.1997 0.2074 0.2579 0.0161  0.0108  0.0252  327  GLY A CA  
2318  C C   . GLY A 329  ? 0.2152 0.2203 0.2725 0.0144  0.0086  0.0255  327  GLY A C   
2319  O O   . GLY A 329  ? 0.1980 0.2047 0.2569 0.0126  0.0079  0.0263  327  GLY A O   
2320  N N   . ASP A 330  ? 0.1917 0.1934 0.2466 0.0148  0.0074  0.0250  328  ASP A N   
2321  C CA  . ASP A 330  ? 0.2141 0.2143 0.2680 0.0131  0.0054  0.0257  328  ASP A CA  
2322  C C   . ASP A 330  ? 0.1767 0.1766 0.2285 0.0106  0.0057  0.0257  328  ASP A C   
2323  O O   . ASP A 330  ? 0.2058 0.2063 0.2574 0.0090  0.0042  0.0262  328  ASP A O   
2324  C CB  . ASP A 330  ? 0.2249 0.2215 0.2768 0.0137  0.0042  0.0255  328  ASP A CB  
2325  C CG  . ASP A 330  ? 0.3028 0.2991 0.3577 0.0160  0.0030  0.0255  328  ASP A CG  
2326  O OD1 . ASP A 330  ? 0.3125 0.3116 0.3708 0.0167  0.0027  0.0260  328  ASP A OD1 
2327  O OD2 . ASP A 330  ? 0.2519 0.2453 0.3061 0.0171  0.0024  0.0248  328  ASP A OD2 
2328  N N   . LEU A 331  ? 0.1788 0.1783 0.2296 0.0104  0.0075  0.0251  329  LEU A N   
2329  C CA  . LEU A 331  ? 0.2076 0.2067 0.2572 0.0083  0.0077  0.0248  329  LEU A CA  
2330  C C   . LEU A 331  ? 0.1986 0.2005 0.2516 0.0073  0.0084  0.0251  329  LEU A C   
2331  O O   . LEU A 331  ? 0.2012 0.2029 0.2544 0.0056  0.0085  0.0247  329  LEU A O   
2332  C CB  . LEU A 331  ? 0.2005 0.1971 0.2473 0.0086  0.0090  0.0241  329  LEU A CB  
2333  C CG  . LEU A 331  ? 0.1915 0.1850 0.2348 0.0089  0.0082  0.0236  329  LEU A CG  
2334  C CD1 . LEU A 331  ? 0.2140 0.2053 0.2547 0.0095  0.0096  0.0229  329  LEU A CD1 
2335  C CD2 . LEU A 331  ? 0.2113 0.2045 0.2533 0.0069  0.0067  0.0235  329  LEU A CD2 
2336  N N   . SER A 332  ? 0.2055 0.2103 0.2617 0.0082  0.0087  0.0259  330  SER A N   
2337  C CA  . SER A 332  ? 0.2223 0.2299 0.2822 0.0072  0.0094  0.0265  330  SER A CA  
2338  C C   . SER A 332  ? 0.1920 0.2006 0.2535 0.0051  0.0077  0.0260  330  SER A C   
2339  O O   . SER A 332  ? 0.2307 0.2393 0.2908 0.0047  0.0060  0.0256  330  SER A O   
2340  C CB  . SER A 332  ? 0.2167 0.2278 0.2799 0.0087  0.0100  0.0274  330  SER A CB  
2341  O OG  . SER A 332  ? 0.2613 0.2733 0.3255 0.0091  0.0083  0.0275  330  SER A OG  
2342  N N   . GLY A 333  ? 0.1822 0.1922 0.2468 0.0036  0.0081  0.0260  331  GLY A N   
2343  C CA  . GLY A 333  ? 0.2082 0.2194 0.2747 0.0016  0.0065  0.0249  331  GLY A CA  
2344  C C   . GLY A 333  ? 0.1942 0.2032 0.2588 0.0003  0.0060  0.0232  331  GLY A C   
2345  O O   . GLY A 333  ? 0.2308 0.2411 0.2973 -0.0013 0.0047  0.0216  331  GLY A O   
2346  N N   . TRP A 334  ? 0.1909 0.1967 0.2519 0.0010  0.0069  0.0231  332  TRP A N   
2347  C CA  . TRP A 334  ? 0.2026 0.2063 0.2614 0.0000  0.0065  0.0214  332  TRP A CA  
2348  C C   . TRP A 334  ? 0.1849 0.1864 0.2445 0.0001  0.0081  0.0220  332  TRP A C   
2349  O O   . TRP A 334  ? 0.2061 0.2068 0.2642 0.0015  0.0096  0.0235  332  TRP A O   
2350  C CB  . TRP A 334  ? 0.2013 0.2034 0.2551 0.0007  0.0060  0.0212  332  TRP A CB  
2351  C CG  . TRP A 334  ? 0.1854 0.1853 0.2363 0.0001  0.0059  0.0197  332  TRP A CG  
2352  C CD1 . TRP A 334  ? 0.1830 0.1839 0.2341 -0.0013 0.0047  0.0175  332  TRP A CD1 
2353  C CD2 . TRP A 334  ? 0.1889 0.1858 0.2363 0.0011  0.0069  0.0200  332  TRP A CD2 
2354  N NE1 . TRP A 334  ? 0.1849 0.1835 0.2328 -0.0013 0.0051  0.0166  332  TRP A NE1 
2355  C CE2 . TRP A 334  ? 0.1754 0.1714 0.2210 0.0001  0.0063  0.0182  332  TRP A CE2 
2356  C CE3 . TRP A 334  ? 0.2041 0.1993 0.2499 0.0028  0.0081  0.0213  332  TRP A CE3 
2357  C CZ2 . TRP A 334  ? 0.1749 0.1680 0.2170 0.0006  0.0070  0.0181  332  TRP A CZ2 
2358  C CZ3 . TRP A 334  ? 0.2031 0.1955 0.2455 0.0033  0.0087  0.0210  332  TRP A CZ3 
2359  C CH2 . TRP A 334  ? 0.2041 0.1955 0.2447 0.0022  0.0082  0.0195  332  TRP A CH2 
2360  N N   . ASN A 335  ? 0.1880 0.1890 0.2501 -0.0014 0.0076  0.0208  333  ASN A N   
2361  C CA  . ASN A 335  ? 0.1822 0.1813 0.2459 -0.0015 0.0088  0.0216  333  ASN A CA  
2362  C C   . ASN A 335  ? 0.1891 0.1853 0.2497 -0.0017 0.0085  0.0199  333  ASN A C   
2363  O O   . ASN A 335  ? 0.1952 0.1897 0.2578 -0.0022 0.0090  0.0200  333  ASN A O   
2364  C CB  . ASN A 335  ? 0.2169 0.2171 0.2871 -0.0031 0.0084  0.0218  333  ASN A CB  
2365  C CG  . ASN A 335  ? 0.2128 0.2157 0.2865 -0.0028 0.0094  0.0245  333  ASN A CG  
2366  O OD1 . ASN A 335  ? 0.2063 0.2100 0.2777 -0.0013 0.0109  0.0265  333  ASN A OD1 
2367  N ND2 . ASN A 335  ? 0.2957 0.3004 0.3753 -0.0043 0.0084  0.0244  333  ASN A ND2 
2368  N N   . GLY A 336  ? 0.1837 0.1796 0.2398 -0.0014 0.0078  0.0185  334  GLY A N   
2369  C CA  . GLY A 336  ? 0.1748 0.1687 0.2280 -0.0016 0.0075  0.0167  334  GLY A CA  
2370  C C   . GLY A 336  ? 0.1671 0.1583 0.2166 -0.0004 0.0088  0.0178  334  GLY A C   
2371  O O   . GLY A 336  ? 0.1875 0.1771 0.2350 -0.0006 0.0086  0.0164  334  GLY A O   
2372  N N   . MET A 337  ? 0.1781 0.1692 0.2268 0.0009  0.0101  0.0200  335  MET A N   
2373  C CA  A MET A 337  ? 0.1950 0.1840 0.2403 0.0021  0.0113  0.0207  335  MET A CA  
2374  C CA  B MET A 337  ? 0.1950 0.1840 0.2403 0.0021  0.0113  0.0207  335  MET A CA  
2375  C C   . MET A 337  ? 0.1745 0.1622 0.2217 0.0017  0.0120  0.0211  335  MET A C   
2376  O O   . MET A 337  ? 0.1928 0.1816 0.2443 0.0012  0.0125  0.0226  335  MET A O   
2377  C CB  A MET A 337  ? 0.2006 0.1906 0.2452 0.0038  0.0125  0.0225  335  MET A CB  
2378  C CB  B MET A 337  ? 0.2001 0.1900 0.2444 0.0038  0.0124  0.0224  335  MET A CB  
2379  C CG  A MET A 337  ? 0.2369 0.2252 0.2776 0.0053  0.0135  0.0227  335  MET A CG  
2380  C CG  B MET A 337  ? 0.2406 0.2289 0.2818 0.0051  0.0137  0.0229  335  MET A CG  
2381  S SD  A MET A 337  ? 0.3032 0.2894 0.3396 0.0055  0.0122  0.0211  335  MET A SD  
2382  S SD  B MET A 337  ? 0.2608 0.2492 0.2989 0.0072  0.0137  0.0227  335  MET A SD  
2383  C CE  A MET A 337  ? 0.2743 0.2619 0.3110 0.0068  0.0117  0.0217  335  MET A CE  
2384  C CE  B MET A 337  ? 0.2204 0.2069 0.2561 0.0062  0.0118  0.0212  335  MET A CE  
2385  N N   . GLY A 338  ? 0.1817 0.1672 0.2260 0.0018  0.0120  0.0201  336  GLY A N   
2386  C CA  . GLY A 338  ? 0.2067 0.1907 0.2528 0.0015  0.0124  0.0205  336  GLY A CA  
2387  C C   . GLY A 338  ? 0.2009 0.1835 0.2432 0.0028  0.0136  0.0214  336  GLY A C   
2388  O O   . GLY A 338  ? 0.1920 0.1742 0.2300 0.0037  0.0137  0.0209  336  GLY A O   
2389  N N   . PHE A 339  ? 0.1760 0.1581 0.2202 0.0028  0.0143  0.0229  337  PHE A N   
2390  C CA  . PHE A 339  ? 0.1852 0.1668 0.2261 0.0041  0.0154  0.0241  337  PHE A CA  
2391  C C   . PHE A 339  ? 0.1920 0.1724 0.2354 0.0035  0.0155  0.0249  337  PHE A C   
2392  O O   . PHE A 339  ? 0.1895 0.1704 0.2380 0.0026  0.0154  0.0266  337  PHE A O   
2393  C CB  . PHE A 339  ? 0.1911 0.1756 0.2320 0.0052  0.0169  0.0265  337  PHE A CB  
2394  C CG  . PHE A 339  ? 0.1858 0.1707 0.2228 0.0069  0.0180  0.0271  337  PHE A CG  
2395  C CD1 . PHE A 339  ? 0.1950 0.1793 0.2276 0.0081  0.0179  0.0254  337  PHE A CD1 
2396  C CD2 . PHE A 339  ? 0.1900 0.1762 0.2279 0.0071  0.0190  0.0295  337  PHE A CD2 
2397  C CE1 . PHE A 339  ? 0.1927 0.1778 0.2221 0.0097  0.0188  0.0255  337  PHE A CE1 
2398  C CE2 . PHE A 339  ? 0.2123 0.1997 0.2465 0.0087  0.0200  0.0299  337  PHE A CE2 
2399  C CZ  . PHE A 339  ? 0.2090 0.1958 0.2389 0.0101  0.0199  0.0276  337  PHE A CZ  
2400  N N   . VAL A 340  ? 0.1867 0.1652 0.2268 0.0041  0.0155  0.0240  338  VAL A N   
2401  C CA  . VAL A 340  ? 0.1885 0.1656 0.2307 0.0037  0.0153  0.0247  338  VAL A CA  
2402  C C   . VAL A 340  ? 0.1841 0.1629 0.2256 0.0048  0.0168  0.0280  338  VAL A C   
2403  O O   . VAL A 340  ? 0.1871 0.1673 0.2244 0.0061  0.0177  0.0283  338  VAL A O   
2404  C CB  . VAL A 340  ? 0.1784 0.1533 0.2173 0.0039  0.0146  0.0220  338  VAL A CB  
2405  C CG1 . VAL A 340  ? 0.1907 0.1642 0.2319 0.0038  0.0145  0.0228  338  VAL A CG1 
2406  C CG2 . VAL A 340  ? 0.1843 0.1588 0.2236 0.0029  0.0133  0.0188  338  VAL A CG2 
2407  N N   . VAL A 341  ? 0.1693 0.1483 0.2155 0.0041  0.0168  0.0305  339  VAL A N   
2408  C CA  A VAL A 341  ? 0.1932 0.1742 0.2390 0.0049  0.0180  0.0340  339  VAL A CA  
2409  C CA  B VAL A 341  ? 0.1932 0.1742 0.2390 0.0049  0.0180  0.0340  339  VAL A CA  
2410  C C   . VAL A 341  ? 0.1826 0.1613 0.2306 0.0045  0.0172  0.0343  339  VAL A C   
2411  O O   . VAL A 341  ? 0.1972 0.1735 0.2502 0.0033  0.0158  0.0334  339  VAL A O   
2412  C CB  A VAL A 341  ? 0.1910 0.1758 0.2409 0.0046  0.0189  0.0381  339  VAL A CB  
2413  C CB  B VAL A 341  ? 0.1909 0.1756 0.2408 0.0046  0.0189  0.0381  339  VAL A CB  
2414  C CG1 A VAL A 341  ? 0.2046 0.1922 0.2520 0.0053  0.0198  0.0375  339  VAL A CG1 
2415  C CG1 B VAL A 341  ? 0.2025 0.1909 0.2499 0.0059  0.0204  0.0412  339  VAL A CG1 
2416  C CG2 A VAL A 341  ? 0.2177 0.2012 0.2751 0.0028  0.0177  0.0391  339  VAL A CG2 
2417  C CG2 B VAL A 341  ? 0.2085 0.1951 0.2582 0.0046  0.0192  0.0372  339  VAL A CG2 
2418  N N   . GLN A 342  ? 0.1852 0.1646 0.2297 0.0057  0.0179  0.0353  340  GLN A N   
2419  C CA  . GLN A 342  ? 0.1957 0.1728 0.2413 0.0056  0.0171  0.0354  340  GLN A CA  
2420  C C   . GLN A 342  ? 0.1798 0.1591 0.2296 0.0054  0.0175  0.0404  340  GLN A C   
2421  O O   . GLN A 342  ? 0.2110 0.1941 0.2580 0.0064  0.0189  0.0432  340  GLN A O   
2422  C CB  . GLN A 342  ? 0.1994 0.1760 0.2385 0.0069  0.0174  0.0333  340  GLN A CB  
2423  C CG  . GLN A 342  ? 0.1799 0.1546 0.2152 0.0069  0.0169  0.0289  340  GLN A CG  
2424  C CD  . GLN A 342  ? 0.1876 0.1631 0.2166 0.0083  0.0176  0.0278  340  GLN A CD  
2425  O OE1 . GLN A 342  ? 0.2058 0.1842 0.2328 0.0094  0.0187  0.0294  340  GLN A OE1 
2426  N NE2 . GLN A 342  ? 0.1861 0.1594 0.2123 0.0083  0.0168  0.0248  340  GLN A NE2 
2427  N N   . ALA A 343  ? 0.1764 0.1537 0.2332 0.0042  0.0162  0.0415  341  ALA A N   
2428  C CA  . ALA A 343  ? 0.1997 0.1788 0.2619 0.0037  0.0163  0.0469  341  ALA A CA  
2429  C C   . ALA A 343  ? 0.2080 0.1878 0.2679 0.0047  0.0165  0.0487  341  ALA A C   
2430  O O   . ALA A 343  ? 0.2047 0.1874 0.2676 0.0045  0.0169  0.0539  341  ALA A O   
2431  C CB  . ALA A 343  ? 0.2401 0.2162 0.3112 0.0020  0.0145  0.0472  341  ALA A CB  
2432  N N   . TYR A 344  ? 0.1974 0.1747 0.2524 0.0056  0.0162  0.0449  342  TYR A N   
2433  C CA  . TYR A 344  ? 0.2000 0.1787 0.2523 0.0067  0.0165  0.0467  342  TYR A CA  
2434  C C   . TYR A 344  ? 0.2105 0.1943 0.2569 0.0080  0.0184  0.0486  342  TYR A C   
2435  O O   . TYR A 344  ? 0.2249 0.2110 0.2690 0.0089  0.0188  0.0506  342  TYR A O   
2436  C CB  . TYR A 344  ? 0.1978 0.1729 0.2474 0.0072  0.0156  0.0424  342  TYR A CB  
2437  C CG  . TYR A 344  ? 0.1996 0.1741 0.2418 0.0081  0.0161  0.0379  342  TYR A CG  
2438  C CD1 . TYR A 344  ? 0.2022 0.1787 0.2404 0.0084  0.0172  0.0370  342  TYR A CD1 
2439  C CD2 . TYR A 344  ? 0.1983 0.1703 0.2382 0.0085  0.0153  0.0346  342  TYR A CD2 
2440  C CE1 . TYR A 344  ? 0.2066 0.1822 0.2391 0.0091  0.0173  0.0331  342  TYR A CE1 
2441  C CE2 . TYR A 344  ? 0.2058 0.1773 0.2399 0.0090  0.0156  0.0309  342  TYR A CE2 
2442  C CZ  . TYR A 344  ? 0.1890 0.1621 0.2195 0.0093  0.0165  0.0303  342  TYR A CZ  
2443  O OH  . TYR A 344  ? 0.2022 0.1744 0.2275 0.0097  0.0165  0.0269  342  TYR A OH  
2444  N N   . GLY A 345  ? 0.1948 0.1809 0.2390 0.0081  0.0194  0.0479  343  GLY A N   
2445  C CA  . GLY A 345  ? 0.2130 0.2042 0.2518 0.0096  0.0210  0.0488  343  GLY A CA  
2446  C C   . GLY A 345  ? 0.2143 0.2113 0.2562 0.0093  0.0221  0.0544  343  GLY A C   
2447  O O   . GLY A 345  ? 0.2044 0.2013 0.2519 0.0079  0.0219  0.0564  343  GLY A O   
2448  N N   . LYS A 346  ? 0.1964 0.1990 0.2347 0.0107  0.0233  0.0566  344  LYS A N   
2449  C CA  . LYS A 346  ? 0.2056 0.2151 0.2465 0.0105  0.0245  0.0624  344  LYS A CA  
2450  C C   . LYS A 346  ? 0.2229 0.2360 0.2638 0.0106  0.0256  0.0623  344  LYS A C   
2451  O O   . LYS A 346  ? 0.2102 0.2285 0.2549 0.0099  0.0264  0.0672  344  LYS A O   
2452  C CB  . LYS A 346  ? 0.2022 0.2176 0.2382 0.0122  0.0255  0.0639  344  LYS A CB  
2453  C CG  . LYS A 346  ? 0.2336 0.2463 0.2701 0.0122  0.0243  0.0649  344  LYS A CG  
2454  C CD  . LYS A 346  ? 0.2348 0.2538 0.2662 0.0140  0.0252  0.0659  344  LYS A CD  
2455  C CE  . LYS A 346  ? 0.2291 0.2462 0.2622 0.0137  0.0240  0.0682  344  LYS A CE  
2456  N NZ  . LYS A 346  ? 0.2549 0.2776 0.2822 0.0156  0.0247  0.0681  344  LYS A NZ  
2457  N N   . ARG A 347  ? 0.1922 0.2031 0.2292 0.0114  0.0257  0.0571  345  ARG A N   
2458  C CA  . ARG A 347  ? 0.2021 0.2160 0.2391 0.0116  0.0267  0.0566  345  ARG A CA  
2459  C C   . ARG A 347  ? 0.2172 0.2271 0.2598 0.0097  0.0258  0.0565  345  ARG A C   
2460  O O   . ARG A 347  ? 0.1980 0.2109 0.2419 0.0096  0.0266  0.0569  345  ARG A O   
2461  C CB  . ARG A 347  ? 0.2042 0.2177 0.2350 0.0135  0.0270  0.0512  345  ARG A CB  
2462  C CG  . ARG A 347  ? 0.2032 0.2223 0.2289 0.0156  0.0280  0.0509  345  ARG A CG  
2463  C CD  . ARG A 347  ? 0.1946 0.2115 0.2151 0.0172  0.0277  0.0452  345  ARG A CD  
2464  N NE  . ARG A 347  ? 0.2026 0.2124 0.2219 0.0167  0.0262  0.0423  345  ARG A NE  
2465  C CZ  . ARG A 347  ? 0.1957 0.2019 0.2114 0.0175  0.0255  0.0376  345  ARG A CZ  
2466  N NH1 . ARG A 347  ? 0.2096 0.2181 0.2230 0.0190  0.0259  0.0349  345  ARG A NH1 
2467  N NH2 . ARG A 347  ? 0.1858 0.1862 0.2008 0.0168  0.0242  0.0356  345  ARG A NH2 
2468  N N   . CYS A 348  ? 0.1957 0.1996 0.2420 0.0082  0.0242  0.0559  346  CYS A N   
2469  C CA  . CYS A 348  ? 0.2174 0.2172 0.2686 0.0066  0.0230  0.0546  346  CYS A CA  
2470  C C   . CYS A 348  ? 0.2041 0.2076 0.2604 0.0055  0.0236  0.0582  346  CYS A C   
2471  O O   . CYS A 348  ? 0.1993 0.2024 0.2557 0.0053  0.0236  0.0559  346  CYS A O   
2472  C CB  . CYS A 348  ? 0.2145 0.2086 0.2701 0.0053  0.0212  0.0542  346  CYS A CB  
2473  S SG  . CYS A 348  ? 0.2543 0.2430 0.3139 0.0037  0.0195  0.0501  346  CYS A SG  
2474  N N   . PRO A 349  ? 0.2035 0.2109 0.2646 0.0046  0.0240  0.0639  347  PRO A N   
2475  C CA  . PRO A 349  ? 0.2077 0.2189 0.2743 0.0034  0.0245  0.0674  347  PRO A CA  
2476  C C   . PRO A 349  ? 0.1931 0.2102 0.2554 0.0048  0.0264  0.0668  347  PRO A C   
2477  O O   . PRO A 349  ? 0.2113 0.2297 0.2766 0.0040  0.0265  0.0669  347  PRO A O   
2478  C CB  . PRO A 349  ? 0.2213 0.2361 0.2933 0.0023  0.0246  0.0743  347  PRO A CB  
2479  C CG  . PRO A 349  ? 0.2451 0.2608 0.3121 0.0037  0.0250  0.0746  347  PRO A CG  
2480  C CD  . PRO A 349  ? 0.2252 0.2347 0.2868 0.0048  0.0241  0.0680  347  PRO A CD  
2481  N N   . PHE A 350  ? 0.2092 0.2302 0.2648 0.0069  0.0277  0.0658  348  PHE A N   
2482  C CA  . PHE A 350  ? 0.2128 0.2396 0.2645 0.0086  0.0293  0.0645  348  PHE A CA  
2483  C C   . PHE A 350  ? 0.2167 0.2388 0.2654 0.0093  0.0286  0.0585  348  PHE A C   
2484  O O   . PHE A 350  ? 0.2050 0.2301 0.2538 0.0099  0.0293  0.0576  348  PHE A O   
2485  C CB  . PHE A 350  ? 0.2151 0.2477 0.2611 0.0108  0.0306  0.0648  348  PHE A CB  
2486  C CG  . PHE A 350  ? 0.2400 0.2772 0.2887 0.0100  0.0310  0.0710  348  PHE A CG  
2487  C CD1 . PHE A 350  ? 0.2297 0.2750 0.2820 0.0094  0.0323  0.0765  348  PHE A CD1 
2488  C CD2 . PHE A 350  ? 0.2460 0.2796 0.2942 0.0098  0.0300  0.0716  348  PHE A CD2 
2489  C CE1 . PHE A 350  ? 0.2774 0.3273 0.3328 0.0086  0.0326  0.0829  348  PHE A CE1 
2490  C CE2 . PHE A 350  ? 0.2571 0.2948 0.3083 0.0091  0.0302  0.0777  348  PHE A CE2 
2491  C CZ  . PHE A 350  ? 0.2785 0.3244 0.3333 0.0084  0.0315  0.0835  348  PHE A CZ  
2492  N N   . VAL A 351  ? 0.1927 0.2079 0.2392 0.0093  0.0272  0.0547  349  VAL A N   
2493  C CA  . VAL A 351  ? 0.1767 0.1873 0.2213 0.0095  0.0263  0.0497  349  VAL A CA  
2494  C C   . VAL A 351  ? 0.2080 0.2169 0.2582 0.0076  0.0256  0.0503  349  VAL A C   
2495  O O   . VAL A 351  ? 0.2061 0.2156 0.2559 0.0080  0.0256  0.0483  349  VAL A O   
2496  C CB  . VAL A 351  ? 0.1836 0.1878 0.2253 0.0095  0.0250  0.0462  349  VAL A CB  
2497  C CG1 . VAL A 351  ? 0.1947 0.1946 0.2350 0.0094  0.0239  0.0418  349  VAL A CG1 
2498  C CG2 . VAL A 351  ? 0.2147 0.2207 0.2507 0.0114  0.0257  0.0453  349  VAL A CG2 
2499  N N   . LEU A 352  ? 0.2053 0.2124 0.2613 0.0057  0.0247  0.0531  350  LEU A N   
2500  C CA  . LEU A 352  ? 0.1986 0.2045 0.2608 0.0038  0.0238  0.0537  350  LEU A CA  
2501  C C   . LEU A 352  ? 0.1974 0.2096 0.2617 0.0039  0.0252  0.0566  350  LEU A C   
2502  O O   . LEU A 352  ? 0.2146 0.2266 0.2809 0.0034  0.0248  0.0551  350  LEU A O   
2503  C CB  . LEU A 352  ? 0.1888 0.1917 0.2575 0.0019  0.0225  0.0562  350  LEU A CB  
2504  C CG  . LEU A 352  ? 0.2040 0.2005 0.2716 0.0017  0.0208  0.0524  350  LEU A CG  
2505  C CD1 . LEU A 352  ? 0.2449 0.2391 0.3197 0.0000  0.0195  0.0551  350  LEU A CD1 
2506  C CD2 . LEU A 352  ? 0.2384 0.2314 0.3053 0.0013  0.0196  0.0475  350  LEU A CD2 
2507  N N   . ASP A 353  ? 0.2062 0.2248 0.2703 0.0045  0.0268  0.0608  351  ASP A N   
2508  C CA  . ASP A 353  ? 0.2126 0.2384 0.2783 0.0048  0.0283  0.0634  351  ASP A CA  
2509  C C   . ASP A 353  ? 0.2069 0.2336 0.2678 0.0067  0.0288  0.0589  351  ASP A C   
2510  O O   . ASP A 353  ? 0.1974 0.2264 0.2608 0.0065  0.0291  0.0588  351  ASP A O   
2511  C CB  . ASP A 353  ? 0.2160 0.2497 0.2809 0.0056  0.0301  0.0681  351  ASP A CB  
2512  C CG  . ASP A 353  ? 0.2431 0.2774 0.3142 0.0035  0.0297  0.0740  351  ASP A CG  
2513  O OD1 . ASP A 353  ? 0.2693 0.2993 0.3470 0.0013  0.0281  0.0750  351  ASP A OD1 
2514  O OD2 . ASP A 353  ? 0.2892 0.3284 0.3589 0.0042  0.0307  0.0776  351  ASP A OD2 
2515  N N   . PHE A 354  ? 0.2078 0.2329 0.2623 0.0087  0.0289  0.0552  352  PHE A N   
2516  C CA  . PHE A 354  ? 0.1913 0.2165 0.2417 0.0106  0.0291  0.0509  352  PHE A CA  
2517  C C   . PHE A 354  ? 0.1922 0.2118 0.2445 0.0094  0.0275  0.0480  352  PHE A C   
2518  O O   . PHE A 354  ? 0.1979 0.2194 0.2510 0.0099  0.0276  0.0469  352  PHE A O   
2519  C CB  . PHE A 354  ? 0.2018 0.2253 0.2459 0.0126  0.0291  0.0475  352  PHE A CB  
2520  C CG  . PHE A 354  ? 0.2010 0.2227 0.2419 0.0142  0.0286  0.0428  352  PHE A CG  
2521  C CD1 . PHE A 354  ? 0.2177 0.2451 0.2570 0.0164  0.0297  0.0417  352  PHE A CD1 
2522  C CD2 . PHE A 354  ? 0.2289 0.2434 0.2687 0.0135  0.0268  0.0396  352  PHE A CD2 
2523  C CE1 . PHE A 354  ? 0.2337 0.2590 0.2710 0.0178  0.0289  0.0375  352  PHE A CE1 
2524  C CE2 . PHE A 354  ? 0.2369 0.2497 0.2744 0.0148  0.0262  0.0359  352  PHE A CE2 
2525  C CZ  . PHE A 354  ? 0.2423 0.2601 0.2788 0.0170  0.0271  0.0349  352  PHE A CZ  
2526  N N   . ILE A 355  ? 0.1802 0.1934 0.2335 0.0079  0.0259  0.0468  353  ILE A N   
2527  C CA  . ILE A 355  ? 0.1838 0.1924 0.2383 0.0069  0.0243  0.0439  353  ILE A CA  
2528  C C   . ILE A 355  ? 0.2063 0.2169 0.2670 0.0053  0.0241  0.0459  353  ILE A C   
2529  O O   . ILE A 355  ? 0.2011 0.2115 0.2624 0.0053  0.0235  0.0439  353  ILE A O   
2530  C CB  . ILE A 355  ? 0.2152 0.2176 0.2695 0.0058  0.0227  0.0420  353  ILE A CB  
2531  C CG1 . ILE A 355  ? 0.2178 0.2180 0.2658 0.0073  0.0227  0.0394  353  ILE A CG1 
2532  C CG2 . ILE A 355  ? 0.2157 0.2148 0.2724 0.0044  0.0210  0.0395  353  ILE A CG2 
2533  C CD1 . ILE A 355  ? 0.2195 0.2147 0.2671 0.0064  0.0215  0.0380  353  ILE A CD1 
2534  N N   . ILE A 356  ? 0.1963 0.2088 0.2622 0.0038  0.0243  0.0500  354  ILE A N   
2535  C CA  . ILE A 356  ? 0.1887 0.2033 0.2612 0.0021  0.0240  0.0522  354  ILE A CA  
2536  C C   . ILE A 356  ? 0.2013 0.2219 0.2732 0.0034  0.0255  0.0529  354  ILE A C   
2537  O O   . ILE A 356  ? 0.2014 0.2225 0.2759 0.0028  0.0249  0.0519  354  ILE A O   
2538  C CB  . ILE A 356  ? 0.1968 0.2124 0.2755 0.0003  0.0240  0.0570  354  ILE A CB  
2539  C CG1 . ILE A 356  ? 0.2162 0.2251 0.2969 -0.0010 0.0220  0.0553  354  ILE A CG1 
2540  C CG2 . ILE A 356  ? 0.2564 0.2757 0.3422 -0.0014 0.0240  0.0601  354  ILE A CG2 
2541  C CD1 . ILE A 356  ? 0.2404 0.2496 0.3261 -0.0023 0.0219  0.0599  354  ILE A CD1 
2542  N N   . ASP A 357  ? 0.1947 0.2203 0.2628 0.0053  0.0273  0.0542  355  ASP A N   
2543  C CA  . ASP A 357  ? 0.2103 0.2422 0.2777 0.0068  0.0287  0.0542  355  ASP A CA  
2544  C C   . ASP A 357  ? 0.1920 0.2211 0.2560 0.0083  0.0279  0.0493  355  ASP A C   
2545  O O   . ASP A 357  ? 0.2022 0.2339 0.2681 0.0086  0.0280  0.0488  355  ASP A O   
2546  C CB  . ASP A 357  ? 0.2350 0.2736 0.2992 0.0087  0.0307  0.0561  355  ASP A CB  
2547  C CG  . ASP A 357  ? 0.2336 0.2790 0.2966 0.0108  0.0321  0.0552  355  ASP A CG  
2548  O OD1 . ASP A 357  ? 0.2737 0.3249 0.3412 0.0101  0.0331  0.0585  355  ASP A OD1 
2549  O OD2 . ASP A 357  ? 0.2231 0.2677 0.2812 0.0132  0.0321  0.0511  355  ASP A OD2 
2550  N N   . LEU A 358  ? 0.1829 0.2067 0.2421 0.0092  0.0270  0.0458  356  LEU A N   
2551  C CA  . LEU A 358  ? 0.1689 0.1897 0.2254 0.0102  0.0259  0.0417  356  LEU A CA  
2552  C C   . LEU A 358  ? 0.2000 0.2179 0.2603 0.0083  0.0244  0.0411  356  LEU A C   
2553  O O   . LEU A 358  ? 0.2025 0.2213 0.2632 0.0090  0.0239  0.0395  356  LEU A O   
2554  C CB  . LEU A 358  ? 0.1806 0.1961 0.2320 0.0110  0.0251  0.0388  356  LEU A CB  
2555  C CG  . LEU A 358  ? 0.1852 0.1970 0.2342 0.0117  0.0237  0.0350  356  LEU A CG  
2556  C CD1 . LEU A 358  ? 0.2200 0.2357 0.2682 0.0140  0.0243  0.0338  356  LEU A CD1 
2557  C CD2 . LEU A 358  ? 0.1978 0.2049 0.2423 0.0121  0.0229  0.0329  356  LEU A CD2 
2558  N N   . ALA A 359  ? 0.1897 0.2045 0.2532 0.0061  0.0234  0.0422  357  ALA A N   
2559  C CA  . ALA A 359  ? 0.2039 0.2168 0.2715 0.0043  0.0218  0.0413  357  ALA A CA  
2560  C C   . ALA A 359  ? 0.2026 0.2207 0.2748 0.0039  0.0225  0.0435  357  ALA A C   
2561  O O   . ALA A 359  ? 0.2127 0.2308 0.2863 0.0037  0.0215  0.0419  357  ALA A O   
2562  C CB  . ALA A 359  ? 0.2120 0.2215 0.2833 0.0020  0.0207  0.0421  357  ALA A CB  
2563  N N   . ARG A 360  ? 0.1893 0.2124 0.2641 0.0039  0.0241  0.0473  358  ARG A N   
2564  C CA  . ARG A 360  ? 0.2061 0.2350 0.2853 0.0036  0.0249  0.0497  358  ARG A CA  
2565  C C   . ARG A 360  ? 0.2398 0.2719 0.3160 0.0060  0.0256  0.0476  358  ARG A C   
2566  O O   . ARG A 360  ? 0.2579 0.2915 0.3369 0.0057  0.0251  0.0470  358  ARG A O   
2567  C CB  . ARG A 360  ? 0.2275 0.2619 0.3096 0.0031  0.0267  0.0546  358  ARG A CB  
2568  C CG  . ARG A 360  ? 0.2451 0.2769 0.3326 0.0004  0.0257  0.0575  358  ARG A CG  
2569  C CD  . ARG A 360  ? 0.2869 0.3252 0.3786 -0.0004 0.0273  0.0634  358  ARG A CD  
2570  N NE  . ARG A 360  ? 0.3674 0.4026 0.4632 -0.0024 0.0264  0.0662  358  ARG A NE  
2571  C CZ  . ARG A 360  ? 0.4552 0.4875 0.5583 -0.0050 0.0247  0.0673  358  ARG A CZ  
2572  N NH1 . ARG A 360  ? 0.4401 0.4728 0.5472 -0.0060 0.0238  0.0662  358  ARG A NH1 
2573  N NH2 . ARG A 360  ? 0.3814 0.4104 0.4882 -0.0065 0.0237  0.0695  358  ARG A NH2 
2574  N N   . ARG A 361  ? 0.2113 0.2445 0.2822 0.0084  0.0267  0.0462  359  ARG A N   
2575  C CA  . ARG A 361  ? 0.2089 0.2452 0.2775 0.0109  0.0272  0.0439  359  ARG A CA  
2576  C C   . ARG A 361  ? 0.2195 0.2510 0.2872 0.0111  0.0252  0.0405  359  ARG A C   
2577  O O   . ARG A 361  ? 0.2424 0.2763 0.3116 0.0120  0.0250  0.0395  359  ARG A O   
2578  C CB  . ARG A 361  ? 0.2640 0.3015 0.3272 0.0134  0.0283  0.0425  359  ARG A CB  
2579  C CG  . ARG A 361  ? 0.2664 0.3109 0.3299 0.0140  0.0304  0.0457  359  ARG A CG  
2580  C CD  . ARG A 361  ? 0.2652 0.3114 0.3233 0.0168  0.0312  0.0432  359  ARG A CD  
2581  N NE  . ARG A 361  ? 0.2686 0.3091 0.3230 0.0165  0.0305  0.0422  359  ARG A NE  
2582  C CZ  . ARG A 361  ? 0.2506 0.2865 0.3007 0.0180  0.0295  0.0383  359  ARG A CZ  
2583  N NH1 . ARG A 361  ? 0.2527 0.2880 0.3021 0.0197  0.0288  0.0350  359  ARG A NH1 
2584  N NH2 . ARG A 361  ? 0.2461 0.2782 0.2930 0.0177  0.0291  0.0379  359  ARG A NH2 
2585  N N   . SER A 362  ? 0.2080 0.2330 0.2732 0.0102  0.0237  0.0386  360  SER A N   
2586  C CA  . SER A 362  ? 0.1784 0.1993 0.2423 0.0103  0.0219  0.0357  360  SER A CA  
2587  C C   . SER A 362  ? 0.2192 0.2393 0.2874 0.0081  0.0205  0.0361  360  SER A C   
2588  O O   . SER A 362  ? 0.2345 0.2532 0.3025 0.0082  0.0190  0.0342  360  SER A O   
2589  C CB  . SER A 362  ? 0.2120 0.2272 0.2715 0.0102  0.0209  0.0337  360  SER A CB  
2590  O OG  . SER A 362  ? 0.1981 0.2106 0.2589 0.0080  0.0204  0.0347  360  SER A OG  
2591  N N   . GLY A 363  ? 0.2172 0.2382 0.2895 0.0060  0.0207  0.0384  361  GLY A N   
2592  C CA  . GLY A 363  ? 0.2292 0.2489 0.3057 0.0038  0.0190  0.0381  361  GLY A CA  
2593  C C   . GLY A 363  ? 0.2485 0.2628 0.3231 0.0027  0.0172  0.0355  361  GLY A C   
2594  O O   . GLY A 363  ? 0.2688 0.2824 0.3462 0.0012  0.0156  0.0343  361  GLY A O   
2595  N N   . ARG A 364  ? 0.2127 0.2237 0.2826 0.0034  0.0173  0.0344  362  ARG A N   
2596  C CA  . ARG A 364  ? 0.2310 0.2374 0.2988 0.0024  0.0157  0.0320  362  ARG A CA  
2597  C C   . ARG A 364  ? 0.2311 0.2358 0.3015 0.0009  0.0158  0.0329  362  ARG A C   
2598  O O   . ARG A 364  ? 0.2311 0.2364 0.3011 0.0014  0.0172  0.0350  362  ARG A O   
2599  C CB  . ARG A 364  ? 0.2598 0.2637 0.3214 0.0040  0.0159  0.0304  362  ARG A CB  
2600  C CG  . ARG A 364  ? 0.3048 0.3100 0.3640 0.0060  0.0160  0.0298  362  ARG A CG  
2601  C CD  . ARG A 364  ? 0.2336 0.2372 0.2914 0.0057  0.0141  0.0278  362  ARG A CD  
2602  N NE  . ARG A 364  ? 0.2181 0.2236 0.2757 0.0075  0.0140  0.0278  362  ARG A NE  
2603  C CZ  . ARG A 364  ? 0.2197 0.2236 0.2740 0.0091  0.0138  0.0268  362  ARG A CZ  
2604  N NH1 . ARG A 364  ? 0.2017 0.2022 0.2522 0.0091  0.0135  0.0258  362  ARG A NH1 
2605  N NH2 . ARG A 364  ? 0.2087 0.2146 0.2640 0.0108  0.0136  0.0267  362  ARG A NH2 
2606  N N   . ARG A 365  ? 0.2113 0.2141 0.2844 -0.0009 0.0140  0.0312  363  ARG A N   
2607  C CA  . ARG A 365  ? 0.1968 0.1975 0.2732 -0.0022 0.0137  0.0317  363  ARG A CA  
2608  C C   . ARG A 365  ? 0.2085 0.2056 0.2799 -0.0016 0.0135  0.0298  363  ARG A C   
2609  O O   . ARG A 365  ? 0.2352 0.2303 0.3054 -0.0022 0.0120  0.0268  363  ARG A O   
2610  C CB  . ARG A 365  ? 0.2025 0.2029 0.2846 -0.0042 0.0117  0.0300  363  ARG A CB  
2611  C CG  . ARG A 365  ? 0.2165 0.2149 0.3036 -0.0056 0.0111  0.0306  363  ARG A CG  
2612  C CD  . ARG A 365  ? 0.2756 0.2747 0.3704 -0.0075 0.0095  0.0300  363  ARG A CD  
2613  N NE  . ARG A 365  ? 0.2383 0.2350 0.3386 -0.0087 0.0088  0.0308  363  ARG A NE  
2614  C CZ  . ARG A 365  ? 0.2175 0.2115 0.3203 -0.0096 0.0068  0.0272  363  ARG A CZ  
2615  N NH1 . ARG A 365  ? 0.2598 0.2538 0.3598 -0.0094 0.0055  0.0227  363  ARG A NH1 
2616  N NH2 . ARG A 365  ? 0.2101 0.2018 0.3185 -0.0105 0.0062  0.0283  363  ARG A NH2 
2617  N N   . ILE A 366  ? 0.1930 0.1900 0.2613 -0.0003 0.0151  0.0316  364  ILE A N   
2618  C CA  . ILE A 366  ? 0.1870 0.1809 0.2501 0.0005  0.0150  0.0299  364  ILE A CA  
2619  C C   . ILE A 366  ? 0.1811 0.1722 0.2468 -0.0009 0.0139  0.0287  364  ILE A C   
2620  O O   . ILE A 366  ? 0.1782 0.1693 0.2491 -0.0019 0.0138  0.0306  364  ILE A O   
2621  C CB  . ILE A 366  ? 0.1890 0.1841 0.2488 0.0021  0.0169  0.0320  364  ILE A CB  
2622  C CG1 . ILE A 366  ? 0.2422 0.2402 0.2998 0.0037  0.0178  0.0323  364  ILE A CG1 
2623  C CG2 . ILE A 366  ? 0.2103 0.2022 0.2652 0.0028  0.0167  0.0303  364  ILE A CG2 
2624  C CD1 . ILE A 366  ? 0.2348 0.2351 0.2895 0.0055  0.0196  0.0340  364  ILE A CD1 
2625  N N   . MET A 367  ? 0.1970 0.1858 0.2594 -0.0009 0.0128  0.0255  365  MET A N   
2626  C CA  . MET A 367  ? 0.1987 0.1849 0.2630 -0.0018 0.0117  0.0237  365  MET A CA  
2627  C C   . MET A 367  ? 0.1990 0.1836 0.2606 -0.0009 0.0127  0.0251  365  MET A C   
2628  O O   . MET A 367  ? 0.2443 0.2285 0.3002 0.0004  0.0135  0.0247  365  MET A O   
2629  C CB  . MET A 367  ? 0.1926 0.1783 0.2544 -0.0021 0.0102  0.0197  365  MET A CB  
2630  C CG  . MET A 367  ? 0.2133 0.2014 0.2768 -0.0028 0.0092  0.0186  365  MET A CG  
2631  S SD  . MET A 367  ? 0.2322 0.2212 0.2928 -0.0033 0.0074  0.0143  365  MET A SD  
2632  C CE  . MET A 367  ? 0.2816 0.2704 0.3487 -0.0047 0.0056  0.0111  365  MET A CE  
2633  N N   . VAL A 368  ? 0.1740 0.1577 0.2400 -0.0015 0.0128  0.0270  366  VAL A N   
2634  C CA  . VAL A 368  ? 0.1861 0.1689 0.2500 -0.0006 0.0138  0.0289  366  VAL A CA  
2635  C C   . VAL A 368  ? 0.1746 0.1543 0.2405 -0.0012 0.0125  0.0269  366  VAL A C   
2636  O O   . VAL A 368  ? 0.1810 0.1599 0.2536 -0.0024 0.0115  0.0272  366  VAL A O   
2637  C CB  . VAL A 368  ? 0.1897 0.1749 0.2569 -0.0007 0.0151  0.0336  366  VAL A CB  
2638  C CG1 . VAL A 368  ? 0.2012 0.1859 0.2657 0.0003  0.0161  0.0355  366  VAL A CG1 
2639  C CG2 . VAL A 368  ? 0.2206 0.2096 0.2861 0.0001  0.0164  0.0352  366  VAL A CG2 
2640  N N   . ARG A 369  ? 0.1758 0.1540 0.2364 -0.0004 0.0125  0.0247  367  ARG A N   
2641  C CA  . ARG A 369  ? 0.1939 0.1695 0.2560 -0.0006 0.0115  0.0227  367  ARG A CA  
2642  C C   . ARG A 369  ? 0.1912 0.1662 0.2535 0.0000  0.0124  0.0259  367  ARG A C   
2643  O O   . ARG A 369  ? 0.2081 0.1837 0.2649 0.0012  0.0136  0.0270  367  ARG A O   
2644  C CB  . ARG A 369  ? 0.2093 0.1842 0.2660 -0.0002 0.0110  0.0189  367  ARG A CB  
2645  C CG  . ARG A 369  ? 0.2121 0.1850 0.2707 -0.0004 0.0098  0.0165  367  ARG A CG  
2646  C CD  . ARG A 369  ? 0.2167 0.1893 0.2693 0.0003  0.0098  0.0139  367  ARG A CD  
2647  N NE  . ARG A 369  ? 0.1934 0.1678 0.2438 -0.0001 0.0091  0.0111  367  ARG A NE  
2648  C CZ  . ARG A 369  ? 0.2185 0.1937 0.2630 0.0003  0.0094  0.0101  367  ARG A CZ  
2649  N NH1 . ARG A 369  ? 0.2260 0.1999 0.2662 0.0012  0.0103  0.0111  367  ARG A NH1 
2650  N NH2 . ARG A 369  ? 0.2096 0.1870 0.2528 -0.0002 0.0086  0.0081  367  ARG A NH2 
2651  N N   . LEU A 370  ? 0.1753 0.1492 0.2443 -0.0009 0.0116  0.0275  368  LEU A N   
2652  C CA  . LEU A 370  ? 0.1851 0.1585 0.2550 -0.0004 0.0121  0.0308  368  LEU A CA  
2653  C C   . LEU A 370  ? 0.1981 0.1687 0.2674 0.0000  0.0111  0.0278  368  LEU A C   
2654  O O   . LEU A 370  ? 0.1964 0.1652 0.2704 -0.0008 0.0093  0.0247  368  LEU A O   
2655  C CB  . LEU A 370  ? 0.2089 0.1827 0.2872 -0.0016 0.0117  0.0348  368  LEU A CB  
2656  C CG  . LEU A 370  ? 0.2108 0.1851 0.2906 -0.0012 0.0123  0.0393  368  LEU A CG  
2657  C CD1 . LEU A 370  ? 0.2445 0.2225 0.3179 0.0000  0.0145  0.0424  368  LEU A CD1 
2658  C CD2 . LEU A 370  ? 0.2287 0.2030 0.3182 -0.0027 0.0113  0.0432  368  LEU A CD2 
2659  N N   . VAL A 371  ? 0.1842 0.1547 0.2478 0.0012  0.0120  0.0283  369  VAL A N   
2660  C CA  . VAL A 371  ? 0.1882 0.1565 0.2507 0.0016  0.0112  0.0257  369  VAL A CA  
2661  C C   . VAL A 371  ? 0.1938 0.1623 0.2567 0.0023  0.0119  0.0297  369  VAL A C   
2662  O O   . VAL A 371  ? 0.2060 0.1769 0.2685 0.0025  0.0132  0.0339  369  VAL A O   
2663  C CB  . VAL A 371  ? 0.1886 0.1570 0.2435 0.0024  0.0116  0.0223  369  VAL A CB  
2664  C CG1 . VAL A 371  ? 0.1925 0.1617 0.2466 0.0018  0.0111  0.0193  369  VAL A CG1 
2665  C CG2 . VAL A 371  ? 0.2093 0.1793 0.2580 0.0036  0.0133  0.0246  369  VAL A CG2 
2666  N N   . LYS A 372  ? 0.1932 0.1596 0.2567 0.0027  0.0111  0.0282  370  LYS A N   
2667  C CA  . LYS A 372  ? 0.2027 0.1697 0.2652 0.0035  0.0117  0.0318  370  LYS A CA  
2668  C C   . LYS A 372  ? 0.2230 0.1914 0.2767 0.0048  0.0131  0.0312  370  LYS A C   
2669  O O   . LYS A 372  ? 0.2401 0.2113 0.2908 0.0054  0.0146  0.0343  370  LYS A O   
2670  C CB  . LYS A 372  ? 0.2476 0.2120 0.3157 0.0034  0.0101  0.0314  370  LYS A CB  
2671  C CG  . LYS A 372  ? 0.2389 0.2023 0.3167 0.0021  0.0088  0.0334  370  LYS A CG  
2672  C CD  . LYS A 372  ? 0.2561 0.2166 0.3413 0.0020  0.0068  0.0328  370  LYS A CD  
2673  C CE  . LYS A 372  ? 0.2418 0.2010 0.3371 0.0006  0.0052  0.0339  370  LYS A CE  
2674  N NZ  . LYS A 372  ? 0.2463 0.2023 0.3500 0.0006  0.0028  0.0326  370  LYS A NZ  
2675  N N   . GLY A 373  ? 0.2035 0.1706 0.2533 0.0052  0.0127  0.0270  371  GLY A N   
2676  C CA  . GLY A 373  ? 0.1947 0.1628 0.2368 0.0062  0.0138  0.0260  371  GLY A CA  
2677  C C   . GLY A 373  ? 0.2010 0.1676 0.2404 0.0066  0.0132  0.0229  371  GLY A C   
2678  O O   . GLY A 373  ? 0.2167 0.1820 0.2594 0.0067  0.0123  0.0228  371  GLY A O   
2679  N N   . ALA A 374  ? 0.2002 0.1671 0.2340 0.0069  0.0135  0.0205  372  ALA A N   
2680  C CA  . ALA A 374  ? 0.2026 0.1685 0.2341 0.0070  0.0128  0.0171  372  ALA A CA  
2681  C C   . ALA A 374  ? 0.2197 0.1860 0.2464 0.0080  0.0134  0.0175  372  ALA A C   
2682  O O   . ALA A 374  ? 0.2431 0.2088 0.2681 0.0081  0.0128  0.0150  372  ALA A O   
2683  C CB  . ALA A 374  ? 0.2133 0.1797 0.2425 0.0063  0.0125  0.0141  372  ALA A CB  
2684  N N   . TYR A 375  ? 0.2125 0.1801 0.2371 0.0089  0.0144  0.0203  373  TYR A N   
2685  C CA  . TYR A 375  ? 0.2043 0.1726 0.2239 0.0099  0.0148  0.0201  373  TYR A CA  
2686  C C   . TYR A 375  ? 0.1920 0.1615 0.2124 0.0108  0.0151  0.0229  373  TYR A C   
2687  O O   . TYR A 375  ? 0.2098 0.1811 0.2264 0.0118  0.0158  0.0237  373  TYR A O   
2688  C CB  . TYR A 375  ? 0.2156 0.1854 0.2313 0.0104  0.0157  0.0202  373  TYR A CB  
2689  C CG  . TYR A 375  ? 0.2047 0.1737 0.2196 0.0097  0.0153  0.0181  373  TYR A CG  
2690  C CD1 . TYR A 375  ? 0.2006 0.1698 0.2186 0.0089  0.0153  0.0186  373  TYR A CD1 
2691  C CD2 . TYR A 375  ? 0.2700 0.2384 0.2813 0.0096  0.0149  0.0158  373  TYR A CD2 
2692  C CE1 . TYR A 375  ? 0.2268 0.1957 0.2441 0.0082  0.0149  0.0169  373  TYR A CE1 
2693  C CE2 . TYR A 375  ? 0.2635 0.2315 0.2743 0.0088  0.0145  0.0144  373  TYR A CE2 
2694  C CZ  . TYR A 375  ? 0.2695 0.2380 0.2831 0.0082  0.0145  0.0150  373  TYR A CZ  
2695  O OH  . TYR A 375  ? 0.2815 0.2501 0.2946 0.0074  0.0140  0.0138  373  TYR A OH  
2696  N N   . TRP A 376  ? 0.1800 0.1487 0.2055 0.0104  0.0146  0.0245  374  TRP A N   
2697  C CA  . TRP A 376  ? 0.1998 0.1701 0.2269 0.0110  0.0148  0.0283  374  TRP A CA  
2698  C C   . TRP A 376  ? 0.2185 0.1898 0.2415 0.0121  0.0149  0.0279  374  TRP A C   
2699  O O   . TRP A 376  ? 0.2146 0.1889 0.2348 0.0131  0.0157  0.0301  374  TRP A O   
2700  C CB  . TRP A 376  ? 0.2124 0.1812 0.2467 0.0104  0.0138  0.0300  374  TRP A CB  
2701  C CG  . TRP A 376  ? 0.2087 0.1796 0.2451 0.0109  0.0139  0.0347  374  TRP A CG  
2702  C CD1 . TRP A 376  ? 0.2179 0.1918 0.2557 0.0109  0.0148  0.0392  374  TRP A CD1 
2703  C CD2 . TRP A 376  ? 0.2228 0.1936 0.2598 0.0116  0.0133  0.0357  374  TRP A CD2 
2704  N NE1 . TRP A 376  ? 0.2037 0.1797 0.2432 0.0114  0.0147  0.0432  374  TRP A NE1 
2705  C CE2 . TRP A 376  ? 0.2166 0.1906 0.2557 0.0119  0.0137  0.0411  374  TRP A CE2 
2706  C CE3 . TRP A 376  ? 0.2428 0.2117 0.2792 0.0120  0.0124  0.0326  374  TRP A CE3 
2707  C CZ2 . TRP A 376  ? 0.2435 0.2185 0.2838 0.0126  0.0131  0.0437  374  TRP A CZ2 
2708  C CZ3 . TRP A 376  ? 0.2820 0.2516 0.3198 0.0128  0.0118  0.0349  374  TRP A CZ3 
2709  C CH2 . TRP A 376  ? 0.2599 0.2323 0.2996 0.0131  0.0122  0.0405  374  TRP A CH2 
2710  N N   . ASP A 377  ? 0.2166 0.1858 0.2393 0.0121  0.0140  0.0250  375  ASP A N   
2711  C CA  A ASP A 377  ? 0.2300 0.2001 0.2492 0.0130  0.0139  0.0244  375  ASP A CA  
2712  C CA  B ASP A 377  ? 0.2299 0.2001 0.2491 0.0130  0.0140  0.0247  375  ASP A CA  
2713  C C   . ASP A 377  ? 0.2260 0.1979 0.2392 0.0137  0.0148  0.0236  375  ASP A C   
2714  O O   . ASP A 377  ? 0.2331 0.2074 0.2436 0.0148  0.0151  0.0247  375  ASP A O   
2715  C CB  A ASP A 377  ? 0.2593 0.2273 0.2784 0.0126  0.0130  0.0206  375  ASP A CB  
2716  C CB  B ASP A 377  ? 0.2635 0.2317 0.2839 0.0129  0.0129  0.0218  375  ASP A CB  
2717  C CG  A ASP A 377  ? 0.3270 0.2933 0.3520 0.0123  0.0119  0.0205  375  ASP A CG  
2718  C CG  B ASP A 377  ? 0.2919 0.2586 0.3108 0.0120  0.0126  0.0178  375  ASP A CG  
2719  O OD1 A ASP A 377  ? 0.3748 0.3413 0.4037 0.0126  0.0116  0.0238  375  ASP A OD1 
2720  O OD1 B ASP A 377  ? 0.3444 0.3118 0.3592 0.0119  0.0131  0.0167  375  ASP A OD1 
2721  O OD2 A ASP A 377  ? 0.3801 0.3451 0.4062 0.0118  0.0112  0.0170  375  ASP A OD2 
2722  O OD2 B ASP A 377  ? 0.3410 0.3065 0.3632 0.0115  0.0117  0.0156  375  ASP A OD2 
2723  N N   . ALA A 378  ? 0.2049 0.1759 0.2164 0.0132  0.0149  0.0214  376  ALA A N   
2724  C CA  . ALA A 378  ? 0.2076 0.1798 0.2143 0.0138  0.0154  0.0201  376  ALA A CA  
2725  C C   . ALA A 378  ? 0.2287 0.2043 0.2344 0.0149  0.0164  0.0227  376  ALA A C   
2726  O O   . ALA A 378  ? 0.2117 0.1894 0.2139 0.0160  0.0167  0.0220  376  ALA A O   
2727  C CB  . ALA A 378  ? 0.2165 0.1871 0.2224 0.0129  0.0152  0.0177  376  ALA A CB  
2728  N N   . GLU A 379  ? 0.2078 0.1843 0.2169 0.0145  0.0169  0.0254  377  GLU A N   
2729  C CA  . GLU A 379  ? 0.1915 0.1722 0.1998 0.0155  0.0180  0.0280  377  GLU A CA  
2730  C C   . GLU A 379  ? 0.2111 0.1951 0.2187 0.0165  0.0182  0.0305  377  GLU A C   
2731  O O   . GLU A 379  ? 0.2107 0.1990 0.2153 0.0177  0.0189  0.0312  377  GLU A O   
2732  C CB  . GLU A 379  ? 0.2135 0.1949 0.2261 0.0146  0.0185  0.0308  377  GLU A CB  
2733  C CG  . GLU A 379  ? 0.2061 0.1851 0.2196 0.0137  0.0183  0.0286  377  GLU A CG  
2734  C CD  . GLU A 379  ? 0.2205 0.2008 0.2302 0.0145  0.0188  0.0267  377  GLU A CD  
2735  O OE1 . GLU A 379  ? 0.2342 0.2177 0.2408 0.0160  0.0194  0.0267  377  GLU A OE1 
2736  O OE2 . GLU A 379  ? 0.2313 0.2096 0.2415 0.0138  0.0185  0.0250  377  GLU A OE2 
2737  N N   . ILE A 380  ? 0.2067 0.1891 0.2172 0.0160  0.0174  0.0318  378  ILE A N   
2738  C CA  . ILE A 380  ? 0.2187 0.2042 0.2286 0.0169  0.0174  0.0344  378  ILE A CA  
2739  C C   . ILE A 380  ? 0.2280 0.2147 0.2326 0.0181  0.0173  0.0315  378  ILE A C   
2740  O O   . ILE A 380  ? 0.2208 0.2122 0.2225 0.0194  0.0178  0.0326  378  ILE A O   
2741  C CB  . ILE A 380  ? 0.2063 0.1892 0.2210 0.0162  0.0163  0.0360  378  ILE A CB  
2742  C CG1 . ILE A 380  ? 0.2319 0.2135 0.2528 0.0151  0.0161  0.0387  378  ILE A CG1 
2743  C CG2 . ILE A 380  ? 0.2278 0.2141 0.2420 0.0172  0.0161  0.0389  378  ILE A CG2 
2744  C CD1 . ILE A 380  ? 0.2355 0.2218 0.2575 0.0152  0.0172  0.0434  378  ILE A CD1 
2745  N N   . LYS A 381  ? 0.2035 0.1863 0.2068 0.0176  0.0165  0.0276  379  LYS A N   
2746  C CA  . LYS A 381  ? 0.2087 0.1922 0.2077 0.0185  0.0162  0.0247  379  LYS A CA  
2747  C C   . LYS A 381  ? 0.2199 0.2063 0.2154 0.0195  0.0168  0.0234  379  LYS A C   
2748  O O   . LYS A 381  ? 0.2214 0.2111 0.2138 0.0208  0.0169  0.0227  379  LYS A O   
2749  C CB  . LYS A 381  ? 0.2185 0.1976 0.2172 0.0175  0.0153  0.0212  379  LYS A CB  
2750  C CG  . LYS A 381  ? 0.2099 0.1895 0.2048 0.0181  0.0148  0.0184  379  LYS A CG  
2751  C CD  . LYS A 381  ? 0.2178 0.1938 0.2130 0.0170  0.0139  0.0156  379  LYS A CD  
2752  C CE  . LYS A 381  ? 0.2376 0.2140 0.2296 0.0174  0.0132  0.0131  379  LYS A CE  
2753  N NZ  . LYS A 381  ? 0.2175 0.1912 0.2098 0.0161  0.0124  0.0109  379  LYS A NZ  
2754  N N   . ARG A 382  ? 0.2037 0.1890 0.1999 0.0190  0.0173  0.0227  380  ARG A N   
2755  C CA  . ARG A 382  ? 0.2199 0.2074 0.2133 0.0201  0.0177  0.0208  380  ARG A CA  
2756  C C   . ARG A 382  ? 0.2164 0.2103 0.2088 0.0216  0.0187  0.0231  380  ARG A C   
2757  O O   . ARG A 382  ? 0.2164 0.2136 0.2057 0.0231  0.0187  0.0210  380  ARG A O   
2758  C CB  . ARG A 382  ? 0.2275 0.2129 0.2225 0.0193  0.0179  0.0202  380  ARG A CB  
2759  C CG  . ARG A 382  ? 0.3025 0.2896 0.2955 0.0205  0.0181  0.0178  380  ARG A CG  
2760  C CD  . ARG A 382  ? 0.4444 0.4281 0.4358 0.0203  0.0169  0.0141  380  ARG A CD  
2761  N NE  . ARG A 382  ? 0.4622 0.4483 0.4510 0.0217  0.0165  0.0122  380  ARG A NE  
2762  C CZ  . ARG A 382  ? 0.4728 0.4566 0.4605 0.0216  0.0153  0.0095  380  ARG A CZ  
2763  N NH1 . ARG A 382  ? 0.5072 0.4864 0.4959 0.0199  0.0144  0.0088  380  ARG A NH1 
2764  N NH2 . ARG A 382  ? 0.4417 0.4283 0.4273 0.0230  0.0148  0.0075  380  ARG A NH2 
2765  N N   . ALA A 383  ? 0.2047 0.2008 0.1997 0.0213  0.0194  0.0273  381  ALA A N   
2766  C CA  . ALA A 383  ? 0.2021 0.2054 0.1962 0.0226  0.0204  0.0301  381  ALA A CA  
2767  C C   . ALA A 383  ? 0.2186 0.2253 0.2101 0.0237  0.0200  0.0303  381  ALA A C   
2768  O O   . ALA A 383  ? 0.2283 0.2412 0.2169 0.0254  0.0206  0.0299  381  ALA A O   
2769  C CB  . ALA A 383  ? 0.2228 0.2276 0.2211 0.0216  0.0211  0.0353  381  ALA A CB  
2770  N N   . GLN A 384  ? 0.2049 0.2080 0.1974 0.0229  0.0191  0.0306  382  GLN A N   
2771  C CA  . GLN A 384  ? 0.2093 0.2154 0.1996 0.0240  0.0186  0.0306  382  GLN A CA  
2772  C C   . GLN A 384  ? 0.2175 0.2240 0.2037 0.0251  0.0180  0.0255  382  GLN A C   
2773  O O   . GLN A 384  ? 0.2402 0.2524 0.2234 0.0267  0.0181  0.0250  382  GLN A O   
2774  C CB  . GLN A 384  ? 0.2102 0.2121 0.2030 0.0229  0.0176  0.0318  382  GLN A CB  
2775  C CG  . GLN A 384  ? 0.2133 0.2157 0.2109 0.0221  0.0177  0.0371  382  GLN A CG  
2776  C CD  . GLN A 384  ? 0.2340 0.2328 0.2344 0.0215  0.0165  0.0379  382  GLN A CD  
2777  O OE1 . GLN A 384  ? 0.2391 0.2341 0.2384 0.0213  0.0157  0.0342  382  GLN A OE1 
2778  N NE2 . GLN A 384  ? 0.2488 0.2492 0.2534 0.0212  0.0163  0.0429  382  GLN A NE2 
2779  N N   . LEU A 385  ? 0.2096 0.2104 0.1958 0.0243  0.0174  0.0219  383  LEU A N   
2780  C CA  . LEU A 385  ? 0.2257 0.2261 0.2090 0.0251  0.0166  0.0172  383  LEU A CA  
2781  C C   . LEU A 385  ? 0.2259 0.2315 0.2072 0.0269  0.0172  0.0157  383  LEU A C   
2782  O O   . LEU A 385  ? 0.2461 0.2549 0.2249 0.0283  0.0167  0.0128  383  LEU A O   
2783  C CB  . LEU A 385  ? 0.2198 0.2136 0.2041 0.0238  0.0158  0.0144  383  LEU A CB  
2784  C CG  . LEU A 385  ? 0.2572 0.2463 0.2428 0.0223  0.0150  0.0141  383  LEU A CG  
2785  C CD1 . LEU A 385  ? 0.2778 0.2620 0.2643 0.0210  0.0144  0.0118  383  LEU A CD1 
2786  C CD2 . LEU A 385  ? 0.2827 0.2729 0.2662 0.0229  0.0140  0.0124  383  LEU A CD2 
2787  N N   . ASP A 386  ? 0.2232 0.2301 0.2059 0.0268  0.0183  0.0173  384  ASP A N   
2788  C CA  . ASP A 386  ? 0.2317 0.2435 0.2131 0.0285  0.0189  0.0154  384  ASP A CA  
2789  C C   . ASP A 386  ? 0.2542 0.2749 0.2340 0.0300  0.0200  0.0181  384  ASP A C   
2790  O O   . ASP A 386  ? 0.2628 0.2893 0.2414 0.0317  0.0206  0.0165  384  ASP A O   
2791  C CB  . ASP A 386  ? 0.2492 0.2585 0.2328 0.0277  0.0195  0.0158  384  ASP A CB  
2792  C CG  . ASP A 386  ? 0.3256 0.3276 0.3102 0.0266  0.0183  0.0126  384  ASP A CG  
2793  O OD1 . ASP A 386  ? 0.3245 0.3239 0.3080 0.0266  0.0171  0.0098  384  ASP A OD1 
2794  O OD2 . ASP A 386  ? 0.3335 0.3327 0.3202 0.0257  0.0186  0.0130  384  ASP A OD2 
2795  N N   . GLY A 387  ? 0.2366 0.2592 0.2168 0.0295  0.0201  0.0221  385  GLY A N   
2796  C CA  . GLY A 387  ? 0.2392 0.2710 0.2181 0.0309  0.0210  0.0253  385  GLY A CA  
2797  C C   . GLY A 387  ? 0.2374 0.2742 0.2176 0.0310  0.0226  0.0284  385  GLY A C   
2798  O O   . GLY A 387  ? 0.2508 0.2965 0.2289 0.0328  0.0234  0.0285  385  GLY A O   
2799  N N   . LEU A 388  ? 0.2373 0.2692 0.2210 0.0293  0.0229  0.0308  386  LEU A N   
2800  C CA  . LEU A 388  ? 0.2589 0.2953 0.2442 0.0294  0.0243  0.0333  386  LEU A CA  
2801  C C   . LEU A 388  ? 0.2655 0.3071 0.2531 0.0287  0.0252  0.0403  386  LEU A C   
2802  O O   . LEU A 388  ? 0.2623 0.3031 0.2509 0.0280  0.0245  0.0433  386  LEU A O   
2803  C CB  . LEU A 388  ? 0.2412 0.2706 0.2292 0.0280  0.0243  0.0320  386  LEU A CB  
2804  C CG  . LEU A 388  ? 0.2619 0.2870 0.2480 0.0287  0.0233  0.0257  386  LEU A CG  
2805  C CD1 . LEU A 388  ? 0.2753 0.2938 0.2641 0.0273  0.0232  0.0248  386  LEU A CD1 
2806  C CD2 . LEU A 388  ? 0.2697 0.3017 0.2530 0.0312  0.0238  0.0223  386  LEU A CD2 
2807  N N   . ALA A 389  ? 0.2739 0.3215 0.2627 0.0289  0.0266  0.0431  387  ALA A N   
2808  C CA  . ALA A 389  ? 0.2960 0.3508 0.2868 0.0284  0.0274  0.0501  387  ALA A CA  
2809  C C   . ALA A 389  ? 0.2676 0.3159 0.2636 0.0261  0.0267  0.0548  387  ALA A C   
2810  O O   . ALA A 389  ? 0.2901 0.3418 0.2879 0.0256  0.0265  0.0601  387  ALA A O   
2811  C CB  . ALA A 389  ? 0.3313 0.3936 0.3228 0.0289  0.0291  0.0520  387  ALA A CB  
2812  N N   . ASP A 390  ? 0.2420 0.2816 0.2409 0.0246  0.0261  0.0530  388  ASP A N   
2813  C CA  . ASP A 390  ? 0.2640 0.2978 0.2687 0.0224  0.0254  0.0568  388  ASP A CA  
2814  C C   . ASP A 390  ? 0.2254 0.2498 0.2312 0.0214  0.0246  0.0521  388  ASP A C   
2815  O O   . ASP A 390  ? 0.2298 0.2526 0.2320 0.0223  0.0246  0.0469  388  ASP A O   
2816  C CB  . ASP A 390  ? 0.2580 0.2967 0.2672 0.0214  0.0263  0.0630  388  ASP A CB  
2817  C CG  . ASP A 390  ? 0.2700 0.3057 0.2855 0.0196  0.0254  0.0686  388  ASP A CG  
2818  O OD1 . ASP A 390  ? 0.2833 0.3105 0.3014 0.0186  0.0240  0.0666  388  ASP A OD1 
2819  O OD2 . ASP A 390  ? 0.3080 0.3502 0.3265 0.0191  0.0259  0.0750  388  ASP A OD2 
2820  N N   . PHE A 391  ? 0.2158 0.2344 0.2266 0.0196  0.0237  0.0541  389  PHE A N   
2821  C CA  . PHE A 391  ? 0.2249 0.2355 0.2371 0.0186  0.0229  0.0501  389  PHE A CA  
2822  C C   . PHE A 391  ? 0.2261 0.2368 0.2407 0.0178  0.0236  0.0505  389  PHE A C   
2823  O O   . PHE A 391  ? 0.2357 0.2513 0.2531 0.0175  0.0245  0.0551  389  PHE A O   
2824  C CB  . PHE A 391  ? 0.2300 0.2348 0.2468 0.0172  0.0215  0.0513  389  PHE A CB  
2825  C CG  . PHE A 391  ? 0.2131 0.2179 0.2281 0.0179  0.0207  0.0510  389  PHE A CG  
2826  C CD1 . PHE A 391  ? 0.2190 0.2208 0.2295 0.0186  0.0202  0.0459  389  PHE A CD1 
2827  C CD2 . PHE A 391  ? 0.2220 0.2303 0.2394 0.0179  0.0205  0.0562  389  PHE A CD2 
2828  C CE1 . PHE A 391  ? 0.2439 0.2460 0.2526 0.0193  0.0195  0.0455  389  PHE A CE1 
2829  C CE2 . PHE A 391  ? 0.2343 0.2430 0.2498 0.0188  0.0197  0.0559  389  PHE A CE2 
2830  C CZ  . PHE A 391  ? 0.2484 0.2540 0.2595 0.0195  0.0193  0.0504  389  PHE A CZ  
2831  N N   . PRO A 392  ? 0.2161 0.2218 0.2298 0.0175  0.0232  0.0460  390  PRO A N   
2832  C CA  . PRO A 392  ? 0.2049 0.2100 0.2214 0.0166  0.0237  0.0463  390  PRO A CA  
2833  C C   . PRO A 392  ? 0.2135 0.2134 0.2359 0.0146  0.0227  0.0477  390  PRO A C   
2834  O O   . PRO A 392  ? 0.2143 0.2133 0.2396 0.0137  0.0228  0.0477  390  PRO A O   
2835  C CB  . PRO A 392  ? 0.2077 0.2100 0.2204 0.0173  0.0235  0.0408  390  PRO A CB  
2836  C CG  . PRO A 392  ? 0.2058 0.2034 0.2164 0.0173  0.0223  0.0378  390  PRO A CG  
2837  C CD  . PRO A 392  ? 0.2025 0.2036 0.2125 0.0179  0.0224  0.0407  390  PRO A CD  
2838  N N   . VAL A 393  ? 0.2156 0.2125 0.2403 0.0140  0.0216  0.0486  391  VAL A N   
2839  C CA  . VAL A 393  ? 0.2103 0.2025 0.2413 0.0123  0.0204  0.0496  391  VAL A CA  
2840  C C   . VAL A 393  ? 0.2095 0.2035 0.2448 0.0120  0.0199  0.0547  391  VAL A C   
2841  O O   . VAL A 393  ? 0.2276 0.2255 0.2600 0.0131  0.0203  0.0566  391  VAL A O   
2842  C CB  . VAL A 393  ? 0.1879 0.1739 0.2182 0.0120  0.0191  0.0446  391  VAL A CB  
2843  C CG1 . VAL A 393  ? 0.2219 0.2062 0.2490 0.0120  0.0193  0.0404  391  VAL A CG1 
2844  C CG2 . VAL A 393  ? 0.2147 0.2005 0.2412 0.0131  0.0187  0.0432  391  VAL A CG2 
2845  N N   . PHE A 394  ? 0.2117 0.2029 0.2542 0.0105  0.0189  0.0569  392  PHE A N   
2846  C CA  . PHE A 394  ? 0.1902 0.1819 0.2382 0.0100  0.0180  0.0616  392  PHE A CA  
2847  C C   . PHE A 394  ? 0.2102 0.1984 0.2568 0.0107  0.0168  0.0590  392  PHE A C   
2848  O O   . PHE A 394  ? 0.2178 0.2024 0.2607 0.0111  0.0165  0.0535  392  PHE A O   
2849  C CB  . PHE A 394  ? 0.2277 0.2165 0.2847 0.0082  0.0168  0.0639  392  PHE A CB  
2850  C CG  . PHE A 394  ? 0.2137 0.2063 0.2724 0.0075  0.0179  0.0668  392  PHE A CG  
2851  C CD1 . PHE A 394  ? 0.2322 0.2318 0.2907 0.0077  0.0192  0.0727  392  PHE A CD1 
2852  C CD2 . PHE A 394  ? 0.2255 0.2154 0.2856 0.0066  0.0178  0.0637  392  PHE A CD2 
2853  C CE1 . PHE A 394  ? 0.2161 0.2199 0.2761 0.0070  0.0203  0.0754  392  PHE A CE1 
2854  C CE2 . PHE A 394  ? 0.2171 0.2107 0.2787 0.0060  0.0188  0.0663  392  PHE A CE2 
2855  C CZ  . PHE A 394  ? 0.2221 0.2227 0.2838 0.0062  0.0201  0.0722  392  PHE A CZ  
2856  N N   . THR A 395  ? 0.2166 0.2064 0.2662 0.0109  0.0162  0.0633  393  THR A N   
2857  C CA  . THR A 395  ? 0.2384 0.2255 0.2872 0.0116  0.0150  0.0613  393  THR A CA  
2858  C C   . THR A 395  ? 0.2461 0.2289 0.3037 0.0107  0.0130  0.0629  393  THR A C   
2859  O O   . THR A 395  ? 0.2393 0.2192 0.2972 0.0112  0.0119  0.0606  393  THR A O   
2860  C CB  . THR A 395  ? 0.2489 0.2414 0.2931 0.0129  0.0157  0.0642  393  THR A CB  
2861  O OG1 . THR A 395  ? 0.2458 0.2431 0.2946 0.0125  0.0158  0.0714  393  THR A OG1 
2862  C CG2 . THR A 395  ? 0.2657 0.2621 0.3014 0.0141  0.0174  0.0614  393  THR A CG2 
2863  N N   . ARG A 396  ? 0.2399 0.2224 0.3051 0.0093  0.0124  0.0667  394  ARG A N   
2864  C CA  . ARG A 396  ? 0.2603 0.2380 0.3349 0.0084  0.0102  0.0673  394  ARG A CA  
2865  C C   . ARG A 396  ? 0.2337 0.2073 0.3116 0.0073  0.0097  0.0632  394  ARG A C   
2866  O O   . ARG A 396  ? 0.2345 0.2102 0.3120 0.0065  0.0107  0.0643  394  ARG A O   
2867  C CB  . ARG A 396  ? 0.2745 0.2549 0.3568 0.0075  0.0095  0.0753  394  ARG A CB  
2868  C CG  . ARG A 396  ? 0.2883 0.2731 0.3682 0.0085  0.0098  0.0798  394  ARG A CG  
2869  C CD  . ARG A 396  ? 0.3139 0.3008 0.4028 0.0075  0.0086  0.0881  394  ARG A CD  
2870  N NE  . ARG A 396  ? 0.3604 0.3536 0.4462 0.0084  0.0092  0.0934  394  ARG A NE  
2871  C CZ  . ARG A 396  ? 0.4121 0.4049 0.5032 0.0086  0.0075  0.0974  394  ARG A CZ  
2872  N NH1 . ARG A 396  ? 0.4399 0.4264 0.5407 0.0079  0.0050  0.0972  394  ARG A NH1 
2873  N NH2 . ARG A 396  ? 0.3570 0.3562 0.4438 0.0096  0.0082  0.1017  394  ARG A NH2 
2874  N N   . LYS A 397  ? 0.2488 0.2172 0.3300 0.0073  0.0080  0.0582  395  LYS A N   
2875  C CA  . LYS A 397  ? 0.2570 0.2222 0.3408 0.0064  0.0074  0.0535  395  LYS A CA  
2876  C C   . LYS A 397  ? 0.2442 0.2094 0.3363 0.0048  0.0067  0.0574  395  LYS A C   
2877  O O   . LYS A 397  ? 0.2329 0.1980 0.3249 0.0040  0.0072  0.0555  395  LYS A O   
2878  C CB  . LYS A 397  ? 0.2894 0.2501 0.3763 0.0068  0.0055  0.0479  395  LYS A CB  
2879  C CG  . LYS A 397  ? 0.2816 0.2400 0.3683 0.0063  0.0051  0.0416  395  LYS A CG  
2880  C CD  . LYS A 397  ? 0.2701 0.2258 0.3672 0.0051  0.0032  0.0415  395  LYS A CD  
2881  C CE  . LYS A 397  ? 0.2752 0.2298 0.3714 0.0046  0.0029  0.0352  395  LYS A CE  
2882  N NZ  . LYS A 397  ? 0.2925 0.2446 0.3993 0.0035  0.0008  0.0343  395  LYS A NZ  
2883  N N   . ILE A 398  ? 0.2424 0.2079 0.3422 0.0043  0.0056  0.0633  396  ILE A N   
2884  C CA  . ILE A 398  ? 0.2649 0.2303 0.3738 0.0026  0.0047  0.0674  396  ILE A CA  
2885  C C   . ILE A 398  ? 0.2253 0.1960 0.3301 0.0020  0.0069  0.0711  396  ILE A C   
2886  O O   . ILE A 398  ? 0.2493 0.2200 0.3592 0.0006  0.0067  0.0724  396  ILE A O   
2887  C CB  . ILE A 398  ? 0.2879 0.2526 0.4063 0.0022  0.0027  0.0734  396  ILE A CB  
2888  C CG1 . ILE A 398  ? 0.3565 0.3193 0.4868 0.0003  0.0010  0.0763  396  ILE A CG1 
2889  C CG2 . ILE A 398  ? 0.2934 0.2642 0.4079 0.0026  0.0043  0.0805  396  ILE A CG2 
2890  C CD1 . ILE A 398  ? 0.3621 0.3217 0.5038 -0.0001 -0.0019 0.0797  396  ILE A CD1 
2891  N N   . HIS A 399  ? 0.2415 0.2169 0.3370 0.0032  0.0090  0.0725  397  HIS A N   
2892  C CA  . HIS A 399  ? 0.2416 0.2225 0.3327 0.0030  0.0112  0.0752  397  HIS A CA  
2893  C C   . HIS A 399  ? 0.2345 0.2137 0.3221 0.0028  0.0119  0.0694  397  HIS A C   
2894  O O   . HIS A 399  ? 0.2403 0.2216 0.3299 0.0018  0.0125  0.0712  397  HIS A O   
2895  C CB  . HIS A 399  ? 0.2449 0.2313 0.3270 0.0046  0.0132  0.0768  397  HIS A CB  
2896  C CG  . HIS A 399  ? 0.2513 0.2413 0.3365 0.0047  0.0128  0.0835  397  HIS A CG  
2897  N ND1 . HIS A 399  ? 0.2535 0.2484 0.3315 0.0062  0.0140  0.0851  397  HIS A ND1 
2898  C CD2 . HIS A 399  ? 0.2874 0.2767 0.3823 0.0034  0.0111  0.0893  397  HIS A CD2 
2899  C CE1 . HIS A 399  ? 0.2711 0.2688 0.3540 0.0059  0.0133  0.0917  397  HIS A CE1 
2900  N NE2 . HIS A 399  ? 0.2842 0.2783 0.3775 0.0042  0.0115  0.0946  397  HIS A NE2 
2901  N N   . THR A 400  ? 0.2292 0.2049 0.3118 0.0037  0.0116  0.0627  398  THR A N   
2902  C CA  . THR A 400  ? 0.2045 0.1783 0.2843 0.0034  0.0119  0.0573  398  THR A CA  
2903  C C   . THR A 400  ? 0.2147 0.1856 0.3036 0.0018  0.0102  0.0568  398  THR A C   
2904  O O   . THR A 400  ? 0.2029 0.1747 0.2917 0.0011  0.0108  0.0559  398  THR A O   
2905  C CB  . THR A 400  ? 0.2340 0.2049 0.3081 0.0045  0.0116  0.0509  398  THR A CB  
2906  O OG1 . THR A 400  ? 0.2216 0.1955 0.2873 0.0059  0.0132  0.0513  398  THR A OG1 
2907  C CG2 . THR A 400  ? 0.2247 0.1937 0.2967 0.0041  0.0116  0.0456  398  THR A CG2 
2908  N N   . ASP A 401  ? 0.2112 0.1787 0.3084 0.0012  0.0081  0.0574  399  ASP A N   
2909  C CA  . ASP A 401  ? 0.2298 0.1944 0.3364 -0.0003 0.0062  0.0564  399  ASP A CA  
2910  C C   . ASP A 401  ? 0.2121 0.1799 0.3236 -0.0017 0.0067  0.0625  399  ASP A C   
2911  O O   . ASP A 401  ? 0.2171 0.1845 0.3318 -0.0028 0.0064  0.0610  399  ASP A O   
2912  C CB  . ASP A 401  ? 0.2293 0.1896 0.3448 -0.0004 0.0036  0.0558  399  ASP A CB  
2913  C CG  . ASP A 401  ? 0.2594 0.2167 0.3713 0.0009  0.0028  0.0487  399  ASP A CG  
2914  O OD1 . ASP A 401  ? 0.2627 0.2203 0.3677 0.0013  0.0037  0.0436  399  ASP A OD1 
2915  O OD2 . ASP A 401  ? 0.2985 0.2533 0.4148 0.0014  0.0012  0.0485  399  ASP A OD2 
2916  N N   . VAL A 402  ? 0.2174 0.1890 0.3297 -0.0017 0.0076  0.0695  400  VAL A N   
2917  C CA  . VAL A 402  ? 0.2151 0.1910 0.3318 -0.0031 0.0083  0.0760  400  VAL A CA  
2918  C C   . VAL A 402  ? 0.2129 0.1926 0.3218 -0.0028 0.0106  0.0745  400  VAL A C   
2919  O O   . VAL A 402  ? 0.2000 0.1810 0.3129 -0.0041 0.0107  0.0757  400  VAL A O   
2920  C CB  . VAL A 402  ? 0.2147 0.1950 0.3327 -0.0031 0.0088  0.0840  400  VAL A CB  
2921  C CG1 . VAL A 402  ? 0.2243 0.2106 0.3457 -0.0045 0.0100  0.0909  400  VAL A CG1 
2922  C CG2 . VAL A 402  ? 0.2700 0.2461 0.3974 -0.0036 0.0062  0.0860  400  VAL A CG2 
2923  N N   . SER A 403  ? 0.2226 0.2043 0.3210 -0.0010 0.0124  0.0719  401  SER A N   
2924  C CA  . SER A 403  ? 0.2321 0.2172 0.3234 -0.0004 0.0144  0.0699  401  SER A CA  
2925  C C   . SER A 403  ? 0.2306 0.2121 0.3236 -0.0012 0.0135  0.0647  401  SER A C   
2926  O O   . SER A 403  ? 0.2051 0.1891 0.2988 -0.0019 0.0143  0.0655  401  SER A O   
2927  C CB  . SER A 403  ? 0.2463 0.2325 0.3271 0.0016  0.0158  0.0667  401  SER A CB  
2928  O OG  . SER A 403  ? 0.2162 0.2047 0.2908 0.0023  0.0173  0.0640  401  SER A OG  
2929  N N   . TYR A 404  ? 0.2132 0.1893 0.3075 -0.0012 0.0118  0.0594  402  TYR A N   
2930  C CA  . TYR A 404  ? 0.2148 0.1881 0.3106 -0.0019 0.0108  0.0541  402  TYR A CA  
2931  C C   . TYR A 404  ? 0.2162 0.1895 0.3215 -0.0037 0.0097  0.0568  402  TYR A C   
2932  O O   . TYR A 404  ? 0.2026 0.1773 0.3078 -0.0044 0.0101  0.0556  402  TYR A O   
2933  C CB  . TYR A 404  ? 0.2058 0.1742 0.3020 -0.0014 0.0090  0.0484  402  TYR A CB  
2934  C CG  . TYR A 404  ? 0.2076 0.1742 0.3031 -0.0017 0.0082  0.0422  402  TYR A CG  
2935  C CD1 . TYR A 404  ? 0.2076 0.1727 0.3113 -0.0032 0.0065  0.0410  402  TYR A CD1 
2936  C CD2 . TYR A 404  ? 0.1981 0.1648 0.2850 -0.0007 0.0091  0.0377  402  TYR A CD2 
2937  C CE1 . TYR A 404  ? 0.2188 0.1830 0.3216 -0.0034 0.0057  0.0353  402  TYR A CE1 
2938  C CE2 . TYR A 404  ? 0.2121 0.1778 0.2981 -0.0010 0.0083  0.0324  402  TYR A CE2 
2939  C CZ  . TYR A 404  ? 0.2074 0.1721 0.3012 -0.0023 0.0066  0.0312  402  TYR A CZ  
2940  O OH  . TYR A 404  ? 0.2277 0.1924 0.3208 -0.0026 0.0058  0.0260  402  TYR A OH  
2941  N N   . ILE A 405  ? 0.2265 0.1985 0.3409 -0.0047 0.0082  0.0607  403  ILE A N   
2942  C CA  . ILE A 405  ? 0.2454 0.2171 0.3701 -0.0067 0.0068  0.0633  403  ILE A CA  
2943  C C   . ILE A 405  ? 0.2005 0.1780 0.3245 -0.0074 0.0087  0.0690  403  ILE A C   
2944  O O   . ILE A 405  ? 0.2208 0.1992 0.3488 -0.0087 0.0085  0.0690  403  ILE A O   
2945  C CB  . ILE A 405  ? 0.2329 0.2015 0.3681 -0.0076 0.0044  0.0663  403  ILE A CB  
2946  C CG1 . ILE A 405  ? 0.2820 0.2451 0.4182 -0.0068 0.0023  0.0594  403  ILE A CG1 
2947  C CG2 . ILE A 405  ? 0.2693 0.2376 0.4159 -0.0098 0.0028  0.0696  403  ILE A CG2 
2948  C CD1 . ILE A 405  ? 0.3618 0.3216 0.5068 -0.0070 0.0001  0.0616  403  ILE A CD1 
2949  N N   . ALA A 406  ? 0.2245 0.2067 0.3432 -0.0065 0.0107  0.0737  404  ALA A N   
2950  C CA  . ALA A 406  ? 0.2132 0.2021 0.3303 -0.0068 0.0128  0.0788  404  ALA A CA  
2951  C C   . ALA A 406  ? 0.2347 0.2249 0.3454 -0.0062 0.0142  0.0742  404  ALA A C   
2952  O O   . ALA A 406  ? 0.2467 0.2402 0.3600 -0.0072 0.0148  0.0763  404  ALA A O   
2953  C CB  . ALA A 406  ? 0.2222 0.2164 0.3333 -0.0055 0.0148  0.0831  404  ALA A CB  
2954  N N   . CYS A 407  ? 0.2293 0.2172 0.3316 -0.0045 0.0146  0.0683  405  CYS A N   
2955  C CA  . CYS A 407  ? 0.2107 0.1997 0.3070 -0.0038 0.0156  0.0641  405  CYS A CA  
2956  C C   . CYS A 407  ? 0.2278 0.2136 0.3295 -0.0052 0.0140  0.0606  405  CYS A C   
2957  O O   . CYS A 407  ? 0.2142 0.2023 0.3146 -0.0054 0.0147  0.0598  405  CYS A O   
2958  C CB  . CYS A 407  ? 0.2220 0.2094 0.3088 -0.0019 0.0163  0.0593  405  CYS A CB  
2959  S SG  . CYS A 407  ? 0.2827 0.2756 0.3622 0.0000  0.0186  0.0630  405  CYS A SG  
2960  N N   . ALA A 408  ? 0.2140 0.1949 0.3221 -0.0061 0.0116  0.0585  406  ALA A N   
2961  C CA  . ALA A 408  ? 0.2161 0.1945 0.3302 -0.0075 0.0098  0.0552  406  ALA A CA  
2962  C C   . ALA A 408  ? 0.1963 0.1777 0.3183 -0.0093 0.0097  0.0602  406  ALA A C   
2963  O O   . ALA A 408  ? 0.2263 0.2083 0.3503 -0.0101 0.0093  0.0582  406  ALA A O   
2964  C CB  . ALA A 408  ? 0.2349 0.2080 0.3549 -0.0080 0.0072  0.0517  406  ALA A CB  
2965  N N   . ALA A 409  ? 0.2204 0.2040 0.3473 -0.0100 0.0100  0.0669  407  ALA A N   
2966  C CA  . ALA A 409  ? 0.2155 0.2028 0.3498 -0.0118 0.0101  0.0725  407  ALA A CA  
2967  C C   . ALA A 409  ? 0.2296 0.2226 0.3578 -0.0112 0.0126  0.0732  407  ALA A C   
2968  O O   . ALA A 409  ? 0.2348 0.2295 0.3675 -0.0125 0.0123  0.0738  407  ALA A O   
2969  C CB  . ALA A 409  ? 0.2318 0.2214 0.3715 -0.0126 0.0102  0.0803  407  ALA A CB  
2970  N N   . LYS A 410  ? 0.2383 0.2341 0.3564 -0.0092 0.0148  0.0728  408  LYS A N   
2971  C CA  . LYS A 410  ? 0.2177 0.2188 0.3299 -0.0082 0.0170  0.0728  408  LYS A CA  
2972  C C   . LYS A 410  ? 0.1919 0.1904 0.3021 -0.0081 0.0163  0.0666  408  LYS A C   
2973  O O   . LYS A 410  ? 0.2197 0.2216 0.3313 -0.0086 0.0169  0.0673  408  LYS A O   
2974  C CB  . LYS A 410  ? 0.2207 0.2247 0.3231 -0.0059 0.0190  0.0727  408  LYS A CB  
2975  C CG  . LYS A 410  ? 0.2474 0.2567 0.3433 -0.0044 0.0212  0.0719  408  LYS A CG  
2976  C CD  . LYS A 410  ? 0.2507 0.2624 0.3376 -0.0021 0.0228  0.0710  408  LYS A CD  
2977  C CE  . LYS A 410  ? 0.2659 0.2824 0.3537 -0.0020 0.0238  0.0771  408  LYS A CE  
2978  N NZ  . LYS A 410  ? 0.3015 0.3266 0.3914 -0.0023 0.0256  0.0823  408  LYS A NZ  
2979  N N   . LEU A 411  ? 0.1937 0.1869 0.3006 -0.0074 0.0150  0.0608  409  LEU A N   
2980  C CA  . LEU A 411  ? 0.1943 0.1854 0.2994 -0.0074 0.0142  0.0551  409  LEU A CA  
2981  C C   . LEU A 411  ? 0.2076 0.1978 0.3219 -0.0095 0.0123  0.0550  409  LEU A C   
2982  O O   . LEU A 411  ? 0.2069 0.1988 0.3211 -0.0098 0.0123  0.0532  409  LEU A O   
2983  C CB  . LEU A 411  ? 0.2040 0.1904 0.3047 -0.0065 0.0130  0.0495  409  LEU A CB  
2984  C CG  . LEU A 411  ? 0.2076 0.1948 0.2981 -0.0044 0.0148  0.0482  409  LEU A CG  
2985  C CD1 . LEU A 411  ? 0.2126 0.1954 0.2997 -0.0037 0.0137  0.0439  409  LEU A CD1 
2986  C CD2 . LEU A 411  ? 0.2079 0.1974 0.2932 -0.0035 0.0157  0.0459  409  LEU A CD2 
2987  N N   . LEU A 412  ? 0.2070 0.1946 0.3300 -0.0110 0.0105  0.0566  410  LEU A N   
2988  C CA  . LEU A 412  ? 0.2369 0.2233 0.3696 -0.0130 0.0083  0.0559  410  LEU A CA  
2989  C C   . LEU A 412  ? 0.2340 0.2253 0.3713 -0.0143 0.0093  0.0611  410  LEU A C   
2990  O O   . LEU A 412  ? 0.2606 0.2517 0.4044 -0.0158 0.0078  0.0600  410  LEU A O   
2991  C CB  . LEU A 412  ? 0.2440 0.2259 0.3855 -0.0141 0.0059  0.0562  410  LEU A CB  
2992  C CG  . LEU A 412  ? 0.2354 0.2125 0.3742 -0.0131 0.0043  0.0494  410  LEU A CG  
2993  C CD1 . LEU A 412  ? 0.2861 0.2592 0.4337 -0.0139 0.0021  0.0501  410  LEU A CD1 
2994  C CD2 . LEU A 412  ? 0.2525 0.2290 0.3916 -0.0134 0.0030  0.0431  410  LEU A CD2 
2995  N N   . ALA A 413  ? 0.2136 0.2097 0.3474 -0.0136 0.0117  0.0665  411  ALA A N   
2996  C CA  . ALA A 413  ? 0.2277 0.2298 0.3648 -0.0146 0.0130  0.0713  411  ALA A CA  
2997  C C   . ALA A 413  ? 0.2311 0.2363 0.3615 -0.0134 0.0144  0.0682  411  ALA A C   
2998  O O   . ALA A 413  ? 0.2545 0.2648 0.3875 -0.0140 0.0154  0.0713  411  ALA A O   
2999  C CB  . ALA A 413  ? 0.2228 0.2302 0.3592 -0.0143 0.0150  0.0784  411  ALA A CB  
3000  N N   . ALA A 414  ? 0.2195 0.2219 0.3419 -0.0116 0.0144  0.0624  412  ALA A N   
3001  C CA  . ALA A 414  ? 0.2283 0.2335 0.3438 -0.0102 0.0158  0.0599  412  ALA A CA  
3002  C C   . ALA A 414  ? 0.2129 0.2142 0.3268 -0.0101 0.0141  0.0534  412  ALA A C   
3003  O O   . ALA A 414  ? 0.2099 0.2117 0.3166 -0.0086 0.0148  0.0503  412  ALA A O   
3004  C CB  . ALA A 414  ? 0.2450 0.2522 0.3511 -0.0078 0.0180  0.0601  412  ALA A CB  
3005  N N   . THR A 415  ? 0.2215 0.2192 0.3424 -0.0118 0.0116  0.0513  413  THR A N   
3006  C CA  . THR A 415  ? 0.2330 0.2280 0.3525 -0.0118 0.0098  0.0451  413  THR A CA  
3007  C C   . THR A 415  ? 0.2475 0.2459 0.3661 -0.0118 0.0101  0.0439  413  THR A C   
3008  O O   . THR A 415  ? 0.2512 0.2485 0.3665 -0.0114 0.0091  0.0391  413  THR A O   
3009  C CB  . THR A 415  ? 0.2632 0.2544 0.3910 -0.0135 0.0070  0.0426  413  THR A CB  
3010  O OG1 . THR A 415  ? 0.2761 0.2690 0.4138 -0.0155 0.0062  0.0460  413  THR A OG1 
3011  C CG2 . THR A 415  ? 0.2549 0.2425 0.3835 -0.0132 0.0066  0.0432  413  THR A CG2 
3012  N N   . ASP A 416  ? 0.2367 0.2395 0.3582 -0.0123 0.0114  0.0483  414  ASP A N   
3013  C CA  . ASP A 416  ? 0.2423 0.2486 0.3625 -0.0120 0.0118  0.0473  414  ASP A CA  
3014  C C   . ASP A 416  ? 0.2427 0.2500 0.3529 -0.0095 0.0134  0.0455  414  ASP A C   
3015  O O   . ASP A 416  ? 0.3177 0.3260 0.4254 -0.0090 0.0130  0.0428  414  ASP A O   
3016  C CB  . ASP A 416  ? 0.2508 0.2621 0.3770 -0.0131 0.0128  0.0524  414  ASP A CB  
3017  C CG  . ASP A 416  ? 0.3567 0.3718 0.4802 -0.0121 0.0153  0.0575  414  ASP A CG  
3018  O OD1 . ASP A 416  ? 0.3119 0.3248 0.4336 -0.0117 0.0157  0.0587  414  ASP A OD1 
3019  O OD2 . ASP A 416  ? 0.4143 0.4350 0.5374 -0.0116 0.0170  0.0602  414  ASP A OD2 
3020  N N   . VAL A 417  ? 0.2241 0.2312 0.3290 -0.0081 0.0149  0.0470  415  VAL A N   
3021  C CA  . VAL A 417  ? 0.2521 0.2604 0.3486 -0.0057 0.0164  0.0456  415  VAL A CA  
3022  C C   . VAL A 417  ? 0.2240 0.2280 0.3140 -0.0046 0.0160  0.0423  415  VAL A C   
3023  O O   . VAL A 417  ? 0.2416 0.2457 0.3252 -0.0029 0.0166  0.0402  415  VAL A O   
3024  C CB  . VAL A 417  ? 0.2886 0.3021 0.3833 -0.0045 0.0189  0.0496  415  VAL A CB  
3025  C CG1 . VAL A 417  ? 0.2924 0.3110 0.3928 -0.0054 0.0193  0.0525  415  VAL A CG1 
3026  C CG2 . VAL A 417  ? 0.2657 0.2791 0.3610 -0.0046 0.0197  0.0530  415  VAL A CG2 
3027  N N   . VAL A 418  ? 0.2061 0.2064 0.2979 -0.0054 0.0150  0.0419  416  VAL A N   
3028  C CA  . VAL A 418  ? 0.2008 0.1972 0.2872 -0.0046 0.0144  0.0384  416  VAL A CA  
3029  C C   . VAL A 418  ? 0.1842 0.1771 0.2751 -0.0061 0.0121  0.0353  416  VAL A C   
3030  O O   . VAL A 418  ? 0.1972 0.1901 0.2958 -0.0077 0.0111  0.0365  416  VAL A O   
3031  C CB  . VAL A 418  ? 0.2030 0.1987 0.2858 -0.0035 0.0157  0.0403  416  VAL A CB  
3032  C CG1 . VAL A 418  ? 0.2387 0.2382 0.3163 -0.0016 0.0179  0.0422  416  VAL A CG1 
3033  C CG2 . VAL A 418  ? 0.2118 0.2075 0.3011 -0.0048 0.0156  0.0441  416  VAL A CG2 
3034  N N   . PHE A 419  ? 0.1817 0.1719 0.2679 -0.0055 0.0113  0.0314  417  PHE A N   
3035  C CA  . PHE A 419  ? 0.1957 0.1832 0.2853 -0.0065 0.0092  0.0277  417  PHE A CA  
3036  C C   . PHE A 419  ? 0.1788 0.1633 0.2667 -0.0060 0.0093  0.0276  417  PHE A C   
3037  O O   . PHE A 419  ? 0.1986 0.1821 0.2796 -0.0048 0.0098  0.0257  417  PHE A O   
3038  C CB  . PHE A 419  ? 0.1973 0.1852 0.2829 -0.0063 0.0081  0.0232  417  PHE A CB  
3039  C CG  . PHE A 419  ? 0.2020 0.1881 0.2899 -0.0070 0.0060  0.0187  417  PHE A CG  
3040  C CD1 . PHE A 419  ? 0.1993 0.1851 0.2956 -0.0085 0.0043  0.0176  417  PHE A CD1 
3041  C CD2 . PHE A 419  ? 0.1907 0.1759 0.2730 -0.0062 0.0057  0.0155  417  PHE A CD2 
3042  C CE1 . PHE A 419  ? 0.1822 0.1669 0.2810 -0.0090 0.0022  0.0128  417  PHE A CE1 
3043  C CE2 . PHE A 419  ? 0.1989 0.1835 0.2834 -0.0068 0.0039  0.0111  417  PHE A CE2 
3044  C CZ  . PHE A 419  ? 0.2060 0.1904 0.2986 -0.0080 0.0021  0.0095  417  PHE A CZ  
3045  N N   . PRO A 420  ? 0.1804 0.1635 0.2745 -0.0068 0.0088  0.0297  418  PRO A N   
3046  C CA  . PRO A 420  ? 0.1815 0.1619 0.2742 -0.0062 0.0088  0.0298  418  PRO A CA  
3047  C C   . PRO A 420  ? 0.1832 0.1610 0.2756 -0.0062 0.0070  0.0243  418  PRO A C   
3048  O O   . PRO A 420  ? 0.1974 0.1750 0.2948 -0.0072 0.0052  0.0211  418  PRO A O   
3049  C CB  . PRO A 420  ? 0.1682 0.1480 0.2692 -0.0074 0.0084  0.0339  418  PRO A CB  
3050  C CG  . PRO A 420  ? 0.1819 0.1652 0.2866 -0.0082 0.0091  0.0373  418  PRO A CG  
3051  C CD  . PRO A 420  ? 0.1946 0.1786 0.2976 -0.0084 0.0082  0.0329  418  PRO A CD  
3052  N N   . GLN A 421  ? 0.1867 0.1631 0.2735 -0.0050 0.0076  0.0232  419  GLN A N   
3053  C CA  . GLN A 421  ? 0.1818 0.1565 0.2673 -0.0048 0.0062  0.0182  419  GLN A CA  
3054  C C   . GLN A 421  ? 0.1863 0.1585 0.2721 -0.0042 0.0063  0.0193  419  GLN A C   
3055  O O   . GLN A 421  ? 0.2184 0.1906 0.2984 -0.0032 0.0079  0.0213  419  GLN A O   
3056  C CB  . GLN A 421  ? 0.1775 0.1536 0.2544 -0.0039 0.0069  0.0158  419  GLN A CB  
3057  C CG  . GLN A 421  ? 0.1862 0.1650 0.2627 -0.0044 0.0067  0.0152  419  GLN A CG  
3058  C CD  . GLN A 421  ? 0.1898 0.1699 0.2582 -0.0035 0.0076  0.0145  419  GLN A CD  
3059  O OE1 . GLN A 421  ? 0.2130 0.1929 0.2769 -0.0024 0.0092  0.0171  419  GLN A OE1 
3060  N NE2 . GLN A 421  ? 0.2012 0.1830 0.2682 -0.0038 0.0065  0.0111  419  GLN A NE2 
3061  N N   . PHE A 422  ? 0.1842 0.1543 0.2774 -0.0049 0.0045  0.0179  420  PHE A N   
3062  C CA  . PHE A 422  ? 0.1596 0.1273 0.2548 -0.0044 0.0044  0.0197  420  PHE A CA  
3063  C C   . PHE A 422  ? 0.1737 0.1402 0.2658 -0.0036 0.0036  0.0148  420  PHE A C   
3064  O O   . PHE A 422  ? 0.2004 0.1660 0.2977 -0.0039 0.0016  0.0105  420  PHE A O   
3065  C CB  . PHE A 422  ? 0.1956 0.1617 0.3015 -0.0056 0.0029  0.0219  420  PHE A CB  
3066  C CG  . PHE A 422  ? 0.1975 0.1656 0.3066 -0.0066 0.0038  0.0272  420  PHE A CG  
3067  C CD1 . PHE A 422  ? 0.2171 0.1870 0.3220 -0.0060 0.0060  0.0326  420  PHE A CD1 
3068  C CD2 . PHE A 422  ? 0.2122 0.1810 0.3278 -0.0080 0.0026  0.0265  420  PHE A CD2 
3069  C CE1 . PHE A 422  ? 0.2393 0.2119 0.3469 -0.0068 0.0070  0.0375  420  PHE A CE1 
3070  C CE2 . PHE A 422  ? 0.2229 0.1940 0.3414 -0.0089 0.0035  0.0315  420  PHE A CE2 
3071  C CZ  . PHE A 422  ? 0.2175 0.1907 0.3319 -0.0083 0.0058  0.0371  420  PHE A CZ  
3072  N N   . ALA A 423  ? 0.1814 0.1483 0.2654 -0.0024 0.0052  0.0153  421  ALA A N   
3073  C CA  . ALA A 423  ? 0.1720 0.1383 0.2521 -0.0016 0.0047  0.0112  421  ALA A CA  
3074  C C   . ALA A 423  ? 0.2147 0.1786 0.2983 -0.0011 0.0043  0.0125  421  ALA A C   
3075  O O   . ALA A 423  ? 0.2453 0.2088 0.3265 -0.0005 0.0056  0.0167  421  ALA A O   
3076  C CB  . ALA A 423  ? 0.1922 0.1600 0.2627 -0.0007 0.0064  0.0116  421  ALA A CB  
3077  N N   . THR A 424  ? 0.1966 0.1592 0.2860 -0.0012 0.0023  0.0086  422  THR A N   
3078  C CA  . THR A 424  ? 0.2058 0.1659 0.2988 -0.0006 0.0016  0.0093  422  THR A CA  
3079  C C   . THR A 424  ? 0.2119 0.1714 0.3097 -0.0003 -0.0006 0.0032  422  THR A C   
3080  O O   . THR A 424  ? 0.2302 0.1906 0.3322 -0.0010 -0.0021 -0.0006 422  THR A O   
3081  C CB  . THR A 424  ? 0.2368 0.1952 0.3374 -0.0013 0.0012  0.0148  422  THR A CB  
3082  O OG1 . THR A 424  ? 0.2350 0.1912 0.3390 -0.0006 0.0004  0.0158  422  THR A OG1 
3083  C CG2 . THR A 424  ? 0.2423 0.2000 0.3522 -0.0025 -0.0007 0.0134  422  THR A CG2 
3084  N N   . HIS A 425  ? 0.2188 0.1771 0.3161 0.0007  -0.0009 0.0019  423  HIS A N   
3085  C CA  . HIS A 425  ? 0.2293 0.1870 0.3325 0.0012  -0.0031 -0.0037 423  HIS A CA  
3086  C C   . HIS A 425  ? 0.2488 0.2030 0.3620 0.0013  -0.0048 -0.0017 423  HIS A C   
3087  O O   . HIS A 425  ? 0.2730 0.2262 0.3922 0.0019  -0.0069 -0.0062 423  HIS A O   
3088  C CB  . HIS A 425  ? 0.2163 0.1756 0.3128 0.0024  -0.0025 -0.0071 423  HIS A CB  
3089  C CG  . HIS A 425  ? 0.2397 0.2026 0.3273 0.0023  -0.0012 -0.0091 423  HIS A CG  
3090  N ND1 . HIS A 425  ? 0.2602 0.2243 0.3389 0.0028  0.0006  -0.0078 423  HIS A ND1 
3091  C CD2 . HIS A 425  ? 0.2319 0.1976 0.3186 0.0015  -0.0015 -0.0119 423  HIS A CD2 
3092  C CE1 . HIS A 425  ? 0.2728 0.2400 0.3457 0.0024  0.0012  -0.0095 423  HIS A CE1 
3093  N NE2 . HIS A 425  ? 0.2437 0.2121 0.3211 0.0017  0.0000  -0.0119 423  HIS A NE2 
3094  N N   . ASN A 426  ? 0.2414 0.1941 0.3569 0.0006  -0.0041 0.0051  424  ASN A N   
3095  C CA  . ASN A 426  ? 0.2467 0.1962 0.3712 0.0006  -0.0056 0.0086  424  ASN A CA  
3096  C C   . ASN A 426  ? 0.2582 0.2063 0.3939 -0.0007 -0.0078 0.0083  424  ASN A C   
3097  O O   . ASN A 426  ? 0.2495 0.1985 0.3857 -0.0020 -0.0070 0.0119  424  ASN A O   
3098  C CB  . ASN A 426  ? 0.2609 0.2108 0.3816 0.0005  -0.0036 0.0163  424  ASN A CB  
3099  C CG  . ASN A 426  ? 0.2537 0.2011 0.3831 0.0005  -0.0050 0.0210  424  ASN A CG  
3100  O OD1 . ASN A 426  ? 0.2938 0.2389 0.4340 -0.0003 -0.0073 0.0210  424  ASN A OD1 
3101  N ND2 . ASN A 426  ? 0.2537 0.2015 0.3785 0.0013  -0.0037 0.0252  424  ASN A ND2 
3102  N N   . ALA A 427  ? 0.2533 0.1992 0.3982 -0.0004 -0.0105 0.0039  425  ALA A N   
3103  C CA  . ALA A 427  ? 0.2635 0.2079 0.4198 -0.0016 -0.0131 0.0025  425  ALA A CA  
3104  C C   . ALA A 427  ? 0.2291 0.1715 0.3926 -0.0030 -0.0133 0.0107  425  ALA A C   
3105  O O   . ALA A 427  ? 0.2550 0.1972 0.4251 -0.0045 -0.0143 0.0116  425  ALA A O   
3106  C CB  . ALA A 427  ? 0.2821 0.2243 0.4475 -0.0006 -0.0162 -0.0040 425  ALA A CB  
3107  N N   . GLN A 428  ? 0.2516 0.1930 0.4141 -0.0026 -0.0124 0.0168  426  GLN A N   
3108  C CA  . GLN A 428  ? 0.2991 0.2399 0.4678 -0.0040 -0.0124 0.0253  426  GLN A CA  
3109  C C   . GLN A 428  ? 0.2447 0.1890 0.4063 -0.0050 -0.0097 0.0295  426  GLN A C   
3110  O O   . GLN A 428  ? 0.2533 0.1979 0.4213 -0.0066 -0.0102 0.0333  426  GLN A O   
3111  C CB  . GLN A 428  ? 0.2629 0.2029 0.4310 -0.0032 -0.0119 0.0308  426  GLN A CB  
3112  C CG  . GLN A 428  ? 0.2765 0.2156 0.4542 -0.0046 -0.0128 0.0395  426  GLN A CG  
3113  C CD  . GLN A 428  ? 0.3423 0.2853 0.5150 -0.0058 -0.0102 0.0466  426  GLN A CD  
3114  O OE1 . GLN A 428  ? 0.3315 0.2780 0.4922 -0.0051 -0.0073 0.0469  426  GLN A OE1 
3115  N NE2 . GLN A 428  ? 0.2964 0.2394 0.4790 -0.0077 -0.0114 0.0523  426  GLN A NE2 
3116  N N   . THR A 429  ? 0.2488 0.1959 0.3976 -0.0040 -0.0070 0.0287  427  THR A N   
3117  C CA  . THR A 429  ? 0.2451 0.1956 0.3868 -0.0046 -0.0045 0.0318  427  THR A CA  
3118  C C   . THR A 429  ? 0.2298 0.1808 0.3747 -0.0058 -0.0054 0.0281  427  THR A C   
3119  O O   . THR A 429  ? 0.2399 0.1925 0.3874 -0.0071 -0.0049 0.0322  427  THR A O   
3120  C CB  . THR A 429  ? 0.2663 0.2191 0.3947 -0.0032 -0.0020 0.0299  427  THR A CB  
3121  O OG1 . THR A 429  ? 0.2581 0.2103 0.3837 -0.0021 -0.0015 0.0323  427  THR A OG1 
3122  C CG2 . THR A 429  ? 0.2711 0.2275 0.3929 -0.0036 0.0005  0.0338  427  THR A CG2 
3123  N N   . LEU A 430  ? 0.2364 0.1867 0.3812 -0.0052 -0.0068 0.0203  428  LEU A N   
3124  C CA  . LEU A 430  ? 0.2552 0.2065 0.4029 -0.0061 -0.0079 0.0161  428  LEU A CA  
3125  C C   . LEU A 430  ? 0.2449 0.1943 0.4056 -0.0078 -0.0101 0.0186  428  LEU A C   
3126  O O   . LEU A 430  ? 0.2489 0.2000 0.4114 -0.0092 -0.0098 0.0205  428  LEU A O   
3127  C CB  . LEU A 430  ? 0.2249 0.1761 0.3718 -0.0051 -0.0094 0.0072  428  LEU A CB  
3128  C CG  . LEU A 430  ? 0.2808 0.2345 0.4274 -0.0055 -0.0103 0.0010  428  LEU A CG  
3129  C CD1 . LEU A 430  ? 0.3261 0.2809 0.4690 -0.0041 -0.0110 -0.0065 428  LEU A CD1 
3130  C CD2 . LEU A 430  ? 0.2933 0.2455 0.4522 -0.0069 -0.0130 -0.0003 428  LEU A CD2 
3131  N N   . ALA A 431  ? 0.2601 0.2061 0.4307 -0.0078 -0.0125 0.0186  429  ALA A N   
3132  C CA  . ALA A 431  ? 0.2678 0.2116 0.4523 -0.0094 -0.0151 0.0207  429  ALA A CA  
3133  C C   . ALA A 431  ? 0.2611 0.2064 0.4471 -0.0110 -0.0136 0.0300  429  ALA A C   
3134  O O   . ALA A 431  ? 0.2522 0.1980 0.4452 -0.0127 -0.0146 0.0316  429  ALA A O   
3135  C CB  . ALA A 431  ? 0.2520 0.1916 0.4465 -0.0089 -0.0179 0.0199  429  ALA A CB  
3136  N N   . ALA A 432  ? 0.2596 0.2063 0.4393 -0.0104 -0.0113 0.0362  430  ALA A N   
3137  C CA  . ALA A 432  ? 0.2868 0.2362 0.4671 -0.0117 -0.0096 0.0451  430  ALA A CA  
3138  C C   . ALA A 432  ? 0.2514 0.2045 0.4264 -0.0125 -0.0078 0.0450  430  ALA A C   
3139  O O   . ALA A 432  ? 0.2765 0.2313 0.4575 -0.0142 -0.0079 0.0499  430  ALA A O   
3140  C CB  . ALA A 432  ? 0.2727 0.2240 0.4448 -0.0106 -0.0072 0.0503  430  ALA A CB  
3141  N N   . ILE A 433  ? 0.2478 0.2024 0.4121 -0.0112 -0.0063 0.0395  431  ILE A N   
3142  C CA  . ILE A 433  ? 0.2510 0.2091 0.4097 -0.0117 -0.0046 0.0394  431  ILE A CA  
3143  C C   . ILE A 433  ? 0.2352 0.1926 0.4015 -0.0130 -0.0069 0.0350  431  ILE A C   
3144  O O   . ILE A 433  ? 0.2315 0.1912 0.3999 -0.0143 -0.0064 0.0376  431  ILE A O   
3145  C CB  . ILE A 433  ? 0.2747 0.2346 0.4199 -0.0099 -0.0024 0.0357  431  ILE A CB  
3146  C CG1 . ILE A 433  ? 0.2690 0.2304 0.4072 -0.0089 -0.0001 0.0408  431  ILE A CG1 
3147  C CG2 . ILE A 433  ? 0.2657 0.2287 0.4060 -0.0103 -0.0012 0.0340  431  ILE A CG2 
3148  C CD1 . ILE A 433  ? 0.2950 0.2575 0.4212 -0.0072 0.0017  0.0374  431  ILE A CD1 
3149  N N   . TYR A 434  ? 0.2562 0.2107 0.4270 -0.0126 -0.0094 0.0281  432  TYR A N   
3150  C CA  . TYR A 434  ? 0.2651 0.2190 0.4440 -0.0137 -0.0120 0.0233  432  TYR A CA  
3151  C C   . TYR A 434  ? 0.2800 0.2331 0.4712 -0.0158 -0.0135 0.0289  432  TYR A C   
3152  O O   . TYR A 434  ? 0.2733 0.2283 0.4680 -0.0172 -0.0139 0.0287  432  TYR A O   
3153  C CB  . TYR A 434  ? 0.2594 0.2105 0.4425 -0.0127 -0.0147 0.0155  432  TYR A CB  
3154  C CG  . TYR A 434  ? 0.2891 0.2394 0.4831 -0.0138 -0.0179 0.0103  432  TYR A CG  
3155  C CD1 . TYR A 434  ? 0.3009 0.2542 0.4918 -0.0141 -0.0180 0.0056  432  TYR A CD1 
3156  C CD2 . TYR A 434  ? 0.3184 0.2647 0.5260 -0.0144 -0.0212 0.0099  432  TYR A CD2 
3157  C CE1 . TYR A 434  ? 0.2973 0.2502 0.4982 -0.0150 -0.0211 0.0004  432  TYR A CE1 
3158  C CE2 . TYR A 434  ? 0.3412 0.2867 0.5594 -0.0153 -0.0244 0.0046  432  TYR A CE2 
3159  C CZ  . TYR A 434  ? 0.3517 0.3006 0.5663 -0.0156 -0.0244 -0.0003 432  TYR A CZ  
3160  O OH  . TYR A 434  ? 0.3904 0.3389 0.6157 -0.0164 -0.0277 -0.0059 432  TYR A OH  
3161  N N   . HIS A 435  ? 0.2862 0.2368 0.4845 -0.0163 -0.0143 0.0341  433  HIS A N   
3162  C CA  . HIS A 435  ? 0.2908 0.2409 0.5016 -0.0185 -0.0158 0.0402  433  HIS A CA  
3163  C C   . HIS A 435  ? 0.2826 0.2373 0.4889 -0.0195 -0.0128 0.0485  433  HIS A C   
3164  O O   . HIS A 435  ? 0.2767 0.2328 0.4906 -0.0215 -0.0134 0.0521  433  HIS A O   
3165  C CB  . HIS A 435  ? 0.3216 0.2675 0.5428 -0.0187 -0.0181 0.0432  433  HIS A CB  
3166  C CG  . HIS A 435  ? 0.3305 0.2722 0.5601 -0.0182 -0.0218 0.0350  433  HIS A CG  
3167  N ND1 . HIS A 435  ? 0.3438 0.2835 0.5863 -0.0197 -0.0251 0.0322  433  HIS A ND1 
3168  C CD2 . HIS A 435  ? 0.3148 0.2542 0.5413 -0.0161 -0.0226 0.0285  433  HIS A CD2 
3169  C CE1 . HIS A 435  ? 0.3328 0.2693 0.5803 -0.0185 -0.0279 0.0241  433  HIS A CE1 
3170  N NE2 . HIS A 435  ? 0.3039 0.2403 0.5417 -0.0163 -0.0264 0.0218  433  HIS A NE2 
3171  N N   . MET A 436  ? 0.2671 0.2245 0.4614 -0.0180 -0.0096 0.0511  434  MET A N   
3172  C CA  . MET A 436  ? 0.2744 0.2370 0.4636 -0.0186 -0.0066 0.0578  434  MET A CA  
3173  C C   . MET A 436  ? 0.2702 0.2356 0.4567 -0.0191 -0.0060 0.0549  434  MET A C   
3174  O O   . MET A 436  ? 0.2822 0.2513 0.4714 -0.0205 -0.0050 0.0602  434  MET A O   
3175  C CB  . MET A 436  ? 0.2522 0.2171 0.4285 -0.0166 -0.0036 0.0594  434  MET A CB  
3176  C CG  . MET A 436  ? 0.2737 0.2446 0.4446 -0.0168 -0.0005 0.0660  434  MET A CG  
3177  S SD  . MET A 436  ? 0.2768 0.2502 0.4323 -0.0142 0.0027  0.0657  434  MET A SD  
3178  C CE  . MET A 436  ? 0.3128 0.2845 0.4718 -0.0139 0.0020  0.0704  434  MET A CE  
3179  N N   . ALA A 437  ? 0.2664 0.2307 0.4476 -0.0180 -0.0065 0.0468  435  ALA A N   
3180  C CA  . ALA A 437  ? 0.2968 0.2639 0.4745 -0.0184 -0.0058 0.0440  435  ALA A CA  
3181  C C   . ALA A 437  ? 0.3252 0.2917 0.5152 -0.0205 -0.0085 0.0433  435  ALA A C   
3182  O O   . ALA A 437  ? 0.3343 0.3041 0.5242 -0.0214 -0.0078 0.0441  435  ALA A O   
3183  C CB  . ALA A 437  ? 0.2965 0.2631 0.4653 -0.0167 -0.0057 0.0359  435  ALA A CB  
3184  N N   . GLY A 438  ? 0.3531 0.3155 0.5543 -0.0213 -0.0116 0.0417  436  GLY A N   
3185  C CA  . GLY A 438  ? 0.3846 0.3460 0.5989 -0.0235 -0.0145 0.0414  436  GLY A CA  
3186  C C   . GLY A 438  ? 0.3971 0.3579 0.6128 -0.0233 -0.0167 0.0321  436  GLY A C   
3187  O O   . GLY A 438  ? 0.3868 0.3480 0.5933 -0.0215 -0.0161 0.0258  436  GLY A O   
3188  N N   . LYS A 439  ? 0.4466 0.4068 0.6742 -0.0253 -0.0193 0.0316  437  LYS A N   
3189  C CA  . LYS A 439  ? 0.4972 0.4567 0.7289 -0.0253 -0.0222 0.0225  437  LYS A CA  
3190  C C   . LYS A 439  ? 0.4304 0.3945 0.6545 -0.0252 -0.0208 0.0197  437  LYS A C   
3191  O O   . LYS A 439  ? 0.5201 0.4851 0.7421 -0.0244 -0.0222 0.0116  437  LYS A O   
3192  C CB  . LYS A 439  ? 0.5430 0.4997 0.7920 -0.0274 -0.0260 0.0225  437  LYS A CB  
3193  N N   . ASP A 440  ? 0.4157 0.3834 0.6358 -0.0259 -0.0182 0.0262  438  ASP A N   
3194  C CA  . ASP A 440  ? 0.4738 0.4459 0.6862 -0.0256 -0.0168 0.0239  438  ASP A CA  
3195  C C   . ASP A 440  ? 0.4466 0.4198 0.6445 -0.0232 -0.0146 0.0204  438  ASP A C   
3196  O O   . ASP A 440  ? 0.4588 0.4323 0.6489 -0.0221 -0.0119 0.0248  438  ASP A O   
3197  C CB  . ASP A 440  ? 0.4986 0.4744 0.7106 -0.0268 -0.0144 0.0319  438  ASP A CB  
3198  C CG  . ASP A 440  ? 0.5548 0.5309 0.7807 -0.0295 -0.0166 0.0346  438  ASP A CG  
3199  O OD1 . ASP A 440  ? 0.5251 0.4980 0.7614 -0.0304 -0.0202 0.0301  438  ASP A OD1 
3200  O OD2 . ASP A 440  ? 0.6055 0.5852 0.8322 -0.0306 -0.0149 0.0410  438  ASP A OD2 
3201  N N   . PHE A 441  ? 0.3336 0.3079 0.5282 -0.0224 -0.0159 0.0126  439  PHE A N   
3202  C CA  . PHE A 441  ? 0.3343 0.3101 0.5157 -0.0203 -0.0140 0.0095  439  PHE A CA  
3203  C C   . PHE A 441  ? 0.3235 0.3033 0.5006 -0.0201 -0.0144 0.0045  439  PHE A C   
3204  O O   . PHE A 441  ? 0.3522 0.3329 0.5367 -0.0211 -0.0171 -0.0001 439  PHE A O   
3205  C CB  . PHE A 441  ? 0.2765 0.2494 0.4565 -0.0189 -0.0150 0.0048  439  PHE A CB  
3206  C CG  . PHE A 441  ? 0.2833 0.2579 0.4498 -0.0170 -0.0129 0.0026  439  PHE A CG  
3207  C CD1 . PHE A 441  ? 0.2615 0.2356 0.4199 -0.0160 -0.0100 0.0077  439  PHE A CD1 
3208  C CD2 . PHE A 441  ? 0.2930 0.2703 0.4552 -0.0162 -0.0139 -0.0045 439  PHE A CD2 
3209  C CE1 . PHE A 441  ? 0.2553 0.2308 0.4022 -0.0144 -0.0083 0.0059  439  PHE A CE1 
3210  C CE2 . PHE A 441  ? 0.2784 0.2575 0.4288 -0.0147 -0.0120 -0.0058 439  PHE A CE2 
3211  C CZ  . PHE A 441  ? 0.2529 0.2308 0.3959 -0.0138 -0.0093 -0.0006 439  PHE A CZ  
3212  N N   . HIS A 442  ? 0.2961 0.2785 0.4615 -0.0189 -0.0119 0.0053  440  HIS A N   
3213  C CA  . HIS A 442  ? 0.3069 0.2932 0.4663 -0.0183 -0.0122 0.0006  440  HIS A CA  
3214  C C   . HIS A 442  ? 0.3215 0.3083 0.4686 -0.0164 -0.0101 0.0000  440  HIS A C   
3215  O O   . HIS A 442  ? 0.2593 0.2443 0.4017 -0.0157 -0.0078 0.0047  440  HIS A O   
3216  C CB  . HIS A 442  ? 0.2890 0.2787 0.4485 -0.0192 -0.0113 0.0038  440  HIS A CB  
3217  C CG  . HIS A 442  ? 0.2430 0.2334 0.3967 -0.0187 -0.0081 0.0107  440  HIS A CG  
3218  N ND1 . HIS A 442  ? 0.2958 0.2851 0.4548 -0.0196 -0.0071 0.0170  440  HIS A ND1 
3219  C CD2 . HIS A 442  ? 0.2859 0.2782 0.4291 -0.0172 -0.0058 0.0121  440  HIS A CD2 
3220  C CE1 . HIS A 442  ? 0.2741 0.2651 0.4258 -0.0187 -0.0042 0.0217  440  HIS A CE1 
3221  N NE2 . HIS A 442  ? 0.2879 0.2804 0.4302 -0.0172 -0.0034 0.0186  440  HIS A NE2 
3222  N N   . VAL A 443  ? 0.3258 0.3155 0.4680 -0.0157 -0.0109 -0.0056 441  VAL A N   
3223  C CA  . VAL A 443  ? 0.3494 0.3400 0.4802 -0.0141 -0.0091 -0.0059 441  VAL A CA  
3224  C C   . VAL A 443  ? 0.2955 0.2874 0.4201 -0.0138 -0.0066 -0.0004 441  VAL A C   
3225  O O   . VAL A 443  ? 0.2942 0.2888 0.4203 -0.0145 -0.0067 0.0007  441  VAL A O   
3226  C CB  . VAL A 443  ? 0.3712 0.3657 0.4983 -0.0136 -0.0106 -0.0125 441  VAL A CB  
3227  C CG1 . VAL A 443  ? 0.3798 0.3761 0.4954 -0.0124 -0.0086 -0.0115 441  VAL A CG1 
3228  C CG2 . VAL A 443  ? 0.4249 0.4181 0.5564 -0.0134 -0.0126 -0.0181 441  VAL A CG2 
3229  N N   . GLY A 444  ? 0.2802 0.2703 0.3981 -0.0126 -0.0043 0.0029  442  GLY A N   
3230  C CA  . GLY A 444  ? 0.2330 0.2239 0.3460 -0.0121 -0.0019 0.0081  442  GLY A CA  
3231  C C   . GLY A 444  ? 0.2001 0.1889 0.3166 -0.0124 -0.0005 0.0137  442  GLY A C   
3232  O O   . GLY A 444  ? 0.2136 0.2033 0.3253 -0.0115 0.0017  0.0178  442  GLY A O   
3233  N N   . LYS A 445  ? 0.2093 0.1959 0.3346 -0.0135 -0.0018 0.0141  443  LYS A N   
3234  C CA  . LYS A 445  ? 0.2021 0.1874 0.3308 -0.0139 -0.0005 0.0201  443  LYS A CA  
3235  C C   . LYS A 445  ? 0.2331 0.2163 0.3558 -0.0125 0.0010  0.0216  443  LYS A C   
3236  O O   . LYS A 445  ? 0.2206 0.2048 0.3389 -0.0117 0.0033  0.0261  443  LYS A O   
3237  C CB  . LYS A 445  ? 0.2275 0.2109 0.3680 -0.0156 -0.0026 0.0206  443  LYS A CB  
3238  C CG  . LYS A 445  ? 0.2833 0.2666 0.4281 -0.0163 -0.0013 0.0278  443  LYS A CG  
3239  C CD  . LYS A 445  ? 0.3573 0.3387 0.5148 -0.0182 -0.0036 0.0291  443  LYS A CD  
3240  C CE  . LYS A 445  ? 0.4152 0.3989 0.5772 -0.0194 -0.0022 0.0368  443  LYS A CE  
3241  N NZ  . LYS A 445  ? 0.4458 0.4276 0.6212 -0.0215 -0.0046 0.0388  443  LYS A NZ  
3242  N N   . TYR A 446  ? 0.2210 0.2016 0.3433 -0.0120 -0.0003 0.0176  444  TYR A N   
3243  C CA  . TYR A 446  ? 0.2172 0.1958 0.3335 -0.0106 0.0009  0.0181  444  TYR A CA  
3244  C C   . TYR A 446  ? 0.2144 0.1918 0.3298 -0.0102 -0.0008 0.0117  444  TYR A C   
3245  O O   . TYR A 446  ? 0.2068 0.1850 0.3271 -0.0109 -0.0029 0.0074  444  TYR A O   
3246  C CB  . TYR A 446  ? 0.2100 0.1865 0.3310 -0.0109 0.0014  0.0230  444  TYR A CB  
3247  C CG  . TYR A 446  ? 0.2478 0.2212 0.3785 -0.0119 -0.0011 0.0212  444  TYR A CG  
3248  C CD1 . TYR A 446  ? 0.2923 0.2631 0.4220 -0.0110 -0.0019 0.0182  444  TYR A CD1 
3249  C CD2 . TYR A 446  ? 0.3246 0.2978 0.4660 -0.0136 -0.0028 0.0226  444  TYR A CD2 
3250  C CE1 . TYR A 446  ? 0.3424 0.3102 0.4813 -0.0116 -0.0043 0.0163  444  TYR A CE1 
3251  C CE2 . TYR A 446  ? 0.2770 0.2470 0.4281 -0.0144 -0.0054 0.0207  444  TYR A CE2 
3252  C CZ  . TYR A 446  ? 0.3150 0.2823 0.4647 -0.0132 -0.0061 0.0174  444  TYR A CZ  
3253  O OH  . TYR A 446  ? 0.3766 0.3406 0.5361 -0.0137 -0.0088 0.0152  444  TYR A OH  
3254  N N   . GLU A 447  ? 0.1881 0.1641 0.2975 -0.0089 0.0000  0.0111  445  GLU A N   
3255  C CA  . GLU A 447  ? 0.2005 0.1757 0.3096 -0.0084 -0.0015 0.0053  445  GLU A CA  
3256  C C   . GLU A 447  ? 0.2072 0.1797 0.3145 -0.0075 -0.0009 0.0066  445  GLU A C   
3257  O O   . GLU A 447  ? 0.2083 0.1800 0.3127 -0.0071 0.0010  0.0116  445  GLU A O   
3258  C CB  . GLU A 447  ? 0.2007 0.1790 0.3019 -0.0078 -0.0013 0.0016  445  GLU A CB  
3259  C CG  . GLU A 447  ? 0.1936 0.1722 0.2852 -0.0067 0.0010  0.0043  445  GLU A CG  
3260  C CD  . GLU A 447  ? 0.2046 0.1863 0.2891 -0.0063 0.0011  0.0016  445  GLU A CD  
3261  O OE1 . GLU A 447  ? 0.2304 0.2148 0.3169 -0.0069 -0.0004 -0.0019 445  GLU A OE1 
3262  O OE2 . GLU A 447  ? 0.2107 0.1924 0.2879 -0.0053 0.0026  0.0031  445  GLU A OE2 
3263  N N   . PHE A 448  ? 0.1963 0.1678 0.3054 -0.0071 -0.0024 0.0018  446  PHE A N   
3264  C CA  . PHE A 448  ? 0.1989 0.1684 0.3047 -0.0059 -0.0018 0.0019  446  PHE A CA  
3265  C C   . PHE A 448  ? 0.1886 0.1604 0.2847 -0.0050 -0.0009 -0.0010 446  PHE A C   
3266  O O   . PHE A 448  ? 0.2136 0.1885 0.3067 -0.0052 -0.0012 -0.0038 446  PHE A O   
3267  C CB  . PHE A 448  ? 0.2183 0.1856 0.3322 -0.0059 -0.0041 -0.0017 446  PHE A CB  
3268  C CG  . PHE A 448  ? 0.2261 0.1905 0.3501 -0.0069 -0.0052 0.0018  446  PHE A CG  
3269  C CD1 . PHE A 448  ? 0.2231 0.1854 0.3478 -0.0067 -0.0041 0.0077  446  PHE A CD1 
3270  C CD2 . PHE A 448  ? 0.2271 0.1916 0.3603 -0.0081 -0.0075 -0.0005 446  PHE A CD2 
3271  C CE1 . PHE A 448  ? 0.2634 0.2236 0.3979 -0.0078 -0.0052 0.0118  446  PHE A CE1 
3272  C CE2 . PHE A 448  ? 0.2657 0.2277 0.4090 -0.0092 -0.0086 0.0033  446  PHE A CE2 
3273  C CZ  . PHE A 448  ? 0.2626 0.2225 0.4066 -0.0091 -0.0075 0.0097  446  PHE A CZ  
3274  N N   . GLN A 449  ? 0.1897 0.1601 0.2811 -0.0039 0.0001  -0.0001 447  GLN A N   
3275  C CA  . GLN A 449  ? 0.1997 0.1721 0.2829 -0.0031 0.0008  -0.0028 447  GLN A CA  
3276  C C   . GLN A 449  ? 0.2076 0.1785 0.2907 -0.0022 0.0005  -0.0047 447  GLN A C   
3277  O O   . GLN A 449  ? 0.2054 0.1733 0.2926 -0.0020 0.0004  -0.0022 447  GLN A O   
3278  C CB  . GLN A 449  ? 0.1928 0.1659 0.2677 -0.0027 0.0030  0.0010  447  GLN A CB  
3279  C CG  . GLN A 449  ? 0.1858 0.1607 0.2605 -0.0033 0.0034  0.0029  447  GLN A CG  
3280  C CD  . GLN A 449  ? 0.2140 0.1902 0.2806 -0.0027 0.0051  0.0050  447  GLN A CD  
3281  O OE1 . GLN A 449  ? 0.2403 0.2156 0.3017 -0.0019 0.0061  0.0058  447  GLN A OE1 
3282  N NE2 . GLN A 449  ? 0.2030 0.1813 0.2688 -0.0032 0.0052  0.0057  447  GLN A NE2 
3283  N N   . CYS A 450  ? 0.1955 0.1689 0.2740 -0.0017 0.0002  -0.0089 448  CYS A N   
3284  C CA  . CYS A 450  ? 0.1885 0.1612 0.2663 -0.0008 -0.0001 -0.0111 448  CYS A CA  
3285  C C   . CYS A 450  ? 0.2017 0.1775 0.2709 -0.0004 0.0008  -0.0128 448  CYS A C   
3286  O O   . CYS A 450  ? 0.2192 0.1979 0.2841 -0.0009 0.0013  -0.0127 448  CYS A O   
3287  C CB  . CYS A 450  ? 0.2275 0.2004 0.3132 -0.0007 -0.0024 -0.0164 448  CYS A CB  
3288  S SG  . CYS A 450  ? 0.2470 0.2259 0.3318 -0.0009 -0.0038 -0.0234 448  CYS A SG  
3289  N N   . LEU A 451  ? 0.2046 0.1801 0.2719 0.0004  0.0010  -0.0140 449  LEU A N   
3290  C CA  . LEU A 451  ? 0.2421 0.2207 0.3019 0.0007  0.0018  -0.0154 449  LEU A CA  
3291  C C   . LEU A 451  ? 0.2303 0.2135 0.2916 0.0008  0.0003  -0.0215 449  LEU A C   
3292  O O   . LEU A 451  ? 0.2463 0.2291 0.3138 0.0012  -0.0011 -0.0251 449  LEU A O   
3293  C CB  . LEU A 451  ? 0.2589 0.2352 0.3157 0.0016  0.0027  -0.0134 449  LEU A CB  
3294  C CG  . LEU A 451  ? 0.2709 0.2501 0.3206 0.0018  0.0035  -0.0144 449  LEU A CG  
3295  C CD1 . LEU A 451  ? 0.2760 0.2566 0.3196 0.0012  0.0046  -0.0116 449  LEU A CD1 
3296  C CD2 . LEU A 451  ? 0.3051 0.2817 0.3535 0.0027  0.0042  -0.0128 449  LEU A CD2 
3297  N N   . HIS A 452  ? 0.2168 0.2047 0.2724 0.0004  0.0007  -0.0225 450  HIS A N   
3298  C CA  . HIS A 452  ? 0.2560 0.2498 0.3115 0.0005  -0.0004 -0.0281 450  HIS A CA  
3299  C C   . HIS A 452  ? 0.2710 0.2650 0.3273 0.0015  -0.0006 -0.0309 450  HIS A C   
3300  O O   . HIS A 452  ? 0.2838 0.2751 0.3369 0.0019  0.0005  -0.0280 450  HIS A O   
3301  C CB  . HIS A 452  ? 0.2433 0.2422 0.2916 -0.0002 0.0003  -0.0272 450  HIS A CB  
3302  C CG  . HIS A 452  ? 0.2382 0.2443 0.2851 -0.0001 -0.0005 -0.0321 450  HIS A CG  
3303  N ND1 . HIS A 452  ? 0.2411 0.2527 0.2904 -0.0004 -0.0019 -0.0365 450  HIS A ND1 
3304  C CD2 . HIS A 452  ? 0.2815 0.2907 0.3250 0.0003  -0.0001 -0.0336 450  HIS A CD2 
3305  C CE1 . HIS A 452  ? 0.2493 0.2677 0.2966 -0.0001 -0.0022 -0.0404 450  HIS A CE1 
3306  N NE2 . HIS A 452  ? 0.2600 0.2771 0.3039 0.0003  -0.0011 -0.0386 450  HIS A NE2 
3307  N N   . GLY A 453  ? 0.2925 0.2900 0.3535 0.0020  -0.0022 -0.0369 451  GLY A N   
3308  C CA  . GLY A 453  ? 0.3285 0.3272 0.3905 0.0031  -0.0026 -0.0402 451  GLY A CA  
3309  C C   . GLY A 453  ? 0.3863 0.3782 0.4526 0.0039  -0.0026 -0.0380 451  GLY A C   
3310  O O   . GLY A 453  ? 0.4254 0.4172 0.4906 0.0048  -0.0023 -0.0387 451  GLY A O   
3311  N N   . MET A 454  ? 0.3088 0.2956 0.3801 0.0035  -0.0030 -0.0352 452  MET A N   
3312  C CA  . MET A 454  ? 0.2818 0.2626 0.3578 0.0041  -0.0031 -0.0325 452  MET A CA  
3313  C C   . MET A 454  ? 0.3000 0.2774 0.3847 0.0037  -0.0046 -0.0322 452  MET A C   
3314  O O   . MET A 454  ? 0.3127 0.2875 0.4055 0.0043  -0.0062 -0.0339 452  MET A O   
3315  C CB  . MET A 454  ? 0.2999 0.2775 0.3699 0.0039  -0.0011 -0.0259 452  MET A CB  
3316  C CG  . MET A 454  ? 0.3234 0.2955 0.3981 0.0044  -0.0012 -0.0221 452  MET A CG  
3317  S SD  . MET A 454  ? 0.3931 0.3646 0.4730 0.0058  -0.0026 -0.0260 452  MET A SD  
3318  C CE  . MET A 454  ? 0.4019 0.3763 0.4716 0.0063  -0.0008 -0.0257 452  MET A CE  
3319  N N   . GLY A 455  ? 0.2483 0.2260 0.3321 0.0026  -0.0042 -0.0299 453  GLY A N   
3320  C CA  . GLY A 455  ? 0.2652 0.2396 0.3572 0.0020  -0.0055 -0.0287 453  GLY A CA  
3321  C C   . GLY A 455  ? 0.2763 0.2535 0.3749 0.0017  -0.0077 -0.0346 453  GLY A C   
3322  O O   . GLY A 455  ? 0.2926 0.2668 0.3995 0.0012  -0.0091 -0.0342 453  GLY A O   
3323  N N   . GLU A 456  ? 0.2979 0.2810 0.3931 0.0020  -0.0081 -0.0401 454  GLU A N   
3324  C CA  . GLU A 456  ? 0.3264 0.3130 0.4274 0.0018  -0.0103 -0.0462 454  GLU A CA  
3325  C C   . GLU A 456  ? 0.3329 0.3170 0.4453 0.0026  -0.0128 -0.0505 454  GLU A C   
3326  O O   . GLU A 456  ? 0.3261 0.3097 0.4460 0.0020  -0.0147 -0.0526 454  GLU A O   
3327  C CB  . GLU A 456  ? 0.3692 0.3639 0.4643 0.0022  -0.0102 -0.0513 454  GLU A CB  
3328  C CG  . GLU A 456  ? 0.4163 0.4141 0.5021 0.0012  -0.0083 -0.0475 454  GLU A CG  
3329  C CD  . GLU A 456  ? 0.3692 0.3672 0.4465 0.0015  -0.0063 -0.0443 454  GLU A CD  
3330  O OE1 . GLU A 456  ? 0.3758 0.3699 0.4543 0.0023  -0.0059 -0.0430 454  GLU A OE1 
3331  O OE2 . GLU A 456  ? 0.3918 0.3942 0.4616 0.0009  -0.0052 -0.0430 454  GLU A OE2 
3332  N N   . PRO A 457  ? 0.3264 0.3089 0.4411 0.0039  -0.0133 -0.0522 455  PRO A N   
3333  C CA  . PRO A 457  ? 0.3355 0.3150 0.4621 0.0046  -0.0160 -0.0562 455  PRO A CA  
3334  C C   . PRO A 457  ? 0.3238 0.2970 0.4586 0.0035  -0.0169 -0.0513 455  PRO A C   
3335  O O   . PRO A 457  ? 0.3336 0.3058 0.4785 0.0034  -0.0195 -0.0550 455  PRO A O   
3336  C CB  . PRO A 457  ? 0.3612 0.3394 0.4873 0.0061  -0.0158 -0.0567 455  PRO A CB  
3337  C CG  . PRO A 457  ? 0.3534 0.3368 0.4678 0.0064  -0.0135 -0.0567 455  PRO A CG  
3338  C CD  . PRO A 457  ? 0.3465 0.3301 0.4537 0.0048  -0.0116 -0.0512 455  PRO A CD  
3339  N N   . LEU A 458  ? 0.3163 0.2855 0.4471 0.0028  -0.0149 -0.0431 456  LEU A N   
3340  C CA  . LEU A 458  ? 0.2779 0.2421 0.4160 0.0016  -0.0155 -0.0377 456  LEU A CA  
3341  C C   . LEU A 458  ? 0.2868 0.2529 0.4262 0.0002  -0.0159 -0.0381 456  LEU A C   
3342  O O   . LEU A 458  ? 0.2861 0.2500 0.4357 -0.0005 -0.0181 -0.0388 456  LEU A O   
3343  C CB  . LEU A 458  ? 0.2785 0.2396 0.4110 0.0013  -0.0130 -0.0292 456  LEU A CB  
3344  C CG  . LEU A 458  ? 0.2743 0.2316 0.4124 -0.0001 -0.0130 -0.0224 456  LEU A CG  
3345  C CD1 . LEU A 458  ? 0.2909 0.2442 0.4426 -0.0002 -0.0159 -0.0232 456  LEU A CD1 
3346  C CD2 . LEU A 458  ? 0.2847 0.2405 0.4158 -0.0001 -0.0104 -0.0148 456  LEU A CD2 
3347  N N   . TYR A 459  ? 0.2758 0.2459 0.4053 -0.0002 -0.0140 -0.0375 457  TYR A N   
3348  C CA  . TYR A 459  ? 0.2890 0.2607 0.4191 -0.0016 -0.0141 -0.0367 457  TYR A CA  
3349  C C   . TYR A 459  ? 0.2843 0.2603 0.4194 -0.0015 -0.0165 -0.0446 457  TYR A C   
3350  O O   . TYR A 459  ? 0.2956 0.2721 0.4347 -0.0027 -0.0175 -0.0445 457  TYR A O   
3351  C CB  . TYR A 459  ? 0.2702 0.2441 0.3891 -0.0021 -0.0113 -0.0321 457  TYR A CB  
3352  C CG  . TYR A 459  ? 0.2548 0.2243 0.3723 -0.0025 -0.0095 -0.0241 457  TYR A CG  
3353  C CD1 . TYR A 459  ? 0.2591 0.2265 0.3818 -0.0037 -0.0096 -0.0197 457  TYR A CD1 
3354  C CD2 . TYR A 459  ? 0.2460 0.2140 0.3576 -0.0016 -0.0077 -0.0211 457  TYR A CD2 
3355  C CE1 . TYR A 459  ? 0.2515 0.2160 0.3731 -0.0040 -0.0079 -0.0124 457  TYR A CE1 
3356  C CE2 . TYR A 459  ? 0.2281 0.1930 0.3385 -0.0018 -0.0061 -0.0140 457  TYR A CE2 
3357  C CZ  . TYR A 459  ? 0.2560 0.2194 0.3713 -0.0030 -0.0062 -0.0097 457  TYR A CZ  
3358  O OH  . TYR A 459  ? 0.2599 0.2212 0.3740 -0.0032 -0.0046 -0.0027 457  TYR A OH  
3359  N N   . GLU A 460  ? 0.2839 0.2632 0.4192 -0.0002 -0.0177 -0.0515 458  GLU A N   
3360  C CA  . GLU A 460  ? 0.3372 0.3202 0.4796 0.0000  -0.0205 -0.0596 458  GLU A CA  
3361  C C   . GLU A 460  ? 0.3455 0.3233 0.5019 -0.0003 -0.0233 -0.0606 458  GLU A C   
3362  O O   . GLU A 460  ? 0.3832 0.3634 0.5470 -0.0004 -0.0259 -0.0668 458  GLU A O   
3363  C CB  . GLU A 460  ? 0.3672 0.3560 0.5065 0.0017  -0.0210 -0.0670 458  GLU A CB  
3364  C CG  . GLU A 460  ? 0.4426 0.4389 0.5707 0.0015  -0.0193 -0.0680 458  GLU A CG  
3365  C CD  . GLU A 460  ? 0.5482 0.5507 0.6719 0.0030  -0.0192 -0.0736 458  GLU A CD  
3366  O OE1 . GLU A 460  ? 0.5107 0.5114 0.6396 0.0043  -0.0203 -0.0768 458  GLU A OE1 
3367  O OE2 . GLU A 460  ? 0.6012 0.6107 0.7163 0.0028  -0.0181 -0.0747 458  GLU A OE2 
3368  N N   . GLU A 461  ? 0.3267 0.2980 0.4873 -0.0005 -0.0230 -0.0547 459  GLU A N   
3369  C CA  . GLU A 461  ? 0.3285 0.2945 0.5026 -0.0012 -0.0256 -0.0535 459  GLU A CA  
3370  C C   . GLU A 461  ? 0.3183 0.2819 0.4935 -0.0032 -0.0247 -0.0463 459  GLU A C   
3371  O O   . GLU A 461  ? 0.3351 0.2942 0.5213 -0.0042 -0.0265 -0.0436 459  GLU A O   
3372  C CB  . GLU A 461  ? 0.3320 0.2926 0.5109 -0.0004 -0.0259 -0.0506 459  GLU A CB  
3373  C CG  . GLU A 461  ? 0.3416 0.3045 0.5190 0.0017  -0.0266 -0.0572 459  GLU A CG  
3374  C CD  . GLU A 461  ? 0.3949 0.3607 0.5812 0.0026  -0.0299 -0.0673 459  GLU A CD  
3375  O OE1 . GLU A 461  ? 0.4188 0.3822 0.6161 0.0017  -0.0325 -0.0684 459  GLU A OE1 
3376  O OE2 . GLU A 461  ? 0.4159 0.3866 0.5984 0.0043  -0.0301 -0.0741 459  GLU A OE2 
3377  N N   . VAL A 462  ? 0.3087 0.2753 0.4731 -0.0039 -0.0220 -0.0429 460  VAL A N   
3378  C CA  . VAL A 462  ? 0.2864 0.2515 0.4503 -0.0056 -0.0207 -0.0358 460  VAL A CA  
3379  C C   . VAL A 462  ? 0.2960 0.2659 0.4575 -0.0064 -0.0208 -0.0385 460  VAL A C   
3380  O O   . VAL A 462  ? 0.3164 0.2855 0.4852 -0.0078 -0.0222 -0.0375 460  VAL A O   
3381  C CB  . VAL A 462  ? 0.2893 0.2534 0.4432 -0.0054 -0.0172 -0.0281 460  VAL A CB  
3382  C CG1 . VAL A 462  ? 0.2756 0.2393 0.4286 -0.0070 -0.0158 -0.0214 460  VAL A CG1 
3383  C CG2 . VAL A 462  ? 0.3045 0.2642 0.4612 -0.0047 -0.0171 -0.0250 460  VAL A CG2 
3384  N N   . VAL A 463  ? 0.2952 0.2704 0.4467 -0.0056 -0.0196 -0.0419 461  VAL A N   
3385  C CA  . VAL A 463  ? 0.2963 0.2765 0.4441 -0.0064 -0.0196 -0.0438 461  VAL A CA  
3386  C C   . VAL A 463  ? 0.3620 0.3449 0.5188 -0.0065 -0.0229 -0.0517 461  VAL A C   
3387  O O   . VAL A 463  ? 0.3669 0.3505 0.5283 -0.0053 -0.0248 -0.0580 461  VAL A O   
3388  C CB  . VAL A 463  ? 0.2944 0.2797 0.4294 -0.0055 -0.0175 -0.0448 461  VAL A CB  
3389  C CG1 . VAL A 463  ? 0.3150 0.3061 0.4463 -0.0062 -0.0176 -0.0467 461  VAL A CG1 
3390  C CG2 . VAL A 463  ? 0.3074 0.2900 0.4342 -0.0054 -0.0144 -0.0374 461  VAL A CG2 
3391  N N   . GLY A 464  ? 0.3568 0.3417 0.5163 -0.0077 -0.0237 -0.0517 462  GLY A N   
3392  C CA  . GLY A 464  ? 0.4196 0.4081 0.5865 -0.0078 -0.0268 -0.0596 462  GLY A CA  
3393  C C   . GLY A 464  ? 0.3966 0.3804 0.5776 -0.0090 -0.0295 -0.0594 462  GLY A C   
3394  O O   . GLY A 464  ? 0.3643 0.3419 0.5514 -0.0093 -0.0296 -0.0549 462  GLY A O   
3395  N N   . ARG A 465  ? 0.4071 0.3944 0.5940 -0.0098 -0.0318 -0.0642 463  ARG A N   
3396  C CA  . ARG A 465  ? 0.3965 0.3797 0.5975 -0.0112 -0.0346 -0.0640 463  ARG A CA  
3397  C C   . ARG A 465  ? 0.4321 0.4109 0.6443 -0.0104 -0.0373 -0.0680 463  ARG A C   
3398  O O   . ARG A 465  ? 0.4909 0.4642 0.7148 -0.0115 -0.0391 -0.0649 463  ARG A O   
3399  C CB  . ARG A 465  ? 0.4693 0.4578 0.6740 -0.0119 -0.0368 -0.0696 463  ARG A CB  
3400  N N   . GLY A 466  ? 0.3908 0.3723 0.6004 -0.0084 -0.0379 -0.0747 464  GLY A N   
3401  C CA  . GLY A 466  ? 0.4146 0.3920 0.6348 -0.0073 -0.0405 -0.0787 464  GLY A CA  
3402  C C   . GLY A 466  ? 0.4239 0.3950 0.6432 -0.0070 -0.0388 -0.0717 464  GLY A C   
3403  O O   . GLY A 466  ? 0.4424 0.4096 0.6708 -0.0061 -0.0410 -0.0742 464  GLY A O   
3404  N N   . LYS A 467  ? 0.3772 0.3475 0.5859 -0.0076 -0.0351 -0.0632 465  LYS A N   
3405  C CA  . LYS A 467  ? 0.3398 0.3049 0.5466 -0.0073 -0.0333 -0.0562 465  LYS A CA  
3406  C C   . LYS A 467  ? 0.3697 0.3309 0.5790 -0.0093 -0.0320 -0.0464 465  LYS A C   
3407  O O   . LYS A 467  ? 0.3901 0.3489 0.6111 -0.0107 -0.0344 -0.0458 465  LYS A O   
3408  C CB  . LYS A 467  ? 0.3362 0.3043 0.5288 -0.0058 -0.0302 -0.0558 465  LYS A CB  
3409  C CG  . LYS A 467  ? 0.3815 0.3541 0.5723 -0.0039 -0.0314 -0.0652 465  LYS A CG  
3410  C CD  . LYS A 467  ? 0.4091 0.3777 0.6111 -0.0027 -0.0341 -0.0689 465  LYS A CD  
3411  C CE  . LYS A 467  ? 0.4578 0.4314 0.6564 -0.0005 -0.0347 -0.0776 465  LYS A CE  
3412  N NZ  . LYS A 467  ? 0.4143 0.3840 0.6238 0.0009  -0.0373 -0.0813 465  LYS A NZ  
3413  N N   . LEU A 468  ? 0.3312 0.2922 0.5301 -0.0094 -0.0285 -0.0389 466  LEU A N   
3414  C CA  . LEU A 468  ? 0.3385 0.2972 0.5384 -0.0112 -0.0269 -0.0298 466  LEU A CA  
3415  C C   . LEU A 468  ? 0.3360 0.2988 0.5294 -0.0122 -0.0254 -0.0286 466  LEU A C   
3416  O O   . LEU A 468  ? 0.3461 0.3080 0.5407 -0.0137 -0.0242 -0.0216 466  LEU A O   
3417  C CB  . LEU A 468  ? 0.3459 0.3022 0.5387 -0.0107 -0.0240 -0.0223 466  LEU A CB  
3418  C CG  . LEU A 468  ? 0.3584 0.3106 0.5566 -0.0096 -0.0253 -0.0226 466  LEU A CG  
3419  C CD1 . LEU A 468  ? 0.3766 0.3271 0.5681 -0.0093 -0.0224 -0.0146 466  LEU A CD1 
3420  C CD2 . LEU A 468  ? 0.3500 0.2982 0.5648 -0.0107 -0.0289 -0.0228 466  LEU A CD2 
3421  N N   . ASP A 469  ? 0.3437 0.3116 0.5305 -0.0114 -0.0254 -0.0350 467  ASP A N   
3422  C CA  . ASP A 469  ? 0.3136 0.2860 0.4945 -0.0122 -0.0243 -0.0346 467  ASP A CA  
3423  C C   . ASP A 469  ? 0.3064 0.2786 0.4780 -0.0125 -0.0207 -0.0262 467  ASP A C   
3424  O O   . ASP A 469  ? 0.2843 0.2573 0.4566 -0.0138 -0.0199 -0.0219 467  ASP A O   
3425  C CB  . ASP A 469  ? 0.3541 0.3268 0.5459 -0.0138 -0.0269 -0.0362 467  ASP A CB  
3426  C CG  . ASP A 469  ? 0.3879 0.3665 0.5742 -0.0142 -0.0266 -0.0389 467  ASP A CG  
3427  O OD1 . ASP A 469  ? 0.4005 0.3834 0.5764 -0.0130 -0.0254 -0.0420 467  ASP A OD1 
3428  O OD2 . ASP A 469  ? 0.4645 0.4436 0.6571 -0.0158 -0.0277 -0.0376 467  ASP A OD2 
3429  N N   . ARG A 470  ? 0.2987 0.2700 0.4620 -0.0112 -0.0186 -0.0241 468  ARG A N   
3430  C CA  . ARG A 470  ? 0.2675 0.2392 0.4208 -0.0111 -0.0152 -0.0176 468  ARG A CA  
3431  C C   . ARG A 470  ? 0.2754 0.2504 0.4169 -0.0097 -0.0137 -0.0205 468  ARG A C   
3432  O O   . ARG A 470  ? 0.2604 0.2357 0.4010 -0.0086 -0.0145 -0.0253 468  ARG A O   
3433  C CB  . ARG A 470  ? 0.2750 0.2425 0.4295 -0.0110 -0.0139 -0.0109 468  ARG A CB  
3434  C CG  . ARG A 470  ? 0.2418 0.2062 0.4080 -0.0126 -0.0152 -0.0065 468  ARG A CG  
3435  C CD  . ARG A 470  ? 0.2450 0.2117 0.4116 -0.0140 -0.0143 -0.0026 468  ARG A CD  
3436  N NE  . ARG A 470  ? 0.2793 0.2436 0.4575 -0.0157 -0.0156 0.0020  468  ARG A NE  
3437  C CZ  . ARG A 470  ? 0.2891 0.2531 0.4782 -0.0170 -0.0185 -0.0009 468  ARG A CZ  
3438  N NH1 . ARG A 470  ? 0.3061 0.2723 0.4956 -0.0168 -0.0203 -0.0087 468  ARG A NH1 
3439  N NH2 . ARG A 470  ? 0.3216 0.2833 0.5214 -0.0187 -0.0196 0.0042  468  ARG A NH2 
3440  N N   . PRO A 471  ? 0.2459 0.2237 0.3788 -0.0098 -0.0116 -0.0178 469  PRO A N   
3441  C CA  . PRO A 471  ? 0.2514 0.2326 0.3737 -0.0087 -0.0104 -0.0202 469  PRO A CA  
3442  C C   . PRO A 471  ? 0.2471 0.2260 0.3630 -0.0076 -0.0084 -0.0170 469  PRO A C   
3443  O O   . PRO A 471  ? 0.2412 0.2165 0.3586 -0.0077 -0.0072 -0.0116 469  PRO A O   
3444  C CB  . PRO A 471  ? 0.2493 0.2336 0.3665 -0.0092 -0.0091 -0.0175 469  PRO A CB  
3445  C CG  . PRO A 471  ? 0.2522 0.2335 0.3739 -0.0101 -0.0083 -0.0112 469  PRO A CG  
3446  C CD  . PRO A 471  ? 0.2352 0.2134 0.3684 -0.0109 -0.0105 -0.0125 469  PRO A CD  
3447  N N   . CYS A 472  ? 0.2271 0.2086 0.3358 -0.0066 -0.0079 -0.0202 470  CYS A N   
3448  C CA  . CYS A 472  ? 0.2270 0.2068 0.3290 -0.0056 -0.0061 -0.0177 470  CYS A CA  
3449  C C   . CYS A 472  ? 0.2208 0.2046 0.3129 -0.0052 -0.0048 -0.0184 470  CYS A C   
3450  O O   . CYS A 472  ? 0.2341 0.2224 0.3250 -0.0052 -0.0060 -0.0233 470  CYS A O   
3451  C CB  . CYS A 472  ? 0.2334 0.2117 0.3387 -0.0047 -0.0073 -0.0215 470  CYS A CB  
3452  S SG  . CYS A 472  ? 0.2566 0.2330 0.3542 -0.0035 -0.0051 -0.0186 470  CYS A SG  
3453  N N   . ARG A 473  ? 0.1959 0.1784 0.2812 -0.0048 -0.0026 -0.0135 471  ARG A N   
3454  C CA  . ARG A 473  ? 0.2052 0.1907 0.2816 -0.0044 -0.0015 -0.0134 471  ARG A CA  
3455  C C   . ARG A 473  ? 0.2167 0.2014 0.2888 -0.0035 -0.0008 -0.0141 471  ARG A C   
3456  O O   . ARG A 473  ? 0.2179 0.1988 0.2902 -0.0030 0.0001  -0.0112 471  ARG A O   
3457  C CB  . ARG A 473  ? 0.2035 0.1881 0.2757 -0.0045 0.0003  -0.0080 471  ARG A CB  
3458  C CG  . ARG A 473  ? 0.2166 0.2043 0.2808 -0.0043 0.0011  -0.0077 471  ARG A CG  
3459  C CD  . ARG A 473  ? 0.2127 0.1998 0.2739 -0.0042 0.0024  -0.0031 471  ARG A CD  
3460  N NE  . ARG A 473  ? 0.2079 0.1956 0.2743 -0.0050 0.0018  -0.0024 471  ARG A NE  
3461  C CZ  . ARG A 473  ? 0.2202 0.2116 0.2873 -0.0056 0.0008  -0.0042 471  ARG A CZ  
3462  N NH1 . ARG A 473  ? 0.2209 0.2160 0.2833 -0.0056 0.0003  -0.0062 471  ARG A NH1 
3463  N NH2 . ARG A 473  ? 0.2129 0.2046 0.2857 -0.0064 0.0001  -0.0037 471  ARG A NH2 
3464  N N   . ILE A 474  ? 0.2043 0.1932 0.2724 -0.0033 -0.0013 -0.0178 472  ILE A N   
3465  C CA  . ILE A 474  ? 0.1922 0.1813 0.2565 -0.0025 -0.0008 -0.0191 472  ILE A CA  
3466  C C   . ILE A 474  ? 0.2157 0.2049 0.2719 -0.0023 0.0009  -0.0153 472  ILE A C   
3467  O O   . ILE A 474  ? 0.2218 0.2145 0.2740 -0.0028 0.0010  -0.0149 472  ILE A O   
3468  C CB  . ILE A 474  ? 0.2020 0.1965 0.2666 -0.0024 -0.0023 -0.0252 472  ILE A CB  
3469  C CG1 . ILE A 474  ? 0.2499 0.2438 0.3235 -0.0023 -0.0043 -0.0296 472  ILE A CG1 
3470  C CG2 . ILE A 474  ? 0.2288 0.2242 0.2888 -0.0016 -0.0016 -0.0262 472  ILE A CG2 
3471  C CD1 . ILE A 474  ? 0.2595 0.2598 0.3341 -0.0022 -0.0059 -0.0363 472  ILE A CD1 
3472  N N   . TYR A 475  ? 0.2057 0.1912 0.2599 -0.0017 0.0022  -0.0124 473  TYR A N   
3473  C CA  . TYR A 475  ? 0.2087 0.1941 0.2558 -0.0014 0.0036  -0.0094 473  TYR A CA  
3474  C C   . TYR A 475  ? 0.2233 0.2123 0.2666 -0.0013 0.0033  -0.0124 473  TYR A C   
3475  O O   . TYR A 475  ? 0.2265 0.2151 0.2713 -0.0008 0.0029  -0.0148 473  TYR A O   
3476  C CB  . TYR A 475  ? 0.2270 0.2078 0.2736 -0.0007 0.0048  -0.0058 473  TYR A CB  
3477  C CG  . TYR A 475  ? 0.2558 0.2358 0.2958 -0.0003 0.0062  -0.0026 473  TYR A CG  
3478  C CD1 . TYR A 475  ? 0.2887 0.2694 0.3244 0.0000  0.0065  -0.0033 473  TYR A CD1 
3479  C CD2 . TYR A 475  ? 0.2462 0.2252 0.2849 -0.0003 0.0071  0.0009  473  TYR A CD2 
3480  C CE1 . TYR A 475  ? 0.2832 0.2631 0.3137 0.0003  0.0075  -0.0006 473  TYR A CE1 
3481  C CE2 . TYR A 475  ? 0.2222 0.2005 0.2557 0.0003  0.0081  0.0033  473  TYR A CE2 
3482  C CZ  . TYR A 475  ? 0.2873 0.2659 0.3169 0.0005  0.0082  0.0026  473  TYR A CZ  
3483  O OH  . TYR A 475  ? 0.2964 0.2741 0.3216 0.0009  0.0090  0.0047  473  TYR A OH  
3484  N N   . ALA A 476  ? 0.2124 0.2053 0.2512 -0.0019 0.0033  -0.0121 474  ALA A N   
3485  C CA  . ALA A 476  ? 0.1988 0.1972 0.2349 -0.0021 0.0027  -0.0151 474  ALA A CA  
3486  C C   . ALA A 476  ? 0.2230 0.2217 0.2529 -0.0022 0.0037  -0.0121 474  ALA A C   
3487  O O   . ALA A 476  ? 0.2160 0.2163 0.2429 -0.0028 0.0038  -0.0096 474  ALA A O   
3488  C CB  . ALA A 476  ? 0.2325 0.2364 0.2693 -0.0029 0.0016  -0.0174 474  ALA A CB  
3489  N N   . PRO A 477  ? 0.2299 0.2273 0.2582 -0.0017 0.0042  -0.0124 475  PRO A N   
3490  C CA  . PRO A 477  ? 0.2338 0.2320 0.2567 -0.0019 0.0049  -0.0099 475  PRO A CA  
3491  C C   . PRO A 477  ? 0.2021 0.2074 0.2224 -0.0028 0.0042  -0.0111 475  PRO A C   
3492  O O   . PRO A 477  ? 0.2166 0.2268 0.2388 -0.0029 0.0034  -0.0152 475  PRO A O   
3493  C CB  . PRO A 477  ? 0.2264 0.2224 0.2491 -0.0011 0.0054  -0.0108 475  PRO A CB  
3494  C CG  . PRO A 477  ? 0.2851 0.2779 0.3132 -0.0004 0.0051  -0.0126 475  PRO A CG  
3495  C CD  . PRO A 477  ? 0.2533 0.2489 0.2850 -0.0009 0.0040  -0.0150 475  PRO A CD  
3496  N N   . VAL A 478  ? 0.1961 0.2022 0.2126 -0.0035 0.0045  -0.0077 476  VAL A N   
3497  C CA  . VAL A 478  ? 0.2343 0.2475 0.2482 -0.0046 0.0038  -0.0076 476  VAL A CA  
3498  C C   . VAL A 478  ? 0.2737 0.2866 0.2840 -0.0050 0.0043  -0.0044 476  VAL A C   
3499  O O   . VAL A 478  ? 0.2963 0.3041 0.3055 -0.0048 0.0047  -0.0009 476  VAL A O   
3500  C CB  . VAL A 478  ? 0.2663 0.2811 0.2805 -0.0052 0.0032  -0.0056 476  VAL A CB  
3501  C CG1 . VAL A 478  ? 0.2520 0.2747 0.2635 -0.0064 0.0025  -0.0048 476  VAL A CG1 
3502  C CG2 . VAL A 478  ? 0.2422 0.2570 0.2605 -0.0049 0.0027  -0.0087 476  VAL A CG2 
3503  N N   . GLY A 479  ? 0.2492 0.2675 0.2577 -0.0055 0.0042  -0.0057 477  GLY A N   
3504  C CA  . GLY A 479  ? 0.3032 0.3218 0.3087 -0.0062 0.0044  -0.0024 477  GLY A CA  
3505  C C   . GLY A 479  ? 0.3002 0.3244 0.3044 -0.0065 0.0045  -0.0046 477  GLY A C   
3506  O O   . GLY A 479  ? 0.2744 0.3020 0.2801 -0.0060 0.0044  -0.0090 477  GLY A O   
3507  N N   . THR A 480  ? 0.3100 0.3350 0.3117 -0.0074 0.0046  -0.0014 478  THR A N   
3508  C CA  . THR A 480  ? 0.3621 0.3932 0.3624 -0.0080 0.0047  -0.0024 478  THR A CA  
3509  C C   . THR A 480  ? 0.3965 0.4235 0.3977 -0.0067 0.0055  -0.0049 478  THR A C   
3510  O O   . THR A 480  ? 0.3779 0.3973 0.3805 -0.0056 0.0058  -0.0051 478  THR A O   
3511  C CB  . THR A 480  ? 0.3784 0.4113 0.3766 -0.0095 0.0045  0.0025  478  THR A CB  
3512  O OG1 . THR A 480  ? 0.4570 0.4813 0.4552 -0.0090 0.0047  0.0052  478  THR A OG1 
3513  C CG2 . THR A 480  ? 0.3860 0.4234 0.3837 -0.0107 0.0036  0.0055  478  THR A CG2 
3514  N N   . HIS A 481  ? 0.3872 0.4198 0.3874 -0.0070 0.0056  -0.0066 479  HIS A N   
3515  C CA  . HIS A 481  ? 0.4566 0.4862 0.4576 -0.0059 0.0062  -0.0088 479  HIS A CA  
3516  C C   . HIS A 481  ? 0.4685 0.4902 0.4686 -0.0058 0.0066  -0.0052 479  HIS A C   
3517  O O   . HIS A 481  ? 0.4695 0.4850 0.4709 -0.0044 0.0070  -0.0064 479  HIS A O   
3518  C CB  . HIS A 481  ? 0.4133 0.4511 0.4131 -0.0065 0.0063  -0.0105 479  HIS A CB  
3519  C CG  . HIS A 481  ? 0.4691 0.5154 0.4700 -0.0062 0.0059  -0.0150 479  HIS A CG  
3520  N ND1 . HIS A 481  ? 0.4161 0.4714 0.4163 -0.0065 0.0060  -0.0174 479  HIS A ND1 
3521  C CD2 . HIS A 481  ? 0.4359 0.4838 0.4387 -0.0057 0.0054  -0.0178 479  HIS A CD2 
3522  C CE1 . HIS A 481  ? 0.4695 0.5316 0.4710 -0.0060 0.0056  -0.0218 479  HIS A CE1 
3523  N NE2 . HIS A 481  ? 0.4560 0.5135 0.4591 -0.0056 0.0051  -0.0222 479  HIS A NE2 
3524  N N   . GLU A 482  ? 0.5254 0.5475 0.5236 -0.0071 0.0063  -0.0010 480  GLU A N   
3525  C CA  . GLU A 482  ? 0.5252 0.5405 0.5229 -0.0070 0.0065  0.0020  480  GLU A CA  
3526  C C   . GLU A 482  ? 0.5169 0.5245 0.5158 -0.0057 0.0067  0.0022  480  GLU A C   
3527  O O   . GLU A 482  ? 0.5345 0.5366 0.5337 -0.0046 0.0071  0.0022  480  GLU A O   
3528  C CB  . GLU A 482  ? 0.5771 0.5942 0.5736 -0.0087 0.0058  0.0065  480  GLU A CB  
3529  N N   . THR A 483  ? 0.4261 0.4340 0.4257 -0.0058 0.0064  0.0026  481  THR A N   
3530  C CA  . THR A 483  ? 0.4716 0.4731 0.4725 -0.0047 0.0066  0.0031  481  THR A CA  
3531  C C   . THR A 483  ? 0.4701 0.4690 0.4730 -0.0033 0.0072  0.0000  481  THR A C   
3532  O O   . THR A 483  ? 0.4691 0.4623 0.4727 -0.0022 0.0076  0.0006  481  THR A O   
3533  C CB  . THR A 483  ? 0.4472 0.4503 0.4486 -0.0053 0.0060  0.0045  481  THR A CB  
3534  N N   . LEU A 484  ? 0.4328 0.4361 0.4370 -0.0032 0.0070  -0.0035 482  LEU A N   
3535  C CA  . LEU A 484  ? 0.4205 0.4212 0.4277 -0.0019 0.0072  -0.0065 482  LEU A CA  
3536  C C   . LEU A 484  ? 0.4279 0.4253 0.4352 -0.0010 0.0077  -0.0068 482  LEU A C   
3537  O O   . LEU A 484  ? 0.4421 0.4348 0.4515 0.0001  0.0080  -0.0070 482  LEU A O   
3538  C CB  . LEU A 484  ? 0.4686 0.4752 0.4778 -0.0020 0.0066  -0.0106 482  LEU A CB  
3539  N N   . LEU A 485  ? 0.4626 0.4627 0.4677 -0.0015 0.0078  -0.0066 483  LEU A N   
3540  C CA  . LEU A 485  ? 0.4514 0.4490 0.4567 -0.0006 0.0081  -0.0072 483  LEU A CA  
3541  C C   . LEU A 485  ? 0.4519 0.4434 0.4562 0.0000  0.0085  -0.0042 483  LEU A C   
3542  O O   . LEU A 485  ? 0.4470 0.4356 0.4519 0.0010  0.0088  -0.0046 483  LEU A O   
3543  C CB  . LEU A 485  ? 0.4122 0.4151 0.4157 -0.0014 0.0081  -0.0077 483  LEU A CB  
3544  C CG  . LEU A 485  ? 0.4221 0.4319 0.4268 -0.0015 0.0078  -0.0116 483  LEU A CG  
3545  C CD1 . LEU A 485  ? 0.4480 0.4641 0.4506 -0.0026 0.0078  -0.0113 483  LEU A CD1 
3546  C CD2 . LEU A 485  ? 0.3719 0.3801 0.3802 0.0001  0.0077  -0.0153 483  LEU A CD2 
3547  N N   . ALA A 486  ? 0.4793 0.4690 0.4822 -0.0006 0.0085  -0.0014 484  ALA A N   
3548  C CA  . ALA A 486  ? 0.4677 0.4526 0.4693 0.0000  0.0088  0.0010  484  ALA A CA  
3549  C C   . ALA A 486  ? 0.4900 0.4707 0.4932 0.0015  0.0093  0.0007  484  ALA A C   
3550  O O   . ALA A 486  ? 0.4690 0.4472 0.4714 0.0023  0.0096  0.0013  484  ALA A O   
3551  C CB  . ALA A 486  ? 0.4494 0.4335 0.4502 -0.0006 0.0085  0.0035  484  ALA A CB  
3552  N N   . TYR A 487  ? 0.4804 0.4606 0.4860 0.0019  0.0094  0.0001  485  TYR A N   
3553  C CA  . TYR A 487  ? 0.4362 0.4129 0.4440 0.0031  0.0099  0.0005  485  TYR A CA  
3554  C C   . TYR A 487  ? 0.4256 0.4030 0.4372 0.0034  0.0095  -0.0019 485  TYR A C   
3555  O O   . TYR A 487  ? 0.4071 0.3822 0.4215 0.0040  0.0097  -0.0012 485  TYR A O   
3556  C CB  . TYR A 487  ? 0.4880 0.4623 0.4957 0.0033  0.0102  0.0028  485  TYR A CB  
3557  C CG  . TYR A 487  ? 0.5168 0.4902 0.5214 0.0033  0.0103  0.0046  485  TYR A CG  
3558  C CD1 . TYR A 487  ? 0.5685 0.5398 0.5718 0.0042  0.0106  0.0055  485  TYR A CD1 
3559  C CD2 . TYR A 487  ? 0.5137 0.4885 0.5174 0.0023  0.0098  0.0054  485  TYR A CD2 
3560  C CE1 . TYR A 487  ? 0.6168 0.5871 0.6179 0.0043  0.0104  0.0067  485  TYR A CE1 
3561  C CE2 . TYR A 487  ? 0.5859 0.5595 0.5878 0.0023  0.0095  0.0070  485  TYR A CE2 
3562  C CZ  . TYR A 487  ? 0.6421 0.6134 0.6429 0.0033  0.0098  0.0074  485  TYR A CZ  
3563  O OH  . TYR A 487  ? 0.6631 0.6330 0.6627 0.0034  0.0093  0.0084  485  TYR A OH  
3564  N N   . LEU A 488  ? 0.4501 0.4311 0.4622 0.0030  0.0090  -0.0046 486  LEU A N   
3565  C CA  . LEU A 488  ? 0.3650 0.3468 0.3814 0.0034  0.0085  -0.0076 486  LEU A CA  
3566  C C   . LEU A 488  ? 0.3849 0.3633 0.4039 0.0047  0.0086  -0.0073 486  LEU A C   
3567  O O   . LEU A 488  ? 0.3324 0.3097 0.3562 0.0052  0.0081  -0.0084 486  LEU A O   
3568  C CB  . LEU A 488  ? 0.4204 0.4076 0.4368 0.0030  0.0080  -0.0110 486  LEU A CB  
3569  C CG  . LEU A 488  ? 0.4673 0.4561 0.4886 0.0035  0.0071  -0.0150 486  LEU A CG  
3570  C CD1 . LEU A 488  ? 0.4596 0.4469 0.4839 0.0033  0.0068  -0.0148 486  LEU A CD1 
3571  C CD2 . LEU A 488  ? 0.3754 0.3709 0.3961 0.0031  0.0067  -0.0187 486  LEU A CD2 
3572  N N   . VAL A 489  ? 0.4238 0.4009 0.4402 0.0051  0.0091  -0.0056 487  VAL A N   
3573  C CA  . VAL A 489  ? 0.3926 0.3670 0.4111 0.0063  0.0091  -0.0048 487  VAL A CA  
3574  C C   . VAL A 489  ? 0.3876 0.3588 0.4086 0.0067  0.0093  -0.0023 487  VAL A C   
3575  O O   . VAL A 489  ? 0.3716 0.3414 0.3973 0.0073  0.0088  -0.0024 487  VAL A O   
3576  C CB  . VAL A 489  ? 0.3895 0.3635 0.4043 0.0066  0.0095  -0.0035 487  VAL A CB  
3577  C CG1 . VAL A 489  ? 0.3947 0.3659 0.4113 0.0078  0.0096  -0.0018 487  VAL A CG1 
3578  C CG2 . VAL A 489  ? 0.3732 0.3506 0.3869 0.0063  0.0092  -0.0061 487  VAL A CG2 
3579  N N   . ARG A 490  ? 0.4198 0.3902 0.4382 0.0064  0.0100  0.0002  488  ARG A N   
3580  C CA  . ARG A 490  ? 0.4215 0.3898 0.4421 0.0067  0.0103  0.0028  488  ARG A CA  
3581  C C   . ARG A 490  ? 0.4419 0.4103 0.4677 0.0063  0.0096  0.0014  488  ARG A C   
3582  O O   . ARG A 490  ? 0.4340 0.4007 0.4642 0.0067  0.0094  0.0027  488  ARG A O   
3583  C CB  . ARG A 490  ? 0.4362 0.4043 0.4532 0.0065  0.0111  0.0049  488  ARG A CB  
3584  C CG  . ARG A 490  ? 0.4249 0.3917 0.4438 0.0070  0.0117  0.0078  488  ARG A CG  
3585  C CD  . ARG A 490  ? 0.4191 0.3861 0.4350 0.0069  0.0123  0.0093  488  ARG A CD  
3586  N NE  . ARG A 490  ? 0.4574 0.4255 0.4737 0.0059  0.0119  0.0080  488  ARG A NE  
3587  C CZ  . ARG A 490  ? 0.4814 0.4503 0.4945 0.0055  0.0118  0.0077  488  ARG A CZ  
3588  N NH1 . ARG A 490  ? 0.4602 0.4286 0.4698 0.0060  0.0121  0.0083  488  ARG A NH1 
3589  N NH2 . ARG A 490  ? 0.3966 0.3668 0.4104 0.0046  0.0114  0.0069  488  ARG A NH2 
3590  N N   . ARG A 491  ? 0.4127 0.3834 0.4383 0.0054  0.0091  -0.0012 489  ARG A N   
3591  C CA  . ARG A 491  ? 0.4270 0.3982 0.4575 0.0050  0.0083  -0.0029 489  ARG A CA  
3592  C C   . ARG A 491  ? 0.4988 0.4695 0.5348 0.0056  0.0073  -0.0054 489  ARG A C   
3593  O O   . ARG A 491  ? 0.4855 0.4549 0.5272 0.0055  0.0066  -0.0055 489  ARG A O   
3594  C CB  . ARG A 491  ? 0.4894 0.4640 0.5179 0.0041  0.0080  -0.0054 489  ARG A CB  
3595  N N   . LEU A 492  ? 0.4638 0.4356 0.4987 0.0061  0.0071  -0.0073 490  LEU A N   
3596  C CA  . LEU A 492  ? 0.4675 0.4391 0.5080 0.0068  0.0059  -0.0101 490  LEU A CA  
3597  C C   . LEU A 492  ? 0.5027 0.4705 0.5472 0.0076  0.0058  -0.0069 490  LEU A C   
3598  O O   . LEU A 492  ? 0.4429 0.4093 0.4942 0.0079  0.0046  -0.0081 490  LEU A O   
3599  C CB  . LEU A 492  ? 0.4745 0.4490 0.5128 0.0072  0.0058  -0.0131 490  LEU A CB  
3600  N N   . LEU A 493  ? 0.4470 0.4134 0.4875 0.0078  0.0069  -0.0030 491  LEU A N   
3601  C CA  . LEU A 493  ? 0.3783 0.3420 0.4220 0.0085  0.0068  0.0006  491  LEU A CA  
3602  C C   . LEU A 493  ? 0.4766 0.4388 0.5252 0.0080  0.0066  0.0029  491  LEU A C   
3603  O O   . LEU A 493  ? 0.5393 0.4997 0.5933 0.0083  0.0060  0.0053  491  LEU A O   
3604  C CB  . LEU A 493  ? 0.4786 0.4422 0.5166 0.0089  0.0081  0.0041  491  LEU A CB  
3605  C CG  . LEU A 493  ? 0.4795 0.4444 0.5133 0.0094  0.0083  0.0024  491  LEU A CG  
3606  C CD1 . LEU A 493  ? 0.5010 0.4655 0.5311 0.0101  0.0091  0.0059  491  LEU A CD1 
3607  C CD2 . LEU A 493  ? 0.5081 0.4731 0.5467 0.0100  0.0070  -0.0005 491  LEU A CD2 
3608  N N   . GLY A 496  ? 0.5846 0.5449 0.6518 0.0088  0.0023  -0.0044 494  GLY A N   
3609  C CA  . GLY A 496  ? 0.5682 0.5291 0.6362 0.0099  0.0016  -0.0074 494  GLY A CA  
3610  C C   . GLY A 496  ? 0.6497 0.6086 0.7183 0.0107  0.0017  -0.0034 494  GLY A C   
3611  O O   . GLY A 496  ? 0.6169 0.5758 0.6881 0.0118  0.0008  -0.0055 494  GLY A O   
3612  N N   . ALA A 497  ? 0.5392 0.4971 0.6056 0.0104  0.0028  0.0022  495  ALA A N   
3613  C CA  . ALA A 497  ? 0.5135 0.4701 0.5807 0.0111  0.0028  0.0066  495  ALA A CA  
3614  C C   . ALA A 497  ? 0.4470 0.4011 0.5244 0.0114  0.0009  0.0078  495  ALA A C   
3615  O O   . ALA A 497  ? 0.4541 0.4071 0.5379 0.0108  -0.0003 0.0064  495  ALA A O   
3616  C CB  . ALA A 497  ? 0.4307 0.3878 0.4932 0.0107  0.0044  0.0120  495  ALA A CB  
3617  N N   . ASN A 498  ? 0.4484 0.4018 0.5280 0.0123  0.0004  0.0105  496  ASN A N   
3618  C CA  . ASN A 498  ? 0.4493 0.4002 0.5393 0.0127  -0.0018 0.0119  496  ASN A CA  
3619  C C   . ASN A 498  ? 0.4322 0.3816 0.5276 0.0115  -0.0021 0.0164  496  ASN A C   
3620  O O   . ASN A 498  ? 0.4531 0.4002 0.5585 0.0113  -0.0041 0.0160  496  ASN A O   
3621  C CB  . ASN A 498  ? 0.5144 0.4651 0.6051 0.0138  -0.0021 0.0153  496  ASN A CB  
3622  N N   . SER A 499  ? 0.4393 0.3904 0.5289 0.0108  -0.0002 0.0205  497  SER A N   
3623  C CA  . SER A 499  ? 0.4264 0.3770 0.5203 0.0096  -0.0002 0.0249  497  SER A CA  
3624  C C   . SER A 499  ? 0.3371 0.2873 0.4325 0.0085  -0.0004 0.0211  497  SER A C   
3625  O O   . SER A 499  ? 0.3850 0.3345 0.4861 0.0075  -0.0009 0.0240  497  SER A O   
3626  C CB  . SER A 499  ? 0.4369 0.3903 0.5238 0.0094  0.0020  0.0305  497  SER A CB  
3627  O OG  . SER A 499  ? 0.4656 0.4210 0.5424 0.0097  0.0038  0.0277  497  SER A OG  
3628  N N   . SER A 500  ? 0.3529 0.3040 0.4436 0.0088  -0.0001 0.0150  498  SER A N   
3629  C CA  . SER A 500  ? 0.3183 0.2700 0.4093 0.0078  -0.0002 0.0116  498  SER A CA  
3630  C C   . SER A 500  ? 0.3802 0.3298 0.4818 0.0076  -0.0027 0.0084  498  SER A C   
3631  O O   . SER A 500  ? 0.3603 0.3087 0.4669 0.0085  -0.0043 0.0052  498  SER A O   
3632  C CB  . SER A 500  ? 0.4109 0.3648 0.4939 0.0081  0.0008  0.0064  498  SER A CB  
3633  O OG  . SER A 500  ? 0.4547 0.4103 0.5286 0.0082  0.0029  0.0091  498  SER A OG  
3634  N N   . PHE A 501  ? 0.3136 0.2629 0.4189 0.0063  -0.0030 0.0090  499  PHE A N   
3635  C CA  . PHE A 501  ? 0.3410 0.2885 0.4567 0.0060  -0.0055 0.0054  499  PHE A CA  
3636  C C   . PHE A 501  ? 0.3729 0.3217 0.4884 0.0069  -0.0066 -0.0028 499  PHE A C   
3637  O O   . PHE A 501  ? 0.3954 0.3426 0.5196 0.0075  -0.0090 -0.0064 499  PHE A O   
3638  C CB  . PHE A 501  ? 0.3071 0.2550 0.4250 0.0045  -0.0055 0.0065  499  PHE A CB  
3639  C CG  . PHE A 501  ? 0.2832 0.2294 0.4119 0.0041  -0.0082 0.0024  499  PHE A CG  
3640  C CD1 . PHE A 501  ? 0.2982 0.2412 0.4381 0.0035  -0.0101 0.0058  499  PHE A CD1 
3641  C CD2 . PHE A 501  ? 0.3704 0.3186 0.4986 0.0042  -0.0090 -0.0050 499  PHE A CD2 
3642  C CE1 . PHE A 501  ? 0.3554 0.2967 0.5061 0.0031  -0.0129 0.0018  499  PHE A CE1 
3643  C CE2 . PHE A 501  ? 0.3167 0.2636 0.4551 0.0040  -0.0117 -0.0094 499  PHE A CE2 
3644  C CZ  . PHE A 501  ? 0.3518 0.2951 0.5018 0.0034  -0.0137 -0.0062 499  PHE A CZ  
3645  N N   . VAL A 502  ? 0.3665 0.3186 0.4726 0.0070  -0.0050 -0.0057 500  VAL A N   
3646  C CA  . VAL A 502  ? 0.4058 0.3604 0.5112 0.0076  -0.0058 -0.0133 500  VAL A CA  
3647  C C   . VAL A 502  ? 0.4142 0.3686 0.5205 0.0092  -0.0065 -0.0155 500  VAL A C   
3648  O O   . VAL A 502  ? 0.5127 0.4684 0.6234 0.0100  -0.0081 -0.0218 500  VAL A O   
3649  C CB  . VAL A 502  ? 0.4232 0.3817 0.5185 0.0071  -0.0040 -0.0150 500  VAL A CB  
3650  N N   . HIS A 503  ? 0.4055 0.3589 0.5079 0.0096  -0.0053 -0.0108 501  HIS A N   
3651  C CA  . HIS A 503  ? 0.3934 0.3462 0.4979 0.0110  -0.0061 -0.0122 501  HIS A CA  
3652  C C   . HIS A 503  ? 0.4254 0.3747 0.5422 0.0115  -0.0087 -0.0118 501  HIS A C   
3653  O O   . HIS A 503  ? 0.4095 0.3587 0.5319 0.0128  -0.0105 -0.0167 501  HIS A O   
3654  C CB  . HIS A 503  ? 0.4326 0.3855 0.5299 0.0113  -0.0043 -0.0070 501  HIS A CB  
3655  C CG  . HIS A 503  ? 0.4786 0.4309 0.5781 0.0128  -0.0051 -0.0076 501  HIS A CG  
3656  N ND1 . HIS A 503  ? 0.4562 0.4054 0.5624 0.0132  -0.0063 -0.0033 501  HIS A ND1 
3657  C CD2 . HIS A 503  ? 0.4592 0.4139 0.5552 0.0138  -0.0049 -0.0118 501  HIS A CD2 
3658  C CE1 . HIS A 503  ? 0.4524 0.4020 0.5593 0.0146  -0.0069 -0.0049 501  HIS A CE1 
3659  N NE2 . HIS A 503  ? 0.5038 0.4567 0.6045 0.0150  -0.0060 -0.0102 501  HIS A NE2 
3660  N N   . ARG A 504  ? 0.3649 0.3114 0.4865 0.0105  -0.0090 -0.0060 502  ARG A N   
3661  C CA  . ARG A 504  ? 0.3839 0.3268 0.5178 0.0108  -0.0116 -0.0043 502  ARG A CA  
3662  C C   . ARG A 504  ? 0.4436 0.3856 0.5871 0.0108  -0.0142 -0.0107 502  ARG A C   
3663  O O   . ARG A 504  ? 0.3865 0.3263 0.5399 0.0118  -0.0168 -0.0131 502  ARG A O   
3664  C CB  . ARG A 504  ? 0.4016 0.3426 0.5376 0.0095  -0.0111 0.0043  502  ARG A CB  
3665  C CG  . ARG A 504  ? 0.4157 0.3577 0.5445 0.0098  -0.0091 0.0105  502  ARG A CG  
3666  C CD  . ARG A 504  ? 0.4264 0.3688 0.5536 0.0084  -0.0077 0.0182  502  ARG A CD  
3667  N NE  . ARG A 504  ? 0.4352 0.3751 0.5742 0.0074  -0.0097 0.0219  502  ARG A NE  
3668  C CZ  . ARG A 504  ? 0.4474 0.3851 0.5947 0.0077  -0.0114 0.0263  502  ARG A CZ  
3669  N NH1 . ARG A 504  ? 0.4916 0.4294 0.6371 0.0090  -0.0115 0.0272  502  ARG A NH1 
3670  N NH2 . ARG A 504  ? 0.4686 0.4042 0.6267 0.0064  -0.0132 0.0301  502  ARG A NH2 
3671  N N   . ILE A 505  ? 0.4168 0.3608 0.5579 0.0099  -0.0138 -0.0139 503  ILE A N   
3672  C CA  . ILE A 505  ? 0.4242 0.3683 0.5738 0.0100  -0.0162 -0.0208 503  ILE A CA  
3673  C C   . ILE A 505  ? 0.4595 0.4056 0.6108 0.0119  -0.0175 -0.0286 503  ILE A C   
3674  O O   . ILE A 505  ? 0.4662 0.4112 0.6281 0.0127  -0.0204 -0.0337 503  ILE A O   
3675  C CB  . ILE A 505  ? 0.4525 0.3994 0.5975 0.0087  -0.0153 -0.0229 503  ILE A CB  
3676  C CG1 . ILE A 505  ? 0.4786 0.4256 0.6334 0.0087  -0.0181 -0.0295 503  ILE A CG1 
3677  C CG2 . ILE A 505  ? 0.4768 0.4286 0.6097 0.0091  -0.0131 -0.0263 503  ILE A CG2 
3678  C CD1 . ILE A 505  ? 0.3885 0.3312 0.5547 0.0075  -0.0201 -0.0257 503  ILE A CD1 
3679  N N   . ASN A 506  ? 0.4440 0.3933 0.5854 0.0127  -0.0155 -0.0296 504  ASN A N   
3680  C CA  . ASN A 506  ? 0.4821 0.4343 0.6237 0.0145  -0.0164 -0.0366 504  ASN A CA  
3681  C C   . ASN A 506  ? 0.4935 0.4431 0.6396 0.0159  -0.0173 -0.0348 504  ASN A C   
3682  O O   . ASN A 506  ? 0.5358 0.4878 0.6830 0.0176  -0.0181 -0.0405 504  ASN A O   
3683  C CB  . ASN A 506  ? 0.5273 0.4850 0.6562 0.0144  -0.0138 -0.0387 504  ASN A CB  
3684  C CG  . ASN A 506  ? 0.5165 0.4779 0.6419 0.0134  -0.0133 -0.0421 504  ASN A CG  
3685  O OD1 . ASN A 506  ? 0.6136 0.5753 0.7467 0.0134  -0.0154 -0.0467 504  ASN A OD1 
3686  N ND2 . ASN A 506  ? 0.6185 0.5830 0.7327 0.0125  -0.0108 -0.0400 504  ASN A ND2 
3687  N N   . ASP A 507  ? 0.4593 0.4046 0.6079 0.0154  -0.0173 -0.0269 505  ASP A N   
3688  C CA  . ASP A 507  ? 0.4796 0.4225 0.6328 0.0167  -0.0184 -0.0246 505  ASP A CA  
3689  C C   . ASP A 507  ? 0.5030 0.4421 0.6716 0.0173  -0.0220 -0.0265 505  ASP A C   
3690  O O   . ASP A 507  ? 0.4495 0.3851 0.6248 0.0160  -0.0230 -0.0217 505  ASP A O   
3691  C CB  . ASP A 507  ? 0.4655 0.4065 0.6141 0.0159  -0.0167 -0.0151 505  ASP A CB  
3692  C CG  . ASP A 507  ? 0.5167 0.4563 0.6681 0.0173  -0.0174 -0.0125 505  ASP A CG  
3693  O OD1 . ASP A 507  ? 0.5349 0.4728 0.6962 0.0187  -0.0201 -0.0162 505  ASP A OD1 
3694  O OD2 . ASP A 507  ? 0.4944 0.4348 0.6382 0.0171  -0.0155 -0.0069 505  ASP A OD2 
3695  N N   . PRO A 508  ? 0.5367 0.4763 0.7118 0.0192  -0.0241 -0.0332 506  PRO A N   
3696  C CA  . PRO A 508  ? 0.5515 0.4871 0.7424 0.0199  -0.0279 -0.0355 506  PRO A CA  
3697  C C   . PRO A 508  ? 0.5081 0.4385 0.7065 0.0196  -0.0292 -0.0268 506  PRO A C   
3698  O O   . PRO A 508  ? 0.5573 0.4836 0.7689 0.0193  -0.0322 -0.0261 506  PRO A O   
3699  C CB  . PRO A 508  ? 0.5866 0.5248 0.7809 0.0224  -0.0295 -0.0444 506  PRO A CB  
3700  C CG  . PRO A 508  ? 0.6047 0.5492 0.7847 0.0226  -0.0264 -0.0477 506  PRO A CG  
3701  C CD  . PRO A 508  ? 0.5290 0.4731 0.6980 0.0209  -0.0232 -0.0389 506  PRO A CD  
3702  N N   . LYS A 509  ? 0.4927 0.4234 0.6833 0.0195  -0.0271 -0.0201 507  LYS A N   
3703  C CA  . LYS A 509  ? 0.4707 0.3976 0.6674 0.0191  -0.0281 -0.0112 507  LYS A CA  
3704  C C   . LYS A 509  ? 0.4957 0.4211 0.6923 0.0167  -0.0272 -0.0032 507  LYS A C   
3705  O O   . LYS A 509  ? 0.5066 0.4294 0.7093 0.0162  -0.0282 0.0047  507  LYS A O   
3706  C CB  . LYS A 509  ? 0.5390 0.4677 0.7271 0.0200  -0.0262 -0.0074 507  LYS A CB  
3707  N N   . VAL A 510  ? 0.4775 0.4049 0.6677 0.0154  -0.0254 -0.0047 508  VAL A N   
3708  C CA  . VAL A 510  ? 0.4360 0.3625 0.6261 0.0131  -0.0245 0.0023  508  VAL A CA  
3709  C C   . VAL A 510  ? 0.4338 0.3576 0.6362 0.0123  -0.0274 -0.0007 508  VAL A C   
3710  O O   . VAL A 510  ? 0.4720 0.3973 0.6743 0.0126  -0.0279 -0.0089 508  VAL A O   
3711  C CB  . VAL A 510  ? 0.4615 0.3919 0.6369 0.0122  -0.0208 0.0029  508  VAL A CB  
3712  C CG1 . VAL A 510  ? 0.4320 0.3620 0.6082 0.0100  -0.0200 0.0093  508  VAL A CG1 
3713  C CG2 . VAL A 510  ? 0.4371 0.3701 0.6011 0.0129  -0.0183 0.0060  508  VAL A CG2 
3714  N N   . SER A 511  ? 0.4156 0.3359 0.6291 0.0112  -0.0294 0.0059  509  SER A N   
3715  C CA  . SER A 511  ? 0.4114 0.3287 0.6382 0.0103  -0.0325 0.0035  509  SER A CA  
3716  C C   . SER A 511  ? 0.4075 0.3265 0.6298 0.0082  -0.0308 0.0047  509  SER A C   
3717  O O   . SER A 511  ? 0.4196 0.3415 0.6303 0.0073  -0.0274 0.0096  509  SER A O   
3718  C CB  . SER A 511  ? 0.4847 0.3984 0.7248 0.0096  -0.0352 0.0108  509  SER A CB  
3719  O OG  . SER A 511  ? 0.4435 0.3577 0.6802 0.0077  -0.0333 0.0215  509  SER A OG  
3720  N N   . ILE A 512  ? 0.3849 0.3022 0.6170 0.0076  -0.0333 -0.0001 510  ILE A N   
3721  C CA  . ILE A 512  ? 0.4093 0.3279 0.6391 0.0056  -0.0322 0.0012  510  ILE A CA  
3722  C C   . ILE A 512  ? 0.4523 0.3697 0.6851 0.0034  -0.0316 0.0125  510  ILE A C   
3723  O O   . ILE A 512  ? 0.4239 0.3441 0.6484 0.0020  -0.0288 0.0166  510  ILE A O   
3724  C CB  . ILE A 512  ? 0.3996 0.3169 0.6398 0.0054  -0.0353 -0.0070 510  ILE A CB  
3725  C CG1 . ILE A 512  ? 0.4005 0.3210 0.6353 0.0075  -0.0352 -0.0181 510  ILE A CG1 
3726  C CG2 . ILE A 512  ? 0.4091 0.3277 0.6483 0.0032  -0.0344 -0.0051 510  ILE A CG2 
3727  C CD1 . ILE A 512  ? 0.4513 0.3719 0.6951 0.0077  -0.0382 -0.0272 510  ILE A CD1 
3728  N N   . ASP A 513  ? 0.4399 0.3546 0.6838 0.0032  -0.0340 0.0178  511  ASP A N   
3729  C CA  . ASP A 513  ? 0.4197 0.3357 0.6648 0.0012  -0.0331 0.0292  511  ASP A CA  
3730  C C   . ASP A 513  ? 0.4351 0.3532 0.6669 0.0015  -0.0292 0.0352  511  ASP A C   
3731  O O   . ASP A 513  ? 0.4015 0.3221 0.6290 -0.0002 -0.0271 0.0422  511  ASP A O   
3732  C CB  . ASP A 513  ? 0.4934 0.4096 0.7491 0.0011  -0.0359 0.0333  511  ASP A CB  
3733  C CG  . ASP A 513  ? 0.5556 0.4714 0.8249 0.0004  -0.0398 0.0291  511  ASP A CG  
3734  O OD1 . ASP A 513  ? 0.5532 0.4693 0.8248 -0.0011 -0.0400 0.0280  511  ASP A OD1 
3735  O OD2 . ASP A 513  ? 0.6767 0.5918 0.9546 0.0014  -0.0427 0.0269  511  ASP A OD2 
3736  N N   . GLU A 514  ? 0.4054 0.3246 0.6288 0.0035  -0.0280 0.0321  512  GLU A N   
3737  C CA  . GLU A 514  ? 0.4147 0.3382 0.6232 0.0038  -0.0242 0.0362  512  GLU A CA  
3738  C C   . GLU A 514  ? 0.3991 0.3259 0.5962 0.0031  -0.0213 0.0333  512  GLU A C   
3739  O O   . GLU A 514  ? 0.4012 0.3313 0.5894 0.0023  -0.0184 0.0389  512  GLU A O   
3740  C CB  . GLU A 514  ? 0.4416 0.3655 0.6443 0.0061  -0.0238 0.0326  512  GLU A CB  
3741  C CG  . GLU A 514  ? 0.4960 0.4178 0.7067 0.0067  -0.0257 0.0382  512  GLU A CG  
3742  C CD  . GLU A 514  ? 0.5550 0.4770 0.7614 0.0091  -0.0257 0.0336  512  GLU A CD  
3743  O OE1 . GLU A 514  ? 0.5559 0.4774 0.7618 0.0104  -0.0265 0.0243  512  GLU A OE1 
3744  O OE2 . GLU A 514  ? 0.6837 0.6069 0.8871 0.0097  -0.0250 0.0395  512  GLU A OE2 
3745  N N   . LEU A 515  ? 0.4051 0.3314 0.6025 0.0034  -0.0221 0.0244  513  LEU A N   
3746  C CA  . LEU A 515  ? 0.3833 0.3130 0.5698 0.0029  -0.0194 0.0215  513  LEU A CA  
3747  C C   . LEU A 515  ? 0.3481 0.2782 0.5379 0.0007  -0.0192 0.0260  513  LEU A C   
3748  O O   . LEU A 515  ? 0.3617 0.2951 0.5419 0.0001  -0.0165 0.0268  513  LEU A O   
3749  C CB  . LEU A 515  ? 0.3784 0.3086 0.5637 0.0039  -0.0203 0.0108  513  LEU A CB  
3750  C CG  . LEU A 515  ? 0.3736 0.3050 0.5520 0.0060  -0.0197 0.0059  513  LEU A CG  
3751  C CD1 . LEU A 515  ? 0.4044 0.3369 0.5840 0.0071  -0.0210 -0.0046 513  LEU A CD1 
3752  C CD2 . LEU A 515  ? 0.3791 0.3139 0.5425 0.0062  -0.0160 0.0088  513  LEU A CD2 
3753  N N   . ILE A 516  ? 0.3304 0.2576 0.5342 -0.0005 -0.0220 0.0290  514  ILE A N   
3754  C CA  . ILE A 516  ? 0.3518 0.2796 0.5599 -0.0027 -0.0219 0.0330  514  ILE A CA  
3755  C C   . ILE A 516  ? 0.3637 0.2927 0.5729 -0.0039 -0.0208 0.0442  514  ILE A C   
3756  O O   . ILE A 516  ? 0.3555 0.2853 0.5702 -0.0059 -0.0210 0.0494  514  ILE A O   
3757  C CB  . ILE A 516  ? 0.3468 0.2709 0.5698 -0.0035 -0.0258 0.0289  514  ILE A CB  
3758  C CG1 . ILE A 516  ? 0.4008 0.3208 0.6378 -0.0034 -0.0290 0.0326  514  ILE A CG1 
3759  C CG2 . ILE A 516  ? 0.3834 0.3076 0.6045 -0.0021 -0.0267 0.0173  514  ILE A CG2 
3760  C CD1 . ILE A 516  ? 0.4094 0.3274 0.6608 -0.0042 -0.0330 0.0286  514  ILE A CD1 
3761  N N   . ALA A 517  ? 0.3312 0.2611 0.5357 -0.0028 -0.0197 0.0482  515  ALA A N   
3762  C CA  . ALA A 517  ? 0.3418 0.2744 0.5458 -0.0038 -0.0184 0.0588  515  ALA A CA  
3763  C C   . ALA A 517  ? 0.3219 0.2592 0.5165 -0.0048 -0.0152 0.0618  515  ALA A C   
3764  O O   . ALA A 517  ? 0.3096 0.2489 0.4927 -0.0040 -0.0129 0.0567  515  ALA A O   
3765  C CB  . ALA A 517  ? 0.3504 0.2842 0.5478 -0.0021 -0.0173 0.0611  515  ALA A CB  
3766  N N   . ASP A 518  ? 0.3177 0.2570 0.5179 -0.0067 -0.0151 0.0700  516  ASP A N   
3767  C CA  . ASP A 518  ? 0.3266 0.2708 0.5197 -0.0078 -0.0122 0.0734  516  ASP A CA  
3768  C C   . ASP A 518  ? 0.3145 0.2640 0.4961 -0.0069 -0.0090 0.0784  516  ASP A C   
3769  O O   . ASP A 518  ? 0.3297 0.2815 0.5145 -0.0073 -0.0090 0.0866  516  ASP A O   
3770  C CB  . ASP A 518  ? 0.3332 0.2779 0.5380 -0.0103 -0.0135 0.0803  516  ASP A CB  
3771  C CG  . ASP A 518  ? 0.3295 0.2797 0.5280 -0.0114 -0.0107 0.0838  516  ASP A CG  
3772  O OD1 . ASP A 518  ? 0.3322 0.2852 0.5176 -0.0102 -0.0079 0.0803  516  ASP A OD1 
3773  O OD2 . ASP A 518  ? 0.3918 0.3436 0.5989 -0.0135 -0.0114 0.0902  516  ASP A OD2 
3774  N N   . PRO A 519  ? 0.3205 0.2723 0.4887 -0.0056 -0.0063 0.0739  517  PRO A N   
3775  C CA  . PRO A 519  ? 0.2984 0.2552 0.4558 -0.0045 -0.0035 0.0780  517  PRO A CA  
3776  C C   . PRO A 519  ? 0.2823 0.2450 0.4401 -0.0059 -0.0019 0.0869  517  PRO A C   
3777  O O   . PRO A 519  ? 0.3061 0.2732 0.4597 -0.0053 -0.0005 0.0925  517  PRO A O   
3778  C CB  . PRO A 519  ? 0.3134 0.2709 0.4582 -0.0032 -0.0014 0.0707  517  PRO A CB  
3779  C CG  . PRO A 519  ? 0.3423 0.2975 0.4909 -0.0042 -0.0024 0.0656  517  PRO A CG  
3780  C CD  . PRO A 519  ? 0.2977 0.2482 0.4603 -0.0052 -0.0058 0.0653  517  PRO A CD  
3781  N N   . VAL A 520  ? 0.2881 0.2516 0.4510 -0.0076 -0.0020 0.0883  518  VAL A N   
3782  C CA  . VAL A 520  ? 0.2753 0.2451 0.4389 -0.0089 -0.0004 0.0968  518  VAL A CA  
3783  C C   . VAL A 520  ? 0.3427 0.3138 0.5157 -0.0099 -0.0019 0.1057  518  VAL A C   
3784  O O   . VAL A 520  ? 0.3242 0.3018 0.4933 -0.0098 -0.0001 0.1126  518  VAL A O   
3785  C CB  . VAL A 520  ? 0.3109 0.2810 0.4793 -0.0107 -0.0005 0.0962  518  VAL A CB  
3786  C CG1 . VAL A 520  ? 0.3255 0.3028 0.4950 -0.0121 0.0012  0.1051  518  VAL A CG1 
3787  C CG2 . VAL A 520  ? 0.2843 0.2538 0.4431 -0.0097 0.0010  0.0880  518  VAL A CG2 
3788  N N   . GLU A 521  ? 0.3263 0.2916 0.5120 -0.0109 -0.0053 0.1055  519  GLU A N   
3789  C CA  . GLU A 521  ? 0.3415 0.3073 0.5376 -0.0119 -0.0072 0.1143  519  GLU A CA  
3790  C C   . GLU A 521  ? 0.3583 0.3245 0.5498 -0.0101 -0.0071 0.1154  519  GLU A C   
3791  O O   . GLU A 521  ? 0.3822 0.3529 0.5763 -0.0105 -0.0071 0.1239  519  GLU A O   
3792  C CB  . GLU A 521  ? 0.3746 0.3349 0.5854 -0.0133 -0.0111 0.1123  519  GLU A CB  
3793  C CG  . GLU A 521  ? 0.3869 0.3485 0.6032 -0.0154 -0.0114 0.1126  519  GLU A CG  
3794  C CD  . GLU A 521  ? 0.4557 0.4261 0.6712 -0.0168 -0.0095 0.1219  519  GLU A CD  
3795  O OE1 . GLU A 521  ? 0.4759 0.4510 0.6938 -0.0169 -0.0100 0.1285  519  GLU A OE1 
3796  O OE2 . GLU A 521  ? 0.4877 0.4609 0.7001 -0.0177 -0.0075 0.1225  519  GLU A OE2 
3797  N N   . VAL A 522  ? 0.3606 0.3230 0.5451 -0.0080 -0.0070 0.1069  520  VAL A N   
3798  C CA  . VAL A 522  ? 0.3163 0.2793 0.4958 -0.0062 -0.0068 0.1075  520  VAL A CA  
3799  C C   . VAL A 522  ? 0.4142 0.3855 0.5822 -0.0055 -0.0035 0.1123  520  VAL A C   
3800  O O   . VAL A 522  ? 0.3782 0.3533 0.5463 -0.0051 -0.0034 0.1190  520  VAL A O   
3801  C CB  . VAL A 522  ? 0.3546 0.3123 0.5292 -0.0042 -0.0074 0.0972  520  VAL A CB  
3802  C CG1 . VAL A 522  ? 0.3515 0.3106 0.5199 -0.0023 -0.0069 0.0978  520  VAL A CG1 
3803  C CG2 . VAL A 522  ? 0.3691 0.3194 0.5562 -0.0047 -0.0111 0.0926  520  VAL A CG2 
3804  N N   . VAL A 523  ? 0.3265 0.3010 0.4844 -0.0051 -0.0007 0.1088  521  VAL A N   
3805  C CA  . VAL A 523  ? 0.3382 0.3209 0.4854 -0.0043 0.0024  0.1126  521  VAL A CA  
3806  C C   . VAL A 523  ? 0.3668 0.3563 0.5198 -0.0060 0.0028  0.1234  521  VAL A C   
3807  O O   . VAL A 523  ? 0.3510 0.3470 0.4999 -0.0054 0.0040  0.1292  521  VAL A O   
3808  C CB  . VAL A 523  ? 0.2963 0.2806 0.4329 -0.0036 0.0050  0.1064  521  VAL A CB  
3809  C CG1 . VAL A 523  ? 0.3401 0.3335 0.4674 -0.0029 0.0080  0.1106  521  VAL A CG1 
3810  C CG2 . VAL A 523  ? 0.3394 0.3185 0.4691 -0.0018 0.0048  0.0971  521  VAL A CG2 
3811  N N   . ARG A 524  ? 0.3331 0.3216 0.4958 -0.0082 0.0017  0.1262  522  ARG A N   
3812  C CA  . ARG A 524  ? 0.3523 0.3477 0.5210 -0.0101 0.0020  0.1368  522  ARG A CA  
3813  C C   . ARG A 524  ? 0.4147 0.4119 0.5896 -0.0102 0.0003  0.1441  522  ARG A C   
3814  O O   . ARG A 524  ? 0.4495 0.4562 0.6232 -0.0107 0.0014  0.1513  522  ARG A O   
3815  C CB  . ARG A 524  ? 0.3973 0.3898 0.5773 -0.0125 0.0004  0.1381  522  ARG A CB  
3816  C CG  . ARG A 524  ? 0.4162 0.4179 0.6013 -0.0143 0.0007  0.1468  522  ARG A CG  
3817  C CD  . ARG A 524  ? 0.4433 0.4423 0.6412 -0.0165 -0.0021 0.1467  522  ARG A CD  
3818  N NE  . ARG A 524  ? 0.4341 0.4269 0.6319 -0.0169 -0.0019 0.1398  522  ARG A NE  
3819  C CZ  . ARG A 524  ? 0.3886 0.3849 0.5814 -0.0174 0.0006  0.1400  522  ARG A CZ  
3820  N NH1 . ARG A 524  ? 0.4272 0.4333 0.6140 -0.0174 0.0035  0.1461  522  ARG A NH1 
3821  N NH2 . ARG A 524  ? 0.4181 0.4085 0.6117 -0.0178 0.0003  0.1333  522  ARG A NH2 
3822  N N   . ALA A 525  ? 0.3777 0.3677 0.5580 -0.0096 -0.0025 0.1404  523  ALA A N   
3823  C CA  . ALA A 525  ? 0.4293 0.4213 0.6159 -0.0096 -0.0048 0.1449  523  ALA A CA  
3824  C C   . ALA A 525  ? 0.4200 0.4141 0.5980 -0.0075 -0.0037 0.1458  523  ALA A C   
3825  O O   . ALA A 525  ? 0.4811 0.4772 0.6637 -0.0074 -0.0054 0.1497  523  ALA A O   
3826  C CB  . ALA A 525  ? 0.4195 0.4031 0.6182 -0.0101 -0.0087 0.1404  523  ALA A CB  
3827  N N   . MET A 526  ? 0.4192 0.4135 0.5850 -0.0057 -0.0010 0.1418  524  MET A N   
3828  C CA  A MET A 526  ? 0.4272 0.4248 0.5836 -0.0036 0.0001  0.1412  524  MET A CA  
3829  C CA  B MET A 526  ? 0.4271 0.4246 0.5838 -0.0036 0.0001  0.1413  524  MET A CA  
3830  C C   . MET A 526  ? 0.4460 0.4546 0.6001 -0.0039 0.0017  0.1513  524  MET A C   
3831  O O   . MET A 526  ? 0.4219 0.4370 0.5764 -0.0053 0.0032  0.1559  524  MET A O   
3832  C CB  A MET A 526  ? 0.4443 0.4419 0.5868 -0.0017 0.0026  0.1320  524  MET A CB  
3833  C CB  B MET A 526  ? 0.4442 0.4410 0.5873 -0.0016 0.0024  0.1317  524  MET A CB  
3834  C CG  A MET A 526  ? 0.4500 0.4380 0.5926 -0.0009 0.0013  0.1218  524  MET A CG  
3835  C CG  B MET A 526  ? 0.4532 0.4403 0.5970 -0.0007 0.0007  0.1222  524  MET A CG  
3836  S SD  A MET A 526  ? 0.5332 0.5157 0.6800 0.0005  -0.0015 0.1202  524  MET A SD  
3837  S SD  B MET A 526  ? 0.4614 0.4477 0.5906 0.0011  0.0032  0.1115  524  MET A SD  
3838  C CE  A MET A 526  ? 0.4462 0.4363 0.5795 0.0026  0.0010  0.1214  524  MET A CE  
3839  C CE  B MET A 526  ? 0.4573 0.4344 0.5890 0.0023  0.0008  0.1031  524  MET A CE  
3840  N N   . PRO A 527  ? 0.4955 0.5072 0.6469 -0.0026 0.0013  0.1545  525  PRO A N   
3841  C CA  . PRO A 527  ? 0.5218 0.5458 0.6703 -0.0028 0.0027  0.1624  525  PRO A CA  
3842  C C   . PRO A 527  ? 0.4820 0.5142 0.6187 -0.0020 0.0065  0.1627  525  PRO A C   
3843  O O   . PRO A 527  ? 0.4584 0.5004 0.5952 -0.0030 0.0078  0.1687  525  PRO A O   
3844  C CB  . PRO A 527  ? 0.5193 0.5437 0.6663 -0.0013 0.0015  0.1636  525  PRO A CB  
3845  C CG  . PRO A 527  ? 0.5442 0.5586 0.6878 0.0004  0.0009  0.1546  525  PRO A CG  
3846  C CD  . PRO A 527  ? 0.4773 0.4829 0.6279 -0.0009 -0.0003 0.1496  525  PRO A CD  
3847  N N   . VAL A 528  ? 0.4557 0.4855 0.5814 0.0000  0.0080  0.1531  526  VAL A N   
3848  C CA  . VAL A 528  ? 0.4176 0.4541 0.5321 0.0010  0.0112  0.1499  526  VAL A CA  
3849  C C   . VAL A 528  ? 0.3663 0.3949 0.4795 0.0009  0.0115  0.1410  526  VAL A C   
3850  O O   . VAL A 528  ? 0.4135 0.4344 0.5235 0.0020  0.0108  0.1328  526  VAL A O   
3851  C CB  . VAL A 528  ? 0.3967 0.4381 0.4993 0.0036  0.0127  0.1465  526  VAL A CB  
3852  C CG1 . VAL A 528  ? 0.4511 0.5001 0.5434 0.0046  0.0158  0.1434  526  VAL A CG1 
3853  C CG2 . VAL A 528  ? 0.4774 0.5261 0.5819 0.0037  0.0120  0.1551  526  VAL A CG2 
3854  N N   . VAL A 529  ? 0.3711 0.4019 0.4871 -0.0006 0.0125  0.1427  527  VAL A N   
3855  C CA  . VAL A 529  ? 0.3447 0.3687 0.4597 -0.0009 0.0126  0.1348  527  VAL A CA  
3856  C C   . VAL A 529  ? 0.3683 0.3936 0.4702 0.0014  0.0149  0.1269  527  VAL A C   
3857  O O   . VAL A 529  ? 0.3687 0.4030 0.4632 0.0024  0.0172  0.1284  527  VAL A O   
3858  C CB  . VAL A 529  ? 0.3186 0.3455 0.4395 -0.0029 0.0132  0.1388  527  VAL A CB  
3859  C CG1 . VAL A 529  ? 0.3292 0.3503 0.4477 -0.0029 0.0137  0.1304  527  VAL A CG1 
3860  C CG2 . VAL A 529  ? 0.3991 0.4231 0.5343 -0.0053 0.0105  0.1459  527  VAL A CG2 
3861  N N   . GLY A 530  ? 0.3238 0.3406 0.4232 0.0022  0.0140  0.1183  528  GLY A N   
3862  C CA  . GLY A 530  ? 0.3182 0.3351 0.4064 0.0041  0.0158  0.1108  528  GLY A CA  
3863  C C   . GLY A 530  ? 0.2827 0.3026 0.3627 0.0061  0.0164  0.1092  528  GLY A C   
3864  O O   . GLY A 530  ? 0.3018 0.3243 0.3725 0.0077  0.0181  0.1045  528  GLY A O   
3865  N N   . ALA A 531  ? 0.3137 0.3333 0.3973 0.0062  0.0149  0.1130  529  ALA A N   
3866  C CA  . ALA A 531  ? 0.2829 0.3053 0.3589 0.0082  0.0153  0.1113  529  ALA A CA  
3867  C C   . ALA A 531  ? 0.3118 0.3271 0.3820 0.0094  0.0151  0.1018  529  ALA A C   
3868  O O   . ALA A 531  ? 0.3075 0.3145 0.3821 0.0087  0.0137  0.0977  529  ALA A O   
3869  C CB  . ALA A 531  ? 0.3218 0.3444 0.4038 0.0080  0.0134  0.1172  529  ALA A CB  
3870  N N   . LYS A 532  ? 0.2701 0.2893 0.3306 0.0113  0.0165  0.0983  530  LYS A N   
3871  C CA  . LYS A 532  ? 0.3175 0.3310 0.3723 0.0124  0.0163  0.0901  530  LYS A CA  
3872  C C   . LYS A 532  ? 0.3153 0.3222 0.3748 0.0123  0.0140  0.0890  530  LYS A C   
3873  O O   . LYS A 532  ? 0.2906 0.2988 0.3557 0.0120  0.0128  0.0947  530  LYS A O   
3874  C CB  . LYS A 532  ? 0.3352 0.3549 0.3803 0.0144  0.0177  0.0881  530  LYS A CB  
3875  C CG  . LYS A 532  ? 0.3919 0.4066 0.4310 0.0155  0.0174  0.0801  530  LYS A CG  
3876  C CD  . LYS A 532  ? 0.3261 0.3472 0.3567 0.0174  0.0185  0.0784  530  LYS A CD  
3877  C CE  . LYS A 532  ? 0.3571 0.3838 0.3882 0.0181  0.0180  0.0837  530  LYS A CE  
3878  N NZ  . LYS A 532  ? 0.3481 0.3687 0.3823 0.0180  0.0160  0.0827  530  LYS A NZ  
3879  N N   . HIS A 533  ? 0.2782 0.2783 0.3359 0.0126  0.0135  0.0818  531  HIS A N   
3880  C CA  . HIS A 533  ? 0.2753 0.2699 0.3363 0.0128  0.0115  0.0796  531  HIS A CA  
3881  C C   . HIS A 533  ? 0.3195 0.3182 0.3768 0.0142  0.0114  0.0817  531  HIS A C   
3882  O O   . HIS A 533  ? 0.3138 0.3172 0.3628 0.0154  0.0129  0.0800  531  HIS A O   
3883  C CB  . HIS A 533  ? 0.2977 0.2864 0.3553 0.0131  0.0114  0.0713  531  HIS A CB  
3884  C CG  . HIS A 533  ? 0.3000 0.2826 0.3631 0.0130  0.0093  0.0686  531  HIS A CG  
3885  N ND1 . HIS A 533  ? 0.3330 0.3156 0.3959 0.0141  0.0083  0.0689  531  HIS A ND1 
3886  C CD2 . HIS A 533  ? 0.3804 0.3571 0.4496 0.0122  0.0079  0.0654  531  HIS A CD2 
3887  C CE1 . HIS A 533  ? 0.4089 0.3858 0.4775 0.0139  0.0065  0.0659  531  HIS A CE1 
3888  N NE2 . HIS A 533  ? 0.4243 0.3978 0.4969 0.0128  0.0062  0.0636  531  HIS A NE2 
3889  N N   . ASP A 534  ? 0.3238 0.3211 0.3878 0.0141  0.0096  0.0853  532  ASP A N   
3890  C CA  . ASP A 534  ? 0.3441 0.3455 0.4054 0.0154  0.0092  0.0880  532  ASP A CA  
3891  C C   . ASP A 534  ? 0.3378 0.3375 0.3916 0.0168  0.0095  0.0811  532  ASP A C   
3892  O O   . ASP A 534  ? 0.3853 0.3902 0.4337 0.0180  0.0099  0.0820  532  ASP A O   
3893  C CB  . ASP A 534  ? 0.3807 0.3795 0.4518 0.0150  0.0068  0.0925  532  ASP A CB  
3894  C CG  . ASP A 534  ? 0.5218 0.5245 0.6001 0.0137  0.0064  0.1014  532  ASP A CG  
3895  O OD1 . ASP A 534  ? 0.5763 0.5846 0.6513 0.0132  0.0083  0.1042  532  ASP A OD1 
3896  O OD2 . ASP A 534  ? 0.6457 0.6458 0.7333 0.0131  0.0043  0.1056  532  ASP A OD2 
3897  N N   . ARG A 535  ? 0.2870 0.2801 0.3407 0.0166  0.0091  0.0744  533  ARG A N   
3898  C CA  . ARG A 535  ? 0.2932 0.2842 0.3412 0.0176  0.0090  0.0683  533  ARG A CA  
3899  C C   . ARG A 535  ? 0.2866 0.2785 0.3261 0.0180  0.0107  0.0631  533  ARG A C   
3900  O O   . ARG A 535  ? 0.3520 0.3415 0.3873 0.0185  0.0106  0.0576  533  ARG A O   
3901  C CB  . ARG A 535  ? 0.3755 0.3595 0.4290 0.0174  0.0072  0.0642  533  ARG A CB  
3902  N N   . ILE A 536  ? 0.2830 0.2784 0.3202 0.0176  0.0122  0.0648  534  ILE A N   
3903  C CA  . ILE A 536  ? 0.2893 0.2858 0.3192 0.0180  0.0137  0.0602  534  ILE A CA  
3904  C C   . ILE A 536  ? 0.3031 0.3077 0.3279 0.0191  0.0150  0.0631  534  ILE A C   
3905  O O   . ILE A 536  ? 0.3230 0.3322 0.3501 0.0187  0.0156  0.0684  534  ILE A O   
3906  C CB  . ILE A 536  ? 0.2709 0.2643 0.3026 0.0169  0.0142  0.0584  534  ILE A CB  
3907  C CG1 . ILE A 536  ? 0.3144 0.3006 0.3508 0.0160  0.0128  0.0548  534  ILE A CG1 
3908  C CG2 . ILE A 536  ? 0.2823 0.2773 0.3068 0.0175  0.0156  0.0543  534  ILE A CG2 
3909  C CD1 . ILE A 536  ? 0.3388 0.3221 0.3772 0.0148  0.0131  0.0529  534  ILE A CD1 
3910  N N   . ALA A 537  ? 0.2699 0.2766 0.2881 0.0204  0.0153  0.0596  535  ALA A N   
3911  C CA  . ALA A 537  ? 0.2681 0.2831 0.2812 0.0217  0.0164  0.0614  535  ALA A CA  
3912  C C   . ALA A 537  ? 0.2480 0.2653 0.2576 0.0218  0.0179  0.0593  535  ALA A C   
3913  O O   . ALA A 537  ? 0.2475 0.2600 0.2553 0.0216  0.0180  0.0540  535  ALA A O   
3914  C CB  . ALA A 537  ? 0.2899 0.3059 0.2976 0.0230  0.0159  0.0576  535  ALA A CB  
3915  N N   . LEU A 538  ? 0.2530 0.2780 0.2620 0.0223  0.0190  0.0635  536  LEU A N   
3916  C CA  . LEU A 538  ? 0.2627 0.2916 0.2674 0.0231  0.0205  0.0609  536  LEU A CA  
3917  C C   . LEU A 538  ? 0.2691 0.2988 0.2672 0.0247  0.0204  0.0549  536  LEU A C   
3918  O O   . LEU A 538  ? 0.2598 0.2907 0.2562 0.0254  0.0195  0.0546  536  LEU A O   
3919  C CB  . LEU A 538  ? 0.2648 0.3037 0.2694 0.0236  0.0217  0.0664  536  LEU A CB  
3920  C CG  . LEU A 538  ? 0.3010 0.3403 0.3121 0.0219  0.0221  0.0724  536  LEU A CG  
3921  C CD1 . LEU A 538  ? 0.3366 0.3872 0.3470 0.0225  0.0233  0.0782  536  LEU A CD1 
3922  C CD2 . LEU A 538  ? 0.3069 0.3410 0.3192 0.0210  0.0226  0.0692  536  LEU A CD2 
3923  N N   . PRO A 539  ? 0.2535 0.2825 0.2485 0.0252  0.0210  0.0501  537  PRO A N   
3924  C CA  . PRO A 539  ? 0.2392 0.2685 0.2289 0.0266  0.0206  0.0442  537  PRO A CA  
3925  C C   . PRO A 539  ? 0.2506 0.2886 0.2367 0.0284  0.0207  0.0451  537  PRO A C   
3926  O O   . PRO A 539  ? 0.2655 0.3027 0.2489 0.0291  0.0197  0.0419  537  PRO A O   
3927  C CB  . PRO A 539  ? 0.2424 0.2710 0.2306 0.0269  0.0214  0.0403  537  PRO A CB  
3928  C CG  . PRO A 539  ? 0.2359 0.2591 0.2289 0.0251  0.0216  0.0425  537  PRO A CG  
3929  C CD  . PRO A 539  ? 0.2321 0.2584 0.2290 0.0243  0.0217  0.0493  537  PRO A CD  
3930  N N   . ALA A 540  ? 0.2476 0.2944 0.2336 0.0290  0.0218  0.0495  538  ALA A N   
3931  C CA  . ALA A 540  ? 0.2657 0.3220 0.2479 0.0308  0.0220  0.0505  538  ALA A CA  
3932  C C   . ALA A 540  ? 0.3008 0.3568 0.2843 0.0305  0.0208  0.0537  538  ALA A C   
3933  O O   . ALA A 540  ? 0.3074 0.3699 0.2873 0.0320  0.0204  0.0533  538  ALA A O   
3934  C CB  . ALA A 540  ? 0.3163 0.3830 0.2987 0.0313  0.0235  0.0555  538  ALA A CB  
3935  N N   . GLU A 541  ? 0.2886 0.3374 0.2771 0.0287  0.0200  0.0567  539  GLU A N   
3936  C CA  . GLU A 541  ? 0.3056 0.3544 0.2965 0.0284  0.0188  0.0607  539  GLU A CA  
3937  C C   . GLU A 541  ? 0.2991 0.3392 0.2904 0.0280  0.0174  0.0565  539  GLU A C   
3938  O O   . GLU A 541  ? 0.2975 0.3355 0.2921 0.0275  0.0162  0.0594  539  GLU A O   
3939  C CB  . GLU A 541  ? 0.3339 0.3827 0.3312 0.0270  0.0188  0.0683  539  GLU A CB  
3940  C CG  . GLU A 541  ? 0.3941 0.4524 0.3912 0.0272  0.0204  0.0731  539  GLU A CG  
3941  C CD  . GLU A 541  ? 0.4763 0.5350 0.4806 0.0256  0.0202  0.0812  539  GLU A CD  
3942  O OE1 . GLU A 541  ? 0.6315 0.6875 0.6400 0.0249  0.0188  0.0848  539  GLU A OE1 
3943  O OE2 . GLU A 541  ? 0.5857 0.6472 0.5918 0.0249  0.0214  0.0839  539  GLU A OE2 
3944  N N   . LEU A 542  ? 0.2749 0.3104 0.2632 0.0282  0.0173  0.0498  540  LEU A N   
3945  C CA  . LEU A 542  ? 0.3029 0.3306 0.2917 0.0276  0.0160  0.0458  540  LEU A CA  
3946  C C   . LEU A 542  ? 0.3039 0.3341 0.2915 0.0285  0.0149  0.0463  540  LEU A C   
3947  O O   . LEU A 542  ? 0.3082 0.3329 0.2982 0.0278  0.0138  0.0457  540  LEU A O   
3948  C CB  . LEU A 542  ? 0.3361 0.3606 0.3213 0.0279  0.0161  0.0390  540  LEU A CB  
3949  C CG  . LEU A 542  ? 0.3242 0.3427 0.3111 0.0267  0.0166  0.0369  540  LEU A CG  
3950  C CD1 . LEU A 542  ? 0.2862 0.3010 0.2701 0.0269  0.0160  0.0305  540  LEU A CD1 
3951  C CD2 . LEU A 542  ? 0.3456 0.3578 0.3379 0.0250  0.0161  0.0392  540  LEU A CD2 
3952  N N   . PHE A 543  ? 0.2726 0.3114 0.2565 0.0300  0.0151  0.0473  541  PHE A N   
3953  C CA  . PHE A 543  ? 0.2975 0.3395 0.2799 0.0309  0.0140  0.0474  541  PHE A CA  
3954  C C   . PHE A 543  ? 0.2702 0.3182 0.2550 0.0311  0.0138  0.0548  541  PHE A C   
3955  O O   . PHE A 543  ? 0.2980 0.3501 0.2814 0.0320  0.0129  0.0558  541  PHE A O   
3956  C CB  . PHE A 543  ? 0.2808 0.3282 0.2573 0.0326  0.0140  0.0424  541  PHE A CB  
3957  C CG  . PHE A 543  ? 0.2759 0.3177 0.2506 0.0324  0.0141  0.0357  541  PHE A CG  
3958  C CD1 . PHE A 543  ? 0.3141 0.3471 0.2906 0.0312  0.0132  0.0326  541  PHE A CD1 
3959  C CD2 . PHE A 543  ? 0.2501 0.2959 0.2220 0.0334  0.0150  0.0328  541  PHE A CD2 
3960  C CE1 . PHE A 543  ? 0.3094 0.3375 0.2847 0.0308  0.0131  0.0272  541  PHE A CE1 
3961  C CE2 . PHE A 543  ? 0.2540 0.2943 0.2250 0.0331  0.0148  0.0271  541  PHE A CE2 
3962  C CZ  . PHE A 543  ? 0.2852 0.3166 0.2579 0.0318  0.0139  0.0246  541  PHE A CZ  
3963  N N   . GLY A 544  ? 0.2968 0.3455 0.2856 0.0302  0.0146  0.0602  542  GLY A N   
3964  C CA  . GLY A 544  ? 0.3324 0.3860 0.3250 0.0300  0.0141  0.0680  542  GLY A CA  
3965  C C   . GLY A 544  ? 0.2845 0.3499 0.2726 0.0317  0.0145  0.0703  542  GLY A C   
3966  O O   . GLY A 544  ? 0.3134 0.3854 0.2969 0.0327  0.0157  0.0681  542  GLY A O   
3967  N N   . ASP A 545  ? 0.3640 0.4327 0.3535 0.0320  0.0132  0.0744  543  ASP A N   
3968  C CA  . ASP A 545  ? 0.3500 0.4310 0.3358 0.0335  0.0134  0.0777  543  ASP A CA  
3969  C C   . ASP A 545  ? 0.3531 0.4380 0.3319 0.0353  0.0132  0.0708  543  ASP A C   
3970  O O   . ASP A 545  ? 0.4012 0.4974 0.3761 0.0368  0.0135  0.0721  543  ASP A O   
3971  C CB  . ASP A 545  ? 0.4234 0.5065 0.4135 0.0333  0.0119  0.0847  543  ASP A CB  
3972  C CG  . ASP A 545  ? 0.5572 0.6371 0.5552 0.0316  0.0117  0.0921  543  ASP A CG  
3973  O OD1 . ASP A 545  ? 0.5593 0.6406 0.5584 0.0308  0.0131  0.0941  543  ASP A OD1 
3974  O OD2 . ASP A 545  ? 0.6828 0.7590 0.6864 0.0310  0.0101  0.0960  543  ASP A OD2 
3975  N N   . ALA A 546  ? 0.3046 0.3811 0.2822 0.0352  0.0127  0.0635  544  ALA A N   
3976  C CA  . ALA A 546  ? 0.3426 0.4221 0.3145 0.0367  0.0121  0.0569  544  ALA A CA  
3977  C C   . ALA A 546  ? 0.3194 0.4061 0.2866 0.0380  0.0134  0.0534  544  ALA A C   
3978  O O   . ALA A 546  ? 0.3353 0.4312 0.2979 0.0398  0.0132  0.0515  544  ALA A O   
3979  C CB  . ALA A 546  ? 0.3178 0.3865 0.2903 0.0360  0.0112  0.0506  544  ALA A CB  
3980  N N   . ARG A 547  ? 0.2837 0.3664 0.2518 0.0373  0.0146  0.0521  545  ARG A N   
3981  C CA  . ARG A 547  ? 0.2979 0.3871 0.2622 0.0386  0.0158  0.0485  545  ARG A CA  
3982  C C   . ARG A 547  ? 0.2349 0.3187 0.2020 0.0374  0.0171  0.0490  545  ARG A C   
3983  O O   . ARG A 547  ? 0.2734 0.3476 0.2448 0.0356  0.0168  0.0505  545  ARG A O   
3984  C CB  . ARG A 547  ? 0.3254 0.4133 0.2858 0.0399  0.0150  0.0396  545  ARG A CB  
3985  C CG  . ARG A 547  ? 0.3357 0.4110 0.2980 0.0385  0.0143  0.0351  545  ARG A CG  
3986  C CD  . ARG A 547  ? 0.3396 0.4139 0.2988 0.0396  0.0132  0.0271  545  ARG A CD  
3987  N NE  . ARG A 547  ? 0.2983 0.3615 0.2597 0.0381  0.0121  0.0243  545  ARG A NE  
3988  C CZ  . ARG A 547  ? 0.2997 0.3549 0.2623 0.0372  0.0122  0.0205  545  ARG A CZ  
3989  N NH1 . ARG A 547  ? 0.2942 0.3507 0.2561 0.0377  0.0132  0.0185  545  ARG A NH1 
3990  N NH2 . ARG A 547  ? 0.2975 0.3438 0.2622 0.0357  0.0113  0.0189  545  ARG A NH2 
3991  N N   . THR A 548  ? 0.2496 0.3402 0.2142 0.0385  0.0184  0.0477  546  THR A N   
3992  C CA  . THR A 548  ? 0.2462 0.3331 0.2130 0.0376  0.0197  0.0478  546  THR A CA  
3993  C C   . THR A 548  ? 0.2458 0.3248 0.2114 0.0377  0.0192  0.0398  546  THR A C   
3994  O O   . THR A 548  ? 0.2438 0.3261 0.2057 0.0394  0.0188  0.0338  546  THR A O   
3995  C CB  . THR A 548  ? 0.2907 0.3898 0.2554 0.0389  0.0212  0.0499  546  THR A CB  
3996  O OG1 . THR A 548  ? 0.3423 0.4500 0.3079 0.0388  0.0215  0.0577  546  THR A OG1 
3997  C CG2 . THR A 548  ? 0.3074 0.4035 0.2748 0.0379  0.0226  0.0507  546  THR A CG2 
3998  N N   . ASN A 549  ? 0.2326 0.3013 0.2018 0.0359  0.0193  0.0397  547  ASN A N   
3999  C CA  . ASN A 549  ? 0.2380 0.2995 0.2066 0.0358  0.0189  0.0330  547  ASN A CA  
4000  C C   . ASN A 549  ? 0.2530 0.3203 0.2194 0.0373  0.0199  0.0299  547  ASN A C   
4001  O O   . ASN A 549  ? 0.2527 0.3267 0.2197 0.0375  0.0214  0.0339  547  ASN A O   
4002  C CB  . ASN A 549  ? 0.2196 0.2707 0.1925 0.0335  0.0189  0.0344  547  ASN A CB  
4003  C CG  . ASN A 549  ? 0.2393 0.2820 0.2120 0.0330  0.0181  0.0282  547  ASN A CG  
4004  O OD1 . ASN A 549  ? 0.2429 0.2862 0.2128 0.0342  0.0173  0.0230  547  ASN A OD1 
4005  N ND2 . ASN A 549  ? 0.2461 0.2810 0.2221 0.0313  0.0183  0.0289  547  ASN A ND2 
4006  N N   . SER A 550  ? 0.2390 0.3042 0.2036 0.0383  0.0192  0.0228  548  SER A N   
4007  C CA  . SER A 550  ? 0.2405 0.3096 0.2040 0.0397  0.0200  0.0192  548  SER A CA  
4008  C C   . SER A 550  ? 0.2430 0.3062 0.2098 0.0381  0.0209  0.0213  548  SER A C   
4009  O O   . SER A 550  ? 0.2595 0.3136 0.2291 0.0361  0.0205  0.0230  548  SER A O   
4010  C CB  . SER A 550  ? 0.2313 0.2974 0.1934 0.0409  0.0185  0.0112  548  SER A CB  
4011  O OG  . SER A 550  ? 0.2378 0.2922 0.2021 0.0390  0.0175  0.0096  548  SER A OG  
4012  N N   . ALA A 551  ? 0.2700 0.3391 0.2366 0.0392  0.0222  0.0209  549  ALA A N   
4013  C CA  . ALA A 551  ? 0.2840 0.3489 0.2535 0.0380  0.0232  0.0226  549  ALA A CA  
4014  C C   . ALA A 551  ? 0.2438 0.3048 0.2133 0.0389  0.0226  0.0161  549  ALA A C   
4015  O O   . ALA A 551  ? 0.2516 0.3179 0.2189 0.0411  0.0223  0.0110  549  ALA A O   
4016  C CB  . ALA A 551  ? 0.2956 0.3702 0.2655 0.0385  0.0250  0.0276  549  ALA A CB  
4017  N N   . GLY A 552  ? 0.2377 0.2896 0.2101 0.0371  0.0225  0.0161  550  GLY A N   
4018  C CA  . GLY A 552  ? 0.2435 0.2915 0.2167 0.0377  0.0220  0.0110  550  GLY A CA  
4019  C C   . GLY A 552  ? 0.2517 0.3032 0.2264 0.0380  0.0235  0.0126  550  GLY A C   
4020  O O   . GLY A 552  ? 0.2691 0.3286 0.2436 0.0383  0.0250  0.0168  550  GLY A O   
4021  N N   . LEU A 553  ? 0.2569 0.3026 0.2335 0.0377  0.0230  0.0094  551  LEU A N   
4022  C CA  . LEU A 553  ? 0.2357 0.2840 0.2141 0.0381  0.0242  0.0102  551  LEU A CA  
4023  C C   . LEU A 553  ? 0.2608 0.2991 0.2422 0.0359  0.0236  0.0105  551  LEU A C   
4024  O O   . LEU A 553  ? 0.2809 0.3116 0.2626 0.0352  0.0221  0.0077  551  LEU A O   
4025  C CB  . LEU A 553  ? 0.2760 0.3296 0.2535 0.0409  0.0240  0.0043  551  LEU A CB  
4026  C CG  . LEU A 553  ? 0.2909 0.3565 0.2654 0.0433  0.0247  0.0034  551  LEU A CG  
4027  C CD1 . LEU A 553  ? 0.3446 0.4144 0.3188 0.0463  0.0240  -0.0036 551  LEU A CD1 
4028  C CD2 . LEU A 553  ? 0.2957 0.3700 0.2701 0.0431  0.0269  0.0096  551  LEU A CD2 
4029  N N   . ASP A 554  ? 0.2427 0.2815 0.2265 0.0349  0.0248  0.0142  552  ASP A N   
4030  C CA  . ASP A 554  ? 0.2757 0.3058 0.2623 0.0328  0.0244  0.0151  552  ASP A CA  
4031  C C   . ASP A 554  ? 0.2496 0.2790 0.2375 0.0339  0.0241  0.0112  552  ASP A C   
4032  O O   . ASP A 554  ? 0.2373 0.2717 0.2263 0.0346  0.0253  0.0123  552  ASP A O   
4033  C CB  . ASP A 554  ? 0.2653 0.2961 0.2545 0.0310  0.0256  0.0210  552  ASP A CB  
4034  C CG  . ASP A 554  ? 0.2344 0.2569 0.2266 0.0288  0.0250  0.0216  552  ASP A CG  
4035  O OD1 . ASP A 554  ? 0.2614 0.2781 0.2535 0.0287  0.0237  0.0178  552  ASP A OD1 
4036  O OD2 . ASP A 554  ? 0.2966 0.3187 0.2915 0.0272  0.0256  0.0260  552  ASP A OD2 
4037  N N   . LEU A 555  ? 0.2299 0.2531 0.2180 0.0339  0.0224  0.0069  553  LEU A N   
4038  C CA  . LEU A 555  ? 0.2577 0.2796 0.2474 0.0350  0.0218  0.0032  553  LEU A CA  
4039  C C   . LEU A 555  ? 0.2389 0.2560 0.2316 0.0332  0.0219  0.0054  553  LEU A C   
4040  O O   . LEU A 555  ? 0.2642 0.2793 0.2588 0.0339  0.0212  0.0028  553  LEU A O   
4041  C CB  . LEU A 555  ? 0.2556 0.2731 0.2451 0.0358  0.0197  -0.0019 553  LEU A CB  
4042  C CG  . LEU A 555  ? 0.2829 0.3058 0.2698 0.0378  0.0193  -0.0049 553  LEU A CG  
4043  C CD1 . LEU A 555  ? 0.3070 0.3253 0.2948 0.0385  0.0170  -0.0102 553  LEU A CD1 
4044  C CD2 . LEU A 555  ? 0.3111 0.3442 0.2971 0.0404  0.0207  -0.0059 553  LEU A CD2 
4045  N N   . SER A 556  ? 0.2238 0.2391 0.2173 0.0311  0.0227  0.0101  554  SER A N   
4046  C CA  . SER A 556  ? 0.2272 0.2397 0.2236 0.0295  0.0231  0.0124  554  SER A CA  
4047  C C   . SER A 556  ? 0.2561 0.2754 0.2537 0.0298  0.0249  0.0158  554  SER A C   
4048  O O   . SER A 556  ? 0.2535 0.2713 0.2538 0.0286  0.0253  0.0178  554  SER A O   
4049  C CB  . SER A 556  ? 0.2557 0.2616 0.2531 0.0268  0.0225  0.0149  554  SER A CB  
4050  O OG  . SER A 556  ? 0.2829 0.2913 0.2803 0.0260  0.0234  0.0189  554  SER A OG  
4051  N N   . ASN A 557  ? 0.2328 0.2599 0.2285 0.0314  0.0260  0.0167  555  ASN A N   
4052  C CA  . ASN A 557  ? 0.2279 0.2625 0.2248 0.0315  0.0278  0.0206  555  ASN A CA  
4053  C C   . ASN A 557  ? 0.2411 0.2820 0.2380 0.0340  0.0285  0.0175  555  ASN A C   
4054  O O   . ASN A 557  ? 0.2308 0.2758 0.2253 0.0363  0.0282  0.0135  555  ASN A O   
4055  C CB  . ASN A 557  ? 0.2435 0.2840 0.2384 0.0318  0.0286  0.0237  555  ASN A CB  
4056  C CG  . ASN A 557  ? 0.2227 0.2718 0.2191 0.0317  0.0305  0.0287  555  ASN A CG  
4057  O OD1 . ASN A 557  ? 0.2659 0.3217 0.2625 0.0333  0.0315  0.0277  555  ASN A OD1 
4058  N ND2 . ASN A 557  ? 0.2434 0.2925 0.2413 0.0299  0.0309  0.0342  555  ASN A ND2 
4059  N N   . GLU A 558  ? 0.2347 0.2767 0.2344 0.0336  0.0292  0.0190  556  GLU A N   
4060  C CA  . GLU A 558  ? 0.2491 0.2969 0.2494 0.0360  0.0297  0.0158  556  GLU A CA  
4061  C C   . GLU A 558  ? 0.2475 0.3070 0.2457 0.0382  0.0313  0.0160  556  GLU A C   
4062  O O   . GLU A 558  ? 0.2587 0.3234 0.2561 0.0410  0.0313  0.0113  556  GLU A O   
4063  C CB  . GLU A 558  ? 0.2592 0.3066 0.2631 0.0350  0.0304  0.0178  556  GLU A CB  
4064  C CG  . GLU A 558  ? 0.2672 0.3047 0.2732 0.0334  0.0288  0.0166  556  GLU A CG  
4065  C CD  . GLU A 558  ? 0.2704 0.3036 0.2761 0.0350  0.0270  0.0108  556  GLU A CD  
4066  O OE1 . GLU A 558  ? 0.2416 0.2795 0.2461 0.0377  0.0269  0.0068  556  GLU A OE1 
4067  O OE2 . GLU A 558  ? 0.2546 0.2796 0.2615 0.0334  0.0255  0.0103  556  GLU A OE2 
4068  N N   . GLU A 559  ? 0.2256 0.2901 0.2234 0.0370  0.0326  0.0215  557  GLU A N   
4069  C CA  . GLU A 559  ? 0.2459 0.3224 0.2414 0.0390  0.0341  0.0223  557  GLU A CA  
4070  C C   . GLU A 559  ? 0.2487 0.3263 0.2405 0.0411  0.0330  0.0174  557  GLU A C   
4071  O O   . GLU A 559  ? 0.2521 0.3382 0.2421 0.0439  0.0334  0.0135  557  GLU A O   
4072  C CB  . GLU A 559  ? 0.2778 0.3587 0.2739 0.0371  0.0353  0.0298  557  GLU A CB  
4073  C CG  . GLU A 559  ? 0.3141 0.3960 0.3144 0.0351  0.0364  0.0351  557  GLU A CG  
4074  C CD  . GLU A 559  ? 0.3860 0.4707 0.3879 0.0330  0.0372  0.0427  557  GLU A CD  
4075  O OE1 . GLU A 559  ? 0.5102 0.5974 0.5094 0.0333  0.0370  0.0438  557  GLU A OE1 
4076  O OE2 . GLU A 559  ? 0.4594 0.5435 0.4654 0.0309  0.0378  0.0476  557  GLU A OE2 
4077  N N   . THR A 560  ? 0.2471 0.3165 0.2379 0.0397  0.0316  0.0173  558  THR A N   
4078  C CA  . THR A 560  ? 0.2560 0.3256 0.2435 0.0414  0.0304  0.0126  558  THR A CA  
4079  C C   . THR A 560  ? 0.2463 0.3139 0.2343 0.0435  0.0291  0.0054  558  THR A C   
4080  O O   . THR A 560  ? 0.2490 0.3226 0.2351 0.0462  0.0288  0.0007  558  THR A O   
4081  C CB  . THR A 560  ? 0.2407 0.3010 0.2277 0.0392  0.0290  0.0139  558  THR A CB  
4082  O OG1 . THR A 560  ? 0.2705 0.3326 0.2579 0.0373  0.0301  0.0206  558  THR A OG1 
4083  C CG2 . THR A 560  ? 0.2846 0.3454 0.2685 0.0408  0.0278  0.0093  558  THR A CG2 
4084  N N   . LEU A 561  ? 0.2393 0.2987 0.2302 0.0425  0.0282  0.0044  559  LEU A N   
4085  C CA  . LEU A 561  ? 0.2274 0.2841 0.2195 0.0444  0.0267  -0.0021 559  LEU A CA  
4086  C C   . LEU A 561  ? 0.2502 0.3171 0.2428 0.0475  0.0278  -0.0050 559  LEU A C   
4087  O O   . LEU A 561  ? 0.2585 0.3277 0.2512 0.0501  0.0266  -0.0113 559  LEU A O   
4088  C CB  . LEU A 561  ? 0.2152 0.2618 0.2106 0.0426  0.0256  -0.0018 559  LEU A CB  
4089  C CG  . LEU A 561  ? 0.2135 0.2502 0.2085 0.0401  0.0242  -0.0006 559  LEU A CG  
4090  C CD1 . LEU A 561  ? 0.2364 0.2650 0.2344 0.0382  0.0233  0.0002  559  LEU A CD1 
4091  C CD2 . LEU A 561  ? 0.2386 0.2730 0.2322 0.0413  0.0223  -0.0056 559  LEU A CD2 
4092  N N   . ALA A 562  ? 0.2383 0.3116 0.2318 0.0471  0.0298  -0.0008 560  ALA A N   
4093  C CA  . ALA A 562  ? 0.2578 0.3417 0.2519 0.0500  0.0310  -0.0034 560  ALA A CA  
4094  C C   . ALA A 562  ? 0.2664 0.3613 0.2570 0.0524  0.0316  -0.0056 560  ALA A C   
4095  O O   . ALA A 562  ? 0.2572 0.3583 0.2478 0.0557  0.0312  -0.0117 560  ALA A O   
4096  C CB  . ALA A 562  ? 0.2791 0.3678 0.2751 0.0487  0.0331  0.0023  560  ALA A CB  
4097  N N   . SER A 563  ? 0.2588 0.3565 0.2467 0.0510  0.0325  -0.0008 561  SER A N   
4098  C CA  A SER A 563  ? 0.2800 0.3886 0.2643 0.0532  0.0330  -0.0024 561  SER A CA  
4099  C CA  B SER A 563  ? 0.2798 0.3885 0.2641 0.0533  0.0330  -0.0025 561  SER A CA  
4100  C C   . SER A 563  ? 0.2666 0.3713 0.2494 0.0550  0.0308  -0.0096 561  SER A C   
4101  O O   . SER A 563  ? 0.2849 0.3985 0.2663 0.0582  0.0306  -0.0150 561  SER A O   
4102  C CB  A SER A 563  ? 0.3086 0.4199 0.2908 0.0510  0.0342  0.0050  561  SER A CB  
4103  C CB  B SER A 563  ? 0.3091 0.4217 0.2912 0.0513  0.0343  0.0049  561  SER A CB  
4104  O OG  A SER A 563  ? 0.3028 0.4232 0.2812 0.0529  0.0343  0.0035  561  SER A OG  
4105  O OG  B SER A 563  ? 0.3383 0.4403 0.3200 0.0490  0.0329  0.0066  561  SER A OG  
4106  N N   . LEU A 564  ? 0.2750 0.3670 0.2586 0.0530  0.0289  -0.0098 562  LEU A N   
4107  C CA  . LEU A 564  ? 0.2676 0.3551 0.2506 0.0543  0.0266  -0.0162 562  LEU A CA  
4108  C C   . LEU A 564  ? 0.2535 0.3413 0.2394 0.0571  0.0253  -0.0236 562  LEU A C   
4109  O O   . LEU A 564  ? 0.2746 0.3665 0.2599 0.0597  0.0241  -0.0300 562  LEU A O   
4110  C CB  . LEU A 564  ? 0.2619 0.3360 0.2458 0.0513  0.0250  -0.0143 562  LEU A CB  
4111  C CG  . LEU A 564  ? 0.3390 0.4084 0.3218 0.0517  0.0228  -0.0187 562  LEU A CG  
4112  C CD1 . LEU A 564  ? 0.3331 0.4118 0.3119 0.0530  0.0234  -0.0188 562  LEU A CD1 
4113  C CD2 . LEU A 564  ? 0.2776 0.3350 0.2611 0.0484  0.0218  -0.0155 562  LEU A CD2 
4114  N N   . THR A 565  ? 0.2666 0.3500 0.2560 0.0565  0.0254  -0.0231 563  THR A N   
4115  C CA  . THR A 565  ? 0.2661 0.3499 0.2589 0.0592  0.0241  -0.0298 563  THR A CA  
4116  C C   . THR A 565  ? 0.2512 0.3489 0.2427 0.0631  0.0249  -0.0345 563  THR A C   
4117  O O   . THR A 565  ? 0.2781 0.3771 0.2708 0.0659  0.0231  -0.0420 563  THR A O   
4118  C CB  . THR A 565  ? 0.2650 0.3453 0.2614 0.0583  0.0247  -0.0275 563  THR A CB  
4119  O OG1 . THR A 565  ? 0.2671 0.3348 0.2649 0.0549  0.0236  -0.0240 563  THR A OG1 
4120  C CG2 . THR A 565  ? 0.3016 0.3831 0.3019 0.0614  0.0233  -0.0345 563  THR A CG2 
4121  N N   . GLU A 566  ? 0.2676 0.3763 0.2568 0.0632  0.0276  -0.0302 564  GLU A N   
4122  C CA  . GLU A 566  ? 0.2915 0.4151 0.2792 0.0669  0.0287  -0.0343 564  GLU A CA  
4123  C C   . GLU A 566  ? 0.2587 0.3870 0.2429 0.0684  0.0277  -0.0381 564  GLU A C   
4124  O O   . GLU A 566  ? 0.2817 0.4168 0.2663 0.0720  0.0267  -0.0458 564  GLU A O   
4125  C CB  . GLU A 566  ? 0.2940 0.4286 0.2802 0.0663  0.0318  -0.0278 564  GLU A CB  
4126  C CG  . GLU A 566  ? 0.4037 0.5356 0.3936 0.0653  0.0328  -0.0251 564  GLU A CG  
4127  C CD  . GLU A 566  ? 0.4552 0.5850 0.4492 0.0681  0.0312  -0.0328 564  GLU A CD  
4128  O OE1 . GLU A 566  ? 0.4843 0.6241 0.4783 0.0719  0.0310  -0.0394 564  GLU A OE1 
4129  O OE2 . GLU A 566  ? 0.4387 0.5572 0.4363 0.0666  0.0299  -0.0324 564  GLU A OE2 
4130  N N   . ALA A 567  ? 0.2596 0.3844 0.2408 0.0659  0.0278  -0.0330 565  ALA A N   
4131  C CA  . ALA A 567  ? 0.2628 0.3922 0.2407 0.0672  0.0269  -0.0363 565  ALA A CA  
4132  C C   . ALA A 567  ? 0.2491 0.3701 0.2293 0.0685  0.0237  -0.0443 565  ALA A C   
4133  O O   . ALA A 567  ? 0.2813 0.4089 0.2605 0.0713  0.0225  -0.0508 565  ALA A O   
4134  C CB  . ALA A 567  ? 0.2933 0.4195 0.2680 0.0641  0.0275  -0.0289 565  ALA A CB  
4135  N N   . LEU A 568  ? 0.2595 0.3665 0.2433 0.0664  0.0221  -0.0439 566  LEU A N   
4136  C CA  . LEU A 568  ? 0.2405 0.3390 0.2274 0.0673  0.0189  -0.0508 566  LEU A CA  
4137  C C   . LEU A 568  ? 0.2707 0.3747 0.2612 0.0712  0.0178  -0.0590 566  LEU A C   
4138  O O   . LEU A 568  ? 0.2723 0.3781 0.2638 0.0737  0.0157  -0.0664 566  LEU A O   
4139  C CB  . LEU A 568  ? 0.2366 0.3199 0.2266 0.0641  0.0177  -0.0477 566  LEU A CB  
4140  C CG  . LEU A 568  ? 0.2425 0.3192 0.2297 0.0604  0.0182  -0.0408 566  LEU A CG  
4141  C CD1 . LEU A 568  ? 0.2513 0.3151 0.2417 0.0574  0.0173  -0.0377 566  LEU A CD1 
4142  C CD2 . LEU A 568  ? 0.2728 0.3485 0.2579 0.0604  0.0166  -0.0434 566  LEU A CD2 
4143  N N   . ARG A 569  ? 0.2599 0.3667 0.2526 0.0720  0.0192  -0.0581 567  ARG A N   
4144  C CA  . ARG A 569  ? 0.2792 0.3927 0.2754 0.0760  0.0183  -0.0660 567  ARG A CA  
4145  C C   . ARG A 569  ? 0.2860 0.4146 0.2789 0.0794  0.0190  -0.0708 567  ARG A C   
4146  O O   . ARG A 569  ? 0.2961 0.4278 0.2915 0.0828  0.0169  -0.0797 567  ARG A O   
4147  C CB  . ARG A 569  ? 0.2896 0.4057 0.2880 0.0762  0.0202  -0.0633 567  ARG A CB  
4148  C CG  . ARG A 569  ? 0.3374 0.4394 0.3400 0.0736  0.0190  -0.0605 567  ARG A CG  
4149  C CD  . ARG A 569  ? 0.3669 0.4725 0.3715 0.0737  0.0209  -0.0576 567  ARG A CD  
4150  N NE  . ARG A 569  ? 0.3998 0.4927 0.4076 0.0708  0.0201  -0.0536 567  ARG A NE  
4151  C CZ  . ARG A 569  ? 0.5034 0.5968 0.5132 0.0701  0.0215  -0.0500 567  ARG A CZ  
4152  N NH1 . ARG A 569  ? 0.5396 0.6451 0.5485 0.0719  0.0239  -0.0496 567  ARG A NH1 
4153  N NH2 . ARG A 569  ? 0.5041 0.5859 0.5167 0.0674  0.0205  -0.0467 567  ARG A NH2 
4154  N N   . GLU A 570  ? 0.2860 0.4245 0.2736 0.0786  0.0218  -0.0650 568  GLU A N   
4155  C CA  . GLU A 570  ? 0.2833 0.4376 0.2673 0.0818  0.0226  -0.0689 568  GLU A CA  
4156  C C   . GLU A 570  ? 0.3417 0.4936 0.3248 0.0826  0.0201  -0.0743 568  GLU A C   
4157  O O   . GLU A 570  ? 0.3195 0.4811 0.3024 0.0863  0.0191  -0.0823 568  GLU A O   
4158  C CB  . GLU A 570  ? 0.3142 0.4786 0.2930 0.0802  0.0260  -0.0603 568  GLU A CB  
4159  C CG  . GLU A 570  ? 0.3718 0.5429 0.3518 0.0803  0.0286  -0.0563 568  GLU A CG  
4160  C CD  . GLU A 570  ? 0.4788 0.6574 0.4548 0.0779  0.0317  -0.0463 568  GLU A CD  
4161  O OE1 . GLU A 570  ? 0.5285 0.7034 0.5014 0.0755  0.0316  -0.0413 568  GLU A OE1 
4162  O OE2 . GLU A 570  ? 0.6090 0.7973 0.5852 0.0785  0.0341  -0.0434 568  GLU A OE2 
4163  N N   . SER A 571  ? 0.2863 0.4255 0.2690 0.0793  0.0188  -0.0705 569  SER A N   
4164  C CA  . SER A 571  ? 0.2860 0.4223 0.2680 0.0797  0.0163  -0.0753 569  SER A CA  
4165  C C   . SER A 571  ? 0.2868 0.4185 0.2747 0.0823  0.0130  -0.0852 569  SER A C   
4166  O O   . SER A 571  ? 0.3104 0.4460 0.2982 0.0846  0.0110  -0.0922 569  SER A O   
4167  C CB  . SER A 571  ? 0.2815 0.4049 0.2625 0.0755  0.0158  -0.0689 569  SER A CB  
4168  O OG  . SER A 571  ? 0.2878 0.3966 0.2739 0.0738  0.0137  -0.0696 569  SER A OG  
4169  N N   . ALA A 572  ? 0.3065 0.4301 0.2997 0.0822  0.0121  -0.0862 570  ALA A N   
4170  C CA  . ALA A 572  ? 0.3186 0.4374 0.3183 0.0846  0.0087  -0.0953 570  ALA A CA  
4171  C C   . ALA A 572  ? 0.3584 0.4909 0.3596 0.0896  0.0087  -0.1038 570  ALA A C   
4172  O O   . ALA A 572  ? 0.3853 0.5158 0.3920 0.0922  0.0056  -0.1126 570  ALA A O   
4173  C CB  . ALA A 572  ? 0.3597 0.4652 0.3651 0.0827  0.0076  -0.0931 570  ALA A CB  
4174  N N   . ALA A 573  ? 0.3281 0.4747 0.3249 0.0909  0.0119  -0.1013 571  ALA A N   
4175  C CA  . ALA A 573  ? 0.3606 0.5226 0.3579 0.0957  0.0123  -0.1091 571  ALA A CA  
4176  C C   . ALA A 573  ? 0.4160 0.5902 0.4086 0.0977  0.0122  -0.1131 571  ALA A C   
4177  O O   . ALA A 573  ? 0.4355 0.6249 0.4273 0.1017  0.0128  -0.1192 571  ALA A O   
4178  C CB  . ALA A 573  ? 0.3548 0.5268 0.3501 0.0961  0.0159  -0.1043 571  ALA A CB  
4179  N N   . MET A 574  ? 0.3588 0.5272 0.3483 0.0951  0.0114  -0.1098 572  MET A N   
4180  C CA  . MET A 574  ? 0.3921 0.5717 0.3769 0.0968  0.0113  -0.1130 572  MET A CA  
4181  C C   . MET A 574  ? 0.3894 0.5656 0.3788 0.0993  0.0071  -0.1238 572  MET A C   
4182  O O   . MET A 574  ? 0.3677 0.5288 0.3627 0.0979  0.0043  -0.1257 572  MET A O   
4183  C CB  . MET A 574  ? 0.4025 0.5791 0.3815 0.0929  0.0127  -0.1036 572  MET A CB  
4184  C CG  . MET A 574  ? 0.4009 0.5840 0.3754 0.0910  0.0167  -0.0933 572  MET A CG  
4185  S SD  . MET A 574  ? 0.4222 0.5990 0.3916 0.0861  0.0181  -0.0817 572  MET A SD  
4186  C CE  . MET A 574  ? 0.5191 0.7040 0.4858 0.0846  0.0224  -0.0715 572  MET A CE  
4187  N N   . LYS A 575  ? 0.3863 0.5760 0.3738 0.1020  0.0063  -0.1298 573  LYS A N   
4188  C CA  . LYS A 575  ? 0.4020 0.5889 0.3944 0.1032  0.0017  -0.1387 573  LYS A CA  
4189  C C   . LYS A 575  ? 0.3560 0.5400 0.3446 0.1017  0.0009  -0.1375 573  LYS A C   
4190  O O   . LYS A 575  ? 0.3664 0.5606 0.3519 0.1024  0.0000  -0.1394 573  LYS A O   
4191  C CB  . LYS A 575  ? 0.3868 0.5884 0.3802 0.1058  0.0003  -0.1446 573  LYS A CB  
4192  N N   . TRP A 576  ? 0.3201 0.4892 0.3094 0.0990  0.0008  -0.1334 574  TRP A N   
4193  C CA  . TRP A 576  ? 0.3115 0.4749 0.2981 0.0963  -0.0003 -0.1303 574  TRP A CA  
4194  C C   . TRP A 576  ? 0.2785 0.4426 0.2688 0.0988  -0.0043 -0.1410 574  TRP A C   
4195  O O   . TRP A 576  ? 0.3189 0.4753 0.3172 0.0995  -0.0077 -0.1473 574  TRP A O   
4196  C CB  . TRP A 576  ? 0.2828 0.4275 0.2720 0.0917  -0.0008 -0.1232 574  TRP A CB  
4197  C CG  . TRP A 576  ? 0.3013 0.4438 0.2872 0.0888  0.0027  -0.1125 574  TRP A CG  
4198  C CD1 . TRP A 576  ? 0.2934 0.4282 0.2828 0.0877  0.0035  -0.1094 574  TRP A CD1 
4199  C CD2 . TRP A 576  ? 0.2763 0.4243 0.2550 0.0867  0.0059  -0.1034 574  TRP A CD2 
4200  N NE1 . TRP A 576  ? 0.2978 0.4329 0.2827 0.0850  0.0068  -0.0993 574  TRP A NE1 
4201  C CE2 . TRP A 576  ? 0.2761 0.4191 0.2547 0.0843  0.0083  -0.0954 574  TRP A CE2 
4202  C CE3 . TRP A 576  ? 0.2816 0.4382 0.2544 0.0866  0.0067  -0.1012 574  TRP A CE3 
4203  C CZ2 . TRP A 576  ? 0.2870 0.4329 0.2603 0.0817  0.0114  -0.0855 574  TRP A CZ2 
4204  C CZ3 . TRP A 576  ? 0.2996 0.4592 0.2671 0.0841  0.0098  -0.0910 574  TRP A CZ3 
4205  C CH2 . TRP A 576  ? 0.3262 0.4803 0.2943 0.0817  0.0120  -0.0834 574  TRP A CH2 
4206  N N   . THR A 577  ? 0.2876 0.4596 0.2732 0.0987  -0.0045 -0.1410 575  THR A N   
4207  C CA  . THR A 577  ? 0.2713 0.4423 0.2611 0.0993  -0.0089 -0.1485 575  THR A CA  
4208  C C   . THR A 577  ? 0.3216 0.4908 0.3065 0.0976  -0.0088 -0.1455 575  THR A C   
4209  O O   . THR A 577  ? 0.3220 0.4945 0.2998 0.0960  -0.0055 -0.1374 575  THR A O   
4210  C CB  . THR A 577  ? 0.3281 0.5146 0.3187 0.1020  -0.0103 -0.1543 575  THR A CB  
4211  O OG1 . THR A 577  ? 0.3433 0.5439 0.3255 0.1021  -0.0074 -0.1490 575  THR A OG1 
4212  C CG2 . THR A 577  ? 0.3483 0.5378 0.3435 0.1039  -0.0104 -0.1575 575  THR A CG2 
4213  N N   . ALA A 578  ? 0.3099 0.4734 0.2996 0.0974  -0.0129 -0.1515 576  ALA A N   
4214  C CA  . ALA A 578  ? 0.2830 0.4458 0.2690 0.0960  -0.0136 -0.1502 576  ALA A CA  
4215  C C   . ALA A 578  ? 0.3100 0.4794 0.3002 0.0976  -0.0175 -0.1584 576  ALA A C   
4216  O O   . ALA A 578  ? 0.3337 0.4972 0.3324 0.0984  -0.0211 -0.1652 576  ALA A O   
4217  C CB  . ALA A 578  ? 0.3142 0.4589 0.3036 0.0926  -0.0150 -0.1471 576  ALA A CB  
4218  N N   . LEU A 579  ? 0.3137 0.4956 0.2983 0.0982  -0.0169 -0.1575 577  LEU A N   
4219  C CA  . LEU A 579  ? 0.3150 0.5056 0.3029 0.1001  -0.0203 -0.1650 577  LEU A CA  
4220  C C   . LEU A 579  ? 0.3229 0.5140 0.3071 0.0987  -0.0211 -0.1636 577  LEU A C   
4221  O O   . LEU A 579  ? 0.3142 0.5039 0.2914 0.0969  -0.0182 -0.1559 577  LEU A O   
4222  C CB  . LEU A 579  ? 0.3079 0.5170 0.2927 0.1026  -0.0189 -0.1657 577  LEU A CB  
4223  C CG  . LEU A 579  ? 0.3607 0.5732 0.3462 0.1038  -0.0168 -0.1647 577  LEU A CG  
4224  C CD1 . LEU A 579  ? 0.3724 0.6045 0.3542 0.1061  -0.0155 -0.1648 577  LEU A CD1 
4225  C CD2 . LEU A 579  ? 0.4276 0.6312 0.4230 0.1048  -0.0201 -0.1722 577  LEU A CD2 
4226  N N   . PRO A 580  ? 0.2952 0.4886 0.2842 0.0997  -0.0250 -0.1707 578  PRO A N   
4227  C CA  . PRO A 580  ? 0.2912 0.4881 0.2762 0.0988  -0.0256 -0.1695 578  PRO A CA  
4228  C C   . PRO A 580  ? 0.3513 0.5656 0.3283 0.1000  -0.0227 -0.1651 578  PRO A C   
4229  O O   . PRO A 580  ? 0.3639 0.5917 0.3422 0.1025  -0.0236 -0.1695 578  PRO A O   
4230  C CB  . PRO A 580  ? 0.3491 0.5464 0.3423 0.1001  -0.0305 -0.1791 578  PRO A CB  
4231  C CG  . PRO A 580  ? 0.3553 0.5443 0.3574 0.1008  -0.0326 -0.1844 578  PRO A CG  
4232  C CD  . PRO A 580  ? 0.2975 0.4908 0.2960 0.1016  -0.0290 -0.1802 578  PRO A CD  
4233  N N   . GLN A 581  ? 0.2879 0.5022 0.2569 0.0982  -0.0194 -0.1562 579  GLN A N   
4234  C CA  . GLN A 581  ? 0.2954 0.5255 0.2570 0.0988  -0.0164 -0.1501 579  GLN A CA  
4235  C C   . GLN A 581  ? 0.3301 0.5651 0.2886 0.0983  -0.0176 -0.1495 579  GLN A C   
4236  O O   . GLN A 581  ? 0.3491 0.5792 0.3027 0.0962  -0.0161 -0.1429 579  GLN A O   
4237  C CB  . GLN A 581  ? 0.3055 0.5328 0.2611 0.0971  -0.0120 -0.1401 579  GLN A CB  
4238  C CG  . GLN A 581  ? 0.2998 0.5229 0.2583 0.0977  -0.0106 -0.1404 579  GLN A CG  
4239  C CD  . GLN A 581  ? 0.3648 0.6033 0.3236 0.1002  -0.0099 -0.1423 579  GLN A CD  
4240  O OE1 . GLN A 581  ? 0.3669 0.6199 0.3236 0.1015  -0.0104 -0.1431 579  GLN A OE1 
4241  N NE2 . GLN A 581  ? 0.3603 0.5962 0.3219 0.1008  -0.0088 -0.1429 579  GLN A NE2 
4242  N N   . LEU A 582  ? 0.3242 0.5689 0.2861 0.1004  -0.0204 -0.1566 580  LEU A N   
4243  C CA  . LEU A 582  ? 0.3255 0.5764 0.2850 0.1003  -0.0218 -0.1567 580  LEU A CA  
4244  C C   . LEU A 582  ? 0.3423 0.6091 0.2942 0.1007  -0.0187 -0.1491 580  LEU A C   
4245  O O   . LEU A 582  ? 0.3883 0.6624 0.3377 0.1014  -0.0160 -0.1449 580  LEU A O   
4246  C CB  . LEU A 582  ? 0.3555 0.6111 0.3221 0.1025  -0.0260 -0.1673 580  LEU A CB  
4247  C CG  . LEU A 582  ? 0.4277 0.6682 0.4017 0.1014  -0.0298 -0.1737 580  LEU A CG  
4248  C CD1 . LEU A 582  ? 0.3746 0.5999 0.3532 0.1004  -0.0299 -0.1745 580  LEU A CD1 
4249  C CD2 . LEU A 582  ? 0.4696 0.7170 0.4506 0.1038  -0.0339 -0.1838 580  LEU A CD2 
4250  N N   . ALA A 583  ? 0.3266 0.5987 0.2753 0.1002  -0.0193 -0.1470 581  ALA A N   
4251  C CA  . ALA A 583  ? 0.3356 0.6229 0.2778 0.1005  -0.0168 -0.1394 581  ALA A CA  
4252  C C   . ALA A 583  ? 0.3728 0.6771 0.3164 0.1034  -0.0167 -0.1428 581  ALA A C   
4253  O O   . ALA A 583  ? 0.4715 0.7871 0.4107 0.1036  -0.0138 -0.1357 581  ALA A O   
4254  C CB  . ALA A 583  ? 0.3676 0.6585 0.3074 0.0999  -0.0181 -0.1382 581  ALA A CB  
4255  N N   . THR A 584  ? 0.3816 0.6879 0.3318 0.1057  -0.0200 -0.1534 582  THR A N   
4256  C CA  . THR A 584  ? 0.3932 0.7160 0.3456 0.1088  -0.0206 -0.1584 582  THR A CA  
4257  C C   . THR A 584  ? 0.4254 0.7470 0.3801 0.1097  -0.0194 -0.1596 582  THR A C   
4258  O O   . THR A 584  ? 0.4336 0.7689 0.3903 0.1123  -0.0199 -0.1637 582  THR A O   
4259  C CB  . THR A 584  ? 0.4648 0.7902 0.4240 0.1109  -0.0249 -0.1697 582  THR A CB  
4260  O OG1 . THR A 584  ? 0.4621 0.7703 0.4277 0.1101  -0.0274 -0.1758 582  THR A OG1 
4261  C CG2 . THR A 584  ? 0.4370 0.7670 0.3939 0.1104  -0.0260 -0.1687 582  THR A CG2 
4262  N N   . GLY A 585  ? 0.3979 0.7041 0.3526 0.1076  -0.0180 -0.1562 583  GLY A N   
4263  C CA  . GLY A 585  ? 0.3898 0.6937 0.3468 0.1083  -0.0168 -0.1572 583  GLY A CA  
4264  C C   . GLY A 585  ? 0.4305 0.7172 0.3944 0.1079  -0.0192 -0.1637 583  GLY A C   
4265  O O   . GLY A 585  ? 0.4082 0.6856 0.3757 0.1073  -0.0221 -0.1683 583  GLY A O   
4266  N N   . PRO A 586  ? 0.3944 0.6768 0.3606 0.1082  -0.0182 -0.1641 584  PRO A N   
4267  C CA  . PRO A 586  ? 0.3863 0.6523 0.3596 0.1078  -0.0205 -0.1698 584  PRO A CA  
4268  C C   . PRO A 586  ? 0.4349 0.7023 0.4165 0.1099  -0.0252 -0.1809 584  PRO A C   
4269  O O   . PRO A 586  ? 0.4199 0.7023 0.4029 0.1126  -0.0264 -0.1858 584  PRO A O   
4270  C CB  . PRO A 586  ? 0.3933 0.6594 0.3673 0.1084  -0.0183 -0.1681 584  PRO A CB  
4271  C CG  . PRO A 586  ? 0.4481 0.7339 0.4179 0.1103  -0.0164 -0.1660 584  PRO A CG  
4272  C CD  . PRO A 586  ? 0.4541 0.7476 0.4174 0.1093  -0.0152 -0.1600 584  PRO A CD  
4273  N N   . ALA A 587  ? 0.4034 0.6551 0.3908 0.1086  -0.0280 -0.1848 585  ALA A N   
4274  C CA  . ALA A 587  ? 0.3741 0.6246 0.3703 0.1101  -0.0327 -0.1950 585  ALA A CA  
4275  C C   . ALA A 587  ? 0.4321 0.6717 0.4370 0.1105  -0.0348 -0.2001 585  ALA A C   
4276  O O   . ALA A 587  ? 0.3969 0.6253 0.4011 0.1089  -0.0329 -0.1956 585  ALA A O   
4277  C CB  . ALA A 587  ? 0.4076 0.6497 0.4048 0.1083  -0.0349 -0.1956 585  ALA A CB  
4278  N N   . ALA A 588  ? 0.4075 0.6507 0.4208 0.1128  -0.0388 -0.2096 586  ALA A N   
4279  C CA  . ALA A 588  ? 0.4035 0.6365 0.4262 0.1132  -0.0414 -0.2149 586  ALA A CA  
4280  C C   . ALA A 588  ? 0.3767 0.5910 0.4052 0.1106  -0.0439 -0.2152 586  ALA A C   
4281  O O   . ALA A 588  ? 0.4673 0.6784 0.4941 0.1090  -0.0447 -0.2140 586  ALA A O   
4282  C CB  . ALA A 588  ? 0.3688 0.6124 0.3992 0.1167  -0.0451 -0.2251 586  ALA A CB  
4283  N N   . GLY A 589  ? 0.3964 0.5984 0.4319 0.1100  -0.0453 -0.2168 587  GLY A N   
4284  C CA  . GLY A 589  ? 0.3656 0.5501 0.4080 0.1075  -0.0481 -0.2172 587  GLY A CA  
4285  C C   . GLY A 589  ? 0.4345 0.6081 0.4848 0.1073  -0.0494 -0.2185 587  GLY A C   
4286  O O   . GLY A 589  ? 0.4291 0.6089 0.4800 0.1093  -0.0485 -0.2200 587  GLY A O   
4287  N N   . GLU A 590  ? 0.4004 0.5577 0.4571 0.1047  -0.0518 -0.2177 588  GLU A N   
4288  C CA  . GLU A 590  ? 0.4069 0.5522 0.4715 0.1040  -0.0532 -0.2179 588  GLU A CA  
4289  C C   . GLU A 590  ? 0.3703 0.5115 0.4277 0.1029  -0.0486 -0.2099 588  GLU A C   
4290  O O   . GLU A 590  ? 0.3927 0.5293 0.4427 0.1006  -0.0457 -0.2029 588  GLU A O   
4291  C CB  . GLU A 590  ? 0.4939 0.6233 0.5671 0.1013  -0.0568 -0.2181 588  GLU A CB  
4292  N N   . THR A 591  ? 0.3780 0.5213 0.4379 0.1045  -0.0479 -0.2111 589  THR A N   
4293  C CA  . THR A 591  ? 0.3668 0.5086 0.4201 0.1040  -0.0435 -0.2042 589  THR A CA  
4294  C C   . THR A 591  ? 0.3750 0.5018 0.4360 0.1026  -0.0448 -0.2028 589  THR A C   
4295  O O   . THR A 591  ? 0.4035 0.5273 0.4747 0.1036  -0.0486 -0.2085 589  THR A O   
4296  C CB  . THR A 591  ? 0.4232 0.5811 0.4726 0.1071  -0.0413 -0.2061 589  THR A CB  
4297  O OG1 . THR A 591  ? 0.4329 0.6050 0.4743 0.1081  -0.0397 -0.2059 589  THR A OG1 
4298  C CG2 . THR A 591  ? 0.3920 0.5480 0.4364 0.1067  -0.0371 -0.1996 589  THR A CG2 
4299  N N   . ARG A 592  ? 0.3392 0.4569 0.3957 0.1002  -0.0417 -0.1950 590  ARG A N   
4300  C CA  . ARG A 592  ? 0.3953 0.4994 0.4581 0.0988  -0.0425 -0.1925 590  ARG A CA  
4301  C C   . ARG A 592  ? 0.3674 0.4708 0.4223 0.0982  -0.0375 -0.1849 590  ARG A C   
4302  O O   . ARG A 592  ? 0.3478 0.4582 0.3926 0.0980  -0.0337 -0.1806 590  ARG A O   
4303  C CB  . ARG A 592  ? 0.4202 0.5088 0.4895 0.0957  -0.0456 -0.1911 590  ARG A CB  
4304  C CG  . ARG A 592  ? 0.4253 0.5088 0.4869 0.0930  -0.0431 -0.1844 590  ARG A CG  
4305  C CD  . ARG A 592  ? 0.4467 0.5136 0.5152 0.0897  -0.0457 -0.1816 590  ARG A CD  
4306  N NE  . ARG A 592  ? 0.4781 0.5410 0.5400 0.0872  -0.0440 -0.1765 590  ARG A NE  
4307  C CZ  . ARG A 592  ? 0.4552 0.5152 0.5097 0.0860  -0.0400 -0.1695 590  ARG A CZ  
4308  N NH1 . ARG A 592  ? 0.4378 0.4981 0.4905 0.0869  -0.0373 -0.1665 590  ARG A NH1 
4309  N NH2 . ARG A 592  ? 0.4677 0.5247 0.5166 0.0832  -0.0388 -0.1641 590  ARG A NH2 
4310  N N   . THR A 593  ? 0.3422 0.4371 0.4019 0.0978  -0.0375 -0.1830 591  THR A N   
4311  C CA  . THR A 593  ? 0.3469 0.4401 0.4004 0.0971  -0.0330 -0.1757 591  THR A CA  
4312  C C   . THR A 593  ? 0.3691 0.4504 0.4198 0.0939  -0.0320 -0.1691 591  THR A C   
4313  O O   . THR A 593  ? 0.3585 0.4298 0.4145 0.0918  -0.0352 -0.1698 591  THR A O   
4314  C CB  . THR A 593  ? 0.4013 0.4898 0.4612 0.0979  -0.0335 -0.1759 591  THR A CB  
4315  O OG1 . THR A 593  ? 0.4356 0.5104 0.5060 0.0962  -0.0379 -0.1773 591  THR A OG1 
4316  C CG2 . THR A 593  ? 0.4084 0.5098 0.4698 0.1012  -0.0340 -0.1820 591  THR A CG2 
4317  N N   . VAL A 594  ? 0.2980 0.3812 0.3406 0.0934  -0.0274 -0.1626 592  VAL A N   
4318  C CA  . VAL A 594  ? 0.3194 0.3914 0.3592 0.0887  -0.0260 -0.1525 592  VAL A CA  
4319  C C   . VAL A 594  ? 0.3313 0.3959 0.3738 0.0873  -0.0248 -0.1470 592  VAL A C   
4320  O O   . VAL A 594  ? 0.3275 0.3996 0.3665 0.0889  -0.0218 -0.1455 592  VAL A O   
4321  C CB  . VAL A 594  ? 0.3066 0.3858 0.3353 0.0870  -0.0221 -0.1455 592  VAL A CB  
4322  C CG1 . VAL A 594  ? 0.3262 0.3940 0.3523 0.0819  -0.0206 -0.1346 592  VAL A CG1 
4323  C CG2 . VAL A 594  ? 0.3484 0.4353 0.3745 0.0885  -0.0235 -0.1510 592  VAL A CG2 
4324  N N   . LEU A 595  ? 0.3302 0.3807 0.3792 0.0843  -0.0272 -0.1439 593  LEU A N   
4325  C CA  . LEU A 595  ? 0.3157 0.3585 0.3686 0.0831  -0.0268 -0.1394 593  LEU A CA  
4326  C C   . LEU A 595  ? 0.3110 0.3465 0.3586 0.0782  -0.0241 -0.1278 593  LEU A C   
4327  O O   . LEU A 595  ? 0.3254 0.3564 0.3706 0.0752  -0.0244 -0.1241 593  LEU A O   
4328  C CB  . LEU A 595  ? 0.3193 0.3517 0.3842 0.0833  -0.0316 -0.1440 593  LEU A CB  
4329  C CG  . LEU A 595  ? 0.3368 0.3746 0.4092 0.0881  -0.0351 -0.1563 593  LEU A CG  
4330  C CD1 . LEU A 595  ? 0.3966 0.4227 0.4813 0.0869  -0.0399 -0.1580 593  LEU A CD1 
4331  C CD2 . LEU A 595  ? 0.3530 0.4026 0.4228 0.0917  -0.0328 -0.1594 593  LEU A CD2 
4332  N N   . ASN A 596  ? 0.2912 0.3260 0.3373 0.0776  -0.0216 -0.1225 594  ASN A N   
4333  C CA  . ASN A 596  ? 0.2925 0.3202 0.3345 0.0732  -0.0193 -0.1120 594  ASN A CA  
4334  C C   . ASN A 596  ? 0.2817 0.2960 0.3305 0.0700  -0.0225 -0.1098 594  ASN A C   
4335  O O   . ASN A 596  ? 0.2940 0.3028 0.3512 0.0709  -0.0253 -0.1127 594  ASN A O   
4336  C CB  . ASN A 596  ? 0.2747 0.3046 0.3159 0.0738  -0.0167 -0.1086 594  ASN A CB  
4337  C CG  . ASN A 596  ? 0.2920 0.3165 0.3283 0.0697  -0.0139 -0.0982 594  ASN A CG  
4338  O OD1 . ASN A 596  ? 0.2821 0.2977 0.3189 0.0661  -0.0149 -0.0936 594  ASN A OD1 
4339  N ND2 . ASN A 596  ? 0.3120 0.3423 0.3440 0.0702  -0.0106 -0.0947 594  ASN A ND2 
4340  N N   . PRO A 597  ? 0.2822 0.2912 0.3281 0.0664  -0.0224 -0.1045 595  PRO A N   
4341  C CA  . PRO A 597  ? 0.2724 0.2695 0.3248 0.0633  -0.0255 -0.1021 595  PRO A CA  
4342  C C   . PRO A 597  ? 0.2963 0.2862 0.3521 0.0614  -0.0253 -0.0965 595  PRO A C   
4343  O O   . PRO A 597  ? 0.2737 0.2548 0.3371 0.0597  -0.0284 -0.0958 595  PRO A O   
4344  C CB  . PRO A 597  ? 0.3077 0.3030 0.3544 0.0599  -0.0243 -0.0968 595  PRO A CB  
4345  C CG  . PRO A 597  ? 0.2923 0.2961 0.3293 0.0604  -0.0200 -0.0935 595  PRO A CG  
4346  C CD  . PRO A 597  ? 0.2698 0.2838 0.3066 0.0650  -0.0194 -0.1003 595  PRO A CD  
4347  N N   . GLY A 598  ? 0.2732 0.2668 0.3237 0.0614  -0.0217 -0.0922 596  GLY A N   
4348  C CA  . GLY A 598  ? 0.2561 0.2440 0.3095 0.0599  -0.0214 -0.0872 596  GLY A CA  
4349  C C   . GLY A 598  ? 0.2898 0.2785 0.3500 0.0631  -0.0230 -0.0922 596  GLY A C   
4350  O O   . GLY A 598  ? 0.3109 0.2943 0.3749 0.0619  -0.0235 -0.0885 596  GLY A O   
4351  N N   . ASP A 599  ? 0.2687 0.2645 0.3308 0.0672  -0.0241 -0.1007 597  ASP A N   
4352  C CA  . ASP A 599  ? 0.2970 0.2948 0.3660 0.0707  -0.0257 -0.1066 597  ASP A CA  
4353  C C   . ASP A 599  ? 0.2876 0.2932 0.3583 0.0749  -0.0273 -0.1167 597  ASP A C   
4354  O O   . ASP A 599  ? 0.2881 0.3047 0.3522 0.0773  -0.0245 -0.1190 597  ASP A O   
4355  C CB  . ASP A 599  ? 0.2827 0.2863 0.3472 0.0718  -0.0221 -0.1036 597  ASP A CB  
4356  C CG  . ASP A 599  ? 0.3062 0.3109 0.3782 0.0752  -0.0238 -0.1088 597  ASP A CG  
4357  O OD1 . ASP A 599  ? 0.3175 0.3218 0.3972 0.0779  -0.0274 -0.1168 597  ASP A OD1 
4358  O OD2 . ASP A 599  ? 0.3379 0.3440 0.4085 0.0751  -0.0215 -0.1049 597  ASP A OD2 
4359  N N   . HIS A 600  ? 0.2933 0.2937 0.3729 0.0758  -0.0318 -0.1225 598  HIS A N   
4360  C CA  . HIS A 600  ? 0.3417 0.3492 0.4236 0.0796  -0.0338 -0.1327 598  HIS A CA  
4361  C C   . HIS A 600  ? 0.3511 0.3687 0.4341 0.0846  -0.0331 -0.1399 598  HIS A C   
4362  O O   . HIS A 600  ? 0.3695 0.3961 0.4520 0.0881  -0.0337 -0.1482 598  HIS A O   
4363  C CB  . HIS A 600  ? 0.3258 0.3247 0.4183 0.0793  -0.0392 -0.1373 598  HIS A CB  
4364  C CG  . HIS A 600  ? 0.3520 0.3443 0.4426 0.0751  -0.0399 -0.1323 598  HIS A CG  
4365  N ND1 . HIS A 600  ? 0.3889 0.3733 0.4885 0.0739  -0.0445 -0.1349 598  HIS A ND1 
4366  C CD2 . HIS A 600  ? 0.3597 0.3524 0.4409 0.0718  -0.0367 -0.1249 598  HIS A CD2 
4367  C CE1 . HIS A 600  ? 0.4106 0.3911 0.5060 0.0701  -0.0439 -0.1293 598  HIS A CE1 
4368  N NE2 . HIS A 600  ? 0.4020 0.3875 0.4863 0.0688  -0.0392 -0.1233 598  HIS A NE2 
4369  N N   . ARG A 601  ? 0.3045 0.3214 0.3888 0.0851  -0.0318 -0.1370 599  ARG A N   
4370  C CA  . ARG A 601  ? 0.3274 0.3548 0.4121 0.0897  -0.0306 -0.1431 599  ARG A CA  
4371  C C   . ARG A 601  ? 0.3407 0.3809 0.4140 0.0905  -0.0257 -0.1413 599  ARG A C   
4372  O O   . ARG A 601  ? 0.3614 0.4131 0.4339 0.0947  -0.0247 -0.1475 599  ARG A O   
4373  C CB  . ARG A 601  ? 0.3185 0.3413 0.4079 0.0896  -0.0305 -0.1398 599  ARG A CB  
4374  C CG  . ARG A 601  ? 0.3337 0.3439 0.4348 0.0886  -0.0353 -0.1404 599  ARG A CG  
4375  C CD  . ARG A 601  ? 0.3760 0.3813 0.4801 0.0876  -0.0346 -0.1348 599  ARG A CD  
4376  N NE  . ARG A 601  ? 0.3470 0.3501 0.4424 0.0833  -0.0308 -0.1240 599  ARG A NE  
4377  C CZ  . ARG A 601  ? 0.3726 0.3724 0.4679 0.0818  -0.0294 -0.1176 599  ARG A CZ  
4378  N NH1 . ARG A 601  ? 0.3893 0.3874 0.4928 0.0840  -0.0314 -0.1204 599  ARG A NH1 
4379  N NH2 . ARG A 601  ? 0.3448 0.3435 0.4321 0.0780  -0.0260 -0.1086 599  ARG A NH2 
4380  N N   . ASP A 602  ? 0.3030 0.3418 0.3679 0.0867  -0.0229 -0.1329 600  ASP A N   
4381  C CA  . ASP A 602  ? 0.3280 0.3781 0.3825 0.0870  -0.0184 -0.1297 600  ASP A CA  
4382  C C   . ASP A 602  ? 0.3587 0.4156 0.4096 0.0882  -0.0190 -0.1347 600  ASP A C   
4383  O O   . ASP A 602  ? 0.3287 0.3803 0.3770 0.0852  -0.0194 -0.1311 600  ASP A O   
4384  C CB  . ASP A 602  ? 0.3053 0.3500 0.3534 0.0823  -0.0153 -0.1183 600  ASP A CB  
4385  C CG  . ASP A 602  ? 0.3508 0.4064 0.3889 0.0823  -0.0109 -0.1143 600  ASP A CG  
4386  O OD1 . ASP A 602  ? 0.3451 0.4132 0.3814 0.0860  -0.0097 -0.1195 600  ASP A OD1 
4387  O OD2 . ASP A 602  ? 0.3175 0.3697 0.3500 0.0786  -0.0087 -0.1059 600  ASP A OD2 
4388  N N   . VAL A 603  ? 0.3469 0.4161 0.3977 0.0928  -0.0190 -0.1431 601  VAL A N   
4389  C CA  . VAL A 603  ? 0.3237 0.4014 0.3707 0.0944  -0.0194 -0.1482 601  VAL A CA  
4390  C C   . VAL A 603  ? 0.3355 0.4221 0.3714 0.0929  -0.0148 -0.1412 601  VAL A C   
4391  O O   . VAL A 603  ? 0.3457 0.4416 0.3775 0.0943  -0.0115 -0.1391 601  VAL A O   
4392  C CB  . VAL A 603  ? 0.3798 0.4678 0.4309 0.0988  -0.0215 -0.1586 601  VAL A CB  
4393  C CG1 . VAL A 603  ? 0.3435 0.4405 0.3902 0.0993  -0.0221 -0.1622 601  VAL A CG1 
4394  C CG2 . VAL A 603  ? 0.3674 0.4455 0.4301 0.0986  -0.0264 -0.1630 601  VAL A CG2 
4395  N N   . VAL A 604  ? 0.3078 0.3917 0.3391 0.0902  -0.0147 -0.1373 602  VAL A N   
4396  C CA  . VAL A 604  ? 0.3226 0.4134 0.3441 0.0884  -0.0107 -0.1299 602  VAL A CA  
4397  C C   . VAL A 604  ? 0.3101 0.4164 0.3266 0.0917  -0.0099 -0.1353 602  VAL A C   
4398  O O   . VAL A 604  ? 0.3220 0.4394 0.3316 0.0922  -0.0063 -0.1314 602  VAL A O   
4399  C CB  . VAL A 604  ? 0.3022 0.3820 0.3214 0.0837  -0.0109 -0.1224 602  VAL A CB  
4400  C CG1 . VAL A 604  ? 0.2868 0.3728 0.2967 0.0818  -0.0069 -0.1144 602  VAL A CG1 
4401  C CG2 . VAL A 604  ? 0.3048 0.3700 0.3291 0.0806  -0.0119 -0.1176 602  VAL A CG2 
4402  N N   . GLY A 605  ? 0.2976 0.4054 0.3180 0.0940  -0.0133 -0.1444 603  GLY A N   
4403  C CA  . GLY A 605  ? 0.2792 0.4023 0.2951 0.0973  -0.0128 -0.1501 603  GLY A CA  
4404  C C   . GLY A 605  ? 0.2810 0.4026 0.3031 0.0983  -0.0176 -0.1588 603  GLY A C   
4405  O O   . GLY A 605  ? 0.3458 0.4565 0.3768 0.0978  -0.0212 -0.1622 603  GLY A O   
4406  N N   . SER A 606  ? 0.3036 0.4364 0.3215 0.0992  -0.0178 -0.1611 604  SER A N   
4407  C CA  A SER A 606  ? 0.2929 0.4261 0.3164 0.0999  -0.0223 -0.1687 604  SER A CA  
4408  C CA  B SER A 606  ? 0.2930 0.4266 0.3164 0.1000  -0.0223 -0.1687 604  SER A CA  
4409  C C   . SER A 606  ? 0.3408 0.4776 0.3585 0.0989  -0.0222 -0.1674 604  SER A C   
4410  O O   . SER A 606  ? 0.3289 0.4754 0.3377 0.0989  -0.0187 -0.1627 604  SER A O   
4411  C CB  A SER A 606  ? 0.3236 0.4700 0.3496 0.1030  -0.0236 -0.1752 604  SER A CB  
4412  C CB  B SER A 606  ? 0.3228 0.4706 0.3479 0.1031  -0.0232 -0.1748 604  SER A CB  
4413  O OG  A SER A 606  ? 0.3356 0.4778 0.3682 0.1040  -0.0245 -0.1772 604  SER A OG  
4414  O OG  B SER A 606  ? 0.3313 0.4817 0.3614 0.1040  -0.0274 -0.1822 604  SER A OG  
4415  N N   . VAL A 607  ? 0.3076 0.4364 0.3307 0.0978  -0.0261 -0.1713 605  VAL A N   
4416  C CA  . VAL A 607  ? 0.3249 0.4563 0.3437 0.0968  -0.0265 -0.1709 605  VAL A CA  
4417  C C   . VAL A 607  ? 0.3105 0.4483 0.3348 0.0985  -0.0306 -0.1793 605  VAL A C   
4418  O O   . VAL A 607  ? 0.3414 0.4729 0.3755 0.0989  -0.0345 -0.1849 605  VAL A O   
4419  C CB  . VAL A 607  ? 0.3215 0.4377 0.3411 0.0937  -0.0272 -0.1671 605  VAL A CB  
4420  C CG1 . VAL A 607  ? 0.3442 0.4467 0.3752 0.0926  -0.0315 -0.1709 605  VAL A CG1 
4421  C CG2 . VAL A 607  ? 0.3260 0.4458 0.3411 0.0928  -0.0278 -0.1670 605  VAL A CG2 
4422  N N   . THR A 608  ? 0.3084 0.4591 0.3269 0.0995  -0.0299 -0.1800 606  THR A N   
4423  C CA  . THR A 608  ? 0.3166 0.4736 0.3395 0.1009  -0.0337 -0.1875 606  THR A CA  
4424  C C   . THR A 608  ? 0.3296 0.4809 0.3507 0.0987  -0.0348 -0.1858 606  THR A C   
4425  O O   . THR A 608  ? 0.3260 0.4817 0.3381 0.0978  -0.0317 -0.1801 606  THR A O   
4426  C CB  . THR A 608  ? 0.3302 0.5065 0.3480 0.1037  -0.0323 -0.1893 606  THR A CB  
4427  O OG1 . THR A 608  ? 0.3368 0.5184 0.3562 0.1056  -0.0312 -0.1906 606  THR A OG1 
4428  C CG2 . THR A 608  ? 0.3510 0.5345 0.3737 0.1054  -0.0363 -0.1974 606  THR A CG2 
4429  N N   . GLU A 609  ? 0.3191 0.4605 0.3489 0.0977  -0.0390 -0.1904 607  GLU A N   
4430  C CA  . GLU A 609  ? 0.3547 0.4889 0.3835 0.0953  -0.0402 -0.1886 607  GLU A CA  
4431  C C   . GLU A 609  ? 0.3536 0.4991 0.3814 0.0966  -0.0420 -0.1932 607  GLU A C   
4432  O O   . GLU A 609  ? 0.3382 0.4947 0.3693 0.0993  -0.0437 -0.1995 607  GLU A O   
4433  C CB  . GLU A 609  ? 0.3913 0.5084 0.4297 0.0929  -0.0436 -0.1896 607  GLU A CB  
4434  C CG  . GLU A 609  ? 0.4401 0.5463 0.4778 0.0913  -0.0411 -0.1834 607  GLU A CG  
4435  C CD  . GLU A 609  ? 0.4886 0.5777 0.5348 0.0885  -0.0441 -0.1826 607  GLU A CD  
4436  O OE1 . GLU A 609  ? 0.5544 0.6399 0.6106 0.0886  -0.0485 -0.1881 607  GLU A OE1 
4437  O OE2 . GLU A 609  ? 0.4694 0.5490 0.5128 0.0862  -0.0420 -0.1761 607  GLU A OE2 
4438  N N   . THR A 610  ? 0.3402 0.4835 0.3635 0.0946  -0.0416 -0.1899 608  THR A N   
4439  C CA  . THR A 610  ? 0.3218 0.4764 0.3422 0.0956  -0.0426 -0.1926 608  THR A CA  
4440  C C   . THR A 610  ? 0.3851 0.5344 0.4155 0.0954  -0.0477 -0.1996 608  THR A C   
4441  O O   . THR A 610  ? 0.3999 0.5347 0.4357 0.0928  -0.0497 -0.1988 608  THR A O   
4442  C CB  . THR A 610  ? 0.3369 0.4910 0.3478 0.0936  -0.0399 -0.1854 608  THR A CB  
4443  O OG1 . THR A 610  ? 0.3263 0.4836 0.3289 0.0935  -0.0352 -0.1782 608  THR A OG1 
4444  C CG2 . THR A 610  ? 0.3626 0.5299 0.3698 0.0947  -0.0405 -0.1874 608  THR A CG2 
4445  N N   . SER A 611  ? 0.3647 0.5262 0.3979 0.0980  -0.0499 -0.2064 609  SER A N   
4446  C CA  . SER A 611  ? 0.3878 0.5461 0.4298 0.0978  -0.0546 -0.2128 609  SER A CA  
4447  C C   . SER A 611  ? 0.4078 0.5641 0.4451 0.0956  -0.0544 -0.2094 609  SER A C   
4448  O O   . SER A 611  ? 0.3604 0.5231 0.3873 0.0953  -0.0510 -0.2039 609  SER A O   
4449  C CB  . SER A 611  ? 0.4076 0.5809 0.4532 0.1015  -0.0567 -0.2209 609  SER A CB  
4450  O OG  . SER A 611  ? 0.4091 0.5970 0.4460 0.1027  -0.0547 -0.2195 609  SER A OG  
4451  N N   . GLU A 612  ? 0.4206 0.5677 0.4658 0.0940  -0.0583 -0.2126 610  GLU A N   
4452  C CA  . GLU A 612  ? 0.4177 0.5631 0.4592 0.0919  -0.0585 -0.2100 610  GLU A CA  
4453  C C   . GLU A 612  ? 0.4060 0.5681 0.4423 0.0942  -0.0581 -0.2126 610  GLU A C   
4454  O O   . GLU A 612  ? 0.4231 0.5880 0.4517 0.0931  -0.0564 -0.2082 610  GLU A O   
4455  C CB  . GLU A 612  ? 0.5407 0.6731 0.5925 0.0896  -0.0628 -0.2128 610  GLU A CB  
4456  C CG  . GLU A 612  ? 0.5298 0.6453 0.5838 0.0862  -0.0623 -0.2072 610  GLU A CG  
4457  C CD  . GLU A 612  ? 0.6420 0.7453 0.7091 0.0844  -0.0670 -0.2105 610  GLU A CD  
4458  O OE1 . GLU A 612  ? 0.6895 0.7922 0.7609 0.0835  -0.0699 -0.2133 610  GLU A OE1 
4459  O OE2 . GLU A 612  ? 0.6569 0.7514 0.7301 0.0838  -0.0677 -0.2099 610  GLU A OE2 
4460  N N   . GLU A 613  ? 0.3769 0.5506 0.4172 0.0976  -0.0596 -0.2195 611  GLU A N   
4461  C CA  . GLU A 613  ? 0.4362 0.6273 0.4714 0.1001  -0.0590 -0.2216 611  GLU A CA  
4462  C C   . GLU A 613  ? 0.3831 0.5833 0.4059 0.1004  -0.0540 -0.2142 611  GLU A C   
4463  O O   . GLU A 613  ? 0.3535 0.5621 0.3692 0.1003  -0.0526 -0.2111 611  GLU A O   
4464  C CB  . GLU A 613  ? 0.4475 0.6494 0.4900 0.1038  -0.0617 -0.2307 611  GLU A CB  
4465  N N   . ASP A 614  ? 0.3761 0.5749 0.3965 0.1007  -0.0514 -0.2109 612  ASP A N   
4466  C CA  . ASP A 614  ? 0.3488 0.5565 0.3581 0.1010  -0.0467 -0.2035 612  ASP A CA  
4467  C C   . ASP A 614  ? 0.3670 0.5661 0.3691 0.0978  -0.0441 -0.1948 612  ASP A C   
4468  O O   . ASP A 614  ? 0.3300 0.5379 0.3228 0.0977  -0.0410 -0.1887 612  ASP A O   
4469  C CB  . ASP A 614  ? 0.3733 0.5825 0.3826 0.1022  -0.0447 -0.2027 612  ASP A CB  
4470  C CG  . ASP A 614  ? 0.3556 0.5786 0.3692 0.1059  -0.0462 -0.2101 612  ASP A CG  
4471  O OD1 . ASP A 614  ? 0.4011 0.6368 0.4144 0.1077  -0.0475 -0.2139 612  ASP A OD1 
4472  O OD2 . ASP A 614  ? 0.4080 0.6296 0.4255 0.1071  -0.0462 -0.2123 612  ASP A OD2 
4473  N N   . ALA A 615  ? 0.3460 0.5283 0.3523 0.0950  -0.0455 -0.1939 613  ALA A N   
4474  C CA  . ALA A 615  ? 0.3400 0.5142 0.3400 0.0920  -0.0436 -0.1865 613  ALA A CA  
4475  C C   . ALA A 615  ? 0.3250 0.5063 0.3213 0.0918  -0.0444 -0.1862 613  ALA A C   
4476  O O   . ALA A 615  ? 0.3256 0.5113 0.3130 0.0909  -0.0415 -0.1794 613  ALA A O   
4477  C CB  . ALA A 615  ? 0.3434 0.4990 0.3499 0.0892  -0.0455 -0.1864 613  ALA A CB  
4478  N N   . ARG A 616  ? 0.3627 0.5458 0.3661 0.0926  -0.0484 -0.1936 614  ARG A N   
4479  C CA  . ARG A 616  ? 0.3928 0.5838 0.3933 0.0926  -0.0493 -0.1939 614  ARG A CA  
4480  C C   . ARG A 616  ? 0.3454 0.5549 0.3383 0.0951  -0.0467 -0.1919 614  ARG A C   
4481  O O   . ARG A 616  ? 0.3489 0.5643 0.3347 0.0945  -0.0452 -0.1869 614  ARG A O   
4482  C CB  . ARG A 616  ? 0.4492 0.6388 0.4598 0.0933  -0.0541 -0.2027 614  ARG A CB  
4483  C CG  . ARG A 616  ? 0.4341 0.6066 0.4509 0.0900  -0.0567 -0.2029 614  ARG A CG  
4484  C CD  . ARG A 616  ? 0.5571 0.7285 0.5849 0.0906  -0.0615 -0.2114 614  ARG A CD  
4485  N NE  . ARG A 616  ? 0.6155 0.7753 0.6536 0.0901  -0.0640 -0.2150 614  ARG A NE  
4486  C CZ  . ARG A 616  ? 0.5421 0.7064 0.5877 0.0928  -0.0660 -0.2218 614  ARG A CZ  
4487  N NH1 . ARG A 616  ? 0.6165 0.7969 0.6606 0.0963  -0.0660 -0.2264 614  ARG A NH1 
4488  N NH2 . ARG A 616  ? 0.5601 0.7128 0.6151 0.0919  -0.0683 -0.2240 614  ARG A NH2 
4489  N N   . ARG A 617  ? 0.3284 0.5473 0.3230 0.0979  -0.0463 -0.1954 615  ARG A N   
4490  C CA  . ARG A 617  ? 0.3396 0.5765 0.3272 0.1002  -0.0437 -0.1928 615  ARG A CA  
4491  C C   . ARG A 617  ? 0.3736 0.6107 0.3512 0.0986  -0.0392 -0.1822 615  ARG A C   
4492  O O   . ARG A 617  ? 0.3340 0.5825 0.3047 0.0989  -0.0373 -0.1772 615  ARG A O   
4493  C CB  . ARG A 617  ? 0.3719 0.6181 0.3636 0.1033  -0.0441 -0.1984 615  ARG A CB  
4494  C CG  . ARG A 617  ? 0.4264 0.6926 0.4122 0.1058  -0.0420 -0.1967 615  ARG A CG  
4495  C CD  . ARG A 617  ? 0.4693 0.7465 0.4615 0.1093  -0.0441 -0.2055 615  ARG A CD  
4496  N NE  . ARG A 617  ? 0.4753 0.7462 0.4715 0.1097  -0.0439 -0.2072 615  ARG A NE  
4497  C CZ  . ARG A 617  ? 0.5273 0.8047 0.5190 0.1105  -0.0407 -0.2030 615  ARG A CZ  
4498  N NH1 . ARG A 617  ? 0.5267 0.8165 0.5098 0.1107  -0.0373 -0.1960 615  ARG A NH1 
4499  N NH2 . ARG A 617  ? 0.4752 0.7467 0.4715 0.1111  -0.0409 -0.2056 615  ARG A NH2 
4500  N N   . ALA A 618  ? 0.3308 0.5554 0.3081 0.0968  -0.0376 -0.1783 616  ALA A N   
4501  C CA  . ALA A 618  ? 0.3382 0.5624 0.3067 0.0953  -0.0333 -0.1682 616  ALA A CA  
4502  C C   . ALA A 618  ? 0.3082 0.5302 0.2713 0.0932  -0.0329 -0.1627 616  ALA A C   
4503  O O   . ALA A 618  ? 0.3181 0.5484 0.2734 0.0930  -0.0300 -0.1551 616  ALA A O   
4504  C CB  . ALA A 618  ? 0.3288 0.5390 0.2988 0.0938  -0.0319 -0.1659 616  ALA A CB  
4505  N N   . VAL A 619  ? 0.2958 0.5069 0.2633 0.0915  -0.0359 -0.1661 617  VAL A N   
4506  C CA  . VAL A 619  ? 0.3155 0.5246 0.2783 0.0895  -0.0357 -0.1612 617  VAL A CA  
4507  C C   . VAL A 619  ? 0.3226 0.5480 0.2818 0.0911  -0.0358 -0.1610 617  VAL A C   
4508  O O   . VAL A 619  ? 0.3435 0.5739 0.2955 0.0903  -0.0338 -0.1536 617  VAL A O   
4509  C CB  . VAL A 619  ? 0.3193 0.5137 0.2883 0.0872  -0.0391 -0.1651 617  VAL A CB  
4510  C CG1 . VAL A 619  ? 0.3320 0.5254 0.2961 0.0853  -0.0392 -0.1604 617  VAL A CG1 
4511  C CG2 . VAL A 619  ? 0.2968 0.4754 0.2690 0.0854  -0.0387 -0.1641 617  VAL A CG2 
4512  N N   . ARG A 620  ? 0.3028 0.5372 0.2673 0.0936  -0.0383 -0.1690 618  ARG A N   
4513  C CA  . ARG A 620  ? 0.3475 0.5983 0.3090 0.0954  -0.0384 -0.1692 618  ARG A CA  
4514  C C   . ARG A 620  ? 0.3278 0.5916 0.2818 0.0965  -0.0345 -0.1618 618  ARG A C   
4515  O O   . ARG A 620  ? 0.3609 0.6342 0.3092 0.0964  -0.0332 -0.1561 618  ARG A O   
4516  C CB  . ARG A 620  ? 0.3873 0.6453 0.3564 0.0981  -0.0418 -0.1796 618  ARG A CB  
4517  C CG  . ARG A 620  ? 0.4208 0.6680 0.3975 0.0969  -0.0459 -0.1862 618  ARG A CG  
4518  C CD  . ARG A 620  ? 0.5206 0.7762 0.5049 0.0997  -0.0493 -0.1965 618  ARG A CD  
4519  N NE  . ARG A 620  ? 0.5647 0.8102 0.5585 0.1000  -0.0518 -0.2033 618  ARG A NE  
4520  C CZ  . ARG A 620  ? 0.5055 0.7563 0.5029 0.1024  -0.0520 -0.2078 618  ARG A CZ  
4521  N NH1 . ARG A 620  ? 0.5835 0.8504 0.5763 0.1049  -0.0498 -0.2067 618  ARG A NH1 
4522  N NH2 . ARG A 620  ? 0.5466 0.7865 0.5529 0.1023  -0.0544 -0.2132 618  ARG A NH2 
4523  N N   . LEU A 621  ? 0.2951 0.5596 0.2494 0.0974  -0.0327 -0.1613 619  LEU A N   
4524  C CA  . LEU A 621  ? 0.3499 0.6257 0.2976 0.0980  -0.0289 -0.1535 619  LEU A CA  
4525  C C   . LEU A 621  ? 0.3452 0.6152 0.2858 0.0953  -0.0260 -0.1427 619  LEU A C   
4526  O O   . LEU A 621  ? 0.3545 0.6355 0.2894 0.0953  -0.0238 -0.1352 619  LEU A O   
4527  C CB  . LEU A 621  ? 0.3157 0.5913 0.2657 0.0992  -0.0276 -0.1553 619  LEU A CB  
4528  C CG  . LEU A 621  ? 0.3420 0.6263 0.2985 0.1023  -0.0300 -0.1651 619  LEU A CG  
4529  C CD1 . LEU A 621  ? 0.3540 0.6353 0.3129 0.1030  -0.0288 -0.1662 619  LEU A CD1 
4530  C CD2 . LEU A 621  ? 0.3514 0.6561 0.3052 0.1046  -0.0296 -0.1647 619  LEU A CD2 
4531  N N   . ALA A 622  ? 0.3292 0.5823 0.2707 0.0930  -0.0262 -0.1415 620  ALA A N   
4532  C CA  . ALA A 622  ? 0.3501 0.5971 0.2855 0.0904  -0.0238 -0.1319 620  ALA A CA  
4533  C C   . ALA A 622  ? 0.3258 0.5781 0.2580 0.0898  -0.0248 -0.1289 620  ALA A C   
4534  O O   . ALA A 622  ? 0.3216 0.5794 0.2477 0.0890  -0.0224 -0.1198 620  ALA A O   
4535  C CB  . ALA A 622  ? 0.3261 0.5542 0.2639 0.0882  -0.0244 -0.1327 620  ALA A CB  
4536  N N   . ALA A 623  ? 0.3148 0.5655 0.2515 0.0901  -0.0283 -0.1364 621  ALA A N   
4537  C CA  . ALA A 623  ? 0.3169 0.5730 0.2511 0.0896  -0.0295 -0.1343 621  ALA A CA  
4538  C C   . ALA A 623  ? 0.3265 0.6013 0.2568 0.0915  -0.0279 -0.1305 621  ALA A C   
4539  O O   . ALA A 623  ? 0.3577 0.6376 0.2830 0.0906  -0.0267 -0.1229 621  ALA A O   
4540  C CB  . ALA A 623  ? 0.3604 0.6124 0.3011 0.0899  -0.0336 -0.1438 621  ALA A CB  
4541  N N   . ASP A 624  ? 0.3355 0.6211 0.2685 0.0941  -0.0280 -0.1356 622  ASP A N   
4542  C CA  . ASP A 624  ? 0.3842 0.6886 0.3140 0.0960  -0.0265 -0.1321 622  ASP A CA  
4543  C C   . ASP A 624  ? 0.3957 0.7033 0.3193 0.0948  -0.0226 -0.1204 622  ASP A C   
4544  O O   . ASP A 624  ? 0.4314 0.7508 0.3510 0.0949  -0.0213 -0.1136 622  ASP A O   
4545  C CB  . ASP A 624  ? 0.4131 0.7279 0.3473 0.0990  -0.0275 -0.1402 622  ASP A CB  
4546  C CG  . ASP A 624  ? 0.4750 0.7887 0.4160 0.1004  -0.0315 -0.1516 622  ASP A CG  
4547  O OD1 . ASP A 624  ? 0.5100 0.8198 0.4514 0.0994  -0.0334 -0.1527 622  ASP A OD1 
4548  O OD2 . ASP A 624  ? 0.5769 0.8937 0.5233 0.1026  -0.0329 -0.1596 622  ASP A OD2 
4549  N N   . ALA A 625  ? 0.3838 0.6810 0.3069 0.0936  -0.0208 -0.1177 623  ALA A N   
4550  C CA  . ALA A 625  ? 0.4026 0.7017 0.3208 0.0924  -0.0171 -0.1068 623  ALA A CA  
4551  C C   . ALA A 625  ? 0.4243 0.7142 0.3383 0.0897  -0.0161 -0.0981 623  ALA A C   
4552  O O   . ALA A 625  ? 0.4489 0.7408 0.3591 0.0885  -0.0132 -0.0881 623  ALA A O   
4553  C CB  . ALA A 625  ? 0.4419 0.7334 0.3616 0.0924  -0.0155 -0.1079 623  ALA A CB  
4554  N N   . ALA A 626  ? 0.3589 0.6390 0.2742 0.0885  -0.0186 -0.1015 624  ALA A N   
4555  C CA  . ALA A 626  ? 0.3504 0.6210 0.2622 0.0860  -0.0179 -0.0937 624  ALA A CA  
4556  C C   . ALA A 626  ? 0.3967 0.6777 0.3038 0.0855  -0.0162 -0.0831 624  ALA A C   
4557  O O   . ALA A 626  ? 0.4047 0.6811 0.3086 0.0837  -0.0139 -0.0737 624  ALA A O   
4558  C CB  . ALA A 626  ? 0.3902 0.6496 0.3046 0.0849  -0.0211 -0.0998 624  ALA A CB  
4559  N N   . PRO A 627  ? 0.3913 0.6861 0.2983 0.0868  -0.0171 -0.0837 625  PRO A N   
4560  C CA  . PRO A 627  ? 0.3854 0.6895 0.2886 0.0862  -0.0156 -0.0728 625  PRO A CA  
4561  C C   . PRO A 627  ? 0.3876 0.6978 0.2889 0.0859  -0.0122 -0.0640 625  PRO A C   
4562  O O   . PRO A 627  ? 0.4071 0.7160 0.3058 0.0842  -0.0105 -0.0532 625  PRO A O   
4563  C CB  . PRO A 627  ? 0.3935 0.7123 0.2979 0.0881  -0.0173 -0.0770 625  PRO A CB  
4564  C CG  . PRO A 627  ? 0.4084 0.7209 0.3167 0.0891  -0.0205 -0.0894 625  PRO A CG  
4565  C CD  . PRO A 627  ? 0.4134 0.7156 0.3240 0.0890  -0.0199 -0.0939 625  PRO A CD  
4566  N N   . ASP A 628  ? 0.3893 0.7060 0.2923 0.0876  -0.0112 -0.0682 626  ASP A N   
4567  C CA  . ASP A 628  ? 0.4161 0.7398 0.3177 0.0874  -0.0081 -0.0600 626  ASP A CA  
4568  C C   . ASP A 628  ? 0.4000 0.7098 0.3002 0.0851  -0.0061 -0.0536 626  ASP A C   
4569  O O   . ASP A 628  ? 0.4217 0.7339 0.3202 0.0837  -0.0038 -0.0427 626  ASP A O   
4570  C CB  . ASP A 628  ? 0.3805 0.7136 0.2846 0.0898  -0.0078 -0.0668 626  ASP A CB  
4571  C CG  . ASP A 628  ? 0.4710 0.8204 0.3763 0.0922  -0.0095 -0.0718 626  ASP A CG  
4572  O OD1 . ASP A 628  ? 0.5045 0.8616 0.4081 0.0918  -0.0097 -0.0664 626  ASP A OD1 
4573  O OD2 . ASP A 628  ? 0.5552 0.9097 0.4635 0.0945  -0.0106 -0.0812 626  ASP A OD2 
4574  N N   . TRP A 629  ? 0.3501 0.6452 0.2516 0.0846  -0.0071 -0.0601 627  TRP A N   
4575  C CA  . TRP A 629  ? 0.3360 0.6181 0.2363 0.0826  -0.0051 -0.0546 627  TRP A CA  
4576  C C   . TRP A 629  ? 0.3229 0.5960 0.2233 0.0798  -0.0053 -0.0459 627  TRP A C   
4577  O O   . TRP A 629  ? 0.3359 0.6034 0.2371 0.0776  -0.0032 -0.0359 627  TRP A O   
4578  C CB  . TRP A 629  ? 0.3332 0.6013 0.2374 0.0826  -0.0062 -0.0636 627  TRP A CB  
4579  C CG  . TRP A 629  ? 0.3069 0.5583 0.2146 0.0794  -0.0044 -0.0571 627  TRP A CG  
4580  C CD1 . TRP A 629  ? 0.2973 0.5302 0.2096 0.0767  -0.0055 -0.0574 627  TRP A CD1 
4581  C CD2 . TRP A 629  ? 0.2836 0.5358 0.1908 0.0785  -0.0013 -0.0490 627  TRP A CD2 
4582  N NE1 . TRP A 629  ? 0.2862 0.5087 0.2005 0.0743  -0.0032 -0.0505 627  TRP A NE1 
4583  C CE2 . TRP A 629  ? 0.2755 0.5091 0.1869 0.0754  -0.0007 -0.0454 627  TRP A CE2 
4584  C CE3 . TRP A 629  ? 0.2957 0.5629 0.1994 0.0800  0.0011  -0.0446 627  TRP A CE3 
4585  C CZ2 . TRP A 629  ? 0.3136 0.5429 0.2261 0.0737  0.0020  -0.0378 627  TRP A CZ2 
4586  C CZ3 . TRP A 629  ? 0.3170 0.5796 0.2219 0.0782  0.0038  -0.0367 627  TRP A CZ3 
4587  C CH2 . TRP A 629  ? 0.3233 0.5669 0.2326 0.0751  0.0042  -0.0335 627  TRP A CH2 
4588  N N   . ALA A 630  ? 0.3211 0.5921 0.2219 0.0797  -0.0080 -0.0495 628  ALA A N   
4589  C CA  . ALA A 630  ? 0.3697 0.6331 0.2716 0.0772  -0.0083 -0.0414 628  ALA A CA  
4590  C C   . ALA A 630  ? 0.3575 0.6331 0.2559 0.0771  -0.0066 -0.0302 628  ALA A C   
4591  O O   . ALA A 630  ? 0.3615 0.6295 0.2616 0.0747  -0.0060 -0.0209 628  ALA A O   
4592  C CB  . ALA A 630  ? 0.3438 0.6059 0.2463 0.0775  -0.0115 -0.0477 628  ALA A CB  
4593  N N   . ALA A 631  ? 0.3579 0.6517 0.2530 0.0795  -0.0060 -0.0308 629  ALA A N   
4594  C CA  . ALA A 631  ? 0.3733 0.6783 0.2679 0.0790  -0.0046 -0.0197 629  ALA A CA  
4595  C C   . ALA A 631  ? 0.3528 0.6566 0.2475 0.0777  -0.0015 -0.0107 629  ALA A C   
4596  O O   . ALA A 631  ? 0.3494 0.6594 0.2445 0.0766  -0.0004 0.0000  629  ALA A O   
4597  C CB  . ALA A 631  ? 0.3794 0.7019 0.2747 0.0811  -0.0050 -0.0231 629  ALA A CB  
4598  N N   . VAL A 632  ? 0.3623 0.6585 0.2573 0.0777  -0.0003 -0.0146 630  VAL A N   
4599  C CA  . VAL A 632  ? 0.3313 0.6242 0.2273 0.0761  0.0025  -0.0060 630  VAL A CA  
4600  C C   . VAL A 632  ? 0.3392 0.6161 0.2393 0.0727  0.0023  0.0020  630  VAL A C   
4601  O O   . VAL A 632  ? 0.3300 0.5915 0.2331 0.0715  0.0009  -0.0028 630  VAL A O   
4602  C CB  . VAL A 632  ? 0.3258 0.6120 0.2236 0.0765  0.0036  -0.0127 630  VAL A CB  
4603  C CG1 . VAL A 632  ? 0.3341 0.6153 0.2340 0.0745  0.0063  -0.0037 630  VAL A CG1 
4604  C CG2 . VAL A 632  ? 0.3373 0.6375 0.2345 0.0795  0.0033  -0.0210 630  VAL A CG2 
4605  N N   . PRO A 633  ? 0.3065 0.5867 0.2071 0.0713  0.0036  0.0139  631  PRO A N   
4606  C CA  . PRO A 633  ? 0.2872 0.5530 0.1920 0.0684  0.0031  0.0209  631  PRO A CA  
4607  C C   . PRO A 633  ? 0.3033 0.5502 0.2125 0.0663  0.0038  0.0186  631  PRO A C   
4608  O O   . PRO A 633  ? 0.3051 0.5509 0.2147 0.0665  0.0054  0.0163  631  PRO A O   
4609  C CB  . PRO A 633  ? 0.3193 0.5936 0.2245 0.0674  0.0046  0.0339  631  PRO A CB  
4610  C CG  . PRO A 633  ? 0.3466 0.6427 0.2464 0.0701  0.0051  0.0335  631  PRO A CG  
4611  C CD  . PRO A 633  ? 0.3327 0.6308 0.2305 0.0722  0.0052  0.0215  631  PRO A CD  
4612  N N   . PRO A 634  ? 0.2831 0.5151 0.1959 0.0643  0.0025  0.0191  632  PRO A N   
4613  C CA  . PRO A 634  ? 0.2727 0.4870 0.1896 0.0623  0.0031  0.0169  632  PRO A CA  
4614  C C   . PRO A 634  ? 0.2566 0.4682 0.1758 0.0610  0.0055  0.0236  632  PRO A C   
4615  O O   . PRO A 634  ? 0.2596 0.4630 0.1802 0.0605  0.0064  0.0195  632  PRO A O   
4616  C CB  . PRO A 634  ? 0.2883 0.4907 0.2085 0.0604  0.0015  0.0192  632  PRO A CB  
4617  C CG  . PRO A 634  ? 0.3116 0.5244 0.2289 0.0620  -0.0004 0.0180  632  PRO A CG  
4618  C CD  . PRO A 634  ? 0.2931 0.5247 0.2062 0.0640  0.0005  0.0213  632  PRO A CD  
4619  N N   . SER A 635  ? 0.2925 0.5108 0.2122 0.0603  0.0065  0.0340  633  SER A N   
4620  C CA  . SER A 635  ? 0.3186 0.5346 0.2409 0.0588  0.0087  0.0409  633  SER A CA  
4621  C C   . SER A 635  ? 0.3148 0.5397 0.2343 0.0605  0.0103  0.0368  633  SER A C   
4622  O O   . SER A 635  ? 0.2879 0.5060 0.2098 0.0594  0.0119  0.0370  633  SER A O   
4623  C CB  . SER A 635  ? 0.3812 0.6050 0.3049 0.0580  0.0091  0.0529  633  SER A CB  
4624  O OG  . SER A 635  ? 0.4627 0.7055 0.3818 0.0601  0.0091  0.0543  633  SER A OG  
4625  N N   . GLU A 636  ? 0.3004 0.5411 0.2151 0.0632  0.0100  0.0327  634  GLU A N   
4626  C CA  . GLU A 636  ? 0.2957 0.5460 0.2077 0.0651  0.0115  0.0281  634  GLU A CA  
4627  C C   . GLU A 636  ? 0.2985 0.5389 0.2112 0.0658  0.0109  0.0167  634  GLU A C   
4628  O O   . GLU A 636  ? 0.2953 0.5346 0.2087 0.0661  0.0124  0.0142  634  GLU A O   
4629  C CB  . GLU A 636  ? 0.3174 0.5890 0.2242 0.0679  0.0114  0.0273  634  GLU A CB  
4630  C CG  . GLU A 636  ? 0.3886 0.6715 0.2927 0.0702  0.0130  0.0219  634  GLU A CG  
4631  C CD  . GLU A 636  ? 0.4910 0.7714 0.3977 0.0687  0.0156  0.0282  634  GLU A CD  
4632  O OE1 . GLU A 636  ? 0.4854 0.7681 0.3939 0.0668  0.0166  0.0395  634  GLU A OE1 
4633  O OE2 . GLU A 636  ? 0.4246 0.7008 0.3321 0.0693  0.0164  0.0218  634  GLU A OE2 
4634  N N   . ARG A 637  ? 0.2734 0.5062 0.1863 0.0660  0.0086  0.0098  635  ARG A N   
4635  C CA  . ARG A 637  ? 0.2743 0.4955 0.1891 0.0661  0.0078  0.0002  635  ARG A CA  
4636  C C   . ARG A 637  ? 0.2486 0.4543 0.1678 0.0634  0.0090  0.0037  635  ARG A C   
4637  O O   . ARG A 637  ? 0.2656 0.4668 0.1860 0.0637  0.0098  -0.0008 635  ARG A O   
4638  C CB  . ARG A 637  ? 0.2506 0.4656 0.1658 0.0662  0.0050  -0.0064 635  ARG A CB  
4639  C CG  . ARG A 637  ? 0.2712 0.5018 0.1821 0.0688  0.0036  -0.0098 635  ARG A CG  
4640  C CD  . ARG A 637  ? 0.2928 0.5181 0.2043 0.0693  0.0008  -0.0186 635  ARG A CD  
4641  N NE  . ARG A 637  ? 0.2839 0.4960 0.1984 0.0668  -0.0003 -0.0149 635  ARG A NE  
4642  C CZ  . ARG A 637  ? 0.2999 0.5150 0.2134 0.0666  -0.0018 -0.0127 635  ARG A CZ  
4643  N NH1 . ARG A 637  ? 0.3370 0.5682 0.2466 0.0688  -0.0024 -0.0128 635  ARG A NH1 
4644  N NH2 . ARG A 637  ? 0.2845 0.4865 0.2013 0.0643  -0.0027 -0.0105 635  ARG A NH2 
4645  N N   . ALA A 638  ? 0.2643 0.4621 0.1862 0.0609  0.0092  0.0120  636  ALA A N   
4646  C CA  . ALA A 638  ? 0.2574 0.4411 0.1835 0.0584  0.0103  0.0155  636  ALA A CA  
4647  C C   . ALA A 638  ? 0.2813 0.4704 0.2077 0.0585  0.0127  0.0195  636  ALA A C   
4648  O O   . ALA A 638  ? 0.2426 0.4222 0.1715 0.0574  0.0136  0.0181  636  ALA A O   
4649  C CB  . ALA A 638  ? 0.2588 0.4350 0.1879 0.0561  0.0099  0.0236  636  ALA A CB  
4650  N N   . ALA A 639  ? 0.2504 0.4550 0.1741 0.0596  0.0138  0.0248  637  ALA A N   
4651  C CA  . ALA A 639  ? 0.2440 0.4554 0.1679 0.0598  0.0161  0.0287  637  ALA A CA  
4652  C C   . ALA A 639  ? 0.2941 0.5077 0.2165 0.0618  0.0166  0.0193  637  ALA A C   
4653  O O   . ALA A 639  ? 0.2760 0.4874 0.2002 0.0612  0.0182  0.0205  637  ALA A O   
4654  C CB  . ALA A 639  ? 0.2889 0.5181 0.2102 0.0607  0.0170  0.0363  637  ALA A CB  
4655  N N   . CYS A 640  ? 0.2529 0.4707 0.1725 0.0641  0.0150  0.0100  638  CYS A N   
4656  C CA  . CYS A 640  ? 0.2668 0.4852 0.1861 0.0661  0.0150  0.0003  638  CYS A CA  
4657  C C   . CYS A 640  ? 0.2722 0.4723 0.1958 0.0642  0.0147  -0.0025 638  CYS A C   
4658  O O   . CYS A 640  ? 0.2553 0.4535 0.1803 0.0645  0.0159  -0.0048 638  CYS A O   
4659  C CB  . CYS A 640  ? 0.2703 0.4951 0.1869 0.0688  0.0128  -0.0095 638  CYS A CB  
4660  S SG  . CYS A 640  ? 0.2962 0.5449 0.2072 0.0718  0.0129  -0.0088 638  CYS A SG  
4661  N N   . LEU A 641  ? 0.2530 0.4400 0.1787 0.0623  0.0132  -0.0023 639  LEU A N   
4662  C CA  . LEU A 641  ? 0.2575 0.4277 0.1872 0.0603  0.0129  -0.0043 639  LEU A CA  
4663  C C   . LEU A 641  ? 0.2368 0.4027 0.1690 0.0583  0.0151  0.0030  639  LEU A C   
4664  O O   . LEU A 641  ? 0.2442 0.4032 0.1786 0.0580  0.0157  0.0002  639  LEU A O   
4665  C CB  . LEU A 641  ? 0.2515 0.4101 0.1830 0.0584  0.0111  -0.0040 639  LEU A CB  
4666  C CG  . LEU A 641  ? 0.2811 0.4363 0.2124 0.0594  0.0086  -0.0134 639  LEU A CG  
4667  C CD1 . LEU A 641  ? 0.3058 0.4757 0.2333 0.0623  0.0076  -0.0175 639  LEU A CD1 
4668  C CD2 . LEU A 641  ? 0.2552 0.3982 0.1889 0.0571  0.0072  -0.0121 639  LEU A CD2 
4669  N N   . ASP A 642  ? 0.2421 0.4120 0.1744 0.0571  0.0161  0.0125  640  ASP A N   
4670  C CA  . ASP A 642  ? 0.2659 0.4320 0.2012 0.0551  0.0180  0.0197  640  ASP A CA  
4671  C C   . ASP A 642  ? 0.2588 0.4341 0.1930 0.0567  0.0199  0.0185  640  ASP A C   
4672  O O   . ASP A 642  ? 0.2609 0.4295 0.1979 0.0555  0.0210  0.0194  640  ASP A O   
4673  C CB  . ASP A 642  ? 0.2523 0.4218 0.1886 0.0536  0.0185  0.0301  640  ASP A CB  
4674  C CG  . ASP A 642  ? 0.2632 0.4195 0.2026 0.0514  0.0172  0.0326  640  ASP A CG  
4675  O OD1 . ASP A 642  ? 0.2721 0.4153 0.2135 0.0504  0.0164  0.0277  640  ASP A OD1 
4676  O OD2 . ASP A 642  ? 0.2935 0.4530 0.2336 0.0506  0.0169  0.0396  640  ASP A OD2 
4677  N N   . ARG A 643  ? 0.2433 0.4344 0.1736 0.0593  0.0202  0.0163  641  ARG A N   
4678  C CA  . ARG A 643  ? 0.2355 0.4365 0.1647 0.0611  0.0219  0.0143  641  ARG A CA  
4679  C C   . ARG A 643  ? 0.2692 0.4620 0.1998 0.0621  0.0212  0.0047  641  ARG A C   
4680  O O   . ARG A 643  ? 0.2817 0.4737 0.2140 0.0620  0.0227  0.0045  641  ARG A O   
4681  C CB  . ARG A 643  ? 0.2636 0.4841 0.1882 0.0640  0.0221  0.0131  641  ARG A CB  
4682  C CG  . ARG A 643  ? 0.2747 0.5064 0.1984 0.0630  0.0235  0.0242  641  ARG A CG  
4683  C CD  . ARG A 643  ? 0.3250 0.5778 0.2440 0.0660  0.0241  0.0231  641  ARG A CD  
4684  N NE  . ARG A 643  ? 0.2984 0.5555 0.2141 0.0680  0.0220  0.0161  641  ARG A NE  
4685  C CZ  . ARG A 643  ? 0.2640 0.5262 0.1778 0.0678  0.0210  0.0204  641  ARG A CZ  
4686  N NH1 . ARG A 643  ? 0.3386 0.6018 0.2539 0.0656  0.0217  0.0319  641  ARG A NH1 
4687  N NH2 . ARG A 643  ? 0.3467 0.6135 0.2575 0.0699  0.0190  0.0131  641  ARG A NH2 
4688  N N   . ALA A 644  ? 0.2339 0.4207 0.1643 0.0629  0.0190  -0.0032 642  ALA A N   
4689  C CA  . ALA A 644  ? 0.2490 0.4271 0.1816 0.0636  0.0180  -0.0119 642  ALA A CA  
4690  C C   . ALA A 644  ? 0.2420 0.4047 0.1787 0.0607  0.0186  -0.0086 642  ALA A C   
4691  O O   . ALA A 644  ? 0.2534 0.4123 0.1922 0.0611  0.0190  -0.0121 642  ALA A O   
4692  C CB  . ALA A 644  ? 0.2542 0.4281 0.1865 0.0646  0.0153  -0.0201 642  ALA A CB  
4693  N N   . ALA A 645  ? 0.2450 0.3991 0.1831 0.0580  0.0184  -0.0020 643  ALA A N   
4694  C CA  . ALA A 645  ? 0.2386 0.3790 0.1807 0.0552  0.0189  0.0013  643  ALA A CA  
4695  C C   . ALA A 645  ? 0.2528 0.3972 0.1960 0.0549  0.0213  0.0060  643  ALA A C   
4696  O O   . ALA A 645  ? 0.2532 0.3901 0.1991 0.0542  0.0217  0.0043  643  ALA A O   
4697  C CB  . ALA A 645  ? 0.2489 0.3815 0.1924 0.0527  0.0184  0.0076  643  ALA A CB  
4698  N N   . GLU A 646  ? 0.2474 0.4042 0.1889 0.0553  0.0227  0.0124  644  GLU A N   
4699  C CA  . GLU A 646  ? 0.2711 0.4335 0.2138 0.0551  0.0250  0.0171  644  GLU A CA  
4700  C C   . GLU A 646  ? 0.2958 0.4629 0.2379 0.0575  0.0255  0.0097  644  GLU A C   
4701  O O   . GLU A 646  ? 0.2812 0.4446 0.2258 0.0568  0.0266  0.0104  644  GLU A O   
4702  C CB  . GLU A 646  ? 0.3501 0.5272 0.2908 0.0554  0.0263  0.0247  644  GLU A CB  
4703  C CG  . GLU A 646  ? 0.3749 0.5481 0.3175 0.0529  0.0260  0.0337  644  GLU A CG  
4704  C CD  . GLU A 646  ? 0.4860 0.6468 0.4335 0.0499  0.0266  0.0389  644  GLU A CD  
4705  O OE1 . GLU A 646  ? 0.5651 0.7263 0.5143 0.0497  0.0280  0.0394  644  GLU A OE1 
4706  O OE2 . GLU A 646  ? 0.4657 0.6166 0.4156 0.0479  0.0255  0.0421  644  GLU A OE2 
4707  N N   . LEU A 647  ? 0.2670 0.4425 0.2060 0.0604  0.0245  0.0023  645  LEU A N   
4708  C CA  . LEU A 647  ? 0.2771 0.4576 0.2159 0.0631  0.0247  -0.0055 645  LEU A CA  
4709  C C   . LEU A 647  ? 0.2874 0.4527 0.2299 0.0623  0.0235  -0.0109 645  LEU A C   
4710  O O   . LEU A 647  ? 0.2858 0.4507 0.2303 0.0629  0.0244  -0.0129 645  LEU A O   
4711  C CB  . LEU A 647  ? 0.2864 0.4784 0.2218 0.0664  0.0234  -0.0130 645  LEU A CB  
4712  C CG  . LEU A 647  ? 0.3001 0.5105 0.2315 0.0678  0.0248  -0.0086 645  LEU A CG  
4713  C CD1 . LEU A 647  ? 0.2884 0.5093 0.2164 0.0710  0.0232  -0.0166 645  LEU A CD1 
4714  C CD2 . LEU A 647  ? 0.3231 0.5444 0.2546 0.0687  0.0273  -0.0058 645  LEU A CD2 
4715  N N   . MET A 648  ? 0.2531 0.4061 0.1968 0.0608  0.0215  -0.0129 646  MET A N   
4716  C CA  . MET A 648  ? 0.2712 0.4099 0.2186 0.0598  0.0203  -0.0172 646  MET A CA  
4717  C C   . MET A 648  ? 0.2663 0.3969 0.2166 0.0572  0.0218  -0.0109 646  MET A C   
4718  O O   . MET A 648  ? 0.2741 0.3984 0.2271 0.0571  0.0217  -0.0138 646  MET A O   
4719  C CB  . MET A 648  ? 0.2291 0.3575 0.1771 0.0587  0.0179  -0.0200 646  MET A CB  
4720  C CG  . MET A 648  ? 0.2711 0.4051 0.2175 0.0613  0.0160  -0.0283 646  MET A CG  
4721  S SD  . MET A 648  ? 0.3011 0.4205 0.2499 0.0597  0.0131  -0.0323 646  MET A SD  
4722  C CE  . MET A 648  ? 0.3355 0.4641 0.2826 0.0630  0.0108  -0.0418 646  MET A CE  
4723  N N   . GLN A 649  ? 0.2543 0.3847 0.2044 0.0550  0.0229  -0.0022 647  GLN A N   
4724  C CA  . GLN A 649  ? 0.2753 0.3987 0.2285 0.0525  0.0242  0.0037  647  GLN A CA  
4725  C C   . GLN A 649  ? 0.2568 0.3879 0.2106 0.0537  0.0261  0.0040  647  GLN A C   
4726  O O   . GLN A 649  ? 0.3011 0.4250 0.2578 0.0528  0.0264  0.0035  647  GLN A O   
4727  C CB  . GLN A 649  ? 0.2937 0.4170 0.2473 0.0502  0.0249  0.0128  647  GLN A CB  
4728  C CG  . GLN A 649  ? 0.2671 0.3821 0.2245 0.0475  0.0259  0.0184  647  GLN A CG  
4729  C CD  . GLN A 649  ? 0.2797 0.3795 0.2397 0.0457  0.0245  0.0161  647  GLN A CD  
4730  O OE1 . GLN A 649  ? 0.2613 0.3552 0.2216 0.0443  0.0234  0.0179  647  GLN A OE1 
4731  N NE2 . GLN A 649  ? 0.2839 0.3776 0.2457 0.0457  0.0244  0.0121  647  GLN A NE2 
4732  N N   . ALA A 650  ? 0.2660 0.4123 0.2170 0.0558  0.0273  0.0049  648  ALA A N   
4733  C CA  . ALA A 650  ? 0.2726 0.4279 0.2242 0.0570  0.0292  0.0055  648  ALA A CA  
4734  C C   . ALA A 650  ? 0.3454 0.4991 0.2979 0.0593  0.0284  -0.0038 648  ALA A C   
4735  O O   . ALA A 650  ? 0.3456 0.4998 0.3002 0.0595  0.0296  -0.0038 648  ALA A O   
4736  C CB  . ALA A 650  ? 0.3134 0.4867 0.2615 0.0588  0.0306  0.0084  648  ALA A CB  
4737  N N   . ARG A 651  ? 0.2751 0.4271 0.2266 0.0611  0.0263  -0.0116 649  ARG A N   
4738  C CA  . ARG A 651  ? 0.2869 0.4376 0.2398 0.0635  0.0251  -0.0209 649  ARG A CA  
4739  C C   . ARG A 651  ? 0.2401 0.3741 0.1969 0.0617  0.0235  -0.0234 649  ARG A C   
4740  O O   . ARG A 651  ? 0.2813 0.4123 0.2403 0.0635  0.0221  -0.0309 649  ARG A O   
4741  C CB  . ARG A 651  ? 0.3459 0.5045 0.2963 0.0665  0.0235  -0.0284 649  ARG A CB  
4742  C CG  . ARG A 651  ? 0.3999 0.5624 0.3519 0.0699  0.0225  -0.0383 649  ARG A CG  
4743  C CD  . ARG A 651  ? 0.3683 0.5477 0.3168 0.0734  0.0224  -0.0432 649  ARG A CD  
4744  N NE  . ARG A 651  ? 0.4210 0.6041 0.3716 0.0769  0.0211  -0.0536 649  ARG A NE  
4745  C CZ  . ARG A 651  ? 0.4154 0.6045 0.3675 0.0788  0.0224  -0.0558 649  ARG A CZ  
4746  N NH1 . ARG A 651  ? 0.4003 0.5921 0.3522 0.0773  0.0251  -0.0482 649  ARG A NH1 
4747  N NH2 . ARG A 651  ? 0.4533 0.6457 0.4078 0.0822  0.0208  -0.0659 649  ARG A NH2 
4748  N N   . MET A 652  ? 0.2859 0.4091 0.2438 0.0584  0.0235  -0.0173 650  MET A N   
4749  C CA  . MET A 652  ? 0.2666 0.3746 0.2278 0.0566  0.0218  -0.0194 650  MET A CA  
4750  C C   . MET A 652  ? 0.2756 0.3800 0.2402 0.0575  0.0216  -0.0237 650  MET A C   
4751  O O   . MET A 652  ? 0.2751 0.3724 0.2419 0.0580  0.0195  -0.0298 650  MET A O   
4752  C CB  . MET A 652  ? 0.2900 0.3886 0.2522 0.0529  0.0223  -0.0119 650  MET A CB  
4753  C CG  . MET A 652  ? 0.2559 0.3402 0.2215 0.0510  0.0209  -0.0135 650  MET A CG  
4754  S SD  . MET A 652  ? 0.2992 0.3737 0.2660 0.0471  0.0214  -0.0055 650  MET A SD  
4755  C CE  . MET A 652  ? 0.2812 0.3549 0.2455 0.0467  0.0200  -0.0058 650  MET A CE  
4756  N N   . PRO A 653  ? 0.2720 0.3810 0.2375 0.0576  0.0236  -0.0207 651  PRO A N   
4757  C CA  . PRO A 653  ? 0.2923 0.3975 0.2613 0.0586  0.0232  -0.0249 651  PRO A CA  
4758  C C   . PRO A 653  ? 0.2816 0.3907 0.2514 0.0620  0.0215  -0.0344 651  PRO A C   
4759  O O   . PRO A 653  ? 0.2752 0.3756 0.2486 0.0622  0.0195  -0.0392 651  PRO A O   
4760  C CB  . PRO A 653  ? 0.3041 0.4176 0.2733 0.0587  0.0259  -0.0201 651  PRO A CB  
4761  C CG  . PRO A 653  ? 0.3237 0.4385 0.2909 0.0562  0.0273  -0.0115 651  PRO A CG  
4762  C CD  . PRO A 653  ? 0.3025 0.4199 0.2665 0.0568  0.0262  -0.0131 651  PRO A CD  
4763  N N   . THR A 654  ? 0.2630 0.3855 0.2299 0.0647  0.0220  -0.0372 652  THR A N   
4764  C CA  . THR A 654  ? 0.2553 0.3822 0.2232 0.0682  0.0201  -0.0469 652  THR A CA  
4765  C C   . THR A 654  ? 0.2716 0.3891 0.2406 0.0677  0.0172  -0.0512 652  THR A C   
4766  O O   . THR A 654  ? 0.2774 0.3897 0.2502 0.0691  0.0149  -0.0583 652  THR A O   
4767  C CB  . THR A 654  ? 0.2882 0.4325 0.2522 0.0712  0.0214  -0.0486 652  THR A CB  
4768  O OG1 . THR A 654  ? 0.3239 0.4771 0.2874 0.0715  0.0241  -0.0442 652  THR A OG1 
4769  C CG2 . THR A 654  ? 0.3091 0.4586 0.2745 0.0751  0.0193  -0.0594 652  THR A CG2 
4770  N N   . LEU A 655  ? 0.2784 0.3933 0.2446 0.0656  0.0171  -0.0469 653  LEU A N   
4771  C CA  . LEU A 655  ? 0.2763 0.3823 0.2436 0.0648  0.0144  -0.0505 653  LEU A CA  
4772  C C   . LEU A 655  ? 0.3003 0.3914 0.2723 0.0626  0.0129  -0.0507 653  LEU A C   
4773  O O   . LEU A 655  ? 0.2900 0.3750 0.2651 0.0632  0.0102  -0.0566 653  LEU A O   
4774  C CB  . LEU A 655  ? 0.2737 0.3798 0.2374 0.0628  0.0148  -0.0450 653  LEU A CB  
4775  C CG  . LEU A 655  ? 0.2732 0.3944 0.2323 0.0649  0.0159  -0.0446 653  LEU A CG  
4776  C CD1 . LEU A 655  ? 0.2779 0.3986 0.2340 0.0628  0.0162  -0.0386 653  LEU A CD1 
4777  C CD2 . LEU A 655  ? 0.3261 0.4543 0.2853 0.0684  0.0139  -0.0542 653  LEU A CD2 
4778  N N   . LEU A 656  ? 0.2864 0.3718 0.2592 0.0602  0.0145  -0.0442 654  LEU A N   
4779  C CA  . LEU A 656  ? 0.2916 0.3639 0.2685 0.0581  0.0132  -0.0440 654  LEU A CA  
4780  C C   . LEU A 656  ? 0.2829 0.3542 0.2642 0.0605  0.0115  -0.0512 654  LEU A C   
4781  O O   . LEU A 656  ? 0.3019 0.3640 0.2870 0.0598  0.0090  -0.0546 654  LEU A O   
4782  C CB  . LEU A 656  ? 0.2959 0.3647 0.2731 0.0557  0.0154  -0.0368 654  LEU A CB  
4783  C CG  . LEU A 656  ? 0.3207 0.3899 0.2949 0.0533  0.0172  -0.0289 654  LEU A CG  
4784  C CD1 . LEU A 656  ? 0.3279 0.3922 0.3038 0.0510  0.0186  -0.0232 654  LEU A CD1 
4785  C CD2 . LEU A 656  ? 0.3079 0.3700 0.2813 0.0514  0.0157  -0.0283 654  LEU A CD2 
4786  N N   . GLY A 657  ? 0.2701 0.3509 0.2513 0.0631  0.0128  -0.0534 655  GLY A N   
4787  C CA  . GLY A 657  ? 0.3163 0.3965 0.3023 0.0656  0.0111  -0.0603 655  GLY A CA  
4788  C C   . GLY A 657  ? 0.2704 0.3498 0.2586 0.0675  0.0081  -0.0684 655  GLY A C   
4789  O O   . GLY A 657  ? 0.3014 0.3734 0.2951 0.0679  0.0056  -0.0729 655  GLY A O   
4790  N N   . LEU A 658  ? 0.2695 0.3569 0.2540 0.0688  0.0080  -0.0703 656  LEU A N   
4791  C CA  . LEU A 658  ? 0.2440 0.3312 0.2308 0.0707  0.0049  -0.0784 656  LEU A CA  
4792  C C   . LEU A 658  ? 0.2435 0.3171 0.2330 0.0677  0.0026  -0.0772 656  LEU A C   
4793  O O   . LEU A 658  ? 0.2647 0.3320 0.2597 0.0683  -0.0004 -0.0829 656  LEU A O   
4794  C CB  . LEU A 658  ? 0.2563 0.3559 0.2380 0.0726  0.0056  -0.0802 656  LEU A CB  
4795  C CG  . LEU A 658  ? 0.2693 0.3706 0.2530 0.0748  0.0024  -0.0891 656  LEU A CG  
4796  C CD1 . LEU A 658  ? 0.2959 0.3977 0.2856 0.0779  0.0003  -0.0979 656  LEU A CD1 
4797  C CD2 . LEU A 658  ? 0.2922 0.4076 0.2703 0.0767  0.0034  -0.0902 656  LEU A CD2 
4798  N N   . ILE A 659  ? 0.2569 0.3259 0.2430 0.0644  0.0039  -0.0698 657  ILE A N   
4799  C CA  . ILE A 659  ? 0.2575 0.3146 0.2458 0.0614  0.0020  -0.0682 657  ILE A CA  
4800  C C   . ILE A 659  ? 0.2671 0.3135 0.2609 0.0600  0.0007  -0.0680 657  ILE A C   
4801  O O   . ILE A 659  ? 0.2692 0.3076 0.2677 0.0592  -0.0021 -0.0709 657  ILE A O   
4802  C CB  . ILE A 659  ? 0.2533 0.3084 0.2370 0.0584  0.0039  -0.0602 657  ILE A CB  
4803  C CG1 . ILE A 659  ? 0.2650 0.3299 0.2440 0.0597  0.0044  -0.0610 657  ILE A CG1 
4804  C CG2 . ILE A 659  ? 0.2570 0.2999 0.2432 0.0551  0.0022  -0.0581 657  ILE A CG2 
4805  C CD1 . ILE A 659  ? 0.2856 0.3519 0.2600 0.0575  0.0068  -0.0529 657  ILE A CD1 
4806  N N   . ILE A 660  ? 0.2554 0.3021 0.2493 0.0597  0.0027  -0.0643 658  ILE A N   
4807  C CA  . ILE A 660  ? 0.2705 0.3080 0.2696 0.0585  0.0016  -0.0636 658  ILE A CA  
4808  C C   . ILE A 660  ? 0.2540 0.2902 0.2593 0.0610  -0.0015 -0.0717 658  ILE A C   
4809  O O   . ILE A 660  ? 0.2944 0.3210 0.3048 0.0596  -0.0040 -0.0725 658  ILE A O   
4810  C CB  . ILE A 660  ? 0.2325 0.2724 0.2305 0.0583  0.0043  -0.0591 658  ILE A CB  
4811  C CG1 . ILE A 660  ? 0.2561 0.2939 0.2500 0.0550  0.0067  -0.0508 658  ILE A CG1 
4812  C CG2 . ILE A 660  ? 0.2749 0.3080 0.2788 0.0582  0.0029  -0.0604 658  ILE A CG2 
4813  C CD1 . ILE A 660  ? 0.3076 0.3496 0.3002 0.0550  0.0095  -0.0464 658  ILE A CD1 
4814  N N   . ARG A 661  ? 0.2472 0.2933 0.2524 0.0648  -0.0014 -0.0777 659  ARG A N   
4815  C CA  . ARG A 661  ? 0.2651 0.3103 0.2770 0.0675  -0.0044 -0.0857 659  ARG A CA  
4816  C C   . ARG A 661  ? 0.2985 0.3420 0.3129 0.0682  -0.0076 -0.0917 659  ARG A C   
4817  O O   . ARG A 661  ? 0.3103 0.3475 0.3319 0.0688  -0.0109 -0.0965 659  ARG A O   
4818  C CB  . ARG A 661  ? 0.2959 0.3527 0.3074 0.0715  -0.0031 -0.0903 659  ARG A CB  
4819  C CG  . ARG A 661  ? 0.2663 0.3229 0.2780 0.0710  -0.0009 -0.0858 659  ARG A CG  
4820  C CD  . ARG A 661  ? 0.2919 0.3615 0.3024 0.0748  0.0009  -0.0896 659  ARG A CD  
4821  N NE  . ARG A 661  ? 0.3017 0.3747 0.3177 0.0787  -0.0018 -0.0995 659  ARG A NE  
4822  C CZ  . ARG A 661  ? 0.3107 0.3959 0.3250 0.0823  -0.0018 -0.1059 659  ARG A CZ  
4823  N NH1 . ARG A 661  ? 0.3224 0.4177 0.3294 0.0824  0.0008  -0.1032 659  ARG A NH1 
4824  N NH2 . ARG A 661  ? 0.3117 0.3994 0.3319 0.0860  -0.0044 -0.1154 659  ARG A NH2 
4825  N N   . GLU A 662  ? 0.2794 0.3287 0.2885 0.0683  -0.0069 -0.0917 660  GLU A N   
4826  C CA  . GLU A 662  ? 0.2897 0.3384 0.3013 0.0691  -0.0100 -0.0977 660  GLU A CA  
4827  C C   . GLU A 662  ? 0.2828 0.3193 0.2968 0.0653  -0.0118 -0.0942 660  GLU A C   
4828  O O   . GLU A 662  ? 0.3102 0.3416 0.3302 0.0654  -0.0153 -0.0991 660  GLU A O   
4829  C CB  . GLU A 662  ? 0.3024 0.3625 0.3075 0.0707  -0.0086 -0.0992 660  GLU A CB  
4830  C CG  . GLU A 662  ? 0.3195 0.3803 0.3271 0.0719  -0.0119 -0.1063 660  GLU A CG  
4831  C CD  . GLU A 662  ? 0.3033 0.3765 0.3046 0.0737  -0.0107 -0.1080 660  GLU A CD  
4832  O OE1 . GLU A 662  ? 0.3078 0.3859 0.3024 0.0725  -0.0075 -0.1012 660  GLU A OE1 
4833  O OE2 . GLU A 662  ? 0.3116 0.3897 0.3150 0.0763  -0.0132 -0.1162 660  GLU A OE2 
4834  N N   . ALA A 663  ? 0.2671 0.2991 0.2771 0.0618  -0.0096 -0.0857 661  ALA A N   
4835  C CA  . ALA A 663  ? 0.2599 0.2829 0.2708 0.0583  -0.0110 -0.0822 661  ALA A CA  
4836  C C   . ALA A 663  ? 0.2842 0.2967 0.2982 0.0551  -0.0110 -0.0765 661  ALA A C   
4837  O O   . ALA A 663  ? 0.3371 0.3427 0.3512 0.0520  -0.0117 -0.0726 661  ALA A O   
4838  C CB  . ALA A 663  ? 0.2966 0.3236 0.3005 0.0570  -0.0089 -0.0778 661  ALA A CB  
4839  N N   . GLY A 664  ? 0.3193 0.3309 0.3357 0.0559  -0.0104 -0.0760 662  GLY A N   
4840  C CA  . GLY A 664  ? 0.3279 0.3302 0.3474 0.0530  -0.0107 -0.0708 662  GLY A CA  
4841  C C   . GLY A 664  ? 0.3048 0.3053 0.3189 0.0499  -0.0078 -0.0626 662  GLY A C   
4842  O O   . GLY A 664  ? 0.3280 0.3206 0.3439 0.0469  -0.0082 -0.0582 662  GLY A O   
4843  N N   . LYS A 665  ? 0.2711 0.2791 0.2788 0.0506  -0.0048 -0.0605 663  LYS A N   
4844  C CA  . LYS A 665  ? 0.2709 0.2776 0.2740 0.0479  -0.0023 -0.0531 663  LYS A CA  
4845  C C   . LYS A 665  ? 0.2543 0.2615 0.2569 0.0477  -0.0001 -0.0493 663  LYS A C   
4846  O O   . LYS A 665  ? 0.2506 0.2636 0.2536 0.0503  0.0006  -0.0519 663  LYS A O   
4847  C CB  . LYS A 665  ? 0.2840 0.2983 0.2811 0.0486  -0.0004 -0.0521 663  LYS A CB  
4848  C CG  . LYS A 665  ? 0.2995 0.3146 0.2965 0.0490  -0.0024 -0.0559 663  LYS A CG  
4849  C CD  . LYS A 665  ? 0.3216 0.3275 0.3208 0.0458  -0.0041 -0.0537 663  LYS A CD  
4850  C CE  . LYS A 665  ? 0.3540 0.3616 0.3522 0.0460  -0.0056 -0.0565 663  LYS A CE  
4851  N NZ  . LYS A 665  ? 0.3673 0.3663 0.3689 0.0432  -0.0078 -0.0555 663  LYS A NZ  
4852  N N   . SER A 666  ? 0.2720 0.2737 0.2737 0.0446  0.0010  -0.0432 664  SER A N   
4853  C CA  . SER A 666  ? 0.2652 0.2681 0.2655 0.0441  0.0033  -0.0389 664  SER A CA  
4854  C C   . SER A 666  ? 0.2723 0.2834 0.2673 0.0449  0.0061  -0.0365 664  SER A C   
4855  O O   . SER A 666  ? 0.2831 0.2979 0.2752 0.0452  0.0062  -0.0370 664  SER A O   
4856  C CB  . SER A 666  ? 0.2905 0.2859 0.2912 0.0406  0.0036  -0.0334 664  SER A CB  
4857  O OG  . SER A 666  ? 0.3075 0.3031 0.3043 0.0389  0.0046  -0.0301 664  SER A OG  
4858  N N   . ALA A 667  ? 0.2973 0.3116 0.2917 0.0451  0.0082  -0.0335 665  ALA A N   
4859  C CA  . ALA A 667  ? 0.2678 0.2900 0.2578 0.0456  0.0108  -0.0304 665  ALA A CA  
4860  C C   . ALA A 667  ? 0.2984 0.3182 0.2855 0.0431  0.0116  -0.0255 665  ALA A C   
4861  O O   . ALA A 667  ? 0.2656 0.2913 0.2494 0.0438  0.0124  -0.0248 665  ALA A O   
4862  C CB  . ALA A 667  ? 0.3102 0.3354 0.3008 0.0458  0.0128  -0.0275 665  ALA A CB  
4863  N N   . LEU A 668  ? 0.2716 0.2832 0.2600 0.0403  0.0112  -0.0222 666  LEU A N   
4864  C CA  . LEU A 668  ? 0.2891 0.2982 0.2753 0.0380  0.0118  -0.0181 666  LEU A CA  
4865  C C   . LEU A 668  ? 0.3074 0.3173 0.2921 0.0385  0.0104  -0.0208 666  LEU A C   
4866  O O   . LEU A 668  ? 0.2957 0.3090 0.2775 0.0383  0.0113  -0.0185 666  LEU A O   
4867  C CB  . LEU A 668  ? 0.3226 0.3229 0.3110 0.0351  0.0111  -0.0156 666  LEU A CB  
4868  C CG  . LEU A 668  ? 0.4374 0.4364 0.4262 0.0336  0.0127  -0.0111 666  LEU A CG  
4869  C CD1 . LEU A 668  ? 0.3799 0.3710 0.3706 0.0309  0.0117  -0.0094 666  LEU A CD1 
4870  C CD2 . LEU A 668  ? 0.4394 0.4427 0.4256 0.0332  0.0146  -0.0070 666  LEU A CD2 
4871  N N   . ASN A 669  ? 0.2777 0.2846 0.2649 0.0391  0.0081  -0.0256 667  ASN A N   
4872  C CA  . ASN A 669  ? 0.3015 0.3088 0.2877 0.0395  0.0067  -0.0284 667  ASN A CA  
4873  C C   . ASN A 669  ? 0.2887 0.3055 0.2723 0.0423  0.0071  -0.0313 667  ASN A C   
4874  O O   . ASN A 669  ? 0.2838 0.3033 0.2649 0.0425  0.0069  -0.0315 667  ASN A O   
4875  C CB  . ASN A 669  ? 0.3279 0.3290 0.3183 0.0391  0.0039  -0.0323 667  ASN A CB  
4876  C CG  . ASN A 669  ? 0.3466 0.3393 0.3390 0.0360  0.0033  -0.0288 667  ASN A CG  
4877  O OD1 . ASN A 669  ? 0.4851 0.4763 0.4753 0.0340  0.0046  -0.0243 667  ASN A OD1 
4878  N ND2 . ASN A 669  ? 0.4212 0.4087 0.4181 0.0355  0.0013  -0.0308 667  ASN A ND2 
4879  N N   . ALA A 670  ? 0.2771 0.2997 0.2611 0.0447  0.0079  -0.0335 668  ALA A N   
4880  C CA  . ALA A 670  ? 0.2719 0.3050 0.2530 0.0475  0.0086  -0.0360 668  ALA A CA  
4881  C C   . ALA A 670  ? 0.2512 0.2898 0.2282 0.0468  0.0110  -0.0302 668  ALA A C   
4882  O O   . ALA A 670  ? 0.2644 0.3100 0.2383 0.0480  0.0112  -0.0307 668  ALA A O   
4883  C CB  . ALA A 670  ? 0.2766 0.3151 0.2595 0.0502  0.0088  -0.0399 668  ALA A CB  
4884  N N   . ILE A 671  ? 0.2548 0.2906 0.2320 0.0449  0.0127  -0.0245 669  ILE A N   
4885  C CA  . ILE A 671  ? 0.2433 0.2831 0.2177 0.0439  0.0147  -0.0185 669  ILE A CA  
4886  C C   . ILE A 671  ? 0.2833 0.3203 0.2561 0.0425  0.0139  -0.0170 669  ILE A C   
4887  O O   . ILE A 671  ? 0.2787 0.3223 0.2487 0.0432  0.0146  -0.0151 669  ILE A O   
4888  C CB  . ILE A 671  ? 0.2742 0.3099 0.2501 0.0418  0.0162  -0.0131 669  ILE A CB  
4889  C CG1 . ILE A 671  ? 0.2756 0.3160 0.2527 0.0434  0.0173  -0.0139 669  ILE A CG1 
4890  C CG2 . ILE A 671  ? 0.3212 0.3592 0.2953 0.0405  0.0177  -0.0068 669  ILE A CG2 
4891  C CD1 . ILE A 671  ? 0.3142 0.3494 0.2935 0.0413  0.0183  -0.0096 669  ILE A CD1 
4892  N N   . ALA A 672  ? 0.2626 0.2903 0.2373 0.0406  0.0124  -0.0177 670  ALA A N   
4893  C CA  . ALA A 672  ? 0.2570 0.2819 0.2306 0.0393  0.0115  -0.0167 670  ALA A CA  
4894  C C   . ALA A 672  ? 0.2597 0.2903 0.2316 0.0413  0.0103  -0.0211 670  ALA A C   
4895  O O   . ALA A 672  ? 0.2675 0.3010 0.2371 0.0412  0.0104  -0.0193 670  ALA A O   
4896  C CB  . ALA A 672  ? 0.2805 0.2954 0.2568 0.0370  0.0100  -0.0173 670  ALA A CB  
4897  N N   . GLU A 673  ? 0.2574 0.2899 0.2307 0.0433  0.0090  -0.0270 671  GLU A N   
4898  C CA  . GLU A 673  ? 0.2672 0.3053 0.2392 0.0455  0.0076  -0.0321 671  GLU A CA  
4899  C C   . GLU A 673  ? 0.2530 0.3025 0.2210 0.0473  0.0092  -0.0304 671  GLU A C   
4900  O O   . GLU A 673  ? 0.2569 0.3104 0.2225 0.0477  0.0087  -0.0305 671  GLU A O   
4901  C CB  . GLU A 673  ? 0.2795 0.3178 0.2546 0.0475  0.0059  -0.0389 671  GLU A CB  
4902  C CG  . GLU A 673  ? 0.3207 0.3652 0.2952 0.0500  0.0042  -0.0452 671  GLU A CG  
4903  C CD  . GLU A 673  ? 0.3342 0.3721 0.3109 0.0487  0.0016  -0.0479 671  GLU A CD  
4904  O OE1 . GLU A 673  ? 0.3796 0.4081 0.3585 0.0459  0.0012  -0.0451 671  GLU A OE1 
4905  O OE2 . GLU A 673  ? 0.3068 0.3494 0.2830 0.0504  0.0001  -0.0528 671  GLU A OE2 
4906  N N   . VAL A 674  ? 0.2402 0.2954 0.2075 0.0484  0.0111  -0.0285 672  VAL A N   
4907  C CA  . VAL A 674  ? 0.2433 0.3102 0.2070 0.0500  0.0127  -0.0262 672  VAL A CA  
4908  C C   . VAL A 674  ? 0.2433 0.3098 0.2052 0.0480  0.0138  -0.0190 672  VAL A C   
4909  O O   . VAL A 674  ? 0.2356 0.3097 0.1947 0.0488  0.0140  -0.0177 672  VAL A O   
4910  C CB  . VAL A 674  ? 0.2476 0.3211 0.2115 0.0515  0.0145  -0.0258 672  VAL A CB  
4911  C CG1 . VAL A 674  ? 0.2523 0.3390 0.2126 0.0530  0.0162  -0.0228 672  VAL A CG1 
4912  C CG2 . VAL A 674  ? 0.2593 0.3335 0.2256 0.0538  0.0131  -0.0336 672  VAL A CG2 
4913  N N   . ARG A 675  ? 0.2336 0.2914 0.1975 0.0453  0.0144  -0.0144 673  ARG A N   
4914  C CA  . ARG A 675  ? 0.2167 0.2733 0.1798 0.0434  0.0151  -0.0081 673  ARG A CA  
4915  C C   . ARG A 675  ? 0.2216 0.2771 0.1835 0.0433  0.0135  -0.0098 673  ARG A C   
4916  O O   . ARG A 675  ? 0.2377 0.2982 0.1977 0.0434  0.0139  -0.0063 673  ARG A O   
4917  C CB  . ARG A 675  ? 0.2245 0.2713 0.1904 0.0407  0.0156  -0.0044 673  ARG A CB  
4918  C CG  . ARG A 675  ? 0.2291 0.2773 0.1963 0.0405  0.0173  -0.0012 673  ARG A CG  
4919  C CD  . ARG A 675  ? 0.2494 0.2887 0.2192 0.0377  0.0176  0.0028  673  ARG A CD  
4920  N NE  . ARG A 675  ? 0.2484 0.2880 0.2180 0.0365  0.0179  0.0080  673  ARG A NE  
4921  C CZ  . ARG A 675  ? 0.2641 0.2962 0.2359 0.0342  0.0178  0.0109  673  ARG A CZ  
4922  N NH1 . ARG A 675  ? 0.2633 0.2876 0.2373 0.0328  0.0173  0.0094  673  ARG A NH1 
4923  N NH2 . ARG A 675  ? 0.2529 0.2860 0.2250 0.0335  0.0179  0.0153  673  ARG A NH2 
4924  N N   . GLU A 676  ? 0.2246 0.2737 0.1879 0.0430  0.0116  -0.0149 674  GLU A N   
4925  C CA  . GLU A 676  ? 0.2329 0.2809 0.1954 0.0428  0.0100  -0.0166 674  GLU A CA  
4926  C C   . GLU A 676  ? 0.2307 0.2895 0.1902 0.0453  0.0096  -0.0191 674  GLU A C   
4927  O O   . GLU A 676  ? 0.2249 0.2865 0.1826 0.0452  0.0092  -0.0172 674  GLU A O   
4928  C CB  . GLU A 676  ? 0.2359 0.2756 0.2012 0.0419  0.0079  -0.0214 674  GLU A CB  
4929  C CG  . GLU A 676  ? 0.3001 0.3381 0.2648 0.0412  0.0063  -0.0225 674  GLU A CG  
4930  C CD  . GLU A 676  ? 0.4178 0.4461 0.3857 0.0393  0.0047  -0.0245 674  GLU A CD  
4931  O OE1 . GLU A 676  ? 0.5848 0.6098 0.5553 0.0395  0.0036  -0.0285 674  GLU A OE1 
4932  O OE2 . GLU A 676  ? 0.4920 0.5163 0.4601 0.0374  0.0044  -0.0219 674  GLU A OE2 
4933  N N   . ALA A 677  ? 0.2230 0.2885 0.1819 0.0477  0.0097  -0.0234 675  ALA A N   
4934  C CA  . ALA A 677  ? 0.2366 0.3137 0.1924 0.0503  0.0094  -0.0260 675  ALA A CA  
4935  C C   . ALA A 677  ? 0.2385 0.3237 0.1914 0.0503  0.0113  -0.0191 675  ALA A C   
4936  O O   . ALA A 677  ? 0.2259 0.3173 0.1763 0.0510  0.0108  -0.0184 675  ALA A O   
4937  C CB  . ALA A 677  ? 0.2267 0.3100 0.1827 0.0530  0.0093  -0.0319 675  ALA A CB  
4938  N N   . ILE A 678  ? 0.2373 0.3227 0.1908 0.0494  0.0133  -0.0138 676  ILE A N   
4939  C CA  . ILE A 678  ? 0.2301 0.3224 0.1819 0.0491  0.0150  -0.0063 676  ILE A CA  
4940  C C   . ILE A 678  ? 0.2286 0.3161 0.1807 0.0472  0.0144  -0.0021 676  ILE A C   
4941  O O   . ILE A 678  ? 0.2347 0.3296 0.1848 0.0477  0.0145  0.0014  676  ILE A O   
4942  C CB  . ILE A 678  ? 0.2472 0.3382 0.2010 0.0480  0.0170  -0.0015 676  ILE A CB  
4943  C CG1 . ILE A 678  ? 0.2501 0.3483 0.2032 0.0503  0.0178  -0.0055 676  ILE A CG1 
4944  C CG2 . ILE A 678  ? 0.2350 0.3306 0.1884 0.0469  0.0185  0.0071  676  ILE A CG2 
4945  C CD1 . ILE A 678  ? 0.2272 0.3218 0.1830 0.0491  0.0194  -0.0023 676  ILE A CD1 
4946  N N   . ASP A 679  ? 0.2185 0.2939 0.1734 0.0450  0.0136  -0.0023 677  ASP A N   
4947  C CA  . ASP A 679  ? 0.2166 0.2867 0.1722 0.0432  0.0129  0.0013  677  ASP A CA  
4948  C C   . ASP A 679  ? 0.2361 0.3096 0.1897 0.0443  0.0112  -0.0020 677  ASP A C   
4949  O O   . ASP A 679  ? 0.2304 0.3065 0.1833 0.0440  0.0110  0.0019  677  ASP A O   
4950  C CB  . ASP A 679  ? 0.2094 0.2669 0.1683 0.0409  0.0125  0.0010  677  ASP A CB  
4951  C CG  . ASP A 679  ? 0.2637 0.3177 0.2249 0.0396  0.0140  0.0050  677  ASP A CG  
4952  O OD1 . ASP A 679  ? 0.2745 0.3341 0.2354 0.0397  0.0155  0.0102  677  ASP A OD1 
4953  O OD2 . ASP A 679  ? 0.2892 0.3347 0.2526 0.0382  0.0138  0.0033  677  ASP A OD2 
4954  N N   . PHE A 680  ? 0.2188 0.2923 0.1719 0.0456  0.0097  -0.0094 678  PHE A N   
4955  C CA  . PHE A 680  ? 0.2276 0.3052 0.1790 0.0467  0.0080  -0.0130 678  PHE A CA  
4956  C C   . PHE A 680  ? 0.2296 0.3203 0.1776 0.0486  0.0086  -0.0105 678  PHE A C   
4957  O O   . PHE A 680  ? 0.2266 0.3204 0.1732 0.0486  0.0080  -0.0084 678  PHE A O   
4958  C CB  . PHE A 680  ? 0.2272 0.3041 0.1792 0.0481  0.0063  -0.0215 678  PHE A CB  
4959  C CG  . PHE A 680  ? 0.2242 0.2896 0.1795 0.0462  0.0047  -0.0244 678  PHE A CG  
4960  C CD1 . PHE A 680  ? 0.2275 0.2876 0.1835 0.0444  0.0038  -0.0225 678  PHE A CD1 
4961  C CD2 . PHE A 680  ? 0.2514 0.3115 0.2093 0.0462  0.0040  -0.0290 678  PHE A CD2 
4962  C CE1 . PHE A 680  ? 0.2293 0.2798 0.1882 0.0426  0.0024  -0.0249 678  PHE A CE1 
4963  C CE2 . PHE A 680  ? 0.2432 0.2934 0.2044 0.0444  0.0025  -0.0311 678  PHE A CE2 
4964  C CZ  . PHE A 680  ? 0.2376 0.2831 0.1992 0.0425  0.0017  -0.0290 678  PHE A CZ  
4965  N N   . LEU A 681  ? 0.2213 0.3203 0.1677 0.0503  0.0099  -0.0110 679  LEU A N   
4966  C CA  . LEU A 681  ? 0.2122 0.3252 0.1552 0.0522  0.0107  -0.0084 679  LEU A CA  
4967  C C   . LEU A 681  ? 0.2335 0.3474 0.1766 0.0507  0.0116  0.0007  679  LEU A C   
4968  O O   . LEU A 681  ? 0.2340 0.3550 0.1751 0.0513  0.0110  0.0028  679  LEU A O   
4969  C CB  . LEU A 681  ? 0.2394 0.3608 0.1814 0.0540  0.0123  -0.0094 679  LEU A CB  
4970  C CG  . LEU A 681  ? 0.2421 0.3654 0.1841 0.0562  0.0111  -0.0189 679  LEU A CG  
4971  C CD1 . LEU A 681  ? 0.2432 0.3699 0.1858 0.0572  0.0128  -0.0196 679  LEU A CD1 
4972  C CD2 . LEU A 681  ? 0.2470 0.3820 0.1857 0.0588  0.0099  -0.0235 679  LEU A CD2 
4973  N N   . ARG A 682  ? 0.2221 0.3291 0.1681 0.0486  0.0129  0.0061  680  ARG A N   
4974  C CA  . ARG A 682  ? 0.2130 0.3208 0.1600 0.0472  0.0137  0.0147  680  ARG A CA  
4975  C C   . ARG A 682  ? 0.2304 0.3310 0.1788 0.0459  0.0122  0.0157  680  ARG A C   
4976  O O   . ARG A 682  ? 0.2325 0.3373 0.1807 0.0457  0.0120  0.0211  680  ARG A O   
4977  C CB  . ARG A 682  ? 0.2071 0.3094 0.1573 0.0455  0.0153  0.0197  680  ARG A CB  
4978  C CG  . ARG A 682  ? 0.2288 0.3401 0.1779 0.0467  0.0170  0.0206  680  ARG A CG  
4979  C CD  . ARG A 682  ? 0.2457 0.3510 0.1983 0.0448  0.0184  0.0252  680  ARG A CD  
4980  N NE  . ARG A 682  ? 0.2643 0.3793 0.2159 0.0460  0.0202  0.0269  680  ARG A NE  
4981  C CZ  . ARG A 682  ? 0.2670 0.3787 0.2211 0.0450  0.0215  0.0286  680  ARG A CZ  
4982  N NH1 . ARG A 682  ? 0.2653 0.3645 0.2229 0.0429  0.0212  0.0289  680  ARG A NH1 
4983  N NH2 . ARG A 682  ? 0.2878 0.4096 0.2409 0.0462  0.0231  0.0300  680  ARG A NH2 
4984  N N   . TYR A 683  ? 0.2177 0.3079 0.1675 0.0449  0.0110  0.0106  681  TYR A N   
4985  C CA  . TYR A 683  ? 0.1986 0.2824 0.1498 0.0437  0.0096  0.0111  681  TYR A CA  
4986  C C   . TYR A 683  ? 0.2456 0.3371 0.1939 0.0453  0.0081  0.0087  681  TYR A C   
4987  O O   . TYR A 683  ? 0.2280 0.3211 0.1765 0.0450  0.0076  0.0128  681  TYR A O   
4988  C CB  . TYR A 683  ? 0.2093 0.2815 0.1627 0.0423  0.0087  0.0062  681  TYR A CB  
4989  C CG  . TYR A 683  ? 0.2194 0.2855 0.1743 0.0410  0.0073  0.0061  681  TYR A CG  
4990  C CD1 . TYR A 683  ? 0.2204 0.2810 0.1780 0.0393  0.0077  0.0114  681  TYR A CD1 
4991  C CD2 . TYR A 683  ? 0.2293 0.2952 0.1831 0.0416  0.0055  0.0004  681  TYR A CD2 
4992  C CE1 . TYR A 683  ? 0.2167 0.2724 0.1758 0.0383  0.0064  0.0111  681  TYR A CE1 
4993  C CE2 . TYR A 683  ? 0.2219 0.2829 0.1771 0.0404  0.0043  0.0004  681  TYR A CE2 
4994  C CZ  . TYR A 683  ? 0.2199 0.2759 0.1776 0.0389  0.0048  0.0058  681  TYR A CZ  
4995  O OH  . TYR A 683  ? 0.2353 0.2869 0.1946 0.0378  0.0036  0.0056  681  TYR A OH  
4996  N N   . TYR A 684  ? 0.2172 0.3137 0.1631 0.0471  0.0073  0.0019  682  TYR A N   
4997  C CA  . TYR A 684  ? 0.2121 0.3162 0.1554 0.0487  0.0058  -0.0008 682  TYR A CA  
4998  C C   . TYR A 684  ? 0.2369 0.3538 0.1776 0.0500  0.0066  0.0047  682  TYR A C   
4999  O O   . TYR A 684  ? 0.2409 0.3629 0.1803 0.0506  0.0055  0.0061  682  TYR A O   
5000  C CB  . TYR A 684  ? 0.2150 0.3217 0.1571 0.0505  0.0045  -0.0099 682  TYR A CB  
5001  C CG  . TYR A 684  ? 0.2094 0.3040 0.1545 0.0490  0.0032  -0.0150 682  TYR A CG  
5002  C CD1 . TYR A 684  ? 0.2306 0.3164 0.1779 0.0470  0.0023  -0.0135 682  TYR A CD1 
5003  C CD2 . TYR A 684  ? 0.2180 0.3103 0.1641 0.0497  0.0029  -0.0211 682  TYR A CD2 
5004  C CE1 . TYR A 684  ? 0.2301 0.3058 0.1803 0.0456  0.0012  -0.0176 682  TYR A CE1 
5005  C CE2 . TYR A 684  ? 0.2161 0.2977 0.1654 0.0483  0.0016  -0.0251 682  TYR A CE2 
5006  C CZ  . TYR A 684  ? 0.2308 0.3042 0.1820 0.0461  0.0008  -0.0232 682  TYR A CZ  
5007  O OH  . TYR A 684  ? 0.2386 0.3023 0.1931 0.0446  -0.0004 -0.0267 682  TYR A OH  
5008  N N   . ALA A 685  ? 0.2122 0.3347 0.1523 0.0505  0.0085  0.0084  683  ALA A N   
5009  C CA  . ALA A 685  ? 0.2205 0.3550 0.1588 0.0513  0.0094  0.0152  683  ALA A CA  
5010  C C   . ALA A 685  ? 0.2439 0.3741 0.1848 0.0495  0.0092  0.0230  683  ALA A C   
5011  O O   . ALA A 685  ? 0.2233 0.3612 0.1629 0.0501  0.0085  0.0266  683  ALA A O   
5012  C CB  . ALA A 685  ? 0.2160 0.3563 0.1540 0.0517  0.0116  0.0182  683  ALA A CB  
5013  N N   . GLU A 686  ? 0.2428 0.3611 0.1877 0.0473  0.0097  0.0257  684  GLU A N   
5014  C CA  . GLU A 686  ? 0.2383 0.3522 0.1866 0.0456  0.0093  0.0326  684  GLU A CA  
5015  C C   . GLU A 686  ? 0.2284 0.3392 0.1766 0.0456  0.0074  0.0301  684  GLU A C   
5016  O O   . GLU A 686  ? 0.2409 0.3554 0.1898 0.0457  0.0066  0.0352  684  GLU A O   
5017  C CB  . GLU A 686  ? 0.2856 0.3878 0.2384 0.0434  0.0102  0.0351  684  GLU A CB  
5018  C CG  . GLU A 686  ? 0.2988 0.3950 0.2559 0.0418  0.0095  0.0410  684  GLU A CG  
5019  C CD  . GLU A 686  ? 0.3677 0.4727 0.3259 0.0421  0.0098  0.0497  684  GLU A CD  
5020  O OE1 . GLU A 686  ? 0.3390 0.4545 0.2950 0.0431  0.0109  0.0523  684  GLU A OE1 
5021  O OE2 . GLU A 686  ? 0.3786 0.4803 0.3403 0.0413  0.0088  0.0541  684  GLU A OE2 
5022  N N   . GLN A 687  ? 0.2234 0.3276 0.1712 0.0455  0.0064  0.0225  685  GLN A N   
5023  C CA  . GLN A 687  ? 0.2262 0.3279 0.1740 0.0455  0.0045  0.0199  685  GLN A CA  
5024  C C   . GLN A 687  ? 0.2458 0.3600 0.1901 0.0475  0.0035  0.0198  685  GLN A C   
5025  O O   . GLN A 687  ? 0.2535 0.3687 0.1982 0.0475  0.0023  0.0220  685  GLN A O   
5026  C CB  . GLN A 687  ? 0.2317 0.3255 0.1797 0.0451  0.0035  0.0117  685  GLN A CB  
5027  C CG  . GLN A 687  ? 0.2213 0.3026 0.1730 0.0429  0.0042  0.0120  685  GLN A CG  
5028  C CD  . GLN A 687  ? 0.2903 0.3658 0.2454 0.0413  0.0039  0.0171  685  GLN A CD  
5029  O OE1 . GLN A 687  ? 0.2705 0.3455 0.2259 0.0413  0.0025  0.0163  685  GLN A OE1 
5030  N NE2 . GLN A 687  ? 0.3219 0.3932 0.2799 0.0401  0.0052  0.0221  685  GLN A NE2 
5031  N N   . THR A 688  ? 0.2201 0.3444 0.1608 0.0494  0.0041  0.0173  686  THR A N   
5032  C CA  . THR A 688  ? 0.2336 0.3714 0.1706 0.0514  0.0033  0.0174  686  THR A CA  
5033  C C   . THR A 688  ? 0.2295 0.3734 0.1672 0.0512  0.0037  0.0271  686  THR A C   
5034  O O   . THR A 688  ? 0.2457 0.3944 0.1827 0.0517  0.0024  0.0290  686  THR A O   
5035  C CB  . THR A 688  ? 0.2349 0.3830 0.1682 0.0536  0.0040  0.0130  686  THR A CB  
5036  O OG1 . THR A 688  ? 0.2480 0.3909 0.1812 0.0541  0.0029  0.0035  686  THR A OG1 
5037  C CG2 . THR A 688  ? 0.2541 0.4182 0.1835 0.0557  0.0034  0.0142  686  THR A CG2 
5038  N N   . ARG A 689  ? 0.2525 0.3963 0.1921 0.0503  0.0055  0.0335  687  ARG A N   
5039  C CA  . ARG A 689  ? 0.2720 0.4212 0.2133 0.0498  0.0058  0.0433  687  ARG A CA  
5040  C C   . ARG A 689  ? 0.2692 0.4097 0.2146 0.0484  0.0045  0.0468  687  ARG A C   
5041  O O   . ARG A 689  ? 0.2765 0.4226 0.2231 0.0485  0.0039  0.0537  687  ARG A O   
5042  C CB  . ARG A 689  ? 0.2643 0.4133 0.2079 0.0488  0.0078  0.0492  687  ARG A CB  
5043  C CG  . ARG A 689  ? 0.2940 0.4546 0.2337 0.0504  0.0093  0.0476  687  ARG A CG  
5044  C CD  . ARG A 689  ? 0.3116 0.4731 0.2541 0.0492  0.0112  0.0549  687  ARG A CD  
5045  N NE  . ARG A 689  ? 0.3157 0.4634 0.2618 0.0475  0.0119  0.0529  687  ARG A NE  
5046  C CZ  . ARG A 689  ? 0.3210 0.4670 0.2659 0.0478  0.0131  0.0480  687  ARG A CZ  
5047  N NH1 . ARG A 689  ? 0.3349 0.4920 0.2756 0.0499  0.0137  0.0441  687  ARG A NH1 
5048  N NH2 . ARG A 689  ? 0.3147 0.4483 0.2633 0.0461  0.0135  0.0470  687  ARG A NH2 
5049  N N   . ARG A 690  ? 0.2314 0.3588 0.1793 0.0471  0.0040  0.0422  688  ARG A N   
5050  C CA  . ARG A 690  ? 0.2517 0.3712 0.2034 0.0459  0.0026  0.0444  688  ARG A CA  
5051  C C   . ARG A 690  ? 0.2793 0.4022 0.2289 0.0470  0.0007  0.0408  688  ARG A C   
5052  O O   . ARG A 690  ? 0.2685 0.3886 0.2210 0.0464  -0.0005 0.0441  688  ARG A O   
5053  C CB  . ARG A 690  ? 0.2528 0.3579 0.2079 0.0441  0.0029  0.0409  688  ARG A CB  
5054  C CG  . ARG A 690  ? 0.2830 0.3832 0.2412 0.0428  0.0045  0.0449  688  ARG A CG  
5055  C CD  . ARG A 690  ? 0.2834 0.3823 0.2467 0.0418  0.0044  0.0536  688  ARG A CD  
5056  N NE  . ARG A 690  ? 0.3192 0.4097 0.2863 0.0410  0.0030  0.0532  688  ARG A NE  
5057  C CZ  . ARG A 690  ? 0.3439 0.4374 0.3125 0.0415  0.0015  0.0567  688  ARG A CZ  
5058  N NH1 . ARG A 690  ? 0.3205 0.4254 0.2870 0.0427  0.0012  0.0611  688  ARG A NH1 
5059  N NH2 . ARG A 690  ? 0.3051 0.3904 0.2774 0.0407  0.0004  0.0557  688  ARG A NH2 
5060  N N   . THR A 691  ? 0.2477 0.3763 0.1928 0.0484  0.0002  0.0338  689  THR A N   
5061  C CA  . THR A 691  ? 0.2608 0.3898 0.2048 0.0490  -0.0018 0.0290  689  THR A CA  
5062  C C   . THR A 691  ? 0.2754 0.4182 0.2147 0.0513  -0.0028 0.0269  689  THR A C   
5063  O O   . THR A 691  ? 0.3092 0.4559 0.2484 0.0518  -0.0044 0.0283  689  THR A O   
5064  C CB  . THR A 691  ? 0.2401 0.3593 0.1846 0.0483  -0.0024 0.0206  689  THR A CB  
5065  O OG1 . THR A 691  ? 0.2672 0.3887 0.2091 0.0491  -0.0015 0.0155  689  THR A OG1 
5066  C CG2 . THR A 691  ? 0.2593 0.3650 0.2085 0.0460  -0.0018 0.0223  689  THR A CG2 
5067  N N   . LEU A 692  ? 0.2490 0.3997 0.1846 0.0527  -0.0021 0.0232  690  LEU A N   
5068  C CA  . LEU A 692  ? 0.2694 0.4314 0.2007 0.0549  -0.0034 0.0177  690  LEU A CA  
5069  C C   . LEU A 692  ? 0.2615 0.4377 0.1903 0.0563  -0.0037 0.0241  690  LEU A C   
5070  O O   . LEU A 692  ? 0.2979 0.4808 0.2264 0.0564  -0.0021 0.0309  690  LEU A O   
5071  C CB  . LEU A 692  ? 0.2783 0.4438 0.2069 0.0562  -0.0027 0.0106  690  LEU A CB  
5072  C CG  . LEU A 692  ? 0.2738 0.4262 0.2048 0.0551  -0.0031 0.0033  690  LEU A CG  
5073  C CD1 . LEU A 692  ? 0.3110 0.4683 0.2397 0.0568  -0.0031 -0.0046 690  LEU A CD1 
5074  C CD2 . LEU A 692  ? 0.3108 0.4566 0.2435 0.0543  -0.0053 -0.0005 690  LEU A CD2 
5075  N N   . GLY A 693  ? 0.2634 0.4448 0.1908 0.0572  -0.0057 0.0220  691  GLY A N   
5076  C CA  . GLY A 693  ? 0.3043 0.5001 0.2291 0.0587  -0.0063 0.0272  691  GLY A CA  
5077  C C   . GLY A 693  ? 0.3337 0.5401 0.2542 0.0609  -0.0080 0.0196  691  GLY A C   
5078  O O   . GLY A 693  ? 0.3428 0.5452 0.2627 0.0613  -0.0088 0.0101  691  GLY A O   
5079  N N   . PRO A 694  ? 0.3604 0.5804 0.2783 0.0623  -0.0089 0.0237  692  PRO A N   
5080  C CA  . PRO A 694  ? 0.3528 0.5850 0.2662 0.0647  -0.0106 0.0164  692  PRO A CA  
5081  C C   . PRO A 694  ? 0.3991 0.6235 0.3138 0.0644  -0.0129 0.0080  692  PRO A C   
5082  O O   . PRO A 694  ? 0.4136 0.6435 0.3258 0.0661  -0.0142 -0.0011 692  PRO A O   
5083  C CB  . PRO A 694  ? 0.4136 0.6603 0.3249 0.0657  -0.0112 0.0245  692  PRO A CB  
5084  C CG  . PRO A 694  ? 0.3585 0.6033 0.2725 0.0642  -0.0092 0.0357  692  PRO A CG  
5085  C CD  . PRO A 694  ? 0.3377 0.5633 0.2568 0.0619  -0.0085 0.0353  692  PRO A CD  
5086  N N   . GLY A 695  ? 0.3146 0.5267 0.2336 0.0625  -0.0136 0.0106  693  GLY A N   
5087  C CA  . GLY A 695  ? 0.3664 0.5713 0.2869 0.0620  -0.0157 0.0035  693  GLY A CA  
5088  C C   . GLY A 695  ? 0.3581 0.5508 0.2808 0.0610  -0.0156 -0.0045 693  GLY A C   
5089  O O   . GLY A 695  ? 0.3799 0.5667 0.3042 0.0604  -0.0174 -0.0106 693  GLY A O   
5090  N N   . HIS A 696  ? 0.3352 0.5239 0.2581 0.0605  -0.0136 -0.0044 694  HIS A N   
5091  C CA  . HIS A 696  ? 0.3291 0.5066 0.2542 0.0596  -0.0134 -0.0116 694  HIS A CA  
5092  C C   . HIS A 696  ? 0.3387 0.5251 0.2606 0.0618  -0.0137 -0.0191 694  HIS A C   
5093  O O   . HIS A 696  ? 0.3667 0.5549 0.2877 0.0623  -0.0118 -0.0187 694  HIS A O   
5094  C CB  . HIS A 696  ? 0.3219 0.4880 0.2499 0.0575  -0.0112 -0.0066 694  HIS A CB  
5095  C CG  . HIS A 696  ? 0.2851 0.4453 0.2161 0.0559  -0.0109 0.0017  694  HIS A CG  
5096  N ND1 . HIS A 696  ? 0.3072 0.4698 0.2386 0.0556  -0.0092 0.0107  694  HIS A ND1 
5097  C CD2 . HIS A 696  ? 0.3028 0.4552 0.2368 0.0545  -0.0122 0.0022  694  HIS A CD2 
5098  C CE1 . HIS A 696  ? 0.3061 0.4621 0.2411 0.0541  -0.0096 0.0161  694  HIS A CE1 
5099  N NE2 . HIS A 696  ? 0.3233 0.4734 0.2597 0.0536  -0.0113 0.0110  694  HIS A NE2 
5100  N N   . GLY A 697  ? 0.3566 0.5494 0.2772 0.0632  -0.0160 -0.0261 695  GLY A N   
5101  C CA  . GLY A 697  ? 0.3371 0.5398 0.2550 0.0657  -0.0167 -0.0341 695  GLY A CA  
5102  C C   . GLY A 697  ? 0.2979 0.4903 0.2188 0.0651  -0.0167 -0.0414 695  GLY A C   
5103  O O   . GLY A 697  ? 0.3057 0.4846 0.2307 0.0630  -0.0174 -0.0432 695  GLY A O   
5104  N N   . PRO A 698  ? 0.3173 0.5164 0.2364 0.0670  -0.0159 -0.0455 696  PRO A N   
5105  C CA  . PRO A 698  ? 0.3381 0.5280 0.2604 0.0667  -0.0162 -0.0528 696  PRO A CA  
5106  C C   . PRO A 698  ? 0.2961 0.4833 0.2210 0.0670  -0.0194 -0.0625 696  PRO A C   
5107  O O   . PRO A 698  ? 0.3318 0.5278 0.2551 0.0684  -0.0214 -0.0655 696  PRO A O   
5108  C CB  . PRO A 698  ? 0.3565 0.5575 0.2758 0.0692  -0.0148 -0.0551 696  PRO A CB  
5109  C CG  . PRO A 698  ? 0.4129 0.6311 0.3274 0.0714  -0.0150 -0.0531 696  PRO A CG  
5110  C CD  . PRO A 698  ? 0.4122 0.6282 0.3265 0.0696  -0.0148 -0.0439 696  PRO A CD  
5111  N N   . LEU A 699  ? 0.2884 0.4628 0.2180 0.0656  -0.0200 -0.0670 697  LEU A N   
5112  C CA  . LEU A 699  ? 0.2729 0.4441 0.2060 0.0659  -0.0232 -0.0765 697  LEU A CA  
5113  C C   . LEU A 699  ? 0.2844 0.4683 0.2159 0.0693  -0.0247 -0.0854 697  LEU A C   
5114  O O   . LEU A 699  ? 0.3204 0.5097 0.2525 0.0705  -0.0275 -0.0919 697  LEU A O   
5115  C CB  . LEU A 699  ? 0.2582 0.4138 0.1969 0.0637  -0.0235 -0.0788 697  LEU A CB  
5116  C CG  . LEU A 699  ? 0.2985 0.4409 0.2396 0.0602  -0.0224 -0.0717 697  LEU A CG  
5117  C CD1 . LEU A 699  ? 0.2924 0.4216 0.2388 0.0584  -0.0227 -0.0746 697  LEU A CD1 
5118  C CD2 . LEU A 699  ? 0.3344 0.4761 0.2763 0.0591  -0.0243 -0.0711 697  LEU A CD2 
5119  N N   . GLY A 700  ? 0.2861 0.4752 0.2158 0.0710  -0.0229 -0.0861 698  GLY A N   
5120  C CA  . GLY A 700  ? 0.2638 0.4635 0.1930 0.0743  -0.0243 -0.0955 698  GLY A CA  
5121  C C   . GLY A 700  ? 0.2756 0.4677 0.2083 0.0743  -0.0235 -0.0990 698  GLY A C   
5122  O O   . GLY A 700  ? 0.2948 0.4771 0.2285 0.0722  -0.0213 -0.0925 698  GLY A O   
5123  N N   . PRO A 701  ? 0.2794 0.4757 0.2143 0.0768  -0.0256 -0.1095 699  PRO A N   
5124  C CA  . PRO A 701  ? 0.2700 0.4594 0.2087 0.0771  -0.0251 -0.1131 699  PRO A CA  
5125  C C   . PRO A 701  ? 0.2762 0.4466 0.2206 0.0735  -0.0255 -0.1107 699  PRO A C   
5126  O O   . PRO A 701  ? 0.2798 0.4427 0.2283 0.0720  -0.0281 -0.1136 699  PRO A O   
5127  C CB  . PRO A 701  ? 0.3016 0.4982 0.2430 0.0803  -0.0282 -0.1258 699  PRO A CB  
5128  C CG  . PRO A 701  ? 0.3164 0.5301 0.2523 0.0827  -0.0288 -0.1272 699  PRO A CG  
5129  C CD  . PRO A 701  ? 0.2818 0.4914 0.2156 0.0799  -0.0283 -0.1184 699  PRO A CD  
5130  N N   . ILE A 702  ? 0.2694 0.4327 0.2140 0.0722  -0.0228 -0.1049 700  ILE A N   
5131  C CA  A ILE A 702  ? 0.2503 0.3966 0.2000 0.0689  -0.0228 -0.1021 700  ILE A CA  
5132  C CA  B ILE A 702  ? 0.2505 0.3968 0.2001 0.0688  -0.0228 -0.1020 700  ILE A CA  
5133  C C   . ILE A 702  ? 0.2511 0.3925 0.2052 0.0697  -0.0233 -0.1077 700  ILE A C   
5134  O O   . ILE A 702  ? 0.2629 0.4110 0.2147 0.0718  -0.0214 -0.1079 700  ILE A O   
5135  C CB  A ILE A 702  ? 0.2592 0.3999 0.2062 0.0662  -0.0197 -0.0907 700  ILE A CB  
5136  C CB  B ILE A 702  ? 0.2588 0.3999 0.2056 0.0663  -0.0195 -0.0906 700  ILE A CB  
5137  C CG1 A ILE A 702  ? 0.2649 0.4074 0.2094 0.0649  -0.0199 -0.0858 700  ILE A CG1 
5138  C CG1 B ILE A 702  ? 0.2720 0.4179 0.2151 0.0656  -0.0192 -0.0848 700  ILE A CG1 
5139  C CG2 A ILE A 702  ? 0.2582 0.3827 0.2101 0.0632  -0.0193 -0.0884 700  ILE A CG2 
5140  C CG2 B ILE A 702  ? 0.2585 0.3829 0.2103 0.0630  -0.0194 -0.0880 700  ILE A CG2 
5141  C CD1 A ILE A 702  ? 0.2463 0.3831 0.1892 0.0624  -0.0172 -0.0752 700  ILE A CD1 
5142  C CD1 B ILE A 702  ? 0.2624 0.4014 0.2087 0.0638  -0.0218 -0.0870 700  ILE A CD1 
5143  N N   . VAL A 703  ? 0.2541 0.3841 0.2149 0.0682  -0.0259 -0.1122 701  VAL A N   
5144  C CA  . VAL A 703  ? 0.2691 0.3924 0.2353 0.0687  -0.0267 -0.1170 701  VAL A CA  
5145  C C   . VAL A 703  ? 0.2546 0.3653 0.2220 0.0654  -0.0245 -0.1090 701  VAL A C   
5146  O O   . VAL A 703  ? 0.2618 0.3630 0.2311 0.0623  -0.0249 -0.1046 701  VAL A O   
5147  C CB  . VAL A 703  ? 0.2697 0.3877 0.2433 0.0687  -0.0310 -0.1259 701  VAL A CB  
5148  C CG1 . VAL A 703  ? 0.2827 0.3915 0.2629 0.0685  -0.0321 -0.1295 701  VAL A CG1 
5149  C CG2 . VAL A 703  ? 0.3002 0.4318 0.2726 0.0723  -0.0333 -0.1350 701  VAL A CG2 
5150  N N   . CYS A 704  ? 0.2393 0.3510 0.2056 0.0663  -0.0222 -0.1068 702  CYS A N   
5151  C CA  . CYS A 704  ? 0.2424 0.3431 0.2097 0.0635  -0.0200 -0.0997 702  CYS A CA  
5152  C C   . CYS A 704  ? 0.2763 0.3695 0.2501 0.0638  -0.0216 -0.1049 702  CYS A C   
5153  O O   . CYS A 704  ? 0.2582 0.3576 0.2324 0.0666  -0.0214 -0.1097 702  CYS A O   
5154  C CB  . CYS A 704  ? 0.2601 0.3670 0.2217 0.0640  -0.0162 -0.0926 702  CYS A CB  
5155  S SG  . CYS A 704  ? 0.2600 0.3757 0.2148 0.0637  -0.0145 -0.0856 702  CYS A SG  
5156  N N   . ILE A 705  ? 0.2369 0.3174 0.2161 0.0608  -0.0231 -0.1038 703  ILE A N   
5157  C CA  . ILE A 705  ? 0.2688 0.3407 0.2550 0.0606  -0.0249 -0.1078 703  ILE A CA  
5158  C C   . ILE A 705  ? 0.2339 0.2958 0.2205 0.0575  -0.0227 -0.0998 703  ILE A C   
5159  O O   . ILE A 705  ? 0.2399 0.2961 0.2253 0.0545  -0.0219 -0.0936 703  ILE A O   
5160  C CB  . ILE A 705  ? 0.2475 0.3136 0.2405 0.0596  -0.0290 -0.1136 703  ILE A CB  
5161  C CG1 . ILE A 705  ? 0.2610 0.3376 0.2541 0.0629  -0.0314 -0.1226 703  ILE A CG1 
5162  C CG2 . ILE A 705  ? 0.2618 0.3175 0.2628 0.0586  -0.0310 -0.1159 703  ILE A CG2 
5163  C CD1 . ILE A 705  ? 0.3011 0.3734 0.3000 0.0618  -0.0353 -0.1273 703  ILE A CD1 
5164  N N   . SER A 706  ? 0.2437 0.3040 0.2319 0.0584  -0.0217 -0.1002 704  SER A N   
5165  C CA  . SER A 706  ? 0.2485 0.3016 0.2358 0.0560  -0.0191 -0.0924 704  SER A CA  
5166  C C   . SER A 706  ? 0.2525 0.2963 0.2468 0.0552  -0.0207 -0.0943 704  SER A C   
5167  O O   . SER A 706  ? 0.2636 0.3081 0.2628 0.0572  -0.0233 -0.1018 704  SER A O   
5168  C CB  . SER A 706  ? 0.2787 0.3401 0.2600 0.0576  -0.0156 -0.0886 704  SER A CB  
5169  O OG  . SER A 706  ? 0.2716 0.3412 0.2534 0.0612  -0.0161 -0.0953 704  SER A OG  
5170  N N   . PRO A 707  ? 0.2509 0.2858 0.2459 0.0522  -0.0193 -0.0877 705  PRO A N   
5171  C CA  . PRO A 707  ? 0.2698 0.2955 0.2715 0.0510  -0.0208 -0.0885 705  PRO A CA  
5172  C C   . PRO A 707  ? 0.2344 0.2624 0.2356 0.0528  -0.0191 -0.0884 705  PRO A C   
5173  O O   . PRO A 707  ? 0.2747 0.3104 0.2702 0.0543  -0.0162 -0.0862 705  PRO A O   
5174  C CB  . PRO A 707  ? 0.2595 0.2766 0.2609 0.0470  -0.0197 -0.0807 705  PRO A CB  
5175  C CG  . PRO A 707  ? 0.2518 0.2742 0.2456 0.0469  -0.0163 -0.0750 705  PRO A CG  
5176  C CD  . PRO A 707  ? 0.2504 0.2834 0.2406 0.0496  -0.0166 -0.0792 705  PRO A CD  
5177  N N   . TRP A 708  ? 0.2558 0.2771 0.2635 0.0526  -0.0208 -0.0906 706  TRP A N   
5178  C CA  . TRP A 708  ? 0.2532 0.2766 0.2610 0.0545  -0.0193 -0.0909 706  TRP A CA  
5179  C C   . TRP A 708  ? 0.2772 0.2970 0.2815 0.0522  -0.0161 -0.0824 706  TRP A C   
5180  O O   . TRP A 708  ? 0.2777 0.3019 0.2795 0.0537  -0.0139 -0.0812 706  TRP A O   
5181  C CB  . TRP A 708  ? 0.2440 0.2616 0.2605 0.0553  -0.0224 -0.0962 706  TRP A CB  
5182  C CG  . TRP A 708  ? 0.2718 0.2780 0.2926 0.0517  -0.0233 -0.0911 706  TRP A CG  
5183  C CD1 . TRP A 708  ? 0.2699 0.2687 0.2957 0.0491  -0.0260 -0.0909 706  TRP A CD1 
5184  C CD2 . TRP A 708  ? 0.2668 0.2682 0.2873 0.0500  -0.0213 -0.0850 706  TRP A CD2 
5185  N NE1 . TRP A 708  ? 0.2786 0.2688 0.3070 0.0460  -0.0258 -0.0849 706  TRP A NE1 
5186  C CE2 . TRP A 708  ? 0.2565 0.2481 0.2816 0.0466  -0.0229 -0.0814 706  TRP A CE2 
5187  C CE3 . TRP A 708  ? 0.2632 0.2682 0.2802 0.0511  -0.0183 -0.0824 706  TRP A CE3 
5188  C CZ2 . TRP A 708  ? 0.2477 0.2333 0.2737 0.0443  -0.0217 -0.0754 706  TRP A CZ2 
5189  C CZ3 . TRP A 708  ? 0.2701 0.2684 0.2880 0.0488  -0.0172 -0.0765 706  TRP A CZ3 
5190  C CH2 . TRP A 708  ? 0.2605 0.2494 0.2829 0.0455  -0.0189 -0.0732 706  TRP A CH2 
5191  N N   . ASN A 709  ? 0.2602 0.2727 0.2643 0.0486  -0.0158 -0.0765 707  ASN A N   
5192  C CA  . ASN A 709  ? 0.2852 0.2923 0.2886 0.0463  -0.0137 -0.0698 707  ASN A CA  
5193  C C   . ASN A 709  ? 0.2855 0.2977 0.2819 0.0462  -0.0101 -0.0642 707  ASN A C   
5194  O O   . ASN A 709  ? 0.2733 0.2831 0.2689 0.0452  -0.0081 -0.0596 707  ASN A O   
5195  C CB  . ASN A 709  ? 0.2758 0.2735 0.2823 0.0426  -0.0150 -0.0660 707  ASN A CB  
5196  C CG  . ASN A 709  ? 0.2854 0.2840 0.2880 0.0409  -0.0142 -0.0628 707  ASN A CG  
5197  O OD1 . ASN A 709  ? 0.3038 0.3062 0.3059 0.0419  -0.0156 -0.0666 707  ASN A OD1 
5198  N ND2 . ASN A 709  ? 0.2930 0.2883 0.2928 0.0384  -0.0122 -0.0561 707  ASN A ND2 
5199  N N   . PHE A 710  ? 0.2650 0.2839 0.2567 0.0470  -0.0092 -0.0641 708  PHE A N   
5200  C CA  . PHE A 710  ? 0.2742 0.2997 0.2598 0.0475  -0.0061 -0.0595 708  PHE A CA  
5201  C C   . PHE A 710  ? 0.2677 0.3043 0.2509 0.0510  -0.0061 -0.0645 708  PHE A C   
5202  O O   . PHE A 710  ? 0.2777 0.3202 0.2574 0.0516  -0.0060 -0.0647 708  PHE A O   
5203  C CB  . PHE A 710  ? 0.2845 0.3082 0.2669 0.0451  -0.0051 -0.0540 708  PHE A CB  
5204  C CG  . PHE A 710  ? 0.3020 0.3159 0.2867 0.0417  -0.0050 -0.0494 708  PHE A CG  
5205  C CD1 . PHE A 710  ? 0.3230 0.3321 0.3097 0.0408  -0.0042 -0.0471 708  PHE A CD1 
5206  C CD2 . PHE A 710  ? 0.3169 0.3269 0.3015 0.0395  -0.0058 -0.0474 708  PHE A CD2 
5207  C CE1 . PHE A 710  ? 0.3368 0.3379 0.3253 0.0377  -0.0042 -0.0430 708  PHE A CE1 
5208  C CE2 . PHE A 710  ? 0.3351 0.3372 0.3217 0.0364  -0.0057 -0.0433 708  PHE A CE2 
5209  C CZ  . PHE A 710  ? 0.3375 0.3353 0.3259 0.0356  -0.0049 -0.0411 708  PHE A CZ  
5210  N N   . PRO A 711  ? 0.2644 0.3046 0.2495 0.0536  -0.0063 -0.0689 709  PRO A N   
5211  C CA  . PRO A 711  ? 0.2685 0.3190 0.2528 0.0572  -0.0072 -0.0758 709  PRO A CA  
5212  C C   . PRO A 711  ? 0.2462 0.3084 0.2241 0.0588  -0.0046 -0.0733 709  PRO A C   
5213  O O   . PRO A 711  ? 0.2734 0.3454 0.2497 0.0616  -0.0053 -0.0786 709  PRO A O   
5214  C CB  . PRO A 711  ? 0.2849 0.3350 0.2736 0.0592  -0.0080 -0.0805 709  PRO A CB  
5215  C CG  . PRO A 711  ? 0.2663 0.3110 0.2548 0.0571  -0.0057 -0.0738 709  PRO A CG  
5216  C CD  . PRO A 711  ? 0.2567 0.2923 0.2450 0.0533  -0.0058 -0.0680 709  PRO A CD  
5217  N N   . LEU A 712  ? 0.2682 0.3302 0.2426 0.0571  -0.0018 -0.0655 710  LEU A N   
5218  C CA  . LEU A 712  ? 0.2353 0.3081 0.2041 0.0581  0.0006  -0.0618 710  LEU A CA  
5219  C C   . LEU A 712  ? 0.2523 0.3228 0.2181 0.0557  0.0013  -0.0557 710  LEU A C   
5220  O O   . LEU A 712  ? 0.2477 0.3265 0.2099 0.0568  0.0015  -0.0554 710  LEU A O   
5221  C CB  . LEU A 712  ? 0.2625 0.3389 0.2299 0.0585  0.0034  -0.0576 710  LEU A CB  
5222  C CG  . LEU A 712  ? 0.2667 0.3549 0.2288 0.0595  0.0058  -0.0532 710  LEU A CG  
5223  C CD1 . LEU A 712  ? 0.2451 0.3462 0.2052 0.0630  0.0050  -0.0596 710  LEU A CD1 
5224  C CD2 . LEU A 712  ? 0.2975 0.3878 0.2590 0.0591  0.0086  -0.0478 710  LEU A CD2 
5225  N N   . ALA A 713  ? 0.2554 0.3152 0.2230 0.0526  0.0015  -0.0510 711  ALA A N   
5226  C CA  . ALA A 713  ? 0.2378 0.2958 0.2030 0.0504  0.0023  -0.0449 711  ALA A CA  
5227  C C   . ALA A 713  ? 0.2483 0.3067 0.2131 0.0504  0.0002  -0.0478 711  ALA A C   
5228  O O   . ALA A 713  ? 0.2514 0.3165 0.2127 0.0509  0.0008  -0.0456 711  ALA A O   
5229  C CB  . ALA A 713  ? 0.2426 0.2894 0.2100 0.0472  0.0029  -0.0400 711  ALA A CB  
5230  N N   . ILE A 714  ? 0.2446 0.2958 0.2133 0.0496  -0.0022 -0.0523 712  ILE A N   
5231  C CA  . ILE A 714  ? 0.2233 0.2746 0.1922 0.0494  -0.0043 -0.0551 712  ILE A CA  
5232  C C   . ILE A 714  ? 0.2424 0.3049 0.2092 0.0526  -0.0053 -0.0607 712  ILE A C   
5233  O O   . ILE A 714  ? 0.2506 0.3184 0.2147 0.0530  -0.0057 -0.0605 712  ILE A O   
5234  C CB  . ILE A 714  ? 0.2638 0.3051 0.2382 0.0477  -0.0069 -0.0583 712  ILE A CB  
5235  C CG1 . ILE A 714  ? 0.2804 0.3123 0.2557 0.0443  -0.0058 -0.0520 712  ILE A CG1 
5236  C CG2 . ILE A 714  ? 0.2624 0.3049 0.2376 0.0479  -0.0095 -0.0626 712  ILE A CG2 
5237  C CD1 . ILE A 714  ? 0.3795 0.4030 0.3590 0.0420  -0.0080 -0.0530 712  ILE A CD1 
5238  N N   . PHE A 715  ? 0.2406 0.3073 0.2088 0.0551  -0.0056 -0.0659 713  PHE A N   
5239  C CA  . PHE A 715  ? 0.2493 0.3281 0.2153 0.0585  -0.0063 -0.0716 713  PHE A CA  
5240  C C   . PHE A 715  ? 0.2450 0.3342 0.2050 0.0592  -0.0040 -0.0664 713  PHE A C   
5241  O O   . PHE A 715  ? 0.2422 0.3388 0.1996 0.0604  -0.0049 -0.0683 713  PHE A O   
5242  C CB  . PHE A 715  ? 0.2314 0.3134 0.1996 0.0609  -0.0062 -0.0764 713  PHE A CB  
5243  C CG  . PHE A 715  ? 0.2573 0.3528 0.2234 0.0647  -0.0066 -0.0826 713  PHE A CG  
5244  C CD1 . PHE A 715  ? 0.2647 0.3619 0.2336 0.0665  -0.0098 -0.0912 713  PHE A CD1 
5245  C CD2 . PHE A 715  ? 0.2839 0.3909 0.2454 0.0666  -0.0040 -0.0800 713  PHE A CD2 
5246  C CE1 . PHE A 715  ? 0.2985 0.4090 0.2656 0.0702  -0.0103 -0.0976 713  PHE A CE1 
5247  C CE2 . PHE A 715  ? 0.2752 0.3958 0.2346 0.0701  -0.0043 -0.0858 713  PHE A CE2 
5248  C CZ  . PHE A 715  ? 0.3041 0.4266 0.2661 0.0721  -0.0075 -0.0949 713  PHE A CZ  
5249  N N   . THR A 716  ? 0.2429 0.3327 0.2008 0.0584  -0.0011 -0.0596 714  THR A N   
5250  C CA  . THR A 716  ? 0.2378 0.3376 0.1907 0.0589  0.0010  -0.0539 714  THR A CA  
5251  C C   . THR A 716  ? 0.2413 0.3383 0.1928 0.0569  0.0008  -0.0491 714  THR A C   
5252  O O   . THR A 716  ? 0.2496 0.3559 0.1974 0.0580  0.0009  -0.0478 714  THR A O   
5253  C CB  . THR A 716  ? 0.2697 0.3695 0.2219 0.0581  0.0039  -0.0475 714  THR A CB  
5254  O OG1 . THR A 716  ? 0.2589 0.3628 0.2122 0.0603  0.0042  -0.0521 714  THR A OG1 
5255  C CG2 . THR A 716  ? 0.2710 0.3806 0.2188 0.0584  0.0060  -0.0407 714  THR A CG2 
5256  N N   . GLY A 717  ? 0.2332 0.3179 0.1874 0.0540  0.0003  -0.0464 715  GLY A N   
5257  C CA  . GLY A 717  ? 0.2404 0.3220 0.1936 0.0520  0.0002  -0.0419 715  GLY A CA  
5258  C C   . GLY A 717  ? 0.2389 0.3254 0.1911 0.0532  -0.0020 -0.0464 715  GLY A C   
5259  O O   . GLY A 717  ? 0.2429 0.3358 0.1921 0.0535  -0.0017 -0.0431 715  GLY A O   
5260  N N   . GLN A 718  ? 0.2185 0.3022 0.1737 0.0539  -0.0045 -0.0540 716  GLN A N   
5261  C CA  . GLN A 718  ? 0.2233 0.3111 0.1782 0.0548  -0.0069 -0.0587 716  GLN A CA  
5262  C C   . GLN A 718  ? 0.2370 0.3396 0.1876 0.0578  -0.0065 -0.0604 716  GLN A C   
5263  O O   . GLN A 718  ? 0.2394 0.3480 0.1873 0.0582  -0.0069 -0.0590 716  GLN A O   
5264  C CB  . GLN A 718  ? 0.2329 0.3154 0.1926 0.0551  -0.0097 -0.0669 716  GLN A CB  
5265  C CG  . GLN A 718  ? 0.2399 0.3087 0.2042 0.0520  -0.0105 -0.0652 716  GLN A CG  
5266  C CD  . GLN A 718  ? 0.2563 0.3198 0.2260 0.0519  -0.0137 -0.0725 716  GLN A CD  
5267  O OE1 . GLN A 718  ? 0.2531 0.3088 0.2258 0.0495  -0.0152 -0.0719 716  GLN A OE1 
5268  N NE2 . GLN A 718  ? 0.2548 0.3228 0.2263 0.0545  -0.0149 -0.0794 716  GLN A NE2 
5269  N N   . ILE A 719  ? 0.2327 0.3420 0.1826 0.0602  -0.0057 -0.0634 717  ILE A N   
5270  C CA  . ILE A 719  ? 0.2349 0.3597 0.1806 0.0633  -0.0053 -0.0655 717  ILE A CA  
5271  C C   . ILE A 719  ? 0.2441 0.3756 0.1852 0.0627  -0.0029 -0.0566 717  ILE A C   
5272  O O   . ILE A 719  ? 0.2527 0.3948 0.1904 0.0641  -0.0033 -0.0563 717  ILE A O   
5273  C CB  . ILE A 719  ? 0.2703 0.4006 0.2166 0.0658  -0.0047 -0.0704 717  ILE A CB  
5274  C CG1 . ILE A 719  ? 0.2470 0.3722 0.1983 0.0668  -0.0077 -0.0801 717  ILE A CG1 
5275  C CG2 . ILE A 719  ? 0.3632 0.5107 0.3046 0.0688  -0.0035 -0.0708 717  ILE A CG2 
5276  C CD1 . ILE A 719  ? 0.3441 0.4697 0.2976 0.0684  -0.0071 -0.0836 717  ILE A CD1 
5277  N N   . ALA A 720  ? 0.2551 0.3810 0.1965 0.0608  -0.0006 -0.0492 718  ALA A N   
5278  C CA  . ALA A 720  ? 0.2595 0.3916 0.1977 0.0602  0.0015  -0.0404 718  ALA A CA  
5279  C C   . ALA A 720  ? 0.2388 0.3693 0.1762 0.0589  0.0005  -0.0371 718  ALA A C   
5280  O O   . ALA A 720  ? 0.2330 0.3736 0.1672 0.0598  0.0009  -0.0334 718  ALA A O   
5281  C CB  . ALA A 720  ? 0.2612 0.3857 0.2011 0.0581  0.0038  -0.0336 718  ALA A CB  
5282  N N   . ALA A 721  ? 0.2397 0.3579 0.1803 0.0568  -0.0010 -0.0384 719  ALA A N   
5283  C CA  . ALA A 721  ? 0.2152 0.3315 0.1555 0.0556  -0.0021 -0.0358 719  ALA A CA  
5284  C C   . ALA A 721  ? 0.2417 0.3685 0.1796 0.0578  -0.0040 -0.0408 719  ALA A C   
5285  O O   . ALA A 721  ? 0.2461 0.3800 0.1814 0.0581  -0.0039 -0.0367 719  ALA A O   
5286  C CB  . ALA A 721  ? 0.2393 0.3416 0.1838 0.0531  -0.0034 -0.0375 719  ALA A CB  
5287  N N   . ALA A 722  ? 0.2220 0.3500 0.1612 0.0594  -0.0059 -0.0498 720  ALA A N   
5288  C CA  . ALA A 722  ? 0.2338 0.3719 0.1712 0.0616  -0.0079 -0.0555 720  ALA A CA  
5289  C C   . ALA A 722  ? 0.2578 0.4119 0.1901 0.0641  -0.0066 -0.0531 720  ALA A C   
5290  O O   . ALA A 722  ? 0.2452 0.4080 0.1747 0.0649  -0.0073 -0.0517 720  ALA A O   
5291  C CB  . ALA A 722  ? 0.2494 0.3857 0.1899 0.0630  -0.0103 -0.0658 720  ALA A CB  
5292  N N   . LEU A 723  ? 0.2325 0.3913 0.1637 0.0652  -0.0046 -0.0522 721  LEU A N   
5293  C CA  . LEU A 723  ? 0.2469 0.4221 0.1735 0.0675  -0.0031 -0.0496 721  LEU A CA  
5294  C C   . LEU A 723  ? 0.2476 0.4257 0.1720 0.0661  -0.0017 -0.0392 721  LEU A C   
5295  O O   . LEU A 723  ? 0.2480 0.4388 0.1688 0.0675  -0.0019 -0.0373 721  LEU A O   
5296  C CB  . LEU A 723  ? 0.2554 0.4335 0.1819 0.0685  -0.0010 -0.0496 721  LEU A CB  
5297  C CG  . LEU A 723  ? 0.2464 0.4266 0.1746 0.0709  -0.0022 -0.0599 721  LEU A CG  
5298  C CD1 . LEU A 723  ? 0.2817 0.4632 0.2101 0.0713  0.0003  -0.0575 721  LEU A CD1 
5299  C CD2 . LEU A 723  ? 0.2897 0.4859 0.2147 0.0742  -0.0035 -0.0662 721  LEU A CD2 
5300  N N   . VAL A 724  ? 0.2554 0.4220 0.1821 0.0633  -0.0004 -0.0322 722  VAL A N   
5301  C CA  . VAL A 724  ? 0.2439 0.4136 0.1693 0.0621  0.0010  -0.0222 722  VAL A CA  
5302  C C   . VAL A 724  ? 0.2368 0.4065 0.1618 0.0616  -0.0009 -0.0212 722  VAL A C   
5303  O O   . VAL A 724  ? 0.2518 0.4292 0.1748 0.0617  -0.0004 -0.0145 722  VAL A O   
5304  C CB  . VAL A 724  ? 0.2323 0.3907 0.1608 0.0594  0.0028  -0.0153 722  VAL A CB  
5305  C CG1 . VAL A 724  ? 0.2569 0.3996 0.1890 0.0569  0.0016  -0.0158 722  VAL A CG1 
5306  C CG2 . VAL A 724  ? 0.2530 0.4180 0.1803 0.0589  0.0046  -0.0051 722  VAL A CG2 
5307  N N   . ALA A 725  ? 0.2376 0.3990 0.1648 0.0610  -0.0031 -0.0277 723  ALA A N   
5308  C CA  . ALA A 725  ? 0.2602 0.4225 0.1870 0.0609  -0.0051 -0.0283 723  ALA A CA  
5309  C C   . ALA A 725  ? 0.2780 0.4558 0.2011 0.0638  -0.0064 -0.0328 723  ALA A C   
5310  O O   . ALA A 725  ? 0.2867 0.4669 0.2092 0.0639  -0.0083 -0.0337 723  ALA A O   
5311  C CB  . ALA A 725  ? 0.2454 0.3945 0.1761 0.0593  -0.0070 -0.0339 723  ALA A CB  
5312  N N   . GLY A 726  ? 0.2716 0.4604 0.1921 0.0661  -0.0056 -0.0357 724  GLY A N   
5313  C CA  . GLY A 726  ? 0.2638 0.4690 0.1804 0.0690  -0.0067 -0.0399 724  GLY A CA  
5314  C C   . GLY A 726  ? 0.2646 0.4712 0.1821 0.0710  -0.0091 -0.0519 724  GLY A C   
5315  O O   . GLY A 726  ? 0.2820 0.5015 0.1965 0.0733  -0.0106 -0.0563 724  GLY A O   
5316  N N   . ASN A 727  ? 0.2645 0.4586 0.1861 0.0701  -0.0097 -0.0573 725  ASN A N   
5317  C CA  . ASN A 727  ? 0.2556 0.4498 0.1794 0.0717  -0.0124 -0.0688 725  ASN A CA  
5318  C C   . ASN A 727  ? 0.2633 0.4628 0.1871 0.0740  -0.0115 -0.0741 725  ASN A C   
5319  O O   . ASN A 727  ? 0.2694 0.4627 0.1944 0.0730  -0.0094 -0.0704 725  ASN A O   
5320  C CB  . ASN A 727  ? 0.2617 0.4384 0.1910 0.0692  -0.0139 -0.0714 725  ASN A CB  
5321  C CG  . ASN A 727  ? 0.2730 0.4429 0.2030 0.0667  -0.0145 -0.0659 725  ASN A CG  
5322  O OD1 . ASN A 727  ? 0.2772 0.4512 0.2067 0.0672  -0.0166 -0.0688 725  ASN A OD1 
5323  N ND2 . ASN A 727  ? 0.2539 0.4136 0.1852 0.0640  -0.0126 -0.0581 725  ASN A ND2 
5324  N N   . PRO A 728  ? 0.2618 0.4724 0.1846 0.0771  -0.0132 -0.0832 726  PRO A N   
5325  C CA  . PRO A 728  ? 0.2946 0.5078 0.2191 0.0793  -0.0130 -0.0902 726  PRO A CA  
5326  C C   . PRO A 728  ? 0.2623 0.4588 0.1933 0.0778  -0.0148 -0.0954 726  PRO A C   
5327  O O   . PRO A 728  ? 0.2908 0.4781 0.2251 0.0761  -0.0171 -0.0974 726  PRO A O   
5328  C CB  . PRO A 728  ? 0.2539 0.4831 0.1761 0.0831  -0.0150 -0.0992 726  PRO A CB  
5329  C CG  . PRO A 728  ? 0.3064 0.5346 0.2287 0.0822  -0.0175 -0.1003 726  PRO A CG  
5330  C CD  . PRO A 728  ? 0.2770 0.4969 0.1983 0.0788  -0.0159 -0.0886 726  PRO A CD  
5331  N N   . VAL A 729  ? 0.2595 0.4526 0.1927 0.0783  -0.0137 -0.0974 727  VAL A N   
5332  C CA  . VAL A 729  ? 0.2544 0.4312 0.1938 0.0765  -0.0147 -0.0999 727  VAL A CA  
5333  C C   . VAL A 729  ? 0.2463 0.4253 0.1896 0.0793  -0.0166 -0.1108 727  VAL A C   
5334  O O   . VAL A 729  ? 0.2585 0.4490 0.1995 0.0821  -0.0154 -0.1135 727  VAL A O   
5335  C CB  . VAL A 729  ? 0.2496 0.4175 0.1891 0.0740  -0.0116 -0.0909 727  VAL A CB  
5336  C CG1 . VAL A 729  ? 0.2852 0.4388 0.2309 0.0727  -0.0125 -0.0942 727  VAL A CG1 
5337  C CG2 . VAL A 729  ? 0.2744 0.4367 0.2122 0.0709  -0.0106 -0.0814 727  VAL A CG2 
5338  N N   . LEU A 730  ? 0.2707 0.4385 0.2202 0.0783  -0.0196 -0.1169 728  LEU A N   
5339  C CA  . LEU A 730  ? 0.2818 0.4468 0.2371 0.0802  -0.0216 -0.1262 728  LEU A CA  
5340  C C   . LEU A 730  ? 0.2581 0.4070 0.2178 0.0772  -0.0207 -0.1217 728  LEU A C   
5341  O O   . LEU A 730  ? 0.2660 0.4023 0.2289 0.0741  -0.0219 -0.1189 728  LEU A O   
5342  C CB  . LEU A 730  ? 0.2887 0.4521 0.2490 0.0810  -0.0259 -0.1359 728  LEU A CB  
5343  C CG  . LEU A 730  ? 0.2751 0.4539 0.2317 0.0838  -0.0274 -0.1414 728  LEU A CG  
5344  C CD1 . LEU A 730  ? 0.2845 0.4801 0.2364 0.0873  -0.0254 -0.1428 728  LEU A CD1 
5345  C CD2 . LEU A 730  ? 0.2694 0.4492 0.2216 0.0817  -0.0268 -0.1341 728  LEU A CD2 
5346  N N   . ALA A 731  ? 0.2657 0.4156 0.2253 0.0782  -0.0187 -0.1207 729  ALA A N   
5347  C CA  . ALA A 731  ? 0.2923 0.4286 0.2552 0.0756  -0.0174 -0.1156 729  ALA A CA  
5348  C C   . ALA A 731  ? 0.2750 0.4045 0.2455 0.0766  -0.0202 -0.1240 729  ALA A C   
5349  O O   . ALA A 731  ? 0.2967 0.4338 0.2683 0.0799  -0.0204 -0.1303 729  ALA A O   
5350  C CB  . ALA A 731  ? 0.2878 0.4292 0.2462 0.0758  -0.0135 -0.1086 729  ALA A CB  
5351  N N   . LYS A 732  ? 0.2393 0.3546 0.2155 0.0738  -0.0223 -0.1239 730  LYS A N   
5352  C CA  . LYS A 732  ? 0.2805 0.3878 0.2651 0.0743  -0.0252 -0.1309 730  LYS A CA  
5353  C C   . LYS A 732  ? 0.2804 0.3749 0.2676 0.0713  -0.0237 -0.1242 730  LYS A C   
5354  O O   . LYS A 732  ? 0.2679 0.3513 0.2571 0.0678  -0.0243 -0.1195 730  LYS A O   
5355  C CB  . LYS A 732  ? 0.2941 0.3960 0.2842 0.0734  -0.0293 -0.1364 730  LYS A CB  
5356  C CG  . LYS A 732  ? 0.3045 0.4059 0.3024 0.0759  -0.0331 -0.1475 730  LYS A CG  
5357  C CD  . LYS A 732  ? 0.2615 0.3526 0.2657 0.0752  -0.0334 -0.1472 730  LYS A CD  
5358  C CE  . LYS A 732  ? 0.2602 0.3358 0.2691 0.0707  -0.0344 -0.1415 730  LYS A CE  
5359  N NZ  . LYS A 732  ? 0.2834 0.3497 0.2984 0.0701  -0.0348 -0.1409 730  LYS A NZ  
5360  N N   . PRO A 733  ? 0.2550 0.3510 0.2420 0.0726  -0.0218 -0.1234 731  PRO A N   
5361  C CA  . PRO A 733  ? 0.2614 0.3457 0.2509 0.0699  -0.0206 -0.1173 731  PRO A CA  
5362  C C   . PRO A 733  ? 0.2481 0.3216 0.2468 0.0693  -0.0241 -0.1224 731  PRO A C   
5363  O O   . PRO A 733  ? 0.2751 0.3511 0.2787 0.0717  -0.0272 -0.1315 731  PRO A O   
5364  C CB  . PRO A 733  ? 0.2704 0.3621 0.2570 0.0722  -0.0178 -0.1164 731  PRO A CB  
5365  C CG  . PRO A 733  ? 0.2752 0.3793 0.2623 0.0766  -0.0193 -0.1262 731  PRO A CG  
5366  C CD  . PRO A 733  ? 0.2652 0.3745 0.2499 0.0768  -0.0209 -0.1287 731  PRO A CD  
5367  N N   . ALA A 734  ? 0.2367 0.2982 0.2380 0.0660  -0.0236 -0.1162 732  ALA A N   
5368  C CA  . ALA A 734  ? 0.2763 0.3271 0.2865 0.0650  -0.0267 -0.1195 732  ALA A CA  
5369  C C   . ALA A 734  ? 0.2636 0.3182 0.2783 0.0686  -0.0279 -0.1271 732  ALA A C   
5370  O O   . ALA A 734  ? 0.2989 0.3610 0.3097 0.0708  -0.0253 -0.1266 732  ALA A O   
5371  C CB  . ALA A 734  ? 0.2834 0.3231 0.2947 0.0612  -0.0252 -0.1110 732  ALA A CB  
5372  N N   . GLU A 735  ? 0.2790 0.3285 0.3025 0.0692  -0.0321 -0.1341 733  GLU A N   
5373  C CA  . GLU A 735  ? 0.3180 0.3708 0.3470 0.0729  -0.0338 -0.1423 733  GLU A CA  
5374  C C   . GLU A 735  ? 0.2948 0.3433 0.3248 0.0726  -0.0319 -0.1382 733  GLU A C   
5375  O O   . GLU A 735  ? 0.3055 0.3601 0.3368 0.0761  -0.0317 -0.1433 733  GLU A O   
5376  C CB  . GLU A 735  ? 0.3186 0.3651 0.3580 0.0733  -0.0390 -0.1501 733  GLU A CB  
5377  C CG  . GLU A 735  ? 0.3161 0.3478 0.3620 0.0690  -0.0409 -0.1449 733  GLU A CG  
5378  C CD  . GLU A 735  ? 0.3967 0.4249 0.4413 0.0658  -0.0417 -0.1417 733  GLU A CD  
5379  O OE1 . GLU A 735  ? 0.3563 0.3921 0.3927 0.0660  -0.0395 -0.1397 733  GLU A OE1 
5380  O OE2 . GLU A 735  ? 0.3746 0.3928 0.4268 0.0632  -0.0447 -0.1410 733  GLU A OE2 
5381  N N   . GLU A 736  ? 0.2821 0.3209 0.3115 0.0687  -0.0304 -0.1291 734  GLU A N   
5382  C CA  . GLU A 736  ? 0.2675 0.3020 0.2984 0.0683  -0.0288 -0.1253 734  GLU A CA  
5383  C C   . GLU A 736  ? 0.3159 0.3596 0.3385 0.0697  -0.0244 -0.1215 734  GLU A C   
5384  O O   . GLU A 736  ? 0.3152 0.3595 0.3392 0.0710  -0.0233 -0.1215 734  GLU A O   
5385  C CB  . GLU A 736  ? 0.2876 0.3096 0.3203 0.0637  -0.0287 -0.1169 734  GLU A CB  
5386  C CG  . GLU A 736  ? 0.3171 0.3293 0.3589 0.0618  -0.0330 -0.1192 734  GLU A CG  
5387  C CD  . GLU A 736  ? 0.3595 0.3705 0.3995 0.0596  -0.0339 -0.1180 734  GLU A CD  
5388  O OE1 . GLU A 736  ? 0.3231 0.3425 0.3558 0.0605  -0.0320 -0.1180 734  GLU A OE1 
5389  O OE2 . GLU A 736  ? 0.3696 0.3715 0.4157 0.0568  -0.0366 -0.1166 734  GLU A OE2 
5390  N N   . THR A 737  ? 0.2850 0.3359 0.2995 0.0693  -0.0219 -0.1179 735  THR A N   
5391  C CA  . THR A 737  ? 0.2833 0.3414 0.2902 0.0696  -0.0176 -0.1121 735  THR A CA  
5392  C C   . THR A 737  ? 0.3008 0.3734 0.3014 0.0724  -0.0162 -0.1148 735  THR A C   
5393  O O   . THR A 737  ? 0.2765 0.3531 0.2703 0.0710  -0.0136 -0.1085 735  THR A O   
5394  C CB  . THR A 737  ? 0.2702 0.3210 0.2735 0.0654  -0.0153 -0.1018 735  THR A CB  
5395  O OG1 . THR A 737  ? 0.2876 0.3363 0.2892 0.0635  -0.0163 -0.1006 735  THR A OG1 
5396  C CG2 . THR A 737  ? 0.2792 0.3175 0.2880 0.0629  -0.0162 -0.0986 735  THR A CG2 
5397  N N   . PRO A 738  ? 0.2569 0.3381 0.2596 0.0764  -0.0179 -0.1241 736  PRO A N   
5398  C CA  . PRO A 738  ? 0.2679 0.3642 0.2644 0.0791  -0.0167 -0.1268 736  PRO A CA  
5399  C C   . PRO A 738  ? 0.2843 0.3912 0.2748 0.0805  -0.0127 -0.1228 736  PRO A C   
5400  O O   . PRO A 738  ? 0.2830 0.4017 0.2670 0.0816  -0.0109 -0.1215 736  PRO A O   
5401  C CB  . PRO A 738  ? 0.3177 0.4192 0.3197 0.0830  -0.0202 -0.1390 736  PRO A CB  
5402  C CG  . PRO A 738  ? 0.2987 0.3919 0.3083 0.0834  -0.0216 -0.1415 736  PRO A CG  
5403  C CD  . PRO A 738  ? 0.2836 0.3619 0.2949 0.0787  -0.0212 -0.1328 736  PRO A CD  
5404  N N   . LEU A 739  ? 0.2741 0.3779 0.2667 0.0805  -0.0114 -0.1208 737  LEU A N   
5405  C CA  . LEU A 739  ? 0.2654 0.3807 0.2531 0.0823  -0.0079 -0.1182 737  LEU A CA  
5406  C C   . LEU A 739  ? 0.2430 0.3598 0.2238 0.0795  -0.0044 -0.1074 737  LEU A C   
5407  O O   . LEU A 739  ? 0.2738 0.4036 0.2487 0.0809  -0.0022 -0.1055 737  LEU A O   
5408  C CB  . LEU A 739  ? 0.2663 0.3776 0.2587 0.0830  -0.0075 -0.1188 737  LEU A CB  
5409  C CG  . LEU A 739  ? 0.2666 0.3765 0.2667 0.0861  -0.0110 -0.1294 737  LEU A CG  
5410  C CD1 . LEU A 739  ? 0.2559 0.3601 0.2606 0.0861  -0.0105 -0.1283 737  LEU A CD1 
5411  C CD2 . LEU A 739  ? 0.2775 0.4036 0.2760 0.0908  -0.0113 -0.1380 737  LEU A CD2 
5412  N N   . ILE A 740  ? 0.2459 0.3498 0.2273 0.0755  -0.0041 -0.1003 738  ILE A N   
5413  C CA  . ILE A 740  ? 0.2621 0.3669 0.2377 0.0729  -0.0010 -0.0904 738  ILE A CA  
5414  C C   . ILE A 740  ? 0.2522 0.3630 0.2234 0.0729  -0.0014 -0.0900 738  ILE A C   
5415  O O   . ILE A 740  ? 0.2731 0.3918 0.2388 0.0725  0.0011  -0.0840 738  ILE A O   
5416  C CB  . ILE A 740  ? 0.2872 0.3774 0.2650 0.0689  -0.0006 -0.0835 738  ILE A CB  
5417  C CG1 . ILE A 740  ? 0.2789 0.3703 0.2514 0.0664  0.0025  -0.0736 738  ILE A CG1 
5418  C CG2 . ILE A 740  ? 0.2815 0.3607 0.2629 0.0669  -0.0037 -0.0855 738  ILE A CG2 
5419  C CD1 . ILE A 740  ? 0.3007 0.4017 0.2703 0.0677  0.0055  -0.0702 738  ILE A CD1 
5420  N N   . ALA A 741  ? 0.2598 0.3676 0.2338 0.0733  -0.0046 -0.0962 739  ALA A N   
5421  C CA  . ALA A 741  ? 0.2890 0.4035 0.2591 0.0737  -0.0052 -0.0969 739  ALA A CA  
5422  C C   . ALA A 741  ? 0.2703 0.4024 0.2361 0.0773  -0.0040 -0.1002 739  ALA A C   
5423  O O   . ALA A 741  ? 0.2797 0.4202 0.2397 0.0772  -0.0024 -0.0956 739  ALA A O   
5424  C CB  . ALA A 741  ? 0.3194 0.4276 0.2943 0.0737  -0.0091 -0.1040 739  ALA A CB  
5425  N N   . ALA A 742  ? 0.2684 0.4064 0.2369 0.0807  -0.0049 -0.1081 740  ALA A N   
5426  C CA  . ALA A 742  ? 0.2499 0.4059 0.2143 0.0844  -0.0037 -0.1118 740  ALA A CA  
5427  C C   . ALA A 742  ? 0.2675 0.4310 0.2265 0.0837  0.0004  -0.1027 740  ALA A C   
5428  O O   . ALA A 742  ? 0.2906 0.4683 0.2442 0.0851  0.0019  -0.1009 740  ALA A O   
5429  C CB  . ALA A 742  ? 0.2630 0.4234 0.2322 0.0882  -0.0054 -0.1221 740  ALA A CB  
5430  N N   . GLU A 743  ? 0.2534 0.4079 0.2142 0.0815  0.0020  -0.0967 741  GLU A N   
5431  C CA  . GLU A 743  ? 0.3007 0.4613 0.2572 0.0804  0.0057  -0.0876 741  GLU A CA  
5432  C C   . GLU A 743  ? 0.2658 0.4254 0.2179 0.0776  0.0069  -0.0790 741  GLU A C   
5433  O O   . GLU A 743  ? 0.2693 0.4403 0.2167 0.0779  0.0092  -0.0734 741  GLU A O   
5434  C CB  . GLU A 743  ? 0.2658 0.4166 0.2257 0.0788  0.0070  -0.0841 741  GLU A CB  
5435  C CG  . GLU A 743  ? 0.3312 0.4856 0.2879 0.0770  0.0105  -0.0741 741  GLU A CG  
5436  C CD  . GLU A 743  ? 0.2780 0.4500 0.2315 0.0800  0.0127  -0.0745 741  GLU A CD  
5437  O OE1 . GLU A 743  ? 0.2961 0.4782 0.2498 0.0837  0.0116  -0.0832 741  GLU A OE1 
5438  O OE2 . GLU A 743  ? 0.3570 0.5332 0.3078 0.0785  0.0156  -0.0660 741  GLU A OE2 
5439  N N   . GLY A 744  ? 0.2792 0.4259 0.2332 0.0749  0.0051  -0.0777 742  GLY A N   
5440  C CA  . GLY A 744  ? 0.2770 0.4230 0.2273 0.0725  0.0058  -0.0705 742  GLY A CA  
5441  C C   . GLY A 744  ? 0.2646 0.4247 0.2106 0.0748  0.0054  -0.0727 742  GLY A C   
5442  O O   . GLY A 744  ? 0.2777 0.4451 0.2194 0.0740  0.0072  -0.0656 742  GLY A O   
5443  N N   . VAL A 745  ? 0.2691 0.4336 0.2165 0.0775  0.0028  -0.0826 743  VAL A N   
5444  C CA  . VAL A 745  ? 0.2704 0.4496 0.2136 0.0800  0.0023  -0.0858 743  VAL A CA  
5445  C C   . VAL A 745  ? 0.2725 0.4687 0.2114 0.0823  0.0050  -0.0835 743  VAL A C   
5446  O O   . VAL A 745  ? 0.2926 0.5007 0.2266 0.0827  0.0061  -0.0794 743  VAL A O   
5447  C CB  . VAL A 745  ? 0.2841 0.4641 0.2306 0.0826  -0.0012 -0.0978 743  VAL A CB  
5448  C CG1 . VAL A 745  ? 0.3105 0.5089 0.2528 0.0860  -0.0016 -0.1027 743  VAL A CG1 
5449  C CG2 . VAL A 745  ? 0.3245 0.4906 0.2742 0.0800  -0.0039 -0.0985 743  VAL A CG2 
5450  N N   . ARG A 746  ? 0.2835 0.4815 0.2245 0.0837  0.0061  -0.0859 744  ARG A N   
5451  C CA  . ARG A 746  ? 0.2719 0.4863 0.2091 0.0858  0.0089  -0.0835 744  ARG A CA  
5452  C C   . ARG A 746  ? 0.2702 0.4860 0.2041 0.0829  0.0118  -0.0707 744  ARG A C   
5453  O O   . ARG A 746  ? 0.3024 0.5331 0.2316 0.0839  0.0134  -0.0667 744  ARG A O   
5454  C CB  . ARG A 746  ? 0.2989 0.5129 0.2398 0.0874  0.0095  -0.0878 744  ARG A CB  
5455  C CG  . ARG A 746  ? 0.3103 0.5424 0.2479 0.0901  0.0121  -0.0871 744  ARG A CG  
5456  C CD  . ARG A 746  ? 0.3045 0.5339 0.2457 0.0906  0.0134  -0.0879 744  ARG A CD  
5457  N NE  . ARG A 746  ? 0.3277 0.5452 0.2700 0.0867  0.0152  -0.0779 744  ARG A NE  
5458  C CZ  . ARG A 746  ? 0.3390 0.5620 0.2779 0.0848  0.0181  -0.0676 744  ARG A CZ  
5459  N NH1 . ARG A 746  ? 0.3877 0.6284 0.3218 0.0864  0.0197  -0.0651 744  ARG A NH1 
5460  N NH2 . ARG A 746  ? 0.3311 0.5419 0.2718 0.0813  0.0194  -0.0595 744  ARG A NH2 
5461  N N   . ILE A 747  ? 0.2783 0.4784 0.2146 0.0793  0.0123  -0.0643 745  ILE A N   
5462  C CA  . ILE A 747  ? 0.2835 0.4831 0.2177 0.0764  0.0147  -0.0524 745  ILE A CA  
5463  C C   . ILE A 747  ? 0.2707 0.4745 0.2013 0.0756  0.0141  -0.0483 745  ILE A C   
5464  O O   . ILE A 747  ? 0.2710 0.4851 0.1983 0.0752  0.0160  -0.0408 745  ILE A O   
5465  C CB  . ILE A 747  ? 0.2670 0.4488 0.2051 0.0729  0.0150  -0.0478 745  ILE A CB  
5466  C CG1 . ILE A 747  ? 0.2782 0.4591 0.2190 0.0737  0.0163  -0.0493 745  ILE A CG1 
5467  C CG2 . ILE A 747  ? 0.3039 0.4827 0.2406 0.0697  0.0166  -0.0365 745  ILE A CG2 
5468  C CD1 . ILE A 747  ? 0.2778 0.4413 0.2231 0.0709  0.0159  -0.0475 745  ILE A CD1 
5469  N N   . LEU A 748  ? 0.2821 0.4781 0.2138 0.0752  0.0115  -0.0529 746  LEU A N   
5470  C CA  . LEU A 748  ? 0.2795 0.4799 0.2080 0.0747  0.0107  -0.0497 746  LEU A CA  
5471  C C   . LEU A 748  ? 0.3069 0.5275 0.2308 0.0778  0.0111  -0.0518 746  LEU A C   
5472  O O   . LEU A 748  ? 0.2756 0.5050 0.1960 0.0773  0.0122  -0.0445 746  LEU A O   
5473  C CB  . LEU A 748  ? 0.2588 0.4482 0.1896 0.0740  0.0076  -0.0556 746  LEU A CB  
5474  C CG  . LEU A 748  ? 0.3123 0.4841 0.2461 0.0702  0.0075  -0.0501 746  LEU A CG  
5475  C CD1 . LEU A 748  ? 0.3423 0.5033 0.2793 0.0696  0.0044  -0.0570 746  LEU A CD1 
5476  C CD2 . LEU A 748  ? 0.3161 0.4900 0.2473 0.0682  0.0086  -0.0404 746  LEU A CD2 
5477  N N   . ARG A 749  ? 0.2697 0.4983 0.1938 0.0812  0.0102  -0.0616 747  ARG A N   
5478  C CA  . ARG A 749  ? 0.2831 0.5323 0.2028 0.0845  0.0106  -0.0642 747  ARG A CA  
5479  C C   . ARG A 749  ? 0.2902 0.5514 0.2070 0.0844  0.0140  -0.0555 747  ARG A C   
5480  O O   . ARG A 749  ? 0.3247 0.6003 0.2377 0.0850  0.0148  -0.0508 747  ARG A O   
5481  C CB  . ARG A 749  ? 0.3031 0.5578 0.2245 0.0883  0.0088  -0.0773 747  ARG A CB  
5482  C CG  . ARG A 749  ? 0.3475 0.5963 0.2708 0.0890  0.0052  -0.0859 747  ARG A CG  
5483  C CD  . ARG A 749  ? 0.3871 0.6388 0.3155 0.0917  0.0025  -0.0974 747  ARG A CD  
5484  N NE  . ARG A 749  ? 0.3542 0.6026 0.2850 0.0923  -0.0013 -0.1052 747  ARG A NE  
5485  C CZ  . ARG A 749  ? 0.3508 0.6050 0.2859 0.0946  -0.0041 -0.1144 747  ARG A CZ  
5486  N NH1 . ARG A 749  ? 0.3675 0.6315 0.3046 0.0966  -0.0038 -0.1173 747  ARG A NH1 
5487  N NH2 . ARG A 749  ? 0.3577 0.6085 0.2954 0.0948  -0.0075 -0.1210 747  ARG A NH2 
5488  N N   . GLU A 750  ? 0.2726 0.5278 0.1922 0.0834  0.0158  -0.0528 748  GLU A N   
5489  C CA  . GLU A 750  ? 0.3224 0.5878 0.2400 0.0828  0.0190  -0.0437 748  GLU A CA  
5490  C C   . GLU A 750  ? 0.3054 0.5686 0.2216 0.0796  0.0200  -0.0316 748  GLU A C   
5491  O O   . GLU A 750  ? 0.3041 0.5811 0.2175 0.0797  0.0219  -0.0242 748  GLU A O   
5492  C CB  . GLU A 750  ? 0.3051 0.5623 0.2265 0.0820  0.0205  -0.0430 748  GLU A CB  
5493  C CG  . GLU A 750  ? 0.3184 0.5864 0.2385 0.0814  0.0238  -0.0341 748  GLU A CG  
5494  C CD  . GLU A 750  ? 0.3741 0.6331 0.2982 0.0803  0.0251  -0.0330 748  GLU A CD  
5495  O OE1 . GLU A 750  ? 0.4724 0.7226 0.3997 0.0814  0.0237  -0.0415 748  GLU A OE1 
5496  O OE2 . GLU A 750  ? 0.3675 0.6280 0.2919 0.0782  0.0275  -0.0234 748  GLU A OE2 
5497  N N   . ALA A 751  ? 0.2747 0.5213 0.1932 0.0768  0.0186  -0.0295 749  ALA A N   
5498  C CA  . ALA A 751  ? 0.3021 0.5453 0.2202 0.0739  0.0192  -0.0187 749  ALA A CA  
5499  C C   . ALA A 751  ? 0.3017 0.5565 0.2158 0.0749  0.0182  -0.0174 749  ALA A C   
5500  O O   . ALA A 751  ? 0.3327 0.5869 0.2464 0.0728  0.0186  -0.0082 749  ALA A O   
5501  C CB  . ALA A 751  ? 0.2741 0.4964 0.1961 0.0708  0.0179  -0.0177 749  ALA A CB  
5502  N N   . GLY A 752  ? 0.2819 0.5473 0.1935 0.0782  0.0167  -0.0266 750  GLY A N   
5503  C CA  . GLY A 752  ? 0.3081 0.5872 0.2155 0.0796  0.0158  -0.0259 750  GLY A CA  
5504  C C   . GLY A 752  ? 0.2856 0.5595 0.1929 0.0804  0.0127  -0.0342 750  GLY A C   
5505  O O   . GLY A 752  ? 0.3120 0.5969 0.2164 0.0816  0.0116  -0.0343 750  GLY A O   
5506  N N   . ILE A 753  ? 0.3071 0.5647 0.2184 0.0796  0.0110  -0.0407 751  ILE A N   
5507  C CA  . ILE A 753  ? 0.3106 0.5643 0.2224 0.0806  0.0079  -0.0492 751  ILE A CA  
5508  C C   . ILE A 753  ? 0.3040 0.5732 0.2136 0.0847  0.0068  -0.0594 751  ILE A C   
5509  O O   . ILE A 753  ? 0.3108 0.5806 0.2229 0.0863  0.0071  -0.0652 751  ILE A O   
5510  C CB  . ILE A 753  ? 0.2601 0.4937 0.1771 0.0788  0.0063  -0.0539 751  ILE A CB  
5511  C CG1 . ILE A 753  ? 0.2823 0.5009 0.2015 0.0748  0.0073  -0.0444 751  ILE A CG1 
5512  C CG2 . ILE A 753  ? 0.2935 0.5241 0.2114 0.0797  0.0029  -0.0624 751  ILE A CG2 
5513  C CD1 . ILE A 753  ? 0.2763 0.4935 0.1942 0.0731  0.0065  -0.0386 751  ILE A CD1 
5514  N N   . PRO A 754  ? 0.3067 0.5860 0.2152 0.0857  0.0050  -0.0611 752  PRO A N   
5515  C CA  . PRO A 754  ? 0.2945 0.5853 0.2056 0.0885  0.0031  -0.0697 752  PRO A CA  
5516  C C   . PRO A 754  ? 0.3051 0.5862 0.2204 0.0898  0.0005  -0.0818 752  PRO A C   
5517  O O   . PRO A 754  ? 0.2801 0.5472 0.1960 0.0886  -0.0007 -0.0844 752  PRO A O   
5518  C CB  . PRO A 754  ? 0.3626 0.6628 0.2720 0.0888  0.0015  -0.0685 752  PRO A CB  
5519  C CG  . PRO A 754  ? 0.3416 0.6384 0.2475 0.0862  0.0031  -0.0571 752  PRO A CG  
5520  C CD  . PRO A 754  ? 0.3322 0.6123 0.2379 0.0844  0.0043  -0.0553 752  PRO A CD  
5521  N N   . ALA A 755  ? 0.3210 0.6100 0.2396 0.0922  -0.0005 -0.0891 753  ALA A N   
5522  C CA  . ALA A 755  ? 0.2976 0.5787 0.2215 0.0936  -0.0033 -0.1008 753  ALA A CA  
5523  C C   . ALA A 755  ? 0.3081 0.5845 0.2333 0.0936  -0.0066 -0.1066 753  ALA A C   
5524  O O   . ALA A 755  ? 0.3258 0.5892 0.2549 0.0933  -0.0087 -0.1133 753  ALA A O   
5525  C CB  . ALA A 755  ? 0.2935 0.5868 0.2208 0.0964  -0.0041 -0.1074 753  ALA A CB  
5526  N N   . SER A 756  ? 0.3154 0.6022 0.2379 0.0937  -0.0071 -0.1038 754  SER A N   
5527  C CA  . SER A 756  ? 0.3217 0.6051 0.2456 0.0937  -0.0103 -0.1091 754  SER A CA  
5528  C C   . SER A 756  ? 0.3132 0.5811 0.2352 0.0910  -0.0102 -0.1052 754  SER A C   
5529  O O   . SER A 756  ? 0.3376 0.5975 0.2622 0.0906  -0.0131 -0.1110 754  SER A O   
5530  C CB  . SER A 756  ? 0.3639 0.6634 0.2854 0.0946  -0.0107 -0.1067 754  SER A CB  
5531  O OG  . SER A 756  ? 0.3667 0.6701 0.2829 0.0929  -0.0079 -0.0948 754  SER A OG  
5532  N N   . ALA A 757  ? 0.3098 0.5739 0.2278 0.0891  -0.0071 -0.0954 755  ALA A N   
5533  C CA  . ALA A 757  ? 0.2710 0.5210 0.1874 0.0865  -0.0069 -0.0910 755  ALA A CA  
5534  C C   . ALA A 757  ? 0.3024 0.5340 0.2247 0.0846  -0.0072 -0.0930 755  ALA A C   
5535  O O   . ALA A 757  ? 0.2751 0.4917 0.2003 0.0816  -0.0082 -0.0904 755  ALA A O   
5536  C CB  . ALA A 757  ? 0.3133 0.5647 0.2262 0.0842  -0.0039 -0.0774 755  ALA A CB  
5537  N N   . LEU A 758  ? 0.2613 0.4942 0.1855 0.0863  -0.0064 -0.0974 756  LEU A N   
5538  C CA  . LEU A 758  ? 0.2547 0.4708 0.1845 0.0846  -0.0067 -0.0987 756  LEU A CA  
5539  C C   . LEU A 758  ? 0.2860 0.5058 0.2193 0.0878  -0.0083 -0.1102 756  LEU A C   
5540  O O   . LEU A 758  ? 0.3167 0.5465 0.2486 0.0900  -0.0065 -0.1111 756  LEU A O   
5541  C CB  . LEU A 758  ? 0.2786 0.4894 0.2077 0.0823  -0.0033 -0.0886 756  LEU A CB  
5542  C CG  . LEU A 758  ? 0.2632 0.4580 0.1979 0.0806  -0.0034 -0.0896 756  LEU A CG  
5543  C CD1 . LEU A 758  ? 0.2635 0.4425 0.2028 0.0782  -0.0061 -0.0920 756  LEU A CD1 
5544  C CD2 . LEU A 758  ? 0.2906 0.4812 0.2242 0.0782  -0.0001 -0.0790 756  LEU A CD2 
5545  N N   . GLN A 759  ? 0.2669 0.4784 0.2054 0.0880  -0.0117 -0.1187 757  GLN A N   
5546  C CA  . GLN A 759  ? 0.3086 0.5205 0.2527 0.0905  -0.0140 -0.1294 757  GLN A CA  
5547  C C   . GLN A 759  ? 0.3056 0.4995 0.2558 0.0887  -0.0149 -0.1307 757  GLN A C   
5548  O O   . GLN A 759  ? 0.3267 0.5071 0.2797 0.0855  -0.0162 -0.1276 757  GLN A O   
5549  C CB  . GLN A 759  ? 0.3094 0.5256 0.2573 0.0916  -0.0180 -0.1371 757  GLN A CB  
5550  C CG  . GLN A 759  ? 0.3399 0.5739 0.2840 0.0932  -0.0175 -0.1356 757  GLN A CG  
5551  C CD  . GLN A 759  ? 0.3076 0.5455 0.2556 0.0942  -0.0213 -0.1431 757  GLN A CD  
5552  O OE1 . GLN A 759  ? 0.3020 0.5457 0.2553 0.0965  -0.0235 -0.1510 757  GLN A OE1 
5553  N NE2 . GLN A 759  ? 0.2949 0.5296 0.2405 0.0927  -0.0222 -0.1408 757  GLN A NE2 
5554  N N   . LEU A 760  ? 0.3111 0.5049 0.2644 0.0904  -0.0144 -0.1343 758  LEU A N   
5555  C CA  . LEU A 760  ? 0.2997 0.4770 0.2598 0.0886  -0.0155 -0.1352 758  LEU A CA  
5556  C C   . LEU A 760  ? 0.2941 0.4693 0.2615 0.0908  -0.0197 -0.1474 758  LEU A C   
5557  O O   . LEU A 760  ? 0.3002 0.4859 0.2701 0.0932  -0.0209 -0.1525 758  LEU A O   
5558  C CB  . LEU A 760  ? 0.3044 0.4823 0.2643 0.0890  -0.0126 -0.1317 758  LEU A CB  
5559  C CG  . LEU A 760  ? 0.2940 0.4558 0.2612 0.0874  -0.0137 -0.1326 758  LEU A CG  
5560  C CD1 . LEU A 760  ? 0.2819 0.4295 0.2488 0.0827  -0.0124 -0.1224 758  LEU A CD1 
5561  C CD2 . LEU A 760  ? 0.3105 0.4764 0.2789 0.0896  -0.0120 -0.1343 758  LEU A CD2 
5562  N N   . LEU A 761  ? 0.2788 0.4389 0.2523 0.0885  -0.0223 -0.1488 759  LEU A N   
5563  C CA  A LEU A 761  ? 0.3043 0.4601 0.2863 0.0896  -0.0268 -0.1589 759  LEU A CA  
5564  C CA  B LEU A 761  ? 0.3044 0.4601 0.2863 0.0896  -0.0268 -0.1589 759  LEU A CA  
5565  C C   . LEU A 761  ? 0.3148 0.4545 0.3039 0.0880  -0.0279 -0.1591 759  LEU A C   
5566  O O   . LEU A 761  ? 0.2897 0.4161 0.2827 0.0846  -0.0296 -0.1562 759  LEU A O   
5567  C CB  A LEU A 761  ? 0.3024 0.4575 0.2851 0.0886  -0.0296 -0.1612 759  LEU A CB  
5568  C CB  B LEU A 761  ? 0.3025 0.4569 0.2855 0.0885  -0.0297 -0.1613 759  LEU A CB  
5569  C CG  A LEU A 761  ? 0.3094 0.4810 0.2853 0.0900  -0.0284 -0.1597 759  LEU A CG  
5570  C CG  B LEU A 761  ? 0.3041 0.4732 0.2813 0.0896  -0.0294 -0.1607 759  LEU A CG  
5571  C CD1 A LEU A 761  ? 0.2852 0.4557 0.2590 0.0885  -0.0299 -0.1589 759  LEU A CD1 
5572  C CD1 B LEU A 761  ? 0.2855 0.4703 0.2624 0.0927  -0.0288 -0.1638 759  LEU A CD1 
5573  C CD2 A LEU A 761  ? 0.2955 0.4792 0.2755 0.0930  -0.0303 -0.1668 759  LEU A CD2 
5574  C CD2 B LEU A 761  ? 0.2989 0.4699 0.2665 0.0880  -0.0258 -0.1515 759  LEU A CD2 
5575  N N   . PRO A 762  ? 0.2949 0.4352 0.2866 0.0897  -0.0271 -0.1610 760  PRO A N   
5576  C CA  . PRO A 762  ? 0.3081 0.4334 0.3073 0.0880  -0.0284 -0.1606 760  PRO A CA  
5577  C C   . PRO A 762  ? 0.3387 0.4566 0.3477 0.0880  -0.0335 -0.1687 760  PRO A C   
5578  O O   . PRO A 762  ? 0.3277 0.4536 0.3398 0.0895  -0.0360 -0.1746 760  PRO A O   
5579  C CB  . PRO A 762  ? 0.2907 0.4220 0.2905 0.0906  -0.0266 -0.1623 760  PRO A CB  
5580  C CG  . PRO A 762  ? 0.2966 0.4440 0.2874 0.0922  -0.0232 -0.1590 760  PRO A CG  
5581  C CD  . PRO A 762  ? 0.2719 0.4264 0.2605 0.0922  -0.0249 -0.1611 760  PRO A CD  
5582  N N   . GLY A 763  ? 0.3054 0.4079 0.3206 0.0853  -0.0350 -0.1666 761  GLY A N   
5583  C CA  . GLY A 763  ? 0.3529 0.4471 0.3785 0.0848  -0.0399 -0.1731 761  GLY A CA  
5584  C C   . GLY A 763  ? 0.3502 0.4288 0.3793 0.0803  -0.0408 -0.1669 761  GLY A C   
5585  O O   . GLY A 763  ? 0.3003 0.3744 0.3241 0.0772  -0.0376 -0.1568 761  GLY A O   
5586  N N   . ASP A 764  ? 0.3514 0.4220 0.3901 0.0797  -0.0454 -0.1725 762  ASP A N   
5587  C CA  . ASP A 764  ? 0.3626 0.4186 0.4062 0.0751  -0.0467 -0.1663 762  ASP A CA  
5588  C C   . ASP A 764  ? 0.3584 0.4143 0.3993 0.0727  -0.0474 -0.1642 762  ASP A C   
5589  O O   . ASP A 764  ? 0.3225 0.3891 0.3558 0.0742  -0.0458 -0.1648 762  ASP A O   
5590  C CB  . ASP A 764  ? 0.4218 0.4682 0.4780 0.0752  -0.0511 -0.1719 762  ASP A CB  
5591  C CG  . ASP A 764  ? 0.4106 0.4618 0.4741 0.0768  -0.0553 -0.1802 762  ASP A CG  
5592  O OD1 . ASP A 764  ? 0.4281 0.4866 0.4878 0.0772  -0.0557 -0.1824 762  ASP A OD1 
5593  O OD2 . ASP A 764  ? 0.5240 0.5721 0.5975 0.0774  -0.0584 -0.1840 762  ASP A OD2 
5594  N N   . GLY A 765  ? 0.3488 0.3929 0.3961 0.0691  -0.0499 -0.1615 763  GLY A N   
5595  C CA  . GLY A 765  ? 0.3461 0.3893 0.3914 0.0665  -0.0505 -0.1589 763  GLY A CA  
5596  C C   . GLY A 765  ? 0.3394 0.3914 0.3857 0.0692  -0.0534 -0.1683 763  GLY A C   
5597  O O   . GLY A 765  ? 0.3649 0.4208 0.4063 0.0681  -0.0529 -0.1663 763  GLY A O   
5598  N N   . ARG A 766  ? 0.3559 0.4114 0.4088 0.0727  -0.0566 -0.1786 764  ARG A N   
5599  C CA  . ARG A 766  ? 0.3575 0.4232 0.4120 0.0746  -0.0588 -0.1850 764  ARG A CA  
5600  C C   . ARG A 766  ? 0.3494 0.4296 0.3922 0.0770  -0.0554 -0.1845 764  ARG A C   
5601  O O   . ARG A 766  ? 0.3603 0.4476 0.4008 0.0774  -0.0564 -0.1866 764  ARG A O   
5602  C CB  . ARG A 766  ? 0.4323 0.5011 0.4961 0.0771  -0.0616 -0.1916 764  ARG A CB  
5603  C CG  . ARG A 766  ? 0.5186 0.5748 0.5953 0.0751  -0.0655 -0.1926 764  ARG A CG  
5604  C CD  . ARG A 766  ? 0.4557 0.5167 0.5402 0.0781  -0.0679 -0.1992 764  ARG A CD  
5605  N NE  . ARG A 766  ? 0.4773 0.5410 0.5580 0.0800  -0.0649 -0.1977 764  ARG A NE  
5606  C CZ  . ARG A 766  ? 0.5370 0.6107 0.6191 0.0835  -0.0650 -0.2030 764  ARG A CZ  
5607  N NH1 . ARG A 766  ? 0.5523 0.6350 0.6388 0.0858  -0.0678 -0.2103 764  ARG A NH1 
5608  N NH2 . ARG A 766  ? 0.5332 0.6080 0.6122 0.0848  -0.0623 -0.2010 764  ARG A NH2 
5609  N N   . VAL A 767  ? 0.3219 0.4072 0.3579 0.0787  -0.0516 -0.1815 765  VAL A N   
5610  C CA  . VAL A 767  ? 0.3696 0.4690 0.3946 0.0807  -0.0482 -0.1798 765  VAL A CA  
5611  C C   . VAL A 767  ? 0.3257 0.4229 0.3432 0.0779  -0.0461 -0.1723 765  VAL A C   
5612  O O   . VAL A 767  ? 0.3243 0.4313 0.3360 0.0788  -0.0456 -0.1728 765  VAL A O   
5613  C CB  . VAL A 767  ? 0.3100 0.4151 0.3303 0.0828  -0.0446 -0.1776 765  VAL A CB  
5614  C CG1 . VAL A 767  ? 0.3273 0.4478 0.3370 0.0847  -0.0412 -0.1751 765  VAL A CG1 
5615  C CG2 . VAL A 767  ? 0.3467 0.4534 0.3757 0.0850  -0.0469 -0.1838 765  VAL A CG2 
5616  N N   . GLY A 768  ? 0.3196 0.4043 0.3382 0.0739  -0.0447 -0.1633 766  GLY A N   
5617  C CA  . GLY A 768  ? 0.3033 0.3847 0.3169 0.0704  -0.0429 -0.1546 766  GLY A CA  
5618  C C   . GLY A 768  ? 0.2957 0.3770 0.3123 0.0696  -0.0463 -0.1586 766  GLY A C   
5619  O O   . GLY A 768  ? 0.3078 0.3957 0.3182 0.0693  -0.0452 -0.1560 766  GLY A O   
5620  N N   . ALA A 769  ? 0.3252 0.3991 0.3519 0.0691  -0.0506 -0.1649 767  ALA A N   
5621  C CA  . ALA A 769  ? 0.3579 0.4309 0.3886 0.0680  -0.0541 -0.1688 767  ALA A CA  
5622  C C   . ALA A 769  ? 0.3246 0.4122 0.3515 0.0718  -0.0552 -0.1768 767  ALA A C   
5623  O O   . ALA A 769  ? 0.3381 0.4297 0.3621 0.0710  -0.0558 -0.1762 767  ALA A O   
5624  C CB  . ALA A 769  ? 0.3443 0.4067 0.3876 0.0669  -0.0588 -0.1742 767  ALA A CB  
5625  N N   . ALA A 770  ? 0.3200 0.4165 0.3475 0.0756  -0.0552 -0.1827 768  ALA A N   
5626  C CA  . ALA A 770  ? 0.3153 0.4268 0.3404 0.0784  -0.0557 -0.1872 768  ALA A CA  
5627  C C   . ALA A 770  ? 0.3207 0.4421 0.3335 0.0790  -0.0521 -0.1820 768  ALA A C   
5628  O O   . ALA A 770  ? 0.3302 0.4610 0.3404 0.0798  -0.0528 -0.1836 768  ALA A O   
5629  C CB  . ALA A 770  ? 0.3516 0.4708 0.3800 0.0818  -0.0558 -0.1921 768  ALA A CB  
5630  N N   . LEU A 771  ? 0.3234 0.4430 0.3289 0.0784  -0.0482 -0.1753 769  LEU A N   
5631  C CA  . LEU A 771  ? 0.3040 0.4319 0.2991 0.0781  -0.0445 -0.1675 769  LEU A CA  
5632  C C   . LEU A 771  ? 0.3299 0.4520 0.3243 0.0745  -0.0449 -0.1617 769  LEU A C   
5633  O O   . LEU A 771  ? 0.3397 0.4710 0.3281 0.0751  -0.0443 -0.1602 769  LEU A O   
5634  C CB  . LEU A 771  ? 0.3026 0.4285 0.2930 0.0773  -0.0400 -0.1586 769  LEU A CB  
5635  C CG  . LEU A 771  ? 0.2919 0.4261 0.2813 0.0809  -0.0388 -0.1631 769  LEU A CG  
5636  C CD1 . LEU A 771  ? 0.3139 0.4429 0.3004 0.0794  -0.0348 -0.1540 769  LEU A CD1 
5637  C CD2 . LEU A 771  ? 0.3086 0.4611 0.2917 0.0843  -0.0379 -0.1658 769  LEU A CD2 
5638  N N   . VAL A 772  ? 0.3254 0.4326 0.3257 0.0708  -0.0458 -0.1579 770  VAL A N   
5639  C CA  . VAL A 772  ? 0.3121 0.4134 0.3122 0.0673  -0.0463 -0.1525 770  VAL A CA  
5640  C C   . VAL A 772  ? 0.3453 0.4524 0.3478 0.0684  -0.0500 -0.1602 770  VAL A C   
5641  O O   . VAL A 772  ? 0.3754 0.4868 0.3735 0.0676  -0.0496 -0.1570 770  VAL A O   
5642  C CB  . VAL A 772  ? 0.3029 0.3880 0.3097 0.0633  -0.0469 -0.1480 770  VAL A CB  
5643  C CG1 . VAL A 772  ? 0.3306 0.4103 0.3390 0.0600  -0.0482 -0.1447 770  VAL A CG1 
5644  C CG2 . VAL A 772  ? 0.3161 0.3963 0.3188 0.0618  -0.0427 -0.1388 770  VAL A CG2 
5645  N N   . ALA A 773  ? 0.3529 0.4604 0.3628 0.0705  -0.0538 -0.1706 771  ALA A N   
5646  C CA  . ALA A 773  ? 0.3231 0.4354 0.3368 0.0714  -0.0579 -0.1789 771  ALA A CA  
5647  C C   . ALA A 773  ? 0.3934 0.5227 0.4011 0.0749  -0.0571 -0.1817 771  ALA A C   
5648  O O   . ALA A 773  ? 0.4363 0.5706 0.4462 0.0751  -0.0596 -0.1853 771  ALA A O   
5649  C CB  . ALA A 773  ? 0.3790 0.4852 0.4049 0.0718  -0.0620 -0.1864 771  ALA A CB  
5650  N N   . ALA A 774  ? 0.3878 0.5262 0.3885 0.0773  -0.0537 -0.1794 772  ALA A N   
5651  C CA  . ALA A 774  ? 0.3845 0.5398 0.3806 0.0803  -0.0529 -0.1810 772  ALA A CA  
5652  C C   . ALA A 774  ? 0.3738 0.5349 0.3632 0.0795  -0.0524 -0.1772 772  ALA A C   
5653  O O   . ALA A 774  ? 0.3665 0.5223 0.3504 0.0772  -0.0506 -0.1706 772  ALA A O   
5654  C CB  . ALA A 774  ? 0.3850 0.5486 0.3748 0.0825  -0.0490 -0.1778 772  ALA A CB  
5655  N N   . ALA A 775  ? 0.4495 0.6221 0.4399 0.0813  -0.0540 -0.1815 773  ALA A N   
5656  C CA  . ALA A 775  ? 0.4362 0.6133 0.4223 0.0804  -0.0545 -0.1790 773  ALA A CA  
5657  C C   . ALA A 775  ? 0.3527 0.5359 0.3276 0.0802  -0.0506 -0.1700 773  ALA A C   
5658  O O   . ALA A 775  ? 0.3727 0.5532 0.3440 0.0782  -0.0505 -0.1654 773  ALA A O   
5659  C CB  . ALA A 775  ? 0.4402 0.6298 0.4294 0.0829  -0.0567 -0.1854 773  ALA A CB  
5660  N N   . GLU A 776  ? 0.3385 0.5300 0.3084 0.0822  -0.0474 -0.1670 774  GLU A N   
5661  C CA  . GLU A 776  ? 0.3154 0.5142 0.2753 0.0822  -0.0438 -0.1581 774  GLU A CA  
5662  C C   . GLU A 776  ? 0.3321 0.5195 0.2889 0.0797  -0.0410 -0.1501 774  GLU A C   
5663  O O   . GLU A 776  ? 0.3331 0.5243 0.2835 0.0790  -0.0378 -0.1407 774  GLU A O   
5664  C CB  . GLU A 776  ? 0.3303 0.5447 0.2867 0.0853  -0.0416 -0.1576 774  GLU A CB  
5665  C CG  . GLU A 776  ? 0.3667 0.5936 0.3268 0.0877  -0.0439 -0.1645 774  GLU A CG  
5666  C CD  . GLU A 776  ? 0.4724 0.6977 0.4414 0.0894  -0.0464 -0.1740 774  GLU A CD  
5667  O OE1 . GLU A 776  ? 0.4023 0.6150 0.3758 0.0883  -0.0469 -0.1756 774  GLU A OE1 
5668  O OE2 . GLU A 776  ? 0.5320 0.7690 0.5038 0.0920  -0.0479 -0.1798 774  GLU A OE2 
5669  N N   . THR A 777  ? 0.3090 0.4813 0.2727 0.0776  -0.0419 -0.1511 775  THR A N   
5670  C CA  . THR A 777  ? 0.2960 0.4561 0.2596 0.0744  -0.0389 -0.1412 775  THR A CA  
5671  C C   . THR A 777  ? 0.3021 0.4574 0.2636 0.0713  -0.0382 -0.1329 775  THR A C   
5672  O O   . THR A 777  ? 0.3366 0.4867 0.3023 0.0697  -0.0410 -0.1355 775  THR A O   
5673  C CB  . THR A 777  ? 0.2955 0.4411 0.2674 0.0727  -0.0406 -0.1445 775  THR A CB  
5674  O OG1 . THR A 777  ? 0.3026 0.4526 0.2761 0.0757  -0.0407 -0.1510 775  THR A OG1 
5675  C CG2 . THR A 777  ? 0.2776 0.4102 0.2497 0.0690  -0.0379 -0.1343 775  THR A CG2 
5676  N N   . ALA A 778  ? 0.2708 0.4281 0.2263 0.0705  -0.0346 -0.1231 776  ALA A N   
5677  C CA  . ALA A 778  ? 0.2752 0.4298 0.2284 0.0680  -0.0338 -0.1152 776  ALA A CA  
5678  C C   . ALA A 778  ? 0.2676 0.4075 0.2229 0.0644  -0.0319 -0.1072 776  ALA A C   
5679  O O   . ALA A 778  ? 0.2814 0.4175 0.2361 0.0622  -0.0315 -0.1013 776  ALA A O   
5680  C CB  . ALA A 778  ? 0.2929 0.4612 0.2384 0.0697  -0.0315 -0.1094 776  ALA A CB  
5681  N N   . GLY A 779  ? 0.2593 0.3916 0.2172 0.0638  -0.0308 -0.1071 777  GLY A N   
5682  C CA  . GLY A 779  ? 0.2446 0.3631 0.2051 0.0604  -0.0293 -0.1005 777  GLY A CA  
5683  C C   . GLY A 779  ? 0.2536 0.3658 0.2177 0.0605  -0.0289 -0.1031 777  GLY A C   
5684  O O   . GLY A 779  ? 0.2590 0.3785 0.2222 0.0633  -0.0288 -0.1078 777  GLY A O   
5685  N N   . VAL A 780  ? 0.2596 0.3585 0.2280 0.0574  -0.0288 -0.0999 778  VAL A N   
5686  C CA  . VAL A 780  ? 0.2547 0.3461 0.2274 0.0571  -0.0288 -0.1018 778  VAL A CA  
5687  C C   . VAL A 780  ? 0.2491 0.3316 0.2210 0.0544  -0.0259 -0.0930 778  VAL A C   
5688  O O   . VAL A 780  ? 0.2481 0.3241 0.2207 0.0516  -0.0257 -0.0881 778  VAL A O   
5689  C CB  . VAL A 780  ? 0.2492 0.3329 0.2300 0.0562  -0.0325 -0.1087 778  VAL A CB  
5690  C CG1 . VAL A 780  ? 0.2554 0.3312 0.2408 0.0558  -0.0324 -0.1099 778  VAL A CG1 
5691  C CG2 . VAL A 780  ? 0.2593 0.3521 0.2413 0.0591  -0.0356 -0.1182 778  VAL A CG2 
5692  N N   . MET A 781  ? 0.2410 0.3240 0.2114 0.0553  -0.0236 -0.0911 779  MET A N   
5693  C CA  . MET A 781  ? 0.2186 0.2927 0.1891 0.0528  -0.0212 -0.0838 779  MET A CA  
5694  C C   . MET A 781  ? 0.2512 0.3179 0.2272 0.0525  -0.0222 -0.0875 779  MET A C   
5695  O O   . MET A 781  ? 0.2465 0.3180 0.2227 0.0551  -0.0222 -0.0920 779  MET A O   
5696  C CB  . MET A 781  ? 0.2658 0.3465 0.2304 0.0539  -0.0177 -0.0779 779  MET A CB  
5697  C CG  . MET A 781  ? 0.2503 0.3398 0.2099 0.0546  -0.0170 -0.0745 779  MET A CG  
5698  S SD  . MET A 781  ? 0.2546 0.3531 0.2082 0.0560  -0.0134 -0.0679 779  MET A SD  
5699  C CE  . MET A 781  ? 0.2581 0.3445 0.2129 0.0525  -0.0110 -0.0591 779  MET A CE  
5700  N N   . PHE A 782  ? 0.2466 0.3020 0.2273 0.0495  -0.0232 -0.0857 780  PHE A N   
5701  C CA  . PHE A 782  ? 0.2588 0.3062 0.2458 0.0488  -0.0247 -0.0887 780  PHE A CA  
5702  C C   . PHE A 782  ? 0.2553 0.2938 0.2427 0.0459  -0.0225 -0.0814 780  PHE A C   
5703  O O   . PHE A 782  ? 0.2408 0.2748 0.2277 0.0433  -0.0219 -0.0763 780  PHE A O   
5704  C CB  . PHE A 782  ? 0.2440 0.2860 0.2376 0.0475  -0.0284 -0.0935 780  PHE A CB  
5705  C CG  . PHE A 782  ? 0.2588 0.2919 0.2597 0.0463  -0.0301 -0.0955 780  PHE A CG  
5706  C CD1 . PHE A 782  ? 0.2632 0.2982 0.2676 0.0489  -0.0318 -0.1023 780  PHE A CD1 
5707  C CD2 . PHE A 782  ? 0.2481 0.2712 0.2523 0.0427  -0.0300 -0.0902 780  PHE A CD2 
5708  C CE1 . PHE A 782  ? 0.2685 0.2952 0.2800 0.0480  -0.0335 -0.1038 780  PHE A CE1 
5709  C CE2 . PHE A 782  ? 0.2532 0.2685 0.2641 0.0416  -0.0316 -0.0914 780  PHE A CE2 
5710  C CZ  . PHE A 782  ? 0.2467 0.2635 0.2614 0.0442  -0.0334 -0.0981 780  PHE A CZ  
5711  N N   . THR A 783  ? 0.2213 0.2576 0.2099 0.0466  -0.0216 -0.0814 781  THR A N   
5712  C CA  . THR A 783  ? 0.2458 0.2728 0.2364 0.0439  -0.0203 -0.0761 781  THR A CA  
5713  C C   . THR A 783  ? 0.2457 0.2673 0.2430 0.0441  -0.0226 -0.0807 781  THR A C   
5714  O O   . THR A 783  ? 0.2464 0.2727 0.2446 0.0470  -0.0232 -0.0859 781  THR A O   
5715  C CB  . THR A 783  ? 0.2756 0.3051 0.2611 0.0442  -0.0167 -0.0703 781  THR A CB  
5716  O OG1 . THR A 783  ? 0.2550 0.2899 0.2350 0.0442  -0.0150 -0.0662 781  THR A OG1 
5717  C CG2 . THR A 783  ? 0.2346 0.2549 0.2220 0.0414  -0.0155 -0.0648 781  THR A CG2 
5718  N N   . GLY A 784  ? 0.2477 0.2601 0.2502 0.0412  -0.0240 -0.0788 782  GLY A N   
5719  C CA  . GLY A 784  ? 0.2540 0.2609 0.2641 0.0411  -0.0268 -0.0830 782  GLY A CA  
5720  C C   . GLY A 784  ? 0.2280 0.2261 0.2434 0.0374  -0.0286 -0.0803 782  GLY A C   
5721  O O   . GLY A 784  ? 0.2528 0.2488 0.2655 0.0349  -0.0270 -0.0744 782  GLY A O   
5722  N N   . SER A 785  ? 0.2545 0.2481 0.2779 0.0372  -0.0320 -0.0846 783  SER A N   
5723  C CA  . SER A 785  ? 0.2639 0.2494 0.2933 0.0335  -0.0339 -0.0816 783  SER A CA  
5724  C C   . SER A 785  ? 0.2769 0.2636 0.3065 0.0321  -0.0353 -0.0821 783  SER A C   
5725  O O   . SER A 785  ? 0.2724 0.2653 0.3004 0.0343  -0.0363 -0.0871 783  SER A O   
5726  C CB  . SER A 785  ? 0.2878 0.2679 0.3266 0.0336  -0.0374 -0.0858 783  SER A CB  
5727  O OG  . SER A 785  ? 0.2994 0.2832 0.3417 0.0361  -0.0405 -0.0940 783  SER A OG  
5728  N N   . THR A 786  ? 0.2540 0.2353 0.2856 0.0284  -0.0353 -0.0767 784  THR A N   
5729  C CA  . THR A 786  ? 0.2711 0.2530 0.3037 0.0267  -0.0367 -0.0767 784  THR A CA  
5730  C C   . THR A 786  ? 0.2608 0.2426 0.3008 0.0275  -0.0411 -0.0839 784  THR A C   
5731  O O   . THR A 786  ? 0.2719 0.2580 0.3110 0.0282  -0.0422 -0.0872 784  THR A O   
5732  C CB  . THR A 786  ? 0.3056 0.2818 0.3402 0.0226  -0.0362 -0.0698 784  THR A CB  
5733  O OG1 . THR A 786  ? 0.3035 0.2804 0.3314 0.0222  -0.0323 -0.0640 784  THR A OG1 
5734  C CG2 . THR A 786  ? 0.3129 0.2903 0.3484 0.0208  -0.0374 -0.0695 784  THR A CG2 
5735  N N   . GLU A 787  ? 0.3262 0.3031 0.3739 0.0275  -0.0436 -0.0866 785  GLU A N   
5736  C CA  . GLU A 787  ? 0.3176 0.2936 0.3737 0.0282  -0.0481 -0.0936 785  GLU A CA  
5737  C C   . GLU A 787  ? 0.2846 0.2685 0.3378 0.0324  -0.0487 -0.1017 785  GLU A C   
5738  O O   . GLU A 787  ? 0.2955 0.2821 0.3518 0.0329  -0.0515 -0.1069 785  GLU A O   
5739  C CB  . GLU A 787  ? 0.3427 0.3115 0.4080 0.0275  -0.0508 -0.0946 785  GLU A CB  
5740  N N   . VAL A 788  ? 0.2851 0.2736 0.3324 0.0354  -0.0462 -0.1026 786  VAL A N   
5741  C CA  . VAL A 788  ? 0.2656 0.2632 0.3096 0.0395  -0.0465 -0.1099 786  VAL A CA  
5742  C C   . VAL A 788  ? 0.2730 0.2775 0.3096 0.0396  -0.0449 -0.1085 786  VAL A C   
5743  O O   . VAL A 788  ? 0.2824 0.2928 0.3193 0.0414  -0.0469 -0.1147 786  VAL A O   
5744  C CB  . VAL A 788  ? 0.2874 0.2888 0.3275 0.0426  -0.0442 -0.1111 786  VAL A CB  
5745  C CG1 . VAL A 788  ? 0.2919 0.3046 0.3268 0.0466  -0.0438 -0.1173 786  VAL A CG1 
5746  C CG2 . VAL A 788  ? 0.3201 0.3157 0.3690 0.0431  -0.0468 -0.1147 786  VAL A CG2 
5747  N N   . ALA A 789  ? 0.2685 0.2724 0.2987 0.0376  -0.0414 -0.1005 787  ALA A N   
5748  C CA  . ALA A 789  ? 0.2682 0.2779 0.2922 0.0376  -0.0400 -0.0986 787  ALA A CA  
5749  C C   . ALA A 789  ? 0.2548 0.2634 0.2839 0.0360  -0.0434 -0.1015 787  ALA A C   
5750  O O   . ALA A 789  ? 0.2538 0.2692 0.2799 0.0374  -0.0439 -0.1045 787  ALA A O   
5751  C CB  . ALA A 789  ? 0.2432 0.2506 0.2616 0.0352  -0.0364 -0.0895 787  ALA A CB  
5752  N N   . ARG A 790  ? 0.2550 0.2553 0.2921 0.0330  -0.0457 -0.1003 788  ARG A N   
5753  C CA  . ARG A 790  ? 0.2645 0.2632 0.3073 0.0311  -0.0490 -0.1026 788  ARG A CA  
5754  C C   . ARG A 790  ? 0.2498 0.2530 0.2969 0.0340  -0.0526 -0.1124 788  ARG A C   
5755  O O   . ARG A 790  ? 0.2836 0.2904 0.3313 0.0339  -0.0545 -0.1155 788  ARG A O   
5756  C CB  . ARG A 790  ? 0.3178 0.3070 0.3687 0.0273  -0.0506 -0.0987 788  ARG A CB  
5757  C CG  . ARG A 790  ? 0.2868 0.2738 0.3441 0.0246  -0.0538 -0.0996 788  ARG A CG  
5758  C CD  . ARG A 790  ? 0.3138 0.2924 0.3779 0.0204  -0.0546 -0.0936 788  ARG A CD  
5759  N NE  . ARG A 790  ? 0.3012 0.2787 0.3591 0.0182  -0.0508 -0.0851 788  ARG A NE  
5760  C CZ  . ARG A 790  ? 0.2989 0.2719 0.3567 0.0168  -0.0489 -0.0797 788  ARG A CZ  
5761  N NH1 . ARG A 790  ? 0.3441 0.3127 0.4074 0.0172  -0.0505 -0.0813 788  ARG A NH1 
5762  N NH2 . ARG A 790  ? 0.3192 0.2922 0.3714 0.0149  -0.0456 -0.0727 788  ARG A NH2 
5763  N N   . LEU A 791  ? 0.2832 0.2865 0.3332 0.0365  -0.0537 -0.1176 789  LEU A N   
5764  C CA  . LEU A 791  ? 0.2976 0.3064 0.3512 0.0398  -0.0570 -0.1277 789  LEU A CA  
5765  C C   . LEU A 791  ? 0.2893 0.3096 0.3338 0.0429  -0.0552 -0.1303 789  LEU A C   
5766  O O   . LEU A 791  ? 0.3039 0.3297 0.3499 0.0444  -0.0578 -0.1367 789  LEU A O   
5767  C CB  . LEU A 791  ? 0.3022 0.3092 0.3600 0.0422  -0.0580 -0.1323 789  LEU A CB  
5768  C CG  . LEU A 791  ? 0.3575 0.3537 0.4258 0.0397  -0.0605 -0.1309 789  LEU A CG  
5769  C CD1 . LEU A 791  ? 0.3826 0.3779 0.4538 0.0424  -0.0608 -0.1347 789  LEU A CD1 
5770  C CD2 . LEU A 791  ? 0.3707 0.3634 0.4491 0.0382  -0.0655 -0.1356 789  LEU A CD2 
5771  N N   . ILE A 792  ? 0.2765 0.3008 0.3118 0.0439  -0.0509 -0.1252 790  ILE A N   
5772  C CA  . ILE A 792  ? 0.2703 0.3058 0.2969 0.0466  -0.0490 -0.1263 790  ILE A CA  
5773  C C   . ILE A 792  ? 0.2904 0.3276 0.3149 0.0447  -0.0492 -0.1235 790  ILE A C   
5774  O O   . ILE A 792  ? 0.3045 0.3501 0.3266 0.0466  -0.0504 -0.1281 790  ILE A O   
5775  C CB  . ILE A 792  ? 0.2793 0.3181 0.2977 0.0477  -0.0444 -0.1206 790  ILE A CB  
5776  C CG1 . ILE A 792  ? 0.2949 0.3349 0.3152 0.0505  -0.0446 -0.1252 790  ILE A CG1 
5777  C CG2 . ILE A 792  ? 0.2970 0.3467 0.3064 0.0496  -0.0423 -0.1193 790  ILE A CG2 
5778  C CD1 . ILE A 792  ? 0.2852 0.3258 0.2994 0.0509  -0.0404 -0.1191 790  ILE A CD1 
5779  N N   . GLN A 793  ? 0.2687 0.2984 0.2940 0.0409  -0.0481 -0.1160 791  GLN A N   
5780  C CA  . GLN A 793  ? 0.2752 0.3057 0.2993 0.0388  -0.0484 -0.1133 791  GLN A CA  
5781  C C   . GLN A 793  ? 0.2737 0.3054 0.3046 0.0389  -0.0529 -0.1207 791  GLN A C   
5782  O O   . GLN A 793  ? 0.2913 0.3295 0.3195 0.0397  -0.0536 -0.1226 791  GLN A O   
5783  C CB  . GLN A 793  ? 0.2743 0.2959 0.3003 0.0347  -0.0471 -0.1052 791  GLN A CB  
5784  C CG  . GLN A 793  ? 0.3069 0.3285 0.3327 0.0322  -0.0475 -0.1021 791  GLN A CG  
5785  C CD  . GLN A 793  ? 0.3196 0.3323 0.3495 0.0280  -0.0470 -0.0957 791  GLN A CD  
5786  O OE1 . GLN A 793  ? 0.3456 0.3513 0.3819 0.0265  -0.0485 -0.0958 791  GLN A OE1 
5787  N NE2 . GLN A 793  ? 0.3500 0.3632 0.3762 0.0262  -0.0451 -0.0899 791  GLN A NE2 
5788  N N   . ALA A 794  ? 0.2916 0.3171 0.3316 0.0383  -0.0562 -0.1252 792  ALA A N   
5789  C CA  . ALA A 794  ? 0.3546 0.3807 0.4024 0.0384  -0.0608 -0.1326 792  ALA A CA  
5790  C C   . ALA A 794  ? 0.3118 0.3487 0.3567 0.0427  -0.0621 -0.1413 792  ALA A C   
5791  O O   . ALA A 794  ? 0.3615 0.4034 0.4071 0.0432  -0.0644 -0.1455 792  ALA A O   
5792  C CB  . ALA A 794  ? 0.3382 0.3552 0.3972 0.0369  -0.0641 -0.1352 792  ALA A CB  
5793  N N   . GLN A 795  ? 0.3203 0.3615 0.3619 0.0460  -0.0607 -0.1441 793  GLN A N   
5794  C CA  . GLN A 795  ? 0.3147 0.3677 0.3524 0.0504  -0.0614 -0.1519 793  GLN A CA  
5795  C C   . GLN A 795  ? 0.3397 0.4019 0.3688 0.0510  -0.0595 -0.1493 793  GLN A C   
5796  O O   . GLN A 795  ? 0.3730 0.4431 0.4022 0.0529  -0.0619 -0.1558 793  GLN A O   
5797  C CB  . GLN A 795  ? 0.3612 0.4178 0.3946 0.0534  -0.0588 -0.1525 793  GLN A CB  
5798  C CG  . GLN A 795  ? 0.4556 0.5118 0.4963 0.0560  -0.0617 -0.1615 793  GLN A CG  
5799  C CD  . GLN A 795  ? 0.4419 0.5030 0.4772 0.0590  -0.0586 -0.1613 793  GLN A CD  
5800  O OE1 . GLN A 795  ? 0.4761 0.5328 0.5076 0.0575  -0.0551 -0.1533 793  GLN A OE1 
5801  N NE2 . GLN A 795  ? 0.3794 0.4503 0.4144 0.0632  -0.0599 -0.1703 793  GLN A NE2 
5802  N N   . LEU A 796  ? 0.3213 0.3826 0.3431 0.0495  -0.0554 -0.1398 794  LEU A N   
5803  C CA  . LEU A 796  ? 0.3234 0.3934 0.3369 0.0502  -0.0534 -0.1365 794  LEU A CA  
5804  C C   . LEU A 796  ? 0.3249 0.3933 0.3409 0.0477  -0.0553 -0.1354 794  LEU A C   
5805  O O   . LEU A 796  ? 0.3727 0.4494 0.3833 0.0487  -0.0548 -0.1348 794  LEU A O   
5806  C CB  . LEU A 796  ? 0.3042 0.3734 0.3103 0.0494  -0.0486 -0.1268 794  LEU A CB  
5807  C CG  . LEU A 796  ? 0.2972 0.3703 0.2991 0.0521  -0.0461 -0.1267 794  LEU A CG  
5808  C CD1 . LEU A 796  ? 0.3291 0.4002 0.3246 0.0508  -0.0417 -0.1167 794  LEU A CD1 
5809  C CD2 . LEU A 796  ? 0.3137 0.4007 0.3112 0.0562  -0.0466 -0.1331 794  LEU A CD2 
5810  N N   . ALA A 797  ? 0.3472 0.4055 0.3714 0.0444  -0.0575 -0.1348 795  ALA A N   
5811  C CA  . ALA A 797  ? 0.3554 0.4125 0.3824 0.0419  -0.0594 -0.1339 795  ALA A CA  
5812  C C   . ALA A 797  ? 0.4079 0.4730 0.4371 0.0441  -0.0631 -0.1429 795  ALA A C   
5813  O O   . ALA A 797  ? 0.5441 0.6121 0.5729 0.0431  -0.0641 -0.1424 795  ALA A O   
5814  C CB  . ALA A 797  ? 0.3602 0.4053 0.3959 0.0378  -0.0609 -0.1311 795  ALA A CB  
5815  N N   . ASP A 798  ? 0.4245 0.4939 0.4560 0.0473  -0.0651 -0.1515 796  ASP A N   
5816  C CA  . ASP A 798  ? 0.5030 0.5816 0.5359 0.0500  -0.0685 -0.1609 796  ASP A CA  
5817  C C   . ASP A 798  ? 0.4868 0.5787 0.5094 0.0529  -0.0663 -0.1602 796  ASP A C   
5818  O O   . ASP A 798  ? 0.4744 0.5748 0.4969 0.0545  -0.0688 -0.1662 796  ASP A O   
5819  C CB  . ASP A 798  ? 0.4257 0.5062 0.4634 0.0531  -0.0709 -0.1703 796  ASP A CB  
5820  C CG  . ASP A 798  ? 0.6156 0.6842 0.6651 0.0509  -0.0741 -0.1729 796  ASP A CG  
5821  O OD1 . ASP A 798  ? 0.6208 0.6829 0.6764 0.0474  -0.0763 -0.1710 796  ASP A OD1 
5822  O OD2 . ASP A 798  ? 0.6206 0.6868 0.6737 0.0525  -0.0747 -0.1766 796  ASP A OD2 
5823  N N   . ARG A 799  ? 0.4109 0.5049 0.4251 0.0534  -0.0619 -0.1529 797  ARG A N   
5824  C CA  . ARG A 799  ? 0.3860 0.4932 0.3911 0.0569  -0.0597 -0.1532 797  ARG A CA  
5825  C C   . ARG A 799  ? 0.3623 0.4734 0.3603 0.0558  -0.0572 -0.1450 797  ARG A C   
5826  O O   . ARG A 799  ? 0.3433 0.4459 0.3413 0.0527  -0.0554 -0.1369 797  ARG A O   
5827  C CB  . ARG A 799  ? 0.4478 0.5554 0.4492 0.0586  -0.0566 -0.1509 797  ARG A CB  
5828  C CG  . ARG A 799  ? 0.4313 0.5338 0.4401 0.0595  -0.0588 -0.1581 797  ARG A CG  
5829  C CD  . ARG A 799  ? 0.4859 0.6001 0.4947 0.0638  -0.0612 -0.1687 797  ARG A CD  
5830  N NE  . ARG A 799  ? 0.5353 0.6623 0.5342 0.0667  -0.0579 -0.1664 797  ARG A NE  
5831  C CZ  . ARG A 799  ? 0.4661 0.5944 0.4612 0.0681  -0.0549 -0.1637 797  ARG A CZ  
5832  N NH1 . ARG A 799  ? 0.5127 0.6307 0.5128 0.0671  -0.0546 -0.1633 797  ARG A NH1 
5833  N NH2 . ARG A 799  ? 0.5173 0.6578 0.5035 0.0705  -0.0520 -0.1609 797  ARG A NH2 
5834  N N   . LEU A 800  ? 0.3294 0.4537 0.3215 0.0586  -0.0573 -0.1472 798  LEU A N   
5835  C CA  . LEU A 800  ? 0.3495 0.4794 0.3341 0.0584  -0.0547 -0.1394 798  LEU A CA  
5836  C C   . LEU A 800  ? 0.3139 0.4575 0.2905 0.0621  -0.0527 -0.1394 798  LEU A C   
5837  O O   . LEU A 800  ? 0.3791 0.5307 0.3558 0.0652  -0.0543 -0.1476 798  LEU A O   
5838  C CB  . LEU A 800  ? 0.3677 0.5012 0.3537 0.0576  -0.0574 -0.1413 798  LEU A CB  
5839  C CG  . LEU A 800  ? 0.3649 0.4866 0.3580 0.0536  -0.0591 -0.1395 798  LEU A CG  
5840  C CD1 . LEU A 800  ? 0.3511 0.4783 0.3459 0.0535  -0.0621 -0.1430 798  LEU A CD1 
5841  C CD2 . LEU A 800  ? 0.3791 0.4924 0.3699 0.0508  -0.0555 -0.1286 798  LEU A CD2 
5842  N N   . SER A 801  ? 0.3497 0.4959 0.3197 0.0617  -0.0492 -0.1302 799  SER A N   
5843  C CA  . SER A 801  ? 0.3954 0.5554 0.3576 0.0648  -0.0472 -0.1285 799  SER A CA  
5844  C C   . SER A 801  ? 0.4068 0.5799 0.3668 0.0670  -0.0497 -0.1335 799  SER A C   
5845  O O   . SER A 801  ? 0.3979 0.5684 0.3618 0.0657  -0.0526 -0.1365 799  SER A O   
5846  C CB  . SER A 801  ? 0.3926 0.5510 0.3495 0.0634  -0.0434 -0.1168 799  SER A CB  
5847  O OG  . SER A 801  ? 0.4107 0.5692 0.3670 0.0619  -0.0440 -0.1126 799  SER A OG  
5848  N N   . PRO A 802  ? 0.3903 0.5783 0.3440 0.0703  -0.0488 -0.1345 800  PRO A N   
5849  C CA  . PRO A 802  ? 0.4531 0.6549 0.4038 0.0724  -0.0510 -0.1381 800  PRO A CA  
5850  C C   . PRO A 802  ? 0.4578 0.6579 0.4074 0.0702  -0.0510 -0.1313 800  PRO A C   
5851  O O   . PRO A 802  ? 0.4959 0.7026 0.4460 0.0709  -0.0538 -0.1356 800  PRO A O   
5852  C CB  . PRO A 802  ? 0.4310 0.6482 0.3741 0.0757  -0.0487 -0.1367 800  PRO A CB  
5853  C CG  . PRO A 802  ? 0.4503 0.6629 0.3948 0.0763  -0.0471 -0.1385 800  PRO A CG  
5854  C CD  . PRO A 802  ? 0.3927 0.5865 0.3422 0.0725  -0.0461 -0.1335 800  PRO A CD  
5855  N N   . ALA A 803  ? 0.4431 0.6348 0.3913 0.0678  -0.0480 -0.1210 801  ALA A N   
5856  C CA  . ALA A 803  ? 0.4763 0.6646 0.4246 0.0656  -0.0480 -0.1145 801  ALA A CA  
5857  C C   . ALA A 803  ? 0.4811 0.6562 0.4368 0.0625  -0.0502 -0.1170 801  ALA A C   
5858  O O   . ALA A 803  ? 0.4632 0.6340 0.4197 0.0603  -0.0500 -0.1116 801  ALA A O   
5859  C CB  . ALA A 803  ? 0.5088 0.6936 0.4534 0.0643  -0.0441 -0.1029 801  ALA A CB  
5860  N N   . GLY A 804  ? 0.4450 0.6140 0.4065 0.0622  -0.0522 -0.1248 802  GLY A N   
5861  C CA  . GLY A 804  ? 0.4087 0.5652 0.3778 0.0590  -0.0543 -0.1267 802  GLY A CA  
5862  C C   . GLY A 804  ? 0.4002 0.5431 0.3713 0.0556  -0.0517 -0.1185 802  GLY A C   
5863  O O   . GLY A 804  ? 0.3884 0.5242 0.3634 0.0528  -0.0527 -0.1164 802  GLY A O   
5864  N N   . ARG A 805  ? 0.3777 0.5170 0.3463 0.0558  -0.0486 -0.1142 803  ARG A N   
5865  C CA  . ARG A 805  ? 0.3761 0.5033 0.3462 0.0527  -0.0462 -0.1067 803  ARG A CA  
5866  C C   . ARG A 805  ? 0.3047 0.4242 0.2779 0.0524  -0.0455 -0.1088 803  ARG A C   
5867  O O   . ARG A 805  ? 0.3251 0.4502 0.2975 0.0550  -0.0460 -0.1144 803  ARG A O   
5868  C CB  . ARG A 805  ? 0.4082 0.5385 0.3720 0.0530  -0.0426 -0.0972 803  ARG A CB  
5869  C CG  . ARG A 805  ? 0.3765 0.5137 0.3377 0.0532  -0.0432 -0.0941 803  ARG A CG  
5870  C CD  . ARG A 805  ? 0.4303 0.5597 0.3969 0.0503  -0.0450 -0.0941 803  ARG A CD  
5871  N NE  . ARG A 805  ? 0.3856 0.5218 0.3501 0.0506  -0.0458 -0.0916 803  ARG A NE  
5872  C CZ  . ARG A 805  ? 0.4447 0.5885 0.4099 0.0518  -0.0489 -0.0974 803  ARG A CZ  
5873  N NH1 . ARG A 805  ? 0.4505 0.5962 0.4188 0.0527  -0.0517 -0.1065 803  ARG A NH1 
5874  N NH2 . ARG A 805  ? 0.5067 0.6565 0.4698 0.0520  -0.0493 -0.0941 803  ARG A NH2 
5875  N N   . PRO A 806  ? 0.3305 0.4376 0.3075 0.0493  -0.0445 -0.1047 804  PRO A N   
5876  C CA  . PRO A 806  ? 0.3155 0.4149 0.2962 0.0488  -0.0442 -0.1068 804  PRO A CA  
5877  C C   . PRO A 806  ? 0.3027 0.4063 0.2780 0.0510  -0.0413 -0.1045 804  PRO A C   
5878  O O   . PRO A 806  ? 0.3115 0.4194 0.2810 0.0515  -0.0385 -0.0979 804  PRO A O   
5879  C CB  . PRO A 806  ? 0.3448 0.4319 0.3291 0.0450  -0.0431 -0.1007 804  PRO A CB  
5880  C CG  . PRO A 806  ? 0.3628 0.4505 0.3482 0.0434  -0.0444 -0.0993 804  PRO A CG  
5881  C CD  . PRO A 806  ? 0.3467 0.4466 0.3258 0.0461  -0.0440 -0.0989 804  PRO A CD  
5882  N N   . ILE A 807  ? 0.2794 0.3820 0.2573 0.0523  -0.0420 -0.1101 805  ILE A N   
5883  C CA  . ILE A 807  ? 0.2662 0.3722 0.2400 0.0543  -0.0394 -0.1085 805  ILE A CA  
5884  C C   . ILE A 807  ? 0.2469 0.3425 0.2210 0.0517  -0.0365 -0.1006 805  ILE A C   
5885  O O   . ILE A 807  ? 0.3036 0.3886 0.2834 0.0494  -0.0374 -0.1011 805  ILE A O   
5886  C CB  . ILE A 807  ? 0.2973 0.4048 0.2748 0.0564  -0.0414 -0.1174 805  ILE A CB  
5887  C CG1 . ILE A 807  ? 0.3511 0.4695 0.3286 0.0591  -0.0445 -0.1260 805  ILE A CG1 
5888  C CG2 . ILE A 807  ? 0.3037 0.4141 0.2774 0.0583  -0.0385 -0.1156 805  ILE A CG2 
5889  C CD1 . ILE A 807  ? 0.3490 0.4819 0.3184 0.0619  -0.0429 -0.1243 805  ILE A CD1 
5890  N N   . PRO A 808  ? 0.2600 0.3583 0.2283 0.0519  -0.0331 -0.0931 806  PRO A N   
5891  C CA  . PRO A 808  ? 0.2564 0.3450 0.2252 0.0495  -0.0305 -0.0859 806  PRO A CA  
5892  C C   . PRO A 808  ? 0.2514 0.3339 0.2233 0.0494  -0.0302 -0.0884 806  PRO A C   
5893  O O   . PRO A 808  ? 0.2543 0.3426 0.2250 0.0520  -0.0303 -0.0927 806  PRO A O   
5894  C CB  . PRO A 808  ? 0.2766 0.3718 0.2388 0.0505  -0.0274 -0.0789 806  PRO A CB  
5895  C CG  . PRO A 808  ? 0.2763 0.3827 0.2353 0.0524  -0.0286 -0.0806 806  PRO A CG  
5896  C CD  . PRO A 808  ? 0.2587 0.3693 0.2204 0.0542  -0.0318 -0.0905 806  PRO A CD  
5897  N N   . LEU A 809  ? 0.2523 0.3234 0.2283 0.0464  -0.0299 -0.0854 807  LEU A N   
5898  C CA  . LEU A 809  ? 0.2564 0.3204 0.2359 0.0459  -0.0296 -0.0864 807  LEU A CA  
5899  C C   . LEU A 809  ? 0.2371 0.2940 0.2153 0.0436  -0.0267 -0.0782 807  LEU A C   
5900  O O   . LEU A 809  ? 0.2626 0.3138 0.2423 0.0409  -0.0265 -0.0742 807  LEU A O   
5901  C CB  . LEU A 809  ? 0.2830 0.3396 0.2702 0.0442  -0.0329 -0.0915 807  LEU A CB  
5902  C CG  . LEU A 809  ? 0.2707 0.3186 0.2624 0.0431  -0.0328 -0.0915 807  LEU A CG  
5903  C CD1 . LEU A 809  ? 0.2729 0.3259 0.2633 0.0463  -0.0324 -0.0958 807  LEU A CD1 
5904  C CD2 . LEU A 809  ? 0.2936 0.3340 0.2935 0.0410  -0.0362 -0.0952 807  LEU A CD2 
5905  N N   . ILE A 810  ? 0.2238 0.2816 0.1994 0.0446  -0.0243 -0.0758 808  ILE A N   
5906  C CA  . ILE A 810  ? 0.2429 0.2929 0.2187 0.0425  -0.0219 -0.0695 808  ILE A CA  
5907  C C   . ILE A 810  ? 0.2501 0.2934 0.2310 0.0420  -0.0230 -0.0730 808  ILE A C   
5908  O O   . ILE A 810  ? 0.2616 0.3086 0.2427 0.0443  -0.0235 -0.0777 808  ILE A O   
5909  C CB  . ILE A 810  ? 0.2343 0.2892 0.2046 0.0438  -0.0187 -0.0645 808  ILE A CB  
5910  C CG1 . ILE A 810  ? 0.2544 0.3172 0.2201 0.0447  -0.0179 -0.0613 808  ILE A CG1 
5911  C CG2 . ILE A 810  ? 0.2646 0.3113 0.2356 0.0415  -0.0165 -0.0583 808  ILE A CG2 
5912  C CD1 . ILE A 810  ? 0.2931 0.3606 0.2542 0.0457  -0.0149 -0.0553 808  ILE A CD1 
5913  N N   . ALA A 811  ? 0.2440 0.2779 0.2293 0.0390  -0.0237 -0.0710 809  ALA A N   
5914  C CA  . ALA A 811  ? 0.2519 0.2789 0.2429 0.0381  -0.0251 -0.0738 809  ALA A CA  
5915  C C   . ALA A 811  ? 0.2363 0.2558 0.2276 0.0355  -0.0230 -0.0672 809  ALA A C   
5916  O O   . ALA A 811  ? 0.2408 0.2554 0.2337 0.0328  -0.0231 -0.0637 809  ALA A O   
5917  C CB  . ALA A 811  ? 0.2735 0.2971 0.2708 0.0369  -0.0287 -0.0784 809  ALA A CB  
5918  N N   . GLU A 812  ? 0.2188 0.2380 0.2086 0.0365  -0.0211 -0.0657 810  GLU A N   
5919  C CA  . GLU A 812  ? 0.2394 0.2524 0.2290 0.0344  -0.0190 -0.0598 810  GLU A CA  
5920  C C   . GLU A 812  ? 0.2264 0.2331 0.2216 0.0336  -0.0204 -0.0620 810  GLU A C   
5921  O O   . GLU A 812  ? 0.2402 0.2490 0.2363 0.0359  -0.0209 -0.0660 810  GLU A O   
5922  C CB  . GLU A 812  ? 0.2659 0.2834 0.2500 0.0359  -0.0158 -0.0561 810  GLU A CB  
5923  C CG  . GLU A 812  ? 0.2569 0.2807 0.2361 0.0366  -0.0147 -0.0535 810  GLU A CG  
5924  C CD  . GLU A 812  ? 0.2869 0.3064 0.2668 0.0339  -0.0146 -0.0495 810  GLU A CD  
5925  O OE1 . GLU A 812  ? 0.2792 0.2949 0.2583 0.0323  -0.0126 -0.0442 810  GLU A OE1 
5926  O OE2 . GLU A 812  ? 0.2851 0.3053 0.2665 0.0334  -0.0166 -0.0517 810  GLU A OE2 
5927  N N   . THR A 813  ? 0.2331 0.2325 0.2324 0.0306  -0.0213 -0.0595 811  THR A N   
5928  C CA  . THR A 813  ? 0.2438 0.2374 0.2499 0.0296  -0.0237 -0.0621 811  THR A CA  
5929  C C   . THR A 813  ? 0.2402 0.2272 0.2480 0.0272  -0.0225 -0.0570 811  THR A C   
5930  O O   . THR A 813  ? 0.2605 0.2480 0.2640 0.0272  -0.0196 -0.0527 811  THR A O   
5931  C CB  . THR A 813  ? 0.2561 0.2482 0.2675 0.0283  -0.0270 -0.0655 811  THR A CB  
5932  O OG1 . THR A 813  ? 0.2553 0.2468 0.2650 0.0260  -0.0263 -0.0614 811  THR A OG1 
5933  C CG2 . THR A 813  ? 0.2704 0.2692 0.2812 0.0314  -0.0287 -0.0723 811  THR A CG2 
5934  N N   . GLY A 814  ? 0.2481 0.2291 0.2626 0.0252  -0.0248 -0.0575 812  GLY A N   
5935  C CA  . GLY A 814  ? 0.2549 0.2304 0.2716 0.0234  -0.0241 -0.0535 812  GLY A CA  
5936  C C   . GLY A 814  ? 0.2690 0.2423 0.2835 0.0204  -0.0222 -0.0470 812  GLY A C   
5937  O O   . GLY A 814  ? 0.2800 0.2556 0.2918 0.0197  -0.0214 -0.0454 812  GLY A O   
5938  N N   . GLY A 815  ? 0.2505 0.2196 0.2666 0.0189  -0.0214 -0.0433 813  GLY A N   
5939  C CA  . GLY A 815  ? 0.2514 0.2187 0.2659 0.0161  -0.0197 -0.0375 813  GLY A CA  
5940  C C   . GLY A 815  ? 0.2541 0.2163 0.2744 0.0135  -0.0211 -0.0350 813  GLY A C   
5941  O O   . GLY A 815  ? 0.2868 0.2462 0.3118 0.0140  -0.0230 -0.0371 813  GLY A O   
5942  N N   . GLN A 816  ? 0.2417 0.2028 0.2617 0.0107  -0.0202 -0.0303 814  GLN A N   
5943  C CA  . GLN A 816  ? 0.2566 0.2140 0.2808 0.0079  -0.0209 -0.0265 814  GLN A CA  
5944  C C   . GLN A 816  ? 0.2437 0.2023 0.2633 0.0068  -0.0179 -0.0218 814  GLN A C   
5945  O O   . GLN A 816  ? 0.2540 0.2133 0.2737 0.0044  -0.0175 -0.0185 814  GLN A O   
5946  C CB  . GLN A 816  ? 0.2601 0.2161 0.2901 0.0052  -0.0235 -0.0258 814  GLN A CB  
5947  C CG  . GLN A 816  ? 0.2913 0.2437 0.3268 0.0024  -0.0248 -0.0219 814  GLN A CG  
5948  C CD  . GLN A 816  ? 0.3222 0.2710 0.3624 0.0037  -0.0268 -0.0243 814  GLN A CD  
5949  O OE1 . GLN A 816  ? 0.3057 0.2541 0.3436 0.0053  -0.0254 -0.0242 814  GLN A OE1 
5950  N NE2 . GLN A 816  ? 0.3418 0.2881 0.3894 0.0031  -0.0303 -0.0266 814  GLN A NE2 
5951  N N   . ASN A 817  ? 0.2167 0.1760 0.2322 0.0087  -0.0158 -0.0217 815  ASN A N   
5952  C CA  . ASN A 817  ? 0.2125 0.1740 0.2229 0.0086  -0.0129 -0.0187 815  ASN A CA  
5953  C C   . ASN A 817  ? 0.2232 0.1830 0.2346 0.0062  -0.0122 -0.0143 815  ASN A C   
5954  O O   . ASN A 817  ? 0.2244 0.1816 0.2385 0.0058  -0.0129 -0.0135 815  ASN A O   
5955  C CB  . ASN A 817  ? 0.2233 0.1865 0.2295 0.0115  -0.0111 -0.0201 815  ASN A CB  
5956  C CG  . ASN A 817  ? 0.2047 0.1704 0.2101 0.0140  -0.0120 -0.0246 815  ASN A CG  
5957  O OD1 . ASN A 817  ? 0.2124 0.1803 0.2167 0.0140  -0.0124 -0.0256 815  ASN A OD1 
5958  N ND2 . ASN A 817  ? 0.2205 0.1863 0.2265 0.0161  -0.0125 -0.0275 815  ASN A ND2 
5959  N N   . ALA A 818  ? 0.2116 0.1732 0.2208 0.0046  -0.0108 -0.0116 816  ALA A N   
5960  C CA  . ALA A 818  ? 0.2038 0.1652 0.2137 0.0023  -0.0100 -0.0076 816  ALA A CA  
5961  C C   . ALA A 818  ? 0.2007 0.1638 0.2061 0.0031  -0.0073 -0.0062 816  ALA A C   
5962  O O   . ALA A 818  ? 0.2062 0.1711 0.2081 0.0049  -0.0060 -0.0075 816  ALA A O   
5963  C CB  . ALA A 818  ? 0.2119 0.1751 0.2235 -0.0003 -0.0106 -0.0058 816  ALA A CB  
5964  N N   . MET A 819  ? 0.2046 0.1672 0.2105 0.0017  -0.0067 -0.0034 817  MET A N   
5965  C CA  . MET A 819  ? 0.1979 0.1623 0.2004 0.0018  -0.0044 -0.0018 817  MET A CA  
5966  C C   . MET A 819  ? 0.2193 0.1855 0.2232 -0.0010 -0.0044 0.0012  817  MET A C   
5967  O O   . MET A 819  ? 0.2212 0.1864 0.2283 -0.0027 -0.0057 0.0030  817  MET A O   
5968  C CB  . MET A 819  ? 0.2233 0.1862 0.2248 0.0031  -0.0035 -0.0017 817  MET A CB  
5969  C CG  . MET A 819  ? 0.2228 0.1875 0.2217 0.0030  -0.0014 -0.0001 817  MET A CG  
5970  S SD  . MET A 819  ? 0.2468 0.2098 0.2453 0.0041  -0.0005 0.0005  817  MET A SD  
5971  C CE  . MET A 819  ? 0.2834 0.2461 0.2799 0.0072  0.0000  -0.0023 817  MET A CE  
5972  N N   . ILE A 820  ? 0.2044 0.1737 0.2061 -0.0014 -0.0030 0.0017  818  ILE A N   
5973  C CA  . ILE A 820  ? 0.2175 0.1899 0.2200 -0.0038 -0.0027 0.0042  818  ILE A CA  
5974  C C   . ILE A 820  ? 0.2091 0.1827 0.2095 -0.0033 -0.0009 0.0049  818  ILE A C   
5975  O O   . ILE A 820  ? 0.2153 0.1888 0.2132 -0.0015 0.0004  0.0034  818  ILE A O   
5976  C CB  . ILE A 820  ? 0.2158 0.1916 0.2181 -0.0045 -0.0026 0.0038  818  ILE A CB  
5977  C CG1 . ILE A 820  ? 0.2201 0.1947 0.2252 -0.0052 -0.0046 0.0032  818  ILE A CG1 
5978  C CG2 . ILE A 820  ? 0.2413 0.2215 0.2440 -0.0067 -0.0019 0.0061  818  ILE A CG2 
5979  C CD1 . ILE A 820  ? 0.2153 0.1934 0.2204 -0.0059 -0.0045 0.0028  818  ILE A CD1 
5980  N N   . VAL A 821  ? 0.2176 0.1924 0.2191 -0.0051 -0.0011 0.0073  819  VAL A N   
5981  C CA  . VAL A 821  ? 0.2201 0.1962 0.2200 -0.0049 0.0003  0.0079  819  VAL A CA  
5982  C C   . VAL A 821  ? 0.2294 0.2107 0.2298 -0.0071 0.0006  0.0098  819  VAL A C   
5983  O O   . VAL A 821  ? 0.2529 0.2355 0.2556 -0.0092 -0.0006 0.0122  819  VAL A O   
5984  C CB  . VAL A 821  ? 0.2232 0.1964 0.2242 -0.0048 -0.0002 0.0091  819  VAL A CB  
5985  C CG1 . VAL A 821  ? 0.2434 0.2184 0.2430 -0.0048 0.0011  0.0097  819  VAL A CG1 
5986  C CG2 . VAL A 821  ? 0.2274 0.1964 0.2282 -0.0025 -0.0005 0.0070  819  VAL A CG2 
5987  N N   . ASP A 822  ? 0.2121 0.1965 0.2105 -0.0066 0.0020  0.0086  820  ASP A N   
5988  C CA  . ASP A 822  ? 0.2298 0.2202 0.2285 -0.0084 0.0024  0.0099  820  ASP A CA  
5989  C C   . ASP A 822  ? 0.2410 0.2329 0.2390 -0.0085 0.0031  0.0105  820  ASP A C   
5990  O O   . ASP A 822  ? 0.2429 0.2310 0.2404 -0.0073 0.0033  0.0101  820  ASP A O   
5991  C CB  . ASP A 822  ? 0.2465 0.2405 0.2443 -0.0080 0.0032  0.0079  820  ASP A CB  
5992  C CG  . ASP A 822  ? 0.2327 0.2265 0.2290 -0.0059 0.0046  0.0052  820  ASP A CG  
5993  O OD1 . ASP A 822  ? 0.2521 0.2439 0.2478 -0.0050 0.0051  0.0050  820  ASP A OD1 
5994  O OD2 . ASP A 822  ? 0.2627 0.2586 0.2589 -0.0051 0.0050  0.0034  820  ASP A OD2 
5995  N N   . SER A 823  ? 0.2456 0.2438 0.2435 -0.0100 0.0035  0.0113  821  SER A N   
5996  C CA  . SER A 823  ? 0.2580 0.2588 0.2554 -0.0104 0.0039  0.0120  821  SER A CA  
5997  C C   . SER A 823  ? 0.2852 0.2855 0.2813 -0.0084 0.0052  0.0089  821  SER A C   
5998  O O   . SER A 823  ? 0.3156 0.3176 0.3113 -0.0086 0.0055  0.0089  821  SER A O   
5999  C CB  . SER A 823  ? 0.2810 0.2899 0.2788 -0.0127 0.0039  0.0139  821  SER A CB  
6000  O OG  . SER A 823  ? 0.3321 0.3455 0.3293 -0.0124 0.0046  0.0116  821  SER A OG  
6001  N N   . SER A 824  ? 0.2323 0.2301 0.2279 -0.0066 0.0057  0.0063  822  SER A N   
6002  C CA  . SER A 824  ? 0.2341 0.2307 0.2293 -0.0048 0.0067  0.0037  822  SER A CA  
6003  C C   . SER A 824  ? 0.2588 0.2491 0.2538 -0.0033 0.0067  0.0039  822  SER A C   
6004  O O   . SER A 824  ? 0.2786 0.2677 0.2737 -0.0020 0.0074  0.0025  822  SER A O   
6005  C CB  . SER A 824  ? 0.2490 0.2467 0.2444 -0.0036 0.0072  0.0012  822  SER A CB  
6006  O OG  . SER A 824  ? 0.2481 0.2413 0.2432 -0.0025 0.0069  0.0012  822  SER A OG  
6007  N N   . ALA A 825  ? 0.2492 0.2358 0.2442 -0.0034 0.0060  0.0055  823  ALA A N   
6008  C CA  . ALA A 825  ? 0.2636 0.2451 0.2584 -0.0019 0.0061  0.0054  823  ALA A CA  
6009  C C   . ALA A 825  ? 0.2621 0.2431 0.2571 -0.0022 0.0061  0.0064  823  ALA A C   
6010  O O   . ALA A 825  ? 0.2781 0.2620 0.2736 -0.0038 0.0057  0.0079  823  ALA A O   
6011  C CB  . ALA A 825  ? 0.2613 0.2397 0.2564 -0.0019 0.0050  0.0062  823  ALA A CB  
6012  N N   . LEU A 826  ? 0.2759 0.2537 0.2708 -0.0006 0.0067  0.0059  824  LEU A N   
6013  C CA  . LEU A 826  ? 0.2774 0.2545 0.2728 -0.0007 0.0068  0.0068  824  LEU A CA  
6014  C C   . LEU A 826  ? 0.2832 0.2573 0.2791 -0.0008 0.0058  0.0083  824  LEU A C   
6015  O O   . LEU A 826  ? 0.2819 0.2530 0.2777 0.0006  0.0058  0.0077  824  LEU A O   
6016  C CB  . LEU A 826  ? 0.3278 0.3031 0.3233 0.0010  0.0077  0.0056  824  LEU A CB  
6017  N N   . ALA A 827  ? 0.2861 0.2616 0.2830 -0.0023 0.0050  0.0102  825  ALA A N   
6018  C CA  . ALA A 827  ? 0.2652 0.2381 0.2636 -0.0026 0.0037  0.0117  825  ALA A CA  
6019  C C   . ALA A 827  ? 0.2724 0.2414 0.2709 -0.0006 0.0039  0.0109  825  ALA A C   
6020  O O   . ALA A 827  ? 0.2622 0.2284 0.2615 0.0002  0.0032  0.0105  825  ALA A O   
6021  C CB  . ALA A 827  ? 0.2940 0.2692 0.2937 -0.0045 0.0028  0.0144  825  ALA A CB  
6022  N N   . GLU A 828  ? 0.2784 0.2475 0.2764 0.0002  0.0049  0.0106  826  GLU A N   
6023  C CA  . GLU A 828  ? 0.2753 0.2416 0.2736 0.0019  0.0053  0.0100  826  GLU A CA  
6024  C C   . GLU A 828  ? 0.2902 0.2549 0.2874 0.0037  0.0058  0.0083  826  GLU A C   
6025  O O   . GLU A 828  ? 0.2803 0.2432 0.2779 0.0051  0.0055  0.0077  826  GLU A O   
6026  C CB  . GLU A 828  ? 0.3461 0.3133 0.3443 0.0023  0.0063  0.0101  826  GLU A CB  
6027  C CG  . GLU A 828  ? 0.3786 0.3472 0.3780 0.0010  0.0057  0.0117  826  GLU A CG  
6028  C CD  . GLU A 828  ? 0.4607 0.4332 0.4598 -0.0009 0.0054  0.0124  826  GLU A CD  
6029  O OE1 . GLU A 828  ? 0.4202 0.3943 0.4184 -0.0012 0.0058  0.0113  826  GLU A OE1 
6030  O OE2 . GLU A 828  ? 0.5395 0.5139 0.5394 -0.0020 0.0049  0.0139  826  GLU A OE2 
6031  N N   . GLN A 829  ? 0.2792 0.2453 0.2752 0.0037  0.0065  0.0075  827  GLN A N   
6032  C CA  . GLN A 829  ? 0.3094 0.2747 0.3043 0.0053  0.0070  0.0062  827  GLN A CA  
6033  C C   . GLN A 829  ? 0.2498 0.2141 0.2450 0.0052  0.0057  0.0056  827  GLN A C   
6034  O O   . GLN A 829  ? 0.2620 0.2251 0.2569 0.0068  0.0056  0.0045  827  GLN A O   
6035  C CB  . GLN A 829  ? 0.3571 0.3241 0.3513 0.0051  0.0077  0.0056  827  GLN A CB  
6036  C CG  . GLN A 829  ? 0.4410 0.4078 0.4346 0.0068  0.0087  0.0051  827  GLN A CG  
6037  C CD  . GLN A 829  ? 0.4508 0.4191 0.4448 0.0065  0.0092  0.0046  827  GLN A CD  
6038  O OE1 . GLN A 829  ? 0.4074 0.3771 0.4013 0.0055  0.0087  0.0041  827  GLN A OE1 
6039  N NE2 . GLN A 829  ? 0.5025 0.4707 0.4974 0.0072  0.0100  0.0049  827  GLN A NE2 
6040  N N   . VAL A 830  ? 0.2459 0.2111 0.2418 0.0034  0.0048  0.0063  828  VAL A N   
6041  C CA  . VAL A 830  ? 0.2396 0.2038 0.2366 0.0030  0.0034  0.0060  828  VAL A CA  
6042  C C   . VAL A 830  ? 0.2267 0.1883 0.2255 0.0038  0.0023  0.0058  828  VAL A C   
6043  O O   . VAL A 830  ? 0.2345 0.1947 0.2337 0.0051  0.0016  0.0041  828  VAL A O   
6044  C CB  . VAL A 830  ? 0.2477 0.2139 0.2459 0.0006  0.0025  0.0076  828  VAL A CB  
6045  C CG1 . VAL A 830  ? 0.2590 0.2237 0.2593 -0.0001 0.0007  0.0078  828  VAL A CG1 
6046  C CG2 . VAL A 830  ? 0.2739 0.2430 0.2705 0.0002  0.0034  0.0071  828  VAL A CG2 
6047  N N   . VAL A 831  ? 0.2281 0.1894 0.2282 0.0032  0.0021  0.0073  829  VAL A N   
6048  C CA  . VAL A 831  ? 0.2355 0.1943 0.2380 0.0039  0.0007  0.0071  829  VAL A CA  
6049  C C   . VAL A 831  ? 0.2213 0.1792 0.2229 0.0065  0.0014  0.0048  829  VAL A C   
6050  O O   . VAL A 831  ? 0.2274 0.1838 0.2306 0.0077  0.0003  0.0031  829  VAL A O   
6051  C CB  . VAL A 831  ? 0.2376 0.1966 0.2419 0.0027  0.0003  0.0095  829  VAL A CB  
6052  C CG1 . VAL A 831  ? 0.2384 0.1948 0.2455 0.0039  -0.0009 0.0090  829  VAL A CG1 
6053  C CG2 . VAL A 831  ? 0.2609 0.2214 0.2666 0.0001  -0.0008 0.0119  829  VAL A CG2 
6054  N N   . GLY A 832  ? 0.2323 0.1916 0.2317 0.0075  0.0033  0.0047  830  GLY A N   
6055  C CA  . GLY A 832  ? 0.2200 0.1795 0.2183 0.0098  0.0041  0.0030  830  GLY A CA  
6056  C C   . GLY A 832  ? 0.2155 0.1754 0.2128 0.0110  0.0037  0.0010  830  GLY A C   
6057  O O   . GLY A 832  ? 0.2379 0.1978 0.2358 0.0127  0.0032  -0.0011 830  GLY A O   
6058  N N   . ASP A 833  ? 0.2257 0.1865 0.2218 0.0100  0.0039  0.0012  831  ASP A N   
6059  C CA  . ASP A 833  ? 0.2200 0.1814 0.2150 0.0110  0.0035  -0.0006 831  ASP A CA  
6060  C C   . ASP A 833  ? 0.2145 0.1744 0.2120 0.0107  0.0014  -0.0021 831  ASP A C   
6061  O O   . ASP A 833  ? 0.2337 0.1941 0.2310 0.0122  0.0008  -0.0045 831  ASP A O   
6062  C CB  . ASP A 833  ? 0.2298 0.1926 0.2233 0.0101  0.0042  0.0001  831  ASP A CB  
6063  C CG  . ASP A 833  ? 0.2395 0.2037 0.2313 0.0108  0.0060  0.0011  831  ASP A CG  
6064  O OD1 . ASP A 833  ? 0.2687 0.2334 0.2602 0.0122  0.0068  0.0011  831  ASP A OD1 
6065  O OD2 . ASP A 833  ? 0.2512 0.2164 0.2426 0.0099  0.0065  0.0018  831  ASP A OD2 
6066  N N   . VAL A 834  ? 0.2172 0.1755 0.2172 0.0087  0.0002  -0.0006 832  VAL A N   
6067  C CA  . VAL A 834  ? 0.2261 0.1824 0.2295 0.0082  -0.0021 -0.0015 832  VAL A CA  
6068  C C   . VAL A 834  ? 0.2177 0.1726 0.2233 0.0101  -0.0030 -0.0035 832  VAL A C   
6069  O O   . VAL A 834  ? 0.2226 0.1768 0.2300 0.0112  -0.0045 -0.0063 832  VAL A O   
6070  C CB  . VAL A 834  ? 0.2247 0.1803 0.2306 0.0054  -0.0031 0.0014  832  VAL A CB  
6071  C CG1 . VAL A 834  ? 0.2473 0.2005 0.2580 0.0049  -0.0057 0.0010  832  VAL A CG1 
6072  C CG2 . VAL A 834  ? 0.2463 0.2041 0.2506 0.0038  -0.0025 0.0026  832  VAL A CG2 
6073  N N   . ILE A 835  ? 0.2270 0.1816 0.2329 0.0104  -0.0023 -0.0024 833  ILE A N   
6074  C CA  . ILE A 835  ? 0.2469 0.2004 0.2550 0.0124  -0.0031 -0.0044 833  ILE A CA  
6075  C C   . ILE A 835  ? 0.2373 0.1930 0.2433 0.0151  -0.0024 -0.0078 833  ILE A C   
6076  O O   . ILE A 835  ? 0.2608 0.2162 0.2691 0.0167  -0.0038 -0.0110 833  ILE A O   
6077  C CB  . ILE A 835  ? 0.2422 0.1958 0.2505 0.0123  -0.0021 -0.0024 833  ILE A CB  
6078  C CG1 . ILE A 835  ? 0.2645 0.2163 0.2756 0.0098  -0.0034 0.0007  833  ILE A CG1 
6079  C CG2 . ILE A 835  ? 0.2959 0.2495 0.3057 0.0148  -0.0023 -0.0049 833  ILE A CG2 
6080  C CD1 . ILE A 835  ? 0.3004 0.2494 0.3168 0.0097  -0.0061 0.0001  833  ILE A CD1 
6081  N N   . THR A 836  ? 0.2380 0.1964 0.2399 0.0156  -0.0002 -0.0072 834  THR A N   
6082  C CA  . THR A 836  ? 0.2324 0.1939 0.2320 0.0180  0.0006  -0.0097 834  THR A CA  
6083  C C   . THR A 836  ? 0.2505 0.2122 0.2505 0.0183  -0.0009 -0.0123 834  THR A C   
6084  O O   . THR A 836  ? 0.2583 0.2212 0.2592 0.0203  -0.0019 -0.0158 834  THR A O   
6085  C CB  . THR A 836  ? 0.2795 0.2437 0.2754 0.0182  0.0029  -0.0077 834  THR A CB  
6086  O OG1 . THR A 836  ? 0.3632 0.3273 0.3591 0.0182  0.0041  -0.0058 834  THR A OG1 
6087  C CG2 . THR A 836  ? 0.3398 0.3079 0.3332 0.0205  0.0037  -0.0096 834  THR A CG2 
6088  N N   . SER A 837  ? 0.2296 0.1905 0.2292 0.0164  -0.0012 -0.0108 835  SER A N   
6089  C CA  . SER A 837  ? 0.2255 0.1870 0.2252 0.0166  -0.0025 -0.0130 835  SER A CA  
6090  C C   . SER A 837  ? 0.2067 0.1658 0.2110 0.0166  -0.0052 -0.0156 835  SER A C   
6091  O O   . SER A 837  ? 0.2389 0.1992 0.2438 0.0180  -0.0064 -0.0191 835  SER A O   
6092  C CB  . SER A 837  ? 0.2229 0.1842 0.2217 0.0144  -0.0022 -0.0108 835  SER A CB  
6093  O OG  . SER A 837  ? 0.2393 0.2026 0.2345 0.0145  0.0000  -0.0089 835  SER A OG  
6094  N N   . ALA A 838  ? 0.2078 0.1637 0.2158 0.0151  -0.0063 -0.0140 836  ALA A N   
6095  C CA  . ALA A 838  ? 0.2055 0.1585 0.2189 0.0148  -0.0092 -0.0158 836  ALA A CA  
6096  C C   . ALA A 838  ? 0.2537 0.2066 0.2696 0.0174  -0.0101 -0.0194 836  ALA A C   
6097  O O   . ALA A 838  ? 0.2414 0.1933 0.2611 0.0183  -0.0125 -0.0230 836  ALA A O   
6098  C CB  . ALA A 838  ? 0.2420 0.1920 0.2590 0.0119  -0.0103 -0.0120 836  ALA A CB  
6099  N N   . PHE A 839  ? 0.2264 0.1803 0.2407 0.0185  -0.0085 -0.0185 837  PHE A N   
6100  C CA  . PHE A 839  ? 0.2310 0.1844 0.2485 0.0206  -0.0096 -0.0214 837  PHE A CA  
6101  C C   . PHE A 839  ? 0.2655 0.2234 0.2796 0.0237  -0.0078 -0.0241 837  PHE A C   
6102  O O   . PHE A 839  ? 0.2579 0.2164 0.2748 0.0259  -0.0088 -0.0276 837  PHE A O   
6103  C CB  . PHE A 839  ? 0.2365 0.1870 0.2570 0.0193  -0.0099 -0.0183 837  PHE A CB  
6104  C CG  . PHE A 839  ? 0.2318 0.1787 0.2560 0.0163  -0.0118 -0.0151 837  PHE A CG  
6105  C CD1 . PHE A 839  ? 0.2723 0.2166 0.3017 0.0159  -0.0147 -0.0170 837  PHE A CD1 
6106  C CD2 . PHE A 839  ? 0.2500 0.1966 0.2725 0.0138  -0.0106 -0.0103 837  PHE A CD2 
6107  C CE1 . PHE A 839  ? 0.2521 0.1937 0.2853 0.0128  -0.0165 -0.0136 837  PHE A CE1 
6108  C CE2 . PHE A 839  ? 0.2877 0.2322 0.3134 0.0109  -0.0122 -0.0071 837  PHE A CE2 
6109  C CZ  . PHE A 839  ? 0.2873 0.2293 0.3183 0.0104  -0.0151 -0.0085 837  PHE A CZ  
6110  N N   . ASP A 840  ? 0.2697 0.2312 0.2784 0.0239  -0.0053 -0.0226 838  ASP A N   
6111  C CA  . ASP A 840  ? 0.2556 0.2224 0.2612 0.0267  -0.0037 -0.0249 838  ASP A CA  
6112  C C   . ASP A 840  ? 0.2792 0.2480 0.2865 0.0289  -0.0056 -0.0304 838  ASP A C   
6113  O O   . ASP A 840  ? 0.2741 0.2413 0.2827 0.0280  -0.0073 -0.0317 838  ASP A O   
6114  C CB  . ASP A 840  ? 0.3129 0.2827 0.3132 0.0262  -0.0013 -0.0222 838  ASP A CB  
6115  C CG  . ASP A 840  ? 0.4103 0.3862 0.4073 0.0288  0.0004  -0.0235 838  ASP A CG  
6116  O OD1 . ASP A 840  ? 0.3712 0.3507 0.3672 0.0306  -0.0002 -0.0269 838  ASP A OD1 
6117  O OD2 . ASP A 840  ? 0.4585 0.4361 0.4540 0.0290  0.0024  -0.0209 838  ASP A OD2 
6118  N N   . SER A 841  ? 0.2620 0.2345 0.2696 0.0318  -0.0054 -0.0339 839  SER A N   
6119  C CA  . SER A 841  ? 0.2517 0.2269 0.2613 0.0343  -0.0073 -0.0399 839  SER A CA  
6120  C C   . SER A 841  ? 0.2505 0.2201 0.2667 0.0334  -0.0107 -0.0423 839  SER A C   
6121  O O   . SER A 841  ? 0.2464 0.2168 0.2646 0.0344  -0.0127 -0.0467 839  SER A O   
6122  C CB  . SER A 841  ? 0.3080 0.2882 0.3132 0.0351  -0.0065 -0.0412 839  SER A CB  
6123  O OG  . SER A 841  ? 0.3677 0.3527 0.3675 0.0355  -0.0035 -0.0379 839  SER A OG  
6124  N N   . ALA A 842  ? 0.2556 0.2197 0.2754 0.0314  -0.0115 -0.0392 840  ALA A N   
6125  C CA  . ALA A 842  ? 0.2371 0.1955 0.2638 0.0301  -0.0148 -0.0401 840  ALA A CA  
6126  C C   . ALA A 842  ? 0.2376 0.1947 0.2645 0.0282  -0.0161 -0.0399 840  ALA A C   
6127  O O   . ALA A 842  ? 0.2685 0.2232 0.3007 0.0283  -0.0191 -0.0432 840  ALA A O   
6128  C CB  . ALA A 842  ? 0.2391 0.1975 0.2717 0.0328  -0.0173 -0.0460 840  ALA A CB  
6129  N N   . GLY A 843  ? 0.2405 0.1990 0.2618 0.0266  -0.0139 -0.0362 841  GLY A N   
6130  C CA  . GLY A 843  ? 0.2319 0.1896 0.2531 0.0248  -0.0148 -0.0357 841  GLY A CA  
6131  C C   . GLY A 843  ? 0.2367 0.1981 0.2571 0.0269  -0.0158 -0.0409 841  GLY A C   
6132  O O   . GLY A 843  ? 0.2407 0.2012 0.2620 0.0256  -0.0171 -0.0413 841  GLY A O   
6133  N N   . GLN A 844  ? 0.2258 0.1919 0.2445 0.0301  -0.0151 -0.0449 842  GLN A N   
6134  C CA  . GLN A 844  ? 0.2215 0.1923 0.2394 0.0325  -0.0161 -0.0504 842  GLN A CA  
6135  C C   . GLN A 844  ? 0.2505 0.2271 0.2611 0.0331  -0.0134 -0.0488 842  GLN A C   
6136  O O   . GLN A 844  ? 0.2686 0.2516 0.2759 0.0358  -0.0123 -0.0516 842  GLN A O   
6137  C CB  . GLN A 844  ? 0.2319 0.2052 0.2528 0.0358  -0.0173 -0.0562 842  GLN A CB  
6138  C CG  . GLN A 844  ? 0.2384 0.2056 0.2679 0.0353  -0.0206 -0.0581 842  GLN A CG  
6139  C CD  . GLN A 844  ? 0.2287 0.1977 0.2615 0.0385  -0.0215 -0.0631 842  GLN A CD  
6140  O OE1 . GLN A 844  ? 0.2510 0.2195 0.2897 0.0401  -0.0245 -0.0689 842  GLN A OE1 
6141  N NE2 . GLN A 844  ? 0.2658 0.2372 0.2954 0.0394  -0.0189 -0.0609 842  GLN A NE2 
6142  N N   . ARG A 845  ? 0.2572 0.2316 0.2655 0.0304  -0.0123 -0.0439 843  ARG A N   
6143  C CA  . ARG A 845  ? 0.2520 0.2306 0.2546 0.0303  -0.0104 -0.0420 843  ARG A CA  
6144  C C   . ARG A 845  ? 0.2389 0.2150 0.2430 0.0283  -0.0121 -0.0418 843  ARG A C   
6145  O O   . ARG A 845  ? 0.2354 0.2061 0.2434 0.0258  -0.0133 -0.0399 843  ARG A O   
6146  C CB  . ARG A 845  ? 0.2627 0.2407 0.2615 0.0289  -0.0075 -0.0361 843  ARG A CB  
6147  C CG  . ARG A 845  ? 0.2701 0.2509 0.2672 0.0306  -0.0056 -0.0354 843  ARG A CG  
6148  C CD  . ARG A 845  ? 0.3023 0.2824 0.2963 0.0290  -0.0030 -0.0297 843  ARG A CD  
6149  N NE  . ARG A 845  ? 0.3804 0.3633 0.3728 0.0304  -0.0011 -0.0287 843  ARG A NE  
6150  C CZ  . ARG A 845  ? 0.4278 0.4167 0.4163 0.0320  0.0008  -0.0278 843  ARG A CZ  
6151  N NH1 . ARG A 845  ? 0.4241 0.4167 0.4097 0.0324  0.0011  -0.0277 843  ARG A NH1 
6152  N NH2 . ARG A 845  ? 0.4501 0.4416 0.4379 0.0331  0.0024  -0.0267 843  ARG A NH2 
6153  N N   . CYS A 846  ? 0.2373 0.2179 0.2386 0.0293  -0.0121 -0.0437 844  CYS A N   
6154  C CA  . CYS A 846  ? 0.2499 0.2286 0.2527 0.0274  -0.0136 -0.0434 844  CYS A CA  
6155  C C   . CYS A 846  ? 0.2311 0.2068 0.2323 0.0245  -0.0120 -0.0375 844  CYS A C   
6156  O O   . CYS A 846  ? 0.2221 0.1947 0.2260 0.0221  -0.0133 -0.0363 844  CYS A O   
6157  C CB  . CYS A 846  ? 0.2355 0.2202 0.2351 0.0291  -0.0137 -0.0462 844  CYS A CB  
6158  S SG  . CYS A 846  ? 0.2651 0.2565 0.2573 0.0308  -0.0103 -0.0432 844  CYS A SG  
6159  N N   . SER A 847  ? 0.2176 0.1946 0.2149 0.0246  -0.0093 -0.0339 845  SER A N   
6160  C CA  . SER A 847  ? 0.2016 0.1765 0.1973 0.0223  -0.0076 -0.0288 845  SER A CA  
6161  C C   . SER A 847  ? 0.2218 0.1917 0.2205 0.0203  -0.0078 -0.0262 845  SER A C   
6162  O O   . SER A 847  ? 0.2152 0.1836 0.2129 0.0183  -0.0065 -0.0223 845  SER A O   
6163  C CB  . SER A 847  ? 0.2212 0.1998 0.2121 0.0236  -0.0049 -0.0263 845  SER A CB  
6164  O OG  . SER A 847  ? 0.2545 0.2343 0.2454 0.0253  -0.0042 -0.0274 845  SER A OG  
6165  N N   . ALA A 848  ? 0.2257 0.1934 0.2283 0.0208  -0.0093 -0.0285 846  ALA A N   
6166  C CA  . ALA A 848  ? 0.2110 0.1747 0.2163 0.0193  -0.0094 -0.0258 846  ALA A CA  
6167  C C   . ALA A 848  ? 0.2223 0.1827 0.2299 0.0160  -0.0102 -0.0226 846  ALA A C   
6168  O O   . ALA A 848  ? 0.2288 0.1888 0.2383 0.0150  -0.0118 -0.0235 846  ALA A O   
6169  C CB  . ALA A 848  ? 0.2363 0.1981 0.2463 0.0205  -0.0114 -0.0291 846  ALA A CB  
6170  N N   . LEU A 849  ? 0.2212 0.1799 0.2287 0.0144  -0.0091 -0.0187 847  LEU A N   
6171  C CA  . LEU A 849  ? 0.2153 0.1720 0.2248 0.0113  -0.0096 -0.0154 847  LEU A CA  
6172  C C   . LEU A 849  ? 0.2178 0.1712 0.2336 0.0101  -0.0126 -0.0160 847  LEU A C   
6173  O O   . LEU A 849  ? 0.2358 0.1870 0.2544 0.0107  -0.0134 -0.0164 847  LEU A O   
6174  C CB  . LEU A 849  ? 0.2180 0.1744 0.2257 0.0101  -0.0078 -0.0115 847  LEU A CB  
6175  C CG  . LEU A 849  ? 0.2046 0.1600 0.2144 0.0070  -0.0083 -0.0079 847  LEU A CG  
6176  C CD1 . LEU A 849  ? 0.2156 0.1730 0.2239 0.0058  -0.0080 -0.0075 847  LEU A CD1 
6177  C CD2 . LEU A 849  ? 0.2336 0.1893 0.2417 0.0062  -0.0066 -0.0048 847  LEU A CD2 
6178  N N   . ARG A 850  ? 0.2088 0.1617 0.2272 0.0084  -0.0143 -0.0160 848  ARG A N   
6179  C CA  . ARG A 850  ? 0.2357 0.1854 0.2610 0.0069  -0.0173 -0.0161 848  ARG A CA  
6180  C C   . ARG A 850  ? 0.2234 0.1721 0.2510 0.0034  -0.0177 -0.0110 848  ARG A C   
6181  O O   . ARG A 850  ? 0.2442 0.1901 0.2776 0.0020  -0.0199 -0.0095 848  ARG A O   
6182  C CB  . ARG A 850  ? 0.2426 0.1925 0.2704 0.0073  -0.0195 -0.0198 848  ARG A CB  
6183  C CG  . ARG A 850  ? 0.2474 0.1996 0.2725 0.0108  -0.0192 -0.0250 848  ARG A CG  
6184  C CD  . ARG A 850  ? 0.2655 0.2166 0.2922 0.0130  -0.0195 -0.0273 848  ARG A CD  
6185  N NE  . ARG A 850  ? 0.2590 0.2132 0.2836 0.0163  -0.0195 -0.0326 848  ARG A NE  
6186  C CZ  . ARG A 850  ? 0.2577 0.2127 0.2824 0.0190  -0.0194 -0.0356 848  ARG A CZ  
6187  N NH1 . ARG A 850  ? 0.2263 0.1786 0.2533 0.0188  -0.0194 -0.0339 848  ARG A NH1 
6188  N NH2 . ARG A 850  ? 0.2447 0.2038 0.2672 0.0219  -0.0193 -0.0404 848  ARG A NH2 
6189  N N   . VAL A 851  ? 0.2431 0.1945 0.2668 0.0020  -0.0158 -0.0084 849  VAL A N   
6190  C CA  . VAL A 851  ? 0.2414 0.1934 0.2672 -0.0013 -0.0161 -0.0038 849  VAL A CA  
6191  C C   . VAL A 851  ? 0.2343 0.1890 0.2548 -0.0017 -0.0132 -0.0012 849  VAL A C   
6192  O O   . VAL A 851  ? 0.2406 0.1979 0.2568 -0.0010 -0.0114 -0.0021 849  VAL A O   
6193  C CB  . VAL A 851  ? 0.2794 0.2327 0.3071 -0.0030 -0.0173 -0.0037 849  VAL A CB  
6194  C CG1 . VAL A 851  ? 0.3184 0.2729 0.3488 -0.0066 -0.0177 0.0013  849  VAL A CG1 
6195  C CG2 . VAL A 851  ? 0.2973 0.2481 0.3301 -0.0023 -0.0203 -0.0072 849  VAL A CG2 
6196  N N   . LEU A 852  ? 0.2165 0.1708 0.2377 -0.0028 -0.0128 0.0019  850  LEU A N   
6197  C CA  . LEU A 852  ? 0.2297 0.1869 0.2469 -0.0034 -0.0104 0.0043  850  LEU A CA  
6198  C C   . LEU A 852  ? 0.2245 0.1845 0.2433 -0.0066 -0.0107 0.0081  850  LEU A C   
6199  O O   . LEU A 852  ? 0.2247 0.1837 0.2482 -0.0086 -0.0127 0.0107  850  LEU A O   
6200  C CB  . LEU A 852  ? 0.2118 0.1676 0.2290 -0.0028 -0.0099 0.0055  850  LEU A CB  
6201  C CG  . LEU A 852  ? 0.2358 0.1945 0.2495 -0.0035 -0.0077 0.0079  850  LEU A CG  
6202  C CD1 . LEU A 852  ? 0.2248 0.1854 0.2335 -0.0018 -0.0054 0.0058  850  LEU A CD1 
6203  C CD2 . LEU A 852  ? 0.2374 0.1944 0.2521 -0.0030 -0.0077 0.0090  850  LEU A CD2 
6204  N N   . CYS A 853  ? 0.2296 0.1932 0.2448 -0.0070 -0.0090 0.0084  851  CYS A N   
6205  C CA  . CYS A 853  ? 0.2093 0.1769 0.2256 -0.0098 -0.0091 0.0115  851  CYS A CA  
6206  C C   . CYS A 853  ? 0.2129 0.1840 0.2259 -0.0102 -0.0070 0.0132  851  CYS A C   
6207  O O   . CYS A 853  ? 0.2287 0.2011 0.2378 -0.0087 -0.0051 0.0113  851  CYS A O   
6208  C CB  . CYS A 853  ? 0.2322 0.2018 0.2475 -0.0098 -0.0089 0.0099  851  CYS A CB  
6209  S SG  . CYS A 853  ? 0.2658 0.2319 0.2841 -0.0088 -0.0111 0.0066  851  CYS A SG  
6210  N N   . LEU A 854  ? 0.2301 0.2029 0.2452 -0.0123 -0.0076 0.0169  852  LEU A N   
6211  C CA  . LEU A 854  ? 0.2223 0.1986 0.2348 -0.0127 -0.0059 0.0184  852  LEU A CA  
6212  C C   . LEU A 854  ? 0.2155 0.1982 0.2282 -0.0153 -0.0056 0.0211  852  LEU A C   
6213  O O   . LEU A 854  ? 0.2435 0.2276 0.2599 -0.0177 -0.0072 0.0243  852  LEU A O   
6214  C CB  . LEU A 854  ? 0.2302 0.2045 0.2448 -0.0131 -0.0068 0.0207  852  LEU A CB  
6215  C CG  . LEU A 854  ? 0.2300 0.1987 0.2447 -0.0106 -0.0071 0.0181  852  LEU A CG  
6216  C CD1 . LEU A 854  ? 0.2324 0.1996 0.2498 -0.0112 -0.0082 0.0207  852  LEU A CD1 
6217  C CD2 . LEU A 854  ? 0.2437 0.2126 0.2537 -0.0082 -0.0048 0.0151  852  LEU A CD2 
6218  N N   . GLN A 855  ? 0.2153 0.2022 0.2244 -0.0147 -0.0036 0.0199  853  GLN A N   
6219  C CA  . GLN A 855  ? 0.2227 0.2168 0.2317 -0.0169 -0.0031 0.0221  853  GLN A CA  
6220  C C   . GLN A 855  ? 0.2448 0.2416 0.2556 -0.0190 -0.0039 0.0263  853  GLN A C   
6221  O O   . GLN A 855  ? 0.2538 0.2484 0.2641 -0.0182 -0.0038 0.0265  853  GLN A O   
6222  C CB  . GLN A 855  ? 0.2191 0.2170 0.2243 -0.0156 -0.0010 0.0194  853  GLN A CB  
6223  C CG  . GLN A 855  ? 0.2335 0.2394 0.2386 -0.0175 -0.0005 0.0206  853  GLN A CG  
6224  C CD  . GLN A 855  ? 0.2725 0.2827 0.2747 -0.0162 0.0014  0.0177  853  GLN A CD  
6225  O OE1 . GLN A 855  ? 0.2974 0.3044 0.2979 -0.0138 0.0023  0.0142  853  GLN A OE1 
6226  N NE2 . GLN A 855  ? 0.3150 0.3329 0.3168 -0.0177 0.0020  0.0191  853  GLN A NE2 
6227  N N   . GLU A 856  ? 0.2495 0.2514 0.2627 -0.0218 -0.0048 0.0300  854  GLU A N   
6228  C CA  . GLU A 856  ? 0.2713 0.2754 0.2876 -0.0241 -0.0062 0.0350  854  GLU A CA  
6229  C C   . GLU A 856  ? 0.2923 0.2996 0.3059 -0.0238 -0.0050 0.0354  854  GLU A C   
6230  O O   . GLU A 856  ? 0.2977 0.3032 0.3131 -0.0242 -0.0060 0.0380  854  GLU A O   
6231  C CB  . GLU A 856  ? 0.2907 0.3016 0.3095 -0.0272 -0.0069 0.0390  854  GLU A CB  
6232  C CG  . GLU A 856  ? 0.3346 0.3495 0.3567 -0.0300 -0.0083 0.0450  854  GLU A CG  
6233  C CD  . GLU A 856  ? 0.4392 0.4465 0.4661 -0.0302 -0.0107 0.0471  854  GLU A CD  
6234  O OE1 . GLU A 856  ? 0.3909 0.3919 0.4204 -0.0296 -0.0120 0.0453  854  GLU A OE1 
6235  O OE2 . GLU A 856  ? 0.4443 0.4521 0.4725 -0.0310 -0.0115 0.0504  854  GLU A OE2 
6236  N N   . ASP A 857  ? 0.2692 0.2815 0.2788 -0.0228 -0.0029 0.0327  855  ASP A N   
6237  C CA  . ASP A 857  ? 0.3297 0.3465 0.3371 -0.0227 -0.0019 0.0329  855  ASP A CA  
6238  C C   . ASP A 857  ? 0.3121 0.3226 0.3186 -0.0206 -0.0017 0.0310  855  ASP A C   
6239  O O   . ASP A 857  ? 0.3419 0.3550 0.3476 -0.0208 -0.0015 0.0321  855  ASP A O   
6240  C CB  . ASP A 857  ? 0.3753 0.3986 0.3794 -0.0220 0.0000  0.0296  855  ASP A CB  
6241  N N   . VAL A 858  ? 0.2478 0.2505 0.2543 -0.0185 -0.0018 0.0282  856  VAL A N   
6242  C CA  . VAL A 858  ? 0.2687 0.2657 0.2745 -0.0165 -0.0016 0.0265  856  VAL A CA  
6243  C C   . VAL A 858  ? 0.2454 0.2357 0.2544 -0.0163 -0.0034 0.0277  856  VAL A C   
6244  O O   . VAL A 858  ? 0.2484 0.2341 0.2573 -0.0145 -0.0034 0.0264  856  VAL A O   
6245  C CB  . VAL A 858  ? 0.2771 0.2716 0.2799 -0.0139 0.0000  0.0218  856  VAL A CB  
6246  C CG1 . VAL A 858  ? 0.3115 0.3123 0.3119 -0.0138 0.0016  0.0201  856  VAL A CG1 
6247  C CG2 . VAL A 858  ? 0.2784 0.2697 0.2815 -0.0130 -0.0002 0.0198  856  VAL A CG2 
6248  N N   . ALA A 859  ? 0.2484 0.2384 0.2608 -0.0180 -0.0051 0.0302  857  ALA A N   
6249  C CA  . ALA A 859  ? 0.2374 0.2208 0.2536 -0.0175 -0.0070 0.0303  857  ALA A CA  
6250  C C   . ALA A 859  ? 0.2599 0.2410 0.2784 -0.0175 -0.0081 0.0326  857  ALA A C   
6251  O O   . ALA A 859  ? 0.2666 0.2419 0.2859 -0.0155 -0.0086 0.0305  857  ALA A O   
6252  C CB  . ALA A 859  ? 0.2560 0.2399 0.2762 -0.0196 -0.0088 0.0327  857  ALA A CB  
6253  N N   . ASP A 860  ? 0.2762 0.2622 0.2957 -0.0197 -0.0086 0.0369  858  ASP A N   
6254  C CA  . ASP A 860  ? 0.3091 0.2932 0.3313 -0.0199 -0.0099 0.0395  858  ASP A CA  
6255  C C   . ASP A 860  ? 0.2878 0.2696 0.3069 -0.0174 -0.0084 0.0364  858  ASP A C   
6256  O O   . ASP A 860  ? 0.2872 0.2639 0.3084 -0.0160 -0.0094 0.0359  858  ASP A O   
6257  C CB  . ASP A 860  ? 0.3028 0.2939 0.3262 -0.0227 -0.0105 0.0450  858  ASP A CB  
6258  C CG  . ASP A 860  ? 0.3845 0.3772 0.4127 -0.0255 -0.0126 0.0493  858  ASP A CG  
6259  O OD1 . ASP A 860  ? 0.4178 0.4045 0.4501 -0.0252 -0.0143 0.0488  858  ASP A OD1 
6260  O OD2 . ASP A 860  ? 0.5893 0.5897 0.6175 -0.0280 -0.0125 0.0533  858  ASP A OD2 
6261  N N   . ARG A 861  ? 0.2581 0.2437 0.2725 -0.0167 -0.0062 0.0342  859  ARG A N   
6262  C CA  . ARG A 861  ? 0.3296 0.3133 0.3415 -0.0145 -0.0049 0.0315  859  ARG A CA  
6263  C C   . ARG A 861  ? 0.2550 0.2321 0.2666 -0.0120 -0.0046 0.0277  859  ARG A C   
6264  O O   . ARG A 861  ? 0.2575 0.2311 0.2698 -0.0104 -0.0047 0.0269  859  ARG A O   
6265  C CB  . ARG A 861  ? 0.3537 0.3428 0.3615 -0.0144 -0.0028 0.0296  859  ARG A CB  
6266  C CG  . ARG A 861  ? 0.4392 0.4256 0.4447 -0.0120 -0.0014 0.0262  859  ARG A CG  
6267  C CD  . ARG A 861  ? 0.5367 0.5287 0.5396 -0.0122 0.0000  0.0250  859  ARG A CD  
6268  N NE  . ARG A 861  ? 0.6282 0.6175 0.6301 -0.0103 0.0009  0.0228  859  ARG A NE  
6269  C CZ  . ARG A 861  ? 0.5427 0.5297 0.5430 -0.0085 0.0023  0.0194  859  ARG A CZ  
6270  N NH1 . ARG A 861  ? 0.5647 0.5519 0.5639 -0.0081 0.0029  0.0175  859  ARG A NH1 
6271  N NH2 . ARG A 861  ? 0.5654 0.5502 0.5655 -0.0071 0.0029  0.0180  859  ARG A NH2 
6272  N N   . ILE A 862  ? 0.2426 0.2186 0.2534 -0.0114 -0.0042 0.0255  860  ILE A N   
6273  C CA  . ILE A 862  ? 0.2493 0.2201 0.2596 -0.0089 -0.0039 0.0219  860  ILE A CA  
6274  C C   . ILE A 862  ? 0.2446 0.2107 0.2591 -0.0085 -0.0060 0.0225  860  ILE A C   
6275  O O   . ILE A 862  ? 0.2224 0.1848 0.2370 -0.0064 -0.0059 0.0203  860  ILE A O   
6276  C CB  . ILE A 862  ? 0.2501 0.2213 0.2586 -0.0085 -0.0032 0.0196  860  ILE A CB  
6277  C CG1 . ILE A 862  ? 0.2747 0.2495 0.2794 -0.0081 -0.0011 0.0181  860  ILE A CG1 
6278  C CG2 . ILE A 862  ? 0.2765 0.2429 0.2852 -0.0062 -0.0034 0.0165  860  ILE A CG2 
6279  C CD1 . ILE A 862  ? 0.2985 0.2748 0.3018 -0.0080 -0.0005 0.0163  860  ILE A CD1 
6280  N N   . LEU A 863  ? 0.2332 0.1995 0.2516 -0.0106 -0.0080 0.0254  861  LEU A N   
6281  C CA  . LEU A 863  ? 0.2303 0.1920 0.2538 -0.0102 -0.0104 0.0258  861  LEU A CA  
6282  C C   . LEU A 863  ? 0.2430 0.2032 0.2682 -0.0096 -0.0109 0.0270  861  LEU A C   
6283  O O   . LEU A 863  ? 0.2480 0.2038 0.2754 -0.0076 -0.0118 0.0249  861  LEU A O   
6284  C CB  . LEU A 863  ? 0.2775 0.2402 0.3056 -0.0130 -0.0126 0.0294  861  LEU A CB  
6285  C CG  . LEU A 863  ? 0.3558 0.3134 0.3902 -0.0128 -0.0155 0.0292  861  LEU A CG  
6286  C CD1 . LEU A 863  ? 0.3215 0.2752 0.3549 -0.0100 -0.0152 0.0237  861  LEU A CD1 
6287  C CD2 . LEU A 863  ? 0.4254 0.3848 0.4637 -0.0158 -0.0173 0.0328  861  LEU A CD2 
6288  N N   . THR A 864  ? 0.2296 0.1938 0.2538 -0.0110 -0.0104 0.0302  862  THR A N   
6289  C CA  . THR A 864  ? 0.2456 0.2088 0.2709 -0.0103 -0.0107 0.0313  862  THR A CA  
6290  C C   . THR A 864  ? 0.2403 0.2012 0.2627 -0.0074 -0.0090 0.0271  862  THR A C   
6291  O O   . THR A 864  ? 0.2469 0.2044 0.2716 -0.0058 -0.0098 0.0261  862  THR A O   
6292  C CB  . THR A 864  ? 0.2617 0.2308 0.2855 -0.0123 -0.0101 0.0349  862  THR A CB  
6293  O OG1 . THR A 864  ? 0.2893 0.2609 0.3165 -0.0151 -0.0120 0.0395  862  THR A OG1 
6294  C CG2 . THR A 864  ? 0.2814 0.2498 0.3059 -0.0114 -0.0103 0.0357  862  THR A CG2 
6295  N N   . MET A 865  ? 0.2175 0.1804 0.2349 -0.0067 -0.0067 0.0247  863  MET A N   
6296  C CA  . MET A 865  ? 0.2224 0.1836 0.2373 -0.0041 -0.0050 0.0214  863  MET A CA  
6297  C C   . MET A 865  ? 0.2112 0.1682 0.2275 -0.0020 -0.0056 0.0183  863  MET A C   
6298  O O   . MET A 865  ? 0.2116 0.1666 0.2282 0.0000  -0.0054 0.0165  863  MET A O   
6299  C CB  . MET A 865  ? 0.2405 0.2046 0.2508 -0.0040 -0.0028 0.0198  863  MET A CB  
6300  C CG  . MET A 865  ? 0.2841 0.2472 0.2921 -0.0017 -0.0010 0.0171  863  MET A CG  
6301  S SD  . MET A 865  ? 0.3342 0.3005 0.3382 -0.0018 0.0011  0.0157  863  MET A SD  
6302  C CE  . MET A 865  ? 0.2850 0.2562 0.2894 -0.0047 0.0005  0.0187  863  MET A CE  
6303  N N   . LEU A 866  ? 0.2165 0.1726 0.2338 -0.0026 -0.0066 0.0177  864  LEU A N   
6304  C CA  . LEU A 866  ? 0.2280 0.1808 0.2466 -0.0005 -0.0073 0.0143  864  LEU A CA  
6305  C C   . LEU A 866  ? 0.2095 0.1591 0.2332 0.0003  -0.0095 0.0143  864  LEU A C   
6306  O O   . LEU A 866  ? 0.2313 0.1790 0.2553 0.0028  -0.0094 0.0111  864  LEU A O   
6307  C CB  . LEU A 866  ? 0.2263 0.1792 0.2456 -0.0016 -0.0082 0.0139  864  LEU A CB  
6308  C CG  . LEU A 866  ? 0.2879 0.2381 0.3087 0.0003  -0.0091 0.0102  864  LEU A CG  
6309  C CD1 . LEU A 866  ? 0.2916 0.2424 0.3079 0.0029  -0.0070 0.0069  864  LEU A CD1 
6310  C CD2 . LEU A 866  ? 0.2807 0.2311 0.3026 -0.0011 -0.0102 0.0102  864  LEU A CD2 
6311  N N   . LYS A 867  ? 0.2208 0.1700 0.2488 -0.0018 -0.0115 0.0179  865  LYS A N   
6312  C CA  . LYS A 867  ? 0.2405 0.1864 0.2741 -0.0011 -0.0138 0.0181  865  LYS A CA  
6313  C C   . LYS A 867  ? 0.2375 0.1834 0.2701 0.0007  -0.0128 0.0175  865  LYS A C   
6314  O O   . LYS A 867  ? 0.2462 0.1896 0.2818 0.0029  -0.0137 0.0150  865  LYS A O   
6315  C CB  . LYS A 867  ? 0.2337 0.1797 0.2723 -0.0039 -0.0162 0.0230  865  LYS A CB  
6316  C CG  . LYS A 867  ? 0.2738 0.2195 0.3147 -0.0057 -0.0176 0.0237  865  LYS A CG  
6317  C CD  . LYS A 867  ? 0.2898 0.2366 0.3355 -0.0088 -0.0198 0.0294  865  LYS A CD  
6318  C CE  . LYS A 867  ? 0.3287 0.2751 0.3773 -0.0105 -0.0213 0.0298  865  LYS A CE  
6319  N NZ  . LYS A 867  ? 0.3987 0.3478 0.4512 -0.0141 -0.0230 0.0361  865  LYS A NZ  
6320  N N   . GLY A 868  ? 0.2278 0.1770 0.2567 -0.0002 -0.0109 0.0195  866  GLY A N   
6321  C CA  . GLY A 868  ? 0.2387 0.1882 0.2665 0.0014  -0.0098 0.0189  866  GLY A CA  
6322  C C   . GLY A 868  ? 0.2205 0.1693 0.2457 0.0042  -0.0081 0.0145  866  GLY A C   
6323  O O   . GLY A 868  ? 0.2419 0.1895 0.2686 0.0062  -0.0082 0.0129  866  GLY A O   
6324  N N   . ALA A 869  ? 0.2130 0.1629 0.2344 0.0045  -0.0067 0.0126  867  ALA A N   
6325  C CA  . ALA A 869  ? 0.2242 0.1742 0.2430 0.0071  -0.0051 0.0090  867  ALA A CA  
6326  C C   . ALA A 869  ? 0.2193 0.1668 0.2415 0.0091  -0.0068 0.0058  867  ALA A C   
6327  O O   . ALA A 869  ? 0.2233 0.1711 0.2451 0.0116  -0.0061 0.0031  867  ALA A O   
6328  C CB  . ALA A 869  ? 0.2386 0.1903 0.2530 0.0068  -0.0035 0.0081  867  ALA A CB  
6329  N N   . LEU A 870  ? 0.2128 0.1582 0.2386 0.0080  -0.0091 0.0061  868  LEU A N   
6330  C CA  . LEU A 870  ? 0.2411 0.1842 0.2710 0.0098  -0.0111 0.0027  868  LEU A CA  
6331  C C   . LEU A 870  ? 0.2496 0.1914 0.2832 0.0116  -0.0120 0.0018  868  LEU A C   
6332  O O   . LEU A 870  ? 0.2594 0.2011 0.2941 0.0143  -0.0122 -0.0023 868  LEU A O   
6333  C CB  . LEU A 870  ? 0.2598 0.2005 0.2943 0.0078  -0.0138 0.0041  868  LEU A CB  
6334  C CG  . LEU A 870  ? 0.2970 0.2350 0.3367 0.0093  -0.0163 0.0004  868  LEU A CG  
6335  C CD1 . LEU A 870  ? 0.3245 0.2638 0.3609 0.0102  -0.0155 -0.0030 868  LEU A CD1 
6336  C CD2 . LEU A 870  ? 0.3269 0.2619 0.3736 0.0071  -0.0196 0.0031  868  LEU A CD2 
6337  N N   . HIS A 871  ? 0.2279 0.1692 0.2635 0.0101  -0.0126 0.0055  869  HIS A N   
6338  C CA  . HIS A 871  ? 0.2527 0.1927 0.2928 0.0116  -0.0138 0.0050  869  HIS A CA  
6339  C C   . HIS A 871  ? 0.2698 0.2122 0.3065 0.0139  -0.0115 0.0032  869  HIS A C   
6340  O O   . HIS A 871  ? 0.2807 0.2224 0.3208 0.0156  -0.0123 0.0021  869  HIS A O   
6341  C CB  . HIS A 871  ? 0.2851 0.2241 0.3289 0.0093  -0.0155 0.0099  869  HIS A CB  
6342  C CG  . HIS A 871  ? 0.3126 0.2489 0.3619 0.0075  -0.0185 0.0116  869  HIS A CG  
6343  N ND1 . HIS A 871  ? 0.3343 0.2671 0.3905 0.0089  -0.0214 0.0092  869  HIS A ND1 
6344  C CD2 . HIS A 871  ? 0.2841 0.2210 0.3335 0.0045  -0.0192 0.0153  869  HIS A CD2 
6345  C CE1 . HIS A 871  ? 0.3532 0.2841 0.4137 0.0067  -0.0238 0.0117  869  HIS A CE1 
6346  N NE2 . HIS A 871  ? 0.3281 0.2617 0.3845 0.0039  -0.0224 0.0156  869  HIS A NE2 
6347  N N   . GLU A 872  ? 0.2230 0.1682 0.2536 0.0139  -0.0087 0.0029  870  GLU A N   
6348  C CA  . GLU A 872  ? 0.2458 0.1936 0.2734 0.0159  -0.0064 0.0013  870  GLU A CA  
6349  C C   . GLU A 872  ? 0.2594 0.2086 0.2858 0.0187  -0.0058 -0.0032 870  GLU A C   
6350  O O   . GLU A 872  ? 0.2540 0.2061 0.2781 0.0205  -0.0038 -0.0045 870  GLU A O   
6351  C CB  . GLU A 872  ? 0.2298 0.1800 0.2522 0.0144  -0.0039 0.0038  870  GLU A CB  
6352  C CG  . GLU A 872  ? 0.2588 0.2090 0.2819 0.0119  -0.0043 0.0079  870  GLU A CG  
6353  C CD  . GLU A 872  ? 0.2960 0.2460 0.3222 0.0125  -0.0050 0.0089  870  GLU A CD  
6354  O OE1 . GLU A 872  ? 0.2930 0.2439 0.3195 0.0149  -0.0042 0.0066  870  GLU A OE1 
6355  O OE2 . GLU A 872  ? 0.2873 0.2368 0.3158 0.0106  -0.0064 0.0122  870  GLU A OE2 
6356  N N   . LEU A 873  ? 0.2367 0.1845 0.2650 0.0192  -0.0074 -0.0058 871  LEU A N   
6357  C CA  . LEU A 873  ? 0.2402 0.1901 0.2673 0.0219  -0.0069 -0.0104 871  LEU A CA  
6358  C C   . LEU A 873  ? 0.2429 0.1926 0.2747 0.0246  -0.0084 -0.0139 871  LEU A C   
6359  O O   . LEU A 873  ? 0.2718 0.2182 0.3094 0.0243  -0.0110 -0.0137 871  LEU A O   
6360  C CB  . LEU A 873  ? 0.2461 0.1947 0.2735 0.0213  -0.0083 -0.0121 871  LEU A CB  
6361  C CG  . LEU A 873  ? 0.2439 0.1930 0.2670 0.0189  -0.0069 -0.0091 871  LEU A CG  
6362  C CD1 . LEU A 873  ? 0.2849 0.2326 0.3091 0.0183  -0.0086 -0.0107 871  LEU A CD1 
6363  C CD2 . LEU A 873  ? 0.2919 0.2449 0.3092 0.0198  -0.0039 -0.0091 871  LEU A CD2 
6364  N N   . HIS A 874  ? 0.2385 0.1923 0.2679 0.0274  -0.0068 -0.0172 872  HIS A N   
6365  C CA  . HIS A 874  ? 0.2357 0.1908 0.2690 0.0305  -0.0079 -0.0215 872  HIS A CA  
6366  C C   . HIS A 874  ? 0.2431 0.1995 0.2771 0.0325  -0.0090 -0.0267 872  HIS A C   
6367  O O   . HIS A 874  ? 0.2483 0.2088 0.2774 0.0332  -0.0072 -0.0280 872  HIS A O   
6368  C CB  . HIS A 874  ? 0.2696 0.2298 0.2997 0.0322  -0.0051 -0.0215 872  HIS A CB  
6369  C CG  . HIS A 874  ? 0.2881 0.2508 0.3217 0.0356  -0.0058 -0.0259 872  HIS A CG  
6370  N ND1 . HIS A 874  ? 0.3635 0.3236 0.4035 0.0371  -0.0089 -0.0298 872  HIS A ND1 
6371  C CD2 . HIS A 874  ? 0.3675 0.3354 0.3996 0.0377  -0.0038 -0.0271 872  HIS A CD2 
6372  C CE1 . HIS A 874  ? 0.2932 0.2570 0.3353 0.0402  -0.0087 -0.0336 872  HIS A CE1 
6373  N NE2 . HIS A 874  ? 0.3788 0.3477 0.4160 0.0407  -0.0056 -0.0319 872  HIS A NE2 
6374  N N   . ILE A 875  ? 0.2472 0.2004 0.2878 0.0333  -0.0122 -0.0297 873  ILE A N   
6375  C CA  . ILE A 875  ? 0.2560 0.2101 0.2986 0.0353  -0.0140 -0.0353 873  ILE A CA  
6376  C C   . ILE A 875  ? 0.2706 0.2278 0.3166 0.0391  -0.0146 -0.0409 873  ILE A C   
6377  O O   . ILE A 875  ? 0.2783 0.2333 0.3296 0.0397  -0.0160 -0.0408 873  ILE A O   
6378  C CB  . ILE A 875  ? 0.2687 0.2168 0.3173 0.0334  -0.0175 -0.0350 873  ILE A CB  
6379  C CG1 . ILE A 875  ? 0.3005 0.2471 0.3452 0.0301  -0.0167 -0.0309 873  ILE A CG1 
6380  C CG2 . ILE A 875  ? 0.3055 0.2540 0.3582 0.0359  -0.0199 -0.0417 873  ILE A CG2 
6381  C CD1 . ILE A 875  ? 0.3331 0.2790 0.3739 0.0272  -0.0146 -0.0244 873  ILE A CD1 
6382  N N   . GLY A 876  ? 0.2566 0.2196 0.2997 0.0418  -0.0136 -0.0456 874  GLY A N   
6383  C CA  . GLY A 876  ? 0.2388 0.2059 0.2852 0.0457  -0.0143 -0.0516 874  GLY A CA  
6384  C C   . GLY A 876  ? 0.2505 0.2254 0.2922 0.0484  -0.0127 -0.0562 874  GLY A C   
6385  O O   . GLY A 876  ? 0.2561 0.2328 0.2927 0.0472  -0.0115 -0.0549 874  GLY A O   
6386  N N   . ARG A 877  ? 0.2629 0.2431 0.3070 0.0521  -0.0130 -0.0617 875  ARG A N   
6387  C CA  . ARG A 877  ? 0.2749 0.2644 0.3145 0.0549  -0.0112 -0.0660 875  ARG A CA  
6388  C C   . ARG A 877  ? 0.2602 0.2543 0.2916 0.0536  -0.0072 -0.0605 875  ARG A C   
6389  O O   . ARG A 877  ? 0.2615 0.2548 0.2917 0.0523  -0.0054 -0.0557 875  ARG A O   
6390  C CB  . ARG A 877  ? 0.2958 0.2908 0.3393 0.0591  -0.0118 -0.0722 875  ARG A CB  
6391  C CG  . ARG A 877  ? 0.2955 0.2999 0.3363 0.0624  -0.0112 -0.0785 875  ARG A CG  
6392  C CD  . ARG A 877  ? 0.3492 0.3590 0.3947 0.0666  -0.0121 -0.0853 875  ARG A CD  
6393  N NE  . ARG A 877  ? 0.3105 0.3276 0.3520 0.0677  -0.0087 -0.0829 875  ARG A NE  
6394  C CZ  . ARG A 877  ? 0.3545 0.3785 0.3987 0.0714  -0.0086 -0.0881 875  ARG A CZ  
6395  N NH1 . ARG A 877  ? 0.3879 0.4120 0.4390 0.0745  -0.0118 -0.0961 875  ARG A NH1 
6396  N NH2 . ARG A 877  ? 0.4040 0.4351 0.4443 0.0720  -0.0053 -0.0852 875  ARG A NH2 
6397  N N   . THR A 878  ? 0.2759 0.2747 0.3019 0.0537  -0.0059 -0.0610 876  THR A N   
6398  C CA  . THR A 878  ? 0.2503 0.2513 0.2694 0.0516  -0.0028 -0.0548 876  THR A CA  
6399  C C   . THR A 878  ? 0.2663 0.2765 0.2813 0.0534  0.0004  -0.0540 876  THR A C   
6400  O O   . THR A 878  ? 0.2631 0.2759 0.2728 0.0519  0.0029  -0.0490 876  THR A O   
6401  C CB  . THR A 878  ? 0.2551 0.2566 0.2707 0.0506  -0.0030 -0.0549 876  THR A CB  
6402  O OG1 . THR A 878  ? 0.2970 0.3049 0.3130 0.0539  -0.0040 -0.0618 876  THR A OG1 
6403  C CG2 . THR A 878  ? 0.3121 0.3042 0.3310 0.0478  -0.0055 -0.0536 876  THR A CG2 
6404  N N   . ASP A 879  ? 0.2550 0.2704 0.2727 0.0566  0.0002  -0.0585 877  ASP A N   
6405  C CA  . ASP A 879  ? 0.2988 0.3233 0.3131 0.0581  0.0033  -0.0572 877  ASP A CA  
6406  C C   . ASP A 879  ? 0.2645 0.2860 0.2794 0.0563  0.0048  -0.0516 877  ASP A C   
6407  O O   . ASP A 879  ? 0.2577 0.2859 0.2723 0.0580  0.0066  -0.0516 877  ASP A O   
6408  C CB  . ASP A 879  ? 0.2563 0.2894 0.2728 0.0625  0.0027  -0.0646 877  ASP A CB  
6409  C CG  . ASP A 879  ? 0.3527 0.3813 0.3766 0.0640  0.0002  -0.0687 877  ASP A CG  
6410  O OD1 . ASP A 879  ? 0.3579 0.3763 0.3861 0.0620  -0.0022 -0.0676 877  ASP A OD1 
6411  O OD2 . ASP A 879  ? 0.3365 0.3722 0.3622 0.0672  0.0007  -0.0727 877  ASP A OD2 
6412  N N   . ARG A 880  ? 0.2694 0.2817 0.2853 0.0530  0.0041  -0.0470 878  ARG A N   
6413  C CA  . ARG A 880  ? 0.2565 0.2659 0.2723 0.0508  0.0056  -0.0413 878  ARG A CA  
6414  C C   . ARG A 880  ? 0.2460 0.2514 0.2580 0.0473  0.0066  -0.0355 878  ARG A C   
6415  O O   . ARG A 880  ? 0.2420 0.2418 0.2543 0.0457  0.0050  -0.0355 878  ARG A O   
6416  C CB  . ARG A 880  ? 0.3060 0.3079 0.3279 0.0503  0.0032  -0.0418 878  ARG A CB  
6417  C CG  . ARG A 880  ? 0.3437 0.3490 0.3706 0.0537  0.0021  -0.0471 878  ARG A CG  
6418  C CD  . ARG A 880  ? 0.3988 0.3960 0.4319 0.0528  -0.0004 -0.0465 878  ARG A CD  
6419  N NE  . ARG A 880  ? 0.5417 0.5413 0.5806 0.0562  -0.0020 -0.0522 878  ARG A NE  
6420  C CZ  . ARG A 880  ? 0.5475 0.5481 0.5892 0.0571  -0.0016 -0.0515 878  ARG A CZ  
6421  N NH1 . ARG A 880  ? 0.5779 0.5772 0.6174 0.0547  0.0002  -0.0453 878  ARG A NH1 
6422  N NH2 . ARG A 880  ? 0.6064 0.6094 0.6536 0.0605  -0.0033 -0.0573 878  ARG A NH2 
6423  N N   . LEU A 881  ? 0.2369 0.2451 0.2457 0.0461  0.0093  -0.0305 879  LEU A N   
6424  C CA  . LEU A 881  ? 0.2409 0.2456 0.2466 0.0429  0.0103  -0.0251 879  LEU A CA  
6425  C C   . LEU A 881  ? 0.2337 0.2291 0.2419 0.0402  0.0086  -0.0232 879  LEU A C   
6426  O O   . LEU A 881  ? 0.2446 0.2363 0.2510 0.0379  0.0084  -0.0208 879  LEU A O   
6427  C CB  . LEU A 881  ? 0.2396 0.2485 0.2432 0.0421  0.0131  -0.0204 879  LEU A CB  
6428  C CG  . LEU A 881  ? 0.2474 0.2538 0.2481 0.0391  0.0143  -0.0151 879  LEU A CG  
6429  C CD1 . LEU A 881  ? 0.2689 0.2781 0.2661 0.0395  0.0145  -0.0156 879  LEU A CD1 
6430  C CD2 . LEU A 881  ? 0.2944 0.3047 0.2946 0.0385  0.0166  -0.0108 879  LEU A CD2 
6431  N N   . SER A 882  ? 0.2343 0.2264 0.2469 0.0404  0.0072  -0.0241 880  SER A N   
6432  C CA  . SER A 882  ? 0.2281 0.2123 0.2431 0.0378  0.0055  -0.0216 880  SER A CA  
6433  C C   . SER A 882  ? 0.2764 0.2558 0.2934 0.0373  0.0029  -0.0240 880  SER A C   
6434  O O   . SER A 882  ? 0.2687 0.2423 0.2875 0.0349  0.0015  -0.0216 880  SER A O   
6435  C CB  . SER A 882  ? 0.2489 0.2315 0.2683 0.0383  0.0047  -0.0216 880  SER A CB  
6436  O OG  . SER A 882  ? 0.2964 0.2802 0.3198 0.0412  0.0029  -0.0269 880  SER A OG  
6437  N N   . VAL A 883  ? 0.2546 0.2369 0.2715 0.0395  0.0021  -0.0286 881  VAL A N   
6438  C CA  . VAL A 883  ? 0.2448 0.2225 0.2643 0.0390  -0.0006 -0.0309 881  VAL A CA  
6439  C C   . VAL A 883  ? 0.2594 0.2359 0.2747 0.0367  0.0001  -0.0283 881  VAL A C   
6440  O O   . VAL A 883  ? 0.2921 0.2734 0.3029 0.0373  0.0020  -0.0281 881  VAL A O   
6441  C CB  . VAL A 883  ? 0.2632 0.2443 0.2851 0.0423  -0.0021 -0.0376 881  VAL A CB  
6442  C CG1 . VAL A 883  ? 0.2497 0.2268 0.2736 0.0415  -0.0047 -0.0399 881  VAL A CG1 
6443  C CG2 . VAL A 883  ? 0.2715 0.2520 0.2991 0.0442  -0.0036 -0.0404 881  VAL A CG2 
6444  N N   . ASP A 884  ? 0.2430 0.2133 0.2601 0.0341  -0.0015 -0.0261 882  ASP A N   
6445  C CA  . ASP A 884  ? 0.2495 0.2185 0.2635 0.0319  -0.0011 -0.0238 882  ASP A CA  
6446  C C   . ASP A 884  ? 0.2765 0.2448 0.2917 0.0325  -0.0031 -0.0275 882  ASP A C   
6447  O O   . ASP A 884  ? 0.3110 0.2814 0.3225 0.0322  -0.0023 -0.0275 882  ASP A O   
6448  C CB  . ASP A 884  ? 0.2531 0.2166 0.2683 0.0286  -0.0017 -0.0194 882  ASP A CB  
6449  C CG  . ASP A 884  ? 0.2557 0.2198 0.2698 0.0279  0.0001  -0.0158 882  ASP A CG  
6450  O OD1 . ASP A 884  ? 0.2795 0.2472 0.2896 0.0281  0.0025  -0.0143 882  ASP A OD1 
6451  O OD2 . ASP A 884  ? 0.2547 0.2159 0.2724 0.0271  -0.0011 -0.0145 882  ASP A OD2 
6452  N N   . VAL A 885  ? 0.2509 0.2161 0.2717 0.0333  -0.0059 -0.0307 883  VAL A N   
6453  C CA  . VAL A 885  ? 0.2598 0.2234 0.2832 0.0334  -0.0083 -0.0340 883  VAL A CA  
6454  C C   . VAL A 885  ? 0.2521 0.2178 0.2795 0.0368  -0.0101 -0.0403 883  VAL A C   
6455  O O   . VAL A 885  ? 0.2518 0.2155 0.2840 0.0376  -0.0113 -0.0412 883  VAL A O   
6456  C CB  . VAL A 885  ? 0.2779 0.2348 0.3056 0.0304  -0.0106 -0.0313 883  VAL A CB  
6457  C CG1 . VAL A 885  ? 0.2790 0.2341 0.3101 0.0306  -0.0134 -0.0349 883  VAL A CG1 
6458  C CG2 . VAL A 885  ? 0.2895 0.2452 0.3131 0.0273  -0.0089 -0.0256 883  VAL A CG2 
6459  N N   . GLY A 886  ? 0.2512 0.2212 0.2769 0.0387  -0.0102 -0.0448 884  GLY A N   
6460  C CA  . GLY A 886  ? 0.2438 0.2168 0.2731 0.0422  -0.0119 -0.0515 884  GLY A CA  
6461  C C   . GLY A 886  ? 0.2483 0.2167 0.2843 0.0420  -0.0158 -0.0553 884  GLY A C   
6462  O O   . GLY A 886  ? 0.2443 0.2063 0.2831 0.0391  -0.0174 -0.0520 884  GLY A O   
6463  N N   . PRO A 887  ? 0.2535 0.2253 0.2924 0.0453  -0.0174 -0.0623 885  PRO A N   
6464  C CA  . PRO A 887  ? 0.2456 0.2130 0.2920 0.0455  -0.0215 -0.0667 885  PRO A CA  
6465  C C   . PRO A 887  ? 0.2453 0.2128 0.2897 0.0442  -0.0222 -0.0673 885  PRO A C   
6466  O O   . PRO A 887  ? 0.2369 0.2089 0.2741 0.0439  -0.0197 -0.0656 885  PRO A O   
6467  C CB  . PRO A 887  ? 0.2444 0.2173 0.2938 0.0500  -0.0226 -0.0748 885  PRO A CB  
6468  C CG  . PRO A 887  ? 0.2622 0.2444 0.3031 0.0517  -0.0189 -0.0749 885  PRO A CG  
6469  C CD  . PRO A 887  ? 0.2679 0.2486 0.3035 0.0490  -0.0157 -0.0668 885  PRO A CD  
6470  N N   . VAL A 888  ? 0.2457 0.2080 0.2973 0.0434  -0.0259 -0.0697 886  VAL A N   
6471  C CA  . VAL A 888  ? 0.2433 0.2066 0.2945 0.0431  -0.0273 -0.0727 886  VAL A CA  
6472  C C   . VAL A 888  ? 0.2567 0.2264 0.3090 0.0474  -0.0284 -0.0815 886  VAL A C   
6473  O O   . VAL A 888  ? 0.2651 0.2368 0.3210 0.0503  -0.0292 -0.0858 886  VAL A O   
6474  C CB  . VAL A 888  ? 0.2649 0.2203 0.3233 0.0402  -0.0308 -0.0712 886  VAL A CB  
6475  C CG1 . VAL A 888  ? 0.2713 0.2221 0.3277 0.0361  -0.0293 -0.0624 886  VAL A CG1 
6476  C CG2 . VAL A 888  ? 0.3192 0.2704 0.3880 0.0415  -0.0347 -0.0753 886  VAL A CG2 
6477  N N   . ILE A 889  ? 0.2509 0.2248 0.3000 0.0479  -0.0285 -0.0843 887  ILE A N   
6478  C CA  . ILE A 889  ? 0.2737 0.2566 0.3207 0.0520  -0.0283 -0.0917 887  ILE A CA  
6479  C C   . ILE A 889  ? 0.3037 0.2858 0.3597 0.0548  -0.0323 -0.1002 887  ILE A C   
6480  O O   . ILE A 889  ? 0.2836 0.2728 0.3395 0.0586  -0.0321 -0.1062 887  ILE A O   
6481  C CB  . ILE A 889  ? 0.2809 0.2691 0.3215 0.0518  -0.0272 -0.0921 887  ILE A CB  
6482  C CG1 . ILE A 889  ? 0.2589 0.2581 0.2960 0.0560  -0.0264 -0.0987 887  ILE A CG1 
6483  C CG2 . ILE A 889  ? 0.2679 0.2507 0.3136 0.0497  -0.0306 -0.0934 887  ILE A CG2 
6484  C CD1 . ILE A 889  ? 0.2781 0.2837 0.3100 0.0578  -0.0229 -0.0969 887  ILE A CD1 
6485  N N   . THR A 890  ? 0.2698 0.2439 0.3343 0.0529  -0.0362 -0.1008 888  THR A N   
6486  C CA  . THR A 890  ? 0.2521 0.2249 0.3263 0.0555  -0.0405 -0.1092 888  THR A CA  
6487  C C   . THR A 890  ? 0.2861 0.2482 0.3703 0.0528  -0.0438 -0.1062 888  THR A C   
6488  O O   . THR A 890  ? 0.2929 0.2492 0.3760 0.0488  -0.0431 -0.0982 888  THR A O   
6489  C CB  . THR A 890  ? 0.3003 0.2762 0.3758 0.0564  -0.0429 -0.1155 888  THR A CB  
6490  O OG1 . THR A 890  ? 0.3155 0.2855 0.3915 0.0523  -0.0437 -0.1103 888  THR A OG1 
6491  C CG2 . THR A 890  ? 0.3054 0.2928 0.3717 0.0593  -0.0400 -0.1190 888  THR A CG2 
6492  N N   . SER A 891  ? 0.3003 0.2603 0.3945 0.0552  -0.0478 -0.1129 889  SER A N   
6493  C CA  A SER A 891  ? 0.3375 0.2875 0.4427 0.0528  -0.0517 -0.1107 889  SER A CA  
6494  C CA  B SER A 891  ? 0.3375 0.2874 0.4426 0.0528  -0.0516 -0.1105 889  SER A CA  
6495  C C   . SER A 891  ? 0.3438 0.2888 0.4519 0.0493  -0.0539 -0.1083 889  SER A C   
6496  O O   . SER A 891  ? 0.3418 0.2791 0.4550 0.0456  -0.0554 -0.1019 889  SER A O   
6497  C CB  A SER A 891  ? 0.3506 0.2997 0.4669 0.0565  -0.0559 -0.1195 889  SER A CB  
6498  C CB  B SER A 891  ? 0.3509 0.2998 0.4670 0.0564  -0.0557 -0.1190 889  SER A CB  
6499  O OG  A SER A 891  ? 0.3397 0.2932 0.4544 0.0597  -0.0540 -0.1217 889  SER A OG  
6500  O OG  B SER A 891  ? 0.3940 0.3474 0.5125 0.0590  -0.0580 -0.1282 889  SER A OG  
6501  N N   . GLU A 892  ? 0.3131 0.2631 0.4183 0.0504  -0.0542 -0.1133 890  GLU A N   
6502  C CA  . GLU A 892  ? 0.3344 0.2803 0.4423 0.0471  -0.0563 -0.1113 890  GLU A CA  
6503  C C   . GLU A 892  ? 0.3306 0.2749 0.4306 0.0429  -0.0529 -0.1012 890  GLU A C   
6504  O O   . GLU A 892  ? 0.3460 0.2841 0.4503 0.0390  -0.0545 -0.0960 890  GLU A O   
6505  C CB  . GLU A 892  ? 0.3744 0.3269 0.4803 0.0493  -0.0572 -0.1191 890  GLU A CB  
6506  C CG  . GLU A 892  ? 0.4364 0.3922 0.5493 0.0539  -0.0605 -0.1303 890  GLU A CG  
6507  C CD  . GLU A 892  ? 0.4984 0.4642 0.6034 0.0583  -0.0572 -0.1347 890  GLU A CD  
6508  O OE1 . GLU A 892  ? 0.4366 0.4024 0.5415 0.0595  -0.0557 -0.1332 890  GLU A OE1 
6509  O OE2 . GLU A 892  ? 0.6348 0.6092 0.7338 0.0604  -0.0561 -0.1395 890  GLU A OE2 
6510  N N   . ALA A 893  ? 0.3209 0.2713 0.4097 0.0437  -0.0482 -0.0985 891  ALA A N   
6511  C CA  . ALA A 893  ? 0.3154 0.2643 0.3969 0.0400  -0.0448 -0.0893 891  ALA A CA  
6512  C C   . ALA A 893  ? 0.3455 0.2874 0.4313 0.0373  -0.0452 -0.0825 891  ALA A C   
6513  O O   . ALA A 893  ? 0.3324 0.2698 0.4188 0.0333  -0.0453 -0.0759 891  ALA A O   
6514  C CB  . ALA A 893  ? 0.3004 0.2570 0.3703 0.0416  -0.0401 -0.0881 891  ALA A CB  
6515  N N   . LYS A 894  ? 0.2960 0.2372 0.3852 0.0394  -0.0455 -0.0841 892  LYS A N   
6516  C CA  . LYS A 894  ? 0.3012 0.2361 0.3953 0.0371  -0.0463 -0.0780 892  LYS A CA  
6517  C C   . LYS A 894  ? 0.3482 0.2757 0.4527 0.0342  -0.0507 -0.0764 892  LYS A C   
6518  O O   . LYS A 894  ? 0.3363 0.2596 0.4417 0.0304  -0.0505 -0.0686 892  LYS A O   
6519  C CB  . LYS A 894  ? 0.2804 0.2160 0.3779 0.0404  -0.0466 -0.0815 892  LYS A CB  
6520  C CG  . LYS A 894  ? 0.3060 0.2350 0.4102 0.0385  -0.0481 -0.0761 892  LYS A CG  
6521  C CD  . LYS A 894  ? 0.3322 0.2632 0.4378 0.0419  -0.0476 -0.0793 892  LYS A CD  
6522  C CE  . LYS A 894  ? 0.3681 0.2926 0.4813 0.0402  -0.0496 -0.0742 892  LYS A CE  
6523  N NZ  . LYS A 894  ? 0.5172 0.4439 0.6314 0.0436  -0.0489 -0.0772 892  LYS A NZ  
6524  N N   . ASP A 895  ? 0.3205 0.2470 0.4335 0.0361  -0.0547 -0.0837 893  ASP A N   
6525  C CA  . ASP A 895  ? 0.3685 0.2879 0.4927 0.0334  -0.0593 -0.0823 893  ASP A CA  
6526  C C   . ASP A 895  ? 0.3445 0.2631 0.4655 0.0292  -0.0586 -0.0767 893  ASP A C   
6527  O O   . ASP A 895  ? 0.3750 0.2882 0.5014 0.0254  -0.0603 -0.0702 893  ASP A O   
6528  C CB  . ASP A 895  ? 0.3508 0.2699 0.4841 0.0363  -0.0637 -0.0921 893  ASP A CB  
6529  C CG  . ASP A 895  ? 0.4218 0.3407 0.5614 0.0402  -0.0654 -0.0977 893  ASP A CG  
6530  O OD1 . ASP A 895  ? 0.4985 0.4155 0.6377 0.0399  -0.0641 -0.0930 893  ASP A OD1 
6531  O OD2 . ASP A 895  ? 0.4780 0.3987 0.6233 0.0436  -0.0683 -0.1072 893  ASP A OD2 
6532  N N   . ASN A 896  ? 0.3327 0.2569 0.4450 0.0300  -0.0562 -0.0789 894  ASN A N   
6533  C CA  . ASN A 896  ? 0.3399 0.2639 0.4489 0.0264  -0.0554 -0.0741 894  ASN A CA  
6534  C C   . ASN A 896  ? 0.3517 0.2746 0.4551 0.0230  -0.0522 -0.0644 894  ASN A C   
6535  O O   . ASN A 896  ? 0.3374 0.2571 0.4434 0.0191  -0.0530 -0.0585 894  ASN A O   
6536  C CB  . ASN A 896  ? 0.3719 0.3027 0.4723 0.0282  -0.0532 -0.0785 894  ASN A CB  
6537  C CG  . ASN A 896  ? 0.4537 0.3850 0.5499 0.0247  -0.0520 -0.0735 894  ASN A CG  
6538  O OD1 . ASN A 896  ? 0.5434 0.4771 0.6306 0.0235  -0.0481 -0.0680 894  ASN A OD1 
6539  N ND2 . ASN A 896  ? 0.4877 0.4167 0.5908 0.0232  -0.0555 -0.0754 894  ASN A ND2 
6540  N N   . ILE A 897  ? 0.3207 0.2466 0.4164 0.0245  -0.0485 -0.0627 895  ILE A N   
6541  C CA  . ILE A 897  ? 0.3191 0.2444 0.4093 0.0215  -0.0454 -0.0541 895  ILE A CA  
6542  C C   . ILE A 897  ? 0.3540 0.2733 0.4526 0.0190  -0.0479 -0.0490 895  ILE A C   
6543  O O   . ILE A 897  ? 0.3174 0.2351 0.4159 0.0152  -0.0475 -0.0418 895  ILE A O   
6544  C CB  . ILE A 897  ? 0.2957 0.2256 0.3768 0.0238  -0.0412 -0.0540 895  ILE A CB  
6545  C CG1 . ILE A 897  ? 0.2767 0.2129 0.3493 0.0259  -0.0387 -0.0578 895  ILE A CG1 
6546  C CG2 . ILE A 897  ? 0.3100 0.2391 0.3866 0.0209  -0.0385 -0.0457 895  ILE A CG2 
6547  C CD1 . ILE A 897  ? 0.2880 0.2293 0.3544 0.0293  -0.0357 -0.0603 895  ILE A CD1 
6548  N N   . GLU A 898  ? 0.3206 0.2372 0.4269 0.0211  -0.0505 -0.0524 896  GLU A N   
6549  C CA  . GLU A 898  ? 0.3665 0.2776 0.4814 0.0189  -0.0530 -0.0472 896  GLU A CA  
6550  C C   . GLU A 898  ? 0.3439 0.2507 0.4675 0.0155  -0.0568 -0.0446 896  GLU A C   
6551  O O   . GLU A 898  ? 0.3703 0.2741 0.4976 0.0120  -0.0576 -0.0371 896  GLU A O   
6552  C CB  . GLU A 898  ? 0.3645 0.2737 0.4861 0.0222  -0.0552 -0.0521 896  GLU A CB  
6553  C CG  . GLU A 898  ? 0.3759 0.2891 0.4894 0.0248  -0.0514 -0.0525 896  GLU A CG  
6554  C CD  . GLU A 898  ? 0.4280 0.3400 0.5480 0.0284  -0.0534 -0.0576 896  GLU A CD  
6555  O OE1 . GLU A 898  ? 0.5161 0.4254 0.6458 0.0299  -0.0575 -0.0633 896  GLU A OE1 
6556  O OE2 . GLU A 898  ? 0.5313 0.4453 0.6471 0.0297  -0.0508 -0.0561 896  GLU A OE2 
6557  N N   . LYS A 899  ? 0.3264 0.2332 0.4536 0.0164  -0.0592 -0.0505 897  LYS A N   
6558  C CA  . LYS A 899  ? 0.3406 0.2438 0.4761 0.0130  -0.0627 -0.0479 897  LYS A CA  
6559  C C   . LYS A 899  ? 0.3781 0.2831 0.5072 0.0088  -0.0600 -0.0399 897  LYS A C   
6560  O O   . LYS A 899  ? 0.3750 0.2771 0.5102 0.0050  -0.0619 -0.0334 897  LYS A O   
6561  C CB  . LYS A 899  ? 0.3738 0.2779 0.5126 0.0149  -0.0651 -0.0563 897  LYS A CB  
6562  N N   . HIS A 900  ? 0.3276 0.2379 0.4447 0.0096  -0.0556 -0.0401 898  HIS A N   
6563  C CA  . HIS A 900  ? 0.3405 0.2531 0.4512 0.0061  -0.0529 -0.0331 898  HIS A CA  
6564  C C   . HIS A 900  ? 0.3278 0.2392 0.4382 0.0037  -0.0517 -0.0251 898  HIS A C   
6565  O O   . HIS A 900  ? 0.3534 0.2644 0.4660 -0.0002 -0.0521 -0.0183 898  HIS A O   
6566  C CB  . HIS A 900  ? 0.3250 0.2433 0.4235 0.0079  -0.0485 -0.0353 898  HIS A CB  
6567  C CG  . HIS A 900  ? 0.3206 0.2415 0.4121 0.0048  -0.0454 -0.0285 898  HIS A CG  
6568  N ND1 . HIS A 900  ? 0.3433 0.2649 0.4356 0.0019  -0.0460 -0.0259 898  HIS A ND1 
6569  C CD2 . HIS A 900  ? 0.3410 0.2641 0.4249 0.0043  -0.0417 -0.0239 898  HIS A CD2 
6570  C CE1 . HIS A 900  ? 0.3382 0.2627 0.4237 -0.0002 -0.0428 -0.0203 898  HIS A CE1 
6571  N NE2 . HIS A 900  ? 0.3183 0.2437 0.3987 0.0012  -0.0402 -0.0191 898  HIS A NE2 
6572  N N   . ILE A 901  ? 0.3104 0.2220 0.4180 0.0061  -0.0501 -0.0258 899  ILE A N   
6573  C CA  . ILE A 901  ? 0.3336 0.2447 0.4406 0.0041  -0.0489 -0.0186 899  ILE A CA  
6574  C C   . ILE A 901  ? 0.3726 0.2791 0.4911 0.0012  -0.0530 -0.0139 899  ILE A C   
6575  O O   . ILE A 901  ? 0.3854 0.2924 0.5040 -0.0023 -0.0526 -0.0062 899  ILE A O   
6576  C CB  . ILE A 901  ? 0.2843 0.1962 0.3877 0.0074  -0.0470 -0.0210 899  ILE A CB  
6577  C CG1 . ILE A 901  ? 0.3160 0.2330 0.4077 0.0096  -0.0427 -0.0240 899  ILE A CG1 
6578  C CG2 . ILE A 901  ? 0.3356 0.2465 0.4398 0.0054  -0.0465 -0.0139 899  ILE A CG2 
6579  C CD1 . ILE A 901  ? 0.2991 0.2176 0.3877 0.0132  -0.0410 -0.0275 899  ILE A CD1 
6580  N N   . GLU A 902  ? 0.3720 0.2743 0.5006 0.0027  -0.0572 -0.0185 900  GLU A N   
6581  C CA  . GLU A 902  ? 0.4021 0.2995 0.5430 0.0001  -0.0616 -0.0140 900  GLU A CA  
6582  C C   . GLU A 902  ? 0.4046 0.3019 0.5492 -0.0041 -0.0632 -0.0095 900  GLU A C   
6583  O O   . GLU A 902  ? 0.4706 0.3665 0.6212 -0.0077 -0.0649 -0.0018 900  GLU A O   
6584  C CB  . GLU A 902  ? 0.4722 0.3650 0.6236 0.0031  -0.0658 -0.0206 900  GLU A CB  
6585  C CG  . GLU A 902  ? 0.4777 0.3706 0.6273 0.0066  -0.0646 -0.0235 900  GLU A CG  
6586  C CD  . GLU A 902  ? 0.5251 0.4183 0.6724 0.0045  -0.0629 -0.0151 900  GLU A CD  
6587  O OE1 . GLU A 902  ? 0.5668 0.4572 0.7220 0.0011  -0.0656 -0.0083 900  GLU A OE1 
6588  O OE2 . GLU A 902  ? 0.5213 0.4180 0.6591 0.0061  -0.0590 -0.0152 900  GLU A OE2 
6589  N N   . ARG A 903  ? 0.3982 0.2975 0.5398 -0.0036 -0.0627 -0.0139 901  ARG A N   
6590  C CA  . ARG A 903  ? 0.4303 0.3305 0.5739 -0.0076 -0.0635 -0.0095 901  ARG A CA  
6591  C C   . ARG A 903  ? 0.4818 0.3861 0.6183 -0.0109 -0.0602 -0.0008 901  ARG A C   
6592  O O   . ARG A 903  ? 0.5054 0.4093 0.6475 -0.0148 -0.0618 0.0065  901  ARG A O   
6593  C CB  . ARG A 903  ? 0.4460 0.3487 0.5853 -0.0062 -0.0628 -0.0159 901  ARG A CB  
6594  N N   . MET A 904  ? 0.4286 0.3370 0.5530 -0.0092 -0.0555 -0.0016 902  MET A N   
6595  C CA  . MET A 904  ? 0.3962 0.3088 0.5136 -0.0119 -0.0522 0.0057  902  MET A CA  
6596  C C   . MET A 904  ? 0.4402 0.3513 0.5630 -0.0138 -0.0536 0.0124  902  MET A C   
6597  O O   . MET A 904  ? 0.4376 0.3510 0.5615 -0.0176 -0.0535 0.0199  902  MET A O   
6598  C CB  . MET A 904  ? 0.3743 0.2909 0.4794 -0.0092 -0.0475 0.0029  902  MET A CB  
6599  C CG  . MET A 904  ? 0.3596 0.2786 0.4585 -0.0075 -0.0458 -0.0027 902  MET A CG  
6600  S SD  . MET A 904  ? 0.4870 0.4097 0.5843 -0.0114 -0.0452 0.0017  902  MET A SD  
6601  C CE  . MET A 904  ? 0.4893 0.4085 0.5963 -0.0115 -0.0497 -0.0029 902  MET A CE  
6602  N N   . ARG A 905  ? 0.4135 0.3213 0.5396 -0.0112 -0.0547 0.0099  903  ARG A N   
6603  C CA  . ARG A 905  ? 0.4361 0.3423 0.5676 -0.0128 -0.0562 0.0161  903  ARG A CA  
6604  C C   . ARG A 905  ? 0.5167 0.4201 0.6604 -0.0164 -0.0607 0.0213  903  ARG A C   
6605  O O   . ARG A 905  ? 0.4924 0.3972 0.6387 -0.0196 -0.0612 0.0296  903  ARG A O   
6606  C CB  . ARG A 905  ? 0.4504 0.3532 0.5843 -0.0090 -0.0571 0.0115  903  ARG A CB  
6607  C CG  . ARG A 905  ? 0.5024 0.4052 0.6375 -0.0099 -0.0570 0.0176  903  ARG A CG  
6608  C CD  . ARG A 905  ? 0.5024 0.4012 0.6428 -0.0064 -0.0589 0.0130  903  ARG A CD  
6609  N NE  . ARG A 905  ? 0.4783 0.3786 0.6108 -0.0021 -0.0560 0.0053  903  ARG A NE  
6610  C CZ  . ARG A 905  ? 0.4832 0.3867 0.6068 -0.0007 -0.0522 0.0056  903  ARG A CZ  
6611  N NH1 . ARG A 905  ? 0.4900 0.3958 0.6106 -0.0031 -0.0507 0.0127  903  ARG A NH1 
6612  N NH2 . ARG A 905  ? 0.4905 0.3954 0.6083 0.0032  -0.0501 -0.0014 903  ARG A NH2 
6613  N N   . GLY A 906  ? 0.4747 0.3744 0.6259 -0.0159 -0.0640 0.0167  904  GLY A N   
6614  C CA  . GLY A 906  ? 0.5201 0.4169 0.6838 -0.0194 -0.0686 0.0215  904  GLY A CA  
6615  C C   . GLY A 906  ? 0.5718 0.4733 0.7334 -0.0239 -0.0674 0.0286  904  GLY A C   
6616  O O   . GLY A 906  ? 0.5928 0.4937 0.7630 -0.0276 -0.0703 0.0359  904  GLY A O   
6617  N N   . LEU A 907  ? 0.5032 0.4096 0.6535 -0.0235 -0.0634 0.0266  905  LEU A N   
6618  C CA  . LEU A 907  ? 0.5124 0.4243 0.6595 -0.0274 -0.0618 0.0328  905  LEU A CA  
6619  C C   . LEU A 907  ? 0.5015 0.4184 0.6437 -0.0297 -0.0593 0.0409  905  LEU A C   
6620  O O   . LEU A 907  ? 0.5567 0.4791 0.6964 -0.0330 -0.0580 0.0465  905  LEU A O   
6621  C CB  . LEU A 907  ? 0.5017 0.4172 0.6390 -0.0260 -0.0585 0.0276  905  LEU A CB  
6622  C CG  . LEU A 907  ? 0.5467 0.4589 0.6881 -0.0243 -0.0608 0.0201  905  LEU A CG  
6623  C CD1 . LEU A 907  ? 0.5468 0.4635 0.6782 -0.0234 -0.0574 0.0164  905  LEU A CD1 
6624  C CD2 . LEU A 907  ? 0.6066 0.5160 0.7610 -0.0277 -0.0656 0.0234  905  LEU A CD2 
6625  N N   . GLY A 908  ? 0.4726 0.3882 0.6133 -0.0279 -0.0587 0.0413  906  GLY A N   
6626  C CA  . GLY A 908  ? 0.4923 0.4130 0.6282 -0.0297 -0.0563 0.0483  906  GLY A CA  
6627  C C   . GLY A 908  ? 0.4325 0.3579 0.5547 -0.0278 -0.0512 0.0457  906  GLY A C   
6628  O O   . GLY A 908  ? 0.4502 0.3807 0.5678 -0.0293 -0.0491 0.0511  906  GLY A O   
6629  N N   . ARG A 909  ? 0.4108 0.3351 0.5270 -0.0245 -0.0493 0.0378  907  ARG A N   
6630  C CA  . ARG A 909  ? 0.3452 0.2737 0.4493 -0.0226 -0.0447 0.0355  907  ARG A CA  
6631  C C   . ARG A 909  ? 0.3969 0.3242 0.4985 -0.0203 -0.0436 0.0348  907  ARG A C   
6632  O O   . ARG A 909  ? 0.4104 0.3325 0.5179 -0.0183 -0.0460 0.0322  907  ARG A O   
6633  C CB  . ARG A 909  ? 0.3483 0.2759 0.4474 -0.0198 -0.0433 0.0276  907  ARG A CB  
6634  C CG  . ARG A 909  ? 0.4062 0.3343 0.5088 -0.0217 -0.0449 0.0272  907  ARG A CG  
6635  C CD  . ARG A 909  ? 0.4360 0.3706 0.5341 -0.0249 -0.0427 0.0326  907  ARG A CD  
6636  N NE  . ARG A 909  ? 0.4654 0.4009 0.5653 -0.0262 -0.0436 0.0312  907  ARG A NE  
6637  C CZ  . ARG A 909  ? 0.5619 0.4978 0.6697 -0.0297 -0.0463 0.0358  907  ARG A CZ  
6638  N NH1 . ARG A 909  ? 0.5544 0.4899 0.6693 -0.0325 -0.0485 0.0425  907  ARG A NH1 
6639  N NH2 . ARG A 909  ? 0.5107 0.4476 0.6194 -0.0306 -0.0469 0.0338  907  ARG A NH2 
6640  N N   . LYS A 910  ? 0.3221 0.2542 0.4152 -0.0205 -0.0401 0.0371  908  LYS A N   
6641  C CA  . LYS A 910  ? 0.3377 0.2693 0.4279 -0.0184 -0.0388 0.0365  908  LYS A CA  
6642  C C   . LYS A 910  ? 0.3413 0.2703 0.4271 -0.0141 -0.0373 0.0285  908  LYS A C   
6643  O O   . LYS A 910  ? 0.3175 0.2486 0.3963 -0.0130 -0.0348 0.0249  908  LYS A O   
6644  C CB  . LYS A 910  ? 0.3637 0.3016 0.4461 -0.0198 -0.0355 0.0406  908  LYS A CB  
6645  C CG  . LYS A 910  ? 0.4492 0.3906 0.5357 -0.0235 -0.0369 0.0489  908  LYS A CG  
6646  C CD  . LYS A 910  ? 0.4630 0.4110 0.5415 -0.0243 -0.0336 0.0518  908  LYS A CD  
6647  C CE  . LYS A 910  ? 0.4875 0.4339 0.5617 -0.0212 -0.0319 0.0485  908  LYS A CE  
6648  N NZ  . LYS A 910  ? 0.5893 0.5420 0.6579 -0.0223 -0.0296 0.0522  908  LYS A NZ  
6649  N N   . VAL A 911  ? 0.3299 0.2548 0.4198 -0.0118 -0.0389 0.0261  909  VAL A N   
6650  C CA  . VAL A 911  ? 0.3212 0.2441 0.4083 -0.0076 -0.0379 0.0186  909  VAL A CA  
6651  C C   . VAL A 911  ? 0.3117 0.2352 0.3956 -0.0059 -0.0362 0.0189  909  VAL A C   
6652  O O   . VAL A 911  ? 0.3384 0.2600 0.4282 -0.0064 -0.0382 0.0222  909  VAL A O   
6653  C CB  . VAL A 911  ? 0.3333 0.2510 0.4295 -0.0060 -0.0417 0.0142  909  VAL A CB  
6654  C CG1 . VAL A 911  ? 0.3689 0.2857 0.4618 -0.0016 -0.0406 0.0062  909  VAL A CG1 
6655  C CG2 . VAL A 911  ? 0.3452 0.2623 0.4453 -0.0081 -0.0436 0.0141  909  VAL A CG2 
6656  N N   . GLU A 912  ? 0.2926 0.2187 0.3677 -0.0038 -0.0326 0.0158  910  GLU A N   
6657  C CA  . GLU A 912  ? 0.3041 0.2311 0.3757 -0.0019 -0.0308 0.0152  910  GLU A CA  
6658  C C   . GLU A 912  ? 0.3291 0.2545 0.3997 0.0021  -0.0304 0.0081  910  GLU A C   
6659  O O   . GLU A 912  ? 0.2917 0.2184 0.3581 0.0034  -0.0290 0.0040  910  GLU A O   
6660  C CB  . GLU A 912  ? 0.3157 0.2475 0.3781 -0.0027 -0.0269 0.0173  910  GLU A CB  
6661  C CG  . GLU A 912  ? 0.3109 0.2440 0.3701 -0.0013 -0.0251 0.0176  910  GLU A CG  
6662  C CD  . GLU A 912  ? 0.3615 0.2948 0.4247 -0.0033 -0.0265 0.0234  910  GLU A CD  
6663  O OE1 . GLU A 912  ? 0.3638 0.2974 0.4310 -0.0063 -0.0284 0.0279  910  GLU A OE1 
6664  O OE2 . GLU A 912  ? 0.3781 0.3117 0.4405 -0.0021 -0.0258 0.0237  910  GLU A OE2 
6665  N N   . GLN A 913  ? 0.3094 0.2327 0.3842 0.0042  -0.0316 0.0065  911  GLN A N   
6666  C CA  . GLN A 913  ? 0.3281 0.2509 0.4023 0.0082  -0.0313 -0.0004 911  GLN A CA  
6667  C C   . GLN A 913  ? 0.3720 0.2958 0.4444 0.0101  -0.0298 -0.0005 911  GLN A C   
6668  O O   . GLN A 913  ? 0.3589 0.2814 0.4351 0.0090  -0.0310 0.0036  911  GLN A O   
6669  C CB  . GLN A 913  ? 0.3303 0.2489 0.4138 0.0095  -0.0352 -0.0042 911  GLN A CB  
6670  C CG  . GLN A 913  ? 0.3618 0.2793 0.4477 0.0080  -0.0369 -0.0051 911  GLN A CG  
6671  C CD  . GLN A 913  ? 0.3759 0.2898 0.4703 0.0100  -0.0406 -0.0107 911  GLN A CD  
6672  O OE1 . GLN A 913  ? 0.3895 0.2996 0.4932 0.0098  -0.0440 -0.0095 911  GLN A OE1 
6673  N NE2 . GLN A 913  ? 0.3462 0.2615 0.4381 0.0121  -0.0401 -0.0169 911  GLN A NE2 
6674  N N   . ILE A 914  ? 0.3380 0.2643 0.4046 0.0129  -0.0272 -0.0050 912  ILE A N   
6675  C CA  . ILE A 914  ? 0.3184 0.2459 0.3840 0.0152  -0.0259 -0.0060 912  ILE A CA  
6676  C C   . ILE A 914  ? 0.3501 0.2745 0.4242 0.0175  -0.0291 -0.0096 912  ILE A C   
6677  O O   . ILE A 914  ? 0.3509 0.2733 0.4297 0.0186  -0.0315 -0.0137 912  ILE A O   
6678  C CB  . ILE A 914  ? 0.4133 0.3449 0.4710 0.0175  -0.0224 -0.0096 912  ILE A CB  
6679  N N   . GLY A 915  ? 0.3710 0.2950 0.4476 0.0183  -0.0294 -0.0081 913  GLY A N   
6680  C CA  . GLY A 915  ? 0.3744 0.2960 0.4589 0.0210  -0.0322 -0.0120 913  GLY A CA  
6681  C C   . GLY A 915  ? 0.3595 0.2845 0.4406 0.0250  -0.0303 -0.0186 913  GLY A C   
6682  O O   . GLY A 915  ? 0.4317 0.3607 0.5054 0.0257  -0.0268 -0.0183 913  GLY A O   
6683  N N   . LEU A 916  ? 0.3539 0.2777 0.4406 0.0277  -0.0327 -0.0248 914  LEU A N   
6684  C CA  . LEU A 916  ? 0.3912 0.3193 0.4751 0.0316  -0.0311 -0.0316 914  LEU A CA  
6685  C C   . LEU A 916  ? 0.4152 0.3437 0.5036 0.0344  -0.0319 -0.0338 914  LEU A C   
6686  O O   . LEU A 916  ? 0.4200 0.3442 0.5170 0.0342  -0.0351 -0.0328 914  LEU A O   
6687  C CB  . LEU A 916  ? 0.3783 0.3058 0.4656 0.0333  -0.0333 -0.0379 914  LEU A CB  
6688  C CG  . LEU A 916  ? 0.3917 0.3195 0.4746 0.0310  -0.0327 -0.0368 914  LEU A CG  
6689  C CD1 . LEU A 916  ? 0.4295 0.3576 0.5160 0.0332  -0.0349 -0.0439 914  LEU A CD1 
6690  C CD2 . LEU A 916  ? 0.4364 0.3692 0.5083 0.0306  -0.0281 -0.0348 914  LEU A CD2 
6691  N N   . ALA A 917  ? 0.3499 0.2839 0.4328 0.0370  -0.0288 -0.0367 915  ALA A N   
6692  C CA  . ALA A 917  ? 0.3639 0.2994 0.4506 0.0401  -0.0292 -0.0396 915  ALA A CA  
6693  C C   . ALA A 917  ? 0.3972 0.3318 0.4920 0.0434  -0.0326 -0.0471 915  ALA A C   
6694  O O   . ALA A 917  ? 0.3969 0.3319 0.4919 0.0441  -0.0335 -0.0514 915  ALA A O   
6695  C CB  . ALA A 917  ? 0.4006 0.3430 0.4793 0.0420  -0.0251 -0.0409 915  ALA A CB  
6696  N N   . SER A 918  ? 0.3944 0.3280 0.4963 0.0457  -0.0345 -0.0491 916  SER A N   
6697  C CA  . SER A 918  ? 0.4233 0.3563 0.5338 0.0492  -0.0379 -0.0569 916  SER A CA  
6698  C C   . SER A 918  ? 0.3725 0.3126 0.4782 0.0527  -0.0359 -0.0644 916  SER A C   
6699  O O   . SER A 918  ? 0.3809 0.3209 0.4918 0.0550  -0.0386 -0.0713 916  SER A O   
6700  C CB  . SER A 918  ? 0.4125 0.3443 0.5306 0.0513  -0.0397 -0.0576 916  SER A CB  
6701  O OG  . SER A 918  ? 0.5039 0.4413 0.6156 0.0525  -0.0359 -0.0566 916  SER A OG  
6702  N N   . GLU A 919  ? 0.3984 0.3450 0.4945 0.0532  -0.0315 -0.0632 917  GLU A N   
6703  C CA  . GLU A 919  ? 0.3917 0.3465 0.4827 0.0564  -0.0293 -0.0695 917  GLU A CA  
6704  C C   . GLU A 919  ? 0.4010 0.3561 0.4894 0.0557  -0.0298 -0.0720 917  GLU A C   
6705  O O   . GLU A 919  ? 0.3699 0.3312 0.4564 0.0588  -0.0293 -0.0787 917  GLU A O   
6706  C CB  . GLU A 919  ? 0.4166 0.3776 0.4979 0.0561  -0.0245 -0.0659 917  GLU A CB  
6707  C CG  . GLU A 919  ? 0.4569 0.4208 0.5399 0.0580  -0.0235 -0.0659 917  GLU A CG  
6708  C CD  . GLU A 919  ? 0.5410 0.4989 0.6268 0.0551  -0.0242 -0.0589 917  GLU A CD  
6709  O OE1 . GLU A 919  ? 0.4968 0.4482 0.5839 0.0517  -0.0257 -0.0542 917  GLU A OE1 
6710  O OE2 . GLU A 919  ? 0.5933 0.5534 0.6800 0.0563  -0.0232 -0.0579 917  GLU A OE2 
6711  N N   . THR A 920  ? 0.3524 0.3016 0.4405 0.0519  -0.0308 -0.0669 918  THR A N   
6712  C CA  . THR A 920  ? 0.3180 0.2674 0.4041 0.0512  -0.0314 -0.0693 918  THR A CA  
6713  C C   . THR A 920  ? 0.3393 0.2865 0.4346 0.0534  -0.0358 -0.0766 918  THR A C   
6714  O O   . THR A 920  ? 0.3255 0.2746 0.4194 0.0539  -0.0364 -0.0806 918  THR A O   
6715  C CB  . THR A 920  ? 0.3397 0.2839 0.4234 0.0464  -0.0312 -0.0618 918  THR A CB  
6716  O OG1 . THR A 920  ? 0.3399 0.2765 0.4322 0.0444  -0.0347 -0.0586 918  THR A OG1 
6717  C CG2 . THR A 920  ? 0.3255 0.2722 0.4002 0.0444  -0.0270 -0.0553 918  THR A CG2 
6718  N N   . GLY A 921  ? 0.3722 0.3157 0.4773 0.0549  -0.0390 -0.0788 919  GLY A N   
6719  C CA  . GLY A 921  ? 0.3511 0.2916 0.4664 0.0569  -0.0436 -0.0857 919  GLY A CA  
6720  C C   . GLY A 921  ? 0.3354 0.2835 0.4493 0.0612  -0.0435 -0.0954 919  GLY A C   
6721  O O   . GLY A 921  ? 0.3890 0.3356 0.5089 0.0623  -0.0468 -0.1013 919  GLY A O   
6722  N N   . VAL A 922  ? 0.3273 0.2840 0.4334 0.0637  -0.0396 -0.0972 920  VAL A N   
6723  C CA  . VAL A 922  ? 0.3068 0.2723 0.4111 0.0679  -0.0392 -0.1062 920  VAL A CA  
6724  C C   . VAL A 922  ? 0.3337 0.3031 0.4300 0.0668  -0.0375 -0.1064 920  VAL A C   
6725  O O   . VAL A 922  ? 0.3424 0.3192 0.4373 0.0700  -0.0375 -0.1139 920  VAL A O   
6726  C CB  . VAL A 922  ? 0.3282 0.3027 0.4280 0.0711  -0.0359 -0.1082 920  VAL A CB  
6727  C CG1 . VAL A 922  ? 0.3326 0.3044 0.4417 0.0734  -0.0383 -0.1107 920  VAL A CG1 
6728  C CG2 . VAL A 922  ? 0.3436 0.3201 0.4332 0.0683  -0.0312 -0.0995 920  VAL A CG2 
6729  N N   . GLY A 923  ? 0.3000 0.2653 0.3911 0.0624  -0.0359 -0.0984 921  GLY A N   
6730  C CA  . GLY A 923  ? 0.3076 0.2757 0.3921 0.0611  -0.0347 -0.0982 921  GLY A CA  
6731  C C   . GLY A 923  ? 0.2856 0.2452 0.3740 0.0574  -0.0374 -0.0948 921  GLY A C   
6732  O O   . GLY A 923  ? 0.3303 0.2824 0.4281 0.0564  -0.0410 -0.0943 921  GLY A O   
6733  N N   . THR A 924  ? 0.2804 0.2414 0.3622 0.0553  -0.0358 -0.0923 922  THR A N   
6734  C CA  . THR A 924  ? 0.2858 0.2398 0.3706 0.0517  -0.0381 -0.0890 922  THR A CA  
6735  C C   . THR A 924  ? 0.2985 0.2506 0.3759 0.0477  -0.0349 -0.0796 922  THR A C   
6736  O O   . THR A 924  ? 0.2872 0.2438 0.3561 0.0471  -0.0320 -0.0780 922  THR A O   
6737  C CB  . THR A 924  ? 0.2789 0.2359 0.3636 0.0528  -0.0396 -0.0950 922  THR A CB  
6738  O OG1 . THR A 924  ? 0.2632 0.2291 0.3376 0.0542  -0.0359 -0.0960 922  THR A OG1 
6739  C CG2 . THR A 924  ? 0.3146 0.2723 0.4086 0.0565  -0.0435 -0.1045 922  THR A CG2 
6740  N N   . PHE A 925  ? 0.2667 0.2125 0.3476 0.0450  -0.0355 -0.0734 923  PHE A N   
6741  C CA  . PHE A 925  ? 0.2543 0.1986 0.3289 0.0414  -0.0326 -0.0649 923  PHE A CA  
6742  C C   . PHE A 925  ? 0.2866 0.2239 0.3659 0.0374  -0.0350 -0.0600 923  PHE A C   
6743  O O   . PHE A 925  ? 0.3005 0.2325 0.3894 0.0370  -0.0389 -0.0610 923  PHE A O   
6744  C CB  . PHE A 925  ? 0.2663 0.2108 0.3397 0.0415  -0.0307 -0.0610 923  PHE A CB  
6745  C CG  . PHE A 925  ? 0.2866 0.2386 0.3541 0.0447  -0.0276 -0.0640 923  PHE A CG  
6746  C CD1 . PHE A 925  ? 0.2800 0.2353 0.3517 0.0487  -0.0288 -0.0709 923  PHE A CD1 
6747  C CD2 . PHE A 925  ? 0.2394 0.1956 0.2975 0.0437  -0.0235 -0.0598 923  PHE A CD2 
6748  C CE1 . PHE A 925  ? 0.2802 0.2434 0.3466 0.0516  -0.0259 -0.0733 923  PHE A CE1 
6749  C CE2 . PHE A 925  ? 0.2615 0.2250 0.3146 0.0465  -0.0207 -0.0620 923  PHE A CE2 
6750  C CZ  . PHE A 925  ? 0.2559 0.2231 0.3129 0.0504  -0.0217 -0.0685 923  PHE A CZ  
6751  N N   . VAL A 926  ? 0.2777 0.2153 0.3504 0.0343  -0.0327 -0.0545 924  VAL A N   
6752  C CA  . VAL A 926  ? 0.2798 0.2121 0.3552 0.0302  -0.0340 -0.0483 924  VAL A CA  
6753  C C   . VAL A 926  ? 0.2771 0.2101 0.3461 0.0280  -0.0307 -0.0412 924  VAL A C   
6754  O O   . VAL A 926  ? 0.2611 0.1987 0.3216 0.0285  -0.0272 -0.0406 924  VAL A O   
6755  C CB  . VAL A 926  ? 0.2900 0.2226 0.3639 0.0285  -0.0346 -0.0488 924  VAL A CB  
6756  C CG1 . VAL A 926  ? 0.2969 0.2252 0.3729 0.0241  -0.0355 -0.0418 924  VAL A CG1 
6757  C CG2 . VAL A 926  ? 0.3042 0.2362 0.3850 0.0307  -0.0382 -0.0562 924  VAL A CG2 
6758  N N   . PRO A 927  ? 0.2815 0.2106 0.3545 0.0256  -0.0317 -0.0358 925  PRO A N   
6759  C CA  . PRO A 927  ? 0.2916 0.2219 0.3587 0.0236  -0.0287 -0.0296 925  PRO A CA  
6760  C C   . PRO A 927  ? 0.2857 0.2171 0.3469 0.0208  -0.0269 -0.0259 925  PRO A C   
6761  O O   . PRO A 927  ? 0.2784 0.2077 0.3429 0.0189  -0.0289 -0.0254 925  PRO A O   
6762  C CB  . PRO A 927  ? 0.3397 0.2654 0.4138 0.0217  -0.0311 -0.0251 925  PRO A CB  
6763  C CG  . PRO A 927  ? 0.3388 0.2603 0.4218 0.0211  -0.0353 -0.0269 925  PRO A CG  
6764  C CD  . PRO A 927  ? 0.3105 0.2340 0.3940 0.0245  -0.0359 -0.0350 925  PRO A CD  
6765  N N   . PRO A 928  ? 0.2867 0.2216 0.3397 0.0205  -0.0233 -0.0235 926  PRO A N   
6766  C CA  . PRO A 928  ? 0.2526 0.1884 0.3008 0.0176  -0.0216 -0.0193 926  PRO A CA  
6767  C C   . PRO A 928  ? 0.2487 0.1811 0.3018 0.0141  -0.0237 -0.0143 926  PRO A C   
6768  O O   . PRO A 928  ? 0.2641 0.1944 0.3210 0.0133  -0.0248 -0.0113 926  PRO A O   
6769  C CB  . PRO A 928  ? 0.2780 0.2169 0.3193 0.0178  -0.0180 -0.0169 926  PRO A CB  
6770  C CG  . PRO A 928  ? 0.2873 0.2288 0.3275 0.0215  -0.0172 -0.0217 926  PRO A CG  
6771  C CD  . PRO A 928  ? 0.3027 0.2412 0.3510 0.0229  -0.0205 -0.0249 926  PRO A CD  
6772  N N   . THR A 929  ? 0.2581 0.1902 0.3112 0.0121  -0.0244 -0.0132 927  THR A N   
6773  C CA  . THR A 929  ? 0.2876 0.2169 0.3464 0.0088  -0.0269 -0.0090 927  THR A CA  
6774  C C   . THR A 929  ? 0.2820 0.2137 0.3358 0.0061  -0.0251 -0.0052 927  THR A C   
6775  O O   . THR A 929  ? 0.2691 0.2032 0.3178 0.0068  -0.0234 -0.0075 927  THR A O   
6776  C CB  . THR A 929  ? 0.3134 0.2397 0.3795 0.0093  -0.0305 -0.0127 927  THR A CB  
6777  O OG1 . THR A 929  ? 0.2935 0.2178 0.3648 0.0122  -0.0323 -0.0168 927  THR A OG1 
6778  C CG2 . THR A 929  ? 0.2907 0.2144 0.3633 0.0057  -0.0332 -0.0079 927  THR A CG2 
6779  N N   . ILE A 930  ? 0.2670 0.1987 0.3223 0.0030  -0.0254 0.0007  928  ILE A N   
6780  C CA  . ILE A 930  ? 0.2885 0.2230 0.3403 0.0001  -0.0241 0.0045  928  ILE A CA  
6781  C C   . ILE A 930  ? 0.2851 0.2178 0.3441 -0.0028 -0.0272 0.0079  928  ILE A C   
6782  O O   . ILE A 930  ? 0.3068 0.2373 0.3717 -0.0039 -0.0293 0.0111  928  ILE A O   
6783  C CB  . ILE A 930  ? 0.2562 0.1936 0.3030 -0.0011 -0.0215 0.0086  928  ILE A CB  
6784  C CG1 . ILE A 930  ? 0.2919 0.2312 0.3320 0.0016  -0.0184 0.0056  928  ILE A CG1 
6785  C CG2 . ILE A 930  ? 0.3118 0.2525 0.3561 -0.0041 -0.0205 0.0125  928  ILE A CG2 
6786  C CD1 . ILE A 930  ? 0.3043 0.2459 0.3409 0.0008  -0.0164 0.0091  928  ILE A CD1 
6787  N N   . ILE A 931  ? 0.2970 0.2305 0.3559 -0.0041 -0.0276 0.0074  929  ILE A N   
6788  C CA  . ILE A 931  ? 0.2705 0.2028 0.3364 -0.0071 -0.0305 0.0106  929  ILE A CA  
6789  C C   . ILE A 931  ? 0.2994 0.2362 0.3612 -0.0099 -0.0287 0.0148  929  ILE A C   
6790  O O   . ILE A 931  ? 0.2891 0.2284 0.3451 -0.0093 -0.0266 0.0124  929  ILE A O   
6791  C CB  . ILE A 931  ? 0.3214 0.2509 0.3921 -0.0060 -0.0330 0.0058  929  ILE A CB  
6792  C CG1 . ILE A 931  ? 0.3021 0.2278 0.3771 -0.0028 -0.0349 0.0009  929  ILE A CG1 
6793  C CG2 . ILE A 931  ? 0.3262 0.2545 0.4045 -0.0093 -0.0361 0.0095  929  ILE A CG2 
6794  C CD1 . ILE A 931  ? 0.3253 0.2484 0.4061 -0.0016 -0.0378 -0.0044 929  ILE A CD1 
6795  N N   . GLU A 932  ? 0.3194 0.2577 0.3843 -0.0131 -0.0296 0.0210  930  GLU A N   
6796  C CA  . GLU A 932  ? 0.2992 0.2427 0.3607 -0.0159 -0.0280 0.0251  930  GLU A CA  
6797  C C   . GLU A 932  ? 0.2895 0.2329 0.3565 -0.0182 -0.0304 0.0263  930  GLU A C   
6798  O O   . GLU A 932  ? 0.3160 0.2569 0.3914 -0.0200 -0.0336 0.0292  930  GLU A O   
6799  C CB  . GLU A 932  ? 0.3118 0.2585 0.3732 -0.0180 -0.0275 0.0312  930  GLU A CB  
6800  C CG  . GLU A 932  ? 0.3083 0.2559 0.3636 -0.0159 -0.0249 0.0297  930  GLU A CG  
6801  C CD  . GLU A 932  ? 0.3831 0.3330 0.4394 -0.0176 -0.0250 0.0352  930  GLU A CD  
6802  O OE1 . GLU A 932  ? 0.3683 0.3232 0.4245 -0.0206 -0.0248 0.0401  930  GLU A OE1 
6803  O OE2 . GLU A 932  ? 0.3585 0.3059 0.4159 -0.0160 -0.0254 0.0347  930  GLU A OE2 
6804  N N   . LEU A 933  ? 0.3233 0.2692 0.3862 -0.0181 -0.0289 0.0240  931  LEU A N   
6805  C CA  . LEU A 933  ? 0.3113 0.2573 0.3788 -0.0201 -0.0309 0.0245  931  LEU A CA  
6806  C C   . LEU A 933  ? 0.3973 0.3495 0.4636 -0.0236 -0.0298 0.0302  931  LEU A C   
6807  O O   . LEU A 933  ? 0.3567 0.3134 0.4167 -0.0238 -0.0270 0.0319  931  LEU A O   
6808  C CB  . LEU A 933  ? 0.3663 0.3117 0.4304 -0.0178 -0.0302 0.0184  931  LEU A CB  
6809  C CG  . LEU A 933  ? 0.3690 0.3098 0.4342 -0.0142 -0.0312 0.0121  931  LEU A CG  
6810  C CD1 . LEU A 933  ? 0.4199 0.3614 0.4821 -0.0125 -0.0307 0.0068  931  LEU A CD1 
6811  C CD2 . LEU A 933  ? 0.3988 0.3346 0.4739 -0.0148 -0.0352 0.0123  931  LEU A CD2 
6812  N N   . GLU A 934  ? 0.3975 0.3501 0.4703 -0.0264 -0.0323 0.0329  932  GLU A N   
6813  C CA  . GLU A 934  ? 0.4817 0.4408 0.5539 -0.0297 -0.0314 0.0379  932  GLU A CA  
6814  C C   . GLU A 934  ? 0.4979 0.4599 0.5651 -0.0290 -0.0296 0.0343  932  GLU A C   
6815  O O   . GLU A 934  ? 0.5565 0.5245 0.6179 -0.0297 -0.0269 0.0357  932  GLU A O   
6816  C CB  . GLU A 934  ? 0.5092 0.4677 0.5913 -0.0333 -0.0350 0.0432  932  GLU A CB  
6817  N N   . LYS A 935  ? 0.4968 0.4548 0.5660 -0.0274 -0.0310 0.0293  933  LYS A N   
6818  C CA  . LYS A 935  ? 0.5143 0.4747 0.5793 -0.0265 -0.0296 0.0257  933  LYS A CA  
6819  C C   . LYS A 935  ? 0.5223 0.4783 0.5847 -0.0226 -0.0295 0.0186  933  LYS A C   
6820  O O   . LYS A 935  ? 0.5140 0.4649 0.5805 -0.0212 -0.0316 0.0163  933  LYS A O   
6821  C CB  . LYS A 935  ? 0.5271 0.4886 0.5986 -0.0294 -0.0320 0.0275  933  LYS A CB  
6822  N N   . LEU A 936  ? 0.5010 0.4596 0.5568 -0.0209 -0.0271 0.0153  934  LEU A N   
6823  C CA  . LEU A 936  ? 0.4983 0.4541 0.5514 -0.0173 -0.0270 0.0089  934  LEU A CA  
6824  C C   . LEU A 936  ? 0.5413 0.4938 0.6011 -0.0173 -0.0304 0.0058  934  LEU A C   
6825  O O   . LEU A 936  ? 0.5472 0.4965 0.6071 -0.0144 -0.0313 0.0006  934  LEU A O   
6826  C CB  . LEU A 936  ? 0.4941 0.4538 0.5396 -0.0158 -0.0241 0.0066  934  LEU A CB  
6827  N N   . SER A 937  ? 0.5791 0.5326 0.6449 -0.0205 -0.0324 0.0089  935  SER A N   
6828  C CA  . SER A 937  ? 0.5269 0.4771 0.6002 -0.0209 -0.0361 0.0063  935  SER A CA  
6829  C C   . SER A 937  ? 0.5217 0.4662 0.6023 -0.0205 -0.0391 0.0057  935  SER A C   
6830  O O   . SER A 937  ? 0.5478 0.4889 0.6349 -0.0201 -0.0423 0.0021  935  SER A O   
6831  C CB  . SER A 937  ? 0.5428 0.4960 0.6211 -0.0248 -0.0375 0.0104  935  SER A CB  
6832  O OG  . SER A 937  ? 0.5770 0.5317 0.6586 -0.0280 -0.0377 0.0175  935  SER A OG  
6833  N N   . ASP A 938  ? 0.5218 0.4652 0.6018 -0.0205 -0.0383 0.0088  936  ASP A N   
6834  C CA  . ASP A 938  ? 0.5275 0.4655 0.6140 -0.0195 -0.0410 0.0076  936  ASP A CA  
6835  C C   . ASP A 938  ? 0.5354 0.4707 0.6202 -0.0153 -0.0414 -0.0003 936  ASP A C   
6836  O O   . ASP A 938  ? 0.5096 0.4404 0.6013 -0.0142 -0.0444 -0.0030 936  ASP A O   
6837  C CB  . ASP A 938  ? 0.5590 0.4971 0.6438 -0.0199 -0.0397 0.0120  936  ASP A CB  
6838  C CG  . ASP A 938  ? 0.5878 0.5294 0.6749 -0.0241 -0.0396 0.0200  936  ASP A CG  
6839  O OD1 . ASP A 938  ? 0.6155 0.5587 0.7070 -0.0268 -0.0412 0.0224  936  ASP A OD1 
6840  O OD2 . ASP A 938  ? 0.5676 0.5107 0.6522 -0.0246 -0.0381 0.0240  936  ASP A OD2 
6841  N N   . LEU A 939  ? 0.4990 0.4372 0.5750 -0.0128 -0.0384 -0.0039 937  LEU A N   
6842  C CA  . LEU A 939  ? 0.4932 0.4302 0.5668 -0.0088 -0.0384 -0.0111 937  LEU A CA  
6843  C C   . LEU A 939  ? 0.5423 0.4798 0.6183 -0.0084 -0.0403 -0.0156 937  LEU A C   
6844  O O   . LEU A 939  ? 0.5514 0.4919 0.6258 -0.0103 -0.0397 -0.0139 937  LEU A O   
6845  C CB  . LEU A 939  ? 0.4370 0.3773 0.5002 -0.0064 -0.0343 -0.0122 937  LEU A CB  
6846  C CG  . LEU A 939  ? 0.4463 0.3862 0.5065 -0.0061 -0.0323 -0.0091 937  LEU A CG  
6847  C CD1 . LEU A 939  ? 0.4391 0.3815 0.4905 -0.0030 -0.0289 -0.0119 937  LEU A CD1 
6848  C CD2 . LEU A 939  ? 0.4464 0.3818 0.5136 -0.0054 -0.0350 -0.0100 937  LEU A CD2 
6849  N N   . GLN A 940  ? 0.4785 0.4135 0.5583 -0.0058 -0.0427 -0.0218 938  GLN A N   
6850  C CA  . GLN A 940  ? 0.5101 0.4458 0.5924 -0.0050 -0.0448 -0.0270 938  GLN A CA  
6851  C C   . GLN A 940  ? 0.5457 0.4850 0.6198 -0.0012 -0.0425 -0.0327 938  GLN A C   
6852  O O   . GLN A 940  ? 0.6383 0.5815 0.7067 -0.0012 -0.0406 -0.0326 938  GLN A O   
6853  C CB  . GLN A 940  ? 0.5273 0.4583 0.6205 -0.0048 -0.0495 -0.0306 938  GLN A CB  
6854  N N   . ARG A 941  ? 0.4823 0.4206 0.5559 0.0022  -0.0428 -0.0374 939  ARG A N   
6855  C CA  . ARG A 941  ? 0.4479 0.3903 0.5143 0.0059  -0.0408 -0.0425 939  ARG A CA  
6856  C C   . ARG A 941  ? 0.3691 0.3120 0.4299 0.0080  -0.0379 -0.0416 939  ARG A C   
6857  O O   . ARG A 941  ? 0.3834 0.3231 0.4469 0.0069  -0.0380 -0.0380 939  ARG A O   
6858  C CB  . ARG A 941  ? 0.4580 0.4003 0.5291 0.0086  -0.0440 -0.0505 939  ARG A CB  
6859  N N   . GLU A 942  ? 0.3232 0.2705 0.3764 0.0109  -0.0355 -0.0445 940  GLU A N   
6860  C CA  . GLU A 942  ? 0.3124 0.2610 0.3603 0.0131  -0.0327 -0.0441 940  GLU A CA  
6861  C C   . GLU A 942  ? 0.3118 0.2571 0.3656 0.0145  -0.0347 -0.0466 940  GLU A C   
6862  O O   . GLU A 942  ? 0.3246 0.2691 0.3840 0.0161  -0.0378 -0.0522 940  GLU A O   
6863  C CB  . GLU A 942  ? 0.3081 0.2624 0.3490 0.0163  -0.0308 -0.0482 940  GLU A CB  
6864  C CG  . GLU A 942  ? 0.2836 0.2401 0.3190 0.0187  -0.0281 -0.0481 940  GLU A CG  
6865  C CD  . GLU A 942  ? 0.2929 0.2555 0.3229 0.0220  -0.0269 -0.0525 940  GLU A CD  
6866  O OE1 . GLU A 942  ? 0.3505 0.3147 0.3837 0.0240  -0.0293 -0.0586 940  GLU A OE1 
6867  O OE2 . GLU A 942  ? 0.2705 0.2366 0.2934 0.0226  -0.0237 -0.0499 940  GLU A OE2 
6868  N N   . VAL A 943  ? 0.2942 0.2376 0.3469 0.0139  -0.0331 -0.0426 941  VAL A N   
6869  C CA  . VAL A 943  ? 0.2824 0.2232 0.3397 0.0156  -0.0345 -0.0445 941  VAL A CA  
6870  C C   . VAL A 943  ? 0.3091 0.2536 0.3590 0.0184  -0.0312 -0.0455 941  VAL A C   
6871  O O   . VAL A 943  ? 0.2748 0.2201 0.3197 0.0174  -0.0283 -0.0406 941  VAL A O   
6872  C CB  . VAL A 943  ? 0.2916 0.2276 0.3543 0.0126  -0.0355 -0.0388 941  VAL A CB  
6873  C CG1 . VAL A 943  ? 0.2944 0.2278 0.3615 0.0145  -0.0368 -0.0406 941  VAL A CG1 
6874  C CG2 . VAL A 943  ? 0.3532 0.2860 0.4236 0.0096  -0.0389 -0.0373 941  VAL A CG2 
6875  N N   . PHE A 944  ? 0.2946 0.2422 0.3441 0.0220  -0.0317 -0.0519 942  PHE A N   
6876  C CA  . PHE A 944  ? 0.2822 0.2351 0.3242 0.0248  -0.0285 -0.0532 942  PHE A CA  
6877  C C   . PHE A 944  ? 0.2843 0.2357 0.3283 0.0261  -0.0282 -0.0531 942  PHE A C   
6878  O O   . PHE A 944  ? 0.2943 0.2475 0.3405 0.0292  -0.0292 -0.0586 942  PHE A O   
6879  C CB  . PHE A 944  ? 0.2513 0.2096 0.2916 0.0279  -0.0291 -0.0600 942  PHE A CB  
6880  C CG  . PHE A 944  ? 0.2479 0.2128 0.2795 0.0300  -0.0256 -0.0599 942  PHE A CG  
6881  C CD1 . PHE A 944  ? 0.2324 0.1992 0.2576 0.0285  -0.0230 -0.0554 942  PHE A CD1 
6882  C CD2 . PHE A 944  ? 0.2409 0.2105 0.2710 0.0336  -0.0249 -0.0643 942  PHE A CD2 
6883  C CE1 . PHE A 944  ? 0.2158 0.1886 0.2338 0.0303  -0.0200 -0.0548 942  PHE A CE1 
6884  C CE2 . PHE A 944  ? 0.2523 0.2286 0.2747 0.0354  -0.0217 -0.0636 942  PHE A CE2 
6885  C CZ  . PHE A 944  ? 0.2484 0.2260 0.2649 0.0337  -0.0194 -0.0587 942  PHE A CZ  
6886  N N   . GLY A 945  ? 0.2593 0.2078 0.3026 0.0238  -0.0268 -0.0470 943  GLY A N   
6887  C CA  . GLY A 945  ? 0.2678 0.2145 0.3132 0.0247  -0.0266 -0.0461 943  GLY A CA  
6888  C C   . GLY A 945  ? 0.2664 0.2115 0.3086 0.0221  -0.0242 -0.0390 943  GLY A C   
6889  O O   . GLY A 945  ? 0.2676 0.2136 0.3055 0.0199  -0.0226 -0.0352 943  GLY A O   
6890  N N   . PRO A 946  ? 0.2372 0.1804 0.2814 0.0223  -0.0241 -0.0373 944  PRO A N   
6891  C CA  . PRO A 946  ? 0.2492 0.1920 0.2898 0.0203  -0.0217 -0.0311 944  PRO A CA  
6892  C C   . PRO A 946  ? 0.2504 0.1890 0.2953 0.0166  -0.0233 -0.0261 944  PRO A C   
6893  O O   . PRO A 946  ? 0.2654 0.2015 0.3138 0.0156  -0.0240 -0.0230 944  PRO A O   
6894  C CB  . PRO A 946  ? 0.2334 0.1766 0.2750 0.0225  -0.0211 -0.0323 944  PRO A CB  
6895  C CG  . PRO A 946  ? 0.2677 0.2084 0.3174 0.0242  -0.0248 -0.0372 944  PRO A CG  
6896  C CD  . PRO A 946  ? 0.2583 0.2005 0.3082 0.0249  -0.0261 -0.0416 944  PRO A CD  
6897  N N   . VAL A 947  ? 0.2577 0.1963 0.3025 0.0146  -0.0239 -0.0249 945  VAL A N   
6898  C CA  . VAL A 947  ? 0.2709 0.2064 0.3203 0.0110  -0.0257 -0.0204 945  VAL A CA  
6899  C C   . VAL A 947  ? 0.2733 0.2113 0.3171 0.0087  -0.0234 -0.0165 945  VAL A C   
6900  O O   . VAL A 947  ? 0.2771 0.2170 0.3187 0.0087  -0.0232 -0.0183 945  VAL A O   
6901  C CB  . VAL A 947  ? 0.2989 0.2316 0.3562 0.0106  -0.0296 -0.0231 945  VAL A CB  
6902  C CG1 . VAL A 947  ? 0.2962 0.2261 0.3588 0.0067  -0.0314 -0.0174 945  VAL A CG1 
6903  C CG2 . VAL A 947  ? 0.2884 0.2190 0.3515 0.0134  -0.0319 -0.0281 945  VAL A CG2 
6904  N N   . LEU A 948  ? 0.2529 0.1913 0.2946 0.0068  -0.0218 -0.0114 946  LEU A N   
6905  C CA  . LEU A 948  ? 0.2566 0.1976 0.2935 0.0047  -0.0197 -0.0078 946  LEU A CA  
6906  C C   . LEU A 948  ? 0.2588 0.1987 0.3005 0.0011  -0.0216 -0.0035 946  LEU A C   
6907  O O   . LEU A 948  ? 0.2895 0.2272 0.3359 -0.0001 -0.0232 -0.0006 946  LEU A O   
6908  C CB  . LEU A 948  ? 0.2464 0.1892 0.2782 0.0048  -0.0169 -0.0052 946  LEU A CB  
6909  C CG  . LEU A 948  ? 0.2546 0.2003 0.2822 0.0026  -0.0149 -0.0017 946  LEU A CG  
6910  C CD1 . LEU A 948  ? 0.2552 0.2033 0.2785 0.0036  -0.0136 -0.0042 946  LEU A CD1 
6911  C CD2 . LEU A 948  ? 0.2781 0.2252 0.3021 0.0027  -0.0126 0.0007  946  LEU A CD2 
6912  N N   . HIS A 949  ? 0.2488 0.1905 0.2895 -0.0005 -0.0215 -0.0028 947  HIS A N   
6913  C CA  . HIS A 949  ? 0.2484 0.1903 0.2930 -0.0040 -0.0229 0.0018  947  HIS A CA  
6914  C C   . HIS A 949  ? 0.2787 0.2247 0.3177 -0.0057 -0.0201 0.0055  947  HIS A C   
6915  O O   . HIS A 949  ? 0.2680 0.2164 0.3008 -0.0043 -0.0176 0.0037  947  HIS A O   
6916  C CB  . HIS A 949  ? 0.2488 0.1902 0.2969 -0.0048 -0.0250 -0.0001 947  HIS A CB  
6917  C CG  . HIS A 949  ? 0.2789 0.2167 0.3322 -0.0028 -0.0277 -0.0049 947  HIS A CG  
6918  N ND1 . HIS A 949  ? 0.2812 0.2196 0.3313 0.0006  -0.0270 -0.0107 947  HIS A ND1 
6919  C CD2 . HIS A 949  ? 0.2957 0.2297 0.3576 -0.0035 -0.0313 -0.0049 947  HIS A CD2 
6920  C CE1 . HIS A 949  ? 0.2935 0.2289 0.3498 0.0019  -0.0300 -0.0146 947  HIS A CE1 
6921  N NE2 . HIS A 949  ? 0.3127 0.2451 0.3766 -0.0005 -0.0327 -0.0113 947  HIS A NE2 
6922  N N   . VAL A 950  ? 0.2589 0.2059 0.3003 -0.0085 -0.0207 0.0107  948  VAL A N   
6923  C CA  . VAL A 950  ? 0.2745 0.2261 0.3112 -0.0101 -0.0182 0.0141  948  VAL A CA  
6924  C C   . VAL A 950  ? 0.2995 0.2539 0.3390 -0.0134 -0.0193 0.0178  948  VAL A C   
6925  O O   . VAL A 950  ? 0.2956 0.2485 0.3415 -0.0155 -0.0219 0.0208  948  VAL A O   
6926  C CB  . VAL A 950  ? 0.2777 0.2296 0.3138 -0.0103 -0.0175 0.0170  948  VAL A CB  
6927  C CG1 . VAL A 950  ? 0.2995 0.2567 0.3313 -0.0121 -0.0153 0.0202  948  VAL A CG1 
6928  C CG2 . VAL A 950  ? 0.2803 0.2300 0.3137 -0.0071 -0.0164 0.0133  948  VAL A CG2 
6929  N N   . ILE A 951  ? 0.2636 0.2221 0.2987 -0.0140 -0.0174 0.0177  949  ILE A N   
6930  C CA  . ILE A 951  ? 0.2774 0.2399 0.3143 -0.0171 -0.0178 0.0213  949  ILE A CA  
6931  C C   . ILE A 951  ? 0.3106 0.2788 0.3424 -0.0178 -0.0151 0.0234  949  ILE A C   
6932  O O   . ILE A 951  ? 0.2770 0.2456 0.3034 -0.0157 -0.0128 0.0208  949  ILE A O   
6933  C CB  . ILE A 951  ? 0.3179 0.2808 0.3552 -0.0170 -0.0183 0.0187  949  ILE A CB  
6934  N N   . ARG A 952  ? 0.2785 0.2514 0.3122 -0.0209 -0.0155 0.0281  950  ARG A N   
6935  C CA  . ARG A 952  ? 0.2711 0.2503 0.3003 -0.0217 -0.0131 0.0298  950  ARG A CA  
6936  C C   . ARG A 952  ? 0.2551 0.2395 0.2837 -0.0231 -0.0125 0.0301  950  ARG A C   
6937  O O   . ARG A 952  ? 0.2899 0.2739 0.3228 -0.0248 -0.0144 0.0314  950  ARG A O   
6938  C CB  . ARG A 952  ? 0.3102 0.2927 0.3419 -0.0241 -0.0138 0.0352  950  ARG A CB  
6939  C CG  . ARG A 952  ? 0.3240 0.3014 0.3576 -0.0230 -0.0149 0.0356  950  ARG A CG  
6940  C CD  . ARG A 952  ? 0.3739 0.3533 0.4124 -0.0259 -0.0168 0.0416  950  ARG A CD  
6941  N NE  . ARG A 952  ? 0.3888 0.3751 0.4239 -0.0270 -0.0151 0.0444  950  ARG A NE  
6942  C CZ  . ARG A 952  ? 0.3892 0.3753 0.4231 -0.0263 -0.0147 0.0454  950  ARG A CZ  
6943  N NH1 . ARG A 952  ? 0.3762 0.3557 0.4122 -0.0246 -0.0158 0.0441  950  ARG A NH1 
6944  N NH2 . ARG A 952  ? 0.3562 0.3494 0.3867 -0.0273 -0.0131 0.0474  950  ARG A NH2 
6945  N N   . TYR A 953  ? 0.2448 0.2339 0.2682 -0.0224 -0.0100 0.0286  951  TYR A N   
6946  C CA  . TYR A 953  ? 0.2523 0.2468 0.2750 -0.0236 -0.0093 0.0286  951  TYR A CA  
6947  C C   . TYR A 953  ? 0.2382 0.2404 0.2575 -0.0242 -0.0072 0.0297  951  TYR A C   
6948  O O   . TYR A 953  ? 0.2508 0.2530 0.2667 -0.0227 -0.0058 0.0284  951  TYR A O   
6949  C CB  . TYR A 953  ? 0.2723 0.2641 0.2928 -0.0212 -0.0087 0.0238  951  TYR A CB  
6950  C CG  . TYR A 953  ? 0.2380 0.2295 0.2530 -0.0184 -0.0064 0.0202  951  TYR A CG  
6951  C CD1 . TYR A 953  ? 0.2339 0.2200 0.2474 -0.0161 -0.0061 0.0182  951  TYR A CD1 
6952  C CD2 . TYR A 953  ? 0.2544 0.2514 0.2665 -0.0181 -0.0045 0.0191  951  TYR A CD2 
6953  C CE1 . TYR A 953  ? 0.2270 0.2131 0.2364 -0.0138 -0.0041 0.0155  951  TYR A CE1 
6954  C CE2 . TYR A 953  ? 0.2198 0.2163 0.2279 -0.0157 -0.0027 0.0160  951  TYR A CE2 
6955  C CZ  . TYR A 953  ? 0.2357 0.2267 0.2426 -0.0136 -0.0025 0.0145  951  TYR A CZ  
6956  O OH  . TYR A 953  ? 0.2504 0.2410 0.2540 -0.0114 -0.0008 0.0119  951  TYR A OH  
6957  N N   . ARG A 954  ? 0.2754 0.2844 0.2957 -0.0264 -0.0071 0.0319  952  ARG A N   
6958  C CA  . ARG A 954  ? 0.2935 0.3109 0.3106 -0.0268 -0.0051 0.0320  952  ARG A CA  
6959  C C   . ARG A 954  ? 0.2484 0.2661 0.2619 -0.0243 -0.0034 0.0269  952  ARG A C   
6960  O O   . ARG A 954  ? 0.2623 0.2770 0.2767 -0.0236 -0.0039 0.0249  952  ARG A O   
6961  C CB  . ARG A 954  ? 0.3080 0.3335 0.3279 -0.0302 -0.0057 0.0365  952  ARG A CB  
6962  N N   . ARG A 955  ? 0.2722 0.2937 0.2821 -0.0230 -0.0015 0.0248  953  ARG A N   
6963  C CA  . ARG A 955  ? 0.2787 0.2998 0.2857 -0.0204 0.0000  0.0201  953  ARG A CA  
6964  C C   . ARG A 955  ? 0.2713 0.2958 0.2794 -0.0210 -0.0001 0.0193  953  ARG A C   
6965  O O   . ARG A 955  ? 0.2969 0.3175 0.3042 -0.0190 0.0001  0.0161  953  ARG A O   
6966  C CB  . ARG A 955  ? 0.3526 0.3790 0.3568 -0.0195 0.0018  0.0183  953  ARG A CB  
6967  C CG  . ARG A 955  ? 0.4318 0.4584 0.4340 -0.0169 0.0031  0.0135  953  ARG A CG  
6968  C CD  . ARG A 955  ? 0.4678 0.4856 0.4696 -0.0147 0.0028  0.0113  953  ARG A CD  
6969  N NE  . ARG A 955  ? 0.5401 0.5571 0.5404 -0.0122 0.0038  0.0074  953  ARG A NE  
6970  C CZ  . ARG A 955  ? 0.4900 0.5075 0.4907 -0.0116 0.0037  0.0058  953  ARG A CZ  
6971  N NH1 . ARG A 955  ? 0.3800 0.3996 0.3825 -0.0134 0.0028  0.0076  953  ARG A NH1 
6972  N NH2 . ARG A 955  ? 0.4651 0.4811 0.4648 -0.0091 0.0045  0.0026  953  ARG A NH2 
6973  N N   . ASP A 956  ? 0.2658 0.2979 0.2757 -0.0236 -0.0003 0.0223  954  ASP A N   
6974  C CA  . ASP A 956  ? 0.2691 0.3051 0.2800 -0.0241 -0.0002 0.0215  954  ASP A CA  
6975  C C   . ASP A 956  ? 0.2896 0.3192 0.3032 -0.0243 -0.0020 0.0217  954  ASP A C   
6976  O O   . ASP A 956  ? 0.3019 0.3328 0.3161 -0.0240 -0.0020 0.0200  954  ASP A O   
6977  C CB  . ASP A 956  ? 0.2844 0.3307 0.2970 -0.0271 -0.0001 0.0252  954  ASP A CB  
6978  C CG  . ASP A 956  ? 0.3544 0.4090 0.3643 -0.0266 0.0018  0.0239  954  ASP A CG  
6979  O OD1 . ASP A 956  ? 0.3663 0.4188 0.3734 -0.0237 0.0030  0.0194  954  ASP A OD1 
6980  O OD2 . ASP A 956  ? 0.4120 0.4753 0.4227 -0.0290 0.0019  0.0274  954  ASP A OD2 
6981  N N   . ASP A 957  ? 0.2657 0.2886 0.2812 -0.0248 -0.0036 0.0235  955  ASP A N   
6982  C CA  . ASP A 957  ? 0.2801 0.2970 0.2986 -0.0249 -0.0055 0.0232  955  ASP A CA  
6983  C C   . ASP A 957  ? 0.2686 0.2780 0.2848 -0.0216 -0.0054 0.0189  955  ASP A C   
6984  O O   . ASP A 957  ? 0.2737 0.2775 0.2921 -0.0213 -0.0071 0.0181  955  ASP A O   
6985  C CB  . ASP A 957  ? 0.3261 0.3405 0.3492 -0.0273 -0.0077 0.0275  955  ASP A CB  
6986  C CG  . ASP A 957  ? 0.3907 0.4129 0.4169 -0.0309 -0.0081 0.0326  955  ASP A CG  
6987  O OD1 . ASP A 957  ? 0.3707 0.3989 0.3971 -0.0318 -0.0076 0.0326  955  ASP A OD1 
6988  O OD2 . ASP A 957  ? 0.4234 0.4462 0.4521 -0.0328 -0.0091 0.0369  955  ASP A OD2 
6989  N N   . LEU A 958  ? 0.2523 0.2618 0.2645 -0.0192 -0.0035 0.0160  956  LEU A N   
6990  C CA  . LEU A 958  ? 0.2353 0.2385 0.2453 -0.0162 -0.0032 0.0124  956  LEU A CA  
6991  C C   . LEU A 958  ? 0.2651 0.2666 0.2759 -0.0154 -0.0041 0.0103  956  LEU A C   
6992  O O   . LEU A 958  ? 0.2398 0.2357 0.2508 -0.0140 -0.0051 0.0086  956  LEU A O   
6993  C CB  . LEU A 958  ? 0.2572 0.2617 0.2634 -0.0141 -0.0012 0.0101  956  LEU A CB  
6994  C CG  . LEU A 958  ? 0.2513 0.2503 0.2554 -0.0110 -0.0008 0.0069  956  LEU A CG  
6995  C CD1 . LEU A 958  ? 0.2827 0.2756 0.2871 -0.0104 -0.0016 0.0074  956  LEU A CD1 
6996  C CD2 . LEU A 958  ? 0.2931 0.2939 0.2945 -0.0092 0.0011  0.0050  956  LEU A CD2 
6997  N N   . ASP A 959  ? 0.2229 0.2296 0.2341 -0.0161 -0.0037 0.0101  957  ASP A N   
6998  C CA  . ASP A 959  ? 0.2470 0.2526 0.2589 -0.0152 -0.0045 0.0079  957  ASP A CA  
6999  C C   . ASP A 959  ? 0.2323 0.2349 0.2482 -0.0169 -0.0069 0.0092  957  ASP A C   
7000  O O   . ASP A 959  ? 0.2573 0.2558 0.2735 -0.0155 -0.0080 0.0068  957  ASP A O   
7001  C CB  . ASP A 959  ? 0.2558 0.2680 0.2676 -0.0157 -0.0036 0.0074  957  ASP A CB  
7002  C CG  . ASP A 959  ? 0.2786 0.2895 0.2902 -0.0140 -0.0041 0.0046  957  ASP A CG  
7003  O OD1 . ASP A 959  ? 0.2787 0.2858 0.2878 -0.0113 -0.0037 0.0021  957  ASP A OD1 
7004  O OD2 . ASP A 959  ? 0.3725 0.3865 0.3866 -0.0155 -0.0050 0.0051  957  ASP A OD2 
7005  N N   . ARG A 960  ? 0.2393 0.2442 0.2586 -0.0199 -0.0079 0.0129  958  ARG A N   
7006  C CA  . ARG A 960  ? 0.2472 0.2487 0.2714 -0.0216 -0.0105 0.0144  958  ARG A CA  
7007  C C   . ARG A 960  ? 0.2724 0.2665 0.2966 -0.0199 -0.0115 0.0127  958  ARG A C   
7008  O O   . ARG A 960  ? 0.2814 0.2713 0.3082 -0.0194 -0.0134 0.0110  958  ARG A O   
7009  C CB  . ARG A 960  ? 0.2822 0.2878 0.3104 -0.0253 -0.0113 0.0195  958  ARG A CB  
7010  C CG  . ARG A 960  ? 0.3228 0.3255 0.3575 -0.0276 -0.0143 0.0217  958  ARG A CG  
7011  C CD  . ARG A 960  ? 0.4560 0.4525 0.4929 -0.0274 -0.0157 0.0226  958  ARG A CD  
7012  N NE  . ARG A 960  ? 0.4714 0.4695 0.5056 -0.0274 -0.0142 0.0248  958  ARG A NE  
7013  C CZ  . ARG A 960  ? 0.4720 0.4650 0.5057 -0.0261 -0.0145 0.0245  958  ARG A CZ  
7014  N NH1 . ARG A 960  ? 0.5131 0.4993 0.5489 -0.0246 -0.0162 0.0219  958  ARG A NH1 
7015  N NH2 . ARG A 960  ? 0.5423 0.5376 0.5735 -0.0263 -0.0130 0.0264  958  ARG A NH2 
7016  N N   . LEU A 961  ? 0.2424 0.2351 0.2637 -0.0188 -0.0101 0.0130  959  LEU A N   
7017  C CA  . LEU A 961  ? 0.2609 0.2473 0.2821 -0.0170 -0.0109 0.0114  959  LEU A CA  
7018  C C   . LEU A 961  ? 0.2699 0.2533 0.2886 -0.0139 -0.0107 0.0069  959  LEU A C   
7019  O O   . LEU A 961  ? 0.2608 0.2398 0.2815 -0.0130 -0.0124 0.0050  959  LEU A O   
7020  C CB  . LEU A 961  ? 0.2357 0.2221 0.2540 -0.0163 -0.0092 0.0124  959  LEU A CB  
7021  C CG  . LEU A 961  ? 0.2446 0.2251 0.2621 -0.0140 -0.0095 0.0105  959  LEU A CG  
7022  C CD1 . LEU A 961  ? 0.3161 0.2928 0.3389 -0.0153 -0.0122 0.0119  959  LEU A CD1 
7023  C CD2 . LEU A 961  ? 0.2934 0.2745 0.3076 -0.0132 -0.0076 0.0112  959  LEU A CD2 
7024  N N   . VAL A 962  ? 0.2402 0.2262 0.2550 -0.0123 -0.0088 0.0052  960  VAL A N   
7025  C CA  . VAL A 962  ? 0.2454 0.2295 0.2579 -0.0096 -0.0088 0.0015  960  VAL A CA  
7026  C C   . VAL A 962  ? 0.2838 0.2674 0.2996 -0.0102 -0.0109 0.0001  960  VAL A C   
7027  O O   . VAL A 962  ? 0.2813 0.2618 0.2970 -0.0084 -0.0120 -0.0027 960  VAL A O   
7028  C CB  . VAL A 962  ? 0.2545 0.2417 0.2630 -0.0080 -0.0066 0.0004  960  VAL A CB  
7029  C CG1 . VAL A 962  ? 0.2984 0.2842 0.3049 -0.0054 -0.0067 -0.0028 960  VAL A CG1 
7030  C CG2 . VAL A 962  ? 0.2580 0.2452 0.2639 -0.0073 -0.0047 0.0012  960  VAL A CG2 
7031  N N   . ASP A 963  ? 0.2865 0.2736 0.3053 -0.0128 -0.0117 0.0021  961  ASP A N   
7032  C CA  . ASP A 963  ? 0.2801 0.2665 0.3030 -0.0138 -0.0141 0.0012  961  ASP A CA  
7033  C C   . ASP A 963  ? 0.2862 0.2675 0.3131 -0.0141 -0.0164 0.0008  961  ASP A C   
7034  O O   . ASP A 963  ? 0.3141 0.2929 0.3426 -0.0129 -0.0182 -0.0024 961  ASP A O   
7035  C CB  . ASP A 963  ? 0.3010 0.2922 0.3273 -0.0171 -0.0145 0.0043  961  ASP A CB  
7036  C CG  . ASP A 963  ? 0.3632 0.3598 0.3867 -0.0166 -0.0127 0.0038  961  ASP A CG  
7037  O OD1 . ASP A 963  ? 0.4199 0.4161 0.4396 -0.0139 -0.0116 0.0008  961  ASP A OD1 
7038  O OD2 . ASP A 963  ? 0.4511 0.4527 0.4766 -0.0191 -0.0125 0.0066  961  ASP A OD2 
7039  N N   . ASP A 964  ? 0.2674 0.2474 0.2962 -0.0156 -0.0166 0.0038  962  ASP A N   
7040  C CA  . ASP A 964  ? 0.3141 0.2891 0.3475 -0.0159 -0.0190 0.0036  962  ASP A CA  
7041  C C   . ASP A 964  ? 0.3500 0.3211 0.3808 -0.0124 -0.0190 -0.0007 962  ASP A C   
7042  O O   . ASP A 964  ? 0.3557 0.3235 0.3900 -0.0117 -0.0213 -0.0035 962  ASP A O   
7043  C CB  . ASP A 964  ? 0.3249 0.2997 0.3604 -0.0179 -0.0190 0.0080  962  ASP A CB  
7044  C CG  . ASP A 964  ? 0.3339 0.3128 0.3735 -0.0217 -0.0198 0.0127  962  ASP A CG  
7045  O OD1 . ASP A 964  ? 0.4263 0.4075 0.4679 -0.0228 -0.0206 0.0123  962  ASP A OD1 
7046  O OD2 . ASP A 964  ? 0.4871 0.4674 0.5278 -0.0236 -0.0195 0.0169  962  ASP A OD2 
7047  N N   . VAL A 965  ? 0.2805 0.2522 0.3054 -0.0103 -0.0164 -0.0015 963  VAL A N   
7048  C CA  . VAL A 965  ? 0.2868 0.2560 0.3090 -0.0070 -0.0161 -0.0052 963  VAL A CA  
7049  C C   . VAL A 965  ? 0.3144 0.2843 0.3361 -0.0054 -0.0170 -0.0090 963  VAL A C   
7050  O O   . VAL A 965  ? 0.3190 0.2867 0.3420 -0.0037 -0.0185 -0.0125 963  VAL A O   
7051  C CB  . VAL A 965  ? 0.2607 0.2310 0.2771 -0.0053 -0.0131 -0.0047 963  VAL A CB  
7052  C CG1 . VAL A 965  ? 0.2835 0.2523 0.2968 -0.0020 -0.0127 -0.0082 963  VAL A CG1 
7053  C CG2 . VAL A 965  ? 0.2926 0.2620 0.3096 -0.0066 -0.0125 -0.0014 963  VAL A CG2 
7054  N N   . ASN A 966  ? 0.2710 0.2446 0.2908 -0.0058 -0.0161 -0.0087 964  ASN A N   
7055  C CA  . ASN A 966  ? 0.2828 0.2577 0.3021 -0.0044 -0.0170 -0.0121 964  ASN A CA  
7056  C C   . ASN A 966  ? 0.3272 0.3005 0.3525 -0.0057 -0.0202 -0.0137 964  ASN A C   
7057  O O   . ASN A 966  ? 0.3030 0.2762 0.3286 -0.0039 -0.0216 -0.0176 964  ASN A O   
7058  C CB  . ASN A 966  ? 0.2700 0.2493 0.2871 -0.0049 -0.0156 -0.0111 964  ASN A CB  
7059  C CG  . ASN A 966  ? 0.2911 0.2720 0.3026 -0.0029 -0.0129 -0.0108 964  ASN A CG  
7060  O OD1 . ASN A 966  ? 0.2769 0.2560 0.2856 -0.0007 -0.0120 -0.0120 964  ASN A OD1 
7061  N ND2 . ASN A 966  ? 0.2694 0.2538 0.2797 -0.0037 -0.0115 -0.0093 964  ASN A ND2 
7062  N N   . ALA A 967  ? 0.3154 0.2878 0.3458 -0.0088 -0.0215 -0.0106 965  ALA A N   
7063  C CA  . ALA A 967  ? 0.3477 0.3188 0.3849 -0.0105 -0.0247 -0.0114 965  ALA A CA  
7064  C C   . ALA A 967  ? 0.3462 0.3128 0.3869 -0.0090 -0.0271 -0.0149 965  ALA A C   
7065  O O   . ALA A 967  ? 0.3567 0.3221 0.4031 -0.0098 -0.0301 -0.0169 965  ALA A O   
7066  C CB  . ALA A 967  ? 0.3871 0.3589 0.4292 -0.0144 -0.0255 -0.0063 965  ALA A CB  
7067  N N   . THR A 968  ? 0.2935 0.2580 0.3314 -0.0069 -0.0261 -0.0159 966  THR A N   
7068  C CA  . THR A 968  ? 0.3009 0.2619 0.3419 -0.0050 -0.0283 -0.0201 966  THR A CA  
7069  C C   . THR A 968  ? 0.3111 0.2739 0.3506 -0.0025 -0.0291 -0.0256 966  THR A C   
7070  O O   . THR A 968  ? 0.3429 0.3037 0.3866 -0.0013 -0.0318 -0.0298 966  THR A O   
7071  C CB  . THR A 968  ? 0.3201 0.2794 0.3577 -0.0029 -0.0266 -0.0202 966  THR A CB  
7072  O OG1 . THR A 968  ? 0.2977 0.2600 0.3280 -0.0002 -0.0240 -0.0220 966  THR A OG1 
7073  C CG2 . THR A 968  ? 0.3083 0.2668 0.3461 -0.0051 -0.0253 -0.0147 966  THR A CG2 
7074  N N   . GLY A 969  ? 0.2780 0.2448 0.3117 -0.0015 -0.0271 -0.0258 967  GLY A N   
7075  C CA  . GLY A 969  ? 0.2828 0.2523 0.3142 0.0011  -0.0276 -0.0305 967  GLY A CA  
7076  C C   . GLY A 969  ? 0.2782 0.2488 0.3038 0.0046  -0.0258 -0.0328 967  GLY A C   
7077  O O   . GLY A 969  ? 0.2496 0.2237 0.2718 0.0069  -0.0255 -0.0359 967  GLY A O   
7078  N N   . TYR A 970  ? 0.2582 0.2265 0.2828 0.0051  -0.0245 -0.0312 968  TYR A N   
7079  C CA  . TYR A 970  ? 0.2381 0.2080 0.2572 0.0081  -0.0225 -0.0326 968  TYR A CA  
7080  C C   . TYR A 970  ? 0.2281 0.2007 0.2412 0.0082  -0.0194 -0.0292 968  TYR A C   
7081  O O   . TYR A 970  ? 0.2777 0.2507 0.2910 0.0060  -0.0187 -0.0260 968  TYR A O   
7082  C CB  . TYR A 970  ? 0.2366 0.2030 0.2572 0.0085  -0.0224 -0.0322 968  TYR A CB  
7083  C CG  . TYR A 970  ? 0.2475 0.2114 0.2742 0.0091  -0.0256 -0.0363 968  TYR A CG  
7084  C CD1 . TYR A 970  ? 0.2774 0.2432 0.3032 0.0123  -0.0263 -0.0416 968  TYR A CD1 
7085  C CD2 . TYR A 970  ? 0.2865 0.2464 0.3203 0.0064  -0.0280 -0.0348 968  TYR A CD2 
7086  C CE1 . TYR A 970  ? 0.2876 0.2511 0.3195 0.0131  -0.0294 -0.0459 968  TYR A CE1 
7087  C CE2 . TYR A 970  ? 0.3082 0.2653 0.3485 0.0070  -0.0312 -0.0386 968  TYR A CE2 
7088  C CZ  . TYR A 970  ? 0.3179 0.2768 0.3574 0.0104  -0.0319 -0.0445 968  TYR A CZ  
7089  O OH  . TYR A 970  ? 0.3917 0.3479 0.4382 0.0112  -0.0352 -0.0489 968  TYR A OH  
7090  N N   . GLY A 971  ? 0.2039 0.1785 0.2121 0.0108  -0.0175 -0.0299 969  GLY A N   
7091  C CA  . GLY A 971  ? 0.2152 0.1922 0.2185 0.0111  -0.0148 -0.0269 969  GLY A CA  
7092  C C   . GLY A 971  ? 0.2167 0.1957 0.2156 0.0139  -0.0130 -0.0275 969  GLY A C   
7093  O O   . GLY A 971  ? 0.2247 0.2074 0.2199 0.0155  -0.0120 -0.0275 969  GLY A O   
7094  N N   . LEU A 972  ? 0.1951 0.1719 0.1945 0.0145  -0.0127 -0.0276 970  LEU A N   
7095  C CA  . LEU A 972  ? 0.2124 0.1915 0.2080 0.0172  -0.0112 -0.0283 970  LEU A CA  
7096  C C   . LEU A 972  ? 0.2188 0.1972 0.2119 0.0167  -0.0086 -0.0241 970  LEU A C   
7097  O O   . LEU A 972  ? 0.2154 0.1961 0.2055 0.0170  -0.0070 -0.0221 970  LEU A O   
7098  C CB  . LEU A 972  ? 0.2165 0.1946 0.2144 0.0186  -0.0125 -0.0317 970  LEU A CB  
7099  C CG  . LEU A 972  ? 0.2190 0.2009 0.2132 0.0215  -0.0111 -0.0331 970  LEU A CG  
7100  C CD1 . LEU A 972  ? 0.2220 0.2097 0.2124 0.0233  -0.0106 -0.0340 970  LEU A CD1 
7101  C CD2 . LEU A 972  ? 0.2434 0.2250 0.2406 0.0231  -0.0129 -0.0376 970  LEU A CD2 
7102  N N   . THR A 973  ? 0.2040 0.1791 0.1985 0.0159  -0.0082 -0.0227 971  THR A N   
7103  C CA  . THR A 973  ? 0.2011 0.1755 0.1937 0.0153  -0.0059 -0.0190 971  THR A CA  
7104  C C   . THR A 973  ? 0.2009 0.1724 0.1959 0.0124  -0.0061 -0.0164 971  THR A C   
7105  O O   . THR A 973  ? 0.2117 0.1812 0.2105 0.0108  -0.0079 -0.0170 971  THR A O   
7106  C CB  . THR A 973  ? 0.1939 0.1678 0.1857 0.0167  -0.0049 -0.0190 971  THR A CB  
7107  O OG1 . THR A 973  ? 0.2191 0.1898 0.2147 0.0160  -0.0066 -0.0204 971  THR A OG1 
7108  C CG2 . THR A 973  ? 0.2262 0.2042 0.2152 0.0195  -0.0044 -0.0211 971  THR A CG2 
7109  N N   . PHE A 974  ? 0.2098 0.1817 0.2030 0.0117  -0.0042 -0.0135 972  PHE A N   
7110  C CA  . PHE A 974  ? 0.2032 0.1737 0.1982 0.0091  -0.0041 -0.0110 972  PHE A CA  
7111  C C   . PHE A 974  ? 0.1917 0.1622 0.1846 0.0092  -0.0020 -0.0086 972  PHE A C   
7112  O O   . PHE A 974  ? 0.2210 0.1933 0.2115 0.0106  -0.0006 -0.0083 972  PHE A O   
7113  C CB  . PHE A 974  ? 0.2088 0.1812 0.2041 0.0079  -0.0045 -0.0107 972  PHE A CB  
7114  C CG  . PHE A 974  ? 0.1963 0.1687 0.1928 0.0055  -0.0040 -0.0081 972  PHE A CG  
7115  C CD1 . PHE A 974  ? 0.1930 0.1641 0.1929 0.0032  -0.0054 -0.0071 972  PHE A CD1 
7116  C CD2 . PHE A 974  ? 0.2199 0.1940 0.2145 0.0055  -0.0022 -0.0066 972  PHE A CD2 
7117  C CE1 . PHE A 974  ? 0.2258 0.1981 0.2267 0.0010  -0.0048 -0.0045 972  PHE A CE1 
7118  C CE2 . PHE A 974  ? 0.2023 0.1774 0.1980 0.0035  -0.0017 -0.0046 972  PHE A CE2 
7119  C CZ  . PHE A 974  ? 0.2122 0.1867 0.2107 0.0012  -0.0030 -0.0035 972  PHE A CZ  
7120  N N   . GLY A 975  ? 0.1890 0.1579 0.1834 0.0076  -0.0018 -0.0068 973  GLY A N   
7121  C CA  . GLY A 975  ? 0.2064 0.1754 0.1995 0.0075  -0.0001 -0.0049 973  GLY A CA  
7122  C C   . GLY A 975  ? 0.2006 0.1706 0.1947 0.0052  0.0002  -0.0030 973  GLY A C   
7123  O O   . GLY A 975  ? 0.1911 0.1609 0.1874 0.0033  -0.0011 -0.0024 973  GLY A O   
7124  N N   . LEU A 976  ? 0.2030 0.1743 0.1958 0.0054  0.0017  -0.0020 974  LEU A N   
7125  C CA  . LEU A 976  ? 0.1955 0.1685 0.1890 0.0035  0.0021  -0.0007 974  LEU A CA  
7126  C C   . LEU A 976  ? 0.1893 0.1621 0.1821 0.0038  0.0035  0.0002  974  LEU A C   
7127  O O   . LEU A 976  ? 0.2095 0.1821 0.2011 0.0055  0.0045  -0.0002 974  LEU A O   
7128  C CB  . LEU A 976  ? 0.2112 0.1869 0.2043 0.0036  0.0025  -0.0013 974  LEU A CB  
7129  C CG  . LEU A 976  ? 0.2044 0.1831 0.1981 0.0021  0.0031  -0.0005 974  LEU A CG  
7130  C CD1 . LEU A 976  ? 0.2424 0.2223 0.2378 -0.0004 0.0022  0.0009  974  LEU A CD1 
7131  C CD2 . LEU A 976  ? 0.2449 0.2260 0.2384 0.0028  0.0035  -0.0016 974  LEU A CD2 
7132  N N   . HIS A 977  ? 0.1972 0.1704 0.1910 0.0022  0.0034  0.0016  975  HIS A N   
7133  C CA  . HIS A 977  ? 0.2063 0.1798 0.1997 0.0022  0.0045  0.0022  975  HIS A CA  
7134  C C   . HIS A 977  ? 0.1967 0.1739 0.1906 0.0007  0.0048  0.0026  975  HIS A C   
7135  O O   . HIS A 977  ? 0.2081 0.1871 0.2030 -0.0012 0.0041  0.0039  975  HIS A O   
7136  C CB  . HIS A 977  ? 0.2266 0.1981 0.2207 0.0018  0.0041  0.0034  975  HIS A CB  
7137  C CG  . HIS A 977  ? 0.2470 0.2160 0.2404 0.0037  0.0045  0.0028  975  HIS A CG  
7138  N ND1 . HIS A 977  ? 0.3114 0.2801 0.3044 0.0043  0.0056  0.0033  975  HIS A ND1 
7139  C CD2 . HIS A 977  ? 0.3250 0.2923 0.3180 0.0052  0.0041  0.0017  975  HIS A CD2 
7140  C CE1 . HIS A 977  ? 0.2945 0.2615 0.2869 0.0060  0.0058  0.0028  975  HIS A CE1 
7141  N NE2 . HIS A 977  ? 0.2911 0.2575 0.2834 0.0067  0.0050  0.0018  975  HIS A NE2 
7142  N N   . THR A 978  ? 0.1958 0.1745 0.1893 0.0016  0.0058  0.0015  976  THR A N   
7143  C CA  . THR A 978  ? 0.2065 0.1893 0.2006 0.0006  0.0062  0.0011  976  THR A CA  
7144  C C   . THR A 978  ? 0.2040 0.1869 0.1984 0.0022  0.0071  -0.0003 976  THR A C   
7145  O O   . THR A 978  ? 0.2297 0.2100 0.2238 0.0038  0.0074  -0.0007 976  THR A O   
7146  C CB  . THR A 978  ? 0.2230 0.2087 0.2175 -0.0001 0.0057  0.0006  976  THR A CB  
7147  O OG1 . THR A 978  ? 0.2090 0.1996 0.2041 -0.0009 0.0062  -0.0002 976  THR A OG1 
7148  C CG2 . THR A 978  ? 0.2324 0.2167 0.2265 0.0016  0.0058  -0.0007 976  THR A CG2 
7149  N N   . ARG A 979  ? 0.2067 0.1928 0.2018 0.0016  0.0075  -0.0012 977  ARG A N   
7150  C CA  . ARG A 979  ? 0.2407 0.2272 0.2372 0.0029  0.0081  -0.0029 977  ARG A CA  
7151  C C   . ARG A 979  ? 0.2281 0.2180 0.2256 0.0032  0.0081  -0.0047 977  ARG A C   
7152  O O   . ARG A 979  ? 0.2557 0.2459 0.2550 0.0045  0.0083  -0.0064 977  ARG A O   
7153  C CB  . ARG A 979  ? 0.2372 0.2254 0.2344 0.0024  0.0084  -0.0034 977  ARG A CB  
7154  C CG  . ARG A 979  ? 0.2930 0.2776 0.2896 0.0025  0.0085  -0.0018 977  ARG A CG  
7155  C CD  . ARG A 979  ? 0.3981 0.3849 0.3954 0.0017  0.0087  -0.0021 977  ARG A CD  
7156  N NE  . ARG A 979  ? 0.4375 0.4209 0.4346 0.0020  0.0088  -0.0008 977  ARG A NE  
7157  C CZ  . ARG A 979  ? 0.4803 0.4648 0.4782 0.0015  0.0089  -0.0009 977  ARG A CZ  
7158  N NH1 . ARG A 979  ? 0.3989 0.3879 0.3976 0.0008  0.0089  -0.0026 977  ARG A NH1 
7159  N NH2 . ARG A 979  ? 0.4611 0.4425 0.4590 0.0019  0.0090  0.0004  977  ARG A NH2 
7160  N N   . LEU A 980  ? 0.1928 0.1852 0.1896 0.0021  0.0077  -0.0044 978  LEU A N   
7161  C CA  . LEU A 980  ? 0.1969 0.1941 0.1949 0.0020  0.0077  -0.0062 978  LEU A CA  
7162  C C   . LEU A 980  ? 0.2142 0.2100 0.2124 0.0032  0.0074  -0.0066 978  LEU A C   
7163  O O   . LEU A 980  ? 0.2091 0.2035 0.2062 0.0027  0.0069  -0.0052 978  LEU A O   
7164  C CB  . LEU A 980  ? 0.2029 0.2050 0.2004 -0.0002 0.0075  -0.0052 978  LEU A CB  
7165  C CG  . LEU A 980  ? 0.2151 0.2191 0.2122 -0.0015 0.0077  -0.0043 978  LEU A CG  
7166  C CD1 . LEU A 980  ? 0.2466 0.2559 0.2434 -0.0039 0.0074  -0.0025 978  LEU A CD1 
7167  C CD2 . LEU A 980  ? 0.2416 0.2483 0.2398 -0.0006 0.0082  -0.0070 978  LEU A CD2 
7168  N N   . ASP A 981  ? 0.2116 0.2079 0.2116 0.0048  0.0076  -0.0085 979  ASP A N   
7169  C CA  . ASP A 981  ? 0.2066 0.2020 0.2071 0.0061  0.0072  -0.0087 979  ASP A CA  
7170  C C   . ASP A 981  ? 0.2180 0.2167 0.2179 0.0049  0.0068  -0.0087 979  ASP A C   
7171  O O   . ASP A 981  ? 0.2047 0.2019 0.2039 0.0053  0.0063  -0.0081 979  ASP A O   
7172  C CB  . ASP A 981  ? 0.2419 0.2381 0.2453 0.0078  0.0072  -0.0108 979  ASP A CB  
7173  C CG  . ASP A 981  ? 0.2456 0.2377 0.2503 0.0091  0.0073  -0.0103 979  ASP A CG  
7174  O OD1 . ASP A 981  ? 0.2885 0.2772 0.2913 0.0090  0.0075  -0.0082 979  ASP A OD1 
7175  O OD2 . ASP A 981  ? 0.2914 0.2840 0.2993 0.0104  0.0072  -0.0120 979  ASP A OD2 
7176  N N   . GLU A 982  ? 0.2005 0.2045 0.2009 0.0034  0.0070  -0.0095 980  GLU A N   
7177  C CA  . GLU A 982  ? 0.2067 0.2143 0.2070 0.0022  0.0066  -0.0091 980  GLU A CA  
7178  C C   . GLU A 982  ? 0.2023 0.2071 0.2011 0.0008  0.0059  -0.0066 980  GLU A C   
7179  O O   . GLU A 982  ? 0.2142 0.2188 0.2130 0.0006  0.0052  -0.0062 980  GLU A O   
7180  C CB  . GLU A 982  ? 0.2362 0.2508 0.2371 0.0007  0.0070  -0.0099 980  GLU A CB  
7181  C CG  . GLU A 982  ? 0.2338 0.2526 0.2349 -0.0011 0.0066  -0.0088 980  GLU A CG  
7182  C CD  . GLU A 982  ? 0.3144 0.3406 0.3158 -0.0031 0.0070  -0.0084 980  GLU A CD  
7183  O OE1 . GLU A 982  ? 0.3210 0.3474 0.3215 -0.0043 0.0071  -0.0068 980  GLU A OE1 
7184  O OE2 . GLU A 982  ? 0.2792 0.3117 0.2817 -0.0034 0.0071  -0.0095 980  GLU A OE2 
7185  N N   . THR A 983  ? 0.1866 0.1888 0.1843 0.0000  0.0060  -0.0051 981  THR A N   
7186  C CA  . THR A 983  ? 0.2020 0.2013 0.1991 -0.0012 0.0051  -0.0030 981  THR A CA  
7187  C C   . THR A 983  ? 0.2073 0.2016 0.2035 0.0006  0.0047  -0.0033 981  THR A C   
7188  O O   . THR A 983  ? 0.2115 0.2047 0.2078 0.0002  0.0037  -0.0028 981  THR A O   
7189  C CB  . THR A 983  ? 0.2178 0.2161 0.2145 -0.0023 0.0052  -0.0014 981  THR A CB  
7190  O OG1 . THR A 983  ? 0.2340 0.2380 0.2312 -0.0041 0.0055  -0.0008 981  THR A OG1 
7191  C CG2 . THR A 983  ? 0.2278 0.2224 0.2244 -0.0033 0.0041  0.0005  981  THR A CG2 
7192  N N   . ILE A 984  ? 0.1968 0.1887 0.1927 0.0026  0.0053  -0.0041 982  ILE A N   
7193  C CA  . ILE A 984  ? 0.2058 0.1942 0.2008 0.0043  0.0050  -0.0041 982  ILE A CA  
7194  C C   . ILE A 984  ? 0.2128 0.2029 0.2081 0.0048  0.0044  -0.0049 982  ILE A C   
7195  O O   . ILE A 984  ? 0.2021 0.1908 0.1967 0.0051  0.0036  -0.0048 982  ILE A O   
7196  C CB  . ILE A 984  ? 0.2020 0.1883 0.1970 0.0061  0.0058  -0.0042 982  ILE A CB  
7197  C CG1 . ILE A 984  ? 0.2211 0.2055 0.2157 0.0056  0.0062  -0.0033 982  ILE A CG1 
7198  C CG2 . ILE A 984  ? 0.2372 0.2215 0.2314 0.0080  0.0055  -0.0040 982  ILE A CG2 
7199  C CD1 . ILE A 984  ? 0.2431 0.2261 0.2384 0.0070  0.0069  -0.0034 982  ILE A CD1 
7200  N N   . ALA A 985  ? 0.1974 0.1909 0.1941 0.0051  0.0048  -0.0061 983  ALA A N   
7201  C CA  . ALA A 985  ? 0.2139 0.2093 0.2113 0.0057  0.0042  -0.0069 983  ALA A CA  
7202  C C   . ALA A 985  ? 0.2128 0.2098 0.2102 0.0039  0.0033  -0.0065 983  ALA A C   
7203  O O   . ALA A 985  ? 0.2128 0.2092 0.2099 0.0044  0.0025  -0.0067 983  ALA A O   
7204  C CB  . ALA A 985  ? 0.2187 0.2177 0.2181 0.0063  0.0047  -0.0085 983  ALA A CB  
7205  N N   . HIS A 986  ? 0.2091 0.2084 0.2071 0.0018  0.0034  -0.0058 984  HIS A N   
7206  C CA  . HIS A 986  ? 0.2409 0.2419 0.2396 -0.0003 0.0024  -0.0049 984  HIS A CA  
7207  C C   . HIS A 986  ? 0.2133 0.2099 0.2115 -0.0003 0.0013  -0.0042 984  HIS A C   
7208  O O   . HIS A 986  ? 0.2253 0.2217 0.2240 -0.0003 0.0003  -0.0047 984  HIS A O   
7209  C CB  . HIS A 986  ? 0.2191 0.2236 0.2187 -0.0026 0.0028  -0.0036 984  HIS A CB  
7210  C CG  . HIS A 986  ? 0.2447 0.2506 0.2458 -0.0051 0.0016  -0.0017 984  HIS A CG  
7211  N ND1 . HIS A 986  ? 0.3150 0.3239 0.3170 -0.0074 0.0017  0.0004  984  HIS A ND1 
7212  C CD2 . HIS A 986  ? 0.2218 0.2268 0.2240 -0.0057 0.0003  -0.0015 984  HIS A CD2 
7213  C CE1 . HIS A 986  ? 0.3294 0.3389 0.3333 -0.0095 0.0004  0.0021  984  HIS A CE1 
7214  N NE2 . HIS A 986  ? 0.2644 0.2714 0.2686 -0.0085 -0.0005 0.0008  984  HIS A NE2 
7215  N N   . VAL A 987  ? 0.2209 0.2142 0.2182 -0.0003 0.0015  -0.0034 985  VAL A N   
7216  C CA  . VAL A 987  ? 0.2136 0.2031 0.2109 -0.0004 0.0004  -0.0031 985  VAL A CA  
7217  C C   . VAL A 987  ? 0.2427 0.2303 0.2388 0.0019  0.0000  -0.0046 985  VAL A C   
7218  O O   . VAL A 987  ? 0.2150 0.2016 0.2117 0.0018  -0.0013 -0.0053 985  VAL A O   
7219  C CB  . VAL A 987  ? 0.1934 0.1802 0.1903 -0.0006 0.0007  -0.0020 985  VAL A CB  
7220  C CG1 . VAL A 987  ? 0.2232 0.2061 0.2202 -0.0001 -0.0004 -0.0022 985  VAL A CG1 
7221  C CG2 . VAL A 987  ? 0.2336 0.2230 0.2320 -0.0031 0.0007  -0.0001 985  VAL A CG2 
7222  N N   . THR A 988  ? 0.2237 0.2109 0.2183 0.0039  0.0011  -0.0051 986  THR A N   
7223  C CA  . THR A 988  ? 0.2266 0.2127 0.2198 0.0060  0.0007  -0.0060 986  THR A CA  
7224  C C   . THR A 988  ? 0.2826 0.2713 0.2765 0.0063  -0.0001 -0.0070 986  THR A C   
7225  O O   . THR A 988  ? 0.2987 0.2870 0.2917 0.0075  -0.0009 -0.0079 986  THR A O   
7226  C CB  . THR A 988  ? 0.2515 0.2367 0.2435 0.0080  0.0019  -0.0056 986  THR A CB  
7227  O OG1 . THR A 988  ? 0.2634 0.2508 0.2565 0.0082  0.0026  -0.0056 986  THR A OG1 
7228  C CG2 . THR A 988  ? 0.2557 0.2385 0.2472 0.0078  0.0026  -0.0047 986  THR A CG2 
7229  N N   . SER A 989  ? 0.2345 0.2262 0.2298 0.0052  0.0001  -0.0070 987  SER A N   
7230  C CA  . SER A 989  ? 0.2788 0.2732 0.2750 0.0053  -0.0007 -0.0079 987  SER A CA  
7231  C C   . SER A 989  ? 0.2823 0.2768 0.2797 0.0035  -0.0023 -0.0082 987  SER A C   
7232  O O   . SER A 989  ? 0.3640 0.3597 0.3619 0.0040  -0.0034 -0.0093 987  SER A O   
7233  C CB  . SER A 989  ? 0.3110 0.3091 0.3085 0.0050  0.0000  -0.0081 987  SER A CB  
7234  O OG  . SER A 989  ? 0.3911 0.3913 0.3900 0.0026  0.0002  -0.0074 987  SER A OG  
7235  N N   . ARG A 990  ? 0.2195 0.2128 0.2180 0.0016  -0.0025 -0.0071 988  ARG A N   
7236  C CA  . ARG A 990  ? 0.2548 0.2483 0.2558 -0.0005 -0.0042 -0.0070 988  ARG A CA  
7237  C C   . ARG A 990  ? 0.2517 0.2412 0.2529 -0.0001 -0.0055 -0.0078 988  ARG A C   
7238  O O   . ARG A 990  ? 0.2577 0.2471 0.2611 -0.0009 -0.0073 -0.0086 988  ARG A O   
7239  C CB  . ARG A 990  ? 0.2817 0.2771 0.2847 -0.0032 -0.0040 -0.0048 988  ARG A CB  
7240  C CG  . ARG A 990  ? 0.3597 0.3600 0.3627 -0.0036 -0.0027 -0.0045 988  ARG A CG  
7241  C CD  . ARG A 990  ? 0.3886 0.3925 0.3934 -0.0044 -0.0035 -0.0050 988  ARG A CD  
7242  N NE  . ARG A 990  ? 0.3502 0.3569 0.3578 -0.0075 -0.0042 -0.0029 988  ARG A NE  
7243  C CZ  . ARG A 990  ? 0.3345 0.3448 0.3446 -0.0090 -0.0051 -0.0026 988  ARG A CZ  
7244  N NH1 . ARG A 990  ? 0.3977 0.4090 0.4078 -0.0077 -0.0055 -0.0046 988  ARG A NH1 
7245  N NH2 . ARG A 990  ? 0.3411 0.3545 0.3540 -0.0120 -0.0055 -0.0001 988  ARG A NH2 
7246  N N   . ILE A 991  ? 0.2195 0.2062 0.2188 0.0012  -0.0047 -0.0077 989  ILE A N   
7247  C CA  . ILE A 991  ? 0.2267 0.2102 0.2263 0.0020  -0.0059 -0.0089 989  ILE A CA  
7248  C C   . ILE A 991  ? 0.2327 0.2170 0.2312 0.0040  -0.0067 -0.0114 989  ILE A C   
7249  O O   . ILE A 991  ? 0.2377 0.2241 0.2341 0.0055  -0.0059 -0.0116 989  ILE A O   
7250  C CB  . ILE A 991  ? 0.2184 0.1994 0.2162 0.0030  -0.0047 -0.0083 989  ILE A CB  
7251  C CG1 . ILE A 991  ? 0.2651 0.2430 0.2641 0.0034  -0.0061 -0.0095 989  ILE A CG1 
7252  C CG2 . ILE A 991  ? 0.2303 0.2121 0.2250 0.0055  -0.0033 -0.0086 989  ILE A CG2 
7253  C CD1 . ILE A 991  ? 0.2804 0.2568 0.2833 0.0009  -0.0076 -0.0084 989  ILE A CD1 
7254  N N   . LYS A 992  ? 0.2343 0.2171 0.2344 0.0041  -0.0086 -0.0133 990  LYS A N   
7255  C CA  . LYS A 992  ? 0.2462 0.2303 0.2453 0.0061  -0.0096 -0.0160 990  LYS A CA  
7256  C C   . LYS A 992  ? 0.2182 0.2003 0.2165 0.0078  -0.0100 -0.0178 990  LYS A C   
7257  O O   . LYS A 992  ? 0.2572 0.2375 0.2582 0.0074  -0.0119 -0.0198 990  LYS A O   
7258  C CB  . LYS A 992  ? 0.2588 0.2439 0.2611 0.0047  -0.0118 -0.0175 990  LYS A CB  
7259  C CG  . LYS A 992  ? 0.2899 0.2777 0.2933 0.0030  -0.0114 -0.0158 990  LYS A CG  
7260  C CD  . LYS A 992  ? 0.3984 0.3870 0.4059 0.0013  -0.0138 -0.0171 990  LYS A CD  
7261  C CE  . LYS A 992  ? 0.4969 0.4889 0.5056 -0.0005 -0.0135 -0.0154 990  LYS A CE  
7262  N NZ  . LYS A 992  ? 0.5968 0.5896 0.6100 -0.0024 -0.0158 -0.0163 990  LYS A NZ  
7263  N N   . ALA A 993  ? 0.2223 0.2048 0.2171 0.0098  -0.0083 -0.0172 991  ALA A N   
7264  C CA  . ALA A 993  ? 0.2083 0.1899 0.2020 0.0117  -0.0083 -0.0188 991  ALA A CA  
7265  C C   . ALA A 993  ? 0.2336 0.2181 0.2233 0.0141  -0.0068 -0.0185 991  ALA A C   
7266  O O   . ALA A 993  ? 0.2464 0.2321 0.2347 0.0141  -0.0054 -0.0162 991  ALA A O   
7267  C CB  . ALA A 993  ? 0.2194 0.1977 0.2140 0.0108  -0.0076 -0.0173 991  ALA A CB  
7268  N N   . GLY A 994  ? 0.2065 0.1923 0.1949 0.0162  -0.0072 -0.0207 992  GLY A N   
7269  C CA  . GLY A 994  ? 0.2206 0.2102 0.2054 0.0185  -0.0060 -0.0202 992  GLY A CA  
7270  C C   . GLY A 994  ? 0.1973 0.1862 0.1803 0.0191  -0.0039 -0.0173 992  GLY A C   
7271  O O   . GLY A 994  ? 0.2018 0.1934 0.1826 0.0203  -0.0027 -0.0153 992  GLY A O   
7272  N N   . ASN A 995  ? 0.1986 0.1841 0.1828 0.0182  -0.0035 -0.0168 993  ASN A N   
7273  C CA  . ASN A 995  ? 0.2045 0.1894 0.1874 0.0187  -0.0016 -0.0143 993  ASN A CA  
7274  C C   . ASN A 995  ? 0.2029 0.1840 0.1877 0.0165  -0.0011 -0.0124 993  ASN A C   
7275  O O   . ASN A 995  ? 0.2064 0.1848 0.1934 0.0153  -0.0020 -0.0134 993  ASN A O   
7276  C CB  . ASN A 995  ? 0.2044 0.1902 0.1864 0.0204  -0.0015 -0.0159 993  ASN A CB  
7277  C CG  . ASN A 995  ? 0.2167 0.2078 0.1960 0.0228  -0.0013 -0.0166 993  ASN A CG  
7278  O OD1 . ASN A 995  ? 0.2192 0.2130 0.1984 0.0238  -0.0027 -0.0196 993  ASN A OD1 
7279  N ND2 . ASN A 995  ? 0.2302 0.2233 0.2076 0.0238  0.0005  -0.0137 993  ASN A ND2 
7280  N N   . LEU A 996  ? 0.1954 0.1764 0.1798 0.0159  0.0002  -0.0099 994  LEU A N   
7281  C CA  . LEU A 996  ? 0.2014 0.1799 0.1874 0.0140  0.0008  -0.0083 994  LEU A CA  
7282  C C   . LEU A 996  ? 0.1897 0.1674 0.1750 0.0145  0.0023  -0.0064 994  LEU A C   
7283  O O   . LEU A 996  ? 0.1961 0.1755 0.1799 0.0161  0.0032  -0.0054 994  LEU A O   
7284  C CB  . LEU A 996  ? 0.2039 0.1835 0.1906 0.0130  0.0010  -0.0073 994  LEU A CB  
7285  C CG  . LEU A 996  ? 0.2122 0.1936 0.1993 0.0128  -0.0004 -0.0088 994  LEU A CG  
7286  C CD1 . LEU A 996  ? 0.2616 0.2444 0.2496 0.0119  0.0000  -0.0079 994  LEU A CD1 
7287  C CD2 . LEU A 996  ? 0.2303 0.2103 0.2194 0.0114  -0.0020 -0.0104 994  LEU A CD2 
7288  N N   . TYR A 997  ? 0.1995 0.1748 0.1861 0.0131  0.0026  -0.0057 995  TYR A N   
7289  C CA  . TYR A 997  ? 0.1992 0.1736 0.1855 0.0134  0.0039  -0.0041 995  TYR A CA  
7290  C C   . TYR A 997  ? 0.1916 0.1647 0.1793 0.0115  0.0043  -0.0029 995  TYR A C   
7291  O O   . TYR A 997  ? 0.2189 0.1911 0.2079 0.0098  0.0034  -0.0032 995  TYR A O   
7292  C CB  . TYR A 997  ? 0.2165 0.1896 0.2028 0.0140  0.0036  -0.0049 995  TYR A CB  
7293  C CG  . TYR A 997  ? 0.2095 0.1847 0.1945 0.0160  0.0031  -0.0067 995  TYR A CG  
7294  C CD1 . TYR A 997  ? 0.2222 0.1998 0.2053 0.0178  0.0042  -0.0059 995  TYR A CD1 
7295  C CD2 . TYR A 997  ? 0.2191 0.1944 0.2049 0.0160  0.0014  -0.0093 995  TYR A CD2 
7296  C CE1 . TYR A 997  ? 0.2291 0.2099 0.2108 0.0198  0.0038  -0.0077 995  TYR A CE1 
7297  C CE2 . TYR A 997  ? 0.2606 0.2384 0.2452 0.0180  0.0008  -0.0115 995  TYR A CE2 
7298  C CZ  . TYR A 997  ? 0.2501 0.2310 0.2325 0.0199  0.0021  -0.0108 995  TYR A CZ  
7299  O OH  . TYR A 997  ? 0.2973 0.2818 0.2782 0.0220  0.0016  -0.0131 995  TYR A OH  
7300  N N   . ILE A 998  ? 0.1845 0.1580 0.1722 0.0116  0.0055  -0.0015 996  ILE A N   
7301  C CA  A ILE A 998  ? 0.1988 0.1721 0.1878 0.0101  0.0059  -0.0008 996  ILE A CA  
7302  C CA  B ILE A 998  ? 0.1987 0.1720 0.1877 0.0101  0.0059  -0.0009 996  ILE A CA  
7303  C C   . ILE A 998  ? 0.1999 0.1719 0.1892 0.0102  0.0068  0.0002  996  ILE A C   
7304  O O   . ILE A 998  ? 0.2018 0.1739 0.1910 0.0114  0.0076  0.0011  996  ILE A O   
7305  C CB  A ILE A 998  ? 0.2208 0.1958 0.2105 0.0103  0.0062  -0.0008 996  ILE A CB  
7306  C CB  B ILE A 998  ? 0.2207 0.1957 0.2104 0.0102  0.0062  -0.0008 996  ILE A CB  
7307  C CG1 A ILE A 998  ? 0.2375 0.2140 0.2268 0.0106  0.0054  -0.0018 996  ILE A CG1 
7308  C CG1 B ILE A 998  ? 0.2379 0.2144 0.2275 0.0099  0.0052  -0.0019 996  ILE A CG1 
7309  C CG2 A ILE A 998  ? 0.2120 0.1878 0.2031 0.0087  0.0065  -0.0009 996  ILE A CG2 
7310  C CG2 B ILE A 998  ? 0.2126 0.1881 0.2037 0.0089  0.0067  -0.0007 996  ILE A CG2 
7311  C CD1 A ILE A 998  ? 0.2306 0.2074 0.2204 0.0089  0.0044  -0.0026 996  ILE A CD1 
7312  C CD1 B ILE A 998  ? 0.2605 0.2389 0.2509 0.0104  0.0054  -0.0021 996  ILE A CD1 
7313  N N   . ASN A 999  ? 0.1902 0.1613 0.1803 0.0087  0.0065  0.0005  997  ASN A N   
7314  C CA  . ASN A 999  ? 0.1937 0.1639 0.1842 0.0085  0.0072  0.0014  997  ASN A CA  
7315  C C   . ASN A 999  ? 0.1969 0.1660 0.1867 0.0099  0.0076  0.0017  997  ASN A C   
7316  O O   . ASN A 999  ? 0.2130 0.1818 0.2032 0.0104  0.0085  0.0027  997  ASN A O   
7317  C CB  . ASN A 999  ? 0.1908 0.1620 0.1823 0.0083  0.0080  0.0017  997  ASN A CB  
7318  C CG  . ASN A 999  ? 0.1909 0.1640 0.1832 0.0068  0.0077  0.0011  997  ASN A CG  
7319  O OD1 . ASN A 999  ? 0.2120 0.1855 0.2042 0.0054  0.0071  0.0013  997  ASN A OD1 
7320  N ND2 . ASN A 999  ? 0.2213 0.1959 0.2146 0.0071  0.0081  0.0004  997  ASN A ND2 
7321  N N   . ARG A 1000 ? 0.1980 0.1667 0.1871 0.0107  0.0069  0.0008  998  ARG A N   
7322  C CA  . ARG A 1000 ? 0.1976 0.1662 0.1861 0.0122  0.0072  0.0007  998  ARG A CA  
7323  C C   . ARG A 1000 ? 0.2265 0.1943 0.2153 0.0124  0.0058  -0.0011 998  ARG A C   
7324  O O   . ARG A 1000 ? 0.2333 0.2004 0.2230 0.0112  0.0046  -0.0017 998  ARG A O   
7325  C CB  . ARG A 1000 ? 0.1985 0.1690 0.1857 0.0140  0.0080  0.0011  998  ARG A CB  
7326  C CG  . ARG A 1000 ? 0.2101 0.1821 0.1965 0.0144  0.0074  0.0003  998  ARG A CG  
7327  C CD  . ARG A 1000 ? 0.2214 0.1960 0.2063 0.0164  0.0078  0.0004  998  ARG A CD  
7328  N NE  . ARG A 1000 ? 0.1937 0.1690 0.1777 0.0175  0.0073  -0.0013 998  ARG A NE  
7329  C CZ  . ARG A 1000 ? 0.2198 0.1983 0.2023 0.0194  0.0076  -0.0015 998  ARG A CZ  
7330  N NH1 . ARG A 1000 ? 0.2309 0.2121 0.2125 0.0203  0.0084  0.0004  998  ARG A NH1 
7331  N NH2 . ARG A 1000 ? 0.2302 0.2096 0.2124 0.0205  0.0071  -0.0036 998  ARG A NH2 
7332  N N   . ASN A 1001 ? 0.2072 0.1753 0.1956 0.0140  0.0058  -0.0019 999  ASN A N   
7333  C CA  . ASN A 1001 ? 0.2017 0.1692 0.1910 0.0145  0.0043  -0.0042 999  ASN A CA  
7334  C C   . ASN A 1001 ? 0.2265 0.1958 0.2147 0.0153  0.0037  -0.0059 999  ASN A C   
7335  O O   . ASN A 1001 ? 0.2249 0.1961 0.2115 0.0157  0.0045  -0.0050 999  ASN A O   
7336  C CB  . ASN A 1001 ? 0.2332 0.2010 0.2227 0.0161  0.0045  -0.0052 999  ASN A CB  
7337  C CG  . ASN A 1001 ? 0.2487 0.2200 0.2360 0.0183  0.0057  -0.0054 999  ASN A CG  
7338  O OD1 . ASN A 1001 ? 0.2544 0.2280 0.2402 0.0192  0.0055  -0.0063 999  ASN A OD1 
7339  N ND2 . ASN A 1001 ? 0.3215 0.2937 0.3085 0.0192  0.0068  -0.0045 999  ASN A ND2 
7340  N N   . ILE A 1002 ? 0.2048 0.1735 0.1943 0.0156  0.0020  -0.0083 1000 ILE A N   
7341  C CA  . ILE A 1002 ? 0.2264 0.1969 0.2153 0.0162  0.0011  -0.0102 1000 ILE A CA  
7342  C C   . ILE A 1002 ? 0.2326 0.2057 0.2206 0.0186  0.0006  -0.0130 1000 ILE A C   
7343  O O   . ILE A 1002 ? 0.2457 0.2201 0.2339 0.0192  -0.0007 -0.0155 1000 ILE A O   
7344  C CB  . ILE A 1002 ? 0.2146 0.1830 0.2061 0.0143  -0.0008 -0.0109 1000 ILE A CB  
7345  C CG1 . ILE A 1002 ? 0.2265 0.1925 0.2213 0.0142  -0.0026 -0.0127 1000 ILE A CG1 
7346  C CG2 . ILE A 1002 ? 0.2146 0.1818 0.2066 0.0119  -0.0002 -0.0080 1000 ILE A CG2 
7347  C CD1 . ILE A 1002 ? 0.2314 0.1957 0.2295 0.0123  -0.0047 -0.0133 1000 ILE A CD1 
7348  N N   A ILE A 1003 ? 0.2293 0.2037 0.2165 0.0201  0.0017  -0.0130 1001 ILE A N   
7349  N N   B ILE A 1003 ? 0.2286 0.2031 0.2156 0.0202  0.0018  -0.0128 1001 ILE A N   
7350  C CA  A ILE A 1003 ? 0.2495 0.2273 0.2358 0.0226  0.0013  -0.0160 1001 ILE A CA  
7351  C CA  B ILE A 1003 ? 0.2498 0.2275 0.2361 0.0226  0.0014  -0.0158 1001 ILE A CA  
7352  C C   A ILE A 1003 ? 0.2798 0.2627 0.2627 0.0243  0.0029  -0.0148 1001 ILE A C   
7353  C C   B ILE A 1003 ? 0.2419 0.2240 0.2252 0.0242  0.0034  -0.0141 1001 ILE A C   
7354  O O   A ILE A 1003 ? 0.2705 0.2577 0.2521 0.0265  0.0030  -0.0168 1001 ILE A O   
7355  O O   B ILE A 1003 ? 0.2548 0.2367 0.2372 0.0234  0.0049  -0.0106 1001 ILE A O   
7356  C CB  A ILE A 1003 ? 0.2417 0.2185 0.2298 0.0235  0.0010  -0.0174 1001 ILE A CB  
7357  C CB  B ILE A 1003 ? 0.2395 0.2151 0.2286 0.0231  0.0004  -0.0178 1001 ILE A CB  
7358  C CG1 A ILE A 1003 ? 0.2465 0.2228 0.2340 0.0231  0.0029  -0.0141 1001 ILE A CG1 
7359  C CG1 B ILE A 1003 ? 0.2294 0.2038 0.2185 0.0227  0.0020  -0.0150 1001 ILE A CG1 
7360  C CG2 A ILE A 1003 ? 0.2510 0.2233 0.2432 0.0221  -0.0011 -0.0189 1001 ILE A CG2 
7361  C CG2 B ILE A 1003 ? 0.2323 0.2037 0.2253 0.0214  -0.0018 -0.0191 1001 ILE A CG2 
7362  C CD1 A ILE A 1003 ? 0.2794 0.2557 0.2685 0.0243  0.0029  -0.0154 1001 ILE A CD1 
7363  C CD1 B ILE A 1003 ? 0.2679 0.2419 0.2592 0.0239  0.0014  -0.0171 1001 ILE A CD1 
7364  N N   A GLY A 1004 ? 0.2726 0.2555 0.2542 0.0233  0.0039  -0.0118 1002 GLY A N   
7365  N N   B GLY A 1004 ? 0.2586 0.2453 0.2407 0.0266  0.0033  -0.0166 1002 GLY A N   
7366  C CA  A GLY A 1004 ? 0.2392 0.2267 0.2183 0.0246  0.0052  -0.0098 1002 GLY A CA  
7367  C CA  B GLY A 1004 ? 0.2682 0.2603 0.2476 0.0282  0.0051  -0.0148 1002 GLY A CA  
7368  C C   A GLY A 1004 ? 0.2345 0.2263 0.2119 0.0260  0.0043  -0.0119 1002 GLY A C   
7369  C C   B GLY A 1004 ? 0.2429 0.2376 0.2200 0.0281  0.0058  -0.0122 1002 GLY A C   
7370  O O   A GLY A 1004 ? 0.2533 0.2440 0.2312 0.0252  0.0032  -0.0129 1002 GLY A O   
7371  O O   B GLY A 1004 ? 0.2687 0.2652 0.2449 0.0280  0.0075  -0.0085 1002 GLY A O   
7372  N N   A ALA A 1005 ? 0.2240 0.2214 0.1995 0.0282  0.0049  -0.0125 1003 ALA A N   
7373  N N   B ALA A 1005 ? 0.2498 0.2450 0.2267 0.0280  0.0045  -0.0140 1003 ALA A N   
7374  C CA  A ALA A 1005 ? 0.2418 0.2447 0.2153 0.0298  0.0042  -0.0141 1003 ALA A CA  
7375  C CA  B ALA A 1005 ? 0.2262 0.2242 0.2012 0.0281  0.0050  -0.0117 1003 ALA A CA  
7376  C C   A ALA A 1005 ? 0.2536 0.2627 0.2246 0.0313  0.0058  -0.0111 1003 ALA A C   
7377  C C   B ALA A 1005 ? 0.2459 0.2509 0.2184 0.0301  0.0062  -0.0103 1003 ALA A C   
7378  O O   A ALA A 1005 ? 0.2371 0.2528 0.2061 0.0333  0.0056  -0.0129 1003 ALA A O   
7379  O O   B ALA A 1005 ? 0.2744 0.2838 0.2460 0.0320  0.0060  -0.0130 1003 ALA A O   
7380  C CB  A ALA A 1005 ? 0.2348 0.2395 0.2087 0.0313  0.0026  -0.0195 1003 ALA A CB  
7381  C CB  B ALA A 1005 ? 0.2517 0.2503 0.2267 0.0281  0.0032  -0.0147 1003 ALA A CB  
7382  N N   A VAL A 1006 ? 0.2380 0.2457 0.2095 0.0302  0.0073  -0.0065 1004 VAL A N   
7383  N N   B VAL A 1006 ? 0.2427 0.2491 0.2145 0.0298  0.0074  -0.0059 1004 VAL A N   
7384  C CA  A VAL A 1006 ? 0.2308 0.2440 0.2008 0.0313  0.0088  -0.0027 1004 VAL A CA  
7385  C CA  B VAL A 1006 ? 0.2311 0.2440 0.2011 0.0313  0.0087  -0.0030 1004 VAL A CA  
7386  C C   A VAL A 1006 ? 0.2318 0.2503 0.1999 0.0323  0.0083  -0.0020 1004 VAL A C   
7387  C C   B VAL A 1006 ? 0.2339 0.2522 0.2020 0.0323  0.0081  -0.0028 1004 VAL A C   
7388  O O   A VAL A 1006 ? 0.2133 0.2295 0.1822 0.0313  0.0078  -0.0005 1004 VAL A O   
7389  O O   B VAL A 1006 ? 0.2213 0.2371 0.1900 0.0314  0.0073  -0.0021 1004 VAL A O   
7390  C CB  A VAL A 1006 ? 0.2296 0.2392 0.2014 0.0298  0.0101  0.0021  1004 VAL A CB  
7391  C CB  B VAL A 1006 ? 0.2295 0.2403 0.2010 0.0301  0.0101  0.0021  1004 VAL A CB  
7392  C CG1 A VAL A 1006 ? 0.2508 0.2664 0.2219 0.0307  0.0114  0.0065  1004 VAL A CG1 
7393  C CG1 B VAL A 1006 ? 0.2482 0.2660 0.2184 0.0313  0.0113  0.0060  1004 VAL A CG1 
7394  C CG2 A VAL A 1006 ? 0.2368 0.2419 0.2104 0.0288  0.0105  0.0013  1004 VAL A CG2 
7395  C CG2 B VAL A 1006 ? 0.2367 0.2433 0.2099 0.0292  0.0107  0.0017  1004 VAL A CG2 
7396  N N   . VAL A 1007 ? 0.2176 0.2438 0.1833 0.0344  0.0084  -0.0033 1005 VAL A N   
7397  C CA  . VAL A 1007 ? 0.2185 0.2510 0.1821 0.0357  0.0077  -0.0032 1005 VAL A CA  
7398  C C   . VAL A 1007 ? 0.2155 0.2480 0.1798 0.0348  0.0083  0.0026  1005 VAL A C   
7399  O O   . VAL A 1007 ? 0.2365 0.2691 0.2018 0.0343  0.0097  0.0072  1005 VAL A O   
7400  C CB  . VAL A 1007 ? 0.2143 0.2564 0.1752 0.0381  0.0082  -0.0044 1005 VAL A CB  
7401  C CG1 . VAL A 1007 ? 0.2357 0.2854 0.1942 0.0394  0.0077  -0.0034 1005 VAL A CG1 
7402  C CG2 . VAL A 1007 ? 0.2471 0.2890 0.2081 0.0392  0.0072  -0.0109 1005 VAL A CG2 
7403  N N   . GLY A 1008 ? 0.2192 0.2514 0.1834 0.0345  0.0072  0.0024  1006 GLY A N   
7404  C CA  . GLY A 1008 ? 0.2220 0.2543 0.1873 0.0339  0.0074  0.0076  1006 GLY A CA  
7405  C C   . GLY A 1008 ? 0.2278 0.2521 0.1965 0.0319  0.0079  0.0098  1006 GLY A C   
7406  O O   . GLY A 1008 ? 0.2589 0.2826 0.2295 0.0314  0.0079  0.0138  1006 GLY A O   
7407  N N   . VAL A 1009 ? 0.2209 0.2393 0.1907 0.0308  0.0080  0.0072  1007 VAL A N   
7408  C CA  . VAL A 1009 ? 0.2371 0.2485 0.2100 0.0289  0.0084  0.0087  1007 VAL A CA  
7409  C C   . VAL A 1009 ? 0.2301 0.2361 0.2037 0.0276  0.0073  0.0048  1007 VAL A C   
7410  O O   . VAL A 1009 ? 0.2269 0.2294 0.2023 0.0264  0.0069  0.0054  1007 VAL A O   
7411  C CB  . VAL A 1009 ? 0.2299 0.2398 0.2038 0.0285  0.0097  0.0104  1007 VAL A CB  
7412  C CG1 . VAL A 1009 ? 0.2398 0.2431 0.2169 0.0266  0.0100  0.0117  1007 VAL A CG1 
7413  C CG2 . VAL A 1009 ? 0.2498 0.2656 0.2234 0.0295  0.0108  0.0148  1007 VAL A CG2 
7414  N N   . GLN A 1010 ? 0.2274 0.2331 0.2000 0.0279  0.0067  0.0008  1008 GLN A N   
7415  C CA  . GLN A 1010 ? 0.2372 0.2395 0.2104 0.0269  0.0053  -0.0029 1008 GLN A CA  
7416  C C   . GLN A 1010 ? 0.2194 0.2264 0.1907 0.0285  0.0041  -0.0064 1008 GLN A C   
7417  O O   . GLN A 1010 ? 0.2543 0.2615 0.2254 0.0291  0.0036  -0.0098 1008 GLN A O   
7418  C CB  . GLN A 1010 ? 0.2524 0.2495 0.2272 0.0256  0.0053  -0.0046 1008 GLN A CB  
7419  C CG  . GLN A 1010 ? 0.2243 0.2175 0.2010 0.0241  0.0064  -0.0016 1008 GLN A CG  
7420  C CD  . GLN A 1010 ? 0.2452 0.2389 0.2217 0.0247  0.0077  0.0000  1008 GLN A CD  
7421  O OE1 . GLN A 1010 ? 0.2457 0.2413 0.2213 0.0257  0.0076  -0.0020 1008 GLN A OE1 
7422  N NE2 . GLN A 1010 ? 0.2483 0.2407 0.2263 0.0240  0.0088  0.0034  1008 GLN A NE2 
7423  N N   . PRO A 1011 ? 0.2321 0.2433 0.2022 0.0294  0.0036  -0.0058 1009 PRO A N   
7424  C CA  . PRO A 1011 ? 0.2177 0.2330 0.1862 0.0307  0.0021  -0.0097 1009 PRO A CA  
7425  C C   . PRO A 1011 ? 0.2076 0.2181 0.1781 0.0295  0.0006  -0.0140 1009 PRO A C   
7426  O O   . PRO A 1011 ? 0.2066 0.2118 0.1792 0.0275  0.0004  -0.0133 1009 PRO A O   
7427  C CB  . PRO A 1011 ? 0.2164 0.2344 0.1845 0.0308  0.0015  -0.0080 1009 PRO A CB  
7428  C CG  . PRO A 1011 ? 0.2352 0.2534 0.2037 0.0307  0.0030  -0.0026 1009 PRO A CG  
7429  C CD  . PRO A 1011 ? 0.2201 0.2320 0.1907 0.0291  0.0040  -0.0017 1009 PRO A CD  
7430  N N   . PHE A 1012 ? 0.2124 0.2251 0.1826 0.0307  -0.0004 -0.0182 1010 PHE A N   
7431  C CA  . PHE A 1012 ? 0.2094 0.2170 0.1823 0.0297  -0.0016 -0.0216 1010 PHE A CA  
7432  C C   . PHE A 1012 ? 0.2308 0.2397 0.2046 0.0300  -0.0039 -0.0261 1010 PHE A C   
7433  O O   . PHE A 1012 ? 0.2388 0.2539 0.2108 0.0320  -0.0046 -0.0287 1010 PHE A O   
7434  C CB  . PHE A 1012 ? 0.2030 0.2108 0.1762 0.0307  -0.0012 -0.0233 1010 PHE A CB  
7435  C CG  . PHE A 1012 ? 0.2117 0.2137 0.1883 0.0295  -0.0026 -0.0261 1010 PHE A CG  
7436  C CD1 . PHE A 1012 ? 0.2323 0.2283 0.2109 0.0273  -0.0020 -0.0234 1010 PHE A CD1 
7437  C CD2 . PHE A 1012 ? 0.2251 0.2280 0.2035 0.0305  -0.0047 -0.0313 1010 PHE A CD2 
7438  C CE1 . PHE A 1012 ? 0.2424 0.2334 0.2245 0.0260  -0.0033 -0.0253 1010 PHE A CE1 
7439  C CE2 . PHE A 1012 ? 0.2388 0.2360 0.2213 0.0292  -0.0062 -0.0334 1010 PHE A CE2 
7440  C CZ  . PHE A 1012 ? 0.2380 0.2293 0.2223 0.0269  -0.0055 -0.0301 1010 PHE A CZ  
7441  N N   . GLY A 1013 ? 0.2364 0.2400 0.2133 0.0279  -0.0052 -0.0271 1011 GLY A N   
7442  C CA  . GLY A 1013 ? 0.2259 0.2298 0.2048 0.0279  -0.0077 -0.0315 1011 GLY A CA  
7443  C C   . GLY A 1013 ? 0.2276 0.2271 0.2092 0.0253  -0.0085 -0.0303 1011 GLY A C   
7444  O O   . GLY A 1013 ? 0.2342 0.2327 0.2149 0.0241  -0.0072 -0.0265 1011 GLY A O   
7445  N N   . GLY A 1014 ? 0.2294 0.2263 0.2145 0.0243  -0.0107 -0.0336 1012 GLY A N   
7446  C CA  . GLY A 1014 ? 0.2589 0.2519 0.2471 0.0216  -0.0116 -0.0324 1012 GLY A CA  
7447  C C   . GLY A 1014 ? 0.2503 0.2452 0.2401 0.0213  -0.0137 -0.0350 1012 GLY A C   
7448  O O   . GLY A 1014 ? 0.2570 0.2569 0.2448 0.0233  -0.0143 -0.0375 1012 GLY A O   
7449  N N   . ARG A 1015 ? 0.2333 0.2245 0.2268 0.0187  -0.0148 -0.0343 1013 ARG A N   
7450  C CA  . ARG A 1015 ? 0.2352 0.2279 0.2309 0.0178  -0.0167 -0.0360 1013 ARG A CA  
7451  C C   . ARG A 1015 ? 0.2309 0.2196 0.2324 0.0159  -0.0192 -0.0380 1013 ARG A C   
7452  O O   . ARG A 1015 ? 0.2335 0.2185 0.2373 0.0153  -0.0194 -0.0378 1013 ARG A O   
7453  C CB  . ARG A 1015 ? 0.2380 0.2309 0.2328 0.0161  -0.0154 -0.0321 1013 ARG A CB  
7454  C CG  . ARG A 1015 ? 0.2604 0.2489 0.2574 0.0136  -0.0146 -0.0288 1013 ARG A CG  
7455  C CD  . ARG A 1015 ? 0.2807 0.2699 0.2779 0.0118  -0.0138 -0.0259 1013 ARG A CD  
7456  N NE  . ARG A 1015 ? 0.3421 0.3342 0.3405 0.0117  -0.0154 -0.0278 1013 ARG A NE  
7457  C CZ  . ARG A 1015 ? 0.3786 0.3698 0.3812 0.0100  -0.0177 -0.0296 1013 ARG A CZ  
7458  N NH1 . ARG A 1015 ? 0.3580 0.3454 0.3646 0.0082  -0.0188 -0.0295 1013 ARG A NH1 
7459  N NH2 . ARG A 1015 ? 0.3301 0.3244 0.3335 0.0101  -0.0191 -0.0314 1013 ARG A NH2 
7460  N N   . GLY A 1016 ? 0.2496 0.2392 0.2539 0.0147  -0.0212 -0.0396 1014 GLY A N   
7461  C CA  . GLY A 1016 ? 0.2628 0.2488 0.2736 0.0128  -0.0239 -0.0413 1014 GLY A CA  
7462  C C   . GLY A 1016 ? 0.2317 0.2169 0.2447 0.0146  -0.0257 -0.0460 1014 GLY A C   
7463  O O   . GLY A 1016 ? 0.2551 0.2444 0.2656 0.0174  -0.0260 -0.0499 1014 GLY A O   
7464  N N   . LEU A 1017 ? 0.2377 0.2179 0.2557 0.0131  -0.0269 -0.0457 1015 LEU A N   
7465  C CA  . LEU A 1017 ? 0.2541 0.2330 0.2752 0.0148  -0.0288 -0.0503 1015 LEU A CA  
7466  C C   . LEU A 1017 ? 0.2369 0.2179 0.2530 0.0177  -0.0266 -0.0509 1015 LEU A C   
7467  O O   . LEU A 1017 ? 0.2523 0.2333 0.2703 0.0197  -0.0279 -0.0552 1015 LEU A O   
7468  C CB  . LEU A 1017 ? 0.2597 0.2325 0.2877 0.0124  -0.0306 -0.0489 1015 LEU A CB  
7469  C CG  . LEU A 1017 ? 0.2770 0.2477 0.3116 0.0093  -0.0332 -0.0482 1015 LEU A CG  
7470  C CD1 . LEU A 1017 ? 0.2872 0.2523 0.3283 0.0068  -0.0345 -0.0455 1015 LEU A CD1 
7471  C CD2 . LEU A 1017 ? 0.2811 0.2537 0.3193 0.0106  -0.0364 -0.0545 1015 LEU A CD2 
7472  N N   . SER A 1018 ? 0.2198 0.2026 0.2300 0.0180  -0.0234 -0.0468 1016 SER A N   
7473  C CA  . SER A 1018 ? 0.2363 0.2210 0.2421 0.0203  -0.0212 -0.0465 1016 SER A CA  
7474  C C   . SER A 1018 ? 0.2044 0.1959 0.2048 0.0232  -0.0203 -0.0485 1016 SER A C   
7475  O O   . SER A 1018 ? 0.2362 0.2302 0.2333 0.0253  -0.0186 -0.0485 1016 SER A O   
7476  C CB  . SER A 1018 ? 0.2380 0.2204 0.2410 0.0188  -0.0184 -0.0406 1016 SER A CB  
7477  O OG  . SER A 1018 ? 0.2295 0.2065 0.2371 0.0163  -0.0192 -0.0386 1016 SER A OG  
7478  N N   . GLY A 1019 ? 0.2295 0.2244 0.2291 0.0233  -0.0212 -0.0497 1017 GLY A N   
7479  C CA  . GLY A 1019 ? 0.2333 0.2352 0.2278 0.0261  -0.0202 -0.0511 1017 GLY A CA  
7480  C C   . GLY A 1019 ? 0.2396 0.2453 0.2331 0.0260  -0.0211 -0.0515 1017 GLY A C   
7481  O O   . GLY A 1019 ? 0.2637 0.2666 0.2592 0.0235  -0.0214 -0.0491 1017 GLY A O   
7482  N N   . THR A 1020 ? 0.2511 0.2636 0.2415 0.0286  -0.0214 -0.0545 1018 THR A N   
7483  C CA  . THR A 1020 ? 0.2400 0.2575 0.2283 0.0290  -0.0218 -0.0543 1018 THR A CA  
7484  C C   . THR A 1020 ? 0.2248 0.2455 0.2079 0.0297  -0.0190 -0.0490 1018 THR A C   
7485  O O   . THR A 1020 ? 0.2433 0.2665 0.2250 0.0294  -0.0189 -0.0471 1018 THR A O   
7486  C CB  . THR A 1020 ? 0.2356 0.2600 0.2231 0.0316  -0.0237 -0.0602 1018 THR A CB  
7487  O OG1 . THR A 1020 ? 0.2436 0.2728 0.2272 0.0344  -0.0223 -0.0609 1018 THR A OG1 
7488  C CG2 . THR A 1020 ? 0.2870 0.3084 0.2807 0.0311  -0.0270 -0.0661 1018 THR A CG2 
7489  N N   . GLY A 1021 ? 0.2510 0.2719 0.2314 0.0307  -0.0169 -0.0468 1019 GLY A N   
7490  C CA  . GLY A 1021 ? 0.2587 0.2841 0.2344 0.0320  -0.0146 -0.0426 1019 GLY A CA  
7491  C C   . GLY A 1021 ? 0.2477 0.2823 0.2203 0.0347  -0.0153 -0.0452 1019 GLY A C   
7492  O O   . GLY A 1021 ? 0.2428 0.2802 0.2167 0.0357  -0.0176 -0.0508 1019 GLY A O   
7493  N N   . PRO A 1022 ? 0.2406 0.2802 0.2092 0.0359  -0.0135 -0.0410 1020 PRO A N   
7494  C CA  . PRO A 1022 ? 0.2374 0.2741 0.2048 0.0350  -0.0110 -0.0347 1020 PRO A CA  
7495  C C   . PRO A 1022 ? 0.2544 0.2886 0.2218 0.0352  -0.0095 -0.0340 1020 PRO A C   
7496  O O   . PRO A 1022 ? 0.2635 0.2992 0.2312 0.0364  -0.0102 -0.0382 1020 PRO A O   
7497  C CB  . PRO A 1022 ? 0.2448 0.2895 0.2085 0.0368  -0.0102 -0.0315 1020 PRO A CB  
7498  C CG  . PRO A 1022 ? 0.2699 0.3227 0.2316 0.0393  -0.0114 -0.0364 1020 PRO A CG  
7499  C CD  . PRO A 1022 ? 0.2398 0.2893 0.2049 0.0385  -0.0139 -0.0425 1020 PRO A CD  
7500  N N   . LYS A 1023 ? 0.2363 0.2665 0.2037 0.0340  -0.0075 -0.0289 1021 LYS A N   
7501  C CA  . LYS A 1023 ? 0.2260 0.2531 0.1937 0.0338  -0.0060 -0.0277 1021 LYS A CA  
7502  C C   . LYS A 1023 ? 0.2349 0.2691 0.1995 0.0362  -0.0049 -0.0274 1021 LYS A C   
7503  O O   . LYS A 1023 ? 0.2318 0.2719 0.1938 0.0373  -0.0040 -0.0241 1021 LYS A O   
7504  C CB  . LYS A 1023 ? 0.2180 0.2401 0.1864 0.0320  -0.0042 -0.0223 1021 LYS A CB  
7505  C CG  . LYS A 1023 ? 0.2136 0.2284 0.1853 0.0295  -0.0048 -0.0223 1021 LYS A CG  
7506  C CD  . LYS A 1023 ? 0.2179 0.2296 0.1899 0.0283  -0.0030 -0.0173 1021 LYS A CD  
7507  C CE  . LYS A 1023 ? 0.2204 0.2254 0.1953 0.0257  -0.0033 -0.0171 1021 LYS A CE  
7508  N NZ  . LYS A 1023 ? 0.2298 0.2307 0.2061 0.0250  -0.0031 -0.0182 1021 LYS A NZ  
7509  N N   . ALA A 1024 ? 0.2415 0.2754 0.2067 0.0370  -0.0049 -0.0305 1022 ALA A N   
7510  C CA  . ALA A 1024 ? 0.2480 0.2879 0.2106 0.0390  -0.0034 -0.0295 1022 ALA A CA  
7511  C C   . ALA A 1024 ? 0.2361 0.2736 0.1982 0.0379  -0.0010 -0.0230 1022 ALA A C   
7512  O O   . ALA A 1024 ? 0.2396 0.2695 0.2040 0.0357  -0.0006 -0.0208 1022 ALA A O   
7513  C CB  . ALA A 1024 ? 0.2563 0.2950 0.2205 0.0398  -0.0039 -0.0342 1022 ALA A CB  
7514  N N   . GLY A 1025 ? 0.2335 0.2783 0.1930 0.0394  0.0004  -0.0198 1023 GLY A N   
7515  C CA  . GLY A 1025 ? 0.2436 0.2868 0.2032 0.0385  0.0024  -0.0136 1023 GLY A CA  
7516  C C   . GLY A 1025 ? 0.2325 0.2724 0.1931 0.0370  0.0024  -0.0094 1023 GLY A C   
7517  O O   . GLY A 1025 ? 0.2344 0.2701 0.1965 0.0357  0.0037  -0.0050 1023 GLY A O   
7518  N N   . GLY A 1026 ? 0.2253 0.2670 0.1854 0.0372  0.0009  -0.0110 1024 GLY A N   
7519  C CA  . GLY A 1026 ? 0.2105 0.2500 0.1717 0.0361  0.0007  -0.0075 1024 GLY A CA  
7520  C C   . GLY A 1026 ? 0.2202 0.2680 0.1792 0.0376  0.0001  -0.0062 1024 GLY A C   
7521  O O   . GLY A 1026 ? 0.2240 0.2795 0.1804 0.0395  -0.0003 -0.0087 1024 GLY A O   
7522  N N   . PRO A 1027 ? 0.2138 0.2606 0.1740 0.0369  -0.0001 -0.0024 1025 PRO A N   
7523  C CA  . PRO A 1027 ? 0.2205 0.2753 0.1789 0.0384  -0.0004 0.0005  1025 PRO A CA  
7524  C C   . PRO A 1027 ? 0.2084 0.2673 0.1655 0.0392  -0.0024 -0.0036 1025 PRO A C   
7525  O O   . PRO A 1027 ? 0.2207 0.2874 0.1759 0.0406  -0.0029 -0.0017 1025 PRO A O   
7526  C CB  . PRO A 1027 ? 0.2406 0.2913 0.2019 0.0372  0.0000  0.0060  1025 PRO A CB  
7527  C CG  . PRO A 1027 ? 0.2398 0.2811 0.2039 0.0352  -0.0002 0.0035  1025 PRO A CG  
7528  C CD  . PRO A 1027 ? 0.2102 0.2489 0.1737 0.0349  0.0003  0.0000  1025 PRO A CD  
7529  N N   . LEU A 1028 ? 0.2158 0.2699 0.1741 0.0384  -0.0036 -0.0090 1026 LEU A N   
7530  C CA  . LEU A 1028 ? 0.2112 0.2691 0.1687 0.0391  -0.0057 -0.0133 1026 LEU A CA  
7531  C C   . LEU A 1028 ? 0.2274 0.2909 0.1828 0.0408  -0.0065 -0.0189 1026 LEU A C   
7532  O O   . LEU A 1028 ? 0.2479 0.3159 0.2025 0.0418  -0.0083 -0.0229 1026 LEU A O   
7533  C CB  . LEU A 1028 ? 0.2200 0.2701 0.1806 0.0371  -0.0069 -0.0160 1026 LEU A CB  
7534  C CG  . LEU A 1028 ? 0.2579 0.3043 0.2206 0.0357  -0.0066 -0.0118 1026 LEU A CG  
7535  C CD1 . LEU A 1028 ? 0.2619 0.3011 0.2278 0.0336  -0.0075 -0.0145 1026 LEU A CD1 
7536  C CD2 . LEU A 1028 ? 0.3432 0.3966 0.3047 0.0370  -0.0076 -0.0101 1026 LEU A CD2 
7537  N N   . TYR A 1029 ? 0.2186 0.2824 0.1734 0.0414  -0.0053 -0.0193 1027 TYR A N   
7538  C CA  . TYR A 1029 ? 0.2291 0.2966 0.1828 0.0429  -0.0062 -0.0255 1027 TYR A CA  
7539  C C   . TYR A 1029 ? 0.2227 0.3022 0.1729 0.0455  -0.0068 -0.0268 1027 TYR A C   
7540  O O   . TYR A 1029 ? 0.2352 0.3184 0.1852 0.0466  -0.0087 -0.0329 1027 TYR A O   
7541  C CB  . TYR A 1029 ? 0.2375 0.3029 0.1914 0.0430  -0.0044 -0.0247 1027 TYR A CB  
7542  C CG  . TYR A 1029 ? 0.2264 0.2917 0.1811 0.0439  -0.0053 -0.0313 1027 TYR A CG  
7543  C CD1 . TYR A 1029 ? 0.2465 0.3038 0.2048 0.0425  -0.0069 -0.0357 1027 TYR A CD1 
7544  C CD2 . TYR A 1029 ? 0.2291 0.3021 0.1815 0.0462  -0.0045 -0.0328 1027 TYR A CD2 
7545  C CE1 . TYR A 1029 ? 0.2314 0.2879 0.1913 0.0434  -0.0080 -0.0415 1027 TYR A CE1 
7546  C CE2 . TYR A 1029 ? 0.2370 0.3095 0.1908 0.0472  -0.0054 -0.0390 1027 TYR A CE2 
7547  C CZ  . TYR A 1029 ? 0.2294 0.2935 0.1871 0.0458  -0.0072 -0.0434 1027 TYR A CZ  
7548  O OH  . TYR A 1029 ? 0.2651 0.3285 0.2249 0.0470  -0.0083 -0.0494 1027 TYR A OH  
7549  N N   . LEU A 1030 ? 0.2211 0.3075 0.1688 0.0464  -0.0052 -0.0212 1028 LEU A N   
7550  C CA  . LEU A 1030 ? 0.2226 0.3218 0.1666 0.0489  -0.0057 -0.0222 1028 LEU A CA  
7551  C C   . LEU A 1030 ? 0.2498 0.3524 0.1933 0.0493  -0.0078 -0.0242 1028 LEU A C   
7552  O O   . LEU A 1030 ? 0.2475 0.3592 0.1888 0.0513  -0.0091 -0.0287 1028 LEU A O   
7553  C CB  . LEU A 1030 ? 0.2393 0.3454 0.1811 0.0496  -0.0037 -0.0147 1028 LEU A CB  
7554  C CG  . LEU A 1030 ? 0.2525 0.3581 0.1943 0.0496  -0.0016 -0.0125 1028 LEU A CG  
7555  C CD1 . LEU A 1030 ? 0.3150 0.4290 0.2549 0.0503  0.0000  -0.0049 1028 LEU A CD1 
7556  C CD2 . LEU A 1030 ? 0.2911 0.4006 0.2318 0.0513  -0.0019 -0.0196 1028 LEU A CD2 
7557  N N   . GLY A 1031 ? 0.2255 0.3214 0.1713 0.0475  -0.0082 -0.0211 1029 GLY A N   
7558  C CA  . GLY A 1031 ? 0.2446 0.3439 0.1902 0.0477  -0.0101 -0.0224 1029 GLY A CA  
7559  C C   . GLY A 1031 ? 0.2365 0.3352 0.1832 0.0480  -0.0125 -0.0307 1029 GLY A C   
7560  O O   . GLY A 1031 ? 0.2662 0.3705 0.2119 0.0489  -0.0143 -0.0329 1029 GLY A O   
7561  N N   . ARG A 1032 ? 0.2217 0.3136 0.1707 0.0472  -0.0126 -0.0352 1030 ARG A N   
7562  C CA  . ARG A 1032 ? 0.2165 0.3076 0.1674 0.0475  -0.0151 -0.0432 1030 ARG A CA  
7563  C C   . ARG A 1032 ? 0.2471 0.3489 0.1952 0.0504  -0.0159 -0.0486 1030 ARG A C   
7564  O O   . ARG A 1032 ? 0.2621 0.3658 0.2117 0.0512  -0.0184 -0.0556 1030 ARG A O   
7565  C CB  . ARG A 1032 ? 0.2774 0.3576 0.2322 0.0457  -0.0150 -0.0456 1030 ARG A CB  
7566  C CG  . ARG A 1032 ? 0.2359 0.3127 0.1944 0.0452  -0.0178 -0.0528 1030 ARG A CG  
7567  C CD  . ARG A 1032 ? 0.2494 0.3228 0.2100 0.0434  -0.0192 -0.0521 1030 ARG A CD  
7568  N NE  . ARG A 1032 ? 0.2514 0.3198 0.2166 0.0423  -0.0217 -0.0581 1030 ARG A NE  
7569  C CZ  . ARG A 1032 ? 0.2742 0.3456 0.2408 0.0425  -0.0243 -0.0625 1030 ARG A CZ  
7570  N NH1 . ARG A 1032 ? 0.3270 0.4070 0.2904 0.0440  -0.0248 -0.0619 1030 ARG A NH1 
7571  N NH2 . ARG A 1032 ? 0.3214 0.3873 0.2931 0.0412  -0.0266 -0.0674 1030 ARG A NH2 
7572  N N   . LEU A 1033 ? 0.2289 0.3384 0.1736 0.0521  -0.0141 -0.0455 1031 LEU A N   
7573  C CA  . LEU A 1033 ? 0.2371 0.3575 0.1792 0.0550  -0.0145 -0.0506 1031 LEU A CA  
7574  C C   . LEU A 1033 ? 0.2492 0.3830 0.1870 0.0570  -0.0148 -0.0490 1031 LEU A C   
7575  O O   . LEU A 1033 ? 0.2762 0.4213 0.2110 0.0596  -0.0148 -0.0519 1031 LEU A O   
7576  C CB  . LEU A 1033 ? 0.2406 0.3614 0.1818 0.0556  -0.0122 -0.0488 1031 LEU A CB  
7577  C CG  . LEU A 1033 ? 0.2599 0.3671 0.2051 0.0534  -0.0117 -0.0492 1031 LEU A CG  
7578  C CD1 . LEU A 1033 ? 0.2577 0.3656 0.2021 0.0540  -0.0094 -0.0469 1031 LEU A CD1 
7579  C CD2 . LEU A 1033 ? 0.2895 0.3919 0.2387 0.0533  -0.0144 -0.0576 1031 LEU A CD2 
7580  N N   . VAL A 1034 ? 0.2628 0.3961 0.2004 0.0560  -0.0153 -0.0445 1032 VAL A N   
7581  C CA  . VAL A 1034 ? 0.2598 0.4054 0.1939 0.0576  -0.0159 -0.0426 1032 VAL A CA  
7582  C C   . VAL A 1034 ? 0.2917 0.4347 0.2278 0.0568  -0.0185 -0.0455 1032 VAL A C   
7583  O O   . VAL A 1034 ? 0.2906 0.4220 0.2307 0.0546  -0.0191 -0.0467 1032 VAL A O   
7584  C CB  . VAL A 1034 ? 0.2762 0.4250 0.2084 0.0573  -0.0138 -0.0324 1032 VAL A CB  
7585  C CG1 . VAL A 1034 ? 0.2916 0.4456 0.2215 0.0583  -0.0114 -0.0297 1032 VAL A CG1 
7586  C CG2 . VAL A 1034 ? 0.2483 0.3840 0.1841 0.0544  -0.0130 -0.0270 1032 VAL A CG2 
7587  N N   . THR A 1035 ? 0.2935 0.4480 0.2268 0.0586  -0.0199 -0.0466 1033 THR A N   
7588  C CA  . THR A 1035 ? 0.3024 0.4555 0.2376 0.0580  -0.0225 -0.0501 1033 THR A CA  
7589  C C   . THR A 1035 ? 0.3310 0.4779 0.2678 0.0560  -0.0221 -0.0429 1033 THR A C   
7590  O O   . THR A 1035 ? 0.3973 0.5374 0.3374 0.0544  -0.0237 -0.0451 1033 THR A O   
7591  C CB  . THR A 1035 ? 0.3283 0.4960 0.2601 0.0607  -0.0244 -0.0542 1033 THR A CB  
7592  O OG1 . THR A 1035 ? 0.4296 0.6083 0.3571 0.0621  -0.0228 -0.0472 1033 THR A OG1 
7593  C CG2 . THR A 1035 ? 0.3430 0.5155 0.2746 0.0626  -0.0255 -0.0635 1033 THR A CG2 
7594  N N   . THR A 1036 ? 0.3000 0.4493 0.2350 0.0560  -0.0200 -0.0343 1034 THR A N   
7595  C CA  . THR A 1036 ? 0.3137 0.4568 0.2508 0.0542  -0.0195 -0.0272 1034 THR A CA  
7596  C C   . THR A 1036 ? 0.2941 0.4291 0.2325 0.0528  -0.0169 -0.0216 1034 THR A C   
7597  O O   . THR A 1036 ? 0.3195 0.4603 0.2555 0.0538  -0.0152 -0.0175 1034 THR A O   
7598  C CB  . THR A 1036 ? 0.3970 0.5510 0.3315 0.0555  -0.0199 -0.0217 1034 THR A CB  
7599  O OG1 . THR A 1036 ? 0.4165 0.5791 0.3494 0.0570  -0.0224 -0.0274 1034 THR A OG1 
7600  C CG2 . THR A 1036 ? 0.3737 0.5210 0.3112 0.0539  -0.0196 -0.0149 1034 THR A CG2 
7601  N N   . ALA A 1037 ? 0.2878 0.4103 0.2302 0.0505  -0.0166 -0.0216 1035 ALA A N   
7602  C CA  . ALA A 1037 ? 0.3063 0.4208 0.2502 0.0491  -0.0143 -0.0173 1035 ALA A CA  
7603  C C   . ALA A 1037 ? 0.2926 0.4086 0.2366 0.0489  -0.0130 -0.0083 1035 ALA A C   
7604  O O   . ALA A 1037 ? 0.3023 0.4187 0.2476 0.0487  -0.0140 -0.0054 1035 ALA A O   
7605  C CB  . ALA A 1037 ? 0.3053 0.4069 0.2533 0.0467  -0.0145 -0.0196 1035 ALA A CB  
7606  N N   . PRO A 1038 ? 0.2755 0.3924 0.2188 0.0491  -0.0110 -0.0037 1036 PRO A N   
7607  C CA  . PRO A 1038 ? 0.2458 0.3626 0.1906 0.0487  -0.0099 0.0050  1036 PRO A CA  
7608  C C   . PRO A 1038 ? 0.2671 0.3710 0.2164 0.0464  -0.0094 0.0067  1036 PRO A C   
7609  O O   . PRO A 1038 ? 0.2704 0.3662 0.2212 0.0451  -0.0096 0.0017  1036 PRO A O   
7610  C CB  . PRO A 1038 ? 0.2806 0.4016 0.2235 0.0493  -0.0079 0.0082  1036 PRO A CB  
7611  C CG  . PRO A 1038 ? 0.3103 0.4261 0.2530 0.0490  -0.0075 0.0014  1036 PRO A CG  
7612  C CD  . PRO A 1038 ? 0.2752 0.3924 0.2170 0.0496  -0.0097 -0.0063 1036 PRO A CD  
7613  N N   . VAL A 1039 ? 0.2698 0.3724 0.2216 0.0459  -0.0088 0.0138  1037 VAL A N   
7614  C CA  . VAL A 1039 ? 0.2634 0.3549 0.2197 0.0440  -0.0082 0.0159  1037 VAL A CA  
7615  C C   . VAL A 1039 ? 0.2517 0.3391 0.2085 0.0433  -0.0062 0.0178  1037 VAL A C   
7616  O O   . VAL A 1039 ? 0.2606 0.3530 0.2171 0.0440  -0.0052 0.0235  1037 VAL A O   
7617  C CB  . VAL A 1039 ? 0.2561 0.3478 0.2156 0.0440  -0.0088 0.0223  1037 VAL A CB  
7618  C CG1 . VAL A 1039 ? 0.2772 0.3579 0.2416 0.0423  -0.0081 0.0237  1037 VAL A CG1 
7619  C CG2 . VAL A 1039 ? 0.3116 0.4077 0.2705 0.0448  -0.0108 0.0203  1037 VAL A CG2 
7620  N N   . PRO A 1040 ? 0.2530 0.3321 0.2109 0.0420  -0.0055 0.0137  1038 PRO A N   
7621  C CA  . PRO A 1040 ? 0.2462 0.3218 0.2045 0.0414  -0.0037 0.0153  1038 PRO A CA  
7622  C C   . PRO A 1040 ? 0.2287 0.3003 0.1909 0.0405  -0.0028 0.0220  1038 PRO A C   
7623  O O   . PRO A 1040 ? 0.2318 0.3001 0.1971 0.0400  -0.0037 0.0239  1038 PRO A O   
7624  C CB  . PRO A 1040 ? 0.2599 0.3269 0.2190 0.0400  -0.0037 0.0093  1038 PRO A CB  
7625  C CG  . PRO A 1040 ? 0.2822 0.3508 0.2404 0.0403  -0.0055 0.0040  1038 PRO A CG  
7626  C CD  . PRO A 1040 ? 0.2798 0.3531 0.2384 0.0410  -0.0066 0.0073  1038 PRO A CD  
7627  N N   . PRO A 1041 ? 0.2219 0.2934 0.1845 0.0403  -0.0013 0.0254  1039 PRO A N   
7628  C CA  . PRO A 1041 ? 0.2139 0.2804 0.1811 0.0392  -0.0006 0.0312  1039 PRO A CA  
7629  C C   . PRO A 1041 ? 0.2257 0.2817 0.1963 0.0376  -0.0008 0.0284  1039 PRO A C   
7630  O O   . PRO A 1041 ? 0.2436 0.2951 0.2130 0.0369  -0.0007 0.0229  1039 PRO A O   
7631  C CB  . PRO A 1041 ? 0.2490 0.3163 0.2157 0.0391  0.0012  0.0332  1039 PRO A CB  
7632  C CG  . PRO A 1041 ? 0.2957 0.3718 0.2572 0.0406  0.0013  0.0303  1039 PRO A CG  
7633  C CD  . PRO A 1041 ? 0.2819 0.3575 0.2413 0.0410  -0.0001 0.0236  1039 PRO A CD  
7634  N N   . GLN A 1042 ? 0.2174 0.2700 0.1926 0.0371  -0.0013 0.0323  1040 GLN A N   
7635  C CA  . GLN A 1042 ? 0.2374 0.2812 0.2166 0.0358  -0.0014 0.0305  1040 GLN A CA  
7636  C C   . GLN A 1042 ? 0.2394 0.2811 0.2175 0.0354  -0.0024 0.0248  1040 GLN A C   
7637  O O   . GLN A 1042 ? 0.2418 0.2768 0.2224 0.0342  -0.0024 0.0225  1040 GLN A O   
7638  C CB  . GLN A 1042 ? 0.2771 0.3145 0.2574 0.0345  0.0000  0.0296  1040 GLN A CB  
7639  C CG  . GLN A 1042 ? 0.3499 0.3890 0.3317 0.0346  0.0011  0.0350  1040 GLN A CG  
7640  C CD  . GLN A 1042 ? 0.4401 0.4726 0.4236 0.0332  0.0023  0.0338  1040 GLN A CD  
7641  O OE1 . GLN A 1042 ? 0.5282 0.5556 0.5165 0.0324  0.0023  0.0360  1040 GLN A OE1 
7642  N NE2 . GLN A 1042 ? 0.4469 0.4794 0.4267 0.0330  0.0032  0.0302  1040 GLN A NE2 
7643  N N   . HIS A 1043 ? 0.2172 0.2648 0.1917 0.0365  -0.0034 0.0226  1041 HIS A N   
7644  C CA  . HIS A 1043 ? 0.2270 0.2731 0.2005 0.0360  -0.0045 0.0169  1041 HIS A CA  
7645  C C   . HIS A 1043 ? 0.2173 0.2642 0.1933 0.0363  -0.0059 0.0181  1041 HIS A C   
7646  O O   . HIS A 1043 ? 0.2251 0.2788 0.1996 0.0376  -0.0070 0.0193  1041 HIS A O   
7647  C CB  . HIS A 1043 ? 0.2477 0.3000 0.2166 0.0370  -0.0050 0.0133  1041 HIS A CB  
7648  C CG  . HIS A 1043 ? 0.2255 0.2763 0.1937 0.0365  -0.0062 0.0074  1041 HIS A CG  
7649  N ND1 . HIS A 1043 ? 0.2284 0.2738 0.1968 0.0351  -0.0060 0.0029  1041 HIS A ND1 
7650  C CD2 . HIS A 1043 ? 0.2181 0.2725 0.1861 0.0370  -0.0079 0.0056  1041 HIS A CD2 
7651  C CE1 . HIS A 1043 ? 0.2473 0.2927 0.2156 0.0348  -0.0075 -0.0014 1041 HIS A CE1 
7652  N NE2 . HIS A 1043 ? 0.2377 0.2885 0.2057 0.0359  -0.0086 0.0000  1041 HIS A NE2 
7653  N N   . SER A 1044 ? 0.2105 0.2510 0.1904 0.0352  -0.0058 0.0176  1042 SER A N   
7654  C CA  . SER A 1044 ? 0.2014 0.2420 0.1843 0.0354  -0.0072 0.0179  1042 SER A CA  
7655  C C   . SER A 1044 ? 0.2070 0.2404 0.1933 0.0338  -0.0067 0.0156  1042 SER A C   
7656  O O   . SER A 1044 ? 0.2462 0.2749 0.2328 0.0328  -0.0055 0.0148  1042 SER A O   
7657  C CB  . SER A 1044 ? 0.2083 0.2518 0.1941 0.0366  -0.0077 0.0239  1042 SER A CB  
7658  O OG  . SER A 1044 ? 0.2354 0.2741 0.2250 0.0360  -0.0067 0.0270  1042 SER A OG  
7659  N N   . SER A 1045 ? 0.1981 0.2311 0.1869 0.0338  -0.0078 0.0145  1043 SER A N   
7660  C CA  . SER A 1045 ? 0.2271 0.2546 0.2194 0.0325  -0.0074 0.0125  1043 SER A CA  
7661  C C   . SER A 1045 ? 0.2001 0.2287 0.1966 0.0333  -0.0086 0.0137  1043 SER A C   
7662  O O   . SER A 1045 ? 0.2057 0.2388 0.2013 0.0342  -0.0099 0.0136  1043 SER A O   
7663  C CB  . SER A 1045 ? 0.2221 0.2479 0.2125 0.0310  -0.0074 0.0073  1043 SER A CB  
7664  O OG  . SER A 1045 ? 0.2323 0.2540 0.2261 0.0298  -0.0070 0.0057  1043 SER A OG  
7665  N N   . VAL A 1046 ? 0.2080 0.2326 0.2092 0.0331  -0.0082 0.0146  1044 VAL A N   
7666  C CA  . VAL A 1046 ? 0.2291 0.2543 0.2350 0.0340  -0.0094 0.0151  1044 VAL A CA  
7667  C C   . VAL A 1046 ? 0.2247 0.2494 0.2311 0.0330  -0.0096 0.0104  1044 VAL A C   
7668  O O   . VAL A 1046 ? 0.2369 0.2628 0.2469 0.0337  -0.0106 0.0102  1044 VAL A O   
7669  C CB  . VAL A 1046 ? 0.2476 0.2693 0.2594 0.0345  -0.0093 0.0177  1044 VAL A CB  
7670  C CG1 . VAL A 1046 ? 0.2693 0.2920 0.2815 0.0354  -0.0093 0.0231  1044 VAL A CG1 
7671  C CG2 . VAL A 1046 ? 0.2357 0.2524 0.2486 0.0330  -0.0080 0.0147  1044 VAL A CG2 
7672  N N   . HIS A 1047 ? 0.2071 0.2303 0.2101 0.0313  -0.0088 0.0070  1045 HIS A N   
7673  C CA  . HIS A 1047 ? 0.2343 0.2570 0.2381 0.0300  -0.0089 0.0031  1045 HIS A CA  
7674  C C   . HIS A 1047 ? 0.2174 0.2443 0.2188 0.0300  -0.0101 0.0013  1045 HIS A C   
7675  O O   . HIS A 1047 ? 0.2457 0.2747 0.2433 0.0302  -0.0104 0.0015  1045 HIS A O   
7676  C CB  . HIS A 1047 ? 0.2742 0.2932 0.2766 0.0281  -0.0075 0.0009  1045 HIS A CB  
7677  C CG  . HIS A 1047 ? 0.3336 0.3489 0.3383 0.0282  -0.0064 0.0024  1045 HIS A CG  
7678  N ND1 . HIS A 1047 ? 0.3412 0.3553 0.3508 0.0286  -0.0064 0.0021  1045 HIS A ND1 
7679  C CD2 . HIS A 1047 ? 0.3193 0.3320 0.3226 0.0280  -0.0054 0.0041  1045 HIS A CD2 
7680  C CE1 . HIS A 1047 ? 0.3263 0.3371 0.3375 0.0286  -0.0056 0.0034  1045 HIS A CE1 
7681  N NE2 . HIS A 1047 ? 0.3577 0.3676 0.3651 0.0282  -0.0049 0.0048  1045 HIS A NE2 
7682  N N   . THR A 1048 ? 0.2223 0.2508 0.2262 0.0297  -0.0108 -0.0006 1046 THR A N   
7683  C CA  . THR A 1048 ? 0.2243 0.2567 0.2268 0.0295  -0.0121 -0.0026 1046 THR A CA  
7684  C C   . THR A 1048 ? 0.2144 0.2457 0.2173 0.0272  -0.0117 -0.0061 1046 THR A C   
7685  O O   . THR A 1048 ? 0.2397 0.2697 0.2456 0.0266  -0.0111 -0.0069 1046 THR A O   
7686  C CB  . THR A 1048 ? 0.2172 0.2534 0.2226 0.0311  -0.0134 -0.0013 1046 THR A CB  
7687  O OG1 . THR A 1048 ? 0.2377 0.2746 0.2435 0.0330  -0.0137 0.0028  1046 THR A OG1 
7688  C CG2 . THR A 1048 ? 0.2354 0.2761 0.2388 0.0310  -0.0149 -0.0031 1046 THR A CG2 
7689  N N   . ASP A 1049 ? 0.2101 0.2422 0.2102 0.0261  -0.0123 -0.0081 1047 ASP A N   
7690  C CA  . ASP A 1049 ? 0.2097 0.2409 0.2105 0.0238  -0.0121 -0.0109 1047 ASP A CA  
7691  C C   . ASP A 1049 ? 0.2130 0.2474 0.2172 0.0236  -0.0129 -0.0120 1047 ASP A C   
7692  O O   . ASP A 1049 ? 0.2045 0.2427 0.2090 0.0248  -0.0143 -0.0118 1047 ASP A O   
7693  C CB  . ASP A 1049 ? 0.2157 0.2474 0.2138 0.0228  -0.0131 -0.0129 1047 ASP A CB  
7694  C CG  . ASP A 1049 ? 0.2211 0.2518 0.2206 0.0202  -0.0132 -0.0153 1047 ASP A CG  
7695  O OD1 . ASP A 1049 ? 0.2262 0.2598 0.2278 0.0195  -0.0142 -0.0165 1047 ASP A OD1 
7696  O OD2 . ASP A 1049 ? 0.2302 0.2574 0.2290 0.0188  -0.0123 -0.0155 1047 ASP A OD2 
7697  N N   . PRO A 1050 ? 0.2014 0.2352 0.2082 0.0222  -0.0120 -0.0130 1048 PRO A N   
7698  C CA  . PRO A 1050 ? 0.2187 0.2562 0.2289 0.0222  -0.0126 -0.0139 1048 PRO A CA  
7699  C C   . PRO A 1050 ? 0.1909 0.2316 0.2013 0.0208  -0.0139 -0.0158 1048 PRO A C   
7700  O O   . PRO A 1050 ? 0.2063 0.2509 0.2190 0.0213  -0.0148 -0.0164 1048 PRO A O   
7701  C CB  . PRO A 1050 ? 0.2349 0.2712 0.2475 0.0211  -0.0111 -0.0146 1048 PRO A CB  
7702  C CG  . PRO A 1050 ? 0.2439 0.2764 0.2537 0.0193  -0.0101 -0.0146 1048 PRO A CG  
7703  C CD  . PRO A 1050 ? 0.2253 0.2555 0.2320 0.0207  -0.0104 -0.0131 1048 PRO A CD  
7704  N N   . VAL A 1051 ? 0.2082 0.2472 0.2166 0.0189  -0.0141 -0.0169 1049 VAL A N   
7705  C CA  . VAL A 1051 ? 0.2022 0.2439 0.2112 0.0175  -0.0157 -0.0187 1049 VAL A CA  
7706  C C   . VAL A 1051 ? 0.1931 0.2374 0.2005 0.0194  -0.0174 -0.0189 1049 VAL A C   
7707  O O   . VAL A 1051 ? 0.2046 0.2528 0.2136 0.0193  -0.0188 -0.0201 1049 VAL A O   
7708  C CB  . VAL A 1051 ? 0.2277 0.2667 0.2361 0.0149  -0.0157 -0.0198 1049 VAL A CB  
7709  C CG1 . VAL A 1051 ? 0.2648 0.3064 0.2749 0.0133  -0.0176 -0.0217 1049 VAL A CG1 
7710  C CG2 . VAL A 1051 ? 0.2218 0.2592 0.2319 0.0130  -0.0140 -0.0192 1049 VAL A CG2 
7711  N N   . LEU A 1052 ? 0.1999 0.2426 0.2042 0.0211  -0.0172 -0.0177 1050 LEU A N   
7712  C CA  . LEU A 1052 ? 0.1905 0.2368 0.1931 0.0232  -0.0186 -0.0174 1050 LEU A CA  
7713  C C   . LEU A 1052 ? 0.2148 0.2647 0.2200 0.0248  -0.0191 -0.0161 1050 LEU A C   
7714  O O   . LEU A 1052 ? 0.1920 0.2462 0.1977 0.0254  -0.0208 -0.0169 1050 LEU A O   
7715  C CB  . LEU A 1052 ? 0.1981 0.2428 0.1973 0.0249  -0.0180 -0.0155 1050 LEU A CB  
7716  C CG  . LEU A 1052 ? 0.2112 0.2603 0.2081 0.0273  -0.0191 -0.0142 1050 LEU A CG  
7717  C CD1 . LEU A 1052 ? 0.2116 0.2631 0.2105 0.0293  -0.0193 -0.0112 1050 LEU A CD1 
7718  C CD2 . LEU A 1052 ? 0.2164 0.2695 0.2126 0.0270  -0.0212 -0.0173 1050 LEU A CD2 
7719  N N   . LEU A 1053 ? 0.2045 0.2527 0.2119 0.0255  -0.0178 -0.0142 1051 LEU A N   
7720  C CA  . LEU A 1053 ? 0.2045 0.2558 0.2150 0.0271  -0.0184 -0.0131 1051 LEU A CA  
7721  C C   . LEU A 1053 ? 0.1969 0.2517 0.2102 0.0258  -0.0193 -0.0154 1051 LEU A C   
7722  O O   . LEU A 1053 ? 0.2110 0.2700 0.2258 0.0271  -0.0207 -0.0153 1051 LEU A O   
7723  C CB  . LEU A 1053 ? 0.2342 0.2828 0.2474 0.0280  -0.0170 -0.0115 1051 LEU A CB  
7724  C CG  . LEU A 1053 ? 0.2328 0.2787 0.2442 0.0295  -0.0165 -0.0085 1051 LEU A CG  
7725  C CD1 . LEU A 1053 ? 0.2484 0.2909 0.2628 0.0299  -0.0151 -0.0075 1051 LEU A CD1 
7726  C CD2 . LEU A 1053 ? 0.2414 0.2909 0.2527 0.0319  -0.0179 -0.0059 1051 LEU A CD2 
7727  N N   . ASP A 1054 ? 0.1938 0.2473 0.2081 0.0233  -0.0184 -0.0172 1052 ASP A N   
7728  C CA  . ASP A 1054 ? 0.2086 0.2659 0.2258 0.0218  -0.0192 -0.0191 1052 ASP A CA  
7729  C C   . ASP A 1054 ? 0.1923 0.2525 0.2084 0.0215  -0.0213 -0.0205 1052 ASP A C   
7730  O O   . ASP A 1054 ? 0.2059 0.2706 0.2244 0.0217  -0.0225 -0.0213 1052 ASP A O   
7731  C CB  . ASP A 1054 ? 0.2028 0.2586 0.2210 0.0189  -0.0180 -0.0202 1052 ASP A CB  
7732  C CG  . ASP A 1054 ? 0.2419 0.2966 0.2620 0.0192  -0.0162 -0.0197 1052 ASP A CG  
7733  O OD1 . ASP A 1054 ? 0.2387 0.2940 0.2603 0.0216  -0.0160 -0.0187 1052 ASP A OD1 
7734  O OD2 . ASP A 1054 ? 0.2907 0.3442 0.3110 0.0170  -0.0150 -0.0201 1052 ASP A OD2 
7735  N N   . PHE A 1055 ? 0.1764 0.2344 0.1891 0.0212  -0.0217 -0.0210 1053 PHE A N   
7736  C CA  . PHE A 1055 ? 0.2225 0.2834 0.2342 0.0210  -0.0238 -0.0228 1053 PHE A CA  
7737  C C   . PHE A 1055 ? 0.1937 0.2589 0.2046 0.0238  -0.0251 -0.0218 1053 PHE A C   
7738  O O   . PHE A 1055 ? 0.2093 0.2789 0.2215 0.0238  -0.0269 -0.0233 1053 PHE A O   
7739  C CB  . PHE A 1055 ? 0.2110 0.2687 0.2195 0.0204  -0.0240 -0.0239 1053 PHE A CB  
7740  C CG  . PHE A 1055 ? 0.2144 0.2750 0.2219 0.0204  -0.0263 -0.0265 1053 PHE A CG  
7741  C CD1 . PHE A 1055 ? 0.2300 0.2930 0.2408 0.0186  -0.0278 -0.0288 1053 PHE A CD1 
7742  C CD2 . PHE A 1055 ? 0.2200 0.2815 0.2239 0.0223  -0.0269 -0.0269 1053 PHE A CD2 
7743  C CE1 . PHE A 1055 ? 0.2472 0.3129 0.2577 0.0186  -0.0302 -0.0317 1053 PHE A CE1 
7744  C CE2 . PHE A 1055 ? 0.2392 0.3040 0.2423 0.0224  -0.0292 -0.0300 1053 PHE A CE2 
7745  C CZ  . PHE A 1055 ? 0.2580 0.3247 0.2647 0.0206  -0.0309 -0.0325 1053 PHE A CZ  
7746  N N   . ALA A 1056 ? 0.2046 0.2688 0.2138 0.0260  -0.0243 -0.0191 1054 ALA A N   
7747  C CA  . ALA A 1056 ? 0.2082 0.2769 0.2171 0.0286  -0.0256 -0.0173 1054 ALA A CA  
7748  C C   . ALA A 1056 ? 0.2137 0.2858 0.2269 0.0290  -0.0263 -0.0172 1054 ALA A C   
7749  O O   . ALA A 1056 ? 0.2278 0.3049 0.2414 0.0301  -0.0281 -0.0175 1054 ALA A O   
7750  C CB  . ALA A 1056 ? 0.2453 0.3120 0.2528 0.0307  -0.0245 -0.0136 1054 ALA A CB  
7751  N N   . LYS A 1057 ? 0.2085 0.2786 0.2250 0.0283  -0.0249 -0.0171 1055 LYS A N   
7752  C CA  . LYS A 1057 ? 0.2572 0.3310 0.2781 0.0287  -0.0255 -0.0175 1055 LYS A CA  
7753  C C   . LYS A 1057 ? 0.2209 0.2985 0.2430 0.0268  -0.0268 -0.0203 1055 LYS A C   
7754  O O   . LYS A 1057 ? 0.2256 0.3080 0.2499 0.0277  -0.0283 -0.0206 1055 LYS A O   
7755  C CB  . LYS A 1057 ? 0.2532 0.3248 0.2774 0.0283  -0.0237 -0.0174 1055 LYS A CB  
7756  C CG  . LYS A 1057 ? 0.2800 0.3490 0.3050 0.0306  -0.0229 -0.0148 1055 LYS A CG  
7757  C CD  . LYS A 1057 ? 0.2511 0.3191 0.2802 0.0305  -0.0215 -0.0155 1055 LYS A CD  
7758  C CE  . LYS A 1057 ? 0.2705 0.3357 0.2983 0.0278  -0.0198 -0.0172 1055 LYS A CE  
7759  N NZ  . LYS A 1057 ? 0.3415 0.4056 0.3725 0.0280  -0.0183 -0.0178 1055 LYS A NZ  
7760  N N   . TRP A 1058 ? 0.2183 0.2936 0.2393 0.0241  -0.0265 -0.0222 1056 TRP A N   
7761  C CA  . TRP A 1058 ? 0.2488 0.3272 0.2714 0.0221  -0.0280 -0.0248 1056 TRP A CA  
7762  C C   . TRP A 1058 ? 0.2333 0.3153 0.2541 0.0233  -0.0303 -0.0257 1056 TRP A C   
7763  O O   . TRP A 1058 ? 0.2640 0.3507 0.2872 0.0231  -0.0320 -0.0270 1056 TRP A O   
7764  C CB  . TRP A 1058 ? 0.2761 0.3507 0.2981 0.0191  -0.0274 -0.0261 1056 TRP A CB  
7765  C CG  . TRP A 1058 ? 0.2667 0.3437 0.2910 0.0166  -0.0291 -0.0286 1056 TRP A CG  
7766  C CD1 . TRP A 1058 ? 0.3114 0.3910 0.3399 0.0144  -0.0291 -0.0292 1056 TRP A CD1 
7767  C CD2 . TRP A 1058 ? 0.2943 0.3717 0.3173 0.0162  -0.0312 -0.0308 1056 TRP A CD2 
7768  N NE1 . TRP A 1058 ? 0.3259 0.4070 0.3560 0.0124  -0.0312 -0.0313 1056 TRP A NE1 
7769  C CE2 . TRP A 1058 ? 0.3191 0.3987 0.3459 0.0135  -0.0326 -0.0326 1056 TRP A CE2 
7770  C CE3 . TRP A 1058 ? 0.2871 0.3635 0.3060 0.0178  -0.0321 -0.0315 1056 TRP A CE3 
7771  C CZ2 . TRP A 1058 ? 0.3304 0.4109 0.3578 0.0124  -0.0350 -0.0354 1056 TRP A CZ2 
7772  C CZ3 . TRP A 1058 ? 0.3158 0.3935 0.3349 0.0169  -0.0344 -0.0346 1056 TRP A CZ3 
7773  C CH2 . TRP A 1058 ? 0.3187 0.3982 0.3422 0.0143  -0.0359 -0.0366 1056 TRP A CH2 
7774  N N   . LEU A 1059 ? 0.2192 0.2997 0.2358 0.0248  -0.0305 -0.0250 1057 LEU A N   
7775  C CA  . LEU A 1059 ? 0.2511 0.3360 0.2656 0.0262  -0.0327 -0.0260 1057 LEU A CA  
7776  C C   . LEU A 1059 ? 0.2287 0.3189 0.2448 0.0284  -0.0337 -0.0242 1057 LEU A C   
7777  O O   . LEU A 1059 ? 0.2683 0.3636 0.2852 0.0286  -0.0359 -0.0259 1057 LEU A O   
7778  C CB  . LEU A 1059 ? 0.2210 0.3041 0.2307 0.0276  -0.0323 -0.0250 1057 LEU A CB  
7779  C CG  . LEU A 1059 ? 0.2435 0.3229 0.2514 0.0258  -0.0321 -0.0276 1057 LEU A CG  
7780  C CD1 . LEU A 1059 ? 0.2202 0.2979 0.2236 0.0274  -0.0313 -0.0262 1057 LEU A CD1 
7781  C CD2 . LEU A 1059 ? 0.2639 0.3468 0.2725 0.0248  -0.0346 -0.0315 1057 LEU A CD2 
7782  N N   . ASP A 1060 ? 0.2349 0.3239 0.2520 0.0302  -0.0325 -0.0210 1058 ASP A N   
7783  C CA  . ASP A 1060 ? 0.3165 0.4101 0.3361 0.0324  -0.0336 -0.0191 1058 ASP A CA  
7784  C C   . ASP A 1060 ? 0.2715 0.3682 0.2955 0.0311  -0.0343 -0.0212 1058 ASP A C   
7785  O O   . ASP A 1060 ? 0.2907 0.3930 0.3161 0.0321  -0.0363 -0.0215 1058 ASP A O   
7786  C CB  . ASP A 1060 ? 0.2953 0.3862 0.3163 0.0342  -0.0322 -0.0155 1058 ASP A CB  
7787  C CG  . ASP A 1060 ? 0.2892 0.3808 0.3070 0.0365  -0.0326 -0.0122 1058 ASP A CG  
7788  O OD1 . ASP A 1060 ? 0.3792 0.4758 0.3947 0.0376  -0.0344 -0.0121 1058 ASP A OD1 
7789  O OD2 . ASP A 1060 ? 0.3671 0.4545 0.3847 0.0373  -0.0311 -0.0096 1058 ASP A OD2 
7790  N N   . GLY A 1061 ? 0.2825 0.3765 0.3088 0.0288  -0.0329 -0.0227 1059 GLY A N   
7791  C CA  . GLY A 1061 ? 0.2701 0.3677 0.3008 0.0274  -0.0335 -0.0245 1059 GLY A CA  
7792  C C   . GLY A 1061 ? 0.2965 0.3977 0.3271 0.0258  -0.0356 -0.0272 1059 GLY A C   
7793  O O   . GLY A 1061 ? 0.3177 0.4239 0.3517 0.0256  -0.0369 -0.0282 1059 GLY A O   
7794  N N   . LYS A 1062 ? 0.2942 0.3931 0.3214 0.0248  -0.0361 -0.0286 1060 LYS A N   
7795  C CA  . LYS A 1062 ? 0.3279 0.4299 0.3552 0.0235  -0.0385 -0.0316 1060 LYS A CA  
7796  C C   . LYS A 1062 ? 0.3255 0.4327 0.3507 0.0261  -0.0406 -0.0316 1060 LYS A C   
7797  O O   . LYS A 1062 ? 0.3806 0.4914 0.4062 0.0254  -0.0429 -0.0344 1060 LYS A O   
7798  C CB  . LYS A 1062 ? 0.3486 0.4462 0.3738 0.0215  -0.0384 -0.0335 1060 LYS A CB  
7799  C CG  . LYS A 1062 ? 0.3491 0.4428 0.3772 0.0183  -0.0370 -0.0339 1060 LYS A CG  
7800  C CD  . LYS A 1062 ? 0.4159 0.5137 0.4491 0.0161  -0.0382 -0.0354 1060 LYS A CD  
7801  C CE  . LYS A 1062 ? 0.4379 0.5328 0.4740 0.0128  -0.0367 -0.0350 1060 LYS A CE  
7802  N NZ  . LYS A 1062 ? 0.4755 0.5748 0.5169 0.0103  -0.0379 -0.0362 1060 LYS A NZ  
7803  N N   . GLY A 1063 ? 0.3003 0.4084 0.3237 0.0290  -0.0402 -0.0284 1061 GLY A N   
7804  C CA  . GLY A 1063 ? 0.3392 0.4528 0.3603 0.0315  -0.0421 -0.0277 1061 GLY A CA  
7805  C C   . GLY A 1063 ? 0.3486 0.4617 0.3643 0.0325  -0.0424 -0.0278 1061 GLY A C   
7806  O O   . GLY A 1063 ? 0.3604 0.4791 0.3738 0.0345  -0.0440 -0.0273 1061 GLY A O   
7807  N N   . ALA A 1064 ? 0.2828 0.3901 0.2966 0.0311  -0.0408 -0.0286 1062 ALA A N   
7808  C CA  . ALA A 1064 ? 0.2753 0.3823 0.2842 0.0320  -0.0409 -0.0292 1062 ALA A CA  
7809  C C   . ALA A 1064 ? 0.2920 0.3979 0.2983 0.0343  -0.0393 -0.0245 1062 ALA A C   
7810  O O   . ALA A 1064 ? 0.2543 0.3549 0.2590 0.0339  -0.0373 -0.0232 1062 ALA A O   
7811  C CB  . ALA A 1064 ? 0.2809 0.3823 0.2894 0.0295  -0.0401 -0.0322 1062 ALA A CB  
7812  N N   . ARG A 1065 ? 0.2614 0.3728 0.2677 0.0367  -0.0404 -0.0216 1063 ARG A N   
7813  C CA  . ARG A 1065 ? 0.2530 0.3635 0.2588 0.0387  -0.0391 -0.0164 1063 ARG A CA  
7814  C C   . ARG A 1065 ? 0.2800 0.3900 0.2809 0.0397  -0.0384 -0.0150 1063 ARG A C   
7815  O O   . ARG A 1065 ? 0.2930 0.3982 0.2935 0.0399  -0.0364 -0.0120 1063 ARG A O   
7816  C CB  . ARG A 1065 ? 0.3132 0.4301 0.3206 0.0410  -0.0409 -0.0134 1063 ARG A CB  
7817  N N   . ALA A 1066 ? 0.2833 0.3987 0.2803 0.0403  -0.0399 -0.0173 1064 ALA A N   
7818  C CA  . ALA A 1066 ? 0.2814 0.3975 0.2737 0.0412  -0.0391 -0.0163 1064 ALA A CA  
7819  C C   . ALA A 1066 ? 0.2584 0.3668 0.2500 0.0393  -0.0372 -0.0184 1064 ALA A C   
7820  O O   . ALA A 1066 ? 0.2690 0.3749 0.2582 0.0399  -0.0355 -0.0159 1064 ALA A O   
7821  C CB  . ALA A 1066 ? 0.2934 0.4176 0.2821 0.0423  -0.0413 -0.0193 1064 ALA A CB  
7822  N N   . GLU A 1067 ? 0.2628 0.3677 0.2566 0.0370  -0.0375 -0.0229 1065 GLU A N   
7823  C CA  . GLU A 1067 ? 0.2512 0.3489 0.2448 0.0350  -0.0358 -0.0247 1065 GLU A CA  
7824  C C   . GLU A 1067 ? 0.2523 0.3437 0.2480 0.0345  -0.0334 -0.0210 1065 GLU A C   
7825  O O   . GLU A 1067 ? 0.2303 0.3169 0.2244 0.0341  -0.0317 -0.0202 1065 GLU A O   
7826  C CB  . GLU A 1067 ? 0.2778 0.3738 0.2740 0.0325  -0.0370 -0.0297 1065 GLU A CB  
7827  C CG  . GLU A 1067 ? 0.2590 0.3599 0.2535 0.0328  -0.0394 -0.0345 1065 GLU A CG  
7828  C CD  . GLU A 1067 ? 0.3240 0.4328 0.3190 0.0341  -0.0418 -0.0352 1065 GLU A CD  
7829  O OE1 . GLU A 1067 ? 0.2733 0.3835 0.2707 0.0345  -0.0417 -0.0322 1065 GLU A OE1 
7830  O OE2 . GLU A 1067 ? 0.3710 0.4849 0.3643 0.0347  -0.0439 -0.0391 1065 GLU A OE2 
7831  N N   . ALA A 1068 ? 0.2415 0.3332 0.2410 0.0346  -0.0334 -0.0191 1066 ALA A N   
7832  C CA  . ALA A 1068 ? 0.2459 0.3323 0.2477 0.0345  -0.0313 -0.0160 1066 ALA A CA  
7833  C C   . ALA A 1068 ? 0.2480 0.3340 0.2475 0.0365  -0.0303 -0.0116 1066 ALA A C   
7834  O O   . ALA A 1068 ? 0.2305 0.3110 0.2301 0.0360  -0.0284 -0.0100 1066 ALA A O   
7835  C CB  . ALA A 1068 ? 0.2746 0.3625 0.2810 0.0348  -0.0318 -0.0150 1066 ALA A CB  
7836  N N   . GLU A 1069 ? 0.2529 0.3451 0.2506 0.0386  -0.0317 -0.0093 1067 GLU A N   
7837  C CA  . GLU A 1069 ? 0.2513 0.3440 0.2469 0.0404  -0.0309 -0.0046 1067 GLU A CA  
7838  C C   . GLU A 1069 ? 0.2479 0.3385 0.2393 0.0398  -0.0297 -0.0059 1067 GLU A C   
7839  O O   . GLU A 1069 ? 0.2594 0.3461 0.2503 0.0400  -0.0280 -0.0030 1067 GLU A O   
7840  C CB  . GLU A 1069 ? 0.2719 0.3729 0.2663 0.0427  -0.0327 -0.0019 1067 GLU A CB  
7841  C CG  . GLU A 1069 ? 0.3262 0.4293 0.3183 0.0444  -0.0321 0.0034  1067 GLU A CG  
7842  C CD  . GLU A 1069 ? 0.4547 0.5541 0.4512 0.0451  -0.0313 0.0086  1067 GLU A CD  
7843  O OE1 . GLU A 1069 ? 0.4885 0.5842 0.4897 0.0446  -0.0313 0.0079  1067 GLU A OE1 
7844  O OE2 . GLU A 1069 ? 0.5696 0.6701 0.5652 0.0463  -0.0308 0.0135  1067 GLU A OE2 
7845  N N   . ALA A 1070 ? 0.2493 0.3425 0.2380 0.0392  -0.0307 -0.0104 1068 ALA A N   
7846  C CA  . ALA A 1070 ? 0.2639 0.3550 0.2490 0.0387  -0.0297 -0.0123 1068 ALA A CA  
7847  C C   . ALA A 1070 ? 0.2065 0.2889 0.1933 0.0366  -0.0278 -0.0131 1068 ALA A C   
7848  O O   . ALA A 1070 ? 0.2368 0.3161 0.2216 0.0366  -0.0262 -0.0121 1068 ALA A O   
7849  C CB  . ALA A 1070 ? 0.2701 0.3652 0.2531 0.0383  -0.0315 -0.0178 1068 ALA A CB  
7850  N N   . ALA A 1071 ? 0.2186 0.2976 0.2092 0.0349  -0.0278 -0.0147 1069 ALA A N   
7851  C CA  . ALA A 1071 ? 0.2059 0.2775 0.1984 0.0330  -0.0260 -0.0152 1069 ALA A CA  
7852  C C   . ALA A 1071 ? 0.2102 0.2786 0.2036 0.0338  -0.0242 -0.0108 1069 ALA A C   
7853  O O   . ALA A 1071 ? 0.2127 0.2764 0.2050 0.0332  -0.0225 -0.0102 1069 ALA A O   
7854  C CB  . ALA A 1071 ? 0.2342 0.3044 0.2306 0.0310  -0.0264 -0.0177 1069 ALA A CB  
7855  N N   . ARG A 1072 ? 0.2147 0.2854 0.2104 0.0353  -0.0246 -0.0075 1070 ARG A N   
7856  C CA  . ARG A 1072 ? 0.2397 0.3074 0.2371 0.0362  -0.0233 -0.0033 1070 ARG A CA  
7857  C C   . ARG A 1072 ? 0.2476 0.3157 0.2414 0.0373  -0.0225 -0.0006 1070 ARG A C   
7858  O O   . ARG A 1072 ? 0.2383 0.3018 0.2325 0.0370  -0.0209 0.0013  1070 ARG A O   
7859  C CB  . ARG A 1072 ? 0.2549 0.3256 0.2561 0.0379  -0.0243 -0.0002 1070 ARG A CB  
7860  C CG  . ARG A 1072 ? 0.2786 0.3480 0.2842 0.0370  -0.0245 -0.0024 1070 ARG A CG  
7861  C CD  . ARG A 1072 ? 0.2910 0.3630 0.3010 0.0390  -0.0256 0.0007  1070 ARG A CD  
7862  N NE  . ARG A 1072 ? 0.3067 0.3855 0.3155 0.0403  -0.0276 0.0015  1070 ARG A NE  
7863  C CZ  . ARG A 1072 ? 0.3176 0.4001 0.3273 0.0400  -0.0290 -0.0013 1070 ARG A CZ  
7864  N NH1 . ARG A 1072 ? 0.3195 0.3999 0.3316 0.0382  -0.0286 -0.0048 1070 ARG A NH1 
7865  N NH2 . ARG A 1072 ? 0.3319 0.4210 0.3402 0.0413  -0.0309 -0.0004 1070 ARG A NH2 
7866  N N   . ASN A 1073 ? 0.2256 0.3000 0.2160 0.0385  -0.0237 -0.0004 1071 ASN A N   
7867  C CA  . ASN A 1073 ? 0.2525 0.3287 0.2392 0.0395  -0.0230 0.0020  1071 ASN A CA  
7868  C C   . ASN A 1073 ? 0.2317 0.3031 0.2161 0.0380  -0.0216 -0.0008 1071 ASN A C   
7869  O O   . ASN A 1073 ? 0.2495 0.3187 0.2329 0.0383  -0.0201 0.0018  1071 ASN A O   
7870  C CB  . ASN A 1073 ? 0.2419 0.3269 0.2251 0.0411  -0.0247 0.0019  1071 ASN A CB  
7871  C CG  . ASN A 1073 ? 0.3341 0.4244 0.3193 0.0429  -0.0260 0.0064  1071 ASN A CG  
7872  O OD1 . ASN A 1073 ? 0.3789 0.4662 0.3679 0.0432  -0.0255 0.0105  1071 ASN A OD1 
7873  N ND2 . ASN A 1073 ? 0.3586 0.4568 0.3415 0.0440  -0.0278 0.0055  1071 ASN A ND2 
7874  N N   . ALA A 1074 ? 0.2173 0.2873 0.2014 0.0365  -0.0221 -0.0060 1072 ALA A N   
7875  C CA  . ALA A 1074 ? 0.2432 0.3082 0.2259 0.0350  -0.0209 -0.0087 1072 ALA A CA  
7876  C C   . ALA A 1074 ? 0.2103 0.2682 0.1956 0.0338  -0.0190 -0.0069 1072 ALA A C   
7877  O O   . ALA A 1074 ? 0.2066 0.2610 0.1905 0.0334  -0.0176 -0.0064 1072 ALA A O   
7878  C CB  . ALA A 1074 ? 0.2626 0.3272 0.2457 0.0334  -0.0221 -0.0142 1072 ALA A CB  
7879  N N   . GLY A 1075 ? 0.2176 0.2738 0.2068 0.0333  -0.0191 -0.0062 1073 GLY A N   
7880  C CA  . GLY A 1075 ? 0.2093 0.2597 0.2012 0.0324  -0.0174 -0.0048 1073 GLY A CA  
7881  C C   . GLY A 1075 ? 0.2009 0.2500 0.1925 0.0336  -0.0163 -0.0005 1073 GLY A C   
7882  O O   . GLY A 1075 ? 0.2272 0.2715 0.2190 0.0328  -0.0148 -0.0001 1073 GLY A O   
7883  N N   . SER A 1076 ? 0.2100 0.2637 0.2015 0.0356  -0.0171 0.0030  1074 SER A N   
7884  C CA  . SER A 1076 ? 0.2245 0.2777 0.2163 0.0367  -0.0163 0.0078  1074 SER A CA  
7885  C C   . SER A 1076 ? 0.2313 0.2857 0.2186 0.0369  -0.0155 0.0081  1074 SER A C   
7886  O O   . SER A 1076 ? 0.2626 0.3138 0.2501 0.0367  -0.0141 0.0104  1074 SER A O   
7887  C CB  . SER A 1076 ? 0.2702 0.3286 0.2636 0.0387  -0.0176 0.0121  1074 SER A CB  
7888  O OG  . SER A 1076 ? 0.3638 0.4206 0.3623 0.0389  -0.0182 0.0126  1074 SER A OG  
7889  N N   . SER A 1077 ? 0.2322 0.2914 0.2156 0.0372  -0.0164 0.0054  1075 SER A N   
7890  C CA  A SER A 1077 ? 0.2665 0.3281 0.2458 0.0377  -0.0157 0.0053  1075 SER A CA  
7891  C CA  B SER A 1077 ? 0.2666 0.3282 0.2458 0.0377  -0.0158 0.0052  1075 SER A CA  
7892  C C   . SER A 1077 ? 0.2286 0.2842 0.2072 0.0360  -0.0144 0.0021  1075 SER A C   
7893  O O   . SER A 1077 ? 0.2477 0.3032 0.2239 0.0363  -0.0133 0.0030  1075 SER A O   
7894  C CB  A SER A 1077 ? 0.2801 0.3492 0.2559 0.0387  -0.0173 0.0026  1075 SER A CB  
7895  C CB  B SER A 1077 ? 0.2796 0.3485 0.2554 0.0386  -0.0174 0.0022  1075 SER A CB  
7896  O OG  A SER A 1077 ? 0.2926 0.3684 0.2683 0.0405  -0.0183 0.0066  1075 SER A OG  
7897  O OG  B SER A 1077 ? 0.2891 0.3607 0.2609 0.0392  -0.0168 0.0010  1075 SER A OG  
7898  N N   . SER A 1078 ? 0.2165 0.2673 0.1970 0.0343  -0.0145 -0.0013 1076 SER A N   
7899  C CA  . SER A 1078 ? 0.2233 0.2686 0.2036 0.0326  -0.0134 -0.0039 1076 SER A CA  
7900  C C   . SER A 1078 ? 0.2260 0.2670 0.2072 0.0325  -0.0115 -0.0006 1076 SER A C   
7901  O O   . SER A 1078 ? 0.2268 0.2665 0.2109 0.0328  -0.0111 0.0027  1076 SER A O   
7902  C CB  . SER A 1078 ? 0.2156 0.2571 0.1988 0.0307  -0.0137 -0.0068 1076 SER A CB  
7903  O OG  . SER A 1078 ? 0.2130 0.2491 0.1963 0.0290  -0.0126 -0.0085 1076 SER A OG  
7904  N N   . ALA A 1079 ? 0.2055 0.2444 0.1845 0.0320  -0.0105 -0.0017 1077 ALA A N   
7905  C CA  . ALA A 1079 ? 0.1968 0.2313 0.1768 0.0316  -0.0088 0.0009  1077 ALA A CA  
7906  C C   . ALA A 1079 ? 0.2005 0.2288 0.1823 0.0295  -0.0081 -0.0015 1077 ALA A C   
7907  O O   . ALA A 1079 ? 0.1976 0.2220 0.1799 0.0290  -0.0067 -0.0002 1077 ALA A O   
7908  C CB  . ALA A 1079 ? 0.2049 0.2418 0.1817 0.0326  -0.0081 0.0020  1077 ALA A CB  
7909  N N   . LEU A 1080 ? 0.1958 0.2232 0.1787 0.0283  -0.0090 -0.0047 1078 LEU A N   
7910  C CA  . LEU A 1080 ? 0.2089 0.2313 0.1940 0.0262  -0.0083 -0.0063 1078 LEU A CA  
7911  C C   . LEU A 1080 ? 0.1902 0.2097 0.1780 0.0262  -0.0071 -0.0036 1078 LEU A C   
7912  O O   . LEU A 1080 ? 0.2006 0.2218 0.1904 0.0272  -0.0075 -0.0016 1078 LEU A O   
7913  C CB  . LEU A 1080 ? 0.2032 0.2267 0.1900 0.0252  -0.0096 -0.0089 1078 LEU A CB  
7914  C CG  . LEU A 1080 ? 0.1933 0.2129 0.1826 0.0230  -0.0090 -0.0101 1078 LEU A CG  
7915  C CD1 . LEU A 1080 ? 0.2334 0.2499 0.2216 0.0215  -0.0087 -0.0119 1078 LEU A CD1 
7916  C CD2 . LEU A 1080 ? 0.2077 0.2295 0.1993 0.0221  -0.0101 -0.0117 1078 LEU A CD2 
7917  N N   . GLY A 1081 ? 0.1903 0.2056 0.1783 0.0250  -0.0059 -0.0036 1079 GLY A N   
7918  C CA  . GLY A 1081 ? 0.2105 0.2231 0.2014 0.0250  -0.0048 -0.0015 1079 GLY A CA  
7919  C C   . GLY A 1081 ? 0.2244 0.2363 0.2148 0.0261  -0.0040 0.0017  1079 GLY A C   
7920  O O   . GLY A 1081 ? 0.2270 0.2362 0.2201 0.0260  -0.0032 0.0032  1079 GLY A O   
7921  N N   . LEU A 1082 ? 0.1960 0.2107 0.1835 0.0272  -0.0041 0.0027  1080 LEU A N   
7922  C CA  A LEU A 1082 ? 0.2044 0.2187 0.1912 0.0280  -0.0031 0.0058  1080 LEU A CA  
7923  C CA  B LEU A 1082 ? 0.2044 0.2188 0.1913 0.0280  -0.0031 0.0058  1080 LEU A CA  
7924  C C   . LEU A 1082 ? 0.2310 0.2405 0.2184 0.0266  -0.0019 0.0050  1080 LEU A C   
7925  O O   . LEU A 1082 ? 0.2215 0.2291 0.2075 0.0253  -0.0018 0.0020  1080 LEU A O   
7926  C CB  A LEU A 1082 ? 0.2093 0.2280 0.1922 0.0291  -0.0034 0.0059  1080 LEU A CB  
7927  C CB  B LEU A 1082 ? 0.2094 0.2280 0.1922 0.0291  -0.0034 0.0058  1080 LEU A CB  
7928  C CG  A LEU A 1082 ? 0.2092 0.2288 0.1910 0.0299  -0.0023 0.0091  1080 LEU A CG  
7929  C CG  B LEU A 1082 ? 0.2095 0.2294 0.1910 0.0299  -0.0023 0.0089  1080 LEU A CG  
7930  C CD1 A LEU A 1082 ? 0.2042 0.2245 0.1892 0.0307  -0.0023 0.0140  1080 LEU A CD1 
7931  C CD1 B LEU A 1082 ? 0.2135 0.2404 0.1920 0.0316  -0.0030 0.0099  1080 LEU A CD1 
7932  C CD2 A LEU A 1082 ? 0.2325 0.2578 0.2103 0.0311  -0.0026 0.0085  1080 LEU A CD2 
7933  C CD2 B LEU A 1082 ? 0.2213 0.2377 0.2015 0.0289  -0.0013 0.0069  1080 LEU A CD2 
7934  N N   . ASP A 1083 ? 0.2254 0.2329 0.2151 0.0268  -0.0010 0.0079  1081 ASP A N   
7935  C CA  . ASP A 1083 ? 0.2489 0.2519 0.2395 0.0255  0.0001  0.0072  1081 ASP A CA  
7936  C C   . ASP A 1083 ? 0.2583 0.2609 0.2501 0.0262  0.0009  0.0110  1081 ASP A C   
7937  O O   . ASP A 1083 ? 0.2925 0.2944 0.2880 0.0267  0.0007  0.0134  1081 ASP A O   
7938  C CB  . ASP A 1083 ? 0.2725 0.2731 0.2666 0.0246  0.0000  0.0057  1081 ASP A CB  
7939  C CG  . ASP A 1083 ? 0.3612 0.3579 0.3562 0.0232  0.0010  0.0047  1081 ASP A CG  
7940  O OD1 . ASP A 1083 ? 0.3936 0.3890 0.3865 0.0228  0.0018  0.0050  1081 ASP A OD1 
7941  O OD2 . ASP A 1083 ? 0.4266 0.4219 0.4246 0.0225  0.0011  0.0035  1081 ASP A OD2 
7942  N N   . LEU A 1084 ? 0.2387 0.2417 0.2276 0.0262  0.0016  0.0113  1082 LEU A N   
7943  C CA  . LEU A 1084 ? 0.2407 0.2445 0.2303 0.0269  0.0024  0.0152  1082 LEU A CA  
7944  C C   . LEU A 1084 ? 0.2490 0.2492 0.2384 0.0259  0.0035  0.0145  1082 LEU A C   
7945  O O   . LEU A 1084 ? 0.2660 0.2645 0.2536 0.0249  0.0037  0.0112  1082 LEU A O   
7946  C CB  . LEU A 1084 ? 0.2688 0.2781 0.2548 0.0282  0.0023  0.0166  1082 LEU A CB  
7947  C CG  . LEU A 1084 ? 0.2885 0.3027 0.2738 0.0295  0.0011  0.0176  1082 LEU A CG  
7948  C CD1 . LEU A 1084 ? 0.2955 0.3157 0.2767 0.0307  0.0011  0.0179  1082 LEU A CD1 
7949  C CD2 . LEU A 1084 ? 0.2980 0.3125 0.2877 0.0301  0.0007  0.0222  1082 LEU A CD2 
7950  N N   . GLU A 1085 ? 0.2437 0.2429 0.2358 0.0260  0.0041  0.0178  1083 GLU A N   
7951  C CA  . GLU A 1085 ? 0.2238 0.2209 0.2156 0.0252  0.0053  0.0180  1083 GLU A CA  
7952  C C   . GLU A 1085 ? 0.2449 0.2462 0.2346 0.0263  0.0058  0.0211  1083 GLU A C   
7953  O O   . GLU A 1085 ? 0.2756 0.2799 0.2671 0.0272  0.0056  0.0252  1083 GLU A O   
7954  C CB  . GLU A 1085 ? 0.2635 0.2565 0.2599 0.0245  0.0056  0.0193  1083 GLU A CB  
7955  C CG  . GLU A 1085 ? 0.2663 0.2576 0.2623 0.0238  0.0067  0.0196  1083 GLU A CG  
7956  C CD  . GLU A 1085 ? 0.3733 0.3605 0.3737 0.0228  0.0069  0.0199  1083 GLU A CD  
7957  O OE1 . GLU A 1085 ? 0.4059 0.3913 0.4097 0.0226  0.0062  0.0189  1083 GLU A OE1 
7958  O OE2 . GLU A 1085 ? 0.3584 0.3444 0.3590 0.0223  0.0077  0.0208  1083 GLU A OE2 
7959  N N   . LEU A 1086 ? 0.2488 0.2509 0.2350 0.0263  0.0065  0.0192  1084 LEU A N   
7960  C CA  . LEU A 1086 ? 0.2268 0.2339 0.2106 0.0274  0.0071  0.0212  1084 LEU A CA  
7961  C C   . LEU A 1086 ? 0.2685 0.2741 0.2542 0.0268  0.0083  0.0239  1084 LEU A C   
7962  O O   . LEU A 1086 ? 0.2638 0.2646 0.2508 0.0256  0.0087  0.0221  1084 LEU A O   
7963  C CB  . LEU A 1086 ? 0.2359 0.2449 0.2155 0.0278  0.0071  0.0171  1084 LEU A CB  
7964  C CG  . LEU A 1086 ? 0.2720 0.2825 0.2499 0.0282  0.0058  0.0140  1084 LEU A CG  
7965  C CD1 . LEU A 1086 ? 0.2742 0.2866 0.2488 0.0287  0.0054  0.0098  1084 LEU A CD1 
7966  C CD2 . LEU A 1086 ? 0.2932 0.3088 0.2710 0.0294  0.0051  0.0170  1084 LEU A CD2 
7967  N N   . PRO A 1087 ? 0.2556 0.2658 0.2418 0.0276  0.0088  0.0283  1085 PRO A N   
7968  C CA  . PRO A 1087 ? 0.2858 0.2951 0.2740 0.0271  0.0099  0.0312  1085 PRO A CA  
7969  C C   . PRO A 1087 ? 0.2548 0.2635 0.2402 0.0269  0.0108  0.0279  1085 PRO A C   
7970  O O   . PRO A 1087 ? 0.2936 0.3057 0.2750 0.0278  0.0108  0.0252  1085 PRO A O   
7971  C CB  . PRO A 1087 ? 0.2956 0.3118 0.2838 0.0281  0.0102  0.0365  1085 PRO A CB  
7972  C CG  . PRO A 1087 ? 0.3315 0.3506 0.3193 0.0290  0.0090  0.0372  1085 PRO A CG  
7973  C CD  . PRO A 1087 ? 0.2639 0.2804 0.2491 0.0290  0.0083  0.0314  1085 PRO A CD  
7974  N N   . GLY A 1088 ? 0.2564 0.2607 0.2443 0.0257  0.0114  0.0281  1086 GLY A N   
7975  C CA  . GLY A 1088 ? 0.2952 0.2985 0.2811 0.0255  0.0122  0.0255  1086 GLY A CA  
7976  C C   . GLY A 1088 ? 0.2388 0.2388 0.2281 0.0243  0.0129  0.0273  1086 GLY A C   
7977  O O   . GLY A 1088 ? 0.2445 0.2441 0.2376 0.0239  0.0130  0.0313  1086 GLY A O   
7978  N N   . PRO A 1089 ? 0.2611 0.2584 0.2494 0.0238  0.0134  0.0245  1087 PRO A N   
7979  C CA  . PRO A 1089 ? 0.2591 0.2535 0.2504 0.0227  0.0140  0.0259  1087 PRO A CA  
7980  C C   . PRO A 1089 ? 0.2517 0.2408 0.2468 0.0213  0.0133  0.0255  1087 PRO A C   
7981  O O   . PRO A 1089 ? 0.2557 0.2428 0.2505 0.0211  0.0125  0.0232  1087 PRO A O   
7982  C CB  . PRO A 1089 ? 0.2969 0.2900 0.2858 0.0225  0.0144  0.0223  1087 PRO A CB  
7983  C CG  . PRO A 1089 ? 0.3152 0.3074 0.3014 0.0228  0.0134  0.0184  1087 PRO A CG  
7984  C CD  . PRO A 1089 ? 0.2654 0.2620 0.2503 0.0240  0.0130  0.0198  1087 PRO A CD  
7985  N N   . VAL A 1090 ? 0.2496 0.2370 0.2486 0.0205  0.0137  0.0278  1088 VAL A N   
7986  C CA  . VAL A 1090 ? 0.2180 0.2005 0.2208 0.0193  0.0130  0.0266  1088 VAL A CA  
7987  C C   . VAL A 1090 ? 0.2164 0.1960 0.2169 0.0185  0.0129  0.0222  1088 VAL A C   
7988  O O   . VAL A 1090 ? 0.2407 0.2211 0.2379 0.0187  0.0134  0.0205  1088 VAL A O   
7989  C CB  . VAL A 1090 ? 0.2419 0.2233 0.2496 0.0185  0.0133  0.0294  1088 VAL A CB  
7990  C CG1 . VAL A 1090 ? 0.2523 0.2367 0.2629 0.0191  0.0132  0.0345  1088 VAL A CG1 
7991  C CG2 . VAL A 1090 ? 0.2571 0.2387 0.2632 0.0182  0.0143  0.0290  1088 VAL A CG2 
7992  N N   . GLY A 1091 ? 0.2199 0.1964 0.2227 0.0177  0.0122  0.0202  1089 GLY A N   
7993  C CA  . GLY A 1091 ? 0.2523 0.2266 0.2536 0.0167  0.0121  0.0166  1089 GLY A CA  
7994  C C   . GLY A 1091 ? 0.2258 0.2009 0.2232 0.0170  0.0117  0.0142  1089 GLY A C   
7995  O O   . GLY A 1091 ? 0.2235 0.1973 0.2193 0.0162  0.0116  0.0118  1089 GLY A O   
7996  N N   . GLU A 1092 ? 0.2286 0.2059 0.2248 0.0180  0.0114  0.0150  1090 GLU A N   
7997  C CA  . GLU A 1092 ? 0.2443 0.2224 0.2373 0.0183  0.0109  0.0127  1090 GLU A CA  
7998  C C   . GLU A 1092 ? 0.2541 0.2338 0.2479 0.0190  0.0102  0.0135  1090 GLU A C   
7999  O O   . GLU A 1092 ? 0.2601 0.2413 0.2557 0.0198  0.0103  0.0165  1090 GLU A O   
8000  C CB  . GLU A 1092 ? 0.2796 0.2602 0.2693 0.0192  0.0112  0.0126  1090 GLU A CB  
8001  C CG  . GLU A 1092 ? 0.3454 0.3256 0.3326 0.0190  0.0106  0.0093  1090 GLU A CG  
8002  C CD  . GLU A 1092 ? 0.3205 0.3030 0.3053 0.0201  0.0108  0.0087  1090 GLU A CD  
8003  O OE1 . GLU A 1092 ? 0.2912 0.2776 0.2746 0.0216  0.0109  0.0095  1090 GLU A OE1 
8004  O OE2 . GLU A 1092 ? 0.3574 0.3383 0.3421 0.0197  0.0109  0.0074  1090 GLU A OE2 
8005  N N   . ARG A 1093 ? 0.2223 0.2017 0.2151 0.0187  0.0095  0.0111  1091 ARG A N   
8006  C CA  . ARG A 1093 ? 0.2275 0.2087 0.2206 0.0195  0.0088  0.0114  1091 ARG A CA  
8007  C C   . ARG A 1093 ? 0.2131 0.1963 0.2025 0.0199  0.0083  0.0096  1091 ARG A C   
8008  O O   . ARG A 1093 ? 0.2306 0.2125 0.2187 0.0190  0.0080  0.0070  1091 ARG A O   
8009  C CB  . ARG A 1093 ? 0.2629 0.2426 0.2587 0.0187  0.0082  0.0099  1091 ARG A CB  
8010  N N   . ASN A 1094 ? 0.2151 0.2018 0.2031 0.0213  0.0082  0.0111  1092 ASN A N   
8011  C CA  . ASN A 1094 ? 0.1977 0.1870 0.1824 0.0220  0.0076  0.0091  1092 ASN A CA  
8012  C C   . ASN A 1094 ? 0.2129 0.2044 0.1976 0.0227  0.0067  0.0091  1092 ASN A C   
8013  O O   . ASN A 1094 ? 0.2369 0.2309 0.2224 0.0237  0.0067  0.0120  1092 ASN A O   
8014  C CB  . ASN A 1094 ? 0.2026 0.1951 0.1852 0.0232  0.0082  0.0102  1092 ASN A CB  
8015  C CG  . ASN A 1094 ? 0.2106 0.2008 0.1929 0.0226  0.0089  0.0092  1092 ASN A CG  
8016  O OD1 . ASN A 1094 ? 0.2240 0.2124 0.2054 0.0220  0.0084  0.0062  1092 ASN A OD1 
8017  N ND2 . ASN A 1094 ? 0.2447 0.2349 0.2283 0.0226  0.0099  0.0119  1092 ASN A ND2 
8018  N N   . LEU A 1095 ? 0.2159 0.2065 0.2002 0.0220  0.0058  0.0062  1093 LEU A N   
8019  C CA  . LEU A 1095 ? 0.2116 0.2037 0.1964 0.0223  0.0049  0.0059  1093 LEU A CA  
8020  C C   . LEU A 1095 ? 0.2196 0.2147 0.2017 0.0230  0.0040  0.0037  1093 LEU A C   
8021  O O   . LEU A 1095 ? 0.2280 0.2225 0.2087 0.0225  0.0037  0.0013  1093 LEU A O   
8022  C CB  . LEU A 1095 ? 0.2398 0.2292 0.2268 0.0208  0.0046  0.0043  1093 LEU A CB  
8023  C CG  . LEU A 1095 ? 0.2907 0.2774 0.2807 0.0201  0.0054  0.0055  1093 LEU A CG  
8024  C CD1 . LEU A 1095 ? 0.3345 0.3197 0.3262 0.0188  0.0051  0.0034  1093 LEU A CD1 
8025  C CD2 . LEU A 1095 ? 0.2905 0.2781 0.2828 0.0213  0.0055  0.0087  1093 LEU A CD2 
8026  N N   . TYR A 1096 ? 0.2138 0.2122 0.1957 0.0240  0.0033  0.0045  1094 TYR A N   
8027  C CA  . TYR A 1096 ? 0.2054 0.2074 0.1849 0.0248  0.0022  0.0024  1094 TYR A CA  
8028  C C   . TYR A 1096 ? 0.2066 0.2095 0.1874 0.0247  0.0012  0.0020  1094 TYR A C   
8029  O O   . TYR A 1096 ? 0.2195 0.2235 0.2020 0.0254  0.0012  0.0047  1094 TYR A O   
8030  C CB  . TYR A 1096 ? 0.2156 0.2226 0.1930 0.0267  0.0025  0.0044  1094 TYR A CB  
8031  C CG  . TYR A 1096 ? 0.2204 0.2324 0.1953 0.0279  0.0013  0.0024  1094 TYR A CG  
8032  C CD1 . TYR A 1096 ? 0.2307 0.2437 0.2035 0.0282  0.0008  -0.0013 1094 TYR A CD1 
8033  C CD2 . TYR A 1096 ? 0.2362 0.2520 0.2111 0.0288  0.0005  0.0040  1094 TYR A CD2 
8034  C CE1 . TYR A 1096 ? 0.2242 0.2423 0.1951 0.0294  -0.0004 -0.0037 1094 TYR A CE1 
8035  C CE2 . TYR A 1096 ? 0.2337 0.2548 0.2063 0.0300  -0.0007 0.0019  1094 TYR A CE2 
8036  C CZ  . TYR A 1096 ? 0.2125 0.2347 0.1831 0.0303  -0.0011 -0.0021 1094 TYR A CZ  
8037  O OH  . TYR A 1096 ? 0.2288 0.2565 0.1974 0.0316  -0.0024 -0.0046 1094 TYR A OH  
8038  N N   . THR A 1097 ? 0.2084 0.2109 0.1889 0.0239  0.0002  -0.0012 1095 THR A N   
8039  C CA  . THR A 1097 ? 0.2058 0.2090 0.1879 0.0235  -0.0007 -0.0018 1095 THR A CA  
8040  C C   . THR A 1097 ? 0.2186 0.2246 0.1993 0.0237  -0.0022 -0.0047 1095 THR A C   
8041  O O   . THR A 1097 ? 0.2205 0.2262 0.1998 0.0235  -0.0026 -0.0071 1095 THR A O   
8042  C CB  . THR A 1097 ? 0.2509 0.2504 0.2355 0.0216  -0.0005 -0.0028 1095 THR A CB  
8043  O OG1 . THR A 1097 ? 0.3074 0.3047 0.2913 0.0202  -0.0006 -0.0051 1095 THR A OG1 
8044  C CG2 . THR A 1097 ? 0.2674 0.2644 0.2538 0.0214  0.0008  -0.0005 1095 THR A CG2 
8045  N N   . LEU A 1098 ? 0.2088 0.2176 0.1901 0.0243  -0.0031 -0.0046 1096 LEU A N   
8046  C CA  . LEU A 1098 ? 0.2171 0.2287 0.1975 0.0244  -0.0047 -0.0075 1096 LEU A CA  
8047  C C   . LEU A 1098 ? 0.1961 0.2062 0.1791 0.0227  -0.0054 -0.0090 1096 LEU A C   
8048  O O   . LEU A 1098 ? 0.2054 0.2156 0.1903 0.0226  -0.0052 -0.0075 1096 LEU A O   
8049  C CB  . LEU A 1098 ? 0.2159 0.2330 0.1948 0.0264  -0.0054 -0.0063 1096 LEU A CB  
8050  C CG  . LEU A 1098 ? 0.1956 0.2157 0.1719 0.0280  -0.0048 -0.0046 1096 LEU A CG  
8051  C CD1 . LEU A 1098 ? 0.2251 0.2515 0.2000 0.0299  -0.0057 -0.0032 1096 LEU A CD1 
8052  C CD2 . LEU A 1098 ? 0.2113 0.2312 0.1857 0.0280  -0.0049 -0.0079 1096 LEU A CD2 
8053  N N   . HIS A 1099 ? 0.1923 0.2011 0.1756 0.0213  -0.0063 -0.0120 1097 HIS A N   
8054  C CA  . HIS A 1099 ? 0.1980 0.2058 0.1839 0.0194  -0.0070 -0.0133 1097 HIS A CA  
8055  C C   . HIS A 1099 ? 0.2166 0.2270 0.2026 0.0194  -0.0089 -0.0161 1097 HIS A C   
8056  O O   . HIS A 1099 ? 0.2118 0.2247 0.1959 0.0209  -0.0098 -0.0175 1097 HIS A O   
8057  C CB  . HIS A 1099 ? 0.2305 0.2341 0.2176 0.0173  -0.0065 -0.0139 1097 HIS A CB  
8058  C CG  . HIS A 1099 ? 0.2474 0.2483 0.2345 0.0172  -0.0048 -0.0116 1097 HIS A CG  
8059  N ND1 . HIS A 1099 ? 0.3110 0.3108 0.3001 0.0159  -0.0040 -0.0106 1097 HIS A ND1 
8060  C CD2 . HIS A 1099 ? 0.2647 0.2644 0.2502 0.0182  -0.0037 -0.0103 1097 HIS A CD2 
8061  C CE1 . HIS A 1099 ? 0.3287 0.3264 0.3175 0.0161  -0.0026 -0.0090 1097 HIS A CE1 
8062  N NE2 . HIS A 1099 ? 0.3125 0.3098 0.2992 0.0174  -0.0024 -0.0086 1097 HIS A NE2 
8063  N N   . ALA A 1100 ? 0.2132 0.2237 0.2018 0.0177  -0.0097 -0.0171 1098 ALA A N   
8064  C CA  . ALA A 1100 ? 0.2233 0.2356 0.2128 0.0172  -0.0118 -0.0200 1098 ALA A CA  
8065  C C   . ALA A 1100 ? 0.2392 0.2490 0.2290 0.0165  -0.0126 -0.0223 1098 ALA A C   
8066  O O   . ALA A 1100 ? 0.2497 0.2558 0.2399 0.0155  -0.0116 -0.0214 1098 ALA A O   
8067  C CB  . ALA A 1100 ? 0.2094 0.2221 0.2021 0.0152  -0.0124 -0.0201 1098 ALA A CB  
8068  N N   . ARG A 1101 ? 0.2312 0.2433 0.2212 0.0171  -0.0145 -0.0254 1099 ARG A N   
8069  C CA  A ARG A 1101 ? 0.2508 0.2604 0.2421 0.0165  -0.0158 -0.0282 1099 ARG A CA  
8070  C CA  B ARG A 1101 ? 0.2508 0.2605 0.2421 0.0165  -0.0158 -0.0282 1099 ARG A CA  
8071  C C   . ARG A 1101 ? 0.2306 0.2373 0.2264 0.0135  -0.0168 -0.0285 1099 ARG A C   
8072  O O   . ARG A 1101 ? 0.2631 0.2660 0.2607 0.0122  -0.0170 -0.0288 1099 ARG A O   
8073  C CB  A ARG A 1101 ? 0.2798 0.2931 0.2703 0.0182  -0.0177 -0.0320 1099 ARG A CB  
8074  C CB  B ARG A 1101 ? 0.2797 0.2931 0.2702 0.0182  -0.0177 -0.0320 1099 ARG A CB  
8075  C CG  A ARG A 1101 ? 0.2635 0.2806 0.2496 0.0211  -0.0168 -0.0316 1099 ARG A CG  
8076  C CG  B ARG A 1101 ? 0.2649 0.2817 0.2512 0.0211  -0.0168 -0.0319 1099 ARG A CG  
8077  C CD  A ARG A 1101 ? 0.2479 0.2695 0.2333 0.0229  -0.0188 -0.0360 1099 ARG A CD  
8078  C CD  B ARG A 1101 ? 0.2826 0.2994 0.2690 0.0220  -0.0181 -0.0358 1099 ARG A CD  
8079  N NE  A ARG A 1101 ? 0.2327 0.2520 0.2194 0.0230  -0.0198 -0.0394 1099 ARG A NE  
8080  N NE  B ARG A 1101 ? 0.2548 0.2747 0.2372 0.0246  -0.0168 -0.0354 1099 ARG A NE  
8081  C CZ  A ARG A 1101 ? 0.2525 0.2724 0.2368 0.0247  -0.0188 -0.0398 1099 ARG A CZ  
8082  C CZ  B ARG A 1101 ? 0.2813 0.3031 0.2630 0.0261  -0.0177 -0.0390 1099 ARG A CZ  
8083  N NH1 A ARG A 1101 ? 0.2827 0.3053 0.2630 0.0262  -0.0167 -0.0365 1099 ARG A NH1 
8084  N NH1 B ARG A 1101 ? 0.2644 0.2849 0.2494 0.0256  -0.0200 -0.0436 1099 ARG A NH1 
8085  N NH2 A ARG A 1101 ? 0.2658 0.2837 0.2522 0.0248  -0.0200 -0.0434 1099 ARG A NH2 
8086  N NH2 B ARG A 1101 ? 0.2312 0.2567 0.2091 0.0284  -0.0163 -0.0380 1099 ARG A NH2 
8087  N N   . GLY A 1102 ? 0.2182 0.2269 0.2160 0.0123  -0.0176 -0.0283 1100 GLY A N   
8088  C CA  . GLY A 1102 ? 0.2515 0.2583 0.2538 0.0093  -0.0186 -0.0282 1100 GLY A CA  
8089  C C   . GLY A 1102 ? 0.2340 0.2441 0.2386 0.0088  -0.0207 -0.0301 1100 GLY A C   
8090  O O   . GLY A 1102 ? 0.2554 0.2690 0.2587 0.0096  -0.0202 -0.0294 1100 GLY A O   
8091  N N   . ARG A 1103 ? 0.2163 0.2251 0.2248 0.0074  -0.0230 -0.0326 1101 ARG A N   
8092  C CA  . ARG A 1103 ? 0.2233 0.2352 0.2347 0.0066  -0.0252 -0.0347 1101 ARG A CA  
8093  C C   . ARG A 1103 ? 0.2335 0.2473 0.2439 0.0090  -0.0271 -0.0391 1101 ARG A C   
8094  O O   . ARG A 1103 ? 0.2474 0.2587 0.2589 0.0093  -0.0283 -0.0416 1101 ARG A O   
8095  C CB  . ARG A 1103 ? 0.2315 0.2413 0.2491 0.0032  -0.0269 -0.0344 1101 ARG A CB  
8096  C CG  . ARG A 1103 ? 0.3061 0.3192 0.3272 0.0022  -0.0292 -0.0363 1101 ARG A CG  
8097  C CD  . ARG A 1103 ? 0.3462 0.3582 0.3732 -0.0015 -0.0301 -0.0342 1101 ARG A CD  
8098  N NE  . ARG A 1103 ? 0.4001 0.4137 0.4256 -0.0026 -0.0275 -0.0301 1101 ARG A NE  
8099  C CZ  . ARG A 1103 ? 0.5280 0.5406 0.5566 -0.0055 -0.0270 -0.0269 1101 ARG A CZ  
8100  N NH1 . ARG A 1103 ? 0.6063 0.6159 0.6400 -0.0080 -0.0288 -0.0266 1101 ARG A NH1 
8101  N NH2 . ARG A 1103 ? 0.4358 0.4510 0.4628 -0.0060 -0.0247 -0.0239 1101 ARG A NH2 
8102  N N   . ILE A 1104 ? 0.2062 0.2249 0.2144 0.0107  -0.0275 -0.0402 1102 ILE A N   
8103  C CA  . ILE A 1104 ? 0.2214 0.2435 0.2279 0.0131  -0.0292 -0.0444 1102 ILE A CA  
8104  C C   . ILE A 1104 ? 0.2211 0.2449 0.2324 0.0118  -0.0323 -0.0477 1102 ILE A C   
8105  O O   . ILE A 1104 ? 0.2209 0.2464 0.2341 0.0103  -0.0326 -0.0463 1102 ILE A O   
8106  C CB  . ILE A 1104 ? 0.2261 0.2533 0.2274 0.0159  -0.0279 -0.0431 1102 ILE A CB  
8107  C CG1 . ILE A 1104 ? 0.2446 0.2699 0.2421 0.0168  -0.0249 -0.0392 1102 ILE A CG1 
8108  C CG2 . ILE A 1104 ? 0.2277 0.2596 0.2269 0.0185  -0.0296 -0.0473 1102 ILE A CG2 
8109  C CD1 . ILE A 1104 ? 0.2578 0.2807 0.2536 0.0179  -0.0244 -0.0402 1102 ILE A CD1 
8110  N N   . LEU A 1105 ? 0.2094 0.2328 0.2230 0.0123  -0.0347 -0.0524 1103 LEU A N   
8111  C CA  . LEU A 1105 ? 0.2333 0.2587 0.2515 0.0115  -0.0379 -0.0563 1103 LEU A CA  
8112  C C   . LEU A 1105 ? 0.2147 0.2470 0.2292 0.0140  -0.0385 -0.0584 1103 LEU A C   
8113  O O   . LEU A 1105 ? 0.2460 0.2816 0.2560 0.0170  -0.0381 -0.0602 1103 LEU A O   
8114  C CB  . LEU A 1105 ? 0.2565 0.2791 0.2787 0.0115  -0.0405 -0.0611 1103 LEU A CB  
8115  C CG  . LEU A 1105 ? 0.2862 0.3110 0.3137 0.0110  -0.0443 -0.0663 1103 LEU A CG  
8116  C CD1 . LEU A 1105 ? 0.2843 0.3071 0.3180 0.0072  -0.0455 -0.0640 1103 LEU A CD1 
8117  C CD2 . LEU A 1105 ? 0.2935 0.3160 0.3246 0.0118  -0.0468 -0.0717 1103 LEU A CD2 
8118  N N   . LEU A 1106 ? 0.2155 0.2508 0.2319 0.0129  -0.0394 -0.0578 1104 LEU A N   
8119  C CA  . LEU A 1106 ? 0.2447 0.2869 0.2583 0.0151  -0.0404 -0.0598 1104 LEU A CA  
8120  C C   . LEU A 1106 ? 0.2631 0.3072 0.2816 0.0145  -0.0441 -0.0653 1104 LEU A C   
8121  O O   . LEU A 1106 ? 0.2438 0.2855 0.2683 0.0116  -0.0457 -0.0653 1104 LEU A O   
8122  C CB  . LEU A 1106 ? 0.2325 0.2773 0.2450 0.0146  -0.0390 -0.0557 1104 LEU A CB  
8123  C CG  . LEU A 1106 ? 0.2827 0.3258 0.2914 0.0151  -0.0355 -0.0503 1104 LEU A CG  
8124  C CD1 . LEU A 1106 ? 0.2581 0.3054 0.2656 0.0156  -0.0347 -0.0476 1104 LEU A CD1 
8125  C CD2 . LEU A 1106 ? 0.2761 0.3190 0.2796 0.0176  -0.0339 -0.0498 1104 LEU A CD2 
8126  N N   . VAL A 1107 ? 0.2239 0.2729 0.2401 0.0173  -0.0457 -0.0700 1105 VAL A N   
8127  C CA  . VAL A 1107 ? 0.2363 0.2882 0.2569 0.0172  -0.0495 -0.0760 1105 VAL A CA  
8128  C C   . VAL A 1107 ? 0.2391 0.2994 0.2557 0.0196  -0.0500 -0.0770 1105 VAL A C   
8129  O O   . VAL A 1107 ? 0.2484 0.3141 0.2608 0.0226  -0.0504 -0.0802 1105 VAL A O   
8130  C CB  . VAL A 1107 ? 0.2414 0.2918 0.2638 0.0184  -0.0513 -0.0817 1105 VAL A CB  
8131  C CG1 . VAL A 1107 ? 0.2632 0.3151 0.2921 0.0177  -0.0556 -0.0879 1105 VAL A CG1 
8132  C CG2 . VAL A 1107 ? 0.2620 0.3041 0.2872 0.0165  -0.0502 -0.0794 1105 VAL A CG2 
8133  N N   . PRO A 1108 ? 0.2298 0.2921 0.2473 0.0183  -0.0498 -0.0742 1106 PRO A N   
8134  C CA  . PRO A 1108 ? 0.2486 0.3190 0.2624 0.0205  -0.0503 -0.0746 1106 PRO A CA  
8135  C C   . PRO A 1108 ? 0.2710 0.3459 0.2888 0.0206  -0.0542 -0.0808 1106 PRO A C   
8136  O O   . PRO A 1108 ? 0.2823 0.3534 0.3066 0.0183  -0.0566 -0.0841 1106 PRO A O   
8137  C CB  . PRO A 1108 ? 0.2623 0.3319 0.2766 0.0189  -0.0486 -0.0690 1106 PRO A CB  
8138  C CG  . PRO A 1108 ? 0.2627 0.3259 0.2836 0.0151  -0.0491 -0.0683 1106 PRO A CG  
8139  C CD  . PRO A 1108 ? 0.2719 0.3295 0.2935 0.0149  -0.0489 -0.0699 1106 PRO A CD  
8140  N N   . ALA A 1109 ? 0.2381 0.3212 0.2519 0.0232  -0.0550 -0.0822 1107 ALA A N   
8141  C CA  . ALA A 1109 ? 0.2659 0.3547 0.2828 0.0234  -0.0587 -0.0878 1107 ALA A CA  
8142  C C   . ALA A 1109 ? 0.3182 0.4116 0.3349 0.0231  -0.0588 -0.0850 1107 ALA A C   
8143  O O   . ALA A 1109 ? 0.3192 0.4140 0.3411 0.0215  -0.0616 -0.0879 1107 ALA A O   
8144  C CB  . ALA A 1109 ? 0.2707 0.3669 0.2834 0.0270  -0.0601 -0.0931 1107 ALA A CB  
8145  N N   . THR A 1110 ? 0.2554 0.3512 0.2668 0.0245  -0.0561 -0.0794 1108 THR A N   
8146  C CA  . THR A 1110 ? 0.2538 0.3544 0.2650 0.0246  -0.0562 -0.0766 1108 THR A CA  
8147  C C   . THR A 1110 ? 0.2596 0.3553 0.2707 0.0232  -0.0531 -0.0698 1108 THR A C   
8148  O O   . THR A 1110 ? 0.2317 0.3217 0.2412 0.0229  -0.0506 -0.0670 1108 THR A O   
8149  C CB  . THR A 1110 ? 0.2848 0.3944 0.2898 0.0283  -0.0563 -0.0763 1108 THR A CB  
8150  O OG1 . THR A 1110 ? 0.2644 0.3730 0.2639 0.0300  -0.0532 -0.0719 1108 THR A OG1 
8151  C CG2 . THR A 1110 ? 0.2785 0.3943 0.2830 0.0300  -0.0593 -0.0835 1108 THR A CG2 
8152  N N   . GLU A 1111 ? 0.2731 0.3714 0.2860 0.0225  -0.0533 -0.0675 1109 GLU A N   
8153  C CA  . GLU A 1111 ? 0.2358 0.3307 0.2488 0.0216  -0.0505 -0.0616 1109 GLU A CA  
8154  C C   . GLU A 1111 ? 0.2722 0.3675 0.2792 0.0242  -0.0478 -0.0573 1109 GLU A C   
8155  O O   . GLU A 1111 ? 0.2358 0.3254 0.2422 0.0234  -0.0451 -0.0538 1109 GLU A O   
8156  C CB  . GLU A 1111 ? 0.2734 0.3724 0.2893 0.0209  -0.0514 -0.0604 1109 GLU A CB  
8157  C CG  . GLU A 1111 ? 0.2871 0.3843 0.3027 0.0207  -0.0486 -0.0546 1109 GLU A CG  
8158  C CD  . GLU A 1111 ? 0.3275 0.4285 0.3469 0.0198  -0.0496 -0.0539 1109 GLU A CD  
8159  O OE1 . GLU A 1111 ? 0.3297 0.4289 0.3545 0.0169  -0.0505 -0.0553 1109 GLU A OE1 
8160  O OE2 . GLU A 1111 ? 0.3634 0.4694 0.3808 0.0221  -0.0495 -0.0518 1109 GLU A OE2 
8161  N N   . SER A 1112 ? 0.2656 0.3679 0.2683 0.0271  -0.0484 -0.0575 1110 SER A N   
8162  C CA  . SER A 1112 ? 0.2828 0.3860 0.2804 0.0295  -0.0461 -0.0529 1110 SER A CA  
8163  C C   . SER A 1112 ? 0.2466 0.3450 0.2418 0.0296  -0.0445 -0.0533 1110 SER A C   
8164  O O   . SER A 1112 ? 0.2486 0.3431 0.2420 0.0299  -0.0418 -0.0489 1110 SER A O   
8165  C CB  . SER A 1112 ? 0.3013 0.4138 0.2950 0.0326  -0.0473 -0.0528 1110 SER A CB  
8166  O OG  . SER A 1112 ? 0.2932 0.4066 0.2827 0.0346  -0.0451 -0.0476 1110 SER A OG  
8167  N N   . GLY A 1113 ? 0.2414 0.3401 0.2371 0.0295  -0.0462 -0.0587 1111 GLY A N   
8168  C CA  . GLY A 1113 ? 0.2029 0.2967 0.1970 0.0295  -0.0449 -0.0595 1111 GLY A CA  
8169  C C   . GLY A 1113 ? 0.2165 0.3012 0.2136 0.0268  -0.0430 -0.0569 1111 GLY A C   
8170  O O   . GLY A 1113 ? 0.2323 0.3130 0.2271 0.0271  -0.0406 -0.0540 1111 GLY A O   
8171  N N   . LEU A 1114 ? 0.2150 0.2969 0.2175 0.0240  -0.0440 -0.0577 1112 LEU A N   
8172  C CA  . LEU A 1114 ? 0.2298 0.3042 0.2353 0.0214  -0.0422 -0.0549 1112 LEU A CA  
8173  C C   . LEU A 1114 ? 0.2256 0.2989 0.2286 0.0221  -0.0392 -0.0490 1112 LEU A C   
8174  O O   . LEU A 1114 ? 0.2153 0.2833 0.2175 0.0214  -0.0370 -0.0465 1112 LEU A O   
8175  C CB  . LEU A 1114 ? 0.2411 0.3144 0.2528 0.0184  -0.0439 -0.0561 1112 LEU A CB  
8176  C CG  . LEU A 1114 ? 0.2337 0.3009 0.2485 0.0155  -0.0419 -0.0526 1112 LEU A CG  
8177  C CD1 . LEU A 1114 ? 0.2601 0.3210 0.2744 0.0148  -0.0408 -0.0526 1112 LEU A CD1 
8178  C CD2 . LEU A 1114 ? 0.2823 0.3495 0.3034 0.0125  -0.0437 -0.0537 1112 LEU A CD2 
8179  N N   . TYR A 1115 ? 0.2285 0.3068 0.2306 0.0234  -0.0393 -0.0469 1113 TYR A N   
8180  C CA  . TYR A 1115 ? 0.2051 0.2824 0.2057 0.0242  -0.0368 -0.0417 1113 TYR A CA  
8181  C C   . TYR A 1115 ? 0.2277 0.3041 0.2236 0.0263  -0.0350 -0.0394 1113 TYR A C   
8182  O O   . TYR A 1115 ? 0.2240 0.2960 0.2195 0.0260  -0.0326 -0.0359 1113 TYR A O   
8183  C CB  . TYR A 1115 ? 0.2183 0.3016 0.2192 0.0256  -0.0377 -0.0401 1113 TYR A CB  
8184  C CG  . TYR A 1115 ? 0.2077 0.2921 0.2136 0.0236  -0.0391 -0.0415 1113 TYR A CG  
8185  C CD1 . TYR A 1115 ? 0.2142 0.2938 0.2240 0.0205  -0.0390 -0.0428 1113 TYR A CD1 
8186  C CD2 . TYR A 1115 ? 0.2711 0.3616 0.2777 0.0247  -0.0405 -0.0413 1113 TYR A CD2 
8187  C CE1 . TYR A 1115 ? 0.2675 0.3488 0.2822 0.0184  -0.0402 -0.0437 1113 TYR A CE1 
8188  C CE2 . TYR A 1115 ? 0.2394 0.3314 0.2508 0.0228  -0.0417 -0.0425 1113 TYR A CE2 
8189  C CZ  . TYR A 1115 ? 0.2538 0.3412 0.2692 0.0196  -0.0415 -0.0437 1113 TYR A CZ  
8190  O OH  . TYR A 1115 ? 0.2794 0.3689 0.2996 0.0176  -0.0427 -0.0446 1113 TYR A OH  
8191  N N   . HIS A 1116 ? 0.2270 0.3081 0.2194 0.0284  -0.0361 -0.0414 1114 HIS A N   
8192  C CA  . HIS A 1116 ? 0.2104 0.2913 0.1984 0.0303  -0.0344 -0.0392 1114 HIS A CA  
8193  C C   . HIS A 1116 ? 0.2109 0.2849 0.1992 0.0288  -0.0331 -0.0402 1114 HIS A C   
8194  O O   . HIS A 1116 ? 0.2227 0.2935 0.2091 0.0293  -0.0308 -0.0368 1114 HIS A O   
8195  C CB  . HIS A 1116 ? 0.2581 0.3468 0.2424 0.0328  -0.0359 -0.0414 1114 HIS A CB  
8196  C CG  . HIS A 1116 ? 0.2663 0.3621 0.2488 0.0349  -0.0364 -0.0383 1114 HIS A CG  
8197  N ND1 . HIS A 1116 ? 0.3015 0.4023 0.2858 0.0350  -0.0386 -0.0399 1114 HIS A ND1 
8198  C CD2 . HIS A 1116 ? 0.2764 0.3754 0.2558 0.0369  -0.0351 -0.0333 1114 HIS A CD2 
8199  C CE1 . HIS A 1116 ? 0.2790 0.3858 0.2613 0.0371  -0.0386 -0.0361 1114 HIS A CE1 
8200  N NE2 . HIS A 1116 ? 0.3422 0.4479 0.3216 0.0382  -0.0366 -0.0319 1114 HIS A NE2 
8201  N N   . GLN A 1117 ? 0.2164 0.2881 0.2075 0.0271  -0.0347 -0.0448 1115 GLN A N   
8202  C CA  . GLN A 1117 ? 0.2182 0.2832 0.2102 0.0257  -0.0336 -0.0455 1115 GLN A CA  
8203  C C   . GLN A 1117 ? 0.2052 0.2643 0.1992 0.0237  -0.0315 -0.0416 1115 GLN A C   
8204  O O   . GLN A 1117 ? 0.2156 0.2703 0.2082 0.0235  -0.0295 -0.0395 1115 GLN A O   
8205  C CB  . GLN A 1117 ? 0.2325 0.2958 0.2283 0.0240  -0.0361 -0.0509 1115 GLN A CB  
8206  C CG  . GLN A 1117 ? 0.2246 0.2933 0.2189 0.0260  -0.0383 -0.0559 1115 GLN A CG  
8207  C CD  . GLN A 1117 ? 0.2787 0.3452 0.2780 0.0242  -0.0410 -0.0614 1115 GLN A CD  
8208  O OE1 . GLN A 1117 ? 0.2414 0.3033 0.2456 0.0213  -0.0415 -0.0609 1115 GLN A OE1 
8209  N NE2 . GLN A 1117 ? 0.2330 0.3030 0.2314 0.0260  -0.0429 -0.0666 1115 GLN A NE2 
8210  N N   . LEU A 1118 ? 0.1935 0.2527 0.1910 0.0221  -0.0319 -0.0408 1116 LEU A N   
8211  C CA  A LEU A 1118 ? 0.2005 0.2552 0.2000 0.0202  -0.0300 -0.0374 1116 LEU A CA  
8212  C CA  B LEU A 1118 ? 0.2006 0.2554 0.2001 0.0202  -0.0300 -0.0374 1116 LEU A CA  
8213  C C   . LEU A 1118 ? 0.2166 0.2712 0.2133 0.0220  -0.0277 -0.0331 1116 LEU A C   
8214  O O   . LEU A 1118 ? 0.2117 0.2616 0.2083 0.0212  -0.0256 -0.0309 1116 LEU A O   
8215  C CB  A LEU A 1118 ? 0.2247 0.2812 0.2285 0.0185  -0.0310 -0.0377 1116 LEU A CB  
8216  C CB  B LEU A 1118 ? 0.2250 0.2818 0.2286 0.0187  -0.0310 -0.0375 1116 LEU A CB  
8217  C CG  A LEU A 1118 ? 0.2219 0.2748 0.2288 0.0161  -0.0294 -0.0352 1116 LEU A CG  
8218  C CG  B LEU A 1118 ? 0.2217 0.2769 0.2299 0.0158  -0.0328 -0.0404 1116 LEU A CG  
8219  C CD1 A LEU A 1118 ? 0.2252 0.2723 0.2329 0.0141  -0.0286 -0.0353 1116 LEU A CD1 
8220  C CD1 B LEU A 1118 ? 0.2290 0.2880 0.2405 0.0148  -0.0340 -0.0405 1116 LEU A CD1 
8221  C CD2 A LEU A 1118 ? 0.2594 0.3151 0.2708 0.0142  -0.0310 -0.0363 1116 LEU A CD2 
8222  C CD2 B LEU A 1118 ? 0.2148 0.2640 0.2249 0.0134  -0.0312 -0.0388 1116 LEU A CD2 
8223  N N   . ALA A 1119 ? 0.2225 0.2823 0.2170 0.0244  -0.0280 -0.0318 1117 ALA A N   
8224  C CA  . ALA A 1119 ? 0.2405 0.3000 0.2330 0.0261  -0.0261 -0.0274 1117 ALA A CA  
8225  C C   . ALA A 1119 ? 0.2242 0.2807 0.2136 0.0268  -0.0246 -0.0265 1117 ALA A C   
8226  O O   . ALA A 1119 ? 0.2207 0.2733 0.2102 0.0266  -0.0226 -0.0236 1117 ALA A O   
8227  C CB  . ALA A 1119 ? 0.2398 0.3058 0.2307 0.0286  -0.0271 -0.0259 1117 ALA A CB  
8228  N N   . ALA A 1120 ? 0.2047 0.2632 0.1918 0.0275  -0.0256 -0.0294 1118 ALA A N   
8229  C CA  . ALA A 1120 ? 0.1968 0.2530 0.1810 0.0283  -0.0243 -0.0288 1118 ALA A CA  
8230  C C   . ALA A 1120 ? 0.2266 0.2756 0.2129 0.0260  -0.0229 -0.0288 1118 ALA A C   
8231  O O   . ALA A 1120 ? 0.2053 0.2510 0.1904 0.0262  -0.0210 -0.0260 1118 ALA A O   
8232  C CB  . ALA A 1120 ? 0.2173 0.2775 0.1993 0.0295  -0.0258 -0.0329 1118 ALA A CB  
8233  N N   . ALA A 1121 ? 0.2051 0.2517 0.1946 0.0238  -0.0241 -0.0317 1119 ALA A N   
8234  C CA  . ALA A 1121 ? 0.2137 0.2541 0.2053 0.0215  -0.0231 -0.0316 1119 ALA A CA  
8235  C C   . ALA A 1121 ? 0.2007 0.2383 0.1936 0.0206  -0.0212 -0.0279 1119 ALA A C   
8236  O O   . ALA A 1121 ? 0.2070 0.2403 0.1997 0.0198  -0.0195 -0.0263 1119 ALA A O   
8237  C CB  . ALA A 1121 ? 0.2275 0.2666 0.2229 0.0193  -0.0252 -0.0352 1119 ALA A CB  
8238  N N   . LEU A 1122 ? 0.1953 0.2356 0.1899 0.0205  -0.0215 -0.0269 1120 LEU A N   
8239  C CA  . LEU A 1122 ? 0.1833 0.2218 0.1798 0.0197  -0.0198 -0.0241 1120 LEU A CA  
8240  C C   . LEU A 1122 ? 0.2007 0.2385 0.1950 0.0217  -0.0181 -0.0209 1120 LEU A C   
8241  O O   . LEU A 1122 ? 0.1997 0.2341 0.1948 0.0210  -0.0164 -0.0190 1120 LEU A O   
8242  C CB  . LEU A 1122 ? 0.2306 0.2727 0.2298 0.0193  -0.0208 -0.0242 1120 LEU A CB  
8243  C CG  . LEU A 1122 ? 0.2126 0.2554 0.2151 0.0169  -0.0224 -0.0269 1120 LEU A CG  
8244  C CD1 . LEU A 1122 ? 0.2350 0.2821 0.2398 0.0170  -0.0232 -0.0267 1120 LEU A CD1 
8245  C CD2 . LEU A 1122 ? 0.2478 0.2863 0.2525 0.0142  -0.0214 -0.0265 1120 LEU A CD2 
8246  N N   . ALA A 1123 ? 0.1984 0.2398 0.1901 0.0240  -0.0186 -0.0200 1121 ALA A N   
8247  C CA  . ALA A 1123 ? 0.1928 0.2340 0.1830 0.0258  -0.0172 -0.0164 1121 ALA A CA  
8248  C C   . ALA A 1123 ? 0.1992 0.2360 0.1877 0.0255  -0.0157 -0.0158 1121 ALA A C   
8249  O O   . ALA A 1123 ? 0.2143 0.2493 0.2028 0.0262  -0.0142 -0.0127 1121 ALA A O   
8250  C CB  . ALA A 1123 ? 0.2003 0.2470 0.1880 0.0283  -0.0182 -0.0154 1121 ALA A CB  
8251  N N   . THR A 1124 ? 0.1879 0.2230 0.1755 0.0244  -0.0161 -0.0186 1122 THR A N   
8252  C CA  . THR A 1124 ? 0.1800 0.2111 0.1663 0.0240  -0.0148 -0.0183 1122 THR A CA  
8253  C C   . THR A 1124 ? 0.1956 0.2219 0.1845 0.0214  -0.0141 -0.0190 1122 THR A C   
8254  O O   . THR A 1124 ? 0.2110 0.2337 0.1992 0.0207  -0.0134 -0.0193 1122 THR A O   
8255  C CB  . THR A 1124 ? 0.2151 0.2482 0.1989 0.0249  -0.0158 -0.0209 1122 THR A CB  
8256  O OG1 . THR A 1124 ? 0.2110 0.2459 0.1960 0.0242  -0.0179 -0.0247 1122 THR A OG1 
8257  C CG2 . THR A 1124 ? 0.2078 0.2461 0.1884 0.0276  -0.0157 -0.0190 1122 THR A CG2 
8258  N N   . GLY A 1125 ? 0.1949 0.2214 0.1866 0.0201  -0.0143 -0.0189 1123 GLY A N   
8259  C CA  . GLY A 1125 ? 0.2066 0.2297 0.2008 0.0178  -0.0135 -0.0187 1123 GLY A CA  
8260  C C   . GLY A 1125 ? 0.1849 0.2065 0.1808 0.0155  -0.0146 -0.0211 1123 GLY A C   
8261  O O   . GLY A 1125 ? 0.2190 0.2382 0.2168 0.0134  -0.0139 -0.0205 1123 GLY A O   
8262  N N   . ASN A 1126 ? 0.1948 0.2184 0.1905 0.0158  -0.0165 -0.0236 1124 ASN A N   
8263  C CA  . ASN A 1126 ? 0.1928 0.2144 0.1909 0.0137  -0.0180 -0.0260 1124 ASN A CA  
8264  C C   . ASN A 1126 ? 0.2038 0.2273 0.2056 0.0117  -0.0192 -0.0266 1124 ASN A C   
8265  O O   . ASN A 1126 ? 0.2252 0.2525 0.2274 0.0124  -0.0194 -0.0263 1124 ASN A O   
8266  C CB  . ASN A 1126 ? 0.2013 0.2243 0.1981 0.0151  -0.0197 -0.0292 1124 ASN A CB  
8267  C CG  . ASN A 1126 ? 0.2074 0.2294 0.2006 0.0171  -0.0186 -0.0287 1124 ASN A CG  
8268  O OD1 . ASN A 1126 ? 0.2220 0.2401 0.2154 0.0163  -0.0178 -0.0284 1124 ASN A OD1 
8269  N ND2 . ASN A 1126 ? 0.1958 0.2219 0.1859 0.0196  -0.0186 -0.0285 1124 ASN A ND2 
8270  N N   . SER A 1127 ? 0.2088 0.2299 0.2138 0.0092  -0.0201 -0.0275 1125 SER A N   
8271  C CA  . SER A 1127 ? 0.2117 0.2349 0.2207 0.0072  -0.0219 -0.0287 1125 SER A CA  
8272  C C   . SER A 1127 ? 0.2115 0.2354 0.2214 0.0078  -0.0245 -0.0324 1125 SER A C   
8273  O O   . SER A 1127 ? 0.2138 0.2367 0.2212 0.0096  -0.0248 -0.0341 1125 SER A O   
8274  C CB  . SER A 1127 ? 0.2338 0.2546 0.2467 0.0039  -0.0218 -0.0272 1125 SER A CB  
8275  O OG  . SER A 1127 ? 0.3111 0.3276 0.3245 0.0032  -0.0223 -0.0279 1125 SER A OG  
8276  N N   . VAL A 1128 ? 0.2277 0.2539 0.2413 0.0063  -0.0266 -0.0340 1126 VAL A N   
8277  C CA  . VAL A 1128 ? 0.2352 0.2627 0.2501 0.0069  -0.0293 -0.0381 1126 VAL A CA  
8278  C C   . VAL A 1128 ? 0.2496 0.2758 0.2708 0.0038  -0.0316 -0.0392 1126 VAL A C   
8279  O O   . VAL A 1128 ? 0.2488 0.2754 0.2731 0.0012  -0.0311 -0.0367 1126 VAL A O   
8280  C CB  . VAL A 1128 ? 0.2474 0.2805 0.2603 0.0091  -0.0301 -0.0396 1126 VAL A CB  
8281  C CG1 . VAL A 1128 ? 0.2564 0.2910 0.2636 0.0122  -0.0282 -0.0380 1126 VAL A CG1 
8282  C CG2 . VAL A 1128 ? 0.2433 0.2794 0.2591 0.0075  -0.0304 -0.0381 1126 VAL A CG2 
8283  N N   . ALA A 1129 ? 0.2470 0.2720 0.2704 0.0039  -0.0340 -0.0431 1127 ALA A N   
8284  C CA  . ALA A 1129 ? 0.2455 0.2702 0.2755 0.0014  -0.0370 -0.0451 1127 ALA A CA  
8285  C C   . ALA A 1129 ? 0.2177 0.2464 0.2475 0.0034  -0.0394 -0.0498 1127 ALA A C   
8286  O O   . ALA A 1129 ? 0.2577 0.2866 0.2848 0.0059  -0.0401 -0.0531 1127 ALA A O   
8287  C CB  . ALA A 1129 ? 0.2839 0.3031 0.3181 -0.0003 -0.0382 -0.0458 1127 ALA A CB  
8288  N N   . ILE A 1130 ? 0.2349 0.2675 0.2673 0.0023  -0.0407 -0.0502 1128 ILE A N   
8289  C CA  . ILE A 1130 ? 0.2451 0.2824 0.2771 0.0042  -0.0430 -0.0545 1128 ILE A CA  
8290  C C   . ILE A 1130 ? 0.2761 0.3122 0.3152 0.0023  -0.0467 -0.0585 1128 ILE A C   
8291  O O   . ILE A 1130 ? 0.2822 0.3165 0.3274 -0.0011 -0.0477 -0.0568 1128 ILE A O   
8292  C CB  . ILE A 1130 ? 0.2402 0.2830 0.2711 0.0045  -0.0424 -0.0528 1128 ILE A CB  
8293  C CG1 . ILE A 1130 ? 0.2625 0.3058 0.2877 0.0060  -0.0389 -0.0485 1128 ILE A CG1 
8294  C CG2 . ILE A 1130 ? 0.2676 0.3158 0.2970 0.0069  -0.0447 -0.0570 1128 ILE A CG2 
8295  C CD1 . ILE A 1130 ? 0.2408 0.2886 0.2662 0.0059  -0.0383 -0.0464 1128 ILE A CD1 
8296  N N   . ASP A 1131 ? 0.2533 0.2909 0.2919 0.0045  -0.0489 -0.0639 1129 ASP A N   
8297  C CA  . ASP A 1131 ? 0.2786 0.3155 0.3243 0.0032  -0.0529 -0.0687 1129 ASP A CA  
8298  C C   . ASP A 1131 ? 0.2800 0.3200 0.3305 0.0009  -0.0547 -0.0685 1129 ASP A C   
8299  O O   . ASP A 1131 ? 0.2810 0.3269 0.3288 0.0025  -0.0549 -0.0697 1129 ASP A O   
8300  C CB  . ASP A 1131 ? 0.2572 0.2975 0.3004 0.0066  -0.0548 -0.0750 1129 ASP A CB  
8301  C CG  . ASP A 1131 ? 0.3342 0.3738 0.3850 0.0056  -0.0591 -0.0809 1129 ASP A CG  
8302  O OD1 . ASP A 1131 ? 0.3155 0.3498 0.3736 0.0023  -0.0605 -0.0799 1129 ASP A OD1 
8303  O OD2 . ASP A 1131 ? 0.3262 0.3709 0.3761 0.0079  -0.0613 -0.0865 1129 ASP A OD2 
8304  N N   . ALA A 1132 ? 0.2920 0.3285 0.3500 -0.0029 -0.0559 -0.0666 1130 ALA A N   
8305  C CA  . ALA A 1132 ? 0.3369 0.3764 0.4003 -0.0055 -0.0577 -0.0662 1130 ALA A CA  
8306  C C   . ALA A 1132 ? 0.3461 0.3887 0.4133 -0.0046 -0.0618 -0.0727 1130 ALA A C   
8307  O O   . ALA A 1132 ? 0.3547 0.4019 0.4241 -0.0054 -0.0630 -0.0732 1130 ALA A O   
8308  C CB  . ALA A 1132 ? 0.3381 0.3736 0.4090 -0.0099 -0.0582 -0.0622 1130 ALA A CB  
8309  N N   . ALA A 1133 ? 0.3022 0.3428 0.3705 -0.0029 -0.0639 -0.0780 1131 ALA A N   
8310  C CA  . ALA A 1133 ? 0.3647 0.4087 0.4363 -0.0018 -0.0678 -0.0850 1131 ALA A CA  
8311  C C   . ALA A 1133 ? 0.3667 0.4184 0.4311 0.0017  -0.0672 -0.0873 1131 ALA A C   
8312  O O   . ALA A 1133 ? 0.3612 0.4173 0.4280 0.0026  -0.0704 -0.0927 1131 ALA A O   
8313  C CB  . ALA A 1133 ? 0.3866 0.4269 0.4611 -0.0005 -0.0701 -0.0905 1131 ALA A CB  
8314  N N   . SER A 1134 ? 0.3338 0.3874 0.3897 0.0037  -0.0634 -0.0831 1132 SER A N   
8315  C CA  . SER A 1134 ? 0.2945 0.3557 0.3440 0.0068  -0.0628 -0.0840 1132 SER A CA  
8316  C C   . SER A 1134 ? 0.3175 0.3831 0.3698 0.0053  -0.0639 -0.0831 1132 SER A C   
8317  O O   . SER A 1134 ? 0.3110 0.3835 0.3600 0.0076  -0.0647 -0.0853 1132 SER A O   
8318  C CB  . SER A 1134 ? 0.2965 0.3578 0.3377 0.0087  -0.0584 -0.0787 1132 SER A CB  
8319  O OG  . SER A 1134 ? 0.2886 0.3479 0.3307 0.0063  -0.0561 -0.0726 1132 SER A OG  
8320  N N   . GLY A 1135 ? 0.3183 0.3809 0.3767 0.0015  -0.0640 -0.0798 1133 GLY A N   
8321  C CA  . GLY A 1135 ? 0.3074 0.3744 0.3688 -0.0001 -0.0649 -0.0786 1133 GLY A CA  
8322  C C   . GLY A 1135 ? 0.3367 0.4081 0.3917 0.0016  -0.0618 -0.0743 1133 GLY A C   
8323  O O   . GLY A 1135 ? 0.3425 0.4192 0.3987 0.0014  -0.0628 -0.0743 1133 GLY A O   
8324  N N   . LEU A 1136 ? 0.2860 0.3554 0.3347 0.0032  -0.0583 -0.0706 1134 LEU A N   
8325  C CA  . LEU A 1136 ? 0.3119 0.3851 0.3548 0.0053  -0.0556 -0.0669 1134 LEU A CA  
8326  C C   . LEU A 1136 ? 0.3018 0.3729 0.3459 0.0030  -0.0529 -0.0612 1134 LEU A C   
8327  O O   . LEU A 1136 ? 0.2937 0.3665 0.3332 0.0047  -0.0502 -0.0577 1134 LEU A O   
8328  C CB  . LEU A 1136 ? 0.2898 0.3632 0.3250 0.0089  -0.0537 -0.0666 1134 LEU A CB  
8329  C CG  . LEU A 1136 ? 0.2925 0.3707 0.3248 0.0119  -0.0559 -0.0719 1134 LEU A CG  
8330  C CD1 . LEU A 1136 ? 0.2834 0.3612 0.3085 0.0149  -0.0537 -0.0709 1134 LEU A CD1 
8331  C CD2 . LEU A 1136 ? 0.3115 0.3975 0.3430 0.0132  -0.0573 -0.0727 1134 LEU A CD2 
8332  N N   . GLN A 1137 ? 0.3137 0.3818 0.3644 -0.0007 -0.0536 -0.0601 1135 GLN A N   
8333  C CA  . GLN A 1137 ? 0.3344 0.4014 0.3864 -0.0030 -0.0510 -0.0548 1135 GLN A CA  
8334  C C   . GLN A 1137 ? 0.3079 0.3808 0.3585 -0.0021 -0.0499 -0.0528 1135 GLN A C   
8335  O O   . GLN A 1137 ? 0.3163 0.3891 0.3641 -0.0016 -0.0469 -0.0489 1135 GLN A O   
8336  C CB  . GLN A 1137 ? 0.3322 0.3966 0.3922 -0.0074 -0.0525 -0.0540 1135 GLN A CB  
8337  C CG  . GLN A 1137 ? 0.3326 0.3903 0.3945 -0.0087 -0.0528 -0.0541 1135 GLN A CG  
8338  C CD  . GLN A 1137 ? 0.3266 0.3827 0.3913 -0.0081 -0.0564 -0.0599 1135 GLN A CD  
8339  O OE1 . GLN A 1137 ? 0.3702 0.4304 0.4340 -0.0061 -0.0584 -0.0640 1135 GLN A OE1 
8340  N NE2 . GLN A 1137 ? 0.3852 0.4354 0.4533 -0.0096 -0.0573 -0.0603 1135 GLN A NE2 
8341  N N   . ALA A 1138 ? 0.2993 0.3773 0.3520 -0.0017 -0.0524 -0.0555 1136 ALA A N   
8342  C CA  . ALA A 1138 ? 0.2827 0.3665 0.3347 -0.0008 -0.0515 -0.0537 1136 ALA A CA  
8343  C C   . ALA A 1138 ? 0.3480 0.4336 0.3928 0.0032  -0.0495 -0.0523 1136 ALA A C   
8344  O O   . ALA A 1138 ? 0.4030 0.4928 0.4472 0.0042  -0.0485 -0.0503 1136 ALA A O   
8345  C CB  . ALA A 1138 ? 0.3065 0.3955 0.3625 -0.0013 -0.0549 -0.0571 1136 ALA A CB  
8346  N N   . SER A 1139 ? 0.3251 0.4078 0.3650 0.0054  -0.0489 -0.0532 1137 SER A N   
8347  C CA  . SER A 1139 ? 0.3345 0.4188 0.3680 0.0090  -0.0470 -0.0513 1137 SER A CA  
8348  C C   . SER A 1139 ? 0.2870 0.3676 0.3185 0.0089  -0.0435 -0.0469 1137 SER A C   
8349  O O   . SER A 1139 ? 0.3147 0.3965 0.3421 0.0116  -0.0418 -0.0447 1137 SER A O   
8350  C CB  . SER A 1139 ? 0.3390 0.4228 0.3680 0.0115  -0.0478 -0.0540 1137 SER A CB  
8351  O OG  . SER A 1139 ? 0.3466 0.4352 0.3767 0.0122  -0.0510 -0.0584 1137 SER A OG  
8352  N N   . LEU A 1140 ? 0.2958 0.3723 0.3306 0.0060  -0.0425 -0.0455 1138 LEU A N   
8353  C CA  . LEU A 1140 ? 0.2904 0.3636 0.3235 0.0057  -0.0393 -0.0418 1138 LEU A CA  
8354  C C   . LEU A 1140 ? 0.3442 0.4192 0.3817 0.0032  -0.0383 -0.0395 1138 LEU A C   
8355  O O   . LEU A 1140 ? 0.3999 0.4719 0.4384 0.0013  -0.0365 -0.0373 1138 LEU A O   
8356  C CB  . LEU A 1140 ? 0.3524 0.4194 0.3843 0.0049  -0.0384 -0.0416 1138 LEU A CB  
8357  C CG  . LEU A 1140 ? 0.3730 0.4378 0.3994 0.0078  -0.0380 -0.0426 1138 LEU A CG  
8358  C CD1 . LEU A 1140 ? 0.3775 0.4362 0.4033 0.0066  -0.0366 -0.0415 1138 LEU A CD1 
8359  C CD2 . LEU A 1140 ? 0.3381 0.4055 0.3600 0.0110  -0.0364 -0.0404 1138 LEU A CD2 
8360  N N   . LYS A 1141 ? 0.3438 0.4244 0.3841 0.0030  -0.0396 -0.0401 1139 LYS A N   
8361  C CA  . LYS A 1141 ? 0.3878 0.4713 0.4325 0.0007  -0.0387 -0.0381 1139 LYS A CA  
8362  C C   . LYS A 1141 ? 0.3635 0.4478 0.4059 0.0024  -0.0357 -0.0354 1139 LYS A C   
8363  O O   . LYS A 1141 ? 0.3478 0.4328 0.3866 0.0057  -0.0352 -0.0351 1139 LYS A O   
8364  C CB  . LYS A 1141 ? 0.4023 0.4918 0.4508 0.0002  -0.0410 -0.0398 1139 LYS A CB  
8365  N N   . ASN A 1142 ? 0.3698 0.4543 0.4147 0.0002  -0.0339 -0.0333 1140 ASN A N   
8366  C CA  . ASN A 1142 ? 0.3628 0.4492 0.4069 0.0015  -0.0314 -0.0313 1140 ASN A CA  
8367  C C   . ASN A 1142 ? 0.3339 0.4157 0.3730 0.0041  -0.0295 -0.0303 1140 ASN A C   
8368  O O   . ASN A 1142 ? 0.3062 0.3894 0.3439 0.0067  -0.0283 -0.0295 1140 ASN A O   
8369  C CB  . ASN A 1142 ? 0.3986 0.4913 0.4444 0.0033  -0.0319 -0.0317 1140 ASN A CB  
8370  C CG  . ASN A 1142 ? 0.4819 0.5793 0.5326 0.0009  -0.0341 -0.0329 1140 ASN A CG  
8371  O OD1 . ASN A 1142 ? 0.5345 0.6342 0.5855 0.0019  -0.0363 -0.0347 1140 ASN A OD1 
8372  N ND2 . ASN A 1142 ? 0.4224 0.5218 0.4771 -0.0025 -0.0334 -0.0316 1140 ASN A ND2 
8373  N N   . LEU A 1143 ? 0.3609 0.4372 0.3978 0.0034  -0.0294 -0.0303 1141 LEU A N   
8374  C CA  . LEU A 1143 ? 0.3417 0.4137 0.3742 0.0055  -0.0275 -0.0292 1141 LEU A CA  
8375  C C   . LEU A 1143 ? 0.3361 0.4087 0.3693 0.0053  -0.0250 -0.0272 1141 LEU A C   
8376  O O   . LEU A 1143 ? 0.3335 0.4081 0.3698 0.0027  -0.0244 -0.0265 1141 LEU A O   
8377  C CB  . LEU A 1143 ? 0.3374 0.4036 0.3680 0.0044  -0.0277 -0.0295 1141 LEU A CB  
8378  C CG  . LEU A 1143 ? 0.3199 0.3846 0.3482 0.0057  -0.0297 -0.0318 1141 LEU A CG  
8379  C CD1 . LEU A 1143 ? 0.3070 0.3661 0.3344 0.0044  -0.0297 -0.0321 1141 LEU A CD1 
8380  C CD2 . LEU A 1143 ? 0.3208 0.3863 0.3449 0.0095  -0.0293 -0.0315 1141 LEU A CD2 
8381  N N   . PRO A 1144 ? 0.2971 0.3681 0.3275 0.0081  -0.0235 -0.0264 1142 PRO A N   
8382  C CA  . PRO A 1144 ? 0.3124 0.3830 0.3432 0.0080  -0.0211 -0.0250 1142 PRO A CA  
8383  C C   . PRO A 1144 ? 0.2985 0.3653 0.3287 0.0053  -0.0202 -0.0242 1142 PRO A C   
8384  O O   . PRO A 1144 ? 0.2828 0.3454 0.3111 0.0047  -0.0211 -0.0245 1142 PRO A O   
8385  C CB  . PRO A 1144 ? 0.3685 0.4365 0.3964 0.0114  -0.0202 -0.0243 1142 PRO A CB  
8386  C CG  . PRO A 1144 ? 0.3677 0.4367 0.3942 0.0134  -0.0222 -0.0249 1142 PRO A CG  
8387  C CD  . PRO A 1144 ? 0.3516 0.4209 0.3785 0.0113  -0.0240 -0.0264 1142 PRO A CD  
8388  N N   . GLN A 1145 ? 0.2918 0.3608 0.3240 0.0037  -0.0186 -0.0233 1143 GLN A N   
8389  C CA  . GLN A 1145 ? 0.3289 0.3951 0.3609 0.0010  -0.0177 -0.0221 1143 GLN A CA  
8390  C C   . GLN A 1145 ? 0.2882 0.3478 0.3162 0.0023  -0.0171 -0.0217 1143 GLN A C   
8391  O O   . GLN A 1145 ? 0.2672 0.3231 0.2947 0.0005  -0.0175 -0.0212 1143 GLN A O   
8392  C CB  . GLN A 1145 ? 0.3976 0.4682 0.4318 -0.0003 -0.0158 -0.0211 1143 GLN A CB  
8393  N N   . THR A 1146 ? 0.2881 0.3463 0.3137 0.0054  -0.0161 -0.0218 1144 THR A N   
8394  C CA  . THR A 1146 ? 0.2962 0.3486 0.3182 0.0066  -0.0154 -0.0212 1144 THR A CA  
8395  C C   . THR A 1146 ? 0.2655 0.3148 0.2856 0.0067  -0.0171 -0.0219 1144 THR A C   
8396  O O   . THR A 1146 ? 0.2723 0.3171 0.2904 0.0062  -0.0168 -0.0216 1144 THR A O   
8397  C CB  . THR A 1146 ? 0.3095 0.3614 0.3301 0.0099  -0.0145 -0.0209 1144 THR A CB  
8398  O OG1 . THR A 1146 ? 0.3102 0.3650 0.3314 0.0118  -0.0159 -0.0215 1144 THR A OG1 
8399  C CG2 . THR A 1146 ? 0.2946 0.3488 0.3171 0.0101  -0.0127 -0.0207 1144 THR A CG2 
8400  N N   . VAL A 1147 ? 0.2594 0.3113 0.2800 0.0076  -0.0189 -0.0232 1145 VAL A N   
8401  C CA  . VAL A 1147 ? 0.2365 0.2864 0.2555 0.0079  -0.0207 -0.0246 1145 VAL A CA  
8402  C C   . VAL A 1147 ? 0.2556 0.3048 0.2773 0.0047  -0.0221 -0.0254 1145 VAL A C   
8403  O O   . VAL A 1147 ? 0.2407 0.2861 0.2614 0.0041  -0.0228 -0.0262 1145 VAL A O   
8404  C CB  . VAL A 1147 ? 0.2485 0.3020 0.2670 0.0101  -0.0223 -0.0257 1145 VAL A CB  
8405  C CG1 . VAL A 1147 ? 0.2591 0.3112 0.2754 0.0107  -0.0241 -0.0275 1145 VAL A CG1 
8406  C CG2 . VAL A 1147 ? 0.2894 0.3437 0.3062 0.0131  -0.0211 -0.0242 1145 VAL A CG2 
8407  N N   . GLY A 1148 ? 0.2606 0.3135 0.2863 0.0024  -0.0225 -0.0252 1146 GLY A N   
8408  C CA  . GLY A 1148 ? 0.2632 0.3156 0.2925 -0.0009 -0.0238 -0.0254 1146 GLY A CA  
8409  C C   . GLY A 1148 ? 0.2702 0.3180 0.2991 -0.0026 -0.0228 -0.0240 1146 GLY A C   
8410  O O   . GLY A 1148 ? 0.2944 0.3392 0.3250 -0.0044 -0.0244 -0.0246 1146 GLY A O   
8411  N N   . LEU A 1149 ? 0.2456 0.2926 0.2724 -0.0020 -0.0204 -0.0222 1147 LEU A N   
8412  C CA  . LEU A 1149 ? 0.3031 0.3461 0.3294 -0.0035 -0.0194 -0.0207 1147 LEU A CA  
8413  C C   . LEU A 1149 ? 0.2790 0.3165 0.3027 -0.0023 -0.0202 -0.0219 1147 LEU A C   
8414  O O   . LEU A 1149 ? 0.3096 0.3434 0.3341 -0.0039 -0.0204 -0.0212 1147 LEU A O   
8415  C CB  . LEU A 1149 ? 0.3153 0.3587 0.3395 -0.0025 -0.0168 -0.0191 1147 LEU A CB  
8416  C CG  . LEU A 1149 ? 0.4217 0.4705 0.4486 -0.0043 -0.0156 -0.0177 1147 LEU A CG  
8417  C CD1 . LEU A 1149 ? 0.4163 0.4653 0.4411 -0.0029 -0.0131 -0.0170 1147 LEU A CD1 
8418  C CD2 . LEU A 1149 ? 0.4004 0.4497 0.4307 -0.0082 -0.0162 -0.0159 1147 LEU A CD2 
8419  N N   . ARG A 1150 ? 0.2607 0.2980 0.2814 0.0007  -0.0208 -0.0236 1148 ARG A N   
8420  C CA  . ARG A 1150 ? 0.2498 0.2831 0.2678 0.0022  -0.0214 -0.0250 1148 ARG A CA  
8421  C C   . ARG A 1150 ? 0.2460 0.2795 0.2659 0.0018  -0.0242 -0.0278 1148 ARG A C   
8422  O O   . ARG A 1150 ? 0.2675 0.2982 0.2855 0.0030  -0.0250 -0.0296 1148 ARG A O   
8423  C CB  . ARG A 1150 ? 0.2564 0.2903 0.2701 0.0057  -0.0204 -0.0251 1148 ARG A CB  
8424  C CG  . ARG A 1150 ? 0.2739 0.3061 0.2856 0.0065  -0.0179 -0.0228 1148 ARG A CG  
8425  C CD  . ARG A 1150 ? 0.2655 0.2951 0.2733 0.0090  -0.0173 -0.0227 1148 ARG A CD  
8426  N NE  . ARG A 1150 ? 0.2651 0.2936 0.2713 0.0102  -0.0152 -0.0207 1148 ARG A NE  
8427  C CZ  . ARG A 1150 ? 0.2418 0.2701 0.2453 0.0129  -0.0146 -0.0199 1148 ARG A CZ  
8428  N NH1 . ARG A 1150 ? 0.2221 0.2516 0.2236 0.0146  -0.0158 -0.0209 1148 ARG A NH1 
8429  N NH2 . ARG A 1150 ? 0.2398 0.2671 0.2429 0.0138  -0.0129 -0.0181 1148 ARG A NH2 
8430  N N   . VAL A 1151 ? 0.2247 0.2617 0.2484 0.0002  -0.0258 -0.0286 1149 VAL A N   
8431  C CA  . VAL A 1151 ? 0.2389 0.2767 0.2647 0.0000  -0.0287 -0.0317 1149 VAL A CA  
8432  C C   . VAL A 1151 ? 0.3016 0.3379 0.3332 -0.0036 -0.0303 -0.0315 1149 VAL A C   
8433  O O   . VAL A 1151 ? 0.3279 0.3663 0.3628 -0.0061 -0.0298 -0.0292 1149 VAL A O   
8434  C CB  . VAL A 1151 ? 0.2477 0.2910 0.2737 0.0012  -0.0296 -0.0328 1149 VAL A CB  
8435  C CG1 . VAL A 1151 ? 0.3030 0.3476 0.3321 0.0006  -0.0328 -0.0362 1149 VAL A CG1 
8436  C CG2 . VAL A 1151 ? 0.2599 0.3045 0.2808 0.0049  -0.0284 -0.0327 1149 VAL A CG2 
8437  N N   . SER A 1152 ? 0.2659 0.2989 0.2991 -0.0039 -0.0324 -0.0340 1150 SER A N   
8438  C CA  . SER A 1152 ? 0.2988 0.3306 0.3386 -0.0071 -0.0348 -0.0345 1150 SER A CA  
8439  C C   . SER A 1152 ? 0.3149 0.3473 0.3565 -0.0061 -0.0380 -0.0392 1150 SER A C   
8440  O O   . SER A 1152 ? 0.3026 0.3353 0.3398 -0.0029 -0.0381 -0.0420 1150 SER A O   
8441  C CB  . SER A 1152 ? 0.3407 0.3671 0.3823 -0.0089 -0.0346 -0.0328 1150 SER A CB  
8442  O OG  . SER A 1152 ? 0.3967 0.4194 0.4352 -0.0065 -0.0348 -0.0353 1150 SER A OG  
8443  N N   . TRP A 1153 ? 0.2880 0.3210 0.3363 -0.0088 -0.0406 -0.0401 1151 TRP A N   
8444  C CA  . TRP A 1153 ? 0.3040 0.3372 0.3554 -0.0084 -0.0441 -0.0450 1151 TRP A CA  
8445  C C   . TRP A 1153 ? 0.3366 0.3644 0.3937 -0.0104 -0.0463 -0.0460 1151 TRP A C   
8446  O O   . TRP A 1153 ? 0.3828 0.4085 0.4443 -0.0137 -0.0461 -0.0423 1151 TRP A O   
8447  C CB  . TRP A 1153 ? 0.3086 0.3467 0.3643 -0.0099 -0.0459 -0.0455 1151 TRP A CB  
8448  C CG  . TRP A 1153 ? 0.3134 0.3568 0.3640 -0.0074 -0.0444 -0.0455 1151 TRP A CG  
8449  C CD1 . TRP A 1153 ? 0.3309 0.3771 0.3791 -0.0075 -0.0417 -0.0417 1151 TRP A CD1 
8450  C CD2 . TRP A 1153 ? 0.3113 0.3582 0.3589 -0.0044 -0.0457 -0.0494 1151 TRP A CD2 
8451  N NE1 . TRP A 1153 ? 0.3499 0.4007 0.3943 -0.0047 -0.0413 -0.0429 1151 TRP A NE1 
8452  C CE2 . TRP A 1153 ? 0.3093 0.3607 0.3529 -0.0028 -0.0437 -0.0474 1151 TRP A CE2 
8453  C CE3 . TRP A 1153 ? 0.2748 0.3220 0.3228 -0.0028 -0.0485 -0.0546 1151 TRP A CE3 
8454  C CZ2 . TRP A 1153 ? 0.2944 0.3505 0.3345 0.0002  -0.0445 -0.0498 1151 TRP A CZ2 
8455  C CZ3 . TRP A 1153 ? 0.2985 0.3509 0.3426 0.0002  -0.0491 -0.0573 1151 TRP A CZ3 
8456  C CH2 . TRP A 1153 ? 0.3190 0.3757 0.3592 0.0016  -0.0471 -0.0545 1151 TRP A CH2 
8457  N N   . SER A 1154 ? 0.3081 0.3341 0.3651 -0.0084 -0.0484 -0.0509 1152 SER A N   
8458  C CA  . SER A 1154 ? 0.3273 0.3478 0.3893 -0.0096 -0.0504 -0.0524 1152 SER A CA  
8459  C C   . SER A 1154 ? 0.3430 0.3639 0.4112 -0.0097 -0.0547 -0.0580 1152 SER A C   
8460  O O   . SER A 1154 ? 0.3418 0.3656 0.4069 -0.0066 -0.0557 -0.0630 1152 SER A O   
8461  C CB  . SER A 1154 ? 0.3186 0.3361 0.3751 -0.0067 -0.0488 -0.0535 1152 SER A CB  
8462  O OG  . SER A 1154 ? 0.3346 0.3468 0.3965 -0.0077 -0.0509 -0.0552 1152 SER A OG  
8463  N N   . LYS A 1155 ? 0.3557 0.3742 0.4330 -0.0134 -0.0573 -0.0572 1153 LYS A N   
8464  C CA  . LYS A 1155 ? 0.3658 0.3833 0.4504 -0.0138 -0.0618 -0.0627 1153 LYS A CA  
8465  C C   . LYS A 1155 ? 0.3905 0.4021 0.4786 -0.0132 -0.0636 -0.0655 1153 LYS A C   
8466  O O   . LYS A 1155 ? 0.4841 0.4953 0.5762 -0.0119 -0.0671 -0.0719 1153 LYS A O   
8467  C CB  . LYS A 1155 ? 0.3958 0.4139 0.4896 -0.0181 -0.0641 -0.0604 1153 LYS A CB  
8468  N N   . ASP A 1156 ? 0.3645 0.3718 0.4513 -0.0140 -0.0614 -0.0613 1154 ASP A N   
8469  C CA  . ASP A 1156 ? 0.3829 0.3844 0.4730 -0.0134 -0.0629 -0.0633 1154 ASP A CA  
8470  C C   . ASP A 1156 ? 0.3866 0.3876 0.4673 -0.0106 -0.0589 -0.0616 1154 ASP A C   
8471  O O   . ASP A 1156 ? 0.3401 0.3392 0.4190 -0.0122 -0.0563 -0.0557 1154 ASP A O   
8472  C CB  . ASP A 1156 ? 0.4215 0.4183 0.5208 -0.0178 -0.0644 -0.0586 1154 ASP A CB  
8473  C CG  . ASP A 1156 ? 0.4849 0.4754 0.5887 -0.0174 -0.0662 -0.0603 1154 ASP A CG  
8474  O OD1 . ASP A 1156 ? 0.4864 0.4763 0.5860 -0.0137 -0.0660 -0.0653 1154 ASP A OD1 
8475  O OD2 . ASP A 1156 ? 0.5353 0.5218 0.6473 -0.0209 -0.0678 -0.0565 1154 ASP A OD2 
8476  N N   . TRP A 1157 ? 0.3430 0.3462 0.4179 -0.0065 -0.0586 -0.0667 1155 TRP A N   
8477  C CA  . TRP A 1157 ? 0.3033 0.3068 0.3690 -0.0038 -0.0548 -0.0650 1155 TRP A CA  
8478  C C   . TRP A 1157 ? 0.3598 0.3573 0.4273 -0.0047 -0.0541 -0.0624 1155 TRP A C   
8479  O O   . TRP A 1157 ? 0.3477 0.3445 0.4097 -0.0046 -0.0506 -0.0577 1155 TRP A O   
8480  C CB  . TRP A 1157 ? 0.3161 0.3232 0.3763 0.0006  -0.0551 -0.0710 1155 TRP A CB  
8481  C CG  . TRP A 1157 ? 0.3078 0.3214 0.3659 0.0019  -0.0560 -0.0739 1155 TRP A CG  
8482  C CD1 . TRP A 1157 ? 0.2885 0.3051 0.3478 -0.0001 -0.0560 -0.0714 1155 TRP A CD1 
8483  C CD2 . TRP A 1157 ? 0.2806 0.2991 0.3351 0.0056  -0.0571 -0.0801 1155 TRP A CD2 
8484  N NE1 . TRP A 1157 ? 0.3098 0.3325 0.3663 0.0022  -0.0571 -0.0755 1155 TRP A NE1 
8485  C CE2 . TRP A 1157 ? 0.2940 0.3182 0.3475 0.0056  -0.0578 -0.0808 1155 TRP A CE2 
8486  C CE3 . TRP A 1157 ? 0.2820 0.3013 0.3339 0.0089  -0.0576 -0.0851 1155 TRP A CE3 
8487  C CZ2 . TRP A 1157 ? 0.2982 0.3288 0.3482 0.0088  -0.0590 -0.0862 1155 TRP A CZ2 
8488  C CZ3 . TRP A 1157 ? 0.2933 0.3195 0.3418 0.0121  -0.0587 -0.0905 1155 TRP A CZ3 
8489  C CH2 . TRP A 1157 ? 0.3218 0.3536 0.3693 0.0120  -0.0594 -0.0909 1155 TRP A CH2 
8490  N N   . ALA A 1158 ? 0.3521 0.3453 0.4275 -0.0055 -0.0574 -0.0654 1156 ALA A N   
8491  C CA  . ALA A 1158 ? 0.3687 0.3562 0.4462 -0.0062 -0.0570 -0.0631 1156 ALA A CA  
8492  C C   . ALA A 1158 ? 0.4172 0.4025 0.4968 -0.0100 -0.0554 -0.0553 1156 ALA A C   
8493  O O   . ALA A 1158 ? 0.4713 0.4533 0.5497 -0.0103 -0.0537 -0.0519 1156 ALA A O   
8494  C CB  . ALA A 1158 ? 0.3972 0.3805 0.4839 -0.0063 -0.0613 -0.0681 1156 ALA A CB  
8495  N N   . ALA A 1159 ? 0.3703 0.3580 0.4532 -0.0130 -0.0559 -0.0524 1157 ALA A N   
8496  C CA  . ALA A 1159 ? 0.4182 0.4053 0.5030 -0.0167 -0.0544 -0.0449 1157 ALA A CA  
8497  C C   . ALA A 1159 ? 0.4176 0.4083 0.4932 -0.0158 -0.0498 -0.0409 1157 ALA A C   
8498  O O   . ALA A 1159 ? 0.4322 0.4223 0.5076 -0.0181 -0.0478 -0.0352 1157 ALA A O   
8499  C CB  . ALA A 1159 ? 0.4199 0.4089 0.5125 -0.0203 -0.0568 -0.0434 1157 ALA A CB  
8500  N N   . ASP A 1160 ? 0.3957 0.3902 0.4639 -0.0126 -0.0481 -0.0438 1158 ASP A N   
8501  C CA  . ASP A 1160 ? 0.3958 0.3940 0.4563 -0.0119 -0.0443 -0.0403 1158 ASP A CA  
8502  C C   . ASP A 1160 ? 0.3399 0.3372 0.3925 -0.0086 -0.0415 -0.0407 1158 ASP A C   
8503  O O   . ASP A 1160 ? 0.3595 0.3597 0.4059 -0.0074 -0.0384 -0.0385 1158 ASP A O   
8504  C CB  . ASP A 1160 ? 0.3934 0.3971 0.4522 -0.0112 -0.0445 -0.0420 1158 ASP A CB  
8505  C CG  . ASP A 1160 ? 0.4318 0.4368 0.4984 -0.0147 -0.0470 -0.0411 1158 ASP A CG  
8506  O OD1 . ASP A 1160 ? 0.4815 0.4845 0.5533 -0.0181 -0.0473 -0.0369 1158 ASP A OD1 
8507  O OD2 . ASP A 1160 ? 0.4064 0.4148 0.4743 -0.0141 -0.0488 -0.0444 1158 ASP A OD2 
8508  N N   . GLY A 1161 ? 0.3669 0.3605 0.4202 -0.0070 -0.0425 -0.0436 1159 GLY A N   
8509  C CA  . GLY A 1161 ? 0.3603 0.3530 0.4069 -0.0042 -0.0400 -0.0437 1159 GLY A CA  
8510  C C   . GLY A 1161 ? 0.3721 0.3618 0.4183 -0.0059 -0.0378 -0.0384 1159 GLY A C   
8511  O O   . GLY A 1161 ? 0.4219 0.4112 0.4721 -0.0092 -0.0379 -0.0343 1159 GLY A O   
8512  N N   . PRO A 1162 ? 0.3605 0.3485 0.4019 -0.0037 -0.0359 -0.0384 1160 PRO A N   
8513  C CA  . PRO A 1162 ? 0.3057 0.2948 0.3422 0.0002  -0.0355 -0.0427 1160 PRO A CA  
8514  C C   . PRO A 1162 ? 0.3382 0.3324 0.3681 0.0022  -0.0334 -0.0426 1160 PRO A C   
8515  O O   . PRO A 1162 ? 0.3333 0.3290 0.3604 0.0013  -0.0311 -0.0386 1160 PRO A O   
8516  C CB  . PRO A 1162 ? 0.3403 0.3260 0.3745 0.0009  -0.0337 -0.0410 1160 PRO A CB  
8517  C CG  . PRO A 1162 ? 0.4181 0.4033 0.4519 -0.0016 -0.0315 -0.0350 1160 PRO A CG  
8518  C CD  . PRO A 1162 ? 0.4001 0.3857 0.4401 -0.0050 -0.0336 -0.0336 1160 PRO A CD  
8519  N N   . PHE A 1163 ? 0.2912 0.2885 0.3189 0.0049  -0.0344 -0.0471 1161 PHE A N   
8520  C CA  . PHE A 1163 ? 0.2516 0.2538 0.2730 0.0072  -0.0325 -0.0468 1161 PHE A CA  
8521  C C   . PHE A 1163 ? 0.2549 0.2573 0.2705 0.0099  -0.0303 -0.0465 1161 PHE A C   
8522  O O   . PHE A 1163 ? 0.2926 0.2916 0.3091 0.0103  -0.0304 -0.0474 1161 PHE A O   
8523  C CB  . PHE A 1163 ? 0.2448 0.2514 0.2668 0.0086  -0.0349 -0.0515 1161 PHE A CB  
8524  C CG  . PHE A 1163 ? 0.2521 0.2586 0.2803 0.0058  -0.0374 -0.0520 1161 PHE A CG  
8525  C CD1 . PHE A 1163 ? 0.2678 0.2754 0.2966 0.0036  -0.0362 -0.0478 1161 PHE A CD1 
8526  C CD2 . PHE A 1163 ? 0.2559 0.2612 0.2901 0.0053  -0.0409 -0.0565 1161 PHE A CD2 
8527  C CE1 . PHE A 1163 ? 0.2892 0.2972 0.3240 0.0009  -0.0384 -0.0479 1161 PHE A CE1 
8528  C CE2 . PHE A 1163 ? 0.3110 0.3162 0.3517 0.0025  -0.0433 -0.0566 1161 PHE A CE2 
8529  C CZ  . PHE A 1163 ? 0.2973 0.3040 0.3382 0.0002  -0.0420 -0.0521 1161 PHE A CZ  
8530  N N   . ALA A 1164 ? 0.2496 0.2558 0.2596 0.0118  -0.0282 -0.0449 1162 ALA A N   
8531  C CA  . ALA A 1164 ? 0.2514 0.2583 0.2561 0.0142  -0.0260 -0.0440 1162 ALA A CA  
8532  C C   . ALA A 1164 ? 0.2365 0.2493 0.2372 0.0174  -0.0263 -0.0466 1162 ALA A C   
8533  O O   . ALA A 1164 ? 0.2709 0.2856 0.2669 0.0195  -0.0243 -0.0453 1162 ALA A O   
8534  C CB  . ALA A 1164 ? 0.2529 0.2588 0.2549 0.0135  -0.0230 -0.0387 1162 ALA A CB  
8535  N N   . GLY A 1165 ? 0.2269 0.2430 0.2294 0.0176  -0.0287 -0.0502 1163 GLY A N   
8536  C CA  . GLY A 1165 ? 0.2140 0.2367 0.2130 0.0205  -0.0293 -0.0531 1163 GLY A CA  
8537  C C   . GLY A 1165 ? 0.2423 0.2677 0.2443 0.0198  -0.0319 -0.0559 1163 GLY A C   
8538  O O   . GLY A 1165 ? 0.2358 0.2581 0.2426 0.0170  -0.0330 -0.0552 1163 GLY A O   
8539  N N   . ALA A 1166 ? 0.2355 0.2676 0.2349 0.0223  -0.0330 -0.0591 1164 ALA A N   
8540  C CA  . ALA A 1166 ? 0.2091 0.2444 0.2113 0.0218  -0.0356 -0.0621 1164 ALA A CA  
8541  C C   . ALA A 1166 ? 0.2320 0.2755 0.2292 0.0245  -0.0355 -0.0626 1164 ALA A C   
8542  O O   . ALA A 1166 ? 0.2603 0.3077 0.2529 0.0271  -0.0343 -0.0628 1164 ALA A O   
8543  C CB  . ALA A 1166 ? 0.2371 0.2715 0.2445 0.0215  -0.0389 -0.0684 1164 ALA A CB  
8544  N N   . LEU A 1167 ? 0.2191 0.2655 0.2176 0.0238  -0.0366 -0.0624 1165 LEU A N   
8545  C CA  . LEU A 1167 ? 0.2152 0.2698 0.2100 0.0262  -0.0372 -0.0632 1165 LEU A CA  
8546  C C   . LEU A 1167 ? 0.2434 0.3010 0.2421 0.0258  -0.0407 -0.0687 1165 LEU A C   
8547  O O   . LEU A 1167 ? 0.2422 0.2963 0.2462 0.0231  -0.0420 -0.0689 1165 LEU A O   
8548  C CB  . LEU A 1167 ? 0.2206 0.2763 0.2134 0.0258  -0.0353 -0.0575 1165 LEU A CB  
8549  C CG  . LEU A 1167 ? 0.2324 0.2850 0.2221 0.0260  -0.0320 -0.0519 1165 LEU A CG  
8550  C CD1 . LEU A 1167 ? 0.2437 0.2972 0.2326 0.0257  -0.0306 -0.0470 1165 LEU A CD1 
8551  C CD2 . LEU A 1167 ? 0.2498 0.3065 0.2344 0.0290  -0.0309 -0.0520 1165 LEU A CD2 
8552  N N   . VAL A 1168 ? 0.2308 0.2953 0.2271 0.0285  -0.0422 -0.0732 1166 VAL A N   
8553  C CA  . VAL A 1168 ? 0.2260 0.2940 0.2262 0.0285  -0.0459 -0.0796 1166 VAL A CA  
8554  C C   . VAL A 1168 ? 0.2506 0.3283 0.2467 0.0309  -0.0466 -0.0803 1166 VAL A C   
8555  O O   . VAL A 1168 ? 0.2286 0.3118 0.2188 0.0335  -0.0450 -0.0786 1166 VAL A O   
8556  C CB  . VAL A 1168 ? 0.2407 0.3083 0.2429 0.0297  -0.0477 -0.0861 1166 VAL A CB  
8557  C CG1 . VAL A 1168 ? 0.2599 0.3307 0.2669 0.0297  -0.0518 -0.0932 1166 VAL A CG1 
8558  C CG2 . VAL A 1168 ? 0.2538 0.3118 0.2599 0.0275  -0.0470 -0.0849 1166 VAL A CG2 
8559  N N   . GLU A 1169 ? 0.2150 0.2949 0.2146 0.0298  -0.0490 -0.0826 1167 GLU A N   
8560  C CA  . GLU A 1169 ? 0.2327 0.3222 0.2292 0.0319  -0.0503 -0.0840 1167 GLU A CA  
8561  C C   . GLU A 1169 ? 0.2558 0.3488 0.2564 0.0323  -0.0543 -0.0922 1167 GLU A C   
8562  O O   . GLU A 1169 ? 0.2674 0.3551 0.2749 0.0297  -0.0564 -0.0947 1167 GLU A O   
8563  C CB  . GLU A 1169 ? 0.2258 0.3157 0.2231 0.0305  -0.0498 -0.0793 1167 GLU A CB  
8564  C CG  . GLU A 1169 ? 0.2506 0.3504 0.2452 0.0326  -0.0513 -0.0804 1167 GLU A CG  
8565  C CD  . GLU A 1169 ? 0.2353 0.3349 0.2322 0.0309  -0.0515 -0.0770 1167 GLU A CD  
8566  O OE1 . GLU A 1169 ? 0.2276 0.3200 0.2286 0.0280  -0.0507 -0.0744 1167 GLU A OE1 
8567  O OE2 . GLU A 1169 ? 0.2542 0.3617 0.2489 0.0325  -0.0525 -0.0769 1167 GLU A OE2 
8568  N N   . GLY A 1170 ? 0.2401 0.3423 0.2369 0.0354  -0.0555 -0.0963 1168 GLY A N   
8569  C CA  . GLY A 1170 ? 0.2648 0.3715 0.2654 0.0360  -0.0595 -0.1045 1168 GLY A CA  
8570  C C   . GLY A 1170 ? 0.2997 0.4169 0.2952 0.0399  -0.0601 -0.1091 1168 GLY A C   
8571  O O   . GLY A 1170 ? 0.2856 0.4062 0.2748 0.0420  -0.0575 -0.1058 1168 GLY A O   
8572  N N   . ASP A 1171 ? 0.2778 0.4004 0.2763 0.0408  -0.0639 -0.1170 1169 ASP A N   
8573  C CA  . ASP A 1171 ? 0.2593 0.3921 0.2539 0.0445  -0.0649 -0.1229 1169 ASP A CA  
8574  C C   . ASP A 1171 ? 0.3025 0.4308 0.2988 0.0452  -0.0647 -0.1268 1169 ASP A C   
8575  O O   . ASP A 1171 ? 0.2745 0.3918 0.2752 0.0427  -0.0639 -0.1248 1169 ASP A O   
8576  C CB  . ASP A 1171 ? 0.2875 0.4289 0.2844 0.0456  -0.0690 -0.1304 1169 ASP A CB  
8577  C CG  . ASP A 1171 ? 0.3438 0.4786 0.3505 0.0434  -0.0728 -0.1372 1169 ASP A CG  
8578  O OD1 . ASP A 1171 ? 0.3196 0.4447 0.3312 0.0417  -0.0727 -0.1378 1169 ASP A OD1 
8579  O OD2 . ASP A 1171 ? 0.4248 0.5645 0.4346 0.0433  -0.0761 -0.1419 1169 ASP A OD2 
8580  N N   . ALA A 1172 ? 0.3028 0.4403 0.2956 0.0487  -0.0654 -0.1324 1170 ALA A N   
8581  C CA  . ALA A 1172 ? 0.2947 0.4294 0.2881 0.0499  -0.0647 -0.1357 1170 ALA A CA  
8582  C C   . ALA A 1172 ? 0.2995 0.4240 0.3025 0.0477  -0.0675 -0.1411 1170 ALA A C   
8583  O O   . ALA A 1172 ? 0.3112 0.4268 0.3166 0.0465  -0.0661 -0.1392 1170 ALA A O   
8584  C CB  . ALA A 1172 ? 0.3268 0.4748 0.3156 0.0541  -0.0656 -0.1421 1170 ALA A CB  
8585  N N   . GLU A 1173 ? 0.3252 0.4510 0.3344 0.0471  -0.0716 -0.1477 1171 GLU A N   
8586  C CA  . GLU A 1173 ? 0.3380 0.4544 0.3572 0.0451  -0.0746 -0.1529 1171 GLU A CA  
8587  C C   . GLU A 1173 ? 0.3242 0.4282 0.3481 0.0406  -0.0735 -0.1457 1171 GLU A C   
8588  O O   . GLU A 1173 ? 0.3240 0.4185 0.3542 0.0388  -0.0741 -0.1463 1171 GLU A O   
8589  C CB  . GLU A 1173 ? 0.3842 0.5056 0.4095 0.0458  -0.0796 -0.1627 1171 GLU A CB  
8590  C CG  . GLU A 1173 ? 0.3984 0.5313 0.4207 0.0503  -0.0812 -0.1715 1171 GLU A CG  
8591  C CD  . GLU A 1173 ? 0.4589 0.5890 0.4811 0.0520  -0.0799 -0.1738 1171 GLU A CD  
8592  O OE1 . GLU A 1173 ? 0.4597 0.5783 0.4894 0.0498  -0.0807 -0.1740 1171 GLU A OE1 
8593  O OE2 . GLU A 1173 ? 0.4713 0.6111 0.4862 0.0555  -0.0781 -0.1751 1171 GLU A OE2 
8594  N N   . ARG A 1174 ? 0.2938 0.3980 0.3148 0.0389  -0.0718 -0.1388 1172 ARG A N   
8595  C CA  . ARG A 1174 ? 0.2879 0.3816 0.3122 0.0350  -0.0701 -0.1314 1172 ARG A CA  
8596  C C   . ARG A 1174 ? 0.2812 0.3690 0.3019 0.0349  -0.0663 -0.1257 1172 ARG A C   
8597  O O   . ARG A 1174 ? 0.2794 0.3574 0.3052 0.0322  -0.0660 -0.1235 1172 ARG A O   
8598  C CB  . ARG A 1174 ? 0.2937 0.3903 0.3149 0.0338  -0.0689 -0.1254 1172 ARG A CB  
8599  C CG  . ARG A 1174 ? 0.2902 0.3776 0.3136 0.0300  -0.0666 -0.1174 1172 ARG A CG  
8600  C CD  . ARG A 1174 ? 0.3403 0.4194 0.3738 0.0266  -0.0694 -0.1197 1172 ARG A CD  
8601  N NE  . ARG A 1174 ? 0.3101 0.3815 0.3457 0.0230  -0.0673 -0.1120 1172 ARG A NE  
8602  C CZ  . ARG A 1174 ? 0.3556 0.4187 0.3991 0.0197  -0.0685 -0.1114 1172 ARG A CZ  
8603  N NH1 . ARG A 1174 ? 0.3371 0.3974 0.3879 0.0193  -0.0720 -0.1177 1172 ARG A NH1 
8604  N NH2 . ARG A 1174 ? 0.3177 0.3755 0.3621 0.0167  -0.0663 -0.1042 1172 ARG A NH2 
8605  N N   . ILE A 1175 ? 0.2655 0.3596 0.2775 0.0377  -0.0634 -0.1231 1173 ILE A N   
8606  C CA  . ILE A 1175 ? 0.2700 0.3594 0.2784 0.0379  -0.0598 -0.1181 1173 ILE A CA  
8607  C C   . ILE A 1175 ? 0.2693 0.3536 0.2828 0.0382  -0.0612 -0.1234 1173 ILE A C   
8608  O O   . ILE A 1175 ? 0.2783 0.3534 0.2943 0.0361  -0.0598 -0.1198 1173 ILE A O   
8609  C CB  . ILE A 1175 ? 0.2805 0.3791 0.2795 0.0411  -0.0570 -0.1153 1173 ILE A CB  
8610  C CG1 . ILE A 1175 ? 0.2940 0.3954 0.2888 0.0404  -0.0552 -0.1083 1173 ILE A CG1 
8611  C CG2 . ILE A 1175 ? 0.2789 0.3736 0.2749 0.0418  -0.0539 -0.1120 1173 ILE A CG2 
8612  C CD1 . ILE A 1175 ? 0.3059 0.4180 0.2924 0.0436  -0.0533 -0.1058 1173 ILE A CD1 
8613  N N   . ARG A 1176 ? 0.2912 0.3816 0.3065 0.0407  -0.0642 -0.1323 1174 ARG A N   
8614  C CA  . ARG A 1176 ? 0.3196 0.4055 0.3403 0.0413  -0.0658 -0.1380 1174 ARG A CA  
8615  C C   . ARG A 1176 ? 0.2789 0.3533 0.3096 0.0375  -0.0680 -0.1378 1174 ARG A C   
8616  O O   . ARG A 1176 ? 0.3006 0.3668 0.3344 0.0363  -0.0672 -0.1360 1174 ARG A O   
8617  C CB  . ARG A 1176 ? 0.2830 0.3781 0.3046 0.0448  -0.0690 -0.1485 1174 ARG A CB  
8618  C CG  . ARG A 1176 ? 0.3874 0.4808 0.4119 0.0468  -0.0698 -0.1541 1174 ARG A CG  
8619  C CD  . ARG A 1176 ? 0.3737 0.4750 0.4017 0.0498  -0.0739 -0.1657 1174 ARG A CD  
8620  N NE  . ARG A 1176 ? 0.3789 0.4942 0.3992 0.0529  -0.0735 -0.1678 1174 ARG A NE  
8621  C CZ  . ARG A 1176 ? 0.4391 0.5643 0.4519 0.0565  -0.0715 -0.1691 1174 ARG A CZ  
8622  N NH1 . ARG A 1176 ? 0.3868 0.5095 0.3984 0.0576  -0.0693 -0.1683 1174 ARG A NH1 
8623  N NH2 . ARG A 1176 ? 0.4126 0.5512 0.4193 0.0591  -0.0716 -0.1711 1174 ARG A NH2 
8624  N N   . ALA A 1177 ? 0.3014 0.3752 0.3370 0.0354  -0.0707 -0.1390 1175 ALA A N   
8625  C CA  . ALA A 1177 ? 0.3197 0.3835 0.3653 0.0315  -0.0729 -0.1382 1175 ALA A CA  
8626  C C   . ALA A 1177 ? 0.2771 0.3327 0.3215 0.0284  -0.0694 -0.1285 1175 ALA A C   
8627  O O   . ALA A 1177 ? 0.3050 0.3519 0.3554 0.0263  -0.0699 -0.1272 1175 ALA A O   
8628  C CB  . ALA A 1177 ? 0.3257 0.3917 0.3760 0.0298  -0.0760 -0.1404 1175 ALA A CB  
8629  N N   . VAL A 1178 ? 0.2776 0.3361 0.3145 0.0282  -0.0661 -0.1218 1176 VAL A N   
8630  C CA  . VAL A 1178 ? 0.2642 0.3159 0.2997 0.0256  -0.0627 -0.1129 1176 VAL A CA  
8631  C C   . VAL A 1178 ? 0.2798 0.3275 0.3129 0.0266  -0.0603 -0.1112 1176 VAL A C   
8632  O O   . VAL A 1178 ? 0.2831 0.3226 0.3197 0.0241  -0.0594 -0.1071 1176 VAL A O   
8633  C CB  . VAL A 1178 ? 0.2636 0.3199 0.2919 0.0257  -0.0598 -0.1068 1176 VAL A CB  
8634  C CG1 . VAL A 1178 ? 0.2522 0.3022 0.2783 0.0236  -0.0561 -0.0984 1176 VAL A CG1 
8635  C CG2 . VAL A 1178 ? 0.2774 0.3359 0.3094 0.0239  -0.0620 -0.1074 1176 VAL A CG2 
8636  N N   . ASN A 1179 ? 0.2975 0.3515 0.3246 0.0304  -0.0593 -0.1143 1177 ASN A N   
8637  C CA  . ASN A 1179 ? 0.2752 0.3264 0.2999 0.0316  -0.0570 -0.1128 1177 ASN A CA  
8638  C C   . ASN A 1179 ? 0.3319 0.3756 0.3651 0.0305  -0.0596 -0.1168 1177 ASN A C   
8639  O O   . ASN A 1179 ? 0.2894 0.3265 0.3235 0.0293  -0.0578 -0.1131 1177 ASN A O   
8640  C CB  . ASN A 1179 ? 0.3216 0.3824 0.3391 0.0359  -0.0560 -0.1162 1177 ASN A CB  
8641  C CG  . ASN A 1179 ? 0.3742 0.4343 0.3853 0.0369  -0.0519 -0.1109 1177 ASN A CG  
8642  O OD1 . ASN A 1179 ? 0.4312 0.4846 0.4419 0.0345  -0.0494 -0.1039 1177 ASN A OD1 
8643  N ND2 . ASN A 1179 ? 0.4273 0.4950 0.4337 0.0405  -0.0512 -0.1142 1177 ASN A ND2 
8644  N N   . LYS A 1180 ? 0.3110 0.3556 0.3512 0.0307  -0.0639 -0.1244 1178 LYS A N   
8645  C CA  . LYS A 1180 ? 0.3351 0.3723 0.3849 0.0295  -0.0668 -0.1281 1178 LYS A CA  
8646  C C   . LYS A 1180 ? 0.3055 0.3331 0.3611 0.0249  -0.0667 -0.1216 1178 LYS A C   
8647  O O   . LYS A 1180 ? 0.3017 0.3221 0.3615 0.0236  -0.0665 -0.1196 1178 LYS A O   
8648  C CB  . LYS A 1180 ? 0.3312 0.3717 0.3879 0.0307  -0.0717 -0.1379 1178 LYS A CB  
8649  C CG  . LYS A 1180 ? 0.3575 0.4079 0.4092 0.0356  -0.0721 -0.1454 1178 LYS A CG  
8650  C CD  . LYS A 1180 ? 0.3498 0.4052 0.4074 0.0368  -0.0769 -0.1550 1178 LYS A CD  
8651  C CE  . LYS A 1180 ? 0.4437 0.4908 0.5143 0.0350  -0.0813 -0.1599 1178 LYS A CE  
8652  N NZ  . LYS A 1180 ? 0.5144 0.5666 0.5911 0.0365  -0.0862 -0.1701 1178 LYS A NZ  
8653  N N   . ALA A 1181 ? 0.2845 0.3126 0.3407 0.0224  -0.0669 -0.1181 1179 ALA A N   
8654  C CA  . ALA A 1181 ? 0.2889 0.3094 0.3502 0.0180  -0.0666 -0.1115 1179 ALA A CA  
8655  C C   . ALA A 1181 ? 0.2650 0.2819 0.3207 0.0171  -0.0622 -0.1036 1179 ALA A C   
8656  O O   . ALA A 1181 ? 0.2892 0.2989 0.3496 0.0144  -0.0620 -0.0996 1179 ALA A O   
8657  C CB  . ALA A 1181 ? 0.2661 0.2893 0.3283 0.0158  -0.0673 -0.1095 1179 ALA A CB  
8658  N N   . ILE A 1182 ? 0.2818 0.3040 0.3276 0.0195  -0.0587 -0.1012 1180 ILE A N   
8659  C CA  . ILE A 1182 ? 0.2595 0.2786 0.3000 0.0189  -0.0545 -0.0940 1180 ILE A CA  
8660  C C   . ILE A 1182 ? 0.2982 0.3129 0.3402 0.0198  -0.0543 -0.0952 1180 ILE A C   
8661  O O   . ILE A 1182 ? 0.2835 0.2920 0.3269 0.0177  -0.0527 -0.0900 1180 ILE A O   
8662  C CB  . ILE A 1182 ? 0.2433 0.2693 0.2739 0.0213  -0.0512 -0.0913 1180 ILE A CB  
8663  C CG1 . ILE A 1182 ? 0.2752 0.3043 0.3047 0.0199  -0.0511 -0.0886 1180 ILE A CG1 
8664  C CG2 . ILE A 1182 ? 0.2816 0.3045 0.3071 0.0213  -0.0473 -0.0853 1180 ILE A CG2 
8665  C CD1 . ILE A 1182 ? 0.3049 0.3410 0.3256 0.0223  -0.0485 -0.0862 1180 ILE A CD1 
8666  N N   . ALA A 1183 ? 0.2659 0.2842 0.3078 0.0231  -0.0558 -0.1021 1181 ALA A N   
8667  C CA  . ALA A 1183 ? 0.2713 0.2858 0.3151 0.0243  -0.0557 -0.1038 1181 ALA A CA  
8668  C C   . ALA A 1183 ? 0.3222 0.3280 0.3761 0.0212  -0.0583 -0.1034 1181 ALA A C   
8669  O O   . ALA A 1183 ? 0.3039 0.3043 0.3591 0.0207  -0.0573 -0.1009 1181 ALA A O   
8670  C CB  . ALA A 1183 ? 0.2906 0.3114 0.3335 0.0284  -0.0575 -0.1124 1181 ALA A CB  
8671  N N   . ALA A 1184 ? 0.2764 0.2807 0.3376 0.0190  -0.0617 -0.1054 1182 ALA A N   
8672  C CA  . ALA A 1184 ? 0.2999 0.2963 0.3718 0.0159  -0.0646 -0.1047 1182 ALA A CA  
8673  C C   . ALA A 1184 ? 0.2831 0.2742 0.3553 0.0119  -0.0624 -0.0955 1182 ALA A C   
8674  O O   . ALA A 1184 ? 0.3108 0.2954 0.3914 0.0091  -0.0644 -0.0936 1182 ALA A O   
8675  C CB  . ALA A 1184 ? 0.2909 0.2878 0.3712 0.0147  -0.0693 -0.1100 1182 ALA A CB  
8676  N N   . LEU A 1185 ? 0.2701 0.2642 0.3339 0.0116  -0.0585 -0.0899 1183 LEU A N   
8677  C CA  . LEU A 1185 ? 0.3012 0.2913 0.3652 0.0081  -0.0564 -0.0817 1183 LEU A CA  
8678  C C   . LEU A 1185 ? 0.3011 0.2860 0.3654 0.0078  -0.0549 -0.0786 1183 LEU A C   
8679  O O   . LEU A 1185 ? 0.3134 0.2995 0.3731 0.0109  -0.0535 -0.0808 1183 LEU A O   
8680  C CB  . LEU A 1185 ? 0.2666 0.2614 0.3216 0.0084  -0.0526 -0.0771 1183 LEU A CB  
8681  C CG  . LEU A 1185 ? 0.2873 0.2877 0.3414 0.0085  -0.0537 -0.0792 1183 LEU A CG  
8682  C CD1 . LEU A 1185 ? 0.2824 0.2871 0.3277 0.0093  -0.0500 -0.0747 1183 LEU A CD1 
8683  C CD2 . LEU A 1185 ? 0.2993 0.2972 0.3621 0.0047  -0.0565 -0.0781 1183 LEU A CD2 
8684  N N   . PRO A 1186 ? 0.3189 0.2984 0.3887 0.0042  -0.0552 -0.0733 1184 PRO A N   
8685  C CA  . PRO A 1186 ? 0.2976 0.2723 0.3676 0.0038  -0.0538 -0.0699 1184 PRO A CA  
8686  C C   . PRO A 1186 ? 0.2820 0.2590 0.3420 0.0051  -0.0491 -0.0656 1184 PRO A C   
8687  O O   . PRO A 1186 ? 0.3019 0.2827 0.3562 0.0049  -0.0469 -0.0629 1184 PRO A O   
8688  C CB  . PRO A 1186 ? 0.3324 0.3024 0.4101 -0.0007 -0.0552 -0.0644 1184 PRO A CB  
8689  C CG  . PRO A 1186 ? 0.3849 0.3585 0.4623 -0.0027 -0.0552 -0.0626 1184 PRO A CG  
8690  C CD  . PRO A 1186 ? 0.3399 0.3181 0.4158 0.0002  -0.0568 -0.0698 1184 PRO A CD  
8691  N N   . GLY A 1187 ? 0.2738 0.2483 0.3321 0.0065  -0.0478 -0.0652 1185 GLY A N   
8692  C CA  . GLY A 1187 ? 0.3348 0.3101 0.3853 0.0070  -0.0437 -0.0603 1185 GLY A CA  
8693  C C   . GLY A 1187 ? 0.2591 0.2394 0.3013 0.0109  -0.0415 -0.0632 1185 GLY A C   
8694  O O   . GLY A 1187 ? 0.2993 0.2808 0.3418 0.0137  -0.0427 -0.0687 1185 GLY A O   
8695  N N   . PRO A 1188 ? 0.2751 0.2587 0.3102 0.0111  -0.0382 -0.0594 1186 PRO A N   
8696  C CA  . PRO A 1188 ? 0.2656 0.2534 0.2929 0.0145  -0.0357 -0.0603 1186 PRO A CA  
8697  C C   . PRO A 1188 ? 0.2548 0.2485 0.2803 0.0172  -0.0372 -0.0661 1186 PRO A C   
8698  O O   . PRO A 1188 ? 0.2669 0.2623 0.2950 0.0163  -0.0392 -0.0680 1186 PRO A O   
8699  C CB  . PRO A 1188 ? 0.2880 0.2771 0.3098 0.0134  -0.0324 -0.0543 1186 PRO A CB  
8700  C CG  . PRO A 1188 ? 0.2892 0.2777 0.3148 0.0104  -0.0337 -0.0525 1186 PRO A CG  
8701  C CD  . PRO A 1188 ? 0.2867 0.2705 0.3209 0.0084  -0.0369 -0.0541 1186 PRO A CD  
8702  N N   . LEU A 1189 ? 0.2599 0.2573 0.2810 0.0205  -0.0361 -0.0688 1187 LEU A N   
8703  C CA  . LEU A 1189 ? 0.2535 0.2582 0.2709 0.0233  -0.0367 -0.0731 1187 LEU A CA  
8704  C C   . LEU A 1189 ? 0.2689 0.2775 0.2810 0.0230  -0.0346 -0.0689 1187 LEU A C   
8705  O O   . LEU A 1189 ? 0.3088 0.3159 0.3172 0.0221  -0.0316 -0.0632 1187 LEU A O   
8706  C CB  . LEU A 1189 ? 0.2705 0.2791 0.2838 0.0268  -0.0355 -0.0759 1187 LEU A CB  
8707  C CG  . LEU A 1189 ? 0.2770 0.2845 0.2956 0.0284  -0.0382 -0.0826 1187 LEU A CG  
8708  C CD1 . LEU A 1189 ? 0.2852 0.2844 0.3094 0.0263  -0.0387 -0.0805 1187 LEU A CD1 
8709  C CD2 . LEU A 1189 ? 0.3207 0.3349 0.3343 0.0322  -0.0370 -0.0859 1187 LEU A CD2 
8710  N N   . LEU A 1190 ? 0.2573 0.2705 0.2694 0.0235  -0.0362 -0.0717 1188 LEU A N   
8711  C CA  . LEU A 1190 ? 0.2738 0.2906 0.2815 0.0232  -0.0346 -0.0680 1188 LEU A CA  
8712  C C   . LEU A 1190 ? 0.2364 0.2613 0.2378 0.0266  -0.0336 -0.0695 1188 LEU A C   
8713  O O   . LEU A 1190 ? 0.2824 0.3120 0.2841 0.0288  -0.0356 -0.0754 1188 LEU A O   
8714  C CB  . LEU A 1190 ? 0.2708 0.2877 0.2829 0.0212  -0.0370 -0.0691 1188 LEU A CB  
8715  C CG  . LEU A 1190 ? 0.2710 0.2809 0.2898 0.0174  -0.0381 -0.0669 1188 LEU A CG  
8716  C CD1 . LEU A 1190 ? 0.3405 0.3518 0.3627 0.0155  -0.0400 -0.0671 1188 LEU A CD1 
8717  C CD2 . LEU A 1190 ? 0.2902 0.2961 0.3069 0.0158  -0.0350 -0.0602 1188 LEU A CD2 
8718  N N   . LEU A 1191 ? 0.2436 0.2705 0.2395 0.0271  -0.0307 -0.0643 1189 LEU A N   
8719  C CA  . LEU A 1191 ? 0.2506 0.2857 0.2407 0.0300  -0.0297 -0.0644 1189 LEU A CA  
8720  C C   . LEU A 1191 ? 0.2421 0.2814 0.2327 0.0297  -0.0314 -0.0655 1189 LEU A C   
8721  O O   . LEU A 1191 ? 0.2646 0.3022 0.2553 0.0280  -0.0306 -0.0613 1189 LEU A O   
8722  C CB  . LEU A 1191 ? 0.2645 0.2996 0.2499 0.0302  -0.0263 -0.0580 1189 LEU A CB  
8723  C CG  . LEU A 1191 ? 0.2320 0.2750 0.2114 0.0333  -0.0248 -0.0571 1189 LEU A CG  
8724  C CD1 . LEU A 1191 ? 0.2491 0.2901 0.2256 0.0331  -0.0216 -0.0509 1189 LEU A CD1 
8725  C CD2 . LEU A 1191 ? 0.2436 0.2936 0.2208 0.0343  -0.0257 -0.0570 1189 LEU A CD2 
8726  N N   . VAL A 1192 ? 0.2301 0.2750 0.2211 0.0316  -0.0338 -0.0714 1190 VAL A N   
8727  C CA  . VAL A 1192 ? 0.2115 0.2610 0.2035 0.0315  -0.0359 -0.0735 1190 VAL A CA  
8728  C C   . VAL A 1192 ? 0.2215 0.2803 0.2072 0.0343  -0.0349 -0.0724 1190 VAL A C   
8729  O O   . VAL A 1192 ? 0.2625 0.3267 0.2445 0.0369  -0.0343 -0.0742 1190 VAL A O   
8730  C CB  . VAL A 1192 ? 0.2596 0.3097 0.2567 0.0317  -0.0397 -0.0813 1190 VAL A CB  
8731  C CG1 . VAL A 1192 ? 0.2906 0.3456 0.2889 0.0316  -0.0420 -0.0836 1190 VAL A CG1 
8732  C CG2 . VAL A 1192 ? 0.3056 0.3464 0.3096 0.0289  -0.0408 -0.0818 1190 VAL A CG2 
8733  N N   . GLN A 1193 ? 0.2436 0.3048 0.2281 0.0337  -0.0348 -0.0693 1191 GLN A N   
8734  C CA  . GLN A 1193 ? 0.2140 0.2847 0.1936 0.0361  -0.0346 -0.0686 1191 GLN A CA  
8735  C C   . GLN A 1193 ? 0.2395 0.3142 0.2215 0.0359  -0.0376 -0.0725 1191 GLN A C   
8736  O O   . GLN A 1193 ? 0.2492 0.3191 0.2354 0.0334  -0.0385 -0.0717 1191 GLN A O   
8737  C CB  . GLN A 1193 ? 0.2254 0.2960 0.2017 0.0359  -0.0319 -0.0610 1191 GLN A CB  
8738  C CG  . GLN A 1193 ? 0.2503 0.3166 0.2248 0.0358  -0.0290 -0.0567 1191 GLN A CG  
8739  C CD  . GLN A 1193 ? 0.2573 0.3253 0.2286 0.0362  -0.0266 -0.0498 1191 GLN A CD  
8740  O OE1 . GLN A 1193 ? 0.2729 0.3487 0.2402 0.0384  -0.0263 -0.0482 1191 GLN A OE1 
8741  N NE2 . GLN A 1193 ? 0.2581 0.3190 0.2313 0.0340  -0.0252 -0.0455 1191 GLN A NE2 
8742  N N   . ALA A 1194 ? 0.2297 0.3136 0.2092 0.0386  -0.0391 -0.0767 1192 ALA A N   
8743  C CA  . ALA A 1194 ? 0.2140 0.3025 0.1956 0.0386  -0.0421 -0.0810 1192 ALA A CA  
8744  C C   . ALA A 1194 ? 0.2262 0.3251 0.2025 0.0409  -0.0418 -0.0789 1192 ALA A C   
8745  O O   . ALA A 1194 ? 0.2523 0.3570 0.2234 0.0432  -0.0400 -0.0767 1192 ALA A O   
8746  C CB  . ALA A 1194 ? 0.2602 0.3507 0.2451 0.0396  -0.0452 -0.0898 1192 ALA A CB  
8747  N N   . ALA A 1195 ? 0.2269 0.3285 0.2048 0.0403  -0.0436 -0.0795 1193 ALA A N   
8748  C CA  . ALA A 1195 ? 0.2475 0.3593 0.2209 0.0424  -0.0439 -0.0778 1193 ALA A CA  
8749  C C   . ALA A 1195 ? 0.2437 0.3592 0.2204 0.0421  -0.0473 -0.0828 1193 ALA A C   
8750  O O   . ALA A 1195 ? 0.2659 0.3746 0.2483 0.0395  -0.0487 -0.0847 1193 ALA A O   
8751  C CB  . ALA A 1195 ? 0.2597 0.3700 0.2309 0.0418  -0.0413 -0.0692 1193 ALA A CB  
8752  N N   . SER A 1196 ? 0.2351 0.3618 0.2083 0.0446  -0.0486 -0.0848 1194 SER A N   
8753  C CA  . SER A 1196 ? 0.2568 0.3879 0.2327 0.0443  -0.0517 -0.0885 1194 SER A CA  
8754  C C   . SER A 1196 ? 0.2436 0.3738 0.2194 0.0431  -0.0507 -0.0818 1194 SER A C   
8755  O O   . SER A 1196 ? 0.2370 0.3655 0.2098 0.0432  -0.0479 -0.0746 1194 SER A O   
8756  C CB  . SER A 1196 ? 0.2788 0.4231 0.2507 0.0475  -0.0535 -0.0930 1194 SER A CB  
8757  O OG  . SER A 1196 ? 0.2933 0.4451 0.2591 0.0494  -0.0515 -0.0866 1194 SER A OG  
8758  N N   . SER A 1197 ? 0.2648 0.3961 0.2444 0.0419  -0.0533 -0.0844 1195 SER A N   
8759  C CA  . SER A 1197 ? 0.2837 0.4154 0.2634 0.0411  -0.0527 -0.0787 1195 SER A CA  
8760  C C   . SER A 1197 ? 0.2498 0.3911 0.2235 0.0439  -0.0516 -0.0741 1195 SER A C   
8761  O O   . SER A 1197 ? 0.2768 0.4164 0.2493 0.0437  -0.0496 -0.0669 1195 SER A O   
8762  C CB  . SER A 1197 ? 0.2896 0.4230 0.2742 0.0398  -0.0559 -0.0830 1195 SER A CB  
8763  O OG  . SER A 1197 ? 0.2845 0.4093 0.2755 0.0370  -0.0571 -0.0866 1195 SER A OG  
8764  N N   . GLY A 1198 ? 0.2863 0.4379 0.2563 0.0466  -0.0531 -0.0780 1196 GLY A N   
8765  C CA  . GLY A 1198 ? 0.2978 0.4595 0.2620 0.0492  -0.0522 -0.0733 1196 GLY A CA  
8766  C C   . GLY A 1198 ? 0.3089 0.4681 0.2695 0.0498  -0.0487 -0.0667 1196 GLY A C   
8767  O O   . GLY A 1198 ? 0.3091 0.4712 0.2673 0.0506  -0.0472 -0.0595 1196 GLY A O   
8768  N N   . GLU A 1199 ? 0.2817 0.4354 0.2426 0.0494  -0.0475 -0.0691 1197 GLU A N   
8769  C CA  . GLU A 1199 ? 0.3021 0.4524 0.2602 0.0496  -0.0442 -0.0631 1197 GLU A CA  
8770  C C   . GLU A 1199 ? 0.2861 0.4270 0.2467 0.0475  -0.0423 -0.0563 1197 GLU A C   
8771  O O   . GLU A 1199 ? 0.2774 0.4189 0.2356 0.0481  -0.0401 -0.0492 1197 GLU A O   
8772  C CB  . GLU A 1199 ? 0.2777 0.4231 0.2364 0.0494  -0.0437 -0.0678 1197 GLU A CB  
8773  C CG  . GLU A 1199 ? 0.3602 0.5039 0.3158 0.0500  -0.0406 -0.0631 1197 GLU A CG  
8774  C CD  . GLU A 1199 ? 0.4505 0.5903 0.4071 0.0500  -0.0405 -0.0687 1197 GLU A CD  
8775  O OE1 . GLU A 1199 ? 0.4039 0.5440 0.3633 0.0500  -0.0431 -0.0765 1197 GLU A OE1 
8776  O OE2 . GLU A 1199 ? 0.5061 0.6426 0.4610 0.0501  -0.0380 -0.0654 1197 GLU A OE2 
8777  N N   . ILE A 1200 ? 0.2602 0.3927 0.2260 0.0449  -0.0430 -0.0583 1198 ILE A N   
8778  C CA  . ILE A 1200 ? 0.2716 0.3963 0.2400 0.0430  -0.0413 -0.0524 1198 ILE A CA  
8779  C C   . ILE A 1200 ? 0.2982 0.4289 0.2654 0.0441  -0.0415 -0.0472 1198 ILE A C   
8780  O O   . ILE A 1200 ? 0.3026 0.4304 0.2696 0.0440  -0.0394 -0.0406 1198 ILE A O   
8781  C CB  . ILE A 1200 ? 0.2491 0.3658 0.2233 0.0401  -0.0425 -0.0558 1198 ILE A CB  
8782  C CG1 . ILE A 1200 ? 0.2625 0.3719 0.2384 0.0387  -0.0420 -0.0594 1198 ILE A CG1 
8783  C CG2 . ILE A 1200 ? 0.2639 0.3747 0.2408 0.0383  -0.0410 -0.0503 1198 ILE A CG2 
8784  C CD1 . ILE A 1200 ? 0.2687 0.3713 0.2505 0.0359  -0.0435 -0.0631 1198 ILE A CD1 
8785  N N   . ALA A 1201 ? 0.2765 0.4159 0.2430 0.0454  -0.0440 -0.0500 1199 ALA A N   
8786  C CA  . ALA A 1201 ? 0.3032 0.4489 0.2688 0.0466  -0.0444 -0.0451 1199 ALA A CA  
8787  C C   . ALA A 1201 ? 0.3130 0.4652 0.2739 0.0489  -0.0429 -0.0393 1199 ALA A C   
8788  O O   . ALA A 1201 ? 0.3194 0.4719 0.2806 0.0493  -0.0420 -0.0325 1199 ALA A O   
8789  C CB  . ALA A 1201 ? 0.3063 0.4603 0.2724 0.0473  -0.0477 -0.0500 1199 ALA A CB  
8790  N N   . ARG A 1202 ? 0.2761 0.4338 0.2330 0.0504  -0.0428 -0.0419 1200 ARG A N   
8791  C CA  . ARG A 1202 ? 0.2795 0.4455 0.2317 0.0527  -0.0416 -0.0366 1200 ARG A CA  
8792  C C   . ARG A 1202 ? 0.3244 0.4837 0.2762 0.0521  -0.0385 -0.0309 1200 ARG A C   
8793  O O   . ARG A 1202 ? 0.3260 0.4890 0.2762 0.0532  -0.0373 -0.0237 1200 ARG A O   
8794  C CB  . ARG A 1202 ? 0.3146 0.4911 0.2627 0.0548  -0.0428 -0.0420 1200 ARG A CB  
8795  C CG  . ARG A 1202 ? 0.2807 0.4671 0.2281 0.0560  -0.0459 -0.0467 1200 ARG A CG  
8796  C CD  . ARG A 1202 ? 0.3098 0.5077 0.2527 0.0584  -0.0469 -0.0519 1200 ARG A CD  
8797  N NE  . ARG A 1202 ? 0.3517 0.5440 0.2958 0.0578  -0.0467 -0.0588 1200 ARG A NE  
8798  C CZ  . ARG A 1202 ? 0.3445 0.5358 0.2913 0.0573  -0.0492 -0.0677 1200 ARG A CZ  
8799  N NH1 . ARG A 1202 ? 0.3001 0.4965 0.2484 0.0575  -0.0521 -0.0714 1200 ARG A NH1 
8800  N NH2 . ARG A 1202 ? 0.3525 0.5373 0.3010 0.0567  -0.0488 -0.0730 1200 ARG A NH2 
8801  N N   . ASN A 1203 ? 0.2859 0.4358 0.2394 0.0505  -0.0373 -0.0339 1201 ASN A N   
8802  C CA  . ASN A 1203 ? 0.2848 0.4296 0.2373 0.0503  -0.0345 -0.0296 1201 ASN A CA  
8803  C C   . ASN A 1203 ? 0.3238 0.4559 0.2807 0.0478  -0.0330 -0.0273 1201 ASN A C   
8804  O O   . ASN A 1203 ? 0.3103 0.4350 0.2698 0.0460  -0.0333 -0.0322 1201 ASN A O   
8805  C CB  . ASN A 1203 ? 0.3196 0.4654 0.2698 0.0508  -0.0341 -0.0350 1201 ASN A CB  
8806  C CG  . ASN A 1203 ? 0.3411 0.4821 0.2903 0.0506  -0.0313 -0.0310 1201 ASN A CG  
8807  O OD1 . ASN A 1203 ? 0.3575 0.4953 0.3074 0.0501  -0.0296 -0.0238 1201 ASN A OD1 
8808  N ND2 . ASN A 1203 ? 0.3505 0.4910 0.2984 0.0509  -0.0309 -0.0357 1201 ASN A ND2 
8809  N N   . PRO A 1204 ? 0.3257 0.4550 0.2837 0.0476  -0.0315 -0.0201 1202 PRO A N   
8810  C CA  . PRO A 1204 ? 0.3622 0.4800 0.3242 0.0455  -0.0301 -0.0183 1202 PRO A CA  
8811  C C   . PRO A 1204 ? 0.3326 0.4431 0.2946 0.0442  -0.0284 -0.0204 1202 PRO A C   
8812  O O   . PRO A 1204 ? 0.3611 0.4626 0.3265 0.0422  -0.0276 -0.0211 1202 PRO A O   
8813  C CB  . PRO A 1204 ? 0.4303 0.5485 0.3933 0.0461  -0.0289 -0.0103 1202 PRO A CB  
8814  C CG  . PRO A 1204 ? 0.4387 0.5684 0.3991 0.0483  -0.0304 -0.0080 1202 PRO A CG  
8815  C CD  . PRO A 1204 ? 0.3679 0.5046 0.3239 0.0494  -0.0312 -0.0132 1202 PRO A CD  
8816  N N   . ASP A 1205 ? 0.3522 0.4668 0.3105 0.0455  -0.0277 -0.0215 1203 ASP A N   
8817  C CA  . ASP A 1205 ? 0.3487 0.4571 0.3070 0.0446  -0.0262 -0.0237 1203 ASP A CA  
8818  C C   . ASP A 1205 ? 0.3526 0.4620 0.3106 0.0445  -0.0278 -0.0317 1203 ASP A C   
8819  O O   . ASP A 1205 ? 0.3772 0.4850 0.3339 0.0447  -0.0269 -0.0339 1203 ASP A O   
8820  C CB  . ASP A 1205 ? 0.4224 0.5340 0.3776 0.0459  -0.0243 -0.0191 1203 ASP A CB  
8821  C CG  . ASP A 1205 ? 0.4786 0.5882 0.4352 0.0457  -0.0229 -0.0111 1203 ASP A CG  
8822  O OD1 . ASP A 1205 ? 0.4222 0.5252 0.3825 0.0443  -0.0229 -0.0098 1203 ASP A OD1 
8823  O OD2 . ASP A 1205 ? 0.5010 0.6158 0.4553 0.0471  -0.0218 -0.0063 1203 ASP A OD2 
8824  N N   . ALA A 1206 ? 0.2989 0.4111 0.2583 0.0444  -0.0302 -0.0360 1204 ALA A N   
8825  C CA  . ALA A 1206 ? 0.2878 0.4003 0.2480 0.0442  -0.0321 -0.0440 1204 ALA A CA  
8826  C C   . ALA A 1206 ? 0.3007 0.4030 0.2638 0.0423  -0.0312 -0.0460 1204 ALA A C   
8827  O O   . ALA A 1206 ? 0.3418 0.4443 0.3043 0.0428  -0.0316 -0.0507 1204 ALA A O   
8828  C CB  . ALA A 1206 ? 0.2753 0.3895 0.2382 0.0436  -0.0348 -0.0476 1204 ALA A CB  
8829  N N   . TYR A 1207 ? 0.2851 0.3788 0.2512 0.0400  -0.0300 -0.0426 1205 TYR A N   
8830  C CA  . TYR A 1207 ? 0.2955 0.3797 0.2638 0.0381  -0.0287 -0.0430 1205 TYR A CA  
8831  C C   . TYR A 1207 ? 0.2971 0.3787 0.2637 0.0383  -0.0258 -0.0366 1205 TYR A C   
8832  O O   . TYR A 1207 ? 0.3584 0.4389 0.3257 0.0380  -0.0249 -0.0316 1205 TYR A O   
8833  C CB  . TYR A 1207 ? 0.2705 0.3477 0.2437 0.0354  -0.0294 -0.0437 1205 TYR A CB  
8834  C CG  . TYR A 1207 ? 0.2413 0.3205 0.2172 0.0348  -0.0323 -0.0497 1205 TYR A CG  
8835  C CD1 . TYR A 1207 ? 0.2607 0.3401 0.2375 0.0351  -0.0339 -0.0557 1205 TYR A CD1 
8836  C CD2 . TYR A 1207 ? 0.2407 0.3218 0.2187 0.0341  -0.0337 -0.0494 1205 TYR A CD2 
8837  C CE1 . TYR A 1207 ? 0.2374 0.3185 0.2174 0.0346  -0.0369 -0.0614 1205 TYR A CE1 
8838  C CE2 . TYR A 1207 ? 0.2566 0.3397 0.2376 0.0335  -0.0366 -0.0549 1205 TYR A CE2 
8839  C CZ  . TYR A 1207 ? 0.2542 0.3371 0.2363 0.0337  -0.0382 -0.0608 1205 TYR A CZ  
8840  O OH  . TYR A 1207 ? 0.2661 0.3508 0.2519 0.0330  -0.0413 -0.0664 1205 TYR A OH  
8841  N N   . CYS A 1208 ? 0.2672 0.3476 0.2320 0.0389  -0.0245 -0.0370 1206 CYS A N   
8842  C CA  . CYS A 1208 ? 0.2625 0.3412 0.2257 0.0392  -0.0219 -0.0312 1206 CYS A CA  
8843  C C   . CYS A 1208 ? 0.2449 0.3134 0.2114 0.0367  -0.0206 -0.0294 1206 CYS A C   
8844  O O   . CYS A 1208 ? 0.2446 0.3077 0.2132 0.0353  -0.0209 -0.0330 1206 CYS A O   
8845  C CB  . CYS A 1208 ? 0.2893 0.3719 0.2493 0.0409  -0.0211 -0.0325 1206 CYS A CB  
8846  S SG  . CYS A 1208 ? 0.3338 0.4147 0.2920 0.0412  -0.0181 -0.0256 1206 CYS A SG  
8847  N N   . LEU A 1209 ? 0.2225 0.2887 0.1897 0.0363  -0.0191 -0.0238 1207 LEU A N   
8848  C CA  . LEU A 1209 ? 0.2109 0.2684 0.1811 0.0341  -0.0179 -0.0222 1207 LEU A CA  
8849  C C   . LEU A 1209 ? 0.2307 0.2839 0.2002 0.0338  -0.0161 -0.0214 1207 LEU A C   
8850  O O   . LEU A 1209 ? 0.2401 0.2863 0.2120 0.0319  -0.0152 -0.0212 1207 LEU A O   
8851  C CB  . LEU A 1209 ? 0.2194 0.2763 0.1911 0.0341  -0.0171 -0.0171 1207 LEU A CB  
8852  C CG  . LEU A 1209 ? 0.2257 0.2871 0.1984 0.0345  -0.0189 -0.0175 1207 LEU A CG  
8853  C CD1 . LEU A 1209 ? 0.2727 0.3328 0.2476 0.0346  -0.0181 -0.0125 1207 LEU A CD1 
8854  C CD2 . LEU A 1209 ? 0.2646 0.3234 0.2400 0.0327  -0.0204 -0.0222 1207 LEU A CD2 
8855  N N   . ASN A 1210 ? 0.2441 0.3018 0.2104 0.0356  -0.0154 -0.0208 1208 ASN A N   
8856  C CA  . ASN A 1210 ? 0.2594 0.3135 0.2250 0.0354  -0.0138 -0.0204 1208 ASN A CA  
8857  C C   . ASN A 1210 ? 0.2457 0.2943 0.2134 0.0338  -0.0145 -0.0252 1208 ASN A C   
8858  O O   . ASN A 1210 ? 0.2718 0.3144 0.2406 0.0327  -0.0132 -0.0244 1208 ASN A O   
8859  C CB  . ASN A 1210 ? 0.2931 0.3546 0.2550 0.0377  -0.0134 -0.0204 1208 ASN A CB  
8860  C CG  . ASN A 1210 ? 0.2938 0.3610 0.2539 0.0391  -0.0125 -0.0145 1208 ASN A CG  
8861  O OD1 . ASN A 1210 ? 0.4159 0.4823 0.3776 0.0387  -0.0126 -0.0110 1208 ASN A OD1 
8862  N ND2 . ASN A 1210 ? 0.3840 0.4575 0.3409 0.0408  -0.0117 -0.0134 1208 ASN A ND2 
8863  N N   . TRP A 1211 ? 0.2452 0.2957 0.2137 0.0339  -0.0167 -0.0302 1209 TRP A N   
8864  C CA  . TRP A 1211 ? 0.2432 0.2892 0.2142 0.0326  -0.0178 -0.0350 1209 TRP A CA  
8865  C C   . TRP A 1211 ? 0.2667 0.3068 0.2419 0.0300  -0.0185 -0.0354 1209 TRP A C   
8866  O O   . TRP A 1211 ? 0.2864 0.3228 0.2645 0.0287  -0.0198 -0.0390 1209 TRP A O   
8867  C CB  . TRP A 1211 ? 0.2542 0.3059 0.2246 0.0343  -0.0199 -0.0408 1209 TRP A CB  
8868  C CG  . TRP A 1211 ? 0.2360 0.2963 0.2020 0.0371  -0.0194 -0.0402 1209 TRP A CG  
8869  C CD1 . TRP A 1211 ? 0.2514 0.3203 0.2152 0.0389  -0.0208 -0.0421 1209 TRP A CD1 
8870  C CD2 . TRP A 1211 ? 0.2301 0.2920 0.1932 0.0383  -0.0172 -0.0373 1209 TRP A CD2 
8871  N NE1 . TRP A 1211 ? 0.2836 0.3598 0.2433 0.0412  -0.0196 -0.0403 1209 TRP A NE1 
8872  C CE2 . TRP A 1211 ? 0.2288 0.3007 0.1881 0.0408  -0.0174 -0.0373 1209 TRP A CE2 
8873  C CE3 . TRP A 1211 ? 0.2384 0.2946 0.2019 0.0374  -0.0152 -0.0346 1209 TRP A CE3 
8874  C CZ2 . TRP A 1211 ? 0.2721 0.3487 0.2282 0.0424  -0.0156 -0.0344 1209 TRP A CZ2 
8875  C CZ3 . TRP A 1211 ? 0.2660 0.3264 0.2264 0.0391  -0.0135 -0.0320 1209 TRP A CZ3 
8876  C CH2 . TRP A 1211 ? 0.2787 0.3493 0.2355 0.0415  -0.0136 -0.0317 1209 TRP A CH2 
8877  N N   . LEU A 1212 ? 0.2240 0.2635 0.1999 0.0292  -0.0179 -0.0316 1210 LEU A N   
8878  C CA  . LEU A 1212 ? 0.2186 0.2535 0.1982 0.0267  -0.0183 -0.0315 1210 LEU A CA  
8879  C C   . LEU A 1212 ? 0.2032 0.2326 0.1837 0.0253  -0.0162 -0.0276 1210 LEU A C   
8880  O O   . LEU A 1212 ? 0.2120 0.2382 0.1955 0.0233  -0.0163 -0.0270 1210 LEU A O   
8881  C CB  . LEU A 1212 ? 0.2021 0.2411 0.1821 0.0270  -0.0195 -0.0311 1210 LEU A CB  
8882  C CG  . LEU A 1212 ? 0.2177 0.2612 0.1983 0.0276  -0.0221 -0.0360 1210 LEU A CG  
8883  C CD1 . LEU A 1212 ? 0.2301 0.2795 0.2099 0.0287  -0.0230 -0.0351 1210 LEU A CD1 
8884  C CD2 . LEU A 1212 ? 0.2516 0.2904 0.2366 0.0251  -0.0236 -0.0391 1210 LEU A CD2 
8885  N N   . VAL A 1213 ? 0.2135 0.2423 0.1918 0.0263  -0.0144 -0.0250 1211 VAL A N   
8886  C CA  . VAL A 1213 ? 0.2234 0.2469 0.2026 0.0251  -0.0125 -0.0219 1211 VAL A CA  
8887  C C   . VAL A 1213 ? 0.2135 0.2338 0.1924 0.0248  -0.0120 -0.0233 1211 VAL A C   
8888  O O   . VAL A 1213 ? 0.2302 0.2529 0.2076 0.0261  -0.0128 -0.0261 1211 VAL A O   
8889  C CB  . VAL A 1213 ? 0.2179 0.2427 0.1958 0.0262  -0.0108 -0.0173 1211 VAL A CB  
8890  C CG1 . VAL A 1213 ? 0.2391 0.2661 0.2183 0.0264  -0.0114 -0.0159 1211 VAL A CG1 
8891  C CG2 . VAL A 1213 ? 0.2257 0.2551 0.2003 0.0286  -0.0105 -0.0164 1211 VAL A CG2 
8892  N N   . GLU A 1214 ? 0.2234 0.2385 0.2039 0.0231  -0.0108 -0.0216 1212 GLU A N   
8893  C CA  . GLU A 1214 ? 0.2538 0.2652 0.2345 0.0226  -0.0102 -0.0224 1212 GLU A CA  
8894  C C   . GLU A 1214 ? 0.2202 0.2303 0.1995 0.0231  -0.0080 -0.0187 1212 GLU A C   
8895  O O   . GLU A 1214 ? 0.2145 0.2231 0.1947 0.0223  -0.0070 -0.0159 1212 GLU A O   
8896  C CB  . GLU A 1214 ? 0.3204 0.3271 0.3046 0.0199  -0.0108 -0.0232 1212 GLU A CB  
8897  C CG  . GLU A 1214 ? 0.4085 0.4111 0.3937 0.0191  -0.0105 -0.0238 1212 GLU A CG  
8898  C CD  . GLU A 1214 ? 0.4544 0.4534 0.4434 0.0164  -0.0116 -0.0244 1212 GLU A CD  
8899  O OE1 . GLU A 1214 ? 0.4580 0.4574 0.4493 0.0158  -0.0137 -0.0273 1212 GLU A OE1 
8900  O OE2 . GLU A 1214 ? 0.4914 0.4876 0.4814 0.0147  -0.0103 -0.0218 1212 GLU A OE2 
8901  N N   . GLU A 1215 ? 0.2221 0.2331 0.1994 0.0244  -0.0074 -0.0188 1213 GLU A N   
8902  C CA  . GLU A 1215 ? 0.2062 0.2159 0.1825 0.0248  -0.0054 -0.0154 1213 GLU A CA  
8903  C C   . GLU A 1215 ? 0.2060 0.2099 0.1842 0.0230  -0.0047 -0.0153 1213 GLU A C   
8904  O O   . GLU A 1215 ? 0.2202 0.2220 0.1996 0.0222  -0.0057 -0.0180 1213 GLU A O   
8905  C CB  . GLU A 1215 ? 0.2058 0.2193 0.1793 0.0269  -0.0049 -0.0156 1213 GLU A CB  
8906  C CG  . GLU A 1215 ? 0.2162 0.2366 0.1875 0.0289  -0.0055 -0.0155 1213 GLU A CG  
8907  C CD  . GLU A 1215 ? 0.2192 0.2444 0.1878 0.0309  -0.0054 -0.0169 1213 GLU A CD  
8908  O OE1 . GLU A 1215 ? 0.2395 0.2657 0.2082 0.0313  -0.0068 -0.0216 1213 GLU A OE1 
8909  O OE2 . GLU A 1215 ? 0.2329 0.2610 0.1999 0.0320  -0.0039 -0.0135 1213 GLU A OE2 
8910  N N   . VAL A 1216 ? 0.2038 0.2054 0.1826 0.0223  -0.0032 -0.0121 1214 VAL A N   
8911  C CA  . VAL A 1216 ? 0.2118 0.2086 0.1920 0.0207  -0.0024 -0.0116 1214 VAL A CA  
8912  C C   . VAL A 1216 ? 0.2178 0.2142 0.1971 0.0214  -0.0007 -0.0087 1214 VAL A C   
8913  O O   . VAL A 1216 ? 0.2280 0.2258 0.2073 0.0221  0.0000  -0.0061 1214 VAL A O   
8914  C CB  . VAL A 1216 ? 0.2267 0.2212 0.2094 0.0186  -0.0025 -0.0111 1214 VAL A CB  
8915  C CG1 . VAL A 1216 ? 0.2331 0.2237 0.2170 0.0170  -0.0016 -0.0103 1214 VAL A CG1 
8916  C CG2 . VAL A 1216 ? 0.2563 0.2513 0.2404 0.0175  -0.0043 -0.0137 1214 VAL A CG2 
8917  N N   . SER A 1217 ? 0.2120 0.2066 0.1911 0.0214  -0.0001 -0.0091 1215 SER A N   
8918  C CA  . SER A 1217 ? 0.2057 0.1996 0.1843 0.0218  0.0015  -0.0064 1215 SER A CA  
8919  C C   . SER A 1217 ? 0.2043 0.1936 0.1848 0.0199  0.0020  -0.0059 1215 SER A C   
8920  O O   . SER A 1217 ? 0.2142 0.2013 0.1957 0.0187  0.0012  -0.0078 1215 SER A O   
8921  C CB  . SER A 1217 ? 0.2160 0.2118 0.1928 0.0233  0.0017  -0.0073 1215 SER A CB  
8922  O OG  . SER A 1217 ? 0.2503 0.2443 0.2274 0.0231  0.0031  -0.0053 1215 SER A OG  
8923  N N   . ALA A 1218 ? 0.2018 0.1900 0.1833 0.0196  0.0032  -0.0033 1216 ALA A N   
8924  C CA  . ALA A 1218 ? 0.2149 0.1995 0.1979 0.0179  0.0038  -0.0029 1216 ALA A CA  
8925  C C   . ALA A 1218 ? 0.2298 0.2138 0.2130 0.0185  0.0051  -0.0006 1216 ALA A C   
8926  O O   . ALA A 1218 ? 0.2375 0.2230 0.2209 0.0195  0.0056  0.0016  1216 ALA A O   
8927  C CB  . ALA A 1218 ? 0.2253 0.2093 0.2102 0.0167  0.0037  -0.0026 1216 ALA A CB  
8928  N N   . SER A 1219 ? 0.2112 0.1931 0.1945 0.0179  0.0055  -0.0009 1217 SER A N   
8929  C CA  . SER A 1219 ? 0.2263 0.2074 0.2099 0.0182  0.0067  0.0011  1217 SER A CA  
8930  C C   . SER A 1219 ? 0.1905 0.1688 0.1760 0.0165  0.0071  0.0014  1217 SER A C   
8931  O O   . SER A 1219 ? 0.2180 0.1945 0.2036 0.0153  0.0066  0.0001  1217 SER A O   
8932  C CB  . SER A 1219 ? 0.2390 0.2209 0.2212 0.0191  0.0069  0.0004  1217 SER A CB  
8933  O OG  . SER A 1219 ? 0.2355 0.2170 0.2182 0.0193  0.0081  0.0026  1217 SER A OG  
8934  N N   . ILE A 1220 ? 0.2113 0.1892 0.1985 0.0164  0.0077  0.0031  1218 ILE A N   
8935  C CA  . ILE A 1220 ? 0.2220 0.1979 0.2111 0.0150  0.0080  0.0029  1218 ILE A CA  
8936  C C   . ILE A 1220 ? 0.2000 0.1749 0.1900 0.0152  0.0089  0.0046  1218 ILE A C   
8937  O O   . ILE A 1220 ? 0.2288 0.2044 0.2199 0.0161  0.0094  0.0065  1218 ILE A O   
8938  C CB  . ILE A 1220 ? 0.2529 0.2294 0.2440 0.0148  0.0078  0.0028  1218 ILE A CB  
8939  C CG1 . ILE A 1220 ? 0.2807 0.2586 0.2709 0.0146  0.0069  0.0014  1218 ILE A CG1 
8940  C CG2 . ILE A 1220 ? 0.2632 0.2387 0.2562 0.0134  0.0081  0.0021  1218 ILE A CG2 
8941  C CD1 . ILE A 1220 ? 0.4170 0.3963 0.4091 0.0151  0.0067  0.0014  1218 ILE A CD1 
8942  N N   . ASN A 1221 ? 0.2113 0.1847 0.2014 0.0141  0.0091  0.0040  1219 ASN A N   
8943  C CA  . ASN A 1221 ? 0.2141 0.1865 0.2053 0.0141  0.0099  0.0054  1219 ASN A CA  
8944  C C   . ASN A 1221 ? 0.2135 0.1853 0.2075 0.0133  0.0100  0.0054  1219 ASN A C   
8945  O O   . ASN A 1221 ? 0.2573 0.2287 0.2518 0.0120  0.0098  0.0041  1219 ASN A O   
8946  C CB  . ASN A 1221 ? 0.2479 0.2191 0.2384 0.0133  0.0099  0.0047  1219 ASN A CB  
8947  C CG  . ASN A 1221 ? 0.2311 0.2014 0.2230 0.0130  0.0106  0.0058  1219 ASN A CG  
8948  O OD1 . ASN A 1221 ? 0.2194 0.1899 0.2129 0.0135  0.0112  0.0073  1219 ASN A OD1 
8949  N ND2 . ASN A 1221 ? 0.2570 0.2262 0.2487 0.0121  0.0105  0.0053  1219 ASN A ND2 
8950  N N   . THR A 1222 ? 0.2086 0.1807 0.2047 0.0142  0.0103  0.0070  1220 THR A N   
8951  C CA  . THR A 1222 ? 0.2469 0.2184 0.2465 0.0137  0.0101  0.0066  1220 THR A CA  
8952  C C   . THR A 1222 ? 0.2876 0.2579 0.2892 0.0132  0.0106  0.0071  1220 THR A C   
8953  O O   . THR A 1222 ? 0.3374 0.3073 0.3425 0.0129  0.0103  0.0065  1220 THR A O   
8954  C CB  . THR A 1222 ? 0.2702 0.2423 0.2721 0.0149  0.0098  0.0080  1220 THR A CB  
8955  O OG1 . THR A 1222 ? 0.2630 0.2354 0.2652 0.0158  0.0103  0.0109  1220 THR A OG1 
8956  C CG2 . THR A 1222 ? 0.2688 0.2424 0.2688 0.0154  0.0093  0.0072  1220 THR A CG2 
8957  N N   . ALA A 1223 ? 0.2630 0.2329 0.2629 0.0130  0.0111  0.0079  1221 ALA A N   
8958  C CA  . ALA A 1223 ? 0.3084 0.2774 0.3100 0.0124  0.0114  0.0082  1221 ALA A CA  
8959  C C   . ALA A 1223 ? 0.3494 0.3182 0.3496 0.0111  0.0113  0.0064  1221 ALA A C   
8960  O O   . ALA A 1223 ? 0.4056 0.3739 0.4068 0.0104  0.0115  0.0065  1221 ALA A O   
8961  C CB  . ALA A 1223 ? 0.2840 0.2532 0.2849 0.0131  0.0122  0.0105  1221 ALA A CB  
8962  N N   . ALA A 1224 ? 0.3556 0.3250 0.3537 0.0106  0.0108  0.0050  1222 ALA A N   
8963  C CA  . ALA A 1224 ? 0.3992 0.3687 0.3959 0.0093  0.0105  0.0042  1222 ALA A CA  
8964  C C   . ALA A 1224 ? 0.4287 0.3991 0.4273 0.0082  0.0104  0.0031  1222 ALA A C   
8965  O O   . ALA A 1224 ? 0.4619 0.4324 0.4600 0.0072  0.0104  0.0032  1222 ALA A O   
8966  C CB  . ALA A 1224 ? 0.3730 0.3432 0.3679 0.0089  0.0099  0.0032  1222 ALA A CB  
8967  N N   . ALA A 1225 ? 0.3947 0.3659 0.3956 0.0084  0.0103  0.0021  1223 ALA A N   
8968  C CA  . ALA A 1225 ? 0.4197 0.3924 0.4226 0.0075  0.0102  0.0004  1223 ALA A CA  
8969  C C   . ALA A 1225 ? 0.4782 0.4499 0.4829 0.0074  0.0104  0.0011  1223 ALA A C   
8970  O O   . ALA A 1225 ? 0.4887 0.4619 0.4948 0.0067  0.0102  -0.0003 1223 ALA A O   
8971  C CB  . ALA A 1225 ? 0.4442 0.4182 0.4499 0.0081  0.0098  -0.0014 1223 ALA A CB  
8972  N N   . GLY A 1226 ? 0.4326 0.4022 0.4371 0.0082  0.0109  0.0033  1224 GLY A N   
8973  C CA  . GLY A 1226 ? 0.4268 0.3956 0.4331 0.0081  0.0112  0.0042  1224 GLY A CA  
8974  C C   . GLY A 1226 ? 0.4833 0.4509 0.4930 0.0090  0.0113  0.0056  1224 GLY A C   
8975  O O   . GLY A 1226 ? 0.4528 0.4199 0.4645 0.0088  0.0116  0.0066  1224 GLY A O   
8976  N N   . GLY A 1227 ? 0.3858 0.3532 0.3966 0.0098  0.0111  0.0058  1225 GLY A N   
8977  C CA  . GLY A 1227 ? 0.4483 0.4149 0.4630 0.0106  0.0111  0.0078  1225 GLY A CA  
8978  C C   . GLY A 1227 ? 0.4261 0.3928 0.4406 0.0116  0.0109  0.0087  1225 GLY A C   
8979  O O   . GLY A 1227 ? 0.4129 0.3804 0.4248 0.0117  0.0107  0.0072  1225 GLY A O   
8980  N N   . ASN A 1228 ? 0.3590 0.3253 0.3767 0.0123  0.0109  0.0114  1226 ASN A N   
8981  C CA  . ASN A 1228 ? 0.4035 0.3703 0.4216 0.0133  0.0106  0.0131  1226 ASN A CA  
8982  C C   . ASN A 1228 ? 0.4488 0.4145 0.4729 0.0135  0.0095  0.0126  1226 ASN A C   
8983  O O   . ASN A 1228 ? 0.4220 0.3867 0.4510 0.0134  0.0092  0.0144  1226 ASN A O   
8984  C CB  . ASN A 1228 ? 0.4081 0.3760 0.4252 0.0140  0.0113  0.0170  1226 ASN A CB  
8985  C CG  . ASN A 1228 ? 0.4519 0.4212 0.4684 0.0151  0.0111  0.0190  1226 ASN A CG  
8986  O OD1 . ASN A 1228 ? 0.4424 0.4111 0.4618 0.0154  0.0102  0.0186  1226 ASN A OD1 
8987  N ND2 . ASN A 1228 ? 0.4058 0.3774 0.4187 0.0158  0.0118  0.0211  1226 ASN A ND2 
8988  N N   . ALA A 1229 ? 0.4287 0.3948 0.4530 0.0139  0.0089  0.0102  1227 ALA A N   
8989  C CA  . ALA A 1229 ? 0.4347 0.4000 0.4651 0.0143  0.0077  0.0090  1227 ALA A CA  
8990  C C   . ALA A 1229 ? 0.4312 0.3958 0.4658 0.0151  0.0072  0.0131  1227 ALA A C   
8991  O O   . ALA A 1229 ? 0.4517 0.4146 0.4929 0.0152  0.0062  0.0137  1227 ALA A O   
8992  C CB  . ALA A 1229 ? 0.3986 0.3652 0.4280 0.0147  0.0072  0.0057  1227 ALA A CB  
8993  N N   . SER A 1230 ? 0.4333 0.3993 0.4644 0.0158  0.0076  0.0160  1228 SER A N   
8994  C CA  . SER A 1230 ? 0.4552 0.4214 0.4900 0.0166  0.0071  0.0205  1228 SER A CA  
8995  C C   . SER A 1230 ? 0.5302 0.4958 0.5683 0.0160  0.0074  0.0240  1228 SER A C   
8996  O O   . SER A 1230 ? 0.5304 0.4950 0.5752 0.0162  0.0064  0.0267  1228 SER A O   
8997  C CB  . SER A 1230 ? 0.5184 0.4872 0.5480 0.0174  0.0077  0.0227  1228 SER A CB  
8998  O OG  . SER A 1230 ? 0.6211 0.5904 0.6490 0.0179  0.0072  0.0199  1228 SER A OG  
8999  N N   . LEU A 1231 ? 0.4619 0.4282 0.4962 0.0154  0.0086  0.0240  1229 LEU A N   
9000  C CA  . LEU A 1231 ? 0.4961 0.4623 0.5334 0.0148  0.0089  0.0274  1229 LEU A CA  
9001  C C   . LEU A 1231 ? 0.5089 0.4724 0.5524 0.0139  0.0080  0.0255  1229 LEU A C   
9002  O O   . LEU A 1231 ? 0.4999 0.4631 0.5476 0.0133  0.0080  0.0284  1229 LEU A O   
9003  C CB  . LEU A 1231 ? 0.4661 0.4343 0.4975 0.0146  0.0105  0.0280  1229 LEU A CB  
9004  C CG  . LEU A 1231 ? 0.4431 0.4148 0.4696 0.0155  0.0114  0.0308  1229 LEU A CG  
9005  C CD1 . LEU A 1231 ? 0.3913 0.3648 0.4134 0.0154  0.0127  0.0308  1229 LEU A CD1 
9006  C CD2 . LEU A 1231 ? 0.5294 0.5031 0.5599 0.0159  0.0111  0.0361  1229 LEU A CD2 
9007  N N   . MET A 1232 ? 0.5126 0.4747 0.5570 0.0138  0.0073  0.0206  1230 MET A N   
9008  C CA  . MET A 1232 ? 0.5172 0.4772 0.5685 0.0132  0.0060  0.0183  1230 MET A CA  
9009  C C   . MET A 1232 ? 0.5058 0.4642 0.5655 0.0136  0.0045  0.0210  1230 MET A C   
9010  O O   . MET A 1232 ? 0.5339 0.4905 0.6006 0.0131  0.0034  0.0206  1230 MET A O   
9011  C CB  . MET A 1232 ? 0.5123 0.4723 0.5627 0.0132  0.0055  0.0124  1230 MET A CB  
9012  C CG  . MET A 1232 ? 0.4660 0.4274 0.5098 0.0125  0.0067  0.0098  1230 MET A CG  
9013  S SD  . MET A 1232 ? 0.5841 0.5469 0.6270 0.0125  0.0061  0.0035  1230 MET A SD  
9014  C CE  . MET A 1232 ? 0.5461 0.5077 0.5983 0.0125  0.0043  0.0005  1230 MET A CE  
9015  N N   . ALA A 1233 ? 0.5816 0.5407 0.6413 0.0146  0.0042  0.0237  1231 ALA A N   
9016  C CA  . ALA A 1233 ? 0.6165 0.5744 0.6843 0.0150  0.0027  0.0272  1231 ALA A CA  
9017  C C   . ALA A 1233 ? 0.6618 0.6210 0.7309 0.0146  0.0032  0.0341  1231 ALA A C   
9018  O O   . ALA A 1233 ? 0.6953 0.6537 0.7719 0.0146  0.0018  0.0380  1231 ALA A O   
9019  C CB  . ALA A 1233 ? 0.6114 0.5698 0.6790 0.0163  0.0019  0.0270  1231 ALA A CB  
9020  N N   . ILE A 1234 ? 0.6383 0.5999 0.7008 0.0141  0.0050  0.0356  1232 ILE A N   
9021  C CA  . ILE A 1234 ? 0.6325 0.5967 0.6954 0.0138  0.0058  0.0420  1232 ILE A CA  
9022  C C   . ILE A 1234 ? 0.6004 0.5636 0.6668 0.0125  0.0060  0.0426  1232 ILE A C   
9023  O O   . ILE A 1234 ? 0.5535 0.5170 0.6153 0.0121  0.0071  0.0397  1232 ILE A O   
9024  C CB  . ILE A 1234 ? 0.5732 0.5415 0.6269 0.0144  0.0076  0.0433  1232 ILE A CB  
9025  C CG1 . ILE A 1234 ? 0.5862 0.5557 0.6373 0.0157  0.0072  0.0431  1232 ILE A CG1 
9026  C CG2 . ILE A 1234 ? 0.4913 0.4634 0.5453 0.0141  0.0086  0.0494  1232 ILE A CG2 
9027  C CD1 . ILE A 1234 ? 0.5236 0.4982 0.5692 0.0165  0.0084  0.0469  1232 ILE A CD1 
9028  N N   . GLY A 1235 ? 0.5648 0.5269 0.6400 0.0119  0.0047  0.0466  1233 GLY A N   
9029  C CA  . GLY A 1235 ? 0.4987 0.4602 0.5783 0.0105  0.0047  0.0480  1233 GLY A CA  
9030  C C   . GLY A 1235 ? 0.4649 0.4286 0.5502 0.0100  0.0044  0.0558  1233 GLY A C   
9031  O O   . GLY A 1235 ? 0.5201 0.4837 0.6099 0.0104  0.0032  0.0593  1233 GLY A O   
9032  O OXT . GLY A 1235 ? 0.3166 0.2825 0.4022 0.0090  0.0054  0.0591  1233 GLY A OXT 
9033  N N   . ALA B 16   ? 0.5925 0.4892 0.5560 0.0613  -0.0335 -0.0332 14   ALA B N   
9034  C CA  . ALA B 16   ? 0.5957 0.4982 0.5623 0.0551  -0.0323 -0.0319 14   ALA B CA  
9035  C C   . ALA B 16   ? 0.5676 0.4615 0.5267 0.0499  -0.0335 -0.0315 14   ALA B C   
9036  O O   . ALA B 16   ? 0.6440 0.5305 0.5971 0.0505  -0.0338 -0.0330 14   ALA B O   
9037  C CB  . ALA B 16   ? 0.5236 0.4366 0.4966 0.0553  -0.0287 -0.0327 14   ALA B CB  
9038  N N   . PRO B 17   ? 0.5429 0.4378 0.5024 0.0446  -0.0343 -0.0296 15   PRO B N   
9039  C CA  . PRO B 17   ? 0.5287 0.4167 0.4817 0.0391  -0.0354 -0.0290 15   PRO B CA  
9040  C C   . PRO B 17   ? 0.4779 0.3690 0.4313 0.0370  -0.0331 -0.0301 15   PRO B C   
9041  O O   . PRO B 17   ? 0.4750 0.3760 0.4350 0.0374  -0.0305 -0.0305 15   PRO B O   
9042  C CB  . PRO B 17   ? 0.5333 0.4250 0.4886 0.0345  -0.0359 -0.0267 15   PRO B CB  
9043  C CG  . PRO B 17   ? 0.5773 0.4803 0.5415 0.0367  -0.0341 -0.0265 15   PRO B CG  
9044  C CD  . PRO B 17   ? 0.5276 0.4305 0.4934 0.0433  -0.0341 -0.0279 15   PRO B CD  
9045  N N   . ALA B 18   ? 0.4929 0.3751 0.4389 0.0347  -0.0344 -0.0307 16   ALA B N   
9046  C CA  . ALA B 18   ? 0.4173 0.3015 0.3628 0.0324  -0.0327 -0.0318 16   ALA B CA  
9047  C C   . ALA B 18   ? 0.3783 0.2714 0.3288 0.0273  -0.0311 -0.0303 16   ALA B C   
9048  O O   . ALA B 18   ? 0.3832 0.2759 0.3333 0.0235  -0.0323 -0.0284 16   ALA B O   
9049  C CB  . ALA B 18   ? 0.4675 0.3401 0.4038 0.0300  -0.0348 -0.0324 16   ALA B CB  
9050  N N   . PRO B 19   ? 0.3722 0.2733 0.3271 0.0272  -0.0285 -0.0310 17   PRO B N   
9051  C CA  . PRO B 19   ? 0.3471 0.2568 0.3070 0.0229  -0.0271 -0.0297 17   PRO B CA  
9052  C C   . PRO B 19   ? 0.3198 0.2251 0.2750 0.0170  -0.0285 -0.0285 17   PRO B C   
9053  O O   . PRO B 19   ? 0.3511 0.2497 0.3004 0.0154  -0.0296 -0.0293 17   PRO B O   
9054  C CB  . PRO B 19   ? 0.3359 0.2520 0.2992 0.0242  -0.0244 -0.0310 17   PRO B CB  
9055  C CG  . PRO B 19   ? 0.3698 0.2845 0.3332 0.0302  -0.0239 -0.0326 17   PRO B CG  
9056  C CD  . PRO B 19   ? 0.3704 0.2736 0.3265 0.0316  -0.0267 -0.0331 17   PRO B CD  
9057  N N   . PHE B 20   ? 0.3348 0.2442 0.2926 0.0136  -0.0286 -0.0266 18   PHE B N   
9058  C CA  . PHE B 20   ? 0.3192 0.2271 0.2741 0.0078  -0.0296 -0.0251 18   PHE B CA  
9059  C C   . PHE B 20   ? 0.3818 0.2783 0.3288 0.0059  -0.0325 -0.0245 18   PHE B C   
9060  O O   . PHE B 20   ? 0.3798 0.2740 0.3234 0.0008  -0.0334 -0.0234 18   PHE B O   
9061  C CB  . PHE B 20   ? 0.3101 0.2220 0.2657 0.0049  -0.0282 -0.0256 18   PHE B CB  
9062  C CG  . PHE B 20   ? 0.2789 0.2016 0.2419 0.0062  -0.0254 -0.0259 18   PHE B CG  
9063  C CD1 . PHE B 20   ? 0.2774 0.2077 0.2453 0.0042  -0.0244 -0.0244 18   PHE B CD1 
9064  C CD2 . PHE B 20   ? 0.2886 0.2137 0.2532 0.0095  -0.0238 -0.0276 18   PHE B CD2 
9065  C CE1 . PHE B 20   ? 0.2779 0.2173 0.2522 0.0054  -0.0220 -0.0247 18   PHE B CE1 
9066  C CE2 . PHE B 20   ? 0.2825 0.2171 0.2536 0.0104  -0.0213 -0.0277 18   PHE B CE2 
9067  C CZ  . PHE B 20   ? 0.2843 0.2258 0.2601 0.0084  -0.0205 -0.0262 18   PHE B CZ  
9068  N N   . ALA B 21   ? 0.4132 0.3026 0.3571 0.0099  -0.0340 -0.0252 19   ALA B N   
9069  C CA  . ALA B 21   ? 0.4309 0.3083 0.3666 0.0084  -0.0370 -0.0247 19   ALA B CA  
9070  C C   . ALA B 21   ? 0.4343 0.3109 0.3689 0.0043  -0.0384 -0.0222 19   ALA B C   
9071  O O   . ALA B 21   ? 0.4956 0.3633 0.4234 0.0009  -0.0406 -0.0212 19   ALA B O   
9072  C CB  . ALA B 21   ? 0.4575 0.3280 0.3906 0.0144  -0.0383 -0.0260 19   ALA B CB  
9073  N N   . ASP B 22   ? 0.3703 0.2555 0.3109 0.0042  -0.0370 -0.0210 20   ASP B N   
9074  C CA  . ASP B 22   ? 0.4037 0.2891 0.3435 0.0004  -0.0379 -0.0186 20   ASP B CA  
9075  C C   . ASP B 22   ? 0.3402 0.2368 0.2861 -0.0024 -0.0356 -0.0178 20   ASP B C   
9076  O O   . ASP B 22   ? 0.3847 0.2859 0.3335 -0.0029 -0.0353 -0.0165 20   ASP B O   
9077  C CB  . ASP B 22   ? 0.4457 0.3286 0.3855 0.0039  -0.0393 -0.0180 20   ASP B CB  
9078  N N   . PHE B 23   ? 0.2969 0.1980 0.2446 -0.0043 -0.0340 -0.0186 21   PHE B N   
9079  C CA  . PHE B 23   ? 0.2910 0.2030 0.2449 -0.0060 -0.0316 -0.0181 21   PHE B CA  
9080  C C   . PHE B 23   ? 0.2864 0.2005 0.2396 -0.0107 -0.0319 -0.0159 21   PHE B C   
9081  O O   . PHE B 23   ? 0.2846 0.2052 0.2421 -0.0103 -0.0308 -0.0151 21   PHE B O   
9082  C CB  . PHE B 23   ? 0.2702 0.1858 0.2253 -0.0073 -0.0302 -0.0193 21   PHE B CB  
9083  C CG  . PHE B 23   ? 0.2854 0.2116 0.2463 -0.0091 -0.0280 -0.0187 21   PHE B CG  
9084  C CD1 . PHE B 23   ? 0.2716 0.2051 0.2388 -0.0059 -0.0262 -0.0191 21   PHE B CD1 
9085  C CD2 . PHE B 23   ? 0.2723 0.2011 0.2325 -0.0140 -0.0277 -0.0177 21   PHE B CD2 
9086  C CE1 . PHE B 23   ? 0.2708 0.2134 0.2430 -0.0074 -0.0242 -0.0186 21   PHE B CE1 
9087  C CE2 . PHE B 23   ? 0.2861 0.2247 0.2516 -0.0152 -0.0257 -0.0172 21   PHE B CE2 
9088  C CZ  . PHE B 23   ? 0.2761 0.2211 0.2473 -0.0119 -0.0240 -0.0177 21   PHE B CZ  
9089  N N   . ALA B 24   ? 0.2951 0.2042 0.2431 -0.0153 -0.0332 -0.0148 22   ALA B N   
9090  C CA  . ALA B 24   ? 0.2877 0.1992 0.2349 -0.0200 -0.0333 -0.0125 22   ALA B CA  
9091  C C   . ALA B 24   ? 0.2878 0.1901 0.2275 -0.0243 -0.0357 -0.0112 22   ALA B C   
9092  O O   . ALA B 24   ? 0.3091 0.2136 0.2479 -0.0292 -0.0355 -0.0102 22   ALA B O   
9093  C CB  . ALA B 24   ? 0.3359 0.2577 0.2880 -0.0225 -0.0310 -0.0123 22   ALA B CB  
9094  N N   . PRO B 25   ? 0.3239 0.2161 0.2582 -0.0228 -0.0380 -0.0110 23   PRO B N   
9095  C CA  . PRO B 25   ? 0.3724 0.2550 0.2991 -0.0271 -0.0405 -0.0097 23   PRO B CA  
9096  C C   . PRO B 25   ? 0.3404 0.2261 0.2664 -0.0324 -0.0404 -0.0069 23   PRO B C   
9097  O O   . PRO B 25   ? 0.3360 0.2266 0.2649 -0.0314 -0.0395 -0.0059 23   PRO B O   
9098  C CB  . PRO B 25   ? 0.4130 0.2851 0.3350 -0.0233 -0.0428 -0.0100 23   PRO B CB  
9099  C CG  . PRO B 25   ? 0.3796 0.2576 0.3070 -0.0185 -0.0416 -0.0105 23   PRO B CG  
9100  C CD  . PRO B 25   ? 0.3217 0.2110 0.2567 -0.0173 -0.0387 -0.0118 23   PRO B CD  
9101  N N   . PRO B 26   ? 0.3523 0.2361 0.2748 -0.0382 -0.0411 -0.0056 24   PRO B N   
9102  C CA  . PRO B 26   ? 0.3647 0.2521 0.2866 -0.0434 -0.0408 -0.0028 24   PRO B CA  
9103  C C   . PRO B 26   ? 0.3753 0.2544 0.2917 -0.0436 -0.0428 -0.0010 24   PRO B C   
9104  O O   . PRO B 26   ? 0.3813 0.2499 0.2928 -0.0411 -0.0451 -0.0016 24   PRO B O   
9105  C CB  . PRO B 26   ? 0.3804 0.2662 0.2992 -0.0493 -0.0416 -0.0020 24   PRO B CB  
9106  C CG  . PRO B 26   ? 0.4053 0.2811 0.3197 -0.0474 -0.0436 -0.0039 24   PRO B CG  
9107  C CD  . PRO B 26   ? 0.3939 0.2720 0.3126 -0.0403 -0.0424 -0.0066 24   PRO B CD  
9108  N N   . VAL B 27   ? 0.3640 0.2482 0.2811 -0.0466 -0.0419 0.0013  25   VAL B N   
9109  C CA  . VAL B 27   ? 0.3693 0.2462 0.2809 -0.0474 -0.0438 0.0034  25   VAL B CA  
9110  C C   . VAL B 27   ? 0.3753 0.2399 0.2786 -0.0512 -0.0468 0.0047  25   VAL B C   
9111  O O   . VAL B 27   ? 0.4307 0.2848 0.3284 -0.0496 -0.0492 0.0052  25   VAL B O   
9112  C CB  . VAL B 27   ? 0.3755 0.2605 0.2889 -0.0506 -0.0421 0.0057  25   VAL B CB  
9113  C CG1 . VAL B 27   ? 0.4012 0.2780 0.3078 -0.0527 -0.0442 0.0083  25   VAL B CG1 
9114  C CG2 . VAL B 27   ? 0.3627 0.2577 0.2833 -0.0461 -0.0397 0.0044  25   VAL B CG2 
9115  N N   . ARG B 28   ? 0.3753 0.2407 0.2776 -0.0563 -0.0468 0.0051  26   ARG B N   
9116  C CA  . ARG B 28   ? 0.3694 0.2229 0.2635 -0.0605 -0.0497 0.0063  26   ARG B CA  
9117  C C   . ARG B 28   ? 0.4363 0.2912 0.3313 -0.0631 -0.0497 0.0050  26   ARG B C   
9118  O O   . ARG B 28   ? 0.3841 0.2503 0.2858 -0.0630 -0.0471 0.0040  26   ARG B O   
9119  C CB  . ARG B 28   ? 0.4413 0.2940 0.3315 -0.0669 -0.0503 0.0100  26   ARG B CB  
9120  C CG  . ARG B 28   ? 0.4395 0.3044 0.3343 -0.0722 -0.0478 0.0114  26   ARG B CG  
9121  C CD  . ARG B 28   ? 0.4470 0.3126 0.3385 -0.0780 -0.0479 0.0151  26   ARG B CD  
9122  N NE  . ARG B 28   ? 0.4555 0.3246 0.3485 -0.0749 -0.0467 0.0158  26   ARG B NE  
9123  C CZ  . ARG B 28   ? 0.5100 0.3700 0.3974 -0.0737 -0.0486 0.0171  26   ARG B CZ  
9124  N NH1 . ARG B 28   ? 0.4979 0.3440 0.3774 -0.0752 -0.0519 0.0179  26   ARG B NH1 
9125  N NH2 . ARG B 28   ? 0.4945 0.3589 0.3838 -0.0708 -0.0474 0.0177  26   ARG B NH2 
9126  N N   . PRO B 29   ? 0.4118 0.2549 0.2998 -0.0653 -0.0525 0.0049  27   PRO B N   
9127  C CA  . PRO B 29   ? 0.4183 0.2625 0.3063 -0.0689 -0.0528 0.0040  27   PRO B CA  
9128  C C   . PRO B 29   ? 0.4274 0.2819 0.3186 -0.0756 -0.0513 0.0064  27   PRO B C   
9129  O O   . PRO B 29   ? 0.4204 0.2746 0.3091 -0.0799 -0.0515 0.0094  27   PRO B O   
9130  C CB  . PRO B 29   ? 0.4559 0.2840 0.3344 -0.0710 -0.0566 0.0042  27   PRO B CB  
9131  C CG  . PRO B 29   ? 0.5256 0.3447 0.4006 -0.0653 -0.0579 0.0036  27   PRO B CG  
9132  C CD  . PRO B 29   ? 0.4737 0.3016 0.3533 -0.0642 -0.0558 0.0053  27   PRO B CD  
9133  N N   . GLN B 30   ? 0.4112 0.2751 0.3079 -0.0762 -0.0495 0.0051  28   GLN B N   
9134  C CA  . GLN B 30   ? 0.4205 0.2963 0.3216 -0.0817 -0.0477 0.0071  28   GLN B CA  
9135  C C   . GLN B 30   ? 0.4148 0.2853 0.3106 -0.0893 -0.0501 0.0089  28   GLN B C   
9136  O O   . GLN B 30   ? 0.4273 0.2926 0.3206 -0.0902 -0.0518 0.0073  28   GLN B O   
9137  C CB  . GLN B 30   ? 0.3840 0.2718 0.2931 -0.0790 -0.0451 0.0049  28   GLN B CB  
9138  C CG  . GLN B 30   ? 0.3787 0.2713 0.2930 -0.0716 -0.0429 0.0030  28   GLN B CG  
9139  C CD  . GLN B 30   ? 0.3804 0.2803 0.2977 -0.0715 -0.0409 0.0049  28   GLN B CD  
9140  O OE1 . GLN B 30   ? 0.3717 0.2832 0.2942 -0.0736 -0.0387 0.0059  28   GLN B OE1 
9141  N NE2 . GLN B 30   ? 0.3583 0.2513 0.2723 -0.0690 -0.0419 0.0055  28   GLN B NE2 
9142  N N   . SER B 31   ? 0.4013 0.2732 0.2952 -0.0949 -0.0501 0.0123  29   SER B N   
9143  C CA  . SER B 31   ? 0.4157 0.2836 0.3049 -0.1029 -0.0523 0.0146  29   SER B CA  
9144  C C   . SER B 31   ? 0.4106 0.2906 0.3057 -0.1065 -0.0509 0.0144  29   SER B C   
9145  O O   . SER B 31   ? 0.3940 0.2860 0.2967 -0.1030 -0.0480 0.0130  29   SER B O   
9146  C CB  . SER B 31   ? 0.4287 0.2971 0.3153 -0.1078 -0.0521 0.0184  29   SER B CB  
9147  O OG  . SER B 31   ? 0.3991 0.2832 0.2931 -0.1084 -0.0486 0.0196  29   SER B OG  
9148  N N   . THR B 32   ? 0.4312 0.3076 0.3224 -0.1137 -0.0531 0.0160  30   THR B N   
9149  C CA  . THR B 32   ? 0.4124 0.3005 0.3089 -0.1179 -0.0521 0.0164  30   THR B CA  
9150  C C   . THR B 32   ? 0.3832 0.2877 0.2874 -0.1185 -0.0484 0.0181  30   THR B C   
9151  O O   . THR B 32   ? 0.3983 0.3150 0.3099 -0.1165 -0.0462 0.0168  30   THR B O   
9152  C CB  . THR B 32   ? 0.4532 0.3348 0.3439 -0.1265 -0.0553 0.0185  30   THR B CB  
9153  O OG1 . THR B 32   ? 0.4951 0.3612 0.3785 -0.1253 -0.0587 0.0164  30   THR B OG1 
9154  C CG2 . THR B 32   ? 0.5074 0.4018 0.4039 -0.1312 -0.0544 0.0191  30   THR B CG2 
9155  N N   . LEU B 33   ? 0.3960 0.3009 0.2985 -0.1208 -0.0477 0.0210  31   LEU B N   
9156  C CA  . LEU B 33   ? 0.3922 0.3124 0.3014 -0.1212 -0.0441 0.0226  31   LEU B CA  
9157  C C   . LEU B 33   ? 0.3481 0.2750 0.2633 -0.1131 -0.0413 0.0201  31   LEU B C   
9158  O O   . LEU B 33   ? 0.3410 0.2819 0.2635 -0.1120 -0.0384 0.0198  31   LEU B O   
9159  C CB  . LEU B 33   ? 0.3740 0.2919 0.2790 -0.1254 -0.0441 0.0263  31   LEU B CB  
9160  C CG  . LEU B 33   ? 0.4023 0.3171 0.3029 -0.1346 -0.0463 0.0293  31   LEU B CG  
9161  C CD1 . LEU B 33   ? 0.4332 0.3427 0.3280 -0.1386 -0.0468 0.0329  31   LEU B CD1 
9162  C CD2 . LEU B 33   ? 0.4342 0.3645 0.3417 -0.1390 -0.0445 0.0304  31   LEU B CD2 
9163  N N   . ARG B 34   ? 0.3342 0.2517 0.2465 -0.1072 -0.0421 0.0182  32   ARG B N   
9164  C CA  . ARG B 34   ? 0.3371 0.2607 0.2550 -0.0997 -0.0396 0.0158  32   ARG B CA  
9165  C C   . ARG B 34   ? 0.3299 0.2593 0.2531 -0.0970 -0.0388 0.0130  32   ARG B C   
9166  O O   . ARG B 34   ? 0.3209 0.2616 0.2510 -0.0936 -0.0361 0.0119  32   ARG B O   
9167  C CB  . ARG B 34   ? 0.3252 0.2372 0.2389 -0.0943 -0.0409 0.0145  32   ARG B CB  
9168  C CG  . ARG B 34   ? 0.3597 0.2676 0.2693 -0.0953 -0.0411 0.0169  32   ARG B CG  
9169  C CD  . ARG B 34   ? 0.3444 0.2643 0.2596 -0.0930 -0.0378 0.0175  32   ARG B CD  
9170  N NE  . ARG B 34   ? 0.3393 0.2619 0.2590 -0.0855 -0.0364 0.0146  32   ARG B NE  
9171  C CZ  . ARG B 34   ? 0.3557 0.2720 0.2735 -0.0807 -0.0370 0.0138  32   ARG B CZ  
9172  N NH1 . ARG B 34   ? 0.3659 0.2725 0.2770 -0.0822 -0.0390 0.0156  32   ARG B NH1 
9173  N NH2 . ARG B 34   ? 0.3534 0.2733 0.2760 -0.0743 -0.0357 0.0112  32   ARG B NH2 
9174  N N   . ARG B 35   ? 0.3475 0.2692 0.2672 -0.0986 -0.0414 0.0118  33   ARG B N   
9175  C CA  . ARG B 35   ? 0.3560 0.2828 0.2800 -0.0964 -0.0409 0.0093  33   ARG B CA  
9176  C C   . ARG B 35   ? 0.3203 0.2615 0.2505 -0.1001 -0.0390 0.0105  33   ARG B C   
9177  O O   . ARG B 35   ? 0.3204 0.2706 0.2567 -0.0967 -0.0371 0.0088  33   ARG B O   
9178  C CB  . ARG B 35   ? 0.3808 0.2959 0.2988 -0.0981 -0.0442 0.0080  33   ARG B CB  
9179  C CG  . ARG B 35   ? 0.4170 0.3196 0.3304 -0.0925 -0.0456 0.0059  33   ARG B CG  
9180  C CD  . ARG B 35   ? 0.4583 0.3484 0.3649 -0.0939 -0.0489 0.0045  33   ARG B CD  
9181  N NE  . ARG B 35   ? 0.5438 0.4222 0.4460 -0.0882 -0.0501 0.0026  33   ARG B NE  
9182  C CZ  . ARG B 35   ? 0.6304 0.5097 0.5355 -0.0813 -0.0489 -0.0003 33   ARG B CZ  
9183  N NH1 . ARG B 35   ? 0.6634 0.5536 0.5752 -0.0792 -0.0466 -0.0017 33   ARG B NH1 
9184  N NH2 . ARG B 35   ? 0.5884 0.4576 0.4895 -0.0762 -0.0499 -0.0017 33   ARG B NH2 
9185  N N   . ALA B 36   ? 0.3215 0.2653 0.2502 -0.1070 -0.0395 0.0136  34   ALA B N   
9186  C CA  . ALA B 36   ? 0.3665 0.3249 0.3015 -0.1104 -0.0377 0.0149  34   ALA B CA  
9187  C C   . ALA B 36   ? 0.3506 0.3211 0.2922 -0.1062 -0.0339 0.0149  34   ALA B C   
9188  O O   . ALA B 36   ? 0.3236 0.3061 0.2717 -0.1053 -0.0320 0.0143  34   ALA B O   
9189  C CB  . ALA B 36   ? 0.3465 0.3053 0.2784 -0.1190 -0.0390 0.0185  34   ALA B CB  
9190  N N   . ILE B 37   ? 0.3088 0.2759 0.2486 -0.1035 -0.0330 0.0154  35   ILE B N   
9191  C CA  . ILE B 37   ? 0.2906 0.2676 0.2360 -0.0988 -0.0297 0.0149  35   ILE B CA  
9192  C C   . ILE B 37   ? 0.3120 0.2915 0.2619 -0.0922 -0.0287 0.0116  35   ILE B C   
9193  O O   . ILE B 37   ? 0.2710 0.2621 0.2273 -0.0904 -0.0264 0.0110  35   ILE B O   
9194  C CB  . ILE B 37   ? 0.2871 0.2582 0.2288 -0.0970 -0.0294 0.0159  35   ILE B CB  
9195  C CG1 . ILE B 37   ? 0.2842 0.2550 0.2220 -0.1036 -0.0299 0.0195  35   ILE B CG1 
9196  C CG2 . ILE B 37   ? 0.2891 0.2687 0.2360 -0.0913 -0.0264 0.0148  35   ILE B CG2 
9197  C CD1 . ILE B 37   ? 0.3217 0.2826 0.2535 -0.1026 -0.0308 0.0206  35   ILE B CD1 
9198  N N   . THR B 38   ? 0.2835 0.2522 0.2301 -0.0885 -0.0304 0.0095  36   THR B N   
9199  C CA  . THR B 38   ? 0.2995 0.2700 0.2501 -0.0822 -0.0294 0.0065  36   THR B CA  
9200  C C   . THR B 38   ? 0.2873 0.2651 0.2419 -0.0832 -0.0291 0.0056  36   THR B C   
9201  O O   . THR B 38   ? 0.2825 0.2684 0.2428 -0.0792 -0.0271 0.0041  36   THR B O   
9202  C CB  . THR B 38   ? 0.2821 0.2393 0.2277 -0.0788 -0.0315 0.0046  36   THR B CB  
9203  O OG1 . THR B 38   ? 0.2971 0.2473 0.2386 -0.0784 -0.0321 0.0058  36   THR B OG1 
9204  C CG2 . THR B 38   ? 0.3243 0.2836 0.2741 -0.0721 -0.0302 0.0017  36   THR B CG2 
9205  N N   . ALA B 39   ? 0.2896 0.2648 0.2413 -0.0888 -0.0312 0.0065  37   ALA B N   
9206  C CA  . ALA B 39   ? 0.3144 0.2961 0.2695 -0.0900 -0.0314 0.0057  37   ALA B CA  
9207  C C   . ALA B 39   ? 0.3240 0.3213 0.2864 -0.0904 -0.0286 0.0067  37   ALA B C   
9208  O O   . ALA B 39   ? 0.3111 0.3155 0.2780 -0.0888 -0.0279 0.0054  37   ALA B O   
9209  C CB  . ALA B 39   ? 0.3151 0.2912 0.2655 -0.0967 -0.0344 0.0068  37   ALA B CB  
9210  N N   . ALA B 40   ? 0.2704 0.2729 0.2337 -0.0923 -0.0271 0.0089  38   ALA B N   
9211  C CA  . ALA B 40   ? 0.2853 0.3024 0.2550 -0.0927 -0.0245 0.0100  38   ALA B CA  
9212  C C   . ALA B 40   ? 0.2436 0.2662 0.2177 -0.0860 -0.0216 0.0085  38   ALA B C   
9213  O O   . ALA B 40   ? 0.2669 0.3015 0.2463 -0.0853 -0.0193 0.0090  38   ALA B O   
9214  C CB  . ALA B 40   ? 0.2880 0.3087 0.2563 -0.0984 -0.0240 0.0133  38   ALA B CB  
9215  N N   . TYR B 41   ? 0.2447 0.2589 0.2167 -0.0812 -0.0219 0.0067  39   TYR B N   
9216  C CA  . TYR B 41   ? 0.2578 0.2757 0.2330 -0.0755 -0.0195 0.0056  39   TYR B CA  
9217  C C   . TYR B 41   ? 0.2319 0.2618 0.2138 -0.0728 -0.0173 0.0047  39   TYR B C   
9218  O O   . TYR B 41   ? 0.2395 0.2776 0.2247 -0.0713 -0.0149 0.0053  39   TYR B O   
9219  C CB  . TYR B 41   ? 0.2398 0.2473 0.2124 -0.0707 -0.0205 0.0034  39   TYR B CB  
9220  C CG  . TYR B 41   ? 0.2453 0.2522 0.2188 -0.0659 -0.0191 0.0027  39   TYR B CG  
9221  C CD1 . TYR B 41   ? 0.2381 0.2546 0.2160 -0.0639 -0.0165 0.0029  39   TYR B CD1 
9222  C CD2 . TYR B 41   ? 0.2721 0.2685 0.2420 -0.0631 -0.0204 0.0016  39   TYR B CD2 
9223  C CE1 . TYR B 41   ? 0.2386 0.2538 0.2169 -0.0595 -0.0154 0.0022  39   TYR B CE1 
9224  C CE2 . TYR B 41   ? 0.2569 0.2526 0.2276 -0.0587 -0.0193 0.0009  39   TYR B CE2 
9225  C CZ  . TYR B 41   ? 0.2292 0.2342 0.2041 -0.0571 -0.0169 0.0012  39   TYR B CZ  
9226  O OH  . TYR B 41   ? 0.2467 0.2507 0.2221 -0.0530 -0.0161 0.0005  39   TYR B OH  
9227  N N   . ARG B 42   ? 0.2432 0.2741 0.2270 -0.0719 -0.0180 0.0033  40   ARG B N   
9228  C CA  . ARG B 42   ? 0.2328 0.2741 0.2227 -0.0690 -0.0162 0.0023  40   ARG B CA  
9229  C C   . ARG B 42   ? 0.2452 0.2924 0.2369 -0.0729 -0.0171 0.0030  40   ARG B C   
9230  O O   . ARG B 42   ? 0.2574 0.3090 0.2525 -0.0705 -0.0169 0.0017  40   ARG B O   
9231  C CB  . ARG B 42   ? 0.2509 0.2889 0.2422 -0.0629 -0.0157 -0.0003 40   ARG B CB  
9232  C CG  . ARG B 42   ? 0.2600 0.2940 0.2502 -0.0592 -0.0147 -0.0007 40   ARG B CG  
9233  C CD  . ARG B 42   ? 0.2404 0.2709 0.2319 -0.0535 -0.0143 -0.0030 40   ARG B CD  
9234  N NE  . ARG B 42   ? 0.2384 0.2629 0.2276 -0.0513 -0.0142 -0.0032 40   ARG B NE  
9235  C CZ  . ARG B 42   ? 0.2429 0.2715 0.2342 -0.0487 -0.0124 -0.0031 40   ARG B CZ  
9236  N NH1 . ARG B 42   ? 0.2351 0.2734 0.2308 -0.0474 -0.0104 -0.0031 40   ARG B NH1 
9237  N NH2 . ARG B 42   ? 0.2310 0.2534 0.2196 -0.0473 -0.0127 -0.0031 40   ARG B NH2 
9238  N N   . ARG B 43   ? 0.2412 0.2886 0.2307 -0.0790 -0.0183 0.0052  41   ARG B N   
9239  C CA  . ARG B 43   ? 0.2419 0.2946 0.2328 -0.0835 -0.0197 0.0060  41   ARG B CA  
9240  C C   . ARG B 43   ? 0.2812 0.3481 0.2789 -0.0818 -0.0175 0.0062  41   ARG B C   
9241  O O   . ARG B 43   ? 0.2458 0.3197 0.2463 -0.0800 -0.0150 0.0069  41   ARG B O   
9242  C CB  . ARG B 43   ? 0.2465 0.2979 0.2341 -0.0906 -0.0210 0.0087  41   ARG B CB  
9243  C CG  . ARG B 43   ? 0.2448 0.3023 0.2339 -0.0962 -0.0225 0.0100  41   ARG B CG  
9244  C CD  . ARG B 43   ? 0.3048 0.3567 0.2888 -0.1033 -0.0245 0.0124  41   ARG B CD  
9245  N NE  . ARG B 43   ? 0.3061 0.3424 0.2833 -0.1035 -0.0272 0.0112  41   ARG B NE  
9246  C CZ  . ARG B 43   ? 0.3445 0.3715 0.3157 -0.1073 -0.0287 0.0127  41   ARG B CZ  
9247  N NH1 . ARG B 43   ? 0.3020 0.3333 0.2730 -0.1115 -0.0278 0.0156  41   ARG B NH1 
9248  N NH2 . ARG B 43   ? 0.3289 0.3417 0.2939 -0.1065 -0.0311 0.0113  41   ARG B NH2 
9249  N N   . PRO B 44   ? 0.2555 0.3269 0.2559 -0.0820 -0.0183 0.0054  42   PRO B N   
9250  C CA  . PRO B 44   ? 0.2500 0.3351 0.2570 -0.0802 -0.0165 0.0057  42   PRO B CA  
9251  C C   . PRO B 44   ? 0.2444 0.3395 0.2538 -0.0840 -0.0151 0.0083  42   PRO B C   
9252  O O   . PRO B 44   ? 0.2379 0.3314 0.2446 -0.0901 -0.0165 0.0103  42   PRO B O   
9253  C CB  . PRO B 44   ? 0.2757 0.3622 0.2836 -0.0817 -0.0185 0.0050  42   PRO B CB  
9254  C CG  . PRO B 44   ? 0.3077 0.3804 0.3103 -0.0802 -0.0204 0.0030  42   PRO B CG  
9255  C CD  . PRO B 44   ? 0.2933 0.3569 0.2907 -0.0827 -0.0210 0.0040  42   PRO B CD  
9256  N N   . GLU B 45   ? 0.2448 0.3500 0.2590 -0.0803 -0.0123 0.0083  43   GLU B N   
9257  C CA  . GLU B 45   ? 0.2278 0.3435 0.2447 -0.0829 -0.0104 0.0106  43   GLU B CA  
9258  C C   . GLU B 45   ? 0.2640 0.3878 0.2831 -0.0890 -0.0118 0.0126  43   GLU B C   
9259  O O   . GLU B 45   ? 0.2733 0.4009 0.2919 -0.0942 -0.0115 0.0151  43   GLU B O   
9260  C CB  . GLU B 45   ? 0.2920 0.4168 0.3137 -0.0769 -0.0074 0.0098  43   GLU B CB  
9261  C CG  . GLU B 45   ? 0.3059 0.4379 0.3286 -0.0776 -0.0049 0.0115  43   GLU B CG  
9262  C CD  . GLU B 45   ? 0.2178 0.3515 0.2419 -0.0709 -0.0023 0.0100  43   GLU B CD  
9263  O OE1 . GLU B 45   ? 0.2263 0.3549 0.2505 -0.0658 -0.0025 0.0076  43   GLU B OE1 
9264  O OE2 . GLU B 45   ? 0.2346 0.3747 0.2595 -0.0709 0.0000  0.0112  43   GLU B OE2 
9265  N N   . THR B 46   ? 0.2741 0.4002 0.2955 -0.0887 -0.0133 0.0116  44   THR B N   
9266  C CA  . THR B 46   ? 0.2592 0.3930 0.2828 -0.0945 -0.0149 0.0134  44   THR B CA  
9267  C C   . THR B 46   ? 0.2654 0.3901 0.2835 -0.1016 -0.0178 0.0147  44   THR B C   
9268  O O   . THR B 46   ? 0.2983 0.4294 0.3177 -0.1078 -0.0189 0.0169  44   THR B O   
9269  C CB  . THR B 46   ? 0.2827 0.4201 0.3095 -0.0923 -0.0162 0.0119  44   THR B CB  
9270  O OG1 . THR B 46   ? 0.2947 0.4190 0.3170 -0.0898 -0.0179 0.0095  44   THR B OG1 
9271  C CG2 . THR B 46   ? 0.2828 0.4313 0.3156 -0.0862 -0.0135 0.0111  44   THR B CG2 
9272  N N   . GLU B 47   ? 0.2650 0.3750 0.2769 -0.1008 -0.0192 0.0134  45   GLU B N   
9273  C CA  . GLU B 47   ? 0.2885 0.3885 0.2943 -0.1071 -0.0219 0.0147  45   GLU B CA  
9274  C C   . GLU B 47   ? 0.2583 0.3573 0.2618 -0.1100 -0.0206 0.0169  45   GLU B C   
9275  O O   . GLU B 47   ? 0.3184 0.4145 0.3186 -0.1168 -0.0224 0.0191  45   GLU B O   
9276  C CB  . GLU B 47   ? 0.2906 0.3751 0.2906 -0.1048 -0.0240 0.0123  45   GLU B CB  
9277  C CG  . GLU B 47   ? 0.3568 0.4409 0.3580 -0.1027 -0.0256 0.0101  45   GLU B CG  
9278  C CD  . GLU B 47   ? 0.4191 0.4886 0.4148 -0.0995 -0.0271 0.0076  45   GLU B CD  
9279  O OE1 . GLU B 47   ? 0.4845 0.5429 0.4744 -0.1012 -0.0282 0.0079  45   GLU B OE1 
9280  O OE2 . GLU B 47   ? 0.4886 0.5579 0.4856 -0.0951 -0.0272 0.0055  45   GLU B OE2 
9281  N N   . CYS B 48   ? 0.2365 0.3376 0.2413 -0.1050 -0.0177 0.0165  46   CYS B N   
9282  C CA  . CYS B 48   ? 0.2585 0.3582 0.2605 -0.1073 -0.0164 0.0186  46   CYS B CA  
9283  C C   . CYS B 48   ? 0.2582 0.3715 0.2640 -0.1121 -0.0149 0.0216  46   CYS B C   
9284  O O   . CYS B 48   ? 0.2664 0.3779 0.2690 -0.1177 -0.0153 0.0241  46   CYS B O   
9285  C CB  . CYS B 48   ? 0.2537 0.3523 0.2560 -0.1006 -0.0137 0.0172  46   CYS B CB  
9286  S SG  . CYS B 48   ? 0.2572 0.3397 0.2546 -0.0954 -0.0152 0.0142  46   CYS B SG  
9287  N N   . LEU B 49   ? 0.2559 0.3830 0.2686 -0.1099 -0.0132 0.0214  47   LEU B N   
9288  C CA  . LEU B 49   ? 0.2380 0.3794 0.2549 -0.1129 -0.0109 0.0241  47   LEU B CA  
9289  C C   . LEU B 49   ? 0.2778 0.4231 0.2946 -0.1217 -0.0128 0.0270  47   LEU B C   
9290  O O   . LEU B 49   ? 0.2738 0.4241 0.2903 -0.1260 -0.0115 0.0298  47   LEU B O   
9291  C CB  . LEU B 49   ? 0.2617 0.4168 0.2858 -0.1073 -0.0083 0.0230  47   LEU B CB  
9292  C CG  . LEU B 49   ? 0.2463 0.4039 0.2711 -0.1015 -0.0048 0.0223  47   LEU B CG  
9293  C CD1 . LEU B 49   ? 0.2716 0.4340 0.2951 -0.1057 -0.0029 0.0252  47   LEU B CD1 
9294  C CD2 . LEU B 49   ? 0.2447 0.3877 0.2645 -0.0968 -0.0054 0.0199  47   LEU B CD2 
9295  N N   . PRO B 50   ? 0.2907 0.4346 0.3079 -0.1248 -0.0159 0.0266  48   PRO B N   
9296  C CA  . PRO B 50   ? 0.2715 0.4212 0.2895 -0.1334 -0.0176 0.0295  48   PRO B CA  
9297  C C   . PRO B 50   ? 0.2929 0.4344 0.3047 -0.1399 -0.0186 0.0321  48   PRO B C   
9298  O O   . PRO B 50   ? 0.2983 0.4486 0.3117 -0.1447 -0.0175 0.0351  48   PRO B O   
9299  C CB  . PRO B 50   ? 0.2767 0.4216 0.2941 -0.1348 -0.0213 0.0279  48   PRO B CB  
9300  C CG  . PRO B 50   ? 0.2828 0.4295 0.3036 -0.1263 -0.0200 0.0248  48   PRO B CG  
9301  C CD  . PRO B 50   ? 0.2657 0.4062 0.2840 -0.1204 -0.0175 0.0236  48   PRO B CD  
9302  N N   . PRO B 51   ? 0.3219 0.4464 0.3262 -0.1395 -0.0204 0.0310  49   PRO B N   
9303  C CA  . PRO B 51   ? 0.3051 0.4221 0.3034 -0.1457 -0.0213 0.0337  49   PRO B CA  
9304  C C   . PRO B 51   ? 0.3067 0.4300 0.3057 -0.1446 -0.0177 0.0355  49   PRO B C   
9305  O O   . PRO B 51   ? 0.3224 0.4470 0.3193 -0.1510 -0.0176 0.0388  49   PRO B O   
9306  C CB  . PRO B 51   ? 0.3431 0.4406 0.3335 -0.1439 -0.0240 0.0316  49   PRO B CB  
9307  C CG  . PRO B 51   ? 0.3588 0.4552 0.3517 -0.1354 -0.0230 0.0280  49   PRO B CG  
9308  C CD  . PRO B 51   ? 0.2918 0.4030 0.2924 -0.1343 -0.0222 0.0276  49   PRO B CD  
9309  N N   . LEU B 52   ? 0.2940 0.4209 0.2958 -0.1367 -0.0147 0.0335  50   LEU B N   
9310  C CA  . LEU B 52   ? 0.2773 0.4113 0.2800 -0.1354 -0.0111 0.0351  50   LEU B CA  
9311  C C   . LEU B 52   ? 0.2905 0.4427 0.2996 -0.1390 -0.0089 0.0377  50   LEU B C   
9312  O O   . LEU B 52   ? 0.2802 0.4371 0.2883 -0.1431 -0.0073 0.0407  50   LEU B O   
9313  C CB  . LEU B 52   ? 0.2850 0.4189 0.2893 -0.1261 -0.0086 0.0321  50   LEU B CB  
9314  C CG  . LEU B 52   ? 0.2766 0.3937 0.2752 -0.1221 -0.0104 0.0296  50   LEU B CG  
9315  C CD1 . LEU B 52   ? 0.2809 0.3998 0.2824 -0.1132 -0.0081 0.0266  50   LEU B CD1 
9316  C CD2 . LEU B 52   ? 0.3049 0.4116 0.2964 -0.1252 -0.0110 0.0314  50   LEU B CD2 
9317  N N   . VAL B 53   ? 0.2647 0.4277 0.2805 -0.1373 -0.0088 0.0367  51   VAL B N   
9318  C CA  . VAL B 53   ? 0.2607 0.4401 0.2823 -0.1393 -0.0071 0.0388  51   VAL B CA  
9319  C C   . VAL B 53   ? 0.3292 0.5056 0.3468 -0.1466 -0.0090 0.0418  51   VAL B C   
9320  O O   . VAL B 53   ? 0.3007 0.4853 0.3192 -0.1484 -0.0070 0.0443  51   VAL B O   
9321  C CB  . VAL B 53   ? 0.2687 0.4565 0.2966 -0.1357 -0.0076 0.0369  51   VAL B CB  
9322  C CG1 . VAL B 53   ? 0.2974 0.4980 0.3294 -0.1375 -0.0070 0.0390  51   VAL B CG1 
9323  C CG2 . VAL B 53   ? 0.2698 0.4638 0.3024 -0.1280 -0.0048 0.0344  51   VAL B CG2 
9324  N N   . GLU B 54   ? 0.3356 0.4998 0.3485 -0.1507 -0.0130 0.0416  52   GLU B N   
9325  C CA  . GLU B 54   ? 0.3392 0.4993 0.3478 -0.1577 -0.0152 0.0444  52   GLU B CA  
9326  C C   . GLU B 54   ? 0.3531 0.5081 0.3563 -0.1606 -0.0140 0.0468  52   GLU B C   
9327  O O   . GLU B 54   ? 0.3599 0.5208 0.3629 -0.1644 -0.0132 0.0496  52   GLU B O   
9328  C CB  . GLU B 54   ? 0.3945 0.5406 0.3981 -0.1608 -0.0198 0.0433  52   GLU B CB  
9329  N N   . ALA B 55   ? 0.3197 0.4640 0.3186 -0.1589 -0.0139 0.0457  53   ALA B N   
9330  C CA  . ALA B 55   ? 0.3547 0.4932 0.3480 -0.1614 -0.0129 0.0479  53   ALA B CA  
9331  C C   . ALA B 55   ? 0.3041 0.4568 0.3014 -0.1593 -0.0084 0.0494  53   ALA B C   
9332  O O   . ALA B 55   ? 0.3674 0.5199 0.3611 -0.1627 -0.0075 0.0522  53   ALA B O   
9333  C CB  . ALA B 55   ? 0.3648 0.4890 0.3529 -0.1594 -0.0137 0.0462  53   ALA B CB  
9334  N N   . ALA B 56   ? 0.3193 0.4839 0.3235 -0.1533 -0.0056 0.0475  54   ALA B N   
9335  C CA  . ALA B 56   ? 0.3387 0.5162 0.3464 -0.1501 -0.0012 0.0484  54   ALA B CA  
9336  C C   . ALA B 56   ? 0.3445 0.5360 0.3567 -0.1518 -0.0001 0.0503  54   ALA B C   
9337  O O   . ALA B 56   ? 0.3622 0.5641 0.3766 -0.1498 0.0034  0.0514  54   ALA B O   
9338  C CB  . ALA B 56   ? 0.3184 0.5020 0.3312 -0.1425 0.0013  0.0454  54   ALA B CB  
9339  N N   . THR B 57   ? 0.3589 0.5508 0.3723 -0.1553 -0.0030 0.0508  55   THR B N   
9340  C CA  . THR B 57   ? 0.3948 0.6008 0.4133 -0.1566 -0.0021 0.0524  55   THR B CA  
9341  C C   . THR B 57   ? 0.3905 0.5989 0.4060 -0.1615 -0.0010 0.0559  55   THR B C   
9342  O O   . THR B 57   ? 0.3912 0.5879 0.3998 -0.1668 -0.0031 0.0575  55   THR B O   
9343  C CB  . THR B 57   ? 0.4127 0.6168 0.4323 -0.1600 -0.0058 0.0522  55   THR B CB  
9344  O OG1 . THR B 57   ? 0.3852 0.5903 0.4088 -0.1547 -0.0063 0.0490  55   THR B OG1 
9345  C CG2 . THR B 57   ? 0.3697 0.5870 0.3935 -0.1628 -0.0054 0.0545  55   THR B CG2 
9346  N N   . GLN B 58   ? 0.4221 0.6456 0.4425 -0.1596 0.0022  0.0569  56   GLN B N   
9347  C CA  . GLN B 58   ? 0.3847 0.6130 0.4032 -0.1639 0.0036  0.0602  56   GLN B CA  
9348  C C   . GLN B 58   ? 0.4234 0.6668 0.4482 -0.1649 0.0041  0.0615  56   GLN B C   
9349  O O   . GLN B 58   ? 0.3949 0.6468 0.4260 -0.1606 0.0045  0.0596  56   GLN B O   
9350  C CB  . GLN B 58   ? 0.4131 0.6447 0.4305 -0.1602 0.0076  0.0604  56   GLN B CB  
9351  C CG  . GLN B 58   ? 0.4089 0.6275 0.4213 -0.1577 0.0075  0.0586  56   GLN B CG  
9352  C CD  . GLN B 58   ? 0.4774 0.6944 0.4852 -0.1576 0.0102  0.0601  56   GLN B CD  
9353  O OE1 . GLN B 58   ? 0.4952 0.7079 0.4980 -0.1633 0.0094  0.0630  56   GLN B OE1 
9354  N NE2 . GLN B 58   ? 0.4610 0.6813 0.4701 -0.1511 0.0134  0.0582  56   GLN B NE2 
9355  N N   . SER B 59   ? 0.4484 0.6948 0.4714 -0.1707 0.0041  0.0648  57   SER B N   
9356  C CA  . SER B 59   ? 0.4204 0.6807 0.4489 -0.1726 0.0044  0.0664  57   SER B CA  
9357  C C   . SER B 59   ? 0.4403 0.7166 0.4755 -0.1660 0.0086  0.0655  57   SER B C   
9358  O O   . SER B 59   ? 0.4091 0.6859 0.4438 -0.1609 0.0116  0.0643  57   SER B O   
9359  C CB  . SER B 59   ? 0.4684 0.7285 0.4931 -0.1801 0.0038  0.0702  57   SER B CB  
9360  O OG  . SER B 59   ? 0.4624 0.7254 0.4852 -0.1788 0.0073  0.0714  57   SER B OG  
9361  N N   . LYS B 60   ? 0.4224 0.7116 0.4638 -0.1660 0.0087  0.0662  58   LYS B N   
9362  C CA  . LYS B 60   ? 0.4443 0.7492 0.4921 -0.1599 0.0126  0.0655  58   LYS B CA  
9363  C C   . LYS B 60   ? 0.4407 0.7504 0.4865 -0.1601 0.0160  0.0675  58   LYS B C   
9364  O O   . LYS B 60   ? 0.4361 0.7529 0.4844 -0.1536 0.0196  0.0661  58   LYS B O   
9365  C CB  . LYS B 60   ? 0.4181 0.7357 0.4723 -0.1609 0.0118  0.0664  58   LYS B CB  
9366  N N   . GLU B 61   ? 0.4533 0.7589 0.4945 -0.1675 0.0150  0.0706  59   GLU B N   
9367  C CA  . GLU B 61   ? 0.4065 0.7162 0.4454 -0.1683 0.0181  0.0726  59   GLU B CA  
9368  C C   . GLU B 61   ? 0.4473 0.7482 0.4816 -0.1641 0.0200  0.0710  59   GLU B C   
9369  O O   . GLU B 61   ? 0.4338 0.7419 0.4694 -0.1589 0.0238  0.0703  59   GLU B O   
9370  C CB  . GLU B 61   ? 0.5220 0.8275 0.5564 -0.1775 0.0161  0.0764  59   GLU B CB  
9371  N N   . ILE B 62   ? 0.4289 0.7139 0.4575 -0.1662 0.0172  0.0702  60   ILE B N   
9372  C CA  . ILE B 62   ? 0.4403 0.7160 0.4642 -0.1625 0.0187  0.0687  60   ILE B CA  
9373  C C   . ILE B 62   ? 0.4137 0.6952 0.4423 -0.1535 0.0211  0.0652  60   ILE B C   
9374  O O   . ILE B 62   ? 0.4527 0.7357 0.4801 -0.1487 0.0244  0.0643  60   ILE B O   
9375  C CB  . ILE B 62   ? 0.4418 0.6993 0.4589 -0.1666 0.0149  0.0685  60   ILE B CB  
9376  C CG1 . ILE B 62   ? 0.4923 0.7433 0.5036 -0.1749 0.0129  0.0721  60   ILE B CG1 
9377  C CG2 . ILE B 62   ? 0.4464 0.6947 0.4597 -0.1619 0.0161  0.0664  60   ILE B CG2 
9378  C CD1 . ILE B 62   ? 0.4960 0.7283 0.5000 -0.1789 0.0091  0.0721  60   ILE B CD1 
9379  N N   . ARG B 63   ? 0.3529 0.6373 0.3865 -0.1509 0.0196  0.0632  61   ARG B N   
9380  C CA  . ARG B 63   ? 0.3870 0.6766 0.4252 -0.1424 0.0216  0.0598  61   ARG B CA  
9381  C C   . ARG B 63   ? 0.4152 0.7196 0.4575 -0.1374 0.0258  0.0599  61   ARG B C   
9382  O O   . ARG B 63   ? 0.3968 0.7028 0.4396 -0.1305 0.0285  0.0577  61   ARG B O   
9383  C CB  . ARG B 63   ? 0.3871 0.6779 0.4300 -0.1411 0.0190  0.0581  61   ARG B CB  
9384  C CG  . ARG B 63   ? 0.3913 0.6669 0.4302 -0.1435 0.0154  0.0569  61   ARG B CG  
9385  C CD  . ARG B 63   ? 0.4753 0.7522 0.5189 -0.1406 0.0134  0.0545  61   ARG B CD  
9386  N NE  . ARG B 63   ? 0.4716 0.7542 0.5181 -0.1452 0.0111  0.0562  61   ARG B NE  
9387  C CZ  . ARG B 63   ? 0.4711 0.7665 0.5243 -0.1421 0.0118  0.0557  61   ARG B CZ  
9388  N NH1 . ARG B 63   ? 0.4857 0.7896 0.5432 -0.1344 0.0148  0.0537  61   ARG B NH1 
9389  N NH2 . ARG B 63   ? 0.4795 0.7789 0.5348 -0.1469 0.0094  0.0574  61   ARG B NH2 
9390  N N   . ASP B 64   ? 0.3561 0.6713 0.4015 -0.1406 0.0262  0.0623  62   ASP B N   
9391  C CA  . ASP B 64   ? 0.3637 0.6929 0.4127 -0.1361 0.0302  0.0625  62   ASP B CA  
9392  C C   . ASP B 64   ? 0.3495 0.6758 0.3932 -0.1359 0.0331  0.0635  62   ASP B C   
9393  O O   . ASP B 64   ? 0.4066 0.7381 0.4512 -0.1292 0.0365  0.0618  62   ASP B O   
9394  C CB  . ASP B 64   ? 0.4158 0.7573 0.4693 -0.1402 0.0300  0.0651  62   ASP B CB  
9395  C CG  . ASP B 64   ? 0.4735 0.8198 0.5328 -0.1393 0.0277  0.0641  62   ASP B CG  
9396  O OD1 . ASP B 64   ? 0.4210 0.7670 0.4830 -0.1327 0.0278  0.0609  62   ASP B OD1 
9397  O OD2 . ASP B 64   ? 0.5405 0.8912 0.6017 -0.1451 0.0257  0.0664  62   ASP B OD2 
9398  N N   . ALA B 65   ? 0.3351 0.6527 0.3729 -0.1431 0.0316  0.0661  63   ALA B N   
9399  C CA  . ALA B 65   ? 0.3876 0.7014 0.4196 -0.1433 0.0340  0.0671  63   ALA B CA  
9400  C C   . ALA B 65   ? 0.4252 0.7307 0.4542 -0.1372 0.0352  0.0642  63   ALA B C   
9401  O O   . ALA B 65   ? 0.4510 0.7596 0.4784 -0.1327 0.0386  0.0635  63   ALA B O   
9402  C CB  . ALA B 65   ? 0.4102 0.7142 0.4359 -0.1522 0.0316  0.0704  63   ALA B CB  
9403  N N   . ALA B 66   ? 0.4132 0.7082 0.4411 -0.1370 0.0324  0.0623  64   ALA B N   
9404  C CA  . ALA B 66   ? 0.3833 0.6703 0.4084 -0.1315 0.0332  0.0595  64   ALA B CA  
9405  C C   . ALA B 66   ? 0.3927 0.6894 0.4230 -0.1225 0.0362  0.0565  64   ALA B C   
9406  O O   . ALA B 66   ? 0.4024 0.6973 0.4300 -0.1173 0.0387  0.0549  64   ALA B O   
9407  C CB  . ALA B 66   ? 0.4054 0.6794 0.4286 -0.1335 0.0295  0.0583  64   ALA B CB  
9408  N N   . ALA B 67   ? 0.3647 0.6714 0.4019 -0.1204 0.0358  0.0557  65   ALA B N   
9409  C CA  . ALA B 67   ? 0.3491 0.6647 0.3910 -0.1116 0.0384  0.0529  65   ALA B CA  
9410  C C   . ALA B 67   ? 0.4515 0.7761 0.4929 -0.1084 0.0425  0.0535  65   ALA B C   
9411  O O   . ALA B 67   ? 0.3836 0.7103 0.4252 -0.1010 0.0451  0.0510  65   ALA B O   
9412  C CB  . ALA B 67   ? 0.4373 0.7617 0.4864 -0.1105 0.0370  0.0524  65   ALA B CB  
9413  N N   . SER B 68   ? 0.4473 0.7772 0.4881 -0.1140 0.0431  0.0568  66   SER B N   
9414  C CA  . SER B 68   ? 0.4170 0.7549 0.4567 -0.1116 0.0469  0.0577  66   SER B CA  
9415  C C   . SER B 68   ? 0.4619 0.7902 0.4941 -0.1106 0.0485  0.0573  66   SER B C   
9416  O O   . SER B 68   ? 0.4838 0.8154 0.5151 -0.1042 0.0517  0.0556  66   SER B O   
9417  C CB  . SER B 68   ? 0.4529 0.7984 0.4936 -0.1184 0.0469  0.0615  66   SER B CB  
9418  N N   . THR B 69   ? 0.4286 0.7447 0.4553 -0.1169 0.0461  0.0589  67   THR B N   
9419  C CA  . THR B 69   ? 0.4231 0.7288 0.4422 -0.1163 0.0471  0.0587  67   THR B CA  
9420  C C   . THR B 69   ? 0.4294 0.7312 0.4483 -0.1084 0.0480  0.0548  67   THR B C   
9421  O O   . THR B 69   ? 0.3954 0.6962 0.4105 -0.1039 0.0507  0.0537  67   THR B O   
9422  C CB  . THR B 69   ? 0.3901 0.6824 0.4036 -0.1240 0.0437  0.0608  67   THR B CB  
9423  O OG1 . THR B 69   ? 0.4569 0.7522 0.4695 -0.1313 0.0431  0.0646  67   THR B OG1 
9424  C CG2 . THR B 69   ? 0.3738 0.6546 0.3794 -0.1230 0.0444  0.0604  67   THR B CG2 
9425  N N   . ALA B 70   ? 0.3633 0.6622 0.3858 -0.1067 0.0457  0.0527  68   ALA B N   
9426  C CA  . ALA B 70   ? 0.4262 0.7223 0.4493 -0.0991 0.0465  0.0490  68   ALA B CA  
9427  C C   . ALA B 70   ? 0.4166 0.7238 0.4429 -0.0912 0.0500  0.0470  68   ALA B C   
9428  O O   . ALA B 70   ? 0.4163 0.7208 0.4399 -0.0851 0.0520  0.0446  68   ALA B O   
9429  C CB  . ALA B 70   ? 0.3961 0.6889 0.4233 -0.0989 0.0434  0.0473  68   ALA B CB  
9430  N N   . ARG B 71   ? 0.4479 0.7675 0.4799 -0.0912 0.0508  0.0480  69   ARG B N   
9431  C CA  . ARG B 71   ? 0.4586 0.7888 0.4935 -0.0838 0.0541  0.0464  69   ARG B CA  
9432  C C   . ARG B 71   ? 0.3241 0.6543 0.3534 -0.0825 0.0573  0.0470  69   ARG B C   
9433  O O   . ARG B 71   ? 0.3777 0.7083 0.4055 -0.0752 0.0597  0.0443  69   ARG B O   
9434  C CB  . ARG B 71   ? 0.4442 0.7876 0.4859 -0.0849 0.0541  0.0478  69   ARG B CB  
9435  C CG  . ARG B 71   ? 0.4445 0.7992 0.4898 -0.0770 0.0573  0.0460  69   ARG B CG  
9436  C CD  . ARG B 71   ? 0.4237 0.7907 0.4765 -0.0772 0.0567  0.0469  69   ARG B CD  
9437  N NE  . ARG B 71   ? 0.4346 0.8016 0.4919 -0.0723 0.0550  0.0442  69   ARG B NE  
9438  C CZ  . ARG B 71   ? 0.4808 0.8502 0.5396 -0.0635 0.0567  0.0410  69   ARG B CZ  
9439  N NH1 . ARG B 71   ? 0.4533 0.8250 0.5092 -0.0584 0.0600  0.0400  69   ARG B NH1 
9440  N NH2 . ARG B 71   ? 0.4922 0.8610 0.5549 -0.0597 0.0548  0.0389  69   ARG B NH2 
9441  N N   . LYS B 72   ? 0.3539 0.6828 0.3796 -0.0895 0.0573  0.0504  70   LYS B N   
9442  C CA  . LYS B 72   ? 0.3563 0.6850 0.3761 -0.0890 0.0602  0.0513  70   LYS B CA  
9443  C C   . LYS B 72   ? 0.4234 0.7406 0.4366 -0.0855 0.0606  0.0492  70   LYS B C   
9444  O O   . LYS B 72   ? 0.4214 0.7395 0.4307 -0.0810 0.0636  0.0481  70   LYS B O   
9445  C CB  . LYS B 72   ? 0.3832 0.7109 0.4001 -0.0980 0.0595  0.0556  70   LYS B CB  
9446  C CG  . LYS B 72   ? 0.4165 0.7438 0.4271 -0.0985 0.0623  0.0571  70   LYS B CG  
9447  C CD  . LYS B 72   ? 0.4271 0.7530 0.4350 -0.1078 0.0611  0.0615  70   LYS B CD  
9448  C CE  . LYS B 72   ? 0.4747 0.7974 0.4750 -0.1090 0.0635  0.0631  70   LYS B CE  
9449  N NZ  . LYS B 72   ? 0.3914 0.7265 0.3933 -0.1046 0.0677  0.0630  70   LYS B NZ  
9450  N N   . LEU B 73   ? 0.4331 0.7392 0.4446 -0.0874 0.0577  0.0484  71   LEU B N   
9451  C CA  . LEU B 73   ? 0.4010 0.6961 0.4062 -0.0842 0.0579  0.0464  71   LEU B CA  
9452  C C   . LEU B 73   ? 0.3764 0.6737 0.3839 -0.0749 0.0593  0.0422  71   LEU B C   
9453  O O   . LEU B 73   ? 0.4471 0.7406 0.4495 -0.0700 0.0612  0.0403  71   LEU B O   
9454  C CB  . LEU B 73   ? 0.3791 0.6618 0.3817 -0.0895 0.0543  0.0471  71   LEU B CB  
9455  C CG  . LEU B 73   ? 0.3649 0.6431 0.3643 -0.0989 0.0523  0.0511  71   LEU B CG  
9456  C CD1 . LEU B 73   ? 0.3893 0.6561 0.3877 -0.1034 0.0484  0.0514  71   LEU B CD1 
9457  C CD2 . LEU B 73   ? 0.4153 0.6888 0.4067 -0.1005 0.0540  0.0529  71   LEU B CD2 
9458  N N   . ILE B 74   ? 0.3900 0.6927 0.4047 -0.0722 0.0582  0.0406  72   ILE B N   
9459  C CA  . ILE B 74   ? 0.4018 0.7054 0.4187 -0.0635 0.0591  0.0366  72   ILE B CA  
9460  C C   . ILE B 74   ? 0.4673 0.7799 0.4846 -0.0571 0.0626  0.0354  72   ILE B C   
9461  O O   . ILE B 74   ? 0.4188 0.7286 0.4332 -0.0501 0.0642  0.0324  72   ILE B O   
9462  C CB  . ILE B 74   ? 0.4006 0.7068 0.4246 -0.0628 0.0567  0.0355  72   ILE B CB  
9463  C CG1 . ILE B 74   ? 0.3961 0.6915 0.4187 -0.0679 0.0534  0.0360  72   ILE B CG1 
9464  C CG2 . ILE B 74   ? 0.3790 0.6875 0.4058 -0.0535 0.0578  0.0316  72   ILE B CG2 
9465  C CD1 . ILE B 74   ? 0.3832 0.6814 0.4121 -0.0711 0.0506  0.0366  72   ILE B CD1 
9466  N N   . GLU B 75   ? 0.4252 0.7486 0.4459 -0.0593 0.0639  0.0377  73   GLU B N   
9467  C CA  . GLU B 75   ? 0.4308 0.7626 0.4511 -0.0540 0.0674  0.0370  73   GLU B CA  
9468  C C   . GLU B 75   ? 0.4738 0.7994 0.4858 -0.0531 0.0694  0.0368  73   GLU B C   
9469  O O   . GLU B 75   ? 0.4948 0.8202 0.5041 -0.0459 0.0716  0.0341  73   GLU B O   
9470  C CB  . GLU B 75   ? 0.3976 0.7416 0.4225 -0.0580 0.0682  0.0400  73   GLU B CB  
9471  N N   . ALA B 76   ? 0.4135 0.7329 0.4206 -0.0604 0.0686  0.0398  74   ALA B N   
9472  C CA  . ALA B 76   ? 0.4525 0.7647 0.4509 -0.0601 0.0701  0.0398  74   ALA B CA  
9473  C C   . ALA B 76   ? 0.4526 0.7549 0.4469 -0.0543 0.0696  0.0362  74   ALA B C   
9474  O O   . ALA B 76   ? 0.4924 0.7926 0.4814 -0.0492 0.0718  0.0343  74   ALA B O   
9475  C CB  . ALA B 76   ? 0.3916 0.6973 0.3856 -0.0692 0.0685  0.0436  74   ALA B CB  
9476  N N   . LEU B 77   ? 0.4163 0.7123 0.4127 -0.0550 0.0668  0.0350  75   LEU B N   
9477  C CA  . LEU B 77   ? 0.4787 0.7655 0.4715 -0.0497 0.0662  0.0316  75   LEU B CA  
9478  C C   . LEU B 77   ? 0.4499 0.7415 0.4451 -0.0403 0.0680  0.0278  75   LEU B C   
9479  O O   . LEU B 77   ? 0.4743 0.7607 0.4639 -0.0350 0.0692  0.0252  75   LEU B O   
9480  C CB  . LEU B 77   ? 0.4470 0.7272 0.4425 -0.0527 0.0628  0.0313  75   LEU B CB  
9481  C CG  . LEU B 77   ? 0.4415 0.7124 0.4326 -0.0608 0.0605  0.0342  75   LEU B CG  
9482  C CD1 . LEU B 77   ? 0.3853 0.6517 0.3805 -0.0632 0.0573  0.0337  75   LEU B CD1 
9483  C CD2 . LEU B 77   ? 0.4343 0.6949 0.4161 -0.0597 0.0609  0.0334  75   LEU B CD2 
9484  N N   . ARG B 78   ? 0.4089 0.7098 0.4119 -0.0382 0.0680  0.0274  76   ARG B N   
9485  C CA  . ARG B 78   ? 0.4407 0.7455 0.4460 -0.0292 0.0694  0.0238  76   ARG B CA  
9486  C C   . ARG B 78   ? 0.4543 0.7649 0.4567 -0.0251 0.0727  0.0234  76   ARG B C   
9487  O O   . ARG B 78   ? 0.4713 0.7824 0.4732 -0.0172 0.0740  0.0202  76   ARG B O   
9488  C CB  . ARG B 78   ? 0.5094 0.8221 0.5236 -0.0283 0.0681  0.0237  76   ARG B CB  
9489  C CG  . ARG B 78   ? 0.4885 0.7953 0.5056 -0.0314 0.0648  0.0235  76   ARG B CG  
9490  C CD  . ARG B 78   ? 0.5242 0.8379 0.5493 -0.0292 0.0636  0.0228  76   ARG B CD  
9491  N NE  . ARG B 78   ? 0.5146 0.8208 0.5409 -0.0266 0.0613  0.0203  76   ARG B NE  
9492  C CZ  . ARG B 78   ? 0.5594 0.8689 0.5920 -0.0247 0.0597  0.0194  76   ARG B CZ  
9493  N NH1 . ARG B 78   ? 0.5750 0.8951 0.6133 -0.0252 0.0598  0.0208  76   ARG B NH1 
9494  N NH2 . ARG B 78   ? 0.5387 0.8408 0.5717 -0.0221 0.0578  0.0170  76   ARG B NH2 
9495  N N   . GLY B 79   ? 0.4218 0.7363 0.4221 -0.0302 0.0742  0.0266  77   GLY B N   
9496  C CA  . GLY B 79   ? 0.4739 0.7944 0.4714 -0.0269 0.0775  0.0266  77   GLY B CA  
9497  C C   . GLY B 79   ? 0.5016 0.8137 0.4896 -0.0247 0.0789  0.0254  77   GLY B C   
9498  O O   . GLY B 79   ? 0.3759 0.6921 0.3610 -0.0211 0.0817  0.0248  77   GLY B O   
9499  N N   . LYS B 80   ? 0.5095 0.8098 0.4925 -0.0267 0.0769  0.0249  78   LYS B N   
9500  C CA  . LYS B 80   ? 0.4674 0.7594 0.4408 -0.0253 0.0779  0.0240  78   LYS B CA  
9501  C C   . LYS B 80   ? 0.4069 0.6878 0.3763 -0.0205 0.0763  0.0203  78   LYS B C   
9502  O O   . LYS B 80   ? 0.5008 0.7806 0.4750 -0.0182 0.0745  0.0184  78   LYS B O   
9503  C CB  . LYS B 80   ? 0.5003 0.7882 0.4691 -0.0339 0.0772  0.0280  78   LYS B CB  
9504  C CG  . LYS B 80   ? 0.4466 0.7276 0.4168 -0.0399 0.0738  0.0295  78   LYS B CG  
9505  C CD  . LYS B 80   ? 0.4712 0.7501 0.4383 -0.0489 0.0731  0.0340  78   LYS B CD  
9506  C CE  . LYS B 80   ? 0.4371 0.7062 0.4034 -0.0545 0.0695  0.0352  78   LYS B CE  
9507  N NZ  . LYS B 80   ? 0.4051 0.6713 0.3684 -0.0634 0.0685  0.0396  78   LYS B NZ  
9508  N N   . GLY B 85   ? 0.5828 0.7744 0.5151 0.0125  0.0609  -0.0058 83   GLY B N   
9509  C CA  . GLY B 85   ? 0.5342 0.7129 0.4584 0.0150  0.0587  -0.0082 83   GLY B CA  
9510  C C   . GLY B 85   ? 0.5209 0.6926 0.4458 0.0214  0.0567  -0.0126 83   GLY B C   
9511  O O   . GLY B 85   ? 0.5128 0.6838 0.4328 0.0273  0.0580  -0.0155 83   GLY B O   
9512  N N   . VAL B 86   ? 0.5178 0.6839 0.4484 0.0202  0.0534  -0.0129 84   VAL B N   
9513  C CA  . VAL B 86   ? 0.5021 0.6619 0.4342 0.0257  0.0515  -0.0166 84   VAL B CA  
9514  C C   . VAL B 86   ? 0.4697 0.6400 0.4054 0.0312  0.0547  -0.0182 84   VAL B C   
9515  O O   . VAL B 86   ? 0.4803 0.6471 0.4134 0.0376  0.0547  -0.0217 84   VAL B O   
9516  C CB  . VAL B 86   ? 0.4958 0.6483 0.4334 0.0227  0.0476  -0.0163 84   VAL B CB  
9517  C CG1 . VAL B 86   ? 0.5658 0.7156 0.5071 0.0280  0.0464  -0.0194 84   VAL B CG1 
9518  C CG2 . VAL B 86   ? 0.5372 0.6769 0.4699 0.0197  0.0441  -0.0161 84   VAL B CG2 
9519  N N   . GLU B 87   ? 0.5020 0.6854 0.4436 0.0290  0.0574  -0.0157 85   GLU B N   
9520  C CA  . GLU B 87   ? 0.5268 0.7214 0.4724 0.0343  0.0604  -0.0169 85   GLU B CA  
9521  C C   . GLU B 87   ? 0.4773 0.6745 0.4160 0.0401  0.0635  -0.0191 85   GLU B C   
9522  O O   . GLU B 87   ? 0.4791 0.6770 0.4177 0.0469  0.0642  -0.0223 85   GLU B O   
9523  C CB  . GLU B 87   ? 0.5469 0.7559 0.4995 0.0301  0.0629  -0.0133 85   GLU B CB  
9524  N N   . GLY B 88   ? 0.4976 0.6961 0.4301 0.0376  0.0652  -0.0176 86   GLY B N   
9525  C CA  . GLY B 88   ? 0.4841 0.6850 0.4094 0.0430  0.0682  -0.0197 86   GLY B CA  
9526  C C   . GLY B 88   ? 0.4471 0.6342 0.3657 0.0482  0.0656  -0.0239 86   GLY B C   
9527  O O   . GLY B 88   ? 0.4379 0.6256 0.3533 0.0548  0.0671  -0.0268 86   GLY B O   
9528  N N   . LEU B 89   ? 0.4390 0.6129 0.3560 0.0451  0.0612  -0.0241 87   LEU B N   
9529  C CA  . LEU B 89   ? 0.4593 0.6199 0.3707 0.0494  0.0583  -0.0280 87   LEU B CA  
9530  C C   . LEU B 89   ? 0.4001 0.5596 0.3158 0.0550  0.0576  -0.0309 87   LEU B C   
9531  O O   . LEU B 89   ? 0.3725 0.5277 0.2834 0.0613  0.0577  -0.0345 87   LEU B O   
9532  C CB  . LEU B 89   ? 0.4578 0.6057 0.3678 0.0445  0.0538  -0.0272 87   LEU B CB  
9533  C CG  . LEU B 89   ? 0.4850 0.6186 0.3899 0.0478  0.0502  -0.0308 87   LEU B CG  
9534  C CD1 . LEU B 89   ? 0.5323 0.6635 0.4274 0.0521  0.0516  -0.0331 87   LEU B CD1 
9535  C CD2 . LEU B 89   ? 0.5159 0.6391 0.4208 0.0424  0.0459  -0.0294 87   LEU B CD2 
9536  N N   . VAL B 90   ? 0.4049 0.5682 0.3296 0.0528  0.0567  -0.0294 88   VAL B N   
9537  C CA  . VAL B 90   ? 0.4169 0.5799 0.3462 0.0578  0.0560  -0.0318 88   VAL B CA  
9538  C C   . VAL B 90   ? 0.4259 0.5992 0.3546 0.0643  0.0600  -0.0333 88   VAL B C   
9539  O O   . VAL B 90   ? 0.4233 0.5923 0.3499 0.0708  0.0596  -0.0368 88   VAL B O   
9540  C CB  . VAL B 90   ? 0.4129 0.5793 0.3517 0.0536  0.0545  -0.0294 88   VAL B CB  
9541  C CG1 . VAL B 90   ? 0.4339 0.6027 0.3778 0.0589  0.0546  -0.0314 88   VAL B CG1 
9542  C CG2 . VAL B 90   ? 0.3702 0.5245 0.3091 0.0487  0.0502  -0.0287 88   VAL B CG2 
9543  N N   . GLN B 91   ? 0.4450 0.6313 0.3753 0.0626  0.0637  -0.0308 89   GLN B N   
9544  C CA  . GLN B 91   ? 0.4573 0.6501 0.3892 0.0672  0.0660  -0.0313 89   GLN B CA  
9545  C C   . GLN B 91   ? 0.4171 0.6027 0.3398 0.0720  0.0664  -0.0342 89   GLN B C   
9546  O O   . GLN B 91   ? 0.4805 0.6640 0.4025 0.0782  0.0664  -0.0368 89   GLN B O   
9547  C CB  . GLN B 91   ? 0.5203 0.7268 0.4571 0.0629  0.0690  -0.0273 89   GLN B CB  
9548  N N   . GLU B 92   ? 0.4366 0.6178 0.3518 0.0692  0.0665  -0.0338 90   GLU B N   
9549  C CA  . GLU B 92   ? 0.4603 0.6354 0.3665 0.0733  0.0670  -0.0362 90   GLU B CA  
9550  C C   . GLU B 92   ? 0.4086 0.5709 0.3104 0.0789  0.0641  -0.0406 90   GLU B C   
9551  O O   . GLU B 92   ? 0.4480 0.6072 0.3456 0.0843  0.0646  -0.0431 90   GLU B O   
9552  C CB  . GLU B 92   ? 0.4911 0.6633 0.3899 0.0688  0.0673  -0.0348 90   GLU B CB  
9553  C CG  . GLU B 92   ? 0.5290 0.6958 0.4183 0.0727  0.0681  -0.0371 90   GLU B CG  
9554  C CD  . GLU B 92   ? 0.5501 0.7119 0.4311 0.0686  0.0676  -0.0360 90   GLU B CD  
9555  O OE1 . GLU B 92   ? 0.6009 0.7648 0.4835 0.0624  0.0671  -0.0330 90   GLU B OE1 
9556  O OE2 . GLU B 92   ? 0.5243 0.6796 0.3966 0.0715  0.0676  -0.0382 90   GLU B OE2 
9557  N N   . TYR B 93   ? 0.4173 0.5720 0.3199 0.0775  0.0610  -0.0416 91   TYR B N   
9558  C CA  . TYR B 93   ? 0.4317 0.5736 0.3301 0.0821  0.0578  -0.0456 91   TYR B CA  
9559  C C   . TYR B 93   ? 0.4245 0.5665 0.3300 0.0851  0.0566  -0.0466 91   TYR B C   
9560  O O   . TYR B 93   ? 0.3959 0.5269 0.2988 0.0882  0.0537  -0.0496 91   TYR B O   
9561  C CB  . TYR B 93   ? 0.3924 0.5223 0.2860 0.0784  0.0542  -0.0461 91   TYR B CB  
9562  C CG  . TYR B 93   ? 0.3840 0.5111 0.2683 0.0773  0.0548  -0.0462 91   TYR B CG  
9563  C CD1 . TYR B 93   ? 0.3798 0.4986 0.2551 0.0823  0.0542  -0.0497 91   TYR B CD1 
9564  C CD2 . TYR B 93   ? 0.4303 0.5626 0.3149 0.0711  0.0560  -0.0424 91   TYR B CD2 
9565  C CE1 . TYR B 93   ? 0.4215 0.5374 0.2882 0.0811  0.0547  -0.0496 91   TYR B CE1 
9566  C CE2 . TYR B 93   ? 0.4473 0.5772 0.3231 0.0702  0.0567  -0.0423 91   TYR B CE2 
9567  C CZ  . TYR B 93   ? 0.4471 0.5693 0.3136 0.0755  0.0562  -0.0461 91   TYR B CZ  
9568  O OH  . TYR B 93   ? 0.4687 0.5880 0.3264 0.0744  0.0566  -0.0459 91   TYR B OH  
9569  N N   . SER B 94   ? 0.3771 0.5309 0.2913 0.0841  0.0587  -0.0441 92   SER B N   
9570  C CA  . SER B 94   ? 0.3488 0.5039 0.2701 0.0870  0.0577  -0.0447 92   SER B CA  
9571  C C   . SER B 94   ? 0.3505 0.4966 0.2727 0.0857  0.0543  -0.0459 92   SER B C   
9572  O O   . SER B 94   ? 0.3681 0.5066 0.2903 0.0897  0.0521  -0.0484 92   SER B O   
9573  C CB  . SER B 94   ? 0.3683 0.5205 0.2873 0.0940  0.0578  -0.0474 92   SER B CB  
9574  O OG  . SER B 94   ? 0.4446 0.6059 0.3632 0.0953  0.0611  -0.0462 92   SER B OG  
9575  N N   . LEU B 95   ? 0.3182 0.4629 0.2422 0.0787  0.0529  -0.0433 93   LEU B N   
9576  C CA  . LEU B 95   ? 0.3156 0.4493 0.2421 0.0753  0.0484  -0.0433 93   LEU B CA  
9577  C C   . LEU B 95   ? 0.3358 0.4747 0.2718 0.0742  0.0480  -0.0417 93   LEU B C   
9578  O O   . LEU B 95   ? 0.3257 0.4769 0.2675 0.0721  0.0504  -0.0391 93   LEU B O   
9579  C CB  . LEU B 95   ? 0.3360 0.4659 0.2613 0.0681  0.0468  -0.0408 93   LEU B CB  
9580  C CG  . LEU B 95   ? 0.3507 0.4747 0.2666 0.0681  0.0467  -0.0418 93   LEU B CG  
9581  C CD1 . LEU B 95   ? 0.3260 0.4447 0.2415 0.0610  0.0443  -0.0394 93   LEU B CD1 
9582  C CD2 . LEU B 95   ? 0.3640 0.4765 0.2732 0.0735  0.0447  -0.0459 93   LEU B CD2 
9583  N N   . SER B 96   ? 0.2993 0.4287 0.2369 0.0753  0.0447  -0.0432 94   SER B N   
9584  C CA  . SER B 96   ? 0.2951 0.4273 0.2412 0.0728  0.0435  -0.0414 94   SER B CA  
9585  C C   . SER B 96   ? 0.3075 0.4383 0.2564 0.0649  0.0418  -0.0384 94   SER B C   
9586  O O   . SER B 96   ? 0.2895 0.4153 0.2336 0.0619  0.0411  -0.0380 94   SER B O   
9587  C CB  . SER B 96   ? 0.2826 0.4043 0.2289 0.0758  0.0404  -0.0438 94   SER B CB  
9588  O OG  . SER B 96   ? 0.2855 0.3943 0.2279 0.0730  0.0369  -0.0445 94   SER B OG  
9589  N N   . SER B 97   ? 0.2859 0.4208 0.2425 0.0617  0.0411  -0.0363 95   SER B N   
9590  C CA  . SER B 97   ? 0.2720 0.4045 0.2312 0.0546  0.0393  -0.0337 95   SER B CA  
9591  C C   . SER B 97   ? 0.2781 0.3964 0.2335 0.0532  0.0356  -0.0349 95   SER B C   
9592  O O   . SER B 97   ? 0.2637 0.3780 0.2163 0.0490  0.0346  -0.0338 95   SER B O   
9593  C CB  . SER B 97   ? 0.3194 0.4574 0.2871 0.0521  0.0389  -0.0316 95   SER B CB  
9594  O OG  . SER B 97   ? 0.3753 0.5272 0.3466 0.0519  0.0422  -0.0299 95   SER B OG  
9595  N N   . GLN B 98   ? 0.2687 0.3792 0.2240 0.0567  0.0335  -0.0373 96   GLN B N   
9596  C CA  . GLN B 98   ? 0.2658 0.3633 0.2180 0.0554  0.0299  -0.0385 96   GLN B CA  
9597  C C   . GLN B 98   ? 0.2642 0.3563 0.2081 0.0563  0.0298  -0.0400 96   GLN B C   
9598  O O   . GLN B 98   ? 0.2616 0.3459 0.2029 0.0530  0.0273  -0.0397 96   GLN B O   
9599  C CB  . GLN B 98   ? 0.2874 0.3781 0.2407 0.0592  0.0279  -0.0408 96   GLN B CB  
9600  C CG  . GLN B 98   ? 0.2718 0.3645 0.2327 0.0573  0.0270  -0.0392 96   GLN B CG  
9601  C CD  . GLN B 98   ? 0.2869 0.3753 0.2503 0.0512  0.0246  -0.0373 96   GLN B CD  
9602  O OE1 . GLN B 98   ? 0.3165 0.4105 0.2821 0.0469  0.0256  -0.0348 96   GLN B OE1 
9603  N NE2 . GLN B 98   ? 0.2694 0.3476 0.2325 0.0508  0.0215  -0.0383 96   GLN B NE2 
9604  N N   . GLU B 99   ? 0.2478 0.3440 0.1873 0.0610  0.0324  -0.0416 97   GLU B N   
9605  C CA  . GLU B 99   ? 0.2613 0.3529 0.1924 0.0618  0.0325  -0.0430 97   GLU B CA  
9606  C C   . GLU B 99   ? 0.3010 0.3969 0.2312 0.0566  0.0335  -0.0401 97   GLU B C   
9607  O O   . GLU B 99   ? 0.2906 0.3793 0.2156 0.0543  0.0317  -0.0403 97   GLU B O   
9608  C CB  . GLU B 99   ? 0.2777 0.3732 0.2041 0.0684  0.0353  -0.0454 97   GLU B CB  
9609  C CG  . GLU B 99   ? 0.2850 0.3723 0.2093 0.0738  0.0335  -0.0487 97   GLU B CG  
9610  C CD  . GLU B 99   ? 0.3038 0.3965 0.2249 0.0807  0.0366  -0.0509 97   GLU B CD  
9611  O OE1 . GLU B 99   ? 0.3250 0.4285 0.2458 0.0811  0.0402  -0.0497 97   GLU B OE1 
9612  O OE2 . GLU B 99   ? 0.3057 0.3919 0.2243 0.0858  0.0354  -0.0538 97   GLU B OE2 
9613  N N   . GLY B 100  ? 0.2626 0.3700 0.1977 0.0543  0.0362  -0.0375 98   GLY B N   
9614  C CA  . GLY B 100  ? 0.2780 0.3891 0.2125 0.0488  0.0370  -0.0345 98   GLY B CA  
9615  C C   . GLY B 100  ? 0.2823 0.3851 0.2183 0.0435  0.0334  -0.0331 98   GLY B C   
9616  O O   . GLY B 100  ? 0.2909 0.3895 0.2224 0.0404  0.0324  -0.0322 98   GLY B O   
9617  N N   . VAL B 101  ? 0.2420 0.3422 0.1840 0.0426  0.0314  -0.0329 99   VAL B N   
9618  C CA  . VAL B 101  ? 0.2471 0.3396 0.1909 0.0380  0.0280  -0.0318 99   VAL B CA  
9619  C C   . VAL B 101  ? 0.2718 0.3527 0.2097 0.0390  0.0251  -0.0339 99   VAL B C   
9620  O O   . VAL B 101  ? 0.2714 0.3474 0.2069 0.0354  0.0232  -0.0328 99   VAL B O   
9621  C CB  . VAL B 101  ? 0.2398 0.3323 0.1911 0.0374  0.0266  -0.0314 99   VAL B CB  
9622  C CG1 . VAL B 101  ? 0.2577 0.3419 0.2106 0.0333  0.0232  -0.0305 99   VAL B CG1 
9623  C CG2 . VAL B 101  ? 0.2944 0.3983 0.2515 0.0357  0.0291  -0.0291 99   VAL B CG2 
9624  N N   . ALA B 102  ? 0.2506 0.3269 0.1861 0.0440  0.0245  -0.0369 100  ALA B N   
9625  C CA  . ALA B 102  ? 0.2645 0.3296 0.1945 0.0449  0.0214  -0.0391 100  ALA B CA  
9626  C C   . ALA B 102  ? 0.2721 0.3362 0.1946 0.0443  0.0220  -0.0391 100  ALA B C   
9627  O O   . ALA B 102  ? 0.2883 0.3446 0.2074 0.0421  0.0192  -0.0392 100  ALA B O   
9628  C CB  . ALA B 102  ? 0.2820 0.3430 0.2100 0.0506  0.0210  -0.0424 100  ALA B CB  
9629  N N   . LEU B 103  ? 0.2704 0.3427 0.1902 0.0462  0.0256  -0.0389 101  LEU B N   
9630  C CA  . LEU B 103  ? 0.2983 0.3703 0.2106 0.0457  0.0266  -0.0387 101  LEU B CA  
9631  C C   . LEU B 103  ? 0.3081 0.3801 0.2210 0.0396  0.0256  -0.0355 101  LEU B C   
9632  O O   . LEU B 103  ? 0.3037 0.3696 0.2107 0.0381  0.0239  -0.0355 101  LEU B O   
9633  C CB  . LEU B 103  ? 0.2909 0.3732 0.2012 0.0489  0.0311  -0.0388 101  LEU B CB  
9634  C CG  . LEU B 103  ? 0.2958 0.3793 0.1983 0.0483  0.0326  -0.0383 101  LEU B CG  
9635  C CD1 . LEU B 103  ? 0.3459 0.4188 0.2401 0.0513  0.0303  -0.0415 101  LEU B CD1 
9636  C CD2 . LEU B 103  ? 0.3024 0.3979 0.2043 0.0509  0.0374  -0.0379 101  LEU B CD2 
9637  N N   . MET B 104  ? 0.2746 0.3531 0.1942 0.0361  0.0266  -0.0327 102  MET B N   
9638  C CA  . MET B 104  ? 0.3085 0.3864 0.2285 0.0303  0.0256  -0.0296 102  MET B CA  
9639  C C   . MET B 104  ? 0.2997 0.3671 0.2202 0.0281  0.0212  -0.0299 102  MET B C   
9640  O O   . MET B 104  ? 0.3214 0.3846 0.2386 0.0249  0.0196  -0.0285 102  MET B O   
9641  C CB  . MET B 104  ? 0.3079 0.3950 0.2347 0.0269  0.0275  -0.0266 102  MET B CB  
9642  C CG  . MET B 104  ? 0.3402 0.4389 0.2667 0.0286  0.0319  -0.0259 102  MET B CG  
9643  S SD  . MET B 104  ? 0.4156 0.5159 0.3328 0.0282  0.0340  -0.0253 102  MET B SD  
9644  C CE  . MET B 104  ? 0.4453 0.5452 0.3636 0.0205  0.0329  -0.0210 102  MET B CE  
9645  N N   . CYS B 105  ? 0.2703 0.3335 0.1950 0.0300  0.0193  -0.0316 103  CYS B N   
9646  C CA  . CYS B 105  ? 0.2943 0.3477 0.2193 0.0284  0.0152  -0.0321 103  CYS B CA  
9647  C C   . CYS B 105  ? 0.3028 0.3487 0.2199 0.0299  0.0134  -0.0340 103  CYS B C   
9648  O O   . CYS B 105  ? 0.3123 0.3523 0.2274 0.0272  0.0106  -0.0332 103  CYS B O   
9649  C CB  . CYS B 105  ? 0.2847 0.3353 0.2150 0.0304  0.0138  -0.0338 103  CYS B CB  
9650  S SG  . CYS B 105  ? 0.2787 0.3361 0.2182 0.0281  0.0149  -0.0315 103  CYS B SG  
9651  N N   . LEU B 106  ? 0.2877 0.3337 0.2002 0.0345  0.0147  -0.0366 104  LEU B N   
9652  C CA  . LEU B 106  ? 0.2938 0.3327 0.1980 0.0360  0.0130  -0.0386 104  LEU B CA  
9653  C C   . LEU B 106  ? 0.3039 0.3443 0.2030 0.0331  0.0137  -0.0365 104  LEU B C   
9654  O O   . LEU B 106  ? 0.3291 0.3625 0.2238 0.0316  0.0108  -0.0366 104  LEU B O   
9655  C CB  . LEU B 106  ? 0.2999 0.3392 0.1995 0.0416  0.0147  -0.0417 104  LEU B CB  
9656  C CG  . LEU B 106  ? 0.3130 0.3454 0.2031 0.0434  0.0133  -0.0438 104  LEU B CG  
9657  C CD1 . LEU B 106  ? 0.3893 0.4109 0.2787 0.0428  0.0086  -0.0455 104  LEU B CD1 
9658  C CD2 . LEU B 106  ? 0.3373 0.3719 0.2220 0.0490  0.0160  -0.0466 104  LEU B CD2 
9659  N N   . ALA B 107  ? 0.3167 0.3664 0.2164 0.0323  0.0174  -0.0345 105  ALA B N   
9660  C CA  . ALA B 107  ? 0.3052 0.3569 0.1999 0.0294  0.0184  -0.0322 105  ALA B CA  
9661  C C   . ALA B 107  ? 0.3545 0.4019 0.2513 0.0243  0.0155  -0.0297 105  ALA B C   
9662  O O   . ALA B 107  ? 0.3764 0.4190 0.2675 0.0225  0.0137  -0.0290 105  ALA B O   
9663  C CB  . ALA B 107  ? 0.3213 0.3846 0.2174 0.0290  0.0230  -0.0303 105  ALA B CB  
9664  N N   . GLU B 108  ? 0.3300 0.3790 0.2348 0.0220  0.0148  -0.0283 106  GLU B N   
9665  C CA  . GLU B 108  ? 0.3542 0.3986 0.2615 0.0177  0.0119  -0.0261 106  GLU B CA  
9666  C C   . GLU B 108  ? 0.3766 0.4110 0.2806 0.0182  0.0078  -0.0278 106  GLU B C   
9667  O O   . GLU B 108  ? 0.3753 0.4055 0.2762 0.0155  0.0057  -0.0263 106  GLU B O   
9668  C CB  . GLU B 108  ? 0.3440 0.3908 0.2603 0.0163  0.0117  -0.0253 106  GLU B CB  
9669  C CG  . GLU B 108  ? 0.3634 0.4046 0.2827 0.0127  0.0084  -0.0237 106  GLU B CG  
9670  C CD  . GLU B 108  ? 0.4249 0.4671 0.3525 0.0122  0.0078  -0.0236 106  GLU B CD  
9671  O OE1 . GLU B 108  ? 0.3885 0.4370 0.3197 0.0138  0.0103  -0.0240 106  GLU B OE1 
9672  O OE2 . GLU B 108  ? 0.4585 0.4953 0.3889 0.0104  0.0049  -0.0231 106  GLU B OE2 
9673  N N   . ALA B 109  ? 0.3482 0.3786 0.2529 0.0216  0.0064  -0.0308 107  ALA B N   
9674  C CA  . ALA B 109  ? 0.3621 0.3833 0.2642 0.0219  0.0023  -0.0324 107  ALA B CA  
9675  C C   . ALA B 109  ? 0.3633 0.3811 0.2560 0.0226  0.0018  -0.0331 107  ALA B C   
9676  O O   . ALA B 109  ? 0.3755 0.3872 0.2654 0.0208  -0.0014 -0.0326 107  ALA B O   
9677  C CB  . ALA B 109  ? 0.3984 0.4161 0.3028 0.0252  0.0012  -0.0354 107  ALA B CB  
9678  N N   . LEU B 110  ? 0.3442 0.3661 0.2319 0.0254  0.0049  -0.0341 108  LEU B N   
9679  C CA  . LEU B 110  ? 0.3425 0.3614 0.2207 0.0262  0.0046  -0.0348 108  LEU B CA  
9680  C C   . LEU B 110  ? 0.3885 0.4086 0.2642 0.0221  0.0047  -0.0315 108  LEU B C   
9681  O O   . LEU B 110  ? 0.4144 0.4293 0.2832 0.0215  0.0026  -0.0315 108  LEU B O   
9682  C CB  . LEU B 110  ? 0.3610 0.3850 0.2347 0.0302  0.0084  -0.0366 108  LEU B CB  
9683  C CG  . LEU B 110  ? 0.3655 0.3857 0.2387 0.0348  0.0077  -0.0404 108  LEU B CG  
9684  C CD1 . LEU B 110  ? 0.3675 0.3943 0.2379 0.0390  0.0120  -0.0418 108  LEU B CD1 
9685  C CD2 . LEU B 110  ? 0.4288 0.4389 0.2953 0.0358  0.0038  -0.0428 108  LEU B CD2 
9686  N N   . LEU B 111  ? 0.3871 0.4137 0.2678 0.0192  0.0068  -0.0285 109  LEU B N   
9687  C CA  . LEU B 111  ? 0.4276 0.4549 0.3060 0.0151  0.0068  -0.0251 109  LEU B CA  
9688  C C   . LEU B 111  ? 0.4633 0.4832 0.3433 0.0122  0.0024  -0.0240 109  LEU B C   
9689  O O   . LEU B 111  ? 0.4743 0.4925 0.3506 0.0093  0.0015  -0.0216 109  LEU B O   
9690  C CB  . LEU B 111  ? 0.4354 0.4715 0.3185 0.0126  0.0103  -0.0223 109  LEU B CB  
9691  C CG  . LEU B 111  ? 0.3786 0.4233 0.2588 0.0147  0.0149  -0.0226 109  LEU B CG  
9692  C CD1 . LEU B 111  ? 0.4488 0.5026 0.3353 0.0122  0.0180  -0.0200 109  LEU B CD1 
9693  C CD2 . LEU B 111  ? 0.4754 0.5195 0.3461 0.0142  0.0158  -0.0217 109  LEU B CD2 
9694  N N   . ARG B 112  ? 0.4247 0.4404 0.3100 0.0131  -0.0003 -0.0256 110  ARG B N   
9695  C CA  . ARG B 112  ? 0.4762 0.4848 0.3626 0.0111  -0.0047 -0.0250 110  ARG B CA  
9696  C C   . ARG B 112  ? 0.4930 0.4949 0.3718 0.0122  -0.0076 -0.0264 110  ARG B C   
9697  O O   . ARG B 112  ? 0.5011 0.4975 0.3796 0.0105  -0.0112 -0.0256 110  ARG B O   
9698  C CB  . ARG B 112  ? 0.4498 0.4566 0.3444 0.0116  -0.0065 -0.0261 110  ARG B CB  
9699  C CG  . ARG B 112  ? 0.4986 0.5112 0.4007 0.0099  -0.0043 -0.0244 110  ARG B CG  
9700  C CD  . ARG B 112  ? 0.5728 0.5829 0.4826 0.0098  -0.0065 -0.0250 110  ARG B CD  
9701  N NE  . ARG B 112  ? 0.5552 0.5655 0.4675 0.0131  -0.0061 -0.0278 110  ARG B NE  
9702  C CZ  . ARG B 112  ? 0.5409 0.5566 0.4582 0.0141  -0.0035 -0.0280 110  ARG B CZ  
9703  N NH1 . ARG B 112  ? 0.5880 0.6097 0.5087 0.0120  -0.0011 -0.0258 110  ARG B NH1 
9704  N NH2 . ARG B 112  ? 0.5501 0.5649 0.4691 0.0172  -0.0035 -0.0306 110  ARG B NH2 
9705  N N   . ILE B 113  ? 0.4669 0.4690 0.3394 0.0152  -0.0062 -0.0287 111  ILE B N   
9706  C CA  . ILE B 113  ? 0.4946 0.4909 0.3585 0.0161  -0.0085 -0.0298 111  ILE B CA  
9707  C C   . ILE B 113  ? 0.5115 0.5102 0.3694 0.0139  -0.0068 -0.0270 111  ILE B C   
9708  O O   . ILE B 113  ? 0.5357 0.5406 0.3907 0.0147  -0.0027 -0.0266 111  ILE B O   
9709  C CB  . ILE B 113  ? 0.4828 0.4779 0.3419 0.0204  -0.0077 -0.0335 111  ILE B CB  
9710  C CG1 . ILE B 113  ? 0.4814 0.4739 0.3466 0.0223  -0.0094 -0.0360 111  ILE B CG1 
9711  C CG2 . ILE B 113  ? 0.5226 0.5115 0.3720 0.0211  -0.0102 -0.0347 111  ILE B CG2 
9712  C CD1 . ILE B 113  ? 0.4854 0.4769 0.3466 0.0266  -0.0082 -0.0396 111  ILE B CD1 
9713  N N   . PRO B 114  ? 0.5775 0.5719 0.4333 0.0110  -0.0097 -0.0249 112  PRO B N   
9714  C CA  . PRO B 114  ? 0.5746 0.5713 0.4252 0.0084  -0.0081 -0.0217 112  PRO B CA  
9715  C C   . PRO B 114  ? 0.5286 0.5248 0.3688 0.0101  -0.0068 -0.0226 112  PRO B C   
9716  O O   . PRO B 114  ? 0.5771 0.5783 0.4134 0.0088  -0.0035 -0.0204 112  PRO B O   
9717  C CB  . PRO B 114  ? 0.5307 0.5216 0.3822 0.0054  -0.0122 -0.0195 112  PRO B CB  
9718  C CG  . PRO B 114  ? 0.5524 0.5372 0.4060 0.0073  -0.0163 -0.0222 112  PRO B CG  
9719  C CD  . PRO B 114  ? 0.5376 0.5253 0.3965 0.0100  -0.0146 -0.0250 112  PRO B CD  
9720  N N   . ASP B 115  ? 0.5738 0.5644 0.4092 0.0128  -0.0094 -0.0256 113  ASP B N   
9721  C CA  . ASP B 115  ? 0.6232 0.6123 0.4479 0.0144  -0.0087 -0.0266 113  ASP B CA  
9722  C C   . ASP B 115  ? 0.6052 0.6000 0.4282 0.0180  -0.0043 -0.0289 113  ASP B C   
9723  O O   . ASP B 115  ? 0.6021 0.5959 0.4281 0.0210  -0.0046 -0.0320 113  ASP B O   
9724  C CB  . ASP B 115  ? 0.5999 0.5802 0.4201 0.0158  -0.0137 -0.0290 113  ASP B CB  
9725  C CG  . ASP B 115  ? 0.6687 0.6469 0.4774 0.0180  -0.0132 -0.0307 113  ASP B CG  
9726  O OD1 . ASP B 115  ? 0.7457 0.7258 0.5480 0.0165  -0.0114 -0.0283 113  ASP B OD1 
9727  O OD2 . ASP B 115  ? 0.6821 0.6564 0.4879 0.0212  -0.0146 -0.0343 113  ASP B OD2 
9728  N N   . THR B 116  ? 0.6163 0.6169 0.4342 0.0176  -0.0003 -0.0272 114  THR B N   
9729  C CA  . THR B 116  ? 0.6250 0.6321 0.4412 0.0212  0.0043  -0.0291 114  THR B CA  
9730  C C   . THR B 116  ? 0.6440 0.6457 0.4541 0.0257  0.0028  -0.0335 114  THR B C   
9731  O O   . THR B 116  ? 0.5883 0.5920 0.4008 0.0294  0.0045  -0.0363 114  THR B O   
9732  C CB  . THR B 116  ? 0.6770 0.6907 0.4874 0.0199  0.0085  -0.0265 114  THR B CB  
9733  O OG1 . THR B 116  ? 0.7446 0.7639 0.5613 0.0157  0.0101  -0.0226 114  THR B OG1 
9734  C CG2 . THR B 116  ? 0.6807 0.7010 0.4882 0.0241  0.0131  -0.0287 114  THR B CG2 
9735  N N   . ALA B 117  ? 0.6861 0.6804 0.4879 0.0257  -0.0005 -0.0342 115  ALA B N   
9736  C CA  . ALA B 117  ? 0.6707 0.6590 0.4657 0.0297  -0.0022 -0.0384 115  ALA B CA  
9737  C C   . ALA B 117  ? 0.6018 0.5858 0.4034 0.0314  -0.0050 -0.0413 115  ALA B C   
9738  O O   . ALA B 117  ? 0.6478 0.6314 0.4482 0.0355  -0.0038 -0.0447 115  ALA B O   
9739  C CB  . ALA B 117  ? 0.6508 0.6315 0.4366 0.0287  -0.0060 -0.0384 115  ALA B CB  
9740  N N   . THR B 118  ? 0.6104 0.5909 0.4189 0.0284  -0.0087 -0.0400 116  THR B N   
9741  C CA  . THR B 118  ? 0.5943 0.5710 0.4095 0.0296  -0.0115 -0.0423 116  THR B CA  
9742  C C   . THR B 118  ? 0.5809 0.5640 0.4033 0.0315  -0.0077 -0.0430 116  THR B C   
9743  O O   . THR B 118  ? 0.5842 0.5647 0.4078 0.0345  -0.0082 -0.0461 116  THR B O   
9744  C CB  . THR B 118  ? 0.5916 0.5649 0.4134 0.0258  -0.0156 -0.0403 116  THR B CB  
9745  O OG1 . THR B 118  ? 0.6443 0.6117 0.4594 0.0243  -0.0193 -0.0397 116  THR B OG1 
9746  C CG2 . THR B 118  ? 0.5790 0.5484 0.4075 0.0268  -0.0184 -0.0425 116  THR B CG2 
9747  N N   . ARG B 119  ? 0.5566 0.5478 0.3835 0.0296  -0.0040 -0.0400 117  ARG B N   
9748  C CA  . ARG B 119  ? 0.5265 0.5246 0.3605 0.0312  -0.0004 -0.0403 117  ARG B CA  
9749  C C   . ARG B 119  ? 0.5395 0.5403 0.3680 0.0361  0.0029  -0.0431 117  ARG B C   
9750  O O   . ARG B 119  ? 0.5107 0.5112 0.3424 0.0393  0.0033  -0.0457 117  ARG B O   
9751  C CB  . ARG B 119  ? 0.5278 0.5342 0.3670 0.0279  0.0027  -0.0363 117  ARG B CB  
9752  C CG  . ARG B 119  ? 0.4638 0.4776 0.3111 0.0290  0.0060  -0.0363 117  ARG B CG  
9753  C CD  . ARG B 119  ? 0.4757 0.4983 0.3265 0.0259  0.0094  -0.0326 117  ARG B CD  
9754  N NE  . ARG B 119  ? 0.5060 0.5258 0.3582 0.0211  0.0070  -0.0294 117  ARG B NE  
9755  C CZ  . ARG B 119  ? 0.5634 0.5858 0.4116 0.0181  0.0083  -0.0263 117  ARG B CZ  
9756  N NH1 . ARG B 119  ? 0.4939 0.5225 0.3368 0.0190  0.0123  -0.0258 117  ARG B NH1 
9757  N NH2 . ARG B 119  ? 0.5855 0.6041 0.4347 0.0140  0.0055  -0.0237 117  ARG B NH2 
9758  N N   . ASP B 120  ? 0.5408 0.5442 0.3609 0.0368  0.0053  -0.0427 118  ASP B N   
9759  C CA  . ASP B 120  ? 0.5361 0.5423 0.3504 0.0417  0.0088  -0.0454 118  ASP B CA  
9760  C C   . ASP B 120  ? 0.5587 0.5557 0.3678 0.0455  0.0057  -0.0499 118  ASP B C   
9761  O O   . ASP B 120  ? 0.5588 0.5569 0.3666 0.0501  0.0077  -0.0528 118  ASP B O   
9762  C CB  . ASP B 120  ? 0.5675 0.5782 0.3734 0.0415  0.0119  -0.0439 118  ASP B CB  
9763  C CG  . ASP B 120  ? 0.6328 0.6538 0.4439 0.0382  0.0158  -0.0398 118  ASP B CG  
9764  O OD1 . ASP B 120  ? 0.6508 0.6762 0.4716 0.0370  0.0166  -0.0386 118  ASP B OD1 
9765  O OD2 . ASP B 120  ? 0.6730 0.6976 0.4781 0.0367  0.0180  -0.0376 118  ASP B OD2 
9766  N N   . ALA B 121  ? 0.5741 0.5619 0.3801 0.0437  0.0006  -0.0504 119  ALA B N   
9767  C CA  . ALA B 121  ? 0.6228 0.6014 0.4243 0.0467  -0.0029 -0.0545 119  ALA B CA  
9768  C C   . ALA B 121  ? 0.5695 0.5467 0.3796 0.0479  -0.0039 -0.0560 119  ALA B C   
9769  O O   . ALA B 121  ? 0.5773 0.5514 0.3848 0.0520  -0.0038 -0.0595 119  ALA B O   
9770  C CB  . ALA B 121  ? 0.6132 0.5832 0.4104 0.0440  -0.0082 -0.0544 119  ALA B CB  
9771  N N   . LEU B 122  ? 0.5426 0.5218 0.3626 0.0442  -0.0051 -0.0535 120  LEU B N   
9772  C CA  . LEU B 122  ? 0.5542 0.5326 0.3825 0.0450  -0.0059 -0.0546 120  LEU B CA  
9773  C C   . LEU B 122  ? 0.5153 0.5005 0.3457 0.0489  -0.0012 -0.0556 120  LEU B C   
9774  O O   . LEU B 122  ? 0.5505 0.5326 0.3823 0.0520  -0.0017 -0.0583 120  LEU B O   
9775  C CB  . LEU B 122  ? 0.5253 0.5057 0.3635 0.0405  -0.0074 -0.0514 120  LEU B CB  
9776  C CG  . LEU B 122  ? 0.5594 0.5384 0.4064 0.0407  -0.0087 -0.0521 120  LEU B CG  
9777  C CD1 . LEU B 122  ? 0.5542 0.5232 0.3991 0.0410  -0.0137 -0.0547 120  LEU B CD1 
9778  C CD2 . LEU B 122  ? 0.5153 0.4986 0.3718 0.0366  -0.0088 -0.0487 120  LEU B CD2 
9779  N N   . ILE B 123  ? 0.4899 0.4843 0.3204 0.0486  0.0032  -0.0534 121  ILE B N   
9780  C CA  . ILE B 123  ? 0.4921 0.4943 0.3247 0.0523  0.0079  -0.0541 121  ILE B CA  
9781  C C   . ILE B 123  ? 0.5902 0.5887 0.4143 0.0580  0.0086  -0.0582 121  ILE B C   
9782  O O   . ILE B 123  ? 0.5709 0.5686 0.3970 0.0618  0.0092  -0.0606 121  ILE B O   
9783  C CB  . ILE B 123  ? 0.4675 0.4807 0.3013 0.0505  0.0124  -0.0508 121  ILE B CB  
9784  C CG1 . ILE B 123  ? 0.4259 0.4427 0.2689 0.0453  0.0118  -0.0470 121  ILE B CG1 
9785  C CG2 . ILE B 123  ? 0.4921 0.5138 0.3265 0.0549  0.0173  -0.0518 121  ILE B CG2 
9786  C CD1 . ILE B 123  ? 0.4006 0.4268 0.2443 0.0426  0.0155  -0.0434 121  ILE B CD1 
9787  N N   . ARG B 124  ? 0.5565 0.5521 0.3705 0.0588  0.0084  -0.0591 122  ARG B N   
9788  C CA  . ARG B 124  ? 0.5846 0.5770 0.3894 0.0645  0.0096  -0.0630 122  ARG B CA  
9789  C C   . ARG B 124  ? 0.6431 0.6238 0.4454 0.0665  0.0050  -0.0667 122  ARG B C   
9790  O O   . ARG B 124  ? 0.7139 0.6922 0.5131 0.0715  0.0059  -0.0700 122  ARG B O   
9791  C CB  . ARG B 124  ? 0.6476 0.6401 0.4418 0.0646  0.0107  -0.0629 122  ARG B CB  
9792  N N   . ASP B 125  ? 0.6497 0.6229 0.4534 0.0625  0.0000  -0.0661 123  ASP B N   
9793  C CA  . ASP B 125  ? 0.6970 0.6587 0.4973 0.0637  -0.0047 -0.0695 123  ASP B CA  
9794  C C   . ASP B 125  ? 0.6959 0.6552 0.5056 0.0629  -0.0067 -0.0696 123  ASP B C   
9795  O O   . ASP B 125  ? 0.7088 0.6601 0.5160 0.0653  -0.0093 -0.0728 123  ASP B O   
9796  C CB  . ASP B 125  ? 0.7680 0.7224 0.5636 0.0601  -0.0094 -0.0691 123  ASP B CB  
9797  C CG  . ASP B 125  ? 0.8107 0.7669 0.5967 0.0605  -0.0077 -0.0686 123  ASP B CG  
9798  O OD1 . ASP B 125  ? 0.7925 0.7525 0.5726 0.0647  -0.0037 -0.0701 123  ASP B OD1 
9799  O OD2 . ASP B 125  ? 0.8778 0.8317 0.6619 0.0566  -0.0104 -0.0667 123  ASP B OD2 
9800  N N   . LYS B 126  ? 0.6467 0.6125 0.4668 0.0595  -0.0058 -0.0663 124  LYS B N   
9801  C CA  . LYS B 126  ? 0.6241 0.5875 0.4530 0.0583  -0.0079 -0.0662 124  LYS B CA  
9802  C C   . LYS B 126  ? 0.6320 0.6040 0.4691 0.0596  -0.0040 -0.0649 124  LYS B C   
9803  O O   . LYS B 126  ? 0.6729 0.6424 0.5136 0.0616  -0.0046 -0.0664 124  LYS B O   
9804  C CB  . LYS B 126  ? 0.6450 0.6061 0.4793 0.0527  -0.0117 -0.0637 124  LYS B CB  
9805  N N   . ILE B 127  ? 0.5822 0.5642 0.4223 0.0583  -0.0002 -0.0620 125  ILE B N   
9806  C CA  . ILE B 127  ? 0.5496 0.5402 0.3984 0.0588  0.0031  -0.0604 125  ILE B CA  
9807  C C   . ILE B 127  ? 0.5734 0.5680 0.4190 0.0646  0.0069  -0.0627 125  ILE B C   
9808  O O   . ILE B 127  ? 0.5769 0.5730 0.4276 0.0669  0.0078  -0.0634 125  ILE B O   
9809  C CB  . ILE B 127  ? 0.4861 0.4856 0.3401 0.0545  0.0053  -0.0563 125  ILE B CB  
9810  C CG1 . ILE B 127  ? 0.5210 0.5158 0.3770 0.0493  0.0014  -0.0543 125  ILE B CG1 
9811  C CG2 . ILE B 127  ? 0.5015 0.5088 0.3651 0.0545  0.0079  -0.0547 125  ILE B CG2 
9812  C CD1 . ILE B 127  ? 0.5579 0.5473 0.4206 0.0477  -0.0022 -0.0546 125  ILE B CD1 
9813  N N   . ALA B 128  ? 0.5398 0.5364 0.3770 0.0671  0.0093  -0.0637 126  ALA B N   
9814  C CA  . ALA B 128  ? 0.5404 0.5424 0.3748 0.0729  0.0134  -0.0656 126  ALA B CA  
9815  C C   . ALA B 128  ? 0.6086 0.6021 0.4397 0.0777  0.0115  -0.0696 126  ALA B C   
9816  O O   . ALA B 128  ? 0.6112 0.6087 0.4431 0.0825  0.0144  -0.0711 126  ALA B O   
9817  C CB  . ALA B 128  ? 0.5314 0.5370 0.3568 0.0745  0.0163  -0.0658 126  ALA B CB  
9818  N N   . ASP B 129  ? 0.6247 0.6065 0.4522 0.0766  0.0067  -0.0715 127  ASP B N   
9819  C CA  . ASP B 129  ? 0.7354 0.7078 0.5599 0.0805  0.0043  -0.0751 127  ASP B CA  
9820  C C   . ASP B 129  ? 0.7704 0.7406 0.6043 0.0784  0.0021  -0.0742 127  ASP B C   
9821  O O   . ASP B 129  ? 0.8658 0.8257 0.6983 0.0780  -0.0021 -0.0761 127  ASP B O   
9822  C CB  . ASP B 129  ? 0.7451 0.7058 0.5599 0.0804  0.0002  -0.0778 127  ASP B CB  
9823  N N   . GLY B 130  ? 0.7997 0.7794 0.6429 0.0769  0.0047  -0.0714 128  GLY B N   
9824  C CA  . GLY B 130  ? 0.8036 0.7821 0.6559 0.0746  0.0029  -0.0701 128  GLY B CA  
9825  C C   . GLY B 130  ? 0.8664 0.8386 0.7210 0.0691  -0.0016 -0.0688 128  GLY B C   
9826  O O   . GLY B 130  ? 0.8940 0.8656 0.7453 0.0661  -0.0027 -0.0678 128  GLY B O   
9827  N N   . ASN B 131  ? 0.8720 0.8394 0.7322 0.0678  -0.0043 -0.0689 129  ASN B N   
9828  C CA  . ASN B 131  ? 0.8481 0.8094 0.7111 0.0628  -0.0087 -0.0679 129  ASN B CA  
9829  C C   . ASN B 131  ? 0.7954 0.7630 0.6631 0.0579  -0.0083 -0.0643 129  ASN B C   
9830  O O   . ASN B 131  ? 0.7920 0.7553 0.6594 0.0542  -0.0116 -0.0635 129  ASN B O   
9831  C CB  . ASN B 131  ? 0.8945 0.8449 0.7489 0.0632  -0.0127 -0.0706 129  ASN B CB  
9832  N N   . TRP B 132  ? 0.7120 0.6900 0.5842 0.0579  -0.0042 -0.0620 130  TRP B N   
9833  C CA  . TRP B 132  ? 0.6031 0.5870 0.4802 0.0532  -0.0037 -0.0585 130  TRP B CA  
9834  C C   . TRP B 132  ? 0.6389 0.6202 0.5238 0.0492  -0.0067 -0.0569 130  TRP B C   
9835  O O   . TRP B 132  ? 0.6861 0.6690 0.5737 0.0451  -0.0077 -0.0544 130  TRP B O   
9836  C CB  . TRP B 132  ? 0.5373 0.5325 0.4185 0.0539  0.0011  -0.0565 130  TRP B CB  
9837  C CG  . TRP B 132  ? 0.4482 0.4464 0.3363 0.0558  0.0024  -0.0566 130  TRP B CG  
9838  C CD1 . TRP B 132  ? 0.4514 0.4508 0.3378 0.0608  0.0044  -0.0587 130  TRP B CD1 
9839  C CD2 . TRP B 132  ? 0.4308 0.4310 0.3281 0.0527  0.0016  -0.0544 130  TRP B CD2 
9840  N NE1 . TRP B 132  ? 0.4317 0.4336 0.3258 0.0610  0.0049  -0.0579 130  TRP B NE1 
9841  C CE2 . TRP B 132  ? 0.3920 0.3946 0.2928 0.0560  0.0032  -0.0553 130  TRP B CE2 
9842  C CE3 . TRP B 132  ? 0.4298 0.4300 0.3325 0.0477  -0.0003 -0.0519 130  TRP B CE3 
9843  C CZ2 . TRP B 132  ? 0.3665 0.3712 0.2757 0.0543  0.0029  -0.0537 130  TRP B CZ2 
9844  C CZ3 . TRP B 132  ? 0.3811 0.3836 0.2922 0.0462  -0.0004 -0.0505 130  TRP B CZ3 
9845  C CH2 . TRP B 132  ? 0.3853 0.3901 0.2995 0.0493  0.0012  -0.0513 130  TRP B CH2 
9846  N N   . LYS B 133  ? 0.6451 0.6225 0.5336 0.0503  -0.0081 -0.0581 131  LYS B N   
9847  C CA  . LYS B 133  ? 0.6549 0.6303 0.5509 0.0467  -0.0107 -0.0565 131  LYS B CA  
9848  C C   . LYS B 133  ? 0.7831 0.7514 0.6767 0.0437  -0.0151 -0.0567 131  LYS B C   
9849  O O   . LYS B 133  ? 0.7889 0.7584 0.6873 0.0398  -0.0165 -0.0544 131  LYS B O   
9850  C CB  . LYS B 133  ? 0.6376 0.6100 0.5370 0.0488  -0.0112 -0.0578 131  LYS B CB  
9851  N N   . SER B 134  ? 0.8291 0.7897 0.7150 0.0456  -0.0173 -0.0595 132  SER B N   
9852  C CA  . SER B 134  ? 0.8156 0.7694 0.6986 0.0429  -0.0216 -0.0599 132  SER B CA  
9853  C C   . SER B 134  ? 0.8312 0.7877 0.7099 0.0414  -0.0212 -0.0586 132  SER B C   
9854  O O   . SER B 134  ? 0.9115 0.8630 0.7822 0.0421  -0.0230 -0.0603 132  SER B O   
9855  C CB  . SER B 134  ? 0.7826 0.7271 0.6584 0.0453  -0.0243 -0.0634 132  SER B CB  
9856  N N   . HIS B 135  ? 0.7964 0.7606 0.6802 0.0393  -0.0189 -0.0556 133  HIS B N   
9857  C CA  . HIS B 135  ? 0.8089 0.7766 0.6898 0.0374  -0.0180 -0.0537 133  HIS B CA  
9858  C C   . HIS B 135  ? 0.8373 0.8132 0.7259 0.0353  -0.0153 -0.0505 133  HIS B C   
9859  O O   . HIS B 135  ? 0.8337 0.8134 0.7280 0.0362  -0.0133 -0.0502 133  HIS B O   
9860  C CB  . HIS B 135  ? 0.7579 0.7268 0.6298 0.0405  -0.0155 -0.0551 133  HIS B CB  
9861  N N   . LEU B 136  ? 0.8416 0.8198 0.7299 0.0323  -0.0155 -0.0480 134  LEU B N   
9862  C CA  . LEU B 136  ? 0.8001 0.7854 0.6949 0.0299  -0.0132 -0.0449 134  LEU B CA  
9863  C C   . LEU B 136  ? 0.7727 0.7580 0.6766 0.0282  -0.0145 -0.0440 134  LEU B C   
9864  O O   . LEU B 136  ? 0.7088 0.6975 0.6174 0.0295  -0.0125 -0.0442 134  LEU B O   
9865  C CB  . LEU B 136  ? 0.6769 0.6698 0.5713 0.0319  -0.0084 -0.0445 134  LEU B CB  
9866  C CG  . LEU B 136  ? 0.6362 0.6300 0.5215 0.0339  -0.0066 -0.0454 134  LEU B CG  
9867  C CD1 . LEU B 136  ? 0.5795 0.5817 0.4652 0.0361  -0.0018 -0.0451 134  LEU B CD1 
9868  C CD2 . LEU B 136  ? 0.6372 0.6305 0.5189 0.0307  -0.0077 -0.0433 134  LEU B CD2 
9869  N N   . ARG B 140  ? 0.5511 0.5397 0.4905 0.0195  -0.0187 -0.0381 138  ARG B N   
9870  C CA  . ARG B 140  ? 0.5721 0.5673 0.5149 0.0191  -0.0154 -0.0364 138  ARG B CA  
9871  C C   . ARG B 140  ? 0.5565 0.5550 0.4964 0.0220  -0.0122 -0.0376 138  ARG B C   
9872  O O   . ARG B 140  ? 0.4713 0.4688 0.4046 0.0236  -0.0118 -0.0388 138  ARG B O   
9873  C CB  . ARG B 140  ? 0.5588 0.5563 0.5006 0.0166  -0.0150 -0.0341 138  ARG B CB  
9874  N N   . SER B 141  ? 0.4681 0.4708 0.4128 0.0228  -0.0100 -0.0373 139  SER B N   
9875  C CA  . SER B 141  ? 0.3930 0.3996 0.3358 0.0258  -0.0070 -0.0384 139  SER B CA  
9876  C C   . SER B 141  ? 0.4062 0.4174 0.3445 0.0257  -0.0046 -0.0374 139  SER B C   
9877  O O   . SER B 141  ? 0.4050 0.4190 0.3444 0.0228  -0.0043 -0.0352 139  SER B O   
9878  C CB  . SER B 141  ? 0.3961 0.4075 0.3454 0.0261  -0.0051 -0.0376 139  SER B CB  
9879  O OG  . SER B 141  ? 0.3930 0.4093 0.3409 0.0290  -0.0021 -0.0383 139  SER B OG  
9880  N N   . LEU B 142  ? 0.3639 0.3758 0.2969 0.0289  -0.0030 -0.0392 140  LEU B N   
9881  C CA  . LEU B 142  ? 0.3466 0.3642 0.2758 0.0291  -0.0001 -0.0383 140  LEU B CA  
9882  C C   . LEU B 142  ? 0.2947 0.3207 0.2293 0.0278  0.0028  -0.0361 140  LEU B C   
9883  O O   . LEU B 142  ? 0.3033 0.3346 0.2363 0.0263  0.0048  -0.0344 140  LEU B O   
9884  C CB  . LEU B 142  ? 0.3304 0.3481 0.2541 0.0335  0.0015  -0.0408 140  LEU B CB  
9885  C CG  . LEU B 142  ? 0.4018 0.4216 0.3183 0.0340  0.0032  -0.0408 140  LEU B CG  
9886  C CD1 . LEU B 142  ? 0.4544 0.4667 0.3657 0.0326  -0.0001 -0.0413 140  LEU B CD1 
9887  C CD2 . LEU B 142  ? 0.4035 0.4254 0.3159 0.0387  0.0056  -0.0431 140  LEU B CD2 
9888  N N   . PHE B 143  ? 0.2950 0.3224 0.2359 0.0281  0.0029  -0.0361 141  PHE B N   
9889  C CA  . PHE B 143  ? 0.2725 0.3081 0.2182 0.0278  0.0057  -0.0345 141  PHE B CA  
9890  C C   . PHE B 143  ? 0.3131 0.3499 0.2646 0.0238  0.0049  -0.0321 141  PHE B C   
9891  O O   . PHE B 143  ? 0.2872 0.3296 0.2436 0.0232  0.0066  -0.0310 141  PHE B O   
9892  C CB  . PHE B 143  ? 0.2823 0.3192 0.2303 0.0315  0.0067  -0.0363 141  PHE B CB  
9893  C CG  . PHE B 143  ? 0.2755 0.3103 0.2175 0.0358  0.0073  -0.0389 141  PHE B CG  
9894  C CD1 . PHE B 143  ? 0.2793 0.3190 0.2167 0.0372  0.0100  -0.0389 141  PHE B CD1 
9895  C CD2 . PHE B 143  ? 0.2662 0.2939 0.2067 0.0385  0.0053  -0.0414 141  PHE B CD2 
9896  C CE1 . PHE B 143  ? 0.2739 0.3115 0.2052 0.0414  0.0106  -0.0415 141  PHE B CE1 
9897  C CE2 . PHE B 143  ? 0.2736 0.2986 0.2079 0.0425  0.0058  -0.0439 141  PHE B CE2 
9898  C CZ  . PHE B 143  ? 0.2655 0.2956 0.1952 0.0442  0.0085  -0.0441 141  PHE B CZ  
9899  N N   . VAL B 144  ? 0.3045 0.3361 0.2552 0.0210  0.0023  -0.0313 142  VAL B N   
9900  C CA  . VAL B 144  ? 0.3078 0.3396 0.2633 0.0175  0.0013  -0.0292 142  VAL B CA  
9901  C C   . VAL B 144  ? 0.3079 0.3470 0.2652 0.0153  0.0039  -0.0269 142  VAL B C   
9902  O O   . VAL B 144  ? 0.2913 0.3327 0.2538 0.0136  0.0041  -0.0256 142  VAL B O   
9903  C CB  . VAL B 144  ? 0.3144 0.3399 0.2677 0.0153  -0.0017 -0.0286 142  VAL B CB  
9904  C CG1 . VAL B 144  ? 0.3660 0.3918 0.3233 0.0118  -0.0025 -0.0263 142  VAL B CG1 
9905  C CG2 . VAL B 144  ? 0.3691 0.3879 0.3224 0.0169  -0.0045 -0.0307 142  VAL B CG2 
9906  N N   . ASN B 145  ? 0.3114 0.3543 0.2643 0.0152  0.0058  -0.0263 143  ASN B N   
9907  C CA  . ASN B 145  ? 0.3085 0.3586 0.2627 0.0127  0.0082  -0.0239 143  ASN B CA  
9908  C C   . ASN B 145  ? 0.3024 0.3605 0.2578 0.0151  0.0115  -0.0243 143  ASN B C   
9909  O O   . ASN B 145  ? 0.3085 0.3735 0.2636 0.0135  0.0138  -0.0226 143  ASN B O   
9910  C CB  . ASN B 145  ? 0.3621 0.4115 0.3109 0.0102  0.0082  -0.0222 143  ASN B CB  
9911  C CG  . ASN B 145  ? 0.4189 0.4622 0.3680 0.0070  0.0053  -0.0209 143  ASN B CG  
9912  O OD1 . ASN B 145  ? 0.4473 0.4902 0.4013 0.0051  0.0045  -0.0198 143  ASN B OD1 
9913  N ND2 . ASN B 145  ? 0.4602 0.4984 0.4038 0.0066  0.0037  -0.0209 143  ASN B ND2 
9914  N N   . ALA B 146  ? 0.2747 0.3323 0.2315 0.0190  0.0116  -0.0266 144  ALA B N   
9915  C CA  . ALA B 146  ? 0.2866 0.3518 0.2441 0.0220  0.0146  -0.0273 144  ALA B CA  
9916  C C   . ALA B 146  ? 0.2803 0.3535 0.2437 0.0201  0.0164  -0.0253 144  ALA B C   
9917  O O   . ALA B 146  ? 0.3200 0.4015 0.2838 0.0214  0.0192  -0.0250 144  ALA B O   
9918  C CB  . ALA B 146  ? 0.2851 0.3468 0.2424 0.0266  0.0140  -0.0301 144  ALA B CB  
9919  N N   . ALA B 147  ? 0.3021 0.3732 0.2700 0.0172  0.0147  -0.0241 145  ALA B N   
9920  C CA  . ALA B 147  ? 0.2645 0.3430 0.2375 0.0151  0.0162  -0.0222 145  ALA B CA  
9921  C C   . ALA B 147  ? 0.3127 0.3970 0.2838 0.0117  0.0179  -0.0198 145  ALA B C   
9922  O O   . ALA B 147  ? 0.3285 0.4217 0.3022 0.0113  0.0203  -0.0187 145  ALA B O   
9923  C CB  . ALA B 147  ? 0.3106 0.3850 0.2879 0.0125  0.0139  -0.0214 145  ALA B CB  
9924  N N   . THR B 148  ? 0.3006 0.3801 0.2674 0.0094  0.0168  -0.0190 146  THR B N   
9925  C CA  . THR B 148  ? 0.2942 0.3783 0.2584 0.0060  0.0184  -0.0166 146  THR B CA  
9926  C C   . THR B 148  ? 0.3007 0.3917 0.2617 0.0087  0.0215  -0.0172 146  THR B C   
9927  O O   . THR B 148  ? 0.3256 0.4254 0.2878 0.0071  0.0240  -0.0155 146  THR B O   
9928  C CB  . THR B 148  ? 0.4139 0.4903 0.3735 0.0033  0.0161  -0.0157 146  THR B CB  
9929  O OG1 . THR B 148  ? 0.4463 0.5172 0.4093 0.0010  0.0135  -0.0151 146  THR B OG1 
9930  C CG2 . THR B 148  ? 0.4742 0.5547 0.4305 -0.0002 0.0177  -0.0131 146  THR B CG2 
9931  N N   . TRP B 149  ? 0.2940 0.3811 0.2509 0.0128  0.0213  -0.0197 147  TRP B N   
9932  C CA  . TRP B 149  ? 0.2846 0.3781 0.2383 0.0160  0.0243  -0.0206 147  TRP B CA  
9933  C C   . TRP B 149  ? 0.2755 0.3775 0.2342 0.0188  0.0265  -0.0211 147  TRP B C   
9934  O O   . TRP B 149  ? 0.2843 0.3952 0.2423 0.0199  0.0297  -0.0206 147  TRP B O   
9935  C CB  . TRP B 149  ? 0.3051 0.3917 0.2527 0.0199  0.0233  -0.0233 147  TRP B CB  
9936  C CG  . TRP B 149  ? 0.2925 0.3725 0.2345 0.0174  0.0216  -0.0226 147  TRP B CG  
9937  C CD1 . TRP B 149  ? 0.3138 0.3839 0.2540 0.0171  0.0181  -0.0236 147  TRP B CD1 
9938  C CD2 . TRP B 149  ? 0.3196 0.4027 0.2571 0.0147  0.0231  -0.0205 147  TRP B CD2 
9939  N NE1 . TRP B 149  ? 0.3491 0.4157 0.2839 0.0147  0.0173  -0.0224 147  TRP B NE1 
9940  C CE2 . TRP B 149  ? 0.3459 0.4201 0.2787 0.0131  0.0202  -0.0205 147  TRP B CE2 
9941  C CE3 . TRP B 149  ? 0.3538 0.4466 0.2907 0.0134  0.0265  -0.0186 147  TRP B CE3 
9942  C CZ2 . TRP B 149  ? 0.3748 0.4488 0.3020 0.0104  0.0207  -0.0186 147  TRP B CZ2 
9943  C CZ3 . TRP B 149  ? 0.3771 0.4699 0.3086 0.0105  0.0271  -0.0167 147  TRP B CZ3 
9944  C CH2 . TRP B 149  ? 0.4130 0.4961 0.3394 0.0090  0.0241  -0.0167 147  TRP B CH2 
9945  N N   . GLY B 150  ? 0.2863 0.3860 0.2499 0.0200  0.0250  -0.0221 148  GLY B N   
9946  C CA  . GLY B 150  ? 0.3073 0.4151 0.2759 0.0223  0.0269  -0.0223 148  GLY B CA  
9947  C C   . GLY B 150  ? 0.2796 0.3972 0.2519 0.0185  0.0288  -0.0194 148  GLY B C   
9948  O O   . GLY B 150  ? 0.2934 0.4209 0.2676 0.0202  0.0316  -0.0191 148  GLY B O   
9949  N N   . LEU B 151  ? 0.2957 0.4108 0.2691 0.0131  0.0273  -0.0172 149  LEU B N   
9950  C CA  A LEU B 151  ? 0.3387 0.4622 0.3149 0.0088  0.0288  -0.0142 149  LEU B CA  
9951  C CA  B LEU B 151  ? 0.3386 0.4622 0.3148 0.0088  0.0288  -0.0142 149  LEU B CA  
9952  C C   . LEU B 151  ? 0.3303 0.4606 0.3025 0.0083  0.0317  -0.0131 149  LEU B C   
9953  O O   . LEU B 151  ? 0.3620 0.5032 0.3370 0.0075  0.0343  -0.0116 149  LEU B O   
9954  C CB  A LEU B 151  ? 0.3562 0.4739 0.3329 0.0033  0.0264  -0.0122 149  LEU B CB  
9955  C CB  B LEU B 151  ? 0.3562 0.4738 0.3330 0.0033  0.0264  -0.0123 149  LEU B CB  
9956  C CG  A LEU B 151  ? 0.3764 0.4961 0.3593 0.0007  0.0254  -0.0111 149  LEU B CG  
9957  C CG  B LEU B 151  ? 0.3731 0.4974 0.3533 -0.0018 0.0271  -0.0093 149  LEU B CG  
9958  C CD1 A LEU B 151  ? 0.4234 0.5360 0.4055 -0.0043 0.0229  -0.0094 149  LEU B CD1 
9959  C CD1 B LEU B 151  ? 0.3743 0.5057 0.3611 -0.0006 0.0278  -0.0095 149  LEU B CD1 
9960  C CD2 A LEU B 151  ? 0.3746 0.5066 0.3611 -0.0007 0.0280  -0.0094 149  LEU B CD2 
9961  C CD2 B LEU B 151  ? 0.4237 0.5400 0.4033 -0.0065 0.0243  -0.0078 149  LEU B CD2 
9962  N N   . VAL B 152  ? 0.3285 0.4530 0.2942 0.0089  0.0314  -0.0138 150  VAL B N   
9963  C CA  . VAL B 152  ? 0.3335 0.4638 0.2947 0.0086  0.0341  -0.0128 150  VAL B CA  
9964  C C   . VAL B 152  ? 0.3349 0.4740 0.2966 0.0139  0.0373  -0.0144 150  VAL B C   
9965  O O   . VAL B 152  ? 0.3584 0.5079 0.3205 0.0131  0.0404  -0.0128 150  VAL B O   
9966  C CB  . VAL B 152  ? 0.3248 0.4459 0.2784 0.0087  0.0327  -0.0135 150  VAL B CB  
9967  C CG1 . VAL B 152  ? 0.3805 0.5075 0.3287 0.0094  0.0358  -0.0129 150  VAL B CG1 
9968  C CG2 . VAL B 152  ? 0.3729 0.4868 0.3258 0.0033  0.0299  -0.0114 150  VAL B CG2 
9969  N N   . VAL B 153  ? 0.3194 0.4543 0.2812 0.0192  0.0365  -0.0175 151  VAL B N   
9970  C CA  . VAL B 153  ? 0.2915 0.4329 0.2526 0.0250  0.0392  -0.0195 151  VAL B CA  
9971  C C   . VAL B 153  ? 0.3433 0.4948 0.3116 0.0262  0.0407  -0.0190 151  VAL B C   
9972  O O   . VAL B 153  ? 0.3460 0.5082 0.3151 0.0285  0.0440  -0.0188 151  VAL B O   
9973  C CB  . VAL B 153  ? 0.3141 0.4457 0.2713 0.0303  0.0374  -0.0231 151  VAL B CB  
9974  C CG1 . VAL B 153  ? 0.3256 0.4629 0.2825 0.0368  0.0398  -0.0254 151  VAL B CG1 
9975  C CG2 . VAL B 153  ? 0.2910 0.4143 0.2405 0.0294  0.0362  -0.0236 151  VAL B CG2 
9976  N N   . THR B 154  ? 0.3302 0.4788 0.3039 0.0249  0.0385  -0.0188 152  THR B N   
9977  C CA  . THR B 154  ? 0.3347 0.4914 0.3150 0.0266  0.0394  -0.0187 152  THR B CA  
9978  C C   . THR B 154  ? 0.3859 0.5487 0.3718 0.0208  0.0392  -0.0156 152  THR B C   
9979  O O   . THR B 154  ? 0.4079 0.5797 0.3993 0.0217  0.0404  -0.0150 152  THR B O   
9980  C CB  . THR B 154  ? 0.3304 0.4794 0.3126 0.0301  0.0369  -0.0211 152  THR B CB  
9981  O OG1 . THR B 154  ? 0.3474 0.4888 0.3316 0.0257  0.0339  -0.0200 152  THR B OG1 
9982  C CG2 . THR B 154  ? 0.3581 0.4985 0.3343 0.0350  0.0363  -0.0242 152  THR B CG2 
9983  N N   . GLY B 155  ? 0.3236 0.4814 0.3081 0.0151  0.0376  -0.0136 153  GLY B N   
9984  C CA  . GLY B 155  ? 0.3609 0.5224 0.3502 0.0096  0.0369  -0.0109 153  GLY B CA  
9985  C C   . GLY B 155  ? 0.3912 0.5476 0.3849 0.0094  0.0342  -0.0116 153  GLY B C   
9986  O O   . GLY B 155  ? 0.4396 0.5989 0.4374 0.0052  0.0334  -0.0096 153  GLY B O   
9987  N N   . LYS B 156  ? 0.3583 0.5070 0.3511 0.0138  0.0327  -0.0142 154  LYS B N   
9988  C CA  . LYS B 156  ? 0.3978 0.5413 0.3945 0.0140  0.0302  -0.0150 154  LYS B CA  
9989  C C   . LYS B 156  ? 0.3627 0.4932 0.3560 0.0131  0.0274  -0.0159 154  LYS B C   
9990  O O   . LYS B 156  ? 0.3756 0.5008 0.3638 0.0151  0.0273  -0.0173 154  LYS B O   
9991  C CB  . LYS B 156  ? 0.4617 0.6073 0.4606 0.0200  0.0308  -0.0172 154  LYS B CB  
9992  N N   . LEU B 157  ? 0.3725 0.4984 0.3686 0.0101  0.0251  -0.0152 155  LEU B N   
9993  C CA  . LEU B 157  ? 0.3981 0.5125 0.3919 0.0092  0.0224  -0.0159 155  LEU B CA  
9994  C C   . LEU B 157  ? 0.4575 0.5674 0.4541 0.0124  0.0209  -0.0178 155  LEU B C   
9995  O O   . LEU B 157  ? 0.4806 0.5948 0.4818 0.0127  0.0210  -0.0175 155  LEU B O   
9996  C CB  . LEU B 157  ? 0.4168 0.5286 0.4114 0.0035  0.0208  -0.0137 155  LEU B CB  
9997  N N   . THR B 158  ? 0.4489 0.5503 0.4424 0.0148  0.0194  -0.0197 156  THR B N   
9998  C CA  . THR B 158  ? 0.4586 0.5538 0.4542 0.0168  0.0175  -0.0212 156  THR B CA  
9999  C C   . THR B 158  ? 0.4393 0.5254 0.4335 0.0141  0.0149  -0.0210 156  THR B C   
10000 O O   . THR B 158  ? 0.4691 0.5522 0.4594 0.0124  0.0145  -0.0205 156  THR B O   
10001 C CB  . THR B 158  ? 0.5038 0.5966 0.4973 0.0221  0.0178  -0.0237 156  THR B CB  
10002 O OG1 . THR B 158  ? 0.5171 0.6037 0.5052 0.0226  0.0170  -0.0247 156  THR B OG1 
10003 C CG2 . THR B 158  ? 0.5280 0.6300 0.5221 0.0253  0.0205  -0.0240 156  THR B CG2 
10004 N N   . SER B 159  ? 0.3959 0.4779 0.3933 0.0139  0.0132  -0.0213 157  SER B N   
10005 C CA  A SER B 159  ? 0.3874 0.4613 0.3840 0.0116  0.0108  -0.0211 157  SER B CA  
10006 C CA  B SER B 159  ? 0.3875 0.4614 0.3840 0.0116  0.0109  -0.0211 157  SER B CA  
10007 C C   . SER B 159  ? 0.4190 0.4857 0.4122 0.0140  0.0095  -0.0229 157  SER B C   
10008 O O   . SER B 159  ? 0.3884 0.4497 0.3793 0.0122  0.0079  -0.0227 157  SER B O   
10009 C CB  A SER B 159  ? 0.4017 0.4740 0.4027 0.0108  0.0097  -0.0208 157  SER B CB  
10010 C CB  B SER B 159  ? 0.4008 0.4731 0.4018 0.0106  0.0096  -0.0207 157  SER B CB  
10011 O OG  A SER B 159  ? 0.4148 0.4916 0.4187 0.0135  0.0107  -0.0214 157  SER B OG  
10012 O OG  B SER B 159  ? 0.3528 0.4178 0.3532 0.0087  0.0075  -0.0206 157  SER B OG  
10013 N N   . THR B 160  ? 0.3373 0.4038 0.3300 0.0180  0.0100  -0.0247 158  THR B N   
10014 C CA  . THR B 160  ? 0.2941 0.3537 0.2834 0.0202  0.0086  -0.0266 158  THR B CA  
10015 C C   . THR B 160  ? 0.2845 0.3468 0.2704 0.0239  0.0103  -0.0281 158  THR B C   
10016 O O   . THR B 160  ? 0.3156 0.3854 0.3026 0.0251  0.0126  -0.0277 158  THR B O   
10017 C CB  . THR B 160  ? 0.3188 0.3730 0.3107 0.0214  0.0068  -0.0276 158  THR B CB  
10018 O OG1 . THR B 160  ? 0.3625 0.4208 0.3574 0.0237  0.0080  -0.0279 158  THR B OG1 
10019 C CG2 . THR B 160  ? 0.3184 0.3694 0.3130 0.0180  0.0051  -0.0264 158  THR B CG2 
10020 N N   . VAL B 161  ? 0.2468 0.3029 0.2287 0.0259  0.0091  -0.0298 159  VAL B N   
10021 C CA  . VAL B 161  ? 0.2782 0.3351 0.2551 0.0289  0.0103  -0.0313 159  VAL B CA  
10022 C C   . VAL B 161  ? 0.2545 0.3070 0.2305 0.0331  0.0096  -0.0336 159  VAL B C   
10023 O O   . VAL B 161  ? 0.2346 0.2799 0.2111 0.0328  0.0072  -0.0344 159  VAL B O   
10024 C CB  . VAL B 161  ? 0.3288 0.3809 0.3007 0.0272  0.0091  -0.0314 159  VAL B CB  
10025 C CG1 . VAL B 161  ? 0.3936 0.4429 0.3596 0.0308  0.0093  -0.0336 159  VAL B CG1 
10026 C CG2 . VAL B 161  ? 0.4196 0.4769 0.3911 0.0238  0.0104  -0.0291 159  VAL B CG2 
10027 N N   . ASN B 162  ? 0.2547 0.3113 0.2293 0.0370  0.0116  -0.0348 160  ASN B N   
10028 C CA  . ASN B 162  ? 0.2382 0.2896 0.2107 0.0412  0.0108  -0.0371 160  ASN B CA  
10029 C C   . ASN B 162  ? 0.2456 0.2914 0.2113 0.0425  0.0100  -0.0389 160  ASN B C   
10030 O O   . ASN B 162  ? 0.2498 0.2987 0.2115 0.0453  0.0118  -0.0399 160  ASN B O   
10031 C CB  . ASN B 162  ? 0.2448 0.3024 0.2187 0.0452  0.0130  -0.0377 160  ASN B CB  
10032 C CG  . ASN B 162  ? 0.2542 0.3053 0.2257 0.0496  0.0119  -0.0401 160  ASN B CG  
10033 O OD1 . ASN B 162  ? 0.2562 0.2987 0.2236 0.0500  0.0098  -0.0417 160  ASN B OD1 
10034 N ND2 . ASN B 162  ? 0.2938 0.3489 0.2677 0.0529  0.0131  -0.0404 160  ASN B ND2 
10035 N N   . ASP B 163  ? 0.2369 0.2747 0.2014 0.0405  0.0071  -0.0393 161  ASP B N   
10036 C CA  . ASP B 163  ? 0.2190 0.2510 0.1770 0.0411  0.0059  -0.0408 161  ASP B CA  
10037 C C   . ASP B 163  ? 0.2371 0.2645 0.1905 0.0458  0.0056  -0.0436 161  ASP B C   
10038 O O   . ASP B 163  ? 0.2438 0.2686 0.1910 0.0474  0.0056  -0.0451 161  ASP B O   
10039 C CB  . ASP B 163  ? 0.2521 0.2774 0.2106 0.0375  0.0028  -0.0403 161  ASP B CB  
10040 C CG  . ASP B 163  ? 0.2635 0.2842 0.2262 0.0369  0.0007  -0.0404 161  ASP B CG  
10041 O OD1 . ASP B 163  ? 0.2504 0.2749 0.2181 0.0370  0.0017  -0.0394 161  ASP B OD1 
10042 O OD2 . ASP B 163  ? 0.3102 0.3234 0.2710 0.0363  -0.0020 -0.0415 161  ASP B OD2 
10043 N N   . ARG B 164  ? 0.2222 0.2481 0.1781 0.0481  0.0053  -0.0444 162  ARG B N   
10044 C CA  A ARG B 164  ? 0.2304 0.2516 0.1814 0.0530  0.0052  -0.0471 162  ARG B CA  
10045 C CA  B ARG B 164  ? 0.2305 0.2518 0.1816 0.0530  0.0052  -0.0471 162  ARG B CA  
10046 C C   . ARG B 164  ? 0.2298 0.2583 0.1785 0.0569  0.0085  -0.0478 162  ARG B C   
10047 O O   . ARG B 164  ? 0.2276 0.2531 0.1700 0.0603  0.0088  -0.0500 162  ARG B O   
10048 C CB  A ARG B 164  ? 0.2444 0.2613 0.1985 0.0543  0.0038  -0.0476 162  ARG B CB  
10049 C CB  B ARG B 164  ? 0.2439 0.2613 0.1982 0.0544  0.0039  -0.0475 162  ARG B CB  
10050 C CG  A ARG B 164  ? 0.2664 0.2754 0.2219 0.0509  0.0004  -0.0473 162  ARG B CG  
10051 C CG  B ARG B 164  ? 0.2650 0.2748 0.2212 0.0510  0.0006  -0.0472 162  ARG B CG  
10052 C CD  A ARG B 164  ? 0.3111 0.3132 0.2608 0.0501  -0.0017 -0.0488 162  ARG B CD  
10053 C CD  B ARG B 164  ? 0.3072 0.3092 0.2577 0.0503  -0.0018 -0.0487 162  ARG B CD  
10054 N NE  A ARG B 164  ? 0.3266 0.3236 0.2695 0.0545  -0.0019 -0.0516 162  ARG B NE  
10055 N NE  B ARG B 164  ? 0.2788 0.2826 0.2301 0.0461  -0.0023 -0.0472 162  ARG B NE  
10056 C CZ  A ARG B 164  ? 0.3503 0.3425 0.2866 0.0551  -0.0031 -0.0533 162  ARG B CZ  
10057 C CZ  B ARG B 164  ? 0.3381 0.3383 0.2842 0.0454  -0.0035 -0.0480 162  ARG B CZ  
10058 N NH1 A ARG B 164  ? 0.3738 0.3659 0.3093 0.0515  -0.0041 -0.0524 162  ARG B NH1 
10059 N NH1 B ARG B 164  ? 0.3617 0.3563 0.3010 0.0485  -0.0042 -0.0506 162  ARG B NH1 
10060 N NH2 A ARG B 164  ? 0.3587 0.3459 0.2888 0.0594  -0.0033 -0.0560 162  ARG B NH2 
10061 N NH2 B ARG B 164  ? 0.3379 0.3397 0.2851 0.0416  -0.0040 -0.0464 162  ARG B NH2 
10062 N N   . SER B 165  ? 0.2348 0.2729 0.1885 0.0563  0.0110  -0.0459 163  SER B N   
10063 C CA  . SER B 165  ? 0.2167 0.2634 0.1690 0.0596  0.0143  -0.0461 163  SER B CA  
10064 C C   . SER B 165  ? 0.2203 0.2688 0.1676 0.0585  0.0154  -0.0461 163  SER B C   
10065 O O   . SER B 165  ? 0.2292 0.2798 0.1716 0.0623  0.0172  -0.0476 163  SER B O   
10066 C CB  . SER B 165  ? 0.2401 0.2969 0.1993 0.0582  0.0163  -0.0437 163  SER B CB  
10067 O OG  . SER B 165  ? 0.2555 0.3220 0.2139 0.0601  0.0196  -0.0434 163  SER B OG  
10068 N N   . LEU B 166  ? 0.2313 0.2788 0.1795 0.0534  0.0142  -0.0443 164  LEU B N   
10069 C CA  . LEU B 166  ? 0.2378 0.2867 0.1812 0.0520  0.0151  -0.0439 164  LEU B CA  
10070 C C   . LEU B 166  ? 0.2501 0.2901 0.1858 0.0542  0.0133  -0.0466 164  LEU B C   
10071 O O   . LEU B 166  ? 0.2616 0.3032 0.1915 0.0560  0.0149  -0.0474 164  LEU B O   
10072 C CB  . LEU B 166  ? 0.2553 0.3046 0.2015 0.0462  0.0140  -0.0413 164  LEU B CB  
10073 C CG  . LEU B 166  ? 0.2139 0.2729 0.1663 0.0438  0.0161  -0.0386 164  LEU B CG  
10074 C CD1 . LEU B 166  ? 0.2776 0.3355 0.2328 0.0383  0.0146  -0.0363 164  LEU B CD1 
10075 C CD2 . LEU B 166  ? 0.2635 0.3318 0.2139 0.0451  0.0197  -0.0381 164  LEU B CD2 
10076 N N   . ALA B 167  ? 0.2248 0.2552 0.1601 0.0539  0.0100  -0.0478 165  ALA B N   
10077 C CA  . ALA B 167  ? 0.2357 0.2571 0.1637 0.0559  0.0079  -0.0505 165  ALA B CA  
10078 C C   . ALA B 167  ? 0.2611 0.2827 0.1843 0.0619  0.0097  -0.0531 165  ALA B C   
10079 O O   . ALA B 167  ? 0.2662 0.2855 0.1821 0.0642  0.0100  -0.0549 165  ALA B O   
10080 C CB  . ALA B 167  ? 0.2696 0.2816 0.1991 0.0543  0.0041  -0.0511 165  ALA B CB  
10081 N N   . ALA B 168  ? 0.2578 0.2822 0.1849 0.0648  0.0108  -0.0533 166  ALA B N   
10082 C CA  . ALA B 168  ? 0.2416 0.2671 0.1647 0.0709  0.0127  -0.0557 166  ALA B CA  
10083 C C   . ALA B 168  ? 0.2326 0.2676 0.1533 0.0726  0.0164  -0.0553 166  ALA B C   
10084 O O   . ALA B 168  ? 0.2709 0.3044 0.1847 0.0768  0.0175  -0.0576 166  ALA B O   
10085 C CB  . ALA B 168  ? 0.2592 0.2875 0.1881 0.0732  0.0133  -0.0554 166  ALA B CB  
10086 N N   . ALA B 169  ? 0.2441 0.2888 0.1703 0.0691  0.0185  -0.0523 167  ALA B N   
10087 C CA  . ALA B 169  ? 0.2335 0.2882 0.1581 0.0701  0.0222  -0.0515 167  ALA B CA  
10088 C C   . ALA B 169  ? 0.2680 0.3193 0.1851 0.0691  0.0219  -0.0522 167  ALA B C   
10089 O O   . ALA B 169  ? 0.2709 0.3261 0.1828 0.0724  0.0245  -0.0533 167  ALA B O   
10090 C CB  . ALA B 169  ? 0.2616 0.3263 0.1936 0.0658  0.0238  -0.0480 167  ALA B CB  
10091 N N   . LEU B 170  ? 0.2586 0.3027 0.1749 0.0646  0.0189  -0.0514 168  LEU B N   
10092 C CA  . LEU B 170  ? 0.2540 0.2946 0.1631 0.0635  0.0183  -0.0520 168  LEU B CA  
10093 C C   . LEU B 170  ? 0.2783 0.3108 0.1790 0.0683  0.0173  -0.0557 168  LEU B C   
10094 O O   . LEU B 170  ? 0.2939 0.3277 0.1877 0.0704  0.0190  -0.0567 168  LEU B O   
10095 C CB  . LEU B 170  ? 0.2912 0.3259 0.2018 0.0579  0.0149  -0.0504 168  LEU B CB  
10096 C CG  . LEU B 170  ? 0.2961 0.3278 0.1997 0.0561  0.0142  -0.0504 168  LEU B CG  
10097 C CD1 . LEU B 170  ? 0.3129 0.3545 0.2150 0.0557  0.0181  -0.0486 168  LEU B CD1 
10098 C CD2 . LEU B 170  ? 0.3238 0.3505 0.2299 0.0508  0.0109  -0.0486 168  LEU B CD2 
10099 N N   . THR B 171  ? 0.2856 0.3095 0.1865 0.0701  0.0145  -0.0576 169  THR B N   
10100 C CA  . THR B 171  ? 0.2837 0.2995 0.1766 0.0749  0.0134  -0.0613 169  THR B CA  
10101 C C   . THR B 171  ? 0.3009 0.3233 0.1907 0.0808  0.0173  -0.0628 169  THR B C   
10102 O O   . THR B 171  ? 0.3009 0.3208 0.1824 0.0842  0.0180  -0.0651 169  THR B O   
10103 C CB  . THR B 171  ? 0.3154 0.3220 0.2100 0.0756  0.0101  -0.0628 169  THR B CB  
10104 O OG1 . THR B 171  ? 0.3625 0.3629 0.2594 0.0703  0.0065  -0.0616 169  THR B OG1 
10105 C CG2 . THR B 171  ? 0.3436 0.3414 0.2298 0.0809  0.0089  -0.0666 169  THR B CG2 
10106 N N   . ARG B 172  ? 0.2978 0.3289 0.1944 0.0822  0.0198  -0.0615 170  ARG B N   
10107 C CA  . ARG B 172  ? 0.2814 0.3196 0.1759 0.0882  0.0235  -0.0628 170  ARG B CA  
10108 C C   . ARG B 172  ? 0.2944 0.3409 0.1853 0.0880  0.0268  -0.0620 170  ARG B C   
10109 O O   . ARG B 172  ? 0.3084 0.3551 0.1922 0.0930  0.0287  -0.0644 170  ARG B O   
10110 C CB  . ARG B 172  ? 0.2874 0.3342 0.1907 0.0890  0.0253  -0.0612 170  ARG B CB  
10111 C CG  . ARG B 172  ? 0.2636 0.3166 0.1653 0.0960  0.0285  -0.0630 170  ARG B CG  
10112 C CD  . ARG B 172  ? 0.2696 0.3326 0.1804 0.0964  0.0303  -0.0609 170  ARG B CD  
10113 N NE  . ARG B 172  ? 0.2469 0.3043 0.1634 0.0936  0.0272  -0.0600 170  ARG B NE  
10114 C CZ  . ARG B 172  ? 0.2364 0.2977 0.1600 0.0877  0.0266  -0.0569 170  ARG B CZ  
10115 N NH1 . ARG B 172  ? 0.2608 0.3308 0.1867 0.0837  0.0286  -0.0543 170  ARG B NH1 
10116 N NH2 . ARG B 172  ? 0.2394 0.2952 0.1675 0.0858  0.0239  -0.0563 170  ARG B NH2 
10117 N N   . LEU B 173  ? 0.2861 0.3393 0.1813 0.0824  0.0276  -0.0586 171  LEU B N   
10118 C CA  . LEU B 173  ? 0.2789 0.3405 0.1708 0.0820  0.0311  -0.0575 171  LEU B CA  
10119 C C   . LEU B 173  ? 0.3126 0.3664 0.1945 0.0824  0.0298  -0.0594 171  LEU B C   
10120 O O   . LEU B 173  ? 0.3205 0.3789 0.1965 0.0854  0.0328  -0.0602 171  LEU B O   
10121 C CB  . LEU B 173  ? 0.2909 0.3609 0.1896 0.0757  0.0321  -0.0533 171  LEU B CB  
10122 C CG  . LEU B 173  ? 0.3138 0.3779 0.2128 0.0692  0.0290  -0.0514 171  LEU B CG  
10123 C CD1 . LEU B 173  ? 0.3161 0.3811 0.2081 0.0676  0.0301  -0.0508 171  LEU B CD1 
10124 C CD2 . LEU B 173  ? 0.3085 0.3789 0.2167 0.0642  0.0292  -0.0479 171  LEU B CD2 
10125 N N   . ILE B 174  ? 0.3153 0.3577 0.1950 0.0795  0.0255  -0.0600 172  ILE B N   
10126 C CA  . ILE B 174  ? 0.2996 0.3344 0.1697 0.0798  0.0240  -0.0618 172  ILE B CA  
10127 C C   . ILE B 174  ? 0.3327 0.3617 0.1950 0.0866  0.0241  -0.0660 172  ILE B C   
10128 O O   . ILE B 174  ? 0.3581 0.3871 0.2121 0.0893  0.0257  -0.0676 172  ILE B O   
10129 C CB  . ILE B 174  ? 0.3128 0.3375 0.1830 0.0748  0.0192  -0.0613 172  ILE B CB  
10130 C CG1 . ILE B 174  ? 0.3303 0.3608 0.2068 0.0684  0.0193  -0.0572 172  ILE B CG1 
10131 C CG2 . ILE B 174  ? 0.3757 0.3915 0.2355 0.0757  0.0171  -0.0636 172  ILE B CG2 
10132 C CD1 . ILE B 174  ? 0.3465 0.3684 0.2249 0.0637  0.0148  -0.0564 172  ILE B CD1 
10133 N N   . SER B 175  ? 0.3320 0.3556 0.1965 0.0895  0.0224  -0.0679 173  SER B N   
10134 C CA  . SER B 175  ? 0.3255 0.3427 0.1824 0.0962  0.0223  -0.0719 173  SER B CA  
10135 C C   . SER B 175  ? 0.3413 0.3689 0.1964 0.1017  0.0274  -0.0726 173  SER B C   
10136 O O   . SER B 175  ? 0.4002 0.4238 0.2489 0.1056  0.0277  -0.0747 173  SER B O   
10137 C CB  . SER B 175  ? 0.3700 0.3795 0.2301 0.0979  0.0195  -0.0734 173  SER B CB  
10138 O OG  . SER B 175  ? 0.4442 0.4438 0.3053 0.0931  0.0149  -0.0730 173  SER B OG  
10139 N N   . ARG B 176  ? 0.3333 0.3741 0.1963 0.1004  0.0307  -0.0696 174  ARG B N   
10140 C CA  . ARG B 176  ? 0.3134 0.3649 0.1775 0.1041  0.0351  -0.0691 174  ARG B CA  
10141 C C   . ARG B 176  ? 0.3520 0.4098 0.2116 0.1024  0.0379  -0.0677 174  ARG B C   
10142 O O   . ARG B 176  ? 0.3836 0.4436 0.2397 0.1058  0.0400  -0.0684 174  ARG B O   
10143 C CB  . ARG B 176  ? 0.3361 0.3992 0.2106 0.1036  0.0374  -0.0665 174  ARG B CB  
10144 C CG  . ARG B 176  ? 0.3307 0.4047 0.2085 0.1071  0.0412  -0.0655 174  ARG B CG  
10145 C CD  . ARG B 176  ? 0.3158 0.4002 0.2042 0.1063  0.0427  -0.0631 174  ARG B CD  
10146 N NE  . ARG B 176  ? 0.3334 0.4281 0.2265 0.1009  0.0446  -0.0598 174  ARG B NE  
10147 C CZ  . ARG B 176  ? 0.3368 0.4318 0.2355 0.0964  0.0431  -0.0581 174  ARG B CZ  
10148 N NH1 . ARG B 176  ? 0.3153 0.4013 0.2168 0.0962  0.0395  -0.0590 174  ARG B NH1 
10149 N NH2 . ARG B 176  ? 0.3877 0.4909 0.2908 0.0905  0.0444  -0.0545 174  ARG B NH2 
10150 N N   . CYS B 177  ? 0.3660 0.4266 0.2258 0.0972  0.0378  -0.0657 175  CYS B N   
10151 C CA  . CYS B 177  ? 0.3469 0.4154 0.2038 0.0950  0.0408  -0.0636 175  CYS B CA  
10152 C C   . CYS B 177  ? 0.3839 0.4438 0.2328 0.0918  0.0383  -0.0640 175  CYS B C   
10153 O O   . CYS B 177  ? 0.4055 0.4702 0.2493 0.0911  0.0408  -0.0630 175  CYS B O   
10154 C CB  . CYS B 177  ? 0.3599 0.4410 0.2257 0.0900  0.0432  -0.0593 175  CYS B CB  
10155 S SG  . CYS B 177  ? 0.4452 0.5378 0.3211 0.0932  0.0461  -0.0584 175  CYS B SG  
10156 N N   . GLY B 178  ? 0.3888 0.4363 0.2370 0.0894  0.0334  -0.0649 176  GLY B N   
10157 C CA  . GLY B 178  ? 0.4270 0.4653 0.2667 0.0874  0.0307  -0.0658 176  GLY B CA  
10158 C C   . GLY B 178  ? 0.3895 0.4322 0.2304 0.0810  0.0310  -0.0620 176  GLY B C   
10159 O O   . GLY B 178  ? 0.3871 0.4371 0.2363 0.0767  0.0319  -0.0585 176  GLY B O   
10160 N N   . GLU B 179  ? 0.4149 0.4524 0.2465 0.0805  0.0300  -0.0628 177  GLU B N   
10161 C CA  . GLU B 179  ? 0.4394 0.4792 0.2704 0.0746  0.0298  -0.0594 177  GLU B CA  
10162 C C   . GLU B 179  ? 0.3564 0.4103 0.1917 0.0727  0.0346  -0.0559 177  GLU B C   
10163 O O   . GLU B 179  ? 0.3796 0.4364 0.2199 0.0668  0.0340  -0.0522 177  GLU B O   
10164 C CB  . GLU B 179  ? 0.4646 0.4967 0.2841 0.0752  0.0282  -0.0612 177  GLU B CB  
10165 C CG  . GLU B 179  ? 0.4718 0.5042 0.2902 0.0691  0.0271  -0.0577 177  GLU B CG  
10166 C CD  . GLU B 179  ? 0.5971 0.6210 0.4040 0.0695  0.0249  -0.0594 177  GLU B CD  
10167 O OE1 . GLU B 179  ? 0.6506 0.6675 0.4504 0.0742  0.0238  -0.0635 177  GLU B OE1 
10168 O OE2 . GLU B 179  ? 0.7016 0.7257 0.5063 0.0650  0.0242  -0.0567 177  GLU B OE2 
10169 N N   . PRO B 180  ? 0.3636 0.4268 0.1973 0.0772  0.0393  -0.0566 178  PRO B N   
10170 C CA  . PRO B 180  ? 0.3773 0.4544 0.2151 0.0746  0.0438  -0.0529 178  PRO B CA  
10171 C C   . PRO B 180  ? 0.4050 0.4880 0.2546 0.0702  0.0436  -0.0496 178  PRO B C   
10172 O O   . PRO B 180  ? 0.4081 0.4975 0.2605 0.0649  0.0449  -0.0458 178  PRO B O   
10173 C CB  . PRO B 180  ? 0.4479 0.5330 0.2833 0.0811  0.0483  -0.0548 178  PRO B CB  
10174 C CG  . PRO B 180  ? 0.4144 0.4878 0.2413 0.0852  0.0461  -0.0587 178  PRO B CG  
10175 C CD  . PRO B 180  ? 0.3915 0.4527 0.2177 0.0846  0.0409  -0.0608 178  PRO B CD  
10176 N N   . VAL B 181  ? 0.3388 0.4194 0.1948 0.0719  0.0420  -0.0509 179  VAL B N   
10177 C CA  . VAL B 181  ? 0.3328 0.4192 0.1997 0.0677  0.0419  -0.0478 179  VAL B CA  
10178 C C   . VAL B 181  ? 0.3406 0.4196 0.2094 0.0612  0.0378  -0.0457 179  VAL B C   
10179 O O   . VAL B 181  ? 0.3518 0.4363 0.2268 0.0562  0.0383  -0.0421 179  VAL B O   
10180 C CB  . VAL B 181  ? 0.3615 0.4485 0.2349 0.0714  0.0416  -0.0495 179  VAL B CB  
10181 C CG1 . VAL B 181  ? 0.3690 0.4422 0.2411 0.0723  0.0368  -0.0522 179  VAL B CG1 
10182 C CG2 . VAL B 181  ? 0.3808 0.4763 0.2648 0.0674  0.0425  -0.0461 179  VAL B CG2 
10183 N N   . ILE B 182  ? 0.3369 0.4035 0.2004 0.0614  0.0338  -0.0478 180  ILE B N   
10184 C CA  . ILE B 182  ? 0.3683 0.4279 0.2332 0.0558  0.0299  -0.0459 180  ILE B CA  
10185 C C   . ILE B 182  ? 0.3673 0.4308 0.2290 0.0514  0.0312  -0.0427 180  ILE B C   
10186 O O   . ILE B 182  ? 0.3849 0.4495 0.2513 0.0460  0.0301  -0.0395 180  ILE B O   
10187 C CB  . ILE B 182  ? 0.3467 0.3928 0.2063 0.0571  0.0253  -0.0489 180  ILE B CB  
10188 C CG1 . ILE B 182  ? 0.3589 0.4007 0.2220 0.0609  0.0239  -0.0517 180  ILE B CG1 
10189 C CG2 . ILE B 182  ? 0.3623 0.4020 0.2235 0.0515  0.0213  -0.0469 180  ILE B CG2 
10190 C CD1 . ILE B 182  ? 0.3795 0.4089 0.2358 0.0633  0.0201  -0.0553 180  ILE B CD1 
10191 N N   . ARG B 183  ? 0.3953 0.4604 0.2483 0.0537  0.0334  -0.0436 181  ARG B N   
10192 C CA  . ARG B 183  ? 0.4304 0.4995 0.2794 0.0498  0.0350  -0.0405 181  ARG B CA  
10193 C C   . ARG B 183  ? 0.3817 0.4628 0.2379 0.0464  0.0384  -0.0367 181  ARG B C   
10194 O O   . ARG B 183  ? 0.4251 0.5071 0.2830 0.0408  0.0377  -0.0332 181  ARG B O   
10195 C CB  . ARG B 183  ? 0.4160 0.4859 0.2546 0.0538  0.0374  -0.0425 181  ARG B CB  
10196 C CG  . ARG B 183  ? 0.5175 0.5962 0.3527 0.0511  0.0412  -0.0392 181  ARG B CG  
10197 C CD  . ARG B 183  ? 0.5840 0.6556 0.4128 0.0467  0.0384  -0.0374 181  ARG B CD  
10198 N NE  . ARG B 183  ? 0.5827 0.6511 0.4180 0.0409  0.0352  -0.0345 181  ARG B NE  
10199 C CZ  . ARG B 183  ? 0.5755 0.6329 0.4101 0.0393  0.0302  -0.0352 181  ARG B CZ  
10200 N NH1 . ARG B 183  ? 0.5936 0.6417 0.4217 0.0426  0.0275  -0.0387 181  ARG B NH1 
10201 N NH2 . ARG B 183  ? 0.6088 0.6644 0.4493 0.0341  0.0278  -0.0324 181  ARG B NH2 
10202 N N   . ARG B 184  ? 0.4009 0.4914 0.2614 0.0498  0.0420  -0.0373 182  ARG B N   
10203 C CA  . ARG B 184  ? 0.4144 0.5170 0.2822 0.0465  0.0451  -0.0337 182  ARG B CA  
10204 C C   . ARG B 184  ? 0.3909 0.4912 0.2674 0.0417  0.0423  -0.0316 182  ARG B C   
10205 O O   . ARG B 184  ? 0.4034 0.5090 0.2834 0.0364  0.0430  -0.0279 182  ARG B O   
10206 C CB  . ARG B 184  ? 0.4287 0.5417 0.2999 0.0516  0.0491  -0.0351 182  ARG B CB  
10207 C CG  . ARG B 184  ? 0.5042 0.6244 0.3683 0.0550  0.0535  -0.0357 182  ARG B CG  
10208 C CD  . ARG B 184  ? 0.5254 0.6583 0.3922 0.0506  0.0573  -0.0314 182  ARG B CD  
10209 N NE  . ARG B 184  ? 0.4864 0.6318 0.3616 0.0522  0.0605  -0.0307 182  ARG B NE  
10210 C CZ  . ARG B 184  ? 0.4841 0.6370 0.3677 0.0471  0.0611  -0.0271 182  ARG B CZ  
10211 N NH1 . ARG B 184  ? 0.5188 0.6676 0.4036 0.0403  0.0587  -0.0241 182  ARG B NH1 
10212 N NH2 . ARG B 184  ? 0.5268 0.6914 0.4175 0.0491  0.0640  -0.0267 182  ARG B NH2 
10213 N N   . GLY B 185  ? 0.3970 0.4896 0.2768 0.0434  0.0389  -0.0339 183  GLY B N   
10214 C CA  . GLY B 185  ? 0.3531 0.4434 0.2409 0.0392  0.0363  -0.0320 183  GLY B CA  
10215 C C   . GLY B 185  ? 0.3667 0.4502 0.2522 0.0338  0.0332  -0.0298 183  GLY B C   
10216 O O   . GLY B 185  ? 0.3805 0.4662 0.2714 0.0289  0.0327  -0.0267 183  GLY B O   
10217 N N   . VAL B 186  ? 0.3613 0.4363 0.2387 0.0347  0.0312  -0.0313 184  VAL B N   
10218 C CA  . VAL B 186  ? 0.3747 0.4432 0.2493 0.0299  0.0282  -0.0292 184  VAL B CA  
10219 C C   . VAL B 186  ? 0.4055 0.4813 0.2788 0.0257  0.0309  -0.0253 184  VAL B C   
10220 O O   . VAL B 186  ? 0.3989 0.4737 0.2753 0.0206  0.0294  -0.0223 184  VAL B O   
10221 C CB  . VAL B 186  ? 0.4096 0.4682 0.2754 0.0321  0.0255  -0.0318 184  VAL B CB  
10222 C CG1 . VAL B 186  ? 0.4236 0.4773 0.2852 0.0275  0.0232  -0.0293 184  VAL B CG1 
10223 C CG2 . VAL B 186  ? 0.3906 0.4407 0.2587 0.0346  0.0218  -0.0349 184  VAL B CG2 
10224 N N   . ASP B 187  ? 0.3885 0.4715 0.2570 0.0278  0.0349  -0.0254 185  ASP B N   
10225 C CA  . ASP B 187  ? 0.4112 0.5019 0.2783 0.0236  0.0377  -0.0215 185  ASP B CA  
10226 C C   . ASP B 187  ? 0.4511 0.5498 0.3275 0.0200  0.0391  -0.0186 185  ASP B C   
10227 O O   . ASP B 187  ? 0.4233 0.5236 0.3006 0.0145  0.0390  -0.0150 185  ASP B O   
10228 C CB  . ASP B 187  ? 0.4333 0.5314 0.2942 0.0270  0.0421  -0.0223 185  ASP B CB  
10229 C CG  . ASP B 187  ? 0.5055 0.5954 0.3559 0.0299  0.0407  -0.0247 185  ASP B CG  
10230 O OD1 . ASP B 187  ? 0.5273 0.6069 0.3747 0.0277  0.0365  -0.0247 185  ASP B OD1 
10231 O OD2 . ASP B 187  ? 0.4951 0.5890 0.3402 0.0344  0.0437  -0.0268 185  ASP B OD2 
10232 N N   . MET B 188  ? 0.4458 0.5495 0.3291 0.0230  0.0403  -0.0203 186  MET B N   
10233 C CA  . MET B 188  ? 0.4021 0.5135 0.2944 0.0198  0.0414  -0.0178 186  MET B CA  
10234 C C   . MET B 188  ? 0.4038 0.5077 0.3003 0.0153  0.0374  -0.0162 186  MET B C   
10235 O O   . MET B 188  ? 0.4152 0.5224 0.3146 0.0100  0.0376  -0.0128 186  MET B O   
10236 C CB  . MET B 188  ? 0.4305 0.5475 0.3285 0.0246  0.0430  -0.0202 186  MET B CB  
10237 C CG  . MET B 188  ? 0.4699 0.5956 0.3772 0.0219  0.0443  -0.0179 186  MET B CG  
10238 S SD  . MET B 188  ? 0.6586 0.7979 0.5661 0.0177  0.0487  -0.0137 186  MET B SD  
10239 C CE  . MET B 188  ? 0.6074 0.7533 0.5084 0.0240  0.0529  -0.0161 186  MET B CE  
10240 N N   . ALA B 189  ? 0.3930 0.4868 0.2897 0.0172  0.0337  -0.0187 187  ALA B N   
10241 C CA  . ALA B 189  ? 0.4137 0.5005 0.3144 0.0133  0.0299  -0.0174 187  ALA B CA  
10242 C C   . ALA B 189  ? 0.4162 0.4987 0.3120 0.0086  0.0284  -0.0146 187  ALA B C   
10243 O O   . ALA B 189  ? 0.3920 0.4732 0.2913 0.0040  0.0270  -0.0120 187  ALA B O   
10244 C CB  . ALA B 189  ? 0.4297 0.5069 0.3309 0.0165  0.0263  -0.0207 187  ALA B CB  
10245 N N   . MET B 190  ? 0.4199 0.4995 0.3071 0.0098  0.0287  -0.0152 188  MET B N   
10246 C CA  . MET B 190  ? 0.4418 0.5173 0.3236 0.0056  0.0274  -0.0124 188  MET B CA  
10247 C C   . MET B 190  ? 0.4370 0.5206 0.3205 0.0007  0.0301  -0.0084 188  MET B C   
10248 O O   . MET B 190  ? 0.4412 0.5214 0.3253 -0.0041 0.0282  -0.0055 188  MET B O   
10249 C CB  . MET B 190  ? 0.4547 0.5272 0.3265 0.0081  0.0277  -0.0138 188  MET B CB  
10250 C CG  . MET B 190  ? 0.5180 0.5822 0.3836 0.0049  0.0247  -0.0121 188  MET B CG  
10251 S SD  . MET B 190  ? 0.5888 0.6510 0.4423 0.0076  0.0258  -0.0133 188  MET B SD  
10252 C CE  . MET B 190  ? 0.5159 0.5743 0.3689 0.0144  0.0248  -0.0188 188  MET B CE  
10253 N N   . ARG B 191  ? 0.4198 0.5144 0.3043 0.0020  0.0345  -0.0081 189  ARG B N   
10254 C CA  . ARG B 191  ? 0.4680 0.5714 0.3547 -0.0028 0.0372  -0.0041 189  ARG B CA  
10255 C C   . ARG B 191  ? 0.4401 0.5443 0.3355 -0.0062 0.0358  -0.0026 189  ARG B C   
10256 O O   . ARG B 191  ? 0.4402 0.5438 0.3362 -0.0117 0.0350  0.0008  189  ARG B O   
10257 C CB  . ARG B 191  ? 0.4416 0.5575 0.3283 -0.0003 0.0422  -0.0044 189  ARG B CB  
10258 N N   . MET B 192  ? 0.3837 0.4886 0.2855 -0.0029 0.0352  -0.0051 190  MET B N   
10259 C CA  . MET B 192  ? 0.3857 0.4919 0.2957 -0.0058 0.0341  -0.0039 190  MET B CA  
10260 C C   . MET B 192  ? 0.4193 0.5147 0.3290 -0.0092 0.0298  -0.0028 190  MET B C   
10261 O O   . MET B 192  ? 0.4094 0.5052 0.3217 -0.0142 0.0291  0.0001  190  MET B O   
10262 C CB  . MET B 192  ? 0.4129 0.5211 0.3290 -0.0012 0.0341  -0.0070 190  MET B CB  
10263 C CG  . MET B 192  ? 0.4511 0.5702 0.3682 0.0027  0.0383  -0.0081 190  MET B CG  
10264 S SD  . MET B 192  ? 0.5708 0.6918 0.4957 0.0073  0.0380  -0.0111 190  MET B SD  
10265 C CE  . MET B 192  ? 0.4796 0.6071 0.4129 0.0018  0.0381  -0.0078 190  MET B CE  
10266 N N   . MET B 193  ? 0.3974 0.4831 0.3040 -0.0066 0.0267  -0.0052 191  MET B N   
10267 C CA  A MET B 193  ? 0.4304 0.5060 0.3373 -0.0091 0.0226  -0.0045 191  MET B CA  
10268 C CA  B MET B 193  ? 0.4302 0.5061 0.3373 -0.0092 0.0226  -0.0044 191  MET B CA  
10269 C C   . MET B 193  ? 0.4569 0.5283 0.3573 -0.0132 0.0215  -0.0016 191  MET B C   
10270 O O   . MET B 193  ? 0.4625 0.5273 0.3637 -0.0163 0.0185  -0.0001 191  MET B O   
10271 C CB  A MET B 193  ? 0.4618 0.5291 0.3680 -0.0050 0.0196  -0.0079 191  MET B CB  
10272 C CB  B MET B 193  ? 0.4616 0.5292 0.3687 -0.0052 0.0196  -0.0078 191  MET B CB  
10273 C CG  A MET B 193  ? 0.4384 0.5087 0.3502 -0.0007 0.0203  -0.0109 191  MET B CG  
10274 C CG  B MET B 193  ? 0.4427 0.5129 0.3570 -0.0022 0.0198  -0.0102 191  MET B CG  
10275 S SD  A MET B 193  ? 0.4137 0.4741 0.3238 0.0037  0.0169  -0.0148 191  MET B SD  
10276 S SD  B MET B 193  ? 0.4497 0.5093 0.3652 0.0008  0.0156  -0.0133 191  MET B SD  
10277 C CE  A MET B 193  ? 0.5119 0.5664 0.4289 0.0013  0.0133  -0.0142 191  MET B CE  
10278 C CE  B MET B 193  ? 0.4440 0.5008 0.3512 0.0052  0.0158  -0.0160 191  MET B CE  
10279 N N   . GLY B 194  ? 0.4286 0.5035 0.3225 -0.0130 0.0239  -0.0008 192  GLY B N   
10280 C CA  . GLY B 194  ? 0.4522 0.5227 0.3392 -0.0167 0.0229  0.0020  192  GLY B CA  
10281 C C   . GLY B 194  ? 0.4465 0.5239 0.3334 -0.0218 0.0255  0.0060  192  GLY B C   
10282 O O   . GLY B 194  ? 0.4480 0.5208 0.3308 -0.0260 0.0241  0.0090  192  GLY B O   
10283 N N   . GLU B 195  ? 0.4207 0.5093 0.3119 -0.0215 0.0293  0.0062  193  GLU B N   
10284 C CA  . GLU B 195  ? 0.4338 0.5307 0.3246 -0.0262 0.0323  0.0100  193  GLU B CA  
10285 C C   . GLU B 195  ? 0.4224 0.5274 0.3217 -0.0284 0.0338  0.0111  193  GLU B C   
10286 O O   . GLU B 195  ? 0.3730 0.4824 0.2727 -0.0338 0.0350  0.0148  193  GLU B O   
10287 C CB  . GLU B 195  ? 0.4307 0.5357 0.3163 -0.0241 0.0364  0.0099  193  GLU B CB  
10288 C CG  . GLU B 195  ? 0.5466 0.6445 0.4230 -0.0216 0.0354  0.0086  193  GLU B CG  
10289 C CD  . GLU B 195  ? 0.5873 0.6933 0.4593 -0.0181 0.0395  0.0075  193  GLU B CD  
10290 O OE1 . GLU B 195  ? 0.6497 0.7668 0.5233 -0.0201 0.0435  0.0097  193  GLU B OE1 
10291 O OE2 . GLU B 195  ? 0.6548 0.7562 0.5218 -0.0134 0.0389  0.0044  193  GLU B OE2 
10292 N N   . GLN B 196  ? 0.4279 0.5351 0.3340 -0.0248 0.0336  0.0083  194  GLN B N   
10293 C CA  . GLN B 196  ? 0.4255 0.5406 0.3398 -0.0266 0.0349  0.0092  194  GLN B CA  
10294 C C   . GLN B 196  ? 0.4205 0.5281 0.3396 -0.0284 0.0311  0.0091  194  GLN B C   
10295 O O   . GLN B 196  ? 0.4777 0.5866 0.3997 -0.0334 0.0307  0.0118  194  GLN B O   
10296 C CB  . GLN B 196  ? 0.4497 0.5735 0.3683 -0.0212 0.0376  0.0064  194  GLN B CB  
10297 N N   . PHE B 197  ? 0.4317 0.5315 0.3517 -0.0245 0.0285  0.0060  195  PHE B N   
10298 C CA  . PHE B 197  ? 0.4457 0.5384 0.3702 -0.0258 0.0250  0.0057  195  PHE B CA  
10299 C C   . PHE B 197  ? 0.4415 0.5255 0.3619 -0.0303 0.0222  0.0083  195  PHE B C   
10300 O O   . PHE B 197  ? 0.4646 0.5447 0.3884 -0.0331 0.0201  0.0093  195  PHE B O   
10301 C CB  . PHE B 197  ? 0.4442 0.5307 0.3700 -0.0205 0.0230  0.0019  195  PHE B CB  
10302 C CG  . PHE B 197  ? 0.4385 0.5322 0.3685 -0.0159 0.0253  -0.0007 195  PHE B CG  
10303 C CD1 . PHE B 197  ? 0.4467 0.5508 0.3820 -0.0168 0.0279  0.0003  195  PHE B CD1 
10304 C CD2 . PHE B 197  ? 0.4551 0.5451 0.3836 -0.0106 0.0246  -0.0041 195  PHE B CD2 
10305 C CE1 . PHE B 197  ? 0.4857 0.5963 0.4247 -0.0122 0.0299  -0.0021 195  PHE B CE1 
10306 C CE2 . PHE B 197  ? 0.4798 0.5756 0.4116 -0.0061 0.0265  -0.0065 195  PHE B CE2 
10307 C CZ  . PHE B 197  ? 0.4627 0.5688 0.3998 -0.0068 0.0292  -0.0055 195  PHE B CZ  
10308 N N   . VAL B 198  ? 0.4257 0.5059 0.3385 -0.0308 0.0220  0.0092  196  VAL B N   
10309 C CA  . VAL B 198  ? 0.4082 0.4804 0.3162 -0.0351 0.0196  0.0119  196  VAL B CA  
10310 C C   . VAL B 198  ? 0.4085 0.4850 0.3101 -0.0379 0.0221  0.0147  196  VAL B C   
10311 O O   . VAL B 198  ? 0.4047 0.4879 0.3040 -0.0354 0.0251  0.0138  196  VAL B O   
10312 C CB  . VAL B 198  ? 0.3678 0.4285 0.2723 -0.0326 0.0157  0.0102  196  VAL B CB  
10313 C CG1 . VAL B 198  ? 0.4100 0.4668 0.3208 -0.0298 0.0134  0.0075  196  VAL B CG1 
10314 C CG2 . VAL B 198  ? 0.4451 0.5057 0.3437 -0.0288 0.0167  0.0084  196  VAL B CG2 
10315 N N   . THR B 199  ? 0.3814 0.4540 0.2800 -0.0433 0.0209  0.0183  197  THR B N   
10316 C CA  A THR B 199  ? 0.3728 0.4479 0.2644 -0.0465 0.0228  0.0213  197  THR B CA  
10317 C CA  B THR B 199  ? 0.3731 0.4483 0.2647 -0.0464 0.0228  0.0212  197  THR B CA  
10318 C C   . THR B 199  ? 0.4074 0.4748 0.2909 -0.0440 0.0212  0.0204  197  THR B C   
10319 O O   . THR B 199  ? 0.4314 0.5021 0.3087 -0.0446 0.0234  0.0218  197  THR B O   
10320 C CB  A THR B 199  ? 0.3828 0.4552 0.2734 -0.0532 0.0217  0.0254  197  THR B CB  
10321 C CB  B THR B 199  ? 0.3821 0.4554 0.2727 -0.0532 0.0220  0.0254  197  THR B CB  
10322 O OG1 A THR B 199  ? 0.3634 0.4421 0.2618 -0.0553 0.0226  0.0258  197  THR B OG1 
10323 O OG1 B THR B 199  ? 0.4066 0.4817 0.2898 -0.0563 0.0237  0.0285  197  THR B OG1 
10324 C CG2 A THR B 199  ? 0.4070 0.4837 0.2912 -0.0571 0.0242  0.0290  197  THR B CG2 
10325 C CG2 B THR B 199  ? 0.3429 0.4034 0.2325 -0.0542 0.0173  0.0256  197  THR B CG2 
10326 N N   . GLY B 200  ? 0.3718 0.4295 0.2554 -0.0413 0.0174  0.0183  198  GLY B N   
10327 C CA  . GLY B 200  ? 0.3952 0.4456 0.2717 -0.0388 0.0155  0.0172  198  GLY B CA  
10328 C C   . GLY B 200  ? 0.3767 0.4182 0.2560 -0.0358 0.0113  0.0145  198  GLY B C   
10329 O O   . GLY B 200  ? 0.3641 0.4039 0.2497 -0.0367 0.0098  0.0143  198  GLY B O   
10330 N N   . GLU B 201  ? 0.4259 0.4619 0.3004 -0.0324 0.0096  0.0126  199  GLU B N   
10331 C CA  . GLU B 201  ? 0.4097 0.4376 0.2866 -0.0296 0.0056  0.0101  199  GLU B CA  
10332 C C   . GLU B 201  ? 0.4214 0.4397 0.2955 -0.0324 0.0017  0.0124  199  GLU B C   
10333 O O   . GLU B 201  ? 0.4894 0.5019 0.3674 -0.0311 -0.0015 0.0111  199  GLU B O   
10334 C CB  . GLU B 201  ? 0.5018 0.5276 0.3748 -0.0249 0.0049  0.0070  199  GLU B CB  
10335 C CG  . GLU B 201  ? 0.5535 0.5865 0.4301 -0.0210 0.0078  0.0039  199  GLU B CG  
10336 C CD  . GLU B 201  ? 0.6743 0.7035 0.5472 -0.0164 0.0064  0.0006  199  GLU B CD  
10337 O OE1 . GLU B 201  ? 0.6227 0.6449 0.4893 -0.0165 0.0037  0.0010  199  GLU B OE1 
10338 O OE2 . GLU B 201  ? 0.6969 0.7299 0.5730 -0.0128 0.0079  -0.0024 199  GLU B OE2 
10339 N N   . THR B 202  ? 0.3853 0.4020 0.2527 -0.0360 0.0020  0.0157  200  THR B N   
10340 C CA  . THR B 202  ? 0.4216 0.4291 0.2857 -0.0388 -0.0016 0.0182  200  THR B CA  
10341 C C   . THR B 202  ? 0.4114 0.4214 0.2742 -0.0444 0.0002  0.0222  200  THR B C   
10342 O O   . THR B 202  ? 0.3645 0.3833 0.2271 -0.0460 0.0041  0.0233  200  THR B O   
10343 C CB  . THR B 202  ? 0.4442 0.4453 0.2996 -0.0379 -0.0037 0.0187  200  THR B CB  
10344 O OG1 . THR B 202  ? 0.4066 0.4125 0.2554 -0.0399 -0.0006 0.0208  200  THR B OG1 
10345 C CG2 . THR B 202  ? 0.4384 0.4378 0.2943 -0.0326 -0.0052 0.0147  200  THR B CG2 
10346 N N   . ILE B 203  ? 0.3757 0.3780 0.2377 -0.0473 -0.0029 0.0244  201  ILE B N   
10347 C CA  . ILE B 203  ? 0.3756 0.3788 0.2358 -0.0531 -0.0017 0.0284  201  ILE B CA  
10348 C C   . ILE B 203  ? 0.4146 0.4194 0.2661 -0.0556 0.0001  0.0312  201  ILE B C   
10349 O O   . ILE B 203  ? 0.3691 0.3803 0.2198 -0.0596 0.0032  0.0339  201  ILE B O   
10350 C CB  . ILE B 203  ? 0.3693 0.3627 0.2298 -0.0553 -0.0056 0.0300  201  ILE B CB  
10351 C CG1 . ILE B 203  ? 0.3916 0.3864 0.2514 -0.0615 -0.0044 0.0337  201  ILE B CG1 
10352 C CG2 . ILE B 203  ? 0.4171 0.4001 0.2707 -0.0543 -0.0094 0.0307  201  ILE B CG2 
10353 C CD1 . ILE B 203  ? 0.3429 0.3480 0.2103 -0.0627 -0.0011 0.0331  201  ILE B CD1 
10354 N N   . ARG B 204  ? 0.4235 0.4229 0.2684 -0.0531 -0.0017 0.0307  202  ARG B N   
10355 C CA  . ARG B 204  ? 0.4385 0.4394 0.2746 -0.0547 0.0001  0.0329  202  ARG B CA  
10356 C C   . ARG B 204  ? 0.3942 0.4075 0.2317 -0.0544 0.0053  0.0323  202  ARG B C   
10357 O O   . ARG B 204  ? 0.4255 0.4439 0.2593 -0.0584 0.0082  0.0355  202  ARG B O   
10358 C CB  . ARG B 204  ? 0.4941 0.4886 0.3247 -0.0506 -0.0026 0.0309  202  ARG B CB  
10359 C CG  . ARG B 204  ? 0.6278 0.6171 0.4480 -0.0527 -0.0036 0.0339  202  ARG B CG  
10360 C CD  . ARG B 204  ? 0.5437 0.5252 0.3598 -0.0485 -0.0074 0.0318  202  ARG B CD  
10361 N NE  . ARG B 204  ? 0.4511 0.4374 0.2680 -0.0437 -0.0059 0.0279  202  ARG B NE  
10362 C CZ  . ARG B 204  ? 0.5379 0.5298 0.3492 -0.0431 -0.0028 0.0278  202  ARG B CZ  
10363 N NH1 . ARG B 204  ? 0.5132 0.5075 0.3182 -0.0471 -0.0003 0.0315  202  ARG B NH1 
10364 N NH2 . ARG B 204  ? 0.5372 0.5319 0.3489 -0.0384 -0.0020 0.0240  202  ARG B NH2 
10365 N N   . GLU B 205  ? 0.4076 0.4258 0.2502 -0.0496 0.0065  0.0283  203  GLU B N   
10366 C CA  . GLU B 205  ? 0.4247 0.4545 0.2687 -0.0483 0.0113  0.0273  203  GLU B CA  
10367 C C   . GLU B 205  ? 0.3886 0.4270 0.2389 -0.0520 0.0142  0.0291  203  GLU B C   
10368 O O   . GLU B 205  ? 0.4160 0.4633 0.2646 -0.0541 0.0182  0.0310  203  GLU B O   
10369 C CB  . GLU B 205  ? 0.4641 0.4958 0.3122 -0.0421 0.0113  0.0224  203  GLU B CB  
10370 C CG  . GLU B 205  ? 0.4495 0.4924 0.2986 -0.0397 0.0161  0.0208  203  GLU B CG  
10371 C CD  . GLU B 205  ? 0.5756 0.6185 0.4272 -0.0334 0.0156  0.0161  203  GLU B CD  
10372 O OE1 . GLU B 205  ? 0.4919 0.5332 0.3509 -0.0317 0.0139  0.0139  203  GLU B OE1 
10373 O OE2 . GLU B 205  ? 0.6913 0.7356 0.5373 -0.0304 0.0170  0.0145  203  GLU B OE2 
10374 N N   . ALA B 206  ? 0.3519 0.3878 0.2092 -0.0528 0.0123  0.0286  204  ALA B N   
10375 C CA  . ALA B 206  ? 0.3612 0.4046 0.2246 -0.0565 0.0145  0.0303  204  ALA B CA  
10376 C C   . ALA B 206  ? 0.3826 0.4267 0.2410 -0.0629 0.0155  0.0351  204  ALA B C   
10377 O O   . ALA B 206  ? 0.3549 0.4092 0.2149 -0.0657 0.0193  0.0369  204  ALA B O   
10378 C CB  . ALA B 206  ? 0.3326 0.3707 0.2028 -0.0565 0.0114  0.0292  204  ALA B CB  
10379 N N   . LEU B 207  ? 0.3617 0.3950 0.2140 -0.0654 0.0122  0.0374  205  LEU B N   
10380 C CA  . LEU B 207  ? 0.3985 0.4309 0.2453 -0.0718 0.0128  0.0422  205  LEU B CA  
10381 C C   . LEU B 207  ? 0.4039 0.4442 0.2449 -0.0726 0.0167  0.0438  205  LEU B C   
10382 O O   . LEU B 207  ? 0.4143 0.4613 0.2546 -0.0776 0.0195  0.0473  205  LEU B O   
10383 C CB  . LEU B 207  ? 0.3936 0.4120 0.2340 -0.0734 0.0081  0.0441  205  LEU B CB  
10384 C CG  . LEU B 207  ? 0.4199 0.4305 0.2653 -0.0741 0.0044  0.0436  205  LEU B CG  
10385 C CD1 . LEU B 207  ? 0.4465 0.4434 0.2859 -0.0735 -0.0003 0.0443  205  LEU B CD1 
10386 C CD2 . LEU B 207  ? 0.3827 0.3962 0.2306 -0.0803 0.0054  0.0467  205  LEU B CD2 
10387 N N   . LYS B 208  ? 0.3706 0.4103 0.2074 -0.0677 0.0170  0.0414  206  LYS B N   
10388 C CA  . LYS B 208  ? 0.3867 0.4337 0.2174 -0.0679 0.0209  0.0427  206  LYS B CA  
10389 C C   . LYS B 208  ? 0.4049 0.4667 0.2419 -0.0675 0.0259  0.0419  206  LYS B C   
10390 O O   . LYS B 208  ? 0.4255 0.4956 0.2598 -0.0709 0.0296  0.0449  206  LYS B O   
10391 C CB  . LYS B 208  ? 0.4300 0.4727 0.2549 -0.0625 0.0198  0.0398  206  LYS B CB  
10392 N N   . ARG B 209  ? 0.3885 0.4540 0.2338 -0.0635 0.0261  0.0382  207  ARG B N   
10393 C CA  . ARG B 209  ? 0.3968 0.4761 0.2484 -0.0625 0.0305  0.0373  207  ARG B CA  
10394 C C   . ARG B 209  ? 0.4394 0.5247 0.2963 -0.0684 0.0317  0.0405  207  ARG B C   
10395 O O   . ARG B 209  ? 0.4227 0.5207 0.2840 -0.0688 0.0358  0.0408  207  ARG B O   
10396 C CB  . ARG B 209  ? 0.4120 0.4923 0.2704 -0.0562 0.0300  0.0323  207  ARG B CB  
10397 C CG  . ARG B 209  ? 0.4154 0.4915 0.2688 -0.0502 0.0292  0.0289  207  ARG B CG  
10398 C CD  . ARG B 209  ? 0.4435 0.5202 0.3039 -0.0445 0.0285  0.0243  207  ARG B CD  
10399 N NE  . ARG B 209  ? 0.5280 0.6023 0.3841 -0.0387 0.0283  0.0208  207  ARG B NE  
10400 C CZ  . ARG B 209  ? 0.5665 0.6397 0.4268 -0.0335 0.0274  0.0166  207  ARG B CZ  
10401 N NH1 . ARG B 209  ? 0.4702 0.5446 0.3393 -0.0331 0.0265  0.0154  207  ARG B NH1 
10402 N NH2 . ARG B 209  ? 0.5654 0.6361 0.4209 -0.0287 0.0272  0.0136  207  ARG B NH2 
10403 N N   . SER B 210  ? 0.3853 0.4618 0.2417 -0.0730 0.0283  0.0430  208  SER B N   
10404 C CA  . SER B 210  ? 0.4052 0.4862 0.2663 -0.0790 0.0290  0.0460  208  SER B CA  
10405 C C   . SER B 210  ? 0.3985 0.4855 0.2547 -0.0850 0.0319  0.0507  208  SER B C   
10406 O O   . SER B 210  ? 0.3895 0.4842 0.2502 -0.0898 0.0336  0.0531  208  SER B O   
10407 C CB  . SER B 210  ? 0.3480 0.4166 0.2099 -0.0815 0.0241  0.0466  208  SER B CB  
10408 O OG  . SER B 210  ? 0.4027 0.4675 0.2704 -0.0763 0.0219  0.0424  208  SER B OG  
10409 N N   . LYS B 211  ? 0.3797 0.4637 0.2268 -0.0850 0.0324  0.0522  209  LYS B N   
10410 C CA  . LYS B 211  ? 0.3790 0.4673 0.2205 -0.0913 0.0348  0.0571  209  LYS B CA  
10411 C C   . LYS B 211  ? 0.3919 0.4972 0.2384 -0.0926 0.0402  0.0580  209  LYS B C   
10412 O O   . LYS B 211  ? 0.4443 0.5550 0.2911 -0.0993 0.0417  0.0622  209  LYS B O   
10413 C CB  . LYS B 211  ? 0.4467 0.5296 0.2775 -0.0900 0.0348  0.0579  209  LYS B CB  
10414 N N   . GLU B 212  ? 0.4043 0.5185 0.2548 -0.0863 0.0430  0.0542  210  GLU B N   
10415 C CA  . GLU B 212  ? 0.4191 0.5501 0.2737 -0.0867 0.0484  0.0549  210  GLU B CA  
10416 C C   . GLU B 212  ? 0.4045 0.5427 0.2678 -0.0915 0.0488  0.0568  210  GLU B C   
10417 O O   . GLU B 212  ? 0.4363 0.5841 0.3001 -0.0971 0.0517  0.0606  210  GLU B O   
10418 C CB  . GLU B 212  ? 0.4850 0.6225 0.3425 -0.0784 0.0507  0.0500  210  GLU B CB  
10419 N N   . LEU B 213  ? 0.3644 0.4982 0.2346 -0.0897 0.0458  0.0541  211  LEU B N   
10420 C CA  . LEU B 213  ? 0.3972 0.5373 0.2757 -0.0941 0.0459  0.0556  211  LEU B CA  
10421 C C   . LEU B 213  ? 0.3923 0.5243 0.2678 -0.1022 0.0430  0.0600  211  LEU B C   
10422 O O   . LEU B 213  ? 0.3845 0.5240 0.2642 -0.1080 0.0442  0.0629  211  LEU B O   
10423 C CB  . LEU B 213  ? 0.3588 0.4982 0.2458 -0.0892 0.0441  0.0513  211  LEU B CB  
10424 C CG  . LEU B 213  ? 0.3643 0.5144 0.2555 -0.0820 0.0475  0.0475  211  LEU B CG  
10425 C CD1 . LEU B 213  ? 0.3713 0.5208 0.2708 -0.0776 0.0458  0.0436  211  LEU B CD1 
10426 C CD2 . LEU B 213  ? 0.3990 0.5662 0.2927 -0.0841 0.0527  0.0497  211  LEU B CD2 
10427 N N   . GLU B 214  ? 0.3526 0.4695 0.2208 -0.1029 0.0392  0.0606  212  GLU B N   
10428 C CA  . GLU B 214  ? 0.3512 0.4596 0.2154 -0.1105 0.0365  0.0649  212  GLU B CA  
10429 C C   . GLU B 214  ? 0.4244 0.5411 0.2844 -0.1169 0.0399  0.0699  212  GLU B C   
10430 O O   . GLU B 214  ? 0.4122 0.5304 0.2737 -0.1242 0.0395  0.0736  212  GLU B O   
10431 C CB  . GLU B 214  ? 0.3934 0.4845 0.2500 -0.1093 0.0320  0.0646  212  GLU B CB  
10432 C CG  . GLU B 214  ? 0.3646 0.4460 0.2257 -0.1055 0.0278  0.0609  212  GLU B CG  
10433 C CD  . GLU B 214  ? 0.4013 0.4659 0.2553 -0.1048 0.0232  0.0610  212  GLU B CD  
10434 O OE1 . GLU B 214  ? 0.4738 0.5343 0.3193 -0.1052 0.0233  0.0628  212  GLU B OE1 
10435 O OE2 . GLU B 214  ? 0.4054 0.4610 0.2623 -0.1037 0.0194  0.0593  212  GLU B OE2 
10436 N N   . GLU B 215  ? 0.4169 0.5393 0.2718 -0.1145 0.0433  0.0701  213  GLU B N   
10437 C CA  . GLU B 215  ? 0.4030 0.5333 0.2562 -0.1187 0.0464  0.0737  213  GLU B CA  
10438 C C   . GLU B 215  ? 0.4153 0.5602 0.2791 -0.1205 0.0490  0.0739  213  GLU B C   
10439 O O   . GLU B 215  ? 0.4348 0.5840 0.2998 -0.1256 0.0499  0.0771  213  GLU B O   
10440 C CB  . GLU B 215  ? 0.4450 0.5789 0.2926 -0.1138 0.0494  0.0725  213  GLU B CB  
10441 C CG  . GLU B 215  ? 0.5031 0.6227 0.3393 -0.1130 0.0467  0.0730  213  GLU B CG  
10442 C CD  . GLU B 215  ? 0.5904 0.7136 0.4206 -0.1091 0.0497  0.0724  213  GLU B CD  
10443 O OE1 . GLU B 215  ? 0.7217 0.8547 0.5537 -0.1106 0.0532  0.0741  213  GLU B OE1 
10444 O OE2 . GLU B 215  ? 0.6835 0.7997 0.5070 -0.1044 0.0485  0.0702  213  GLU B OE2 
10445 N N   . LYS B 216  ? 0.4055 0.5582 0.2772 -0.1162 0.0502  0.0705  214  LYS B N   
10446 C CA  . LYS B 216  ? 0.4029 0.5692 0.2850 -0.1174 0.0523  0.0705  214  LYS B CA  
10447 C C   . LYS B 216  ? 0.4314 0.5939 0.3182 -0.1233 0.0490  0.0721  214  LYS B C   
10448 O O   . LYS B 216  ? 0.4214 0.5941 0.3162 -0.1257 0.0500  0.0728  214  LYS B O   
10449 C CB  . LYS B 216  ? 0.4133 0.5899 0.3018 -0.1098 0.0549  0.0661  214  LYS B CB  
10450 N N   . GLY B 217  ? 0.3656 0.5133 0.2472 -0.1257 0.0449  0.0728  215  GLY B N   
10451 C CA  . GLY B 217  ? 0.3555 0.4977 0.2404 -0.1313 0.0414  0.0743  215  GLY B CA  
10452 C C   . GLY B 217  ? 0.4250 0.5613 0.3138 -0.1279 0.0387  0.0709  215  GLY B C   
10453 O O   . GLY B 217  ? 0.4037 0.5350 0.2955 -0.1319 0.0357  0.0716  215  GLY B O   
10454 N N   . PHE B 218  ? 0.3618 0.4974 0.2519 -0.1194 0.0391  0.0663  216  PHE B N   
10455 C CA  . PHE B 218  ? 0.3375 0.4642 0.2314 -0.1148 0.0355  0.0622  216  PHE B CA  
10456 C C   . PHE B 218  ? 0.3574 0.4658 0.2441 -0.1155 0.0309  0.0626  216  PHE B C   
10457 O O   . PHE B 218  ? 0.3642 0.4666 0.2425 -0.1178 0.0306  0.0652  216  PHE B O   
10458 C CB  . PHE B 218  ? 0.3200 0.4508 0.2168 -0.1057 0.0372  0.0574  216  PHE B CB  
10459 C CG  . PHE B 218  ? 0.3751 0.5227 0.2799 -0.1035 0.0412  0.0561  216  PHE B CG  
10460 C CD1 . PHE B 218  ? 0.3609 0.5216 0.2647 -0.1039 0.0459  0.0578  216  PHE B CD1 
10461 C CD2 . PHE B 218  ? 0.3778 0.5283 0.2911 -0.1007 0.0403  0.0532  216  PHE B CD2 
10462 C CE1 . PHE B 218  ? 0.3919 0.5682 0.3031 -0.1014 0.0496  0.0566  216  PHE B CE1 
10463 C CE2 . PHE B 218  ? 0.3647 0.5305 0.2853 -0.0984 0.0438  0.0521  216  PHE B CE2 
10464 C CZ  . PHE B 218  ? 0.3675 0.5463 0.2872 -0.0986 0.0484  0.0537  216  PHE B CZ  
10465 N N   . SER B 219  ? 0.3497 0.4493 0.2398 -0.1134 0.0272  0.0600  217  SER B N   
10466 C CA  . SER B 219  ? 0.3495 0.4323 0.2341 -0.1118 0.0228  0.0591  217  SER B CA  
10467 C C   . SER B 219  ? 0.3337 0.4137 0.2227 -0.1039 0.0215  0.0539  217  SER B C   
10468 O O   . SER B 219  ? 0.3046 0.3950 0.2003 -0.1000 0.0240  0.0513  217  SER B O   
10469 C CB  . SER B 219  ? 0.3506 0.4234 0.2339 -0.1179 0.0190  0.0616  217  SER B CB  
10470 O OG  . SER B 219  ? 0.3815 0.4588 0.2732 -0.1184 0.0186  0.0601  217  SER B OG  
10471 N N   . TYR B 220  ? 0.3388 0.4048 0.2242 -0.1016 0.0176  0.0526  218  TYR B N   
10472 C CA  . TYR B 220  ? 0.3202 0.3827 0.2089 -0.0942 0.0163  0.0479  218  TYR B CA  
10473 C C   . TYR B 220  ? 0.2931 0.3429 0.1825 -0.0939 0.0117  0.0468  218  TYR B C   
10474 O O   . TYR B 220  ? 0.3250 0.3650 0.2093 -0.0982 0.0089  0.0494  218  TYR B O   
10475 C CB  . TYR B 220  ? 0.3024 0.3617 0.1852 -0.0895 0.0166  0.0465  218  TYR B CB  
10476 C CG  . TYR B 220  ? 0.3060 0.3782 0.1900 -0.0866 0.0211  0.0455  218  TYR B CG  
10477 C CD1 . TYR B 220  ? 0.3299 0.4097 0.2099 -0.0905 0.0243  0.0489  218  TYR B CD1 
10478 C CD2 . TYR B 220  ? 0.2961 0.3732 0.1854 -0.0801 0.0222  0.0413  218  TYR B CD2 
10479 C CE1 . TYR B 220  ? 0.3271 0.4190 0.2081 -0.0876 0.0287  0.0479  218  TYR B CE1 
10480 C CE2 . TYR B 220  ? 0.3378 0.4263 0.2279 -0.0771 0.0264  0.0402  218  TYR B CE2 
10481 C CZ  . TYR B 220  ? 0.3189 0.4150 0.2050 -0.0807 0.0296  0.0434  218  TYR B CZ  
10482 O OH  . TYR B 220  ? 0.3862 0.4938 0.2729 -0.0774 0.0338  0.0423  218  TYR B OH  
10483 N N   . SER B 221  ? 0.2888 0.3390 0.1843 -0.0887 0.0110  0.0428  219  SER B N   
10484 C CA  . SER B 221  ? 0.2824 0.3209 0.1787 -0.0865 0.0069  0.0409  219  SER B CA  
10485 C C   . SER B 221  ? 0.3048 0.3429 0.2033 -0.0791 0.0068  0.0368  219  SER B C   
10486 O O   . SER B 221  ? 0.3077 0.3549 0.2121 -0.0757 0.0091  0.0343  219  SER B O   
10487 C CB  . SER B 221  ? 0.2962 0.3363 0.1991 -0.0885 0.0061  0.0404  219  SER B CB  
10488 O OG  . SER B 221  ? 0.3000 0.3291 0.2036 -0.0861 0.0023  0.0384  219  SER B OG  
10489 N N   . TYR B 222  ? 0.3039 0.3316 0.1973 -0.0766 0.0040  0.0361  220  TYR B N   
10490 C CA  . TYR B 222  ? 0.2837 0.3107 0.1782 -0.0700 0.0038  0.0325  220  TYR B CA  
10491 C C   . TYR B 222  ? 0.2966 0.3185 0.1964 -0.0663 0.0012  0.0294  220  TYR B C   
10492 O O   . TYR B 222  ? 0.3070 0.3204 0.2064 -0.0680 -0.0018 0.0301  220  TYR B O   
10493 C CB  . TYR B 222  ? 0.2787 0.2981 0.1650 -0.0690 0.0022  0.0333  220  TYR B CB  
10494 C CG  . TYR B 222  ? 0.2826 0.3080 0.1636 -0.0719 0.0051  0.0361  220  TYR B CG  
10495 C CD1 . TYR B 222  ? 0.2905 0.3258 0.1725 -0.0689 0.0087  0.0346  220  TYR B CD1 
10496 C CD2 . TYR B 222  ? 0.2996 0.3211 0.1746 -0.0777 0.0046  0.0403  220  TYR B CD2 
10497 C CE1 . TYR B 222  ? 0.2884 0.3300 0.1657 -0.0715 0.0117  0.0371  220  TYR B CE1 
10498 C CE2 . TYR B 222  ? 0.3048 0.3325 0.1750 -0.0807 0.0075  0.0430  220  TYR B CE2 
10499 C CZ  . TYR B 222  ? 0.2866 0.3246 0.1580 -0.0774 0.0112  0.0413  220  TYR B CZ  
10500 O OH  . TYR B 222  ? 0.3127 0.3574 0.1794 -0.0802 0.0144  0.0440  220  TYR B OH  
10501 N N   . ASP B 223  ? 0.2772 0.3043 0.1819 -0.0612 0.0025  0.0260  221  ASP B N   
10502 C CA  . ASP B 223  ? 0.3078 0.3317 0.2182 -0.0573 0.0006  0.0228  221  ASP B CA  
10503 C C   . ASP B 223  ? 0.3281 0.3480 0.2365 -0.0521 -0.0007 0.0203  221  ASP B C   
10504 O O   . ASP B 223  ? 0.3191 0.3451 0.2278 -0.0491 0.0016  0.0187  221  ASP B O   
10505 C CB  . ASP B 223  ? 0.3326 0.3667 0.2504 -0.0560 0.0032  0.0211  221  ASP B CB  
10506 C CG  . ASP B 223  ? 0.3772 0.4093 0.3006 -0.0512 0.0019  0.0175  221  ASP B CG  
10507 O OD1 . ASP B 223  ? 0.3593 0.3822 0.2819 -0.0499 -0.0013 0.0167  221  ASP B OD1 
10508 O OD2 . ASP B 223  ? 0.4031 0.4432 0.3317 -0.0487 0.0041  0.0156  221  ASP B OD2 
10509 N N   . MET B 224  ? 0.3015 0.3112 0.2080 -0.0510 -0.0043 0.0199  222  MET B N   
10510 C CA  . MET B 224  ? 0.3460 0.3516 0.2507 -0.0464 -0.0059 0.0177  222  MET B CA  
10511 C C   . MET B 224  ? 0.3342 0.3415 0.2456 -0.0418 -0.0062 0.0141  222  MET B C   
10512 O O   . MET B 224  ? 0.3539 0.3569 0.2648 -0.0382 -0.0081 0.0122  222  MET B O   
10513 C CB  . MET B 224  ? 0.3657 0.3601 0.2652 -0.0470 -0.0097 0.0191  222  MET B CB  
10514 C CG  . MET B 224  ? 0.3162 0.3077 0.2082 -0.0515 -0.0097 0.0228  222  MET B CG  
10515 S SD  . MET B 224  ? 0.4027 0.4019 0.2897 -0.0519 -0.0062 0.0237  222  MET B SD  
10516 C CE  . MET B 224  ? 0.4351 0.4304 0.3202 -0.0460 -0.0082 0.0206  222  MET B CE  
10517 N N   . LEU B 225  ? 0.3509 0.3643 0.2686 -0.0421 -0.0044 0.0132  223  LEU B N   
10518 C CA  . LEU B 225  ? 0.3254 0.3423 0.2497 -0.0381 -0.0039 0.0100  223  LEU B CA  
10519 C C   . LEU B 225  ? 0.4177 0.4280 0.3457 -0.0363 -0.0068 0.0086  223  LEU B C   
10520 O O   . LEU B 225  ? 0.4126 0.4253 0.3459 -0.0332 -0.0065 0.0060  223  LEU B O   
10521 C CB  . LEU B 225  ? 0.3870 0.4073 0.3106 -0.0340 -0.0026 0.0077  223  LEU B CB  
10522 C CG  . LEU B 225  ? 0.4023 0.4298 0.3224 -0.0349 0.0006  0.0088  223  LEU B CG  
10523 C CD1 . LEU B 225  ? 0.4978 0.5271 0.4166 -0.0305 0.0014  0.0062  223  LEU B CD1 
10524 C CD2 . LEU B 225  ? 0.4009 0.4377 0.3255 -0.0369 0.0037  0.0095  223  LEU B CD2 
10525 N N   . GLY B 226  ? 0.3412 0.3431 0.2661 -0.0381 -0.0096 0.0101  224  GLY B N   
10526 C CA  . GLY B 226  ? 0.3647 0.3608 0.2931 -0.0361 -0.0123 0.0087  224  GLY B CA  
10527 C C   . GLY B 226  ? 0.3145 0.3140 0.2489 -0.0370 -0.0113 0.0081  224  GLY B C   
10528 O O   . GLY B 226  ? 0.3148 0.3172 0.2490 -0.0407 -0.0100 0.0099  224  GLY B O   
10529 N N   . GLU B 227  ? 0.3027 0.3018 0.2422 -0.0336 -0.0121 0.0056  225  GLU B N   
10530 C CA  . GLU B 227  ? 0.3110 0.3131 0.2561 -0.0340 -0.0113 0.0049  225  GLU B CA  
10531 C C   . GLU B 227  ? 0.2603 0.2599 0.2098 -0.0301 -0.0128 0.0024  225  GLU B C   
10532 O O   . GLU B 227  ? 0.2844 0.2837 0.2343 -0.0269 -0.0132 0.0008  225  GLU B O   
10533 C CB  . GLU B 227  ? 0.3286 0.3407 0.2767 -0.0342 -0.0080 0.0044  225  GLU B CB  
10534 C CG  . GLU B 227  ? 0.3293 0.3453 0.2828 -0.0349 -0.0070 0.0039  225  GLU B CG  
10535 C CD  . GLU B 227  ? 0.3646 0.3905 0.3204 -0.0355 -0.0038 0.0039  225  GLU B CD  
10536 O OE1 . GLU B 227  ? 0.3567 0.3864 0.3094 -0.0357 -0.0022 0.0046  225  GLU B OE1 
10537 O OE2 . GLU B 227  ? 0.4127 0.4429 0.3733 -0.0355 -0.0030 0.0033  225  GLU B OE2 
10538 N N   . ALA B 228  ? 0.2464 0.2441 0.1992 -0.0306 -0.0135 0.0021  226  ALA B N   
10539 C CA  . ALA B 228  ? 0.2600 0.2573 0.2180 -0.0272 -0.0142 -0.0003 226  ALA B CA  
10540 C C   . ALA B 228  ? 0.2613 0.2537 0.2185 -0.0240 -0.0163 -0.0014 226  ALA B C   
10541 O O   . ALA B 228  ? 0.2731 0.2680 0.2332 -0.0210 -0.0160 -0.0033 226  ALA B O   
10542 C CB  . ALA B 228  ? 0.2845 0.2897 0.2472 -0.0256 -0.0117 -0.0019 226  ALA B CB  
10543 N N   . ALA B 229  ? 0.2424 0.2278 0.1956 -0.0248 -0.0187 -0.0001 227  ALA B N   
10544 C CA  . ALA B 229  ? 0.2435 0.2242 0.1964 -0.0219 -0.0211 -0.0010 227  ALA B CA  
10545 C C   . ALA B 229  ? 0.2287 0.2101 0.1877 -0.0189 -0.0215 -0.0031 227  ALA B C   
10546 O O   . ALA B 229  ? 0.2522 0.2334 0.2140 -0.0193 -0.0212 -0.0033 227  ALA B O   
10547 C CB  . ALA B 229  ? 0.2549 0.2276 0.2032 -0.0231 -0.0237 0.0008  227  ALA B CB  
10548 N N   . THR B 230  ? 0.2394 0.2217 0.2004 -0.0159 -0.0222 -0.0047 228  THR B N   
10549 C CA  . THR B 230  ? 0.2255 0.2086 0.1922 -0.0131 -0.0226 -0.0066 228  THR B CA  
10550 C C   . THR B 230  ? 0.2430 0.2205 0.2097 -0.0113 -0.0255 -0.0067 228  THR B C   
10551 O O   . THR B 230  ? 0.2450 0.2219 0.2158 -0.0097 -0.0261 -0.0076 228  THR B O   
10552 C CB  . THR B 230  ? 0.2496 0.2373 0.2189 -0.0111 -0.0216 -0.0083 228  THR B CB  
10553 O OG1 . THR B 230  ? 0.3153 0.3083 0.2842 -0.0125 -0.0188 -0.0083 228  THR B OG1 
10554 C CG2 . THR B 230  ? 0.2454 0.2345 0.2208 -0.0087 -0.0217 -0.0101 228  THR B CG2 
10555 N N   . THR B 231  ? 0.2415 0.2152 0.2035 -0.0114 -0.0274 -0.0057 229  THR B N   
10556 C CA  . THR B 231  ? 0.2360 0.2048 0.1979 -0.0095 -0.0304 -0.0056 229  THR B CA  
10557 C C   . THR B 231  ? 0.2435 0.2061 0.1991 -0.0112 -0.0320 -0.0035 229  THR B C   
10558 O O   . THR B 231  ? 0.2397 0.2023 0.1909 -0.0141 -0.0309 -0.0020 229  THR B O   
10559 C CB  . THR B 231  ? 0.2478 0.2176 0.2100 -0.0075 -0.0317 -0.0066 229  THR B CB  
10560 O OG1 . THR B 231  ? 0.2590 0.2279 0.2152 -0.0090 -0.0317 -0.0055 229  THR B OG1 
10561 C CG2 . THR B 231  ? 0.2577 0.2331 0.2251 -0.0061 -0.0300 -0.0086 229  THR B CG2 
10562 N N   . ALA B 232  ? 0.2402 0.1977 0.1955 -0.0095 -0.0347 -0.0032 230  ALA B N   
10563 C CA  . ALA B 232  ? 0.2504 0.2013 0.1993 -0.0108 -0.0367 -0.0011 230  ALA B CA  
10564 C C   . ALA B 232  ? 0.2736 0.2242 0.2172 -0.0119 -0.0371 0.0000  230  ALA B C   
10565 O O   . ALA B 232  ? 0.2833 0.2306 0.2210 -0.0146 -0.0372 0.0020  230  ALA B O   
10566 C CB  . ALA B 232  ? 0.2747 0.2206 0.2245 -0.0078 -0.0397 -0.0013 230  ALA B CB  
10567 N N   . ALA B 233  ? 0.2613 0.2153 0.2068 -0.0101 -0.0374 -0.0014 231  ALA B N   
10568 C CA  . ALA B 233  ? 0.2729 0.2267 0.2130 -0.0109 -0.0378 -0.0006 231  ALA B CA  
10569 C C   . ALA B 233  ? 0.2566 0.2140 0.1939 -0.0140 -0.0347 0.0002  231  ALA B C   
10570 O O   . ALA B 233  ? 0.2770 0.2325 0.2080 -0.0159 -0.0348 0.0020  231  ALA B O   
10571 C CB  . ALA B 233  ? 0.3072 0.2639 0.2499 -0.0084 -0.0387 -0.0024 231  ALA B CB  
10572 N N   . ASP B 234  ? 0.2496 0.2124 0.1914 -0.0143 -0.0319 -0.0010 232  ASP B N   
10573 C CA  . ASP B 234  ? 0.2641 0.2310 0.2039 -0.0171 -0.0290 -0.0001 232  ASP B CA  
10574 C C   . ASP B 234  ? 0.2615 0.2245 0.1966 -0.0204 -0.0291 0.0025  232  ASP B C   
10575 O O   . ASP B 234  ? 0.2634 0.2268 0.1933 -0.0229 -0.0281 0.0042  232  ASP B O   
10576 C CB  . ASP B 234  ? 0.2718 0.2446 0.2176 -0.0169 -0.0264 -0.0016 232  ASP B CB  
10577 C CG  . ASP B 234  ? 0.3199 0.2971 0.2697 -0.0142 -0.0257 -0.0040 232  ASP B CG  
10578 O OD1 . ASP B 234  ? 0.3137 0.2909 0.2610 -0.0131 -0.0264 -0.0045 232  ASP B OD1 
10579 O OD2 . ASP B 234  ? 0.3162 0.2967 0.2715 -0.0133 -0.0244 -0.0053 232  ASP B OD2 
10580 N N   . ALA B 235  ? 0.2597 0.2189 0.1965 -0.0206 -0.0302 0.0028  233  ALA B N   
10581 C CA  . ALA B 235  ? 0.2650 0.2199 0.1976 -0.0239 -0.0304 0.0051  233  ALA B CA  
10582 C C   . ALA B 235  ? 0.2683 0.2170 0.1937 -0.0249 -0.0326 0.0072  233  ALA B C   
10583 O O   . ALA B 235  ? 0.2800 0.2273 0.2002 -0.0285 -0.0320 0.0095  233  ALA B O   
10584 C CB  . ALA B 235  ? 0.2739 0.2252 0.2095 -0.0234 -0.0315 0.0046  233  ALA B CB  
10585 N N   . GLU B 236  ? 0.2750 0.2200 0.2000 -0.0219 -0.0353 0.0066  234  GLU B N   
10586 C CA  . GLU B 236  ? 0.2780 0.2169 0.1960 -0.0225 -0.0377 0.0086  234  GLU B CA  
10587 C C   . GLU B 236  ? 0.2855 0.2278 0.1991 -0.0243 -0.0361 0.0095  234  GLU B C   
10588 O O   . GLU B 236  ? 0.2956 0.2344 0.2024 -0.0271 -0.0365 0.0120  234  GLU B O   
10589 C CB  . GLU B 236  ? 0.3098 0.2451 0.2290 -0.0186 -0.0410 0.0076  234  GLU B CB  
10590 C CG  . GLU B 236  ? 0.3666 0.2944 0.2788 -0.0189 -0.0440 0.0097  234  GLU B CG  
10591 C CD  . GLU B 236  ? 0.4579 0.3829 0.3720 -0.0148 -0.0473 0.0087  234  GLU B CD  
10592 O OE1 . GLU B 236  ? 0.4995 0.4292 0.4202 -0.0121 -0.0470 0.0063  234  GLU B OE1 
10593 O OE2 . GLU B 236  ? 0.5168 0.4351 0.4258 -0.0143 -0.0502 0.0103  234  GLU B OE2 
10594 N N   . ARG B 237  ? 0.2706 0.2196 0.1875 -0.0227 -0.0344 0.0075  235  ARG B N   
10595 C CA  . ARG B 237  ? 0.2939 0.2466 0.2068 -0.0239 -0.0326 0.0080  235  ARG B CA  
10596 C C   . ARG B 237  ? 0.2886 0.2444 0.1991 -0.0280 -0.0297 0.0099  235  ARG B C   
10597 O O   . ARG B 237  ? 0.2980 0.2528 0.2021 -0.0304 -0.0293 0.0120  235  ARG B O   
10598 C CB  . ARG B 237  ? 0.2969 0.2558 0.2140 -0.0212 -0.0312 0.0052  235  ARG B CB  
10599 C CG  . ARG B 237  ? 0.3477 0.3103 0.2601 -0.0221 -0.0294 0.0056  235  ARG B CG  
10600 C CD  . ARG B 237  ? 0.4235 0.3921 0.3395 -0.0197 -0.0277 0.0028  235  ARG B CD  
10601 N NE  . ARG B 237  ? 0.4802 0.4513 0.3905 -0.0205 -0.0261 0.0033  235  ARG B NE  
10602 C CZ  . ARG B 237  ? 0.5058 0.4801 0.4159 -0.0183 -0.0253 0.0013  235  ARG B CZ  
10603 N NH1 . ARG B 237  ? 0.5571 0.5326 0.4726 -0.0154 -0.0260 -0.0014 235  ARG B NH1 
10604 N NH2 . ARG B 237  ? 0.4960 0.4723 0.4002 -0.0190 -0.0237 0.0019  235  ARG B NH2 
10605 N N   . TYR B 238  ? 0.2802 0.2399 0.1959 -0.0289 -0.0277 0.0092  236  TYR B N   
10606 C CA  . TYR B 238  ? 0.2661 0.2295 0.1802 -0.0329 -0.0250 0.0110  236  TYR B CA  
10607 C C   . TYR B 238  ? 0.2765 0.2331 0.1846 -0.0364 -0.0265 0.0141  236  TYR B C   
10608 O O   . TYR B 238  ? 0.2746 0.2328 0.1782 -0.0400 -0.0250 0.0164  236  TYR B O   
10609 C CB  . TYR B 238  ? 0.2559 0.2244 0.1766 -0.0332 -0.0230 0.0098  236  TYR B CB  
10610 C CG  . TYR B 238  ? 0.2687 0.2444 0.1950 -0.0302 -0.0211 0.0070  236  TYR B CG  
10611 C CD1 . TYR B 238  ? 0.3166 0.2966 0.2411 -0.0291 -0.0196 0.0063  236  TYR B CD1 
10612 C CD2 . TYR B 238  ? 0.2866 0.2644 0.2195 -0.0286 -0.0207 0.0051  236  TYR B CD2 
10613 C CE1 . TYR B 238  ? 0.3850 0.3708 0.3142 -0.0263 -0.0180 0.0037  236  TYR B CE1 
10614 C CE2 . TYR B 238  ? 0.2835 0.2673 0.2212 -0.0260 -0.0191 0.0028  236  TYR B CE2 
10615 C CZ  . TYR B 238  ? 0.3797 0.3674 0.3156 -0.0249 -0.0178 0.0021  236  TYR B CZ  
10616 O OH  . TYR B 238  ? 0.3575 0.3503 0.2979 -0.0222 -0.0163 -0.0004 236  TYR B OH  
10617 N N   . TYR B 239  ? 0.2699 0.2188 0.1778 -0.0355 -0.0296 0.0143  237  TYR B N   
10618 C CA  . TYR B 239  ? 0.2704 0.2114 0.1719 -0.0385 -0.0315 0.0172  237  TYR B CA  
10619 C C   . TYR B 239  ? 0.3072 0.2458 0.2014 -0.0394 -0.0322 0.0192  237  TYR B C   
10620 O O   . TYR B 239  ? 0.3002 0.2375 0.1888 -0.0435 -0.0315 0.0220  237  TYR B O   
10621 C CB  . TYR B 239  ? 0.2796 0.2125 0.1819 -0.0362 -0.0348 0.0167  237  TYR B CB  
10622 C CG  . TYR B 239  ? 0.3300 0.2535 0.2250 -0.0388 -0.0373 0.0197  237  TYR B CG  
10623 C CD1 . TYR B 239  ? 0.3580 0.2782 0.2513 -0.0425 -0.0371 0.0213  237  TYR B CD1 
10624 C CD2 . TYR B 239  ? 0.4248 0.3425 0.3141 -0.0376 -0.0399 0.0209  237  TYR B CD2 
10625 C CE1 . TYR B 239  ? 0.3353 0.2463 0.2215 -0.0449 -0.0394 0.0241  237  TYR B CE1 
10626 C CE2 . TYR B 239  ? 0.4201 0.3287 0.3022 -0.0399 -0.0422 0.0238  237  TYR B CE2 
10627 C CZ  . TYR B 239  ? 0.4125 0.3176 0.2931 -0.0436 -0.0419 0.0253  237  TYR B CZ  
10628 O OH  . TYR B 239  ? 0.4901 0.3855 0.3633 -0.0461 -0.0444 0.0282  237  TYR B OH  
10629 N N   . ARG B 240  ? 0.3053 0.2431 0.1992 -0.0358 -0.0338 0.0178  238  ARG B N   
10630 C CA  . ARG B 240  ? 0.3163 0.2514 0.2029 -0.0363 -0.0348 0.0195  238  ARG B CA  
10631 C C   . ARG B 240  ? 0.3199 0.2620 0.2039 -0.0389 -0.0313 0.0204  238  ARG B C   
10632 O O   . ARG B 240  ? 0.3303 0.2702 0.2072 -0.0416 -0.0312 0.0231  238  ARG B O   
10633 C CB  . ARG B 240  ? 0.3187 0.2525 0.2062 -0.0318 -0.0371 0.0175  238  ARG B CB  
10634 C CG  . ARG B 240  ? 0.3549 0.2815 0.2437 -0.0292 -0.0409 0.0171  238  ARG B CG  
10635 C CD  . ARG B 240  ? 0.4297 0.3474 0.3113 -0.0314 -0.0433 0.0203  238  ARG B CD  
10636 N NE  . ARG B 240  ? 0.4498 0.3607 0.3330 -0.0285 -0.0468 0.0198  238  ARG B NE  
10637 C CZ  . ARG B 240  ? 0.5243 0.4264 0.4026 -0.0296 -0.0493 0.0220  238  ARG B CZ  
10638 N NH1 . ARG B 240  ? 0.4884 0.3870 0.3597 -0.0339 -0.0488 0.0251  238  ARG B NH1 
10639 N NH2 . ARG B 240  ? 0.5685 0.4653 0.4489 -0.0263 -0.0523 0.0212  238  ARG B NH2 
10640 N N   . ASP B 241  ? 0.3229 0.2736 0.2126 -0.0380 -0.0283 0.0183  239  ASP B N   
10641 C CA  . ASP B 241  ? 0.3517 0.3099 0.2396 -0.0401 -0.0247 0.0190  239  ASP B CA  
10642 C C   . ASP B 241  ? 0.3198 0.2787 0.2051 -0.0453 -0.0230 0.0220  239  ASP B C   
10643 O O   . ASP B 241  ? 0.3194 0.2804 0.1993 -0.0481 -0.0214 0.0242  239  ASP B O   
10644 C CB  . ASP B 241  ? 0.3568 0.3237 0.2515 -0.0376 -0.0220 0.0159  239  ASP B CB  
10645 C CG  . ASP B 241  ? 0.4255 0.3926 0.3215 -0.0330 -0.0232 0.0131  239  ASP B CG  
10646 O OD1 . ASP B 241  ? 0.4497 0.4113 0.3408 -0.0319 -0.0258 0.0136  239  ASP B OD1 
10647 O OD2 . ASP B 241  ? 0.5185 0.4911 0.4204 -0.0306 -0.0217 0.0105  239  ASP B OD2 
10648 N N   . TYR B 242  ? 0.2934 0.2504 0.1824 -0.0468 -0.0235 0.0222  240  TYR B N   
10649 C CA  . TYR B 242  ? 0.3014 0.2581 0.1877 -0.0522 -0.0225 0.0253  240  TYR B CA  
10650 C C   . TYR B 242  ? 0.3048 0.2527 0.1824 -0.0548 -0.0248 0.0285  240  TYR B C   
10651 O O   . TYR B 242  ? 0.3013 0.2505 0.1741 -0.0592 -0.0233 0.0314  240  TYR B O   
10652 C CB  . TYR B 242  ? 0.2957 0.2501 0.1868 -0.0530 -0.0233 0.0247  240  TYR B CB  
10653 C CG  . TYR B 242  ? 0.2760 0.2392 0.1750 -0.0519 -0.0207 0.0224  240  TYR B CG  
10654 C CD1 . TYR B 242  ? 0.2958 0.2692 0.1967 -0.0528 -0.0171 0.0222  240  TYR B CD1 
10655 C CD2 . TYR B 242  ? 0.2787 0.2400 0.1832 -0.0500 -0.0219 0.0204  240  TYR B CD2 
10656 C CE1 . TYR B 242  ? 0.3017 0.2830 0.2099 -0.0518 -0.0149 0.0202  240  TYR B CE1 
10657 C CE2 . TYR B 242  ? 0.2805 0.2494 0.1919 -0.0492 -0.0197 0.0185  240  TYR B CE2 
10658 C CZ  . TYR B 242  ? 0.3065 0.2852 0.2198 -0.0500 -0.0163 0.0184  240  TYR B CZ  
10659 O OH  . TYR B 242  ? 0.2918 0.2777 0.2119 -0.0489 -0.0143 0.0164  240  TYR B OH  
10660 N N   . GLU B 243  ? 0.3141 0.2531 0.1898 -0.0521 -0.0286 0.0281  241  GLU B N   
10661 C CA  . GLU B 243  ? 0.3063 0.2361 0.1737 -0.0541 -0.0312 0.0311  241  GLU B CA  
10662 C C   . GLU B 243  ? 0.3411 0.2733 0.2022 -0.0551 -0.0300 0.0327  241  GLU B C   
10663 O O   . GLU B 243  ? 0.3153 0.2449 0.1697 -0.0594 -0.0297 0.0361  241  GLU B O   
10664 C CB  . GLU B 243  ? 0.3220 0.2434 0.1896 -0.0498 -0.0353 0.0298  241  GLU B CB  
10665 C CG  . GLU B 243  ? 0.3721 0.2833 0.2312 -0.0510 -0.0386 0.0327  241  GLU B CG  
10666 C CD  . GLU B 243  ? 0.4356 0.3400 0.2953 -0.0461 -0.0425 0.0311  241  GLU B CD  
10667 O OE1 . GLU B 243  ? 0.4671 0.3759 0.3320 -0.0418 -0.0425 0.0281  241  GLU B OE1 
10668 O OE2 . GLU B 243  ? 0.4825 0.3771 0.3375 -0.0465 -0.0457 0.0330  241  GLU B OE2 
10669 N N   . SER B 244  ? 0.3150 0.2521 0.1780 -0.0512 -0.0292 0.0302  242  SER B N   
10670 C CA  A SER B 244  ? 0.3169 0.2566 0.1739 -0.0516 -0.0280 0.0313  242  SER B CA  
10671 C CA  B SER B 244  ? 0.3172 0.2569 0.1741 -0.0517 -0.0280 0.0313  242  SER B CA  
10672 C C   . SER B 244  ? 0.3008 0.2485 0.1567 -0.0559 -0.0237 0.0331  242  SER B C   
10673 O O   . SER B 244  ? 0.3147 0.2620 0.1634 -0.0588 -0.0229 0.0359  242  SER B O   
10674 C CB  A SER B 244  ? 0.3271 0.2709 0.1872 -0.0466 -0.0278 0.0278  242  SER B CB  
10675 C CB  B SER B 244  ? 0.3277 0.2712 0.1874 -0.0466 -0.0279 0.0279  242  SER B CB  
10676 O OG  A SER B 244  ? 0.3758 0.3226 0.2301 -0.0467 -0.0264 0.0284  242  SER B OG  
10677 O OG  B SER B 244  ? 0.3342 0.2707 0.1944 -0.0430 -0.0320 0.0266  242  SER B OG  
10678 N N   . ALA B 245  ? 0.3156 0.2710 0.1786 -0.0562 -0.0210 0.0316  243  ALA B N   
10679 C CA  . ALA B 245  ? 0.3132 0.2774 0.1763 -0.0600 -0.0170 0.0332  243  ALA B CA  
10680 C C   . ALA B 245  ? 0.3300 0.2901 0.1885 -0.0659 -0.0173 0.0373  243  ALA B C   
10681 O O   . ALA B 245  ? 0.3333 0.2975 0.1873 -0.0697 -0.0149 0.0399  243  ALA B O   
10682 C CB  . ALA B 245  ? 0.3186 0.2914 0.1907 -0.0587 -0.0145 0.0306  243  ALA B CB  
10683 N N   . ILE B 246  ? 0.3163 0.2682 0.1755 -0.0670 -0.0203 0.0378  244  ILE B N   
10684 C CA  . ILE B 246  ? 0.3269 0.2735 0.1812 -0.0728 -0.0211 0.0417  244  ILE B CA  
10685 C C   . ILE B 246  ? 0.3492 0.2902 0.1938 -0.0748 -0.0222 0.0449  244  ILE B C   
10686 O O   . ILE B 246  ? 0.3594 0.3018 0.1993 -0.0801 -0.0206 0.0484  244  ILE B O   
10687 C CB  . ILE B 246  ? 0.3397 0.2774 0.1959 -0.0728 -0.0244 0.0414  244  ILE B CB  
10688 C CG1 . ILE B 246  ? 0.3374 0.2818 0.2025 -0.0724 -0.0227 0.0391  244  ILE B CG1 
10689 C CG2 . ILE B 246  ? 0.3659 0.2954 0.2151 -0.0785 -0.0261 0.0455  244  ILE B CG2 
10690 C CD1 . ILE B 246  ? 0.3490 0.2854 0.2167 -0.0714 -0.0257 0.0380  244  ILE B CD1 
10691 N N   . HIS B 247  ? 0.3551 0.2897 0.1963 -0.0708 -0.0249 0.0439  245  HIS B N   
10692 C CA  . HIS B 247  ? 0.3517 0.2811 0.1833 -0.0724 -0.0260 0.0469  245  HIS B CA  
10693 C C   . HIS B 247  ? 0.3585 0.2975 0.1875 -0.0742 -0.0219 0.0480  245  HIS B C   
10694 O O   . HIS B 247  ? 0.3740 0.3118 0.1960 -0.0788 -0.0211 0.0518  245  HIS B O   
10695 C CB  . HIS B 247  ? 0.3716 0.2938 0.2007 -0.0673 -0.0297 0.0453  245  HIS B CB  
10696 C CG  . HIS B 247  ? 0.3948 0.3060 0.2239 -0.0661 -0.0340 0.0454  245  HIS B CG  
10697 N ND1 . HIS B 247  ? 0.3879 0.2894 0.2103 -0.0698 -0.0364 0.0489  245  HIS B ND1 
10698 C CD2 . HIS B 247  ? 0.4265 0.3348 0.2613 -0.0615 -0.0364 0.0423  245  HIS B CD2 
10699 C CE1 . HIS B 247  ? 0.4270 0.3200 0.2510 -0.0673 -0.0400 0.0479  245  HIS B CE1 
10700 N NE2 . HIS B 247  ? 0.4556 0.3529 0.2872 -0.0622 -0.0400 0.0439  245  HIS B NE2 
10701 N N   . ALA B 248  ? 0.3358 0.2846 0.1703 -0.0708 -0.0191 0.0448  246  ALA B N   
10702 C CA  . ALA B 248  ? 0.3513 0.3093 0.1831 -0.0719 -0.0151 0.0455  246  ALA B CA  
10703 C C   . ALA B 248  ? 0.3475 0.3128 0.1807 -0.0775 -0.0117 0.0481  246  ALA B C   
10704 O O   . ALA B 248  ? 0.3470 0.3153 0.1744 -0.0813 -0.0095 0.0513  246  ALA B O   
10705 C CB  . ALA B 248  ? 0.3661 0.3321 0.2034 -0.0665 -0.0132 0.0413  246  ALA B CB  
10706 N N   . ILE B 249  ? 0.3550 0.3237 0.1960 -0.0781 -0.0111 0.0469  247  ILE B N   
10707 C CA  . ILE B 249  ? 0.3551 0.3311 0.1983 -0.0836 -0.0081 0.0492  247  ILE B CA  
10708 C C   . ILE B 249  ? 0.3361 0.3044 0.1724 -0.0898 -0.0098 0.0538  247  ILE B C   
10709 O O   . ILE B 249  ? 0.3690 0.3426 0.2024 -0.0950 -0.0071 0.0571  247  ILE B O   
10710 C CB  . ILE B 249  ? 0.3261 0.3061 0.1789 -0.0827 -0.0078 0.0467  247  ILE B CB  
10711 C CG1 . ILE B 249  ? 0.3013 0.2898 0.1607 -0.0770 -0.0057 0.0425  247  ILE B CG1 
10712 C CG2 . ILE B 249  ? 0.3430 0.3291 0.1978 -0.0889 -0.0055 0.0495  247  ILE B CG2 
10713 C CD1 . ILE B 249  ? 0.3275 0.3159 0.1953 -0.0744 -0.0068 0.0394  247  ILE B CD1 
10714 N N   . GLY B 250  ? 0.3719 0.3274 0.2055 -0.0894 -0.0142 0.0542  248  GLY B N   
10715 C CA  . GLY B 250  ? 0.3791 0.3256 0.2057 -0.0950 -0.0163 0.0585  248  GLY B CA  
10716 C C   . GLY B 250  ? 0.4134 0.3584 0.2305 -0.0974 -0.0157 0.0619  248  GLY B C   
10717 O O   . GLY B 250  ? 0.4087 0.3539 0.2212 -0.1036 -0.0145 0.0659  248  GLY B O   
10718 N N   . LYS B 251  ? 0.3849 0.3283 0.1988 -0.0926 -0.0164 0.0603  249  LYS B N   
10719 C CA  . LYS B 251  ? 0.4253 0.3678 0.2299 -0.0945 -0.0156 0.0633  249  LYS B CA  
10720 C C   . LYS B 251  ? 0.3763 0.3324 0.1816 -0.0975 -0.0102 0.0646  249  LYS B C   
10721 O O   . LYS B 251  ? 0.4413 0.3977 0.2398 -0.1026 -0.0088 0.0687  249  LYS B O   
10722 C CB  . LYS B 251  ? 0.4502 0.3888 0.2516 -0.0885 -0.0176 0.0610  249  LYS B CB  
10723 N N   . ALA B 252  ? 0.4054 0.3727 0.2188 -0.0944 -0.0071 0.0611  250  ALA B N   
10724 C CA  . ALA B 252  ? 0.3808 0.3618 0.1956 -0.0966 -0.0019 0.0621  250  ALA B CA  
10725 C C   . ALA B 252  ? 0.4055 0.3902 0.2219 -0.1038 -0.0003 0.0656  250  ALA B C   
10726 O O   . ALA B 252  ? 0.4218 0.4141 0.2351 -0.1080 0.0031  0.0686  250  ALA B O   
10727 C CB  . ALA B 252  ? 0.4030 0.3944 0.2263 -0.0912 0.0007  0.0574  250  ALA B CB  
10728 N N   . SER B 253  ? 0.3972 0.3770 0.2182 -0.1053 -0.0027 0.0653  251  SER B N   
10729 C CA  . SER B 253  ? 0.4143 0.3964 0.2364 -0.1125 -0.0018 0.0687  251  SER B CA  
10730 C C   . SER B 253  ? 0.4114 0.3874 0.2235 -0.1185 -0.0024 0.0739  251  SER B C   
10731 O O   . SER B 253  ? 0.4409 0.4245 0.2521 -0.1244 0.0006  0.0773  251  SER B O   
10732 C CB  . SER B 253  ? 0.3912 0.3656 0.2178 -0.1128 -0.0053 0.0675  251  SER B CB  
10733 O OG  . SER B 253  ? 0.4149 0.3907 0.2420 -0.1201 -0.0048 0.0708  251  SER B OG  
10734 N N   . ALA B 254  ? 0.4252 0.3878 0.2299 -0.1173 -0.0064 0.0748  252  ALA B N   
10735 C CA  . ALA B 254  ? 0.4552 0.4108 0.2493 -0.1222 -0.0073 0.0796  252  ALA B CA  
10736 C C   . ALA B 254  ? 0.5069 0.4610 0.2997 -0.1306 -0.0073 0.0840  252  ALA B C   
10737 O O   . ALA B 254  ? 0.5368 0.4950 0.3247 -0.1363 -0.0049 0.0881  252  ALA B O   
10738 C CB  . ALA B 254  ? 0.4754 0.4394 0.2647 -0.1217 -0.0035 0.0807  252  ALA B CB  
10739 N N   . GLY B 255  ? 0.5047 0.4528 0.3019 -0.1313 -0.0101 0.0829  253  GLY B N   
10740 C CA  . GLY B 255  ? 0.4970 0.4414 0.2926 -0.1391 -0.0110 0.0867  253  GLY B CA  
10741 C C   . GLY B 255  ? 0.4917 0.4507 0.2939 -0.1438 -0.0068 0.0877  253  GLY B C   
10742 O O   . GLY B 255  ? 0.5409 0.4981 0.3412 -0.1513 -0.0072 0.0914  253  GLY B O   
10743 N N   . ARG B 256  ? 0.4513 0.4245 0.2612 -0.1398 -0.0030 0.0845  254  ARG B N   
10744 C CA  . ARG B 256  ? 0.4740 0.4617 0.2907 -0.1439 0.0009  0.0853  254  ARG B CA  
10745 C C   . ARG B 256  ? 0.4678 0.4537 0.2911 -0.1460 -0.0011 0.0842  254  ARG B C   
10746 O O   . ARG B 256  ? 0.4573 0.4533 0.2854 -0.1510 0.0013  0.0858  254  ARG B O   
10747 C CB  . ARG B 256  ? 0.4457 0.4486 0.2688 -0.1385 0.0053  0.0820  254  ARG B CB  
10748 C CG  . ARG B 256  ? 0.4112 0.4214 0.2287 -0.1391 0.0090  0.0842  254  ARG B CG  
10749 C CD  . ARG B 256  ? 0.4059 0.4298 0.2295 -0.1330 0.0130  0.0805  254  ARG B CD  
10750 N NE  . ARG B 256  ? 0.4200 0.4376 0.2437 -0.1249 0.0109  0.0760  254  ARG B NE  
10751 C CZ  . ARG B 256  ? 0.4211 0.4471 0.2506 -0.1185 0.0131  0.0717  254  ARG B CZ  
10752 N NH1 . ARG B 256  ? 0.4602 0.5012 0.2965 -0.1185 0.0174  0.0709  254  ARG B NH1 
10753 N NH2 . ARG B 256  ? 0.4440 0.4632 0.2724 -0.1118 0.0109  0.0682  254  ARG B NH2 
10754 N N   . GLY B 257  ? 0.4692 0.4429 0.2929 -0.1425 -0.0053 0.0817  255  GLY B N   
10755 C CA  . GLY B 257  ? 0.4335 0.4041 0.2624 -0.1444 -0.0074 0.0806  255  GLY B CA  
10756 C C   . GLY B 257  ? 0.4216 0.4029 0.2613 -0.1395 -0.0055 0.0761  255  GLY B C   
10757 O O   . GLY B 257  ? 0.4158 0.4075 0.2593 -0.1346 -0.0024 0.0737  255  GLY B O   
10758 N N   . ILE B 258  ? 0.4302 0.4088 0.2747 -0.1408 -0.0075 0.0749  256  ILE B N   
10759 C CA  . ILE B 258  ? 0.3946 0.3802 0.2486 -0.1354 -0.0066 0.0702  256  ILE B CA  
10760 C C   . ILE B 258  ? 0.3604 0.3639 0.2220 -0.1369 -0.0020 0.0701  256  ILE B C   
10761 O O   . ILE B 258  ? 0.3782 0.3894 0.2473 -0.1316 -0.0005 0.0663  256  ILE B O   
10762 C CB  . ILE B 258  ? 0.4477 0.4237 0.3039 -0.1358 -0.0104 0.0687  256  ILE B CB  
10763 C CG1 . ILE B 258  ? 0.4333 0.4090 0.2884 -0.1445 -0.0110 0.0723  256  ILE B CG1 
10764 C CG2 . ILE B 258  ? 0.4341 0.3931 0.2837 -0.1327 -0.0148 0.0681  256  ILE B CG2 
10765 C CD1 . ILE B 258  ? 0.4351 0.4019 0.2921 -0.1452 -0.0146 0.0708  256  ILE B CD1 
10766 N N   . TYR B 259  ? 0.3981 0.4087 0.2578 -0.1439 0.0002  0.0743  257  TYR B N   
10767 C CA  . TYR B 259  ? 0.3966 0.4248 0.2638 -0.1455 0.0045  0.0744  257  TYR B CA  
10768 C C   . TYR B 259  ? 0.4043 0.4439 0.2711 -0.1426 0.0089  0.0744  257  TYR B C   
10769 O O   . TYR B 259  ? 0.3787 0.4290 0.2521 -0.1373 0.0116  0.0712  257  TYR B O   
10770 C CB  . TYR B 259  ? 0.4193 0.4502 0.2860 -0.1550 0.0045  0.0788  257  TYR B CB  
10771 C CG  . TYR B 259  ? 0.4104 0.4289 0.2766 -0.1578 -0.0001 0.0786  257  TYR B CG  
10772 C CD1 . TYR B 259  ? 0.4190 0.4392 0.2927 -0.1546 -0.0011 0.0749  257  TYR B CD1 
10773 C CD2 . TYR B 259  ? 0.4614 0.4660 0.3190 -0.1634 -0.0035 0.0821  257  TYR B CD2 
10774 C CE1 . TYR B 259  ? 0.4316 0.4401 0.3044 -0.1568 -0.0053 0.0745  257  TYR B CE1 
10775 C CE2 . TYR B 259  ? 0.4205 0.4130 0.2771 -0.1655 -0.0078 0.0817  257  TYR B CE2 
10776 C CZ  . TYR B 259  ? 0.4773 0.4720 0.3415 -0.1622 -0.0086 0.0778  257  TYR B CZ  
10777 O OH  . TYR B 259  ? 0.4579 0.4405 0.3208 -0.1641 -0.0127 0.0773  257  TYR B OH  
10778 N N   . GLU B 260  ? 0.3917 0.4284 0.2502 -0.1458 0.0095  0.0780  258  GLU B N   
10779 C CA  . GLU B 260  ? 0.4264 0.4728 0.2833 -0.1427 0.0135  0.0780  258  GLU B CA  
10780 C C   . GLU B 260  ? 0.4458 0.4864 0.3014 -0.1341 0.0125  0.0738  258  GLU B C   
10781 O O   . GLU B 260  ? 0.4384 0.4887 0.2971 -0.1288 0.0157  0.0713  258  GLU B O   
10782 C CB  . GLU B 260  ? 0.4180 0.4624 0.2659 -0.1488 0.0144  0.0831  258  GLU B CB  
10783 C CG  . GLU B 260  ? 0.5131 0.5662 0.3580 -0.1455 0.0184  0.0831  258  GLU B CG  
10784 C CD  . GLU B 260  ? 0.5284 0.5783 0.3640 -0.1509 0.0190  0.0880  258  GLU B CD  
10785 O OE1 . GLU B 260  ? 0.6324 0.6739 0.4656 -0.1566 0.0160  0.0907  258  GLU B OE1 
10786 O OE2 . GLU B 260  ? 0.5802 0.6353 0.4125 -0.1479 0.0218  0.0878  258  GLU B OE2 
10787 N N   . GLY B 261  ? 0.4176 0.4425 0.2687 -0.1325 0.0080  0.0731  259  GLY B N   
10788 C CA  . GLY B 261  ? 0.3854 0.4037 0.2341 -0.1252 0.0066  0.0699  259  GLY B CA  
10789 C C   . GLY B 261  ? 0.3570 0.3769 0.2138 -0.1185 0.0059  0.0647  259  GLY B C   
10790 O O   . GLY B 261  ? 0.3637 0.3863 0.2272 -0.1194 0.0055  0.0635  259  GLY B O   
10791 N N   . PRO B 262  ? 0.3543 0.3722 0.2102 -0.1116 0.0056  0.0615  260  PRO B N   
10792 C CA  . PRO B 262  ? 0.3523 0.3721 0.2157 -0.1051 0.0053  0.0566  260  PRO B CA  
10793 C C   . PRO B 262  ? 0.3527 0.3603 0.2173 -0.1039 0.0007  0.0551  260  PRO B C   
10794 O O   . PRO B 262  ? 0.3846 0.3802 0.2431 -0.1065 -0.0026 0.0573  260  PRO B O   
10795 C CB  . PRO B 262  ? 0.3548 0.3746 0.2150 -0.0990 0.0060  0.0544  260  PRO B CB  
10796 C CG  . PRO B 262  ? 0.3638 0.3748 0.2140 -0.1019 0.0044  0.0578  260  PRO B CG  
10797 C CD  . PRO B 262  ? 0.3594 0.3738 0.2073 -0.1099 0.0059  0.0624  260  PRO B CD  
10798 N N   . GLY B 263  ? 0.3163 0.3271 0.1887 -0.0997 0.0007  0.0514  261  GLY B N   
10799 C CA  . GLY B 263  ? 0.3228 0.3232 0.1971 -0.0975 -0.0032 0.0493  261  GLY B CA  
10800 C C   . GLY B 263  ? 0.3076 0.3089 0.1868 -0.0900 -0.0035 0.0447  261  GLY B C   
10801 O O   . GLY B 263  ? 0.3088 0.3173 0.1890 -0.0863 -0.0010 0.0430  261  GLY B O   
10802 N N   . ILE B 264  ? 0.3090 0.3029 0.1911 -0.0877 -0.0064 0.0426  262  ILE B N   
10803 C CA  . ILE B 264  ? 0.2990 0.2934 0.1863 -0.0810 -0.0069 0.0384  262  ILE B CA  
10804 C C   . ILE B 264  ? 0.3038 0.3001 0.1984 -0.0806 -0.0073 0.0364  262  ILE B C   
10805 O O   . ILE B 264  ? 0.3093 0.3020 0.2038 -0.0849 -0.0086 0.0381  262  ILE B O   
10806 C CB  . ILE B 264  ? 0.3223 0.3047 0.2050 -0.0775 -0.0106 0.0375  262  ILE B CB  
10807 C CG1 . ILE B 264  ? 0.2987 0.2832 0.1861 -0.0707 -0.0106 0.0334  262  ILE B CG1 
10808 C CG2 . ILE B 264  ? 0.3173 0.2888 0.1988 -0.0794 -0.0142 0.0383  262  ILE B CG2 
10809 C CD1 . ILE B 264  ? 0.3257 0.3003 0.2091 -0.0671 -0.0140 0.0325  262  ILE B CD1 
10810 N N   . SER B 265  ? 0.2596 0.2617 0.1606 -0.0755 -0.0061 0.0329  263  SER B N   
10811 C CA  . SER B 265  ? 0.2639 0.2678 0.1720 -0.0742 -0.0064 0.0306  263  SER B CA  
10812 C C   . SER B 265  ? 0.2913 0.2893 0.2014 -0.0683 -0.0086 0.0273  263  SER B C   
10813 O O   . SER B 265  ? 0.3136 0.3128 0.2231 -0.0642 -0.0081 0.0257  263  SER B O   
10814 C CB  . SER B 265  ? 0.3084 0.3258 0.2229 -0.0735 -0.0028 0.0294  263  SER B CB  
10815 O OG  . SER B 265  ? 0.2980 0.3216 0.2124 -0.0793 -0.0010 0.0324  263  SER B OG  
10816 N N   . ILE B 266  ? 0.2612 0.2528 0.1735 -0.0679 -0.0111 0.0263  264  ILE B N   
10817 C CA  . ILE B 266  ? 0.2803 0.2665 0.1950 -0.0625 -0.0132 0.0234  264  ILE B CA  
10818 C C   . ILE B 266  ? 0.2688 0.2586 0.1908 -0.0610 -0.0127 0.0210  264  ILE B C   
10819 O O   . ILE B 266  ? 0.2631 0.2564 0.1872 -0.0644 -0.0119 0.0219  264  ILE B O   
10820 C CB  . ILE B 266  ? 0.2922 0.2656 0.2018 -0.0626 -0.0170 0.0242  264  ILE B CB  
10821 C CG1 . ILE B 266  ? 0.3416 0.3096 0.2506 -0.0665 -0.0186 0.0256  264  ILE B CG1 
10822 C CG2 . ILE B 266  ? 0.3031 0.2726 0.2051 -0.0643 -0.0176 0.0268  264  ILE B CG2 
10823 C CD1 . ILE B 266  ? 0.3476 0.3028 0.2525 -0.0655 -0.0224 0.0259  264  ILE B CD1 
10824 N N   . LYS B 267  ? 0.2476 0.2362 0.1732 -0.0558 -0.0135 0.0180  265  LYS B N   
10825 C CA  . LYS B 267  ? 0.2403 0.2306 0.1722 -0.0538 -0.0136 0.0158  265  LYS B CA  
10826 C C   . LYS B 267  ? 0.2390 0.2193 0.1703 -0.0515 -0.0168 0.0147  265  LYS B C   
10827 O O   . LYS B 267  ? 0.2572 0.2331 0.1865 -0.0484 -0.0183 0.0140  265  LYS B O   
10828 C CB  . LYS B 267  ? 0.2443 0.2429 0.1817 -0.0497 -0.0114 0.0131  265  LYS B CB  
10829 C CG  . LYS B 267  ? 0.2943 0.3037 0.2339 -0.0517 -0.0080 0.0138  265  LYS B CG  
10830 C CD  . LYS B 267  ? 0.3395 0.3561 0.2835 -0.0472 -0.0060 0.0112  265  LYS B CD  
10831 C CE  . LYS B 267  ? 0.3625 0.3901 0.3082 -0.0487 -0.0026 0.0119  265  LYS B CE  
10832 N NZ  . LYS B 267  ? 0.3643 0.3935 0.3045 -0.0518 -0.0015 0.0145  265  LYS B NZ  
10833 N N   . LEU B 268  ? 0.2370 0.2138 0.1695 -0.0530 -0.0180 0.0147  266  LEU B N   
10834 C CA  . LEU B 268  ? 0.2638 0.2315 0.1959 -0.0504 -0.0209 0.0135  266  LEU B CA  
10835 C C   . LEU B 268  ? 0.2626 0.2323 0.1997 -0.0448 -0.0208 0.0105  266  LEU B C   
10836 O O   . LEU B 268  ? 0.2529 0.2162 0.1889 -0.0418 -0.0230 0.0097  266  LEU B O   
10837 C CB  . LEU B 268  ? 0.2522 0.2163 0.1849 -0.0528 -0.0219 0.0137  266  LEU B CB  
10838 C CG  . LEU B 268  ? 0.2882 0.2487 0.2153 -0.0587 -0.0226 0.0168  266  LEU B CG  
10839 C CD1 . LEU B 268  ? 0.2950 0.2505 0.2221 -0.0608 -0.0241 0.0167  266  LEU B CD1 
10840 C CD2 . LEU B 268  ? 0.3297 0.2821 0.2499 -0.0594 -0.0246 0.0188  266  LEU B CD2 
10841 N N   . SER B 269  ? 0.2515 0.2300 0.1940 -0.0433 -0.0184 0.0088  267  SER B N   
10842 C CA  . SER B 269  ? 0.2657 0.2461 0.2128 -0.0383 -0.0183 0.0061  267  SER B CA  
10843 C C   . SER B 269  ? 0.2425 0.2215 0.1872 -0.0358 -0.0190 0.0059  267  SER B C   
10844 O O   . SER B 269  ? 0.2490 0.2269 0.1965 -0.0319 -0.0199 0.0039  267  SER B O   
10845 C CB  . SER B 269  ? 0.2546 0.2445 0.2074 -0.0374 -0.0156 0.0046  267  SER B CB  
10846 O OG  . SER B 269  ? 0.2605 0.2566 0.2120 -0.0382 -0.0135 0.0054  267  SER B OG  
10847 N N   . ALA B 270  ? 0.2290 0.2081 0.1687 -0.0381 -0.0186 0.0078  268  ALA B N   
10848 C CA  . ALA B 270  ? 0.2582 0.2351 0.1947 -0.0360 -0.0196 0.0077  268  ALA B CA  
10849 C C   . ALA B 270  ? 0.2658 0.2332 0.1993 -0.0348 -0.0230 0.0081  268  ALA B C   
10850 O O   . ALA B 270  ? 0.2635 0.2287 0.1960 -0.0320 -0.0244 0.0074  268  ALA B O   
10851 C CB  . ALA B 270  ? 0.2519 0.2310 0.1830 -0.0391 -0.0182 0.0100  268  ALA B CB  
10852 N N   . LEU B 271  ? 0.2557 0.2172 0.1875 -0.0369 -0.0244 0.0093  269  LEU B N   
10853 C CA  . LEU B 271  ? 0.2850 0.2369 0.2124 -0.0363 -0.0276 0.0103  269  LEU B CA  
10854 C C   . LEU B 271  ? 0.2629 0.2109 0.1940 -0.0326 -0.0295 0.0083  269  LEU B C   
10855 O O   . LEU B 271  ? 0.2914 0.2317 0.2195 -0.0313 -0.0323 0.0088  269  LEU B O   
10856 C CB  . LEU B 271  ? 0.2826 0.2290 0.2042 -0.0409 -0.0285 0.0131  269  LEU B CB  
10857 C CG  . LEU B 271  ? 0.2985 0.2478 0.2154 -0.0446 -0.0270 0.0155  269  LEU B CG  
10858 C CD1 . LEU B 271  ? 0.3327 0.2769 0.2445 -0.0497 -0.0277 0.0184  269  LEU B CD1 
10859 C CD2 . LEU B 271  ? 0.2942 0.2406 0.2069 -0.0426 -0.0283 0.0160  269  LEU B CD2 
10860 N N   . HIS B 272  ? 0.2405 0.1937 0.1781 -0.0307 -0.0281 0.0061  270  HIS B N   
10861 C CA  . HIS B 272  ? 0.2577 0.2079 0.1989 -0.0271 -0.0296 0.0043  270  HIS B CA  
10862 C C   . HIS B 272  ? 0.2338 0.1916 0.1819 -0.0249 -0.0275 0.0019  270  HIS B C   
10863 O O   . HIS B 272  ? 0.2615 0.2252 0.2116 -0.0268 -0.0252 0.0019  270  HIS B O   
10864 C CB  . HIS B 272  ? 0.2856 0.2300 0.2255 -0.0286 -0.0307 0.0048  270  HIS B CB  
10865 C CG  . HIS B 272  ? 0.2669 0.2063 0.2087 -0.0247 -0.0328 0.0034  270  HIS B CG  
10866 N ND1 . HIS B 272  ? 0.3127 0.2558 0.2607 -0.0217 -0.0320 0.0010  270  HIS B ND1 
10867 C CD2 . HIS B 272  ? 0.3404 0.2715 0.2785 -0.0232 -0.0357 0.0040  270  HIS B CD2 
10868 C CE1 . HIS B 272  ? 0.3347 0.2727 0.2831 -0.0185 -0.0341 0.0003  270  HIS B CE1 
10869 N NE2 . HIS B 272  ? 0.3330 0.2636 0.2755 -0.0192 -0.0364 0.0020  270  HIS B NE2 
10870 N N   . PRO B 273  ? 0.2358 0.1940 0.1877 -0.0209 -0.0284 0.0001  271  PRO B N   
10871 C CA  . PRO B 273  ? 0.2380 0.2031 0.1964 -0.0189 -0.0265 -0.0020 271  PRO B CA  
10872 C C   . PRO B 273  ? 0.2360 0.2020 0.1981 -0.0188 -0.0257 -0.0030 271  PRO B C   
10873 O O   . PRO B 273  ? 0.2535 0.2253 0.2205 -0.0177 -0.0239 -0.0045 271  PRO B O   
10874 C CB  . PRO B 273  ? 0.2697 0.2338 0.2303 -0.0150 -0.0282 -0.0034 271  PRO B CB  
10875 C CG  . PRO B 273  ? 0.2764 0.2328 0.2334 -0.0145 -0.0310 -0.0023 271  PRO B CG  
10876 C CD  . PRO B 273  ? 0.2576 0.2103 0.2080 -0.0182 -0.0312 0.0000  271  PRO B CD  
10877 N N   . ARG B 274  ? 0.2366 0.1967 0.1962 -0.0199 -0.0270 -0.0022 272  ARG B N   
10878 C CA  . ARG B 274  ? 0.2638 0.2241 0.2262 -0.0199 -0.0264 -0.0031 272  ARG B CA  
10879 C C   . ARG B 274  ? 0.2581 0.2159 0.2167 -0.0241 -0.0263 -0.0015 272  ARG B C   
10880 O O   . ARG B 274  ? 0.2708 0.2229 0.2276 -0.0246 -0.0275 -0.0014 272  ARG B O   
10881 C CB  . ARG B 274  ? 0.2522 0.2077 0.2161 -0.0165 -0.0282 -0.0043 272  ARG B CB  
10882 C CG  . ARG B 274  ? 0.2632 0.2219 0.2319 -0.0126 -0.0283 -0.0059 272  ARG B CG  
10883 C CD  . ARG B 274  ? 0.2779 0.2445 0.2520 -0.0120 -0.0259 -0.0073 272  ARG B CD  
10884 N NE  . ARG B 274  ? 0.2587 0.2266 0.2351 -0.0125 -0.0247 -0.0080 272  ARG B NE  
10885 C CZ  . ARG B 274  ? 0.2457 0.2122 0.2248 -0.0100 -0.0250 -0.0093 272  ARG B CZ  
10886 N NH1 . ARG B 274  ? 0.2538 0.2178 0.2341 -0.0069 -0.0266 -0.0099 272  ARG B NH1 
10887 N NH2 . ARG B 274  ? 0.2663 0.2344 0.2472 -0.0107 -0.0238 -0.0099 272  ARG B NH2 
10888 N N   . TYR B 275  ? 0.2434 0.2055 0.2004 -0.0273 -0.0247 -0.0002 273  TYR B N   
10889 C CA  . TYR B 275  ? 0.2619 0.2230 0.2158 -0.0318 -0.0244 0.0015  273  TYR B CA  
10890 C C   . TYR B 275  ? 0.2673 0.2330 0.2254 -0.0324 -0.0229 0.0003  273  TYR B C   
10891 O O   . TYR B 275  ? 0.2510 0.2247 0.2123 -0.0330 -0.0206 0.0000  273  TYR B O   
10892 C CB  . TYR B 275  ? 0.2332 0.1981 0.1842 -0.0349 -0.0232 0.0033  273  TYR B CB  
10893 C CG  . TYR B 275  ? 0.2357 0.2008 0.1840 -0.0399 -0.0226 0.0053  273  TYR B CG  
10894 C CD1 . TYR B 275  ? 0.2518 0.2089 0.1961 -0.0422 -0.0247 0.0064  273  TYR B CD1 
10895 C CD2 . TYR B 275  ? 0.2465 0.2201 0.1964 -0.0424 -0.0202 0.0060  273  TYR B CD2 
10896 C CE1 . TYR B 275  ? 0.2698 0.2269 0.2115 -0.0473 -0.0244 0.0082  273  TYR B CE1 
10897 C CE2 . TYR B 275  ? 0.2299 0.2045 0.1778 -0.0473 -0.0197 0.0079  273  TYR B CE2 
10898 C CZ  . TYR B 275  ? 0.2640 0.2303 0.2078 -0.0499 -0.0219 0.0090  273  TYR B CZ  
10899 O OH  . TYR B 275  ? 0.2827 0.2496 0.2244 -0.0552 -0.0218 0.0110  273  TYR B OH  
10900 N N   . SER B 276  ? 0.2480 0.2086 0.2060 -0.0319 -0.0242 -0.0004 274  SER B N   
10901 C CA  . SER B 276  ? 0.2412 0.2056 0.2028 -0.0322 -0.0230 -0.0015 274  SER B CA  
10902 C C   . SER B 276  ? 0.2505 0.2071 0.2093 -0.0329 -0.0248 -0.0017 274  SER B C   
10903 O O   . SER B 276  ? 0.2511 0.1998 0.2065 -0.0315 -0.0270 -0.0015 274  SER B O   
10904 C CB  . SER B 276  ? 0.2950 0.2646 0.2626 -0.0280 -0.0217 -0.0038 274  SER B CB  
10905 O OG  . SER B 276  ? 0.3250 0.2892 0.2930 -0.0245 -0.0233 -0.0050 274  SER B OG  
10906 N N   . ARG B 277  ? 0.2332 0.1920 0.1932 -0.0349 -0.0242 -0.0020 275  ARG B N   
10907 C CA  . ARG B 277  ? 0.2342 0.1854 0.1912 -0.0355 -0.0259 -0.0024 275  ARG B CA  
10908 C C   . ARG B 277  ? 0.2523 0.1997 0.2110 -0.0305 -0.0268 -0.0044 275  ARG B C   
10909 O O   . ARG B 277  ? 0.2567 0.1954 0.2114 -0.0299 -0.0288 -0.0046 275  ARG B O   
10910 C CB  . ARG B 277  ? 0.2472 0.2026 0.2059 -0.0383 -0.0250 -0.0026 275  ARG B CB  
10911 C CG  . ARG B 277  ? 0.2669 0.2150 0.2229 -0.0386 -0.0267 -0.0035 275  ARG B CG  
10912 C CD  . ARG B 277  ? 0.2588 0.1968 0.2077 -0.0412 -0.0292 -0.0019 275  ARG B CD  
10913 N NE  . ARG B 277  ? 0.2832 0.2136 0.2290 -0.0414 -0.0309 -0.0029 275  ARG B NE  
10914 C CZ  . ARG B 277  ? 0.2674 0.1913 0.2121 -0.0372 -0.0321 -0.0046 275  ARG B CZ  
10915 N NH1 . ARG B 277  ? 0.3031 0.2274 0.2501 -0.0326 -0.0318 -0.0054 275  ARG B NH1 
10916 N NH2 . ARG B 277  ? 0.2864 0.2031 0.2275 -0.0377 -0.0337 -0.0054 275  ARG B NH2 
10917 N N   . ALA B 278  ? 0.2429 0.1964 0.2071 -0.0269 -0.0252 -0.0059 276  ALA B N   
10918 C CA  . ALA B 278  ? 0.2309 0.1818 0.1972 -0.0223 -0.0258 -0.0077 276  ALA B CA  
10919 C C   . ALA B 278  ? 0.2522 0.1965 0.2153 -0.0203 -0.0278 -0.0073 276  ALA B C   
10920 O O   . ALA B 278  ? 0.2713 0.2110 0.2344 -0.0169 -0.0289 -0.0084 276  ALA B O   
10921 C CB  . ALA B 278  ? 0.2803 0.2393 0.2530 -0.0194 -0.0238 -0.0091 276  ALA B CB  
10922 N N   . GLN B 279  ? 0.2602 0.2042 0.2208 -0.0220 -0.0283 -0.0056 277  GLN B N   
10923 C CA  . GLN B 279  ? 0.2481 0.1858 0.2054 -0.0204 -0.0304 -0.0049 277  GLN B CA  
10924 C C   . GLN B 279  ? 0.2644 0.1945 0.2146 -0.0241 -0.0322 -0.0028 277  GLN B C   
10925 O O   . GLN B 279  ? 0.2663 0.1933 0.2131 -0.0244 -0.0334 -0.0014 277  GLN B O   
10926 C CB  . GLN B 279  ? 0.2695 0.2120 0.2291 -0.0188 -0.0298 -0.0047 277  GLN B CB  
10927 C CG  . GLN B 279  ? 0.2663 0.2155 0.2326 -0.0154 -0.0283 -0.0067 277  GLN B CG  
10928 C CD  . GLN B 279  ? 0.3031 0.2489 0.2712 -0.0112 -0.0295 -0.0081 277  GLN B CD  
10929 O OE1 . GLN B 279  ? 0.3556 0.2942 0.3201 -0.0100 -0.0316 -0.0077 277  GLN B OE1 
10930 N NE2 . GLN B 279  ? 0.2801 0.2310 0.2537 -0.0090 -0.0280 -0.0098 277  GLN B NE2 
10931 N N   . ALA B 280  ? 0.2749 0.2018 0.2225 -0.0270 -0.0325 -0.0026 278  ALA B N   
10932 C CA  . ALA B 280  ? 0.2947 0.2149 0.2356 -0.0313 -0.0340 -0.0004 278  ALA B CA  
10933 C C   . ALA B 280  ? 0.3016 0.2119 0.2373 -0.0295 -0.0368 0.0004  278  ALA B C   
10934 O O   . ALA B 280  ? 0.3071 0.2135 0.2378 -0.0324 -0.0379 0.0026  278  ALA B O   
10935 C CB  . ALA B 280  ? 0.3038 0.2213 0.2428 -0.0344 -0.0343 -0.0005 278  ALA B CB  
10936 N N   . ALA B 281  ? 0.3094 0.2157 0.2461 -0.0248 -0.0380 -0.0014 279  ALA B N   
10937 C CA  . ALA B 281  ? 0.3109 0.2078 0.2427 -0.0226 -0.0407 -0.0008 279  ALA B CA  
10938 C C   . ALA B 281  ? 0.3017 0.2009 0.2336 -0.0219 -0.0410 0.0005  279  ALA B C   
10939 O O   . ALA B 281  ? 0.3372 0.2295 0.2631 -0.0233 -0.0430 0.0024  279  ALA B O   
10940 C CB  . ALA B 281  ? 0.3511 0.2451 0.2850 -0.0170 -0.0415 -0.0030 279  ALA B CB  
10941 N N   . ARG B 282  ? 0.2755 0.1838 0.2134 -0.0199 -0.0391 -0.0005 280  ARG B N   
10942 C CA  . ARG B 282  ? 0.2779 0.1885 0.2157 -0.0193 -0.0394 0.0006  280  ARG B CA  
10943 C C   . ARG B 282  ? 0.2833 0.1952 0.2173 -0.0245 -0.0387 0.0029  280  ARG B C   
10944 O O   . ARG B 282  ? 0.2956 0.2046 0.2256 -0.0251 -0.0400 0.0046  280  ARG B O   
10945 C CB  . ARG B 282  ? 0.3010 0.2208 0.2460 -0.0163 -0.0376 -0.0012 280  ARG B CB  
10946 C CG  . ARG B 282  ? 0.3170 0.2362 0.2659 -0.0110 -0.0384 -0.0031 280  ARG B CG  
10947 C CD  . ARG B 282  ? 0.3128 0.2404 0.2680 -0.0086 -0.0371 -0.0043 280  ARG B CD  
10948 N NE  . ARG B 282  ? 0.3035 0.2309 0.2567 -0.0085 -0.0383 -0.0031 280  ARG B NE  
10949 C CZ  . ARG B 282  ? 0.2950 0.2290 0.2518 -0.0077 -0.0373 -0.0036 280  ARG B CZ  
10950 N NH1 . ARG B 282  ? 0.2997 0.2410 0.2624 -0.0070 -0.0351 -0.0052 280  ARG B NH1 
10951 N NH2 . ARG B 282  ? 0.3104 0.2432 0.2644 -0.0077 -0.0387 -0.0025 280  ARG B NH2 
10952 N N   . VAL B 283  ? 0.2748 0.1912 0.2099 -0.0281 -0.0367 0.0031  281  VAL B N   
10953 C CA  . VAL B 283  ? 0.2879 0.2064 0.2198 -0.0331 -0.0359 0.0054  281  VAL B CA  
10954 C C   . VAL B 283  ? 0.2983 0.2065 0.2222 -0.0360 -0.0383 0.0077  281  VAL B C   
10955 O O   . VAL B 283  ? 0.3008 0.2074 0.2205 -0.0379 -0.0389 0.0098  281  VAL B O   
10956 C CB  . VAL B 283  ? 0.2791 0.2045 0.2141 -0.0363 -0.0334 0.0051  281  VAL B CB  
10957 C CG1 . VAL B 283  ? 0.3074 0.2340 0.2385 -0.0420 -0.0328 0.0077  281  VAL B CG1 
10958 C CG2 . VAL B 283  ? 0.2780 0.2136 0.2201 -0.0337 -0.0310 0.0033  281  VAL B CG2 
10959 N N   . MET B 284  ? 0.2920 0.1927 0.2134 -0.0362 -0.0400 0.0073  282  MET B N   
10960 C CA  . MET B 284  ? 0.2925 0.1824 0.2059 -0.0390 -0.0426 0.0095  282  MET B CA  
10961 C C   . MET B 284  ? 0.3371 0.2202 0.2470 -0.0356 -0.0450 0.0100  282  MET B C   
10962 O O   . MET B 284  ? 0.3635 0.2401 0.2669 -0.0382 -0.0467 0.0125  282  MET B O   
10963 C CB  . MET B 284  ? 0.3258 0.2087 0.2370 -0.0397 -0.0439 0.0087  282  MET B CB  
10964 C CG  . MET B 284  ? 0.3024 0.1914 0.2164 -0.0436 -0.0418 0.0083  282  MET B CG  
10965 S SD  . MET B 284  ? 0.3663 0.2601 0.2778 -0.0509 -0.0405 0.0115  282  MET B SD  
10966 C CE  . MET B 284  ? 0.3860 0.2654 0.2875 -0.0549 -0.0439 0.0140  282  MET B CE  
10967 N N   . GLY B 285  ? 0.3236 0.2081 0.2378 -0.0299 -0.0453 0.0079  283  GLY B N   
10968 C CA  . GLY B 285  ? 0.3473 0.2257 0.2587 -0.0263 -0.0479 0.0082  283  GLY B CA  
10969 C C   . GLY B 285  ? 0.3426 0.2254 0.2541 -0.0262 -0.0476 0.0094  283  GLY B C   
10970 O O   . GLY B 285  ? 0.3860 0.2624 0.2926 -0.0254 -0.0499 0.0109  283  GLY B O   
10971 N N   . GLU B 286  ? 0.3163 0.2096 0.2330 -0.0268 -0.0448 0.0087  284  GLU B N   
10972 C CA  . GLU B 286  ? 0.3139 0.2122 0.2315 -0.0259 -0.0444 0.0092  284  GLU B CA  
10973 C C   . GLU B 286  ? 0.3336 0.2375 0.2498 -0.0305 -0.0422 0.0108  284  GLU B C   
10974 O O   . GLU B 286  ? 0.3692 0.2725 0.2816 -0.0315 -0.0427 0.0125  284  GLU B O   
10975 C CB  . GLU B 286  ? 0.3147 0.2207 0.2401 -0.0214 -0.0432 0.0065  284  GLU B CB  
10976 C CG  . GLU B 286  ? 0.3340 0.2362 0.2620 -0.0166 -0.0449 0.0047  284  GLU B CG  
10977 C CD  . GLU B 286  ? 0.3737 0.2841 0.3098 -0.0130 -0.0433 0.0022  284  GLU B CD  
10978 O OE1 . GLU B 286  ? 0.3648 0.2826 0.3041 -0.0132 -0.0418 0.0019  284  GLU B OE1 
10979 O OE2 . GLU B 286  ? 0.3687 0.2780 0.3080 -0.0099 -0.0437 0.0005  284  GLU B OE2 
10980 N N   . LEU B 287  ? 0.3095 0.2192 0.2286 -0.0333 -0.0397 0.0104  285  LEU B N   
10981 C CA  . LEU B 287  ? 0.3168 0.2329 0.2350 -0.0375 -0.0374 0.0120  285  LEU B CA  
10982 C C   . LEU B 287  ? 0.3493 0.2591 0.2602 -0.0426 -0.0384 0.0150  285  LEU B C   
10983 O O   . LEU B 287  ? 0.3094 0.2200 0.2163 -0.0449 -0.0380 0.0171  285  LEU B O   
10984 C CB  . LEU B 287  ? 0.3029 0.2278 0.2271 -0.0385 -0.0344 0.0105  285  LEU B CB  
10985 C CG  . LEU B 287  ? 0.3213 0.2561 0.2475 -0.0407 -0.0314 0.0110  285  LEU B CG  
10986 C CD1 . LEU B 287  ? 0.2937 0.2362 0.2263 -0.0404 -0.0291 0.0092  285  LEU B CD1 
10987 C CD2 . LEU B 287  ? 0.3374 0.2714 0.2581 -0.0462 -0.0310 0.0140  285  LEU B CD2 
10988 N N   . LEU B 288  ? 0.3329 0.2359 0.2414 -0.0443 -0.0397 0.0154  286  LEU B N   
10989 C CA  . LEU B 288  ? 0.3239 0.2202 0.2252 -0.0496 -0.0409 0.0183  286  LEU B CA  
10990 C C   . LEU B 288  ? 0.3458 0.2350 0.2402 -0.0499 -0.0431 0.0207  286  LEU B C   
10991 O O   . LEU B 288  ? 0.3376 0.2275 0.2278 -0.0545 -0.0424 0.0234  286  LEU B O   
10992 C CB  . LEU B 288  ? 0.3733 0.2620 0.2730 -0.0506 -0.0426 0.0179  286  LEU B CB  
10993 C CG  . LEU B 288  ? 0.4037 0.2832 0.2953 -0.0558 -0.0445 0.0209  286  LEU B CG  
10994 C CD1 . LEU B 288  ? 0.3975 0.2838 0.2885 -0.0621 -0.0422 0.0232  286  LEU B CD1 
10995 C CD2 . LEU B 288  ? 0.4489 0.3198 0.3385 -0.0559 -0.0465 0.0200  286  LEU B CD2 
10996 N N   . PRO B 289  ? 0.3404 0.2231 0.2334 -0.0453 -0.0456 0.0199  287  PRO B N   
10997 C CA  . PRO B 289  ? 0.3625 0.2387 0.2487 -0.0455 -0.0478 0.0222  287  PRO B CA  
10998 C C   . PRO B 289  ? 0.3399 0.2237 0.2261 -0.0468 -0.0458 0.0233  287  PRO B C   
10999 O O   . PRO B 289  ? 0.3695 0.2493 0.2490 -0.0498 -0.0466 0.0262  287  PRO B O   
11000 C CB  . PRO B 289  ? 0.4014 0.2724 0.2887 -0.0393 -0.0504 0.0205  287  PRO B CB  
11001 C CG  . PRO B 289  ? 0.4113 0.2811 0.3026 -0.0373 -0.0504 0.0181  287  PRO B CG  
11002 C CD  . PRO B 289  ? 0.3734 0.2537 0.2705 -0.0398 -0.0469 0.0171  287  PRO B CD  
11003 N N   . ARG B 290  ? 0.3141 0.2085 0.2072 -0.0447 -0.0432 0.0212  288  ARG B N   
11004 C CA  A ARG B 290  ? 0.3351 0.2369 0.2280 -0.0457 -0.0412 0.0219  288  ARG B CA  
11005 C CA  B ARG B 290  ? 0.3351 0.2369 0.2281 -0.0457 -0.0412 0.0219  288  ARG B CA  
11006 C C   . ARG B 290  ? 0.3045 0.2101 0.1949 -0.0517 -0.0389 0.0243  288  ARG B C   
11007 O O   . ARG B 290  ? 0.3325 0.2385 0.2179 -0.0542 -0.0385 0.0266  288  ARG B O   
11008 C CB  A ARG B 290  ? 0.3425 0.2539 0.2432 -0.0418 -0.0392 0.0189  288  ARG B CB  
11009 C CB  B ARG B 290  ? 0.3423 0.2538 0.2431 -0.0419 -0.0391 0.0189  288  ARG B CB  
11010 C CG  A ARG B 290  ? 0.3629 0.2715 0.2658 -0.0362 -0.0414 0.0170  288  ARG B CG  
11011 C CG  B ARG B 290  ? 0.3621 0.2708 0.2656 -0.0361 -0.0413 0.0168  288  ARG B CG  
11012 C CD  A ARG B 290  ? 0.3599 0.2763 0.2712 -0.0327 -0.0398 0.0138  288  ARG B CD  
11013 C CD  B ARG B 290  ? 0.3623 0.2802 0.2737 -0.0328 -0.0393 0.0139  288  ARG B CD  
11014 N NE  A ARG B 290  ? 0.3776 0.2909 0.2915 -0.0276 -0.0421 0.0121  288  ARG B NE  
11015 N NE  B ARG B 290  ? 0.3413 0.2598 0.2535 -0.0289 -0.0407 0.0129  288  ARG B NE  
11016 C CZ  A ARG B 290  ? 0.3639 0.2819 0.2848 -0.0242 -0.0413 0.0094  288  ARG B CZ  
11017 C CZ  B ARG B 290  ? 0.3695 0.2939 0.2880 -0.0254 -0.0399 0.0104  288  ARG B CZ  
11018 N NH1 A ARG B 290  ? 0.3285 0.2540 0.2545 -0.0250 -0.0385 0.0081  288  ARG B NH1 
11019 N NH1 B ARG B 290  ? 0.3601 0.2902 0.2847 -0.0249 -0.0378 0.0085  288  ARG B NH1 
11020 N NH2 A ARG B 290  ? 0.3669 0.2821 0.2899 -0.0198 -0.0436 0.0082  288  ARG B NH2 
11021 N NH2 B ARG B 290  ? 0.3571 0.2816 0.2756 -0.0225 -0.0414 0.0097  288  ARG B NH2 
11022 N N   . VAL B 291  ? 0.3270 0.2357 0.2206 -0.0543 -0.0374 0.0238  289  VAL B N   
11023 C CA  . VAL B 291  ? 0.3138 0.2266 0.2053 -0.0603 -0.0354 0.0263  289  VAL B CA  
11024 C C   . VAL B 291  ? 0.3161 0.2190 0.1988 -0.0644 -0.0376 0.0297  289  VAL B C   
11025 O O   . VAL B 291  ? 0.3362 0.2413 0.2149 -0.0687 -0.0364 0.0325  289  VAL B O   
11026 C CB  . VAL B 291  ? 0.3428 0.2606 0.2394 -0.0622 -0.0338 0.0252  289  VAL B CB  
11027 C CG1 . VAL B 291  ? 0.3469 0.2704 0.2420 -0.0684 -0.0315 0.0277  289  VAL B CG1 
11028 C CG2 . VAL B 291  ? 0.3659 0.2924 0.2707 -0.0578 -0.0318 0.0219  289  VAL B CG2 
11029 N N   . LYS B 292  ? 0.3298 0.2216 0.2095 -0.0633 -0.0409 0.0297  290  LYS B N   
11030 C CA  . LYS B 292  ? 0.3481 0.2292 0.2190 -0.0672 -0.0434 0.0329  290  LYS B CA  
11031 C C   . LYS B 292  ? 0.3737 0.2531 0.2391 -0.0670 -0.0439 0.0350  290  LYS B C   
11032 O O   . LYS B 292  ? 0.3846 0.2616 0.2438 -0.0720 -0.0439 0.0384  290  LYS B O   
11033 C CB  . LYS B 292  ? 0.3874 0.2564 0.2558 -0.0649 -0.0469 0.0321  290  LYS B CB  
11034 C CG  . LYS B 292  ? 0.4496 0.3064 0.3085 -0.0690 -0.0497 0.0355  290  LYS B CG  
11035 C CD  . LYS B 292  ? 0.4957 0.3447 0.3488 -0.0663 -0.0524 0.0368  290  LYS B CD  
11036 C CE  . LYS B 292  ? 0.4906 0.3272 0.3337 -0.0708 -0.0551 0.0405  290  LYS B CE  
11037 N NZ  . LYS B 292  ? 0.4997 0.3256 0.3406 -0.0705 -0.0578 0.0397  290  LYS B NZ  
11038 N N   . ALA B 293  ? 0.3644 0.2452 0.2321 -0.0614 -0.0445 0.0331  291  ALA B N   
11039 C CA  . ALA B 293  ? 0.3735 0.2527 0.2361 -0.0608 -0.0453 0.0348  291  ALA B CA  
11040 C C   . ALA B 293  ? 0.3787 0.2674 0.2408 -0.0645 -0.0419 0.0364  291  ALA B C   
11041 O O   . ALA B 293  ? 0.3664 0.2523 0.2215 -0.0677 -0.0422 0.0394  291  ALA B O   
11042 C CB  . ALA B 293  ? 0.3640 0.2443 0.2301 -0.0542 -0.0465 0.0321  291  ALA B CB  
11043 N N   . LEU B 294  ? 0.3453 0.2454 0.2146 -0.0640 -0.0386 0.0343  292  LEU B N   
11044 C CA  . LEU B 294  ? 0.3648 0.2746 0.2341 -0.0672 -0.0351 0.0356  292  LEU B CA  
11045 C C   . LEU B 294  ? 0.3623 0.2712 0.2274 -0.0742 -0.0342 0.0390  292  LEU B C   
11046 O O   . LEU B 294  ? 0.3493 0.2606 0.2097 -0.0777 -0.0328 0.0417  292  LEU B O   
11047 C CB  . LEU B 294  ? 0.3463 0.2679 0.2243 -0.0649 -0.0319 0.0325  292  LEU B CB  
11048 C CG  . LEU B 294  ? 0.3278 0.2518 0.2103 -0.0584 -0.0323 0.0292  292  LEU B CG  
11049 C CD1 . LEU B 294  ? 0.3200 0.2544 0.2109 -0.0568 -0.0294 0.0264  292  LEU B CD1 
11050 C CD2 . LEU B 294  ? 0.3629 0.2875 0.2410 -0.0571 -0.0323 0.0299  292  LEU B CD2 
11051 N N   . ALA B 295  ? 0.3433 0.2487 0.2099 -0.0764 -0.0351 0.0389  293  ALA B N   
11052 C CA  . ALA B 295  ? 0.3774 0.2814 0.2401 -0.0834 -0.0347 0.0422  293  ALA B CA  
11053 C C   . ALA B 295  ? 0.3917 0.2847 0.2446 -0.0863 -0.0373 0.0457  293  ALA B C   
11054 O O   . ALA B 295  ? 0.3771 0.2715 0.2254 -0.0920 -0.0361 0.0492  293  ALA B O   
11055 C CB  . ALA B 295  ? 0.3749 0.2761 0.2408 -0.0847 -0.0357 0.0411  293  ALA B CB  
11056 N N   . LEU B 296  ? 0.3817 0.2639 0.2312 -0.0824 -0.0409 0.0451  294  LEU B N   
11057 C CA  . LEU B 296  ? 0.3996 0.2707 0.2394 -0.0846 -0.0436 0.0485  294  LEU B CA  
11058 C C   . LEU B 296  ? 0.3994 0.2756 0.2355 -0.0856 -0.0419 0.0505  294  LEU B C   
11059 O O   . LEU B 296  ? 0.4163 0.2887 0.2450 -0.0906 -0.0421 0.0543  294  LEU B O   
11060 C CB  . LEU B 296  ? 0.4285 0.2883 0.2663 -0.0792 -0.0477 0.0470  294  LEU B CB  
11061 C CG  . LEU B 296  ? 0.4920 0.3387 0.3197 -0.0807 -0.0512 0.0503  294  LEU B CG  
11062 C CD1 . LEU B 296  ? 0.5258 0.3665 0.3476 -0.0880 -0.0517 0.0538  294  LEU B CD1 
11063 C CD2 . LEU B 296  ? 0.5510 0.3872 0.3778 -0.0748 -0.0551 0.0485  294  LEU B CD2 
11064 N N   . LEU B 297  ? 0.3904 0.2751 0.2313 -0.0809 -0.0401 0.0479  295  LEU B N   
11065 C CA  . LEU B 297  ? 0.4026 0.2928 0.2400 -0.0817 -0.0381 0.0495  295  LEU B CA  
11066 C C   . LEU B 297  ? 0.4012 0.3006 0.2387 -0.0876 -0.0343 0.0517  295  LEU B C   
11067 O O   . LEU B 297  ? 0.4000 0.2991 0.2309 -0.0915 -0.0335 0.0551  295  LEU B O   
11068 C CB  . LEU B 297  ? 0.3955 0.2930 0.2383 -0.0755 -0.0370 0.0460  295  LEU B CB  
11069 C CG  . LEU B 297  ? 0.4619 0.3521 0.3040 -0.0695 -0.0405 0.0441  295  LEU B CG  
11070 C CD1 . LEU B 297  ? 0.4348 0.3338 0.2838 -0.0642 -0.0389 0.0404  295  LEU B CD1 
11071 C CD2 . LEU B 297  ? 0.5005 0.3827 0.3331 -0.0703 -0.0428 0.0471  295  LEU B CD2 
11072 N N   . ALA B 298  ? 0.3837 0.2917 0.2287 -0.0885 -0.0319 0.0500  296  ALA B N   
11073 C CA  . ALA B 298  ? 0.3964 0.3141 0.2424 -0.0940 -0.0282 0.0521  296  ALA B CA  
11074 C C   . ALA B 298  ? 0.4126 0.3230 0.2517 -0.1011 -0.0296 0.0564  296  ALA B C   
11075 O O   . ALA B 298  ? 0.4172 0.3323 0.2526 -0.1060 -0.0274 0.0596  296  ALA B O   
11076 C CB  . ALA B 298  ? 0.3750 0.3023 0.2304 -0.0934 -0.0260 0.0493  296  ALA B CB  
11077 N N   . LYS B 299  ? 0.4051 0.3040 0.2422 -0.1016 -0.0332 0.0565  297  LYS B N   
11078 C CA  . LYS B 299  ? 0.4453 0.3353 0.2751 -0.1083 -0.0350 0.0606  297  LYS B CA  
11079 C C   . LYS B 299  ? 0.4782 0.3620 0.2986 -0.1099 -0.0361 0.0640  297  LYS B C   
11080 O O   . LYS B 299  ? 0.4843 0.3682 0.2994 -0.1164 -0.0352 0.0681  297  LYS B O   
11081 C CB  . LYS B 299  ? 0.4653 0.3427 0.2940 -0.1074 -0.0390 0.0596  297  LYS B CB  
11082 C CG  . LYS B 299  ? 0.5135 0.3793 0.3335 -0.1138 -0.0416 0.0637  297  LYS B CG  
11083 C CD  . LYS B 299  ? 0.5750 0.4247 0.3901 -0.1106 -0.0464 0.0631  297  LYS B CD  
11084 C CE  . LYS B 299  ? 0.5875 0.4250 0.3940 -0.1172 -0.0491 0.0670  297  LYS B CE  
11085 N NZ  . LYS B 299  ? 0.6870 0.5217 0.4850 -0.1214 -0.0491 0.0715  297  LYS B NZ  
11086 N N   . ASN B 300  ? 0.4398 0.3183 0.2579 -0.1041 -0.0381 0.0626  298  ASN B N   
11087 C CA  . ASN B 300  ? 0.4375 0.3091 0.2461 -0.1053 -0.0395 0.0659  298  ASN B CA  
11088 C C   . ASN B 300  ? 0.4692 0.3518 0.2764 -0.1083 -0.0355 0.0679  298  ASN B C   
11089 O O   . ASN B 300  ? 0.5025 0.3810 0.3014 -0.1126 -0.0358 0.0720  298  ASN B O   
11090 C CB  . ASN B 300  ? 0.4599 0.3249 0.2673 -0.0981 -0.0425 0.0636  298  ASN B CB  
11091 C CG  . ASN B 300  ? 0.5144 0.3663 0.3207 -0.0957 -0.0469 0.0626  298  ASN B CG  
11092 O OD1 . ASN B 300  ? 0.6431 0.4875 0.4462 -0.1001 -0.0484 0.0646  298  ASN B OD1 
11093 N ND2 . ASN B 300  ? 0.6124 0.4615 0.4214 -0.0887 -0.0490 0.0595  298  ASN B ND2 
11094 N N   . TYR B 301  ? 0.4197 0.3161 0.2345 -0.1060 -0.0317 0.0653  299  TYR B N   
11095 C CA  . TYR B 301  ? 0.4173 0.3252 0.2313 -0.1087 -0.0275 0.0669  299  TYR B CA  
11096 C C   . TYR B 301  ? 0.4037 0.3198 0.2205 -0.1153 -0.0246 0.0690  299  TYR B C   
11097 O O   . TYR B 301  ? 0.4255 0.3519 0.2418 -0.1181 -0.0208 0.0708  299  TYR B O   
11098 C CB  . TYR B 301  ? 0.3810 0.2998 0.2015 -0.1026 -0.0249 0.0630  299  TYR B CB  
11099 C CG  . TYR B 301  ? 0.4194 0.3327 0.2367 -0.0967 -0.0271 0.0613  299  TYR B CG  
11100 C CD1 . TYR B 301  ? 0.4149 0.3260 0.2238 -0.0976 -0.0271 0.0639  299  TYR B CD1 
11101 C CD2 . TYR B 301  ? 0.4028 0.3135 0.2253 -0.0904 -0.0292 0.0573  299  TYR B CD2 
11102 C CE1 . TYR B 301  ? 0.4169 0.3232 0.2228 -0.0923 -0.0293 0.0624  299  TYR B CE1 
11103 C CE2 . TYR B 301  ? 0.4410 0.3473 0.2609 -0.0852 -0.0314 0.0558  299  TYR B CE2 
11104 C CZ  . TYR B 301  ? 0.4159 0.3200 0.2275 -0.0862 -0.0315 0.0584  299  TYR B CZ  
11105 O OH  . TYR B 301  ? 0.4412 0.3410 0.2502 -0.0811 -0.0339 0.0570  299  TYR B OH  
11106 N N   . ASP B 302  ? 0.4147 0.3268 0.2344 -0.1177 -0.0261 0.0688  300  ASP B N   
11107 C CA  . ASP B 302  ? 0.4475 0.3677 0.2711 -0.1237 -0.0237 0.0703  300  ASP B CA  
11108 C C   . ASP B 302  ? 0.3902 0.3276 0.2221 -0.1220 -0.0190 0.0682  300  ASP B C   
11109 O O   . ASP B 302  ? 0.4165 0.3640 0.2484 -0.1264 -0.0155 0.0706  300  ASP B O   
11110 C CB  . ASP B 302  ? 0.4513 0.3682 0.2672 -0.1320 -0.0237 0.0758  300  ASP B CB  
11111 C CG  . ASP B 302  ? 0.4637 0.3848 0.2831 -0.1386 -0.0228 0.0773  300  ASP B CG  
11112 O OD1 . ASP B 302  ? 0.5086 0.4286 0.3339 -0.1369 -0.0241 0.0745  300  ASP B OD1 
11113 O OD2 . ASP B 302  ? 0.5394 0.4651 0.3558 -0.1454 -0.0209 0.0814  300  ASP B OD2 
11114 N N   . ILE B 303  ? 0.3809 0.3215 0.2197 -0.1152 -0.0189 0.0636  301  ILE B N   
11115 C CA  . ILE B 303  ? 0.3681 0.3236 0.2152 -0.1129 -0.0149 0.0610  301  ILE B CA  
11116 C C   . ILE B 303  ? 0.3863 0.3432 0.2413 -0.1118 -0.0156 0.0582  301  ILE B C   
11117 O O   . ILE B 303  ? 0.3752 0.3212 0.2294 -0.1111 -0.0192 0.0574  301  ILE B O   
11118 C CB  . ILE B 303  ? 0.3426 0.3023 0.1911 -0.1058 -0.0137 0.0579  301  ILE B CB  
11119 C CG1 . ILE B 303  ? 0.3735 0.3250 0.2245 -0.0995 -0.0170 0.0542  301  ILE B CG1 
11120 C CG2 . ILE B 303  ? 0.3801 0.3370 0.2199 -0.1067 -0.0135 0.0606  301  ILE B CG2 
11121 C CD1 . ILE B 303  ? 0.3874 0.3443 0.2416 -0.0927 -0.0157 0.0506  301  ILE B CD1 
11122 N N   . GLY B 304  ? 0.3417 0.3122 0.2043 -0.1115 -0.0121 0.0567  302  GLY B N   
11123 C CA  . GLY B 304  ? 0.3335 0.3065 0.2039 -0.1099 -0.0125 0.0538  302  GLY B CA  
11124 C C   . GLY B 304  ? 0.3297 0.3010 0.2043 -0.1019 -0.0134 0.0493  302  GLY B C   
11125 O O   . GLY B 304  ? 0.3399 0.3148 0.2145 -0.0975 -0.0121 0.0478  302  GLY B O   
11126 N N   . LEU B 305  ? 0.3068 0.2722 0.1846 -0.1002 -0.0159 0.0472  303  LEU B N   
11127 C CA  . LEU B 305  ? 0.3244 0.2893 0.2073 -0.0932 -0.0166 0.0429  303  LEU B CA  
11128 C C   . LEU B 305  ? 0.3100 0.2803 0.2005 -0.0933 -0.0159 0.0409  303  LEU B C   
11129 O O   . LEU B 305  ? 0.3225 0.2864 0.2124 -0.0962 -0.0181 0.0416  303  LEU B O   
11130 C CB  . LEU B 305  ? 0.3558 0.3067 0.2346 -0.0901 -0.0207 0.0422  303  LEU B CB  
11131 C CG  . LEU B 305  ? 0.3453 0.2961 0.2296 -0.0830 -0.0215 0.0379  303  LEU B CG  
11132 C CD1 . LEU B 305  ? 0.3791 0.3215 0.2589 -0.0789 -0.0239 0.0374  303  LEU B CD1 
11133 C CD2 . LEU B 305  ? 0.3919 0.3385 0.2801 -0.0824 -0.0233 0.0361  303  LEU B CD2 
11134 N N   . ASN B 306  ? 0.2907 0.2723 0.1880 -0.0900 -0.0130 0.0385  304  ASN B N   
11135 C CA  . ASN B 306  ? 0.2934 0.2821 0.1981 -0.0901 -0.0119 0.0368  304  ASN B CA  
11136 C C   . ASN B 306  ? 0.2809 0.2680 0.1906 -0.0836 -0.0128 0.0328  304  ASN B C   
11137 O O   . ASN B 306  ? 0.2826 0.2706 0.1929 -0.0786 -0.0123 0.0308  304  ASN B O   
11138 C CB  . ASN B 306  ? 0.3197 0.3232 0.2286 -0.0910 -0.0077 0.0371  304  ASN B CB  
11139 C CG  . ASN B 306  ? 0.2887 0.3000 0.2054 -0.0903 -0.0066 0.0351  304  ASN B CG  
11140 O OD1 . ASN B 306  ? 0.3203 0.3325 0.2382 -0.0950 -0.0071 0.0366  304  ASN B OD1 
11141 N ND2 . ASN B 306  ? 0.2958 0.3125 0.2179 -0.0845 -0.0052 0.0318  304  ASN B ND2 
11142 N N   . ILE B 307  ? 0.2905 0.2753 0.2037 -0.0839 -0.0142 0.0315  305  ILE B N   
11143 C CA  . ILE B 307  ? 0.2735 0.2581 0.1922 -0.0783 -0.0147 0.0278  305  ILE B CA  
11144 C C   . ILE B 307  ? 0.2692 0.2664 0.1952 -0.0776 -0.0117 0.0263  305  ILE B C   
11145 O O   . ILE B 307  ? 0.2594 0.2603 0.1877 -0.0813 -0.0113 0.0271  305  ILE B O   
11146 C CB  . ILE B 307  ? 0.2955 0.2697 0.2133 -0.0785 -0.0179 0.0271  305  ILE B CB  
11147 C CG1 . ILE B 307  ? 0.3277 0.2892 0.2381 -0.0785 -0.0210 0.0284  305  ILE B CG1 
11148 C CG2 . ILE B 307  ? 0.3071 0.2827 0.2312 -0.0729 -0.0180 0.0233  305  ILE B CG2 
11149 C CD1 . ILE B 307  ? 0.3724 0.3230 0.2811 -0.0786 -0.0242 0.0279  305  ILE B CD1 
11150 N N   . ASP B 308  ? 0.2690 0.2725 0.1983 -0.0728 -0.0098 0.0242  306  ASP B N   
11151 C CA  . ASP B 308  ? 0.2707 0.2856 0.2068 -0.0711 -0.0071 0.0225  306  ASP B CA  
11152 C C   . ASP B 308  ? 0.2537 0.2668 0.1946 -0.0694 -0.0084 0.0203  306  ASP B C   
11153 O O   . ASP B 308  ? 0.2747 0.2787 0.2146 -0.0672 -0.0109 0.0190  306  ASP B O   
11154 C CB  . ASP B 308  ? 0.2651 0.2849 0.2030 -0.0658 -0.0053 0.0204  306  ASP B CB  
11155 C CG  . ASP B 308  ? 0.2885 0.3123 0.2222 -0.0670 -0.0033 0.0223  306  ASP B CG  
11156 O OD1 . ASP B 308  ? 0.2864 0.3115 0.2168 -0.0723 -0.0028 0.0254  306  ASP B OD1 
11157 O OD2 . ASP B 308  ? 0.2855 0.3112 0.2191 -0.0628 -0.0024 0.0206  306  ASP B OD2 
11158 N N   . ALA B 309  ? 0.2280 0.2502 0.1742 -0.0704 -0.0066 0.0199  307  ALA B N   
11159 C CA  . ALA B 309  ? 0.2249 0.2463 0.1756 -0.0690 -0.0076 0.0179  307  ALA B CA  
11160 C C   . ALA B 309  ? 0.2271 0.2536 0.1831 -0.0630 -0.0062 0.0148  307  ALA B C   
11161 O O   . ALA B 309  ? 0.2426 0.2777 0.2007 -0.0614 -0.0036 0.0145  307  ALA B O   
11162 C CB  . ALA B 309  ? 0.2353 0.2634 0.1886 -0.0737 -0.0068 0.0193  307  ALA B CB  
11163 N N   . GLU B 310  ? 0.2258 0.2465 0.1836 -0.0598 -0.0079 0.0126  308  GLU B N   
11164 C CA  . GLU B 310  ? 0.2241 0.2480 0.1864 -0.0542 -0.0069 0.0097  308  GLU B CA  
11165 C C   . GLU B 310  ? 0.2143 0.2416 0.1819 -0.0533 -0.0068 0.0082  308  GLU B C   
11166 O O   . GLU B 310  ? 0.2127 0.2460 0.1822 -0.0565 -0.0059 0.0092  308  GLU B O   
11167 C CB  . GLU B 310  ? 0.2179 0.2331 0.1779 -0.0505 -0.0088 0.0085  308  GLU B CB  
11168 C CG  . GLU B 310  ? 0.2422 0.2545 0.1966 -0.0515 -0.0090 0.0102  308  GLU B CG  
11169 C CD  . GLU B 310  ? 0.2724 0.2772 0.2247 -0.0479 -0.0109 0.0090  308  GLU B CD  
11170 O OE1 . GLU B 310  ? 0.2646 0.2721 0.2195 -0.0437 -0.0101 0.0070  308  GLU B OE1 
11171 O OE2 . GLU B 310  ? 0.2580 0.2539 0.2058 -0.0492 -0.0133 0.0101  308  GLU B OE2 
11172 N N   . GLU B 311  ? 0.2166 0.2404 0.1866 -0.0491 -0.0076 0.0058  309  GLU B N   
11173 C CA  . GLU B 311  ? 0.2058 0.2329 0.1807 -0.0478 -0.0074 0.0042  309  GLU B CA  
11174 C C   . GLU B 311  ? 0.2222 0.2452 0.1958 -0.0517 -0.0091 0.0052  309  GLU B C   
11175 O O   . GLU B 311  ? 0.2225 0.2375 0.1914 -0.0541 -0.0110 0.0064  309  GLU B O   
11176 C CB  . GLU B 311  ? 0.2125 0.2359 0.1897 -0.0427 -0.0080 0.0017  309  GLU B CB  
11177 C CG  . GLU B 311  ? 0.2437 0.2715 0.2228 -0.0388 -0.0065 0.0004  309  GLU B CG  
11178 C CD  . GLU B 311  ? 0.2616 0.2837 0.2367 -0.0376 -0.0074 0.0007  309  GLU B CD  
11179 O OE1 . GLU B 311  ? 0.2474 0.2637 0.2179 -0.0404 -0.0089 0.0024  309  GLU B OE1 
11180 O OE2 . GLU B 311  ? 0.3353 0.3586 0.3117 -0.0339 -0.0068 -0.0008 309  GLU B OE2 
11181 N N   . ALA B 312  ? 0.2056 0.2341 0.1832 -0.0521 -0.0085 0.0045  310  ALA B N   
11182 C CA  . ALA B 312  ? 0.2185 0.2436 0.1949 -0.0559 -0.0101 0.0053  310  ALA B CA  
11183 C C   . ALA B 312  ? 0.1986 0.2124 0.1721 -0.0548 -0.0126 0.0043  310  ALA B C   
11184 O O   . ALA B 312  ? 0.2154 0.2230 0.1850 -0.0585 -0.0145 0.0055  310  ALA B O   
11185 C CB  . ALA B 312  ? 0.1994 0.2321 0.1809 -0.0558 -0.0092 0.0044  310  ALA B CB  
11186 N N   . ASP B 313  ? 0.2123 0.2233 0.1873 -0.0497 -0.0128 0.0022  311  ASP B N   
11187 C CA  . ASP B 313  ? 0.2174 0.2184 0.1900 -0.0482 -0.0150 0.0012  311  ASP B CA  
11188 C C   . ASP B 313  ? 0.2578 0.2503 0.2249 -0.0489 -0.0167 0.0023  311  ASP B C   
11189 O O   . ASP B 313  ? 0.2461 0.2302 0.2111 -0.0472 -0.0186 0.0015  311  ASP B O   
11190 C CB  . ASP B 313  ? 0.2271 0.2284 0.2037 -0.0429 -0.0146 -0.0014 311  ASP B CB  
11191 C CG  . ASP B 313  ? 0.2551 0.2583 0.2331 -0.0392 -0.0136 -0.0021 311  ASP B CG  
11192 O OD1 . ASP B 313  ? 0.2640 0.2677 0.2397 -0.0402 -0.0133 -0.0008 311  ASP B OD1 
11193 O OD2 . ASP B 313  ? 0.2924 0.2963 0.2738 -0.0351 -0.0132 -0.0040 311  ASP B OD2 
11194 N N   . ARG B 314  ? 0.2217 0.2166 0.1866 -0.0512 -0.0160 0.0043  312  ARG B N   
11195 C CA  . ARG B 314  ? 0.2415 0.2284 0.2006 -0.0525 -0.0176 0.0058  312  ARG B CA  
11196 C C   . ARG B 314  ? 0.2404 0.2250 0.1951 -0.0585 -0.0184 0.0084  312  ARG B C   
11197 O O   . ARG B 314  ? 0.2658 0.2427 0.2150 -0.0601 -0.0202 0.0099  312  ARG B O   
11198 C CB  . ARG B 314  ? 0.2277 0.2178 0.1867 -0.0505 -0.0164 0.0060  312  ARG B CB  
11199 C CG  . ARG B 314  ? 0.2367 0.2252 0.1982 -0.0449 -0.0166 0.0037  312  ARG B CG  
11200 C CD  . ARG B 314  ? 0.2277 0.2217 0.1905 -0.0426 -0.0149 0.0034  312  ARG B CD  
11201 N NE  . ARG B 314  ? 0.2262 0.2164 0.1899 -0.0380 -0.0160 0.0017  312  ARG B NE  
11202 C CZ  . ARG B 314  ? 0.2187 0.2121 0.1836 -0.0353 -0.0151 0.0009  312  ARG B CZ  
11203 N NH1 . ARG B 314  ? 0.2402 0.2410 0.2058 -0.0360 -0.0129 0.0013  312  ARG B NH1 
11204 N NH2 . ARG B 314  ? 0.2459 0.2350 0.2110 -0.0317 -0.0164 -0.0003 312  ARG B NH2 
11205 N N   . LEU B 315  ? 0.2340 0.2252 0.1909 -0.0619 -0.0174 0.0091  313  LEU B N   
11206 C CA  . LEU B 315  ? 0.2495 0.2398 0.2027 -0.0682 -0.0181 0.0118  313  LEU B CA  
11207 C C   . LEU B 315  ? 0.2596 0.2375 0.2071 -0.0701 -0.0212 0.0123  313  LEU B C   
11208 O O   . LEU B 315  ? 0.2709 0.2425 0.2128 -0.0730 -0.0225 0.0145  313  LEU B O   
11209 C CB  . LEU B 315  ? 0.2252 0.2248 0.1825 -0.0711 -0.0168 0.0121  313  LEU B CB  
11210 C CG  . LEU B 315  ? 0.2493 0.2533 0.2049 -0.0776 -0.0163 0.0152  313  LEU B CG  
11211 C CD1 . LEU B 315  ? 0.2754 0.2893 0.2361 -0.0794 -0.0151 0.0150  313  LEU B CD1 
11212 C CD2 . LEU B 315  ? 0.2974 0.2908 0.2464 -0.0824 -0.0191 0.0170  313  LEU B CD2 
11213 N N   . GLU B 316  ? 0.2510 0.2248 0.1996 -0.0687 -0.0225 0.0105  314  GLU B N   
11214 C CA  . GLU B 316  ? 0.2663 0.2284 0.2091 -0.0709 -0.0255 0.0110  314  GLU B CA  
11215 C C   . GLU B 316  ? 0.2815 0.2336 0.2200 -0.0677 -0.0272 0.0107  314  GLU B C   
11216 O O   . GLU B 316  ? 0.2992 0.2419 0.2314 -0.0705 -0.0295 0.0123  314  GLU B O   
11217 C CB  . GLU B 316  ? 0.2910 0.2514 0.2356 -0.0703 -0.0265 0.0090  314  GLU B CB  
11218 C CG  . GLU B 316  ? 0.2585 0.2278 0.2062 -0.0746 -0.0254 0.0098  314  GLU B CG  
11219 C CD  . GLU B 316  ? 0.3168 0.2847 0.2659 -0.0741 -0.0264 0.0079  314  GLU B CD  
11220 O OE1 . GLU B 316  ? 0.3167 0.2737 0.2613 -0.0739 -0.0288 0.0071  314  GLU B OE1 
11221 O OE2 . GLU B 316  ? 0.3143 0.2917 0.2686 -0.0740 -0.0248 0.0072  314  GLU B OE2 
11222 N N   . LEU B 317  ? 0.2854 0.2394 0.2272 -0.0621 -0.0263 0.0088  315  LEU B N   
11223 C CA  . LEU B 317  ? 0.2944 0.2404 0.2326 -0.0590 -0.0278 0.0088  315  LEU B CA  
11224 C C   . LEU B 317  ? 0.3030 0.2471 0.2363 -0.0625 -0.0281 0.0117  315  LEU B C   
11225 O O   . LEU B 317  ? 0.3170 0.2508 0.2443 -0.0631 -0.0305 0.0128  315  LEU B O   
11226 C CB  . LEU B 317  ? 0.2763 0.2269 0.2195 -0.0531 -0.0264 0.0066  315  LEU B CB  
11227 C CG  . LEU B 317  ? 0.3029 0.2464 0.2432 -0.0496 -0.0280 0.0064  315  LEU B CG  
11228 C CD1 . LEU B 317  ? 0.3606 0.2926 0.2966 -0.0489 -0.0309 0.0061  315  LEU B CD1 
11229 C CD2 . LEU B 317  ? 0.3171 0.2658 0.2630 -0.0442 -0.0267 0.0042  315  LEU B CD2 
11230 N N   . SER B 318  ? 0.2685 0.2220 0.2038 -0.0647 -0.0258 0.0130  316  SER B N   
11231 C CA  . SER B 318  ? 0.2823 0.2347 0.2130 -0.0679 -0.0258 0.0158  316  SER B CA  
11232 C C   . SER B 318  ? 0.2835 0.2284 0.2080 -0.0738 -0.0278 0.0183  316  SER B C   
11233 O O   . SER B 318  ? 0.3091 0.2477 0.2277 -0.0758 -0.0291 0.0205  316  SER B O   
11234 C CB  . SER B 318  ? 0.2776 0.2423 0.2117 -0.0691 -0.0226 0.0166  316  SER B CB  
11235 O OG  . SER B 318  ? 0.2684 0.2395 0.2044 -0.0737 -0.0215 0.0177  316  SER B OG  
11236 N N   . LEU B 319  ? 0.2812 0.2262 0.2067 -0.0767 -0.0284 0.0180  317  LEU B N   
11237 C CA  . LEU B 319  ? 0.3101 0.2473 0.2296 -0.0826 -0.0306 0.0204  317  LEU B CA  
11238 C C   . LEU B 319  ? 0.3206 0.2431 0.2337 -0.0809 -0.0339 0.0202  317  LEU B C   
11239 O O   . LEU B 319  ? 0.3225 0.2369 0.2289 -0.0851 -0.0358 0.0227  317  LEU B O   
11240 C CB  . LEU B 319  ? 0.3130 0.2534 0.2351 -0.0856 -0.0306 0.0198  317  LEU B CB  
11241 C CG  . LEU B 319  ? 0.3082 0.2631 0.2364 -0.0879 -0.0276 0.0202  317  LEU B CG  
11242 C CD1 . LEU B 319  ? 0.3090 0.2657 0.2397 -0.0899 -0.0283 0.0192  317  LEU B CD1 
11243 C CD2 . LEU B 319  ? 0.3248 0.2840 0.2506 -0.0935 -0.0266 0.0238  317  LEU B CD2 
11244 N N   . ASP B 320  ? 0.3210 0.2400 0.2361 -0.0748 -0.0346 0.0173  318  ASP B N   
11245 C CA  . ASP B 320  ? 0.3476 0.2532 0.2570 -0.0725 -0.0376 0.0170  318  ASP B CA  
11246 C C   . ASP B 320  ? 0.3177 0.2195 0.2227 -0.0722 -0.0383 0.0190  318  ASP B C   
11247 O O   . ASP B 320  ? 0.3748 0.2650 0.2729 -0.0732 -0.0410 0.0204  318  ASP B O   
11248 C CB  . ASP B 320  ? 0.3449 0.2492 0.2580 -0.0658 -0.0379 0.0136  318  ASP B CB  
11249 C CG  . ASP B 320  ? 0.3258 0.2294 0.2404 -0.0664 -0.0383 0.0119  318  ASP B CG  
11250 O OD1 . ASP B 320  ? 0.3619 0.2568 0.2710 -0.0701 -0.0405 0.0128  318  ASP B OD1 
11251 O OD2 . ASP B 320  ? 0.3651 0.2765 0.2861 -0.0635 -0.0364 0.0097  318  ASP B OD2 
11252 N N   . LEU B 321  ? 0.3006 0.2115 0.2091 -0.0707 -0.0359 0.0192  319  LEU B N   
11253 C CA  . LEU B 321  ? 0.3378 0.2454 0.2416 -0.0709 -0.0365 0.0213  319  LEU B CA  
11254 C C   . LEU B 321  ? 0.3264 0.2332 0.2251 -0.0780 -0.0365 0.0250  319  LEU B C   
11255 O O   . LEU B 321  ? 0.3496 0.2472 0.2412 -0.0797 -0.0386 0.0272  319  LEU B O   
11256 C CB  . LEU B 321  ? 0.3454 0.2627 0.2541 -0.0672 -0.0340 0.0203  319  LEU B CB  
11257 C CG  . LEU B 321  ? 0.3383 0.2546 0.2506 -0.0602 -0.0345 0.0173  319  LEU B CG  
11258 C CD1 . LEU B 321  ? 0.3419 0.2650 0.2614 -0.0578 -0.0329 0.0145  319  LEU B CD1 
11259 C CD2 . LEU B 321  ? 0.3513 0.2721 0.2645 -0.0575 -0.0334 0.0174  319  LEU B CD2 
11260 N N   . LEU B 322  ? 0.3279 0.2441 0.2298 -0.0822 -0.0343 0.0258  320  LEU B N   
11261 C CA  . LEU B 322  ? 0.3330 0.2493 0.2306 -0.0893 -0.0342 0.0294  320  LEU B CA  
11262 C C   . LEU B 322  ? 0.3378 0.2406 0.2282 -0.0929 -0.0377 0.0308  320  LEU B C   
11263 O O   . LEU B 322  ? 0.3612 0.2580 0.2449 -0.0972 -0.0389 0.0340  320  LEU B O   
11264 C CB  . LEU B 322  ? 0.3540 0.2827 0.2571 -0.0929 -0.0315 0.0296  320  LEU B CB  
11265 C CG  . LEU B 322  ? 0.3577 0.2890 0.2574 -0.1006 -0.0310 0.0335  320  LEU B CG  
11266 C CD1 . LEU B 322  ? 0.3497 0.2846 0.2470 -0.1009 -0.0293 0.0356  320  LEU B CD1 
11267 C CD2 . LEU B 322  ? 0.3523 0.2955 0.2580 -0.1039 -0.0287 0.0334  320  LEU B CD2 
11268 N N   . GLU B 323  ? 0.3438 0.2413 0.2352 -0.0912 -0.0394 0.0285  321  GLU B N   
11269 C CA  . GLU B 323  ? 0.3837 0.2675 0.2681 -0.0941 -0.0429 0.0295  321  GLU B CA  
11270 C C   . GLU B 323  ? 0.3672 0.2387 0.2445 -0.0921 -0.0455 0.0305  321  GLU B C   
11271 O O   . GLU B 323  ? 0.4169 0.2794 0.2867 -0.0968 -0.0476 0.0334  321  GLU B O   
11272 C CB  . GLU B 323  ? 0.4031 0.2835 0.2899 -0.0911 -0.0440 0.0262  321  GLU B CB  
11273 C CG  . GLU B 323  ? 0.4687 0.3336 0.3479 -0.0927 -0.0479 0.0265  321  GLU B CG  
11274 C CD  . GLU B 323  ? 0.4731 0.3372 0.3503 -0.1000 -0.0487 0.0280  321  GLU B CD  
11275 O OE1 . GLU B 323  ? 0.4492 0.3255 0.3320 -0.1030 -0.0463 0.0282  321  GLU B OE1 
11276 O OE2 . GLU B 323  ? 0.4826 0.3335 0.3525 -0.1027 -0.0520 0.0288  321  GLU B OE2 
11277 N N   . VAL B 324  ? 0.3561 0.2269 0.2354 -0.0850 -0.0455 0.0283  322  VAL B N   
11278 C CA  . VAL B 324  ? 0.4038 0.2635 0.2769 -0.0824 -0.0481 0.0292  322  VAL B CA  
11279 C C   . VAL B 324  ? 0.3978 0.2583 0.2663 -0.0863 -0.0476 0.0328  322  VAL B C   
11280 O O   . VAL B 324  ? 0.4210 0.2705 0.2816 -0.0889 -0.0502 0.0353  322  VAL B O   
11281 C CB  . VAL B 324  ? 0.4108 0.2717 0.2881 -0.0742 -0.0480 0.0261  322  VAL B CB  
11282 C CG1 . VAL B 324  ? 0.4252 0.2759 0.2964 -0.0715 -0.0506 0.0272  322  VAL B CG1 
11283 C CG2 . VAL B 324  ? 0.4310 0.2895 0.3115 -0.0706 -0.0487 0.0228  322  VAL B CG2 
11284 N N   . LEU B 325  ? 0.3608 0.2342 0.2342 -0.0869 -0.0443 0.0332  323  LEU B N   
11285 C CA  . LEU B 325  ? 0.3949 0.2701 0.2642 -0.0901 -0.0435 0.0365  323  LEU B CA  
11286 C C   . LEU B 325  ? 0.3918 0.2626 0.2550 -0.0982 -0.0444 0.0402  323  LEU B C   
11287 O O   . LEU B 325  ? 0.3915 0.2551 0.2474 -0.1008 -0.0459 0.0432  323  LEU B O   
11288 C CB  . LEU B 325  ? 0.3805 0.2708 0.2563 -0.0890 -0.0396 0.0359  323  LEU B CB  
11289 C CG  . LEU B 325  ? 0.3850 0.2789 0.2659 -0.0814 -0.0389 0.0326  323  LEU B CG  
11290 C CD1 . LEU B 325  ? 0.4302 0.3390 0.3182 -0.0804 -0.0351 0.0314  323  LEU B CD1 
11291 C CD2 . LEU B 325  ? 0.3931 0.2798 0.2685 -0.0787 -0.0408 0.0337  323  LEU B CD2 
11292 N N   . CYS B 326  ? 0.4075 0.2824 0.2735 -0.1024 -0.0436 0.0401  324  CYS B N   
11293 C CA  . CYS B 326  ? 0.4143 0.2856 0.2749 -0.1106 -0.0445 0.0437  324  CYS B CA  
11294 C C   . CYS B 326  ? 0.4233 0.2771 0.2752 -0.1121 -0.0489 0.0448  324  CYS B C   
11295 O O   . CYS B 326  ? 0.4248 0.2728 0.2701 -0.1185 -0.0501 0.0485  324  CYS B O   
11296 C CB  . CYS B 326  ? 0.4115 0.2926 0.2778 -0.1147 -0.0427 0.0434  324  CYS B CB  
11297 S SG  . CYS B 326  ? 0.4222 0.3238 0.2971 -0.1147 -0.0376 0.0433  324  CYS B SG  
11298 N N   . LEU B 327  ? 0.4163 0.2616 0.2680 -0.1063 -0.0511 0.0418  325  LEU B N   
11299 C CA  . LEU B 327  ? 0.4680 0.2961 0.3114 -0.1066 -0.0554 0.0424  325  LEU B CA  
11300 C C   . LEU B 327  ? 0.4887 0.3081 0.3268 -0.1023 -0.0573 0.0431  325  LEU B C   
11301 O O   . LEU B 327  ? 0.4945 0.2991 0.3252 -0.1017 -0.0609 0.0437  325  LEU B O   
11302 C CB  . LEU B 327  ? 0.4371 0.2602 0.2826 -0.1028 -0.0569 0.0388  325  LEU B CB  
11303 C CG  . LEU B 327  ? 0.4765 0.3061 0.3262 -0.1071 -0.0558 0.0380  325  LEU B CG  
11304 C CD1 . LEU B 327  ? 0.5576 0.3811 0.4084 -0.1029 -0.0575 0.0343  325  LEU B CD1 
11305 C CD2 . LEU B 327  ? 0.5641 0.3897 0.4081 -0.1162 -0.0570 0.0417  325  LEU B CD2 
11306 N N   . ASP B 328  ? 0.4424 0.2703 0.2837 -0.0992 -0.0550 0.0432  326  ASP B N   
11307 C CA  . ASP B 328  ? 0.4675 0.2883 0.3044 -0.0948 -0.0568 0.0437  326  ASP B CA  
11308 C C   . ASP B 328  ? 0.4649 0.2794 0.2931 -0.1006 -0.0580 0.0483  326  ASP B C   
11309 O O   . ASP B 328  ? 0.4660 0.2897 0.2949 -0.1046 -0.0553 0.0506  326  ASP B O   
11310 C CB  . ASP B 328  ? 0.4348 0.2676 0.2786 -0.0895 -0.0541 0.0418  326  ASP B CB  
11311 C CG  . ASP B 328  ? 0.5166 0.3426 0.3571 -0.0838 -0.0562 0.0415  326  ASP B CG  
11312 O OD1 . ASP B 328  ? 0.4939 0.3080 0.3259 -0.0854 -0.0591 0.0440  326  ASP B OD1 
11313 O OD2 . ASP B 328  ? 0.5227 0.3555 0.3692 -0.0779 -0.0549 0.0388  326  ASP B OD2 
11314 N N   . GLY B 329  ? 0.5146 0.3132 0.3342 -0.1008 -0.0620 0.0497  327  GLY B N   
11315 C CA  . GLY B 329  ? 0.4946 0.2855 0.3050 -0.1063 -0.0635 0.0542  327  GLY B CA  
11316 C C   . GLY B 329  ? 0.4981 0.2934 0.3071 -0.1048 -0.0623 0.0559  327  GLY B C   
11317 O O   . GLY B 329  ? 0.5142 0.3076 0.3171 -0.1104 -0.0623 0.0600  327  GLY B O   
11318 N N   . ASP B 330  ? 0.4772 0.2783 0.2916 -0.0975 -0.0614 0.0530  328  ASP B N   
11319 C CA  . ASP B 330  ? 0.4610 0.2676 0.2746 -0.0961 -0.0600 0.0544  328  ASP B CA  
11320 C C   . ASP B 330  ? 0.4967 0.3170 0.3133 -0.1014 -0.0559 0.0562  328  ASP B C   
11321 O O   . ASP B 330  ? 0.5468 0.3696 0.3598 -0.1029 -0.0549 0.0587  328  ASP B O   
11322 C CB  . ASP B 330  ? 0.4977 0.3091 0.3175 -0.0876 -0.0597 0.0506  328  ASP B CB  
11323 C CG  . ASP B 330  ? 0.5721 0.3705 0.3883 -0.0819 -0.0638 0.0494  328  ASP B CG  
11324 O OD1 . ASP B 330  ? 0.6079 0.3928 0.4157 -0.0842 -0.0671 0.0518  328  ASP B OD1 
11325 O OD2 . ASP B 330  ? 0.5820 0.3838 0.4039 -0.0750 -0.0638 0.0461  328  ASP B OD2 
11326 N N   . LEU B 331  ? 0.4454 0.2746 0.2683 -0.1041 -0.0534 0.0550  329  LEU B N   
11327 C CA  . LEU B 331  ? 0.4527 0.2958 0.2792 -0.1088 -0.0494 0.0565  329  LEU B CA  
11328 C C   . LEU B 331  ? 0.4308 0.2711 0.2523 -0.1178 -0.0495 0.0604  329  LEU B C   
11329 O O   . LEU B 331  ? 0.4955 0.3477 0.3211 -0.1223 -0.0463 0.0614  329  LEU B O   
11330 C CB  . LEU B 331  ? 0.4271 0.2833 0.2643 -0.1059 -0.0464 0.0528  329  LEU B CB  
11331 C CG  . LEU B 331  ? 0.4183 0.2773 0.2608 -0.0973 -0.0462 0.0488  329  LEU B CG  
11332 C CD1 . LEU B 331  ? 0.4092 0.2803 0.2617 -0.0950 -0.0434 0.0454  329  LEU B CD1 
11333 C CD2 . LEU B 331  ? 0.4386 0.3015 0.2793 -0.0952 -0.0451 0.0498  329  LEU B CD2 
11334 N N   . SER B 332  ? 0.5095 0.3346 0.3225 -0.1203 -0.0534 0.0625  330  SER B N   
11335 C CA  . SER B 332  ? 0.5073 0.3275 0.3149 -0.1290 -0.0543 0.0662  330  SER B CA  
11336 C C   . SER B 332  ? 0.5270 0.3580 0.3342 -0.1353 -0.0509 0.0699  330  SER B C   
11337 O O   . SER B 332  ? 0.5581 0.3912 0.3623 -0.1344 -0.0498 0.0716  330  SER B O   
11338 C CB  . SER B 332  ? 0.5651 0.3666 0.3619 -0.1300 -0.0589 0.0686  330  SER B CB  
11339 O OG  . SER B 332  ? 0.6437 0.4398 0.4343 -0.1389 -0.0599 0.0726  330  SER B OG  
11340 N N   . GLY B 333  ? 0.4886 0.3267 0.2988 -0.1418 -0.0492 0.0711  331  GLY B N   
11341 C CA  . GLY B 333  ? 0.5237 0.3717 0.3333 -0.1487 -0.0462 0.0750  331  GLY B CA  
11342 C C   . GLY B 333  ? 0.5226 0.3883 0.3396 -0.1459 -0.0414 0.0737  331  GLY B C   
11343 O O   . GLY B 333  ? 0.5145 0.3898 0.3314 -0.1512 -0.0384 0.0768  331  GLY B O   
11344 N N   . TRP B 334  ? 0.4904 0.3611 0.3140 -0.1380 -0.0405 0.0693  332  TRP B N   
11345 C CA  . TRP B 334  ? 0.4677 0.3542 0.2981 -0.1347 -0.0362 0.0677  332  TRP B CA  
11346 C C   . TRP B 334  ? 0.4339 0.3334 0.2734 -0.1362 -0.0334 0.0659  332  TRP B C   
11347 O O   . TRP B 334  ? 0.4299 0.3280 0.2742 -0.1333 -0.0346 0.0627  332  TRP B O   
11348 C CB  . TRP B 334  ? 0.4881 0.3727 0.3207 -0.1256 -0.0368 0.0640  332  TRP B CB  
11349 C CG  . TRP B 334  ? 0.4464 0.3458 0.2861 -0.1214 -0.0329 0.0616  332  TRP B CG  
11350 C CD1 . TRP B 334  ? 0.4555 0.3646 0.2945 -0.1228 -0.0296 0.0635  332  TRP B CD1 
11351 C CD2 . TRP B 334  ? 0.4392 0.3446 0.2871 -0.1147 -0.0319 0.0570  332  TRP B CD2 
11352 N NE1 . TRP B 334  ? 0.4300 0.3505 0.2763 -0.1173 -0.0268 0.0601  332  TRP B NE1 
11353 C CE2 . TRP B 334  ? 0.4021 0.3204 0.2540 -0.1125 -0.0282 0.0562  332  TRP B CE2 
11354 C CE3 . TRP B 334  ? 0.4264 0.3275 0.2786 -0.1105 -0.0338 0.0535  332  TRP B CE3 
11355 C CZ2 . TRP B 334  ? 0.3843 0.3108 0.2442 -0.1063 -0.0265 0.0521  332  TRP B CZ2 
11356 C CZ3 . TRP B 334  ? 0.4502 0.3599 0.3105 -0.1046 -0.0320 0.0496  332  TRP B CZ3 
11357 C CH2 . TRP B 334  ? 0.4202 0.3422 0.2842 -0.1026 -0.0284 0.0490  332  TRP B CH2 
11358 N N   . ASN B 335  ? 0.4352 0.3476 0.2771 -0.1408 -0.0298 0.0682  333  ASN B N   
11359 C CA  . ASN B 335  ? 0.4198 0.3457 0.2703 -0.1424 -0.0271 0.0669  333  ASN B CA  
11360 C C   . ASN B 335  ? 0.3828 0.3225 0.2411 -0.1363 -0.0234 0.0637  333  ASN B C   
11361 O O   . ASN B 335  ? 0.4025 0.3556 0.2679 -0.1374 -0.0204 0.0631  333  ASN B O   
11362 C CB  . ASN B 335  ? 0.4520 0.3840 0.3010 -0.1516 -0.0255 0.0713  333  ASN B CB  
11363 C CG  . ASN B 335  ? 0.5067 0.4250 0.3490 -0.1579 -0.0295 0.0739  333  ASN B CG  
11364 O OD1 . ASN B 335  ? 0.4655 0.3732 0.3073 -0.1556 -0.0328 0.0716  333  ASN B OD1 
11365 N ND2 . ASN B 335  ? 0.4862 0.4044 0.3233 -0.1658 -0.0291 0.0787  333  ASN B ND2 
11366 N N   . GLY B 336  ? 0.3975 0.3338 0.2544 -0.1297 -0.0237 0.0618  334  GLY B N   
11367 C CA  . GLY B 336  ? 0.3983 0.3462 0.2614 -0.1238 -0.0206 0.0589  334  GLY B CA  
11368 C C   . GLY B 336  ? 0.3714 0.3212 0.2420 -0.1175 -0.0208 0.0542  334  GLY B C   
11369 O O   . GLY B 336  ? 0.3462 0.3058 0.2222 -0.1128 -0.0182 0.0517  334  GLY B O   
11370 N N   . MET B 337  ? 0.3874 0.3280 0.2582 -0.1171 -0.0239 0.0528  335  MET B N   
11371 C CA  A MET B 337  ? 0.3653 0.3083 0.2433 -0.1115 -0.0240 0.0485  335  MET B CA  
11372 C CA  B MET B 337  ? 0.3653 0.3084 0.2434 -0.1114 -0.0240 0.0485  335  MET B CA  
11373 C C   . MET B 337  ? 0.3495 0.3072 0.2355 -0.1129 -0.0207 0.0476  335  MET B C   
11374 O O   . MET B 337  ? 0.3616 0.3222 0.2480 -0.1190 -0.0205 0.0497  335  MET B O   
11375 C CB  A MET B 337  ? 0.4026 0.3332 0.2787 -0.1117 -0.0278 0.0476  335  MET B CB  
11376 C CB  B MET B 337  ? 0.4024 0.3329 0.2787 -0.1111 -0.0279 0.0473  335  MET B CB  
11377 C CG  A MET B 337  ? 0.3699 0.3031 0.2533 -0.1067 -0.0279 0.0434  335  MET B CG  
11378 C CG  B MET B 337  ? 0.3912 0.3223 0.2737 -0.1044 -0.0282 0.0429  335  MET B CG  
11379 S SD  A MET B 337  ? 0.4241 0.3509 0.3079 -0.0978 -0.0294 0.0400  335  MET B SD  
11380 S SD  B MET B 337  ? 0.4034 0.3341 0.2866 -0.0963 -0.0280 0.0404  335  MET B SD  
11381 C CE  A MET B 337  ? 0.3595 0.3021 0.2513 -0.0932 -0.0252 0.0376  335  MET B CE  
11382 C CE  B MET B 337  ? 0.4081 0.3206 0.2838 -0.0944 -0.0328 0.0407  335  MET B CE  
11383 N N   . GLY B 338  ? 0.3321 0.2991 0.2243 -0.1073 -0.0183 0.0446  336  GLY B N   
11384 C CA  . GLY B 338  ? 0.3588 0.3398 0.2587 -0.1075 -0.0151 0.0435  336  GLY B CA  
11385 C C   . GLY B 338  ? 0.3183 0.3004 0.2248 -0.1022 -0.0156 0.0395  336  GLY B C   
11386 O O   . GLY B 338  ? 0.3040 0.2793 0.2102 -0.0967 -0.0172 0.0370  336  GLY B O   
11387 N N   . PHE B 339  ? 0.3071 0.2980 0.2196 -0.1039 -0.0141 0.0388  337  PHE B N   
11388 C CA  . PHE B 339  ? 0.2989 0.2905 0.2173 -0.0995 -0.0147 0.0353  337  PHE B CA  
11389 C C   . PHE B 339  ? 0.2819 0.2881 0.2076 -0.0999 -0.0116 0.0346  337  PHE B C   
11390 O O   . PHE B 339  ? 0.2904 0.3028 0.2168 -0.1056 -0.0106 0.0370  337  PHE B O   
11391 C CB  . PHE B 339  ? 0.3065 0.2874 0.2226 -0.1019 -0.0181 0.0352  337  PHE B CB  
11392 C CG  . PHE B 339  ? 0.3048 0.2837 0.2255 -0.0968 -0.0191 0.0315  337  PHE B CG  
11393 C CD1 . PHE B 339  ? 0.3007 0.2708 0.2199 -0.0913 -0.0209 0.0293  337  PHE B CD1 
11394 C CD2 . PHE B 339  ? 0.2992 0.2852 0.2257 -0.0976 -0.0183 0.0303  337  PHE B CD2 
11395 C CE1 . PHE B 339  ? 0.3273 0.2959 0.2507 -0.0867 -0.0216 0.0260  337  PHE B CE1 
11396 C CE2 . PHE B 339  ? 0.2988 0.2829 0.2291 -0.0931 -0.0191 0.0270  337  PHE B CE2 
11397 C CZ  . PHE B 339  ? 0.3144 0.2899 0.2432 -0.0877 -0.0207 0.0249  337  PHE B CZ  
11398 N N   . VAL B 340  ? 0.2760 0.2880 0.2072 -0.0939 -0.0100 0.0314  338  VAL B N   
11399 C CA  . VAL B 340  ? 0.2681 0.2939 0.2064 -0.0931 -0.0071 0.0305  338  VAL B CA  
11400 C C   . VAL B 340  ? 0.2555 0.2811 0.1981 -0.0934 -0.0085 0.0289  338  VAL B C   
11401 O O   . VAL B 340  ? 0.2672 0.2839 0.2094 -0.0905 -0.0108 0.0268  338  VAL B O   
11402 C CB  . VAL B 340  ? 0.2770 0.3085 0.2186 -0.0864 -0.0049 0.0279  338  VAL B CB  
11403 C CG1 . VAL B 340  ? 0.2751 0.3202 0.2239 -0.0853 -0.0021 0.0268  338  VAL B CG1 
11404 C CG2 . VAL B 340  ? 0.2742 0.3057 0.2110 -0.0862 -0.0037 0.0294  338  VAL B CG2 
11405 N N   . VAL B 341  ? 0.2651 0.3008 0.2119 -0.0968 -0.0070 0.0299  339  VAL B N   
11406 C CA  . VAL B 341  ? 0.2748 0.3128 0.2265 -0.0966 -0.0077 0.0282  339  VAL B CA  
11407 C C   . VAL B 341  ? 0.2415 0.2943 0.2003 -0.0942 -0.0046 0.0271  339  VAL B C   
11408 O O   . VAL B 341  ? 0.2515 0.3142 0.2113 -0.0965 -0.0020 0.0291  339  VAL B O   
11409 C CB  . VAL B 341  ? 0.3062 0.3408 0.2558 -0.1036 -0.0099 0.0304  339  VAL B CB  
11410 C CG1 . VAL B 341  ? 0.3270 0.3462 0.2691 -0.1054 -0.0132 0.0313  339  VAL B CG1 
11411 C CG2 . VAL B 341  ? 0.3620 0.4068 0.3121 -0.1096 -0.0080 0.0338  339  VAL B CG2 
11412 N N   . GLN B 342  ? 0.2320 0.2863 0.1957 -0.0895 -0.0046 0.0241  340  GLN B N   
11413 C CA  . GLN B 342  ? 0.2338 0.3005 0.2040 -0.0859 -0.0019 0.0226  340  GLN B CA  
11414 C C   . GLN B 342  ? 0.2254 0.2993 0.2002 -0.0890 -0.0020 0.0230  340  GLN B C   
11415 O O   . GLN B 342  ? 0.2408 0.3096 0.2166 -0.0887 -0.0041 0.0215  340  GLN B O   
11416 C CB  . GLN B 342  ? 0.2362 0.2995 0.2085 -0.0787 -0.0019 0.0191  340  GLN B CB  
11417 C CG  . GLN B 342  ? 0.2251 0.2821 0.1933 -0.0754 -0.0019 0.0186  340  GLN B CG  
11418 C CD  . GLN B 342  ? 0.2275 0.2758 0.1959 -0.0702 -0.0036 0.0157  340  GLN B CD  
11419 O OE1 . GLN B 342  ? 0.2210 0.2623 0.1890 -0.0709 -0.0059 0.0150  340  GLN B OE1 
11420 N NE2 . GLN B 342  ? 0.2167 0.2657 0.1858 -0.0651 -0.0025 0.0140  340  GLN B NE2 
11421 N N   . ALA B 343  ? 0.2188 0.3051 0.1966 -0.0918 0.0003  0.0248  341  ALA B N   
11422 C CA  . ALA B 343  ? 0.2227 0.3171 0.2050 -0.0953 0.0001  0.0256  341  ALA B CA  
11423 C C   . ALA B 343  ? 0.2216 0.3217 0.2100 -0.0900 0.0008  0.0227  341  ALA B C   
11424 O O   . ALA B 343  ? 0.2242 0.3288 0.2161 -0.0923 -0.0001 0.0228  341  ALA B O   
11425 C CB  . ALA B 343  ? 0.2505 0.3573 0.2345 -0.0996 0.0026  0.0286  341  ALA B CB  
11426 N N   . TYR B 344  ? 0.2222 0.3222 0.2119 -0.0833 0.0022  0.0203  342  TYR B N   
11427 C CA  . TYR B 344  ? 0.2176 0.3210 0.2124 -0.0786 0.0023  0.0176  342  TYR B CA  
11428 C C   . TYR B 344  ? 0.2024 0.2950 0.1959 -0.0781 -0.0007 0.0160  342  TYR B C   
11429 O O   . TYR B 344  ? 0.2144 0.3091 0.2118 -0.0749 -0.0009 0.0139  342  TYR B O   
11430 C CB  . TYR B 344  ? 0.2186 0.3257 0.2157 -0.0716 0.0046  0.0154  342  TYR B CB  
11431 C CG  . TYR B 344  ? 0.2060 0.3026 0.1995 -0.0672 0.0039  0.0135  342  TYR B CG  
11432 C CD1 . TYR B 344  ? 0.2171 0.3012 0.2054 -0.0690 0.0014  0.0138  342  TYR B CD1 
11433 C CD2 . TYR B 344  ? 0.1866 0.2860 0.1820 -0.0613 0.0057  0.0115  342  TYR B CD2 
11434 C CE1 . TYR B 344  ? 0.1890 0.2646 0.1747 -0.0649 0.0008  0.0121  342  TYR B CE1 
11435 C CE2 . TYR B 344  ? 0.2064 0.2971 0.1989 -0.0575 0.0050  0.0099  342  TYR B CE2 
11436 C CZ  . TYR B 344  ? 0.1989 0.2782 0.1869 -0.0593 0.0026  0.0102  342  TYR B CZ  
11437 O OH  . TYR B 344  ? 0.1983 0.2699 0.1839 -0.0553 0.0019  0.0086  342  TYR B OH  
11438 N N   . GLY B 345  ? 0.2108 0.2921 0.1987 -0.0812 -0.0030 0.0168  343  GLY B N   
11439 C CA  . GLY B 345  ? 0.2223 0.2927 0.2083 -0.0805 -0.0058 0.0153  343  GLY B CA  
11440 C C   . GLY B 345  ? 0.2381 0.3079 0.2238 -0.0862 -0.0079 0.0165  343  GLY B C   
11441 O O   . GLY B 345  ? 0.2337 0.3054 0.2174 -0.0921 -0.0082 0.0192  343  GLY B O   
11442 N N   . LYS B 346  ? 0.2249 0.2913 0.2120 -0.0845 -0.0095 0.0145  344  LYS B N   
11443 C CA  . LYS B 346  ? 0.2347 0.3001 0.2214 -0.0894 -0.0117 0.0152  344  LYS B CA  
11444 C C   . LYS B 346  ? 0.2346 0.2880 0.2145 -0.0941 -0.0144 0.0166  344  LYS B C   
11445 O O   . LYS B 346  ? 0.2599 0.3128 0.2386 -0.0997 -0.0162 0.0180  344  LYS B O   
11446 C CB  . LYS B 346  ? 0.2337 0.2975 0.2230 -0.0857 -0.0126 0.0125  344  LYS B CB  
11447 C CG  . LYS B 346  ? 0.2336 0.3088 0.2294 -0.0813 -0.0102 0.0113  344  LYS B CG  
11448 C CD  . LYS B 346  ? 0.2423 0.3150 0.2400 -0.0774 -0.0112 0.0087  344  LYS B CD  
11449 C CE  . LYS B 346  ? 0.2359 0.3207 0.2400 -0.0740 -0.0091 0.0080  344  LYS B CE  
11450 N NZ  . LYS B 346  ? 0.2245 0.3067 0.2303 -0.0699 -0.0098 0.0055  344  LYS B NZ  
11451 N N   . ARG B 347  ? 0.2347 0.2780 0.2100 -0.0919 -0.0150 0.0162  345  ARG B N   
11452 C CA  . ARG B 347  ? 0.2640 0.2950 0.2324 -0.0959 -0.0177 0.0174  345  ARG B CA  
11453 C C   . ARG B 347  ? 0.2448 0.2774 0.2102 -0.1013 -0.0172 0.0208  345  ARG B C   
11454 O O   . ARG B 347  ? 0.2764 0.2993 0.2358 -0.1056 -0.0196 0.0224  345  ARG B O   
11455 C CB  . ARG B 347  ? 0.2571 0.2762 0.2218 -0.0910 -0.0188 0.0155  345  ARG B CB  
11456 C CG  . ARG B 347  ? 0.2313 0.2472 0.1980 -0.0867 -0.0197 0.0125  345  ARG B CG  
11457 C CD  . ARG B 347  ? 0.2391 0.2472 0.2043 -0.0808 -0.0198 0.0105  345  ARG B CD  
11458 N NE  . ARG B 347  ? 0.2303 0.2458 0.1994 -0.0763 -0.0171 0.0098  345  ARG B NE  
11459 C CZ  . ARG B 347  ? 0.2536 0.2641 0.2217 -0.0716 -0.0169 0.0085  345  ARG B CZ  
11460 N NH1 . ARG B 347  ? 0.2613 0.2602 0.2251 -0.0703 -0.0191 0.0077  345  ARG B NH1 
11461 N NH2 . ARG B 347  ? 0.2175 0.2348 0.1890 -0.0679 -0.0146 0.0079  345  ARG B NH2 
11462 N N   . CYS B 348  ? 0.2556 0.3002 0.2247 -0.1011 -0.0142 0.0220  346  CYS B N   
11463 C CA  . CYS B 348  ? 0.2561 0.3027 0.2222 -0.1053 -0.0132 0.0251  346  CYS B CA  
11464 C C   . CYS B 348  ? 0.2822 0.3247 0.2441 -0.1133 -0.0154 0.0280  346  CYS B C   
11465 O O   . CYS B 348  ? 0.2977 0.3311 0.2533 -0.1159 -0.0166 0.0297  346  CYS B O   
11466 C CB  . CYS B 348  ? 0.2537 0.3157 0.2253 -0.1041 -0.0095 0.0258  346  CYS B CB  
11467 S SG  . CYS B 348  ? 0.3301 0.3939 0.2975 -0.1073 -0.0077 0.0291  346  CYS B SG  
11468 N N   . PRO B 349  ? 0.2767 0.3252 0.2415 -0.1177 -0.0161 0.0288  347  PRO B N   
11469 C CA  . PRO B 349  ? 0.3053 0.3491 0.2657 -0.1259 -0.0184 0.0317  347  PRO B CA  
11470 C C   . PRO B 349  ? 0.2695 0.2958 0.2226 -0.1268 -0.0222 0.0310  347  PRO B C   
11471 O O   . PRO B 349  ? 0.3020 0.3208 0.2491 -0.1322 -0.0239 0.0336  347  PRO B O   
11472 C CB  . PRO B 349  ? 0.2973 0.3516 0.2631 -0.1295 -0.0186 0.0321  347  PRO B CB  
11473 C CG  . PRO B 349  ? 0.3106 0.3696 0.2819 -0.1228 -0.0176 0.0287  347  PRO B CG  
11474 C CD  . PRO B 349  ? 0.2883 0.3470 0.2601 -0.1157 -0.0153 0.0271  347  PRO B CD  
11475 N N   . PHE B 350  ? 0.2820 0.3015 0.2353 -0.1213 -0.0233 0.0277  348  PHE B N   
11476 C CA  . PHE B 350  ? 0.3108 0.3138 0.2572 -0.1213 -0.0267 0.0267  348  PHE B CA  
11477 C C   . PHE B 350  ? 0.2780 0.2719 0.2194 -0.1186 -0.0268 0.0271  348  PHE B C   
11478 O O   . PHE B 350  ? 0.3220 0.3032 0.2562 -0.1214 -0.0295 0.0282  348  PHE B O   
11479 C CB  . PHE B 350  ? 0.2776 0.2779 0.2264 -0.1163 -0.0277 0.0231  348  PHE B CB  
11480 C CG  . PHE B 350  ? 0.2856 0.2959 0.2398 -0.1185 -0.0275 0.0228  348  PHE B CG  
11481 C CD1 . PHE B 350  ? 0.3325 0.3395 0.2841 -0.1249 -0.0302 0.0240  348  PHE B CD1 
11482 C CD2 . PHE B 350  ? 0.2961 0.3194 0.2578 -0.1144 -0.0247 0.0215  348  PHE B CD2 
11483 C CE1 . PHE B 350  ? 0.3614 0.3783 0.3180 -0.1272 -0.0302 0.0238  348  PHE B CE1 
11484 C CE2 . PHE B 350  ? 0.2940 0.3270 0.2607 -0.1163 -0.0246 0.0214  348  PHE B CE2 
11485 C CZ  . PHE B 350  ? 0.3039 0.3340 0.2682 -0.1227 -0.0273 0.0225  348  PHE B CZ  
11486 N N   . VAL B 351  ? 0.2751 0.2753 0.2197 -0.1134 -0.0240 0.0263  349  VAL B N   
11487 C CA  . VAL B 351  ? 0.2792 0.2724 0.2192 -0.1114 -0.0239 0.0270  349  VAL B CA  
11488 C C   . VAL B 351  ? 0.3133 0.3061 0.2488 -0.1181 -0.0240 0.0310  349  VAL B C   
11489 O O   . VAL B 351  ? 0.3243 0.3056 0.2528 -0.1195 -0.0259 0.0323  349  VAL B O   
11490 C CB  . VAL B 351  ? 0.2686 0.2698 0.2132 -0.1049 -0.0208 0.0254  349  VAL B CB  
11491 C CG1 . VAL B 351  ? 0.2745 0.2690 0.2142 -0.1031 -0.0208 0.0263  349  VAL B CG1 
11492 C CG2 . VAL B 351  ? 0.2802 0.2808 0.2288 -0.0986 -0.0209 0.0217  349  VAL B CG2 
11493 N N   . LEU B 352  ? 0.2802 0.2856 0.2195 -0.1225 -0.0220 0.0330  350  LEU B N   
11494 C CA  . LEU B 352  ? 0.2937 0.2997 0.2290 -0.1294 -0.0220 0.0370  350  LEU B CA  
11495 C C   . LEU B 352  ? 0.3197 0.3133 0.2484 -0.1356 -0.0258 0.0386  350  LEU B C   
11496 O O   . LEU B 352  ? 0.3384 0.3236 0.2604 -0.1391 -0.0271 0.0412  350  LEU B O   
11497 C CB  . LEU B 352  ? 0.3074 0.3303 0.2487 -0.1329 -0.0190 0.0389  350  LEU B CB  
11498 C CG  . LEU B 352  ? 0.3169 0.3515 0.2630 -0.1277 -0.0151 0.0381  350  LEU B CG  
11499 C CD1 . LEU B 352  ? 0.3449 0.3962 0.2971 -0.1311 -0.0124 0.0398  350  LEU B CD1 
11500 C CD2 . LEU B 352  ? 0.3752 0.4051 0.3158 -0.1274 -0.0143 0.0399  350  LEU B CD2 
11501 N N   . ASP B 353  ? 0.3186 0.3104 0.2489 -0.1369 -0.0278 0.0372  351  ASP B N   
11502 C CA  . ASP B 353  ? 0.3519 0.3304 0.2754 -0.1421 -0.0318 0.0382  351  ASP B CA  
11503 C C   . ASP B 353  ? 0.3155 0.2775 0.2317 -0.1387 -0.0341 0.0373  351  ASP B C   
11504 O O   . ASP B 353  ? 0.3605 0.3115 0.2692 -0.1433 -0.0365 0.0396  351  ASP B O   
11505 C CB  . ASP B 353  ? 0.3726 0.3509 0.2988 -0.1421 -0.0336 0.0358  351  ASP B CB  
11506 C CG  . ASP B 353  ? 0.3957 0.3887 0.3282 -0.1469 -0.0323 0.0371  351  ASP B CG  
11507 O OD1 . ASP B 353  ? 0.4071 0.4082 0.3404 -0.1521 -0.0308 0.0405  351  ASP B OD1 
11508 O OD2 . ASP B 353  ? 0.4451 0.4417 0.3817 -0.1452 -0.0328 0.0348  351  ASP B OD2 
11509 N N   . PHE B 354  ? 0.3449 0.3047 0.2630 -0.1306 -0.0334 0.0339  352  PHE B N   
11510 C CA  . PHE B 354  ? 0.3379 0.2833 0.2498 -0.1267 -0.0354 0.0329  352  PHE B CA  
11511 C C   . PHE B 354  ? 0.3400 0.2829 0.2474 -0.1282 -0.0348 0.0358  352  PHE B C   
11512 O O   . PHE B 354  ? 0.3713 0.3009 0.2710 -0.1302 -0.0375 0.0372  352  PHE B O   
11513 C CB  . PHE B 354  ? 0.3471 0.2934 0.2632 -0.1179 -0.0343 0.0291  352  PHE B CB  
11514 C CG  . PHE B 354  ? 0.3449 0.2790 0.2558 -0.1132 -0.0358 0.0282  352  PHE B CG  
11515 C CD1 . PHE B 354  ? 0.3669 0.2868 0.2725 -0.1121 -0.0391 0.0268  352  PHE B CD1 
11516 C CD2 . PHE B 354  ? 0.3449 0.2817 0.2561 -0.1100 -0.0340 0.0288  352  PHE B CD2 
11517 C CE1 . PHE B 354  ? 0.3749 0.2839 0.2758 -0.1076 -0.0406 0.0261  352  PHE B CE1 
11518 C CE2 . PHE B 354  ? 0.3658 0.2917 0.2723 -0.1059 -0.0355 0.0281  352  PHE B CE2 
11519 C CZ  . PHE B 354  ? 0.3874 0.2997 0.2890 -0.1046 -0.0388 0.0268  352  PHE B CZ  
11520 N N   . ILE B 355  ? 0.3253 0.2807 0.2371 -0.1272 -0.0313 0.0367  353  ILE B N   
11521 C CA  . ILE B 355  ? 0.3347 0.2886 0.2423 -0.1282 -0.0305 0.0394  353  ILE B CA  
11522 C C   . ILE B 355  ? 0.3453 0.2956 0.2472 -0.1370 -0.0319 0.0435  353  ILE B C   
11523 O O   . ILE B 355  ? 0.3629 0.3027 0.2574 -0.1386 -0.0335 0.0456  353  ILE B O   
11524 C CB  . ILE B 355  ? 0.3418 0.3104 0.2553 -0.1252 -0.0263 0.0393  353  ILE B CB  
11525 C CG1 . ILE B 355  ? 0.3647 0.3348 0.2826 -0.1166 -0.0253 0.0353  353  ILE B CG1 
11526 C CG2 . ILE B 355  ? 0.3692 0.3372 0.2779 -0.1274 -0.0253 0.0424  353  ILE B CG2 
11527 C CD1 . ILE B 355  ? 0.3364 0.3207 0.2603 -0.1135 -0.0214 0.0348  353  ILE B CD1 
11528 N N   . ILE B 356  ? 0.3505 0.3096 0.2558 -0.1428 -0.0312 0.0450  354  ILE B N   
11529 C CA  . ILE B 356  ? 0.3764 0.3331 0.2768 -0.1517 -0.0325 0.0491  354  ILE B CA  
11530 C C   . ILE B 356  ? 0.3766 0.3147 0.2685 -0.1542 -0.0371 0.0494  354  ILE B C   
11531 O O   . ILE B 356  ? 0.3964 0.3259 0.2809 -0.1589 -0.0387 0.0527  354  ILE B O   
11532 C CB  . ILE B 356  ? 0.3654 0.3355 0.2718 -0.1572 -0.0312 0.0503  354  ILE B CB  
11533 C CG1 . ILE B 356  ? 0.4042 0.3924 0.3177 -0.1555 -0.0265 0.0509  354  ILE B CG1 
11534 C CG2 . ILE B 356  ? 0.3945 0.3599 0.2955 -0.1670 -0.0334 0.0543  354  ILE B CG2 
11535 C CD1 . ILE B 356  ? 0.3725 0.3760 0.2937 -0.1587 -0.0249 0.0511  354  ILE B CD1 
11536 N N   . ASP B 357  ? 0.3818 0.3132 0.2742 -0.1508 -0.0392 0.0461  355  ASP B N   
11537 C CA  . ASP B 357  ? 0.4037 0.3170 0.2879 -0.1522 -0.0436 0.0459  355  ASP B CA  
11538 C C   . ASP B 357  ? 0.3694 0.2708 0.2474 -0.1475 -0.0447 0.0458  355  ASP B C   
11539 O O   . ASP B 357  ? 0.3973 0.2851 0.2668 -0.1510 -0.0476 0.0479  355  ASP B O   
11540 C CB  . ASP B 357  ? 0.4069 0.3165 0.2932 -0.1490 -0.0453 0.0421  355  ASP B CB  
11541 C CG  . ASP B 357  ? 0.4258 0.3160 0.3034 -0.1484 -0.0496 0.0412  355  ASP B CG  
11542 O OD1 . ASP B 357  ? 0.4556 0.3376 0.3274 -0.1554 -0.0525 0.0434  355  ASP B OD1 
11543 O OD2 . ASP B 357  ? 0.4078 0.2911 0.2845 -0.1410 -0.0502 0.0384  355  ASP B OD2 
11544 N N   . LEU B 358  ? 0.3791 0.2851 0.2613 -0.1397 -0.0425 0.0433  356  LEU B N   
11545 C CA  . LEU B 358  ? 0.3729 0.2690 0.2500 -0.1351 -0.0435 0.0432  356  LEU B CA  
11546 C C   . LEU B 358  ? 0.3650 0.2598 0.2366 -0.1401 -0.0432 0.0475  356  LEU B C   
11547 O O   . LEU B 358  ? 0.4021 0.2833 0.2657 -0.1406 -0.0459 0.0489  356  LEU B O   
11548 C CB  . LEU B 358  ? 0.3517 0.2556 0.2351 -0.1267 -0.0408 0.0402  356  LEU B CB  
11549 C CG  . LEU B 358  ? 0.3838 0.2800 0.2631 -0.1215 -0.0414 0.0399  356  LEU B CG  
11550 C CD1 . LEU B 358  ? 0.4164 0.2953 0.2889 -0.1194 -0.0455 0.0389  356  LEU B CD1 
11551 C CD2 . LEU B 358  ? 0.3583 0.2637 0.2447 -0.1140 -0.0388 0.0369  356  LEU B CD2 
11552 N N   . ALA B 359  ? 0.3827 0.2918 0.2586 -0.1438 -0.0399 0.0497  357  ALA B N   
11553 C CA  . ALA B 359  ? 0.3831 0.2924 0.2541 -0.1490 -0.0392 0.0540  357  ALA B CA  
11554 C C   . ALA B 359  ? 0.4074 0.3044 0.2702 -0.1568 -0.0427 0.0571  357  ALA B C   
11555 O O   . ALA B 359  ? 0.4304 0.3167 0.2852 -0.1585 -0.0445 0.0596  357  ALA B O   
11556 C CB  . ALA B 359  ? 0.4243 0.3520 0.3018 -0.1520 -0.0350 0.0556  357  ALA B CB  
11557 N N   . ARG B 360  ? 0.4016 0.2996 0.2662 -0.1614 -0.0440 0.0569  358  ARG B N   
11558 C CA  . ARG B 360  ? 0.4483 0.3348 0.3054 -0.1693 -0.0475 0.0598  358  ARG B CA  
11559 C C   . ARG B 360  ? 0.3914 0.2575 0.2396 -0.1664 -0.0517 0.0588  358  ARG B C   
11560 O O   . ARG B 360  ? 0.4399 0.2947 0.2796 -0.1708 -0.0541 0.0619  358  ARG B O   
11561 C CB  . ARG B 360  ? 0.4316 0.3232 0.2926 -0.1741 -0.0482 0.0592  358  ARG B CB  
11562 C CG  . ARG B 360  ? 0.5341 0.4395 0.3984 -0.1806 -0.0461 0.0624  358  ARG B CG  
11563 C CD  . ARG B 360  ? 0.5471 0.4555 0.4139 -0.1839 -0.0477 0.0616  358  ARG B CD  
11564 N NE  . ARG B 360  ? 0.5841 0.5081 0.4609 -0.1827 -0.0450 0.0597  358  ARG B NE  
11565 C CZ  . ARG B 360  ? 0.5489 0.4898 0.4321 -0.1859 -0.0422 0.0614  358  ARG B CZ  
11566 N NH1 . ARG B 360  ? 0.6428 0.5879 0.5239 -0.1908 -0.0414 0.0650  358  ARG B NH1 
11567 N NH2 . ARG B 360  ? 0.6336 0.5876 0.5257 -0.1841 -0.0400 0.0594  358  ARG B NH2 
11568 N N   . ARG B 361  ? 0.4326 0.2942 0.2829 -0.1588 -0.0527 0.0544  359  ARG B N   
11569 C CA  . ARG B 361  ? 0.4611 0.3035 0.3031 -0.1561 -0.0568 0.0533  359  ARG B CA  
11570 C C   . ARG B 361  ? 0.4192 0.2548 0.2569 -0.1510 -0.0570 0.0538  359  ARG B C   
11571 O O   . ARG B 361  ? 0.4603 0.2794 0.2895 -0.1504 -0.0605 0.0542  359  ARG B O   
11572 C CB  . ARG B 361  ? 0.5238 0.3626 0.3686 -0.1506 -0.0581 0.0487  359  ARG B CB  
11573 C CG  . ARG B 361  ? 0.5164 0.3656 0.3696 -0.1420 -0.0551 0.0450  359  ARG B CG  
11574 C CD  . ARG B 361  ? 0.4628 0.3093 0.3188 -0.1378 -0.0562 0.0408  359  ARG B CD  
11575 N NE  . ARG B 361  ? 0.4196 0.2797 0.2851 -0.1316 -0.0528 0.0379  359  ARG B NE  
11576 C CZ  . ARG B 361  ? 0.4248 0.2842 0.2923 -0.1235 -0.0520 0.0352  359  ARG B CZ  
11577 N NH1 . ARG B 361  ? 0.4410 0.2873 0.3023 -0.1200 -0.0544 0.0351  359  ARG B NH1 
11578 N NH2 . ARG B 361  ? 0.3807 0.2529 0.2570 -0.1187 -0.0489 0.0328  359  ARG B NH2 
11579 N N   . SER B 362  ? 0.4298 0.2773 0.2726 -0.1475 -0.0534 0.0538  360  SER B N   
11580 C CA  . SER B 362  ? 0.4502 0.2923 0.2893 -0.1427 -0.0536 0.0542  360  SER B CA  
11581 C C   . SER B 362  ? 0.4465 0.2886 0.2801 -0.1484 -0.0530 0.0590  360  SER B C   
11582 O O   . SER B 362  ? 0.4776 0.3130 0.3063 -0.1453 -0.0538 0.0599  360  SER B O   
11583 C CB  . SER B 362  ? 0.4705 0.3243 0.3177 -0.1348 -0.0503 0.0510  360  SER B CB  
11584 O OG  . SER B 362  ? 0.4303 0.3009 0.2836 -0.1374 -0.0463 0.0523  360  SER B OG  
11585 N N   . GLY B 363  ? 0.4393 0.2893 0.2738 -0.1564 -0.0516 0.0621  361  GLY B N   
11586 C CA  . GLY B 363  ? 0.4514 0.3025 0.2810 -0.1619 -0.0507 0.0667  361  GLY B CA  
11587 C C   . GLY B 363  ? 0.4571 0.3207 0.2910 -0.1579 -0.0467 0.0667  361  GLY B C   
11588 O O   . GLY B 363  ? 0.4835 0.3437 0.3117 -0.1588 -0.0466 0.0695  361  GLY B O   
11589 N N   . ARG B 364  ? 0.4596 0.3373 0.3030 -0.1535 -0.0435 0.0636  362  ARG B N   
11590 C CA  . ARG B 364  ? 0.4594 0.3498 0.3076 -0.1494 -0.0397 0.0631  362  ARG B CA  
11591 C C   . ARG B 364  ? 0.4576 0.3658 0.3137 -0.1528 -0.0359 0.0635  362  ARG B C   
11592 O O   . ARG B 364  ? 0.4896 0.4024 0.3516 -0.1526 -0.0358 0.0612  362  ARG B O   
11593 C CB  . ARG B 364  ? 0.4740 0.3649 0.3270 -0.1398 -0.0394 0.0583  362  ARG B CB  
11594 C CG  . ARG B 364  ? 0.4238 0.2986 0.2707 -0.1349 -0.0430 0.0571  362  ARG B CG  
11595 C CD  . ARG B 364  ? 0.4443 0.3160 0.2858 -0.1334 -0.0429 0.0592  362  ARG B CD  
11596 N NE  . ARG B 364  ? 0.4335 0.2893 0.2688 -0.1293 -0.0468 0.0584  362  ARG B NE  
11597 C CZ  . ARG B 364  ? 0.4345 0.2883 0.2724 -0.1211 -0.0473 0.0549  362  ARG B CZ  
11598 N NH1 . ARG B 364  ? 0.4278 0.2940 0.2742 -0.1162 -0.0444 0.0519  362  ARG B NH1 
11599 N NH2 . ARG B 364  ? 0.4865 0.3256 0.3183 -0.1179 -0.0510 0.0545  362  ARG B NH2 
11600 N N   . ARG B 365  ? 0.4221 0.3404 0.2785 -0.1558 -0.0328 0.0664  363  ARG B N   
11601 C CA  . ARG B 365  ? 0.4213 0.3581 0.2864 -0.1566 -0.0286 0.0659  363  ARG B CA  
11602 C C   . ARG B 365  ? 0.3765 0.3203 0.2477 -0.1476 -0.0264 0.0619  363  ARG B C   
11603 O O   . ARG B 365  ? 0.4077 0.3499 0.2762 -0.1435 -0.0257 0.0617  363  ARG B O   
11604 C CB  . ARG B 365  ? 0.4225 0.3684 0.2858 -0.1626 -0.0258 0.0703  363  ARG B CB  
11605 C CG  . ARG B 365  ? 0.4337 0.3986 0.3057 -0.1647 -0.0219 0.0704  363  ARG B CG  
11606 C CD  . ARG B 365  ? 0.4497 0.4223 0.3193 -0.1723 -0.0196 0.0753  363  ARG B CD  
11607 N NE  . ARG B 365  ? 0.4957 0.4862 0.3735 -0.1753 -0.0162 0.0758  363  ARG B NE  
11608 C CZ  . ARG B 365  ? 0.4591 0.4645 0.3402 -0.1752 -0.0118 0.0771  363  ARG B CZ  
11609 N NH1 . ARG B 365  ? 0.4538 0.4584 0.3304 -0.1726 -0.0102 0.0780  363  ARG B NH1 
11610 N NH2 . ARG B 365  ? 0.3998 0.4213 0.2887 -0.1776 -0.0090 0.0774  363  ARG B NH2 
11611 N N   . ILE B 366  ? 0.3779 0.3284 0.2567 -0.1444 -0.0257 0.0585  364  ILE B N   
11612 C CA  . ILE B 366  ? 0.3665 0.3235 0.2514 -0.1361 -0.0237 0.0546  364  ILE B CA  
11613 C C   . ILE B 366  ? 0.3786 0.3536 0.2700 -0.1364 -0.0192 0.0549  364  ILE B C   
11614 O O   . ILE B 366  ? 0.3688 0.3528 0.2639 -0.1415 -0.0179 0.0564  364  ILE B O   
11615 C CB  . ILE B 366  ? 0.3553 0.3089 0.2446 -0.1321 -0.0255 0.0507  364  ILE B CB  
11616 C CG1 . ILE B 366  ? 0.4058 0.3414 0.2884 -0.1311 -0.0299 0.0501  364  ILE B CG1 
11617 C CG2 . ILE B 366  ? 0.3452 0.3072 0.2416 -0.1242 -0.0231 0.0468  364  ILE B CG2 
11618 C CD1 . ILE B 366  ? 0.3912 0.3223 0.2769 -0.1282 -0.0318 0.0467  364  ILE B CD1 
11619 N N   . MET B 367  ? 0.3549 0.3352 0.2475 -0.1312 -0.0168 0.0538  365  MET B N   
11620 C CA  . MET B 367  ? 0.3596 0.3566 0.2583 -0.1302 -0.0125 0.0535  365  MET B CA  
11621 C C   . MET B 367  ? 0.3329 0.3364 0.2400 -0.1249 -0.0117 0.0494  365  MET B C   
11622 O O   . MET B 367  ? 0.3643 0.3617 0.2722 -0.1187 -0.0130 0.0462  365  MET B O   
11623 C CB  . MET B 367  ? 0.3417 0.3408 0.2376 -0.1265 -0.0104 0.0538  365  MET B CB  
11624 C CG  . MET B 367  ? 0.3751 0.3652 0.2617 -0.1308 -0.0118 0.0575  365  MET B CG  
11625 S SD  . MET B 367  ? 0.3738 0.3661 0.2567 -0.1262 -0.0096 0.0576  365  MET B SD  
11626 C CE  . MET B 367  ? 0.4347 0.4427 0.3184 -0.1315 -0.0050 0.0611  365  MET B CE  
11627 N N   . VAL B 368  ? 0.3061 0.3218 0.2195 -0.1275 -0.0097 0.0496  366  VAL B N   
11628 C CA  . VAL B 368  ? 0.2976 0.3190 0.2186 -0.1231 -0.0092 0.0460  366  VAL B CA  
11629 C C   . VAL B 368  ? 0.3257 0.3633 0.2530 -0.1204 -0.0049 0.0453  366  VAL B C   
11630 O O   . VAL B 368  ? 0.3109 0.3596 0.2406 -0.1249 -0.0027 0.0476  366  VAL B O   
11631 C CB  . VAL B 368  ? 0.3286 0.3492 0.2518 -0.1278 -0.0111 0.0464  366  VAL B CB  
11632 C CG1 . VAL B 368  ? 0.3125 0.3386 0.2432 -0.1227 -0.0106 0.0426  366  VAL B CG1 
11633 C CG2 . VAL B 368  ? 0.3472 0.3511 0.2635 -0.1303 -0.0154 0.0471  366  VAL B CG2 
11634 N N   . ARG B 369  ? 0.2873 0.3262 0.2171 -0.1130 -0.0038 0.0420  367  ARG B N   
11635 C CA  . ARG B 369  ? 0.2796 0.3328 0.2152 -0.1094 0.0000  0.0408  367  ARG B CA  
11636 C C   . ARG B 369  ? 0.2796 0.3391 0.2228 -0.1076 0.0001  0.0384  367  ARG B C   
11637 O O   . ARG B 369  ? 0.2783 0.3317 0.2232 -0.1031 -0.0016 0.0353  367  ARG B O   
11638 C CB  . ARG B 369  ? 0.2731 0.3247 0.2076 -0.1025 0.0010  0.0384  367  ARG B CB  
11639 C CG  . ARG B 369  ? 0.3184 0.3844 0.2583 -0.0989 0.0049  0.0372  367  ARG B CG  
11640 C CD  . ARG B 369  ? 0.2754 0.3393 0.2154 -0.0915 0.0054  0.0340  367  ARG B CD  
11641 N NE  . ARG B 369  ? 0.2772 0.3335 0.2100 -0.0912 0.0048  0.0352  367  ARG B NE  
11642 C CZ  . ARG B 369  ? 0.2792 0.3278 0.2098 -0.0861 0.0034  0.0329  367  ARG B CZ  
11643 N NH1 . ARG B 369  ? 0.2841 0.3312 0.2190 -0.0808 0.0026  0.0295  367  ARG B NH1 
11644 N NH2 . ARG B 369  ? 0.3005 0.3428 0.2242 -0.0864 0.0028  0.0344  367  ARG B NH2 
11645 N N   . LEU B 370  ? 0.2720 0.3440 0.2198 -0.1111 0.0021  0.0398  368  LEU B N   
11646 C CA  . LEU B 370  ? 0.2606 0.3404 0.2158 -0.1092 0.0026  0.0377  368  LEU B CA  
11647 C C   . LEU B 370  ? 0.2438 0.3343 0.2038 -0.1028 0.0060  0.0355  368  LEU B C   
11648 O O   . LEU B 370  ? 0.2628 0.3630 0.2231 -0.1034 0.0090  0.0370  368  LEU B O   
11649 C CB  . LEU B 370  ? 0.2632 0.3515 0.2211 -0.1161 0.0029  0.0404  368  LEU B CB  
11650 C CG  . LEU B 370  ? 0.2763 0.3720 0.2417 -0.1149 0.0028  0.0385  368  LEU B CG  
11651 C CD1 . LEU B 370  ? 0.2878 0.3715 0.2522 -0.1135 -0.0008 0.0362  368  LEU B CD1 
11652 C CD2 . LEU B 370  ? 0.2865 0.3925 0.2547 -0.1219 0.0034  0.0415  368  LEU B CD2 
11653 N N   . VAL B 371  ? 0.2365 0.3246 0.1997 -0.0967 0.0054  0.0319  369  VAL B N   
11654 C CA  . VAL B 371  ? 0.2377 0.3345 0.2055 -0.0904 0.0081  0.0294  369  VAL B CA  
11655 C C   . VAL B 371  ? 0.2382 0.3404 0.2127 -0.0886 0.0078  0.0275  369  VAL B C   
11656 O O   . VAL B 371  ? 0.2437 0.3411 0.2187 -0.0915 0.0053  0.0276  369  VAL B O   
11657 C CB  . VAL B 371  ? 0.2133 0.3017 0.1783 -0.0842 0.0075  0.0269  369  VAL B CB  
11658 C CG1 . VAL B 371  ? 0.2556 0.3370 0.2133 -0.0861 0.0071  0.0288  369  VAL B CG1 
11659 C CG2 . VAL B 371  ? 0.2507 0.3289 0.2164 -0.0818 0.0045  0.0245  369  VAL B CG2 
11660 N N   . LYS B 372  ? 0.2336 0.3454 0.2130 -0.0836 0.0103  0.0256  370  LYS B N   
11661 C CA  . LYS B 372  ? 0.2483 0.3633 0.2336 -0.0807 0.0098  0.0233  370  LYS B CA  
11662 C C   . LYS B 372  ? 0.2171 0.3211 0.2014 -0.0758 0.0078  0.0203  370  LYS B C   
11663 O O   . LYS B 372  ? 0.2312 0.3278 0.2153 -0.0770 0.0051  0.0197  370  LYS B O   
11664 C CB  . LYS B 372  ? 0.2454 0.3752 0.2365 -0.0778 0.0131  0.0227  370  LYS B CB  
11665 C CG  . LYS B 372  ? 0.2599 0.4007 0.2528 -0.0837 0.0145  0.0259  370  LYS B CG  
11666 C CD  . LYS B 372  ? 0.2530 0.4094 0.2515 -0.0812 0.0178  0.0258  370  LYS B CD  
11667 C CE  . LYS B 372  ? 0.2986 0.4654 0.2980 -0.0876 0.0193  0.0294  370  LYS B CE  
11668 N NZ  . LYS B 372  ? 0.2903 0.4731 0.2951 -0.0848 0.0229  0.0294  370  LYS B NZ  
11669 N N   . GLY B 373  ? 0.2182 0.3207 0.2015 -0.0704 0.0089  0.0184  371  GLY B N   
11670 C CA  . GLY B 373  ? 0.2014 0.2931 0.1832 -0.0662 0.0069  0.0159  371  GLY B CA  
11671 C C   . GLY B 373  ? 0.2199 0.3145 0.2037 -0.0595 0.0087  0.0133  371  GLY B C   
11672 O O   . GLY B 373  ? 0.2497 0.3542 0.2378 -0.0571 0.0108  0.0126  371  GLY B O   
11673 N N   . ALA B 374  ? 0.2072 0.2926 0.1877 -0.0564 0.0074  0.0119  372  ALA B N   
11674 C CA  . ALA B 374  ? 0.2289 0.3157 0.2098 -0.0507 0.0089  0.0097  372  ALA B CA  
11675 C C   . ALA B 374  ? 0.2078 0.2911 0.1920 -0.0459 0.0078  0.0068  372  ALA B C   
11676 O O   . ALA B 374  ? 0.2449 0.3290 0.2296 -0.0411 0.0088  0.0048  372  ALA B O   
11677 C CB  . ALA B 374  ? 0.2323 0.3121 0.2072 -0.0505 0.0083  0.0102  372  ALA B CB  
11678 N N   . TYR B 375  ? 0.2050 0.2843 0.1912 -0.0469 0.0059  0.0064  373  TYR B N   
11679 C CA  . TYR B 375  ? 0.1977 0.2726 0.1864 -0.0426 0.0048  0.0038  373  TYR B CA  
11680 C C   . TYR B 375  ? 0.2132 0.2942 0.2073 -0.0418 0.0052  0.0029  373  TYR B C   
11681 O O   . TYR B 375  ? 0.1961 0.2726 0.1919 -0.0399 0.0039  0.0013  373  TYR B O   
11682 C CB  . TYR B 375  ? 0.2217 0.2851 0.2076 -0.0435 0.0019  0.0036  373  TYR B CB  
11683 C CG  . TYR B 375  ? 0.2326 0.2891 0.2131 -0.0442 0.0010  0.0044  373  TYR B CG  
11684 C CD1 . TYR B 375  ? 0.2307 0.2863 0.2071 -0.0489 0.0008  0.0071  373  TYR B CD1 
11685 C CD2 . TYR B 375  ? 0.2554 0.3059 0.2347 -0.0403 0.0001  0.0027  373  TYR B CD2 
11686 C CE1 . TYR B 375  ? 0.2512 0.3002 0.2223 -0.0495 -0.0002 0.0080  373  TYR B CE1 
11687 C CE2 . TYR B 375  ? 0.2970 0.3411 0.2712 -0.0408 -0.0010 0.0036  373  TYR B CE2 
11688 C CZ  . TYR B 375  ? 0.2633 0.3065 0.2334 -0.0453 -0.0011 0.0062  373  TYR B CZ  
11689 O OH  . TYR B 375  ? 0.2955 0.3322 0.2603 -0.0458 -0.0023 0.0071  373  TYR B OH  
11690 N N   . TRP B 376  ? 0.1883 0.2797 0.1851 -0.0430 0.0072  0.0039  374  TRP B N   
11691 C CA  . TRP B 376  ? 0.1882 0.2853 0.1898 -0.0432 0.0072  0.0035  374  TRP B CA  
11692 C C   . TRP B 376  ? 0.1798 0.2758 0.1845 -0.0379 0.0071  0.0009  374  TRP B C   
11693 O O   . TRP B 376  ? 0.1870 0.2795 0.1933 -0.0379 0.0055  0.0002  374  TRP B O   
11694 C CB  . TRP B 376  ? 0.1748 0.2843 0.1791 -0.0447 0.0095  0.0050  374  TRP B CB  
11695 C CG  . TRP B 376  ? 0.1912 0.3064 0.2003 -0.0452 0.0092  0.0048  374  TRP B CG  
11696 C CD1 . TRP B 376  ? 0.1934 0.3079 0.2030 -0.0498 0.0075  0.0060  374  TRP B CD1 
11697 C CD2 . TRP B 376  ? 0.2082 0.3303 0.2220 -0.0409 0.0104  0.0032  374  TRP B CD2 
11698 N NE1 . TRP B 376  ? 0.1821 0.3031 0.1966 -0.0487 0.0076  0.0054  374  TRP B NE1 
11699 C CE2 . TRP B 376  ? 0.2030 0.3286 0.2201 -0.0431 0.0094  0.0037  374  TRP B CE2 
11700 C CE3 . TRP B 376  ? 0.2323 0.3576 0.2474 -0.0352 0.0121  0.0014  374  TRP B CE3 
11701 C CZ2 . TRP B 376  ? 0.1945 0.3269 0.2163 -0.0398 0.0100  0.0025  374  TRP B CZ2 
11702 C CZ3 . TRP B 376  ? 0.2432 0.3748 0.2628 -0.0320 0.0128  0.0003  374  TRP B CZ3 
11703 C CH2 . TRP B 376  ? 0.2227 0.3580 0.2457 -0.0342 0.0117  0.0009  374  TRP B CH2 
11704 N N   . ASP B 377  ? 0.1936 0.2923 0.1989 -0.0334 0.0087  -0.0005 375  ASP B N   
11705 C CA  . ASP B 377  ? 0.2226 0.3205 0.2308 -0.0285 0.0086  -0.0028 375  ASP B CA  
11706 C C   . ASP B 377  ? 0.1898 0.2772 0.1967 -0.0278 0.0064  -0.0039 375  ASP B C   
11707 O O   . ASP B 377  ? 0.2000 0.2861 0.2096 -0.0260 0.0056  -0.0051 375  ASP B O   
11708 C CB  . ASP B 377  ? 0.2683 0.3681 0.2760 -0.0239 0.0103  -0.0042 375  ASP B CB  
11709 C CG  . ASP B 377  ? 0.4157 0.5263 0.4250 -0.0234 0.0128  -0.0036 375  ASP B CG  
11710 O OD1 . ASP B 377  ? 0.5137 0.6316 0.5268 -0.0240 0.0133  -0.0031 375  ASP B OD1 
11711 O OD2 . ASP B 377  ? 0.5938 0.7057 0.6003 -0.0221 0.0142  -0.0036 375  ASP B OD2 
11712 N N   . ALA B 378  ? 0.1869 0.2669 0.1897 -0.0290 0.0053  -0.0035 376  ALA B N   
11713 C CA  . ALA B 378  ? 0.1859 0.2565 0.1876 -0.0280 0.0032  -0.0046 376  ALA B CA  
11714 C C   . ALA B 378  ? 0.2017 0.2691 0.2039 -0.0309 0.0016  -0.0040 376  ALA B C   
11715 O O   . ALA B 378  ? 0.1956 0.2579 0.1987 -0.0292 0.0003  -0.0053 376  ALA B O   
11716 C CB  . ALA B 378  ? 0.2291 0.2930 0.2261 -0.0285 0.0024  -0.0041 376  ALA B CB  
11717 N N   . GLU B 379  ? 0.1868 0.2570 0.1881 -0.0354 0.0015  -0.0021 377  GLU B N   
11718 C CA  . GLU B 379  ? 0.1771 0.2439 0.1783 -0.0384 -0.0002 -0.0016 377  GLU B CA  
11719 C C   . GLU B 379  ? 0.2053 0.2768 0.2109 -0.0368 0.0000  -0.0027 377  GLU B C   
11720 O O   . GLU B 379  ? 0.1931 0.2599 0.1990 -0.0368 -0.0015 -0.0034 377  GLU B O   
11721 C CB  . GLU B 379  ? 0.1901 0.2588 0.1892 -0.0440 -0.0005 0.0009  377  GLU B CB  
11722 C CG  . GLU B 379  ? 0.2140 0.2771 0.2079 -0.0463 -0.0011 0.0023  377  GLU B CG  
11723 C CD  . GLU B 379  ? 0.2288 0.2802 0.2192 -0.0460 -0.0034 0.0017  377  GLU B CD  
11724 O OE1 . GLU B 379  ? 0.2516 0.2988 0.2433 -0.0444 -0.0047 0.0003  377  GLU B OE1 
11725 O OE2 . GLU B 379  ? 0.2317 0.2783 0.2179 -0.0474 -0.0040 0.0029  377  GLU B OE2 
11726 N N   . ILE B 380  ? 0.1881 0.2690 0.1971 -0.0353 0.0020  -0.0027 378  ILE B N   
11727 C CA  . ILE B 380  ? 0.1713 0.2567 0.1843 -0.0333 0.0022  -0.0037 378  ILE B CA  
11728 C C   . ILE B 380  ? 0.1793 0.2590 0.1931 -0.0290 0.0016  -0.0058 378  ILE B C   
11729 O O   . ILE B 380  ? 0.1737 0.2507 0.1886 -0.0287 0.0005  -0.0066 378  ILE B O   
11730 C CB  . ILE B 380  ? 0.1795 0.2759 0.1959 -0.0318 0.0043  -0.0035 378  ILE B CB  
11731 C CG1 . ILE B 380  ? 0.1757 0.2786 0.1917 -0.0363 0.0050  -0.0012 378  ILE B CG1 
11732 C CG2 . ILE B 380  ? 0.1875 0.2882 0.2079 -0.0295 0.0043  -0.0045 378  ILE B CG2 
11733 C CD1 . ILE B 380  ? 0.2046 0.3078 0.2210 -0.0410 0.0034  0.0000  378  ILE B CD1 
11734 N N   . LYS B 381  ? 0.1710 0.2487 0.1840 -0.0258 0.0024  -0.0068 379  LYS B N   
11735 C CA  . LYS B 381  ? 0.1758 0.2485 0.1895 -0.0219 0.0019  -0.0086 379  LYS B CA  
11736 C C   . LYS B 381  ? 0.1801 0.2441 0.1920 -0.0230 -0.0001 -0.0089 379  LYS B C   
11737 O O   . LYS B 381  ? 0.1796 0.2413 0.1931 -0.0213 -0.0007 -0.0099 379  LYS B O   
11738 C CB  . LYS B 381  ? 0.1856 0.2571 0.1982 -0.0189 0.0027  -0.0094 379  LYS B CB  
11739 C CG  . LYS B 381  ? 0.1919 0.2578 0.2052 -0.0154 0.0020  -0.0111 379  LYS B CG  
11740 C CD  . LYS B 381  ? 0.1721 0.2374 0.1843 -0.0125 0.0027  -0.0120 379  LYS B CD  
11741 C CE  . LYS B 381  ? 0.2109 0.2718 0.2243 -0.0091 0.0021  -0.0136 379  LYS B CE  
11742 N NZ  . LYS B 381  ? 0.1829 0.2427 0.1949 -0.0066 0.0025  -0.0145 379  LYS B NZ  
11743 N N   . ARG B 382  ? 0.1830 0.2423 0.1914 -0.0258 -0.0010 -0.0078 380  ARG B N   
11744 C CA  . ARG B 382  ? 0.1837 0.2343 0.1900 -0.0262 -0.0029 -0.0082 380  ARG B CA  
11745 C C   . ARG B 382  ? 0.1808 0.2307 0.1879 -0.0279 -0.0039 -0.0082 380  ARG B C   
11746 O O   . ARG B 382  ? 0.1860 0.2311 0.1934 -0.0262 -0.0048 -0.0093 380  ARG B O   
11747 C CB  . ARG B 382  ? 0.2225 0.2684 0.2245 -0.0291 -0.0038 -0.0069 380  ARG B CB  
11748 C CG  . ARG B 382  ? 0.2873 0.3239 0.2868 -0.0291 -0.0058 -0.0072 380  ARG B CG  
11749 C CD  . ARG B 382  ? 0.3997 0.4329 0.3997 -0.0252 -0.0059 -0.0086 380  ARG B CD  
11750 N NE  . ARG B 382  ? 0.4344 0.4655 0.4369 -0.0225 -0.0063 -0.0101 380  ARG B NE  
11751 C CZ  . ARG B 382  ? 0.4412 0.4714 0.4455 -0.0189 -0.0061 -0.0114 380  ARG B CZ  
11752 N NH1 . ARG B 382  ? 0.4242 0.4553 0.4282 -0.0174 -0.0056 -0.0116 380  ARG B NH1 
11753 N NH2 . ARG B 382  ? 0.4179 0.4462 0.4243 -0.0170 -0.0064 -0.0125 380  ARG B NH2 
11754 N N   . ALA B 383  ? 0.1721 0.2269 0.1795 -0.0312 -0.0037 -0.0070 381  ALA B N   
11755 C CA  . ALA B 383  ? 0.1714 0.2252 0.1791 -0.0331 -0.0049 -0.0070 381  ALA B CA  
11756 C C   . ALA B 383  ? 0.1848 0.2417 0.1961 -0.0299 -0.0043 -0.0084 381  ALA B C   
11757 O O   . ALA B 383  ? 0.1930 0.2459 0.2040 -0.0295 -0.0054 -0.0092 381  ALA B O   
11758 C CB  . ALA B 383  ? 0.1924 0.2517 0.1999 -0.0377 -0.0049 -0.0052 381  ALA B CB  
11759 N N   . GLN B 384  ? 0.1624 0.2259 0.1767 -0.0273 -0.0027 -0.0087 382  GLN B N   
11760 C CA  . GLN B 384  ? 0.1790 0.2449 0.1964 -0.0239 -0.0021 -0.0100 382  GLN B CA  
11761 C C   . GLN B 384  ? 0.1675 0.2265 0.1844 -0.0208 -0.0026 -0.0114 382  GLN B C   
11762 O O   . GLN B 384  ? 0.1799 0.2370 0.1977 -0.0197 -0.0031 -0.0122 382  GLN B O   
11763 C CB  . GLN B 384  ? 0.1812 0.2550 0.2014 -0.0216 -0.0004 -0.0100 382  GLN B CB  
11764 C CG  . GLN B 384  ? 0.1690 0.2512 0.1908 -0.0241 0.0002  -0.0087 382  GLN B CG  
11765 C CD  . GLN B 384  ? 0.1839 0.2740 0.2085 -0.0212 0.0019  -0.0089 382  GLN B CD  
11766 O OE1 . GLN B 384  ? 0.2023 0.2909 0.2268 -0.0179 0.0028  -0.0098 382  GLN B OE1 
11767 N NE2 . GLN B 384  ? 0.1766 0.2750 0.2037 -0.0224 0.0024  -0.0080 382  GLN B NE2 
11768 N N   . LEU B 385  ? 0.1806 0.2363 0.1963 -0.0195 -0.0024 -0.0116 383  LEU B N   
11769 C CA  . LEU B 385  ? 0.1792 0.2288 0.1948 -0.0168 -0.0029 -0.0128 383  LEU B CA  
11770 C C   . LEU B 385  ? 0.1762 0.2197 0.1901 -0.0180 -0.0043 -0.0130 383  LEU B C   
11771 O O   . LEU B 385  ? 0.1816 0.2223 0.1965 -0.0158 -0.0045 -0.0141 383  LEU B O   
11772 C CB  . LEU B 385  ? 0.2048 0.2515 0.2187 -0.0159 -0.0029 -0.0129 383  LEU B CB  
11773 C CG  . LEU B 385  ? 0.2306 0.2817 0.2458 -0.0137 -0.0015 -0.0132 383  LEU B CG  
11774 C CD1 . LEU B 385  ? 0.2433 0.2905 0.2561 -0.0134 -0.0019 -0.0132 383  LEU B CD1 
11775 C CD2 . LEU B 385  ? 0.2432 0.2952 0.2613 -0.0103 -0.0009 -0.0144 383  LEU B CD2 
11776 N N   . ASP B 386  ? 0.2007 0.2416 0.2116 -0.0214 -0.0054 -0.0121 384  ASP B N   
11777 C CA  . ASP B 386  ? 0.1997 0.2336 0.2082 -0.0224 -0.0069 -0.0123 384  ASP B CA  
11778 C C   . ASP B 386  ? 0.2102 0.2450 0.2188 -0.0237 -0.0074 -0.0125 384  ASP B C   
11779 O O   . ASP B 386  ? 0.2078 0.2368 0.2142 -0.0243 -0.0087 -0.0129 384  ASP B O   
11780 C CB  . ASP B 386  ? 0.2200 0.2492 0.2245 -0.0252 -0.0081 -0.0113 384  ASP B CB  
11781 C CG  . ASP B 386  ? 0.2714 0.2979 0.2751 -0.0235 -0.0080 -0.0113 384  ASP B CG  
11782 O OD1 . ASP B 386  ? 0.2897 0.3171 0.2957 -0.0201 -0.0073 -0.0123 384  ASP B OD1 
11783 O OD2 . ASP B 386  ? 0.2911 0.3146 0.2916 -0.0257 -0.0088 -0.0102 384  ASP B OD2 
11784 N N   . GLY B 387  ? 0.1836 0.2257 0.1948 -0.0241 -0.0066 -0.0122 385  GLY B N   
11785 C CA  . GLY B 387  ? 0.2072 0.2506 0.2188 -0.0252 -0.0072 -0.0124 385  GLY B CA  
11786 C C   . GLY B 387  ? 0.2227 0.2628 0.2308 -0.0295 -0.0088 -0.0116 385  GLY B C   
11787 O O   . GLY B 387  ? 0.2240 0.2606 0.2306 -0.0301 -0.0100 -0.0122 385  GLY B O   
11788 N N   . LEU B 388  ? 0.2098 0.2508 0.2164 -0.0325 -0.0090 -0.0102 386  LEU B N   
11789 C CA  . LEU B 388  ? 0.2078 0.2446 0.2107 -0.0368 -0.0107 -0.0093 386  LEU B CA  
11790 C C   . LEU B 388  ? 0.1945 0.2376 0.1986 -0.0402 -0.0111 -0.0084 386  LEU B C   
11791 O O   . LEU B 388  ? 0.2110 0.2624 0.2190 -0.0391 -0.0098 -0.0083 386  LEU B O   
11792 C CB  . LEU B 388  ? 0.2127 0.2462 0.2128 -0.0387 -0.0110 -0.0081 386  LEU B CB  
11793 C CG  . LEU B 388  ? 0.2173 0.2441 0.2161 -0.0354 -0.0111 -0.0091 386  LEU B CG  
11794 C CD1 . LEU B 388  ? 0.2578 0.2811 0.2535 -0.0371 -0.0115 -0.0079 386  LEU B CD1 
11795 C CD2 . LEU B 388  ? 0.2548 0.2740 0.2516 -0.0340 -0.0125 -0.0105 386  LEU B CD2 
11796 N N   . ALA B 389  ? 0.2130 0.2519 0.2136 -0.0443 -0.0130 -0.0077 387  ALA B N   
11797 C CA  . ALA B 389  ? 0.2037 0.2474 0.2052 -0.0475 -0.0138 -0.0071 387  ALA B CA  
11798 C C   . ALA B 389  ? 0.2229 0.2771 0.2278 -0.0496 -0.0126 -0.0055 387  ALA B C   
11799 O O   . ALA B 389  ? 0.2543 0.3161 0.2623 -0.0500 -0.0123 -0.0053 387  ALA B O   
11800 C CB  . ALA B 389  ? 0.2616 0.2979 0.2581 -0.0519 -0.0163 -0.0067 387  ALA B CB  
11801 N N   . ASP B 390  ? 0.2135 0.2684 0.2176 -0.0508 -0.0117 -0.0042 388  ASP B N   
11802 C CA  . ASP B 390  ? 0.2125 0.2774 0.2194 -0.0527 -0.0104 -0.0026 388  ASP B CA  
11803 C C   . ASP B 390  ? 0.1882 0.2518 0.1939 -0.0518 -0.0091 -0.0020 388  ASP B C   
11804 O O   . ASP B 390  ? 0.2000 0.2554 0.2030 -0.0498 -0.0095 -0.0028 388  ASP B O   
11805 C CB  . ASP B 390  ? 0.2178 0.2851 0.2236 -0.0589 -0.0118 -0.0008 388  ASP B CB  
11806 C CG  . ASP B 390  ? 0.2364 0.3166 0.2469 -0.0603 -0.0105 0.0005  388  ASP B CG  
11807 O OD1 . ASP B 390  ? 0.2375 0.3240 0.2503 -0.0585 -0.0083 0.0010  388  ASP B OD1 
11808 O OD2 . ASP B 390  ? 0.2844 0.3686 0.2961 -0.0631 -0.0117 0.0009  388  ASP B OD2 
11809 N N   . PHE B 391  ? 0.1913 0.2634 0.1991 -0.0530 -0.0075 -0.0006 389  PHE B N   
11810 C CA  . PHE B 391  ? 0.2037 0.2751 0.2099 -0.0527 -0.0064 0.0002  389  PHE B CA  
11811 C C   . PHE B 391  ? 0.1984 0.2643 0.1999 -0.0579 -0.0078 0.0020  389  PHE B C   
11812 O O   . PHE B 391  ? 0.2163 0.2825 0.2169 -0.0625 -0.0092 0.0032  389  PHE B O   
11813 C CB  . PHE B 391  ? 0.2096 0.2925 0.2195 -0.0520 -0.0040 0.0010  389  PHE B CB  
11814 C CG  . PHE B 391  ? 0.1792 0.2672 0.1933 -0.0469 -0.0027 -0.0007 389  PHE B CG  
11815 C CD1 . PHE B 391  ? 0.1859 0.2701 0.1999 -0.0420 -0.0019 -0.0023 389  PHE B CD1 
11816 C CD2 . PHE B 391  ? 0.1828 0.2787 0.2008 -0.0470 -0.0026 -0.0006 389  PHE B CD2 
11817 C CE1 . PHE B 391  ? 0.2003 0.2883 0.2179 -0.0374 -0.0009 -0.0038 389  PHE B CE1 
11818 C CE2 . PHE B 391  ? 0.1916 0.2913 0.2130 -0.0421 -0.0015 -0.0021 389  PHE B CE2 
11819 C CZ  . PHE B 391  ? 0.1853 0.2809 0.2064 -0.0374 -0.0007 -0.0037 389  PHE B CZ  
11820 N N   . PRO B 392  ? 0.1915 0.2521 0.1898 -0.0574 -0.0076 0.0024  390  PRO B N   
11821 C CA  . PRO B 392  ? 0.1733 0.2289 0.1669 -0.0624 -0.0088 0.0044  390  PRO B CA  
11822 C C   . PRO B 392  ? 0.2068 0.2709 0.2011 -0.0653 -0.0071 0.0067  390  PRO B C   
11823 O O   . PRO B 392  ? 0.2129 0.2736 0.2032 -0.0694 -0.0078 0.0086  390  PRO B O   
11824 C CB  . PRO B 392  ? 0.2091 0.2552 0.1992 -0.0595 -0.0094 0.0036  390  PRO B CB  
11825 C CG  . PRO B 392  ? 0.2129 0.2640 0.2065 -0.0541 -0.0073 0.0021  390  PRO B CG  
11826 C CD  . PRO B 392  ? 0.1993 0.2573 0.1978 -0.0523 -0.0065 0.0010  390  PRO B CD  
11827 N N   . VAL B 393  ? 0.2056 0.2805 0.2047 -0.0630 -0.0048 0.0064  391  VAL B N   
11828 C CA  . VAL B 393  ? 0.2014 0.2864 0.2020 -0.0652 -0.0028 0.0083  391  VAL B CA  
11829 C C   . VAL B 393  ? 0.2019 0.2980 0.2080 -0.0656 -0.0020 0.0084  391  VAL B C   
11830 O O   . VAL B 393  ? 0.2037 0.2997 0.2123 -0.0630 -0.0027 0.0067  391  VAL B O   
11831 C CB  . VAL B 393  ? 0.2069 0.2944 0.2078 -0.0608 -0.0005 0.0077  391  VAL B CB  
11832 C CG1 . VAL B 393  ? 0.2065 0.2834 0.2021 -0.0605 -0.0015 0.0077  391  VAL B CG1 
11833 C CG2 . VAL B 393  ? 0.2047 0.2949 0.2095 -0.0547 0.0005  0.0051  391  VAL B CG2 
11834 N N   . PHE B 394  ? 0.2046 0.3105 0.2124 -0.0688 -0.0005 0.0105  392  PHE B N   
11835 C CA  . PHE B 394  ? 0.1802 0.2983 0.1936 -0.0687 0.0005  0.0107  392  PHE B CA  
11836 C C   . PHE B 394  ? 0.1862 0.3100 0.2033 -0.0620 0.0027  0.0087  392  PHE B C   
11837 O O   . PHE B 394  ? 0.2043 0.3242 0.2196 -0.0581 0.0038  0.0077  392  PHE B O   
11838 C CB  . PHE B 394  ? 0.1979 0.3253 0.2121 -0.0740 0.0016  0.0136  392  PHE B CB  
11839 C CG  . PHE B 394  ? 0.2043 0.3258 0.2146 -0.0809 -0.0007 0.0156  392  PHE B CG  
11840 C CD1 . PHE B 394  ? 0.2047 0.3242 0.2157 -0.0838 -0.0032 0.0155  392  PHE B CD1 
11841 C CD2 . PHE B 394  ? 0.2050 0.3216 0.2105 -0.0844 -0.0007 0.0175  392  PHE B CD2 
11842 C CE1 . PHE B 394  ? 0.2234 0.3361 0.2303 -0.0901 -0.0057 0.0171  392  PHE B CE1 
11843 C CE2 . PHE B 394  ? 0.2181 0.3281 0.2196 -0.0907 -0.0031 0.0193  392  PHE B CE2 
11844 C CZ  . PHE B 394  ? 0.2364 0.3443 0.2385 -0.0936 -0.0056 0.0191  392  PHE B CZ  
11845 N N   . THR B 395  ? 0.1967 0.3292 0.2188 -0.0605 0.0031  0.0083  393  THR B N   
11846 C CA  . THR B 395  ? 0.1901 0.3279 0.2157 -0.0542 0.0050  0.0064  393  THR B CA  
11847 C C   . THR B 395  ? 0.1688 0.3208 0.1987 -0.0537 0.0074  0.0075  393  THR B C   
11848 O O   . THR B 395  ? 0.2210 0.3775 0.2532 -0.0482 0.0092  0.0061  393  THR B O   
11849 C CB  . THR B 395  ? 0.2097 0.3452 0.2376 -0.0514 0.0035  0.0046  393  THR B CB  
11850 O OG1 . THR B 395  ? 0.2113 0.3528 0.2417 -0.0551 0.0023  0.0057  393  THR B OG1 
11851 C CG2 . THR B 395  ? 0.2045 0.3264 0.2283 -0.0510 0.0015  0.0033  393  THR B CG2 
11852 N N   . ARG B 396  ? 0.2146 0.3737 0.2455 -0.0592 0.0074  0.0100  394  ARG B N   
11853 C CA  . ARG B 396  ? 0.2132 0.3863 0.2479 -0.0592 0.0099  0.0113  394  ARG B CA  
11854 C C   . ARG B 396  ? 0.2012 0.3746 0.2325 -0.0627 0.0113  0.0134  394  ARG B C   
11855 O O   . ARG B 396  ? 0.1994 0.3670 0.2273 -0.0684 0.0096  0.0151  394  ARG B O   
11856 C CB  . ARG B 396  ? 0.2093 0.3922 0.2484 -0.0630 0.0091  0.0129  394  ARG B CB  
11857 C CG  . ARG B 396  ? 0.2217 0.4056 0.2643 -0.0596 0.0078  0.0111  394  ARG B CG  
11858 C CD  . ARG B 396  ? 0.2555 0.4516 0.3032 -0.0629 0.0073  0.0127  394  ARG B CD  
11859 N NE  . ARG B 396  ? 0.2713 0.4666 0.3214 -0.0604 0.0056  0.0111  394  ARG B NE  
11860 C CZ  . ARG B 396  ? 0.3065 0.5125 0.3620 -0.0572 0.0062  0.0108  394  ARG B CZ  
11861 N NH1 . ARG B 396  ? 0.3090 0.5282 0.3685 -0.0563 0.0086  0.0120  394  ARG B NH1 
11862 N NH2 . ARG B 396  ? 0.2904 0.4939 0.3472 -0.0548 0.0044  0.0093  394  ARG B NH2 
11863 N N   . LYS B 397  ? 0.2258 0.4060 0.2578 -0.0593 0.0142  0.0133  395  LYS B N   
11864 C CA  . LYS B 397  ? 0.2636 0.4436 0.2918 -0.0619 0.0157  0.0150  395  LYS B CA  
11865 C C   . LYS B 397  ? 0.2113 0.3981 0.2402 -0.0694 0.0156  0.0183  395  LYS B C   
11866 O O   . LYS B 397  ? 0.2352 0.4167 0.2596 -0.0741 0.0151  0.0202  395  LYS B O   
11867 C CB  . LYS B 397  ? 0.2716 0.4586 0.3007 -0.0565 0.0190  0.0141  395  LYS B CB  
11868 C CG  . LYS B 397  ? 0.2516 0.4355 0.2756 -0.0575 0.0204  0.0151  395  LYS B CG  
11869 C CD  . LYS B 397  ? 0.2668 0.4620 0.2918 -0.0620 0.0225  0.0181  395  LYS B CD  
11870 C CE  . LYS B 397  ? 0.2680 0.4605 0.2876 -0.0628 0.0241  0.0192  395  LYS B CE  
11871 N NZ  . LYS B 397  ? 0.2497 0.4534 0.2702 -0.0678 0.0262  0.0224  395  LYS B NZ  
11872 N N   . ILE B 398  ? 0.2128 0.4113 0.2474 -0.0706 0.0158  0.0191  396  ILE B N   
11873 C CA  . ILE B 398  ? 0.2612 0.4670 0.2971 -0.0780 0.0155  0.0224  396  ILE B CA  
11874 C C   . ILE B 398  ? 0.1896 0.3838 0.2214 -0.0842 0.0120  0.0233  396  ILE B C   
11875 O O   . ILE B 398  ? 0.2229 0.4181 0.2529 -0.0910 0.0116  0.0262  396  ILE B O   
11876 C CB  . ILE B 398  ? 0.2697 0.4903 0.3130 -0.0776 0.0161  0.0228  396  ILE B CB  
11877 C CG1 . ILE B 398  ? 0.3544 0.5854 0.3997 -0.0849 0.0166  0.0263  396  ILE B CG1 
11878 C CG2 . ILE B 398  ? 0.2632 0.4794 0.3085 -0.0767 0.0132  0.0211  396  ILE B CG2 
11879 C CD1 . ILE B 398  ? 0.3324 0.5800 0.3852 -0.0839 0.0179  0.0269  396  ILE B CD1 
11880 N N   . HIS B 399  ? 0.2246 0.4074 0.2547 -0.0819 0.0096  0.0211  397  HIS B N   
11881 C CA  . HIS B 399  ? 0.2428 0.4137 0.2685 -0.0870 0.0062  0.0217  397  HIS B CA  
11882 C C   . HIS B 399  ? 0.1996 0.3603 0.2186 -0.0890 0.0061  0.0226  397  HIS B C   
11883 O O   . HIS B 399  ? 0.2287 0.3844 0.2442 -0.0955 0.0044  0.0248  397  HIS B O   
11884 C CB  . HIS B 399  ? 0.2291 0.3908 0.2545 -0.0833 0.0040  0.0188  397  HIS B CB  
11885 C CG  . HIS B 399  ? 0.2346 0.4045 0.2656 -0.0824 0.0033  0.0181  397  HIS B CG  
11886 N ND1 . HIS B 399  ? 0.2340 0.3985 0.2657 -0.0782 0.0019  0.0156  397  HIS B ND1 
11887 C CD2 . HIS B 399  ? 0.2673 0.4506 0.3034 -0.0852 0.0038  0.0198  397  HIS B CD2 
11888 C CE1 . HIS B 399  ? 0.2424 0.4161 0.2792 -0.0784 0.0014  0.0156  397  HIS B CE1 
11889 N NE2 . HIS B 399  ? 0.2508 0.4361 0.2905 -0.0825 0.0025  0.0181  397  HIS B NE2 
11890 N N   . THR B 400  ? 0.2225 0.3798 0.2397 -0.0836 0.0078  0.0211  398  THR B N   
11891 C CA  . THR B 400  ? 0.2337 0.3827 0.2447 -0.0852 0.0080  0.0221  398  THR B CA  
11892 C C   . THR B 400  ? 0.2000 0.3574 0.2105 -0.0906 0.0097  0.0255  398  THR B C   
11893 O O   . THR B 400  ? 0.2477 0.3982 0.2531 -0.0957 0.0085  0.0276  398  THR B O   
11894 C CB  . THR B 400  ? 0.2043 0.3501 0.2140 -0.0782 0.0096  0.0199  398  THR B CB  
11895 O OG1 . THR B 400  ? 0.1926 0.3289 0.2019 -0.0742 0.0077  0.0171  398  THR B OG1 
11896 C CG2 . THR B 400  ? 0.2528 0.3921 0.2565 -0.0797 0.0101  0.0211  398  THR B CG2 
11897 N N   . ASP B 401  ? 0.2368 0.4092 0.2525 -0.0897 0.0124  0.0262  399  ASP B N   
11898 C CA  . ASP B 401  ? 0.2909 0.4728 0.3067 -0.0948 0.0143  0.0296  399  ASP B CA  
11899 C C   . ASP B 401  ? 0.2068 0.3880 0.2221 -0.1033 0.0119  0.0323  399  ASP B C   
11900 O O   . ASP B 401  ? 0.2556 0.4350 0.2669 -0.1090 0.0119  0.0352  399  ASP B O   
11901 C CB  . ASP B 401  ? 0.2815 0.4803 0.3036 -0.0917 0.0177  0.0296  399  ASP B CB  
11902 C CG  . ASP B 401  ? 0.3114 0.5112 0.3328 -0.0843 0.0205  0.0275  399  ASP B CG  
11903 O OD1 . ASP B 401  ? 0.2930 0.4824 0.3084 -0.0832 0.0203  0.0270  399  ASP B OD1 
11904 O OD2 . ASP B 401  ? 0.3079 0.5186 0.3343 -0.0795 0.0227  0.0263  399  ASP B OD2 
11905 N N   . VAL B 402  ? 0.2328 0.4150 0.2517 -0.1042 0.0097  0.0315  400  VAL B N   
11906 C CA  . VAL B 402  ? 0.2665 0.4471 0.2846 -0.1122 0.0070  0.0338  400  VAL B CA  
11907 C C   . VAL B 402  ? 0.2234 0.3865 0.2338 -0.1152 0.0041  0.0340  400  VAL B C   
11908 O O   . VAL B 402  ? 0.2431 0.4031 0.2499 -0.1224 0.0028  0.0368  400  VAL B O   
11909 C CB  . VAL B 402  ? 0.2519 0.4368 0.2753 -0.1119 0.0052  0.0325  400  VAL B CB  
11910 C CG1 . VAL B 402  ? 0.2883 0.4688 0.3098 -0.1202 0.0017  0.0345  400  VAL B CG1 
11911 C CG2 . VAL B 402  ? 0.2650 0.4680 0.2961 -0.1095 0.0079  0.0328  400  VAL B CG2 
11912 N N   . SER B 403  ? 0.2456 0.3971 0.2533 -0.1097 0.0030  0.0310  401  SER B N   
11913 C CA  . SER B 403  ? 0.2859 0.4208 0.2863 -0.1115 0.0003  0.0309  401  SER B CA  
11914 C C   . SER B 403  ? 0.2143 0.3462 0.2096 -0.1143 0.0014  0.0333  401  SER B C   
11915 O O   . SER B 403  ? 0.2502 0.3732 0.2401 -0.1200 -0.0008 0.0353  401  SER B O   
11916 C CB  . SER B 403  ? 0.2331 0.3584 0.2324 -0.1043 -0.0004 0.0273  401  SER B CB  
11917 O OG  . SER B 403  ? 0.2551 0.3650 0.2475 -0.1054 -0.0027 0.0272  401  SER B OG  
11918 N N   . TYR B 404  ? 0.2463 0.3855 0.2427 -0.1105 0.0048  0.0332  402  TYR B N   
11919 C CA  . TYR B 404  ? 0.2709 0.4083 0.2623 -0.1128 0.0062  0.0356  402  TYR B CA  
11920 C C   . TYR B 404  ? 0.2447 0.3883 0.2357 -0.1213 0.0062  0.0396  402  TYR B C   
11921 O O   . TYR B 404  ? 0.2685 0.4037 0.2534 -0.1264 0.0049  0.0420  402  TYR B O   
11922 C CB  . TYR B 404  ? 0.2708 0.4172 0.2645 -0.1070 0.0100  0.0346  402  TYR B CB  
11923 C CG  . TYR B 404  ? 0.2730 0.4156 0.2607 -0.1077 0.0114  0.0362  402  TYR B CG  
11924 C CD1 . TYR B 404  ? 0.2873 0.4371 0.2737 -0.1135 0.0130  0.0399  402  TYR B CD1 
11925 C CD2 . TYR B 404  ? 0.2634 0.3955 0.2467 -0.1027 0.0109  0.0342  402  TYR B CD2 
11926 C CE1 . TYR B 404  ? 0.3156 0.4619 0.2962 -0.1142 0.0143  0.0415  402  TYR B CE1 
11927 C CE2 . TYR B 404  ? 0.2587 0.3872 0.2363 -0.1033 0.0120  0.0357  402  TYR B CE2 
11928 C CZ  . TYR B 404  ? 0.2863 0.4219 0.2625 -0.1090 0.0137  0.0393  402  TYR B CZ  
11929 O OH  . TYR B 404  ? 0.3075 0.4394 0.2776 -0.1097 0.0148  0.0409  402  TYR B OH  
11930 N N   . ILE B 405  ? 0.2803 0.4387 0.2779 -0.1232 0.0077  0.0406  403  ILE B N   
11931 C CA  . ILE B 405  ? 0.3260 0.4921 0.3241 -0.1315 0.0079  0.0446  403  ILE B CA  
11932 C C   . ILE B 405  ? 0.2512 0.4064 0.2456 -0.1383 0.0037  0.0458  403  ILE B C   
11933 O O   . ILE B 405  ? 0.3064 0.4584 0.2964 -0.1454 0.0028  0.0491  403  ILE B O   
11934 C CB  . ILE B 405  ? 0.3322 0.5174 0.3387 -0.1312 0.0104  0.0451  403  ILE B CB  
11935 C CG1 . ILE B 405  ? 0.3364 0.5317 0.3452 -0.1251 0.0148  0.0443  403  ILE B CG1 
11936 C CG2 . ILE B 405  ? 0.2805 0.4727 0.2878 -0.1395 0.0100  0.0489  403  ILE B CG2 
11937 C CD1 . ILE B 405  ? 0.3842 0.5973 0.4016 -0.1224 0.0173  0.0439  403  ILE B CD1 
11938 N N   . ALA B 406  ? 0.2721 0.4208 0.2676 -0.1362 0.0009  0.0432  404  ALA B N   
11939 C CA  . ALA B 406  ? 0.3024 0.4394 0.2937 -0.1419 -0.0033 0.0439  404  ALA B CA  
11940 C C   . ALA B 406  ? 0.2973 0.4175 0.2797 -0.1431 -0.0051 0.0444  404  ALA B C   
11941 O O   . ALA B 406  ? 0.3229 0.4357 0.3004 -0.1501 -0.0075 0.0469  404  ALA B O   
11942 C CB  . ALA B 406  ? 0.3047 0.4378 0.2987 -0.1383 -0.0056 0.0406  404  ALA B CB  
11943 N N   . CYS B 407  ? 0.2967 0.4104 0.2769 -0.1361 -0.0041 0.0421  405  CYS B N   
11944 C CA  . CYS B 407  ? 0.3052 0.4035 0.2773 -0.1364 -0.0057 0.0424  405  CYS B CA  
11945 C C   . CYS B 407  ? 0.2704 0.3710 0.2386 -0.1410 -0.0041 0.0461  405  CYS B C   
11946 O O   . CYS B 407  ? 0.3429 0.4318 0.3040 -0.1453 -0.0063 0.0480  405  CYS B O   
11947 C CB  . CYS B 407  ? 0.2608 0.3527 0.2323 -0.1277 -0.0052 0.0389  405  CYS B CB  
11948 S SG  . CYS B 407  ? 0.3477 0.4322 0.3213 -0.1232 -0.0079 0.0349  405  CYS B SG  
11949 N N   . ALA B 408  ? 0.3036 0.4191 0.2761 -0.1400 -0.0002 0.0472  406  ALA B N   
11950 C CA  . ALA B 408  ? 0.3353 0.4553 0.3048 -0.1451 0.0017  0.0511  406  ALA B CA  
11951 C C   . ALA B 408  ? 0.3128 0.4327 0.2808 -0.1549 -0.0004 0.0547  406  ALA B C   
11952 O O   . ALA B 408  ? 0.3750 0.4883 0.3366 -0.1603 -0.0011 0.0578  406  ALA B O   
11953 C CB  . ALA B 408  ? 0.3727 0.5105 0.3482 -0.1423 0.0063  0.0514  406  ALA B CB  
11954 N N   . ALA B 409  ? 0.3280 0.4545 0.3014 -0.1574 -0.0015 0.0544  407  ALA B N   
11955 C CA  . ALA B 409  ? 0.3680 0.4928 0.3396 -0.1654 -0.0041 0.0572  407  ALA B CA  
11956 C C   . ALA B 409  ? 0.3307 0.4361 0.2939 -0.1690 -0.0083 0.0576  407  ALA B C   
11957 O O   . ALA B 409  ? 0.3747 0.4740 0.3323 -0.1742 -0.0100 0.0603  407  ALA B O   
11958 C CB  . ALA B 409  ? 0.3356 0.4691 0.3141 -0.1651 -0.0052 0.0558  407  ALA B CB  
11959 N N   . LYS B 410  ? 0.3637 0.4579 0.3253 -0.1642 -0.0103 0.0542  408  LYS B N   
11960 C CA  . LYS B 410  ? 0.3359 0.4108 0.2891 -0.1660 -0.0142 0.0541  408  LYS B CA  
11961 C C   . LYS B 410  ? 0.3914 0.4582 0.3374 -0.1665 -0.0137 0.0561  408  LYS B C   
11962 O O   . LYS B 410  ? 0.4167 0.4721 0.3556 -0.1723 -0.0163 0.0585  408  LYS B O   
11963 C CB  . LYS B 410  ? 0.3487 0.4143 0.3021 -0.1586 -0.0159 0.0495  408  LYS B CB  
11964 C CG  . LYS B 410  ? 0.3725 0.4182 0.3176 -0.1595 -0.0200 0.0489  408  LYS B CG  
11965 C CD  . LYS B 410  ? 0.4007 0.4387 0.3463 -0.1515 -0.0211 0.0445  408  LYS B CD  
11966 C CE  . LYS B 410  ? 0.4045 0.4483 0.3561 -0.1505 -0.0219 0.0422  408  LYS B CE  
11967 N NZ  . LYS B 410  ? 0.4367 0.4713 0.3844 -0.1564 -0.0259 0.0427  408  LYS B NZ  
11968 N N   . LEU B 411  ? 0.3784 0.4503 0.3258 -0.1603 -0.0104 0.0551  409  LEU B N   
11969 C CA  . LEU B 411  ? 0.3960 0.4609 0.3365 -0.1605 -0.0098 0.0569  409  LEU B CA  
11970 C C   . LEU B 411  ? 0.3731 0.4441 0.3115 -0.1689 -0.0086 0.0618  409  LEU B C   
11971 O O   . LEU B 411  ? 0.3957 0.4557 0.3262 -0.1730 -0.0103 0.0644  409  LEU B O   
11972 C CB  . LEU B 411  ? 0.3430 0.4131 0.2857 -0.1523 -0.0065 0.0547  409  LEU B CB  
11973 C CG  . LEU B 411  ? 0.3653 0.4252 0.3075 -0.1444 -0.0081 0.0504  409  LEU B CG  
11974 C CD1 . LEU B 411  ? 0.3412 0.4097 0.2877 -0.1367 -0.0047 0.0480  409  LEU B CD1 
11975 C CD2 . LEU B 411  ? 0.3692 0.4114 0.3025 -0.1446 -0.0110 0.0509  409  LEU B CD2 
11976 N N   . LEU B 412  ? 0.3684 0.4570 0.3137 -0.1713 -0.0057 0.0633  410  LEU B N   
11977 C CA  . LEU B 412  ? 0.3871 0.4819 0.3309 -0.1760 -0.0046 0.0667  410  LEU B CA  
11978 C C   . LEU B 412  ? 0.4062 0.4915 0.3454 -0.1823 -0.0088 0.0684  410  LEU B C   
11979 O O   . LEU B 412  ? 0.4579 0.5414 0.3925 -0.1867 -0.0091 0.0714  410  LEU B O   
11980 C CB  . LEU B 412  ? 0.4174 0.5325 0.3699 -0.1744 -0.0010 0.0666  410  LEU B CB  
11981 C CG  . LEU B 412  ? 0.3990 0.5245 0.3545 -0.1686 0.0037  0.0657  410  LEU B CG  
11982 C CD1 . LEU B 412  ? 0.4520 0.5963 0.4168 -0.1657 0.0066  0.0647  410  LEU B CD1 
11983 C CD2 . LEU B 412  ? 0.4395 0.5633 0.3888 -0.1701 0.0054  0.0685  410  LEU B CD2 
11984 N N   . ALA B 413  ? 0.4093 0.4882 0.3494 -0.1829 -0.0121 0.0665  411  ALA B N   
11985 C CA  . ALA B 413  ? 0.4789 0.5465 0.4136 -0.1884 -0.0164 0.0678  411  ALA B CA  
11986 C C   . ALA B 413  ? 0.4378 0.4854 0.3628 -0.1891 -0.0194 0.0681  411  ALA B C   
11987 O O   . ALA B 413  ? 0.5029 0.5392 0.4221 -0.1934 -0.0232 0.0691  411  ALA B O   
11988 C CB  . ALA B 413  ? 0.4857 0.5538 0.4246 -0.1884 -0.0188 0.0655  411  ALA B CB  
11989 N N   . ALA B 414  ? 0.4645 0.5073 0.3872 -0.1849 -0.0180 0.0672  412  ALA B N   
11990 C CA  . ALA B 414  ? 0.4002 0.4239 0.3138 -0.1848 -0.0209 0.0674  412  ALA B CA  
11991 C C   . ALA B 414  ? 0.4599 0.4821 0.3687 -0.1841 -0.0188 0.0696  412  ALA B C   
11992 O O   . ALA B 414  ? 0.4385 0.4472 0.3412 -0.1816 -0.0202 0.0690  412  ALA B O   
11993 C CB  . ALA B 414  ? 0.4515 0.4663 0.3656 -0.1793 -0.0225 0.0635  412  ALA B CB  
11994 N N   . THR B 415  ? 0.4376 0.4732 0.3488 -0.1858 -0.0155 0.0719  413  THR B N   
11995 C CA  . THR B 415  ? 0.4268 0.4620 0.3336 -0.1848 -0.0132 0.0738  413  THR B CA  
11996 C C   . THR B 415  ? 0.4277 0.4461 0.3241 -0.1881 -0.0165 0.0761  413  THR B C   
11997 O O   . THR B 415  ? 0.4760 0.4891 0.3670 -0.1865 -0.0156 0.0773  413  THR B O   
11998 C CB  . THR B 415  ? 0.4441 0.4971 0.3555 -0.1858 -0.0090 0.0757  413  THR B CB  
11999 O OG1 . THR B 415  ? 0.4835 0.5388 0.3947 -0.1919 -0.0106 0.0779  413  THR B OG1 
12000 C CG2 . THR B 415  ? 0.4408 0.5103 0.3621 -0.1815 -0.0055 0.0733  413  THR B CG2 
12001 N N   . ASP B 416  ? 0.4866 0.4962 0.3799 -0.1925 -0.0204 0.0767  414  ASP B N   
12002 C CA  . ASP B 416  ? 0.4999 0.4918 0.3830 -0.1951 -0.0240 0.0784  414  ASP B CA  
12003 C C   . ASP B 416  ? 0.4360 0.4115 0.3141 -0.1908 -0.0266 0.0763  414  ASP B C   
12004 O O   . ASP B 416  ? 0.5276 0.4885 0.3971 -0.1914 -0.0291 0.0776  414  ASP B O   
12005 C CB  . ASP B 416  ? 0.4334 0.4207 0.3145 -0.2009 -0.0275 0.0795  414  ASP B CB  
12006 C CG  . ASP B 416  ? 0.5960 0.5815 0.4810 -0.2000 -0.0298 0.0766  414  ASP B CG  
12007 O OD1 . ASP B 416  ? 0.5972 0.5917 0.4894 -0.1960 -0.0276 0.0740  414  ASP B OD1 
12008 O OD2 . ASP B 416  ? 0.6508 0.6257 0.5313 -0.2033 -0.0337 0.0767  414  ASP B OD2 
12009 N N   . VAL B 417  ? 0.4627 0.4406 0.3461 -0.1862 -0.0259 0.0731  415  VAL B N   
12010 C CA  . VAL B 417  ? 0.4447 0.4074 0.3245 -0.1814 -0.0288 0.0703  415  VAL B CA  
12011 C C   . VAL B 417  ? 0.4402 0.4074 0.3235 -0.1717 -0.0263 0.0669  415  VAL B C   
12012 O O   . VAL B 417  ? 0.4259 0.3811 0.3049 -0.1663 -0.0281 0.0651  415  VAL B O   
12013 C CB  . VAL B 417  ? 0.5063 0.4661 0.3893 -0.1816 -0.0313 0.0676  415  VAL B CB  
12014 C CG1 . VAL B 417  ? 0.4248 0.3702 0.3050 -0.1745 -0.0342 0.0637  415  VAL B CG1 
12015 C CG2 . VAL B 417  ? 0.5165 0.4719 0.3961 -0.1879 -0.0343 0.0694  415  VAL B CG2 
12016 N N   . VAL B 418  ? 0.4200 0.4044 0.3114 -0.1694 -0.0222 0.0660  416  VAL B N   
12017 C CA  . VAL B 418  ? 0.3875 0.3774 0.2826 -0.1607 -0.0195 0.0630  416  VAL B CA  
12018 C C   . VAL B 418  ? 0.4440 0.4492 0.3418 -0.1619 -0.0151 0.0652  416  VAL B C   
12019 O O   . VAL B 418  ? 0.4023 0.4166 0.3015 -0.1687 -0.0136 0.0684  416  VAL B O   
12020 C CB  . VAL B 418  ? 0.3927 0.3878 0.2957 -0.1545 -0.0192 0.0584  416  VAL B CB  
12021 C CG1 . VAL B 418  ? 0.3607 0.3402 0.2605 -0.1519 -0.0233 0.0558  416  VAL B CG1 
12022 C CG2 . VAL B 418  ? 0.3753 0.3843 0.2855 -0.1586 -0.0176 0.0589  416  VAL B CG2 
12023 N N   . PHE B 419  ? 0.3789 0.3868 0.2774 -0.1550 -0.0129 0.0633  417  PHE B N   
12024 C CA  . PHE B 419  ? 0.3714 0.3935 0.2722 -0.1548 -0.0085 0.0648  417  PHE B CA  
12025 C C   . PHE B 419  ? 0.3320 0.3671 0.2421 -0.1485 -0.0057 0.0611  417  PHE B C   
12026 O O   . PHE B 419  ? 0.3430 0.3755 0.2542 -0.1409 -0.0055 0.0577  417  PHE B O   
12027 C CB  . PHE B 419  ? 0.3960 0.4115 0.2901 -0.1518 -0.0082 0.0655  417  PHE B CB  
12028 C CG  . PHE B 419  ? 0.3638 0.3929 0.2594 -0.1509 -0.0036 0.0667  417  PHE B CG  
12029 C CD1 . PHE B 419  ? 0.4083 0.4477 0.3042 -0.1578 -0.0012 0.0707  417  PHE B CD1 
12030 C CD2 . PHE B 419  ? 0.3757 0.4074 0.2725 -0.1431 -0.0018 0.0638  417  PHE B CD2 
12031 C CE1 . PHE B 419  ? 0.4016 0.4538 0.2987 -0.1566 0.0031  0.0717  417  PHE B CE1 
12032 C CE2 . PHE B 419  ? 0.3695 0.4131 0.2672 -0.1420 0.0023  0.0647  417  PHE B CE2 
12033 C CZ  . PHE B 419  ? 0.3753 0.4293 0.2731 -0.1486 0.0049  0.0686  417  PHE B CZ  
12034 N N   . PRO B 420  ? 0.3217 0.3707 0.2385 -0.1514 -0.0036 0.0617  418  PRO B N   
12035 C CA  . PRO B 420  ? 0.3177 0.3784 0.2432 -0.1454 -0.0012 0.0582  418  PRO B CA  
12036 C C   . PRO B 420  ? 0.3092 0.3799 0.2361 -0.1407 0.0028  0.0577  418  PRO B C   
12037 O O   . PRO B 420  ? 0.3109 0.3877 0.2353 -0.1443 0.0051  0.0608  418  PRO B O   
12038 C CB  . PRO B 420  ? 0.3549 0.4272 0.2862 -0.1510 -0.0005 0.0597  418  PRO B CB  
12039 C CG  . PRO B 420  ? 0.3658 0.4284 0.2914 -0.1594 -0.0037 0.0631  418  PRO B CG  
12040 C CD  . PRO B 420  ? 0.3605 0.4139 0.2775 -0.1605 -0.0040 0.0654  418  PRO B CD  
12041 N N   . GLN B 421  ? 0.3145 0.3866 0.2451 -0.1326 0.0036  0.0536  419  GLN B N   
12042 C CA  . GLN B 421  ? 0.3037 0.3840 0.2356 -0.1272 0.0072  0.0524  419  GLN B CA  
12043 C C   . GLN B 421  ? 0.2780 0.3695 0.2186 -0.1222 0.0091  0.0492  419  GLN B C   
12044 O O   . GLN B 421  ? 0.2728 0.3591 0.2159 -0.1173 0.0074  0.0458  419  GLN B O   
12045 C CB  . GLN B 421  ? 0.2830 0.3511 0.2092 -0.1219 0.0057  0.0506  419  GLN B CB  
12046 C CG  . GLN B 421  ? 0.3015 0.3570 0.2189 -0.1265 0.0032  0.0536  419  GLN B CG  
12047 C CD  . GLN B 421  ? 0.3156 0.3573 0.2283 -0.1214 0.0006  0.0515  419  GLN B CD  
12048 O OE1 . GLN B 421  ? 0.3286 0.3633 0.2433 -0.1181 -0.0018 0.0487  419  GLN B OE1 
12049 N NE2 . GLN B 421  ? 0.3253 0.3634 0.2317 -0.1208 0.0011  0.0529  419  GLN B NE2 
12050 N N   . PHE B 422  ? 0.2962 0.4035 0.2416 -0.1235 0.0126  0.0504  420  PHE B N   
12051 C CA  . PHE B 422  ? 0.2775 0.3962 0.2314 -0.1197 0.0142  0.0478  420  PHE B CA  
12052 C C   . PHE B 422  ? 0.2949 0.4192 0.2503 -0.1119 0.0172  0.0451  420  PHE B C   
12053 O O   . PHE B 422  ? 0.2799 0.4151 0.2358 -0.1117 0.0207  0.0463  420  PHE B O   
12054 C CB  . PHE B 422  ? 0.2869 0.4194 0.2455 -0.1255 0.0160  0.0506  420  PHE B CB  
12055 C CG  . PHE B 422  ? 0.3138 0.4402 0.2707 -0.1335 0.0128  0.0532  420  PHE B CG  
12056 C CD1 . PHE B 422  ? 0.3273 0.4466 0.2862 -0.1332 0.0095  0.0512  420  PHE B CD1 
12057 C CD2 . PHE B 422  ? 0.3384 0.4658 0.2912 -0.1412 0.0131  0.0576  420  PHE B CD2 
12058 C CE1 . PHE B 422  ? 0.3634 0.4763 0.3201 -0.1403 0.0064  0.0534  420  PHE B CE1 
12059 C CE2 . PHE B 422  ? 0.3778 0.4988 0.3286 -0.1487 0.0099  0.0600  420  PHE B CE2 
12060 C CZ  . PHE B 422  ? 0.3862 0.4998 0.3389 -0.1481 0.0065  0.0577  420  PHE B CZ  
12061 N N   . ALA B 423  ? 0.2743 0.3907 0.2301 -0.1056 0.0156  0.0415  421  ALA B N   
12062 C CA  . ALA B 423  ? 0.2525 0.3723 0.2095 -0.0981 0.0178  0.0385  421  ALA B CA  
12063 C C   . ALA B 423  ? 0.2997 0.4319 0.2650 -0.0946 0.0198  0.0365  421  ALA B C   
12064 O O   . ALA B 423  ? 0.3104 0.4404 0.2798 -0.0931 0.0179  0.0345  421  ALA B O   
12065 C CB  . ALA B 423  ? 0.2650 0.3711 0.2192 -0.0933 0.0150  0.0356  421  ALA B CB  
12066 N N   . THR B 424  ? 0.3086 0.4540 0.2762 -0.0932 0.0236  0.0369  422  THR B N   
12067 C CA  . THR B 424  ? 0.2631 0.4206 0.2383 -0.0891 0.0256  0.0349  422  THR B CA  
12068 C C   . THR B 424  ? 0.2539 0.4225 0.2292 -0.0858 0.0298  0.0349  422  THR B C   
12069 O O   . THR B 424  ? 0.3072 0.4785 0.2783 -0.0891 0.0315  0.0376  422  THR B O   
12070 C CB  . THR B 424  ? 0.2826 0.4486 0.2634 -0.0943 0.0253  0.0368  422  THR B CB  
12071 O OG1 . THR B 424  ? 0.2881 0.4655 0.2761 -0.0898 0.0272  0.0347  422  THR B OG1 
12072 C CG2 . THR B 424  ? 0.2976 0.4715 0.2768 -0.1014 0.0271  0.0411  422  THR B CG2 
12073 N N   . HIS B 425  ? 0.2802 0.4543 0.2597 -0.0789 0.0313  0.0317  423  HIS B N   
12074 C CA  . HIS B 425  ? 0.2783 0.4646 0.2590 -0.0752 0.0355  0.0314  423  HIS B CA  
12075 C C   . HIS B 425  ? 0.3468 0.5489 0.3352 -0.0756 0.0376  0.0320  423  HIS B C   
12076 O O   . HIS B 425  ? 0.3194 0.5329 0.3096 -0.0721 0.0412  0.0315  423  HIS B O   
12077 C CB  . HIS B 425  ? 0.2852 0.4671 0.2647 -0.0670 0.0359  0.0274  423  HIS B CB  
12078 C CG  . HIS B 425  ? 0.2576 0.4256 0.2297 -0.0661 0.0340  0.0268  423  HIS B CG  
12079 N ND1 . HIS B 425  ? 0.3260 0.4831 0.2971 -0.0614 0.0316  0.0236  423  HIS B ND1 
12080 C CD2 . HIS B 425  ? 0.2895 0.4526 0.2546 -0.0696 0.0341  0.0291  423  HIS B CD2 
12081 C CE1 . HIS B 425  ? 0.3042 0.4509 0.2685 -0.0618 0.0302  0.0239  423  HIS B CE1 
12082 N NE2 . HIS B 425  ? 0.2924 0.4422 0.2528 -0.0666 0.0317  0.0272  423  HIS B NE2 
12083 N N   . ASN B 426  ? 0.2937 0.4966 0.2865 -0.0797 0.0355  0.0329  424  ASN B N   
12084 C CA  . ASN B 426  ? 0.2909 0.5081 0.2915 -0.0800 0.0369  0.0333  424  ASN B CA  
12085 C C   . ASN B 426  ? 0.3173 0.5452 0.3186 -0.0872 0.0387  0.0375  424  ASN B C   
12086 O O   . ASN B 426  ? 0.2908 0.5132 0.2898 -0.0944 0.0365  0.0402  424  ASN B O   
12087 C CB  . ASN B 426  ? 0.2960 0.5078 0.3004 -0.0809 0.0334  0.0321  424  ASN B CB  
12088 C CG  . ASN B 426  ? 0.2939 0.5194 0.3065 -0.0802 0.0344  0.0320  424  ASN B CG  
12089 O OD1 . ASN B 426  ? 0.3007 0.5395 0.3165 -0.0837 0.0365  0.0346  424  ASN B OD1 
12090 N ND2 . ASN B 426  ? 0.2891 0.5118 0.3053 -0.0755 0.0328  0.0290  424  ASN B ND2 
12091 N N   . ALA B 427  ? 0.3229 0.5659 0.3272 -0.0852 0.0427  0.0382  425  ALA B N   
12092 C CA  . ALA B 427  ? 0.3754 0.6286 0.3805 -0.0912 0.0445  0.0420  425  ALA B CA  
12093 C C   . ALA B 427  ? 0.2925 0.5488 0.3030 -0.0964 0.0418  0.0436  425  ALA B C   
12094 O O   . ALA B 427  ? 0.3224 0.5790 0.3315 -0.1030 0.0408  0.0468  425  ALA B O   
12095 C CB  . ALA B 427  ? 0.3885 0.6535 0.3959 -0.0855 0.0480  0.0412  425  ALA B CB  
12096 N N   . GLN B 428  ? 0.3039 0.5622 0.3201 -0.0936 0.0404  0.0414  426  GLN B N   
12097 C CA  . GLN B 428  ? 0.3125 0.5728 0.3332 -0.0985 0.0375  0.0427  426  GLN B CA  
12098 C C   . GLN B 428  ? 0.2920 0.5396 0.3081 -0.1059 0.0342  0.0445  426  GLN B C   
12099 O O   . GLN B 428  ? 0.3009 0.5480 0.3164 -0.1126 0.0323  0.0473  426  GLN B O   
12100 C CB  . GLN B 428  ? 0.3324 0.5971 0.3598 -0.0935 0.0367  0.0399  426  GLN B CB  
12101 C CG  . GLN B 428  ? 0.3478 0.6177 0.3804 -0.0974 0.0343  0.0412  426  GLN B CG  
12102 C CD  . GLN B 428  ? 0.3172 0.5764 0.3475 -0.1044 0.0304  0.0424  426  GLN B CD  
12103 O OE1 . GLN B 428  ? 0.3523 0.6012 0.3799 -0.1040 0.0290  0.0410  426  GLN B OE1 
12104 N NE2 . GLN B 428  ? 0.3680 0.6294 0.3992 -0.1106 0.0285  0.0449  426  GLN B NE2 
12105 N N   . THR B 429  ? 0.3060 0.5407 0.3180 -0.1038 0.0327  0.0426  427  THR B N   
12106 C CA  . THR B 429  ? 0.3380 0.5572 0.3444 -0.1090 0.0289  0.0436  427  THR B CA  
12107 C C   . THR B 429  ? 0.2748 0.4920 0.2754 -0.1156 0.0295  0.0474  427  THR B C   
12108 O O   . THR B 429  ? 0.2891 0.5021 0.2878 -0.1233 0.0271  0.0502  427  THR B O   
12109 C CB  . THR B 429  ? 0.2942 0.4980 0.2965 -0.1032 0.0269  0.0401  427  THR B CB  
12110 O OG1 . THR B 429  ? 0.2867 0.4933 0.2943 -0.0965 0.0269  0.0366  427  THR B OG1 
12111 C CG2 . THR B 429  ? 0.3385 0.5268 0.3361 -0.1079 0.0227  0.0407  427  THR B CG2 
12112 N N   . LEU B 430  ? 0.3335 0.5531 0.3305 -0.1128 0.0326  0.0476  428  LEU B N   
12113 C CA  . LEU B 430  ? 0.3069 0.5246 0.2978 -0.1186 0.0335  0.0513  428  LEU B CA  
12114 C C   . LEU B 430  ? 0.2867 0.5131 0.2808 -0.1238 0.0332  0.0541  428  LEU B C   
12115 O O   . LEU B 430  ? 0.3203 0.5402 0.3104 -0.1307 0.0310  0.0569  428  LEU B O   
12116 C CB  . LEU B 430  ? 0.3366 0.5573 0.3240 -0.1134 0.0371  0.0506  428  LEU B CB  
12117 C CG  . LEU B 430  ? 0.3591 0.5762 0.3388 -0.1174 0.0383  0.0537  428  LEU B CG  
12118 C CD1 . LEU B 430  ? 0.3525 0.5709 0.3292 -0.1101 0.0412  0.0515  428  LEU B CD1 
12119 C CD2 . LEU B 430  ? 0.4203 0.6451 0.4013 -0.1221 0.0388  0.0567  428  LEU B CD2 
12120 N N   . ALA B 431  ? 0.3497 0.5900 0.3507 -0.1201 0.0352  0.0531  429  ALA B N   
12121 C CA  . ALA B 431  ? 0.3580 0.6074 0.3623 -0.1243 0.0351  0.0556  429  ALA B CA  
12122 C C   . ALA B 431  ? 0.3503 0.5946 0.3558 -0.1307 0.0310  0.0568  429  ALA B C   
12123 O O   . ALA B 431  ? 0.3798 0.6235 0.3833 -0.1372 0.0296  0.0599  429  ALA B O   
12124 C CB  . ALA B 431  ? 0.3748 0.6396 0.3865 -0.1184 0.0377  0.0540  429  ALA B CB  
12125 N N   . ALA B 432  ? 0.3515 0.5911 0.3594 -0.1290 0.0288  0.0545  430  ALA B N   
12126 C CA  . ALA B 432  ? 0.3016 0.5352 0.3100 -0.1347 0.0247  0.0554  430  ALA B CA  
12127 C C   . ALA B 432  ? 0.3595 0.5788 0.3599 -0.1414 0.0221  0.0577  430  ALA B C   
12128 O O   . ALA B 432  ? 0.3762 0.5930 0.3755 -0.1478 0.0195  0.0600  430  ALA B O   
12129 C CB  . ALA B 432  ? 0.3210 0.5515 0.3331 -0.1310 0.0230  0.0522  430  ALA B CB  
12130 N N   . ILE B 433  ? 0.3524 0.5619 0.3470 -0.1399 0.0227  0.0572  431  ILE B N   
12131 C CA  . ILE B 433  ? 0.3881 0.5827 0.3745 -0.1458 0.0200  0.0594  431  ILE B CA  
12132 C C   . ILE B 433  ? 0.3570 0.5541 0.3396 -0.1500 0.0212  0.0628  431  ILE B C   
12133 O O   . ILE B 433  ? 0.3488 0.5377 0.3267 -0.1566 0.0185  0.0653  431  ILE B O   
12134 C CB  . ILE B 433  ? 0.3359 0.5192 0.3172 -0.1428 0.0201  0.0579  431  ILE B CB  
12135 C CG1 . ILE B 433  ? 0.3962 0.5734 0.3806 -0.1382 0.0176  0.0540  431  ILE B CG1 
12136 C CG2 . ILE B 433  ? 0.4138 0.5820 0.3859 -0.1482 0.0177  0.0604  431  ILE B CG2 
12137 C CD1 . ILE B 433  ? 0.4125 0.5765 0.3924 -0.1316 0.0166  0.0509  431  ILE B CD1 
12138 N N   . TYR B 434  ? 0.3810 0.5886 0.3650 -0.1461 0.0252  0.0628  432  TYR B N   
12139 C CA  . TYR B 434  ? 0.3786 0.5897 0.3592 -0.1497 0.0267  0.0659  432  TYR B CA  
12140 C C   . TYR B 434  ? 0.4033 0.6196 0.3869 -0.1558 0.0249  0.0683  432  TYR B C   
12141 O O   . TYR B 434  ? 0.4007 0.6112 0.3792 -0.1621 0.0233  0.0713  432  TYR B O   
12142 C CB  . TYR B 434  ? 0.4013 0.6248 0.3845 -0.1437 0.0314  0.0650  432  TYR B CB  
12143 C CG  . TYR B 434  ? 0.3700 0.6007 0.3517 -0.1467 0.0334  0.0680  432  TYR B CG  
12144 C CD1 . TYR B 434  ? 0.3927 0.6152 0.3663 -0.1500 0.0335  0.0703  432  TYR B CD1 
12145 C CD2 . TYR B 434  ? 0.3938 0.6398 0.3822 -0.1461 0.0352  0.0685  432  TYR B CD2 
12146 C CE1 . TYR B 434  ? 0.4126 0.6419 0.3849 -0.1527 0.0355  0.0731  432  TYR B CE1 
12147 C CE2 . TYR B 434  ? 0.4112 0.6644 0.3986 -0.1488 0.0373  0.0712  432  TYR B CE2 
12148 C CZ  . TYR B 434  ? 0.4316 0.6764 0.4109 -0.1522 0.0374  0.0735  432  TYR B CZ  
12149 O OH  . TYR B 434  ? 0.4030 0.6551 0.3813 -0.1550 0.0395  0.0763  432  TYR B OH  
12150 N N   . HIS B 435  ? 0.4167 0.6430 0.4080 -0.1541 0.0247  0.0670  433  HIS B N   
12151 C CA  . HIS B 435  ? 0.4257 0.6574 0.4198 -0.1598 0.0229  0.0692  433  HIS B CA  
12152 C C   . HIS B 435  ? 0.4245 0.6434 0.4157 -0.1653 0.0181  0.0696  433  HIS B C   
12153 O O   . HIS B 435  ? 0.4262 0.6426 0.4150 -0.1721 0.0159  0.0723  433  HIS B O   
12154 C CB  . HIS B 435  ? 0.4417 0.6895 0.4449 -0.1559 0.0247  0.0678  433  HIS B CB  
12155 C CG  . HIS B 435  ? 0.4316 0.6926 0.4372 -0.1522 0.0291  0.0683  433  HIS B CG  
12156 N ND1 . HIS B 435  ? 0.4046 0.6728 0.4099 -0.1566 0.0302  0.0714  433  HIS B ND1 
12157 C CD2 . HIS B 435  ? 0.4026 0.6707 0.4107 -0.1445 0.0326  0.0659  433  HIS B CD2 
12158 C CE1 . HIS B 435  ? 0.4791 0.7583 0.4866 -0.1517 0.0343  0.0710  433  HIS B CE1 
12159 N NE2 . HIS B 435  ? 0.4076 0.6867 0.4167 -0.1442 0.0358  0.0676  433  HIS B NE2 
12160 N N   . MET B 436  ? 0.3729 0.5832 0.3639 -0.1625 0.0163  0.0669  434  MET B N   
12161 C CA  . MET B 436  ? 0.3937 0.5904 0.3811 -0.1673 0.0117  0.0671  434  MET B CA  
12162 C C   . MET B 436  ? 0.3658 0.5490 0.3441 -0.1729 0.0099  0.0697  434  MET B C   
12163 O O   . MET B 436  ? 0.4333 0.6080 0.4083 -0.1787 0.0062  0.0711  434  MET B O   
12164 C CB  . MET B 436  ? 0.4065 0.5957 0.3944 -0.1627 0.0107  0.0637  434  MET B CB  
12165 C CG  . MET B 436  ? 0.4545 0.6280 0.4379 -0.1667 0.0060  0.0635  434  MET B CG  
12166 S SD  . MET B 436  ? 0.4532 0.6183 0.4371 -0.1609 0.0054  0.0596  434  MET B SD  
12167 C CE  . MET B 436  ? 0.4181 0.5986 0.4124 -0.1561 0.0066  0.0570  434  MET B CE  
12168 N N   . ALA B 437  ? 0.3973 0.5782 0.3712 -0.1711 0.0123  0.0704  435  ALA B N   
12169 C CA  . ALA B 437  ? 0.4230 0.5906 0.3878 -0.1759 0.0105  0.0729  435  ALA B CA  
12170 C C   . ALA B 437  ? 0.4633 0.6353 0.4268 -0.1821 0.0103  0.0765  435  ALA B C   
12171 O O   . ALA B 437  ? 0.4649 0.6250 0.4211 -0.1873 0.0078  0.0787  435  ALA B O   
12172 C CB  . ALA B 437  ? 0.4522 0.6167 0.4126 -0.1718 0.0133  0.0726  435  ALA B CB  
12173 N N   . GLY B 438  ? 0.4876 0.6762 0.4578 -0.1815 0.0128  0.0770  436  GLY B N   
12174 C CA  . GLY B 438  ? 0.4728 0.6667 0.4425 -0.1876 0.0126  0.0804  436  GLY B CA  
12175 C C   . GLY B 438  ? 0.5135 0.7103 0.4794 -0.1879 0.0157  0.0826  436  GLY B C   
12176 O O   . GLY B 438  ? 0.5443 0.7397 0.5079 -0.1831 0.0182  0.0815  436  GLY B O   
12177 N N   . LYS B 439  ? 0.5134 0.7140 0.4781 -0.1938 0.0154  0.0860  437  LYS B N   
12178 C CA  . LYS B 439  ? 0.4994 0.7050 0.4613 -0.1946 0.0186  0.0884  437  LYS B CA  
12179 C C   . LYS B 439  ? 0.5215 0.7112 0.4733 -0.1971 0.0171  0.0899  437  LYS B C   
12180 O O   . LYS B 439  ? 0.5544 0.7459 0.5030 -0.1953 0.0201  0.0909  437  LYS B O   
12181 C CB  . LYS B 439  ? 0.4488 0.6653 0.4136 -0.2001 0.0189  0.0914  437  LYS B CB  
12182 N N   . ASP B 440  ? 0.4946 0.6684 0.4410 -0.2011 0.0126  0.0903  438  ASP B N   
12183 C CA  . ASP B 440  ? 0.5469 0.7049 0.4834 -0.2039 0.0108  0.0920  438  ASP B CA  
12184 C C   . ASP B 440  ? 0.5229 0.6726 0.4561 -0.1979 0.0116  0.0896  438  ASP B C   
12185 O O   . ASP B 440  ? 0.5593 0.7027 0.4937 -0.1951 0.0097  0.0869  438  ASP B O   
12186 C CB  . ASP B 440  ? 0.5749 0.7187 0.5067 -0.2101 0.0055  0.0931  438  ASP B CB  
12187 N N   . PHE B 441  ? 0.4966 0.6463 0.4256 -0.1959 0.0143  0.0906  439  PHE B N   
12188 C CA  . PHE B 441  ? 0.4641 0.6062 0.3895 -0.1902 0.0151  0.0885  439  PHE B CA  
12189 C C   . PHE B 441  ? 0.4794 0.6119 0.3954 -0.1916 0.0152  0.0908  439  PHE B C   
12190 O O   . PHE B 441  ? 0.4505 0.5884 0.3648 -0.1947 0.0169  0.0936  439  PHE B O   
12191 C CB  . PHE B 441  ? 0.4481 0.6039 0.3798 -0.1828 0.0195  0.0858  439  PHE B CB  
12192 C CG  . PHE B 441  ? 0.4785 0.6263 0.4063 -0.1772 0.0202  0.0836  439  PHE B CG  
12193 C CD1 . PHE B 441  ? 0.3947 0.5352 0.3238 -0.1745 0.0180  0.0809  439  PHE B CD1 
12194 C CD2 . PHE B 441  ? 0.4253 0.5721 0.3477 -0.1747 0.0227  0.0844  439  PHE B CD2 
12195 C CE1 . PHE B 441  ? 0.4490 0.5818 0.3743 -0.1695 0.0184  0.0790  439  PHE B CE1 
12196 C CE2 . PHE B 441  ? 0.4425 0.5813 0.3607 -0.1697 0.0229  0.0824  439  PHE B CE2 
12197 C CZ  . PHE B 441  ? 0.4484 0.5804 0.3682 -0.1672 0.0208  0.0798  439  PHE B CZ  
12198 N N   . HIS B 442  ? 0.4954 0.6135 0.4053 -0.1892 0.0134  0.0896  440  HIS B N   
12199 C CA  . HIS B 442  ? 0.4783 0.5871 0.3794 -0.1887 0.0137  0.0912  440  HIS B CA  
12200 C C   . HIS B 442  ? 0.4499 0.5511 0.3486 -0.1826 0.0137  0.0885  440  HIS B C   
12201 O O   . HIS B 442  ? 0.4418 0.5404 0.3440 -0.1803 0.0122  0.0859  440  HIS B O   
12202 C CB  . HIS B 442  ? 0.4850 0.5784 0.3780 -0.1950 0.0094  0.0940  440  HIS B CB  
12203 C CG  . HIS B 442  ? 0.5232 0.6034 0.4150 -0.1965 0.0048  0.0927  440  HIS B CG  
12204 N ND1 . HIS B 442  ? 0.5715 0.6373 0.4583 -0.1932 0.0025  0.0910  440  HIS B ND1 
12205 C CD2 . HIS B 442  ? 0.5063 0.5856 0.4011 -0.2006 0.0019  0.0927  440  HIS B CD2 
12206 C CE1 . HIS B 442  ? 0.5002 0.5567 0.3871 -0.1951 -0.0014 0.0900  440  HIS B CE1 
12207 N NE2 . HIS B 442  ? 0.5766 0.6408 0.4681 -0.1996 -0.0019 0.0910  440  HIS B NE2 
12208 N N   . VAL B 443  ? 0.4664 0.5640 0.3589 -0.1799 0.0153  0.0890  441  VAL B N   
12209 C CA  . VAL B 443  ? 0.4781 0.5662 0.3666 -0.1746 0.0147  0.0868  441  VAL B CA  
12210 C C   . VAL B 443  ? 0.4367 0.5062 0.3197 -0.1771 0.0095  0.0871  441  VAL B C   
12211 O O   . VAL B 443  ? 0.4810 0.5406 0.3579 -0.1821 0.0067  0.0898  441  VAL B O   
12212 C CB  . VAL B 443  ? 0.4994 0.5868 0.3816 -0.1714 0.0171  0.0876  441  VAL B CB  
12213 C CG1 . VAL B 443  ? 0.4527 0.5273 0.3292 -0.1669 0.0153  0.0858  441  VAL B CG1 
12214 C CG2 . VAL B 443  ? 0.5131 0.6185 0.4011 -0.1673 0.0223  0.0864  441  VAL B CG2 
12215 N N   . GLY B 444  ? 0.4583 0.5229 0.3433 -0.1736 0.0081  0.0843  442  GLY B N   
12216 C CA  . GLY B 444  ? 0.4621 0.5097 0.3429 -0.1753 0.0033  0.0840  442  GLY B CA  
12217 C C   . GLY B 444  ? 0.4260 0.4755 0.3133 -0.1775 0.0013  0.0827  442  GLY B C   
12218 O O   . GLY B 444  ? 0.4292 0.4658 0.3143 -0.1776 -0.0023 0.0815  442  GLY B O   
12219 N N   . LYS B 445  ? 0.4254 0.4904 0.3205 -0.1793 0.0036  0.0828  443  LYS B N   
12220 C CA  . LYS B 445  ? 0.4000 0.4680 0.3016 -0.1810 0.0018  0.0813  443  LYS B CA  
12221 C C   . LYS B 445  ? 0.4078 0.4797 0.3152 -0.1753 0.0029  0.0777  443  LYS B C   
12222 O O   . LYS B 445  ? 0.4208 0.4836 0.3284 -0.1750 -0.0001 0.0760  443  LYS B O   
12223 C CB  . LYS B 445  ? 0.3856 0.4692 0.2935 -0.1843 0.0038  0.0827  443  LYS B CB  
12224 C CG  . LYS B 445  ? 0.4541 0.5401 0.3678 -0.1868 0.0015  0.0816  443  LYS B CG  
12225 C CD  . LYS B 445  ? 0.5022 0.6027 0.4212 -0.1906 0.0030  0.0834  443  LYS B CD  
12226 C CE  . LYS B 445  ? 0.5127 0.6142 0.4362 -0.1936 0.0002  0.0825  443  LYS B CE  
12227 N NZ  . LYS B 445  ? 0.5569 0.6716 0.4848 -0.1978 0.0013  0.0847  443  LYS B NZ  
12228 N N   . TYR B 446  ? 0.3907 0.4762 0.3028 -0.1706 0.0073  0.0764  444  TYR B N   
12229 C CA  . TYR B 446  ? 0.3665 0.4551 0.2843 -0.1623 0.0081  0.0718  444  TYR B CA  
12230 C C   . TYR B 446  ? 0.3927 0.4916 0.3115 -0.1569 0.0125  0.0709  444  TYR B C   
12231 O O   . TYR B 446  ? 0.3649 0.4704 0.2808 -0.1604 0.0152  0.0743  444  TYR B O   
12232 C CB  . TYR B 446  ? 0.3696 0.4682 0.2965 -0.1628 0.0083  0.0702  444  TYR B CB  
12233 C CG  . TYR B 446  ? 0.4299 0.5476 0.3632 -0.1648 0.0120  0.0717  444  TYR B CG  
12234 C CD1 . TYR B 446  ? 0.3440 0.4757 0.2830 -0.1589 0.0162  0.0698  444  TYR B CD1 
12235 C CD2 . TYR B 446  ? 0.4103 0.5311 0.3444 -0.1706 0.0108  0.0741  444  TYR B CD2 
12236 C CE1 . TYR B 446  ? 0.4502 0.5982 0.3954 -0.1587 0.0191  0.0703  444  TYR B CE1 
12237 C CE2 . TYR B 446  ? 0.4494 0.5868 0.3898 -0.1708 0.0136  0.0748  444  TYR B CE2 
12238 C CZ  . TYR B 446  ? 0.4227 0.5737 0.3688 -0.1647 0.0178  0.0728  444  TYR B CZ  
12239 O OH  . TYR B 446  ? 0.5072 0.6744 0.4594 -0.1645 0.0205  0.0734  444  TYR B OH  
12240 N N   . GLU B 447  ? 0.3635 0.4636 0.2861 -0.1483 0.0132  0.0665  445  GLU B N   
12241 C CA  . GLU B 447  ? 0.3313 0.4415 0.2555 -0.1426 0.0173  0.0651  445  GLU B CA  
12242 C C   . GLU B 447  ? 0.2979 0.4161 0.2304 -0.1357 0.0185  0.0607  445  GLU B C   
12243 O O   . GLU B 447  ? 0.3080 0.4215 0.2441 -0.1344 0.0158  0.0585  445  GLU B O   
12244 C CB  . GLU B 447  ? 0.3247 0.4236 0.2411 -0.1385 0.0165  0.0643  445  GLU B CB  
12245 C CG  . GLU B 447  ? 0.3234 0.4099 0.2398 -0.1324 0.0133  0.0603  445  GLU B CG  
12246 C CD  . GLU B 447  ? 0.3374 0.4124 0.2462 -0.1289 0.0120  0.0597  445  GLU B CD  
12247 O OE1 . GLU B 447  ? 0.3425 0.4170 0.2449 -0.1320 0.0132  0.0629  445  GLU B OE1 
12248 O OE2 . GLU B 447  ? 0.3267 0.3934 0.2359 -0.1230 0.0099  0.0562  445  GLU B OE2 
12249 N N   . PHE B 448  ? 0.3065 0.4367 0.2419 -0.1311 0.0225  0.0596  446  PHE B N   
12250 C CA  . PHE B 448  ? 0.2805 0.4156 0.2220 -0.1231 0.0235  0.0551  446  PHE B CA  
12251 C C   . PHE B 448  ? 0.2679 0.3930 0.2048 -0.1163 0.0228  0.0523  446  PHE B C   
12252 O O   . PHE B 448  ? 0.3080 0.4246 0.2373 -0.1175 0.0220  0.0538  446  PHE B O   
12253 C CB  . PHE B 448  ? 0.3381 0.4918 0.2855 -0.1215 0.0281  0.0552  446  PHE B CB  
12254 C CG  . PHE B 448  ? 0.3299 0.4948 0.2830 -0.1277 0.0288  0.0578  446  PHE B CG  
12255 C CD1 . PHE B 448  ? 0.3543 0.5230 0.3147 -0.1264 0.0276  0.0557  446  PHE B CD1 
12256 C CD2 . PHE B 448  ? 0.3545 0.5261 0.3055 -0.1349 0.0305  0.0623  446  PHE B CD2 
12257 C CE1 . PHE B 448  ? 0.3377 0.5167 0.3034 -0.1322 0.0279  0.0581  446  PHE B CE1 
12258 C CE2 . PHE B 448  ? 0.3706 0.5515 0.3273 -0.1399 0.0304  0.0642  446  PHE B CE2 
12259 C CZ  . PHE B 448  ? 0.3339 0.5189 0.2979 -0.1388 0.0292  0.0621  446  PHE B CZ  
12260 N N   . GLN B 449  ? 0.2948 0.4205 0.2363 -0.1093 0.0227  0.0481  447  GLN B N   
12261 C CA  . GLN B 449  ? 0.2487 0.3668 0.1870 -0.1025 0.0222  0.0451  447  GLN B CA  
12262 C C   . GLN B 449  ? 0.2742 0.4020 0.2184 -0.0955 0.0248  0.0416  447  GLN B C   
12263 O O   . GLN B 449  ? 0.2702 0.4071 0.2215 -0.0951 0.0257  0.0407  447  GLN B O   
12264 C CB  . GLN B 449  ? 0.2599 0.3621 0.1959 -0.1009 0.0178  0.0432  447  GLN B CB  
12265 C CG  . GLN B 449  ? 0.2965 0.3875 0.2264 -0.1073 0.0148  0.0463  447  GLN B CG  
12266 C CD  . GLN B 449  ? 0.2766 0.3519 0.2024 -0.1043 0.0111  0.0445  447  GLN B CD  
12267 O OE1 . GLN B 449  ? 0.3188 0.3920 0.2478 -0.0982 0.0104  0.0409  447  GLN B OE1 
12268 N NE2 . GLN B 449  ? 0.2903 0.3545 0.2091 -0.1086 0.0085  0.0471  447  GLN B NE2 
12269 N N   . CYS B 450  ? 0.2884 0.4140 0.2293 -0.0899 0.0259  0.0395  448  CYS B N   
12270 C CA  . CYS B 450  ? 0.2517 0.3845 0.1972 -0.0828 0.0280  0.0360  448  CYS B CA  
12271 C C   . CYS B 450  ? 0.2359 0.3586 0.1770 -0.0771 0.0266  0.0332  448  CYS B C   
12272 O O   . CYS B 450  ? 0.2787 0.3907 0.2132 -0.0786 0.0246  0.0343  448  CYS B O   
12273 C CB  . CYS B 450  ? 0.2700 0.4178 0.2167 -0.0824 0.0326  0.0371  448  CYS B CB  
12274 S SG  . CYS B 450  ? 0.3123 0.4589 0.2500 -0.0822 0.0347  0.0387  448  CYS B SG  
12275 N N   . LEU B 451  ? 0.2815 0.4080 0.2262 -0.0705 0.0278  0.0296  449  LEU B N   
12276 C CA  . LEU B 451  ? 0.2956 0.4138 0.2370 -0.0647 0.0267  0.0267  449  LEU B CA  
12277 C C   . LEU B 451  ? 0.3221 0.4454 0.2589 -0.0624 0.0297  0.0267  449  LEU B C   
12278 O O   . LEU B 451  ? 0.3269 0.4626 0.2661 -0.0618 0.0333  0.0271  449  LEU B O   
12279 C CB  . LEU B 451  ? 0.3108 0.4301 0.2582 -0.0589 0.0263  0.0228  449  LEU B CB  
12280 C CG  . LEU B 451  ? 0.3782 0.4883 0.3235 -0.0532 0.0244  0.0195  449  LEU B CG  
12281 C CD1 . LEU B 451  ? 0.3329 0.4291 0.2734 -0.0552 0.0207  0.0202  449  LEU B CD1 
12282 C CD2 . LEU B 451  ? 0.4085 0.5202 0.3604 -0.0487 0.0240  0.0163  449  LEU B CD2 
12283 N N   . HIS B 452  ? 0.2922 0.4059 0.2222 -0.0611 0.0282  0.0264  450  HIS B N   
12284 C CA  . HIS B 452  ? 0.3411 0.4579 0.2660 -0.0581 0.0306  0.0259  450  HIS B CA  
12285 C C   . HIS B 452  ? 0.3331 0.4574 0.2621 -0.0516 0.0329  0.0224  450  HIS B C   
12286 O O   . HIS B 452  ? 0.3611 0.4820 0.2943 -0.0477 0.0313  0.0194  450  HIS B O   
12287 C CB  . HIS B 452  ? 0.3186 0.4224 0.2367 -0.0564 0.0277  0.0251  450  HIS B CB  
12288 C CG  . HIS B 452  ? 0.3280 0.4334 0.2407 -0.0523 0.0297  0.0237  450  HIS B CG  
12289 N ND1 . HIS B 452  ? 0.3596 0.4680 0.2659 -0.0549 0.0318  0.0263  450  HIS B ND1 
12290 C CD2 . HIS B 452  ? 0.3677 0.4722 0.2804 -0.0459 0.0299  0.0199  450  HIS B CD2 
12291 C CE1 . HIS B 452  ? 0.3910 0.5002 0.2934 -0.0500 0.0332  0.0242  450  HIS B CE1 
12292 N NE2 . HIS B 452  ? 0.3603 0.4670 0.2664 -0.0446 0.0320  0.0202  450  HIS B NE2 
12293 N N   . GLY B 453  ? 0.3770 0.5114 0.3045 -0.0503 0.0368  0.0228  451  GLY B N   
12294 C CA  . GLY B 453  ? 0.4907 0.6316 0.4209 -0.0436 0.0391  0.0194  451  GLY B CA  
12295 C C   . GLY B 453  ? 0.5264 0.6755 0.4655 -0.0423 0.0399  0.0182  451  GLY B C   
12296 O O   . GLY B 453  ? 0.5298 0.6818 0.4716 -0.0364 0.0408  0.0150  451  GLY B O   
12297 N N   . MET B 454  ? 0.4164 0.5689 0.3598 -0.0477 0.0394  0.0208  452  MET B N   
12298 C CA  . MET B 454  ? 0.3961 0.5576 0.3478 -0.0471 0.0403  0.0202  452  MET B CA  
12299 C C   . MET B 454  ? 0.4123 0.5839 0.3663 -0.0535 0.0421  0.0242  452  MET B C   
12300 O O   . MET B 454  ? 0.4243 0.6091 0.3833 -0.0527 0.0451  0.0244  452  MET B O   
12301 C CB  . MET B 454  ? 0.3840 0.5368 0.3396 -0.0471 0.0365  0.0188  452  MET B CB  
12302 C CG  . MET B 454  ? 0.3905 0.5519 0.3543 -0.0474 0.0370  0.0186  452  MET B CG  
12303 S SD  . MET B 454  ? 0.4794 0.6530 0.4474 -0.0402 0.0406  0.0158  452  MET B SD  
12304 C CE  . MET B 454  ? 0.4818 0.6432 0.4474 -0.0333 0.0383  0.0114  452  MET B CE  
12305 N N   . GLY B 455  ? 0.3065 0.4718 0.2568 -0.0599 0.0403  0.0273  453  GLY B N   
12306 C CA  . GLY B 455  ? 0.3212 0.4940 0.2737 -0.0670 0.0412  0.0312  453  GLY B CA  
12307 C C   . GLY B 455  ? 0.3813 0.5631 0.3302 -0.0699 0.0448  0.0342  453  GLY B C   
12308 O O   . GLY B 455  ? 0.3618 0.5528 0.3135 -0.0753 0.0462  0.0374  453  GLY B O   
12309 N N   . GLU B 456  ? 0.4202 0.5996 0.3626 -0.0666 0.0463  0.0334  454  GLU B N   
12310 C CA  . GLU B 456  ? 0.4240 0.6112 0.3620 -0.0696 0.0497  0.0365  454  GLU B CA  
12311 C C   . GLU B 456  ? 0.4055 0.6107 0.3492 -0.0693 0.0540  0.0373  454  GLU B C   
12312 O O   . GLU B 456  ? 0.4212 0.6343 0.3648 -0.0754 0.0559  0.0413  454  GLU B O   
12313 C CB  . GLU B 456  ? 0.4631 0.6438 0.3926 -0.0658 0.0502  0.0352  454  GLU B CB  
12314 C CG  . GLU B 456  ? 0.4812 0.6453 0.4041 -0.0679 0.0461  0.0357  454  GLU B CG  
12315 C CD  . GLU B 456  ? 0.4650 0.6185 0.3891 -0.0624 0.0428  0.0316  454  GLU B CD  
12316 O OE1 . GLU B 456  ? 0.5002 0.6572 0.4316 -0.0597 0.0425  0.0294  454  GLU B OE1 
12317 O OE2 . GLU B 456  ? 0.4475 0.5895 0.3653 -0.0608 0.0405  0.0307  454  GLU B OE2 
12318 N N   . PRO B 457  ? 0.3914 0.6040 0.3400 -0.0625 0.0558  0.0340  455  PRO B N   
12319 C CA  . PRO B 457  ? 0.4053 0.6359 0.3598 -0.0622 0.0600  0.0350  455  PRO B CA  
12320 C C   . PRO B 457  ? 0.4095 0.6476 0.3700 -0.0694 0.0596  0.0384  455  PRO B C   
12321 O O   . PRO B 457  ? 0.4363 0.6838 0.3986 -0.0723 0.0616  0.0410  455  PRO B O   
12322 C CB  . PRO B 457  ? 0.3726 0.6058 0.3318 -0.0539 0.0604  0.0304  455  PRO B CB  
12323 C CG  . PRO B 457  ? 0.4615 0.6806 0.4145 -0.0491 0.0583  0.0273  455  PRO B CG  
12324 C CD  . PRO B 457  ? 0.4555 0.6609 0.4042 -0.0548 0.0544  0.0292  455  PRO B CD  
12325 N N   . LEU B 458  ? 0.3871 0.6176 0.3512 -0.0715 0.0557  0.0379  456  LEU B N   
12326 C CA  . LEU B 458  ? 0.3835 0.6195 0.3525 -0.0788 0.0548  0.0412  456  LEU B CA  
12327 C C   . LEU B 458  ? 0.3542 0.5864 0.3174 -0.0870 0.0544  0.0457  456  LEU B C   
12328 O O   . LEU B 458  ? 0.3665 0.6063 0.3324 -0.0913 0.0552  0.0484  456  LEU B O   
12329 C CB  . LEU B 458  ? 0.3485 0.5757 0.3216 -0.0789 0.0506  0.0395  456  LEU B CB  
12330 C CG  . LEU B 458  ? 0.3429 0.5741 0.3208 -0.0864 0.0490  0.0425  456  LEU B CG  
12331 C CD1 . LEU B 458  ? 0.3727 0.6215 0.3579 -0.0864 0.0519  0.0434  456  LEU B CD1 
12332 C CD2 . LEU B 458  ? 0.3604 0.5822 0.3416 -0.0856 0.0449  0.0403  456  LEU B CD2 
12333 N N   . TYR B 459  ? 0.3286 0.5452 0.2844 -0.0877 0.0516  0.0455  457  TYR B N   
12334 C CA  . TYR B 459  ? 0.3197 0.5304 0.2699 -0.0957 0.0504  0.0498  457  TYR B CA  
12335 C C   . TYR B 459  ? 0.3475 0.5641 0.2920 -0.0972 0.0539  0.0523  457  TYR B C   
12336 O O   . TYR B 459  ? 0.3341 0.5474 0.2752 -0.1037 0.0529  0.0559  457  TYR B O   
12337 C CB  . TYR B 459  ? 0.3687 0.5604 0.3136 -0.0963 0.0456  0.0489  457  TYR B CB  
12338 C CG  . TYR B 459  ? 0.3233 0.5106 0.2737 -0.0982 0.0422  0.0482  457  TYR B CG  
12339 C CD1 . TYR B 459  ? 0.3082 0.4958 0.2597 -0.1064 0.0407  0.0517  457  TYR B CD1 
12340 C CD2 . TYR B 459  ? 0.3236 0.5071 0.2782 -0.0920 0.0405  0.0439  457  TYR B CD2 
12341 C CE1 . TYR B 459  ? 0.3081 0.4918 0.2643 -0.1081 0.0375  0.0509  457  TYR B CE1 
12342 C CE2 . TYR B 459  ? 0.3422 0.5222 0.3017 -0.0937 0.0375  0.0433  457  TYR B CE2 
12343 C CZ  . TYR B 459  ? 0.2830 0.4630 0.2432 -0.1017 0.0360  0.0467  457  TYR B CZ  
12344 O OH  . TYR B 459  ? 0.3119 0.4881 0.2764 -0.1033 0.0329  0.0459  457  TYR B OH  
12345 N N   . GLU B 460  ? 0.3724 0.5952 0.3163 -0.0903 0.0571  0.0499  458  GLU B N   
12346 C CA  . GLU B 460  ? 0.4108 0.6399 0.3521 -0.0903 0.0599  0.0515  458  GLU B CA  
12347 C C   . GLU B 460  ? 0.4542 0.6953 0.4029 -0.0937 0.0609  0.0536  458  GLU B C   
12348 O O   . GLU B 460  ? 0.4172 0.6626 0.3638 -0.0964 0.0627  0.0562  458  GLU B O   
12349 C CB  . GLU B 460  ? 0.4155 0.6489 0.3551 -0.0817 0.0630  0.0480  458  GLU B CB  
12350 N N   . GLU B 461  ? 0.4052 0.6518 0.3624 -0.0937 0.0598  0.0527  459  GLU B N   
12351 C CA  . GLU B 461  ? 0.4246 0.6819 0.3888 -0.0973 0.0601  0.0547  459  GLU B CA  
12352 C C   . GLU B 461  ? 0.4452 0.6966 0.4094 -0.1062 0.0567  0.0581  459  GLU B C   
12353 O O   . GLU B 461  ? 0.3921 0.6515 0.3622 -0.1099 0.0563  0.0598  459  GLU B O   
12354 C CB  . GLU B 461  ? 0.4064 0.6733 0.3798 -0.0921 0.0607  0.0518  459  GLU B CB  
12355 C CG  . GLU B 461  ? 0.3750 0.6459 0.3484 -0.0828 0.0635  0.0480  459  GLU B CG  
12356 C CD  . GLU B 461  ? 0.5126 0.7910 0.4836 -0.0805 0.0671  0.0486  459  GLU B CD  
12357 O OE1 . GLU B 461  ? 0.5287 0.8128 0.5007 -0.0856 0.0678  0.0519  459  GLU B OE1 
12358 O OE2 . GLU B 461  ? 0.5642 0.8425 0.5322 -0.0734 0.0693  0.0458  459  GLU B OE2 
12359 N N   . VAL B 462  ? 0.4129 0.6503 0.3703 -0.1097 0.0541  0.0590  460  VAL B N   
12360 C CA  . VAL B 462  ? 0.3732 0.6027 0.3298 -0.1176 0.0504  0.0618  460  VAL B CA  
12361 C C   . VAL B 462  ? 0.4001 0.6201 0.3477 -0.1230 0.0495  0.0651  460  VAL B C   
12362 O O   . VAL B 462  ? 0.4092 0.6294 0.3565 -0.1296 0.0484  0.0684  460  VAL B O   
12363 C CB  . VAL B 462  ? 0.3738 0.5938 0.3310 -0.1172 0.0473  0.0599  460  VAL B CB  
12364 C CG1 . VAL B 462  ? 0.3597 0.5697 0.3148 -0.1253 0.0433  0.0626  460  VAL B CG1 
12365 C CG2 . VAL B 462  ? 0.3492 0.5786 0.3155 -0.1124 0.0479  0.0568  460  VAL B CG2 
12366 N N   . VAL B 463  ? 0.3709 0.5820 0.3107 -0.1201 0.0499  0.0643  461  VAL B N   
12367 C CA  . VAL B 463  ? 0.3528 0.5537 0.2834 -0.1246 0.0488  0.0673  461  VAL B CA  
12368 C C   . VAL B 463  ? 0.3956 0.6056 0.3251 -0.1253 0.0520  0.0693  461  VAL B C   
12369 O O   . VAL B 463  ? 0.4453 0.6659 0.3775 -0.1196 0.0556  0.0674  461  VAL B O   
12370 C CB  . VAL B 463  ? 0.3579 0.5472 0.2805 -0.1208 0.0481  0.0656  461  VAL B CB  
12371 C CG1 . VAL B 463  ? 0.3841 0.5619 0.2968 -0.1253 0.0466  0.0688  461  VAL B CG1 
12372 C CG2 . VAL B 463  ? 0.3779 0.5592 0.3020 -0.1198 0.0452  0.0635  461  VAL B CG2 
12373 N N   . GLY B 464  ? 0.4216 0.6271 0.3470 -0.1322 0.0507  0.0732  462  GLY B N   
12374 C CA  . GLY B 464  ? 0.4290 0.6418 0.3522 -0.1333 0.0537  0.0754  462  GLY B CA  
12375 C C   . GLY B 464  ? 0.4993 0.7217 0.4285 -0.1389 0.0538  0.0780  462  GLY B C   
12376 O O   . GLY B 464  ? 0.4477 0.6773 0.3851 -0.1389 0.0532  0.0770  462  GLY B O   
12377 N N   . ARG B 465  ? 0.5094 0.7317 0.4342 -0.1437 0.0545  0.0816  463  ARG B N   
12378 C CA  . ARG B 465  ? 0.5176 0.7497 0.4475 -0.1492 0.0548  0.0843  463  ARG B CA  
12379 C C   . ARG B 465  ? 0.5301 0.7798 0.4689 -0.1446 0.0583  0.0825  463  ARG B C   
12380 O O   . ARG B 465  ? 0.5697 0.8280 0.5155 -0.1478 0.0577  0.0835  463  ARG B O   
12381 C CB  . ARG B 465  ? 0.5708 0.8006 0.4939 -0.1541 0.0556  0.0882  463  ARG B CB  
12382 N N   . GLY B 466  ? 0.4946 0.7495 0.4330 -0.1369 0.0618  0.0798  464  GLY B N   
12383 C CA  . GLY B 466  ? 0.5104 0.7811 0.4567 -0.1316 0.0651  0.0778  464  GLY B CA  
12384 C C   . GLY B 466  ? 0.5347 0.8089 0.4888 -0.1279 0.0639  0.0746  464  GLY B C   
12385 O O   . GLY B 466  ? 0.4861 0.7734 0.4473 -0.1236 0.0662  0.0730  464  GLY B O   
12386 N N   . LYS B 467  ? 0.4739 0.7366 0.4268 -0.1293 0.0602  0.0737  465  LYS B N   
12387 C CA  . LYS B 467  ? 0.4361 0.7009 0.3959 -0.1261 0.0588  0.0708  465  LYS B CA  
12388 C C   . LYS B 467  ? 0.5076 0.7675 0.4699 -0.1333 0.0547  0.0727  465  LYS B C   
12389 O O   . LYS B 467  ? 0.4533 0.7180 0.4173 -0.1393 0.0542  0.0758  465  LYS B O   
12390 C CB  . LYS B 467  ? 0.4662 0.7220 0.4226 -0.1202 0.0584  0.0674  465  LYS B CB  
12391 C CG  . LYS B 467  ? 0.4982 0.7566 0.4508 -0.1133 0.0620  0.0654  465  LYS B CG  
12392 C CD  . LYS B 467  ? 0.5376 0.8108 0.4975 -0.1069 0.0652  0.0630  465  LYS B CD  
12393 C CE  . LYS B 467  ? 0.5650 0.8399 0.5203 -0.0999 0.0687  0.0609  465  LYS B CE  
12394 N NZ  . LYS B 467  ? 0.5804 0.8671 0.5424 -0.0923 0.0713  0.0577  465  LYS B NZ  
12395 N N   . LEU B 468  ? 0.4399 0.6900 0.4019 -0.1329 0.0517  0.0710  466  LEU B N   
12396 C CA  . LEU B 468  ? 0.4290 0.6730 0.3925 -0.1395 0.0476  0.0725  466  LEU B CA  
12397 C C   . LEU B 468  ? 0.3640 0.5936 0.3190 -0.1461 0.0448  0.0755  466  LEU B C   
12398 O O   . LEU B 468  ? 0.3967 0.6205 0.3518 -0.1522 0.0413  0.0771  466  LEU B O   
12399 C CB  . LEU B 468  ? 0.4473 0.6877 0.4148 -0.1363 0.0455  0.0694  466  LEU B CB  
12400 C CG  . LEU B 468  ? 0.4474 0.7012 0.4235 -0.1296 0.0478  0.0663  466  LEU B CG  
12401 C CD1 . LEU B 468  ? 0.4640 0.7139 0.4441 -0.1274 0.0454  0.0636  466  LEU B CD1 
12402 C CD2 . LEU B 468  ? 0.4351 0.7031 0.4175 -0.1318 0.0490  0.0681  466  LEU B CD2 
12403 N N   . ASP B 469  ? 0.3996 0.6229 0.3467 -0.1449 0.0461  0.0761  467  ASP B N   
12404 C CA  . ASP B 469  ? 0.4550 0.6643 0.3933 -0.1506 0.0436  0.0790  467  ASP B CA  
12405 C C   . ASP B 469  ? 0.4165 0.6111 0.3523 -0.1526 0.0392  0.0782  467  ASP B C   
12406 O O   . ASP B 469  ? 0.4083 0.5933 0.3405 -0.1591 0.0358  0.0807  467  ASP B O   
12407 C CB  . ASP B 469  ? 0.4857 0.6982 0.4235 -0.1580 0.0431  0.0829  467  ASP B CB  
12408 C CG  . ASP B 469  ? 0.5169 0.7175 0.4448 -0.1621 0.0420  0.0859  467  ASP B CG  
12409 O OD1 . ASP B 469  ? 0.5193 0.7119 0.4409 -0.1585 0.0425  0.0848  467  ASP B OD1 
12410 O OD2 . ASP B 469  ? 0.6171 0.8164 0.5434 -0.1690 0.0405  0.0893  467  ASP B OD2 
12411 N N   . ARG B 470  ? 0.4619 0.6546 0.3994 -0.1468 0.0393  0.0748  468  ARG B N   
12412 C CA  . ARG B 470  ? 0.3728 0.5522 0.3082 -0.1476 0.0356  0.0737  468  ARG B CA  
12413 C C   . ARG B 470  ? 0.3919 0.5628 0.3212 -0.1425 0.0361  0.0718  468  ARG B C   
12414 O O   . ARG B 470  ? 0.3760 0.5546 0.3069 -0.1359 0.0394  0.0694  468  ARG B O   
12415 C CB  . ARG B 470  ? 0.3879 0.5732 0.3321 -0.1457 0.0348  0.0712  468  ARG B CB  
12416 C CG  . ARG B 470  ? 0.3652 0.5577 0.3152 -0.1509 0.0336  0.0729  468  ARG B CG  
12417 C CD  . ARG B 470  ? 0.3466 0.5266 0.2910 -0.1588 0.0296  0.0759  468  ARG B CD  
12418 N NE  . ARG B 470  ? 0.4137 0.6001 0.3631 -0.1640 0.0282  0.0776  468  ARG B NE  
12419 C CZ  . ARG B 470  ? 0.4293 0.6229 0.3787 -0.1680 0.0293  0.0804  468  ARG B CZ  
12420 N NH1 . ARG B 470  ? 0.3962 0.5918 0.3413 -0.1674 0.0320  0.0820  468  ARG B NH1 
12421 N NH2 . ARG B 470  ? 0.4561 0.6548 0.4099 -0.1728 0.0276  0.0818  468  ARG B NH2 
12422 N N   . PRO B 471  ? 0.3602 0.5150 0.2820 -0.1450 0.0328  0.0728  469  PRO B N   
12423 C CA  . PRO B 471  ? 0.3822 0.5279 0.2975 -0.1401 0.0328  0.0711  469  PRO B CA  
12424 C C   . PRO B 471  ? 0.3485 0.4920 0.2696 -0.1324 0.0314  0.0658  469  PRO B C   
12425 O O   . PRO B 471  ? 0.3123 0.4573 0.2397 -0.1331 0.0298  0.0646  469  PRO B O   
12426 C CB  . PRO B 471  ? 0.3643 0.4922 0.2714 -0.1446 0.0285  0.0732  469  PRO B CB  
12427 C CG  . PRO B 471  ? 0.3960 0.5226 0.3066 -0.1510 0.0260  0.0749  469  PRO B CG  
12428 C CD  . PRO B 471  ? 0.3904 0.5337 0.3090 -0.1521 0.0286  0.0753  469  PRO B CD  
12429 N N   . CYS B 472  ? 0.3515 0.4911 0.2699 -0.1251 0.0320  0.0627  470  CYS B N   
12430 C CA  . CYS B 472  ? 0.3097 0.4456 0.2323 -0.1176 0.0306  0.0578  470  CYS B CA  
12431 C C   . CYS B 472  ? 0.2837 0.4049 0.1994 -0.1134 0.0281  0.0560  470  CYS B C   
12432 O O   . CYS B 472  ? 0.3398 0.4603 0.2493 -0.1124 0.0297  0.0569  470  CYS B O   
12433 C CB  . CYS B 472  ? 0.3439 0.4944 0.2725 -0.1116 0.0346  0.0551  470  CYS B CB  
12434 S SG  . CYS B 472  ? 0.3535 0.5001 0.2878 -0.1028 0.0329  0.0493  470  CYS B SG  
12435 N N   . ARG B 473  ? 0.3024 0.4121 0.2190 -0.1112 0.0242  0.0535  471  ARG B N   
12436 C CA  . ARG B 473  ? 0.3104 0.4069 0.2218 -0.1066 0.0217  0.0514  471  ARG B CA  
12437 C C   . ARG B 473  ? 0.2997 0.3993 0.2157 -0.0983 0.0226  0.0466  471  ARG B C   
12438 O O   . ARG B 473  ? 0.3020 0.4053 0.2252 -0.0962 0.0223  0.0443  471  ARG B O   
12439 C CB  . ARG B 473  ? 0.2959 0.3776 0.2052 -0.1088 0.0169  0.0515  471  ARG B CB  
12440 C CG  . ARG B 473  ? 0.3057 0.3738 0.2093 -0.1043 0.0141  0.0497  471  ARG B CG  
12441 C CD  . ARG B 473  ? 0.3170 0.3706 0.2177 -0.1069 0.0095  0.0504  471  ARG B CD  
12442 N NE  . ARG B 473  ? 0.3355 0.3872 0.2324 -0.1151 0.0088  0.0548  471  ARG B NE  
12443 C CZ  . ARG B 473  ? 0.3692 0.4153 0.2579 -0.1187 0.0084  0.0582  471  ARG B CZ  
12444 N NH1 . ARG B 473  ? 0.3346 0.3757 0.2179 -0.1148 0.0083  0.0575  471  ARG B NH1 
12445 N NH2 . ARG B 473  ? 0.3723 0.4179 0.2582 -0.1264 0.0081  0.0623  471  ARG B NH2 
12446 N N   . ILE B 474  ? 0.3123 0.4103 0.2241 -0.0936 0.0236  0.0452  472  ILE B N   
12447 C CA  . ILE B 474  ? 0.2885 0.3893 0.2038 -0.0859 0.0245  0.0408  472  ILE B CA  
12448 C C   . ILE B 474  ? 0.3124 0.3995 0.2265 -0.0823 0.0205  0.0382  472  ILE B C   
12449 O O   . ILE B 474  ? 0.3053 0.3818 0.2126 -0.0828 0.0182  0.0391  472  ILE B O   
12450 C CB  . ILE B 474  ? 0.2798 0.3861 0.1908 -0.0827 0.0277  0.0405  472  ILE B CB  
12451 C CG1 . ILE B 474  ? 0.2987 0.4199 0.2115 -0.0860 0.0321  0.0431  472  ILE B CG1 
12452 C CG2 . ILE B 474  ? 0.3063 0.4134 0.2200 -0.0747 0.0282  0.0359  472  ILE B CG2 
12453 C CD1 . ILE B 474  ? 0.3486 0.4751 0.2562 -0.0837 0.0353  0.0434  472  ILE B CD1 
12454 N N   . TYR B 475  ? 0.2813 0.3690 0.2021 -0.0787 0.0196  0.0351  473  TYR B N   
12455 C CA  . TYR B 475  ? 0.2843 0.3609 0.2050 -0.0744 0.0163  0.0321  473  TYR B CA  
12456 C C   . TYR B 475  ? 0.3018 0.3788 0.2204 -0.0683 0.0173  0.0294  473  TYR B C   
12457 O O   . TYR B 475  ? 0.2931 0.3791 0.2157 -0.0644 0.0200  0.0273  473  TYR B O   
12458 C CB  . TYR B 475  ? 0.2687 0.3471 0.1972 -0.0728 0.0154  0.0299  473  TYR B CB  
12459 C CG  . TYR B 475  ? 0.2875 0.3545 0.2165 -0.0695 0.0118  0.0273  473  TYR B CG  
12460 C CD1 . TYR B 475  ? 0.2951 0.3611 0.2258 -0.0630 0.0117  0.0238  473  TYR B CD1 
12461 C CD2 . TYR B 475  ? 0.2745 0.3320 0.2022 -0.0727 0.0085  0.0285  473  TYR B CD2 
12462 C CE1 . TYR B 475  ? 0.3010 0.3574 0.2325 -0.0601 0.0086  0.0216  473  TYR B CE1 
12463 C CE2 . TYR B 475  ? 0.2651 0.3129 0.1934 -0.0695 0.0054  0.0262  473  TYR B CE2 
12464 C CZ  . TYR B 475  ? 0.2796 0.3273 0.2100 -0.0633 0.0055  0.0228  473  TYR B CZ  
12465 O OH  . TYR B 475  ? 0.3182 0.3571 0.2496 -0.0601 0.0026  0.0207  473  TYR B OH  
12466 N N   . ALA B 476  ? 0.2857 0.3526 0.1979 -0.0673 0.0152  0.0295  474  ALA B N   
12467 C CA  . ALA B 476  ? 0.3363 0.4033 0.2446 -0.0627 0.0162  0.0278  474  ALA B CA  
12468 C C   . ALA B 476  ? 0.3068 0.3644 0.2152 -0.0578 0.0131  0.0246  474  ALA B C   
12469 O O   . ALA B 476  ? 0.3077 0.3546 0.2117 -0.0586 0.0099  0.0253  474  ALA B O   
12470 C CB  . ALA B 476  ? 0.3312 0.3957 0.2310 -0.0659 0.0166  0.0309  474  ALA B CB  
12471 N N   . PRO B 477  ? 0.3046 0.3657 0.2181 -0.0526 0.0137  0.0210  475  PRO B N   
12472 C CA  . PRO B 477  ? 0.3077 0.3604 0.2211 -0.0480 0.0109  0.0180  475  PRO B CA  
12473 C C   . PRO B 477  ? 0.3126 0.3611 0.2188 -0.0461 0.0105  0.0178  475  PRO B C   
12474 O O   . PRO B 477  ? 0.3158 0.3705 0.2186 -0.0457 0.0133  0.0183  475  PRO B O   
12475 C CB  . PRO B 477  ? 0.3410 0.4004 0.2610 -0.0434 0.0125  0.0147  475  PRO B CB  
12476 C CG  . PRO B 477  ? 0.3510 0.4202 0.2757 -0.0461 0.0152  0.0160  475  PRO B CG  
12477 C CD  . PRO B 477  ? 0.3272 0.3997 0.2470 -0.0509 0.0169  0.0197  475  PRO B CD  
12478 N N   . VAL B 478  ? 0.3015 0.3396 0.2052 -0.0448 0.0068  0.0171  476  VAL B N   
12479 C CA  . VAL B 478  ? 0.3185 0.3512 0.2152 -0.0431 0.0056  0.0169  476  VAL B CA  
12480 C C   . VAL B 478  ? 0.3566 0.3832 0.2554 -0.0384 0.0028  0.0136  476  VAL B C   
12481 O O   . VAL B 478  ? 0.3480 0.3687 0.2500 -0.0385 0.0000  0.0133  476  VAL B O   
12482 C CB  . VAL B 478  ? 0.3344 0.3595 0.2245 -0.0473 0.0035  0.0204  476  VAL B CB  
12483 C CG1 . VAL B 478  ? 0.3724 0.3922 0.2551 -0.0453 0.0021  0.0201  476  VAL B CG1 
12484 C CG2 . VAL B 478  ? 0.3195 0.3505 0.2078 -0.0527 0.0061  0.0240  476  VAL B CG2 
12485 N N   . GLY B 479  ? 0.3748 0.4029 0.2719 -0.0343 0.0035  0.0112  477  GLY B N   
12486 C CA  . GLY B 479  ? 0.4622 0.4843 0.3607 -0.0302 0.0006  0.0082  477  GLY B CA  
12487 C C   . GLY B 479  ? 0.4622 0.4884 0.3609 -0.0257 0.0022  0.0051  477  GLY B C   
12488 O O   . GLY B 479  ? 0.4085 0.4421 0.3058 -0.0253 0.0056  0.0050  477  GLY B O   
12489 N N   . THR B 480  ? 0.5097 0.5309 0.4103 -0.0223 -0.0004 0.0024  478  THR B N   
12490 C CA  . THR B 480  ? 0.5711 0.5933 0.4707 -0.0180 0.0000  -0.0008 478  THR B CA  
12491 C C   . THR B 480  ? 0.6205 0.6496 0.5266 -0.0157 0.0025  -0.0028 478  THR B C   
12492 O O   . THR B 480  ? 0.5980 0.6313 0.5096 -0.0174 0.0038  -0.0019 478  THR B O   
12493 C CB  . THR B 480  ? 0.5577 0.5717 0.4572 -0.0157 -0.0041 -0.0026 478  THR B CB  
12494 O OG1 . THR B 480  ? 0.6536 0.6659 0.5604 -0.0157 -0.0057 -0.0032 478  THR B OG1 
12495 C CG2 . THR B 480  ? 0.5546 0.5617 0.4477 -0.0177 -0.0068 -0.0005 478  THR B CG2 
12496 N N   . HIS B 481  ? 0.6569 0.6868 0.5621 -0.0116 0.0030  -0.0058 479  HIS B N   
12497 C CA  . HIS B 481  ? 0.6473 0.6831 0.5580 -0.0088 0.0051  -0.0080 479  HIS B CA  
12498 C C   . HIS B 481  ? 0.6965 0.7298 0.6146 -0.0084 0.0031  -0.0090 479  HIS B C   
12499 O O   . HIS B 481  ? 0.6689 0.7074 0.5928 -0.0087 0.0048  -0.0089 479  HIS B O   
12500 C CB  . HIS B 481  ? 0.6188 0.6545 0.5259 -0.0045 0.0057  -0.0110 479  HIS B CB  
12501 C CG  . HIS B 481  ? 0.6204 0.6597 0.5205 -0.0044 0.0082  -0.0103 479  HIS B CG  
12502 N ND1 . HIS B 481  ? 0.6787 0.7177 0.5740 -0.0005 0.0089  -0.0129 479  HIS B ND1 
12503 C CD2 . HIS B 481  ? 0.6095 0.6527 0.5061 -0.0076 0.0103  -0.0073 479  HIS B CD2 
12504 C CE1 . HIS B 481  ? 0.6825 0.7254 0.5718 -0.0013 0.0114  -0.0115 479  HIS B CE1 
12505 N NE2 . HIS B 481  ? 0.6938 0.7395 0.5838 -0.0056 0.0123  -0.0081 479  HIS B NE2 
12506 N N   . GLU B 482  ? 0.6488 0.6744 0.5668 -0.0076 -0.0005 -0.0099 480  GLU B N   
12507 C CA  . GLU B 482  ? 0.6220 0.6452 0.5468 -0.0070 -0.0023 -0.0110 480  GLU B CA  
12508 C C   . GLU B 482  ? 0.6372 0.6616 0.5660 -0.0104 -0.0021 -0.0087 480  GLU B C   
12509 O O   . GLU B 482  ? 0.6623 0.6889 0.5973 -0.0100 -0.0017 -0.0093 480  GLU B O   
12510 C CB  . GLU B 482  ? 0.6367 0.6518 0.5603 -0.0059 -0.0062 -0.0121 480  GLU B CB  
12511 N N   . THR B 483  ? 0.6572 0.6798 0.5821 -0.0138 -0.0025 -0.0059 481  THR B N   
12512 C CA  . THR B 483  ? 0.6445 0.6675 0.5725 -0.0172 -0.0026 -0.0037 481  THR B CA  
12513 C C   . THR B 483  ? 0.5938 0.6255 0.5246 -0.0186 0.0010  -0.0028 481  THR B C   
12514 O O   . THR B 483  ? 0.6408 0.6746 0.5771 -0.0195 0.0012  -0.0027 481  THR B O   
12515 C CB  . THR B 483  ? 0.6515 0.6695 0.5738 -0.0205 -0.0041 -0.0009 481  THR B CB  
12516 N N   . LEU B 484  ? 0.6166 0.6537 0.5436 -0.0186 0.0037  -0.0023 482  LEU B N   
12517 C CA  . LEU B 484  ? 0.5921 0.6386 0.5219 -0.0198 0.0071  -0.0014 482  LEU B CA  
12518 C C   . LEU B 484  ? 0.5735 0.6242 0.5100 -0.0168 0.0081  -0.0038 482  LEU B C   
12519 O O   . LEU B 484  ? 0.6084 0.6644 0.5497 -0.0184 0.0094  -0.0030 482  LEU B O   
12520 C CB  . LEU B 484  ? 0.5571 0.6090 0.4817 -0.0196 0.0100  -0.0008 482  LEU B CB  
12521 N N   . LEU B 485  ? 0.5774 0.6256 0.5141 -0.0126 0.0073  -0.0067 483  LEU B N   
12522 C CA  . LEU B 485  ? 0.6277 0.6795 0.5700 -0.0095 0.0082  -0.0089 483  LEU B CA  
12523 C C   . LEU B 485  ? 0.6016 0.6515 0.5500 -0.0106 0.0066  -0.0088 483  LEU B C   
12524 O O   . LEU B 485  ? 0.5763 0.6308 0.5298 -0.0093 0.0079  -0.0097 483  LEU B O   
12525 C CB  . LEU B 485  ? 0.6005 0.6485 0.5410 -0.0051 0.0072  -0.0119 483  LEU B CB  
12526 C CG  . LEU B 485  ? 0.5483 0.5998 0.4838 -0.0026 0.0094  -0.0131 483  LEU B CG  
12527 C CD1 . LEU B 485  ? 0.5793 0.6243 0.5117 0.0008  0.0073  -0.0157 483  LEU B CD1 
12528 C CD2 . LEU B 485  ? 0.5207 0.5810 0.4596 -0.0005 0.0127  -0.0138 483  LEU B CD2 
12529 N N   . ALA B 486  ? 0.5824 0.6254 0.5302 -0.0128 0.0039  -0.0077 484  ALA B N   
12530 C CA  . ALA B 486  ? 0.5208 0.5606 0.4738 -0.0132 0.0021  -0.0080 484  ALA B CA  
12531 C C   . ALA B 486  ? 0.5872 0.6322 0.5445 -0.0158 0.0035  -0.0065 484  ALA B C   
12532 O O   . ALA B 486  ? 0.6159 0.6587 0.5774 -0.0159 0.0022  -0.0069 484  ALA B O   
12533 C CB  . ALA B 486  ? 0.5640 0.5954 0.5148 -0.0146 -0.0011 -0.0072 484  ALA B CB  
12534 N N   . TYR B 487  ? 0.6287 0.6805 0.5849 -0.0178 0.0060  -0.0049 485  TYR B N   
12535 C CA  . TYR B 487  ? 0.5646 0.6217 0.5248 -0.0205 0.0072  -0.0035 485  TYR B CA  
12536 C C   . TYR B 487  ? 0.5903 0.6567 0.5498 -0.0216 0.0105  -0.0023 485  TYR B C   
12537 O O   . TYR B 487  ? 0.5355 0.6067 0.4970 -0.0251 0.0114  -0.0003 485  TYR B O   
12538 C CB  . TYR B 487  ? 0.5015 0.5533 0.4608 -0.0247 0.0052  -0.0013 485  TYR B CB  
12539 N N   . LEU B 488  ? 0.6941 0.7636 0.6509 -0.0186 0.0121  -0.0035 486  LEU B N   
12540 C CA  . LEU B 488  ? 0.6979 0.7766 0.6536 -0.0189 0.0155  -0.0026 486  LEU B CA  
12541 C C   . LEU B 488  ? 0.7167 0.8045 0.6785 -0.0189 0.0175  -0.0025 486  LEU B C   
12542 O O   . LEU B 488  ? 0.7578 0.8545 0.7196 -0.0197 0.0203  -0.0013 486  LEU B O   
12543 C CB  . LEU B 488  ? 0.6689 0.7480 0.6212 -0.0143 0.0165  -0.0048 486  LEU B CB  
12544 C CG  . LEU B 488  ? 0.6179 0.7049 0.5669 -0.0137 0.0199  -0.0043 486  LEU B CG  
12545 C CD1 . LEU B 488  ? 0.6536 0.7352 0.5962 -0.0111 0.0192  -0.0057 486  LEU B CD1 
12546 C CD2 . LEU B 488  ? 0.6490 0.7449 0.6024 -0.0103 0.0225  -0.0058 486  LEU B CD2 
12547 N N   . VAL B 489  ? 0.6939 0.7799 0.6607 -0.0180 0.0161  -0.0036 487  VAL B N   
12548 C CA  . VAL B 489  ? 0.6818 0.7758 0.6545 -0.0178 0.0176  -0.0036 487  VAL B CA  
12549 C C   . VAL B 489  ? 0.6604 0.7599 0.6342 -0.0231 0.0184  -0.0006 487  VAL B C   
12550 O O   . VAL B 489  ? 0.6248 0.7334 0.6026 -0.0234 0.0203  -0.0001 487  VAL B O   
12551 C CB  . VAL B 489  ? 0.6131 0.7020 0.5900 -0.0161 0.0154  -0.0053 487  VAL B CB  
12552 C CG1 . VAL B 489  ? 0.7115 0.8076 0.6942 -0.0158 0.0165  -0.0054 487  VAL B CG1 
12553 C CG2 . VAL B 489  ? 0.6116 0.6955 0.5872 -0.0112 0.0146  -0.0081 487  VAL B CG2 
12554 N N   . ARG B 490  ? 0.4761 0.5702 0.4461 -0.0274 0.0170  0.0016  488  ARG B N   
12555 C CA  . ARG B 490  ? 0.5290 0.6271 0.4997 -0.0329 0.0175  0.0045  488  ARG B CA  
12556 C C   . ARG B 490  ? 0.5091 0.6174 0.4786 -0.0343 0.0207  0.0062  488  ARG B C   
12557 O O   . ARG B 490  ? 0.4766 0.5933 0.4496 -0.0370 0.0221  0.0078  488  ARG B O   
12558 C CB  . ARG B 490  ? 0.5064 0.5949 0.4730 -0.0369 0.0148  0.0063  488  ARG B CB  
12559 C CG  . ARG B 490  ? 0.4589 0.5389 0.4276 -0.0360 0.0118  0.0049  488  ARG B CG  
12560 C CD  . ARG B 490  ? 0.4499 0.5201 0.4143 -0.0392 0.0091  0.0064  488  ARG B CD  
12561 N NE  . ARG B 490  ? 0.4278 0.4907 0.3945 -0.0380 0.0066  0.0050  488  ARG B NE  
12562 C CZ  . ARG B 490  ? 0.3985 0.4515 0.3622 -0.0378 0.0039  0.0048  488  ARG B CZ  
12563 N NH1 . ARG B 490  ? 0.4016 0.4502 0.3596 -0.0389 0.0033  0.0061  488  ARG B NH1 
12564 N NH2 . ARG B 490  ? 0.4175 0.4653 0.3840 -0.0364 0.0019  0.0034  488  ARG B NH2 
12565 N N   . ARG B 491  ? 0.5170 0.6249 0.4815 -0.0324 0.0219  0.0059  489  ARG B N   
12566 C CA  . ARG B 491  ? 0.4930 0.6110 0.4561 -0.0334 0.0253  0.0075  489  ARG B CA  
12567 C C   . ARG B 491  ? 0.5355 0.6648 0.5043 -0.0305 0.0279  0.0064  489  ARG B C   
12568 O O   . ARG B 491  ? 0.5251 0.6648 0.4955 -0.0329 0.0304  0.0084  489  ARG B O   
12569 C CB  . ARG B 491  ? 0.4872 0.6025 0.4437 -0.0309 0.0262  0.0068  489  ARG B CB  
12570 N N   . LEU B 492  ? 0.5692 0.6969 0.5412 -0.0255 0.0272  0.0034  490  LEU B N   
12571 C CA  . LEU B 492  ? 0.5679 0.7055 0.5447 -0.0218 0.0295  0.0020  490  LEU B CA  
12572 C C   . LEU B 492  ? 0.4927 0.6324 0.4762 -0.0225 0.0284  0.0019  490  LEU B C   
12573 O O   . LEU B 492  ? 0.6541 0.8041 0.6417 -0.0240 0.0301  0.0032  490  LEU B O   
12574 C CB  . LEU B 492  ? 0.5390 0.6739 0.5140 -0.0151 0.0299  -0.0013 490  LEU B CB  
12575 N N   . LEU B 493  ? 0.6542 0.7848 0.6388 -0.0214 0.0255  0.0003  491  LEU B N   
12576 C CA  . LEU B 493  ? 0.5638 0.6963 0.5543 -0.0216 0.0245  0.0000  491  LEU B CA  
12577 C C   . LEU B 493  ? 0.5983 0.7351 0.5909 -0.0277 0.0243  0.0029  491  LEU B C   
12578 O O   . LEU B 493  ? 0.5931 0.7362 0.5909 -0.0282 0.0245  0.0032  491  LEU B O   
12579 C CB  . LEU B 493  ? 0.5955 0.7171 0.5863 -0.0200 0.0215  -0.0018 491  LEU B CB  
12580 C CG  . LEU B 493  ? 0.5518 0.6754 0.5480 -0.0170 0.0211  -0.0035 491  LEU B CG  
12581 C CD1 . LEU B 493  ? 0.4826 0.6131 0.4801 -0.0117 0.0234  -0.0053 491  LEU B CD1 
12582 C CD2 . LEU B 493  ? 0.5958 0.7088 0.5920 -0.0156 0.0183  -0.0051 491  LEU B CD2 
12583 N N   . GLU B 494  ? 0.6031 0.7366 0.5914 -0.0324 0.0238  0.0052  492  GLU B N   
12584 C CA  . GLU B 494  ? 0.6169 0.7560 0.6064 -0.0384 0.0242  0.0083  492  GLU B CA  
12585 C C   . GLU B 494  ? 0.5312 0.6811 0.5199 -0.0389 0.0276  0.0098  492  GLU B C   
12586 O O   . GLU B 494  ? 0.6891 0.8471 0.6797 -0.0434 0.0287  0.0123  492  GLU B O   
12587 C CB  . GLU B 494  ? 0.3867 0.5159 0.3716 -0.0434 0.0218  0.0102  492  GLU B CB  
12588 N N   . ALA B 497  ? 0.6498 0.8130 0.6544 -0.0179 0.0296  0.0002  495  ALA B N   
12589 C CA  . ALA B 497  ? 0.5690 0.7362 0.5796 -0.0177 0.0288  0.0000  495  ALA B CA  
12590 C C   . ALA B 497  ? 0.4519 0.6337 0.4668 -0.0178 0.0313  0.0013  495  ALA B C   
12591 O O   . ALA B 497  ? 0.5201 0.7086 0.5340 -0.0213 0.0330  0.0035  495  ALA B O   
12592 C CB  . ALA B 497  ? 0.4745 0.6356 0.4857 -0.0230 0.0260  0.0014  495  ALA B CB  
12593 N N   . ASN B 498  ? 0.4927 0.6797 0.5125 -0.0142 0.0314  0.0000  496  ASN B N   
12594 C CA  . ASN B 498  ? 0.5102 0.7117 0.5346 -0.0135 0.0338  0.0010  496  ASN B CA  
12595 C C   . ASN B 498  ? 0.5009 0.7092 0.5277 -0.0206 0.0337  0.0043  496  ASN B C   
12596 O O   . ASN B 498  ? 0.4626 0.6830 0.4915 -0.0218 0.0361  0.0060  496  ASN B O   
12597 C CB  . ASN B 498  ? 0.5253 0.7296 0.5544 -0.0088 0.0333  -0.0008 496  ASN B CB  
12598 N N   . SER B 499  ? 0.4380 0.6387 0.4646 -0.0253 0.0308  0.0052  497  SER B N   
12599 C CA  . SER B 499  ? 0.3993 0.6048 0.4278 -0.0323 0.0302  0.0081  497  SER B CA  
12600 C C   . SER B 499  ? 0.3942 0.5985 0.4181 -0.0373 0.0310  0.0105  497  SER B C   
12601 O O   . SER B 499  ? 0.3590 0.5681 0.3841 -0.0435 0.0307  0.0133  497  SER B O   
12602 C CB  . SER B 499  ? 0.4281 0.6247 0.4572 -0.0352 0.0267  0.0080  497  SER B CB  
12603 O OG  . SER B 499  ? 0.4236 0.6062 0.4477 -0.0344 0.0250  0.0067  497  SER B OG  
12604 N N   . SER B 500  ? 0.4036 0.6014 0.4221 -0.0350 0.0317  0.0095  498  SER B N   
12605 C CA  . SER B 500  ? 0.3848 0.5799 0.3983 -0.0397 0.0322  0.0118  498  SER B CA  
12606 C C   . SER B 500  ? 0.4354 0.6438 0.4495 -0.0403 0.0358  0.0135  498  SER B C   
12607 O O   . SER B 500  ? 0.4580 0.6742 0.4740 -0.0349 0.0382  0.0120  498  SER B O   
12608 C CB  . SER B 500  ? 0.4497 0.6322 0.4569 -0.0371 0.0313  0.0101  498  SER B CB  
12609 O OG  . SER B 500  ? 0.5285 0.7129 0.5352 -0.0303 0.0331  0.0076  498  SER B OG  
12610 N N   . PHE B 501  ? 0.3542 0.5650 0.3666 -0.0470 0.0361  0.0168  499  PHE B N   
12611 C CA  . PHE B 501  ? 0.3914 0.6146 0.4039 -0.0484 0.0396  0.0189  499  PHE B CA  
12612 C C   . PHE B 501  ? 0.4884 0.7106 0.4962 -0.0430 0.0420  0.0173  499  PHE B C   
12613 O O   . PHE B 501  ? 0.5200 0.7540 0.5296 -0.0400 0.0454  0.0172  499  PHE B O   
12614 C CB  . PHE B 501  ? 0.3855 0.6077 0.3953 -0.0569 0.0390  0.0227  499  PHE B CB  
12615 C CG  . PHE B 501  ? 0.3935 0.6295 0.4039 -0.0596 0.0425  0.0255  499  PHE B CG  
12616 C CD1 . PHE B 501  ? 0.4176 0.6539 0.4226 -0.0583 0.0450  0.0259  499  PHE B CD1 
12617 C CD2 . PHE B 501  ? 0.3673 0.6160 0.3837 -0.0637 0.0433  0.0278  499  PHE B CD2 
12618 C CE1 . PHE B 501  ? 0.4393 0.6887 0.4448 -0.0608 0.0485  0.0286  499  PHE B CE1 
12619 C CE2 . PHE B 501  ? 0.3940 0.6562 0.4114 -0.0664 0.0466  0.0306  499  PHE B CE2 
12620 C CZ  . PHE B 501  ? 0.4011 0.6637 0.4131 -0.0649 0.0494  0.0310  499  PHE B CZ  
12621 N N   . VAL B 502  ? 0.5438 0.7524 0.5457 -0.0416 0.0403  0.0158  500  VAL B N   
12622 C CA  . VAL B 502  ? 0.6090 0.8156 0.6058 -0.0370 0.0422  0.0143  500  VAL B CA  
12623 C C   . VAL B 502  ? 0.6153 0.8257 0.6145 -0.0290 0.0436  0.0109  500  VAL B C   
12624 O O   . VAL B 502  ? 0.6530 0.8659 0.6488 -0.0248 0.0461  0.0097  500  VAL B O   
12625 C CB  . VAL B 502  ? 0.6064 0.7975 0.5963 -0.0378 0.0397  0.0137  500  VAL B CB  
12626 N N   . HIS B 503  ? 0.5299 0.7403 0.5343 -0.0266 0.0421  0.0093  501  HIS B N   
12627 C CA  . HIS B 503  ? 0.5603 0.7760 0.5677 -0.0193 0.0436  0.0065  501  HIS B CA  
12628 C C   . HIS B 503  ? 0.5729 0.8051 0.5864 -0.0191 0.0462  0.0078  501  HIS B C   
12629 O O   . HIS B 503  ? 0.5418 0.7817 0.5561 -0.0135 0.0489  0.0064  501  HIS B O   
12630 C CB  . HIS B 503  ? 0.5779 0.7849 0.5875 -0.0163 0.0406  0.0040  501  HIS B CB  
12631 C CG  . HIS B 503  ? 0.5841 0.7975 0.5979 -0.0098 0.0418  0.0017  501  HIS B CG  
12632 N ND1 . HIS B 503  ? 0.5681 0.7916 0.5886 -0.0100 0.0421  0.0025  501  HIS B ND1 
12633 C CD2 . HIS B 503  ? 0.6080 0.8185 0.6198 -0.0028 0.0425  -0.0013 501  HIS B CD2 
12634 C CE1 . HIS B 503  ? 0.5907 0.8175 0.6133 -0.0033 0.0430  0.0001  501  HIS B CE1 
12635 N NE2 . HIS B 503  ? 0.6075 0.8263 0.6248 0.0012  0.0433  -0.0022 501  HIS B NE2 
12636 N N   . ARG B 504  ? 0.5026 0.7403 0.5202 -0.0252 0.0454  0.0105  502  ARG B N   
12637 C CA  . ARG B 504  ? 0.4572 0.7109 0.4814 -0.0254 0.0475  0.0119  502  ARG B CA  
12638 C C   . ARG B 504  ? 0.4977 0.7632 0.5209 -0.0266 0.0513  0.0140  502  ARG B C   
12639 O O   . ARG B 504  ? 0.5076 0.7863 0.5352 -0.0235 0.0538  0.0140  502  ARG B O   
12640 C CB  . ARG B 504  ? 0.4446 0.6999 0.4733 -0.0319 0.0451  0.0142  502  ARG B CB  
12641 C CG  . ARG B 504  ? 0.4624 0.7098 0.4936 -0.0298 0.0419  0.0121  502  ARG B CG  
12642 C CD  . ARG B 504  ? 0.4245 0.6682 0.4573 -0.0370 0.0389  0.0141  502  ARG B CD  
12643 N NE  . ARG B 504  ? 0.3876 0.6448 0.4253 -0.0419 0.0399  0.0171  502  ARG B NE  
12644 C CZ  . ARG B 504  ? 0.3678 0.6365 0.4122 -0.0402 0.0404  0.0171  502  ARG B CZ  
12645 N NH1 . ARG B 504  ? 0.4119 0.6808 0.4588 -0.0333 0.0403  0.0142  502  ARG B NH1 
12646 N NH2 . ARG B 504  ? 0.3674 0.6478 0.4161 -0.0457 0.0408  0.0200  502  ARG B NH2 
12647 N N   . ILE B 505  ? 0.4476 0.7082 0.4649 -0.0309 0.0517  0.0158  503  ILE B N   
12648 C CA  . ILE B 505  ? 0.5150 0.7862 0.5305 -0.0322 0.0555  0.0178  503  ILE B CA  
12649 C C   . ILE B 505  ? 0.5198 0.7948 0.5336 -0.0239 0.0583  0.0151  503  ILE B C   
12650 O O   . ILE B 505  ? 0.4885 0.7713 0.5028 -0.0226 0.0604  0.0159  503  ILE B O   
12651 C CB  . ILE B 505  ? 0.4419 0.7049 0.4505 -0.0381 0.0549  0.0201  503  ILE B CB  
12652 N N   . ASN B 506  ? 0.4806 0.7460 0.4921 -0.0178 0.0571  0.0115  504  ASN B N   
12653 C CA  . ASN B 506  ? 0.5472 0.8143 0.5560 -0.0098 0.0595  0.0085  504  ASN B CA  
12654 C C   . ASN B 506  ? 0.5824 0.8535 0.5966 -0.0032 0.0593  0.0059  504  ASN B C   
12655 O O   . ASN B 506  ? 0.6064 0.8762 0.6183 0.0040  0.0605  0.0031  504  ASN B O   
12656 C CB  . ASN B 506  ? 0.5964 0.8480 0.5972 -0.0075 0.0580  0.0063  504  ASN B CB  
12657 C CG  . ASN B 506  ? 0.5869 0.8351 0.5815 -0.0127 0.0586  0.0087  504  ASN B CG  
12658 O OD1 . ASN B 506  ? 0.6019 0.8608 0.5959 -0.0148 0.0618  0.0109  504  ASN B OD1 
12659 N ND2 . ASN B 506  ? 0.6204 0.8538 0.6101 -0.0148 0.0555  0.0083  504  ASN B ND2 
12660 N N   . ASP B 507  ? 0.5335 0.8079 0.5544 -0.0054 0.0574  0.0068  505  ASP B N   
12661 C CA  . ASP B 507  ? 0.6028 0.8800 0.6287 0.0006  0.0567  0.0046  505  ASP B CA  
12662 C C   . ASP B 507  ? 0.6245 0.9134 0.6552 0.0006  0.0577  0.0064  505  ASP B C   
12663 O O   . ASP B 507  ? 0.6155 0.9098 0.6505 -0.0053 0.0567  0.0091  505  ASP B O   
12664 C CB  . ASP B 507  ? 0.5819 0.8552 0.6118 -0.0014 0.0539  0.0044  505  ASP B CB  
12665 C CG  . ASP B 507  ? 0.6513 0.9240 0.6845 0.0057  0.0529  0.0015  505  ASP B CG  
12666 O OD1 . ASP B 507  ? 0.6964 0.9719 0.7289 0.0120  0.0544  -0.0001 505  ASP B OD1 
12667 O OD2 . ASP B 507  ? 0.7393 1.0064 0.7751 0.0050  0.0501  0.0009  505  ASP B OD2 
12668 N N   . PRO B 508  ? 0.6604 0.9535 0.6905 0.0070  0.0596  0.0048  506  PRO B N   
12669 C CA  . PRO B 508  ? 0.6223 0.9273 0.6569 0.0070  0.0608  0.0066  506  PRO B CA  
12670 C C   . PRO B 508  ? 0.6593 0.9695 0.7011 0.0068  0.0588  0.0071  506  PRO B C   
12671 O O   . PRO B 508  ? 0.6985 1.0190 0.7447 0.0048  0.0592  0.0092  506  PRO B O   
12672 C CB  . PRO B 508  ? 0.6929 0.9990 0.7245 0.0150  0.0631  0.0041  506  PRO B CB  
12673 C CG  . PRO B 508  ? 0.6870 0.9820 0.7113 0.0174  0.0634  0.0018  506  PRO B CG  
12674 C CD  . PRO B 508  ? 0.6467 0.9336 0.6715 0.0144  0.0608  0.0014  506  PRO B CD  
12675 N N   . LYS B 509  ? 0.6734 0.9772 0.7167 0.0089  0.0566  0.0052  507  LYS B N   
12676 C CA  . LYS B 509  ? 0.6732 0.9811 0.7229 0.0082  0.0544  0.0058  507  LYS B CA  
12677 C C   . LYS B 509  ? 0.6974 1.0078 0.7500 -0.0007 0.0528  0.0090  507  LYS B C   
12678 O O   . LYS B 509  ? 0.7346 1.0498 0.7924 -0.0022 0.0510  0.0100  507  LYS B O   
12679 C CB  . LYS B 509  ? 0.6207 0.9201 0.6705 0.0127  0.0524  0.0030  507  LYS B CB  
12680 N N   . VAL B 510  ? 0.6821 0.9889 0.7310 -0.0065 0.0532  0.0106  508  VAL B N   
12681 C CA  . VAL B 510  ? 0.6506 0.9581 0.7011 -0.0153 0.0515  0.0137  508  VAL B CA  
12682 C C   . VAL B 510  ? 0.6119 0.9280 0.6625 -0.0195 0.0532  0.0166  508  VAL B C   
12683 O O   . VAL B 510  ? 0.6283 0.9431 0.6740 -0.0198 0.0554  0.0170  508  VAL B O   
12684 C CB  . VAL B 510  ? 0.5876 0.8844 0.6337 -0.0194 0.0505  0.0137  508  VAL B CB  
12685 C CG1 . VAL B 510  ? 0.5741 0.8705 0.6220 -0.0282 0.0483  0.0166  508  VAL B CG1 
12686 C CG2 . VAL B 510  ? 0.5590 0.8475 0.6045 -0.0143 0.0493  0.0105  508  VAL B CG2 
12687 N N   . SER B 511  ? 0.5815 0.9060 0.6372 -0.0228 0.0523  0.0187  509  SER B N   
12688 C CA  . SER B 511  ? 0.5729 0.9065 0.6294 -0.0267 0.0538  0.0216  509  SER B CA  
12689 C C   . SER B 511  ? 0.5728 0.9022 0.6262 -0.0356 0.0531  0.0245  509  SER B C   
12690 O O   . SER B 511  ? 0.5526 0.8733 0.6045 -0.0393 0.0509  0.0245  509  SER B O   
12691 C CB  . SER B 511  ? 0.6008 0.9448 0.6639 -0.0275 0.0528  0.0229  509  SER B CB  
12692 O OG  . SER B 511  ? 0.5887 0.9308 0.6540 -0.0347 0.0499  0.0248  509  SER B OG  
12693 N N   . ILE B 512  ? 0.4901 0.8259 0.5425 -0.0391 0.0548  0.0270  510  ILE B N   
12694 C CA  . ILE B 512  ? 0.5040 0.8364 0.5536 -0.0479 0.0540  0.0301  510  ILE B CA  
12695 C C   . ILE B 512  ? 0.5623 0.8962 0.6162 -0.0542 0.0508  0.0321  510  ILE B C   
12696 O O   . ILE B 512  ? 0.5137 0.8407 0.5652 -0.0612 0.0489  0.0338  510  ILE B O   
12697 C CB  . ILE B 512  ? 0.4079 0.7468 0.4552 -0.0500 0.0567  0.0324  510  ILE B CB  
12698 N N   . ASP B 513  ? 0.5223 0.8645 0.5822 -0.0518 0.0501  0.0317  511  ASP B N   
12699 C CA  . ASP B 513  ? 0.5156 0.8589 0.5795 -0.0573 0.0469  0.0333  511  ASP B CA  
12700 C C   . ASP B 513  ? 0.4629 0.7948 0.5256 -0.0583 0.0442  0.0318  511  ASP B C   
12701 O O   . ASP B 513  ? 0.4709 0.7978 0.5328 -0.0653 0.0416  0.0335  511  ASP B O   
12702 C CB  . ASP B 513  ? 0.5491 0.9033 0.6194 -0.0535 0.0468  0.0328  511  ASP B CB  
12703 C CG  . ASP B 513  ? 0.5727 0.9389 0.6452 -0.0557 0.0485  0.0354  511  ASP B CG  
12704 O OD1 . ASP B 513  ? 0.5570 0.9235 0.6278 -0.0632 0.0482  0.0384  511  ASP B OD1 
12705 O OD2 . ASP B 513  ? 0.6790 1.0546 0.7550 -0.0500 0.0502  0.0345  511  ASP B OD2 
12706 N N   . GLU B 514  ? 0.4350 0.7626 0.4973 -0.0512 0.0446  0.0285  512  GLU B N   
12707 C CA  . GLU B 514  ? 0.4882 0.8051 0.5493 -0.0517 0.0422  0.0270  512  GLU B CA  
12708 C C   . GLU B 514  ? 0.4628 0.7699 0.5180 -0.0572 0.0419  0.0281  512  GLU B C   
12709 O O   . GLU B 514  ? 0.4560 0.7560 0.5105 -0.0625 0.0392  0.0289  512  GLU B O   
12710 C CB  . GLU B 514  ? 0.4467 0.7607 0.5079 -0.0429 0.0431  0.0233  512  GLU B CB  
12711 C CG  . GLU B 514  ? 0.5891 0.9120 0.6552 -0.0366 0.0436  0.0221  512  GLU B CG  
12712 C CD  . GLU B 514  ? 0.6282 0.9470 0.6935 -0.0279 0.0444  0.0185  512  GLU B CD  
12713 O OE1 . GLU B 514  ? 0.6893 0.9990 0.7532 -0.0274 0.0429  0.0169  512  GLU B OE1 
12714 O OE2 . GLU B 514  ? 0.6433 0.9679 0.7094 -0.0217 0.0464  0.0173  512  GLU B OE2 
12715 N N   . LEU B 515  ? 0.4490 0.7554 0.4997 -0.0561 0.0446  0.0284  513  LEU B N   
12716 C CA  . LEU B 515  ? 0.3898 0.6867 0.4343 -0.0610 0.0443  0.0295  513  LEU B CA  
12717 C C   . LEU B 515  ? 0.4260 0.7222 0.4697 -0.0703 0.0425  0.0331  513  LEU B C   
12718 O O   . LEU B 515  ? 0.4122 0.6987 0.4518 -0.0754 0.0410  0.0341  513  LEU B O   
12719 C CB  . LEU B 515  ? 0.4075 0.7045 0.4471 -0.0576 0.0476  0.0291  513  LEU B CB  
12720 C CG  . LEU B 515  ? 0.4282 0.7230 0.4665 -0.0488 0.0493  0.0254  513  LEU B CG  
12721 C CD1 . LEU B 515  ? 0.4719 0.7680 0.5052 -0.0461 0.0525  0.0254  513  LEU B CD1 
12722 C CD2 . LEU B 515  ? 0.4345 0.7179 0.4703 -0.0484 0.0477  0.0236  513  LEU B CD2 
12723 N N   . ILE B 516  ? 0.3744 0.6805 0.4219 -0.0726 0.0426  0.0351  514  ILE B N   
12724 C CA  . ILE B 516  ? 0.3562 0.6620 0.4029 -0.0815 0.0409  0.0386  514  ILE B CA  
12725 C C   . ILE B 516  ? 0.3481 0.6517 0.3982 -0.0854 0.0372  0.0389  514  ILE B C   
12726 O O   . ILE B 516  ? 0.3884 0.6905 0.4376 -0.0929 0.0352  0.0416  514  ILE B O   
12727 C CB  . ILE B 516  ? 0.4269 0.7443 0.4754 -0.0829 0.0429  0.0409  514  ILE B CB  
12728 N N   . ALA B 517  ? 0.4105 0.7136 0.4641 -0.0805 0.0361  0.0362  515  ALA B N   
12729 C CA  . ALA B 517  ? 0.3971 0.6981 0.4537 -0.0837 0.0326  0.0363  515  ALA B CA  
12730 C C   . ALA B 517  ? 0.3626 0.6516 0.4146 -0.0909 0.0299  0.0376  515  ALA B C   
12731 O O   . ALA B 517  ? 0.3705 0.6502 0.4179 -0.0907 0.0302  0.0369  515  ALA B O   
12732 C CB  . ALA B 517  ? 0.3736 0.6736 0.4334 -0.0768 0.0321  0.0330  515  ALA B CB  
12733 N N   . ASP B 518  ? 0.3979 0.6870 0.4509 -0.0974 0.0271  0.0397  516  ASP B N   
12734 C CA  . ASP B 518  ? 0.3738 0.6512 0.4223 -0.1046 0.0241  0.0411  516  ASP B CA  
12735 C C   . ASP B 518  ? 0.3258 0.5948 0.3748 -0.1030 0.0216  0.0386  516  ASP B C   
12736 O O   . ASP B 518  ? 0.3212 0.5936 0.3745 -0.1019 0.0199  0.0377  516  ASP B O   
12737 C CB  . ASP B 518  ? 0.3393 0.6198 0.3885 -0.1118 0.0220  0.0440  516  ASP B CB  
12738 C CG  . ASP B 518  ? 0.3921 0.6599 0.4356 -0.1196 0.0189  0.0456  516  ASP B CG  
12739 O OD1 . ASP B 518  ? 0.3648 0.6211 0.4043 -0.1193 0.0181  0.0444  516  ASP B OD1 
12740 O OD2 . ASP B 518  ? 0.4154 0.6843 0.4583 -0.1259 0.0172  0.0482  516  ASP B OD2 
12741 N N   . PRO B 519  ? 0.2860 0.5440 0.3306 -0.1028 0.0214  0.0375  517  PRO B N   
12742 C CA  . PRO B 519  ? 0.3435 0.5935 0.3886 -0.1014 0.0190  0.0352  517  PRO B CA  
12743 C C   . PRO B 519  ? 0.2715 0.5163 0.3164 -0.1075 0.0150  0.0362  517  PRO B C   
12744 O O   . PRO B 519  ? 0.2971 0.5405 0.3448 -0.1056 0.0130  0.0343  517  PRO B O   
12745 C CB  . PRO B 519  ? 0.3097 0.5460 0.3482 -0.1001 0.0191  0.0341  517  PRO B CB  
12746 C CG  . PRO B 519  ? 0.3200 0.5575 0.3546 -0.1052 0.0207  0.0372  517  PRO B CG  
12747 C CD  . PRO B 519  ? 0.2644 0.5168 0.3032 -0.1040 0.0232  0.0385  517  PRO B CD  
12748 N N   . VAL B 520  ? 0.2896 0.5311 0.3309 -0.1147 0.0136  0.0390  518  VAL B N   
12749 C CA  . VAL B 520  ? 0.2940 0.5292 0.3341 -0.1207 0.0096  0.0399  518  VAL B CA  
12750 C C   . VAL B 520  ? 0.2912 0.5363 0.3372 -0.1195 0.0086  0.0396  518  VAL B C   
12751 O O   . VAL B 520  ? 0.2928 0.5339 0.3400 -0.1197 0.0058  0.0382  518  VAL B O   
12752 C CB  . VAL B 520  ? 0.3311 0.5612 0.3658 -0.1283 0.0085  0.0431  518  VAL B CB  
12753 C CG1 . VAL B 520  ? 0.3641 0.5850 0.3962 -0.1344 0.0041  0.0437  518  VAL B CG1 
12754 C CG2 . VAL B 520  ? 0.3274 0.5490 0.3563 -0.1289 0.0099  0.0436  518  VAL B CG2 
12755 N N   . GLU B 521  ? 0.3199 0.5779 0.3696 -0.1180 0.0110  0.0408  519  GLU B N   
12756 C CA  . GLU B 521  ? 0.3306 0.5984 0.3859 -0.1171 0.0101  0.0408  519  GLU B CA  
12757 C C   . GLU B 521  ? 0.3162 0.5876 0.3760 -0.1094 0.0107  0.0377  519  GLU B C   
12758 O O   . GLU B 521  ? 0.3374 0.6115 0.4006 -0.1090 0.0086  0.0371  519  GLU B O   
12759 C CB  . GLU B 521  ? 0.3554 0.6360 0.4133 -0.1178 0.0124  0.0431  519  GLU B CB  
12760 C CG  . GLU B 521  ? 0.3548 0.6322 0.4084 -0.1259 0.0114  0.0464  519  GLU B CG  
12761 C CD  . GLU B 521  ? 0.4073 0.6764 0.4586 -0.1326 0.0071  0.0473  519  GLU B CD  
12762 O OE1 . GLU B 521  ? 0.3997 0.6712 0.4545 -0.1317 0.0051  0.0462  519  GLU B OE1 
12763 O OE2 . GLU B 521  ? 0.4986 0.7585 0.5442 -0.1387 0.0056  0.0491  519  GLU B OE2 
12764 N N   . VAL B 522  ? 0.3154 0.5866 0.3752 -0.1033 0.0134  0.0358  520  VAL B N   
12765 C CA  . VAL B 522  ? 0.3148 0.5880 0.3783 -0.0961 0.0137  0.0329  520  VAL B CA  
12766 C C   . VAL B 522  ? 0.3557 0.6183 0.4178 -0.0974 0.0104  0.0313  520  VAL B C   
12767 O O   . VAL B 522  ? 0.3432 0.6079 0.4087 -0.0949 0.0088  0.0299  520  VAL B O   
12768 C CB  . VAL B 522  ? 0.3645 0.6393 0.4277 -0.0892 0.0173  0.0312  520  VAL B CB  
12769 C CG1 . VAL B 522  ? 0.3445 0.6197 0.4110 -0.0819 0.0173  0.0281  520  VAL B CG1 
12770 C CG2 . VAL B 522  ? 0.3949 0.6812 0.4599 -0.0872 0.0204  0.0325  520  VAL B CG2 
12771 N N   . VAL B 523  ? 0.2835 0.5342 0.3404 -0.1013 0.0092  0.0315  521  VAL B N   
12772 C CA  . VAL B 523  ? 0.2878 0.5277 0.3428 -0.1030 0.0059  0.0300  521  VAL B CA  
12773 C C   . VAL B 523  ? 0.3051 0.5449 0.3607 -0.1078 0.0025  0.0310  521  VAL B C   
12774 O O   . VAL B 523  ? 0.2879 0.5254 0.3451 -0.1063 0.0003  0.0293  521  VAL B O   
12775 C CB  . VAL B 523  ? 0.3200 0.5448 0.3678 -0.1055 0.0050  0.0299  521  VAL B CB  
12776 C CG1 . VAL B 523  ? 0.3355 0.5468 0.3797 -0.1074 0.0010  0.0285  521  VAL B CG1 
12777 C CG2 . VAL B 523  ? 0.3313 0.5510 0.3768 -0.0979 0.0074  0.0276  521  VAL B CG2 
12778 N N   . ARG B 524  ? 0.3202 0.5621 0.3743 -0.1137 0.0019  0.0338  522  ARG B N   
12779 C CA  . ARG B 524  ? 0.3501 0.5912 0.4043 -0.1188 -0.0014 0.0349  522  ARG B CA  
12780 C C   . ARG B 524  ? 0.3536 0.6048 0.4138 -0.1148 -0.0017 0.0339  522  ARG B C   
12781 O O   . ARG B 524  ? 0.3594 0.6078 0.4198 -0.1170 -0.0048 0.0335  522  ARG B O   
12782 C CB  . ARG B 524  ? 0.3669 0.6106 0.4191 -0.1252 -0.0014 0.0382  522  ARG B CB  
12783 C CG  . ARG B 524  ? 0.3539 0.5960 0.4054 -0.1311 -0.0050 0.0395  522  ARG B CG  
12784 C CD  . ARG B 524  ? 0.3942 0.6440 0.4461 -0.1360 -0.0044 0.0428  522  ARG B CD  
12785 N NE  . ARG B 524  ? 0.4007 0.6470 0.4483 -0.1384 -0.0025 0.0445  522  ARG B NE  
12786 C CZ  . ARG B 524  ? 0.4298 0.6634 0.4708 -0.1438 -0.0045 0.0455  522  ARG B CZ  
12787 N NH1 . ARG B 524  ? 0.4181 0.6405 0.4556 -0.1474 -0.0084 0.0449  522  ARG B NH1 
12788 N NH2 . ARG B 524  ? 0.4314 0.6629 0.4688 -0.1456 -0.0026 0.0472  522  ARG B NH2 
12789 N N   . ALA B 525  ? 0.3292 0.5915 0.3940 -0.1088 0.0015  0.0334  523  ALA B N   
12790 C CA  . ALA B 525  ? 0.3981 0.6708 0.4686 -0.1049 0.0015  0.0327  523  ALA B CA  
12791 C C   . ALA B 525  ? 0.3984 0.6693 0.4711 -0.0983 0.0012  0.0297  523  ALA B C   
12792 O O   . ALA B 525  ? 0.3928 0.6712 0.4699 -0.0947 0.0009  0.0290  523  ALA B O   
12793 C CB  . ALA B 525  ? 0.3572 0.6433 0.4315 -0.1018 0.0049  0.0339  523  ALA B CB  
12794 N N   . MET B 526  ? 0.3622 0.6232 0.4317 -0.0966 0.0012  0.0279  524  MET B N   
12795 C CA  A MET B 526  ? 0.3941 0.6529 0.4655 -0.0906 0.0009  0.0251  524  MET B CA  
12796 C CA  B MET B 526  ? 0.3941 0.6530 0.4655 -0.0906 0.0009  0.0251  524  MET B CA  
12797 C C   . MET B 526  ? 0.3674 0.6221 0.4388 -0.0930 -0.0030 0.0244  524  MET B C   
12798 O O   . MET B 526  ? 0.3544 0.6026 0.4223 -0.0996 -0.0056 0.0256  524  MET B O   
12799 C CB  A MET B 526  ? 0.3850 0.6340 0.4529 -0.0891 0.0016  0.0234  524  MET B CB  
12800 C CB  B MET B 526  ? 0.3849 0.6343 0.4529 -0.0889 0.0017  0.0234  524  MET B CB  
12801 C CG  A MET B 526  ? 0.4298 0.6826 0.4976 -0.0857 0.0055  0.0236  524  MET B CG  
12802 C CG  B MET B 526  ? 0.4302 0.6841 0.4987 -0.0845 0.0057  0.0233  524  MET B CG  
12803 S SD  A MET B 526  ? 0.4750 0.7399 0.5483 -0.0765 0.0084  0.0222  524  MET B SD  
12804 S SD  B MET B 526  ? 0.4444 0.6812 0.5054 -0.0826 0.0061  0.0216  524  MET B SD  
12805 C CE  A MET B 526  ? 0.4114 0.6695 0.4854 -0.0708 0.0068  0.0189  524  MET B CE  
12806 C CE  B MET B 526  ? 0.4321 0.6707 0.4949 -0.0720 0.0089  0.0187  524  MET B CE  
12807 N N   . PRO B 527  ? 0.4005 0.6583 0.4752 -0.0876 -0.0034 0.0226  525  PRO B N   
12808 C CA  . PRO B 527  ? 0.4680 0.7223 0.5426 -0.0897 -0.0071 0.0220  525  PRO B CA  
12809 C C   . PRO B 527  ? 0.4088 0.6493 0.4781 -0.0936 -0.0098 0.0210  525  PRO B C   
12810 O O   . PRO B 527  ? 0.4092 0.6450 0.4764 -0.0985 -0.0130 0.0215  525  PRO B O   
12811 C CB  . PRO B 527  ? 0.4679 0.7276 0.5466 -0.0821 -0.0065 0.0200  525  PRO B CB  
12812 C CG  . PRO B 527  ? 0.4849 0.7452 0.5641 -0.0764 -0.0032 0.0188  525  PRO B CG  
12813 C CD  . PRO B 527  ? 0.4590 0.7224 0.5371 -0.0793 -0.0008 0.0208  525  PRO B CD  
12814 N N   . VAL B 528  ? 0.4291 0.6620 0.4958 -0.0912 -0.0086 0.0195  526  VAL B N   
12815 C CA  . VAL B 528  ? 0.3539 0.5695 0.4134 -0.0932 -0.0107 0.0184  526  VAL B CA  
12816 C C   . VAL B 528  ? 0.3244 0.5342 0.3799 -0.0946 -0.0088 0.0193  526  VAL B C   
12817 O O   . VAL B 528  ? 0.3503 0.5580 0.4052 -0.0890 -0.0062 0.0181  526  VAL B O   
12818 C CB  . VAL B 528  ? 0.3583 0.5643 0.4156 -0.0865 -0.0112 0.0153  526  VAL B CB  
12819 C CG1 . VAL B 528  ? 0.3409 0.5296 0.3909 -0.0882 -0.0130 0.0141  526  VAL B CG1 
12820 C CG2 . VAL B 528  ? 0.4032 0.6144 0.4639 -0.0854 -0.0133 0.0146  526  VAL B CG2 
12821 N N   . VAL B 529  ? 0.2701 0.4768 0.3226 -0.1022 -0.0103 0.0214  527  VAL B N   
12822 C CA  . VAL B 529  ? 0.2767 0.4781 0.3251 -0.1041 -0.0087 0.0225  527  VAL B CA  
12823 C C   . VAL B 529  ? 0.2993 0.4847 0.3417 -0.0998 -0.0089 0.0201  527  VAL B C   
12824 O O   . VAL B 529  ? 0.3082 0.4820 0.3466 -0.1005 -0.0116 0.0187  527  VAL B O   
12825 C CB  . VAL B 529  ? 0.2660 0.4657 0.3116 -0.1134 -0.0107 0.0253  527  VAL B CB  
12826 C CG1 . VAL B 529  ? 0.2995 0.4908 0.3396 -0.1152 -0.0095 0.0264  527  VAL B CG1 
12827 C CG2 . VAL B 529  ? 0.2921 0.5060 0.3425 -0.1160 -0.0100 0.0277  527  VAL B CG2 
12828 N N   . GLY B 530  ? 0.2556 0.4408 0.2976 -0.0952 -0.0059 0.0196  528  GLY B N   
12829 C CA  . GLY B 530  ? 0.2734 0.4444 0.3100 -0.0916 -0.0060 0.0176  528  GLY B CA  
12830 C C   . GLY B 530  ? 0.2454 0.4123 0.2829 -0.0844 -0.0059 0.0146  528  GLY B C   
12831 O O   . GLY B 530  ? 0.2292 0.3835 0.2622 -0.0821 -0.0067 0.0129  528  GLY B O   
12832 N N   . ALA B 531  ? 0.2274 0.4048 0.2705 -0.0809 -0.0051 0.0140  529  ALA B N   
12833 C CA  . ALA B 531  ? 0.2127 0.3865 0.2566 -0.0740 -0.0049 0.0113  529  ALA B CA  
12834 C C   . ALA B 531  ? 0.2286 0.3975 0.2706 -0.0686 -0.0025 0.0100  529  ALA B C   
12835 O O   . ALA B 531  ? 0.2550 0.4295 0.2978 -0.0682 -0.0001 0.0110  529  ALA B O   
12836 C CB  . ALA B 531  ? 0.2868 0.4735 0.3370 -0.0710 -0.0043 0.0111  529  ALA B CB  
12837 N N   . LYS B 532  ? 0.2212 0.3796 0.2606 -0.0646 -0.0033 0.0077  530  LYS B N   
12838 C CA  . LYS B 532  ? 0.2517 0.4053 0.2897 -0.0591 -0.0014 0.0062  530  LYS B CA  
12839 C C   . LYS B 532  ? 0.2506 0.4153 0.2932 -0.0543 0.0013  0.0059  530  LYS B C   
12840 O O   . LYS B 532  ? 0.2302 0.4046 0.2773 -0.0535 0.0013  0.0062  530  LYS B O   
12841 C CB  . LYS B 532  ? 0.2306 0.3739 0.2666 -0.0554 -0.0027 0.0038  530  LYS B CB  
12842 C CG  . LYS B 532  ? 0.2879 0.4253 0.3225 -0.0498 -0.0012 0.0021  530  LYS B CG  
12843 C CD  . LYS B 532  ? 0.2491 0.3777 0.2822 -0.0467 -0.0026 0.0000  530  LYS B CD  
12844 C CE  . LYS B 532  ? 0.2802 0.4149 0.3172 -0.0443 -0.0029 -0.0006 530  LYS B CE  
12845 N NZ  . LYS B 532  ? 0.2782 0.4205 0.3188 -0.0390 -0.0007 -0.0012 530  LYS B NZ  
12846 N N   . HIS B 533  ? 0.2131 0.3762 0.2543 -0.0511 0.0034  0.0054  531  HIS B N   
12847 C CA  . HIS B 533  ? 0.2184 0.3896 0.2630 -0.0455 0.0059  0.0046  531  HIS B CA  
12848 C C   . HIS B 533  ? 0.2148 0.3856 0.2617 -0.0407 0.0052  0.0028  531  HIS B C   
12849 O O   . HIS B 533  ? 0.2365 0.3973 0.2811 -0.0392 0.0038  0.0013  531  HIS B O   
12850 C CB  . HIS B 533  ? 0.2312 0.3966 0.2725 -0.0424 0.0075  0.0037  531  HIS B CB  
12851 C CG  . HIS B 533  ? 0.2543 0.4285 0.2981 -0.0379 0.0103  0.0034  531  HIS B CG  
12852 N ND1 . HIS B 533  ? 0.2600 0.4378 0.3068 -0.0322 0.0110  0.0018  531  HIS B ND1 
12853 C CD2 . HIS B 533  ? 0.3355 0.5154 0.3789 -0.0381 0.0126  0.0044  531  HIS B CD2 
12854 C CE1 . HIS B 533  ? 0.3469 0.5320 0.3950 -0.0288 0.0135  0.0017  531  HIS B CE1 
12855 N NE2 . HIS B 533  ? 0.4126 0.5993 0.4587 -0.0323 0.0146  0.0032  531  HIS B NE2 
12856 N N   . ASP B 534  ? 0.2302 0.4124 0.2819 -0.0381 0.0062  0.0029  532  ASP B N   
12857 C CA  . ASP B 534  ? 0.2551 0.4379 0.3092 -0.0336 0.0056  0.0015  532  ASP B CA  
12858 C C   . ASP B 534  ? 0.2698 0.4448 0.3219 -0.0277 0.0064  -0.0007 532  ASP B C   
12859 O O   . ASP B 534  ? 0.2921 0.4636 0.3447 -0.0246 0.0054  -0.0020 532  ASP B O   
12860 C CB  . ASP B 534  ? 0.2726 0.4696 0.3321 -0.0316 0.0067  0.0022  532  ASP B CB  
12861 C CG  . ASP B 534  ? 0.4276 0.6333 0.4899 -0.0373 0.0055  0.0043  532  ASP B CG  
12862 O OD1 . ASP B 534  ? 0.5068 0.7068 0.5674 -0.0415 0.0030  0.0046  532  ASP B OD1 
12863 O OD2 . ASP B 534  ? 0.5356 0.7537 0.6017 -0.0376 0.0070  0.0056  532  ASP B OD2 
12864 N N   . ARG B 535  ? 0.2218 0.3943 0.2718 -0.0261 0.0081  -0.0011 533  ARG B N   
12865 C CA  . ARG B 535  ? 0.2351 0.4014 0.2835 -0.0204 0.0090  -0.0030 533  ARG B CA  
12866 C C   . ARG B 535  ? 0.2432 0.3969 0.2869 -0.0213 0.0082  -0.0038 533  ARG B C   
12867 O O   . ARG B 535  ? 0.2711 0.4197 0.3131 -0.0174 0.0090  -0.0052 533  ARG B O   
12868 C CB  . ARG B 535  ? 0.2881 0.4615 0.3377 -0.0166 0.0116  -0.0033 533  ARG B CB  
12869 N N   . ILE B 536  ? 0.2044 0.3531 0.2459 -0.0265 0.0066  -0.0029 534  ILE B N   
12870 C CA  . ILE B 536  ? 0.1892 0.3260 0.2264 -0.0273 0.0056  -0.0036 534  ILE B CA  
12871 C C   . ILE B 536  ? 0.1857 0.3165 0.2223 -0.0289 0.0034  -0.0040 534  ILE B C   
12872 O O   . ILE B 536  ? 0.2241 0.3572 0.2611 -0.0333 0.0020  -0.0028 534  ILE B O   
12873 C CB  . ILE B 536  ? 0.1991 0.3343 0.2334 -0.0318 0.0058  -0.0021 534  ILE B CB  
12874 C CG1 . ILE B 536  ? 0.2120 0.3534 0.2466 -0.0301 0.0082  -0.0017 534  ILE B CG1 
12875 C CG2 . ILE B 536  ? 0.2166 0.3392 0.2465 -0.0324 0.0045  -0.0028 534  ILE B CG2 
12876 C CD1 . ILE B 536  ? 0.2914 0.4326 0.3232 -0.0347 0.0086  0.0001  534  ILE B CD1 
12877 N N   . ALA B 537  ? 0.1933 0.3166 0.2288 -0.0256 0.0029  -0.0056 535  ALA B N   
12878 C CA  . ALA B 537  ? 0.2119 0.3297 0.2468 -0.0264 0.0009  -0.0062 535  ALA B CA  
12879 C C   . ALA B 537  ? 0.1804 0.2893 0.2112 -0.0302 -0.0005 -0.0059 535  ALA B C   
12880 O O   . ALA B 537  ? 0.1847 0.2881 0.2131 -0.0298 -0.0001 -0.0061 535  ALA B O   
12881 C CB  . ALA B 537  ? 0.2216 0.3349 0.2568 -0.0214 0.0011  -0.0079 535  ALA B CB  
12882 N N   . LEU B 538  ? 0.1945 0.3020 0.2245 -0.0337 -0.0023 -0.0054 536  LEU B N   
12883 C CA  . LEU B 538  ? 0.1934 0.2907 0.2192 -0.0361 -0.0039 -0.0057 536  LEU B CA  
12884 C C   . LEU B 538  ? 0.1914 0.2810 0.2162 -0.0319 -0.0038 -0.0075 536  LEU B C   
12885 O O   . LEU B 538  ? 0.2001 0.2919 0.2273 -0.0280 -0.0032 -0.0084 536  LEU B O   
12886 C CB  . LEU B 538  ? 0.2162 0.3124 0.2412 -0.0395 -0.0060 -0.0054 536  LEU B CB  
12887 C CG  . LEU B 538  ? 0.2781 0.3793 0.3031 -0.0451 -0.0069 -0.0035 536  LEU B CG  
12888 C CD1 . LEU B 538  ? 0.2916 0.3914 0.3158 -0.0478 -0.0091 -0.0036 536  LEU B CD1 
12889 C CD2 . LEU B 538  ? 0.2471 0.3428 0.2683 -0.0486 -0.0072 -0.0025 536  LEU B CD2 
12890 N N   . PRO B 539  ? 0.1825 0.2632 0.2038 -0.0325 -0.0045 -0.0078 537  PRO B N   
12891 C CA  . PRO B 539  ? 0.1845 0.2585 0.2051 -0.0286 -0.0045 -0.0094 537  PRO B CA  
12892 C C   . PRO B 539  ? 0.1790 0.2522 0.2006 -0.0270 -0.0051 -0.0104 537  PRO B C   
12893 O O   . PRO B 539  ? 0.1754 0.2484 0.1986 -0.0231 -0.0043 -0.0114 537  PRO B O   
12894 C CB  . PRO B 539  ? 0.2049 0.2701 0.2215 -0.0305 -0.0056 -0.0094 537  PRO B CB  
12895 C CG  . PRO B 539  ? 0.1783 0.2464 0.1938 -0.0341 -0.0054 -0.0077 537  PRO B CG  
12896 C CD  . PRO B 539  ? 0.2103 0.2871 0.2283 -0.0365 -0.0053 -0.0067 537  PRO B CD  
12897 N N   . ALA B 540  ? 0.1801 0.2534 0.2007 -0.0300 -0.0066 -0.0100 538  ALA B N   
12898 C CA  . ALA B 540  ? 0.1984 0.2708 0.2194 -0.0285 -0.0072 -0.0109 538  ALA B CA  
12899 C C   . ALA B 540  ? 0.2038 0.2842 0.2288 -0.0257 -0.0061 -0.0110 538  ALA B C   
12900 O O   . ALA B 540  ? 0.1988 0.2781 0.2243 -0.0232 -0.0062 -0.0118 538  ALA B O   
12901 C CB  . ALA B 540  ? 0.2172 0.2883 0.2361 -0.0326 -0.0092 -0.0106 538  ALA B CB  
12902 N N   . GLU B 541  ? 0.2168 0.3051 0.2444 -0.0259 -0.0051 -0.0100 539  GLU B N   
12903 C CA  . GLU B 541  ? 0.2036 0.3001 0.2348 -0.0235 -0.0043 -0.0099 539  GLU B CA  
12904 C C   . GLU B 541  ? 0.1888 0.2870 0.2218 -0.0192 -0.0024 -0.0104 539  GLU B C   
12905 O O   . GLU B 541  ? 0.1992 0.3047 0.2352 -0.0171 -0.0016 -0.0102 539  GLU B O   
12906 C CB  . GLU B 541  ? 0.2367 0.3419 0.2698 -0.0269 -0.0047 -0.0084 539  GLU B CB  
12907 C CG  . GLU B 541  ? 0.2575 0.3601 0.2885 -0.0312 -0.0069 -0.0081 539  GLU B CG  
12908 C CD  . GLU B 541  ? 0.3724 0.4827 0.4049 -0.0357 -0.0077 -0.0065 539  GLU B CD  
12909 O OE1 . GLU B 541  ? 0.3636 0.4825 0.3991 -0.0356 -0.0064 -0.0055 539  GLU B OE1 
12910 O OE2 . GLU B 541  ? 0.4150 0.5227 0.4454 -0.0394 -0.0097 -0.0062 539  GLU B OE2 
12911 N N   . LEU B 542  ? 0.1720 0.2633 0.2032 -0.0176 -0.0020 -0.0112 540  LEU B N   
12912 C CA  . LEU B 542  ? 0.1889 0.2812 0.2213 -0.0138 -0.0004 -0.0117 540  LEU B CA  
12913 C C   . LEU B 542  ? 0.1936 0.2885 0.2283 -0.0099 0.0000  -0.0124 540  LEU B C   
12914 O O   . LEU B 542  ? 0.2156 0.3141 0.2517 -0.0070 0.0012  -0.0126 540  LEU B O   
12915 C CB  . LEU B 542  ? 0.2132 0.2971 0.2433 -0.0128 -0.0004 -0.0126 540  LEU B CB  
12916 C CG  . LEU B 542  ? 0.2192 0.3000 0.2470 -0.0151 -0.0005 -0.0121 540  LEU B CG  
12917 C CD1 . LEU B 542  ? 0.2044 0.2784 0.2310 -0.0128 -0.0003 -0.0131 540  LEU B CD1 
12918 C CD2 . LEU B 542  ? 0.2221 0.3098 0.2508 -0.0159 0.0007  -0.0112 540  LEU B CD2 
12919 N N   . PHE B 543  ? 0.1966 0.2892 0.2311 -0.0097 -0.0009 -0.0127 541  PHE B N   
12920 C CA  . PHE B 543  ? 0.2040 0.2980 0.2401 -0.0061 -0.0007 -0.0131 541  PHE B CA  
12921 C C   . PHE B 543  ? 0.2048 0.3060 0.2428 -0.0066 -0.0012 -0.0124 541  PHE B C   
12922 O O   . PHE B 543  ? 0.2144 0.3165 0.2534 -0.0039 -0.0013 -0.0127 541  PHE B O   
12923 C CB  . PHE B 543  ? 0.1821 0.2684 0.2164 -0.0051 -0.0012 -0.0139 541  PHE B CB  
12924 C CG  . PHE B 543  ? 0.2011 0.2808 0.2338 -0.0050 -0.0008 -0.0145 541  PHE B CG  
12925 C CD1 . PHE B 543  ? 0.2126 0.2925 0.2460 -0.0028 0.0003  -0.0148 541  PHE B CD1 
12926 C CD2 . PHE B 543  ? 0.1820 0.2558 0.2124 -0.0071 -0.0016 -0.0148 541  PHE B CD2 
12927 C CE1 . PHE B 543  ? 0.2351 0.3093 0.2670 -0.0027 0.0004  -0.0153 541  PHE B CE1 
12928 C CE2 . PHE B 543  ? 0.1962 0.2644 0.2253 -0.0067 -0.0014 -0.0153 541  PHE B CE2 
12929 C CZ  . PHE B 543  ? 0.2411 0.3098 0.2711 -0.0047 -0.0004 -0.0155 541  PHE B CZ  
12930 N N   . GLY B 544  ? 0.2016 0.3080 0.2402 -0.0099 -0.0017 -0.0115 542  GLY B N   
12931 C CA  . GLY B 544  ? 0.1917 0.3061 0.2327 -0.0105 -0.0023 -0.0107 542  GLY B CA  
12932 C C   . GLY B 544  ? 0.2163 0.3282 0.2564 -0.0107 -0.0038 -0.0110 542  GLY B C   
12933 O O   . GLY B 544  ? 0.2362 0.3414 0.2734 -0.0127 -0.0048 -0.0114 542  GLY B O   
12934 N N   . ASP B 545  ? 0.2402 0.3576 0.2825 -0.0083 -0.0040 -0.0108 543  ASP B N   
12935 C CA  . ASP B 545  ? 0.2732 0.3892 0.3145 -0.0085 -0.0055 -0.0108 543  ASP B CA  
12936 C C   . ASP B 545  ? 0.2537 0.3613 0.2927 -0.0060 -0.0052 -0.0118 543  ASP B C   
12937 O O   . ASP B 545  ? 0.2624 0.3676 0.2999 -0.0064 -0.0064 -0.0120 543  ASP B O   
12938 C CB  . ASP B 545  ? 0.2848 0.4092 0.3291 -0.0064 -0.0058 -0.0102 543  ASP B CB  
12939 C CG  . ASP B 545  ? 0.4621 0.5961 0.5092 -0.0090 -0.0061 -0.0091 543  ASP B CG  
12940 O OD1 . ASP B 545  ? 0.4923 0.6259 0.5385 -0.0134 -0.0066 -0.0087 543  ASP B OD1 
12941 O OD2 . ASP B 545  ? 0.5321 0.6742 0.5824 -0.0065 -0.0058 -0.0086 543  ASP B OD2 
12942 N N   . ALA B 546  ? 0.2247 0.3282 0.2635 -0.0035 -0.0038 -0.0124 544  ALA B N   
12943 C CA  . ALA B 546  ? 0.2063 0.3028 0.2434 -0.0011 -0.0036 -0.0131 544  ALA B CA  
12944 C C   . ALA B 546  ? 0.2056 0.2952 0.2396 -0.0036 -0.0043 -0.0136 544  ALA B C   
12945 O O   . ALA B 546  ? 0.2145 0.3005 0.2470 -0.0028 -0.0047 -0.0140 544  ALA B O   
12946 C CB  . ALA B 546  ? 0.2346 0.3283 0.2721 0.0017  -0.0021 -0.0136 544  ALA B CB  
12947 N N   . ARG B 547  ? 0.2034 0.2909 0.2364 -0.0065 -0.0044 -0.0137 545  ARG B N   
12948 C CA  . ARG B 547  ? 0.1862 0.2666 0.2160 -0.0085 -0.0051 -0.0143 545  ARG B CA  
12949 C C   . ARG B 547  ? 0.1966 0.2763 0.2255 -0.0118 -0.0055 -0.0141 545  ARG B C   
12950 O O   . ARG B 547  ? 0.2000 0.2838 0.2306 -0.0121 -0.0048 -0.0135 545  ARG B O   
12951 C CB  . ARG B 547  ? 0.2469 0.3208 0.2758 -0.0060 -0.0042 -0.0151 545  ARG B CB  
12952 C CG  . ARG B 547  ? 0.1983 0.2714 0.2284 -0.0046 -0.0030 -0.0152 545  ARG B CG  
12953 C CD  . ARG B 547  ? 0.2097 0.2768 0.2392 -0.0023 -0.0023 -0.0159 545  ARG B CD  
12954 N NE  . ARG B 547  ? 0.1894 0.2569 0.2204 -0.0004 -0.0013 -0.0160 545  ARG B NE  
12955 C CZ  . ARG B 547  ? 0.1889 0.2529 0.2194 -0.0007 -0.0010 -0.0163 545  ARG B CZ  
12956 N NH1 . ARG B 547  ? 0.1970 0.2567 0.2256 -0.0027 -0.0016 -0.0166 545  ARG B NH1 
12957 N NH2 . ARG B 547  ? 0.2135 0.2781 0.2451 0.0010  -0.0002 -0.0164 545  ARG B NH2 
12958 N N   . THR B 548  ? 0.1813 0.2555 0.2071 -0.0142 -0.0065 -0.0144 546  THR B N   
12959 C CA  . THR B 548  ? 0.1807 0.2525 0.2049 -0.0175 -0.0071 -0.0142 546  THR B CA  
12960 C C   . THR B 548  ? 0.1743 0.2400 0.1974 -0.0160 -0.0062 -0.0148 546  THR B C   
12961 O O   . THR B 548  ? 0.1706 0.2311 0.1926 -0.0140 -0.0060 -0.0156 546  THR B O   
12962 C CB  . THR B 548  ? 0.1843 0.2522 0.2051 -0.0206 -0.0089 -0.0144 546  THR B CB  
12963 O OG1 . THR B 548  ? 0.2320 0.3058 0.2538 -0.0220 -0.0099 -0.0138 546  THR B OG1 
12964 C CG2 . THR B 548  ? 0.2142 0.2788 0.2327 -0.0241 -0.0097 -0.0140 546  THR B CG2 
12965 N N   . ASN B 549  ? 0.1696 0.2364 0.1933 -0.0169 -0.0057 -0.0143 547  ASN B N   
12966 C CA  . ASN B 549  ? 0.1808 0.2421 0.2034 -0.0158 -0.0051 -0.0147 547  ASN B CA  
12967 C C   . ASN B 549  ? 0.1771 0.2309 0.1962 -0.0175 -0.0063 -0.0152 547  ASN B C   
12968 O O   . ASN B 549  ? 0.1899 0.2429 0.2069 -0.0207 -0.0077 -0.0149 547  ASN B O   
12969 C CB  . ASN B 549  ? 0.1673 0.2316 0.1906 -0.0169 -0.0046 -0.0140 547  ASN B CB  
12970 C CG  . ASN B 549  ? 0.1501 0.2099 0.1728 -0.0153 -0.0039 -0.0144 547  ASN B CG  
12971 O OD1 . ASN B 549  ? 0.1712 0.2269 0.1939 -0.0128 -0.0037 -0.0153 547  ASN B OD1 
12972 N ND2 . ASN B 549  ? 0.1692 0.2299 0.1912 -0.0168 -0.0037 -0.0137 547  ASN B ND2 
12973 N N   . SER B 550  ? 0.1709 0.2192 0.1893 -0.0153 -0.0059 -0.0161 548  SER B N   
12974 C CA  . SER B 550  ? 0.1965 0.2375 0.2114 -0.0164 -0.0070 -0.0166 548  SER B CA  
12975 C C   . SER B 550  ? 0.1750 0.2146 0.1880 -0.0195 -0.0078 -0.0158 548  SER B C   
12976 O O   . SER B 550  ? 0.1911 0.2343 0.2057 -0.0198 -0.0071 -0.0150 548  SER B O   
12977 C CB  . SER B 550  ? 0.1675 0.2040 0.1826 -0.0134 -0.0063 -0.0174 548  SER B CB  
12978 O OG  . SER B 550  ? 0.1765 0.2141 0.1933 -0.0124 -0.0056 -0.0171 548  SER B OG  
12979 N N   . ALA B 551  ? 0.1962 0.2302 0.2056 -0.0217 -0.0092 -0.0159 549  ALA B N   
12980 C CA  . ALA B 551  ? 0.2113 0.2425 0.2181 -0.0249 -0.0102 -0.0151 549  ALA B CA  
12981 C C   . ALA B 551  ? 0.2049 0.2285 0.2093 -0.0235 -0.0106 -0.0157 549  ALA B C   
12982 O O   . ALA B 551  ? 0.2159 0.2349 0.2192 -0.0213 -0.0108 -0.0168 549  ALA B O   
12983 C CB  . ALA B 551  ? 0.2385 0.2684 0.2424 -0.0288 -0.0120 -0.0147 549  ALA B CB  
12984 N N   . GLY B 552  ? 0.2160 0.2386 0.2197 -0.0247 -0.0107 -0.0148 550  GLY B N   
12985 C CA  . GLY B 552  ? 0.2318 0.2473 0.2330 -0.0238 -0.0114 -0.0152 550  GLY B CA  
12986 C C   . GLY B 552  ? 0.2064 0.2157 0.2028 -0.0271 -0.0133 -0.0147 550  GLY B C   
12987 O O   . GLY B 552  ? 0.2431 0.2525 0.2378 -0.0299 -0.0143 -0.0144 550  GLY B O   
12988 N N   . LEU B 553  ? 0.2318 0.2354 0.2258 -0.0268 -0.0140 -0.0145 551  LEU B N   
12989 C CA  . LEU B 553  ? 0.2346 0.2312 0.2236 -0.0298 -0.0160 -0.0139 551  LEU B CA  
12990 C C   . LEU B 553  ? 0.2369 0.2328 0.2248 -0.0310 -0.0161 -0.0126 551  LEU B C   
12991 O O   . LEU B 553  ? 0.2629 0.2600 0.2529 -0.0282 -0.0151 -0.0128 551  LEU B O   
12992 C CB  . LEU B 553  ? 0.2567 0.2448 0.2426 -0.0274 -0.0171 -0.0153 551  LEU B CB  
12993 C CG  . LEU B 553  ? 0.2728 0.2603 0.2584 -0.0265 -0.0172 -0.0167 551  LEU B CG  
12994 C CD1 . LEU B 553  ? 0.3279 0.3081 0.3112 -0.0232 -0.0177 -0.0182 551  LEU B CD1 
12995 C CD2 . LEU B 553  ? 0.3165 0.3026 0.2988 -0.0310 -0.0187 -0.0161 551  LEU B CD2 
12996 N N   . ASP B 554  ? 0.2342 0.2283 0.2189 -0.0353 -0.0172 -0.0111 552  ASP B N   
12997 C CA  . ASP B 554  ? 0.2409 0.2350 0.2243 -0.0370 -0.0172 -0.0096 552  ASP B CA  
12998 C C   . ASP B 554  ? 0.2339 0.2181 0.2127 -0.0364 -0.0190 -0.0096 552  ASP B C   
12999 O O   . ASP B 554  ? 0.2514 0.2291 0.2256 -0.0393 -0.0208 -0.0091 552  ASP B O   
13000 C CB  . ASP B 554  ? 0.2585 0.2564 0.2409 -0.0421 -0.0175 -0.0077 552  ASP B CB  
13001 C CG  . ASP B 554  ? 0.2545 0.2529 0.2354 -0.0441 -0.0172 -0.0059 552  ASP B CG  
13002 O OD1 . ASP B 554  ? 0.2706 0.2661 0.2511 -0.0415 -0.0171 -0.0062 552  ASP B OD1 
13003 O OD2 . ASP B 554  ? 0.2849 0.2870 0.2652 -0.0484 -0.0172 -0.0042 552  ASP B OD2 
13004 N N   . LEU B 555  ? 0.2481 0.2309 0.2281 -0.0328 -0.0186 -0.0101 553  LEU B N   
13005 C CA  . LEU B 555  ? 0.2698 0.2436 0.2458 -0.0316 -0.0202 -0.0103 553  LEU B CA  
13006 C C   . LEU B 555  ? 0.2677 0.2385 0.2398 -0.0347 -0.0212 -0.0083 553  LEU B C   
13007 O O   . LEU B 555  ? 0.2803 0.2439 0.2492 -0.0336 -0.0227 -0.0081 553  LEU B O   
13008 C CB  . LEU B 555  ? 0.2595 0.2333 0.2383 -0.0266 -0.0196 -0.0116 553  LEU B CB  
13009 C CG  . LEU B 555  ? 0.2504 0.2268 0.2328 -0.0234 -0.0186 -0.0134 553  LEU B CG  
13010 C CD1 . LEU B 555  ? 0.3017 0.2776 0.2866 -0.0189 -0.0181 -0.0144 553  LEU B CD1 
13011 C CD2 . LEU B 555  ? 0.3092 0.2799 0.2884 -0.0240 -0.0198 -0.0142 553  LEU B CD2 
13012 N N   . SER B 556  ? 0.2621 0.2385 0.2347 -0.0385 -0.0205 -0.0067 554  SER B N   
13013 C CA  . SER B 556  ? 0.2669 0.2402 0.2352 -0.0424 -0.0215 -0.0046 554  SER B CA  
13014 C C   . SER B 556  ? 0.2884 0.2585 0.2530 -0.0474 -0.0229 -0.0035 554  SER B C   
13015 O O   . SER B 556  ? 0.2867 0.2537 0.2473 -0.0512 -0.0239 -0.0015 554  SER B O   
13016 C CB  . SER B 556  ? 0.2681 0.2499 0.2389 -0.0434 -0.0196 -0.0033 554  SER B CB  
13017 O OG  . SER B 556  ? 0.2806 0.2703 0.2541 -0.0461 -0.0183 -0.0028 554  SER B OG  
13018 N N   . ASN B 557  ? 0.2657 0.2363 0.2313 -0.0475 -0.0232 -0.0047 555  ASN B N   
13019 C CA  . ASN B 557  ? 0.2602 0.2281 0.2225 -0.0523 -0.0247 -0.0039 555  ASN B CA  
13020 C C   . ASN B 557  ? 0.2835 0.2392 0.2402 -0.0517 -0.0272 -0.0047 555  ASN B C   
13021 O O   . ASN B 557  ? 0.2819 0.2349 0.2394 -0.0476 -0.0273 -0.0069 555  ASN B O   
13022 C CB  . ASN B 557  ? 0.2763 0.2518 0.2428 -0.0526 -0.0236 -0.0048 555  ASN B CB  
13023 C CG  . ASN B 557  ? 0.2938 0.2675 0.2574 -0.0577 -0.0253 -0.0040 555  ASN B CG  
13024 O OD1 . ASN B 557  ? 0.3014 0.2654 0.2598 -0.0589 -0.0276 -0.0043 555  ASN B OD1 
13025 N ND2 . ASN B 557  ? 0.2833 0.2664 0.2503 -0.0608 -0.0243 -0.0030 555  ASN B ND2 
13026 N N   . GLU B 558  ? 0.2958 0.2442 0.2468 -0.0556 -0.0292 -0.0031 556  GLU B N   
13027 C CA  . GLU B 558  ? 0.3210 0.2568 0.2659 -0.0547 -0.0317 -0.0039 556  GLU B CA  
13028 C C   . GLU B 558  ? 0.3233 0.2563 0.2672 -0.0548 -0.0327 -0.0057 556  GLU B C   
13029 O O   . GLU B 558  ? 0.3408 0.2658 0.2818 -0.0514 -0.0339 -0.0074 556  GLU B O   
13030 C CB  . GLU B 558  ? 0.3656 0.2936 0.3041 -0.0595 -0.0339 -0.0016 556  GLU B CB  
13031 C CG  . GLU B 558  ? 0.3572 0.2844 0.2947 -0.0589 -0.0336 0.0000  556  GLU B CG  
13032 C CD  . GLU B 558  ? 0.3612 0.2837 0.2987 -0.0527 -0.0338 -0.0015 556  GLU B CD  
13033 O OE1 . GLU B 558  ? 0.3461 0.2630 0.2828 -0.0490 -0.0347 -0.0036 556  GLU B OE1 
13034 O OE2 . GLU B 558  ? 0.3432 0.2680 0.2817 -0.0516 -0.0330 -0.0005 556  GLU B OE2 
13035 N N   . GLU B 559  ? 0.3079 0.2471 0.2536 -0.0587 -0.0324 -0.0052 557  GLU B N   
13036 C CA  . GLU B 559  ? 0.3113 0.2485 0.2562 -0.0586 -0.0333 -0.0069 557  GLU B CA  
13037 C C   . GLU B 559  ? 0.2972 0.2375 0.2462 -0.0524 -0.0316 -0.0093 557  GLU B C   
13038 O O   . GLU B 559  ? 0.3247 0.2585 0.2711 -0.0497 -0.0326 -0.0113 557  GLU B O   
13039 C CB  . GLU B 559  ? 0.3653 0.3106 0.3126 -0.0635 -0.0330 -0.0059 557  GLU B CB  
13040 C CG  . GLU B 559  ? 0.4371 0.3795 0.3801 -0.0704 -0.0349 -0.0036 557  GLU B CG  
13041 C CD  . GLU B 559  ? 0.5341 0.4849 0.4800 -0.0747 -0.0348 -0.0029 557  GLU B CD  
13042 O OE1 . GLU B 559  ? 0.5386 0.4907 0.4858 -0.0730 -0.0350 -0.0048 557  GLU B OE1 
13043 O OE2 . GLU B 559  ? 0.4993 0.4558 0.4462 -0.0797 -0.0346 -0.0005 557  GLU B OE2 
13044 N N   . THR B 560  ? 0.2805 0.2307 0.2357 -0.0502 -0.0291 -0.0092 558  THR B N   
13045 C CA  . THR B 560  ? 0.2698 0.2233 0.2292 -0.0446 -0.0274 -0.0113 558  THR B CA  
13046 C C   . THR B 560  ? 0.2828 0.2284 0.2400 -0.0401 -0.0280 -0.0125 558  THR B C   
13047 O O   . THR B 560  ? 0.2818 0.2249 0.2390 -0.0364 -0.0279 -0.0144 558  THR B O   
13048 C CB  . THR B 560  ? 0.2615 0.2262 0.2275 -0.0433 -0.0248 -0.0107 558  THR B CB  
13049 O OG1 . THR B 560  ? 0.2831 0.2555 0.2512 -0.0473 -0.0243 -0.0096 558  THR B OG1 
13050 C CG2 . THR B 560  ? 0.2808 0.2488 0.2510 -0.0380 -0.0232 -0.0127 558  THR B CG2 
13051 N N   . LEU B 561  ? 0.2760 0.2180 0.2312 -0.0403 -0.0286 -0.0112 559  LEU B N   
13052 C CA  . LEU B 561  ? 0.2543 0.1893 0.2077 -0.0358 -0.0292 -0.0123 559  LEU B CA  
13053 C C   . LEU B 561  ? 0.2994 0.2237 0.2468 -0.0354 -0.0315 -0.0135 559  LEU B C   
13054 O O   . LEU B 561  ? 0.2789 0.1998 0.2263 -0.0306 -0.0314 -0.0153 559  LEU B O   
13055 C CB  . LEU B 561  ? 0.2773 0.2101 0.2292 -0.0364 -0.0298 -0.0106 559  LEU B CB  
13056 C CG  . LEU B 561  ? 0.2617 0.2043 0.2193 -0.0354 -0.0275 -0.0098 559  LEU B CG  
13057 C CD1 . LEU B 561  ? 0.2783 0.2181 0.2334 -0.0367 -0.0283 -0.0080 559  LEU B CD1 
13058 C CD2 . LEU B 561  ? 0.2744 0.2209 0.2370 -0.0299 -0.0260 -0.0116 559  LEU B CD2 
13059 N N   . ALA B 562  ? 0.2990 0.2180 0.2413 -0.0402 -0.0334 -0.0125 560  ALA B N   
13060 C CA  . ALA B 562  ? 0.3073 0.2152 0.2432 -0.0399 -0.0358 -0.0138 560  ALA B CA  
13061 C C   . ALA B 562  ? 0.3381 0.2476 0.2753 -0.0376 -0.0351 -0.0161 560  ALA B C   
13062 O O   . ALA B 562  ? 0.3280 0.2308 0.2624 -0.0337 -0.0357 -0.0181 560  ALA B O   
13063 C CB  . ALA B 562  ? 0.3447 0.2466 0.2747 -0.0463 -0.0382 -0.0121 560  ALA B CB  
13064 N N   . SER B 563  ? 0.3019 0.2204 0.2431 -0.0399 -0.0338 -0.0159 561  SER B N   
13065 C CA  . SER B 563  ? 0.2989 0.2190 0.2411 -0.0378 -0.0331 -0.0180 561  SER B CA  
13066 C C   . SER B 563  ? 0.3149 0.2391 0.2618 -0.0315 -0.0309 -0.0195 561  SER B C   
13067 O O   . SER B 563  ? 0.3182 0.2390 0.2637 -0.0280 -0.0309 -0.0216 561  SER B O   
13068 C CB  . SER B 563  ? 0.3203 0.2489 0.2655 -0.0418 -0.0326 -0.0173 561  SER B CB  
13069 O OG  . SER B 563  ? 0.3584 0.2981 0.3105 -0.0413 -0.0302 -0.0162 561  SER B OG  
13070 N N   . LEU B 564  ? 0.2862 0.2177 0.2386 -0.0302 -0.0291 -0.0185 562  LEU B N   
13071 C CA  . LEU B 564  ? 0.2740 0.2093 0.2309 -0.0247 -0.0271 -0.0198 562  LEU B CA  
13072 C C   . LEU B 564  ? 0.2952 0.2220 0.2488 -0.0206 -0.0281 -0.0209 562  LEU B C   
13073 O O   . LEU B 564  ? 0.3042 0.2311 0.2592 -0.0163 -0.0271 -0.0227 562  LEU B O   
13074 C CB  . LEU B 564  ? 0.2893 0.2331 0.2519 -0.0245 -0.0253 -0.0184 562  LEU B CB  
13075 C CG  . LEU B 564  ? 0.3048 0.2533 0.2726 -0.0195 -0.0234 -0.0194 562  LEU B CG  
13076 C CD1 . LEU B 564  ? 0.3015 0.2546 0.2721 -0.0177 -0.0219 -0.0208 562  LEU B CD1 
13077 C CD2 . LEU B 564  ? 0.3330 0.2886 0.3053 -0.0199 -0.0221 -0.0180 562  LEU B CD2 
13078 N N   . THR B 565  ? 0.2918 0.2114 0.2411 -0.0219 -0.0300 -0.0199 563  THR B N   
13079 C CA  . THR B 565  ? 0.2922 0.2032 0.2380 -0.0179 -0.0312 -0.0210 563  THR B CA  
13080 C C   . THR B 565  ? 0.3454 0.2504 0.2873 -0.0158 -0.0319 -0.0232 563  THR B C   
13081 O O   . THR B 565  ? 0.3185 0.2221 0.2611 -0.0106 -0.0312 -0.0248 563  THR B O   
13082 C CB  . THR B 565  ? 0.3224 0.2249 0.2626 -0.0205 -0.0337 -0.0195 563  THR B CB  
13083 O OG1 . THR B 565  ? 0.3140 0.2218 0.2575 -0.0218 -0.0330 -0.0175 563  THR B OG1 
13084 C CG2 . THR B 565  ? 0.3469 0.2397 0.2828 -0.0162 -0.0352 -0.0206 563  THR B CG2 
13085 N N   . GLU B 566  ? 0.3089 0.2106 0.2467 -0.0198 -0.0332 -0.0232 564  GLU B N   
13086 C CA  . GLU B 566  ? 0.3108 0.2063 0.2441 -0.0181 -0.0340 -0.0254 564  GLU B CA  
13087 C C   . GLU B 566  ? 0.3375 0.2407 0.2757 -0.0146 -0.0315 -0.0270 564  GLU B C   
13088 O O   . GLU B 566  ? 0.3279 0.2276 0.2646 -0.0101 -0.0311 -0.0290 564  GLU B O   
13089 C CB  . GLU B 566  ? 0.3645 0.2548 0.2922 -0.0237 -0.0362 -0.0250 564  GLU B CB  
13090 C CG  . GLU B 566  ? 0.4562 0.3370 0.3778 -0.0269 -0.0390 -0.0236 564  GLU B CG  
13091 C CD  . GLU B 566  ? 0.5569 0.4288 0.4750 -0.0221 -0.0400 -0.0245 564  GLU B CD  
13092 O OE1 . GLU B 566  ? 0.6227 0.4890 0.5377 -0.0180 -0.0403 -0.0268 564  GLU B OE1 
13093 O OE2 . GLU B 566  ? 0.5624 0.4332 0.4809 -0.0224 -0.0404 -0.0228 564  GLU B OE2 
13094 N N   . ALA B 567  ? 0.2924 0.2060 0.2365 -0.0165 -0.0296 -0.0260 565  ALA B N   
13095 C CA  . ALA B 567  ? 0.3038 0.2246 0.2524 -0.0135 -0.0273 -0.0272 565  ALA B CA  
13096 C C   . ALA B 567  ? 0.3042 0.2274 0.2568 -0.0080 -0.0255 -0.0279 565  ALA B C   
13097 O O   . ALA B 567  ? 0.2793 0.2038 0.2329 -0.0041 -0.0242 -0.0295 565  ALA B O   
13098 C CB  . ALA B 567  ? 0.2934 0.2245 0.2473 -0.0166 -0.0259 -0.0259 565  ALA B CB  
13099 N N   . LEU B 568  ? 0.2631 0.1874 0.2180 -0.0076 -0.0255 -0.0266 566  LEU B N   
13100 C CA  . LEU B 568  ? 0.2559 0.1826 0.2148 -0.0026 -0.0242 -0.0271 566  LEU B CA  
13101 C C   . LEU B 568  ? 0.2665 0.1849 0.2210 0.0015  -0.0251 -0.0288 566  LEU B C   
13102 O O   . LEU B 568  ? 0.2765 0.1973 0.2335 0.0060  -0.0236 -0.0301 566  LEU B O   
13103 C CB  . LEU B 568  ? 0.2532 0.1823 0.2149 -0.0035 -0.0244 -0.0253 566  LEU B CB  
13104 C CG  . LEU B 568  ? 0.2528 0.1910 0.2193 -0.0067 -0.0231 -0.0238 566  LEU B CG  
13105 C CD1 . LEU B 568  ? 0.2724 0.2113 0.2400 -0.0078 -0.0236 -0.0221 566  LEU B CD1 
13106 C CD2 . LEU B 568  ? 0.2702 0.2169 0.2428 -0.0042 -0.0205 -0.0245 566  LEU B CD2 
13107 N N   . ARG B 569  ? 0.2856 0.1942 0.2335 0.0000  -0.0277 -0.0287 567  ARG B N   
13108 C CA  . ARG B 569  ? 0.3083 0.2081 0.2512 0.0041  -0.0288 -0.0304 567  ARG B CA  
13109 C C   . ARG B 569  ? 0.3305 0.2300 0.2719 0.0061  -0.0278 -0.0325 567  ARG B C   
13110 O O   . ARG B 569  ? 0.3280 0.2271 0.2699 0.0114  -0.0268 -0.0341 567  ARG B O   
13111 C CB  . ARG B 569  ? 0.3454 0.2338 0.2805 0.0014  -0.0320 -0.0299 567  ARG B CB  
13112 C CG  . ARG B 569  ? 0.4162 0.3029 0.3518 0.0010  -0.0331 -0.0281 567  ARG B CG  
13113 C CD  . ARG B 569  ? 0.4323 0.3076 0.3599 -0.0022 -0.0363 -0.0274 567  ARG B CD  
13114 N NE  . ARG B 569  ? 0.4964 0.3713 0.4247 -0.0033 -0.0372 -0.0253 567  ARG B NE  
13115 C CZ  . ARG B 569  ? 0.5319 0.3991 0.4545 -0.0073 -0.0397 -0.0237 567  ARG B CZ  
13116 N NH1 . ARG B 569  ? 0.5594 0.4185 0.4754 -0.0107 -0.0417 -0.0240 567  ARG B NH1 
13117 N NH2 . ARG B 569  ? 0.5594 0.4271 0.4831 -0.0080 -0.0402 -0.0218 567  ARG B NH2 
13118 N N   . GLU B 570  ? 0.3087 0.2090 0.2483 0.0021  -0.0281 -0.0325 568  GLU B N   
13119 C CA  . GLU B 570  ? 0.3180 0.2180 0.2556 0.0038  -0.0273 -0.0345 568  GLU B CA  
13120 C C   . GLU B 570  ? 0.3269 0.2365 0.2712 0.0074  -0.0241 -0.0350 568  GLU B C   
13121 O O   . GLU B 570  ? 0.3369 0.2457 0.2800 0.0112  -0.0230 -0.0368 568  GLU B O   
13122 C CB  . GLU B 570  ? 0.3365 0.2364 0.2715 -0.0016 -0.0284 -0.0341 568  GLU B CB  
13123 C CG  . GLU B 570  ? 0.3845 0.2736 0.3117 -0.0053 -0.0317 -0.0340 568  GLU B CG  
13124 C CD  . GLU B 570  ? 0.5090 0.4003 0.4355 -0.0119 -0.0328 -0.0326 568  GLU B CD  
13125 O OE1 . GLU B 570  ? 0.4639 0.3652 0.3960 -0.0133 -0.0310 -0.0319 568  GLU B OE1 
13126 O OE2 . GLU B 570  ? 0.5936 0.4768 0.5141 -0.0157 -0.0355 -0.0322 568  GLU B OE2 
13127 N N   . SER B 571  ? 0.2952 0.2140 0.2466 0.0063  -0.0226 -0.0333 569  SER B N   
13128 C CA  . SER B 571  ? 0.2945 0.2222 0.2522 0.0094  -0.0197 -0.0336 569  SER B CA  
13129 C C   . SER B 571  ? 0.3264 0.2531 0.2853 0.0150  -0.0188 -0.0346 569  SER B C   
13130 O O   . SER B 571  ? 0.3121 0.2431 0.2736 0.0184  -0.0167 -0.0356 569  SER B O   
13131 C CB  . SER B 571  ? 0.2931 0.2298 0.2575 0.0071  -0.0186 -0.0317 569  SER B CB  
13132 O OG  . SER B 571  ? 0.2991 0.2363 0.2662 0.0084  -0.0188 -0.0307 569  SER B OG  
13133 N N   . ALA B 572  ? 0.3011 0.2223 0.2581 0.0161  -0.0205 -0.0343 570  ALA B N   
13134 C CA  . ALA B 572  ? 0.3056 0.2264 0.2643 0.0216  -0.0198 -0.0352 570  ALA B CA  
13135 C C   . ALA B 572  ? 0.3548 0.2687 0.3078 0.0252  -0.0200 -0.0374 570  ALA B C   
13136 O O   . ALA B 572  ? 0.3917 0.3071 0.3466 0.0303  -0.0187 -0.0384 570  ALA B O   
13137 C CB  . ALA B 572  ? 0.3198 0.2372 0.2784 0.0218  -0.0215 -0.0340 570  ALA B CB  
13138 N N   . ALA B 573  ? 0.3387 0.2455 0.2849 0.0228  -0.0216 -0.0383 571  ALA B N   
13139 C CA  . ALA B 573  ? 0.3781 0.2778 0.3181 0.0262  -0.0219 -0.0407 571  ALA B CA  
13140 C C   . ALA B 573  ? 0.3674 0.2724 0.3086 0.0273  -0.0195 -0.0419 571  ALA B C   
13141 O O   . ALA B 573  ? 0.3846 0.2849 0.3211 0.0307  -0.0193 -0.0440 571  ALA B O   
13142 C CB  . ALA B 573  ? 0.3950 0.2832 0.3262 0.0230  -0.0251 -0.0412 571  ALA B CB  
13143 N N   . MET B 574  ? 0.3322 0.2467 0.2792 0.0247  -0.0178 -0.0406 572  MET B N   
13144 C CA  . MET B 574  ? 0.3015 0.2212 0.2496 0.0256  -0.0156 -0.0414 572  MET B CA  
13145 C C   . MET B 574  ? 0.3238 0.2497 0.2768 0.0308  -0.0128 -0.0419 572  MET B C   
13146 O O   . MET B 574  ? 0.3254 0.2552 0.2837 0.0325  -0.0121 -0.0409 572  MET B O   
13147 C CB  . MET B 574  ? 0.3440 0.2713 0.2964 0.0210  -0.0149 -0.0397 572  MET B CB  
13148 C CG  . MET B 574  ? 0.3483 0.2709 0.2962 0.0156  -0.0175 -0.0392 572  MET B CG  
13149 S SD  . MET B 574  ? 0.3597 0.2920 0.3139 0.0107  -0.0168 -0.0369 572  MET B SD  
13150 C CE  . MET B 574  ? 0.3720 0.2976 0.3199 0.0048  -0.0200 -0.0365 572  MET B CE  
13151 N N   . LYS B 575  ? 0.3074 0.2343 0.2586 0.0332  -0.0111 -0.0434 573  LYS B N   
13152 C CA  . LYS B 575  ? 0.3118 0.2459 0.2680 0.0377  -0.0080 -0.0437 573  LYS B CA  
13153 C C   . LYS B 575  ? 0.2817 0.2260 0.2446 0.0352  -0.0060 -0.0419 573  LYS B C   
13154 O O   . LYS B 575  ? 0.2970 0.2431 0.2585 0.0335  -0.0053 -0.0421 573  LYS B O   
13155 C CB  . LYS B 575  ? 0.3153 0.2460 0.2661 0.0415  -0.0069 -0.0460 573  LYS B CB  
13156 C CG  . LYS B 575  ? 0.3387 0.2771 0.2943 0.0461  -0.0035 -0.0463 573  LYS B CG  
13157 C CD  . LYS B 575  ? 0.4129 0.3470 0.3622 0.0501  -0.0025 -0.0487 573  LYS B CD  
13158 C CE  . LYS B 575  ? 0.5662 0.5070 0.5197 0.0555  0.0007  -0.0491 573  LYS B CE  
13159 N NZ  . LYS B 575  ? 0.5931 0.5444 0.5527 0.0545  0.0037  -0.0477 573  LYS B NZ  
13160 N N   . TRP B 576  ? 0.2736 0.2241 0.2435 0.0352  -0.0053 -0.0403 574  TRP B N   
13161 C CA  . TRP B 576  ? 0.2518 0.2115 0.2283 0.0331  -0.0036 -0.0386 574  TRP B CA  
13162 C C   . TRP B 576  ? 0.2407 0.2071 0.2215 0.0368  -0.0006 -0.0387 574  TRP B C   
13163 O O   . TRP B 576  ? 0.2646 0.2322 0.2479 0.0404  0.0001  -0.0389 574  TRP B O   
13164 C CB  . TRP B 576  ? 0.2414 0.2038 0.2227 0.0309  -0.0045 -0.0368 574  TRP B CB  
13165 C CG  . TRP B 576  ? 0.2509 0.2082 0.2288 0.0267  -0.0072 -0.0363 574  TRP B CG  
13166 C CD1 . TRP B 576  ? 0.2800 0.2308 0.2550 0.0263  -0.0095 -0.0362 574  TRP B CD1 
13167 C CD2 . TRP B 576  ? 0.2447 0.2032 0.2217 0.0224  -0.0077 -0.0355 574  TRP B CD2 
13168 N NE1 . TRP B 576  ? 0.2714 0.2195 0.2438 0.0217  -0.0113 -0.0354 574  TRP B NE1 
13169 C CE2 . TRP B 576  ? 0.2642 0.2173 0.2380 0.0192  -0.0103 -0.0350 574  TRP B CE2 
13170 C CE3 . TRP B 576  ? 0.2404 0.2042 0.2190 0.0208  -0.0063 -0.0351 574  TRP B CE3 
13171 C CZ2 . TRP B 576  ? 0.2807 0.2340 0.2532 0.0146  -0.0114 -0.0342 574  TRP B CZ2 
13172 C CZ3 . TRP B 576  ? 0.2530 0.2169 0.2303 0.0165  -0.0076 -0.0344 574  TRP B CZ3 
13173 C CH2 . TRP B 576  ? 0.2715 0.2306 0.2461 0.0134  -0.0100 -0.0339 574  TRP B CH2 
13174 N N   . THR B 577  ? 0.2621 0.2332 0.2438 0.0359  0.0012  -0.0384 575  THR B N   
13175 C CA  . THR B 577  ? 0.2263 0.2041 0.2119 0.0389  0.0042  -0.0383 575  THR B CA  
13176 C C   . THR B 577  ? 0.2246 0.2098 0.2153 0.0360  0.0055  -0.0364 575  THR B C   
13177 O O   . THR B 577  ? 0.2274 0.2122 0.2174 0.0323  0.0043  -0.0357 575  THR B O   
13178 C CB  . THR B 577  ? 0.2765 0.2517 0.2566 0.0415  0.0054  -0.0401 575  THR B CB  
13179 O OG1 . THR B 577  ? 0.3185 0.2918 0.2946 0.0383  0.0047  -0.0402 575  THR B OG1 
13180 C CG2 . THR B 577  ? 0.2881 0.2550 0.2624 0.0445  0.0040  -0.0422 575  THR B CG2 
13181 N N   . ALA B 578  ? 0.2109 0.2031 0.2068 0.0380  0.0080  -0.0357 576  ALA B N   
13182 C CA  . ALA B 578  ? 0.2117 0.2105 0.2118 0.0359  0.0095  -0.0340 576  ALA B CA  
13183 C C   . ALA B 578  ? 0.2041 0.2076 0.2054 0.0388  0.0125  -0.0341 576  ALA B C   
13184 O O   . ALA B 578  ? 0.2270 0.2329 0.2311 0.0419  0.0137  -0.0343 576  ALA B O   
13185 C CB  . ALA B 578  ? 0.2170 0.2203 0.2237 0.0342  0.0091  -0.0323 576  ALA B CB  
13186 N N   . LEU B 579  ? 0.2121 0.2167 0.2111 0.0378  0.0136  -0.0340 577  LEU B N   
13187 C CA  . LEU B 579  ? 0.2298 0.2381 0.2285 0.0404  0.0165  -0.0342 577  LEU B CA  
13188 C C   . LEU B 579  ? 0.2168 0.2312 0.2192 0.0382  0.0180  -0.0322 577  LEU B C   
13189 O O   . LEU B 579  ? 0.1987 0.2130 0.2018 0.0348  0.0166  -0.0312 577  LEU B O   
13190 C CB  . LEU B 579  ? 0.2607 0.2635 0.2514 0.0414  0.0163  -0.0361 577  LEU B CB  
13191 C CG  . LEU B 579  ? 0.2950 0.2896 0.2801 0.0429  0.0141  -0.0382 577  LEU B CG  
13192 C CD1 . LEU B 579  ? 0.3149 0.3040 0.2918 0.0436  0.0139  -0.0401 577  LEU B CD1 
13193 C CD2 . LEU B 579  ? 0.2935 0.2891 0.2810 0.0470  0.0152  -0.0389 577  LEU B CD2 
13194 N N   . PRO B 580  ? 0.2011 0.2209 0.2057 0.0400  0.0208  -0.0315 578  PRO B N   
13195 C CA  . PRO B 580  ? 0.2018 0.2261 0.2083 0.0380  0.0223  -0.0297 578  PRO B CA  
13196 C C   . PRO B 580  ? 0.2048 0.2253 0.2046 0.0371  0.0217  -0.0305 578  PRO B C   
13197 O O   . PRO B 580  ? 0.2356 0.2547 0.2307 0.0394  0.0231  -0.0317 578  PRO B O   
13198 C CB  . PRO B 580  ? 0.2362 0.2665 0.2457 0.0405  0.0255  -0.0290 578  PRO B CB  
13199 C CG  . PRO B 580  ? 0.2361 0.2664 0.2478 0.0435  0.0254  -0.0300 578  PRO B CG  
13200 C CD  . PRO B 580  ? 0.2386 0.2609 0.2444 0.0440  0.0230  -0.0322 578  PRO B CD  
13201 N N   . GLN B 581  ? 0.1948 0.2135 0.1939 0.0339  0.0197  -0.0299 579  GLN B N   
13202 C CA  . GLN B 581  ? 0.2235 0.2385 0.2165 0.0326  0.0186  -0.0307 579  GLN B CA  
13203 C C   . GLN B 581  ? 0.2440 0.2633 0.2381 0.0313  0.0200  -0.0289 579  GLN B C   
13204 O O   . GLN B 581  ? 0.2309 0.2521 0.2278 0.0287  0.0190  -0.0274 579  GLN B O   
13205 C CB  . GLN B 581  ? 0.2181 0.2292 0.2100 0.0298  0.0155  -0.0310 579  GLN B CB  
13206 C CG  . GLN B 581  ? 0.2292 0.2351 0.2191 0.0307  0.0138  -0.0326 579  GLN B CG  
13207 C CD  . GLN B 581  ? 0.2994 0.2995 0.2818 0.0325  0.0134  -0.0349 579  GLN B CD  
13208 O OE1 . GLN B 581  ? 0.2919 0.2920 0.2705 0.0332  0.0144  -0.0353 579  GLN B OE1 
13209 N NE2 . GLN B 581  ? 0.3494 0.3440 0.3294 0.0333  0.0117  -0.0363 579  GLN B NE2 
13210 N N   . LEU B 582  ? 0.2247 0.2457 0.2164 0.0333  0.0224  -0.0290 580  LEU B N   
13211 C CA  . LEU B 582  ? 0.2205 0.2450 0.2123 0.0323  0.0238  -0.0273 580  LEU B CA  
13212 C C   . LEU B 582  ? 0.2464 0.2671 0.2318 0.0310  0.0222  -0.0280 580  LEU B C   
13213 O O   . LEU B 582  ? 0.2615 0.2770 0.2423 0.0311  0.0202  -0.0300 580  LEU B O   
13214 C CB  . LEU B 582  ? 0.2365 0.2651 0.2289 0.0348  0.0272  -0.0267 580  LEU B CB  
13215 C CG  . LEU B 582  ? 0.2948 0.3292 0.2949 0.0347  0.0288  -0.0249 580  LEU B CG  
13216 C CD1 . LEU B 582  ? 0.2628 0.2967 0.2666 0.0359  0.0280  -0.0258 580  LEU B CD1 
13217 C CD2 . LEU B 582  ? 0.3541 0.3935 0.3549 0.0364  0.0323  -0.0238 580  LEU B CD2 
13218 N N   . ALA B 583  ? 0.2347 0.2580 0.2198 0.0298  0.0228  -0.0264 581  ALA B N   
13219 C CA  . ALA B 583  ? 0.2398 0.2602 0.2192 0.0285  0.0211  -0.0269 581  ALA B CA  
13220 C C   . ALA B 583  ? 0.2986 0.3151 0.2708 0.0306  0.0215  -0.0291 581  ALA B C   
13221 O O   . ALA B 583  ? 0.3128 0.3249 0.2798 0.0296  0.0192  -0.0304 581  ALA B O   
13222 C CB  . ALA B 583  ? 0.2769 0.3008 0.2570 0.0273  0.0220  -0.0247 581  ALA B CB  
13223 N N   . THR B 584  ? 0.2608 0.2789 0.2327 0.0335  0.0243  -0.0294 582  THR B N   
13224 C CA  . THR B 584  ? 0.2670 0.2816 0.2317 0.0360  0.0250  -0.0316 582  THR B CA  
13225 C C   . THR B 584  ? 0.2488 0.2586 0.2117 0.0378  0.0240  -0.0341 582  THR B C   
13226 O O   . THR B 584  ? 0.2724 0.2787 0.2292 0.0404  0.0246  -0.0361 582  THR B O   
13227 C CB  . THR B 584  ? 0.3224 0.3415 0.2875 0.0384  0.0289  -0.0307 582  THR B CB  
13228 O OG1 . THR B 584  ? 0.3142 0.3383 0.2869 0.0390  0.0306  -0.0293 582  THR B OG1 
13229 C CG2 . THR B 584  ? 0.3988 0.4207 0.3627 0.0368  0.0296  -0.0286 582  THR B CG2 
13230 N N   . GLY B 585  ? 0.2731 0.2824 0.2406 0.0367  0.0225  -0.0339 583  GLY B N   
13231 C CA  . GLY B 585  ? 0.2647 0.2690 0.2304 0.0383  0.0212  -0.0361 583  GLY B CA  
13232 C C   . GLY B 585  ? 0.2503 0.2582 0.2228 0.0398  0.0225  -0.0354 583  GLY B C   
13233 O O   . GLY B 585  ? 0.2805 0.2948 0.2590 0.0395  0.0244  -0.0333 583  GLY B O   
13234 N N   . PRO B 586  ? 0.2487 0.2524 0.2204 0.0413  0.0213  -0.0370 584  PRO B N   
13235 C CA  . PRO B 586  ? 0.2332 0.2402 0.2113 0.0428  0.0222  -0.0364 584  PRO B CA  
13236 C C   . PRO B 586  ? 0.2504 0.2622 0.2300 0.0465  0.0257  -0.0364 584  PRO B C   
13237 O O   . PRO B 586  ? 0.2774 0.2872 0.2514 0.0492  0.0270  -0.0380 584  PRO B O   
13238 C CB  . PRO B 586  ? 0.2617 0.2617 0.2367 0.0437  0.0198  -0.0384 584  PRO B CB  
13239 C CG  . PRO B 586  ? 0.3151 0.3086 0.2813 0.0445  0.0189  -0.0406 584  PRO B CG  
13240 C CD  . PRO B 586  ? 0.2985 0.2939 0.2633 0.0415  0.0187  -0.0394 584  PRO B CD  
13241 N N   . ALA B 587  ? 0.2321 0.2504 0.2194 0.0466  0.0272  -0.0346 585  ALA B N   
13242 C CA  . ALA B 587  ? 0.2376 0.2619 0.2277 0.0497  0.0306  -0.0341 585  ALA B CA  
13243 C C   . ALA B 587  ? 0.2478 0.2719 0.2405 0.0528  0.0305  -0.0352 585  ALA B C   
13244 O O   . ALA B 587  ? 0.2607 0.2817 0.2552 0.0518  0.0280  -0.0355 585  ALA B O   
13245 C CB  . ALA B 587  ? 0.2597 0.2917 0.2567 0.0475  0.0323  -0.0312 585  ALA B CB  
13246 N N   . ALA B 588  ? 0.2531 0.2808 0.2461 0.0567  0.0333  -0.0358 586  ALA B N   
13247 C CA  . ALA B 588  ? 0.2541 0.2832 0.2504 0.0602  0.0336  -0.0366 586  ALA B CA  
13248 C C   . ALA B 588  ? 0.2447 0.2811 0.2505 0.0585  0.0340  -0.0342 586  ALA B C   
13249 O O   . ALA B 588  ? 0.2679 0.3096 0.2776 0.0556  0.0351  -0.0319 586  ALA B O   
13250 C CB  . ALA B 588  ? 0.2533 0.2853 0.2475 0.0650  0.0369  -0.0378 586  ALA B CB  
13251 N N   . GLY B 589  ? 0.2514 0.2876 0.2605 0.0603  0.0329  -0.0347 587  GLY B N   
13252 C CA  . GLY B 589  ? 0.2565 0.2998 0.2745 0.0591  0.0331  -0.0326 587  GLY B CA  
13253 C C   . GLY B 589  ? 0.2586 0.3012 0.2791 0.0621  0.0319  -0.0336 587  GLY B C   
13254 O O   . GLY B 589  ? 0.2801 0.3170 0.2954 0.0655  0.0312  -0.0359 587  GLY B O   
13255 N N   . GLU B 590  ? 0.2974 0.3455 0.3256 0.0608  0.0315  -0.0319 588  GLU B N   
13256 C CA  . GLU B 590  ? 0.2779 0.3258 0.3092 0.0633  0.0300  -0.0325 588  GLU B CA  
13257 C C   . GLU B 590  ? 0.2461 0.2851 0.2737 0.0615  0.0262  -0.0334 588  GLU B C   
13258 O O   . GLU B 590  ? 0.2551 0.2927 0.2835 0.0572  0.0246  -0.0323 588  GLU B O   
13259 C CB  . GLU B 590  ? 0.3093 0.3659 0.3499 0.0620  0.0305  -0.0302 588  GLU B CB  
13260 C CG  . GLU B 590  ? 0.3695 0.4358 0.4146 0.0635  0.0342  -0.0290 588  GLU B CG  
13261 C CD  . GLU B 590  ? 0.4804 0.5483 0.5241 0.0694  0.0361  -0.0308 588  GLU B CD  
13262 O OE1 . GLU B 590  ? 0.5782 0.6427 0.6215 0.0724  0.0342  -0.0322 588  GLU B OE1 
13263 O OE2 . GLU B 590  ? 0.6142 0.6867 0.6572 0.0712  0.0394  -0.0307 588  GLU B OE2 
13264 N N   . THR B 591  ? 0.2760 0.3092 0.2997 0.0649  0.0248  -0.0354 589  THR B N   
13265 C CA  . THR B 591  ? 0.2949 0.3190 0.3141 0.0634  0.0213  -0.0364 589  THR B CA  
13266 C C   . THR B 591  ? 0.2729 0.2969 0.2959 0.0648  0.0193  -0.0362 589  THR B C   
13267 O O   . THR B 591  ? 0.2894 0.3171 0.3153 0.0690  0.0204  -0.0366 589  THR B O   
13268 C CB  . THR B 591  ? 0.2827 0.2982 0.2929 0.0658  0.0207  -0.0389 589  THR B CB  
13269 O OG1 . THR B 591  ? 0.3216 0.3372 0.3281 0.0643  0.0224  -0.0390 589  THR B OG1 
13270 C CG2 . THR B 591  ? 0.3173 0.3232 0.3226 0.0638  0.0171  -0.0397 589  THR B CG2 
13271 N N   . ARG B 592  ? 0.2634 0.2835 0.2865 0.0614  0.0164  -0.0355 590  ARG B N   
13272 C CA  . ARG B 592  ? 0.3093 0.3279 0.3348 0.0625  0.0141  -0.0354 590  ARG B CA  
13273 C C   . ARG B 592  ? 0.2922 0.3015 0.3123 0.0597  0.0109  -0.0359 590  ARG B C   
13274 O O   . ARG B 592  ? 0.2607 0.2668 0.2772 0.0563  0.0105  -0.0359 590  ARG B O   
13275 C CB  . ARG B 592  ? 0.2923 0.3193 0.3265 0.0607  0.0143  -0.0333 590  ARG B CB  
13276 C CG  . ARG B 592  ? 0.3135 0.3411 0.3492 0.0553  0.0136  -0.0317 590  ARG B CG  
13277 C CD  . ARG B 592  ? 0.3907 0.4244 0.4339 0.0536  0.0129  -0.0299 590  ARG B CD  
13278 N NE  . ARG B 592  ? 0.3666 0.4014 0.4113 0.0488  0.0126  -0.0285 590  ARG B NE  
13279 C CZ  . ARG B 592  ? 0.3801 0.4098 0.4223 0.0458  0.0103  -0.0284 590  ARG B CZ  
13280 N NH1 . ARG B 592  ? 0.3674 0.3903 0.4056 0.0466  0.0079  -0.0294 590  ARG B NH1 
13281 N NH2 . ARG B 592  ? 0.3642 0.3957 0.4081 0.0420  0.0103  -0.0271 590  ARG B NH2 
13282 N N   . THR B 593  ? 0.2887 0.2943 0.3086 0.0612  0.0085  -0.0362 591  THR B N   
13283 C CA  . THR B 593  ? 0.2747 0.2719 0.2899 0.0585  0.0054  -0.0364 591  THR B CA  
13284 C C   . THR B 593  ? 0.2779 0.2782 0.2975 0.0539  0.0043  -0.0344 591  THR B C   
13285 O O   . THR B 593  ? 0.2871 0.2950 0.3137 0.0535  0.0052  -0.0331 591  THR B O   
13286 C CB  . THR B 593  ? 0.3183 0.3096 0.3310 0.0619  0.0032  -0.0374 591  THR B CB  
13287 O OG1 . THR B 593  ? 0.3435 0.3411 0.3632 0.0635  0.0031  -0.0362 591  THR B OG1 
13288 C CG2 . THR B 593  ? 0.3790 0.3662 0.3865 0.0667  0.0042  -0.0395 591  THR B CG2 
13289 N N   . VAL B 594  ? 0.2417 0.2360 0.2570 0.0503  0.0024  -0.0344 592  VAL B N   
13290 C CA  . VAL B 594  ? 0.2406 0.2360 0.2585 0.0461  0.0010  -0.0328 592  VAL B CA  
13291 C C   . VAL B 594  ? 0.2629 0.2516 0.2778 0.0462  -0.0020 -0.0329 592  VAL B C   
13292 O O   . VAL B 594  ? 0.2801 0.2608 0.2884 0.0463  -0.0034 -0.0340 592  VAL B O   
13293 C CB  . VAL B 594  ? 0.2465 0.2409 0.2619 0.0420  0.0012  -0.0324 592  VAL B CB  
13294 C CG1 . VAL B 594  ? 0.2471 0.2427 0.2650 0.0380  -0.0002 -0.0309 592  VAL B CG1 
13295 C CG2 . VAL B 594  ? 0.2677 0.2681 0.2855 0.0422  0.0040  -0.0322 592  VAL B CG2 
13296 N N   . LEU B 595  ? 0.2616 0.2534 0.2812 0.0462  -0.0030 -0.0318 593  LEU B N   
13297 C CA  . LEU B 595  ? 0.2525 0.2386 0.2698 0.0468  -0.0058 -0.0318 593  LEU B CA  
13298 C C   . LEU B 595  ? 0.2377 0.2230 0.2553 0.0422  -0.0074 -0.0304 593  LEU B C   
13299 O O   . LEU B 595  ? 0.2625 0.2537 0.2844 0.0397  -0.0064 -0.0293 593  LEU B O   
13300 C CB  . LEU B 595  ? 0.2531 0.2434 0.2754 0.0505  -0.0060 -0.0315 593  LEU B CB  
13301 C CG  . LEU B 595  ? 0.2772 0.2700 0.3004 0.0554  -0.0041 -0.0327 593  LEU B CG  
13302 C CD1 . LEU B 595  ? 0.3178 0.3155 0.3466 0.0588  -0.0046 -0.0323 593  LEU B CD1 
13303 C CD2 . LEU B 595  ? 0.2952 0.2790 0.3105 0.0578  -0.0047 -0.0346 593  LEU B CD2 
13304 N N   . ASN B 596  ? 0.2227 0.2004 0.2352 0.0412  -0.0098 -0.0305 594  ASN B N   
13305 C CA  . ASN B 596  ? 0.2358 0.2124 0.2480 0.0372  -0.0114 -0.0292 594  ASN B CA  
13306 C C   . ASN B 596  ? 0.2295 0.2117 0.2478 0.0378  -0.0119 -0.0281 594  ASN B C   
13307 O O   . ASN B 596  ? 0.2218 0.2031 0.2409 0.0409  -0.0130 -0.0282 594  ASN B O   
13308 C CB  . ASN B 596  ? 0.2217 0.1889 0.2272 0.0367  -0.0140 -0.0294 594  ASN B CB  
13309 C CG  . ASN B 596  ? 0.2329 0.1983 0.2369 0.0323  -0.0155 -0.0281 594  ASN B CG  
13310 O OD1 . ASN B 596  ? 0.2420 0.2127 0.2504 0.0306  -0.0153 -0.0270 594  ASN B OD1 
13311 N ND2 . ASN B 596  ? 0.2788 0.2365 0.2763 0.0303  -0.0170 -0.0282 594  ASN B ND2 
13312 N N   . PRO B 597  ? 0.2140 0.2018 0.2364 0.0349  -0.0112 -0.0270 595  PRO B N   
13313 C CA  . PRO B 597  ? 0.2297 0.2223 0.2574 0.0352  -0.0118 -0.0260 595  PRO B CA  
13314 C C   . PRO B 597  ? 0.2268 0.2146 0.2521 0.0351  -0.0146 -0.0255 595  PRO B C   
13315 O O   . PRO B 597  ? 0.2033 0.1940 0.2323 0.0366  -0.0156 -0.0250 595  PRO B O   
13316 C CB  . PRO B 597  ? 0.2078 0.2053 0.2386 0.0317  -0.0108 -0.0251 595  PRO B CB  
13317 C CG  . PRO B 597  ? 0.2162 0.2098 0.2420 0.0290  -0.0104 -0.0254 595  PRO B CG  
13318 C CD  . PRO B 597  ? 0.2052 0.1948 0.2273 0.0314  -0.0099 -0.0267 595  PRO B CD  
13319 N N   . GLY B 598  ? 0.2204 0.2011 0.2395 0.0332  -0.0160 -0.0255 596  GLY B N   
13320 C CA  . GLY B 598  ? 0.2380 0.2135 0.2541 0.0331  -0.0186 -0.0249 596  GLY B CA  
13321 C C   . GLY B 598  ? 0.2516 0.2217 0.2648 0.0369  -0.0200 -0.0256 596  GLY B C   
13322 O O   . GLY B 598  ? 0.2600 0.2260 0.2711 0.0374  -0.0224 -0.0250 596  GLY B O   
13323 N N   . ASP B 599  ? 0.2310 0.2008 0.2438 0.0399  -0.0187 -0.0269 597  ASP B N   
13324 C CA  . ASP B 599  ? 0.2607 0.2253 0.2705 0.0441  -0.0199 -0.0278 597  ASP B CA  
13325 C C   . ASP B 599  ? 0.2596 0.2270 0.2708 0.0473  -0.0175 -0.0292 597  ASP B C   
13326 O O   . ASP B 599  ? 0.2528 0.2164 0.2596 0.0466  -0.0166 -0.0302 597  ASP B O   
13327 C CB  . ASP B 599  ? 0.2844 0.2384 0.2859 0.0427  -0.0219 -0.0279 597  ASP B CB  
13328 C CG  . ASP B 599  ? 0.3229 0.2701 0.3206 0.0471  -0.0236 -0.0288 597  ASP B CG  
13329 O OD1 . ASP B 599  ? 0.3018 0.2528 0.3029 0.0518  -0.0227 -0.0296 597  ASP B OD1 
13330 O OD2 . ASP B 599  ? 0.3431 0.2813 0.3342 0.0459  -0.0259 -0.0285 597  ASP B OD2 
13331 N N   . HIS B 600  ? 0.2473 0.2213 0.2643 0.0509  -0.0166 -0.0293 598  HIS B N   
13332 C CA  . HIS B 600  ? 0.2611 0.2390 0.2799 0.0539  -0.0140 -0.0305 598  HIS B CA  
13333 C C   . HIS B 600  ? 0.2624 0.2326 0.2748 0.0574  -0.0144 -0.0322 598  HIS B C   
13334 O O   . HIS B 600  ? 0.3114 0.2835 0.3237 0.0596  -0.0121 -0.0334 598  HIS B O   
13335 C CB  . HIS B 600  ? 0.2722 0.2597 0.2991 0.0568  -0.0128 -0.0301 598  HIS B CB  
13336 C CG  . HIS B 600  ? 0.2800 0.2754 0.3130 0.0532  -0.0118 -0.0287 598  HIS B CG  
13337 N ND1 . HIS B 600  ? 0.3250 0.3294 0.3656 0.0546  -0.0109 -0.0280 598  HIS B ND1 
13338 C CD2 . HIS B 600  ? 0.2724 0.2679 0.3049 0.0484  -0.0117 -0.0279 598  HIS B CD2 
13339 C CE1 . HIS B 600  ? 0.3286 0.3377 0.3728 0.0506  -0.0104 -0.0269 598  HIS B CE1 
13340 N NE2 . HIS B 600  ? 0.2883 0.2921 0.3276 0.0471  -0.0107 -0.0269 598  HIS B NE2 
13341 N N   . ARG B 601  ? 0.2762 0.2375 0.2830 0.0581  -0.0171 -0.0323 599  ARG B N   
13342 C CA  . ARG B 601  ? 0.2805 0.2330 0.2802 0.0610  -0.0177 -0.0340 599  ARG B CA  
13343 C C   . ARG B 601  ? 0.2916 0.2390 0.2856 0.0575  -0.0172 -0.0347 599  ARG B C   
13344 O O   . ARG B 601  ? 0.3324 0.2737 0.3208 0.0597  -0.0171 -0.0363 599  ARG B O   
13345 C CB  . ARG B 601  ? 0.3257 0.2694 0.3205 0.0624  -0.0211 -0.0338 599  ARG B CB  
13346 C CG  . ARG B 601  ? 0.3306 0.2788 0.3307 0.0662  -0.0220 -0.0331 599  ARG B CG  
13347 C CD  . ARG B 601  ? 0.3731 0.3128 0.3685 0.0663  -0.0256 -0.0324 599  ARG B CD  
13348 N NE  . ARG B 601  ? 0.3456 0.2830 0.3392 0.0604  -0.0269 -0.0308 599  ARG B NE  
13349 C CZ  . ARG B 601  ? 0.4016 0.3309 0.3900 0.0590  -0.0298 -0.0299 599  ARG B CZ  
13350 N NH1 . ARG B 601  ? 0.4216 0.3438 0.4060 0.0632  -0.0321 -0.0303 599  ARG B NH1 
13351 N NH2 . ARG B 601  ? 0.3830 0.3112 0.3699 0.0535  -0.0306 -0.0285 599  ARG B NH2 
13352 N N   . ASP B 602  ? 0.2778 0.2275 0.2728 0.0521  -0.0169 -0.0335 600  ASP B N   
13353 C CA  . ASP B 602  ? 0.2867 0.2326 0.2770 0.0484  -0.0166 -0.0339 600  ASP B CA  
13354 C C   . ASP B 602  ? 0.2832 0.2365 0.2771 0.0486  -0.0134 -0.0344 600  ASP B C   
13355 O O   . ASP B 602  ? 0.2576 0.2189 0.2573 0.0464  -0.0120 -0.0333 600  ASP B O   
13356 C CB  . ASP B 602  ? 0.3044 0.2497 0.2943 0.0428  -0.0179 -0.0322 600  ASP B CB  
13357 C CG  . ASP B 602  ? 0.3234 0.2649 0.3085 0.0387  -0.0178 -0.0324 600  ASP B CG  
13358 O OD1 . ASP B 602  ? 0.3285 0.2650 0.3087 0.0401  -0.0176 -0.0340 600  ASP B OD1 
13359 O OD2 . ASP B 602  ? 0.3204 0.2643 0.3067 0.0342  -0.0179 -0.0311 600  ASP B OD2 
13360 N N   . VAL B 603  ? 0.2946 0.2450 0.2849 0.0514  -0.0124 -0.0362 601  VAL B N   
13361 C CA  . VAL B 603  ? 0.2912 0.2477 0.2838 0.0516  -0.0095 -0.0367 601  VAL B CA  
13362 C C   . VAL B 603  ? 0.2910 0.2453 0.2801 0.0466  -0.0096 -0.0365 601  VAL B C   
13363 O O   . VAL B 603  ? 0.2974 0.2431 0.2794 0.0454  -0.0112 -0.0374 601  VAL B O   
13364 C CB  . VAL B 603  ? 0.2895 0.2439 0.2791 0.0568  -0.0082 -0.0388 601  VAL B CB  
13365 C CG1 . VAL B 603  ? 0.2936 0.2544 0.2853 0.0568  -0.0051 -0.0392 601  VAL B CG1 
13366 C CG2 . VAL B 603  ? 0.2908 0.2480 0.2843 0.0619  -0.0082 -0.0389 601  VAL B CG2 
13367 N N   . VAL B 604  ? 0.2526 0.2145 0.2467 0.0437  -0.0080 -0.0354 602  VAL B N   
13368 C CA  . VAL B 604  ? 0.2388 0.1997 0.2304 0.0391  -0.0081 -0.0350 602  VAL B CA  
13369 C C   . VAL B 604  ? 0.2583 0.2198 0.2476 0.0400  -0.0062 -0.0363 602  VAL B C   
13370 O O   . VAL B 604  ? 0.2643 0.2208 0.2481 0.0376  -0.0070 -0.0368 602  VAL B O   
13371 C CB  . VAL B 604  ? 0.2452 0.2135 0.2428 0.0358  -0.0075 -0.0332 602  VAL B CB  
13372 C CG1 . VAL B 604  ? 0.2413 0.2084 0.2363 0.0311  -0.0078 -0.0327 602  VAL B CG1 
13373 C CG2 . VAL B 604  ? 0.2473 0.2151 0.2471 0.0354  -0.0092 -0.0321 602  VAL B CG2 
13374 N N   . GLY B 605  ? 0.2454 0.2129 0.2384 0.0433  -0.0037 -0.0366 603  GLY B N   
13375 C CA  . GLY B 605  ? 0.2589 0.2276 0.2498 0.0440  -0.0018 -0.0377 603  GLY B CA  
13376 C C   . GLY B 605  ? 0.2547 0.2309 0.2506 0.0476  0.0011  -0.0377 603  GLY B C   
13377 O O   . GLY B 605  ? 0.2524 0.2316 0.2525 0.0504  0.0012  -0.0374 603  GLY B O   
13378 N N   . SER B 606  ? 0.2376 0.2171 0.2332 0.0475  0.0032  -0.0380 604  SER B N   
13379 C CA  A SER B 606  ? 0.2543 0.2412 0.2542 0.0507  0.0062  -0.0380 604  SER B CA  
13380 C CA  B SER B 606  ? 0.2543 0.2411 0.2540 0.0508  0.0062  -0.0380 604  SER B CA  
13381 C CA  C SER B 606  ? 0.2544 0.2410 0.2539 0.0508  0.0062  -0.0381 604  SER B CA  
13382 C C   . SER B 606  ? 0.2404 0.2336 0.2433 0.0479  0.0081  -0.0367 604  SER B C   
13383 O O   . SER B 606  ? 0.2588 0.2495 0.2581 0.0449  0.0076  -0.0367 604  SER B O   
13384 C CB  A SER B 606  ? 0.2902 0.2734 0.2848 0.0551  0.0073  -0.0401 604  SER B CB  
13385 C CB  B SER B 606  ? 0.2901 0.2729 0.2842 0.0549  0.0072  -0.0402 604  SER B CB  
13386 C CB  C SER B 606  ? 0.2899 0.2721 0.2834 0.0547  0.0071  -0.0403 604  SER B CB  
13387 O OG  A SER B 606  ? 0.3008 0.2792 0.2889 0.0534  0.0071  -0.0411 604  SER B OG  
13388 O OG  B SER B 606  ? 0.3311 0.3078 0.3222 0.0582  0.0055  -0.0414 604  SER B OG  
13389 O OG  C SER B 606  ? 0.3138 0.3031 0.3103 0.0573  0.0104  -0.0402 604  SER B OG  
13390 N N   . VAL B 607  ? 0.2213 0.2230 0.2310 0.0488  0.0102  -0.0355 605  VAL B N   
13391 C CA  . VAL B 607  ? 0.2073 0.2152 0.2202 0.0465  0.0121  -0.0341 605  VAL B CA  
13392 C C   . VAL B 607  ? 0.2160 0.2295 0.2306 0.0497  0.0153  -0.0343 605  VAL B C   
13393 O O   . VAL B 607  ? 0.2262 0.2432 0.2444 0.0529  0.0163  -0.0343 605  VAL B O   
13394 C CB  . VAL B 607  ? 0.2054 0.2183 0.2248 0.0434  0.0116  -0.0321 605  VAL B CB  
13395 C CG1 . VAL B 607  ? 0.2154 0.2328 0.2408 0.0457  0.0118  -0.0315 605  VAL B CG1 
13396 C CG2 . VAL B 607  ? 0.2219 0.2402 0.2438 0.0412  0.0135  -0.0307 605  VAL B CG2 
13397 N N   . THR B 608  ? 0.2100 0.2243 0.2220 0.0488  0.0169  -0.0343 606  THR B N   
13398 C CA  . THR B 608  ? 0.2127 0.2331 0.2265 0.0510  0.0201  -0.0340 606  THR B CA  
13399 C C   . THR B 608  ? 0.2069 0.2339 0.2261 0.0478  0.0213  -0.0317 606  THR B C   
13400 O O   . THR B 608  ? 0.2294 0.2548 0.2467 0.0445  0.0206  -0.0311 606  THR B O   
13401 C CB  . THR B 608  ? 0.2310 0.2471 0.2373 0.0524  0.0210  -0.0357 606  THR B CB  
13402 O OG1 . THR B 608  ? 0.2536 0.2628 0.2546 0.0555  0.0197  -0.0379 606  THR B OG1 
13403 C CG2 . THR B 608  ? 0.2486 0.2712 0.2563 0.0545  0.0246  -0.0353 606  THR B CG2 
13404 N N   . GLU B 609  ? 0.2174 0.2517 0.2431 0.0487  0.0230  -0.0304 607  GLU B N   
13405 C CA  . GLU B 609  ? 0.2229 0.2628 0.2539 0.0454  0.0237  -0.0281 607  GLU B CA  
13406 C C   . GLU B 609  ? 0.2076 0.2520 0.2383 0.0455  0.0267  -0.0272 607  GLU B C   
13407 O O   . GLU B 609  ? 0.2364 0.2816 0.2645 0.0486  0.0287  -0.0282 607  GLU B O   
13408 C CB  . GLU B 609  ? 0.2549 0.2999 0.2934 0.0454  0.0233  -0.0269 607  GLU B CB  
13409 C CG  . GLU B 609  ? 0.2816 0.3214 0.3195 0.0445  0.0200  -0.0275 607  GLU B CG  
13410 C CD  . GLU B 609  ? 0.3456 0.3897 0.3903 0.0442  0.0191  -0.0263 607  GLU B CD  
13411 O OE1 . GLU B 609  ? 0.3764 0.4270 0.4260 0.0460  0.0209  -0.0256 607  GLU B OE1 
13412 O OE2 . GLU B 609  ? 0.3029 0.3439 0.3479 0.0420  0.0166  -0.0261 607  GLU B OE2 
13413 N N   . THR B 610  ? 0.1992 0.2459 0.2320 0.0420  0.0268  -0.0254 608  THR B N   
13414 C CA  . THR B 610  ? 0.2039 0.2534 0.2354 0.0413  0.0292  -0.0244 608  THR B CA  
13415 C C   . THR B 610  ? 0.2289 0.2866 0.2662 0.0419  0.0319  -0.0227 608  THR B C   
13416 O O   . THR B 610  ? 0.2166 0.2781 0.2601 0.0405  0.0314  -0.0213 608  THR B O   
13417 C CB  . THR B 610  ? 0.1983 0.2463 0.2294 0.0373  0.0279  -0.0231 608  THR B CB  
13418 O OG1 . THR B 610  ? 0.2137 0.2551 0.2406 0.0363  0.0251  -0.0244 608  THR B OG1 
13419 C CG2 . THR B 610  ? 0.2135 0.2630 0.2418 0.0367  0.0298  -0.0222 608  THR B CG2 
13420 N N   . SER B 611  ? 0.2067 0.2671 0.2420 0.0439  0.0347  -0.0227 609  SER B N   
13421 C CA  . SER B 611  ? 0.2279 0.2965 0.2685 0.0439  0.0375  -0.0207 609  SER B CA  
13422 C C   . SER B 611  ? 0.2544 0.3247 0.2968 0.0397  0.0376  -0.0183 609  SER B C   
13423 O O   . SER B 611  ? 0.2090 0.2746 0.2472 0.0378  0.0363  -0.0184 609  SER B O   
13424 C CB  . SER B 611  ? 0.2317 0.3029 0.2691 0.0471  0.0407  -0.0213 609  SER B CB  
13425 O OG  . SER B 611  ? 0.2499 0.3182 0.2815 0.0459  0.0414  -0.0212 609  SER B OG  
13426 N N   . GLU B 612  ? 0.2338 0.3108 0.2827 0.0383  0.0389  -0.0161 610  GLU B N   
13427 C CA  . GLU B 612  ? 0.2354 0.3135 0.2857 0.0345  0.0390  -0.0137 610  GLU B CA  
13428 C C   . GLU B 612  ? 0.2583 0.3356 0.3032 0.0345  0.0410  -0.0132 610  GLU B C   
13429 O O   . GLU B 612  ? 0.2520 0.3264 0.2946 0.0318  0.0400  -0.0122 610  GLU B O   
13430 C CB  . GLU B 612  ? 0.2868 0.3721 0.3447 0.0329  0.0400  -0.0114 610  GLU B CB  
13431 C CG  . GLU B 612  ? 0.3403 0.4260 0.4035 0.0325  0.0376  -0.0117 610  GLU B CG  
13432 C CD  . GLU B 612  ? 0.3856 0.4782 0.4563 0.0304  0.0382  -0.0094 610  GLU B CD  
13433 O OE1 . GLU B 612  ? 0.5569 0.6528 0.6287 0.0283  0.0400  -0.0072 610  GLU B OE1 
13434 O OE2 . GLU B 612  ? 0.4202 0.5149 0.4956 0.0309  0.0368  -0.0097 610  GLU B OE2 
13435 N N   . GLU B 613  ? 0.2567 0.3363 0.2990 0.0375  0.0436  -0.0140 611  GLU B N   
13436 C CA  . GLU B 613  ? 0.2546 0.3331 0.2910 0.0377  0.0454  -0.0138 611  GLU B CA  
13437 C C   . GLU B 613  ? 0.2457 0.3162 0.2753 0.0374  0.0430  -0.0155 611  GLU B C   
13438 O O   . GLU B 613  ? 0.2596 0.3281 0.2858 0.0355  0.0429  -0.0145 611  GLU B O   
13439 C CB  . GLU B 613  ? 0.2894 0.3717 0.3240 0.0415  0.0486  -0.0146 611  GLU B CB  
13440 N N   . ASP B 614  ? 0.2271 0.2929 0.2547 0.0391  0.0409  -0.0180 612  ASP B N   
13441 C CA  . ASP B 614  ? 0.2284 0.2870 0.2498 0.0385  0.0385  -0.0195 612  ASP B CA  
13442 C C   . ASP B 614  ? 0.2309 0.2874 0.2543 0.0348  0.0359  -0.0183 612  ASP B C   
13443 O O   . ASP B 614  ? 0.2134 0.2658 0.2323 0.0335  0.0346  -0.0185 612  ASP B O   
13444 C CB  . ASP B 614  ? 0.2372 0.2911 0.2555 0.0412  0.0370  -0.0224 612  ASP B CB  
13445 C CG  . ASP B 614  ? 0.2723 0.3258 0.2855 0.0449  0.0392  -0.0240 612  ASP B CG  
13446 O OD1 . ASP B 614  ? 0.3484 0.4034 0.3584 0.0449  0.0412  -0.0233 612  ASP B OD1 
13447 O OD2 . ASP B 614  ? 0.2882 0.3397 0.3004 0.0479  0.0389  -0.0261 612  ASP B OD2 
13448 N N   . ALA B 615  ? 0.2187 0.2780 0.2486 0.0333  0.0352  -0.0171 613  ALA B N   
13449 C CA  . ALA B 615  ? 0.2114 0.2690 0.2430 0.0301  0.0331  -0.0159 613  ALA B CA  
13450 C C   . ALA B 615  ? 0.2108 0.2696 0.2411 0.0281  0.0342  -0.0138 613  ALA B C   
13451 O O   . ALA B 615  ? 0.1999 0.2552 0.2273 0.0266  0.0326  -0.0136 613  ALA B O   
13452 C CB  . ALA B 615  ? 0.2279 0.2883 0.2664 0.0289  0.0322  -0.0149 613  ALA B CB  
13453 N N   . ARG B 616  ? 0.2368 0.3006 0.2691 0.0284  0.0370  -0.0122 614  ARG B N   
13454 C CA  . ARG B 616  ? 0.2129 0.2774 0.2434 0.0266  0.0381  -0.0100 614  ARG B CA  
13455 C C   . ARG B 616  ? 0.2093 0.2702 0.2323 0.0276  0.0382  -0.0111 614  ARG B C   
13456 O O   . ARG B 616  ? 0.2223 0.2810 0.2426 0.0259  0.0374  -0.0101 614  ARG B O   
13457 C CB  . ARG B 616  ? 0.2599 0.3308 0.2939 0.0265  0.0412  -0.0080 614  ARG B CB  
13458 C CG  . ARG B 616  ? 0.2713 0.3454 0.3125 0.0241  0.0406  -0.0062 614  ARG B CG  
13459 C CD  . ARG B 616  ? 0.3242 0.4047 0.3688 0.0233  0.0436  -0.0037 614  ARG B CD  
13460 N NE  . ARG B 616  ? 0.3735 0.4590 0.4200 0.0262  0.0458  -0.0046 614  ARG B NE  
13461 C CZ  . ARG B 616  ? 0.3760 0.4646 0.4281 0.0269  0.0453  -0.0052 614  ARG B CZ  
13462 N NH1 . ARG B 616  ? 0.3561 0.4434 0.4123 0.0249  0.0427  -0.0049 614  ARG B NH1 
13463 N NH2 . ARG B 616  ? 0.3597 0.4530 0.4132 0.0300  0.0475  -0.0061 614  ARG B NH2 
13464 N N   . ARG B 617  ? 0.2056 0.2659 0.2251 0.0305  0.0392  -0.0132 615  ARG B N   
13465 C CA  . ARG B 617  ? 0.2341 0.2904 0.2460 0.0315  0.0390  -0.0144 615  ARG B CA  
13466 C C   . ARG B 617  ? 0.2178 0.2686 0.2272 0.0300  0.0356  -0.0154 615  ARG B C   
13467 O O   . ARG B 617  ? 0.2348 0.2833 0.2398 0.0291  0.0349  -0.0151 615  ARG B O   
13468 C CB  . ARG B 617  ? 0.2777 0.3333 0.2862 0.0351  0.0403  -0.0169 615  ARG B CB  
13469 C CG  . ARG B 617  ? 0.2628 0.3141 0.2630 0.0361  0.0400  -0.0184 615  ARG B CG  
13470 C CD  . ARG B 617  ? 0.3369 0.3887 0.3335 0.0399  0.0423  -0.0202 615  ARG B CD  
13471 N NE  . ARG B 617  ? 0.4088 0.4574 0.4053 0.0419  0.0408  -0.0228 615  ARG B NE  
13472 C CZ  . ARG B 617  ? 0.4775 0.5196 0.4682 0.0426  0.0386  -0.0252 615  ARG B CZ  
13473 N NH1 . ARG B 617  ? 0.4545 0.4928 0.4392 0.0414  0.0374  -0.0255 615  ARG B NH1 
13474 N NH2 . ARG B 617  ? 0.5216 0.5606 0.5122 0.0444  0.0373  -0.0273 615  ARG B NH2 
13475 N N   . ALA B 618  ? 0.2042 0.2534 0.2166 0.0296  0.0335  -0.0165 616  ALA B N   
13476 C CA  . ALA B 618  ? 0.1879 0.2326 0.1984 0.0280  0.0304  -0.0173 616  ALA B CA  
13477 C C   . ALA B 618  ? 0.1870 0.2323 0.1987 0.0255  0.0296  -0.0151 616  ALA B C   
13478 O O   . ALA B 618  ? 0.1971 0.2396 0.2052 0.0245  0.0280  -0.0153 616  ALA B O   
13479 C CB  . ALA B 618  ? 0.1955 0.2388 0.2094 0.0280  0.0285  -0.0184 616  ALA B CB  
13480 N N   . VAL B 619  ? 0.2076 0.2564 0.2245 0.0243  0.0307  -0.0131 617  VAL B N   
13481 C CA  . VAL B 619  ? 0.1981 0.2467 0.2158 0.0221  0.0298  -0.0111 617  VAL B CA  
13482 C C   . VAL B 619  ? 0.2145 0.2628 0.2273 0.0222  0.0309  -0.0100 617  VAL B C   
13483 O O   . VAL B 619  ? 0.2234 0.2697 0.2340 0.0211  0.0294  -0.0095 617  VAL B O   
13484 C CB  . VAL B 619  ? 0.1998 0.2517 0.2237 0.0207  0.0305  -0.0091 617  VAL B CB  
13485 C CG1 . VAL B 619  ? 0.2444 0.2952 0.2685 0.0186  0.0295  -0.0071 617  VAL B CG1 
13486 C CG2 . VAL B 619  ? 0.2121 0.2639 0.2403 0.0206  0.0291  -0.0102 617  VAL B CG2 
13487 N N   . ARG B 620  ? 0.2240 0.2745 0.2350 0.0236  0.0335  -0.0099 618  ARG B N   
13488 C CA  . ARG B 620  ? 0.2386 0.2887 0.2442 0.0238  0.0346  -0.0090 618  ARG B CA  
13489 C C   . ARG B 620  ? 0.2108 0.2568 0.2105 0.0244  0.0326  -0.0109 618  ARG B C   
13490 O O   . ARG B 620  ? 0.2361 0.2805 0.2323 0.0236  0.0317  -0.0100 618  ARG B O   
13491 C CB  . ARG B 620  ? 0.2645 0.3181 0.2692 0.0254  0.0380  -0.0086 618  ARG B CB  
13492 C CG  . ARG B 620  ? 0.3653 0.4233 0.3749 0.0241  0.0401  -0.0058 618  ARG B CG  
13493 C CD  . ARG B 620  ? 0.4449 0.5071 0.4533 0.0255  0.0437  -0.0051 618  ARG B CD  
13494 N NE  . ARG B 620  ? 0.5168 0.5828 0.5298 0.0270  0.0451  -0.0060 618  ARG B NE  
13495 C CZ  . ARG B 620  ? 0.4192 0.4850 0.4299 0.0300  0.0459  -0.0085 618  ARG B CZ  
13496 N NH1 . ARG B 620  ? 0.4982 0.5602 0.5018 0.0316  0.0455  -0.0103 618  ARG B NH1 
13497 N NH2 . ARG B 620  ? 0.4565 0.5259 0.4718 0.0314  0.0470  -0.0091 618  ARG B NH2 
13498 N N   . LEU B 621  ? 0.2265 0.2704 0.2249 0.0258  0.0318  -0.0135 619  LEU B N   
13499 C CA  . LEU B 621  ? 0.2310 0.2707 0.2238 0.0259  0.0296  -0.0154 619  LEU B CA  
13500 C C   . LEU B 621  ? 0.2343 0.2725 0.2285 0.0238  0.0267  -0.0148 619  LEU B C   
13501 O O   . LEU B 621  ? 0.2388 0.2749 0.2288 0.0233  0.0252  -0.0150 619  LEU B O   
13502 C CB  . LEU B 621  ? 0.2471 0.2844 0.2387 0.0276  0.0290  -0.0181 619  LEU B CB  
13503 C CG  . LEU B 621  ? 0.2575 0.2957 0.2464 0.0303  0.0317  -0.0192 619  LEU B CG  
13504 C CD1 . LEU B 621  ? 0.2902 0.3256 0.2786 0.0321  0.0309  -0.0217 619  LEU B CD1 
13505 C CD2 . LEU B 621  ? 0.3355 0.3719 0.3170 0.0310  0.0322  -0.0195 619  LEU B CD2 
13506 N N   . ALA B 622  ? 0.2082 0.2474 0.2081 0.0227  0.0259  -0.0142 620  ALA B N   
13507 C CA  . ALA B 622  ? 0.2177 0.2559 0.2191 0.0210  0.0235  -0.0137 620  ALA B CA  
13508 C C   . ALA B 622  ? 0.2258 0.2649 0.2263 0.0201  0.0236  -0.0115 620  ALA B C   
13509 O O   . ALA B 622  ? 0.2021 0.2398 0.2005 0.0194  0.0217  -0.0114 620  ALA B O   
13510 C CB  . ALA B 622  ? 0.2281 0.2672 0.2355 0.0202  0.0228  -0.0136 620  ALA B CB  
13511 N N   . ALA B 623  ? 0.2172 0.2585 0.2192 0.0202  0.0259  -0.0096 621  ALA B N   
13512 C CA  . ALA B 623  ? 0.2258 0.2673 0.2266 0.0193  0.0260  -0.0073 621  ALA B CA  
13513 C C   . ALA B 623  ? 0.2335 0.2737 0.2278 0.0200  0.0257  -0.0076 621  ALA B C   
13514 O O   . ALA B 623  ? 0.2504 0.2895 0.2428 0.0194  0.0242  -0.0067 621  ALA B O   
13515 C CB  . ALA B 623  ? 0.2260 0.2702 0.2293 0.0190  0.0286  -0.0052 621  ALA B CB  
13516 N N   . ASP B 624  ? 0.2442 0.2842 0.2349 0.0214  0.0271  -0.0090 622  ASP B N   
13517 C CA  . ASP B 624  ? 0.2550 0.2934 0.2390 0.0220  0.0267  -0.0095 622  ASP B CA  
13518 C C   . ASP B 624  ? 0.2832 0.3191 0.2652 0.0214  0.0235  -0.0108 622  ASP B C   
13519 O O   . ASP B 624  ? 0.3505 0.3857 0.3287 0.0211  0.0223  -0.0101 622  ASP B O   
13520 C CB  . ASP B 624  ? 0.3479 0.3859 0.3282 0.0239  0.0285  -0.0113 622  ASP B CB  
13521 C CG  . ASP B 624  ? 0.4249 0.4661 0.4066 0.0247  0.0321  -0.0099 622  ASP B CG  
13522 O OD1 . ASP B 624  ? 0.4638 0.5070 0.4477 0.0236  0.0331  -0.0073 622  ASP B OD1 
13523 O OD2 . ASP B 624  ? 0.4609 0.5025 0.4413 0.0265  0.0337  -0.0115 622  ASP B OD2 
13524 N N   . ALA B 625  ? 0.2997 0.3347 0.2842 0.0210  0.0220  -0.0125 623  ALA B N   
13525 C CA  . ALA B 625  ? 0.3475 0.3809 0.3306 0.0202  0.0190  -0.0138 623  ALA B CA  
13526 C C   . ALA B 625  ? 0.2999 0.3343 0.2868 0.0189  0.0172  -0.0125 623  ALA B C   
13527 O O   . ALA B 625  ? 0.3077 0.3415 0.2938 0.0181  0.0148  -0.0132 623  ALA B O   
13528 C CB  . ALA B 625  ? 0.4175 0.4490 0.4011 0.0203  0.0182  -0.0161 623  ALA B CB  
13529 N N   . ALA B 626  ? 0.2642 0.3002 0.2552 0.0187  0.0184  -0.0106 624  ALA B N   
13530 C CA  . ALA B 626  ? 0.2433 0.2799 0.2379 0.0178  0.0167  -0.0096 624  ALA B CA  
13531 C C   . ALA B 626  ? 0.2424 0.2789 0.2341 0.0176  0.0148  -0.0089 624  ALA B C   
13532 O O   . ALA B 626  ? 0.2461 0.2830 0.2394 0.0170  0.0126  -0.0095 624  ALA B O   
13533 C CB  . ALA B 626  ? 0.2356 0.2732 0.2343 0.0175  0.0182  -0.0076 624  ALA B CB  
13534 N N   . PRO B 627  ? 0.2544 0.2906 0.2418 0.0181  0.0153  -0.0078 625  PRO B N   
13535 C CA  . PRO B 627  ? 0.2551 0.2914 0.2401 0.0180  0.0131  -0.0072 625  PRO B CA  
13536 C C   . PRO B 627  ? 0.2599 0.2961 0.2428 0.0175  0.0108  -0.0092 625  PRO B C   
13537 O O   . PRO B 627  ? 0.2608 0.2982 0.2446 0.0171  0.0086  -0.0090 625  PRO B O   
13538 C CB  . PRO B 627  ? 0.2969 0.3327 0.2772 0.0187  0.0143  -0.0057 625  PRO B CB  
13539 C CG  . PRO B 627  ? 0.3262 0.3621 0.3081 0.0189  0.0173  -0.0048 625  PRO B CG  
13540 C CD  . PRO B 627  ? 0.2767 0.3129 0.2618 0.0188  0.0179  -0.0067 625  PRO B CD  
13541 N N   . ASP B 628  ? 0.2440 0.2788 0.2242 0.0176  0.0113  -0.0111 626  ASP B N   
13542 C CA  . ASP B 628  ? 0.2720 0.3061 0.2497 0.0167  0.0090  -0.0129 626  ASP B CA  
13543 C C   . ASP B 628  ? 0.2667 0.3017 0.2488 0.0156  0.0074  -0.0137 626  ASP B C   
13544 O O   . ASP B 628  ? 0.2791 0.3150 0.2608 0.0146  0.0050  -0.0142 626  ASP B O   
13545 C CB  . ASP B 628  ? 0.3030 0.3346 0.2764 0.0171  0.0098  -0.0149 626  ASP B CB  
13546 C CG  . ASP B 628  ? 0.3789 0.4095 0.3465 0.0182  0.0109  -0.0144 626  ASP B CG  
13547 O OD1 . ASP B 628  ? 0.4035 0.4351 0.3694 0.0182  0.0101  -0.0129 626  ASP B OD1 
13548 O OD2 . ASP B 628  ? 0.4569 0.4858 0.4217 0.0192  0.0126  -0.0155 626  ASP B OD2 
13549 N N   . TRP B 629  ? 0.2340 0.2691 0.2205 0.0157  0.0087  -0.0137 627  TRP B N   
13550 C CA  . TRP B 629  ? 0.2247 0.2606 0.2151 0.0146  0.0074  -0.0144 627  TRP B CA  
13551 C C   . TRP B 629  ? 0.2144 0.2528 0.2080 0.0145  0.0063  -0.0129 627  TRP B C   
13552 O O   . TRP B 629  ? 0.2116 0.2516 0.2067 0.0136  0.0044  -0.0133 627  TRP B O   
13553 C CB  . TRP B 629  ? 0.2057 0.2407 0.1994 0.0148  0.0089  -0.0150 627  TRP B CB  
13554 C CG  . TRP B 629  ? 0.1812 0.2169 0.1786 0.0138  0.0076  -0.0156 627  TRP B CG  
13555 C CD1 . TRP B 629  ? 0.2072 0.2439 0.2094 0.0138  0.0081  -0.0149 627  TRP B CD1 
13556 C CD2 . TRP B 629  ? 0.2150 0.2502 0.2114 0.0124  0.0056  -0.0170 627  TRP B CD2 
13557 N NE1 . TRP B 629  ? 0.1921 0.2291 0.1962 0.0127  0.0066  -0.0158 627  TRP B NE1 
13558 C CE2 . TRP B 629  ? 0.1981 0.2344 0.1989 0.0117  0.0051  -0.0169 627  TRP B CE2 
13559 C CE3 . TRP B 629  ? 0.2268 0.2607 0.2189 0.0115  0.0040  -0.0181 627  TRP B CE3 
13560 C CZ2 . TRP B 629  ? 0.1933 0.2296 0.1943 0.0101  0.0033  -0.0179 627  TRP B CZ2 
13561 C CZ3 . TRP B 629  ? 0.2230 0.2569 0.2156 0.0097  0.0021  -0.0191 627  TRP B CZ3 
13562 C CH2 . TRP B 629  ? 0.2226 0.2578 0.2196 0.0090  0.0018  -0.0189 627  TRP B CH2 
13563 N N   . ALA B 630  ? 0.2174 0.2563 0.2119 0.0155  0.0075  -0.0111 628  ALA B N   
13564 C CA  . ALA B 630  ? 0.2234 0.2640 0.2203 0.0158  0.0065  -0.0097 628  ALA B CA  
13565 C C   . ALA B 630  ? 0.2400 0.2822 0.2344 0.0157  0.0043  -0.0095 628  ALA B C   
13566 O O   . ALA B 630  ? 0.2603 0.3047 0.2570 0.0159  0.0028  -0.0091 628  ALA B O   
13567 C CB  . ALA B 630  ? 0.2639 0.3037 0.2611 0.0168  0.0081  -0.0077 628  ALA B CB  
13568 N N   . ALA B 631  ? 0.2252 0.2665 0.2148 0.0156  0.0040  -0.0100 629  ALA B N   
13569 C CA  . ALA B 631  ? 0.2247 0.2677 0.2117 0.0154  0.0017  -0.0099 629  ALA B CA  
13570 C C   . ALA B 631  ? 0.2592 0.3037 0.2469 0.0138  -0.0003 -0.0115 629  ALA B C   
13571 O O   . ALA B 631  ? 0.2731 0.3201 0.2599 0.0134  -0.0025 -0.0112 629  ALA B O   
13572 C CB  . ALA B 631  ? 0.2640 0.3052 0.2452 0.0158  0.0021  -0.0098 629  ALA B CB  
13573 N N   . VAL B 632  ? 0.2365 0.2798 0.2258 0.0128  0.0002  -0.0129 630  VAL B N   
13574 C CA  . VAL B 632  ? 0.2268 0.2715 0.2171 0.0110  -0.0018 -0.0141 630  VAL B CA  
13575 C C   . VAL B 632  ? 0.2286 0.2771 0.2237 0.0111  -0.0026 -0.0132 630  VAL B C   
13576 O O   . VAL B 632  ? 0.2271 0.2754 0.2257 0.0120  -0.0012 -0.0126 630  VAL B O   
13577 C CB  . VAL B 632  ? 0.2276 0.2695 0.2182 0.0101  -0.0010 -0.0157 630  VAL B CB  
13578 C CG1 . VAL B 632  ? 0.2459 0.2891 0.2375 0.0079  -0.0031 -0.0167 630  VAL B CG1 
13579 C CG2 . VAL B 632  ? 0.2459 0.2840 0.2315 0.0104  -0.0002 -0.0168 630  VAL B CG2 
13580 N N   . PRO B 633  ? 0.2195 0.2716 0.2150 0.0103  -0.0048 -0.0130 631  PRO B N   
13581 C CA  . PRO B 633  ? 0.2159 0.2720 0.2157 0.0110  -0.0054 -0.0121 631  PRO B CA  
13582 C C   . PRO B 633  ? 0.2093 0.2653 0.2129 0.0103  -0.0046 -0.0127 631  PRO B C   
13583 O O   . PRO B 633  ? 0.2085 0.2628 0.2115 0.0085  -0.0046 -0.0140 631  PRO B O   
13584 C CB  . PRO B 633  ? 0.2297 0.2900 0.2291 0.0097  -0.0080 -0.0121 631  PRO B CB  
13585 C CG  . PRO B 633  ? 0.2703 0.3284 0.2644 0.0092  -0.0087 -0.0125 631  PRO B CG  
13586 C CD  . PRO B 633  ? 0.2278 0.2805 0.2195 0.0090  -0.0069 -0.0136 631  PRO B CD  
13587 N N   . PRO B 634  ? 0.2016 0.2592 0.2088 0.0117  -0.0039 -0.0118 632  PRO B N   
13588 C CA  . PRO B 634  ? 0.2031 0.2608 0.2137 0.0111  -0.0033 -0.0124 632  PRO B CA  
13589 C C   . PRO B 634  ? 0.1972 0.2572 0.2086 0.0088  -0.0046 -0.0134 632  PRO B C   
13590 O O   . PRO B 634  ? 0.1975 0.2553 0.2095 0.0076  -0.0040 -0.0143 632  PRO B O   
13591 C CB  . PRO B 634  ? 0.2235 0.2834 0.2372 0.0132  -0.0030 -0.0114 632  PRO B CB  
13592 C CG  . PRO B 634  ? 0.2708 0.3292 0.2825 0.0150  -0.0027 -0.0101 632  PRO B CG  
13593 C CD  . PRO B 634  ? 0.2111 0.2695 0.2189 0.0141  -0.0037 -0.0103 632  PRO B CD  
13594 N N   . SER B 635  ? 0.2177 0.2820 0.2291 0.0080  -0.0064 -0.0131 633  SER B N   
13595 C CA  . SER B 635  ? 0.2229 0.2894 0.2351 0.0053  -0.0077 -0.0139 633  SER B CA  
13596 C C   . SER B 635  ? 0.2004 0.2625 0.2090 0.0032  -0.0080 -0.0151 633  SER B C   
13597 O O   . SER B 635  ? 0.2079 0.2694 0.2170 0.0010  -0.0084 -0.0158 633  SER B O   
13598 C CB  . SER B 635  ? 0.2564 0.3289 0.2693 0.0048  -0.0097 -0.0132 633  SER B CB  
13599 O OG  . SER B 635  ? 0.3695 0.4412 0.3788 0.0047  -0.0108 -0.0131 633  SER B OG  
13600 N N   . GLU B 636  ? 0.2102 0.2691 0.2149 0.0037  -0.0079 -0.0153 634  GLU B N   
13601 C CA  . GLU B 636  ? 0.2040 0.2582 0.2048 0.0021  -0.0082 -0.0167 634  GLU B CA  
13602 C C   . GLU B 636  ? 0.2101 0.2598 0.2113 0.0029  -0.0062 -0.0174 634  GLU B C   
13603 O O   . GLU B 636  ? 0.2079 0.2544 0.2076 0.0014  -0.0064 -0.0185 634  GLU B O   
13604 C CB  . GLU B 636  ? 0.2326 0.2848 0.2286 0.0026  -0.0087 -0.0169 634  GLU B CB  
13605 C CG  . GLU B 636  ? 0.3546 0.4014 0.3460 0.0013  -0.0090 -0.0185 634  GLU B CG  
13606 C CD  . GLU B 636  ? 0.4464 0.4928 0.4377 -0.0017 -0.0106 -0.0195 634  GLU B CD  
13607 O OE1 . GLU B 636  ? 0.4162 0.4669 0.4087 -0.0037 -0.0126 -0.0190 634  GLU B OE1 
13608 O OE2 . GLU B 636  ? 0.3813 0.4233 0.3716 -0.0022 -0.0100 -0.0205 634  GLU B OE2 
13609 N N   . ARG B 637  ? 0.1825 0.2319 0.1857 0.0052  -0.0043 -0.0166 635  ARG B N   
13610 C CA  . ARG B 637  ? 0.1919 0.2381 0.1964 0.0058  -0.0026 -0.0171 635  ARG B CA  
13611 C C   . ARG B 637  ? 0.1846 0.2319 0.1921 0.0044  -0.0030 -0.0174 635  ARG B C   
13612 O O   . ARG B 637  ? 0.1901 0.2341 0.1970 0.0036  -0.0028 -0.0184 635  ARG B O   
13613 C CB  . ARG B 637  ? 0.1773 0.2234 0.1837 0.0081  -0.0008 -0.0160 635  ARG B CB  
13614 C CG  . ARG B 637  ? 0.1959 0.2412 0.1992 0.0094  -0.0003 -0.0154 635  ARG B CG  
13615 C CD  . ARG B 637  ? 0.1964 0.2406 0.2012 0.0112  0.0017  -0.0144 635  ARG B CD  
13616 N NE  . ARG B 637  ? 0.2008 0.2473 0.2093 0.0120  0.0017  -0.0133 635  ARG B NE  
13617 C CZ  . ARG B 637  ? 0.2091 0.2564 0.2176 0.0134  0.0018  -0.0119 635  ARG B CZ  
13618 N NH1 . ARG B 637  ? 0.2749 0.3217 0.2800 0.0140  0.0018  -0.0112 635  ARG B NH1 
13619 N NH2 . ARG B 637  ? 0.2050 0.2534 0.2166 0.0144  0.0020  -0.0111 635  ARG B NH2 
13620 N N   . ALA B 638  ? 0.1642 0.2159 0.1745 0.0042  -0.0038 -0.0166 636  ALA B N   
13621 C CA  . ALA B 638  ? 0.1725 0.2258 0.1854 0.0028  -0.0042 -0.0168 636  ALA B CA  
13622 C C   . ALA B 638  ? 0.1721 0.2243 0.1828 0.0000  -0.0056 -0.0177 636  ALA B C   
13623 O O   . ALA B 638  ? 0.1670 0.2175 0.1783 -0.0013 -0.0056 -0.0182 636  ALA B O   
13624 C CB  . ALA B 638  ? 0.1931 0.2521 0.2092 0.0034  -0.0046 -0.0158 636  ALA B CB  
13625 N N   . ALA B 639  ? 0.1858 0.2385 0.1936 -0.0012 -0.0071 -0.0178 637  ALA B N   
13626 C CA  . ALA B 639  ? 0.1917 0.2426 0.1968 -0.0042 -0.0088 -0.0187 637  ALA B CA  
13627 C C   . ALA B 639  ? 0.1768 0.2210 0.1790 -0.0043 -0.0082 -0.0199 637  ALA B C   
13628 O O   . ALA B 639  ? 0.1838 0.2255 0.1847 -0.0065 -0.0091 -0.0206 637  ALA B O   
13629 C CB  . ALA B 639  ? 0.1974 0.2499 0.1998 -0.0054 -0.0106 -0.0187 637  ALA B CB  
13630 N N   . CYS B 640  ? 0.1765 0.2177 0.1774 -0.0019 -0.0067 -0.0202 638  CYS B N   
13631 C CA  . CYS B 640  ? 0.1807 0.2162 0.1794 -0.0013 -0.0058 -0.0214 638  CYS B CA  
13632 C C   . CYS B 640  ? 0.1724 0.2073 0.1742 -0.0014 -0.0051 -0.0213 638  CYS B C   
13633 O O   . CYS B 640  ? 0.1809 0.2118 0.1809 -0.0025 -0.0056 -0.0222 638  CYS B O   
13634 C CB  . CYS B 640  ? 0.1717 0.2055 0.1695 0.0015  -0.0039 -0.0214 638  CYS B CB  
13635 S SG  . CYS B 640  ? 0.2102 0.2432 0.2031 0.0019  -0.0045 -0.0217 638  CYS B SG  
13636 N N   . LEU B 641  ? 0.1626 0.2011 0.1687 -0.0002 -0.0041 -0.0203 639  LEU B N   
13637 C CA  . LEU B 641  ? 0.1758 0.2138 0.1846 -0.0003 -0.0035 -0.0202 639  LEU B CA  
13638 C C   . LEU B 641  ? 0.1689 0.2075 0.1775 -0.0032 -0.0051 -0.0203 639  LEU B C   
13639 O O   . LEU B 641  ? 0.1716 0.2070 0.1796 -0.0040 -0.0053 -0.0208 639  LEU B O   
13640 C CB  . LEU B 641  ? 0.1657 0.2075 0.1786 0.0013  -0.0024 -0.0192 639  LEU B CB  
13641 C CG  . LEU B 641  ? 0.1746 0.2149 0.1888 0.0037  -0.0006 -0.0190 639  LEU B CG  
13642 C CD1 . LEU B 641  ? 0.2084 0.2474 0.2201 0.0050  0.0000  -0.0190 639  LEU B CD1 
13643 C CD2 . LEU B 641  ? 0.1665 0.2100 0.1844 0.0049  0.0000  -0.0180 639  LEU B CD2 
13644 N N   . ASP B 642  ? 0.1534 0.1963 0.1623 -0.0048 -0.0063 -0.0197 640  ASP B N   
13645 C CA  . ASP B 642  ? 0.1627 0.2069 0.1715 -0.0079 -0.0078 -0.0196 640  ASP B CA  
13646 C C   . ASP B 642  ? 0.1549 0.1934 0.1592 -0.0100 -0.0091 -0.0206 640  ASP B C   
13647 O O   . ASP B 642  ? 0.1855 0.2219 0.1892 -0.0120 -0.0098 -0.0207 640  ASP B O   
13648 C CB  . ASP B 642  ? 0.1758 0.2263 0.1860 -0.0091 -0.0089 -0.0187 640  ASP B CB  
13649 C CG  . ASP B 642  ? 0.2073 0.2634 0.2220 -0.0076 -0.0078 -0.0177 640  ASP B CG  
13650 O OD1 . ASP B 642  ? 0.1932 0.2483 0.2097 -0.0066 -0.0067 -0.0177 640  ASP B OD1 
13651 O OD2 . ASP B 642  ? 0.2154 0.2770 0.2317 -0.0074 -0.0083 -0.0170 640  ASP B OD2 
13652 N N   . ARG B 643  ? 0.1725 0.2080 0.1732 -0.0095 -0.0095 -0.0214 641  ARG B N   
13653 C CA  . ARG B 643  ? 0.1885 0.2177 0.1844 -0.0111 -0.0108 -0.0226 641  ARG B CA  
13654 C C   . ARG B 643  ? 0.1853 0.2093 0.1807 -0.0097 -0.0098 -0.0233 641  ARG B C   
13655 O O   . ARG B 643  ? 0.2029 0.2223 0.1957 -0.0114 -0.0109 -0.0239 641  ARG B O   
13656 C CB  . ARG B 643  ? 0.1940 0.2210 0.1858 -0.0103 -0.0113 -0.0235 641  ARG B CB  
13657 C CG  . ARG B 643  ? 0.2216 0.2521 0.2124 -0.0129 -0.0134 -0.0231 641  ARG B CG  
13658 C CD  . ARG B 643  ? 0.2647 0.2918 0.2503 -0.0125 -0.0142 -0.0241 641  ARG B CD  
13659 N NE  . ARG B 643  ? 0.2581 0.2861 0.2442 -0.0090 -0.0123 -0.0240 641  ARG B NE  
13660 C CZ  . ARG B 643  ? 0.2489 0.2819 0.2366 -0.0081 -0.0122 -0.0231 641  ARG B CZ  
13661 N NH1 . ARG B 643  ? 0.2572 0.2955 0.2466 -0.0102 -0.0139 -0.0222 641  ARG B NH1 
13662 N NH2 . ARG B 643  ? 0.2644 0.2973 0.2521 -0.0050 -0.0104 -0.0229 641  ARG B NH2 
13663 N N   . ALA B 644  ? 0.1682 0.1926 0.1659 -0.0065 -0.0078 -0.0233 642  ALA B N   
13664 C CA  . ALA B 644  ? 0.1862 0.2063 0.1839 -0.0050 -0.0068 -0.0239 642  ALA B CA  
13665 C C   . ALA B 644  ? 0.1890 0.2096 0.1888 -0.0067 -0.0073 -0.0233 642  ALA B C   
13666 O O   . ALA B 644  ? 0.1840 0.1997 0.1820 -0.0070 -0.0078 -0.0239 642  ALA B O   
13667 C CB  . ALA B 644  ? 0.1802 0.2019 0.1807 -0.0017 -0.0046 -0.0236 642  ALA B CB  
13668 N N   . ALA B 645  ? 0.1766 0.2029 0.1800 -0.0075 -0.0072 -0.0221 643  ALA B N   
13669 C CA  . ALA B 645  ? 0.1941 0.2212 0.1992 -0.0091 -0.0075 -0.0215 643  ALA B CA  
13670 C C   . ALA B 645  ? 0.1708 0.1950 0.1726 -0.0125 -0.0095 -0.0216 643  ALA B C   
13671 O O   . ALA B 645  ? 0.1942 0.2153 0.1953 -0.0135 -0.0099 -0.0216 643  ALA B O   
13672 C CB  . ALA B 645  ? 0.1778 0.2119 0.1871 -0.0091 -0.0070 -0.0203 643  ALA B CB  
13673 N N   . GLU B 646  ? 0.1837 0.2088 0.1833 -0.0145 -0.0108 -0.0217 644  GLU B N   
13674 C CA  . GLU B 646  ? 0.2042 0.2261 0.2003 -0.0182 -0.0129 -0.0218 644  GLU B CA  
13675 C C   . GLU B 646  ? 0.2016 0.2148 0.1932 -0.0177 -0.0135 -0.0231 644  GLU B C   
13676 O O   . GLU B 646  ? 0.2204 0.2296 0.2098 -0.0200 -0.0147 -0.0230 644  GLU B O   
13677 C CB  . GLU B 646  ? 0.2460 0.2699 0.2402 -0.0202 -0.0144 -0.0219 644  GLU B CB  
13678 C CG  . GLU B 646  ? 0.3084 0.3411 0.3067 -0.0211 -0.0143 -0.0205 644  GLU B CG  
13679 C CD  . GLU B 646  ? 0.3803 0.4165 0.3809 -0.0238 -0.0147 -0.0193 644  GLU B CD  
13680 O OE1 . GLU B 646  ? 0.4627 0.4954 0.4605 -0.0271 -0.0162 -0.0193 644  GLU B OE1 
13681 O OE2 . GLU B 646  ? 0.4083 0.4507 0.4134 -0.0225 -0.0133 -0.0184 644  GLU B OE2 
13682 N N   . LEU B 647  ? 0.2112 0.2213 0.2013 -0.0146 -0.0126 -0.0242 645  LEU B N   
13683 C CA  . LEU B 647  ? 0.2289 0.2310 0.2147 -0.0135 -0.0130 -0.0256 645  LEU B CA  
13684 C C   . LEU B 647  ? 0.2219 0.2220 0.2095 -0.0122 -0.0122 -0.0253 645  LEU B C   
13685 O O   . LEU B 647  ? 0.2310 0.2251 0.2153 -0.0132 -0.0134 -0.0258 645  LEU B O   
13686 C CB  . LEU B 647  ? 0.2147 0.2152 0.1989 -0.0103 -0.0119 -0.0267 645  LEU B CB  
13687 C CG  . LEU B 647  ? 0.2434 0.2444 0.2245 -0.0113 -0.0129 -0.0272 645  LEU B CG  
13688 C CD1 . LEU B 647  ? 0.2407 0.2399 0.2201 -0.0077 -0.0114 -0.0283 645  LEU B CD1 
13689 C CD2 . LEU B 647  ? 0.2854 0.2808 0.2611 -0.0147 -0.0155 -0.0279 645  LEU B CD2 
13690 N N   . MET B 648  ? 0.1819 0.1868 0.1744 -0.0102 -0.0104 -0.0246 646  MET B N   
13691 C CA  . MET B 648  ? 0.1928 0.1962 0.1871 -0.0090 -0.0098 -0.0243 646  MET B CA  
13692 C C   . MET B 648  ? 0.2023 0.2054 0.1963 -0.0123 -0.0112 -0.0234 646  MET B C   
13693 O O   . MET B 648  ? 0.2260 0.2246 0.2186 -0.0124 -0.0117 -0.0235 646  MET B O   
13694 C CB  . MET B 648  ? 0.1988 0.2078 0.1985 -0.0067 -0.0079 -0.0237 646  MET B CB  
13695 C CG  . MET B 648  ? 0.2333 0.2420 0.2335 -0.0033 -0.0064 -0.0244 646  MET B CG  
13696 S SD  . MET B 648  ? 0.2325 0.2455 0.2384 -0.0010 -0.0045 -0.0236 646  MET B SD  
13697 C CE  . MET B 648  ? 0.2556 0.2686 0.2617 0.0022  -0.0028 -0.0243 646  MET B CE  
13698 N N   . GLN B 649  ? 0.1878 0.1960 0.1830 -0.0150 -0.0117 -0.0224 647  GLN B N   
13699 C CA  . GLN B 649  ? 0.1914 0.1999 0.1863 -0.0184 -0.0128 -0.0214 647  GLN B CA  
13700 C C   . GLN B 649  ? 0.2159 0.2169 0.2052 -0.0209 -0.0149 -0.0218 647  GLN B C   
13701 O O   . GLN B 649  ? 0.2409 0.2381 0.2287 -0.0222 -0.0156 -0.0214 647  GLN B O   
13702 C CB  . GLN B 649  ? 0.1941 0.2101 0.1914 -0.0207 -0.0129 -0.0203 647  GLN B CB  
13703 C CG  . GLN B 649  ? 0.2167 0.2346 0.2144 -0.0242 -0.0136 -0.0189 647  GLN B CG  
13704 C CD  . GLN B 649  ? 0.1954 0.2157 0.1963 -0.0227 -0.0122 -0.0183 647  GLN B CD  
13705 O OE1 . GLN B 649  ? 0.2164 0.2431 0.2213 -0.0212 -0.0109 -0.0178 647  GLN B OE1 
13706 N NE2 . GLN B 649  ? 0.2228 0.2374 0.2217 -0.0226 -0.0126 -0.0184 647  GLN B NE2 
13707 N N   . ALA B 650  ? 0.2204 0.2188 0.2063 -0.0216 -0.0160 -0.0227 648  ALA B N   
13708 C CA  . ALA B 650  ? 0.2327 0.2234 0.2129 -0.0242 -0.0182 -0.0233 648  ALA B CA  
13709 C C   . ALA B 650  ? 0.2583 0.2409 0.2354 -0.0215 -0.0182 -0.0245 648  ALA B C   
13710 O O   . ALA B 650  ? 0.2907 0.2666 0.2637 -0.0233 -0.0199 -0.0245 648  ALA B O   
13711 C CB  . ALA B 650  ? 0.2721 0.2618 0.2490 -0.0253 -0.0194 -0.0242 648  ALA B CB  
13712 N N   . ARG B 651  ? 0.2358 0.2192 0.2150 -0.0171 -0.0164 -0.0253 649  ARG B N   
13713 C CA  . ARG B 651  ? 0.2358 0.2125 0.2127 -0.0140 -0.0163 -0.0264 649  ARG B CA  
13714 C C   . ARG B 651  ? 0.2330 0.2110 0.2134 -0.0124 -0.0153 -0.0257 649  ARG B C   
13715 O O   . ARG B 651  ? 0.2417 0.2157 0.2214 -0.0093 -0.0149 -0.0265 649  ARG B O   
13716 C CB  . ARG B 651  ? 0.2547 0.2313 0.2314 -0.0103 -0.0149 -0.0278 649  ARG B CB  
13717 C CG  . ARG B 651  ? 0.2761 0.2505 0.2484 -0.0120 -0.0162 -0.0287 649  ARG B CG  
13718 C CD  . ARG B 651  ? 0.2639 0.2396 0.2361 -0.0086 -0.0146 -0.0299 649  ARG B CD  
13719 N NE  . ARG B 651  ? 0.2986 0.2732 0.2669 -0.0106 -0.0159 -0.0305 649  ARG B NE  
13720 C CZ  . ARG B 651  ? 0.2832 0.2588 0.2504 -0.0085 -0.0150 -0.0314 649  ARG B CZ  
13721 N NH1 . ARG B 651  ? 0.2706 0.2482 0.2402 -0.0045 -0.0126 -0.0318 649  ARG B NH1 
13722 N NH2 . ARG B 651  ? 0.2816 0.2560 0.2449 -0.0107 -0.0165 -0.0319 649  ARG B NH2 
13723 N N   . MET B 652  ? 0.2300 0.2135 0.2140 -0.0143 -0.0149 -0.0242 650  MET B N   
13724 C CA  . MET B 652  ? 0.2211 0.2060 0.2083 -0.0129 -0.0141 -0.0234 650  MET B CA  
13725 C C   . MET B 652  ? 0.2363 0.2135 0.2200 -0.0123 -0.0154 -0.0237 650  MET B C   
13726 O O   . MET B 652  ? 0.2401 0.2168 0.2257 -0.0091 -0.0145 -0.0240 650  MET B O   
13727 C CB  . MET B 652  ? 0.2173 0.2083 0.2075 -0.0156 -0.0139 -0.0218 650  MET B CB  
13728 C CG  . MET B 652  ? 0.2133 0.2053 0.2061 -0.0143 -0.0132 -0.0212 650  MET B CG  
13729 S SD  . MET B 652  ? 0.2562 0.2553 0.2520 -0.0172 -0.0128 -0.0194 650  MET B SD  
13730 C CE  . MET B 652  ? 0.2184 0.2254 0.2191 -0.0150 -0.0108 -0.0197 650  MET B CE  
13731 N N   . PRO B 653  ? 0.2316 0.2025 0.2102 -0.0151 -0.0174 -0.0237 651  PRO B N   
13732 C CA  . PRO B 653  ? 0.2657 0.2289 0.2409 -0.0142 -0.0187 -0.0239 651  PRO B CA  
13733 C C   . PRO B 653  ? 0.2635 0.2227 0.2377 -0.0095 -0.0182 -0.0255 651  PRO B C   
13734 O O   . PRO B 653  ? 0.2727 0.2299 0.2478 -0.0070 -0.0181 -0.0256 651  PRO B O   
13735 C CB  . PRO B 653  ? 0.2665 0.2235 0.2359 -0.0183 -0.0211 -0.0236 651  PRO B CB  
13736 C CG  . PRO B 653  ? 0.2650 0.2290 0.2366 -0.0223 -0.0209 -0.0223 651  PRO B CG  
13737 C CD  . PRO B 653  ? 0.2453 0.2164 0.2214 -0.0197 -0.0189 -0.0230 651  PRO B CD  
13738 N N   . THR B 654  ? 0.2496 0.2081 0.2222 -0.0083 -0.0178 -0.0269 652  THR B N   
13739 C CA  . THR B 654  ? 0.2532 0.2087 0.2251 -0.0037 -0.0170 -0.0285 652  THR B CA  
13740 C C   . THR B 654  ? 0.2725 0.2350 0.2508 -0.0005 -0.0146 -0.0283 652  THR B C   
13741 O O   . THR B 654  ? 0.2596 0.2206 0.2389 0.0030  -0.0141 -0.0287 652  THR B O   
13742 C CB  . THR B 654  ? 0.2721 0.2257 0.2405 -0.0034 -0.0170 -0.0299 652  THR B CB  
13743 O OG1 . THR B 654  ? 0.3081 0.2544 0.2702 -0.0066 -0.0195 -0.0302 652  THR B OG1 
13744 C CG2 . THR B 654  ? 0.2943 0.2455 0.2620 0.0016  -0.0159 -0.0316 652  THR B CG2 
13745 N N   . LEU B 655  ? 0.2401 0.2103 0.2227 -0.0015 -0.0133 -0.0275 653  LEU B N   
13746 C CA  . LEU B 655  ? 0.2343 0.2109 0.2228 0.0011  -0.0112 -0.0271 653  LEU B CA  
13747 C C   . LEU B 655  ? 0.2482 0.2247 0.2390 0.0016  -0.0115 -0.0263 653  LEU B C   
13748 O O   . LEU B 655  ? 0.2347 0.2128 0.2286 0.0048  -0.0104 -0.0265 653  LEU B O   
13749 C CB  . LEU B 655  ? 0.2324 0.2162 0.2244 -0.0006 -0.0101 -0.0262 653  LEU B CB  
13750 C CG  . LEU B 655  ? 0.2516 0.2362 0.2417 -0.0011 -0.0099 -0.0269 653  LEU B CG  
13751 C CD1 . LEU B 655  ? 0.2539 0.2457 0.2475 -0.0026 -0.0090 -0.0259 653  LEU B CD1 
13752 C CD2 . LEU B 655  ? 0.2744 0.2580 0.2642 0.0027  -0.0085 -0.0281 653  LEU B CD2 
13753 N N   . LEU B 656  ? 0.2549 0.2298 0.2442 -0.0014 -0.0129 -0.0253 654  LEU B N   
13754 C CA  . LEU B 656  ? 0.2518 0.2262 0.2426 -0.0011 -0.0134 -0.0244 654  LEU B CA  
13755 C C   . LEU B 656  ? 0.2440 0.2127 0.2329 0.0021  -0.0141 -0.0253 654  LEU B C   
13756 O O   . LEU B 656  ? 0.2656 0.2360 0.2577 0.0044  -0.0136 -0.0251 654  LEU B O   
13757 C CB  . LEU B 656  ? 0.2947 0.2668 0.2827 -0.0050 -0.0150 -0.0232 654  LEU B CB  
13758 C CG  . LEU B 656  ? 0.3114 0.2890 0.3008 -0.0085 -0.0146 -0.0222 654  LEU B CG  
13759 C CD1 . LEU B 656  ? 0.3121 0.2876 0.2991 -0.0120 -0.0160 -0.0208 654  LEU B CD1 
13760 C CD2 . LEU B 656  ? 0.2892 0.2744 0.2843 -0.0071 -0.0127 -0.0218 654  LEU B CD2 
13761 N N   . GLY B 657  ? 0.2639 0.2257 0.2475 0.0021  -0.0153 -0.0262 655  GLY B N   
13762 C CA  . GLY B 657  ? 0.2796 0.2355 0.2610 0.0055  -0.0161 -0.0272 655  GLY B CA  
13763 C C   . GLY B 657  ? 0.2790 0.2388 0.2644 0.0098  -0.0142 -0.0280 655  GLY B C   
13764 O O   . GLY B 657  ? 0.2820 0.2414 0.2692 0.0127  -0.0143 -0.0281 655  GLY B O   
13765 N N   . LEU B 658  ? 0.2481 0.2122 0.2352 0.0103  -0.0125 -0.0286 656  LEU B N   
13766 C CA  . LEU B 658  ? 0.2356 0.2041 0.2268 0.0141  -0.0105 -0.0292 656  LEU B CA  
13767 C C   . LEU B 658  ? 0.2379 0.2128 0.2353 0.0144  -0.0096 -0.0280 656  LEU B C   
13768 O O   . LEU B 658  ? 0.2312 0.2076 0.2316 0.0175  -0.0091 -0.0282 656  LEU B O   
13769 C CB  . LEU B 658  ? 0.2439 0.2153 0.2350 0.0142  -0.0090 -0.0298 656  LEU B CB  
13770 C CG  . LEU B 658  ? 0.2250 0.2007 0.2197 0.0179  -0.0068 -0.0304 656  LEU B CG  
13771 C CD1 . LEU B 658  ? 0.2288 0.2001 0.2216 0.0218  -0.0070 -0.0316 656  LEU B CD1 
13772 C CD2 . LEU B 658  ? 0.2394 0.2173 0.2331 0.0176  -0.0054 -0.0309 656  LEU B CD2 
13773 N N   . ILE B 659  ? 0.2049 0.1837 0.2044 0.0114  -0.0095 -0.0269 657  ILE B N   
13774 C CA  . ILE B 659  ? 0.2034 0.1879 0.2083 0.0116  -0.0087 -0.0259 657  ILE B CA  
13775 C C   . ILE B 659  ? 0.2020 0.1838 0.2070 0.0123  -0.0101 -0.0254 657  ILE B C   
13776 O O   . ILE B 659  ? 0.2109 0.1960 0.2201 0.0143  -0.0096 -0.0252 657  ILE B O   
13777 C CB  . ILE B 659  ? 0.2017 0.1901 0.2077 0.0083  -0.0085 -0.0249 657  ILE B CB  
13778 C CG1 . ILE B 659  ? 0.2005 0.1923 0.2073 0.0082  -0.0070 -0.0252 657  ILE B CG1 
13779 C CG2 . ILE B 659  ? 0.2272 0.2200 0.2377 0.0082  -0.0081 -0.0239 657  ILE B CG2 
13780 C CD1 . ILE B 659  ? 0.2162 0.2108 0.2229 0.0050  -0.0071 -0.0244 657  ILE B CD1 
13781 N N   . ILE B 660  ? 0.2124 0.1885 0.2129 0.0106  -0.0120 -0.0253 658  ILE B N   
13782 C CA  . ILE B 660  ? 0.2137 0.1866 0.2135 0.0113  -0.0136 -0.0247 658  ILE B CA  
13783 C C   . ILE B 660  ? 0.2132 0.1849 0.2143 0.0155  -0.0135 -0.0256 658  ILE B C   
13784 O O   . ILE B 660  ? 0.2423 0.2160 0.2466 0.0172  -0.0138 -0.0252 658  ILE B O   
13785 C CB  . ILE B 660  ? 0.2260 0.1919 0.2198 0.0087  -0.0156 -0.0244 658  ILE B CB  
13786 C CG1 . ILE B 660  ? 0.2526 0.2211 0.2463 0.0045  -0.0157 -0.0231 658  ILE B CG1 
13787 C CG2 . ILE B 660  ? 0.2376 0.1983 0.2295 0.0103  -0.0174 -0.0241 658  ILE B CG2 
13788 C CD1 . ILE B 660  ? 0.2631 0.2253 0.2510 0.0013  -0.0176 -0.0226 658  ILE B CD1 
13789 N N   . ARG B 661  ? 0.2070 0.1755 0.2054 0.0175  -0.0132 -0.0269 659  ARG B N   
13790 C CA  . ARG B 661  ? 0.2172 0.1841 0.2161 0.0219  -0.0132 -0.0278 659  ARG B CA  
13791 C C   . ARG B 661  ? 0.2367 0.2109 0.2415 0.0245  -0.0109 -0.0280 659  ARG B C   
13792 O O   . ARG B 661  ? 0.2420 0.2177 0.2497 0.0276  -0.0109 -0.0282 659  ARG B O   
13793 C CB  . ARG B 661  ? 0.2361 0.1956 0.2289 0.0232  -0.0139 -0.0291 659  ARG B CB  
13794 C CG  . ARG B 661  ? 0.2808 0.2320 0.2679 0.0215  -0.0166 -0.0288 659  ARG B CG  
13795 C CD  . ARG B 661  ? 0.3030 0.2459 0.2832 0.0223  -0.0176 -0.0302 659  ARG B CD  
13796 N NE  . ARG B 661  ? 0.2878 0.2293 0.2679 0.0274  -0.0170 -0.0317 659  ARG B NE  
13797 C CZ  . ARG B 661  ? 0.3161 0.2575 0.2948 0.0294  -0.0157 -0.0332 659  ARG B CZ  
13798 N NH1 . ARG B 661  ? 0.3311 0.2738 0.3085 0.0267  -0.0148 -0.0334 659  ARG B NH1 
13799 N NH2 . ARG B 661  ? 0.3110 0.2512 0.2895 0.0344  -0.0151 -0.0345 659  ARG B NH2 
13800 N N   . GLU B 662  ? 0.2236 0.2026 0.2305 0.0231  -0.0091 -0.0280 660  GLU B N   
13801 C CA  . GLU B 662  ? 0.2252 0.2108 0.2373 0.0253  -0.0070 -0.0280 660  GLU B CA  
13802 C C   . GLU B 662  ? 0.2095 0.2010 0.2273 0.0244  -0.0067 -0.0268 660  GLU B C   
13803 O O   . GLU B 662  ? 0.2171 0.2129 0.2394 0.0266  -0.0058 -0.0267 660  GLU B O   
13804 C CB  . GLU B 662  ? 0.2362 0.2240 0.2476 0.0245  -0.0052 -0.0284 660  GLU B CB  
13805 C CG  . GLU B 662  ? 0.2426 0.2371 0.2590 0.0265  -0.0029 -0.0283 660  GLU B CG  
13806 C CD  . GLU B 662  ? 0.2203 0.2167 0.2356 0.0259  -0.0011 -0.0286 660  GLU B CD  
13807 O OE1 . GLU B 662  ? 0.2305 0.2257 0.2434 0.0230  -0.0016 -0.0284 660  GLU B OE1 
13808 O OE2 . GLU B 662  ? 0.2409 0.2404 0.2579 0.0283  0.0007  -0.0290 660  GLU B OE2 
13809 N N   . ALA B 663  ? 0.1976 0.1894 0.2151 0.0211  -0.0074 -0.0259 661  ALA B N   
13810 C CA  . ALA B 663  ? 0.2086 0.2058 0.2310 0.0200  -0.0070 -0.0249 661  ALA B CA  
13811 C C   . ALA B 663  ? 0.2093 0.2048 0.2316 0.0191  -0.0089 -0.0242 661  ALA B C   
13812 O O   . ALA B 663  ? 0.2652 0.2644 0.2907 0.0179  -0.0089 -0.0234 661  ALA B O   
13813 C CB  . ALA B 663  ? 0.2164 0.2165 0.2392 0.0173  -0.0060 -0.0244 661  ALA B CB  
13814 N N   . GLY B 664  ? 0.2216 0.2113 0.2400 0.0196  -0.0107 -0.0244 662  GLY B N   
13815 C CA  . GLY B 664  ? 0.2508 0.2387 0.2687 0.0189  -0.0125 -0.0236 662  GLY B CA  
13816 C C   . GLY B 664  ? 0.2775 0.2654 0.2939 0.0153  -0.0130 -0.0228 662  GLY B C   
13817 O O   . GLY B 664  ? 0.2583 0.2467 0.2755 0.0145  -0.0140 -0.0220 662  GLY B O   
13818 N N   . LYS B 665  ? 0.2108 0.1982 0.2248 0.0131  -0.0123 -0.0228 663  LYS B N   
13819 C CA  . LYS B 665  ? 0.2192 0.2074 0.2319 0.0097  -0.0125 -0.0220 663  LYS B CA  
13820 C C   . LYS B 665  ? 0.2123 0.1946 0.2198 0.0079  -0.0143 -0.0215 663  LYS B C   
13821 O O   . LYS B 665  ? 0.2214 0.1985 0.2252 0.0084  -0.0151 -0.0221 663  LYS B O   
13822 C CB  . LYS B 665  ? 0.2129 0.2041 0.2259 0.0082  -0.0110 -0.0222 663  LYS B CB  
13823 C CG  . LYS B 665  ? 0.2742 0.2708 0.2917 0.0097  -0.0092 -0.0225 663  LYS B CG  
13824 C CD  . LYS B 665  ? 0.2930 0.2936 0.3145 0.0098  -0.0090 -0.0219 663  LYS B CD  
13825 C CE  . LYS B 665  ? 0.2855 0.2909 0.3113 0.0110  -0.0073 -0.0220 663  LYS B CE  
13826 N NZ  . LYS B 665  ? 0.3167 0.3254 0.3462 0.0112  -0.0074 -0.0216 663  LYS B NZ  
13827 N N   . SER B 666  ? 0.2413 0.2243 0.2481 0.0055  -0.0149 -0.0205 664  SER B N   
13828 C CA  . SER B 666  ? 0.2455 0.2237 0.2472 0.0029  -0.0163 -0.0198 664  SER B CA  
13829 C C   . SER B 666  ? 0.2403 0.2193 0.2402 0.0002  -0.0155 -0.0198 664  SER B C   
13830 O O   . SER B 666  ? 0.2412 0.2249 0.2440 0.0004  -0.0140 -0.0202 664  SER B O   
13831 C CB  . SER B 666  ? 0.2671 0.2470 0.2688 0.0011  -0.0167 -0.0187 664  SER B CB  
13832 O OG  . SER B 666  ? 0.2948 0.2805 0.2989 -0.0005 -0.0152 -0.0185 664  SER B OG  
13833 N N   . ALA B 667  ? 0.2450 0.2190 0.2401 -0.0023 -0.0169 -0.0193 665  ALA B N   
13834 C CA  . ALA B 667  ? 0.2197 0.1942 0.2128 -0.0052 -0.0165 -0.0192 665  ALA B CA  
13835 C C   . ALA B 667  ? 0.2398 0.2216 0.2360 -0.0070 -0.0151 -0.0185 665  ALA B C   
13836 O O   . ALA B 667  ? 0.2250 0.2102 0.2225 -0.0075 -0.0140 -0.0189 665  ALA B O   
13837 C CB  . ALA B 667  ? 0.2648 0.2328 0.2521 -0.0081 -0.0184 -0.0184 665  ALA B CB  
13838 N N   . LEU B 668  ? 0.2354 0.2196 0.2326 -0.0078 -0.0151 -0.0176 666  LEU B N   
13839 C CA  . LEU B 668  ? 0.2692 0.2602 0.2691 -0.0092 -0.0136 -0.0171 666  LEU B CA  
13840 C C   . LEU B 668  ? 0.2304 0.2262 0.2350 -0.0066 -0.0121 -0.0180 666  LEU B C   
13841 O O   . LEU B 668  ? 0.2332 0.2336 0.2395 -0.0074 -0.0109 -0.0180 666  LEU B O   
13842 C CB  . LEU B 668  ? 0.2687 0.2611 0.2686 -0.0100 -0.0138 -0.0161 666  LEU B CB  
13843 C CG  . LEU B 668  ? 0.3314 0.3218 0.3272 -0.0136 -0.0147 -0.0147 666  LEU B CG  
13844 C CD1 . LEU B 668  ? 0.4097 0.4015 0.4053 -0.0139 -0.0147 -0.0139 666  LEU B CD1 
13845 C CD2 . LEU B 668  ? 0.3814 0.3759 0.3773 -0.0164 -0.0139 -0.0143 666  LEU B CD2 
13846 N N   . ASN B 669  ? 0.2219 0.2168 0.2285 -0.0036 -0.0121 -0.0187 667  ASN B N   
13847 C CA  . ASN B 669  ? 0.2225 0.2218 0.2334 -0.0015 -0.0106 -0.0193 667  ASN B CA  
13848 C C   . ASN B 669  ? 0.2115 0.2106 0.2224 -0.0009 -0.0100 -0.0201 667  ASN B C   
13849 O O   . ASN B 669  ? 0.2313 0.2347 0.2450 -0.0002 -0.0086 -0.0203 667  ASN B O   
13850 C CB  . ASN B 669  ? 0.2783 0.2774 0.2918 0.0010  -0.0109 -0.0196 667  ASN B CB  
13851 C CG  . ASN B 669  ? 0.3492 0.3497 0.3631 0.0004  -0.0113 -0.0190 667  ASN B CG  
13852 O OD1 . ASN B 669  ? 0.4262 0.4299 0.4403 -0.0012 -0.0107 -0.0185 667  ASN B OD1 
13853 N ND2 . ASN B 669  ? 0.3898 0.3881 0.4040 0.0018  -0.0124 -0.0189 667  ASN B ND2 
13854 N N   . ALA B 670  ? 0.2047 0.1987 0.2121 -0.0010 -0.0109 -0.0205 668  ALA B N   
13855 C CA  . ALA B 670  ? 0.2094 0.2028 0.2159 -0.0006 -0.0104 -0.0213 668  ALA B CA  
13856 C C   . ALA B 670  ? 0.2023 0.1983 0.2078 -0.0034 -0.0101 -0.0209 668  ALA B C   
13857 O O   . ALA B 670  ? 0.2011 0.1998 0.2078 -0.0029 -0.0091 -0.0213 668  ALA B O   
13858 C CB  . ALA B 670  ? 0.2209 0.2074 0.2233 0.0001  -0.0117 -0.0219 668  ALA B CB  
13859 N N   . ILE B 671  ? 0.2039 0.1994 0.2073 -0.0063 -0.0110 -0.0199 669  ILE B N   
13860 C CA  . ILE B 671  ? 0.2010 0.2002 0.2042 -0.0091 -0.0107 -0.0194 669  ILE B CA  
13861 C C   . ILE B 671  ? 0.2021 0.2082 0.2097 -0.0080 -0.0091 -0.0193 669  ILE B C   
13862 O O   . ILE B 671  ? 0.2077 0.2172 0.2163 -0.0083 -0.0084 -0.0194 669  ILE B O   
13863 C CB  . ILE B 671  ? 0.1896 0.1879 0.1903 -0.0124 -0.0118 -0.0182 669  ILE B CB  
13864 C CG1 . ILE B 671  ? 0.2093 0.2004 0.2050 -0.0141 -0.0135 -0.0182 669  ILE B CG1 
13865 C CG2 . ILE B 671  ? 0.2329 0.2371 0.2347 -0.0149 -0.0111 -0.0174 669  ILE B CG2 
13866 C CD1 . ILE B 671  ? 0.2567 0.2453 0.2494 -0.0171 -0.0147 -0.0168 669  ILE B CD1 
13867 N N   . ALA B 672  ? 0.2009 0.2089 0.2110 -0.0068 -0.0086 -0.0190 670  ALA B N   
13868 C CA  . ALA B 672  ? 0.2089 0.2226 0.2226 -0.0056 -0.0072 -0.0189 670  ALA B CA  
13869 C C   . ALA B 672  ? 0.2074 0.2221 0.2232 -0.0034 -0.0063 -0.0197 670  ALA B C   
13870 O O   . ALA B 672  ? 0.2163 0.2352 0.2340 -0.0032 -0.0053 -0.0196 670  ALA B O   
13871 C CB  . ALA B 672  ? 0.2366 0.2509 0.2520 -0.0045 -0.0071 -0.0187 670  ALA B CB  
13872 N N   . GLU B 673  ? 0.1980 0.2091 0.2134 -0.0017 -0.0065 -0.0204 671  GLU B N   
13873 C CA  . GLU B 673  ? 0.2086 0.2206 0.2257 0.0004  -0.0055 -0.0210 671  GLU B CA  
13874 C C   . GLU B 673  ? 0.1997 0.2124 0.2151 -0.0006 -0.0053 -0.0212 671  GLU B C   
13875 O O   . GLU B 673  ? 0.1922 0.2083 0.2095 0.0002  -0.0042 -0.0212 671  GLU B O   
13876 C CB  . GLU B 673  ? 0.2247 0.2326 0.2411 0.0023  -0.0059 -0.0217 671  GLU B CB  
13877 C CG  . GLU B 673  ? 0.2234 0.2324 0.2416 0.0047  -0.0046 -0.0223 671  GLU B CG  
13878 C CD  . GLU B 673  ? 0.2305 0.2432 0.2532 0.0062  -0.0036 -0.0219 671  GLU B CD  
13879 O OE1 . GLU B 673  ? 0.2599 0.2732 0.2840 0.0059  -0.0041 -0.0215 671  GLU B OE1 
13880 O OE2 . GLU B 673  ? 0.2043 0.2189 0.2287 0.0076  -0.0024 -0.0221 671  GLU B OE2 
13881 N N   . VAL B 674  ? 0.1762 0.1853 0.1878 -0.0024 -0.0064 -0.0214 672  VAL B N   
13882 C CA  . VAL B 674  ? 0.1850 0.1945 0.1947 -0.0036 -0.0065 -0.0216 672  VAL B CA  
13883 C C   . VAL B 674  ? 0.1741 0.1891 0.1853 -0.0053 -0.0062 -0.0208 672  VAL B C   
13884 O O   . VAL B 674  ? 0.1850 0.2029 0.1969 -0.0050 -0.0056 -0.0209 672  VAL B O   
13885 C CB  . VAL B 674  ? 0.1871 0.1909 0.1920 -0.0053 -0.0082 -0.0220 672  VAL B CB  
13886 C CG1 . VAL B 674  ? 0.1992 0.2033 0.2019 -0.0067 -0.0085 -0.0224 672  VAL B CG1 
13887 C CG2 . VAL B 674  ? 0.2188 0.2172 0.2221 -0.0029 -0.0084 -0.0229 672  VAL B CG2 
13888 N N   . ARG B 675  ? 0.1750 0.1918 0.1868 -0.0069 -0.0065 -0.0200 673  ARG B N   
13889 C CA  . ARG B 675  ? 0.1720 0.1946 0.1856 -0.0082 -0.0061 -0.0193 673  ARG B CA  
13890 C C   . ARG B 675  ? 0.1581 0.1847 0.1751 -0.0058 -0.0047 -0.0193 673  ARG B C   
13891 O O   . ARG B 675  ? 0.1740 0.2046 0.1920 -0.0059 -0.0043 -0.0191 673  ARG B O   
13892 C CB  . ARG B 675  ? 0.1839 0.2079 0.1976 -0.0098 -0.0063 -0.0184 673  ARG B CB  
13893 C CG  . ARG B 675  ? 0.2003 0.2214 0.2106 -0.0130 -0.0077 -0.0179 673  ARG B CG  
13894 C CD  . ARG B 675  ? 0.1990 0.2230 0.2098 -0.0146 -0.0076 -0.0168 673  ARG B CD  
13895 N NE  . ARG B 675  ? 0.1801 0.2112 0.1932 -0.0151 -0.0067 -0.0163 673  ARG B NE  
13896 C CZ  . ARG B 675  ? 0.1891 0.2246 0.2037 -0.0154 -0.0060 -0.0156 673  ARG B CZ  
13897 N NH1 . ARG B 675  ? 0.1955 0.2290 0.2093 -0.0153 -0.0060 -0.0153 673  ARG B NH1 
13898 N NH2 . ARG B 675  ? 0.1974 0.2394 0.2141 -0.0156 -0.0052 -0.0152 673  ARG B NH2 
13899 N N   . GLU B 676  ? 0.1584 0.1840 0.1772 -0.0036 -0.0041 -0.0196 674  GLU B N   
13900 C CA  A GLU B 676  ? 0.1708 0.1996 0.1927 -0.0015 -0.0029 -0.0196 674  GLU B CA  
13901 C CA  B GLU B 676  ? 0.1706 0.1994 0.1925 -0.0015 -0.0029 -0.0196 674  GLU B CA  
13902 C C   . GLU B 676  ? 0.1617 0.1907 0.1835 -0.0005 -0.0023 -0.0199 674  GLU B C   
13903 O O   . GLU B 676  ? 0.1574 0.1898 0.1807 0.0002  -0.0017 -0.0196 674  GLU B O   
13904 C CB  A GLU B 676  ? 0.1773 0.2044 0.2011 0.0003  -0.0026 -0.0198 674  GLU B CB  
13905 C CB  B GLU B 676  ? 0.1771 0.2045 0.2009 0.0003  -0.0025 -0.0197 674  GLU B CB  
13906 C CG  A GLU B 676  ? 0.1989 0.2287 0.2256 0.0022  -0.0015 -0.0197 674  GLU B CG  
13907 C CG  B GLU B 676  ? 0.1897 0.2200 0.2164 0.0019  -0.0016 -0.0196 674  GLU B CG  
13908 C CD  A GLU B 676  ? 0.2243 0.2567 0.2522 0.0021  -0.0014 -0.0193 674  GLU B CD  
13909 C CD  B GLU B 676  ? 0.2503 0.2795 0.2788 0.0031  -0.0015 -0.0196 674  GLU B CD  
13910 O OE1 A GLU B 676  ? 0.2635 0.2970 0.2902 0.0005  -0.0019 -0.0190 674  GLU B OE1 
13911 O OE1 B GLU B 676  ? 0.2749 0.3029 0.3027 0.0024  -0.0023 -0.0196 674  GLU B OE1 
13912 O OE2 A GLU B 676  ? 0.2288 0.2622 0.2588 0.0036  -0.0009 -0.0193 674  GLU B OE2 
13913 O OE2 B GLU B 676  ? 0.2965 0.3261 0.3271 0.0046  -0.0009 -0.0197 674  GLU B OE2 
13914 N N   . ALA B 677  ? 0.1677 0.1929 0.1874 -0.0003 -0.0027 -0.0205 675  ALA B N   
13915 C CA  . ALA B 677  ? 0.1606 0.1858 0.1794 0.0006  -0.0022 -0.0209 675  ALA B CA  
13916 C C   . ALA B 677  ? 0.1650 0.1928 0.1826 -0.0011 -0.0027 -0.0206 675  ALA B C   
13917 O O   . ALA B 677  ? 0.1654 0.1960 0.1839 -0.0003 -0.0020 -0.0204 675  ALA B O   
13918 C CB  . ALA B 677  ? 0.1761 0.1965 0.1923 0.0012  -0.0025 -0.0218 675  ALA B CB  
13919 N N   . ILE B 678  ? 0.1473 0.1744 0.1629 -0.0036 -0.0039 -0.0205 676  ILE B N   
13920 C CA  . ILE B 678  ? 0.1422 0.1724 0.1569 -0.0056 -0.0046 -0.0201 676  ILE B CA  
13921 C C   . ILE B 678  ? 0.1453 0.1815 0.1633 -0.0049 -0.0038 -0.0193 676  ILE B C   
13922 O O   . ILE B 678  ? 0.1578 0.1972 0.1762 -0.0048 -0.0038 -0.0191 676  ILE B O   
13923 C CB  . ILE B 678  ? 0.1552 0.1839 0.1676 -0.0088 -0.0060 -0.0198 676  ILE B CB  
13924 C CG1 . ILE B 678  ? 0.1777 0.1999 0.1861 -0.0094 -0.0070 -0.0207 676  ILE B CG1 
13925 C CG2 . ILE B 678  ? 0.1565 0.1901 0.1691 -0.0111 -0.0067 -0.0191 676  ILE B CG2 
13926 C CD1 . ILE B 678  ? 0.1800 0.1988 0.1860 -0.0120 -0.0084 -0.0204 676  ILE B CD1 
13927 N N   . ASP B 679  ? 0.1526 0.1902 0.1728 -0.0044 -0.0033 -0.0189 677  ASP B N   
13928 C CA  . ASP B 679  ? 0.1572 0.2000 0.1801 -0.0034 -0.0026 -0.0183 677  ASP B CA  
13929 C C   . ASP B 679  ? 0.1589 0.2023 0.1833 -0.0009 -0.0016 -0.0184 677  ASP B C   
13930 O O   . ASP B 679  ? 0.1558 0.2032 0.1814 -0.0002 -0.0014 -0.0180 677  ASP B O   
13931 C CB  . ASP B 679  ? 0.1553 0.1985 0.1795 -0.0033 -0.0023 -0.0181 677  ASP B CB  
13932 C CG  . ASP B 679  ? 0.1731 0.2168 0.1958 -0.0060 -0.0031 -0.0177 677  ASP B CG  
13933 O OD1 . ASP B 679  ? 0.1924 0.2387 0.2143 -0.0080 -0.0037 -0.0173 677  ASP B OD1 
13934 O OD2 . ASP B 679  ? 0.2108 0.2525 0.2332 -0.0063 -0.0031 -0.0177 677  ASP B OD2 
13935 N N   . PHE B 680  ? 0.1445 0.1844 0.1690 0.0006  -0.0011 -0.0188 678  PHE B N   
13936 C CA  . PHE B 680  ? 0.1479 0.1884 0.1735 0.0027  -0.0001 -0.0187 678  PHE B CA  
13937 C C   . PHE B 680  ? 0.1542 0.1959 0.1783 0.0024  -0.0004 -0.0186 678  PHE B C   
13938 O O   . PHE B 680  ? 0.1455 0.1899 0.1705 0.0035  0.0000  -0.0181 678  PHE B O   
13939 C CB  . PHE B 680  ? 0.1497 0.1866 0.1756 0.0039  0.0005  -0.0191 678  PHE B CB  
13940 C CG  . PHE B 680  ? 0.1479 0.1843 0.1761 0.0049  0.0009  -0.0190 678  PHE B CG  
13941 C CD1 . PHE B 680  ? 0.1582 0.1968 0.1884 0.0059  0.0013  -0.0185 678  PHE B CD1 
13942 C CD2 . PHE B 680  ? 0.1627 0.1961 0.1908 0.0049  0.0007  -0.0194 678  PHE B CD2 
13943 C CE1 . PHE B 680  ? 0.1685 0.2061 0.2004 0.0067  0.0015  -0.0185 678  PHE B CE1 
13944 C CE2 . PHE B 680  ? 0.1789 0.2118 0.2091 0.0057  0.0008  -0.0194 678  PHE B CE2 
13945 C CZ  . PHE B 680  ? 0.1740 0.2090 0.2061 0.0064  0.0012  -0.0189 678  PHE B CZ  
13946 N N   . LEU B 681  ? 0.1411 0.1804 0.1624 0.0010  -0.0011 -0.0192 679  LEU B N   
13947 C CA  . LEU B 681  ? 0.1460 0.1860 0.1653 0.0006  -0.0016 -0.0192 679  LEU B CA  
13948 C C   . LEU B 681  ? 0.1452 0.1902 0.1654 -0.0002 -0.0022 -0.0185 679  LEU B C   
13949 O O   . LEU B 681  ? 0.1512 0.1986 0.1717 0.0008  -0.0020 -0.0181 679  LEU B O   
13950 C CB  . LEU B 681  ? 0.1543 0.1904 0.1700 -0.0011 -0.0026 -0.0200 679  LEU B CB  
13951 C CG  . LEU B 681  ? 0.1455 0.1769 0.1599 0.0004  -0.0019 -0.0208 679  LEU B CG  
13952 C CD1 . LEU B 681  ? 0.1570 0.1839 0.1680 -0.0011 -0.0031 -0.0217 679  LEU B CD1 
13953 C CD2 . LEU B 681  ? 0.1733 0.2048 0.1869 0.0021  -0.0010 -0.0209 679  LEU B CD2 
13954 N N   . ARG B 682  ? 0.1422 0.1892 0.1630 -0.0021 -0.0029 -0.0183 680  ARG B N   
13955 C CA  . ARG B 682  ? 0.1294 0.1819 0.1512 -0.0030 -0.0035 -0.0176 680  ARG B CA  
13956 C C   . ARG B 682  ? 0.1350 0.1913 0.1598 -0.0007 -0.0026 -0.0170 680  ARG B C   
13957 O O   . ARG B 682  ? 0.1547 0.2154 0.1805 -0.0002 -0.0029 -0.0165 680  ARG B O   
13958 C CB  . ARG B 682  ? 0.1417 0.1956 0.1634 -0.0058 -0.0044 -0.0174 680  ARG B CB  
13959 C CG  . ARG B 682  ? 0.1505 0.2007 0.1687 -0.0084 -0.0057 -0.0179 680  ARG B CG  
13960 C CD  . ARG B 682  ? 0.1738 0.2248 0.1917 -0.0114 -0.0065 -0.0174 680  ARG B CD  
13961 N NE  . ARG B 682  ? 0.1795 0.2270 0.1939 -0.0143 -0.0081 -0.0178 680  ARG B NE  
13962 C CZ  . ARG B 682  ? 0.1835 0.2289 0.1962 -0.0171 -0.0090 -0.0175 680  ARG B CZ  
13963 N NH1 . ARG B 682  ? 0.1980 0.2448 0.2122 -0.0176 -0.0085 -0.0169 680  ARG B NH1 
13964 N NH2 . ARG B 682  ? 0.2334 0.2746 0.2423 -0.0196 -0.0106 -0.0180 680  ARG B NH2 
13965 N N   . TYR B 683  ? 0.1355 0.1900 0.1617 0.0008  -0.0016 -0.0171 681  TYR B N   
13966 C CA  . TYR B 683  ? 0.1403 0.1975 0.1689 0.0031  -0.0009 -0.0167 681  TYR B CA  
13967 C C   . TYR B 683  ? 0.1397 0.1963 0.1682 0.0051  -0.0004 -0.0165 681  TYR B C   
13968 O O   . TYR B 683  ? 0.1493 0.2093 0.1787 0.0064  -0.0005 -0.0159 681  TYR B O   
13969 C CB  . TYR B 683  ? 0.1447 0.1994 0.1743 0.0039  -0.0002 -0.0170 681  TYR B CB  
13970 C CG  . TYR B 683  ? 0.1362 0.1924 0.1676 0.0062  0.0005  -0.0168 681  TYR B CG  
13971 C CD1 . TYR B 683  ? 0.1589 0.2194 0.1914 0.0067  0.0005  -0.0165 681  TYR B CD1 
13972 C CD2 . TYR B 683  ? 0.1586 0.2118 0.1904 0.0080  0.0011  -0.0167 681  TYR B CD2 
13973 C CE1 . TYR B 683  ? 0.1686 0.2298 0.2023 0.0092  0.0010  -0.0164 681  TYR B CE1 
13974 C CE2 . TYR B 683  ? 0.1499 0.2036 0.1829 0.0101  0.0015  -0.0165 681  TYR B CE2 
13975 C CZ  . TYR B 683  ? 0.1414 0.1988 0.1752 0.0108  0.0014  -0.0165 681  TYR B CZ  
13976 O OH  . TYR B 683  ? 0.1746 0.2319 0.2091 0.0131  0.0017  -0.0164 681  TYR B OH  
13977 N N   . TYR B 684  ? 0.1320 0.1844 0.1593 0.0054  0.0000  -0.0168 682  TYR B N   
13978 C CA  . TYR B 684  ? 0.1381 0.1900 0.1650 0.0071  0.0005  -0.0163 682  TYR B CA  
13979 C C   . TYR B 684  ? 0.1501 0.2045 0.1755 0.0066  -0.0003 -0.0160 682  TYR B C   
13980 O O   . TYR B 684  ? 0.1613 0.2170 0.1867 0.0082  -0.0002 -0.0154 682  TYR B O   
13981 C CB  . TYR B 684  ? 0.1464 0.1939 0.1725 0.0076  0.0013  -0.0166 682  TYR B CB  
13982 C CG  . TYR B 684  ? 0.1382 0.1838 0.1663 0.0082  0.0020  -0.0168 682  TYR B CG  
13983 C CD1 . TYR B 684  ? 0.1491 0.1959 0.1791 0.0094  0.0022  -0.0164 682  TYR B CD1 
13984 C CD2 . TYR B 684  ? 0.1467 0.1892 0.1746 0.0077  0.0023  -0.0173 682  TYR B CD2 
13985 C CE1 . TYR B 684  ? 0.1520 0.1969 0.1835 0.0098  0.0026  -0.0165 682  TYR B CE1 
13986 C CE2 . TYR B 684  ? 0.1438 0.1848 0.1735 0.0082  0.0027  -0.0174 682  TYR B CE2 
13987 C CZ  . TYR B 684  ? 0.1499 0.1920 0.1813 0.0091  0.0028  -0.0170 682  TYR B CZ  
13988 O OH  . TYR B 684  ? 0.1618 0.2023 0.1949 0.0094  0.0029  -0.0172 682  TYR B OH  
13989 N N   . ALA B 685  ? 0.1391 0.1939 0.1629 0.0044  -0.0013 -0.0165 683  ALA B N   
13990 C CA  . ALA B 685  ? 0.1433 0.2008 0.1657 0.0037  -0.0024 -0.0162 683  ALA B CA  
13991 C C   . ALA B 685  ? 0.1655 0.2286 0.1901 0.0044  -0.0028 -0.0154 683  ALA B C   
13992 O O   . ALA B 685  ? 0.1543 0.2197 0.1789 0.0058  -0.0031 -0.0148 683  ALA B O   
13993 C CB  . ALA B 685  ? 0.1518 0.2083 0.1720 0.0008  -0.0036 -0.0168 683  ALA B CB  
13994 N N   . GLU B 686  ? 0.1541 0.2196 0.1808 0.0038  -0.0028 -0.0154 684  GLU B N   
13995 C CA  . GLU B 686  ? 0.1573 0.2287 0.1862 0.0049  -0.0030 -0.0148 684  GLU B CA  
13996 C C   . GLU B 686  ? 0.1661 0.2372 0.1961 0.0082  -0.0022 -0.0144 684  GLU B C   
13997 O O   . GLU B 686  ? 0.1654 0.2401 0.1960 0.0097  -0.0026 -0.0137 684  GLU B O   
13998 C CB  . GLU B 686  ? 0.1719 0.2460 0.2025 0.0036  -0.0029 -0.0148 684  GLU B CB  
13999 C CG  . GLU B 686  ? 0.1999 0.2804 0.2330 0.0053  -0.0028 -0.0143 684  GLU B CG  
14000 C CD  . GLU B 686  ? 0.2444 0.3306 0.2780 0.0047  -0.0040 -0.0136 684  GLU B CD  
14001 O OE1 . GLU B 686  ? 0.2355 0.3212 0.2674 0.0025  -0.0051 -0.0136 684  GLU B OE1 
14002 O OE2 . GLU B 686  ? 0.2685 0.3602 0.3043 0.0066  -0.0039 -0.0131 684  GLU B OE2 
14003 N N   . GLN B 687  ? 0.1454 0.2121 0.1756 0.0093  -0.0011 -0.0146 685  GLN B N   
14004 C CA  . GLN B 687  ? 0.1520 0.2178 0.1829 0.0121  -0.0005 -0.0142 685  GLN B CA  
14005 C C   . GLN B 687  ? 0.1587 0.2237 0.1880 0.0131  -0.0008 -0.0136 685  GLN B C   
14006 O O   . GLN B 687  ? 0.1723 0.2387 0.2020 0.0153  -0.0009 -0.0129 685  GLN B O   
14007 C CB  . GLN B 687  ? 0.1618 0.2228 0.1930 0.0126  0.0004  -0.0146 685  GLN B CB  
14008 C CG  . GLN B 687  ? 0.1864 0.2481 0.2189 0.0121  0.0006  -0.0151 685  GLN B CG  
14009 C CD  . GLN B 687  ? 0.2034 0.2690 0.2372 0.0139  0.0006  -0.0149 685  GLN B CD  
14010 O OE1 . GLN B 687  ? 0.1981 0.2628 0.2321 0.0164  0.0008  -0.0146 685  GLN B OE1 
14011 N NE2 . GLN B 687  ? 0.2306 0.3004 0.2652 0.0128  0.0003  -0.0151 685  GLN B NE2 
14012 N N   . THR B 688  ? 0.1534 0.2161 0.1806 0.0116  -0.0009 -0.0138 686  THR B N   
14013 C CA  . THR B 688  ? 0.1559 0.2182 0.1812 0.0123  -0.0012 -0.0132 686  THR B CA  
14014 C C   . THR B 688  ? 0.1560 0.2234 0.1814 0.0126  -0.0025 -0.0126 686  THR B C   
14015 O O   . THR B 688  ? 0.1779 0.2461 0.2029 0.0146  -0.0028 -0.0118 686  THR B O   
14016 C CB  . THR B 688  ? 0.1418 0.2011 0.1646 0.0106  -0.0012 -0.0137 686  THR B CB  
14017 O OG1 . THR B 688  ? 0.1686 0.2235 0.1915 0.0108  0.0001  -0.0140 686  THR B OG1 
14018 C CG2 . THR B 688  ? 0.1676 0.2268 0.1878 0.0112  -0.0016 -0.0132 686  THR B CG2 
14019 N N   . ARG B 689  ? 0.1434 0.2144 0.1694 0.0106  -0.0035 -0.0130 687  ARG B N   
14020 C CA  . ARG B 689  ? 0.1649 0.2416 0.1915 0.0106  -0.0048 -0.0125 687  ARG B CA  
14021 C C   . ARG B 689  ? 0.1576 0.2381 0.1868 0.0134  -0.0046 -0.0118 687  ARG B C   
14022 O O   . ARG B 689  ? 0.1854 0.2698 0.2148 0.0147  -0.0056 -0.0111 687  ARG B O   
14023 C CB  . ARG B 689  ? 0.1642 0.2442 0.1914 0.0075  -0.0058 -0.0129 687  ARG B CB  
14024 C CG  . ARG B 689  ? 0.1855 0.2622 0.2095 0.0049  -0.0065 -0.0135 687  ARG B CG  
14025 C CD  . ARG B 689  ? 0.2016 0.2814 0.2258 0.0016  -0.0078 -0.0137 687  ARG B CD  
14026 N NE  . ARG B 689  ? 0.2114 0.2913 0.2374 0.0005  -0.0071 -0.0140 687  ARG B NE  
14027 C CZ  . ARG B 689  ? 0.2157 0.2909 0.2401 -0.0015 -0.0069 -0.0148 687  ARG B CZ  
14028 N NH1 . ARG B 689  ? 0.2086 0.2786 0.2296 -0.0024 -0.0073 -0.0154 687  ARG B NH1 
14029 N NH2 . ARG B 689  ? 0.2014 0.2770 0.2273 -0.0024 -0.0063 -0.0149 687  ARG B NH2 
14030 N N   . ARG B 690  ? 0.1622 0.2413 0.1929 0.0145  -0.0035 -0.0121 688  ARG B N   
14031 C CA  . ARG B 690  ? 0.1562 0.2378 0.1887 0.0175  -0.0033 -0.0117 688  ARG B CA  
14032 C C   . ARG B 690  ? 0.1655 0.2434 0.1968 0.0203  -0.0030 -0.0111 688  ARG B C   
14033 O O   . ARG B 690  ? 0.1794 0.2594 0.2116 0.0231  -0.0032 -0.0107 688  ARG B O   
14034 C CB  . ARG B 690  ? 0.1736 0.2546 0.2077 0.0176  -0.0023 -0.0124 688  ARG B CB  
14035 C CG  . ARG B 690  ? 0.1914 0.2766 0.2267 0.0150  -0.0025 -0.0128 688  ARG B CG  
14036 C CD  . ARG B 690  ? 0.2322 0.3254 0.2697 0.0159  -0.0031 -0.0123 688  ARG B CD  
14037 N NE  . ARG B 690  ? 0.2872 0.3815 0.3260 0.0194  -0.0024 -0.0123 688  ARG B NE  
14038 C CZ  . ARG B 690  ? 0.2679 0.3643 0.3070 0.0226  -0.0029 -0.0118 688  ARG B CZ  
14039 N NH1 . ARG B 690  ? 0.2579 0.3562 0.2964 0.0226  -0.0040 -0.0111 688  ARG B NH1 
14040 N NH2 . ARG B 690  ? 0.2131 0.3094 0.2529 0.0259  -0.0022 -0.0120 688  ARG B NH2 
14041 N N   . THR B 691  ? 0.1733 0.2457 0.2025 0.0197  -0.0025 -0.0110 689  THR B N   
14042 C CA  . THR B 691  ? 0.1798 0.2480 0.2081 0.0221  -0.0020 -0.0103 689  THR B CA  
14043 C C   . THR B 691  ? 0.1823 0.2478 0.2079 0.0222  -0.0022 -0.0095 689  THR B C   
14044 O O   . THR B 691  ? 0.2254 0.2899 0.2501 0.0244  -0.0025 -0.0085 689  THR B O   
14045 C CB  . THR B 691  ? 0.1810 0.2443 0.2097 0.0219  -0.0008 -0.0108 689  THR B CB  
14046 O OG1 . THR B 691  ? 0.1912 0.2522 0.2192 0.0193  -0.0003 -0.0113 689  THR B OG1 
14047 C CG2 . THR B 691  ? 0.1814 0.2465 0.2121 0.0226  -0.0006 -0.0115 689  THR B CG2 
14048 N N   . LEU B 692  ? 0.1797 0.2437 0.2038 0.0199  -0.0020 -0.0098 690  LEU B N   
14049 C CA  . LEU B 692  ? 0.1976 0.2579 0.2189 0.0201  -0.0016 -0.0090 690  LEU B CA  
14050 C C   . LEU B 692  ? 0.2062 0.2688 0.2255 0.0208  -0.0028 -0.0082 690  LEU B C   
14051 O O   . LEU B 692  ? 0.2265 0.2928 0.2456 0.0196  -0.0039 -0.0086 690  LEU B O   
14052 C CB  . LEU B 692  ? 0.1881 0.2455 0.2083 0.0179  -0.0007 -0.0098 690  LEU B CB  
14053 C CG  . LEU B 692  ? 0.2118 0.2663 0.2337 0.0174  0.0006  -0.0104 690  LEU B CG  
14054 C CD1 . LEU B 692  ? 0.2338 0.2854 0.2543 0.0159  0.0015  -0.0109 690  LEU B CD1 
14055 C CD2 . LEU B 692  ? 0.2359 0.2880 0.2588 0.0192  0.0012  -0.0096 690  LEU B CD2 
14056 N N   . GLY B 693  ? 0.1976 0.2579 0.2153 0.0227  -0.0027 -0.0070 691  GLY B N   
14057 C CA  . GLY B 693  ? 0.2197 0.2814 0.2350 0.0237  -0.0039 -0.0060 691  GLY B CA  
14058 C C   . GLY B 693  ? 0.2296 0.2867 0.2417 0.0238  -0.0030 -0.0050 691  GLY B C   
14059 O O   . GLY B 693  ? 0.2381 0.2914 0.2501 0.0229  -0.0014 -0.0051 691  GLY B O   
14060 N N   . PRO B 694  ? 0.2489 0.3065 0.2583 0.0249  -0.0040 -0.0038 692  PRO B N   
14061 C CA  . PRO B 694  ? 0.2707 0.3243 0.2764 0.0247  -0.0031 -0.0028 692  PRO B CA  
14062 C C   . PRO B 694  ? 0.2727 0.3216 0.2784 0.0255  -0.0017 -0.0017 692  PRO B C   
14063 O O   . PRO B 694  ? 0.3211 0.3668 0.3249 0.0245  -0.0002 -0.0012 692  PRO B O   
14064 C CB  . PRO B 694  ? 0.3146 0.3701 0.3176 0.0260  -0.0049 -0.0017 692  PRO B CB  
14065 C CG  . PRO B 694  ? 0.3593 0.4196 0.3652 0.0275  -0.0065 -0.0019 692  PRO B CG  
14066 C CD  . PRO B 694  ? 0.2850 0.3473 0.2945 0.0261  -0.0060 -0.0035 692  PRO B CD  
14067 N N   . GLY B 695  ? 0.2762 0.3246 0.2840 0.0272  -0.0020 -0.0013 693  GLY B N   
14068 C CA  . GLY B 695  ? 0.2717 0.3152 0.2793 0.0278  -0.0010 -0.0002 693  GLY B CA  
14069 C C   . GLY B 695  ? 0.2646 0.3062 0.2747 0.0262  0.0005  -0.0012 693  GLY B C   
14070 O O   . GLY B 695  ? 0.3334 0.3711 0.3437 0.0263  0.0013  -0.0004 693  GLY B O   
14071 N N   . HIS B 696  ? 0.2417 0.2860 0.2537 0.0247  0.0008  -0.0029 694  HIS B N   
14072 C CA  . HIS B 696  ? 0.2340 0.2767 0.2482 0.0232  0.0021  -0.0038 694  HIS B CA  
14073 C C   . HIS B 696  ? 0.2286 0.2705 0.2415 0.0214  0.0034  -0.0040 694  HIS B C   
14074 O O   . HIS B 696  ? 0.2936 0.3373 0.3069 0.0201  0.0035  -0.0054 694  HIS B O   
14075 C CB  . HIS B 696  ? 0.2345 0.2802 0.2517 0.0229  0.0015  -0.0054 694  HIS B CB  
14076 C CG  . HIS B 696  ? 0.2170 0.2646 0.2353 0.0250  0.0003  -0.0053 694  HIS B CG  
14077 N ND1 . HIS B 696  ? 0.2257 0.2783 0.2446 0.0254  -0.0010 -0.0059 694  HIS B ND1 
14078 C CD2 . HIS B 696  ? 0.2261 0.2714 0.2448 0.0268  0.0001  -0.0047 694  HIS B CD2 
14079 C CE1 . HIS B 696  ? 0.2420 0.2957 0.2620 0.0277  -0.0017 -0.0056 694  HIS B CE1 
14080 N NE2 . HIS B 696  ? 0.2445 0.2935 0.2641 0.0287  -0.0012 -0.0050 694  HIS B NE2 
14081 N N   . GLY B 697  ? 0.2641 0.3031 0.2751 0.0214  0.0044  -0.0026 695  GLY B N   
14082 C CA  . GLY B 697  ? 0.2433 0.2817 0.2526 0.0201  0.0058  -0.0026 695  GLY B CA  
14083 C C   . GLY B 697  ? 0.2398 0.2776 0.2517 0.0188  0.0072  -0.0036 695  GLY B C   
14084 O O   . GLY B 697  ? 0.2343 0.2710 0.2489 0.0187  0.0073  -0.0036 695  GLY B O   
14085 N N   . PRO B 698  ? 0.2470 0.2854 0.2579 0.0178  0.0081  -0.0045 696  PRO B N   
14086 C CA  . PRO B 698  ? 0.2316 0.2697 0.2450 0.0168  0.0093  -0.0055 696  PRO B CA  
14087 C C   . PRO B 698  ? 0.2211 0.2574 0.2353 0.0165  0.0110  -0.0040 696  PRO B C   
14088 O O   . PRO B 698  ? 0.2297 0.2649 0.2418 0.0168  0.0115  -0.0023 696  PRO B O   
14089 C CB  . PRO B 698  ? 0.2783 0.3171 0.2894 0.0164  0.0097  -0.0067 696  PRO B CB  
14090 C CG  . PRO B 698  ? 0.3438 0.3826 0.3508 0.0169  0.0096  -0.0058 696  PRO B CG  
14091 C CD  . PRO B 698  ? 0.2844 0.3237 0.2916 0.0178  0.0079  -0.0049 696  PRO B CD  
14092 N N   . LEU B 699  ? 0.2122 0.2484 0.2296 0.0158  0.0117  -0.0046 697  LEU B N   
14093 C CA  . LEU B 699  ? 0.1852 0.2205 0.2039 0.0151  0.0133  -0.0034 697  LEU B CA  
14094 C C   . LEU B 699  ? 0.1906 0.2268 0.2073 0.0150  0.0152  -0.0031 697  LEU B C   
14095 O O   . LEU B 699  ? 0.2337 0.2695 0.2496 0.0146  0.0165  -0.0014 697  LEU B O   
14096 C CB  . LEU B 699  ? 0.1890 0.2244 0.2118 0.0144  0.0134  -0.0042 697  LEU B CB  
14097 C CG  . LEU B 699  ? 0.2156 0.2499 0.2404 0.0145  0.0118  -0.0046 697  LEU B CG  
14098 C CD1 . LEU B 699  ? 0.2066 0.2411 0.2348 0.0137  0.0119  -0.0056 697  LEU B CD1 
14099 C CD2 . LEU B 699  ? 0.2845 0.3164 0.3087 0.0146  0.0115  -0.0027 697  LEU B CD2 
14100 N N   . GLY B 700  ? 0.1799 0.2172 0.1956 0.0152  0.0152  -0.0049 698  GLY B N   
14101 C CA  . GLY B 700  ? 0.1921 0.2302 0.2062 0.0154  0.0171  -0.0052 698  GLY B CA  
14102 C C   . GLY B 700  ? 0.1895 0.2283 0.2059 0.0153  0.0174  -0.0069 698  GLY B C   
14103 O O   . GLY B 700  ? 0.1910 0.2295 0.2094 0.0151  0.0159  -0.0081 698  GLY B O   
14104 N N   . PRO B 701  ? 0.1830 0.2228 0.1994 0.0157  0.0193  -0.0071 699  PRO B N   
14105 C CA  . PRO B 701  ? 0.1730 0.2133 0.1913 0.0160  0.0195  -0.0088 699  PRO B CA  
14106 C C   . PRO B 701  ? 0.1752 0.2157 0.1983 0.0152  0.0188  -0.0088 699  PRO B C   
14107 O O   . PRO B 701  ? 0.1824 0.2235 0.2082 0.0145  0.0194  -0.0072 699  PRO B O   
14108 C CB  . PRO B 701  ? 0.1888 0.2307 0.2066 0.0167  0.0221  -0.0084 699  PRO B CB  
14109 C CG  . PRO B 701  ? 0.2118 0.2535 0.2254 0.0169  0.0227  -0.0072 699  PRO B CG  
14110 C CD  . PRO B 701  ? 0.2161 0.2567 0.2303 0.0159  0.0214  -0.0057 699  PRO B CD  
14111 N N   . ILE B 702  ? 0.1744 0.2141 0.1983 0.0152  0.0173  -0.0104 700  ILE B N   
14112 C CA  A ILE B 702  ? 0.1680 0.2077 0.1960 0.0146  0.0165  -0.0106 700  ILE B CA  
14113 C CA  B ILE B 702  ? 0.1680 0.2077 0.1960 0.0146  0.0164  -0.0106 700  ILE B CA  
14114 C C   . ILE B 702  ? 0.1721 0.2123 0.2017 0.0151  0.0169  -0.0119 700  ILE B C   
14115 O O   . ILE B 702  ? 0.1716 0.2108 0.1987 0.0158  0.0166  -0.0134 700  ILE B O   
14116 C CB  A ILE B 702  ? 0.1621 0.2006 0.1899 0.0141  0.0144  -0.0112 700  ILE B CB  
14117 C CB  B ILE B 702  ? 0.1621 0.2006 0.1898 0.0141  0.0143  -0.0113 700  ILE B CB  
14118 C CG1 A ILE B 702  ? 0.1660 0.2042 0.1934 0.0138  0.0139  -0.0097 700  ILE B CG1 
14119 C CG1 B ILE B 702  ? 0.1686 0.2068 0.1947 0.0140  0.0137  -0.0101 700  ILE B CG1 
14120 C CG2 A ILE B 702  ? 0.1750 0.2133 0.2062 0.0136  0.0135  -0.0119 700  ILE B CG2 
14121 C CG2 B ILE B 702  ? 0.1752 0.2135 0.2066 0.0135  0.0135  -0.0116 700  ILE B CG2 
14122 C CD1 A ILE B 702  ? 0.1670 0.2048 0.1942 0.0138  0.0121  -0.0101 700  ILE B CD1 
14123 C CD1 B ILE B 702  ? 0.1830 0.2210 0.2111 0.0136  0.0143  -0.0083 700  ILE B CD1 
14124 N N   . VAL B 703  ? 0.1618 0.2033 0.1954 0.0148  0.0175  -0.0113 701  VAL B N   
14125 C CA  . VAL B 703  ? 0.1568 0.1990 0.1925 0.0154  0.0177  -0.0124 701  VAL B CA  
14126 C C   . VAL B 703  ? 0.1452 0.1860 0.1826 0.0148  0.0157  -0.0132 701  VAL B C   
14127 O O   . VAL B 703  ? 0.1596 0.2003 0.1993 0.0138  0.0150  -0.0124 701  VAL B O   
14128 C CB  . VAL B 703  ? 0.1515 0.1965 0.1909 0.0153  0.0194  -0.0111 701  VAL B CB  
14129 C CG1 . VAL B 703  ? 0.1681 0.2142 0.2104 0.0161  0.0193  -0.0122 701  VAL B CG1 
14130 C CG2 . VAL B 703  ? 0.1730 0.2196 0.2102 0.0161  0.0216  -0.0104 701  VAL B CG2 
14131 N N   . CYS B 704  ? 0.1420 0.1814 0.1780 0.0154  0.0149  -0.0148 702  CYS B N   
14132 C CA  . CYS B 704  ? 0.1406 0.1785 0.1775 0.0147  0.0130  -0.0156 702  CYS B CA  
14133 C C   . CYS B 704  ? 0.1603 0.1985 0.1994 0.0155  0.0131  -0.0163 702  CYS B C   
14134 O O   . CYS B 704  ? 0.1570 0.1945 0.1943 0.0167  0.0135  -0.0174 702  CYS B O   
14135 C CB  . CYS B 704  ? 0.1518 0.1877 0.1850 0.0145  0.0118  -0.0167 702  CYS B CB  
14136 S SG  . CYS B 704  ? 0.1698 0.2058 0.2005 0.0138  0.0114  -0.0160 702  CYS B SG  
14137 N N   . ILE B 705  ? 0.1392 0.1783 0.1820 0.0149  0.0125  -0.0158 703  ILE B N   
14138 C CA  . ILE B 705  ? 0.1520 0.1919 0.1975 0.0156  0.0124  -0.0163 703  ILE B CA  
14139 C C   . ILE B 705  ? 0.1477 0.1857 0.1937 0.0149  0.0104  -0.0169 703  ILE B C   
14140 O O   . ILE B 705  ? 0.1505 0.1881 0.1972 0.0137  0.0095  -0.0164 703  ILE B O   
14141 C CB  . ILE B 705  ? 0.1475 0.1906 0.1973 0.0153  0.0134  -0.0149 703  ILE B CB  
14142 C CG1 . ILE B 705  ? 0.1823 0.2277 0.2317 0.0162  0.0157  -0.0143 703  ILE B CG1 
14143 C CG2 . ILE B 705  ? 0.1587 0.2029 0.2119 0.0159  0.0128  -0.0153 703  ILE B CG2 
14144 C CD1 . ILE B 705  ? 0.1860 0.2347 0.2393 0.0152  0.0168  -0.0125 703  ILE B CD1 
14145 N N   . SER B 706  ? 0.1554 0.1918 0.2003 0.0158  0.0096  -0.0181 704  SER B N   
14146 C CA  . SER B 706  ? 0.1579 0.1919 0.2019 0.0150  0.0077  -0.0187 704  SER B CA  
14147 C C   . SER B 706  ? 0.1657 0.1996 0.2118 0.0158  0.0069  -0.0191 704  SER B C   
14148 O O   . SER B 706  ? 0.1639 0.1991 0.2115 0.0173  0.0078  -0.0193 704  SER B O   
14149 C CB  . SER B 706  ? 0.1673 0.1985 0.2067 0.0149  0.0072  -0.0197 704  SER B CB  
14150 O OG  . SER B 706  ? 0.1537 0.1839 0.1912 0.0164  0.0079  -0.0205 704  SER B OG  
14151 N N   . PRO B 707  ? 0.1584 0.1909 0.2048 0.0148  0.0053  -0.0193 705  PRO B N   
14152 C CA  . PRO B 707  ? 0.1642 0.1964 0.2125 0.0155  0.0042  -0.0196 705  PRO B CA  
14153 C C   . PRO B 707  ? 0.1742 0.2030 0.2192 0.0163  0.0033  -0.0206 705  PRO B C   
14154 O O   . PRO B 707  ? 0.1925 0.2190 0.2337 0.0159  0.0033  -0.0211 705  PRO B O   
14155 C CB  . PRO B 707  ? 0.1659 0.1974 0.2148 0.0139  0.0027  -0.0193 705  PRO B CB  
14156 C CG  . PRO B 707  ? 0.1634 0.1935 0.2090 0.0129  0.0027  -0.0194 705  PRO B CG  
14157 C CD  . PRO B 707  ? 0.1654 0.1969 0.2105 0.0133  0.0044  -0.0191 705  PRO B CD  
14158 N N   . TRP B 708  ? 0.1594 0.1878 0.2058 0.0175  0.0025  -0.0209 706  TRP B N   
14159 C CA  . TRP B 708  ? 0.1616 0.1863 0.2046 0.0185  0.0015  -0.0218 706  TRP B CA  
14160 C C   . TRP B 708  ? 0.1539 0.1752 0.1941 0.0168  -0.0002 -0.0220 706  TRP B C   
14161 O O   . TRP B 708  ? 0.1807 0.1982 0.2170 0.0168  -0.0010 -0.0226 706  TRP B O   
14162 C CB  . TRP B 708  ? 0.1693 0.1945 0.2145 0.0207  0.0011  -0.0221 706  TRP B CB  
14163 C CG  . TRP B 708  ? 0.1698 0.1952 0.2173 0.0200  -0.0006 -0.0216 706  TRP B CG  
14164 C CD1 . TRP B 708  ? 0.2137 0.2428 0.2658 0.0196  -0.0006 -0.0209 706  TRP B CD1 
14165 C CD2 . TRP B 708  ? 0.1906 0.2121 0.2354 0.0195  -0.0026 -0.0219 706  TRP B CD2 
14166 N NE1 . TRP B 708  ? 0.2038 0.2316 0.2562 0.0190  -0.0026 -0.0207 706  TRP B NE1 
14167 C CE2 . TRP B 708  ? 0.1710 0.1941 0.2189 0.0189  -0.0038 -0.0213 706  TRP B CE2 
14168 C CE3 . TRP B 708  ? 0.1930 0.2095 0.2329 0.0192  -0.0036 -0.0225 706  TRP B CE3 
14169 C CZ2 . TRP B 708  ? 0.1858 0.2060 0.2319 0.0183  -0.0058 -0.0213 706  TRP B CZ2 
14170 C CZ3 . TRP B 708  ? 0.1852 0.1989 0.2235 0.0184  -0.0055 -0.0224 706  TRP B CZ3 
14171 C CH2 . TRP B 708  ? 0.2006 0.2161 0.2419 0.0181  -0.0066 -0.0218 706  TRP B CH2 
14172 N N   . ASN B 709  ? 0.1694 0.1919 0.2112 0.0153  -0.0009 -0.0214 707  ASN B N   
14173 C CA  . ASN B 709  ? 0.1727 0.1924 0.2124 0.0141  -0.0027 -0.0214 707  ASN B CA  
14174 C C   . ASN B 709  ? 0.1918 0.2098 0.2277 0.0123  -0.0028 -0.0215 707  ASN B C   
14175 O O   . ASN B 709  ? 0.2096 0.2247 0.2428 0.0114  -0.0041 -0.0216 707  ASN B O   
14176 C CB  . ASN B 709  ? 0.1741 0.1955 0.2166 0.0134  -0.0035 -0.0209 707  ASN B CB  
14177 C CG  . ASN B 709  ? 0.1901 0.2136 0.2334 0.0121  -0.0027 -0.0205 707  ASN B CG  
14178 O OD1 . ASN B 709  ? 0.2360 0.2619 0.2813 0.0124  -0.0014 -0.0201 707  ASN B OD1 
14179 N ND2 . ASN B 709  ? 0.2192 0.2417 0.2607 0.0108  -0.0035 -0.0204 707  ASN B ND2 
14180 N N   . PHE B 710  ? 0.1775 0.1973 0.2134 0.0118  -0.0016 -0.0214 708  PHE B N   
14181 C CA  . PHE B 710  ? 0.2052 0.2240 0.2378 0.0103  -0.0016 -0.0215 708  PHE B CA  
14182 C C   . PHE B 710  ? 0.1926 0.2112 0.2238 0.0112  -0.0005 -0.0219 708  PHE B C   
14183 O O   . PHE B 710  ? 0.1824 0.2033 0.2142 0.0110  0.0006  -0.0216 708  PHE B O   
14184 C CB  . PHE B 710  ? 0.1845 0.2060 0.2181 0.0091  -0.0013 -0.0209 708  PHE B CB  
14185 C CG  . PHE B 710  ? 0.2158 0.2374 0.2502 0.0084  -0.0022 -0.0206 708  PHE B CG  
14186 C CD1 . PHE B 710  ? 0.2362 0.2553 0.2686 0.0077  -0.0036 -0.0207 708  PHE B CD1 
14187 C CD2 . PHE B 710  ? 0.2262 0.2502 0.2630 0.0084  -0.0019 -0.0202 708  PHE B CD2 
14188 C CE1 . PHE B 710  ? 0.2346 0.2538 0.2674 0.0071  -0.0044 -0.0205 708  PHE B CE1 
14189 C CE2 . PHE B 710  ? 0.2333 0.2571 0.2703 0.0079  -0.0028 -0.0201 708  PHE B CE2 
14190 C CZ  . PHE B 710  ? 0.2476 0.2692 0.2826 0.0073  -0.0040 -0.0203 708  PHE B CZ  
14191 N N   . PRO B 711  ? 0.1914 0.2069 0.2205 0.0122  -0.0009 -0.0226 709  PRO B N   
14192 C CA  . PRO B 711  ? 0.1916 0.2071 0.2199 0.0138  0.0003  -0.0232 709  PRO B CA  
14193 C C   . PRO B 711  ? 0.1876 0.2022 0.2125 0.0127  0.0005  -0.0234 709  PRO B C   
14194 O O   . PRO B 711  ? 0.1914 0.2065 0.2156 0.0139  0.0017  -0.0238 709  PRO B O   
14195 C CB  . PRO B 711  ? 0.1982 0.2100 0.2248 0.0155  -0.0005 -0.0239 709  PRO B CB  
14196 C CG  . PRO B 711  ? 0.1991 0.2076 0.2234 0.0137  -0.0024 -0.0238 709  PRO B CG  
14197 C CD  . PRO B 711  ? 0.1836 0.1954 0.2109 0.0123  -0.0025 -0.0229 709  PRO B CD  
14198 N N   . LEU B 712  ? 0.1626 0.1761 0.1853 0.0105  -0.0005 -0.0233 710  LEU B N   
14199 C CA  . LEU B 712  ? 0.1762 0.1899 0.1963 0.0092  -0.0005 -0.0234 710  LEU B CA  
14200 C C   . LEU B 712  ? 0.1828 0.2004 0.2048 0.0079  -0.0001 -0.0225 710  LEU B C   
14201 O O   . LEU B 712  ? 0.1966 0.2162 0.2183 0.0078  0.0006  -0.0224 710  LEU B O   
14202 C CB  . LEU B 712  ? 0.1789 0.1884 0.1946 0.0075  -0.0020 -0.0239 710  LEU B CB  
14203 C CG  . LEU B 712  ? 0.1678 0.1773 0.1806 0.0059  -0.0023 -0.0240 710  LEU B CG  
14204 C CD1 . LEU B 712  ? 0.1860 0.1950 0.1973 0.0076  -0.0013 -0.0248 710  LEU B CD1 
14205 C CD2 . LEU B 712  ? 0.2352 0.2406 0.2439 0.0037  -0.0041 -0.0243 710  LEU B CD2 
14206 N N   . ALA B 713  ? 0.1675 0.1865 0.1915 0.0071  -0.0006 -0.0219 711  ALA B N   
14207 C CA  . ALA B 713  ? 0.1758 0.1981 0.2009 0.0060  -0.0004 -0.0213 711  ALA B CA  
14208 C C   . ALA B 713  ? 0.1678 0.1931 0.1958 0.0072  0.0009  -0.0208 711  ALA B C   
14209 O O   . ALA B 713  ? 0.1732 0.2005 0.2009 0.0070  0.0014  -0.0205 711  ALA B O   
14210 C CB  . ALA B 713  ? 0.1930 0.2155 0.2188 0.0049  -0.0013 -0.0209 711  ALA B CB  
14211 N N   . ILE B 714  ? 0.1738 0.1995 0.2046 0.0084  0.0013  -0.0206 712  ILE B N   
14212 C CA  . ILE B 714  ? 0.1725 0.2005 0.2058 0.0093  0.0025  -0.0200 712  ILE B CA  
14213 C C   . ILE B 714  ? 0.1738 0.2021 0.2062 0.0102  0.0036  -0.0201 712  ILE B C   
14214 O O   . ILE B 714  ? 0.1649 0.1949 0.1975 0.0103  0.0044  -0.0195 712  ILE B O   
14215 C CB  . ILE B 714  ? 0.1683 0.1967 0.2048 0.0100  0.0025  -0.0198 712  ILE B CB  
14216 C CG1 . ILE B 714  ? 0.2046 0.2331 0.2416 0.0091  0.0014  -0.0196 712  ILE B CG1 
14217 C CG2 . ILE B 714  ? 0.1811 0.2116 0.2200 0.0107  0.0037  -0.0191 712  ILE B CG2 
14218 C CD1 . ILE B 714  ? 0.3021 0.3309 0.3419 0.0095  0.0012  -0.0194 712  ILE B CD1 
14219 N N   . PHE B 715  ? 0.1608 0.1870 0.1917 0.0109  0.0036  -0.0208 713  PHE B N   
14220 C CA  . PHE B 715  ? 0.1467 0.1727 0.1760 0.0119  0.0047  -0.0211 713  PHE B CA  
14221 C C   . PHE B 715  ? 0.1570 0.1835 0.1836 0.0110  0.0046  -0.0210 713  PHE B C   
14222 O O   . PHE B 715  ? 0.1651 0.1933 0.1918 0.0115  0.0056  -0.0205 713  PHE B O   
14223 C CB  . PHE B 715  ? 0.1560 0.1789 0.1830 0.0128  0.0043  -0.0222 713  PHE B CB  
14224 C CG  . PHE B 715  ? 0.1657 0.1879 0.1903 0.0141  0.0054  -0.0227 713  PHE B CG  
14225 C CD1 . PHE B 715  ? 0.1605 0.1847 0.1871 0.0158  0.0071  -0.0225 713  PHE B CD1 
14226 C CD2 . PHE B 715  ? 0.1741 0.1938 0.1942 0.0134  0.0047  -0.0235 713  PHE B CD2 
14227 C CE1 . PHE B 715  ? 0.1786 0.2024 0.2027 0.0171  0.0082  -0.0230 713  PHE B CE1 
14228 C CE2 . PHE B 715  ? 0.1809 0.1997 0.1983 0.0146  0.0056  -0.0241 713  PHE B CE2 
14229 C CZ  . PHE B 715  ? 0.1698 0.1906 0.1891 0.0166  0.0075  -0.0239 713  PHE B CZ  
14230 N N   . THR B 716  ? 0.1501 0.1752 0.1744 0.0095  0.0032  -0.0214 714  THR B N   
14231 C CA  . THR B 716  ? 0.1541 0.1799 0.1759 0.0083  0.0028  -0.0214 714  THR B CA  
14232 C C   . THR B 716  ? 0.1561 0.1855 0.1801 0.0081  0.0032  -0.0204 714  THR B C   
14233 O O   . THR B 716  ? 0.1623 0.1932 0.1853 0.0082  0.0035  -0.0200 714  THR B O   
14234 C CB  . THR B 716  ? 0.1670 0.1909 0.1863 0.0064  0.0012  -0.0218 714  THR B CB  
14235 O OG1 . THR B 716  ? 0.1904 0.2102 0.2070 0.0068  0.0008  -0.0228 714  THR B OG1 
14236 C CG2 . THR B 716  ? 0.1855 0.2110 0.2029 0.0050  0.0006  -0.0217 714  THR B CG2 
14237 N N   . GLY B 717  ? 0.1597 0.1902 0.1863 0.0079  0.0029  -0.0199 715  GLY B N   
14238 C CA  . GLY B 717  ? 0.1694 0.2028 0.1977 0.0079  0.0031  -0.0191 715  GLY B CA  
14239 C C   . GLY B 717  ? 0.1616 0.1960 0.1909 0.0092  0.0043  -0.0184 715  GLY B C   
14240 O O   . GLY B 717  ? 0.1599 0.1960 0.1885 0.0093  0.0044  -0.0179 715  GLY B O   
14241 N N   . GLN B 718  ? 0.1483 0.1819 0.1792 0.0101  0.0052  -0.0183 716  GLN B N   
14242 C CA  . GLN B 718  ? 0.1417 0.1763 0.1736 0.0110  0.0064  -0.0175 716  GLN B CA  
14243 C C   . GLN B 718  ? 0.1504 0.1852 0.1795 0.0113  0.0069  -0.0175 716  GLN B C   
14244 O O   . GLN B 718  ? 0.1591 0.1950 0.1877 0.0115  0.0073  -0.0166 716  GLN B O   
14245 C CB  . GLN B 718  ? 0.1436 0.1780 0.1779 0.0116  0.0073  -0.0173 716  GLN B CB  
14246 C CG  . GLN B 718  ? 0.1424 0.1766 0.1795 0.0113  0.0065  -0.0172 716  GLN B CG  
14247 C CD  . GLN B 718  ? 0.1619 0.1964 0.2018 0.0118  0.0073  -0.0168 716  GLN B CD  
14248 O OE1 . GLN B 718  ? 0.1646 0.1996 0.2069 0.0115  0.0071  -0.0162 716  GLN B OE1 
14249 N NE2 . GLN B 718  ? 0.1690 0.2035 0.2086 0.0126  0.0080  -0.0173 716  GLN B NE2 
14250 N N   . ILE B 719  ? 0.1437 0.1768 0.1705 0.0113  0.0069  -0.0184 717  ILE B N   
14251 C CA  . ILE B 719  ? 0.1551 0.1878 0.1787 0.0117  0.0074  -0.0187 717  ILE B CA  
14252 C C   . ILE B 719  ? 0.1634 0.1971 0.1850 0.0107  0.0063  -0.0185 717  ILE B C   
14253 O O   . ILE B 719  ? 0.1644 0.1990 0.1845 0.0111  0.0067  -0.0179 717  ILE B O   
14254 C CB  . ILE B 719  ? 0.1750 0.2051 0.1962 0.0120  0.0072  -0.0200 717  ILE B CB  
14255 C CG1 . ILE B 719  ? 0.1688 0.1988 0.1921 0.0134  0.0085  -0.0200 717  ILE B CG1 
14256 C CG2 . ILE B 719  ? 0.2188 0.2478 0.2357 0.0121  0.0072  -0.0205 717  ILE B CG2 
14257 C CD1 . ILE B 719  ? 0.2313 0.2583 0.2527 0.0140  0.0081  -0.0214 717  ILE B CD1 
14258 N N   . ALA B 720  ? 0.1525 0.1862 0.1741 0.0095  0.0049  -0.0189 718  ALA B N   
14259 C CA  . ALA B 720  ? 0.1558 0.1913 0.1760 0.0085  0.0038  -0.0187 718  ALA B CA  
14260 C C   . ALA B 720  ? 0.1540 0.1921 0.1757 0.0092  0.0042  -0.0175 718  ALA B C   
14261 O O   . ALA B 720  ? 0.1545 0.1940 0.1746 0.0092  0.0038  -0.0171 718  ALA B O   
14262 C CB  . ALA B 720  ? 0.1634 0.1990 0.1838 0.0069  0.0025  -0.0191 718  ALA B CB  
14263 N N   . ALA B 721  ? 0.1516 0.1902 0.1763 0.0098  0.0046  -0.0170 719  ALA B N   
14264 C CA  . ALA B 721  ? 0.1467 0.1871 0.1727 0.0106  0.0048  -0.0159 719  ALA B CA  
14265 C C   . ALA B 721  ? 0.1398 0.1797 0.1646 0.0116  0.0058  -0.0152 719  ALA B C   
14266 O O   . ALA B 721  ? 0.1530 0.1943 0.1768 0.0120  0.0055  -0.0144 719  ALA B O   
14267 C CB  . ALA B 721  ? 0.1552 0.1952 0.1841 0.0110  0.0050  -0.0157 719  ALA B CB  
14268 N N   . ALA B 722  ? 0.1437 0.1821 0.1688 0.0119  0.0070  -0.0152 720  ALA B N   
14269 C CA  . ALA B 722  ? 0.1377 0.1759 0.1616 0.0127  0.0082  -0.0143 720  ALA B CA  
14270 C C   . ALA B 722  ? 0.1519 0.1904 0.1721 0.0126  0.0078  -0.0146 720  ALA B C   
14271 O O   . ALA B 722  ? 0.1578 0.1970 0.1766 0.0132  0.0080  -0.0136 720  ALA B O   
14272 C CB  . ALA B 722  ? 0.1553 0.1926 0.1803 0.0130  0.0096  -0.0144 720  ALA B CB  
14273 N N   . LEU B 723  ? 0.1596 0.1972 0.1779 0.0120  0.0072  -0.0159 721  LEU B N   
14274 C CA  . LEU B 723  ? 0.1625 0.1999 0.1769 0.0117  0.0066  -0.0163 721  LEU B CA  
14275 C C   . LEU B 723  ? 0.1637 0.2034 0.1777 0.0113  0.0052  -0.0157 721  LEU B C   
14276 O O   . LEU B 723  ? 0.1737 0.2140 0.1853 0.0117  0.0050  -0.0152 721  LEU B O   
14277 C CB  . LEU B 723  ? 0.1727 0.2081 0.1851 0.0108  0.0058  -0.0178 721  LEU B CB  
14278 C CG  . LEU B 723  ? 0.1725 0.2055 0.1840 0.0116  0.0070  -0.0187 721  LEU B CG  
14279 C CD1 . LEU B 723  ? 0.1830 0.2135 0.1926 0.0107  0.0057  -0.0202 721  LEU B CD1 
14280 C CD2 . LEU B 723  ? 0.1885 0.2210 0.1967 0.0127  0.0081  -0.0186 721  LEU B CD2 
14281 N N   . VAL B 724  ? 0.1444 0.1856 0.1606 0.0106  0.0041  -0.0158 722  VAL B N   
14282 C CA  . VAL B 724  ? 0.1485 0.1926 0.1645 0.0102  0.0028  -0.0153 722  VAL B CA  
14283 C C   . VAL B 724  ? 0.1540 0.1993 0.1708 0.0118  0.0032  -0.0140 722  VAL B C   
14284 O O   . VAL B 724  ? 0.1750 0.2224 0.1907 0.0121  0.0023  -0.0134 722  VAL B O   
14285 C CB  . VAL B 724  ? 0.1511 0.1969 0.1691 0.0090  0.0017  -0.0158 722  VAL B CB  
14286 C CG1 . VAL B 724  ? 0.1769 0.2236 0.1983 0.0100  0.0022  -0.0153 722  VAL B CG1 
14287 C CG2 . VAL B 724  ? 0.1589 0.2079 0.1759 0.0081  0.0001  -0.0157 722  VAL B CG2 
14288 N N   . ALA B 725  ? 0.1688 0.2128 0.1876 0.0127  0.0044  -0.0133 723  ALA B N   
14289 C CA  . ALA B 725  ? 0.1739 0.2179 0.1929 0.0140  0.0049  -0.0119 723  ALA B CA  
14290 C C   . ALA B 725  ? 0.1812 0.2242 0.1972 0.0145  0.0056  -0.0112 723  ALA B C   
14291 O O   . ALA B 725  ? 0.2084 0.2511 0.2240 0.0155  0.0059  -0.0098 723  ALA B O   
14292 C CB  . ALA B 725  ? 0.1808 0.2232 0.2026 0.0144  0.0058  -0.0115 723  ALA B CB  
14293 N N   . GLY B 726  ? 0.1649 0.2072 0.1784 0.0138  0.0058  -0.0121 724  GLY B N   
14294 C CA  . GLY B 726  ? 0.1772 0.2187 0.1872 0.0143  0.0064  -0.0115 724  GLY B CA  
14295 C C   . GLY B 726  ? 0.1941 0.2338 0.2039 0.0147  0.0085  -0.0113 724  GLY B C   
14296 O O   . GLY B 726  ? 0.2058 0.2451 0.2128 0.0153  0.0093  -0.0104 724  GLY B O   
14297 N N   . ASN B 727  ? 0.1739 0.2129 0.1863 0.0144  0.0093  -0.0119 725  ASN B N   
14298 C CA  . ASN B 727  ? 0.1699 0.2080 0.1830 0.0148  0.0113  -0.0115 725  ASN B CA  
14299 C C   . ASN B 727  ? 0.1660 0.2032 0.1776 0.0148  0.0117  -0.0132 725  ASN B C   
14300 O O   . ASN B 727  ? 0.1928 0.2295 0.2051 0.0142  0.0106  -0.0145 725  ASN B O   
14301 C CB  . ASN B 727  ? 0.1760 0.2142 0.1935 0.0146  0.0117  -0.0110 725  ASN B CB  
14302 C CG  . ASN B 727  ? 0.1920 0.2304 0.2108 0.0147  0.0110  -0.0097 725  ASN B CG  
14303 O OD1 . ASN B 727  ? 0.1931 0.2310 0.2113 0.0151  0.0118  -0.0081 725  ASN B OD1 
14304 N ND2 . ASN B 727  ? 0.1756 0.2145 0.1962 0.0145  0.0096  -0.0103 725  ASN B ND2 
14305 N N   . PRO B 728  ? 0.1727 0.2094 0.1820 0.0155  0.0133  -0.0131 726  PRO B N   
14306 C CA  . PRO B 728  ? 0.1827 0.2182 0.1910 0.0160  0.0140  -0.0147 726  PRO B CA  
14307 C C   . PRO B 728  ? 0.1959 0.2319 0.2087 0.0161  0.0148  -0.0147 726  PRO B C   
14308 O O   . PRO B 728  ? 0.1885 0.2259 0.2046 0.0159  0.0155  -0.0133 726  PRO B O   
14309 C CB  . PRO B 728  ? 0.1899 0.2254 0.1948 0.0171  0.0158  -0.0144 726  PRO B CB  
14310 C CG  . PRO B 728  ? 0.2058 0.2428 0.2121 0.0170  0.0168  -0.0122 726  PRO B CG  
14311 C CD  . PRO B 728  ? 0.1812 0.2185 0.1891 0.0161  0.0148  -0.0115 726  PRO B CD  
14312 N N   . VAL B 729  ? 0.1659 0.2007 0.1788 0.0163  0.0145  -0.0163 727  VAL B N   
14313 C CA  . VAL B 729  ? 0.1738 0.2090 0.1909 0.0164  0.0147  -0.0165 727  VAL B CA  
14314 C C   . VAL B 729  ? 0.1950 0.2300 0.2119 0.0178  0.0162  -0.0173 727  VAL B C   
14315 O O   . VAL B 729  ? 0.1814 0.2144 0.1944 0.0186  0.0162  -0.0187 727  VAL B O   
14316 C CB  . VAL B 729  ? 0.1650 0.1988 0.1826 0.0154  0.0126  -0.0175 727  VAL B CB  
14317 C CG1 . VAL B 729  ? 0.1640 0.1975 0.1849 0.0156  0.0127  -0.0180 727  VAL B CG1 
14318 C CG2 . VAL B 729  ? 0.1879 0.2227 0.2068 0.0143  0.0114  -0.0166 727  VAL B CG2 
14319 N N   . LEU B 730  ? 0.1641 0.2011 0.1852 0.0181  0.0174  -0.0165 728  LEU B N   
14320 C CA  . LEU B 730  ? 0.1741 0.2116 0.1965 0.0195  0.0185  -0.0173 728  LEU B CA  
14321 C C   . LEU B 730  ? 0.1470 0.1838 0.1727 0.0191  0.0171  -0.0179 728  LEU B C   
14322 O O   . LEU B 730  ? 0.1766 0.2149 0.2062 0.0181  0.0168  -0.0168 728  LEU B O   
14323 C CB  . LEU B 730  ? 0.1780 0.2189 0.2033 0.0200  0.0208  -0.0158 728  LEU B CB  
14324 C CG  . LEU B 730  ? 0.1820 0.2241 0.2044 0.0204  0.0226  -0.0148 728  LEU B CG  
14325 C CD1 . LEU B 730  ? 0.1922 0.2320 0.2089 0.0218  0.0228  -0.0164 728  LEU B CD1 
14326 C CD2 . LEU B 730  ? 0.1874 0.2295 0.2095 0.0189  0.0220  -0.0131 728  LEU B CD2 
14327 N N   . ALA B 731  ? 0.1601 0.1942 0.1838 0.0197  0.0160  -0.0195 729  ALA B N   
14328 C CA  . ALA B 731  ? 0.1505 0.1833 0.1762 0.0191  0.0144  -0.0201 729  ALA B CA  
14329 C C   . ALA B 731  ? 0.1657 0.1995 0.1940 0.0208  0.0152  -0.0205 729  ALA B C   
14330 O O   . ALA B 731  ? 0.1616 0.1939 0.1873 0.0226  0.0158  -0.0217 729  ALA B O   
14331 C CB  . ALA B 731  ? 0.1849 0.2139 0.2065 0.0185  0.0125  -0.0215 729  ALA B CB  
14332 N N   . LYS B 732  ? 0.1514 0.1874 0.1845 0.0203  0.0152  -0.0196 730  LYS B N   
14333 C CA  . LYS B 732  ? 0.1628 0.2005 0.1991 0.0218  0.0157  -0.0198 730  LYS B CA  
14334 C C   . LYS B 732  ? 0.1577 0.1935 0.1955 0.0212  0.0137  -0.0203 730  LYS B C   
14335 O O   . LYS B 732  ? 0.1684 0.2056 0.2096 0.0198  0.0129  -0.0194 730  LYS B O   
14336 C CB  . LYS B 732  ? 0.1881 0.2304 0.2291 0.0215  0.0173  -0.0181 730  LYS B CB  
14337 C CG  . LYS B 732  ? 0.1790 0.2245 0.2224 0.0236  0.0190  -0.0182 730  LYS B CG  
14338 C CD  . LYS B 732  ? 0.1818 0.2267 0.2272 0.0248  0.0178  -0.0191 730  LYS B CD  
14339 C CE  . LYS B 732  ? 0.1704 0.2168 0.2205 0.0231  0.0165  -0.0182 730  LYS B CE  
14340 N NZ  . LYS B 732  ? 0.1667 0.2123 0.2183 0.0244  0.0151  -0.0191 730  LYS B NZ  
14341 N N   . PRO B 733  ? 0.1536 0.1861 0.1888 0.0222  0.0126  -0.0217 731  PRO B N   
14342 C CA  . PRO B 733  ? 0.1659 0.1962 0.2018 0.0215  0.0106  -0.0221 731  PRO B CA  
14343 C C   . PRO B 733  ? 0.1536 0.1863 0.1939 0.0229  0.0107  -0.0218 731  PRO B C   
14344 O O   . PRO B 733  ? 0.1610 0.1966 0.2031 0.0247  0.0124  -0.0217 731  PRO B O   
14345 C CB  . PRO B 733  ? 0.1831 0.2087 0.2141 0.0223  0.0095  -0.0236 731  PRO B CB  
14346 C CG  . PRO B 733  ? 0.1852 0.2111 0.2142 0.0246  0.0113  -0.0243 731  PRO B CG  
14347 C CD  . PRO B 733  ? 0.1703 0.2002 0.2009 0.0239  0.0131  -0.0231 731  PRO B CD  
14348 N N   . ALA B 734  ? 0.1636 0.1955 0.2057 0.0219  0.0090  -0.0217 732  ALA B N   
14349 C CA  . ALA B 734  ? 0.1551 0.1891 0.2012 0.0231  0.0087  -0.0215 732  ALA B CA  
14350 C C   . ALA B 734  ? 0.1734 0.2063 0.2183 0.0260  0.0090  -0.0226 732  ALA B C   
14351 O O   . ALA B 734  ? 0.1865 0.2150 0.2266 0.0267  0.0085  -0.0238 732  ALA B O   
14352 C CB  . ALA B 734  ? 0.1838 0.2158 0.2305 0.0217  0.0064  -0.0214 732  ALA B CB  
14353 N N   . GLU B 735  ? 0.1653 0.2021 0.2144 0.0277  0.0098  -0.0222 733  GLU B N   
14354 C CA  . GLU B 735  ? 0.1831 0.2194 0.2313 0.0310  0.0103  -0.0233 733  GLU B CA  
14355 C C   . GLU B 735  ? 0.1637 0.1947 0.2090 0.0318  0.0081  -0.0244 733  GLU B C   
14356 O O   . GLU B 735  ? 0.1789 0.2069 0.2209 0.0344  0.0081  -0.0257 733  GLU B O   
14357 C CB  . GLU B 735  ? 0.1930 0.2357 0.2470 0.0326  0.0116  -0.0225 733  GLU B CB  
14358 C CG  . GLU B 735  ? 0.2450 0.2903 0.3040 0.0313  0.0102  -0.0215 733  GLU B CG  
14359 C CD  . GLU B 735  ? 0.2620 0.3109 0.3244 0.0284  0.0108  -0.0199 733  GLU B CD  
14360 O OE1 . GLU B 735  ? 0.2466 0.2940 0.3064 0.0266  0.0114  -0.0197 733  GLU B OE1 
14361 O OE2 . GLU B 735  ? 0.2672 0.3205 0.3350 0.0278  0.0105  -0.0189 733  GLU B OE2 
14362 N N   . GLU B 736  ? 0.1730 0.2025 0.2191 0.0298  0.0060  -0.0239 734  GLU B N   
14363 C CA  . GLU B 736  ? 0.1981 0.2226 0.2415 0.0305  0.0038  -0.0247 734  GLU B CA  
14364 C C   . GLU B 736  ? 0.1930 0.2113 0.2299 0.0296  0.0030  -0.0256 734  GLU B C   
14365 O O   . GLU B 736  ? 0.2175 0.2307 0.2510 0.0307  0.0015  -0.0265 734  GLU B O   
14366 C CB  . GLU B 736  ? 0.1846 0.2095 0.2304 0.0284  0.0020  -0.0238 734  GLU B CB  
14367 C CG  . GLU B 736  ? 0.2084 0.2389 0.2605 0.0291  0.0021  -0.0229 734  GLU B CG  
14368 C CD  . GLU B 736  ? 0.1992 0.2343 0.2550 0.0269  0.0033  -0.0218 734  GLU B CD  
14369 O OE1 . GLU B 736  ? 0.2025 0.2374 0.2564 0.0257  0.0046  -0.0216 734  GLU B OE1 
14370 O OE2 . GLU B 736  ? 0.2867 0.3255 0.3472 0.0264  0.0028  -0.0209 734  GLU B OE2 
14371 N N   . THR B 737  ? 0.1858 0.2041 0.2209 0.0274  0.0037  -0.0254 735  THR B N   
14372 C CA  . THR B 737  ? 0.1939 0.2069 0.2235 0.0257  0.0026  -0.0260 735  THR B CA  
14373 C C   . THR B 737  ? 0.1809 0.1937 0.2075 0.0256  0.0040  -0.0265 735  THR B C   
14374 O O   . THR B 737  ? 0.1993 0.2117 0.2242 0.0231  0.0038  -0.0262 735  THR B O   
14375 C CB  . THR B 737  ? 0.1877 0.2006 0.2178 0.0225  0.0013  -0.0251 735  THR B CB  
14376 O OG1 . THR B 737  ? 0.1881 0.2060 0.2220 0.0213  0.0025  -0.0241 735  THR B OG1 
14377 C CG2 . THR B 737  ? 0.2086 0.2203 0.2401 0.0226  -0.0005 -0.0249 735  THR B CG2 
14378 N N   . PRO B 738  ? 0.1787 0.1917 0.2043 0.0283  0.0054  -0.0273 736  PRO B N   
14379 C CA  . PRO B 738  ? 0.1855 0.1982 0.2079 0.0283  0.0067  -0.0278 736  PRO B CA  
14380 C C   . PRO B 738  ? 0.1966 0.2030 0.2125 0.0273  0.0053  -0.0290 736  PRO B C   
14381 O O   . PRO B 738  ? 0.1871 0.1933 0.2003 0.0262  0.0059  -0.0291 736  PRO B O   
14382 C CB  . PRO B 738  ? 0.1890 0.2038 0.2122 0.0318  0.0087  -0.0284 736  PRO B CB  
14383 C CG  . PRO B 738  ? 0.2065 0.2190 0.2302 0.0340  0.0074  -0.0291 736  PRO B CG  
14384 C CD  . PRO B 738  ? 0.1957 0.2092 0.2229 0.0317  0.0058  -0.0279 736  PRO B CD  
14385 N N   . LEU B 739  ? 0.1907 0.1918 0.2038 0.0276  0.0034  -0.0297 737  LEU B N   
14386 C CA  . LEU B 739  ? 0.2038 0.1983 0.2103 0.0269  0.0020  -0.0309 737  LEU B CA  
14387 C C   . LEU B 739  ? 0.1892 0.1833 0.1943 0.0229  0.0009  -0.0302 737  LEU B C   
14388 O O   . LEU B 739  ? 0.1958 0.1880 0.1969 0.0218  0.0008  -0.0308 737  LEU B O   
14389 C CB  . LEU B 739  ? 0.1887 0.1772 0.1924 0.0281  0.0001  -0.0317 737  LEU B CB  
14390 C CG  . LEU B 739  ? 0.1934 0.1822 0.1982 0.0325  0.0011  -0.0325 737  LEU B CG  
14391 C CD1 . LEU B 739  ? 0.2358 0.2180 0.2374 0.0335  -0.0012 -0.0332 737  LEU B CD1 
14392 C CD2 . LEU B 739  ? 0.2174 0.2057 0.2191 0.0350  0.0028  -0.0339 737  LEU B CD2 
14393 N N   . ILE B 740  ? 0.1843 0.1804 0.1925 0.0208  0.0000  -0.0290 738  ILE B N   
14394 C CA  . ILE B 740  ? 0.1751 0.1714 0.1822 0.0172  -0.0009 -0.0283 738  ILE B CA  
14395 C C   . ILE B 740  ? 0.1851 0.1864 0.1941 0.0167  0.0007  -0.0278 738  ILE B C   
14396 O O   . ILE B 740  ? 0.1895 0.1907 0.1962 0.0145  0.0002  -0.0277 738  ILE B O   
14397 C CB  . ILE B 740  ? 0.2152 0.2124 0.2247 0.0153  -0.0021 -0.0273 738  ILE B CB  
14398 C CG1 . ILE B 740  ? 0.1943 0.1916 0.2022 0.0118  -0.0031 -0.0266 738  ILE B CG1 
14399 C CG2 . ILE B 740  ? 0.2318 0.2344 0.2471 0.0162  -0.0009 -0.0263 738  ILE B CG2 
14400 C CD1 . ILE B 740  ? 0.2390 0.2307 0.2412 0.0102  -0.0047 -0.0274 738  ILE B CD1 
14401 N N   . ALA B 741  ? 0.1754 0.1812 0.1884 0.0185  0.0026  -0.0273 739  ALA B N   
14402 C CA  . ALA B 741  ? 0.1791 0.1890 0.1935 0.0182  0.0041  -0.0266 739  ALA B CA  
14403 C C   . ALA B 741  ? 0.1812 0.1889 0.1909 0.0189  0.0046  -0.0277 739  ALA B C   
14404 O O   . ALA B 741  ? 0.1807 0.1895 0.1889 0.0173  0.0046  -0.0274 739  ALA B O   
14405 C CB  . ALA B 741  ? 0.1920 0.2066 0.2113 0.0199  0.0060  -0.0259 739  ALA B CB  
14406 N N   . ALA B 742  ? 0.1781 0.1826 0.1852 0.0213  0.0049  -0.0289 740  ALA B N   
14407 C CA  . ALA B 742  ? 0.1923 0.1938 0.1941 0.0222  0.0052  -0.0302 740  ALA B CA  
14408 C C   . ALA B 742  ? 0.1862 0.1837 0.1835 0.0193  0.0031  -0.0306 740  ALA B C   
14409 O O   . ALA B 742  ? 0.1932 0.1906 0.1874 0.0185  0.0031  -0.0309 740  ALA B O   
14410 C CB  . ALA B 742  ? 0.2022 0.2003 0.2017 0.0255  0.0056  -0.0316 740  ALA B CB  
14411 N N   . GLU B 743  ? 0.1970 0.1915 0.1939 0.0177  0.0011  -0.0305 741  GLU B N   
14412 C CA  . GLU B 743  ? 0.2067 0.1979 0.1996 0.0146  -0.0010 -0.0307 741  GLU B CA  
14413 C C   . GLU B 743  ? 0.1843 0.1804 0.1795 0.0120  -0.0009 -0.0294 741  GLU B C   
14414 O O   . GLU B 743  ? 0.1987 0.1940 0.1907 0.0102  -0.0018 -0.0296 741  GLU B O   
14415 C CB  . GLU B 743  ? 0.2161 0.2032 0.2082 0.0134  -0.0029 -0.0307 741  GLU B CB  
14416 C CG  . GLU B 743  ? 0.2129 0.1968 0.2012 0.0098  -0.0051 -0.0306 741  GLU B CG  
14417 C CD  . GLU B 743  ? 0.2697 0.2475 0.2514 0.0097  -0.0061 -0.0322 741  GLU B CD  
14418 O OE1 . GLU B 743  ? 0.2577 0.2331 0.2372 0.0129  -0.0052 -0.0335 741  GLU B OE1 
14419 O OE2 . GLU B 743  ? 0.2891 0.2646 0.2676 0.0064  -0.0080 -0.0321 741  GLU B OE2 
14420 N N   . GLY B 744  ? 0.1951 0.1963 0.1957 0.0120  0.0001  -0.0281 742  GLY B N   
14421 C CA  . GLY B 744  ? 0.2053 0.2112 0.2081 0.0102  0.0004  -0.0270 742  GLY B CA  
14422 C C   . GLY B 744  ? 0.1779 0.1853 0.1790 0.0109  0.0014  -0.0271 742  GLY B C   
14423 O O   . GLY B 744  ? 0.1909 0.1996 0.1906 0.0091  0.0007  -0.0268 742  GLY B O   
14424 N N   . VAL B 745  ? 0.1879 0.1956 0.1892 0.0136  0.0032  -0.0276 743  VAL B N   
14425 C CA  . VAL B 745  ? 0.1719 0.1809 0.1712 0.0144  0.0043  -0.0277 743  VAL B CA  
14426 C C   . VAL B 745  ? 0.1954 0.1999 0.1884 0.0136  0.0029  -0.0290 743  VAL B C   
14427 O O   . VAL B 745  ? 0.1949 0.2005 0.1858 0.0126  0.0027  -0.0288 743  VAL B O   
14428 C CB  . VAL B 745  ? 0.1854 0.1961 0.1863 0.0174  0.0067  -0.0277 743  VAL B CB  
14429 C CG1 . VAL B 745  ? 0.1801 0.1910 0.1774 0.0184  0.0078  -0.0281 743  VAL B CG1 
14430 C CG2 . VAL B 745  ? 0.2043 0.2199 0.2112 0.0174  0.0078  -0.0261 743  VAL B CG2 
14431 N N   . ARG B 746  ? 0.1910 0.1901 0.1807 0.0140  0.0018  -0.0304 744  ARG B N   
14432 C CA  . ARG B 746  ? 0.2025 0.1965 0.1858 0.0129  0.0001  -0.0317 744  ARG B CA  
14433 C C   . ARG B 746  ? 0.1859 0.1810 0.1688 0.0092  -0.0018 -0.0309 744  ARG B C   
14434 O O   . ARG B 746  ? 0.2081 0.2025 0.1873 0.0080  -0.0027 -0.0313 744  ARG B O   
14435 C CB  . ARG B 746  ? 0.2103 0.1976 0.1903 0.0135  -0.0013 -0.0330 744  ARG B CB  
14436 C CG  . ARG B 746  ? 0.2278 0.2128 0.2067 0.0174  0.0002  -0.0342 744  ARG B CG  
14437 C CD  . ARG B 746  ? 0.2202 0.1978 0.1950 0.0177  -0.0016 -0.0355 744  ARG B CD  
14438 N NE  . ARG B 746  ? 0.2579 0.2342 0.2328 0.0219  -0.0002 -0.0365 744  ARG B NE  
14439 C CZ  . ARG B 746  ? 0.2331 0.2108 0.2122 0.0234  0.0003  -0.0360 744  ARG B CZ  
14440 N NH1 . ARG B 746  ? 0.2400 0.2186 0.2224 0.0211  -0.0009 -0.0348 744  ARG B NH1 
14441 N NH2 . ARG B 746  ? 0.2524 0.2309 0.2326 0.0274  0.0021  -0.0367 744  ARG B NH2 
14442 N N   . ILE B 747  ? 0.1759 0.1732 0.1626 0.0074  -0.0025 -0.0298 745  ILE B N   
14443 C CA  . ILE B 747  ? 0.1752 0.1742 0.1619 0.0039  -0.0042 -0.0290 745  ILE B CA  
14444 C C   . ILE B 747  ? 0.1948 0.1996 0.1837 0.0037  -0.0034 -0.0280 745  ILE B C   
14445 O O   . ILE B 747  ? 0.1828 0.1883 0.1695 0.0017  -0.0047 -0.0279 745  ILE B O   
14446 C CB  . ILE B 747  ? 0.1916 0.1915 0.1816 0.0024  -0.0049 -0.0281 745  ILE B CB  
14447 C CG1 . ILE B 747  ? 0.2114 0.2047 0.1977 0.0017  -0.0065 -0.0291 745  ILE B CG1 
14448 C CG2 . ILE B 747  ? 0.1921 0.1962 0.1837 -0.0007 -0.0060 -0.0269 745  ILE B CG2 
14449 C CD1 . ILE B 747  ? 0.2408 0.2342 0.2298 0.0007  -0.0070 -0.0282 745  ILE B CD1 
14450 N N   . LEU B 748  ? 0.1883 0.1971 0.1814 0.0057  -0.0014 -0.0271 746  LEU B N   
14451 C CA  . LEU B 748  ? 0.1981 0.2117 0.1928 0.0057  -0.0007 -0.0261 746  LEU B CA  
14452 C C   . LEU B 748  ? 0.1808 0.1930 0.1711 0.0064  -0.0006 -0.0268 746  LEU B C   
14453 O O   . LEU B 748  ? 0.1871 0.2016 0.1764 0.0052  -0.0014 -0.0263 746  LEU B O   
14454 C CB  . LEU B 748  ? 0.1794 0.1967 0.1790 0.0076  0.0013  -0.0250 746  LEU B CB  
14455 C CG  . LEU B 748  ? 0.2258 0.2461 0.2300 0.0066  0.0011  -0.0239 746  LEU B CG  
14456 C CD1 . LEU B 748  ? 0.2393 0.2613 0.2476 0.0085  0.0028  -0.0233 746  LEU B CD1 
14457 C CD2 . LEU B 748  ? 0.2524 0.2767 0.2576 0.0052  0.0004  -0.0229 746  LEU B CD2 
14458 N N   . ARG B 749  ? 0.1790 0.1876 0.1663 0.0085  0.0004  -0.0280 747  ARG B N   
14459 C CA  . ARG B 749  ? 0.1879 0.1947 0.1702 0.0092  0.0004  -0.0289 747  ARG B CA  
14460 C C   . ARG B 749  ? 0.1960 0.1995 0.1736 0.0066  -0.0023 -0.0298 747  ARG B C   
14461 O O   . ARG B 749  ? 0.1989 0.2033 0.1738 0.0057  -0.0031 -0.0298 747  ARG B O   
14462 C CB  . ARG B 749  ? 0.2038 0.2073 0.1837 0.0122  0.0020  -0.0302 747  ARG B CB  
14463 C CG  . ARG B 749  ? 0.2129 0.2205 0.1968 0.0146  0.0048  -0.0291 747  ARG B CG  
14464 C CD  . ARG B 749  ? 0.2309 0.2358 0.2120 0.0176  0.0064  -0.0304 747  ARG B CD  
14465 N NE  . ARG B 749  ? 0.2175 0.2268 0.2023 0.0197  0.0092  -0.0293 747  ARG B NE  
14466 C CZ  . ARG B 749  ? 0.2797 0.2885 0.2627 0.0225  0.0112  -0.0301 747  ARG B CZ  
14467 N NH1 . ARG B 749  ? 0.3007 0.3046 0.2780 0.0238  0.0108  -0.0321 747  ARG B NH1 
14468 N NH2 . ARG B 749  ? 0.2776 0.2909 0.2644 0.0239  0.0137  -0.0288 747  ARG B NH2 
14469 N N   . GLU B 750  ? 0.1968 0.1963 0.1732 0.0051  -0.0039 -0.0305 748  GLU B N   
14470 C CA  . GLU B 750  ? 0.2120 0.2081 0.1840 0.0022  -0.0066 -0.0312 748  GLU B CA  
14471 C C   . GLU B 750  ? 0.1929 0.1944 0.1674 -0.0006 -0.0078 -0.0298 748  GLU B C   
14472 O O   . GLU B 750  ? 0.2191 0.2200 0.1901 -0.0026 -0.0096 -0.0302 748  GLU B O   
14473 C CB  . GLU B 750  ? 0.2146 0.2059 0.1856 0.0009  -0.0080 -0.0318 748  GLU B CB  
14474 C CG  . GLU B 750  ? 0.2516 0.2386 0.2175 -0.0025 -0.0109 -0.0326 748  GLU B CG  
14475 C CD  . GLU B 750  ? 0.2466 0.2277 0.2106 -0.0037 -0.0123 -0.0331 748  GLU B CD  
14476 O OE1 . GLU B 750  ? 0.2740 0.2537 0.2399 -0.0014 -0.0110 -0.0333 748  GLU B OE1 
14477 O OE2 . GLU B 750  ? 0.3036 0.2815 0.2642 -0.0072 -0.0149 -0.0334 748  GLU B OE2 
14478 N N   . ALA B 751  ? 0.1943 0.2013 0.1747 -0.0005 -0.0067 -0.0283 749  ALA B N   
14479 C CA  . ALA B 751  ? 0.1966 0.2093 0.1799 -0.0026 -0.0076 -0.0269 749  ALA B CA  
14480 C C   . ALA B 751  ? 0.2125 0.2290 0.1959 -0.0015 -0.0070 -0.0263 749  ALA B C   
14481 O O   . ALA B 751  ? 0.2149 0.2361 0.2002 -0.0030 -0.0080 -0.0252 749  ALA B O   
14482 C CB  . ALA B 751  ? 0.1994 0.2160 0.1886 -0.0025 -0.0067 -0.0256 749  ALA B CB  
14483 N N   . GLY B 752  ? 0.2024 0.2170 0.1834 0.0010  -0.0055 -0.0269 750  GLY B N   
14484 C CA  . GLY B 752  ? 0.2119 0.2293 0.1920 0.0020  -0.0051 -0.0263 750  GLY B CA  
14485 C C   . GLY B 752  ? 0.1984 0.2181 0.1812 0.0049  -0.0024 -0.0254 750  GLY B C   
14486 O O   . GLY B 752  ? 0.2354 0.2570 0.2170 0.0058  -0.0019 -0.0248 750  GLY B O   
14487 N N   . ILE B 753  ? 0.1912 0.2108 0.1775 0.0062  -0.0008 -0.0252 751  ILE B N   
14488 C CA  . ILE B 753  ? 0.2103 0.2321 0.1992 0.0086  0.0017  -0.0242 751  ILE B CA  
14489 C C   . ILE B 753  ? 0.2223 0.2411 0.2069 0.0105  0.0030  -0.0252 751  ILE B C   
14490 O O   . ILE B 753  ? 0.2285 0.2433 0.2109 0.0112  0.0031  -0.0267 751  ILE B O   
14491 C CB  . ILE B 753  ? 0.1864 0.2089 0.1802 0.0093  0.0029  -0.0237 751  ILE B CB  
14492 C CG1 . ILE B 753  ? 0.2030 0.2282 0.2005 0.0075  0.0016  -0.0229 751  ILE B CG1 
14493 C CG2 . ILE B 753  ? 0.2117 0.2364 0.2079 0.0113  0.0052  -0.0227 751  ILE B CG2 
14494 C CD1 . ILE B 753  ? 0.2049 0.2345 0.2044 0.0073  0.0015  -0.0214 751  ILE B CD1 
14495 N N   . PRO B 754  ? 0.2033 0.2238 0.1864 0.0116  0.0040  -0.0245 752  PRO B N   
14496 C CA  . PRO B 754  ? 0.2130 0.2309 0.1916 0.0135  0.0055  -0.0254 752  PRO B CA  
14497 C C   . PRO B 754  ? 0.2133 0.2308 0.1942 0.0156  0.0078  -0.0257 752  PRO B C   
14498 O O   . PRO B 754  ? 0.2147 0.2349 0.2010 0.0158  0.0088  -0.0245 752  PRO B O   
14499 C CB  . PRO B 754  ? 0.2514 0.2722 0.2292 0.0141  0.0063  -0.0240 752  PRO B CB  
14500 C CG  . PRO B 754  ? 0.2763 0.3002 0.2565 0.0122  0.0044  -0.0228 752  PRO B CG  
14501 C CD  . PRO B 754  ? 0.2131 0.2376 0.1980 0.0112  0.0038  -0.0227 752  PRO B CD  
14502 N N   . ALA B 755  ? 0.2401 0.2541 0.2167 0.0173  0.0086  -0.0272 753  ALA B N   
14503 C CA  . ALA B 755  ? 0.2621 0.2761 0.2409 0.0196  0.0109  -0.0275 753  ALA B CA  
14504 C C   . ALA B 755  ? 0.2286 0.2474 0.2114 0.0207  0.0134  -0.0256 753  ALA B C   
14505 O O   . ALA B 755  ? 0.2416 0.2623 0.2291 0.0215  0.0147  -0.0250 753  ALA B O   
14506 C CB  . ALA B 755  ? 0.3104 0.3203 0.2835 0.0217  0.0115  -0.0296 753  ALA B CB  
14507 N N   . SER B 756  ? 0.2233 0.2438 0.2041 0.0205  0.0139  -0.0245 754  SER B N   
14508 C CA  . SER B 756  ? 0.2184 0.2430 0.2027 0.0212  0.0162  -0.0225 754  SER B CA  
14509 C C   . SER B 756  ? 0.2151 0.2423 0.2052 0.0197  0.0155  -0.0208 754  SER B C   
14510 O O   . SER B 756  ? 0.2252 0.2553 0.2192 0.0201  0.0173  -0.0192 754  SER B O   
14511 C CB  . SER B 756  ? 0.2650 0.2902 0.2451 0.0215  0.0168  -0.0217 754  SER B CB  
14512 O OG  . SER B 756  ? 0.3163 0.3411 0.2947 0.0197  0.0143  -0.0214 754  SER B OG  
14513 N N   . ALA B 757  ? 0.1894 0.2160 0.1802 0.0179  0.0131  -0.0211 755  ALA B N   
14514 C CA  . ALA B 757  ? 0.1775 0.2064 0.1735 0.0168  0.0124  -0.0197 755  ALA B CA  
14515 C C   . ALA B 757  ? 0.1827 0.2113 0.1828 0.0167  0.0124  -0.0202 755  ALA B C   
14516 O O   . ALA B 757  ? 0.1846 0.2152 0.1891 0.0160  0.0122  -0.0192 755  ALA B O   
14517 C CB  . ALA B 757  ? 0.1895 0.2187 0.1846 0.0150  0.0100  -0.0196 755  ALA B CB  
14518 N N   . LEU B 758  ? 0.1947 0.2207 0.1931 0.0175  0.0124  -0.0219 756  LEU B N   
14519 C CA  . LEU B 758  ? 0.1880 0.2134 0.1899 0.0175  0.0121  -0.0224 756  LEU B CA  
14520 C C   . LEU B 758  ? 0.1785 0.2022 0.1791 0.0195  0.0134  -0.0236 756  LEU B C   
14521 O O   . LEU B 758  ? 0.2107 0.2307 0.2069 0.0200  0.0126  -0.0253 756  LEU B O   
14522 C CB  . LEU B 758  ? 0.1807 0.2042 0.1820 0.0156  0.0096  -0.0231 756  LEU B CB  
14523 C CG  . LEU B 758  ? 0.1825 0.2049 0.1867 0.0156  0.0092  -0.0236 756  LEU B CG  
14524 C CD1 . LEU B 758  ? 0.1911 0.2168 0.2010 0.0157  0.0101  -0.0222 756  LEU B CD1 
14525 C CD2 . LEU B 758  ? 0.1951 0.2154 0.1981 0.0135  0.0068  -0.0242 756  LEU B CD2 
14526 N N   . GLN B 759  ? 0.1755 0.2018 0.1799 0.0208  0.0154  -0.0228 757  GLN B N   
14527 C CA  . GLN B 759  ? 0.1807 0.2066 0.1849 0.0231  0.0169  -0.0238 757  GLN B CA  
14528 C C   . GLN B 759  ? 0.1856 0.2122 0.1947 0.0232  0.0166  -0.0237 757  GLN B C   
14529 O O   . GLN B 759  ? 0.2067 0.2358 0.2203 0.0219  0.0163  -0.0223 757  GLN B O   
14530 C CB  . GLN B 759  ? 0.1792 0.2086 0.1841 0.0245  0.0196  -0.0226 757  GLN B CB  
14531 C CG  . GLN B 759  ? 0.1874 0.2157 0.1866 0.0247  0.0201  -0.0229 757  GLN B CG  
14532 C CD  . GLN B 759  ? 0.1944 0.2263 0.1943 0.0257  0.0228  -0.0214 757  GLN B CD  
14533 O OE1 . GLN B 759  ? 0.2174 0.2497 0.2152 0.0278  0.0247  -0.0221 757  GLN B OE1 
14534 N NE2 . GLN B 759  ? 0.2044 0.2388 0.2069 0.0241  0.0229  -0.0193 757  GLN B NE2 
14535 N N   . LEU B 760  ? 0.1895 0.2135 0.1973 0.0249  0.0163  -0.0252 758  LEU B N   
14536 C CA  . LEU B 760  ? 0.1805 0.2047 0.1923 0.0253  0.0158  -0.0253 758  LEU B CA  
14537 C C   . LEU B 760  ? 0.2044 0.2317 0.2189 0.0278  0.0181  -0.0252 758  LEU B C   
14538 O O   . LEU B 760  ? 0.1991 0.2254 0.2103 0.0301  0.0193  -0.0263 758  LEU B O   
14539 C CB  . LEU B 760  ? 0.1904 0.2092 0.1987 0.0255  0.0138  -0.0271 758  LEU B CB  
14540 C CG  . LEU B 760  ? 0.1857 0.2043 0.1977 0.0260  0.0130  -0.0272 758  LEU B CG  
14541 C CD1 . LEU B 760  ? 0.2022 0.2219 0.2174 0.0233  0.0115  -0.0260 758  LEU B CD1 
14542 C CD2 . LEU B 760  ? 0.2196 0.2326 0.2275 0.0272  0.0116  -0.0290 758  LEU B CD2 
14543 N N   . LEU B 761  ? 0.1814 0.2126 0.2018 0.0275  0.0186  -0.0238 759  LEU B N   
14544 C CA  . LEU B 761  ? 0.1785 0.2139 0.2026 0.0296  0.0207  -0.0234 759  LEU B CA  
14545 C C   . LEU B 761  ? 0.1798 0.2155 0.2080 0.0300  0.0196  -0.0236 759  LEU B C   
14546 O O   . LEU B 761  ? 0.1856 0.2243 0.2187 0.0285  0.0193  -0.0222 759  LEU B O   
14547 C CB  . LEU B 761  ? 0.1911 0.2316 0.2187 0.0285  0.0226  -0.0213 759  LEU B CB  
14548 C CG  . LEU B 761  ? 0.2250 0.2659 0.2491 0.0281  0.0240  -0.0207 759  LEU B CG  
14549 C CD1 . LEU B 761  ? 0.2171 0.2560 0.2356 0.0305  0.0251  -0.0223 759  LEU B CD1 
14550 C CD2 . LEU B 761  ? 0.2271 0.2658 0.2493 0.0256  0.0222  -0.0202 759  LEU B CD2 
14551 N N   . PRO B 762  ? 0.1739 0.2061 0.1998 0.0320  0.0187  -0.0253 760  PRO B N   
14552 C CA  . PRO B 762  ? 0.1695 0.2021 0.1991 0.0327  0.0176  -0.0253 760  PRO B CA  
14553 C C   . PRO B 762  ? 0.1851 0.2240 0.2204 0.0342  0.0195  -0.0243 760  PRO B C   
14554 O O   . PRO B 762  ? 0.1876 0.2297 0.2229 0.0357  0.0220  -0.0241 760  PRO B O   
14555 C CB  . PRO B 762  ? 0.1766 0.2038 0.2016 0.0350  0.0165  -0.0274 760  PRO B CB  
14556 C CG  . PRO B 762  ? 0.1886 0.2116 0.2072 0.0344  0.0164  -0.0284 760  PRO B CG  
14557 C CD  . PRO B 762  ? 0.1786 0.2061 0.1982 0.0338  0.0186  -0.0272 760  PRO B CD  
14558 N N   . GLY B 763  ? 0.1800 0.2206 0.2200 0.0337  0.0184  -0.0237 761  GLY B N   
14559 C CA  . GLY B 763  ? 0.1666 0.2133 0.2124 0.0351  0.0198  -0.0228 761  GLY B CA  
14560 C C   . GLY B 763  ? 0.1644 0.2135 0.2155 0.0326  0.0185  -0.0214 761  GLY B C   
14561 O O   . GLY B 763  ? 0.1818 0.2275 0.2318 0.0303  0.0165  -0.0213 761  GLY B O   
14562 N N   . ASP B 764  ? 0.2037 0.2588 0.2605 0.0331  0.0196  -0.0203 762  ASP B N   
14563 C CA  . ASP B 764  ? 0.1937 0.2511 0.2556 0.0309  0.0181  -0.0190 762  ASP B CA  
14564 C C   . ASP B 764  ? 0.2069 0.2668 0.2707 0.0279  0.0190  -0.0172 762  ASP B C   
14565 O O   . ASP B 764  ? 0.1951 0.2537 0.2555 0.0272  0.0201  -0.0170 762  ASP B O   
14566 C CB  . ASP B 764  ? 0.2088 0.2708 0.2758 0.0329  0.0181  -0.0189 762  ASP B CB  
14567 C CG  . ASP B 764  ? 0.2633 0.3323 0.3340 0.0341  0.0210  -0.0179 762  ASP B CG  
14568 O OD1 . ASP B 764  ? 0.2158 0.2864 0.2856 0.0330  0.0230  -0.0170 762  ASP B OD1 
14569 O OD2 . ASP B 764  ? 0.3492 0.4225 0.4238 0.0364  0.0213  -0.0179 762  ASP B OD2 
14570 N N   . GLY B 765  ? 0.1954 0.2585 0.2643 0.0261  0.0182  -0.0159 763  GLY B N   
14571 C CA  . GLY B 765  ? 0.1732 0.2376 0.2436 0.0231  0.0186  -0.0142 763  GLY B CA  
14572 C C   . GLY B 765  ? 0.1950 0.2638 0.2663 0.0231  0.0214  -0.0130 763  GLY B C   
14573 O O   . GLY B 765  ? 0.2024 0.2708 0.2730 0.0209  0.0219  -0.0117 763  GLY B O   
14574 N N   . ARG B 766  ? 0.1811 0.2539 0.2538 0.0257  0.0234  -0.0132 764  ARG B N   
14575 C CA  . ARG B 766  ? 0.1952 0.2723 0.2682 0.0258  0.0263  -0.0120 764  ARG B CA  
14576 C C   . ARG B 766  ? 0.1962 0.2691 0.2628 0.0261  0.0272  -0.0126 764  ARG B C   
14577 O O   . ARG B 766  ? 0.1932 0.2677 0.2591 0.0248  0.0289  -0.0111 764  ARG B O   
14578 C CB  . ARG B 766  ? 0.2074 0.2898 0.2829 0.0290  0.0283  -0.0124 764  ARG B CB  
14579 C CG  . ARG B 766  ? 0.2469 0.3343 0.3291 0.0291  0.0274  -0.0118 764  ARG B CG  
14580 C CD  . ARG B 766  ? 0.3327 0.4246 0.4166 0.0332  0.0291  -0.0127 764  ARG B CD  
14581 N NE  . ARG B 766  ? 0.3599 0.4460 0.4388 0.0363  0.0280  -0.0151 764  ARG B NE  
14582 C CZ  . ARG B 766  ? 0.4422 0.5297 0.5203 0.0404  0.0292  -0.0165 764  ARG B CZ  
14583 N NH1 . ARG B 766  ? 0.4458 0.5411 0.5280 0.0422  0.0318  -0.0157 764  ARG B NH1 
14584 N NH2 . ARG B 766  ? 0.4871 0.5682 0.5601 0.0428  0.0278  -0.0187 764  ARG B NH2 
14585 N N   . VAL B 767  ? 0.1821 0.2496 0.2439 0.0276  0.0260  -0.0146 765  VAL B N   
14586 C CA  . VAL B 767  ? 0.1936 0.2569 0.2492 0.0275  0.0263  -0.0152 765  VAL B CA  
14587 C C   . VAL B 767  ? 0.1876 0.2485 0.2425 0.0244  0.0250  -0.0141 765  VAL B C   
14588 O O   . VAL B 767  ? 0.1806 0.2412 0.2330 0.0234  0.0261  -0.0133 765  VAL B O   
14589 C CB  . VAL B 767  ? 0.1682 0.2263 0.2191 0.0297  0.0251  -0.0176 765  VAL B CB  
14590 C CG1 . VAL B 767  ? 0.1898 0.2438 0.2344 0.0293  0.0252  -0.0182 765  VAL B CG1 
14591 C CG2 . VAL B 767  ? 0.2185 0.2787 0.2697 0.0332  0.0264  -0.0187 765  VAL B CG2 
14592 N N   . GLY B 768  ? 0.1630 0.2221 0.2200 0.0229  0.0227  -0.0142 766  GLY B N   
14593 C CA  . GLY B 768  ? 0.1857 0.2428 0.2423 0.0202  0.0215  -0.0131 766  GLY B CA  
14594 C C   . GLY B 768  ? 0.1619 0.2225 0.2212 0.0185  0.0230  -0.0109 766  GLY B C   
14595 O O   . GLY B 768  ? 0.1774 0.2364 0.2342 0.0172  0.0233  -0.0100 766  GLY B O   
14596 N N   . ALA B 769  ? 0.1775 0.2430 0.2418 0.0184  0.0239  -0.0100 767  ALA B N   
14597 C CA  . ALA B 769  ? 0.1789 0.2476 0.2459 0.0163  0.0252  -0.0076 767  ALA B CA  
14598 C C   . ALA B 769  ? 0.1842 0.2542 0.2482 0.0169  0.0278  -0.0069 767  ALA B C   
14599 O O   . ALA B 769  ? 0.1952 0.2648 0.2582 0.0150  0.0283  -0.0052 767  ALA B O   
14600 C CB  . ALA B 769  ? 0.1848 0.2592 0.2582 0.0160  0.0257  -0.0067 767  ALA B CB  
14601 N N   . ALA B 770  ? 0.1653 0.2364 0.2270 0.0197  0.0294  -0.0081 768  ALA B N   
14602 C CA  . ALA B 770  ? 0.1762 0.2484 0.2344 0.0205  0.0318  -0.0076 768  ALA B CA  
14603 C C   . ALA B 770  ? 0.1787 0.2457 0.2314 0.0196  0.0309  -0.0077 768  ALA B C   
14604 O O   . ALA B 770  ? 0.2051 0.2725 0.2557 0.0187  0.0323  -0.0063 768  ALA B O   
14605 C CB  . ALA B 770  ? 0.1779 0.2514 0.2342 0.0239  0.0334  -0.0093 768  ALA B CB  
14606 N N   . LEU B 771  ? 0.1670 0.2293 0.2173 0.0199  0.0286  -0.0094 769  LEU B N   
14607 C CA  . LEU B 771  ? 0.1855 0.2435 0.2311 0.0191  0.0275  -0.0096 769  LEU B CA  
14608 C C   . LEU B 771  ? 0.1871 0.2446 0.2342 0.0165  0.0267  -0.0076 769  LEU B C   
14609 O O   . LEU B 771  ? 0.2047 0.2610 0.2489 0.0157  0.0272  -0.0066 769  LEU B O   
14610 C CB  . LEU B 771  ? 0.1751 0.2289 0.2185 0.0196  0.0251  -0.0117 769  LEU B CB  
14611 C CG  . LEU B 771  ? 0.1809 0.2334 0.2210 0.0221  0.0255  -0.0137 769  LEU B CG  
14612 C CD1 . LEU B 771  ? 0.1919 0.2405 0.2309 0.0222  0.0230  -0.0154 769  LEU B CD1 
14613 C CD2 . LEU B 771  ? 0.1915 0.2428 0.2261 0.0230  0.0267  -0.0140 769  LEU B CD2 
14614 N N   . VAL B 772  ? 0.1699 0.2279 0.2214 0.0151  0.0254  -0.0072 770  VAL B N   
14615 C CA  . VAL B 772  ? 0.1671 0.2238 0.2199 0.0127  0.0244  -0.0055 770  VAL B CA  
14616 C C   . VAL B 772  ? 0.2144 0.2736 0.2677 0.0115  0.0264  -0.0032 770  VAL B C   
14617 O O   . VAL B 772  ? 0.2193 0.2762 0.2707 0.0102  0.0261  -0.0018 770  VAL B O   
14618 C CB  . VAL B 772  ? 0.1865 0.2436 0.2439 0.0116  0.0227  -0.0056 770  VAL B CB  
14619 C CG1 . VAL B 772  ? 0.2071 0.2633 0.2662 0.0091  0.0220  -0.0037 770  VAL B CG1 
14620 C CG2 . VAL B 772  ? 0.2017 0.2555 0.2577 0.0124  0.0205  -0.0076 770  VAL B CG2 
14621 N N   . ALA B 773  ? 0.2047 0.2688 0.2608 0.0120  0.0285  -0.0025 771  ALA B N   
14622 C CA  . ALA B 773  ? 0.2161 0.2831 0.2731 0.0105  0.0306  0.0000  771  ALA B CA  
14623 C C   . ALA B 773  ? 0.2626 0.3292 0.3145 0.0115  0.0325  0.0004  771  ALA B C   
14624 O O   . ALA B 773  ? 0.2656 0.3338 0.3173 0.0100  0.0341  0.0027  771  ALA B O   
14625 C CB  . ALA B 773  ? 0.2165 0.2898 0.2786 0.0107  0.0324  0.0006  771  ALA B CB  
14626 N N   . ALA B 774  ? 0.2002 0.2645 0.2478 0.0137  0.0323  -0.0016 772  ALA B N   
14627 C CA  . ALA B 774  ? 0.2243 0.2883 0.2667 0.0148  0.0340  -0.0014 772  ALA B CA  
14628 C C   . ALA B 774  ? 0.2440 0.3051 0.2835 0.0131  0.0335  0.0004  772  ALA B C   
14629 O O   . ALA B 774  ? 0.2391 0.2967 0.2785 0.0120  0.0311  0.0004  772  ALA B O   
14630 C CB  . ALA B 774  ? 0.2527 0.3141 0.2909 0.0173  0.0333  -0.0041 772  ALA B CB  
14631 N N   . ALA B 775  ? 0.2777 0.3402 0.3142 0.0132  0.0357  0.0019  773  ALA B N   
14632 C CA  . ALA B 775  ? 0.2756 0.3359 0.3097 0.0114  0.0355  0.0041  773  ALA B CA  
14633 C C   . ALA B 775  ? 0.2487 0.3039 0.2787 0.0119  0.0330  0.0032  773  ALA B C   
14634 O O   . ALA B 775  ? 0.2860 0.3384 0.3157 0.0104  0.0316  0.0045  773  ALA B O   
14635 C CB  . ALA B 775  ? 0.3064 0.3692 0.3374 0.0117  0.0384  0.0057  773  ALA B CB  
14636 N N   . GLU B 776  ? 0.2431 0.2971 0.2699 0.0139  0.0325  0.0008  774  GLU B N   
14637 C CA  . GLU B 776  ? 0.2286 0.2787 0.2514 0.0142  0.0303  0.0000  774  GLU B CA  
14638 C C   . GLU B 776  ? 0.2098 0.2577 0.2347 0.0141  0.0276  -0.0015 774  GLU B C   
14639 O O   . GLU B 776  ? 0.2240 0.2692 0.2462 0.0143  0.0258  -0.0022 774  GLU B O   
14640 C CB  . GLU B 776  ? 0.2242 0.2738 0.2418 0.0161  0.0309  -0.0016 774  GLU B CB  
14641 C CG  . GLU B 776  ? 0.2895 0.3410 0.3038 0.0166  0.0336  -0.0002 774  GLU B CG  
14642 C CD  . GLU B 776  ? 0.3789 0.4344 0.3953 0.0177  0.0362  -0.0007 774  GLU B CD  
14643 O OE1 . GLU B 776  ? 0.3063 0.3631 0.3270 0.0180  0.0359  -0.0020 774  GLU B OE1 
14644 O OE2 . GLU B 776  ? 0.4240 0.4814 0.4375 0.0183  0.0386  0.0002  774  GLU B OE2 
14645 N N   . THR B 777  ? 0.1922 0.2414 0.2219 0.0137  0.0274  -0.0021 775  THR B N   
14646 C CA  . THR B 777  ? 0.1859 0.2331 0.2175 0.0134  0.0249  -0.0034 775  THR B CA  
14647 C C   . THR B 777  ? 0.1883 0.2330 0.2199 0.0121  0.0234  -0.0020 775  THR B C   
14648 O O   . THR B 777  ? 0.2142 0.2591 0.2476 0.0107  0.0240  0.0000  775  THR B O   
14649 C CB  . THR B 777  ? 0.2055 0.2548 0.2421 0.0131  0.0251  -0.0039 775  THR B CB  
14650 O OG1 . THR B 777  ? 0.2201 0.2711 0.2561 0.0148  0.0262  -0.0055 775  THR B OG1 
14651 C CG2 . THR B 777  ? 0.1852 0.2324 0.2238 0.0126  0.0226  -0.0049 775  THR B CG2 
14652 N N   . ALA B 778  ? 0.1622 0.2044 0.1915 0.0126  0.0215  -0.0030 776  ALA B N   
14653 C CA  . ALA B 778  ? 0.1785 0.2183 0.2070 0.0121  0.0200  -0.0020 776  ALA B CA  
14654 C C   . ALA B 778  ? 0.1765 0.2150 0.2077 0.0118  0.0180  -0.0030 776  ALA B C   
14655 O O   . ALA B 778  ? 0.2006 0.2369 0.2314 0.0115  0.0167  -0.0022 776  ALA B O   
14656 C CB  . ALA B 778  ? 0.1828 0.2215 0.2068 0.0130  0.0193  -0.0022 776  ALA B CB  
14657 N N   . GLY B 779  ? 0.1622 0.2017 0.1956 0.0119  0.0177  -0.0046 777  GLY B N   
14658 C CA  . GLY B 779  ? 0.1760 0.2144 0.2118 0.0116  0.0160  -0.0055 777  GLY B CA  
14659 C C   . GLY B 779  ? 0.1665 0.2063 0.2045 0.0118  0.0161  -0.0071 777  GLY B C   
14660 O O   . GLY B 779  ? 0.1734 0.2146 0.2103 0.0126  0.0171  -0.0078 777  GLY B O   
14661 N N   . VAL B 780  ? 0.1591 0.1984 0.2000 0.0112  0.0149  -0.0075 778  VAL B N   
14662 C CA  . VAL B 780  ? 0.1558 0.1962 0.1989 0.0114  0.0147  -0.0088 778  VAL B CA  
14663 C C   . VAL B 780  ? 0.1469 0.1856 0.1901 0.0114  0.0128  -0.0100 778  VAL B C   
14664 O O   . VAL B 780  ? 0.1548 0.1921 0.1987 0.0108  0.0118  -0.0095 778  VAL B O   
14665 C CB  . VAL B 780  ? 0.1613 0.2035 0.2083 0.0107  0.0155  -0.0080 778  VAL B CB  
14666 C CG1 . VAL B 780  ? 0.1802 0.2234 0.2294 0.0112  0.0150  -0.0094 778  VAL B CG1 
14667 C CG2 . VAL B 780  ? 0.1638 0.2084 0.2107 0.0108  0.0178  -0.0067 778  VAL B CG2 
14668 N N   . MET B 781  ? 0.1491 0.1878 0.1915 0.0120  0.0123  -0.0115 779  MET B N   
14669 C CA  . MET B 781  ? 0.1489 0.1864 0.1916 0.0118  0.0106  -0.0126 779  MET B CA  
14670 C C   . MET B 781  ? 0.1623 0.2003 0.2073 0.0118  0.0105  -0.0134 779  MET B C   
14671 O O   . MET B 781  ? 0.1615 0.2001 0.2058 0.0126  0.0112  -0.0141 779  MET B O   
14672 C CB  . MET B 781  ? 0.1631 0.1999 0.2025 0.0121  0.0100  -0.0136 779  MET B CB  
14673 C CG  . MET B 781  ? 0.1695 0.2063 0.2067 0.0123  0.0101  -0.0129 779  MET B CG  
14674 S SD  . MET B 781  ? 0.1640 0.2009 0.1978 0.0124  0.0092  -0.0139 779  MET B SD  
14675 C CE  . MET B 781  ? 0.1793 0.2159 0.2141 0.0120  0.0076  -0.0145 779  MET B CE  
14676 N N   . PHE B 782  ? 0.1604 0.1982 0.2081 0.0112  0.0096  -0.0132 780  PHE B N   
14677 C CA  . PHE B 782  ? 0.1593 0.1979 0.2096 0.0113  0.0093  -0.0137 780  PHE B CA  
14678 C C   . PHE B 782  ? 0.1406 0.1776 0.1909 0.0109  0.0075  -0.0146 780  PHE B C   
14679 O O   . PHE B 782  ? 0.1548 0.1906 0.2050 0.0103  0.0067  -0.0143 780  PHE B O   
14680 C CB  . PHE B 782  ? 0.1407 0.1810 0.1947 0.0105  0.0098  -0.0125 780  PHE B CB  
14681 C CG  . PHE B 782  ? 0.1393 0.1807 0.1963 0.0105  0.0092  -0.0129 780  PHE B CG  
14682 C CD1 . PHE B 782  ? 0.1638 0.2071 0.2217 0.0117  0.0101  -0.0133 780  PHE B CD1 
14683 C CD2 . PHE B 782  ? 0.1486 0.1890 0.2074 0.0096  0.0075  -0.0130 780  PHE B CD2 
14684 C CE1 . PHE B 782  ? 0.1648 0.2094 0.2256 0.0121  0.0094  -0.0137 780  PHE B CE1 
14685 C CE2 . PHE B 782  ? 0.1723 0.2140 0.2339 0.0097  0.0067  -0.0133 780  PHE B CE2 
14686 C CZ  . PHE B 782  ? 0.1670 0.2109 0.2298 0.0110  0.0077  -0.0136 780  PHE B CZ  
14687 N N   . THR B 783  ? 0.1445 0.1811 0.1946 0.0114  0.0070  -0.0156 781  THR B N   
14688 C CA  . THR B 783  ? 0.1576 0.1929 0.2081 0.0111  0.0054  -0.0163 781  THR B CA  
14689 C C   . THR B 783  ? 0.1579 0.1941 0.2109 0.0116  0.0051  -0.0165 781  THR B C   
14690 O O   . THR B 783  ? 0.1570 0.1937 0.2095 0.0127  0.0059  -0.0169 781  THR B O   
14691 C CB  . THR B 783  ? 0.1563 0.1900 0.2035 0.0111  0.0046  -0.0172 781  THR B CB  
14692 O OG1 . THR B 783  ? 0.1662 0.1998 0.2115 0.0108  0.0049  -0.0169 781  THR B OG1 
14693 C CG2 . THR B 783  ? 0.1598 0.1921 0.2071 0.0106  0.0030  -0.0177 781  THR B CG2 
14694 N N   . GLY B 784  ? 0.1628 0.1992 0.2183 0.0110  0.0040  -0.0163 782  GLY B N   
14695 C CA  . GLY B 784  ? 0.1609 0.1987 0.2193 0.0115  0.0037  -0.0163 782  GLY B CA  
14696 C C   . GLY B 784  ? 0.1852 0.2236 0.2466 0.0103  0.0025  -0.0158 782  GLY B C   
14697 O O   . GLY B 784  ? 0.1786 0.2151 0.2388 0.0094  0.0016  -0.0158 782  GLY B O   
14698 N N   . SER B 785  ? 0.1826 0.2235 0.2476 0.0105  0.0024  -0.0154 783  SER B N   
14699 C CA  . SER B 785  ? 0.1910 0.2325 0.2589 0.0092  0.0010  -0.0149 783  SER B CA  
14700 C C   . SER B 785  ? 0.1801 0.2220 0.2491 0.0077  0.0015  -0.0138 783  SER B C   
14701 O O   . SER B 785  ? 0.1935 0.2368 0.2626 0.0077  0.0033  -0.0130 783  SER B O   
14702 C CB  . SER B 785  ? 0.1977 0.2426 0.2697 0.0098  0.0007  -0.0146 783  SER B CB  
14703 O OG  . SER B 785  ? 0.2008 0.2494 0.2753 0.0102  0.0027  -0.0138 783  SER B OG  
14704 N N   . THR B 786  ? 0.2146 0.2548 0.2841 0.0063  -0.0001 -0.0136 784  THR B N   
14705 C CA  . THR B 786  ? 0.2109 0.2506 0.2812 0.0046  0.0000  -0.0125 784  THR B CA  
14706 C C   . THR B 786  ? 0.2018 0.2456 0.2763 0.0038  0.0011  -0.0111 784  THR B C   
14707 O O   . THR B 786  ? 0.2245 0.2687 0.2991 0.0029  0.0024  -0.0099 784  THR B O   
14708 C CB  . THR B 786  ? 0.2088 0.2456 0.2787 0.0034  -0.0023 -0.0129 784  THR B CB  
14709 O OG1 . THR B 786  ? 0.2358 0.2694 0.3017 0.0043  -0.0030 -0.0142 784  THR B OG1 
14710 C CG2 . THR B 786  ? 0.2533 0.2882 0.3229 0.0018  -0.0023 -0.0119 784  THR B CG2 
14711 N N   . GLU B 787  ? 0.2250 0.2722 0.3030 0.0042  0.0008  -0.0112 785  GLU B N   
14712 C CA  . GLU B 787  ? 0.2024 0.2546 0.2850 0.0035  0.0019  -0.0098 785  GLU B CA  
14713 C C   . GLU B 787  ? 0.2032 0.2575 0.2851 0.0046  0.0047  -0.0092 785  GLU B C   
14714 O O   . GLU B 787  ? 0.2141 0.2706 0.2977 0.0033  0.0060  -0.0077 785  GLU B O   
14715 C CB  . GLU B 787  ? 0.2629 0.3186 0.3492 0.0044  0.0010  -0.0101 785  GLU B CB  
14716 N N   . VAL B 788  ? 0.1853 0.2385 0.2642 0.0068  0.0055  -0.0104 786  VAL B N   
14717 C CA  . VAL B 788  ? 0.1879 0.2427 0.2655 0.0079  0.0080  -0.0100 786  VAL B CA  
14718 C C   . VAL B 788  ? 0.1612 0.2133 0.2357 0.0069  0.0087  -0.0093 786  VAL B C   
14719 O O   . VAL B 788  ? 0.1814 0.2354 0.2560 0.0066  0.0106  -0.0081 786  VAL B O   
14720 C CB  . VAL B 788  ? 0.1985 0.2523 0.2733 0.0104  0.0083  -0.0116 786  VAL B CB  
14721 C CG1 . VAL B 788  ? 0.1977 0.2519 0.2699 0.0115  0.0106  -0.0115 786  VAL B CG1 
14722 C CG2 . VAL B 788  ? 0.2047 0.2617 0.2828 0.0119  0.0080  -0.0120 786  VAL B CG2 
14723 N N   . ALA B 789  ? 0.1725 0.2202 0.2441 0.0064  0.0071  -0.0100 787  ALA B N   
14724 C CA  . ALA B 789  ? 0.1590 0.2041 0.2277 0.0057  0.0076  -0.0094 787  ALA B CA  
14725 C C   . ALA B 789  ? 0.1769 0.2229 0.2477 0.0037  0.0080  -0.0075 787  ALA B C   
14726 O O   . ALA B 789  ? 0.1876 0.2333 0.2569 0.0034  0.0093  -0.0065 787  ALA B O   
14727 C CB  . ALA B 789  ? 0.1636 0.2045 0.2294 0.0056  0.0057  -0.0104 787  ALA B CB  
14728 N N   . ARG B 790  ? 0.1797 0.2268 0.2541 0.0021  0.0067  -0.0071 788  ARG B N   
14729 C CA  . ARG B 790  ? 0.1851 0.2329 0.2616 -0.0002 0.0069  -0.0052 788  ARG B CA  
14730 C C   . ARG B 790  ? 0.2028 0.2554 0.2814 -0.0003 0.0095  -0.0037 788  ARG B C   
14731 O O   . ARG B 790  ? 0.2311 0.2836 0.3096 -0.0019 0.0104  -0.0020 788  ARG B O   
14732 C CB  . ARG B 790  ? 0.2260 0.2749 0.3064 -0.0020 0.0050  -0.0049 788  ARG B CB  
14733 C CG  . ARG B 790  ? 0.2540 0.2982 0.3324 -0.0024 0.0025  -0.0061 788  ARG B CG  
14734 C CD  . ARG B 790  ? 0.3325 0.3778 0.4147 -0.0047 0.0006  -0.0055 788  ARG B CD  
14735 N NE  . ARG B 790  ? 0.3839 0.4246 0.4639 -0.0049 -0.0019 -0.0068 788  ARG B NE  
14736 C CZ  . ARG B 790  ? 0.3804 0.4156 0.4569 -0.0055 -0.0030 -0.0070 788  ARG B CZ  
14737 N NH1 . ARG B 790  ? 0.3327 0.3660 0.4075 -0.0063 -0.0020 -0.0057 788  ARG B NH1 
14738 N NH2 . ARG B 790  ? 0.4445 0.4759 0.5187 -0.0052 -0.0051 -0.0085 788  ARG B NH2 
14739 N N   . LEU B 791  ? 0.1923 0.2490 0.2728 0.0015  0.0106  -0.0044 789  LEU B N   
14740 C CA  . LEU B 791  ? 0.2078 0.2694 0.2901 0.0018  0.0132  -0.0032 789  LEU B CA  
14741 C C   . LEU B 791  ? 0.2017 0.2613 0.2794 0.0027  0.0150  -0.0029 789  LEU B C   
14742 O O   . LEU B 791  ? 0.2197 0.2811 0.2976 0.0017  0.0167  -0.0012 789  LEU B O   
14743 C CB  . LEU B 791  ? 0.2129 0.2787 0.2974 0.0041  0.0139  -0.0042 789  LEU B CB  
14744 C CG  . LEU B 791  ? 0.2263 0.2948 0.3156 0.0036  0.0122  -0.0044 789  LEU B CG  
14745 C CD1 . LEU B 791  ? 0.2354 0.3076 0.3262 0.0065  0.0131  -0.0055 789  LEU B CD1 
14746 C CD2 . LEU B 791  ? 0.2537 0.3261 0.3477 0.0008  0.0124  -0.0023 789  LEU B CD2 
14747 N N   . ILE B 792  ? 0.1948 0.2508 0.2684 0.0045  0.0144  -0.0046 790  ILE B N   
14748 C CA  . ILE B 792  ? 0.2023 0.2563 0.2715 0.0053  0.0156  -0.0045 790  ILE B CA  
14749 C C   . ILE B 792  ? 0.1869 0.2380 0.2546 0.0035  0.0152  -0.0030 790  ILE B C   
14750 O O   . ILE B 792  ? 0.2068 0.2581 0.2726 0.0032  0.0168  -0.0016 790  ILE B O   
14751 C CB  . ILE B 792  ? 0.1681 0.2190 0.2337 0.0071  0.0146  -0.0065 790  ILE B CB  
14752 C CG1 . ILE B 792  ? 0.1726 0.2259 0.2389 0.0091  0.0152  -0.0079 790  ILE B CG1 
14753 C CG2 . ILE B 792  ? 0.1766 0.2250 0.2375 0.0077  0.0152  -0.0064 790  ILE B CG2 
14754 C CD1 . ILE B 792  ? 0.1842 0.2344 0.2475 0.0105  0.0139  -0.0098 790  ILE B CD1 
14755 N N   . GLN B 793  ? 0.1857 0.2335 0.2535 0.0023  0.0130  -0.0032 791  GLN B N   
14756 C CA  . GLN B 793  ? 0.2114 0.2556 0.2776 0.0006  0.0123  -0.0019 791  GLN B CA  
14757 C C   . GLN B 793  ? 0.2217 0.2682 0.2902 -0.0015 0.0136  0.0005  791  GLN B C   
14758 O O   . GLN B 793  ? 0.2135 0.2581 0.2795 -0.0022 0.0144  0.0020  791  GLN B O   
14759 C CB  . GLN B 793  ? 0.2151 0.2558 0.2817 -0.0002 0.0098  -0.0027 791  GLN B CB  
14760 C CG  . GLN B 793  ? 0.2363 0.2725 0.3010 -0.0017 0.0087  -0.0015 791  GLN B CG  
14761 C CD  . GLN B 793  ? 0.2695 0.3030 0.3354 -0.0030 0.0063  -0.0021 791  GLN B CD  
14762 O OE1 . GLN B 793  ? 0.2801 0.3164 0.3499 -0.0041 0.0057  -0.0021 791  GLN B OE1 
14763 N NE2 . GLN B 793  ? 0.3161 0.3443 0.3787 -0.0027 0.0048  -0.0026 791  GLN B NE2 
14764 N N   . ALA B 794  ? 0.2094 0.2603 0.2826 -0.0026 0.0139  0.0010  792  ALA B N   
14765 C CA  . ALA B 794  ? 0.2149 0.2689 0.2908 -0.0049 0.0153  0.0035  792  ALA B CA  
14766 C C   . ALA B 794  ? 0.2222 0.2792 0.2966 -0.0039 0.0182  0.0044  792  ALA B C   
14767 O O   . ALA B 794  ? 0.2540 0.3106 0.3273 -0.0055 0.0193  0.0066  792  ALA B O   
14768 C CB  . ALA B 794  ? 0.2545 0.3135 0.3362 -0.0062 0.0149  0.0038  792  ALA B CB  
14769 N N   . GLN B 795  ? 0.2097 0.2693 0.2835 -0.0011 0.0195  0.0029  793  GLN B N   
14770 C CA  . GLN B 795  ? 0.2121 0.2739 0.2836 0.0001  0.0222  0.0035  793  GLN B CA  
14771 C C   . GLN B 795  ? 0.2344 0.2915 0.3006 0.0000  0.0221  0.0042  793  GLN B C   
14772 O O   . GLN B 795  ? 0.2326 0.2907 0.2974 -0.0007 0.0239  0.0060  793  GLN B O   
14773 C CB  . GLN B 795  ? 0.2766 0.3401 0.3469 0.0033  0.0229  0.0013  793  GLN B CB  
14774 C CG  . GLN B 795  ? 0.3002 0.3689 0.3748 0.0044  0.0236  0.0006  793  GLN B CG  
14775 C CD  . GLN B 795  ? 0.3520 0.4205 0.4240 0.0077  0.0241  -0.0017 793  GLN B CD  
14776 O OE1 . GLN B 795  ? 0.3591 0.4247 0.4301 0.0088  0.0223  -0.0035 793  GLN B OE1 
14777 N NE2 . GLN B 795  ? 0.2996 0.3712 0.3704 0.0093  0.0267  -0.0015 793  GLN B NE2 
14778 N N   . LEU B 796  ? 0.2029 0.2551 0.2663 0.0009  0.0201  0.0027  794  LEU B N   
14779 C CA  . LEU B 796  ? 0.1987 0.2468 0.2571 0.0014  0.0200  0.0031  794  LEU B CA  
14780 C C   . LEU B 796  ? 0.2314 0.2768 0.2892 -0.0010 0.0195  0.0054  794  LEU B C   
14781 O O   . LEU B 796  ? 0.2611 0.3047 0.3154 -0.0009 0.0203  0.0067  794  LEU B O   
14782 C CB  . LEU B 796  ? 0.2022 0.2466 0.2582 0.0029  0.0179  0.0010  794  LEU B CB  
14783 C CG  . LEU B 796  ? 0.2108 0.2567 0.2658 0.0052  0.0183  -0.0011 794  LEU B CG  
14784 C CD1 . LEU B 796  ? 0.2104 0.2528 0.2632 0.0061  0.0162  -0.0028 794  LEU B CD1 
14785 C CD2 . LEU B 796  ? 0.2131 0.2602 0.2648 0.0064  0.0202  -0.0007 794  LEU B CD2 
14786 N N   . ALA B 797  ? 0.2344 0.2789 0.2953 -0.0031 0.0181  0.0060  795  ALA B N   
14787 C CA  . ALA B 797  ? 0.2674 0.3082 0.3274 -0.0055 0.0173  0.0081  795  ALA B CA  
14788 C C   . ALA B 797  ? 0.2931 0.3368 0.3537 -0.0073 0.0196  0.0108  795  ALA B C   
14789 O O   . ALA B 797  ? 0.3220 0.3621 0.3804 -0.0090 0.0193  0.0129  795  ALA B O   
14790 C CB  . ALA B 797  ? 0.2856 0.3246 0.3487 -0.0075 0.0151  0.0080  795  ALA B CB  
14791 N N   . ASP B 798  ? 0.2844 0.3344 0.3475 -0.0068 0.0219  0.0109  796  ASP B N   
14792 C CA  . ASP B 798  ? 0.3300 0.3833 0.3932 -0.0082 0.0244  0.0135  796  ASP B CA  
14793 C C   . ASP B 798  ? 0.3352 0.3863 0.3928 -0.0067 0.0257  0.0140  796  ASP B C   
14794 O O   . ASP B 798  ? 0.3646 0.4167 0.4210 -0.0081 0.0274  0.0164  796  ASP B O   
14795 C CB  . ASP B 798  ? 0.2677 0.3288 0.3352 -0.0076 0.0267  0.0132  796  ASP B CB  
14796 N N   . ARG B 799  ? 0.2909 0.3393 0.3451 -0.0040 0.0247  0.0118  797  ARG B N   
14797 C CA  . ARG B 799  ? 0.3485 0.3955 0.3975 -0.0022 0.0258  0.0119  797  ARG B CA  
14798 C C   . ARG B 799  ? 0.3286 0.3693 0.3736 -0.0018 0.0237  0.0119  797  ARG B C   
14799 O O   . ARG B 799  ? 0.2581 0.2953 0.3039 -0.0021 0.0213  0.0111  797  ARG B O   
14800 C CB  . ARG B 799  ? 0.3462 0.3957 0.3943 0.0008  0.0265  0.0093  797  ARG B CB  
14801 C CG  . ARG B 799  ? 0.4221 0.4778 0.4738 0.0012  0.0286  0.0089  797  ARG B CG  
14802 C CD  . ARG B 799  ? 0.4005 0.4579 0.4494 0.0041  0.0299  0.0071  797  ARG B CD  
14803 N NE  . ARG B 799  ? 0.3838 0.4392 0.4322 0.0060  0.0281  0.0043  797  ARG B NE  
14804 C CZ  . ARG B 799  ? 0.4038 0.4557 0.4479 0.0073  0.0269  0.0030  797  ARG B CZ  
14805 N NH1 . ARG B 799  ? 0.3494 0.3992 0.3892 0.0074  0.0272  0.0041  797  ARG B NH1 
14806 N NH2 . ARG B 799  ? 0.3217 0.3724 0.3659 0.0086  0.0252  0.0007  797  ARG B NH2 
14807 N N   . LEU B 800  ? 0.2830 0.3222 0.3233 -0.0009 0.0245  0.0129  798  LEU B N   
14808 C CA  . LEU B 800  ? 0.2839 0.3178 0.3199 0.0003  0.0226  0.0127  798  LEU B CA  
14809 C C   . LEU B 800  ? 0.3076 0.3427 0.3398 0.0027  0.0234  0.0116  798  LEU B C   
14810 O O   . LEU B 800  ? 0.3089 0.3478 0.3407 0.0031  0.0257  0.0118  798  LEU B O   
14811 C CB  . LEU B 800  ? 0.3300 0.3598 0.3634 -0.0014 0.0223  0.0155  798  LEU B CB  
14812 C CG  . LEU B 800  ? 0.3610 0.3880 0.3971 -0.0041 0.0210  0.0168  798  LEU B CG  
14813 C CD1 . LEU B 800  ? 0.3744 0.3973 0.4072 -0.0058 0.0210  0.0199  798  LEU B CD1 
14814 C CD2 . LEU B 800  ? 0.2842 0.3075 0.3207 -0.0030 0.0183  0.0147  798  LEU B CD2 
14815 N N   . SER B 801  ? 0.3048 0.3368 0.3342 0.0044  0.0216  0.0104  799  SER B N   
14816 C CA  . SER B 801  ? 0.2978 0.3303 0.3232 0.0064  0.0219  0.0097  799  SER B CA  
14817 C C   . SER B 801  ? 0.3559 0.3875 0.3775 0.0059  0.0232  0.0123  799  SER B C   
14818 O O   . SER B 801  ? 0.3616 0.3913 0.3835 0.0040  0.0234  0.0146  799  SER B O   
14819 C CB  . SER B 801  ? 0.3233 0.3528 0.3468 0.0081  0.0195  0.0083  799  SER B CB  
14820 O OG  . SER B 801  ? 0.3374 0.3626 0.3587 0.0077  0.0183  0.0101  799  SER B OG  
14821 N N   . PRO B 802  ? 0.4060 0.4387 0.4237 0.0074  0.0240  0.0119  800  PRO B N   
14822 C CA  . PRO B 802  ? 0.3980 0.4293 0.4113 0.0070  0.0249  0.0144  800  PRO B CA  
14823 C C   . PRO B 802  ? 0.3852 0.4112 0.3962 0.0069  0.0228  0.0160  800  PRO B C   
14824 O O   . PRO B 802  ? 0.4272 0.4511 0.4356 0.0058  0.0234  0.0187  800  PRO B O   
14825 C CB  . PRO B 802  ? 0.3750 0.4079 0.3844 0.0090  0.0254  0.0131  800  PRO B CB  
14826 C CG  . PRO B 802  ? 0.4056 0.4418 0.4179 0.0097  0.0259  0.0104  800  PRO B CG  
14827 C CD  . PRO B 802  ? 0.3820 0.4171 0.3988 0.0092  0.0242  0.0094  800  PRO B CD  
14828 N N   . ALA B 803  ? 0.4038 0.4278 0.4157 0.0081  0.0204  0.0144  801  ALA B N   
14829 C CA  . ALA B 803  ? 0.3975 0.4163 0.4076 0.0084  0.0183  0.0155  801  ALA B CA  
14830 C C   . ALA B 803  ? 0.3811 0.3972 0.3940 0.0062  0.0180  0.0169  801  ALA B C   
14831 O O   . ALA B 803  ? 0.4438 0.4549 0.4549 0.0063  0.0162  0.0179  801  ALA B O   
14832 C CB  . ALA B 803  ? 0.4075 0.4257 0.4178 0.0107  0.0160  0.0132  801  ALA B CB  
14833 N N   . GLY B 804  ? 0.3472 0.3663 0.3641 0.0043  0.0194  0.0168  802  GLY B N   
14834 C CA  . GLY B 804  ? 0.3679 0.3846 0.3874 0.0018  0.0190  0.0181  802  GLY B CA  
14835 C C   . GLY B 804  ? 0.3518 0.3664 0.3740 0.0022  0.0168  0.0162  802  GLY B C   
14836 O O   . GLY B 804  ? 0.3608 0.3709 0.3832 0.0009  0.0154  0.0172  802  GLY B O   
14837 N N   . ARG B 805  ? 0.3409 0.3584 0.3649 0.0039  0.0164  0.0134  803  ARG B N   
14838 C CA  . ARG B 805  ? 0.2927 0.3085 0.3188 0.0046  0.0145  0.0114  803  ARG B CA  
14839 C C   . ARG B 805  ? 0.2966 0.3168 0.3270 0.0042  0.0151  0.0095  803  ARG B C   
14840 O O   . ARG B 805  ? 0.2801 0.3047 0.3113 0.0043  0.0170  0.0092  803  ARG B O   
14841 C CB  . ARG B 805  ? 0.3314 0.3459 0.3548 0.0075  0.0129  0.0099  803  ARG B CB  
14842 C CG  . ARG B 805  ? 0.3800 0.3899 0.3991 0.0084  0.0119  0.0116  803  ARG B CG  
14843 C CD  . ARG B 805  ? 0.4158 0.4201 0.4347 0.0071  0.0106  0.0129  803  ARG B CD  
14844 N NE  . ARG B 805  ? 0.4555 0.4548 0.4699 0.0082  0.0094  0.0146  803  ARG B NE  
14845 C CZ  . ARG B 805  ? 0.4091 0.4059 0.4211 0.0068  0.0101  0.0174  803  ARG B CZ  
14846 N NH1 . ARG B 805  ? 0.4157 0.4147 0.4294 0.0039  0.0120  0.0190  803  ARG B NH1 
14847 N NH2 . ARG B 805  ? 0.4843 0.4764 0.4919 0.0083  0.0088  0.0188  803  ARG B NH2 
14848 N N   . PRO B 806  ? 0.2683 0.2872 0.3013 0.0038  0.0136  0.0083  804  PRO B N   
14849 C CA  . PRO B 806  ? 0.2513 0.2741 0.2884 0.0034  0.0141  0.0066  804  PRO B CA  
14850 C C   . PRO B 806  ? 0.2431 0.2691 0.2797 0.0054  0.0145  0.0045  804  PRO B C   
14851 O O   . PRO B 806  ? 0.2348 0.2595 0.2687 0.0073  0.0136  0.0036  804  PRO B O   
14852 C CB  . PRO B 806  ? 0.2620 0.2817 0.3007 0.0029  0.0120  0.0056  804  PRO B CB  
14853 C CG  . PRO B 806  ? 0.2934 0.3077 0.3297 0.0021  0.0109  0.0075  804  PRO B CG  
14854 C CD  . PRO B 806  ? 0.2853 0.2988 0.3175 0.0037  0.0115  0.0084  804  PRO B CD  
14855 N N   . ILE B 807  ? 0.2160 0.2462 0.2553 0.0051  0.0159  0.0038  805  ILE B N   
14856 C CA  . ILE B 807  ? 0.2033 0.2361 0.2422 0.0068  0.0162  0.0018  805  ILE B CA  
14857 C C   . ILE B 807  ? 0.1915 0.2233 0.2319 0.0074  0.0144  -0.0002 805  ILE B C   
14858 O O   . ILE B 807  ? 0.2139 0.2458 0.2575 0.0063  0.0138  -0.0004 805  ILE B O   
14859 C CB  . ILE B 807  ? 0.2006 0.2378 0.2418 0.0065  0.0182  0.0016  805  ILE B CB  
14860 C CG1 . ILE B 807  ? 0.2544 0.2931 0.2943 0.0058  0.0203  0.0037  805  ILE B CG1 
14861 C CG2 . ILE B 807  ? 0.2181 0.2570 0.2585 0.0083  0.0182  -0.0006 805  ILE B CG2 
14862 C CD1 . ILE B 807  ? 0.2929 0.3310 0.3281 0.0073  0.0209  0.0038  805  ILE B CD1 
14863 N N   . PRO B 808  ? 0.1857 0.2167 0.2239 0.0090  0.0133  -0.0016 806  PRO B N   
14864 C CA  . PRO B 808  ? 0.1800 0.2102 0.2194 0.0094  0.0117  -0.0033 806  PRO B CA  
14865 C C   . PRO B 808  ? 0.1982 0.2309 0.2402 0.0092  0.0120  -0.0047 806  PRO B C   
14866 O O   . PRO B 808  ? 0.1857 0.2208 0.2275 0.0096  0.0132  -0.0052 806  PRO B O   
14867 C CB  . PRO B 808  ? 0.2109 0.2409 0.2472 0.0111  0.0109  -0.0042 806  PRO B CB  
14868 C CG  . PRO B 808  ? 0.2558 0.2850 0.2892 0.0114  0.0116  -0.0026 806  PRO B CG  
14869 C CD  . PRO B 808  ? 0.1873 0.2181 0.2216 0.0103  0.0135  -0.0014 806  PRO B CD  
14870 N N   . LEU B 809  ? 0.1702 0.2019 0.2144 0.0087  0.0107  -0.0054 807  LEU B N   
14871 C CA  . LEU B 809  ? 0.1695 0.2031 0.2161 0.0086  0.0106  -0.0068 807  LEU B CA  
14872 C C   . LEU B 809  ? 0.1539 0.1859 0.2000 0.0091  0.0089  -0.0082 807  LEU B C   
14873 O O   . LEU B 809  ? 0.1822 0.2117 0.2283 0.0088  0.0077  -0.0081 807  LEU B O   
14874 C CB  . LEU B 809  ? 0.1817 0.2161 0.2319 0.0070  0.0108  -0.0060 807  LEU B CB  
14875 C CG  . LEU B 809  ? 0.1895 0.2254 0.2426 0.0069  0.0101  -0.0072 807  LEU B CG  
14876 C CD1 . LEU B 809  ? 0.1724 0.2110 0.2253 0.0081  0.0113  -0.0081 807  LEU B CD1 
14877 C CD2 . LEU B 809  ? 0.1957 0.2326 0.2525 0.0052  0.0100  -0.0062 807  LEU B CD2 
14878 N N   . ILE B 810  ? 0.1514 0.1847 0.1969 0.0099  0.0087  -0.0096 808  ILE B N   
14879 C CA  . ILE B 810  ? 0.1544 0.1869 0.1999 0.0101  0.0073  -0.0110 808  ILE B CA  
14880 C C   . ILE B 810  ? 0.1656 0.1991 0.2137 0.0096  0.0073  -0.0116 808  ILE B C   
14881 O O   . ILE B 810  ? 0.1819 0.2172 0.2303 0.0099  0.0082  -0.0119 808  ILE B O   
14882 C CB  . ILE B 810  ? 0.1671 0.2002 0.2101 0.0110  0.0071  -0.0120 808  ILE B CB  
14883 C CG1 . ILE B 810  ? 0.1796 0.2124 0.2203 0.0117  0.0073  -0.0113 808  ILE B CG1 
14884 C CG2 . ILE B 810  ? 0.1914 0.2239 0.2345 0.0111  0.0058  -0.0132 808  ILE B CG2 
14885 C CD1 . ILE B 810  ? 0.1920 0.2261 0.2306 0.0124  0.0068  -0.0122 808  ILE B CD1 
14886 N N   . ALA B 811  ? 0.1712 0.2036 0.2211 0.0089  0.0061  -0.0118 809  ALA B N   
14887 C CA  . ALA B 811  ? 0.1588 0.1923 0.2114 0.0084  0.0058  -0.0122 809  ALA B CA  
14888 C C   . ALA B 811  ? 0.1630 0.1949 0.2151 0.0085  0.0042  -0.0134 809  ALA B C   
14889 O O   . ALA B 811  ? 0.1846 0.2146 0.2368 0.0080  0.0030  -0.0133 809  ALA B O   
14890 C CB  . ALA B 811  ? 0.1912 0.2253 0.2468 0.0072  0.0060  -0.0109 809  ALA B CB  
14891 N N   . GLU B 812  ? 0.1560 0.1887 0.2073 0.0091  0.0040  -0.0144 810  GLU B N   
14892 C CA  . GLU B 812  ? 0.1538 0.1852 0.2041 0.0091  0.0026  -0.0155 810  GLU B CA  
14893 C C   . GLU B 812  ? 0.1789 0.2110 0.2315 0.0089  0.0020  -0.0158 810  GLU B C   
14894 O O   . GLU B 812  ? 0.1792 0.2125 0.2322 0.0093  0.0027  -0.0160 810  GLU B O   
14895 C CB  . GLU B 812  ? 0.1888 0.2204 0.2363 0.0097  0.0028  -0.0162 810  GLU B CB  
14896 C CG  . GLU B 812  ? 0.1843 0.2160 0.2301 0.0101  0.0033  -0.0157 810  GLU B CG  
14897 C CD  . GLU B 812  ? 0.2214 0.2514 0.2668 0.0102  0.0025  -0.0156 810  GLU B CD  
14898 O OE1 . GLU B 812  ? 0.2120 0.2415 0.2562 0.0105  0.0017  -0.0164 810  GLU B OE1 
14899 O OE2 . GLU B 812  ? 0.2127 0.2417 0.2588 0.0101  0.0027  -0.0148 810  GLU B OE2 
14900 N N   . THR B 813  ? 0.1710 0.2019 0.2247 0.0082  0.0007  -0.0159 811  THR B N   
14901 C CA  . THR B 813  ? 0.1680 0.2000 0.2247 0.0078  0.0000  -0.0158 811  THR B CA  
14902 C C   . THR B 813  ? 0.1642 0.1948 0.2202 0.0078  -0.0017 -0.0168 811  THR B C   
14903 O O   . THR B 813  ? 0.1797 0.2090 0.2328 0.0082  -0.0020 -0.0175 811  THR B O   
14904 C CB  . THR B 813  ? 0.1729 0.2056 0.2324 0.0068  0.0001  -0.0147 811  THR B CB  
14905 O OG1 . THR B 813  ? 0.1793 0.2092 0.2372 0.0062  -0.0007 -0.0147 811  THR B OG1 
14906 C CG2 . THR B 813  ? 0.1938 0.2285 0.2540 0.0069  0.0021  -0.0137 811  THR B CG2 
14907 N N   . GLY B 814  ? 0.1835 0.2143 0.2419 0.0072  -0.0029 -0.0166 812  GLY B N   
14908 C CA  . GLY B 814  ? 0.1875 0.2174 0.2454 0.0073  -0.0045 -0.0174 812  GLY B CA  
14909 C C   . GLY B 814  ? 0.1876 0.2148 0.2430 0.0069  -0.0058 -0.0180 812  GLY B C   
14910 O O   . GLY B 814  ? 0.2180 0.2439 0.2720 0.0067  -0.0055 -0.0180 812  GLY B O   
14911 N N   . GLY B 815  ? 0.1726 0.1988 0.2270 0.0070  -0.0072 -0.0187 813  GLY B N   
14912 C CA  . GLY B 815  ? 0.1730 0.1967 0.2247 0.0067  -0.0085 -0.0194 813  GLY B CA  
14913 C C   . GLY B 815  ? 0.1799 0.2030 0.2326 0.0063  -0.0105 -0.0196 813  GLY B C   
14914 O O   . GLY B 815  ? 0.2189 0.2436 0.2740 0.0064  -0.0109 -0.0193 813  GLY B O   
14915 N N   . GLN B 816  ? 0.1745 0.1952 0.2251 0.0059  -0.0118 -0.0202 814  GLN B N   
14916 C CA  . GLN B 816  ? 0.1860 0.2055 0.2363 0.0055  -0.0140 -0.0207 814  GLN B CA  
14917 C C   . GLN B 816  ? 0.1772 0.1943 0.2229 0.0059  -0.0143 -0.0215 814  GLN B C   
14918 O O   . GLN B 816  ? 0.1962 0.2110 0.2400 0.0057  -0.0154 -0.0222 814  GLN B O   
14919 C CB  . GLN B 816  ? 0.1905 0.2095 0.2432 0.0043  -0.0155 -0.0204 814  GLN B CB  
14920 C CG  . GLN B 816  ? 0.1921 0.2107 0.2454 0.0038  -0.0179 -0.0207 814  GLN B CG  
14921 C CD  . GLN B 816  ? 0.1896 0.2111 0.2458 0.0043  -0.0179 -0.0201 814  GLN B CD  
14922 O OE1 . GLN B 816  ? 0.2076 0.2290 0.2620 0.0053  -0.0175 -0.0203 814  GLN B OE1 
14923 N NE2 . GLN B 816  ? 0.1890 0.2133 0.2500 0.0036  -0.0185 -0.0194 814  GLN B NE2 
14924 N N   . ASN B 817  ? 0.1554 0.1729 0.1989 0.0065  -0.0135 -0.0216 815  ASN B N   
14925 C CA  . ASN B 817  ? 0.1617 0.1782 0.2012 0.0069  -0.0129 -0.0222 815  ASN B CA  
14926 C C   . ASN B 817  ? 0.1776 0.1922 0.2141 0.0068  -0.0145 -0.0228 815  ASN B C   
14927 O O   . ASN B 817  ? 0.1837 0.1982 0.2205 0.0065  -0.0156 -0.0225 815  ASN B O   
14928 C CB  . ASN B 817  ? 0.1740 0.1922 0.2127 0.0072  -0.0113 -0.0218 815  ASN B CB  
14929 C CG  . ASN B 817  ? 0.1565 0.1765 0.1980 0.0073  -0.0098 -0.0213 815  ASN B CG  
14930 O OD1 . ASN B 817  ? 0.1615 0.1816 0.2037 0.0075  -0.0091 -0.0212 815  ASN B OD1 
14931 N ND2 . ASN B 817  ? 0.1615 0.1825 0.2040 0.0074  -0.0094 -0.0208 815  ASN B ND2 
14932 N N   . ALA B 818  ? 0.1600 0.1730 0.1935 0.0071  -0.0146 -0.0235 816  ALA B N   
14933 C CA  . ALA B 818  ? 0.1709 0.1820 0.2010 0.0071  -0.0160 -0.0242 816  ALA B CA  
14934 C C   . ALA B 818  ? 0.1590 0.1707 0.1853 0.0076  -0.0147 -0.0244 816  ALA B C   
14935 O O   . ALA B 818  ? 0.1751 0.1885 0.2013 0.0082  -0.0129 -0.0243 816  ALA B O   
14936 C CB  . ALA B 818  ? 0.1854 0.1938 0.2144 0.0072  -0.0174 -0.0251 816  ALA B CB  
14937 N N   . MET B 819  ? 0.1687 0.1792 0.1919 0.0074  -0.0157 -0.0246 817  MET B N   
14938 C CA  . MET B 819  ? 0.1633 0.1744 0.1824 0.0078  -0.0147 -0.0249 817  MET B CA  
14939 C C   . MET B 819  ? 0.1858 0.1942 0.2014 0.0081  -0.0162 -0.0258 817  MET B C   
14940 O O   . MET B 819  ? 0.1917 0.1983 0.2071 0.0075  -0.0182 -0.0258 817  MET B O   
14941 C CB  . MET B 819  ? 0.1756 0.1877 0.1936 0.0069  -0.0143 -0.0240 817  MET B CB  
14942 C CG  . MET B 819  ? 0.1912 0.2042 0.2048 0.0069  -0.0133 -0.0240 817  MET B CG  
14943 S SD  . MET B 819  ? 0.2234 0.2367 0.2353 0.0054  -0.0133 -0.0227 817  MET B SD  
14944 C CE  . MET B 819  ? 0.2491 0.2653 0.2640 0.0050  -0.0115 -0.0220 817  MET B CE  
14945 N N   . ILE B 820  ? 0.1897 0.1978 0.2024 0.0092  -0.0154 -0.0268 818  ILE B N   
14946 C CA  . ILE B 820  ? 0.1729 0.1784 0.1815 0.0098  -0.0166 -0.0279 818  ILE B CA  
14947 C C   . ILE B 820  ? 0.1925 0.1994 0.1969 0.0099  -0.0155 -0.0277 818  ILE B C   
14948 O O   . ILE B 820  ? 0.1916 0.2017 0.1958 0.0104  -0.0133 -0.0274 818  ILE B O   
14949 C CB  . ILE B 820  ? 0.1928 0.1964 0.2002 0.0112  -0.0165 -0.0291 818  ILE B CB  
14950 C CG1 . ILE B 820  ? 0.2047 0.2066 0.2161 0.0106  -0.0178 -0.0291 818  ILE B CG1 
14951 C CG2 . ILE B 820  ? 0.2212 0.2218 0.2234 0.0121  -0.0177 -0.0305 818  ILE B CG2 
14952 C CD1 . ILE B 820  ? 0.2285 0.2277 0.2387 0.0118  -0.0180 -0.0302 818  ILE B CD1 
14953 N N   . VAL B 821  ? 0.2033 0.2083 0.2046 0.0094  -0.0170 -0.0278 819  VAL B N   
14954 C CA  . VAL B 821  ? 0.1978 0.2039 0.1948 0.0092  -0.0162 -0.0274 819  VAL B CA  
14955 C C   . VAL B 821  ? 0.2176 0.2210 0.2097 0.0102  -0.0172 -0.0287 819  VAL B C   
14956 O O   . VAL B 821  ? 0.2237 0.2237 0.2151 0.0099  -0.0197 -0.0292 819  VAL B O   
14957 C CB  . VAL B 821  ? 0.1889 0.1947 0.1861 0.0075  -0.0172 -0.0260 819  VAL B CB  
14958 C CG1 . VAL B 821  ? 0.2311 0.2378 0.2236 0.0070  -0.0162 -0.0254 819  VAL B CG1 
14959 C CG2 . VAL B 821  ? 0.1987 0.2064 0.2007 0.0067  -0.0164 -0.0249 819  VAL B CG2 
14960 N N   . ASP B 822  ? 0.2110 0.2160 0.1995 0.0114  -0.0154 -0.0293 820  ASP B N   
14961 C CA  . ASP B 822  ? 0.2319 0.2343 0.2150 0.0126  -0.0162 -0.0307 820  ASP B CA  
14962 C C   . ASP B 822  ? 0.2569 0.2602 0.2357 0.0117  -0.0159 -0.0299 820  ASP B C   
14963 O O   . ASP B 822  ? 0.2448 0.2503 0.2247 0.0101  -0.0151 -0.0282 820  ASP B O   
14964 C CB  . ASP B 822  ? 0.2489 0.2514 0.2303 0.0150  -0.0148 -0.0323 820  ASP B CB  
14965 C CG  . ASP B 822  ? 0.2539 0.2614 0.2341 0.0160  -0.0117 -0.0319 820  ASP B CG  
14966 O OD1 . ASP B 822  ? 0.2406 0.2513 0.2202 0.0146  -0.0106 -0.0305 820  ASP B OD1 
14967 O OD2 . ASP B 822  ? 0.2629 0.2712 0.2426 0.0182  -0.0104 -0.0331 820  ASP B OD2 
14968 N N   . SER B 823  ? 0.2661 0.2671 0.2392 0.0127  -0.0165 -0.0310 821  SER B N   
14969 C CA  . SER B 823  ? 0.2703 0.2716 0.2387 0.0119  -0.0164 -0.0302 821  SER B CA  
14970 C C   . SER B 823  ? 0.2982 0.3046 0.2652 0.0120  -0.0131 -0.0293 821  SER B C   
14971 O O   . SER B 823  ? 0.3189 0.3262 0.2822 0.0108  -0.0127 -0.0283 821  SER B O   
14972 C CB  . SER B 823  ? 0.2880 0.2853 0.2506 0.0129  -0.0181 -0.0318 821  SER B CB  
14973 O OG  . SER B 823  ? 0.3314 0.3287 0.2914 0.0154  -0.0167 -0.0336 821  SER B OG  
14974 N N   . SER B 824  ? 0.2456 0.2556 0.2154 0.0131  -0.0109 -0.0297 822  SER B N   
14975 C CA  . SER B 824  ? 0.2501 0.2659 0.2193 0.0130  -0.0079 -0.0287 822  SER B CA  
14976 C C   . SER B 824  ? 0.2718 0.2906 0.2452 0.0106  -0.0072 -0.0266 822  SER B C   
14977 O O   . SER B 824  ? 0.2736 0.2971 0.2465 0.0097  -0.0051 -0.0254 822  SER B O   
14978 C CB  . SER B 824  ? 0.2668 0.2855 0.2365 0.0158  -0.0059 -0.0301 822  SER B CB  
14979 O OG  . SER B 824  ? 0.2502 0.2700 0.2257 0.0159  -0.0057 -0.0299 822  SER B OG  
14980 N N   . ALA B 825  ? 0.2436 0.2599 0.2211 0.0095  -0.0090 -0.0262 823  ALA B N   
14981 C CA  . ALA B 825  ? 0.2463 0.2648 0.2275 0.0075  -0.0085 -0.0245 823  ALA B CA  
14982 C C   . ALA B 825  ? 0.2610 0.2789 0.2393 0.0051  -0.0089 -0.0227 823  ALA B C   
14983 O O   . ALA B 825  ? 0.2993 0.3139 0.2737 0.0049  -0.0104 -0.0228 823  ALA B O   
14984 C CB  . ALA B 825  ? 0.2413 0.2568 0.2270 0.0072  -0.0103 -0.0246 823  ALA B CB  
14985 N N   . LEU B 826  ? 0.2669 0.2879 0.2470 0.0032  -0.0076 -0.0212 824  LEU B N   
14986 C CA  . LEU B 826  ? 0.2588 0.2788 0.2362 0.0007  -0.0081 -0.0193 824  LEU B CA  
14987 C C   . LEU B 826  ? 0.2865 0.3020 0.2661 -0.0002 -0.0105 -0.0188 824  LEU B C   
14988 O O   . LEU B 826  ? 0.2565 0.2724 0.2404 -0.0004 -0.0105 -0.0187 824  LEU B O   
14989 C CB  . LEU B 826  ? 0.3227 0.3476 0.3008 -0.0012 -0.0059 -0.0178 824  LEU B CB  
14990 C CG  . LEU B 826  ? 0.3617 0.3857 0.3366 -0.0042 -0.0061 -0.0157 824  LEU B CG  
14991 C CD1 . LEU B 826  ? 0.3987 0.4213 0.3678 -0.0042 -0.0064 -0.0155 824  LEU B CD1 
14992 C CD2 . LEU B 826  ? 0.4530 0.4825 0.4291 -0.0062 -0.0039 -0.0143 824  LEU B CD2 
14993 N N   . ALA B 827  ? 0.2844 0.2957 0.2607 -0.0006 -0.0126 -0.0184 825  ALA B N   
14994 C CA  . ALA B 827  ? 0.2549 0.2620 0.2332 -0.0009 -0.0152 -0.0181 825  ALA B CA  
14995 C C   . ALA B 827  ? 0.2559 0.2631 0.2365 -0.0026 -0.0149 -0.0167 825  ALA B C   
14996 O O   . ALA B 827  ? 0.2465 0.2525 0.2312 -0.0021 -0.0158 -0.0170 825  ALA B O   
14997 C CB  . ALA B 827  ? 0.2759 0.2789 0.2497 -0.0012 -0.0174 -0.0177 825  ALA B CB  
14998 N N   . GLU B 828  ? 0.2669 0.2755 0.2448 -0.0047 -0.0137 -0.0151 826  GLU B N   
14999 C CA  . GLU B 828  ? 0.2740 0.2818 0.2533 -0.0066 -0.0137 -0.0138 826  GLU B CA  
15000 C C   . GLU B 828  ? 0.2698 0.2807 0.2543 -0.0060 -0.0124 -0.0145 826  GLU B C   
15001 O O   . GLU B 828  ? 0.2529 0.2620 0.2401 -0.0063 -0.0132 -0.0143 826  GLU B O   
15002 C CB  . GLU B 828  ? 0.2944 0.3036 0.2698 -0.0093 -0.0125 -0.0120 826  GLU B CB  
15003 C CG  . GLU B 828  ? 0.3379 0.3429 0.3079 -0.0105 -0.0141 -0.0107 826  GLU B CG  
15004 C CD  . GLU B 828  ? 0.3640 0.3698 0.3301 -0.0094 -0.0139 -0.0112 826  GLU B CD  
15005 O OE1 . GLU B 828  ? 0.3500 0.3593 0.3176 -0.0076 -0.0125 -0.0128 826  GLU B OE1 
15006 O OE2 . GLU B 828  ? 0.3773 0.3797 0.3385 -0.0104 -0.0151 -0.0101 826  GLU B OE2 
15007 N N   . GLN B 829  ? 0.2419 0.2574 0.2278 -0.0050 -0.0105 -0.0154 827  GLN B N   
15008 C CA  . GLN B 829  ? 0.2496 0.2681 0.2401 -0.0043 -0.0093 -0.0161 827  GLN B CA  
15009 C C   . GLN B 829  ? 0.2403 0.2564 0.2344 -0.0024 -0.0106 -0.0173 827  GLN B C   
15010 O O   . GLN B 829  ? 0.2310 0.2470 0.2285 -0.0024 -0.0107 -0.0173 827  GLN B O   
15011 C CB  . GLN B 829  ? 0.3189 0.3427 0.3098 -0.0033 -0.0070 -0.0168 827  GLN B CB  
15012 C CG  . GLN B 829  ? 0.3596 0.3878 0.3486 -0.0052 -0.0052 -0.0155 827  GLN B CG  
15013 C CD  . GLN B 829  ? 0.4441 0.4781 0.4344 -0.0036 -0.0030 -0.0163 827  GLN B CD  
15014 O OE1 . GLN B 829  ? 0.3792 0.4129 0.3697 -0.0010 -0.0030 -0.0179 827  GLN B OE1 
15015 N NE2 . GLN B 829  ? 0.4952 0.5344 0.4862 -0.0052 -0.0012 -0.0153 827  GLN B NE2 
15016 N N   . VAL B 830  ? 0.2236 0.2379 0.2168 -0.0008 -0.0116 -0.0184 828  VAL B N   
15017 C CA  . VAL B 830  ? 0.2076 0.2197 0.2041 0.0007  -0.0131 -0.0194 828  VAL B CA  
15018 C C   . VAL B 830  ? 0.2371 0.2463 0.2351 0.0000  -0.0147 -0.0186 828  VAL B C   
15019 O O   . VAL B 830  ? 0.2186 0.2279 0.2206 0.0005  -0.0149 -0.0189 828  VAL B O   
15020 C CB  . VAL B 830  ? 0.2207 0.2307 0.2152 0.0020  -0.0145 -0.0205 828  VAL B CB  
15021 C CG1 . VAL B 830  ? 0.2271 0.2348 0.2250 0.0029  -0.0164 -0.0212 828  VAL B CG1 
15022 C CG2 . VAL B 830  ? 0.2497 0.2622 0.2429 0.0032  -0.0129 -0.0216 828  VAL B CG2 
15023 N N   . VAL B 831  ? 0.2218 0.2282 0.2162 -0.0012 -0.0160 -0.0176 829  VAL B N   
15024 C CA  . VAL B 831  ? 0.2224 0.2254 0.2177 -0.0014 -0.0178 -0.0169 829  VAL B CA  
15025 C C   . VAL B 831  ? 0.2245 0.2282 0.2221 -0.0022 -0.0168 -0.0163 829  VAL B C   
15026 O O   . VAL B 831  ? 0.2223 0.2249 0.2231 -0.0013 -0.0175 -0.0166 829  VAL B O   
15027 C CB  . VAL B 831  ? 0.2324 0.2318 0.2230 -0.0023 -0.0194 -0.0158 829  VAL B CB  
15028 C CG1 . VAL B 831  ? 0.2430 0.2389 0.2340 -0.0026 -0.0210 -0.0149 829  VAL B CG1 
15029 C CG2 . VAL B 831  ? 0.2401 0.2381 0.2293 -0.0011 -0.0211 -0.0166 829  VAL B CG2 
15030 N N   . GLY B 832  ? 0.2099 0.2157 0.2058 -0.0039 -0.0151 -0.0156 830  GLY B N   
15031 C CA  . GLY B 832  ? 0.2231 0.2295 0.2208 -0.0048 -0.0143 -0.0152 830  GLY B CA  
15032 C C   . GLY B 832  ? 0.2222 0.2311 0.2247 -0.0032 -0.0134 -0.0163 830  GLY B C   
15033 O O   . GLY B 832  ? 0.2290 0.2368 0.2338 -0.0029 -0.0137 -0.0164 830  GLY B O   
15034 N N   . ASP B 833  ? 0.1943 0.2063 0.1981 -0.0021 -0.0124 -0.0172 831  ASP B N   
15035 C CA  . ASP B 833  ? 0.2156 0.2298 0.2235 -0.0008 -0.0115 -0.0181 831  ASP B CA  
15036 C C   . ASP B 833  ? 0.1974 0.2094 0.2081 0.0007  -0.0129 -0.0188 831  ASP B C   
15037 O O   . ASP B 833  ? 0.1954 0.2082 0.2096 0.0014  -0.0125 -0.0191 831  ASP B O   
15038 C CB  . ASP B 833  ? 0.2093 0.2270 0.2174 0.0001  -0.0101 -0.0189 831  ASP B CB  
15039 C CG  . ASP B 833  ? 0.2128 0.2340 0.2193 -0.0012 -0.0084 -0.0182 831  ASP B CG  
15040 O OD1 . ASP B 833  ? 0.2493 0.2706 0.2555 -0.0029 -0.0082 -0.0172 831  ASP B OD1 
15041 O OD2 . ASP B 833  ? 0.2360 0.2601 0.2415 -0.0004 -0.0072 -0.0187 831  ASP B OD2 
15042 N N   . VAL B 834  ? 0.1967 0.2062 0.2061 0.0012  -0.0146 -0.0189 832  VAL B N   
15043 C CA  . VAL B 834  ? 0.2103 0.2183 0.2227 0.0024  -0.0161 -0.0193 832  VAL B CA  
15044 C C   . VAL B 834  ? 0.2061 0.2123 0.2196 0.0023  -0.0168 -0.0187 832  VAL B C   
15045 O O   . VAL B 834  ? 0.2076 0.2143 0.2248 0.0033  -0.0168 -0.0191 832  VAL B O   
15046 C CB  . VAL B 834  ? 0.1980 0.2039 0.2084 0.0027  -0.0180 -0.0196 832  VAL B CB  
15047 C CG1 . VAL B 834  ? 0.2188 0.2232 0.2320 0.0037  -0.0200 -0.0196 832  VAL B CG1 
15048 C CG2 . VAL B 834  ? 0.2052 0.2125 0.2154 0.0034  -0.0176 -0.0206 832  VAL B CG2 
15049 N N   . ILE B 835  ? 0.2020 0.2059 0.2120 0.0012  -0.0173 -0.0178 833  ILE B N   
15050 C CA  . ILE B 835  ? 0.2385 0.2398 0.2489 0.0013  -0.0181 -0.0173 833  ILE B CA  
15051 C C   . ILE B 835  ? 0.2285 0.2316 0.2413 0.0013  -0.0165 -0.0176 833  ILE B C   
15052 O O   . ILE B 835  ? 0.2521 0.2548 0.2677 0.0026  -0.0167 -0.0179 833  ILE B O   
15053 C CB  . ILE B 835  ? 0.2623 0.2602 0.2679 -0.0002 -0.0190 -0.0162 833  ILE B CB  
15054 C CG1 . ILE B 835  ? 0.2979 0.2934 0.3013 0.0003  -0.0210 -0.0159 833  ILE B CG1 
15055 C CG2 . ILE B 835  ? 0.3047 0.2995 0.3100 -0.0001 -0.0195 -0.0158 833  ILE B CG2 
15056 C CD1 . ILE B 835  ? 0.3482 0.3397 0.3467 -0.0010 -0.0221 -0.0147 833  ILE B CD1 
15057 N N   . THR B 836  ? 0.2104 0.2158 0.2223 0.0000  -0.0148 -0.0174 834  THR B N   
15058 C CA  . THR B 836  ? 0.2102 0.2176 0.2242 0.0000  -0.0134 -0.0177 834  THR B CA  
15059 C C   . THR B 836  ? 0.2507 0.2602 0.2690 0.0018  -0.0129 -0.0185 834  THR B C   
15060 O O   . THR B 836  ? 0.2773 0.2867 0.2978 0.0026  -0.0126 -0.0188 834  THR B O   
15061 C CB  . THR B 836  ? 0.2402 0.2506 0.2527 -0.0016 -0.0118 -0.0174 834  THR B CB  
15062 O OG1 . THR B 836  ? 0.3220 0.3306 0.3306 -0.0036 -0.0123 -0.0163 834  THR B OG1 
15063 C CG2 . THR B 836  ? 0.2808 0.2937 0.2956 -0.0015 -0.0104 -0.0177 834  THR B CG2 
15064 N N   . SER B 837  ? 0.1899 0.2011 0.2093 0.0024  -0.0128 -0.0190 835  SER B N   
15065 C CA  . SER B 837  ? 0.1924 0.2057 0.2156 0.0036  -0.0121 -0.0197 835  SER B CA  
15066 C C   . SER B 837  ? 0.1822 0.1944 0.2083 0.0048  -0.0133 -0.0198 835  SER B C   
15067 O O   . SER B 837  ? 0.1908 0.2044 0.2201 0.0056  -0.0127 -0.0201 835  SER B O   
15068 C CB  . SER B 837  ? 0.1767 0.1915 0.1997 0.0039  -0.0118 -0.0202 835  SER B CB  
15069 O OG  . SER B 837  ? 0.1784 0.1950 0.1992 0.0031  -0.0105 -0.0200 835  SER B OG  
15070 N N   . ALA B 838  ? 0.1890 0.1989 0.2138 0.0049  -0.0151 -0.0197 836  ALA B N   
15071 C CA  . ALA B 838  ? 0.1898 0.1995 0.2177 0.0061  -0.0165 -0.0198 836  ALA B CA  
15072 C C   . ALA B 838  ? 0.1984 0.2065 0.2267 0.0069  -0.0170 -0.0195 836  ALA B C   
15073 O O   . ALA B 838  ? 0.2225 0.2318 0.2545 0.0081  -0.0171 -0.0196 836  ALA B O   
15074 C CB  . ALA B 838  ? 0.1909 0.1992 0.2174 0.0061  -0.0184 -0.0198 836  ALA B CB  
15075 N N   . PHE B 839  ? 0.2123 0.2176 0.2368 0.0062  -0.0173 -0.0190 837  PHE B N   
15076 C CA  . PHE B 839  ? 0.2323 0.2350 0.2564 0.0072  -0.0183 -0.0187 837  PHE B CA  
15077 C C   . PHE B 839  ? 0.2670 0.2682 0.2894 0.0068  -0.0173 -0.0186 837  PHE B C   
15078 O O   . PHE B 839  ? 0.2685 0.2679 0.2914 0.0082  -0.0178 -0.0187 837  PHE B O   
15079 C CB  . PHE B 839  ? 0.2308 0.2301 0.2515 0.0069  -0.0204 -0.0182 837  PHE B CB  
15080 C CG  . PHE B 839  ? 0.2123 0.2127 0.2343 0.0073  -0.0218 -0.0183 837  PHE B CG  
15081 C CD1 . PHE B 839  ? 0.2129 0.2152 0.2394 0.0089  -0.0226 -0.0187 837  PHE B CD1 
15082 C CD2 . PHE B 839  ? 0.2446 0.2442 0.2633 0.0061  -0.0223 -0.0181 837  PHE B CD2 
15083 C CE1 . PHE B 839  ? 0.2063 0.2095 0.2340 0.0090  -0.0241 -0.0188 837  PHE B CE1 
15084 C CE2 . PHE B 839  ? 0.2485 0.2486 0.2680 0.0065  -0.0238 -0.0184 837  PHE B CE2 
15085 C CZ  . PHE B 839  ? 0.2442 0.2460 0.2682 0.0078  -0.0248 -0.0187 837  PHE B CZ  
15086 N N   . ASP B 840  ? 0.2496 0.2515 0.2701 0.0051  -0.0160 -0.0185 838  ASP B N   
15087 C CA  . ASP B 840  ? 0.2543 0.2553 0.2737 0.0047  -0.0151 -0.0186 838  ASP B CA  
15088 C C   . ASP B 840  ? 0.2539 0.2569 0.2772 0.0065  -0.0141 -0.0192 838  ASP B C   
15089 O O   . ASP B 840  ? 0.2525 0.2589 0.2794 0.0072  -0.0134 -0.0195 838  ASP B O   
15090 C CB  . ASP B 840  ? 0.3387 0.3414 0.3563 0.0026  -0.0138 -0.0183 838  ASP B CB  
15091 N N   . SER B 841  ? 0.2413 0.2420 0.2635 0.0071  -0.0140 -0.0194 839  SER B N   
15092 C CA  . SER B 841  ? 0.2209 0.2232 0.2463 0.0091  -0.0131 -0.0200 839  SER B CA  
15093 C C   . SER B 841  ? 0.2269 0.2308 0.2560 0.0111  -0.0138 -0.0201 839  SER B C   
15094 O O   . SER B 841  ? 0.2052 0.2122 0.2380 0.0123  -0.0127 -0.0204 839  SER B O   
15095 C CB  . SER B 841  ? 0.2699 0.2759 0.2972 0.0085  -0.0111 -0.0203 839  SER B CB  
15096 O OG  . SER B 841  ? 0.2957 0.3008 0.3198 0.0066  -0.0107 -0.0201 839  SER B OG  
15097 N N   . ALA B 842  ? 0.2137 0.2157 0.2418 0.0112  -0.0156 -0.0198 840  ALA B N   
15098 C CA  . ALA B 842  ? 0.1939 0.1978 0.2256 0.0128  -0.0166 -0.0198 840  ALA B CA  
15099 C C   . ALA B 842  ? 0.1701 0.1786 0.2060 0.0125  -0.0156 -0.0199 840  ALA B C   
15100 O O   . ALA B 842  ? 0.1865 0.1979 0.2266 0.0138  -0.0156 -0.0200 840  ALA B O   
15101 C CB  . ALA B 842  ? 0.2128 0.2161 0.2461 0.0154  -0.0170 -0.0201 840  ALA B CB  
15102 N N   . GLY B 843  ? 0.1843 0.1936 0.2189 0.0106  -0.0149 -0.0198 841  GLY B N   
15103 C CA  . GLY B 843  ? 0.1858 0.1985 0.2235 0.0103  -0.0141 -0.0199 841  GLY B CA  
15104 C C   . GLY B 843  ? 0.1749 0.1905 0.2157 0.0109  -0.0123 -0.0201 841  GLY B C   
15105 O O   . GLY B 843  ? 0.1785 0.1967 0.2224 0.0107  -0.0119 -0.0201 841  GLY B O   
15106 N N   . GLN B 844  ? 0.1647 0.1794 0.2045 0.0115  -0.0114 -0.0202 842  GLN B N   
15107 C CA  . GLN B 844  ? 0.1632 0.1804 0.2055 0.0122  -0.0096 -0.0204 842  GLN B CA  
15108 C C   . GLN B 844  ? 0.1894 0.2073 0.2301 0.0110  -0.0082 -0.0204 842  GLN B C   
15109 O O   . GLN B 844  ? 0.1957 0.2132 0.2352 0.0112  -0.0071 -0.0206 842  GLN B O   
15110 C CB  . GLN B 844  ? 0.1681 0.1841 0.2101 0.0140  -0.0094 -0.0207 842  GLN B CB  
15111 C CG  . GLN B 844  ? 0.1719 0.1884 0.2164 0.0156  -0.0108 -0.0206 842  GLN B CG  
15112 C CD  . GLN B 844  ? 0.1779 0.1923 0.2212 0.0178  -0.0110 -0.0210 842  GLN B CD  
15113 O OE1 . GLN B 844  ? 0.1757 0.1927 0.2223 0.0197  -0.0104 -0.0211 842  GLN B OE1 
15114 N NE2 . GLN B 844  ? 0.2037 0.2133 0.2422 0.0174  -0.0117 -0.0212 842  GLN B NE2 
15115 N N   . ARG B 845  ? 0.1895 0.2082 0.2302 0.0098  -0.0083 -0.0203 843  ARG B N   
15116 C CA  . ARG B 845  ? 0.1803 0.2004 0.2203 0.0089  -0.0070 -0.0202 843  ARG B CA  
15117 C C   . ARG B 845  ? 0.1639 0.1861 0.2068 0.0089  -0.0068 -0.0201 843  ARG B C   
15118 O O   . ARG B 845  ? 0.1777 0.1996 0.2215 0.0088  -0.0080 -0.0201 843  ARG B O   
15119 C CB  . ARG B 845  ? 0.1851 0.2041 0.2217 0.0076  -0.0074 -0.0202 843  ARG B CB  
15120 C CG  . ARG B 845  ? 0.2036 0.2201 0.2368 0.0070  -0.0078 -0.0202 843  ARG B CG  
15121 C CD  . ARG B 845  ? 0.2898 0.3065 0.3202 0.0054  -0.0078 -0.0200 843  ARG B CD  
15122 N NE  . ARG B 845  ? 0.3430 0.3575 0.3700 0.0042  -0.0080 -0.0198 843  ARG B NE  
15123 C CZ  . ARG B 845  ? 0.3869 0.3990 0.4112 0.0033  -0.0092 -0.0194 843  ARG B CZ  
15124 N NH1 . ARG B 845  ? 0.3675 0.3788 0.3917 0.0036  -0.0102 -0.0193 843  ARG B NH1 
15125 N NH2 . ARG B 845  ? 0.4571 0.4672 0.4782 0.0018  -0.0095 -0.0191 843  ARG B NH2 
15126 N N   . CYS B 846  ? 0.1665 0.1905 0.2106 0.0090  -0.0054 -0.0199 844  CYS B N   
15127 C CA  . CYS B 846  ? 0.1717 0.1970 0.2180 0.0088  -0.0053 -0.0197 844  CYS B CA  
15128 C C   . CYS B 846  ? 0.1512 0.1754 0.1955 0.0081  -0.0061 -0.0200 844  CYS B C   
15129 O O   . CYS B 846  ? 0.1781 0.2020 0.2235 0.0080  -0.0069 -0.0200 844  CYS B O   
15130 C CB  . CYS B 846  ? 0.1838 0.2106 0.2307 0.0089  -0.0037 -0.0194 844  CYS B CB  
15131 S SG  . CYS B 846  ? 0.1854 0.2121 0.2289 0.0086  -0.0028 -0.0195 844  CYS B SG  
15132 N N   . SER B 847  ? 0.1509 0.1744 0.1921 0.0077  -0.0060 -0.0202 845  SER B N   
15133 C CA  . SER B 847  ? 0.1486 0.1716 0.1875 0.0073  -0.0065 -0.0205 845  SER B CA  
15134 C C   . SER B 847  ? 0.1643 0.1855 0.2019 0.0070  -0.0081 -0.0206 845  SER B C   
15135 O O   . SER B 847  ? 0.1671 0.1877 0.2025 0.0067  -0.0085 -0.0209 845  SER B O   
15136 C CB  . SER B 847  ? 0.1711 0.1948 0.2074 0.0068  -0.0056 -0.0204 845  SER B CB  
15137 O OG  . SER B 847  ? 0.1832 0.2059 0.2185 0.0064  -0.0058 -0.0202 845  SER B OG  
15138 N N   . ALA B 848  ? 0.1559 0.1762 0.1946 0.0072  -0.0090 -0.0205 846  ALA B N   
15139 C CA  . ALA B 848  ? 0.1580 0.1763 0.1949 0.0070  -0.0105 -0.0205 846  ALA B CA  
15140 C C   . ALA B 848  ? 0.1619 0.1797 0.1988 0.0069  -0.0117 -0.0208 846  ALA B C   
15141 O O   . ALA B 848  ? 0.1631 0.1817 0.2025 0.0071  -0.0118 -0.0210 846  ALA B O   
15142 C CB  . ALA B 848  ? 0.1627 0.1804 0.2013 0.0077  -0.0114 -0.0203 846  ALA B CB  
15143 N N   . LEU B 849  ? 0.1656 0.1817 0.1994 0.0065  -0.0128 -0.0209 847  LEU B N   
15144 C CA  . LEU B 849  ? 0.1667 0.1818 0.1997 0.0064  -0.0142 -0.0213 847  LEU B CA  
15145 C C   . LEU B 849  ? 0.1698 0.1845 0.2056 0.0067  -0.0159 -0.0212 847  LEU B C   
15146 O O   . LEU B 849  ? 0.1892 0.2030 0.2249 0.0070  -0.0169 -0.0209 847  LEU B O   
15147 C CB  . LEU B 849  ? 0.1931 0.2066 0.2217 0.0059  -0.0147 -0.0213 847  LEU B CB  
15148 C CG  . LEU B 849  ? 0.1798 0.1918 0.2067 0.0059  -0.0163 -0.0218 847  LEU B CG  
15149 C CD1 . LEU B 849  ? 0.2013 0.2138 0.2286 0.0062  -0.0158 -0.0225 847  LEU B CD1 
15150 C CD2 . LEU B 849  ? 0.1951 0.2057 0.2174 0.0053  -0.0167 -0.0216 847  LEU B CD2 
15151 N N   . ARG B 850  ? 0.1501 0.1653 0.1881 0.0067  -0.0164 -0.0215 848  ARG B N   
15152 C CA  . ARG B 850  ? 0.1650 0.1806 0.2063 0.0067  -0.0181 -0.0214 848  ARG B CA  
15153 C C   . ARG B 850  ? 0.1674 0.1811 0.2069 0.0063  -0.0203 -0.0218 848  ARG B C   
15154 O O   . ARG B 850  ? 0.1760 0.1897 0.2170 0.0063  -0.0222 -0.0217 848  ARG B O   
15155 C CB  . ARG B 850  ? 0.1825 0.2002 0.2280 0.0066  -0.0174 -0.0211 848  ARG B CB  
15156 C CG  . ARG B 850  ? 0.1760 0.1956 0.2231 0.0071  -0.0152 -0.0207 848  ARG B CG  
15157 C CD  . ARG B 850  ? 0.1744 0.1943 0.2217 0.0078  -0.0152 -0.0204 848  ARG B CD  
15158 N NE  . ARG B 850  ? 0.1756 0.1971 0.2243 0.0084  -0.0133 -0.0201 848  ARG B NE  
15159 C CZ  . ARG B 850  ? 0.1793 0.2008 0.2278 0.0092  -0.0129 -0.0200 848  ARG B CZ  
15160 N NH1 . ARG B 850  ? 0.1756 0.1953 0.2226 0.0096  -0.0143 -0.0200 848  ARG B NH1 
15161 N NH2 . ARG B 850  ? 0.1767 0.1995 0.2261 0.0097  -0.0111 -0.0199 848  ARG B NH2 
15162 N N   . VAL B 851  ? 0.1914 0.2037 0.2278 0.0060  -0.0200 -0.0225 849  VAL B N   
15163 C CA  . VAL B 851  ? 0.1809 0.1909 0.2151 0.0057  -0.0220 -0.0232 849  VAL B CA  
15164 C C   . VAL B 851  ? 0.1877 0.1961 0.2166 0.0059  -0.0215 -0.0237 849  VAL B C   
15165 O O   . VAL B 851  ? 0.1840 0.1926 0.2114 0.0062  -0.0199 -0.0241 849  VAL B O   
15166 C CB  . VAL B 851  ? 0.1908 0.2004 0.2268 0.0052  -0.0226 -0.0236 849  VAL B CB  
15167 C CG1 . VAL B 851  ? 0.2339 0.2408 0.2673 0.0048  -0.0250 -0.0244 849  VAL B CG1 
15168 C CG2 . VAL B 851  ? 0.2299 0.2419 0.2715 0.0048  -0.0227 -0.0229 849  VAL B CG2 
15169 N N   . LEU B 852  ? 0.1946 0.2016 0.2206 0.0058  -0.0229 -0.0236 850  LEU B N   
15170 C CA  . LEU B 852  ? 0.1802 0.1858 0.2009 0.0059  -0.0225 -0.0240 850  LEU B CA  
15171 C C   . LEU B 852  ? 0.1957 0.1990 0.2139 0.0059  -0.0243 -0.0250 850  LEU B C   
15172 O O   . LEU B 852  ? 0.1888 0.1908 0.2074 0.0055  -0.0267 -0.0250 850  LEU B O   
15173 C CB  . LEU B 852  ? 0.1796 0.1846 0.1982 0.0056  -0.0230 -0.0231 850  LEU B CB  
15174 C CG  . LEU B 852  ? 0.1845 0.1883 0.1974 0.0054  -0.0227 -0.0232 850  LEU B CG  
15175 C CD1 . LEU B 852  ? 0.2031 0.2087 0.2147 0.0055  -0.0200 -0.0234 850  LEU B CD1 
15176 C CD2 . LEU B 852  ? 0.2055 0.2082 0.2163 0.0048  -0.0234 -0.0222 850  LEU B CD2 
15177 N N   . CYS B 853  ? 0.1952 0.1978 0.2105 0.0064  -0.0232 -0.0259 851  CYS B N   
15178 C CA  . CYS B 853  ? 0.2027 0.2025 0.2151 0.0066  -0.0248 -0.0271 851  CYS B CA  
15179 C C   . CYS B 853  ? 0.1872 0.1860 0.1937 0.0071  -0.0244 -0.0275 851  CYS B C   
15180 O O   . CYS B 853  ? 0.2077 0.2080 0.2123 0.0078  -0.0221 -0.0276 851  CYS B O   
15181 C CB  . CYS B 853  ? 0.2057 0.2049 0.2189 0.0072  -0.0240 -0.0280 851  CYS B CB  
15182 S SG  . CYS B 853  ? 0.2332 0.2340 0.2532 0.0065  -0.0239 -0.0272 851  CYS B SG  
15183 N N   . LEU B 854  ? 0.2189 0.2157 0.2226 0.0067  -0.0265 -0.0276 852  LEU B N   
15184 C CA  . LEU B 854  ? 0.2180 0.2139 0.2159 0.0070  -0.0262 -0.0277 852  LEU B CA  
15185 C C   . LEU B 854  ? 0.2165 0.2093 0.2100 0.0076  -0.0276 -0.0292 852  LEU B C   
15186 O O   . LEU B 854  ? 0.2344 0.2248 0.2285 0.0071  -0.0303 -0.0297 852  LEU B O   
15187 C CB  . LEU B 854  ? 0.2180 0.2135 0.2152 0.0061  -0.0276 -0.0265 852  LEU B CB  
15188 C CG  . LEU B 854  ? 0.2118 0.2096 0.2128 0.0056  -0.0265 -0.0251 852  LEU B CG  
15189 C CD1 . LEU B 854  ? 0.2174 0.2137 0.2172 0.0050  -0.0285 -0.0240 852  LEU B CD1 
15190 C CD2 . LEU B 854  ? 0.2203 0.2203 0.2198 0.0056  -0.0236 -0.0247 852  LEU B CD2 
15191 N N   . GLN B 855  ? 0.2162 0.2091 0.2053 0.0086  -0.0259 -0.0300 853  GLN B N   
15192 C CA  . GLN B 855  ? 0.2270 0.2165 0.2108 0.0095  -0.0272 -0.0316 853  GLN B CA  
15193 C C   . GLN B 855  ? 0.2537 0.2411 0.2346 0.0086  -0.0298 -0.0312 853  GLN B C   
15194 O O   . GLN B 855  ? 0.2530 0.2418 0.2334 0.0078  -0.0295 -0.0298 853  GLN B O   
15195 C CB  . GLN B 855  ? 0.2353 0.2260 0.2145 0.0110  -0.0247 -0.0323 853  GLN B CB  
15196 C CG  . GLN B 855  ? 0.2799 0.2669 0.2538 0.0124  -0.0257 -0.0343 853  GLN B CG  
15197 C CD  . GLN B 855  ? 0.3148 0.3034 0.2841 0.0143  -0.0230 -0.0351 853  GLN B CD  
15198 O OE1 . GLN B 855  ? 0.3566 0.3489 0.3281 0.0150  -0.0203 -0.0346 853  GLN B OE1 
15199 N NE2 . GLN B 855  ? 0.3462 0.3323 0.3091 0.0152  -0.0237 -0.0363 853  GLN B NE2 
15200 N N   . GLU B 856  ? 0.2563 0.2401 0.2353 0.0086  -0.0325 -0.0325 854  GLU B N   
15201 C CA  . GLU B 856  ? 0.2690 0.2508 0.2467 0.0076  -0.0356 -0.0320 854  GLU B CA  
15202 C C   . GLU B 856  ? 0.2772 0.2589 0.2492 0.0077  -0.0351 -0.0314 854  GLU B C   
15203 O O   . GLU B 856  ? 0.3140 0.2956 0.2860 0.0068  -0.0367 -0.0301 854  GLU B O   
15204 C CB  . GLU B 856  ? 0.3264 0.3042 0.3022 0.0075  -0.0386 -0.0337 854  GLU B CB  
15205 N N   . ASP B 857  ? 0.2986 0.2805 0.2655 0.0088  -0.0329 -0.0322 855  ASP B N   
15206 C CA  . ASP B 857  ? 0.3211 0.3028 0.2818 0.0089  -0.0324 -0.0317 855  ASP B CA  
15207 C C   . ASP B 857  ? 0.3075 0.2924 0.2697 0.0078  -0.0306 -0.0295 855  ASP B C   
15208 O O   . ASP B 857  ? 0.3476 0.3319 0.3054 0.0072  -0.0308 -0.0285 855  ASP B O   
15209 C CB  . ASP B 857  ? 0.3997 0.3813 0.3549 0.0106  -0.0302 -0.0332 855  ASP B CB  
15210 N N   . VAL B 858  ? 0.2462 0.2341 0.2142 0.0075  -0.0288 -0.0287 856  VAL B N   
15211 C CA  . VAL B 858  ? 0.2633 0.2537 0.2327 0.0064  -0.0273 -0.0267 856  VAL B CA  
15212 C C   . VAL B 858  ? 0.2351 0.2253 0.2099 0.0055  -0.0289 -0.0256 856  VAL B C   
15213 O O   . VAL B 858  ? 0.2574 0.2488 0.2334 0.0045  -0.0281 -0.0240 856  VAL B O   
15214 C CB  . VAL B 858  ? 0.2686 0.2629 0.2392 0.0067  -0.0237 -0.0265 856  VAL B CB  
15215 C CG1 . VAL B 858  ? 0.3238 0.3192 0.2886 0.0076  -0.0219 -0.0272 856  VAL B CG1 
15216 C CG2 . VAL B 858  ? 0.2766 0.2721 0.2525 0.0075  -0.0231 -0.0275 856  VAL B CG2 
15217 N N   . ALA B 859  ? 0.2422 0.2310 0.2205 0.0057  -0.0312 -0.0264 857  ALA B N   
15218 C CA  . ALA B 859  ? 0.2661 0.2556 0.2504 0.0052  -0.0323 -0.0255 857  ALA B CA  
15219 C C   . ALA B 859  ? 0.2495 0.2379 0.2326 0.0045  -0.0338 -0.0239 857  ALA B C   
15220 O O   . ALA B 859  ? 0.2501 0.2398 0.2362 0.0042  -0.0331 -0.0227 857  ALA B O   
15221 C CB  . ALA B 859  ? 0.2578 0.2463 0.2455 0.0054  -0.0346 -0.0265 857  ALA B CB  
15222 N N   . ASP B 860  ? 0.2790 0.2647 0.2575 0.0045  -0.0361 -0.0239 858  ASP B N   
15223 C CA  . ASP B 860  ? 0.2802 0.2643 0.2574 0.0040  -0.0380 -0.0224 858  ASP B CA  
15224 C C   . ASP B 860  ? 0.2588 0.2434 0.2335 0.0032  -0.0358 -0.0209 858  ASP B C   
15225 O O   . ASP B 860  ? 0.2613 0.2455 0.2378 0.0029  -0.0363 -0.0195 858  ASP B O   
15226 C CB  . ASP B 860  ? 0.2577 0.2387 0.2297 0.0040  -0.0409 -0.0227 858  ASP B CB  
15227 C CG  . ASP B 860  ? 0.3571 0.3375 0.3322 0.0044  -0.0438 -0.0239 858  ASP B CG  
15228 O OD1 . ASP B 860  ? 0.3804 0.3626 0.3620 0.0045  -0.0442 -0.0238 858  ASP B OD1 
15229 O OD2 . ASP B 860  ? 0.4282 0.4062 0.3988 0.0045  -0.0457 -0.0248 858  ASP B OD2 
15230 N N   . ARG B 861  ? 0.2602 0.2456 0.2306 0.0029  -0.0334 -0.0211 859  ARG B N   
15231 C CA  . ARG B 861  ? 0.2833 0.2694 0.2512 0.0018  -0.0314 -0.0195 859  ARG B CA  
15232 C C   . ARG B 861  ? 0.2567 0.2454 0.2301 0.0015  -0.0295 -0.0190 859  ARG B C   
15233 O O   . ARG B 861  ? 0.2614 0.2494 0.2347 0.0005  -0.0293 -0.0174 859  ARG B O   
15234 C CB  . ARG B 861  ? 0.3439 0.3314 0.3066 0.0016  -0.0291 -0.0198 859  ARG B CB  
15235 C CG  . ARG B 861  ? 0.4519 0.4413 0.4130 0.0000  -0.0266 -0.0181 859  ARG B CG  
15236 C CD  . ARG B 861  ? 0.5272 0.5172 0.4817 -0.0006 -0.0252 -0.0176 859  ARG B CD  
15237 N NE  . ARG B 861  ? 0.5934 0.5856 0.5470 -0.0025 -0.0229 -0.0158 859  ARG B NE  
15238 C CZ  . ARG B 861  ? 0.5520 0.5486 0.5081 -0.0027 -0.0200 -0.0159 859  ARG B CZ  
15239 N NH1 . ARG B 861  ? 0.5228 0.5219 0.4821 -0.0010 -0.0189 -0.0178 859  ARG B NH1 
15240 N NH2 . ARG B 861  ? 0.5706 0.5689 0.5258 -0.0048 -0.0184 -0.0141 859  ARG B NH2 
15241 N N   . ILE B 862  ? 0.2174 0.2085 0.1950 0.0023  -0.0282 -0.0203 860  ILE B N   
15242 C CA  . ILE B 862  ? 0.2345 0.2279 0.2171 0.0021  -0.0266 -0.0198 860  ILE B CA  
15243 C C   . ILE B 862  ? 0.2115 0.2035 0.1980 0.0022  -0.0285 -0.0192 860  ILE B C   
15244 O O   . ILE B 862  ? 0.2407 0.2328 0.2285 0.0016  -0.0277 -0.0181 860  ILE B O   
15245 C CB  . ILE B 862  ? 0.2326 0.2289 0.2187 0.0030  -0.0248 -0.0212 860  ILE B CB  
15246 C CG1 . ILE B 862  ? 0.2573 0.2557 0.2397 0.0029  -0.0224 -0.0216 860  ILE B CG1 
15247 C CG2 . ILE B 862  ? 0.2307 0.2288 0.2223 0.0029  -0.0237 -0.0209 860  ILE B CG2 
15248 C CD1 . ILE B 862  ? 0.2941 0.2943 0.2785 0.0043  -0.0211 -0.0232 860  ILE B CD1 
15249 N N   . LEU B 863  ? 0.2258 0.2165 0.2141 0.0031  -0.0310 -0.0198 861  LEU B N   
15250 C CA  . LEU B 863  ? 0.2421 0.2322 0.2344 0.0036  -0.0328 -0.0192 861  LEU B CA  
15251 C C   . LEU B 863  ? 0.2516 0.2388 0.2406 0.0031  -0.0341 -0.0177 861  LEU B C   
15252 O O   . LEU B 863  ? 0.2403 0.2270 0.2317 0.0034  -0.0343 -0.0169 861  LEU B O   
15253 C CB  . LEU B 863  ? 0.2419 0.2319 0.2370 0.0044  -0.0353 -0.0201 861  LEU B CB  
15254 C CG  . LEU B 863  ? 0.2679 0.2602 0.2671 0.0047  -0.0343 -0.0214 861  LEU B CG  
15255 C CD1 . LEU B 863  ? 0.3153 0.3070 0.3159 0.0049  -0.0370 -0.0223 861  LEU B CD1 
15256 C CD2 . LEU B 863  ? 0.2947 0.2895 0.2997 0.0050  -0.0328 -0.0211 861  LEU B CD2 
15257 N N   . THR B 864  ? 0.2404 0.2253 0.2234 0.0026  -0.0350 -0.0172 862  THR B N   
15258 C CA  . THR B 864  ? 0.2593 0.2410 0.2385 0.0020  -0.0362 -0.0156 862  THR B CA  
15259 C C   . THR B 864  ? 0.2608 0.2427 0.2394 0.0008  -0.0339 -0.0145 862  THR B C   
15260 O O   . THR B 864  ? 0.2649 0.2444 0.2436 0.0008  -0.0347 -0.0134 862  THR B O   
15261 C CB  . THR B 864  ? 0.3147 0.2941 0.2871 0.0014  -0.0372 -0.0152 862  THR B CB  
15262 O OG1 . THR B 864  ? 0.3299 0.3084 0.3027 0.0024  -0.0400 -0.0161 862  THR B OG1 
15263 C CG2 . THR B 864  ? 0.3630 0.3387 0.3306 0.0004  -0.0381 -0.0132 862  THR B CG2 
15264 N N   . MET B 865  ? 0.2429 0.2276 0.2209 -0.0001 -0.0310 -0.0149 863  MET B N   
15265 C CA  . MET B 865  ? 0.2338 0.2191 0.2112 -0.0016 -0.0289 -0.0139 863  MET B CA  
15266 C C   . MET B 865  ? 0.2289 0.2152 0.2118 -0.0009 -0.0284 -0.0141 863  MET B C   
15267 O O   . MET B 865  ? 0.2354 0.2198 0.2178 -0.0017 -0.0283 -0.0131 863  MET B O   
15268 C CB  . MET B 865  ? 0.2440 0.2330 0.2199 -0.0024 -0.0261 -0.0143 863  MET B CB  
15269 C CG  . MET B 865  ? 0.2700 0.2602 0.2451 -0.0043 -0.0240 -0.0131 863  MET B CG  
15270 S SD  . MET B 865  ? 0.2814 0.2769 0.2554 -0.0050 -0.0207 -0.0136 863  MET B SD  
15271 C CE  . MET B 865  ? 0.3290 0.3231 0.2962 -0.0053 -0.0214 -0.0132 863  MET B CE  
15272 N N   . LEU B 866  ? 0.2388 0.2277 0.2267 0.0004  -0.0281 -0.0156 864  LEU B N   
15273 C CA  . LEU B 866  ? 0.2226 0.2128 0.2159 0.0012  -0.0276 -0.0159 864  LEU B CA  
15274 C C   . LEU B 866  ? 0.2285 0.2155 0.2224 0.0021  -0.0298 -0.0152 864  LEU B C   
15275 O O   . LEU B 866  ? 0.2263 0.2124 0.2213 0.0020  -0.0292 -0.0147 864  LEU B O   
15276 C CB  . LEU B 866  ? 0.2304 0.2235 0.2284 0.0025  -0.0273 -0.0173 864  LEU B CB  
15277 C CG  . LEU B 866  ? 0.2205 0.2151 0.2242 0.0034  -0.0269 -0.0177 864  LEU B CG  
15278 C CD1 . LEU B 866  ? 0.2381 0.2339 0.2422 0.0026  -0.0246 -0.0173 864  LEU B CD1 
15279 C CD2 . LEU B 866  ? 0.2570 0.2542 0.2647 0.0043  -0.0269 -0.0189 864  LEU B CD2 
15280 N N   . LYS B 867  ? 0.2317 0.2169 0.2249 0.0030  -0.0323 -0.0151 865  LYS B N   
15281 C CA  . LYS B 867  ? 0.2421 0.2247 0.2361 0.0042  -0.0346 -0.0145 865  LYS B CA  
15282 C C   . LYS B 867  ? 0.2400 0.2183 0.2290 0.0032  -0.0349 -0.0130 865  LYS B C   
15283 O O   . LYS B 867  ? 0.2406 0.2168 0.2306 0.0040  -0.0354 -0.0125 865  LYS B O   
15284 C CB  . LYS B 867  ? 0.2424 0.2244 0.2368 0.0054  -0.0374 -0.0147 865  LYS B CB  
15285 C CG  . LYS B 867  ? 0.2755 0.2615 0.2756 0.0062  -0.0374 -0.0161 865  LYS B CG  
15286 C CD  . LYS B 867  ? 0.3318 0.3175 0.3316 0.0068  -0.0402 -0.0165 865  LYS B CD  
15287 C CE  . LYS B 867  ? 0.3770 0.3664 0.3820 0.0070  -0.0399 -0.0177 865  LYS B CE  
15288 N NZ  . LYS B 867  ? 0.4671 0.4562 0.4718 0.0072  -0.0428 -0.0182 865  LYS B NZ  
15289 N N   . GLY B 868  ? 0.2518 0.2287 0.2353 0.0014  -0.0344 -0.0122 866  GLY B N   
15290 C CA  . GLY B 868  ? 0.2569 0.2297 0.2354 -0.0001 -0.0346 -0.0106 866  GLY B CA  
15291 C C   . GLY B 868  ? 0.2408 0.2142 0.2207 -0.0011 -0.0325 -0.0104 866  GLY B C   
15292 O O   . GLY B 868  ? 0.2572 0.2266 0.2353 -0.0014 -0.0332 -0.0095 866  GLY B O   
15293 N N   . ALA B 869  ? 0.2485 0.2265 0.2313 -0.0016 -0.0300 -0.0114 867  ALA B N   
15294 C CA  . ALA B 869  ? 0.2541 0.2331 0.2385 -0.0025 -0.0281 -0.0114 867  ALA B CA  
15295 C C   . ALA B 869  ? 0.2286 0.2068 0.2172 -0.0005 -0.0288 -0.0120 867  ALA B C   
15296 O O   . ALA B 869  ? 0.2410 0.2168 0.2289 -0.0010 -0.0285 -0.0116 867  ALA B O   
15297 C CB  . ALA B 869  ? 0.2618 0.2462 0.2485 -0.0032 -0.0255 -0.0123 867  ALA B CB  
15298 N N   . LEU B 870  ? 0.2259 0.2058 0.2187 0.0017  -0.0297 -0.0130 868  LEU B N   
15299 C CA  . LEU B 870  ? 0.2441 0.2240 0.2412 0.0038  -0.0302 -0.0136 868  LEU B CA  
15300 C C   . LEU B 870  ? 0.2386 0.2132 0.2330 0.0047  -0.0323 -0.0127 868  LEU B C   
15301 O O   . LEU B 870  ? 0.2498 0.2230 0.2456 0.0059  -0.0322 -0.0129 868  LEU B O   
15302 C CB  . LEU B 870  ? 0.2376 0.2209 0.2398 0.0057  -0.0309 -0.0146 868  LEU B CB  
15303 C CG  . LEU B 870  ? 0.2616 0.2497 0.2673 0.0053  -0.0288 -0.0157 868  LEU B CG  
15304 C CD1 . LEU B 870  ? 0.2710 0.2619 0.2811 0.0067  -0.0298 -0.0165 868  LEU B CD1 
15305 C CD2 . LEU B 870  ? 0.2802 0.2698 0.2884 0.0054  -0.0267 -0.0160 868  LEU B CD2 
15306 N N   . HIS B 871  ? 0.2261 0.1973 0.2161 0.0043  -0.0343 -0.0117 869  HIS B N   
15307 C CA  A HIS B 871  ? 0.2688 0.2343 0.2557 0.0053  -0.0365 -0.0107 869  HIS B CA  
15308 C CA  B HIS B 871  ? 0.2689 0.2343 0.2556 0.0052  -0.0365 -0.0107 869  HIS B CA  
15309 C C   . HIS B 871  ? 0.2700 0.2313 0.2529 0.0036  -0.0357 -0.0099 869  HIS B C   
15310 O O   . HIS B 871  ? 0.3006 0.2567 0.2813 0.0047  -0.0374 -0.0093 869  HIS B O   
15311 C CB  A HIS B 871  ? 0.2799 0.2426 0.2626 0.0052  -0.0389 -0.0097 869  HIS B CB  
15312 C CB  B HIS B 871  ? 0.2766 0.2394 0.2587 0.0047  -0.0386 -0.0096 869  HIS B CB  
15313 C CG  A HIS B 871  ? 0.2947 0.2593 0.2810 0.0077  -0.0409 -0.0104 869  HIS B CG  
15314 C CG  B HIS B 871  ? 0.2896 0.2460 0.2678 0.0058  -0.0412 -0.0084 869  HIS B CG  
15315 N ND1 A HIS B 871  ? 0.3077 0.2764 0.2961 0.0075  -0.0409 -0.0111 869  HIS B ND1 
15316 N ND1 B HIS B 871  ? 0.3471 0.3028 0.3281 0.0090  -0.0434 -0.0088 869  HIS B ND1 
15317 C CD2 A HIS B 871  ? 0.3250 0.2882 0.3134 0.0105  -0.0431 -0.0104 869  HIS B CD2 
15318 C CD2 B HIS B 871  ? 0.3529 0.3034 0.3248 0.0041  -0.0421 -0.0069 869  HIS B CD2 
15319 C CE1 A HIS B 871  ? 0.3293 0.2990 0.3208 0.0097  -0.0431 -0.0115 869  HIS B CE1 
15320 C CE1 B HIS B 871  ? 0.3215 0.2708 0.2979 0.0096  -0.0456 -0.0075 869  HIS B CE1 
15321 N NE2 A HIS B 871  ? 0.3166 0.2834 0.3084 0.0116  -0.0445 -0.0110 869  HIS B NE2 
15322 N NE2 B HIS B 871  ? 0.3598 0.3055 0.3304 0.0065  -0.0448 -0.0063 869  HIS B NE2 
15323 N N   . GLU B 872  ? 0.2478 0.2112 0.2298 0.0010  -0.0334 -0.0098 870  GLU B N   
15324 C CA  . GLU B 872  ? 0.2361 0.1960 0.2145 -0.0012 -0.0327 -0.0090 870  GLU B CA  
15325 C C   . GLU B 872  ? 0.2417 0.2030 0.2237 -0.0004 -0.0313 -0.0101 870  GLU B C   
15326 O O   . GLU B 872  ? 0.2729 0.2313 0.2521 -0.0023 -0.0308 -0.0095 870  GLU B O   
15327 C CB  . GLU B 872  ? 0.2530 0.2148 0.2283 -0.0047 -0.0312 -0.0080 870  GLU B CB  
15328 C CG  . GLU B 872  ? 0.2742 0.2344 0.2452 -0.0055 -0.0324 -0.0069 870  GLU B CG  
15329 C CD  . GLU B 872  ? 0.2843 0.2371 0.2499 -0.0057 -0.0349 -0.0054 870  GLU B CD  
15330 O OE1 . GLU B 872  ? 0.3215 0.2700 0.2853 -0.0064 -0.0353 -0.0049 870  GLU B OE1 
15331 O OE2 . GLU B 872  ? 0.3063 0.2572 0.2693 -0.0051 -0.0367 -0.0047 870  GLU B OE2 
15332 N N   . LEU B 873  ? 0.2457 0.2112 0.2335 0.0020  -0.0307 -0.0115 871  LEU B N   
15333 C CA  . LEU B 873  ? 0.2553 0.2224 0.2462 0.0028  -0.0292 -0.0125 871  LEU B CA  
15334 C C   . LEU B 873  ? 0.2568 0.2190 0.2471 0.0052  -0.0306 -0.0127 871  LEU B C   
15335 O O   . LEU B 873  ? 0.2689 0.2291 0.2593 0.0075  -0.0326 -0.0126 871  LEU B O   
15336 C CB  . LEU B 873  ? 0.2392 0.2126 0.2363 0.0043  -0.0278 -0.0138 871  LEU B CB  
15337 C CG  . LEU B 873  ? 0.2737 0.2519 0.2717 0.0024  -0.0261 -0.0139 871  LEU B CG  
15338 C CD1 . LEU B 873  ? 0.2779 0.2614 0.2818 0.0040  -0.0248 -0.0151 871  LEU B CD1 
15339 C CD2 . LEU B 873  ? 0.2717 0.2500 0.2668 -0.0005 -0.0246 -0.0133 871  LEU B CD2 
15340 N N   . HIS B 874  ? 0.2600 0.2205 0.2497 0.0048  -0.0297 -0.0131 872  HIS B N   
15341 C CA  . HIS B 874  ? 0.2715 0.2276 0.2605 0.0073  -0.0307 -0.0136 872  HIS B CA  
15342 C C   . HIS B 874  ? 0.2436 0.2048 0.2386 0.0097  -0.0291 -0.0152 872  HIS B C   
15343 O O   . HIS B 874  ? 0.2338 0.1982 0.2303 0.0083  -0.0270 -0.0157 872  HIS B O   
15344 C CB  . HIS B 874  ? 0.2816 0.2318 0.2652 0.0051  -0.0309 -0.0131 872  HIS B CB  
15345 C CG  . HIS B 874  ? 0.2755 0.2200 0.2573 0.0076  -0.0320 -0.0137 872  HIS B CG  
15346 N ND1 . HIS B 874  ? 0.3704 0.3082 0.3468 0.0059  -0.0327 -0.0134 872  HIS B ND1 
15347 C CD2 . HIS B 874  ? 0.2988 0.2432 0.2834 0.0118  -0.0326 -0.0148 872  HIS B CD2 
15348 C CE1 . HIS B 874  ? 0.3562 0.2895 0.3317 0.0092  -0.0337 -0.0143 872  HIS B CE1 
15349 N NE2 . HIS B 874  ? 0.3637 0.3013 0.3444 0.0129  -0.0336 -0.0151 872  HIS B NE2 
15350 N N   . ILE B 875  ? 0.2352 0.1973 0.2334 0.0132  -0.0300 -0.0157 873  ILE B N   
15351 C CA  . ILE B 875  ? 0.2541 0.2209 0.2579 0.0157  -0.0285 -0.0170 873  ILE B CA  
15352 C C   . ILE B 875  ? 0.2545 0.2166 0.2564 0.0183  -0.0290 -0.0176 873  ILE B C   
15353 O O   . ILE B 875  ? 0.2651 0.2223 0.2644 0.0202  -0.0312 -0.0173 873  ILE B O   
15354 C CB  . ILE B 875  ? 0.2808 0.2524 0.2898 0.0179  -0.0292 -0.0171 873  ILE B CB  
15355 C CG1 . ILE B 875  ? 0.3134 0.2886 0.3233 0.0156  -0.0291 -0.0166 873  ILE B CG1 
15356 C CG2 . ILE B 875  ? 0.2720 0.2487 0.2866 0.0202  -0.0275 -0.0182 873  ILE B CG2 
15357 C CD1 . ILE B 875  ? 0.3534 0.3311 0.3666 0.0172  -0.0307 -0.0165 873  ILE B CD1 
15358 N N   . GLY B 876  ? 0.2240 0.1874 0.2271 0.0186  -0.0272 -0.0186 874  GLY B N   
15359 C CA  . GLY B 876  ? 0.2549 0.2138 0.2560 0.0214  -0.0276 -0.0194 874  GLY B CA  
15360 C C   . GLY B 876  ? 0.2286 0.1888 0.2301 0.0210  -0.0254 -0.0205 874  GLY B C   
15361 O O   . GLY B 876  ? 0.2304 0.1958 0.2346 0.0190  -0.0235 -0.0205 874  GLY B O   
15362 N N   . ARG B 877  ? 0.2578 0.2129 0.2562 0.0232  -0.0258 -0.0213 875  ARG B N   
15363 C CA  . ARG B 877  ? 0.2298 0.1849 0.2275 0.0230  -0.0241 -0.0224 875  ARG B CA  
15364 C C   . ARG B 877  ? 0.2665 0.2198 0.2606 0.0184  -0.0238 -0.0218 875  ARG B C   
15365 O O   . ARG B 877  ? 0.2754 0.2233 0.2647 0.0161  -0.0255 -0.0209 875  ARG B O   
15366 C CB  . ARG B 877  ? 0.2812 0.2297 0.2751 0.0263  -0.0250 -0.0235 875  ARG B CB  
15367 C CG  . ARG B 877  ? 0.2994 0.2493 0.2937 0.0275  -0.0230 -0.0249 875  ARG B CG  
15368 C CD  . ARG B 877  ? 0.3806 0.3239 0.3710 0.0313  -0.0239 -0.0261 875  ARG B CD  
15369 N NE  . ARG B 877  ? 0.3503 0.2841 0.3330 0.0292  -0.0256 -0.0262 875  ARG B NE  
15370 C CZ  . ARG B 877  ? 0.4097 0.3362 0.3875 0.0319  -0.0266 -0.0273 875  ARG B CZ  
15371 N NH1 . ARG B 877  ? 0.3928 0.3204 0.3726 0.0371  -0.0261 -0.0286 875  ARG B NH1 
15372 N NH2 . ARG B 877  ? 0.4572 0.3750 0.4278 0.0294  -0.0282 -0.0273 875  ARG B NH2 
15373 N N   . THR B 878  ? 0.2276 0.1857 0.2240 0.0170  -0.0217 -0.0223 876  THR B N   
15374 C CA  . THR B 878  ? 0.2469 0.2064 0.2420 0.0127  -0.0212 -0.0215 876  THR B CA  
15375 C C   . THR B 878  ? 0.2234 0.1769 0.2126 0.0104  -0.0218 -0.0217 876  THR B C   
15376 O O   . THR B 878  ? 0.2518 0.2070 0.2402 0.0067  -0.0212 -0.0211 876  THR B O   
15377 C CB  . THR B 878  ? 0.2443 0.2118 0.2446 0.0122  -0.0188 -0.0218 876  THR B CB  
15378 O OG1 . THR B 878  ? 0.2682 0.2369 0.2700 0.0148  -0.0175 -0.0230 876  THR B OG1 
15379 C CG2 . THR B 878  ? 0.2690 0.2418 0.2742 0.0131  -0.0186 -0.0213 876  THR B CG2 
15380 N N   . ASP B 879  ? 0.2382 0.1849 0.2234 0.0123  -0.0230 -0.0225 877  ASP B N   
15381 C CA  . ASP B 879  ? 0.2486 0.1888 0.2278 0.0100  -0.0239 -0.0227 877  ASP B CA  
15382 C C   . ASP B 879  ? 0.2555 0.1892 0.2294 0.0070  -0.0261 -0.0213 877  ASP B C   
15383 O O   . ASP B 879  ? 0.2892 0.2149 0.2572 0.0060  -0.0277 -0.0215 877  ASP B O   
15384 C CB  . ASP B 879  ? 0.2990 0.2342 0.2756 0.0135  -0.0241 -0.0244 877  ASP B CB  
15385 C CG  . ASP B 879  ? 0.3110 0.2410 0.2860 0.0173  -0.0257 -0.0246 877  ASP B CG  
15386 O OD1 . ASP B 879  ? 0.3331 0.2661 0.3115 0.0186  -0.0261 -0.0238 877  ASP B OD1 
15387 O OD2 . ASP B 879  ? 0.3380 0.2605 0.3081 0.0192  -0.0268 -0.0257 877  ASP B OD2 
15388 N N   . ARG B 880  ? 0.2769 0.2136 0.2526 0.0056  -0.0263 -0.0199 878  ARG B N   
15389 C CA  . ARG B 880  ? 0.2773 0.2092 0.2483 0.0021  -0.0281 -0.0182 878  ARG B CA  
15390 C C   . ARG B 880  ? 0.2646 0.2037 0.2386 -0.0013 -0.0267 -0.0171 878  ARG B C   
15391 O O   . ARG B 880  ? 0.2579 0.2040 0.2372 0.0002  -0.0254 -0.0172 878  ARG B O   
15392 C CB  . ARG B 880  ? 0.3038 0.2317 0.2735 0.0043  -0.0300 -0.0175 878  ARG B CB  
15393 C CG  . ARG B 880  ? 0.3776 0.2972 0.3434 0.0078  -0.0318 -0.0184 878  ARG B CG  
15394 C CD  . ARG B 880  ? 0.4361 0.3523 0.4008 0.0099  -0.0338 -0.0175 878  ARG B CD  
15395 N NE  . ARG B 880  ? 0.6225 0.5312 0.5840 0.0139  -0.0354 -0.0185 878  ARG B NE  
15396 C CZ  . ARG B 880  ? 0.6548 0.5534 0.6092 0.0133  -0.0378 -0.0179 878  ARG B CZ  
15397 N NH1 . ARG B 880  ? 0.6861 0.5807 0.6358 0.0085  -0.0389 -0.0161 878  ARG B NH1 
15398 N NH2 . ARG B 880  ? 0.6705 0.5627 0.6223 0.0177  -0.0392 -0.0190 878  ARG B NH2 
15399 N N   . LEU B 881  ? 0.2617 0.1993 0.2322 -0.0058 -0.0271 -0.0160 879  LEU B N   
15400 C CA  . LEU B 881  ? 0.2697 0.2141 0.2425 -0.0089 -0.0258 -0.0148 879  LEU B CA  
15401 C C   . LEU B 881  ? 0.2312 0.1777 0.2054 -0.0082 -0.0260 -0.0138 879  LEU B C   
15402 O O   . LEU B 881  ? 0.2413 0.1950 0.2194 -0.0087 -0.0245 -0.0136 879  LEU B O   
15403 C CB  . LEU B 881  ? 0.2631 0.2047 0.2313 -0.0139 -0.0265 -0.0135 879  LEU B CB  
15404 C CG  . LEU B 881  ? 0.2840 0.2329 0.2542 -0.0174 -0.0250 -0.0123 879  LEU B CG  
15405 C CD1 . LEU B 881  ? 0.3061 0.2629 0.2816 -0.0167 -0.0228 -0.0134 879  LEU B CD1 
15406 C CD2 . LEU B 881  ? 0.2834 0.2289 0.2488 -0.0224 -0.0261 -0.0107 879  LEU B CD2 
15407 N N   . SER B 882  ? 0.2347 0.1749 0.2058 -0.0068 -0.0280 -0.0134 880  SER B N   
15408 C CA  . SER B 882  ? 0.2405 0.1822 0.2123 -0.0062 -0.0286 -0.0124 880  SER B CA  
15409 C C   . SER B 882  ? 0.2663 0.2136 0.2441 -0.0024 -0.0277 -0.0135 880  SER B C   
15410 O O   . SER B 882  ? 0.2755 0.2245 0.2543 -0.0019 -0.0282 -0.0128 880  SER B O   
15411 C CB  . SER B 882  ? 0.2842 0.2170 0.2505 -0.0057 -0.0313 -0.0115 880  SER B CB  
15412 O OG  . SER B 882  ? 0.3449 0.2742 0.3119 -0.0013 -0.0322 -0.0128 880  SER B OG  
15413 N N   . VAL B 883  ? 0.2462 0.1964 0.2279 0.0001  -0.0265 -0.0150 881  VAL B N   
15414 C CA  . VAL B 883  ? 0.2695 0.2250 0.2569 0.0034  -0.0258 -0.0159 881  VAL B CA  
15415 C C   . VAL B 883  ? 0.2429 0.2063 0.2346 0.0021  -0.0238 -0.0159 881  VAL B C   
15416 O O   . VAL B 883  ? 0.2663 0.2325 0.2586 0.0003  -0.0222 -0.0162 881  VAL B O   
15417 C CB  . VAL B 883  ? 0.2723 0.2274 0.2619 0.0070  -0.0254 -0.0174 881  VAL B CB  
15418 C CG1 . VAL B 883  ? 0.2735 0.2356 0.2697 0.0096  -0.0241 -0.0181 881  VAL B CG1 
15419 C CG2 . VAL B 883  ? 0.2792 0.2267 0.2650 0.0093  -0.0276 -0.0174 881  VAL B CG2 
15420 N N   . ASP B 884  ? 0.2411 0.2079 0.2353 0.0028  -0.0239 -0.0156 882  ASP B N   
15421 C CA  . ASP B 884  ? 0.2528 0.2262 0.2505 0.0019  -0.0223 -0.0157 882  ASP B CA  
15422 C C   . ASP B 884  ? 0.2690 0.2474 0.2725 0.0045  -0.0211 -0.0168 882  ASP B C   
15423 O O   . ASP B 884  ? 0.3160 0.2992 0.3222 0.0038  -0.0193 -0.0173 882  ASP B O   
15424 C CB  . ASP B 884  ? 0.2612 0.2350 0.2578 0.0010  -0.0232 -0.0148 882  ASP B CB  
15425 C CG  . ASP B 884  ? 0.2696 0.2389 0.2603 -0.0018 -0.0242 -0.0134 882  ASP B CG  
15426 O OD1 . ASP B 884  ? 0.2668 0.2369 0.2558 -0.0046 -0.0231 -0.0130 882  ASP B OD1 
15427 O OD2 . ASP B 884  ? 0.2600 0.2249 0.2477 -0.0014 -0.0262 -0.0126 882  ASP B OD2 
15428 N N   . VAL B 885  ? 0.2381 0.2156 0.2436 0.0074  -0.0222 -0.0173 883  VAL B N   
15429 C CA  . VAL B 885  ? 0.2335 0.2160 0.2448 0.0098  -0.0213 -0.0181 883  VAL B CA  
15430 C C   . VAL B 885  ? 0.2319 0.2126 0.2440 0.0126  -0.0214 -0.0188 883  VAL B C   
15431 O O   . VAL B 885  ? 0.2304 0.2066 0.2403 0.0142  -0.0231 -0.0187 883  VAL B O   
15432 C CB  . VAL B 885  ? 0.2402 0.2246 0.2537 0.0107  -0.0225 -0.0178 883  VAL B CB  
15433 C CG1 . VAL B 885  ? 0.2599 0.2495 0.2795 0.0127  -0.0217 -0.0185 883  VAL B CG1 
15434 C CG2 . VAL B 885  ? 0.3070 0.2925 0.3188 0.0082  -0.0225 -0.0172 883  VAL B CG2 
15435 N N   . GLY B 886  ? 0.2197 0.2036 0.2346 0.0133  -0.0195 -0.0196 884  GLY B N   
15436 C CA  . GLY B 886  ? 0.2159 0.1989 0.2318 0.0161  -0.0192 -0.0205 884  GLY B CA  
15437 C C   . GLY B 886  ? 0.2091 0.1968 0.2307 0.0188  -0.0189 -0.0208 884  GLY B C   
15438 O O   . GLY B 886  ? 0.2142 0.2050 0.2386 0.0186  -0.0195 -0.0203 884  GLY B O   
15439 N N   . PRO B 887  ? 0.1931 0.1814 0.2162 0.0214  -0.0180 -0.0216 885  PRO B N   
15440 C CA  . PRO B 887  ? 0.1692 0.1623 0.1978 0.0242  -0.0177 -0.0218 885  PRO B CA  
15441 C C   . PRO B 887  ? 0.1799 0.1796 0.2134 0.0232  -0.0158 -0.0217 885  PRO B C   
15442 O O   . PRO B 887  ? 0.1915 0.1921 0.2242 0.0210  -0.0144 -0.0218 885  PRO B O   
15443 C CB  . PRO B 887  ? 0.2004 0.1915 0.2280 0.0271  -0.0171 -0.0227 885  PRO B CB  
15444 C CG  . PRO B 887  ? 0.2034 0.1912 0.2266 0.0251  -0.0160 -0.0231 885  PRO B CG  
15445 C CD  . PRO B 887  ? 0.2007 0.1850 0.2201 0.0219  -0.0174 -0.0223 885  PRO B CD  
15446 N N   . VAL B 888  ? 0.1894 0.1938 0.2281 0.0248  -0.0158 -0.0216 886  VAL B N   
15447 C CA  . VAL B 888  ? 0.1949 0.2052 0.2383 0.0244  -0.0138 -0.0216 886  VAL B CA  
15448 C C   . VAL B 888  ? 0.1805 0.1920 0.2246 0.0266  -0.0120 -0.0222 886  VAL B C   
15449 O O   . VAL B 888  ? 0.1853 0.1938 0.2274 0.0291  -0.0124 -0.0228 886  VAL B O   
15450 C CB  . VAL B 888  ? 0.2140 0.2293 0.2628 0.0246  -0.0146 -0.0210 886  VAL B CB  
15451 C CG1 . VAL B 888  ? 0.2014 0.2151 0.2487 0.0224  -0.0164 -0.0205 886  VAL B CG1 
15452 C CG2 . VAL B 888  ? 0.2741 0.2908 0.3256 0.0278  -0.0156 -0.0211 886  VAL B CG2 
15453 N N   . ILE B 889  ? 0.1819 0.1973 0.2283 0.0257  -0.0099 -0.0222 887  ILE B N   
15454 C CA  . ILE B 889  ? 0.1803 0.1957 0.2256 0.0271  -0.0079 -0.0229 887  ILE B CA  
15455 C C   . ILE B 889  ? 0.1854 0.2034 0.2335 0.0307  -0.0073 -0.0233 887  ILE B C   
15456 O O   . ILE B 889  ? 0.1845 0.2001 0.2299 0.0328  -0.0066 -0.0241 887  ILE B O   
15457 C CB  . ILE B 889  ? 0.1901 0.2086 0.2365 0.0252  -0.0059 -0.0226 887  ILE B CB  
15458 C CG1 . ILE B 889  ? 0.2125 0.2303 0.2568 0.0264  -0.0041 -0.0234 887  ILE B CG1 
15459 C CG2 . ILE B 889  ? 0.2129 0.2376 0.2653 0.0249  -0.0052 -0.0218 887  ILE B CG2 
15460 C CD1 . ILE B 889  ? 0.2077 0.2191 0.2458 0.0262  -0.0049 -0.0242 887  ILE B CD1 
15461 N N   . THR B 890  ? 0.1750 0.1981 0.2287 0.0315  -0.0076 -0.0226 888  THR B N   
15462 C CA  . THR B 890  ? 0.1862 0.2132 0.2434 0.0349  -0.0068 -0.0229 888  THR B CA  
15463 C C   . THR B 890  ? 0.1925 0.2223 0.2538 0.0358  -0.0087 -0.0223 888  THR B C   
15464 O O   . THR B 890  ? 0.1837 0.2136 0.2460 0.0335  -0.0103 -0.0216 888  THR B O   
15465 C CB  . THR B 890  ? 0.1970 0.2306 0.2586 0.0348  -0.0041 -0.0225 888  THR B CB  
15466 O OG1 . THR B 890  ? 0.2136 0.2509 0.2790 0.0319  -0.0043 -0.0214 888  THR B OG1 
15467 C CG2 . THR B 890  ? 0.2289 0.2604 0.2867 0.0344  -0.0021 -0.0231 888  THR B CG2 
15468 N N   . SER B 891  ? 0.2028 0.2354 0.2668 0.0394  -0.0085 -0.0225 889  SER B N   
15469 C CA  A SER B 891  ? 0.1918 0.2286 0.2608 0.0406  -0.0102 -0.0219 889  SER B CA  
15470 C CA  B SER B 891  ? 0.1919 0.2286 0.2608 0.0405  -0.0102 -0.0218 889  SER B CA  
15471 C CA  C SER B 891  ? 0.1922 0.2289 0.2612 0.0405  -0.0102 -0.0218 889  SER B CA  
15472 C C   . SER B 891  ? 0.1821 0.2257 0.2570 0.0380  -0.0096 -0.0207 889  SER B C   
15473 O O   . SER B 891  ? 0.2025 0.2479 0.2802 0.0368  -0.0117 -0.0200 889  SER B O   
15474 C CB  A SER B 891  ? 0.2269 0.2666 0.2983 0.0452  -0.0097 -0.0223 889  SER B CB  
15475 C CB  B SER B 891  ? 0.2273 0.2666 0.2984 0.0452  -0.0099 -0.0224 889  SER B CB  
15476 C CB  C SER B 891  ? 0.2273 0.2667 0.2984 0.0452  -0.0098 -0.0223 889  SER B CB  
15477 O OG  A SER B 891  ? 0.2294 0.2620 0.2950 0.0478  -0.0107 -0.0234 889  SER B OG  
15478 O OG  B SER B 891  ? 0.2179 0.2629 0.2922 0.0462  -0.0069 -0.0224 889  SER B OG  
15479 O OG  C SER B 891  ? 0.2498 0.2933 0.3258 0.0464  -0.0118 -0.0217 889  SER B OG  
15480 N N   . GLU B 892  ? 0.1739 0.2212 0.2506 0.0370  -0.0070 -0.0205 890  GLU B N   
15481 C CA  . GLU B 892  ? 0.1966 0.2496 0.2784 0.0342  -0.0064 -0.0194 890  GLU B CA  
15482 C C   . GLU B 892  ? 0.1969 0.2464 0.2766 0.0306  -0.0080 -0.0191 890  GLU B C   
15483 O O   . GLU B 892  ? 0.2020 0.2544 0.2853 0.0288  -0.0094 -0.0183 890  GLU B O   
15484 C CB  . GLU B 892  ? 0.2469 0.3033 0.3299 0.0337  -0.0032 -0.0192 890  GLU B CB  
15485 N N   . ALA B 893  ? 0.1950 0.2384 0.2688 0.0295  -0.0079 -0.0197 891  ALA B N   
15486 C CA  . ALA B 893  ? 0.1842 0.2244 0.2557 0.0264  -0.0093 -0.0195 891  ALA B CA  
15487 C C   . ALA B 893  ? 0.1856 0.2240 0.2569 0.0266  -0.0122 -0.0194 891  ALA B C   
15488 O O   . ALA B 893  ? 0.1920 0.2313 0.2648 0.0245  -0.0136 -0.0189 891  ALA B O   
15489 C CB  . ALA B 893  ? 0.2014 0.2360 0.2668 0.0255  -0.0086 -0.0201 891  ALA B CB  
15490 N N   . LYS B 894  ? 0.1822 0.2178 0.2514 0.0292  -0.0133 -0.0199 892  LYS B N   
15491 C CA  . LYS B 894  ? 0.1801 0.2137 0.2487 0.0297  -0.0162 -0.0197 892  LYS B CA  
15492 C C   . LYS B 894  ? 0.1805 0.2203 0.2555 0.0296  -0.0174 -0.0189 892  LYS B C   
15493 O O   . LYS B 894  ? 0.2132 0.2525 0.2884 0.0279  -0.0195 -0.0185 892  LYS B O   
15494 C CB  . LYS B 894  ? 0.2065 0.2364 0.2722 0.0330  -0.0170 -0.0202 892  LYS B CB  
15495 C CG  . LYS B 894  ? 0.2058 0.2334 0.2707 0.0339  -0.0201 -0.0200 892  LYS B CG  
15496 C CD  . LYS B 894  ? 0.2680 0.2908 0.3291 0.0372  -0.0207 -0.0206 892  LYS B CD  
15497 C CE  . LYS B 894  ? 0.3643 0.3868 0.4263 0.0395  -0.0236 -0.0202 892  LYS B CE  
15498 N NZ  . LYS B 894  ? 0.4096 0.4267 0.4672 0.0375  -0.0261 -0.0198 892  LYS B NZ  
15499 N N   . ASP B 895  ? 0.1849 0.2308 0.2651 0.0314  -0.0159 -0.0187 893  ASP B N   
15500 C CA  . ASP B 895  ? 0.1990 0.2515 0.2858 0.0310  -0.0170 -0.0178 893  ASP B CA  
15501 C C   . ASP B 895  ? 0.1811 0.2351 0.2695 0.0271  -0.0171 -0.0172 893  ASP B C   
15502 O O   . ASP B 895  ? 0.2064 0.2625 0.2976 0.0258  -0.0193 -0.0167 893  ASP B O   
15503 C CB  . ASP B 895  ? 0.2226 0.2820 0.3147 0.0334  -0.0150 -0.0176 893  ASP B CB  
15504 C CG  . ASP B 895  ? 0.2507 0.3092 0.3418 0.0378  -0.0152 -0.0183 893  ASP B CG  
15505 O OD1 . ASP B 895  ? 0.2709 0.3243 0.3585 0.0390  -0.0176 -0.0186 893  ASP B OD1 
15506 O OD2 . ASP B 895  ? 0.3007 0.3635 0.3945 0.0403  -0.0130 -0.0184 893  ASP B OD2 
15507 N N   . ASN B 896  ? 0.1909 0.2437 0.2775 0.0253  -0.0149 -0.0173 894  ASN B N   
15508 C CA  . ASN B 896  ? 0.1998 0.2532 0.2872 0.0219  -0.0149 -0.0168 894  ASN B CA  
15509 C C   . ASN B 896  ? 0.2181 0.2666 0.3017 0.0202  -0.0174 -0.0171 894  ASN B C   
15510 O O   . ASN B 896  ? 0.2124 0.2622 0.2981 0.0182  -0.0191 -0.0167 894  ASN B O   
15511 C CB  . ASN B 896  ? 0.2034 0.2557 0.2886 0.0210  -0.0121 -0.0169 894  ASN B CB  
15512 C CG  . ASN B 896  ? 0.2984 0.3508 0.3840 0.0177  -0.0118 -0.0164 894  ASN B CG  
15513 O OD1 . ASN B 896  ? 0.3164 0.3655 0.3998 0.0160  -0.0136 -0.0166 894  ASN B OD1 
15514 N ND2 . ASN B 896  ? 0.3582 0.4138 0.4462 0.0170  -0.0095 -0.0158 894  ASN B ND2 
15515 N N   . ILE B 897  ? 0.1800 0.2228 0.2579 0.0209  -0.0176 -0.0178 895  ILE B N   
15516 C CA  . ILE B 897  ? 0.1876 0.2257 0.2614 0.0194  -0.0198 -0.0180 895  ILE B CA  
15517 C C   . ILE B 897  ? 0.1860 0.2251 0.2617 0.0201  -0.0227 -0.0178 895  ILE B C   
15518 O O   . ILE B 897  ? 0.1786 0.2170 0.2540 0.0183  -0.0246 -0.0176 895  ILE B O   
15519 C CB  . ILE B 897  ? 0.1807 0.2130 0.2482 0.0201  -0.0193 -0.0186 895  ILE B CB  
15520 C CG1 . ILE B 897  ? 0.1949 0.2263 0.2604 0.0191  -0.0167 -0.0189 895  ILE B CG1 
15521 C CG2 . ILE B 897  ? 0.1863 0.2143 0.2496 0.0188  -0.0215 -0.0187 895  ILE B CG2 
15522 C CD1 . ILE B 897  ? 0.1949 0.2219 0.2556 0.0202  -0.0160 -0.0194 895  ILE B CD1 
15523 N N   . GLU B 898  ? 0.1869 0.2274 0.2643 0.0230  -0.0232 -0.0177 896  GLU B N   
15524 C CA  . GLU B 898  ? 0.1859 0.2275 0.2651 0.0240  -0.0262 -0.0174 896  GLU B CA  
15525 C C   . GLU B 898  ? 0.2096 0.2574 0.2950 0.0226  -0.0272 -0.0167 896  GLU B C   
15526 O O   . GLU B 898  ? 0.1980 0.2457 0.2839 0.0219  -0.0300 -0.0165 896  GLU B O   
15527 C CB  . GLU B 898  ? 0.2147 0.2564 0.2942 0.0277  -0.0264 -0.0175 896  GLU B CB  
15528 C CG  . GLU B 898  ? 0.2472 0.2815 0.3196 0.0286  -0.0265 -0.0181 896  GLU B CG  
15529 C CD  . GLU B 898  ? 0.3369 0.3701 0.4088 0.0325  -0.0268 -0.0183 896  GLU B CD  
15530 O OE1 . GLU B 898  ? 0.3610 0.3998 0.4381 0.0348  -0.0263 -0.0182 896  GLU B OE1 
15531 O OE2 . GLU B 898  ? 0.4225 0.4492 0.4885 0.0332  -0.0276 -0.0186 896  GLU B OE2 
15532 N N   . LYS B 899  ? 0.1792 0.2319 0.2691 0.0219  -0.0250 -0.0164 897  LYS B N   
15533 C CA  . LYS B 899  ? 0.2048 0.2631 0.3004 0.0199  -0.0260 -0.0156 897  LYS B CA  
15534 C C   . LYS B 899  ? 0.1918 0.2467 0.2849 0.0166  -0.0275 -0.0157 897  LYS B C   
15535 O O   . LYS B 899  ? 0.1883 0.2449 0.2837 0.0152  -0.0301 -0.0154 897  LYS B O   
15536 C CB  . LYS B 899  ? 0.2221 0.2858 0.3223 0.0195  -0.0231 -0.0150 897  LYS B CB  
15537 C CG  . LYS B 899  ? 0.2329 0.3025 0.3393 0.0170  -0.0241 -0.0140 897  LYS B CG  
15538 C CD  . LYS B 899  ? 0.3285 0.4046 0.4400 0.0169  -0.0213 -0.0131 897  LYS B CD  
15539 C CE  . LYS B 899  ? 0.3117 0.3849 0.4204 0.0149  -0.0188 -0.0131 897  LYS B CE  
15540 N NZ  . LYS B 899  ? 0.3030 0.3828 0.4172 0.0135  -0.0168 -0.0119 897  LYS B NZ  
15541 N N   . HIS B 900  ? 0.1740 0.2240 0.2620 0.0154  -0.0261 -0.0163 898  HIS B N   
15542 C CA  . HIS B 900  ? 0.1764 0.2227 0.2613 0.0128  -0.0274 -0.0166 898  HIS B CA  
15543 C C   . HIS B 900  ? 0.1848 0.2276 0.2663 0.0131  -0.0304 -0.0169 898  HIS B C   
15544 O O   . HIS B 900  ? 0.2041 0.2466 0.2859 0.0113  -0.0327 -0.0169 898  HIS B O   
15545 C CB  . HIS B 900  ? 0.1721 0.2142 0.2522 0.0120  -0.0251 -0.0171 898  HIS B CB  
15546 C CG  . HIS B 900  ? 0.1854 0.2231 0.2612 0.0100  -0.0263 -0.0176 898  HIS B CG  
15547 N ND1 . HIS B 900  ? 0.2418 0.2801 0.3192 0.0077  -0.0271 -0.0175 898  HIS B ND1 
15548 C CD2 . HIS B 900  ? 0.2013 0.2339 0.2712 0.0101  -0.0269 -0.0183 898  HIS B CD2 
15549 C CE1 . HIS B 900  ? 0.2122 0.2459 0.2846 0.0067  -0.0281 -0.0182 898  HIS B CE1 
15550 N NE2 . HIS B 900  ? 0.2083 0.2388 0.2764 0.0081  -0.0279 -0.0186 898  HIS B NE2 
15551 N N   . ILE B 901  ? 0.1828 0.2224 0.2606 0.0152  -0.0304 -0.0172 899  ILE B N   
15552 C CA  . ILE B 901  ? 0.1893 0.2251 0.2633 0.0156  -0.0332 -0.0174 899  ILE B CA  
15553 C C   . ILE B 901  ? 0.2001 0.2397 0.2784 0.0159  -0.0361 -0.0169 899  ILE B C   
15554 O O   . ILE B 901  ? 0.2081 0.2460 0.2848 0.0145  -0.0387 -0.0170 899  ILE B O   
15555 C CB  . ILE B 901  ? 0.1756 0.2077 0.2455 0.0179  -0.0327 -0.0176 899  ILE B CB  
15556 C CG1 . ILE B 901  ? 0.1780 0.2062 0.2431 0.0171  -0.0302 -0.0180 899  ILE B CG1 
15557 C CG2 . ILE B 901  ? 0.2228 0.2512 0.2889 0.0183  -0.0357 -0.0175 899  ILE B CG2 
15558 C CD1 . ILE B 901  ? 0.2188 0.2433 0.2801 0.0190  -0.0296 -0.0181 899  ILE B CD1 
15559 N N   . GLU B 902  ? 0.1926 0.2376 0.2766 0.0177  -0.0357 -0.0164 900  GLU B N   
15560 C CA  . GLU B 902  ? 0.2074 0.2571 0.2963 0.0182  -0.0385 -0.0158 900  GLU B CA  
15561 C C   . GLU B 902  ? 0.2027 0.2555 0.2952 0.0150  -0.0396 -0.0155 900  GLU B C   
15562 O O   . GLU B 902  ? 0.2194 0.2735 0.3134 0.0142  -0.0428 -0.0153 900  GLU B O   
15563 C CB  . GLU B 902  ? 0.2148 0.2702 0.3092 0.0212  -0.0375 -0.0153 900  GLU B CB  
15564 C CG  . GLU B 902  ? 0.2904 0.3422 0.3811 0.0247  -0.0374 -0.0156 900  GLU B CG  
15565 C CD  . GLU B 902  ? 0.3829 0.4293 0.4685 0.0250  -0.0406 -0.0157 900  GLU B CD  
15566 O OE1 . GLU B 902  ? 0.3735 0.4223 0.4616 0.0246  -0.0437 -0.0153 900  GLU B OE1 
15567 O OE2 . GLU B 902  ? 0.4189 0.4587 0.4980 0.0255  -0.0401 -0.0161 900  GLU B OE2 
15568 N N   . ARG B 903  ? 0.2140 0.2677 0.3076 0.0130  -0.0372 -0.0155 901  ARG B N   
15569 C CA  A ARG B 903  ? 0.2337 0.2890 0.3297 0.0097  -0.0383 -0.0152 901  ARG B CA  
15570 C CA  B ARG B 903  ? 0.2334 0.2888 0.3295 0.0097  -0.0384 -0.0152 901  ARG B CA  
15571 C C   . ARG B 903  ? 0.2680 0.3173 0.3583 0.0080  -0.0407 -0.0160 901  ARG B C   
15572 O O   . ARG B 903  ? 0.2628 0.3129 0.3545 0.0062  -0.0436 -0.0159 901  ARG B O   
15573 C CB  A ARG B 903  ? 0.2642 0.3207 0.3617 0.0081  -0.0353 -0.0150 901  ARG B CB  
15574 C CB  B ARG B 903  ? 0.2639 0.3205 0.3615 0.0081  -0.0353 -0.0150 901  ARG B CB  
15575 C CG  A ARG B 903  ? 0.3319 0.3904 0.4325 0.0046  -0.0365 -0.0145 901  ARG B CG  
15576 C CG  B ARG B 903  ? 0.3322 0.3886 0.4307 0.0045  -0.0365 -0.0148 901  ARG B CG  
15577 C CD  A ARG B 903  ? 0.3599 0.4193 0.4617 0.0031  -0.0334 -0.0141 901  ARG B CD  
15578 C CD  B ARG B 903  ? 0.3637 0.4239 0.4664 0.0030  -0.0340 -0.0140 901  ARG B CD  
15579 N NE  A ARG B 903  ? 0.3691 0.4219 0.4646 0.0023  -0.0323 -0.0150 901  ARG B NE  
15580 N NE  B ARG B 903  ? 0.3655 0.4258 0.4698 -0.0006 -0.0358 -0.0136 901  ARG B NE  
15581 C CZ  A ARG B 903  ? 0.3577 0.4068 0.4508 -0.0002 -0.0335 -0.0153 901  ARG B CZ  
15582 C CZ  B ARG B 903  ? 0.3764 0.4307 0.4758 -0.0025 -0.0363 -0.0144 901  ARG B CZ  
15583 N NH1 A ARG B 903  ? 0.4051 0.4560 0.5013 -0.0026 -0.0361 -0.0149 901  ARG B NH1 
15584 N NH1 B ARG B 903  ? 0.3704 0.4189 0.4634 -0.0013 -0.0350 -0.0154 901  ARG B NH1 
15585 N NH2 A ARG B 903  ? 0.3697 0.4134 0.4573 -0.0004 -0.0321 -0.0161 901  ARG B NH2 
15586 N NH2 B ARG B 903  ? 0.3391 0.3932 0.4399 -0.0057 -0.0381 -0.0141 901  ARG B NH2 
15587 N N   . MET B 904  ? 0.2293 0.2726 0.3131 0.0084  -0.0395 -0.0168 902  MET B N   
15588 C CA  . MET B 904  ? 0.2195 0.2572 0.2973 0.0072  -0.0414 -0.0176 902  MET B CA  
15589 C C   . MET B 904  ? 0.2497 0.2870 0.3267 0.0082  -0.0449 -0.0175 902  MET B C   
15590 O O   . MET B 904  ? 0.2477 0.2834 0.3231 0.0066  -0.0476 -0.0178 902  MET B O   
15591 C CB  . MET B 904  ? 0.2344 0.2668 0.3058 0.0078  -0.0392 -0.0182 902  MET B CB  
15592 C CG  . MET B 904  ? 0.2397 0.2721 0.3112 0.0070  -0.0361 -0.0184 902  MET B CG  
15593 S SD  . MET B 904  ? 0.3466 0.3776 0.4179 0.0039  -0.0369 -0.0188 902  MET B SD  
15594 C CE  . MET B 904  ? 0.3531 0.3907 0.4326 0.0029  -0.0362 -0.0177 902  MET B CE  
15595 N N   . ARG B 905  ? 0.2228 0.2612 0.3005 0.0109  -0.0449 -0.0170 903  ARG B N   
15596 C CA  . ARG B 905  ? 0.2558 0.2937 0.3327 0.0121  -0.0482 -0.0168 903  ARG B CA  
15597 C C   . ARG B 905  ? 0.2708 0.3141 0.3536 0.0110  -0.0510 -0.0163 903  ARG B C   
15598 O O   . ARG B 905  ? 0.2719 0.3136 0.3529 0.0101  -0.0544 -0.0165 903  ARG B O   
15599 C CB  . ARG B 905  ? 0.2878 0.3263 0.3650 0.0155  -0.0477 -0.0164 903  ARG B CB  
15600 C CG  . ARG B 905  ? 0.4011 0.4359 0.4741 0.0170  -0.0506 -0.0162 903  ARG B CG  
15601 C CD  . ARG B 905  ? 0.3919 0.4277 0.4662 0.0205  -0.0504 -0.0157 903  ARG B CD  
15602 N NE  . ARG B 905  ? 0.3576 0.3911 0.4297 0.0215  -0.0470 -0.0160 903  ARG B NE  
15603 C CZ  . ARG B 905  ? 0.3307 0.3577 0.3960 0.0218  -0.0462 -0.0163 903  ARG B CZ  
15604 N NH1 . ARG B 905  ? 0.3821 0.4042 0.4417 0.0209  -0.0484 -0.0162 903  ARG B NH1 
15605 N NH2 . ARG B 905  ? 0.3752 0.4008 0.4392 0.0227  -0.0433 -0.0165 903  ARG B NH2 
15606 N N   . GLY B 906  ? 0.2507 0.3004 0.3406 0.0108  -0.0497 -0.0157 904  GLY B N   
15607 C CA  . GLY B 906  ? 0.2495 0.3053 0.3458 0.0095  -0.0523 -0.0150 904  GLY B CA  
15608 C C   . GLY B 906  ? 0.2593 0.3132 0.3545 0.0057  -0.0540 -0.0154 904  GLY B C   
15609 O O   . GLY B 906  ? 0.2916 0.3487 0.3903 0.0043  -0.0572 -0.0150 904  GLY B O   
15610 N N   . LEU B 907  ? 0.3144 0.3631 0.4048 0.0042  -0.0521 -0.0162 905  LEU B N   
15611 C CA  . LEU B 907  ? 0.3023 0.3478 0.3903 0.0010  -0.0538 -0.0168 905  LEU B CA  
15612 C C   . LEU B 907  ? 0.2801 0.3193 0.3609 0.0010  -0.0563 -0.0177 905  LEU B C   
15613 O O   . LEU B 907  ? 0.3140 0.3496 0.3917 -0.0013 -0.0578 -0.0185 905  LEU B O   
15614 C CB  . LEU B 907  ? 0.3430 0.3861 0.4293 -0.0004 -0.0506 -0.0172 905  LEU B CB  
15615 C CG  . LEU B 907  ? 0.3979 0.4470 0.4912 -0.0013 -0.0485 -0.0161 905  LEU B CG  
15616 C CD1 . LEU B 907  ? 0.4190 0.4649 0.5098 -0.0024 -0.0454 -0.0164 905  LEU B CD1 
15617 C CD2 . LEU B 907  ? 0.3853 0.4389 0.4842 -0.0040 -0.0513 -0.0154 905  LEU B CD2 
15618 N N   . GLY B 908  ? 0.2729 0.3105 0.3507 0.0036  -0.0568 -0.0177 906  GLY B N   
15619 C CA  . GLY B 908  ? 0.2851 0.3172 0.3561 0.0037  -0.0593 -0.0184 906  GLY B CA  
15620 C C   . GLY B 908  ? 0.3334 0.3590 0.3967 0.0040  -0.0571 -0.0193 906  GLY B C   
15621 O O   . GLY B 908  ? 0.3100 0.3310 0.3671 0.0039  -0.0588 -0.0198 906  GLY B O   
15622 N N   . ARG B 909  ? 0.2683 0.2939 0.3319 0.0043  -0.0533 -0.0193 907  ARG B N   
15623 C CA  . ARG B 909  ? 0.2609 0.2813 0.3177 0.0046  -0.0511 -0.0200 907  ARG B CA  
15624 C C   . ARG B 909  ? 0.2682 0.2864 0.3214 0.0068  -0.0511 -0.0196 907  ARG B C   
15625 O O   . ARG B 909  ? 0.2864 0.3074 0.3430 0.0086  -0.0512 -0.0188 907  ARG B O   
15626 C CB  . ARG B 909  ? 0.2767 0.2982 0.3354 0.0045  -0.0472 -0.0200 907  ARG B CB  
15627 C CG  . ARG B 909  ? 0.3051 0.3279 0.3666 0.0023  -0.0469 -0.0203 907  ARG B CG  
15628 C CD  . ARG B 909  ? 0.3853 0.4031 0.4414 0.0007  -0.0483 -0.0214 907  ARG B CD  
15629 N NE  . ARG B 909  ? 0.4680 0.4862 0.5264 -0.0014 -0.0480 -0.0216 907  ARG B NE  
15630 C CZ  . ARG B 909  ? 0.4951 0.5151 0.5571 -0.0033 -0.0507 -0.0214 907  ARG B CZ  
15631 N NH1 . ARG B 909  ? 0.5423 0.5644 0.6062 -0.0033 -0.0538 -0.0211 907  ARG B NH1 
15632 N NH2 . ARG B 909  ? 0.5841 0.6037 0.6476 -0.0053 -0.0503 -0.0216 907  ARG B NH2 
15633 N N   . LYS B 910  ? 0.2521 0.2652 0.2981 0.0066  -0.0510 -0.0202 908  LYS B N   
15634 C CA  . LYS B 910  ? 0.2767 0.2871 0.3185 0.0083  -0.0509 -0.0196 908  LYS B CA  
15635 C C   . LYS B 910  ? 0.2479 0.2589 0.2907 0.0094  -0.0475 -0.0193 908  LYS B C   
15636 O O   . LYS B 910  ? 0.2571 0.2674 0.2987 0.0085  -0.0448 -0.0198 908  LYS B O   
15637 C CB  . LYS B 910  ? 0.2876 0.2928 0.3215 0.0076  -0.0514 -0.0202 908  LYS B CB  
15638 C CG  . LYS B 910  ? 0.3696 0.3717 0.3988 0.0089  -0.0519 -0.0194 908  LYS B CG  
15639 C CD  . LYS B 910  ? 0.4460 0.4435 0.4672 0.0080  -0.0518 -0.0198 908  LYS B CD  
15640 C CE  . LYS B 910  ? 0.5858 0.5801 0.6023 0.0090  -0.0527 -0.0188 908  LYS B CE  
15641 N NZ  . LYS B 910  ? 0.5608 0.5510 0.5695 0.0081  -0.0517 -0.0189 908  LYS B NZ  
15642 N N   . VAL B 911  ? 0.2361 0.2482 0.2807 0.0113  -0.0477 -0.0185 909  VAL B N   
15643 C CA  . VAL B 911  ? 0.2221 0.2345 0.2675 0.0125  -0.0448 -0.0182 909  VAL B CA  
15644 C C   . VAL B 911  ? 0.2553 0.2636 0.2958 0.0139  -0.0454 -0.0177 909  VAL B C   
15645 O O   . VAL B 911  ? 0.2688 0.2767 0.3094 0.0153  -0.0481 -0.0171 909  VAL B O   
15646 C CB  . VAL B 911  ? 0.2261 0.2439 0.2790 0.0139  -0.0443 -0.0179 909  VAL B CB  
15647 C CG1 . VAL B 911  ? 0.2282 0.2456 0.2810 0.0155  -0.0417 -0.0177 909  VAL B CG1 
15648 C CG2 . VAL B 911  ? 0.2372 0.2590 0.2949 0.0121  -0.0436 -0.0182 909  VAL B CG2 
15649 N N   . GLU B 912  ? 0.2376 0.2427 0.2738 0.0135  -0.0432 -0.0177 910  GLU B N   
15650 C CA  . GLU B 912  ? 0.2431 0.2439 0.2743 0.0144  -0.0435 -0.0170 910  GLU B CA  
15651 C C   . GLU B 912  ? 0.2404 0.2408 0.2720 0.0151  -0.0408 -0.0170 910  GLU B C   
15652 O O   . GLU B 912  ? 0.2555 0.2574 0.2880 0.0140  -0.0382 -0.0175 910  GLU B O   
15653 C CB  . GLU B 912  ? 0.2709 0.2675 0.2950 0.0127  -0.0437 -0.0170 910  GLU B CB  
15654 C CG  . GLU B 912  ? 0.3758 0.3719 0.3984 0.0121  -0.0466 -0.0171 910  GLU B CG  
15655 C CD  . GLU B 912  ? 0.4916 0.4842 0.5072 0.0105  -0.0462 -0.0173 910  GLU B CD  
15656 O OE1 . GLU B 912  ? 0.5259 0.5147 0.5363 0.0105  -0.0465 -0.0164 910  GLU B OE1 
15657 O OE2 . GLU B 912  ? 0.5712 0.5647 0.5864 0.0092  -0.0456 -0.0182 910  GLU B OE2 
15658 N N   . GLN B 913  ? 0.2293 0.2277 0.2600 0.0170  -0.0415 -0.0164 911  GLN B N   
15659 C CA  . GLN B 913  ? 0.2365 0.2336 0.2667 0.0177  -0.0393 -0.0164 911  GLN B CA  
15660 C C   . GLN B 913  ? 0.2880 0.2790 0.3117 0.0177  -0.0401 -0.0157 911  GLN B C   
15661 O O   . GLN B 913  ? 0.3143 0.3027 0.3359 0.0188  -0.0427 -0.0150 911  GLN B O   
15662 C CB  . GLN B 913  ? 0.2600 0.2604 0.2959 0.0203  -0.0391 -0.0165 911  GLN B CB  
15663 C CG  . GLN B 913  ? 0.2691 0.2758 0.3115 0.0199  -0.0382 -0.0170 911  GLN B CG  
15664 C CD  . GLN B 913  ? 0.3000 0.3106 0.3479 0.0224  -0.0375 -0.0171 911  GLN B CD  
15665 O OE1 . GLN B 913  ? 0.4005 0.4122 0.4505 0.0246  -0.0394 -0.0168 911  GLN B OE1 
15666 N NE2 . GLN B 913  ? 0.2777 0.2907 0.3280 0.0221  -0.0346 -0.0175 911  GLN B NE2 
15667 N N   . ILE B 914  ? 0.2860 0.2747 0.3066 0.0165  -0.0379 -0.0157 912  ILE B N   
15668 C CA  . ILE B 914  ? 0.3707 0.3535 0.3846 0.0156  -0.0385 -0.0148 912  ILE B CA  
15669 C C   . ILE B 914  ? 0.3357 0.3162 0.3487 0.0163  -0.0370 -0.0149 912  ILE B C   
15670 O O   . ILE B 914  ? 0.3253 0.3079 0.3398 0.0153  -0.0345 -0.0155 912  ILE B O   
15671 C CB  . ILE B 914  ? 0.3661 0.3480 0.3757 0.0127  -0.0375 -0.0146 912  ILE B CB  
15672 C CG1 . ILE B 914  ? 0.3816 0.3649 0.3911 0.0123  -0.0393 -0.0147 912  ILE B CG1 
15673 C CG2 . ILE B 914  ? 0.3485 0.3248 0.3514 0.0114  -0.0377 -0.0136 912  ILE B CG2 
15674 C CD1 . ILE B 914  ? 0.3472 0.3313 0.3539 0.0099  -0.0379 -0.0149 912  ILE B CD1 
15675 N N   . GLU B 919  ? 0.4664 0.4099 0.4661 0.0435  -0.0391 -0.0195 917  GLU B N   
15676 C CA  . GLU B 919  ? 0.4512 0.3929 0.4488 0.0424  -0.0369 -0.0206 917  GLU B CA  
15677 C C   . GLU B 919  ? 0.4612 0.4125 0.4656 0.0419  -0.0338 -0.0214 917  GLU B C   
15678 O O   . GLU B 919  ? 0.4799 0.4318 0.4846 0.0430  -0.0319 -0.0226 917  GLU B O   
15679 C CB  . GLU B 919  ? 0.4678 0.4035 0.4590 0.0374  -0.0371 -0.0198 917  GLU B CB  
15680 N N   . THR B 920  ? 0.4160 0.3744 0.4256 0.0403  -0.0336 -0.0206 918  THR B N   
15681 C CA  . THR B 920  ? 0.3981 0.3651 0.4138 0.0394  -0.0309 -0.0211 918  THR B CA  
15682 C C   . THR B 920  ? 0.4018 0.3748 0.4235 0.0437  -0.0299 -0.0220 918  THR B C   
15683 O O   . THR B 920  ? 0.3501 0.3293 0.3762 0.0433  -0.0273 -0.0225 918  THR B O   
15684 C CB  . THR B 920  ? 0.3823 0.3543 0.4011 0.0362  -0.0310 -0.0201 918  THR B CB  
15685 O OG1 . THR B 920  ? 0.3882 0.3614 0.4090 0.0379  -0.0334 -0.0194 918  THR B OG1 
15686 C CG2 . THR B 920  ? 0.3341 0.3015 0.3474 0.0318  -0.0313 -0.0194 918  THR B CG2 
15687 N N   . GLY B 921  ? 0.4046 0.3760 0.4265 0.0478  -0.0317 -0.0220 919  GLY B N   
15688 C CA  . GLY B 921  ? 0.4024 0.3806 0.4306 0.0520  -0.0308 -0.0227 919  GLY B CA  
15689 C C   . GLY B 921  ? 0.4085 0.3878 0.4370 0.0540  -0.0281 -0.0240 919  GLY B C   
15690 O O   . GLY B 921  ? 0.4139 0.4009 0.4485 0.0563  -0.0264 -0.0244 919  GLY B O   
15691 N N   . VAL B 922  ? 0.3133 0.2850 0.3351 0.0529  -0.0277 -0.0247 920  VAL B N   
15692 C CA  . VAL B 922  ? 0.3012 0.2730 0.3222 0.0546  -0.0253 -0.0261 920  VAL B CA  
15693 C C   . VAL B 922  ? 0.2710 0.2485 0.2950 0.0512  -0.0225 -0.0261 920  VAL B C   
15694 O O   . VAL B 922  ? 0.2626 0.2418 0.2869 0.0525  -0.0202 -0.0272 920  VAL B O   
15695 C CB  . VAL B 922  ? 0.3095 0.2703 0.3218 0.0549  -0.0263 -0.0269 920  VAL B CB  
15696 C CG1 . VAL B 922  ? 0.3689 0.3238 0.3783 0.0593  -0.0289 -0.0271 920  VAL B CG1 
15697 C CG2 . VAL B 922  ? 0.3285 0.2840 0.3359 0.0495  -0.0272 -0.0260 920  VAL B CG2 
15698 N N   . GLY B 923  ? 0.2597 0.2401 0.2856 0.0470  -0.0226 -0.0250 921  GLY B N   
15699 C CA  . GLY B 923  ? 0.2472 0.2331 0.2761 0.0440  -0.0202 -0.0249 921  GLY B CA  
15700 C C   . GLY B 923  ? 0.2653 0.2590 0.3009 0.0428  -0.0201 -0.0240 921  GLY B C   
15701 O O   . GLY B 923  ? 0.2779 0.2738 0.3165 0.0448  -0.0218 -0.0235 921  GLY B O   
15702 N N   . THR B 924  ? 0.2127 0.2105 0.2505 0.0395  -0.0185 -0.0236 922  THR B N   
15703 C CA  . THR B 924  ? 0.2004 0.2052 0.2442 0.0381  -0.0184 -0.0228 922  THR B CA  
15704 C C   . THR B 924  ? 0.2129 0.2155 0.2543 0.0340  -0.0194 -0.0220 922  THR B C   
15705 O O   . THR B 924  ? 0.2312 0.2336 0.2711 0.0313  -0.0180 -0.0221 922  THR B O   
15706 C CB  . THR B 924  ? 0.2120 0.2236 0.2606 0.0379  -0.0156 -0.0229 922  THR B CB  
15707 O OG1 . THR B 924  ? 0.2206 0.2297 0.2656 0.0360  -0.0139 -0.0234 922  THR B OG1 
15708 C CG2 . THR B 924  ? 0.2307 0.2458 0.2824 0.0421  -0.0146 -0.0235 922  THR B CG2 
15709 N N   . PHE B 925  ? 0.2102 0.2113 0.2511 0.0338  -0.0219 -0.0214 923  PHE B N   
15710 C CA  . PHE B 925  ? 0.2063 0.2052 0.2445 0.0303  -0.0229 -0.0207 923  PHE B CA  
15711 C C   . PHE B 925  ? 0.2163 0.2199 0.2590 0.0296  -0.0241 -0.0201 923  PHE B C   
15712 O O   . PHE B 925  ? 0.2111 0.2174 0.2573 0.0319  -0.0254 -0.0199 923  PHE B O   
15713 C CB  . PHE B 925  ? 0.2196 0.2108 0.2515 0.0302  -0.0251 -0.0204 923  PHE B CB  
15714 C CG  . PHE B 925  ? 0.2174 0.2028 0.2439 0.0300  -0.0244 -0.0209 923  PHE B CG  
15715 C CD1 . PHE B 925  ? 0.2223 0.2052 0.2477 0.0333  -0.0243 -0.0217 923  PHE B CD1 
15716 C CD2 . PHE B 925  ? 0.2193 0.2018 0.2417 0.0264  -0.0239 -0.0206 923  PHE B CD2 
15717 C CE1 . PHE B 925  ? 0.2337 0.2107 0.2537 0.0330  -0.0239 -0.0223 923  PHE B CE1 
15718 C CE2 . PHE B 925  ? 0.2332 0.2105 0.2507 0.0259  -0.0234 -0.0211 923  PHE B CE2 
15719 C CZ  . PHE B 925  ? 0.2367 0.2108 0.2527 0.0291  -0.0235 -0.0219 923  PHE B CZ  
15720 N N   . VAL B 926  ? 0.1926 0.1971 0.2348 0.0264  -0.0237 -0.0197 924  VAL B N   
15721 C CA  . VAL B 926  ? 0.1940 0.2010 0.2385 0.0251  -0.0252 -0.0192 924  VAL B CA  
15722 C C   . VAL B 926  ? 0.2017 0.2039 0.2405 0.0226  -0.0263 -0.0188 924  VAL B C   
15723 O O   . VAL B 926  ? 0.2157 0.2161 0.2515 0.0206  -0.0247 -0.0190 924  VAL B O   
15724 C CB  . VAL B 926  ? 0.1988 0.2117 0.2481 0.0235  -0.0237 -0.0193 924  VAL B CB  
15725 C CG1 . VAL B 926  ? 0.2197 0.2340 0.2703 0.0220  -0.0255 -0.0188 924  VAL B CG1 
15726 C CG2 . VAL B 926  ? 0.2137 0.2318 0.2686 0.0257  -0.0224 -0.0194 924  VAL B CG2 
15727 N N   . PRO B 927  ? 0.2369 0.2368 0.2738 0.0226  -0.0288 -0.0183 925  PRO B N   
15728 C CA  . PRO B 927  ? 0.2370 0.2326 0.2683 0.0202  -0.0295 -0.0178 925  PRO B CA  
15729 C C   . PRO B 927  ? 0.2264 0.2249 0.2587 0.0177  -0.0288 -0.0179 925  PRO B C   
15730 O O   . PRO B 927  ? 0.2235 0.2267 0.2607 0.0179  -0.0286 -0.0182 925  PRO B O   
15731 C CB  . PRO B 927  ? 0.2996 0.2923 0.3290 0.0214  -0.0325 -0.0172 925  PRO B CB  
15732 C CG  . PRO B 927  ? 0.2594 0.2573 0.2950 0.0233  -0.0334 -0.0174 925  PRO B CG  
15733 C CD  . PRO B 927  ? 0.2507 0.2525 0.2908 0.0247  -0.0310 -0.0180 925  PRO B CD  
15734 N N   . PRO B 928  ? 0.2229 0.2187 0.2506 0.0154  -0.0283 -0.0177 926  PRO B N   
15735 C CA  . PRO B 928  ? 0.2139 0.2119 0.2417 0.0134  -0.0279 -0.0178 926  PRO B CA  
15736 C C   . PRO B 928  ? 0.2208 0.2203 0.2507 0.0139  -0.0301 -0.0178 926  PRO B C   
15737 O O   . PRO B 928  ? 0.2299 0.2270 0.2580 0.0147  -0.0324 -0.0173 926  PRO B O   
15738 C CB  . PRO B 928  ? 0.2131 0.2071 0.2347 0.0114  -0.0279 -0.0173 926  PRO B CB  
15739 C CG  . PRO B 928  ? 0.2700 0.2612 0.2895 0.0117  -0.0270 -0.0172 926  PRO B CG  
15740 C CD  . PRO B 928  ? 0.2585 0.2493 0.2806 0.0145  -0.0281 -0.0173 926  PRO B CD  
15741 N N   . THR B 929  ? 0.2167 0.2202 0.2504 0.0133  -0.0295 -0.0182 927  THR B N   
15742 C CA  . THR B 929  ? 0.2103 0.2160 0.2470 0.0135  -0.0315 -0.0183 927  THR B CA  
15743 C C   . THR B 929  ? 0.2029 0.2091 0.2384 0.0116  -0.0312 -0.0187 927  THR B C   
15744 O O   . THR B 929  ? 0.2060 0.2132 0.2418 0.0106  -0.0290 -0.0191 927  THR B O   
15745 C CB  . THR B 929  ? 0.2089 0.2192 0.2522 0.0148  -0.0310 -0.0184 927  THR B CB  
15746 O OG1 . THR B 929  ? 0.2123 0.2222 0.2565 0.0170  -0.0312 -0.0182 927  THR B OG1 
15747 C CG2 . THR B 929  ? 0.2253 0.2384 0.2721 0.0146  -0.0332 -0.0184 927  THR B CG2 
15748 N N   . ILE B 930  ? 0.2102 0.2151 0.2438 0.0111  -0.0335 -0.0187 928  ILE B N   
15749 C CA  . ILE B 930  ? 0.2167 0.2215 0.2487 0.0096  -0.0336 -0.0193 928  ILE B CA  
15750 C C   . ILE B 930  ? 0.2143 0.2212 0.2499 0.0096  -0.0358 -0.0195 928  ILE B C   
15751 O O   . ILE B 930  ? 0.2194 0.2261 0.2555 0.0104  -0.0384 -0.0191 928  ILE B O   
15752 C CB  . ILE B 930  ? 0.2066 0.2076 0.2320 0.0087  -0.0343 -0.0191 928  ILE B CB  
15753 C CG1 . ILE B 930  ? 0.2428 0.2422 0.2648 0.0083  -0.0320 -0.0188 928  ILE B CG1 
15754 C CG2 . ILE B 930  ? 0.2345 0.2354 0.2580 0.0076  -0.0345 -0.0199 928  ILE B CG2 
15755 C CD1 . ILE B 930  ? 0.2995 0.2953 0.3150 0.0074  -0.0327 -0.0182 928  ILE B CD1 
15756 N N   . ILE B 931  ? 0.2199 0.2289 0.2582 0.0086  -0.0351 -0.0201 929  ILE B N   
15757 C CA  . ILE B 931  ? 0.2021 0.2132 0.2441 0.0081  -0.0371 -0.0203 929  ILE B CA  
15758 C C   . ILE B 931  ? 0.2254 0.2346 0.2643 0.0066  -0.0376 -0.0211 929  ILE B C   
15759 O O   . ILE B 931  ? 0.2186 0.2274 0.2564 0.0060  -0.0354 -0.0216 929  ILE B O   
15760 C CB  . ILE B 931  ? 0.1962 0.2117 0.2448 0.0082  -0.0359 -0.0200 929  ILE B CB  
15761 C CG1 . ILE B 931  ? 0.2249 0.2424 0.2762 0.0101  -0.0352 -0.0193 929  ILE B CG1 
15762 C CG2 . ILE B 931  ? 0.2041 0.2221 0.2568 0.0072  -0.0382 -0.0200 929  ILE B CG2 
15763 C CD1 . ILE B 931  ? 0.2259 0.2481 0.2836 0.0104  -0.0339 -0.0190 929  ILE B CD1 
15764 N N   . GLU B 932  ? 0.2269 0.2346 0.2640 0.0061  -0.0404 -0.0214 930  GLU B N   
15765 C CA  . GLU B 932  ? 0.2234 0.2287 0.2571 0.0049  -0.0411 -0.0224 930  GLU B CA  
15766 C C   . GLU B 932  ? 0.2365 0.2439 0.2749 0.0038  -0.0419 -0.0227 930  GLU B C   
15767 O O   . GLU B 932  ? 0.2312 0.2413 0.2742 0.0035  -0.0439 -0.0222 930  GLU B O   
15768 C CB  . GLU B 932  ? 0.2967 0.2991 0.3256 0.0048  -0.0440 -0.0226 930  GLU B CB  
15769 C CG  . GLU B 932  ? 0.3275 0.3275 0.3515 0.0057  -0.0434 -0.0221 930  GLU B CG  
15770 C CD  . GLU B 932  ? 0.4955 0.4918 0.5123 0.0052  -0.0436 -0.0228 930  GLU B CD  
15771 O OE1 . GLU B 932  ? 0.4930 0.4885 0.5084 0.0046  -0.0430 -0.0238 930  GLU B OE1 
15772 O OE2 . GLU B 932  ? 0.4388 0.4331 0.4513 0.0056  -0.0443 -0.0222 930  GLU B OE2 
15773 N N   . LEU B 933  ? 0.2492 0.2556 0.2867 0.0030  -0.0403 -0.0234 931  LEU B N   
15774 C CA  . LEU B 933  ? 0.2495 0.2569 0.2906 0.0016  -0.0411 -0.0236 931  LEU B CA  
15775 C C   . LEU B 933  ? 0.3001 0.3036 0.3368 0.0006  -0.0431 -0.0249 931  LEU B C   
15776 O O   . LEU B 933  ? 0.3541 0.3541 0.3847 0.0012  -0.0427 -0.0257 931  LEU B O   
15777 C CB  . LEU B 933  ? 0.2565 0.2650 0.2995 0.0015  -0.0380 -0.0236 931  LEU B CB  
15778 C CG  . LEU B 933  ? 0.2879 0.2999 0.3347 0.0026  -0.0356 -0.0226 931  LEU B CG  
15779 C CD1 . LEU B 933  ? 0.3351 0.3475 0.3827 0.0023  -0.0328 -0.0226 931  LEU B CD1 
15780 C CD2 . LEU B 933  ? 0.3549 0.3711 0.4079 0.0025  -0.0369 -0.0216 931  LEU B CD2 
15781 N N   . GLU B 934  ? 0.3315 0.3355 0.3712 -0.0010 -0.0453 -0.0250 932  GLU B N   
15782 C CA  . GLU B 934  ? 0.3516 0.3512 0.3871 -0.0021 -0.0472 -0.0263 932  GLU B CA  
15783 C C   . GLU B 934  ? 0.3680 0.3654 0.4021 -0.0023 -0.0451 -0.0269 932  GLU B C   
15784 O O   . GLU B 934  ? 0.4184 0.4114 0.4468 -0.0019 -0.0452 -0.0283 932  GLU B O   
15785 C CB  . GLU B 934  ? 0.3844 0.3850 0.4234 -0.0040 -0.0508 -0.0261 932  GLU B CB  
15786 N N   . LYS B 935  ? 0.3251 0.3256 0.3642 -0.0026 -0.0430 -0.0260 933  LYS B N   
15787 C CA  . LYS B 935  ? 0.3471 0.3457 0.3854 -0.0028 -0.0411 -0.0264 933  LYS B CA  
15788 C C   . LYS B 935  ? 0.2889 0.2914 0.3312 -0.0020 -0.0379 -0.0253 933  LYS B C   
15789 O O   . LYS B 935  ? 0.2959 0.3028 0.3430 -0.0020 -0.0377 -0.0241 933  LYS B O   
15790 C CB  . LYS B 935  ? 0.3929 0.3902 0.4334 -0.0050 -0.0431 -0.0265 933  LYS B CB  
15791 N N   . LEU B 936  ? 0.2747 0.2757 0.3147 -0.0011 -0.0354 -0.0256 934  LEU B N   
15792 C CA  . LEU B 936  ? 0.3063 0.3106 0.3494 -0.0004 -0.0324 -0.0246 934  LEU B CA  
15793 C C   . LEU B 936  ? 0.2957 0.3033 0.3452 -0.0019 -0.0325 -0.0234 934  LEU B C   
15794 O O   . LEU B 936  ? 0.2878 0.2995 0.3411 -0.0014 -0.0308 -0.0224 934  LEU B O   
15795 C CB  . LEU B 936  ? 0.3345 0.3367 0.3743 0.0006  -0.0301 -0.0252 934  LEU B CB  
15796 C CG  . LEU B 936  ? 0.3404 0.3451 0.3801 0.0021  -0.0272 -0.0248 934  LEU B CG  
15797 C CD1 . LEU B 936  ? 0.3379 0.3402 0.3728 0.0034  -0.0256 -0.0257 934  LEU B CD1 
15798 C CD2 . LEU B 936  ? 0.3541 0.3622 0.3988 0.0018  -0.0255 -0.0235 934  LEU B CD2 
15799 N N   . SER B 937  ? 0.2831 0.2890 0.3335 -0.0038 -0.0345 -0.0235 935  SER B N   
15800 C CA  . SER B 937  ? 0.3043 0.3136 0.3607 -0.0056 -0.0346 -0.0222 935  SER B CA  
15801 C C   . SER B 937  ? 0.3052 0.3199 0.3669 -0.0058 -0.0355 -0.0212 935  SER B C   
15802 O O   . SER B 937  ? 0.3053 0.3241 0.3725 -0.0069 -0.0351 -0.0199 935  SER B O   
15803 C CB  . SER B 937  ? 0.3197 0.3255 0.3756 -0.0079 -0.0368 -0.0225 935  SER B CB  
15804 O OG  . SER B 937  ? 0.3592 0.3627 0.4129 -0.0087 -0.0401 -0.0234 935  SER B OG  
15805 N N   . ASP B 938  ? 0.2927 0.3074 0.3526 -0.0046 -0.0368 -0.0217 936  ASP B N   
15806 C CA  . ASP B 938  ? 0.2980 0.3177 0.3626 -0.0041 -0.0374 -0.0208 936  ASP B CA  
15807 C C   . ASP B 938  ? 0.2658 0.2893 0.3333 -0.0026 -0.0343 -0.0199 936  ASP B C   
15808 O O   . ASP B 938  ? 0.3079 0.3363 0.3805 -0.0022 -0.0343 -0.0189 936  ASP B O   
15809 C CB  . ASP B 938  ? 0.3480 0.3663 0.4092 -0.0027 -0.0391 -0.0214 936  ASP B CB  
15810 C CG  . ASP B 938  ? 0.4447 0.4596 0.5029 -0.0041 -0.0425 -0.0223 936  ASP B CG  
15811 O OD1 . ASP B 938  ? 0.4431 0.4577 0.5032 -0.0062 -0.0441 -0.0222 936  ASP B OD1 
15812 O OD2 . ASP B 938  ? 0.4907 0.5030 0.5444 -0.0030 -0.0437 -0.0230 936  ASP B OD2 
15813 N N   . LEU B 939  ? 0.2502 0.2717 0.3146 -0.0016 -0.0317 -0.0202 937  LEU B N   
15814 C CA  . LEU B 939  ? 0.2964 0.3207 0.3625 -0.0001 -0.0288 -0.0196 937  LEU B CA  
15815 C C   . LEU B 939  ? 0.2751 0.3008 0.3439 -0.0012 -0.0270 -0.0189 937  LEU B C   
15816 O O   . LEU B 939  ? 0.3796 0.4017 0.4454 -0.0019 -0.0265 -0.0193 937  LEU B O   
15817 C CB  . LEU B 939  ? 0.2560 0.2772 0.3167 0.0014  -0.0273 -0.0204 937  LEU B CB  
15818 C CG  . LEU B 939  ? 0.3457 0.3685 0.4065 0.0030  -0.0246 -0.0201 937  LEU B CG  
15819 C CD1 . LEU B 939  ? 0.3269 0.3531 0.3911 0.0040  -0.0250 -0.0194 937  LEU B CD1 
15820 C CD2 . LEU B 939  ? 0.2926 0.3120 0.3476 0.0039  -0.0240 -0.0209 937  LEU B CD2 
15821 N N   . GLN B 940  ? 0.2497 0.2803 0.3238 -0.0012 -0.0259 -0.0177 938  GLN B N   
15822 C CA  . GLN B 940  ? 0.3185 0.3509 0.3955 -0.0026 -0.0244 -0.0168 938  GLN B CA  
15823 C C   . GLN B 940  ? 0.2836 0.3183 0.3616 -0.0012 -0.0212 -0.0162 938  GLN B C   
15824 O O   . GLN B 940  ? 0.3004 0.3363 0.3802 -0.0022 -0.0197 -0.0153 938  GLN B O   
15825 C CB  . GLN B 940  ? 0.4011 0.4378 0.4840 -0.0045 -0.0259 -0.0157 938  GLN B CB  
15826 N N   . ARG B 941  ? 0.2054 0.2405 0.2819 0.0010  -0.0201 -0.0167 939  ARG B N   
15827 C CA  . ARG B 941  ? 0.2383 0.2753 0.3152 0.0023  -0.0172 -0.0163 939  ARG B CA  
15828 C C   . ARG B 941  ? 0.1936 0.2279 0.2659 0.0041  -0.0166 -0.0172 939  ARG B C   
15829 O O   . ARG B 941  ? 0.1962 0.2285 0.2662 0.0046  -0.0183 -0.0179 939  ARG B O   
15830 C CB  . ARG B 941  ? 0.2375 0.2802 0.3198 0.0030  -0.0165 -0.0153 939  ARG B CB  
15831 C CG  . ARG B 941  ? 0.2295 0.2736 0.3127 0.0047  -0.0179 -0.0157 939  ARG B CG  
15832 C CD  . ARG B 941  ? 0.2344 0.2848 0.3235 0.0054  -0.0172 -0.0147 939  ARG B CD  
15833 N NE  . ARG B 941  ? 0.2385 0.2902 0.3286 0.0075  -0.0185 -0.0150 939  ARG B NE  
15834 C CZ  . ARG B 941  ? 0.2521 0.3033 0.3404 0.0101  -0.0173 -0.0155 939  ARG B CZ  
15835 N NH1 . ARG B 941  ? 0.2687 0.3182 0.3542 0.0107  -0.0149 -0.0158 939  ARG B NH1 
15836 N NH2 . ARG B 941  ? 0.2568 0.3092 0.3462 0.0120  -0.0188 -0.0157 939  ARG B NH2 
15837 N N   . GLU B 942  ? 0.2179 0.2521 0.2888 0.0050  -0.0142 -0.0172 940  GLU B N   
15838 C CA  . GLU B 942  ? 0.2099 0.2421 0.2770 0.0064  -0.0135 -0.0179 940  GLU B CA  
15839 C C   . GLU B 942  ? 0.2200 0.2541 0.2886 0.0080  -0.0137 -0.0178 940  GLU B C   
15840 O O   . GLU B 942  ? 0.2332 0.2709 0.3053 0.0087  -0.0125 -0.0172 940  GLU B O   
15841 C CB  . GLU B 942  ? 0.2346 0.2667 0.3001 0.0068  -0.0110 -0.0177 940  GLU B CB  
15842 C CG  . GLU B 942  ? 0.2110 0.2414 0.2728 0.0080  -0.0102 -0.0183 940  GLU B CG  
15843 C CD  . GLU B 942  ? 0.2080 0.2391 0.2690 0.0084  -0.0079 -0.0181 940  GLU B CD  
15844 O OE1 . GLU B 942  ? 0.2418 0.2756 0.3058 0.0085  -0.0066 -0.0175 940  GLU B OE1 
15845 O OE2 . GLU B 942  ? 0.1815 0.2107 0.2390 0.0085  -0.0073 -0.0186 940  GLU B OE2 
15846 N N   . VAL B 943  ? 0.1894 0.2213 0.2555 0.0086  -0.0153 -0.0184 941  VAL B N   
15847 C CA  . VAL B 943  ? 0.1867 0.2194 0.2535 0.0103  -0.0158 -0.0184 941  VAL B CA  
15848 C C   . VAL B 943  ? 0.1899 0.2197 0.2523 0.0112  -0.0147 -0.0188 941  VAL B C   
15849 O O   . VAL B 943  ? 0.1774 0.2039 0.2356 0.0107  -0.0154 -0.0192 941  VAL B O   
15850 C CB  . VAL B 943  ? 0.2106 0.2426 0.2776 0.0102  -0.0187 -0.0185 941  VAL B CB  
15851 C CG1 . VAL B 943  ? 0.2062 0.2387 0.2737 0.0123  -0.0194 -0.0184 941  VAL B CG1 
15852 C CG2 . VAL B 943  ? 0.2345 0.2695 0.3060 0.0089  -0.0199 -0.0180 941  VAL B CG2 
15853 N N   . PHE B 944  ? 0.1696 0.2008 0.2328 0.0125  -0.0130 -0.0187 942  PHE B N   
15854 C CA  . PHE B 944  ? 0.1776 0.2062 0.2368 0.0129  -0.0117 -0.0191 942  PHE B CA  
15855 C C   . PHE B 944  ? 0.1784 0.2046 0.2352 0.0143  -0.0127 -0.0194 942  PHE B C   
15856 O O   . PHE B 944  ? 0.1925 0.2187 0.2494 0.0159  -0.0120 -0.0196 942  PHE B O   
15857 C CB  . PHE B 944  ? 0.1728 0.2037 0.2335 0.0134  -0.0093 -0.0190 942  PHE B CB  
15858 C CG  . PHE B 944  ? 0.1744 0.2032 0.2313 0.0130  -0.0079 -0.0193 942  PHE B CG  
15859 C CD1 . PHE B 944  ? 0.1715 0.1995 0.2268 0.0116  -0.0076 -0.0193 942  PHE B CD1 
15860 C CD2 . PHE B 944  ? 0.1773 0.2048 0.2321 0.0143  -0.0071 -0.0197 942  PHE B CD2 
15861 C CE1 . PHE B 944  ? 0.1759 0.2025 0.2279 0.0113  -0.0064 -0.0195 942  PHE B CE1 
15862 C CE2 . PHE B 944  ? 0.1864 0.2121 0.2377 0.0137  -0.0060 -0.0199 942  PHE B CE2 
15863 C CZ  . PHE B 944  ? 0.2028 0.2285 0.2530 0.0121  -0.0057 -0.0198 942  PHE B CZ  
15864 N N   . GLY B 945  ? 0.1662 0.1896 0.2204 0.0136  -0.0146 -0.0195 943  GLY B N   
15865 C CA  . GLY B 945  ? 0.1835 0.2040 0.2352 0.0147  -0.0159 -0.0196 943  GLY B CA  
15866 C C   . GLY B 945  ? 0.1906 0.2079 0.2383 0.0134  -0.0175 -0.0196 943  GLY B C   
15867 O O   . GLY B 945  ? 0.1931 0.2106 0.2400 0.0119  -0.0173 -0.0197 943  GLY B O   
15868 N N   . PRO B 946  ? 0.1939 0.2082 0.2390 0.0141  -0.0191 -0.0195 944  PRO B N   
15869 C CA  . PRO B 946  ? 0.2001 0.2110 0.2406 0.0128  -0.0203 -0.0194 944  PRO B CA  
15870 C C   . PRO B 946  ? 0.1902 0.2017 0.2318 0.0125  -0.0224 -0.0193 944  PRO B C   
15871 O O   . PRO B 946  ? 0.2157 0.2249 0.2553 0.0129  -0.0244 -0.0190 944  PRO B O   
15872 C CB  . PRO B 946  ? 0.1842 0.1912 0.2214 0.0138  -0.0212 -0.0192 944  PRO B CB  
15873 C CG  . PRO B 946  ? 0.2025 0.2113 0.2435 0.0162  -0.0217 -0.0193 944  PRO B CG  
15874 C CD  . PRO B 946  ? 0.2053 0.2187 0.2509 0.0163  -0.0196 -0.0195 944  PRO B CD  
15875 N N   . VAL B 947  ? 0.1898 0.2041 0.2342 0.0117  -0.0220 -0.0195 945  VAL B N   
15876 C CA  . VAL B 947  ? 0.1914 0.2066 0.2374 0.0113  -0.0240 -0.0195 945  VAL B CA  
15877 C C   . VAL B 947  ? 0.2213 0.2356 0.2649 0.0096  -0.0237 -0.0199 945  VAL B C   
15878 O O   . VAL B 947  ? 0.2067 0.2227 0.2521 0.0090  -0.0222 -0.0201 945  VAL B O   
15879 C CB  . VAL B 947  ? 0.2031 0.2224 0.2551 0.0118  -0.0243 -0.0193 945  VAL B CB  
15880 C CG1 . VAL B 947  ? 0.2076 0.2275 0.2609 0.0112  -0.0268 -0.0193 945  VAL B CG1 
15881 C CG2 . VAL B 947  ? 0.2222 0.2428 0.2766 0.0139  -0.0242 -0.0190 945  VAL B CG2 
15882 N N   . LEU B 948  ? 0.1871 0.1985 0.2263 0.0090  -0.0250 -0.0200 946  LEU B N   
15883 C CA  . LEU B 948  ? 0.1949 0.2053 0.2313 0.0078  -0.0248 -0.0205 946  LEU B CA  
15884 C C   . LEU B 948  ? 0.1956 0.2059 0.2328 0.0075  -0.0270 -0.0208 946  LEU B C   
15885 O O   . LEU B 948  ? 0.2196 0.2290 0.2564 0.0078  -0.0293 -0.0205 946  LEU B O   
15886 C CB  . LEU B 948  ? 0.1975 0.2050 0.2282 0.0074  -0.0248 -0.0203 946  LEU B CB  
15887 C CG  . LEU B 948  ? 0.1907 0.1974 0.2180 0.0065  -0.0244 -0.0209 946  LEU B CG  
15888 C CD1 . LEU B 948  ? 0.1913 0.1999 0.2199 0.0063  -0.0220 -0.0213 946  LEU B CD1 
15889 C CD2 . LEU B 948  ? 0.2504 0.2548 0.2723 0.0059  -0.0244 -0.0205 946  LEU B CD2 
15890 N N   . HIS B 949  ? 0.1816 0.1927 0.2200 0.0067  -0.0266 -0.0213 947  HIS B N   
15891 C CA  . HIS B 949  ? 0.1881 0.1987 0.2268 0.0061  -0.0288 -0.0218 947  HIS B CA  
15892 C C   . HIS B 949  ? 0.2042 0.2118 0.2373 0.0056  -0.0290 -0.0225 947  HIS B C   
15893 O O   . HIS B 949  ? 0.2214 0.2286 0.2522 0.0056  -0.0269 -0.0228 947  HIS B O   
15894 C CB  . HIS B 949  ? 0.2157 0.2284 0.2588 0.0054  -0.0284 -0.0219 947  HIS B CB  
15895 C CG  . HIS B 949  ? 0.1885 0.2047 0.2371 0.0060  -0.0278 -0.0211 947  HIS B CG  
15896 N ND1 . HIS B 949  ? 0.1916 0.2093 0.2414 0.0066  -0.0252 -0.0208 947  HIS B ND1 
15897 C CD2 . HIS B 949  ? 0.1897 0.2084 0.2425 0.0062  -0.0294 -0.0206 947  HIS B CD2 
15898 C CE1 . HIS B 949  ? 0.1819 0.2027 0.2363 0.0072  -0.0251 -0.0201 947  HIS B CE1 
15899 N NE2 . HIS B 949  ? 0.1931 0.2149 0.2497 0.0070  -0.0276 -0.0200 947  HIS B NE2 
15900 N N   . VAL B 950  ? 0.2087 0.2144 0.2396 0.0053  -0.0315 -0.0229 948  VAL B N   
15901 C CA  . VAL B 950  ? 0.2278 0.2307 0.2529 0.0051  -0.0318 -0.0236 948  VAL B CA  
15902 C C   . VAL B 950  ? 0.2221 0.2235 0.2468 0.0044  -0.0336 -0.0246 948  VAL B C   
15903 O O   . VAL B 950  ? 0.2219 0.2237 0.2491 0.0040  -0.0361 -0.0245 948  VAL B O   
15904 C CB  . VAL B 950  ? 0.2364 0.2373 0.2574 0.0053  -0.0331 -0.0231 948  VAL B CB  
15905 C CG1 . VAL B 950  ? 0.2755 0.2738 0.2905 0.0051  -0.0335 -0.0239 948  VAL B CG1 
15906 C CG2 . VAL B 950  ? 0.2579 0.2594 0.2784 0.0057  -0.0313 -0.0222 948  VAL B CG2 
15907 N N   . ILE B 951  ? 0.2096 0.2094 0.2311 0.0045  -0.0324 -0.0255 949  ILE B N   
15908 C CA  . ILE B 951  ? 0.2187 0.2160 0.2384 0.0040  -0.0340 -0.0267 949  ILE B CA  
15909 C C   . ILE B 951  ? 0.2274 0.2220 0.2403 0.0046  -0.0339 -0.0276 949  ILE B C   
15910 O O   . ILE B 951  ? 0.2343 0.2296 0.2447 0.0053  -0.0315 -0.0275 949  ILE B O   
15911 C CB  . ILE B 951  ? 0.2599 0.2575 0.2817 0.0039  -0.0325 -0.0271 949  ILE B CB  
15912 C CG1 . ILE B 951  ? 0.3115 0.3119 0.3400 0.0032  -0.0327 -0.0262 949  ILE B CG1 
15913 C CG2 . ILE B 951  ? 0.3493 0.3432 0.3675 0.0038  -0.0338 -0.0285 949  ILE B CG2 
15914 C CD1 . ILE B 951  ? 0.4162 0.4166 0.4466 0.0029  -0.0313 -0.0264 949  ILE B CD1 
15915 N N   . ARG B 952  ? 0.2227 0.2145 0.2325 0.0043  -0.0365 -0.0284 950  ARG B N   
15916 C CA  A ARG B 952  ? 0.2557 0.2447 0.2586 0.0050  -0.0365 -0.0295 950  ARG B CA  
15917 C CA  B ARG B 952  ? 0.2559 0.2448 0.2587 0.0050  -0.0365 -0.0295 950  ARG B CA  
15918 C C   . ARG B 952  ? 0.2460 0.2322 0.2470 0.0052  -0.0368 -0.0310 950  ARG B C   
15919 O O   . ARG B 952  ? 0.2987 0.2839 0.3026 0.0042  -0.0386 -0.0313 950  ARG B O   
15920 C CB  A ARG B 952  ? 0.2497 0.2368 0.2494 0.0046  -0.0394 -0.0294 950  ARG B CB  
15921 C CB  B ARG B 952  ? 0.2504 0.2373 0.2500 0.0045  -0.0396 -0.0295 950  ARG B CB  
15922 C CG  A ARG B 952  ? 0.2765 0.2655 0.2776 0.0045  -0.0395 -0.0278 950  ARG B CG  
15923 C CG  B ARG B 952  ? 0.2893 0.2775 0.2883 0.0046  -0.0394 -0.0281 950  ARG B CG  
15924 C CD  A ARG B 952  ? 0.3083 0.2958 0.3083 0.0041  -0.0430 -0.0276 950  ARG B CD  
15925 C CD  B ARG B 952  ? 0.3123 0.2983 0.3085 0.0043  -0.0429 -0.0281 950  ARG B CD  
15926 N NE  A ARG B 952  ? 0.3528 0.3418 0.3544 0.0042  -0.0432 -0.0260 950  ARG B NE  
15927 N NE  B ARG B 952  ? 0.3244 0.3103 0.3178 0.0045  -0.0428 -0.0269 950  ARG B NE  
15928 C CZ  A ARG B 952  ? 0.3456 0.3331 0.3424 0.0045  -0.0435 -0.0254 950  ARG B CZ  
15929 C CZ  B ARG B 952  ? 0.3458 0.3336 0.3428 0.0045  -0.0428 -0.0254 950  ARG B CZ  
15930 N NH1 A ARG B 952  ? 0.2963 0.2813 0.2865 0.0046  -0.0433 -0.0261 950  ARG B NH1 
15931 N NH1 B ARG B 952  ? 0.3607 0.3511 0.3643 0.0045  -0.0426 -0.0250 950  ARG B NH1 
15932 N NH2 A ARG B 952  ? 0.3564 0.3447 0.3549 0.0047  -0.0440 -0.0239 950  ARG B NH2 
15933 N NH2 B ARG B 952  ? 0.3526 0.3394 0.3461 0.0046  -0.0430 -0.0243 950  ARG B NH2 
15934 N N   . TYR B 953  ? 0.2398 0.2248 0.2360 0.0065  -0.0349 -0.0320 951  TYR B N   
15935 C CA  . TYR B 953  ? 0.2367 0.2185 0.2307 0.0071  -0.0351 -0.0336 951  TYR B CA  
15936 C C   . TYR B 953  ? 0.2541 0.2332 0.2406 0.0085  -0.0349 -0.0350 951  TYR B C   
15937 O O   . TYR B 953  ? 0.2661 0.2469 0.2496 0.0091  -0.0333 -0.0346 951  TYR B O   
15938 C CB  . TYR B 953  ? 0.2633 0.2468 0.2604 0.0077  -0.0325 -0.0334 951  TYR B CB  
15939 C CG  . TYR B 953  ? 0.2264 0.2123 0.2213 0.0093  -0.0292 -0.0333 951  TYR B CG  
15940 C CD1 . TYR B 953  ? 0.2153 0.2053 0.2127 0.0089  -0.0275 -0.0318 951  TYR B CD1 
15941 C CD2 . TYR B 953  ? 0.2402 0.2244 0.2304 0.0111  -0.0280 -0.0347 951  TYR B CD2 
15942 C CE1 . TYR B 953  ? 0.2279 0.2204 0.2234 0.0100  -0.0247 -0.0316 951  TYR B CE1 
15943 C CE2 . TYR B 953  ? 0.2447 0.2319 0.2332 0.0125  -0.0251 -0.0345 951  TYR B CE2 
15944 C CZ  . TYR B 953  ? 0.2383 0.2298 0.2296 0.0117  -0.0235 -0.0329 951  TYR B CZ  
15945 O OH  . TYR B 953  ? 0.2341 0.2289 0.2239 0.0127  -0.0207 -0.0326 951  TYR B OH  
15946 N N   . ARG B 954  ? 0.2832 0.2579 0.2664 0.0089  -0.0365 -0.0367 952  ARG B N   
15947 C CA  . ARG B 954  ? 0.3346 0.3064 0.3104 0.0107  -0.0360 -0.0384 952  ARG B CA  
15948 C C   . ARG B 954  ? 0.3076 0.2803 0.2829 0.0127  -0.0329 -0.0390 952  ARG B C   
15949 O O   . ARG B 954  ? 0.3043 0.2767 0.2835 0.0125  -0.0326 -0.0389 952  ARG B O   
15950 C CB  . ARG B 954  ? 0.3591 0.3250 0.3310 0.0103  -0.0394 -0.0402 952  ARG B CB  
15951 N N   . ARG B 955  ? 0.3265 0.3003 0.2970 0.0146  -0.0307 -0.0396 953  ARG B N   
15952 C CA  . ARG B 955  ? 0.3514 0.3270 0.3217 0.0167  -0.0276 -0.0400 953  ARG B CA  
15953 C C   . ARG B 955  ? 0.3217 0.2926 0.2910 0.0179  -0.0286 -0.0417 953  ARG B C   
15954 O O   . ARG B 955  ? 0.3287 0.3009 0.3008 0.0189  -0.0268 -0.0415 953  ARG B O   
15955 C CB  . ARG B 955  ? 0.3902 0.3678 0.3551 0.0186  -0.0254 -0.0405 953  ARG B CB  
15956 C CG  . ARG B 955  ? 0.4484 0.4290 0.4134 0.0211  -0.0221 -0.0409 953  ARG B CG  
15957 C CD  . ARG B 955  ? 0.4135 0.3985 0.3855 0.0201  -0.0205 -0.0391 953  ARG B CD  
15958 N NE  . ARG B 955  ? 0.4109 0.3992 0.3830 0.0224  -0.0175 -0.0394 953  ARG B NE  
15959 C CZ  . ARG B 955  ? 0.4296 0.4153 0.4009 0.0246  -0.0173 -0.0407 953  ARG B CZ  
15960 N NH1 . ARG B 955  ? 0.4505 0.4301 0.4207 0.0245  -0.0199 -0.0419 953  ARG B NH1 
15961 N NH2 . ARG B 955  ? 0.4003 0.3898 0.3719 0.0268  -0.0146 -0.0408 953  ARG B NH2 
15962 N N   . ASP B 956  ? 0.3224 0.2875 0.2875 0.0178  -0.0314 -0.0433 954  ASP B N   
15963 C CA  A ASP B 956  ? 0.3604 0.3200 0.3238 0.0187  -0.0327 -0.0449 954  ASP B CA  
15964 C CA  B ASP B 956  ? 0.3602 0.3200 0.3238 0.0187  -0.0326 -0.0449 954  ASP B CA  
15965 C C   . ASP B 956  ? 0.3554 0.3149 0.3255 0.0166  -0.0337 -0.0437 954  ASP B C   
15966 O O   . ASP B 956  ? 0.4027 0.3583 0.3724 0.0172  -0.0341 -0.0446 954  ASP B O   
15967 C CB  A ASP B 956  ? 0.3734 0.3265 0.3307 0.0186  -0.0359 -0.0469 954  ASP B CB  
15968 C CB  B ASP B 956  ? 0.3761 0.3291 0.3327 0.0191  -0.0355 -0.0471 954  ASP B CB  
15969 C CG  A ASP B 956  ? 0.4356 0.3880 0.3853 0.0212  -0.0346 -0.0484 954  ASP B CG  
15970 C CG  B ASP B 956  ? 0.3680 0.3196 0.3256 0.0162  -0.0390 -0.0466 954  ASP B CG  
15971 O OD1 A ASP B 956  ? 0.4315 0.3874 0.3803 0.0237  -0.0313 -0.0484 954  ASP B OD1 
15972 O OD1 B ASP B 956  ? 0.4130 0.3678 0.3772 0.0137  -0.0396 -0.0447 954  ASP B OD1 
15973 O OD2 A ASP B 956  ? 0.4693 0.4179 0.4138 0.0209  -0.0370 -0.0496 954  ASP B OD2 
15974 O OD2 B ASP B 956  ? 0.4484 0.3955 0.3998 0.0164  -0.0411 -0.0482 954  ASP B OD2 
15975 N N   . ASP B 957  ? 0.3097 0.2732 0.2856 0.0142  -0.0340 -0.0418 955  ASP B N   
15976 C CA  . ASP B 957  ? 0.3379 0.3023 0.3204 0.0121  -0.0347 -0.0404 955  ASP B CA  
15977 C C   . ASP B 957  ? 0.2756 0.2453 0.2629 0.0127  -0.0315 -0.0389 955  ASP B C   
15978 O O   . ASP B 957  ? 0.2881 0.2598 0.2812 0.0110  -0.0316 -0.0375 955  ASP B O   
15979 C CB  . ASP B 957  ? 0.3505 0.3162 0.3367 0.0093  -0.0372 -0.0393 955  ASP B CB  
15980 C CG  . ASP B 957  ? 0.4563 0.4167 0.4391 0.0081  -0.0410 -0.0406 955  ASP B CG  
15981 O OD1 . ASP B 957  ? 0.4802 0.4351 0.4592 0.0088  -0.0421 -0.0422 955  ASP B OD1 
15982 O OD2 . ASP B 957  ? 0.4883 0.4499 0.4720 0.0066  -0.0430 -0.0400 955  ASP B OD2 
15983 N N   . LEU B 958  ? 0.2730 0.2454 0.2580 0.0149  -0.0287 -0.0391 956  LEU B N   
15984 C CA  . LEU B 958  ? 0.2506 0.2284 0.2399 0.0152  -0.0258 -0.0376 956  LEU B CA  
15985 C C   . LEU B 958  ? 0.2448 0.2216 0.2375 0.0152  -0.0254 -0.0373 956  LEU B C   
15986 O O   . LEU B 958  ? 0.2392 0.2193 0.2373 0.0140  -0.0246 -0.0357 956  LEU B O   
15987 C CB  . LEU B 958  ? 0.2579 0.2385 0.2438 0.0177  -0.0230 -0.0381 956  LEU B CB  
15988 C CG  . LEU B 958  ? 0.2414 0.2276 0.2313 0.0181  -0.0201 -0.0367 956  LEU B CG  
15989 C CD1 . LEU B 958  ? 0.2755 0.2654 0.2702 0.0157  -0.0201 -0.0348 956  LEU B CD1 
15990 C CD2 . LEU B 958  ? 0.2871 0.2763 0.2734 0.0203  -0.0177 -0.0372 956  LEU B CD2 
15991 N N   . ASP B 959  ? 0.2518 0.2236 0.2411 0.0167  -0.0261 -0.0388 957  ASP B N   
15992 C CA  . ASP B 959  ? 0.2443 0.2147 0.2363 0.0167  -0.0258 -0.0383 957  ASP B CA  
15993 C C   . ASP B 959  ? 0.2476 0.2174 0.2446 0.0135  -0.0277 -0.0370 957  ASP B C   
15994 O O   . ASP B 959  ? 0.2485 0.2208 0.2502 0.0127  -0.0266 -0.0356 957  ASP B O   
15995 C CB  . ASP B 959  ? 0.2594 0.2235 0.2461 0.0189  -0.0265 -0.0402 957  ASP B CB  
15996 C CG  . ASP B 959  ? 0.2753 0.2387 0.2639 0.0199  -0.0253 -0.0396 957  ASP B CG  
15997 O OD1 . ASP B 959  ? 0.2663 0.2351 0.2577 0.0209  -0.0227 -0.0385 957  ASP B OD1 
15998 O OD2 . ASP B 959  ? 0.2968 0.2542 0.2838 0.0197  -0.0271 -0.0402 957  ASP B OD2 
15999 N N   . ARG B 960  ? 0.2428 0.2098 0.2389 0.0117  -0.0306 -0.0375 958  ARG B N   
16000 C CA  . ARG B 960  ? 0.2362 0.2037 0.2374 0.0086  -0.0324 -0.0362 958  ARG B CA  
16001 C C   . ARG B 960  ? 0.2440 0.2182 0.2509 0.0076  -0.0310 -0.0343 958  ARG B C   
16002 O O   . ARG B 960  ? 0.2426 0.2190 0.2548 0.0058  -0.0309 -0.0329 958  ARG B O   
16003 C CB  . ARG B 960  ? 0.2826 0.2463 0.2815 0.0069  -0.0359 -0.0371 958  ARG B CB  
16004 N N   . LEU B 961  ? 0.2144 0.1917 0.2198 0.0086  -0.0298 -0.0343 959  LEU B N   
16005 C CA  . LEU B 961  ? 0.2149 0.1979 0.2250 0.0078  -0.0284 -0.0327 959  LEU B CA  
16006 C C   . LEU B 961  ? 0.2239 0.2099 0.2373 0.0084  -0.0258 -0.0317 959  LEU B C   
16007 O O   . LEU B 961  ? 0.2132 0.2024 0.2317 0.0072  -0.0253 -0.0302 959  LEU B O   
16008 C CB  . LEU B 961  ? 0.2181 0.2031 0.2251 0.0088  -0.0276 -0.0329 959  LEU B CB  
16009 C CG  . LEU B 961  ? 0.2214 0.2114 0.2322 0.0082  -0.0261 -0.0313 959  LEU B CG  
16010 C CD1 . LEU B 961  ? 0.2883 0.2794 0.3036 0.0063  -0.0281 -0.0303 959  LEU B CD1 
16011 C CD2 . LEU B 961  ? 0.2483 0.2397 0.2554 0.0091  -0.0252 -0.0314 959  LEU B CD2 
16012 N N   . VAL B 962  ? 0.2096 0.1946 0.2200 0.0105  -0.0241 -0.0324 960  VAL B N   
16013 C CA  . VAL B 962  ? 0.2128 0.2004 0.2260 0.0111  -0.0218 -0.0315 960  VAL B CA  
16014 C C   . VAL B 962  ? 0.2240 0.2101 0.2409 0.0095  -0.0227 -0.0306 960  VAL B C   
16015 O O   . VAL B 962  ? 0.2268 0.2161 0.2480 0.0088  -0.0215 -0.0292 960  VAL B O   
16016 C CB  . VAL B 962  ? 0.2250 0.2118 0.2343 0.0139  -0.0201 -0.0325 960  VAL B CB  
16017 C CG1 . VAL B 962  ? 0.2450 0.2339 0.2571 0.0145  -0.0182 -0.0315 960  VAL B CG1 
16018 C CG2 . VAL B 962  ? 0.2528 0.2427 0.2595 0.0151  -0.0188 -0.0328 960  VAL B CG2 
16019 N N   . ASP B 963  ? 0.2191 0.2000 0.2340 0.0089  -0.0250 -0.0315 961  ASP B N   
16020 C CA  . ASP B 963  ? 0.2483 0.2277 0.2667 0.0068  -0.0261 -0.0305 961  ASP B CA  
16021 C C   . ASP B 963  ? 0.2384 0.2221 0.2624 0.0045  -0.0265 -0.0290 961  ASP B C   
16022 O O   . ASP B 963  ? 0.2409 0.2269 0.2692 0.0033  -0.0257 -0.0276 961  ASP B O   
16023 C CB  . ASP B 963  ? 0.2762 0.2492 0.2915 0.0058  -0.0290 -0.0316 961  ASP B CB  
16024 C CG  . ASP B 963  ? 0.3477 0.3155 0.3580 0.0079  -0.0288 -0.0329 961  ASP B CG  
16025 O OD1 . ASP B 963  ? 0.3303 0.2997 0.3405 0.0099  -0.0265 -0.0326 961  ASP B OD1 
16026 O OD2 . ASP B 963  ? 0.3517 0.3136 0.3581 0.0077  -0.0312 -0.0343 961  ASP B OD2 
16027 N N   . ASP B 964  ? 0.2197 0.2047 0.2435 0.0040  -0.0278 -0.0293 962  ASP B N   
16028 C CA  . ASP B 964  ? 0.2367 0.2258 0.2657 0.0022  -0.0284 -0.0280 962  ASP B CA  
16029 C C   . ASP B 964  ? 0.2241 0.2183 0.2564 0.0029  -0.0257 -0.0268 962  ASP B C   
16030 O O   . ASP B 964  ? 0.2288 0.2261 0.2661 0.0017  -0.0253 -0.0255 962  ASP B O   
16031 C CB  . ASP B 964  ? 0.2320 0.2211 0.2594 0.0020  -0.0303 -0.0286 962  ASP B CB  
16032 C CG  . ASP B 964  ? 0.2713 0.2558 0.2961 0.0008  -0.0334 -0.0297 962  ASP B CG  
16033 O OD1 . ASP B 964  ? 0.3091 0.2904 0.3341 -0.0003 -0.0343 -0.0298 962  ASP B OD1 
16034 O OD2 . ASP B 964  ? 0.3668 0.3504 0.3890 0.0009  -0.0351 -0.0304 962  ASP B OD2 
16035 N N   . VAL B 965  ? 0.2006 0.1958 0.2302 0.0048  -0.0237 -0.0272 963  VAL B N   
16036 C CA  . VAL B 965  ? 0.1812 0.1807 0.2134 0.0054  -0.0213 -0.0261 963  VAL B CA  
16037 C C   . VAL B 965  ? 0.2005 0.2004 0.2352 0.0051  -0.0200 -0.0253 963  VAL B C   
16038 O O   . VAL B 965  ? 0.2016 0.2047 0.2404 0.0044  -0.0190 -0.0241 963  VAL B O   
16039 C CB  . VAL B 965  ? 0.1911 0.1915 0.2197 0.0072  -0.0196 -0.0267 963  VAL B CB  
16040 C CG1 . VAL B 965  ? 0.2000 0.2043 0.2311 0.0075  -0.0173 -0.0257 963  VAL B CG1 
16041 C CG2 . VAL B 965  ? 0.2246 0.2248 0.2507 0.0071  -0.0207 -0.0273 963  VAL B CG2 
16042 N N   . ASN B 966  ? 0.2012 0.1974 0.2332 0.0058  -0.0201 -0.0259 964  ASN B N   
16043 C CA  . ASN B 966  ? 0.2062 0.2022 0.2400 0.0057  -0.0190 -0.0250 964  ASN B CA  
16044 C C   . ASN B 966  ? 0.2033 0.1995 0.2412 0.0033  -0.0202 -0.0239 964  ASN B C   
16045 O O   . ASN B 966  ? 0.2274 0.2253 0.2682 0.0027  -0.0189 -0.0226 964  ASN B O   
16046 C CB  . ASN B 966  ? 0.2176 0.2090 0.2472 0.0071  -0.0191 -0.0260 964  ASN B CB  
16047 C CG  . ASN B 966  ? 0.2136 0.2061 0.2399 0.0097  -0.0174 -0.0268 964  ASN B CG  
16048 O OD1 . ASN B 966  ? 0.2215 0.2184 0.2493 0.0102  -0.0157 -0.0263 964  ASN B OD1 
16049 N ND2 . ASN B 966  ? 0.2287 0.2172 0.2506 0.0114  -0.0179 -0.0281 964  ASN B ND2 
16050 N N   . ALA B 967  ? 0.1983 0.1928 0.2364 0.0018  -0.0226 -0.0243 965  ALA B N   
16051 C CA  . ALA B 967  ? 0.2274 0.2220 0.2693 -0.0008 -0.0241 -0.0233 965  ALA B CA  
16052 C C   . ALA B 967  ? 0.2145 0.2149 0.2621 -0.0017 -0.0230 -0.0217 965  ALA B C   
16053 O O   . ALA B 967  ? 0.2394 0.2410 0.2908 -0.0038 -0.0236 -0.0205 965  ALA B O   
16054 C CB  . ALA B 967  ? 0.2398 0.2315 0.2805 -0.0022 -0.0272 -0.0242 965  ALA B CB  
16055 N N   . THR B 968  ? 0.2010 0.2050 0.2491 -0.0003 -0.0214 -0.0217 966  THR B N   
16056 C CA  . THR B 968  ? 0.2070 0.2163 0.2601 -0.0008 -0.0203 -0.0204 966  THR B CA  
16057 C C   . THR B 968  ? 0.2152 0.2257 0.2702 -0.0010 -0.0182 -0.0192 966  THR B C   
16058 O O   . THR B 968  ? 0.2290 0.2435 0.2883 -0.0018 -0.0174 -0.0180 966  THR B O   
16059 C CB  . THR B 968  ? 0.1905 0.2023 0.2430 0.0009  -0.0191 -0.0207 966  THR B CB  
16060 O OG1 . THR B 968  ? 0.1994 0.2110 0.2494 0.0024  -0.0170 -0.0209 966  THR B OG1 
16061 C CG2 . THR B 968  ? 0.2233 0.2334 0.2730 0.0012  -0.0210 -0.0218 966  THR B CG2 
16062 N N   . GLY B 969  ? 0.1985 0.2060 0.2502 0.0000  -0.0173 -0.0195 967  GLY B N   
16063 C CA  . GLY B 969  ? 0.2060 0.2145 0.2587 0.0001  -0.0153 -0.0184 967  GLY B CA  
16064 C C   . GLY B 969  ? 0.2054 0.2168 0.2576 0.0019  -0.0130 -0.0184 967  GLY B C   
16065 O O   . GLY B 969  ? 0.2033 0.2149 0.2553 0.0024  -0.0114 -0.0177 967  GLY B O   
16066 N N   . TYR B 970  ? 0.1915 0.2047 0.2433 0.0028  -0.0130 -0.0191 968  TYR B N   
16067 C CA  . TYR B 970  ? 0.1804 0.1958 0.2312 0.0043  -0.0111 -0.0192 968  TYR B CA  
16068 C C   . TYR B 970  ? 0.1793 0.1924 0.2256 0.0058  -0.0108 -0.0202 968  TYR B C   
16069 O O   . TYR B 970  ? 0.2100 0.2198 0.2539 0.0059  -0.0121 -0.0211 968  TYR B O   
16070 C CB  . TYR B 970  ? 0.1849 0.2027 0.2368 0.0045  -0.0113 -0.0194 968  TYR B CB  
16071 C CG  . TYR B 970  ? 0.2079 0.2290 0.2643 0.0037  -0.0110 -0.0184 968  TYR B CG  
16072 C CD1 . TYR B 970  ? 0.2230 0.2467 0.2808 0.0042  -0.0090 -0.0176 968  TYR B CD1 
16073 C CD2 . TYR B 970  ? 0.2275 0.2495 0.2867 0.0027  -0.0127 -0.0182 968  TYR B CD2 
16074 C CE1 . TYR B 970  ? 0.2589 0.2859 0.3206 0.0039  -0.0084 -0.0168 968  TYR B CE1 
16075 C CE2 . TYR B 970  ? 0.2639 0.2897 0.3275 0.0023  -0.0122 -0.0172 968  TYR B CE2 
16076 C CZ  . TYR B 970  ? 0.2789 0.3072 0.3436 0.0030  -0.0099 -0.0166 968  TYR B CZ  
16077 O OH  . TYR B 970  ? 0.3736 0.4059 0.4424 0.0030  -0.0091 -0.0157 968  TYR B OH  
16078 N N   . GLY B 971  ? 0.1729 0.1880 0.2183 0.0069  -0.0092 -0.0202 969  GLY B N   
16079 C CA  . GLY B 971  ? 0.1830 0.1971 0.2248 0.0083  -0.0087 -0.0210 969  GLY B CA  
16080 C C   . GLY B 971  ? 0.1528 0.1700 0.1943 0.0091  -0.0071 -0.0208 969  GLY B C   
16081 O O   . GLY B 971  ? 0.1607 0.1784 0.2011 0.0100  -0.0059 -0.0206 969  GLY B O   
16082 N N   . LEU B 972  ? 0.1435 0.1624 0.1856 0.0086  -0.0071 -0.0208 970  LEU B N   
16083 C CA  . LEU B 972  ? 0.1549 0.1763 0.1967 0.0090  -0.0058 -0.0206 970  LEU B CA  
16084 C C   . LEU B 972  ? 0.1437 0.1653 0.1824 0.0094  -0.0058 -0.0213 970  LEU B C   
16085 O O   . LEU B 972  ? 0.1672 0.1894 0.2042 0.0103  -0.0051 -0.0215 970  LEU B O   
16086 C CB  . LEU B 972  ? 0.1683 0.1911 0.2125 0.0083  -0.0056 -0.0201 970  LEU B CB  
16087 C CG  . LEU B 972  ? 0.1582 0.1830 0.2018 0.0085  -0.0044 -0.0199 970  LEU B CG  
16088 C CD1 . LEU B 972  ? 0.1912 0.2169 0.2346 0.0090  -0.0031 -0.0194 970  LEU B CD1 
16089 C CD2 . LEU B 972  ? 0.1963 0.2218 0.2420 0.0082  -0.0043 -0.0195 970  LEU B CD2 
16090 N N   . THR B 973  ? 0.1501 0.1716 0.1882 0.0088  -0.0066 -0.0215 971  THR B N   
16091 C CA  . THR B 973  ? 0.1490 0.1708 0.1841 0.0090  -0.0066 -0.0220 971  THR B CA  
16092 C C   . THR B 973  ? 0.1380 0.1576 0.1714 0.0091  -0.0080 -0.0227 971  THR B C   
16093 O O   . THR B 973  ? 0.1581 0.1758 0.1927 0.0086  -0.0093 -0.0228 971  THR B O   
16094 C CB  . THR B 973  ? 0.1482 0.1711 0.1829 0.0082  -0.0064 -0.0216 971  THR B CB  
16095 O OG1 . THR B 973  ? 0.1517 0.1732 0.1876 0.0077  -0.0077 -0.0215 971  THR B OG1 
16096 C CG2 . THR B 973  ? 0.1807 0.2055 0.2164 0.0081  -0.0051 -0.0211 971  THR B CG2 
16097 N N   . PHE B 974  ? 0.1533 0.1731 0.1836 0.0096  -0.0077 -0.0232 972  PHE B N   
16098 C CA  . PHE B 974  ? 0.1559 0.1736 0.1837 0.0099  -0.0089 -0.0240 972  PHE B CA  
16099 C C   . PHE B 974  ? 0.1502 0.1695 0.1748 0.0100  -0.0082 -0.0242 972  PHE B C   
16100 O O   . PHE B 974  ? 0.1573 0.1791 0.1813 0.0107  -0.0067 -0.0241 972  PHE B O   
16101 C CB  . PHE B 974  ? 0.1499 0.1656 0.1769 0.0111  -0.0092 -0.0248 972  PHE B CB  
16102 C CG  . PHE B 974  ? 0.1529 0.1661 0.1764 0.0116  -0.0103 -0.0259 972  PHE B CG  
16103 C CD1 . PHE B 974  ? 0.1870 0.1975 0.2106 0.0108  -0.0123 -0.0262 972  PHE B CD1 
16104 C CD2 . PHE B 974  ? 0.1639 0.1780 0.1842 0.0130  -0.0093 -0.0265 972  PHE B CD2 
16105 C CE1 . PHE B 974  ? 0.1816 0.1896 0.2015 0.0112  -0.0134 -0.0272 972  PHE B CE1 
16106 C CE2 . PHE B 974  ? 0.1915 0.2034 0.2082 0.0136  -0.0102 -0.0276 972  PHE B CE2 
16107 C CZ  . PHE B 974  ? 0.1907 0.1992 0.2069 0.0127  -0.0123 -0.0280 972  PHE B CZ  
16108 N N   . GLY B 975  ? 0.1645 0.1824 0.1870 0.0095  -0.0093 -0.0244 973  GLY B N   
16109 C CA  . GLY B 975  ? 0.1551 0.1743 0.1743 0.0094  -0.0087 -0.0244 973  GLY B CA  
16110 C C   . GLY B 975  ? 0.1720 0.1893 0.1877 0.0103  -0.0094 -0.0255 973  GLY B C   
16111 O O   . GLY B 975  ? 0.1842 0.1983 0.1998 0.0103  -0.0111 -0.0260 973  GLY B O   
16112 N N   . LEU B 976  ? 0.1700 0.1894 0.1829 0.0109  -0.0082 -0.0257 974  LEU B N   
16113 C CA  . LEU B 976  ? 0.1924 0.2103 0.2013 0.0119  -0.0087 -0.0267 974  LEU B CA  
16114 C C   . LEU B 976  ? 0.1937 0.2142 0.1998 0.0111  -0.0076 -0.0261 974  LEU B C   
16115 O O   . LEU B 976  ? 0.1871 0.2117 0.1938 0.0110  -0.0059 -0.0255 974  LEU B O   
16116 C CB  . LEU B 976  ? 0.2060 0.2238 0.2138 0.0141  -0.0079 -0.0278 974  LEU B CB  
16117 C CG  . LEU B 976  ? 0.2189 0.2353 0.2220 0.0156  -0.0080 -0.0291 974  LEU B CG  
16118 C CD1 . LEU B 976  ? 0.2484 0.2597 0.2499 0.0151  -0.0104 -0.0298 974  LEU B CD1 
16119 C CD2 . LEU B 976  ? 0.2319 0.2486 0.2342 0.0182  -0.0070 -0.0302 974  LEU B CD2 
16120 N N   . HIS B 977  ? 0.1856 0.2039 0.1887 0.0104  -0.0089 -0.0261 975  HIS B N   
16121 C CA  . HIS B 977  ? 0.1976 0.2179 0.1972 0.0096  -0.0080 -0.0255 975  HIS B CA  
16122 C C   . HIS B 977  ? 0.1935 0.2127 0.1887 0.0112  -0.0080 -0.0268 975  HIS B C   
16123 O O   . HIS B 977  ? 0.2061 0.2212 0.1993 0.0114  -0.0099 -0.0275 975  HIS B O   
16124 C CB  . HIS B 977  ? 0.2102 0.2287 0.2092 0.0075  -0.0093 -0.0244 975  HIS B CB  
16125 C CG  . HIS B 977  ? 0.2255 0.2461 0.2268 0.0058  -0.0086 -0.0230 975  HIS B CG  
16126 N ND1 . HIS B 977  ? 0.3143 0.3369 0.3134 0.0042  -0.0077 -0.0217 975  HIS B ND1 
16127 C CD2 . HIS B 977  ? 0.2841 0.3049 0.2895 0.0054  -0.0086 -0.0226 975  HIS B CD2 
16128 C CE1 . HIS B 977  ? 0.2786 0.3020 0.2802 0.0028  -0.0074 -0.0207 975  HIS B CE1 
16129 N NE2 . HIS B 977  ? 0.2777 0.3001 0.2830 0.0037  -0.0079 -0.0213 975  HIS B NE2 
16130 N N   . THR B 978  ? 0.1911 0.2141 0.1847 0.0125  -0.0059 -0.0270 976  THR B N   
16131 C CA  . THR B 978  ? 0.1986 0.2212 0.1877 0.0144  -0.0055 -0.0283 976  THR B CA  
16132 C C   . THR B 978  ? 0.2100 0.2386 0.1982 0.0150  -0.0028 -0.0279 976  THR B C   
16133 O O   . THR B 978  ? 0.2267 0.2594 0.2185 0.0147  -0.0015 -0.0271 976  THR B O   
16134 C CB  . THR B 978  ? 0.2248 0.2440 0.2136 0.0168  -0.0062 -0.0301 976  THR B CB  
16135 O OG1 . THR B 978  ? 0.2202 0.2389 0.2040 0.0189  -0.0057 -0.0315 976  THR B OG1 
16136 C CG2 . THR B 978  ? 0.2349 0.2569 0.2274 0.0181  -0.0048 -0.0302 976  THR B CG2 
16137 N N   . ARG B 979  ? 0.2264 0.2559 0.2099 0.0159  -0.0020 -0.0284 977  ARG B N   
16138 C CA  . ARG B 979  ? 0.2400 0.2759 0.2228 0.0170  0.0007  -0.0281 977  ARG B CA  
16139 C C   . ARG B 979  ? 0.2583 0.2945 0.2397 0.0208  0.0016  -0.0301 977  ARG B C   
16140 O O   . ARG B 979  ? 0.2486 0.2905 0.2295 0.0224  0.0040  -0.0300 977  ARG B O   
16141 C CB  . ARG B 979  ? 0.2819 0.3197 0.2604 0.0156  0.0015  -0.0272 977  ARG B CB  
16142 C CG  . ARG B 979  ? 0.3642 0.4024 0.3440 0.0119  0.0010  -0.0251 977  ARG B CG  
16143 C CD  . ARG B 979  ? 0.4402 0.4785 0.4151 0.0104  0.0013  -0.0242 977  ARG B CD  
16144 N NE  . ARG B 979  ? 0.5194 0.5580 0.4951 0.0068  0.0009  -0.0220 977  ARG B NE  
16145 C CZ  . ARG B 979  ? 0.5246 0.5638 0.4964 0.0048  0.0012  -0.0206 977  ARG B CZ  
16146 N NH1 . ARG B 979  ? 0.4711 0.5109 0.4379 0.0060  0.0020  -0.0212 977  ARG B NH1 
16147 N NH2 . ARG B 979  ? 0.5328 0.5714 0.5053 0.0015  0.0006  -0.0186 977  ARG B NH2 
16148 N N   . LEU B 980  ? 0.2240 0.2544 0.2049 0.0224  -0.0002 -0.0316 978  LEU B N   
16149 C CA  . LEU B 980  ? 0.2328 0.2615 0.2106 0.0261  0.0002  -0.0337 978  LEU B CA  
16150 C C   . LEU B 980  ? 0.2218 0.2505 0.2032 0.0280  0.0004  -0.0342 978  LEU B C   
16151 O O   . LEU B 980  ? 0.2188 0.2434 0.2029 0.0270  -0.0014 -0.0342 978  LEU B O   
16152 C CB  . LEU B 980  ? 0.2455 0.2668 0.2192 0.0265  -0.0022 -0.0352 978  LEU B CB  
16153 C CG  . LEU B 980  ? 0.2624 0.2828 0.2324 0.0246  -0.0029 -0.0347 978  LEU B CG  
16154 C CD1 . LEU B 980  ? 0.2625 0.2753 0.2287 0.0249  -0.0057 -0.0362 978  LEU B CD1 
16155 C CD2 . LEU B 980  ? 0.2473 0.2729 0.2136 0.0256  -0.0003 -0.0345 978  LEU B CD2 
16156 N N   . ASP B 981  ? 0.2134 0.2468 0.1946 0.0308  0.0026  -0.0347 979  ASP B N   
16157 C CA  . ASP B 981  ? 0.2082 0.2421 0.1927 0.0327  0.0028  -0.0350 979  ASP B CA  
16158 C C   . ASP B 981  ? 0.2272 0.2531 0.2101 0.0344  0.0007  -0.0367 979  ASP B C   
16159 O O   . ASP B 981  ? 0.2144 0.2386 0.2007 0.0344  0.0000  -0.0364 979  ASP B O   
16160 C CB  . ASP B 981  ? 0.2286 0.2688 0.2126 0.0360  0.0053  -0.0354 979  ASP B CB  
16161 C CG  . ASP B 981  ? 0.2697 0.3186 0.2566 0.0342  0.0074  -0.0335 979  ASP B CG  
16162 O OD1 . ASP B 981  ? 0.2612 0.3108 0.2513 0.0305  0.0068  -0.0318 979  ASP B OD1 
16163 O OD2 . ASP B 981  ? 0.2851 0.3402 0.2712 0.0365  0.0096  -0.0337 979  ASP B OD2 
16164 N N   . GLU B 982  ? 0.2323 0.2532 0.2101 0.0358  -0.0003 -0.0384 980  GLU B N   
16165 C CA  . GLU B 982  ? 0.2345 0.2475 0.2107 0.0370  -0.0026 -0.0399 980  GLU B CA  
16166 C C   . GLU B 982  ? 0.2415 0.2506 0.2211 0.0336  -0.0049 -0.0389 980  GLU B C   
16167 O O   . GLU B 982  ? 0.2415 0.2466 0.2230 0.0337  -0.0062 -0.0391 980  GLU B O   
16168 C CB  . GLU B 982  ? 0.2489 0.2569 0.2184 0.0388  -0.0035 -0.0420 980  GLU B CB  
16169 C CG  . GLU B 982  ? 0.3168 0.3158 0.2844 0.0396  -0.0063 -0.0436 980  GLU B CG  
16170 C CD  . GLU B 982  ? 0.3591 0.3522 0.3203 0.0401  -0.0080 -0.0455 980  GLU B CD  
16171 O OE1 . GLU B 982  ? 0.3998 0.3938 0.3598 0.0379  -0.0085 -0.0449 980  GLU B OE1 
16172 O OE2 . GLU B 982  ? 0.3477 0.3350 0.3049 0.0429  -0.0090 -0.0475 980  GLU B OE2 
16173 N N   . THR B 983  ? 0.2228 0.2331 0.2031 0.0305  -0.0054 -0.0378 981  THR B N   
16174 C CA  . THR B 983  ? 0.2114 0.2188 0.1952 0.0274  -0.0074 -0.0368 981  THR B CA  
16175 C C   . THR B 983  ? 0.2176 0.2283 0.2071 0.0264  -0.0066 -0.0352 981  THR B C   
16176 O O   . THR B 983  ? 0.2199 0.2275 0.2123 0.0253  -0.0080 -0.0350 981  THR B O   
16177 C CB  . THR B 983  ? 0.2452 0.2533 0.2281 0.0248  -0.0081 -0.0359 981  THR B CB  
16178 O OG1 . THR B 983  ? 0.2526 0.2568 0.2298 0.0257  -0.0093 -0.0374 981  THR B OG1 
16179 C CG2 . THR B 983  ? 0.2381 0.2440 0.2249 0.0219  -0.0101 -0.0347 981  THR B CG2 
16180 N N   . ILE B 984  ? 0.1951 0.2123 0.1862 0.0267  -0.0043 -0.0343 982  ILE B N   
16181 C CA  . ILE B 984  ? 0.1969 0.2174 0.1930 0.0259  -0.0034 -0.0329 982  ILE B CA  
16182 C C   . ILE B 984  ? 0.2098 0.2276 0.2066 0.0282  -0.0037 -0.0337 982  ILE B C   
16183 O O   . ILE B 984  ? 0.2057 0.2218 0.2060 0.0271  -0.0045 -0.0330 982  ILE B O   
16184 C CB  . ILE B 984  ? 0.2019 0.2299 0.1992 0.0259  -0.0011 -0.0319 982  ILE B CB  
16185 C CG1 . ILE B 984  ? 0.2485 0.2784 0.2452 0.0230  -0.0010 -0.0307 982  ILE B CG1 
16186 C CG2 . ILE B 984  ? 0.2433 0.2744 0.2452 0.0254  -0.0003 -0.0307 982  ILE B CG2 
16187 C CD1 . ILE B 984  ? 0.2456 0.2826 0.2425 0.0226  0.0012  -0.0297 982  ILE B CD1 
16188 N N   . ALA B 985  ? 0.2101 0.2272 0.2035 0.0315  -0.0031 -0.0352 983  ALA B N   
16189 C CA  . ALA B 985  ? 0.2174 0.2315 0.2110 0.0340  -0.0034 -0.0359 983  ALA B CA  
16190 C C   . ALA B 985  ? 0.2226 0.2290 0.2159 0.0328  -0.0059 -0.0364 983  ALA B C   
16191 O O   . ALA B 985  ? 0.2277 0.2322 0.2237 0.0325  -0.0065 -0.0358 983  ALA B O   
16192 C CB  . ALA B 985  ? 0.2090 0.2234 0.1985 0.0381  -0.0023 -0.0376 983  ALA B CB  
16193 N N   . HIS B 986  ? 0.2167 0.2190 0.2067 0.0320  -0.0075 -0.0374 984  HIS B N   
16194 C CA  . HIS B 986  ? 0.2378 0.2330 0.2275 0.0307  -0.0101 -0.0379 984  HIS B CA  
16195 C C   . HIS B 986  ? 0.2093 0.2056 0.2043 0.0274  -0.0108 -0.0361 984  HIS B C   
16196 O O   . HIS B 986  ? 0.2290 0.2226 0.2263 0.0269  -0.0116 -0.0357 984  HIS B O   
16197 C CB  . HIS B 986  ? 0.2559 0.2476 0.2413 0.0301  -0.0117 -0.0391 984  HIS B CB  
16198 C CG  . HIS B 986  ? 0.2565 0.2417 0.2418 0.0282  -0.0146 -0.0395 984  HIS B CG  
16199 N ND1 . HIS B 986  ? 0.3317 0.3126 0.3129 0.0276  -0.0166 -0.0407 984  HIS B ND1 
16200 C CD2 . HIS B 986  ? 0.2830 0.2653 0.2716 0.0265  -0.0160 -0.0387 984  HIS B CD2 
16201 C CE1 . HIS B 986  ? 0.3295 0.3054 0.3118 0.0256  -0.0192 -0.0407 984  HIS B CE1 
16202 N NE2 . HIS B 986  ? 0.2751 0.2519 0.2620 0.0249  -0.0188 -0.0395 984  HIS B NE2 
16203 N N   . VAL B 987  ? 0.1970 0.1972 0.1940 0.0252  -0.0103 -0.0350 985  VAL B N   
16204 C CA  . VAL B 987  ? 0.1968 0.1976 0.1985 0.0222  -0.0111 -0.0335 985  VAL B CA  
16205 C C   . VAL B 987  ? 0.2083 0.2119 0.2139 0.0223  -0.0098 -0.0323 985  VAL B C   
16206 O O   . VAL B 987  ? 0.2312 0.2329 0.2397 0.0210  -0.0107 -0.0316 985  VAL B O   
16207 C CB  . VAL B 987  ? 0.2050 0.2089 0.2073 0.0202  -0.0110 -0.0326 985  VAL B CB  
16208 C CG1 . VAL B 987  ? 0.2221 0.2271 0.2293 0.0177  -0.0115 -0.0311 985  VAL B CG1 
16209 C CG2 . VAL B 987  ? 0.2236 0.2239 0.2221 0.0198  -0.0128 -0.0336 985  VAL B CG2 
16210 N N   . THR B 988  ? 0.2064 0.2148 0.2122 0.0238  -0.0077 -0.0320 986  THR B N   
16211 C CA  . THR B 988  ? 0.2260 0.2371 0.2353 0.0238  -0.0066 -0.0309 986  THR B CA  
16212 C C   . THR B 988  ? 0.2369 0.2442 0.2458 0.0256  -0.0071 -0.0314 986  THR B C   
16213 O O   . THR B 988  ? 0.2970 0.3046 0.3089 0.0250  -0.0069 -0.0303 986  THR B O   
16214 C CB  . THR B 988  ? 0.2538 0.2714 0.2637 0.0246  -0.0044 -0.0303 986  THR B CB  
16215 O OG1 . THR B 988  ? 0.2623 0.2808 0.2690 0.0276  -0.0036 -0.0315 986  THR B OG1 
16216 C CG2 . THR B 988  ? 0.2572 0.2782 0.2677 0.0224  -0.0041 -0.0295 986  THR B CG2 
16217 N N   . SER B 989  ? 0.2317 0.2348 0.2365 0.0278  -0.0078 -0.0329 987  SER B N   
16218 C CA  . SER B 989  ? 0.2665 0.2647 0.2703 0.0294  -0.0086 -0.0334 987  SER B CA  
16219 C C   . SER B 989  ? 0.2809 0.2738 0.2860 0.0270  -0.0107 -0.0330 987  SER B C   
16220 O O   . SER B 989  ? 0.3240 0.3134 0.3295 0.0273  -0.0113 -0.0327 987  SER B O   
16221 C CB  . SER B 989  ? 0.2998 0.2947 0.2985 0.0329  -0.0088 -0.0353 987  SER B CB  
16222 O OG  . SER B 989  ? 0.3641 0.3544 0.3594 0.0323  -0.0105 -0.0366 987  SER B OG  
16223 N N   . ARG B 990  ? 0.2294 0.2217 0.2352 0.0245  -0.0119 -0.0329 988  ARG B N   
16224 C CA  . ARG B 990  ? 0.2156 0.2032 0.2225 0.0221  -0.0141 -0.0327 988  ARG B CA  
16225 C C   . ARG B 990  ? 0.2247 0.2154 0.2368 0.0192  -0.0140 -0.0309 988  ARG B C   
16226 O O   . ARG B 990  ? 0.2387 0.2269 0.2529 0.0173  -0.0153 -0.0303 988  ARG B O   
16227 C CB  . ARG B 990  ? 0.2406 0.2244 0.2440 0.0217  -0.0160 -0.0341 988  ARG B CB  
16228 C CG  . ARG B 990  ? 0.3285 0.3088 0.3261 0.0247  -0.0162 -0.0361 988  ARG B CG  
16229 C CD  . ARG B 990  ? 0.3257 0.2993 0.3212 0.0257  -0.0175 -0.0367 988  ARG B CD  
16230 N NE  . ARG B 990  ? 0.2666 0.2341 0.2601 0.0239  -0.0204 -0.0376 988  ARG B NE  
16231 C CZ  . ARG B 990  ? 0.2605 0.2209 0.2516 0.0240  -0.0222 -0.0382 988  ARG B CZ  
16232 N NH1 . ARG B 990  ? 0.3156 0.2740 0.3062 0.0258  -0.0216 -0.0380 988  ARG B NH1 
16233 N NH2 . ARG B 990  ? 0.3065 0.2617 0.2957 0.0221  -0.0250 -0.0390 988  ARG B NH2 
16234 N N   . ILE B 991  ? 0.2108 0.2071 0.2249 0.0186  -0.0126 -0.0302 989  ILE B N   
16235 C CA  . ILE B 991  ? 0.2097 0.2088 0.2283 0.0163  -0.0125 -0.0287 989  ILE B CA  
16236 C C   . ILE B 991  ? 0.2169 0.2172 0.2382 0.0164  -0.0114 -0.0276 989  ILE B C   
16237 O O   . ILE B 991  ? 0.2284 0.2293 0.2484 0.0184  -0.0102 -0.0277 989  ILE B O   
16238 C CB  . ILE B 991  ? 0.2069 0.2107 0.2259 0.0159  -0.0114 -0.0283 989  ILE B CB  
16239 C CG1 . ILE B 991  ? 0.2543 0.2600 0.2773 0.0136  -0.0117 -0.0271 989  ILE B CG1 
16240 C CG2 . ILE B 991  ? 0.2262 0.2341 0.2452 0.0174  -0.0092 -0.0280 989  ILE B CG2 
16241 C CD1 . ILE B 991  ? 0.2769 0.2797 0.3002 0.0121  -0.0139 -0.0274 989  ILE B CD1 
16242 N N   . LYS B 992  ? 0.1877 0.1884 0.2127 0.0143  -0.0117 -0.0264 990  LYS B N   
16243 C CA  . LYS B 992  ? 0.2015 0.2033 0.2289 0.0142  -0.0107 -0.0252 990  LYS B CA  
16244 C C   . LYS B 992  ? 0.2155 0.2219 0.2464 0.0129  -0.0096 -0.0241 990  LYS B C   
16245 O O   . LYS B 992  ? 0.2515 0.2581 0.2853 0.0111  -0.0101 -0.0232 990  LYS B O   
16246 C CB  . LYS B 992  ? 0.2168 0.2144 0.2450 0.0130  -0.0121 -0.0247 990  LYS B CB  
16247 C CG  . LYS B 992  ? 0.2563 0.2484 0.2805 0.0144  -0.0133 -0.0259 990  LYS B CG  
16248 C CD  . LYS B 992  ? 0.3396 0.3270 0.3645 0.0126  -0.0149 -0.0254 990  LYS B CD  
16249 C CE  . LYS B 992  ? 0.4326 0.4212 0.4603 0.0118  -0.0139 -0.0236 990  LYS B CE  
16250 N NZ  . LYS B 992  ? 0.5440 0.5287 0.5728 0.0095  -0.0154 -0.0228 990  LYS B NZ  
16251 N N   . ALA B 993  ? 0.1857 0.1958 0.2161 0.0138  -0.0082 -0.0241 991  ALA B N   
16252 C CA  . ALA B 993  ? 0.1719 0.1857 0.2049 0.0127  -0.0073 -0.0232 991  ALA B CA  
16253 C C   . ALA B 993  ? 0.1733 0.1902 0.2059 0.0138  -0.0056 -0.0228 991  ALA B C   
16254 O O   . ALA B 993  ? 0.1900 0.2072 0.2203 0.0155  -0.0052 -0.0234 991  ALA B O   
16255 C CB  . ALA B 993  ? 0.2035 0.2184 0.2360 0.0119  -0.0077 -0.0235 991  ALA B CB  
16256 N N   . GLY B 994  ? 0.1577 0.1771 0.1926 0.0130  -0.0047 -0.0219 992  GLY B N   
16257 C CA  . GLY B 994  ? 0.1673 0.1895 0.2020 0.0138  -0.0034 -0.0215 992  GLY B CA  
16258 C C   . GLY B 994  ? 0.1582 0.1836 0.1917 0.0138  -0.0028 -0.0217 992  GLY B C   
16259 O O   . GLY B 994  ? 0.1471 0.1751 0.1801 0.0148  -0.0019 -0.0216 992  GLY B O   
16260 N N   . ASN B 995  ? 0.1620 0.1874 0.1952 0.0127  -0.0033 -0.0220 993  ASN B N   
16261 C CA  . ASN B 995  ? 0.1654 0.1935 0.1974 0.0123  -0.0028 -0.0220 993  ASN B CA  
16262 C C   . ASN B 995  ? 0.1444 0.1711 0.1743 0.0122  -0.0036 -0.0227 993  ASN B C   
16263 O O   . ASN B 995  ? 0.1623 0.1869 0.1927 0.0113  -0.0047 -0.0228 993  ASN B O   
16264 C CB  . ASN B 995  ? 0.1724 0.2016 0.2057 0.0108  -0.0026 -0.0214 993  ASN B CB  
16265 C CG  . ASN B 995  ? 0.1708 0.2022 0.2052 0.0109  -0.0016 -0.0208 993  ASN B CG  
16266 O OD1 . ASN B 995  ? 0.1596 0.1901 0.1955 0.0111  -0.0014 -0.0204 993  ASN B OD1 
16267 N ND2 . ASN B 995  ? 0.1630 0.1973 0.1963 0.0107  -0.0010 -0.0206 993  ASN B ND2 
16268 N N   . LEU B 996  ? 0.1505 0.1789 0.1783 0.0133  -0.0031 -0.0232 994  LEU B N   
16269 C CA  . LEU B 996  ? 0.1582 0.1855 0.1834 0.0134  -0.0036 -0.0240 994  LEU B CA  
16270 C C   . LEU B 996  ? 0.1646 0.1951 0.1886 0.0124  -0.0029 -0.0235 994  LEU B C   
16271 O O   . LEU B 996  ? 0.1513 0.1855 0.1760 0.0123  -0.0018 -0.0230 994  LEU B O   
16272 C CB  . LEU B 996  ? 0.1639 0.1904 0.1870 0.0157  -0.0035 -0.0249 994  LEU B CB  
16273 C CG  . LEU B 996  ? 0.1700 0.1933 0.1940 0.0168  -0.0040 -0.0252 994  LEU B CG  
16274 C CD1 . LEU B 996  ? 0.2169 0.2389 0.2380 0.0193  -0.0040 -0.0263 994  LEU B CD1 
16275 C CD2 . LEU B 996  ? 0.1869 0.2063 0.2119 0.0154  -0.0056 -0.0252 994  LEU B CD2 
16276 N N   . TYR B 997  ? 0.1599 0.1892 0.1820 0.0116  -0.0036 -0.0237 995  TYR B N   
16277 C CA  . TYR B 997  ? 0.1650 0.1968 0.1856 0.0102  -0.0031 -0.0231 995  TYR B CA  
16278 C C   . TYR B 997  ? 0.1625 0.1934 0.1798 0.0106  -0.0034 -0.0237 995  TYR B C   
16279 O O   . TYR B 997  ? 0.1795 0.2067 0.1958 0.0107  -0.0048 -0.0243 995  TYR B O   
16280 C CB  . TYR B 997  ? 0.1865 0.2168 0.2080 0.0082  -0.0039 -0.0223 995  TYR B CB  
16281 C CG  . TYR B 997  ? 0.1702 0.2007 0.1946 0.0079  -0.0037 -0.0219 995  TYR B CG  
16282 C CD1 . TYR B 997  ? 0.1601 0.1881 0.1866 0.0085  -0.0044 -0.0221 995  TYR B CD1 
16283 C CD2 . TYR B 997  ? 0.1833 0.2167 0.2084 0.0070  -0.0028 -0.0212 995  TYR B CD2 
16284 C CE1 . TYR B 997  ? 0.1888 0.2171 0.2177 0.0083  -0.0041 -0.0217 995  TYR B CE1 
16285 C CE2 . TYR B 997  ? 0.1728 0.2061 0.2001 0.0069  -0.0027 -0.0209 995  TYR B CE2 
16286 C CZ  . TYR B 997  ? 0.1813 0.2121 0.2105 0.0077  -0.0032 -0.0212 995  TYR B CZ  
16287 O OH  . TYR B 997  ? 0.2148 0.2458 0.2460 0.0076  -0.0028 -0.0208 995  TYR B OH  
16288 N N   . ILE B 998  ? 0.1670 0.2016 0.1825 0.0109  -0.0022 -0.0236 996  ILE B N   
16289 C CA  . ILE B 998  ? 0.1706 0.2051 0.1826 0.0116  -0.0021 -0.0242 996  ILE B CA  
16290 C C   . ILE B 998  ? 0.1861 0.2226 0.1964 0.0093  -0.0017 -0.0231 996  ILE B C   
16291 O O   . ILE B 998  ? 0.1795 0.2203 0.1905 0.0084  -0.0005 -0.0223 996  ILE B O   
16292 C CB  . ILE B 998  ? 0.1977 0.2351 0.2087 0.0141  -0.0007 -0.0250 996  ILE B CB  
16293 C CG1 . ILE B 998  ? 0.2484 0.2833 0.2608 0.0162  -0.0012 -0.0260 996  ILE B CG1 
16294 C CG2 . ILE B 998  ? 0.2005 0.2378 0.2074 0.0149  -0.0005 -0.0258 996  ILE B CG2 
16295 C CD1 . ILE B 998  ? 0.3117 0.3408 0.3229 0.0166  -0.0029 -0.0269 996  ILE B CD1 
16296 N N   . ASN B 999  ? 0.1750 0.2081 0.1829 0.0084  -0.0030 -0.0231 997  ASN B N   
16297 C CA  . ASN B 999  ? 0.1910 0.2251 0.1965 0.0064  -0.0028 -0.0221 997  ASN B CA  
16298 C C   . ASN B 999  ? 0.1850 0.2197 0.1922 0.0040  -0.0029 -0.0207 997  ASN B C   
16299 O O   . ASN B 999  ? 0.1895 0.2270 0.1955 0.0021  -0.0021 -0.0196 997  ASN B O   
16300 C CB  . ASN B 999  ? 0.1766 0.2151 0.1795 0.0069  -0.0011 -0.0220 997  ASN B CB  
16301 C CG  . ASN B 999  ? 0.1947 0.2314 0.1947 0.0091  -0.0013 -0.0235 997  ASN B CG  
16302 O OD1 . ASN B 999  ? 0.1979 0.2297 0.1965 0.0092  -0.0030 -0.0240 997  ASN B OD1 
16303 N ND2 . ASN B 999  ? 0.2102 0.2507 0.2091 0.0111  0.0004  -0.0241 997  ASN B ND2 
16304 N N   . ARG B 1000 ? 0.1770 0.2092 0.1870 0.0039  -0.0039 -0.0208 998  ARG B N   
16305 C CA  . ARG B 1000 ? 0.1619 0.1937 0.1733 0.0020  -0.0042 -0.0198 998  ARG B CA  
16306 C C   . ARG B 1000 ? 0.1798 0.2076 0.1933 0.0025  -0.0057 -0.0201 998  ARG B C   
16307 O O   . ARG B 1000 ? 0.1974 0.2230 0.2113 0.0039  -0.0065 -0.0210 998  ARG B O   
16308 C CB  . ARG B 1000 ? 0.1767 0.2127 0.1903 0.0019  -0.0028 -0.0194 998  ARG B CB  
16309 C CG  . ARG B 1000 ? 0.1839 0.2210 0.2000 0.0042  -0.0022 -0.0204 998  ARG B CG  
16310 C CD  . ARG B 1000 ? 0.1744 0.2141 0.1930 0.0039  -0.0015 -0.0200 998  ARG B CD  
16311 N NE  . ARG B 1000 ? 0.1623 0.1990 0.1822 0.0027  -0.0025 -0.0196 998  ARG B NE  
16312 C CZ  . ARG B 1000 ? 0.1694 0.2073 0.1908 0.0020  -0.0022 -0.0192 998  ARG B CZ  
16313 N NH1 . ARG B 1000 ? 0.1798 0.2220 0.2021 0.0021  -0.0011 -0.0190 998  ARG B NH1 
16314 N NH2 . ARG B 1000 ? 0.1863 0.2210 0.2082 0.0012  -0.0030 -0.0190 998  ARG B NH2 
16315 N N   . ASN B 1001 ? 0.1651 0.1918 0.1797 0.0012  -0.0060 -0.0194 999  ASN B N   
16316 C CA  . ASN B 1001 ? 0.1655 0.1891 0.1823 0.0019  -0.0071 -0.0197 999  ASN B CA  
16317 C C   . ASN B 1001 ? 0.1608 0.1860 0.1809 0.0034  -0.0064 -0.0204 999  ASN B C   
16318 O O   . ASN B 1001 ? 0.1772 0.2054 0.1976 0.0039  -0.0051 -0.0205 999  ASN B O   
16319 C CB  . ASN B 1001 ? 0.1906 0.2125 0.2073 0.0005  -0.0077 -0.0190 999  ASN B CB  
16320 C CG  . ASN B 1001 ? 0.2043 0.2285 0.2221 -0.0003 -0.0066 -0.0186 999  ASN B CG  
16321 O OD1 . ASN B 1001 ? 0.1949 0.2211 0.2151 0.0008  -0.0057 -0.0191 999  ASN B OD1 
16322 N ND2 . ASN B 1001 ? 0.3272 0.3508 0.3429 -0.0023 -0.0067 -0.0178 999  ASN B ND2 
16323 N N   . ILE B 1002 ? 0.1653 0.1884 0.1877 0.0041  -0.0072 -0.0207 1000 ILE B N   
16324 C CA  . ILE B 1002 ? 0.1831 0.2070 0.2083 0.0054  -0.0067 -0.0211 1000 ILE B CA  
16325 C C   . ILE B 1002 ? 0.1848 0.2092 0.2123 0.0052  -0.0062 -0.0207 1000 ILE B C   
16326 O O   . ILE B 1002 ? 0.2012 0.2256 0.2312 0.0060  -0.0060 -0.0209 1000 ILE B O   
16327 C CB  . ILE B 1002 ? 0.1657 0.1876 0.1919 0.0063  -0.0078 -0.0217 1000 ILE B CB  
16328 C CG1 . ILE B 1002 ? 0.1765 0.1961 0.2041 0.0060  -0.0092 -0.0215 1000 ILE B CG1 
16329 C CG2 . ILE B 1002 ? 0.1709 0.1922 0.1943 0.0066  -0.0082 -0.0223 1000 ILE B CG2 
16330 C CD1 . ILE B 1002 ? 0.1802 0.1986 0.2098 0.0066  -0.0103 -0.0220 1000 ILE B CD1 
16331 N N   . ILE B 1003 ? 0.1820 0.2064 0.2084 0.0040  -0.0061 -0.0202 1001 ILE B N   
16332 C CA  . ILE B 1003 ? 0.2061 0.2303 0.2342 0.0040  -0.0057 -0.0200 1001 ILE B CA  
16333 C C   . ILE B 1003 ? 0.2638 0.2907 0.2917 0.0035  -0.0046 -0.0198 1001 ILE B C   
16334 O O   . ILE B 1003 ? 0.2588 0.2855 0.2872 0.0033  -0.0043 -0.0196 1001 ILE B O   
16335 C CB  . ILE B 1003 ? 0.2271 0.2484 0.2543 0.0034  -0.0068 -0.0198 1001 ILE B CB  
16336 C CG1 . ILE B 1003 ? 0.2995 0.3200 0.3233 0.0018  -0.0072 -0.0193 1001 ILE B CG1 
16337 C CG2 . ILE B 1003 ? 0.2116 0.2310 0.2400 0.0043  -0.0080 -0.0200 1001 ILE B CG2 
16338 C CD1 . ILE B 1003 ? 0.3750 0.3922 0.3974 0.0012  -0.0083 -0.0190 1001 ILE B CD1 
16339 N N   . GLY B 1004 ? 0.2223 0.2520 0.2494 0.0035  -0.0038 -0.0198 1002 GLY B N   
16340 C CA  . GLY B 1004 ? 0.2199 0.2527 0.2470 0.0030  -0.0029 -0.0195 1002 GLY B CA  
16341 C C   . GLY B 1004 ? 0.2219 0.2557 0.2513 0.0043  -0.0022 -0.0196 1002 GLY B C   
16342 O O   . GLY B 1004 ? 0.2355 0.2693 0.2660 0.0057  -0.0020 -0.0200 1002 GLY B O   
16343 N N   . ALA B 1005 ? 0.2097 0.2440 0.2391 0.0036  -0.0019 -0.0194 1003 ALA B N   
16344 C CA  . ALA B 1005 ? 0.2142 0.2495 0.2453 0.0046  -0.0013 -0.0194 1003 ALA B CA  
16345 C C   . ALA B 1005 ? 0.2294 0.2674 0.2597 0.0037  -0.0009 -0.0190 1003 ALA B C   
16346 O O   . ALA B 1005 ? 0.2467 0.2845 0.2774 0.0037  -0.0007 -0.0190 1003 ALA B O   
16347 C CB  . ALA B 1005 ? 0.2354 0.2681 0.2677 0.0051  -0.0014 -0.0195 1003 ALA B CB  
16348 N N   . VAL B 1006 ? 0.1736 0.2143 0.2028 0.0026  -0.0008 -0.0188 1004 VAL B N   
16349 C CA  . VAL B 1006 ? 0.1912 0.2347 0.2198 0.0013  -0.0007 -0.0183 1004 VAL B CA  
16350 C C   . VAL B 1006 ? 0.1744 0.2204 0.2045 0.0028  -0.0001 -0.0183 1004 VAL B C   
16351 O O   . VAL B 1006 ? 0.1716 0.2196 0.2028 0.0045  0.0004  -0.0184 1004 VAL B O   
16352 C CB  . VAL B 1006 ? 0.1901 0.2368 0.2177 -0.0002 -0.0007 -0.0179 1004 VAL B CB  
16353 C CG1 . VAL B 1006 ? 0.1934 0.2437 0.2208 -0.0018 -0.0007 -0.0173 1004 VAL B CG1 
16354 C CG2 . VAL B 1006 ? 0.2002 0.2436 0.2257 -0.0019 -0.0014 -0.0177 1004 VAL B CG2 
16355 N N   . VAL B 1007 ? 0.1788 0.2243 0.2086 0.0023  -0.0002 -0.0182 1005 VAL B N   
16356 C CA  . VAL B 1007 ? 0.1654 0.2126 0.1963 0.0037  0.0002  -0.0181 1005 VAL B CA  
16357 C C   . VAL B 1007 ? 0.1755 0.2278 0.2071 0.0041  0.0005  -0.0178 1005 VAL B C   
16358 O O   . VAL B 1007 ? 0.1666 0.2219 0.1976 0.0025  0.0003  -0.0174 1005 VAL B O   
16359 C CB  . VAL B 1007 ? 0.1652 0.2112 0.1949 0.0027  -0.0001 -0.0181 1005 VAL B CB  
16360 C CG1 . VAL B 1007 ? 0.1868 0.2348 0.2172 0.0039  0.0003  -0.0178 1005 VAL B CG1 
16361 C CG2 . VAL B 1007 ? 0.1790 0.2204 0.2084 0.0029  -0.0002 -0.0185 1005 VAL B CG2 
16362 N N   . GLY B 1008 ? 0.1621 0.2153 0.1948 0.0064  0.0010  -0.0178 1006 GLY B N   
16363 C CA  . GLY B 1008 ? 0.1643 0.2223 0.1977 0.0075  0.0013  -0.0175 1006 GLY B CA  
16364 C C   . GLY B 1008 ? 0.1696 0.2299 0.2030 0.0076  0.0016  -0.0176 1006 GLY B C   
16365 O O   . GLY B 1008 ? 0.1942 0.2592 0.2283 0.0087  0.0019  -0.0175 1006 GLY B O   
16366 N N   . VAL B 1009 ? 0.1691 0.2265 0.2017 0.0067  0.0014  -0.0180 1007 VAL B N   
16367 C CA  . VAL B 1009 ? 0.1595 0.2186 0.1915 0.0067  0.0017  -0.0181 1007 VAL B CA  
16368 C C   . VAL B 1009 ? 0.1736 0.2286 0.2053 0.0082  0.0017  -0.0188 1007 VAL B C   
16369 O O   . VAL B 1009 ? 0.1745 0.2305 0.2060 0.0101  0.0021  -0.0192 1007 VAL B O   
16370 C CB  . VAL B 1009 ? 0.1701 0.2298 0.2009 0.0038  0.0014  -0.0177 1007 VAL B CB  
16371 C CG1 . VAL B 1009 ? 0.1648 0.2264 0.1947 0.0038  0.0019  -0.0177 1007 VAL B CG1 
16372 C CG2 . VAL B 1009 ? 0.1816 0.2453 0.2127 0.0020  0.0012  -0.0170 1007 VAL B CG2 
16373 N N   . GLN B 1010 ? 0.1718 0.2222 0.2033 0.0075  0.0011  -0.0189 1008 GLN B N   
16374 C CA  . GLN B 1010 ? 0.1705 0.2168 0.2022 0.0089  0.0008  -0.0195 1008 GLN B CA  
16375 C C   . GLN B 1010 ? 0.1821 0.2263 0.2151 0.0093  0.0008  -0.0193 1008 GLN B C   
16376 O O   . GLN B 1010 ? 0.1850 0.2264 0.2183 0.0084  0.0004  -0.0193 1008 GLN B O   
16377 C CB  . GLN B 1010 ? 0.1936 0.2369 0.2244 0.0077  0.0002  -0.0197 1008 GLN B CB  
16378 C CG  . GLN B 1010 ? 0.1882 0.2333 0.2173 0.0071  0.0003  -0.0198 1008 GLN B CG  
16379 C CD  . GLN B 1010 ? 0.1917 0.2377 0.2197 0.0046  0.0001  -0.0191 1008 GLN B CD  
16380 O OE1 . GLN B 1010 ? 0.1955 0.2388 0.2235 0.0034  -0.0005 -0.0190 1008 GLN B OE1 
16381 N NE2 . GLN B 1010 ? 0.1799 0.2297 0.2070 0.0038  0.0006  -0.0188 1008 GLN B NE2 
16382 N N   . PRO B 1011 ? 0.1627 0.2082 0.1964 0.0108  0.0012  -0.0191 1009 PRO B N   
16383 C CA  . PRO B 1011 ? 0.1761 0.2193 0.2108 0.0113  0.0012  -0.0189 1009 PRO B CA  
16384 C C   . PRO B 1011 ? 0.1482 0.1875 0.1833 0.0113  0.0008  -0.0192 1009 PRO B C   
16385 O O   . PRO B 1011 ? 0.1472 0.1853 0.1820 0.0120  0.0005  -0.0196 1009 PRO B O   
16386 C CB  . PRO B 1011 ? 0.1692 0.2137 0.2040 0.0134  0.0015  -0.0187 1009 PRO B CB  
16387 C CG  . PRO B 1011 ? 0.1709 0.2199 0.2052 0.0135  0.0018  -0.0187 1009 PRO B CG  
16388 C CD  . PRO B 1011 ? 0.1801 0.2292 0.2137 0.0123  0.0016  -0.0191 1009 PRO B CD  
16389 N N   . PHE B 1012 ? 0.1460 0.1835 0.1820 0.0106  0.0008  -0.0190 1010 PHE B N   
16390 C CA  . PHE B 1012 ? 0.1464 0.1811 0.1831 0.0101  0.0002  -0.0192 1010 PHE B CA  
16391 C C   . PHE B 1012 ? 0.1507 0.1836 0.1890 0.0107  0.0004  -0.0188 1010 PHE B C   
16392 O O   . PHE B 1012 ? 0.1645 0.1979 0.2033 0.0107  0.0010  -0.0183 1010 PHE B O   
16393 C CB  . PHE B 1012 ? 0.1405 0.1747 0.1769 0.0088  0.0000  -0.0193 1010 PHE B CB  
16394 C CG  . PHE B 1012 ? 0.1483 0.1800 0.1854 0.0085  -0.0008 -0.0195 1010 PHE B CG  
16395 C CD1 . PHE B 1012 ? 0.1697 0.2008 0.2059 0.0082  -0.0015 -0.0199 1010 PHE B CD1 
16396 C CD2 . PHE B 1012 ? 0.1742 0.2047 0.2132 0.0087  -0.0007 -0.0193 1010 PHE B CD2 
16397 C CE1 . PHE B 1012 ? 0.1639 0.1929 0.2008 0.0080  -0.0024 -0.0201 1010 PHE B CE1 
16398 C CE2 . PHE B 1012 ? 0.1752 0.2042 0.2153 0.0085  -0.0015 -0.0195 1010 PHE B CE2 
16399 C CZ  . PHE B 1012 ? 0.1759 0.2039 0.2149 0.0082  -0.0025 -0.0199 1010 PHE B CZ  
16400 N N   . GLY B 1013 ? 0.1518 0.1826 0.1907 0.0109  -0.0002 -0.0191 1011 GLY B N   
16401 C CA  . GLY B 1013 ? 0.1455 0.1747 0.1862 0.0109  -0.0003 -0.0186 1011 GLY B CA  
16402 C C   . GLY B 1013 ? 0.1498 0.1767 0.1902 0.0113  -0.0011 -0.0189 1011 GLY B C   
16403 O O   . GLY B 1013 ? 0.1672 0.1940 0.2060 0.0122  -0.0013 -0.0194 1011 GLY B O   
16404 N N   . GLY B 1014 ? 0.1713 0.1965 0.2135 0.0106  -0.0016 -0.0186 1012 GLY B N   
16405 C CA  . GLY B 1014 ? 0.1954 0.2179 0.2373 0.0107  -0.0027 -0.0190 1012 GLY B CA  
16406 C C   . GLY B 1014 ? 0.1998 0.2204 0.2426 0.0106  -0.0028 -0.0182 1012 GLY B C   
16407 O O   . GLY B 1014 ? 0.2071 0.2285 0.2504 0.0107  -0.0018 -0.0173 1012 GLY B O   
16408 N N   . ARG B 1015 ? 0.1850 0.2027 0.2278 0.0101  -0.0041 -0.0185 1013 ARG B N   
16409 C CA  . ARG B 1015 ? 0.1879 0.2027 0.2308 0.0097  -0.0046 -0.0178 1013 ARG B CA  
16410 C C   . ARG B 1015 ? 0.1794 0.1934 0.2249 0.0078  -0.0057 -0.0175 1013 ARG B C   
16411 O O   . ARG B 1015 ? 0.1745 0.1901 0.2213 0.0072  -0.0061 -0.0179 1013 ARG B O   
16412 C CB  . ARG B 1015 ? 0.1954 0.2068 0.2352 0.0111  -0.0054 -0.0187 1013 ARG B CB  
16413 C CG  . ARG B 1015 ? 0.2041 0.2141 0.2424 0.0112  -0.0067 -0.0200 1013 ARG B CG  
16414 C CD  . ARG B 1015 ? 0.2368 0.2418 0.2724 0.0118  -0.0081 -0.0207 1013 ARG B CD  
16415 N NE  . ARG B 1015 ? 0.2827 0.2849 0.3199 0.0098  -0.0094 -0.0201 1013 ARG B NE  
16416 C CZ  . ARG B 1015 ? 0.2789 0.2811 0.3177 0.0082  -0.0107 -0.0204 1013 ARG B CZ  
16417 N NH1 . ARG B 1015 ? 0.2641 0.2682 0.3026 0.0084  -0.0109 -0.0213 1013 ARG B NH1 
16418 N NH2 . ARG B 1015 ? 0.3174 0.3176 0.3580 0.0062  -0.0119 -0.0196 1013 ARG B NH2 
16419 N N   . GLY B 1016 ? 0.1893 0.2005 0.2351 0.0069  -0.0063 -0.0168 1014 GLY B N   
16420 C CA  . GLY B 1016 ? 0.1816 0.1925 0.2301 0.0048  -0.0075 -0.0163 1014 GLY B CA  
16421 C C   . GLY B 1016 ? 0.1975 0.2129 0.2497 0.0040  -0.0064 -0.0154 1014 GLY B C   
16422 O O   . GLY B 1016 ? 0.2028 0.2202 0.2556 0.0044  -0.0047 -0.0145 1014 GLY B O   
16423 N N   . LEU B 1017 ? 0.1789 0.1959 0.2335 0.0031  -0.0073 -0.0156 1015 LEU B N   
16424 C CA  . LEU B 1017 ? 0.1907 0.2120 0.2488 0.0027  -0.0063 -0.0149 1015 LEU B CA  
16425 C C   . LEU B 1017 ? 0.1816 0.2051 0.2387 0.0043  -0.0050 -0.0155 1015 LEU B C   
16426 O O   . LEU B 1017 ? 0.1820 0.2087 0.2413 0.0044  -0.0040 -0.0150 1015 LEU B O   
16427 C CB  . LEU B 1017 ? 0.1881 0.2105 0.2489 0.0016  -0.0079 -0.0151 1015 LEU B CB  
16428 C CG  . LEU B 1017 ? 0.2201 0.2409 0.2826 -0.0005 -0.0095 -0.0145 1015 LEU B CG  
16429 C CD1 . LEU B 1017 ? 0.2272 0.2495 0.2923 -0.0014 -0.0114 -0.0148 1015 LEU B CD1 
16430 C CD2 . LEU B 1017 ? 0.2235 0.2462 0.2887 -0.0018 -0.0082 -0.0127 1015 LEU B CD2 
16431 N N   . SER B 1018 ? 0.1554 0.1773 0.2090 0.0056  -0.0049 -0.0164 1016 SER B N   
16432 C CA  . SER B 1018 ? 0.1596 0.1834 0.2120 0.0067  -0.0039 -0.0169 1016 SER B CA  
16433 C C   . SER B 1018 ? 0.1457 0.1704 0.1969 0.0074  -0.0022 -0.0164 1016 SER B C   
16434 O O   . SER B 1018 ? 0.1649 0.1914 0.2154 0.0080  -0.0014 -0.0167 1016 SER B O   
16435 C CB  . SER B 1018 ? 0.1691 0.1913 0.2184 0.0074  -0.0048 -0.0181 1016 SER B CB  
16436 O OG  . SER B 1018 ? 0.1710 0.1924 0.2211 0.0067  -0.0064 -0.0186 1016 SER B OG  
16437 N N   . GLY B 1019 ? 0.1581 0.1817 0.2090 0.0073  -0.0018 -0.0156 1017 GLY B N   
16438 C CA  . GLY B 1019 ? 0.1682 0.1929 0.2178 0.0081  -0.0003 -0.0151 1017 GLY B CA  
16439 C C   . GLY B 1019 ? 0.1623 0.1850 0.2111 0.0081  -0.0001 -0.0142 1017 GLY B C   
16440 O O   . GLY B 1019 ? 0.1967 0.2164 0.2448 0.0079  -0.0013 -0.0143 1017 GLY B O   
16441 N N   . THR B 1020 ? 0.1679 0.1920 0.2164 0.0085  0.0012  -0.0133 1018 THR B N   
16442 C CA  . THR B 1020 ? 0.1772 0.1994 0.2240 0.0089  0.0015  -0.0124 1018 THR B CA  
16443 C C   . THR B 1020 ? 0.1799 0.2019 0.2239 0.0107  0.0015  -0.0131 1018 THR B C   
16444 O O   . THR B 1020 ? 0.1856 0.2053 0.2278 0.0115  0.0011  -0.0127 1018 THR B O   
16445 C CB  . THR B 1020 ? 0.1647 0.1887 0.2122 0.0085  0.0030  -0.0111 1018 THR B CB  
16446 O OG1 . THR B 1020 ? 0.1636 0.1905 0.2107 0.0092  0.0040  -0.0116 1018 THR B OG1 
16447 C CG2 . THR B 1020 ? 0.1605 0.1854 0.2112 0.0068  0.0033  -0.0101 1018 THR B CG2 
16448 N N   . GLY B 1021 ? 0.1732 0.1977 0.2168 0.0112  0.0017  -0.0140 1019 GLY B N   
16449 C CA  . GLY B 1021 ? 0.1651 0.1908 0.2065 0.0126  0.0020  -0.0143 1019 GLY B CA  
16450 C C   . GLY B 1021 ? 0.1679 0.1948 0.2089 0.0128  0.0031  -0.0133 1019 GLY B C   
16451 O O   . GLY B 1021 ? 0.1703 0.1970 0.2124 0.0119  0.0037  -0.0123 1019 GLY B O   
16452 N N   . PRO B 1022 ? 0.1653 0.1937 0.2045 0.0139  0.0032  -0.0134 1020 PRO B N   
16453 C CA  . PRO B 1022 ? 0.1602 0.1899 0.1983 0.0149  0.0027  -0.0144 1020 PRO B CA  
16454 C C   . PRO B 1022 ? 0.1795 0.2112 0.2182 0.0139  0.0027  -0.0153 1020 PRO B C   
16455 O O   . PRO B 1022 ? 0.1896 0.2218 0.2293 0.0129  0.0032  -0.0152 1020 PRO B O   
16456 C CB  . PRO B 1022 ? 0.1930 0.2246 0.2296 0.0160  0.0030  -0.0139 1020 PRO B CB  
16457 C CG  . PRO B 1022 ? 0.1797 0.2118 0.2165 0.0152  0.0039  -0.0131 1020 PRO B CG  
16458 C CD  . PRO B 1022 ? 0.1753 0.2049 0.2136 0.0142  0.0041  -0.0124 1020 PRO B CD  
16459 N N   . LYS B 1023 ? 0.1570 0.1898 0.1951 0.0143  0.0022  -0.0162 1021 LYS B N   
16460 C CA  . LYS B 1023 ? 0.1548 0.1890 0.1930 0.0133  0.0020  -0.0169 1021 LYS B CA  
16461 C C   . LYS B 1023 ? 0.1530 0.1895 0.1907 0.0127  0.0025  -0.0168 1021 LYS B C   
16462 O O   . LYS B 1023 ? 0.1567 0.1951 0.1934 0.0132  0.0027  -0.0165 1021 LYS B O   
16463 C CB  . LYS B 1023 ? 0.1594 0.1947 0.1967 0.0138  0.0016  -0.0177 1021 LYS B CB  
16464 C CG  . LYS B 1023 ? 0.1588 0.1915 0.1960 0.0143  0.0009  -0.0182 1021 LYS B CG  
16465 C CD  . LYS B 1023 ? 0.1446 0.1792 0.1805 0.0150  0.0007  -0.0189 1021 LYS B CD  
16466 C CE  . LYS B 1023 ? 0.1725 0.2047 0.2077 0.0154  0.0000  -0.0197 1021 LYS B CE  
16467 N NZ  . LYS B 1023 ? 0.1646 0.1963 0.2002 0.0138  -0.0004 -0.0200 1021 LYS B NZ  
16468 N N   . ALA B 1024 ? 0.1781 0.2142 0.2162 0.0115  0.0026  -0.0170 1022 ALA B N   
16469 C CA  . ALA B 1024 ? 0.1696 0.2070 0.2065 0.0108  0.0027  -0.0172 1022 ALA B CA  
16470 C C   . ALA B 1024 ? 0.1677 0.2072 0.2036 0.0103  0.0022  -0.0176 1022 ALA B C   
16471 O O   . ALA B 1024 ? 0.1606 0.2000 0.1966 0.0104  0.0018  -0.0180 1022 ALA B O   
16472 C CB  . ALA B 1024 ? 0.1885 0.2244 0.2258 0.0100  0.0027  -0.0176 1022 ALA B CB  
16473 N N   . GLY B 1025 ? 0.1492 0.1908 0.1839 0.0098  0.0022  -0.0175 1023 GLY B N   
16474 C CA  . GLY B 1025 ? 0.1739 0.2181 0.2078 0.0091  0.0018  -0.0177 1023 GLY B CA  
16475 C C   . GLY B 1025 ? 0.1578 0.2043 0.1922 0.0105  0.0018  -0.0175 1023 GLY B C   
16476 O O   . GLY B 1025 ? 0.1594 0.2084 0.1936 0.0101  0.0016  -0.0177 1023 GLY B O   
16477 N N   . GLY B 1026 ? 0.1654 0.2112 0.2003 0.0121  0.0021  -0.0172 1024 GLY B N   
16478 C CA  . GLY B 1026 ? 0.1680 0.2154 0.2030 0.0139  0.0021  -0.0171 1024 GLY B CA  
16479 C C   . GLY B 1026 ? 0.1623 0.2108 0.1970 0.0151  0.0022  -0.0164 1024 GLY B C   
16480 O O   . GLY B 1026 ? 0.1575 0.2052 0.1919 0.0145  0.0024  -0.0159 1024 GLY B O   
16481 N N   . PRO B 1027 ? 0.1626 0.2130 0.1973 0.0170  0.0021  -0.0162 1025 PRO B N   
16482 C CA  . PRO B 1027 ? 0.1434 0.1957 0.1777 0.0182  0.0020  -0.0155 1025 PRO B CA  
16483 C C   . PRO B 1027 ? 0.1491 0.1977 0.1829 0.0193  0.0021  -0.0148 1025 PRO B C   
16484 O O   . PRO B 1027 ? 0.1545 0.2041 0.1876 0.0202  0.0020  -0.0141 1025 PRO B O   
16485 C CB  . PRO B 1027 ? 0.1652 0.2209 0.1998 0.0202  0.0018  -0.0157 1025 PRO B CB  
16486 C CG  . PRO B 1027 ? 0.1851 0.2384 0.2197 0.0207  0.0020  -0.0165 1025 PRO B CG  
16487 C CD  . PRO B 1027 ? 0.1656 0.2169 0.2004 0.0182  0.0021  -0.0168 1025 PRO B CD  
16488 N N   . LEU B 1028 ? 0.1594 0.2038 0.1934 0.0192  0.0023  -0.0149 1026 LEU B N   
16489 C CA  . LEU B 1028 ? 0.1577 0.1986 0.1912 0.0198  0.0024  -0.0141 1026 LEU B CA  
16490 C C   . LEU B 1028 ? 0.1567 0.1964 0.1903 0.0181  0.0030  -0.0136 1026 LEU B C   
16491 O O   . LEU B 1028 ? 0.1953 0.2329 0.2285 0.0183  0.0033  -0.0126 1026 LEU B O   
16492 C CB  . LEU B 1028 ? 0.1661 0.2029 0.1998 0.0203  0.0022  -0.0143 1026 LEU B CB  
16493 C CG  . LEU B 1028 ? 0.2162 0.2531 0.2492 0.0224  0.0017  -0.0149 1026 LEU B CG  
16494 C CD1 . LEU B 1028 ? 0.2349 0.2668 0.2675 0.0228  0.0012  -0.0151 1026 LEU B CD1 
16495 C CD2 . LEU B 1028 ? 0.2477 0.2863 0.2797 0.0246  0.0015  -0.0143 1026 LEU B CD2 
16496 N N   . TYR B 1029 ? 0.1499 0.1911 0.1840 0.0165  0.0032  -0.0142 1027 TYR B N   
16497 C CA  . TYR B 1029 ? 0.1551 0.1949 0.1894 0.0152  0.0038  -0.0140 1027 TYR B CA  
16498 C C   . TYR B 1029 ? 0.1518 0.1921 0.1847 0.0153  0.0042  -0.0132 1027 TYR B C   
16499 O O   . TYR B 1029 ? 0.1491 0.1875 0.1821 0.0151  0.0049  -0.0125 1027 TYR B O   
16500 C CB  . TYR B 1029 ? 0.1639 0.2049 0.1984 0.0138  0.0036  -0.0149 1027 TYR B CB  
16501 C CG  . TYR B 1029 ? 0.1501 0.1893 0.1851 0.0127  0.0041  -0.0151 1027 TYR B CG  
16502 C CD1 . TYR B 1029 ? 0.1619 0.1991 0.1986 0.0125  0.0042  -0.0152 1027 TYR B CD1 
16503 C CD2 . TYR B 1029 ? 0.1748 0.2146 0.2087 0.0119  0.0043  -0.0154 1027 TYR B CD2 
16504 C CE1 . TYR B 1029 ? 0.1537 0.1900 0.1912 0.0118  0.0046  -0.0154 1027 TYR B CE1 
16505 C CE2 . TYR B 1029 ? 0.1635 0.2018 0.1978 0.0113  0.0048  -0.0158 1027 TYR B CE2 
16506 C CZ  . TYR B 1029 ? 0.1551 0.1919 0.1914 0.0113  0.0050  -0.0157 1027 TYR B CZ  
16507 O OH  . TYR B 1029 ? 0.1777 0.2136 0.2146 0.0110  0.0054  -0.0160 1027 TYR B OH  
16508 N N   . LEU B 1030 ? 0.1515 0.1945 0.1832 0.0155  0.0038  -0.0132 1028 LEU B N   
16509 C CA  . LEU B 1030 ? 0.1556 0.1990 0.1856 0.0155  0.0040  -0.0126 1028 LEU B CA  
16510 C C   . LEU B 1030 ? 0.1711 0.2128 0.2005 0.0168  0.0043  -0.0113 1028 LEU B C   
16511 O O   . LEU B 1030 ? 0.1642 0.2049 0.1923 0.0166  0.0049  -0.0105 1028 LEU B O   
16512 C CB  . LEU B 1030 ? 0.1573 0.2041 0.1862 0.0154  0.0032  -0.0128 1028 LEU B CB  
16513 C CG  . LEU B 1030 ? 0.1740 0.2221 0.2028 0.0136  0.0029  -0.0138 1028 LEU B CG  
16514 C CD1 . LEU B 1030 ? 0.2040 0.2556 0.2317 0.0132  0.0019  -0.0138 1028 LEU B CD1 
16515 C CD2 . LEU B 1030 ? 0.1979 0.2435 0.2258 0.0126  0.0035  -0.0142 1028 LEU B CD2 
16516 N N   . GLY B 1031 ? 0.1616 0.2027 0.1915 0.0182  0.0038  -0.0110 1029 GLY B N   
16517 C CA  . GLY B 1031 ? 0.1788 0.2176 0.2076 0.0194  0.0038  -0.0098 1029 GLY B CA  
16518 C C   . GLY B 1031 ? 0.1671 0.2025 0.1963 0.0186  0.0047  -0.0090 1029 GLY B C   
16519 O O   . GLY B 1031 ? 0.1923 0.2257 0.2202 0.0191  0.0048  -0.0076 1029 GLY B O   
16520 N N   . ARG B 1032 ? 0.1509 0.1858 0.1818 0.0172  0.0051  -0.0097 1030 ARG B N   
16521 C CA  . ARG B 1032 ? 0.1619 0.1945 0.1936 0.0162  0.0060  -0.0089 1030 ARG B CA  
16522 C C   . ARG B 1032 ? 0.1708 0.2044 0.2015 0.0155  0.0071  -0.0083 1030 ARG B C   
16523 O O   . ARG B 1032 ? 0.1846 0.2170 0.2158 0.0148  0.0081  -0.0073 1030 ARG B O   
16524 C CB  . ARG B 1032 ? 0.1810 0.2132 0.2151 0.0151  0.0060  -0.0098 1030 ARG B CB  
16525 C CG  . ARG B 1032 ? 0.1813 0.2114 0.2169 0.0141  0.0066  -0.0090 1030 ARG B CG  
16526 C CD  . ARG B 1032 ? 0.1922 0.2192 0.2275 0.0144  0.0060  -0.0081 1030 ARG B CD  
16527 N NE  . ARG B 1032 ? 0.1973 0.2226 0.2344 0.0129  0.0063  -0.0074 1030 ARG B NE  
16528 C CZ  . ARG B 1032 ? 0.2387 0.2619 0.2754 0.0122  0.0067  -0.0057 1030 ARG B CZ  
16529 N NH1 . ARG B 1032 ? 0.2522 0.2744 0.2865 0.0131  0.0068  -0.0045 1030 ARG B NH1 
16530 N NH2 . ARG B 1032 ? 0.2348 0.2571 0.2737 0.0105  0.0069  -0.0051 1030 ARG B NH2 
16531 N N   . LEU B 1033 ? 0.1705 0.2064 0.1998 0.0156  0.0070  -0.0090 1031 LEU B N   
16532 C CA  . LEU B 1033 ? 0.1607 0.1974 0.1887 0.0151  0.0080  -0.0089 1031 LEU B CA  
16533 C C   . LEU B 1033 ? 0.1787 0.2157 0.2037 0.0158  0.0080  -0.0079 1031 LEU B C   
16534 O O   . LEU B 1033 ? 0.1861 0.2239 0.2092 0.0156  0.0086  -0.0080 1031 LEU B O   
16535 C CB  . LEU B 1033 ? 0.1774 0.2156 0.2054 0.0145  0.0078  -0.0105 1031 LEU B CB  
16536 C CG  . LEU B 1033 ? 0.1628 0.2006 0.1933 0.0139  0.0075  -0.0114 1031 LEU B CG  
16537 C CD1 . LEU B 1033 ? 0.1845 0.2232 0.2145 0.0132  0.0071  -0.0128 1031 LEU B CD1 
16538 C CD2 . LEU B 1033 ? 0.1951 0.2316 0.2276 0.0134  0.0085  -0.0110 1031 LEU B CD2 
16539 N N   . VAL B 1034 ? 0.1744 0.2105 0.1988 0.0169  0.0073  -0.0069 1032 VAL B N   
16540 C CA  . VAL B 1034 ? 0.1935 0.2296 0.2151 0.0178  0.0071  -0.0057 1032 VAL B CA  
16541 C C   . VAL B 1034 ? 0.1957 0.2288 0.2172 0.0183  0.0072  -0.0041 1032 VAL B C   
16542 O O   . VAL B 1034 ? 0.2303 0.2615 0.2537 0.0180  0.0071  -0.0041 1032 VAL B O   
16543 C CB  . VAL B 1034 ? 0.1852 0.2237 0.2060 0.0189  0.0056  -0.0062 1032 VAL B CB  
16544 C CG1 . VAL B 1034 ? 0.2054 0.2465 0.2257 0.0179  0.0053  -0.0076 1032 VAL B CG1 
16545 C CG2 . VAL B 1034 ? 0.1964 0.2349 0.2191 0.0198  0.0046  -0.0067 1032 VAL B CG2 
16546 N N   . THR B 1035 ? 0.2243 0.2565 0.2431 0.0188  0.0074  -0.0025 1033 THR B N   
16547 C CA  . THR B 1035 ? 0.2432 0.2718 0.2613 0.0189  0.0076  -0.0007 1033 THR B CA  
16548 C C   . THR B 1035 ? 0.2676 0.2945 0.2854 0.0206  0.0060  -0.0005 1033 THR B C   
16549 O O   . THR B 1035 ? 0.3219 0.3450 0.3396 0.0206  0.0058  0.0006  1033 THR B O   
16550 C CB  . THR B 1035 ? 0.3076 0.3355 0.3226 0.0187  0.0085  0.0010  1033 THR B CB  
16551 O OG1 . THR B 1035 ? 0.3600 0.3898 0.3724 0.0199  0.0076  0.0008  1033 THR B OG1 
16552 C CG2 . THR B 1035 ? 0.3316 0.3606 0.3471 0.0171  0.0104  0.0010  1033 THR B CG2 
16553 N N   . THR B 1036 ? 0.2249 0.2543 0.2424 0.0221  0.0048  -0.0014 1034 THR B N   
16554 C CA  . THR B 1036 ? 0.2751 0.3037 0.2926 0.0242  0.0034  -0.0015 1034 THR B CA  
16555 C C   . THR B 1036 ? 0.2459 0.2780 0.2657 0.0244  0.0029  -0.0035 1034 THR B C   
16556 O O   . THR B 1036 ? 0.2375 0.2736 0.2573 0.0241  0.0027  -0.0042 1034 THR B O   
16557 C CB  . THR B 1036 ? 0.3329 0.3620 0.3476 0.0261  0.0024  -0.0004 1034 THR B CB  
16558 O OG1 . THR B 1036 ? 0.4167 0.4427 0.4288 0.0256  0.0030  0.0015  1034 THR B OG1 
16559 C CG2 . THR B 1036 ? 0.3806 0.4085 0.3953 0.0287  0.0010  -0.0004 1034 THR B CG2 
16560 N N   . ALA B 1037 ? 0.2461 0.2769 0.2677 0.0247  0.0026  -0.0043 1035 ALA B N   
16561 C CA  . ALA B 1037 ? 0.2047 0.2388 0.2283 0.0247  0.0023  -0.0061 1035 ALA B CA  
16562 C C   . ALA B 1037 ? 0.2080 0.2456 0.2313 0.0269  0.0012  -0.0063 1035 ALA B C   
16563 O O   . ALA B 1037 ? 0.2261 0.2621 0.2481 0.0292  0.0004  -0.0056 1035 ALA B O   
16564 C CB  . ALA B 1037 ? 0.2507 0.2822 0.2759 0.0247  0.0022  -0.0068 1035 ALA B CB  
16565 N N   . PRO B 1038 ? 0.1783 0.2207 0.2028 0.0263  0.0010  -0.0074 1036 PRO B N   
16566 C CA  . PRO B 1038 ? 0.1768 0.2235 0.2017 0.0282  0.0000  -0.0077 1036 PRO B CA  
16567 C C   . PRO B 1038 ? 0.1814 0.2280 0.2077 0.0295  -0.0001 -0.0087 1036 PRO B C   
16568 O O   . PRO B 1038 ? 0.1903 0.2337 0.2173 0.0287  0.0004  -0.0092 1036 PRO B O   
16569 C CB  . PRO B 1038 ? 0.2204 0.2717 0.2461 0.0263  0.0000  -0.0085 1036 PRO B CB  
16570 C CG  . PRO B 1038 ? 0.2385 0.2877 0.2650 0.0239  0.0010  -0.0092 1036 PRO B CG  
16571 C CD  . PRO B 1038 ? 0.2097 0.2537 0.2351 0.0238  0.0017  -0.0083 1036 PRO B CD  
16572 N N   . VAL B 1039 ? 0.2059 0.2564 0.2327 0.0317  -0.0009 -0.0089 1037 VAL B N   
16573 C CA  . VAL B 1039 ? 0.2075 0.2593 0.2355 0.0332  -0.0009 -0.0100 1037 VAL B CA  
16574 C C   . VAL B 1039 ? 0.1894 0.2459 0.2195 0.0310  -0.0005 -0.0110 1037 VAL B C   
16575 O O   . VAL B 1039 ? 0.1895 0.2514 0.2203 0.0305  -0.0009 -0.0109 1037 VAL B O   
16576 C CB  . VAL B 1039 ? 0.1951 0.2495 0.2228 0.0368  -0.0017 -0.0097 1037 VAL B CB  
16577 C CG1 . VAL B 1039 ? 0.2294 0.2856 0.2584 0.0385  -0.0015 -0.0110 1037 VAL B CG1 
16578 C CG2 . VAL B 1039 ? 0.2296 0.2785 0.2549 0.0389  -0.0023 -0.0086 1037 VAL B CG2 
16579 N N   . PRO B 1040 ? 0.1794 0.2340 0.2102 0.0296  0.0001  -0.0120 1038 PRO B N   
16580 C CA  . PRO B 1040 ? 0.1797 0.2382 0.2120 0.0273  0.0004  -0.0128 1038 PRO B CA  
16581 C C   . PRO B 1040 ? 0.1771 0.2416 0.2106 0.0286  0.0002  -0.0132 1038 PRO B C   
16582 O O   . PRO B 1040 ? 0.1842 0.2492 0.2176 0.0317  0.0000  -0.0133 1038 PRO B O   
16583 C CB  . PRO B 1040 ? 0.2113 0.2656 0.2438 0.0261  0.0010  -0.0135 1038 PRO B CB  
16584 C CG  . PRO B 1040 ? 0.2327 0.2812 0.2641 0.0267  0.0010  -0.0129 1038 PRO B CG  
16585 C CD  . PRO B 1040 ? 0.1984 0.2468 0.2286 0.0295  0.0005  -0.0121 1038 PRO B CD  
16586 N N   . PRO B 1041 ? 0.1880 0.2572 0.2227 0.0264  0.0002  -0.0135 1039 PRO B N   
16587 C CA  . PRO B 1041 ? 0.1810 0.2564 0.2172 0.0273  0.0002  -0.0138 1039 PRO B CA  
16588 C C   . PRO B 1041 ? 0.1779 0.2517 0.2141 0.0290  0.0009  -0.0147 1039 PRO B C   
16589 O O   . PRO B 1041 ? 0.1952 0.2642 0.2308 0.0279  0.0012  -0.0152 1039 PRO B O   
16590 C CB  . PRO B 1041 ? 0.2045 0.2831 0.2415 0.0237  0.0002  -0.0140 1039 PRO B CB  
16591 C CG  . PRO B 1041 ? 0.2463 0.3214 0.2820 0.0217  -0.0001 -0.0136 1039 PRO B CG  
16592 C CD  . PRO B 1041 ? 0.2117 0.2802 0.2462 0.0230  0.0003  -0.0136 1039 PRO B CD  
16593 N N   . GLN B 1042 ? 0.1947 0.2726 0.2316 0.0318  0.0009  -0.0149 1040 GLN B N   
16594 C CA  . GLN B 1042 ? 0.2003 0.2777 0.2369 0.0339  0.0015  -0.0158 1040 GLN B CA  
16595 C C   . GLN B 1042 ? 0.1870 0.2564 0.2215 0.0356  0.0014  -0.0162 1040 GLN B C   
16596 O O   . GLN B 1042 ? 0.2032 0.2707 0.2370 0.0369  0.0017  -0.0172 1040 GLN B O   
16597 C CB  . GLN B 1042 ? 0.2268 0.3058 0.2640 0.0312  0.0022  -0.0165 1040 GLN B CB  
16598 C CG  . GLN B 1042 ? 0.3029 0.3898 0.3420 0.0292  0.0022  -0.0160 1040 GLN B CG  
16599 C CD  . GLN B 1042 ? 0.3409 0.4287 0.3802 0.0265  0.0029  -0.0165 1040 GLN B CD  
16600 O OE1 . GLN B 1042 ? 0.4739 0.5569 0.5123 0.0240  0.0028  -0.0167 1040 GLN B OE1 
16601 N NE2 . GLN B 1042 ? 0.4931 0.5869 0.5333 0.0273  0.0036  -0.0166 1040 GLN B NE2 
16602 N N   . HIS B 1043 ? 0.1861 0.2509 0.2196 0.0356  0.0008  -0.0155 1041 HIS B N   
16603 C CA  . HIS B 1043 ? 0.1845 0.2414 0.2162 0.0363  0.0006  -0.0156 1041 HIS B CA  
16604 C C   . HIS B 1043 ? 0.1776 0.2326 0.2078 0.0404  0.0001  -0.0156 1041 HIS B C   
16605 O O   . HIS B 1043 ? 0.2075 0.2609 0.2368 0.0416  -0.0005 -0.0145 1041 HIS B O   
16606 C CB  . HIS B 1043 ? 0.1838 0.2368 0.2151 0.0339  0.0005  -0.0147 1041 HIS B CB  
16607 C CG  . HIS B 1043 ? 0.1930 0.2385 0.2228 0.0340  0.0003  -0.0146 1041 HIS B CG  
16608 N ND1 . HIS B 1043 ? 0.2043 0.2464 0.2343 0.0321  0.0005  -0.0153 1041 HIS B ND1 
16609 C CD2 . HIS B 1043 ? 0.2231 0.2639 0.2513 0.0356  -0.0002 -0.0138 1041 HIS B CD2 
16610 C CE1 . HIS B 1043 ? 0.2064 0.2422 0.2351 0.0323  0.0001  -0.0149 1041 HIS B CE1 
16611 N NE2 . HIS B 1043 ? 0.1929 0.2276 0.2203 0.0343  -0.0003 -0.0140 1041 HIS B NE2 
16612 N N   . SER B 1044 ? 0.1578 0.2127 0.1873 0.0428  0.0003  -0.0167 1042 SER B N   
16613 C CA  . SER B 1044 ? 0.1674 0.2193 0.1948 0.0471  -0.0003 -0.0169 1042 SER B CA  
16614 C C   . SER B 1044 ? 0.1737 0.2237 0.1999 0.0486  0.0001  -0.0185 1042 SER B C   
16615 O O   . SER B 1044 ? 0.1895 0.2420 0.2168 0.0466  0.0008  -0.0192 1042 SER B O   
16616 C CB  . SER B 1044 ? 0.1832 0.2419 0.2117 0.0501  -0.0004 -0.0165 1042 SER B CB  
16617 O OG  . SER B 1044 ? 0.1899 0.2560 0.2203 0.0503  0.0004  -0.0173 1042 SER B OG  
16618 N N   . SER B 1045 ? 0.1704 0.2158 0.1941 0.0523  -0.0005 -0.0190 1043 SER B N   
16619 C CA  . SER B 1045 ? 0.1746 0.2180 0.1965 0.0544  -0.0003 -0.0207 1043 SER B CA  
16620 C C   . SER B 1045 ? 0.1950 0.2370 0.2147 0.0597  -0.0008 -0.0211 1043 SER B C   
16621 O O   . SER B 1045 ? 0.2072 0.2451 0.2255 0.0612  -0.0018 -0.0202 1043 SER B O   
16622 C CB  . SER B 1045 ? 0.1977 0.2323 0.2176 0.0524  -0.0009 -0.0212 1043 SER B CB  
16623 O OG  . SER B 1045 ? 0.2134 0.2450 0.2307 0.0547  -0.0009 -0.0229 1043 SER B OG  
16624 N N   . VAL B 1046 ? 0.1799 0.2253 0.1990 0.0628  -0.0001 -0.0225 1044 VAL B N   
16625 C CA  . VAL B 1046 ? 0.2027 0.2463 0.2193 0.0684  -0.0006 -0.0232 1044 VAL B CA  
16626 C C   . VAL B 1046 ? 0.2174 0.2503 0.2296 0.0699  -0.0016 -0.0244 1044 VAL B C   
16627 O O   . VAL B 1046 ? 0.2246 0.2538 0.2338 0.0746  -0.0023 -0.0251 1044 VAL B O   
16628 C CB  . VAL B 1046 ? 0.2217 0.2743 0.2396 0.0716  0.0007  -0.0242 1044 VAL B CB  
16629 C CG1 . VAL B 1046 ? 0.2514 0.3147 0.2738 0.0700  0.0013  -0.0229 1044 VAL B CG1 
16630 C CG2 . VAL B 1046 ? 0.2389 0.2917 0.2560 0.0705  0.0017  -0.0258 1044 VAL B CG2 
16631 N N   . HIS B 1047 ? 0.2096 0.2371 0.2210 0.0661  -0.0018 -0.0247 1045 HIS B N   
16632 C CA  A HIS B 1047 ? 0.2378 0.2552 0.2450 0.0670  -0.0029 -0.0258 1045 HIS B CA  
16633 C CA  B HIS B 1047 ? 0.2378 0.2550 0.2450 0.0667  -0.0029 -0.0258 1045 HIS B CA  
16634 C C   . HIS B 1047 ? 0.2045 0.2136 0.2100 0.0660  -0.0045 -0.0245 1045 HIS B C   
16635 O O   . HIS B 1047 ? 0.2355 0.2457 0.2434 0.0626  -0.0045 -0.0228 1045 HIS B O   
16636 C CB  A HIS B 1047 ? 0.2349 0.2509 0.2421 0.0634  -0.0026 -0.0268 1045 HIS B CB  
16637 C CB  B HIS B 1047 ? 0.2299 0.2457 0.2377 0.0624  -0.0027 -0.0264 1045 HIS B CB  
16638 C CG  A HIS B 1047 ? 0.2296 0.2540 0.2384 0.0639  -0.0010 -0.0278 1045 HIS B CG  
16639 C CG  B HIS B 1047 ? 0.2204 0.2255 0.2247 0.0614  -0.0042 -0.0270 1045 HIS B CG  
16640 N ND1 A HIS B 1047 ? 0.2437 0.2694 0.2502 0.0682  -0.0005 -0.0295 1045 HIS B ND1 
16641 N ND1 B HIS B 1047 ? 0.2697 0.2690 0.2697 0.0645  -0.0049 -0.0289 1045 HIS B ND1 
16642 C CD2 A HIS B 1047 ? 0.2711 0.3033 0.2835 0.0607  0.0002  -0.0272 1045 HIS B CD2 
16643 C CD2 B HIS B 1047 ? 0.2281 0.2275 0.2327 0.0574  -0.0051 -0.0260 1045 HIS B CD2 
16644 C CE1 A HIS B 1047 ? 0.2934 0.3275 0.3020 0.0674  0.0011  -0.0298 1045 HIS B CE1 
16645 C CE1 B HIS B 1047 ? 0.2655 0.2557 0.2632 0.0623  -0.0064 -0.0290 1045 HIS B CE1 
16646 N NE2 A HIS B 1047 ? 0.2454 0.2833 0.2576 0.0628  0.0014  -0.0284 1045 HIS B NE2 
16647 N NE2 B HIS B 1047 ? 0.2735 0.2640 0.2741 0.0579  -0.0065 -0.0272 1045 HIS B NE2 
16648 N N   . THR B 1048 ? 0.2178 0.2184 0.2190 0.0691  -0.0057 -0.0253 1046 THR B N   
16649 C CA  . THR B 1048 ? 0.2501 0.2416 0.2489 0.0681  -0.0073 -0.0240 1046 THR B CA  
16650 C C   . THR B 1048 ? 0.2212 0.2033 0.2168 0.0663  -0.0085 -0.0251 1046 THR B C   
16651 O O   . THR B 1048 ? 0.2477 0.2268 0.2401 0.0692  -0.0088 -0.0272 1046 THR B O   
16652 C CB  . THR B 1048 ? 0.2664 0.2546 0.2623 0.0731  -0.0083 -0.0237 1046 THR B CB  
16653 O OG1 . THR B 1048 ? 0.2439 0.2419 0.2429 0.0753  -0.0073 -0.0230 1046 THR B OG1 
16654 C CG2 . THR B 1048 ? 0.2823 0.2622 0.2764 0.0713  -0.0098 -0.0219 1046 THR B CG2 
16655 N N   . ASP B 1049 ? 0.2247 0.2027 0.2212 0.0617  -0.0091 -0.0238 1047 ASP B N   
16656 C CA  . ASP B 1049 ? 0.2381 0.2076 0.2319 0.0596  -0.0104 -0.0247 1047 ASP B CA  
16657 C C   . ASP B 1049 ? 0.2250 0.1846 0.2132 0.0632  -0.0122 -0.0255 1047 ASP B C   
16658 O O   . ASP B 1049 ? 0.2462 0.2025 0.2329 0.0650  -0.0129 -0.0241 1047 ASP B O   
16659 C CB  . ASP B 1049 ? 0.2117 0.1791 0.2078 0.0542  -0.0108 -0.0228 1047 ASP B CB  
16660 C CG  . ASP B 1049 ? 0.2414 0.2010 0.2354 0.0514  -0.0122 -0.0235 1047 ASP B CG  
16661 O OD1 . ASP B 1049 ? 0.2531 0.2034 0.2431 0.0521  -0.0139 -0.0233 1047 ASP B OD1 
16662 O OD2 . ASP B 1049 ? 0.2517 0.2144 0.2478 0.0487  -0.0117 -0.0242 1047 ASP B OD2 
16663 N N   . PRO B 1050 ? 0.2500 0.2044 0.2345 0.0647  -0.0130 -0.0277 1048 PRO B N   
16664 C CA  . PRO B 1050 ? 0.2846 0.2293 0.2631 0.0689  -0.0147 -0.0287 1048 PRO B CA  
16665 C C   . PRO B 1050 ? 0.2759 0.2100 0.2519 0.0660  -0.0168 -0.0273 1048 PRO B C   
16666 O O   . PRO B 1050 ? 0.2951 0.2214 0.2667 0.0690  -0.0182 -0.0272 1048 PRO B O   
16667 C CB  . PRO B 1050 ? 0.3241 0.2671 0.2996 0.0707  -0.0148 -0.0315 1048 PRO B CB  
16668 C CG  . PRO B 1050 ? 0.3127 0.2605 0.2920 0.0657  -0.0140 -0.0315 1048 PRO B CG  
16669 C CD  . PRO B 1050 ? 0.2736 0.2312 0.2589 0.0634  -0.0123 -0.0294 1048 PRO B CD  
16670 N N   . VAL B 1051 ? 0.2862 0.2197 0.2647 0.0602  -0.0170 -0.0263 1049 VAL B N   
16671 C CA  . VAL B 1051 ? 0.2791 0.2034 0.2558 0.0569  -0.0189 -0.0247 1049 VAL B CA  
16672 C C   . VAL B 1051 ? 0.2682 0.1937 0.2462 0.0566  -0.0185 -0.0220 1049 VAL B C   
16673 O O   . VAL B 1051 ? 0.2940 0.2110 0.2684 0.0570  -0.0201 -0.0208 1049 VAL B O   
16674 C CB  . VAL B 1051 ? 0.3017 0.2260 0.2810 0.0509  -0.0192 -0.0243 1049 VAL B CB  
16675 C CG1 . VAL B 1051 ? 0.3477 0.2637 0.3258 0.0471  -0.0209 -0.0223 1049 VAL B CG1 
16676 C CG2 . VAL B 1051 ? 0.3324 0.2544 0.3094 0.0515  -0.0199 -0.0271 1049 VAL B CG2 
16677 N N   . LEU B 1052 ? 0.2434 0.1795 0.2265 0.0560  -0.0165 -0.0209 1050 LEU B N   
16678 C CA  . LEU B 1052 ? 0.2481 0.1863 0.2321 0.0568  -0.0160 -0.0187 1050 LEU B CA  
16679 C C   . LEU B 1052 ? 0.2895 0.2228 0.2689 0.0625  -0.0171 -0.0191 1050 LEU B C   
16680 O O   . LEU B 1052 ? 0.2802 0.2075 0.2570 0.0628  -0.0182 -0.0173 1050 LEU B O   
16681 C CB  . LEU B 1052 ? 0.2411 0.1915 0.2304 0.0562  -0.0138 -0.0182 1050 LEU B CB  
16682 C CG  . LEU B 1052 ? 0.2316 0.1859 0.2225 0.0568  -0.0132 -0.0159 1050 LEU B CG  
16683 C CD1 . LEU B 1052 ? 0.2769 0.2323 0.2656 0.0627  -0.0135 -0.0163 1050 LEU B CD1 
16684 C CD2 . LEU B 1052 ? 0.2560 0.2037 0.2456 0.0534  -0.0141 -0.0135 1050 LEU B CD2 
16685 N N   . LEU B 1053 ? 0.2880 0.2240 0.2662 0.0672  -0.0167 -0.0214 1051 LEU B N   
16686 C CA  . LEU B 1053 ? 0.3177 0.2497 0.2916 0.0733  -0.0176 -0.0219 1051 LEU B CA  
16687 C C   . LEU B 1053 ? 0.3000 0.2178 0.2676 0.0738  -0.0201 -0.0220 1051 LEU B C   
16688 O O   . LEU B 1053 ? 0.3292 0.2413 0.2935 0.0764  -0.0213 -0.0208 1051 LEU B O   
16689 C CB  . LEU B 1053 ? 0.3644 0.3019 0.3381 0.0782  -0.0166 -0.0246 1051 LEU B CB  
16690 C CG  . LEU B 1053 ? 0.3440 0.2954 0.3232 0.0790  -0.0144 -0.0243 1051 LEU B CG  
16691 C CD1 . LEU B 1053 ? 0.3508 0.3075 0.3298 0.0829  -0.0133 -0.0269 1051 LEU B CD1 
16692 C CD2 . LEU B 1053 ? 0.3638 0.3181 0.3436 0.0818  -0.0144 -0.0225 1051 LEU B CD2 
16693 N N   . ASP B 1054 ? 0.3058 0.2175 0.2716 0.0710  -0.0211 -0.0233 1052 ASP B N   
16694 C CA  . ASP B 1054 ? 0.3422 0.2399 0.3018 0.0708  -0.0237 -0.0233 1052 ASP B CA  
16695 C C   . ASP B 1054 ? 0.3067 0.1999 0.2666 0.0665  -0.0246 -0.0201 1052 ASP B C   
16696 O O   . ASP B 1054 ? 0.3416 0.2244 0.2964 0.0678  -0.0265 -0.0192 1052 ASP B O   
16697 C CB  . ASP B 1054 ? 0.3373 0.2301 0.2952 0.0682  -0.0247 -0.0253 1052 ASP B CB  
16698 C CG  . ASP B 1054 ? 0.4043 0.2990 0.3600 0.0731  -0.0242 -0.0286 1052 ASP B CG  
16699 O OD1 . ASP B 1054 ? 0.4095 0.3068 0.3638 0.0790  -0.0236 -0.0294 1052 ASP B OD1 
16700 O OD2 . ASP B 1054 ? 0.4489 0.3426 0.4042 0.0711  -0.0245 -0.0303 1052 ASP B OD2 
16701 N N   . PHE B 1055 ? 0.3011 0.2017 0.2667 0.0616  -0.0231 -0.0183 1053 PHE B N   
16702 C CA  . PHE B 1055 ? 0.3149 0.2126 0.2812 0.0575  -0.0235 -0.0151 1053 PHE B CA  
16703 C C   . PHE B 1055 ? 0.3239 0.2218 0.2887 0.0611  -0.0235 -0.0134 1053 PHE B C   
16704 O O   . PHE B 1055 ? 0.3304 0.2198 0.2915 0.0604  -0.0250 -0.0114 1053 PHE B O   
16705 C CB  . PHE B 1055 ? 0.2902 0.1970 0.2630 0.0521  -0.0216 -0.0140 1053 PHE B CB  
16706 C CG  . PHE B 1055 ? 0.3114 0.2160 0.2852 0.0475  -0.0217 -0.0108 1053 PHE B CG  
16707 C CD1 . PHE B 1055 ? 0.3233 0.2175 0.2938 0.0443  -0.0237 -0.0097 1053 PHE B CD1 
16708 C CD2 . PHE B 1055 ? 0.2847 0.1979 0.2627 0.0461  -0.0199 -0.0089 1053 PHE B CD2 
16709 C CE1 . PHE B 1055 ? 0.3405 0.2332 0.3120 0.0398  -0.0236 -0.0066 1053 PHE B CE1 
16710 C CE2 . PHE B 1055 ? 0.3083 0.2198 0.2870 0.0419  -0.0197 -0.0059 1053 PHE B CE2 
16711 C CZ  . PHE B 1055 ? 0.3109 0.2125 0.2865 0.0388  -0.0215 -0.0047 1053 PHE B CZ  
16712 N N   . ALA B 1056 ? 0.3042 0.2116 0.2716 0.0649  -0.0219 -0.0141 1054 ALA B N   
16713 C CA  . ALA B 1056 ? 0.3299 0.2383 0.2961 0.0687  -0.0220 -0.0126 1054 ALA B CA  
16714 C C   . ALA B 1056 ? 0.3126 0.2097 0.2719 0.0734  -0.0243 -0.0131 1054 ALA B C   
16715 O O   . ALA B 1056 ? 0.3346 0.2263 0.2910 0.0742  -0.0254 -0.0109 1054 ALA B O   
16716 C CB  . ALA B 1056 ? 0.3384 0.2593 0.3087 0.0721  -0.0201 -0.0136 1054 ALA B CB  
16717 N N   . LYS B 1057 ? 0.3470 0.2402 0.3032 0.0768  -0.0250 -0.0160 1055 LYS B N   
16718 C CA  . LYS B 1057 ? 0.3728 0.2544 0.3219 0.0816  -0.0273 -0.0167 1055 LYS B CA  
16719 C C   . LYS B 1057 ? 0.4097 0.2781 0.3543 0.0776  -0.0295 -0.0149 1055 LYS B C   
16720 O O   . LYS B 1057 ? 0.4080 0.2675 0.3476 0.0801  -0.0313 -0.0136 1055 LYS B O   
16721 C CB  . LYS B 1057 ? 0.4100 0.2899 0.3565 0.0855  -0.0275 -0.0203 1055 LYS B CB  
16722 C CG  . LYS B 1057 ? 0.4531 0.3442 0.4024 0.0911  -0.0257 -0.0220 1055 LYS B CG  
16723 C CD  . LYS B 1057 ? 0.3946 0.2832 0.3406 0.0951  -0.0258 -0.0255 1055 LYS B CD  
16724 C CE  . LYS B 1057 ? 0.4249 0.3132 0.3722 0.0899  -0.0256 -0.0268 1055 LYS B CE  
16725 N NZ  . LYS B 1057 ? 0.4583 0.3471 0.4032 0.0939  -0.0252 -0.0302 1055 LYS B NZ  
16726 N N   . TRP B 1058 ? 0.3907 0.2577 0.3371 0.0714  -0.0296 -0.0147 1056 TRP B N   
16727 C CA  . TRP B 1058 ? 0.4110 0.2668 0.3541 0.0667  -0.0316 -0.0127 1056 TRP B CA  
16728 C C   . TRP B 1058 ? 0.3718 0.2280 0.3157 0.0646  -0.0313 -0.0090 1056 TRP B C   
16729 O O   . TRP B 1058 ? 0.4093 0.2546 0.3480 0.0646  -0.0334 -0.0073 1056 TRP B O   
16730 C CB  . TRP B 1058 ? 0.3953 0.2522 0.3415 0.0603  -0.0313 -0.0131 1056 TRP B CB  
16731 C CG  . TRP B 1058 ? 0.4125 0.2593 0.3562 0.0546  -0.0333 -0.0110 1056 TRP B CG  
16732 C CD1 . TRP B 1058 ? 0.5021 0.3353 0.4395 0.0543  -0.0361 -0.0117 1056 TRP B CD1 
16733 C CD2 . TRP B 1058 ? 0.4168 0.2667 0.3646 0.0483  -0.0324 -0.0079 1056 TRP B CD2 
16734 N NE1 . TRP B 1058 ? 0.4784 0.3062 0.4158 0.0478  -0.0372 -0.0090 1056 TRP B NE1 
16735 C CE2 . TRP B 1058 ? 0.4613 0.2994 0.4051 0.0441  -0.0349 -0.0066 1056 TRP B CE2 
16736 C CE3 . TRP B 1058 ? 0.3935 0.2549 0.3476 0.0457  -0.0299 -0.0060 1056 TRP B CE3 
16737 C CZ2 . TRP B 1058 ? 0.4596 0.2979 0.4060 0.0375  -0.0346 -0.0035 1056 TRP B CZ2 
16738 C CZ3 . TRP B 1058 ? 0.4626 0.3237 0.4189 0.0395  -0.0296 -0.0031 1056 TRP B CZ3 
16739 C CH2 . TRP B 1058 ? 0.4351 0.2852 0.3878 0.0355  -0.0319 -0.0017 1056 TRP B CH2 
16740 N N   . LEU B 1059 ? 0.3449 0.2133 0.2951 0.0629  -0.0289 -0.0078 1057 LEU B N   
16741 C CA  . LEU B 1059 ? 0.3898 0.2595 0.3406 0.0614  -0.0285 -0.0044 1057 LEU B CA  
16742 C C   . LEU B 1059 ? 0.4306 0.2955 0.3765 0.0676  -0.0298 -0.0039 1057 LEU B C   
16743 O O   . LEU B 1059 ? 0.4455 0.3027 0.3876 0.0668  -0.0311 -0.0013 1057 LEU B O   
16744 C CB  . LEU B 1059 ? 0.3496 0.2334 0.3074 0.0595  -0.0258 -0.0037 1057 LEU B CB  
16745 C CG  . LEU B 1059 ? 0.3323 0.2209 0.2951 0.0530  -0.0244 -0.0035 1057 LEU B CG  
16746 C CD1 . LEU B 1059 ? 0.3280 0.2301 0.2970 0.0523  -0.0218 -0.0034 1057 LEU B CD1 
16747 C CD2 . LEU B 1059 ? 0.3929 0.2747 0.3544 0.0473  -0.0252 -0.0005 1057 LEU B CD2 
16748 N N   . ASP B 1060 ? 0.4248 0.2946 0.3709 0.0738  -0.0294 -0.0063 1058 ASP B N   
16749 C CA  . ASP B 1060 ? 0.4282 0.2937 0.3697 0.0805  -0.0307 -0.0063 1058 ASP B CA  
16750 C C   . ASP B 1060 ? 0.4693 0.3184 0.4029 0.0812  -0.0337 -0.0057 1058 ASP B C   
16751 O O   . ASP B 1060 ? 0.5191 0.3618 0.4488 0.0826  -0.0351 -0.0034 1058 ASP B O   
16752 C CB  . ASP B 1060 ? 0.4632 0.3348 0.4055 0.0870  -0.0301 -0.0096 1058 ASP B CB  
16753 C CG  . ASP B 1060 ? 0.5013 0.3887 0.4503 0.0880  -0.0276 -0.0097 1058 ASP B CG  
16754 O OD1 . ASP B 1060 ? 0.4719 0.3646 0.4235 0.0862  -0.0269 -0.0072 1058 ASP B OD1 
16755 O OD2 . ASP B 1060 ? 0.5073 0.4018 0.4588 0.0907  -0.0264 -0.0124 1058 ASP B OD2 
16756 N N   . GLY B 1061 ? 0.4572 0.2990 0.3881 0.0803  -0.0348 -0.0079 1059 GLY B N   
16757 C CA  . GLY B 1061 ? 0.5224 0.3479 0.4453 0.0811  -0.0378 -0.0078 1059 GLY B CA  
16758 C C   . GLY B 1061 ? 0.5298 0.3475 0.4508 0.0752  -0.0390 -0.0041 1059 GLY B C   
16759 O O   . GLY B 1061 ? 0.5537 0.3584 0.4678 0.0766  -0.0415 -0.0029 1059 GLY B O   
16760 N N   . LYS B 1062 ? 0.4941 0.3192 0.4208 0.0686  -0.0373 -0.0022 1060 LYS B N   
16761 C CA  . LYS B 1062 ? 0.5132 0.3328 0.4389 0.0627  -0.0379 0.0016  1060 LYS B CA  
16762 C C   . LYS B 1062 ? 0.5440 0.3667 0.4696 0.0642  -0.0373 0.0046  1060 LYS B C   
16763 O O   . LYS B 1062 ? 0.6213 0.4395 0.5456 0.0597  -0.0377 0.0080  1060 LYS B O   
16764 C CB  . LYS B 1062 ? 0.5127 0.3398 0.4447 0.0553  -0.0361 0.0024  1060 LYS B CB  
16765 C CG  . LYS B 1062 ? 0.5354 0.3591 0.4676 0.0525  -0.0369 0.0000  1060 LYS B CG  
16766 C CD  . LYS B 1062 ? 0.5520 0.3828 0.4904 0.0451  -0.0352 0.0014  1060 LYS B CD  
16767 C CE  . LYS B 1062 ? 0.5268 0.3528 0.4642 0.0397  -0.0357 0.0055  1060 LYS B CE  
16768 N NZ  . LYS B 1062 ? 0.6086 0.4375 0.5504 0.0323  -0.0350 0.0064  1060 LYS B NZ  
16769 N N   . GLY B 1063 ? 0.5109 0.3415 0.4381 0.0702  -0.0363 0.0035  1061 GLY B N   
16770 C CA  . GLY B 1063 ? 0.5342 0.3691 0.4619 0.0713  -0.0357 0.0063  1061 GLY B CA  
16771 C C   . GLY B 1063 ? 0.5383 0.3851 0.4728 0.0662  -0.0330 0.0080  1061 GLY B C   
16772 O O   . GLY B 1063 ? 0.5093 0.3589 0.4439 0.0662  -0.0325 0.0106  1061 GLY B O   
16773 N N   . ALA B 1064 ? 0.4846 0.3381 0.4244 0.0621  -0.0313 0.0066  1062 ALA B N   
16774 C CA  . ALA B 1064 ? 0.4475 0.3127 0.3938 0.0577  -0.0287 0.0078  1062 ALA B CA  
16775 C C   . ALA B 1064 ? 0.4475 0.3251 0.3979 0.0621  -0.0271 0.0063  1062 ALA B C   
16776 O O   . ALA B 1064 ? 0.3949 0.2814 0.3502 0.0619  -0.0255 0.0040  1062 ALA B O   
16777 C CB  . ALA B 1064 ? 0.4638 0.3314 0.4141 0.0522  -0.0277 0.0068  1062 ALA B CB  
16778 N N   . ARG B 1065 ? 0.4468 0.3245 0.3949 0.0660  -0.0276 0.0078  1063 ARG B N   
16779 C CA  . ARG B 1065 ? 0.4442 0.3320 0.3950 0.0712  -0.0268 0.0063  1063 ARG B CA  
16780 C C   . ARG B 1065 ? 0.4137 0.3149 0.3714 0.0681  -0.0242 0.0063  1063 ARG B C   
16781 O O   . ARG B 1065 ? 0.3906 0.3009 0.3524 0.0700  -0.0230 0.0039  1063 ARG B O   
16782 C CB  . ARG B 1065 ? 0.4786 0.3631 0.4252 0.0759  -0.0283 0.0081  1063 ARG B CB  
16783 N N   . ALA B 1066 ? 0.3538 0.2563 0.3125 0.0634  -0.0233 0.0090  1064 ALA B N   
16784 C CA  . ALA B 1066 ? 0.3843 0.2987 0.3488 0.0604  -0.0209 0.0090  1064 ALA B CA  
16785 C C   . ALA B 1066 ? 0.3684 0.2870 0.3373 0.0575  -0.0196 0.0067  1064 ALA B C   
16786 O O   . ALA B 1066 ? 0.3721 0.3009 0.3457 0.0578  -0.0181 0.0050  1064 ALA B O   
16787 C CB  . ALA B 1066 ? 0.4089 0.3227 0.3731 0.0557  -0.0202 0.0123  1064 ALA B CB  
16788 N N   . GLU B 1067 ? 0.3652 0.2759 0.3325 0.0545  -0.0204 0.0065  1065 GLU B N   
16789 C CA  . GLU B 1067 ? 0.3559 0.2700 0.3271 0.0516  -0.0193 0.0044  1065 GLU B CA  
16790 C C   . GLU B 1067 ? 0.3183 0.2354 0.2903 0.0560  -0.0195 0.0011  1065 GLU B C   
16791 O O   . GLU B 1067 ? 0.3053 0.2307 0.2818 0.0550  -0.0180 -0.0007 1065 GLU B O   
16792 C CB  . GLU B 1067 ? 0.3642 0.2689 0.3333 0.0473  -0.0204 0.0052  1065 GLU B CB  
16793 C CG  . GLU B 1067 ? 0.3586 0.2625 0.3283 0.0419  -0.0196 0.0084  1065 GLU B CG  
16794 C CD  . GLU B 1067 ? 0.4124 0.3090 0.3769 0.0429  -0.0209 0.0113  1065 GLU B CD  
16795 O OE1 . GLU B 1067 ? 0.4110 0.3016 0.3710 0.0478  -0.0227 0.0108  1065 GLU B OE1 
16796 O OE2 . GLU B 1067 ? 0.4010 0.2978 0.3657 0.0389  -0.0200 0.0141  1065 GLU B OE2 
16797 N N   . ALA B 1068 ? 0.3314 0.2418 0.2987 0.0610  -0.0213 0.0002  1066 ALA B N   
16798 C CA  . ALA B 1068 ? 0.3398 0.2534 0.3075 0.0658  -0.0213 -0.0029 1066 ALA B CA  
16799 C C   . ALA B 1068 ? 0.3267 0.2532 0.2990 0.0680  -0.0196 -0.0034 1066 ALA B C   
16800 O O   . ALA B 1068 ? 0.3109 0.2445 0.2866 0.0687  -0.0185 -0.0057 1066 ALA B O   
16801 C CB  . ALA B 1068 ? 0.3444 0.2486 0.3060 0.0713  -0.0235 -0.0034 1066 ALA B CB  
16802 N N   . GLU B 1069 ? 0.3119 0.2414 0.2843 0.0688  -0.0195 -0.0013 1067 GLU B N   
16803 C CA  . GLU B 1069 ? 0.3513 0.2929 0.3280 0.0703  -0.0181 -0.0016 1067 GLU B CA  
16804 C C   . GLU B 1069 ? 0.3347 0.2844 0.3168 0.0652  -0.0161 -0.0020 1067 GLU B C   
16805 O O   . GLU B 1069 ? 0.3197 0.2785 0.3057 0.0661  -0.0149 -0.0037 1067 GLU B O   
16806 C CB  . GLU B 1069 ? 0.3679 0.3102 0.3431 0.0716  -0.0187 0.0009  1067 GLU B CB  
16807 C CG  . GLU B 1069 ? 0.3837 0.3384 0.3633 0.0723  -0.0175 0.0010  1067 GLU B CG  
16808 C CD  . GLU B 1069 ? 0.4961 0.4571 0.4770 0.0779  -0.0177 -0.0011 1067 GLU B CD  
16809 O OE1 . GLU B 1069 ? 0.5034 0.4588 0.4813 0.0820  -0.0188 -0.0024 1067 GLU B OE1 
16810 O OE2 . GLU B 1069 ? 0.6094 0.5811 0.5944 0.0781  -0.0167 -0.0014 1067 GLU B OE2 
16811 N N   . ALA B 1070 ? 0.3105 0.2572 0.2929 0.0600  -0.0157 -0.0003 1068 ALA B N   
16812 C CA  . ALA B 1070 ? 0.2869 0.2404 0.2740 0.0554  -0.0138 -0.0007 1068 ALA B CA  
16813 C C   . ALA B 1070 ? 0.2586 0.2132 0.2475 0.0553  -0.0135 -0.0034 1068 ALA B C   
16814 O O   . ALA B 1070 ? 0.2915 0.2546 0.2847 0.0541  -0.0120 -0.0047 1068 ALA B O   
16815 C CB  . ALA B 1070 ? 0.3440 0.2935 0.3309 0.0502  -0.0135 0.0015  1068 ALA B CB  
16816 N N   . ALA B 1071 ? 0.2871 0.2332 0.2726 0.0565  -0.0149 -0.0044 1069 ALA B N   
16817 C CA  . ALA B 1071 ? 0.2802 0.2267 0.2668 0.0565  -0.0147 -0.0070 1069 ALA B CA  
16818 C C   . ALA B 1071 ? 0.2734 0.2277 0.2616 0.0608  -0.0140 -0.0091 1069 ALA B C   
16819 O O   . ALA B 1071 ? 0.2582 0.2192 0.2500 0.0596  -0.0128 -0.0106 1069 ALA B O   
16820 C CB  . ALA B 1071 ? 0.2945 0.2295 0.2763 0.0571  -0.0166 -0.0077 1069 ALA B CB  
16821 N N   . ARG B 1072 ? 0.2754 0.2292 0.2612 0.0660  -0.0148 -0.0091 1070 ARG B N   
16822 C CA  A ARG B 1072 ? 0.2788 0.2409 0.2665 0.0702  -0.0141 -0.0108 1070 ARG B CA  
16823 C CA  B ARG B 1072 ? 0.2790 0.2411 0.2668 0.0702  -0.0141 -0.0109 1070 ARG B CA  
16824 C C   . ARG B 1072 ? 0.2872 0.2609 0.2803 0.0680  -0.0124 -0.0104 1070 ARG B C   
16825 O O   . ARG B 1072 ? 0.2621 0.2433 0.2582 0.0683  -0.0112 -0.0120 1070 ARG B O   
16826 C CB  A ARG B 1072 ? 0.3035 0.2634 0.2880 0.0762  -0.0153 -0.0106 1070 ARG B CB  
16827 C CB  B ARG B 1072 ? 0.3039 0.2636 0.2883 0.0762  -0.0153 -0.0107 1070 ARG B CB  
16828 C CG  A ARG B 1072 ? 0.3367 0.2861 0.3158 0.0796  -0.0170 -0.0119 1070 ARG B CG  
16829 C CG  B ARG B 1072 ? 0.3323 0.2798 0.3109 0.0787  -0.0172 -0.0113 1070 ARG B CG  
16830 C CD  A ARG B 1072 ? 0.3427 0.2911 0.3190 0.0862  -0.0181 -0.0118 1070 ARG B CD  
16831 C CD  B ARG B 1072 ? 0.3435 0.2898 0.3191 0.0857  -0.0182 -0.0120 1070 ARG B CD  
16832 N NE  A ARG B 1072 ? 0.3617 0.3074 0.3364 0.0859  -0.0191 -0.0090 1070 ARG B NE  
16833 N NE  B ARG B 1072 ? 0.3549 0.2882 0.3242 0.0880  -0.0202 -0.0128 1070 ARG B NE  
16834 C CZ  A ARG B 1072 ? 0.3794 0.3134 0.3489 0.0862  -0.0209 -0.0076 1070 ARG B CZ  
16835 C CZ  B ARG B 1072 ? 0.3298 0.2592 0.2971 0.0892  -0.0204 -0.0153 1070 ARG B CZ  
16836 N NH1 A ARG B 1072 ? 0.3401 0.2636 0.3051 0.0869  -0.0222 -0.0089 1070 ARG B NH1 
16837 N NH1 B ARG B 1072 ? 0.3505 0.2881 0.3215 0.0888  -0.0187 -0.0173 1070 ARG B NH1 
16838 N NH2 A ARG B 1072 ? 0.3252 0.2576 0.2935 0.0856  -0.0216 -0.0049 1070 ARG B NH2 
16839 N NH2 B ARG B 1072 ? 0.3633 0.2799 0.3245 0.0908  -0.0224 -0.0158 1070 ARG B NH2 
16840 N N   . ASN B 1073 ? 0.2567 0.2317 0.2506 0.0656  -0.0122 -0.0081 1071 ASN B N   
16841 C CA  . ASN B 1073 ? 0.2737 0.2589 0.2720 0.0634  -0.0108 -0.0077 1071 ASN B CA  
16842 C C   . ASN B 1073 ? 0.2627 0.2507 0.2642 0.0590  -0.0095 -0.0087 1071 ASN B C   
16843 O O   . ASN B 1073 ? 0.2812 0.2778 0.2862 0.0584  -0.0083 -0.0096 1071 ASN B O   
16844 C CB  . ASN B 1073 ? 0.3158 0.3006 0.3135 0.0617  -0.0110 -0.0051 1071 ASN B CB  
16845 C CG  . ASN B 1073 ? 0.3572 0.3418 0.3526 0.0663  -0.0122 -0.0041 1071 ASN B CG  
16846 O OD1 . ASN B 1073 ? 0.3844 0.3725 0.3800 0.0707  -0.0125 -0.0054 1071 ASN B OD1 
16847 N ND2 . ASN B 1073 ? 0.4181 0.3986 0.4111 0.0654  -0.0129 -0.0018 1071 ASN B ND2 
16848 N N   . ALA B 1074 ? 0.2380 0.2192 0.2384 0.0557  -0.0097 -0.0084 1072 ALA B N   
16849 C CA  . ALA B 1074 ? 0.2459 0.2294 0.2492 0.0518  -0.0086 -0.0093 1072 ALA B CA  
16850 C C   . ALA B 1074 ? 0.2064 0.1924 0.2103 0.0538  -0.0084 -0.0118 1072 ALA B C   
16851 O O   . ALA B 1074 ? 0.2204 0.2130 0.2276 0.0520  -0.0072 -0.0128 1072 ALA B O   
16852 C CB  . ALA B 1074 ? 0.2619 0.2374 0.2638 0.0482  -0.0092 -0.0085 1072 ALA B CB  
16853 N N   . GLY B 1075 ? 0.2189 0.1994 0.2194 0.0575  -0.0096 -0.0129 1073 GLY B N   
16854 C CA  . GLY B 1075 ? 0.2474 0.2302 0.2479 0.0598  -0.0093 -0.0153 1073 GLY B CA  
16855 C C   . GLY B 1075 ? 0.2544 0.2481 0.2582 0.0615  -0.0080 -0.0159 1073 GLY B C   
16856 O O   . GLY B 1075 ? 0.2389 0.2376 0.2448 0.0606  -0.0070 -0.0173 1073 GLY B O   
16857 N N   . SER B 1076 ? 0.2610 0.2587 0.2654 0.0635  -0.0080 -0.0147 1074 SER B N   
16858 C CA  . SER B 1076 ? 0.2421 0.2504 0.2497 0.0650  -0.0070 -0.0151 1074 SER B CA  
16859 C C   . SER B 1076 ? 0.2606 0.2754 0.2721 0.0604  -0.0058 -0.0144 1074 SER B C   
16860 O O   . SER B 1076 ? 0.2613 0.2835 0.2756 0.0598  -0.0048 -0.0154 1074 SER B O   
16861 C CB  . SER B 1076 ? 0.2831 0.2934 0.2899 0.0689  -0.0078 -0.0140 1074 SER B CB  
16862 O OG  . SER B 1076 ? 0.2978 0.3036 0.3013 0.0740  -0.0087 -0.0149 1074 SER B OG  
16863 N N   . SER B 1077 ? 0.2288 0.2410 0.2405 0.0571  -0.0060 -0.0128 1075 SER B N   
16864 C CA  A SER B 1077 ? 0.2526 0.2705 0.2675 0.0530  -0.0049 -0.0121 1075 SER B CA  
16865 C CA  B SER B 1077 ? 0.2518 0.2701 0.2668 0.0532  -0.0049 -0.0122 1075 SER B CA  
16866 C C   . SER B 1077 ? 0.2390 0.2567 0.2555 0.0496  -0.0041 -0.0132 1075 SER B C   
16867 O O   . SER B 1077 ? 0.2683 0.2920 0.2876 0.0471  -0.0032 -0.0133 1075 SER B O   
16868 C CB  A SER B 1077 ? 0.2830 0.2977 0.2971 0.0509  -0.0052 -0.0101 1075 SER B CB  
16869 C CB  B SER B 1077 ? 0.2872 0.3038 0.3017 0.0513  -0.0051 -0.0101 1075 SER B CB  
16870 O OG  A SER B 1077 ? 0.3001 0.3154 0.3127 0.0539  -0.0060 -0.0089 1075 SER B OG  
16871 O OG  B SER B 1077 ? 0.2887 0.2973 0.3014 0.0490  -0.0054 -0.0094 1075 SER B OG  
16872 N N   . SER B 1078 ? 0.2134 0.2241 0.2280 0.0494  -0.0047 -0.0139 1076 SER B N   
16873 C CA  . SER B 1078 ? 0.2226 0.2328 0.2384 0.0464  -0.0042 -0.0149 1076 SER B CA  
16874 C C   . SER B 1078 ? 0.2038 0.2214 0.2218 0.0469  -0.0032 -0.0164 1076 SER B C   
16875 O O   . SER B 1078 ? 0.1967 0.2173 0.2141 0.0504  -0.0032 -0.0172 1076 SER B O   
16876 C CB  . SER B 1078 ? 0.2245 0.2265 0.2374 0.0472  -0.0052 -0.0159 1076 SER B CB  
16877 O OG  . SER B 1078 ? 0.2000 0.2024 0.2142 0.0448  -0.0048 -0.0171 1076 SER B OG  
16878 N N   . ALA B 1079 ? 0.1804 0.2011 0.2008 0.0434  -0.0025 -0.0165 1077 ALA B N   
16879 C CA  . ALA B 1079 ? 0.1938 0.2209 0.2159 0.0432  -0.0016 -0.0177 1077 ALA B CA  
16880 C C   . ALA B 1079 ? 0.1930 0.2169 0.2142 0.0425  -0.0017 -0.0192 1077 ALA B C   
16881 O O   . ALA B 1079 ? 0.1776 0.2060 0.2002 0.0416  -0.0010 -0.0200 1077 ALA B O   
16882 C CB  . ALA B 1079 ? 0.2121 0.2448 0.2370 0.0400  -0.0008 -0.0170 1077 ALA B CB  
16883 N N   . LEU B 1080 ? 0.1811 0.1971 0.1999 0.0428  -0.0027 -0.0194 1078 LEU B N   
16884 C CA  . LEU B 1080 ? 0.1599 0.1724 0.1773 0.0425  -0.0031 -0.0209 1078 LEU B CA  
16885 C C   . LEU B 1080 ? 0.1835 0.2000 0.2001 0.0456  -0.0025 -0.0224 1078 LEU B C   
16886 O O   . LEU B 1080 ? 0.1903 0.2077 0.2056 0.0494  -0.0025 -0.0227 1078 LEU B O   
16887 C CB  . LEU B 1080 ? 0.1779 0.1812 0.1921 0.0433  -0.0045 -0.0210 1078 LEU B CB  
16888 C CG  . LEU B 1080 ? 0.1929 0.1917 0.2049 0.0437  -0.0052 -0.0227 1078 LEU B CG  
16889 C CD1 . LEU B 1080 ? 0.2003 0.1992 0.2143 0.0395  -0.0052 -0.0228 1078 LEU B CD1 
16890 C CD2 . LEU B 1080 ? 0.2100 0.1997 0.2181 0.0453  -0.0068 -0.0229 1078 LEU B CD2 
16891 N N   . GLY B 1081 ? 0.1722 0.1913 0.1895 0.0440  -0.0020 -0.0234 1079 GLY B N   
16892 C CA  . GLY B 1081 ? 0.2016 0.2250 0.2181 0.0465  -0.0012 -0.0247 1079 GLY B CA  
16893 C C   . GLY B 1081 ? 0.1959 0.2286 0.2154 0.0458  0.0001  -0.0242 1079 GLY B C   
16894 O O   . GLY B 1081 ? 0.2118 0.2492 0.2310 0.0475  0.0010  -0.0251 1079 GLY B O   
16895 N N   . LEU B 1082 ? 0.1901 0.2257 0.2121 0.0435  0.0003  -0.0227 1080 LEU B N   
16896 C CA  A LEU B 1082 ? 0.1997 0.2435 0.2244 0.0420  0.0013  -0.0222 1080 LEU B CA  
16897 C CA  B LEU B 1082 ? 0.1996 0.2435 0.2244 0.0420  0.0013  -0.0222 1080 LEU B CA  
16898 C C   . LEU B 1082 ? 0.1907 0.2361 0.2156 0.0399  0.0019  -0.0230 1080 LEU B C   
16899 O O   . LEU B 1082 ? 0.1955 0.2360 0.2197 0.0378  0.0013  -0.0234 1080 LEU B O   
16900 C CB  A LEU B 1082 ? 0.1845 0.2291 0.2113 0.0391  0.0012  -0.0208 1080 LEU B CB  
16901 C CB  B LEU B 1082 ? 0.1844 0.2291 0.2112 0.0391  0.0012  -0.0208 1080 LEU B CB  
16902 C CG  A LEU B 1082 ? 0.1878 0.2398 0.2171 0.0369  0.0019  -0.0201 1080 LEU B CG  
16903 C CG  B LEU B 1082 ? 0.1878 0.2397 0.2171 0.0368  0.0019  -0.0201 1080 LEU B CG  
16904 C CD1 A LEU B 1082 ? 0.2507 0.3096 0.2808 0.0395  0.0024  -0.0202 1080 LEU B CD1 
16905 C CD1 B LEU B 1082 ? 0.1861 0.2385 0.2165 0.0358  0.0016  -0.0188 1080 LEU B CD1 
16906 C CD2 A LEU B 1082 ? 0.1826 0.2341 0.2131 0.0346  0.0016  -0.0189 1080 LEU B CD2 
16907 C CD2 B LEU B 1082 ? 0.1944 0.2460 0.2243 0.0333  0.0021  -0.0204 1080 LEU B CD2 
16908 N N   . ASP B 1083 ? 0.2014 0.2538 0.2271 0.0404  0.0028  -0.0233 1081 ASP B N   
16909 C CA  . ASP B 1083 ? 0.2378 0.2918 0.2632 0.0388  0.0034  -0.0240 1081 ASP B CA  
16910 C C   . ASP B 1083 ? 0.2136 0.2763 0.2412 0.0375  0.0044  -0.0233 1081 ASP B C   
16911 O O   . ASP B 1083 ? 0.2637 0.3320 0.2915 0.0400  0.0053  -0.0235 1081 ASP B O   
16912 C CB  . ASP B 1083 ? 0.2475 0.2991 0.2698 0.0420  0.0035  -0.0255 1081 ASP B CB  
16913 C CG  . ASP B 1083 ? 0.3828 0.4355 0.4042 0.0404  0.0041  -0.0263 1081 ASP B CG  
16914 O OD1 . ASP B 1083 ? 0.4470 0.5008 0.4697 0.0368  0.0041  -0.0256 1081 ASP B OD1 
16915 O OD2 . ASP B 1083 ? 0.4567 0.5088 0.4755 0.0431  0.0044  -0.0276 1081 ASP B OD2 
16916 N N   . LEU B 1084 ? 0.2195 0.2835 0.2489 0.0337  0.0043  -0.0224 1082 LEU B N   
16917 C CA  . LEU B 1084 ? 0.2310 0.3024 0.2625 0.0319  0.0049  -0.0214 1082 LEU B CA  
16918 C C   . LEU B 1084 ? 0.2085 0.2809 0.2399 0.0286  0.0053  -0.0214 1082 LEU B C   
16919 O O   . LEU B 1084 ? 0.2127 0.2796 0.2429 0.0269  0.0048  -0.0217 1082 LEU B O   
16920 C CB  . LEU B 1084 ? 0.2693 0.3405 0.3024 0.0300  0.0043  -0.0203 1082 LEU B CB  
16921 C CG  . LEU B 1084 ? 0.3236 0.3948 0.3571 0.0327  0.0039  -0.0199 1082 LEU B CG  
16922 C CD1 . LEU B 1084 ? 0.3125 0.3830 0.3471 0.0304  0.0033  -0.0189 1082 LEU B CD1 
16923 C CD2 . LEU B 1084 ? 0.3396 0.4182 0.3741 0.0353  0.0045  -0.0198 1082 LEU B CD2 
16924 N N   . GLU B 1085 ? 0.2125 0.2921 0.2450 0.0276  0.0061  -0.0209 1083 GLU B N   
16925 C CA  . GLU B 1085 ? 0.1975 0.2785 0.2300 0.0238  0.0062  -0.0204 1083 GLU B CA  
16926 C C   . GLU B 1085 ? 0.2095 0.2928 0.2439 0.0209  0.0057  -0.0192 1083 GLU B C   
16927 O O   . GLU B 1085 ? 0.2248 0.3136 0.2609 0.0215  0.0059  -0.0186 1083 GLU B O   
16928 C CB  . GLU B 1085 ? 0.2035 0.2905 0.2357 0.0239  0.0074  -0.0204 1083 GLU B CB  
16929 C CG  . GLU B 1085 ? 0.2464 0.3341 0.2783 0.0197  0.0074  -0.0197 1083 GLU B CG  
16930 C CD  . GLU B 1085 ? 0.3032 0.3957 0.3341 0.0193  0.0086  -0.0196 1083 GLU B CD  
16931 O OE1 . GLU B 1085 ? 0.3214 0.4168 0.3517 0.0226  0.0096  -0.0203 1083 GLU B OE1 
16932 O OE2 . GLU B 1085 ? 0.3047 0.3981 0.3353 0.0157  0.0086  -0.0187 1083 GLU B OE2 
16933 N N   . LEU B 1086 ? 0.1846 0.2635 0.2185 0.0180  0.0051  -0.0190 1084 LEU B N   
16934 C CA  . LEU B 1086 ? 0.1862 0.2658 0.2212 0.0153  0.0045  -0.0181 1084 LEU B CA  
16935 C C   . LEU B 1086 ? 0.2253 0.3091 0.2604 0.0120  0.0046  -0.0174 1084 LEU B C   
16936 O O   . LEU B 1086 ? 0.2371 0.3204 0.2709 0.0110  0.0050  -0.0176 1084 LEU B O   
16937 C CB  . LEU B 1086 ? 0.2220 0.2945 0.2562 0.0140  0.0037  -0.0183 1084 LEU B CB  
16938 C CG  . LEU B 1086 ? 0.2286 0.2966 0.2627 0.0167  0.0034  -0.0188 1084 LEU B CG  
16939 C CD1 . LEU B 1086 ? 0.2263 0.2885 0.2601 0.0152  0.0028  -0.0188 1084 LEU B CD1 
16940 C CD2 . LEU B 1086 ? 0.2666 0.3376 0.3019 0.0185  0.0034  -0.0184 1084 LEU B CD2 
16941 N N   . PRO B 1087 ? 0.1899 0.2780 0.2263 0.0102  0.0043  -0.0166 1085 PRO B N   
16942 C CA  . PRO B 1087 ? 0.2298 0.3214 0.2662 0.0065  0.0042  -0.0157 1085 PRO B CA  
16943 C C   . PRO B 1087 ? 0.2077 0.2930 0.2420 0.0038  0.0036  -0.0158 1085 PRO B C   
16944 O O   . PRO B 1087 ? 0.2263 0.3058 0.2600 0.0038  0.0029  -0.0162 1085 PRO B O   
16945 C CB  . PRO B 1087 ? 0.2349 0.3302 0.2727 0.0052  0.0035  -0.0150 1085 PRO B CB  
16946 C CG  . PRO B 1087 ? 0.2814 0.3783 0.3205 0.0090  0.0037  -0.0153 1085 PRO B CG  
16947 C CD  . PRO B 1087 ? 0.2332 0.3235 0.2711 0.0116  0.0039  -0.0163 1085 PRO B CD  
16948 N N   . GLY B 1088 ? 0.2077 0.2943 0.2409 0.0015  0.0038  -0.0153 1086 GLY B N   
16949 C CA  . GLY B 1088 ? 0.2318 0.3126 0.2630 -0.0010 0.0032  -0.0153 1086 GLY B CA  
16950 C C   . GLY B 1088 ? 0.1956 0.2793 0.2256 -0.0039 0.0034  -0.0143 1086 GLY B C   
16951 O O   . GLY B 1088 ? 0.2098 0.3005 0.2410 -0.0047 0.0041  -0.0136 1086 GLY B O   
16952 N N   . PRO B 1089 ? 0.1873 0.2657 0.2150 -0.0055 0.0029  -0.0143 1087 PRO B N   
16953 C CA  . PRO B 1089 ? 0.1921 0.2723 0.2181 -0.0086 0.0031  -0.0133 1087 PRO B CA  
16954 C C   . PRO B 1089 ? 0.2017 0.2867 0.2276 -0.0070 0.0046  -0.0132 1087 PRO B C   
16955 O O   . PRO B 1089 ? 0.2007 0.2854 0.2270 -0.0034 0.0052  -0.0143 1087 PRO B O   
16956 C CB  . PRO B 1089 ? 0.2470 0.3193 0.2704 -0.0098 0.0020  -0.0134 1087 PRO B CB  
16957 C CG  . PRO B 1089 ? 0.2585 0.3264 0.2824 -0.0063 0.0019  -0.0148 1087 PRO B CG  
16958 C CD  . PRO B 1089 ? 0.2106 0.2812 0.2370 -0.0045 0.0022  -0.0152 1087 PRO B CD  
16959 N N   . VAL B 1090 ? 0.1868 0.2765 0.2121 -0.0098 0.0051  -0.0120 1088 VAL B N   
16960 C CA  . VAL B 1090 ? 0.1785 0.2723 0.2030 -0.0087 0.0066  -0.0119 1088 VAL B CA  
16961 C C   . VAL B 1090 ? 0.1872 0.2742 0.2087 -0.0078 0.0063  -0.0126 1088 VAL B C   
16962 O O   . VAL B 1090 ? 0.1967 0.2765 0.2167 -0.0090 0.0049  -0.0127 1088 VAL B O   
16963 C CB  . VAL B 1090 ? 0.2026 0.3028 0.2269 -0.0124 0.0073  -0.0101 1088 VAL B CB  
16964 C CG1 . VAL B 1090 ? 0.2147 0.3224 0.2424 -0.0133 0.0074  -0.0094 1088 VAL B CG1 
16965 C CG2 . VAL B 1090 ? 0.2349 0.3296 0.2563 -0.0167 0.0060  -0.0091 1088 VAL B CG2 
16966 N N   . GLY B 1091 ? 0.2053 0.2946 0.2257 -0.0055 0.0076  -0.0131 1089 GLY B N   
16967 C CA  . GLY B 1091 ? 0.1951 0.2784 0.2124 -0.0047 0.0073  -0.0137 1089 GLY B CA  
16968 C C   . GLY B 1091 ? 0.1949 0.2718 0.2125 -0.0018 0.0063  -0.0153 1089 GLY B C   
16969 O O   . GLY B 1091 ? 0.1847 0.2557 0.2000 -0.0016 0.0054  -0.0158 1089 GLY B O   
16970 N N   . GLU B 1092 ? 0.1986 0.2766 0.2189 0.0003  0.0063  -0.0160 1090 GLU B N   
16971 C CA  . GLU B 1092 ? 0.1928 0.2652 0.2136 0.0029  0.0054  -0.0173 1090 GLU B CA  
16972 C C   . GLU B 1092 ? 0.2012 0.2773 0.2241 0.0061  0.0062  -0.0180 1090 GLU B C   
16973 O O   . GLU B 1092 ? 0.2067 0.2889 0.2316 0.0057  0.0069  -0.0173 1090 GLU B O   
16974 C CB  . GLU B 1092 ? 0.2144 0.2823 0.2361 0.0011  0.0040  -0.0170 1090 GLU B CB  
16975 C CG  . GLU B 1092 ? 0.3234 0.3839 0.3440 0.0016  0.0028  -0.0177 1090 GLU B CG  
16976 C CD  . GLU B 1092 ? 0.3041 0.3607 0.3254 -0.0001 0.0016  -0.0174 1090 GLU B CD  
16977 O OE1 . GLU B 1092 ? 0.2385 0.2963 0.2619 0.0003  0.0017  -0.0174 1090 GLU B OE1 
16978 O OE2 . GLU B 1092 ? 0.2988 0.3512 0.3183 -0.0018 0.0007  -0.0171 1090 GLU B OE2 
16979 N N   . ARG B 1093 ? 0.1865 0.2591 0.2090 0.0092  0.0060  -0.0193 1091 ARG B N   
16980 C CA  . ARG B 1093 ? 0.1956 0.2698 0.2197 0.0125  0.0064  -0.0200 1091 ARG B CA  
16981 C C   . ARG B 1093 ? 0.1785 0.2464 0.2034 0.0129  0.0052  -0.0205 1091 ARG B C   
16982 O O   . ARG B 1093 ? 0.1854 0.2476 0.2088 0.0132  0.0044  -0.0211 1091 ARG B O   
16983 C CB  . ARG B 1093 ? 0.2120 0.2871 0.2344 0.0159  0.0073  -0.0211 1091 ARG B CB  
16984 N N   . ASN B 1094 ? 0.1561 0.2252 0.1832 0.0129  0.0050  -0.0200 1092 ASN B N   
16985 C CA  . ASN B 1094 ? 0.1531 0.2171 0.1811 0.0131  0.0040  -0.0203 1092 ASN B CA  
16986 C C   . ASN B 1094 ? 0.1923 0.2567 0.2213 0.0163  0.0042  -0.0207 1092 ASN B C   
16987 O O   . ASN B 1094 ? 0.1860 0.2552 0.2164 0.0170  0.0047  -0.0203 1092 ASN B O   
16988 C CB  . ASN B 1094 ? 0.1661 0.2302 0.1952 0.0103  0.0035  -0.0193 1092 ASN B CB  
16989 C CG  . ASN B 1094 ? 0.1662 0.2277 0.1938 0.0075  0.0029  -0.0190 1092 ASN B CG  
16990 O OD1 . ASN B 1094 ? 0.1768 0.2330 0.2037 0.0075  0.0022  -0.0195 1092 ASN B OD1 
16991 N ND2 . ASN B 1094 ? 0.1840 0.2491 0.2111 0.0051  0.0032  -0.0182 1092 ASN B ND2 
16992 N N   . LEU B 1095 ? 0.1710 0.2304 0.1989 0.0182  0.0038  -0.0216 1093 LEU B N   
16993 C CA  . LEU B 1095 ? 0.1694 0.2281 0.1973 0.0214  0.0038  -0.0222 1093 LEU B CA  
16994 C C   . LEU B 1095 ? 0.1505 0.2043 0.1794 0.0213  0.0030  -0.0220 1093 LEU B C   
16995 O O   . LEU B 1095 ? 0.1709 0.2208 0.1999 0.0195  0.0023  -0.0219 1093 LEU B O   
16996 C CB  . LEU B 1095 ? 0.1879 0.2440 0.2134 0.0237  0.0039  -0.0234 1093 LEU B CB  
16997 C CG  . LEU B 1095 ? 0.2357 0.2963 0.2599 0.0237  0.0048  -0.0236 1093 LEU B CG  
16998 C CD1 . LEU B 1095 ? 0.2939 0.3513 0.3151 0.0261  0.0048  -0.0250 1093 LEU B CD1 
16999 C CD2 . LEU B 1095 ? 0.2375 0.3058 0.2631 0.0246  0.0060  -0.0230 1093 LEU B CD2 
17000 N N   . TYR B 1096 ? 0.1550 0.2093 0.1844 0.0235  0.0031  -0.0219 1094 TYR B N   
17001 C CA  . TYR B 1096 ? 0.1511 0.2014 0.1813 0.0235  0.0024  -0.0215 1094 TYR B CA  
17002 C C   . TYR B 1096 ? 0.1651 0.2132 0.1943 0.0268  0.0022  -0.0220 1094 TYR B C   
17003 O O   . TYR B 1096 ? 0.1630 0.2149 0.1920 0.0291  0.0027  -0.0220 1094 TYR B O   
17004 C CB  . TYR B 1096 ? 0.1627 0.2164 0.1947 0.0222  0.0026  -0.0204 1094 TYR B CB  
17005 C CG  . TYR B 1096 ? 0.1563 0.2067 0.1888 0.0225  0.0022  -0.0199 1094 TYR B CG  
17006 C CD1 . TYR B 1096 ? 0.1770 0.2236 0.2100 0.0205  0.0018  -0.0196 1094 TYR B CD1 
17007 C CD2 . TYR B 1096 ? 0.2025 0.2540 0.2351 0.0247  0.0022  -0.0195 1094 TYR B CD2 
17008 C CE1 . TYR B 1096 ? 0.1744 0.2186 0.2079 0.0206  0.0017  -0.0189 1094 TYR B CE1 
17009 C CE2 . TYR B 1096 ? 0.1746 0.2232 0.2074 0.0248  0.0019  -0.0188 1094 TYR B CE2 
17010 C CZ  . TYR B 1096 ? 0.1685 0.2137 0.2018 0.0227  0.0017  -0.0185 1094 TYR B CZ  
17011 O OH  . TYR B 1096 ? 0.1781 0.2206 0.2114 0.0227  0.0016  -0.0177 1094 TYR B OH  
17012 N N   . THR B 1097 ? 0.1735 0.2154 0.2017 0.0270  0.0014  -0.0223 1095 THR B N   
17013 C CA  . THR B 1097 ? 0.1683 0.2066 0.1947 0.0300  0.0010  -0.0229 1095 THR B CA  
17014 C C   . THR B 1097 ? 0.1597 0.1926 0.1864 0.0294  0.0002  -0.0223 1095 THR B C   
17015 O O   . THR B 1097 ? 0.1791 0.2101 0.2070 0.0268  -0.0001 -0.0218 1095 THR B O   
17016 C CB  . THR B 1097 ? 0.2024 0.2377 0.2264 0.0310  0.0007  -0.0243 1095 THR B CB  
17017 O OG1 . THR B 1097 ? 0.2576 0.2892 0.2818 0.0283  -0.0001 -0.0244 1095 THR B OG1 
17018 C CG2 . THR B 1097 ? 0.2174 0.2582 0.2409 0.0315  0.0017  -0.0248 1095 THR B CG2 
17019 N N   . LEU B 1098 ? 0.1777 0.2084 0.2032 0.0319  -0.0001 -0.0222 1096 LEU B N   
17020 C CA  . LEU B 1098 ? 0.1700 0.1954 0.1954 0.0314  -0.0009 -0.0214 1096 LEU B CA  
17021 C C   . LEU B 1098 ? 0.1696 0.1884 0.1923 0.0330  -0.0019 -0.0223 1096 LEU B C   
17022 O O   . LEU B 1098 ? 0.1875 0.2057 0.2080 0.0362  -0.0020 -0.0231 1096 LEU B O   
17023 C CB  . LEU B 1098 ? 0.1689 0.1958 0.1947 0.0327  -0.0006 -0.0203 1096 LEU B CB  
17024 C CG  . LEU B 1098 ? 0.1618 0.1944 0.1899 0.0309  0.0002  -0.0194 1096 LEU B CG  
17025 C CD1 . LEU B 1098 ? 0.1761 0.2097 0.2042 0.0324  0.0001  -0.0183 1096 LEU B CD1 
17026 C CD2 . LEU B 1098 ? 0.1807 0.2122 0.2104 0.0275  0.0002  -0.0189 1096 LEU B CD2 
17027 N N   . HIS B 1099 ? 0.1781 0.1922 0.2009 0.0307  -0.0028 -0.0222 1097 HIS B N   
17028 C CA  . HIS B 1099 ? 0.1936 0.2010 0.2139 0.0313  -0.0041 -0.0230 1097 HIS B CA  
17029 C C   . HIS B 1099 ? 0.1870 0.1896 0.2076 0.0301  -0.0048 -0.0217 1097 HIS B C   
17030 O O   . HIS B 1099 ? 0.1882 0.1931 0.2110 0.0286  -0.0042 -0.0203 1097 HIS B O   
17031 C CB  . HIS B 1099 ? 0.1993 0.2056 0.2199 0.0291  -0.0046 -0.0238 1097 HIS B CB  
17032 C CG  . HIS B 1099 ? 0.2182 0.2289 0.2383 0.0298  -0.0039 -0.0249 1097 HIS B CG  
17033 N ND1 . HIS B 1099 ? 0.2658 0.2745 0.2828 0.0317  -0.0043 -0.0265 1097 HIS B ND1 
17034 C CD2 . HIS B 1099 ? 0.2462 0.2630 0.2683 0.0287  -0.0028 -0.0245 1097 HIS B CD2 
17035 C CE1 . HIS B 1099 ? 0.2821 0.2959 0.2994 0.0318  -0.0033 -0.0269 1097 HIS B CE1 
17036 N NE2 . HIS B 1099 ? 0.2586 0.2773 0.2790 0.0299  -0.0025 -0.0257 1097 HIS B NE2 
17037 N N   . ALA B 1100 ? 0.2061 0.2019 0.2240 0.0307  -0.0062 -0.0222 1098 ALA B N   
17038 C CA  . ALA B 1100 ? 0.2090 0.1999 0.2273 0.0288  -0.0070 -0.0209 1098 ALA B CA  
17039 C C   . ALA B 1100 ? 0.2019 0.1946 0.2235 0.0249  -0.0069 -0.0201 1098 ALA B C   
17040 O O   . ALA B 1100 ? 0.2144 0.2091 0.2370 0.0238  -0.0069 -0.0210 1098 ALA B O   
17041 C CB  . ALA B 1100 ? 0.2237 0.2065 0.2383 0.0295  -0.0088 -0.0217 1098 ALA B CB  
17042 N N   . ARG B 1101 ? 0.2033 0.1952 0.2265 0.0230  -0.0067 -0.0184 1099 ARG B N   
17043 C CA  . ARG B 1101 ? 0.1991 0.1923 0.2255 0.0196  -0.0067 -0.0176 1099 ARG B CA  
17044 C C   . ARG B 1101 ? 0.1926 0.1808 0.2184 0.0178  -0.0084 -0.0181 1099 ARG B C   
17045 O O   . ARG B 1101 ? 0.2229 0.2130 0.2510 0.0158  -0.0086 -0.0184 1099 ARG B O   
17046 C CB  . ARG B 1101 ? 0.2197 0.2134 0.2477 0.0182  -0.0059 -0.0155 1099 ARG B CB  
17047 C CG  . ARG B 1101 ? 0.2587 0.2584 0.2884 0.0186  -0.0042 -0.0149 1099 ARG B CG  
17048 C CD  . ARG B 1101 ? 0.2463 0.2502 0.2794 0.0163  -0.0035 -0.0148 1099 ARG B CD  
17049 N NE  . ARG B 1101 ? 0.2507 0.2597 0.2849 0.0166  -0.0020 -0.0144 1099 ARG B NE  
17050 C CZ  . ARG B 1101 ? 0.2264 0.2384 0.2630 0.0149  -0.0011 -0.0136 1099 ARG B CZ  
17051 N NH1 . ARG B 1101 ? 0.2131 0.2244 0.2518 0.0127  -0.0014 -0.0132 1099 ARG B NH1 
17052 N NH2 . ARG B 1101 ? 0.2453 0.2612 0.2822 0.0153  0.0000  -0.0133 1099 ARG B NH2 
17053 N N   . GLY B 1102 ? 0.1895 0.1713 0.2122 0.0187  -0.0097 -0.0183 1100 GLY B N   
17054 C CA  . GLY B 1102 ? 0.2244 0.2009 0.2463 0.0167  -0.0116 -0.0187 1100 GLY B CA  
17055 C C   . GLY B 1102 ? 0.2332 0.2035 0.2535 0.0158  -0.0127 -0.0174 1100 GLY B C   
17056 O O   . GLY B 1102 ? 0.2422 0.2087 0.2591 0.0183  -0.0129 -0.0175 1100 GLY B O   
17057 N N   . ARG B 1103 ? 0.2126 0.1819 0.2353 0.0122  -0.0133 -0.0161 1101 ARG B N   
17058 C CA  . ARG B 1103 ? 0.2308 0.1945 0.2523 0.0106  -0.0142 -0.0144 1101 ARG B CA  
17059 C C   . ARG B 1103 ? 0.2351 0.2032 0.2597 0.0090  -0.0125 -0.0121 1101 ARG B C   
17060 O O   . ARG B 1103 ? 0.2314 0.2052 0.2603 0.0069  -0.0114 -0.0115 1101 ARG B O   
17061 C CB  . ARG B 1103 ? 0.2438 0.2031 0.2655 0.0073  -0.0164 -0.0144 1101 ARG B CB  
17062 C CG  . ARG B 1103 ? 0.2759 0.2283 0.2956 0.0055  -0.0176 -0.0127 1101 ARG B CG  
17063 C CD  . ARG B 1103 ? 0.3411 0.2877 0.3599 0.0025  -0.0203 -0.0130 1101 ARG B CD  
17064 N NE  . ARG B 1103 ? 0.4094 0.3488 0.4228 0.0049  -0.0222 -0.0152 1101 ARG B NE  
17065 C CZ  . ARG B 1103 ? 0.4593 0.3983 0.4718 0.0053  -0.0234 -0.0174 1101 ARG B CZ  
17066 N NH1 . ARG B 1103 ? 0.5683 0.5136 0.5851 0.0035  -0.0230 -0.0176 1101 ARG B NH1 
17067 N NH2 . ARG B 1103 ? 0.4295 0.3615 0.4364 0.0078  -0.0251 -0.0194 1101 ARG B NH2 
17068 N N   . ILE B 1104 ? 0.2011 0.1664 0.2235 0.0102  -0.0121 -0.0108 1102 ILE B N   
17069 C CA  . ILE B 1104 ? 0.2088 0.1777 0.2333 0.0091  -0.0104 -0.0086 1102 ILE B CA  
17070 C C   . ILE B 1104 ? 0.2012 0.1655 0.2255 0.0058  -0.0113 -0.0065 1102 ILE B C   
17071 O O   . ILE B 1104 ? 0.2157 0.1722 0.2362 0.0060  -0.0130 -0.0064 1102 ILE B O   
17072 C CB  . ILE B 1104 ? 0.1969 0.1663 0.2189 0.0126  -0.0094 -0.0085 1102 ILE B CB  
17073 C CG1 . ILE B 1104 ? 0.2060 0.1798 0.2279 0.0157  -0.0088 -0.0106 1102 ILE B CG1 
17074 C CG2 . ILE B 1104 ? 0.2137 0.1869 0.2374 0.0115  -0.0077 -0.0063 1102 ILE B CG2 
17075 C CD1 . ILE B 1104 ? 0.2104 0.1917 0.2363 0.0145  -0.0074 -0.0110 1102 ILE B CD1 
17076 N N   . LEU B 1105 ? 0.1936 0.1624 0.2219 0.0029  -0.0100 -0.0048 1103 LEU B N   
17077 C CA  . LEU B 1105 ? 0.2248 0.1905 0.2534 -0.0005 -0.0104 -0.0023 1103 LEU B CA  
17078 C C   . LEU B 1105 ? 0.1999 0.1637 0.2257 0.0008  -0.0095 -0.0006 1103 LEU B C   
17079 O O   . LEU B 1105 ? 0.2141 0.1832 0.2409 0.0023  -0.0075 -0.0002 1103 LEU B O   
17080 C CB  . LEU B 1105 ? 0.2053 0.1778 0.2394 -0.0037 -0.0091 -0.0011 1103 LEU B CB  
17081 C CG  . LEU B 1105 ? 0.2402 0.2115 0.2754 -0.0075 -0.0088 0.0018  1103 LEU B CG  
17082 C CD1 . LEU B 1105 ? 0.2293 0.1932 0.2627 -0.0100 -0.0115 0.0020  1103 LEU B CD1 
17083 C CD2 . LEU B 1105 ? 0.2404 0.2198 0.2812 -0.0098 -0.0071 0.0027  1103 LEU B CD2 
17084 N N   . LEU B 1106 ? 0.2153 0.1710 0.2372 0.0004  -0.0110 0.0004  1104 LEU B N   
17085 C CA  . LEU B 1106 ? 0.2337 0.1865 0.2524 0.0016  -0.0105 0.0023  1104 LEU B CA  
17086 C C   . LEU B 1106 ? 0.2418 0.1933 0.2616 -0.0027 -0.0103 0.0053  1104 LEU B C   
17087 O O   . LEU B 1106 ? 0.2487 0.1953 0.2682 -0.0058 -0.0120 0.0059  1104 LEU B O   
17088 C CB  . LEU B 1106 ? 0.2450 0.1890 0.2579 0.0045  -0.0125 0.0014  1104 LEU B CB  
17089 C CG  . LEU B 1106 ? 0.2989 0.2447 0.3099 0.0097  -0.0121 -0.0005 1104 LEU B CG  
17090 C CD1 . LEU B 1106 ? 0.3148 0.2685 0.3294 0.0107  -0.0110 -0.0027 1104 LEU B CD1 
17091 C CD2 . LEU B 1106 ? 0.2467 0.1838 0.2523 0.0126  -0.0143 -0.0018 1104 LEU B CD2 
17092 N N   . VAL B 1107 ? 0.2119 0.1679 0.2327 -0.0031 -0.0081 0.0073  1105 VAL B N   
17093 C CA  . VAL B 1107 ? 0.2508 0.2060 0.2724 -0.0071 -0.0075 0.0104  1105 VAL B CA  
17094 C C   . VAL B 1107 ? 0.2282 0.1795 0.2452 -0.0054 -0.0072 0.0122  1105 VAL B C   
17095 O O   . VAL B 1107 ? 0.2428 0.1993 0.2606 -0.0047 -0.0051 0.0133  1105 VAL B O   
17096 C CB  . VAL B 1107 ? 0.2161 0.1809 0.2433 -0.0092 -0.0051 0.0112  1105 VAL B CB  
17097 C CG1 . VAL B 1107 ? 0.2285 0.1930 0.2570 -0.0138 -0.0045 0.0143  1105 VAL B CG1 
17098 C CG2 . VAL B 1107 ? 0.2387 0.2079 0.2700 -0.0096 -0.0054 0.0088  1105 VAL B CG2 
17099 N N   . PRO B 1108 ? 0.2339 0.1759 0.2460 -0.0046 -0.0094 0.0125  1106 PRO B N   
17100 C CA  . PRO B 1108 ? 0.2681 0.2058 0.2756 -0.0028 -0.0093 0.0144  1106 PRO B CA  
17101 C C   . PRO B 1108 ? 0.2755 0.2111 0.2825 -0.0070 -0.0088 0.0180  1106 PRO B C   
17102 O O   . PRO B 1108 ? 0.3007 0.2365 0.3104 -0.0115 -0.0090 0.0191  1106 PRO B O   
17103 C CB  . PRO B 1108 ? 0.2804 0.2082 0.2827 -0.0003 -0.0122 0.0131  1106 PRO B CB  
17104 C CG  . PRO B 1108 ? 0.2773 0.2019 0.2810 -0.0035 -0.0138 0.0123  1106 PRO B CG  
17105 C CD  . PRO B 1108 ? 0.2732 0.2078 0.2832 -0.0048 -0.0121 0.0110  1106 PRO B CD  
17106 N N   . ALA B 1109 ? 0.2677 0.2015 0.2711 -0.0056 -0.0081 0.0199  1107 ALA B N   
17107 C CA  . ALA B 1109 ? 0.2851 0.2150 0.2864 -0.0091 -0.0079 0.0236  1107 ALA B CA  
17108 C C   . ALA B 1109 ? 0.3283 0.2469 0.3229 -0.0077 -0.0104 0.0247  1107 ALA B C   
17109 O O   . ALA B 1109 ? 0.3463 0.2581 0.3387 -0.0113 -0.0115 0.0271  1107 ALA B O   
17110 C CB  . ALA B 1109 ? 0.2963 0.2332 0.2985 -0.0090 -0.0051 0.0255  1107 ALA B CB  
17111 N N   . THR B 1110 ? 0.3061 0.2223 0.2973 -0.0024 -0.0112 0.0230  1108 THR B N   
17112 C CA  . THR B 1110 ? 0.3007 0.2066 0.2853 -0.0001 -0.0134 0.0239  1108 THR B CA  
17113 C C   . THR B 1110 ? 0.2951 0.1964 0.2776 0.0041  -0.0156 0.0206  1108 THR B C   
17114 O O   . THR B 1110 ? 0.2973 0.2047 0.2833 0.0060  -0.0150 0.0176  1108 THR B O   
17115 C CB  . THR B 1110 ? 0.3346 0.2420 0.3163 0.0030  -0.0124 0.0253  1108 THR B CB  
17116 O OG1 . THR B 1110 ? 0.3179 0.2326 0.3017 0.0075  -0.0115 0.0226  1108 THR B OG1 
17117 C CG2 . THR B 1110 ? 0.3637 0.2761 0.3470 -0.0008 -0.0100 0.0285  1108 THR B CG2 
17118 N N   . GLU B 1111 ? 0.3151 0.2052 0.2915 0.0056  -0.0181 0.0211  1109 GLU B N   
17119 C CA  . GLU B 1111 ? 0.3292 0.2141 0.3028 0.0100  -0.0202 0.0180  1109 GLU B CA  
17120 C C   . GLU B 1111 ? 0.3314 0.2233 0.3060 0.0157  -0.0191 0.0158  1109 GLU B C   
17121 O O   . GLU B 1111 ? 0.3254 0.2206 0.3021 0.0181  -0.0192 0.0127  1109 GLU B O   
17122 C CB  . GLU B 1111 ? 0.3353 0.2068 0.3016 0.0112  -0.0230 0.0193  1109 GLU B CB  
17123 C CG  . GLU B 1111 ? 0.3806 0.2466 0.3432 0.0168  -0.0250 0.0161  1109 GLU B CG  
17124 C CD  . GLU B 1111 ? 0.4380 0.2899 0.3931 0.0178  -0.0279 0.0172  1109 GLU B CD  
17125 O OE1 . GLU B 1111 ? 0.4211 0.2649 0.3742 0.0142  -0.0298 0.0174  1109 GLU B OE1 
17126 O OE2 . GLU B 1111 ? 0.4703 0.3190 0.4212 0.0222  -0.0285 0.0179  1109 GLU B OE2 
17127 N N   . SER B 1112 ? 0.3291 0.2235 0.3024 0.0177  -0.0181 0.0175  1110 SER B N   
17128 C CA  . SER B 1112 ? 0.3225 0.2240 0.2971 0.0228  -0.0172 0.0156  1110 SER B CA  
17129 C C   . SER B 1112 ? 0.3125 0.2254 0.2935 0.0215  -0.0149 0.0138  1110 SER B C   
17130 O O   . SER B 1112 ? 0.3092 0.2268 0.2919 0.0249  -0.0147 0.0111  1110 SER B O   
17131 C CB  . SER B 1112 ? 0.3637 0.2662 0.3358 0.0245  -0.0166 0.0180  1110 SER B CB  
17132 O OG  . SER B 1112 ? 0.3750 0.2848 0.3485 0.0291  -0.0159 0.0162  1110 SER B OG  
17133 N N   . GLY B 1113 ? 0.2951 0.2126 0.2797 0.0168  -0.0132 0.0155  1111 GLY B N   
17134 C CA  . GLY B 1113 ? 0.2628 0.1904 0.2533 0.0155  -0.0112 0.0138  1111 GLY B CA  
17135 C C   . GLY B 1113 ? 0.2773 0.2044 0.2697 0.0157  -0.0122 0.0109  1111 GLY B C   
17136 O O   . GLY B 1113 ? 0.2685 0.2022 0.2638 0.0178  -0.0114 0.0085  1111 GLY B O   
17137 N N   . LEU B 1114 ? 0.2863 0.2052 0.2766 0.0135  -0.0141 0.0112  1112 LEU B N   
17138 C CA  . LEU B 1114 ? 0.2685 0.1860 0.2599 0.0138  -0.0153 0.0084  1112 LEU B CA  
17139 C C   . LEU B 1114 ? 0.2666 0.1832 0.2555 0.0195  -0.0162 0.0057  1112 LEU B C   
17140 O O   . LEU B 1114 ? 0.2522 0.1735 0.2436 0.0208  -0.0158 0.0031  1112 LEU B O   
17141 C CB  . LEU B 1114 ? 0.2957 0.2034 0.2843 0.0105  -0.0175 0.0093  1112 LEU B CB  
17142 C CG  . LEU B 1114 ? 0.3028 0.2068 0.2908 0.0112  -0.0193 0.0063  1112 LEU B CG  
17143 C CD1 . LEU B 1114 ? 0.2836 0.1968 0.2776 0.0096  -0.0179 0.0046  1112 LEU B CD1 
17144 C CD2 . LEU B 1114 ? 0.3460 0.2395 0.3307 0.0078  -0.0219 0.0073  1112 LEU B CD2 
17145 N N   . TYR B 1115 ? 0.2791 0.1898 0.2630 0.0230  -0.0173 0.0064  1113 TYR B N   
17146 C CA  . TYR B 1115 ? 0.2872 0.1976 0.2690 0.0288  -0.0180 0.0039  1113 TYR B CA  
17147 C C   . TYR B 1115 ? 0.2875 0.2094 0.2734 0.0309  -0.0159 0.0026  1113 TYR B C   
17148 O O   . TYR B 1115 ? 0.2637 0.1890 0.2507 0.0337  -0.0158 0.0000  1113 TYR B O   
17149 C CB  . TYR B 1115 ? 0.3190 0.2217 0.2950 0.0323  -0.0195 0.0050  1113 TYR B CB  
17150 C CG  . TYR B 1115 ? 0.3025 0.1923 0.2731 0.0312  -0.0221 0.0058  1113 TYR B CG  
17151 C CD1 . TYR B 1115 ? 0.3191 0.2047 0.2901 0.0280  -0.0232 0.0047  1113 TYR B CD1 
17152 C CD2 . TYR B 1115 ? 0.3665 0.2482 0.3317 0.0333  -0.0235 0.0076  1113 TYR B CD2 
17153 C CE1 . TYR B 1115 ? 0.3648 0.2380 0.3305 0.0267  -0.0257 0.0054  1113 TYR B CE1 
17154 C CE2 . TYR B 1115 ? 0.3944 0.2635 0.3542 0.0322  -0.0260 0.0084  1113 TYR B CE2 
17155 C CZ  . TYR B 1115 ? 0.4144 0.2793 0.3745 0.0288  -0.0271 0.0072  1113 TYR B CZ  
17156 O OH  . TYR B 1115 ? 0.4290 0.2809 0.3835 0.0274  -0.0298 0.0080  1113 TYR B OH  
17157 N N   . HIS B 1116 ? 0.2531 0.1810 0.2413 0.0295  -0.0142 0.0046  1114 HIS B N   
17158 C CA  . HIS B 1116 ? 0.2623 0.2008 0.2544 0.0309  -0.0123 0.0035  1114 HIS B CA  
17159 C C   . HIS B 1116 ? 0.2634 0.2078 0.2602 0.0285  -0.0113 0.0017  1114 HIS B C   
17160 O O   . HIS B 1116 ? 0.2729 0.2235 0.2718 0.0307  -0.0106 -0.0004 1114 HIS B O   
17161 C CB  . HIS B 1116 ? 0.2644 0.2071 0.2572 0.0297  -0.0109 0.0059  1114 HIS B CB  
17162 C CG  . HIS B 1116 ? 0.3005 0.2406 0.2893 0.0333  -0.0117 0.0071  1114 HIS B CG  
17163 N ND1 . HIS B 1116 ? 0.3177 0.2492 0.3020 0.0331  -0.0130 0.0095  1114 HIS B ND1 
17164 C CD2 . HIS B 1116 ? 0.3217 0.2669 0.3105 0.0374  -0.0115 0.0064  1114 HIS B CD2 
17165 C CE1 . HIS B 1116 ? 0.3577 0.2888 0.3391 0.0370  -0.0136 0.0101  1114 HIS B CE1 
17166 N NE2 . HIS B 1116 ? 0.3628 0.3024 0.3471 0.0396  -0.0127 0.0083  1114 HIS B NE2 
17167 N N   . GLN B 1117 ? 0.2235 0.1663 0.2220 0.0239  -0.0111 0.0027  1115 GLN B N   
17168 C CA  . GLN B 1117 ? 0.2198 0.1680 0.2227 0.0217  -0.0103 0.0010  1115 GLN B CA  
17169 C C   . GLN B 1117 ? 0.2240 0.1695 0.2258 0.0239  -0.0116 -0.0017 1115 GLN B C   
17170 O O   . GLN B 1117 ? 0.2290 0.1806 0.2336 0.0247  -0.0108 -0.0037 1115 GLN B O   
17171 C CB  . GLN B 1117 ? 0.2344 0.1810 0.2393 0.0165  -0.0102 0.0027  1115 GLN B CB  
17172 C CG  . GLN B 1117 ? 0.2287 0.1798 0.2356 0.0140  -0.0083 0.0051  1115 GLN B CG  
17173 C CD  . GLN B 1117 ? 0.2308 0.1808 0.2398 0.0090  -0.0082 0.0068  1115 GLN B CD  
17174 O OE1 . GLN B 1117 ? 0.2584 0.2030 0.2668 0.0073  -0.0098 0.0065  1115 GLN B OE1 
17175 N NE2 . GLN B 1117 ? 0.2487 0.2040 0.2601 0.0068  -0.0062 0.0087  1115 GLN B NE2 
17176 N N   . LEU B 1118 ? 0.2253 0.1616 0.2228 0.0248  -0.0137 -0.0019 1116 LEU B N   
17177 C CA  . LEU B 1118 ? 0.2424 0.1753 0.2380 0.0273  -0.0151 -0.0046 1116 LEU B CA  
17178 C C   . LEU B 1118 ? 0.2399 0.1778 0.2352 0.0322  -0.0144 -0.0064 1116 LEU B C   
17179 O O   . LEU B 1118 ? 0.2616 0.2031 0.2583 0.0335  -0.0141 -0.0087 1116 LEU B O   
17180 C CB  . LEU B 1118 ? 0.2861 0.2074 0.2761 0.0280  -0.0175 -0.0043 1116 LEU B CB  
17181 C CG  . LEU B 1118 ? 0.3031 0.2187 0.2932 0.0229  -0.0187 -0.0033 1116 LEU B CG  
17182 C CD1 . LEU B 1118 ? 0.3314 0.2349 0.3154 0.0234  -0.0212 -0.0025 1116 LEU B CD1 
17183 C CD2 . LEU B 1118 ? 0.3198 0.2370 0.3118 0.0219  -0.0192 -0.0058 1116 LEU B CD2 
17184 N N   . ALA B 1119 ? 0.2582 0.1968 0.2519 0.0350  -0.0141 -0.0052 1117 ALA B N   
17185 C CA  . ALA B 1119 ? 0.2523 0.1963 0.2461 0.0397  -0.0135 -0.0067 1117 ALA B CA  
17186 C C   . ALA B 1119 ? 0.2450 0.1995 0.2439 0.0386  -0.0116 -0.0077 1117 ALA B C   
17187 O O   . ALA B 1119 ? 0.2443 0.2027 0.2440 0.0409  -0.0112 -0.0099 1117 ALA B O   
17188 C CB  . ALA B 1119 ? 0.2591 0.2029 0.2509 0.0424  -0.0135 -0.0050 1117 ALA B CB  
17189 N N   . ALA B 1120 ? 0.2138 0.1727 0.2159 0.0350  -0.0103 -0.0061 1118 ALA B N   
17190 C CA  . ALA B 1120 ? 0.1977 0.1658 0.2042 0.0338  -0.0086 -0.0069 1118 ALA B CA  
17191 C C   . ALA B 1120 ? 0.2153 0.1839 0.2234 0.0325  -0.0087 -0.0089 1118 ALA B C   
17192 O O   . ALA B 1120 ? 0.2256 0.1997 0.2353 0.0339  -0.0080 -0.0106 1118 ALA B O   
17193 C CB  . ALA B 1120 ? 0.2217 0.1933 0.2307 0.0303  -0.0073 -0.0049 1118 ALA B CB  
17194 N N   . ALA B 1121 ? 0.2028 0.1657 0.2104 0.0297  -0.0097 -0.0086 1119 ALA B N   
17195 C CA  . ALA B 1121 ? 0.2071 0.1706 0.2163 0.0281  -0.0100 -0.0104 1119 ALA B CA  
17196 C C   . ALA B 1121 ? 0.1928 0.1536 0.1991 0.0316  -0.0110 -0.0127 1119 ALA B C   
17197 O O   . ALA B 1121 ? 0.2017 0.1666 0.2096 0.0319  -0.0106 -0.0145 1119 ALA B O   
17198 C CB  . ALA B 1121 ? 0.2189 0.1773 0.2284 0.0240  -0.0110 -0.0093 1119 ALA B CB  
17199 N N   . LEU B 1122 ? 0.2106 0.1642 0.2124 0.0343  -0.0124 -0.0128 1120 LEU B N   
17200 C CA  . LEU B 1122 ? 0.1987 0.1496 0.1974 0.0381  -0.0133 -0.0152 1120 LEU B CA  
17201 C C   . LEU B 1122 ? 0.2277 0.1865 0.2277 0.0417  -0.0119 -0.0163 1120 LEU B C   
17202 O O   . LEU B 1122 ? 0.2238 0.1848 0.2235 0.0434  -0.0117 -0.0184 1120 LEU B O   
17203 C CB  . LEU B 1122 ? 0.2343 0.1754 0.2276 0.0405  -0.0152 -0.0150 1120 LEU B CB  
17204 C CG  . LEU B 1122 ? 0.2765 0.2085 0.2678 0.0370  -0.0170 -0.0141 1120 LEU B CG  
17205 C CD1 . LEU B 1122 ? 0.2828 0.2049 0.2683 0.0396  -0.0188 -0.0136 1120 LEU B CD1 
17206 C CD2 . LEU B 1122 ? 0.2702 0.2001 0.2614 0.0351  -0.0179 -0.0160 1120 LEU B CD2 
17207 N N   . ALA B 1123 ? 0.2046 0.1679 0.2058 0.0428  -0.0109 -0.0148 1121 ALA B N   
17208 C CA  . ALA B 1123 ? 0.2199 0.1910 0.2225 0.0460  -0.0097 -0.0157 1121 ALA B CA  
17209 C C   . ALA B 1123 ? 0.2437 0.2225 0.2501 0.0439  -0.0084 -0.0166 1121 ALA B C   
17210 O O   . ALA B 1123 ? 0.2077 0.1925 0.2150 0.0464  -0.0076 -0.0179 1121 ALA B O   
17211 C CB  . ALA B 1123 ? 0.2193 0.1939 0.2228 0.0465  -0.0092 -0.0137 1121 ALA B CB  
17212 N N   . THR B 1124 ? 0.1920 0.1710 0.2008 0.0396  -0.0081 -0.0160 1122 THR B N   
17213 C CA  . THR B 1124 ? 0.1840 0.1695 0.1962 0.0375  -0.0070 -0.0168 1122 THR B CA  
17214 C C   . THR B 1124 ? 0.1727 0.1548 0.1842 0.0364  -0.0078 -0.0184 1122 THR B C   
17215 O O   . THR B 1124 ? 0.2055 0.1914 0.2196 0.0340  -0.0072 -0.0189 1122 THR B O   
17216 C CB  . THR B 1124 ? 0.1992 0.1882 0.2147 0.0339  -0.0061 -0.0152 1122 THR B CB  
17217 O OG1 . THR B 1124 ? 0.1926 0.1758 0.2075 0.0316  -0.0068 -0.0137 1122 THR B OG1 
17218 C CG2 . THR B 1124 ? 0.1840 0.1784 0.2005 0.0353  -0.0051 -0.0141 1122 THR B CG2 
17219 N N   . GLY B 1125 ? 0.1840 0.1589 0.1916 0.0382  -0.0093 -0.0194 1123 GLY B N   
17220 C CA  . GLY B 1125 ? 0.2011 0.1726 0.2071 0.0381  -0.0102 -0.0212 1123 GLY B CA  
17221 C C   . GLY B 1125 ? 0.2062 0.1730 0.2127 0.0339  -0.0114 -0.0207 1123 GLY B C   
17222 O O   . GLY B 1125 ? 0.2229 0.1875 0.2284 0.0332  -0.0123 -0.0222 1123 GLY B O   
17223 N N   . ASN B 1126 ? 0.2082 0.1738 0.2163 0.0312  -0.0114 -0.0187 1124 ASN B N   
17224 C CA  . ASN B 1126 ? 0.1866 0.1497 0.1964 0.0269  -0.0122 -0.0179 1124 ASN B CA  
17225 C C   . ASN B 1126 ? 0.1977 0.1510 0.2037 0.0264  -0.0144 -0.0179 1124 ASN B C   
17226 O O   . ASN B 1126 ? 0.2272 0.1753 0.2295 0.0290  -0.0151 -0.0177 1124 ASN B O   
17227 C CB  . ASN B 1126 ? 0.2115 0.1785 0.2249 0.0241  -0.0110 -0.0156 1124 ASN B CB  
17228 C CG  . ASN B 1126 ? 0.1928 0.1686 0.2096 0.0243  -0.0091 -0.0157 1124 ASN B CG  
17229 O OD1 . ASN B 1126 ? 0.2015 0.1810 0.2206 0.0230  -0.0088 -0.0166 1124 ASN B OD1 
17230 N ND2 . ASN B 1126 ? 0.1883 0.1674 0.2054 0.0259  -0.0080 -0.0147 1124 ASN B ND2 
17231 N N   . SER B 1127 ? 0.2212 0.1721 0.2283 0.0229  -0.0156 -0.0179 1125 SER B N   
17232 C CA  . SER B 1127 ? 0.2289 0.1714 0.2337 0.0206  -0.0176 -0.0170 1125 SER B CA  
17233 C C   . SER B 1127 ? 0.2351 0.1797 0.2435 0.0170  -0.0168 -0.0143 1125 SER B C   
17234 O O   . SER B 1127 ? 0.2224 0.1747 0.2348 0.0162  -0.0149 -0.0134 1125 SER B O   
17235 C CB  . SER B 1127 ? 0.2577 0.1968 0.2620 0.0185  -0.0194 -0.0185 1125 SER B CB  
17236 O OG  . SER B 1127 ? 0.2997 0.2455 0.3089 0.0156  -0.0186 -0.0182 1125 SER B OG  
17237 N N   . VAL B 1128 ? 0.2401 0.1776 0.2466 0.0147  -0.0183 -0.0128 1126 VAL B N   
17238 C CA  . VAL B 1128 ? 0.2381 0.1774 0.2475 0.0112  -0.0175 -0.0100 1126 VAL B CA  
17239 C C   . VAL B 1128 ? 0.2683 0.2028 0.2782 0.0067  -0.0194 -0.0091 1126 VAL B C   
17240 O O   . VAL B 1128 ? 0.2750 0.2016 0.2811 0.0066  -0.0218 -0.0102 1126 VAL B O   
17241 C CB  . VAL B 1128 ? 0.2399 0.1763 0.2467 0.0128  -0.0171 -0.0082 1126 VAL B CB  
17242 C CG1 . VAL B 1128 ? 0.2385 0.1803 0.2452 0.0172  -0.0153 -0.0090 1126 VAL B CG1 
17243 C CG2 . VAL B 1128 ? 0.2736 0.1989 0.2745 0.0138  -0.0195 -0.0084 1126 VAL B CG2 
17244 N N   . ALA B 1129 ? 0.2318 0.1711 0.2463 0.0029  -0.0183 -0.0070 1127 ALA B N   
17245 C CA  . ALA B 1129 ? 0.2412 0.1768 0.2566 -0.0018 -0.0197 -0.0052 1127 ALA B CA  
17246 C C   . ALA B 1129 ? 0.2317 0.1675 0.2474 -0.0031 -0.0184 -0.0022 1127 ALA B C   
17247 O O   . ALA B 1129 ? 0.2290 0.1726 0.2482 -0.0030 -0.0159 -0.0012 1127 ALA B O   
17248 C CB  . ALA B 1129 ? 0.2623 0.2044 0.2834 -0.0052 -0.0195 -0.0052 1127 ALA B CB  
17249 N N   . ILE B 1130 ? 0.2300 0.1572 0.2416 -0.0041 -0.0200 -0.0008 1128 ILE B N   
17250 C CA  . ILE B 1130 ? 0.2337 0.1598 0.2445 -0.0052 -0.0190 0.0021  1128 ILE B CA  
17251 C C   . ILE B 1130 ? 0.2326 0.1596 0.2467 -0.0110 -0.0191 0.0047  1128 ILE B C   
17252 O O   . ILE B 1130 ? 0.2541 0.1760 0.2677 -0.0141 -0.0214 0.0045  1128 ILE B O   
17253 C CB  . ILE B 1130 ? 0.2552 0.1709 0.2592 -0.0029 -0.0207 0.0024  1128 ILE B CB  
17254 C CG1 . ILE B 1130 ? 0.2706 0.1854 0.2714 0.0030  -0.0208 -0.0004 1128 ILE B CG1 
17255 C CG2 . ILE B 1130 ? 0.2743 0.1898 0.2773 -0.0034 -0.0194 0.0054  1128 ILE B CG2 
17256 C CD1 . ILE B 1130 ? 0.2834 0.1873 0.2773 0.0056  -0.0229 -0.0008 1128 ILE B CD1 
17257 N N   . ASP B 1131 ? 0.2394 0.1727 0.2567 -0.0126 -0.0167 0.0070  1129 ASP B N   
17258 C CA  . ASP B 1131 ? 0.2416 0.1768 0.2624 -0.0180 -0.0164 0.0097  1129 ASP B CA  
17259 C C   . ASP B 1131 ? 0.2531 0.1780 0.2696 -0.0208 -0.0187 0.0117  1129 ASP B C   
17260 O O   . ASP B 1131 ? 0.2690 0.1887 0.2811 -0.0196 -0.0186 0.0132  1129 ASP B O   
17261 C CB  . ASP B 1131 ? 0.2229 0.1658 0.2466 -0.0183 -0.0133 0.0119  1129 ASP B CB  
17262 C CG  . ASP B 1131 ? 0.2379 0.1836 0.2651 -0.0236 -0.0125 0.0149  1129 ASP B CG  
17263 O OD1 . ASP B 1131 ? 0.2651 0.2110 0.2952 -0.0270 -0.0140 0.0148  1129 ASP B OD1 
17264 O OD2 . ASP B 1131 ? 0.2784 0.2262 0.3054 -0.0243 -0.0106 0.0174  1129 ASP B OD2 
17265 N N   . ALA B 1132 ? 0.2687 0.1904 0.2862 -0.0247 -0.0210 0.0117  1130 ALA B N   
17266 C CA  . ALA B 1132 ? 0.2740 0.1852 0.2872 -0.0279 -0.0235 0.0134  1130 ALA B CA  
17267 C C   . ALA B 1132 ? 0.3014 0.2138 0.3155 -0.0316 -0.0220 0.0175  1130 ALA B C   
17268 O O   . ALA B 1132 ? 0.3150 0.2182 0.3241 -0.0329 -0.0235 0.0194  1130 ALA B O   
17269 C CB  . ALA B 1132 ? 0.2858 0.1943 0.3004 -0.0318 -0.0263 0.0126  1130 ALA B CB  
17270 N N   . ALA B 1133 ? 0.2896 0.2130 0.3097 -0.0332 -0.0191 0.0189  1131 ALA B N   
17271 C CA  . ALA B 1133 ? 0.3393 0.2646 0.3604 -0.0366 -0.0174 0.0228  1131 ALA B CA  
17272 C C   . ALA B 1133 ? 0.3392 0.2607 0.3551 -0.0334 -0.0163 0.0239  1131 ALA B C   
17273 O O   . ALA B 1133 ? 0.3542 0.2750 0.3693 -0.0361 -0.0152 0.0273  1131 ALA B O   
17274 C CB  . ALA B 1133 ? 0.3081 0.2465 0.3367 -0.0384 -0.0143 0.0237  1131 ALA B CB  
17275 N N   . SER B 1134 ? 0.3097 0.2291 0.3222 -0.0277 -0.0164 0.0213  1132 SER B N   
17276 C CA  . SER B 1134 ? 0.3230 0.2381 0.3303 -0.0244 -0.0159 0.0223  1132 SER B CA  
17277 C C   . SER B 1134 ? 0.3002 0.2027 0.3012 -0.0258 -0.0185 0.0241  1132 SER B C   
17278 O O   . SER B 1134 ? 0.3357 0.2344 0.3325 -0.0247 -0.0181 0.0261  1132 SER B O   
17279 C CB  . SER B 1134 ? 0.3066 0.2222 0.3120 -0.0180 -0.0159 0.0190  1132 SER B CB  
17280 O OG  . SER B 1134 ? 0.3062 0.2137 0.3081 -0.0164 -0.0188 0.0165  1132 SER B OG  
17281 N N   . GLY B 1135 ? 0.3149 0.2103 0.3145 -0.0283 -0.0215 0.0233  1133 GLY B N   
17282 C CA  . GLY B 1135 ? 0.3287 0.2110 0.3218 -0.0298 -0.0243 0.0248  1133 GLY B CA  
17283 C C   . GLY B 1135 ? 0.3621 0.2358 0.3483 -0.0239 -0.0258 0.0230  1133 GLY B C   
17284 O O   . GLY B 1135 ? 0.3677 0.2304 0.3477 -0.0243 -0.0278 0.0246  1133 GLY B O   
17285 N N   . LEU B 1136 ? 0.3527 0.2309 0.3396 -0.0184 -0.0250 0.0198  1134 LEU B N   
17286 C CA  . LEU B 1136 ? 0.3531 0.2255 0.3343 -0.0122 -0.0258 0.0181  1134 LEU B CA  
17287 C C   . LEU B 1136 ? 0.3725 0.2365 0.3497 -0.0097 -0.0288 0.0149  1134 LEU B C   
17288 O O   . LEU B 1136 ? 0.3592 0.2206 0.3328 -0.0039 -0.0292 0.0128  1134 LEU B O   
17289 C CB  . LEU B 1136 ? 0.3139 0.1967 0.2981 -0.0078 -0.0230 0.0168  1134 LEU B CB  
17290 C CG  . LEU B 1136 ? 0.3170 0.2066 0.3036 -0.0091 -0.0202 0.0198  1134 LEU B CG  
17291 C CD1 . LEU B 1136 ? 0.3185 0.2185 0.3083 -0.0051 -0.0177 0.0181  1134 LEU B CD1 
17292 C CD2 . LEU B 1136 ? 0.3807 0.2616 0.3610 -0.0086 -0.0212 0.0225  1134 LEU B CD2 
17293 N N   . GLN B 1137 ? 0.3669 0.2271 0.3447 -0.0139 -0.0308 0.0145  1135 GLN B N   
17294 C CA  . GLN B 1137 ? 0.3840 0.2366 0.3580 -0.0117 -0.0336 0.0112  1135 GLN B CA  
17295 C C   . GLN B 1137 ? 0.4276 0.2678 0.3932 -0.0073 -0.0357 0.0106  1135 GLN B C   
17296 O O   . GLN B 1137 ? 0.4229 0.2604 0.3854 -0.0021 -0.0366 0.0073  1135 GLN B O   
17297 C CB  . GLN B 1137 ? 0.4523 0.3011 0.4275 -0.0177 -0.0359 0.0114  1135 GLN B CB  
17298 C CG  . GLN B 1137 ? 0.3889 0.2496 0.3722 -0.0208 -0.0343 0.0109  1135 GLN B CG  
17299 C CD  . GLN B 1137 ? 0.3796 0.2489 0.3687 -0.0255 -0.0318 0.0145  1135 GLN B CD  
17300 O OE1 . GLN B 1137 ? 0.3900 0.2580 0.3774 -0.0259 -0.0307 0.0173  1135 GLN B OE1 
17301 N NE2 . GLN B 1137 ? 0.3666 0.2448 0.3624 -0.0289 -0.0310 0.0143  1135 GLN B NE2 
17302 N N   . ALA B 1138 ? 0.3963 0.2292 0.3580 -0.0092 -0.0365 0.0138  1136 ALA B N   
17303 C CA  . ALA B 1138 ? 0.4421 0.2623 0.3954 -0.0052 -0.0388 0.0136  1136 ALA B CA  
17304 C C   . ALA B 1138 ? 0.4525 0.2766 0.4046 0.0023  -0.0372 0.0120  1136 ALA B C   
17305 O O   . ALA B 1138 ? 0.4707 0.2857 0.4163 0.0072  -0.0391 0.0106  1136 ALA B O   
17306 C CB  . ALA B 1138 ? 0.4536 0.2660 0.4033 -0.0091 -0.0397 0.0178  1136 ALA B CB  
17307 N N   . SER B 1139 ? 0.4187 0.2559 0.3767 0.0033  -0.0340 0.0121  1137 SER B N   
17308 C CA  . SER B 1139 ? 0.4065 0.2483 0.3639 0.0098  -0.0325 0.0109  1137 SER B CA  
17309 C C   . SER B 1139 ? 0.4323 0.2752 0.3892 0.0150  -0.0330 0.0066  1137 SER B C   
17310 O O   . SER B 1139 ? 0.4107 0.2551 0.3658 0.0209  -0.0325 0.0053  1137 SER B O   
17311 C CB  . SER B 1139 ? 0.4134 0.2688 0.3774 0.0089  -0.0290 0.0122  1137 SER B CB  
17312 O OG  . SER B 1139 ? 0.4318 0.2863 0.3953 0.0053  -0.0283 0.0161  1137 SER B OG  
17313 N N   . LEU B 1140 ? 0.4252 0.2677 0.3836 0.0127  -0.0340 0.0045  1138 LEU B N   
17314 C CA  . LEU B 1140 ? 0.4376 0.2808 0.3951 0.0172  -0.0345 0.0005  1138 LEU B CA  
17315 C C   . LEU B 1140 ? 0.4645 0.2940 0.4150 0.0181  -0.0379 -0.0012 1138 LEU B C   
17316 O O   . LEU B 1140 ? 0.5034 0.3323 0.4534 0.0194  -0.0388 -0.0043 1138 LEU B O   
17317 C CB  . LEU B 1140 ? 0.4439 0.2978 0.4082 0.0149  -0.0329 -0.0010 1138 LEU B CB  
17318 C CG  . LEU B 1140 ? 0.4241 0.2916 0.3948 0.0149  -0.0295 0.0000  1138 LEU B CG  
17319 C CD1 . LEU B 1140 ? 0.3972 0.2742 0.3738 0.0136  -0.0282 -0.0020 1138 LEU B CD1 
17320 C CD2 . LEU B 1140 ? 0.4338 0.3040 0.4028 0.0211  -0.0283 -0.0005 1138 LEU B CD2 
17321 N N   . LYS B 1141 ? 0.5013 0.3192 0.4460 0.0174  -0.0400 0.0008  1139 LYS B N   
17322 C CA  . LYS B 1141 ? 0.5607 0.3644 0.4979 0.0186  -0.0435 -0.0008 1139 LYS B CA  
17323 C C   . LYS B 1141 ? 0.5620 0.3640 0.4951 0.0268  -0.0437 -0.0042 1139 LYS B C   
17324 O O   . LYS B 1141 ? 0.5710 0.3776 0.5044 0.0316  -0.0420 -0.0039 1139 LYS B O   
17325 C CB  . LYS B 1141 ? 0.5554 0.3470 0.4868 0.0165  -0.0456 0.0023  1139 LYS B CB  
17326 N N   . ASN B 1142 ? 0.5972 0.3931 0.5267 0.0283  -0.0456 -0.0075 1140 ASN B N   
17327 C CA  . ASN B 1142 ? 0.5837 0.3768 0.5086 0.0360  -0.0460 -0.0109 1140 ASN B CA  
17328 C C   . ASN B 1142 ? 0.5546 0.3623 0.4852 0.0400  -0.0427 -0.0126 1140 ASN B C   
17329 O O   . ASN B 1142 ? 0.5409 0.3495 0.4691 0.0468  -0.0422 -0.0144 1140 ASN B O   
17330 C CB  . ASN B 1142 ? 0.6545 0.4369 0.5721 0.0407  -0.0476 -0.0101 1140 ASN B CB  
17331 C CG  . ASN B 1142 ? 0.7117 0.4788 0.6232 0.0366  -0.0510 -0.0083 1140 ASN B CG  
17332 O OD1 . ASN B 1142 ? 0.7438 0.5037 0.6528 0.0333  -0.0533 -0.0097 1140 ASN B OD1 
17333 N ND2 . ASN B 1142 ? 0.7490 0.5110 0.6578 0.0364  -0.0515 -0.0051 1140 ASN B ND2 
17334 N N   . LEU B 1143 ? 0.5244 0.3437 0.4626 0.0358  -0.0406 -0.0120 1141 LEU B N   
17335 C CA  . LEU B 1143 ? 0.5003 0.3330 0.4439 0.0388  -0.0377 -0.0136 1141 LEU B CA  
17336 C C   . LEU B 1143 ? 0.4583 0.2894 0.3989 0.0431  -0.0384 -0.0176 1141 LEU B C   
17337 O O   . LEU B 1143 ? 0.5397 0.3634 0.4773 0.0410  -0.0405 -0.0191 1141 LEU B O   
17338 C CB  . LEU B 1143 ? 0.4708 0.3141 0.4222 0.0330  -0.0358 -0.0123 1141 LEU B CB  
17339 C CG  . LEU B 1143 ? 0.4634 0.3214 0.4213 0.0344  -0.0326 -0.0127 1141 LEU B CG  
17340 C CD1 . LEU B 1143 ? 0.4205 0.2827 0.3795 0.0365  -0.0310 -0.0104 1141 LEU B CD1 
17341 C CD2 . LEU B 1143 ? 0.3996 0.2654 0.3641 0.0286  -0.0315 -0.0119 1141 LEU B CD2 
17342 N N   . PRO B 1144 ? 0.4642 0.3022 0.4054 0.0491  -0.0366 -0.0194 1142 PRO B N   
17343 C CA  . PRO B 1144 ? 0.5126 0.3505 0.4513 0.0531  -0.0367 -0.0232 1142 PRO B CA  
17344 C C   . PRO B 1144 ? 0.4725 0.3160 0.4155 0.0486  -0.0363 -0.0243 1142 PRO B C   
17345 O O   . PRO B 1144 ? 0.4130 0.2656 0.3626 0.0443  -0.0346 -0.0225 1142 PRO B O   
17346 C CB  . PRO B 1144 ? 0.5158 0.3639 0.4570 0.0590  -0.0341 -0.0240 1142 PRO B CB  
17347 C CG  . PRO B 1144 ? 0.4967 0.3460 0.4390 0.0594  -0.0336 -0.0210 1142 PRO B CG  
17348 C CD  . PRO B 1144 ? 0.4840 0.3310 0.4285 0.0522  -0.0342 -0.0180 1142 PRO B CD  
17349 N N   . GLN B 1145 ? 0.5005 0.3380 0.4392 0.0499  -0.0379 -0.0273 1143 GLN B N   
17350 C CA  . GLN B 1145 ? 0.4549 0.2965 0.3967 0.0458  -0.0379 -0.0284 1143 GLN B CA  
17351 C C   . GLN B 1145 ? 0.4478 0.3044 0.3965 0.0463  -0.0347 -0.0287 1143 GLN B C   
17352 O O   . GLN B 1145 ? 0.4046 0.2674 0.3585 0.0415  -0.0340 -0.0280 1143 GLN B O   
17353 C CB  . GLN B 1145 ? 0.5052 0.3381 0.4405 0.0481  -0.0401 -0.0319 1143 GLN B CB  
17354 N N   . THR B 1146 ? 0.4434 0.3058 0.3922 0.0520  -0.0327 -0.0296 1144 THR B N   
17355 C CA  . THR B 1146 ? 0.4433 0.3196 0.3984 0.0523  -0.0297 -0.0297 1144 THR B CA  
17356 C C   . THR B 1146 ? 0.4125 0.2959 0.3742 0.0474  -0.0284 -0.0265 1144 THR B C   
17357 O O   . THR B 1146 ? 0.4432 0.3353 0.4103 0.0445  -0.0269 -0.0263 1144 THR B O   
17358 C CB  . THR B 1146 ? 0.4409 0.3222 0.3952 0.0590  -0.0280 -0.0306 1144 THR B CB  
17359 O OG1 . THR B 1146 ? 0.5388 0.4136 0.4897 0.0615  -0.0289 -0.0292 1144 THR B OG1 
17360 C CG2 . THR B 1146 ? 0.4932 0.3727 0.4431 0.0637  -0.0282 -0.0341 1144 THR B CG2 
17361 N N   . VAL B 1147 ? 0.3689 0.2483 0.3299 0.0467  -0.0289 -0.0241 1145 VAL B N   
17362 C CA  . VAL B 1147 ? 0.3376 0.2233 0.3044 0.0421  -0.0275 -0.0211 1145 VAL B CA  
17363 C C   . VAL B 1147 ? 0.3740 0.2564 0.3424 0.0357  -0.0289 -0.0200 1145 VAL B C   
17364 O O   . VAL B 1147 ? 0.3610 0.2515 0.3352 0.0318  -0.0275 -0.0190 1145 VAL B O   
17365 C CB  . VAL B 1147 ? 0.3284 0.2118 0.2939 0.0435  -0.0274 -0.0187 1145 VAL B CB  
17366 C CG1 . VAL B 1147 ? 0.3839 0.2749 0.3553 0.0392  -0.0257 -0.0158 1145 VAL B CG1 
17367 C CG2 . VAL B 1147 ? 0.3441 0.2305 0.3078 0.0502  -0.0264 -0.0198 1145 VAL B CG2 
17368 N N   . GLY B 1148 ? 0.3693 0.2400 0.3325 0.0344  -0.0317 -0.0204 1146 GLY B N   
17369 C CA  . GLY B 1148 ? 0.3656 0.2331 0.3304 0.0281  -0.0333 -0.0193 1146 GLY B CA  
17370 C C   . GLY B 1148 ? 0.3755 0.2498 0.3443 0.0258  -0.0328 -0.0208 1146 GLY B C   
17371 O O   . GLY B 1148 ? 0.3804 0.2582 0.3538 0.0205  -0.0328 -0.0193 1146 GLY B O   
17372 N N   . LEU B 1149 ? 0.3704 0.2468 0.3374 0.0298  -0.0324 -0.0238 1147 LEU B N   
17373 C CA  . LEU B 1149 ? 0.3878 0.2704 0.3582 0.0280  -0.0319 -0.0253 1147 LEU B CA  
17374 C C   . LEU B 1149 ? 0.3741 0.2687 0.3521 0.0255  -0.0293 -0.0235 1147 LEU B C   
17375 O O   . LEU B 1149 ? 0.3878 0.2869 0.3695 0.0222  -0.0293 -0.0237 1147 LEU B O   
17376 C CB  . LEU B 1149 ? 0.4709 0.3544 0.4379 0.0333  -0.0315 -0.0285 1147 LEU B CB  
17377 N N   . ARG B 1150 ? 0.3349 0.2346 0.3151 0.0271  -0.0273 -0.0219 1148 ARG B N   
17378 C CA  . ARG B 1150 ? 0.3282 0.2388 0.3151 0.0251  -0.0248 -0.0203 1148 ARG B CA  
17379 C C   . ARG B 1150 ? 0.2847 0.1953 0.2748 0.0202  -0.0248 -0.0172 1148 ARG B C   
17380 O O   . ARG B 1150 ? 0.2844 0.2035 0.2798 0.0183  -0.0228 -0.0158 1148 ARG B O   
17381 C CB  . ARG B 1150 ? 0.3034 0.2200 0.2909 0.0293  -0.0226 -0.0201 1148 ARG B CB  
17382 C CG  . ARG B 1150 ? 0.3232 0.2437 0.3095 0.0338  -0.0217 -0.0227 1148 ARG B CG  
17383 C CD  . ARG B 1150 ? 0.3416 0.2738 0.3333 0.0335  -0.0191 -0.0224 1148 ARG B CD  
17384 N NE  . ARG B 1150 ? 0.2991 0.2356 0.2897 0.0381  -0.0180 -0.0243 1148 ARG B NE  
17385 C CZ  . ARG B 1150 ? 0.3124 0.2553 0.3045 0.0409  -0.0162 -0.0238 1148 ARG B CZ  
17386 N NH1 . ARG B 1150 ? 0.2776 0.2236 0.2725 0.0396  -0.0153 -0.0216 1148 ARG B NH1 
17387 N NH2 . ARG B 1150 ? 0.2819 0.2286 0.2729 0.0449  -0.0153 -0.0256 1148 ARG B NH2 
17388 N N   . VAL B 1151 ? 0.3117 0.2130 0.2984 0.0183  -0.0269 -0.0161 1149 VAL B N   
17389 C CA  . VAL B 1151 ? 0.2899 0.1905 0.2788 0.0140  -0.0268 -0.0130 1149 VAL B CA  
17390 C C   . VAL B 1151 ? 0.3306 0.2279 0.3207 0.0087  -0.0288 -0.0125 1149 VAL B C   
17391 O O   . VAL B 1151 ? 0.3556 0.2443 0.3413 0.0085  -0.0314 -0.0139 1149 VAL B O   
17392 C CB  . VAL B 1151 ? 0.3300 0.2225 0.3140 0.0157  -0.0277 -0.0115 1149 VAL B CB  
17393 C CG1 . VAL B 1151 ? 0.3712 0.2617 0.3569 0.0106  -0.0280 -0.0081 1149 VAL B CG1 
17394 C CG2 . VAL B 1151 ? 0.3480 0.2452 0.3318 0.0206  -0.0257 -0.0115 1149 VAL B CG2 
17395 N N   . SER B 1152 ? 0.3009 0.2051 0.2969 0.0044  -0.0276 -0.0105 1150 SER B N   
17396 C CA  . SER B 1152 ? 0.3069 0.2085 0.3047 -0.0011 -0.0294 -0.0092 1150 SER B CA  
17397 C C   . SER B 1152 ? 0.3173 0.2219 0.3185 -0.0046 -0.0280 -0.0057 1150 SER B C   
17398 O O   . SER B 1152 ? 0.3029 0.2133 0.3059 -0.0029 -0.0255 -0.0046 1150 SER B O   
17399 C CB  . SER B 1152 ? 0.3358 0.2435 0.3379 -0.0031 -0.0295 -0.0106 1150 SER B CB  
17400 O OG  . SER B 1152 ? 0.3783 0.2972 0.3862 -0.0030 -0.0267 -0.0100 1150 SER B OG  
17401 N N   . TRP B 1153 ? 0.2941 0.1944 0.2956 -0.0096 -0.0298 -0.0039 1151 TRP B N   
17402 C CA  . TRP B 1153 ? 0.2871 0.1902 0.2919 -0.0136 -0.0286 -0.0004 1151 TRP B CA  
17403 C C   . TRP B 1153 ? 0.3179 0.2286 0.3294 -0.0182 -0.0283 0.0003  1151 TRP B C   
17404 O O   . TRP B 1153 ? 0.3489 0.2572 0.3605 -0.0202 -0.0305 -0.0010 1151 TRP B O   
17405 C CB  . TRP B 1153 ? 0.3197 0.2116 0.3196 -0.0161 -0.0309 0.0014  1151 TRP B CB  
17406 C CG  . TRP B 1153 ? 0.3186 0.2037 0.3123 -0.0116 -0.0310 0.0012  1151 TRP B CG  
17407 C CD1 . TRP B 1153 ? 0.3563 0.2332 0.3438 -0.0073 -0.0328 -0.0013 1151 TRP B CD1 
17408 C CD2 . TRP B 1153 ? 0.3258 0.2119 0.3189 -0.0106 -0.0291 0.0037  1151 TRP B CD2 
17409 N NE1 . TRP B 1153 ? 0.3536 0.2264 0.3369 -0.0036 -0.0323 -0.0006 1151 TRP B NE1 
17410 C CE2 . TRP B 1153 ? 0.3368 0.2150 0.3233 -0.0056 -0.0301 0.0026  1151 TRP B CE2 
17411 C CE3 . TRP B 1153 ? 0.3152 0.2079 0.3123 -0.0133 -0.0267 0.0068  1151 TRP B CE3 
17412 C CZ2 . TRP B 1153 ? 0.3634 0.2404 0.3475 -0.0034 -0.0289 0.0044  1151 TRP B CZ2 
17413 C CZ3 . TRP B 1153 ? 0.3269 0.2182 0.3214 -0.0112 -0.0255 0.0086  1151 TRP B CZ3 
17414 C CH2 . TRP B 1153 ? 0.3497 0.2332 0.3378 -0.0063 -0.0267 0.0075  1151 TRP B CH2 
17415 N N   . SER B 1154 ? 0.2675 0.1875 0.2843 -0.0194 -0.0255 0.0022  1152 SER B N   
17416 C CA  . SER B 1154 ? 0.2649 0.1934 0.2885 -0.0230 -0.0248 0.0028  1152 SER B CA  
17417 C C   . SER B 1154 ? 0.2592 0.1896 0.2858 -0.0279 -0.0241 0.0064  1152 SER B C   
17418 O O   . SER B 1154 ? 0.2710 0.2036 0.2977 -0.0273 -0.0219 0.0084  1152 SER B O   
17419 C CB  . SER B 1154 ? 0.2890 0.2279 0.3168 -0.0202 -0.0220 0.0017  1152 SER B CB  
17420 O OG  . SER B 1154 ? 0.2660 0.2127 0.3002 -0.0234 -0.0215 0.0024  1152 SER B OG  
17421 N N   . LYS B 1155 ? 0.2683 0.1983 0.2976 -0.0327 -0.0260 0.0072  1153 LYS B N   
17422 C CA  . LYS B 1155 ? 0.3154 0.2498 0.3493 -0.0379 -0.0252 0.0106  1153 LYS B CA  
17423 C C   . LYS B 1155 ? 0.3068 0.2532 0.3484 -0.0392 -0.0236 0.0105  1153 LYS B C   
17424 O O   . LYS B 1155 ? 0.3115 0.2629 0.3579 -0.0437 -0.0230 0.0130  1153 LYS B O   
17425 C CB  . LYS B 1155 ? 0.3464 0.2726 0.3783 -0.0429 -0.0285 0.0118  1153 LYS B CB  
17426 N N   . ASP B 1156 ? 0.2495 0.2004 0.2923 -0.0354 -0.0228 0.0078  1154 ASP B N   
17427 C CA  . ASP B 1156 ? 0.2260 0.1875 0.2757 -0.0361 -0.0216 0.0075  1154 ASP B CA  
17428 C C   . ASP B 1156 ? 0.2341 0.1994 0.2833 -0.0308 -0.0199 0.0049  1154 ASP B C   
17429 O O   . ASP B 1156 ? 0.2309 0.1942 0.2784 -0.0287 -0.0215 0.0022  1154 ASP B O   
17430 C CB  . ASP B 1156 ? 0.2488 0.2093 0.3005 -0.0392 -0.0247 0.0065  1154 ASP B CB  
17431 C CG  . ASP B 1156 ? 0.2289 0.2004 0.2881 -0.0405 -0.0237 0.0068  1154 ASP B CG  
17432 O OD1 . ASP B 1156 ? 0.2134 0.1923 0.2752 -0.0375 -0.0209 0.0063  1154 ASP B OD1 
17433 O OD2 . ASP B 1156 ? 0.2368 0.2093 0.2992 -0.0446 -0.0258 0.0074  1154 ASP B OD2 
17434 N N   . TRP B 1157 ? 0.2020 0.1728 0.2525 -0.0288 -0.0168 0.0059  1155 TRP B N   
17435 C CA  . TRP B 1157 ? 0.2035 0.1769 0.2527 -0.0239 -0.0152 0.0037  1155 TRP B CA  
17436 C C   . TRP B 1157 ? 0.2302 0.2097 0.2833 -0.0232 -0.0154 0.0018  1155 TRP B C   
17437 O O   . TRP B 1157 ? 0.2380 0.2163 0.2889 -0.0200 -0.0159 -0.0008 1155 TRP B O   
17438 C CB  . TRP B 1157 ? 0.2314 0.2099 0.2815 -0.0223 -0.0120 0.0051  1155 TRP B CB  
17439 C CG  . TRP B 1157 ? 0.2019 0.1751 0.2480 -0.0226 -0.0115 0.0071  1155 TRP B CG  
17440 C CD1 . TRP B 1157 ? 0.2124 0.1761 0.2538 -0.0236 -0.0137 0.0076  1155 TRP B CD1 
17441 C CD2 . TRP B 1157 ? 0.2031 0.1800 0.2494 -0.0219 -0.0088 0.0089  1155 TRP B CD2 
17442 N NE1 . TRP B 1157 ? 0.2223 0.1836 0.2611 -0.0235 -0.0125 0.0097  1155 TRP B NE1 
17443 C CE2 . TRP B 1157 ? 0.2046 0.1740 0.2463 -0.0226 -0.0095 0.0106  1155 TRP B CE2 
17444 C CE3 . TRP B 1157 ? 0.2228 0.2082 0.2725 -0.0207 -0.0059 0.0092  1155 TRP B CE3 
17445 C CZ2 . TRP B 1157 ? 0.2365 0.2071 0.2768 -0.0221 -0.0073 0.0127  1155 TRP B CZ2 
17446 C CZ3 . TRP B 1157 ? 0.2283 0.2147 0.2764 -0.0202 -0.0037 0.0112  1155 TRP B CZ3 
17447 C CH2 . TRP B 1157 ? 0.2394 0.2186 0.2830 -0.0210 -0.0045 0.0129  1155 TRP B CH2 
17448 N N   . ALA B 1158 ? 0.2051 0.1913 0.2640 -0.0261 -0.0150 0.0030  1156 ALA B N   
17449 C CA  . ALA B 1158 ? 0.2132 0.2056 0.2760 -0.0252 -0.0150 0.0014  1156 ALA B CA  
17450 C C   . ALA B 1158 ? 0.2322 0.2198 0.2933 -0.0257 -0.0183 -0.0006 1156 ALA B C   
17451 O O   . ALA B 1158 ? 0.2929 0.2827 0.3542 -0.0234 -0.0186 -0.0027 1156 ALA B O   
17452 C CB  . ALA B 1158 ? 0.1904 0.1912 0.2599 -0.0281 -0.0138 0.0033  1156 ALA B CB  
17453 N N   . ALA B 1159 ? 0.2116 0.1925 0.2705 -0.0286 -0.0209 0.0000  1157 ALA B N   
17454 C CA  . ALA B 1159 ? 0.2519 0.2276 0.3085 -0.0291 -0.0241 -0.0020 1157 ALA B CA  
17455 C C   . ALA B 1159 ? 0.2702 0.2387 0.3202 -0.0252 -0.0248 -0.0045 1157 ALA B C   
17456 O O   . ALA B 1159 ? 0.2831 0.2493 0.3311 -0.0240 -0.0268 -0.0067 1157 ALA B O   
17457 C CB  . ALA B 1159 ? 0.2613 0.2321 0.3179 -0.0339 -0.0269 -0.0006 1157 ALA B CB  
17458 N N   . ASP B 1160 ? 0.2564 0.2218 0.3028 -0.0229 -0.0233 -0.0040 1158 ASP B N   
17459 C CA  . ASP B 1160 ? 0.2801 0.2383 0.3200 -0.0193 -0.0240 -0.0060 1158 ASP B CA  
17460 C C   . ASP B 1160 ? 0.2655 0.2281 0.3049 -0.0148 -0.0218 -0.0076 1158 ASP B C   
17461 O O   . ASP B 1160 ? 0.3174 0.2754 0.3519 -0.0114 -0.0221 -0.0094 1158 ASP B O   
17462 C CB  . ASP B 1160 ? 0.2552 0.2066 0.2911 -0.0195 -0.0240 -0.0045 1158 ASP B CB  
17463 C CG  . ASP B 1160 ? 0.2775 0.2223 0.3123 -0.0238 -0.0268 -0.0032 1158 ASP B CG  
17464 O OD1 . ASP B 1160 ? 0.3414 0.2862 0.3779 -0.0262 -0.0290 -0.0040 1158 ASP B OD1 
17465 O OD2 . ASP B 1160 ? 0.3109 0.2505 0.3432 -0.0251 -0.0269 -0.0013 1158 ASP B OD2 
17466 N N   . GLY B 1161 ? 0.2356 0.2070 0.2800 -0.0147 -0.0197 -0.0071 1159 GLY B N   
17467 C CA  . GLY B 1161 ? 0.2733 0.2490 0.3175 -0.0110 -0.0179 -0.0086 1159 GLY B CA  
17468 C C   . GLY B 1161 ? 0.3247 0.3007 0.3684 -0.0100 -0.0194 -0.0110 1159 GLY B C   
17469 O O   . GLY B 1161 ? 0.3395 0.3113 0.3822 -0.0117 -0.0220 -0.0117 1159 GLY B O   
17470 N N   . PRO B 1162 ? 0.3361 0.3170 0.3806 -0.0074 -0.0179 -0.0121 1160 PRO B N   
17471 C CA  . PRO B 1162 ? 0.2807 0.2668 0.3266 -0.0055 -0.0150 -0.0114 1160 PRO B CA  
17472 C C   . PRO B 1162 ? 0.2646 0.2471 0.3061 -0.0028 -0.0142 -0.0117 1160 PRO B C   
17473 O O   . PRO B 1162 ? 0.2813 0.2588 0.3185 -0.0009 -0.0153 -0.0132 1160 PRO B O   
17474 C CB  . PRO B 1162 ? 0.3336 0.3244 0.3807 -0.0039 -0.0145 -0.0130 1160 PRO B CB  
17475 C CG  . PRO B 1162 ? 0.3569 0.3428 0.4005 -0.0032 -0.0168 -0.0150 1160 PRO B CG  
17476 C CD  . PRO B 1162 ? 0.3397 0.3207 0.3831 -0.0061 -0.0191 -0.0143 1160 PRO B CD  
17477 N N   . PHE B 1163 ? 0.2036 0.1887 0.2461 -0.0025 -0.0121 -0.0101 1161 PHE B N   
17478 C CA  . PHE B 1163 ? 0.2054 0.1886 0.2444 0.0003  -0.0111 -0.0102 1161 PHE B CA  
17479 C C   . PHE B 1163 ? 0.2016 0.1906 0.2415 0.0026  -0.0093 -0.0111 1161 PHE B C   
17480 O O   . PHE B 1163 ? 0.2000 0.1939 0.2430 0.0020  -0.0088 -0.0115 1161 PHE B O   
17481 C CB  . PHE B 1163 ? 0.2401 0.2221 0.2791 -0.0010 -0.0103 -0.0078 1161 PHE B CB  
17482 C CG  . PHE B 1163 ? 0.2335 0.2098 0.2718 -0.0039 -0.0122 -0.0067 1161 PHE B CG  
17483 C CD1 . PHE B 1163 ? 0.2808 0.2494 0.3146 -0.0031 -0.0143 -0.0079 1161 PHE B CD1 
17484 C CD2 . PHE B 1163 ? 0.2520 0.2306 0.2939 -0.0075 -0.0118 -0.0046 1161 PHE B CD2 
17485 C CE1 . PHE B 1163 ? 0.2850 0.2477 0.3178 -0.0060 -0.0163 -0.0069 1161 PHE B CE1 
17486 C CE2 . PHE B 1163 ? 0.2593 0.2327 0.3006 -0.0106 -0.0137 -0.0035 1161 PHE B CE2 
17487 C CZ  . PHE B 1163 ? 0.2641 0.2293 0.3008 -0.0100 -0.0161 -0.0046 1161 PHE B CZ  
17488 N N   . ALA B 1164 ? 0.2019 0.1901 0.2388 0.0054  -0.0085 -0.0114 1162 ALA B N   
17489 C CA  . ALA B 1164 ? 0.2349 0.2283 0.2723 0.0075  -0.0069 -0.0122 1162 ALA B CA  
17490 C C   . ALA B 1164 ? 0.2213 0.2164 0.2582 0.0084  -0.0053 -0.0108 1162 ALA B C   
17491 O O   . ALA B 1164 ? 0.2272 0.2258 0.2638 0.0104  -0.0042 -0.0114 1162 ALA B O   
17492 C CB  . ALA B 1164 ? 0.2296 0.2217 0.2641 0.0102  -0.0076 -0.0142 1162 ALA B CB  
17493 N N   . GLY B 1165 ? 0.2002 0.1931 0.2372 0.0069  -0.0052 -0.0089 1163 GLY B N   
17494 C CA  . GLY B 1165 ? 0.2047 0.1989 0.2411 0.0076  -0.0037 -0.0074 1163 GLY B CA  
17495 C C   . GLY B 1165 ? 0.2033 0.1927 0.2385 0.0058  -0.0043 -0.0055 1163 GLY B C   
17496 O O   . GLY B 1165 ? 0.2038 0.1886 0.2384 0.0043  -0.0059 -0.0055 1163 GLY B O   
17497 N N   . ALA B 1166 ? 0.1945 0.1850 0.2291 0.0059  -0.0030 -0.0038 1164 ALA B N   
17498 C CA  . ALA B 1166 ? 0.1836 0.1695 0.2168 0.0042  -0.0034 -0.0016 1164 ALA B CA  
17499 C C   . ALA B 1166 ? 0.2114 0.1967 0.2417 0.0060  -0.0025 -0.0004 1164 ALA B C   
17500 O O   . ALA B 1166 ? 0.2186 0.2089 0.2497 0.0073  -0.0010 -0.0006 1164 ALA B O   
17501 C CB  . ALA B 1166 ? 0.2085 0.1974 0.2454 0.0005  -0.0025 0.0001  1164 ALA B CB  
17502 N N   . LEU B 1167 ? 0.2005 0.1792 0.2274 0.0062  -0.0037 0.0007  1165 LEU B N   
17503 C CA  . LEU B 1167 ? 0.2050 0.1822 0.2288 0.0077  -0.0031 0.0022  1165 LEU B CA  
17504 C C   . LEU B 1167 ? 0.2426 0.2165 0.2660 0.0045  -0.0031 0.0050  1165 LEU B C   
17505 O O   . LEU B 1167 ? 0.2280 0.1965 0.2508 0.0025  -0.0046 0.0055  1165 LEU B O   
17506 C CB  . LEU B 1167 ? 0.2056 0.1774 0.2251 0.0111  -0.0047 0.0013  1165 LEU B CB  
17507 C CG  . LEU B 1167 ? 0.2086 0.1834 0.2284 0.0143  -0.0049 -0.0014 1165 LEU B CG  
17508 C CD1 . LEU B 1167 ? 0.2454 0.2148 0.2609 0.0178  -0.0064 -0.0022 1165 LEU B CD1 
17509 C CD2 . LEU B 1167 ? 0.2425 0.2250 0.2642 0.0154  -0.0031 -0.0017 1165 LEU B CD2 
17510 N N   . VAL B 1168 ? 0.2237 0.2008 0.2473 0.0039  -0.0013 0.0069  1166 VAL B N   
17511 C CA  . VAL B 1168 ? 0.2364 0.2120 0.2601 0.0005  -0.0007 0.0097  1166 VAL B CA  
17512 C C   . VAL B 1168 ? 0.2274 0.2003 0.2470 0.0019  -0.0003 0.0116  1166 VAL B C   
17513 O O   . VAL B 1168 ? 0.2402 0.2166 0.2589 0.0046  0.0006  0.0110  1166 VAL B O   
17514 C CB  . VAL B 1168 ? 0.2302 0.2135 0.2586 -0.0018 0.0015  0.0103  1166 VAL B CB  
17515 C CG1 . VAL B 1168 ? 0.2311 0.2136 0.2598 -0.0055 0.0024  0.0134  1166 VAL B CG1 
17516 C CG2 . VAL B 1168 ? 0.2252 0.2114 0.2576 -0.0028 0.0010  0.0083  1166 VAL B CG2 
17517 N N   . GLU B 1169 ? 0.2361 0.2026 0.2530 0.0000  -0.0012 0.0139  1167 GLU B N   
17518 C CA  . GLU B 1169 ? 0.2506 0.2140 0.2633 0.0008  -0.0010 0.0162  1167 GLU B CA  
17519 C C   . GLU B 1169 ? 0.2482 0.2123 0.2618 -0.0034 0.0004  0.0193  1167 GLU B C   
17520 O O   . GLU B 1169 ? 0.2726 0.2347 0.2881 -0.0069 -0.0003 0.0201  1167 GLU B O   
17521 C CB  . GLU B 1169 ? 0.2523 0.2061 0.2601 0.0024  -0.0035 0.0164  1167 GLU B CB  
17522 C CG  . GLU B 1169 ? 0.2746 0.2241 0.2776 0.0033  -0.0036 0.0189  1167 GLU B CG  
17523 C CD  . GLU B 1169 ? 0.2962 0.2351 0.2941 0.0043  -0.0063 0.0195  1167 GLU B CD  
17524 O OE1 . GLU B 1169 ? 0.2831 0.2175 0.2811 0.0038  -0.0080 0.0180  1167 GLU B OE1 
17525 O OE2 . GLU B 1169 ? 0.3133 0.2479 0.3068 0.0057  -0.0067 0.0214  1167 GLU B OE2 
17526 N N   . GLY B 1170 ? 0.2663 0.2337 0.2789 -0.0032 0.0023  0.0210  1168 GLY B N   
17527 C CA  . GLY B 1170 ? 0.2823 0.2505 0.2953 -0.0071 0.0038  0.0242  1168 GLY B CA  
17528 C C   . GLY B 1170 ? 0.3081 0.2822 0.3206 -0.0063 0.0063  0.0252  1168 GLY B C   
17529 O O   . GLY B 1170 ? 0.2908 0.2685 0.3030 -0.0030 0.0068  0.0234  1168 GLY B O   
17530 N N   . ASP B 1171 ? 0.3206 0.2955 0.3329 -0.0095 0.0079  0.0283  1169 ASP B N   
17531 C CA  . ASP B 1171 ? 0.3349 0.3157 0.3468 -0.0091 0.0105  0.0293  1169 ASP B CA  
17532 C C   . ASP B 1171 ? 0.3077 0.2974 0.3251 -0.0095 0.0125  0.0275  1169 ASP B C   
17533 O O   . ASP B 1171 ? 0.2792 0.2703 0.3007 -0.0103 0.0118  0.0258  1169 ASP B O   
17534 C CB  . ASP B 1171 ? 0.3382 0.3170 0.3475 -0.0121 0.0117  0.0333  1169 ASP B CB  
17535 C CG  . ASP B 1171 ? 0.3432 0.3234 0.3563 -0.0169 0.0125  0.0351  1169 ASP B CG  
17536 O OD1 . ASP B 1171 ? 0.3427 0.3264 0.3609 -0.0180 0.0123  0.0333  1169 ASP B OD1 
17537 O OD2 . ASP B 1171 ? 0.4313 0.4092 0.4422 -0.0199 0.0132  0.0385  1169 ASP B OD2 
17538 N N   . ALA B 1172 ? 0.3019 0.2973 0.3192 -0.0087 0.0150  0.0279  1170 ALA B N   
17539 C CA  . ALA B 1172 ? 0.3034 0.3067 0.3251 -0.0083 0.0168  0.0259  1170 ALA B CA  
17540 C C   . ALA B 1172 ? 0.3096 0.3160 0.3367 -0.0117 0.0174  0.0264  1170 ALA B C   
17541 O O   . ALA B 1172 ? 0.3197 0.3294 0.3509 -0.0113 0.0171  0.0241  1170 ALA B O   
17542 C CB  . ALA B 1172 ? 0.3400 0.3483 0.3600 -0.0073 0.0194  0.0265  1170 ALA B CB  
17543 N N   . GLU B 1173 ? 0.2909 0.2964 0.3180 -0.0152 0.0183  0.0296  1171 GLU B N   
17544 C CA  . GLU B 1173 ? 0.3095 0.3191 0.3421 -0.0186 0.0190  0.0302  1171 GLU B CA  
17545 C C   . GLU B 1173 ? 0.2942 0.2994 0.3289 -0.0198 0.0160  0.0290  1171 GLU B C   
17546 O O   . GLU B 1173 ? 0.2905 0.3000 0.3304 -0.0210 0.0160  0.0279  1171 GLU B O   
17547 C CB  . GLU B 1173 ? 0.4190 0.4301 0.4516 -0.0224 0.0209  0.0340  1171 GLU B CB  
17548 C CG  . GLU B 1173 ? 0.4187 0.4365 0.4507 -0.0213 0.0243  0.0348  1171 GLU B CG  
17549 C CD  . GLU B 1173 ? 0.4514 0.4773 0.4879 -0.0193 0.0259  0.0320  1171 GLU B CD  
17550 O OE1 . GLU B 1173 ? 0.4512 0.4807 0.4932 -0.0208 0.0257  0.0313  1171 GLU B OE1 
17551 O OE2 . GLU B 1173 ? 0.4952 0.5235 0.5294 -0.0161 0.0272  0.0306  1171 GLU B OE2 
17552 N N   . ARG B 1174 ? 0.2941 0.2907 0.3246 -0.0192 0.0135  0.0291  1172 ARG B N   
17553 C CA  . ARG B 1174 ? 0.2833 0.2752 0.3148 -0.0195 0.0106  0.0274  1172 ARG B CA  
17554 C C   . ARG B 1174 ? 0.2496 0.2451 0.2836 -0.0163 0.0102  0.0237  1172 ARG B C   
17555 O O   . ARG B 1174 ? 0.2577 0.2547 0.2955 -0.0173 0.0093  0.0223  1172 ARG B O   
17556 C CB  . ARG B 1174 ? 0.2873 0.2692 0.3132 -0.0186 0.0081  0.0280  1172 ARG B CB  
17557 C CG  . ARG B 1174 ? 0.2836 0.2598 0.3094 -0.0182 0.0051  0.0260  1172 ARG B CG  
17558 C CD  . ARG B 1174 ? 0.3036 0.2799 0.3333 -0.0226 0.0043  0.0268  1172 ARG B CD  
17559 N NE  . ARG B 1174 ? 0.3096 0.2797 0.3385 -0.0223 0.0012  0.0249  1172 ARG B NE  
17560 C CZ  . ARG B 1174 ? 0.2977 0.2682 0.3302 -0.0252 -0.0001 0.0244  1172 ARG B CZ  
17561 N NH1 . ARG B 1174 ? 0.2986 0.2757 0.3362 -0.0288 0.0014  0.0258  1172 ARG B NH1 
17562 N NH2 . ARG B 1174 ? 0.3095 0.2738 0.3404 -0.0243 -0.0029 0.0223  1172 ARG B NH2 
17563 N N   . ILE B 1175 ? 0.2452 0.2420 0.2767 -0.0126 0.0109  0.0223  1173 ILE B N   
17564 C CA  . ILE B 1175 ? 0.2395 0.2397 0.2730 -0.0097 0.0106  0.0189  1173 ILE B CA  
17565 C C   . ILE B 1175 ? 0.2432 0.2510 0.2822 -0.0109 0.0122  0.0182  1173 ILE B C   
17566 O O   . ILE B 1175 ? 0.2320 0.2413 0.2741 -0.0105 0.0112  0.0160  1173 ILE B O   
17567 C CB  . ILE B 1175 ? 0.2508 0.2517 0.2808 -0.0060 0.0112  0.0179  1173 ILE B CB  
17568 C CG1 . ILE B 1175 ? 0.2646 0.2581 0.2898 -0.0041 0.0090  0.0180  1173 ILE B CG1 
17569 C CG2 . ILE B 1175 ? 0.2383 0.2441 0.2707 -0.0037 0.0114  0.0149  1173 ILE B CG2 
17570 C CD1 . ILE B 1175 ? 0.2716 0.2656 0.2931 -0.0010 0.0094  0.0178  1173 ILE B CD1 
17571 N N   . ARG B 1176 ? 0.2675 0.2805 0.3078 -0.0122 0.0148  0.0200  1174 ARG B N   
17572 C CA  . ARG B 1176 ? 0.2499 0.2704 0.2954 -0.0128 0.0165  0.0192  1174 ARG B CA  
17573 C C   . ARG B 1176 ? 0.2315 0.2522 0.2814 -0.0159 0.0152  0.0196  1174 ARG B C   
17574 O O   . ARG B 1176 ? 0.2282 0.2525 0.2820 -0.0155 0.0149  0.0177  1174 ARG B O   
17575 C CB  . ARG B 1176 ? 0.2628 0.2887 0.3086 -0.0136 0.0196  0.0212  1174 ARG B CB  
17576 C CG  . ARG B 1176 ? 0.3058 0.3397 0.3564 -0.0134 0.0215  0.0202  1174 ARG B CG  
17577 C CD  . ARG B 1176 ? 0.3448 0.3843 0.3966 -0.0150 0.0246  0.0226  1174 ARG B CD  
17578 N NE  . ARG B 1176 ? 0.3905 0.4282 0.4369 -0.0140 0.0260  0.0240  1174 ARG B NE  
17579 C CZ  . ARG B 1176 ? 0.4193 0.4594 0.4633 -0.0111 0.0275  0.0228  1174 ARG B CZ  
17580 N NH1 . ARG B 1176 ? 0.3872 0.4314 0.4333 -0.0088 0.0280  0.0201  1174 ARG B NH1 
17581 N NH2 . ARG B 1176 ? 0.4311 0.4692 0.4700 -0.0105 0.0285  0.0243  1174 ARG B NH2 
17582 N N   . ALA B 1177 ? 0.2456 0.2621 0.2946 -0.0192 0.0144  0.0221  1175 ALA B N   
17583 C CA  . ALA B 1177 ? 0.2491 0.2656 0.3022 -0.0225 0.0130  0.0226  1175 ALA B CA  
17584 C C   . ALA B 1177 ? 0.2252 0.2376 0.2783 -0.0213 0.0101  0.0199  1175 ALA B C   
17585 O O   . ALA B 1177 ? 0.2374 0.2528 0.2949 -0.0224 0.0093  0.0188  1175 ALA B O   
17586 C CB  . ALA B 1177 ? 0.2690 0.2806 0.3202 -0.0263 0.0123  0.0259  1175 ALA B CB  
17587 N N   . VAL B 1178 ? 0.2345 0.2402 0.2827 -0.0188 0.0085  0.0187  1176 VAL B N   
17588 C CA  . VAL B 1178 ? 0.2255 0.2273 0.2732 -0.0173 0.0059  0.0161  1176 VAL B CA  
17589 C C   . VAL B 1178 ? 0.2313 0.2387 0.2816 -0.0147 0.0066  0.0134  1176 VAL B C   
17590 O O   . VAL B 1178 ? 0.2378 0.2457 0.2907 -0.0149 0.0051  0.0117  1176 VAL B O   
17591 C CB  . VAL B 1178 ? 0.2696 0.2634 0.3114 -0.0151 0.0043  0.0157  1176 VAL B CB  
17592 C CG1 . VAL B 1178 ? 0.2556 0.2463 0.2966 -0.0128 0.0021  0.0127  1176 VAL B CG1 
17593 C CG2 . VAL B 1178 ? 0.2625 0.2493 0.3014 -0.0179 0.0031  0.0183  1176 VAL B CG2 
17594 N N   . ASN B 1179 ? 0.2165 0.2280 0.2661 -0.0123 0.0087  0.0130  1177 ASN B N   
17595 C CA  . ASN B 1179 ? 0.2271 0.2434 0.2787 -0.0099 0.0093  0.0105  1177 ASN B CA  
17596 C C   . ASN B 1179 ? 0.2337 0.2559 0.2909 -0.0117 0.0099  0.0105  1177 ASN B C   
17597 O O   . ASN B 1179 ? 0.2296 0.2535 0.2891 -0.0108 0.0090  0.0083  1177 ASN B O   
17598 C CB  . ASN B 1179 ? 0.2261 0.2452 0.2755 -0.0075 0.0113  0.0104  1177 ASN B CB  
17599 C CG  . ASN B 1179 ? 0.2648 0.2863 0.3143 -0.0046 0.0113  0.0077  1177 ASN B CG  
17600 O OD1 . ASN B 1179 ? 0.2678 0.2872 0.3175 -0.0037 0.0095  0.0058  1177 ASN B OD1 
17601 N ND2 . ASN B 1179 ? 0.2407 0.2664 0.2898 -0.0031 0.0133  0.0074  1177 ASN B ND2 
17602 N N   . LYS B 1180 ? 0.2189 0.2445 0.2786 -0.0143 0.0115  0.0128  1178 LYS B N   
17603 C CA  . LYS B 1180 ? 0.2431 0.2749 0.3086 -0.0161 0.0120  0.0130  1178 LYS B CA  
17604 C C   . LYS B 1180 ? 0.2004 0.2293 0.2679 -0.0181 0.0092  0.0124  1178 LYS B C   
17605 O O   . LYS B 1180 ? 0.2243 0.2566 0.2953 -0.0177 0.0085  0.0108  1178 LYS B O   
17606 C CB  . LYS B 1180 ? 0.2615 0.2977 0.3292 -0.0187 0.0142  0.0159  1178 LYS B CB  
17607 C CG  . LYS B 1180 ? 0.3184 0.3587 0.3846 -0.0167 0.0173  0.0164  1178 LYS B CG  
17608 C CD  . LYS B 1180 ? 0.3489 0.3943 0.4175 -0.0194 0.0197  0.0194  1178 LYS B CD  
17609 C CE  . LYS B 1180 ? 0.4767 0.5303 0.5516 -0.0199 0.0209  0.0190  1178 LYS B CE  
17610 N NZ  . LYS B 1180 ? 0.4780 0.5359 0.5530 -0.0160 0.0225  0.0168  1178 LYS B NZ  
17611 N N   . ALA B 1181 ? 0.2270 0.2491 0.2918 -0.0201 0.0073  0.0135  1179 ALA B N   
17612 C CA  . ALA B 1181 ? 0.2104 0.2290 0.2765 -0.0220 0.0044  0.0128  1179 ALA B CA  
17613 C C   . ALA B 1181 ? 0.2009 0.2173 0.2656 -0.0190 0.0028  0.0096  1179 ALA B C   
17614 O O   . ALA B 1181 ? 0.2182 0.2358 0.2857 -0.0196 0.0012  0.0083  1179 ALA B O   
17615 C CB  . ALA B 1181 ? 0.2169 0.2275 0.2793 -0.0244 0.0027  0.0145  1179 ALA B CB  
17616 N N   . ILE B 1182 ? 0.2113 0.2250 0.2718 -0.0157 0.0032  0.0084  1180 ILE B N   
17617 C CA  . ILE B 1182 ? 0.2133 0.2253 0.2723 -0.0128 0.0018  0.0055  1180 ILE B CA  
17618 C C   . ILE B 1182 ? 0.2042 0.2230 0.2670 -0.0117 0.0028  0.0041  1180 ILE B C   
17619 O O   . ILE B 1182 ? 0.2206 0.2392 0.2844 -0.0111 0.0013  0.0022  1180 ILE B O   
17620 C CB  . ILE B 1182 ? 0.2116 0.2201 0.2656 -0.0097 0.0021  0.0048  1180 ILE B CB  
17621 C CG1 . ILE B 1182 ? 0.2293 0.2297 0.2791 -0.0104 0.0004  0.0056  1180 ILE B CG1 
17622 C CG2 . ILE B 1182 ? 0.2531 0.2621 0.3063 -0.0068 0.0015  0.0020  1180 ILE B CG2 
17623 C CD1 . ILE B 1182 ? 0.2300 0.2271 0.2750 -0.0074 0.0007  0.0054  1180 ILE B CD1 
17624 N N   . ALA B 1183 ? 0.2245 0.2491 0.2891 -0.0112 0.0054  0.0049  1181 ALA B N   
17625 C CA  . ALA B 1183 ? 0.2296 0.2602 0.2976 -0.0099 0.0063  0.0036  1181 ALA B CA  
17626 C C   . ALA B 1183 ? 0.2483 0.2817 0.3211 -0.0121 0.0052  0.0037  1181 ALA B C   
17627 O O   . ALA B 1183 ? 0.2886 0.3251 0.3636 -0.0108 0.0048  0.0021  1181 ALA B O   
17628 C CB  . ALA B 1183 ? 0.2508 0.2866 0.3195 -0.0090 0.0092  0.0045  1181 ALA B CB  
17629 N N   . ALA B 1184 ? 0.2253 0.2578 0.2998 -0.0154 0.0044  0.0056  1182 ALA B N   
17630 C CA  . ALA B 1184 ? 0.2426 0.2781 0.3219 -0.0178 0.0031  0.0059  1182 ALA B CA  
17631 C C   . ALA B 1184 ? 0.2322 0.2623 0.3102 -0.0185 -0.0002 0.0044  1182 ALA B C   
17632 O O   . ALA B 1184 ? 0.2362 0.2683 0.3179 -0.0205 -0.0017 0.0045  1182 ALA B O   
17633 C CB  . ALA B 1184 ? 0.2593 0.2969 0.3413 -0.0216 0.0038  0.0089  1182 ALA B CB  
17634 N N   . LEU B 1185 ? 0.2168 0.2403 0.2896 -0.0167 -0.0013 0.0031  1183 LEU B N   
17635 C CA  . LEU B 1185 ? 0.2067 0.2250 0.2780 -0.0171 -0.0043 0.0016  1183 LEU B CA  
17636 C C   . LEU B 1185 ? 0.2538 0.2753 0.3270 -0.0154 -0.0049 -0.0005 1183 LEU B C   
17637 O O   . LEU B 1185 ? 0.2721 0.2971 0.3454 -0.0128 -0.0033 -0.0014 1183 LEU B O   
17638 C CB  . LEU B 1185 ? 0.2059 0.2168 0.2710 -0.0151 -0.0050 0.0006  1183 LEU B CB  
17639 C CG  . LEU B 1185 ? 0.2089 0.2151 0.2712 -0.0165 -0.0049 0.0025  1183 LEU B CG  
17640 C CD1 . LEU B 1185 ? 0.2239 0.2239 0.2805 -0.0136 -0.0055 0.0013  1183 LEU B CD1 
17641 C CD2 . LEU B 1185 ? 0.2290 0.2318 0.2923 -0.0204 -0.0070 0.0038  1183 LEU B CD2 
17642 N N   . PRO B 1186 ? 0.2457 0.2658 0.3201 -0.0169 -0.0075 -0.0013 1184 PRO B N   
17643 C CA  . PRO B 1186 ? 0.2294 0.2517 0.3049 -0.0151 -0.0084 -0.0033 1184 PRO B CA  
17644 C C   . PRO B 1186 ? 0.2234 0.2411 0.2938 -0.0122 -0.0088 -0.0054 1184 PRO B C   
17645 O O   . PRO B 1186 ? 0.2819 0.2941 0.3480 -0.0116 -0.0090 -0.0055 1184 PRO B O   
17646 C CB  . PRO B 1186 ? 0.2966 0.3176 0.3741 -0.0179 -0.0113 -0.0033 1184 PRO B CB  
17647 C CG  . PRO B 1186 ? 0.3316 0.3457 0.4057 -0.0199 -0.0125 -0.0025 1184 PRO B CG  
17648 C CD  . PRO B 1186 ? 0.2847 0.3000 0.3586 -0.0201 -0.0099 -0.0005 1184 PRO B CD  
17649 N N   . GLY B 1187 ? 0.2291 0.2491 0.2999 -0.0103 -0.0089 -0.0070 1185 GLY B N   
17650 C CA  . GLY B 1187 ? 0.2366 0.2530 0.3030 -0.0077 -0.0094 -0.0090 1185 GLY B CA  
17651 C C   . GLY B 1187 ? 0.2457 0.2637 0.3103 -0.0052 -0.0071 -0.0091 1185 GLY B C   
17652 O O   . GLY B 1187 ? 0.2569 0.2797 0.3239 -0.0048 -0.0052 -0.0085 1185 GLY B O   
17653 N N   . PRO B 1188 ? 0.2171 0.2311 0.2773 -0.0034 -0.0072 -0.0102 1186 PRO B N   
17654 C CA  . PRO B 1188 ? 0.2225 0.2381 0.2808 -0.0011 -0.0053 -0.0105 1186 PRO B CA  
17655 C C   . PRO B 1188 ? 0.2128 0.2301 0.2718 -0.0014 -0.0033 -0.0088 1186 PRO B C   
17656 O O   . PRO B 1188 ? 0.2260 0.2412 0.2851 -0.0031 -0.0035 -0.0073 1186 PRO B O   
17657 C CB  . PRO B 1188 ? 0.2699 0.2809 0.3236 0.0006  -0.0061 -0.0117 1186 PRO B CB  
17658 C CG  . PRO B 1188 ? 0.2975 0.3035 0.3501 -0.0009 -0.0081 -0.0116 1186 PRO B CG  
17659 C CD  . PRO B 1188 ? 0.2572 0.2651 0.3138 -0.0034 -0.0092 -0.0110 1186 PRO B CD  
17660 N N   . LEU B 1189 ? 0.1956 0.2163 0.2545 0.0001  -0.0015 -0.0089 1187 LEU B N   
17661 C CA  . LEU B 1189 ? 0.1915 0.2134 0.2500 0.0003  0.0005  -0.0075 1187 LEU B CA  
17662 C C   . LEU B 1189 ? 0.1979 0.2158 0.2523 0.0015  0.0003  -0.0075 1187 LEU B C   
17663 O O   . LEU B 1189 ? 0.2434 0.2605 0.2954 0.0034  0.0000  -0.0089 1187 LEU B O   
17664 C CB  . LEU B 1189 ? 0.2024 0.2287 0.2616 0.0017  0.0022  -0.0079 1187 LEU B CB  
17665 C CG  . LEU B 1189 ? 0.2250 0.2560 0.2883 0.0009  0.0031  -0.0074 1187 LEU B CG  
17666 C CD1 . LEU B 1189 ? 0.2741 0.3058 0.3394 0.0008  0.0015  -0.0086 1187 LEU B CD1 
17667 C CD2 . LEU B 1189 ? 0.2393 0.2733 0.3019 0.0025  0.0051  -0.0076 1187 LEU B CD2 
17668 N N   . LEU B 1190 ? 0.1857 0.2010 0.2392 0.0004  0.0004  -0.0060 1188 LEU B N   
17669 C CA  . LEU B 1190 ? 0.2128 0.2237 0.2623 0.0018  -0.0001 -0.0060 1188 LEU B CA  
17670 C C   . LEU B 1190 ? 0.2214 0.2342 0.2691 0.0034  0.0016  -0.0055 1188 LEU B C   
17671 O O   . LEU B 1190 ? 0.1980 0.2137 0.2470 0.0027  0.0032  -0.0042 1188 LEU B O   
17672 C CB  . LEU B 1190 ? 0.2082 0.2144 0.2568 0.0000  -0.0011 -0.0045 1188 LEU B CB  
17673 C CG  . LEU B 1190 ? 0.1900 0.1935 0.2398 -0.0020 -0.0031 -0.0048 1188 LEU B CG  
17674 C CD1 . LEU B 1190 ? 0.2076 0.2051 0.2550 -0.0034 -0.0042 -0.0034 1188 LEU B CD1 
17675 C CD2 . LEU B 1190 ? 0.2248 0.2267 0.2731 -0.0003 -0.0046 -0.0072 1188 LEU B CD2 
17676 N N   . LEU B 1191 ? 0.2077 0.2189 0.2524 0.0057  0.0012  -0.0066 1189 LEU B N   
17677 C CA  . LEU B 1191 ? 0.1825 0.1948 0.2251 0.0073  0.0023  -0.0061 1189 LEU B CA  
17678 C C   . LEU B 1191 ? 0.1795 0.1877 0.2198 0.0070  0.0021  -0.0044 1189 LEU B C   
17679 O O   . LEU B 1191 ? 0.2267 0.2303 0.2647 0.0079  0.0006  -0.0047 1189 LEU B O   
17680 C CB  . LEU B 1191 ? 0.1917 0.2045 0.2323 0.0097  0.0018  -0.0078 1189 LEU B CB  
17681 C CG  . LEU B 1191 ? 0.1897 0.2053 0.2289 0.0112  0.0030  -0.0076 1189 LEU B CG  
17682 C CD1 . LEU B 1191 ? 0.2109 0.2281 0.2492 0.0129  0.0025  -0.0094 1189 LEU B CD1 
17683 C CD2 . LEU B 1191 ? 0.1938 0.2069 0.2304 0.0120  0.0031  -0.0062 1189 LEU B CD2 
17684 N N   . VAL B 1192 ? 0.1986 0.2083 0.2395 0.0059  0.0034  -0.0026 1190 VAL B N   
17685 C CA  . VAL B 1192 ? 0.2033 0.2092 0.2422 0.0050  0.0034  -0.0005 1190 VAL B CA  
17686 C C   . VAL B 1192 ? 0.1995 0.2053 0.2352 0.0071  0.0040  0.0000  1190 VAL B C   
17687 O O   . VAL B 1192 ? 0.2294 0.2394 0.2653 0.0079  0.0053  -0.0002 1190 VAL B O   
17688 C CB  . VAL B 1192 ? 0.1931 0.2011 0.2345 0.0022  0.0046  0.0014  1190 VAL B CB  
17689 C CG1 . VAL B 1192 ? 0.2189 0.2228 0.2580 0.0011  0.0046  0.0038  1190 VAL B CG1 
17690 C CG2 . VAL B 1192 ? 0.2065 0.2154 0.2516 0.0001  0.0039  0.0009  1190 VAL B CG2 
17691 N N   . GLN B 1193 ? 0.1980 0.1987 0.2304 0.0080  0.0029  0.0007  1191 GLN B N   
17692 C CA  . GLN B 1193 ? 0.1914 0.1914 0.2207 0.0099  0.0032  0.0017  1191 GLN B CA  
17693 C C   . GLN B 1193 ? 0.2162 0.2117 0.2435 0.0084  0.0031  0.0042  1191 GLN B C   
17694 O O   . GLN B 1193 ? 0.2325 0.2226 0.2589 0.0075  0.0016  0.0046  1191 GLN B O   
17695 C CB  . GLN B 1193 ? 0.2165 0.2144 0.2433 0.0130  0.0018  0.0003  1191 GLN B CB  
17696 C CG  . GLN B 1193 ? 0.2209 0.2227 0.2494 0.0142  0.0018  -0.0021 1191 GLN B CG  
17697 C CD  . GLN B 1193 ? 0.2348 0.2364 0.2609 0.0174  0.0009  -0.0031 1191 GLN B CD  
17698 O OE1 . GLN B 1193 ? 0.2368 0.2398 0.2613 0.0189  0.0013  -0.0025 1191 GLN B OE1 
17699 N NE2 . GLN B 1193 ? 0.2188 0.2185 0.2447 0.0186  -0.0002 -0.0047 1191 GLN B NE2 
17700 N N   . ALA B 1194 ? 0.2137 0.2111 0.2400 0.0080  0.0045  0.0059  1192 ALA B N   
17701 C CA  . ALA B 1194 ? 0.2249 0.2183 0.2491 0.0064  0.0046  0.0086  1192 ALA B CA  
17702 C C   . ALA B 1194 ? 0.2441 0.2359 0.2642 0.0085  0.0046  0.0097  1192 ALA B C   
17703 O O   . ALA B 1194 ? 0.2754 0.2711 0.2949 0.0106  0.0052  0.0087  1192 ALA B O   
17704 C CB  . ALA B 1194 ? 0.2362 0.2334 0.2631 0.0034  0.0066  0.0101  1192 ALA B CB  
17705 N N   . ALA B 1195 ? 0.2375 0.2233 0.2544 0.0080  0.0037  0.0117  1193 ALA B N   
17706 C CA  . ALA B 1195 ? 0.2705 0.2541 0.2832 0.0100  0.0034  0.0131  1193 ALA B CA  
17707 C C   . ALA B 1195 ? 0.2855 0.2635 0.2957 0.0076  0.0033  0.0161  1193 ALA B C   
17708 O O   . ALA B 1195 ? 0.2799 0.2539 0.2909 0.0053  0.0024  0.0166  1193 ALA B O   
17709 C CB  . ALA B 1195 ? 0.2682 0.2487 0.2785 0.0137  0.0015  0.0116  1193 ALA B CB  
17710 N N   . SER B 1196 ? 0.2866 0.2643 0.2936 0.0080  0.0040  0.0182  1194 SER B N   
17711 C CA  . SER B 1196 ? 0.2843 0.2558 0.2880 0.0061  0.0035  0.0212  1194 SER B CA  
17712 C C   . SER B 1196 ? 0.3114 0.2751 0.3110 0.0088  0.0009  0.0211  1194 SER B C   
17713 O O   . SER B 1196 ? 0.3179 0.2822 0.3170 0.0124  -0.0001 0.0190  1194 SER B O   
17714 C CB  . SER B 1196 ? 0.3278 0.3014 0.3289 0.0059  0.0052  0.0235  1194 SER B CB  
17715 O OG  . SER B 1196 ? 0.3372 0.3111 0.3354 0.0097  0.0044  0.0227  1194 SER B OG  
17716 N N   . SER B 1197 ? 0.2989 0.2552 0.2954 0.0069  -0.0001 0.0236  1195 SER B N   
17717 C CA  . SER B 1197 ? 0.3249 0.2728 0.3167 0.0095  -0.0026 0.0238  1195 SER B CA  
17718 C C   . SER B 1197 ? 0.3330 0.2819 0.3215 0.0135  -0.0028 0.0240  1195 SER B C   
17719 O O   . SER B 1197 ? 0.3329 0.2792 0.3195 0.0175  -0.0046 0.0224  1195 SER B O   
17720 C CB  . SER B 1197 ? 0.3432 0.2830 0.3318 0.0064  -0.0035 0.0268  1195 SER B CB  
17721 O OG  . SER B 1197 ? 0.3365 0.2755 0.3283 0.0025  -0.0035 0.0267  1195 SER B OG  
17722 N N   . GLY B 1198 ? 0.3243 0.2770 0.3120 0.0127  -0.0011 0.0258  1196 GLY B N   
17723 C CA  . GLY B 1198 ? 0.3903 0.3443 0.3748 0.0162  -0.0015 0.0260  1196 GLY B CA  
17724 C C   . GLY B 1198 ? 0.3865 0.3472 0.3738 0.0194  -0.0015 0.0228  1196 GLY B C   
17725 O O   . GLY B 1198 ? 0.3755 0.3357 0.3607 0.0233  -0.0029 0.0221  1196 GLY B O   
17726 N N   . GLU B 1199 ? 0.3469 0.3140 0.3390 0.0178  0.0000  0.0210  1197 GLU B N   
17727 C CA  . GLU B 1199 ? 0.3784 0.3516 0.3732 0.0203  0.0001  0.0180  1197 GLU B CA  
17728 C C   . GLU B 1199 ? 0.3543 0.3244 0.3492 0.0231  -0.0020 0.0160  1197 GLU B C   
17729 O O   . GLU B 1199 ? 0.3639 0.3366 0.3585 0.0266  -0.0028 0.0146  1197 GLU B O   
17730 C CB  . GLU B 1199 ? 0.3972 0.3766 0.3968 0.0177  0.0020  0.0167  1197 GLU B CB  
17731 C CG  . GLU B 1199 ? 0.4595 0.4458 0.4620 0.0195  0.0023  0.0140  1197 GLU B CG  
17732 C CD  . GLU B 1199 ? 0.4684 0.4599 0.4751 0.0169  0.0042  0.0129  1197 GLU B CD  
17733 O OE1 . GLU B 1199 ? 0.4744 0.4651 0.4819 0.0138  0.0054  0.0145  1197 GLU B OE1 
17734 O OE2 . GLU B 1199 ? 0.5594 0.5557 0.5686 0.0178  0.0044  0.0106  1197 GLU B OE2 
17735 N N   . ILE B 1200 ? 0.3140 0.2785 0.3091 0.0216  -0.0028 0.0160  1198 ILE B N   
17736 C CA  . ILE B 1200 ? 0.3039 0.2645 0.2983 0.0244  -0.0047 0.0141  1198 ILE B CA  
17737 C C   . ILE B 1200 ? 0.3736 0.3298 0.3634 0.0284  -0.0065 0.0149  1198 ILE B C   
17738 O O   . ILE B 1200 ? 0.3623 0.3196 0.3520 0.0322  -0.0075 0.0129  1198 ILE B O   
17739 C CB  . ILE B 1200 ? 0.2967 0.2510 0.2912 0.0218  -0.0055 0.0142  1198 ILE B CB  
17740 C CG1 . ILE B 1200 ? 0.3200 0.2797 0.3197 0.0185  -0.0041 0.0130  1198 ILE B CG1 
17741 C CG2 . ILE B 1200 ? 0.2962 0.2449 0.2887 0.0250  -0.0077 0.0125  1198 ILE B CG2 
17742 C CD1 . ILE B 1200 ? 0.3078 0.2620 0.3080 0.0153  -0.0049 0.0135  1198 ILE B CD1 
17743 N N   . ALA B 1201 ? 0.3739 0.3252 0.3598 0.0276  -0.0068 0.0178  1199 ALA B N   
17744 C CA  . ALA B 1201 ? 0.4160 0.3626 0.3973 0.0315  -0.0086 0.0187  1199 ALA B CA  
17745 C C   . ALA B 1201 ? 0.3963 0.3499 0.3778 0.0347  -0.0083 0.0181  1199 ALA B C   
17746 O O   . ALA B 1201 ? 0.4594 0.4119 0.4389 0.0390  -0.0099 0.0175  1199 ALA B O   
17747 C CB  . ALA B 1201 ? 0.4016 0.3407 0.3782 0.0296  -0.0091 0.0222  1199 ALA B CB  
17748 N N   . ARG B 1202 ? 0.3944 0.3552 0.3784 0.0326  -0.0064 0.0183  1200 ARG B N   
17749 C CA  . ARG B 1202 ? 0.4121 0.3793 0.3959 0.0349  -0.0063 0.0181  1200 ARG B CA  
17750 C C   . ARG B 1202 ? 0.4410 0.4158 0.4290 0.0365  -0.0060 0.0150  1200 ARG B C   
17751 O O   . ARG B 1202 ? 0.4553 0.4340 0.4429 0.0397  -0.0068 0.0144  1200 ARG B O   
17752 C CB  . ARG B 1202 ? 0.4377 0.4083 0.4213 0.0319  -0.0044 0.0198  1200 ARG B CB  
17753 C CG  . ARG B 1202 ? 0.5447 0.5089 0.5239 0.0302  -0.0044 0.0232  1200 ARG B CG  
17754 C CD  . ARG B 1202 ? 0.5623 0.5309 0.5410 0.0278  -0.0024 0.0247  1200 ARG B CD  
17755 N NE  . ARG B 1202 ? 0.5257 0.5005 0.5091 0.0252  -0.0004 0.0230  1200 ARG B NE  
17756 C CZ  . ARG B 1202 ? 0.5459 0.5204 0.5309 0.0214  0.0013  0.0239  1200 ARG B CZ  
17757 N NH1 . ARG B 1202 ? 0.5327 0.5011 0.5152 0.0193  0.0013  0.0266  1200 ARG B NH1 
17758 N NH2 . ARG B 1202 ? 0.5177 0.4982 0.5071 0.0197  0.0030  0.0221  1200 ARG B NH2 
17759 N N   . ASN B 1203 ? 0.3859 0.3631 0.3778 0.0344  -0.0050 0.0133  1201 ASN B N   
17760 C CA  . ASN B 1203 ? 0.3705 0.3554 0.3664 0.0350  -0.0043 0.0107  1201 ASN B CA  
17761 C C   . ASN B 1203 ? 0.3835 0.3670 0.3810 0.0364  -0.0051 0.0085  1201 ASN B C   
17762 O O   . ASN B 1203 ? 0.3432 0.3238 0.3421 0.0341  -0.0048 0.0081  1201 ASN B O   
17763 C CB  . ASN B 1203 ? 0.3955 0.3848 0.3943 0.0312  -0.0023 0.0105  1201 ASN B CB  
17764 C CG  . ASN B 1203 ? 0.4099 0.4066 0.4125 0.0315  -0.0017 0.0079  1201 ASN B CG  
17765 O OD1 . ASN B 1203 ? 0.4354 0.4347 0.4385 0.0343  -0.0027 0.0065  1201 ASN B OD1 
17766 N ND2 . ASN B 1203 ? 0.4417 0.4416 0.4468 0.0285  0.0000  0.0075  1201 ASN B ND2 
17767 N N   . PRO B 1204 ? 0.3896 0.3756 0.3872 0.0402  -0.0062 0.0071  1202 PRO B N   
17768 C CA  . PRO B 1204 ? 0.3991 0.3845 0.3982 0.0418  -0.0068 0.0048  1202 PRO B CA  
17769 C C   . PRO B 1204 ? 0.3748 0.3645 0.3780 0.0391  -0.0054 0.0031  1202 PRO B C   
17770 O O   . PRO B 1204 ? 0.3808 0.3683 0.3849 0.0392  -0.0058 0.0016  1202 PRO B O   
17771 C CB  . PRO B 1204 ? 0.4265 0.4164 0.4257 0.0462  -0.0077 0.0038  1202 PRO B CB  
17772 C CG  . PRO B 1204 ? 0.4403 0.4301 0.4368 0.0474  -0.0083 0.0059  1202 PRO B CG  
17773 C CD  . PRO B 1204 ? 0.4058 0.3958 0.4023 0.0432  -0.0070 0.0075  1202 PRO B CD  
17774 N N   . ASP B 1205 ? 0.3619 0.3574 0.3674 0.0368  -0.0041 0.0031  1203 ASP B N   
17775 C CA  . ASP B 1205 ? 0.3754 0.3750 0.3846 0.0343  -0.0029 0.0015  1203 ASP B CA  
17776 C C   . ASP B 1205 ? 0.3814 0.3791 0.3914 0.0304  -0.0017 0.0026  1203 ASP B C   
17777 O O   . ASP B 1205 ? 0.3483 0.3504 0.3610 0.0282  -0.0004 0.0019  1203 ASP B O   
17778 C CB  . ASP B 1205 ? 0.4184 0.4260 0.4297 0.0347  -0.0023 0.0004  1203 ASP B CB  
17779 C CG  . ASP B 1205 ? 0.4438 0.4545 0.4554 0.0382  -0.0033 -0.0009 1203 ASP B CG  
17780 O OD1 . ASP B 1205 ? 0.4138 0.4209 0.4245 0.0403  -0.0042 -0.0016 1203 ASP B OD1 
17781 O OD2 . ASP B 1205 ? 0.5057 0.5227 0.5185 0.0388  -0.0032 -0.0014 1203 ASP B OD2 
17782 N N   . ALA B 1206 ? 0.3227 0.3140 0.3302 0.0295  -0.0020 0.0045  1204 ALA B N   
17783 C CA  . ALA B 1206 ? 0.3145 0.3044 0.3231 0.0257  -0.0009 0.0057  1204 ALA B CA  
17784 C C   . ALA B 1206 ? 0.3034 0.2948 0.3156 0.0238  -0.0004 0.0040  1204 ALA B C   
17785 O O   . ALA B 1206 ? 0.3300 0.3247 0.3446 0.0211  0.0010  0.0041  1204 ALA B O   
17786 C CB  . ALA B 1206 ? 0.3190 0.3012 0.3244 0.0249  -0.0017 0.0079  1204 ALA B CB  
17787 N N   . TYR B 1207 ? 0.2669 0.2560 0.2791 0.0253  -0.0016 0.0024  1205 TYR B N   
17788 C CA  . TYR B 1207 ? 0.2643 0.2552 0.2796 0.0240  -0.0014 0.0005  1205 TYR B CA  
17789 C C   . TYR B 1207 ? 0.2598 0.2556 0.2762 0.0265  -0.0016 -0.0016 1205 TYR B C   
17790 O O   . TYR B 1207 ? 0.3410 0.3359 0.3555 0.0297  -0.0025 -0.0021 1205 TYR B O   
17791 C CB  . TYR B 1207 ? 0.2635 0.2478 0.2779 0.0235  -0.0028 0.0002  1205 TYR B CB  
17792 C CG  . TYR B 1207 ? 0.2360 0.2155 0.2495 0.0205  -0.0028 0.0024  1205 TYR B CG  
17793 C CD1 . TYR B 1207 ? 0.2363 0.2187 0.2527 0.0170  -0.0014 0.0032  1205 TYR B CD1 
17794 C CD2 . TYR B 1207 ? 0.2490 0.2208 0.2587 0.0212  -0.0042 0.0037  1205 TYR B CD2 
17795 C CE1 . TYR B 1207 ? 0.2351 0.2139 0.2511 0.0141  -0.0013 0.0054  1205 TYR B CE1 
17796 C CE2 . TYR B 1207 ? 0.2763 0.2437 0.2853 0.0180  -0.0043 0.0059  1205 TYR B CE2 
17797 C CZ  . TYR B 1207 ? 0.2694 0.2406 0.2816 0.0144  -0.0027 0.0068  1205 TYR B CZ  
17798 O OH  . TYR B 1207 ? 0.2577 0.2252 0.2694 0.0111  -0.0027 0.0092  1205 TYR B OH  
17799 N N   . CYS B 1208 ? 0.2087 0.2097 0.2282 0.0250  -0.0006 -0.0028 1206 CYS B N   
17800 C CA  . CYS B 1208 ? 0.2186 0.2250 0.2393 0.0267  -0.0005 -0.0045 1206 CYS B CA  
17801 C C   . CYS B 1208 ? 0.1877 0.1930 0.2092 0.0272  -0.0011 -0.0064 1206 CYS B C   
17802 O O   . CYS B 1208 ? 0.2063 0.2105 0.2295 0.0249  -0.0009 -0.0068 1206 CYS B O   
17803 C CB  . CYS B 1208 ? 0.2413 0.2532 0.2642 0.0248  0.0009  -0.0047 1206 CYS B CB  
17804 S SG  . CYS B 1208 ? 0.2689 0.2874 0.2933 0.0261  0.0009  -0.0066 1206 CYS B SG  
17805 N N   . LEU B 1209 ? 0.1891 0.1952 0.2097 0.0302  -0.0018 -0.0075 1207 LEU B N   
17806 C CA  . LEU B 1209 ? 0.1931 0.1981 0.2139 0.0310  -0.0024 -0.0093 1207 LEU B CA  
17807 C C   . LEU B 1209 ? 0.1841 0.1946 0.2077 0.0296  -0.0016 -0.0106 1207 LEU B C   
17808 O O   . LEU B 1209 ? 0.1878 0.1973 0.2117 0.0294  -0.0019 -0.0120 1207 LEU B O   
17809 C CB  . LEU B 1209 ? 0.1883 0.1926 0.2069 0.0350  -0.0032 -0.0101 1207 LEU B CB  
17810 C CG  . LEU B 1209 ? 0.2185 0.2170 0.2339 0.0370  -0.0043 -0.0089 1207 LEU B CG  
17811 C CD1 . LEU B 1209 ? 0.2492 0.2476 0.2627 0.0413  -0.0050 -0.0100 1207 LEU B CD1 
17812 C CD2 . LEU B 1209 ? 0.2498 0.2406 0.2637 0.0350  -0.0050 -0.0082 1207 LEU B CD2 
17813 N N   . ASN B 1210 ? 0.1897 0.2054 0.2149 0.0285  -0.0006 -0.0103 1208 ASN B N   
17814 C CA  . ASN B 1210 ? 0.2103 0.2305 0.2377 0.0270  0.0000  -0.0114 1208 ASN B CA  
17815 C C   . ASN B 1210 ? 0.1827 0.2005 0.2115 0.0245  0.0001  -0.0117 1208 ASN B C   
17816 O O   . ASN B 1210 ? 0.2134 0.2329 0.2434 0.0238  0.0002  -0.0129 1208 ASN B O   
17817 C CB  . ASN B 1210 ? 0.2485 0.2734 0.2768 0.0259  0.0008  -0.0108 1208 ASN B CB  
17818 C CG  . ASN B 1210 ? 0.2475 0.2759 0.2749 0.0282  0.0006  -0.0105 1208 ASN B CG  
17819 O OD1 . ASN B 1210 ? 0.3073 0.3343 0.3332 0.0308  -0.0001 -0.0105 1208 ASN B OD1 
17820 N ND2 . ASN B 1210 ? 0.3132 0.3459 0.3412 0.0272  0.0010  -0.0103 1208 ASN B ND2 
17821 N N   . TRP B 1211 ? 0.1852 0.1992 0.2138 0.0230  0.0001  -0.0104 1209 TRP B N   
17822 C CA  . TRP B 1211 ? 0.1784 0.1911 0.2089 0.0204  0.0003  -0.0105 1209 TRP B CA  
17823 C C   . TRP B 1211 ? 0.2036 0.2113 0.2333 0.0204  -0.0010 -0.0111 1209 TRP B C   
17824 O O   . TRP B 1211 ? 0.2176 0.2241 0.2488 0.0183  -0.0012 -0.0112 1209 TRP B O   
17825 C CB  . TRP B 1211 ? 0.2001 0.2124 0.2314 0.0184  0.0011  -0.0088 1209 TRP B CB  
17826 C CG  . TRP B 1211 ? 0.2139 0.2298 0.2448 0.0189  0.0020  -0.0081 1209 TRP B CG  
17827 C CD1 . TRP B 1211 ? 0.2375 0.2525 0.2669 0.0190  0.0024  -0.0065 1209 TRP B CD1 
17828 C CD2 . TRP B 1211 ? 0.1969 0.2177 0.2286 0.0191  0.0026  -0.0091 1209 TRP B CD2 
17829 N NE1 . TRP B 1211 ? 0.2560 0.2752 0.2852 0.0194  0.0032  -0.0065 1209 TRP B NE1 
17830 C CE2 . TRP B 1211 ? 0.2220 0.2446 0.2525 0.0194  0.0032  -0.0080 1209 TRP B CE2 
17831 C CE3 . TRP B 1211 ? 0.2034 0.2270 0.2363 0.0189  0.0025  -0.0106 1209 TRP B CE3 
17832 C CZ2 . TRP B 1211 ? 0.2313 0.2583 0.2620 0.0195  0.0036  -0.0086 1209 TRP B CZ2 
17833 C CZ3 . TRP B 1211 ? 0.2244 0.2523 0.2576 0.0189  0.0030  -0.0110 1209 TRP B CZ3 
17834 C CH2 . TRP B 1211 ? 0.2123 0.2417 0.2443 0.0191  0.0035  -0.0101 1209 TRP B CH2 
17835 N N   . LEU B 1212 ? 0.1931 0.1977 0.2202 0.0229  -0.0019 -0.0114 1210 LEU B N   
17836 C CA  . LEU B 1212 ? 0.1703 0.1692 0.1958 0.0231  -0.0032 -0.0120 1210 LEU B CA  
17837 C C   . LEU B 1212 ? 0.1876 0.1873 0.2125 0.0247  -0.0037 -0.0141 1210 LEU B C   
17838 O O   . LEU B 1212 ? 0.1829 0.1778 0.2059 0.0254  -0.0048 -0.0149 1210 LEU B O   
17839 C CB  . LEU B 1212 ? 0.1754 0.1690 0.1977 0.0249  -0.0040 -0.0111 1210 LEU B CB  
17840 C CG  . LEU B 1212 ? 0.1661 0.1573 0.1887 0.0226  -0.0038 -0.0089 1210 LEU B CG  
17841 C CD1 . LEU B 1212 ? 0.2168 0.2038 0.2361 0.0246  -0.0044 -0.0077 1210 LEU B CD1 
17842 C CD2 . LEU B 1212 ? 0.2052 0.1924 0.2286 0.0197  -0.0045 -0.0086 1210 LEU B CD2 
17843 N N   . VAL B 1213 ? 0.1811 0.1867 0.2074 0.0252  -0.0028 -0.0149 1211 VAL B N   
17844 C CA  . VAL B 1213 ? 0.1732 0.1804 0.1992 0.0262  -0.0029 -0.0166 1211 VAL B CA  
17845 C C   . VAL B 1213 ? 0.1704 0.1808 0.1990 0.0236  -0.0024 -0.0169 1211 VAL B C   
17846 O O   . VAL B 1213 ? 0.1942 0.2070 0.2248 0.0217  -0.0017 -0.0159 1211 VAL B O   
17847 C CB  . VAL B 1213 ? 0.1777 0.1893 0.2029 0.0290  -0.0024 -0.0172 1211 VAL B CB  
17848 C CG1 . VAL B 1213 ? 0.2165 0.2245 0.2389 0.0322  -0.0031 -0.0172 1211 VAL B CG1 
17849 C CG2 . VAL B 1213 ? 0.1927 0.2099 0.2198 0.0282  -0.0013 -0.0163 1211 VAL B CG2 
17850 N N   . GLU B 1214 ? 0.1840 0.1942 0.2123 0.0235  -0.0029 -0.0182 1212 GLU B N   
17851 C CA  . GLU B 1214 ? 0.1968 0.2100 0.2272 0.0214  -0.0026 -0.0186 1212 GLU B CA  
17852 C C   . GLU B 1214 ? 0.1621 0.1801 0.1922 0.0225  -0.0019 -0.0195 1212 GLU B C   
17853 O O   . GLU B 1214 ? 0.1843 0.2022 0.2125 0.0246  -0.0021 -0.0205 1212 GLU B O   
17854 C CB  . GLU B 1214 ? 0.2106 0.2202 0.2407 0.0202  -0.0038 -0.0194 1212 GLU B CB  
17855 C CG  . GLU B 1214 ? 0.2853 0.2976 0.3176 0.0182  -0.0036 -0.0197 1212 GLU B CG  
17856 C CD  . GLU B 1214 ? 0.3098 0.3191 0.3416 0.0172  -0.0049 -0.0206 1212 GLU B CD  
17857 O OE1 . GLU B 1214 ? 0.2969 0.3015 0.3274 0.0173  -0.0061 -0.0208 1212 GLU B OE1 
17858 O OE2 . GLU B 1214 ? 0.3233 0.3348 0.3559 0.0163  -0.0049 -0.0211 1212 GLU B OE2 
17859 N N   . GLU B 1215 ? 0.1671 0.1892 0.1990 0.0210  -0.0011 -0.0191 1213 GLU B N   
17860 C CA  . GLU B 1215 ? 0.1650 0.1917 0.1970 0.0213  -0.0005 -0.0197 1213 GLU B CA  
17861 C C   . GLU B 1215 ? 0.1494 0.1755 0.1812 0.0202  -0.0010 -0.0206 1213 GLU B C   
17862 O O   . GLU B 1215 ? 0.1700 0.1941 0.2029 0.0184  -0.0014 -0.0204 1213 GLU B O   
17863 C CB  . GLU B 1215 ? 0.1828 0.2131 0.2164 0.0198  0.0002  -0.0189 1213 GLU B CB  
17864 C CG  . GLU B 1215 ? 0.2017 0.2329 0.2353 0.0207  0.0007  -0.0179 1213 GLU B CG  
17865 C CD  . GLU B 1215 ? 0.1656 0.1992 0.2004 0.0190  0.0012  -0.0172 1213 GLU B CD  
17866 O OE1 . GLU B 1215 ? 0.1701 0.2018 0.2059 0.0176  0.0013  -0.0167 1213 GLU B OE1 
17867 O OE2 . GLU B 1215 ? 0.1810 0.2186 0.2158 0.0189  0.0016  -0.0172 1213 GLU B OE2 
17868 N N   . VAL B 1216 ? 0.1668 0.1948 0.1972 0.0213  -0.0008 -0.0215 1214 VAL B N   
17869 C CA  . VAL B 1216 ? 0.1753 0.2033 0.2051 0.0203  -0.0012 -0.0222 1214 VAL B CA  
17870 C C   . VAL B 1216 ? 0.1574 0.1906 0.1871 0.0200  -0.0003 -0.0222 1214 VAL B C   
17871 O O   . VAL B 1216 ? 0.1709 0.2072 0.2000 0.0218  0.0004  -0.0223 1214 VAL B O   
17872 C CB  . VAL B 1216 ? 0.1874 0.2118 0.2148 0.0217  -0.0020 -0.0234 1214 VAL B CB  
17873 C CG1 . VAL B 1216 ? 0.1954 0.2203 0.2219 0.0206  -0.0023 -0.0241 1214 VAL B CG1 
17874 C CG2 . VAL B 1216 ? 0.2236 0.2426 0.2511 0.0213  -0.0031 -0.0233 1214 VAL B CG2 
17875 N N   . SER B 1217 ? 0.1491 0.1833 0.1796 0.0179  -0.0003 -0.0220 1215 SER B N   
17876 C CA  . SER B 1217 ? 0.1527 0.1911 0.1828 0.0170  0.0003  -0.0219 1215 SER B CA  
17877 C C   . SER B 1217 ? 0.1442 0.1816 0.1726 0.0166  -0.0001 -0.0226 1215 SER B C   
17878 O O   . SER B 1217 ? 0.1661 0.1998 0.1943 0.0158  -0.0010 -0.0229 1215 SER B O   
17879 C CB  . SER B 1217 ? 0.1785 0.2178 0.2101 0.0148  0.0003  -0.0211 1215 SER B CB  
17880 O OG  . SER B 1217 ? 0.2007 0.2423 0.2315 0.0132  0.0005  -0.0210 1215 SER B OG  
17881 N N   . ALA B 1218 ? 0.1539 0.1948 0.1809 0.0172  0.0006  -0.0228 1216 ALA B N   
17882 C CA  . ALA B 1218 ? 0.1811 0.2216 0.2061 0.0168  0.0004  -0.0234 1216 ALA B CA  
17883 C C   . ALA B 1218 ? 0.1699 0.2151 0.1947 0.0152  0.0012  -0.0227 1216 ALA B C   
17884 O O   . ALA B 1218 ? 0.1812 0.2311 0.2066 0.0159  0.0022  -0.0224 1216 ALA B O   
17885 C CB  . ALA B 1218 ? 0.1997 0.2393 0.2224 0.0194  0.0005  -0.0245 1216 ALA B CB  
17886 N N   . SER B 1219 ? 0.1587 0.2026 0.1828 0.0130  0.0007  -0.0224 1217 SER B N   
17887 C CA  . SER B 1219 ? 0.1596 0.2071 0.1831 0.0111  0.0012  -0.0216 1217 SER B CA  
17888 C C   . SER B 1219 ? 0.1582 0.2054 0.1789 0.0109  0.0012  -0.0219 1217 SER B C   
17889 O O   . SER B 1219 ? 0.1668 0.2098 0.1863 0.0103  0.0001  -0.0222 1217 SER B O   
17890 C CB  . SER B 1219 ? 0.1791 0.2250 0.2035 0.0086  0.0005  -0.0208 1217 SER B CB  
17891 O OG  . SER B 1219 ? 0.1915 0.2402 0.2149 0.0064  0.0009  -0.0200 1217 SER B OG  
17892 N N   . ILE B 1220 ? 0.1653 0.2173 0.1850 0.0114  0.0024  -0.0218 1218 ILE B N   
17893 C CA  . ILE B 1220 ? 0.1675 0.2199 0.1842 0.0116  0.0028  -0.0222 1218 ILE B CA  
17894 C C   . ILE B 1220 ? 0.1855 0.2415 0.2015 0.0088  0.0033  -0.0209 1218 ILE B C   
17895 O O   . ILE B 1220 ? 0.1803 0.2418 0.1979 0.0082  0.0043  -0.0201 1218 ILE B O   
17896 C CB  . ILE B 1220 ? 0.2119 0.2671 0.2276 0.0147  0.0039  -0.0231 1218 ILE B CB  
17897 C CG1 . ILE B 1220 ? 0.2530 0.3041 0.2692 0.0173  0.0032  -0.0242 1218 ILE B CG1 
17898 C CG2 . ILE B 1220 ? 0.2354 0.2910 0.2476 0.0150  0.0043  -0.0235 1218 ILE B CG2 
17899 C CD1 . ILE B 1220 ? 0.3750 0.4289 0.3908 0.0207  0.0042  -0.0251 1218 ILE B CD1 
17900 N N   . ASN B 1221 ? 0.1837 0.2367 0.1975 0.0069  0.0026  -0.0205 1219 ASN B N   
17901 C CA  . ASN B 1221 ? 0.1780 0.2336 0.1904 0.0041  0.0030  -0.0192 1219 ASN B CA  
17902 C C   . ASN B 1221 ? 0.2054 0.2657 0.2157 0.0051  0.0045  -0.0193 1219 ASN B C   
17903 O O   . ASN B 1221 ? 0.2315 0.2895 0.2389 0.0061  0.0044  -0.0199 1219 ASN B O   
17904 C CB  . ASN B 1221 ? 0.1956 0.2457 0.2059 0.0022  0.0015  -0.0188 1219 ASN B CB  
17905 C CG  . ASN B 1221 ? 0.2061 0.2579 0.2142 -0.0008 0.0017  -0.0173 1219 ASN B CG  
17906 O OD1 . ASN B 1221 ? 0.2045 0.2619 0.2130 -0.0019 0.0031  -0.0165 1219 ASN B OD1 
17907 N ND2 . ASN B 1221 ? 0.2499 0.2967 0.2555 -0.0022 0.0004  -0.0169 1219 ASN B ND2 
17908 N N   . THR B 1222 ? 0.1800 0.2471 0.1917 0.0048  0.0060  -0.0186 1220 THR B N   
17909 C CA  . THR B 1222 ? 0.2179 0.2906 0.2281 0.0060  0.0078  -0.0186 1220 THR B CA  
17910 C C   . THR B 1222 ? 0.2811 0.3565 0.2892 0.0027  0.0083  -0.0170 1220 THR B C   
17911 O O   . THR B 1222 ? 0.3107 0.3919 0.3177 0.0031  0.0101  -0.0167 1220 THR B O   
17912 C CB  . THR B 1222 ? 0.2239 0.3035 0.2372 0.0079  0.0091  -0.0187 1220 THR B CB  
17913 O OG1 . THR B 1222 ? 0.2489 0.3316 0.2649 0.0050  0.0089  -0.0173 1220 THR B OG1 
17914 C CG2 . THR B 1222 ? 0.2379 0.3143 0.2524 0.0115  0.0086  -0.0202 1220 THR B CG2 
17915 N N   . ALA B 1223 ? 0.2315 0.3029 0.2389 -0.0006 0.0070  -0.0160 1221 ALA B N   
17916 C CA  . ALA B 1223 ? 0.2845 0.3565 0.2892 -0.0040 0.0071  -0.0144 1221 ALA B CA  
17917 C C   . ALA B 1223 ? 0.3859 0.4515 0.3866 -0.0039 0.0061  -0.0148 1221 ALA B C   
17918 O O   . ALA B 1223 ? 0.4255 0.4903 0.4233 -0.0066 0.0059  -0.0134 1221 ALA B O   
17919 C CB  . ALA B 1223 ? 0.3187 0.3897 0.3245 -0.0078 0.0061  -0.0129 1221 ALA B CB  
17920 N N   . ALA B 1224 ? 0.3610 0.4221 0.3614 -0.0009 0.0052  -0.0165 1222 ALA B N   
17921 C CA  . ALA B 1224 ? 0.4204 0.4749 0.4176 -0.0010 0.0036  -0.0168 1222 ALA B CA  
17922 C C   . ALA B 1224 ? 0.4664 0.5220 0.4591 -0.0011 0.0044  -0.0165 1222 ALA B C   
17923 O O   . ALA B 1224 ? 0.4335 0.4842 0.4230 -0.0021 0.0031  -0.0162 1222 ALA B O   
17924 C CB  . ALA B 1224 ? 0.3847 0.4344 0.3829 0.0020  0.0024  -0.0187 1222 ALA B CB  
17925 N N   . ALA B 1225 ? 0.4086 0.4707 0.4009 0.0001  0.0066  -0.0166 1223 ALA B N   
17926 C CA  . ALA B 1225 ? 0.4577 0.5216 0.4456 0.0001  0.0077  -0.0163 1223 ALA B CA  
17927 C C   . ALA B 1225 ? 0.5500 0.6167 0.5363 -0.0040 0.0084  -0.0139 1223 ALA B C   
17928 O O   . ALA B 1225 ? 0.5139 0.5822 0.4962 -0.0046 0.0094  -0.0133 1223 ALA B O   
17929 C CB  . ALA B 1225 ? 0.4710 0.5409 0.4588 0.0034  0.0100  -0.0175 1223 ALA B CB  
17930 N N   . GLY B 1226 ? 0.5133 0.5802 0.5021 -0.0070 0.0077  -0.0125 1224 GLY B N   
17931 C CA  . GLY B 1226 ? 0.5124 0.5809 0.4995 -0.0114 0.0080  -0.0101 1224 GLY B CA  
17932 C C   . GLY B 1226 ? 0.5472 0.6236 0.5376 -0.0134 0.0095  -0.0088 1224 GLY B C   
17933 O O   . GLY B 1226 ? 0.5027 0.5806 0.4919 -0.0174 0.0097  -0.0067 1224 GLY B O   
17934 N N   . GLY B 1227 ? 0.4639 0.5451 0.4583 -0.0109 0.0105  -0.0099 1225 GLY B N   
17935 C CA  . GLY B 1227 ? 0.4661 0.5552 0.4640 -0.0127 0.0118  -0.0087 1225 GLY B CA  
17936 C C   . GLY B 1227 ? 0.4980 0.5906 0.5002 -0.0092 0.0123  -0.0103 1225 GLY B C   
17937 O O   . GLY B 1227 ? 0.4521 0.5407 0.4543 -0.0055 0.0118  -0.0123 1225 GLY B O   
17938 N N   . ASN B 1228 ? 0.4118 0.5120 0.4175 -0.0104 0.0133  -0.0094 1226 ASN B N   
17939 C CA  . ASN B 1228 ? 0.4936 0.5976 0.5034 -0.0074 0.0137  -0.0105 1226 ASN B CA  
17940 C C   . ASN B 1228 ? 0.5590 0.6728 0.5700 -0.0052 0.0162  -0.0105 1226 ASN B C   
17941 O O   . ASN B 1228 ? 0.6320 0.7531 0.6435 -0.0079 0.0175  -0.0088 1226 ASN B O   
17942 C CB  . ASN B 1228 ? 0.5256 0.6305 0.5387 -0.0103 0.0126  -0.0095 1226 ASN B CB  
17943 C CG  . ASN B 1228 ? 0.5392 0.6454 0.5561 -0.0071 0.0123  -0.0108 1226 ASN B CG  
17944 O OD1 . ASN B 1228 ? 0.5763 0.6857 0.5941 -0.0030 0.0135  -0.0121 1226 ASN B OD1 
17945 N ND2 . ASN B 1228 ? 0.4495 0.5528 0.4681 -0.0090 0.0108  -0.0105 1226 ASN B ND2 
17946 N N   . ALA B 1229 ? 0.5604 0.6745 0.5720 -0.0001 0.0168  -0.0125 1227 ALA B N   
17947 C CA  . ALA B 1229 ? 0.5738 0.6971 0.5865 0.0028  0.0192  -0.0128 1227 ALA B CA  
17948 C C   . ALA B 1229 ? 0.6251 0.7569 0.6428 0.0020  0.0197  -0.0118 1227 ALA B C   
17949 O O   . ALA B 1229 ? 0.6274 0.7688 0.6465 0.0012  0.0216  -0.0106 1227 ALA B O   
17950 C CB  . ALA B 1229 ? 0.4935 0.6136 0.5051 0.0086  0.0194  -0.0153 1227 ALA B CB  
17951 N N   . SER B 1230 ? 0.6062 0.7348 0.6267 0.0023  0.0181  -0.0122 1228 SER B N   
17952 C CA  . SER B 1230 ? 0.6134 0.7497 0.6384 0.0019  0.0183  -0.0115 1228 SER B CA  
17953 C C   . SER B 1230 ? 0.6608 0.8024 0.6870 -0.0037 0.0183  -0.0091 1228 SER B C   
17954 O O   . SER B 1230 ? 0.6563 0.8081 0.6857 -0.0043 0.0196  -0.0080 1228 SER B O   
17955 C CB  . SER B 1230 ? 0.6314 0.7623 0.6585 0.0030  0.0164  -0.0124 1228 SER B CB  
17956 O OG  . SER B 1230 ? 0.6563 0.7847 0.6832 0.0083  0.0166  -0.0143 1228 SER B OG  
17957 N N   . LEU B 1231 ? 0.6025 0.7375 0.6263 -0.0079 0.0169  -0.0081 1229 LEU B N   
17958 C CA  . LEU B 1231 ? 0.5913 0.7299 0.6157 -0.0136 0.0166  -0.0058 1229 LEU B CA  
17959 C C   . LEU B 1231 ? 0.6541 0.7996 0.6771 -0.0157 0.0186  -0.0042 1229 LEU B C   
17960 O O   . LEU B 1231 ? 0.6740 0.8243 0.6980 -0.0205 0.0186  -0.0021 1229 LEU B O   
17961 C CB  . LEU B 1231 ? 0.5772 0.7057 0.5991 -0.0172 0.0143  -0.0054 1229 LEU B CB  
17962 C CG  . LEU B 1231 ? 0.4502 0.5733 0.4738 -0.0172 0.0122  -0.0062 1229 LEU B CG  
17963 C CD1 . LEU B 1231 ? 0.3509 0.4655 0.3717 -0.0212 0.0102  -0.0054 1229 LEU B CD1 
17964 C CD2 . LEU B 1231 ? 0.4925 0.6235 0.5204 -0.0180 0.0122  -0.0055 1229 LEU B CD2 
17965 N N   . MET B 1232 ? 0.6407 0.7867 0.6612 -0.0124 0.0203  -0.0052 1230 MET B N   
17966 C CA  . MET B 1232 ? 0.6405 0.7948 0.6600 -0.0138 0.0226  -0.0037 1230 MET B CA  
17967 C C   . MET B 1232 ? 0.6648 0.8322 0.6893 -0.0134 0.0243  -0.0028 1230 MET B C   
17968 O O   . MET B 1232 ? 0.5559 0.7313 0.5811 -0.0171 0.0256  -0.0006 1230 MET B O   
17969 C CB  . MET B 1232 ? 0.6208 0.7731 0.6366 -0.0095 0.0241  -0.0053 1230 MET B CB  
17970 N N   . ALA B 1233 ? 0.7108 0.8805 0.7387 -0.0091 0.0242  -0.0044 1231 ALA B N   
17971 C CA  . ALA B 1233 ? 0.7826 0.9647 0.8157 -0.0082 0.0254  -0.0037 1231 ALA B CA  
17972 C C   . ALA B 1233 ? 0.8045 0.9887 0.8411 -0.0128 0.0236  -0.0021 1231 ALA B C   
17973 O O   . ALA B 1233 ? 0.8247 1.0191 0.8659 -0.0124 0.0242  -0.0014 1231 ALA B O   
17974 C CB  . ALA B 1233 ? 0.7422 0.9255 0.7770 -0.0013 0.0259  -0.0060 1231 ALA B CB  
17975 N N   . ILE B 1234 ? 0.7349 0.9099 0.7694 -0.0168 0.0213  -0.0016 1232 ILE B N   
17976 C CA  . ILE B 1234 ? 0.7007 0.8760 0.7377 -0.0212 0.0193  -0.0004 1232 ILE B CA  
17977 C C   . ILE B 1234 ? 0.6541 0.8315 0.6897 -0.0279 0.0192  0.0022  1232 ILE B C   
17978 O O   . ILE B 1234 ? 0.6272 0.7957 0.6584 -0.0307 0.0182  0.0026  1232 ILE B O   
17979 C CB  . ILE B 1234 ? 0.6358 0.7992 0.6713 -0.0208 0.0167  -0.0018 1232 ILE B CB  
17980 C CG1 . ILE B 1234 ? 0.6908 0.8531 0.7280 -0.0145 0.0168  -0.0040 1232 ILE B CG1 
17981 C CG2 . ILE B 1234 ? 0.5900 0.7529 0.6270 -0.0257 0.0146  -0.0005 1232 ILE B CG2 
17982 C CD1 . ILE B 1234 ? 0.5186 0.6756 0.5572 -0.0146 0.0145  -0.0047 1232 ILE B CD1 
17983 N N   . GLY B 1235 ? 0.5751 0.7643 0.6143 -0.0305 0.0202  0.0040  1233 GLY B N   
17984 C CA  . GLY B 1235 ? 0.4756 0.6679 0.5140 -0.0373 0.0201  0.0068  1233 GLY B CA  
17985 C C   . GLY B 1235 ? 0.3700 0.5680 0.4124 -0.0416 0.0185  0.0083  1233 GLY B C   
17986 O O   . GLY B 1235 ? 0.5882 0.7950 0.6354 -0.0393 0.0189  0.0079  1233 GLY B O   
17987 O OXT . GLY B 1235 ? 0.2955 0.4892 0.3361 -0.0476 0.0167  0.0098  1233 GLY B OXT 
# 
