data_9E0C
# 
_entry.id   9E0C 
# 
_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   9E0C         pdb_00009e0c 10.2210/pdb9e0c/pdb 
WWPDB D_1000289166 ?            ?                   
# 
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                        9E0C 
_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 'DI(HYDROXYETHYL)ETHER'           106.120    5    ?                ? ? ? 
4  non-polymer syn 'FORMIC ACID'                     46.025     4    ?                ? ? ? 
5  non-polymer syn '(1-benzofuran-5-yl)methanol'     148.159    2    ?                ? ? ? 
6  non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE 663.425    2    ?                ? ? ? 
7  non-polymer syn 'SULFATE ION'                     96.063     7    ?                ? ? ? 
8  non-polymer syn 'MAGNESIUM ION'                   24.305     2    ?                ? ? ? 
9  non-polymer syn 'TRIETHYLENE GLYCOL'              150.173    1    ?                ? ? ? 
10 non-polymer syn 'PENTAETHYLENE GLYCOL'            238.278    1    ?                ? ? ? 
11 water       nat water                             18.015     2577 ?                ? ? ? 
# 
_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  'DI(HYDROXYETHYL)ETHER'           PEG   
4  'FORMIC ACID'                     FMT   
5  '(1-benzofuran-5-yl)methanol'     A1BDX 
6  NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD   
7  'SULFATE ION'                     SO4   
8  'MAGNESIUM ION'                   MG    
9  'TRIETHYLENE GLYCOL'              PGE   
10 'PENTAETHYLENE GLYCOL'            1PE   
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 
A1BDX non-polymer         . '(1-benzofuran-5-yl)methanol'     ?      'C9 H8 O2'          148.159 
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  492  GLU GLU A . n 
A 1 495  ASN 495  493  493  ASN ASN 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   79   HIS HIS B . n 
B 1 82   SER 82   80   ?    ?   ?   B . n 
B 1 83   GLY 83   81   ?    ?   ?   B . n 
B 1 84   SER 84   82   ?    ?   ?   B . n 
B 1 85   GLY 85   83   83   GLY GLY B . n 
B 1 86   VAL 86   84   84   VAL VAL B . n 
B 1 87   GLU 87   85   85   GLU GLU B . n 
B 1 88   GLY 88   86   86   GLY GLY B . n 
B 1 89   LEU 89   87   87   LEU LEU B . n 
B 1 90   VAL 90   88   88   VAL VAL B . n 
B 1 91   GLN 91   89   89   GLN GLN B . n 
B 1 92   GLU 92   90   90   GLU GLU B . n 
B 1 93   TYR 93   91   91   TYR TYR B . n 
B 1 94   SER 94   92   92   SER SER B . n 
B 1 95   LEU 95   93   93   LEU LEU B . n 
B 1 96   SER 96   94   94   SER SER B . n 
B 1 97   SER 97   95   95   SER SER B . n 
B 1 98   GLN 98   96   96   GLN GLN B . n 
B 1 99   GLU 99   97   97   GLU GLU B . n 
B 1 100  GLY 100  98   98   GLY GLY B . n 
B 1 101  VAL 101  99   99   VAL VAL B . n 
B 1 102  ALA 102  100  100  ALA ALA B . n 
B 1 103  LEU 103  101  101  LEU LEU B . n 
B 1 104  MET 104  102  102  MET MET B . n 
B 1 105  CYS 105  103  103  CYS CYS B . n 
B 1 106  LEU 106  104  104  LEU LEU B . n 
B 1 107  ALA 107  105  105  ALA ALA B . n 
B 1 108  GLU 108  106  106  GLU GLU B . n 
B 1 109  ALA 109  107  107  ALA ALA B . n 
B 1 110  LEU 110  108  108  LEU LEU B . n 
B 1 111  LEU 111  109  109  LEU LEU B . n 
B 1 112  ARG 112  110  110  ARG ARG B . n 
B 1 113  ILE 113  111  111  ILE ILE B . n 
B 1 114  PRO 114  112  112  PRO PRO B . n 
B 1 115  ASP 115  113  113  ASP ASP B . n 
B 1 116  THR 116  114  114  THR THR B . n 
B 1 117  ALA 117  115  115  ALA ALA B . n 
B 1 118  THR 118  116  116  THR THR B . n 
B 1 119  ARG 119  117  117  ARG ARG B . n 
B 1 120  ASP 120  118  118  ASP ASP B . n 
B 1 121  ALA 121  119  119  ALA ALA B . n 
B 1 122  LEU 122  120  120  LEU LEU B . n 
B 1 123  ILE 123  121  121  ILE ILE B . n 
B 1 124  ARG 124  122  122  ARG ARG B . n 
B 1 125  ASP 125  123  123  ASP ASP B . n 
B 1 126  LYS 126  124  124  LYS LYS B . n 
B 1 127  ILE 127  125  125  ILE ILE B . n 
B 1 128  ALA 128  126  126  ALA ALA B . n 
B 1 129  ASP 129  127  127  ASP ASP B . n 
B 1 130  GLY 130  128  128  GLY GLY B . n 
B 1 131  ASN 131  129  129  ASN ASN B . n 
B 1 132  TRP 132  130  130  TRP TRP B . n 
B 1 133  LYS 133  131  131  LYS LYS B . n 
B 1 134  SER 134  132  132  SER SER B . n 
B 1 135  HIS 135  133  133  HIS HIS B . n 
B 1 136  LEU 136  134  134  LEU LEU B . n 
B 1 137  GLY 137  135  ?    ?   ?   B . n 
B 1 138  GLY 138  136  ?    ?   ?   B . n 
B 1 139  SER 139  137  ?    ?   ?   B . n 
B 1 140  ARG 140  138  138  ARG ARG B . n 
B 1 141  SER 141  139  139  SER SER B . n 
B 1 142  LEU 142  140  140  LEU LEU B . n 
B 1 143  PHE 143  141  141  PHE PHE B . n 
B 1 144  VAL 144  142  142  VAL VAL B . n 
B 1 145  ASN 145  143  143  ASN ASN B . n 
B 1 146  ALA 146  144  144  ALA ALA B . n 
B 1 147  ALA 147  145  145  ALA ALA B . n 
B 1 148  THR 148  146  146  THR THR B . n 
B 1 149  TRP 149  147  147  TRP TRP B . n 
B 1 150  GLY 150  148  148  GLY GLY B . n 
B 1 151  LEU 151  149  149  LEU LEU B . n 
B 1 152  VAL 152  150  150  VAL VAL B . n 
B 1 153  VAL 153  151  151  VAL VAL B . n 
B 1 154  THR 154  152  152  THR THR B . n 
B 1 155  GLY 155  153  153  GLY GLY B . n 
B 1 156  LYS 156  154  154  LYS LYS B . n 
B 1 157  LEU 157  155  155  LEU LEU B . n 
B 1 158  THR 158  156  156  THR THR B . n 
B 1 159  SER 159  157  157  SER SER B . n 
B 1 160  THR 160  158  158  THR THR B . n 
B 1 161  VAL 161  159  159  VAL VAL B . n 
B 1 162  ASN 162  160  160  ASN ASN B . n 
B 1 163  ASP 163  161  161  ASP ASP B . n 
B 1 164  ARG 164  162  162  ARG ARG B . n 
B 1 165  SER 165  163  163  SER SER B . n 
B 1 166  LEU 166  164  164  LEU LEU B . n 
B 1 167  ALA 167  165  165  ALA ALA B . n 
B 1 168  ALA 168  166  166  ALA ALA B . n 
B 1 169  ALA 169  167  167  ALA ALA B . n 
B 1 170  LEU 170  168  168  LEU LEU B . n 
B 1 171  THR 171  169  169  THR THR B . n 
B 1 172  ARG 172  170  170  ARG ARG B . n 
B 1 173  LEU 173  171  171  LEU LEU B . n 
B 1 174  ILE 174  172  172  ILE ILE B . n 
B 1 175  SER 175  173  173  SER SER B . n 
B 1 176  ARG 176  174  174  ARG ARG B . n 
B 1 177  CYS 177  175  175  CYS CYS B . n 
B 1 178  GLY 178  176  176  GLY GLY B . n 
B 1 179  GLU 179  177  177  GLU GLU B . n 
B 1 180  PRO 180  178  178  PRO PRO B . n 
B 1 181  VAL 181  179  179  VAL VAL B . n 
B 1 182  ILE 182  180  180  ILE ILE B . n 
B 1 183  ARG 183  181  181  ARG ARG B . n 
B 1 184  ARG 184  182  182  ARG ARG B . n 
B 1 185  GLY 185  183  183  GLY GLY B . n 
B 1 186  VAL 186  184  184  VAL VAL B . n 
B 1 187  ASP 187  185  185  ASP ASP B . n 
B 1 188  MET 188  186  186  MET MET B . n 
B 1 189  ALA 189  187  187  ALA ALA B . n 
B 1 190  MET 190  188  188  MET MET B . n 
B 1 191  ARG 191  189  189  ARG ARG B . n 
B 1 192  MET 192  190  190  MET MET B . n 
B 1 193  MET 193  191  191  MET MET B . n 
B 1 194  GLY 194  192  192  GLY GLY B . n 
B 1 195  GLU 195  193  193  GLU GLU B . n 
B 1 196  GLN 196  194  194  GLN GLN B . n 
B 1 197  PHE 197  195  195  PHE PHE B . n 
B 1 198  VAL 198  196  196  VAL VAL B . n 
B 1 199  THR 199  197  197  THR THR B . n 
B 1 200  GLY 200  198  198  GLY GLY B . n 
B 1 201  GLU 201  199  199  GLU GLU B . n 
B 1 202  THR 202  200  200  THR THR B . n 
B 1 203  ILE 203  201  201  ILE ILE B . n 
B 1 204  ARG 204  202  202  ARG ARG B . n 
B 1 205  GLU 205  203  203  GLU GLU B . n 
B 1 206  ALA 206  204  204  ALA ALA B . n 
B 1 207  LEU 207  205  205  LEU LEU B . n 
B 1 208  LYS 208  206  206  LYS LYS B . n 
B 1 209  ARG 209  207  207  ARG ARG B . n 
B 1 210  SER 210  208  208  SER SER B . n 
B 1 211  LYS 211  209  209  LYS LYS B . n 
B 1 212  GLU 212  210  210  GLU GLU B . n 
B 1 213  LEU 213  211  211  LEU LEU B . n 
B 1 214  GLU 214  212  212  GLU GLU B . n 
B 1 215  GLU 215  213  213  GLU GLU B . n 
B 1 216  LYS 216  214  214  LYS LYS B . n 
B 1 217  GLY 217  215  215  GLY GLY B . n 
B 1 218  PHE 218  216  216  PHE PHE B . n 
B 1 219  SER 219  217  217  SER SER B . n 
B 1 220  TYR 220  218  218  TYR TYR B . n 
B 1 221  SER 221  219  219  SER SER B . n 
B 1 222  TYR 222  220  220  TYR TYR B . n 
B 1 223  ASP 223  221  221  ASP ASP B . n 
B 1 224  MET 224  222  222  MET MET B . n 
B 1 225  LEU 225  223  223  LEU LEU B . n 
B 1 226  GLY 226  224  224  GLY GLY B . n 
B 1 227  GLU 227  225  225  GLU GLU B . n 
B 1 228  ALA 228  226  226  ALA ALA B . n 
B 1 229  ALA 229  227  227  ALA ALA B . n 
B 1 230  THR 230  228  228  THR THR B . n 
B 1 231  THR 231  229  229  THR THR B . n 
B 1 232  ALA 232  230  230  ALA ALA B . n 
B 1 233  ALA 233  231  231  ALA ALA B . n 
B 1 234  ASP 234  232  232  ASP ASP B . n 
B 1 235  ALA 235  233  233  ALA ALA B . n 
B 1 236  GLU 236  234  234  GLU GLU B . n 
B 1 237  ARG 237  235  235  ARG ARG B . n 
B 1 238  TYR 238  236  236  TYR TYR B . n 
B 1 239  TYR 239  237  237  TYR TYR B . n 
B 1 240  ARG 240  238  238  ARG ARG B . n 
B 1 241  ASP 241  239  239  ASP ASP B . n 
B 1 242  TYR 242  240  240  TYR TYR B . n 
B 1 243  GLU 243  241  241  GLU GLU B . n 
B 1 244  SER 244  242  242  SER SER B . n 
B 1 245  ALA 245  243  243  ALA ALA B . n 
B 1 246  ILE 246  244  244  ILE ILE B . n 
B 1 247  HIS 247  245  245  HIS HIS B . n 
B 1 248  ALA 248  246  246  ALA ALA B . n 
B 1 249  ILE 249  247  247  ILE ILE B . n 
B 1 250  GLY 250  248  248  GLY GLY B . n 
B 1 251  LYS 251  249  249  LYS LYS B . n 
B 1 252  ALA 252  250  250  ALA ALA B . n 
B 1 253  SER 253  251  251  SER SER B . n 
B 1 254  ALA 254  252  252  ALA ALA B . n 
B 1 255  GLY 255  253  253  GLY GLY B . n 
B 1 256  ARG 256  254  254  ARG ARG B . n 
B 1 257  GLY 257  255  255  GLY GLY B . n 
B 1 258  ILE 258  256  256  ILE ILE B . n 
B 1 259  TYR 259  257  257  TYR TYR B . n 
B 1 260  GLU 260  258  258  GLU GLU B . n 
B 1 261  GLY 261  259  259  GLY GLY B . n 
B 1 262  PRO 262  260  260  PRO PRO B . n 
B 1 263  GLY 263  261  261  GLY GLY B . n 
B 1 264  ILE 264  262  262  ILE ILE B . n 
B 1 265  SER 265  263  263  SER SER B . n 
B 1 266  ILE 266  264  264  ILE ILE B . n 
B 1 267  LYS 267  265  265  LYS LYS B . n 
B 1 268  LEU 268  266  266  LEU LEU B . n 
B 1 269  SER 269  267  267  SER SER B . n 
B 1 270  ALA 270  268  268  ALA ALA B . n 
B 1 271  LEU 271  269  269  LEU LEU B . n 
B 1 272  HIS 272  270  270  HIS HIS B . n 
B 1 273  PRO 273  271  271  PRO PRO B . n 
B 1 274  ARG 274  272  272  ARG ARG B . n 
B 1 275  TYR 275  273  273  TYR TYR B . n 
B 1 276  SER 276  274  274  SER SER B . n 
B 1 277  ARG 277  275  275  ARG ARG B . n 
B 1 278  ALA 278  276  276  ALA ALA B . n 
B 1 279  GLN 279  277  277  GLN GLN B . n 
B 1 280  ALA 280  278  278  ALA ALA B . n 
B 1 281  ALA 281  279  279  ALA ALA B . n 
B 1 282  ARG 282  280  280  ARG ARG B . n 
B 1 283  VAL 283  281  281  VAL VAL B . n 
B 1 284  MET 284  282  282  MET MET B . n 
B 1 285  GLY 285  283  283  GLY GLY B . n 
B 1 286  GLU 286  284  284  GLU GLU B . n 
B 1 287  LEU 287  285  285  LEU LEU B . n 
B 1 288  LEU 288  286  286  LEU LEU B . n 
B 1 289  PRO 289  287  287  PRO PRO B . n 
B 1 290  ARG 290  288  288  ARG ARG B . n 
B 1 291  VAL 291  289  289  VAL VAL B . n 
B 1 292  LYS 292  290  290  LYS LYS B . n 
B 1 293  ALA 293  291  291  ALA ALA B . n 
B 1 294  LEU 294  292  292  LEU LEU B . n 
B 1 295  ALA 295  293  293  ALA ALA B . n 
B 1 296  LEU 296  294  294  LEU LEU B . n 
B 1 297  LEU 297  295  295  LEU LEU B . n 
B 1 298  ALA 298  296  296  ALA ALA B . n 
B 1 299  LYS 299  297  297  LYS LYS B . n 
B 1 300  ASN 300  298  298  ASN ASN B . n 
B 1 301  TYR 301  299  299  TYR TYR B . n 
B 1 302  ASP 302  300  300  ASP ASP B . n 
B 1 303  ILE 303  301  301  ILE ILE B . n 
B 1 304  GLY 304  302  302  GLY GLY B . n 
B 1 305  LEU 305  303  303  LEU LEU B . n 
B 1 306  ASN 306  304  304  ASN ASN B . n 
B 1 307  ILE 307  305  305  ILE ILE B . n 
B 1 308  ASP 308  306  306  ASP ASP B . n 
B 1 309  ALA 309  307  307  ALA ALA B . n 
B 1 310  GLU 310  308  308  GLU GLU B . n 
B 1 311  GLU 311  309  309  GLU GLU B . n 
B 1 312  ALA 312  310  310  ALA ALA B . n 
B 1 313  ASP 313  311  311  ASP ASP B . n 
B 1 314  ARG 314  312  312  ARG ARG B . n 
B 1 315  LEU 315  313  313  LEU LEU B . n 
B 1 316  GLU 316  314  314  GLU GLU B . n 
B 1 317  LEU 317  315  315  LEU LEU B . n 
B 1 318  SER 318  316  316  SER SER B . n 
B 1 319  LEU 319  317  317  LEU LEU B . n 
B 1 320  ASP 320  318  318  ASP ASP B . n 
B 1 321  LEU 321  319  319  LEU LEU B . n 
B 1 322  LEU 322  320  320  LEU LEU B . n 
B 1 323  GLU 323  321  321  GLU GLU B . n 
B 1 324  VAL 324  322  322  VAL VAL B . n 
B 1 325  LEU 325  323  323  LEU LEU B . n 
B 1 326  CYS 326  324  324  CYS CYS B . n 
B 1 327  LEU 327  325  325  LEU LEU B . n 
B 1 328  ASP 328  326  326  ASP ASP B . n 
B 1 329  GLY 329  327  327  GLY GLY B . n 
B 1 330  ASP 330  328  328  ASP ASP B . n 
B 1 331  LEU 331  329  329  LEU LEU B . n 
B 1 332  SER 332  330  330  SER SER B . n 
B 1 333  GLY 333  331  331  GLY GLY B . n 
B 1 334  TRP 334  332  332  TRP TRP B . n 
B 1 335  ASN 335  333  333  ASN ASN B . n 
B 1 336  GLY 336  334  334  GLY GLY B . n 
B 1 337  MET 337  335  335  MET MET B . n 
B 1 338  GLY 338  336  336  GLY GLY B . n 
B 1 339  PHE 339  337  337  PHE PHE B . n 
B 1 340  VAL 340  338  338  VAL VAL B . n 
B 1 341  VAL 341  339  339  VAL VAL B . n 
B 1 342  GLN 342  340  340  GLN GLN B . n 
B 1 343  ALA 343  341  341  ALA ALA B . n 
B 1 344  TYR 344  342  342  TYR TYR B . n 
B 1 345  GLY 345  343  343  GLY GLY B . n 
B 1 346  LYS 346  344  344  LYS LYS B . n 
B 1 347  ARG 347  345  345  ARG ARG B . n 
B 1 348  CYS 348  346  346  CYS CYS B . n 
B 1 349  PRO 349  347  347  PRO PRO B . n 
B 1 350  PHE 350  348  348  PHE PHE B . n 
B 1 351  VAL 351  349  349  VAL VAL B . n 
B 1 352  LEU 352  350  350  LEU LEU B . n 
B 1 353  ASP 353  351  351  ASP ASP B . n 
B 1 354  PHE 354  352  352  PHE PHE B . n 
B 1 355  ILE 355  353  353  ILE ILE B . n 
B 1 356  ILE 356  354  354  ILE ILE B . n 
B 1 357  ASP 357  355  355  ASP ASP B . n 
B 1 358  LEU 358  356  356  LEU LEU B . n 
B 1 359  ALA 359  357  357  ALA ALA B . n 
B 1 360  ARG 360  358  358  ARG ARG B . n 
B 1 361  ARG 361  359  359  ARG ARG B . n 
B 1 362  SER 362  360  360  SER SER B . n 
B 1 363  GLY 363  361  361  GLY GLY B . n 
B 1 364  ARG 364  362  362  ARG ARG B . n 
B 1 365  ARG 365  363  363  ARG ARG B . n 
B 1 366  ILE 366  364  364  ILE ILE B . n 
B 1 367  MET 367  365  365  MET MET B . n 
B 1 368  VAL 368  366  366  VAL VAL B . n 
B 1 369  ARG 369  367  367  ARG ARG B . n 
B 1 370  LEU 370  368  368  LEU LEU B . n 
B 1 371  VAL 371  369  369  VAL VAL B . n 
B 1 372  LYS 372  370  370  LYS LYS B . n 
B 1 373  GLY 373  371  371  GLY GLY B . n 
B 1 374  ALA 374  372  372  ALA ALA B . n 
B 1 375  TYR 375  373  373  TYR TYR B . n 
B 1 376  TRP 376  374  374  TRP TRP B . n 
B 1 377  ASP 377  375  375  ASP ASP B . n 
B 1 378  ALA 378  376  376  ALA ALA B . n 
B 1 379  GLU 379  377  377  GLU GLU B . n 
B 1 380  ILE 380  378  378  ILE ILE B . n 
B 1 381  LYS 381  379  379  LYS LYS B . n 
B 1 382  ARG 382  380  380  ARG ARG B . n 
B 1 383  ALA 383  381  381  ALA ALA B . n 
B 1 384  GLN 384  382  382  GLN GLN B . n 
B 1 385  LEU 385  383  383  LEU LEU B . n 
B 1 386  ASP 386  384  384  ASP ASP B . n 
B 1 387  GLY 387  385  385  GLY GLY B . n 
B 1 388  LEU 388  386  386  LEU LEU B . n 
B 1 389  ALA 389  387  387  ALA ALA B . n 
B 1 390  ASP 390  388  388  ASP ASP B . n 
B 1 391  PHE 391  389  389  PHE PHE B . n 
B 1 392  PRO 392  390  390  PRO PRO B . n 
B 1 393  VAL 393  391  391  VAL VAL B . n 
B 1 394  PHE 394  392  392  PHE PHE B . n 
B 1 395  THR 395  393  393  THR THR B . n 
B 1 396  ARG 396  394  394  ARG ARG B . n 
B 1 397  LYS 397  395  395  LYS LYS B . n 
B 1 398  ILE 398  396  396  ILE ILE B . n 
B 1 399  HIS 399  397  397  HIS HIS B . n 
B 1 400  THR 400  398  398  THR THR B . n 
B 1 401  ASP 401  399  399  ASP ASP B . n 
B 1 402  VAL 402  400  400  VAL VAL B . n 
B 1 403  SER 403  401  401  SER SER B . n 
B 1 404  TYR 404  402  402  TYR TYR B . n 
B 1 405  ILE 405  403  403  ILE ILE B . n 
B 1 406  ALA 406  404  404  ALA ALA B . n 
B 1 407  CYS 407  405  405  CYS CYS B . n 
B 1 408  ALA 408  406  406  ALA ALA B . n 
B 1 409  ALA 409  407  407  ALA ALA B . n 
B 1 410  LYS 410  408  408  LYS LYS B . n 
B 1 411  LEU 411  409  409  LEU LEU B . n 
B 1 412  LEU 412  410  410  LEU LEU B . n 
B 1 413  ALA 413  411  411  ALA ALA B . n 
B 1 414  ALA 414  412  412  ALA ALA B . n 
B 1 415  THR 415  413  413  THR THR B . n 
B 1 416  ASP 416  414  414  ASP ASP B . n 
B 1 417  VAL 417  415  415  VAL VAL B . n 
B 1 418  VAL 418  416  416  VAL VAL B . n 
B 1 419  PHE 419  417  417  PHE PHE B . n 
B 1 420  PRO 420  418  418  PRO PRO B . n 
B 1 421  GLN 421  419  419  GLN GLN B . n 
B 1 422  PHE 422  420  420  PHE PHE B . n 
B 1 423  ALA 423  421  421  ALA ALA B . n 
B 1 424  THR 424  422  422  THR THR B . n 
B 1 425  HIS 425  423  423  HIS HIS B . n 
B 1 426  ASN 426  424  424  ASN ASN B . n 
B 1 427  ALA 427  425  425  ALA ALA B . n 
B 1 428  GLN 428  426  426  GLN GLN B . n 
B 1 429  THR 429  427  427  THR THR B . n 
B 1 430  LEU 430  428  428  LEU LEU B . n 
B 1 431  ALA 431  429  429  ALA ALA B . n 
B 1 432  ALA 432  430  430  ALA ALA B . n 
B 1 433  ILE 433  431  431  ILE ILE B . n 
B 1 434  TYR 434  432  432  TYR TYR B . n 
B 1 435  HIS 435  433  433  HIS HIS B . n 
B 1 436  MET 436  434  434  MET MET B . n 
B 1 437  ALA 437  435  435  ALA ALA B . n 
B 1 438  GLY 438  436  436  GLY GLY B . n 
B 1 439  LYS 439  437  437  LYS LYS B . n 
B 1 440  ASP 440  438  438  ASP ASP B . n 
B 1 441  PHE 441  439  439  PHE PHE B . n 
B 1 442  HIS 442  440  440  HIS HIS B . n 
B 1 443  VAL 443  441  441  VAL VAL B . n 
B 1 444  GLY 444  442  442  GLY GLY B . n 
B 1 445  LYS 445  443  443  LYS LYS B . n 
B 1 446  TYR 446  444  444  TYR TYR B . n 
B 1 447  GLU 447  445  445  GLU GLU B . n 
B 1 448  PHE 448  446  446  PHE PHE B . n 
B 1 449  GLN 449  447  447  GLN GLN B . n 
B 1 450  CYS 450  448  448  CYS CYS B . n 
B 1 451  LEU 451  449  449  LEU LEU B . n 
B 1 452  HIS 452  450  450  HIS HIS B . n 
B 1 453  GLY 453  451  451  GLY GLY B . n 
B 1 454  MET 454  452  452  MET MET B . n 
B 1 455  GLY 455  453  453  GLY GLY B . n 
B 1 456  GLU 456  454  454  GLU GLU B . n 
B 1 457  PRO 457  455  455  PRO PRO B . n 
B 1 458  LEU 458  456  456  LEU LEU B . n 
B 1 459  TYR 459  457  457  TYR TYR B . n 
B 1 460  GLU 460  458  458  GLU GLU B . n 
B 1 461  GLU 461  459  459  GLU GLU B . n 
B 1 462  VAL 462  460  460  VAL VAL B . n 
B 1 463  VAL 463  461  461  VAL VAL B . n 
B 1 464  GLY 464  462  462  GLY GLY B . n 
B 1 465  ARG 465  463  463  ARG ARG B . n 
B 1 466  GLY 466  464  464  GLY GLY B . n 
B 1 467  LYS 467  465  465  LYS LYS B . n 
B 1 468  LEU 468  466  466  LEU LEU B . n 
B 1 469  ASP 469  467  467  ASP ASP B . n 
B 1 470  ARG 470  468  468  ARG ARG B . n 
B 1 471  PRO 471  469  469  PRO PRO B . n 
B 1 472  CYS 472  470  470  CYS CYS B . n 
B 1 473  ARG 473  471  471  ARG ARG B . n 
B 1 474  ILE 474  472  472  ILE ILE B . n 
B 1 475  TYR 475  473  473  TYR TYR B . n 
B 1 476  ALA 476  474  474  ALA ALA B . n 
B 1 477  PRO 477  475  475  PRO PRO B . n 
B 1 478  VAL 478  476  476  VAL VAL B . n 
B 1 479  GLY 479  477  477  GLY GLY B . n 
B 1 480  THR 480  478  478  THR THR B . n 
B 1 481  HIS 481  479  479  HIS HIS B . n 
B 1 482  GLU 482  480  480  GLU GLU B . n 
B 1 483  THR 483  481  481  THR THR B . n 
B 1 484  LEU 484  482  482  LEU LEU B . n 
B 1 485  LEU 485  483  483  LEU LEU B . n 
B 1 486  ALA 486  484  484  ALA ALA B . n 
B 1 487  TYR 487  485  485  TYR TYR B . n 
B 1 488  LEU 488  486  486  LEU LEU B . n 
B 1 489  VAL 489  487  487  VAL VAL B . n 
B 1 490  ARG 490  488  488  ARG ARG B . n 
B 1 491  ARG 491  489  489  ARG ARG B . n 
B 1 492  LEU 492  490  490  LEU LEU B . n 
B 1 493  LEU 493  491  491  LEU LEU B . n 
B 1 494  GLU 494  492  ?    ?   ?   B . n 
B 1 495  ASN 495  493  ?    ?   ?   B . n 
B 1 496  GLY 496  494  ?    ?   ?   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  914  LEU LEU B . n 
B 1 917  ALA 917  915  915  ALA ALA B . n 
B 1 918  SER 918  916  916  SER SER B . n 
B 1 919  GLU 919  917  917  GLU GLU B . n 
B 1 920  THR 920  918  918  THR THR B . n 
B 1 921  GLY 921  919  919  GLY GLY B . n 
B 1 922  VAL 922  920  920  VAL VAL B . n 
B 1 923  GLY 923  921  921  GLY GLY B . n 
B 1 924  THR 924  922  922  THR THR B . n 
B 1 925  PHE 925  923  923  PHE PHE B . n 
B 1 926  VAL 926  924  924  VAL VAL B . n 
B 1 927  PRO 927  925  925  PRO PRO B . n 
B 1 928  PRO 928  926  926  PRO PRO B . n 
B 1 929  THR 929  927  927  THR THR B . n 
B 1 930  ILE 930  928  928  ILE ILE B . n 
B 1 931  ILE 931  929  929  ILE ILE B . n 
B 1 932  GLU 932  930  930  GLU GLU B . n 
B 1 933  LEU 933  931  931  LEU LEU B . n 
B 1 934  GLU 934  932  932  GLU GLU B . n 
B 1 935  LYS 935  933  933  LYS LYS B . n 
B 1 936  LEU 936  934  934  LEU LEU B . n 
B 1 937  SER 937  935  935  SER SER B . n 
B 1 938  ASP 938  936  936  ASP ASP B . n 
B 1 939  LEU 939  937  937  LEU LEU B . n 
B 1 940  GLN 940  938  938  GLN GLN B . n 
B 1 941  ARG 941  939  939  ARG ARG B . n 
B 1 942  GLU 942  940  940  GLU GLU B . n 
B 1 943  VAL 943  941  941  VAL VAL B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  GLY 945  943  943  GLY GLY B . n 
B 1 946  PRO 946  944  944  PRO PRO B . n 
B 1 947  VAL 947  945  945  VAL VAL B . n 
B 1 948  LEU 948  946  946  LEU LEU B . n 
B 1 949  HIS 949  947  947  HIS HIS B . n 
B 1 950  VAL 950  948  948  VAL VAL B . n 
B 1 951  ILE 951  949  949  ILE ILE B . n 
B 1 952  ARG 952  950  950  ARG ARG B . n 
B 1 953  TYR 953  951  951  TYR TYR B . n 
B 1 954  ARG 954  952  952  ARG ARG B . n 
B 1 955  ARG 955  953  953  ARG ARG B . n 
B 1 956  ASP 956  954  954  ASP ASP B . n 
B 1 957  ASP 957  955  955  ASP ASP B . n 
B 1 958  LEU 958  956  956  LEU LEU B . n 
B 1 959  ASP 959  957  957  ASP ASP B . n 
B 1 960  ARG 960  958  958  ARG ARG B . n 
B 1 961  LEU 961  959  959  LEU LEU B . n 
B 1 962  VAL 962  960  960  VAL VAL B . n 
B 1 963  ASP 963  961  961  ASP ASP B . n 
B 1 964  ASP 964  962  962  ASP ASP B . n 
B 1 965  VAL 965  963  963  VAL VAL B . n 
B 1 966  ASN 966  964  964  ASN ASN B . n 
B 1 967  ALA 967  965  965  ALA ALA B . n 
B 1 968  THR 968  966  966  THR THR B . n 
B 1 969  GLY 969  967  967  GLY GLY B . n 
B 1 970  TYR 970  968  968  TYR TYR B . n 
B 1 971  GLY 971  969  969  GLY GLY B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  THR 973  971  971  THR THR B . n 
B 1 974  PHE 974  972  972  PHE PHE B . n 
B 1 975  GLY 975  973  973  GLY GLY B . n 
B 1 976  LEU 976  974  974  LEU LEU B . n 
B 1 977  HIS 977  975  975  HIS HIS B . n 
B 1 978  THR 978  976  976  THR THR B . n 
B 1 979  ARG 979  977  977  ARG ARG B . n 
B 1 980  LEU 980  978  978  LEU LEU B . n 
B 1 981  ASP 981  979  979  ASP ASP B . n 
B 1 982  GLU 982  980  980  GLU GLU B . n 
B 1 983  THR 983  981  981  THR THR B . n 
B 1 984  ILE 984  982  982  ILE ILE B . n 
B 1 985  ALA 985  983  983  ALA ALA B . n 
B 1 986  HIS 986  984  984  HIS HIS B . n 
B 1 987  VAL 987  985  985  VAL VAL B . n 
B 1 988  THR 988  986  986  THR THR B . n 
B 1 989  SER 989  987  987  SER SER B . n 
B 1 990  ARG 990  988  988  ARG ARG B . n 
B 1 991  ILE 991  989  989  ILE ILE B . n 
B 1 992  LYS 992  990  990  LYS LYS B . n 
B 1 993  ALA 993  991  991  ALA ALA B . n 
B 1 994  GLY 994  992  992  GLY GLY B . n 
B 1 995  ASN 995  993  993  ASN ASN B . n 
B 1 996  LEU 996  994  994  LEU LEU B . n 
B 1 997  TYR 997  995  995  TYR TYR B . n 
B 1 998  ILE 998  996  996  ILE ILE B . n 
B 1 999  ASN 999  997  997  ASN ASN B . n 
B 1 1000 ARG 1000 998  998  ARG ARG B . n 
B 1 1001 ASN 1001 999  999  ASN ASN B . n 
B 1 1002 ILE 1002 1000 1000 ILE ILE B . n 
B 1 1003 ILE 1003 1001 1001 ILE ILE B . n 
B 1 1004 GLY 1004 1002 1002 GLY GLY B . n 
B 1 1005 ALA 1005 1003 1003 ALA ALA B . n 
B 1 1006 VAL 1006 1004 1004 VAL VAL B . n 
B 1 1007 VAL 1007 1005 1005 VAL VAL B . n 
B 1 1008 GLY 1008 1006 1006 GLY GLY B . n 
B 1 1009 VAL 1009 1007 1007 VAL VAL B . n 
B 1 1010 GLN 1010 1008 1008 GLN GLN B . n 
B 1 1011 PRO 1011 1009 1009 PRO PRO B . n 
B 1 1012 PHE 1012 1010 1010 PHE PHE B . n 
B 1 1013 GLY 1013 1011 1011 GLY GLY B . n 
B 1 1014 GLY 1014 1012 1012 GLY GLY B . n 
B 1 1015 ARG 1015 1013 1013 ARG ARG B . n 
B 1 1016 GLY 1016 1014 1014 GLY GLY B . n 
B 1 1017 LEU 1017 1015 1015 LEU LEU B . n 
B 1 1018 SER 1018 1016 1016 SER SER B . n 
B 1 1019 GLY 1019 1017 1017 GLY GLY B . n 
B 1 1020 THR 1020 1018 1018 THR THR B . n 
B 1 1021 GLY 1021 1019 1019 GLY GLY B . n 
B 1 1022 PRO 1022 1020 1020 PRO PRO B . n 
B 1 1023 LYS 1023 1021 1021 LYS LYS B . n 
B 1 1024 ALA 1024 1022 1022 ALA ALA B . n 
B 1 1025 GLY 1025 1023 1023 GLY GLY B . n 
B 1 1026 GLY 1026 1024 1024 GLY GLY B . n 
B 1 1027 PRO 1027 1025 1025 PRO PRO B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 TYR 1029 1027 1027 TYR TYR B . n 
B 1 1030 LEU 1030 1028 1028 LEU LEU B . n 
B 1 1031 GLY 1031 1029 1029 GLY GLY B . n 
B 1 1032 ARG 1032 1030 1030 ARG ARG B . n 
B 1 1033 LEU 1033 1031 1031 LEU LEU B . n 
B 1 1034 VAL 1034 1032 1032 VAL VAL B . n 
B 1 1035 THR 1035 1033 1033 THR THR B . n 
B 1 1036 THR 1036 1034 1034 THR THR B . n 
B 1 1037 ALA 1037 1035 1035 ALA ALA B . n 
B 1 1038 PRO 1038 1036 1036 PRO PRO B . n 
B 1 1039 VAL 1039 1037 1037 VAL VAL B . n 
B 1 1040 PRO 1040 1038 1038 PRO PRO B . n 
B 1 1041 PRO 1041 1039 1039 PRO PRO B . n 
B 1 1042 GLN 1042 1040 1040 GLN GLN B . n 
B 1 1043 HIS 1043 1041 1041 HIS HIS B . n 
B 1 1044 SER 1044 1042 1042 SER SER B . n 
B 1 1045 SER 1045 1043 1043 SER SER B . n 
B 1 1046 VAL 1046 1044 1044 VAL VAL B . n 
B 1 1047 HIS 1047 1045 1045 HIS HIS B . n 
B 1 1048 THR 1048 1046 1046 THR THR B . n 
B 1 1049 ASP 1049 1047 1047 ASP ASP B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 VAL 1051 1049 1049 VAL VAL B . n 
B 1 1052 LEU 1052 1050 1050 LEU LEU B . n 
B 1 1053 LEU 1053 1051 1051 LEU LEU B . n 
B 1 1054 ASP 1054 1052 1052 ASP ASP B . n 
B 1 1055 PHE 1055 1053 1053 PHE PHE B . n 
B 1 1056 ALA 1056 1054 1054 ALA ALA B . n 
B 1 1057 LYS 1057 1055 1055 LYS LYS B . n 
B 1 1058 TRP 1058 1056 1056 TRP TRP B . n 
B 1 1059 LEU 1059 1057 1057 LEU LEU B . n 
B 1 1060 ASP 1060 1058 1058 ASP ASP B . n 
B 1 1061 GLY 1061 1059 1059 GLY GLY B . n 
B 1 1062 LYS 1062 1060 1060 LYS LYS B . n 
B 1 1063 GLY 1063 1061 1061 GLY GLY B . n 
B 1 1064 ALA 1064 1062 1062 ALA ALA B . n 
B 1 1065 ARG 1065 1063 1063 ARG ARG B . n 
B 1 1066 ALA 1066 1064 1064 ALA ALA B . n 
B 1 1067 GLU 1067 1065 1065 GLU GLU B . n 
B 1 1068 ALA 1068 1066 1066 ALA ALA B . n 
B 1 1069 GLU 1069 1067 1067 GLU GLU B . n 
B 1 1070 ALA 1070 1068 1068 ALA ALA B . n 
B 1 1071 ALA 1071 1069 1069 ALA ALA B . n 
B 1 1072 ARG 1072 1070 1070 ARG ARG B . n 
B 1 1073 ASN 1073 1071 1071 ASN ASN B . n 
B 1 1074 ALA 1074 1072 1072 ALA ALA B . n 
B 1 1075 GLY 1075 1073 1073 GLY GLY B . n 
B 1 1076 SER 1076 1074 1074 SER SER B . n 
B 1 1077 SER 1077 1075 1075 SER SER B . n 
B 1 1078 SER 1078 1076 1076 SER SER B . n 
B 1 1079 ALA 1079 1077 1077 ALA ALA B . n 
B 1 1080 LEU 1080 1078 1078 LEU LEU B . n 
B 1 1081 GLY 1081 1079 1079 GLY GLY B . n 
B 1 1082 LEU 1082 1080 1080 LEU LEU B . n 
B 1 1083 ASP 1083 1081 1081 ASP ASP B . n 
B 1 1084 LEU 1084 1082 1082 LEU LEU B . n 
B 1 1085 GLU 1085 1083 1083 GLU GLU B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 PRO 1087 1085 1085 PRO PRO B . n 
B 1 1088 GLY 1088 1086 1086 GLY GLY B . n 
B 1 1089 PRO 1089 1087 1087 PRO PRO B . n 
B 1 1090 VAL 1090 1088 1088 VAL VAL B . n 
B 1 1091 GLY 1091 1089 1089 GLY GLY B . n 
B 1 1092 GLU 1092 1090 1090 GLU GLU B . n 
B 1 1093 ARG 1093 1091 1091 ARG ARG B . n 
B 1 1094 ASN 1094 1092 1092 ASN ASN B . n 
B 1 1095 LEU 1095 1093 1093 LEU LEU B . n 
B 1 1096 TYR 1096 1094 1094 TYR TYR B . n 
B 1 1097 THR 1097 1095 1095 THR THR B . n 
B 1 1098 LEU 1098 1096 1096 LEU LEU B . n 
B 1 1099 HIS 1099 1097 1097 HIS HIS B . n 
B 1 1100 ALA 1100 1098 1098 ALA ALA B . n 
B 1 1101 ARG 1101 1099 1099 ARG ARG B . n 
B 1 1102 GLY 1102 1100 1100 GLY GLY B . n 
B 1 1103 ARG 1103 1101 1101 ARG ARG B . n 
B 1 1104 ILE 1104 1102 1102 ILE ILE B . n 
B 1 1105 LEU 1105 1103 1103 LEU LEU B . n 
B 1 1106 LEU 1106 1104 1104 LEU LEU B . n 
B 1 1107 VAL 1107 1105 1105 VAL VAL B . n 
B 1 1108 PRO 1108 1106 1106 PRO PRO B . n 
B 1 1109 ALA 1109 1107 1107 ALA ALA B . n 
B 1 1110 THR 1110 1108 1108 THR THR B . n 
B 1 1111 GLU 1111 1109 1109 GLU GLU B . n 
B 1 1112 SER 1112 1110 1110 SER SER B . n 
B 1 1113 GLY 1113 1111 1111 GLY GLY B . n 
B 1 1114 LEU 1114 1112 1112 LEU LEU B . n 
B 1 1115 TYR 1115 1113 1113 TYR TYR B . n 
B 1 1116 HIS 1116 1114 1114 HIS HIS B . n 
B 1 1117 GLN 1117 1115 1115 GLN GLN B . n 
B 1 1118 LEU 1118 1116 1116 LEU LEU B . n 
B 1 1119 ALA 1119 1117 1117 ALA ALA B . n 
B 1 1120 ALA 1120 1118 1118 ALA ALA B . n 
B 1 1121 ALA 1121 1119 1119 ALA ALA B . n 
B 1 1122 LEU 1122 1120 1120 LEU LEU B . n 
B 1 1123 ALA 1123 1121 1121 ALA ALA B . n 
B 1 1124 THR 1124 1122 1122 THR THR B . n 
B 1 1125 GLY 1125 1123 1123 GLY GLY B . n 
B 1 1126 ASN 1126 1124 1124 ASN ASN B . n 
B 1 1127 SER 1127 1125 1125 SER SER B . n 
B 1 1128 VAL 1128 1126 1126 VAL VAL B . n 
B 1 1129 ALA 1129 1127 1127 ALA ALA B . n 
B 1 1130 ILE 1130 1128 1128 ILE ILE B . n 
B 1 1131 ASP 1131 1129 1129 ASP ASP B . n 
B 1 1132 ALA 1132 1130 1130 ALA ALA B . n 
B 1 1133 ALA 1133 1131 1131 ALA ALA B . n 
B 1 1134 SER 1134 1132 1132 SER SER B . n 
B 1 1135 GLY 1135 1133 1133 GLY GLY B . n 
B 1 1136 LEU 1136 1134 1134 LEU LEU B . n 
B 1 1137 GLN 1137 1135 1135 GLN GLN B . n 
B 1 1138 ALA 1138 1136 1136 ALA ALA B . n 
B 1 1139 SER 1139 1137 1137 SER SER B . n 
B 1 1140 LEU 1140 1138 1138 LEU LEU B . n 
B 1 1141 LYS 1141 1139 1139 LYS LYS B . n 
B 1 1142 ASN 1142 1140 1140 ASN ASN B . n 
B 1 1143 LEU 1143 1141 1141 LEU LEU B . n 
B 1 1144 PRO 1144 1142 1142 PRO PRO B . n 
B 1 1145 GLN 1145 1143 1143 GLN GLN B . n 
B 1 1146 THR 1146 1144 1144 THR THR B . n 
B 1 1147 VAL 1147 1145 1145 VAL VAL B . n 
B 1 1148 GLY 1148 1146 1146 GLY GLY B . n 
B 1 1149 LEU 1149 1147 1147 LEU LEU B . n 
B 1 1150 ARG 1150 1148 1148 ARG ARG B . n 
B 1 1151 VAL 1151 1149 1149 VAL VAL B . n 
B 1 1152 SER 1152 1150 1150 SER SER B . n 
B 1 1153 TRP 1153 1151 1151 TRP TRP B . n 
B 1 1154 SER 1154 1152 1152 SER SER B . n 
B 1 1155 LYS 1155 1153 1153 LYS LYS B . n 
B 1 1156 ASP 1156 1154 1154 ASP ASP B . n 
B 1 1157 TRP 1157 1155 1155 TRP TRP B . n 
B 1 1158 ALA 1158 1156 1156 ALA ALA B . n 
B 1 1159 ALA 1159 1157 1157 ALA ALA B . n 
B 1 1160 ASP 1160 1158 1158 ASP ASP B . n 
B 1 1161 GLY 1161 1159 1159 GLY GLY B . n 
B 1 1162 PRO 1162 1160 1160 PRO PRO B . n 
B 1 1163 PHE 1163 1161 1161 PHE PHE B . n 
B 1 1164 ALA 1164 1162 1162 ALA ALA B . n 
B 1 1165 GLY 1165 1163 1163 GLY GLY B . n 
B 1 1166 ALA 1166 1164 1164 ALA ALA B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 VAL 1168 1166 1166 VAL VAL B . n 
B 1 1169 GLU 1169 1167 1167 GLU GLU B . n 
B 1 1170 GLY 1170 1168 1168 GLY GLY B . n 
B 1 1171 ASP 1171 1169 1169 ASP ASP B . n 
B 1 1172 ALA 1172 1170 1170 ALA ALA B . n 
B 1 1173 GLU 1173 1171 1171 GLU GLU B . n 
B 1 1174 ARG 1174 1172 1172 ARG ARG B . n 
B 1 1175 ILE 1175 1173 1173 ILE ILE B . n 
B 1 1176 ARG 1176 1174 1174 ARG ARG B . n 
B 1 1177 ALA 1177 1175 1175 ALA ALA B . n 
B 1 1178 VAL 1178 1176 1176 VAL VAL B . n 
B 1 1179 ASN 1179 1177 1177 ASN ASN B . n 
B 1 1180 LYS 1180 1178 1178 LYS LYS B . n 
B 1 1181 ALA 1181 1179 1179 ALA ALA B . n 
B 1 1182 ILE 1182 1180 1180 ILE ILE B . n 
B 1 1183 ALA 1183 1181 1181 ALA ALA B . n 
B 1 1184 ALA 1184 1182 1182 ALA ALA B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 PRO 1186 1184 1184 PRO PRO B . n 
B 1 1187 GLY 1187 1185 1185 GLY GLY B . n 
B 1 1188 PRO 1188 1186 1186 PRO PRO B . n 
B 1 1189 LEU 1189 1187 1187 LEU LEU B . n 
B 1 1190 LEU 1190 1188 1188 LEU LEU B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 VAL 1192 1190 1190 VAL VAL B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 ALA 1194 1192 1192 ALA ALA B . n 
B 1 1195 ALA 1195 1193 1193 ALA ALA B . n 
B 1 1196 SER 1196 1194 1194 SER SER B . n 
B 1 1197 SER 1197 1195 1195 SER SER B . n 
B 1 1198 GLY 1198 1196 1196 GLY GLY B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 ILE 1200 1198 1198 ILE ILE B . n 
B 1 1201 ALA 1201 1199 1199 ALA ALA B . n 
B 1 1202 ARG 1202 1200 1200 ARG ARG B . n 
B 1 1203 ASN 1203 1201 1201 ASN ASN B . n 
B 1 1204 PRO 1204 1202 1202 PRO PRO B . n 
B 1 1205 ASP 1205 1203 1203 ASP ASP B . n 
B 1 1206 ALA 1206 1204 1204 ALA ALA B . n 
B 1 1207 TYR 1207 1205 1205 TYR TYR B . n 
B 1 1208 CYS 1208 1206 1206 CYS CYS B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 ASN 1210 1208 1208 ASN ASN B . n 
B 1 1211 TRP 1211 1209 1209 TRP TRP B . n 
B 1 1212 LEU 1212 1210 1210 LEU LEU B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 GLU 1214 1212 1212 GLU GLU B . n 
B 1 1215 GLU 1215 1213 1213 GLU GLU B . n 
B 1 1216 VAL 1216 1214 1214 VAL VAL B . n 
B 1 1217 SER 1217 1215 1215 SER SER B . n 
B 1 1218 ALA 1218 1216 1216 ALA ALA B . n 
B 1 1219 SER 1219 1217 1217 SER SER B . n 
B 1 1220 ILE 1220 1218 1218 ILE ILE B . n 
B 1 1221 ASN 1221 1219 1219 ASN ASN B . n 
B 1 1222 THR 1222 1220 1220 THR THR B . n 
B 1 1223 ALA 1223 1221 1221 ALA ALA B . n 
B 1 1224 ALA 1224 1222 1222 ALA ALA B . n 
B 1 1225 ALA 1225 1223 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 A1BDX ? ? A1BDX ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAD   ? ? NAD   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 FAD   ? ? FAD   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  2  FAD   1    1301 1301 FAD   FAD A . 
D  3  PEG   1    1302 1302 PEG   PEG A . 
E  4  FMT   1    1303 1303 FMT   FMT A . 
F  5  A1BDX 1    1304 1306 A1BDX 211 A . 
G  6  NAD   1    1305 2002 NAD   NAD A . 
H  7  SO4   1    1306 2    SO4   SO4 A . 
I  7  SO4   1    1307 3    SO4   SO4 A . 
J  7  SO4   1    1308 5    SO4   SO4 A . 
K  7  SO4   1    1309 6    SO4   SO4 A . 
L  7  SO4   1    1310 7    SO4   SO4 A . 
M  8  MG    1    1311 1    MG    MG  A . 
N  3  PEG   1    1312 2062 PEG   PEG A . 
O  2  FAD   1    1301 1301 FAD   FAD B . 
P  9  PGE   1    1302 1302 PGE   PGE B . 
Q  4  FMT   1    1303 1303 FMT   FMT B . 
R  10 1PE   1    1304 1304 1PE   1PE B . 
S  4  FMT   1    1305 1305 FMT   FMT B . 
T  3  PEG   1    1306 1306 PEG   PEG B . 
U  3  PEG   1    1307 1307 PEG   PEG B . 
V  3  PEG   1    1308 1308 PEG   PEG B . 
W  4  FMT   1    1309 1310 FMT   FMT B . 
X  5  A1BDX 1    1310 1312 A1BDX 211 B . 
Y  6  NAD   1    1311 2002 NAD   NAD B . 
Z  7  SO4   1    1312 1    SO4   SO4 B . 
AA 7  SO4   1    1313 4    SO4   SO4 B . 
BA 8  MG    1    1314 2    MG    MG  B . 
CA 11 HOH   1    1401 736  HOH   HOH A . 
CA 11 HOH   2    1402 181  HOH   HOH A . 
CA 11 HOH   3    1403 3110 HOH   HOH A . 
CA 11 HOH   4    1404 1684 HOH   HOH A . 
CA 11 HOH   5    1405 3030 HOH   HOH A . 
CA 11 HOH   6    1406 349  HOH   HOH A . 
CA 11 HOH   7    1407 3575 HOH   HOH A . 
CA 11 HOH   8    1408 3095 HOH   HOH A . 
CA 11 HOH   9    1409 3335 HOH   HOH A . 
CA 11 HOH   10   1410 1667 HOH   HOH A . 
CA 11 HOH   11   1411 1620 HOH   HOH A . 
CA 11 HOH   12   1412 3135 HOH   HOH A . 
CA 11 HOH   13   1413 3145 HOH   HOH A . 
CA 11 HOH   14   1414 1229 HOH   HOH A . 
CA 11 HOH   15   1415 3582 HOH   HOH A . 
CA 11 HOH   16   1416 1771 HOH   HOH A . 
CA 11 HOH   17   1417 711  HOH   HOH A . 
CA 11 HOH   18   1418 1548 HOH   HOH A . 
CA 11 HOH   19   1419 1535 HOH   HOH A . 
CA 11 HOH   20   1420 3417 HOH   HOH A . 
CA 11 HOH   21   1421 1763 HOH   HOH A . 
CA 11 HOH   22   1422 859  HOH   HOH A . 
CA 11 HOH   23   1423 1827 HOH   HOH A . 
CA 11 HOH   24   1424 3466 HOH   HOH A . 
CA 11 HOH   25   1425 3545 HOH   HOH A . 
CA 11 HOH   26   1426 3109 HOH   HOH A . 
CA 11 HOH   27   1427 3080 HOH   HOH A . 
CA 11 HOH   28   1428 3361 HOH   HOH A . 
CA 11 HOH   29   1429 617  HOH   HOH A . 
CA 11 HOH   30   1430 619  HOH   HOH A . 
CA 11 HOH   31   1431 1164 HOH   HOH A . 
CA 11 HOH   32   1432 1365 HOH   HOH A . 
CA 11 HOH   33   1433 842  HOH   HOH A . 
CA 11 HOH   34   1434 3451 HOH   HOH A . 
CA 11 HOH   35   1435 176  HOH   HOH A . 
CA 11 HOH   36   1436 3277 HOH   HOH A . 
CA 11 HOH   37   1437 3160 HOH   HOH A . 
CA 11 HOH   38   1438 714  HOH   HOH A . 
CA 11 HOH   39   1439 3069 HOH   HOH A . 
CA 11 HOH   40   1440 1732 HOH   HOH A . 
CA 11 HOH   41   1441 3231 HOH   HOH A . 
CA 11 HOH   42   1442 1749 HOH   HOH A . 
CA 11 HOH   43   1443 949  HOH   HOH A . 
CA 11 HOH   44   1444 468  HOH   HOH A . 
CA 11 HOH   45   1445 836  HOH   HOH A . 
CA 11 HOH   46   1446 1196 HOH   HOH A . 
CA 11 HOH   47   1447 3502 HOH   HOH A . 
CA 11 HOH   48   1448 1073 HOH   HOH A . 
CA 11 HOH   49   1449 1485 HOH   HOH A . 
CA 11 HOH   50   1450 3526 HOH   HOH A . 
CA 11 HOH   51   1451 1946 HOH   HOH A . 
CA 11 HOH   52   1452 1394 HOH   HOH A . 
CA 11 HOH   53   1453 375  HOH   HOH A . 
CA 11 HOH   54   1454 1990 HOH   HOH A . 
CA 11 HOH   55   1455 355  HOH   HOH A . 
CA 11 HOH   56   1456 3462 HOH   HOH A . 
CA 11 HOH   57   1457 1127 HOH   HOH A . 
CA 11 HOH   58   1458 1474 HOH   HOH A . 
CA 11 HOH   59   1459 1075 HOH   HOH A . 
CA 11 HOH   60   1460 3593 HOH   HOH A . 
CA 11 HOH   61   1461 484  HOH   HOH A . 
CA 11 HOH   62   1462 1318 HOH   HOH A . 
CA 11 HOH   63   1463 464  HOH   HOH A . 
CA 11 HOH   64   1464 1737 HOH   HOH A . 
CA 11 HOH   65   1465 1403 HOH   HOH A . 
CA 11 HOH   66   1466 1396 HOH   HOH A . 
CA 11 HOH   67   1467 226  HOH   HOH A . 
CA 11 HOH   68   1468 1959 HOH   HOH A . 
CA 11 HOH   69   1469 851  HOH   HOH A . 
CA 11 HOH   70   1470 3082 HOH   HOH A . 
CA 11 HOH   71   1471 1056 HOH   HOH A . 
CA 11 HOH   72   1472 1567 HOH   HOH A . 
CA 11 HOH   73   1473 1255 HOH   HOH A . 
CA 11 HOH   74   1474 1975 HOH   HOH A . 
CA 11 HOH   75   1475 387  HOH   HOH A . 
CA 11 HOH   76   1476 656  HOH   HOH A . 
CA 11 HOH   77   1477 873  HOH   HOH A . 
CA 11 HOH   78   1478 3039 HOH   HOH A . 
CA 11 HOH   79   1479 1801 HOH   HOH A . 
CA 11 HOH   80   1480 1508 HOH   HOH A . 
CA 11 HOH   81   1481 1461 HOH   HOH A . 
CA 11 HOH   82   1482 222  HOH   HOH A . 
CA 11 HOH   83   1483 599  HOH   HOH A . 
CA 11 HOH   84   1484 1559 HOH   HOH A . 
CA 11 HOH   85   1485 3177 HOH   HOH A . 
CA 11 HOH   86   1486 1982 HOH   HOH A . 
CA 11 HOH   87   1487 1826 HOH   HOH A . 
CA 11 HOH   88   1488 1721 HOH   HOH A . 
CA 11 HOH   89   1489 1102 HOH   HOH A . 
CA 11 HOH   90   1490 1305 HOH   HOH A . 
CA 11 HOH   91   1491 1831 HOH   HOH A . 
CA 11 HOH   92   1492 3101 HOH   HOH A . 
CA 11 HOH   93   1493 1389 HOH   HOH A . 
CA 11 HOH   94   1494 624  HOH   HOH A . 
CA 11 HOH   95   1495 1080 HOH   HOH A . 
CA 11 HOH   96   1496 3518 HOH   HOH A . 
CA 11 HOH   97   1497 20   HOH   HOH A . 
CA 11 HOH   98   1498 1468 HOH   HOH A . 
CA 11 HOH   99   1499 1638 HOH   HOH A . 
CA 11 HOH   100  1500 1985 HOH   HOH A . 
CA 11 HOH   101  1501 3443 HOH   HOH A . 
CA 11 HOH   102  1502 230  HOH   HOH A . 
CA 11 HOH   103  1503 1858 HOH   HOH A . 
CA 11 HOH   104  1504 1382 HOH   HOH A . 
CA 11 HOH   105  1505 234  HOH   HOH A . 
CA 11 HOH   106  1506 901  HOH   HOH A . 
CA 11 HOH   107  1507 3038 HOH   HOH A . 
CA 11 HOH   108  1508 251  HOH   HOH A . 
CA 11 HOH   109  1509 1126 HOH   HOH A . 
CA 11 HOH   110  1510 1565 HOH   HOH A . 
CA 11 HOH   111  1511 368  HOH   HOH A . 
CA 11 HOH   112  1512 753  HOH   HOH A . 
CA 11 HOH   113  1513 472  HOH   HOH A . 
CA 11 HOH   114  1514 549  HOH   HOH A . 
CA 11 HOH   115  1515 770  HOH   HOH A . 
CA 11 HOH   116  1516 1957 HOH   HOH A . 
CA 11 HOH   117  1517 65   HOH   HOH A . 
CA 11 HOH   118  1518 379  HOH   HOH A . 
CA 11 HOH   119  1519 479  HOH   HOH A . 
CA 11 HOH   120  1520 1860 HOH   HOH A . 
CA 11 HOH   121  1521 3188 HOH   HOH A . 
CA 11 HOH   122  1522 182  HOH   HOH A . 
CA 11 HOH   123  1523 1699 HOH   HOH A . 
CA 11 HOH   124  1524 343  HOH   HOH A . 
CA 11 HOH   125  1525 1220 HOH   HOH A . 
CA 11 HOH   126  1526 630  HOH   HOH A . 
CA 11 HOH   127  1527 291  HOH   HOH A . 
CA 11 HOH   128  1528 1458 HOH   HOH A . 
CA 11 HOH   129  1529 3293 HOH   HOH A . 
CA 11 HOH   130  1530 562  HOH   HOH A . 
CA 11 HOH   131  1531 692  HOH   HOH A . 
CA 11 HOH   132  1532 1340 HOH   HOH A . 
CA 11 HOH   133  1533 3049 HOH   HOH A . 
CA 11 HOH   134  1534 3078 HOH   HOH A . 
CA 11 HOH   135  1535 548  HOH   HOH A . 
CA 11 HOH   136  1536 1063 HOH   HOH A . 
CA 11 HOH   137  1537 60   HOH   HOH A . 
CA 11 HOH   138  1538 944  HOH   HOH A . 
CA 11 HOH   139  1539 662  HOH   HOH A . 
CA 11 HOH   140  1540 977  HOH   HOH A . 
CA 11 HOH   141  1541 897  HOH   HOH A . 
CA 11 HOH   142  1542 3096 HOH   HOH A . 
CA 11 HOH   143  1543 1600 HOH   HOH A . 
CA 11 HOH   144  1544 1739 HOH   HOH A . 
CA 11 HOH   145  1545 687  HOH   HOH A . 
CA 11 HOH   146  1546 1608 HOH   HOH A . 
CA 11 HOH   147  1547 850  HOH   HOH A . 
CA 11 HOH   148  1548 639  HOH   HOH A . 
CA 11 HOH   149  1549 297  HOH   HOH A . 
CA 11 HOH   150  1550 1205 HOH   HOH A . 
CA 11 HOH   151  1551 1430 HOH   HOH A . 
CA 11 HOH   152  1552 508  HOH   HOH A . 
CA 11 HOH   153  1553 773  HOH   HOH A . 
CA 11 HOH   154  1554 1254 HOH   HOH A . 
CA 11 HOH   155  1555 1663 HOH   HOH A . 
CA 11 HOH   156  1556 1678 HOH   HOH A . 
CA 11 HOH   157  1557 179  HOH   HOH A . 
CA 11 HOH   158  1558 107  HOH   HOH A . 
CA 11 HOH   159  1559 910  HOH   HOH A . 
CA 11 HOH   160  1560 431  HOH   HOH A . 
CA 11 HOH   161  1561 779  HOH   HOH A . 
CA 11 HOH   162  1562 888  HOH   HOH A . 
CA 11 HOH   163  1563 3001 HOH   HOH A . 
CA 11 HOH   164  1564 1109 HOH   HOH A . 
CA 11 HOH   165  1565 123  HOH   HOH A . 
CA 11 HOH   166  1566 3168 HOH   HOH A . 
CA 11 HOH   167  1567 1543 HOH   HOH A . 
CA 11 HOH   168  1568 270  HOH   HOH A . 
CA 11 HOH   169  1569 960  HOH   HOH A . 
CA 11 HOH   170  1570 3588 HOH   HOH A . 
CA 11 HOH   171  1571 3179 HOH   HOH A . 
CA 11 HOH   172  1572 1661 HOH   HOH A . 
CA 11 HOH   173  1573 620  HOH   HOH A . 
CA 11 HOH   174  1574 3214 HOH   HOH A . 
CA 11 HOH   175  1575 568  HOH   HOH A . 
CA 11 HOH   176  1576 74   HOH   HOH A . 
CA 11 HOH   177  1577 3447 HOH   HOH A . 
CA 11 HOH   178  1578 688  HOH   HOH A . 
CA 11 HOH   179  1579 860  HOH   HOH A . 
CA 11 HOH   180  1580 1320 HOH   HOH A . 
CA 11 HOH   181  1581 1122 HOH   HOH A . 
CA 11 HOH   182  1582 1806 HOH   HOH A . 
CA 11 HOH   183  1583 1432 HOH   HOH A . 
CA 11 HOH   184  1584 1726 HOH   HOH A . 
CA 11 HOH   185  1585 3125 HOH   HOH A . 
CA 11 HOH   186  1586 84   HOH   HOH A . 
CA 11 HOH   187  1587 3542 HOH   HOH A . 
CA 11 HOH   188  1588 1377 HOH   HOH A . 
CA 11 HOH   189  1589 668  HOH   HOH A . 
CA 11 HOH   190  1590 572  HOH   HOH A . 
CA 11 HOH   191  1591 3467 HOH   HOH A . 
CA 11 HOH   192  1592 399  HOH   HOH A . 
CA 11 HOH   193  1593 393  HOH   HOH A . 
CA 11 HOH   194  1594 982  HOH   HOH A . 
CA 11 HOH   195  1595 101  HOH   HOH A . 
CA 11 HOH   196  1596 895  HOH   HOH A . 
CA 11 HOH   197  1597 1111 HOH   HOH A . 
CA 11 HOH   198  1598 26   HOH   HOH A . 
CA 11 HOH   199  1599 1000 HOH   HOH A . 
CA 11 HOH   200  1600 3337 HOH   HOH A . 
CA 11 HOH   201  1601 1146 HOH   HOH A . 
CA 11 HOH   202  1602 311  HOH   HOH A . 
CA 11 HOH   203  1603 989  HOH   HOH A . 
CA 11 HOH   204  1604 841  HOH   HOH A . 
CA 11 HOH   205  1605 19   HOH   HOH A . 
CA 11 HOH   206  1606 1924 HOH   HOH A . 
CA 11 HOH   207  1607 167  HOH   HOH A . 
CA 11 HOH   208  1608 48   HOH   HOH A . 
CA 11 HOH   209  1609 1505 HOH   HOH A . 
CA 11 HOH   210  1610 1768 HOH   HOH A . 
CA 11 HOH   211  1611 1787 HOH   HOH A . 
CA 11 HOH   212  1612 556  HOH   HOH A . 
CA 11 HOH   213  1613 855  HOH   HOH A . 
CA 11 HOH   214  1614 3129 HOH   HOH A . 
CA 11 HOH   215  1615 308  HOH   HOH A . 
CA 11 HOH   216  1616 869  HOH   HOH A . 
CA 11 HOH   217  1617 1529 HOH   HOH A . 
CA 11 HOH   218  1618 321  HOH   HOH A . 
CA 11 HOH   219  1619 587  HOH   HOH A . 
CA 11 HOH   220  1620 3184 HOH   HOH A . 
CA 11 HOH   221  1621 45   HOH   HOH A . 
CA 11 HOH   222  1622 1576 HOH   HOH A . 
CA 11 HOH   223  1623 858  HOH   HOH A . 
CA 11 HOH   224  1624 400  HOH   HOH A . 
CA 11 HOH   225  1625 966  HOH   HOH A . 
CA 11 HOH   226  1626 313  HOH   HOH A . 
CA 11 HOH   227  1627 3142 HOH   HOH A . 
CA 11 HOH   228  1628 941  HOH   HOH A . 
CA 11 HOH   229  1629 1129 HOH   HOH A . 
CA 11 HOH   230  1630 170  HOH   HOH A . 
CA 11 HOH   231  1631 184  HOH   HOH A . 
CA 11 HOH   232  1632 1479 HOH   HOH A . 
CA 11 HOH   233  1633 1350 HOH   HOH A . 
CA 11 HOH   234  1634 3338 HOH   HOH A . 
CA 11 HOH   235  1635 3373 HOH   HOH A . 
CA 11 HOH   236  1636 614  HOH   HOH A . 
CA 11 HOH   237  1637 908  HOH   HOH A . 
CA 11 HOH   238  1638 804  HOH   HOH A . 
CA 11 HOH   239  1639 3226 HOH   HOH A . 
CA 11 HOH   240  1640 1290 HOH   HOH A . 
CA 11 HOH   241  1641 1745 HOH   HOH A . 
CA 11 HOH   242  1642 492  HOH   HOH A . 
CA 11 HOH   243  1643 1496 HOH   HOH A . 
CA 11 HOH   244  1644 3002 HOH   HOH A . 
CA 11 HOH   245  1645 1012 HOH   HOH A . 
CA 11 HOH   246  1646 962  HOH   HOH A . 
CA 11 HOH   247  1647 218  HOH   HOH A . 
CA 11 HOH   248  1648 3183 HOH   HOH A . 
CA 11 HOH   249  1649 1336 HOH   HOH A . 
CA 11 HOH   250  1650 737  HOH   HOH A . 
CA 11 HOH   251  1651 30   HOH   HOH A . 
CA 11 HOH   252  1652 1988 HOH   HOH A . 
CA 11 HOH   253  1653 214  HOH   HOH A . 
CA 11 HOH   254  1654 3024 HOH   HOH A . 
CA 11 HOH   255  1655 1406 HOH   HOH A . 
CA 11 HOH   256  1656 163  HOH   HOH A . 
CA 11 HOH   257  1657 1472 HOH   HOH A . 
CA 11 HOH   258  1658 372  HOH   HOH A . 
CA 11 HOH   259  1659 1086 HOH   HOH A . 
CA 11 HOH   260  1660 1702 HOH   HOH A . 
CA 11 HOH   261  1661 1799 HOH   HOH A . 
CA 11 HOH   262  1662 512  HOH   HOH A . 
CA 11 HOH   263  1663 128  HOH   HOH A . 
CA 11 HOH   264  1664 389  HOH   HOH A . 
CA 11 HOH   265  1665 1264 HOH   HOH A . 
CA 11 HOH   266  1666 1006 HOH   HOH A . 
CA 11 HOH   267  1667 3477 HOH   HOH A . 
CA 11 HOH   268  1668 726  HOH   HOH A . 
CA 11 HOH   269  1669 85   HOH   HOH A . 
CA 11 HOH   270  1670 877  HOH   HOH A . 
CA 11 HOH   271  1671 3428 HOH   HOH A . 
CA 11 HOH   272  1672 71   HOH   HOH A . 
CA 11 HOH   273  1673 177  HOH   HOH A . 
CA 11 HOH   274  1674 263  HOH   HOH A . 
CA 11 HOH   275  1675 412  HOH   HOH A . 
CA 11 HOH   276  1676 723  HOH   HOH A . 
CA 11 HOH   277  1677 447  HOH   HOH A . 
CA 11 HOH   278  1678 284  HOH   HOH A . 
CA 11 HOH   279  1679 902  HOH   HOH A . 
CA 11 HOH   280  1680 3178 HOH   HOH A . 
CA 11 HOH   281  1681 1840 HOH   HOH A . 
CA 11 HOH   282  1682 1733 HOH   HOH A . 
CA 11 HOH   283  1683 269  HOH   HOH A . 
CA 11 HOH   284  1684 224  HOH   HOH A . 
CA 11 HOH   285  1685 397  HOH   HOH A . 
CA 11 HOH   286  1686 1646 HOH   HOH A . 
CA 11 HOH   287  1687 885  HOH   HOH A . 
CA 11 HOH   288  1688 187  HOH   HOH A . 
CA 11 HOH   289  1689 430  HOH   HOH A . 
CA 11 HOH   290  1690 621  HOH   HOH A . 
CA 11 HOH   291  1691 500  HOH   HOH A . 
CA 11 HOH   292  1692 615  HOH   HOH A . 
CA 11 HOH   293  1693 1166 HOH   HOH A . 
CA 11 HOH   294  1694 749  HOH   HOH A . 
CA 11 HOH   295  1695 3487 HOH   HOH A . 
CA 11 HOH   296  1696 1443 HOH   HOH A . 
CA 11 HOH   297  1697 1092 HOH   HOH A . 
CA 11 HOH   298  1698 341  HOH   HOH A . 
CA 11 HOH   299  1699 746  HOH   HOH A . 
CA 11 HOH   300  1700 1551 HOH   HOH A . 
CA 11 HOH   301  1701 575  HOH   HOH A . 
CA 11 HOH   302  1702 1818 HOH   HOH A . 
CA 11 HOH   303  1703 3372 HOH   HOH A . 
CA 11 HOH   304  1704 535  HOH   HOH A . 
CA 11 HOH   305  1705 631  HOH   HOH A . 
CA 11 HOH   306  1706 143  HOH   HOH A . 
CA 11 HOH   307  1707 1681 HOH   HOH A . 
CA 11 HOH   308  1708 3302 HOH   HOH A . 
CA 11 HOH   309  1709 718  HOH   HOH A . 
CA 11 HOH   310  1710 243  HOH   HOH A . 
CA 11 HOH   311  1711 3523 HOH   HOH A . 
CA 11 HOH   312  1712 3464 HOH   HOH A . 
CA 11 HOH   313  1713 868  HOH   HOH A . 
CA 11 HOH   314  1714 3099 HOH   HOH A . 
CA 11 HOH   315  1715 1271 HOH   HOH A . 
CA 11 HOH   316  1716 1095 HOH   HOH A . 
CA 11 HOH   317  1717 1249 HOH   HOH A . 
CA 11 HOH   318  1718 127  HOH   HOH A . 
CA 11 HOH   319  1719 55   HOH   HOH A . 
CA 11 HOH   320  1720 22   HOH   HOH A . 
CA 11 HOH   321  1721 762  HOH   HOH A . 
CA 11 HOH   322  1722 1067 HOH   HOH A . 
CA 11 HOH   323  1723 1101 HOH   HOH A . 
CA 11 HOH   324  1724 427  HOH   HOH A . 
CA 11 HOH   325  1725 202  HOH   HOH A . 
CA 11 HOH   326  1726 220  HOH   HOH A . 
CA 11 HOH   327  1727 1026 HOH   HOH A . 
CA 11 HOH   328  1728 867  HOH   HOH A . 
CA 11 HOH   329  1729 871  HOH   HOH A . 
CA 11 HOH   330  1730 403  HOH   HOH A . 
CA 11 HOH   331  1731 99   HOH   HOH A . 
CA 11 HOH   332  1732 1514 HOH   HOH A . 
CA 11 HOH   333  1733 206  HOH   HOH A . 
CA 11 HOH   334  1734 180  HOH   HOH A . 
CA 11 HOH   335  1735 204  HOH   HOH A . 
CA 11 HOH   336  1736 550  HOH   HOH A . 
CA 11 HOH   337  1737 646  HOH   HOH A . 
CA 11 HOH   338  1738 1855 HOH   HOH A . 
CA 11 HOH   339  1739 3567 HOH   HOH A . 
CA 11 HOH   340  1740 3424 HOH   HOH A . 
CA 11 HOH   341  1741 625  HOH   HOH A . 
CA 11 HOH   342  1742 286  HOH   HOH A . 
CA 11 HOH   343  1743 171  HOH   HOH A . 
CA 11 HOH   344  1744 1693 HOH   HOH A . 
CA 11 HOH   345  1745 547  HOH   HOH A . 
CA 11 HOH   346  1746 384  HOH   HOH A . 
CA 11 HOH   347  1747 786  HOH   HOH A . 
CA 11 HOH   348  1748 250  HOH   HOH A . 
CA 11 HOH   349  1749 1583 HOH   HOH A . 
CA 11 HOH   350  1750 236  HOH   HOH A . 
CA 11 HOH   351  1751 193  HOH   HOH A . 
CA 11 HOH   352  1752 1236 HOH   HOH A . 
CA 11 HOH   353  1753 118  HOH   HOH A . 
CA 11 HOH   354  1754 732  HOH   HOH A . 
CA 11 HOH   355  1755 1526 HOH   HOH A . 
CA 11 HOH   356  1756 1160 HOH   HOH A . 
CA 11 HOH   357  1757 241  HOH   HOH A . 
CA 11 HOH   358  1758 1381 HOH   HOH A . 
CA 11 HOH   359  1759 239  HOH   HOH A . 
CA 11 HOH   360  1760 640  HOH   HOH A . 
CA 11 HOH   361  1761 91   HOH   HOH A . 
CA 11 HOH   362  1762 132  HOH   HOH A . 
CA 11 HOH   363  1763 342  HOH   HOH A . 
CA 11 HOH   364  1764 800  HOH   HOH A . 
CA 11 HOH   365  1765 724  HOH   HOH A . 
CA 11 HOH   366  1766 661  HOH   HOH A . 
CA 11 HOH   367  1767 1388 HOH   HOH A . 
CA 11 HOH   368  1768 607  HOH   HOH A . 
CA 11 HOH   369  1769 499  HOH   HOH A . 
CA 11 HOH   370  1770 339  HOH   HOH A . 
CA 11 HOH   371  1771 1510 HOH   HOH A . 
CA 11 HOH   372  1772 1312 HOH   HOH A . 
CA 11 HOH   373  1773 3097 HOH   HOH A . 
CA 11 HOH   374  1774 832  HOH   HOH A . 
CA 11 HOH   375  1775 591  HOH   HOH A . 
CA 11 HOH   376  1776 452  HOH   HOH A . 
CA 11 HOH   377  1777 364  HOH   HOH A . 
CA 11 HOH   378  1778 539  HOH   HOH A . 
CA 11 HOH   379  1779 360  HOH   HOH A . 
CA 11 HOH   380  1780 272  HOH   HOH A . 
CA 11 HOH   381  1781 742  HOH   HOH A . 
CA 11 HOH   382  1782 507  HOH   HOH A . 
CA 11 HOH   383  1783 199  HOH   HOH A . 
CA 11 HOH   384  1784 354  HOH   HOH A . 
CA 11 HOH   385  1785 1020 HOH   HOH A . 
CA 11 HOH   386  1786 1423 HOH   HOH A . 
CA 11 HOH   387  1787 2059 HOH   HOH A . 
CA 11 HOH   388  1788 1859 HOH   HOH A . 
CA 11 HOH   389  1789 469  HOH   HOH A . 
CA 11 HOH   390  1790 31   HOH   HOH A . 
CA 11 HOH   391  1791 1209 HOH   HOH A . 
CA 11 HOH   392  1792 164  HOH   HOH A . 
CA 11 HOH   393  1793 1098 HOH   HOH A . 
CA 11 HOH   394  1794 3070 HOH   HOH A . 
CA 11 HOH   395  1795 57   HOH   HOH A . 
CA 11 HOH   396  1796 363  HOH   HOH A . 
CA 11 HOH   397  1797 916  HOH   HOH A . 
CA 11 HOH   398  1798 491  HOH   HOH A . 
CA 11 HOH   399  1799 1040 HOH   HOH A . 
CA 11 HOH   400  1800 432  HOH   HOH A . 
CA 11 HOH   401  1801 253  HOH   HOH A . 
CA 11 HOH   402  1802 3020 HOH   HOH A . 
CA 11 HOH   403  1803 1145 HOH   HOH A . 
CA 11 HOH   404  1804 264  HOH   HOH A . 
CA 11 HOH   405  1805 330  HOH   HOH A . 
CA 11 HOH   406  1806 984  HOH   HOH A . 
CA 11 HOH   407  1807 1270 HOH   HOH A . 
CA 11 HOH   408  1808 3276 HOH   HOH A . 
CA 11 HOH   409  1809 1448 HOH   HOH A . 
CA 11 HOH   410  1810 312  HOH   HOH A . 
CA 11 HOH   411  1811 768  HOH   HOH A . 
CA 11 HOH   412  1812 294  HOH   HOH A . 
CA 11 HOH   413  1813 1462 HOH   HOH A . 
CA 11 HOH   414  1814 542  HOH   HOH A . 
CA 11 HOH   415  1815 552  HOH   HOH A . 
CA 11 HOH   416  1816 104  HOH   HOH A . 
CA 11 HOH   417  1817 268  HOH   HOH A . 
CA 11 HOH   418  1818 160  HOH   HOH A . 
CA 11 HOH   419  1819 1410 HOH   HOH A . 
CA 11 HOH   420  1820 1198 HOH   HOH A . 
CA 11 HOH   421  1821 505  HOH   HOH A . 
CA 11 HOH   422  1822 365  HOH   HOH A . 
CA 11 HOH   423  1823 28   HOH   HOH A . 
CA 11 HOH   424  1824 553  HOH   HOH A . 
CA 11 HOH   425  1825 3532 HOH   HOH A . 
CA 11 HOH   426  1826 896  HOH   HOH A . 
CA 11 HOH   427  1827 1790 HOH   HOH A . 
CA 11 HOH   428  1828 1276 HOH   HOH A . 
CA 11 HOH   429  1829 439  HOH   HOH A . 
CA 11 HOH   430  1830 271  HOH   HOH A . 
CA 11 HOH   431  1831 141  HOH   HOH A . 
CA 11 HOH   432  1832 2025 HOH   HOH A . 
CA 11 HOH   433  1833 1070 HOH   HOH A . 
CA 11 HOH   434  1834 700  HOH   HOH A . 
CA 11 HOH   435  1835 1444 HOH   HOH A . 
CA 11 HOH   436  1836 683  HOH   HOH A . 
CA 11 HOH   437  1837 137  HOH   HOH A . 
CA 11 HOH   438  1838 3195 HOH   HOH A . 
CA 11 HOH   439  1839 3365 HOH   HOH A . 
CA 11 HOH   440  1840 1222 HOH   HOH A . 
CA 11 HOH   441  1841 383  HOH   HOH A . 
CA 11 HOH   442  1842 1817 HOH   HOH A . 
CA 11 HOH   443  1843 136  HOH   HOH A . 
CA 11 HOH   444  1844 701  HOH   HOH A . 
CA 11 HOH   445  1845 1046 HOH   HOH A . 
CA 11 HOH   446  1846 316  HOH   HOH A . 
CA 11 HOH   447  1847 3212 HOH   HOH A . 
CA 11 HOH   448  1848 530  HOH   HOH A . 
CA 11 HOH   449  1849 1225 HOH   HOH A . 
CA 11 HOH   450  1850 1009 HOH   HOH A . 
CA 11 HOH   451  1851 1321 HOH   HOH A . 
CA 11 HOH   452  1852 979  HOH   HOH A . 
CA 11 HOH   453  1853 609  HOH   HOH A . 
CA 11 HOH   454  1854 69   HOH   HOH A . 
CA 11 HOH   455  1855 1874 HOH   HOH A . 
CA 11 HOH   456  1856 1542 HOH   HOH A . 
CA 11 HOH   457  1857 73   HOH   HOH A . 
CA 11 HOH   458  1858 404  HOH   HOH A . 
CA 11 HOH   459  1859 3133 HOH   HOH A . 
CA 11 HOH   460  1860 883  HOH   HOH A . 
CA 11 HOH   461  1861 1714 HOH   HOH A . 
CA 11 HOH   462  1862 766  HOH   HOH A . 
CA 11 HOH   463  1863 540  HOH   HOH A . 
CA 11 HOH   464  1864 965  HOH   HOH A . 
CA 11 HOH   465  1865 3260 HOH   HOH A . 
CA 11 HOH   466  1866 1748 HOH   HOH A . 
CA 11 HOH   467  1867 3404 HOH   HOH A . 
CA 11 HOH   468  1868 1149 HOH   HOH A . 
CA 11 HOH   469  1869 1016 HOH   HOH A . 
CA 11 HOH   470  1870 857  HOH   HOH A . 
CA 11 HOH   471  1871 1435 HOH   HOH A . 
CA 11 HOH   472  1872 3103 HOH   HOH A . 
CA 11 HOH   473  1873 604  HOH   HOH A . 
CA 11 HOH   474  1874 3503 HOH   HOH A . 
CA 11 HOH   475  1875 265  HOH   HOH A . 
CA 11 HOH   476  1876 454  HOH   HOH A . 
CA 11 HOH   477  1877 1243 HOH   HOH A . 
CA 11 HOH   478  1878 1257 HOH   HOH A . 
CA 11 HOH   479  1879 642  HOH   HOH A . 
CA 11 HOH   480  1880 1685 HOH   HOH A . 
CA 11 HOH   481  1881 754  HOH   HOH A . 
CA 11 HOH   482  1882 227  HOH   HOH A . 
CA 11 HOH   483  1883 320  HOH   HOH A . 
CA 11 HOH   484  1884 671  HOH   HOH A . 
CA 11 HOH   485  1885 1911 HOH   HOH A . 
CA 11 HOH   486  1886 473  HOH   HOH A . 
CA 11 HOH   487  1887 1204 HOH   HOH A . 
CA 11 HOH   488  1888 1773 HOH   HOH A . 
CA 11 HOH   489  1889 1913 HOH   HOH A . 
CA 11 HOH   490  1890 1778 HOH   HOH A . 
CA 11 HOH   491  1891 697  HOH   HOH A . 
CA 11 HOH   492  1892 1413 HOH   HOH A . 
CA 11 HOH   493  1893 848  HOH   HOH A . 
CA 11 HOH   494  1894 150  HOH   HOH A . 
CA 11 HOH   495  1895 544  HOH   HOH A . 
CA 11 HOH   496  1896 798  HOH   HOH A . 
CA 11 HOH   497  1897 1136 HOH   HOH A . 
CA 11 HOH   498  1898 1115 HOH   HOH A . 
CA 11 HOH   499  1899 2043 HOH   HOH A . 
CA 11 HOH   500  1900 436  HOH   HOH A . 
CA 11 HOH   501  1901 3340 HOH   HOH A . 
CA 11 HOH   502  1902 1942 HOH   HOH A . 
CA 11 HOH   503  1903 414  HOH   HOH A . 
CA 11 HOH   504  1904 146  HOH   HOH A . 
CA 11 HOH   505  1905 586  HOH   HOH A . 
CA 11 HOH   506  1906 1019 HOH   HOH A . 
CA 11 HOH   507  1907 172  HOH   HOH A . 
CA 11 HOH   508  1908 3243 HOH   HOH A . 
CA 11 HOH   509  1909 3241 HOH   HOH A . 
CA 11 HOH   510  1910 33   HOH   HOH A . 
CA 11 HOH   511  1911 1713 HOH   HOH A . 
CA 11 HOH   512  1912 3217 HOH   HOH A . 
CA 11 HOH   513  1913 707  HOH   HOH A . 
CA 11 HOH   514  1914 3317 HOH   HOH A . 
CA 11 HOH   515  1915 784  HOH   HOH A . 
CA 11 HOH   516  1916 1369 HOH   HOH A . 
CA 11 HOH   517  1917 3521 HOH   HOH A . 
CA 11 HOH   518  1918 402  HOH   HOH A . 
CA 11 HOH   519  1919 3344 HOH   HOH A . 
CA 11 HOH   520  1920 348  HOH   HOH A . 
CA 11 HOH   521  1921 788  HOH   HOH A . 
CA 11 HOH   522  1922 3595 HOH   HOH A . 
CA 11 HOH   523  1923 2034 HOH   HOH A . 
CA 11 HOH   524  1924 80   HOH   HOH A . 
CA 11 HOH   525  1925 1295 HOH   HOH A . 
CA 11 HOH   526  1926 46   HOH   HOH A . 
CA 11 HOH   527  1927 1814 HOH   HOH A . 
CA 11 HOH   528  1928 476  HOH   HOH A . 
CA 11 HOH   529  1929 288  HOH   HOH A . 
CA 11 HOH   530  1930 231  HOH   HOH A . 
CA 11 HOH   531  1931 92   HOH   HOH A . 
CA 11 HOH   532  1932 680  HOH   HOH A . 
CA 11 HOH   533  1933 3128 HOH   HOH A . 
CA 11 HOH   534  1934 729  HOH   HOH A . 
CA 11 HOH   535  1935 3397 HOH   HOH A . 
CA 11 HOH   536  1936 3026 HOH   HOH A . 
CA 11 HOH   537  1937 1546 HOH   HOH A . 
CA 11 HOH   538  1938 1033 HOH   HOH A . 
CA 11 HOH   539  1939 600  HOH   HOH A . 
CA 11 HOH   540  1940 3473 HOH   HOH A . 
CA 11 HOH   541  1941 952  HOH   HOH A . 
CA 11 HOH   542  1942 3215 HOH   HOH A . 
CA 11 HOH   543  1943 870  HOH   HOH A . 
CA 11 HOH   544  1944 156  HOH   HOH A . 
CA 11 HOH   545  1945 1048 HOH   HOH A . 
CA 11 HOH   546  1946 603  HOH   HOH A . 
CA 11 HOH   547  1947 517  HOH   HOH A . 
CA 11 HOH   548  1948 744  HOH   HOH A . 
CA 11 HOH   549  1949 369  HOH   HOH A . 
CA 11 HOH   550  1950 174  HOH   HOH A . 
CA 11 HOH   551  1951 559  HOH   HOH A . 
CA 11 HOH   552  1952 853  HOH   HOH A . 
CA 11 HOH   553  1953 3047 HOH   HOH A . 
CA 11 HOH   554  1954 1823 HOH   HOH A . 
CA 11 HOH   555  1955 856  HOH   HOH A . 
CA 11 HOH   556  1956 1079 HOH   HOH A . 
CA 11 HOH   557  1957 17   HOH   HOH A . 
CA 11 HOH   558  1958 808  HOH   HOH A . 
CA 11 HOH   559  1959 970  HOH   HOH A . 
CA 11 HOH   560  1960 346  HOH   HOH A . 
CA 11 HOH   561  1961 1135 HOH   HOH A . 
CA 11 HOH   562  1962 443  HOH   HOH A . 
CA 11 HOH   563  1963 818  HOH   HOH A . 
CA 11 HOH   564  1964 1832 HOH   HOH A . 
CA 11 HOH   565  1965 3180 HOH   HOH A . 
CA 11 HOH   566  1966 1977 HOH   HOH A . 
CA 11 HOH   567  1967 1399 HOH   HOH A . 
CA 11 HOH   568  1968 3318 HOH   HOH A . 
CA 11 HOH   569  1969 273  HOH   HOH A . 
CA 11 HOH   570  1970 1004 HOH   HOH A . 
CA 11 HOH   571  1971 1609 HOH   HOH A . 
CA 11 HOH   572  1972 3316 HOH   HOH A . 
CA 11 HOH   573  1973 41   HOH   HOH A . 
CA 11 HOH   574  1974 963  HOH   HOH A . 
CA 11 HOH   575  1975 791  HOH   HOH A . 
CA 11 HOH   576  1976 3278 HOH   HOH A . 
CA 11 HOH   577  1977 169  HOH   HOH A . 
CA 11 HOH   578  1978 811  HOH   HOH A . 
CA 11 HOH   579  1979 3603 HOH   HOH A . 
CA 11 HOH   580  1980 1703 HOH   HOH A . 
CA 11 HOH   581  1981 675  HOH   HOH A . 
CA 11 HOH   582  1982 1024 HOH   HOH A . 
CA 11 HOH   583  1983 1167 HOH   HOH A . 
CA 11 HOH   584  1984 433  HOH   HOH A . 
CA 11 HOH   585  1985 1836 HOH   HOH A . 
CA 11 HOH   586  1986 986  HOH   HOH A . 
CA 11 HOH   587  1987 225  HOH   HOH A . 
CA 11 HOH   588  1988 887  HOH   HOH A . 
CA 11 HOH   589  1989 381  HOH   HOH A . 
CA 11 HOH   590  1990 674  HOH   HOH A . 
CA 11 HOH   591  1991 3498 HOH   HOH A . 
CA 11 HOH   592  1992 510  HOH   HOH A . 
CA 11 HOH   593  1993 1036 HOH   HOH A . 
CA 11 HOH   594  1994 893  HOH   HOH A . 
CA 11 HOH   595  1995 326  HOH   HOH A . 
CA 11 HOH   596  1996 1441 HOH   HOH A . 
CA 11 HOH   597  1997 1660 HOH   HOH A . 
CA 11 HOH   598  1998 1317 HOH   HOH A . 
CA 11 HOH   599  1999 678  HOH   HOH A . 
CA 11 HOH   600  2000 677  HOH   HOH A . 
CA 11 HOH   601  2001 835  HOH   HOH A . 
CA 11 HOH   602  2002 3084 HOH   HOH A . 
CA 11 HOH   603  2003 1059 HOH   HOH A . 
CA 11 HOH   604  2004 1304 HOH   HOH A . 
CA 11 HOH   605  2005 733  HOH   HOH A . 
CA 11 HOH   606  2006 395  HOH   HOH A . 
CA 11 HOH   607  2007 708  HOH   HOH A . 
CA 11 HOH   608  2008 3157 HOH   HOH A . 
CA 11 HOH   609  2009 324  HOH   HOH A . 
CA 11 HOH   610  2010 90   HOH   HOH A . 
CA 11 HOH   611  2011 3008 HOH   HOH A . 
CA 11 HOH   612  2012 3022 HOH   HOH A . 
CA 11 HOH   613  2013 480  HOH   HOH A . 
CA 11 HOH   614  2014 444  HOH   HOH A . 
CA 11 HOH   615  2015 1910 HOH   HOH A . 
CA 11 HOH   616  2016 1414 HOH   HOH A . 
CA 11 HOH   617  2017 1439 HOH   HOH A . 
CA 11 HOH   618  2018 1513 HOH   HOH A . 
CA 11 HOH   619  2019 833  HOH   HOH A . 
CA 11 HOH   620  2020 772  HOH   HOH A . 
CA 11 HOH   621  2021 63   HOH   HOH A . 
CA 11 HOH   622  2022 3439 HOH   HOH A . 
CA 11 HOH   623  2023 1992 HOH   HOH A . 
CA 11 HOH   624  2024 3005 HOH   HOH A . 
CA 11 HOH   625  2025 3497 HOH   HOH A . 
CA 11 HOH   626  2026 1346 HOH   HOH A . 
CA 11 HOH   627  2027 516  HOH   HOH A . 
CA 11 HOH   628  2028 1503 HOH   HOH A . 
CA 11 HOH   629  2029 1060 HOH   HOH A . 
CA 11 HOH   630  2030 131  HOH   HOH A . 
CA 11 HOH   631  2031 532  HOH   HOH A . 
CA 11 HOH   632  2032 2028 HOH   HOH A . 
CA 11 HOH   633  2033 1923 HOH   HOH A . 
CA 11 HOH   634  2034 1088 HOH   HOH A . 
CA 11 HOH   635  2035 931  HOH   HOH A . 
CA 11 HOH   636  2036 577  HOH   HOH A . 
CA 11 HOH   637  2037 1042 HOH   HOH A . 
CA 11 HOH   638  2038 1683 HOH   HOH A . 
CA 11 HOH   639  2039 3303 HOH   HOH A . 
CA 11 HOH   640  2040 983  HOH   HOH A . 
CA 11 HOH   641  2041 511  HOH   HOH A . 
CA 11 HOH   642  2042 1116 HOH   HOH A . 
CA 11 HOH   643  2043 1580 HOH   HOH A . 
CA 11 HOH   644  2044 866  HOH   HOH A . 
CA 11 HOH   645  2045 775  HOH   HOH A . 
CA 11 HOH   646  2046 796  HOH   HOH A . 
CA 11 HOH   647  2047 1527 HOH   HOH A . 
CA 11 HOH   648  2048 730  HOH   HOH A . 
CA 11 HOH   649  2049 1436 HOH   HOH A . 
CA 11 HOH   650  2050 644  HOH   HOH A . 
CA 11 HOH   651  2051 1677 HOH   HOH A . 
CA 11 HOH   652  2052 612  HOH   HOH A . 
CA 11 HOH   653  2053 252  HOH   HOH A . 
CA 11 HOH   654  2054 1869 HOH   HOH A . 
CA 11 HOH   655  2055 274  HOH   HOH A . 
CA 11 HOH   656  2056 574  HOH   HOH A . 
CA 11 HOH   657  2057 1903 HOH   HOH A . 
CA 11 HOH   658  2058 3149 HOH   HOH A . 
CA 11 HOH   659  2059 501  HOH   HOH A . 
CA 11 HOH   660  2060 3398 HOH   HOH A . 
CA 11 HOH   661  2061 290  HOH   HOH A . 
CA 11 HOH   662  2062 1538 HOH   HOH A . 
CA 11 HOH   663  2063 416  HOH   HOH A . 
CA 11 HOH   664  2064 1309 HOH   HOH A . 
CA 11 HOH   665  2065 1193 HOH   HOH A . 
CA 11 HOH   666  2066 210  HOH   HOH A . 
CA 11 HOH   667  2067 595  HOH   HOH A . 
CA 11 HOH   668  2068 3511 HOH   HOH A . 
CA 11 HOH   669  2069 3031 HOH   HOH A . 
CA 11 HOH   670  2070 637  HOH   HOH A . 
CA 11 HOH   671  2071 598  HOH   HOH A . 
CA 11 HOH   672  2072 1323 HOH   HOH A . 
CA 11 HOH   673  2073 470  HOH   HOH A . 
CA 11 HOH   674  2074 764  HOH   HOH A . 
CA 11 HOH   675  2075 396  HOH   HOH A . 
CA 11 HOH   676  2076 1842 HOH   HOH A . 
CA 11 HOH   677  2077 3356 HOH   HOH A . 
CA 11 HOH   678  2078 1872 HOH   HOH A . 
CA 11 HOH   679  2079 1965 HOH   HOH A . 
CA 11 HOH   680  2080 481  HOH   HOH A . 
CA 11 HOH   681  2081 478  HOH   HOH A . 
CA 11 HOH   682  2082 1599 HOH   HOH A . 
CA 11 HOH   683  2083 246  HOH   HOH A . 
CA 11 HOH   684  2084 2036 HOH   HOH A . 
CA 11 HOH   685  2085 119  HOH   HOH A . 
CA 11 HOH   686  2086 485  HOH   HOH A . 
CA 11 HOH   687  2087 663  HOH   HOH A . 
CA 11 HOH   688  2088 2046 HOH   HOH A . 
CA 11 HOH   689  2089 347  HOH   HOH A . 
CA 11 HOH   690  2090 1228 HOH   HOH A . 
CA 11 HOH   691  2091 1744 HOH   HOH A . 
CA 11 HOH   692  2092 961  HOH   HOH A . 
CA 11 HOH   693  2093 58   HOH   HOH A . 
CA 11 HOH   694  2094 1130 HOH   HOH A . 
CA 11 HOH   695  2095 992  HOH   HOH A . 
CA 11 HOH   696  2096 1244 HOH   HOH A . 
CA 11 HOH   697  2097 53   HOH   HOH A . 
CA 11 HOH   698  2098 1096 HOH   HOH A . 
CA 11 HOH   699  2099 1156 HOH   HOH A . 
CA 11 HOH   700  2100 889  HOH   HOH A . 
CA 11 HOH   701  2101 3371 HOH   HOH A . 
CA 11 HOH   702  2102 3272 HOH   HOH A . 
CA 11 HOH   703  2103 1330 HOH   HOH A . 
CA 11 HOH   704  2104 1191 HOH   HOH A . 
CA 11 HOH   705  2105 1899 HOH   HOH A . 
CA 11 HOH   706  2106 3100 HOH   HOH A . 
CA 11 HOH   707  2107 391  HOH   HOH A . 
CA 11 HOH   708  2108 1494 HOH   HOH A . 
CA 11 HOH   709  2109 1983 HOH   HOH A . 
CA 11 HOH   710  2110 1536 HOH   HOH A . 
CA 11 HOH   711  2111 1039 HOH   HOH A . 
CA 11 HOH   712  2112 3138 HOH   HOH A . 
CA 11 HOH   713  2113 1057 HOH   HOH A . 
CA 11 HOH   714  2114 795  HOH   HOH A . 
CA 11 HOH   715  2115 915  HOH   HOH A . 
CA 11 HOH   716  2116 943  HOH   HOH A . 
CA 11 HOH   717  2117 819  HOH   HOH A . 
CA 11 HOH   718  2118 1272 HOH   HOH A . 
CA 11 HOH   719  2119 211  HOH   HOH A . 
CA 11 HOH   720  2120 426  HOH   HOH A . 
CA 11 HOH   721  2121 876  HOH   HOH A . 
CA 11 HOH   722  2122 1833 HOH   HOH A . 
CA 11 HOH   723  2123 1476 HOH   HOH A . 
CA 11 HOH   724  2124 1386 HOH   HOH A . 
CA 11 HOH   725  2125 1750 HOH   HOH A . 
CA 11 HOH   726  2126 1339 HOH   HOH A . 
CA 11 HOH   727  2127 1927 HOH   HOH A . 
CA 11 HOH   728  2128 1451 HOH   HOH A . 
CA 11 HOH   729  2129 1259 HOH   HOH A . 
CA 11 HOH   730  2130 3281 HOH   HOH A . 
CA 11 HOH   731  2131 287  HOH   HOH A . 
CA 11 HOH   732  2132 235  HOH   HOH A . 
CA 11 HOH   733  2133 299  HOH   HOH A . 
CA 11 HOH   734  2134 228  HOH   HOH A . 
CA 11 HOH   735  2135 696  HOH   HOH A . 
CA 11 HOH   736  2136 3352 HOH   HOH A . 
CA 11 HOH   737  2137 913  HOH   HOH A . 
CA 11 HOH   738  2138 1097 HOH   HOH A . 
CA 11 HOH   739  2139 626  HOH   HOH A . 
CA 11 HOH   740  2140 238  HOH   HOH A . 
CA 11 HOH   741  2141 1187 HOH   HOH A . 
CA 11 HOH   742  2142 3450 HOH   HOH A . 
CA 11 HOH   743  2143 912  HOH   HOH A . 
CA 11 HOH   744  2144 934  HOH   HOH A . 
CA 11 HOH   745  2145 3172 HOH   HOH A . 
CA 11 HOH   746  2146 995  HOH   HOH A . 
CA 11 HOH   747  2147 844  HOH   HOH A . 
CA 11 HOH   748  2148 1532 HOH   HOH A . 
CA 11 HOH   749  2149 442  HOH   HOH A . 
CA 11 HOH   750  2150 1484 HOH   HOH A . 
CA 11 HOH   751  2151 309  HOH   HOH A . 
CA 11 HOH   752  2152 1184 HOH   HOH A . 
CA 11 HOH   753  2153 1515 HOH   HOH A . 
CA 11 HOH   754  2154 1694 HOH   HOH A . 
CA 11 HOH   755  2155 817  HOH   HOH A . 
CA 11 HOH   756  2156 3029 HOH   HOH A . 
CA 11 HOH   757  2157 1922 HOH   HOH A . 
CA 11 HOH   758  2158 1150 HOH   HOH A . 
CA 11 HOH   759  2159 3519 HOH   HOH A . 
CA 11 HOH   760  2160 821  HOH   HOH A . 
CA 11 HOH   761  2161 1512 HOH   HOH A . 
CA 11 HOH   762  2162 1017 HOH   HOH A . 
CA 11 HOH   763  2163 1915 HOH   HOH A . 
CA 11 HOH   764  2164 760  HOH   HOH A . 
CA 11 HOH   765  2165 390  HOH   HOH A . 
CA 11 HOH   766  2166 1856 HOH   HOH A . 
CA 11 HOH   767  2167 3159 HOH   HOH A . 
CA 11 HOH   768  2168 994  HOH   HOH A . 
CA 11 HOH   769  2169 3444 HOH   HOH A . 
CA 11 HOH   770  2170 3589 HOH   HOH A . 
CA 11 HOH   771  2171 3558 HOH   HOH A . 
CA 11 HOH   772  2172 743  HOH   HOH A . 
CA 11 HOH   773  2173 633  HOH   HOH A . 
CA 11 HOH   774  2174 1788 HOH   HOH A . 
CA 11 HOH   775  2175 1168 HOH   HOH A . 
CA 11 HOH   776  2176 1751 HOH   HOH A . 
CA 11 HOH   777  2177 345  HOH   HOH A . 
CA 11 HOH   778  2178 1972 HOH   HOH A . 
CA 11 HOH   779  2179 1664 HOH   HOH A . 
CA 11 HOH   780  2180 3430 HOH   HOH A . 
CA 11 HOH   781  2181 3412 HOH   HOH A . 
CA 11 HOH   782  2182 2058 HOH   HOH A . 
CA 11 HOH   783  2183 3094 HOH   HOH A . 
CA 11 HOH   784  2184 797  HOH   HOH A . 
CA 11 HOH   785  2185 453  HOH   HOH A . 
CA 11 HOH   786  2186 3252 HOH   HOH A . 
CA 11 HOH   787  2187 353  HOH   HOH A . 
CA 11 HOH   788  2188 1269 HOH   HOH A . 
CA 11 HOH   789  2189 886  HOH   HOH A . 
CA 11 HOH   790  2190 3036 HOH   HOH A . 
CA 11 HOH   791  2191 1354 HOH   HOH A . 
CA 11 HOH   792  2192 1591 HOH   HOH A . 
CA 11 HOH   793  2193 1384 HOH   HOH A . 
CA 11 HOH   794  2194 260  HOH   HOH A . 
CA 11 HOH   795  2195 1592 HOH   HOH A . 
CA 11 HOH   796  2196 1314 HOH   HOH A . 
CA 11 HOH   797  2197 905  HOH   HOH A . 
CA 11 HOH   798  2198 3374 HOH   HOH A . 
CA 11 HOH   799  2199 1415 HOH   HOH A . 
CA 11 HOH   800  2200 713  HOH   HOH A . 
CA 11 HOH   801  2201 1142 HOH   HOH A . 
CA 11 HOH   802  2202 441  HOH   HOH A . 
CA 11 HOH   803  2203 809  HOH   HOH A . 
CA 11 HOH   804  2204 410  HOH   HOH A . 
CA 11 HOH   805  2205 1087 HOH   HOH A . 
CA 11 HOH   806  2206 1710 HOH   HOH A . 
CA 11 HOH   807  2207 3605 HOH   HOH A . 
CA 11 HOH   808  2208 3126 HOH   HOH A . 
CA 11 HOH   809  2209 1717 HOH   HOH A . 
CA 11 HOH   810  2210 3041 HOH   HOH A . 
CA 11 HOH   811  2211 455  HOH   HOH A . 
CA 11 HOH   812  2212 805  HOH   HOH A . 
CA 11 HOH   813  2213 731  HOH   HOH A . 
CA 11 HOH   814  2214 1979 HOH   HOH A . 
CA 11 HOH   815  2215 161  HOH   HOH A . 
CA 11 HOH   816  2216 138  HOH   HOH A . 
CA 11 HOH   817  2217 1936 HOH   HOH A . 
CA 11 HOH   818  2218 1590 HOH   HOH A . 
CA 11 HOH   819  2219 3206 HOH   HOH A . 
CA 11 HOH   820  2220 1293 HOH   HOH A . 
CA 11 HOH   821  2221 3104 HOH   HOH A . 
CA 11 HOH   822  2222 44   HOH   HOH A . 
CA 11 HOH   823  2223 528  HOH   HOH A . 
CA 11 HOH   824  2224 1065 HOH   HOH A . 
CA 11 HOH   825  2225 1830 HOH   HOH A . 
CA 11 HOH   826  2226 1549 HOH   HOH A . 
CA 11 HOH   827  2227 1589 HOH   HOH A . 
CA 11 HOH   828  2228 3155 HOH   HOH A . 
CA 11 HOH   829  2229 495  HOH   HOH A . 
CA 11 HOH   830  2230 1438 HOH   HOH A . 
CA 11 HOH   831  2231 198  HOH   HOH A . 
CA 11 HOH   832  2232 2032 HOH   HOH A . 
CA 11 HOH   833  2233 996  HOH   HOH A . 
CA 11 HOH   834  2234 1908 HOH   HOH A . 
CA 11 HOH   835  2235 1696 HOH   HOH A . 
CA 11 HOH   836  2236 221  HOH   HOH A . 
CA 11 HOH   837  2237 879  HOH   HOH A . 
CA 11 HOH   838  2238 3442 HOH   HOH A . 
CA 11 HOH   839  2239 1631 HOH   HOH A . 
CA 11 HOH   840  2240 1128 HOH   HOH A . 
CA 11 HOH   841  2241 1650 HOH   HOH A . 
CA 11 HOH   842  2242 3068 HOH   HOH A . 
CA 11 HOH   843  2243 467  HOH   HOH A . 
CA 11 HOH   844  2244 3472 HOH   HOH A . 
CA 11 HOH   845  2245 1540 HOH   HOH A . 
CA 11 HOH   846  2246 50   HOH   HOH A . 
CA 11 HOH   847  2247 1248 HOH   HOH A . 
CA 11 HOH   848  2248 1119 HOH   HOH A . 
CA 11 HOH   849  2249 585  HOH   HOH A . 
CA 11 HOH   850  2250 3025 HOH   HOH A . 
CA 11 HOH   851  2251 1516 HOH   HOH A . 
CA 11 HOH   852  2252 356  HOH   HOH A . 
CA 11 HOH   853  2253 3360 HOH   HOH A . 
CA 11 HOH   854  2254 1797 HOH   HOH A . 
CA 11 HOH   855  2255 3522 HOH   HOH A . 
CA 11 HOH   856  2256 578  HOH   HOH A . 
CA 11 HOH   857  2257 3198 HOH   HOH A . 
CA 11 HOH   858  2258 739  HOH   HOH A . 
CA 11 HOH   859  2259 3111 HOH   HOH A . 
CA 11 HOH   860  2260 1338 HOH   HOH A . 
CA 11 HOH   861  2261 3416 HOH   HOH A . 
CA 11 HOH   862  2262 148  HOH   HOH A . 
CA 11 HOH   863  2263 1611 HOH   HOH A . 
CA 11 HOH   864  2264 3458 HOH   HOH A . 
CA 11 HOH   865  2265 3134 HOH   HOH A . 
CA 11 HOH   866  2266 1107 HOH   HOH A . 
CA 11 HOH   867  2267 820  HOH   HOH A . 
CA 11 HOH   868  2268 3410 HOH   HOH A . 
CA 11 HOH   869  2269 536  HOH   HOH A . 
CA 11 HOH   870  2270 1247 HOH   HOH A . 
CA 11 HOH   871  2271 1798 HOH   HOH A . 
CA 11 HOH   872  2272 1241 HOH   HOH A . 
CA 11 HOH   873  2273 1868 HOH   HOH A . 
CA 11 HOH   874  2274 3476 HOH   HOH A . 
CA 11 HOH   875  2275 1032 HOH   HOH A . 
CA 11 HOH   876  2276 3027 HOH   HOH A . 
CA 11 HOH   877  2277 1242 HOH   HOH A . 
CA 11 HOH   878  2278 3213 HOH   HOH A . 
CA 11 HOH   879  2279 1200 HOH   HOH A . 
CA 11 HOH   880  2280 1557 HOH   HOH A . 
CA 11 HOH   881  2281 1973 HOH   HOH A . 
CA 11 HOH   882  2282 3275 HOH   HOH A . 
CA 11 HOH   883  2283 1880 HOH   HOH A . 
CA 11 HOH   884  2284 3006 HOH   HOH A . 
CA 11 HOH   885  2285 1575 HOH   HOH A . 
CA 11 HOH   886  2286 863  HOH   HOH A . 
CA 11 HOH   887  2287 652  HOH   HOH A . 
CA 11 HOH   888  2288 3309 HOH   HOH A . 
CA 11 HOH   889  2289 1803 HOH   HOH A . 
CA 11 HOH   890  2290 3229 HOH   HOH A . 
CA 11 HOH   891  2291 3048 HOH   HOH A . 
CA 11 HOH   892  2292 1313 HOH   HOH A . 
CA 11 HOH   893  2293 567  HOH   HOH A . 
CA 11 HOH   894  2294 3131 HOH   HOH A . 
CA 11 HOH   895  2295 703  HOH   HOH A . 
CA 11 HOH   896  2296 3114 HOH   HOH A . 
CA 11 HOH   897  2297 3023 HOH   HOH A . 
CA 11 HOH   898  2298 1431 HOH   HOH A . 
CA 11 HOH   899  2299 1008 HOH   HOH A . 
CA 11 HOH   900  2300 1477 HOH   HOH A . 
CA 11 HOH   901  2301 1089 HOH   HOH A . 
CA 11 HOH   902  2302 1687 HOH   HOH A . 
CA 11 HOH   903  2303 3102 HOH   HOH A . 
CA 11 HOH   904  2304 3262 HOH   HOH A . 
CA 11 HOH   905  2305 1118 HOH   HOH A . 
CA 11 HOH   906  2306 3140 HOH   HOH A . 
CA 11 HOH   907  2307 3391 HOH   HOH A . 
CA 11 HOH   908  2308 1766 HOH   HOH A . 
CA 11 HOH   909  2309 3273 HOH   HOH A . 
CA 11 HOH   910  2310 1302 HOH   HOH A . 
CA 11 HOH   911  2311 3209 HOH   HOH A . 
CA 11 HOH   912  2312 3354 HOH   HOH A . 
CA 11 HOH   913  2313 1519 HOH   HOH A . 
CA 11 HOH   914  2314 1563 HOH   HOH A . 
CA 11 HOH   915  2315 3433 HOH   HOH A . 
CA 11 HOH   916  2316 3496 HOH   HOH A . 
CA 11 HOH   917  2317 3370 HOH   HOH A . 
CA 11 HOH   918  2318 1094 HOH   HOH A . 
CA 11 HOH   919  2319 3421 HOH   HOH A . 
CA 11 HOH   920  2320 3254 HOH   HOH A . 
CA 11 HOH   921  2321 3113 HOH   HOH A . 
CA 11 HOH   922  2322 1478 HOH   HOH A . 
CA 11 HOH   923  2323 3286 HOH   HOH A . 
CA 11 HOH   924  2324 849  HOH   HOH A . 
CA 11 HOH   925  2325 3124 HOH   HOH A . 
CA 11 HOH   926  2326 3028 HOH   HOH A . 
CA 11 HOH   927  2327 1658 HOH   HOH A . 
CA 11 HOH   928  2328 904  HOH   HOH A . 
CA 11 HOH   929  2329 3105 HOH   HOH A . 
CA 11 HOH   930  2330 3571 HOH   HOH A . 
CA 11 HOH   931  2331 1047 HOH   HOH A . 
CA 11 HOH   932  2332 1769 HOH   HOH A . 
CA 11 HOH   933  2333 1617 HOH   HOH A . 
CA 11 HOH   934  2334 951  HOH   HOH A . 
CA 11 HOH   935  2335 3205 HOH   HOH A . 
CA 11 HOH   936  2336 3144 HOH   HOH A . 
CA 11 HOH   937  2337 1133 HOH   HOH A . 
CA 11 HOH   938  2338 3308 HOH   HOH A . 
CA 11 HOH   939  2339 653  HOH   HOH A . 
CA 11 HOH   940  2340 451  HOH   HOH A . 
CA 11 HOH   941  2341 3233 HOH   HOH A . 
CA 11 HOH   942  2342 3294 HOH   HOH A . 
CA 11 HOH   943  2343 3156 HOH   HOH A . 
CA 11 HOH   944  2344 3445 HOH   HOH A . 
CA 11 HOH   945  2345 1045 HOH   HOH A . 
CA 11 HOH   946  2346 3162 HOH   HOH A . 
CA 11 HOH   947  2347 3282 HOH   HOH A . 
CA 11 HOH   948  2348 2051 HOH   HOH A . 
CA 11 HOH   949  2349 3401 HOH   HOH A . 
CA 11 HOH   950  2350 3598 HOH   HOH A . 
CA 11 HOH   951  2351 1772 HOH   HOH A . 
CA 11 HOH   952  2352 1003 HOH   HOH A . 
CA 11 HOH   953  2353 3414 HOH   HOH A . 
CA 11 HOH   954  2354 3379 HOH   HOH A . 
CA 11 HOH   955  2355 3531 HOH   HOH A . 
CA 11 HOH   956  2356 3158 HOH   HOH A . 
CA 11 HOH   957  2357 922  HOH   HOH A . 
CA 11 HOH   958  2358 2033 HOH   HOH A . 
CA 11 HOH   959  2359 3486 HOH   HOH A . 
CA 11 HOH   960  2360 1955 HOH   HOH A . 
CA 11 HOH   961  2361 3170 HOH   HOH A . 
CA 11 HOH   962  2362 3570 HOH   HOH A . 
CA 11 HOH   963  2363 1754 HOH   HOH A . 
CA 11 HOH   964  2364 3395 HOH   HOH A . 
CA 11 HOH   965  2365 1427 HOH   HOH A . 
CA 11 HOH   966  2366 1759 HOH   HOH A . 
CA 11 HOH   967  2367 1594 HOH   HOH A . 
CA 11 HOH   968  2368 964  HOH   HOH A . 
CA 11 HOH   969  2369 1493 HOH   HOH A . 
CA 11 HOH   970  2370 3081 HOH   HOH A . 
CA 11 HOH   971  2371 3491 HOH   HOH A . 
CA 11 HOH   972  2372 3153 HOH   HOH A . 
CA 11 HOH   973  2373 3426 HOH   HOH A . 
CA 11 HOH   974  2374 3390 HOH   HOH A . 
CA 11 HOH   975  2375 1174 HOH   HOH A . 
CA 11 HOH   976  2376 3251 HOH   HOH A . 
CA 11 HOH   977  2377 3147 HOH   HOH A . 
CA 11 HOH   978  2378 3411 HOH   HOH A . 
CA 11 HOH   979  2379 3490 HOH   HOH A . 
CA 11 HOH   980  2380 1223 HOH   HOH A . 
CA 11 HOH   981  2381 1916 HOH   HOH A . 
CA 11 HOH   982  2382 3035 HOH   HOH A . 
CA 11 HOH   983  2383 1919 HOH   HOH A . 
CA 11 HOH   984  2384 1099 HOH   HOH A . 
CA 11 HOH   985  2385 1704 HOH   HOH A . 
CA 11 HOH   986  2386 1132 HOH   HOH A . 
CA 11 HOH   987  2387 3146 HOH   HOH A . 
CA 11 HOH   988  2388 971  HOH   HOH A . 
CA 11 HOH   989  2389 576  HOH   HOH A . 
CA 11 HOH   990  2390 1018 HOH   HOH A . 
CA 11 HOH   991  2391 3259 HOH   HOH A . 
CA 11 HOH   992  2392 3474 HOH   HOH A . 
CA 11 HOH   993  2393 3457 HOH   HOH A . 
CA 11 HOH   994  2394 1192 HOH   HOH A . 
CA 11 HOH   995  2395 1938 HOH   HOH A . 
CA 11 HOH   996  2396 3339 HOH   HOH A . 
CA 11 HOH   997  2397 3572 HOH   HOH A . 
CA 11 HOH   998  2398 831  HOH   HOH A . 
CA 11 HOH   999  2399 1691 HOH   HOH A . 
CA 11 HOH   1000 2400 955  HOH   HOH A . 
CA 11 HOH   1001 2401 1407 HOH   HOH A . 
CA 11 HOH   1002 2402 2052 HOH   HOH A . 
CA 11 HOH   1003 2403 698  HOH   HOH A . 
CA 11 HOH   1004 2404 1387 HOH   HOH A . 
CA 11 HOH   1005 2405 1917 HOH   HOH A . 
CA 11 HOH   1006 2406 1401 HOH   HOH A . 
CA 11 HOH   1007 2407 1728 HOH   HOH A . 
CA 11 HOH   1008 2408 1442 HOH   HOH A . 
CA 11 HOH   1009 2409 1277 HOH   HOH A . 
CA 11 HOH   1010 2410 2008 HOH   HOH A . 
CA 11 HOH   1011 2411 1962 HOH   HOH A . 
CA 11 HOH   1012 2412 3223 HOH   HOH A . 
CA 11 HOH   1013 2413 1560 HOH   HOH A . 
CA 11 HOH   1014 2414 3455 HOH   HOH A . 
CA 11 HOH   1015 2415 1966 HOH   HOH A . 
CA 11 HOH   1016 2416 1956 HOH   HOH A . 
CA 11 HOH   1017 2417 3197 HOH   HOH A . 
CA 11 HOH   1018 2418 2014 HOH   HOH A . 
CA 11 HOH   1019 2419 702  HOH   HOH A . 
CA 11 HOH   1020 2420 1558 HOH   HOH A . 
CA 11 HOH   1021 2421 1964 HOH   HOH A . 
CA 11 HOH   1022 2422 3301 HOH   HOH A . 
CA 11 HOH   1023 2423 3169 HOH   HOH A . 
CA 11 HOH   1024 2424 1459 HOH   HOH A . 
CA 11 HOH   1025 2425 1030 HOH   HOH A . 
CA 11 HOH   1026 2426 1215 HOH   HOH A . 
CA 11 HOH   1027 2427 3283 HOH   HOH A . 
CA 11 HOH   1028 2428 3244 HOH   HOH A . 
CA 11 HOH   1029 2429 1632 HOH   HOH A . 
CA 11 HOH   1030 2430 865  HOH   HOH A . 
CA 11 HOH   1031 2431 3508 HOH   HOH A . 
CA 11 HOH   1032 2432 3019 HOH   HOH A . 
CA 11 HOH   1033 2433 3403 HOH   HOH A . 
CA 11 HOH   1034 2434 1756 HOH   HOH A . 
CA 11 HOH   1035 2435 1547 HOH   HOH A . 
CA 11 HOH   1036 2436 3599 HOH   HOH A . 
CA 11 HOH   1037 2437 993  HOH   HOH A . 
CA 11 HOH   1038 2438 3604 HOH   HOH A . 
CA 11 HOH   1039 2439 3136 HOH   HOH A . 
CA 11 HOH   1040 2440 1894 HOH   HOH A . 
CA 11 HOH   1041 2441 3515 HOH   HOH A . 
CA 11 HOH   1042 2442 1319 HOH   HOH A . 
CA 11 HOH   1043 2443 2017 HOH   HOH A . 
CA 11 HOH   1044 2444 929  HOH   HOH A . 
CA 11 HOH   1045 2445 3115 HOH   HOH A . 
CA 11 HOH   1046 2446 1873 HOH   HOH A . 
CA 11 HOH   1047 2447 3533 HOH   HOH A . 
CA 11 HOH   1048 2448 1328 HOH   HOH A . 
CA 11 HOH   1049 2449 1649 HOH   HOH A . 
CA 11 HOH   1050 2450 1783 HOH   HOH A . 
CA 11 HOH   1051 2451 1605 HOH   HOH A . 
CA 11 HOH   1052 2452 3130 HOH   HOH A . 
CA 11 HOH   1053 2453 1335 HOH   HOH A . 
CA 11 HOH   1054 2454 3480 HOH   HOH A . 
CA 11 HOH   1055 2455 611  HOH   HOH A . 
CA 11 HOH   1056 2456 1267 HOH   HOH A . 
CA 11 HOH   1057 2457 1930 HOH   HOH A . 
CA 11 HOH   1058 2458 1289 HOH   HOH A . 
CA 11 HOH   1059 2459 3557 HOH   HOH A . 
CA 11 HOH   1060 2460 1207 HOH   HOH A . 
CA 11 HOH   1061 2461 3544 HOH   HOH A . 
CA 11 HOH   1062 2462 1603 HOH   HOH A . 
CA 11 HOH   1063 2463 237  HOH   HOH A . 
CA 11 HOH   1064 2464 1072 HOH   HOH A . 
CA 11 HOH   1065 2465 3098 HOH   HOH A . 
CA 11 HOH   1066 2466 3530 HOH   HOH A . 
CA 11 HOH   1067 2467 3221 HOH   HOH A . 
CA 11 HOH   1068 2468 307  HOH   HOH A . 
CA 11 HOH   1069 2469 1781 HOH   HOH A . 
CA 11 HOH   1070 2470 1454 HOH   HOH A . 
CA 11 HOH   1071 2471 3242 HOH   HOH A . 
CA 11 HOH   1072 2472 3326 HOH   HOH A . 
CA 11 HOH   1073 2473 3584 HOH   HOH A . 
CA 11 HOH   1074 2474 2041 HOH   HOH A . 
CA 11 HOH   1075 2475 1695 HOH   HOH A . 
CA 11 HOH   1076 2476 1724 HOH   HOH A . 
CA 11 HOH   1077 2477 3295 HOH   HOH A . 
CA 11 HOH   1078 2478 1492 HOH   HOH A . 
CA 11 HOH   1079 2479 3493 HOH   HOH A . 
CA 11 HOH   1080 2480 1366 HOH   HOH A . 
CA 11 HOH   1081 2481 3541 HOH   HOH A . 
CA 11 HOH   1082 2482 1158 HOH   HOH A . 
CA 11 HOH   1083 2483 2004 HOH   HOH A . 
CA 11 HOH   1084 2484 1310 HOH   HOH A . 
CA 11 HOH   1085 2485 3378 HOH   HOH A . 
CA 11 HOH   1086 2486 2057 HOH   HOH A . 
CA 11 HOH   1087 2487 1504 HOH   HOH A . 
CA 11 HOH   1088 2488 583  HOH   HOH A . 
CA 11 HOH   1089 2489 3583 HOH   HOH A . 
CA 11 HOH   1090 2490 1573 HOH   HOH A . 
CA 11 HOH   1091 2491 3045 HOH   HOH A . 
CA 11 HOH   1092 2492 1705 HOH   HOH A . 
CA 11 HOH   1093 2493 2061 HOH   HOH A . 
CA 11 HOH   1094 2494 1148 HOH   HOH A . 
CA 11 HOH   1095 2495 3210 HOH   HOH A . 
CA 11 HOH   1096 2496 3016 HOH   HOH A . 
CA 11 HOH   1097 2497 1525 HOH   HOH A . 
CA 11 HOH   1098 2498 3261 HOH   HOH A . 
CA 11 HOH   1099 2499 3050 HOH   HOH A . 
CA 11 HOH   1100 2500 1854 HOH   HOH A . 
CA 11 HOH   1101 2501 1151 HOH   HOH A . 
CA 11 HOH   1102 2502 959  HOH   HOH A . 
CA 11 HOH   1103 2503 3299 HOH   HOH A . 
CA 11 HOH   1104 2504 3009 HOH   HOH A . 
CA 11 HOH   1105 2505 554  HOH   HOH A . 
CA 11 HOH   1106 2506 3577 HOH   HOH A . 
CA 11 HOH   1107 2507 1161 HOH   HOH A . 
CA 11 HOH   1108 2508 3230 HOH   HOH A . 
CA 11 HOH   1109 2509 1950 HOH   HOH A . 
CA 11 HOH   1110 2510 1511 HOH   HOH A . 
CA 11 HOH   1111 2511 1618 HOH   HOH A . 
CA 11 HOH   1112 2512 3200 HOH   HOH A . 
CA 11 HOH   1113 2513 1774 HOH   HOH A . 
CA 11 HOH   1114 2514 3485 HOH   HOH A . 
CA 11 HOH   1115 2515 1838 HOH   HOH A . 
CA 11 HOH   1116 2516 1342 HOH   HOH A . 
CA 11 HOH   1117 2517 1896 HOH   HOH A . 
CA 11 HOH   1118 2518 3296 HOH   HOH A . 
CA 11 HOH   1119 2519 3548 HOH   HOH A . 
CA 11 HOH   1120 2520 1035 HOH   HOH A . 
CA 11 HOH   1121 2521 954  HOH   HOH A . 
CA 11 HOH   1122 2522 3556 HOH   HOH A . 
CA 11 HOH   1123 2523 1928 HOH   HOH A . 
CA 11 HOH   1124 2524 1852 HOH   HOH A . 
CA 11 HOH   1125 2525 1593 HOH   HOH A . 
CA 11 HOH   1126 2526 917  HOH   HOH A . 
CA 11 HOH   1127 2527 3525 HOH   HOH A . 
CA 11 HOH   1128 2528 3290 HOH   HOH A . 
CA 11 HOH   1129 2529 3274 HOH   HOH A . 
CA 11 HOH   1130 2530 1951 HOH   HOH A . 
CA 11 HOH   1131 2531 3298 HOH   HOH A . 
CA 11 HOH   1132 2532 1729 HOH   HOH A . 
CA 11 HOH   1133 2533 722  HOH   HOH A . 
CA 11 HOH   1134 2534 3224 HOH   HOH A . 
CA 11 HOH   1135 2535 3083 HOH   HOH A . 
CA 11 HOH   1136 2536 3488 HOH   HOH A . 
CA 11 HOH   1137 2537 1996 HOH   HOH A . 
CA 11 HOH   1138 2538 3258 HOH   HOH A . 
CA 11 HOH   1139 2539 1434 HOH   HOH A . 
CA 11 HOH   1140 2540 1848 HOH   HOH A . 
CA 11 HOH   1141 2541 407  HOH   HOH A . 
CA 11 HOH   1142 2542 3310 HOH   HOH A . 
CA 11 HOH   1143 2543 894  HOH   HOH A . 
CA 11 HOH   1144 2544 3154 HOH   HOH A . 
CA 11 HOH   1145 2545 953  HOH   HOH A . 
CA 11 HOH   1146 2546 3524 HOH   HOH A . 
CA 11 HOH   1147 2547 874  HOH   HOH A . 
CA 11 HOH   1148 2548 1214 HOH   HOH A . 
CA 11 HOH   1149 2549 3353 HOH   HOH A . 
CA 11 HOH   1150 2550 1568 HOH   HOH A . 
CA 11 HOH   1151 2551 3300 HOH   HOH A . 
CA 11 HOH   1152 2552 1470 HOH   HOH A . 
CA 11 HOH   1153 2553 1445 HOH   HOH A . 
CA 11 HOH   1154 2554 3546 HOH   HOH A . 
CA 11 HOH   1155 2555 3163 HOH   HOH A . 
CA 11 HOH   1156 2556 1877 HOH   HOH A . 
CA 11 HOH   1157 2557 1506 HOH   HOH A . 
CA 11 HOH   1158 2558 3040 HOH   HOH A . 
CA 11 HOH   1159 2559 2040 HOH   HOH A . 
CA 11 HOH   1160 2560 1970 HOH   HOH A . 
CA 11 HOH   1161 2561 3369 HOH   HOH A . 
CA 11 HOH   1162 2562 3459 HOH   HOH A . 
CA 11 HOH   1163 2563 792  HOH   HOH A . 
CA 11 HOH   1164 2564 1055 HOH   HOH A . 
CA 11 HOH   1165 2565 1412 HOH   HOH A . 
CA 11 HOH   1166 2566 406  HOH   HOH A . 
CA 11 HOH   1167 2567 1188 HOH   HOH A . 
CA 11 HOH   1168 2568 1280 HOH   HOH A . 
CA 11 HOH   1169 2569 1981 HOH   HOH A . 
CA 11 HOH   1170 2570 1550 HOH   HOH A . 
CA 11 HOH   1171 2571 3287 HOH   HOH A . 
CA 11 HOH   1172 2572 3574 HOH   HOH A . 
CA 11 HOH   1173 2573 3534 HOH   HOH A . 
CA 11 HOH   1174 2574 3225 HOH   HOH A . 
CA 11 HOH   1175 2575 1553 HOH   HOH A . 
CA 11 HOH   1176 2576 987  HOH   HOH A . 
CA 11 HOH   1177 2577 3529 HOH   HOH A . 
CA 11 HOH   1178 2578 1002 HOH   HOH A . 
CA 11 HOH   1179 2579 3380 HOH   HOH A . 
CA 11 HOH   1180 2580 3271 HOH   HOH A . 
CA 11 HOH   1181 2581 3362 HOH   HOH A . 
CA 11 HOH   1182 2582 3137 HOH   HOH A . 
CA 11 HOH   1183 2583 1179 HOH   HOH A . 
CA 11 HOH   1184 2584 1674 HOH   HOH A . 
CA 11 HOH   1185 2585 3289 HOH   HOH A . 
CA 11 HOH   1186 2586 1634 HOH   HOH A . 
CA 11 HOH   1187 2587 1810 HOH   HOH A . 
CA 11 HOH   1188 2588 1355 HOH   HOH A . 
CA 11 HOH   1189 2589 2029 HOH   HOH A . 
CA 11 HOH   1190 2590 1582 HOH   HOH A . 
CA 11 HOH   1191 2591 691  HOH   HOH A . 
CA 11 HOH   1192 2592 1571 HOH   HOH A . 
CA 11 HOH   1193 2593 3288 HOH   HOH A . 
CA 11 HOH   1194 2594 3139 HOH   HOH A . 
CA 11 HOH   1195 2595 1231 HOH   HOH A . 
CA 11 HOH   1196 2596 1023 HOH   HOH A . 
CA 11 HOH   1197 2597 1804 HOH   HOH A . 
CA 11 HOH   1198 2598 3368 HOH   HOH A . 
CA 11 HOH   1199 2599 1409 HOH   HOH A . 
CA 11 HOH   1200 2600 3602 HOH   HOH A . 
CA 11 HOH   1201 2601 3211 HOH   HOH A . 
CA 11 HOH   1202 2602 3315 HOH   HOH A . 
CA 11 HOH   1203 2603 3336 HOH   HOH A . 
CA 11 HOH   1204 2604 2002 HOH   HOH A . 
CA 11 HOH   1205 2605 1262 HOH   HOH A . 
CA 11 HOH   1206 2606 1140 HOH   HOH A . 
CA 11 HOH   1207 2607 3164 HOH   HOH A . 
CA 11 HOH   1208 2608 1893 HOH   HOH A . 
CA 11 HOH   1209 2609 3037 HOH   HOH A . 
CA 11 HOH   1210 2610 1878 HOH   HOH A . 
CA 11 HOH   1211 2611 706  HOH   HOH A . 
CA 11 HOH   1212 2612 1676 HOH   HOH A . 
CA 11 HOH   1213 2613 1815 HOH   HOH A . 
CA 11 HOH   1214 2614 1081 HOH   HOH A . 
CA 11 HOH   1215 2615 1707 HOH   HOH A . 
CA 11 HOH   1216 2616 1672 HOH   HOH A . 
CA 11 HOH   1217 2617 719  HOH   HOH A . 
CA 11 HOH   1218 2618 1785 HOH   HOH A . 
CA 11 HOH   1219 2619 3066 HOH   HOH A . 
CA 11 HOH   1220 2620 1844 HOH   HOH A . 
CA 11 HOH   1221 2621 3311 HOH   HOH A . 
CA 11 HOH   1222 2622 3173 HOH   HOH A . 
CA 11 HOH   1223 2623 928  HOH   HOH A . 
CA 11 HOH   1224 2624 1595 HOH   HOH A . 
CA 11 HOH   1225 2625 3007 HOH   HOH A . 
CA 11 HOH   1226 2626 1971 HOH   HOH A . 
CA 11 HOH   1227 2627 1984 HOH   HOH A . 
CA 11 HOH   1228 2628 1978 HOH   HOH A . 
CA 11 HOH   1229 2629 256  HOH   HOH A . 
CA 11 HOH   1230 2630 3578 HOH   HOH A . 
CA 11 HOH   1231 2631 3216 HOH   HOH A . 
CA 11 HOH   1232 2632 2035 HOH   HOH A . 
CA 11 HOH   1233 2633 1358 HOH   HOH A . 
CA 11 HOH   1234 2634 2060 HOH   HOH A . 
CA 11 HOH   1235 2635 1341 HOH   HOH A . 
CA 11 HOH   1236 2636 1379 HOH   HOH A . 
CA 11 HOH   1237 2637 3367 HOH   HOH A . 
CA 11 HOH   1238 2638 985  HOH   HOH A . 
CA 11 HOH   1239 2639 1612 HOH   HOH A . 
CA 11 HOH   1240 2640 3196 HOH   HOH A . 
CA 11 HOH   1241 2641 1961 HOH   HOH A . 
CA 11 HOH   1242 2642 3393 HOH   HOH A . 
CA 11 HOH   1243 2643 1509 HOH   HOH A . 
CA 11 HOH   1244 2644 3257 HOH   HOH A . 
CA 11 HOH   1245 2645 3581 HOH   HOH A . 
CA 11 HOH   1246 2646 1578 HOH   HOH A . 
CA 11 HOH   1247 2647 1711 HOH   HOH A . 
CA 11 HOH   1248 2648 3366 HOH   HOH A . 
CA 11 HOH   1249 2649 1010 HOH   HOH A . 
CA 11 HOH   1250 2650 2006 HOH   HOH A . 
CA 11 HOH   1251 2651 1233 HOH   HOH A . 
CA 11 HOH   1252 2652 1637 HOH   HOH A . 
CA 11 HOH   1253 2653 3549 HOH   HOH A . 
CA 11 HOH   1254 2654 3375 HOH   HOH A . 
CA 11 HOH   1255 2655 3067 HOH   HOH A . 
CA 11 HOH   1256 2656 1929 HOH   HOH A . 
CA 11 HOH   1257 2657 3079 HOH   HOH A . 
CA 11 HOH   1258 2658 1199 HOH   HOH A . 
CA 11 HOH   1259 2659 1332 HOH   HOH A . 
CA 11 HOH   1260 2660 1937 HOH   HOH A . 
CA 11 HOH   1261 2661 1490 HOH   HOH A . 
CA 11 HOH   1262 2662 1210 HOH   HOH A . 
CA 11 HOH   1263 2663 1682 HOH   HOH A . 
CA 11 HOH   1264 2664 3475 HOH   HOH A . 
CA 11 HOH   1265 2665 3034 HOH   HOH A . 
CA 11 HOH   1266 2666 1652 HOH   HOH A . 
CA 11 HOH   1267 2667 3573 HOH   HOH A . 
CA 11 HOH   1268 2668 3132 HOH   HOH A . 
CA 11 HOH   1269 2669 1068 HOH   HOH A . 
CA 11 HOH   1270 2670 1131 HOH   HOH A . 
CA 11 HOH   1271 2671 3431 HOH   HOH A . 
CA 11 HOH   1272 2672 3527 HOH   HOH A . 
CA 11 HOH   1273 2673 3141 HOH   HOH A . 
CA 11 HOH   1274 2674 1586 HOH   HOH A . 
CA 11 HOH   1275 2675 1539 HOH   HOH A . 
CA 11 HOH   1276 2676 3312 HOH   HOH A . 
CA 11 HOH   1277 2677 1835 HOH   HOH A . 
CA 11 HOH   1278 2678 3460 HOH   HOH A . 
CA 11 HOH   1279 2679 3291 HOH   HOH A . 
CA 11 HOH   1280 2680 1528 HOH   HOH A . 
CA 11 HOH   1281 2681 2048 HOH   HOH A . 
CA 11 HOH   1282 2682 1597 HOH   HOH A . 
CA 11 HOH   1283 2683 1066 HOH   HOH A . 
CA 11 HOH   1284 2684 3249 HOH   HOH A . 
CA 11 HOH   1285 2685 3506 HOH   HOH A . 
CA 11 HOH   1286 2686 1315 HOH   HOH A . 
CA 11 HOH   1287 2687 1808 HOH   HOH A . 
CA 11 HOH   1288 2688 852  HOH   HOH A . 
CA 11 HOH   1289 2689 1296 HOH   HOH A . 
CA 11 HOH   1290 2690 3314 HOH   HOH A . 
CA 11 HOH   1291 2691 1723 HOH   HOH A . 
CA 11 HOH   1292 2692 1998 HOH   HOH A . 
CA 11 HOH   1293 2693 1368 HOH   HOH A . 
CA 11 HOH   1294 2694 3313 HOH   HOH A . 
CA 11 HOH   1295 2695 1824 HOH   HOH A . 
DA 11 HOH   1    1401 3167 HOH   HOH B . 
DA 11 HOH   2    1402 3085 HOH   HOH B . 
DA 11 HOH   3    1403 1613 HOH   HOH B . 
DA 11 HOH   4    1404 721  HOH   HOH B . 
DA 11 HOH   5    1405 1402 HOH   HOH B . 
DA 11 HOH   6    1406 1422 HOH   HOH B . 
DA 11 HOH   7    1407 1743 HOH   HOH B . 
DA 11 HOH   8    1408 3562 HOH   HOH B . 
DA 11 HOH   9    1409 3093 HOH   HOH B . 
DA 11 HOH   10   1410 1268 HOH   HOH B . 
DA 11 HOH   11   1411 3207 HOH   HOH B . 
DA 11 HOH   12   1412 608  HOH   HOH B . 
DA 11 HOH   13   1413 803  HOH   HOH B . 
DA 11 HOH   14   1414 1303 HOH   HOH B . 
DA 11 HOH   15   1415 3238 HOH   HOH B . 
DA 11 HOH   16   1416 1294 HOH   HOH B . 
DA 11 HOH   17   1417 2022 HOH   HOH B . 
DA 11 HOH   18   1418 1497 HOH   HOH B . 
DA 11 HOH   19   1419 3185 HOH   HOH B . 
DA 11 HOH   20   1420 741  HOH   HOH B . 
DA 11 HOH   21   1421 1686 HOH   HOH B . 
DA 11 HOH   22   1422 514  HOH   HOH B . 
DA 11 HOH   23   1423 1666 HOH   HOH B . 
DA 11 HOH   24   1424 1237 HOH   HOH B . 
DA 11 HOH   25   1425 1811 HOH   HOH B . 
DA 11 HOH   26   1426 1061 HOH   HOH B . 
DA 11 HOH   27   1427 358  HOH   HOH B . 
DA 11 HOH   28   1428 838  HOH   HOH B . 
DA 11 HOH   29   1429 1176 HOH   HOH B . 
DA 11 HOH   30   1430 1909 HOH   HOH B . 
DA 11 HOH   31   1431 1400 HOH   HOH B . 
DA 11 HOH   32   1432 1239 HOH   HOH B . 
DA 11 HOH   33   1433 1675 HOH   HOH B . 
DA 11 HOH   34   1434 1864 HOH   HOH B . 
DA 11 HOH   35   1435 1521 HOH   HOH B . 
DA 11 HOH   36   1436 756  HOH   HOH B . 
DA 11 HOH   37   1437 437  HOH   HOH B . 
DA 11 HOH   38   1438 740  HOH   HOH B . 
DA 11 HOH   39   1439 3292 HOH   HOH B . 
DA 11 HOH   40   1440 1408 HOH   HOH B . 
DA 11 HOH   41   1441 1574 HOH   HOH B . 
DA 11 HOH   42   1442 3171 HOH   HOH B . 
DA 11 HOH   43   1443 1812 HOH   HOH B . 
DA 11 HOH   44   1444 1367 HOH   HOH B . 
DA 11 HOH   45   1445 3122 HOH   HOH B . 
DA 11 HOH   46   1446 1849 HOH   HOH B . 
DA 11 HOH   47   1447 1316 HOH   HOH B . 
DA 11 HOH   48   1448 1234 HOH   HOH B . 
DA 11 HOH   49   1449 1001 HOH   HOH B . 
DA 11 HOH   50   1450 3327 HOH   HOH B . 
DA 11 HOH   51   1451 1862 HOH   HOH B . 
DA 11 HOH   52   1452 1183 HOH   HOH B . 
DA 11 HOH   53   1453 533  HOH   HOH B . 
DA 11 HOH   54   1454 1425 HOH   HOH B . 
DA 11 HOH   55   1455 1028 HOH   HOH B . 
DA 11 HOH   56   1456 39   HOH   HOH B . 
DA 11 HOH   57   1457 338  HOH   HOH B . 
DA 11 HOH   58   1458 109  HOH   HOH B . 
DA 11 HOH   59   1459 329  HOH   HOH B . 
DA 11 HOH   60   1460 1642 HOH   HOH B . 
DA 11 HOH   61   1461 1861 HOH   HOH B . 
DA 11 HOH   62   1462 538  HOH   HOH B . 
DA 11 HOH   63   1463 1123 HOH   HOH B . 
DA 11 HOH   64   1464 1629 HOH   HOH B . 
DA 11 HOH   65   1465 113  HOH   HOH B . 
DA 11 HOH   66   1466 1481 HOH   HOH B . 
DA 11 HOH   67   1467 3077 HOH   HOH B . 
DA 11 HOH   68   1468 658  HOH   HOH B . 
DA 11 HOH   69   1469 1376 HOH   HOH B . 
DA 11 HOH   70   1470 70   HOH   HOH B . 
DA 11 HOH   71   1471 3204 HOH   HOH B . 
DA 11 HOH   72   1472 3076 HOH   HOH B . 
DA 11 HOH   73   1473 3470 HOH   HOH B . 
DA 11 HOH   74   1474 1562 HOH   HOH B . 
DA 11 HOH   75   1475 1370 HOH   HOH B . 
DA 11 HOH   76   1476 1275 HOH   HOH B . 
DA 11 HOH   77   1477 1106 HOH   HOH B . 
DA 11 HOH   78   1478 352  HOH   HOH B . 
DA 11 HOH   79   1479 649  HOH   HOH B . 
DA 11 HOH   80   1480 689  HOH   HOH B . 
DA 11 HOH   81   1481 1175 HOH   HOH B . 
DA 11 HOH   82   1482 1380 HOH   HOH B . 
DA 11 HOH   83   1483 323  HOH   HOH B . 
DA 11 HOH   84   1484 515  HOH   HOH B . 
DA 11 HOH   85   1485 3376 HOH   HOH B . 
DA 11 HOH   86   1486 1813 HOH   HOH B . 
DA 11 HOH   87   1487 771  HOH   HOH B . 
DA 11 HOH   88   1488 82   HOH   HOH B . 
DA 11 HOH   89   1489 1211 HOH   HOH B . 
DA 11 HOH   90   1490 1385 HOH   HOH B . 
DA 11 HOH   91   1491 3516 HOH   HOH B . 
DA 11 HOH   92   1492 1250 HOH   HOH B . 
DA 11 HOH   93   1493 2011 HOH   HOH B . 
DA 11 HOH   94   1494 388  HOH   HOH B . 
DA 11 HOH   95   1495 275  HOH   HOH B . 
DA 11 HOH   96   1496 3127 HOH   HOH B . 
DA 11 HOH   97   1497 9    HOH   HOH B . 
DA 11 HOH   98   1498 405  HOH   HOH B . 
DA 11 HOH   99   1499 793  HOH   HOH B . 
DA 11 HOH   100  1500 618  HOH   HOH B . 
DA 11 HOH   101  1501 61   HOH   HOH B . 
DA 11 HOH   102  1502 3512 HOH   HOH B . 
DA 11 HOH   103  1503 278  HOH   HOH B . 
DA 11 HOH   104  1504 3320 HOH   HOH B . 
DA 11 HOH   105  1505 1375 HOH   HOH B . 
DA 11 HOH   106  1506 890  HOH   HOH B . 
DA 11 HOH   107  1507 3406 HOH   HOH B . 
DA 11 HOH   108  1508 1344 HOH   HOH B . 
DA 11 HOH   109  1509 1825 HOH   HOH B . 
DA 11 HOH   110  1510 829  HOH   HOH B . 
DA 11 HOH   111  1511 3429 HOH   HOH B . 
DA 11 HOH   112  1512 529  HOH   HOH B . 
DA 11 HOH   113  1513 921  HOH   HOH B . 
DA 11 HOH   114  1514 3116 HOH   HOH B . 
DA 11 HOH   115  1515 280  HOH   HOH B . 
DA 11 HOH   116  1516 1372 HOH   HOH B . 
DA 11 HOH   117  1517 571  HOH   HOH B . 
DA 11 HOH   118  1518 650  HOH   HOH B . 
DA 11 HOH   119  1519 632  HOH   HOH B . 
DA 11 HOH   120  1520 298  HOH   HOH B . 
DA 11 HOH   121  1521 814  HOH   HOH B . 
DA 11 HOH   122  1522 245  HOH   HOH B . 
DA 11 HOH   123  1523 498  HOH   HOH B . 
DA 11 HOH   124  1524 240  HOH   HOH B . 
DA 11 HOH   125  1525 801  HOH   HOH B . 
DA 11 HOH   126  1526 988  HOH   HOH B . 
DA 11 HOH   127  1527 1544 HOH   HOH B . 
DA 11 HOH   128  1528 3329 HOH   HOH B . 
DA 11 HOH   129  1529 1383 HOH   HOH B . 
DA 11 HOH   130  1530 1820 HOH   HOH B . 
DA 11 HOH   131  1531 232  HOH   HOH B . 
DA 11 HOH   132  1532 15   HOH   HOH B . 
DA 11 HOH   133  1533 3264 HOH   HOH B . 
DA 11 HOH   134  1534 1186 HOH   HOH B . 
DA 11 HOH   135  1535 3219 HOH   HOH B . 
DA 11 HOH   136  1536 781  HOH   HOH B . 
DA 11 HOH   137  1537 1670 HOH   HOH B . 
DA 11 HOH   138  1538 3536 HOH   HOH B . 
DA 11 HOH   139  1539 3596 HOH   HOH B . 
DA 11 HOH   140  1540 1285 HOH   HOH B . 
DA 11 HOH   141  1541 219  HOH   HOH B . 
DA 11 HOH   142  1542 502  HOH   HOH B . 
DA 11 HOH   143  1543 973  HOH   HOH B . 
DA 11 HOH   144  1544 315  HOH   HOH B . 
DA 11 HOH   145  1545 1405 HOH   HOH B . 
DA 11 HOH   146  1546 596  HOH   HOH B . 
DA 11 HOH   147  1547 667  HOH   HOH B . 
DA 11 HOH   148  1548 117  HOH   HOH B . 
DA 11 HOH   149  1549 293  HOH   HOH B . 
DA 11 HOH   150  1550 1517 HOH   HOH B . 
DA 11 HOH   151  1551 1742 HOH   HOH B . 
DA 11 HOH   152  1552 3389 HOH   HOH B . 
DA 11 HOH   153  1553 1263 HOH   HOH B . 
DA 11 HOH   154  1554 3413 HOH   HOH B . 
DA 11 HOH   155  1555 21   HOH   HOH B . 
DA 11 HOH   156  1556 3328 HOH   HOH B . 
DA 11 HOH   157  1557 1718 HOH   HOH B . 
DA 11 HOH   158  1558 25   HOH   HOH B . 
DA 11 HOH   159  1559 1669 HOH   HOH B . 
DA 11 HOH   160  1560 23   HOH   HOH B . 
DA 11 HOH   161  1561 382  HOH   HOH B . 
DA 11 HOH   162  1562 318  HOH   HOH B . 
DA 11 HOH   163  1563 847  HOH   HOH B . 
DA 11 HOH   164  1564 310  HOH   HOH B . 
DA 11 HOH   165  1565 1572 HOH   HOH B . 
DA 11 HOH   166  1566 134  HOH   HOH B . 
DA 11 HOH   167  1567 3385 HOH   HOH B . 
DA 11 HOH   168  1568 1172 HOH   HOH B . 
DA 11 HOH   169  1569 1078 HOH   HOH B . 
DA 11 HOH   170  1570 1585 HOH   HOH B . 
DA 11 HOH   171  1571 3032 HOH   HOH B . 
DA 11 HOH   172  1572 1708 HOH   HOH B . 
DA 11 HOH   173  1573 3044 HOH   HOH B . 
DA 11 HOH   174  1574 664  HOH   HOH B . 
DA 11 HOH   175  1575 878  HOH   HOH B . 
DA 11 HOH   176  1576 94   HOH   HOH B . 
DA 11 HOH   177  1577 424  HOH   HOH B . 
DA 11 HOH   178  1578 362  HOH   HOH B . 
DA 11 HOH   179  1579 47   HOH   HOH B . 
DA 11 HOH   180  1580 279  HOH   HOH B . 
DA 11 HOH   181  1581 564  HOH   HOH B . 
DA 11 HOH   182  1582 3463 HOH   HOH B . 
DA 11 HOH   183  1583 1324 HOH   HOH B . 
DA 11 HOH   184  1584 958  HOH   HOH B . 
DA 11 HOH   185  1585 1038 HOH   HOH B . 
DA 11 HOH   186  1586 37   HOH   HOH B . 
DA 11 HOH   187  1587 1288 HOH   HOH B . 
DA 11 HOH   188  1588 755  HOH   HOH B . 
DA 11 HOH   189  1589 277  HOH   HOH B . 
DA 11 HOH   190  1590 1282 HOH   HOH B . 
DA 11 HOH   191  1591 799  HOH   HOH B . 
DA 11 HOH   192  1592 1904 HOH   HOH B . 
DA 11 HOH   193  1593 185  HOH   HOH B . 
DA 11 HOH   194  1594 1736 HOH   HOH B . 
DA 11 HOH   195  1595 1190 HOH   HOH B . 
DA 11 HOH   196  1596 111  HOH   HOH B . 
DA 11 HOH   197  1597 3341 HOH   HOH B . 
DA 11 HOH   198  1598 1162 HOH   HOH B . 
DA 11 HOH   199  1599 1655 HOH   HOH B . 
DA 11 HOH   200  1600 3342 HOH   HOH B . 
DA 11 HOH   201  1601 672  HOH   HOH B . 
DA 11 HOH   202  1602 1279 HOH   HOH B . 
DA 11 HOH   203  1603 1144 HOH   HOH B . 
DA 11 HOH   204  1604 1746 HOH   HOH B . 
DA 11 HOH   205  1605 474  HOH   HOH B . 
DA 11 HOH   206  1606 1828 HOH   HOH B . 
DA 11 HOH   207  1607 108  HOH   HOH B . 
DA 11 HOH   208  1608 3355 HOH   HOH B . 
DA 11 HOH   209  1609 1507 HOH   HOH B . 
DA 11 HOH   210  1610 1925 HOH   HOH B . 
DA 11 HOH   211  1611 292  HOH   HOH B . 
DA 11 HOH   212  1612 446  HOH   HOH B . 
DA 11 HOH   213  1613 594  HOH   HOH B . 
DA 11 HOH   214  1614 112  HOH   HOH B . 
DA 11 HOH   215  1615 54   HOH   HOH B . 
DA 11 HOH   216  1616 110  HOH   HOH B . 
DA 11 HOH   217  1617 317  HOH   HOH B . 
DA 11 HOH   218  1618 216  HOH   HOH B . 
DA 11 HOH   219  1619 560  HOH   HOH B . 
DA 11 HOH   220  1620 3399 HOH   HOH B . 
DA 11 HOH   221  1621 1501 HOH   HOH B . 
DA 11 HOH   222  1622 1362 HOH   HOH B . 
DA 11 HOH   223  1623 1821 HOH   HOH B . 
DA 11 HOH   224  1624 1433 HOH   HOH B . 
DA 11 HOH   225  1625 1780 HOH   HOH B . 
DA 11 HOH   226  1626 493  HOH   HOH B . 
DA 11 HOH   227  1627 1138 HOH   HOH B . 
DA 11 HOH   228  1628 126  HOH   HOH B . 
DA 11 HOH   229  1629 337  HOH   HOH B . 
DA 11 HOH   230  1630 139  HOH   HOH B . 
DA 11 HOH   231  1631 1216 HOH   HOH B . 
DA 11 HOH   232  1632 1361 HOH   HOH B . 
DA 11 HOH   233  1633 259  HOH   HOH B . 
DA 11 HOH   234  1634 3268 HOH   HOH B . 
DA 11 HOH   235  1635 606  HOH   HOH B . 
DA 11 HOH   236  1636 173  HOH   HOH B . 
DA 11 HOH   237  1637 3033 HOH   HOH B . 
DA 11 HOH   238  1638 981  HOH   HOH B . 
DA 11 HOH   239  1639 419  HOH   HOH B . 
DA 11 HOH   240  1640 116  HOH   HOH B . 
DA 11 HOH   241  1641 525  HOH   HOH B . 
DA 11 HOH   242  1642 1673 HOH   HOH B . 
DA 11 HOH   243  1643 423  HOH   HOH B . 
DA 11 HOH   244  1644 66   HOH   HOH B . 
DA 11 HOH   245  1645 579  HOH   HOH B . 
DA 11 HOH   246  1646 1397 HOH   HOH B . 
DA 11 HOH   247  1647 1043 HOH   HOH B . 
DA 11 HOH   248  1648 1648 HOH   HOH B . 
DA 11 HOH   249  1649 1834 HOH   HOH B . 
DA 11 HOH   250  1650 1846 HOH   HOH B . 
DA 11 HOH   251  1651 880  HOH   HOH B . 
DA 11 HOH   252  1652 462  HOH   HOH B . 
DA 11 HOH   253  1653 3227 HOH   HOH B . 
DA 11 HOH   254  1654 613  HOH   HOH B . 
DA 11 HOH   255  1655 262  HOH   HOH B . 
DA 11 HOH   256  1656 10   HOH   HOH B . 
DA 11 HOH   257  1657 428  HOH   HOH B . 
DA 11 HOH   258  1658 945  HOH   HOH B . 
DA 11 HOH   259  1659 215  HOH   HOH B . 
DA 11 HOH   260  1660 151  HOH   HOH B . 
DA 11 HOH   261  1661 558  HOH   HOH B . 
DA 11 HOH   262  1662 673  HOH   HOH B . 
DA 11 HOH   263  1663 1266 HOH   HOH B . 
DA 11 HOH   264  1664 582  HOH   HOH B . 
DA 11 HOH   265  1665 257  HOH   HOH B . 
DA 11 HOH   266  1666 1829 HOH   HOH B . 
DA 11 HOH   267  1667 281  HOH   HOH B . 
DA 11 HOH   268  1668 3535 HOH   HOH B . 
DA 11 HOH   269  1669 1049 HOH   HOH B . 
DA 11 HOH   270  1670 834  HOH   HOH B . 
DA 11 HOH   271  1671 1165 HOH   HOH B . 
DA 11 HOH   272  1672 3405 HOH   HOH B . 
DA 11 HOH   273  1673 1074 HOH   HOH B . 
DA 11 HOH   274  1674 276  HOH   HOH B . 
DA 11 HOH   275  1675 3119 HOH   HOH B . 
DA 11 HOH   276  1676 1641 HOH   HOH B . 
DA 11 HOH   277  1677 38   HOH   HOH B . 
DA 11 HOH   278  1678 3561 HOH   HOH B . 
DA 11 HOH   279  1679 344  HOH   HOH B . 
DA 11 HOH   280  1680 76   HOH   HOH B . 
DA 11 HOH   281  1681 8    HOH   HOH B . 
DA 11 HOH   282  1682 302  HOH   HOH B . 
DA 11 HOH   283  1683 191  HOH   HOH B . 
DA 11 HOH   284  1684 125  HOH   HOH B . 
DA 11 HOH   285  1685 336  HOH   HOH B . 
DA 11 HOH   286  1686 497  HOH   HOH B . 
DA 11 HOH   287  1687 1791 HOH   HOH B . 
DA 11 HOH   288  1688 635  HOH   HOH B . 
DA 11 HOH   289  1689 332  HOH   HOH B . 
DA 11 HOH   290  1690 367  HOH   HOH B . 
DA 11 HOH   291  1691 1561 HOH   HOH B . 
DA 11 HOH   292  1692 3255 HOH   HOH B . 
DA 11 HOH   293  1693 195  HOH   HOH B . 
DA 11 HOH   294  1694 1278 HOH   HOH B . 
DA 11 HOH   295  1695 1645 HOH   HOH B . 
DA 11 HOH   296  1696 3306 HOH   HOH B . 
DA 11 HOH   297  1697 59   HOH   HOH B . 
DA 11 HOH   298  1698 212  HOH   HOH B . 
DA 11 HOH   299  1699 1530 HOH   HOH B . 
DA 11 HOH   300  1700 3117 HOH   HOH B . 
DA 11 HOH   301  1701 695  HOH   HOH B . 
DA 11 HOH   302  1702 1865 HOH   HOH B . 
DA 11 HOH   303  1703 14   HOH   HOH B . 
DA 11 HOH   304  1704 925  HOH   HOH B . 
DA 11 HOH   305  1705 1764 HOH   HOH B . 
DA 11 HOH   306  1706 1416 HOH   HOH B . 
DA 11 HOH   307  1707 242  HOH   HOH B . 
DA 11 HOH   308  1708 144  HOH   HOH B . 
DA 11 HOH   309  1709 1891 HOH   HOH B . 
DA 11 HOH   310  1710 4    HOH   HOH B . 
DA 11 HOH   311  1711 248  HOH   HOH B . 
DA 11 HOH   312  1712 3052 HOH   HOH B . 
DA 11 HOH   313  1713 78   HOH   HOH B . 
DA 11 HOH   314  1714 1298 HOH   HOH B . 
DA 11 HOH   315  1715 208  HOH   HOH B . 
DA 11 HOH   316  1716 1297 HOH   HOH B . 
DA 11 HOH   317  1717 373  HOH   HOH B . 
DA 11 HOH   318  1718 1722 HOH   HOH B . 
DA 11 HOH   319  1719 457  HOH   HOH B . 
DA 11 HOH   320  1720 1054 HOH   HOH B . 
DA 11 HOH   321  1721 2016 HOH   HOH B . 
DA 11 HOH   322  1722 247  HOH   HOH B . 
DA 11 HOH   323  1723 3055 HOH   HOH B . 
DA 11 HOH   324  1724 486  HOH   HOH B . 
DA 11 HOH   325  1725 489  HOH   HOH B . 
DA 11 HOH   326  1726 918  HOH   HOH B . 
DA 11 HOH   327  1727 89   HOH   HOH B . 
DA 11 HOH   328  1728 759  HOH   HOH B . 
DA 11 HOH   329  1729 1888 HOH   HOH B . 
DA 11 HOH   330  1730 1853 HOH   HOH B . 
DA 11 HOH   331  1731 1194 HOH   HOH B . 
DA 11 HOH   332  1732 1452 HOH   HOH B . 
DA 11 HOH   333  1733 333  HOH   HOH B . 
DA 11 HOH   334  1734 114  HOH   HOH B . 
DA 11 HOH   335  1735 1845 HOH   HOH B . 
DA 11 HOH   336  1736 168  HOH   HOH B . 
DA 11 HOH   337  1737 7    HOH   HOH B . 
DA 11 HOH   338  1738 891  HOH   HOH B . 
DA 11 HOH   339  1739 34   HOH   HOH B . 
DA 11 HOH   340  1740 686  HOH   HOH B . 
DA 11 HOH   341  1741 1755 HOH   HOH B . 
DA 11 HOH   342  1742 1633 HOH   HOH B . 
DA 11 HOH   343  1743 750  HOH   HOH B . 
DA 11 HOH   344  1744 670  HOH   HOH B . 
DA 11 HOH   345  1745 415  HOH   HOH B . 
DA 11 HOH   346  1746 991  HOH   HOH B . 
DA 11 HOH   347  1747 660  HOH   HOH B . 
DA 11 HOH   348  1748 254  HOH   HOH B . 
DA 11 HOH   349  1749 774  HOH   HOH B . 
DA 11 HOH   350  1750 629  HOH   HOH B . 
DA 11 HOH   351  1751 186  HOH   HOH B . 
DA 11 HOH   352  1752 3    HOH   HOH B . 
DA 11 HOH   353  1753 1531 HOH   HOH B . 
DA 11 HOH   354  1754 3427 HOH   HOH B . 
DA 11 HOH   355  1755 18   HOH   HOH B . 
DA 11 HOH   356  1756 49   HOH   HOH B . 
DA 11 HOH   357  1757 561  HOH   HOH B . 
DA 11 HOH   358  1758 1654 HOH   HOH B . 
DA 11 HOH   359  1759 16   HOH   HOH B . 
DA 11 HOH   360  1760 790  HOH   HOH B . 
DA 11 HOH   361  1761 1761 HOH   HOH B . 
DA 11 HOH   362  1762 1588 HOH   HOH B . 
DA 11 HOH   363  1763 1805 HOH   HOH B . 
DA 11 HOH   364  1764 1502 HOH   HOH B . 
DA 11 HOH   365  1765 900  HOH   HOH B . 
DA 11 HOH   366  1766 810  HOH   HOH B . 
DA 11 HOH   367  1767 3383 HOH   HOH B . 
DA 11 HOH   368  1768 520  HOH   HOH B . 
DA 11 HOH   369  1769 1775 HOH   HOH B . 
DA 11 HOH   370  1770 1185 HOH   HOH B . 
DA 11 HOH   371  1771 1219 HOH   HOH B . 
DA 11 HOH   372  1772 328  HOH   HOH B . 
DA 11 HOH   373  1773 728  HOH   HOH B . 
DA 11 HOH   374  1774 1731 HOH   HOH B . 
DA 11 HOH   375  1775 541  HOH   HOH B . 
DA 11 HOH   376  1776 52   HOH   HOH B . 
DA 11 HOH   377  1777 3597 HOH   HOH B . 
DA 11 HOH   378  1778 29   HOH   HOH B . 
DA 11 HOH   379  1779 3246 HOH   HOH B . 
DA 11 HOH   380  1780 566  HOH   HOH B . 
DA 11 HOH   381  1781 1103 HOH   HOH B . 
DA 11 HOH   382  1782 1489 HOH   HOH B . 
DA 11 HOH   383  1783 840  HOH   HOH B . 
DA 11 HOH   384  1784 1349 HOH   HOH B . 
DA 11 HOH   385  1785 351  HOH   HOH B . 
DA 11 HOH   386  1786 331  HOH   HOH B . 
DA 11 HOH   387  1787 289  HOH   HOH B . 
DA 11 HOH   388  1788 149  HOH   HOH B . 
DA 11 HOH   389  1789 304  HOH   HOH B . 
DA 11 HOH   390  1790 1064 HOH   HOH B . 
DA 11 HOH   391  1791 1351 HOH   HOH B . 
DA 11 HOH   392  1792 420  HOH   HOH B . 
DA 11 HOH   393  1793 976  HOH   HOH B . 
DA 11 HOH   394  1794 175  HOH   HOH B . 
DA 11 HOH   395  1795 555  HOH   HOH B . 
DA 11 HOH   396  1796 978  HOH   HOH B . 
DA 11 HOH   397  1797 1041 HOH   HOH B . 
DA 11 HOH   398  1798 605  HOH   HOH B . 
DA 11 HOH   399  1799 1027 HOH   HOH B . 
DA 11 HOH   400  1800 188  HOH   HOH B . 
DA 11 HOH   401  1801 933  HOH   HOH B . 
DA 11 HOH   402  1802 1463 HOH   HOH B . 
DA 11 HOH   403  1803 957  HOH   HOH B . 
DA 11 HOH   404  1804 822  HOH   HOH B . 
DA 11 HOH   405  1805 152  HOH   HOH B . 
DA 11 HOH   406  1806 162  HOH   HOH B . 
DA 11 HOH   407  1807 133  HOH   HOH B . 
DA 11 HOH   408  1808 325  HOH   HOH B . 
DA 11 HOH   409  1809 178  HOH   HOH B . 
DA 11 HOH   410  1810 319  HOH   HOH B . 
DA 11 HOH   411  1811 1015 HOH   HOH B . 
DA 11 HOH   412  1812 77   HOH   HOH B . 
DA 11 HOH   413  1813 3073 HOH   HOH B . 
DA 11 HOH   414  1814 477  HOH   HOH B . 
DA 11 HOH   415  1815 892  HOH   HOH B . 
DA 11 HOH   416  1816 201  HOH   HOH B . 
DA 11 HOH   417  1817 305  HOH   HOH B . 
DA 11 HOH   418  1818 1901 HOH   HOH B . 
DA 11 HOH   419  1819 839  HOH   HOH B . 
DA 11 HOH   420  1820 43   HOH   HOH B . 
DA 11 HOH   421  1821 926  HOH   HOH B . 
DA 11 HOH   422  1822 580  HOH   HOH B . 
DA 11 HOH   423  1823 1104 HOH   HOH B . 
DA 11 HOH   424  1824 813  HOH   HOH B . 
DA 11 HOH   425  1825 460  HOH   HOH B . 
DA 11 HOH   426  1826 359  HOH   HOH B . 
DA 11 HOH   427  1827 806  HOH   HOH B . 
DA 11 HOH   428  1828 643  HOH   HOH B . 
DA 11 HOH   429  1829 385  HOH   HOH B . 
DA 11 HOH   430  1830 1679 HOH   HOH B . 
DA 11 HOH   431  1831 301  HOH   HOH B . 
DA 11 HOH   432  1832 3590 HOH   HOH B . 
DA 11 HOH   433  1833 727  HOH   HOH B . 
DA 11 HOH   434  1834 948  HOH   HOH B . 
DA 11 HOH   435  1835 1598 HOH   HOH B . 
DA 11 HOH   436  1836 35   HOH   HOH B . 
DA 11 HOH   437  1837 377  HOH   HOH B . 
DA 11 HOH   438  1838 79   HOH   HOH B . 
DA 11 HOH   439  1839 3437 HOH   HOH B . 
DA 11 HOH   440  1840 75   HOH   HOH B . 
DA 11 HOH   441  1841 87   HOH   HOH B . 
DA 11 HOH   442  1842 335  HOH   HOH B . 
DA 11 HOH   443  1843 398  HOH   HOH B . 
DA 11 HOH   444  1844 135  HOH   HOH B . 
DA 11 HOH   445  1845 1226 HOH   HOH B . 
DA 11 HOH   446  1846 669  HOH   HOH B . 
DA 11 HOH   447  1847 638  HOH   HOH B . 
DA 11 HOH   448  1848 1260 HOH   HOH B . 
DA 11 HOH   449  1849 448  HOH   HOH B . 
DA 11 HOH   450  1850 115  HOH   HOH B . 
DA 11 HOH   451  1851 357  HOH   HOH B . 
DA 11 HOH   452  1852 815  HOH   HOH B . 
DA 11 HOH   453  1853 1941 HOH   HOH B . 
DA 11 HOH   454  1854 105  HOH   HOH B . 
DA 11 HOH   455  1855 121  HOH   HOH B . 
DA 11 HOH   456  1856 641  HOH   HOH B . 
DA 11 HOH   457  1857 12   HOH   HOH B . 
DA 11 HOH   458  1858 903  HOH   HOH B . 
DA 11 HOH   459  1859 196  HOH   HOH B . 
DA 11 HOH   460  1860 1021 HOH   HOH B . 
DA 11 HOH   461  1861 11   HOH   HOH B . 
DA 11 HOH   462  1862 140  HOH   HOH B . 
DA 11 HOH   463  1863 1256 HOH   HOH B . 
DA 11 HOH   464  1864 1090 HOH   HOH B . 
DA 11 HOH   465  1865 681  HOH   HOH B . 
DA 11 HOH   466  1866 1245 HOH   HOH B . 
DA 11 HOH   467  1867 830  HOH   HOH B . 
DA 11 HOH   468  1868 862  HOH   HOH B . 
DA 11 HOH   469  1869 1311 HOH   HOH B . 
DA 11 HOH   470  1870 1353 HOH   HOH B . 
DA 11 HOH   471  1871 411  HOH   HOH B . 
DA 11 HOH   472  1872 233  HOH   HOH B . 
DA 11 HOH   473  1873 255  HOH   HOH B . 
DA 11 HOH   474  1874 421  HOH   HOH B . 
DA 11 HOH   475  1875 513  HOH   HOH B . 
DA 11 HOH   476  1876 1958 HOH   HOH B . 
DA 11 HOH   477  1877 998  HOH   HOH B . 
DA 11 HOH   478  1878 1644 HOH   HOH B . 
DA 11 HOH   479  1879 1287 HOH   HOH B . 
DA 11 HOH   480  1880 1994 HOH   HOH B . 
DA 11 HOH   481  1881 378  HOH   HOH B . 
DA 11 HOH   482  1882 968  HOH   HOH B . 
DA 11 HOH   483  1883 1363 HOH   HOH B . 
DA 11 HOH   484  1884 217  HOH   HOH B . 
DA 11 HOH   485  1885 158  HOH   HOH B . 
DA 11 HOH   486  1886 392  HOH   HOH B . 
DA 11 HOH   487  1887 106  HOH   HOH B . 
DA 11 HOH   488  1888 655  HOH   HOH B . 
DA 11 HOH   489  1889 5    HOH   HOH B . 
DA 11 HOH   490  1890 153  HOH   HOH B . 
DA 11 HOH   491  1891 413  HOH   HOH B . 
DA 11 HOH   492  1892 785  HOH   HOH B . 
DA 11 HOH   493  1893 249  HOH   HOH B . 
DA 11 HOH   494  1894 3010 HOH   HOH B . 
DA 11 HOH   495  1895 1392 HOH   HOH B . 
DA 11 HOH   496  1896 927  HOH   HOH B . 
DA 11 HOH   497  1897 36   HOH   HOH B . 
DA 11 HOH   498  1898 872  HOH   HOH B . 
DA 11 HOH   499  1899 682  HOH   HOH B . 
DA 11 HOH   500  1900 40   HOH   HOH B . 
DA 11 HOH   501  1901 258  HOH   HOH B . 
DA 11 HOH   502  1902 285  HOH   HOH B . 
DA 11 HOH   503  1903 3143 HOH   HOH B . 
DA 11 HOH   504  1904 602  HOH   HOH B . 
DA 11 HOH   505  1905 154  HOH   HOH B . 
DA 11 HOH   506  1906 709  HOH   HOH B . 
DA 11 HOH   507  1907 2    HOH   HOH B . 
DA 11 HOH   508  1908 1727 HOH   HOH B . 
DA 11 HOH   509  1909 1491 HOH   HOH B . 
DA 11 HOH   510  1910 1776 HOH   HOH B . 
DA 11 HOH   511  1911 147  HOH   HOH B . 
DA 11 HOH   512  1912 716  HOH   HOH B . 
DA 11 HOH   513  1913 846  HOH   HOH B . 
DA 11 HOH   514  1914 1283 HOH   HOH B . 
DA 11 HOH   515  1915 88   HOH   HOH B . 
DA 11 HOH   516  1916 1253 HOH   HOH B . 
DA 11 HOH   517  1917 371  HOH   HOH B . 
DA 11 HOH   518  1918 1327 HOH   HOH B . 
DA 11 HOH   519  1919 327  HOH   HOH B . 
DA 11 HOH   520  1920 636  HOH   HOH B . 
DA 11 HOH   521  1921 1121 HOH   HOH B . 
DA 11 HOH   522  1922 1499 HOH   HOH B . 
DA 11 HOH   523  1923 67   HOH   HOH B . 
DA 11 HOH   524  1924 95   HOH   HOH B . 
DA 11 HOH   525  1925 3166 HOH   HOH B . 
DA 11 HOH   526  1926 244  HOH   HOH B . 
DA 11 HOH   527  1927 1117 HOH   HOH B . 
DA 11 HOH   528  1928 1626 HOH   HOH B . 
DA 11 HOH   529  1929 919  HOH   HOH B . 
DA 11 HOH   530  1930 705  HOH   HOH B . 
DA 11 HOH   531  1931 51   HOH   HOH B . 
DA 11 HOH   532  1932 777  HOH   HOH B . 
DA 11 HOH   533  1933 83   HOH   HOH B . 
DA 11 HOH   534  1934 1157 HOH   HOH B . 
DA 11 HOH   535  1935 3392 HOH   HOH B . 
DA 11 HOH   536  1936 1784 HOH   HOH B . 
DA 11 HOH   537  1937 72   HOH   HOH B . 
DA 11 HOH   538  1938 3331 HOH   HOH B . 
DA 11 HOH   539  1939 1051 HOH   HOH B . 
DA 11 HOH   540  1940 3053 HOH   HOH B . 
DA 11 HOH   541  1941 1124 HOH   HOH B . 
DA 11 HOH   542  1942 213  HOH   HOH B . 
DA 11 HOH   543  1943 843  HOH   HOH B . 
DA 11 HOH   544  1944 647  HOH   HOH B . 
DA 11 HOH   545  1945 13   HOH   HOH B . 
DA 11 HOH   546  1946 32   HOH   HOH B . 
DA 11 HOH   547  1947 2031 HOH   HOH B . 
DA 11 HOH   548  1948 610  HOH   HOH B . 
DA 11 HOH   549  1949 361  HOH   HOH B . 
DA 11 HOH   550  1950 189  HOH   HOH B . 
DA 11 HOH   551  1951 1420 HOH   HOH B . 
DA 11 HOH   552  1952 122  HOH   HOH B . 
DA 11 HOH   553  1953 425  HOH   HOH B . 
DA 11 HOH   554  1954 1159 HOH   HOH B . 
DA 11 HOH   555  1955 3509 HOH   HOH B . 
DA 11 HOH   556  1956 1954 HOH   HOH B . 
DA 11 HOH   557  1957 557  HOH   HOH B . 
DA 11 HOH   558  1958 763  HOH   HOH B . 
DA 11 HOH   559  1959 504  HOH   HOH B . 
DA 11 HOH   560  1960 303  HOH   HOH B . 
DA 11 HOH   561  1961 875  HOH   HOH B . 
DA 11 HOH   562  1962 1163 HOH   HOH B . 
DA 11 HOH   563  1963 93   HOH   HOH B . 
DA 11 HOH   564  1964 1997 HOH   HOH B . 
DA 11 HOH   565  1965 266  HOH   HOH B . 
DA 11 HOH   566  1966 1171 HOH   HOH B . 
DA 11 HOH   567  1967 1    HOH   HOH B . 
DA 11 HOH   568  1968 623  HOH   HOH B . 
DA 11 HOH   569  1969 155  HOH   HOH B . 
DA 11 HOH   570  1970 794  HOH   HOH B . 
DA 11 HOH   571  1971 1601 HOH   HOH B . 
DA 11 HOH   572  1972 1113 HOH   HOH B . 
DA 11 HOH   573  1973 593  HOH   HOH B . 
DA 11 HOH   574  1974 194  HOH   HOH B . 
DA 11 HOH   575  1975 1417 HOH   HOH B . 
DA 11 HOH   576  1976 394  HOH   HOH B . 
DA 11 HOH   577  1977 459  HOH   HOH B . 
DA 11 HOH   578  1978 1895 HOH   HOH B . 
DA 11 HOH   579  1979 778  HOH   HOH B . 
DA 11 HOH   580  1980 1429 HOH   HOH B . 
DA 11 HOH   581  1981 1762 HOH   HOH B . 
DA 11 HOH   582  1982 956  HOH   HOH B . 
DA 11 HOH   583  1983 2038 HOH   HOH B . 
DA 11 HOH   584  1984 789  HOH   HOH B . 
DA 11 HOH   585  1985 374  HOH   HOH B . 
DA 11 HOH   586  1986 3504 HOH   HOH B . 
DA 11 HOH   587  1987 96   HOH   HOH B . 
DA 11 HOH   588  1988 748  HOH   HOH B . 
DA 11 HOH   589  1989 27   HOH   HOH B . 
DA 11 HOH   590  1990 1522 HOH   HOH B . 
DA 11 HOH   591  1991 1963 HOH   HOH B . 
DA 11 HOH   592  1992 704  HOH   HOH B . 
DA 11 HOH   593  1993 366  HOH   HOH B . 
DA 11 HOH   594  1994 909  HOH   HOH B . 
DA 11 HOH   595  1995 524  HOH   HOH B . 
DA 11 HOH   596  1996 546  HOH   HOH B . 
DA 11 HOH   597  1997 828  HOH   HOH B . 
DA 11 HOH   598  1998 837  HOH   HOH B . 
DA 11 HOH   599  1999 648  HOH   HOH B . 
DA 11 HOH   600  2000 864  HOH   HOH B . 
DA 11 HOH   601  2001 693  HOH   HOH B . 
DA 11 HOH   602  2002 589  HOH   HOH B . 
DA 11 HOH   603  2003 267  HOH   HOH B . 
DA 11 HOH   604  2004 1005 HOH   HOH B . 
DA 11 HOH   605  2005 1395 HOH   HOH B . 
DA 11 HOH   606  2006 1875 HOH   HOH B . 
DA 11 HOH   607  2007 1486 HOH   HOH B . 
DA 11 HOH   608  2008 1147 HOH   HOH B . 
DA 11 HOH   609  2009 1235 HOH   HOH B . 
DA 11 HOH   610  2010 1524 HOH   HOH B . 
DA 11 HOH   611  2011 3386 HOH   HOH B . 
DA 11 HOH   612  2012 826  HOH   HOH B . 
DA 11 HOH   613  2013 438  HOH   HOH B . 
DA 11 HOH   614  2014 3415 HOH   HOH B . 
DA 11 HOH   615  2015 940  HOH   HOH B . 
DA 11 HOH   616  2016 1466 HOH   HOH B . 
DA 11 HOH   617  2017 458  HOH   HOH B . 
DA 11 HOH   618  2018 717  HOH   HOH B . 
DA 11 HOH   619  2019 1457 HOH   HOH B . 
DA 11 HOH   620  2020 616  HOH   HOH B . 
DA 11 HOH   621  2021 306  HOH   HOH B . 
DA 11 HOH   622  2022 522  HOH   HOH B . 
DA 11 HOH   623  2023 1857 HOH   HOH B . 
DA 11 HOH   624  2024 3152 HOH   HOH B . 
DA 11 HOH   625  2025 725  HOH   HOH B . 
DA 11 HOH   626  2026 1577 HOH   HOH B . 
DA 11 HOH   627  2027 1447 HOH   HOH B . 
DA 11 HOH   628  2028 401  HOH   HOH B . 
DA 11 HOH   629  2029 6    HOH   HOH B . 
DA 11 HOH   630  2030 1782 HOH   HOH B . 
DA 11 HOH   631  2031 761  HOH   HOH B . 
DA 11 HOH   632  2032 980  HOH   HOH B . 
DA 11 HOH   633  2033 3235 HOH   HOH B . 
DA 11 HOH   634  2034 145  HOH   HOH B . 
DA 11 HOH   635  2035 1025 HOH   HOH B . 
DA 11 HOH   636  2036 715  HOH   HOH B . 
DA 11 HOH   637  2037 1393 HOH   HOH B . 
DA 11 HOH   638  2038 990  HOH   HOH B . 
DA 11 HOH   639  2039 3192 HOH   HOH B . 
DA 11 HOH   640  2040 1052 HOH   HOH B . 
DA 11 HOH   641  2041 1227 HOH   HOH B . 
DA 11 HOH   642  2042 3304 HOH   HOH B . 
DA 11 HOH   643  2043 1643 HOH   HOH B . 
DA 11 HOH   644  2044 812  HOH   HOH B . 
DA 11 HOH   645  2045 3    HOH   HOH B . 
DA 11 HOH   646  2046 1887 HOH   HOH B . 
DA 11 HOH   647  2047 165  HOH   HOH B . 
DA 11 HOH   648  2048 665  HOH   HOH B . 
DA 11 HOH   649  2049 881  HOH   HOH B . 
DA 11 HOH   650  2050 183  HOH   HOH B . 
DA 11 HOH   651  2051 1945 HOH   HOH B . 
DA 11 HOH   652  2052 1753 HOH   HOH B . 
DA 11 HOH   653  2053 824  HOH   HOH B . 
DA 11 HOH   654  2054 124  HOH   HOH B . 
DA 11 HOH   655  2055 1105 HOH   HOH B . 
DA 11 HOH   656  2056 1898 HOH   HOH B . 
DA 11 HOH   657  2057 200  HOH   HOH B . 
DA 11 HOH   658  2058 666  HOH   HOH B . 
DA 11 HOH   659  2059 1326 HOH   HOH B . 
DA 11 HOH   660  2060 1301 HOH   HOH B . 
DA 11 HOH   661  2061 3004 HOH   HOH B . 
DA 11 HOH   662  2062 3186 HOH   HOH B . 
DA 11 HOH   663  2063 81   HOH   HOH B . 
DA 11 HOH   664  2064 570  HOH   HOH B . 
DA 11 HOH   665  2065 3267 HOH   HOH B . 
DA 11 HOH   666  2066 209  HOH   HOH B . 
DA 11 HOH   667  2067 1587 HOH   HOH B . 
DA 11 HOH   668  2068 972  HOH   HOH B . 
DA 11 HOH   669  2069 3432 HOH   HOH B . 
DA 11 HOH   670  2070 494  HOH   HOH B . 
DA 11 HOH   671  2071 526  HOH   HOH B . 
DA 11 HOH   672  2072 3449 HOH   HOH B . 
DA 11 HOH   673  2073 1692 HOH   HOH B . 
DA 11 HOH   674  2074 100  HOH   HOH B . 
DA 11 HOH   675  2075 157  HOH   HOH B . 
DA 11 HOH   676  2076 1155 HOH   HOH B . 
DA 11 HOH   677  2077 1085 HOH   HOH B . 
DA 11 HOH   678  2078 3483 HOH   HOH B . 
DA 11 HOH   679  2079 1876 HOH   HOH B . 
DA 11 HOH   680  2080 1261 HOH   HOH B . 
DA 11 HOH   681  2081 314  HOH   HOH B . 
DA 11 HOH   682  2082 3481 HOH   HOH B . 
DA 11 HOH   683  2083 1446 HOH   HOH B . 
DA 11 HOH   684  2084 1760 HOH   HOH B . 
DA 11 HOH   685  2085 1232 HOH   HOH B . 
DA 11 HOH   686  2086 1292 HOH   HOH B . 
DA 11 HOH   687  2087 1007 HOH   HOH B . 
DA 11 HOH   688  2088 475  HOH   HOH B . 
DA 11 HOH   689  2089 418  HOH   HOH B . 
DA 11 HOH   690  2090 197  HOH   HOH B . 
DA 11 HOH   691  2091 3591 HOH   HOH B . 
DA 11 HOH   692  2092 699  HOH   HOH B . 
DA 11 HOH   693  2093 3440 HOH   HOH B . 
DA 11 HOH   694  2094 601  HOH   HOH B . 
DA 11 HOH   695  2095 159  HOH   HOH B . 
DA 11 HOH   696  2096 679  HOH   HOH B . 
DA 11 HOH   697  2097 434  HOH   HOH B . 
DA 11 HOH   698  2098 1238 HOH   HOH B . 
DA 11 HOH   699  2099 1870 HOH   HOH B . 
DA 11 HOH   700  2100 3148 HOH   HOH B . 
DA 11 HOH   701  2101 3408 HOH   HOH B . 
DA 11 HOH   702  2102 261  HOH   HOH B . 
DA 11 HOH   703  2103 496  HOH   HOH B . 
DA 11 HOH   704  2104 129  HOH   HOH B . 
DA 11 HOH   705  2105 340  HOH   HOH B . 
DA 11 HOH   706  2106 531  HOH   HOH B . 
DA 11 HOH   707  2107 1    HOH   HOH B . 
DA 11 HOH   708  2108 3248 HOH   HOH B . 
DA 11 HOH   709  2109 422  HOH   HOH B . 
DA 11 HOH   710  2110 1141 HOH   HOH B . 
DA 11 HOH   711  2111 690  HOH   HOH B . 
DA 11 HOH   712  2112 1453 HOH   HOH B . 
DA 11 HOH   713  2113 752  HOH   HOH B . 
DA 11 HOH   714  2114 42   HOH   HOH B . 
DA 11 HOH   715  2115 376  HOH   HOH B . 
DA 11 HOH   716  2116 1252 HOH   HOH B . 
DA 11 HOH   717  2117 449  HOH   HOH B . 
DA 11 HOH   718  2118 3269 HOH   HOH B . 
DA 11 HOH   719  2119 628  HOH   HOH B . 
DA 11 HOH   720  2120 488  HOH   HOH B . 
DA 11 HOH   721  2121 1195 HOH   HOH B . 
DA 11 HOH   722  2122 1424 HOH   HOH B . 
DA 11 HOH   723  2123 102  HOH   HOH B . 
DA 11 HOH   724  2124 223  HOH   HOH B . 
DA 11 HOH   725  2125 86   HOH   HOH B . 
DA 11 HOH   726  2126 685  HOH   HOH B . 
DA 11 HOH   727  2127 783  HOH   HOH B . 
DA 11 HOH   728  2128 203  HOH   HOH B . 
DA 11 HOH   729  2129 1752 HOH   HOH B . 
DA 11 HOH   730  2130 142  HOH   HOH B . 
DA 11 HOH   731  2131 584  HOH   HOH B . 
DA 11 HOH   732  2132 1709 HOH   HOH B . 
DA 11 HOH   733  2133 1656 HOH   HOH B . 
DA 11 HOH   734  2134 487  HOH   HOH B . 
DA 11 HOH   735  2135 710  HOH   HOH B . 
DA 11 HOH   736  2136 969  HOH   HOH B . 
DA 11 HOH   737  2137 1360 HOH   HOH B . 
DA 11 HOH   738  2138 466  HOH   HOH B . 
DA 11 HOH   739  2139 950  HOH   HOH B . 
DA 11 HOH   740  2140 205  HOH   HOH B . 
DA 11 HOH   741  2141 935  HOH   HOH B . 
DA 11 HOH   742  2142 1467 HOH   HOH B . 
DA 11 HOH   743  2143 898  HOH   HOH B . 
DA 11 HOH   744  2144 370  HOH   HOH B . 
DA 11 HOH   745  2145 1741 HOH   HOH B . 
DA 11 HOH   746  2146 295  HOH   HOH B . 
DA 11 HOH   747  2147 1944 HOH   HOH B . 
DA 11 HOH   748  2148 1076 HOH   HOH B . 
DA 11 HOH   749  2149 229  HOH   HOH B . 
DA 11 HOH   750  2150 827  HOH   HOH B . 
DA 11 HOH   751  2151 519  HOH   HOH B . 
DA 11 HOH   752  2152 1331 HOH   HOH B . 
DA 11 HOH   753  2153 417  HOH   HOH B . 
DA 11 HOH   754  2154 3245 HOH   HOH B . 
DA 11 HOH   755  2155 490  HOH   HOH B . 
DA 11 HOH   756  2156 1698 HOH   HOH B . 
DA 11 HOH   757  2157 543  HOH   HOH B . 
DA 11 HOH   758  2158 1058 HOH   HOH B . 
DA 11 HOH   759  2159 120  HOH   HOH B . 
DA 11 HOH   760  2160 1329 HOH   HOH B . 
DA 11 HOH   761  2161 130  HOH   HOH B . 
DA 11 HOH   762  2162 1533 HOH   HOH B . 
DA 11 HOH   763  2163 1796 HOH   HOH B . 
DA 11 HOH   764  2164 684  HOH   HOH B . 
DA 11 HOH   765  2165 592  HOH   HOH B . 
DA 11 HOH   766  2166 3165 HOH   HOH B . 
DA 11 HOH   767  2167 322  HOH   HOH B . 
DA 11 HOH   768  2168 440  HOH   HOH B . 
DA 11 HOH   769  2169 56   HOH   HOH B . 
DA 11 HOH   770  2170 192  HOH   HOH B . 
DA 11 HOH   771  2171 997  HOH   HOH B . 
DA 11 HOH   772  2172 3594 HOH   HOH B . 
DA 11 HOH   773  2173 24   HOH   HOH B . 
DA 11 HOH   774  2174 1534 HOH   HOH B . 
DA 11 HOH   775  2175 3359 HOH   HOH B . 
DA 11 HOH   776  2176 3266 HOH   HOH B . 
DA 11 HOH   777  2177 3265 HOH   HOH B . 
DA 11 HOH   778  2178 1920 HOH   HOH B . 
DA 11 HOH   779  2179 408  HOH   HOH B . 
DA 11 HOH   780  2180 1307 HOH   HOH B . 
DA 11 HOH   781  2181 1391 HOH   HOH B . 
DA 11 HOH   782  2182 1688 HOH   HOH B . 
DA 11 HOH   783  2183 62   HOH   HOH B . 
DA 11 HOH   784  2184 1552 HOH   HOH B . 
DA 11 HOH   785  2185 1793 HOH   HOH B . 
DA 11 HOH   786  2186 911  HOH   HOH B . 
DA 11 HOH   787  2187 409  HOH   HOH B . 
DA 11 HOH   788  2188 1802 HOH   HOH B . 
DA 11 HOH   789  2189 3072 HOH   HOH B . 
DA 11 HOH   790  2190 282  HOH   HOH B . 
DA 11 HOH   791  2191 767  HOH   HOH B . 
DA 11 HOH   792  2192 745  HOH   HOH B . 
DA 11 HOH   793  2193 694  HOH   HOH B . 
DA 11 HOH   794  2194 1947 HOH   HOH B . 
DA 11 HOH   795  2195 98   HOH   HOH B . 
DA 11 HOH   796  2196 1564 HOH   HOH B . 
DA 11 HOH   797  2197 1082 HOH   HOH B . 
DA 11 HOH   798  2198 1640 HOH   HOH B . 
DA 11 HOH   799  2199 758  HOH   HOH B . 
DA 11 HOH   800  2200 3228 HOH   HOH B . 
DA 11 HOH   801  2201 380  HOH   HOH B . 
DA 11 HOH   802  2202 350  HOH   HOH B . 
DA 11 HOH   803  2203 3202 HOH   HOH B . 
DA 11 HOH   804  2204 190  HOH   HOH B . 
DA 11 HOH   805  2205 2021 HOH   HOH B . 
DA 11 HOH   806  2206 3239 HOH   HOH B . 
DA 11 HOH   807  2207 506  HOH   HOH B . 
DA 11 HOH   808  2208 3448 HOH   HOH B . 
DA 11 HOH   809  2209 1980 HOH   HOH B . 
DA 11 HOH   810  2210 1614 HOH   HOH B . 
DA 11 HOH   811  2211 1352 HOH   HOH B . 
DA 11 HOH   812  2212 1300 HOH   HOH B . 
DA 11 HOH   813  2213 3539 HOH   HOH B . 
DA 11 HOH   814  2214 1203 HOH   HOH B . 
DA 11 HOH   815  2215 1498 HOH   HOH B . 
DA 11 HOH   816  2216 1273 HOH   HOH B . 
DA 11 HOH   817  2217 590  HOH   HOH B . 
DA 11 HOH   818  2218 651  HOH   HOH B . 
DA 11 HOH   819  2219 3218 HOH   HOH B . 
DA 11 HOH   820  2220 1240 HOH   HOH B . 
DA 11 HOH   821  2221 461  HOH   HOH B . 
DA 11 HOH   822  2222 3505 HOH   HOH B . 
DA 11 HOH   823  2223 1120 HOH   HOH B . 
DA 11 HOH   824  2224 463  HOH   HOH B . 
DA 11 HOH   825  2225 1622 HOH   HOH B . 
DA 11 HOH   826  2226 780  HOH   HOH B . 
DA 11 HOH   827  2227 68   HOH   HOH B . 
DA 11 HOH   828  2228 802  HOH   HOH B . 
DA 11 HOH   829  2229 1730 HOH   HOH B . 
DA 11 HOH   830  2230 1398 HOH   HOH B . 
DA 11 HOH   831  2231 103  HOH   HOH B . 
DA 11 HOH   832  2232 3441 HOH   HOH B . 
DA 11 HOH   833  2233 807  HOH   HOH B . 
DA 11 HOH   834  2234 1715 HOH   HOH B . 
DA 11 HOH   835  2235 1455 HOH   HOH B . 
DA 11 HOH   836  2236 300  HOH   HOH B . 
DA 11 HOH   837  2237 483  HOH   HOH B . 
DA 11 HOH   838  2238 659  HOH   HOH B . 
DA 11 HOH   839  2239 509  HOH   HOH B . 
DA 11 HOH   840  2240 899  HOH   HOH B . 
DA 11 HOH   841  2241 386  HOH   HOH B . 
DA 11 HOH   842  2242 3324 HOH   HOH B . 
DA 11 HOH   843  2243 825  HOH   HOH B . 
DA 11 HOH   844  2244 166  HOH   HOH B . 
DA 11 HOH   845  2245 3552 HOH   HOH B . 
DA 11 HOH   846  2246 3465 HOH   HOH B . 
DA 11 HOH   847  2247 456  HOH   HOH B . 
DA 11 HOH   848  2248 1935 HOH   HOH B . 
DA 11 HOH   849  2249 861  HOH   HOH B . 
DA 11 HOH   850  2250 1069 HOH   HOH B . 
DA 11 HOH   851  2251 3323 HOH   HOH B . 
DA 11 HOH   852  2252 3453 HOH   HOH B . 
DA 11 HOH   853  2253 3174 HOH   HOH B . 
DA 11 HOH   854  2254 1905 HOH   HOH B . 
DA 11 HOH   855  2255 2003 HOH   HOH B . 
DA 11 HOH   856  2256 1077 HOH   HOH B . 
DA 11 HOH   857  2257 3423 HOH   HOH B . 
DA 11 HOH   858  2258 1537 HOH   HOH B . 
DA 11 HOH   859  2259 521  HOH   HOH B . 
DA 11 HOH   860  2260 3560 HOH   HOH B . 
DA 11 HOH   861  2261 1037 HOH   HOH B . 
DA 11 HOH   862  2262 1556 HOH   HOH B . 
DA 11 HOH   863  2263 3175 HOH   HOH B . 
DA 11 HOH   864  2264 1206 HOH   HOH B . 
DA 11 HOH   865  2265 296  HOH   HOH B . 
DA 11 HOH   866  2266 3333 HOH   HOH B . 
DA 11 HOH   867  2267 712  HOH   HOH B . 
DA 11 HOH   868  2268 765  HOH   HOH B . 
DA 11 HOH   869  2269 3051 HOH   HOH B . 
DA 11 HOH   870  2270 2030 HOH   HOH B . 
DA 11 HOH   871  2271 1720 HOH   HOH B . 
DA 11 HOH   872  2272 3256 HOH   HOH B . 
DA 11 HOH   873  2273 3555 HOH   HOH B . 
DA 11 HOH   874  2274 1178 HOH   HOH B . 
DA 11 HOH   875  2275 1630 HOH   HOH B . 
DA 11 HOH   876  2276 3247 HOH   HOH B . 
DA 11 HOH   877  2277 1274 HOH   HOH B . 
DA 11 HOH   878  2278 3092 HOH   HOH B . 
DA 11 HOH   879  2279 816  HOH   HOH B . 
DA 11 HOH   880  2280 3074 HOH   HOH B . 
DA 11 HOH   881  2281 334  HOH   HOH B . 
DA 11 HOH   882  2282 936  HOH   HOH B . 
DA 11 HOH   883  2283 3107 HOH   HOH B . 
DA 11 HOH   884  2284 974  HOH   HOH B . 
DA 11 HOH   885  2285 738  HOH   HOH B . 
DA 11 HOH   886  2286 3592 HOH   HOH B . 
DA 11 HOH   887  2287 1371 HOH   HOH B . 
DA 11 HOH   888  2288 1770 HOH   HOH B . 
DA 11 HOH   889  2289 3071 HOH   HOH B . 
DA 11 HOH   890  2290 1921 HOH   HOH B . 
DA 11 HOH   891  2291 3469 HOH   HOH B . 
DA 11 HOH   892  2292 1665 HOH   HOH B . 
DA 11 HOH   893  2293 3203 HOH   HOH B . 
DA 11 HOH   894  2294 3089 HOH   HOH B . 
DA 11 HOH   895  2295 1606 HOH   HOH B . 
DA 11 HOH   896  2296 757  HOH   HOH B . 
DA 11 HOH   897  2297 3118 HOH   HOH B . 
DA 11 HOH   898  2298 3334 HOH   HOH B . 
DA 11 HOH   899  2299 3015 HOH   HOH B . 
DA 11 HOH   900  2300 3388 HOH   HOH B . 
DA 11 HOH   901  2301 3046 HOH   HOH B . 
DA 11 HOH   902  2302 3554 HOH   HOH B . 
DA 11 HOH   903  2303 2054 HOH   HOH B . 
DA 11 HOH   904  2304 1181 HOH   HOH B . 
DA 11 HOH   905  2305 1974 HOH   HOH B . 
DA 11 HOH   906  2306 3058 HOH   HOH B . 
DA 11 HOH   907  2307 3305 HOH   HOH B . 
DA 11 HOH   908  2308 1465 HOH   HOH B . 
DA 11 HOH   909  2309 3120 HOH   HOH B . 
DA 11 HOH   910  2310 3434 HOH   HOH B . 
DA 11 HOH   911  2311 3510 HOH   HOH B . 
DA 11 HOH   912  2312 1487 HOH   HOH B . 
DA 11 HOH   913  2313 534  HOH   HOH B . 
DA 11 HOH   914  2314 1333 HOH   HOH B . 
DA 11 HOH   915  2315 3576 HOH   HOH B . 
DA 11 HOH   916  2316 1615 HOH   HOH B . 
DA 11 HOH   917  2317 939  HOH   HOH B . 
DA 11 HOH   918  2318 2050 HOH   HOH B . 
DA 11 HOH   919  2319 3348 HOH   HOH B . 
DA 11 HOH   920  2320 3307 HOH   HOH B . 
DA 11 HOH   921  2321 581  HOH   HOH B . 
DA 11 HOH   922  2322 3551 HOH   HOH B . 
DA 11 HOH   923  2323 3161 HOH   HOH B . 
DA 11 HOH   924  2324 1758 HOH   HOH B . 
DA 11 HOH   925  2325 1495 HOH   HOH B . 
DA 11 HOH   926  2326 3422 HOH   HOH B . 
DA 11 HOH   927  2327 3381 HOH   HOH B . 
DA 11 HOH   928  2328 3543 HOH   HOH B . 
DA 11 HOH   929  2329 3452 HOH   HOH B . 
DA 11 HOH   930  2330 1807 HOH   HOH B . 
DA 11 HOH   931  2331 1134 HOH   HOH B . 
DA 11 HOH   932  2332 3407 HOH   HOH B . 
DA 11 HOH   933  2333 3087 HOH   HOH B . 
DA 11 HOH   934  2334 3121 HOH   HOH B . 
DA 11 HOH   935  2335 1114 HOH   HOH B . 
DA 11 HOH   936  2336 1819 HOH   HOH B . 
DA 11 HOH   937  2337 3011 HOH   HOH B . 
DA 11 HOH   938  2338 3436 HOH   HOH B . 
DA 11 HOH   939  2339 1426 HOH   HOH B . 
DA 11 HOH   940  2340 1969 HOH   HOH B . 
DA 11 HOH   941  2341 1347 HOH   HOH B . 
DA 11 HOH   942  2342 3150 HOH   HOH B . 
DA 11 HOH   943  2343 3182 HOH   HOH B . 
DA 11 HOH   944  2344 1883 HOH   HOH B . 
DA 11 HOH   945  2345 3250 HOH   HOH B . 
DA 11 HOH   946  2346 923  HOH   HOH B . 
DA 11 HOH   947  2347 1747 HOH   HOH B . 
DA 11 HOH   948  2348 1767 HOH   HOH B . 
DA 11 HOH   949  2349 3528 HOH   HOH B . 
DA 11 HOH   950  2350 1735 HOH   HOH B . 
DA 11 HOH   951  2351 1093 HOH   HOH B . 
DA 11 HOH   952  2352 676  HOH   HOH B . 
DA 11 HOH   953  2353 2023 HOH   HOH B . 
DA 11 HOH   954  2354 1680 HOH   HOH B . 
DA 11 HOH   955  2355 1931 HOH   HOH B . 
DA 11 HOH   956  2356 207  HOH   HOH B . 
DA 11 HOH   957  2357 3495 HOH   HOH B . 
DA 11 HOH   958  2358 1976 HOH   HOH B . 
DA 11 HOH   959  2359 1373 HOH   HOH B . 
DA 11 HOH   960  2360 2055 HOH   HOH B . 
DA 11 HOH   961  2361 3199 HOH   HOH B . 
DA 11 HOH   962  2362 3565 HOH   HOH B . 
DA 11 HOH   963  2363 1712 HOH   HOH B . 
DA 11 HOH   964  2364 3091 HOH   HOH B . 
DA 11 HOH   965  2365 2053 HOH   HOH B . 
DA 11 HOH   966  2366 3280 HOH   HOH B . 
DA 11 HOH   967  2367 3438 HOH   HOH B . 
DA 11 HOH   968  2368 1246 HOH   HOH B . 
DA 11 HOH   969  2369 1866 HOH   HOH B . 
DA 11 HOH   970  2370 523  HOH   HOH B . 
DA 11 HOH   971  2371 1464 HOH   HOH B . 
DA 11 HOH   972  2372 1843 HOH   HOH B . 
DA 11 HOH   973  2373 1841 HOH   HOH B . 
DA 11 HOH   974  2374 1483 HOH   HOH B . 
DA 11 HOH   975  2375 1639 HOH   HOH B . 
DA 11 HOH   976  2376 882  HOH   HOH B . 
DA 11 HOH   977  2377 1306 HOH   HOH B . 
DA 11 HOH   978  2378 3394 HOH   HOH B . 
DA 11 HOH   979  2379 527  HOH   HOH B . 
DA 11 HOH   980  2380 518  HOH   HOH B . 
DA 11 HOH   981  2381 1659 HOH   HOH B . 
DA 11 HOH   982  2382 3325 HOH   HOH B . 
DA 11 HOH   983  2383 3547 HOH   HOH B . 
DA 11 HOH   984  2384 782  HOH   HOH B . 
DA 11 HOH   985  2385 1071 HOH   HOH B . 
DA 11 HOH   986  2386 1500 HOH   HOH B . 
DA 11 HOH   987  2387 1940 HOH   HOH B . 
DA 11 HOH   988  2388 1566 HOH   HOH B . 
DA 11 HOH   989  2389 1886 HOH   HOH B . 
DA 11 HOH   990  2390 3586 HOH   HOH B . 
DA 11 HOH   991  2391 3201 HOH   HOH B . 
DA 11 HOH   992  2392 845  HOH   HOH B . 
DA 11 HOH   993  2393 1879 HOH   HOH B . 
DA 11 HOH   994  2394 1177 HOH   HOH B . 
DA 11 HOH   995  2395 1029 HOH   HOH B . 
DA 11 HOH   996  2396 465  HOH   HOH B . 
DA 11 HOH   997  2397 3187 HOH   HOH B . 
DA 11 HOH   998  2398 3559 HOH   HOH B . 
DA 11 HOH   999  2399 563  HOH   HOH B . 
DA 11 HOH   1000 2400 1014 HOH   HOH B . 
DA 11 HOH   1001 2401 3418 HOH   HOH B . 
DA 11 HOH   1002 2402 3499 HOH   HOH B . 
DA 11 HOH   1003 2403 1359 HOH   HOH B . 
DA 11 HOH   1004 2404 3270 HOH   HOH B . 
DA 11 HOH   1005 2405 1281 HOH   HOH B . 
DA 11 HOH   1006 2406 3517 HOH   HOH B . 
DA 11 HOH   1007 2407 3319 HOH   HOH B . 
DA 11 HOH   1008 2408 3494 HOH   HOH B . 
DA 11 HOH   1009 2409 64   HOH   HOH B . 
DA 11 HOH   1010 2410 3123 HOH   HOH B . 
DA 11 HOH   1011 2411 1154 HOH   HOH B . 
DA 11 HOH   1012 2412 1967 HOH   HOH B . 
DA 11 HOH   1013 2413 3086 HOH   HOH B . 
DA 11 HOH   1014 2414 1449 HOH   HOH B . 
DA 11 HOH   1015 2415 1863 HOH   HOH B . 
DA 11 HOH   1016 2416 1668 HOH   HOH B . 
DA 11 HOH   1017 2417 3112 HOH   HOH B . 
DA 11 HOH   1018 2418 3176 HOH   HOH B . 
DA 11 HOH   1019 2419 1837 HOH   HOH B . 
DA 11 HOH   1020 2420 482  HOH   HOH B . 
DA 11 HOH   1021 2421 1357 HOH   HOH B . 
DA 11 HOH   1022 2422 1221 HOH   HOH B . 
DA 11 HOH   1023 2423 1428 HOH   HOH B . 
DA 11 HOH   1024 2424 2    HOH   HOH B . 
DA 11 HOH   1025 2425 1871 HOH   HOH B . 
DA 11 HOH   1026 2426 1657 HOH   HOH B . 
DA 11 HOH   1027 2427 2027 HOH   HOH B . 
DA 11 HOH   1028 2428 3181 HOH   HOH B . 
DA 11 HOH   1029 2429 3054 HOH   HOH B . 
DA 11 HOH   1030 2430 1197 HOH   HOH B . 
DA 11 HOH   1031 2431 1948 HOH   HOH B . 
DA 11 HOH   1032 2432 645  HOH   HOH B . 
DA 11 HOH   1033 2433 1325 HOH   HOH B . 
DA 11 HOH   1034 2434 3190 HOH   HOH B . 
DA 11 HOH   1035 2435 1989 HOH   HOH B . 
DA 11 HOH   1036 2436 3222 HOH   HOH B . 
DA 11 HOH   1037 2437 734  HOH   HOH B . 
DA 11 HOH   1038 2438 1993 HOH   HOH B . 
DA 11 HOH   1039 2439 1208 HOH   HOH B . 
DA 11 HOH   1040 2440 2056 HOH   HOH B . 
DA 11 HOH   1041 2441 3468 HOH   HOH B . 
DA 11 HOH   1042 2442 1900 HOH   HOH B . 
DA 11 HOH   1043 2443 1779 HOH   HOH B . 
DA 11 HOH   1044 2444 1348 HOH   HOH B . 
DA 11 HOH   1045 2445 3346 HOH   HOH B . 
DA 11 HOH   1046 2446 1700 HOH   HOH B . 
DA 11 HOH   1047 2447 1473 HOH   HOH B . 
DA 11 HOH   1048 2448 1170 HOH   HOH B . 
DA 11 HOH   1049 2449 1230 HOH   HOH B . 
DA 11 HOH   1050 2450 3500 HOH   HOH B . 
DA 11 HOH   1051 2451 3321 HOH   HOH B . 
DA 11 HOH   1052 2452 1213 HOH   HOH B . 
DA 11 HOH   1053 2453 1523 HOH   HOH B . 
DA 11 HOH   1054 2454 932  HOH   HOH B . 
DA 11 HOH   1055 2455 3065 HOH   HOH B . 
DA 11 HOH   1056 2456 3090 HOH   HOH B . 
DA 11 HOH   1057 2457 3017 HOH   HOH B . 
DA 11 HOH   1058 2458 1881 HOH   HOH B . 
DA 11 HOH   1059 2459 914  HOH   HOH B . 
DA 11 HOH   1060 2460 1378 HOH   HOH B . 
DA 11 HOH   1061 2461 1789 HOH   HOH B . 
DA 11 HOH   1062 2462 1011 HOH   HOH B . 
DA 11 HOH   1063 2463 924  HOH   HOH B . 
DA 11 HOH   1064 2464 1596 HOH   HOH B . 
DA 11 HOH   1065 2465 3191 HOH   HOH B . 
DA 11 HOH   1066 2466 1719 HOH   HOH B . 
DA 11 HOH   1067 2467 1738 HOH   HOH B . 
DA 11 HOH   1068 2468 3402 HOH   HOH B . 
DA 11 HOH   1069 2469 3012 HOH   HOH B . 
DA 11 HOH   1070 2470 1889 HOH   HOH B . 
DA 11 HOH   1071 2471 1411 HOH   HOH B . 
DA 11 HOH   1072 2472 3284 HOH   HOH B . 
DA 11 HOH   1073 2473 967  HOH   HOH B . 
DA 11 HOH   1074 2474 4    HOH   HOH B . 
DA 11 HOH   1075 2475 1953 HOH   HOH B . 
DA 11 HOH   1076 2476 1152 HOH   HOH B . 
DA 11 HOH   1077 2477 3056 HOH   HOH B . 
DA 11 HOH   1078 2478 1337 HOH   HOH B . 
DA 11 HOH   1079 2479 1265 HOH   HOH B . 
DA 11 HOH   1080 2480 1579 HOH   HOH B . 
DA 11 HOH   1081 2481 1100 HOH   HOH B . 
DA 11 HOH   1082 2482 3564 HOH   HOH B . 
DA 11 HOH   1083 2483 2007 HOH   HOH B . 
DA 11 HOH   1084 2484 1619 HOH   HOH B . 
DA 11 HOH   1085 2485 1792 HOH   HOH B . 
DA 11 HOH   1086 2486 947  HOH   HOH B . 
DA 11 HOH   1087 2487 1554 HOH   HOH B . 
DA 11 HOH   1088 2488 1777 HOH   HOH B . 
DA 11 HOH   1089 2489 1604 HOH   HOH B . 
DA 11 HOH   1090 2490 1201 HOH   HOH B . 
DA 11 HOH   1091 2491 2000 HOH   HOH B . 
DA 11 HOH   1092 2492 1217 HOH   HOH B . 
DA 11 HOH   1093 2493 3454 HOH   HOH B . 
DA 11 HOH   1094 2494 1050 HOH   HOH B . 
DA 11 HOH   1095 2495 3382 HOH   HOH B . 
DA 11 HOH   1096 2496 1062 HOH   HOH B . 
DA 11 HOH   1097 2497 3220 HOH   HOH B . 
DA 11 HOH   1098 2498 3061 HOH   HOH B . 
DA 11 HOH   1099 2499 1584 HOH   HOH B . 
DA 11 HOH   1100 2500 1716 HOH   HOH B . 
DA 11 HOH   1101 2501 3088 HOH   HOH B . 
DA 11 HOH   1102 2502 1456 HOH   HOH B . 
DA 11 HOH   1103 2503 1939 HOH   HOH B . 
DA 11 HOH   1104 2504 3400 HOH   HOH B . 
DA 11 HOH   1105 2505 3550 HOH   HOH B . 
DA 11 HOH   1106 2506 3059 HOH   HOH B . 
DA 11 HOH   1107 2507 1299 HOH   HOH B . 
DA 11 HOH   1108 2508 2049 HOH   HOH B . 
DA 11 HOH   1109 2509 3351 HOH   HOH B . 
DA 11 HOH   1110 2510 1437 HOH   HOH B . 
DA 11 HOH   1111 2511 471  HOH   HOH B . 
DA 11 HOH   1112 2512 1671 HOH   HOH B . 
DA 11 HOH   1113 2513 975  HOH   HOH B . 
DA 11 HOH   1114 2514 1897 HOH   HOH B . 
DA 11 HOH   1115 2515 569  HOH   HOH B . 
DA 11 HOH   1116 2516 1291 HOH   HOH B . 
DA 11 HOH   1117 2517 3585 HOH   HOH B . 
DA 11 HOH   1118 2518 1635 HOH   HOH B . 
DA 11 HOH   1119 2519 3553 HOH   HOH B . 
DA 11 HOH   1120 2520 3075 HOH   HOH B . 
DA 11 HOH   1121 2521 3387 HOH   HOH B . 
DA 11 HOH   1122 2522 3263 HOH   HOH B . 
DA 11 HOH   1123 2523 776  HOH   HOH B . 
DA 11 HOH   1124 2524 884  HOH   HOH B . 
DA 11 HOH   1125 2525 1110 HOH   HOH B . 
DA 11 HOH   1126 2526 3062 HOH   HOH B . 
DA 11 HOH   1127 2527 597  HOH   HOH B . 
DA 11 HOH   1128 2528 1013 HOH   HOH B . 
DA 11 HOH   1129 2529 1404 HOH   HOH B . 
DA 11 HOH   1130 2530 545  HOH   HOH B . 
DA 11 HOH   1131 2531 3332 HOH   HOH B . 
DA 11 HOH   1132 2532 3563 HOH   HOH B . 
DA 11 HOH   1133 2533 97   HOH   HOH B . 
DA 11 HOH   1134 2534 3013 HOH   HOH B . 
DA 11 HOH   1135 2535 1084 HOH   HOH B . 
DA 11 HOH   1136 2536 1480 HOH   HOH B . 
DA 11 HOH   1137 2537 573  HOH   HOH B . 
DA 11 HOH   1138 2538 3345 HOH   HOH B . 
DA 11 HOH   1139 2539 3106 HOH   HOH B . 
DA 11 HOH   1140 2540 3471 HOH   HOH B . 
DA 11 HOH   1141 2541 1765 HOH   HOH B . 
DA 11 HOH   1142 2542 3343 HOH   HOH B . 
DA 11 HOH   1143 2543 1251 HOH   HOH B . 
DA 11 HOH   1144 2544 3042 HOH   HOH B . 
DA 11 HOH   1145 2545 1286 HOH   HOH B . 
DA 11 HOH   1146 2546 1475 HOH   HOH B . 
DA 11 HOH   1147 2547 634  HOH   HOH B . 
DA 11 HOH   1148 2548 1173 HOH   HOH B . 
DA 11 HOH   1149 2549 450  HOH   HOH B . 
DA 11 HOH   1150 2550 1545 HOH   HOH B . 
DA 11 HOH   1151 2551 3580 HOH   HOH B . 
DA 11 HOH   1152 2552 1345 HOH   HOH B . 
DA 11 HOH   1153 2553 3377 HOH   HOH B . 
DA 11 HOH   1154 2554 3538 HOH   HOH B . 
DA 11 HOH   1155 2555 3507 HOH   HOH B . 
DA 11 HOH   1156 2556 1390 HOH   HOH B . 
DA 11 HOH   1157 2557 3236 HOH   HOH B . 
DA 11 HOH   1158 2558 1112 HOH   HOH B . 
DA 11 HOH   1159 2559 3279 HOH   HOH B . 
DA 11 HOH   1160 2560 3189 HOH   HOH B . 
DA 11 HOH   1161 2561 3064 HOH   HOH B . 
DA 11 HOH   1162 2562 3234 HOH   HOH B . 
DA 11 HOH   1163 2563 1734 HOH   HOH B . 
DA 11 HOH   1164 2564 1180 HOH   HOH B . 
DA 11 HOH   1165 2565 2010 HOH   HOH B . 
DA 11 HOH   1166 2566 1482 HOH   HOH B . 
DA 11 HOH   1167 2567 1625 HOH   HOH B . 
DA 11 HOH   1168 2568 1918 HOH   HOH B . 
DA 11 HOH   1169 2569 787  HOH   HOH B . 
DA 11 HOH   1170 2570 3537 HOH   HOH B . 
DA 11 HOH   1171 2571 907  HOH   HOH B . 
DA 11 HOH   1172 2572 3193 HOH   HOH B . 
DA 11 HOH   1173 2573 1914 HOH   HOH B . 
DA 11 HOH   1174 2574 1022 HOH   HOH B . 
DA 11 HOH   1175 2575 3018 HOH   HOH B . 
DA 11 HOH   1176 2576 3194 HOH   HOH B . 
DA 11 HOH   1177 2577 1907 HOH   HOH B . 
DA 11 HOH   1178 2578 3419 HOH   HOH B . 
DA 11 HOH   1179 2579 3240 HOH   HOH B . 
DA 11 HOH   1180 2580 720  HOH   HOH B . 
DA 11 HOH   1181 2581 1083 HOH   HOH B . 
DA 11 HOH   1182 2582 1202 HOH   HOH B . 
DA 11 HOH   1183 2583 3484 HOH   HOH B . 
DA 11 HOH   1184 2584 906  HOH   HOH B . 
DA 11 HOH   1185 2585 1850 HOH   HOH B . 
DA 11 HOH   1186 2586 1421 HOH   HOH B . 
DA 11 HOH   1187 2587 3330 HOH   HOH B . 
DA 11 HOH   1188 2588 3384 HOH   HOH B . 
DA 11 HOH   1189 2589 1143 HOH   HOH B . 
DA 11 HOH   1190 2590 2026 HOH   HOH B . 
DA 11 HOH   1191 2591 2005 HOH   HOH B . 
DA 11 HOH   1192 2592 1218 HOH   HOH B . 
DA 11 HOH   1193 2593 3349 HOH   HOH B . 
DA 11 HOH   1194 2594 2019 HOH   HOH B . 
DA 11 HOH   1195 2595 1706 HOH   HOH B . 
DA 11 HOH   1196 2596 2037 HOH   HOH B . 
DA 11 HOH   1197 2597 565  HOH   HOH B . 
DA 11 HOH   1198 2598 1212 HOH   HOH B . 
DA 11 HOH   1199 2599 1689 HOH   HOH B . 
DA 11 HOH   1200 2600 1885 HOH   HOH B . 
DA 11 HOH   1201 2601 1374 HOH   HOH B . 
DA 11 HOH   1202 2602 999  HOH   HOH B . 
DA 11 HOH   1203 2603 3014 HOH   HOH B . 
DA 11 HOH   1204 2604 1460 HOH   HOH B . 
DA 11 HOH   1205 2605 588  HOH   HOH B . 
DA 11 HOH   1206 2606 1816 HOH   HOH B . 
DA 11 HOH   1207 2607 1334 HOH   HOH B . 
DA 11 HOH   1208 2608 1053 HOH   HOH B . 
DA 11 HOH   1209 2609 3003 HOH   HOH B . 
DA 11 HOH   1210 2610 1182 HOH   HOH B . 
DA 11 HOH   1211 2611 3350 HOH   HOH B . 
DA 11 HOH   1212 2612 1701 HOH   HOH B . 
DA 11 HOH   1213 2613 1623 HOH   HOH B . 
DA 11 HOH   1214 2614 3357 HOH   HOH B . 
DA 11 HOH   1215 2615 2015 HOH   HOH B . 
DA 11 HOH   1216 2616 3569 HOH   HOH B . 
DA 11 HOH   1217 2617 3425 HOH   HOH B . 
DA 11 HOH   1218 2618 2044 HOH   HOH B . 
DA 11 HOH   1219 2619 1034 HOH   HOH B . 
DA 11 HOH   1220 2620 1690 HOH   HOH B . 
DA 11 HOH   1221 2621 3540 HOH   HOH B . 
DA 11 HOH   1222 2622 1628 HOH   HOH B . 
DA 11 HOH   1223 2623 3456 HOH   HOH B . 
DA 11 HOH   1224 2624 1258 HOH   HOH B . 
DA 11 HOH   1225 2625 1044 HOH   HOH B . 
DA 11 HOH   1226 2626 1926 HOH   HOH B . 
DA 11 HOH   1227 2627 3479 HOH   HOH B . 
DA 11 HOH   1228 2628 283  HOH   HOH B . 
DA 11 HOH   1229 2629 657  HOH   HOH B . 
DA 11 HOH   1230 2630 1520 HOH   HOH B . 
DA 11 HOH   1231 2631 1794 HOH   HOH B . 
DA 11 HOH   1232 2632 1224 HOH   HOH B . 
DA 11 HOH   1233 2633 1987 HOH   HOH B . 
DA 11 HOH   1234 2634 1189 HOH   HOH B . 
DA 11 HOH   1235 2635 747  HOH   HOH B . 
DA 11 HOH   1236 2636 3253 HOH   HOH B . 
DA 11 HOH   1237 2637 1867 HOH   HOH B . 
DA 11 HOH   1238 2638 1322 HOH   HOH B . 
DA 11 HOH   1239 2639 1892 HOH   HOH B . 
DA 11 HOH   1240 2640 1108 HOH   HOH B . 
DA 11 HOH   1241 2641 1934 HOH   HOH B . 
DA 11 HOH   1242 2642 1356 HOH   HOH B . 
DA 11 HOH   1243 2643 3060 HOH   HOH B . 
DA 11 HOH   1244 2644 1488 HOH   HOH B . 
DA 11 HOH   1245 2645 3601 HOH   HOH B . 
DA 11 HOH   1246 2646 1809 HOH   HOH B . 
DA 11 HOH   1247 2647 1308 HOH   HOH B . 
DA 11 HOH   1248 2648 3237 HOH   HOH B . 
DA 11 HOH   1249 2649 1943 HOH   HOH B . 
DA 11 HOH   1250 2650 937  HOH   HOH B . 
DA 11 HOH   1251 2651 3063 HOH   HOH B . 
DA 11 HOH   1252 2652 1125 HOH   HOH B . 
DA 11 HOH   1253 2653 435  HOH   HOH B . 
DA 11 HOH   1254 2654 3482 HOH   HOH B . 
DA 11 HOH   1255 2655 3358 HOH   HOH B . 
DA 11 HOH   1256 2656 1795 HOH   HOH B . 
DA 11 HOH   1257 2657 3396 HOH   HOH B . 
DA 11 HOH   1258 2658 1418 HOH   HOH B . 
DA 11 HOH   1259 2659 3347 HOH   HOH B . 
DA 11 HOH   1260 2660 3461 HOH   HOH B . 
DA 11 HOH   1261 2661 1890 HOH   HOH B . 
DA 11 HOH   1262 2662 1581 HOH   HOH B . 
DA 11 HOH   1263 2663 938  HOH   HOH B . 
DA 11 HOH   1264 2664 1450 HOH   HOH B . 
DA 11 HOH   1265 2665 3151 HOH   HOH B . 
DA 11 HOH   1266 2666 3600 HOH   HOH B . 
DA 11 HOH   1267 2667 3108 HOH   HOH B . 
DA 11 HOH   1268 2668 3478 HOH   HOH B . 
DA 11 HOH   1269 2669 1697 HOH   HOH B . 
DA 11 HOH   1270 2670 3566 HOH   HOH B . 
DA 11 HOH   1271 2671 3057 HOH   HOH B . 
DA 11 HOH   1272 2672 1906 HOH   HOH B . 
DA 11 HOH   1273 2673 1518 HOH   HOH B . 
DA 11 HOH   1274 2674 1031 HOH   HOH B . 
DA 11 HOH   1275 2675 1139 HOH   HOH B . 
DA 11 HOH   1276 2676 3435 HOH   HOH B . 
DA 11 HOH   1277 2677 1995 HOH   HOH B . 
DA 11 HOH   1278 2678 1851 HOH   HOH B . 
DA 11 HOH   1279 2679 2039 HOH   HOH B . 
DA 11 HOH   1280 2680 3587 HOH   HOH B . 
DA 11 HOH   1281 2681 1822 HOH   HOH B . 
DA 11 HOH   1282 2682 3579 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   ? NH1 ? A ARG 35   NH1 
3   1 Y 1 A ARG 33   ? NH2 ? A ARG 35   NH2 
4   1 Y 1 A GLU 52   ? CG  ? A GLU 54   CG  
5   1 Y 1 A GLU 52   ? CD  ? A GLU 54   CD  
6   1 Y 1 A GLU 52   ? OE1 ? A GLU 54   OE1 
7   1 Y 1 A GLU 52   ? OE2 ? A GLU 54   OE2 
8   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
9   1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
10  1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
11  1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
12  1 Y 1 A HIS 79   ? CG  ? A HIS 81   CG  
13  1 Y 1 A HIS 79   ? ND1 ? A HIS 81   ND1 
14  1 Y 1 A HIS 79   ? CD2 ? A HIS 81   CD2 
15  1 Y 1 A HIS 79   ? CE1 ? A HIS 81   CE1 
16  1 Y 1 A HIS 79   ? NE2 ? A HIS 81   NE2 
17  1 Y 1 A SER 82   ? OG  ? A SER 84   OG  
18  1 Y 1 A GLU 85   ? CG  ? A GLU 87   CG  
19  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
20  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
21  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
22  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
23  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
24  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
25  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
26  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
27  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
28  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
29  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
30  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
31  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
32  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
33  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
34  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
35  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
36  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
37  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
38  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
39  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
40  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
41  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
42  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
43  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
44  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
45  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
46  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
47  1 Y 1 A SER 137  ? OG  ? A SER 139  OG  
48  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
49  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
50  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
51  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
52  1 Y 1 A ARG 189  ? CG  ? A ARG 191  CG  
53  1 Y 1 A ARG 189  ? CD  ? A ARG 191  CD  
54  1 Y 1 A ARG 189  ? NE  ? A ARG 191  NE  
55  1 Y 1 A ARG 189  ? CZ  ? A ARG 191  CZ  
56  1 Y 1 A ARG 189  ? NH1 ? A ARG 191  NH1 
57  1 Y 1 A ARG 189  ? NH2 ? A ARG 191  NH2 
58  1 Y 1 A GLN 194  ? CG  ? A GLN 196  CG  
59  1 Y 1 A GLN 194  ? CD  ? A GLN 196  CD  
60  1 Y 1 A GLN 194  ? OE1 ? A GLN 196  OE1 
61  1 Y 1 A GLN 194  ? NE2 ? A GLN 196  NE2 
62  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
63  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
64  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
65  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
66  1 Y 1 A LYS 209  ? CG  ? A LYS 211  CG  
67  1 Y 1 A LYS 209  ? CD  ? A LYS 211  CD  
68  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
69  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
70  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
71  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
72  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
73  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
74  1 Y 1 A LYS 214  ? CG  ? A LYS 216  CG  
75  1 Y 1 A LYS 214  ? CD  ? A LYS 216  CD  
76  1 Y 1 A LYS 214  ? CE  ? A LYS 216  CE  
77  1 Y 1 A LYS 214  ? NZ  ? A LYS 216  NZ  
78  1 Y 1 A GLU 234  ? CG  ? A GLU 236  CG  
79  1 Y 1 A GLU 234  ? CD  ? A GLU 236  CD  
80  1 Y 1 A GLU 234  ? OE1 ? A GLU 236  OE1 
81  1 Y 1 A GLU 234  ? OE2 ? A GLU 236  OE2 
82  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
83  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
84  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
85  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
86  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
87  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
88  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
89  1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
90  1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
91  1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
92  1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
93  1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
94  1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
95  1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
96  1 Y 1 A ARG 489  ? CG  ? A ARG 491  CG  
97  1 Y 1 A ARG 489  ? CD  ? A ARG 491  CD  
98  1 Y 1 A ARG 489  ? NE  ? A ARG 491  NE  
99  1 Y 1 A ARG 489  ? CZ  ? A ARG 491  CZ  
100 1 Y 1 A ARG 489  ? NH1 ? A ARG 491  NH1 
101 1 Y 1 A ARG 489  ? NH2 ? A ARG 491  NH2 
102 1 Y 1 A GLU 492  ? CG  ? A GLU 494  CG  
103 1 Y 1 A GLU 492  ? CD  ? A GLU 494  CD  
104 1 Y 1 A GLU 492  ? OE1 ? A GLU 494  OE1 
105 1 Y 1 A GLU 492  ? OE2 ? A GLU 494  OE2 
106 1 Y 1 A ASN 493  ? CG  ? A ASN 495  CG  
107 1 Y 1 A ASN 493  ? OD1 ? A ASN 495  OD1 
108 1 Y 1 A ASN 493  ? ND2 ? A ASN 495  ND2 
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 ASP 532  ? CG  ? A ASP 534  CG  
119 1 Y 1 A ASP 532  ? OD1 ? A ASP 534  OD1 
120 1 Y 1 A ASP 532  ? OD2 ? A ASP 534  OD2 
121 1 Y 1 A ARG 533  ? CG  ? A ARG 535  CG  
122 1 Y 1 A ARG 533  ? CD  ? A ARG 535  CD  
123 1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
124 1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
125 1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
126 1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
127 1 Y 1 A LYS 573  ? CG  ? A LYS 575  CG  
128 1 Y 1 A LYS 573  ? CD  ? A LYS 575  CD  
129 1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
130 1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
131 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
132 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
133 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
134 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
135 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
136 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
137 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
138 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
139 1 Y 1 A GLU 785  ? CG  ? A GLU 787  CG  
140 1 Y 1 A GLU 785  ? CD  ? A GLU 787  CD  
141 1 Y 1 A GLU 785  ? OE1 ? A GLU 787  OE1 
142 1 Y 1 A GLU 785  ? OE2 ? A GLU 787  OE2 
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 ARG 859  ? CG  ? A ARG 861  CG  
147 1 Y 1 A ARG 859  ? CD  ? A ARG 861  CD  
148 1 Y 1 A ARG 859  ? NE  ? A ARG 861  NE  
149 1 Y 1 A ARG 859  ? CZ  ? A ARG 861  CZ  
150 1 Y 1 A ARG 859  ? NH1 ? A ARG 861  NH1 
151 1 Y 1 A ARG 859  ? NH2 ? A ARG 861  NH2 
152 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
153 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
154 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
155 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
156 1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
157 1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
158 1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
159 1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
160 1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
161 1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
162 1 Y 1 A GLU 932  ? CG  ? A GLU 934  CG  
163 1 Y 1 A GLU 932  ? CD  ? A GLU 934  CD  
164 1 Y 1 A GLU 932  ? OE1 ? A GLU 934  OE1 
165 1 Y 1 A GLU 932  ? OE2 ? A GLU 934  OE2 
166 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
167 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
168 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
169 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
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 ARG 952  ? CG  ? A ARG 954  CG  
181 1 Y 1 A ARG 952  ? CD  ? A ARG 954  CD  
182 1 Y 1 A ARG 952  ? NE  ? A ARG 954  NE  
183 1 Y 1 A ARG 952  ? CZ  ? A ARG 954  CZ  
184 1 Y 1 A ARG 952  ? NH1 ? A ARG 954  NH1 
185 1 Y 1 A ARG 952  ? NH2 ? A ARG 954  NH2 
186 1 Y 1 A ARG 1063 ? CG  ? A ARG 1065 CG  
187 1 Y 1 A ARG 1063 ? CD  ? A ARG 1065 CD  
188 1 Y 1 A ARG 1063 ? NE  ? A ARG 1065 NE  
189 1 Y 1 A ARG 1063 ? CZ  ? A ARG 1065 CZ  
190 1 Y 1 A ARG 1063 ? NH1 ? A ARG 1065 NH1 
191 1 Y 1 A ARG 1063 ? NH2 ? A ARG 1065 NH2 
192 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
193 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
194 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
195 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
196 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
197 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
198 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
199 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
200 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
201 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
202 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
203 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
204 1 Y 1 A SER 1228 ? OG  ? A SER 1230 OG  
205 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
206 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
207 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
208 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
209 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
210 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
211 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
212 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
213 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
214 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
215 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
216 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
217 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
218 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
219 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
220 1 Y 1 B ILE 60   ? CG1 ? B ILE 62   CG1 
221 1 Y 1 B ILE 60   ? CG2 ? B ILE 62   CG2 
222 1 Y 1 B ILE 60   ? CD1 ? B ILE 62   CD1 
223 1 Y 1 B SER 66   ? OG  ? B SER 68   OG  
224 1 Y 1 B GLU 73   ? CG  ? B GLU 75   CG  
225 1 Y 1 B GLU 73   ? CD  ? B GLU 75   CD  
226 1 Y 1 B GLU 73   ? OE1 ? B GLU 75   OE1 
227 1 Y 1 B GLU 73   ? OE2 ? B GLU 75   OE2 
228 1 Y 1 B HIS 79   ? CG  ? B HIS 81   CG  
229 1 Y 1 B HIS 79   ? ND1 ? B HIS 81   ND1 
230 1 Y 1 B HIS 79   ? CD2 ? B HIS 81   CD2 
231 1 Y 1 B HIS 79   ? CE1 ? B HIS 81   CE1 
232 1 Y 1 B HIS 79   ? NE2 ? B HIS 81   NE2 
233 1 Y 1 B VAL 84   ? CG1 ? B VAL 86   CG1 
234 1 Y 1 B VAL 84   ? CG2 ? B VAL 86   CG2 
235 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
236 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
237 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
238 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
239 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
240 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
241 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
242 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
243 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
244 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
245 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
246 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
247 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
248 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
249 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
250 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
251 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
252 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
253 1 Y 1 B ASP 127  ? CG  ? B ASP 129  CG  
254 1 Y 1 B ASP 127  ? OD1 ? B ASP 129  OD1 
255 1 Y 1 B ASP 127  ? OD2 ? B ASP 129  OD2 
256 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
257 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
258 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
259 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
260 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
261 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
262 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
263 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
264 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
265 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
266 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
267 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
268 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
269 1 Y 1 B ARG 138  ? CG  ? B ARG 140  CG  
270 1 Y 1 B ARG 138  ? CD  ? B ARG 140  CD  
271 1 Y 1 B ARG 138  ? NE  ? B ARG 140  NE  
272 1 Y 1 B ARG 138  ? CZ  ? B ARG 140  CZ  
273 1 Y 1 B ARG 138  ? NH1 ? B ARG 140  NH1 
274 1 Y 1 B ARG 138  ? NH2 ? B ARG 140  NH2 
275 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
276 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
277 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
278 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
279 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
280 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
281 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
282 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
283 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
284 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
285 1 Y 1 B GLN 194  ? CG  ? B GLN 196  CG  
286 1 Y 1 B GLN 194  ? CD  ? B GLN 196  CD  
287 1 Y 1 B GLN 194  ? OE1 ? B GLN 196  OE1 
288 1 Y 1 B GLN 194  ? NE2 ? B GLN 196  NE2 
289 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
290 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
291 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
292 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
293 1 Y 1 B LYS 214  ? CG  ? B LYS 216  CG  
294 1 Y 1 B LYS 214  ? CD  ? B LYS 216  CD  
295 1 Y 1 B LYS 214  ? CE  ? B LYS 216  CE  
296 1 Y 1 B LYS 214  ? NZ  ? B LYS 216  NZ  
297 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
298 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
299 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
300 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
301 1 Y 1 B ASP 414  ? CG  ? B ASP 416  CG  
302 1 Y 1 B ASP 414  ? OD1 ? B ASP 416  OD1 
303 1 Y 1 B ASP 414  ? OD2 ? B ASP 416  OD2 
304 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
305 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
306 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
307 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
308 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
309 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
310 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
311 1 Y 1 B GLU 458  ? CG  ? B GLU 460  CG  
312 1 Y 1 B GLU 458  ? CD  ? B GLU 460  CD  
313 1 Y 1 B GLU 458  ? OE1 ? B GLU 460  OE1 
314 1 Y 1 B GLU 458  ? OE2 ? B GLU 460  OE2 
315 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
316 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
317 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
318 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
319 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
320 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
321 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
322 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
323 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
324 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
325 1 Y 1 B THR 481  ? OG1 ? B THR 483  OG1 
326 1 Y 1 B THR 481  ? CG2 ? B THR 483  CG2 
327 1 Y 1 B ARG 489  ? CG  ? B ARG 491  CG  
328 1 Y 1 B ARG 489  ? CD  ? B ARG 491  CD  
329 1 Y 1 B ARG 489  ? NE  ? B ARG 491  NE  
330 1 Y 1 B ARG 489  ? CZ  ? B ARG 491  CZ  
331 1 Y 1 B ARG 489  ? NH1 ? B ARG 491  NH1 
332 1 Y 1 B ARG 489  ? NH2 ? B ARG 491  NH2 
333 1 Y 1 B LEU 490  ? CG  ? B LEU 492  CG  
334 1 Y 1 B LEU 490  ? CD1 ? B LEU 492  CD1 
335 1 Y 1 B LEU 490  ? CD2 ? B LEU 492  CD2 
336 1 Y 1 B LEU 491  ? CG  ? B LEU 493  CG  
337 1 Y 1 B LEU 491  ? CD1 ? B LEU 493  CD1 
338 1 Y 1 B LEU 491  ? CD2 ? B LEU 493  CD2 
339 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
340 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
341 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
342 1 Y 1 B SER 498  ? OG  ? B SER 500  OG  
343 1 Y 1 B VAL 500  ? CG1 ? B VAL 502  CG1 
344 1 Y 1 B VAL 500  ? CG2 ? B VAL 502  CG2 
345 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
346 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
347 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
348 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
349 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
350 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
351 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
352 1 Y 1 B ILE 510  ? CG1 ? B ILE 512  CG1 
353 1 Y 1 B ILE 510  ? CG2 ? B ILE 512  CG2 
354 1 Y 1 B ILE 510  ? CD1 ? B ILE 512  CD1 
355 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
356 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
357 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
358 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
359 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
360 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
361 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
362 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
363 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
364 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
365 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
366 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
367 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
368 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
369 1 Y 1 B ASP 796  ? CG  ? B ASP 798  CG  
370 1 Y 1 B ASP 796  ? OD1 ? B ASP 798  OD1 
371 1 Y 1 B ASP 796  ? OD2 ? B ASP 798  OD2 
372 1 Y 1 B GLN 827  ? CG  ? B GLN 829  CG  
373 1 Y 1 B GLN 827  ? CD  ? B GLN 829  CD  
374 1 Y 1 B GLN 827  ? OE1 ? B GLN 829  OE1 
375 1 Y 1 B GLN 827  ? NE2 ? B GLN 829  NE2 
376 1 Y 1 B GLU 854  ? CG  ? B GLU 856  CG  
377 1 Y 1 B GLU 854  ? CD  ? B GLU 856  CD  
378 1 Y 1 B GLU 854  ? OE1 ? B GLU 856  OE1 
379 1 Y 1 B GLU 854  ? OE2 ? B GLU 856  OE2 
380 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
381 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
382 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
383 1 Y 1 B GLU 890  ? CG  ? B GLU 892  CG  
384 1 Y 1 B GLU 890  ? CD  ? B GLU 892  CD  
385 1 Y 1 B GLU 890  ? OE1 ? B GLU 892  OE1 
386 1 Y 1 B GLU 890  ? OE2 ? B GLU 892  OE2 
387 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
388 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
389 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
390 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
391 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
392 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
393 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
394 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
395 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
396 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
397 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
398 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
399 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
400 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
401 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
402 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
403 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
404 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
405 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
406 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
407 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
408 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
409 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
410 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
411 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
412 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
413 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
414 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
415 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
416 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
417 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
418 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
419 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
420 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
421 1 Y 1 B ASN 1140 ? CG  ? B ASN 1142 CG  
422 1 Y 1 B ASN 1140 ? OD1 ? B ASN 1142 OD1 
423 1 Y 1 B ASN 1140 ? ND2 ? B ASN 1142 ND2 
424 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
425 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
426 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
427 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
428 1 Y 1 B LEU 1147 ? CG  ? B LEU 1149 CG  
429 1 Y 1 B LEU 1147 ? CD1 ? B LEU 1149 CD1 
430 1 Y 1 B LEU 1147 ? CD2 ? B LEU 1149 CD2 
431 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
432 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
433 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
434 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
435 1 Y 1 B SER 1228 ? OG  ? B SER 1230 OG  
436 1 Y 1 B MET 1230 ? CG  ? B MET 1232 CG  
437 1 Y 1 B MET 1230 ? SD  ? B MET 1232 SD  
438 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                   106.42 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9E0C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.369 
_cell.length_a_esd                 ? 
_cell.length_b                     101.642 
_cell.length_b_esd                 ? 
_cell.length_c                     125.924 
_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                         9E0C 
_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                   9E0C 
_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             2.33 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.31 
_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 24 mM 1-benzofuran-5-ylmethanol. Crystal was soaked in cryobuffer containing 50 mM 1-benzofuran-5-ylmethanol 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   1.00009 
_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        1.00009 
_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                                       9E0C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.32 
_reflns.d_resolution_low                               48.14 
_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                                     1044248 
_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                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.89 
_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                                0.065 
_reflns.pdbx_Rpim_I_all                                0.025 
_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                              0.060 
_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                                    1.32 
_reflns_shell.d_res_low                                     1.34 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           80388 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             16856 
_reflns_shell.percent_possible_obs                          60.3 
_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                               4.8 
_reflns_shell.pdbx_chi_squared                              0.58 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.7 
_reflns_shell.pdbx_Rrim_I_all                               1.975 
_reflns_shell.pdbx_Rpim_I_all                               0.884 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.369 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.757 
_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                                 9E0C 
_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                            1.32 
_refine.ls_d_res_low                             48.14 
_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                     1044248 
_refine.ls_number_reflns_R_free                  52912 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.07 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1733 
_refine.ls_R_factor_R_free                       0.1904 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1724 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.03 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.69 
_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                            0.15 
_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        17809 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         326 
_refine_hist.number_atoms_solvent             2577 
_refine_hist.number_atoms_total               20712 
_refine_hist.d_res_high                       1.32 
_refine_hist.d_res_low                        48.14 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 18904 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.899  ? 25851 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.446 ? 7093  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.068  ? 3035  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3339  ? 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' 1.32 1.34  . . 1070 20391 57.00  . . . . 0.3258 . . . . . . . . . . . 0.3263 
'X-RAY DIFFRACTION' 1.34 1.35  . . 1136 22220 63.00  . . . . 0.3205 . . . . . . . . . . . 0.3422 
'X-RAY DIFFRACTION' 1.35 1.37  . . 1353 24217 68.00  . . . . 0.3155 . . . . . . . . . . . 0.3330 
'X-RAY DIFFRACTION' 1.37 1.38  . . 1386 26472 75.00  . . . . 0.3054 . . . . . . . . . . . 0.3234 
'X-RAY DIFFRACTION' 1.38 1.40  . . 1544 28612 81.00  . . . . 0.2912 . . . . . . . . . . . 0.3086 
'X-RAY DIFFRACTION' 1.40 1.42  . . 1696 31405 88.00  . . . . 0.2831 . . . . . . . . . . . 0.3014 
'X-RAY DIFFRACTION' 1.42 1.44  . . 1869 35150 99.00  . . . . 0.2668 . . . . . . . . . . . 0.2881 
'X-RAY DIFFRACTION' 1.44 1.46  . . 1929 35233 100.00 . . . . 0.2574 . . . . . . . . . . . 0.2695 
'X-RAY DIFFRACTION' 1.46 1.49  . . 1929 35413 100.00 . . . . 0.2465 . . . . . . . . . . . 0.2697 
'X-RAY DIFFRACTION' 1.49 1.51  . . 2016 35178 100.00 . . . . 0.2335 . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 1.51 1.54  . . 1923 35377 100.00 . . . . 0.2200 . . . . . . . . . . . 0.2420 
'X-RAY DIFFRACTION' 1.54 1.57  . . 1861 35386 100.00 . . . . 0.2137 . . . . . . . . . . . 0.2295 
'X-RAY DIFFRACTION' 1.57 1.60  . . 1857 35404 99.00  . . . . 0.2064 . . . . . . . . . . . 0.2208 
'X-RAY DIFFRACTION' 1.60 1.63  . . 1857 35064 99.00  . . . . 0.2038 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 1.63 1.66  . . 1828 35239 99.00  . . . . 0.2023 . . . . . . . . . . . 0.2217 
'X-RAY DIFFRACTION' 1.66 1.70  . . 1915 35116 99.00  . . . . 0.1954 . . . . . . . . . . . 0.2301 
'X-RAY DIFFRACTION' 1.70 1.74  . . 1738 35022 98.00  . . . . 0.1925 . . . . . . . . . . . 0.2173 
'X-RAY DIFFRACTION' 1.74 1.79  . . 1753 34788 98.00  . . . . 0.1871 . . . . . . . . . . . 0.2173 
'X-RAY DIFFRACTION' 1.79 1.84  . . 1901 34290 96.00  . . . . 0.1802 . . . . . . . . . . . 0.2025 
'X-RAY DIFFRACTION' 1.84 1.90  . . 1876 32541 92.00  . . . . 0.1845 . . . . . . . . . . . 0.2094 
'X-RAY DIFFRACTION' 1.90 1.97  . . 1903 34674 98.00  . . . . 0.1837 . . . . . . . . . . . 0.2071 
'X-RAY DIFFRACTION' 1.97 2.05  . . 1758 35477 100.00 . . . . 0.1698 . . . . . . . . . . . 0.1992 
'X-RAY DIFFRACTION' 2.05 2.14  . . 1882 35263 99.00  . . . . 0.1668 . . . . . . . . . . . 0.1863 
'X-RAY DIFFRACTION' 2.14 2.26  . . 1916 35251 99.00  . . . . 0.1620 . . . . . . . . . . . 0.1838 
'X-RAY DIFFRACTION' 2.26 2.40  . . 1926 35155 99.00  . . . . 0.1614 . . . . . . . . . . . 0.1859 
'X-RAY DIFFRACTION' 2.40 2.58  . . 1860 35193 99.00  . . . . 0.1634 . . . . . . . . . . . 0.1806 
'X-RAY DIFFRACTION' 2.58 2.84  . . 1872 34897 98.00  . . . . 0.1639 . . . . . . . . . . . 0.1782 
'X-RAY DIFFRACTION' 2.84 3.25  . . 1686 34251 96.00  . . . . 0.1630 . . . . . . . . . . . 0.1783 
'X-RAY DIFFRACTION' 3.26 4.10  . . 1704 33252 94.00  . . . . 0.1409 . . . . . . . . . . . 0.1566 
'X-RAY DIFFRACTION' 4.10 48.14 . . 1968 35405 100.00 . . . . 0.1406 . . . . . . . . . . . 0.1490 
# 
_struct.entry_id                     9E0C 
_struct.title                        'Structure of proline utilization A complexed with 1-benzofuran-5-ylmethanol' 
_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        9E0C 
_struct_keywords.text            
;FLAVOENZYME, ROSSMANN FOLD, PROLINE DEHYDROGENASE, ALDEHYDE DEHYDROGENASE, PROLINE CATABOLISM, SUBSTRATE CHANNELING, BIFUNCTIONAL ENZYME, OXIDOREDUCTASE
;
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 1  ? 
C  N N 2  ? 
D  N N 3  ? 
E  N N 4  ? 
F  N N 5  ? 
G  N N 6  ? 
H  N N 7  ? 
I  N N 7  ? 
J  N N 7  ? 
K  N N 7  ? 
L  N N 7  ? 
M  N N 8  ? 
N  N N 3  ? 
O  N N 2  ? 
P  N N 9  ? 
Q  N N 4  ? 
R  N N 10 ? 
S  N N 4  ? 
T  N N 3  ? 
U  N N 3  ? 
V  N N 3  ? 
W  N N 4  ? 
X  N N 5  ? 
Y  N N 6  ? 
Z  N N 7  ? 
AA N N 7  ? 
BA N N 8  ? 
CA N N 11 ? 
DA 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 9E0C A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9E0C 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 9E0C SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9E0C MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9E0C SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9E0C 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)' 12480 ? 
1 MORE         -145  ? 
1 'SSA (A^2)'  76930 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,CA                                    
3 1 B,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,DA                              
# 
_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  ? ALA A 497  ? TYR A 485  ALA A 495  1 ? 11 
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  ? ARG A 651  ? PRO A 631  ARG A 649  1 ? 19 
HELX_P HELX_P33  AD6 ARG A 651  ? GLY A 664  ? ARG A 649  GLY A 662  1 ? 14 
HELX_P HELX_P34  AD7 SER A 666  ? LEU A 692  ? SER A 664  LEU A 690  1 ? 27 
HELX_P HELX_P35  AD8 LEU A 712  ? ALA A 725  ? LEU A 710  ALA A 723  1 ? 14 
HELX_P HELX_P36  AD9 THR A 737  ? ALA A 751  ? THR A 735  ALA A 749  1 ? 15 
HELX_P HELX_P37  AE1 ASP A 764  ? ALA A 774  ? ASP A 762  ALA A 772  1 ? 11 
HELX_P HELX_P38  AE2 SER A 785  ? ASP A 798  ? SER A 783  ASP A 796  1 ? 14 
HELX_P HELX_P39  AE3 LEU A 826  ? ASP A 840  ? LEU A 824  ASP A 838  1 ? 15 
HELX_P HELX_P40  AE4 SER A 841  ? GLN A 844  ? SER A 839  GLN A 842  5 ? 4  
HELX_P HELX_P41  AE5 GLU A 856  ? HIS A 871  ? GLU A 854  HIS A 869  1 ? 16 
HELX_P HELX_P42  AE6 THR A 890  ? LEU A 907  ? THR A 888  LEU A 905  1 ? 18 
HELX_P HELX_P43  AE7 ALA A 917  ? GLY A 923  ? ALA A 915  GLY A 921  5 ? 7  
HELX_P HELX_P44  AE8 LYS A 935  ? LEU A 939  ? LYS A 933  LEU A 937  5 ? 5  
HELX_P HELX_P45  AE9 ARG A 954  ? ASP A 956  ? ARG A 952  ASP A 954  5 ? 3  
HELX_P HELX_P46  AF1 ASP A 957  ? THR A 968  ? ASP A 955  THR A 966  1 ? 12 
HELX_P HELX_P47  AF2 LEU A 980  ? ILE A 991  ? LEU A 978  ILE A 989  1 ? 12 
HELX_P HELX_P48  AF3 ARG A 1015 ? GLY A 1019 ? ARG A 1013 GLY A 1017 5 ? 5  
HELX_P HELX_P49  AF4 TYR A 1029 ? VAL A 1034 ? TYR A 1027 VAL A 1032 5 ? 6  
HELX_P HELX_P50  AF5 ASP A 1049 ? GLY A 1063 ? ASP A 1047 GLY A 1061 1 ? 15 
HELX_P HELX_P51  AF6 ALA A 1064 ? SER A 1078 ? ALA A 1062 SER A 1076 1 ? 15 
HELX_P HELX_P52  AF7 THR A 1110 ? THR A 1124 ? THR A 1108 THR A 1122 1 ? 15 
HELX_P HELX_P53  AF8 ALA A 1133 ? GLY A 1135 ? ALA A 1131 GLY A 1133 5 ? 3  
HELX_P HELX_P54  AF9 LEU A 1136 ? LYS A 1141 ? LEU A 1134 LYS A 1139 5 ? 6  
HELX_P HELX_P55  AG1 PRO A 1144 ? LEU A 1149 ? PRO A 1142 LEU A 1147 1 ? 6  
HELX_P HELX_P56  AG2 ASP A 1156 ? ASP A 1160 ? ASP A 1154 ASP A 1158 5 ? 5  
HELX_P HELX_P57  AG3 ASP A 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P58  AG4 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P59  AG5 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
HELX_P HELX_P60  AG6 ALA A 1229 ? ILE A 1234 ? ALA A 1227 ILE A 1232 5 ? 6  
HELX_P HELX_P61  AG7 SER B 31   ? ALA B 40   ? SER B 29   ALA B 38   1 ? 10 
HELX_P HELX_P62  AG8 PRO B 44   ? THR B 57   ? PRO B 42   THR B 55   1 ? 14 
HELX_P HELX_P63  AG9 SER B 59   ? GLY B 79   ? SER B 57   GLY B 77   1 ? 21 
HELX_P HELX_P64  AH1 VAL B 86   ? TYR B 93   ? VAL B 84   TYR B 91   1 ? 8  
HELX_P HELX_P65  AH2 SER B 96   ? ARG B 112  ? SER B 94   ARG B 110  1 ? 17 
HELX_P HELX_P66  AH3 ASP B 115  ? LYS B 126  ? ASP B 113  LYS B 124  1 ? 12 
HELX_P HELX_P67  AH4 ASN B 131  ? LEU B 136  ? ASN B 129  LEU B 134  1 ? 6  
HELX_P HELX_P68  AH5 ASN B 145  ? GLY B 155  ? ASN B 143  GLY B 153  1 ? 11 
HELX_P HELX_P69  AH6 ASN B 162  ? GLN B 196  ? ASN B 160  GLN B 194  1 ? 35 
HELX_P HELX_P70  AH7 THR B 202  ? GLY B 217  ? THR B 200  GLY B 215  1 ? 16 
HELX_P HELX_P71  AH8 THR B 231  ? ALA B 254  ? THR B 229  ALA B 252  1 ? 24 
HELX_P HELX_P72  AH9 ARG B 256  ? GLY B 261  ? ARG B 254  GLY B 259  1 ? 6  
HELX_P HELX_P73  AI1 LYS B 267  ? LEU B 271  ? LYS B 265  LEU B 269  5 ? 5  
HELX_P HELX_P74  AI2 SER B 276  ? ALA B 278  ? SER B 274  ALA B 276  5 ? 3  
HELX_P HELX_P75  AI3 GLN B 279  ? ASP B 302  ? GLN B 277  ASP B 300  1 ? 24 
HELX_P HELX_P76  AI4 GLU B 311  ? ASP B 313  ? GLU B 309  ASP B 311  5 ? 3  
HELX_P HELX_P77  AI5 ARG B 314  ? ASP B 328  ? ARG B 312  ASP B 326  1 ? 15 
HELX_P HELX_P78  AI6 GLY B 329  ? SER B 332  ? GLY B 327  SER B 330  5 ? 4  
HELX_P HELX_P79  AI7 ARG B 347  ? GLY B 363  ? ARG B 345  GLY B 361  1 ? 17 
HELX_P HELX_P80  AI8 TYR B 375  ? GLY B 387  ? TYR B 373  GLY B 385  1 ? 13 
HELX_P HELX_P81  AI9 ARG B 396  ? ALA B 413  ? ARG B 394  ALA B 411  1 ? 18 
HELX_P HELX_P82  AJ1 ASN B 426  ? ALA B 437  ? ASN B 424  ALA B 435  1 ? 12 
HELX_P HELX_P83  AJ2 GLY B 455  ? GLU B 460  ? GLY B 453  GLU B 458  1 ? 6  
HELX_P HELX_P84  AJ3 THR B 480  ? ALA B 486  ? THR B 478  ALA B 484  1 ? 7  
HELX_P HELX_P85  AJ4 TYR B 487  ? LEU B 493  ? TYR B 485  LEU B 491  1 ? 7  
HELX_P HELX_P86  AJ5 SER B 500  ? ILE B 505  ? SER B 498  ILE B 503  1 ? 6  
HELX_P HELX_P87  AJ6 SER B 511  ? ILE B 516  ? SER B 509  ILE B 514  1 ? 6  
HELX_P HELX_P88  AJ7 ASP B 518  ? ALA B 525  ? ASP B 516  ALA B 523  1 ? 8  
HELX_P HELX_P89  AJ8 LEU B 538  ? LEU B 542  ? LEU B 536  LEU B 540  5 ? 5  
HELX_P HELX_P90  AJ9 PHE B 543  ? ARG B 547  ? PHE B 541  ARG B 545  5 ? 5  
HELX_P HELX_P91  AK1 ASN B 557  ? ALA B 573  ? ASN B 555  ALA B 571  1 ? 17 
HELX_P HELX_P92  AK2 SER B 611  ? ALA B 631  ? SER B 609  ALA B 629  1 ? 21 
HELX_P HELX_P93  AK3 PRO B 633  ? ARG B 651  ? PRO B 631  ARG B 649  1 ? 19 
HELX_P HELX_P94  AK4 ARG B 651  ? GLY B 664  ? ARG B 649  GLY B 662  1 ? 14 
HELX_P HELX_P95  AK5 SER B 666  ? LEU B 692  ? SER B 664  LEU B 690  1 ? 27 
HELX_P HELX_P96  AK6 LEU B 712  ? ALA B 725  ? LEU B 710  ALA B 723  1 ? 14 
HELX_P HELX_P97  AK7 THR B 737  ? ALA B 751  ? THR B 735  ALA B 749  1 ? 15 
HELX_P HELX_P98  AK8 PRO B 754  ? SER B 756  ? PRO B 752  SER B 754  5 ? 3  
HELX_P HELX_P99  AK9 ASP B 764  ? ALA B 774  ? ASP B 762  ALA B 772  1 ? 11 
HELX_P HELX_P100 AL1 SER B 785  ? ASP B 798  ? SER B 783  ASP B 796  1 ? 14 
HELX_P HELX_P101 AL2 LEU B 826  ? ASP B 840  ? LEU B 824  ASP B 838  1 ? 15 
HELX_P HELX_P102 AL3 SER B 841  ? GLN B 844  ? SER B 839  GLN B 842  5 ? 4  
HELX_P HELX_P103 AL4 GLU B 856  ? HIS B 871  ? GLU B 854  HIS B 869  1 ? 16 
HELX_P HELX_P104 AL5 THR B 890  ? LEU B 907  ? THR B 888  LEU B 905  1 ? 18 
HELX_P HELX_P105 AL6 ALA B 917  ? GLY B 923  ? ALA B 915  GLY B 921  5 ? 7  
HELX_P HELX_P106 AL7 LYS B 935  ? LEU B 939  ? LYS B 933  LEU B 937  5 ? 5  
HELX_P HELX_P107 AL8 ARG B 954  ? ASP B 956  ? ARG B 952  ASP B 954  5 ? 3  
HELX_P HELX_P108 AL9 ASP B 957  ? ALA B 967  ? ASP B 955  ALA B 965  1 ? 11 
HELX_P HELX_P109 AM1 LEU B 980  ? ILE B 991  ? LEU B 978  ILE B 989  1 ? 12 
HELX_P HELX_P110 AM2 ARG B 1015 ? GLY B 1019 ? ARG B 1013 GLY B 1017 5 ? 5  
HELX_P HELX_P111 AM3 TYR B 1029 ? VAL B 1034 ? TYR B 1027 VAL B 1032 5 ? 6  
HELX_P HELX_P112 AM4 ASP B 1049 ? LYS B 1062 ? ASP B 1047 LYS B 1060 1 ? 14 
HELX_P HELX_P113 AM5 ALA B 1064 ? SER B 1078 ? ALA B 1062 SER B 1076 1 ? 15 
HELX_P HELX_P114 AM6 THR B 1110 ? THR B 1124 ? THR B 1108 THR B 1122 1 ? 15 
HELX_P HELX_P115 AM7 ALA B 1133 ? GLY B 1135 ? ALA B 1131 GLY B 1133 5 ? 3  
HELX_P HELX_P116 AM8 LEU B 1136 ? LYS B 1141 ? LEU B 1134 LYS B 1139 5 ? 6  
HELX_P HELX_P117 AM9 PRO B 1144 ? LEU B 1149 ? PRO B 1142 LEU B 1147 1 ? 6  
HELX_P HELX_P118 AN1 ASP B 1156 ? GLY B 1161 ? ASP B 1154 GLY B 1159 1 ? 6  
HELX_P HELX_P119 AN2 ASP B 1171 ? ALA B 1184 ? ASP B 1169 ALA B 1182 1 ? 14 
HELX_P HELX_P120 AN3 SER B 1196 ? ASN B 1203 ? SER B 1194 ASN B 1201 1 ? 8  
HELX_P HELX_P121 AN4 CYS B 1208 ? TRP B 1211 ? CYS B 1206 TRP B 1209 5 ? 4  
HELX_P HELX_P122 AN5 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 ? ? G  NAD . O2A ? ? ? 1_555 M  MG  . MG ? ? A NAD 1305 A MG  1311 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc2  metalc ? ? M  MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? A MG  1311 A HOH 1578 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc3  metalc ? ? M  MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? A MG  1311 A HOH 1745 1_555 ? ? ? ? ? ? ? 2.158 ? ? 
metalc4  metalc ? ? M  MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? A MG  1311 A HOH 1953 1_555 ? ? ? ? ? ? ? 1.959 ? ? 
metalc5  metalc ? ? M  MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? A MG  1311 A HOH 2291 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc6  metalc ? ? M  MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? A MG  1311 A HOH 2444 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc7  metalc ? ? Y  NAD . O2A ? ? ? 1_555 BA MG  . MG ? ? B NAD 1311 B MG  1314 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc8  metalc ? ? BA MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? B MG  1314 B HOH 1712 1_555 ? ? ? ? ? ? ? 1.899 ? ? 
metalc9  metalc ? ? BA MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? B MG  1314 B HOH 1940 1_555 ? ? ? ? ? ? ? 1.874 ? ? 
metalc10 metalc ? ? BA MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? B MG  1314 B HOH 2127 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc11 metalc ? ? BA MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? B MG  1314 B HOH 2269 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc12 metalc ? ? BA MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? B MG  1314 B HOH 2429 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
# 
_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 ? G  NAD . ? A NAD 1305 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 1578 ? 1_555 85.6  ? 
2  O2A ? G  NAD . ? A NAD 1305 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 1745 ? 1_555 91.1  ? 
3  O   ? CA HOH . ? A HOH 1578 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 1745 ? 1_555 93.1  ? 
4  O2A ? G  NAD . ? A NAD 1305 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 1953 ? 1_555 87.3  ? 
5  O   ? CA HOH . ? A HOH 1578 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 1953 ? 1_555 92.0  ? 
6  O   ? CA HOH . ? A HOH 1745 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 1953 ? 1_555 174.5 ? 
7  O2A ? G  NAD . ? A NAD 1305 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2291 ? 1_555 93.8  ? 
8  O   ? CA HOH . ? A HOH 1578 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2291 ? 1_555 178.3 ? 
9  O   ? CA HOH . ? A HOH 1745 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2291 ? 1_555 85.3  ? 
10 O   ? CA HOH . ? A HOH 1953 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2291 ? 1_555 89.6  ? 
11 O2A ? G  NAD . ? A NAD 1305 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2444 ? 1_555 173.5 ? 
12 O   ? CA HOH . ? A HOH 1578 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2444 ? 1_555 87.9  ? 
13 O   ? CA HOH . ? A HOH 1745 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2444 ? 1_555 89.2  ? 
14 O   ? CA HOH . ? A HOH 1953 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2444 ? 1_555 92.9  ? 
15 O   ? CA HOH . ? A HOH 2291 ? 1_555 MG ? M  MG . ? A MG 1311 ? 1_555 O ? CA HOH . ? A HOH 2444 ? 1_555 92.7  ? 
16 O2A ? Y  NAD . ? B NAD 1311 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 1712 ? 1_555 95.3  ? 
17 O2A ? Y  NAD . ? B NAD 1311 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 1940 ? 1_555 97.1  ? 
18 O   ? DA HOH . ? B HOH 1712 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 1940 ? 1_555 110.9 ? 
19 O2A ? Y  NAD . ? B NAD 1311 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2127 ? 1_555 82.5  ? 
20 O   ? DA HOH . ? B HOH 1712 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2127 ? 1_555 88.4  ? 
21 O   ? DA HOH . ? B HOH 1940 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2127 ? 1_555 160.6 ? 
22 O2A ? Y  NAD . ? B NAD 1311 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2269 ? 1_555 90.5  ? 
23 O   ? DA HOH . ? B HOH 1712 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2269 ? 1_555 160.8 ? 
24 O   ? DA HOH . ? B HOH 1940 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2269 ? 1_555 86.4  ? 
25 O   ? DA HOH . ? B HOH 2127 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2269 ? 1_555 74.2  ? 
26 O2A ? Y  NAD . ? B NAD 1311 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2429 ? 1_555 166.3 ? 
27 O   ? DA HOH . ? B HOH 1712 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2429 ? 1_555 90.0  ? 
28 O   ? DA HOH . ? B HOH 1940 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2429 ? 1_555 92.8  ? 
29 O   ? DA HOH . ? B HOH 2127 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2429 ? 1_555 85.0  ? 
30 O   ? DA HOH . ? B HOH 2269 ? 1_555 MG ? BA MG . ? B MG 1314 ? 1_555 O ? DA HOH . ? B HOH 2429 ? 1_555 80.6  ? 
# 
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 -4.13 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 0.40  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -3.96 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 2.82  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9  ? 
AA2 ? 3  ? 
AA3 ? 2  ? 
AA4 ? 5  ? 
AA5 ? 10 ? 
AA6 ? 5  ? 
AA7 ? 9  ? 
AA8 ? 3  ? 
AA9 ? 2  ? 
AB1 ? 5  ? 
AB2 ? 10 ? 
AB3 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? parallel      
AA1 8 9  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA5 1 2  ? anti-parallel 
AA5 2 3  ? parallel      
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
AA5 6 7  ? parallel      
AA5 7 8  ? parallel      
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? parallel      
AA6 2 3  ? parallel      
AA6 3 4  ? parallel      
AA6 4 5  ? parallel      
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? parallel      
AA7 8 9  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AB1 1 2  ? parallel      
AB1 2 3  ? parallel      
AB1 3 4  ? parallel      
AB1 4 5  ? parallel      
AB2 1 2  ? anti-parallel 
AB2 2 3  ? parallel      
AB2 3 4  ? parallel      
AB2 4 5  ? parallel      
AB2 5 6  ? parallel      
AB2 6 7  ? parallel      
AB2 7 8  ? parallel      
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? parallel      
AB3 2 3  ? parallel      
AB3 3 4  ? parallel      
AB3 4 5  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA1 2  GLY A 263  ? ILE A 266  ? GLY A 261  ILE A 264  
AA1 3  LEU A 305  ? ILE A 307  ? LEU A 303  ILE A 305  
AA1 4  MET A 337  ? GLN A 342  ? MET A 335  GLN A 340  
AA1 5  ILE A 366  ? VAL A 371  ? ILE A 364  VAL A 369  
AA1 6  VAL A 418  ? ALA A 423  ? VAL A 416  ALA A 421  
AA1 7  GLU A 447  ? LEU A 451  ? GLU A 445  LEU A 449  
AA1 8  CYS A 472  ? PRO A 477  ? CYS A 470  PRO A 475  
AA1 9  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA2 1  TRP A 576  ? ALA A 578  ? TRP A 574  ALA A 576  
AA2 2  ASP A 599  ? THR A 608  ? ASP A 597  THR A 606  
AA2 3  THR A 591  ? ASN A 596  ? THR A 589  ASN A 594  
AA3 1  GLN A 581  ? LEU A 582  ? GLN A 579  LEU A 580  
AA3 2  GLY A 585  ? PRO A 586  ? GLY A 583  PRO A 584  
AA4 1  LEU A 758  ? LEU A 760  ? LEU A 756  LEU A 758  
AA4 2  VAL A 729  ? LYS A 732  ? VAL A 727  LYS A 730  
AA4 3  ILE A 702  ? ILE A 705  ? ILE A 700  ILE A 703  
AA4 4  GLY A 779  ? THR A 783  ? GLY A 777  THR A 781  
AA4 5  LEU A 809  ? GLU A 812  ? LEU A 807  GLU A 810  
AA5 1  VAL A 911  ? GLN A 913  ? VAL A 909  GLN A 911  
AA5 2  THR A 929  ? GLU A 932  ? THR A 927  GLU A 930  
AA5 3  VAL A 947  ? TYR A 953  ? VAL A 945  TYR A 951  
AA5 4  LEU A 849  ? GLN A 855  ? LEU A 847  GLN A 853  
AA5 5  ASN A 817  ? VAL A 821  ? ASN A 815  VAL A 819  
AA5 6  THR A 973  ? HIS A 977  ? THR A 971  HIS A 975  
AA5 7  ASN A 995  ? ILE A 998  ? ASN A 993  ILE A 996  
AA5 8  VAL A 1213 ? ASN A 1221 ? VAL A 1211 ASN A 1219 
AA5 9  GLU A 1092 ? ALA A 1100 ? GLU A 1090 ALA A 1098 
AA5 10 ASP A 1083 ? LEU A 1086 ? ASP A 1081 LEU A 1084 
AA6 1  VAL A 1151 ? SER A 1154 ? VAL A 1149 SER A 1152 
AA6 2  SER A 1127 ? ASP A 1131 ? SER A 1125 ASP A 1129 
AA6 3  ARG A 1103 ? VAL A 1107 ? ARG A 1101 VAL A 1105 
AA6 4  GLY A 1165 ? GLU A 1169 ? GLY A 1163 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  PHE B 218  ? ASP B 223  ? PHE B 216  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  PHE B 218  ? ASP B 223  ? PHE B 216  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 VAL A 607  ? O VAL A 605  N ARG A 592  ? N ARG A 590  
AA3 1 2  N LEU A 582  ? N LEU A 580  O GLY A 585  ? O GLY A 583  
AA4 1 2  O GLN A 759  ? O GLN A 757  N ALA A 731  ? N ALA A 729  
AA4 2 3  O LYS A 732  ? O LYS A 730  N CYS A 704  ? N CYS A 702  
AA4 3 4  N VAL A 703  ? N VAL A 701  O MET A 781  ? O MET A 779  
AA4 4 5  N PHE A 782  ? N PHE A 780  O ILE A 810  ? O ILE A 808  
AA5 1 2  N GLU A 912  ? N GLU A 910  O ILE A 930  ? O ILE A 928  
AA5 2 3  N ILE A 931  ? N ILE A 929  O LEU A 948  ? O LEU A 946  
AA5 3 4  O HIS A 949  ? O HIS A 947  N LEU A 852  ? N LEU A 850  
AA5 4 5  O CYS A 853  ? O CYS A 851  N MET A 819  ? N MET A 817  
AA5 5 6  N ILE A 820  ? N ILE A 818  O HIS A 977  ? O HIS A 975  
AA5 6 7  N LEU A 976  ? N LEU A 974  O TYR A 997  ? O TYR A 995  
AA5 7 8  N LEU A 996  ? N LEU A 994  O SER A 1217 ? O SER A 1215 
AA5 8 9  O ALA A 1218 ? O ALA A 1216 N LEU A 1095 ? N LEU A 1093 
AA5 9 10 O ASN A 1094 ? O ASN A 1092 N LEU A 1086 ? N LEU A 1084 
AA6 1 2  O SER A 1152 ? O SER A 1150 N ILE A 1130 ? N ILE A 1128 
AA6 2 3  O ALA A 1129 ? O ALA A 1127 N LEU A 1106 ? N LEU A 1104 
AA6 3 4  N VAL A 1107 ? N VAL A 1105 O LEU A 1167 ? O LEU A 1165 
AA6 4 5  N VAL A 1168 ? N VAL A 1166 O GLN A 1193 ? O GLN A 1191 
AA7 1 2  N TYR B 222  ? N TYR B 220  O SER B 265  ? O SER B 263  
AA7 2 3  N ILE B 266  ? N ILE B 264  O ASN B 306  ? O ASN B 304  
AA7 3 4  N LEU B 305  ? N LEU B 303  O GLY B 338  ? O GLY B 336  
AA7 4 5  N MET B 337  ? N MET B 335  O MET B 367  ? O MET B 365  
AA7 5 6  N VAL B 368  ? N VAL B 366  O GLN B 421  ? O GLN B 419  
AA7 6 7  N PHE B 422  ? N PHE B 420  O GLU B 447  ? O GLU B 445  
AA7 7 8  N CYS B 450  ? N CYS B 448  O TYR B 475  ? O TYR B 473  
AA7 8 9  O ILE B 474  ? O ILE B 472  N SER B 219  ? N SER B 217  
AA8 1 2  N ALA B 578  ? N ALA B 576  O THR B 608  ? O THR B 606  
AA8 2 3  O GLU B 609  ? O GLU B 607  N GLU B 590  ? N GLU B 588  
AA9 1 2  N LEU B 582  ? N LEU B 580  O GLY B 585  ? O GLY B 583  
AB1 1 2  O GLN B 759  ? O GLN B 757  N ALA B 731  ? N ALA B 729  
AB1 2 3  O 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                   9E0C 
_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 GLU 674  ? ? O B HOH 1401 ? ? 2.07 
2  1 OE1 B GLN 793  ? ? O B HOH 1402 ? ? 2.08 
3  1 O   A HOH 2439 ? ? O A HOH 2582 ? ? 2.09 
4  1 O   B HOH 1405 ? ? O B HOH 2486 ? ? 2.13 
5  1 O   B HOH 1410 ? ? O B HOH 2250 ? ? 2.14 
6  1 O   A HOH 2228 ? ? O A HOH 2544 ? ? 2.15 
7  1 OD1 A ASP 796  ? ? O A HOH 1401 ? ? 2.15 
8  1 OE1 B GLU 539  ? ? O B HOH 1403 ? ? 2.16 
9  1 O   A LEU 1183 ? ? O A HOH 1402 ? ? 2.17 
10 1 OE1 A GLN 793  ? ? O A HOH 1403 ? ? 2.17 
11 1 OH  B TYR 968  ? B O B HOH 1404 ? ? 2.18 
12 1 OE1 A GLU 458  ? ? O A HOH 1404 ? ? 2.19 
13 1 O   B HOH 1485 ? ? O B HOH 2553 ? ? 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     1407 
_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     2315 
_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              2.18 
# 
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   ? ? -156.64 56.73   
2  1 ASP A 127  ? ? -89.98  46.93   
3  1 GLU A 225  ? ? -174.70 145.39  
4  1 GLU A 308  ? ? -121.06 -134.38 
5  1 MET A 452  ? ? -148.50 -49.79  
6  1 VAL A 460  ? ? -120.40 -53.09  
7  1 LYS A 465  ? ? -115.10 -124.21 
8  1 ASP A 597  ? ? -169.43 99.51   
9  1 THR A 689  ? ? -130.70 -47.33  
10 1 THR A 811  ? ? -125.44 -156.35 
11 1 GLN A 842  ? ? -94.80  51.91   
12 1 GLN A 938  ? ? -106.05 -63.23  
13 1 LEU A 970  ? ? -96.82  -89.22  
14 1 VAL A 1004 ? A -59.64  109.43  
15 1 GLN A 1008 ? ? -117.89 78.54   
16 1 ALA B 22   ? ? -158.03 60.66   
17 1 ASN B 129  ? ? -68.55  61.72   
18 1 LEU B 223  ? ? 77.96   -0.72   
19 1 GLU B 308  ? ? -117.76 -134.57 
20 1 MET B 452  ? ? -139.95 -45.43  
21 1 VAL B 460  ? ? -123.30 -51.39  
22 1 LYS B 465  ? ? -120.66 -129.93 
23 1 ASP B 597  ? ? -167.89 99.63   
24 1 THR B 689  ? ? -130.87 -44.93  
25 1 HIS B 694  ? ? -100.48 77.95   
26 1 THR B 811  ? ? -123.17 -155.21 
27 1 GLN B 842  ? ? -93.45  55.33   
28 1 LEU B 970  ? ? -98.65  -87.33  
29 1 GLN B 1008 ? ? -115.65 79.04   
# 
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 -25.7067 66.1915 92.6346 0.1402 ? 0.0189  ? 0.0160 ? 0.1249 ? 0.0053  ? 0.1231 ? 0.5990 ? -0.0260 
? 0.1621 ? 0.1048 ? -0.0149 ? 0.1131 ? -0.0312 ? -0.1039 ? 0.0058  ? 0.0308 ? 0.0379 ? 0.0108  ? -0.0178 ? -0.0196 ? -0.0064 ? 
2 'X-RAY DIFFRACTION' ? refined 5.6454   31.5967 91.1531 0.1024 ? -0.0023 ? 0.0006 ? 0.1109 ? -0.0119 ? 0.1074 ? 0.1860 ? -0.0152 
? 0.0824 ? 0.2108 ? -0.0463 ? 0.3925 ? 0.0160  ? -0.0356 ? -0.0079 ? 0.0483 ? 0.0061 ? -0.0036 ? 0.0443  ? -0.0863 ? -0.0238 ? 
# 
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 2693 ? 5.83 . 
2 1 O ? A HOH 2694 ? 5.85 . 
3 1 O ? A HOH 2695 ? 5.88 . 
4 1 O ? B HOH 2680 ? 5.96 . 
5 1 O ? B HOH 2681 ? 6.00 . 
6 1 O ? B HOH 2682 ? 6.48 . 
# 
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 B SER -1  ? B SER 1   
21 1 Y 1 B MET 0   ? B MET 2   
22 1 Y 1 B MET 1   ? B MET 3   
23 1 Y 1 B SER 2   ? B SER 4   
24 1 Y 1 B PRO 3   ? B PRO 5   
25 1 Y 1 B ASN 4   ? B ASN 6   
26 1 Y 1 B PRO 5   ? B PRO 7   
27 1 Y 1 B LEU 6   ? B LEU 8   
28 1 Y 1 B GLN 7   ? B GLN 9   
29 1 Y 1 B LYS 8   ? B LYS 10  
30 1 Y 1 B PRO 9   ? B PRO 11  
31 1 Y 1 B ALA 10  ? B ALA 12  
32 1 Y 1 B ILE 11  ? B ILE 13  
33 1 Y 1 B ASP 12  ? B ASP 14  
34 1 Y 1 B ALA 13  ? B ALA 15  
35 1 Y 1 B SER 80  ? B SER 82  
36 1 Y 1 B GLY 81  ? B GLY 83  
37 1 Y 1 B SER 82  ? B SER 84  
38 1 Y 1 B GLY 135 ? B GLY 137 
39 1 Y 1 B GLY 136 ? B GLY 138 
40 1 Y 1 B SER 137 ? B SER 139 
41 1 Y 1 B GLU 492 ? B GLU 494 
42 1 Y 1 B ASN 493 ? B ASN 495 
43 1 Y 1 B GLY 494 ? B GLY 496 
44 1 Y 1 B GLY 913 ? B GLY 915 
# 
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  
A1BDX C02    C  N N 39  
A1BDX C03    C  Y N 40  
A1BDX C04    C  Y N 41  
A1BDX C05    C  Y N 42  
A1BDX C06    C  Y N 43  
A1BDX C08    C  Y N 44  
A1BDX C09    C  Y N 45  
A1BDX C10    C  Y N 46  
A1BDX C11    C  Y N 47  
A1BDX O01    O  N N 48  
A1BDX O07    O  Y N 49  
A1BDX H1     H  N N 50  
A1BDX H2     H  N N 51  
A1BDX H3     H  N N 52  
A1BDX H4     H  N N 53  
A1BDX H5     H  N N 54  
A1BDX H6     H  N N 55  
A1BDX H7     H  N N 56  
A1BDX 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  
A1BDX C02   O01    sing N N 38  
A1BDX C02   C03    sing N N 39  
A1BDX C04   C03    sing Y N 40  
A1BDX C04   C05    doub Y N 41  
A1BDX C03   C11    doub Y N 42  
A1BDX C05   C06    sing Y N 43  
A1BDX C11   C10    sing Y N 44  
A1BDX C06   C10    doub Y N 45  
A1BDX C06   O07    sing Y N 46  
A1BDX C10   C09    sing Y N 47  
A1BDX O07   C08    sing Y N 48  
A1BDX C09   C08    doub Y N 49  
A1BDX C02   H1     sing N N 50  
A1BDX C02   H2     sing N N 51  
A1BDX C04   H3     sing N N 52  
A1BDX C05   H4     sing N N 53  
A1BDX C08   H5     sing N N 54  
A1BDX C09   H6     sing N N 55  
A1BDX C11   H7     sing N N 56  
A1BDX 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                    9E0C 
_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]   0.009963 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002937 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009838 
_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]   0.008279 
_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   ? -49.088 93.685  103.850 1.00 45.93 ? 14   ALA   A N     1 
ATOM   2     C  CA    . ALA   A  1  16   ? -48.118 92.608  103.676 1.00 45.29 ? 14   ALA   A CA    1 
ATOM   3     C  C     . ALA   A  1  16   ? -48.799 91.249  103.786 1.00 44.13 ? 14   ALA   A C     1 
ATOM   4     O  O     . ALA   A  1  16   ? -49.538 91.001  104.734 1.00 40.49 ? 14   ALA   A O     1 
ATOM   5     C  CB    . ALA   A  1  16   ? -47.002 92.724  104.705 1.00 46.86 ? 14   ALA   A CB    1 
ATOM   6     N  N     . PRO   A  1  17   ? -48.551 90.370  102.816 1.00 42.90 ? 15   PRO   A N     1 
ATOM   7     C  CA    . PRO   A  1  17   ? -49.149 89.031  102.876 1.00 36.70 ? 15   PRO   A CA    1 
ATOM   8     C  C     . PRO   A  1  17   ? -48.627 88.261  104.079 1.00 37.98 ? 15   PRO   A C     1 
ATOM   9     O  O     . PRO   A  1  17   ? -47.457 88.371  104.450 1.00 32.88 ? 15   PRO   A O     1 
ATOM   10    C  CB    . PRO   A  1  17   ? -48.711 88.384  101.556 1.00 38.44 ? 15   PRO   A CB    1 
ATOM   11    C  CG    . PRO   A  1  17   ? -47.504 89.157  101.132 1.00 42.65 ? 15   PRO   A CG    1 
ATOM   12    C  CD    . PRO   A  1  17   ? -47.726 90.560  101.611 1.00 39.48 ? 15   PRO   A CD    1 
ATOM   13    N  N     . ALA   A  1  18   ? -49.516 87.494  104.700 1.00 32.04 ? 16   ALA   A N     1 
ATOM   14    C  CA    . ALA   A  1  18   ? -49.144 86.766  105.901 1.00 30.26 ? 16   ALA   A CA    1 
ATOM   15    C  C     . ALA   A  1  18   ? -48.084 85.722  105.555 1.00 27.19 ? 16   ALA   A C     1 
ATOM   16    O  O     . ALA   A  1  18   ? -48.124 85.133  104.471 1.00 25.99 ? 16   ALA   A O     1 
ATOM   17    C  CB    . ALA   A  1  18   ? -50.372 86.082  106.504 1.00 34.62 ? 16   ALA   A CB    1 
ATOM   18    N  N     . PRO   A  1  19   ? -47.127 85.476  106.443 1.00 25.38 ? 17   PRO   A N     1 
ATOM   19    C  CA    . PRO   A  1  19   ? -46.056 84.527  106.125 1.00 24.58 ? 17   PRO   A CA    1 
ATOM   20    C  C     . PRO   A  1  19   ? -46.614 83.131  105.911 1.00 23.50 ? 17   PRO   A C     1 
ATOM   21    O  O     . PRO   A  1  19   ? -47.407 82.630  106.712 1.00 27.61 ? 17   PRO   A O     1 
ATOM   22    C  CB    . PRO   A  1  19   ? -45.151 84.587  107.362 1.00 28.05 ? 17   PRO   A CB    1 
ATOM   23    C  CG    . PRO   A  1  19   ? -45.459 85.902  107.993 1.00 29.75 ? 17   PRO   A CG    1 
ATOM   24    C  CD    . PRO   A  1  19   ? -46.912 86.145  107.737 1.00 26.95 ? 17   PRO   A CD    1 
ATOM   25    N  N     . PHE   A  1  20   ? -46.210 82.516  104.800 1.00 21.90 ? 18   PHE   A N     1 
ATOM   26    C  CA    . PHE   A  1  20   ? -46.559 81.149  104.436 1.00 24.11 ? 18   PHE   A CA    1 
ATOM   27    C  C     . PHE   A  1  20   ? -48.041 80.962  104.148 1.00 25.09 ? 18   PHE   A C     1 
ATOM   28    O  O     . PHE   A  1  20   ? -48.502 79.821  104.055 1.00 25.60 ? 18   PHE   A O     1 
ATOM   29    C  CB    . PHE   A  1  20   ? -46.078 80.128  105.473 1.00 23.10 ? 18   PHE   A CB    1 
ATOM   30    C  CG    . PHE   A  1  20   ? -44.603 80.194  105.742 1.00 22.74 ? 18   PHE   A CG    1 
ATOM   31    C  CD1   . PHE   A  1  20   ? -43.704 79.669  104.836 1.00 22.61 ? 18   PHE   A CD1   1 
ATOM   32    C  CD2   . PHE   A  1  20   ? -44.119 80.778  106.903 1.00 23.45 ? 18   PHE   A CD2   1 
ATOM   33    C  CE1   . PHE   A  1  20   ? -42.340 79.723  105.078 1.00 22.91 ? 18   PHE   A CE1   1 
ATOM   34    C  CE2   . PHE   A  1  20   ? -42.758 80.831  107.153 1.00 25.71 ? 18   PHE   A CE2   1 
ATOM   35    C  CZ    . PHE   A  1  20   ? -41.871 80.306  106.242 1.00 26.46 ? 18   PHE   A CZ    1 
ATOM   36    N  N     . ALA   A  1  21   ? -48.796 82.045  103.999 1.00 25.29 ? 19   ALA   A N     1 
ATOM   37    C  CA    . ALA   A  1  21   ? -50.217 81.909  103.704 1.00 24.73 ? 19   ALA   A CA    1 
ATOM   38    C  C     . ALA   A  1  21   ? -50.466 81.318  102.325 1.00 30.39 ? 19   ALA   A C     1 
ATOM   39    O  O     . ALA   A  1  21   ? -51.551 80.785  102.079 1.00 29.89 ? 19   ALA   A O     1 
ATOM   40    C  CB    . ALA   A  1  21   ? -50.917 83.261  103.852 1.00 28.27 ? 19   ALA   A CB    1 
ATOM   41    N  N     . ASP   A  1  22   ? -49.491 81.387  101.429 1.00 24.66 ? 20   ASP   A N     1 
ATOM   42    C  CA    . ASP   A  1  22   ? -49.615 80.844  100.084 1.00 28.05 ? 20   ASP   A CA    1 
ATOM   43    C  C     . ASP   A  1  22   ? -48.441 79.933  99.780  1.00 21.01 ? 20   ASP   A C     1 
ATOM   44    O  O     . ASP   A  1  22   ? -47.932 79.903  98.658  1.00 23.86 ? 20   ASP   A O     1 
ATOM   45    C  CB    . ASP   A  1  22   ? -49.703 81.956  99.040  1.00 31.12 ? 20   ASP   A CB    1 
ATOM   46    C  CG    . ASP   A  1  22   ? -50.946 82.819  99.198  1.00 43.57 ? 20   ASP   A CG    1 
ATOM   47    O  OD1   . ASP   A  1  22   ? -51.919 82.373  99.840  1.00 46.84 ? 20   ASP   A OD1   1 
ATOM   48    O  OD2   . ASP   A  1  22   ? -50.952 83.949  98.664  1.00 54.32 ? 20   ASP   A OD2   1 
ATOM   49    N  N     . PHE   A  1  23   ? -47.987 79.181  100.784 1.00 19.11 ? 21   PHE   A N     1 
ATOM   50    C  CA    . PHE   A  1  23   ? -46.723 78.466  100.645 1.00 18.48 ? 21   PHE   A CA    1 
ATOM   51    C  C     . PHE   A  1  23   ? -46.770 77.448  99.511  1.00 19.07 ? 21   PHE   A C     1 
ATOM   52    O  O     . PHE   A  1  23   ? -45.930 77.471  98.605  1.00 19.97 ? 21   PHE   A O     1 
ATOM   53    C  CB    . PHE   A  1  23   ? -46.339 77.787  101.955 1.00 19.47 ? 21   PHE   A CB    1 
ATOM   54    C  CG    . PHE   A  1  23   ? -45.128 76.919  101.821 1.00 18.17 ? 21   PHE   A CG    1 
ATOM   55    C  CD1   . PHE   A  1  23   ? -43.913 77.468  101.446 1.00 20.01 ? 21   PHE   A CD1   1 
ATOM   56    C  CD2   . PHE   A  1  23   ? -45.204 75.553  102.041 1.00 19.05 ? 21   PHE   A CD2   1 
ATOM   57    C  CE1   . PHE   A  1  23   ? -42.779 76.674  101.295 1.00 20.70 ? 21   PHE   A CE1   1 
ATOM   58    C  CE2   . PHE   A  1  23   ? -44.074 74.751  101.897 1.00 20.41 ? 21   PHE   A CE2   1 
ATOM   59    C  CZ    . PHE   A  1  23   ? -42.861 75.314  101.519 1.00 21.24 ? 21   PHE   A CZ    1 
ATOM   60    N  N     . ALA   A  1  24   ? -47.724 76.526  99.562  1.00 18.92 ? 22   ALA   A N     1 
ATOM   61    C  CA    . ALA   A  1  24   ? -47.756 75.465  98.562  1.00 19.31 ? 22   ALA   A CA    1 
ATOM   62    C  C     . ALA   A  1  24   ? -49.158 74.887  98.427  1.00 19.57 ? 22   ALA   A C     1 
ATOM   63    O  O     . ALA   A  1  24   ? -49.347 73.672  98.577  1.00 19.09 ? 22   ALA   A O     1 
ATOM   64    C  CB    . ALA   A  1  24   ? -46.771 74.353  98.925  1.00 21.91 ? 22   ALA   A CB    1 
ATOM   65    N  N     . PRO   A  1  25   ? -50.160 75.706  98.128  1.00 21.34 ? 23   PRO   A N     1 
ATOM   66    C  CA    . PRO   A  1  25   ? -51.518 75.185  98.034  1.00 23.19 ? 23   PRO   A CA    1 
ATOM   67    C  C     . PRO   A  1  25   ? -51.607 74.187  96.897  1.00 21.52 ? 23   PRO   A C     1 
ATOM   68    O  O     . PRO   A  1  25   ? -51.020 74.401  95.827  1.00 21.03 ? 23   PRO   A O     1 
ATOM   69    C  CB    . PRO   A  1  25   ? -52.350 76.439  97.736  1.00 24.17 ? 23   PRO   A CB    1 
ATOM   70    C  CG    . PRO   A  1  25   ? -51.417 77.336  97.025  1.00 23.92 ? 23   PRO   A CG    1 
ATOM   71    C  CD    . PRO   A  1  25   ? -50.077 77.109  97.678  1.00 22.69 ? 23   PRO   A CD    1 
ATOM   72    N  N     . PRO   A  1  26   ? -52.288 73.067  97.101  1.00 20.69 ? 24   PRO   A N     1 
ATOM   73    C  CA    . PRO   A  1  26   ? -52.409 72.078  96.025  1.00 20.66 ? 24   PRO   A CA    1 
ATOM   74    C  C     . PRO   A  1  26   ? -53.238 72.626  94.877  1.00 19.38 ? 24   PRO   A C     1 
ATOM   75    O  O     . PRO   A  1  26   ? -54.043 73.549  95.034  1.00 20.81 ? 24   PRO   A O     1 
ATOM   76    C  CB    . PRO   A  1  26   ? -53.114 70.897  96.699  1.00 22.83 ? 24   PRO   A CB    1 
ATOM   77    C  CG    . PRO   A  1  26   ? -53.868 71.522  97.833  1.00 27.85 ? 24   PRO   A CG    1 
ATOM   78    C  CD    . PRO   A  1  26   ? -53.011 72.666  98.316  1.00 21.99 ? 24   PRO   A CD    1 
ATOM   79    N  N     . VAL   A  1  27   ? -53.020 72.035  93.699  1.00 19.16 ? 25   VAL   A N     1 
ATOM   80    C  CA    . VAL   A  1  27   ? -53.795 72.397  92.514  1.00 20.27 ? 25   VAL   A CA    1 
ATOM   81    C  C     . VAL   A  1  27   ? -55.282 72.280  92.798  1.00 21.94 ? 25   VAL   A C     1 
ATOM   82    O  O     . VAL   A  1  27   ? -56.078 73.144  92.409  1.00 22.37 ? 25   VAL   A O     1 
ATOM   83    C  CB    . VAL   A  1  27   ? -53.378 71.518  91.320  1.00 19.57 ? 25   VAL   A CB    1 
ATOM   84    C  CG1   . VAL   A  1  27   ? -54.345 71.697  90.164  1.00 22.31 ? 25   VAL   A CG1   1 
ATOM   85    C  CG2   . VAL   A  1  27   ? -51.952 71.842  90.893  1.00 20.74 ? 25   VAL   A CG2   1 
ATOM   86    N  N     . ARG   A  1  28   ? -55.677 71.225  93.501  1.00 22.18 ? 26   ARG   A N     1 
ATOM   87    C  CA    . ARG   A  1  28   ? -57.073 70.990  93.834  1.00 22.85 ? 26   ARG   A CA    1 
ATOM   88    C  C     . ARG   A  1  28   ? -57.123 70.294  95.184  1.00 26.35 ? 26   ARG   A C     1 
ATOM   89    O  O     . ARG   A  1  28   ? -56.124 69.709  95.622  1.00 22.88 ? 26   ARG   A O     1 
ATOM   90    C  CB    . ARG   A  1  28   ? -57.739 70.115  92.763  1.00 26.71 ? 26   ARG   A CB    1 
ATOM   91    C  CG    . ARG   A  1  28   ? -57.235 68.680  92.743  1.00 27.10 ? 26   ARG   A CG    1 
ATOM   92    C  CD    . ARG   A  1  28   ? -57.760 67.899  91.542  1.00 27.47 ? 26   ARG   A CD    1 
ATOM   93    N  NE    . ARG   A  1  28   ? -57.099 68.300  90.305  1.00 30.67 ? 26   ARG   A NE    1 
ATOM   94    C  CZ    . ARG   A  1  28   ? -57.606 69.156  89.429  1.00 34.44 ? 26   ARG   A CZ    1 
ATOM   95    N  NH1   . ARG   A  1  28   ? -58.808 69.684  89.593  1.00 33.95 ? 26   ARG   A NH1   1 
ATOM   96    N  NH2   . ARG   A  1  28   ? -56.883 69.500  88.369  1.00 27.25 ? 26   ARG   A NH2   1 
ATOM   97    N  N     . PRO   A  1  29   ? -58.263 70.346  95.880  1.00 23.44 ? 27   PRO   A N     1 
ATOM   98    C  CA    . PRO   A  1  29   ? -58.390 69.559  97.110  1.00 23.54 ? 27   PRO   A CA    1 
ATOM   99    C  C     . PRO   A  1  29   ? -58.199 68.086  96.787  1.00 23.15 ? 27   PRO   A C     1 
ATOM   100   O  O     . PRO   A  1  29   ? -58.667 67.589  95.764  1.00 23.56 ? 27   PRO   A O     1 
ATOM   101   C  CB    . PRO   A  1  29   ? -59.822 69.851  97.579  1.00 25.64 ? 27   PRO   A CB    1 
ATOM   102   C  CG    . PRO   A  1  29   ? -60.186 71.140  96.918  1.00 26.78 ? 27   PRO   A CG    1 
ATOM   103   C  CD    . PRO   A  1  29   ? -59.478 71.133  95.599  1.00 26.10 ? 27   PRO   A CD    1 
ATOM   104   N  N     . GLN   A  1  30   ? -57.493 67.392  97.665  1.00 23.37 ? 28   GLN   A N     1 
ATOM   105   C  CA    . GLN   A  1  30   ? -57.107 66.016  97.387  1.00 23.74 ? 28   GLN   A CA    1 
ATOM   106   C  C     . GLN   A  1  30   ? -58.264 65.085  97.728  1.00 25.50 ? 28   GLN   A C     1 
ATOM   107   O  O     . GLN   A  1  30   ? -58.679 65.001  98.887  1.00 26.04 ? 28   GLN   A O     1 
ATOM   108   C  CB    . GLN   A  1  30   ? -55.862 65.666  98.194  1.00 23.36 ? 28   GLN   A CB    1 
ATOM   109   C  CG    . GLN   A  1  30   ? -54.700 66.591  97.897  1.00 20.81 ? 28   GLN   A CG    1 
ATOM   110   C  CD    . GLN   A  1  30   ? -54.190 66.420  96.487  1.00 22.57 ? 28   GLN   A CD    1 
ATOM   111   O  OE1   . GLN   A  1  30   ? -53.509 65.443  96.186  1.00 20.36 ? 28   GLN   A OE1   1 
ATOM   112   N  NE2   . GLN   A  1  30   ? -54.520 67.359  95.611  1.00 20.85 ? 28   GLN   A NE2   1 
ATOM   113   N  N     . SER   A  1  31   ? -58.777 64.391  96.718  1.00 23.05 ? 29   SER   A N     1 
ATOM   114   C  CA    . SER   A  1  31   ? -59.857 63.440  96.922  1.00 20.59 ? 29   SER   A CA    1 
ATOM   115   C  C     . SER   A  1  31   ? -59.346 62.241  97.709  1.00 23.32 ? 29   SER   A C     1 
ATOM   116   O  O     . SER   A  1  31   ? -58.139 62.053  97.898  1.00 21.85 ? 29   SER   A O     1 
ATOM   117   C  CB    . SER   A  1  31   ? -60.372 62.949  95.574  1.00 22.19 ? 29   SER   A CB    1 
ATOM   118   O  OG    . SER   A  1  31   ? -59.387 62.133  94.946  1.00 20.13 ? 29   SER   A OG    1 
ATOM   119   N  N     . THR   A  1  32   ? -60.288 61.413  98.167  1.00 22.93 ? 30   THR   A N     1 
ATOM   120   C  CA    . THR   A  1  32   ? -59.926 60.166  98.828  1.00 21.42 ? 30   THR   A CA    1 
ATOM   121   C  C     . THR   A  1  32   ? -58.983 59.343  97.958  1.00 20.61 ? 30   THR   A C     1 
ATOM   122   O  O     . THR   A  1  32   ? -57.980 58.814  98.439  1.00 21.52 ? 30   THR   A O     1 
ATOM   123   C  CB    . THR   A  1  32   ? -61.193 59.370  99.158  1.00 23.80 ? 30   THR   A CB    1 
ATOM   124   O  OG1   . THR   A  1  32   ? -62.038 60.159  100.002 1.00 29.76 ? 30   THR   A OG1   1 
ATOM   125   C  CG2   . THR   A  1  32   ? -60.840 58.078  99.866  1.00 27.85 ? 30   THR   A CG2   1 
ATOM   126   N  N     . LEU   A  1  33   ? -59.289 59.233  96.668  1.00 19.11 ? 31   LEU   A N     1 
ATOM   127   C  CA    . LEU   A  1  33   ? -58.440 58.441  95.788  1.00 18.43 ? 31   LEU   A CA    1 
ATOM   128   C  C     . LEU   A  1  33   ? -57.073 59.083  95.615  1.00 19.46 ? 31   LEU   A C     1 
ATOM   129   O  O     . LEU   A  1  33   ? -56.056 58.382  95.551  1.00 19.36 ? 31   LEU   A O     1 
ATOM   130   C  CB    . LEU   A  1  33   ? -59.123 58.248  94.441  1.00 19.51 ? 31   LEU   A CB    1 
ATOM   131   C  CG    . LEU   A  1  33   ? -60.268 57.241  94.502  1.00 21.49 ? 31   LEU   A CG    1 
ATOM   132   C  CD1   . LEU   A  1  33   ? -61.102 57.324  93.247  1.00 21.74 ? 31   LEU   A CD1   1 
ATOM   133   C  CD2   . LEU   A  1  33   ? -59.740 55.826  94.711  1.00 27.15 ? 31   LEU   A CD2   1 
ATOM   134   N  N     . ARG   A  1  34   ? -57.024 60.413  95.527  1.00 18.10 ? 32   ARG   A N     1 
ATOM   135   C  CA    . ARG   A  1  34   ? -55.723 61.066  95.412  1.00 18.30 ? 32   ARG   A CA    1 
ATOM   136   C  C     . ARG   A  1  34   ? -54.922 60.898  96.690  1.00 17.66 ? 32   ARG   A C     1 
ATOM   137   O  O     . ARG   A  1  34   ? -53.708 60.676  96.643  1.00 18.54 ? 32   ARG   A O     1 
ATOM   138   C  CB    . ARG   A  1  34   ? -55.897 62.543  95.078  1.00 19.43 ? 32   ARG   A CB    1 
ATOM   139   C  CG    . ARG   A  1  34   ? -56.304 62.809  93.643  1.00 20.02 ? 32   ARG   A CG    1 
ATOM   140   C  CD    . ARG   A  1  34   ? -55.157 62.538  92.674  1.00 18.70 ? 32   ARG   A CD    1 
ATOM   141   N  NE    . ARG   A  1  34   ? -54.051 63.483  92.804  1.00 19.70 ? 32   ARG   A NE    1 
ATOM   142   C  CZ    . ARG   A  1  34   ? -53.974 64.653  92.180  1.00 20.57 ? 32   ARG   A CZ    1 
ATOM   143   N  NH1   . ARG   A  1  34   ? -54.937 65.076  91.365  1.00 20.97 ? 32   ARG   A NH1   1 
ATOM   144   N  NH2   . ARG   A  1  34   ? -52.902 65.419  92.367  1.00 21.59 ? 32   ARG   A NH2   1 
ATOM   145   N  N     . ARG   A  1  35   ? -55.589 60.978  97.842  1.00 18.75 ? 33   ARG   A N     1 
ATOM   146   C  CA    . ARG   A  1  35   ? -54.890 60.836  99.112  1.00 19.66 ? 33   ARG   A CA    1 
ATOM   147   C  C     . ARG   A  1  35   ? -54.326 59.434  99.278  1.00 19.06 ? 33   ARG   A C     1 
ATOM   148   O  O     . ARG   A  1  35   ? -53.262 59.264  99.883  1.00 20.24 ? 33   ARG   A O     1 
ATOM   149   C  CB    . ARG   A  1  35   ? -55.829 61.183  100.271 1.00 23.16 ? 33   ARG   A CB    1 
ATOM   150   C  CG    . ARG   A  1  35   ? -56.178 62.666  100.336 1.00 23.26 ? 33   ARG   A CG    1 
ATOM   151   C  CD    . ARG   A  1  35   ? -57.223 62.954  101.418 1.00 26.99 ? 33   ARG   A CD    1 
ATOM   152   C  CZ    . ARG   A  1  35   ? -56.318 66.269  101.992 1.00 34.18 ? 33   ARG   A CZ    1 
ATOM   153   N  N     . ALA   A  1  36   ? -55.027 58.424  98.758  1.00 19.92 ? 34   ALA   A N     1 
ATOM   154   C  CA    . ALA   A  1  36   ? -54.517 57.062  98.836  1.00 21.04 ? 34   ALA   A CA    1 
ATOM   155   C  C     . ALA   A  1  36   ? -53.252 56.906  98.014  1.00 20.24 ? 34   ALA   A C     1 
ATOM   156   O  O     . ALA   A  1  36   ? -52.357 56.148  98.393  1.00 21.05 ? 34   ALA   A O     1 
ATOM   157   C  CB    . ALA   A  1  36   ? -55.575 56.063  98.373  1.00 21.60 ? 34   ALA   A CB    1 
ATOM   158   N  N     . ILE   A  1  37   ? -53.155 57.634  96.904  1.00 17.13 ? 35   ILE   A N     1 
ATOM   159   C  CA    . ILE   A  1  37   ? -51.914 57.660  96.136  1.00 16.27 ? 35   ILE   A CA    1 
ATOM   160   C  C     . ILE   A  1  37   ? -50.791 58.243  96.975  1.00 16.88 ? 35   ILE   A C     1 
ATOM   161   O  O     . ILE   A  1  37   ? -49.731 57.633  97.140  1.00 17.71 ? 35   ILE   A O     1 
ATOM   162   C  CB    . ILE   A  1  37   ? -52.107 58.452  94.836  1.00 17.17 ? 35   ILE   A CB    1 
ATOM   163   C  CG1   . ILE   A  1  37   ? -53.082 57.728  93.916  1.00 16.94 ? 35   ILE   A CG1   1 
ATOM   164   C  CG2   . ILE   A  1  37   ? -50.761 58.626  94.142  1.00 15.35 ? 35   ILE   A CG2   1 
ATOM   165   C  CD1   . ILE   A  1  37   ? -53.518 58.581  92.728  1.00 17.39 ? 35   ILE   A CD1   1 
ATOM   166   N  N     . THR   A  1  38   ? -51.000 59.446  97.506  1.00 17.13 ? 36   THR   A N     1 
ATOM   167   C  CA    . THR   A  1  38   ? -49.926 60.096  98.244  1.00 17.73 ? 36   THR   A CA    1 
ATOM   168   C  C     . THR   A  1  38   ? -49.498 59.261  99.441  1.00 19.14 ? 36   THR   A C     1 
ATOM   169   O  O     . THR   A  1  38   ? -48.304 59.188  99.759  1.00 18.83 ? 36   THR   A O     1 
ATOM   170   C  CB    . THR   A  1  38   ? -50.387 61.477  98.682  1.00 17.88 ? 36   THR   A CB    1 
ATOM   171   O  OG1   . THR   A  1  38   ? -50.889 62.183  97.540  1.00 18.33 ? 36   THR   A OG1   1 
ATOM   172   C  CG2   . THR   A  1  38   ? -49.241 62.248  99.287  1.00 20.13 ? 36   THR   A CG2   1 
ATOM   173   N  N     . ALA   A  1  39   ? -50.451 58.582  100.082 1.00 18.60 ? 37   ALA   A N     1 
ATOM   174   C  CA    . ALA   A  1  39   ? -50.129 57.775  101.249 1.00 18.78 ? 37   ALA   A CA    1 
ATOM   175   C  C     . ALA   A  1  39   ? -49.188 56.620  100.936 1.00 21.00 ? 37   ALA   A C     1 
ATOM   176   O  O     . ALA   A  1  39   ? -48.480 56.156  101.838 1.00 22.88 ? 37   ALA   A O     1 
ATOM   177   C  CB    . ALA   A  1  39   ? -51.422 57.240  101.873 1.00 20.74 ? 37   ALA   A CB    1 
ATOM   178   N  N     . ALA   A  1  40   ? -49.146 56.158  99.690  1.00 18.28 ? 38   ALA   A N     1 
ATOM   179   C  CA    . ALA   A  1  40   ? -48.305 55.031  99.305  1.00 19.43 ? 38   ALA   A CA    1 
ATOM   180   C  C     . ALA   A  1  40   ? -46.948 55.457  98.770  1.00 18.64 ? 38   ALA   A C     1 
ATOM   181   O  O     . ALA   A  1  40   ? -46.132 54.587  98.438  1.00 19.13 ? 38   ALA   A O     1 
ATOM   182   C  CB    . ALA   A  1  40   ? -49.013 54.184  98.248  1.00 19.37 ? 38   ALA   A CB    1 
ATOM   183   N  N     . TYR   A  1  41   ? -46.686 56.765  98.698  1.00 16.91 ? 39   TYR   A N     1 
ATOM   184   C  CA    . TYR   A  1  41   ? -45.526 57.290  97.979  1.00 17.47 ? 39   TYR   A CA    1 
ATOM   185   C  C     . TYR   A  1  41   ? -44.244 56.556  98.354  1.00 18.13 ? 39   TYR   A C     1 
ATOM   186   O  O     . TYR   A  1  41   ? -43.500 56.085  97.484  1.00 17.74 ? 39   TYR   A O     1 
ATOM   187   C  CB    . TYR   A  1  41   ? -45.427 58.783  98.285  1.00 16.42 ? 39   TYR   A CB    1 
ATOM   188   C  CG    . TYR   A  1  41   ? -44.670 59.655  97.298  1.00 16.73 ? 39   TYR   A CG    1 
ATOM   189   C  CD1   . TYR   A  1  41   ? -43.588 59.175  96.578  1.00 16.46 ? 39   TYR   A CD1   1 
ATOM   190   C  CD2   . TYR   A  1  41   ? -45.032 60.984  97.121  1.00 17.58 ? 39   TYR   A CD2   1 
ATOM   191   C  CE1   . TYR   A  1  41   ? -42.885 60.000  95.703  1.00 16.19 ? 39   TYR   A CE1   1 
ATOM   192   C  CE2   . TYR   A  1  41   ? -44.348 61.809  96.255  1.00 18.81 ? 39   TYR   A CE2   1 
ATOM   193   C  CZ    . TYR   A  1  41   ? -43.272 61.313  95.551  1.00 17.05 ? 39   TYR   A CZ    1 
ATOM   194   O  OH    . TYR   A  1  41   ? -42.586 62.142  94.695  1.00 17.06 ? 39   TYR   A OH    1 
ATOM   195   N  N     . ARG   A  1  42   ? -43.972 56.439  99.648  1.00 18.10 ? 40   ARG   A N     1 
ATOM   196   C  CA    . ARG   A  1  42   ? -42.757 55.786  100.116 1.00 19.82 ? 40   ARG   A CA    1 
ATOM   197   C  C     . ARG   A  1  42   ? -43.084 54.683  101.112 1.00 18.53 ? 40   ARG   A C     1 
ATOM   198   O  O     . ARG   A  1  42   ? -42.325 54.434  102.059 1.00 22.27 ? 40   ARG   A O     1 
ATOM   199   C  CB    . ARG   A  1  42   ? -41.767 56.806  100.668 1.00 21.69 ? 40   ARG   A CB    1 
ATOM   200   C  CG    . ARG   A  1  42   ? -41.313 57.758  99.586  1.00 20.46 ? 40   ARG   A CG    1 
ATOM   201   C  CD    . ARG   A  1  42   ? -40.491 58.880  100.112 1.00 21.72 ? 40   ARG   A CD    1 
ATOM   202   N  NE    . ARG   A  1  42   ? -40.495 59.928  99.106  1.00 20.28 ? 40   ARG   A NE    1 
ATOM   203   C  CZ    . ARG   A  1  42   ? -39.671 59.973  98.071  1.00 18.41 ? 40   ARG   A CZ    1 
ATOM   204   N  NH1   . ARG   A  1  42   ? -38.670 59.109  97.945  1.00 20.04 ? 40   ARG   A NH1   1 
ATOM   205   N  NH2   . ARG   A  1  42   ? -39.857 60.903  97.138  1.00 18.38 ? 40   ARG   A NH2   1 
ATOM   206   N  N     . ARG   A  1  43   ? -44.206 54.013  100.889 1.00 20.25 ? 41   ARG   A N     1 
ATOM   207   C  CA    . ARG   A  1  43   ? -44.649 52.947  101.773 1.00 21.41 ? 41   ARG   A CA    1 
ATOM   208   C  C     . ARG   A  1  43   ? -43.580 51.861  101.848 1.00 22.20 ? 41   ARG   A C     1 
ATOM   209   O  O     . ARG   A  1  43   ? -42.985 51.504  100.824 1.00 21.53 ? 41   ARG   A O     1 
ATOM   210   C  CB    . ARG   A  1  43   ? -45.941 52.345  101.229 1.00 22.96 ? 41   ARG   A CB    1 
ATOM   211   C  CG    . ARG   A  1  43   ? -46.468 51.148  102.015 1.00 21.33 ? 41   ARG   A CG    1 
ATOM   212   C  CD    . ARG   A  1  43   ? -47.897 50.888  101.637 1.00 24.31 ? 41   ARG   A CD    1 
ATOM   213   N  NE    . ARG   A  1  43   ? -48.729 52.029  102.002 1.00 23.04 ? 41   ARG   A NE    1 
ATOM   214   C  CZ    . ARG   A  1  43   ? -49.865 52.354  101.406 1.00 21.68 ? 41   ARG   A CZ    1 
ATOM   215   N  NH1   . ARG   A  1  43   ? -50.337 51.654  100.391 1.00 23.41 ? 41   ARG   A NH1   1 
ATOM   216   N  NH2   . ARG   A  1  43   ? -50.539 53.417  101.835 1.00 23.69 ? 41   ARG   A NH2   1 
ATOM   217   N  N     . PRO   A  1  44   ? -43.298 51.330  103.035 1.00 23.31 ? 42   PRO   A N     1 
ATOM   218   C  CA    . PRO   A  1  44   ? -42.298 50.267  103.142 1.00 22.99 ? 42   PRO   A CA    1 
ATOM   219   C  C     . PRO   A  1  44   ? -42.596 49.136  102.172 1.00 19.52 ? 42   PRO   A C     1 
ATOM   220   O  O     . PRO   A  1  44   ? -43.747 48.773  101.930 1.00 22.65 ? 42   PRO   A O     1 
ATOM   221   C  CB    . PRO   A  1  44   ? -42.421 49.812  104.599 1.00 23.39 ? 42   PRO   A CB    1 
ATOM   222   C  CG    . PRO   A  1  44   ? -42.874 51.040  105.317 1.00 26.97 ? 42   PRO   A CG    1 
ATOM   223   C  CD    . PRO   A  1  44   ? -43.817 51.736  104.354 1.00 24.46 ? 42   PRO   A CD    1 
ATOM   224   N  N     . GLU   A  1  45   ? -41.525 48.610  101.582 1.00 22.82 ? 43   GLU   A N     1 
ATOM   225   C  CA    . GLU   A  1  45   ? -41.666 47.589  100.559 1.00 23.60 ? 43   GLU   A CA    1 
ATOM   226   C  C     . GLU   A  1  45   ? -42.384 46.353  101.095 1.00 23.70 ? 43   GLU   A C     1 
ATOM   227   O  O     . GLU   A  1  45   ? -43.158 45.713  100.374 1.00 25.28 ? 43   GLU   A O     1 
ATOM   228   C  CB    . GLU   A  1  45   ? -40.274 47.258  100.025 1.00 23.88 ? 43   GLU   A CB    1 
ATOM   229   C  CG    . GLU   A  1  45   ? -40.274 46.771  98.615  1.00 26.39 ? 43   GLU   A CG    1 
ATOM   230   C  CD    . GLU   A  1  45   ? -38.978 47.036  97.884  1.00 23.50 ? 43   GLU   A CD    1 
ATOM   231   O  OE1   . GLU   A  1  45   ? -38.077 47.738  98.407  1.00 21.59 ? 43   GLU   A OE1   1 
ATOM   232   O  OE2   . GLU   A  1  45   ? -38.876 46.510  96.769  1.00 21.20 ? 43   GLU   A OE2   1 
ATOM   233   N  N     . THR   A  1  46   ? -42.149 46.004  102.363 1.00 23.34 ? 44   THR   A N     1 
ATOM   234   C  CA    . THR   A  1  46   ? -42.818 44.844  102.949 1.00 27.50 ? 44   THR   A CA    1 
ATOM   235   C  C     . THR   A  1  46   ? -44.327 45.025  103.050 1.00 27.08 ? 44   THR   A C     1 
ATOM   236   O  O     . THR   A  1  46   ? -45.059 44.029  103.097 1.00 28.82 ? 44   THR   A O     1 
ATOM   237   C  CB    . THR   A  1  46   ? -42.250 44.543  104.338 1.00 23.95 ? 44   THR   A CB    1 
ATOM   238   O  OG1   . THR   A  1  46   ? -42.321 45.724  105.144 1.00 28.83 ? 44   THR   A OG1   1 
ATOM   239   C  CG2   . THR   A  1  46   ? -40.802 44.080  104.240 1.00 25.91 ? 44   THR   A CG2   1 
ATOM   240   N  N     . GLU   A  1  47   ? -44.808 46.263  103.099 1.00 23.98 ? 45   GLU   A N     1 
ATOM   241   C  CA    . GLU   A  1  47   ? -46.241 46.517  103.148 1.00 26.18 ? 45   GLU   A CA    1 
ATOM   242   C  C     . GLU   A  1  47   ? -46.871 46.561  101.761 1.00 24.47 ? 45   GLU   A C     1 
ATOM   243   O  O     . GLU   A  1  47   ? -48.063 46.259  101.613 1.00 26.38 ? 45   GLU   A O     1 
ATOM   244   C  CB    . GLU   A  1  47   ? -46.502 47.832  103.887 1.00 27.91 ? 45   GLU   A CB    1 
ATOM   245   C  CG    . GLU   A  1  47   ? -45.895 47.871  105.283 1.00 37.03 ? 45   GLU   A CG    1 
ATOM   246   C  CD    . GLU   A  1  47   ? -46.144 49.182  106.003 1.00 39.41 ? 45   GLU   A CD    1 
ATOM   247   O  OE1   . GLU   A  1  47   ? -46.977 49.978  105.521 1.00 40.31 ? 45   GLU   A OE1   1 
ATOM   248   O  OE2   . GLU   A  1  47   ? -45.505 49.413  107.053 1.00 49.48 ? 45   GLU   A OE2   1 
ATOM   249   N  N     . CYS   A  1  48   ? -46.092 46.925  100.739 1.00 20.43 ? 46   CYS   A N     1 
ATOM   250   C  CA    . CYS   A  1  48   ? -46.631 47.000  99.383  1.00 21.23 ? 46   CYS   A CA    1 
ATOM   251   C  C     . CYS   A  1  48   ? -46.888 45.620  98.794  1.00 18.33 ? 46   CYS   A C     1 
ATOM   252   O  O     . CYS   A  1  48   ? -47.861 45.427  98.060  1.00 21.22 ? 46   CYS   A O     1 
ATOM   253   C  CB    . CYS   A  1  48   ? -45.658 47.744  98.472  1.00 21.54 ? 46   CYS   A CB    1 
ATOM   254   S  SG    . CYS   A  1  48   ? -45.375 49.468  98.889  1.00 22.65 ? 46   CYS   A SG    1 
ATOM   255   N  N     . LEU   A  1  49   ? -46.002 44.663  99.057  1.00 21.23 ? 47   LEU   A N     1 
ATOM   256   C  CA    . LEU   A  1  49   ? -46.028 43.428  98.278  1.00 24.05 ? 47   LEU   A CA    1 
ATOM   257   C  C     . LEU   A  1  49   ? -47.215 42.495  98.526  1.00 23.05 ? 47   LEU   A C     1 
ATOM   258   O  O     . LEU   A  1  49   ? -47.750 41.946  97.553  1.00 23.81 ? 47   LEU   A O     1 
ATOM   259   C  CB    . LEU   A  1  49   ? -44.694 42.677  98.372  1.00 24.53 ? 47   LEU   A CB    1 
ATOM   260   C  CG    . LEU   A  1  49   ? -43.713 42.939  97.228  1.00 23.60 ? 47   LEU   A CG    1 
ATOM   261   C  CD1   . LEU   A  1  49   ? -44.289 42.462  95.900  1.00 23.56 ? 47   LEU   A CD1   1 
ATOM   262   C  CD2   . LEU   A  1  49   ? -43.379 44.417  97.151  1.00 22.66 ? 47   LEU   A CD2   1 
ATOM   263   N  N     . PRO   A  1  50   ? -47.636 42.248  99.770  1.00 25.24 ? 48   PRO   A N     1 
ATOM   264   C  CA    . PRO   A  1  50   ? -48.690 41.242  100.009 1.00 25.52 ? 48   PRO   A CA    1 
ATOM   265   C  C     . PRO   A  1  50   ? -49.947 41.485  99.187  1.00 26.48 ? 48   PRO   A C     1 
ATOM   266   O  O     . PRO   A  1  50   ? -50.426 40.549  98.527  1.00 27.45 ? 48   PRO   A O     1 
ATOM   267   C  CB    . PRO   A  1  50   ? -48.949 41.345  101.521 1.00 26.42 ? 48   PRO   A CB    1 
ATOM   268   C  CG    . PRO   A  1  50   ? -47.620 41.708  102.069 1.00 26.99 ? 48   PRO   A CG    1 
ATOM   269   C  CD    . PRO   A  1  50   ? -47.004 42.660  101.039 1.00 23.78 ? 48   PRO   A CD    1 
ATOM   270   N  N     . PRO   A  1  51   ? -50.518 42.702  99.167  1.00 24.43 ? 49   PRO   A N     1 
ATOM   271   C  CA    . PRO   A  1  51   ? -51.708 42.887  98.320  1.00 27.44 ? 49   PRO   A CA    1 
ATOM   272   C  C     . PRO   A  1  51   ? -51.424 42.706  96.838  1.00 22.45 ? 49   PRO   A C     1 
ATOM   273   O  O     . PRO   A  1  51   ? -52.315 42.276  96.093  1.00 24.78 ? 49   PRO   A O     1 
ATOM   274   C  CB    . PRO   A  1  51   ? -52.201 44.301  98.668  1.00 26.34 ? 49   PRO   A CB    1 
ATOM   275   C  CG    . PRO   A  1  51   ? -51.021 44.993  99.198  1.00 27.11 ? 49   PRO   A CG    1 
ATOM   276   C  CD    . PRO   A  1  51   ? -50.173 43.948  99.879  1.00 27.66 ? 49   PRO   A CD    1 
ATOM   277   N  N     . LEU   A  1  52   ? -50.204 43.012  96.387  1.00 23.66 ? 50   LEU   A N     1 
ATOM   278   C  CA    . LEU   A  1  52   ? -49.867 42.777  94.986  1.00 22.21 ? 50   LEU   A CA    1 
ATOM   279   C  C     . LEU   A  1  52   ? -49.779 41.286  94.696  1.00 20.25 ? 50   LEU   A C     1 
ATOM   280   O  O     . LEU   A  1  52   ? -50.280 40.815  93.670  1.00 22.03 ? 50   LEU   A O     1 
ATOM   281   C  CB    . LEU   A  1  52   ? -48.564 43.490  94.624  1.00 21.07 ? 50   LEU   A CB    1 
ATOM   282   C  CG    . LEU   A  1  52   ? -48.541 45.010  94.791  1.00 21.32 ? 50   LEU   A CG    1 
ATOM   283   C  CD1   . LEU   A  1  52   ? -47.119 45.533  94.614  1.00 20.26 ? 50   LEU   A CD1   1 
ATOM   284   C  CD2   . LEU   A  1  52   ? -49.458 45.682  93.782  1.00 22.34 ? 50   LEU   A CD2   1 
ATOM   285   N  N     . VAL   A  1  53   ? -49.153 40.528  95.597  1.00 22.87 ? 51   VAL   A N     1 
ATOM   286   C  CA    . VAL   A  1  53   ? -49.120 39.074  95.452  1.00 24.23 ? 51   VAL   A CA    1 
ATOM   287   C  C     . VAL   A  1  53   ? -50.535 38.515  95.367  1.00 23.68 ? 51   VAL   A C     1 
ATOM   288   O  O     . VAL   A  1  53   ? -50.846 37.693  94.493  1.00 26.26 ? 51   VAL   A O     1 
ATOM   289   C  CB    . VAL   A  1  53   ? -48.324 38.440  96.605  1.00 22.14 ? 51   VAL   A CB    1 
ATOM   290   C  CG1   . VAL   A  1  53   ? -48.450 36.927  96.575  1.00 28.36 ? 51   VAL   A CG1   1 
ATOM   291   C  CG2   . VAL   A  1  53   ? -46.860 38.855  96.520  1.00 23.99 ? 51   VAL   A CG2   1 
ATOM   292   N  N     . GLU   A  1  54   ? -51.420 38.974  96.259  1.00 24.15 ? 52   GLU   A N     1 
ATOM   293   C  CA    . GLU   A  1  54   ? -52.806 38.513  96.241  1.00 26.74 ? 52   GLU   A CA    1 
ATOM   294   C  C     . GLU   A  1  54   ? -53.477 38.843  94.913  1.00 24.80 ? 52   GLU   A C     1 
ATOM   295   O  O     . GLU   A  1  54   ? -54.078 37.969  94.277  1.00 26.80 ? 52   GLU   A O     1 
ATOM   296   C  CB    . GLU   A  1  54   ? -53.579 39.113  97.418  1.00 28.45 ? 52   GLU   A CB    1 
ATOM   297   N  N     . ALA   A  1  55   ? -53.336 40.092  94.449  1.00 23.59 ? 53   ALA   A N     1 
ATOM   298   C  CA    . ALA   A  1  55   ? -54.010 40.505  93.222  1.00 25.80 ? 53   ALA   A CA    1 
ATOM   299   C  C     . ALA   A  1  55   ? -53.443 39.796  92.002  1.00 21.48 ? 53   ALA   A C     1 
ATOM   300   O  O     . ALA   A  1  55   ? -54.164 39.578  91.022  1.00 24.67 ? 53   ALA   A O     1 
ATOM   301   C  CB    . ALA   A  1  55   ? -53.897 42.017  93.049  1.00 24.96 ? 53   ALA   A CB    1 
ATOM   302   N  N     . ALA   A  1  56   ? -52.163 39.439  92.037  1.00 22.46 ? 54   ALA   A N     1 
ATOM   303   C  CA    . ALA   A  1  56   ? -51.494 38.806  90.911  1.00 24.71 ? 54   ALA   A CA    1 
ATOM   304   C  C     . ALA   A  1  56   ? -51.634 37.290  90.902  1.00 28.03 ? 54   ALA   A C     1 
ATOM   305   O  O     . ALA   A  1  56   ? -51.162 36.647  89.959  1.00 25.99 ? 54   ALA   A O     1 
ATOM   306   C  CB    . ALA   A  1  56   ? -50.007 39.177  90.916  1.00 20.61 ? 54   ALA   A CB    1 
ATOM   307   N  N     . THR   A  1  57   ? -52.256 36.707  91.922  1.00 26.98 ? 55   THR   A N     1 
ATOM   308   C  CA    . THR   A  1  57   ? -52.351 35.257  92.016  1.00 27.44 ? 55   THR   A CA    1 
ATOM   309   C  C     . THR   A  1  57   ? -53.285 34.720  90.940  1.00 26.46 ? 55   THR   A C     1 
ATOM   310   O  O     . THR   A  1  57   ? -54.350 35.284  90.684  1.00 28.07 ? 55   THR   A O     1 
ATOM   311   C  CB    . THR   A  1  57   ? -52.860 34.879  93.407  1.00 29.46 ? 55   THR   A CB    1 
ATOM   312   O  OG1   . THR   A  1  57   ? -51.854 35.204  94.375  1.00 30.00 ? 55   THR   A OG1   1 
ATOM   313   C  CG2   . THR   A  1  57   ? -53.178 33.383  93.497  1.00 33.24 ? 55   THR   A CG2   1 
ATOM   314   N  N     . GLN   A  1  58   ? -52.870 33.636  90.286  1.00 26.09 ? 56   GLN   A N     1 
ATOM   315   C  CA    . GLN   A  1  58   ? -53.716 32.960  89.314  1.00 24.89 ? 56   GLN   A CA    1 
ATOM   316   C  C     . GLN   A  1  58   ? -53.756 31.474  89.638  1.00 26.74 ? 56   GLN   A C     1 
ATOM   317   O  O     . GLN   A  1  58   ? -52.946 30.968  90.416  1.00 28.51 ? 56   GLN   A O     1 
ATOM   318   C  CB    . GLN   A  1  58   ? -53.241 33.213  87.878  1.00 26.49 ? 56   GLN   A CB    1 
ATOM   319   C  CG    . GLN   A  1  58   ? -53.138 34.692  87.522  1.00 26.00 ? 56   GLN   A CG    1 
ATOM   320   C  CD    . GLN   A  1  58   ? -52.987 34.916  86.041  1.00 24.10 ? 56   GLN   A CD    1 
ATOM   321   O  OE1   . GLN   A  1  58   ? -53.964 34.874  85.299  1.00 26.84 ? 56   GLN   A OE1   1 
ATOM   322   N  NE2   . GLN   A  1  58   ? -51.754 35.151  85.594  1.00 26.28 ? 56   GLN   A NE2   1 
ATOM   323   N  N     . SER   A  1  59   ? -54.720 30.780  89.040  1.00 28.82 ? 57   SER   A N     1 
ATOM   324   C  CA    . SER   A  1  59   ? -54.887 29.360  89.299  1.00 27.04 ? 57   SER   A CA    1 
ATOM   325   C  C     . SER   A  1  59   ? -53.668 28.589  88.814  1.00 31.83 ? 57   SER   A C     1 
ATOM   326   O  O     . SER   A  1  59   ? -52.912 29.041  87.946  1.00 28.36 ? 57   SER   A O     1 
ATOM   327   C  CB    . SER   A  1  59   ? -56.102 28.830  88.553  1.00 30.61 ? 57   SER   A CB    1 
ATOM   328   O  OG    . SER   A  1  59   ? -55.883 28.863  87.150  1.00 30.69 ? 57   SER   A OG    1 
ATOM   329   N  N     . LYS   A  1  60   ? -53.491 27.396  89.387  1.00 30.33 ? 58   LYS   A N     1 
ATOM   330   C  CA    . LYS   A  1  60   ? -52.416 26.516  88.950  1.00 29.62 ? 58   LYS   A CA    1 
ATOM   331   C  C     . LYS   A  1  60   ? -52.515 26.220  87.457  1.00 31.25 ? 58   LYS   A C     1 
ATOM   332   O  O     . LYS   A  1  60   ? -51.498 26.200  86.754  1.00 32.00 ? 58   LYS   A O     1 
ATOM   333   C  CB    . LYS   A  1  60   ? -52.431 25.224  89.772  1.00 30.47 ? 58   LYS   A CB    1 
ATOM   334   C  CG    . LYS   A  1  60   ? -51.293 24.265  89.453  1.00 33.95 ? 58   LYS   A CG    1 
ATOM   335   C  CD    . LYS   A  1  60   ? -49.943 24.910  89.712  1.00 41.24 ? 58   LYS   A CD    1 
ATOM   336   C  CE    . LYS   A  1  60   ? -48.827 23.876  89.810  1.00 44.96 ? 58   LYS   A CE    1 
ATOM   337   N  NZ    . LYS   A  1  60   ? -48.583 23.181  88.517  1.00 45.27 ? 58   LYS   A NZ    1 
ATOM   338   N  N     . GLU   A  1  61   ? -53.730 25.996  86.953  1.00 30.83 ? 59   GLU   A N     1 
ATOM   339   C  CA    . GLU   A  1  61   ? -53.905 25.733  85.526  1.00 33.93 ? 59   GLU   A CA    1 
ATOM   340   C  C     . GLU   A  1  61   ? -53.395 26.897  84.682  1.00 34.32 ? 59   GLU   A C     1 
ATOM   341   O  O     . GLU   A  1  61   ? -52.691 26.696  83.686  1.00 32.57 ? 59   GLU   A O     1 
ATOM   342   C  CB    . GLU   A  1  61   ? -55.375 25.442  85.220  1.00 32.57 ? 59   GLU   A CB    1 
ATOM   343   N  N     . ILE   A  1  62   ? -53.735 28.128  85.073  1.00 30.87 ? 60   ILE   A N     1 
ATOM   344   C  CA    . ILE   A  1  62   ? -53.268 29.295  84.331  1.00 29.04 ? 60   ILE   A CA    1 
ATOM   345   C  C     . ILE   A  1  62   ? -51.757 29.432  84.427  1.00 32.01 ? 60   ILE   A C     1 
ATOM   346   O  O     . ILE   A  1  62   ? -51.081 29.734  83.435  1.00 30.70 ? 60   ILE   A O     1 
ATOM   347   C  CB    . ILE   A  1  62   ? -53.988 30.565  84.809  1.00 28.90 ? 60   ILE   A CB    1 
ATOM   348   C  CG1   . ILE   A  1  62   ? -55.399 30.594  84.243  1.00 31.16 ? 60   ILE   A CG1   1 
ATOM   349   C  CG2   . ILE   A  1  62   ? -53.208 31.814  84.404  1.00 29.61 ? 60   ILE   A CG2   1 
ATOM   350   C  CD1   . ILE   A  1  62   ? -56.167 31.767  84.683  1.00 34.86 ? 60   ILE   A CD1   1 
ATOM   351   N  N     . ARG   A  1  63   ? -51.204 29.228  85.622  1.00 28.86 ? 61   ARG   A N     1 
ATOM   352   C  CA    . ARG   A  1  63   ? -49.761 29.352  85.788  1.00 28.32 ? 61   ARG   A CA    1 
ATOM   353   C  C     . ARG   A  1  63   ? -49.016 28.355  84.913  1.00 30.13 ? 61   ARG   A C     1 
ATOM   354   O  O     . ARG   A  1  63   ? -48.003 28.700  84.292  1.00 28.30 ? 61   ARG   A O     1 
ATOM   355   C  CB    . ARG   A  1  63   ? -49.385 29.220  87.262  1.00 28.41 ? 61   ARG   A CB    1 
ATOM   356   C  CG    . ARG   A  1  63   ? -49.884 30.401  88.066  1.00 34.56 ? 61   ARG   A CG    1 
ATOM   357   C  CD    . ARG   A  1  63   ? -49.388 30.402  89.489  1.00 39.64 ? 61   ARG   A CD    1 
ATOM   358   N  NE    . ARG   A  1  63   ? -50.102 29.452  90.325  1.00 41.83 ? 61   ARG   A NE    1 
ATOM   359   C  CZ    . ARG   A  1  63   ? -49.581 28.321  90.772  1.00 44.21 ? 61   ARG   A CZ    1 
ATOM   360   N  NH1   . ARG   A  1  63   ? -48.341 27.971  90.478  1.00 45.24 ? 61   ARG   A NH1   1 
ATOM   361   N  NH2   . ARG   A  1  63   ? -50.320 27.528  91.542  1.00 41.54 ? 61   ARG   A NH2   1 
ATOM   362   N  N     . ASP   A  1  64   ? -49.516 27.118  84.833  1.00 32.28 ? 62   ASP   A N     1 
ATOM   363   C  CA    . ASP   A  1  64   ? -48.910 26.133  83.944  1.00 31.48 ? 62   ASP   A CA    1 
ATOM   364   C  C     . ASP   A  1  64   ? -49.064 26.538  82.483  1.00 29.80 ? 62   ASP   A C     1 
ATOM   365   O  O     . ASP   A  1  64   ? -48.127 26.386  81.691  1.00 31.26 ? 62   ASP   A O     1 
ATOM   366   C  CB    . ASP   A  1  64   ? -49.527 24.756  84.191  1.00 32.50 ? 62   ASP   A CB    1 
ATOM   367   C  CG    . ASP   A  1  64   ? -49.168 24.193  85.556  1.00 34.25 ? 62   ASP   A CG    1 
ATOM   368   O  OD1   . ASP   A  1  64   ? -48.338 24.806  86.260  1.00 36.76 ? 62   ASP   A OD1   1 
ATOM   369   O  OD2   . ASP   A  1  64   ? -49.722 23.133  85.925  1.00 41.44 ? 62   ASP   A OD2   1 
ATOM   370   N  N     . ALA   A  1  65   ? -50.238 27.051  82.108  1.00 27.06 ? 63   ALA   A N     1 
ATOM   371   C  CA    . ALA   A  1  65   ? -50.439 27.498  80.734  1.00 29.44 ? 63   ALA   A CA    1 
ATOM   372   C  C     . ALA   A  1  65   ? -49.552 28.692  80.417  1.00 31.73 ? 63   ALA   A C     1 
ATOM   373   O  O     . ALA   A  1  65   ? -48.977 28.779  79.325  1.00 29.38 ? 63   ALA   A O     1 
ATOM   374   C  CB    . ALA   A  1  65   ? -51.909 27.854  80.504  1.00 31.54 ? 63   ALA   A CB    1 
ATOM   375   N  N     . ALA   A  1  66   ? -49.427 29.622  81.365  1.00 29.66 ? 64   ALA   A N     1 
ATOM   376   C  CA    . ALA   A  1  66   ? -48.562 30.776  81.157  1.00 29.34 ? 64   ALA   A CA    1 
ATOM   377   C  C     . ALA   A  1  66   ? -47.108 30.350  81.015  1.00 28.00 ? 64   ALA   A C     1 
ATOM   378   O  O     . ALA   A  1  66   ? -46.379 30.870  80.160  1.00 26.89 ? 64   ALA   A O     1 
ATOM   379   C  CB    . ALA   A  1  66   ? -48.720 31.760  82.315  1.00 28.04 ? 64   ALA   A CB    1 
ATOM   380   N  N     . ALA   A  1  67   ? -46.668 29.399  81.842  1.00 24.65 ? 65   ALA   A N     1 
ATOM   381   C  CA    . ALA   A  1  67   ? -45.294 28.924  81.737  1.00 27.90 ? 65   ALA   A CA    1 
ATOM   382   C  C     . ALA   A  1  67   ? -45.046 28.266  80.385  1.00 27.71 ? 65   ALA   A C     1 
ATOM   383   O  O     . ALA   A  1  67   ? -43.993 28.476  79.768  1.00 29.56 ? 65   ALA   A O     1 
ATOM   384   C  CB    . ALA   A  1  67   ? -44.979 27.961  82.882  1.00 29.33 ? 65   ALA   A CB    1 
ATOM   385   N  N     . SER   A  1  68   ? -46.009 27.478  79.903  1.00 29.04 ? 66   SER   A N     1 
ATOM   386   C  CA    . SER   A  1  68   ? -45.859 26.850  78.595  1.00 32.20 ? 66   SER   A CA    1 
ATOM   387   C  C     . SER   A  1  68   ? -45.807 27.896  77.488  1.00 32.55 ? 66   SER   A C     1 
ATOM   388   O  O     . SER   A  1  68   ? -44.981 27.804  76.571  1.00 30.13 ? 66   SER   A O     1 
ATOM   389   C  CB    . SER   A  1  68   ? -46.992 25.853  78.356  1.00 33.45 ? 66   SER   A CB    1 
ATOM   390   O  OG    . SER   A  1  68   ? -47.007 25.413  77.009  1.00 40.19 ? 66   SER   A OG    1 
ATOM   391   N  N     . THR   A  1  69   ? -46.674 28.908  77.561  1.00 30.83 ? 67   THR   A N     1 
ATOM   392   C  CA    . THR   A  1  69   ? -46.643 29.963  76.557  1.00 28.10 ? 67   THR   A CA    1 
ATOM   393   C  C     . THR   A  1  69   ? -45.331 30.728  76.605  1.00 25.14 ? 67   THR   A C     1 
ATOM   394   O  O     . THR   A  1  69   ? -44.738 31.020  75.561  1.00 26.44 ? 67   THR   A O     1 
ATOM   395   C  CB    . THR   A  1  69   ? -47.821 30.908  76.756  1.00 26.17 ? 67   THR   A CB    1 
ATOM   396   O  OG1   . THR   A  1  69   ? -49.034 30.207  76.468  1.00 27.71 ? 67   THR   A OG1   1 
ATOM   397   C  CG2   . THR   A  1  69   ? -47.699 32.123  75.836  1.00 25.16 ? 67   THR   A CG2   1 
ATOM   398   N  N     . ALA   A  1  70   ? -44.862 31.061  77.809  1.00 26.32 ? 68   ALA   A N     1 
ATOM   399   C  CA    . ALA   A  1  70   ? -43.607 31.795  77.930  1.00 27.60 ? 68   ALA   A CA    1 
ATOM   400   C  C     . ALA   A  1  70   ? -42.446 30.984  77.377  1.00 28.17 ? 68   ALA   A C     1 
ATOM   401   O  O     . ALA   A  1  70   ? -41.585 31.524  76.672  1.00 27.94 ? 68   ALA   A O     1 
ATOM   402   C  CB    . ALA   A  1  70   ? -43.345 32.186  79.385  1.00 25.35 ? 68   ALA   A CB    1 
ATOM   403   N  N     . ARG   A  1  71   ? -42.410 29.683  77.685  1.00 28.99 ? 69   ARG   A N     1 
ATOM   404   C  CA    . ARG   A  1  71   ? -41.350 28.831  77.154  1.00 28.06 ? 69   ARG   A CA    1 
ATOM   405   C  C     . ARG   A  1  71   ? -41.391 28.803  75.634  1.00 30.02 ? 69   ARG   A C     1 
ATOM   406   O  O     . ARG   A  1  71   ? -40.352 28.931  74.977  1.00 31.15 ? 69   ARG   A O     1 
ATOM   407   C  CB    . ARG   A  1  71   ? -41.481 27.420  77.726  1.00 31.11 ? 69   ARG   A CB    1 
ATOM   408   C  CG    . ARG   A  1  71   ? -40.671 26.375  76.980  1.00 35.88 ? 69   ARG   A CG    1 
ATOM   409   C  CD    . ARG   A  1  71   ? -40.694 25.026  77.689  1.00 35.44 ? 69   ARG   A CD    1 
ATOM   410   N  NE    . ARG   A  1  71   ? -39.915 25.064  78.919  1.00 35.45 ? 69   ARG   A NE    1 
ATOM   411   C  CZ    . ARG   A  1  71   ? -38.591 25.018  78.961  1.00 35.69 ? 69   ARG   A CZ    1 
ATOM   412   N  NH1   . ARG   A  1  71   ? -37.868 24.935  77.856  1.00 37.80 ? 69   ARG   A NH1   1 
ATOM   413   N  NH2   . ARG   A  1  71   ? -37.977 25.074  80.139  1.00 36.25 ? 69   ARG   A NH2   1 
ATOM   414   N  N     . LYS   A  1  72   ? -42.589 28.667  75.059  1.00 29.03 ? 70   LYS   A N     1 
ATOM   415   C  CA    . LYS   A  1  72   ? -42.732 28.671  73.605  1.00 31.56 ? 70   LYS   A CA    1 
ATOM   416   C  C     . LYS   A  1  72   ? -42.228 29.978  72.999  1.00 33.54 ? 70   LYS   A C     1 
ATOM   417   O  O     . LYS   A  1  72   ? -41.483 29.973  72.012  1.00 30.57 ? 70   LYS   A O     1 
ATOM   418   C  CB    . LYS   A  1  72   ? -44.187 28.421  73.220  1.00 31.74 ? 70   LYS   A CB    1 
ATOM   419   C  CG    . LYS   A  1  72   ? -44.443 28.532  71.731  1.00 36.56 ? 70   LYS   A CG    1 
ATOM   420   C  CD    . LYS   A  1  72   ? -45.848 28.092  71.372  1.00 38.38 ? 70   LYS   A CD    1 
ATOM   421   C  CE    . LYS   A  1  72   ? -46.047 28.094  69.865  1.00 44.71 ? 70   LYS   A CE    1 
ATOM   422   N  NZ    . LYS   A  1  72   ? -47.338 27.472  69.464  1.00 53.04 ? 70   LYS   A NZ    1 
ATOM   423   N  N     . LEU   A  1  73   ? -42.623 31.112  73.582  1.00 28.91 ? 71   LEU   A N     1 
ATOM   424   C  CA    . LEU   A  1  73   ? -42.127 32.403  73.114  1.00 28.53 ? 71   LEU   A CA    1 
ATOM   425   C  C     . LEU   A  1  73   ? -40.611 32.488  73.225  1.00 29.21 ? 71   LEU   A C     1 
ATOM   426   O  O     . LEU   A  1  73   ? -39.940 32.977  72.309  1.00 30.52 ? 71   LEU   A O     1 
ATOM   427   C  CB    . LEU   A  1  73   ? -42.760 33.528  73.929  1.00 27.86 ? 71   LEU   A CB    1 
ATOM   428   C  CG    . LEU   A  1  73   ? -44.268 33.708  73.807  1.00 24.69 ? 71   LEU   A CG    1 
ATOM   429   C  CD1   . LEU   A  1  73   ? -44.728 34.756  74.802  1.00 24.69 ? 71   LEU   A CD1   1 
ATOM   430   C  CD2   . LEU   A  1  73   ? -44.647 34.097  72.392  1.00 28.67 ? 71   LEU   A CD2   1 
ATOM   431   N  N     . ILE   A  1  74   ? -40.056 32.027  74.346  1.00 25.37 ? 72   ILE   A N     1 
ATOM   432   C  CA    . ILE   A  1  74   ? -38.616 32.128  74.566  1.00 27.19 ? 72   ILE   A CA    1 
ATOM   433   C  C     . ILE   A  1  74   ? -37.856 31.202  73.624  1.00 29.07 ? 72   ILE   A C     1 
ATOM   434   O  O     . ILE   A  1  74   ? -36.792 31.563  73.105  1.00 29.70 ? 72   ILE   A O     1 
ATOM   435   C  CB    . ILE   A  1  74   ? -38.295 31.874  76.050  1.00 26.60 ? 72   ILE   A CB    1 
ATOM   436   C  CG1   . ILE   A  1  74   ? -38.841 33.035  76.888  1.00 29.81 ? 72   ILE   A CG1   1 
ATOM   437   C  CG2   . ILE   A  1  74   ? -36.792 31.698  76.267  1.00 27.73 ? 72   ILE   A CG2   1 
ATOM   438   C  CD1   . ILE   A  1  74   ? -38.943 32.734  78.358  1.00 29.08 ? 72   ILE   A CD1   1 
ATOM   439   N  N     . GLU   A  1  75   ? -38.387 30.001  73.382  1.00 30.55 ? 73   GLU   A N     1 
ATOM   440   C  CA    . GLU   A  1  75   ? -37.749 29.096  72.432  1.00 32.26 ? 73   GLU   A CA    1 
ATOM   441   C  C     . GLU   A  1  75   ? -37.731 29.694  71.030  1.00 34.96 ? 73   GLU   A C     1 
ATOM   442   O  O     . GLU   A  1  75   ? -36.720 29.611  70.325  1.00 31.44 ? 73   GLU   A O     1 
ATOM   443   C  CB    . GLU   A  1  75   ? -38.435 27.729  72.467  1.00 35.84 ? 73   GLU   A CB    1 
ATOM   444   C  CG    . GLU   A  1  75   ? -38.020 26.916  73.680  1.00 37.49 ? 73   GLU   A CG    1 
ATOM   445   C  CD    . GLU   A  1  75   ? -38.923 25.736  73.975  1.00 46.17 ? 73   GLU   A CD    1 
ATOM   446   O  OE1   . GLU   A  1  75   ? -39.975 25.594  73.313  1.00 44.72 ? 73   GLU   A OE1   1 
ATOM   447   O  OE2   . GLU   A  1  75   ? -38.573 24.952  74.886  1.00 44.68 ? 73   GLU   A OE2   1 
ATOM   448   N  N     . ALA   A  1  76   ? -38.830 30.330  70.621  1.00 32.80 ? 74   ALA   A N     1 
ATOM   449   C  CA    . ALA   A  1  76   ? -38.854 31.008  69.329  1.00 32.26 ? 74   ALA   A CA    1 
ATOM   450   C  C     . ALA   A  1  76   ? -37.855 32.159  69.288  1.00 35.46 ? 74   ALA   A C     1 
ATOM   451   O  O     . ALA   A  1  76   ? -37.183 32.368  68.272  1.00 38.09 ? 74   ALA   A O     1 
ATOM   452   C  CB    . ALA   A  1  76   ? -40.266 31.510  69.032  1.00 34.53 ? 74   ALA   A CB    1 
ATOM   453   N  N     . LEU   A  1  77   ? -37.747 32.919  70.380  1.00 33.01 ? 75   LEU   A N     1 
ATOM   454   C  CA    . LEU   A  1  77   ? -36.790 34.022  70.431  1.00 31.06 ? 75   LEU   A CA    1 
ATOM   455   C  C     . LEU   A  1  77   ? -35.361 33.516  70.296  1.00 35.94 ? 75   LEU   A C     1 
ATOM   456   O  O     . LEU   A  1  77   ? -34.580 34.020  69.479  1.00 36.89 ? 75   LEU   A O     1 
ATOM   457   C  CB    . LEU   A  1  77   ? -36.945 34.792  71.741  1.00 31.90 ? 75   LEU   A CB    1 
ATOM   458   C  CG    . LEU   A  1  77   ? -38.044 35.847  71.799  1.00 33.26 ? 75   LEU   A CG    1 
ATOM   459   C  CD1   . LEU   A  1  77   ? -38.063 36.487  73.170  1.00 29.99 ? 75   LEU   A CD1   1 
ATOM   460   C  CD2   . LEU   A  1  77   ? -37.800 36.883  70.724  1.00 31.05 ? 75   LEU   A CD2   1 
ATOM   461   N  N     . ARG   A  1  78   ? -34.997 32.519  71.104  1.00 30.98 ? 76   ARG   A N     1 
ATOM   462   C  CA    . ARG   A  1  78   ? -33.640 31.995  71.066  1.00 33.38 ? 76   ARG   A CA    1 
ATOM   463   C  C     . ARG   A  1  78   ? -33.342 31.225  69.788  1.00 34.28 ? 76   ARG   A C     1 
ATOM   464   O  O     . ARG   A  1  78   ? -32.173 31.126  69.402  1.00 39.88 ? 76   ARG   A O     1 
ATOM   465   C  CB    . ARG   A  1  78   ? -33.386 31.134  72.300  1.00 31.54 ? 76   ARG   A CB    1 
ATOM   466   C  CG    . ARG   A  1  78   ? -33.235 31.961  73.553  1.00 34.56 ? 76   ARG   A CG    1 
ATOM   467   C  CD    . ARG   A  1  78   ? -32.861 31.114  74.743  1.00 28.87 ? 76   ARG   A CD    1 
ATOM   468   N  NE    . ARG   A  1  78   ? -32.282 31.948  75.783  1.00 30.25 ? 76   ARG   A NE    1 
ATOM   469   C  CZ    . ARG   A  1  78   ? -31.882 31.504  76.963  1.00 29.82 ? 76   ARG   A CZ    1 
ATOM   470   N  NH1   . ARG   A  1  78   ? -32.022 30.234  77.305  1.00 32.81 ? 76   ARG   A NH1   1 
ATOM   471   N  NH2   . ARG   A  1  78   ? -31.319 32.353  77.818  1.00 33.20 ? 76   ARG   A NH2   1 
ATOM   472   N  N     . GLY   A  1  79   ? -34.364 30.693  69.119  1.00 35.61 ? 77   GLY   A N     1 
ATOM   473   C  CA    . GLY   A  1  79   ? -34.157 29.949  67.891  1.00 39.48 ? 77   GLY   A CA    1 
ATOM   474   C  C     . GLY   A  1  79   ? -33.980 30.789  66.647  1.00 45.40 ? 77   GLY   A C     1 
ATOM   475   O  O     . GLY   A  1  79   ? -33.714 30.235  65.577  1.00 48.26 ? 77   GLY   A O     1 
ATOM   476   N  N     . LYS   A  1  80   ? -34.123 32.110  66.753  1.00 46.06 ? 78   LYS   A N     1 
ATOM   477   C  CA    . LYS   A  1  80   ? -33.961 32.991  65.604  1.00 47.10 ? 78   LYS   A CA    1 
ATOM   478   C  C     . LYS   A  1  80   ? -33.000 34.142  65.876  1.00 46.28 ? 78   LYS   A C     1 
ATOM   479   O  O     . LYS   A  1  80   ? -32.879 35.040  65.034  1.00 51.07 ? 78   LYS   A O     1 
ATOM   480   C  CB    . LYS   A  1  80   ? -35.319 33.529  65.134  1.00 46.75 ? 78   LYS   A CB    1 
ATOM   481   C  CG    . LYS   A  1  80   ? -36.035 34.396  66.164  1.00 47.35 ? 78   LYS   A CG    1 
ATOM   482   C  CD    . LYS   A  1  80   ? -37.448 34.733  65.716  1.00 42.19 ? 78   LYS   A CD    1 
ATOM   483   C  CE    . LYS   A  1  80   ? -38.176 35.594  66.742  1.00 40.93 ? 78   LYS   A CE    1 
ATOM   484   N  NZ    . LYS   A  1  80   ? -39.570 35.938  66.309  1.00 32.50 ? 78   LYS   A NZ    1 
ATOM   485   N  N     . HIS   A  1  81   ? -32.314 34.136  67.018  1.00 50.77 ? 79   HIS   A N     1 
ATOM   486   C  CA    . HIS   A  1  81   ? -31.447 35.241  67.430  1.00 57.05 ? 79   HIS   A CA    1 
ATOM   487   C  C     . HIS   A  1  81   ? -30.406 35.621  66.377  1.00 59.00 ? 79   HIS   A C     1 
ATOM   488   O  O     . HIS   A  1  81   ? -29.606 34.791  65.949  1.00 63.44 ? 79   HIS   A O     1 
ATOM   489   C  CB    . HIS   A  1  81   ? -30.750 34.901  68.751  1.00 58.05 ? 79   HIS   A CB    1 
ATOM   490   N  N     . SER   A  1  84   ? -26.310 41.357  66.673  1.00 46.18 ? 82   SER   A N     1 
ATOM   491   C  CA    . SER   A  1  84   ? -25.528 40.494  65.797  1.00 47.39 ? 82   SER   A CA    1 
ATOM   492   C  C     . SER   A  1  84   ? -24.789 41.319  64.747  1.00 43.10 ? 82   SER   A C     1 
ATOM   493   O  O     . SER   A  1  84   ? -23.746 40.904  64.251  1.00 39.39 ? 82   SER   A O     1 
ATOM   494   C  CB    . SER   A  1  84   ? -26.420 39.448  65.121  1.00 44.88 ? 82   SER   A CB    1 
ATOM   495   N  N     . GLY   A  1  85   ? -25.340 42.488  64.411  1.00 41.97 ? 83   GLY   A N     1 
ATOM   496   C  CA    . GLY   A  1  85   ? -24.673 43.357  63.454  1.00 35.01 ? 83   GLY   A CA    1 
ATOM   497   C  C     . GLY   A  1  85   ? -23.324 43.837  63.956  1.00 29.82 ? 83   GLY   A C     1 
ATOM   498   O  O     . GLY   A  1  85   ? -22.297 43.650  63.297  1.00 30.63 ? 83   GLY   A O     1 
ATOM   499   N  N     . VAL   A  1  86   ? -23.311 44.471  65.130  1.00 32.46 ? 84   VAL   A N     1 
ATOM   500   C  CA    . VAL   A  1  86   ? -22.051 44.909  65.722  1.00 31.37 ? 84   VAL   A CA    1 
ATOM   501   C  C     . VAL   A  1  86   ? -21.174 43.711  66.049  1.00 31.26 ? 84   VAL   A C     1 
ATOM   502   O  O     . VAL   A  1  86   ? -19.964 43.721  65.789  1.00 25.94 ? 84   VAL   A O     1 
ATOM   503   C  CB    . VAL   A  1  86   ? -22.317 45.797  66.952  1.00 33.88 ? 84   VAL   A CB    1 
ATOM   504   C  CG1   . VAL   A  1  86   ? -21.025 46.043  67.727  1.00 37.60 ? 84   VAL   A CG1   1 
ATOM   505   C  CG2   . VAL   A  1  86   ? -22.940 47.112  66.518  1.00 36.32 ? 84   VAL   A CG2   1 
ATOM   506   N  N     . GLU   A  1  87   ? -21.770 42.654  66.607  1.00 31.07 ? 85   GLU   A N     1 
ATOM   507   C  CA    . GLU   A  1  87   ? -21.010 41.448  66.918  1.00 32.37 ? 85   GLU   A CA    1 
ATOM   508   C  C     . GLU   A  1  87   ? -20.364 40.862  65.669  1.00 32.18 ? 85   GLU   A C     1 
ATOM   509   O  O     . GLU   A  1  87   ? -19.194 40.458  65.698  1.00 32.90 ? 85   GLU   A O     1 
ATOM   510   C  CB    . GLU   A  1  87   ? -21.915 40.417  67.596  1.00 37.93 ? 85   GLU   A CB    1 
ATOM   511   N  N     . GLY   A  1  88   ? -21.101 40.821  64.559  1.00 30.10 ? 86   GLY   A N     1 
ATOM   512   C  CA    . GLY   A  1  88   ? -20.531 40.304  63.327  1.00 31.24 ? 86   GLY   A CA    1 
ATOM   513   C  C     . GLY   A  1  88   ? -19.389 41.158  62.811  1.00 26.96 ? 86   GLY   A C     1 
ATOM   514   O  O     . GLY   A  1  88   ? -18.410 40.640  62.268  1.00 28.88 ? 86   GLY   A O     1 
ATOM   515   N  N     . LEU   A  1  89   ? -19.497 42.477  62.981  1.00 28.05 ? 87   LEU   A N     1 
ATOM   516   C  CA    . LEU   A  1  89   ? -18.420 43.375  62.585  1.00 28.68 ? 87   LEU   A CA    1 
ATOM   517   C  C     . LEU   A  1  89   ? -17.189 43.149  63.453  1.00 24.71 ? 87   LEU   A C     1 
ATOM   518   O  O     . LEU   A  1  89   ? -16.070 43.006  62.942  1.00 24.37 ? 87   LEU   A O     1 
ATOM   519   C  CB    . LEU   A  1  89   ? -18.912 44.820  62.701  1.00 29.44 ? 87   LEU   A CB    1 
ATOM   520   C  CG    . LEU   A  1  89   ? -18.310 45.935  61.843  1.00 34.06 ? 87   LEU   A CG    1 
ATOM   521   C  CD1   . LEU   A  1  89   ? -18.999 47.248  62.179  1.00 34.10 ? 87   LEU   A CD1   1 
ATOM   522   C  CD2   . LEU   A  1  89   ? -16.816 46.057  62.044  1.00 37.36 ? 87   LEU   A CD2   1 
ATOM   523   N  N     . VAL   A  1  90   ? -17.383 43.119  64.775  1.00 25.56 ? 88   VAL   A N     1 
ATOM   524   C  CA    . VAL   A  1  90   ? -16.285 42.843  65.698  1.00 24.76 ? 88   VAL   A CA    1 
ATOM   525   C  C     . VAL   A  1  90   ? -15.605 41.526  65.348  1.00 27.17 ? 88   VAL   A C     1 
ATOM   526   O  O     . VAL   A  1  90   ? -14.371 41.426  65.343  1.00 25.24 ? 88   VAL   A O     1 
ATOM   527   C  CB    . VAL   A  1  90   ? -16.808 42.862  67.146  1.00 25.61 ? 88   VAL   A CB    1 
ATOM   528   C  CG1   . VAL   A  1  90   ? -15.790 42.264  68.094  1.00 26.40 ? 88   VAL   A CG1   1 
ATOM   529   C  CG2   . VAL   A  1  90   ? -17.154 44.279  67.556  1.00 25.57 ? 88   VAL   A CG2   1 
ATOM   530   N  N     . GLN   A  1  91   ? -16.396 40.500  65.030  1.00 28.03 ? 89   GLN   A N     1 
ATOM   531   C  CA    . GLN   A  1  91   ? -15.829 39.199  64.683  1.00 28.26 ? 89   GLN   A CA    1 
ATOM   532   C  C     . GLN   A  1  91   ? -15.058 39.257  63.368  1.00 28.74 ? 89   GLN   A C     1 
ATOM   533   O  O     . GLN   A  1  91   ? -13.927 38.760  63.279  1.00 30.47 ? 89   GLN   A O     1 
ATOM   534   C  CB    . GLN   A  1  91   ? -16.939 38.145  64.617  1.00 33.86 ? 89   GLN   A CB    1 
ATOM   535   N  N     . GLU   A  1  92   ? -15.649 39.858  62.332  1.00 28.81 ? 90   GLU   A N     1 
ATOM   536   C  CA    . GLU   A  1  92   ? -15.029 39.826  61.009  1.00 28.29 ? 90   GLU   A CA    1 
ATOM   537   C  C     . GLU   A  1  92   ? -13.658 40.491  61.012  1.00 27.30 ? 90   GLU   A C     1 
ATOM   538   O  O     . GLU   A  1  92   ? -12.720 40.006  60.367  1.00 28.42 ? 90   GLU   A O     1 
ATOM   539   C  CB    . GLU   A  1  92   ? -15.944 40.485  59.978  1.00 28.96 ? 90   GLU   A CB    1 
ATOM   540   C  CG    . GLU   A  1  92   ? -15.267 40.737  58.635  1.00 30.84 ? 90   GLU   A CG    1 
ATOM   541   C  CD    . GLU   A  1  92   ? -16.231 41.232  57.571  1.00 38.11 ? 90   GLU   A CD    1 
ATOM   542   O  OE1   . GLU   A  1  92   ? -17.417 41.458  57.898  1.00 37.73 ? 90   GLU   A OE1   1 
ATOM   543   O  OE2   . GLU   A  1  92   ? -15.800 41.395  56.408  1.00 37.62 ? 90   GLU   A OE2   1 
ATOM   544   N  N     . TYR   A  1  93   ? -13.515 41.597  61.738  1.00 26.09 ? 91   TYR   A N     1 
ATOM   545   C  CA    . TYR   A  1  93   ? -12.268 42.348  61.758  1.00 25.93 ? 91   TYR   A CA    1 
ATOM   546   C  C     . TYR   A  1  93   ? -11.452 42.120  63.024  1.00 25.14 ? 91   TYR   A C     1 
ATOM   547   O  O     . TYR   A  1  93   ? -10.465 42.832  63.247  1.00 24.54 ? 91   TYR   A O     1 
ATOM   548   C  CB    . TYR   A  1  93   ? -12.545 43.836  61.538  1.00 26.98 ? 91   TYR   A CB    1 
ATOM   549   C  CG    . TYR   A  1  93   ? -13.043 44.106  60.146  1.00 24.57 ? 91   TYR   A CG    1 
ATOM   550   C  CD1   . TYR   A  1  93   ? -12.153 44.259  59.089  1.00 24.84 ? 91   TYR   A CD1   1 
ATOM   551   C  CD2   . TYR   A  1  93   ? -14.403 44.170  59.878  1.00 25.84 ? 91   TYR   A CD2   1 
ATOM   552   C  CE1   . TYR   A  1  93   ? -12.603 44.484  57.809  1.00 25.82 ? 91   TYR   A CE1   1 
ATOM   553   C  CE2   . TYR   A  1  93   ? -14.864 44.397  58.594  1.00 29.35 ? 91   TYR   A CE2   1 
ATOM   554   C  CZ    . TYR   A  1  93   ? -13.956 44.559  57.570  1.00 24.68 ? 91   TYR   A CZ    1 
ATOM   555   O  OH    . TYR   A  1  93   ? -14.398 44.780  56.286  1.00 32.94 ? 91   TYR   A OH    1 
ATOM   556   N  N     . SER   A  1  94   ? -11.832 41.136  63.839  1.00 24.40 ? 92   SER   A N     1 
ATOM   557   C  CA    . SER   A  1  94   ? -11.105 40.787  65.060  1.00 23.83 ? 92   SER   A CA    1 
ATOM   558   C  C     . SER   A  1  94   ? -10.881 42.019  65.930  1.00 21.20 ? 92   SER   A C     1 
ATOM   559   O  O     . SER   A  1  94   ? -9.775  42.293  66.399  1.00 22.99 ? 92   SER   A O     1 
ATOM   560   C  CB    . SER   A  1  94   ? -9.785  40.084  64.749  1.00 24.61 ? 92   SER   A CB    1 
ATOM   561   O  OG    . SER   A  1  94   ? -9.994  39.011  63.846  1.00 28.25 ? 92   SER   A OG    1 
ATOM   562   N  N     . LEU   A  1  95   ? -11.943 42.787  66.119  1.00 20.33 ? 93   LEU   A N     1 
ATOM   563   C  CA    . LEU   A  1  95   ? -11.836 44.025  66.867  1.00 21.15 ? 93   LEU   A CA    1 
ATOM   564   C  C     . LEU   A  1  95   ? -11.859 43.744  68.359  1.00 19.48 ? 93   LEU   A C     1 
ATOM   565   O  O     . LEU   A  1  95   ? -12.616 42.900  68.839  1.00 21.16 ? 93   LEU   A O     1 
ATOM   566   C  CB    . LEU   A  1  95   ? -13.007 44.944  66.531  1.00 18.03 ? 93   LEU   A CB    1 
ATOM   567   C  CG    . LEU   A  1  95   ? -13.135 45.369  65.070  1.00 18.67 ? 93   LEU   A CG    1 
ATOM   568   C  CD1   . LEU   A  1  95   ? -14.287 46.380  64.970  1.00 23.27 ? 93   LEU   A CD1   1 
ATOM   569   C  CD2   . LEU   A  1  95   ? -11.832 45.940  64.522  1.00 19.82 ? 93   LEU   A CD2   1 
ATOM   570   N  N     . SER   A  1  96   ? -11.031 44.468  69.095  1.00 17.71 ? 94   SER   A N     1 
ATOM   571   C  CA    . SER   A  1  96   ? -11.218 44.511  70.530  1.00 18.04 ? 94   SER   A CA    1 
ATOM   572   C  C     . SER   A  1  96   ? -12.466 45.336  70.838  1.00 17.81 ? 94   SER   A C     1 
ATOM   573   O  O     . SER   A  1  96   ? -13.019 46.013  69.970  1.00 16.96 ? 94   SER   A O     1 
ATOM   574   C  CB    . SER   A  1  96   ? -10.014 45.179  71.181  1.00 18.85 ? 94   SER   A CB    1 
ATOM   575   O  OG    . SER   A  1  96   ? -9.976  46.549  70.828  1.00 16.59 ? 94   SER   A OG    1 
ATOM   576   N  N     . SER   A  1  97   ? -12.898 45.299  72.097  1.00 17.04 ? 95   SER   A N     1 
ATOM   577   C  CA    . SER   A  1  97   ? -14.051 46.102  72.495  1.00 17.39 ? 95   SER   A CA    1 
ATOM   578   C  C     . SER   A  1  97   ? -13.787 47.581  72.259  1.00 16.60 ? 95   SER   A C     1 
ATOM   579   O  O     . SER   A  1  97   ? -14.626 48.292  71.699  1.00 16.78 ? 95   SER   A O     1 
ATOM   580   C  CB    . SER   A  1  97   ? -14.384 45.846  73.964  1.00 22.59 ? 95   SER   A CB    1 
ATOM   581   O  OG    . SER   A  1  97   ? -14.970 44.567  74.098  1.00 29.89 ? 95   SER   A OG    1 
ATOM   582   N  N     . GLN   A  1  98   ? -12.616 48.063  72.668  1.00 15.11 ? 96   GLN   A N     1 
ATOM   583   C  CA    . GLN   A  1  98   ? -12.321 49.472  72.462  1.00 15.25 ? 96   GLN   A CA    1 
ATOM   584   C  C     . GLN   A  1  98   ? -12.273 49.814  70.983  1.00 14.49 ? 96   GLN   A C     1 
ATOM   585   O  O     . GLN   A  1  98   ? -12.687 50.905  70.586  1.00 14.74 ? 96   GLN   A O     1 
ATOM   586   C  CB    . GLN   A  1  98   ? -11.019 49.853  73.159  1.00 15.06 ? 96   GLN   A CB    1 
ATOM   587   C  CG    . GLN   A  1  98   ? -11.162 49.926  74.681  1.00 16.75 ? 96   GLN   A CG    1 
ATOM   588   C  CD    . GLN   A  1  98   ? -12.102 51.022  75.132  1.00 15.75 ? 96   GLN   A CD    1 
ATOM   589   O  OE1   . GLN   A  1  98   ? -13.321 50.840  75.156  1.00 19.15 ? 96   GLN   A OE1   1 
ATOM   590   N  NE2   . GLN   A  1  98   ? -11.545 52.169  75.497  1.00 17.78 ? 96   GLN   A NE2   1 
ATOM   591   N  N     . GLU   A  1  99   ? -11.747 48.907  70.154  1.00 14.74 ? 97   GLU   A N     1 
ATOM   592   C  CA    . GLU   A  1  99   ? -11.763 49.157  68.718  1.00 13.98 ? 97   GLU   A CA    1 
ATOM   593   C  C     . GLU   A  1  99   ? -13.185 49.231  68.191  1.00 15.89 ? 97   GLU   A C     1 
ATOM   594   O  O     . GLU   A  1  99   ? -13.505 50.107  67.380  1.00 15.74 ? 97   GLU   A O     1 
ATOM   595   C  CB    . GLU   A  1  99   ? -10.964 48.085  67.992  1.00 14.75 ? 97   GLU   A CB    1 
ATOM   596   C  CG    . GLU   A  1  99   ? -9.471  48.257  68.220  1.00 14.96 ? 97   GLU   A CG    1 
ATOM   597   C  CD    . GLU   A  1  99   ? -8.669  47.074  67.746  1.00 15.48 ? 97   GLU   A CD    1 
ATOM   598   O  OE1   . GLU   A  1  99   ? -9.288  46.086  67.307  1.00 17.01 ? 97   GLU   A OE1   1 
ATOM   599   O  OE2   . GLU   A  1  99   ? -7.418  47.130  67.812  1.00 17.47 ? 97   GLU   A OE2   1 
ATOM   600   N  N     . GLY   A  1  100  ? -14.058 48.328  68.644  1.00 14.51 ? 98   GLY   A N     1 
ATOM   601   C  CA    . GLY   A  1  100  ? -15.445 48.395  68.217  1.00 14.97 ? 98   GLY   A CA    1 
ATOM   602   C  C     . GLY   A  1  100  ? -16.086 49.711  68.604  1.00 16.82 ? 98   GLY   A C     1 
ATOM   603   O  O     . GLY   A  1  100  ? -16.759 50.351  67.797  1.00 15.18 ? 98   GLY   A O     1 
ATOM   604   N  N     . VAL   A  1  101  ? -15.873 50.137  69.849  1.00 15.35 ? 99   VAL   A N     1 
ATOM   605   C  CA    . VAL   A  1  101  ? -16.428 51.408  70.298  1.00 14.82 ? 99   VAL   A CA    1 
ATOM   606   C  C     . VAL   A  1  101  ? -15.863 52.553  69.476  1.00 14.54 ? 99   VAL   A C     1 
ATOM   607   O  O     . VAL   A  1  101  ? -16.606 53.421  68.995  1.00 15.40 ? 99   VAL   A O     1 
ATOM   608   C  CB    . VAL   A  1  101  ? -16.180 51.616  71.800  1.00 14.35 ? 99   VAL   A CB    1 
ATOM   609   C  CG1   . VAL   A  1  101  ? -16.615 53.013  72.206  1.00 15.86 ? 99   VAL   A CG1   1 
ATOM   610   C  CG2   . VAL   A  1  101  ? -16.941 50.560  72.587  1.00 15.97 ? 99   VAL   A CG2   1 
ATOM   611   N  N     . ALA   A  1  102  ? -14.537 52.559  69.282  1.00 13.79 ? 100  ALA   A N     1 
ATOM   612   C  CA    . ALA   A  1  102  ? -13.903 53.651  68.554  1.00 15.19 ? 100  ALA   A CA    1 
ATOM   613   C  C     . ALA   A  1  102  ? -14.393 53.693  67.123  1.00 14.04 ? 100  ALA   A C     1 
ATOM   614   O  O     . ALA   A  1  102  ? -14.629 54.774  66.572  1.00 16.29 ? 100  ALA   A O     1 
ATOM   615   C  CB    . ALA   A  1  102  ? -12.382 53.486  68.579  1.00 15.04 ? 100  ALA   A CB    1 
ATOM   616   N  N     . LEU   A  1  103  ? -14.544 52.524  66.505  1.00 13.94 ? 101  LEU   A N     1 
ATOM   617   C  CA    . LEU   A  1  103  ? -15.063 52.463  65.146  1.00 14.67 ? 101  LEU   A CA    1 
ATOM   618   C  C     . LEU   A  1  103  ? -16.453 53.069  65.067  1.00 15.47 ? 101  LEU   A C     1 
ATOM   619   O  O     . LEU   A  1  103  ? -16.755 53.818  64.130  1.00 17.55 ? 101  LEU   A O     1 
ATOM   620   C  CB    . LEU   A  1  103  ? -15.086 51.015  64.669  1.00 15.71 ? 101  LEU   A CB    1 
ATOM   621   C  CG    . LEU   A  1  103  ? -15.688 50.808  63.283  1.00 15.72 ? 101  LEU   A CG    1 
ATOM   622   C  CD1   . LEU   A  1  103  ? -14.876 51.575  62.247  1.00 18.80 ? 101  LEU   A CD1   1 
ATOM   623   C  CD2   . LEU   A  1  103  ? -15.747 49.339  62.978  1.00 17.70 ? 101  LEU   A CD2   1 
ATOM   624   N  N     . MET   A  1  104  ? -17.324 52.740  66.021  1.00 15.27 ? 102  MET   A N     1 
ATOM   625   C  CA    . MET   A  1  104  ? -18.675 53.282  65.967  1.00 14.87 ? 102  MET   A CA    1 
ATOM   626   C  C     . MET   A  1  104  ? -18.672 54.789  66.192  1.00 16.86 ? 102  MET   A C     1 
ATOM   627   O  O     . MET   A  1  104  ? -19.466 55.513  65.576  1.00 18.13 ? 102  MET   A O     1 
ATOM   628   C  CB    . MET   A  1  104  ? -19.578 52.551  66.961  1.00 15.58 ? 102  MET   A CB    1 
ATOM   629   C  CG    . MET   A  1  104  ? -19.698 51.068  66.646  1.00 19.28 ? 102  MET   A CG    1 
ATOM   630   S  SD    . MET   A  1  104  ? -20.184 50.728  64.923  1.00 24.43 ? 102  MET   A SD    1 
ATOM   631   C  CE    . MET   A  1  104  ? -21.858 51.346  64.918  1.00 27.18 ? 102  MET   A CE    1 
ATOM   632   N  N     . CYS   A  1  105  ? -17.777 55.283  67.052  1.00 15.07 ? 103  CYS   A N     1 
ATOM   633   C  CA    . CYS   A  1  105  ? -17.650 56.727  67.215  1.00 16.16 ? 103  CYS   A CA    1 
ATOM   634   C  C     . CYS   A  1  105  ? -17.187 57.380  65.929  1.00 18.71 ? 103  CYS   A C     1 
ATOM   635   O  O     . CYS   A  1  105  ? -17.695 58.440  65.543  1.00 19.72 ? 103  CYS   A O     1 
ATOM   636   C  CB    . CYS   A  1  105  ? -16.662 57.048  68.324  1.00 17.69 ? 103  CYS   A CB    1 
ATOM   637   S  SG    . CYS   A  1  105  ? -17.230 56.556  69.943  1.00 17.37 ? 103  CYS   A SG    1 
ATOM   638   N  N     . LEU   A  1  106  ? -16.208 56.775  65.258  1.00 15.81 ? 104  LEU   A N     1 
ATOM   639   C  CA    . LEU   A  1  106  ? -15.776 57.305  63.973  1.00 18.38 ? 104  LEU   A CA    1 
ATOM   640   C  C     . LEU   A  1  106  ? -16.921 57.291  62.979  1.00 20.73 ? 104  LEU   A C     1 
ATOM   641   O  O     . LEU   A  1  106  ? -17.121 58.258  62.234  1.00 19.14 ? 104  LEU   A O     1 
ATOM   642   C  CB    . LEU   A  1  106  ? -14.617 56.476  63.431  1.00 16.89 ? 104  LEU   A CB    1 
ATOM   643   C  CG    . LEU   A  1  106  ? -14.286 56.828  61.979  1.00 17.97 ? 104  LEU   A CG    1 
ATOM   644   C  CD1   . LEU   A  1  106  ? -13.738 58.245  61.901  1.00 23.28 ? 104  LEU   A CD1   1 
ATOM   645   C  CD2   . LEU   A  1  106  ? -13.318 55.810  61.396  1.00 20.85 ? 104  LEU   A CD2   1 
ATOM   646   N  N     . ALA   A  1  107  ? -17.665 56.186  62.929  1.00 16.12 ? 105  ALA   A N     1 
ATOM   647   C  CA    . ALA   A  1  107  ? -18.790 56.115  62.008  1.00 18.50 ? 105  ALA   A CA    1 
ATOM   648   C  C     . ALA   A  1  107  ? -19.801 57.207  62.321  1.00 21.67 ? 105  ALA   A C     1 
ATOM   649   O  O     . ALA   A  1  107  ? -20.282 57.892  61.413  1.00 20.62 ? 105  ALA   A O     1 
ATOM   650   C  CB    . ALA   A  1  107  ? -19.424 54.728  62.059  1.00 17.85 ? 105  ALA   A CB    1 
ATOM   651   N  N     . GLU   A  1  108  ? -20.108 57.407  63.607  1.00 18.21 ? 106  GLU   A N     1 
ATOM   652   C  CA    . GLU   A  1  108  ? -21.021 58.472  64.016  1.00 20.38 ? 106  GLU   A CA    1 
ATOM   653   C  C     . GLU   A  1  108  ? -20.552 59.825  63.492  1.00 23.56 ? 106  GLU   A C     1 
ATOM   654   O  O     . GLU   A  1  108  ? -21.344 60.605  62.948  1.00 26.42 ? 106  GLU   A O     1 
ATOM   655   C  CB    . GLU   A  1  108  ? -21.111 58.490  65.544  1.00 19.77 ? 106  GLU   A CB    1 
ATOM   656   C  CG    . GLU   A  1  108  ? -21.993 59.597  66.112  1.00 20.63 ? 106  GLU   A CG    1 
ATOM   657   C  CD    . GLU   A  1  108  ? -21.706 59.895  67.570  1.00 23.25 ? 106  GLU   A CD    1 
ATOM   658   O  OE1   . GLU   A  1  108  ? -21.217 58.997  68.295  1.00 23.34 ? 106  GLU   A OE1   1 
ATOM   659   O  OE2   . GLU   A  1  108  ? -21.958 61.043  67.996  1.00 26.33 ? 106  GLU   A OE2   1 
ATOM   660   N  N     . ALA   A  1  109  ? -19.256 60.109  63.631  1.00 21.81 ? 107  ALA   A N     1 
ATOM   661   C  CA    . ALA   A  1  109  ? -18.711 61.384  63.173  1.00 23.45 ? 107  ALA   A CA    1 
ATOM   662   C  C     . ALA   A  1  109  ? -18.769 61.500  61.657  1.00 26.04 ? 107  ALA   A C     1 
ATOM   663   O  O     . ALA   A  1  109  ? -19.109 62.562  61.122  1.00 29.63 ? 107  ALA   A O     1 
ATOM   664   C  CB    . ALA   A  1  109  ? -17.269 61.533  63.647  1.00 27.22 ? 107  ALA   A CB    1 
ATOM   665   N  N     . LEU   A  1  110  ? -18.416 60.424  60.948  1.00 22.76 ? 108  LEU   A N     1 
ATOM   666   C  CA    . LEU   A  1  110  ? -18.512 60.421  59.496  1.00 23.82 ? 108  LEU   A CA    1 
ATOM   667   C  C     . LEU   A  1  110  ? -19.937 60.665  59.029  1.00 25.99 ? 108  LEU   A C     1 
ATOM   668   O  O     . LEU   A  1  110  ? -20.150 61.302  57.990  1.00 28.32 ? 108  LEU   A O     1 
ATOM   669   C  CB    . LEU   A  1  110  ? -17.984 59.096  58.940  1.00 21.15 ? 108  LEU   A CB    1 
ATOM   670   C  CG    . LEU   A  1  110  ? -16.460 58.977  59.017  1.00 23.34 ? 108  LEU   A CG    1 
ATOM   671   C  CD1   . LEU   A  1  110  ? -15.982 57.570  58.716  1.00 21.95 ? 108  LEU   A CD1   1 
ATOM   672   C  CD2   . LEU   A  1  110  ? -15.818 59.977  58.054  1.00 29.43 ? 108  LEU   A CD2   1 
ATOM   673   N  N     . LEU   A  1  111  ? -20.924 60.169  59.775  1.00 24.63 ? 109  LEU   A N     1 
ATOM   674   C  CA    . LEU   A  1  111  ? -22.319 60.369  59.409  1.00 28.51 ? 109  LEU   A CA    1 
ATOM   675   C  C     . LEU   A  1  111  ? -22.803 61.784  59.687  1.00 33.13 ? 109  LEU   A C     1 
ATOM   676   O  O     . LEU   A  1  111  ? -23.893 62.141  59.226  1.00 32.92 ? 109  LEU   A O     1 
ATOM   677   C  CB    . LEU   A  1  111  ? -23.196 59.337  60.118  1.00 26.70 ? 109  LEU   A CB    1 
ATOM   678   C  CG    . LEU   A  1  111  ? -22.970 57.918  59.594  1.00 25.38 ? 109  LEU   A CG    1 
ATOM   679   C  CD1   . LEU   A  1  111  ? -23.668 56.911  60.480  1.00 28.72 ? 109  LEU   A CD1   1 
ATOM   680   C  CD2   . LEU   A  1  111  ? -23.427 57.791  58.147  1.00 26.15 ? 109  LEU   A CD2   1 
ATOM   681   N  N     . ARG   A  1  112  ? -22.035 62.586  60.428  1.00 33.21 ? 110  ARG   A N     1 
ATOM   682   C  CA    . ARG   A  1  112  ? -22.316 64.012  60.539  1.00 35.67 ? 110  ARG   A CA    1 
ATOM   683   C  C     . ARG   A  1  112  ? -21.945 64.775  59.274  1.00 38.74 ? 110  ARG   A C     1 
ATOM   684   O  O     . ARG   A  1  112  ? -22.332 65.940  59.137  1.00 41.21 ? 110  ARG   A O     1 
ATOM   685   C  CB    . ARG   A  1  112  ? -21.602 64.609  61.753  1.00 36.44 ? 110  ARG   A CB    1 
ATOM   686   C  CG    . ARG   A  1  112  ? -22.038 64.014  63.087  1.00 35.00 ? 110  ARG   A CG    1 
ATOM   687   C  CD    . ARG   A  1  112  ? -21.022 64.292  64.187  1.00 39.07 ? 110  ARG   A CD    1 
ATOM   688   N  NE    . ARG   A  1  112  ? -20.967 65.701  64.559  1.00 49.64 ? 110  ARG   A NE    1 
ATOM   689   C  CZ    . ARG   A  1  112  ? -21.626 66.236  65.578  1.00 53.70 ? 110  ARG   A CZ    1 
ATOM   690   N  NH1   . ARG   A  1  112  ? -22.416 65.507  66.352  1.00 50.90 ? 110  ARG   A NH1   1 
ATOM   691   N  NH2   . ARG   A  1  112  ? -21.488 67.535  65.830  1.00 54.82 ? 110  ARG   A NH2   1 
ATOM   692   N  N     . ILE   A  1  113  ? -21.202 64.156  58.361  1.00 37.55 ? 111  ILE   A N     1 
ATOM   693   C  CA    . ILE   A  1  113  ? -20.964 64.713  57.031  1.00 40.59 ? 111  ILE   A CA    1 
ATOM   694   C  C     . ILE   A  1  113  ? -22.191 64.431  56.172  1.00 43.06 ? 111  ILE   A C     1 
ATOM   695   O  O     . ILE   A  1  113  ? -22.459 63.268  55.839  1.00 41.75 ? 111  ILE   A O     1 
ATOM   696   C  CB    . ILE   A  1  113  ? -19.691 64.128  56.403  1.00 35.55 ? 111  ILE   A CB    1 
ATOM   697   C  CG1   . ILE   A  1  113  ? -18.468 64.526  57.226  1.00 34.79 ? 111  ILE   A CG1   1 
ATOM   698   C  CG2   . ILE   A  1  113  ? -19.549 64.584  54.958  1.00 41.73 ? 111  ILE   A CG2   1 
ATOM   699   C  CD1   . ILE   A  1  113  ? -17.200 63.881  56.762  1.00 37.90 ? 111  ILE   A CD1   1 
ATOM   700   N  N     . PRO   A  1  114  ? -22.963 65.454  55.791  1.00 49.71 ? 112  PRO   A N     1 
ATOM   701   C  CA    . PRO   A  1  114  ? -24.243 65.204  55.111  1.00 47.98 ? 112  PRO   A CA    1 
ATOM   702   C  C     . PRO   A  1  114  ? -24.118 64.566  53.735  1.00 46.25 ? 112  PRO   A C     1 
ATOM   703   O  O     . PRO   A  1  114  ? -24.823 63.596  53.436  1.00 51.52 ? 112  PRO   A O     1 
ATOM   704   C  CB    . PRO   A  1  114  ? -24.876 66.601  55.028  1.00 48.30 ? 112  PRO   A CB    1 
ATOM   705   C  CG    . PRO   A  1  114  ? -24.187 67.399  56.093  1.00 52.07 ? 112  PRO   A CG    1 
ATOM   706   C  CD    . PRO   A  1  114  ? -22.781 66.877  56.118  1.00 50.67 ? 112  PRO   A CD    1 
ATOM   707   N  N     . ASP   A  1  115  ? -23.241 65.095  52.885  1.00 47.34 ? 113  ASP   A N     1 
ATOM   708   C  CA    . ASP   A  1  115  ? -23.137 64.605  51.517  1.00 49.91 ? 113  ASP   A CA    1 
ATOM   709   C  C     . ASP   A  1  115  ? -22.400 63.273  51.480  1.00 45.65 ? 113  ASP   A C     1 
ATOM   710   O  O     . ASP   A  1  115  ? -21.279 63.159  51.984  1.00 45.34 ? 113  ASP   A O     1 
ATOM   711   C  CB    . ASP   A  1  115  ? -22.419 65.620  50.632  1.00 45.68 ? 113  ASP   A CB    1 
ATOM   712   C  CG    . ASP   A  1  115  ? -22.242 65.121  49.214  1.00 51.52 ? 113  ASP   A CG    1 
ATOM   713   O  OD1   . ASP   A  1  115  ? -23.262 64.806  48.563  1.00 54.30 ? 113  ASP   A OD1   1 
ATOM   714   O  OD2   . ASP   A  1  115  ? -21.083 65.037  48.753  1.00 52.15 ? 113  ASP   A OD2   1 
ATOM   715   N  N     . THR   A  1  116  ? -23.030 62.272  50.860  1.00 44.02 ? 114  THR   A N     1 
ATOM   716   C  CA    . THR   A  1  116  ? -22.465 60.926  50.836  1.00 42.84 ? 114  THR   A CA    1 
ATOM   717   C  C     . THR   A  1  116  ? -21.149 60.885  50.069  1.00 44.81 ? 114  THR   A C     1 
ATOM   718   O  O     . THR   A  1  116  ? -20.168 60.288  50.528  1.00 42.46 ? 114  THR   A O     1 
ATOM   719   C  CB    . THR   A  1  116  ? -23.475 59.957  50.225  1.00 41.82 ? 114  THR   A CB    1 
ATOM   720   O  OG1   . THR   A  1  116  ? -24.637 59.892  51.061  1.00 47.43 ? 114  THR   A OG1   1 
ATOM   721   C  CG2   . THR   A  1  116  ? -22.866 58.569  50.084  1.00 43.65 ? 114  THR   A CG2   1 
ATOM   722   N  N     . ALA   A  1  117  ? -21.110 61.506  48.888  1.00 41.69 ? 115  ALA   A N     1 
ATOM   723   C  CA    . ALA   A  1  117  ? -19.885 61.492  48.095  1.00 45.17 ? 115  ALA   A CA    1 
ATOM   724   C  C     . ALA   A  1  117  ? -18.740 62.166  48.839  1.00 38.81 ? 115  ALA   A C     1 
ATOM   725   O  O     . ALA   A  1  117  ? -17.593 61.707  48.775  1.00 41.80 ? 115  ALA   A O     1 
ATOM   726   C  CB    . ALA   A  1  117  ? -20.123 62.154  46.737  1.00 44.62 ? 115  ALA   A CB    1 
ATOM   727   N  N     . THR   A  1  118  ? -19.029 63.255  49.554  1.00 38.41 ? 116  THR   A N     1 
ATOM   728   C  CA    . THR   A  1  118  ? -17.986 63.917  50.330  1.00 40.77 ? 116  THR   A CA    1 
ATOM   729   C  C     . THR   A  1  118  ? -17.486 63.012  51.449  1.00 37.05 ? 116  THR   A C     1 
ATOM   730   O  O     . THR   A  1  118  ? -16.279 62.932  51.704  1.00 36.53 ? 116  THR   A O     1 
ATOM   731   C  CB    . THR   A  1  118  ? -18.522 65.227  50.908  1.00 40.64 ? 116  THR   A CB    1 
ATOM   732   O  OG1   . THR   A  1  118  ? -19.067 66.028  49.852  1.00 48.80 ? 116  THR   A OG1   1 
ATOM   733   C  CG2   . THR   A  1  118  ? -17.410 65.999  51.600  1.00 38.42 ? 116  THR   A CG2   1 
ATOM   734   N  N     . ARG   A  1  119  ? -18.405 62.322  52.123  1.00 38.04 ? 117  ARG   A N     1 
ATOM   735   C  CA    . ARG   A  1  119  ? -18.017 61.408  53.191  1.00 36.47 ? 117  ARG   A CA    1 
ATOM   736   C  C     . ARG   A  1  119  ? -17.154 60.273  52.652  1.00 34.09 ? 117  ARG   A C     1 
ATOM   737   O  O     . ARG   A  1  119  ? -16.115 59.937  53.231  1.00 34.42 ? 117  ARG   A O     1 
ATOM   738   C  CB    . ARG   A  1  119  ? -19.273 60.857  53.862  1.00 34.73 ? 117  ARG   A CB    1 
ATOM   739   C  CG    . ARG   A  1  119  ? -19.003 60.003  55.086  1.00 30.64 ? 117  ARG   A CG    1 
ATOM   740   C  CD    . ARG   A  1  119  ? -20.243 59.215  55.468  1.00 32.45 ? 117  ARG   A CD    1 
ATOM   741   N  NE    . ARG   A  1  119  ? -21.402 60.080  55.649  1.00 32.94 ? 117  ARG   A NE    1 
ATOM   742   C  CZ    . ARG   A  1  119  ? -22.575 59.900  55.056  1.00 34.51 ? 117  ARG   A CZ    1 
ATOM   743   N  NH1   . ARG   A  1  119  ? -22.798 58.865  54.265  1.00 35.06 ? 117  ARG   A NH1   1 
ATOM   744   N  NH2   . ARG   A  1  119  ? -23.553 60.776  55.274  1.00 43.10 ? 117  ARG   A NH2   1 
ATOM   745   N  N     . ASP   A  1  120  ? -17.568 59.675  51.530  1.00 35.68 ? 118  ASP   A N     1 
ATOM   746   C  CA    . ASP   A  1  120  ? -16.807 58.569  50.960  1.00 35.44 ? 118  ASP   A CA    1 
ATOM   747   C  C     . ASP   A  1  120  ? -15.435 59.018  50.480  1.00 38.49 ? 118  ASP   A C     1 
ATOM   748   O  O     . ASP   A  1  120  ? -14.468 58.254  50.577  1.00 37.51 ? 118  ASP   A O     1 
ATOM   749   C  CB    . ASP   A  1  120  ? -17.593 57.902  49.830  1.00 38.08 ? 118  ASP   A CB    1 
ATOM   750   C  CG    . ASP   A  1  120  ? -18.929 57.355  50.296  1.00 42.51 ? 118  ASP   A CG    1 
ATOM   751   O  OD1   . ASP   A  1  120  ? -19.236 57.485  51.500  1.00 42.92 ? 118  ASP   A OD1   1 
ATOM   752   O  OD2   . ASP   A  1  120  ? -19.676 56.796  49.465  1.00 42.83 ? 118  ASP   A OD2   1 
ATOM   753   N  N     . ALA   A  1  121  ? -15.325 60.248  49.971  1.00 37.43 ? 119  ALA   A N     1 
ATOM   754   C  CA    . ALA   A  1  121  ? -14.019 60.768  49.579  1.00 38.39 ? 119  ALA   A CA    1 
ATOM   755   C  C     . ALA   A  1  121  ? -13.113 60.942  50.790  1.00 36.81 ? 119  ALA   A C     1 
ATOM   756   O  O     . ALA   A  1  121  ? -11.922 60.610  50.738  1.00 39.23 ? 119  ALA   A O     1 
ATOM   757   C  CB    . ALA   A  1  121  ? -14.182 62.094  48.837  1.00 38.82 ? 119  ALA   A CB    1 
ATOM   758   N  N     . LEU   A  1  122  ? -13.658 61.464  51.891  1.00 35.84 ? 120  LEU   A N     1 
ATOM   759   C  CA    . LEU   A  1  122  ? -12.865 61.598  53.105  1.00 36.35 ? 120  LEU   A CA    1 
ATOM   760   C  C     . LEU   A  1  122  ? -12.407 60.235  53.606  1.00 36.91 ? 120  LEU   A C     1 
ATOM   761   O  O     . LEU   A  1  122  ? -11.244 60.066  53.989  1.00 34.40 ? 120  LEU   A O     1 
ATOM   762   C  CB    . LEU   A  1  122  ? -13.672 62.320  54.179  1.00 39.74 ? 120  LEU   A CB    1 
ATOM   763   C  CG    . LEU   A  1  122  ? -12.830 62.790  55.360  1.00 35.94 ? 120  LEU   A CG    1 
ATOM   764   C  CD1   . LEU   A  1  122  ? -11.818 63.820  54.899  1.00 42.14 ? 120  LEU   A CD1   1 
ATOM   765   C  CD2   . LEU   A  1  122  ? -13.709 63.353  56.453  1.00 34.76 ? 120  LEU   A CD2   1 
ATOM   766   N  N     . ILE   A  1  123  ? -13.305 59.248  53.590  1.00 34.83 ? 121  ILE   A N     1 
ATOM   767   C  CA    . ILE   A  1  123  ? -12.948 57.896  54.013  1.00 33.96 ? 121  ILE   A CA    1 
ATOM   768   C  C     . ILE   A  1  123  ? -11.823 57.347  53.143  1.00 35.10 ? 121  ILE   A C     1 
ATOM   769   O  O     . ILE   A  1  123  ? -10.763 56.950  53.640  1.00 35.40 ? 121  ILE   A O     1 
ATOM   770   C  CB    . ILE   A  1  123  ? -14.182 56.978  53.984  1.00 32.38 ? 121  ILE   A CB    1 
ATOM   771   C  CG1   . ILE   A  1  123  ? -15.208 57.420  55.034  1.00 30.28 ? 121  ILE   A CG1   1 
ATOM   772   C  CG2   . ILE   A  1  123  ? -13.764 55.517  54.161  1.00 30.13 ? 121  ILE   A CG2   1 
ATOM   773   C  CD1   . ILE   A  1  123  ? -16.522 56.693  54.941  1.00 30.25 ? 121  ILE   A CD1   1 
ATOM   774   N  N     . ARG   A  1  124  ? -12.037 57.334  51.824  1.00 34.17 ? 122  ARG   A N     1 
ATOM   775   C  CA    . ARG   A  1  124  ? -11.101 56.666  50.923  1.00 34.52 ? 122  ARG   A CA    1 
ATOM   776   C  C     . ARG   A  1  124  ? -9.755  57.378  50.871  1.00 40.20 ? 122  ARG   A C     1 
ATOM   777   O  O     . ARG   A  1  124  ? -8.703  56.728  50.888  1.00 41.53 ? 122  ARG   A O     1 
ATOM   778   C  CB    . ARG   A  1  124  ? -11.704 56.565  49.522  1.00 37.07 ? 122  ARG   A CB    1 
ATOM   779   N  N     . ASP   A  1  125  ? -9.763  58.708  50.813  1.00 42.72 ? 123  ASP   A N     1 
ATOM   780   C  CA    . ASP   A  1  125  ? -8.535  59.449  50.553  1.00 47.18 ? 123  ASP   A CA    1 
ATOM   781   C  C     . ASP   A  1  125  ? -7.826  59.914  51.817  1.00 48.37 ? 123  ASP   A C     1 
ATOM   782   O  O     . ASP   A  1  125  ? -6.594  60.027  51.816  1.00 50.91 ? 123  ASP   A O     1 
ATOM   783   C  CB    . ASP   A  1  125  ? -8.821  60.656  49.652  1.00 53.92 ? 123  ASP   A CB    1 
ATOM   784   C  CG    . ASP   A  1  125  ? -9.540  60.275  48.367  1.00 55.16 ? 123  ASP   A CG    1 
ATOM   785   O  OD1   . ASP   A  1  125  ? -9.312  59.158  47.856  1.00 58.18 ? 123  ASP   A OD1   1 
ATOM   786   O  OD2   . ASP   A  1  125  ? -10.335 61.099  47.865  1.00 52.64 ? 123  ASP   A OD2   1 
ATOM   787   N  N     . LYS   A  1  126  ? -8.561  60.183  52.895  1.00 41.85 ? 124  LYS   A N     1 
ATOM   788   C  CA    . LYS   A  1  126  ? -7.978  60.780  54.090  1.00 38.61 ? 124  LYS   A CA    1 
ATOM   789   C  C     . LYS   A  1  126  ? -8.047  59.881  55.316  1.00 43.36 ? 124  LYS   A C     1 
ATOM   790   O  O     . LYS   A  1  126  ? -7.023  59.664  55.972  1.00 47.83 ? 124  LYS   A O     1 
ATOM   791   C  CB    . LYS   A  1  126  ? -8.633  62.140  54.383  1.00 46.71 ? 124  LYS   A CB    1 
ATOM   792   N  N     . ILE   A  1  127  ? -9.226  59.352  55.654  1.00 39.99 ? 125  ILE   A N     1 
ATOM   793   C  CA    . ILE   A  1  127  ? -9.362  58.568  56.882  1.00 33.55 ? 125  ILE   A CA    1 
ATOM   794   C  C     . ILE   A  1  127  ? -8.594  57.256  56.773  1.00 37.80 ? 125  ILE   A C     1 
ATOM   795   O  O     . ILE   A  1  127  ? -7.841  56.882  57.680  1.00 42.97 ? 125  ILE   A O     1 
ATOM   796   C  CB    . ILE   A  1  127  ? -10.844 58.325  57.219  1.00 33.30 ? 125  ILE   A CB    1 
ATOM   797   C  CG1   . ILE   A  1  127  ? -11.628 59.639  57.222  1.00 38.59 ? 125  ILE   A CG1   1 
ATOM   798   C  CG2   . ILE   A  1  127  ? -10.968 57.641  58.580  1.00 33.73 ? 125  ILE   A CG2   1 
ATOM   799   C  CD1   . ILE   A  1  127  ? -11.078 60.665  58.172  1.00 36.85 ? 125  ILE   A CD1   1 
ATOM   800   N  N     . ALA   A  1  128  ? -8.778  56.536  55.664  1.00 35.07 ? 126  ALA   A N     1 
ATOM   801   C  CA    . ALA   A  1  128  ? -8.217  55.195  55.543  1.00 32.59 ? 126  ALA   A CA    1 
ATOM   802   C  C     . ALA   A  1  128  ? -6.698  55.207  55.596  1.00 40.29 ? 126  ALA   A C     1 
ATOM   803   O  O     . ALA   A  1  128  ? -6.091  54.227  56.039  1.00 38.15 ? 126  ALA   A O     1 
ATOM   804   C  CB    . ALA   A  1  128  ? -8.699  54.532  54.254  1.00 34.62 ? 126  ALA   A CB    1 
ATOM   805   N  N     . ASP   A  1  129  ? -6.072  56.295  55.157  1.00 51.38 ? 127  ASP   A N     1 
ATOM   806   C  CA    . ASP   A  1  129  ? -4.615  56.430  55.170  1.00 58.25 ? 127  ASP   A CA    1 
ATOM   807   C  C     . ASP   A  1  129  ? -4.122  57.043  56.477  1.00 59.30 ? 127  ASP   A C     1 
ATOM   808   O  O     . ASP   A  1  129  ? -3.298  57.957  56.488  1.00 65.91 ? 127  ASP   A O     1 
ATOM   809   C  CB    . ASP   A  1  129  ? -4.153  57.243  53.966  1.00 54.84 ? 127  ASP   A CB    1 
ATOM   810   N  N     . GLY   A  1  130  ? -4.632  56.528  57.594  1.00 59.58 ? 128  GLY   A N     1 
ATOM   811   C  CA    . GLY   A  1  130  ? -4.308  57.058  58.900  1.00 59.08 ? 128  GLY   A CA    1 
ATOM   812   C  C     . GLY   A  1  130  ? -4.765  58.502  59.032  1.00 60.77 ? 128  GLY   A C     1 
ATOM   813   O  O     . GLY   A  1  130  ? -5.638  58.984  58.306  1.00 64.53 ? 128  GLY   A O     1 
ATOM   814   N  N     . ASN   A  1  131  ? -4.152  59.192  59.994  1.00 61.77 ? 129  ASN   A N     1 
ATOM   815   C  CA    . ASN   A  1  131  ? -4.351  60.630  60.190  1.00 59.55 ? 129  ASN   A CA    1 
ATOM   816   C  C     . ASN   A  1  131  ? -5.831  60.999  60.275  1.00 48.73 ? 129  ASN   A C     1 
ATOM   817   O  O     . ASN   A  1  131  ? -6.263  62.038  59.773  1.00 54.32 ? 129  ASN   A O     1 
ATOM   818   C  CB    . ASN   A  1  131  ? -3.625  61.453  59.122  1.00 59.16 ? 129  ASN   A CB    1 
ATOM   819   N  N     . TRP   A  1  132  ? -6.621  60.131  60.914  1.00 48.19 ? 130  TRP   A N     1 
ATOM   820   C  CA    . TRP   A  1  132  ? -8.032  60.445  61.120  1.00 41.33 ? 130  TRP   A CA    1 
ATOM   821   C  C     . TRP   A  1  132  ? -8.204  61.665  62.010  1.00 37.90 ? 130  TRP   A C     1 
ATOM   822   O  O     . TRP   A  1  132  ? -9.184  62.406  61.868  1.00 44.37 ? 130  TRP   A O     1 
ATOM   823   C  CB    . TRP   A  1  132  ? -8.765  59.249  61.732  1.00 37.45 ? 130  TRP   A CB    1 
ATOM   824   C  CG    . TRP   A  1  132  ? -8.212  58.807  63.060  1.00 30.74 ? 130  TRP   A CG    1 
ATOM   825   C  CD1   . TRP   A  1  132  ? -7.301  57.813  63.273  1.00 30.12 ? 130  TRP   A CD1   1 
ATOM   826   C  CD2   . TRP   A  1  132  ? -8.538  59.335  64.356  1.00 25.23 ? 130  TRP   A CD2   1 
ATOM   827   N  NE1   . TRP   A  1  132  ? -7.042  57.687  64.617  1.00 29.54 ? 130  TRP   A NE1   1 
ATOM   828   C  CE2   . TRP   A  1  132  ? -7.783  58.612  65.304  1.00 24.75 ? 130  TRP   A CE2   1 
ATOM   829   C  CE3   . TRP   A  1  132  ? -9.391  60.346  64.806  1.00 26.57 ? 130  TRP   A CE3   1 
ATOM   830   C  CZ2   . TRP   A  1  132  ? -7.852  58.869  66.668  1.00 25.47 ? 130  TRP   A CZ2   1 
ATOM   831   C  CZ3   . TRP   A  1  132  ? -9.458  60.601  66.164  1.00 25.11 ? 130  TRP   A CZ3   1 
ATOM   832   C  CH2   . TRP   A  1  132  ? -8.698  59.864  67.080  1.00 25.06 ? 130  TRP   A CH2   1 
ATOM   833   N  N     . LYS   A  1  133  ? -7.268  61.884  62.935  1.00 42.36 ? 131  LYS   A N     1 
ATOM   834   C  CA    . LYS   A  1  133  ? -7.373  63.021  63.842  1.00 47.38 ? 131  LYS   A CA    1 
ATOM   835   C  C     . LYS   A  1  133  ? -7.287  64.339  63.083  1.00 55.58 ? 131  LYS   A C     1 
ATOM   836   O  O     . LYS   A  1  133  ? -7.981  65.305  63.421  1.00 60.94 ? 131  LYS   A O     1 
ATOM   837   C  CB    . LYS   A  1  133  ? -6.279  62.937  64.907  1.00 41.36 ? 131  LYS   A CB    1 
ATOM   838   N  N     . SER   A  1  134  ? -6.452  64.388  62.041  1.00 57.99 ? 132  SER   A N     1 
ATOM   839   C  CA    . SER   A  1  134  ? -6.262  65.626  61.292  1.00 59.85 ? 132  SER   A CA    1 
ATOM   840   C  C     . SER   A  1  134  ? -7.553  66.096  60.632  1.00 59.98 ? 132  SER   A C     1 
ATOM   841   O  O     . SER   A  1  134  ? -7.756  67.303  60.461  1.00 64.51 ? 132  SER   A O     1 
ATOM   842   C  CB    . SER   A  1  134  ? -5.158  65.441  60.248  1.00 56.29 ? 132  SER   A CB    1 
ATOM   843   N  N     . HIS   A  1  135  ? -8.441  65.170  60.269  1.00 58.90 ? 133  HIS   A N     1 
ATOM   844   C  CA    . HIS   A  1  135  ? -9.646  65.522  59.530  1.00 58.20 ? 133  HIS   A CA    1 
ATOM   845   C  C     . HIS   A  1  135  ? -10.911 65.521  60.378  1.00 59.35 ? 133  HIS   A C     1 
ATOM   846   O  O     . HIS   A  1  135  ? -11.917 66.102  59.957  1.00 59.85 ? 133  HIS   A O     1 
ATOM   847   C  CB    . HIS   A  1  135  ? -9.834  64.581  58.335  1.00 55.28 ? 133  HIS   A CB    1 
ATOM   848   C  CG    . HIS   A  1  135  ? -8.641  64.510  57.434  1.00 60.25 ? 133  HIS   A CG    1 
ATOM   849   N  ND1   . HIS   A  1  135  ? -7.518  63.771  57.741  1.00 59.04 ? 133  HIS   A ND1   1 
ATOM   850   C  CD2   . HIS   A  1  135  ? -8.391  65.092  56.237  1.00 57.50 ? 133  HIS   A CD2   1 
ATOM   851   C  CE1   . HIS   A  1  135  ? -6.631  63.897  56.771  1.00 59.46 ? 133  HIS   A CE1   1 
ATOM   852   N  NE2   . HIS   A  1  135  ? -7.136  64.694  55.846  1.00 61.53 ? 133  HIS   A NE2   1 
ATOM   853   N  N     . LEU   A  1  136  ? -10.890 64.890  61.548  1.00 60.18 ? 134  LEU   A N     1 
ATOM   854   C  CA    . LEU   A  1  136  ? -12.058 64.868  62.423  1.00 61.61 ? 134  LEU   A CA    1 
ATOM   855   C  C     . LEU   A  1  136  ? -11.653 65.052  63.886  1.00 65.32 ? 134  LEU   A C     1 
ATOM   856   O  O     . LEU   A  1  136  ? -12.427 65.563  64.698  1.00 64.51 ? 134  LEU   A O     1 
ATOM   857   C  CB    . LEU   A  1  136  ? -12.837 63.560  62.251  1.00 58.53 ? 134  LEU   A CB    1 
ATOM   858   C  CG    . LEU   A  1  136  ? -13.525 63.297  60.909  1.00 51.87 ? 134  LEU   A CG    1 
ATOM   859   C  CD1   . LEU   A  1  136  ? -13.946 61.842  60.811  1.00 45.03 ? 134  LEU   A CD1   1 
ATOM   860   C  CD2   . LEU   A  1  136  ? -14.725 64.213  60.725  1.00 47.58 ? 134  LEU   A CD2   1 
ATOM   861   N  N     . SER   A  1  139  ? -12.478 70.228  67.337  1.00 41.42 ? 137  SER   A N     1 
ATOM   862   C  CA    . SER   A  1  139  ? -13.281 71.007  68.280  1.00 41.51 ? 137  SER   A CA    1 
ATOM   863   C  C     . SER   A  1  139  ? -14.106 70.097  69.189  1.00 40.94 ? 137  SER   A C     1 
ATOM   864   O  O     . SER   A  1  139  ? -14.392 70.432  70.340  1.00 39.36 ? 137  SER   A O     1 
ATOM   865   C  CB    . SER   A  1  139  ? -14.207 71.968  67.528  1.00 40.84 ? 137  SER   A CB    1 
ATOM   866   N  N     . ARG   A  1  140  ? -14.487 68.941  68.658  1.00 32.56 ? 138  ARG   A N     1 
ATOM   867   C  CA    . ARG   A  1  140  ? -15.316 67.979  69.367  1.00 30.31 ? 138  ARG   A CA    1 
ATOM   868   C  C     . ARG   A  1  140  ? -14.632 66.626  69.286  1.00 30.13 ? 138  ARG   A C     1 
ATOM   869   O  O     . ARG   A  1  140  ? -14.295 66.163  68.191  1.00 30.37 ? 138  ARG   A O     1 
ATOM   870   C  CB    . ARG   A  1  140  ? -16.703 67.906  68.721  1.00 33.32 ? 138  ARG   A CB    1 
ATOM   871   C  CG    . ARG   A  1  140  ? -17.587 66.758  69.184  1.00 37.52 ? 138  ARG   A CG    1 
ATOM   872   C  CD    . ARG   A  1  140  ? -18.803 66.633  68.268  1.00 43.08 ? 138  ARG   A CD    1 
ATOM   873   N  NE    . ARG   A  1  140  ? -19.686 65.531  68.633  1.00 48.40 ? 138  ARG   A NE    1 
ATOM   874   C  CZ    . ARG   A  1  140  ? -19.563 64.288  68.183  1.00 48.06 ? 138  ARG   A CZ    1 
ATOM   875   N  NH1   . ARG   A  1  140  ? -18.573 63.939  67.374  1.00 42.49 ? 138  ARG   A NH1   1 
ATOM   876   N  NH2   . ARG   A  1  140  ? -20.455 63.372  68.554  1.00 44.63 ? 138  ARG   A NH2   1 
ATOM   877   N  N     . SER   A  1  141  ? -14.401 66.012  70.443  1.00 27.41 ? 139  SER   A N     1 
ATOM   878   C  CA    . SER   A  1  141  ? -13.842 64.672  70.463  1.00 21.06 ? 139  SER   A CA    1 
ATOM   879   C  C     . SER   A  1  141  ? -14.712 63.741  69.634  1.00 21.62 ? 139  SER   A C     1 
ATOM   880   O  O     . SER   A  1  141  ? -15.942 63.807  69.673  1.00 22.57 ? 139  SER   A O     1 
ATOM   881   C  CB    . SER   A  1  141  ? -13.794 64.158  71.898  1.00 22.92 ? 139  SER   A CB    1 
ATOM   882   O  OG    . SER   A  1  141  ? -13.340 62.814  71.931  1.00 22.00 ? 139  SER   A OG    1 
ATOM   883   N  N     . LEU   A  1  142  ? -14.065 62.869  68.868  1.00 22.81 ? 140  LEU   A N     1 
ATOM   884   C  CA    . LEU   A  1  142  ? -14.811 61.831  68.175  1.00 19.03 ? 140  LEU   A CA    1 
ATOM   885   C  C     . LEU   A  1  142  ? -15.589 60.961  69.148  1.00 18.02 ? 140  LEU   A C     1 
ATOM   886   O  O     . LEU   A  1  142  ? -16.567 60.310  68.762  1.00 20.37 ? 140  LEU   A O     1 
ATOM   887   C  CB    . LEU   A  1  142  ? -13.814 60.945  67.432  1.00 21.03 ? 140  LEU   A CB    1 
ATOM   888   C  CG    . LEU   A  1  142  ? -14.157 60.565  66.005  1.00 25.50 ? 140  LEU   A CG    1 
ATOM   889   C  CD1   . LEU   A  1  142  ? -14.016 61.778  65.112  1.00 30.77 ? 140  LEU   A CD1   1 
ATOM   890   C  CD2   . LEU   A  1  142  ? -13.232 59.470  65.560  1.00 26.08 ? 140  LEU   A CD2   1 
ATOM   891   N  N     . PHE   A  1  143  ? -15.172 60.943  70.407  1.00 16.77 ? 141  PHE   A N     1 
ATOM   892   C  CA    . PHE   A  1  143  ? -15.598 59.942  71.359  1.00 17.11 ? 141  PHE   A CA    1 
ATOM   893   C  C     . PHE   A  1  143  ? -16.608 60.487  72.356  1.00 18.84 ? 141  PHE   A C     1 
ATOM   894   O  O     . PHE   A  1  143  ? -16.854 59.851  73.381  1.00 17.61 ? 141  PHE   A O     1 
ATOM   895   C  CB    . PHE   A  1  143  ? -14.361 59.351  72.038  1.00 16.54 ? 141  PHE   A CB    1 
ATOM   896   C  CG    . PHE   A  1  143  ? -13.346 58.867  71.048  1.00 16.78 ? 141  PHE   A CG    1 
ATOM   897   C  CD1   . PHE   A  1  143  ? -13.690 57.880  70.143  1.00 16.52 ? 141  PHE   A CD1   1 
ATOM   898   C  CD2   . PHE   A  1  143  ? -12.081 59.427  70.977  1.00 17.15 ? 141  PHE   A CD2   1 
ATOM   899   C  CE1   . PHE   A  1  143  ? -12.792 57.434  69.203  1.00 17.55 ? 141  PHE   A CE1   1 
ATOM   900   C  CE2   . PHE   A  1  143  ? -11.172 58.978  70.035  1.00 17.46 ? 141  PHE   A CE2   1 
ATOM   901   C  CZ    . PHE   A  1  143  ? -11.524 57.987  69.149  1.00 15.56 ? 141  PHE   A CZ    1 
ATOM   902   N  N     . VAL   A  1  144  ? -17.241 61.622  72.035  1.00 17.71 ? 142  VAL   A N     1 
ATOM   903   C  CA    . VAL   A  1  144  ? -18.203 62.240  72.950  1.00 18.51 ? 142  VAL   A CA    1 
ATOM   904   C  C     . VAL   A  1  144  ? -19.281 61.258  73.378  1.00 19.76 ? 142  VAL   A C     1 
ATOM   905   O  O     . VAL   A  1  144  ? -19.685 61.229  74.546  1.00 21.25 ? 142  VAL   A O     1 
ATOM   906   C  CB    . VAL   A  1  144  ? -18.807 63.513  72.326  1.00 19.52 ? 142  VAL   A CB    1 
ATOM   907   C  CG1   . VAL   A  1  144  ? -20.028 63.986  73.122  1.00 23.78 ? 142  VAL   A CG1   1 
ATOM   908   C  CG2   . VAL   A  1  144  ? -17.758 64.602  72.254  1.00 24.20 ? 142  VAL   A CG2   1 
ATOM   909   N  N     . ASN   A  1  145  ? -19.767 60.439  72.450  1.00 16.61 ? 143  ASN   A N     1 
ATOM   910   C  CA    . ASN   A  1  145  ? -20.824 59.493  72.776  1.00 18.67 ? 143  ASN   A CA    1 
ATOM   911   C  C     . ASN   A  1  145  ? -20.303 58.080  72.973  1.00 19.71 ? 143  ASN   A C     1 
ATOM   912   O  O     . ASN   A  1  145  ? -21.069 57.117  72.860  1.00 17.86 ? 143  ASN   A O     1 
ATOM   913   C  CB    . ASN   A  1  145  ? -21.908 59.535  71.704  1.00 19.05 ? 143  ASN   A CB    1 
ATOM   914   C  CG    . ASN   A  1  145  ? -22.655 60.839  71.709  1.00 22.28 ? 143  ASN   A CG    1 
ATOM   915   O  OD1   . ASN   A  1  145  ? -23.170 61.255  72.746  1.00 26.17 ? 143  ASN   A OD1   1 
ATOM   916   N  ND2   . ASN   A  1  145  ? -22.692 61.508  70.570  1.00 25.28 ? 143  ASN   A ND2   1 
ATOM   917   N  N     . ALA   A  1  146  ? -19.018 57.928  73.292  1.00 17.07 ? 144  ALA   A N     1 
ATOM   918   C  CA    . ALA   A  1  146  ? -18.470 56.582  73.404  1.00 16.92 ? 144  ALA   A CA    1 
ATOM   919   C  C     . ALA   A  1  146  ? -19.101 55.771  74.531  1.00 16.78 ? 144  ALA   A C     1 
ATOM   920   O  O     . ALA   A  1  146  ? -19.106 54.540  74.464  1.00 19.26 ? 144  ALA   A O     1 
ATOM   921   C  CB    . ALA   A  1  146  ? -16.960 56.647  73.574  1.00 16.46 ? 144  ALA   A CB    1 
ATOM   922   N  N     . ALA   A  1  147  ? -19.645 56.415  75.567  1.00 18.93 ? 145  ALA   A N     1 
ATOM   923   C  CA    . ALA   A  1  147  ? -20.294 55.626  76.612  1.00 20.09 ? 145  ALA   A CA    1 
ATOM   924   C  C     . ALA   A  1  147  ? -21.513 54.910  76.057  1.00 20.22 ? 145  ALA   A C     1 
ATOM   925   O  O     . ALA   A  1  147  ? -21.780 53.750  76.394  1.00 20.47 ? 145  ALA   A O     1 
ATOM   926   C  CB    . ALA   A  1  147  ? -20.670 56.511  77.802  1.00 24.85 ? 145  ALA   A CB    1 
ATOM   927   N  N     . THR   A  1  148  ? -22.232 55.571  75.155  1.00 18.28 ? 146  THR   A N     1 
ATOM   928   C  CA    . THR   A  1  148  ? -23.373 54.945  74.507  1.00 19.02 ? 146  THR   A CA    1 
ATOM   929   C  C     . THR   A  1  148  ? -22.917 53.811  73.604  1.00 17.28 ? 146  THR   A C     1 
ATOM   930   O  O     . THR   A  1  148  ? -23.426 52.690  73.690  1.00 18.92 ? 146  THR   A O     1 
ATOM   931   C  CB    . THR   A  1  148  ? -24.121 56.005  73.707  1.00 21.06 ? 146  THR   A CB    1 
ATOM   932   O  OG1   . THR   A  1  148  ? -24.504 57.051  74.603  1.00 23.32 ? 146  THR   A OG1   1 
ATOM   933   C  CG2   . THR   A  1  148  ? -25.363 55.422  73.040  1.00 24.81 ? 146  THR   A CG2   1 
ATOM   934   N  N     . TRP   A  1  149  ? -21.936 54.078  72.736  1.00 17.54 ? 147  TRP   A N     1 
ATOM   935   C  CA    . TRP   A  1  149  ? -21.428 53.009  71.888  1.00 18.31 ? 147  TRP   A CA    1 
ATOM   936   C  C     . TRP   A  1  149  ? -20.805 51.888  72.705  1.00 15.13 ? 147  TRP   A C     1 
ATOM   937   O  O     . TRP   A  1  149  ? -20.853 50.727  72.289  1.00 17.26 ? 147  TRP   A O     1 
ATOM   938   C  CB    . TRP   A  1  149  ? -20.428 53.559  70.875  1.00 17.73 ? 147  TRP   A CB    1 
ATOM   939   C  CG    . TRP   A  1  149  ? -21.083 54.448  69.868  1.00 17.41 ? 147  TRP   A CG    1 
ATOM   940   C  CD1   . TRP   A  1  149  ? -20.865 55.778  69.694  1.00 19.24 ? 147  TRP   A CD1   1 
ATOM   941   C  CD2   . TRP   A  1  149  ? -22.086 54.074  68.919  1.00 19.32 ? 147  TRP   A CD2   1 
ATOM   942   N  NE1   . TRP   A  1  149  ? -21.655 56.259  68.675  1.00 18.84 ? 147  TRP   A NE1   1 
ATOM   943   C  CE2   . TRP   A  1  149  ? -22.416 55.231  68.185  1.00 18.68 ? 147  TRP   A CE2   1 
ATOM   944   C  CE3   . TRP   A  1  149  ? -22.727 52.872  68.609  1.00 19.11 ? 147  TRP   A CE3   1 
ATOM   945   C  CZ2   . TRP   A  1  149  ? -23.369 55.224  67.164  1.00 21.48 ? 147  TRP   A CZ2   1 
ATOM   946   C  CZ3   . TRP   A  1  149  ? -23.674 52.865  67.588  1.00 23.89 ? 147  TRP   A CZ3   1 
ATOM   947   C  CH2   . TRP   A  1  149  ? -23.981 54.034  66.880  1.00 25.70 ? 147  TRP   A CH2   1 
ATOM   948   N  N     . GLY   A  1  150  ? -20.208 52.214  73.856  1.00 16.04 ? 148  GLY   A N     1 
ATOM   949   C  CA    . GLY   A  1  150  ? -19.721 51.170  74.744  1.00 18.83 ? 148  GLY   A CA    1 
ATOM   950   C  C     . GLY   A  1  150  ? -20.830 50.243  75.191  1.00 18.61 ? 148  GLY   A C     1 
ATOM   951   O  O     . GLY   A  1  150  ? -20.657 49.025  75.233  1.00 20.54 ? 148  GLY   A O     1 
ATOM   952   N  N     . LEU   A  1  151  ? -21.995 50.809  75.527  1.00 18.78 ? 149  LEU   A N     1 
ATOM   953   C  CA    A LEU   A  1  151  ? -23.138 49.973  75.877  0.43 21.62 ? 149  LEU   A CA    1 
ATOM   954   C  CA    B LEU   A  1  151  ? -23.138 49.976  75.879  0.57 21.61 ? 149  LEU   A CA    1 
ATOM   955   C  C     . LEU   A  1  151  ? -23.551 49.100  74.703  1.00 19.95 ? 149  LEU   A C     1 
ATOM   956   O  O     . LEU   A  1  151  ? -23.829 47.912  74.875  1.00 23.91 ? 149  LEU   A O     1 
ATOM   957   C  CB    A LEU   A  1  151  ? -24.307 50.842  76.341  0.43 23.96 ? 149  LEU   A CB    1 
ATOM   958   C  CB    B LEU   A  1  151  ? -24.291 50.867  76.342  0.57 23.99 ? 149  LEU   A CB    1 
ATOM   959   C  CG    A LEU   A  1  151  ? -24.397 51.077  77.846  0.43 23.95 ? 149  LEU   A CG    1 
ATOM   960   C  CG    B LEU   A  1  151  ? -25.380 50.263  77.221  0.57 23.66 ? 149  LEU   A CG    1 
ATOM   961   C  CD1   A LEU   A  1  151  ? -25.427 52.148  78.151  0.43 22.62 ? 149  LEU   A CD1   1 
ATOM   962   C  CD1   B LEU   A  1  151  ? -24.775 49.403  78.316  0.57 23.85 ? 149  LEU   A CD1   1 
ATOM   963   C  CD2   A LEU   A  1  151  ? -24.747 49.781  78.571  0.43 22.89 ? 149  LEU   A CD2   1 
ATOM   964   C  CD2   B LEU   A  1  151  ? -26.178 51.392  77.837  0.57 26.57 ? 149  LEU   A CD2   1 
ATOM   965   N  N     . VAL   A  1  152  ? -23.581 49.673  73.499  1.00 18.25 ? 150  VAL   A N     1 
ATOM   966   C  CA    . VAL   A  1  152  ? -23.947 48.918  72.299  1.00 21.30 ? 150  VAL   A CA    1 
ATOM   967   C  C     . VAL   A  1  152  ? -22.975 47.767  72.063  1.00 23.07 ? 150  VAL   A C     1 
ATOM   968   O  O     . VAL   A  1  152  ? -23.378 46.634  71.764  1.00 26.33 ? 150  VAL   A O     1 
ATOM   969   C  CB    . VAL   A  1  152  ? -24.019 49.857  71.081  1.00 21.82 ? 150  VAL   A CB    1 
ATOM   970   C  CG1   . VAL   A  1  152  ? -24.119 49.058  69.791  1.00 25.57 ? 150  VAL   A CG1   1 
ATOM   971   C  CG2   . VAL   A  1  152  ? -25.191 50.829  71.219  1.00 23.15 ? 150  VAL   A CG2   1 
ATOM   972   N  N     . VAL   A  1  153  ? -21.676 48.046  72.172  1.00 20.55 ? 151  VAL   A N     1 
ATOM   973   C  CA    . VAL   A  1  153  ? -20.664 47.059  71.818  1.00 23.66 ? 151  VAL   A CA    1 
ATOM   974   C  C     . VAL   A  1  153  ? -20.469 46.036  72.928  1.00 22.38 ? 151  VAL   A C     1 
ATOM   975   O  O     . VAL   A  1  153  ? -20.358 44.835  72.663  1.00 26.18 ? 151  VAL   A O     1 
ATOM   976   C  CB    . VAL   A  1  153  ? -19.348 47.771  71.464  1.00 21.50 ? 151  VAL   A CB    1 
ATOM   977   C  CG1   . VAL   A  1  153  ? -18.240 46.757  71.243  1.00 23.92 ? 151  VAL   A CG1   1 
ATOM   978   C  CG2   . VAL   A  1  153  ? -19.537 48.647  70.246  1.00 21.36 ? 151  VAL   A CG2   1 
ATOM   979   N  N     . THR   A  1  154  ? -20.387 46.488  74.180  1.00 22.08 ? 152  THR   A N     1 
ATOM   980   C  CA    . THR   A  1  154  ? -19.966 45.630  75.279  1.00 22.58 ? 152  THR   A CA    1 
ATOM   981   C  C     . THR   A  1  154  ? -21.096 45.252  76.222  1.00 26.73 ? 152  THR   A C     1 
ATOM   982   O  O     . THR   A  1  154  ? -20.920 44.331  77.027  1.00 28.39 ? 152  THR   A O     1 
ATOM   983   C  CB    . THR   A  1  154  ? -18.857 46.298  76.108  1.00 25.08 ? 152  THR   A CB    1 
ATOM   984   O  OG1   . THR   A  1  154  ? -19.414 47.363  76.892  1.00 25.33 ? 152  THR   A OG1   1 
ATOM   985   C  CG2   . THR   A  1  154  ? -17.761 46.859  75.216  1.00 24.35 ? 152  THR   A CG2   1 
ATOM   986   N  N     . GLY   A  1  155  ? -22.232 45.941  76.165  1.00 24.08 ? 153  GLY   A N     1 
ATOM   987   C  CA    . GLY   A  1  155  ? -23.289 45.739  77.133  1.00 23.62 ? 153  GLY   A CA    1 
ATOM   988   C  C     . GLY   A  1  155  ? -23.030 46.366  78.482  1.00 29.00 ? 153  GLY   A C     1 
ATOM   989   O  O     . GLY   A  1  155  ? -23.871 46.239  79.382  1.00 27.10 ? 153  GLY   A O     1 
ATOM   990   N  N     . LYS   A  1  156  ? -21.896 47.034  78.653  1.00 26.22 ? 154  LYS   A N     1 
ATOM   991   C  CA    . LYS   A  1  156  ? -21.511 47.638  79.916  1.00 27.40 ? 154  LYS   A CA    1 
ATOM   992   C  C     . LYS   A  1  156  ? -21.505 49.151  79.767  1.00 28.13 ? 154  LYS   A C     1 
ATOM   993   O  O     . LYS   A  1  156  ? -21.134 49.685  78.716  1.00 24.79 ? 154  LYS   A O     1 
ATOM   994   C  CB    . LYS   A  1  156  ? -20.123 47.160  80.349  1.00 33.60 ? 154  LYS   A CB    1 
ATOM   995   N  N     . LEU   A  1  157  ? -21.932 49.836  80.815  1.00 25.30 ? 155  LEU   A N     1 
ATOM   996   C  CA    . LEU   A  1  157  ? -21.941 51.287  80.839  1.00 27.89 ? 155  LEU   A CA    1 
ATOM   997   C  C     . LEU   A  1  157  ? -20.717 51.781  81.601  1.00 34.18 ? 155  LEU   A C     1 
ATOM   998   O  O     . LEU   A  1  157  ? -20.420 51.292  82.696  1.00 34.42 ? 155  LEU   A O     1 
ATOM   999   C  CB    . LEU   A  1  157  ? -23.210 51.783  81.519  1.00 26.79 ? 155  LEU   A CB    1 
ATOM   1000  C  CG    . LEU   A  1  157  ? -23.269 53.290  81.715  1.00 31.10 ? 155  LEU   A CG    1 
ATOM   1001  C  CD1   . LEU   A  1  157  ? -23.210 54.011  80.374  1.00 30.09 ? 155  LEU   A CD1   1 
ATOM   1002  C  CD2   . LEU   A  1  157  ? -24.537 53.624  82.463  1.00 31.82 ? 155  LEU   A CD2   1 
ATOM   1003  N  N     . THR   A  1  158  ? -19.996 52.725  81.004  1.00 38.09 ? 156  THR   A N     1 
ATOM   1004  C  CA    . THR   A  1  158  ? -18.923 53.448  81.673  1.00 38.56 ? 156  THR   A CA    1 
ATOM   1005  C  C     . THR   A  1  158  ? -19.265 54.928  81.616  1.00 39.95 ? 156  THR   A C     1 
ATOM   1006  O  O     . THR   A  1  158  ? -19.502 55.469  80.531  1.00 44.47 ? 156  THR   A O     1 
ATOM   1007  C  CB    . THR   A  1  158  ? -17.573 53.195  80.995  1.00 43.97 ? 156  THR   A CB    1 
ATOM   1008  O  OG1   . THR   A  1  158  ? -17.403 51.792  80.754  1.00 44.60 ? 156  THR   A OG1   1 
ATOM   1009  C  CG2   . THR   A  1  158  ? -16.436 53.682  81.883  1.00 47.46 ? 156  THR   A CG2   1 
ATOM   1010  N  N     . SER   A  1  159  ? -19.288 55.578  82.782  1.00 30.35 ? 157  SER   A N     1 
ATOM   1011  C  CA    . SER   A  1  159  ? -19.812 56.939  82.871  1.00 24.73 ? 157  SER   A CA    1 
ATOM   1012  C  C     . SER   A  1  159  ? -18.977 57.929  82.064  1.00 28.78 ? 157  SER   A C     1 
ATOM   1013  O  O     . SER   A  1  159  ? -19.516 58.866  81.465  1.00 34.09 ? 157  SER   A O     1 
ATOM   1014  C  CB    . SER   A  1  159  ? -19.889 57.368  84.335  1.00 33.49 ? 157  SER   A CB    1 
ATOM   1015  O  OG    . SER   A  1  159  ? -18.706 57.002  85.025  1.00 38.14 ? 157  SER   A OG    1 
ATOM   1016  N  N     . THR   A  1  160  ? -17.666 57.755  82.053  1.00 25.41 ? 158  THR   A N     1 
ATOM   1017  C  CA    . THR   A  1  160  ? -16.786 58.611  81.281  1.00 22.82 ? 158  THR   A CA    1 
ATOM   1018  C  C     . THR   A  1  160  ? -16.036 57.764  80.270  1.00 20.70 ? 158  THR   A C     1 
ATOM   1019  O  O     . THR   A  1  160  ? -16.023 56.534  80.334  1.00 24.12 ? 158  THR   A O     1 
ATOM   1020  C  CB    . THR   A  1  160  ? -15.790 59.342  82.185  1.00 23.00 ? 158  THR   A CB    1 
ATOM   1021  O  OG1   . THR   A  1  160  ? -14.964 58.373  82.835  1.00 25.62 ? 158  THR   A OG1   1 
ATOM   1022  C  CG2   . THR   A  1  160  ? -16.521 60.181  83.219  1.00 29.85 ? 158  THR   A CG2   1 
ATOM   1023  N  N     . VAL   A  1  161  ? -15.385 58.456  79.347  1.00 17.16 ? 159  VAL   A N     1 
ATOM   1024  C  CA    . VAL   A  1  161  ? -14.841 57.871  78.133  1.00 17.58 ? 159  VAL   A CA    1 
ATOM   1025  C  C     . VAL   A  1  161  ? -13.325 57.917  78.238  1.00 16.07 ? 159  VAL   A C     1 
ATOM   1026  O  O     . VAL   A  1  161  ? -12.751 58.987  78.454  1.00 15.87 ? 159  VAL   A O     1 
ATOM   1027  C  CB    . VAL   A  1  161  ? -15.313 58.699  76.926  1.00 19.28 ? 159  VAL   A CB    1 
ATOM   1028  C  CG1   . VAL   A  1  161  ? -14.564 58.327  75.692  1.00 20.33 ? 159  VAL   A CG1   1 
ATOM   1029  C  CG2   . VAL   A  1  161  ? -16.842 58.553  76.748  1.00 22.60 ? 159  VAL   A CG2   1 
ATOM   1030  N  N     . ASN   A  1  162  ? -12.666 56.771  78.064  1.00 15.01 ? 160  ASN   A N     1 
ATOM   1031  C  CA    . ASN   A  1  162  ? -11.208 56.793  77.994  1.00 14.96 ? 160  ASN   A CA    1 
ATOM   1032  C  C     . ASN   A  1  162  ? -10.856 57.133  76.558  1.00 14.67 ? 160  ASN   A C     1 
ATOM   1033  O  O     . ASN   A  1  162  ? -10.674 56.254  75.707  1.00 14.78 ? 160  ASN   A O     1 
ATOM   1034  C  CB    . ASN   A  1  162  ? -10.601 55.477  78.446  1.00 14.39 ? 160  ASN   A CB    1 
ATOM   1035  C  CG    . ASN   A  1  162  ? -9.093  55.560  78.511  1.00 15.24 ? 160  ASN   A CG    1 
ATOM   1036  O  OD1   . ASN   A  1  162  ? -8.490  56.402  77.844  1.00 16.42 ? 160  ASN   A OD1   1 
ATOM   1037  N  ND2   . ASN   A  1  162  ? -8.479  54.700  79.309  1.00 20.07 ? 160  ASN   A ND2   1 
ATOM   1038  N  N     . ASP   A  1  163  ? -10.785 58.442  76.288  1.00 13.68 ? 161  ASP   A N     1 
ATOM   1039  C  CA    . ASP   A  1  163  ? -10.610 58.906  74.920  1.00 14.46 ? 161  ASP   A CA    1 
ATOM   1040  C  C     . ASP   A  1  163  ? -9.223  58.598  74.379  1.00 14.33 ? 161  ASP   A C     1 
ATOM   1041  O  O     . ASP   A  1  163  ? -9.058  58.442  73.174  1.00 14.70 ? 161  ASP   A O     1 
ATOM   1042  C  CB    . ASP   A  1  163  ? -10.967 60.392  74.770  1.00 16.44 ? 161  ASP   A CB    1 
ATOM   1043  C  CG    . ASP   A  1  163  ? -10.317 61.289  75.807  1.00 18.19 ? 161  ASP   A CG    1 
ATOM   1044  O  OD1   . ASP   A  1  163  ? -10.193 60.900  76.988  1.00 17.01 ? 161  ASP   A OD1   1 
ATOM   1045  O  OD2   . ASP   A  1  163  ? -9.980  62.432  75.426  1.00 20.36 ? 161  ASP   A OD2   1 
ATOM   1046  N  N     . ARG   A  1  164  ? -8.224  58.485  75.251  1.00 14.62 ? 162  ARG   A N     1 
ATOM   1047  C  CA    A ARG   A  1  164  ? -6.899  58.116  74.772  0.63 14.02 ? 162  ARG   A CA    1 
ATOM   1048  C  CA    B ARG   A  1  164  ? -6.893  58.113  74.787  0.37 14.09 ? 162  ARG   A CA    1 
ATOM   1049  C  C     . ARG   A  1  164  ? -6.840  56.647  74.376  1.00 13.46 ? 162  ARG   A C     1 
ATOM   1050  O  O     . ARG   A  1  164  ? -6.189  56.297  73.389  1.00 14.44 ? 162  ARG   A O     1 
ATOM   1051  C  CB    A ARG   A  1  164  ? -5.832  58.476  75.804  0.63 15.91 ? 162  ARG   A CB    1 
ATOM   1052  C  CB    B ARG   A  1  164  ? -5.862  58.428  75.868  0.37 15.91 ? 162  ARG   A CB    1 
ATOM   1053  C  CG    A ARG   A  1  164  ? -5.681  59.975  76.025  0.63 15.61 ? 162  ARG   A CG    1 
ATOM   1054  C  CG    B ARG   A  1  164  ? -5.852  59.891  76.274  0.37 16.38 ? 162  ARG   A CG    1 
ATOM   1055  C  CD    A ARG   A  1  164  ? -5.807  60.766  74.733  0.63 19.68 ? 162  ARG   A CD    1 
ATOM   1056  C  CD    B ARG   A  1  164  ? -4.867  60.717  75.456  0.37 18.93 ? 162  ARG   A CD    1 
ATOM   1057  N  NE    A ARG   A  1  164  ? -4.852  60.367  73.705  0.63 24.37 ? 162  ARG   A NE    1 
ATOM   1058  N  NE    B ARG   A  1  164  ? -5.103  60.657  74.019  0.37 22.33 ? 162  ARG   A NE    1 
ATOM   1059  C  CZ    A ARG   A  1  164  ? -4.960  60.698  72.424  0.63 24.27 ? 162  ARG   A CZ    1 
ATOM   1060  C  CZ    B ARG   A  1  164  ? -6.105  61.260  73.392  0.37 23.17 ? 162  ARG   A CZ    1 
ATOM   1061  N  NH1   A ARG   A  1  164  ? -5.960  61.446  71.987  0.63 26.19 ? 162  ARG   A NH1   1 
ATOM   1062  N  NH1   B ARG   A  1  164  ? -7.018  61.952  74.052  0.37 24.95 ? 162  ARG   A NH1   1 
ATOM   1063  N  NH2   A ARG   A  1  164  ? -4.046  60.266  71.560  0.63 23.20 ? 162  ARG   A NH2   1 
ATOM   1064  N  NH2   B ARG   A  1  164  ? -6.196  61.160  72.070  0.37 25.94 ? 162  ARG   A NH2   1 
ATOM   1065  N  N     . SER   A  1  165  ? -7.527  55.776  75.122  1.00 12.68 ? 163  SER   A N     1 
ATOM   1066  C  CA    . SER   A  1  165  ? -7.623  54.375  74.717  1.00 12.42 ? 163  SER   A CA    1 
ATOM   1067  C  C     . SER   A  1  165  ? -8.366  54.238  73.402  1.00 13.71 ? 163  SER   A C     1 
ATOM   1068  O  O     . SER   A  1  165  ? -7.981  53.449  72.536  1.00 13.16 ? 163  SER   A O     1 
ATOM   1069  C  CB    . SER   A  1  165  ? -8.340  53.578  75.810  1.00 14.38 ? 163  SER   A CB    1 
ATOM   1070  O  OG    . SER   A  1  165  ? -8.663  52.269  75.360  1.00 15.70 ? 163  SER   A OG    1 
ATOM   1071  N  N     . LEU   A  1  166  ? -9.473  54.973  73.258  1.00 13.35 ? 164  LEU   A N     1 
ATOM   1072  C  CA    . LEU   A  1  166  ? -10.233 54.921  72.021  1.00 13.85 ? 164  LEU   A CA    1 
ATOM   1073  C  C     . LEU   A  1  166  ? -9.433  55.473  70.854  1.00 13.30 ? 164  LEU   A C     1 
ATOM   1074  O  O     . LEU   A  1  166  ? -9.510  54.940  69.749  1.00 13.78 ? 164  LEU   A O     1 
ATOM   1075  C  CB    . LEU   A  1  166  ? -11.525 55.706  72.212  1.00 13.66 ? 164  LEU   A CB    1 
ATOM   1076  C  CG    . LEU   A  1  166  ? -12.484 54.989  73.146  1.00 13.10 ? 164  LEU   A CG    1 
ATOM   1077  C  CD1   . LEU   A  1  166  ? -13.646 55.885  73.439  1.00 15.39 ? 164  LEU   A CD1   1 
ATOM   1078  C  CD2   . LEU   A  1  166  ? -12.934 53.662  72.553  1.00 15.50 ? 164  LEU   A CD2   1 
ATOM   1079  N  N     . ALA   A  1  167  ? -8.684  56.558  71.070  1.00 13.27 ? 165  ALA   A N     1 
ATOM   1080  C  CA    . ALA   A  1  167  ? -7.886  57.100  69.976  1.00 14.77 ? 165  ALA   A CA    1 
ATOM   1081  C  C     . ALA   A  1  167  ? -6.828  56.099  69.541  1.00 14.24 ? 165  ALA   A C     1 
ATOM   1082  O  O     . ALA   A  1  167  ? -6.604  55.906  68.345  1.00 14.81 ? 165  ALA   A O     1 
ATOM   1083  C  CB    . ALA   A  1  167  ? -7.232  58.409  70.407  1.00 16.12 ? 165  ALA   A CB    1 
ATOM   1084  N  N     . ALA   A  1  168  ? -6.167  55.457  70.506  1.00 14.29 ? 166  ALA   A N     1 
ATOM   1085  C  CA    . ALA   A  1  168  ? -5.186  54.434  70.160  1.00 14.11 ? 166  ALA   A CA    1 
ATOM   1086  C  C     . ALA   A  1  168  ? -5.842  53.287  69.409  1.00 13.64 ? 166  ALA   A C     1 
ATOM   1087  O  O     . ALA   A  1  168  ? -5.299  52.780  68.419  1.00 15.40 ? 166  ALA   A O     1 
ATOM   1088  C  CB    . ALA   A  1  168  ? -4.532  53.939  71.453  1.00 14.23 ? 166  ALA   A CB    1 
ATOM   1089  N  N     . ALA   A  1  169  ? -7.026  52.882  69.863  1.00 14.06 ? 167  ALA   A N     1 
ATOM   1090  C  CA    . ALA   A  1  169  ? -7.714  51.767  69.238  1.00 13.35 ? 167  ALA   A CA    1 
ATOM   1091  C  C     . ALA   A  1  169  ? -8.142  52.112  67.821  1.00 14.58 ? 167  ALA   A C     1 
ATOM   1092  O  O     . ALA   A  1  169  ? -8.089  51.263  66.932  1.00 14.75 ? 167  ALA   A O     1 
ATOM   1093  C  CB    . ALA   A  1  169  ? -8.935  51.392  70.078  1.00 14.10 ? 167  ALA   A CB    1 
ATOM   1094  N  N     . LEU   A  1  170  ? -8.594  53.346  67.607  1.00 13.64 ? 168  LEU   A N     1 
ATOM   1095  C  CA    . LEU   A  1  170  ? -9.005  53.752  66.271  1.00 14.21 ? 168  LEU   A CA    1 
ATOM   1096  C  C     . LEU   A  1  170  ? -7.815  53.781  65.323  1.00 15.02 ? 168  LEU   A C     1 
ATOM   1097  O  O     . LEU   A  1  170  ? -7.886  53.273  64.199  1.00 15.09 ? 168  LEU   A O     1 
ATOM   1098  C  CB    . LEU   A  1  170  ? -9.657  55.126  66.359  1.00 16.36 ? 168  LEU   A CB    1 
ATOM   1099  C  CG    . LEU   A  1  170  ? -10.284 55.562  65.044  1.00 15.80 ? 168  LEU   A CG    1 
ATOM   1100  C  CD1   . LEU   A  1  170  ? -11.270 54.512  64.553  1.00 17.13 ? 168  LEU   A CD1   1 
ATOM   1101  C  CD2   . LEU   A  1  170  ? -10.967 56.882  65.264  1.00 17.39 ? 168  LEU   A CD2   1 
ATOM   1102  N  N     . THR   A  1  171  ? -6.703  54.372  65.760  1.00 15.37 ? 169  THR   A N     1 
ATOM   1103  C  CA    . THR   A  1  171  ? -5.503  54.348  64.938  1.00 16.62 ? 169  THR   A CA    1 
ATOM   1104  C  C     . THR   A  1  171  ? -5.112  52.918  64.619  1.00 15.26 ? 169  THR   A C     1 
ATOM   1105  O  O     . THR   A  1  171  ? -4.808  52.584  63.469  1.00 15.98 ? 169  THR   A O     1 
ATOM   1106  C  CB    . THR   A  1  171  ? -4.374  55.043  65.685  1.00 17.43 ? 169  THR   A CB    1 
ATOM   1107  O  OG1   . THR   A  1  171  ? -4.749  56.403  65.950  1.00 20.03 ? 169  THR   A OG1   1 
ATOM   1108  C  CG2   . THR   A  1  171  ? -3.058  54.998  64.896  1.00 19.07 ? 169  THR   A CG2   1 
ATOM   1109  N  N     . ARG   A  1  172  ? -5.151  52.051  65.632  1.00 15.02 ? 170  ARG   A N     1 
ATOM   1110  C  CA    . ARG   A  1  172  ? -4.729  50.672  65.434  1.00 14.25 ? 170  ARG   A CA    1 
ATOM   1111  C  C     . ARG   A  1  172  ? -5.620  49.968  64.428  1.00 15.51 ? 170  ARG   A C     1 
ATOM   1112  O  O     . ARG   A  1  172  ? -5.139  49.288  63.513  1.00 16.34 ? 170  ARG   A O     1 
ATOM   1113  C  CB    . ARG   A  1  172  ? -4.757  49.932  66.773  1.00 15.53 ? 170  ARG   A CB    1 
ATOM   1114  C  CG    . ARG   A  1  172  ? -4.011  48.611  66.721  1.00 14.19 ? 170  ARG   A CG    1 
ATOM   1115  C  CD    . ARG   A  1  172  ? -4.175  47.794  67.986  1.00 15.71 ? 170  ARG   A CD    1 
ATOM   1116  N  NE    . ARG   A  1  172  ? -3.936  48.581  69.186  1.00 14.36 ? 170  ARG   A NE    1 
ATOM   1117  C  CZ    . ARG   A  1  172  ? -4.885  49.036  69.996  1.00 13.81 ? 170  ARG   A CZ    1 
ATOM   1118  N  NH1   . ARG   A  1  172  ? -6.165  48.782  69.782  1.00 15.10 ? 170  ARG   A NH1   1 
ATOM   1119  N  NH2   . ARG   A  1  172  ? -4.539  49.764  71.049  1.00 14.93 ? 170  ARG   A NH2   1 
ATOM   1120  N  N     . LEU   A  1  173  ? -6.933  50.120  64.571  1.00 15.42 ? 171  LEU   A N     1 
ATOM   1121  C  CA    . LEU   A  1  173  ? -7.814  49.353  63.706  1.00 15.98 ? 171  LEU   A CA    1 
ATOM   1122  C  C     . LEU   A  1  173  ? -7.769  49.878  62.285  1.00 16.92 ? 171  LEU   A C     1 
ATOM   1123  O  O     . LEU   A  1  173  ? -7.858  49.102  61.332  1.00 16.87 ? 171  LEU   A O     1 
ATOM   1124  C  CB    . LEU   A  1  173  ? -9.241  49.340  64.260  1.00 17.38 ? 171  LEU   A CB    1 
ATOM   1125  C  CG    . LEU   A  1  173  ? -10.136 50.574  64.162  1.00 17.59 ? 171  LEU   A CG    1 
ATOM   1126  C  CD1   . LEU   A  1  173  ? -10.909 50.615  62.834  1.00 19.08 ? 171  LEU   A CD1   1 
ATOM   1127  C  CD2   . LEU   A  1  173  ? -11.111 50.603  65.322  1.00 16.95 ? 171  LEU   A CD2   1 
ATOM   1128  N  N     . ILE   A  1  174  ? -7.636  51.196  62.121  1.00 16.34 ? 172  ILE   A N     1 
ATOM   1129  C  CA    . ILE   A  1  174  ? -7.561  51.738  60.768  1.00 16.41 ? 172  ILE   A CA    1 
ATOM   1130  C  C     . ILE   A  1  174  ? -6.255  51.321  60.115  1.00 17.41 ? 172  ILE   A C     1 
ATOM   1131  O  O     . ILE   A  1  174  ? -6.227  50.926  58.948  1.00 17.76 ? 172  ILE   A O     1 
ATOM   1132  C  CB    . ILE   A  1  174  ? -7.725  53.268  60.792  1.00 16.57 ? 172  ILE   A CB    1 
ATOM   1133  C  CG1   . ILE   A  1  174  ? -9.156  53.646  61.170  1.00 17.88 ? 172  ILE   A CG1   1 
ATOM   1134  C  CG2   . ILE   A  1  174  ? -7.317  53.874  59.432  1.00 20.79 ? 172  ILE   A CG2   1 
ATOM   1135  C  CD1   . ILE   A  1  174  ? -9.334  55.121  61.447  1.00 20.87 ? 172  ILE   A CD1   1 
ATOM   1136  N  N     . SER   A  1  175  ? -5.157  51.378  60.863  1.00 18.21 ? 173  SER   A N     1 
ATOM   1137  C  CA    . SER   A  1  175  ? -3.878  51.000  60.274  1.00 16.86 ? 173  SER   A CA    1 
ATOM   1138  C  C     . SER   A  1  175  ? -3.836  49.519  59.958  1.00 19.01 ? 173  SER   A C     1 
ATOM   1139  O  O     . SER   A  1  175  ? -3.114  49.098  59.049  1.00 21.42 ? 173  SER   A O     1 
ATOM   1140  C  CB    . SER   A  1  175  ? -2.744  51.362  61.224  1.00 20.41 ? 173  SER   A CB    1 
ATOM   1141  O  OG    . SER   A  1  175  ? -2.600  52.763  61.327  1.00 25.16 ? 173  SER   A OG    1 
ATOM   1142  N  N     . ARG   A  1  176  ? -4.608  48.719  60.682  1.00 17.36 ? 174  ARG   A N     1 
ATOM   1143  C  CA    . ARG   A  1  176  ? -4.598  47.285  60.456  1.00 18.38 ? 174  ARG   A CA    1 
ATOM   1144  C  C     . ARG   A  1  176  ? -5.550  46.877  59.344  1.00 21.18 ? 174  ARG   A C     1 
ATOM   1145  O  O     . ARG   A  1  176  ? -5.208  46.025  58.521  1.00 23.15 ? 174  ARG   A O     1 
ATOM   1146  C  CB    . ARG   A  1  176  ? -4.977  46.581  61.765  1.00 19.35 ? 174  ARG   A CB    1 
ATOM   1147  C  CG    . ARG   A  1  176  ? -4.823  45.072  61.717  1.00 20.69 ? 174  ARG   A CG    1 
ATOM   1148  C  CD    . ARG   A  1  176  ? -5.079  44.478  63.103  1.00 20.78 ? 174  ARG   A CD    1 
ATOM   1149  N  NE    . ARG   A  1  176  ? -6.496  44.507  63.453  1.00 20.80 ? 174  ARG   A NE    1 
ATOM   1150  C  CZ    . ARG   A  1  176  ? -7.052  45.198  64.451  1.00 20.78 ? 174  ARG   A CZ    1 
ATOM   1151  N  NH1   . ARG   A  1  176  ? -6.328  45.916  65.310  1.00 18.21 ? 174  ARG   A NH1   1 
ATOM   1152  N  NH2   . ARG   A  1  176  ? -8.376  45.158  64.601  1.00 24.03 ? 174  ARG   A NH2   1 
ATOM   1153  N  N     . CYS   A  1  177  ? -6.736  47.490  59.291  1.00 19.56 ? 175  CYS   A N     1 
ATOM   1154  C  CA    . CYS   A  1  177  ? -7.802  47.024  58.423  1.00 21.15 ? 175  CYS   A CA    1 
ATOM   1155  C  C     . CYS   A  1  177  ? -8.247  48.021  57.366  1.00 21.42 ? 175  CYS   A C     1 
ATOM   1156  O  O     . CYS   A  1  177  ? -8.954  47.620  56.439  1.00 24.87 ? 175  CYS   A O     1 
ATOM   1157  C  CB    . CYS   A  1  177  ? -9.033  46.618  59.245  1.00 22.25 ? 175  CYS   A CB    1 
ATOM   1158  S  SG    . CYS   A  1  177  ? -8.670  45.425  60.563  1.00 25.76 ? 175  CYS   A SG    1 
ATOM   1159  N  N     . GLY   A  1  178  ? -7.899  49.293  57.495  1.00 23.13 ? 176  GLY   A N     1 
ATOM   1160  C  CA    . GLY   A  1  178  ? -8.098  50.225  56.402  1.00 21.92 ? 176  GLY   A CA    1 
ATOM   1161  C  C     . GLY   A  1  178  ? -9.548  50.569  56.090  1.00 20.58 ? 176  GLY   A C     1 
ATOM   1162  O  O     . GLY   A  1  178  ? -10.471 50.437  56.906  1.00 21.03 ? 176  GLY   A O     1 
ATOM   1163  N  N     . GLU   A  1  179  ? -9.729  51.025  54.855  1.00 21.94 ? 177  GLU   A N     1 
ATOM   1164  C  CA    . GLU   A  1  179  ? -11.046 51.452  54.395  1.00 21.80 ? 177  GLU   A CA    1 
ATOM   1165  C  C     . GLU   A  1  179  ? -12.139 50.411  54.592  1.00 19.76 ? 177  GLU   A C     1 
ATOM   1166  O  O     . GLU   A  1  179  ? -13.254 50.798  54.983  1.00 22.55 ? 177  GLU   A O     1 
ATOM   1167  C  CB    . GLU   A  1  179  ? -10.960 51.902  52.927  1.00 22.99 ? 177  GLU   A CB    1 
ATOM   1168  C  CG    . GLU   A  1  179  ? -12.245 52.533  52.412  1.00 30.70 ? 177  GLU   A CG    1 
ATOM   1169  C  CD    . GLU   A  1  179  ? -13.181 51.528  51.756  1.00 40.83 ? 177  GLU   A CD    1 
ATOM   1170  O  OE1   . GLU   A  1  179  ? -12.702 50.462  51.307  1.00 44.51 ? 177  GLU   A OE1   1 
ATOM   1171  O  OE2   . GLU   A  1  179  ? -14.401 51.806  51.687  1.00 46.30 ? 177  GLU   A OE2   1 
ATOM   1172  N  N     . PRO   A  1  180  ? -11.920 49.116  54.340  1.00 20.59 ? 178  PRO   A N     1 
ATOM   1173  C  CA    . PRO   A  1  180  ? -13.034 48.167  54.482  1.00 21.86 ? 178  PRO   A CA    1 
ATOM   1174  C  C     . PRO   A  1  180  ? -13.684 48.183  55.851  1.00 20.46 ? 178  PRO   A C     1 
ATOM   1175  O  O     . PRO   A  1  180  ? -14.915 48.105  55.944  1.00 21.72 ? 178  PRO   A O     1 
ATOM   1176  C  CB    . PRO   A  1  180  ? -12.386 46.819  54.151  1.00 25.23 ? 178  PRO   A CB    1 
ATOM   1177  C  CG    . PRO   A  1  180  ? -11.290 47.171  53.211  1.00 24.83 ? 178  PRO   A CG    1 
ATOM   1178  C  CD    . PRO   A  1  180  ? -10.750 48.478  53.706  1.00 21.38 ? 178  PRO   A CD    1 
ATOM   1179  N  N     . VAL   A  1  181  ? -12.904 48.312  56.926  1.00 19.97 ? 179  VAL   A N     1 
ATOM   1180  C  CA    . VAL   A  1  181  ? -13.528 48.330  58.244  1.00 20.06 ? 179  VAL   A CA    1 
ATOM   1181  C  C     . VAL   A  1  181  ? -14.267 49.640  58.484  1.00 18.75 ? 179  VAL   A C     1 
ATOM   1182  O  O     . VAL   A  1  181  ? -15.309 49.656  59.144  1.00 18.20 ? 179  VAL   A O     1 
ATOM   1183  C  CB    . VAL   A  1  181  ? -12.513 48.002  59.359  1.00 19.43 ? 179  VAL   A CB    1 
ATOM   1184  C  CG1   . VAL   A  1  181  ? -11.512 49.136  59.550  1.00 19.46 ? 179  VAL   A CG1   1 
ATOM   1185  C  CG2   . VAL   A  1  181  ? -13.248 47.698  60.659  1.00 23.60 ? 179  VAL   A CG2   1 
ATOM   1186  N  N     . ILE   A  1  182  ? -13.751 50.754  57.964  1.00 19.84 ? 180  ILE   A N     1 
ATOM   1187  C  CA    . ILE   A  1  182  ? -14.444 52.029  58.117  1.00 19.56 ? 180  ILE   A CA    1 
ATOM   1188  C  C     . ILE   A  1  182  ? -15.778 51.983  57.396  1.00 23.09 ? 180  ILE   A C     1 
ATOM   1189  O  O     . ILE   A  1  182  ? -16.811 52.395  57.933  1.00 20.30 ? 180  ILE   A O     1 
ATOM   1190  C  CB    . ILE   A  1  182  ? -13.575 53.183  57.601  1.00 19.89 ? 180  ILE   A CB    1 
ATOM   1191  C  CG1   . ILE   A  1  182  ? -12.241 53.201  58.334  1.00 20.25 ? 180  ILE   A CG1   1 
ATOM   1192  C  CG2   . ILE   A  1  182  ? -14.316 54.504  57.758  1.00 20.54 ? 180  ILE   A CG2   1 
ATOM   1193  C  CD1   . ILE   A  1  182  ? -11.214 54.107  57.692  1.00 24.01 ? 180  ILE   A CD1   1 
ATOM   1194  N  N     . ARG   A  1  183  ? -15.758 51.491  56.160  1.00 21.18 ? 181  ARG   A N     1 
ATOM   1195  C  CA    A ARG   A  1  183  ? -16.988 51.351  55.389  0.34 23.93 ? 181  ARG   A CA    1 
ATOM   1196  C  CA    B ARG   A  1  183  ? -16.979 51.329  55.376  0.66 23.89 ? 181  ARG   A CA    1 
ATOM   1197  C  C     . ARG   A  1  183  ? -18.017 50.516  56.140  1.00 23.97 ? 181  ARG   A C     1 
ATOM   1198  O  O     . ARG   A  1  183  ? -19.200 50.887  56.216  1.00 22.91 ? 181  ARG   A O     1 
ATOM   1199  C  CB    A ARG   A  1  183  ? -16.667 50.738  54.023  0.34 25.14 ? 181  ARG   A CB    1 
ATOM   1200  C  CB    B ARG   A  1  183  ? -16.613 50.628  54.065  0.66 24.95 ? 181  ARG   A CB    1 
ATOM   1201  C  CG    A ARG   A  1  183  ? -17.881 50.337  53.189  0.34 30.37 ? 181  ARG   A CG    1 
ATOM   1202  C  CG    B ARG   A  1  183  ? -17.761 50.391  53.094  0.66 30.57 ? 181  ARG   A CG    1 
ATOM   1203  C  CD    A ARG   A  1  183  ? -18.890 51.471  53.069  0.34 29.93 ? 181  ARG   A CD    1 
ATOM   1204  C  CD    B ARG   A  1  183  ? -18.173 51.684  52.413  0.66 33.13 ? 181  ARG   A CD    1 
ATOM   1205  N  NE    A ARG   A  1  183  ? -18.272 52.732  52.677  0.34 30.61 ? 181  ARG   A NE    1 
ATOM   1206  N  NE    B ARG   A  1  183  ? -19.194 52.398  53.168  0.66 29.08 ? 181  ARG   A NE    1 
ATOM   1207  C  CZ    A ARG   A  1  183  ? -18.843 53.918  52.833  0.34 32.48 ? 181  ARG   A CZ    1 
ATOM   1208  C  CZ    B ARG   A  1  183  ? -19.382 53.709  53.116  0.66 32.52 ? 181  ARG   A CZ    1 
ATOM   1209  N  NH1   A ARG   A  1  183  ? -20.039 54.040  53.386  0.34 31.49 ? 181  ARG   A NH1   1 
ATOM   1210  N  NH1   B ARG   A  1  183  ? -18.590 54.491  52.399  0.66 33.59 ? 181  ARG   A NH1   1 
ATOM   1211  N  NH2   A ARG   A  1  183  ? -18.197 55.008  52.430  0.34 33.78 ? 181  ARG   A NH2   1 
ATOM   1212  N  NH2   B ARG   A  1  183  ? -20.384 54.248  53.802  0.66 31.26 ? 181  ARG   A NH2   1 
ATOM   1213  N  N     . ARG   A  1  184  ? -17.590 49.388  56.708  1.00 21.92 ? 182  ARG   A N     1 
ATOM   1214  C  CA    . ARG   A  1  184  ? -18.527 48.528  57.415  1.00 22.03 ? 182  ARG   A CA    1 
ATOM   1215  C  C     . ARG   A  1  184  ? -19.060 49.218  58.657  1.00 23.23 ? 182  ARG   A C     1 
ATOM   1216  O  O     . ARG   A  1  184  ? -20.251 49.116  58.973  1.00 23.45 ? 182  ARG   A O     1 
ATOM   1217  C  CB    . ARG   A  1  184  ? -17.856 47.206  57.770  1.00 22.60 ? 182  ARG   A CB    1 
ATOM   1218  C  CG    . ARG   A  1  184  ? -17.746 46.258  56.589  1.00 28.95 ? 182  ARG   A CG    1 
ATOM   1219  C  CD    . ARG   A  1  184  ? -18.948 45.316  56.514  1.00 28.21 ? 182  ARG   A CD    1 
ATOM   1220  N  NE    . ARG   A  1  184  ? -18.806 44.186  57.426  1.00 35.01 ? 182  ARG   A NE    1 
ATOM   1221  C  CZ    . ARG   A  1  184  ? -19.639 43.896  58.416  1.00 33.71 ? 182  ARG   A CZ    1 
ATOM   1222  N  NH1   . ARG   A  1  184  ? -20.727 44.614  58.641  1.00 32.55 ? 182  ARG   A NH1   1 
ATOM   1223  N  NH2   . ARG   A  1  184  ? -19.381 42.847  59.193  1.00 28.55 ? 182  ARG   A NH2   1 
ATOM   1224  N  N     . GLY   A  1  185  ? -18.191 49.933  59.370  1.00 20.76 ? 183  GLY   A N     1 
ATOM   1225  C  CA    . GLY   A  1  185  ? -18.643 50.669  60.536  1.00 20.40 ? 183  GLY   A CA    1 
ATOM   1226  C  C     . GLY   A  1  185  ? -19.640 51.753  60.179  1.00 20.34 ? 183  GLY   A C     1 
ATOM   1227  O  O     . GLY   A  1  185  ? -20.659 51.914  60.854  1.00 19.72 ? 183  GLY   A O     1 
ATOM   1228  N  N     . VAL   A  1  186  ? -19.362 52.506  59.110  1.00 20.03 ? 184  VAL   A N     1 
ATOM   1229  C  CA    . VAL   A  1  186  ? -20.276 53.567  58.686  1.00 22.37 ? 184  VAL   A CA    1 
ATOM   1230  C  C     . VAL   A  1  186  ? -21.638 52.989  58.327  1.00 22.48 ? 184  VAL   A C     1 
ATOM   1231  O  O     . VAL   A  1  186  ? -22.684 53.509  58.738  1.00 21.76 ? 184  VAL   A O     1 
ATOM   1232  C  CB    . VAL   A  1  186  ? -19.672 54.367  57.519  1.00 22.88 ? 184  VAL   A CB    1 
ATOM   1233  C  CG1   . VAL   A  1  186  ? -20.761 55.232  56.841  1.00 23.54 ? 184  VAL   A CG1   1 
ATOM   1234  C  CG2   . VAL   A  1  186  ? -18.547 55.235  58.019  1.00 22.78 ? 184  VAL   A CG2   1 
ATOM   1235  N  N     . ASP   A  1  187  ? -21.646 51.901  57.562  1.00 20.56 ? 185  ASP   A N     1 
ATOM   1236  C  CA    . ASP   A  1  187  ? -22.916 51.307  57.157  1.00 24.21 ? 185  ASP   A CA    1 
ATOM   1237  C  C     . ASP   A  1  187  ? -23.672 50.774  58.365  1.00 25.89 ? 185  ASP   A C     1 
ATOM   1238  O  O     . ASP   A  1  187  ? -24.899 50.900  58.441  1.00 25.13 ? 185  ASP   A O     1 
ATOM   1239  C  CB    . ASP   A  1  187  ? -22.681 50.204  56.132  1.00 23.94 ? 185  ASP   A CB    1 
ATOM   1240  C  CG    . ASP   A  1  187  ? -22.175 50.739  54.802  1.00 28.23 ? 185  ASP   A CG    1 
ATOM   1241  O  OD1   . ASP   A  1  187  ? -22.272 51.966  54.567  1.00 32.88 ? 185  ASP   A OD1   1 
ATOM   1242  O  OD2   . ASP   A  1  187  ? -21.671 49.936  53.998  1.00 31.18 ? 185  ASP   A OD2   1 
ATOM   1243  N  N     . MET   A  1  188  ? -22.954 50.193  59.327  1.00 23.00 ? 186  MET   A N     1 
ATOM   1244  C  CA    . MET   A  1  188  ? -23.596 49.693  60.537  1.00 25.10 ? 186  MET   A CA    1 
ATOM   1245  C  C     . MET   A  1  188  ? -24.186 50.831  61.353  1.00 24.80 ? 186  MET   A C     1 
ATOM   1246  O  O     . MET   A  1  188  ? -25.343 50.765  61.786  1.00 22.68 ? 186  MET   A O     1 
ATOM   1247  C  CB    . MET   A  1  188  ? -22.577 48.923  61.375  1.00 26.98 ? 186  MET   A CB    1 
ATOM   1248  C  CG    . MET   A  1  188  ? -23.151 48.321  62.638  1.00 31.37 ? 186  MET   A CG    1 
ATOM   1249  S  SD    . MET   A  1  188  ? -24.314 47.017  62.221  1.00 39.52 ? 186  MET   A SD    1 
ATOM   1250  C  CE    . MET   A  1  188  ? -23.263 46.003  61.172  1.00 30.67 ? 186  MET   A CE    1 
ATOM   1251  N  N     . ALA   A  1  189  ? -23.400 51.881  61.593  1.00 22.10 ? 187  ALA   A N     1 
ATOM   1252  C  CA    . ALA   A  1  189  ? -23.900 53.013  62.360  1.00 22.86 ? 187  ALA   A CA    1 
ATOM   1253  C  C     . ALA   A  1  189  ? -25.073 53.670  61.655  1.00 22.74 ? 187  ALA   A C     1 
ATOM   1254  O  O     . ALA   A  1  189  ? -26.040 54.086  62.302  1.00 21.56 ? 187  ALA   A O     1 
ATOM   1255  C  CB    . ALA   A  1  189  ? -22.787 54.030  62.595  1.00 23.87 ? 187  ALA   A CB    1 
ATOM   1256  N  N     . MET   A  1  190  ? -25.012 53.759  60.328  1.00 21.45 ? 188  MET   A N     1 
ATOM   1257  C  CA    . MET   A  1  190  ? -26.110 54.364  59.583  1.00 22.88 ? 188  MET   A CA    1 
ATOM   1258  C  C     . MET   A  1  190  ? -27.392 53.571  59.777  1.00 22.05 ? 188  MET   A C     1 
ATOM   1259  O  O     . MET   A  1  190  ? -28.462 54.148  60.017  1.00 25.10 ? 188  MET   A O     1 
ATOM   1260  C  CB    . MET   A  1  190  ? -25.750 54.422  58.103  1.00 24.62 ? 188  MET   A CB    1 
ATOM   1261  C  CG    . MET   A  1  190  ? -26.720 55.229  57.267  1.00 31.19 ? 188  MET   A CG    1 
ATOM   1262  S  SD    . MET   A  1  190  ? -26.324 55.123  55.510  1.00 36.66 ? 188  MET   A SD    1 
ATOM   1263  C  CE    . MET   A  1  190  ? -24.577 55.509  55.532  1.00 34.45 ? 188  MET   A CE    1 
ATOM   1264  N  N     . ARG   A  1  191  ? -27.299 52.247  59.684  1.00 21.66 ? 189  ARG   A N     1 
ATOM   1265  C  CA    . ARG   A  1  191  ? -28.465 51.401  59.902  1.00 25.85 ? 189  ARG   A CA    1 
ATOM   1266  C  C     . ARG   A  1  191  ? -28.976 51.535  61.327  1.00 24.06 ? 189  ARG   A C     1 
ATOM   1267  O  O     . ARG   A  1  191  ? -30.181 51.689  61.557  1.00 23.69 ? 189  ARG   A O     1 
ATOM   1268  C  CB    . ARG   A  1  191  ? -28.108 49.945  59.609  1.00 24.87 ? 189  ARG   A CB    1 
ATOM   1269  N  N     . MET   A  1  192  ? -28.075 51.476  62.307  1.00 19.57 ? 190  MET   A N     1 
ATOM   1270  C  CA    . MET   A  1  192  ? -28.525 51.495  63.693  1.00 21.84 ? 190  MET   A CA    1 
ATOM   1271  C  C     . MET   A  1  192  ? -29.159 52.827  64.042  1.00 24.54 ? 190  MET   A C     1 
ATOM   1272  O  O     . MET   A  1  192  ? -30.234 52.873  64.642  1.00 22.64 ? 190  MET   A O     1 
ATOM   1273  C  CB    . MET   A  1  192  ? -27.364 51.189  64.634  1.00 25.29 ? 190  MET   A CB    1 
ATOM   1274  C  CG    . MET   A  1  192  ? -26.841 49.787  64.484  1.00 22.34 ? 190  MET   A CG    1 
ATOM   1275  S  SD    . MET   A  1  192  ? -25.532 49.487  65.671  1.00 33.09 ? 190  MET   A SD    1 
ATOM   1276  C  CE    . MET   A  1  192  ? -26.514 49.240  67.143  1.00 33.34 ? 190  MET   A CE    1 
ATOM   1277  N  N     . MET   A  1  193  ? -28.523 53.926  63.658  1.00 22.38 ? 191  MET   A N     1 
ATOM   1278  C  CA    A MET   A  1  193  ? -29.023 55.244  64.026  0.53 23.83 ? 191  MET   A CA    1 
ATOM   1279  C  CA    B MET   A  1  193  ? -29.043 55.228  64.042  0.47 23.84 ? 191  MET   A CA    1 
ATOM   1280  C  C     . MET   A  1  193  ? -30.207 55.685  63.176  1.00 23.33 ? 191  MET   A C     1 
ATOM   1281  O  O     . MET   A  1  193  ? -30.961 56.561  63.604  1.00 26.09 ? 191  MET   A O     1 
ATOM   1282  C  CB    A MET   A  1  193  ? -27.901 56.279  63.927  0.53 25.18 ? 191  MET   A CB    1 
ATOM   1283  C  CB    B MET   A  1  193  ? -27.929 56.266  64.040  0.47 25.21 ? 191  MET   A CB    1 
ATOM   1284  C  CG    A MET   A  1  193  ? -26.639 55.889  64.690  0.53 22.50 ? 191  MET   A CG    1 
ATOM   1285  C  CG    B MET   A  1  193  ? -26.929 56.039  65.155  0.47 22.33 ? 191  MET   A CG    1 
ATOM   1286  S  SD    A MET   A  1  193  ? -25.303 57.081  64.482  0.53 25.53 ? 191  MET   A SD    1 
ATOM   1287  S  SD    B MET   A  1  193  ? -25.901 57.481  65.416  0.47 25.28 ? 191  MET   A SD    1 
ATOM   1288  C  CE    A MET   A  1  193  ? -25.747 58.279  65.735  0.53 30.35 ? 191  MET   A CE    1 
ATOM   1289  C  CE    B MET   A  1  193  ? -24.852 57.409  63.964  0.47 26.61 ? 191  MET   A CE    1 
ATOM   1290  N  N     . GLY   A  1  194  ? -30.386 55.106  61.993  1.00 24.34 ? 192  GLY   A N     1 
ATOM   1291  C  CA    . GLY   A  1  194  ? -31.458 55.539  61.122  1.00 25.51 ? 192  GLY   A CA    1 
ATOM   1292  C  C     . GLY   A  1  194  ? -32.660 54.621  61.126  1.00 26.69 ? 192  GLY   A C     1 
ATOM   1293  O  O     . GLY   A  1  194  ? -33.768 55.044  60.774  1.00 27.71 ? 192  GLY   A O     1 
ATOM   1294  N  N     . GLU   A  1  195  ? -32.457 53.362  61.521  1.00 21.88 ? 193  GLU   A N     1 
ATOM   1295  C  CA    . GLU   A  1  195  ? -33.493 52.344  61.401  1.00 21.78 ? 193  GLU   A CA    1 
ATOM   1296  C  C     . GLU   A  1  195  ? -33.727 51.514  62.647  1.00 21.63 ? 193  GLU   A C     1 
ATOM   1297  O  O     . GLU   A  1  195  ? -34.781 50.879  62.731  1.00 21.03 ? 193  GLU   A O     1 
ATOM   1298  C  CB    . GLU   A  1  195  ? -33.177 51.372  60.257  1.00 25.99 ? 193  GLU   A CB    1 
ATOM   1299  C  CG    . GLU   A  1  195  ? -32.859 52.026  58.939  1.00 35.32 ? 193  GLU   A CG    1 
ATOM   1300  C  CD    . GLU   A  1  195  ? -32.343 51.022  57.931  1.00 42.42 ? 193  GLU   A CD    1 
ATOM   1301  O  OE1   . GLU   A  1  195  ? -32.767 49.848  58.000  1.00 47.35 ? 193  GLU   A OE1   1 
ATOM   1302  O  OE2   . GLU   A  1  195  ? -31.500 51.399  57.090  1.00 50.28 ? 193  GLU   A OE2   1 
ATOM   1303  N  N     . GLN   A  1  196  ? -32.794 51.468  63.599  1.00 23.06 ? 194  GLN   A N     1 
ATOM   1304  C  CA    . GLN   A  1  196  ? -32.959 50.638  64.788  1.00 24.06 ? 194  GLN   A CA    1 
ATOM   1305  C  C     . GLN   A  1  196  ? -33.271 51.457  66.034  1.00 25.20 ? 194  GLN   A C     1 
ATOM   1306  O  O     . GLN   A  1  196  ? -34.272 51.207  66.713  1.00 25.57 ? 194  GLN   A O     1 
ATOM   1307  C  CB    . GLN   A  1  196  ? -31.704 49.783  65.023  1.00 25.74 ? 194  GLN   A CB    1 
ATOM   1308  N  N     . PHE   A  1  197  ? -32.428 52.437  66.349  1.00 21.54 ? 195  PHE   A N     1 
ATOM   1309  C  CA    . PHE   A  1  197  ? -32.669 53.279  67.511  1.00 23.14 ? 195  PHE   A CA    1 
ATOM   1310  C  C     . PHE   A  1  197  ? -33.855 54.193  67.283  1.00 25.25 ? 195  PHE   A C     1 
ATOM   1311  O  O     . PHE   A  1  197  ? -34.463 54.667  68.247  1.00 24.07 ? 195  PHE   A O     1 
ATOM   1312  C  CB    . PHE   A  1  197  ? -31.439 54.130  67.806  1.00 25.02 ? 195  PHE   A CB    1 
ATOM   1313  C  CG    . PHE   A  1  197  ? -30.226 53.331  68.167  1.00 27.17 ? 195  PHE   A CG    1 
ATOM   1314  C  CD1   . PHE   A  1  197  ? -30.339 52.164  68.899  1.00 30.42 ? 195  PHE   A CD1   1 
ATOM   1315  C  CD2   . PHE   A  1  197  ? -28.969 53.759  67.782  1.00 28.63 ? 195  PHE   A CD2   1 
ATOM   1316  C  CE1   . PHE   A  1  197  ? -29.216 51.435  69.240  1.00 32.02 ? 195  PHE   A CE1   1 
ATOM   1317  C  CE2   . PHE   A  1  197  ? -27.845 53.029  68.118  1.00 30.75 ? 195  PHE   A CE2   1 
ATOM   1318  C  CZ    . PHE   A  1  197  ? -27.977 51.868  68.849  1.00 28.05 ? 195  PHE   A CZ    1 
ATOM   1319  N  N     . VAL   A  1  198  ? -34.164 54.478  66.022  1.00 20.85 ? 196  VAL   A N     1 
ATOM   1320  C  CA    . VAL   A  1  198  ? -35.350 55.231  65.651  1.00 20.11 ? 196  VAL   A CA    1 
ATOM   1321  C  C     . VAL   A  1  198  ? -36.032 54.487  64.522  1.00 19.22 ? 196  VAL   A C     1 
ATOM   1322  O  O     . VAL   A  1  198  ? -35.398 53.756  63.755  1.00 23.06 ? 196  VAL   A O     1 
ATOM   1323  C  CB    . VAL   A  1  198  ? -35.044 56.688  65.218  1.00 20.34 ? 196  VAL   A CB    1 
ATOM   1324  C  CG1   . VAL   A  1  198  ? -34.433 57.484  66.370  1.00 22.53 ? 196  VAL   A CG1   1 
ATOM   1325  C  CG2   . VAL   A  1  198  ? -34.139 56.705  63.994  1.00 22.17 ? 196  VAL   A CG2   1 
ATOM   1326  N  N     . THR   A  1  199  ? -37.347 54.661  64.439  1.00 19.15 ? 197  THR   A N     1 
ATOM   1327  C  CA    . THR   A  1  199  ? -38.069 54.143  63.290  1.00 19.84 ? 197  THR   A CA    1 
ATOM   1328  C  C     . THR   A  1  199  ? -37.753 54.958  62.050  1.00 22.93 ? 197  THR   A C     1 
ATOM   1329  O  O     . THR   A  1  199  ? -37.697 54.411  60.946  1.00 26.55 ? 197  THR   A O     1 
ATOM   1330  C  CB    . THR   A  1  199  ? -39.566 54.141  63.598  1.00 21.76 ? 197  THR   A CB    1 
ATOM   1331  O  OG1   . THR   A  1  199  ? -39.772 53.392  64.805  1.00 23.72 ? 197  THR   A OG1   1 
ATOM   1332  C  CG2   . THR   A  1  199  ? -40.342 53.490  62.480  1.00 25.73 ? 197  THR   A CG2   1 
ATOM   1333  N  N     . GLY   A  1  200  ? -37.526 56.251  62.216  1.00 20.93 ? 198  GLY   A N     1 
ATOM   1334  C  CA    . GLY   A  1  200  ? -37.099 57.085  61.110  1.00 22.15 ? 198  GLY   A CA    1 
ATOM   1335  C  C     . GLY   A  1  200  ? -36.557 58.383  61.654  1.00 20.85 ? 198  GLY   A C     1 
ATOM   1336  O  O     . GLY   A  1  200  ? -36.731 58.712  62.831  1.00 19.15 ? 198  GLY   A O     1 
ATOM   1337  N  N     . GLU   A  1  201  ? -35.871 59.110  60.774  1.00 20.65 ? 199  GLU   A N     1 
ATOM   1338  C  CA    . GLU   A  1  201  ? -35.301 60.394  61.160  1.00 20.68 ? 199  GLU   A CA    1 
ATOM   1339  C  C     . GLU   A  1  201  ? -36.380 61.457  61.287  1.00 23.16 ? 199  GLU   A C     1 
ATOM   1340  O  O     . GLU   A  1  201  ? -36.259 62.371  62.111  1.00 23.88 ? 199  GLU   A O     1 
ATOM   1341  C  CB    . GLU   A  1  201  ? -34.267 60.817  60.117  1.00 24.15 ? 199  GLU   A CB    1 
ATOM   1342  C  CG    . GLU   A  1  201  ? -33.468 62.046  60.473  1.00 35.35 ? 199  GLU   A CG    1 
ATOM   1343  C  CD    . GLU   A  1  201  ? -32.364 62.313  59.466  1.00 47.39 ? 199  GLU   A CD    1 
ATOM   1344  O  OE1   . GLU   A  1  201  ? -32.421 61.740  58.357  1.00 45.74 ? 199  GLU   A OE1   1 
ATOM   1345  O  OE2   . GLU   A  1  201  ? -31.436 63.086  59.788  1.00 55.79 ? 199  GLU   A OE2   1 
ATOM   1346  N  N     . THR   A  1  202  ? -37.436 61.349  60.487  1.00 21.38 ? 200  THR   A N     1 
ATOM   1347  C  CA    . THR   A  1  202  ? -38.545 62.283  60.511  1.00 19.13 ? 200  THR   A CA    1 
ATOM   1348  C  C     . THR   A  1  202  ? -39.831 61.487  60.606  1.00 19.67 ? 200  THR   A C     1 
ATOM   1349  O  O     . THR   A  1  202  ? -39.863 60.286  60.328  1.00 19.51 ? 200  THR   A O     1 
ATOM   1350  C  CB    . THR   A  1  202  ? -38.622 63.074  59.214  1.00 21.56 ? 200  THR   A CB    1 
ATOM   1351  O  OG1   . THR   A  1  202  ? -38.851 62.156  58.139  1.00 25.00 ? 200  THR   A OG1   1 
ATOM   1352  C  CG2   . THR   A  1  202  ? -37.318 63.842  58.967  1.00 24.99 ? 200  THR   A CG2   1 
ATOM   1353  N  N     . ILE   A  1  203  ? -40.904 62.177  60.984  1.00 18.57 ? 201  ILE   A N     1 
ATOM   1354  C  CA    . ILE   A  1  203  ? -42.182 61.487  61.118  1.00 18.86 ? 201  ILE   A CA    1 
ATOM   1355  C  C     . ILE   A  1  203  ? -42.615 60.890  59.785  1.00 19.93 ? 201  ILE   A C     1 
ATOM   1356  O  O     . ILE   A  1  203  ? -43.142 59.777  59.737  1.00 19.58 ? 201  ILE   A O     1 
ATOM   1357  C  CB    . ILE   A  1  203  ? -43.247 62.391  61.771  1.00 19.14 ? 201  ILE   A CB    1 
ATOM   1358  C  CG1   . ILE   A  1  203  ? -44.499 61.576  62.116  1.00 17.77 ? 201  ILE   A CG1   1 
ATOM   1359  C  CG2   . ILE   A  1  203  ? -43.594 63.583  60.888  1.00 20.46 ? 201  ILE   A CG2   1 
ATOM   1360  C  CD1   . ILE   A  1  203  ? -44.230 60.440  63.073  1.00 17.57 ? 201  ILE   A CD1   1 
ATOM   1361  N  N     . ARG   A  1  204  ? -42.336 61.581  58.677  1.00 19.05 ? 202  ARG   A N     1 
ATOM   1362  C  CA    . ARG   A  1  204  ? -42.722 61.052  57.372  1.00 20.51 ? 202  ARG   A CA    1 
ATOM   1363  C  C     . ARG   A  1  204  ? -41.991 59.756  57.053  1.00 20.94 ? 202  ARG   A C     1 
ATOM   1364  O  O     . ARG   A  1  204  ? -42.595 58.796  56.566  1.00 20.82 ? 202  ARG   A O     1 
ATOM   1365  C  CB    . ARG   A  1  204  ? -42.474 62.093  56.286  1.00 26.05 ? 202  ARG   A CB    1 
ATOM   1366  C  CG    . ARG   A  1  204  ? -43.621 63.052  56.131  1.00 33.02 ? 202  ARG   A CG    1 
ATOM   1367  C  CD    . ARG   A  1  204  ? -43.184 64.340  55.460  1.00 34.25 ? 202  ARG   A CD    1 
ATOM   1368  N  NE    . ARG   A  1  204  ? -44.307 65.264  55.377  1.00 35.12 ? 202  ARG   A NE    1 
ATOM   1369  C  CZ    . ARG   A  1  204  ? -44.799 65.940  56.407  1.00 33.78 ? 202  ARG   A CZ    1 
ATOM   1370  N  NH1   . ARG   A  1  204  ? -44.264 65.844  57.619  1.00 28.41 ? 202  ARG   A NH1   1 
ATOM   1371  N  NH2   . ARG   A  1  204  ? -45.853 66.731  56.217  1.00 28.77 ? 202  ARG   A NH2   1 
ATOM   1372  N  N     . GLU   A  1  205  ? -40.680 59.722  57.292  1.00 20.48 ? 203  GLU   A N     1 
ATOM   1373  C  CA    . GLU   A  1  205  ? -39.928 58.489  57.096  1.00 22.44 ? 203  GLU   A CA    1 
ATOM   1374  C  C     . GLU   A  1  205  ? -40.430 57.392  58.024  1.00 22.81 ? 203  GLU   A C     1 
ATOM   1375  O  O     . GLU   A  1  205  ? -40.604 56.241  57.604  1.00 21.49 ? 203  GLU   A O     1 
ATOM   1376  C  CB    . GLU   A  1  205  ? -38.440 58.748  57.327  1.00 22.55 ? 203  GLU   A CB    1 
ATOM   1377  C  CG    . GLU   A  1  205  ? -37.558 57.556  57.029  1.00 26.36 ? 203  GLU   A CG    1 
ATOM   1378  C  CD    . GLU   A  1  205  ? -36.085 57.907  57.097  1.00 33.14 ? 203  GLU   A CD    1 
ATOM   1379  O  OE1   . GLU   A  1  205  ? -35.586 58.173  58.211  1.00 30.37 ? 203  GLU   A OE1   1 
ATOM   1380  O  OE2   . GLU   A  1  205  ? -35.428 57.931  56.034  1.00 34.88 ? 203  GLU   A OE2   1 
ATOM   1381  N  N     . ALA   A  1  206  ? -40.685 57.734  59.287  1.00 19.40 ? 204  ALA   A N     1 
ATOM   1382  C  CA    . ALA   A  1  206  ? -41.182 56.741  60.229  1.00 19.05 ? 204  ALA   A CA    1 
ATOM   1383  C  C     . ALA   A  1  206  ? -42.522 56.180  59.784  1.00 20.80 ? 204  ALA   A C     1 
ATOM   1384  O  O     . ALA   A  1  206  ? -42.750 54.969  59.865  1.00 21.20 ? 204  ALA   A O     1 
ATOM   1385  C  CB    . ALA   A  1  206  ? -41.300 57.360  61.620  1.00 19.82 ? 204  ALA   A CB    1 
ATOM   1386  N  N     . LEU   A  1  207  ? -43.416 57.043  59.293  1.00 18.82 ? 205  LEU   A N     1 
ATOM   1387  C  CA    . LEU   A  1  207  ? -44.720 56.569  58.843  1.00 19.67 ? 205  LEU   A CA    1 
ATOM   1388  C  C     . LEU   A  1  207  ? -44.591 55.653  57.636  1.00 22.44 ? 205  LEU   A C     1 
ATOM   1389  O  O     . LEU   A  1  207  ? -45.288 54.635  57.548  1.00 21.54 ? 205  LEU   A O     1 
ATOM   1390  C  CB    . LEU   A  1  207  ? -45.636 57.746  58.524  1.00 20.32 ? 205  LEU   A CB    1 
ATOM   1391  C  CG    . LEU   A  1  207  ? -46.105 58.502  59.758  1.00 20.65 ? 205  LEU   A CG    1 
ATOM   1392  C  CD1   . LEU   A  1  207  ? -46.685 59.834  59.351  1.00 19.79 ? 205  LEU   A CD1   1 
ATOM   1393  C  CD2   . LEU   A  1  207  ? -47.139 57.667  60.504  1.00 20.96 ? 205  LEU   A CD2   1 
ATOM   1394  N  N     . LYS   A  1  208  ? -43.696 55.988  56.703  1.00 21.96 ? 206  LYS   A N     1 
ATOM   1395  C  CA    . LYS   A  1  208  ? -43.490 55.130  55.540  1.00 23.92 ? 206  LYS   A CA    1 
ATOM   1396  C  C     . LYS   A  1  208  ? -43.027 53.746  55.963  1.00 23.99 ? 206  LYS   A C     1 
ATOM   1397  O  O     . LYS   A  1  208  ? -43.509 52.733  55.440  1.00 26.77 ? 206  LYS   A O     1 
ATOM   1398  C  CB    . LYS   A  1  208  ? -42.478 55.768  54.587  1.00 26.83 ? 206  LYS   A CB    1 
ATOM   1399  N  N     . ARG   A  1  209  ? -42.122 53.683  56.935  1.00 21.99 ? 207  ARG   A N     1 
ATOM   1400  C  CA    . ARG   A  1  209  ? -41.564 52.421  57.400  1.00 23.25 ? 207  ARG   A CA    1 
ATOM   1401  C  C     . ARG   A  1  209  ? -42.503 51.649  58.310  1.00 24.53 ? 207  ARG   A C     1 
ATOM   1402  O  O     . ARG   A  1  209  ? -42.219 50.489  58.620  1.00 30.29 ? 207  ARG   A O     1 
ATOM   1403  C  CB    . ARG   A  1  209  ? -40.252 52.675  58.125  1.00 24.54 ? 207  ARG   A CB    1 
ATOM   1404  C  CG    . ARG   A  1  209  ? -39.166 53.157  57.191  1.00 27.94 ? 207  ARG   A CG    1 
ATOM   1405  C  CD    . ARG   A  1  209  ? -37.973 53.632  57.963  1.00 27.60 ? 207  ARG   A CD    1 
ATOM   1406  N  NE    . ARG   A  1  209  ? -36.922 54.099  57.073  1.00 28.98 ? 207  ARG   A NE    1 
ATOM   1407  C  CZ    . ARG   A  1  209  ? -35.768 54.595  57.493  1.00 33.42 ? 207  ARG   A CZ    1 
ATOM   1408  N  NH1   . ARG   A  1  209  ? -35.498 54.712  58.784  1.00 30.59 ? 207  ARG   A NH1   1 
ATOM   1409  N  NH2   . ARG   A  1  209  ? -34.866 54.989  56.597  1.00 38.76 ? 207  ARG   A NH2   1 
ATOM   1410  N  N     . SER   A  1  210  ? -43.604 52.253  58.744  1.00 23.63 ? 208  SER   A N     1 
ATOM   1411  C  CA    . SER   A  1  210  ? -44.525 51.559  59.632  1.00 22.88 ? 208  SER   A CA    1 
ATOM   1412  C  C     . SER   A  1  210  ? -45.508 50.669  58.886  1.00 25.32 ? 208  SER   A C     1 
ATOM   1413  O  O     . SER   A  1  210  ? -46.131 49.802  59.506  1.00 23.79 ? 208  SER   A O     1 
ATOM   1414  C  CB    . SER   A  1  210  ? -45.290 52.587  60.463  1.00 21.97 ? 208  SER   A CB    1 
ATOM   1415  O  OG    . SER   A  1  210  ? -44.393 53.311  61.290  1.00 23.37 ? 208  SER   A OG    1 
ATOM   1416  N  N     . LYS   A  1  211  ? -45.653 50.859  57.572  1.00 25.38 ? 209  LYS   A N     1 
ATOM   1417  C  CA    . LYS   A  1  211  ? -46.675 50.135  56.822  1.00 25.34 ? 209  LYS   A CA    1 
ATOM   1418  C  C     . LYS   A  1  211  ? -46.470 48.627  56.902  1.00 26.66 ? 209  LYS   A C     1 
ATOM   1419  O  O     . LYS   A  1  211  ? -47.440 47.869  57.023  1.00 27.73 ? 209  LYS   A O     1 
ATOM   1420  C  CB    . LYS   A  1  211  ? -46.676 50.603  55.366  1.00 30.44 ? 209  LYS   A CB    1 
ATOM   1421  N  N     . GLU   A  1  212  ? -45.215 48.178  56.857  1.00 24.80 ? 210  GLU   A N     1 
ATOM   1422  C  CA    . GLU   A  1  212  ? -44.933 46.745  56.815  1.00 30.32 ? 210  GLU   A CA    1 
ATOM   1423  C  C     . GLU   A  1  212  ? -45.511 46.026  58.029  1.00 28.98 ? 210  GLU   A C     1 
ATOM   1424  O  O     . GLU   A  1  212  ? -46.230 45.031  57.889  1.00 28.62 ? 210  GLU   A O     1 
ATOM   1425  C  CB    . GLU   A  1  212  ? -43.429 46.509  56.705  1.00 31.41 ? 210  GLU   A CB    1 
ATOM   1426  C  CG    . GLU   A  1  212  ? -43.046 45.045  56.598  1.00 39.39 ? 210  GLU   A CG    1 
ATOM   1427  C  CD    . GLU   A  1  212  ? -41.552 44.850  56.459  1.00 47.25 ? 210  GLU   A CD    1 
ATOM   1428  O  OE1   . GLU   A  1  212  ? -40.803 45.817  56.713  1.00 50.63 ? 210  GLU   A OE1   1 
ATOM   1429  O  OE2   . GLU   A  1  212  ? -41.128 43.734  56.090  1.00 58.50 ? 210  GLU   A OE2   1 
ATOM   1430  N  N     . LEU   A  1  213  ? -45.221 46.521  59.232  1.00 26.18 ? 211  LEU   A N     1 
ATOM   1431  C  CA    . LEU   A  1  213  ? -45.726 45.846  60.422  1.00 24.84 ? 211  LEU   A CA    1 
ATOM   1432  C  C     . LEU   A  1  213  ? -47.189 46.168  60.701  1.00 26.49 ? 211  LEU   A C     1 
ATOM   1433  O  O     . LEU   A  1  213  ? -47.888 45.351  61.308  1.00 24.30 ? 211  LEU   A O     1 
ATOM   1434  C  CB    . LEU   A  1  213  ? -44.839 46.139  61.631  1.00 23.91 ? 211  LEU   A CB    1 
ATOM   1435  C  CG    . LEU   A  1  213  ? -43.461 45.469  61.552  1.00 25.94 ? 211  LEU   A CG    1 
ATOM   1436  C  CD1   . LEU   A  1  213  ? -42.641 45.733  62.809  1.00 27.16 ? 211  LEU   A CD1   1 
ATOM   1437  C  CD2   . LEU   A  1  213  ? -43.603 43.974  61.304  1.00 33.13 ? 211  LEU   A CD2   1 
ATOM   1438  N  N     . GLU   A  1  214  ? -47.686 47.324  60.258  1.00 23.27 ? 212  GLU   A N     1 
ATOM   1439  C  CA    . GLU   A  1  214  ? -49.119 47.569  60.388  1.00 24.77 ? 212  GLU   A CA    1 
ATOM   1440  C  C     . GLU   A  1  214  ? -49.920 46.551  59.586  1.00 26.47 ? 212  GLU   A C     1 
ATOM   1441  O  O     . GLU   A  1  214  ? -50.984 46.102  60.028  1.00 26.57 ? 212  GLU   A O     1 
ATOM   1442  C  CB    . GLU   A  1  214  ? -49.467 48.997  59.975  1.00 22.03 ? 212  GLU   A CB    1 
ATOM   1443  C  CG    . GLU   A  1  214  ? -48.979 50.033  60.970  1.00 24.03 ? 212  GLU   A CG    1 
ATOM   1444  C  CD    . GLU   A  1  214  ? -49.420 51.430  60.617  1.00 24.55 ? 212  GLU   A CD    1 
ATOM   1445  O  OE1   . GLU   A  1  214  ? -49.756 51.672  59.438  1.00 28.17 ? 212  GLU   A OE1   1 
ATOM   1446  O  OE2   . GLU   A  1  214  ? -49.430 52.291  61.521  1.00 25.98 ? 212  GLU   A OE2   1 
ATOM   1447  N  N     . GLU   A  1  215  ? -49.411 46.159  58.414  1.00 26.99 ? 213  GLU   A N     1 
ATOM   1448  C  CA    . GLU   A  1  215  ? -50.090 45.160  57.598  1.00 29.87 ? 213  GLU   A CA    1 
ATOM   1449  C  C     . GLU   A  1  215  ? -50.121 43.796  58.272  1.00 32.70 ? 213  GLU   A C     1 
ATOM   1450  O  O     . GLU   A  1  215  ? -50.983 42.974  57.940  1.00 34.94 ? 213  GLU   A O     1 
ATOM   1451  C  CB    . GLU   A  1  215  ? -49.426 45.053  56.222  1.00 32.60 ? 213  GLU   A CB    1 
ATOM   1452  N  N     . LYS   A  1  216  ? -49.211 43.544  59.209  1.00 31.19 ? 214  LYS   A N     1 
ATOM   1453  C  CA    . LYS   A  1  216  ? -49.186 42.302  59.968  1.00 32.53 ? 214  LYS   A CA    1 
ATOM   1454  C  C     . LYS   A  1  216  ? -50.028 42.359  61.238  1.00 34.12 ? 214  LYS   A C     1 
ATOM   1455  O  O     . LYS   A  1  216  ? -50.208 41.325  61.888  1.00 37.83 ? 214  LYS   A O     1 
ATOM   1456  C  CB    . LYS   A  1  216  ? -47.745 41.925  60.319  1.00 29.69 ? 214  LYS   A CB    1 
ATOM   1457  N  N     . GLY   A  1  217  ? -50.550 43.530  61.601  1.00 26.50 ? 215  GLY   A N     1 
ATOM   1458  C  CA    . GLY   A  1  217  ? -51.401 43.676  62.765  1.00 26.24 ? 215  GLY   A CA    1 
ATOM   1459  C  C     . GLY   A  1  217  ? -50.807 44.492  63.893  1.00 25.05 ? 215  GLY   A C     1 
ATOM   1460  O  O     . GLY   A  1  217  ? -51.447 44.618  64.944  1.00 26.35 ? 215  GLY   A O     1 
ATOM   1461  N  N     . PHE   A  1  218  ? -49.602 45.028  63.727  1.00 22.64 ? 216  PHE   A N     1 
ATOM   1462  C  CA    . PHE   A  1  218  ? -49.065 45.940  64.719  1.00 19.41 ? 216  PHE   A CA    1 
ATOM   1463  C  C     . PHE   A  1  218  ? -49.664 47.325  64.532  1.00 20.08 ? 216  PHE   A C     1 
ATOM   1464  O  O     . PHE   A  1  218  ? -50.193 47.672  63.474  1.00 21.57 ? 216  PHE   A O     1 
ATOM   1465  C  CB    . PHE   A  1  218  ? -47.545 46.079  64.581  1.00 19.32 ? 216  PHE   A CB    1 
ATOM   1466  C  CG    . PHE   A  1  218  ? -46.773 44.860  64.999  1.00 22.18 ? 216  PHE   A CG    1 
ATOM   1467  C  CD1   . PHE   A  1  218  ? -46.637 43.782  64.140  1.00 25.06 ? 216  PHE   A CD1   1 
ATOM   1468  C  CD2   . PHE   A  1  218  ? -46.148 44.810  66.231  1.00 20.06 ? 216  PHE   A CD2   1 
ATOM   1469  C  CE1   . PHE   A  1  218  ? -45.918 42.667  64.517  1.00 25.12 ? 216  PHE   A CE1   1 
ATOM   1470  C  CE2   . PHE   A  1  218  ? -45.419 43.693  66.612  1.00 23.72 ? 216  PHE   A CE2   1 
ATOM   1471  C  CZ    . PHE   A  1  218  ? -45.307 42.623  65.752  1.00 22.30 ? 216  PHE   A CZ    1 
ATOM   1472  N  N     . SER   A  1  219  ? -49.559 48.129  65.579  1.00 18.28 ? 217  SER   A N     1 
ATOM   1473  C  CA    . SER   A  1  219  ? -49.834 49.551  65.489  1.00 18.48 ? 217  SER   A CA    1 
ATOM   1474  C  C     . SER   A  1  219  ? -48.612 50.293  65.998  1.00 18.17 ? 217  SER   A C     1 
ATOM   1475  O  O     . SER   A  1  219  ? -47.630 49.681  66.420  1.00 16.12 ? 217  SER   A O     1 
ATOM   1476  C  CB    . SER   A  1  219  ? -51.086 49.937  66.281  1.00 18.60 ? 217  SER   A CB    1 
ATOM   1477  O  OG    . SER   A  1  219  ? -50.897 49.615  67.642  1.00 19.64 ? 217  SER   A OG    1 
ATOM   1478  N  N     . TYR   A  1  220  ? -48.681 51.622  65.963  1.00 15.85 ? 218  TYR   A N     1 
ATOM   1479  C  CA    . TYR   A  1  220  ? -47.556 52.474  66.310  1.00 16.86 ? 218  TYR   A CA    1 
ATOM   1480  C  C     . TYR   A  1  220  ? -47.976 53.598  67.242  1.00 15.53 ? 218  TYR   A C     1 
ATOM   1481  O  O     . TYR   A  1  220  ? -49.104 54.096  67.187  1.00 16.18 ? 218  TYR   A O     1 
ATOM   1482  C  CB    . TYR   A  1  220  ? -46.919 53.075  65.052  1.00 17.50 ? 218  TYR   A CB    1 
ATOM   1483  C  CG    . TYR   A  1  220  ? -46.000 52.106  64.390  1.00 17.63 ? 218  TYR   A CG    1 
ATOM   1484  C  CD1   . TYR   A  1  220  ? -46.483 51.153  63.502  1.00 20.53 ? 218  TYR   A CD1   1 
ATOM   1485  C  CD2   . TYR   A  1  220  ? -44.650 52.121  64.670  1.00 17.75 ? 218  TYR   A CD2   1 
ATOM   1486  C  CE1   . TYR   A  1  220  ? -45.635 50.247  62.915  1.00 19.76 ? 218  TYR   A CE1   1 
ATOM   1487  C  CE2   . TYR   A  1  220  ? -43.798 51.223  64.086  1.00 18.69 ? 218  TYR   A CE2   1 
ATOM   1488  C  CZ    . TYR   A  1  220  ? -44.292 50.296  63.209  1.00 19.42 ? 218  TYR   A CZ    1 
ATOM   1489  O  OH    . TYR   A  1  220  ? -43.423 49.403  62.637  1.00 20.74 ? 218  TYR   A OH    1 
ATOM   1490  N  N     . SER   A  1  221  ? -47.049 53.985  68.112  1.00 16.08 ? 219  SER   A N     1 
ATOM   1491  C  CA    . SER   A  1  221  ? -47.139 55.232  68.859  1.00 16.62 ? 219  SER   A CA    1 
ATOM   1492  C  C     . SER   A  1  221  ? -45.810 55.938  68.676  1.00 16.17 ? 219  SER   A C     1 
ATOM   1493  O  O     . SER   A  1  221  ? -44.768 55.404  69.069  1.00 18.72 ? 219  SER   A O     1 
ATOM   1494  C  CB    . SER   A  1  221  ? -47.363 54.980  70.349  1.00 17.10 ? 219  SER   A CB    1 
ATOM   1495  O  OG    . SER   A  1  221  ? -47.497 56.227  71.021  1.00 18.49 ? 219  SER   A OG    1 
ATOM   1496  N  N     . TYR   A  1  222  ? -45.834 57.130  68.110  1.00 13.11 ? 220  TYR   A N     1 
ATOM   1497  C  CA    . TYR   A  1  222  ? -44.579 57.786  67.756  1.00 14.52 ? 220  TYR   A CA    1 
ATOM   1498  C  C     . TYR   A  1  222  ? -44.101 58.703  68.865  1.00 17.40 ? 220  TYR   A C     1 
ATOM   1499  O  O     . TYR   A  1  222  ? -44.880 59.449  69.460  1.00 16.27 ? 220  TYR   A O     1 
ATOM   1500  C  CB    . TYR   A  1  222  ? -44.727 58.559  66.448  1.00 15.76 ? 220  TYR   A CB    1 
ATOM   1501  C  CG    . TYR   A  1  222  ? -45.047 57.621  65.320  1.00 14.99 ? 220  TYR   A CG    1 
ATOM   1502  C  CD1   . TYR   A  1  222  ? -44.056 56.859  64.714  1.00 16.09 ? 220  TYR   A CD1   1 
ATOM   1503  C  CD2   . TYR   A  1  222  ? -46.359 57.455  64.894  1.00 14.29 ? 220  TYR   A CD2   1 
ATOM   1504  C  CE1   . TYR   A  1  222  ? -44.369 55.977  63.708  1.00 15.89 ? 220  TYR   A CE1   1 
ATOM   1505  C  CE2   . TYR   A  1  222  ? -46.674 56.583  63.889  1.00 16.20 ? 220  TYR   A CE2   1 
ATOM   1506  C  CZ    . TYR   A  1  222  ? -45.682 55.849  63.300  1.00 16.78 ? 220  TYR   A CZ    1 
ATOM   1507  O  OH    . TYR   A  1  222  ? -46.010 54.975  62.301  1.00 18.70 ? 220  TYR   A OH    1 
ATOM   1508  N  N     . ASP   A  1  223  ? -42.793 58.664  69.100  1.00 18.96 ? 221  ASP   A N     1 
ATOM   1509  C  CA    . ASP   A  1  223  ? -42.119 59.472  70.109  1.00 22.58 ? 221  ASP   A CA    1 
ATOM   1510  C  C     . ASP   A  1  223  ? -41.144 60.402  69.402  1.00 21.44 ? 221  ASP   A C     1 
ATOM   1511  O  O     . ASP   A  1  223  ? -40.102 59.953  68.901  1.00 20.68 ? 221  ASP   A O     1 
ATOM   1512  C  CB    . ASP   A  1  223  ? -41.362 58.550  71.048  1.00 21.12 ? 221  ASP   A CB    1 
ATOM   1513  C  CG    . ASP   A  1  223  ? -40.417 59.300  71.978  1.00 24.82 ? 221  ASP   A CG    1 
ATOM   1514  O  OD1   . ASP   A  1  223  ? -40.657 60.493  72.253  1.00 28.30 ? 221  ASP   A OD1   1 
ATOM   1515  O  OD2   . ASP   A  1  223  ? -39.433 58.675  72.428  1.00 35.40 ? 221  ASP   A OD2   1 
ATOM   1516  N  N     . MET   A  1  224  ? -41.461 61.693  69.387  1.00 20.57 ? 222  MET   A N     1 
ATOM   1517  C  CA    . MET   A  1  224  ? -40.605 62.683  68.753  1.00 22.67 ? 222  MET   A CA    1 
ATOM   1518  C  C     . MET   A  1  224  ? -39.390 63.027  69.598  1.00 25.32 ? 222  MET   A C     1 
ATOM   1519  O  O     . MET   A  1  224  ? -38.621 63.917  69.218  1.00 27.33 ? 222  MET   A O     1 
ATOM   1520  C  CB    . MET   A  1  224  ? -41.404 63.937  68.387  1.00 21.47 ? 222  MET   A CB    1 
ATOM   1521  C  CG    . MET   A  1  224  ? -42.615 63.653  67.486  1.00 26.97 ? 222  MET   A CG    1 
ATOM   1522  S  SD    . MET   A  1  224  ? -42.209 62.686  66.014  1.00 27.99 ? 222  MET   A SD    1 
ATOM   1523  C  CE    . MET   A  1  224  ? -41.081 63.801  65.190  1.00 33.77 ? 222  MET   A CE    1 
ATOM   1524  N  N     . LEU   A  1  225  ? -39.207 62.328  70.713  1.00 24.59 ? 223  LEU   A N     1 
ATOM   1525  C  CA    . LEU   A  1  225  ? -37.994 62.330  71.525  1.00 26.46 ? 223  LEU   A CA    1 
ATOM   1526  C  C     . LEU   A  1  225  ? -37.787 63.627  72.301  1.00 31.13 ? 223  LEU   A C     1 
ATOM   1527  O  O     . LEU   A  1  225  ? -36.717 63.822  72.885  1.00 33.17 ? 223  LEU   A O     1 
ATOM   1528  C  CB    . LEU   A  1  225  ? -36.744 61.915  70.730  1.00 30.82 ? 223  LEU   A CB    1 
ATOM   1529  C  CG    . LEU   A  1  225  ? -36.662 60.452  70.269  1.00 24.74 ? 223  LEU   A CG    1 
ATOM   1530  C  CD1   . LEU   A  1  225  ? -35.542 60.281  69.246  1.00 32.08 ? 223  LEU   A CD1   1 
ATOM   1531  C  CD2   . LEU   A  1  225  ? -36.446 59.513  71.453  1.00 28.05 ? 223  LEU   A CD2   1 
ATOM   1532  N  N     . GLY   A  1  226  ? -38.784 64.508  72.335  1.00 25.79 ? 224  GLY   A N     1 
ATOM   1533  C  CA    . GLY   A  1  226  ? -38.697 65.682  73.182  1.00 28.62 ? 224  GLY   A CA    1 
ATOM   1534  C  C     . GLY   A  1  226  ? -38.799 65.319  74.652  1.00 25.67 ? 224  GLY   A C     1 
ATOM   1535  O  O     . GLY   A  1  226  ? -39.534 64.412  75.048  1.00 25.01 ? 224  GLY   A O     1 
ATOM   1536  N  N     . GLU   A  1  227  ? -38.048 66.052  75.476  1.00 23.49 ? 225  GLU   A N     1 
ATOM   1537  C  CA    . GLU   A  1  227  ? -37.983 65.749  76.897  1.00 19.93 ? 225  GLU   A CA    1 
ATOM   1538  C  C     . GLU   A  1  227  ? -37.164 66.823  77.586  1.00 21.94 ? 225  GLU   A C     1 
ATOM   1539  O  O     . GLU   A  1  227  ? -36.229 67.366  76.991  1.00 20.16 ? 225  GLU   A O     1 
ATOM   1540  C  CB    . GLU   A  1  227  ? -37.324 64.384  77.069  1.00 24.76 ? 225  GLU   A CB    1 
ATOM   1541  C  CG    . GLU   A  1  227  ? -37.188 63.874  78.456  1.00 29.32 ? 225  GLU   A CG    1 
ATOM   1542  C  CD    . GLU   A  1  227  ? -36.458 62.547  78.459  1.00 35.20 ? 225  GLU   A CD    1 
ATOM   1543  O  OE1   . GLU   A  1  227  ? -36.401 61.899  77.386  1.00 28.76 ? 225  GLU   A OE1   1 
ATOM   1544  O  OE2   . GLU   A  1  227  ? -35.927 62.166  79.517  1.00 35.13 ? 225  GLU   A OE2   1 
ATOM   1545  N  N     . ALA   A  1  228  ? -37.532 67.160  78.818  1.00 20.50 ? 226  ALA   A N     1 
ATOM   1546  C  CA    . ALA   A  1  228  ? -36.729 68.013  79.686  1.00 20.65 ? 226  ALA   A CA    1 
ATOM   1547  C  C     . ALA   A  1  228  ? -36.356 69.332  79.004  1.00 17.16 ? 226  ALA   A C     1 
ATOM   1548  O  O     . ALA   A  1  228  ? -35.181 69.692  78.881  1.00 20.66 ? 226  ALA   A O     1 
ATOM   1549  C  CB    . ALA   A  1  228  ? -35.489 67.265  80.178  1.00 23.92 ? 226  ALA   A CB    1 
ATOM   1550  N  N     . ALA   A  1  229  ? -37.381 70.065  78.580  1.00 16.76 ? 227  ALA   A N     1 
ATOM   1551  C  CA    . ALA   A  1  229  ? -37.175 71.417  78.082  1.00 17.17 ? 227  ALA   A CA    1 
ATOM   1552  C  C     . ALA   A  1  229  ? -36.447 72.247  79.128  1.00 17.56 ? 227  ALA   A C     1 
ATOM   1553  O  O     . ALA   A  1  229  ? -36.800 72.238  80.308  1.00 16.98 ? 227  ALA   A O     1 
ATOM   1554  C  CB    . ALA   A  1  229  ? -38.519 72.065  77.763  1.00 17.38 ? 227  ALA   A CB    1 
ATOM   1555  N  N     . THR   A  1  230  ? -35.422 72.958  78.680  1.00 17.70 ? 228  THR   A N     1 
ATOM   1556  C  CA    . THR   A  1  230  ? -34.646 73.824  79.552  1.00 18.72 ? 228  THR   A CA    1 
ATOM   1557  C  C     . THR   A  1  230  ? -35.076 75.274  79.439  1.00 16.43 ? 228  THR   A C     1 
ATOM   1558  O  O     . THR   A  1  230  ? -34.911 76.045  80.387  1.00 16.79 ? 228  THR   A O     1 
ATOM   1559  C  CB    . THR   A  1  230  ? -33.164 73.700  79.175  1.00 20.22 ? 228  THR   A CB    1 
ATOM   1560  O  OG1   . THR   A  1  230  ? -32.788 72.316  79.216  1.00 26.77 ? 228  THR   A OG1   1 
ATOM   1561  C  CG2   . THR   A  1  230  ? -32.299 74.462  80.150  1.00 25.24 ? 228  THR   A CG2   1 
ATOM   1562  N  N     . THR   A  1  231  ? -35.654 75.658  78.305  1.00 16.09 ? 229  THR   A N     1 
ATOM   1563  C  CA    . THR   A  1  231  ? -36.006 77.043  78.039  1.00 15.38 ? 229  THR   A CA    1 
ATOM   1564  C  C     . THR   A  1  231  ? -37.400 77.076  77.439  1.00 15.86 ? 229  THR   A C     1 
ATOM   1565  O  O     . THR   A  1  231  ? -37.915 76.056  76.965  1.00 16.68 ? 229  THR   A O     1 
ATOM   1566  C  CB    . THR   A  1  231  ? -35.041 77.691  77.035  1.00 17.13 ? 229  THR   A CB    1 
ATOM   1567  O  OG1   . THR   A  1  231  ? -35.243 77.104  75.743  1.00 18.47 ? 229  THR   A OG1   1 
ATOM   1568  C  CG2   . THR   A  1  231  ? -33.578 77.485  77.437  1.00 17.62 ? 229  THR   A CG2   1 
ATOM   1569  N  N     . ALA   A  1  232  ? -38.003 78.261  77.485  1.00 15.89 ? 230  ALA   A N     1 
ATOM   1570  C  CA    . ALA   A  1  232  ? -39.263 78.463  76.779  1.00 16.95 ? 230  ALA   A CA    1 
ATOM   1571  C  C     . ALA   A  1  232  ? -39.122 78.111  75.305  1.00 18.70 ? 230  ALA   A C     1 
ATOM   1572  O  O     . ALA   A  1  232  ? -40.016 77.491  74.720  1.00 17.61 ? 230  ALA   A O     1 
ATOM   1573  C  CB    . ALA   A  1  232  ? -39.733 79.903  76.959  1.00 17.38 ? 230  ALA   A CB    1 
ATOM   1574  N  N     . ALA   A  1  233  ? -38.002 78.480  74.685  1.00 17.76 ? 231  ALA   A N     1 
ATOM   1575  C  CA    . ALA   A  1  233  ? -37.832 78.190  73.264  1.00 19.72 ? 231  ALA   A CA    1 
ATOM   1576  C  C     . ALA   A  1  233  ? -37.763 76.690  73.007  1.00 19.09 ? 231  ALA   A C     1 
ATOM   1577  O  O     . ALA   A  1  233  ? -38.294 76.205  71.998  1.00 20.93 ? 231  ALA   A O     1 
ATOM   1578  C  CB    . ALA   A  1  233  ? -36.592 78.897  72.722  1.00 21.93 ? 231  ALA   A CB    1 
ATOM   1579  N  N     . ASP   A  1  234  ? -37.113 75.938  73.900  1.00 17.76 ? 232  ASP   A N     1 
ATOM   1580  C  CA    . ASP   A  1  234  ? -37.101 74.484  73.784  1.00 20.15 ? 232  ASP   A CA    1 
ATOM   1581  C  C     . ASP   A  1  234  ? -38.514 73.941  73.844  1.00 19.61 ? 232  ASP   A C     1 
ATOM   1582  O  O     . ASP   A  1  234  ? -38.895 73.069  73.059  1.00 19.76 ? 232  ASP   A O     1 
ATOM   1583  C  CB    . ASP   A  1  234  ? -36.357 73.859  74.964  1.00 24.98 ? 232  ASP   A CB    1 
ATOM   1584  C  CG    . ASP   A  1  234  ? -34.863 73.938  74.855  1.00 32.50 ? 232  ASP   A CG    1 
ATOM   1585  O  OD1   . ASP   A  1  234  ? -34.327 74.276  73.782  1.00 29.71 ? 232  ASP   A OD1   1 
ATOM   1586  O  OD2   . ASP   A  1  234  ? -34.226 73.636  75.890  1.00 29.60 ? 232  ASP   A OD2   1 
ATOM   1587  N  N     . ALA   A  1  235  ? -39.286 74.402  74.828  1.00 16.85 ? 233  ALA   A N     1 
ATOM   1588  C  CA    . ALA   A  1  235  ? -40.640 73.905  74.997  1.00 15.77 ? 233  ALA   A CA    1 
ATOM   1589  C  C     . ALA   A  1  235  ? -41.479 74.221  73.773  1.00 18.25 ? 233  ALA   A C     1 
ATOM   1590  O  O     . ALA   A  1  235  ? -42.300 73.404  73.345  1.00 16.90 ? 233  ALA   A O     1 
ATOM   1591  C  CB    . ALA   A  1  235  ? -41.263 74.520  76.250  1.00 17.62 ? 233  ALA   A CB    1 
ATOM   1592  N  N     . GLU   A  1  236  ? -41.300 75.411  73.207  1.00 16.79 ? 234  GLU   A N     1 
ATOM   1593  C  CA    . GLU   A  1  236  ? -42.027 75.755  71.992  1.00 17.41 ? 234  GLU   A CA    1 
ATOM   1594  C  C     . GLU   A  1  236  ? -41.604 74.873  70.823  1.00 16.72 ? 234  GLU   A C     1 
ATOM   1595  O  O     . GLU   A  1  236  ? -42.448 74.454  70.021  1.00 17.68 ? 234  GLU   A O     1 
ATOM   1596  C  CB    . GLU   A  1  236  ? -41.840 77.238  71.671  1.00 21.81 ? 234  GLU   A CB    1 
ATOM   1597  N  N     . ARG   A  1  237  ? -40.308 74.573  70.708  1.00 17.49 ? 235  ARG   A N     1 
ATOM   1598  C  CA    . ARG   A  1  237  ? -39.844 73.680  69.649  1.00 18.79 ? 235  ARG   A CA    1 
ATOM   1599  C  C     . ARG   A  1  237  ? -40.441 72.290  69.807  1.00 19.84 ? 235  ARG   A C     1 
ATOM   1600  O  O     . ARG   A  1  237  ? -40.894 71.680  68.834  1.00 17.98 ? 235  ARG   A O     1 
ATOM   1601  C  CB    . ARG   A  1  237  ? -38.311 73.620  69.629  1.00 20.29 ? 235  ARG   A CB    1 
ATOM   1602  C  CG    . ARG   A  1  237  ? -37.734 72.626  68.633  1.00 26.18 ? 235  ARG   A CG    1 
ATOM   1603  C  CD    . ARG   A  1  237  ? -36.249 72.886  68.395  1.00 32.45 ? 235  ARG   A CD    1 
ATOM   1604  N  NE    . ARG   A  1  237  ? -35.503 72.848  69.645  1.00 36.96 ? 235  ARG   A NE    1 
ATOM   1605  C  CZ    . ARG   A  1  237  ? -35.020 71.742  70.193  1.00 39.14 ? 235  ARG   A CZ    1 
ATOM   1606  N  NH1   . ARG   A  1  237  ? -35.156 70.563  69.607  1.00 43.91 ? 235  ARG   A NH1   1 
ATOM   1607  N  NH2   . ARG   A  1  237  ? -34.388 71.820  71.362  1.00 34.90 ? 235  ARG   A NH2   1 
ATOM   1608  N  N     . TYR   A  1  238  ? -40.455 71.772  71.026  1.00 16.62 ? 236  TYR   A N     1 
ATOM   1609  C  CA    . TYR   A  1  238  ? -41.026 70.451  71.226  1.00 15.67 ? 236  TYR   A CA    1 
ATOM   1610  C  C     . TYR   A  1  238  ? -42.517 70.471  70.938  1.00 16.37 ? 236  TYR   A C     1 
ATOM   1611  O  O     . TYR   A  1  238  ? -43.051 69.529  70.347  1.00 16.71 ? 236  TYR   A O     1 
ATOM   1612  C  CB    . TYR   A  1  238  ? -40.738 69.969  72.645  1.00 14.39 ? 236  TYR   A CB    1 
ATOM   1613  C  CG    . TYR   A  1  238  ? -39.282 69.658  72.911  1.00 16.46 ? 236  TYR   A CG    1 
ATOM   1614  C  CD1   . TYR   A  1  238  ? -38.488 69.054  71.947  1.00 21.87 ? 236  TYR   A CD1   1 
ATOM   1615  C  CD2   . TYR   A  1  238  ? -38.714 69.943  74.142  1.00 17.19 ? 236  TYR   A CD2   1 
ATOM   1616  C  CE1   . TYR   A  1  238  ? -37.155 68.757  72.205  1.00 22.32 ? 236  TYR   A CE1   1 
ATOM   1617  C  CE2   . TYR   A  1  238  ? -37.398 69.659  74.403  1.00 21.74 ? 236  TYR   A CE2   1 
ATOM   1618  C  CZ    . TYR   A  1  238  ? -36.624 69.058  73.441  1.00 22.89 ? 236  TYR   A CZ    1 
ATOM   1619  O  OH    . TYR   A  1  238  ? -35.304 68.774  73.712  1.00 25.45 ? 236  TYR   A OH    1 
ATOM   1620  N  N     . TYR   A  1  239  ? -43.196 71.550  71.318  1.00 14.76 ? 237  TYR   A N     1 
ATOM   1621  C  CA    . TYR   A  1  239  ? -44.608 71.674  70.991  1.00 14.80 ? 237  TYR   A CA    1 
ATOM   1622  C  C     . TYR   A  1  239  ? -44.822 71.600  69.488  1.00 16.54 ? 237  TYR   A C     1 
ATOM   1623  O  O     . TYR   A  1  239  ? -45.671 70.839  69.005  1.00 15.33 ? 237  TYR   A O     1 
ATOM   1624  C  CB    . TYR   A  1  239  ? -45.170 72.984  71.528  1.00 17.04 ? 237  TYR   A CB    1 
ATOM   1625  C  CG    . TYR   A  1  239  ? -46.614 73.105  71.174  1.00 17.40 ? 237  TYR   A CG    1 
ATOM   1626  C  CD1   . TYR   A  1  239  ? -47.004 73.599  69.937  1.00 17.08 ? 237  TYR   A CD1   1 
ATOM   1627  C  CD2   . TYR   A  1  239  ? -47.596 72.668  72.044  1.00 18.25 ? 237  TYR   A CD2   1 
ATOM   1628  C  CE1   . TYR   A  1  239  ? -48.332 73.677  69.583  1.00 20.61 ? 237  TYR   A CE1   1 
ATOM   1629  C  CE2   . TYR   A  1  239  ? -48.924 72.754  71.708  1.00 18.77 ? 237  TYR   A CE2   1 
ATOM   1630  C  CZ    . TYR   A  1  239  ? -49.290 73.251  70.478  1.00 19.30 ? 237  TYR   A CZ    1 
ATOM   1631  O  OH    . TYR   A  1  239  ? -50.617 73.332  70.130  1.00 24.07 ? 237  TYR   A OH    1 
ATOM   1632  N  N     . ARG   A  1  240  ? -44.090 72.415  68.733  1.00 16.00 ? 238  ARG   A N     1 
ATOM   1633  C  CA    . ARG   A  1  240  ? -44.350 72.420  67.301  1.00 15.57 ? 238  ARG   A CA    1 
ATOM   1634  C  C     . ARG   A  1  240  ? -43.954 71.100  66.662  1.00 15.55 ? 238  ARG   A C     1 
ATOM   1635  O  O     . ARG   A  1  240  ? -44.555 70.699  65.660  1.00 15.72 ? 238  ARG   A O     1 
ATOM   1636  C  CB    . ARG   A  1  240  ? -43.722 73.635  66.615  1.00 19.91 ? 238  ARG   A CB    1 
ATOM   1637  C  CG    . ARG   A  1  240  ? -42.237 73.622  66.565  1.00 24.40 ? 238  ARG   A CG    1 
ATOM   1638  C  CD    . ARG   A  1  240  ? -41.736 74.820  65.763  1.00 20.66 ? 238  ARG   A CD    1 
ATOM   1639  N  NE    . ARG   A  1  240  ? -40.303 74.982  65.951  1.00 23.11 ? 238  ARG   A NE    1 
ATOM   1640  C  CZ    . ARG   A  1  240  ? -39.747 75.781  66.855  1.00 27.70 ? 238  ARG   A CZ    1 
ATOM   1641  N  NH1   . ARG   A  1  240  ? -40.475 76.600  67.602  1.00 21.43 ? 238  ARG   A NH1   1 
ATOM   1642  N  NH2   . ARG   A  1  240  ? -38.426 75.765  67.007  1.00 28.20 ? 238  ARG   A NH2   1 
ATOM   1643  N  N     . ASP   A  1  241  ? -42.977 70.390  67.230  1.00 15.58 ? 239  ASP   A N     1 
ATOM   1644  C  CA    . ASP   A  1  241  ? -42.661 69.057  66.734  1.00 15.01 ? 239  ASP   A CA    1 
ATOM   1645  C  C     . ASP   A  1  241  ? -43.813 68.094  66.989  1.00 17.19 ? 239  ASP   A C     1 
ATOM   1646  O  O     . ASP   A  1  241  ? -44.166 67.293  66.119  1.00 16.84 ? 239  ASP   A O     1 
ATOM   1647  C  CB    . ASP   A  1  241  ? -41.392 68.524  67.389  1.00 20.88 ? 239  ASP   A CB    1 
ATOM   1648  C  CG    . ASP   A  1  241  ? -40.142 69.227  66.905  1.00 29.70 ? 239  ASP   A CG    1 
ATOM   1649  O  OD1   . ASP   A  1  241  ? -40.234 70.053  65.968  1.00 34.00 ? 239  ASP   A OD1   1 
ATOM   1650  O  OD2   . ASP   A  1  241  ? -39.070 68.960  67.488  1.00 39.55 ? 239  ASP   A OD2   1 
ATOM   1651  N  N     . TYR   A  1  242  ? -44.406 68.147  68.179  1.00 15.44 ? 240  TYR   A N     1 
ATOM   1652  C  CA    . TYR   A  1  242  ? -45.554 67.291  68.454  1.00 15.45 ? 240  TYR   A CA    1 
ATOM   1653  C  C     . TYR   A  1  242  ? -46.721 67.641  67.549  1.00 15.00 ? 240  TYR   A C     1 
ATOM   1654  O  O     . TYR   A  1  242  ? -47.400 66.753  67.023  1.00 14.02 ? 240  TYR   A O     1 
ATOM   1655  C  CB    . TYR   A  1  242  ? -46.003 67.461  69.901  1.00 14.81 ? 240  TYR   A CB    1 
ATOM   1656  C  CG    . TYR   A  1  242  ? -45.129 66.833  70.947  1.00 14.57 ? 240  TYR   A CG    1 
ATOM   1657  C  CD1   . TYR   A  1  242  ? -44.471 65.629  70.731  1.00 16.41 ? 240  TYR   A CD1   1 
ATOM   1658  C  CD2   . TYR   A  1  242  ? -45.004 67.433  72.179  1.00 15.02 ? 240  TYR   A CD2   1 
ATOM   1659  C  CE1   . TYR   A  1  242  ? -43.687 65.061  71.742  1.00 16.47 ? 240  TYR   A CE1   1 
ATOM   1660  C  CE2   . TYR   A  1  242  ? -44.231 66.891  73.165  1.00 15.18 ? 240  TYR   A CE2   1 
ATOM   1661  C  CZ    . TYR   A  1  242  ? -43.584 65.710  72.943  1.00 14.01 ? 240  TYR   A CZ    1 
ATOM   1662  O  OH    . TYR   A  1  242  ? -42.826 65.193  73.966  1.00 15.27 ? 240  TYR   A OH    1 
ATOM   1663  N  N     . GLU   A  1  243  ? -46.980 68.932  67.374  1.00 13.34 ? 241  GLU   A N     1 
ATOM   1664  C  CA    . GLU   A  1  243  ? -48.117 69.345  66.568  1.00 14.58 ? 241  GLU   A CA    1 
ATOM   1665  C  C     . GLU   A  1  243  ? -47.938 68.902  65.125  1.00 13.81 ? 241  GLU   A C     1 
ATOM   1666  O  O     . GLU   A  1  243  ? -48.859 68.351  64.516  1.00 15.28 ? 241  GLU   A O     1 
ATOM   1667  C  CB    . GLU   A  1  243  ? -48.272 70.857  66.667  1.00 15.18 ? 241  GLU   A CB    1 
ATOM   1668  C  CG    . GLU   A  1  243  ? -49.330 71.445  65.791  1.00 19.06 ? 241  GLU   A CG    1 
ATOM   1669  C  CD    . GLU   A  1  243  ? -49.181 72.955  65.691  1.00 22.57 ? 241  GLU   A CD    1 
ATOM   1670  O  OE1   . GLU   A  1  243  ? -48.036 73.475  65.734  1.00 29.13 ? 241  GLU   A OE1   1 
ATOM   1671  O  OE2   . GLU   A  1  243  ? -50.212 73.613  65.578  1.00 19.93 ? 241  GLU   A OE2   1 
ATOM   1672  N  N     . SER   A  1  244  ? -46.742 69.089  64.575  1.00 14.74 ? 242  SER   A N     1 
ATOM   1673  C  CA    . SER   A  1  244  ? -46.514 68.652  63.206  1.00 14.39 ? 242  SER   A CA    1 
ATOM   1674  C  C     . SER   A  1  244  ? -46.588 67.137  63.093  1.00 15.83 ? 242  SER   A C     1 
ATOM   1675  O  O     . SER   A  1  244  ? -47.112 66.612  62.105  1.00 17.63 ? 242  SER   A O     1 
ATOM   1676  C  CB    . SER   A  1  244  ? -45.173 69.184  62.696  1.00 16.44 ? 242  SER   A CB    1 
ATOM   1677  O  OG    . SER   A  1  244  ? -44.089 68.659  63.430  1.00 20.47 ? 242  SER   A OG    1 
ATOM   1678  N  N     . ALA   A  1  245  ? -46.109 66.414  64.109  1.00 15.17 ? 243  ALA   A N     1 
ATOM   1679  C  CA    . ALA   A  1  245  ? -46.210 64.958  64.074  1.00 14.68 ? 243  ALA   A CA    1 
ATOM   1680  C  C     . ALA   A  1  245  ? -47.665 64.508  64.139  1.00 15.36 ? 243  ALA   A C     1 
ATOM   1681  O  O     . ALA   A  1  245  ? -48.054 63.566  63.448  1.00 15.67 ? 243  ALA   A O     1 
ATOM   1682  C  CB    . ALA   A  1  245  ? -45.395 64.325  65.198  1.00 16.58 ? 243  ALA   A CB    1 
ATOM   1683  N  N     . ILE   A  1  246  ? -48.483 65.157  64.969  1.00 14.19 ? 244  ILE   A N     1 
ATOM   1684  C  CA    . ILE   A  1  246  ? -49.895 64.791  65.029  1.00 14.58 ? 244  ILE   A CA    1 
ATOM   1685  C  C     . ILE   A  1  246  ? -50.546 64.934  63.663  1.00 17.11 ? 244  ILE   A C     1 
ATOM   1686  O  O     . ILE   A  1  246  ? -51.304 64.061  63.235  1.00 15.69 ? 244  ILE   A O     1 
ATOM   1687  C  CB    . ILE   A  1  246  ? -50.631 65.595  66.109  1.00 13.88 ? 244  ILE   A CB    1 
ATOM   1688  C  CG1   . ILE   A  1  246  ? -50.162 65.149  67.490  1.00 14.74 ? 244  ILE   A CG1   1 
ATOM   1689  C  CG2   . ILE   A  1  246  ? -52.139 65.381  65.997  1.00 16.90 ? 244  ILE   A CG2   1 
ATOM   1690  C  CD1   . ILE   A  1  246  ? -50.579 66.096  68.581  1.00 16.56 ? 244  ILE   A CD1   1 
ATOM   1691  N  N     . HIS   A  1  247  ? -50.259 66.026  62.951  1.00 14.69 ? 245  HIS   A N     1 
ATOM   1692  C  CA    . HIS   A  1  247  ? -50.820 66.174  61.611  1.00 14.92 ? 245  HIS   A CA    1 
ATOM   1693  C  C     . HIS   A  1  247  ? -50.380 65.029  60.713  1.00 15.95 ? 245  HIS   A C     1 
ATOM   1694  O  O     . HIS   A  1  247  ? -51.199 64.429  60.014  1.00 15.69 ? 245  HIS   A O     1 
ATOM   1695  C  CB    . HIS   A  1  247  ? -50.407 67.508  60.997  1.00 17.19 ? 245  HIS   A CB    1 
ATOM   1696  C  CG    . HIS   A  1  247  ? -51.104 68.687  61.586  1.00 17.25 ? 245  HIS   A CG    1 
ATOM   1697  N  ND1   . HIS   A  1  247  ? -52.455 68.902  61.452  1.00 17.52 ? 245  HIS   A ND1   1 
ATOM   1698  C  CD2   . HIS   A  1  247  ? -50.625 69.734  62.300  1.00 19.81 ? 245  HIS   A CD2   1 
ATOM   1699  C  CE1   . HIS   A  1  247  ? -52.785 70.024  62.067  1.00 21.93 ? 245  HIS   A CE1   1 
ATOM   1700  N  NE2   . HIS   A  1  247  ? -51.693 70.542  62.596  1.00 19.40 ? 245  HIS   A NE2   1 
ATOM   1701  N  N     . ALA   A  1  248  ? -49.088 64.708  60.719  1.00 15.68 ? 246  ALA   A N     1 
ATOM   1702  C  CA    . ALA   A  1  248  ? -48.610 63.646  59.843  1.00 15.71 ? 246  ALA   A CA    1 
ATOM   1703  C  C     . ALA   A  1  248  ? -49.219 62.307  60.227  1.00 16.78 ? 246  ALA   A C     1 
ATOM   1704  O  O     . ALA   A  1  248  ? -49.664 61.549  59.360  1.00 16.92 ? 246  ALA   A O     1 
ATOM   1705  C  CB    . ALA   A  1  248  ? -47.081 63.587  59.863  1.00 15.92 ? 246  ALA   A CB    1 
ATOM   1706  N  N     . ILE   A  1  249  ? -49.259 62.010  61.526  1.00 15.85 ? 247  ILE   A N     1 
ATOM   1707  C  CA    . ILE   A  1  249  ? -49.831 60.757  62.003  1.00 14.38 ? 247  ILE   A CA    1 
ATOM   1708  C  C     . ILE   A  1  249  ? -51.325 60.714  61.724  1.00 15.66 ? 247  ILE   A C     1 
ATOM   1709  O  O     . ILE   A  1  249  ? -51.863 59.682  61.314  1.00 16.41 ? 247  ILE   A O     1 
ATOM   1710  C  CB    . ILE   A  1  249  ? -49.541 60.608  63.507  1.00 14.64 ? 247  ILE   A CB    1 
ATOM   1711  C  CG1   . ILE   A  1  249  ? -48.049 60.458  63.750  1.00 15.08 ? 247  ILE   A CG1   1 
ATOM   1712  C  CG2   . ILE   A  1  249  ? -50.271 59.400  64.081  1.00 15.55 ? 247  ILE   A CG2   1 
ATOM   1713  C  CD1   . ILE   A  1  249  ? -47.660 60.833  65.177  1.00 16.71 ? 247  ILE   A CD1   1 
ATOM   1714  N  N     . GLY   A  1  250  ? -52.022 61.819  61.974  1.00 14.92 ? 248  GLY   A N     1 
ATOM   1715  C  CA    . GLY   A  1  250  ? -53.451 61.845  61.726  1.00 15.30 ? 248  GLY   A CA    1 
ATOM   1716  C  C     . GLY   A  1  250  ? -53.794 61.730  60.255  1.00 15.93 ? 248  GLY   A C     1 
ATOM   1717  O  O     . GLY   A  1  250  ? -54.781 61.091  59.892  1.00 16.56 ? 248  GLY   A O     1 
ATOM   1718  N  N     . LYS   A  1  251  ? -52.994 62.355  59.392  1.00 15.78 ? 249  LYS   A N     1 
ATOM   1719  C  CA    . LYS   A  1  251  ? -53.214 62.203  57.959  1.00 16.86 ? 249  LYS   A CA    1 
ATOM   1720  C  C     . LYS   A  1  251  ? -53.031 60.757  57.545  1.00 17.73 ? 249  LYS   A C     1 
ATOM   1721  O  O     . LYS   A  1  251  ? -53.777 60.248  56.699  1.00 18.28 ? 249  LYS   A O     1 
ATOM   1722  C  CB    . LYS   A  1  251  ? -52.221 63.056  57.181  1.00 17.59 ? 249  LYS   A CB    1 
ATOM   1723  C  CG    . LYS   A  1  251  ? -52.486 64.539  57.201  1.00 18.21 ? 249  LYS   A CG    1 
ATOM   1724  C  CD    . LYS   A  1  251  ? -51.279 65.222  56.610  1.00 19.58 ? 249  LYS   A CD    1 
ATOM   1725  C  CE    . LYS   A  1  251  ? -51.414 66.722  56.620  1.00 19.08 ? 249  LYS   A CE    1 
ATOM   1726  N  NZ    . LYS   A  1  251  ? -50.138 67.281  56.067  1.00 20.24 ? 249  LYS   A NZ    1 
ATOM   1727  N  N     . ALA   A  1  252  ? -52.017 60.091  58.108  1.00 16.86 ? 250  ALA   A N     1 
ATOM   1728  C  CA    . ALA   A  1  252  ? -51.739 58.708  57.758  1.00 18.70 ? 250  ALA   A CA    1 
ATOM   1729  C  C     . ALA   A  1  252  ? -52.738 57.767  58.400  1.00 19.04 ? 250  ALA   A C     1 
ATOM   1730  O  O     . ALA   A  1  252  ? -53.099 56.747  57.807  1.00 19.71 ? 250  ALA   A O     1 
ATOM   1731  C  CB    . ALA   A  1  252  ? -50.328 58.328  58.190  1.00 21.14 ? 250  ALA   A CB    1 
ATOM   1732  N  N     . SER   A  1  253  ? -53.180 58.079  59.617  1.00 18.62 ? 251  SER   A N     1 
ATOM   1733  C  CA    . SER   A  1  253  ? -54.180 57.235  60.247  1.00 16.90 ? 251  SER   A CA    1 
ATOM   1734  C  C     . SER   A  1  253  ? -55.404 57.109  59.359  1.00 19.01 ? 251  SER   A C     1 
ATOM   1735  O  O     . SER   A  1  253  ? -55.957 56.015  59.202  1.00 19.34 ? 251  SER   A O     1 
ATOM   1736  C  CB    . SER   A  1  253  ? -54.555 57.804  61.607  1.00 17.83 ? 251  SER   A CB    1 
ATOM   1737  O  OG    . SER   A  1  253  ? -55.589 57.025  62.161  1.00 17.68 ? 251  SER   A OG    1 
ATOM   1738  N  N     . ALA   A  1  254  ? -55.808 58.215  58.735  1.00 18.57 ? 252  ALA   A N     1 
ATOM   1739  C  CA    . ALA   A  1  254  ? -56.879 58.230  57.742  1.00 19.61 ? 252  ALA   A CA    1 
ATOM   1740  C  C     . ALA   A  1  254  ? -58.135 57.527  58.254  1.00 22.62 ? 252  ALA   A C     1 
ATOM   1741  O  O     . ALA   A  1  254  ? -58.746 56.698  57.571  1.00 21.30 ? 252  ALA   A O     1 
ATOM   1742  C  CB    . ALA   A  1  254  ? -56.411 57.667  56.400  1.00 22.49 ? 252  ALA   A CB    1 
ATOM   1743  N  N     . GLY   A  1  255  ? -58.517 57.859  59.481  1.00 18.97 ? 253  GLY   A N     1 
ATOM   1744  C  CA    . GLY   A  1  255  ? -59.755 57.351  60.027  1.00 21.05 ? 253  GLY   A CA    1 
ATOM   1745  C  C     . GLY   A  1  255  ? -59.696 55.963  60.618  1.00 18.85 ? 253  GLY   A C     1 
ATOM   1746  O  O     . GLY   A  1  255  ? -60.746 55.415  60.956  1.00 22.13 ? 253  GLY   A O     1 
ATOM   1747  N  N     . ARG   A  1  256  ? -58.508 55.371  60.769  1.00 19.22 ? 254  ARG   A N     1 
ATOM   1748  C  CA    . ARG   A  1  256  ? -58.429 54.045  61.372  1.00 18.61 ? 254  ARG   A CA    1 
ATOM   1749  C  C     . ARG   A  1  256  ? -58.799 54.054  62.844  1.00 18.53 ? 254  ARG   A C     1 
ATOM   1750  O  O     . ARG   A  1  256  ? -59.076 52.988  63.406  1.00 21.01 ? 254  ARG   A O     1 
ATOM   1751  C  CB    . ARG   A  1  256  ? -57.042 53.440  61.189  1.00 18.67 ? 254  ARG   A CB    1 
ATOM   1752  C  CG    . ARG   A  1  256  ? -56.853 52.801  59.832  1.00 20.98 ? 254  ARG   A CG    1 
ATOM   1753  C  CD    . ARG   A  1  256  ? -55.434 52.316  59.672  1.00 24.00 ? 254  ARG   A CD    1 
ATOM   1754  N  NE    . ARG   A  1  256  ? -54.508 53.419  59.462  1.00 20.68 ? 254  ARG   A NE    1 
ATOM   1755  C  CZ    . ARG   A  1  256  ? -53.190 53.287  59.436  1.00 22.95 ? 254  ARG   A CZ    1 
ATOM   1756  N  NH1   . ARG   A  1  256  ? -52.607 52.131  59.716  1.00 25.07 ? 254  ARG   A NH1   1 
ATOM   1757  N  NH2   . ARG   A  1  256  ? -52.440 54.334  59.109  1.00 22.06 ? 254  ARG   A NH2   1 
ATOM   1758  N  N     . GLY   A  1  257  ? -58.787 55.214  63.484  1.00 18.15 ? 255  GLY   A N     1 
ATOM   1759  C  CA    . GLY   A  1  257  ? -59.183 55.289  64.872  1.00 17.69 ? 255  GLY   A CA    1 
ATOM   1760  C  C     . GLY   A  1  257  ? -58.043 54.994  65.821  1.00 16.15 ? 255  GLY   A C     1 
ATOM   1761  O  O     . GLY   A  1  257  ? -56.906 54.710  65.440  1.00 17.35 ? 255  GLY   A O     1 
ATOM   1762  N  N     . ILE   A  1  258  ? -58.377 55.021  67.106  1.00 15.77 ? 256  ILE   A N     1 
ATOM   1763  C  CA    . ILE   A  1  258  ? -57.330 55.053  68.119  1.00 15.79 ? 256  ILE   A CA    1 
ATOM   1764  C  C     . ILE   A  1  258  ? -56.736 53.691  68.427  1.00 17.42 ? 256  ILE   A C     1 
ATOM   1765  O  O     . ILE   A  1  258  ? -55.654 53.624  69.018  1.00 16.20 ? 256  ILE   A O     1 
ATOM   1766  C  CB    . ILE   A  1  258  ? -57.830 55.705  69.410  1.00 15.34 ? 256  ILE   A CB    1 
ATOM   1767  C  CG1   . ILE   A  1  258  ? -58.970 54.876  70.007  1.00 17.26 ? 256  ILE   A CG1   1 
ATOM   1768  C  CG2   . ILE   A  1  258  ? -58.269 57.144  69.136  1.00 16.27 ? 256  ILE   A CG2   1 
ATOM   1769  C  CD1   . ILE   A  1  258  ? -59.499 55.431  71.311  1.00 18.55 ? 256  ILE   A CD1   1 
ATOM   1770  N  N     . TYR   A  1  259  ? -57.404 52.604  68.060  1.00 18.28 ? 257  TYR   A N     1 
ATOM   1771  C  CA    . TYR   A  1  259  ? -56.880 51.278  68.360  1.00 18.10 ? 257  TYR   A CA    1 
ATOM   1772  C  C     . TYR   A  1  259  ? -56.098 50.696  67.194  1.00 19.69 ? 257  TYR   A C     1 
ATOM   1773  O  O     . TYR   A  1  259  ? -54.941 50.300  67.360  1.00 21.17 ? 257  TYR   A O     1 
ATOM   1774  C  CB    . TYR   A  1  259  ? -58.014 50.346  68.788  1.00 20.56 ? 257  TYR   A CB    1 
ATOM   1775  C  CG    . TYR   A  1  259  ? -58.827 50.930  69.913  1.00 18.23 ? 257  TYR   A CG    1 
ATOM   1776  C  CD1   . TYR   A  1  259  ? -58.240 51.231  71.132  1.00 20.08 ? 257  TYR   A CD1   1 
ATOM   1777  C  CD2   . TYR   A  1  259  ? -60.178 51.209  69.755  1.00 18.35 ? 257  TYR   A CD2   1 
ATOM   1778  C  CE1   . TYR   A  1  259  ? -58.973 51.783  72.160  1.00 20.59 ? 257  TYR   A CE1   1 
ATOM   1779  C  CE2   . TYR   A  1  259  ? -60.914 51.760  70.777  1.00 20.03 ? 257  TYR   A CE2   1 
ATOM   1780  C  CZ    . TYR   A  1  259  ? -60.308 52.044  71.977  1.00 19.75 ? 257  TYR   A CZ    1 
ATOM   1781  O  OH    . TYR   A  1  259  ? -61.043 52.608  72.990  1.00 19.07 ? 257  TYR   A OH    1 
ATOM   1782  N  N     . GLU   A  1  260  ? -56.695 50.671  66.005  1.00 18.78 ? 258  GLU   A N     1 
ATOM   1783  C  CA    . GLU   A  1  260  ? -55.982 50.157  64.844  1.00 22.78 ? 258  GLU   A CA    1 
ATOM   1784  C  C     . GLU   A  1  260  ? -54.950 51.147  64.335  1.00 21.81 ? 258  GLU   A C     1 
ATOM   1785  O  O     . GLU   A  1  260  ? -53.887 50.741  63.847  1.00 25.22 ? 258  GLU   A O     1 
ATOM   1786  C  CB    . GLU   A  1  260  ? -56.956 49.833  63.710  1.00 24.39 ? 258  GLU   A CB    1 
ATOM   1787  C  CG    . GLU   A  1  260  ? -56.269 49.179  62.510  1.00 34.69 ? 258  GLU   A CG    1 
ATOM   1788  C  CD    . GLU   A  1  260  ? -57.113 49.177  61.246  1.00 39.03 ? 258  GLU   A CD    1 
ATOM   1789  O  OE1   . GLU   A  1  260  ? -58.358 49.216  61.350  1.00 40.56 ? 258  GLU   A OE1   1 
ATOM   1790  O  OE2   . GLU   A  1  260  ? -56.521 49.134  60.143  1.00 37.37 ? 258  GLU   A OE2   1 
ATOM   1791  N  N     . GLY   A  1  261  ? -55.229 52.440  64.455  1.00 18.04 ? 259  GLY   A N     1 
ATOM   1792  C  CA    . GLY   A  1  261  ? -54.397 53.440  63.845  1.00 16.09 ? 259  GLY   A CA    1 
ATOM   1793  C  C     . GLY   A  1  261  ? -53.326 53.943  64.782  1.00 17.31 ? 259  GLY   A C     1 
ATOM   1794  O  O     . GLY   A  1  261  ? -53.337 53.697  65.993  1.00 16.97 ? 259  GLY   A O     1 
ATOM   1795  N  N     . PRO   A  1  262  ? -52.373 54.670  64.213  1.00 15.81 ? 260  PRO   A N     1 
ATOM   1796  C  CA    . PRO   A  1  262  ? -51.219 55.135  64.982  1.00 17.29 ? 260  PRO   A CA    1 
ATOM   1797  C  C     . PRO   A  1  262  ? -51.592 56.283  65.902  1.00 16.55 ? 260  PRO   A C     1 
ATOM   1798  O  O     . PRO   A  1  262  ? -52.596 56.974  65.721  1.00 18.59 ? 260  PRO   A O     1 
ATOM   1799  C  CB    . PRO   A  1  262  ? -50.254 55.614  63.894  1.00 16.36 ? 260  PRO   A CB    1 
ATOM   1800  C  CG    . PRO   A  1  262  ? -51.163 55.991  62.735  1.00 17.81 ? 260  PRO   A CG    1 
ATOM   1801  C  CD    . PRO   A  1  262  ? -52.261 54.979  62.781  1.00 17.72 ? 260  PRO   A CD    1 
ATOM   1802  N  N     . GLY   A  1  263  ? -50.766 56.460  66.928  1.00 15.57 ? 261  GLY   A N     1 
ATOM   1803  C  CA    . GLY   A  1  263  ? -50.912 57.576  67.834  1.00 15.50 ? 261  GLY   A CA    1 
ATOM   1804  C  C     . GLY   A  1  263  ? -49.576 58.220  68.126  1.00 13.23 ? 261  GLY   A C     1 
ATOM   1805  O  O     . GLY   A  1  263  ? -48.558 57.901  67.497  1.00 14.51 ? 261  GLY   A O     1 
ATOM   1806  N  N     . ILE   A  1  264  ? -49.577 59.139  69.077  1.00 14.05 ? 262  ILE   A N     1 
ATOM   1807  C  CA    . ILE   A  1  264  ? -48.376 59.852  69.471  1.00 14.16 ? 262  ILE   A CA    1 
ATOM   1808  C  C     . ILE   A  1  264  ? -48.214 59.718  70.975  1.00 15.50 ? 262  ILE   A C     1 
ATOM   1809  O  O     . ILE   A  1  264  ? -49.190 59.544  71.712  1.00 15.64 ? 262  ILE   A O     1 
ATOM   1810  C  CB    . ILE   A  1  264  ? -48.445 61.333  69.045  1.00 15.10 ? 262  ILE   A CB    1 
ATOM   1811  C  CG1   . ILE   A  1  264  ? -47.062 61.972  69.121  1.00 16.19 ? 262  ILE   A CG1   1 
ATOM   1812  C  CG2   . ILE   A  1  264  ? -49.475 62.104  69.894  1.00 15.76 ? 262  ILE   A CG2   1 
ATOM   1813  C  CD1   . ILE   A  1  264  ? -47.032 63.388  68.556  1.00 17.53 ? 262  ILE   A CD1   1 
ATOM   1814  N  N     . SER   A  1  265  ? -46.968 59.794  71.422  1.00 13.27 ? 263  SER   A N     1 
ATOM   1815  C  CA    . SER   A  1  265  ? -46.645 59.866  72.833  1.00 13.99 ? 263  SER   A CA    1 
ATOM   1816  C  C     . SER   A  1  265  ? -45.911 61.167  73.081  1.00 15.11 ? 263  SER   A C     1 
ATOM   1817  O  O     . SER   A  1  265  ? -45.050 61.563  72.285  1.00 19.41 ? 263  SER   A O     1 
ATOM   1818  C  CB    . SER   A  1  265  ? -45.751 58.709  73.264  1.00 16.46 ? 263  SER   A CB    1 
ATOM   1819  O  OG    . SER   A  1  265  ? -46.466 57.488  73.284  1.00 17.84 ? 263  SER   A OG    1 
ATOM   1820  N  N     . ILE   A  1  266  ? -46.230 61.812  74.197  1.00 14.68 ? 264  ILE   A N     1 
ATOM   1821  C  CA    . ILE   A  1  266  ? -45.608 63.073  74.574  1.00 14.54 ? 264  ILE   A CA    1 
ATOM   1822  C  C     . ILE   A  1  266  ? -45.074 62.955  75.990  1.00 14.61 ? 264  ILE   A C     1 
ATOM   1823  O  O     . ILE   A  1  266  ? -45.520 62.128  76.785  1.00 14.85 ? 264  ILE   A O     1 
ATOM   1824  C  CB    . ILE   A  1  266  ? -46.562 64.276  74.468  1.00 14.32 ? 264  ILE   A CB    1 
ATOM   1825  C  CG1   . ILE   A  1  266  ? -47.694 64.169  75.490  1.00 16.09 ? 264  ILE   A CG1   1 
ATOM   1826  C  CG2   . ILE   A  1  266  ? -47.134 64.377  73.064  1.00 16.67 ? 264  ILE   A CG2   1 
ATOM   1827  C  CD1   . ILE   A  1  266  ? -48.504 65.452  75.636  1.00 17.77 ? 264  ILE   A CD1   1 
ATOM   1828  N  N     . LYS   A  1  267  ? -44.115 63.809  76.304  1.00 14.41 ? 265  LYS   A N     1 
ATOM   1829  C  CA    . LYS   A  1  267  ? -43.624 63.948  77.663  1.00 12.82 ? 265  LYS   A CA    1 
ATOM   1830  C  C     . LYS   A  1  267  ? -43.942 65.350  78.131  1.00 13.72 ? 265  LYS   A C     1 
ATOM   1831  O  O     . LYS   A  1  267  ? -43.625 66.328  77.447  1.00 14.37 ? 265  LYS   A O     1 
ATOM   1832  C  CB    . LYS   A  1  267  ? -42.119 63.708  77.739  1.00 16.51 ? 265  LYS   A CB    1 
ATOM   1833  C  CG    . LYS   A  1  267  ? -41.745 62.240  77.642  1.00 16.00 ? 265  LYS   A CG    1 
ATOM   1834  C  CD    . LYS   A  1  267  ? -40.232 62.062  77.679  1.00 18.93 ? 265  LYS   A CD    1 
ATOM   1835  C  CE    . LYS   A  1  267  ? -39.866 60.597  77.731  1.00 22.78 ? 265  LYS   A CE    1 
ATOM   1836  N  NZ    . LYS   A  1  267  ? -40.418 59.868  76.561  1.00 24.48 ? 265  LYS   A NZ    1 
ATOM   1837  N  N     . LEU   A  1  268  ? -44.599 65.451  79.283  1.00 13.51 ? 266  LEU   A N     1 
ATOM   1838  C  CA    . LEU   A  1  268  ? -44.943 66.768  79.786  1.00 14.25 ? 266  LEU   A CA    1 
ATOM   1839  C  C     . LEU   A  1  268  ? -43.708 67.623  80.019  1.00 14.70 ? 266  LEU   A C     1 
ATOM   1840  O  O     . LEU   A  1  268  ? -43.771 68.842  79.854  1.00 15.63 ? 266  LEU   A O     1 
ATOM   1841  C  CB    . LEU   A  1  268  ? -45.759 66.648  81.068  1.00 15.29 ? 266  LEU   A CB    1 
ATOM   1842  C  CG    . LEU   A  1  268  ? -47.112 65.961  80.861  1.00 15.97 ? 266  LEU   A CG    1 
ATOM   1843  C  CD1   . LEU   A  1  268  ? -47.879 65.910  82.167  1.00 16.97 ? 266  LEU   A CD1   1 
ATOM   1844  C  CD2   . LEU   A  1  268  ? -47.926 66.642  79.762  1.00 17.94 ? 266  LEU   A CD2   1 
ATOM   1845  N  N     . SER   A  1  269  ? -42.581 67.008  80.388  1.00 13.69 ? 267  SER   A N     1 
ATOM   1846  C  CA    . SER   A  1  269  ? -41.366 67.776  80.617  1.00 15.47 ? 267  SER   A CA    1 
ATOM   1847  C  C     . SER   A  1  269  ? -40.861 68.438  79.350  1.00 16.48 ? 267  SER   A C     1 
ATOM   1848  O  O     . SER   A  1  269  ? -40.077 69.384  79.439  1.00 16.49 ? 267  SER   A O     1 
ATOM   1849  C  CB    . SER   A  1  269  ? -40.269 66.892  81.208  1.00 16.21 ? 267  SER   A CB    1 
ATOM   1850  O  OG    . SER   A  1  269  ? -39.748 66.010  80.242  1.00 16.41 ? 267  SER   A OG    1 
ATOM   1851  N  N     . ALA   A  1  270  ? -41.275 67.956  78.176  1.00 14.37 ? 268  ALA   A N     1 
ATOM   1852  C  CA    . ALA   A  1  270  ? -40.877 68.614  76.939  1.00 14.89 ? 268  ALA   A CA    1 
ATOM   1853  C  C     . ALA   A  1  270  ? -41.639 69.906  76.719  1.00 14.84 ? 268  ALA   A C     1 
ATOM   1854  O  O     . ALA   A  1  270  ? -41.203 70.748  75.930  1.00 15.98 ? 268  ALA   A O     1 
ATOM   1855  C  CB    . ALA   A  1  270  ? -41.137 67.689  75.748  1.00 16.05 ? 268  ALA   A CB    1 
ATOM   1856  N  N     . LEU   A  1  271  ? -42.776 70.076  77.376  1.00 14.28 ? 269  LEU   A N     1 
ATOM   1857  C  CA    . LEU   A  1  271  ? -43.685 71.153  77.023  1.00 14.52 ? 269  LEU   A CA    1 
ATOM   1858  C  C     . LEU   A  1  271  ? -43.613 72.330  77.969  1.00 15.93 ? 269  LEU   A C     1 
ATOM   1859  O  O     . LEU   A  1  271  ? -44.317 73.320  77.761  1.00 16.61 ? 269  LEU   A O     1 
ATOM   1860  C  CB    . LEU   A  1  271  ? -45.112 70.634  76.927  1.00 15.76 ? 269  LEU   A CB    1 
ATOM   1861  C  CG    . LEU   A  1  271  ? -45.315 69.660  75.775  1.00 16.52 ? 269  LEU   A CG    1 
ATOM   1862  C  CD1   . LEU   A  1  271  ? -46.703 69.052  75.874  1.00 21.98 ? 269  LEU   A CD1   1 
ATOM   1863  C  CD2   . LEU   A  1  271  ? -45.170 70.423  74.484  1.00 19.18 ? 269  LEU   A CD2   1 
ATOM   1864  N  N     . HIS   A  1  272  ? -42.781 72.249  79.001  1.00 16.05 ? 270  HIS   A N     1 
ATOM   1865  C  CA    . HIS   A  1  272  ? -42.614 73.416  79.834  1.00 16.04 ? 270  HIS   A CA    1 
ATOM   1866  C  C     . HIS   A  1  272  ? -41.269 73.286  80.513  1.00 15.07 ? 270  HIS   A C     1 
ATOM   1867  O  O     . HIS   A  1  272  ? -40.936 72.195  80.984  1.00 16.26 ? 270  HIS   A O     1 
ATOM   1868  C  CB    . HIS   A  1  272  ? -43.702 73.502  80.896  1.00 15.79 ? 270  HIS   A CB    1 
ATOM   1869  C  CG    . HIS   A  1  272  ? -43.823 74.860  81.489  1.00 16.67 ? 270  HIS   A CG    1 
ATOM   1870  N  ND1   . HIS   A  1  272  ? -42.920 75.354  82.407  1.00 18.58 ? 270  HIS   A ND1   1 
ATOM   1871  C  CD2   . HIS   A  1  272  ? -44.732 75.841  81.285  1.00 19.87 ? 270  HIS   A CD2   1 
ATOM   1872  C  CE1   . HIS   A  1  272  ? -43.260 76.591  82.729  1.00 20.61 ? 270  HIS   A CE1   1 
ATOM   1873  N  NE2   . HIS   A  1  272  ? -44.360 76.906  82.068  1.00 21.42 ? 270  HIS   A NE2   1 
ATOM   1874  N  N     . PRO   A  1  273  ? -40.491 74.366  80.605  1.00 15.53 ? 271  PRO   A N     1 
ATOM   1875  C  CA    . PRO   A  1  273  ? -39.172 74.273  81.242  1.00 15.39 ? 271  PRO   A CA    1 
ATOM   1876  C  C     . PRO   A  1  273  ? -39.226 74.169  82.747  1.00 16.25 ? 271  PRO   A C     1 
ATOM   1877  O  O     . PRO   A  1  273  ? -38.194 73.869  83.356  1.00 17.15 ? 271  PRO   A O     1 
ATOM   1878  C  CB    . PRO   A  1  273  ? -38.487 75.574  80.814  1.00 16.22 ? 271  PRO   A CB    1 
ATOM   1879  C  CG    . PRO   A  1  273  ? -39.605 76.526  80.638  1.00 18.85 ? 271  PRO   A CG    1 
ATOM   1880  C  CD    . PRO   A  1  273  ? -40.737 75.705  80.045  1.00 16.74 ? 271  PRO   A CD    1 
ATOM   1881  N  N     . ARG   A  1  274  ? -40.381 74.390  83.368  1.00 14.33 ? 272  ARG   A N     1 
ATOM   1882  C  CA    . ARG   A  1  274  ? -40.495 74.309  84.822  1.00 14.47 ? 272  ARG   A CA    1 
ATOM   1883  C  C     . ARG   A  1  274  ? -41.609 73.359  85.217  1.00 16.63 ? 272  ARG   A C     1 
ATOM   1884  O  O     . ARG   A  1  274  ? -42.530 73.695  85.967  1.00 17.51 ? 272  ARG   A O     1 
ATOM   1885  C  CB    . ARG   A  1  274  ? -40.732 75.676  85.439  1.00 16.01 ? 272  ARG   A CB    1 
ATOM   1886  C  CG    . ARG   A  1  274  ? -39.587 76.651  85.214  1.00 16.41 ? 272  ARG   A CG    1 
ATOM   1887  C  CD    . ARG   A  1  274  ? -38.246 76.116  85.754  1.00 17.14 ? 272  ARG   A CD    1 
ATOM   1888  N  NE    . ARG   A  1  274  ? -38.326 75.715  87.153  1.00 17.89 ? 272  ARG   A NE    1 
ATOM   1889  C  CZ    . ARG   A  1  274  ? -38.281 76.555  88.178  1.00 17.40 ? 272  ARG   A CZ    1 
ATOM   1890  N  NH1   . ARG   A  1  274  ? -38.224 77.863  87.996  1.00 17.71 ? 272  ARG   A NH1   1 
ATOM   1891  N  NH2   . ARG   A  1  274  ? -38.274 76.068  89.414  1.00 18.31 ? 272  ARG   A NH2   1 
ATOM   1892  N  N     . TYR   A  1  275  ? -41.531 72.143  84.705  1.00 14.58 ? 273  TYR   A N     1 
ATOM   1893  C  CA    . TYR   A  1  275  ? -42.541 71.135  84.966  1.00 13.49 ? 273  TYR   A CA    1 
ATOM   1894  C  C     . TYR   A  1  275  ? -42.172 70.475  86.284  1.00 15.92 ? 273  TYR   A C     1 
ATOM   1895  O  O     . TYR   A  1  275  ? -41.372 69.545  86.341  1.00 15.68 ? 273  TYR   A O     1 
ATOM   1896  C  CB    . TYR   A  1  275  ? -42.610 70.157  83.800  1.00 15.35 ? 273  TYR   A CB    1 
ATOM   1897  C  CG    . TYR   A  1  275  ? -43.529 69.009  84.068  1.00 12.87 ? 273  TYR   A CG    1 
ATOM   1898  C  CD1   . TYR   A  1  275  ? -44.820 69.225  84.506  1.00 14.59 ? 273  TYR   A CD1   1 
ATOM   1899  C  CD2   . TYR   A  1  275  ? -43.095 67.706  83.900  1.00 13.76 ? 273  TYR   A CD2   1 
ATOM   1900  C  CE1   . TYR   A  1  275  ? -45.661 68.160  84.773  1.00 15.94 ? 273  TYR   A CE1   1 
ATOM   1901  C  CE2   . TYR   A  1  275  ? -43.923 66.637  84.162  1.00 14.36 ? 273  TYR   A CE2   1 
ATOM   1902  C  CZ    . TYR   A  1  275  ? -45.208 66.875  84.611  1.00 14.54 ? 273  TYR   A CZ    1 
ATOM   1903  O  OH    . TYR   A  1  275  ? -46.048 65.825  84.886  1.00 16.72 ? 273  TYR   A OH    1 
ATOM   1904  N  N     . SER   A  1  276  ? -42.754 70.985  87.362  1.00 13.70 ? 274  SER   A N     1 
ATOM   1905  C  CA    . SER   A  1  276  ? -42.473 70.458  88.685  1.00 12.63 ? 274  SER   A CA    1 
ATOM   1906  C  C     . SER   A  1  276  ? -43.577 70.891  89.623  1.00 15.34 ? 274  SER   A C     1 
ATOM   1907  O  O     . SER   A  1  276  ? -44.283 71.873  89.375  1.00 15.86 ? 274  SER   A O     1 
ATOM   1908  C  CB    . SER   A  1  276  ? -41.135 70.978  89.211  1.00 17.57 ? 274  SER   A CB    1 
ATOM   1909  O  OG    . SER   A  1  276  ? -41.245 72.356  89.510  1.00 21.67 ? 274  SER   A OG    1 
ATOM   1910  N  N     . ARG   A  1  277  ? -43.714 70.134  90.715  1.00 14.58 ? 275  ARG   A N     1 
ATOM   1911  C  CA    . ARG   A  1  277  ? -44.705 70.470  91.729  1.00 14.72 ? 275  ARG   A CA    1 
ATOM   1912  C  C     . ARG   A  1  277  ? -44.482 71.872  92.283  1.00 15.84 ? 275  ARG   A C     1 
ATOM   1913  O  O     . ARG   A  1  277  ? -45.440 72.588  92.576  1.00 16.21 ? 275  ARG   A O     1 
ATOM   1914  C  CB    . ARG   A  1  277  ? -44.690 69.425  92.849  1.00 16.13 ? 275  ARG   A CB    1 
ATOM   1915  C  CG    . ARG   A  1  277  ? -45.567 69.756  94.063  1.00 15.28 ? 275  ARG   A CG    1 
ATOM   1916  C  CD    . ARG   A  1  277  ? -47.028 69.972  93.674  1.00 16.51 ? 275  ARG   A CD    1 
ATOM   1917  N  NE    . ARG   A  1  277  ? -47.850 70.290  94.835  1.00 16.15 ? 275  ARG   A NE    1 
ATOM   1918  C  CZ    . ARG   A  1  277  ? -48.034 71.511  95.319  1.00 16.19 ? 275  ARG   A CZ    1 
ATOM   1919  N  NH1   . ARG   A  1  277  ? -47.414 72.563  94.804  1.00 16.01 ? 275  ARG   A NH1   1 
ATOM   1920  N  NH2   . ARG   A  1  277  ? -48.871 71.686  96.342  1.00 16.44 ? 275  ARG   A NH2   1 
ATOM   1921  N  N     . ALA   A  1  278  ? -43.221 72.289  92.419  1.00 15.82 ? 276  ALA   A N     1 
ATOM   1922  C  CA    . ALA   A  1  278  ? -42.955 73.612  92.980  1.00 16.73 ? 276  ALA   A CA    1 
ATOM   1923  C  C     . ALA   A  1  278  ? -43.519 74.710  92.099  1.00 14.83 ? 276  ALA   A C     1 
ATOM   1924  O  O     . ALA   A  1  278  ? -43.842 75.797  92.586  1.00 18.86 ? 276  ALA   A O     1 
ATOM   1925  C  CB    . ALA   A  1  278  ? -41.447 73.817  93.139  1.00 17.39 ? 276  ALA   A CB    1 
ATOM   1926  N  N     . GLN   A  1  279  ? -43.645 74.439  90.806  1.00 15.49 ? 277  GLN   A N     1 
ATOM   1927  C  CA    . GLN   A  1  279  ? -44.172 75.394  89.843  1.00 15.22 ? 277  GLN   A CA    1 
ATOM   1928  C  C     . GLN   A  1  279  ? -45.552 74.974  89.358  1.00 17.36 ? 277  GLN   A C     1 
ATOM   1929  O  O     . GLN   A  1  279  ? -45.918 75.239  88.213  1.00 15.59 ? 277  GLN   A O     1 
ATOM   1930  C  CB    . GLN   A  1  279  ? -43.213 75.529  88.661  1.00 15.95 ? 277  GLN   A CB    1 
ATOM   1931  C  CG    . GLN   A  1  279  ? -41.823 75.996  89.057  1.00 17.82 ? 277  GLN   A CG    1 
ATOM   1932  C  CD    . GLN   A  1  279  ? -41.853 77.379  89.643  1.00 20.61 ? 277  GLN   A CD    1 
ATOM   1933  O  OE1   . GLN   A  1  279  ? -42.592 78.248  89.184  1.00 29.55 ? 277  GLN   A OE1   1 
ATOM   1934  N  NE2   . GLN   A  1  279  ? -41.079 77.588  90.695  1.00 18.24 ? 277  GLN   A NE2   1 
ATOM   1935  N  N     . ALA   A  1  280  ? -46.325 74.317  90.221  1.00 16.49 ? 278  ALA   A N     1 
ATOM   1936  C  CA    . ALA   A  1  280  ? -47.589 73.731  89.779  1.00 17.30 ? 278  ALA   A CA    1 
ATOM   1937  C  C     . ALA   A  1  280  ? -48.512 74.772  89.167  1.00 16.29 ? 278  ALA   A C     1 
ATOM   1938  O  O     . ALA   A  1  280  ? -49.221 74.479  88.200  1.00 16.58 ? 278  ALA   A O     1 
ATOM   1939  C  CB    . ALA   A  1  280  ? -48.284 73.020  90.937  1.00 18.67 ? 278  ALA   A CB    1 
ATOM   1940  N  N     . ALA   A  1  281  ? -48.527 75.989  89.709  1.00 15.33 ? 279  ALA   A N     1 
ATOM   1941  C  CA    . ALA   A  1  281  ? -49.409 77.009  89.150  1.00 17.89 ? 279  ALA   A CA    1 
ATOM   1942  C  C     . ALA   A  1  281  ? -49.029 77.341  87.712  1.00 17.61 ? 279  ALA   A C     1 
ATOM   1943  O  O     . ALA   A  1  281  ? -49.901 77.470  86.840  1.00 18.00 ? 279  ALA   A O     1 
ATOM   1944  C  CB    . ALA   A  1  281  ? -49.422 78.264  90.026  1.00 20.90 ? 279  ALA   A CB    1 
ATOM   1945  N  N     . ARG   A  1  282  ? -47.732 77.453  87.432  1.00 16.35 ? 280  ARG   A N     1 
ATOM   1946  C  CA    . ARG   A  1  282  ? -47.318 77.683  86.054  1.00 16.21 ? 280  ARG   A CA    1 
ATOM   1947  C  C     . ARG   A  1  282  ? -47.618 76.475  85.185  1.00 15.54 ? 280  ARG   A C     1 
ATOM   1948  O  O     . ARG   A  1  282  ? -47.959 76.621  84.006  1.00 16.12 ? 280  ARG   A O     1 
ATOM   1949  C  CB    . ARG   A  1  282  ? -45.830 78.009  85.990  1.00 17.00 ? 280  ARG   A CB    1 
ATOM   1950  C  CG    . ARG   A  1  282  ? -45.469 79.346  86.591  1.00 19.61 ? 280  ARG   A CG    1 
ATOM   1951  C  CD    . ARG   A  1  282  ? -44.028 79.667  86.234  1.00 19.49 ? 280  ARG   A CD    1 
ATOM   1952  N  NE    . ARG   A  1  282  ? -43.900 79.817  84.791  1.00 19.31 ? 280  ARG   A NE    1 
ATOM   1953  C  CZ    . ARG   A  1  282  ? -42.753 79.800  84.128  1.00 18.98 ? 280  ARG   A CZ    1 
ATOM   1954  N  NH1   . ARG   A  1  282  ? -41.593 79.650  84.752  1.00 19.25 ? 280  ARG   A NH1   1 
ATOM   1955  N  NH2   . ARG   A  1  282  ? -42.766 79.950  82.805  1.00 19.25 ? 280  ARG   A NH2   1 
ATOM   1956  N  N     . VAL   A  1  283  ? -47.476 75.274  85.737  1.00 16.11 ? 281  VAL   A N     1 
ATOM   1957  C  CA    . VAL   A  1  283  ? -47.798 74.069  84.982  1.00 15.79 ? 281  VAL   A CA    1 
ATOM   1958  C  C     . VAL   A  1  283  ? -49.265 74.074  84.566  1.00 16.30 ? 281  VAL   A C     1 
ATOM   1959  O  O     . VAL   A  1  283  ? -49.596 73.866  83.391  1.00 15.96 ? 281  VAL   A O     1 
ATOM   1960  C  CB    . VAL   A  1  283  ? -47.438 72.822  85.805  1.00 14.65 ? 281  VAL   A CB    1 
ATOM   1961  C  CG1   . VAL   A  1  283  ? -48.001 71.586  85.148  1.00 16.96 ? 281  VAL   A CG1   1 
ATOM   1962  C  CG2   . VAL   A  1  283  ? -45.933 72.716  85.928  1.00 16.23 ? 281  VAL   A CG2   1 
ATOM   1963  N  N     . MET   A  1  284  ? -50.166 74.321  85.513  1.00 15.28 ? 282  MET   A N     1 
ATOM   1964  C  CA    . MET   A  1  284  ? -51.583 74.315  85.164  1.00 15.66 ? 282  MET   A CA    1 
ATOM   1965  C  C     . MET   A  1  284  ? -51.941 75.481  84.260  1.00 18.10 ? 282  MET   A C     1 
ATOM   1966  O  O     . MET   A  1  284  ? -52.828 75.355  83.407  1.00 20.06 ? 282  MET   A O     1 
ATOM   1967  C  CB    . MET   A  1  284  ? -52.433 74.359  86.426  1.00 16.93 ? 282  MET   A CB    1 
ATOM   1968  C  CG    . MET   A  1  284  ? -52.171 73.194  87.375  1.00 18.48 ? 282  MET   A CG    1 
ATOM   1969  S  SD    . MET   A  1  284  ? -52.339 71.579  86.586  1.00 20.18 ? 282  MET   A SD    1 
ATOM   1970  C  CE    . MET   A  1  284  ? -54.080 71.576  86.169  1.00 20.11 ? 282  MET   A CE    1 
ATOM   1971  N  N     . GLY   A  1  285  ? -51.264 76.618  84.417  1.00 15.87 ? 283  GLY   A N     1 
ATOM   1972  C  CA    . GLY   A  1  285  ? -51.621 77.783  83.632  1.00 17.33 ? 283  GLY   A CA    1 
ATOM   1973  C  C     . GLY   A  1  285  ? -51.013 77.792  82.250  1.00 17.21 ? 283  GLY   A C     1 
ATOM   1974  O  O     . GLY   A  1  285  ? -51.602 78.342  81.317  1.00 18.99 ? 283  GLY   A O     1 
ATOM   1975  N  N     . GLU   A  1  286  ? -49.844 77.192  82.091  1.00 16.17 ? 284  GLU   A N     1 
ATOM   1976  C  CA    . GLU   A  1  286  ? -49.064 77.331  80.872  1.00 16.76 ? 284  GLU   A CA    1 
ATOM   1977  C  C     . GLU   A  1  286  ? -48.850 76.019  80.153  1.00 16.37 ? 284  GLU   A C     1 
ATOM   1978  O  O     . GLU   A  1  286  ? -48.880 75.983  78.924  1.00 19.82 ? 284  GLU   A O     1 
ATOM   1979  C  CB    . GLU   A  1  286  ? -47.689 77.943  81.180  1.00 16.71 ? 284  GLU   A CB    1 
ATOM   1980  C  CG    . GLU   A  1  286  ? -47.770 79.294  81.853  1.00 20.58 ? 284  GLU   A CG    1 
ATOM   1981  C  CD    . GLU   A  1  286  ? -46.431 79.753  82.399  1.00 20.21 ? 284  GLU   A CD    1 
ATOM   1982  O  OE1   . GLU   A  1  286  ? -45.395 79.385  81.811  1.00 22.32 ? 284  GLU   A OE1   1 
ATOM   1983  O  OE2   . GLU   A  1  286  ? -46.424 80.487  83.414  1.00 24.01 ? 284  GLU   A OE2   1 
ATOM   1984  N  N     . LEU   A  1  287  ? -48.590 74.944  80.881  1.00 14.92 ? 285  LEU   A N     1 
ATOM   1985  C  CA    A LEU   A  1  287  ? -48.376 73.657  80.237  0.69 15.84 ? 285  LEU   A CA    1 
ATOM   1986  C  CA    B LEU   A  1  287  ? -48.379 73.655  80.240  0.31 15.88 ? 285  LEU   A CA    1 
ATOM   1987  C  C     . LEU   A  1  287  ? -49.704 73.026  79.836  1.00 16.74 ? 285  LEU   A C     1 
ATOM   1988  O  O     . LEU   A  1  287  ? -49.852 72.544  78.708  1.00 16.55 ? 285  LEU   A O     1 
ATOM   1989  C  CB    A LEU   A  1  287  ? -47.589 72.736  81.177  0.69 15.87 ? 285  LEU   A CB    1 
ATOM   1990  C  CB    B LEU   A  1  287  ? -47.602 72.730  81.178  0.31 15.89 ? 285  LEU   A CB    1 
ATOM   1991  C  CG    A LEU   A  1  287  ? -46.751 71.601  80.589  0.69 16.76 ? 285  LEU   A CG    1 
ATOM   1992  C  CG    B LEU   A  1  287  ? -47.689 71.233  80.898  0.31 16.99 ? 285  LEU   A CG    1 
ATOM   1993  C  CD1   A LEU   A  1  287  ? -45.930 70.970  81.684  0.69 16.59 ? 285  LEU   A CD1   1 
ATOM   1994  C  CD1   B LEU   A  1  287  ? -47.197 70.908  79.516  0.31 19.43 ? 285  LEU   A CD1   1 
ATOM   1995  C  CD2   A LEU   A  1  287  ? -47.629 70.555  79.977  0.69 18.71 ? 285  LEU   A CD2   1 
ATOM   1996  C  CD2   B LEU   A  1  287  ? -46.883 70.468  81.933  0.31 16.47 ? 285  LEU   A CD2   1 
ATOM   1997  N  N     . LEU   A  1  288  ? -50.673 73.016  80.745  1.00 16.37 ? 286  LEU   A N     1 
ATOM   1998  C  CA    . LEU   A  1  288  ? -51.977 72.420  80.463  1.00 15.88 ? 286  LEU   A CA    1 
ATOM   1999  C  C     . LEU   A  1  288  ? -52.597 72.905  79.157  1.00 18.00 ? 286  LEU   A C     1 
ATOM   2000  O  O     . LEU   A  1  288  ? -53.026 72.058  78.358  1.00 16.53 ? 286  LEU   A O     1 
ATOM   2001  C  CB    . LEU   A  1  288  ? -52.906 72.592  81.669  1.00 19.38 ? 286  LEU   A CB    1 
ATOM   2002  C  CG    . LEU   A  1  288  ? -54.367 72.217  81.422  1.00 22.56 ? 286  LEU   A CG    1 
ATOM   2003  C  CD1   . LEU   A  1  288  ? -54.498 70.720  81.155  1.00 21.18 ? 286  LEU   A CD1   1 
ATOM   2004  C  CD2   . LEU   A  1  288  ? -55.199 72.647  82.618  1.00 31.18 ? 286  LEU   A CD2   1 
ATOM   2005  N  N     . PRO   A  1  289  ? -52.662 74.204  78.859  1.00 16.14 ? 287  PRO   A N     1 
ATOM   2006  C  CA    . PRO   A  1  289  ? -53.265 74.607  77.577  1.00 16.31 ? 287  PRO   A CA    1 
ATOM   2007  C  C     . PRO   A  1  289  ? -52.534 74.059  76.379  1.00 16.07 ? 287  PRO   A C     1 
ATOM   2008  O  O     . PRO   A  1  289  ? -53.152 73.857  75.326  1.00 15.50 ? 287  PRO   A O     1 
ATOM   2009  C  CB    . PRO   A  1  289  ? -53.188 76.137  77.616  1.00 18.48 ? 287  PRO   A CB    1 
ATOM   2010  C  CG    . PRO   A  1  289  ? -53.181 76.466  79.070  1.00 22.95 ? 287  PRO   A CG    1 
ATOM   2011  C  CD    . PRO   A  1  289  ? -52.379 75.374  79.715  1.00 18.63 ? 287  PRO   A CD    1 
ATOM   2012  N  N     . ARG   A  1  290  ? -51.225 73.860  76.482  1.00 14.57 ? 288  ARG   A N     1 
ATOM   2013  C  CA    . ARG   A  1  290  ? -50.479 73.286  75.374  1.00 14.78 ? 288  ARG   A CA    1 
ATOM   2014  C  C     . ARG   A  1  290  ? -50.864 71.836  75.152  1.00 14.07 ? 288  ARG   A C     1 
ATOM   2015  O  O     . ARG   A  1  290  ? -51.064 71.412  74.005  1.00 14.92 ? 288  ARG   A O     1 
ATOM   2016  C  CB    . ARG   A  1  290  ? -48.979 73.433  75.614  1.00 15.15 ? 288  ARG   A CB    1 
ATOM   2017  C  CG    . ARG   A  1  290  ? -48.556 74.862  75.653  1.00 17.99 ? 288  ARG   A CG    1 
ATOM   2018  C  CD    . ARG   A  1  290  ? -47.116 74.999  76.101  1.00 21.27 ? 288  ARG   A CD    1 
ATOM   2019  N  NE    . ARG   A  1  290  ? -46.783 76.409  76.259  1.00 24.45 ? 288  ARG   A NE    1 
ATOM   2020  C  CZ    . ARG   A  1  290  ? -45.818 76.859  77.051  1.00 25.23 ? 288  ARG   A CZ    1 
ATOM   2021  N  NH1   . ARG   A  1  290  ? -45.044 76.032  77.735  1.00 21.98 ? 288  ARG   A NH1   1 
ATOM   2022  N  NH2   . ARG   A  1  290  ? -45.638 78.172  77.173  1.00 28.52 ? 288  ARG   A NH2   1 
ATOM   2023  N  N     . VAL   A  1  291  ? -50.957 71.055  76.231  1.00 14.12 ? 289  VAL   A N     1 
ATOM   2024  C  CA    . VAL   A  1  291  ? -51.430 69.681  76.091  1.00 14.26 ? 289  VAL   A CA    1 
ATOM   2025  C  C     . VAL   A  1  291  ? -52.839 69.666  75.531  1.00 14.56 ? 289  VAL   A C     1 
ATOM   2026  O  O     . VAL   A  1  291  ? -53.167 68.837  74.672  1.00 14.43 ? 289  VAL   A O     1 
ATOM   2027  C  CB    . VAL   A  1  291  ? -51.360 68.933  77.430  1.00 15.12 ? 289  VAL   A CB    1 
ATOM   2028  C  CG1   . VAL   A  1  291  ? -51.733 67.491  77.213  1.00 15.70 ? 289  VAL   A CG1   1 
ATOM   2029  C  CG2   . VAL   A  1  291  ? -49.982 69.039  77.991  1.00 17.77 ? 289  VAL   A CG2   1 
ATOM   2030  N  N     . LYS   A  1  292  ? -53.693 70.567  76.012  1.00 14.92 ? 290  LYS   A N     1 
ATOM   2031  C  CA    . LYS   A  1  292  ? -55.053 70.606  75.502  1.00 13.82 ? 290  LYS   A CA    1 
ATOM   2032  C  C     . LYS   A  1  292  ? -55.063 70.866  74.008  1.00 16.32 ? 290  LYS   A C     1 
ATOM   2033  O  O     . LYS   A  1  292  ? -55.807 70.220  73.264  1.00 14.25 ? 290  LYS   A O     1 
ATOM   2034  C  CB    . LYS   A  1  292  ? -55.861 71.674  76.218  1.00 14.89 ? 290  LYS   A CB    1 
ATOM   2035  C  CG    . LYS   A  1  292  ? -57.271 71.766  75.658  1.00 15.82 ? 290  LYS   A CG    1 
ATOM   2036  C  CD    . LYS   A  1  292  ? -58.129 72.779  76.365  1.00 17.25 ? 290  LYS   A CD    1 
ATOM   2037  C  CE    . LYS   A  1  292  ? -59.500 72.813  75.707  1.00 19.52 ? 290  LYS   A CE    1 
ATOM   2038  N  NZ    . LYS   A  1  292  ? -60.420 73.662  76.490  1.00 19.00 ? 290  LYS   A NZ    1 
ATOM   2039  N  N     . ALA   A  1  293  ? -54.232 71.800  73.541  1.00 13.89 ? 291  ALA   A N     1 
ATOM   2040  C  CA    . ALA   A  1  293  ? -54.230 72.103  72.115  1.00 13.87 ? 291  ALA   A CA    1 
ATOM   2041  C  C     . ALA   A  1  293  ? -53.770 70.899  71.302  1.00 13.10 ? 291  ALA   A C     1 
ATOM   2042  O  O     . ALA   A  1  293  ? -54.322 70.607  70.234  1.00 14.71 ? 291  ALA   A O     1 
ATOM   2043  C  CB    . ALA   A  1  293  ? -53.357 73.328  71.843  1.00 15.01 ? 291  ALA   A CB    1 
ATOM   2044  N  N     . LEU   A  1  294  ? -52.761 70.181  71.784  1.00 13.77 ? 292  LEU   A N     1 
ATOM   2045  C  CA    . LEU   A  1  294  ? -52.339 68.977  71.084  1.00 13.11 ? 292  LEU   A CA    1 
ATOM   2046  C  C     . LEU   A  1  294  ? -53.427 67.922  71.135  1.00 13.68 ? 292  LEU   A C     1 
ATOM   2047  O  O     . LEU   A  1  294  ? -53.692 67.245  70.138  1.00 13.20 ? 292  LEU   A O     1 
ATOM   2048  C  CB    . LEU   A  1  294  ? -51.062 68.441  71.716  1.00 14.21 ? 292  LEU   A CB    1 
ATOM   2049  C  CG    . LEU   A  1  294  ? -49.844 69.339  71.555  1.00 13.74 ? 292  LEU   A CG    1 
ATOM   2050  C  CD1   . LEU   A  1  294  ? -48.716 68.813  72.414  1.00 15.60 ? 292  LEU   A CD1   1 
ATOM   2051  C  CD2   . LEU   A  1  294  ? -49.423 69.433  70.092  1.00 16.40 ? 292  LEU   A CD2   1 
ATOM   2052  N  N     . ALA   A  1  295  ? -54.095 67.798  72.280  1.00 13.33 ? 293  ALA   A N     1 
ATOM   2053  C  CA    . ALA   A  1  295  ? -55.153 66.802  72.405  1.00 13.93 ? 293  ALA   A CA    1 
ATOM   2054  C  C     . ALA   A  1  295  ? -56.324 67.129  71.493  1.00 14.01 ? 293  ALA   A C     1 
ATOM   2055  O  O     . ALA   A  1  295  ? -56.923 66.223  70.911  1.00 14.42 ? 293  ALA   A O     1 
ATOM   2056  C  CB    . ALA   A  1  295  ? -55.606 66.714  73.857  1.00 14.60 ? 293  ALA   A CB    1 
ATOM   2057  N  N     . LEU   A  1  296  ? -56.657 68.410  71.352  1.00 12.86 ? 294  LEU   A N     1 
ATOM   2058  C  CA    . LEU   A  1  296  ? -57.723 68.785  70.430  1.00 13.62 ? 294  LEU   A CA    1 
ATOM   2059  C  C     . LEU   A  1  296  ? -57.395 68.351  69.013  1.00 14.68 ? 294  LEU   A C     1 
ATOM   2060  O  O     . LEU   A  1  296  ? -58.277 67.918  68.267  1.00 14.33 ? 294  LEU   A O     1 
ATOM   2061  C  CB    . LEU   A  1  296  ? -57.938 70.294  70.469  1.00 13.86 ? 294  LEU   A CB    1 
ATOM   2062  C  CG    . LEU   A  1  296  ? -58.645 70.798  71.724  1.00 14.86 ? 294  LEU   A CG    1 
ATOM   2063  C  CD1   . LEU   A  1  296  ? -58.594 72.312  71.769  1.00 16.33 ? 294  LEU   A CD1   1 
ATOM   2064  C  CD2   . LEU   A  1  296  ? -60.105 70.332  71.744  1.00 19.81 ? 294  LEU   A CD2   1 
ATOM   2065  N  N     . LEU   A  1  297  ? -56.129 68.462  68.619  1.00 13.94 ? 295  LEU   A N     1 
ATOM   2066  C  CA    . LEU   A  1  297  ? -55.760 68.042  67.276  1.00 14.71 ? 295  LEU   A CA    1 
ATOM   2067  C  C     . LEU   A  1  297  ? -55.800 66.526  67.157  1.00 14.08 ? 295  LEU   A C     1 
ATOM   2068  O  O     . LEU   A  1  297  ? -56.270 65.989  66.150  1.00 14.96 ? 295  LEU   A O     1 
ATOM   2069  C  CB    . LEU   A  1  297  ? -54.383 68.600  66.907  1.00 16.76 ? 295  LEU   A CB    1 
ATOM   2070  C  CG    . LEU   A  1  297  ? -54.014 68.468  65.428  1.00 18.82 ? 295  LEU   A CG    1 
ATOM   2071  C  CD1   . LEU   A  1  297  ? -54.969 69.228  64.510  1.00 22.57 ? 295  LEU   A CD1   1 
ATOM   2072  C  CD2   . LEU   A  1  297  ? -52.576 68.938  65.264  1.00 23.52 ? 295  LEU   A CD2   1 
ATOM   2073  N  N     . ALA   A  1  298  ? -55.333 65.819  68.185  1.00 13.09 ? 296  ALA   A N     1 
ATOM   2074  C  CA    . ALA   A  1  298  ? -55.435 64.368  68.167  1.00 14.20 ? 296  ALA   A CA    1 
ATOM   2075  C  C     . ALA   A  1  298  ? -56.892 63.933  68.099  1.00 15.15 ? 296  ALA   A C     1 
ATOM   2076  O  O     . ALA   A  1  298  ? -57.227 62.964  67.402  1.00 15.71 ? 296  ALA   A O     1 
ATOM   2077  C  CB    . ALA   A  1  298  ? -54.748 63.786  69.402  1.00 14.66 ? 296  ALA   A CB    1 
ATOM   2078  N  N     . LYS   A  1  299  ? -57.769 64.636  68.817  1.00 14.12 ? 297  LYS   A N     1 
ATOM   2079  C  CA    . LYS   A  1  299  ? -59.197 64.352  68.756  1.00 14.20 ? 297  LYS   A CA    1 
ATOM   2080  C  C     . LYS   A  1  299  ? -59.720 64.524  67.339  1.00 15.85 ? 297  LYS   A C     1 
ATOM   2081  O  O     . LYS   A  1  299  ? -60.479 63.683  66.846  1.00 16.26 ? 297  LYS   A O     1 
ATOM   2082  C  CB    . LYS   A  1  299  ? -59.941 65.277  69.711  1.00 14.20 ? 297  LYS   A CB    1 
ATOM   2083  C  CG    . LYS   A  1  299  ? -61.413 65.394  69.396  1.00 15.09 ? 297  LYS   A CG    1 
ATOM   2084  C  CD    . LYS   A  1  299  ? -62.170 66.197  70.442  1.00 17.77 ? 297  LYS   A CD    1 
ATOM   2085  C  CE    . LYS   A  1  299  ? -63.509 66.681  69.883  1.00 18.96 ? 297  LYS   A CE    1 
ATOM   2086  N  NZ    . LYS   A  1  299  ? -64.356 67.320  70.920  1.00 24.81 ? 297  LYS   A NZ    1 
ATOM   2087  N  N     . ASN   A  1  300  ? -59.311 65.592  66.654  1.00 15.17 ? 298  ASN   A N     1 
ATOM   2088  C  CA    . ASN   A  1  300  ? -59.857 65.805  65.324  1.00 14.11 ? 298  ASN   A CA    1 
ATOM   2089  C  C     . ASN   A  1  300  ? -59.453 64.700  64.354  1.00 16.32 ? 298  ASN   A C     1 
ATOM   2090  O  O     . ASN   A  1  300  ? -60.256 64.293  63.503  1.00 18.65 ? 298  ASN   A O     1 
ATOM   2091  C  CB    . ASN   A  1  300  ? -59.491 67.177  64.784  1.00 17.02 ? 298  ASN   A CB    1 
ATOM   2092  C  CG    . ASN   A  1  300  ? -60.306 67.523  63.563  1.00 24.01 ? 298  ASN   A CG    1 
ATOM   2093  O  OD1   . ASN   A  1  300  ? -61.464 67.955  63.669  1.00 28.73 ? 298  ASN   A OD1   1 
ATOM   2094  N  ND2   . ASN   A  1  300  ? -59.738 67.287  62.398  1.00 21.53 ? 298  ASN   A ND2   1 
ATOM   2095  N  N     . TYR   A  1  301  ? -58.215 64.220  64.442  1.00 14.20 ? 299  TYR   A N     1 
ATOM   2096  C  CA    . TYR   A  1  301  ? -57.784 63.101  63.615  1.00 15.72 ? 299  TYR   A CA    1 
ATOM   2097  C  C     . TYR   A  1  301  ? -58.185 61.750  64.184  1.00 16.13 ? 299  TYR   A C     1 
ATOM   2098  O  O     . TYR   A  1  301  ? -58.028 60.741  63.488  1.00 17.33 ? 299  TYR   A O     1 
ATOM   2099  C  CB    . TYR   A  1  301  ? -56.269 63.114  63.460  1.00 15.73 ? 299  TYR   A CB    1 
ATOM   2100  C  CG    . TYR   A  1  301  ? -55.735 64.198  62.567  1.00 15.23 ? 299  TYR   A CG    1 
ATOM   2101  C  CD1   . TYR   A  1  301  ? -55.930 64.151  61.192  1.00 17.29 ? 299  TYR   A CD1   1 
ATOM   2102  C  CD2   . TYR   A  1  301  ? -54.982 65.238  63.088  1.00 15.50 ? 299  TYR   A CD2   1 
ATOM   2103  C  CE1   . TYR   A  1  301  ? -55.386 65.121  60.365  1.00 16.99 ? 299  TYR   A CE1   1 
ATOM   2104  C  CE2   . TYR   A  1  301  ? -54.443 66.212  62.278  1.00 15.88 ? 299  TYR   A CE2   1 
ATOM   2105  C  CZ    . TYR   A  1  301  ? -54.658 66.156  60.913  1.00 17.96 ? 299  TYR   A CZ    1 
ATOM   2106  O  OH    . TYR   A  1  301  ? -54.108 67.119  60.091  1.00 18.55 ? 299  TYR   A OH    1 
ATOM   2107  N  N     . ASP   A  1  302  ? -58.691 61.716  65.418  1.00 14.57 ? 300  ASP   A N     1 
ATOM   2108  C  CA    . ASP   A  1  302  ? -59.035 60.490  66.137  1.00 14.19 ? 300  ASP   A CA    1 
ATOM   2109  C  C     . ASP   A  1  302  ? -57.843 59.540  66.241  1.00 15.46 ? 300  ASP   A C     1 
ATOM   2110  O  O     . ASP   A  1  302  ? -57.900 58.379  65.844  1.00 15.68 ? 300  ASP   A O     1 
ATOM   2111  C  CB    . ASP   A  1  302  ? -60.262 59.788  65.549  1.00 14.79 ? 300  ASP   A CB    1 
ATOM   2112  C  CG    . ASP   A  1  302  ? -60.918 58.866  66.543  1.00 20.09 ? 300  ASP   A CG    1 
ATOM   2113  O  OD1   . ASP   A  1  302  ? -60.866 59.176  67.758  1.00 18.32 ? 300  ASP   A OD1   1 
ATOM   2114  O  OD2   . ASP   A  1  302  ? -61.470 57.831  66.119  1.00 21.58 ? 300  ASP   A OD2   1 
ATOM   2115  N  N     . ILE   A  1  303  ? -56.753 60.058  66.801  1.00 14.07 ? 301  ILE   A N     1 
ATOM   2116  C  CA    . ILE   A  1  303  ? -55.566 59.268  67.096  1.00 14.72 ? 301  ILE   A CA    1 
ATOM   2117  C  C     . ILE   A  1  303  ? -55.318 59.282  68.597  1.00 14.77 ? 301  ILE   A C     1 
ATOM   2118  O  O     . ILE   A  1  303  ? -55.815 60.137  69.332  1.00 14.36 ? 301  ILE   A O     1 
ATOM   2119  C  CB    . ILE   A  1  303  ? -54.310 59.765  66.354  1.00 14.39 ? 301  ILE   A CB    1 
ATOM   2120  C  CG1   . ILE   A  1  303  ? -53.830 61.116  66.909  1.00 14.45 ? 301  ILE   A CG1   1 
ATOM   2121  C  CG2   . ILE   A  1  303  ? -54.585 59.874  64.863  1.00 16.15 ? 301  ILE   A CG2   1 
ATOM   2122  C  CD1   . ILE   A  1  303  ? -52.454 61.531  66.378  1.00 15.96 ? 301  ILE   A CD1   1 
ATOM   2123  N  N     . GLY   A  1  304  ? -54.531 58.312  69.047  1.00 14.55 ? 302  GLY   A N     1 
ATOM   2124  C  CA    . GLY   A  1  304  ? -54.149 58.274  70.447  1.00 15.01 ? 302  GLY   A CA    1 
ATOM   2125  C  C     . GLY   A  1  304  ? -53.121 59.349  70.750  1.00 14.78 ? 302  GLY   A C     1 
ATOM   2126  O  O     . GLY   A  1  304  ? -52.279 59.690  69.917  1.00 14.33 ? 302  GLY   A O     1 
ATOM   2127  N  N     . LEU   A  1  305  ? -53.219 59.913  71.947  1.00 13.22 ? 303  LEU   A N     1 
ATOM   2128  C  CA    . LEU   A  1  305  ? -52.214 60.832  72.470  1.00 13.39 ? 303  LEU   A CA    1 
ATOM   2129  C  C     . LEU   A  1  305  ? -51.898 60.371  73.883  1.00 14.21 ? 303  LEU   A C     1 
ATOM   2130  O  O     . LEU   A  1  305  ? -52.733 60.494  74.783  1.00 14.35 ? 303  LEU   A O     1 
ATOM   2131  C  CB    . LEU   A  1  305  ? -52.707 62.277  72.454  1.00 14.48 ? 303  LEU   A CB    1 
ATOM   2132  C  CG    . LEU   A  1  305  ? -51.668 63.324  72.880  1.00 18.70 ? 303  LEU   A CG    1 
ATOM   2133  C  CD1   . LEU   A  1  305  ? -51.921 64.635  72.177  1.00 21.41 ? 303  LEU   A CD1   1 
ATOM   2134  C  CD2   . LEU   A  1  305  ? -51.665 63.546  74.382  1.00 24.49 ? 303  LEU   A CD2   1 
ATOM   2135  N  N     . ASN   A  1  306  ? -50.693 59.854  74.080  1.00 13.75 ? 304  ASN   A N     1 
ATOM   2136  C  CA    . ASN   A  1  306  ? -50.309 59.242  75.337  1.00 13.71 ? 304  ASN   A CA    1 
ATOM   2137  C  C     . ASN   A  1  306  ? -49.365 60.167  76.086  1.00 13.18 ? 304  ASN   A C     1 
ATOM   2138  O  O     . ASN   A  1  306  ? -48.414 60.693  75.504  1.00 14.90 ? 304  ASN   A O     1 
ATOM   2139  C  CB    . ASN   A  1  306  ? -49.589 57.929  75.071  1.00 13.63 ? 304  ASN   A CB    1 
ATOM   2140  C  CG    . ASN   A  1  306  ? -48.954 57.379  76.312  1.00 15.75 ? 304  ASN   A CG    1 
ATOM   2141  O  OD1   . ASN   A  1  306  ? -47.753 57.558  76.556  1.00 18.64 ? 304  ASN   A OD1   1 
ATOM   2142  N  ND2   . ASN   A  1  306  ? -49.749 56.716  77.119  1.00 14.33 ? 304  ASN   A ND2   1 
ATOM   2143  N  N     . ILE   A  1  307  ? -49.602 60.326  77.384  1.00 13.55 ? 305  ILE   A N     1 
ATOM   2144  C  CA    . ILE   A  1  307  ? -48.684 61.047  78.263  1.00 15.01 ? 305  ILE   A CA    1 
ATOM   2145  C  C     . ILE   A  1  307  ? -47.725 60.040  78.885  1.00 13.95 ? 305  ILE   A C     1 
ATOM   2146  O  O     . ILE   A  1  307  ? -48.119 59.214  79.716  1.00 14.24 ? 305  ILE   A O     1 
ATOM   2147  C  CB    . ILE   A  1  307  ? -49.434 61.836  79.338  1.00 16.89 ? 305  ILE   A CB    1 
ATOM   2148  C  CG1   . ILE   A  1  307  ? -50.331 62.872  78.660  1.00 18.68 ? 305  ILE   A CG1   1 
ATOM   2149  C  CG2   . ILE   A  1  307  ? -48.429 62.490  80.310  1.00 17.77 ? 305  ILE   A CG2   1 
ATOM   2150  C  CD1   . ILE   A  1  307  ? -51.285 63.543  79.610  1.00 20.93 ? 305  ILE   A CD1   1 
ATOM   2151  N  N     . ASP   A  1  308  ? -46.459 60.103  78.479  1.00 14.21 ? 306  ASP   A N     1 
ATOM   2152  C  CA    . ASP   A  1  308  ? -45.427 59.238  79.026  1.00 13.76 ? 306  ASP   A CA    1 
ATOM   2153  C  C     . ASP   A  1  308  ? -45.191 59.583  80.490  1.00 13.85 ? 306  ASP   A C     1 
ATOM   2154  O  O     . ASP   A  1  308  ? -45.381 60.717  80.919  1.00 15.28 ? 306  ASP   A O     1 
ATOM   2155  C  CB    . ASP   A  1  308  ? -44.109 59.460  78.276  1.00 15.80 ? 306  ASP   A CB    1 
ATOM   2156  C  CG    . ASP   A  1  308  ? -44.094 58.842  76.892  1.00 18.96 ? 306  ASP   A CG    1 
ATOM   2157  O  OD1   . ASP   A  1  308  ? -45.014 58.077  76.550  1.00 18.41 ? 306  ASP   A OD1   1 
ATOM   2158  O  OD2   . ASP   A  1  308  ? -43.131 59.100  76.133  1.00 19.05 ? 306  ASP   A OD2   1 
ATOM   2159  N  N     . ALA   A  1  309  ? -44.793 58.587  81.265  1.00 13.00 ? 307  ALA   A N     1 
ATOM   2160  C  CA    . ALA   A  1  309  ? -44.509 58.804  82.673  1.00 13.46 ? 307  ALA   A CA    1 
ATOM   2161  C  C     . ALA   A  1  309  ? -43.025 59.068  82.875  1.00 14.29 ? 307  ALA   A C     1 
ATOM   2162  O  O     . ALA   A  1  309  ? -42.173 58.433  82.250  1.00 15.03 ? 307  ALA   A O     1 
ATOM   2163  C  CB    . ALA   A  1  309  ? -44.943 57.617  83.524  1.00 14.74 ? 307  ALA   A CB    1 
ATOM   2164  N  N     . GLU   A  1  310  ? -42.724 59.994  83.777  1.00 13.86 ? 308  GLU   A N     1 
ATOM   2165  C  CA    . GLU   A  1  310  ? -41.342 60.400  83.971  1.00 13.92 ? 308  GLU   A CA    1 
ATOM   2166  C  C     . GLU   A  1  310  ? -40.911 60.153  85.412  1.00 13.37 ? 308  GLU   A C     1 
ATOM   2167  O  O     . GLU   A  1  310  ? -41.183 59.082  85.959  1.00 14.79 ? 308  GLU   A O     1 
ATOM   2168  C  CB    . GLU   A  1  310  ? -41.195 61.846  83.508  1.00 14.62 ? 308  GLU   A CB    1 
ATOM   2169  C  CG    . GLU   A  1  310  ? -41.559 61.987  82.017  1.00 16.27 ? 308  GLU   A CG    1 
ATOM   2170  C  CD    . GLU   A  1  310  ? -41.302 63.370  81.477  1.00 16.07 ? 308  GLU   A CD    1 
ATOM   2171  O  OE1   . GLU   A  1  310  ? -40.117 63.672  81.217  1.00 18.07 ? 308  GLU   A OE1   1 
ATOM   2172  O  OE2   . GLU   A  1  310  ? -42.273 64.143  81.321  1.00 16.59 ? 308  GLU   A OE2   1 
ATOM   2173  N  N     . GLU   A  1  311  ? -40.245 61.114  86.039  1.00 14.58 ? 309  GLU   A N     1 
ATOM   2174  C  CA    . GLU   A  1  311  ? -39.721 60.869  87.375  1.00 14.93 ? 309  GLU   A CA    1 
ATOM   2175  C  C     . GLU   A  1  311  ? -40.847 60.773  88.392  1.00 13.96 ? 309  GLU   A C     1 
ATOM   2176  O  O     . GLU   A  1  311  ? -41.952 61.286  88.200  1.00 13.98 ? 309  GLU   A O     1 
ATOM   2177  C  CB    . GLU   A  1  311  ? -38.783 61.996  87.788  1.00 16.54 ? 309  GLU   A CB    1 
ATOM   2178  C  CG    . GLU   A  1  311  ? -37.508 62.095  86.949  1.00 17.38 ? 309  GLU   A CG    1 
ATOM   2179  C  CD    . GLU   A  1  311  ? -37.664 62.970  85.726  1.00 18.33 ? 309  GLU   A CD    1 
ATOM   2180  O  OE1   . GLU   A  1  311  ? -38.795 63.302  85.329  1.00 16.28 ? 309  GLU   A OE1   1 
ATOM   2181  O  OE2   . GLU   A  1  311  ? -36.621 63.340  85.140  1.00 24.51 ? 309  GLU   A OE2   1 
ATOM   2182  N  N     . ALA   A  1  312  ? -40.547 60.101  89.505  1.00 14.36 ? 310  ALA   A N     1 
ATOM   2183  C  CA    . ALA   A  1  312  ? -41.571 59.864  90.517  1.00 14.05 ? 310  ALA   A CA    1 
ATOM   2184  C  C     . ALA   A  1  312  ? -42.150 61.157  91.062  1.00 13.65 ? 310  ALA   A C     1 
ATOM   2185  O  O     . ALA   A  1  312  ? -43.332 61.199  91.412  1.00 14.87 ? 310  ALA   A O     1 
ATOM   2186  C  CB    . ALA   A  1  312  ? -40.984 59.039  91.665  1.00 14.33 ? 310  ALA   A CB    1 
ATOM   2187  N  N     . ASP   A  1  313  ? -41.353 62.221  91.140  1.00 14.96 ? 311  ASP   A N     1 
ATOM   2188  C  CA    . ASP   A  1  313  ? -41.864 63.466  91.703  1.00 15.36 ? 311  ASP   A CA    1 
ATOM   2189  C  C     . ASP   A  1  313  ? -42.748 64.241  90.738  1.00 14.38 ? 311  ASP   A C     1 
ATOM   2190  O  O     . ASP   A  1  313  ? -43.198 65.339  91.081  1.00 15.79 ? 311  ASP   A O     1 
ATOM   2191  C  CB    . ASP   A  1  313  ? -40.746 64.332  92.312  1.00 16.31 ? 311  ASP   A CB    1 
ATOM   2192  C  CG    . ASP   A  1  313  ? -39.781 64.879  91.278  1.00 19.40 ? 311  ASP   A CG    1 
ATOM   2193  O  OD1   . ASP   A  1  313  ? -39.949 64.623  90.064  1.00 18.10 ? 311  ASP   A OD1   1 
ATOM   2194  O  OD2   . ASP   A  1  313  ? -38.843 65.589  91.692  1.00 24.35 ? 311  ASP   A OD2   1 
ATOM   2195  N  N     . ARG   A  1  314  ? -43.001 63.695  89.557  1.00 13.55 ? 312  ARG   A N     1 
ATOM   2196  C  CA    . ARG   A  1  314  ? -43.901 64.304  88.595  1.00 14.32 ? 312  ARG   A CA    1 
ATOM   2197  C  C     . ARG   A  1  314  ? -45.187 63.516  88.436  1.00 14.56 ? 312  ARG   A C     1 
ATOM   2198  O  O     . ARG   A  1  314  ? -46.122 64.009  87.795  1.00 14.29 ? 312  ARG   A O     1 
ATOM   2199  C  CB    . ARG   A  1  314  ? -43.208 64.448  87.231  1.00 15.45 ? 312  ARG   A CB    1 
ATOM   2200  C  CG    . ARG   A  1  314  ? -42.225 65.587  87.227  1.00 17.08 ? 312  ARG   A CG    1 
ATOM   2201  C  CD    . ARG   A  1  314  ? -41.225 65.467  86.113  1.00 17.72 ? 312  ARG   A CD    1 
ATOM   2202  N  NE    . ARG   A  1  314  ? -40.642 66.770  85.834  1.00 17.76 ? 312  ARG   A NE    1 
ATOM   2203  C  CZ    . ARG   A  1  314  ? -39.652 66.969  84.977  1.00 15.59 ? 312  ARG   A CZ    1 
ATOM   2204  N  NH1   . ARG   A  1  314  ? -39.053 65.959  84.374  1.00 17.03 ? 312  ARG   A NH1   1 
ATOM   2205  N  NH2   . ARG   A  1  314  ? -39.258 68.215  84.721  1.00 18.01 ? 312  ARG   A NH2   1 
ATOM   2206  N  N     . LEU   A  1  315  ? -45.277 62.329  89.034  1.00 14.07 ? 313  LEU   A N     1 
ATOM   2207  C  CA    . LEU   A  1  315  ? -46.456 61.485  88.852  1.00 14.24 ? 313  LEU   A CA    1 
ATOM   2208  C  C     . LEU   A  1  315  ? -47.729 62.213  89.273  1.00 16.03 ? 313  LEU   A C     1 
ATOM   2209  O  O     . LEU   A  1  315  ? -48.673 62.361  88.488  1.00 15.20 ? 313  LEU   A O     1 
ATOM   2210  C  CB    . LEU   A  1  315  ? -46.275 60.213  89.674  1.00 15.22 ? 313  LEU   A CB    1 
ATOM   2211  C  CG    . LEU   A  1  315  ? -47.069 58.964  89.272  1.00 14.87 ? 313  LEU   A CG    1 
ATOM   2212  C  CD1   . LEU   A  1  315  ? -46.703 57.799  90.175  1.00 16.02 ? 313  LEU   A CD1   1 
ATOM   2213  C  CD2   . LEU   A  1  315  ? -48.570 59.177  89.313  1.00 19.15 ? 313  LEU   A CD2   1 
ATOM   2214  N  N     . GLU   A  1  316  ? -47.789 62.638  90.530  1.00 14.93 ? 314  GLU   A N     1 
ATOM   2215  C  CA    . GLU   A  1  316  ? -49.046 63.183  91.026  1.00 14.72 ? 314  GLU   A CA    1 
ATOM   2216  C  C     . GLU   A  1  316  ? -49.392 64.497  90.338  1.00 15.88 ? 314  GLU   A C     1 
ATOM   2217  O  O     . GLU   A  1  316  ? -50.564 64.754  90.038  1.00 15.74 ? 314  GLU   A O     1 
ATOM   2218  C  CB    . GLU   A  1  316  ? -49.022 63.275  92.549  1.00 16.29 ? 314  GLU   A CB    1 
ATOM   2219  C  CG    . GLU   A  1  316  ? -49.044 61.881  93.148  1.00 16.95 ? 314  GLU   A CG    1 
ATOM   2220  C  CD    . GLU   A  1  316  ? -49.031 61.872  94.653  1.00 16.39 ? 314  GLU   A CD    1 
ATOM   2221  O  OE1   . GLU   A  1  316  ? -49.778 62.667  95.249  1.00 17.96 ? 314  GLU   A OE1   1 
ATOM   2222  O  OE2   . GLU   A  1  316  ? -48.297 61.062  95.245  1.00 17.49 ? 314  GLU   A OE2   1 
ATOM   2223  N  N     . LEU   A  1  317  ? -48.386 65.316  90.038  1.00 15.66 ? 315  LEU   A N     1 
ATOM   2224  C  CA    . LEU   A  1  317  ? -48.634 66.533  89.275  1.00 15.60 ? 315  LEU   A CA    1 
ATOM   2225  C  C     . LEU   A  1  317  ? -49.284 66.213  87.934  1.00 16.37 ? 315  LEU   A C     1 
ATOM   2226  O  O     . LEU   A  1  317  ? -50.243 66.877  87.517  1.00 16.36 ? 315  LEU   A O     1 
ATOM   2227  C  CB    . LEU   A  1  317  ? -47.313 67.261  89.060  1.00 18.08 ? 315  LEU   A CB    1 
ATOM   2228  C  CG    . LEU   A  1  317  ? -47.435 68.540  88.247  1.00 18.28 ? 315  LEU   A CG    1 
ATOM   2229  C  CD1   . LEU   A  1  317  ? -48.419 69.512  88.900  1.00 21.51 ? 315  LEU   A CD1   1 
ATOM   2230  C  CD2   . LEU   A  1  317  ? -46.055 69.152  88.099  1.00 21.04 ? 315  LEU   A CD2   1 
ATOM   2231  N  N     . SER   A  1  318  ? -48.795 65.175  87.257  1.00 13.99 ? 316  SER   A N     1 
ATOM   2232  C  CA    . SER   A  1  318  ? -49.348 64.828  85.954  1.00 14.70 ? 316  SER   A CA    1 
ATOM   2233  C  C     . SER   A  1  318  ? -50.802 64.412  86.068  1.00 16.05 ? 316  SER   A C     1 
ATOM   2234  O  O     . SER   A  1  318  ? -51.567 64.595  85.115  1.00 15.08 ? 316  SER   A O     1 
ATOM   2235  C  CB    . SER   A  1  318  ? -48.528 63.726  85.285  1.00 13.57 ? 316  SER   A CB    1 
ATOM   2236  O  OG    . SER   A  1  318  ? -48.744 62.472  85.904  1.00 14.62 ? 316  SER   A OG    1 
ATOM   2237  N  N     . LEU   A  1  319  ? -51.195 63.852  87.212  1.00 15.09 ? 317  LEU   A N     1 
ATOM   2238  C  CA    . LEU   A  1  319  ? -52.593 63.482  87.416  1.00 14.40 ? 317  LEU   A CA    1 
ATOM   2239  C  C     . LEU   A  1  319  ? -53.492 64.699  87.423  1.00 16.36 ? 317  LEU   A C     1 
ATOM   2240  O  O     . LEU   A  1  319  ? -54.657 64.618  87.016  1.00 15.80 ? 317  LEU   A O     1 
ATOM   2241  C  CB    . LEU   A  1  319  ? -52.760 62.723  88.732  1.00 15.23 ? 317  LEU   A CB    1 
ATOM   2242  C  CG    . LEU   A  1  319  ? -52.070 61.363  88.798  1.00 16.19 ? 317  LEU   A CG    1 
ATOM   2243  C  CD1   . LEU   A  1  319  ? -52.270 60.752  90.182  1.00 17.33 ? 317  LEU   A CD1   1 
ATOM   2244  C  CD2   . LEU   A  1  319  ? -52.567 60.420  87.728  1.00 16.09 ? 317  LEU   A CD2   1 
ATOM   2245  N  N     . ASP   A  1  320  ? -52.985 65.838  87.880  1.00 16.03 ? 318  ASP   A N     1 
ATOM   2246  C  CA    . ASP   A  1  320  ? -53.803 67.041  87.832  1.00 17.13 ? 318  ASP   A CA    1 
ATOM   2247  C  C     . ASP   A  1  320  ? -54.059 67.480  86.403  1.00 16.77 ? 318  ASP   A C     1 
ATOM   2248  O  O     . ASP   A  1  320  ? -55.145 67.988  86.098  1.00 18.31 ? 318  ASP   A O     1 
ATOM   2249  C  CB    . ASP   A  1  320  ? -53.170 68.146  88.668  1.00 17.42 ? 318  ASP   A CB    1 
ATOM   2250  C  CG    . ASP   A  1  320  ? -53.349 67.905  90.138  1.00 20.22 ? 318  ASP   A CG    1 
ATOM   2251  O  OD1   . ASP   A  1  320  ? -54.526 67.760  90.555  1.00 22.05 ? 318  ASP   A OD1   1 
ATOM   2252  O  OD2   . ASP   A  1  320  ? -52.329 67.812  90.856  1.00 23.45 ? 318  ASP   A OD2   1 
ATOM   2253  N  N     . LEU   A  1  321  ? -53.093 67.275  85.507  1.00 14.97 ? 319  LEU   A N     1 
ATOM   2254  C  CA    . LEU   A  1  321  ? -53.343 67.592  84.109  1.00 16.25 ? 319  LEU   A CA    1 
ATOM   2255  C  C     . LEU   A  1  321  ? -54.289 66.579  83.494  1.00 15.33 ? 319  LEU   A C     1 
ATOM   2256  O  O     . LEU   A  1  321  ? -55.200 66.950  82.746  1.00 16.09 ? 319  LEU   A O     1 
ATOM   2257  C  CB    . LEU   A  1  321  ? -52.033 67.657  83.331  1.00 15.46 ? 319  LEU   A CB    1 
ATOM   2258  C  CG    . LEU   A  1  321  ? -51.229 68.932  83.555  1.00 20.01 ? 319  LEU   A CG    1 
ATOM   2259  C  CD1   . LEU   A  1  321  ? -50.348 68.793  84.772  1.00 23.30 ? 319  LEU   A CD1   1 
ATOM   2260  C  CD2   . LEU   A  1  321  ? -50.401 69.257  82.308  1.00 22.47 ? 319  LEU   A CD2   1 
ATOM   2261  N  N     . LEU   A  1  322  ? -54.095 65.299  83.806  1.00 16.25 ? 320  LEU   A N     1 
ATOM   2262  C  CA    . LEU   A  1  322  ? -54.980 64.277  83.263  1.00 16.10 ? 320  LEU   A CA    1 
ATOM   2263  C  C     . LEU   A  1  322  ? -56.411 64.530  83.692  1.00 16.24 ? 320  LEU   A C     1 
ATOM   2264  O  O     . LEU   A  1  322  ? -57.332 64.438  82.875  1.00 16.50 ? 320  LEU   A O     1 
ATOM   2265  C  CB    . LEU   A  1  322  ? -54.524 62.902  83.726  1.00 15.78 ? 320  LEU   A CB    1 
ATOM   2266  C  CG    . LEU   A  1  322  ? -55.356 61.740  83.188  1.00 17.24 ? 320  LEU   A CG    1 
ATOM   2267  C  CD1   . LEU   A  1  322  ? -55.127 61.530  81.704  1.00 17.95 ? 320  LEU   A CD1   1 
ATOM   2268  C  CD2   . LEU   A  1  322  ? -55.023 60.492  83.976  1.00 16.37 ? 320  LEU   A CD2   1 
ATOM   2269  N  N     . GLU   A  1  323  ? -56.609 64.911  84.954  1.00 14.64 ? 321  GLU   A N     1 
ATOM   2270  C  CA    . GLU   A  1  323  ? -57.951 65.191  85.467  1.00 16.82 ? 321  GLU   A CA    1 
ATOM   2271  C  C     . GLU   A  1  323  ? -58.606 66.322  84.691  1.00 16.94 ? 321  GLU   A C     1 
ATOM   2272  O  O     . GLU   A  1  323  ? -59.749 66.196  84.238  1.00 16.91 ? 321  GLU   A O     1 
ATOM   2273  C  CB    . GLU   A  1  323  ? -57.881 65.549  86.953  1.00 17.17 ? 321  GLU   A CB    1 
ATOM   2274  C  CG    . GLU   A  1  323  ? -59.184 66.115  87.530  1.00 22.62 ? 321  GLU   A CG    1 
ATOM   2275  C  CD    . GLU   A  1  323  ? -59.924 65.121  88.390  1.00 25.43 ? 321  GLU   A CD    1 
ATOM   2276  O  OE1   . GLU   A  1  323  ? -59.390 64.034  88.660  1.00 25.32 ? 321  GLU   A OE1   1 
ATOM   2277  O  OE2   . GLU   A  1  323  ? -61.070 65.420  88.793  1.00 28.80 ? 321  GLU   A OE2   1 
ATOM   2278  N  N     . VAL   A  1  324  ? -57.906 67.449  84.534  1.00 16.07 ? 322  VAL   A N     1 
ATOM   2279  C  CA    . VAL   A  1  324  ? -58.506 68.581  83.842  1.00 16.98 ? 322  VAL   A CA    1 
ATOM   2280  C  C     . VAL   A  1  324  ? -58.819 68.220  82.399  1.00 15.36 ? 322  VAL   A C     1 
ATOM   2281  O  O     . VAL   A  1  324  ? -59.895 68.550  81.883  1.00 16.75 ? 322  VAL   A O     1 
ATOM   2282  C  CB    . VAL   A  1  324  ? -57.608 69.827  83.935  1.00 19.07 ? 322  VAL   A CB    1 
ATOM   2283  C  CG1   . VAL   A  1  324  ? -58.208 70.958  83.098  1.00 19.88 ? 322  VAL   A CG1   1 
ATOM   2284  C  CG2   . VAL   A  1  324  ? -57.446 70.258  85.372  1.00 19.95 ? 322  VAL   A CG2   1 
ATOM   2285  N  N     . LEU   A  1  325  ? -57.892 67.534  81.726  1.00 14.69 ? 323  LEU   A N     1 
ATOM   2286  C  CA    . LEU   A  1  325  ? -58.114 67.196  80.321  1.00 14.38 ? 323  LEU   A CA    1 
ATOM   2287  C  C     . LEU   A  1  325  ? -59.308 66.271  80.165  1.00 14.73 ? 323  LEU   A C     1 
ATOM   2288  O  O     . LEU   A  1  325  ? -60.141 66.464  79.271  1.00 15.59 ? 323  LEU   A O     1 
ATOM   2289  C  CB    . LEU   A  1  325  ? -56.867 66.551  79.725  1.00 15.07 ? 323  LEU   A CB    1 
ATOM   2290  C  CG    . LEU   A  1  325  ? -55.671 67.500  79.642  1.00 15.83 ? 323  LEU   A CG    1 
ATOM   2291  C  CD1   . LEU   A  1  325  ? -54.393 66.708  79.488  1.00 17.69 ? 323  LEU   A CD1   1 
ATOM   2292  C  CD2   . LEU   A  1  325  ? -55.859 68.432  78.485  1.00 18.29 ? 323  LEU   A CD2   1 
ATOM   2293  N  N     . CYS   A  1  326  ? -59.400 65.253  81.013  1.00 15.66 ? 324  CYS   A N     1 
ATOM   2294  C  CA    . CYS   A  1  326  ? -60.500 64.306  80.887  1.00 14.45 ? 324  CYS   A CA    1 
ATOM   2295  C  C     . CYS   A  1  326  ? -61.845 64.919  81.231  1.00 18.33 ? 324  CYS   A C     1 
ATOM   2296  O  O     . CYS   A  1  326  ? -62.871 64.419  80.761  1.00 17.23 ? 324  CYS   A O     1 
ATOM   2297  C  CB    . CYS   A  1  326  ? -60.250 63.073  81.747  1.00 15.37 ? 324  CYS   A CB    1 
ATOM   2298  S  SG    . CYS   A  1  326  ? -58.920 62.068  81.085  1.00 18.15 ? 324  CYS   A SG    1 
ATOM   2299  N  N     . LEU   A  1  327  ? -61.866 65.977  82.026  1.00 15.53 ? 325  LEU   A N     1 
ATOM   2300  C  CA    . LEU   A  1  327  ? -63.100 66.654  82.378  1.00 15.57 ? 325  LEU   A CA    1 
ATOM   2301  C  C     . LEU   A  1  327  ? -63.409 67.819  81.452  1.00 15.48 ? 325  LEU   A C     1 
ATOM   2302  O  O     . LEU   A  1  327  ? -64.465 68.441  81.597  1.00 16.81 ? 325  LEU   A O     1 
ATOM   2303  C  CB    . LEU   A  1  327  ? -63.032 67.150  83.821  1.00 17.24 ? 325  LEU   A CB    1 
ATOM   2304  C  CG    . LEU   A  1  327  ? -62.929 66.038  84.868  1.00 20.09 ? 325  LEU   A CG    1 
ATOM   2305  C  CD1   . LEU   A  1  327  ? -62.804 66.647  86.264  1.00 22.95 ? 325  LEU   A CD1   1 
ATOM   2306  C  CD2   . LEU   A  1  327  ? -64.100 65.083  84.790  1.00 22.82 ? 325  LEU   A CD2   1 
ATOM   2307  N  N     . ASP   A  1  328  ? -62.537 68.114  80.494  1.00 16.12 ? 326  ASP   A N     1 
ATOM   2308  C  CA    . ASP   A  1  328  ? -62.716 69.262  79.618  1.00 15.22 ? 326  ASP   A CA    1 
ATOM   2309  C  C     . ASP   A  1  328  ? -63.653 68.876  78.483  1.00 16.50 ? 326  ASP   A C     1 
ATOM   2310  O  O     . ASP   A  1  328  ? -63.314 68.037  77.645  1.00 15.48 ? 326  ASP   A O     1 
ATOM   2311  C  CB    . ASP   A  1  328  ? -61.357 69.697  79.084  1.00 16.16 ? 326  ASP   A CB    1 
ATOM   2312  C  CG    . ASP   A  1  328  ? -61.419 71.008  78.350  1.00 20.12 ? 326  ASP   A CG    1 
ATOM   2313  O  OD1   . ASP   A  1  328  ? -62.404 71.263  77.633  1.00 19.67 ? 326  ASP   A OD1   1 
ATOM   2314  O  OD2   . ASP   A  1  328  ? -60.485 71.810  78.504  1.00 21.86 ? 326  ASP   A OD2   1 
ATOM   2315  N  N     . GLY   A  1  329  ? -64.828 69.502  78.449  1.00 15.29 ? 327  GLY   A N     1 
ATOM   2316  C  CA    . GLY   A  1  329  ? -65.823 69.164  77.445  1.00 17.24 ? 327  GLY   A CA    1 
ATOM   2317  C  C     . GLY   A  1  329  ? -65.354 69.353  76.021  1.00 18.25 ? 327  GLY   A C     1 
ATOM   2318  O  O     . GLY   A  1  329  ? -65.867 68.691  75.115  1.00 16.89 ? 327  GLY   A O     1 
ATOM   2319  N  N     . ASP   A  1  330  ? -64.371 70.230  75.793  1.00 16.04 ? 328  ASP   A N     1 
ATOM   2320  C  CA    . ASP   A  1  330  ? -63.892 70.438  74.432  1.00 16.72 ? 328  ASP   A CA    1 
ATOM   2321  C  C     . ASP   A  1  330  ? -63.238 69.191  73.860  1.00 14.66 ? 328  ASP   A C     1 
ATOM   2322  O  O     . ASP   A  1  330  ? -63.143 69.065  72.637  1.00 15.91 ? 328  ASP   A O     1 
ATOM   2323  C  CB    . ASP   A  1  330  ? -62.864 71.563  74.370  1.00 16.90 ? 328  ASP   A CB    1 
ATOM   2324  C  CG    . ASP   A  1  330  ? -63.467 72.914  74.633  1.00 23.12 ? 328  ASP   A CG    1 
ATOM   2325  O  OD1   . ASP   A  1  330  ? -64.692 73.083  74.455  1.00 25.42 ? 328  ASP   A OD1   1 
ATOM   2326  O  OD2   . ASP   A  1  330  ? -62.707 73.810  75.012  1.00 20.19 ? 328  ASP   A OD2   1 
ATOM   2327  N  N     . LEU   A  1  331  ? -62.804 68.267  74.712  1.00 13.71 ? 329  LEU   A N     1 
ATOM   2328  C  CA    . LEU   A  1  331  ? -62.179 67.033  74.264  1.00 16.25 ? 329  LEU   A CA    1 
ATOM   2329  C  C     . LEU   A  1  331  ? -63.146 65.871  74.242  1.00 15.89 ? 329  LEU   A C     1 
ATOM   2330  O  O     . LEU   A  1  331  ? -62.738 64.745  73.959  1.00 16.00 ? 329  LEU   A O     1 
ATOM   2331  C  CB    . LEU   A  1  331  ? -60.988 66.694  75.155  1.00 14.42 ? 329  LEU   A CB    1 
ATOM   2332  C  CG    . LEU   A  1  331  ? -59.778 67.609  74.951  1.00 16.08 ? 329  LEU   A CG    1 
ATOM   2333  C  CD1   . LEU   A  1  331  ? -58.766 67.390  76.054  1.00 16.32 ? 329  LEU   A CD1   1 
ATOM   2334  C  CD2   . LEU   A  1  331  ? -59.150 67.355  73.594  1.00 16.63 ? 329  LEU   A CD2   1 
ATOM   2335  N  N     . SER   A  1  332  ? -64.420 66.117  74.526  1.00 16.08 ? 330  SER   A N     1 
ATOM   2336  C  CA    . SER   A  1  332  ? -65.364 65.018  74.619  1.00 18.90 ? 330  SER   A CA    1 
ATOM   2337  C  C     . SER   A  1  332  ? -65.581 64.378  73.252  1.00 16.71 ? 330  SER   A C     1 
ATOM   2338  O  O     . SER   A  1  332  ? -65.413 65.007  72.204  1.00 18.93 ? 330  SER   A O     1 
ATOM   2339  C  CB    . SER   A  1  332  ? -66.691 65.498  75.197  1.00 18.88 ? 330  SER   A CB    1 
ATOM   2340  O  OG    . SER   A  1  332  ? -67.340 66.369  74.300  1.00 21.48 ? 330  SER   A OG    1 
ATOM   2341  N  N     . GLY   A  1  333  ? -65.931 63.098  73.275  1.00 15.89 ? 331  GLY   A N     1 
ATOM   2342  C  CA    . GLY   A  1  333  ? -66.135 62.350  72.059  1.00 16.68 ? 331  GLY   A CA    1 
ATOM   2343  C  C     . GLY   A  1  333  ? -64.912 61.609  71.589  1.00 16.43 ? 331  GLY   A C     1 
ATOM   2344  O  O     . GLY   A  1  333  ? -65.003 60.814  70.641  1.00 20.00 ? 331  GLY   A O     1 
ATOM   2345  N  N     . TRP   A  1  334  ? -63.776 61.829  72.231  1.00 15.65 ? 332  TRP   A N     1 
ATOM   2346  C  CA    . TRP   A  1  334  ? -62.515 61.234  71.828  1.00 16.07 ? 332  TRP   A CA    1 
ATOM   2347  C  C     . TRP   A  1  334  ? -61.988 60.419  72.990  1.00 14.12 ? 332  TRP   A C     1 
ATOM   2348  O  O     . TRP   A  1  334  ? -61.902 60.920  74.112  1.00 15.78 ? 332  TRP   A O     1 
ATOM   2349  C  CB    . TRP   A  1  334  ? -61.551 62.357  71.501  1.00 16.55 ? 332  TRP   A CB    1 
ATOM   2350  C  CG    . TRP   A  1  334  ? -60.115 61.987  71.327  1.00 14.93 ? 332  TRP   A CG    1 
ATOM   2351  C  CD1   . TRP   A  1  334  ? -59.571 61.227  70.330  1.00 13.59 ? 332  TRP   A CD1   1 
ATOM   2352  C  CD2   . TRP   A  1  334  ? -59.038 62.447  72.128  1.00 14.31 ? 332  TRP   A CD2   1 
ATOM   2353  N  NE1   . TRP   A  1  334  ? -58.198 61.172  70.478  1.00 14.61 ? 332  TRP   A NE1   1 
ATOM   2354  C  CE2   . TRP   A  1  334  ? -57.848 61.922  71.572  1.00 14.19 ? 332  TRP   A CE2   1 
ATOM   2355  C  CE3   . TRP   A  1  334  ? -58.953 63.254  73.269  1.00 16.08 ? 332  TRP   A CE3   1 
ATOM   2356  C  CZ2   . TRP   A  1  334  ? -56.592 62.166  72.126  1.00 15.26 ? 332  TRP   A CZ2   1 
ATOM   2357  C  CZ3   . TRP   A  1  334  ? -57.702 63.498  73.820  1.00 17.51 ? 332  TRP   A CZ3   1 
ATOM   2358  C  CH2   . TRP   A  1  334  ? -56.535 62.954  73.244  1.00 16.01 ? 332  TRP   A CH2   1 
ATOM   2359  N  N     . ASN   A  1  335  ? -61.639 59.162  72.719  1.00 13.78 ? 333  ASN   A N     1 
ATOM   2360  C  CA    . ASN   A  1  335  ? -61.128 58.253  73.736  1.00 14.42 ? 333  ASN   A CA    1 
ATOM   2361  C  C     . ASN   A  1  335  ? -59.632 58.019  73.586  1.00 15.12 ? 333  ASN   A C     1 
ATOM   2362  O  O     . ASN   A  1  335  ? -59.100 57.049  74.134  1.00 15.55 ? 333  ASN   A O     1 
ATOM   2363  C  CB    . ASN   A  1  335  ? -61.858 56.913  73.666  1.00 16.86 ? 333  ASN   A CB    1 
ATOM   2364  C  CG    . ASN   A  1  335  ? -63.197 56.940  74.345  1.00 18.51 ? 333  ASN   A CG    1 
ATOM   2365  O  OD1   . ASN   A  1  335  ? -63.437 57.729  75.259  1.00 16.44 ? 333  ASN   A OD1   1 
ATOM   2366  N  ND2   . ASN   A  1  335  ? -64.074 56.045  73.918  1.00 21.44 ? 333  ASN   A ND2   1 
ATOM   2367  N  N     . GLY   A  1  336  ? -58.955 58.881  72.830  1.00 14.73 ? 334  GLY   A N     1 
ATOM   2368  C  CA    . GLY   A  1  336  ? -57.549 58.676  72.553  1.00 13.58 ? 334  GLY   A CA    1 
ATOM   2369  C  C     . GLY   A  1  336  ? -56.586 59.159  73.610  1.00 14.37 ? 334  GLY   A C     1 
ATOM   2370  O  O     . GLY   A  1  336  ? -55.388 58.909  73.472  1.00 14.66 ? 334  GLY   A O     1 
ATOM   2371  N  N     . MET   A  1  337  ? -57.044 59.837  74.657  1.00 13.94 ? 335  MET   A N     1 
ATOM   2372  C  CA    A MET   A  1  337  ? -56.125 60.271  75.702  0.54 14.77 ? 335  MET   A CA    1 
ATOM   2373  C  CA    B MET   A  1  337  ? -56.118 60.268  75.694  0.46 14.78 ? 335  MET   A CA    1 
ATOM   2374  C  C     . MET   A  1  337  ? -55.546 59.059  76.419  1.00 14.20 ? 335  MET   A C     1 
ATOM   2375  O  O     . MET   A  1  337  ? -56.289 58.188  76.894  1.00 14.88 ? 335  MET   A O     1 
ATOM   2376  C  CB    A MET   A  1  337  ? -56.844 61.175  76.699  0.54 15.95 ? 335  MET   A CB    1 
ATOM   2377  C  CB    B MET   A  1  337  ? -56.810 61.192  76.686  0.46 15.93 ? 335  MET   A CB    1 
ATOM   2378  C  CG    A MET   A  1  337  ? -55.926 61.848  77.697  0.54 17.47 ? 335  MET   A CG    1 
ATOM   2379  C  CG    B MET   A  1  337  ? -55.973 61.505  77.903  0.46 18.26 ? 335  MET   A CG    1 
ATOM   2380  S  SD    A MET   A  1  337  ? -54.856 63.055  76.905  0.54 24.61 ? 335  MET   A SD    1 
ATOM   2381  S  SD    B MET   A  1  337  ? -56.013 63.260  78.246  0.46 19.37 ? 335  MET   A SD    1 
ATOM   2382  C  CE    A MET   A  1  337  ? -55.940 64.475  76.797  0.54 21.91 ? 335  MET   A CE    1 
ATOM   2383  C  CE    B MET   A  1  337  ? -55.242 63.879  76.758  0.46 15.73 ? 335  MET   A CE    1 
ATOM   2384  N  N     . GLY   A  1  338  ? -54.221 59.004  76.492  1.00 14.45 ? 336  GLY   A N     1 
ATOM   2385  C  CA    . GLY   A  1  338  ? -53.526 57.896  77.111  1.00 16.10 ? 336  GLY   A CA    1 
ATOM   2386  C  C     . GLY   A  1  338  ? -52.606 58.363  78.215  1.00 15.11 ? 336  GLY   A C     1 
ATOM   2387  O  O     . GLY   A  1  338  ? -52.211 59.531  78.255  1.00 13.95 ? 336  GLY   A O     1 
ATOM   2388  N  N     . PHE   A  1  339  ? -52.290 57.465  79.135  1.00 14.16 ? 337  PHE   A N     1 
ATOM   2389  C  CA    . PHE   A  1  339  ? -51.496 57.845  80.293  1.00 14.52 ? 337  PHE   A CA    1 
ATOM   2390  C  C     . PHE   A  1  339  ? -50.733 56.624  80.768  1.00 14.72 ? 337  PHE   A C     1 
ATOM   2391  O  O     . PHE   A  1  339  ? -51.310 55.541  80.907  1.00 14.55 ? 337  PHE   A O     1 
ATOM   2392  C  CB    . PHE   A  1  339  ? -52.453 58.317  81.386  1.00 13.67 ? 337  PHE   A CB    1 
ATOM   2393  C  CG    . PHE   A  1  339  ? -51.785 58.962  82.557  1.00 14.71 ? 337  PHE   A CG    1 
ATOM   2394  C  CD1   . PHE   A  1  339  ? -51.473 60.316  82.530  1.00 14.73 ? 337  PHE   A CD1   1 
ATOM   2395  C  CD2   . PHE   A  1  339  ? -51.479 58.224  83.688  1.00 14.53 ? 337  PHE   A CD2   1 
ATOM   2396  C  CE1   . PHE   A  1  339  ? -50.882 60.922  83.631  1.00 15.31 ? 337  PHE   A CE1   1 
ATOM   2397  C  CE2   . PHE   A  1  339  ? -50.883 58.821  84.793  1.00 16.42 ? 337  PHE   A CE2   1 
ATOM   2398  C  CZ    . PHE   A  1  339  ? -50.585 60.179  84.755  1.00 15.77 ? 337  PHE   A CZ    1 
ATOM   2399  N  N     . VAL   A  1  340  ? -49.440 56.794  80.999  1.00 14.11 ? 338  VAL   A N     1 
ATOM   2400  C  CA    . VAL   A  1  340  ? -48.589 55.708  81.462  1.00 14.19 ? 338  VAL   A CA    1 
ATOM   2401  C  C     . VAL   A  1  340  ? -48.593 55.652  82.976  1.00 12.88 ? 338  VAL   A C     1 
ATOM   2402  O  O     . VAL   A  1  340  ? -48.540 56.690  83.648  1.00 14.41 ? 338  VAL   A O     1 
ATOM   2403  C  CB    . VAL   A  1  340  ? -47.156 55.936  80.969  1.00 13.94 ? 338  VAL   A CB    1 
ATOM   2404  C  CG1   . VAL   A  1  340  ? -46.228 54.835  81.486  1.00 15.78 ? 338  VAL   A CG1   1 
ATOM   2405  C  CG2   . VAL   A  1  340  ? -47.150 55.999  79.455  1.00 15.22 ? 338  VAL   A CG2   1 
ATOM   2406  N  N     . VAL   A  1  341  ? -48.608 54.439  83.514  1.00 14.30 ? 339  VAL   A N     1 
ATOM   2407  C  CA    A VAL   A  1  341  ? -48.350 54.209  84.930  0.50 14.49 ? 339  VAL   A CA    1 
ATOM   2408  C  CA    B VAL   A  1  341  ? -48.355 54.205  84.929  0.50 14.49 ? 339  VAL   A CA    1 
ATOM   2409  C  C     . VAL   A  1  341  ? -47.213 53.209  85.057  1.00 15.35 ? 339  VAL   A C     1 
ATOM   2410  O  O     . VAL   A  1  341  ? -47.151 52.218  84.317  1.00 15.81 ? 339  VAL   A O     1 
ATOM   2411  C  CB    A VAL   A  1  341  ? -49.598 53.744  85.707  0.50 15.39 ? 339  VAL   A CB    1 
ATOM   2412  C  CB    B VAL   A  1  341  ? -49.603 53.706  85.680  0.50 15.37 ? 339  VAL   A CB    1 
ATOM   2413  C  CG1   A VAL   A  1  341  ? -50.675 54.814  85.647  0.50 15.99 ? 339  VAL   A CG1   1 
ATOM   2414  C  CG1   B VAL   A  1  341  ? -49.414 53.940  87.158  0.50 16.46 ? 339  VAL   A CG1   1 
ATOM   2415  C  CG2   A VAL   A  1  341  ? -50.107 52.430  85.165  0.50 17.15 ? 339  VAL   A CG2   1 
ATOM   2416  C  CG2   B VAL   A  1  341  ? -50.852 54.420  85.177  0.50 16.80 ? 339  VAL   A CG2   1 
ATOM   2417  N  N     . GLN   A  1  342  ? -46.313 53.478  85.999  1.00 14.46 ? 340  GLN   A N     1 
ATOM   2418  C  CA    . GLN   A  1  342  ? -45.074 52.722  86.165  1.00 14.73 ? 340  GLN   A CA    1 
ATOM   2419  C  C     . GLN   A  1  342  ? -45.240 51.735  87.312  1.00 14.81 ? 340  GLN   A C     1 
ATOM   2420  O  O     . GLN   A  1  342  ? -45.333 52.134  88.478  1.00 16.33 ? 340  GLN   A O     1 
ATOM   2421  C  CB    . GLN   A  1  342  ? -43.917 53.678  86.443  1.00 14.64 ? 340  GLN   A CB    1 
ATOM   2422  C  CG    . GLN   A  1  342  ? -43.657 54.653  85.292  1.00 14.03 ? 340  GLN   A CG    1 
ATOM   2423  C  CD    . GLN   A  1  342  ? -43.109 55.958  85.775  1.00 14.11 ? 340  GLN   A CD    1 
ATOM   2424  O  OE1   . GLN   A  1  342  ? -43.614 56.538  86.725  1.00 14.95 ? 340  GLN   A OE1   1 
ATOM   2425  N  NE2   . GLN   A  1  342  ? -42.065 56.446  85.111  1.00 14.29 ? 340  GLN   A NE2   1 
ATOM   2426  N  N     . ALA   A  1  343  ? -45.252 50.445  86.974  1.00 14.12 ? 341  ALA   A N     1 
ATOM   2427  C  CA    . ALA   A  1  343  ? -45.449 49.399  87.969  1.00 17.08 ? 341  ALA   A CA    1 
ATOM   2428  C  C     . ALA   A  1  343  ? -44.281 49.281  88.935  1.00 16.48 ? 341  ALA   A C     1 
ATOM   2429  O  O     . ALA   A  1  343  ? -44.427 48.649  89.985  1.00 16.76 ? 341  ALA   A O     1 
ATOM   2430  C  CB    . ALA   A  1  343  ? -45.668 48.063  87.275  1.00 18.44 ? 341  ALA   A CB    1 
ATOM   2431  N  N     . TYR   A  1  344  ? -43.120 49.849  88.606  1.00 15.02 ? 342  TYR   A N     1 
ATOM   2432  C  CA    . TYR   A  1  344  ? -42.062 49.848  89.603  1.00 14.92 ? 342  TYR   A CA    1 
ATOM   2433  C  C     . TYR   A  1  344  ? -42.333 50.816  90.736  1.00 17.30 ? 342  TYR   A C     1 
ATOM   2434  O  O     . TYR   A  1  344  ? -41.587 50.810  91.715  1.00 17.33 ? 342  TYR   A O     1 
ATOM   2435  C  CB    . TYR   A  1  344  ? -40.667 50.041  88.996  1.00 15.78 ? 342  TYR   A CB    1 
ATOM   2436  C  CG    . TYR   A  1  344  ? -40.240 51.415  88.496  1.00 14.74 ? 342  TYR   A CG    1 
ATOM   2437  C  CD1   . TYR   A  1  344  ? -41.087 52.515  88.468  1.00 15.23 ? 342  TYR   A CD1   1 
ATOM   2438  C  CD2   . TYR   A  1  344  ? -38.941 51.588  88.037  1.00 15.00 ? 342  TYR   A CD2   1 
ATOM   2439  C  CE1   . TYR   A  1  344  ? -40.645 53.737  87.973  1.00 15.63 ? 342  TYR   A CE1   1 
ATOM   2440  C  CE2   . TYR   A  1  344  ? -38.495 52.784  87.552  1.00 14.78 ? 342  TYR   A CE2   1 
ATOM   2441  C  CZ    . TYR   A  1  344  ? -39.331 53.859  87.534  1.00 14.80 ? 342  TYR   A CZ    1 
ATOM   2442  O  OH    . TYR   A  1  344  ? -38.843 55.042  87.039  1.00 14.65 ? 342  TYR   A OH    1 
ATOM   2443  N  N     . GLY   A  1  345  ? -43.390 51.616  90.639  1.00 15.73 ? 343  GLY   A N     1 
ATOM   2444  C  CA    . GLY   A  1  345  ? -43.697 52.615  91.636  1.00 16.50 ? 343  GLY   A CA    1 
ATOM   2445  C  C     . GLY   A  1  345  ? -44.694 52.076  92.644  1.00 16.51 ? 343  GLY   A C     1 
ATOM   2446  O  O     . GLY   A  1  345  ? -45.650 51.377  92.288  1.00 16.78 ? 343  GLY   A O     1 
ATOM   2447  N  N     . LYS   A  1  346  ? -44.468 52.431  93.907  1.00 16.76 ? 344  LYS   A N     1 
ATOM   2448  C  CA    . LYS   A  1  346  ? -45.313 51.932  94.982  1.00 16.27 ? 344  LYS   A CA    1 
ATOM   2449  C  C     . LYS   A  1  346  ? -46.736 52.463  94.902  1.00 17.96 ? 344  LYS   A C     1 
ATOM   2450  O  O     . LYS   A  1  346  ? -47.651 51.848  95.459  1.00 17.64 ? 344  LYS   A O     1 
ATOM   2451  C  CB    . LYS   A  1  346  ? -44.696 52.298  96.322  1.00 16.79 ? 344  LYS   A CB    1 
ATOM   2452  C  CG    . LYS   A  1  346  ? -43.334 51.687  96.502  1.00 18.32 ? 344  LYS   A CG    1 
ATOM   2453  C  CD    . LYS   A  1  346  ? -42.699 52.181  97.764  1.00 20.99 ? 344  LYS   A CD    1 
ATOM   2454  C  CE    . LYS   A  1  346  ? -41.477 51.363  98.044  1.00 19.30 ? 344  LYS   A CE    1 
ATOM   2455  N  NZ    . LYS   A  1  346  ? -40.727 51.939  99.189  1.00 20.75 ? 344  LYS   A NZ    1 
ATOM   2456  N  N     . ARG   A  1  347  ? -46.938 53.587  94.225  1.00 16.13 ? 345  ARG   A N     1 
ATOM   2457  C  CA    . ARG   A  1  347  ? -48.270 54.158  94.099  1.00 16.48 ? 345  ARG   A CA    1 
ATOM   2458  C  C     . ARG   A  1  347  ? -49.082 53.553  92.965  1.00 17.10 ? 345  ARG   A C     1 
ATOM   2459  O  O     . ARG   A  1  347  ? -50.280 53.829  92.892  1.00 16.39 ? 345  ARG   A O     1 
ATOM   2460  C  CB    . ARG   A  1  347  ? -48.162 55.668  93.914  1.00 16.87 ? 345  ARG   A CB    1 
ATOM   2461  C  CG    . ARG   A  1  347  ? -47.661 56.348  95.169  1.00 15.56 ? 345  ARG   A CG    1 
ATOM   2462  C  CD    . ARG   A  1  347  ? -47.248 57.763  94.873  1.00 14.82 ? 345  ARG   A CD    1 
ATOM   2463  N  NE    . ARG   A  1  347  ? -46.022 57.791  94.082  1.00 16.40 ? 345  ARG   A NE    1 
ATOM   2464  C  CZ    . ARG   A  1  347  ? -45.534 58.895  93.530  1.00 15.86 ? 345  ARG   A CZ    1 
ATOM   2465  N  NH1   . ARG   A  1  347  ? -46.137 60.064  93.679  1.00 16.61 ? 345  ARG   A NH1   1 
ATOM   2466  N  NH2   . ARG   A  1  347  ? -44.417 58.823  92.808  1.00 14.61 ? 345  ARG   A NH2   1 
ATOM   2467  N  N     . CYS   A  1  348  ? -48.487 52.715  92.120  1.00 16.22 ? 346  CYS   A N     1 
ATOM   2468  C  CA    . CYS   A  1  348  ? -49.117 52.264  90.882  1.00 16.39 ? 346  CYS   A CA    1 
ATOM   2469  C  C     . CYS   A  1  348  ? -50.566 51.794  91.029  1.00 17.00 ? 346  CYS   A C     1 
ATOM   2470  O  O     . CYS   A  1  348  ? -51.442 52.299  90.319  1.00 16.90 ? 346  CYS   A O     1 
ATOM   2471  C  CB    . CYS   A  1  348  ? -48.267 51.186  90.203  1.00 17.16 ? 346  CYS   A CB    1 
ATOM   2472  S  SG    . CYS   A  1  348  ? -48.731 50.935  88.494  1.00 20.17 ? 346  CYS   A SG    1 
ATOM   2473  N  N     . PRO   A  1  349  ? -50.873 50.832  91.900  1.00 16.98 ? 347  PRO   A N     1 
ATOM   2474  C  CA    . PRO   A  1  349  ? -52.272 50.383  91.983  1.00 17.01 ? 347  PRO   A CA    1 
ATOM   2475  C  C     . PRO   A  1  349  ? -53.223 51.485  92.404  1.00 16.02 ? 347  PRO   A C     1 
ATOM   2476  O  O     . PRO   A  1  349  ? -54.368 51.519  91.939  1.00 18.07 ? 347  PRO   A O     1 
ATOM   2477  C  CB    . PRO   A  1  349  ? -52.235 49.230  92.997  1.00 17.79 ? 347  PRO   A CB    1 
ATOM   2478  C  CG    . PRO   A  1  349  ? -50.978 49.391  93.733  1.00 19.25 ? 347  PRO   A CG    1 
ATOM   2479  C  CD    . PRO   A  1  349  ? -50.010 50.150  92.882  1.00 18.08 ? 347  PRO   A CD    1 
ATOM   2480  N  N     . PHE   A  1  350  ? -52.765 52.401  93.251  1.00 17.40 ? 348  PHE   A N     1 
ATOM   2481  C  CA    . PHE   A  1  350  ? -53.612 53.498  93.707  1.00 17.45 ? 348  PHE   A CA    1 
ATOM   2482  C  C     . PHE   A  1  350  ? -53.788 54.538  92.622  1.00 16.26 ? 348  PHE   A C     1 
ATOM   2483  O  O     . PHE   A  1  350  ? -54.856 55.151  92.513  1.00 17.46 ? 348  PHE   A O     1 
ATOM   2484  C  CB    . PHE   A  1  350  ? -53.004 54.097  94.970  1.00 18.16 ? 348  PHE   A CB    1 
ATOM   2485  C  CG    . PHE   A  1  350  ? -52.682 53.061  95.997  1.00 20.33 ? 348  PHE   A CG    1 
ATOM   2486  C  CD1   . PHE   A  1  350  ? -53.684 52.546  96.791  1.00 19.92 ? 348  PHE   A CD1   1 
ATOM   2487  C  CD2   . PHE   A  1  350  ? -51.402 52.551  96.119  1.00 20.03 ? 348  PHE   A CD2   1 
ATOM   2488  C  CE1   . PHE   A  1  350  ? -53.401 51.559  97.718  1.00 22.02 ? 348  PHE   A CE1   1 
ATOM   2489  C  CE2   . PHE   A  1  350  ? -51.116 51.555  97.043  1.00 21.33 ? 348  PHE   A CE2   1 
ATOM   2490  C  CZ    . PHE   A  1  350  ? -52.115 51.067  97.844  1.00 23.44 ? 348  PHE   A CZ    1 
ATOM   2491  N  N     . VAL   A  1  351  ? -52.762 54.722  91.795  1.00 15.65 ? 349  VAL   A N     1 
ATOM   2492  C  CA    . VAL   A  1  351  ? -52.893 55.573  90.621  1.00 15.00 ? 349  VAL   A CA    1 
ATOM   2493  C  C     . VAL   A  1  351  ? -53.904 54.975  89.658  1.00 16.86 ? 349  VAL   A C     1 
ATOM   2494  O  O     . VAL   A  1  351  ? -54.767 55.679  89.122  1.00 16.69 ? 349  VAL   A O     1 
ATOM   2495  C  CB    . VAL   A  1  351  ? -51.520 55.759  89.951  1.00 14.87 ? 349  VAL   A CB    1 
ATOM   2496  C  CG1   . VAL   A  1  351  ? -51.675 56.544  88.654  1.00 17.25 ? 349  VAL   A CG1   1 
ATOM   2497  C  CG2   . VAL   A  1  351  ? -50.572 56.474  90.893  1.00 18.93 ? 349  VAL   A CG2   1 
ATOM   2498  N  N     . LEU   A  1  352  ? -53.832 53.657  89.449  1.00 17.20 ? 350  LEU   A N     1 
ATOM   2499  C  CA    . LEU   A  1  352  ? -54.801 52.997  88.586  1.00 16.35 ? 350  LEU   A CA    1 
ATOM   2500  C  C     . LEU   A  1  352  ? -56.218 53.144  89.130  1.00 17.17 ? 350  LEU   A C     1 
ATOM   2501  O  O     . LEU   A  1  352  ? -57.155 53.381  88.361  1.00 18.16 ? 350  LEU   A O     1 
ATOM   2502  C  CB    . LEU   A  1  352  ? -54.429 51.527  88.406  1.00 16.90 ? 350  LEU   A CB    1 
ATOM   2503  C  CG    . LEU   A  1  352  ? -53.167 51.314  87.572  1.00 17.43 ? 350  LEU   A CG    1 
ATOM   2504  C  CD1   . LEU   A  1  352  ? -52.809 49.852  87.565  1.00 20.99 ? 350  LEU   A CD1   1 
ATOM   2505  C  CD2   . LEU   A  1  352  ? -53.403 51.803  86.158  1.00 19.48 ? 350  LEU   A CD2   1 
ATOM   2506  N  N     . ASP   A  1  353  ? -56.401 53.012  90.452  1.00 17.13 ? 351  ASP   A N     1 
ATOM   2507  C  CA    . ASP   A  1  353  ? -57.734 53.231  91.016  1.00 17.13 ? 351  ASP   A CA    1 
ATOM   2508  C  C     . ASP   A  1  353  ? -58.217 54.635  90.708  1.00 16.53 ? 351  ASP   A C     1 
ATOM   2509  O  O     . ASP   A  1  353  ? -59.387 54.841  90.371  1.00 17.08 ? 351  ASP   A O     1 
ATOM   2510  C  CB    . ASP   A  1  353  ? -57.720 53.041  92.532  1.00 17.09 ? 351  ASP   A CB    1 
ATOM   2511  C  CG    . ASP   A  1  353  ? -57.524 51.599  92.953  1.00 20.30 ? 351  ASP   A CG    1 
ATOM   2512  O  OD1   . ASP   A  1  353  ? -57.832 50.683  92.167  1.00 22.31 ? 351  ASP   A OD1   1 
ATOM   2513  O  OD2   . ASP   A  1  353  ? -57.064 51.401  94.092  1.00 23.62 ? 351  ASP   A OD2   1 
ATOM   2514  N  N     . PHE   A  1  354  ? -57.333 55.617  90.838  1.00 17.18 ? 352  PHE   A N     1 
ATOM   2515  C  CA    . PHE   A  1  354  ? -57.705 56.987  90.532  1.00 15.47 ? 352  PHE   A CA    1 
ATOM   2516  C  C     . PHE   A  1  354  ? -58.070 57.130  89.062  1.00 16.33 ? 352  PHE   A C     1 
ATOM   2517  O  O     . PHE   A  1  354  ? -59.070 57.766  88.720  1.00 16.61 ? 352  PHE   A O     1 
ATOM   2518  C  CB    . PHE   A  1  354  ? -56.556 57.931  90.891  1.00 17.35 ? 352  PHE   A CB    1 
ATOM   2519  C  CG    . PHE   A  1  354  ? -56.734 59.307  90.338  1.00 17.30 ? 352  PHE   A CG    1 
ATOM   2520  C  CD1   . PHE   A  1  354  ? -57.486 60.247  91.018  1.00 18.99 ? 352  PHE   A CD1   1 
ATOM   2521  C  CD2   . PHE   A  1  354  ? -56.182 59.649  89.115  1.00 19.29 ? 352  PHE   A CD2   1 
ATOM   2522  C  CE1   . PHE   A  1  354  ? -57.672 61.516  90.491  1.00 20.27 ? 352  PHE   A CE1   1 
ATOM   2523  C  CE2   . PHE   A  1  354  ? -56.368 60.908  88.586  1.00 19.29 ? 352  PHE   A CE2   1 
ATOM   2524  C  CZ    . PHE   A  1  354  ? -57.113 61.842  89.270  1.00 19.11 ? 352  PHE   A CZ    1 
ATOM   2525  N  N     . ILE   A  1  355  ? -57.253 56.562  88.172  1.00 15.62 ? 353  ILE   A N     1 
ATOM   2526  C  CA    . ILE   A  1  355  ? -57.497 56.708  86.738  1.00 14.88 ? 353  ILE   A CA    1 
ATOM   2527  C  C     . ILE   A  1  355  ? -58.783 56.011  86.335  1.00 19.32 ? 353  ILE   A C     1 
ATOM   2528  O  O     . ILE   A  1  355  ? -59.558 56.537  85.536  1.00 17.21 ? 353  ILE   A O     1 
ATOM   2529  C  CB    . ILE   A  1  355  ? -56.310 56.174  85.928  1.00 16.03 ? 353  ILE   A CB    1 
ATOM   2530  C  CG1   . ILE   A  1  355  ? -55.084 57.056  86.144  1.00 16.84 ? 353  ILE   A CG1   1 
ATOM   2531  C  CG2   . ILE   A  1  355  ? -56.677 56.105  84.452  1.00 17.91 ? 353  ILE   A CG2   1 
ATOM   2532  C  CD1   . ILE   A  1  355  ? -53.816 56.450  85.584  1.00 16.87 ? 353  ILE   A CD1   1 
ATOM   2533  N  N     . ILE   A  1  356  ? -58.992 54.790  86.824  1.00 17.24 ? 354  ILE   A N     1 
ATOM   2534  C  CA    . ILE   A  1  356  ? -60.218 54.075  86.492  1.00 16.55 ? 354  ILE   A CA    1 
ATOM   2535  C  C     . ILE   A  1  356  ? -61.432 54.866  86.949  1.00 17.12 ? 354  ILE   A C     1 
ATOM   2536  O  O     . ILE   A  1  356  ? -62.409 55.013  86.209  1.00 17.53 ? 354  ILE   A O     1 
ATOM   2537  C  CB    . ILE   A  1  356  ? -60.172 52.655  87.083  1.00 18.59 ? 354  ILE   A CB    1 
ATOM   2538  C  CG1   . ILE   A  1  356  ? -59.135 51.822  86.324  1.00 18.55 ? 354  ILE   A CG1   1 
ATOM   2539  C  CG2   . ILE   A  1  356  ? -61.557 52.017  87.076  1.00 19.97 ? 354  ILE   A CG2   1 
ATOM   2540  C  CD1   . ILE   A  1  356  ? -58.681 50.588  87.087  1.00 19.72 ? 354  ILE   A CD1   1 
ATOM   2541  N  N     . ASP   A  1  357  ? -61.368 55.434  88.150  1.00 17.17 ? 355  ASP   A N     1 
ATOM   2542  C  CA    . ASP   A  1  357  ? -62.468 56.266  88.613  1.00 16.62 ? 355  ASP   A CA    1 
ATOM   2543  C  C     . ASP   A  1  357  ? -62.620 57.522  87.762  1.00 16.82 ? 355  ASP   A C     1 
ATOM   2544  O  O     . ASP   A  1  357  ? -63.746 57.932  87.450  1.00 17.55 ? 355  ASP   A O     1 
ATOM   2545  C  CB    . ASP   A  1  357  ? -62.269 56.629  90.077  1.00 19.53 ? 355  ASP   A CB    1 
ATOM   2546  C  CG    . ASP   A  1  357  ? -63.303 57.614  90.556  1.00 19.19 ? 355  ASP   A CG    1 
ATOM   2547  O  OD1   . ASP   A  1  357  ? -64.442 57.176  90.825  1.00 23.76 ? 355  ASP   A OD1   1 
ATOM   2548  O  OD2   . ASP   A  1  357  ? -63.002 58.820  90.618  1.00 20.36 ? 355  ASP   A OD2   1 
ATOM   2549  N  N     . LEU   A  1  358  ? -61.506 58.141  87.367  1.00 17.50 ? 356  LEU   A N     1 
ATOM   2550  C  CA    . LEU   A  1  358  ? -61.585 59.301  86.486  1.00 15.63 ? 356  LEU   A CA    1 
ATOM   2551  C  C     . LEU   A  1  358  ? -62.207 58.926  85.151  1.00 15.74 ? 356  LEU   A C     1 
ATOM   2552  O  O     . LEU   A  1  358  ? -63.018 59.678  84.599  1.00 16.47 ? 356  LEU   A O     1 
ATOM   2553  C  CB    . LEU   A  1  358  ? -60.190 59.875  86.256  1.00 14.19 ? 356  LEU   A CB    1 
ATOM   2554  C  CG    . LEU   A  1  358  ? -60.119 61.020  85.257  1.00 14.59 ? 356  LEU   A CG    1 
ATOM   2555  C  CD1   . LEU   A  1  358  ? -60.967 62.198  85.707  1.00 18.03 ? 356  LEU   A CD1   1 
ATOM   2556  C  CD2   . LEU   A  1  358  ? -58.638 61.435  85.095  1.00 16.42 ? 356  LEU   A CD2   1 
ATOM   2557  N  N     . ALA   A  1  359  ? -61.859 57.751  84.623  1.00 16.65 ? 357  ALA   A N     1 
ATOM   2558  C  CA    . ALA   A  1  359  ? -62.475 57.298  83.385  1.00 16.38 ? 357  ALA   A CA    1 
ATOM   2559  C  C     . ALA   A  1  359  ? -63.976 57.137  83.560  1.00 15.85 ? 357  ALA   A C     1 
ATOM   2560  O  O     . ALA   A  1  359  ? -64.747 57.484  82.666  1.00 17.45 ? 357  ALA   A O     1 
ATOM   2561  C  CB    . ALA   A  1  359  ? -61.842 55.982  82.934  1.00 18.61 ? 357  ALA   A CB    1 
ATOM   2562  N  N     . ARG   A  1  360  ? -64.407 56.606  84.705  1.00 17.14 ? 358  ARG   A N     1 
ATOM   2563  C  CA    . ARG   A  1  360  ? -65.837 56.465  84.953  1.00 18.52 ? 358  ARG   A CA    1 
ATOM   2564  C  C     . ARG   A  1  360  ? -66.513 57.827  85.053  1.00 19.22 ? 358  ARG   A C     1 
ATOM   2565  O  O     . ARG   A  1  360  ? -67.561 58.058  84.439  1.00 20.89 ? 358  ARG   A O     1 
ATOM   2566  C  CB    . ARG   A  1  360  ? -66.061 55.663  86.235  1.00 19.68 ? 358  ARG   A CB    1 
ATOM   2567  C  CG    . ARG   A  1  360  ? -65.654 54.200  86.144  1.00 22.85 ? 358  ARG   A CG    1 
ATOM   2568  C  CD    . ARG   A  1  360  ? -66.191 53.392  87.334  1.00 26.22 ? 358  ARG   A CD    1 
ATOM   2569  N  NE    . ARG   A  1  360  ? -65.455 52.142  87.489  1.00 31.39 ? 358  ARG   A NE    1 
ATOM   2570  C  CZ    . ARG   A  1  360  ? -65.702 51.037  86.799  1.00 37.63 ? 358  ARG   A CZ    1 
ATOM   2571  N  NH1   . ARG   A  1  360  ? -66.704 50.971  85.934  1.00 40.69 ? 358  ARG   A NH1   1 
ATOM   2572  N  NH2   . ARG   A  1  360  ? -64.920 49.973  86.975  1.00 32.83 ? 358  ARG   A NH2   1 
ATOM   2573  N  N     . ARG   A  1  361  ? -65.926 58.744  85.823  1.00 19.39 ? 359  ARG   A N     1 
ATOM   2574  C  CA    . ARG   A  1  361  ? -66.527 60.062  86.014  1.00 18.74 ? 359  ARG   A CA    1 
ATOM   2575  C  C     . ARG   A  1  361  ? -66.592 60.836  84.710  1.00 19.22 ? 359  ARG   A C     1 
ATOM   2576  O  O     . ARG   A  1  361  ? -67.589 61.509  84.425  1.00 21.19 ? 359  ARG   A O     1 
ATOM   2577  C  CB    . ARG   A  1  361  ? -65.696 60.863  87.016  1.00 22.27 ? 359  ARG   A CB    1 
ATOM   2578  C  CG    . ARG   A  1  361  ? -65.804 60.395  88.445  1.00 24.35 ? 359  ARG   A CG    1 
ATOM   2579  C  CD    . ARG   A  1  361  ? -65.115 61.391  89.355  1.00 23.27 ? 359  ARG   A CD    1 
ATOM   2580  N  NE    . ARG   A  1  361  ? -63.661 61.272  89.339  1.00 23.20 ? 359  ARG   A NE    1 
ATOM   2581  C  CZ    . ARG   A  1  361  ? -62.819 62.257  89.058  1.00 22.31 ? 359  ARG   A CZ    1 
ATOM   2582  N  NH1   . ARG   A  1  361  ? -63.244 63.434  88.630  1.00 21.11 ? 359  ARG   A NH1   1 
ATOM   2583  N  NH2   . ARG   A  1  361  ? -61.516 62.066  89.235  1.00 20.10 ? 359  ARG   A NH2   1 
ATOM   2584  N  N     . SER   A  1  362  ? -65.528 60.780  83.917  1.00 17.87 ? 360  SER   A N     1 
ATOM   2585  C  CA    . SER   A  1  362  ? -65.483 61.562  82.694  1.00 16.96 ? 360  SER   A CA    1 
ATOM   2586  C  C     . SER   A  1  362  ? -66.153 60.860  81.529  1.00 17.19 ? 360  SER   A C     1 
ATOM   2587  O  O     . SER   A  1  362  ? -66.468 61.507  80.526  1.00 17.99 ? 360  SER   A O     1 
ATOM   2588  C  CB    . SER   A  1  362  ? -64.019 61.814  82.321  1.00 18.64 ? 360  SER   A CB    1 
ATOM   2589  O  OG    . SER   A  1  362  ? -63.372 60.591  81.971  1.00 16.89 ? 360  SER   A OG    1 
ATOM   2590  N  N     . GLY   A  1  363  ? -66.348 59.551  81.627  1.00 17.82 ? 361  GLY   A N     1 
ATOM   2591  C  CA    . GLY   A  1  363  ? -66.816 58.798  80.489  1.00 19.90 ? 361  GLY   A CA    1 
ATOM   2592  C  C     . GLY   A  1  363  ? -65.803 58.626  79.384  1.00 20.94 ? 361  GLY   A C     1 
ATOM   2593  O  O     . GLY   A  1  363  ? -66.182 58.214  78.282  1.00 21.23 ? 361  GLY   A O     1 
ATOM   2594  N  N     . ARG   A  1  364  ? -64.535 58.952  79.637  1.00 18.22 ? 362  ARG   A N     1 
ATOM   2595  C  CA    . ARG   A  1  364  ? -63.457 58.772  78.670  1.00 19.30 ? 362  ARG   A CA    1 
ATOM   2596  C  C     . ARG   A  1  364  ? -62.823 57.418  78.933  1.00 17.68 ? 362  ARG   A C     1 
ATOM   2597  O  O     . ARG   A  1  364  ? -62.443 57.117  80.068  1.00 18.56 ? 362  ARG   A O     1 
ATOM   2598  C  CB    . ARG   A  1  364  ? -62.368 59.827  78.865  1.00 21.06 ? 362  ARG   A CB    1 
ATOM   2599  C  CG    . ARG   A  1  364  ? -62.824 61.273  78.911  1.00 24.40 ? 362  ARG   A CG    1 
ATOM   2600  C  CD    . ARG   A  1  364  ? -62.844 61.919  77.552  1.00 18.31 ? 362  ARG   A CD    1 
ATOM   2601  N  NE    . ARG   A  1  364  ? -63.655 63.126  77.611  1.00 17.25 ? 362  ARG   A NE    1 
ATOM   2602  C  CZ    . ARG   A  1  364  ? -63.173 64.354  77.748  1.00 16.74 ? 362  ARG   A CZ    1 
ATOM   2603  N  NH1   . ARG   A  1  364  ? -61.871 64.593  77.712  1.00 16.50 ? 362  ARG   A NH1   1 
ATOM   2604  N  NH2   . ARG   A  1  364  ? -64.019 65.366  77.920  1.00 16.85 ? 362  ARG   A NH2   1 
ATOM   2605  N  N     . ARG   A  1  365  ? -62.693 56.615  77.887  1.00 16.74 ? 363  ARG   A N     1 
ATOM   2606  C  CA    . ARG   A  1  365  ? -62.051 55.314  78.034  1.00 16.36 ? 363  ARG   A CA    1 
ATOM   2607  C  C     . ARG   A  1  365  ? -60.551 55.557  77.954  1.00 18.19 ? 363  ARG   A C     1 
ATOM   2608  O  O     . ARG   A  1  365  ? -59.936 55.501  76.886  1.00 18.38 ? 363  ARG   A O     1 
ATOM   2609  C  CB    . ARG   A  1  365  ? -62.525 54.362  76.952  1.00 17.15 ? 363  ARG   A CB    1 
ATOM   2610  C  CG    . ARG   A  1  365  ? -61.978 52.973  77.140  1.00 17.85 ? 363  ARG   A CG    1 
ATOM   2611  C  CD    . ARG   A  1  365  ? -62.812 51.961  76.434  1.00 21.11 ? 363  ARG   A CD    1 
ATOM   2612  N  NE    . ARG   A  1  365  ? -62.334 50.627  76.750  1.00 19.57 ? 363  ARG   A NE    1 
ATOM   2613  C  CZ    . ARG   A  1  365  ? -61.601 49.895  75.928  1.00 18.97 ? 363  ARG   A CZ    1 
ATOM   2614  N  NH1   . ARG   A  1  365  ? -61.328 50.301  74.699  1.00 22.41 ? 363  ARG   A NH1   1 
ATOM   2615  N  NH2   . ARG   A  1  365  ? -61.137 48.727  76.347  1.00 17.90 ? 363  ARG   A NH2   1 
ATOM   2616  N  N     . ILE   A  1  366  ? -59.962 55.867  79.105  1.00 16.16 ? 364  ILE   A N     1 
ATOM   2617  C  CA    . ILE   A  1  366  ? -58.569 56.284  79.139  1.00 15.71 ? 364  ILE   A CA    1 
ATOM   2618  C  C     . ILE   A  1  366  ? -57.695 55.126  78.701  1.00 15.15 ? 364  ILE   A C     1 
ATOM   2619  O  O     . ILE   A  1  366  ? -57.863 53.990  79.161  1.00 15.37 ? 364  ILE   A O     1 
ATOM   2620  C  CB    . ILE   A  1  366  ? -58.193 56.780  80.540  1.00 16.25 ? 364  ILE   A CB    1 
ATOM   2621  C  CG1   . ILE   A  1  366  ? -59.051 57.996  80.900  1.00 19.08 ? 364  ILE   A CG1   1 
ATOM   2622  C  CG2   . ILE   A  1  366  ? -56.705 57.121  80.609  1.00 17.22 ? 364  ILE   A CG2   1 
ATOM   2623  C  CD1   . ILE   A  1  366  ? -58.875 58.471  82.329  1.00 17.65 ? 364  ILE   A CD1   1 
ATOM   2624  N  N     . MET   A  1  367  ? -56.759 55.407  77.800  1.00 15.91 ? 365  MET   A N     1 
ATOM   2625  C  CA    . MET   A  1  367  ? -55.793 54.404  77.384  1.00 15.78 ? 365  MET   A CA    1 
ATOM   2626  C  C     . MET   A  1  367  ? -54.691 54.384  78.427  1.00 15.51 ? 365  MET   A C     1 
ATOM   2627  O  O     . MET   A  1  367  ? -54.031 55.400  78.654  1.00 18.89 ? 365  MET   A O     1 
ATOM   2628  C  CB    . MET   A  1  367  ? -55.238 54.763  76.010  1.00 15.76 ? 365  MET   A CB    1 
ATOM   2629  C  CG    . MET   A  1  367  ? -56.343 55.020  74.992  1.00 17.38 ? 365  MET   A CG    1 
ATOM   2630  S  SD    . MET   A  1  367  ? -55.733 55.389  73.335  1.00 17.97 ? 365  MET   A SD    1 
ATOM   2631  C  CE    . MET   A  1  367  ? -55.617 53.761  72.571  1.00 21.52 ? 365  MET   A CE    1 
ATOM   2632  N  N     . VAL   A  1  368  ? -54.516 53.260  79.097  1.00 14.36 ? 366  VAL   A N     1 
ATOM   2633  C  CA    . VAL   A  1  368  ? -53.575 53.189  80.200  1.00 15.05 ? 366  VAL   A CA    1 
ATOM   2634  C  C     . VAL   A  1  368  ? -52.445 52.272  79.780  1.00 14.54 ? 366  VAL   A C     1 
ATOM   2635  O  O     . VAL   A  1  368  ? -52.640 51.061  79.616  1.00 15.39 ? 366  VAL   A O     1 
ATOM   2636  C  CB    . VAL   A  1  368  ? -54.223 52.685  81.491  1.00 16.50 ? 366  VAL   A CB    1 
ATOM   2637  C  CG1   . VAL   A  1  368  ? -53.176 52.632  82.603  1.00 17.70 ? 366  VAL   A CG1   1 
ATOM   2638  C  CG2   . VAL   A  1  368  ? -55.402 53.559  81.878  1.00 18.00 ? 366  VAL   A CG2   1 
ATOM   2639  N  N     . ARG   A  1  369  ? -51.255 52.840  79.619  1.00 13.30 ? 367  ARG   A N     1 
ATOM   2640  C  CA    . ARG   A  1  369  ? -50.076 52.051  79.308  1.00 15.34 ? 367  ARG   A CA    1 
ATOM   2641  C  C     . ARG   A  1  369  ? -49.411 51.664  80.614  1.00 14.90 ? 367  ARG   A C     1 
ATOM   2642  O  O     . ARG   A  1  369  ? -48.942 52.528  81.363  1.00 16.70 ? 367  ARG   A O     1 
ATOM   2643  C  CB    . ARG   A  1  369  ? -49.103 52.825  78.433  1.00 15.31 ? 367  ARG   A CB    1 
ATOM   2644  C  CG    . ARG   A  1  369  ? -47.922 51.955  78.060  1.00 16.00 ? 367  ARG   A CG    1 
ATOM   2645  C  CD    . ARG   A  1  369  ? -46.733 52.755  77.611  1.00 16.20 ? 367  ARG   A CD    1 
ATOM   2646  N  NE    . ARG   A  1  369  ? -47.028 53.424  76.356  1.00 15.38 ? 367  ARG   A NE    1 
ATOM   2647  C  CZ    . ARG   A  1  369  ? -46.464 54.556  75.960  1.00 16.80 ? 367  ARG   A CZ    1 
ATOM   2648  N  NH1   . ARG   A  1  369  ? -45.551 55.169  76.697  1.00 16.95 ? 367  ARG   A NH1   1 
ATOM   2649  N  NH2   . ARG   A  1  369  ? -46.845 55.096  74.805  1.00 17.29 ? 367  ARG   A NH2   1 
ATOM   2650  N  N     . LEU   A  1  370  ? -49.386 50.373  80.887  1.00 14.88 ? 368  LEU   A N     1 
ATOM   2651  C  CA    . LEU   A  1  370  ? -48.714 49.855  82.060  1.00 14.36 ? 368  LEU   A CA    1 
ATOM   2652  C  C     . LEU   A  1  370  ? -47.284 49.513  81.654  1.00 14.79 ? 368  LEU   A C     1 
ATOM   2653  O  O     . LEU   A  1  370  ? -47.065 48.708  80.744  1.00 15.43 ? 368  LEU   A O     1 
ATOM   2654  C  CB    . LEU   A  1  370  ? -49.453 48.628  82.589  1.00 16.82 ? 368  LEU   A CB    1 
ATOM   2655  C  CG    . LEU   A  1  370  ? -48.903 48.054  83.887  1.00 17.15 ? 368  LEU   A CG    1 
ATOM   2656  C  CD1   . LEU   A  1  370  ? -49.071 49.028  85.054  1.00 18.88 ? 368  LEU   A CD1   1 
ATOM   2657  C  CD2   . LEU   A  1  370  ? -49.576 46.723  84.183  1.00 18.43 ? 368  LEU   A CD2   1 
ATOM   2658  N  N     . VAL   A  1  371  ? -46.319 50.141  82.316  1.00 14.74 ? 369  VAL   A N     1 
ATOM   2659  C  CA    . VAL   A  1  371  ? -44.913 49.893  82.067  1.00 13.99 ? 369  VAL   A CA    1 
ATOM   2660  C  C     . VAL   A  1  371  ? -44.313 49.517  83.399  1.00 14.69 ? 369  VAL   A C     1 
ATOM   2661  O  O     . VAL   A  1  371  ? -44.926 49.697  84.446  1.00 16.83 ? 369  VAL   A O     1 
ATOM   2662  C  CB    . VAL   A  1  371  ? -44.200 51.128  81.495  1.00 14.23 ? 369  VAL   A CB    1 
ATOM   2663  C  CG1   . VAL   A  1  371  ? -44.897 51.627  80.252  1.00 15.33 ? 369  VAL   A CG1   1 
ATOM   2664  C  CG2   . VAL   A  1  371  ? -44.079 52.220  82.550  1.00 16.15 ? 369  VAL   A CG2   1 
ATOM   2665  N  N     . LYS   A  1  372  ? -43.082 49.015  83.363  1.00 15.05 ? 370  LYS   A N     1 
ATOM   2666  C  CA    . LYS   A  1  372  ? -42.388 48.829  84.631  1.00 15.83 ? 370  LYS   A CA    1 
ATOM   2667  C  C     . LYS   A  1  372  ? -41.777 50.144  85.113  1.00 17.01 ? 370  LYS   A C     1 
ATOM   2668  O  O     . LYS   A  1  372  ? -42.155 50.663  86.171  1.00 18.88 ? 370  LYS   A O     1 
ATOM   2669  C  CB    . LYS   A  1  372  ? -41.427 47.641  84.546  1.00 17.17 ? 370  LYS   A CB    1 
ATOM   2670  C  CG    . LYS   A  1  372  ? -42.250 46.359  84.422  1.00 17.24 ? 370  LYS   A CG    1 
ATOM   2671  C  CD    . LYS   A  1  372  ? -41.429 45.099  84.283  1.00 18.99 ? 370  LYS   A CD    1 
ATOM   2672  C  CE    . LYS   A  1  372  ? -42.366 43.931  83.958  1.00 17.83 ? 370  LYS   A CE    1 
ATOM   2673  N  NZ    . LYS   A  1  372  ? -41.588 42.674  83.753  1.00 18.94 ? 370  LYS   A NZ    1 
ATOM   2674  N  N     . GLY   A  1  373  ? -40.908 50.754  84.313  1.00 15.20 ? 371  GLY   A N     1 
ATOM   2675  C  CA    . GLY   A  1  373  ? -40.435 52.097  84.621  1.00 14.41 ? 371  GLY   A CA    1 
ATOM   2676  C  C     . GLY   A  1  373  ? -38.997 52.314  84.189  1.00 15.55 ? 371  GLY   A C     1 
ATOM   2677  O  O     . GLY   A  1  373  ? -38.179 51.397  84.280  1.00 15.97 ? 371  GLY   A O     1 
ATOM   2678  N  N     . ALA   A  1  374  ? -38.668 53.519  83.731  1.00 14.36 ? 372  ALA   A N     1 
ATOM   2679  C  CA    . ALA   A  1  374  ? -37.406 53.745  83.044  1.00 15.03 ? 372  ALA   A CA    1 
ATOM   2680  C  C     . ALA   A  1  374  ? -36.358 54.474  83.867  1.00 17.15 ? 372  ALA   A C     1 
ATOM   2681  O  O     . ALA   A  1  374  ? -35.238 54.665  83.374  1.00 17.27 ? 372  ALA   A O     1 
ATOM   2682  C  CB    . ALA   A  1  374  ? -37.659 54.529  81.757  1.00 16.70 ? 372  ALA   A CB    1 
ATOM   2683  N  N     . TYR   A  1  375  ? -36.669 54.898  85.086  1.00 15.33 ? 373  TYR   A N     1 
ATOM   2684  C  CA    . TYR   A  1  375  ? -35.804 55.807  85.828  1.00 14.58 ? 373  TYR   A CA    1 
ATOM   2685  C  C     . TYR   A  1  375  ? -35.294 55.188  87.119  1.00 12.86 ? 373  TYR   A C     1 
ATOM   2686  O  O     . TYR   A  1  375  ? -35.005 55.913  88.071  1.00 15.31 ? 373  TYR   A O     1 
ATOM   2687  C  CB    . TYR   A  1  375  ? -36.525 57.114  86.159  1.00 15.68 ? 373  TYR   A CB    1 
ATOM   2688  C  CG    . TYR   A  1  375  ? -37.100 57.832  84.971  1.00 14.78 ? 373  TYR   A CG    1 
ATOM   2689  C  CD1   . TYR   A  1  375  ? -38.286 57.398  84.379  1.00 14.37 ? 373  TYR   A CD1   1 
ATOM   2690  C  CD2   . TYR   A  1  375  ? -36.479 58.960  84.460  1.00 18.00 ? 373  TYR   A CD2   1 
ATOM   2691  C  CE1   . TYR   A  1  375  ? -38.820 58.060  83.284  1.00 16.10 ? 373  TYR   A CE1   1 
ATOM   2692  C  CE2   . TYR   A  1  375  ? -37.002 59.631  83.376  1.00 19.25 ? 373  TYR   A CE2   1 
ATOM   2693  C  CZ    . TYR   A  1  375  ? -38.171 59.182  82.801  1.00 19.48 ? 373  TYR   A CZ    1 
ATOM   2694  O  OH    . TYR   A  1  375  ? -38.678 59.872  81.722  1.00 20.93 ? 373  TYR   A OH    1 
ATOM   2695  N  N     . TRP   A  1  376  ? -35.190 53.861  87.167  1.00 13.23 ? 374  TRP   A N     1 
ATOM   2696  C  CA    . TRP   A  1  376  ? -34.988 53.182  88.444  1.00 16.12 ? 374  TRP   A CA    1 
ATOM   2697  C  C     . TRP   A  1  376  ? -33.736 53.669  89.161  1.00 15.94 ? 374  TRP   A C     1 
ATOM   2698  O  O     . TRP   A  1  376  ? -33.801 54.092  90.324  1.00 15.31 ? 374  TRP   A O     1 
ATOM   2699  C  CB    . TRP   A  1  376  ? -34.967 51.667  88.275  1.00 16.57 ? 374  TRP   A CB    1 
ATOM   2700  C  CG    . TRP   A  1  376  ? -34.812 50.986  89.588  1.00 16.22 ? 374  TRP   A CG    1 
ATOM   2701  C  CD1   . TRP   A  1  376  ? -35.790 50.759  90.514  1.00 17.43 ? 374  TRP   A CD1   1 
ATOM   2702  C  CD2   . TRP   A  1  376  ? -33.600 50.472  90.148  1.00 16.76 ? 374  TRP   A CD2   1 
ATOM   2703  N  NE1   . TRP   A  1  376  ? -35.261 50.121  91.610  1.00 16.46 ? 374  TRP   A NE1   1 
ATOM   2704  C  CE2   . TRP   A  1  376  ? -33.918 49.931  91.406  1.00 16.91 ? 374  TRP   A CE2   1 
ATOM   2705  C  CE3   . TRP   A  1  376  ? -32.281 50.398  89.698  1.00 19.52 ? 374  TRP   A CE3   1 
ATOM   2706  C  CZ2   . TRP   A  1  376  ? -32.963 49.338  92.226  1.00 18.51 ? 374  TRP   A CZ2   1 
ATOM   2707  C  CZ3   . TRP   A  1  376  ? -31.331 49.800  90.518  1.00 20.42 ? 374  TRP   A CZ3   1 
ATOM   2708  C  CH2   . TRP   A  1  376  ? -31.678 49.279  91.761  1.00 20.08 ? 374  TRP   A CH2   1 
ATOM   2709  N  N     . ASP   A  1  377  ? -32.575 53.600  88.492  1.00 16.84 ? 375  ASP   A N     1 
ATOM   2710  C  CA    A ASP   A  1  377  ? -31.312 54.030  89.104  0.51 16.89 ? 375  ASP   A CA    1 
ATOM   2711  C  CA    B ASP   A  1  377  ? -31.367 53.990  89.203  0.49 16.87 ? 375  ASP   A CA    1 
ATOM   2712  C  C     . ASP   A  1  377  ? -31.409 55.450  89.631  1.00 16.18 ? 375  ASP   A C     1 
ATOM   2713  O  O     . ASP   A  1  377  ? -30.905 55.774  90.709  1.00 16.12 ? 375  ASP   A O     1 
ATOM   2714  C  CB    A ASP   A  1  377  ? -30.184 54.019  88.065  0.51 19.15 ? 375  ASP   A CB    1 
ATOM   2715  C  CB    B ASP   A  1  377  ? -30.083 53.595  88.457  0.49 19.94 ? 375  ASP   A CB    1 
ATOM   2716  C  CG    A ASP   A  1  377  ? -29.802 52.632  87.606  0.51 22.84 ? 375  ASP   A CG    1 
ATOM   2717  C  CG    B ASP   A  1  377  ? -29.995 54.180  87.065  0.49 20.10 ? 375  ASP   A CG    1 
ATOM   2718  O  OD1   A ASP   A  1  377  ? -29.906 51.685  88.399  0.51 30.12 ? 375  ASP   A OD1   1 
ATOM   2719  O  OD1   B ASP   A  1  377  ? -30.578 55.251  86.818  0.49 24.54 ? 375  ASP   A OD1   1 
ATOM   2720  O  OD2   A ASP   A  1  377  ? -29.373 52.499  86.440  0.51 29.86 ? 375  ASP   A OD2   1 
ATOM   2721  O  OD2   B ASP   A  1  377  ? -29.325 53.555  86.212  0.49 21.99 ? 375  ASP   A OD2   1 
ATOM   2722  N  N     . ALA   A  1  378  ? -32.032 56.324  88.843  1.00 15.39 ? 376  ALA   A N     1 
ATOM   2723  C  CA    . ALA   A  1  378  ? -32.104 57.727  89.210  1.00 14.57 ? 376  ALA   A CA    1 
ATOM   2724  C  C     . ALA   A  1  378  ? -32.992 57.918  90.422  1.00 14.99 ? 376  ALA   A C     1 
ATOM   2725  O  O     . ALA   A  1  378  ? -32.721 58.783  91.266  1.00 15.47 ? 376  ALA   A O     1 
ATOM   2726  C  CB    . ALA   A  1  378  ? -32.633 58.545  88.030  1.00 16.11 ? 376  ALA   A CB    1 
ATOM   2727  N  N     . GLU   A  1  379  ? -34.054 57.114  90.530  1.00 15.01 ? 377  GLU   A N     1 
ATOM   2728  C  CA    . GLU   A  1  379  ? -34.925 57.240  91.690  1.00 14.77 ? 377  GLU   A CA    1 
ATOM   2729  C  C     . GLU   A  1  379  ? -34.212 56.792  92.951  1.00 13.92 ? 377  GLU   A C     1 
ATOM   2730  O  O     . GLU   A  1  379  ? -34.429 57.363  94.022  1.00 15.64 ? 377  GLU   A O     1 
ATOM   2731  C  CB    . GLU   A  1  379  ? -36.205 56.431  91.507  1.00 15.23 ? 377  GLU   A CB    1 
ATOM   2732  C  CG    . GLU   A  1  379  ? -37.066 56.834  90.314  1.00 17.08 ? 377  GLU   A CG    1 
ATOM   2733  C  CD    . GLU   A  1  379  ? -37.651 58.230  90.407  1.00 16.58 ? 377  GLU   A CD    1 
ATOM   2734  O  OE1   . GLU   A  1  379  ? -37.534 58.906  91.452  1.00 16.70 ? 377  GLU   A OE1   1 
ATOM   2735  O  OE2   . GLU   A  1  379  ? -38.263 58.642  89.404  1.00 16.08 ? 377  GLU   A OE2   1 
ATOM   2736  N  N     . ILE   A  1  380  ? -33.362 55.764  92.848  1.00 15.17 ? 378  ILE   A N     1 
ATOM   2737  C  CA    . ILE   A  1  380  ? -32.610 55.337  94.025  1.00 15.58 ? 378  ILE   A CA    1 
ATOM   2738  C  C     . ILE   A  1  380  ? -31.674 56.451  94.463  1.00 16.50 ? 378  ILE   A C     1 
ATOM   2739  O  O     . ILE   A  1  380  ? -31.630 56.834  95.639  1.00 15.46 ? 378  ILE   A O     1 
ATOM   2740  C  CB    . ILE   A  1  380  ? -31.835 54.043  93.726  1.00 16.40 ? 378  ILE   A CB    1 
ATOM   2741  C  CG1   . ILE   A  1  380  ? -32.762 52.914  93.281  1.00 15.63 ? 378  ILE   A CG1   1 
ATOM   2742  C  CG2   . ILE   A  1  380  ? -31.024 53.611  94.954  1.00 16.60 ? 378  ILE   A CG2   1 
ATOM   2743  C  CD1   . ILE   A  1  380  ? -33.899 52.620  94.258  1.00 17.90 ? 378  ILE   A CD1   1 
ATOM   2744  N  N     . LYS   A  1  381  ? -30.910 56.994  93.512  1.00 14.65 ? 379  LYS   A N     1 
ATOM   2745  C  CA    . LYS   A  1  381  ? -29.976 58.063  93.834  1.00 15.38 ? 379  LYS   A CA    1 
ATOM   2746  C  C     . LYS   A  1  381  ? -30.694 59.258  94.440  1.00 15.04 ? 379  LYS   A C     1 
ATOM   2747  O  O     . LYS   A  1  381  ? -30.262 59.802  95.462  1.00 15.09 ? 379  LYS   A O     1 
ATOM   2748  C  CB    . LYS   A  1  381  ? -29.201 58.477  92.588  1.00 15.20 ? 379  LYS   A CB    1 
ATOM   2749  C  CG    . LYS   A  1  381  ? -28.221 59.598  92.853  1.00 15.26 ? 379  LYS   A CG    1 
ATOM   2750  C  CD    . LYS   A  1  381  ? -27.324 59.844  91.640  1.00 15.24 ? 379  LYS   A CD    1 
ATOM   2751  C  CE    . LYS   A  1  381  ? -26.306 60.928  91.941  1.00 17.83 ? 379  LYS   A CE    1 
ATOM   2752  N  NZ    . LYS   A  1  381  ? -25.413 61.219  90.777  1.00 15.41 ? 379  LYS   A NZ    1 
ATOM   2753  N  N     . ARG   A  1  382  ? -31.809 59.670  93.834  1.00 15.47 ? 380  ARG   A N     1 
ATOM   2754  C  CA    . ARG   A  1  382  ? -32.490 60.875  94.293  1.00 16.30 ? 380  ARG   A CA    1 
ATOM   2755  C  C     . ARG   A  1  382  ? -32.965 60.723  95.728  1.00 14.32 ? 380  ARG   A C     1 
ATOM   2756  O  O     . ARG   A  1  382  ? -32.826 61.643  96.543  1.00 16.19 ? 380  ARG   A O     1 
ATOM   2757  C  CB    . ARG   A  1  382  ? -33.689 61.164  93.390  1.00 17.57 ? 380  ARG   A CB    1 
ATOM   2758  C  CG    . ARG   A  1  382  ? -34.377 62.482  93.669  1.00 21.85 ? 380  ARG   A CG    1 
ATOM   2759  C  CD    . ARG   A  1  382  ? -33.597 63.624  93.049  1.00 35.89 ? 380  ARG   A CD    1 
ATOM   2760  N  NE    . ARG   A  1  382  ? -32.794 64.324  94.043  1.00 36.66 ? 380  ARG   A NE    1 
ATOM   2761  C  CZ    . ARG   A  1  382  ? -31.838 65.198  93.762  1.00 40.79 ? 380  ARG   A CZ    1 
ATOM   2762  N  NH1   . ARG   A  1  382  ? -31.483 65.458  92.513  1.00 46.37 ? 380  ARG   A NH1   1 
ATOM   2763  N  NH2   . ARG   A  1  382  ? -31.226 65.833  94.760  1.00 34.57 ? 380  ARG   A NH2   1 
ATOM   2764  N  N     . ALA   A  1  383  ? -33.567 59.577  96.050  1.00 15.79 ? 381  ALA   A N     1 
ATOM   2765  C  CA    . ALA   A  1  383  ? -34.079 59.383  97.402  1.00 15.41 ? 381  ALA   A CA    1 
ATOM   2766  C  C     . ALA   A  1  383  ? -32.939 59.382  98.409  1.00 15.43 ? 381  ALA   A C     1 
ATOM   2767  O  O     . ALA   A  1  383  ? -33.078 59.916  99.518  1.00 17.10 ? 381  ALA   A O     1 
ATOM   2768  C  CB    . ALA   A  1  383  ? -34.873 58.081  97.478  1.00 17.11 ? 381  ALA   A CB    1 
ATOM   2769  N  N     . GLN   A  1  384  ? -31.795 58.815  98.031  1.00 15.27 ? 382  GLN   A N     1 
ATOM   2770  C  CA    . GLN   A  1  384  ? -30.654 58.832  98.936  1.00 16.38 ? 382  GLN   A CA    1 
ATOM   2771  C  C     . GLN   A  1  384  ? -30.137 60.248  99.117  1.00 16.70 ? 382  GLN   A C     1 
ATOM   2772  O  O     . GLN   A  1  384  ? -29.892 60.683  100.245 1.00 18.31 ? 382  GLN   A O     1 
ATOM   2773  C  CB    . GLN   A  1  384  ? -29.568 57.903  98.412  1.00 15.06 ? 382  GLN   A CB    1 
ATOM   2774  C  CG    . GLN   A  1  384  ? -29.956 56.448  98.515  1.00 16.09 ? 382  GLN   A CG    1 
ATOM   2775  C  CD    . GLN   A  1  384  ? -28.810 55.545  98.134  1.00 16.97 ? 382  GLN   A CD    1 
ATOM   2776  O  OE1   . GLN   A  1  384  ? -27.861 55.981  97.481  1.00 18.92 ? 382  GLN   A OE1   1 
ATOM   2777  N  NE2   . GLN   A  1  384  ? -28.877 54.289  98.557  1.00 18.32 ? 382  GLN   A NE2   1 
ATOM   2778  N  N     . LEU   A  1  385  ? -29.984 60.992  98.017  1.00 15.52 ? 383  LEU   A N     1 
ATOM   2779  C  CA    . LEU   A  1  385  ? -29.486 62.360  98.122  1.00 16.59 ? 383  LEU   A CA    1 
ATOM   2780  C  C     . LEU   A  1  385  ? -30.381 63.200  99.010  1.00 16.30 ? 383  LEU   A C     1 
ATOM   2781  O  O     . LEU   A  1  385  ? -29.899 64.019  99.795  1.00 17.44 ? 383  LEU   A O     1 
ATOM   2782  C  CB    . LEU   A  1  385  ? -29.421 63.007  96.743  1.00 16.76 ? 383  LEU   A CB    1 
ATOM   2783  C  CG    . LEU   A  1  385  ? -28.304 62.579  95.794  1.00 19.81 ? 383  LEU   A CG    1 
ATOM   2784  C  CD1   . LEU   A  1  385  ? -28.490 63.275  94.472  1.00 19.21 ? 383  LEU   A CD1   1 
ATOM   2785  C  CD2   . LEU   A  1  385  ? -26.958 62.927  96.377  1.00 21.91 ? 383  LEU   A CD2   1 
ATOM   2786  N  N     . ASP   A  1  386  ? -31.694 63.024  98.884  1.00 16.75 ? 384  ASP   A N     1 
ATOM   2787  C  CA    . ASP   A  1  386  ? -32.654 63.862  99.577  1.00 17.68 ? 384  ASP   A CA    1 
ATOM   2788  C  C     . ASP   A  1  386  ? -32.942 63.378  100.986 1.00 18.36 ? 384  ASP   A C     1 
ATOM   2789  O  O     . ASP   A  1  386  ? -33.719 64.019  101.697 1.00 19.19 ? 384  ASP   A O     1 
ATOM   2790  C  CB    . ASP   A  1  386  ? -33.940 63.967  98.752  1.00 19.02 ? 384  ASP   A CB    1 
ATOM   2791  C  CG    . ASP   A  1  386  ? -33.756 64.797  97.493  1.00 24.55 ? 384  ASP   A CG    1 
ATOM   2792  O  OD1   . ASP   A  1  386  ? -32.683 65.416  97.328  1.00 24.85 ? 384  ASP   A OD1   1 
ATOM   2793  O  OD2   . ASP   A  1  386  ? -34.680 64.828  96.655  1.00 25.70 ? 384  ASP   A OD2   1 
ATOM   2794  N  N     . GLY   A  1  387  ? -32.338 62.271  101.402 1.00 17.61 ? 385  GLY   A N     1 
ATOM   2795  C  CA    . GLY   A  1  387  ? -32.501 61.794  102.769 1.00 17.13 ? 385  GLY   A CA    1 
ATOM   2796  C  C     . GLY   A  1  387  ? -33.929 61.434  103.109 1.00 18.90 ? 385  GLY   A C     1 
ATOM   2797  O  O     . GLY   A  1  387  ? -34.396 61.722  104.217 1.00 20.36 ? 385  GLY   A O     1 
ATOM   2798  N  N     . LEU   A  1  388  ? -34.636 60.811  102.178 1.00 18.27 ? 386  LEU   A N     1 
ATOM   2799  C  CA    . LEU   A  1  388  ? -36.055 60.580  102.391 1.00 19.72 ? 386  LEU   A CA    1 
ATOM   2800  C  C     . LEU   A  1  388  ? -36.292 59.233  103.051 1.00 19.55 ? 386  LEU   A C     1 
ATOM   2801  O  O     . LEU   A  1  388  ? -35.388 58.409  103.204 1.00 21.15 ? 386  LEU   A O     1 
ATOM   2802  C  CB    . LEU   A  1  388  ? -36.815 60.726  101.075 1.00 18.80 ? 386  LEU   A CB    1 
ATOM   2803  C  CG    . LEU   A  1  388  ? -36.684 62.140  100.510 1.00 19.16 ? 386  LEU   A CG    1 
ATOM   2804  C  CD1   . LEU   A  1  388  ? -37.405 62.300  99.168  1.00 20.48 ? 386  LEU   A CD1   1 
ATOM   2805  C  CD2   . LEU   A  1  388  ? -37.167 63.184  101.497 1.00 20.56 ? 386  LEU   A CD2   1 
ATOM   2806  N  N     . ALA   A  1  389  ? -37.536 59.025  103.483 1.00 21.31 ? 387  ALA   A N     1 
ATOM   2807  C  CA    . ALA   A  1  389  ? -37.825 57.891  104.344 1.00 22.78 ? 387  ALA   A CA    1 
ATOM   2808  C  C     . ALA   A  1  389  ? -37.585 56.571  103.629 1.00 20.46 ? 387  ALA   A C     1 
ATOM   2809  O  O     . ALA   A  1  389  ? -37.146 55.591  104.240 1.00 23.32 ? 387  ALA   A O     1 
ATOM   2810  C  CB    . ALA   A  1  389  ? -39.268 57.987  104.837 1.00 22.79 ? 387  ALA   A CB    1 
ATOM   2811  N  N     . ASP   A  1  390  ? -37.871 56.522  102.337 1.00 18.26 ? 388  ASP   A N     1 
ATOM   2812  C  CA    . ASP   A  1  390  ? -37.814 55.278  101.584 1.00 19.80 ? 388  ASP   A CA    1 
ATOM   2813  C  C     . ASP   A  1  390  ? -37.839 55.661  100.113 1.00 18.13 ? 388  ASP   A C     1 
ATOM   2814  O  O     . ASP   A  1  390  ? -37.885 56.844  99.764  1.00 18.35 ? 388  ASP   A O     1 
ATOM   2815  C  CB    . ASP   A  1  390  ? -39.000 54.384  101.963 1.00 20.46 ? 388  ASP   A CB    1 
ATOM   2816  C  CG    . ASP   A  1  390  ? -38.718 52.908  101.779 1.00 20.63 ? 388  ASP   A CG    1 
ATOM   2817  O  OD1   . ASP   A  1  390  ? -38.045 52.533  100.795 1.00 22.26 ? 388  ASP   A OD1   1 
ATOM   2818  O  OD2   . ASP   A  1  390  ? -39.168 52.115  102.638 1.00 25.48 ? 388  ASP   A OD2   1 
ATOM   2819  N  N     . PHE   A  1  391  ? -37.792 54.686  99.286  1.00 16.61 ? 389  PHE   A N     1 
ATOM   2820  C  CA    . PHE   A  1  391  ? -37.814 54.896  97.853  1.00 18.00 ? 389  PHE   A CA    1 
ATOM   2821  C  C     . PHE   A  1  391  ? -39.246 54.930  97.347  1.00 17.29 ? 389  PHE   A C     1 
ATOM   2822  O  O     . PHE   A  1  391  ? -40.138 54.323  97.941  1.00 17.82 ? 389  PHE   A O     1 
ATOM   2823  C  CB    . PHE   A  1  391  ? -37.050 53.768  97.170  1.00 18.24 ? 389  PHE   A CB    1 
ATOM   2824  C  CG    . PHE   A  1  391  ? -35.633 53.684  97.631  1.00 15.81 ? 389  PHE   A CG    1 
ATOM   2825  C  CD1   . PHE   A  1  391  ? -34.732 54.632  97.220  1.00 16.74 ? 389  PHE   A CD1   1 
ATOM   2826  C  CD2   . PHE   A  1  391  ? -35.234 52.726  98.550  1.00 17.25 ? 389  PHE   A CD2   1 
ATOM   2827  C  CE1   . PHE   A  1  391  ? -33.422 54.603  97.662  1.00 17.84 ? 389  PHE   A CE1   1 
ATOM   2828  C  CE2   . PHE   A  1  391  ? -33.931 52.695  99.004  1.00 18.12 ? 389  PHE   A CE2   1 
ATOM   2829  C  CZ    . PHE   A  1  391  ? -33.028 53.628  98.565  1.00 17.57 ? 389  PHE   A CZ    1 
ATOM   2830  N  N     . PRO   A  1  392  ? -39.491 55.658  96.260  1.00 16.03 ? 390  PRO   A N     1 
ATOM   2831  C  CA    . PRO   A  1  392  ? -40.819 55.643  95.637  1.00 16.73 ? 390  PRO   A CA    1 
ATOM   2832  C  C     . PRO   A  1  392  ? -40.968 54.521  94.625  1.00 16.18 ? 390  PRO   A C     1 
ATOM   2833  O  O     . PRO   A  1  392  ? -41.998 54.436  93.942  1.00 16.79 ? 390  PRO   A O     1 
ATOM   2834  C  CB    . PRO   A  1  392  ? -40.856 57.005  94.940  1.00 15.32 ? 390  PRO   A CB    1 
ATOM   2835  C  CG    . PRO   A  1  392  ? -39.414 57.192  94.480  1.00 15.46 ? 390  PRO   A CG    1 
ATOM   2836  C  CD    . PRO   A  1  392  ? -38.569 56.599  95.596  1.00 15.97 ? 390  PRO   A CD    1 
ATOM   2837  N  N     . VAL   A  1  393  ? -39.941 53.686  94.495  1.00 16.16 ? 391  VAL   A N     1 
ATOM   2838  C  CA    . VAL   A  1  393  ? -39.949 52.534  93.614  1.00 15.54 ? 391  VAL   A CA    1 
ATOM   2839  C  C     . VAL   A  1  393  ? -39.514 51.326  94.426  1.00 17.27 ? 391  VAL   A C     1 
ATOM   2840  O  O     . VAL   A  1  393  ? -38.907 51.448  95.489  1.00 17.78 ? 391  VAL   A O     1 
ATOM   2841  C  CB    . VAL   A  1  393  ? -39.019 52.707  92.392  1.00 15.26 ? 391  VAL   A CB    1 
ATOM   2842  C  CG1   . VAL   A  1  393  ? -39.519 53.821  91.479  1.00 17.02 ? 391  VAL   A CG1   1 
ATOM   2843  C  CG2   . VAL   A  1  393  ? -37.600 52.998  92.832  1.00 16.44 ? 391  VAL   A CG2   1 
ATOM   2844  N  N     . PHE   A  1  394  ? -39.834 50.151  93.907  1.00 16.70 ? 392  PHE   A N     1 
ATOM   2845  C  CA    . PHE   A  1  394  ? -39.332 48.926  94.500  1.00 16.53 ? 392  PHE   A CA    1 
ATOM   2846  C  C     . PHE   A  1  394  ? -37.825 48.841  94.306  1.00 16.46 ? 392  PHE   A C     1 
ATOM   2847  O  O     . PHE   A  1  394  ? -37.244 49.540  93.477  1.00 17.05 ? 392  PHE   A O     1 
ATOM   2848  C  CB    . PHE   A  1  394  ? -40.043 47.737  93.871  1.00 17.99 ? 392  PHE   A CB    1 
ATOM   2849  C  CG    . PHE   A  1  394  ? -41.514 47.779  94.090  1.00 17.57 ? 392  PHE   A CG    1 
ATOM   2850  C  CD1   . PHE   A  1  394  ? -42.012 47.682  95.377  1.00 19.82 ? 392  PHE   A CD1   1 
ATOM   2851  C  CD2   . PHE   A  1  394  ? -42.392 47.973  93.044  1.00 17.95 ? 392  PHE   A CD2   1 
ATOM   2852  C  CE1   . PHE   A  1  394  ? -43.363 47.757  95.617  1.00 18.16 ? 392  PHE   A CE1   1 
ATOM   2853  C  CE2   . PHE   A  1  394  ? -43.763 48.041  93.279  1.00 17.49 ? 392  PHE   A CE2   1 
ATOM   2854  C  CZ    . PHE   A  1  394  ? -44.241 47.927  94.569  1.00 17.13 ? 392  PHE   A CZ    1 
ATOM   2855  N  N     . THR   A  1  395  ? -37.186 48.014  95.129  1.00 16.83 ? 393  THR   A N     1 
ATOM   2856  C  CA    . THR   A  1  395  ? -35.744 47.835  95.052  1.00 18.29 ? 393  THR   A CA    1 
ATOM   2857  C  C     . THR   A  1  395  ? -35.336 46.445  94.607  1.00 19.78 ? 393  THR   A C     1 
ATOM   2858  O  O     . THR   A  1  395  ? -34.151 46.227  94.340  1.00 18.59 ? 393  THR   A O     1 
ATOM   2859  C  CB    . THR   A  1  395  ? -35.070 48.150  96.394  1.00 19.14 ? 393  THR   A CB    1 
ATOM   2860  O  OG1   . THR   A  1  395  ? -35.608 47.304  97.418  1.00 19.47 ? 393  THR   A OG1   1 
ATOM   2861  C  CG2   . THR   A  1  395  ? -35.273 49.594  96.769  1.00 19.55 ? 393  THR   A CG2   1 
ATOM   2862  N  N     . ARG   A  1  396  ? -36.266 45.504  94.527  1.00 19.17 ? 394  ARG   A N     1 
ATOM   2863  C  CA    . ARG   A  1  396  ? -36.010 44.205  93.930  1.00 21.10 ? 394  ARG   A CA    1 
ATOM   2864  C  C     . ARG   A  1  396  ? -36.799 44.108  92.643  1.00 19.34 ? 394  ARG   A C     1 
ATOM   2865  O  O     . ARG   A  1  396  ? -37.992 44.425  92.619  1.00 19.16 ? 394  ARG   A O     1 
ATOM   2866  C  CB    . ARG   A  1  396  ? -36.421 43.069  94.858  1.00 20.75 ? 394  ARG   A CB    1 
ATOM   2867  C  CG    . ARG   A  1  396  ? -35.606 43.002  96.112  1.00 20.56 ? 394  ARG   A CG    1 
ATOM   2868  C  CD    . ARG   A  1  396  ? -35.934 41.717  96.852  1.00 25.58 ? 394  ARG   A CD    1 
ATOM   2869  N  NE    . ARG   A  1  396  ? -35.408 41.747  98.206  1.00 27.72 ? 394  ARG   A NE    1 
ATOM   2870  C  CZ    . ARG   A  1  396  ? -34.566 40.853  98.703  1.00 32.74 ? 394  ARG   A CZ    1 
ATOM   2871  N  NH1   . ARG   A  1  396  ? -34.186 39.798  97.999  1.00 35.21 ? 394  ARG   A NH1   1 
ATOM   2872  N  NH2   . ARG   A  1  396  ? -34.094 41.025  99.935  1.00 29.83 ? 394  ARG   A NH2   1 
ATOM   2873  N  N     . LYS   A  1  397  ? -36.128 43.676  91.582  1.00 20.16 ? 395  LYS   A N     1 
ATOM   2874  C  CA    . LYS   A  1  397  ? -36.763 43.636  90.275  1.00 19.89 ? 395  LYS   A CA    1 
ATOM   2875  C  C     . LYS   A  1  397  ? -38.003 42.761  90.300  1.00 20.07 ? 395  LYS   A C     1 
ATOM   2876  O  O     . LYS   A  1  397  ? -39.008 43.067  89.646  1.00 19.00 ? 395  LYS   A O     1 
ATOM   2877  C  CB    . LYS   A  1  397  ? -35.749 43.157  89.236  1.00 23.45 ? 395  LYS   A CB    1 
ATOM   2878  C  CG    . LYS   A  1  397  ? -36.150 43.436  87.811  1.00 21.69 ? 395  LYS   A CG    1 
ATOM   2879  C  CD    . LYS   A  1  397  ? -36.863 42.270  87.207  1.00 22.42 ? 395  LYS   A CD    1 
ATOM   2880  C  CE    . LYS   A  1  397  ? -37.331 42.611  85.813  1.00 20.94 ? 395  LYS   A CE    1 
ATOM   2881  N  NZ    . LYS   A  1  397  ? -37.961 41.433  85.170  1.00 22.53 ? 395  LYS   A NZ    1 
ATOM   2882  N  N     . ILE   A  1  398  ? -37.964 41.681  91.079  1.00 19.85 ? 396  ILE   A N     1 
ATOM   2883  C  CA    . ILE   A  1  398  ? -39.088 40.762  91.111  1.00 20.19 ? 396  ILE   A CA    1 
ATOM   2884  C  C     . ILE   A  1  398  ? -40.315 41.434  91.714  1.00 18.10 ? 396  ILE   A C     1 
ATOM   2885  O  O     . ILE   A  1  398  ? -41.456 41.079  91.387  1.00 20.38 ? 396  ILE   A O     1 
ATOM   2886  C  CB    . ILE   A  1  398  ? -38.665 39.470  91.838  1.00 23.58 ? 396  ILE   A CB    1 
ATOM   2887  C  CG1   . ILE   A  1  398  ? -39.674 38.366  91.584  1.00 26.59 ? 396  ILE   A CG1   1 
ATOM   2888  C  CG2   . ILE   A  1  398  ? -38.474 39.717  93.323  1.00 21.90 ? 396  ILE   A CG2   1 
ATOM   2889  C  CD1   . ILE   A  1  398  ? -39.141 37.010  91.943  1.00 29.71 ? 396  ILE   A CD1   1 
ATOM   2890  N  N     . HIS   A  1  399  ? -40.106 42.433  92.570  1.00 20.73 ? 397  HIS   A N     1 
ATOM   2891  C  CA    . HIS   A  1  399  ? -41.233 43.175  93.122  1.00 20.61 ? 397  HIS   A CA    1 
ATOM   2892  C  C     . HIS   A  1  399  ? -41.944 43.961  92.036  1.00 17.40 ? 397  HIS   A C     1 
ATOM   2893  O  O     . HIS   A  1  399  ? -43.177 43.959  91.964  1.00 18.93 ? 397  HIS   A O     1 
ATOM   2894  C  CB    . HIS   A  1  399  ? -40.751 44.095  94.237  1.00 19.74 ? 397  HIS   A CB    1 
ATOM   2895  C  CG    . HIS   A  1  399  ? -40.256 43.357  95.441  1.00 18.43 ? 397  HIS   A CG    1 
ATOM   2896  N  ND1   . HIS   A  1  399  ? -39.623 43.982  96.491  1.00 20.33 ? 397  HIS   A ND1   1 
ATOM   2897  C  CD2   . HIS   A  1  399  ? -40.300 42.040  95.754  1.00 23.79 ? 397  HIS   A CD2   1 
ATOM   2898  C  CE1   . HIS   A  1  399  ? -39.300 43.081  97.404  1.00 21.40 ? 397  HIS   A CE1   1 
ATOM   2899  N  NE2   . HIS   A  1  399  ? -39.695 41.895  96.978  1.00 22.64 ? 397  HIS   A NE2   1 
ATOM   2900  N  N     . THR   A  1  400  ? -41.179 44.614  91.167  1.00 17.62 ? 398  THR   A N     1 
ATOM   2901  C  CA    . THR   A  1  400  ? -41.771 45.292  90.024  1.00 15.93 ? 398  THR   A CA    1 
ATOM   2902  C  C     . THR   A  1  400  ? -42.566 44.327  89.153  1.00 17.33 ? 398  THR   A C     1 
ATOM   2903  O  O     . THR   A  1  400  ? -43.663 44.661  88.691  1.00 16.53 ? 398  THR   A O     1 
ATOM   2904  C  CB    . THR   A  1  400  ? -40.664 45.992  89.240  1.00 17.39 ? 398  THR   A CB    1 
ATOM   2905  O  OG1   . THR   A  1  400  ? -40.141 47.032  90.066  1.00 17.51 ? 398  THR   A OG1   1 
ATOM   2906  C  CG2   . THR   A  1  400  ? -41.205 46.601  87.945  1.00 16.37 ? 398  THR   A CG2   1 
ATOM   2907  N  N     . ASP   A  1  401  ? -42.049 43.112  88.945  1.00 17.45 ? 399  ASP   A N     1 
ATOM   2908  C  CA    . ASP   A  1  401  ? -42.762 42.148  88.110  1.00 17.39 ? 399  ASP   A CA    1 
ATOM   2909  C  C     . ASP   A  1  401  ? -44.097 41.769  88.732  1.00 17.61 ? 399  ASP   A C     1 
ATOM   2910  O  O     . ASP   A  1  401  ? -45.113 41.689  88.031  1.00 18.17 ? 399  ASP   A O     1 
ATOM   2911  C  CB    . ASP   A  1  401  ? -41.911 40.897  87.872  1.00 18.37 ? 399  ASP   A CB    1 
ATOM   2912  C  CG    . ASP   A  1  401  ? -40.715 41.166  86.986  1.00 22.90 ? 399  ASP   A CG    1 
ATOM   2913  O  OD1   . ASP   A  1  401  ? -40.772 42.117  86.184  1.00 21.68 ? 399  ASP   A OD1   1 
ATOM   2914  O  OD2   . ASP   A  1  401  ? -39.720 40.425  87.090  1.00 23.73 ? 399  ASP   A OD2   1 
ATOM   2915  N  N     . VAL   A  1  402  ? -44.107 41.515  90.044  1.00 19.72 ? 400  VAL   A N     1 
ATOM   2916  C  CA    . VAL   A  1  402  ? -45.360 41.188  90.722  1.00 19.22 ? 400  VAL   A CA    1 
ATOM   2917  C  C     . VAL   A  1  402  ? -46.303 42.377  90.676  1.00 18.60 ? 400  VAL   A C     1 
ATOM   2918  O  O     . VAL   A  1  402  ? -47.503 42.224  90.417  1.00 18.97 ? 400  VAL   A O     1 
ATOM   2919  C  CB    . VAL   A  1  402  ? -45.088 40.742  92.167  1.00 19.64 ? 400  VAL   A CB    1 
ATOM   2920  C  CG1   . VAL   A  1  402  ? -46.407 40.548  92.935  1.00 19.57 ? 400  VAL   A CG1   1 
ATOM   2921  C  CG2   . VAL   A  1  402  ? -44.278 39.467  92.162  1.00 23.29 ? 400  VAL   A CG2   1 
ATOM   2922  N  N     . SER   A  1  403  ? -45.777 43.575  90.945  1.00 19.97 ? 401  SER   A N     1 
ATOM   2923  C  CA    . SER   A  1  403  ? -46.589 44.781  90.859  1.00 19.07 ? 401  SER   A CA    1 
ATOM   2924  C  C     . SER   A  1  403  ? -47.219 44.907  89.479  1.00 19.46 ? 401  SER   A C     1 
ATOM   2925  O  O     . SER   A  1  403  ? -48.413 45.195  89.351  1.00 18.14 ? 401  SER   A O     1 
ATOM   2926  C  CB    . SER   A  1  403  ? -45.718 45.998  91.162  1.00 19.72 ? 401  SER   A CB    1 
ATOM   2927  O  OG    . SER   A  1  403  ? -46.419 47.203  90.914  1.00 18.21 ? 401  SER   A OG    1 
ATOM   2928  N  N     . TYR   A  1  404  ? -46.434 44.649  88.433  1.00 17.78 ? 402  TYR   A N     1 
ATOM   2929  C  CA    . TYR   A  1  404  ? -46.956 44.735  87.076  1.00 17.96 ? 402  TYR   A CA    1 
ATOM   2930  C  C     . TYR   A  1  404  ? -48.127 43.777  86.877  1.00 17.68 ? 402  TYR   A C     1 
ATOM   2931  O  O     . TYR   A  1  404  ? -49.190 44.168  86.384  1.00 17.39 ? 402  TYR   A O     1 
ATOM   2932  C  CB    . TYR   A  1  404  ? -45.814 44.468  86.089  1.00 16.12 ? 402  TYR   A CB    1 
ATOM   2933  C  CG    . TYR   A  1  404  ? -46.135 44.815  84.656  1.00 17.06 ? 402  TYR   A CG    1 
ATOM   2934  C  CD1   . TYR   A  1  404  ? -46.921 43.977  83.880  1.00 16.78 ? 402  TYR   A CD1   1 
ATOM   2935  C  CD2   . TYR   A  1  404  ? -45.636 45.969  84.075  1.00 16.20 ? 402  TYR   A CD2   1 
ATOM   2936  C  CE1   . TYR   A  1  404  ? -47.211 44.282  82.571  1.00 17.81 ? 402  TYR   A CE1   1 
ATOM   2937  C  CE2   . TYR   A  1  404  ? -45.931 46.282  82.751  1.00 15.52 ? 402  TYR   A CE2   1 
ATOM   2938  C  CZ    . TYR   A  1  404  ? -46.707 45.428  82.011  1.00 16.02 ? 402  TYR   A CZ    1 
ATOM   2939  O  OH    . TYR   A  1  404  ? -47.009 45.726  80.708  1.00 18.34 ? 402  TYR   A OH    1 
ATOM   2940  N  N     . ILE   A  1  405  ? -47.958 42.521  87.280  1.00 18.50 ? 403  ILE   A N     1 
ATOM   2941  C  CA    . ILE   A  1  405  ? -49.010 41.537  87.071  1.00 18.31 ? 403  ILE   A CA    1 
ATOM   2942  C  C     . ILE   A  1  405  ? -50.235 41.861  87.919  1.00 18.61 ? 403  ILE   A C     1 
ATOM   2943  O  O     . ILE   A  1  405  ? -51.373 41.737  87.457  1.00 19.81 ? 403  ILE   A O     1 
ATOM   2944  C  CB    . ILE   A  1  405  ? -48.449 40.128  87.325  1.00 20.42 ? 403  ILE   A CB    1 
ATOM   2945  C  CG1   . ILE   A  1  405  ? -47.330 39.860  86.322  1.00 23.10 ? 403  ILE   A CG1   1 
ATOM   2946  C  CG2   . ILE   A  1  405  ? -49.542 39.085  87.202  1.00 22.90 ? 403  ILE   A CG2   1 
ATOM   2947  C  CD1   . ILE   A  1  405  ? -46.430 38.705  86.679  1.00 26.52 ? 403  ILE   A CD1   1 
ATOM   2948  N  N     . ALA   A  1  406  ? -50.020 42.307  89.160  1.00 19.79 ? 404  ALA   A N     1 
ATOM   2949  C  CA    . ALA   A  1  406  ? -51.139 42.721  90.005  1.00 19.70 ? 404  ALA   A CA    1 
ATOM   2950  C  C     . ALA   A  1  406  ? -51.904 43.878  89.380  1.00 19.01 ? 404  ALA   A C     1 
ATOM   2951  O  O     . ALA   A  1  406  ? -53.142 43.909  89.408  1.00 20.29 ? 404  ALA   A O     1 
ATOM   2952  C  CB    . ALA   A  1  406  ? -50.617 43.140  91.374  1.00 19.95 ? 404  ALA   A CB    1 
ATOM   2953  N  N     . CYS   A  1  407  ? -51.182 44.852  88.823  1.00 18.62 ? 405  CYS   A N     1 
ATOM   2954  C  CA    . CYS   A  1  407  ? -51.835 45.996  88.206  1.00 17.76 ? 405  CYS   A CA    1 
ATOM   2955  C  C     . CYS   A  1  407  ? -52.515 45.611  86.903  1.00 18.48 ? 405  CYS   A C     1 
ATOM   2956  O  O     . CYS   A  1  407  ? -53.553 46.186  86.555  1.00 17.91 ? 405  CYS   A O     1 
ATOM   2957  C  CB    . CYS   A  1  407  ? -50.812 47.106  88.002  1.00 18.08 ? 405  CYS   A CB    1 
ATOM   2958  S  SG    . CYS   A  1  407  ? -50.340 47.848  89.579  1.00 22.71 ? 405  CYS   A SG    1 
ATOM   2959  N  N     . ALA   A  1  408  ? -51.974 44.624  86.186  1.00 18.36 ? 406  ALA   A N     1 
ATOM   2960  C  CA    . ALA   A  1  408  ? -52.658 44.130  84.999  1.00 18.17 ? 406  ALA   A CA    1 
ATOM   2961  C  C     . ALA   A  1  408  ? -53.979 43.478  85.369  1.00 17.69 ? 406  ALA   A C     1 
ATOM   2962  O  O     . ALA   A  1  408  ? -54.954 43.575  84.621  1.00 19.36 ? 406  ALA   A O     1 
ATOM   2963  C  CB    . ALA   A  1  408  ? -51.767 43.142  84.244  1.00 19.30 ? 406  ALA   A CB    1 
ATOM   2964  N  N     . ALA   A  1  409  ? -54.020 42.786  86.507  1.00 20.53 ? 407  ALA   A N     1 
ATOM   2965  C  CA    . ALA   A  1  409  ? -55.269 42.187  86.955  1.00 19.51 ? 407  ALA   A CA    1 
ATOM   2966  C  C     . ALA   A  1  409  ? -56.311 43.259  87.228  1.00 19.49 ? 407  ALA   A C     1 
ATOM   2967  O  O     . ALA   A  1  409  ? -57.490 43.092  86.892  1.00 21.21 ? 407  ALA   A O     1 
ATOM   2968  C  CB    . ALA   A  1  409  ? -55.021 41.335  88.204  1.00 21.63 ? 407  ALA   A CB    1 
ATOM   2969  N  N     . LYS   A  1  410  ? -55.885 44.377  87.819  1.00 20.10 ? 408  LYS   A N     1 
ATOM   2970  C  CA    . LYS   A  1  410  ? -56.798 45.484  88.076  1.00 18.13 ? 408  LYS   A CA    1 
ATOM   2971  C  C     . LYS   A  1  410  ? -57.287 46.093  86.770  1.00 17.56 ? 408  LYS   A C     1 
ATOM   2972  O  O     . LYS   A  1  410  ? -58.479 46.366  86.605  1.00 19.27 ? 408  LYS   A O     1 
ATOM   2973  C  CB    . LYS   A  1  410  ? -56.080 46.534  88.924  1.00 19.05 ? 408  LYS   A CB    1 
ATOM   2974  C  CG    . LYS   A  1  410  ? -56.901 47.773  89.246  1.00 20.53 ? 408  LYS   A CG    1 
ATOM   2975  C  CD    . LYS   A  1  410  ? -56.096 48.781  90.050  1.00 21.99 ? 408  LYS   A CD    1 
ATOM   2976  C  CE    . LYS   A  1  410  ? -55.672 48.255  91.411  1.00 20.63 ? 408  LYS   A CE    1 
ATOM   2977  N  NZ    . LYS   A  1  410  ? -56.839 48.136  92.315  1.00 25.48 ? 408  LYS   A NZ    1 
ATOM   2978  N  N     . LEU   A  1  411  ? -56.367 46.328  85.831  1.00 17.28 ? 409  LEU   A N     1 
ATOM   2979  C  CA    . LEU   A  1  411  ? -56.750 46.863  84.532  1.00 17.01 ? 409  LEU   A CA    1 
ATOM   2980  C  C     . LEU   A  1  411  ? -57.677 45.916  83.785  1.00 16.48 ? 409  LEU   A C     1 
ATOM   2981  O  O     . LEU   A  1  411  ? -58.636 46.358  83.145  1.00 17.13 ? 409  LEU   A O     1 
ATOM   2982  C  CB    . LEU   A  1  411  ? -55.496 47.162  83.707  1.00 17.55 ? 409  LEU   A CB    1 
ATOM   2983  C  CG    . LEU   A  1  411  ? -54.804 48.441  84.155  1.00 17.10 ? 409  LEU   A CG    1 
ATOM   2984  C  CD1   . LEU   A  1  411  ? -53.374 48.511  83.605  1.00 17.89 ? 409  LEU   A CD1   1 
ATOM   2985  C  CD2   . LEU   A  1  411  ? -55.594 49.667  83.745  1.00 16.97 ? 409  LEU   A CD2   1 
ATOM   2986  N  N     . LEU   A  1  412  ? -57.399 44.610  83.833  1.00 16.91 ? 410  LEU   A N     1 
ATOM   2987  C  CA    . LEU   A  1  412  ? -58.208 43.680  83.056  1.00 18.01 ? 410  LEU   A CA    1 
ATOM   2988  C  C     . LEU   A  1  412  ? -59.613 43.540  83.609  1.00 20.69 ? 410  LEU   A C     1 
ATOM   2989  O  O     . LEU   A  1  412  ? -60.497 43.079  82.887  1.00 22.72 ? 410  LEU   A O     1 
ATOM   2990  C  CB    . LEU   A  1  412  ? -57.522 42.317  82.935  1.00 20.15 ? 410  LEU   A CB    1 
ATOM   2991  C  CG    . LEU   A  1  412  ? -56.327 42.303  81.970  1.00 18.88 ? 410  LEU   A CG    1 
ATOM   2992  C  CD1   . LEU   A  1  412  ? -55.583 40.993  82.075  1.00 23.91 ? 410  LEU   A CD1   1 
ATOM   2993  C  CD2   . LEU   A  1  412  ? -56.792 42.531  80.540  1.00 22.05 ? 410  LEU   A CD2   1 
ATOM   2994  N  N     . ALA   A  1  413  ? -59.844 43.942  84.854  1.00 18.55 ? 411  ALA   A N     1 
ATOM   2995  C  CA    . ALA   A  1  413  ? -61.198 43.963  85.393  1.00 18.92 ? 411  ALA   A CA    1 
ATOM   2996  C  C     . ALA   A  1  413  ? -61.958 45.224  85.017  1.00 22.03 ? 411  ALA   A C     1 
ATOM   2997  O  O     . ALA   A  1  413  ? -63.135 45.353  85.365  1.00 22.29 ? 411  ALA   A O     1 
ATOM   2998  C  CB    . ALA   A  1  413  ? -61.143 43.840  86.915  1.00 20.14 ? 411  ALA   A CB    1 
ATOM   2999  N  N     . ALA   A  1  414  ? -61.326 46.147  84.299  1.00 19.76 ? 412  ALA   A N     1 
ATOM   3000  C  CA    . ALA   A  1  414  ? -61.894 47.460  84.035  1.00 20.53 ? 412  ALA   A CA    1 
ATOM   3001  C  C     . ALA   A  1  414  ? -61.821 47.817  82.557  1.00 19.36 ? 412  ALA   A C     1 
ATOM   3002  O  O     . ALA   A  1  414  ? -61.826 48.992  82.203  1.00 18.33 ? 412  ALA   A O     1 
ATOM   3003  C  CB    . ALA   A  1  414  ? -61.220 48.536  84.890  1.00 21.73 ? 412  ALA   A CB    1 
ATOM   3004  N  N     . THR   A  1  415  ? -61.784 46.807  81.678  1.00 19.08 ? 413  THR   A N     1 
ATOM   3005  C  CA    . THR   A  1  415  ? -61.686 47.072  80.246  1.00 19.74 ? 413  THR   A CA    1 
ATOM   3006  C  C     . THR   A  1  415  ? -62.906 47.781  79.683  1.00 19.95 ? 413  THR   A C     1 
ATOM   3007  O  O     . THR   A  1  415  ? -62.828 48.328  78.577  1.00 21.50 ? 413  THR   A O     1 
ATOM   3008  C  CB    . THR   A  1  415  ? -61.408 45.793  79.449  1.00 22.28 ? 413  THR   A CB    1 
ATOM   3009  O  OG1   . THR   A  1  415  ? -62.469 44.853  79.651  1.00 24.44 ? 413  THR   A OG1   1 
ATOM   3010  C  CG2   . THR   A  1  415  ? -60.101 45.161  79.893  1.00 21.86 ? 413  THR   A CG2   1 
ATOM   3011  N  N     . ASP   A  1  416  ? -64.035 47.782  80.398  1.00 20.32 ? 414  ASP   A N     1 
ATOM   3012  C  CA    . ASP   A  1  416  ? -65.161 48.564  79.910  1.00 20.48 ? 414  ASP   A CA    1 
ATOM   3013  C  C     . ASP   A  1  416  ? -64.915 50.059  80.035  1.00 20.03 ? 414  ASP   A C     1 
ATOM   3014  O  O     . ASP   A  1  416  ? -65.487 50.835  79.264  1.00 25.82 ? 414  ASP   A O     1 
ATOM   3015  C  CB    . ASP   A  1  416  ? -66.450 48.165  80.631  1.00 23.70 ? 414  ASP   A CB    1 
ATOM   3016  C  CG    . ASP   A  1  416  ? -66.358 48.350  82.126  1.00 29.99 ? 414  ASP   A CG    1 
ATOM   3017  O  OD1   . ASP   A  1  416  ? -65.290 48.044  82.703  1.00 29.97 ? 414  ASP   A OD1   1 
ATOM   3018  O  OD2   . ASP   A  1  416  ? -67.355 48.816  82.728  1.00 37.41 ? 414  ASP   A OD2   1 
ATOM   3019  N  N     . VAL   A  1  417  ? -64.043 50.482  80.948  1.00 19.88 ? 415  VAL   A N     1 
ATOM   3020  C  CA    . VAL   A  1  417  ? -63.855 51.905  81.186  1.00 21.33 ? 415  VAL   A CA    1 
ATOM   3021  C  C     . VAL   A  1  417  ? -62.454 52.402  80.878  1.00 18.14 ? 415  VAL   A C     1 
ATOM   3022  O  O     . VAL   A  1  417  ? -62.284 53.617  80.716  1.00 19.01 ? 415  VAL   A O     1 
ATOM   3023  C  CB    . VAL   A  1  417  ? -64.287 52.338  82.599  1.00 27.05 ? 415  VAL   A CB    1 
ATOM   3024  C  CG1   . VAL   A  1  417  ? -65.747 52.006  82.816  1.00 28.28 ? 415  VAL   A CG1   1 
ATOM   3025  C  CG2   . VAL   A  1  417  ? -63.441 51.668  83.623  1.00 22.45 ? 415  VAL   A CG2   1 
ATOM   3026  N  N     . VAL   A  1  418  ? -61.444 51.529  80.801  1.00 16.64 ? 416  VAL   A N     1 
ATOM   3027  C  CA    . VAL   A  1  418  ? -60.111 51.900  80.348  1.00 16.01 ? 416  VAL   A CA    1 
ATOM   3028  C  C     . VAL   A  1  418  ? -59.668 50.914  79.282  1.00 16.51 ? 416  VAL   A C     1 
ATOM   3029  O  O     . VAL   A  1  418  ? -60.181 49.802  79.171  1.00 17.61 ? 416  VAL   A O     1 
ATOM   3030  C  CB    . VAL   A  1  418  ? -59.074 51.972  81.488  1.00 16.48 ? 416  VAL   A CB    1 
ATOM   3031  C  CG1   . VAL   A  1  418  ? -59.440 53.069  82.475  1.00 19.15 ? 416  VAL   A CG1   1 
ATOM   3032  C  CG2   . VAL   A  1  418  ? -58.938 50.635  82.184  1.00 19.29 ? 416  VAL   A CG2   1 
ATOM   3033  N  N     . PHE   A  1  419  ? -58.677 51.329  78.509  1.00 15.92 ? 417  PHE   A N     1 
ATOM   3034  C  CA    . PHE   A  1  419  ? -58.071 50.472  77.498  1.00 16.05 ? 417  PHE   A CA    1 
ATOM   3035  C  C     . PHE   A  1  419  ? -56.670 50.121  77.981  1.00 15.37 ? 417  PHE   A C     1 
ATOM   3036  O  O     . PHE   A  1  419  ? -55.750 50.953  77.875  1.00 16.43 ? 417  PHE   A O     1 
ATOM   3037  C  CB    . PHE   A  1  419  ? -58.011 51.211  76.157  1.00 15.73 ? 417  PHE   A CB    1 
ATOM   3038  C  CG    . PHE   A  1  419  ? -57.291 50.456  75.070  1.00 16.42 ? 417  PHE   A CG    1 
ATOM   3039  C  CD1   . PHE   A  1  419  ? -57.733 49.212  74.652  1.00 16.97 ? 417  PHE   A CD1   1 
ATOM   3040  C  CD2   . PHE   A  1  419  ? -56.184 51.009  74.449  1.00 15.59 ? 417  PHE   A CD2   1 
ATOM   3041  C  CE1   . PHE   A  1  419  ? -57.080 48.528  73.639  1.00 17.41 ? 417  PHE   A CE1   1 
ATOM   3042  C  CE2   . PHE   A  1  419  ? -55.527 50.329  73.433  1.00 16.45 ? 417  PHE   A CE2   1 
ATOM   3043  C  CZ    . PHE   A  1  419  ? -55.980 49.089  73.029  1.00 16.50 ? 417  PHE   A CZ    1 
ATOM   3044  N  N     . PRO   A  1  420  ? -56.450 48.928  78.525  1.00 15.26 ? 418  PRO   A N     1 
ATOM   3045  C  CA    . PRO   A  1  420  ? -55.112 48.598  79.029  1.00 16.46 ? 418  PRO   A CA    1 
ATOM   3046  C  C     . PRO   A  1  420  ? -54.149 48.329  77.893  1.00 15.89 ? 418  PRO   A C     1 
ATOM   3047  O  O     . PRO   A  1  420  ? -54.489 47.682  76.899  1.00 16.59 ? 418  PRO   A O     1 
ATOM   3048  C  CB    . PRO   A  1  420  ? -55.340 47.326  79.859  1.00 15.85 ? 418  PRO   A CB    1 
ATOM   3049  C  CG    . PRO   A  1  420  ? -56.844 47.290  80.098  1.00 14.56 ? 418  PRO   A CG    1 
ATOM   3050  C  CD    . PRO   A  1  420  ? -57.425 47.875  78.847  1.00 16.15 ? 418  PRO   A CD    1 
ATOM   3051  N  N     . GLN   A  1  421  ? -52.921 48.806  78.075  1.00 15.18 ? 419  GLN   A N     1 
ATOM   3052  C  CA    . GLN   A  1  421  ? -51.857 48.628  77.096  1.00 14.74 ? 419  GLN   A CA    1 
ATOM   3053  C  C     . GLN   A  1  421  ? -50.652 48.104  77.859  1.00 14.34 ? 419  GLN   A C     1 
ATOM   3054  O  O     . GLN   A  1  421  ? -50.062 48.826  78.665  1.00 16.37 ? 419  GLN   A O     1 
ATOM   3055  C  CB    . GLN   A  1  421  ? -51.548 49.954  76.416  1.00 13.92 ? 419  GLN   A CB    1 
ATOM   3056  C  CG    . GLN   A  1  421  ? -52.772 50.568  75.756  1.00 16.02 ? 419  GLN   A CG    1 
ATOM   3057  C  CD    . GLN   A  1  421  ? -52.561 52.019  75.452  1.00 14.92 ? 419  GLN   A CD    1 
ATOM   3058  O  OE1   . GLN   A  1  421  ? -52.351 52.822  76.357  1.00 16.51 ? 419  GLN   A OE1   1 
ATOM   3059  N  NE2   . GLN   A  1  421  ? -52.621 52.373  74.175  1.00 16.11 ? 419  GLN   A NE2   1 
ATOM   3060  N  N     . PHE   A  1  422  ? -50.312 46.847  77.640  1.00 14.28 ? 420  PHE   A N     1 
ATOM   3061  C  CA    . PHE   A  1  422  ? -49.292 46.188  78.444  1.00 13.88 ? 420  PHE   A CA    1 
ATOM   3062  C  C     . PHE   A  1  422  ? -47.956 46.271  77.717  1.00 14.23 ? 420  PHE   A C     1 
ATOM   3063  O  O     . PHE   A  1  422  ? -47.661 45.457  76.838  1.00 15.72 ? 420  PHE   A O     1 
ATOM   3064  C  CB    . PHE   A  1  422  ? -49.702 44.760  78.767  1.00 16.39 ? 420  PHE   A CB    1 
ATOM   3065  C  CG    . PHE   A  1  422  ? -51.006 44.686  79.502  1.00 17.28 ? 420  PHE   A CG    1 
ATOM   3066  C  CD1   . PHE   A  1  422  ? -51.098 45.177  80.791  1.00 18.89 ? 420  PHE   A CD1   1 
ATOM   3067  C  CD2   . PHE   A  1  422  ? -52.135 44.173  78.892  1.00 17.20 ? 420  PHE   A CD2   1 
ATOM   3068  C  CE1   . PHE   A  1  422  ? -52.297 45.131  81.471  1.00 18.32 ? 420  PHE   A CE1   1 
ATOM   3069  C  CE2   . PHE   A  1  422  ? -53.339 44.120  79.572  1.00 18.61 ? 420  PHE   A CE2   1 
ATOM   3070  C  CZ    . PHE   A  1  422  ? -53.406 44.603  80.863  1.00 18.83 ? 420  PHE   A CZ    1 
ATOM   3071  N  N     . ALA   A  1  423  ? -47.169 47.266  78.089  1.00 14.61 ? 421  ALA   A N     1 
ATOM   3072  C  CA    . ALA   A  1  423  ? -45.862 47.491  77.485  1.00 15.44 ? 421  ALA   A CA    1 
ATOM   3073  C  C     . ALA   A  1  423  ? -44.848 46.628  78.219  1.00 17.38 ? 421  ALA   A C     1 
ATOM   3074  O  O     . ALA   A  1  423  ? -44.556 46.868  79.394  1.00 17.78 ? 421  ALA   A O     1 
ATOM   3075  C  CB    . ALA   A  1  423  ? -45.499 48.965  77.603  1.00 15.88 ? 421  ALA   A CB    1 
ATOM   3076  N  N     . THR   A  1  424  ? -44.321 45.615  77.540  1.00 16.06 ? 422  THR   A N     1 
ATOM   3077  C  CA    . THR   A  1  424  ? -43.277 44.811  78.161  1.00 17.44 ? 422  THR   A CA    1 
ATOM   3078  C  C     . THR   A  1  424  ? -42.575 43.987  77.095  1.00 17.08 ? 422  THR   A C     1 
ATOM   3079  O  O     . THR   A  1  424  ? -43.181 43.561  76.108  1.00 18.58 ? 422  THR   A O     1 
ATOM   3080  C  CB    . THR   A  1  424  ? -43.828 43.882  79.246  1.00 19.10 ? 422  THR   A CB    1 
ATOM   3081  O  OG1   . THR   A  1  424  ? -42.728 43.193  79.861  1.00 19.17 ? 422  THR   A OG1   1 
ATOM   3082  C  CG2   . THR   A  1  424  ? -44.775 42.865  78.649  1.00 20.99 ? 422  THR   A CG2   1 
ATOM   3083  N  N     . HIS   A  1  425  ? -41.281 43.770  77.311  1.00 17.12 ? 423  HIS   A N     1 
ATOM   3084  C  CA    . HIS   A  1  425  ? -40.506 42.850  76.495  1.00 17.36 ? 423  HIS   A CA    1 
ATOM   3085  C  C     . HIS   A  1  425  ? -40.288 41.520  77.175  1.00 19.57 ? 423  HIS   A C     1 
ATOM   3086  O  O     . HIS   A  1  425  ? -39.586 40.668  76.626  1.00 21.62 ? 423  HIS   A O     1 
ATOM   3087  C  CB    . HIS   A  1  425  ? -39.160 43.473  76.149  1.00 18.51 ? 423  HIS   A CB    1 
ATOM   3088  C  CG    . HIS   A  1  425  ? -39.289 44.724  75.358  1.00 18.09 ? 423  HIS   A CG    1 
ATOM   3089  N  ND1   . HIS   A  1  425  ? -38.559 45.858  75.635  1.00 21.57 ? 423  HIS   A ND1   1 
ATOM   3090  C  CD2   . HIS   A  1  425  ? -40.100 45.034  74.320  1.00 19.26 ? 423  HIS   A CD2   1 
ATOM   3091  C  CE1   . HIS   A  1  425  ? -38.901 46.810  74.783  1.00 21.20 ? 423  HIS   A CE1   1 
ATOM   3092  N  NE2   . HIS   A  1  425  ? -39.832 46.334  73.975  1.00 18.61 ? 423  HIS   A NE2   1 
ATOM   3093  N  N     . ASN   A  1  426  ? -40.872 41.324  78.344  1.00 18.50 ? 424  ASN   A N     1 
ATOM   3094  C  CA    . ASN   A  1  426  ? -40.614 40.138  79.149  1.00 20.12 ? 424  ASN   A CA    1 
ATOM   3095  C  C     . ASN   A  1  426  ? -41.659 39.088  78.783  1.00 20.47 ? 424  ASN   A C     1 
ATOM   3096  O  O     . ASN   A  1  426  ? -42.857 39.284  79.014  1.00 19.99 ? 424  ASN   A O     1 
ATOM   3097  C  CB    . ASN   A  1  426  ? -40.667 40.543  80.619  1.00 20.79 ? 424  ASN   A CB    1 
ATOM   3098  C  CG    . ASN   A  1  426  ? -40.334 39.411  81.553  1.00 20.14 ? 424  ASN   A CG    1 
ATOM   3099  O  OD1   . ASN   A  1  426  ? -40.781 38.289  81.360  1.00 22.32 ? 424  ASN   A OD1   1 
ATOM   3100  N  ND2   . ASN   A  1  426  ? -39.563 39.714  82.597  1.00 22.02 ? 424  ASN   A ND2   1 
ATOM   3101  N  N     . ALA   A  1  427  ? -41.207 37.973  78.196  1.00 19.93 ? 425  ALA   A N     1 
ATOM   3102  C  CA    . ALA   A  1  427  ? -42.131 36.950  77.720  1.00 21.47 ? 425  ALA   A CA    1 
ATOM   3103  C  C     . ALA   A  1  427  ? -42.889 36.291  78.863  1.00 19.73 ? 425  ALA   A C     1 
ATOM   3104  O  O     . ALA   A  1  427  ? -44.011 35.814  78.662  1.00 21.03 ? 425  ALA   A O     1 
ATOM   3105  C  CB    . ALA   A  1  427  ? -41.374 35.885  76.923  1.00 24.67 ? 425  ALA   A CB    1 
ATOM   3106  N  N     . GLN   A  1  428  ? -42.298 36.246  80.057  1.00 20.71 ? 426  GLN   A N     1 
ATOM   3107  C  CA    . GLN   A  1  428  ? -43.014 35.710  81.209  1.00 24.11 ? 426  GLN   A CA    1 
ATOM   3108  C  C     . GLN   A  1  428  ? -44.151 36.639  81.601  1.00 20.75 ? 426  GLN   A C     1 
ATOM   3109  O  O     . GLN   A  1  428  ? -45.285 36.191  81.811  1.00 21.06 ? 426  GLN   A O     1 
ATOM   3110  C  CB    . GLN   A  1  428  ? -42.055 35.507  82.384  1.00 21.26 ? 426  GLN   A CB    1 
ATOM   3111  C  CG    . GLN   A  1  428  ? -42.605 34.603  83.489  1.00 22.68 ? 426  GLN   A CG    1 
ATOM   3112  C  CD    . GLN   A  1  428  ? -43.691 35.257  84.336  1.00 27.64 ? 426  GLN   A CD    1 
ATOM   3113  O  OE1   . GLN   A  1  428  ? -43.648 36.460  84.613  1.00 27.58 ? 426  GLN   A OE1   1 
ATOM   3114  N  NE2   . GLN   A  1  428  ? -44.674 34.461  84.754  1.00 25.38 ? 426  GLN   A NE2   1 
ATOM   3115  N  N     . THR   A  1  429  ? -43.853 37.936  81.724  1.00 20.55 ? 427  THR   A N     1 
ATOM   3116  C  CA    . THR   A  1  429  ? -44.894 38.922  81.996  1.00 19.91 ? 427  THR   A CA    1 
ATOM   3117  C  C     . THR   A  1  429  ? -45.992 38.838  80.951  1.00 21.08 ? 427  THR   A C     1 
ATOM   3118  O  O     . THR   A  1  429  ? -47.183 38.782  81.283  1.00 20.42 ? 427  THR   A O     1 
ATOM   3119  C  CB    . THR   A  1  429  ? -44.285 40.324  81.974  1.00 20.66 ? 427  THR   A CB    1 
ATOM   3120  O  OG1   . THR   A  1  429  ? -43.116 40.357  82.794  1.00 20.60 ? 427  THR   A OG1   1 
ATOM   3121  C  CG2   . THR   A  1  429  ? -45.281 41.333  82.511  1.00 21.23 ? 427  THR   A CG2   1 
ATOM   3122  N  N     . LEU   A  1  430  ? -45.603 38.813  79.678  1.00 19.41 ? 428  LEU   A N     1 
ATOM   3123  C  CA    . LEU   A  1  430  ? -46.566 38.769  78.586  1.00 21.92 ? 428  LEU   A CA    1 
ATOM   3124  C  C     . LEU   A  1  430  ? -47.468 37.551  78.712  1.00 21.96 ? 428  LEU   A C     1 
ATOM   3125  O  O     . LEU   A  1  430  ? -48.699 37.655  78.642  1.00 21.24 ? 428  LEU   A O     1 
ATOM   3126  C  CB    . LEU   A  1  430  ? -45.792 38.729  77.267  1.00 19.03 ? 428  LEU   A CB    1 
ATOM   3127  C  CG    . LEU   A  1  430  ? -46.457 38.945  75.905  1.00 23.10 ? 428  LEU   A CG    1 
ATOM   3128  C  CD1   . LEU   A  1  430  ? -45.333 39.077  74.894  1.00 26.23 ? 428  LEU   A CD1   1 
ATOM   3129  C  CD2   . LEU   A  1  430  ? -47.382 37.803  75.505  1.00 25.67 ? 428  LEU   A CD2   1 
ATOM   3130  N  N     . ALA   A  1  431  ? -46.864 36.379  78.898  1.00 22.70 ? 429  ALA   A N     1 
ATOM   3131  C  CA    . ALA   A  1  431  ? -47.636 35.145  78.965  1.00 23.75 ? 429  ALA   A CA    1 
ATOM   3132  C  C     . ALA   A  1  431  ? -48.605 35.155  80.138  1.00 21.91 ? 429  ALA   A C     1 
ATOM   3133  O  O     . ALA   A  1  431  ? -49.753 34.713  80.006  1.00 21.84 ? 429  ALA   A O     1 
ATOM   3134  C  CB    . ALA   A  1  431  ? -46.686 33.955  79.080  1.00 23.66 ? 429  ALA   A CB    1 
ATOM   3135  N  N     . ALA   A  1  432  ? -48.162 35.660  81.293  1.00 22.29 ? 430  ALA   A N     1 
ATOM   3136  C  CA    . ALA   A  1  432  ? -49.038 35.723  82.459  1.00 22.98 ? 430  ALA   A CA    1 
ATOM   3137  C  C     . ALA   A  1  432  ? -50.272 36.558  82.166  1.00 21.54 ? 430  ALA   A C     1 
ATOM   3138  O  O     . ALA   A  1  432  ? -51.389 36.191  82.551  1.00 23.20 ? 430  ALA   A O     1 
ATOM   3139  C  CB    . ALA   A  1  432  ? -48.279 36.299  83.655  1.00 23.18 ? 430  ALA   A CB    1 
ATOM   3140  N  N     . ILE   A  1  433  ? -50.096 37.670  81.460  1.00 21.16 ? 431  ILE   A N     1 
ATOM   3141  C  CA    . ILE   A  1  433  ? -51.217 38.554  81.185  1.00 19.68 ? 431  ILE   A CA    1 
ATOM   3142  C  C     . ILE   A  1  433  ? -52.080 37.999  80.070  1.00 21.22 ? 431  ILE   A C     1 
ATOM   3143  O  O     . ILE   A  1  433  ? -53.307 38.100  80.115  1.00 21.29 ? 431  ILE   A O     1 
ATOM   3144  C  CB    . ILE   A  1  433  ? -50.672 39.952  80.862  1.00 20.50 ? 431  ILE   A CB    1 
ATOM   3145  C  CG1   . ILE   A  1  433  ? -50.041 40.539  82.121  1.00 25.42 ? 431  ILE   A CG1   1 
ATOM   3146  C  CG2   . ILE   A  1  433  ? -51.763 40.838  80.295  1.00 21.11 ? 431  ILE   A CG2   1 
ATOM   3147  C  CD1   . ILE   A  1  433  ? -49.312 41.795  81.880  1.00 24.62 ? 431  ILE   A CD1   1 
ATOM   3148  N  N     . TYR   A  1  434  ? -51.453 37.412  79.051  1.00 22.21 ? 432  TYR   A N     1 
ATOM   3149  C  CA    . TYR   A  1  434  ? -52.212 36.803  77.968  1.00 21.65 ? 432  TYR   A CA    1 
ATOM   3150  C  C     . TYR   A  1  434  ? -53.202 35.779  78.505  1.00 23.06 ? 432  TYR   A C     1 
ATOM   3151  O  O     . TYR   A  1  434  ? -54.360 35.726  78.068  1.00 24.91 ? 432  TYR   A O     1 
ATOM   3152  C  CB    . TYR   A  1  434  ? -51.229 36.153  76.997  1.00 23.16 ? 432  TYR   A CB    1 
ATOM   3153  C  CG    . TYR   A  1  434  ? -51.845 35.235  75.982  1.00 24.26 ? 432  TYR   A CG    1 
ATOM   3154  C  CD1   . TYR   A  1  434  ? -52.654 35.728  74.965  1.00 25.21 ? 432  TYR   A CD1   1 
ATOM   3155  C  CD2   . TYR   A  1  434  ? -51.602 33.868  76.030  1.00 28.22 ? 432  TYR   A CD2   1 
ATOM   3156  C  CE1   . TYR   A  1  434  ? -53.209 34.883  74.033  1.00 25.37 ? 432  TYR   A CE1   1 
ATOM   3157  C  CE2   . TYR   A  1  434  ? -52.146 33.017  75.103  1.00 27.56 ? 432  TYR   A CE2   1 
ATOM   3158  C  CZ    . TYR   A  1  434  ? -52.950 33.523  74.109  1.00 30.70 ? 432  TYR   A CZ    1 
ATOM   3159  O  OH    . TYR   A  1  434  ? -53.489 32.660  73.190  1.00 31.88 ? 432  TYR   A OH    1 
ATOM   3160  N  N     . HIS   A  1  435  ? -52.767 34.960  79.458  1.00 23.26 ? 433  HIS   A N     1 
ATOM   3161  C  CA    . HIS   A  1  435  ? -53.665 33.965  80.027  1.00 24.66 ? 433  HIS   A CA    1 
ATOM   3162  C  C     . HIS   A  1  435  ? -54.610 34.575  81.047  1.00 24.87 ? 433  HIS   A C     1 
ATOM   3163  O  O     . HIS   A  1  435  ? -55.765 34.145  81.145  1.00 24.35 ? 433  HIS   A O     1 
ATOM   3164  C  CB    . HIS   A  1  435  ? -52.863 32.809  80.613  1.00 26.81 ? 433  HIS   A CB    1 
ATOM   3165  C  CG    . HIS   A  1  435  ? -52.241 31.943  79.567  1.00 28.49 ? 433  HIS   A CG    1 
ATOM   3166  N  ND1   . HIS   A  1  435  ? -52.922 30.911  78.960  1.00 30.30 ? 433  HIS   A ND1   1 
ATOM   3167  C  CD2   . HIS   A  1  435  ? -51.024 31.991  78.977  1.00 25.78 ? 433  HIS   A CD2   1 
ATOM   3168  C  CE1   . HIS   A  1  435  ? -52.139 30.338  78.063  1.00 28.89 ? 433  HIS   A CE1   1 
ATOM   3169  N  NE2   . HIS   A  1  435  ? -50.982 30.973  78.054  1.00 25.67 ? 433  HIS   A NE2   1 
ATOM   3170  N  N     . MET   A  1  436  ? -54.149 35.585  81.788  1.00 23.16 ? 434  MET   A N     1 
ATOM   3171  C  CA    . MET   A  1  436  ? -55.041 36.292  82.701  1.00 24.44 ? 434  MET   A CA    1 
ATOM   3172  C  C     . MET   A  1  436  ? -56.204 36.924  81.953  1.00 22.25 ? 434  MET   A C     1 
ATOM   3173  O  O     . MET   A  1  436  ? -57.338 36.940  82.448  1.00 24.39 ? 434  MET   A O     1 
ATOM   3174  C  CB    . MET   A  1  436  ? -54.258 37.366  83.442  1.00 23.86 ? 434  MET   A CB    1 
ATOM   3175  C  CG    . MET   A  1  436  ? -55.061 38.076  84.496  1.00 23.14 ? 434  MET   A CG    1 
ATOM   3176  S  SD    . MET   A  1  436  ? -54.157 39.485  85.129  1.00 24.30 ? 434  MET   A SD    1 
ATOM   3177  C  CE    . MET   A  1  436  ? -52.895 38.669  86.092  1.00 25.98 ? 434  MET   A CE    1 
ATOM   3178  N  N     . ALA   A  1  437  ? -55.947 37.448  80.752  1.00 21.79 ? 435  ALA   A N     1 
ATOM   3179  C  CA    . ALA   A  1  437  ? -56.989 38.144  80.008  1.00 25.14 ? 435  ALA   A CA    1 
ATOM   3180  C  C     . ALA   A  1  437  ? -58.017 37.181  79.440  1.00 28.03 ? 435  ALA   A C     1 
ATOM   3181  O  O     . ALA   A  1  437  ? -59.170 37.567  79.230  1.00 27.49 ? 435  ALA   A O     1 
ATOM   3182  C  CB    . ALA   A  1  437  ? -56.373 38.970  78.885  1.00 25.53 ? 435  ALA   A CB    1 
ATOM   3183  N  N     . GLY   A  1  438  ? -57.625 35.938  79.177  1.00 29.80 ? 436  GLY   A N     1 
ATOM   3184  C  CA    . GLY   A  1  438  ? -58.571 34.924  78.759  1.00 31.30 ? 436  GLY   A CA    1 
ATOM   3185  C  C     . GLY   A  1  438  ? -58.817 34.912  77.268  1.00 31.37 ? 436  GLY   A C     1 
ATOM   3186  O  O     . GLY   A  1  438  ? -58.236 35.671  76.489  1.00 29.25 ? 436  GLY   A O     1 
ATOM   3187  N  N     . LYS   A  1  439  ? -59.739 34.025  76.874  1.00 35.61 ? 437  LYS   A N     1 
ATOM   3188  C  CA    . LYS   A  1  439  ? -59.950 33.713  75.465  1.00 39.59 ? 437  LYS   A CA    1 
ATOM   3189  C  C     . LYS   A  1  439  ? -60.832 34.732  74.756  1.00 35.54 ? 437  LYS   A C     1 
ATOM   3190  O  O     . LYS   A  1  439  ? -60.737 34.872  73.532  1.00 42.82 ? 437  LYS   A O     1 
ATOM   3191  C  CB    . LYS   A  1  439  ? -60.546 32.311  75.318  1.00 45.80 ? 437  LYS   A CB    1 
ATOM   3192  N  N     . ASP   A  1  440  ? -61.689 35.441  75.485  1.00 34.28 ? 438  ASP   A N     1 
ATOM   3193  C  CA    . ASP   A  1  440  ? -62.549 36.443  74.865  1.00 38.73 ? 438  ASP   A CA    1 
ATOM   3194  C  C     . ASP   A  1  440  ? -61.715 37.666  74.521  1.00 37.41 ? 438  ASP   A C     1 
ATOM   3195  O  O     . ASP   A  1  440  ? -61.237 38.371  75.416  1.00 37.20 ? 438  ASP   A O     1 
ATOM   3196  C  CB    . ASP   A  1  440  ? -63.686 36.820  75.810  1.00 40.34 ? 438  ASP   A CB    1 
ATOM   3197  C  CG    . ASP   A  1  440  ? -64.756 35.754  75.881  1.00 45.94 ? 438  ASP   A CG    1 
ATOM   3198  O  OD1   . ASP   A  1  440  ? -64.638 34.749  75.148  1.00 42.82 ? 438  ASP   A OD1   1 
ATOM   3199  O  OD2   . ASP   A  1  440  ? -65.713 35.922  76.667  1.00 47.64 ? 438  ASP   A OD2   1 
ATOM   3200  N  N     . PHE   A  1  441  ? -61.531 37.923  73.230  1.00 28.98 ? 439  PHE   A N     1 
ATOM   3201  C  CA    . PHE   A  1  441  ? -60.757 39.083  72.822  1.00 27.45 ? 439  PHE   A CA    1 
ATOM   3202  C  C     . PHE   A  1  441  ? -61.390 39.760  71.619  1.00 28.46 ? 439  PHE   A C     1 
ATOM   3203  O  O     . PHE   A  1  441  ? -61.910 39.101  70.716  1.00 29.93 ? 439  PHE   A O     1 
ATOM   3204  C  CB    . PHE   A  1  441  ? -59.294 38.756  72.490  1.00 23.71 ? 439  PHE   A CB    1 
ATOM   3205  C  CG    . PHE   A  1  441  ? -58.489 39.979  72.182  1.00 23.85 ? 439  PHE   A CG    1 
ATOM   3206  C  CD1   . PHE   A  1  441  ? -58.010 40.777  73.210  1.00 22.18 ? 439  PHE   A CD1   1 
ATOM   3207  C  CD2   . PHE   A  1  441  ? -58.268 40.373  70.874  1.00 24.39 ? 439  PHE   A CD2   1 
ATOM   3208  C  CE1   . PHE   A  1  441  ? -57.300 41.929  72.942  1.00 21.00 ? 439  PHE   A CE1   1 
ATOM   3209  C  CE2   . PHE   A  1  441  ? -57.560 41.528  70.603  1.00 22.75 ? 439  PHE   A CE2   1 
ATOM   3210  C  CZ    . PHE   A  1  441  ? -57.084 42.309  71.642  1.00 20.68 ? 439  PHE   A CZ    1 
ATOM   3211  N  N     . HIS   A  1  442  ? -61.325 41.085  71.616  1.00 25.86 ? 440  HIS   A N     1 
ATOM   3212  C  CA    . HIS   A  1  442  ? -61.665 41.883  70.452  1.00 27.35 ? 440  HIS   A CA    1 
ATOM   3213  C  C     . HIS   A  1  442  ? -60.690 43.043  70.409  1.00 26.81 ? 440  HIS   A C     1 
ATOM   3214  O  O     . HIS   A  1  442  ? -60.206 43.492  71.452  1.00 22.57 ? 440  HIS   A O     1 
ATOM   3215  C  CB    . HIS   A  1  442  ? -63.106 42.412  70.514  1.00 26.63 ? 440  HIS   A CB    1 
ATOM   3216  C  CG    . HIS   A  1  442  ? -63.396 43.255  71.719  1.00 22.87 ? 440  HIS   A CG    1 
ATOM   3217  N  ND1   . HIS   A  1  442  ? -63.792 42.717  72.926  1.00 26.72 ? 440  HIS   A ND1   1 
ATOM   3218  C  CD2   . HIS   A  1  442  ? -63.355 44.596  71.898  1.00 26.24 ? 440  HIS   A CD2   1 
ATOM   3219  C  CE1   . HIS   A  1  442  ? -63.979 43.694  73.797  1.00 24.26 ? 440  HIS   A CE1   1 
ATOM   3220  N  NE2   . HIS   A  1  442  ? -63.717 44.841  73.199  1.00 24.39 ? 440  HIS   A NE2   1 
ATOM   3221  N  N     . VAL   A  1  443  ? -60.372 43.503  69.197  1.00 27.75 ? 441  VAL   A N     1 
ATOM   3222  C  CA    . VAL   A  1  443  ? -59.528 44.683  69.085  1.00 28.32 ? 441  VAL   A CA    1 
ATOM   3223  C  C     . VAL   A  1  443  ? -60.227 45.835  69.787  1.00 24.45 ? 441  VAL   A C     1 
ATOM   3224  O  O     . VAL   A  1  443  ? -61.434 46.057  69.610  1.00 25.89 ? 441  VAL   A O     1 
ATOM   3225  C  CB    . VAL   A  1  443  ? -59.192 44.987  67.616  1.00 29.95 ? 441  VAL   A CB    1 
ATOM   3226  C  CG1   . VAL   A  1  443  ? -58.582 46.369  67.490  1.00 30.62 ? 441  VAL   A CG1   1 
ATOM   3227  C  CG2   . VAL   A  1  443  ? -58.222 43.945  67.077  1.00 35.98 ? 441  VAL   A CG2   1 
ATOM   3228  N  N     . GLY   A  1  444  ? -59.476 46.550  70.618  1.00 23.46 ? 442  GLY   A N     1 
ATOM   3229  C  CA    . GLY   A  1  444  ? -60.029 47.538  71.512  1.00 20.98 ? 442  GLY   A CA    1 
ATOM   3230  C  C     . GLY   A  1  444  ? -60.196 47.068  72.941  1.00 18.46 ? 442  GLY   A C     1 
ATOM   3231  O  O     . GLY   A  1  444  ? -60.430 47.898  73.824  1.00 19.06 ? 442  GLY   A O     1 
ATOM   3232  N  N     . LYS   A  1  445  ? -60.092 45.769  73.203  1.00 18.10 ? 443  LYS   A N     1 
ATOM   3233  C  CA    . LYS   A  1  445  ? -60.226 45.325  74.583  1.00 18.05 ? 443  LYS   A CA    1 
ATOM   3234  C  C     . LYS   A  1  445  ? -58.984 45.679  75.385  1.00 19.30 ? 443  LYS   A C     1 
ATOM   3235  O  O     . LYS   A  1  445  ? -59.069 46.323  76.436  1.00 19.37 ? 443  LYS   A O     1 
ATOM   3236  C  CB    . LYS   A  1  445  ? -60.501 43.831  74.650  1.00 20.73 ? 443  LYS   A CB    1 
ATOM   3237  C  CG    . LYS   A  1  445  ? -60.851 43.398  76.064  1.00 24.26 ? 443  LYS   A CG    1 
ATOM   3238  C  CD    . LYS   A  1  445  ? -61.249 41.950  76.163  1.00 29.66 ? 443  LYS   A CD    1 
ATOM   3239  C  CE    . LYS   A  1  445  ? -62.090 41.745  77.418  1.00 30.17 ? 443  LYS   A CE    1 
ATOM   3240  N  NZ    . LYS   A  1  445  ? -62.467 40.317  77.606  1.00 37.39 ? 443  LYS   A NZ    1 
ATOM   3241  N  N     . TYR   A  1  446  ? -57.819 45.257  74.900  1.00 17.79 ? 444  TYR   A N     1 
ATOM   3242  C  CA    . TYR   A  1  446  ? -56.532 45.659  75.444  1.00 17.93 ? 444  TYR   A CA    1 
ATOM   3243  C  C     . TYR   A  1  446  ? -55.527 45.423  74.331  1.00 18.85 ? 444  TYR   A C     1 
ATOM   3244  O  O     . TYR   A  1  446  ? -55.858 44.862  73.286  1.00 17.58 ? 444  TYR   A O     1 
ATOM   3245  C  CB    . TYR   A  1  446  ? -56.194 44.857  76.706  1.00 17.17 ? 444  TYR   A CB    1 
ATOM   3246  C  CG    . TYR   A  1  446  ? -55.793 43.416  76.452  1.00 19.95 ? 444  TYR   A CG    1 
ATOM   3247  C  CD1   . TYR   A  1  446  ? -56.739 42.389  76.419  1.00 26.96 ? 444  TYR   A CD1   1 
ATOM   3248  C  CD2   . TYR   A  1  446  ? -54.464 43.087  76.249  1.00 23.69 ? 444  TYR   A CD2   1 
ATOM   3249  C  CE1   . TYR   A  1  446  ? -56.344 41.069  76.188  1.00 23.20 ? 444  TYR   A CE1   1 
ATOM   3250  C  CE2   . TYR   A  1  446  ? -54.070 41.791  76.020  1.00 27.85 ? 444  TYR   A CE2   1 
ATOM   3251  C  CZ    . TYR   A  1  446  ? -55.006 40.791  75.986  1.00 27.13 ? 444  TYR   A CZ    1 
ATOM   3252  O  OH    . TYR   A  1  446  ? -54.576 39.499  75.760  1.00 35.79 ? 444  TYR   A OH    1 
ATOM   3253  N  N     . GLU   A  1  447  ? -54.292 45.850  74.555  1.00 15.96 ? 445  GLU   A N     1 
ATOM   3254  C  CA    . GLU   A  1  447  ? -53.232 45.512  73.620  1.00 16.39 ? 445  GLU   A CA    1 
ATOM   3255  C  C     . GLU   A  1  447  ? -51.953 45.354  74.409  1.00 17.39 ? 445  GLU   A C     1 
ATOM   3256  O  O     . GLU   A  1  447  ? -51.875 45.713  75.582  1.00 16.76 ? 445  GLU   A O     1 
ATOM   3257  C  CB    . GLU   A  1  447  ? -53.038 46.595  72.556  1.00 16.78 ? 445  GLU   A CB    1 
ATOM   3258  C  CG    . GLU   A  1  447  ? -52.583 47.912  73.142  1.00 16.91 ? 445  GLU   A CG    1 
ATOM   3259  C  CD    . GLU   A  1  447  ? -52.518 49.035  72.132  1.00 16.79 ? 445  GLU   A CD    1 
ATOM   3260  O  OE1   . GLU   A  1  447  ? -53.050 48.876  71.010  1.00 18.27 ? 445  GLU   A OE1   1 
ATOM   3261  O  OE2   . GLU   A  1  447  ? -51.945 50.093  72.482  1.00 16.63 ? 445  GLU   A OE2   1 
ATOM   3262  N  N     . PHE   A  1  448  ? -50.945 44.812  73.744  1.00 16.36 ? 446  PHE   A N     1 
ATOM   3263  C  CA    . PHE   A  1  448  ? -49.581 44.856  74.235  1.00 16.18 ? 446  PHE   A CA    1 
ATOM   3264  C  C     . PHE   A  1  448  ? -48.851 46.007  73.566  1.00 14.66 ? 446  PHE   A C     1 
ATOM   3265  O  O     . PHE   A  1  448  ? -49.314 46.579  72.580  1.00 16.85 ? 446  PHE   A O     1 
ATOM   3266  C  CB    . PHE   A  1  448  ? -48.875 43.539  73.921  1.00 17.98 ? 446  PHE   A CB    1 
ATOM   3267  C  CG    . PHE   A  1  448  ? -49.424 42.376  74.674  1.00 19.06 ? 446  PHE   A CG    1 
ATOM   3268  C  CD1   . PHE   A  1  448  ? -49.090 42.190  76.003  1.00 18.17 ? 446  PHE   A CD1   1 
ATOM   3269  C  CD2   . PHE   A  1  448  ? -50.289 41.482  74.064  1.00 20.16 ? 446  PHE   A CD2   1 
ATOM   3270  C  CE1   . PHE   A  1  448  ? -49.603 41.128  76.717  1.00 23.09 ? 446  PHE   A CE1   1 
ATOM   3271  C  CE2   . PHE   A  1  448  ? -50.806 40.412  74.771  1.00 23.08 ? 446  PHE   A CE2   1 
ATOM   3272  C  CZ    . PHE   A  1  448  ? -50.461 40.235  76.099  1.00 21.21 ? 446  PHE   A CZ    1 
ATOM   3273  N  N     . GLN   A  1  449  ? -47.695 46.349  74.116  1.00 15.51 ? 447  GLN   A N     1 
ATOM   3274  C  CA    . GLN   A  1  449  ? -46.841 47.343  73.491  1.00 15.62 ? 447  GLN   A CA    1 
ATOM   3275  C  C     . GLN   A  1  449  ? -45.395 46.929  73.630  1.00 17.28 ? 447  GLN   A C     1 
ATOM   3276  O  O     . GLN   A  1  449  ? -45.017 46.203  74.552  1.00 17.52 ? 447  GLN   A O     1 
ATOM   3277  C  CB    . GLN   A  1  449  ? -47.007 48.737  74.077  1.00 15.07 ? 447  GLN   A CB    1 
ATOM   3278  C  CG    . GLN   A  1  449  ? -48.429 49.243  73.990  1.00 14.27 ? 447  GLN   A CG    1 
ATOM   3279  C  CD    . GLN   A  1  449  ? -48.515 50.727  74.200  1.00 16.60 ? 447  GLN   A CD    1 
ATOM   3280  O  OE1   . GLN   A  1  449  ? -47.567 51.353  74.680  1.00 17.51 ? 447  GLN   A OE1   1 
ATOM   3281  N  NE2   . GLN   A  1  449  ? -49.648 51.308  73.850  1.00 15.76 ? 447  GLN   A NE2   1 
ATOM   3282  N  N     . CYS   A  1  450  ? -44.592 47.409  72.693  1.00 15.61 ? 448  CYS   A N     1 
ATOM   3283  C  CA    . CYS   A  1  450  ? -43.173 47.122  72.717  1.00 15.69 ? 448  CYS   A CA    1 
ATOM   3284  C  C     . CYS   A  1  450  ? -42.433 48.295  72.104  1.00 16.78 ? 448  CYS   A C     1 
ATOM   3285  O  O     . CYS   A  1  450  ? -43.028 49.201  71.513  1.00 17.09 ? 448  CYS   A O     1 
ATOM   3286  C  CB    . CYS   A  1  450  ? -42.852 45.823  71.979  1.00 18.12 ? 448  CYS   A CB    1 
ATOM   3287  S  SG    . CYS   A  1  450  ? -42.944 45.949  70.190  1.00 19.72 ? 448  CYS   A SG    1 
ATOM   3288  N  N     . LEU   A  1  451  ? -41.114 48.262  72.250  1.00 16.49 ? 449  LEU   A N     1 
ATOM   3289  C  CA    . LEU   A  1  451  ? -40.264 49.299  71.702  1.00 19.30 ? 449  LEU   A CA    1 
ATOM   3290  C  C     . LEU   A  1  451  ? -39.771 48.898  70.320  1.00 18.08 ? 449  LEU   A C     1 
ATOM   3291  O  O     . LEU   A  1  451  ? -39.390 47.746  70.090  1.00 18.60 ? 449  LEU   A O     1 
ATOM   3292  C  CB    . LEU   A  1  451  ? -39.066 49.499  72.624  1.00 19.89 ? 449  LEU   A CB    1 
ATOM   3293  C  CG    . LEU   A  1  451  ? -38.022 50.510  72.168  1.00 22.15 ? 449  LEU   A CG    1 
ATOM   3294  C  CD1   . LEU   A  1  451  ? -38.600 51.918  72.109  1.00 22.86 ? 449  LEU   A CD1   1 
ATOM   3295  C  CD2   . LEU   A  1  451  ? -36.830 50.439  73.125  1.00 21.79 ? 449  LEU   A CD2   1 
ATOM   3296  N  N     . HIS   A  1  452  ? -39.798 49.857  69.397  1.00 17.54 ? 450  HIS   A N     1 
ATOM   3297  C  CA    . HIS   A  1  452  ? -39.232 49.645  68.068  1.00 18.84 ? 450  HIS   A CA    1 
ATOM   3298  C  C     . HIS   A  1  452  ? -37.793 49.154  68.150  1.00 20.94 ? 450  HIS   A C     1 
ATOM   3299  O  O     . HIS   A  1  452  ? -37.013 49.611  68.985  1.00 22.20 ? 450  HIS   A O     1 
ATOM   3300  C  CB    . HIS   A  1  452  ? -39.253 50.969  67.306  1.00 18.67 ? 450  HIS   A CB    1 
ATOM   3301  C  CG    . HIS   A  1  452  ? -38.471 50.931  66.035  1.00 16.91 ? 450  HIS   A CG    1 
ATOM   3302  N  ND1   . HIS   A  1  452  ? -39.002 50.476  64.847  1.00 18.96 ? 450  HIS   A ND1   1 
ATOM   3303  C  CD2   . HIS   A  1  452  ? -37.183 51.257  65.775  1.00 20.79 ? 450  HIS   A CD2   1 
ATOM   3304  C  CE1   . HIS   A  1  452  ? -38.081 50.549  63.903  1.00 21.18 ? 450  HIS   A CE1   1 
ATOM   3305  N  NE2   . HIS   A  1  452  ? -36.966 51.006  64.443  1.00 20.69 ? 450  HIS   A NE2   1 
ATOM   3306  N  N     . GLY   A  1  453  ? -37.444 48.228  67.262  1.00 23.24 ? 451  GLY   A N     1 
ATOM   3307  C  CA    . GLY   A  1  453  ? -36.069 47.763  67.219  1.00 25.52 ? 451  GLY   A CA    1 
ATOM   3308  C  C     . GLY   A  1  453  ? -35.633 47.024  68.459  1.00 33.02 ? 451  GLY   A C     1 
ATOM   3309  O  O     . GLY   A  1  453  ? -34.432 46.944  68.741  1.00 32.38 ? 451  GLY   A O     1 
ATOM   3310  N  N     . MET   A  1  454  ? -36.582 46.487  69.217  1.00 25.17 ? 452  MET   A N     1 
ATOM   3311  C  CA    . MET   A  1  454  ? -36.273 45.733  70.421  1.00 22.07 ? 452  MET   A CA    1 
ATOM   3312  C  C     . MET   A  1  454  ? -37.324 44.655  70.625  1.00 23.36 ? 452  MET   A C     1 
ATOM   3313  O  O     . MET   A  1  454  ? -36.998 43.481  70.823  1.00 24.89 ? 452  MET   A O     1 
ATOM   3314  C  CB    . MET   A  1  454  ? -36.227 46.657  71.636  1.00 22.48 ? 452  MET   A CB    1 
ATOM   3315  C  CG    . MET   A  1  454  ? -36.123 45.912  72.951  1.00 24.44 ? 452  MET   A CG    1 
ATOM   3316  S  SD    . MET   A  1  454  ? -34.628 44.905  73.003  1.00 30.04 ? 452  MET   A SD    1 
ATOM   3317  C  CE    . MET   A  1  454  ? -33.377 46.183  72.966  1.00 30.81 ? 452  MET   A CE    1 
ATOM   3318  N  N     . GLY   A  1  455  ? -38.592 45.041  70.558  1.00 21.97 ? 453  GLY   A N     1 
ATOM   3319  C  CA    . GLY   A  1  455  ? -39.655 44.115  70.892  1.00 22.40 ? 453  GLY   A CA    1 
ATOM   3320  C  C     . GLY   A  1  455  ? -40.236 43.314  69.756  1.00 22.66 ? 453  GLY   A C     1 
ATOM   3321  O  O     . GLY   A  1  455  ? -41.017 42.390  70.009  1.00 23.31 ? 453  GLY   A O     1 
ATOM   3322  N  N     . GLU   A  1  456  ? -39.896 43.640  68.510  1.00 25.00 ? 454  GLU   A N     1 
ATOM   3323  C  CA    . GLU   A  1  456  ? -40.502 42.936  67.383  1.00 25.76 ? 454  GLU   A CA    1 
ATOM   3324  C  C     . GLU   A  1  456  ? -40.248 41.437  67.377  1.00 27.86 ? 454  GLU   A C     1 
ATOM   3325  O  O     . GLU   A  1  456  ? -41.192 40.690  67.066  1.00 26.37 ? 454  GLU   A O     1 
ATOM   3326  C  CB    . GLU   A  1  456  ? -40.105 43.565  66.041  1.00 27.91 ? 454  GLU   A CB    1 
ATOM   3327  C  CG    . GLU   A  1  456  ? -40.576 44.985  65.861  1.00 31.47 ? 454  GLU   A CG    1 
ATOM   3328  C  CD    . GLU   A  1  456  ? -39.505 45.970  66.230  1.00 30.86 ? 454  GLU   A CD    1 
ATOM   3329  O  OE1   . GLU   A  1  456  ? -38.614 45.596  67.030  1.00 28.84 ? 454  GLU   A OE1   1 
ATOM   3330  O  OE2   . GLU   A  1  456  ? -39.540 47.106  65.709  1.00 29.26 ? 454  GLU   A OE2   1 
ATOM   3331  N  N     . PRO   A  1  457  ? -39.038 40.933  67.658  1.00 27.07 ? 455  PRO   A N     1 
ATOM   3332  C  CA    . PRO   A  1  457  ? -38.866 39.471  67.685  1.00 29.20 ? 455  PRO   A CA    1 
ATOM   3333  C  C     . PRO   A  1  457  ? -39.840 38.770  68.614  1.00 25.81 ? 455  PRO   A C     1 
ATOM   3334  O  O     . PRO   A  1  457  ? -40.408 37.739  68.236  1.00 28.81 ? 455  PRO   A O     1 
ATOM   3335  C  CB    . PRO   A  1  457  ? -37.402 39.293  68.115  1.00 28.89 ? 455  PRO   A CB    1 
ATOM   3336  C  CG    . PRO   A  1  457  ? -36.730 40.542  67.658  1.00 30.41 ? 455  PRO   A CG    1 
ATOM   3337  C  CD    . PRO   A  1  457  ? -37.756 41.632  67.876  1.00 27.68 ? 455  PRO   A CD    1 
ATOM   3338  N  N     . LEU   A  1  458  ? -40.063 39.313  69.814  1.00 24.69 ? 456  LEU   A N     1 
ATOM   3339  C  CA    . LEU   A  1  458  ? -41.047 38.717  70.714  1.00 23.76 ? 456  LEU   A CA    1 
ATOM   3340  C  C     . LEU   A  1  458  ? -42.450 38.845  70.142  1.00 24.58 ? 456  LEU   A C     1 
ATOM   3341  O  O     . LEU   A  1  458  ? -43.190 37.862  70.050  1.00 24.14 ? 456  LEU   A O     1 
ATOM   3342  C  CB    . LEU   A  1  458  ? -40.981 39.390  72.083  1.00 23.85 ? 456  LEU   A CB    1 
ATOM   3343  C  CG    . LEU   A  1  458  ? -42.054 38.979  73.096  1.00 23.98 ? 456  LEU   A CG    1 
ATOM   3344  C  CD1   . LEU   A  1  458  ? -42.044 37.460  73.298  1.00 25.01 ? 456  LEU   A CD1   1 
ATOM   3345  C  CD2   . LEU   A  1  458  ? -41.811 39.705  74.405  1.00 25.76 ? 456  LEU   A CD2   1 
ATOM   3346  N  N     . TYR   A  1  459  ? -42.829 40.051  69.736  1.00 22.05 ? 457  TYR   A N     1 
ATOM   3347  C  CA    . TYR   A  1  459  ? -44.216 40.262  69.358  1.00 22.90 ? 457  TYR   A CA    1 
ATOM   3348  C  C     . TYR   A  1  459  ? -44.567 39.708  67.988  1.00 23.03 ? 457  TYR   A C     1 
ATOM   3349  O  O     . TYR   A  1  459  ? -45.755 39.531  67.694  1.00 24.90 ? 457  TYR   A O     1 
ATOM   3350  C  CB    . TYR   A  1  459  ? -44.611 41.719  69.563  1.00 21.48 ? 457  TYR   A CB    1 
ATOM   3351  C  CG    . TYR   A  1  459  ? -44.824 41.970  71.025  1.00 20.43 ? 457  TYR   A CG    1 
ATOM   3352  C  CD1   . TYR   A  1  459  ? -46.024 41.616  71.626  1.00 20.21 ? 457  TYR   A CD1   1 
ATOM   3353  C  CD2   . TYR   A  1  459  ? -43.823 42.504  71.816  1.00 19.88 ? 457  TYR   A CD2   1 
ATOM   3354  C  CE1   . TYR   A  1  459  ? -46.225 41.808  72.956  1.00 21.62 ? 457  TYR   A CE1   1 
ATOM   3355  C  CE2   . TYR   A  1  459  ? -44.026 42.714  73.167  1.00 18.37 ? 457  TYR   A CE2   1 
ATOM   3356  C  CZ    . TYR   A  1  459  ? -45.234 42.364  73.725  1.00 21.00 ? 457  TYR   A CZ    1 
ATOM   3357  O  OH    . TYR   A  1  459  ? -45.444 42.560  75.065  1.00 19.97 ? 457  TYR   A OH    1 
ATOM   3358  N  N     . GLU   A  1  460  ? -43.572 39.398  67.157  1.00 24.52 ? 458  GLU   A N     1 
ATOM   3359  C  CA    . GLU   A  1  460  ? -43.872 38.605  65.973  1.00 26.68 ? 458  GLU   A CA    1 
ATOM   3360  C  C     . GLU   A  1  460  ? -44.284 37.180  66.314  1.00 30.35 ? 458  GLU   A C     1 
ATOM   3361  O  O     . GLU   A  1  460  ? -44.786 36.472  65.436  1.00 30.45 ? 458  GLU   A O     1 
ATOM   3362  C  CB    . GLU   A  1  460  ? -42.711 38.645  64.983  1.00 33.68 ? 458  GLU   A CB    1 
ATOM   3363  C  CG    . GLU   A  1  460  ? -42.718 39.912  64.141  1.00 36.68 ? 458  GLU   A CG    1 
ATOM   3364  C  CD    . GLU   A  1  460  ? -41.578 39.973  63.149  1.00 49.14 ? 458  GLU   A CD    1 
ATOM   3365  O  OE1   . GLU   A  1  460  ? -40.563 39.276  63.362  1.00 49.75 ? 458  GLU   A OE1   1 
ATOM   3366  O  OE2   . GLU   A  1  460  ? -41.701 40.719  62.155  1.00 53.61 ? 458  GLU   A OE2   1 
ATOM   3367  N  N     . GLU   A  1  461  ? -44.100 36.753  67.560  1.00 25.54 ? 459  GLU   A N     1 
ATOM   3368  C  CA    . GLU   A  1  461  ? -44.643 35.496  68.057  1.00 30.75 ? 459  GLU   A CA    1 
ATOM   3369  C  C     . GLU   A  1  461  ? -45.984 35.683  68.750  1.00 28.12 ? 459  GLU   A C     1 
ATOM   3370  O  O     . GLU   A  1  461  ? -46.523 34.725  69.314  1.00 28.31 ? 459  GLU   A O     1 
ATOM   3371  C  CB    . GLU   A  1  461  ? -43.653 34.841  69.021  1.00 26.58 ? 459  GLU   A CB    1 
ATOM   3372  C  CG    . GLU   A  1  461  ? -42.269 34.699  68.447  1.00 29.20 ? 459  GLU   A CG    1 
ATOM   3373  C  CD    . GLU   A  1  461  ? -42.241 33.799  67.224  1.00 32.47 ? 459  GLU   A CD    1 
ATOM   3374  O  OE1   . GLU   A  1  461  ? -43.123 32.921  67.104  1.00 36.65 ? 459  GLU   A OE1   1 
ATOM   3375  O  OE2   . GLU   A  1  461  ? -41.327 33.967  66.386  1.00 34.81 ? 459  GLU   A OE2   1 
ATOM   3376  N  N     . VAL   A  1  462  ? -46.526 36.900  68.720  1.00 26.38 ? 460  VAL   A N     1 
ATOM   3377  C  CA    . VAL   A  1  462  ? -47.745 37.263  69.430  1.00 23.48 ? 460  VAL   A CA    1 
ATOM   3378  C  C     . VAL   A  1  462  ? -48.822 37.751  68.468  1.00 25.62 ? 460  VAL   A C     1 
ATOM   3379  O  O     . VAL   A  1  462  ? -49.951 37.242  68.461  1.00 26.41 ? 460  VAL   A O     1 
ATOM   3380  C  CB    . VAL   A  1  462  ? -47.461 38.324  70.517  1.00 24.74 ? 460  VAL   A CB    1 
ATOM   3381  C  CG1   . VAL   A  1  462  ? -48.747 38.766  71.175  1.00 22.60 ? 460  VAL   A CG1   1 
ATOM   3382  C  CG2   . VAL   A  1  462  ? -46.485 37.782  71.556  1.00 25.45 ? 460  VAL   A CG2   1 
ATOM   3383  N  N     . VAL   A  1  463  ? -48.482 38.733  67.632  1.00 26.42 ? 461  VAL   A N     1 
ATOM   3384  C  CA    . VAL   A  1  463  ? -49.441 39.339  66.720  1.00 25.47 ? 461  VAL   A CA    1 
ATOM   3385  C  C     . VAL   A  1  463  ? -49.795 38.361  65.609  1.00 30.32 ? 461  VAL   A C     1 
ATOM   3386  O  O     . VAL   A  1  463  ? -48.929 37.646  65.088  1.00 32.04 ? 461  VAL   A O     1 
ATOM   3387  C  CB    . VAL   A  1  463  ? -48.833 40.627  66.142  1.00 24.31 ? 461  VAL   A CB    1 
ATOM   3388  C  CG1   . VAL   A  1  463  ? -49.763 41.241  65.114  1.00 26.36 ? 461  VAL   A CG1   1 
ATOM   3389  C  CG2   . VAL   A  1  463  ? -48.533 41.616  67.258  1.00 25.53 ? 461  VAL   A CG2   1 
ATOM   3390  N  N     . GLY   A  1  464  ? -51.061 38.331  65.236  1.00 30.36 ? 462  GLY   A N     1 
ATOM   3391  C  CA    . GLY   A  1  464  ? -51.463 37.544  64.091  1.00 34.08 ? 462  GLY   A CA    1 
ATOM   3392  C  C     . GLY   A  1  464  ? -52.224 36.294  64.495  1.00 34.43 ? 462  GLY   A C     1 
ATOM   3393  O  O     . GLY   A  1  464  ? -51.981 35.695  65.551  1.00 30.41 ? 462  GLY   A O     1 
ATOM   3394  N  N     . ARG   A  1  465  ? -53.154 35.882  63.628  1.00 34.11 ? 463  ARG   A N     1 
ATOM   3395  C  CA    . ARG   A  1  465  ? -53.980 34.714  63.915  1.00 37.45 ? 463  ARG   A CA    1 
ATOM   3396  C  C     . ARG   A  1  465  ? -53.148 33.442  64.027  1.00 38.09 ? 463  ARG   A C     1 
ATOM   3397  O  O     . ARG   A  1  465  ? -53.542 32.503  64.726  1.00 43.10 ? 463  ARG   A O     1 
ATOM   3398  C  CB    . ARG   A  1  465  ? -55.068 34.562  62.848  1.00 39.38 ? 463  ARG   A CB    1 
ATOM   3399  N  N     . GLY   A  1  466  ? -52.001 33.390  63.353  1.00 33.02 ? 464  GLY   A N     1 
ATOM   3400  C  CA    . GLY   A  1  466  ? -51.115 32.247  63.473  1.00 35.46 ? 464  GLY   A CA    1 
ATOM   3401  C  C     . GLY   A  1  466  ? -50.293 32.209  64.742  1.00 38.89 ? 464  GLY   A C     1 
ATOM   3402  O  O     . GLY   A  1  466  ? -49.596 31.219  64.987  1.00 39.23 ? 464  GLY   A O     1 
ATOM   3403  N  N     . LYS   A  1  467  ? -50.349 33.267  65.549  1.00 33.43 ? 465  LYS   A N     1 
ATOM   3404  C  CA    . LYS   A  1  467  ? -49.648 33.303  66.825  1.00 27.48 ? 465  LYS   A CA    1 
ATOM   3405  C  C     . LYS   A  1  467  ? -50.665 33.373  67.959  1.00 31.36 ? 465  LYS   A C     1 
ATOM   3406  O  O     . LYS   A  1  467  ? -51.545 32.513  68.053  1.00 35.43 ? 465  LYS   A O     1 
ATOM   3407  C  CB    . LYS   A  1  467  ? -48.670 34.475  66.864  1.00 30.64 ? 465  LYS   A CB    1 
ATOM   3408  C  CG    . LYS   A  1  467  ? -47.592 34.412  65.790  1.00 30.50 ? 465  LYS   A CG    1 
ATOM   3409  C  CD    . LYS   A  1  467  ? -46.729 33.166  65.939  1.00 34.74 ? 465  LYS   A CD    1 
ATOM   3410  C  CE    . LYS   A  1  467  ? -45.609 33.152  64.911  1.00 36.37 ? 465  LYS   A CE    1 
ATOM   3411  N  NZ    . LYS   A  1  467  ? -44.687 32.002  65.113  1.00 33.13 ? 465  LYS   A NZ    1 
ATOM   3412  N  N     . LEU   A  1  468  ? -50.561 34.382  68.821  1.00 29.33 ? 466  LEU   A N     1 
ATOM   3413  C  CA    . LEU   A  1  468  ? -51.518 34.552  69.907  1.00 28.52 ? 466  LEU   A CA    1 
ATOM   3414  C  C     . LEU   A  1  468  ? -52.703 35.425  69.521  1.00 27.41 ? 466  LEU   A C     1 
ATOM   3415  O  O     . LEU   A  1  468  ? -53.647 35.544  70.309  1.00 29.26 ? 466  LEU   A O     1 
ATOM   3416  C  CB    . LEU   A  1  468  ? -50.827 35.118  71.154  1.00 30.87 ? 466  LEU   A CB    1 
ATOM   3417  C  CG    . LEU   A  1  468  ? -49.637 34.304  71.675  1.00 29.19 ? 466  LEU   A CG    1 
ATOM   3418  C  CD1   . LEU   A  1  468  ? -49.162 34.825  73.018  1.00 30.77 ? 466  LEU   A CD1   1 
ATOM   3419  C  CD2   . LEU   A  1  468  ? -49.988 32.820  71.763  1.00 33.16 ? 466  LEU   A CD2   1 
ATOM   3420  N  N     . ASP   A  1  469  ? -52.672 36.029  68.331  1.00 28.35 ? 467  ASP   A N     1 
ATOM   3421  C  CA    . ASP   A  1  469  ? -53.752 36.883  67.844  1.00 27.16 ? 467  ASP   A CA    1 
ATOM   3422  C  C     . ASP   A  1  469  ? -54.068 38.000  68.831  1.00 24.92 ? 467  ASP   A C     1 
ATOM   3423  O  O     . ASP   A  1  469  ? -55.228 38.272  69.147  1.00 24.40 ? 467  ASP   A O     1 
ATOM   3424  C  CB    . ASP   A  1  469  ? -55.001 36.082  67.476  1.00 29.89 ? 467  ASP   A CB    1 
ATOM   3425  C  CG    . ASP   A  1  469  ? -55.908 36.824  66.514  1.00 34.64 ? 467  ASP   A CG    1 
ATOM   3426  O  OD1   . ASP   A  1  469  ? -55.423 37.731  65.807  1.00 32.47 ? 467  ASP   A OD1   1 
ATOM   3427  O  OD2   . ASP   A  1  469  ? -57.112 36.504  66.468  1.00 37.68 ? 467  ASP   A OD2   1 
ATOM   3428  N  N     . ARG   A  1  470  ? -53.017 38.634  69.341  1.00 24.93 ? 468  ARG   A N     1 
ATOM   3429  C  CA    . ARG   A  1  470  ? -53.159 39.815  70.159  1.00 22.27 ? 468  ARG   A CA    1 
ATOM   3430  C  C     . ARG   A  1  470  ? -52.349 40.947  69.548  1.00 22.84 ? 468  ARG   A C     1 
ATOM   3431  O  O     . ARG   A  1  470  ? -51.240 40.722  69.046  1.00 22.09 ? 468  ARG   A O     1 
ATOM   3432  C  CB    . ARG   A  1  470  ? -52.682 39.575  71.599  1.00 22.83 ? 468  ARG   A CB    1 
ATOM   3433  C  CG    . ARG   A  1  470  ? -53.450 38.495  72.351  1.00 22.34 ? 468  ARG   A CG    1 
ATOM   3434  C  CD    . ARG   A  1  470  ? -54.916 38.876  72.555  1.00 22.20 ? 468  ARG   A CD    1 
ATOM   3435  N  NE    . ARG   A  1  470  ? -55.660 37.824  73.241  1.00 24.69 ? 468  ARG   A NE    1 
ATOM   3436  C  CZ    . ARG   A  1  470  ? -56.382 36.896  72.630  1.00 24.52 ? 468  ARG   A CZ    1 
ATOM   3437  N  NH1   . ARG   A  1  470  ? -56.514 36.878  71.313  1.00 26.10 ? 468  ARG   A NH1   1 
ATOM   3438  N  NH2   . ARG   A  1  470  ? -57.009 35.978  73.361  1.00 28.40 ? 468  ARG   A NH2   1 
ATOM   3439  N  N     . PRO   A  1  471  ? -52.877 42.162  69.568  1.00 19.93 ? 469  PRO   A N     1 
ATOM   3440  C  CA    . PRO   A  1  471  ? -52.209 43.281  68.907  1.00 19.35 ? 469  PRO   A CA    1 
ATOM   3441  C  C     . PRO   A  1  471  ? -51.097 43.843  69.771  1.00 21.04 ? 469  PRO   A C     1 
ATOM   3442  O  O     . PRO   A  1  471  ? -51.070 43.700  70.996  1.00 19.45 ? 469  PRO   A O     1 
ATOM   3443  C  CB    . PRO   A  1  471  ? -53.330 44.313  68.758  1.00 19.80 ? 469  PRO   A CB    1 
ATOM   3444  C  CG    . PRO   A  1  471  ? -54.226 44.026  69.923  1.00 21.80 ? 469  PRO   A CG    1 
ATOM   3445  C  CD    . PRO   A  1  471  ? -54.198 42.532  70.095  1.00 20.51 ? 469  PRO   A CD    1 
ATOM   3446  N  N     . CYS   A  1  472  ? -50.158 44.490  69.098  1.00 18.90 ? 470  CYS   A N     1 
ATOM   3447  C  CA    . CYS   A  1  472  ? -49.056 45.120  69.795  1.00 18.94 ? 470  CYS   A CA    1 
ATOM   3448  C  C     . CYS   A  1  472  ? -48.817 46.467  69.152  1.00 17.01 ? 470  CYS   A C     1 
ATOM   3449  O  O     . CYS   A  1  472  ? -48.733 46.562  67.921  1.00 19.38 ? 470  CYS   A O     1 
ATOM   3450  C  CB    . CYS   A  1  472  ? -47.784 44.276  69.684  1.00 19.93 ? 470  CYS   A CB    1 
ATOM   3451  S  SG    . CYS   A  1  472  ? -46.376 44.983  70.548  1.00 20.23 ? 470  CYS   A SG    1 
ATOM   3452  N  N     . ARG   A  1  473  ? -48.697 47.496  69.977  1.00 16.84 ? 471  ARG   A N     1 
ATOM   3453  C  CA    . ARG   A  1  473  ? -48.372 48.832  69.511  1.00 16.42 ? 471  ARG   A CA    1 
ATOM   3454  C  C     . ARG   A  1  473  ? -46.888 49.075  69.721  1.00 17.06 ? 471  ARG   A C     1 
ATOM   3455  O  O     . ARG   A  1  473  ? -46.372 48.915  70.832  1.00 17.35 ? 471  ARG   A O     1 
ATOM   3456  C  CB    . ARG   A  1  473  ? -49.167 49.891  70.265  1.00 17.03 ? 471  ARG   A CB    1 
ATOM   3457  C  CG    . ARG   A  1  473  ? -48.984 51.296  69.694  1.00 16.23 ? 471  ARG   A CG    1 
ATOM   3458  C  CD    . ARG   A  1  473  ? -49.918 52.285  70.364  1.00 17.24 ? 471  ARG   A CD    1 
ATOM   3459  N  NE    . ARG   A  1  473  ? -51.296 51.806  70.331  1.00 16.41 ? 471  ARG   A NE    1 
ATOM   3460  C  CZ    . ARG   A  1  473  ? -52.126 51.952  69.308  1.00 17.73 ? 471  ARG   A CZ    1 
ATOM   3461  N  NH1   . ARG   A  1  473  ? -51.805 52.681  68.252  1.00 18.73 ? 471  ARG   A NH1   1 
ATOM   3462  N  NH2   . ARG   A  1  473  ? -53.314 51.357  69.352  1.00 17.96 ? 471  ARG   A NH2   1 
ATOM   3463  N  N     . ILE   A  1  474  ? -46.218 49.492  68.655  1.00 16.63 ? 472  ILE   A N     1 
ATOM   3464  C  CA    . ILE   A  1  474  ? -44.780 49.711  68.671  1.00 17.13 ? 472  ILE   A CA    1 
ATOM   3465  C  C     . ILE   A  1  474  ? -44.521 51.162  69.037  1.00 16.38 ? 472  ILE   A C     1 
ATOM   3466  O  O     . ILE   A  1  474  ? -44.969 52.077  68.334  1.00 17.30 ? 472  ILE   A O     1 
ATOM   3467  C  CB    . ILE   A  1  474  ? -44.171 49.371  67.307  1.00 16.71 ? 472  ILE   A CB    1 
ATOM   3468  C  CG1   . ILE   A  1  474  ? -44.383 47.889  67.011  1.00 20.54 ? 472  ILE   A CG1   1 
ATOM   3469  C  CG2   . ILE   A  1  474  ? -42.692 49.683  67.298  1.00 18.08 ? 472  ILE   A CG2   1 
ATOM   3470  C  CD1   . ILE   A  1  474  ? -44.077 47.522  65.573  1.00 21.45 ? 472  ILE   A CD1   1 
ATOM   3471  N  N     . TYR   A  1  475  ? -43.804 51.376  70.140  1.00 16.74 ? 473  TYR   A N     1 
ATOM   3472  C  CA    . TYR   A  1  475  ? -43.369 52.709  70.531  1.00 16.92 ? 473  TYR   A CA    1 
ATOM   3473  C  C     . TYR   A  1  475  ? -42.167 53.061  69.670  1.00 16.43 ? 473  TYR   A C     1 
ATOM   3474  O  O     . TYR   A  1  475  ? -41.130 52.383  69.725  1.00 16.74 ? 473  TYR   A O     1 
ATOM   3475  C  CB    . TYR   A  1  475  ? -42.988 52.716  72.010  1.00 17.15 ? 473  TYR   A CB    1 
ATOM   3476  C  CG    . TYR   A  1  475  ? -42.702 54.080  72.590  1.00 17.81 ? 473  TYR   A CG    1 
ATOM   3477  C  CD1   . TYR   A  1  475  ? -41.438 54.643  72.489  1.00 21.62 ? 473  TYR   A CD1   1 
ATOM   3478  C  CD2   . TYR   A  1  475  ? -43.693 54.809  73.237  1.00 18.68 ? 473  TYR   A CD2   1 
ATOM   3479  C  CE1   . TYR   A  1  475  ? -41.168 55.888  73.016  1.00 22.72 ? 473  TYR   A CE1   1 
ATOM   3480  C  CE2   . TYR   A  1  475  ? -43.432 56.056  73.771  1.00 17.94 ? 473  TYR   A CE2   1 
ATOM   3481  C  CZ    . TYR   A  1  475  ? -42.167 56.594  73.654  1.00 22.24 ? 473  TYR   A CZ    1 
ATOM   3482  O  OH    . TYR   A  1  475  ? -41.884 57.838  74.172  1.00 23.07 ? 473  TYR   A OH    1 
ATOM   3483  N  N     . ALA   A  1  476  ? -42.323 54.088  68.846  1.00 16.13 ? 474  ALA   A N     1 
ATOM   3484  C  CA    . ALA   A  1  476  ? -41.438 54.315  67.707  1.00 15.64 ? 474  ALA   A CA    1 
ATOM   3485  C  C     . ALA   A  1  476  ? -40.744 55.651  67.873  1.00 16.76 ? 474  ALA   A C     1 
ATOM   3486  O  O     . ALA   A  1  476  ? -41.331 56.705  67.576  1.00 16.47 ? 474  ALA   A O     1 
ATOM   3487  C  CB    . ALA   A  1  476  ? -42.256 54.294  66.416  1.00 19.27 ? 474  ALA   A CB    1 
ATOM   3488  N  N     . PRO   A  1  477  ? -39.487 55.665  68.311  1.00 17.92 ? 475  PRO   A N     1 
ATOM   3489  C  CA    . PRO   A  1  477  ? -38.766 56.934  68.400  1.00 18.48 ? 475  PRO   A CA    1 
ATOM   3490  C  C     . PRO   A  1  477  ? -38.520 57.475  67.007  1.00 16.81 ? 475  PRO   A C     1 
ATOM   3491  O  O     . PRO   A  1  477  ? -38.299 56.721  66.060  1.00 16.43 ? 475  PRO   A O     1 
ATOM   3492  C  CB    . PRO   A  1  477  ? -37.445 56.544  69.074  1.00 18.01 ? 475  PRO   A CB    1 
ATOM   3493  C  CG    . PRO   A  1  477  ? -37.701 55.190  69.687  1.00 21.99 ? 475  PRO   A CG    1 
ATOM   3494  C  CD    . PRO   A  1  477  ? -38.677 54.526  68.761  1.00 18.34 ? 475  PRO   A CD    1 
ATOM   3495  N  N     . VAL   A  1  478  ? -38.578 58.792  66.886  1.00 15.25 ? 476  VAL   A N     1 
ATOM   3496  C  CA    . VAL   A  1  478  ? -38.409 59.475  65.613  1.00 17.58 ? 476  VAL   A CA    1 
ATOM   3497  C  C     . VAL   A  1  478  ? -37.469 60.634  65.872  1.00 20.39 ? 476  VAL   A C     1 
ATOM   3498  O  O     . VAL   A  1  478  ? -37.738 61.465  66.743  1.00 22.72 ? 476  VAL   A O     1 
ATOM   3499  C  CB    . VAL   A  1  478  ? -39.753 59.997  65.086  1.00 18.79 ? 476  VAL   A CB    1 
ATOM   3500  C  CG1   . VAL   A  1  478  ? -39.554 60.740  63.779  1.00 19.44 ? 476  VAL   A CG1   1 
ATOM   3501  C  CG2   . VAL   A  1  478  ? -40.756 58.849  64.916  1.00 19.18 ? 476  VAL   A CG2   1 
ATOM   3502  N  N     . GLY   A  1  479  ? -36.364 60.686  65.150  1.00 19.97 ? 477  GLY   A N     1 
ATOM   3503  C  CA    . GLY   A  1  479  ? -35.498 61.830  65.329  1.00 22.49 ? 477  GLY   A CA    1 
ATOM   3504  C  C     . GLY   A  1  479  ? -34.148 61.611  64.699  1.00 20.58 ? 477  GLY   A C     1 
ATOM   3505  O  O     . GLY   A  1  479  ? -33.814 60.526  64.227  1.00 20.72 ? 477  GLY   A O     1 
ATOM   3506  N  N     . THR   A  1  480  ? -33.376 62.689  64.705  1.00 24.10 ? 478  THR   A N     1 
ATOM   3507  C  CA    . THR   A  1  480  ? -32.042 62.708  64.133  1.00 24.28 ? 478  THR   A CA    1 
ATOM   3508  C  C     . THR   A  1  480  ? -31.063 62.003  65.062  1.00 27.87 ? 478  THR   A C     1 
ATOM   3509  O  O     . THR   A  1  480  ? -31.386 61.639  66.195  1.00 27.55 ? 478  THR   A O     1 
ATOM   3510  C  CB    . THR   A  1  480  ? -31.590 64.149  63.953  1.00 27.18 ? 478  THR   A CB    1 
ATOM   3511  O  OG1   . THR   A  1  480  ? -31.611 64.800  65.231  1.00 31.74 ? 478  THR   A OG1   1 
ATOM   3512  C  CG2   . THR   A  1  480  ? -32.519 64.871  63.007  1.00 29.76 ? 478  THR   A CG2   1 
ATOM   3513  N  N     . HIS   A  1  481  ? -29.833 61.837  64.568  1.00 30.02 ? 479  HIS   A N     1 
ATOM   3514  C  CA    . HIS   A  1  481  ? -28.781 61.221  65.371  1.00 32.89 ? 479  HIS   A CA    1 
ATOM   3515  C  C     . HIS   A  1  481  ? -28.561 61.991  66.667  1.00 35.16 ? 479  HIS   A C     1 
ATOM   3516  O  O     . HIS   A  1  481  ? -28.455 61.395  67.746  1.00 33.48 ? 479  HIS   A O     1 
ATOM   3517  C  CB    . HIS   A  1  481  ? -27.481 61.165  64.571  1.00 29.11 ? 479  HIS   A CB    1 
ATOM   3518  C  CG    . HIS   A  1  481  ? -27.551 60.303  63.349  1.00 33.54 ? 479  HIS   A CG    1 
ATOM   3519  N  ND1   . HIS   A  1  481  ? -26.475 60.131  62.504  1.00 31.75 ? 479  HIS   A ND1   1 
ATOM   3520  C  CD2   . HIS   A  1  481  ? -28.561 59.565  62.830  1.00 30.28 ? 479  HIS   A CD2   1 
ATOM   3521  C  CE1   . HIS   A  1  481  ? -26.820 59.325  61.515  1.00 32.61 ? 479  HIS   A CE1   1 
ATOM   3522  N  NE2   . HIS   A  1  481  ? -28.079 58.964  61.691  1.00 33.70 ? 479  HIS   A NE2   1 
ATOM   3523  N  N     . GLU   A  1  482  ? -28.483 63.323  66.575  1.00 35.76 ? 480  GLU   A N     1 
ATOM   3524  C  CA    . GLU   A  1  482  ? -28.274 64.146  67.763  1.00 39.99 ? 480  GLU   A CA    1 
ATOM   3525  C  C     . GLU   A  1  482  ? -29.368 63.904  68.791  1.00 38.57 ? 480  GLU   A C     1 
ATOM   3526  O  O     . GLU   A  1  482  ? -29.093 63.733  69.985  1.00 39.32 ? 480  GLU   A O     1 
ATOM   3527  C  CB    . GLU   A  1  482  ? -28.232 65.623  67.367  1.00 39.72 ? 480  GLU   A CB    1 
ATOM   3528  N  N     . THR   A  1  483  ? -30.622 63.874  68.337  1.00 34.31 ? 481  THR   A N     1 
ATOM   3529  C  CA    . THR   A  1  483  ? -31.742 63.729  69.258  1.00 34.67 ? 481  THR   A CA    1 
ATOM   3530  C  C     . THR   A  1  483  ? -31.746 62.357  69.918  1.00 33.36 ? 481  THR   A C     1 
ATOM   3531  O  O     . THR   A  1  483  ? -31.987 62.246  71.125  1.00 34.73 ? 481  THR   A O     1 
ATOM   3532  C  CB    . THR   A  1  483  ? -33.054 63.967  68.515  1.00 33.95 ? 481  THR   A CB    1 
ATOM   3533  O  OG1   . THR   A  1  483  ? -32.978 65.210  67.811  1.00 40.80 ? 481  THR   A OG1   1 
ATOM   3534  C  CG2   . THR   A  1  483  ? -34.214 64.029  69.493  1.00 38.24 ? 481  THR   A CG2   1 
ATOM   3535  N  N     . LEU   A  1  484  ? -31.484 61.298  69.147  1.00 29.60 ? 482  LEU   A N     1 
ATOM   3536  C  CA    . LEU   A  1  484  ? -31.608 59.954  69.702  1.00 30.11 ? 482  LEU   A CA    1 
ATOM   3537  C  C     . LEU   A  1  484  ? -30.488 59.646  70.689  1.00 31.88 ? 482  LEU   A C     1 
ATOM   3538  O  O     . LEU   A  1  484  ? -30.704 58.933  71.675  1.00 31.51 ? 482  LEU   A O     1 
ATOM   3539  C  CB    . LEU   A  1  484  ? -31.685 58.914  68.581  1.00 29.76 ? 482  LEU   A CB    1 
ATOM   3540  C  CG    . LEU   A  1  484  ? -30.447 58.660  67.716  1.00 32.08 ? 482  LEU   A CG    1 
ATOM   3541  C  CD1   . LEU   A  1  484  ? -29.608 57.527  68.289  1.00 31.00 ? 482  LEU   A CD1   1 
ATOM   3542  C  CD2   . LEU   A  1  484  ? -30.842 58.352  66.278  1.00 33.99 ? 482  LEU   A CD2   1 
ATOM   3543  N  N     . LEU   A  1  485  ? -29.287 60.176  70.450  1.00 33.62 ? 483  LEU   A N     1 
ATOM   3544  C  CA    . LEU   A  1  485  ? -28.162 59.866  71.325  1.00 31.56 ? 483  LEU   A CA    1 
ATOM   3545  C  C     . LEU   A  1  485  ? -28.307 60.492  72.706  1.00 33.03 ? 483  LEU   A C     1 
ATOM   3546  O  O     . LEU   A  1  485  ? -27.682 60.008  73.657  1.00 31.30 ? 483  LEU   A O     1 
ATOM   3547  C  CB    . LEU   A  1  485  ? -26.847 60.312  70.677  1.00 31.58 ? 483  LEU   A CB    1 
ATOM   3548  C  CG    . LEU   A  1  485  ? -26.405 59.520  69.445  1.00 30.94 ? 483  LEU   A CG    1 
ATOM   3549  C  CD1   . LEU   A  1  485  ? -25.285 60.249  68.717  1.00 31.86 ? 483  LEU   A CD1   1 
ATOM   3550  C  CD2   . LEU   A  1  485  ? -25.977 58.111  69.830  1.00 28.30 ? 483  LEU   A CD2   1 
ATOM   3551  N  N     . ALA   A  1  486  ? -29.132 61.536  72.835  1.00 33.80 ? 484  ALA   A N     1 
ATOM   3552  C  CA    . ALA   A  1  486  ? -29.187 62.312  74.072  1.00 34.24 ? 484  ALA   A CA    1 
ATOM   3553  C  C     . ALA   A  1  486  ? -29.527 61.439  75.275  1.00 35.58 ? 484  ALA   A C     1 
ATOM   3554  O  O     . ALA   A  1  486  ? -28.883 61.538  76.327  1.00 34.31 ? 484  ALA   A O     1 
ATOM   3555  C  CB    . ALA   A  1  486  ? -30.190 63.456  73.924  1.00 36.89 ? 484  ALA   A CB    1 
ATOM   3556  N  N     . TYR   A  1  487  ? -30.539 60.576  75.144  1.00 33.57 ? 485  TYR   A N     1 
ATOM   3557  C  CA    . TYR   A  1  487  ? -30.963 59.726  76.254  1.00 29.57 ? 485  TYR   A CA    1 
ATOM   3558  C  C     . TYR   A  1  487  ? -30.984 58.257  75.853  1.00 31.23 ? 485  TYR   A C     1 
ATOM   3559  O  O     . TYR   A  1  487  ? -31.763 57.464  76.397  1.00 28.38 ? 485  TYR   A O     1 
ATOM   3560  C  CB    . TYR   A  1  487  ? -32.311 60.171  76.822  1.00 34.20 ? 485  TYR   A CB    1 
ATOM   3561  C  CG    . TYR   A  1  487  ? -32.300 61.613  77.281  1.00 37.02 ? 485  TYR   A CG    1 
ATOM   3562  C  CD1   . TYR   A  1  487  ? -31.764 61.965  78.515  1.00 40.31 ? 485  TYR   A CD1   1 
ATOM   3563  C  CD2   . TYR   A  1  487  ? -32.801 62.624  76.470  1.00 36.70 ? 485  TYR   A CD2   1 
ATOM   3564  C  CE1   . TYR   A  1  487  ? -31.738 63.286  78.934  1.00 45.51 ? 485  TYR   A CE1   1 
ATOM   3565  C  CE2   . TYR   A  1  487  ? -32.781 63.946  76.879  1.00 40.78 ? 485  TYR   A CE2   1 
ATOM   3566  C  CZ    . TYR   A  1  487  ? -32.249 64.272  78.111  1.00 47.61 ? 485  TYR   A CZ    1 
ATOM   3567  O  OH    . TYR   A  1  487  ? -32.228 65.590  78.518  1.00 50.24 ? 485  TYR   A OH    1 
ATOM   3568  N  N     . LEU   A  1  488  ? -30.122 57.877  74.905  1.00 29.25 ? 486  LEU   A N     1 
ATOM   3569  C  CA    . LEU   A  1  488  ? -30.091 56.486  74.466  1.00 24.99 ? 486  LEU   A CA    1 
ATOM   3570  C  C     . LEU   A  1  488  ? -29.583 55.562  75.566  1.00 25.83 ? 486  LEU   A C     1 
ATOM   3571  O  O     . LEU   A  1  488  ? -29.959 54.385  75.608  1.00 25.43 ? 486  LEU   A O     1 
ATOM   3572  C  CB    . LEU   A  1  488  ? -29.234 56.348  73.205  1.00 27.93 ? 486  LEU   A CB    1 
ATOM   3573  C  CG    . LEU   A  1  488  ? -29.281 54.964  72.554  1.00 35.60 ? 486  LEU   A CG    1 
ATOM   3574  C  CD1   . LEU   A  1  488  ? -30.727 54.549  72.328  1.00 31.61 ? 486  LEU   A CD1   1 
ATOM   3575  C  CD2   . LEU   A  1  488  ? -28.509 54.941  71.248  1.00 26.93 ? 486  LEU   A CD2   1 
ATOM   3576  N  N     . VAL   A  1  489  ? -28.731 56.074  76.458  1.00 28.85 ? 487  VAL   A N     1 
ATOM   3577  C  CA    . VAL   A  1  489  ? -28.215 55.247  77.546  1.00 25.60 ? 487  VAL   A CA    1 
ATOM   3578  C  C     . VAL   A  1  489  ? -29.356 54.748  78.425  1.00 26.30 ? 487  VAL   A C     1 
ATOM   3579  O  O     . VAL   A  1  489  ? -29.420 53.564  78.774  1.00 26.49 ? 487  VAL   A O     1 
ATOM   3580  C  CB    . VAL   A  1  489  ? -27.156 56.013  78.355  1.00 27.04 ? 487  VAL   A CB    1 
ATOM   3581  C  CG1   . VAL   A  1  489  ? -26.890 55.312  79.684  1.00 28.49 ? 487  VAL   A CG1   1 
ATOM   3582  C  CG2   . VAL   A  1  489  ? -25.865 56.150  77.540  1.00 27.81 ? 487  VAL   A CG2   1 
ATOM   3583  N  N     . ARG   A  1  490  ? -30.271 55.646  78.804  1.00 26.93 ? 488  ARG   A N     1 
ATOM   3584  C  CA    . ARG   A  1  490  ? -31.412 55.231  79.617  1.00 25.89 ? 488  ARG   A CA    1 
ATOM   3585  C  C     . ARG   A  1  490  ? -32.231 54.158  78.906  1.00 29.33 ? 488  ARG   A C     1 
ATOM   3586  O  O     . ARG   A  1  490  ? -32.646 53.170  79.525  1.00 29.50 ? 488  ARG   A O     1 
ATOM   3587  C  CB    . ARG   A  1  490  ? -32.287 56.440  79.975  1.00 29.82 ? 488  ARG   A CB    1 
ATOM   3588  C  CG    . ARG   A  1  490  ? -33.481 56.096  80.878  1.00 29.12 ? 488  ARG   A CG    1 
ATOM   3589  C  CD    . ARG   A  1  490  ? -34.464 57.267  81.067  1.00 29.95 ? 488  ARG   A CD    1 
ATOM   3590  N  NE    . ARG   A  1  490  ? -35.176 57.617  79.838  1.00 29.30 ? 488  ARG   A NE    1 
ATOM   3591  C  CZ    . ARG   A  1  490  ? -35.352 58.856  79.394  1.00 29.96 ? 488  ARG   A CZ    1 
ATOM   3592  N  NH1   . ARG   A  1  490  ? -34.882 59.902  80.056  1.00 30.73 ? 488  ARG   A NH1   1 
ATOM   3593  N  NH2   . ARG   A  1  490  ? -36.018 59.049  78.258  1.00 28.09 ? 488  ARG   A NH2   1 
ATOM   3594  N  N     . ARG   A  1  491  ? -32.455 54.323  77.600  1.00 28.77 ? 489  ARG   A N     1 
ATOM   3595  C  CA    . ARG   A  1  491  ? -33.275 53.363  76.872  1.00 28.22 ? 489  ARG   A CA    1 
ATOM   3596  C  C     . ARG   A  1  491  ? -32.580 52.017  76.743  1.00 35.59 ? 489  ARG   A C     1 
ATOM   3597  O  O     . ARG   A  1  491  ? -33.245 50.977  76.784  1.00 34.22 ? 489  ARG   A O     1 
ATOM   3598  C  CB    . ARG   A  1  491  ? -33.645 53.921  75.496  1.00 31.85 ? 489  ARG   A CB    1 
ATOM   3599  N  N     . LEU   A  1  492  ? -31.247 52.016  76.606  1.00 31.66 ? 490  LEU   A N     1 
ATOM   3600  C  CA    . LEU   A  1  492  ? -30.513 50.757  76.506  1.00 30.84 ? 490  LEU   A CA    1 
ATOM   3601  C  C     . LEU   A  1  492  ? -30.525 49.999  77.831  1.00 32.81 ? 490  LEU   A C     1 
ATOM   3602  O  O     . LEU   A  1  492  ? -30.608 48.762  77.847  1.00 30.47 ? 490  LEU   A O     1 
ATOM   3603  C  CB    . LEU   A  1  492  ? -29.076 51.017  76.042  1.00 29.78 ? 490  LEU   A CB    1 
ATOM   3604  C  CG    . LEU   A  1  492  ? -28.846 51.572  74.632  1.00 30.63 ? 490  LEU   A CG    1 
ATOM   3605  C  CD1   . LEU   A  1  492  ? -27.398 52.026  74.446  1.00 31.41 ? 490  LEU   A CD1   1 
ATOM   3606  C  CD2   . LEU   A  1  492  ? -29.226 50.546  73.573  1.00 34.31 ? 490  LEU   A CD2   1 
ATOM   3607  N  N     . LEU   A  1  493  ? -30.432 50.720  78.954  1.00 29.85 ? 491  LEU   A N     1 
ATOM   3608  C  CA    . LEU   A  1  493  ? -30.436 50.056  80.253  1.00 27.14 ? 491  LEU   A CA    1 
ATOM   3609  C  C     . LEU   A  1  493  ? -31.771 49.386  80.536  1.00 31.86 ? 491  LEU   A C     1 
ATOM   3610  O  O     . LEU   A  1  493  ? -31.829 48.431  81.320  1.00 35.59 ? 491  LEU   A O     1 
ATOM   3611  C  CB    . LEU   A  1  493  ? -30.123 51.056  81.365  1.00 31.93 ? 491  LEU   A CB    1 
ATOM   3612  C  CG    . LEU   A  1  493  ? -28.726 51.665  81.350  1.00 37.09 ? 491  LEU   A CG    1 
ATOM   3613  C  CD1   . LEU   A  1  493  ? -28.411 52.284  82.706  1.00 34.91 ? 491  LEU   A CD1   1 
ATOM   3614  C  CD2   . LEU   A  1  493  ? -27.717 50.601  80.983  1.00 36.02 ? 491  LEU   A CD2   1 
ATOM   3615  N  N     . GLU   A  1  494  ? -32.851 49.884  79.925  1.00 34.05 ? 492  GLU   A N     1 
ATOM   3616  C  CA    . GLU   A  1  494  ? -34.173 49.312  80.164  1.00 36.01 ? 492  GLU   A CA    1 
ATOM   3617  C  C     . GLU   A  1  494  ? -34.189 47.822  79.855  1.00 34.08 ? 492  GLU   A C     1 
ATOM   3618  O  O     . GLU   A  1  494  ? -34.788 47.031  80.594  1.00 31.79 ? 492  GLU   A O     1 
ATOM   3619  C  CB    . GLU   A  1  494  ? -35.214 50.040  79.315  1.00 29.39 ? 492  GLU   A CB    1 
ATOM   3620  N  N     . ASN   A  1  495  ? -33.520 47.420  78.776  1.00 31.50 ? 493  ASN   A N     1 
ATOM   3621  C  CA    . ASN   A  1  495  ? -33.455 46.022  78.372  1.00 34.12 ? 493  ASN   A CA    1 
ATOM   3622  C  C     . ASN   A  1  495  ? -32.036 45.459  78.396  1.00 35.60 ? 493  ASN   A C     1 
ATOM   3623  O  O     . ASN   A  1  495  ? -31.817 44.348  77.898  1.00 34.62 ? 493  ASN   A O     1 
ATOM   3624  C  CB    . ASN   A  1  495  ? -34.086 45.839  76.987  1.00 33.42 ? 493  ASN   A CB    1 
ATOM   3625  N  N     . GLY   A  1  496  ? -31.072 46.177  78.978  1.00 36.43 ? 494  GLY   A N     1 
ATOM   3626  C  CA    . GLY   A  1  496  ? -29.684 45.747  78.916  1.00 38.69 ? 494  GLY   A CA    1 
ATOM   3627  C  C     . GLY   A  1  496  ? -28.991 45.503  80.244  1.00 42.79 ? 494  GLY   A C     1 
ATOM   3628  O  O     . GLY   A  1  496  ? -27.853 45.021  80.265  1.00 41.65 ? 494  GLY   A O     1 
ATOM   3629  N  N     . ALA   A  1  497  ? -29.645 45.842  81.356  1.00 36.47 ? 495  ALA   A N     1 
ATOM   3630  C  CA    . ALA   A  1  497  ? -29.085 45.556  82.671  1.00 37.71 ? 495  ALA   A CA    1 
ATOM   3631  C  C     . ALA   A  1  497  ? -29.124 44.055  82.944  1.00 33.34 ? 495  ALA   A C     1 
ATOM   3632  O  O     . ALA   A  1  497  ? -29.887 43.306  82.328  1.00 32.79 ? 495  ALA   A O     1 
ATOM   3633  C  CB    . ALA   A  1  497  ? -29.868 46.292  83.761  1.00 30.92 ? 495  ALA   A CB    1 
ATOM   3634  N  N     . ASN   A  1  498  ? -28.290 43.614  83.892  1.00 34.11 ? 496  ASN   A N     1 
ATOM   3635  C  CA    . ASN   A  1  498  ? -28.180 42.180  84.158  1.00 32.19 ? 496  ASN   A CA    1 
ATOM   3636  C  C     . ASN   A  1  498  ? -29.521 41.567  84.547  1.00 32.05 ? 496  ASN   A C     1 
ATOM   3637  O  O     . ASN   A  1  498  ? -29.766 40.385  84.276  1.00 34.54 ? 496  ASN   A O     1 
ATOM   3638  C  CB    . ASN   A  1  498  ? -27.125 41.911  85.233  1.00 37.50 ? 496  ASN   A CB    1 
ATOM   3639  N  N     . SER   A  1  499  ? -30.398 42.351  85.179  1.00 33.15 ? 497  SER   A N     1 
ATOM   3640  C  CA    . SER   A  1  499  ? -31.721 41.885  85.573  1.00 33.33 ? 497  SER   A CA    1 
ATOM   3641  C  C     . SER   A  1  499  ? -32.749 41.971  84.451  1.00 26.33 ? 497  SER   A C     1 
ATOM   3642  O  O     . SER   A  1  499  ? -33.842 41.410  84.594  1.00 30.15 ? 497  SER   A O     1 
ATOM   3643  C  CB    . SER   A  1  499  ? -32.215 42.702  86.772  1.00 36.61 ? 497  SER   A CB    1 
ATOM   3644  O  OG    . SER   A  1  499  ? -31.976 44.087  86.565  1.00 38.17 ? 497  SER   A OG    1 
ATOM   3645  N  N     . SER   A  1  500  ? -32.431 42.652  83.352  1.00 25.68 ? 498  SER   A N     1 
ATOM   3646  C  CA    . SER   A  1  500  ? -33.399 42.860  82.283  1.00 24.51 ? 498  SER   A CA    1 
ATOM   3647  C  C     . SER   A  1  500  ? -33.628 41.584  81.488  1.00 28.58 ? 498  SER   A C     1 
ATOM   3648  O  O     . SER   A  1  500  ? -32.690 40.828  81.211  1.00 26.94 ? 498  SER   A O     1 
ATOM   3649  C  CB    . SER   A  1  500  ? -32.907 43.949  81.337  1.00 29.75 ? 498  SER   A CB    1 
ATOM   3650  O  OG    . SER   A  1  500  ? -32.791 45.182  82.011  1.00 31.41 ? 498  SER   A OG    1 
ATOM   3651  N  N     . PHE   A  1  501  ? -34.890 41.362  81.103  1.00 24.55 ? 499  PHE   A N     1 
ATOM   3652  C  CA    . PHE   A  1  501  ? -35.246 40.176  80.332  1.00 24.47 ? 499  PHE   A CA    1 
ATOM   3653  C  C     . PHE   A  1  501  ? -34.442 40.079  79.042  1.00 29.67 ? 499  PHE   A C     1 
ATOM   3654  O  O     . PHE   A  1  501  ? -33.977 38.995  78.673  1.00 29.43 ? 499  PHE   A O     1 
ATOM   3655  C  CB    . PHE   A  1  501  ? -36.739 40.180  80.002  1.00 22.93 ? 499  PHE   A CB    1 
ATOM   3656  C  CG    . PHE   A  1  501  ? -37.160 39.016  79.151  1.00 22.65 ? 499  PHE   A CG    1 
ATOM   3657  C  CD1   . PHE   A  1  501  ? -37.474 37.808  79.732  1.00 25.17 ? 499  PHE   A CD1   1 
ATOM   3658  C  CD2   . PHE   A  1  501  ? -37.215 39.125  77.768  1.00 28.51 ? 499  PHE   A CD2   1 
ATOM   3659  C  CE1   . PHE   A  1  501  ? -37.854 36.726  78.959  1.00 28.54 ? 499  PHE   A CE1   1 
ATOM   3660  C  CE2   . PHE   A  1  501  ? -37.591 38.040  76.985  1.00 25.20 ? 499  PHE   A CE2   1 
ATOM   3661  C  CZ    . PHE   A  1  501  ? -37.910 36.843  77.586  1.00 27.91 ? 499  PHE   A CZ    1 
ATOM   3662  N  N     . VAL   A  1  502  ? -34.305 41.196  78.321  1.00 30.16 ? 500  VAL   A N     1 
ATOM   3663  C  CA    . VAL   A  1  502  ? -33.650 41.149  77.017  1.00 29.62 ? 500  VAL   A CA    1 
ATOM   3664  C  C     . VAL   A  1  502  ? -32.166 40.850  77.163  1.00 32.79 ? 500  VAL   A C     1 
ATOM   3665  O  O     . VAL   A  1  502  ? -31.551 40.274  76.258  1.00 40.56 ? 500  VAL   A O     1 
ATOM   3666  C  CB    . VAL   A  1  502  ? -33.904 42.429  76.204  1.00 31.47 ? 500  VAL   A CB    1 
ATOM   3667  N  N     . HIS   A  1  503  ? -31.559 41.244  78.280  1.00 30.85 ? 501  HIS   A N     1 
ATOM   3668  C  CA    . HIS   A  1  503  ? -30.193 40.809  78.545  1.00 27.44 ? 501  HIS   A CA    1 
ATOM   3669  C  C     . HIS   A  1  503  ? -30.160 39.323  78.871  1.00 33.87 ? 501  HIS   A C     1 
ATOM   3670  O  O     . HIS   A  1  503  ? -29.306 38.585  78.365  1.00 30.23 ? 501  HIS   A O     1 
ATOM   3671  C  CB    . HIS   A  1  503  ? -29.599 41.632  79.687  1.00 31.90 ? 501  HIS   A CB    1 
ATOM   3672  C  CG    . HIS   A  1  503  ? -28.236 41.181  80.117  1.00 34.08 ? 501  HIS   A CG    1 
ATOM   3673  N  ND1   . HIS   A  1  503  ? -28.027 40.382  81.222  1.00 34.28 ? 501  HIS   A ND1   1 
ATOM   3674  C  CD2   . HIS   A  1  503  ? -27.010 41.423  79.593  1.00 35.50 ? 501  HIS   A CD2   1 
ATOM   3675  C  CE1   . HIS   A  1  503  ? -26.734 40.149  81.358  1.00 34.10 ? 501  HIS   A CE1   1 
ATOM   3676  N  NE2   . HIS   A  1  503  ? -26.095 40.769  80.382  1.00 36.27 ? 501  HIS   A NE2   1 
ATOM   3677  N  N     . ARG   A  1  504  ? -31.108 38.860  79.686  1.00 26.89 ? 502  ARG   A N     1 
ATOM   3678  C  CA    . ARG   A  1  504  ? -31.091 37.473  80.132  1.00 29.00 ? 502  ARG   A CA    1 
ATOM   3679  C  C     . ARG   A  1  504  ? -31.436 36.511  78.999  1.00 31.49 ? 502  ARG   A C     1 
ATOM   3680  O  O     . ARG   A  1  504  ? -30.878 35.408  78.927  1.00 30.61 ? 502  ARG   A O     1 
ATOM   3681  C  CB    . ARG   A  1  504  ? -32.026 37.303  81.330  1.00 31.29 ? 502  ARG   A CB    1 
ATOM   3682  C  CG    . ARG   A  1  504  ? -31.530 38.037  82.572  1.00 30.52 ? 502  ARG   A CG    1 
ATOM   3683  C  CD    . ARG   A  1  504  ? -32.646 38.257  83.583  1.00 31.44 ? 502  ARG   A CD    1 
ATOM   3684  N  NE    . ARG   A  1  504  ? -33.378 37.030  83.866  1.00 34.35 ? 502  ARG   A NE    1 
ATOM   3685  C  CZ    . ARG   A  1  504  ? -32.965 36.081  84.697  1.00 37.34 ? 502  ARG   A CZ    1 
ATOM   3686  N  NH1   . ARG   A  1  504  ? -31.800 36.166  85.319  1.00 39.38 ? 502  ARG   A NH1   1 
ATOM   3687  N  NH2   . ARG   A  1  504  ? -33.739 35.019  84.906  1.00 37.84 ? 502  ARG   A NH2   1 
ATOM   3688  N  N     . ILE   A  1  505  ? -32.344 36.912  78.101  1.00 32.68 ? 503  ILE   A N     1 
ATOM   3689  C  CA    . ILE   A  1  505  ? -32.693 36.065  76.960  1.00 32.07 ? 503  ILE   A CA    1 
ATOM   3690  C  C     . ILE   A  1  505  ? -31.456 35.767  76.119  1.00 36.08 ? 503  ILE   A C     1 
ATOM   3691  O  O     . ILE   A  1  505  ? -31.302 34.662  75.584  1.00 38.46 ? 503  ILE   A O     1 
ATOM   3692  C  CB    . ILE   A  1  505  ? -33.829 36.700  76.129  1.00 36.64 ? 503  ILE   A CB    1 
ATOM   3693  C  CG1   . ILE   A  1  505  ? -34.290 35.760  75.021  1.00 39.93 ? 503  ILE   A CG1   1 
ATOM   3694  C  CG2   . ILE   A  1  505  ? -33.384 37.978  75.472  1.00 38.93 ? 503  ILE   A CG2   1 
ATOM   3695  C  CD1   . ILE   A  1  505  ? -35.304 34.760  75.466  1.00 32.00 ? 503  ILE   A CD1   1 
ATOM   3696  N  N     . ASN   A  1  506  ? -30.548 36.735  76.011  1.00 34.29 ? 504  ASN   A N     1 
ATOM   3697  C  CA    . ASN   A  1  506  ? -29.322 36.584  75.241  1.00 39.12 ? 504  ASN   A CA    1 
ATOM   3698  C  C     . ASN   A  1  506  ? -28.185 35.968  76.041  1.00 38.14 ? 504  ASN   A C     1 
ATOM   3699  O  O     . ASN   A  1  506  ? -27.097 35.772  75.490  1.00 43.14 ? 504  ASN   A O     1 
ATOM   3700  C  CB    . ASN   A  1  506  ? -28.872 37.937  74.686  1.00 42.27 ? 504  ASN   A CB    1 
ATOM   3701  C  CG    . ASN   A  1  506  ? -29.789 38.454  73.601  1.00 42.76 ? 504  ASN   A CG    1 
ATOM   3702  O  OD1   . ASN   A  1  506  ? -30.369 37.679  72.840  1.00 49.26 ? 504  ASN   A OD1   1 
ATOM   3703  N  ND2   . ASN   A  1  506  ? -29.925 39.773  73.520  1.00 51.91 ? 504  ASN   A ND2   1 
ATOM   3704  N  N     . ASP   A  1  507  ? -28.400 35.667  77.321  1.00 34.17 ? 505  ASP   A N     1 
ATOM   3705  C  CA    . ASP   A  1  507  ? -27.355 35.080  78.147  1.00 36.36 ? 505  ASP   A CA    1 
ATOM   3706  C  C     . ASP   A  1  507  ? -27.468 33.565  78.055  1.00 38.49 ? 505  ASP   A C     1 
ATOM   3707  O  O     . ASP   A  1  507  ? -28.477 33.004  78.509  1.00 34.35 ? 505  ASP   A O     1 
ATOM   3708  C  CB    . ASP   A  1  507  ? -27.501 35.534  79.592  1.00 34.99 ? 505  ASP   A CB    1 
ATOM   3709  C  CG    . ASP   A  1  507  ? -26.293 35.174  80.446  1.00 38.91 ? 505  ASP   A CG    1 
ATOM   3710  O  OD1   . ASP   A  1  507  ? -25.634 34.152  80.161  1.00 44.66 ? 505  ASP   A OD1   1 
ATOM   3711  O  OD2   . ASP   A  1  507  ? -26.001 35.916  81.406  1.00 42.93 ? 505  ASP   A OD2   1 
ATOM   3712  N  N     . PRO   A  1  508  ? -26.476 32.867  77.498  1.00 44.33 ? 506  PRO   A N     1 
ATOM   3713  C  CA    . PRO   A  1  508  ? -26.576 31.401  77.401  1.00 45.54 ? 506  PRO   A CA    1 
ATOM   3714  C  C     . PRO   A  1  508  ? -26.602 30.706  78.749  1.00 38.44 ? 506  PRO   A C     1 
ATOM   3715  O  O     . PRO   A  1  508  ? -27.121 29.587  78.844  1.00 47.19 ? 506  PRO   A O     1 
ATOM   3716  C  CB    . PRO   A  1  508  ? -25.328 31.009  76.594  1.00 49.54 ? 506  PRO   A CB    1 
ATOM   3717  C  CG    . PRO   A  1  508  ? -24.819 32.297  75.986  1.00 52.13 ? 506  PRO   A CG    1 
ATOM   3718  C  CD    . PRO   A  1  508  ? -25.216 33.380  76.935  1.00 43.31 ? 506  PRO   A CD    1 
ATOM   3719  N  N     . LYS   A  1  509  ? -26.065 31.334  79.794  1.00 38.23 ? 507  LYS   A N     1 
ATOM   3720  C  CA    . LYS   A  1  509  ? -26.058 30.749  81.128  1.00 38.51 ? 507  LYS   A CA    1 
ATOM   3721  C  C     . LYS   A  1  509  ? -27.408 30.834  81.829  1.00 41.90 ? 507  LYS   A C     1 
ATOM   3722  O  O     . LYS   A  1  509  ? -27.560 30.262  82.912  1.00 42.82 ? 507  LYS   A O     1 
ATOM   3723  C  CB    . LYS   A  1  509  ? -24.988 31.424  81.990  1.00 44.42 ? 507  LYS   A CB    1 
ATOM   3724  N  N     . VAL   A  1  510  ? -28.383 31.532  81.255  1.00 37.82 ? 508  VAL   A N     1 
ATOM   3725  C  CA    . VAL   A  1  510  ? -29.717 31.646  81.837  1.00 35.12 ? 508  VAL   A CA    1 
ATOM   3726  C  C     . VAL   A  1  510  ? -30.628 30.663  81.116  1.00 34.06 ? 508  VAL   A C     1 
ATOM   3727  O  O     . VAL   A  1  510  ? -30.780 30.729  79.891  1.00 36.75 ? 508  VAL   A O     1 
ATOM   3728  C  CB    . VAL   A  1  510  ? -30.250 33.084  81.739  1.00 34.89 ? 508  VAL   A CB    1 
ATOM   3729  C  CG1   . VAL   A  1  510  ? -31.652 33.176  82.330  1.00 33.42 ? 508  VAL   A CG1   1 
ATOM   3730  C  CG2   . VAL   A  1  510  ? -29.312 34.053  82.445  1.00 33.41 ? 508  VAL   A CG2   1 
ATOM   3731  N  N     . SER   A  1  511  ? -31.222 29.741  81.869  1.00 31.35 ? 509  SER   A N     1 
ATOM   3732  C  CA    . SER   A  1  511  ? -32.071 28.720  81.281  1.00 31.60 ? 509  SER   A CA    1 
ATOM   3733  C  C     . SER   A  1  511  ? -33.473 29.267  81.033  1.00 30.53 ? 509  SER   A C     1 
ATOM   3734  O  O     . SER   A  1  511  ? -33.879 30.292  81.591  1.00 33.53 ? 509  SER   A O     1 
ATOM   3735  C  CB    . SER   A  1  511  ? -32.172 27.510  82.208  1.00 38.93 ? 509  SER   A CB    1 
ATOM   3736  O  OG    . SER   A  1  511  ? -32.885 27.837  83.388  1.00 33.35 ? 509  SER   A OG    1 
ATOM   3737  N  N     . ILE   A  1  512  ? -34.212 28.563  80.177  1.00 31.44 ? 510  ILE   A N     1 
ATOM   3738  C  CA    . ILE   A  1  512  ? -35.609 28.915  79.943  1.00 30.23 ? 510  ILE   A CA    1 
ATOM   3739  C  C     . ILE   A  1  512  ? -36.420 28.745  81.219  1.00 36.04 ? 510  ILE   A C     1 
ATOM   3740  O  O     . ILE   A  1  512  ? -37.282 29.572  81.539  1.00 32.52 ? 510  ILE   A O     1 
ATOM   3741  C  CB    . ILE   A  1  512  ? -36.178 28.105  78.767  1.00 32.49 ? 510  ILE   A CB    1 
ATOM   3742  C  CG1   . ILE   A  1  512  ? -35.413 28.454  77.489  1.00 31.89 ? 510  ILE   A CG1   1 
ATOM   3743  C  CG2   . ILE   A  1  512  ? -37.670 28.370  78.601  1.00 33.04 ? 510  ILE   A CG2   1 
ATOM   3744  C  CD1   . ILE   A  1  512  ? -35.887 27.722  76.272  1.00 35.76 ? 510  ILE   A CD1   1 
ATOM   3745  N  N     . ASP   A  1  513  ? -36.147 27.678  81.977  1.00 34.45 ? 511  ASP   A N     1 
ATOM   3746  C  CA    . ASP   A  1  513  ? -36.799 27.504  83.271  1.00 35.62 ? 511  ASP   A CA    1 
ATOM   3747  C  C     . ASP   A  1  513  ? -36.582 28.716  84.167  1.00 34.78 ? 511  ASP   A C     1 
ATOM   3748  O  O     . ASP   A  1  513  ? -37.499 29.144  84.877  1.00 33.55 ? 511  ASP   A O     1 
ATOM   3749  C  CB    . ASP   A  1  513  ? -36.293 26.232  83.948  1.00 38.81 ? 511  ASP   A CB    1 
ATOM   3750  C  CG    . ASP   A  1  513  ? -36.749 24.976  83.237  1.00 45.20 ? 511  ASP   A CG    1 
ATOM   3751  O  OD1   . ASP   A  1  513  ? -37.906 24.945  82.769  1.00 45.88 ? 511  ASP   A OD1   1 
ATOM   3752  O  OD2   . ASP   A  1  513  ? -35.947 24.022  83.140  1.00 57.01 ? 511  ASP   A OD2   1 
ATOM   3753  N  N     . GLU   A  1  514  ? -35.380 29.291  84.141  1.00 31.84 ? 512  GLU   A N     1 
ATOM   3754  C  CA    . GLU   A  1  514  ? -35.135 30.511  84.902  1.00 31.21 ? 512  GLU   A CA    1 
ATOM   3755  C  C     . GLU   A  1  514  ? -35.954 31.675  84.354  1.00 32.25 ? 512  GLU   A C     1 
ATOM   3756  O  O     . GLU   A  1  514  ? -36.473 32.494  85.122  1.00 32.37 ? 512  GLU   A O     1 
ATOM   3757  C  CB    . GLU   A  1  514  ? -33.644 30.853  84.887  1.00 37.09 ? 512  GLU   A CB    1 
ATOM   3758  C  CG    . GLU   A  1  514  ? -32.797 29.985  85.808  1.00 41.54 ? 512  GLU   A CG    1 
ATOM   3759  C  CD    . GLU   A  1  514  ? -31.309 30.293  85.705  1.00 46.08 ? 512  GLU   A CD    1 
ATOM   3760  O  OE1   . GLU   A  1  514  ? -30.724 30.072  84.625  1.00 45.20 ? 512  GLU   A OE1   1 
ATOM   3761  O  OE2   . GLU   A  1  514  ? -30.725 30.763  86.704  1.00 58.93 ? 512  GLU   A OE2   1 
ATOM   3762  N  N     . LEU   A  1  515  ? -36.076 31.766  83.030  1.00 34.03 ? 513  LEU   A N     1 
ATOM   3763  C  CA    . LEU   A  1  515  ? -36.786 32.895  82.438  1.00 30.19 ? 513  LEU   A CA    1 
ATOM   3764  C  C     . LEU   A  1  515  ? -38.288 32.787  82.648  1.00 28.05 ? 513  LEU   A C     1 
ATOM   3765  O  O     . LEU   A  1  515  ? -38.976 33.810  82.694  1.00 28.71 ? 513  LEU   A O     1 
ATOM   3766  C  CB    . LEU   A  1  515  ? -36.457 33.007  80.950  1.00 31.23 ? 513  LEU   A CB    1 
ATOM   3767  C  CG    . LEU   A  1  515  ? -35.022 33.434  80.634  1.00 31.18 ? 513  LEU   A CG    1 
ATOM   3768  C  CD1   . LEU   A  1  515  ? -34.725 33.223  79.156  1.00 31.82 ? 513  LEU   A CD1   1 
ATOM   3769  C  CD2   . LEU   A  1  515  ? -34.797 34.888  81.038  1.00 30.29 ? 513  LEU   A CD2   1 
ATOM   3770  N  N     . ILE   A  1  516  ? -38.816 31.572  82.775  1.00 27.47 ? 514  ILE   A N     1 
ATOM   3771  C  CA    . ILE   A  1  516  ? -40.251 31.383  82.948  1.00 28.36 ? 514  ILE   A CA    1 
ATOM   3772  C  C     . ILE   A  1  516  ? -40.646 31.265  84.414  1.00 28.93 ? 514  ILE   A C     1 
ATOM   3773  O  O     . ILE   A  1  516  ? -41.815 30.985  84.713  1.00 29.20 ? 514  ILE   A O     1 
ATOM   3774  C  CB    . ILE   A  1  516  ? -40.798 30.217  82.109  1.00 28.38 ? 514  ILE   A CB    1 
ATOM   3775  C  CG1   . ILE   A  1  516  ? -40.274 28.879  82.643  1.00 34.05 ? 514  ILE   A CG1   1 
ATOM   3776  C  CG2   . ILE   A  1  516  ? -40.438 30.403  80.641  1.00 29.90 ? 514  ILE   A CG2   1 
ATOM   3777  C  CD1   . ILE   A  1  516  ? -40.836 27.669  81.917  1.00 34.91 ? 514  ILE   A CD1   1 
ATOM   3778  N  N     . ALA   A  1  517  ? -39.702 31.466  85.334  1.00 25.86 ? 515  ALA   A N     1 
ATOM   3779  C  CA    . ALA   A  1  517  ? -40.032 31.470  86.751  1.00 29.75 ? 515  ALA   A CA    1 
ATOM   3780  C  C     . ALA   A  1  517  ? -41.114 32.502  87.018  1.00 28.91 ? 515  ALA   A C     1 
ATOM   3781  O  O     . ALA   A  1  517  ? -41.078 33.614  86.491  1.00 27.34 ? 515  ALA   A O     1 
ATOM   3782  C  CB    . ALA   A  1  517  ? -38.798 31.814  87.583  1.00 30.79 ? 515  ALA   A CB    1 
ATOM   3783  N  N     . ASP   A  1  518  ? -42.085 32.118  87.824  1.00 26.83 ? 516  ASP   A N     1 
ATOM   3784  C  CA    . ASP   A  1  518  ? -43.231 32.956  88.127  1.00 25.50 ? 516  ASP   A CA    1 
ATOM   3785  C  C     . ASP   A  1  518  ? -42.888 33.897  89.273  1.00 25.81 ? 516  ASP   A C     1 
ATOM   3786  O  O     . ASP   A  1  518  ? -42.765 33.453  90.421  1.00 27.05 ? 516  ASP   A O     1 
ATOM   3787  C  CB    . ASP   A  1  518  ? -44.402 32.061  88.505  1.00 28.03 ? 516  ASP   A CB    1 
ATOM   3788  C  CG    . ASP   A  1  518  ? -45.662 32.840  88.781  1.00 28.96 ? 516  ASP   A CG    1 
ATOM   3789  O  OD1   . ASP   A  1  518  ? -45.644 34.091  88.677  1.00 28.68 ? 516  ASP   A OD1   1 
ATOM   3790  O  OD2   . ASP   A  1  518  ? -46.675 32.190  89.096  1.00 34.94 ? 516  ASP   A OD2   1 
ATOM   3791  N  N     . PRO   A  1  519  ? -42.751 35.200  89.015  1.00 26.14 ? 517  PRO   A N     1 
ATOM   3792  C  CA    . PRO   A  1  519  ? -42.364 36.111  90.103  1.00 25.80 ? 517  PRO   A CA    1 
ATOM   3793  C  C     . PRO   A  1  519  ? -43.362 36.140  91.246  1.00 23.38 ? 517  PRO   A C     1 
ATOM   3794  O  O     . PRO   A  1  519  ? -42.962 36.356  92.398  1.00 25.13 ? 517  PRO   A O     1 
ATOM   3795  C  CB    . PRO   A  1  519  ? -42.235 37.473  89.403  1.00 25.71 ? 517  PRO   A CB    1 
ATOM   3796  C  CG    . PRO   A  1  519  ? -43.038 37.348  88.159  1.00 28.55 ? 517  PRO   A CG    1 
ATOM   3797  C  CD    . PRO   A  1  519  ? -42.988 35.909  87.745  1.00 23.86 ? 517  PRO   A CD    1 
ATOM   3798  N  N     . VAL   A  1  520  ? -44.645 35.901  90.962  1.00 26.59 ? 518  VAL   A N     1 
ATOM   3799  C  CA    . VAL   A  1  520  ? -45.665 35.936  92.005  1.00 24.02 ? 518  VAL   A CA    1 
ATOM   3800  C  C     . VAL   A  1  520  ? -45.427 34.825  93.017  1.00 28.65 ? 518  VAL   A C     1 
ATOM   3801  O  O     . VAL   A  1  520  ? -45.437 35.052  94.230  1.00 28.05 ? 518  VAL   A O     1 
ATOM   3802  C  CB    . VAL   A  1  520  ? -47.069 35.849  91.385  1.00 26.19 ? 518  VAL   A CB    1 
ATOM   3803  C  CG1   . VAL   A  1  520  ? -48.130 35.898  92.480  1.00 28.76 ? 518  VAL   A CG1   1 
ATOM   3804  C  CG2   . VAL   A  1  520  ? -47.270 36.974  90.381  1.00 25.98 ? 518  VAL   A CG2   1 
ATOM   3805  N  N     . GLU   A  1  521  ? -45.200 33.607  92.526  1.00 28.70 ? 519  GLU   A N     1 
ATOM   3806  C  CA    . GLU   A  1  521  ? -44.967 32.489  93.430  1.00 30.54 ? 519  GLU   A CA    1 
ATOM   3807  C  C     . GLU   A  1  521  ? -43.601 32.577  94.095  1.00 33.60 ? 519  GLU   A C     1 
ATOM   3808  O  O     . GLU   A  1  521  ? -43.453 32.166  95.251  1.00 32.91 ? 519  GLU   A O     1 
ATOM   3809  C  CB    . GLU   A  1  521  ? -45.155 31.167  92.686  1.00 32.08 ? 519  GLU   A CB    1 
ATOM   3810  C  CG    . GLU   A  1  521  ? -46.585 30.960  92.213  1.00 33.75 ? 519  GLU   A CG    1 
ATOM   3811  C  CD    . GLU   A  1  521  ? -47.583 31.070  93.350  1.00 39.60 ? 519  GLU   A CD    1 
ATOM   3812  O  OE1   . GLU   A  1  521  ? -47.276 30.579  94.460  1.00 43.92 ? 519  GLU   A OE1   1 
ATOM   3813  O  OE2   . GLU   A  1  521  ? -48.672 31.646  93.144  1.00 40.23 ? 519  GLU   A OE2   1 
ATOM   3814  N  N     . VAL   A  1  522  ? -42.601 33.119  93.396  1.00 29.36 ? 520  VAL   A N     1 
ATOM   3815  C  CA    . VAL   A  1  522  ? -41.286 33.296  94.002  1.00 25.86 ? 520  VAL   A CA    1 
ATOM   3816  C  C     . VAL   A  1  522  ? -41.357 34.291  95.155  1.00 34.57 ? 520  VAL   A C     1 
ATOM   3817  O  O     . VAL   A  1  522  ? -40.812 34.051  96.239  1.00 32.33 ? 520  VAL   A O     1 
ATOM   3818  C  CB    . VAL   A  1  522  ? -40.241 33.701  92.946  1.00 31.22 ? 520  VAL   A CB    1 
ATOM   3819  C  CG1   . VAL   A  1  522  ? -38.908 33.999  93.615  1.00 28.62 ? 520  VAL   A CG1   1 
ATOM   3820  C  CG2   . VAL   A  1  522  ? -40.079 32.596  91.902  1.00 32.63 ? 520  VAL   A CG2   1 
ATOM   3821  N  N     . VAL   A  1  523  ? -42.034 35.423  94.942  1.00 28.66 ? 521  VAL   A N     1 
ATOM   3822  C  CA    . VAL   A  1  523  ? -42.175 36.398  96.018  1.00 28.03 ? 521  VAL   A CA    1 
ATOM   3823  C  C     . VAL   A  1  523  ? -42.999 35.818  97.159  1.00 30.52 ? 521  VAL   A C     1 
ATOM   3824  O  O     . VAL   A  1  523  ? -42.671 36.005  98.336  1.00 30.42 ? 521  VAL   A O     1 
ATOM   3825  C  CB    . VAL   A  1  523  ? -42.763 37.718  95.491  1.00 23.12 ? 521  VAL   A CB    1 
ATOM   3826  C  CG1   . VAL   A  1  523  ? -43.183 38.606  96.646  1.00 28.10 ? 521  VAL   A CG1   1 
ATOM   3827  C  CG2   . VAL   A  1  523  ? -41.736 38.429  94.634  1.00 26.65 ? 521  VAL   A CG2   1 
ATOM   3828  N  N     . ARG   A  1  524  ? -44.077 35.099  96.827  1.00 29.06 ? 522  ARG   A N     1 
ATOM   3829  C  CA    . ARG   A  1  524  ? -44.943 34.519  97.850  1.00 31.38 ? 522  ARG   A CA    1 
ATOM   3830  C  C     . ARG   A  1  524  ? -44.171 33.621  98.807  1.00 34.21 ? 522  ARG   A C     1 
ATOM   3831  O  O     . ARG   A  1  524  ? -44.498 33.560  99.998  1.00 37.91 ? 522  ARG   A O     1 
ATOM   3832  C  CB    . ARG   A  1  524  ? -46.059 33.713  97.189  1.00 34.11 ? 522  ARG   A CB    1 
ATOM   3833  C  CG    . ARG   A  1  524  ? -47.007 33.064  98.186  1.00 36.10 ? 522  ARG   A CG    1 
ATOM   3834  C  CD    . ARG   A  1  524  ? -47.885 32.019  97.538  1.00 39.64 ? 522  ARG   A CD    1 
ATOM   3835  N  NE    . ARG   A  1  524  ? -48.530 32.524  96.334  1.00 40.16 ? 522  ARG   A NE    1 
ATOM   3836  C  CZ    . ARG   A  1  524  ? -49.568 33.350  96.327  1.00 33.56 ? 522  ARG   A CZ    1 
ATOM   3837  N  NH1   . ARG   A  1  524  ? -50.083 33.822  97.451  1.00 39.24 ? 522  ARG   A NH1   1 
ATOM   3838  N  NH2   . ARG   A  1  524  ? -50.098 33.713  95.164  1.00 38.59 ? 522  ARG   A NH2   1 
ATOM   3839  N  N     . ALA   A  1  525  ? -43.141 32.935  98.316  1.00 32.48 ? 523  ALA   A N     1 
ATOM   3840  C  CA    . ALA   A  1  525  ? -42.407 31.950  99.098  1.00 34.94 ? 523  ALA   A CA    1 
ATOM   3841  C  C     . ALA   A  1  525  ? -41.203 32.528  99.829  1.00 38.48 ? 523  ALA   A C     1 
ATOM   3842  O  O     . ALA   A  1  525  ? -40.554 31.801  100.589 1.00 39.70 ? 523  ALA   A O     1 
ATOM   3843  C  CB    . ALA   A  1  525  ? -41.957 30.795  98.199  1.00 36.49 ? 523  ALA   A CB    1 
ATOM   3844  N  N     . MET   A  1  526  ? -40.887 33.804  99.624  1.00 34.15 ? 524  MET   A N     1 
ATOM   3845  C  CA    A MET   A  1  526  ? -39.746 34.413  100.291 0.51 35.10 ? 524  MET   A CA    1 
ATOM   3846  C  CA    B MET   A  1  526  ? -39.739 34.386  100.292 0.49 35.10 ? 524  MET   A CA    1 
ATOM   3847  C  C     . MET   A  1  526  ? -39.981 34.456  101.800 1.00 36.68 ? 524  MET   A C     1 
ATOM   3848  O  O     . MET   A  1  526  ? -41.126 34.550  102.252 1.00 35.54 ? 524  MET   A O     1 
ATOM   3849  C  CB    A MET   A  1  526  ? -39.535 35.833  99.770  0.51 37.45 ? 524  MET   A CB    1 
ATOM   3850  C  CB    B MET   A  1  526  ? -39.449 35.773  99.729  0.49 37.44 ? 524  MET   A CB    1 
ATOM   3851  C  CG    A MET   A  1  526  ? -39.027 35.900  98.344  0.51 37.57 ? 524  MET   A CG    1 
ATOM   3852  C  CG    B MET   A  1  526  ? -38.596 35.735  98.472  0.49 37.56 ? 524  MET   A CG    1 
ATOM   3853  S  SD    A MET   A  1  526  ? -37.431 35.083  98.164  0.51 42.12 ? 524  MET   A SD    1 
ATOM   3854  S  SD    B MET   A  1  526  ? -38.519 37.310  97.609  0.49 34.85 ? 524  MET   A SD    1 
ATOM   3855  C  CE    A MET   A  1  526  ? -36.411 36.085  99.247  0.51 38.43 ? 524  MET   A CE    1 
ATOM   3856  C  CE    B MET   A  1  526  ? -37.118 37.044  96.524  0.49 36.40 ? 524  MET   A CE    1 
ATOM   3857  N  N     . PRO   A  1  527  ? -38.913 34.389  102.605 1.00 40.96 ? 525  PRO   A N     1 
ATOM   3858  C  CA    . PRO   A  1  527  ? -39.112 34.390  104.065 1.00 41.77 ? 525  PRO   A CA    1 
ATOM   3859  C  C     . PRO   A  1  527  ? -39.781 35.651  104.579 1.00 38.93 ? 525  PRO   A C     1 
ATOM   3860  O  O     . PRO   A  1  527  ? -40.680 35.574  105.425 1.00 37.56 ? 525  PRO   A O     1 
ATOM   3861  C  CB    . PRO   A  1  527  ? -37.688 34.210  104.615 1.00 40.48 ? 525  PRO   A CB    1 
ATOM   3862  C  CG    . PRO   A  1  527  ? -36.798 34.688  103.523 1.00 40.09 ? 525  PRO   A CG    1 
ATOM   3863  C  CD    . PRO   A  1  527  ? -37.487 34.304  102.246 1.00 39.44 ? 525  PRO   A CD    1 
ATOM   3864  N  N     . VAL   A  1  528  ? -39.370 36.813  104.084 1.00 38.25 ? 526  VAL   A N     1 
ATOM   3865  C  CA    . VAL   A  1  528  ? -40.055 38.070  104.349 1.00 33.52 ? 526  VAL   A CA    1 
ATOM   3866  C  C     . VAL   A  1  528  ? -40.556 38.577  103.009 1.00 31.85 ? 526  VAL   A C     1 
ATOM   3867  O  O     . VAL   A  1  528  ? -39.755 38.937  102.137 1.00 33.81 ? 526  VAL   A O     1 
ATOM   3868  C  CB    . VAL   A  1  528  ? -39.138 39.097  105.020 1.00 35.60 ? 526  VAL   A CB    1 
ATOM   3869  C  CG1   . VAL   A  1  528  ? -39.890 40.395  105.252 1.00 38.03 ? 526  VAL   A CG1   1 
ATOM   3870  C  CG2   . VAL   A  1  528  ? -38.601 38.541  106.333 1.00 38.07 ? 526  VAL   A CG2   1 
ATOM   3871  N  N     . VAL   A  1  529  ? -41.873 38.593  102.831 1.00 30.60 ? 527  VAL   A N     1 
ATOM   3872  C  CA    . VAL   A  1  529  ? -42.445 39.041  101.568 1.00 29.54 ? 527  VAL   A CA    1 
ATOM   3873  C  C     . VAL   A  1  529  ? -42.190 40.534  101.409 1.00 29.54 ? 527  VAL   A C     1 
ATOM   3874  O  O     . VAL   A  1  529  ? -42.545 41.339  102.278 1.00 30.99 ? 527  VAL   A O     1 
ATOM   3875  C  CB    . VAL   A  1  529  ? -43.939 38.711  101.488 1.00 26.43 ? 527  VAL   A CB    1 
ATOM   3876  C  CG1   . VAL   A  1  529  ? -44.547 39.373  100.268 1.00 28.70 ? 527  VAL   A CG1   1 
ATOM   3877  C  CG2   . VAL   A  1  529  ? -44.136 37.199  101.430 1.00 33.74 ? 527  VAL   A CG2   1 
ATOM   3878  N  N     . GLY   A  1  530  ? -41.548 40.908  100.306 1.00 26.88 ? 528  GLY   A N     1 
ATOM   3879  C  CA    . GLY   A  1  530  ? -41.345 42.309  100.011 1.00 25.98 ? 528  GLY   A CA    1 
ATOM   3880  C  C     . GLY   A  1  530  ? -40.173 42.969  100.695 1.00 23.88 ? 528  GLY   A C     1 
ATOM   3881  O  O     . GLY   A  1  530  ? -40.143 44.198  100.781 1.00 24.57 ? 528  GLY   A O     1 
ATOM   3882  N  N     . ALA   A  1  531  ? -39.206 42.201  101.199 1.00 25.71 ? 529  ALA   A N     1 
ATOM   3883  C  CA    . ALA   A  1  531  ? -38.043 42.816  101.827 1.00 24.45 ? 529  ALA   A CA    1 
ATOM   3884  C  C     . ALA   A  1  531  ? -37.268 43.667  100.824 1.00 22.29 ? 529  ALA   A C     1 
ATOM   3885  O  O     . ALA   A  1  531  ? -37.128 43.302  99.652  1.00 26.16 ? 529  ALA   A O     1 
ATOM   3886  C  CB    . ALA   A  1  531  ? -37.118 41.745  102.414 1.00 25.88 ? 529  ALA   A CB    1 
ATOM   3887  N  N     . LYS   A  1  532  ? -36.770 44.811  101.302 1.00 23.21 ? 530  LYS   A N     1 
ATOM   3888  C  CA    . LYS   A  1  532  ? -35.887 45.675  100.528 1.00 24.76 ? 530  LYS   A CA    1 
ATOM   3889  C  C     . LYS   A  1  532  ? -34.687 44.886  100.022 1.00 25.09 ? 530  LYS   A C     1 
ATOM   3890  O  O     . LYS   A  1  532  ? -34.263 43.899  100.629 1.00 23.48 ? 530  LYS   A O     1 
ATOM   3891  C  CB    . LYS   A  1  532  ? -35.386 46.813  101.433 1.00 27.66 ? 530  LYS   A CB    1 
ATOM   3892  C  CG    . LYS   A  1  532  ? -34.386 47.771  100.788 1.00 30.74 ? 530  LYS   A CG    1 
ATOM   3893  C  CD    . LYS   A  1  532  ? -33.896 48.843  101.751 1.00 25.28 ? 530  LYS   A CD    1 
ATOM   3894  C  CE    . LYS   A  1  532  ? -33.080 48.251  102.898 1.00 26.91 ? 530  LYS   A CE    1 
ATOM   3895  N  NZ    . LYS   A  1  532  ? -31.777 47.695  102.428 1.00 27.15 ? 530  LYS   A NZ    1 
ATOM   3896  N  N     . HIS   A  1  533  ? -34.144 45.319  98.889  1.00 21.38 ? 531  HIS   A N     1 
ATOM   3897  C  CA    . HIS   A  1  533  ? -32.906 44.742  98.397  1.00 19.85 ? 531  HIS   A CA    1 
ATOM   3898  C  C     . HIS   A  1  533  ? -31.815 44.905  99.446  1.00 24.35 ? 531  HIS   A C     1 
ATOM   3899  O  O     . HIS   A  1  533  ? -31.630 45.989  100.007 1.00 24.33 ? 531  HIS   A O     1 
ATOM   3900  C  CB    . HIS   A  1  533  ? -32.492 45.433  97.102  1.00 22.36 ? 531  HIS   A CB    1 
ATOM   3901  C  CG    . HIS   A  1  533  ? -31.514 44.641  96.301  1.00 23.25 ? 531  HIS   A CG    1 
ATOM   3902  N  ND1   . HIS   A  1  533  ? -30.219 44.422  96.722  1.00 23.91 ? 531  HIS   A ND1   1 
ATOM   3903  C  CD2   . HIS   A  1  533  ? -31.647 43.973  95.131  1.00 28.89 ? 531  HIS   A CD2   1 
ATOM   3904  C  CE1   . HIS   A  1  533  ? -29.589 43.675  95.833  1.00 30.88 ? 531  HIS   A CE1   1 
ATOM   3905  N  NE2   . HIS   A  1  533  ? -30.434 43.386  94.859  1.00 32.24 ? 531  HIS   A NE2   1 
ATOM   3906  N  N     . ASP   A  1  534  ? -31.096 43.811  99.714  1.00 24.65 ? 532  ASP   A N     1 
ATOM   3907  C  CA    . ASP   A  1  534  ? -30.067 43.832  100.745 1.00 24.27 ? 532  ASP   A CA    1 
ATOM   3908  C  C     . ASP   A  1  534  ? -28.924 44.776  100.396 1.00 25.33 ? 532  ASP   A C     1 
ATOM   3909  O  O     . ASP   A  1  534  ? -28.241 45.278  101.296 1.00 30.49 ? 532  ASP   A O     1 
ATOM   3910  C  CB    . ASP   A  1  534  ? -29.526 42.418  100.955 1.00 29.67 ? 532  ASP   A CB    1 
ATOM   3911  N  N     . ARG   A  1  535  ? -28.704 45.040  99.111  1.00 22.53 ? 533  ARG   A N     1 
ATOM   3912  C  CA    . ARG   A  1  535  ? -27.555 45.816  98.671  1.00 23.47 ? 533  ARG   A CA    1 
ATOM   3913  C  C     . ARG   A  1  535  ? -27.892 47.271  98.368  1.00 22.34 ? 533  ARG   A C     1 
ATOM   3914  O  O     . ARG   A  1  535  ? -27.043 47.995  97.839  1.00 24.67 ? 533  ARG   A O     1 
ATOM   3915  C  CB    . ARG   A  1  535  ? -26.893 45.160  97.456  1.00 29.49 ? 533  ARG   A CB    1 
ATOM   3916  N  N     . ILE   A  1  536  ? -29.096 47.724  98.696  1.00 21.46 ? 534  ILE   A N     1 
ATOM   3917  C  CA    . ILE   A  1  536  ? -29.471 49.116  98.504  1.00 21.29 ? 534  ILE   A CA    1 
ATOM   3918  C  C     . ILE   A  1  536  ? -29.769 49.714  99.868  1.00 21.49 ? 534  ILE   A C     1 
ATOM   3919  O  O     . ILE   A  1  536  ? -30.658 49.237  100.581 1.00 24.48 ? 534  ILE   A O     1 
ATOM   3920  C  CB    . ILE   A  1  536  ? -30.666 49.258  97.556  1.00 22.03 ? 534  ILE   A CB    1 
ATOM   3921  C  CG1   . ILE   A  1  536  ? -30.289 48.711  96.183  1.00 25.75 ? 534  ILE   A CG1   1 
ATOM   3922  C  CG2   . ILE   A  1  536  ? -31.112 50.713  97.482  1.00 21.50 ? 534  ILE   A CG2   1 
ATOM   3923  C  CD1   . ILE   A  1  536  ? -31.424 48.739  95.221  1.00 24.66 ? 534  ILE   A CD1   1 
ATOM   3924  N  N     . ALA   A  1  537  ? -29.032 50.750  100.229 1.00 20.50 ? 535  ALA   A N     1 
ATOM   3925  C  CA    . ALA   A  1  537  ? -29.206 51.367  101.531 1.00 19.75 ? 535  ALA   A CA    1 
ATOM   3926  C  C     . ALA   A  1  537  ? -30.398 52.314  101.504 1.00 20.14 ? 535  ALA   A C     1 
ATOM   3927  O  O     . ALA   A  1  537  ? -30.541 53.124  100.583 1.00 19.14 ? 535  ALA   A O     1 
ATOM   3928  C  CB    . ALA   A  1  537  ? -27.946 52.145  101.899 1.00 22.76 ? 535  ALA   A CB    1 
ATOM   3929  N  N     . LEU   A  1  538  ? -31.252 52.218  102.515 1.00 20.11 ? 536  LEU   A N     1 
ATOM   3930  C  CA    . LEU   A  1  538  ? -32.204 53.286  102.732 1.00 20.02 ? 536  LEU   A CA    1 
ATOM   3931  C  C     . LEU   A  1  538  ? -31.426 54.579  102.957 1.00 22.47 ? 536  LEU   A C     1 
ATOM   3932  O  O     . LEU   A  1  538  ? -30.285 54.556  103.433 1.00 20.47 ? 536  LEU   A O     1 
ATOM   3933  C  CB    . LEU   A  1  538  ? -33.070 52.994  103.955 1.00 21.25 ? 536  LEU   A CB    1 
ATOM   3934  C  CG    . LEU   A  1  538  ? -34.138 51.918  103.792 1.00 22.02 ? 536  LEU   A CG    1 
ATOM   3935  C  CD1   . LEU   A  1  538  ? -34.773 51.625  105.139 1.00 25.41 ? 536  LEU   A CD1   1 
ATOM   3936  C  CD2   . LEU   A  1  538  ? -35.185 52.365  102.800 1.00 23.54 ? 536  LEU   A CD2   1 
ATOM   3937  N  N     . PRO   A  1  539  ? -32.002 55.718  102.607 1.00 18.99 ? 537  PRO   A N     1 
ATOM   3938  C  CA    . PRO   A  1  539  ? -31.258 56.977  102.764 1.00 18.39 ? 537  PRO   A CA    1 
ATOM   3939  C  C     . PRO   A  1  539  ? -30.729 57.196  104.172 1.00 18.64 ? 537  PRO   A C     1 
ATOM   3940  O  O     . PRO   A  1  539  ? -29.588 57.646  104.325 1.00 19.53 ? 537  PRO   A O     1 
ATOM   3941  C  CB    . PRO   A  1  539  ? -32.273 58.032  102.317 1.00 18.29 ? 537  PRO   A CB    1 
ATOM   3942  C  CG    . PRO   A  1  539  ? -33.105 57.286  101.297 1.00 18.81 ? 537  PRO   A CG    1 
ATOM   3943  C  CD    . PRO   A  1  539  ? -33.263 55.906  101.868 1.00 19.55 ? 537  PRO   A CD    1 
ATOM   3944  N  N     . ALA   A  1  540  ? -31.499 56.838  105.203 1.00 19.51 ? 538  ALA   A N     1 
ATOM   3945  C  CA    . ALA   A  1  540  ? -31.032 57.019  106.572 1.00 21.08 ? 538  ALA   A CA    1 
ATOM   3946  C  C     . ALA   A  1  540  ? -29.796 56.188  106.876 1.00 24.26 ? 538  ALA   A C     1 
ATOM   3947  O  O     . ALA   A  1  540  ? -29.090 56.486  107.846 1.00 23.45 ? 538  ALA   A O     1 
ATOM   3948  C  CB    . ALA   A  1  540  ? -32.139 56.657  107.564 1.00 24.30 ? 538  ALA   A CB    1 
ATOM   3949  N  N     . GLU   A  1  541  ? -29.520 55.156  106.081 1.00 22.63 ? 539  GLU   A N     1 
ATOM   3950  C  CA    . GLU   A  1  541  ? -28.473 54.191  106.394 1.00 24.00 ? 539  GLU   A CA    1 
ATOM   3951  C  C     . GLU   A  1  541  ? -27.252 54.329  105.489 1.00 22.80 ? 539  GLU   A C     1 
ATOM   3952  O  O     . GLU   A  1  541  ? -26.412 53.422  105.440 1.00 22.78 ? 539  GLU   A O     1 
ATOM   3953  C  CB    . GLU   A  1  541  ? -29.048 52.773  106.380 1.00 26.44 ? 539  GLU   A CB    1 
ATOM   3954  C  CG    . GLU   A  1  541  ? -30.201 52.620  107.362 1.00 32.17 ? 539  GLU   A CG    1 
ATOM   3955  C  CD    . GLU   A  1  541  ? -30.782 51.223  107.395 1.00 43.90 ? 539  GLU   A CD    1 
ATOM   3956  O  OE1   . GLU   A  1  541  ? -30.007 50.250  107.291 1.00 54.79 ? 539  GLU   A OE1   1 
ATOM   3957  O  OE2   . GLU   A  1  541  ? -32.018 51.097  107.521 1.00 48.96 ? 539  GLU   A OE2   1 
ATOM   3958  N  N     . LEU   A  1  542  ? -27.130 55.460  104.783 1.00 20.43 ? 540  LEU   A N     1 
ATOM   3959  C  CA    . LEU   A  1  542  ? -26.028 55.642  103.842 1.00 24.32 ? 540  LEU   A CA    1 
ATOM   3960  C  C     . LEU   A  1  542  ? -24.671 55.445  104.491 1.00 22.68 ? 540  LEU   A C     1 
ATOM   3961  O  O     . LEU   A  1  542  ? -23.721 55.021  103.828 1.00 24.19 ? 540  LEU   A O     1 
ATOM   3962  C  CB    . LEU   A  1  542  ? -26.060 57.046  103.254 1.00 24.98 ? 540  LEU   A CB    1 
ATOM   3963  C  CG    . LEU   A  1  542  ? -26.924 57.332  102.038 1.00 28.73 ? 540  LEU   A CG    1 
ATOM   3964  C  CD1   . LEU   A  1  542  ? -26.455 58.645  101.448 1.00 23.46 ? 540  LEU   A CD1   1 
ATOM   3965  C  CD2   . LEU   A  1  542  ? -26.858 56.208  101.015 1.00 27.09 ? 540  LEU   A CD2   1 
ATOM   3966  N  N     . PHE   A  1  543  ? -24.548 55.772  105.773 1.00 20.64 ? 541  PHE   A N     1 
ATOM   3967  C  CA    . PHE   A  1  543  ? -23.266 55.697  106.451 1.00 22.82 ? 541  PHE   A CA    1 
ATOM   3968  C  C     . PHE   A  1  543  ? -23.171 54.491  107.365 1.00 23.09 ? 541  PHE   A C     1 
ATOM   3969  O  O     . PHE   A  1  543  ? -22.198 54.368  108.115 1.00 23.38 ? 541  PHE   A O     1 
ATOM   3970  C  CB    . PHE   A  1  543  ? -22.993 57.001  107.195 1.00 22.44 ? 541  PHE   A CB    1 
ATOM   3971  C  CG    . PHE   A  1  543  ? -23.230 58.211  106.350 1.00 21.27 ? 541  PHE   A CG    1 
ATOM   3972  C  CD1   . PHE   A  1  543  ? -22.538 58.373  105.163 1.00 25.62 ? 541  PHE   A CD1   1 
ATOM   3973  C  CD2   . PHE   A  1  543  ? -24.168 59.164  106.714 1.00 20.24 ? 541  PHE   A CD2   1 
ATOM   3974  C  CE1   . PHE   A  1  543  ? -22.768 59.468  104.362 1.00 23.03 ? 541  PHE   A CE1   1 
ATOM   3975  C  CE2   . PHE   A  1  543  ? -24.399 60.262  105.920 1.00 19.59 ? 541  PHE   A CE2   1 
ATOM   3976  C  CZ    . PHE   A  1  543  ? -23.708 60.417  104.744 1.00 21.20 ? 541  PHE   A CZ    1 
ATOM   3977  N  N     . GLY   A  1  544  ? -24.163 53.607  107.317 1.00 21.42 ? 542  GLY   A N     1 
ATOM   3978  C  CA    . GLY   A  1  544  ? -24.101 52.377  108.088 1.00 26.45 ? 542  GLY   A CA    1 
ATOM   3979  C  C     . GLY   A  1  544  ? -23.959 52.654  109.569 1.00 24.81 ? 542  GLY   A C     1 
ATOM   3980  O  O     . GLY   A  1  544  ? -24.638 53.517  110.136 1.00 25.16 ? 542  GLY   A O     1 
ATOM   3981  N  N     . ASP   A  1  545  ? -23.037 51.931  110.200 1.00 27.52 ? 543  ASP   A N     1 
ATOM   3982  C  CA    . ASP   A  1  545  ? -22.852 52.010  111.643 1.00 29.83 ? 543  ASP   A CA    1 
ATOM   3983  C  C     . ASP   A  1  545  ? -22.167 53.289  112.097 1.00 30.16 ? 543  ASP   A C     1 
ATOM   3984  O  O     . ASP   A  1  545  ? -22.189 53.580  113.299 1.00 30.54 ? 543  ASP   A O     1 
ATOM   3985  C  CB    . ASP   A  1  545  ? -22.028 50.816  112.132 1.00 34.68 ? 543  ASP   A CB    1 
ATOM   3986  C  CG    . ASP   A  1  545  ? -22.686 49.487  111.818 1.00 47.64 ? 543  ASP   A CG    1 
ATOM   3987  O  OD1   . ASP   A  1  545  ? -23.935 49.443  111.756 1.00 46.99 ? 543  ASP   A OD1   1 
ATOM   3988  O  OD2   . ASP   A  1  545  ? -21.956 48.487  111.636 1.00 59.32 ? 543  ASP   A OD2   1 
ATOM   3989  N  N     . ALA   A  1  546  ? -21.563 54.052  111.185 1.00 26.13 ? 544  ALA   A N     1 
ATOM   3990  C  CA    . ALA   A  1  546  ? -20.831 55.248  111.594 1.00 26.76 ? 544  ALA   A CA    1 
ATOM   3991  C  C     . ALA   A  1  546  ? -21.769 56.280  112.200 1.00 27.87 ? 544  ALA   A C     1 
ATOM   3992  O  O     . ALA   A  1  546  ? -21.486 56.848  113.259 1.00 27.58 ? 544  ALA   A O     1 
ATOM   3993  C  CB    . ALA   A  1  546  ? -20.072 55.843  110.411 1.00 24.03 ? 544  ALA   A CB    1 
ATOM   3994  N  N     . ARG   A  1  547  ? -22.895 56.532  111.543 1.00 23.19 ? 545  ARG   A N     1 
ATOM   3995  C  CA    . ARG   A  1  547  ? -23.842 57.516  112.041 1.00 25.32 ? 545  ARG   A CA    1 
ATOM   3996  C  C     . ARG   A  1  547  ? -25.097 57.434  111.195 1.00 20.49 ? 545  ARG   A C     1 
ATOM   3997  O  O     . ARG   A  1  547  ? -25.105 56.855  110.105 1.00 21.79 ? 545  ARG   A O     1 
ATOM   3998  C  CB    . ARG   A  1  547  ? -23.287 58.938  112.017 1.00 29.18 ? 545  ARG   A CB    1 
ATOM   3999  C  CG    . ARG   A  1  547  ? -23.026 59.454  110.646 1.00 28.70 ? 545  ARG   A CG    1 
ATOM   4000  C  CD    . ARG   A  1  547  ? -22.384 60.814  110.704 1.00 26.73 ? 545  ARG   A CD    1 
ATOM   4001  N  NE    . ARG   A  1  547  ? -21.556 61.006  109.524 1.00 24.49 ? 545  ARG   A NE    1 
ATOM   4002  C  CZ    . ARG   A  1  547  ? -21.937 61.646  108.426 1.00 21.93 ? 545  ARG   A CZ    1 
ATOM   4003  N  NH1   . ARG   A  1  547  ? -23.107 62.263  108.350 1.00 22.66 ? 545  ARG   A NH1   1 
ATOM   4004  N  NH2   . ARG   A  1  547  ? -21.120 61.668  107.378 1.00 24.99 ? 545  ARG   A NH2   1 
ATOM   4005  N  N     . THR   A  1  548  ? -26.150 58.045  111.716 1.00 20.34 ? 546  THR   A N     1 
ATOM   4006  C  CA    . THR   A  1  548  ? -27.438 58.097  111.051 1.00 19.61 ? 546  THR   A CA    1 
ATOM   4007  C  C     . THR   A  1  548  ? -27.458 59.316  110.148 1.00 18.95 ? 546  THR   A C     1 
ATOM   4008  O  O     . THR   A  1  548  ? -27.189 60.434  110.598 1.00 19.67 ? 546  THR   A O     1 
ATOM   4009  C  CB    . THR   A  1  548  ? -28.533 58.228  112.105 1.00 23.20 ? 546  THR   A CB    1 
ATOM   4010  O  OG1   . THR   A  1  548  ? -28.423 57.139  113.028 1.00 28.32 ? 546  THR   A OG1   1 
ATOM   4011  C  CG2   . THR   A  1  548  ? -29.890 58.204  111.455 1.00 23.23 ? 546  THR   A CG2   1 
ATOM   4012  N  N     . ASN   A  1  549  ? -27.773 59.099  108.876 1.00 18.40 ? 547  ASN   A N     1 
ATOM   4013  C  CA    . ASN   A  1  549  ? -27.904 60.209  107.947 1.00 17.66 ? 547  ASN   A CA    1 
ATOM   4014  C  C     . ASN   A  1  549  ? -29.039 61.117  108.399 1.00 19.86 ? 547  ASN   A C     1 
ATOM   4015  O  O     . ASN   A  1  549  ? -30.039 60.657  108.953 1.00 20.55 ? 547  ASN   A O     1 
ATOM   4016  C  CB    . ASN   A  1  549  ? -28.213 59.648  106.560 1.00 18.05 ? 547  ASN   A CB    1 
ATOM   4017  C  CG    . ASN   A  1  549  ? -28.045 60.673  105.459 1.00 18.13 ? 547  ASN   A CG    1 
ATOM   4018  O  OD1   . ASN   A  1  549  ? -27.511 61.766  105.665 1.00 18.71 ? 547  ASN   A OD1   1 
ATOM   4019  N  ND2   . ASN   A  1  549  ? -28.489 60.317  104.265 1.00 19.31 ? 547  ASN   A ND2   1 
ATOM   4020  N  N     . SER   A  1  550  ? -28.875 62.418  108.188 1.00 18.41 ? 548  SER   A N     1 
ATOM   4021  C  CA    . SER   A  1  550  ? -29.997 63.319  108.410 1.00 17.33 ? 548  SER   A CA    1 
ATOM   4022  C  C     . SER   A  1  550  ? -31.103 63.014  107.414 1.00 18.40 ? 548  SER   A C     1 
ATOM   4023  O  O     . SER   A  1  550  ? -30.864 62.493  106.324 1.00 20.04 ? 548  SER   A O     1 
ATOM   4024  C  CB    . SER   A  1  550  ? -29.557 64.763  108.230 1.00 18.69 ? 548  SER   A CB    1 
ATOM   4025  O  OG    . SER   A  1  550  ? -29.029 64.966  106.935 1.00 18.52 ? 548  SER   A OG    1 
ATOM   4026  N  N     . ALA   A  1  551  ? -32.329 63.335  107.809 1.00 20.09 ? 549  ALA   A N     1 
ATOM   4027  C  CA    . ALA   A  1  551  ? -33.498 63.136  106.965 1.00 21.57 ? 549  ALA   A CA    1 
ATOM   4028  C  C     . ALA   A  1  551  ? -33.983 64.470  106.421 1.00 19.68 ? 549  ALA   A C     1 
ATOM   4029  O  O     . ALA   A  1  551  ? -34.010 65.477  107.132 1.00 19.92 ? 549  ALA   A O     1 
ATOM   4030  C  CB    . ALA   A  1  551  ? -34.630 62.470  107.749 1.00 21.93 ? 549  ALA   A CB    1 
ATOM   4031  N  N     . GLY   A  1  552  ? -34.388 64.464  105.157 1.00 18.77 ? 550  GLY   A N     1 
ATOM   4032  C  CA    . GLY   A  1  552  ? -34.990 65.614  104.536 1.00 19.43 ? 550  GLY   A CA    1 
ATOM   4033  C  C     . GLY   A  1  552  ? -36.498 65.511  104.517 1.00 20.99 ? 550  GLY   A C     1 
ATOM   4034  O  O     . GLY   A  1  552  ? -37.110 64.752  105.275 1.00 22.33 ? 550  GLY   A O     1 
ATOM   4035  N  N     . LEU   A  1  553  ? -37.103 66.272  103.611 1.00 19.88 ? 551  LEU   A N     1 
ATOM   4036  C  CA    . LEU   A  1  553  ? -38.547 66.323  103.463 1.00 19.22 ? 551  LEU   A CA    1 
ATOM   4037  C  C     . LEU   A  1  553  ? -38.846 66.310  101.977 1.00 19.82 ? 551  LEU   A C     1 
ATOM   4038  O  O     . LEU   A  1  553  ? -38.112 66.906  101.190 1.00 21.59 ? 551  LEU   A O     1 
ATOM   4039  C  CB    . LEU   A  1  553  ? -39.103 67.608  104.065 1.00 23.29 ? 551  LEU   A CB    1 
ATOM   4040  C  CG    . LEU   A  1  553  ? -39.001 67.716  105.585 1.00 21.80 ? 551  LEU   A CG    1 
ATOM   4041  C  CD1   . LEU   A  1  553  ? -39.499 69.078  106.043 1.00 29.15 ? 551  LEU   A CD1   1 
ATOM   4042  C  CD2   . LEU   A  1  553  ? -39.793 66.598  106.265 1.00 24.06 ? 551  LEU   A CD2   1 
ATOM   4043  N  N     . ASP   A  1  554  ? -39.922 65.633  101.604 1.00 19.40 ? 552  ASP   A N     1 
ATOM   4044  C  CA    . ASP   A  1  554  ? -40.279 65.491  100.195 1.00 21.08 ? 552  ASP   A CA    1 
ATOM   4045  C  C     . ASP   A  1  554  ? -41.249 66.607  99.840  1.00 17.85 ? 552  ASP   A C     1 
ATOM   4046  O  O     . ASP   A  1  554  ? -42.441 66.529  100.150 1.00 18.09 ? 552  ASP   A O     1 
ATOM   4047  C  CB    . ASP   A  1  554  ? -40.904 64.129  99.940  1.00 18.84 ? 552  ASP   A CB    1 
ATOM   4048  C  CG    . ASP   A  1  554  ? -41.213 63.908  98.477  1.00 18.76 ? 552  ASP   A CG    1 
ATOM   4049  O  OD1   . ASP   A  1  554  ? -40.971 64.834  97.670  1.00 20.63 ? 552  ASP   A OD1   1 
ATOM   4050  O  OD2   . ASP   A  1  554  ? -41.683 62.805  98.136  1.00 21.56 ? 552  ASP   A OD2   1 
ATOM   4051  N  N     . LEU   A  1  555  ? -40.746 67.629  99.148  1.00 17.73 ? 553  LEU   A N     1 
ATOM   4052  C  CA    . LEU   A  1  555  ? -41.583 68.765  98.783  1.00 16.80 ? 553  LEU   A CA    1 
ATOM   4053  C  C     . LEU   A  1  555  ? -42.469 68.490  97.578  1.00 18.26 ? 553  LEU   A C     1 
ATOM   4054  O  O     . LEU   A  1  555  ? -43.158 69.403  97.115  1.00 19.68 ? 553  LEU   A O     1 
ATOM   4055  C  CB    . LEU   A  1  555  ? -40.736 70.016  98.580  1.00 18.83 ? 553  LEU   A CB    1 
ATOM   4056  C  CG    . LEU   A  1  555  ? -39.939 70.402  99.829  1.00 19.57 ? 553  LEU   A CG    1 
ATOM   4057  C  CD1   . LEU   A  1  555  ? -39.219 71.717  99.594  1.00 23.67 ? 553  LEU   A CD1   1 
ATOM   4058  C  CD2   . LEU   A  1  555  ? -40.855 70.477  101.047 1.00 23.60 ? 553  LEU   A CD2   1 
ATOM   4059  N  N     . SER   A  1  556  ? -42.484 67.255  97.092  1.00 16.96 ? 554  SER   A N     1 
ATOM   4060  C  CA    . SER   A  1  556  ? -43.473 66.819  96.117  1.00 18.61 ? 554  SER   A CA    1 
ATOM   4061  C  C     . SER   A  1  556  ? -44.611 66.041  96.757  1.00 19.79 ? 554  SER   A C     1 
ATOM   4062  O  O     . SER   A  1  556  ? -45.540 65.645  96.056  1.00 19.28 ? 554  SER   A O     1 
ATOM   4063  C  CB    . SER   A  1  556  ? -42.812 65.958  95.034  1.00 18.74 ? 554  SER   A CB    1 
ATOM   4064  O  OG    . SER   A  1  556  ? -42.531 64.650  95.518  1.00 20.41 ? 554  SER   A OG    1 
ATOM   4065  N  N     . ASN   A  1  557  ? -44.571 65.821  98.066  1.00 16.52 ? 555  ASN   A N     1 
ATOM   4066  C  CA    . ASN   A  1  557  ? -45.572 65.019  98.752  1.00 17.34 ? 555  ASN   A CA    1 
ATOM   4067  C  C     . ASN   A  1  557  ? -46.608 65.963  99.345  1.00 20.30 ? 555  ASN   A C     1 
ATOM   4068  O  O     . ASN   A  1  557  ? -46.268 66.802  100.185 1.00 18.46 ? 555  ASN   A O     1 
ATOM   4069  C  CB    . ASN   A  1  557  ? -44.871 64.205  99.844  1.00 19.08 ? 555  ASN   A CB    1 
ATOM   4070  C  CG    . ASN   A  1  557  ? -45.820 63.315  100.611 1.00 18.67 ? 555  ASN   A CG    1 
ATOM   4071  O  OD1   . ASN   A  1  557  ? -46.846 63.768  101.096 1.00 20.76 ? 555  ASN   A OD1   1 
ATOM   4072  N  ND2   . ASN   A  1  557  ? -45.483 62.033  100.713 1.00 21.38 ? 555  ASN   A ND2   1 
ATOM   4073  N  N     . GLU   A  1  558  ? -47.876 65.823  98.916  1.00 19.05 ? 556  GLU   A N     1 
ATOM   4074  C  CA    . GLU   A  1  558  ? -48.907 66.755  99.376  1.00 19.34 ? 556  GLU   A CA    1 
ATOM   4075  C  C     . GLU   A  1  558  ? -49.120 66.683  100.873 1.00 18.42 ? 556  GLU   A C     1 
ATOM   4076  O  O     . GLU   A  1  558  ? -49.448 67.702  101.496 1.00 21.02 ? 556  GLU   A O     1 
ATOM   4077  C  CB    . GLU   A  1  558  ? -50.250 66.528  98.678  1.00 20.79 ? 556  GLU   A CB    1 
ATOM   4078  C  CG    . GLU   A  1  558  ? -50.247 66.838  97.200  1.00 21.66 ? 556  GLU   A CG    1 
ATOM   4079  C  CD    . GLU   A  1  558  ? -49.973 68.299  96.845  1.00 18.85 ? 556  GLU   A CD    1 
ATOM   4080  O  OE1   . GLU   A  1  558  ? -49.987 69.200  97.702  1.00 20.05 ? 556  GLU   A OE1   1 
ATOM   4081  O  OE2   . GLU   A  1  558  ? -49.762 68.551  95.646  1.00 19.36 ? 556  GLU   A OE2   1 
ATOM   4082  N  N     . GLU   A  1  559  ? -48.981 65.495  101.468 1.00 19.33 ? 557  GLU   A N     1 
ATOM   4083  C  CA    . GLU   A  1  559  ? -49.079 65.401  102.921 1.00 22.13 ? 557  GLU   A CA    1 
ATOM   4084  C  C     . GLU   A  1  559  ? -47.977 66.216  103.568 1.00 20.52 ? 557  GLU   A C     1 
ATOM   4085  O  O     . GLU   A  1  559  ? -48.218 66.973  104.514 1.00 21.71 ? 557  GLU   A O     1 
ATOM   4086  C  CB    . GLU   A  1  559  ? -48.979 63.947  103.386 1.00 24.66 ? 557  GLU   A CB    1 
ATOM   4087  C  CG    . GLU   A  1  559  ? -50.087 63.011  102.946 1.00 24.05 ? 557  GLU   A CG    1 
ATOM   4088  C  CD    . GLU   A  1  559  ? -49.806 61.574  103.371 1.00 34.20 ? 557  GLU   A CD    1 
ATOM   4089  O  OE1   . GLU   A  1  559  ? -48.827 61.355  104.120 1.00 41.32 ? 557  GLU   A OE1   1 
ATOM   4090  O  OE2   . GLU   A  1  559  ? -50.550 60.661  102.953 1.00 31.96 ? 557  GLU   A OE2   1 
ATOM   4091  N  N     . THR   A  1  560  ? -46.751 66.075  103.058 1.00 19.68 ? 558  THR   A N     1 
ATOM   4092  C  CA    . THR   A  1  560  ? -45.638 66.837  103.606 1.00 21.28 ? 558  THR   A CA    1 
ATOM   4093  C  C     . THR   A  1  560  ? -45.861 68.325  103.411 1.00 18.81 ? 558  THR   A C     1 
ATOM   4094  O  O     . THR   A  1  560  ? -45.626 69.121  104.324 1.00 20.87 ? 558  THR   A O     1 
ATOM   4095  C  CB    . THR   A  1  560  ? -44.342 66.405  102.933 1.00 20.61 ? 558  THR   A CB    1 
ATOM   4096  O  OG1   . THR   A  1  560  ? -44.174 64.997  103.119 1.00 22.53 ? 558  THR   A OG1   1 
ATOM   4097  C  CG2   . THR   A  1  560  ? -43.153 67.167  103.517 1.00 22.65 ? 558  THR   A CG2   1 
ATOM   4098  N  N     . LEU   A  1  561  ? -46.342 68.721  102.231 1.00 19.74 ? 559  LEU   A N     1 
ATOM   4099  C  CA    . LEU   A  1  561  ? -46.554 70.139  101.983 1.00 17.42 ? 559  LEU   A CA    1 
ATOM   4100  C  C     . LEU   A  1  561  ? -47.631 70.693  102.895 1.00 18.96 ? 559  LEU   A C     1 
ATOM   4101  O  O     . LEU   A  1  561  ? -47.521 71.829  103.371 1.00 20.60 ? 559  LEU   A O     1 
ATOM   4102  C  CB    . LEU   A  1  561  ? -46.925 70.368  100.524 1.00 17.06 ? 559  LEU   A CB    1 
ATOM   4103  C  CG    . LEU   A  1  561  ? -45.762 70.123  99.577  1.00 16.42 ? 559  LEU   A CG    1 
ATOM   4104  C  CD1   . LEU   A  1  561  ? -46.259 70.241  98.142  1.00 17.19 ? 559  LEU   A CD1   1 
ATOM   4105  C  CD2   . LEU   A  1  561  ? -44.613 71.103  99.848  1.00 19.45 ? 559  LEU   A CD2   1 
ATOM   4106  N  N     . ALA   A  1  562  ? -48.684 69.910  103.147 1.00 19.35 ? 560  ALA   A N     1 
ATOM   4107  C  CA    . ALA   A  1  562  ? -49.758 70.403  103.999 1.00 21.71 ? 560  ALA   A CA    1 
ATOM   4108  C  C     . ALA   A  1  562  ? -49.288 70.529  105.438 1.00 21.28 ? 560  ALA   A C     1 
ATOM   4109  O  O     . ALA   A  1  562  ? -49.585 71.523  106.111 1.00 22.30 ? 560  ALA   A O     1 
ATOM   4110  C  CB    . ALA   A  1  562  ? -50.978 69.487  103.907 1.00 24.12 ? 560  ALA   A CB    1 
ATOM   4111  N  N     . SER   A  1  563  ? -48.546 69.535  105.925 1.00 20.49 ? 561  SER   A N     1 
ATOM   4112  C  CA    A SER   A  1  563  ? -48.034 69.595  107.288 0.48 22.33 ? 561  SER   A CA    1 
ATOM   4113  C  CA    B SER   A  1  563  ? -48.056 69.615  107.293 0.52 22.31 ? 561  SER   A CA    1 
ATOM   4114  C  C     . SER   A  1  563  ? -47.003 70.705  107.428 1.00 21.87 ? 561  SER   A C     1 
ATOM   4115  O  O     . SER   A  1  563  ? -46.993 71.439  108.421 1.00 24.28 ? 561  SER   A O     1 
ATOM   4116  C  CB    A SER   A  1  563  ? -47.425 68.243  107.655 0.48 24.31 ? 561  SER   A CB    1 
ATOM   4117  C  CB    B SER   A  1  563  ? -47.519 68.260  107.748 0.52 24.41 ? 561  SER   A CB    1 
ATOM   4118  O  OG    A SER   A  1  563  ? -46.821 68.282  108.933 0.48 26.28 ? 561  SER   A OG    1 
ATOM   4119  O  OG    B SER   A  1  563  ? -46.351 67.908  107.038 0.52 27.94 ? 561  SER   A OG    1 
ATOM   4120  N  N     . LEU   A  1  564  ? -46.127 70.841  106.431 1.00 22.01 ? 562  LEU   A N     1 
ATOM   4121  C  CA    . LEU   A  1  564  ? -45.116 71.887  106.474 1.00 22.72 ? 562  LEU   A CA    1 
ATOM   4122  C  C     . LEU   A  1  564  ? -45.754 73.269  106.446 1.00 21.04 ? 562  LEU   A C     1 
ATOM   4123  O  O     . LEU   A  1  564  ? -45.338 74.163  107.192 1.00 22.77 ? 562  LEU   A O     1 
ATOM   4124  C  CB    . LEU   A  1  564  ? -44.148 71.708  105.308 1.00 22.24 ? 562  LEU   A CB    1 
ATOM   4125  C  CG    . LEU   A  1  564  ? -42.813 72.427  105.362 1.00 27.43 ? 562  LEU   A CG    1 
ATOM   4126  C  CD1   . LEU   A  1  564  ? -42.082 72.032  106.628 1.00 23.92 ? 562  LEU   A CD1   1 
ATOM   4127  C  CD2   . LEU   A  1  564  ? -41.997 72.062  104.135 1.00 24.45 ? 562  LEU   A CD2   1 
ATOM   4128  N  N     . THR   A  1  565  ? -46.785 73.460  105.614 1.00 21.20 ? 563  THR   A N     1 
ATOM   4129  C  CA    . THR   A  1  565  ? -47.476 74.743  105.588 1.00 22.28 ? 563  THR   A CA    1 
ATOM   4130  C  C     . THR   A  1  565  ? -47.887 75.164  106.993 1.00 21.01 ? 563  THR   A C     1 
ATOM   4131  O  O     . THR   A  1  565  ? -47.649 76.301  107.413 1.00 23.12 ? 563  THR   A O     1 
ATOM   4132  C  CB    . THR   A  1  565  ? -48.709 74.667  104.689 1.00 21.93 ? 563  THR   A CB    1 
ATOM   4133  O  OG1   . THR   A  1  565  ? -48.307 74.423  103.337 1.00 23.40 ? 563  THR   A OG1   1 
ATOM   4134  C  CG2   . THR   A  1  565  ? -49.488 75.978  104.758 1.00 24.21 ? 563  THR   A CG2   1 
ATOM   4135  N  N     . GLU   A  1  566  ? -48.495 74.242  107.742 1.00 24.18 ? 564  GLU   A N     1 
ATOM   4136  C  CA    . GLU   A  1  566  ? -48.950 74.572  109.087 1.00 23.53 ? 564  GLU   A CA    1 
ATOM   4137  C  C     . GLU   A  1  566  ? -47.778 74.838  110.018 1.00 22.99 ? 564  GLU   A C     1 
ATOM   4138  O  O     . GLU   A  1  566  ? -47.795 75.807  110.783 1.00 25.46 ? 564  GLU   A O     1 
ATOM   4139  C  CB    . GLU   A  1  566  ? -49.840 73.452  109.621 1.00 26.81 ? 564  GLU   A CB    1 
ATOM   4140  C  CG    . GLU   A  1  566  ? -51.090 73.238  108.779 1.00 34.86 ? 564  GLU   A CG    1 
ATOM   4141  C  CD    . GLU   A  1  566  ? -51.858 74.532  108.537 1.00 38.27 ? 564  GLU   A CD    1 
ATOM   4142  O  OE1   . GLU   A  1  566  ? -52.090 75.283  109.511 1.00 42.36 ? 564  GLU   A OE1   1 
ATOM   4143  O  OE2   . GLU   A  1  566  ? -52.217 74.804  107.367 1.00 39.42 ? 564  GLU   A OE2   1 
ATOM   4144  N  N     . ALA   A  1  567  ? -46.742 74.002  109.955 1.00 21.91 ? 565  ALA   A N     1 
ATOM   4145  C  CA    . ALA   A  1  567  ? -45.589 74.215  110.823 1.00 24.59 ? 565  ALA   A CA    1 
ATOM   4146  C  C     . ALA   A  1  567  ? -44.885 75.524  110.485 1.00 21.00 ? 565  ALA   A C     1 
ATOM   4147  O  O     . ALA   A  1  567  ? -44.408 76.232  111.383 1.00 23.05 ? 565  ALA   A O     1 
ATOM   4148  C  CB    . ALA   A  1  567  ? -44.629 73.034  110.708 1.00 25.42 ? 565  ALA   A CB    1 
ATOM   4149  N  N     . LEU   A  1  568  ? -44.829 75.870  109.199 1.00 22.36 ? 566  LEU   A N     1 
ATOM   4150  C  CA    . LEU   A  1  568  ? -44.185 77.113  108.795 1.00 19.58 ? 566  LEU   A CA    1 
ATOM   4151  C  C     . LEU   A  1  568  ? -44.981 78.316  109.268 1.00 21.32 ? 566  LEU   A C     1 
ATOM   4152  O  O     . LEU   A  1  568  ? -44.417 79.271  109.814 1.00 23.32 ? 566  LEU   A O     1 
ATOM   4153  C  CB    . LEU   A  1  568  ? -44.006 77.145  107.277 1.00 19.69 ? 566  LEU   A CB    1 
ATOM   4154  C  CG    . LEU   A  1  568  ? -43.053 76.083  106.738 1.00 19.20 ? 566  LEU   A CG    1 
ATOM   4155  C  CD1   . LEU   A  1  568  ? -43.108 76.091  105.232 1.00 20.80 ? 566  LEU   A CD1   1 
ATOM   4156  C  CD2   . LEU   A  1  568  ? -41.632 76.305  107.212 1.00 22.62 ? 566  LEU   A CD2   1 
ATOM   4157  N  N     . ARG   A  1  569  ? -46.303 78.284  109.076 1.00 21.66 ? 567  ARG   A N     1 
ATOM   4158  C  CA    . ARG   A  1  569  ? -47.149 79.335  109.629 1.00 23.68 ? 567  ARG   A CA    1 
ATOM   4159  C  C     . ARG   A  1  569  ? -46.973 79.437  111.135 1.00 22.72 ? 567  ARG   A C     1 
ATOM   4160  O  O     . ARG   A  1  569  ? -46.832 80.541  111.677 1.00 26.30 ? 567  ARG   A O     1 
ATOM   4161  C  CB    . ARG   A  1  569  ? -48.609 79.070  109.277 1.00 24.39 ? 567  ARG   A CB    1 
ATOM   4162  C  CG    . ARG   A  1  569  ? -48.918 79.273  107.805 1.00 28.92 ? 567  ARG   A CG    1 
ATOM   4163  C  CD    . ARG   A  1  569  ? -50.378 78.966  107.502 1.00 30.40 ? 567  ARG   A CD    1 
ATOM   4164  N  NE    . ARG   A  1  569  ? -50.647 78.947  106.069 1.00 33.32 ? 567  ARG   A NE    1 
ATOM   4165  C  CZ    . ARG   A  1  569  ? -51.784 78.525  105.534 1.00 43.60 ? 567  ARG   A CZ    1 
ATOM   4166  N  NH1   . ARG   A  1  569  ? -52.769 78.058  106.286 1.00 42.80 ? 567  ARG   A NH1   1 
ATOM   4167  N  NH2   . ARG   A  1  569  ? -51.937 78.570  104.212 1.00 45.84 ? 567  ARG   A NH2   1 
ATOM   4168  N  N     . GLU   A  1  570  ? -46.950 78.294  111.825 1.00 23.06 ? 568  GLU   A N     1 
ATOM   4169  C  CA    . GLU   A  1  570  ? -46.780 78.317  113.274 1.00 23.65 ? 568  GLU   A CA    1 
ATOM   4170  C  C     . GLU   A  1  570  ? -45.434 78.911  113.658 1.00 28.16 ? 568  GLU   A C     1 
ATOM   4171  O  O     . GLU   A  1  570  ? -45.328 79.634  114.657 1.00 29.78 ? 568  GLU   A O     1 
ATOM   4172  C  CB    . GLU   A  1  570  ? -46.950 76.910  113.846 1.00 28.36 ? 568  GLU   A CB    1 
ATOM   4173  C  CG    . GLU   A  1  570  ? -48.392 76.413  113.807 1.00 31.08 ? 568  GLU   A CG    1 
ATOM   4174  C  CD    . GLU   A  1  570  ? -48.516 74.929  114.100 1.00 41.28 ? 568  GLU   A CD    1 
ATOM   4175  O  OE1   . GLU   A  1  570  ? -47.505 74.207  113.970 1.00 49.46 ? 568  GLU   A OE1   1 
ATOM   4176  O  OE2   . GLU   A  1  570  ? -49.628 74.485  114.461 1.00 53.93 ? 568  GLU   A OE2   1 
ATOM   4177  N  N     . SER   A  1  571  ? -44.396 78.637  112.865 1.00 23.68 ? 569  SER   A N     1 
ATOM   4178  C  CA    . SER   A  1  571  ? -43.084 79.195  113.171 1.00 24.52 ? 569  SER   A CA    1 
ATOM   4179  C  C     . SER   A  1  571  ? -43.080 80.710  113.035 1.00 26.48 ? 569  SER   A C     1 
ATOM   4180  O  O     . SER   A  1  571  ? -42.350 81.392  113.762 1.00 27.24 ? 569  SER   A O     1 
ATOM   4181  C  CB    . SER   A  1  571  ? -42.023 78.589  112.258 1.00 23.43 ? 569  SER   A CB    1 
ATOM   4182  O  OG    . SER   A  1  571  ? -42.065 79.179  110.967 1.00 24.15 ? 569  SER   A OG    1 
ATOM   4183  N  N     . ALA   A  1  572  ? -43.886 81.254  112.126 1.00 26.92 ? 570  ALA   A N     1 
ATOM   4184  C  CA    . ALA   A  1  572  ? -43.941 82.698  111.949 1.00 28.58 ? 570  ALA   A CA    1 
ATOM   4185  C  C     . ALA   A  1  572  ? -44.709 83.396  113.060 1.00 32.23 ? 570  ALA   A C     1 
ATOM   4186  O  O     . ALA   A  1  572  ? -44.598 84.617  113.194 1.00 34.29 ? 570  ALA   A O     1 
ATOM   4187  C  CB    . ALA   A  1  572  ? -44.544 83.054  110.591 1.00 29.92 ? 570  ALA   A CB    1 
ATOM   4188  N  N     . ALA   A  1  573  ? -45.475 82.654  113.852 1.00 29.07 ? 571  ALA   A N     1 
ATOM   4189  C  CA    . ALA   A  1  573  ? -46.183 83.198  115.003 1.00 32.59 ? 571  ALA   A CA    1 
ATOM   4190  C  C     . ALA   A  1  573  ? -45.355 83.124  116.279 1.00 37.25 ? 571  ALA   A C     1 
ATOM   4191  O  O     . ALA   A  1  573  ? -45.848 83.494  117.350 1.00 40.28 ? 571  ALA   A O     1 
ATOM   4192  C  CB    . ALA   A  1  573  ? -47.515 82.466  115.200 1.00 33.09 ? 571  ALA   A CB    1 
ATOM   4193  N  N     . MET   A  1  574  ? -44.115 82.660  116.193 1.00 32.03 ? 572  MET   A N     1 
ATOM   4194  C  CA    . MET   A  1  574  ? -43.263 82.550  117.366 1.00 33.07 ? 572  MET   A CA    1 
ATOM   4195  C  C     . MET   A  1  574  ? -42.507 83.852  117.592 1.00 34.70 ? 572  MET   A C     1 
ATOM   4196  O  O     . MET   A  1  574  ? -42.194 84.585  116.650 1.00 30.46 ? 572  MET   A O     1 
ATOM   4197  C  CB    . MET   A  1  574  ? -42.302 81.373  117.220 1.00 36.69 ? 572  MET   A CB    1 
ATOM   4198  C  CG    . MET   A  1  574  ? -43.011 80.031  117.283 1.00 36.73 ? 572  MET   A CG    1 
ATOM   4199  S  SD    . MET   A  1  574  ? -41.954 78.637  116.897 1.00 35.76 ? 572  MET   A SD    1 
ATOM   4200  C  CE    . MET   A  1  574  ? -43.098 77.267  117.085 1.00 43.72 ? 572  MET   A CE    1 
ATOM   4201  N  N     . LYS   A  1  575  ? -42.249 84.148  118.867 1.00 33.35 ? 573  LYS   A N     1 
ATOM   4202  C  CA    . LYS   A  1  575  ? -41.548 85.370  119.264 1.00 35.77 ? 573  LYS   A CA    1 
ATOM   4203  C  C     . LYS   A  1  575  ? -40.051 85.081  119.378 1.00 34.27 ? 573  LYS   A C     1 
ATOM   4204  O  O     . LYS   A  1  575  ? -39.469 85.006  120.462 1.00 33.32 ? 573  LYS   A O     1 
ATOM   4205  C  CB    . LYS   A  1  575  ? -42.124 85.918  120.565 1.00 38.12 ? 573  LYS   A CB    1 
ATOM   4206  N  N     . TRP   A  1  576  ? -39.434 84.924  118.210 1.00 30.24 ? 574  TRP   A N     1 
ATOM   4207  C  CA    . TRP   A  1  576  ? -38.021 84.574  118.125 1.00 27.94 ? 574  TRP   A CA    1 
ATOM   4208  C  C     . TRP   A  1  576  ? -37.163 85.696  118.684 1.00 25.27 ? 574  TRP   A C     1 
ATOM   4209  O  O     . TRP   A  1  576  ? -37.328 86.864  118.319 1.00 27.06 ? 574  TRP   A O     1 
ATOM   4210  C  CB    . TRP   A  1  576  ? -37.634 84.348  116.669 1.00 26.01 ? 574  TRP   A CB    1 
ATOM   4211  C  CG    . TRP   A  1  576  ? -38.319 83.195  116.023 1.00 24.55 ? 574  TRP   A CG    1 
ATOM   4212  C  CD1   . TRP   A  1  576  ? -39.306 83.249  115.079 1.00 24.85 ? 574  TRP   A CD1   1 
ATOM   4213  C  CD2   . TRP   A  1  576  ? -38.084 81.811  116.280 1.00 24.46 ? 574  TRP   A CD2   1 
ATOM   4214  N  NE1   . TRP   A  1  576  ? -39.689 81.982  114.726 1.00 25.59 ? 574  TRP   A NE1   1 
ATOM   4215  C  CE2   . TRP   A  1  576  ? -38.949 81.079  115.445 1.00 25.14 ? 574  TRP   A CE2   1 
ATOM   4216  C  CE3   . TRP   A  1  576  ? -37.215 81.117  117.131 1.00 23.61 ? 574  TRP   A CE3   1 
ATOM   4217  C  CZ2   . TRP   A  1  576  ? -38.974 79.685  115.431 1.00 24.37 ? 574  TRP   A CZ2   1 
ATOM   4218  C  CZ3   . TRP   A  1  576  ? -37.236 79.736  117.116 1.00 24.72 ? 574  TRP   A CZ3   1 
ATOM   4219  C  CH2   . TRP   A  1  576  ? -38.114 79.032  116.274 1.00 28.25 ? 574  TRP   A CH2   1 
ATOM   4220  N  N     . THR   A  1  577  ? -36.241 85.343  119.574 1.00 26.15 ? 575  THR   A N     1 
ATOM   4221  C  CA    . THR   A  1  577  ? -35.301 86.315  120.101 1.00 24.73 ? 575  THR   A CA    1 
ATOM   4222  C  C     . THR   A  1  577  ? -33.903 85.724  120.110 1.00 26.99 ? 575  THR   A C     1 
ATOM   4223  O  O     . THR   A  1  577  ? -33.707 84.505  120.074 1.00 27.43 ? 575  THR   A O     1 
ATOM   4224  C  CB    . THR   A  1  577  ? -35.642 86.755  121.531 1.00 26.70 ? 575  THR   A CB    1 
ATOM   4225  O  OG1   . THR   A  1  577  ? -35.555 85.622  122.401 1.00 30.59 ? 575  THR   A OG1   1 
ATOM   4226  C  CG2   . THR   A  1  577  ? -37.037 87.350  121.589 1.00 31.29 ? 575  THR   A CG2   1 
ATOM   4227  N  N     . ALA   A  1  578  ? -32.923 86.617  120.162 1.00 27.75 ? 576  ALA   A N     1 
ATOM   4228  C  CA    . ALA   A  1  578  ? -31.536 86.249  120.383 1.00 23.77 ? 576  ALA   A CA    1 
ATOM   4229  C  C     . ALA   A  1  578  ? -30.988 87.232  121.396 1.00 26.45 ? 576  ALA   A C     1 
ATOM   4230  O  O     . ALA   A  1  578  ? -31.120 88.445  121.212 1.00 27.31 ? 576  ALA   A O     1 
ATOM   4231  C  CB    . ALA   A  1  578  ? -30.722 86.345  119.089 1.00 25.85 ? 576  ALA   A CB    1 
ATOM   4232  N  N     . LEU   A  1  579  ? -30.394 86.712  122.460 1.00 25.83 ? 577  LEU   A N     1 
ATOM   4233  C  CA    . LEU   A  1  579  ? -29.904 87.507  123.574 1.00 26.83 ? 577  LEU   A CA    1 
ATOM   4234  C  C     . LEU   A  1  579  ? -28.473 87.097  123.858 1.00 28.63 ? 577  LEU   A C     1 
ATOM   4235  O  O     . LEU   A  1  579  ? -28.062 85.981  123.524 1.00 26.72 ? 577  LEU   A O     1 
ATOM   4236  C  CB    . LEU   A  1  579  ? -30.740 87.252  124.838 1.00 28.62 ? 577  LEU   A CB    1 
ATOM   4237  C  CG    . LEU   A  1  579  ? -32.261 87.270  124.725 1.00 32.99 ? 577  LEU   A CG    1 
ATOM   4238  C  CD1   . LEU   A  1  579  ? -32.873 86.922  126.072 1.00 34.52 ? 577  LEU   A CD1   1 
ATOM   4239  C  CD2   . LEU   A  1  579  ? -32.745 88.627  124.245 1.00 36.14 ? 577  LEU   A CD2   1 
ATOM   4240  N  N     . PRO   A  1  580  ? -27.686 87.977  124.481 1.00 28.68 ? 578  PRO   A N     1 
ATOM   4241  C  CA    . PRO   A  1  580  ? -26.371 87.557  124.968 1.00 26.58 ? 578  PRO   A CA    1 
ATOM   4242  C  C     . PRO   A  1  580  ? -26.572 86.567  126.097 1.00 32.27 ? 578  PRO   A C     1 
ATOM   4243  O  O     . PRO   A  1  580  ? -26.990 86.943  127.195 1.00 33.90 ? 578  PRO   A O     1 
ATOM   4244  C  CB    . PRO   A  1  580  ? -25.741 88.863  125.471 1.00 31.17 ? 578  PRO   A CB    1 
ATOM   4245  C  CG    . PRO   A  1  580  ? -26.602 89.967  124.915 1.00 30.64 ? 578  PRO   A CG    1 
ATOM   4246  C  CD    . PRO   A  1  580  ? -27.969 89.379  124.826 1.00 29.38 ? 578  PRO   A CD    1 
ATOM   4247  N  N     . GLN   A  1  581  ? -26.325 85.292  125.816 1.00 27.27 ? 579  GLN   A N     1 
ATOM   4248  C  CA    . GLN   A  1  581  ? -26.546 84.216  126.774 1.00 28.35 ? 579  GLN   A CA    1 
ATOM   4249  C  C     . GLN   A  1  581  ? -25.204 83.893  127.415 1.00 30.13 ? 579  GLN   A C     1 
ATOM   4250  O  O     . GLN   A  1  581  ? -24.486 82.984  127.005 1.00 29.79 ? 579  GLN   A O     1 
ATOM   4251  C  CB    . GLN   A  1  581  ? -27.139 82.997  126.073 1.00 27.51 ? 579  GLN   A CB    1 
ATOM   4252  C  CG    . GLN   A  1  581  ? -28.515 83.223  125.467 1.00 25.81 ? 579  GLN   A CG    1 
ATOM   4253  C  CD    . GLN   A  1  581  ? -29.603 83.359  126.520 1.00 30.36 ? 579  GLN   A CD    1 
ATOM   4254  O  OE1   . GLN   A  1  581  ? -29.356 83.191  127.717 1.00 31.19 ? 579  GLN   A OE1   1 
ATOM   4255  N  NE2   . GLN   A  1  581  ? -30.821 83.668  126.076 1.00 29.95 ? 579  GLN   A NE2   1 
ATOM   4256  N  N     . LEU   A  1  582  ? -24.868 84.677  128.436 1.00 28.36 ? 580  LEU   A N     1 
ATOM   4257  C  CA    . LEU   A  1  582  ? -23.656 84.456  129.198 1.00 29.44 ? 580  LEU   A CA    1 
ATOM   4258  C  C     . LEU   A  1  582  ? -23.836 83.253  130.120 1.00 29.06 ? 580  LEU   A C     1 
ATOM   4259  O  O     . LEU   A  1  582  ? -24.949 82.762  130.339 1.00 32.67 ? 580  LEU   A O     1 
ATOM   4260  C  CB    . LEU   A  1  582  ? -23.295 85.710  129.992 1.00 29.53 ? 580  LEU   A CB    1 
ATOM   4261  C  CG    . LEU   A  1  582  ? -22.418 86.744  129.272 1.00 36.77 ? 580  LEU   A CG    1 
ATOM   4262  C  CD1   . LEU   A  1  582  ? -23.069 87.269  128.006 1.00 34.79 ? 580  LEU   A CD1   1 
ATOM   4263  C  CD2   . LEU   A  1  582  ? -22.095 87.895  130.203 1.00 41.85 ? 580  LEU   A CD2   1 
ATOM   4264  N  N     . ALA   A  1  583  ? -22.714 82.765  130.656 1.00 30.11 ? 581  ALA   A N     1 
ATOM   4265  C  CA    . ALA   A  1  583  ? -22.782 81.652  131.593 1.00 31.56 ? 581  ALA   A CA    1 
ATOM   4266  C  C     . ALA   A  1  583  ? -23.682 81.985  132.772 1.00 31.80 ? 581  ALA   A C     1 
ATOM   4267  O  O     . ALA   A  1  583  ? -24.330 81.094  133.330 1.00 40.56 ? 581  ALA   A O     1 
ATOM   4268  C  CB    . ALA   A  1  583  ? -21.381 81.289  132.085 1.00 31.18 ? 581  ALA   A CB    1 
ATOM   4269  N  N     . THR   A  1  584  ? -23.747 83.264  133.142 1.00 33.77 ? 582  THR   A N     1 
ATOM   4270  C  CA    . THR   A  1  584  ? -24.521 83.732  134.284 1.00 37.93 ? 582  THR   A CA    1 
ATOM   4271  C  C     . THR   A  1  584  ? -25.980 83.993  133.947 1.00 38.40 ? 582  THR   A C     1 
ATOM   4272  O  O     . THR   A  1  584  ? -26.769 84.256  134.861 1.00 42.02 ? 582  THR   A O     1 
ATOM   4273  C  CB    . THR   A  1  584  ? -23.910 85.029  134.825 1.00 42.41 ? 582  THR   A CB    1 
ATOM   4274  O  OG1   . THR   A  1  584  ? -23.810 85.988  133.763 1.00 41.29 ? 582  THR   A OG1   1 
ATOM   4275  C  CG2   . THR   A  1  584  ? -22.530 84.774  135.413 1.00 37.23 ? 582  THR   A CG2   1 
ATOM   4276  N  N     . GLY   A  1  585  ? -26.352 83.949  132.670 1.00 35.40 ? 583  GLY   A N     1 
ATOM   4277  C  CA    . GLY   A  1  585  ? -27.709 84.219  132.262 1.00 36.30 ? 583  GLY   A CA    1 
ATOM   4278  C  C     . GLY   A  1  585  ? -27.781 85.281  131.183 1.00 37.16 ? 583  GLY   A C     1 
ATOM   4279  O  O     . GLY   A  1  585  ? -26.778 85.915  130.836 1.00 37.30 ? 583  GLY   A O     1 
ATOM   4280  N  N     . PRO   A  1  586  ? -28.979 85.499  130.638 1.00 34.95 ? 584  PRO   A N     1 
ATOM   4281  C  CA    . PRO   A  1  586  ? -29.141 86.518  129.594 1.00 34.09 ? 584  PRO   A CA    1 
ATOM   4282  C  C     . PRO   A  1  586  ? -28.690 87.881  130.092 1.00 40.82 ? 584  PRO   A C     1 
ATOM   4283  O  O     . PRO   A  1  586  ? -28.960 88.266  131.231 1.00 37.77 ? 584  PRO   A O     1 
ATOM   4284  C  CB    . PRO   A  1  586  ? -30.648 86.507  129.312 1.00 42.48 ? 584  PRO   A CB    1 
ATOM   4285  C  CG    . PRO   A  1  586  ? -31.191 85.288  129.999 1.00 42.55 ? 584  PRO   A CG    1 
ATOM   4286  C  CD    . PRO   A  1  586  ? -30.269 84.975  131.116 1.00 37.58 ? 584  PRO   A CD    1 
ATOM   4287  N  N     . ALA   A  1  587  ? -27.984 88.604  129.231 1.00 35.18 ? 585  ALA   A N     1 
ATOM   4288  C  CA    . ALA   A  1  587  ? -27.467 89.925  129.546 1.00 38.00 ? 585  ALA   A CA    1 
ATOM   4289  C  C     . ALA   A  1  587  ? -28.276 90.987  128.815 1.00 38.67 ? 585  ALA   A C     1 
ATOM   4290  O  O     . ALA   A  1  587  ? -28.870 90.728  127.765 1.00 37.14 ? 585  ALA   A O     1 
ATOM   4291  C  CB    . ALA   A  1  587  ? -25.991 90.044  129.156 1.00 39.64 ? 585  ALA   A CB    1 
ATOM   4292  N  N     . ALA   A  1  588  ? -28.310 92.183  129.391 1.00 38.47 ? 586  ALA   A N     1 
ATOM   4293  C  CA    . ALA   A  1  588  ? -28.963 93.303  128.742 1.00 35.43 ? 586  ALA   A CA    1 
ATOM   4294  C  C     . ALA   A  1  588  ? -28.070 93.865  127.641 1.00 34.96 ? 586  ALA   A C     1 
ATOM   4295  O  O     . ALA   A  1  588  ? -26.854 93.656  127.619 1.00 39.64 ? 586  ALA   A O     1 
ATOM   4296  C  CB    . ALA   A  1  588  ? -29.257 94.407  129.755 1.00 36.03 ? 586  ALA   A CB    1 
ATOM   4297  N  N     . GLY   A  1  589  ? -28.690 94.598  126.727 1.00 36.31 ? 587  GLY   A N     1 
ATOM   4298  C  CA    . GLY   A  1  589  ? -27.934 95.230  125.666 1.00 33.80 ? 587  GLY   A CA    1 
ATOM   4299  C  C     . GLY   A  1  589  ? -28.859 95.948  124.715 1.00 36.05 ? 587  GLY   A C     1 
ATOM   4300  O  O     . GLY   A  1  589  ? -30.066 96.048  124.948 1.00 38.97 ? 587  GLY   A O     1 
ATOM   4301  N  N     . GLU   A  1  590  ? -28.269 96.460  123.638 1.00 37.77 ? 588  GLU   A N     1 
ATOM   4302  C  CA    . GLU   A  1  590  ? -29.044 97.139  122.609 1.00 35.16 ? 588  GLU   A CA    1 
ATOM   4303  C  C     . GLU   A  1  590  ? -29.893 96.127  121.851 1.00 31.43 ? 588  GLU   A C     1 
ATOM   4304  O  O     . GLU   A  1  590  ? -29.380 95.130  121.331 1.00 33.60 ? 588  GLU   A O     1 
ATOM   4305  C  CB    . GLU   A  1  590  ? -28.107 97.860  121.641 1.00 41.97 ? 588  GLU   A CB    1 
ATOM   4306  N  N     . THR   A  1  591  ? -31.192 96.393  121.780 1.00 33.09 ? 589  THR   A N     1 
ATOM   4307  C  CA    . THR   A  1  591  ? -32.154 95.490  121.168 1.00 31.74 ? 589  THR   A CA    1 
ATOM   4308  C  C     . THR   A  1  591  ? -32.719 96.109  119.897 1.00 32.46 ? 589  THR   A C     1 
ATOM   4309  O  O     . THR   A  1  591  ? -33.049 97.298  119.864 1.00 36.40 ? 589  THR   A O     1 
ATOM   4310  C  CB    . THR   A  1  591  ? -33.286 95.191  122.156 1.00 35.99 ? 589  THR   A CB    1 
ATOM   4311  O  OG1   . THR   A  1  591  ? -32.759 94.484  123.289 1.00 36.40 ? 589  THR   A OG1   1 
ATOM   4312  C  CG2   . THR   A  1  591  ? -34.369 94.364  121.502 1.00 35.81 ? 589  THR   A CG2   1 
ATOM   4313  N  N     . ARG   A  1  592  ? -32.818 95.298  118.845 1.00 29.33 ? 590  ARG   A N     1 
ATOM   4314  C  CA    . ARG   A  1  592  ? -33.410 95.748  117.596 1.00 33.06 ? 590  ARG   A CA    1 
ATOM   4315  C  C     . ARG   A  1  592  ? -34.146 94.582  116.956 1.00 29.45 ? 590  ARG   A C     1 
ATOM   4316  O  O     . ARG   A  1  592  ? -33.904 93.416  117.283 1.00 30.38 ? 590  ARG   A O     1 
ATOM   4317  C  CB    . ARG   A  1  592  ? -32.356 96.293  116.625 1.00 35.07 ? 590  ARG   A CB    1 
ATOM   4318  C  CG    . ARG   A  1  592  ? -31.369 95.251  116.136 1.00 37.25 ? 590  ARG   A CG    1 
ATOM   4319  C  CD    . ARG   A  1  592  ? -30.607 95.737  114.912 1.00 39.92 ? 590  ARG   A CD    1 
ATOM   4320  N  NE    . ARG   A  1  592  ? -29.562 94.797  114.529 1.00 37.40 ? 590  ARG   A NE    1 
ATOM   4321  C  CZ    . ARG   A  1  592  ? -29.771 93.693  113.826 1.00 37.57 ? 590  ARG   A CZ    1 
ATOM   4322  N  NH1   . ARG   A  1  592  ? -30.977 93.371  113.387 1.00 37.03 ? 590  ARG   A NH1   1 
ATOM   4323  N  NH2   . ARG   A  1  592  ? -28.745 92.888  113.562 1.00 39.20 ? 590  ARG   A NH2   1 
ATOM   4324  N  N     . THR   A  1  593  ? -35.047 94.910  116.034 1.00 30.15 ? 591  THR   A N     1 
ATOM   4325  C  CA    . THR   A  1  593  ? -35.775 93.880  115.317 1.00 29.63 ? 591  THR   A CA    1 
ATOM   4326  C  C     . THR   A  1  593  ? -34.903 93.252  114.234 1.00 31.67 ? 591  THR   A C     1 
ATOM   4327  O  O     . THR   A  1  593  ? -33.943 93.847  113.734 1.00 31.61 ? 591  THR   A O     1 
ATOM   4328  C  CB    . THR   A  1  593  ? -37.020 94.464  114.659 1.00 32.44 ? 591  THR   A CB    1 
ATOM   4329  O  OG1   . THR   A  1  593  ? -36.635 95.568  113.831 1.00 34.37 ? 591  THR   A OG1   1 
ATOM   4330  C  CG2   . THR   A  1  593  ? -37.999 94.936  115.714 1.00 34.55 ? 591  THR   A CG2   1 
ATOM   4331  N  N     . VAL   A  1  594  ? -35.261 92.026  113.878 1.00 24.89 ? 592  VAL   A N     1 
ATOM   4332  C  CA    . VAL   A  1  594  ? -34.672 91.304  112.760 1.00 26.69 ? 592  VAL   A CA    1 
ATOM   4333  C  C     . VAL   A  1  594  ? -35.748 91.234  111.686 1.00 26.48 ? 592  VAL   A C     1 
ATOM   4334  O  O     . VAL   A  1  594  ? -36.840 90.707  111.933 1.00 27.37 ? 592  VAL   A O     1 
ATOM   4335  C  CB    . VAL   A  1  594  ? -34.222 89.901  113.188 1.00 26.62 ? 592  VAL   A CB    1 
ATOM   4336  C  CG1   . VAL   A  1  594  ? -33.664 89.140  112.001 1.00 26.54 ? 592  VAL   A CG1   1 
ATOM   4337  C  CG2   . VAL   A  1  594  ? -33.171 89.990  114.302 1.00 27.98 ? 592  VAL   A CG2   1 
ATOM   4338  N  N     . LEU   A  1  595  ? -35.456 91.780  110.507 1.00 26.42 ? 593  LEU   A N     1 
ATOM   4339  C  CA    . LEU   A  1  595  ? -36.438 91.878  109.435 1.00 26.48 ? 593  LEU   A CA    1 
ATOM   4340  C  C     . LEU   A  1  595  ? -36.156 90.845  108.350 1.00 26.02 ? 593  LEU   A C     1 
ATOM   4341  O  O     . LEU   A  1  595  ? -35.005 90.522  108.064 1.00 25.77 ? 593  LEU   A O     1 
ATOM   4342  C  CB    . LEU   A  1  595  ? -36.425 93.281  108.819 1.00 27.24 ? 593  LEU   A CB    1 
ATOM   4343  C  CG    . LEU   A  1  595  ? -36.587 94.458  109.781 1.00 31.41 ? 593  LEU   A CG    1 
ATOM   4344  C  CD1   . LEU   A  1  595  ? -36.586 95.777  109.026 1.00 33.04 ? 593  LEU   A CD1   1 
ATOM   4345  C  CD2   . LEU   A  1  595  ? -37.862 94.307  110.585 1.00 30.63 ? 593  LEU   A CD2   1 
ATOM   4346  N  N     . ASN   A  1  596  ? -37.223 90.327  107.755 1.00 24.39 ? 594  ASN   A N     1 
ATOM   4347  C  CA    . ASN   A  1  596  ? -37.115 89.407  106.632 1.00 23.74 ? 594  ASN   A CA    1 
ATOM   4348  C  C     . ASN   A  1  596  ? -36.448 90.129  105.465 1.00 22.39 ? 594  ASN   A C     1 
ATOM   4349  O  O     . ASN   A  1  596  ? -36.967 91.153  105.001 1.00 22.70 ? 594  ASN   A O     1 
ATOM   4350  C  CB    . ASN   A  1  596  ? -38.544 88.993  106.263 1.00 22.67 ? 594  ASN   A CB    1 
ATOM   4351  C  CG    . ASN   A  1  596  ? -38.599 87.899  105.207 1.00 23.57 ? 594  ASN   A CG    1 
ATOM   4352  O  OD1   . ASN   A  1  596  ? -37.750 87.823  104.326 1.00 22.36 ? 594  ASN   A OD1   1 
ATOM   4353  N  ND2   . ASN   A  1  596  ? -39.619 87.053  105.290 1.00 24.34 ? 594  ASN   A ND2   1 
ATOM   4354  N  N     . PRO   A  1  597  ? -35.309 89.648  104.962 1.00 21.28 ? 595  PRO   A N     1 
ATOM   4355  C  CA    . PRO   A  1  597  ? -34.641 90.366  103.864 1.00 21.92 ? 595  PRO   A CA    1 
ATOM   4356  C  C     . PRO   A  1  597  ? -35.481 90.442  102.608 1.00 23.63 ? 595  PRO   A C     1 
ATOM   4357  O  O     . PRO   A  1  597  ? -35.249 91.323  101.768 1.00 21.40 ? 595  PRO   A O     1 
ATOM   4358  C  CB    . PRO   A  1  597  ? -33.358 89.553  103.625 1.00 21.70 ? 595  PRO   A CB    1 
ATOM   4359  C  CG    . PRO   A  1  597  ? -33.634 88.202  104.207 1.00 21.97 ? 595  PRO   A CG    1 
ATOM   4360  C  CD    . PRO   A  1  597  ? -34.573 88.438  105.367 1.00 20.16 ? 595  PRO   A CD    1 
ATOM   4361  N  N     . GLY   A  1  598  ? -36.449 89.546  102.458 1.00 20.95 ? 596  GLY   A N     1 
ATOM   4362  C  CA    . GLY   A  1  598  ? -37.341 89.560  101.324 1.00 20.15 ? 596  GLY   A CA    1 
ATOM   4363  C  C     . GLY   A  1  598  ? -38.537 90.464  101.472 1.00 22.43 ? 596  GLY   A C     1 
ATOM   4364  O  O     . GLY   A  1  598  ? -39.249 90.694  100.494 1.00 24.44 ? 596  GLY   A O     1 
ATOM   4365  N  N     . ASP   A  1  599  ? -38.761 90.996  102.671 1.00 21.39 ? 597  ASP   A N     1 
ATOM   4366  C  CA    . ASP   A  1  599  ? -39.879 91.899  102.918 1.00 22.03 ? 597  ASP   A CA    1 
ATOM   4367  C  C     . ASP   A  1  599  ? -39.663 92.500  104.293 1.00 22.32 ? 597  ASP   A C     1 
ATOM   4368  O  O     . ASP   A  1  599  ? -39.968 91.865  105.310 1.00 23.90 ? 597  ASP   A O     1 
ATOM   4369  C  CB    . ASP   A  1  599  ? -41.205 91.143  102.885 1.00 22.75 ? 597  ASP   A CB    1 
ATOM   4370  C  CG    . ASP   A  1  599  ? -42.405 92.056  102.953 1.00 24.37 ? 597  ASP   A CG    1 
ATOM   4371  O  OD1   . ASP   A  1  599  ? -42.263 93.210  103.401 1.00 26.74 ? 597  ASP   A OD1   1 
ATOM   4372  O  OD2   . ASP   A  1  599  ? -43.494 91.598  102.561 1.00 27.82 ? 597  ASP   A OD2   1 
ATOM   4373  N  N     . HIS   A  1  600  ? -39.138 93.721  104.330 1.00 23.22 ? 598  HIS   A N     1 
ATOM   4374  C  CA    . HIS   A  1  600  ? -38.786 94.338  105.603 1.00 26.68 ? 598  HIS   A CA    1 
ATOM   4375  C  C     . HIS   A  1  600  ? -39.992 94.595  106.498 1.00 27.14 ? 598  HIS   A C     1 
ATOM   4376  O  O     . HIS   A  1  600  ? -39.811 94.847  107.697 1.00 30.59 ? 598  HIS   A O     1 
ATOM   4377  C  CB    . HIS   A  1  600  ? -38.000 95.624  105.362 1.00 28.18 ? 598  HIS   A CB    1 
ATOM   4378  C  CG    . HIS   A  1  600  ? -36.608 95.384  104.871 1.00 29.53 ? 598  HIS   A CG    1 
ATOM   4379  N  ND1   . HIS   A  1  600  ? -35.746 96.405  104.532 1.00 34.39 ? 598  HIS   A ND1   1 
ATOM   4380  C  CD2   . HIS   A  1  600  ? -35.927 94.232  104.666 1.00 27.36 ? 598  HIS   A CD2   1 
ATOM   4381  C  CE1   . HIS   A  1  600  ? -34.595 95.892  104.135 1.00 33.47 ? 598  HIS   A CE1   1 
ATOM   4382  N  NE2   . HIS   A  1  600  ? -34.676 94.575  104.211 1.00 30.51 ? 598  HIS   A NE2   1 
ATOM   4383  N  N     . ARG   A  1  601  ? -41.205 94.531  105.953 1.00 27.58 ? 599  ARG   A N     1 
ATOM   4384  C  CA    . ARG   A  1  601  ? -42.405 94.632  106.772 1.00 28.29 ? 599  ARG   A CA    1 
ATOM   4385  C  C     . ARG   A  1  601  ? -42.610 93.402  107.640 1.00 30.68 ? 599  ARG   A C     1 
ATOM   4386  O  O     . ARG   A  1  601  ? -43.345 93.476  108.631 1.00 30.45 ? 599  ARG   A O     1 
ATOM   4387  C  CB    . ARG   A  1  601  ? -43.625 94.832  105.875 1.00 27.28 ? 599  ARG   A CB    1 
ATOM   4388  C  CG    . ARG   A  1  601  ? -43.511 96.024  104.956 1.00 26.13 ? 599  ARG   A CG    1 
ATOM   4389  C  CD    . ARG   A  1  601  ? -44.612 96.008  103.914 1.00 30.76 ? 599  ARG   A CD    1 
ATOM   4390  N  NE    . ARG   A  1  601  ? -44.601 94.778  103.131 1.00 29.05 ? 599  ARG   A NE    1 
ATOM   4391  C  CZ    . ARG   A  1  601  ? -45.471 94.499  102.171 1.00 31.50 ? 599  ARG   A CZ    1 
ATOM   4392  N  NH1   . ARG   A  1  601  ? -46.425 95.353  101.830 1.00 32.00 ? 599  ARG   A NH1   1 
ATOM   4393  N  NH2   . ARG   A  1  601  ? -45.387 93.332  101.540 1.00 29.37 ? 599  ARG   A NH2   1 
ATOM   4394  N  N     . ASP   A  1  602  ? -41.979 92.281  107.292 1.00 26.48 ? 600  ASP   A N     1 
ATOM   4395  C  CA    . ASP   A  1  602  ? -42.125 91.030  108.032 1.00 30.25 ? 600  ASP   A CA    1 
ATOM   4396  C  C     . ASP   A  1  602  ? -41.054 91.015  109.112 1.00 30.25 ? 600  ASP   A C     1 
ATOM   4397  O  O     . ASP   A  1  602  ? -39.889 90.722  108.840 1.00 28.94 ? 600  ASP   A O     1 
ATOM   4398  C  CB    . ASP   A  1  602  ? -41.978 89.833  107.097 1.00 27.82 ? 600  ASP   A CB    1 
ATOM   4399  C  CG    . ASP   A  1  602  ? -42.169 88.512  107.816 1.00 29.17 ? 600  ASP   A CG    1 
ATOM   4400  O  OD1   . ASP   A  1  602  ? -42.764 88.525  108.916 1.00 29.74 ? 600  ASP   A OD1   1 
ATOM   4401  O  OD2   . ASP   A  1  602  ? -41.710 87.469  107.296 1.00 27.91 ? 600  ASP   A OD2   1 
ATOM   4402  N  N     . VAL   A  1  603  ? -41.446 91.344  110.337 1.00 28.46 ? 601  VAL   A N     1 
ATOM   4403  C  CA    . VAL   A  1  603  ? -40.528 91.305  111.468 1.00 28.46 ? 601  VAL   A CA    1 
ATOM   4404  C  C     . VAL   A  1  603  ? -40.432 89.862  111.945 1.00 28.94 ? 601  VAL   A C     1 
ATOM   4405  O  O     . VAL   A  1  603  ? -41.438 89.250  112.317 1.00 31.78 ? 601  VAL   A O     1 
ATOM   4406  C  CB    . VAL   A  1  603  ? -40.998 92.236  112.595 1.00 31.20 ? 601  VAL   A CB    1 
ATOM   4407  C  CG1   . VAL   A  1  603  ? -40.054 92.148  113.782 1.00 30.87 ? 601  VAL   A CG1   1 
ATOM   4408  C  CG2   . VAL   A  1  603  ? -41.088 93.666  112.092 1.00 32.47 ? 601  VAL   A CG2   1 
ATOM   4409  N  N     . VAL   A  1  604  ? -39.225 89.317  111.925 1.00 24.83 ? 602  VAL   A N     1 
ATOM   4410  C  CA    . VAL   A  1  604  ? -39.009 87.915  112.263 1.00 26.07 ? 602  VAL   A CA    1 
ATOM   4411  C  C     . VAL   A  1  604  ? -38.749 87.742  113.747 1.00 25.20 ? 602  VAL   A C     1 
ATOM   4412  O  O     . VAL   A  1  604  ? -39.176 86.760  114.356 1.00 28.63 ? 602  VAL   A O     1 
ATOM   4413  C  CB    . VAL   A  1  604  ? -37.849 87.362  111.414 1.00 23.85 ? 602  VAL   A CB    1 
ATOM   4414  C  CG1   . VAL   A  1  604  ? -37.670 85.882  111.670 1.00 23.25 ? 602  VAL   A CG1   1 
ATOM   4415  C  CG2   . VAL   A  1  604  ? -38.109 87.625  109.937 1.00 24.32 ? 602  VAL   A CG2   1 
ATOM   4416  N  N     . GLY   A  1  605  ? -38.059 88.691  114.352 1.00 25.07 ? 603  GLY   A N     1 
ATOM   4417  C  CA    . GLY   A  1  605  ? -37.789 88.587  115.764 1.00 25.56 ? 603  GLY   A CA    1 
ATOM   4418  C  C     . GLY   A  1  605  ? -37.023 89.785  116.254 1.00 24.05 ? 603  GLY   A C     1 
ATOM   4419  O  O     . GLY   A  1  605  ? -37.012 90.839  115.620 1.00 29.21 ? 603  GLY   A O     1 
ATOM   4420  N  N     . SER   A  1  606  ? -36.376 89.603  117.397 1.00 24.81 ? 604  SER   A N     1 
ATOM   4421  C  CA    A SER   A  1  606  ? -35.631 90.673  118.032 0.58 26.12 ? 604  SER   A CA    1 
ATOM   4422  C  CA    B SER   A  1  606  ? -35.646 90.670  118.057 0.42 26.15 ? 604  SER   A CA    1 
ATOM   4423  C  C     . SER   A  1  606  ? -34.319 90.122  118.550 1.00 28.33 ? 604  SER   A C     1 
ATOM   4424  O  O     . SER   A  1  606  ? -34.262 89.005  119.072 1.00 28.54 ? 604  SER   A O     1 
ATOM   4425  C  CB    A SER   A  1  606  ? -36.422 91.292  119.184 0.58 27.59 ? 604  SER   A CB    1 
ATOM   4426  C  CB    B SER   A  1  606  ? -36.446 91.196  119.250 0.42 27.58 ? 604  SER   A CB    1 
ATOM   4427  O  OG    A SER   A  1  606  ? -37.546 91.984  118.681 0.58 29.89 ? 604  SER   A OG    1 
ATOM   4428  O  OG    B SER   A  1  606  ? -35.662 92.075  120.023 0.42 27.97 ? 604  SER   A OG    1 
ATOM   4429  N  N     . VAL   A  1  607  ? -33.261 90.904  118.385 1.00 25.82 ? 605  VAL   A N     1 
ATOM   4430  C  CA    . VAL   A  1  607  ? -31.940 90.524  118.856 1.00 24.60 ? 605  VAL   A CA    1 
ATOM   4431  C  C     . VAL   A  1  607  ? -31.464 91.567  119.852 1.00 25.56 ? 605  VAL   A C     1 
ATOM   4432  O  O     . VAL   A  1  607  ? -31.577 92.773  119.605 1.00 27.83 ? 605  VAL   A O     1 
ATOM   4433  C  CB    . VAL   A  1  607  ? -30.934 90.347  117.702 1.00 25.15 ? 605  VAL   A CB    1 
ATOM   4434  C  CG1   . VAL   A  1  607  ? -30.859 91.600  116.830 1.00 27.53 ? 605  VAL   A CG1   1 
ATOM   4435  C  CG2   . VAL   A  1  607  ? -29.569 90.006  118.259 1.00 25.97 ? 605  VAL   A CG2   1 
ATOM   4436  N  N     . THR   A  1  608  ? -30.955 91.099  120.981 1.00 26.55 ? 606  THR   A N     1 
ATOM   4437  C  CA    . THR   A  1  608  ? -30.247 91.941  121.927 1.00 28.34 ? 606  THR   A CA    1 
ATOM   4438  C  C     . THR   A  1  608  ? -28.765 91.679  121.719 1.00 27.66 ? 606  THR   A C     1 
ATOM   4439  O  O     . THR   A  1  608  ? -28.305 90.543  121.866 1.00 28.85 ? 606  THR   A O     1 
ATOM   4440  C  CB    . THR   A  1  608  ? -30.666 91.589  123.350 1.00 30.22 ? 606  THR   A CB    1 
ATOM   4441  O  OG1   . THR   A  1  608  ? -32.081 91.777  123.475 1.00 31.59 ? 606  THR   A OG1   1 
ATOM   4442  C  CG2   . THR   A  1  608  ? -29.948 92.479  124.349 1.00 31.97 ? 606  THR   A CG2   1 
ATOM   4443  N  N     . GLU   A  1  609  ? -28.028 92.718  121.353 1.00 29.58 ? 607  GLU   A N     1 
ATOM   4444  C  CA    . GLU   A  1  609  ? -26.625 92.540  121.022 1.00 30.72 ? 607  GLU   A CA    1 
ATOM   4445  C  C     . GLU   A  1  609  ? -25.725 92.699  122.247 1.00 29.92 ? 607  GLU   A C     1 
ATOM   4446  O  O     . GLU   A  1  609  ? -26.096 93.296  123.264 1.00 28.71 ? 607  GLU   A O     1 
ATOM   4447  C  CB    . GLU   A  1  609  ? -26.229 93.445  119.851 1.00 34.55 ? 607  GLU   A CB    1 
ATOM   4448  C  CG    . GLU   A  1  609  ? -26.995 93.043  118.583 1.00 37.65 ? 607  GLU   A CG    1 
ATOM   4449  C  CD    . GLU   A  1  609  ? -26.604 93.821  117.341 1.00 40.67 ? 607  GLU   A CD    1 
ATOM   4450  O  OE1   . GLU   A  1  609  ? -26.391 95.047  117.446 1.00 46.37 ? 607  GLU   A OE1   1 
ATOM   4451  O  OE2   . GLU   A  1  609  ? -26.524 93.196  116.252 1.00 39.67 ? 607  GLU   A OE2   1 
ATOM   4452  N  N     . THR   A  1  610  ? -24.538 92.116  122.143 1.00 30.35 ? 608  THR   A N     1 
ATOM   4453  C  CA    . THR   A  1  610  ? -23.625 91.982  123.265 1.00 29.02 ? 608  THR   A CA    1 
ATOM   4454  C  C     . THR   A  1  610  ? -22.744 93.217  123.342 1.00 32.48 ? 608  THR   A C     1 
ATOM   4455  O  O     . THR   A  1  610  ? -22.188 93.655  122.329 1.00 34.76 ? 608  THR   A O     1 
ATOM   4456  C  CB    . THR   A  1  610  ? -22.740 90.750  123.049 1.00 28.95 ? 608  THR   A CB    1 
ATOM   4457  O  OG1   . THR   A  1  610  ? -23.567 89.614  122.776 1.00 27.83 ? 608  THR   A OG1   1 
ATOM   4458  C  CG2   . THR   A  1  610  ? -21.891 90.473  124.282 1.00 28.36 ? 608  THR   A CG2   1 
ATOM   4459  N  N     . SER   A  1  611  ? -22.611 93.773  124.540 1.00 30.91 ? 609  SER   A N     1 
ATOM   4460  C  CA    . SER   A  1  611  ? -21.629 94.823  124.739 1.00 32.47 ? 609  SER   A CA    1 
ATOM   4461  C  C     . SER   A  1  611  ? -20.234 94.223  124.676 1.00 34.62 ? 609  SER   A C     1 
ATOM   4462  O  O     . SER   A  1  611  ? -20.030 93.035  124.943 1.00 32.43 ? 609  SER   A O     1 
ATOM   4463  C  CB    . SER   A  1  611  ? -21.834 95.487  126.099 1.00 33.62 ? 609  SER   A CB    1 
ATOM   4464  O  OG    . SER   A  1  611  ? -21.382 94.649  127.145 1.00 36.14 ? 609  SER   A OG    1 
ATOM   4465  N  N     . GLU   A  1  612  ? -19.263 95.049  124.290 1.00 35.07 ? 610  GLU   A N     1 
ATOM   4466  C  CA    . GLU   A  1  612  ? -17.890 94.563  124.270 1.00 36.56 ? 610  GLU   A CA    1 
ATOM   4467  C  C     . GLU   A  1  612  ? -17.413 94.197  125.670 1.00 36.80 ? 610  GLU   A C     1 
ATOM   4468  O  O     . GLU   A  1  612  ? -16.584 93.293  125.826 1.00 36.31 ? 610  GLU   A O     1 
ATOM   4469  C  CB    . GLU   A  1  612  ? -16.975 95.578  123.585 1.00 45.76 ? 610  GLU   A CB    1 
ATOM   4470  C  CG    . GLU   A  1  612  ? -17.273 95.722  122.094 1.00 46.87 ? 610  GLU   A CG    1 
ATOM   4471  C  CD    . GLU   A  1  612  ? -16.499 96.846  121.438 1.00 54.41 ? 610  GLU   A CD    1 
ATOM   4472  O  OE1   . GLU   A  1  612  ? -15.331 97.071  121.819 1.00 62.74 ? 610  GLU   A OE1   1 
ATOM   4473  O  OE2   . GLU   A  1  612  ? -17.066 97.509  120.543 1.00 50.68 ? 610  GLU   A OE2   1 
ATOM   4474  N  N     . GLU   A  1  613  ? -17.958 94.852  126.698 1.00 35.44 ? 611  GLU   A N     1 
ATOM   4475  C  CA    . GLU   A  1  613  ? -17.641 94.467  128.069 1.00 38.46 ? 611  GLU   A CA    1 
ATOM   4476  C  C     . GLU   A  1  613  ? -18.149 93.062  128.374 1.00 32.87 ? 611  GLU   A C     1 
ATOM   4477  O  O     . GLU   A  1  613  ? -17.426 92.243  128.952 1.00 31.50 ? 611  GLU   A O     1 
ATOM   4478  C  CB    . GLU   A  1  613  ? -18.223 95.486  129.053 1.00 39.12 ? 611  GLU   A CB    1 
ATOM   4479  N  N     . ASP   A  1  614  ? -19.391 92.759  127.984 1.00 34.69 ? 612  ASP   A N     1 
ATOM   4480  C  CA    . ASP   A  1  614  ? -19.940 91.436  128.264 1.00 29.59 ? 612  ASP   A CA    1 
ATOM   4481  C  C     . ASP   A  1  614  ? -19.277 90.362  127.412 1.00 30.99 ? 612  ASP   A C     1 
ATOM   4482  O  O     . ASP   A  1  614  ? -19.181 89.206  127.839 1.00 29.44 ? 612  ASP   A O     1 
ATOM   4483  C  CB    . ASP   A  1  614  ? -21.452 91.428  128.057 1.00 32.55 ? 612  ASP   A CB    1 
ATOM   4484  C  CG    . ASP   A  1  614  ? -22.192 92.208  129.134 1.00 33.04 ? 612  ASP   A CG    1 
ATOM   4485  O  OD1   . ASP   A  1  614  ? -21.688 92.272  130.275 1.00 37.44 ? 612  ASP   A OD1   1 
ATOM   4486  O  OD2   . ASP   A  1  614  ? -23.273 92.752  128.838 1.00 35.53 ? 612  ASP   A OD2   1 
ATOM   4487  N  N     . ALA   A  1  615  ? -18.814 90.720  126.215 1.00 28.65 ? 613  ALA   A N     1 
ATOM   4488  C  CA    . ALA   A  1  615  ? -18.060 89.767  125.407 1.00 29.16 ? 613  ALA   A CA    1 
ATOM   4489  C  C     . ALA   A  1  615  ? -16.773 89.367  126.114 1.00 27.37 ? 613  ALA   A C     1 
ATOM   4490  O  O     . ALA   A  1  615  ? -16.435 88.180  126.192 1.00 27.72 ? 613  ALA   A O     1 
ATOM   4491  C  CB    . ALA   A  1  615  ? -17.762 90.352  124.026 1.00 27.57 ? 613  ALA   A CB    1 
ATOM   4492  N  N     . ARG   A  1  616  ? -16.048 90.351  126.652 1.00 31.83 ? 614  ARG   A N     1 
ATOM   4493  C  CA    . ARG   A  1  616  ? -14.849 90.043  127.423 1.00 34.24 ? 614  ARG   A CA    1 
ATOM   4494  C  C     . ARG   A  1  616  ? -15.194 89.258  128.681 1.00 26.49 ? 614  ARG   A C     1 
ATOM   4495  O  O     . ARG   A  1  616  ? -14.486 88.313  129.046 1.00 31.64 ? 614  ARG   A O     1 
ATOM   4496  C  CB    . ARG   A  1  616  ? -14.099 91.331  127.758 1.00 36.37 ? 614  ARG   A CB    1 
ATOM   4497  C  CG    . ARG   A  1  616  ? -13.168 91.788  126.644 1.00 41.22 ? 614  ARG   A CG    1 
ATOM   4498  C  CD    . ARG   A  1  616  ? -12.544 93.152  126.927 1.00 47.76 ? 614  ARG   A CD    1 
ATOM   4499  N  NE    . ARG   A  1  616  ? -13.336 94.238  126.361 1.00 53.48 ? 614  ARG   A NE    1 
ATOM   4500  C  CZ    . ARG   A  1  616  ? -14.005 95.135  127.072 1.00 48.52 ? 614  ARG   A CZ    1 
ATOM   4501  N  NH1   . ARG   A  1  616  ? -13.979 95.131  128.396 1.00 53.33 ? 614  ARG   A NH1   1 
ATOM   4502  N  NH2   . ARG   A  1  616  ? -14.711 96.066  126.438 1.00 50.09 ? 614  ARG   A NH2   1 
ATOM   4503  N  N     . ARG   A  1  617  ? -16.304 89.612  129.337 1.00 27.00 ? 615  ARG   A N     1 
ATOM   4504  C  CA    . ARG   A  1  617  ? -16.734 88.849  130.504 1.00 30.85 ? 615  ARG   A CA    1 
ATOM   4505  C  C     . ARG   A  1  617  ? -17.061 87.408  130.129 1.00 31.38 ? 615  ARG   A C     1 
ATOM   4506  O  O     . ARG   A  1  617  ? -16.739 86.478  130.875 1.00 29.97 ? 615  ARG   A O     1 
ATOM   4507  C  CB    . ARG   A  1  617  ? -17.934 89.524  131.163 1.00 34.39 ? 615  ARG   A CB    1 
ATOM   4508  C  CG    . ARG   A  1  617  ? -18.354 88.870  132.461 1.00 39.35 ? 615  ARG   A CG    1 
ATOM   4509  C  CD    . ARG   A  1  617  ? -19.087 89.850  133.357 1.00 43.94 ? 615  ARG   A CD    1 
ATOM   4510  N  NE    . ARG   A  1  617  ? -20.361 90.282  132.796 1.00 45.74 ? 615  ARG   A NE    1 
ATOM   4511  C  CZ    . ARG   A  1  617  ? -21.518 89.672  133.017 1.00 50.64 ? 615  ARG   A CZ    1 
ATOM   4512  N  NH1   . ARG   A  1  617  ? -21.589 88.567  133.745 1.00 46.88 ? 615  ARG   A NH1   1 
ATOM   4513  N  NH2   . ARG   A  1  617  ? -22.632 90.184  132.497 1.00 44.70 ? 615  ARG   A NH2   1 
ATOM   4514  N  N     . ALA   A  1  618  ? -17.702 87.201  128.974 1.00 30.08 ? 616  ALA   A N     1 
ATOM   4515  C  CA    . ALA   A  1  618  ? -18.040 85.843  128.555 1.00 27.37 ? 616  ALA   A CA    1 
ATOM   4516  C  C     . ALA   A  1  618  ? -16.789 84.988  128.379 1.00 24.70 ? 616  ALA   A C     1 
ATOM   4517  O  O     . ALA   A  1  618  ? -16.769 83.812  128.767 1.00 27.11 ? 616  ALA   A O     1 
ATOM   4518  C  CB    . ALA   A  1  618  ? -18.867 85.872  127.266 1.00 27.20 ? 616  ALA   A CB    1 
ATOM   4519  N  N     . VAL   A  1  619  ? -15.728 85.562  127.812 1.00 25.42 ? 617  VAL   A N     1 
ATOM   4520  C  CA    . VAL   A  1  619  ? -14.494 84.799  127.653 1.00 26.41 ? 617  VAL   A CA    1 
ATOM   4521  C  C     . VAL   A  1  619  ? -13.935 84.402  129.013 1.00 28.45 ? 617  VAL   A C     1 
ATOM   4522  O  O     . VAL   A  1  619  ? -13.481 83.266  129.205 1.00 28.20 ? 617  VAL   A O     1 
ATOM   4523  C  CB    . VAL   A  1  619  ? -13.470 85.578  126.808 1.00 25.48 ? 617  VAL   A CB    1 
ATOM   4524  C  CG1   . VAL   A  1  619  ? -12.172 84.780  126.678 1.00 27.69 ? 617  VAL   A CG1   1 
ATOM   4525  C  CG2   . VAL   A  1  619  ? -14.038 85.883  125.434 1.00 27.39 ? 617  VAL   A CG2   1 
ATOM   4526  N  N     . ARG   A  1  620  ? -13.965 85.323  129.981 1.00 27.51 ? 618  ARG   A N     1 
ATOM   4527  C  CA    . ARG   A  1  620  ? -13.474 84.989  131.313 1.00 30.02 ? 618  ARG   A CA    1 
ATOM   4528  C  C     . ARG   A  1  620  ? -14.309 83.884  131.941 1.00 28.68 ? 618  ARG   A C     1 
ATOM   4529  O  O     . ARG   A  1  620  ? -13.763 82.960  132.556 1.00 33.41 ? 618  ARG   A O     1 
ATOM   4530  C  CB    . ARG   A  1  620  ? -13.442 86.237  132.195 1.00 32.90 ? 618  ARG   A CB    1 
ATOM   4531  C  CG    . ARG   A  1  620  ? -12.303 87.174  131.844 1.00 35.82 ? 618  ARG   A CG    1 
ATOM   4532  C  CD    . ARG   A  1  620  ? -12.211 88.354  132.800 1.00 45.64 ? 618  ARG   A CD    1 
ATOM   4533  N  NE    . ARG   A  1  620  ? -12.630 89.589  132.150 1.00 49.04 ? 618  ARG   A NE    1 
ATOM   4534  C  CZ    . ARG   A  1  620  ? -13.758 90.235  132.414 1.00 42.03 ? 618  ARG   A CZ    1 
ATOM   4535  N  NH1   . ARG   A  1  620  ? -14.579 89.834  133.373 1.00 49.60 ? 618  ARG   A NH1   1 
ATOM   4536  N  NH2   . ARG   A  1  620  ? -14.066 91.315  131.702 1.00 44.20 ? 618  ARG   A NH2   1 
ATOM   4537  N  N     . LEU   A  1  621  ? -15.634 83.940  131.767 1.00 27.00 ? 619  LEU   A N     1 
ATOM   4538  C  CA    . LEU   A  1  621  ? -16.487 82.881  132.296 1.00 29.56 ? 619  LEU   A CA    1 
ATOM   4539  C  C     . LEU   A  1  621  ? -16.204 81.555  131.601 1.00 27.25 ? 619  LEU   A C     1 
ATOM   4540  O  O     . LEU   A  1  621  ? -16.209 80.497  132.242 1.00 29.32 ? 619  LEU   A O     1 
ATOM   4541  C  CB    . LEU   A  1  621  ? -17.958 83.263  132.145 1.00 29.12 ? 619  LEU   A CB    1 
ATOM   4542  C  CG    . LEU   A  1  621  ? -18.443 84.498  132.903 1.00 31.30 ? 619  LEU   A CG    1 
ATOM   4543  C  CD1   . LEU   A  1  621  ? -19.808 84.909  132.399 1.00 30.44 ? 619  LEU   A CD1   1 
ATOM   4544  C  CD2   . LEU   A  1  621  ? -18.496 84.224  134.392 1.00 33.01 ? 619  LEU   A CD2   1 
ATOM   4545  N  N     . ALA   A  1  622  ? -15.956 81.594  130.288 1.00 28.16 ? 620  ALA   A N     1 
ATOM   4546  C  CA    . ALA   A  1  622  ? -15.579 80.384  129.563 1.00 28.78 ? 620  ALA   A CA    1 
ATOM   4547  C  C     . ALA   A  1  622  ? -14.264 79.827  130.086 1.00 25.80 ? 620  ALA   A C     1 
ATOM   4548  O  O     . ALA   A  1  622  ? -14.121 78.612  130.268 1.00 28.05 ? 620  ALA   A O     1 
ATOM   4549  C  CB    . ALA   A  1  622  ? -15.476 80.674  128.066 1.00 26.72 ? 620  ALA   A CB    1 
ATOM   4550  N  N     . ALA   A  1  623  ? -13.290 80.705  130.336 1.00 27.73 ? 621  ALA   A N     1 
ATOM   4551  C  CA    . ALA   A  1  623  ? -12.016 80.259  130.889 1.00 28.85 ? 621  ALA   A CA    1 
ATOM   4552  C  C     . ALA   A  1  623  ? -12.209 79.602  132.249 1.00 27.46 ? 621  ALA   A C     1 
ATOM   4553  O  O     . ALA   A  1  623  ? -11.609 78.560  132.534 1.00 30.76 ? 621  ALA   A O     1 
ATOM   4554  C  CB    . ALA   A  1  623  ? -11.053 81.440  130.994 1.00 31.90 ? 621  ALA   A CB    1 
ATOM   4555  N  N     . ASP   A  1  624  ? -13.059 80.184  133.097 1.00 27.67 ? 622  ASP   A N     1 
ATOM   4556  C  CA    . ASP   A  1  624  ? -13.297 79.591  134.411 1.00 33.65 ? 622  ASP   A CA    1 
ATOM   4557  C  C     . ASP   A  1  624  ? -14.010 78.252  134.289 1.00 33.45 ? 622  ASP   A C     1 
ATOM   4558  O  O     . ASP   A  1  624  ? -13.759 77.339  135.084 1.00 38.21 ? 622  ASP   A O     1 
ATOM   4559  C  CB    . ASP   A  1  624  ? -14.122 80.540  135.283 1.00 38.95 ? 622  ASP   A CB    1 
ATOM   4560  C  CG    . ASP   A  1  624  ? -13.391 81.835  135.596 1.00 44.60 ? 622  ASP   A CG    1 
ATOM   4561  O  OD1   . ASP   A  1  624  ? -12.140 81.834  135.599 1.00 50.15 ? 622  ASP   A OD1   1 
ATOM   4562  O  OD2   . ASP   A  1  624  ? -14.075 82.852  135.841 1.00 49.91 ? 622  ASP   A OD2   1 
ATOM   4563  N  N     . ALA   A  1  625  ? -14.883 78.119  133.293 1.00 34.37 ? 623  ALA   A N     1 
ATOM   4564  C  CA    . ALA   A  1  625  ? -15.659 76.911  133.058 1.00 37.19 ? 623  ALA   A CA    1 
ATOM   4565  C  C     . ALA   A  1  625  ? -14.901 75.852  132.279 1.00 36.43 ? 623  ALA   A C     1 
ATOM   4566  O  O     . ALA   A  1  625  ? -15.402 74.730  132.150 1.00 37.12 ? 623  ALA   A O     1 
ATOM   4567  C  CB    . ALA   A  1  625  ? -16.905 77.266  132.251 1.00 38.32 ? 623  ALA   A CB    1 
ATOM   4568  N  N     . ALA   A  1  626  ? -13.733 76.181  131.738 1.00 30.77 ? 624  ALA   A N     1 
ATOM   4569  C  CA    . ALA   A  1  626  ? -13.041 75.245  130.854 1.00 29.28 ? 624  ALA   A CA    1 
ATOM   4570  C  C     . ALA   A  1  626  ? -12.741 73.902  131.509 1.00 33.46 ? 624  ALA   A C     1 
ATOM   4571  O  O     . ALA   A  1  626  ? -12.996 72.864  130.875 1.00 34.02 ? 624  ALA   A O     1 
ATOM   4572  C  CB    . ALA   A  1  626  ? -11.804 75.912  130.245 1.00 31.26 ? 624  ALA   A CB    1 
ATOM   4573  N  N     . PRO   A  1  627  ? -12.213 73.830  132.740 1.00 31.91 ? 625  PRO   A N     1 
ATOM   4574  C  CA    . PRO   A  1  627  ? -11.914 72.502  133.304 1.00 31.74 ? 625  PRO   A CA    1 
ATOM   4575  C  C     . PRO   A  1  627  ? -13.142 71.622  133.462 1.00 31.39 ? 625  PRO   A C     1 
ATOM   4576  O  O     . PRO   A  1  627  ? -13.075 70.413  133.198 1.00 33.93 ? 625  PRO   A O     1 
ATOM   4577  C  CB    . PRO   A  1  627  ? -11.273 72.833  134.662 1.00 32.47 ? 625  PRO   A CB    1 
ATOM   4578  C  CG    . PRO   A  1  627  ? -10.776 74.234  134.516 1.00 34.05 ? 625  PRO   A CG    1 
ATOM   4579  C  CD    . PRO   A  1  627  ? -11.803 74.906  133.662 1.00 32.95 ? 625  PRO   A CD    1 
ATOM   4580  N  N     . ASP   A  1  628  ? -14.266 72.199  133.884 1.00 32.32 ? 626  ASP   A N     1 
ATOM   4581  C  CA    . ASP   A  1  628  ? -15.462 71.399  134.107 1.00 32.38 ? 626  ASP   A CA    1 
ATOM   4582  C  C     . ASP   A  1  628  ? -15.954 70.781  132.809 1.00 33.03 ? 626  ASP   A C     1 
ATOM   4583  O  O     . ASP   A  1  628  ? -16.439 69.644  132.796 1.00 36.78 ? 626  ASP   A O     1 
ATOM   4584  C  CB    . ASP   A  1  628  ? -16.558 72.264  134.729 1.00 30.77 ? 626  ASP   A CB    1 
ATOM   4585  C  CG    . ASP   A  1  628  ? -16.199 72.743  136.122 1.00 38.37 ? 626  ASP   A CG    1 
ATOM   4586  O  OD1   . ASP   A  1  628  ? -15.137 72.337  136.628 1.00 43.25 ? 626  ASP   A OD1   1 
ATOM   4587  O  OD2   . ASP   A  1  628  ? -16.976 73.524  136.703 1.00 47.99 ? 626  ASP   A OD2   1 
ATOM   4588  N  N     . TRP   A  1  629  ? -15.838 71.515  131.705 1.00 30.06 ? 627  TRP   A N     1 
ATOM   4589  C  CA    . TRP   A  1  629  ? -16.309 70.982  130.438 1.00 30.17 ? 627  TRP   A CA    1 
ATOM   4590  C  C     . TRP   A  1  629  ? -15.315 69.986  129.860 1.00 29.86 ? 627  TRP   A C     1 
ATOM   4591  O  O     . TRP   A  1  629  ? -15.716 68.952  129.313 1.00 29.25 ? 627  TRP   A O     1 
ATOM   4592  C  CB    . TRP   A  1  629  ? -16.579 72.119  129.460 1.00 28.97 ? 627  TRP   A CB    1 
ATOM   4593  C  CG    . TRP   A  1  629  ? -17.047 71.622  128.140 1.00 25.97 ? 627  TRP   A CG    1 
ATOM   4594  C  CD1   . TRP   A  1  629  ? -16.444 71.814  126.929 1.00 23.59 ? 627  TRP   A CD1   1 
ATOM   4595  C  CD2   . TRP   A  1  629  ? -18.189 70.791  127.893 1.00 23.72 ? 627  TRP   A CD2   1 
ATOM   4596  N  NE1   . TRP   A  1  629  ? -17.162 71.184  125.945 1.00 23.40 ? 627  TRP   A NE1   1 
ATOM   4597  C  CE2   . TRP   A  1  629  ? -18.240 70.554  126.509 1.00 23.23 ? 627  TRP   A CE2   1 
ATOM   4598  C  CE3   . TRP   A  1  629  ? -19.192 70.253  128.704 1.00 26.68 ? 627  TRP   A CE3   1 
ATOM   4599  C  CZ2   . TRP   A  1  629  ? -19.239 69.787  125.919 1.00 24.94 ? 627  TRP   A CZ2   1 
ATOM   4600  C  CZ3   . TRP   A  1  629  ? -20.184 69.486  128.110 1.00 26.66 ? 627  TRP   A CZ3   1 
ATOM   4601  C  CH2   . TRP   A  1  629  ? -20.195 69.259  126.733 1.00 26.02 ? 627  TRP   A CH2   1 
ATOM   4602  N  N     . ALA   A  1  630  ? -14.018 70.277  129.983 1.00 26.79 ? 628  ALA   A N     1 
ATOM   4603  C  CA    . ALA   A  1  630  ? -13.002 69.331  129.535 1.00 30.81 ? 628  ALA   A CA    1 
ATOM   4604  C  C     . ALA   A  1  630  ? -13.113 68.003  130.268 1.00 32.25 ? 628  ALA   A C     1 
ATOM   4605  O  O     . ALA   A  1  630  ? -12.761 66.953  129.712 1.00 29.42 ? 628  ALA   A O     1 
ATOM   4606  C  CB    . ALA   A  1  630  ? -11.607 69.923  129.730 1.00 32.04 ? 628  ALA   A CB    1 
ATOM   4607  N  N     . ALA   A  1  631  ? -13.596 68.028  131.513 1.00 29.67 ? 629  ALA   A N     1 
ATOM   4608  C  CA    . ALA   A  1  631  ? -13.733 66.819  132.316 1.00 30.38 ? 629  ALA   A CA    1 
ATOM   4609  C  C     . ALA   A  1  631  ? -14.946 65.980  131.943 1.00 30.97 ? 629  ALA   A C     1 
ATOM   4610  O  O     . ALA   A  1  631  ? -15.045 64.833  132.388 1.00 31.98 ? 629  ALA   A O     1 
ATOM   4611  C  CB    . ALA   A  1  631  ? -13.772 67.163  133.806 1.00 30.98 ? 629  ALA   A CB    1 
ATOM   4612  N  N     . VAL   A  1  632  ? -15.872 66.510  131.151 1.00 31.07 ? 630  VAL   A N     1 
ATOM   4613  C  CA    . VAL   A  1  632  ? -16.955 65.687  130.622 1.00 29.20 ? 630  VAL   A CA    1 
ATOM   4614  C  C     . VAL   A  1  632  ? -16.301 64.747  129.618 1.00 27.78 ? 630  VAL   A C     1 
ATOM   4615  O  O     . VAL   A  1  632  ? -15.614 65.219  128.704 1.00 29.75 ? 630  VAL   A O     1 
ATOM   4616  C  CB    . VAL   A  1  632  ? -18.056 66.550  129.991 1.00 29.53 ? 630  VAL   A CB    1 
ATOM   4617  C  CG1   . VAL   A  1  632  ? -19.160 65.677  129.385 1.00 29.71 ? 630  VAL   A CG1   1 
ATOM   4618  C  CG2   . VAL   A  1  632  ? -18.625 67.497  131.042 1.00 28.30 ? 630  VAL   A CG2   1 
ATOM   4619  N  N     . PRO   A  1  633  ? -16.451 63.430  129.770 1.00 26.09 ? 631  PRO   A N     1 
ATOM   4620  C  CA    . PRO   A  1  633  ? -15.744 62.511  128.881 1.00 26.74 ? 631  PRO   A CA    1 
ATOM   4621  C  C     . PRO   A  1  633  ? -16.141 62.751  127.433 1.00 25.75 ? 631  PRO   A C     1 
ATOM   4622  O  O     . PRO   A  1  633  ? -17.284 63.143  127.145 1.00 25.57 ? 631  PRO   A O     1 
ATOM   4623  C  CB    . PRO   A  1  633  ? -16.212 61.131  129.362 1.00 29.23 ? 631  PRO   A CB    1 
ATOM   4624  C  CG    . PRO   A  1  633  ? -16.599 61.343  130.786 1.00 31.67 ? 631  PRO   A CG    1 
ATOM   4625  C  CD    . PRO   A  1  633  ? -17.187 62.721  130.830 1.00 28.06 ? 631  PRO   A CD    1 
ATOM   4626  N  N     . PRO   A  1  634  ? -15.213 62.545  126.498 1.00 23.34 ? 632  PRO   A N     1 
ATOM   4627  C  CA    . PRO   A  1  634  ? -15.553 62.762  125.077 1.00 23.85 ? 632  PRO   A CA    1 
ATOM   4628  C  C     . PRO   A  1  634  ? -16.815 62.047  124.638 1.00 24.24 ? 632  PRO   A C     1 
ATOM   4629  O  O     . PRO   A  1  634  ? -17.600 62.617  123.877 1.00 22.66 ? 632  PRO   A O     1 
ATOM   4630  C  CB    . PRO   A  1  634  ? -14.321 62.234  124.329 1.00 22.84 ? 632  PRO   A CB    1 
ATOM   4631  C  CG    . PRO   A  1  634  ? -13.210 62.308  125.315 1.00 25.79 ? 632  PRO   A CG    1 
ATOM   4632  C  CD    . PRO   A  1  634  ? -13.808 62.156  126.693 1.00 24.78 ? 632  PRO   A CD    1 
ATOM   4633  N  N     . SER   A  1  635  ? -17.033 60.813  125.097 1.00 24.24 ? 633  SER   A N     1 
ATOM   4634  C  CA    . SER   A  1  635  ? -18.226 60.075  124.693 1.00 27.13 ? 633  SER   A CA    1 
ATOM   4635  C  C     . SER   A  1  635  ? -19.491 60.793  125.140 1.00 26.74 ? 633  SER   A C     1 
ATOM   4636  O  O     . SER   A  1  635  ? -20.495 60.806  124.417 1.00 25.58 ? 633  SER   A O     1 
ATOM   4637  C  CB    . SER   A  1  635  ? -18.188 58.671  125.292 1.00 36.40 ? 633  SER   A CB    1 
ATOM   4638  O  OG    . SER   A  1  635  ? -18.256 58.736  126.706 1.00 41.50 ? 633  SER   A OG    1 
ATOM   4639  N  N     . GLU   A  1  636  ? -19.459 61.406  126.325 1.00 25.20 ? 634  GLU   A N     1 
ATOM   4640  C  CA    . GLU   A  1  636  ? -20.626 62.138  126.803 1.00 26.22 ? 634  GLU   A CA    1 
ATOM   4641  C  C     . GLU   A  1  636  ? -20.786 63.466  126.076 1.00 24.51 ? 634  GLU   A C     1 
ATOM   4642  O  O     . GLU   A  1  636  ? -21.913 63.879  125.786 1.00 24.95 ? 634  GLU   A O     1 
ATOM   4643  C  CB    . GLU   A  1  636  ? -20.571 62.334  128.319 1.00 26.85 ? 634  GLU   A CB    1 
ATOM   4644  C  CG    . GLU   A  1  636  ? -21.750 63.126  128.861 1.00 35.13 ? 634  GLU   A CG    1 
ATOM   4645  C  CD    . GLU   A  1  636  ? -23.100 62.571  128.412 1.00 43.69 ? 634  GLU   A CD    1 
ATOM   4646  O  OE1   . GLU   A  1  636  ? -23.285 61.334  128.459 1.00 41.36 ? 634  GLU   A OE1   1 
ATOM   4647  O  OE2   . GLU   A  1  636  ? -23.974 63.368  127.997 1.00 37.80 ? 634  GLU   A OE2   1 
ATOM   4648  N  N     . ARG   A  1  637  ? -19.683 64.151  125.766 1.00 24.64 ? 635  ARG   A N     1 
ATOM   4649  C  CA    . ARG   A  1  637  ? -19.786 65.333  124.915 1.00 22.70 ? 635  ARG   A CA    1 
ATOM   4650  C  C     . ARG   A  1  637  ? -20.410 64.967  123.578 1.00 22.47 ? 635  ARG   A C     1 
ATOM   4651  O  O     . ARG   A  1  637  ? -21.317 65.651  123.092 1.00 22.35 ? 635  ARG   A O     1 
ATOM   4652  C  CB    . ARG   A  1  637  ? -18.414 65.989  124.727 1.00 21.74 ? 635  ARG   A CB    1 
ATOM   4653  C  CG    . ARG   A  1  637  ? -17.766 66.350  126.065 1.00 23.42 ? 635  ARG   A CG    1 
ATOM   4654  C  CD    . ARG   A  1  637  ? -16.590 67.297  125.927 1.00 25.50 ? 635  ARG   A CD    1 
ATOM   4655  N  NE    . ARG   A  1  637  ? -15.530 66.762  125.086 1.00 24.60 ? 635  ARG   A NE    1 
ATOM   4656  C  CZ    . ARG   A  1  637  ? -14.355 66.314  125.518 1.00 26.56 ? 635  ARG   A CZ    1 
ATOM   4657  N  NH1   . ARG   A  1  637  ? -14.062 66.254  126.810 1.00 26.92 ? 635  ARG   A NH1   1 
ATOM   4658  N  NH2   . ARG   A  1  637  ? -13.443 65.934  124.630 1.00 24.94 ? 635  ARG   A NH2   1 
ATOM   4659  N  N     . ALA   A  1  638  ? -19.952 63.862  122.985 1.00 23.66 ? 636  ALA   A N     1 
ATOM   4660  C  CA    . ALA   A  1  638  ? -20.507 63.409  121.715 1.00 21.77 ? 636  ALA   A CA    1 
ATOM   4661  C  C     . ALA   A  1  638  ? -21.988 63.077  121.847 1.00 22.99 ? 636  ALA   A C     1 
ATOM   4662  O  O     . ALA   A  1  638  ? -22.770 63.308  120.916 1.00 20.57 ? 636  ALA   A O     1 
ATOM   4663  C  CB    . ALA   A  1  638  ? -19.725 62.189  121.229 1.00 22.20 ? 636  ALA   A CB    1 
ATOM   4664  N  N     . ALA   A  1  639  ? -22.389 62.518  122.992 1.00 22.02 ? 637  ALA   A N     1 
ATOM   4665  C  CA    . ALA   A  1  639  ? -23.801 62.228  123.204 1.00 22.97 ? 637  ALA   A CA    1 
ATOM   4666  C  C     . ALA   A  1  639  ? -24.629 63.505  123.233 1.00 24.35 ? 637  ALA   A C     1 
ATOM   4667  O  O     . ALA   A  1  639  ? -25.777 63.507  122.777 1.00 24.82 ? 637  ALA   A O     1 
ATOM   4668  C  CB    . ALA   A  1  639  ? -23.999 61.394  124.471 1.00 24.78 ? 637  ALA   A CB    1 
ATOM   4669  N  N     . CYS   A  1  640  ? -24.061 64.606  123.736 1.00 22.78 ? 638  CYS   A N     1 
ATOM   4670  C  CA    . CYS   A  1  640  ? -24.758 65.884  123.653 1.00 22.60 ? 638  CYS   A CA    1 
ATOM   4671  C  C     . CYS   A  1  640  ? -24.993 66.273  122.206 1.00 22.56 ? 638  CYS   A C     1 
ATOM   4672  O  O     . CYS   A  1  640  ? -26.092 66.702  121.834 1.00 22.17 ? 638  CYS   A O     1 
ATOM   4673  C  CB    . CYS   A  1  640  ? -23.963 66.980  124.348 1.00 23.02 ? 638  CYS   A CB    1 
ATOM   4674  S  SG    . CYS   A  1  640  ? -23.865 66.807  126.128 1.00 26.08 ? 638  CYS   A SG    1 
ATOM   4675  N  N     . LEU   A  1  641  ? -23.963 66.132  121.372 1.00 21.22 ? 639  LEU   A N     1 
ATOM   4676  C  CA    . LEU   A  1  641  ? -24.114 66.474  119.966 1.00 21.38 ? 639  LEU   A CA    1 
ATOM   4677  C  C     . LEU   A  1  641  ? -25.166 65.602  119.314 1.00 20.44 ? 639  LEU   A C     1 
ATOM   4678  O  O     . LEU   A  1  641  ? -25.991 66.091  118.532 1.00 19.83 ? 639  LEU   A O     1 
ATOM   4679  C  CB    . LEU   A  1  641  ? -22.778 66.316  119.247 1.00 20.11 ? 639  LEU   A CB    1 
ATOM   4680  C  CG    . LEU   A  1  641  ? -21.875 67.549  119.211 1.00 21.86 ? 639  LEU   A CG    1 
ATOM   4681  C  CD1   . LEU   A  1  641  ? -21.473 68.025  120.591 1.00 24.51 ? 639  LEU   A CD1   1 
ATOM   4682  C  CD2   . LEU   A  1  641  ? -20.642 67.243  118.379 1.00 19.72 ? 639  LEU   A CD2   1 
ATOM   4683  N  N     . ASP   A  1  642  ? -25.164 64.306  119.625 1.00 20.35 ? 640  ASP   A N     1 
ATOM   4684  C  CA    . ASP   A  1  642  ? -26.155 63.423  119.021 1.00 20.41 ? 640  ASP   A CA    1 
ATOM   4685  C  C     . ASP   A  1  642  ? -27.560 63.773  119.490 1.00 20.54 ? 640  ASP   A C     1 
ATOM   4686  O  O     . ASP   A  1  642  ? -28.511 63.741  118.698 1.00 21.51 ? 640  ASP   A O     1 
ATOM   4687  C  CB    . ASP   A  1  642  ? -25.836 61.965  119.332 1.00 20.93 ? 640  ASP   A CB    1 
ATOM   4688  C  CG    . ASP   A  1  642  ? -24.751 61.403  118.437 1.00 21.84 ? 640  ASP   A CG    1 
ATOM   4689  O  OD1   . ASP   A  1  642  ? -24.539 61.949  117.327 1.00 22.86 ? 640  ASP   A OD1   1 
ATOM   4690  O  OD2   . ASP   A  1  642  ? -24.131 60.402  118.847 1.00 24.34 ? 640  ASP   A OD2   1 
ATOM   4691  N  N     . ARG   A  1  643  ? -27.714 64.129  120.764 1.00 21.50 ? 641  ARG   A N     1 
ATOM   4692  C  CA    . ARG   A  1  643  ? -29.024 64.568  121.231 1.00 22.06 ? 641  ARG   A CA    1 
ATOM   4693  C  C     . ARG   A  1  643  ? -29.443 65.852  120.538 1.00 22.77 ? 641  ARG   A C     1 
ATOM   4694  O  O     . ARG   A  1  643  ? -30.613 66.016  120.172 1.00 22.80 ? 641  ARG   A O     1 
ATOM   4695  C  CB    . ARG   A  1  643  ? -29.019 64.761  122.746 1.00 21.70 ? 641  ARG   A CB    1 
ATOM   4696  C  CG    . ARG   A  1  643  ? -29.195 63.469  123.516 1.00 23.83 ? 641  ARG   A CG    1 
ATOM   4697  C  CD    . ARG   A  1  643  ? -29.361 63.732  125.002 1.00 27.24 ? 641  ARG   A CD    1 
ATOM   4698  N  NE    . ARG   A  1  643  ? -28.206 64.396  125.593 1.00 26.47 ? 641  ARG   A NE    1 
ATOM   4699  C  CZ    . ARG   A  1  643  ? -27.205 63.761  126.186 1.00 25.15 ? 641  ARG   A CZ    1 
ATOM   4700  N  NH1   . ARG   A  1  643  ? -27.139 62.441  126.200 1.00 29.11 ? 641  ARG   A NH1   1 
ATOM   4701  N  NH2   . ARG   A  1  643  ? -26.249 64.468  126.781 1.00 29.86 ? 641  ARG   A NH2   1 
ATOM   4702  N  N     . ALA   A  1  644  ? -28.503 66.778  120.344 1.00 19.86 ? 642  ALA   A N     1 
ATOM   4703  C  CA    . ALA   A  1  644  ? -28.836 68.005  119.630 1.00 20.30 ? 642  ALA   A CA    1 
ATOM   4704  C  C     . ALA   A  1  644  ? -29.274 67.704  118.206 1.00 20.51 ? 642  ALA   A C     1 
ATOM   4705  O  O     . ALA   A  1  644  ? -30.191 68.345  117.687 1.00 21.49 ? 642  ALA   A O     1 
ATOM   4706  C  CB    . ALA   A  1  644  ? -27.662 68.976  119.643 1.00 22.59 ? 642  ALA   A CB    1 
ATOM   4707  N  N     . ALA   A  1  645  ? -28.640 66.723  117.560 1.00 19.51 ? 643  ALA   A N     1 
ATOM   4708  C  CA    . ALA   A  1  645  ? -29.029 66.368  116.202 1.00 19.20 ? 643  ALA   A CA    1 
ATOM   4709  C  C     . ALA   A  1  645  ? -30.446 65.808  116.167 1.00 20.57 ? 643  ALA   A C     1 
ATOM   4710  O  O     . ALA   A  1  645  ? -31.220 66.121  115.253 1.00 21.64 ? 643  ALA   A O     1 
ATOM   4711  C  CB    . ALA   A  1  645  ? -28.014 65.374  115.635 1.00 19.24 ? 643  ALA   A CB    1 
ATOM   4712  N  N     . GLU   A  1  646  ? -30.791 64.961  117.137 1.00 21.11 ? 644  GLU   A N     1 
ATOM   4713  C  CA    . GLU   A  1  646  ? -32.158 64.460  117.236 1.00 22.32 ? 644  GLU   A CA    1 
ATOM   4714  C  C     . GLU   A  1  646  ? -33.142 65.603  117.411 1.00 23.77 ? 644  GLU   A C     1 
ATOM   4715  O  O     . GLU   A  1  646  ? -34.204 65.621  116.776 1.00 24.54 ? 644  GLU   A O     1 
ATOM   4716  C  CB    . GLU   A  1  646  ? -32.287 63.495  118.411 1.00 27.76 ? 644  GLU   A CB    1 
ATOM   4717  C  CG    . GLU   A  1  646  ? -31.516 62.207  118.259 1.00 30.32 ? 644  GLU   A CG    1 
ATOM   4718  C  CD    . GLU   A  1  646  ? -31.973 61.394  117.067 1.00 39.44 ? 644  GLU   A CD    1 
ATOM   4719  O  OE1   . GLU   A  1  646  ? -33.186 61.392  116.772 1.00 42.69 ? 644  GLU   A OE1   1 
ATOM   4720  O  OE2   . GLU   A  1  646  ? -31.113 60.767  116.415 1.00 37.89 ? 644  GLU   A OE2   1 
ATOM   4721  N  N     . LEU   A  1  647  ? -32.806 66.567  118.272 1.00 23.16 ? 645  LEU   A N     1 
ATOM   4722  C  CA    . LEU   A  1  647  ? -33.699 67.698  118.499 1.00 22.50 ? 645  LEU   A CA    1 
ATOM   4723  C  C     . LEU   A  1  647  ? -33.848 68.541  117.240 1.00 24.17 ? 645  LEU   A C     1 
ATOM   4724  O  O     . LEU   A  1  647  ? -34.954 68.992  116.918 1.00 25.52 ? 645  LEU   A O     1 
ATOM   4725  C  CB    . LEU   A  1  647  ? -33.189 68.549  119.658 1.00 23.29 ? 645  LEU   A CB    1 
ATOM   4726  C  CG    . LEU   A  1  647  ? -33.221 67.893  121.036 1.00 25.09 ? 645  LEU   A CG    1 
ATOM   4727  C  CD1   . LEU   A  1  647  ? -32.523 68.765  122.065 1.00 25.30 ? 645  LEU   A CD1   1 
ATOM   4728  C  CD2   . LEU   A  1  647  ? -34.666 67.624  121.469 1.00 29.20 ? 645  LEU   A CD2   1 
ATOM   4729  N  N     . MET   A  1  648  ? -32.753 68.767  116.515 1.00 21.26 ? 646  MET   A N     1 
ATOM   4730  C  CA    . MET   A  1  648  ? -32.852 69.540  115.282 1.00 20.96 ? 646  MET   A CA    1 
ATOM   4731  C  C     . MET   A  1  648  ? -33.655 68.799  114.232 1.00 22.33 ? 646  MET   A C     1 
ATOM   4732  O  O     . MET   A  1  648  ? -34.428 69.416  113.493 1.00 22.37 ? 646  MET   A O     1 
ATOM   4733  C  CB    . MET   A  1  648  ? -31.468 69.883  114.740 1.00 19.40 ? 646  MET   A CB    1 
ATOM   4734  C  CG    . MET   A  1  648  ? -30.801 70.965  115.522 1.00 22.20 ? 646  MET   A CG    1 
ATOM   4735  S  SD    . MET   A  1  648  ? -29.392 71.608  114.617 1.00 24.41 ? 646  MET   A SD    1 
ATOM   4736  C  CE    . MET   A  1  648  ? -28.690 72.678  115.866 1.00 26.63 ? 646  MET   A CE    1 
ATOM   4737  N  N     . GLN   A  1  649  ? -33.493 67.478  114.153 1.00 21.20 ? 647  GLN   A N     1 
ATOM   4738  C  CA    . GLN   A  1  649  ? -34.282 66.704  113.204 1.00 20.80 ? 647  GLN   A CA    1 
ATOM   4739  C  C     . GLN   A  1  649  ? -35.768 66.824  113.514 1.00 22.18 ? 647  GLN   A C     1 
ATOM   4740  O  O     . GLN   A  1  649  ? -36.585 67.061  112.616 1.00 24.17 ? 647  GLN   A O     1 
ATOM   4741  C  CB    . GLN   A  1  649  ? -33.852 65.240  113.227 1.00 23.17 ? 647  GLN   A CB    1 
ATOM   4742  C  CG    . GLN   A  1  649  ? -34.536 64.412  112.159 1.00 22.07 ? 647  GLN   A CG    1 
ATOM   4743  C  CD    . GLN   A  1  649  ? -33.973 64.680  110.778 1.00 22.39 ? 647  GLN   A CD    1 
ATOM   4744  O  OE1   . GLN   A  1  649  ? -32.883 64.229  110.442 1.00 21.07 ? 647  GLN   A OE1   1 
ATOM   4745  N  NE2   . GLN   A  1  649  ? -34.718 65.412  109.963 1.00 21.95 ? 647  GLN   A NE2   1 
ATOM   4746  N  N     . ALA   A  1  650  ? -36.133 66.669  114.782 1.00 23.08 ? 648  ALA   A N     1 
ATOM   4747  C  CA    . ALA   A  1  650  ? -37.540 66.732  115.162 1.00 23.99 ? 648  ALA   A CA    1 
ATOM   4748  C  C     . ALA   A  1  650  ? -38.107 68.127  114.964 1.00 28.17 ? 648  ALA   A C     1 
ATOM   4749  O  O     . ALA   A  1  650  ? -39.297 68.276  114.660 1.00 28.73 ? 648  ALA   A O     1 
ATOM   4750  C  CB    . ALA   A  1  650  ? -37.699 66.304  116.617 1.00 26.40 ? 648  ALA   A CB    1 
ATOM   4751  N  N     . ARG   A  1  651  ? -37.278 69.150  115.125 1.00 24.05 ? 649  ARG   A N     1 
ATOM   4752  C  CA    . ARG   A  1  651  ? -37.694 70.540  115.026 1.00 23.46 ? 649  ARG   A CA    1 
ATOM   4753  C  C     . ARG   A  1  651  ? -37.512 71.095  113.626 1.00 22.81 ? 649  ARG   A C     1 
ATOM   4754  O  O     . ARG   A  1  651  ? -37.773 72.281  113.405 1.00 22.91 ? 649  ARG   A O     1 
ATOM   4755  C  CB    . ARG   A  1  651  ? -36.900 71.391  116.028 1.00 25.92 ? 649  ARG   A CB    1 
ATOM   4756  C  CG    . ARG   A  1  651  ? -37.500 72.762  116.339 1.00 31.43 ? 649  ARG   A CG    1 
ATOM   4757  C  CD    . ARG   A  1  651  ? -37.333 73.127  117.819 1.00 31.27 ? 649  ARG   A CD    1 
ATOM   4758  N  NE    . ARG   A  1  651  ? -37.812 74.474  118.114 1.00 33.79 ? 649  ARG   A NE    1 
ATOM   4759  C  CZ    . ARG   A  1  651  ? -39.086 74.807  118.275 1.00 35.81 ? 649  ARG   A CZ    1 
ATOM   4760  N  NH1   . ARG   A  1  651  ? -40.056 73.916  118.147 1.00 37.67 ? 649  ARG   A NH1   1 
ATOM   4761  N  NH2   . ARG   A  1  651  ? -39.396 76.068  118.559 1.00 37.28 ? 649  ARG   A NH2   1 
ATOM   4762  N  N     . MET   A  1  652  ? -37.072 70.267  112.682 1.00 22.17 ? 650  MET   A N     1 
ATOM   4763  C  CA    . MET   A  1  652  ? -36.758 70.764  111.345 1.00 22.09 ? 650  MET   A CA    1 
ATOM   4764  C  C     . MET   A  1  652  ? -37.830 71.670  110.757 1.00 23.55 ? 650  MET   A C     1 
ATOM   4765  O  O     . MET   A  1  652  ? -37.481 72.758  110.278 1.00 21.62 ? 650  MET   A O     1 
ATOM   4766  C  CB    . MET   A  1  652  ? -36.397 69.618  110.394 1.00 20.84 ? 650  MET   A CB    1 
ATOM   4767  C  CG    . MET   A  1  652  ? -36.267 70.078  108.956 1.00 22.72 ? 650  MET   A CG    1 
ATOM   4768  S  SD    . MET   A  1  652  ? -35.759 68.772  107.825 1.00 24.95 ? 650  MET   A SD    1 
ATOM   4769  C  CE    . MET   A  1  652  ? -34.053 68.546  108.300 1.00 22.21 ? 650  MET   A CE    1 
ATOM   4770  N  N     . PRO   A  1  653  ? -39.124 71.317  110.771 1.00 21.34 ? 651  PRO   A N     1 
ATOM   4771  C  CA    . PRO   A  1  653  ? -40.106 72.205  110.125 1.00 25.21 ? 651  PRO   A CA    1 
ATOM   4772  C  C     . PRO   A  1  653  ? -40.106 73.609  110.700 1.00 24.11 ? 651  PRO   A C     1 
ATOM   4773  O  O     . PRO   A  1  653  ? -40.145 74.589  109.944 1.00 23.10 ? 651  PRO   A O     1 
ATOM   4774  C  CB    . PRO   A  1  653  ? -41.438 71.478  110.354 1.00 23.56 ? 651  PRO   A CB    1 
ATOM   4775  C  CG    . PRO   A  1  653  ? -41.049 70.039  110.484 1.00 25.61 ? 651  PRO   A CG    1 
ATOM   4776  C  CD    . PRO   A  1  653  ? -39.746 70.073  111.249 1.00 23.97 ? 651  PRO   A CD    1 
ATOM   4777  N  N     . THR   A  1  654  ? -40.032 73.728  112.024 1.00 21.74 ? 652  THR   A N     1 
ATOM   4778  C  CA    . THR   A  1  654  ? -39.966 75.043  112.646 1.00 22.72 ? 652  THR   A CA    1 
ATOM   4779  C  C     . THR   A  1  654  ? -38.672 75.755  112.290 1.00 21.83 ? 652  THR   A C     1 
ATOM   4780  O  O     . THR   A  1  654  ? -38.681 76.953  111.982 1.00 24.06 ? 652  THR   A O     1 
ATOM   4781  C  CB    . THR   A  1  654  ? -40.112 74.904  114.158 1.00 22.87 ? 652  THR   A CB    1 
ATOM   4782  O  OG1   . THR   A  1  654  ? -41.360 74.266  114.438 1.00 26.09 ? 652  THR   A OG1   1 
ATOM   4783  C  CG2   . THR   A  1  654  ? -40.071 76.272  114.838 1.00 27.31 ? 652  THR   A CG2   1 
ATOM   4784  N  N     . LEU   A  1  655  ? -37.549 75.035  112.329 1.00 21.28 ? 653  LEU   A N     1 
ATOM   4785  C  CA    . LEU   A  1  655  ? -36.276 75.629  111.935 1.00 22.51 ? 653  LEU   A CA    1 
ATOM   4786  C  C     . LEU   A  1  655  ? -36.313 76.116  110.493 1.00 24.68 ? 653  LEU   A C     1 
ATOM   4787  O  O     . LEU   A  1  655  ? -35.782 77.189  110.185 1.00 23.10 ? 653  LEU   A O     1 
ATOM   4788  C  CB    . LEU   A  1  655  ? -35.142 74.625  112.133 1.00 21.24 ? 653  LEU   A CB    1 
ATOM   4789  C  CG    . LEU   A  1  655  ? -34.991 74.123  113.569 1.00 21.03 ? 653  LEU   A CG    1 
ATOM   4790  C  CD1   . LEU   A  1  655  ? -33.886 73.093  113.667 1.00 22.81 ? 653  LEU   A CD1   1 
ATOM   4791  C  CD2   . LEU   A  1  655  ? -34.706 75.271  114.512 1.00 26.06 ? 653  LEU   A CD2   1 
ATOM   4792  N  N     . LEU   A  1  656  ? -36.935 75.340  109.594 1.00 22.83 ? 654  LEU   A N     1 
ATOM   4793  C  CA    . LEU   A  1  656  ? -37.081 75.781  108.207 1.00 22.50 ? 654  LEU   A CA    1 
ATOM   4794  C  C     . LEU   A  1  656  ? -37.729 77.151  108.137 1.00 22.83 ? 654  LEU   A C     1 
ATOM   4795  O  O     . LEU   A  1  656  ? -37.251 78.048  107.433 1.00 24.39 ? 654  LEU   A O     1 
ATOM   4796  C  CB    . LEU   A  1  656  ? -37.954 74.806  107.413 1.00 22.83 ? 654  LEU   A CB    1 
ATOM   4797  C  CG    . LEU   A  1  656  ? -37.501 73.366  107.245 1.00 23.94 ? 654  LEU   A CG    1 
ATOM   4798  C  CD1   . LEU   A  1  656  ? -38.369 72.663  106.229 1.00 26.87 ? 654  LEU   A CD1   1 
ATOM   4799  C  CD2   . LEU   A  1  656  ? -36.053 73.336  106.850 1.00 24.14 ? 654  LEU   A CD2   1 
ATOM   4800  N  N     . GLY   A  1  657  ? -38.851 77.310  108.833 1.00 22.85 ? 655  GLY   A N     1 
ATOM   4801  C  CA    . GLY   A  1  657  ? -39.580 78.558  108.749 1.00 24.00 ? 655  GLY   A CA    1 
ATOM   4802  C  C     . GLY   A  1  657  ? -38.752 79.738  109.199 1.00 22.17 ? 655  GLY   A C     1 
ATOM   4803  O  O     . GLY   A  1  657  ? -38.812 80.816  108.608 1.00 24.59 ? 655  GLY   A O     1 
ATOM   4804  N  N     . LEU   A  1  658  ? -37.968 79.553  110.260 1.00 22.29 ? 656  LEU   A N     1 
ATOM   4805  C  CA    . LEU   A  1  658  ? -37.135 80.645  110.737 1.00 21.48 ? 656  LEU   A CA    1 
ATOM   4806  C  C     . LEU   A  1  658  ? -36.042 80.964  109.723 1.00 19.37 ? 656  LEU   A C     1 
ATOM   4807  O  O     . LEU   A  1  658  ? -35.799 82.132  109.402 1.00 22.60 ? 656  LEU   A O     1 
ATOM   4808  C  CB    . LEU   A  1  658  ? -36.552 80.291  112.107 1.00 21.39 ? 656  LEU   A CB    1 
ATOM   4809  C  CG    . LEU   A  1  658  ? -35.643 81.338  112.732 1.00 24.01 ? 656  LEU   A CG    1 
ATOM   4810  C  CD1   . LEU   A  1  658  ? -36.370 82.672  112.832 1.00 25.10 ? 656  LEU   A CD1   1 
ATOM   4811  C  CD2   . LEU   A  1  658  ? -35.173 80.858  114.100 1.00 23.74 ? 656  LEU   A CD2   1 
ATOM   4812  N  N     . ILE   A  1  659  ? -35.372 79.932  109.209 1.00 20.32 ? 657  ILE   A N     1 
ATOM   4813  C  CA    . ILE   A  1  659  ? -34.322 80.139  108.217 1.00 19.86 ? 657  ILE   A CA    1 
ATOM   4814  C  C     . ILE   A  1  659  ? -34.880 80.811  106.971 1.00 20.54 ? 657  ILE   A C     1 
ATOM   4815  O  O     . ILE   A  1  659  ? -34.264 81.724  106.405 1.00 20.37 ? 657  ILE   A O     1 
ATOM   4816  C  CB    . ILE   A  1  659  ? -33.648 78.799  107.884 1.00 19.84 ? 657  ILE   A CB    1 
ATOM   4817  C  CG1   . ILE   A  1  659  ? -32.905 78.295  109.119 1.00 22.42 ? 657  ILE   A CG1   1 
ATOM   4818  C  CG2   . ILE   A  1  659  ? -32.713 78.952  106.703 1.00 21.11 ? 657  ILE   A CG2   1 
ATOM   4819  C  CD1   . ILE   A  1  659  ? -32.471 76.869  109.012 1.00 22.32 ? 657  ILE   A CD1   1 
ATOM   4820  N  N     . ILE   A  1  660  ? -36.053 80.363  106.525 1.00 19.19 ? 658  ILE   A N     1 
ATOM   4821  C  CA    . ILE   A  1  660  ? -36.679 80.940  105.338 1.00 20.96 ? 658  ILE   A CA    1 
ATOM   4822  C  C     . ILE   A  1  660  ? -36.879 82.438  105.520 1.00 21.38 ? 658  ILE   A C     1 
ATOM   4823  O  O     . ILE   A  1  660  ? -36.551 83.242  104.638 1.00 23.23 ? 658  ILE   A O     1 
ATOM   4824  C  CB    . ILE   A  1  660  ? -38.005 80.215  105.047 1.00 18.71 ? 658  ILE   A CB    1 
ATOM   4825  C  CG1   . ILE   A  1  660  ? -37.741 78.838  104.444 1.00 20.28 ? 658  ILE   A CG1   1 
ATOM   4826  C  CG2   . ILE   A  1  660  ? -38.894 81.041  104.126 1.00 21.26 ? 658  ILE   A CG2   1 
ATOM   4827  C  CD1   . ILE   A  1  660  ? -39.012 78.010  104.355 1.00 24.01 ? 658  ILE   A CD1   1 
ATOM   4828  N  N     . ARG   A  1  661  ? -37.393 82.834  106.681 1.00 20.79 ? 659  ARG   A N     1 
ATOM   4829  C  CA    . ARG   A  1  661  ? -37.746 84.228  106.885 1.00 22.12 ? 659  ARG   A CA    1 
ATOM   4830  C  C     . ARG   A  1  661  ? -36.558 85.079  107.308 1.00 25.81 ? 659  ARG   A C     1 
ATOM   4831  O  O     . ARG   A  1  661  ? -36.488 86.253  106.929 1.00 23.33 ? 659  ARG   A O     1 
ATOM   4832  C  CB    . ARG   A  1  661  ? -38.879 84.332  107.904 1.00 23.55 ? 659  ARG   A CB    1 
ATOM   4833  C  CG    . ARG   A  1  661  ? -40.204 83.887  107.314 1.00 22.34 ? 659  ARG   A CG    1 
ATOM   4834  C  CD    . ARG   A  1  661  ? -41.341 83.867  108.312 1.00 23.45 ? 659  ARG   A CD    1 
ATOM   4835  N  NE    . ARG   A  1  661  ? -41.591 85.169  108.915 1.00 25.32 ? 659  ARG   A NE    1 
ATOM   4836  C  CZ    . ARG   A  1  661  ? -41.555 85.409  110.219 1.00 24.42 ? 659  ARG   A CZ    1 
ATOM   4837  N  NH1   . ARG   A  1  661  ? -41.218 84.468  111.086 1.00 25.78 ? 659  ARG   A NH1   1 
ATOM   4838  N  NH2   . ARG   A  1  661  ? -41.880 86.617  110.666 1.00 25.38 ? 659  ARG   A NH2   1 
ATOM   4839  N  N     . GLU   A  1  662  ? -35.625 84.521  108.088 1.00 23.50 ? 660  GLU   A N     1 
ATOM   4840  C  CA    . GLU   A  1  662  ? -34.512 85.325  108.578 1.00 22.09 ? 660  GLU   A CA    1 
ATOM   4841  C  C     . GLU   A  1  662  ? -33.415 85.480  107.532 1.00 21.95 ? 660  GLU   A C     1 
ATOM   4842  O  O     . GLU   A  1  662  ? -32.816 86.553  107.420 1.00 23.93 ? 660  GLU   A O     1 
ATOM   4843  C  CB    . GLU   A  1  662  ? -33.939 84.726  109.864 1.00 25.26 ? 660  GLU   A CB    1 
ATOM   4844  C  CG    . GLU   A  1  662  ? -32.812 85.563  110.457 1.00 23.98 ? 660  GLU   A CG    1 
ATOM   4845  C  CD    . GLU   A  1  662  ? -32.279 85.012  111.762 1.00 24.38 ? 660  GLU   A CD    1 
ATOM   4846  O  OE1   . GLU   A  1  662  ? -32.313 83.778  111.947 1.00 24.07 ? 660  GLU   A OE1   1 
ATOM   4847  O  OE2   . GLU   A  1  662  ? -31.833 85.817  112.599 1.00 25.97 ? 660  GLU   A OE2   1 
ATOM   4848  N  N     . ALA   A  1  663  ? -33.155 84.437  106.744 1.00 21.74 ? 661  ALA   A N     1 
ATOM   4849  C  CA    . ALA   A  1  663  ? -31.960 84.387  105.907 1.00 20.53 ? 661  ALA   A CA    1 
ATOM   4850  C  C     . ALA   A  1  663  ? -32.253 84.370  104.412 1.00 21.83 ? 661  ALA   A C     1 
ATOM   4851  O  O     . ALA   A  1  663  ? -31.333 84.137  103.621 1.00 26.02 ? 661  ALA   A O     1 
ATOM   4852  C  CB    . ALA   A  1  663  ? -31.068 83.199  106.290 1.00 23.36 ? 661  ALA   A CB    1 
ATOM   4853  N  N     . GLY   A  1  664  ? -33.501 84.581  104.002 1.00 23.68 ? 662  GLY   A N     1 
ATOM   4854  C  CA    . GLY   A  1  664  ? -33.791 84.633  102.580 1.00 25.38 ? 662  GLY   A CA    1 
ATOM   4855  C  C     . GLY   A  1  664  ? -33.690 83.314  101.855 1.00 22.73 ? 662  GLY   A C     1 
ATOM   4856  O  O     . GLY   A  1  664  ? -33.474 83.299  100.641 1.00 26.52 ? 662  GLY   A O     1 
ATOM   4857  N  N     . LYS   A  1  665  ? -33.845 82.203  102.560 1.00 19.77 ? 663  LYS   A N     1 
ATOM   4858  C  CA    . LYS   A  1  665  ? -33.667 80.888  101.970 1.00 20.12 ? 663  LYS   A CA    1 
ATOM   4859  C  C     . LYS   A  1  665  ? -34.999 80.329  101.490 1.00 17.64 ? 663  LYS   A C     1 
ATOM   4860  O  O     . LYS   A  1  665  ? -36.044 80.550  102.098 1.00 19.33 ? 663  LYS   A O     1 
ATOM   4861  C  CB    . LYS   A  1  665  ? -33.087 79.926  103.004 1.00 21.71 ? 663  LYS   A CB    1 
ATOM   4862  C  CG    . LYS   A  1  665  ? -31.780 80.380  103.617 1.00 21.85 ? 663  LYS   A CG    1 
ATOM   4863  C  CD    . LYS   A  1  665  ? -30.717 80.592  102.561 1.00 24.85 ? 663  LYS   A CD    1 
ATOM   4864  C  CE    . LYS   A  1  665  ? -29.367 80.835  103.228 1.00 26.95 ? 663  LYS   A CE    1 
ATOM   4865  N  NZ    . LYS   A  1  665  ? -28.305 81.260  102.250 1.00 28.23 ? 663  LYS   A NZ    1 
ATOM   4866  N  N     . SER   A  1  666  ? -34.942 79.590  100.387 1.00 19.69 ? 664  SER   A N     1 
ATOM   4867  C  CA    . SER   A  1  666  ? -36.079 78.791  99.975  1.00 19.50 ? 664  SER   A CA    1 
ATOM   4868  C  C     . SER   A  1  666  ? -36.230 77.596  100.909 1.00 23.34 ? 664  SER   A C     1 
ATOM   4869  O  O     . SER   A  1  666  ? -35.332 77.262  101.688 1.00 20.81 ? 664  SER   A O     1 
ATOM   4870  C  CB    . SER   A  1  666  ? -35.847 78.257  98.569  1.00 22.34 ? 664  SER   A CB    1 
ATOM   4871  O  OG    . SER   A  1  666  ? -34.832 77.268  98.601  1.00 23.62 ? 664  SER   A OG    1 
ATOM   4872  N  N     . ALA   A  1  667  ? -37.390 76.946  100.832 1.00 22.33 ? 665  ALA   A N     1 
ATOM   4873  C  CA    . ALA   A  1  667  ? -37.625 75.762  101.652 1.00 20.36 ? 665  ALA   A CA    1 
ATOM   4874  C  C     . ALA   A  1  667  ? -36.596 74.673  101.363 1.00 21.60 ? 665  ALA   A C     1 
ATOM   4875  O  O     . ALA   A  1  667  ? -36.041 74.079  102.293 1.00 19.83 ? 665  ALA   A O     1 
ATOM   4876  C  CB    . ALA   A  1  667  ? -39.048 75.239  101.442 1.00 22.31 ? 665  ALA   A CB    1 
ATOM   4877  N  N     . LEU   A  1  668  ? -36.338 74.384  100.082 1.00 20.87 ? 666  LEU   A N     1 
ATOM   4878  C  CA    . LEU   A  1  668  ? -35.333 73.382  99.735  1.00 22.75 ? 666  LEU   A CA    1 
ATOM   4879  C  C     . LEU   A  1  668  ? -33.995 73.720  100.365 1.00 22.66 ? 666  LEU   A C     1 
ATOM   4880  O  O     . LEU   A  1  668  ? -33.321 72.846  100.925 1.00 21.84 ? 666  LEU   A O     1 
ATOM   4881  C  CB    . LEU   A  1  668  ? -35.161 73.298  98.218  1.00 25.11 ? 666  LEU   A CB    1 
ATOM   4882  C  CG    . LEU   A  1  668  ? -36.122 72.406  97.453  1.00 31.89 ? 666  LEU   A CG    1 
ATOM   4883  C  CD1   . LEU   A  1  668  ? -35.815 72.518  95.969  1.00 28.23 ? 666  LEU   A CD1   1 
ATOM   4884  C  CD2   . LEU   A  1  668  ? -35.965 70.979  97.934  1.00 33.09 ? 666  LEU   A CD2   1 
ATOM   4885  N  N     . ASN   A  1  669  ? -33.595 74.986  100.294 1.00 19.92 ? 667  ASN   A N     1 
ATOM   4886  C  CA    . ASN   A  1  669  ? -32.293 75.349  100.834 1.00 20.53 ? 667  ASN   A CA    1 
ATOM   4887  C  C     . ASN   A  1  669  ? -32.288 75.317  102.353 1.00 19.86 ? 667  ASN   A C     1 
ATOM   4888  O  O     . ASN   A  1  669  ? -31.267 74.973  102.957 1.00 21.63 ? 667  ASN   A O     1 
ATOM   4889  C  CB    . ASN   A  1  669  ? -31.865 76.710  100.301 1.00 24.42 ? 667  ASN   A CB    1 
ATOM   4890  C  CG    . ASN   A  1  669  ? -31.574 76.674  98.805  1.00 26.96 ? 667  ASN   A CG    1 
ATOM   4891  O  OD1   . ASN   A  1  669  ? -31.811 77.644  98.097  1.00 33.81 ? 667  ASN   A OD1   1 
ATOM   4892  N  ND2   . ASN   A  1  669  ? -31.065 75.543  98.325  1.00 32.94 ? 667  ASN   A ND2   1 
ATOM   4893  N  N     . ALA   A  1  670  ? -33.410 75.650  102.981 1.00 18.83 ? 668  ALA   A N     1 
ATOM   4894  C  CA    . ALA   A  1  670  ? -33.486 75.564  104.429 1.00 19.28 ? 668  ALA   A CA    1 
ATOM   4895  C  C     . ALA   A  1  670  ? -33.433 74.115  104.891 1.00 19.69 ? 668  ALA   A C     1 
ATOM   4896  O  O     . ALA   A  1  670  ? -32.830 73.811  105.926 1.00 20.15 ? 668  ALA   A O     1 
ATOM   4897  C  CB    . ALA   A  1  670  ? -34.763 76.246  104.912 1.00 19.89 ? 668  ALA   A CB    1 
ATOM   4898  N  N     . ILE   A  1  671  ? -34.069 73.206  104.152 1.00 18.84 ? 669  ILE   A N     1 
ATOM   4899  C  CA    . ILE   A  1  671  ? -33.966 71.788  104.485 1.00 19.57 ? 669  ILE   A CA    1 
ATOM   4900  C  C     . ILE   A  1  671  ? -32.515 71.350  104.446 1.00 20.57 ? 669  ILE   A C     1 
ATOM   4901  O  O     . ILE   A  1  671  ? -32.018 70.700  105.373 1.00 20.85 ? 669  ILE   A O     1 
ATOM   4902  C  CB    . ILE   A  1  671  ? -34.813 70.945  103.519 1.00 20.47 ? 669  ILE   A CB    1 
ATOM   4903  C  CG1   . ILE   A  1  671  ? -36.296 71.197  103.746 1.00 20.17 ? 669  ILE   A CG1   1 
ATOM   4904  C  CG2   . ILE   A  1  671  ? -34.478 69.472  103.687 1.00 23.70 ? 669  ILE   A CG2   1 
ATOM   4905  C  CD1   . ILE   A  1  671  ? -37.158 70.671  102.606 1.00 22.55 ? 669  ILE   A CD1   1 
ATOM   4906  N  N     . ALA   A  1  672  ? -31.820 71.688  103.357 1.00 18.62 ? 670  ALA   A N     1 
ATOM   4907  C  CA    . ALA   A  1  672  ? -30.413 71.337  103.237 1.00 19.19 ? 670  ALA   A CA    1 
ATOM   4908  C  C     . ALA   A  1  672  ? -29.604 71.941  104.373 1.00 18.96 ? 670  ALA   A C     1 
ATOM   4909  O  O     . ALA   A  1  672  ? -28.687 71.301  104.894 1.00 19.56 ? 670  ALA   A O     1 
ATOM   4910  C  CB    . ALA   A  1  672  ? -29.873 71.817  101.892 1.00 20.18 ? 670  ALA   A CB    1 
ATOM   4911  N  N     . GLU   A  1  673  ? -29.945 73.165  104.780 1.00 18.20 ? 671  GLU   A N     1 
ATOM   4912  C  CA    . GLU   A  1  673  ? -29.235 73.839  105.861 1.00 18.56 ? 671  GLU   A CA    1 
ATOM   4913  C  C     . GLU   A  1  673  ? -29.386 73.078  107.172 1.00 20.86 ? 671  GLU   A C     1 
ATOM   4914  O  O     . GLU   A  1  673  ? -28.406 72.837  107.886 1.00 18.79 ? 671  GLU   A O     1 
ATOM   4915  C  CB    . GLU   A  1  673  ? -29.792 75.253  106.008 1.00 20.19 ? 671  GLU   A CB    1 
ATOM   4916  C  CG    . GLU   A  1  673  ? -29.201 76.048  107.149 1.00 24.63 ? 671  GLU   A CG    1 
ATOM   4917  C  CD    . GLU   A  1  673  ? -27.904 76.695  106.761 1.00 24.78 ? 671  GLU   A CD    1 
ATOM   4918  O  OE1   . GLU   A  1  673  ? -27.545 76.662  105.560 1.00 28.31 ? 671  GLU   A OE1   1 
ATOM   4919  O  OE2   . GLU   A  1  673  ? -27.237 77.237  107.657 1.00 22.80 ? 671  GLU   A OE2   1 
ATOM   4920  N  N     . VAL   A  1  674  ? -30.615 72.685  107.505 1.00 18.71 ? 672  VAL   A N     1 
ATOM   4921  C  CA    . VAL   A  1  674  ? -30.850 71.950  108.742 1.00 18.09 ? 672  VAL   A CA    1 
ATOM   4922  C  C     . VAL   A  1  674  ? -30.229 70.562  108.674 1.00 18.42 ? 672  VAL   A C     1 
ATOM   4923  O  O     . VAL   A  1  674  ? -29.624 70.091  109.647 1.00 17.48 ? 672  VAL   A O     1 
ATOM   4924  C  CB    . VAL   A  1  674  ? -32.351 71.904  109.081 1.00 18.16 ? 672  VAL   A CB    1 
ATOM   4925  C  CG1   . VAL   A  1  674  ? -32.565 71.160  110.381 1.00 19.15 ? 672  VAL   A CG1   1 
ATOM   4926  C  CG2   . VAL   A  1  674  ? -32.932 73.317  109.186 1.00 20.31 ? 672  VAL   A CG2   1 
ATOM   4927  N  N     . ARG   A  1  675  ? -30.363 69.883  107.534 1.00 17.95 ? 673  ARG   A N     1 
ATOM   4928  C  CA    . ARG   A  1  675  ? -29.701 68.595  107.387 1.00 17.85 ? 673  ARG   A CA    1 
ATOM   4929  C  C     . ARG   A  1  675  ? -28.212 68.725  107.626 1.00 17.01 ? 673  ARG   A C     1 
ATOM   4930  O  O     . ARG   A  1  675  ? -27.621 67.884  108.304 1.00 17.93 ? 673  ARG   A O     1 
ATOM   4931  C  CB    . ARG   A  1  675  ? -29.947 68.012  106.004 1.00 16.13 ? 673  ARG   A CB    1 
ATOM   4932  C  CG    . ARG   A  1  675  ? -31.369 67.557  105.787 1.00 17.40 ? 673  ARG   A CG    1 
ATOM   4933  C  CD    . ARG   A  1  675  ? -31.434 66.770  104.505 1.00 18.64 ? 673  ARG   A CD    1 
ATOM   4934  N  NE    . ARG   A  1  675  ? -30.662 65.538  104.620 1.00 18.28 ? 673  ARG   A NE    1 
ATOM   4935  C  CZ    . ARG   A  1  675  ? -30.283 64.794  103.593 1.00 17.43 ? 673  ARG   A CZ    1 
ATOM   4936  N  NH1   . ARG   A  1  675  ? -30.542 65.156  102.350 1.00 17.64 ? 673  ARG   A NH1   1 
ATOM   4937  N  NH2   . ARG   A  1  675  ? -29.651 63.646  103.823 1.00 16.92 ? 673  ARG   A NH2   1 
ATOM   4938  N  N     . GLU   A  1  676  ? -27.589 69.773  107.082 1.00 17.34 ? 674  GLU   A N     1 
ATOM   4939  C  CA    . GLU   A  1  676  ? -26.152 69.927  107.261 1.00 17.19 ? 674  GLU   A CA    1 
ATOM   4940  C  C     . GLU   A  1  676  ? -25.807 70.113  108.727 1.00 18.00 ? 674  GLU   A C     1 
ATOM   4941  O  O     . GLU   A  1  676  ? -24.799 69.583  109.207 1.00 17.69 ? 674  GLU   A O     1 
ATOM   4942  C  CB    . GLU   A  1  676  ? -25.621 71.089  106.429 1.00 16.57 ? 674  GLU   A CB    1 
ATOM   4943  C  CG    . GLU   A  1  676  ? -24.108 71.147  106.422 1.00 21.90 ? 674  GLU   A CG    1 
ATOM   4944  C  CD    . GLU   A  1  676  ? -23.542 71.962  105.277 1.00 34.70 ? 674  GLU   A CD    1 
ATOM   4945  O  OE1   . GLU   A  1  676  ? -24.289 72.776  104.690 1.00 46.76 ? 674  GLU   A OE1   1 
ATOM   4946  O  OE2   . GLU   A  1  676  ? -22.347 71.772  104.957 1.00 43.09 ? 674  GLU   A OE2   1 
ATOM   4947  N  N     . ALA   A  1  677  ? -26.632 70.858  109.458 1.00 17.68 ? 675  ALA   A N     1 
ATOM   4948  C  CA    . ALA   A  1  677  ? -26.365 71.038  110.880 1.00 15.84 ? 675  ALA   A CA    1 
ATOM   4949  C  C     . ALA   A  1  677  ? -26.438 69.709  111.614 1.00 18.62 ? 675  ALA   A C     1 
ATOM   4950  O  O     . ALA   A  1  677  ? -25.576 69.391  112.443 1.00 18.12 ? 675  ALA   A O     1 
ATOM   4951  C  CB    . ALA   A  1  677  ? -27.354 72.047  111.468 1.00 17.67 ? 675  ALA   A CB    1 
ATOM   4952  N  N     . ILE   A  1  678  ? -27.478 68.924  111.327 1.00 17.43 ? 676  ILE   A N     1 
ATOM   4953  C  CA    . ILE   A  1  678  ? -27.631 67.603  111.918 1.00 17.66 ? 676  ILE   A CA    1 
ATOM   4954  C  C     . ILE   A  1  678  ? -26.428 66.738  111.585 1.00 17.77 ? 676  ILE   A C     1 
ATOM   4955  O  O     . ILE   A  1  678  ? -25.904 66.013  112.440 1.00 19.07 ? 676  ILE   A O     1 
ATOM   4956  C  CB    . ILE   A  1  678  ? -28.940 66.975  111.402 1.00 18.00 ? 676  ILE   A CB    1 
ATOM   4957  C  CG1   . ILE   A  1  678  ? -30.141 67.767  111.925 1.00 19.17 ? 676  ILE   A CG1   1 
ATOM   4958  C  CG2   . ILE   A  1  678  ? -29.037 65.512  111.771 1.00 19.21 ? 676  ILE   A CG2   1 
ATOM   4959  C  CD1   . ILE   A  1  678  ? -31.435 67.462  111.187 1.00 18.49 ? 676  ILE   A CD1   1 
ATOM   4960  N  N     . ASP   A  1  679  ? -25.991 66.793  110.329 1.00 17.26 ? 677  ASP   A N     1 
ATOM   4961  C  CA    . ASP   A  1  679  ? -24.866 65.980  109.888 1.00 16.81 ? 677  ASP   A CA    1 
ATOM   4962  C  C     . ASP   A  1  679  ? -23.571 66.397  110.573 1.00 18.12 ? 677  ASP   A C     1 
ATOM   4963  O  O     . ASP   A  1  679  ? -22.784 65.537  110.972 1.00 17.57 ? 677  ASP   A O     1 
ATOM   4964  C  CB    . ASP   A  1  679  ? -24.728 66.070  108.368 1.00 16.52 ? 677  ASP   A CB    1 
ATOM   4965  C  CG    . ASP   A  1  679  ? -25.867 65.403  107.638 1.00 19.48 ? 677  ASP   A CG    1 
ATOM   4966  O  OD1   . ASP   A  1  679  ? -26.470 64.471  108.193 1.00 20.58 ? 677  ASP   A OD1   1 
ATOM   4967  O  OD2   . ASP   A  1  679  ? -26.124 65.780  106.482 1.00 22.28 ? 677  ASP   A OD2   1 
ATOM   4968  N  N     . PHE   A  1  680  ? -23.324 67.704  110.706 1.00 16.88 ? 678  PHE   A N     1 
ATOM   4969  C  CA    . PHE   A  1  680  ? -22.165 68.158  111.477 1.00 16.43 ? 678  PHE   A CA    1 
ATOM   4970  C  C     . PHE   A  1  680  ? -22.189 67.594  112.891 1.00 17.71 ? 678  PHE   A C     1 
ATOM   4971  O  O     . PHE   A  1  680  ? -21.183 67.081  113.391 1.00 17.90 ? 678  PHE   A O     1 
ATOM   4972  C  CB    . PHE   A  1  680  ? -22.143 69.679  111.570 1.00 16.70 ? 678  PHE   A CB    1 
ATOM   4973  C  CG    . PHE   A  1  680  ? -21.507 70.363  110.410 1.00 18.42 ? 678  PHE   A CG    1 
ATOM   4974  C  CD1   . PHE   A  1  680  ? -20.286 69.947  109.907 1.00 16.73 ? 678  PHE   A CD1   1 
ATOM   4975  C  CD2   . PHE   A  1  680  ? -22.136 71.448  109.825 1.00 18.93 ? 678  PHE   A CD2   1 
ATOM   4976  C  CE1   . PHE   A  1  680  ? -19.702 70.610  108.841 1.00 17.88 ? 678  PHE   A CE1   1 
ATOM   4977  C  CE2   . PHE   A  1  680  ? -21.566 72.107  108.763 1.00 18.18 ? 678  PHE   A CE2   1 
ATOM   4978  C  CZ    . PHE   A  1  680  ? -20.350 71.688  108.260 1.00 18.49 ? 678  PHE   A CZ    1 
ATOM   4979  N  N     . LEU   A  1  681  ? -23.325 67.722  113.571 1.00 17.10 ? 679  LEU   A N     1 
ATOM   4980  C  CA    . LEU   A  1  681  ? -23.418 67.224  114.935 1.00 16.98 ? 679  LEU   A CA    1 
ATOM   4981  C  C     . LEU   A  1  681  ? -23.089 65.743  114.996 1.00 18.61 ? 679  LEU   A C     1 
ATOM   4982  O  O     . LEU   A  1  681  ? -22.277 65.305  115.822 1.00 17.48 ? 679  LEU   A O     1 
ATOM   4983  C  CB    . LEU   A  1  681  ? -24.824 67.480  115.471 1.00 18.86 ? 679  LEU   A CB    1 
ATOM   4984  C  CG    . LEU   A  1  681  ? -25.143 68.956  115.716 1.00 19.26 ? 679  LEU   A CG    1 
ATOM   4985  C  CD1   . LEU   A  1  681  ? -26.646 69.191  115.794 1.00 19.29 ? 679  LEU   A CD1   1 
ATOM   4986  C  CD2   . LEU   A  1  681  ? -24.459 69.440  116.985 1.00 20.57 ? 679  LEU   A CD2   1 
ATOM   4987  N  N     . ARG   A  1  682  ? -23.704 64.951  114.119 1.00 16.98 ? 680  ARG   A N     1 
ATOM   4988  C  CA    . ARG   A  1  682  ? -23.497 63.511  114.185 1.00 18.53 ? 680  ARG   A CA    1 
ATOM   4989  C  C     . ARG   A  1  682  ? -22.112 63.125  113.705 1.00 17.64 ? 680  ARG   A C     1 
ATOM   4990  O  O     . ARG   A  1  682  ? -21.530 62.173  114.228 1.00 17.83 ? 680  ARG   A O     1 
ATOM   4991  C  CB    . ARG   A  1  682  ? -24.562 62.788  113.374 1.00 17.55 ? 680  ARG   A CB    1 
ATOM   4992  C  CG    . ARG   A  1  682  ? -25.918 62.873  114.018 1.00 19.52 ? 680  ARG   A CG    1 
ATOM   4993  C  CD    . ARG   A  1  682  ? -26.948 62.254  113.133 1.00 19.55 ? 680  ARG   A CD    1 
ATOM   4994  N  NE    . ARG   A  1  682  ? -28.241 62.275  113.795 1.00 20.39 ? 680  ARG   A NE    1 
ATOM   4995  C  CZ    . ARG   A  1  682  ? -29.393 62.085  113.173 1.00 22.93 ? 680  ARG   A CZ    1 
ATOM   4996  N  NH1   . ARG   A  1  682  ? -29.445 61.854  111.875 1.00 22.31 ? 680  ARG   A NH1   1 
ATOM   4997  N  NH2   . ARG   A  1  682  ? -30.522 62.128  113.876 1.00 24.54 ? 680  ARG   A NH2   1 
ATOM   4998  N  N     . TYR   A  1  683  ? -21.573 63.861  112.737 1.00 17.39 ? 681  TYR   A N     1 
ATOM   4999  C  CA    . TYR   A  1  683  ? -20.246 63.543  112.227 1.00 16.32 ? 681  TYR   A CA    1 
ATOM   5000  C  C     . TYR   A  1  683  ? -19.188 63.838  113.273 1.00 19.32 ? 681  TYR   A C     1 
ATOM   5001  O  O     . TYR   A  1  683  ? -18.321 62.998  113.544 1.00 17.67 ? 681  TYR   A O     1 
ATOM   5002  C  CB    . TYR   A  1  683  ? -19.977 64.343  110.959 1.00 17.34 ? 681  TYR   A CB    1 
ATOM   5003  C  CG    . TYR   A  1  683  ? -18.597 64.112  110.406 1.00 16.29 ? 681  TYR   A CG    1 
ATOM   5004  C  CD1   . TYR   A  1  683  ? -18.298 62.953  109.702 1.00 16.79 ? 681  TYR   A CD1   1 
ATOM   5005  C  CD2   . TYR   A  1  683  ? -17.594 65.049  110.586 1.00 16.93 ? 681  TYR   A CD2   1 
ATOM   5006  C  CE1   . TYR   A  1  683  ? -17.033 62.729  109.208 1.00 17.57 ? 681  TYR   A CE1   1 
ATOM   5007  C  CE2   . TYR   A  1  683  ? -16.334 64.840  110.107 1.00 16.74 ? 681  TYR   A CE2   1 
ATOM   5008  C  CZ    . TYR   A  1  683  ? -16.059 63.685  109.404 1.00 17.41 ? 681  TYR   A CZ    1 
ATOM   5009  O  OH    . TYR   A  1  683  ? -14.786 63.481  108.921 1.00 18.03 ? 681  TYR   A OH    1 
ATOM   5010  N  N     . TYR   A  1  684  ? -19.245 65.021  113.887 1.00 17.27 ? 682  TYR   A N     1 
ATOM   5011  C  CA    . TYR   A  1  684  ? -18.233 65.333  114.889 1.00 17.07 ? 682  TYR   A CA    1 
ATOM   5012  C  C     . TYR   A  1  684  ? -18.395 64.458  116.121 1.00 20.13 ? 682  TYR   A C     1 
ATOM   5013  O  O     . TYR   A  1  684  ? -17.403 64.112  116.764 1.00 18.73 ? 682  TYR   A O     1 
ATOM   5014  C  CB    . TYR   A  1  684  ? -18.235 66.815  115.264 1.00 17.49 ? 682  TYR   A CB    1 
ATOM   5015  C  CG    . TYR   A  1  684  ? -17.867 67.720  114.115 1.00 16.81 ? 682  TYR   A CG    1 
ATOM   5016  C  CD1   . TYR   A  1  684  ? -16.808 67.413  113.275 1.00 16.46 ? 682  TYR   A CD1   1 
ATOM   5017  C  CD2   . TYR   A  1  684  ? -18.580 68.881  113.866 1.00 17.90 ? 682  TYR   A CD2   1 
ATOM   5018  C  CE1   . TYR   A  1  684  ? -16.480 68.238  112.211 1.00 17.56 ? 682  TYR   A CE1   1 
ATOM   5019  C  CE2   . TYR   A  1  684  ? -18.258 69.711  112.814 1.00 16.97 ? 682  TYR   A CE2   1 
ATOM   5020  C  CZ    . TYR   A  1  684  ? -17.210 69.387  111.983 1.00 17.42 ? 682  TYR   A CZ    1 
ATOM   5021  O  OH    . TYR   A  1  684  ? -16.887 70.216  110.938 1.00 17.48 ? 682  TYR   A OH    1 
ATOM   5022  N  N     . ALA   A  1  685  ? -19.626 64.076  116.458 1.00 17.51 ? 683  ALA   A N     1 
ATOM   5023  C  CA    . ALA   A  1  685  ? -19.818 63.102  117.521 1.00 19.19 ? 683  ALA   A CA    1 
ATOM   5024  C  C     . ALA   A  1  685  ? -19.114 61.792  117.192 1.00 19.05 ? 683  ALA   A C     1 
ATOM   5025  O  O     . ALA   A  1  685  ? -18.410 61.227  118.034 1.00 18.83 ? 683  ALA   A O     1 
ATOM   5026  C  CB    . ALA   A  1  685  ? -21.311 62.876  117.773 1.00 18.92 ? 683  ALA   A CB    1 
ATOM   5027  N  N     . GLU   A  1  686  ? -19.313 61.283  115.976 1.00 18.73 ? 684  GLU   A N     1 
ATOM   5028  C  CA    . GLU   A  1  686  ? -18.687 60.017  115.614 1.00 19.24 ? 684  GLU   A CA    1 
ATOM   5029  C  C     . GLU   A  1  686  ? -17.176 60.152  115.548 1.00 17.66 ? 684  GLU   A C     1 
ATOM   5030  O  O     . GLU   A  1  686  ? -16.453 59.280  116.040 1.00 19.66 ? 684  GLU   A O     1 
ATOM   5031  C  CB    . GLU   A  1  686  ? -19.257 59.486  114.300 1.00 21.73 ? 684  GLU   A CB    1 
ATOM   5032  C  CG    . GLU   A  1  686  ? -18.548 58.230  113.784 1.00 24.49 ? 684  GLU   A CG    1 
ATOM   5033  C  CD    . GLU   A  1  686  ? -18.621 57.037  114.733 1.00 27.36 ? 684  GLU   A CD    1 
ATOM   5034  O  OE1   . GLU   A  1  686  ? -19.458 57.024  115.672 1.00 27.12 ? 684  GLU   A OE1   1 
ATOM   5035  O  OE2   . GLU   A  1  686  ? -17.834 56.086  114.527 1.00 31.73 ? 684  GLU   A OE2   1 
ATOM   5036  N  N     . GLN   A  1  687  ? -16.681 61.244  114.959 1.00 17.02 ? 685  GLN   A N     1 
ATOM   5037  C  CA    . GLN   A  1  687  ? -15.237 61.437  114.893 1.00 17.52 ? 685  GLN   A CA    1 
ATOM   5038  C  C     . GLN   A  1  687  ? -14.643 61.507  116.288 1.00 19.19 ? 685  GLN   A C     1 
ATOM   5039  O  O     . GLN   A  1  687  ? -13.523 61.039  116.521 1.00 18.83 ? 685  GLN   A O     1 
ATOM   5040  C  CB    . GLN   A  1  687  ? -14.910 62.708  114.120 1.00 16.69 ? 685  GLN   A CB    1 
ATOM   5041  C  CG    . GLN   A  1  687  ? -15.233 62.595  112.637 1.00 17.04 ? 685  GLN   A CG    1 
ATOM   5042  C  CD    . GLN   A  1  687  ? -14.495 61.441  111.986 1.00 21.59 ? 685  GLN   A CD    1 
ATOM   5043  O  OE1   . GLN   A  1  687  ? -13.274 61.367  112.059 1.00 20.42 ? 685  GLN   A OE1   1 
ATOM   5044  N  NE2   . GLN   A  1  687  ? -15.232 60.539  111.346 1.00 24.53 ? 685  GLN   A NE2   1 
ATOM   5045  N  N     . THR   A  1  688  ? -15.374 62.094  117.227 1.00 18.27 ? 686  THR   A N     1 
ATOM   5046  C  CA    . THR   A  1  688  ? -14.913 62.121  118.605 1.00 16.50 ? 686  THR   A CA    1 
ATOM   5047  C  C     . THR   A  1  688  ? -14.810 60.715  119.171 1.00 20.53 ? 686  THR   A C     1 
ATOM   5048  O  O     . THR   A  1  688  ? -13.796 60.351  119.781 1.00 20.39 ? 686  THR   A O     1 
ATOM   5049  C  CB    . THR   A  1  688  ? -15.876 62.961  119.440 1.00 19.37 ? 686  THR   A CB    1 
ATOM   5050  O  OG1   . THR   A  1  688  ? -15.736 64.324  119.048 1.00 19.68 ? 686  THR   A OG1   1 
ATOM   5051  C  CG2   . THR   A  1  688  ? -15.527 62.846  120.910 1.00 18.85 ? 686  THR   A CG2   1 
ATOM   5052  N  N     . ARG   A  1  689  ? -15.860 59.914  118.988 1.00 19.42 ? 687  ARG   A N     1 
ATOM   5053  C  CA    . ARG   A  1  689  ? -15.858 58.551  119.504 1.00 21.20 ? 687  ARG   A CA    1 
ATOM   5054  C  C     . ARG   A  1  689  ? -14.753 57.722  118.877 1.00 20.56 ? 687  ARG   A C     1 
ATOM   5055  O  O     . ARG   A  1  689  ? -14.301 56.741  119.475 1.00 23.01 ? 687  ARG   A O     1 
ATOM   5056  C  CB    . ARG   A  1  689  ? -17.209 57.887  119.251 1.00 21.19 ? 687  ARG   A CB    1 
ATOM   5057  C  CG    . ARG   A  1  689  ? -18.330 58.436  120.119 1.00 24.37 ? 687  ARG   A CG    1 
ATOM   5058  C  CD    . ARG   A  1  689  ? -19.586 57.612  119.942 1.00 25.08 ? 687  ARG   A CD    1 
ATOM   5059  N  NE    . ARG   A  1  689  ? -20.128 57.727  118.596 1.00 25.97 ? 687  ARG   A NE    1 
ATOM   5060  C  CZ    . ARG   A  1  689  ? -21.112 58.550  118.256 1.00 25.74 ? 687  ARG   A CZ    1 
ATOM   5061  N  NH1   . ARG   A  1  689  ? -21.675 59.353  119.146 1.00 26.89 ? 687  ARG   A NH1   1 
ATOM   5062  N  NH2   . ARG   A  1  689  ? -21.541 58.563  116.999 1.00 24.43 ? 687  ARG   A NH2   1 
ATOM   5063  N  N     . ARG   A  1  690  ? -14.314 58.093  117.678 1.00 18.94 ? 688  ARG   A N     1 
ATOM   5064  C  CA    . ARG   A  1  690  ? -13.215 57.387  117.039 1.00 19.85 ? 688  ARG   A CA    1 
ATOM   5065  C  C     . ARG   A  1  690  ? -11.849 57.830  117.538 1.00 21.44 ? 688  ARG   A C     1 
ATOM   5066  O  O     . ARG   A  1  690  ? -10.878 57.090  117.354 1.00 20.78 ? 688  ARG   A O     1 
ATOM   5067  C  CB    . ARG   A  1  690  ? -13.257 57.610  115.525 1.00 19.20 ? 688  ARG   A CB    1 
ATOM   5068  C  CG    . ARG   A  1  690  ? -14.467 56.998  114.825 1.00 21.90 ? 688  ARG   A CG    1 
ATOM   5069  C  CD    . ARG   A  1  690  ? -14.377 55.483  114.721 1.00 23.00 ? 688  ARG   A CD    1 
ATOM   5070  N  NE    . ARG   A  1  690  ? -13.198 55.055  113.972 1.00 23.31 ? 688  ARG   A NE    1 
ATOM   5071  C  CZ    . ARG   A  1  690  ? -12.163 54.422  114.505 1.00 29.14 ? 688  ARG   A CZ    1 
ATOM   5072  N  NH1   . ARG   A  1  690  ? -12.135 54.102  115.789 1.00 25.67 ? 688  ARG   A NH1   1 
ATOM   5073  N  NH2   . ARG   A  1  690  ? -11.132 54.099  113.729 1.00 23.34 ? 688  ARG   A NH2   1 
ATOM   5074  N  N     . THR   A  1  691  ? -11.732 59.014  118.148 1.00 18.53 ? 689  THR   A N     1 
ATOM   5075  C  CA    . THR   A  1  691  ? -10.393 59.572  118.323 1.00 18.85 ? 689  THR   A CA    1 
ATOM   5076  C  C     . THR   A  1  691  ? -10.035 60.065  119.715 1.00 23.03 ? 689  THR   A C     1 
ATOM   5077  O  O     . THR   A  1  691  ? -8.947  59.760  120.212 1.00 24.29 ? 689  THR   A O     1 
ATOM   5078  C  CB    . THR   A  1  691  ? -10.143 60.720  117.342 1.00 18.68 ? 689  THR   A CB    1 
ATOM   5079  O  OG1   . THR   A  1  691  ? -11.146 61.733  117.511 1.00 19.93 ? 689  THR   A OG1   1 
ATOM   5080  C  CG2   . THR   A  1  691  ? -10.178 60.219  115.905 1.00 20.99 ? 689  THR   A CG2   1 
ATOM   5081  N  N     . LEU   A  1  692  ? -10.904 60.842  120.355 1.00 20.10 ? 690  LEU   A N     1 
ATOM   5082  C  CA    . LEU   A  1  692  ? -10.442 61.674  121.460 1.00 22.45 ? 690  LEU   A CA    1 
ATOM   5083  C  C     . LEU   A  1  692  ? -10.233 60.873  122.743 1.00 23.46 ? 690  LEU   A C     1 
ATOM   5084  O  O     . LEU   A  1  692  ? -11.113 60.124  123.180 1.00 25.11 ? 690  LEU   A O     1 
ATOM   5085  C  CB    . LEU   A  1  692  ? -11.393 62.847  121.678 1.00 22.18 ? 690  LEU   A CB    1 
ATOM   5086  C  CG    . LEU   A  1  692  ? -11.425 63.866  120.535 1.00 23.64 ? 690  LEU   A CG    1 
ATOM   5087  C  CD1   . LEU   A  1  692  ? -12.176 65.120  120.954 1.00 25.86 ? 690  LEU   A CD1   1 
ATOM   5088  C  CD2   . LEU   A  1  692  ? -10.029 64.219  120.074 1.00 23.51 ? 690  LEU   A CD2   1 
ATOM   5089  N  N     . GLY   A  1  693  ? -9.058  61.039  123.337 1.00 23.30 ? 691  GLY   A N     1 
ATOM   5090  C  CA    . GLY   A  1  693  ? -8.715  60.404  124.585 1.00 25.54 ? 691  GLY   A CA    1 
ATOM   5091  C  C     . GLY   A  1  693  ? -8.125  61.406  125.552 1.00 28.02 ? 691  GLY   A C     1 
ATOM   5092  O  O     . GLY   A  1  693  ? -8.066  62.610  125.279 1.00 27.58 ? 691  GLY   A O     1 
ATOM   5093  N  N     . PRO   A  1  694  ? -7.661  60.916  126.702 1.00 27.69 ? 692  PRO   A N     1 
ATOM   5094  C  CA    . PRO   A  1  694  ? -7.183  61.827  127.758 1.00 29.18 ? 692  PRO   A CA    1 
ATOM   5095  C  C     . PRO   A  1  694  ? -6.030  62.721  127.335 1.00 29.59 ? 692  PRO   A C     1 
ATOM   5096  O  O     . PRO   A  1  694  ? -5.914  63.846  127.836 1.00 35.42 ? 692  PRO   A O     1 
ATOM   5097  C  CB    . PRO   A  1  694  ? -6.775  60.870  128.887 1.00 35.52 ? 692  PRO   A CB    1 
ATOM   5098  C  CG    . PRO   A  1  694  ? -7.569  59.622  128.639 1.00 31.39 ? 692  PRO   A CG    1 
ATOM   5099  C  CD    . PRO   A  1  694  ? -7.715  59.512  127.144 1.00 28.92 ? 692  PRO   A CD    1 
ATOM   5100  N  N     . GLY   A  1  695  ? -5.172  62.260  126.428 1.00 26.89 ? 693  GLY   A N     1 
ATOM   5101  C  CA    . GLY   A  1  695  ? -4.029  63.045  126.012 1.00 30.96 ? 693  GLY   A CA    1 
ATOM   5102  C  C     . GLY   A  1  695  ? -4.313  64.111  124.981 1.00 29.46 ? 693  GLY   A C     1 
ATOM   5103  O  O     . GLY   A  1  695  ? -3.405  64.867  124.627 1.00 30.30 ? 693  GLY   A O     1 
ATOM   5104  N  N     . HIS   A  1  696  ? -5.545  64.194  124.477 1.00 28.53 ? 694  HIS   A N     1 
ATOM   5105  C  CA    . HIS   A  1  696  ? -5.900  65.222  123.503 1.00 24.99 ? 694  HIS   A CA    1 
ATOM   5106  C  C     . HIS   A  1  696  ? -6.630  66.317  124.270 1.00 29.25 ? 694  HIS   A C     1 
ATOM   5107  O  O     . HIS   A  1  696  ? -7.859  66.385  124.313 1.00 30.10 ? 694  HIS   A O     1 
ATOM   5108  C  CB    . HIS   A  1  696  ? -6.723  64.630  122.364 1.00 27.77 ? 694  HIS   A CB    1 
ATOM   5109  C  CG    . HIS   A  1  696  ? -6.156  63.355  121.822 1.00 22.16 ? 694  HIS   A CG    1 
ATOM   5110  N  ND1   . HIS   A  1  696  ? -6.811  62.148  121.927 1.00 24.63 ? 694  HIS   A ND1   1 
ATOM   5111  C  CD2   . HIS   A  1  696  ? -4.974  63.094  121.214 1.00 23.27 ? 694  HIS   A CD2   1 
ATOM   5112  C  CE1   . HIS   A  1  696  ? -6.070  61.201  121.379 1.00 22.94 ? 694  HIS   A CE1   1 
ATOM   5113  N  NE2   . HIS   A  1  696  ? -4.948  61.748  120.947 1.00 25.16 ? 694  HIS   A NE2   1 
ATOM   5114  N  N     . GLY   A  1  697  ? -5.841  67.162  124.922 1.00 27.93 ? 695  GLY   A N     1 
ATOM   5115  C  CA    . GLY   A  1  697  ? -6.383  68.190  125.774 1.00 29.30 ? 695  GLY   A CA    1 
ATOM   5116  C  C     . GLY   A  1  697  ? -6.976  69.315  124.959 1.00 23.54 ? 695  GLY   A C     1 
ATOM   5117  O  O     . GLY   A  1  697  ? -6.479  69.658  123.883 1.00 25.40 ? 695  GLY   A O     1 
ATOM   5118  N  N     . PRO   A  1  698  ? -8.057  69.910  125.444 1.00 26.95 ? 696  PRO   A N     1 
ATOM   5119  C  CA    . PRO   A  1  698  ? -8.670  71.016  124.705 1.00 27.53 ? 696  PRO   A CA    1 
ATOM   5120  C  C     . PRO   A  1  698  ? -7.768  72.240  124.706 1.00 24.57 ? 696  PRO   A C     1 
ATOM   5121  O  O     . PRO   A  1  698  ? -6.894  72.408  125.560 1.00 26.26 ? 696  PRO   A O     1 
ATOM   5122  C  CB    . PRO   A  1  698  ? -9.962  71.282  125.478 1.00 29.15 ? 696  PRO   A CB    1 
ATOM   5123  C  CG    . PRO   A  1  698  ? -9.665  70.836  126.853 1.00 34.23 ? 696  PRO   A CG    1 
ATOM   5124  C  CD    . PRO   A  1  698  ? -8.756  69.637  126.709 1.00 33.90 ? 696  PRO   A CD    1 
ATOM   5125  N  N     . LEU   A  1  699  ? -7.970  73.089  123.700 1.00 24.00 ? 697  LEU   A N     1 
ATOM   5126  C  CA    . LEU   A  1  699  ? -7.248  74.355  123.659 1.00 23.34 ? 697  LEU   A CA    1 
ATOM   5127  C  C     . LEU   A  1  699  ? -7.655  75.260  124.812 1.00 26.00 ? 697  LEU   A C     1 
ATOM   5128  O  O     . LEU   A  1  699  ? -6.806  75.911  125.427 1.00 26.20 ? 697  LEU   A O     1 
ATOM   5129  C  CB    . LEU   A  1  699  ? -7.513  75.063  122.335 1.00 21.32 ? 697  LEU   A CB    1 
ATOM   5130  C  CG    . LEU   A  1  699  ? -6.981  74.418  121.065 1.00 25.59 ? 697  LEU   A CG    1 
ATOM   5131  C  CD1   . LEU   A  1  699  ? -7.383  75.287  119.902 1.00 23.12 ? 697  LEU   A CD1   1 
ATOM   5132  C  CD2   . LEU   A  1  699  ? -5.470  74.278  121.151 1.00 26.82 ? 697  LEU   A CD2   1 
ATOM   5133  N  N     . GLY   A  1  700  ? -8.949  75.312  125.118 1.00 24.51 ? 698  GLY   A N     1 
ATOM   5134  C  CA    . GLY   A  1  700  ? -9.495  76.295  126.024 1.00 23.29 ? 698  GLY   A CA    1 
ATOM   5135  C  C     . GLY   A  1  700  ? -10.638 77.008  125.339 1.00 21.91 ? 698  GLY   A C     1 
ATOM   5136  O  O     . GLY   A  1  700  ? -11.206 76.501  124.365 1.00 23.85 ? 698  GLY   A O     1 
ATOM   5137  N  N     . PRO   A  1  701  ? -10.981 78.207  125.806 1.00 24.73 ? 699  PRO   A N     1 
ATOM   5138  C  CA    . PRO   A  1  701  ? -12.106 78.933  125.201 1.00 23.79 ? 699  PRO   A CA    1 
ATOM   5139  C  C     . PRO   A  1  701  ? -11.871 79.165  123.717 1.00 23.22 ? 699  PRO   A C     1 
ATOM   5140  O  O     . PRO   A  1  701  ? -10.830 79.676  123.303 1.00 23.52 ? 699  PRO   A O     1 
ATOM   5141  C  CB    . PRO   A  1  701  ? -12.132 80.251  125.980 1.00 25.88 ? 699  PRO   A CB    1 
ATOM   5142  C  CG    . PRO   A  1  701  ? -11.546 79.885  127.322 1.00 25.00 ? 699  PRO   A CG    1 
ATOM   5143  C  CD    . PRO   A  1  701  ? -10.446 78.907  126.986 1.00 22.46 ? 699  PRO   A CD    1 
ATOM   5144  N  N     . ILE   A  1  702  ? -12.838 78.757  122.910 1.00 22.74 ? 700  ILE   A N     1 
ATOM   5145  C  CA    A ILE   A  1  702  ? -12.768 78.940  121.470 0.60 21.98 ? 700  ILE   A CA    1 
ATOM   5146  C  CA    B ILE   A  1  702  ? -12.785 78.917  121.461 0.40 21.97 ? 700  ILE   A CA    1 
ATOM   5147  C  C     . ILE   A  1  702  ? -13.839 79.931  121.045 1.00 20.91 ? 700  ILE   A C     1 
ATOM   5148  O  O     . ILE   A  1  702  ? -15.010 79.816  121.435 1.00 21.48 ? 700  ILE   A O     1 
ATOM   5149  C  CB    A ILE   A  1  702  ? -12.868 77.605  120.716 0.60 19.95 ? 700  ILE   A CB    1 
ATOM   5150  C  CB    B ILE   A  1  702  ? -13.009 77.579  120.738 0.40 19.98 ? 700  ILE   A CB    1 
ATOM   5151  C  CG1   A ILE   A  1  702  ? -11.594 76.792  120.959 0.60 21.01 ? 700  ILE   A CG1   1 
ATOM   5152  C  CG1   B ILE   A  1  702  ? -11.946 76.567  121.152 0.40 21.43 ? 700  ILE   A CG1   1 
ATOM   5153  C  CG2   A ILE   A  1  702  ? -13.071 77.842  119.219 0.60 20.38 ? 700  ILE   A CG2   1 
ATOM   5154  C  CG2   B ILE   A  1  702  ? -12.978 77.774  119.223 0.40 20.38 ? 700  ILE   A CG2   1 
ATOM   5155  C  CD1   A ILE   A  1  702  ? -11.552 75.492  120.224 0.60 18.98 ? 700  ILE   A CD1   1 
ATOM   5156  C  CD1   B ILE   A  1  702  ? -10.559 76.959  120.755 0.40 19.99 ? 700  ILE   A CD1   1 
ATOM   5157  N  N     . VAL   A  1  703  ? -13.429 80.911  120.256 1.00 20.01 ? 701  VAL   A N     1 
ATOM   5158  C  CA    . VAL   A  1  703  ? -14.330 81.906  119.706 1.00 21.67 ? 701  VAL   A CA    1 
ATOM   5159  C  C     . VAL   A  1  703  ? -14.759 81.399  118.340 1.00 20.66 ? 701  VAL   A C     1 
ATOM   5160  O  O     . VAL   A  1  703  ? -13.914 81.149  117.479 1.00 20.55 ? 701  VAL   A O     1 
ATOM   5161  C  CB    . VAL   A  1  703  ? -13.619 83.261  119.602 1.00 21.10 ? 701  VAL   A CB    1 
ATOM   5162  C  CG1   . VAL   A  1  703  ? -14.443 84.238  118.823 1.00 22.67 ? 701  VAL   A CG1   1 
ATOM   5163  C  CG2   . VAL   A  1  703  ? -13.357 83.795  121.002 1.00 23.77 ? 701  VAL   A CG2   1 
ATOM   5164  N  N     . CYS   A  1  704  ? -16.059 81.186  118.163 1.00 19.05 ? 702  CYS   A N     1 
ATOM   5165  C  CA    . CYS   A  1  704  ? -16.609 80.700  116.903 1.00 20.28 ? 702  CYS   A CA    1 
ATOM   5166  C  C     . CYS   A  1  704  ? -17.363 81.855  116.273 1.00 22.78 ? 702  CYS   A C     1 
ATOM   5167  O  O     . CYS   A  1  704  ? -18.386 82.297  116.797 1.00 20.39 ? 702  CYS   A O     1 
ATOM   5168  C  CB    . CYS   A  1  704  ? -17.541 79.515  117.126 1.00 19.51 ? 702  CYS   A CB    1 
ATOM   5169  S  SG    . CYS   A  1  704  ? -16.720 78.110  117.866 1.00 20.45 ? 702  CYS   A SG    1 
ATOM   5170  N  N     . ILE   A  1  705  ? -16.857 82.337  115.150 1.00 19.24 ? 703  ILE   A N     1 
ATOM   5171  C  CA    . ILE   A  1  705  ? -17.445 83.448  114.428 1.00 19.91 ? 703  ILE   A CA    1 
ATOM   5172  C  C     . ILE   A  1  705  ? -17.935 82.898  113.101 1.00 19.19 ? 703  ILE   A C     1 
ATOM   5173  O  O     . ILE   A  1  705  ? -17.169 82.263  112.367 1.00 19.59 ? 703  ILE   A O     1 
ATOM   5174  C  CB    . ILE   A  1  705  ? -16.400 84.556  114.238 1.00 21.05 ? 703  ILE   A CB    1 
ATOM   5175  C  CG1   . ILE   A  1  705  ? -16.036 85.163  115.591 1.00 22.00 ? 703  ILE   A CG1   1 
ATOM   5176  C  CG2   . ILE   A  1  705  ? -16.912 85.613  113.312 1.00 21.67 ? 703  ILE   A CG2   1 
ATOM   5177  C  CD1   . ILE   A  1  705  ? -14.799 86.024  115.543 1.00 23.59 ? 703  ILE   A CD1   1 
ATOM   5178  N  N     . SER   A  1  706  ? -19.205 83.115  112.804 1.00 20.47 ? 704  SER   A N     1 
ATOM   5179  C  CA    . SER   A  1  706  ? -19.833 82.427  111.689 1.00 19.28 ? 704  SER   A CA    1 
ATOM   5180  C  C     . SER   A  1  706  ? -20.470 83.421  110.734 1.00 20.27 ? 704  SER   A C     1 
ATOM   5181  O  O     . SER   A  1  706  ? -20.767 84.559  111.111 1.00 20.36 ? 704  SER   A O     1 
ATOM   5182  C  CB    . SER   A  1  706  ? -20.874 81.425  112.206 1.00 19.72 ? 704  SER   A CB    1 
ATOM   5183  O  OG    . SER   A  1  706  ? -21.780 82.062  113.073 1.00 20.29 ? 704  SER   A OG    1 
ATOM   5184  N  N     . PRO   A  1  707  ? -20.700 83.015  109.492 1.00 20.42 ? 705  PRO   A N     1 
ATOM   5185  C  CA    . PRO   A  1  707  ? -21.253 83.916  108.481 1.00 21.71 ? 705  PRO   A CA    1 
ATOM   5186  C  C     . PRO   A  1  707  ? -22.778 83.866  108.495 1.00 18.23 ? 705  PRO   A C     1 
ATOM   5187  O  O     . PRO   A  1  707  ? -23.396 82.973  109.080 1.00 20.77 ? 705  PRO   A O     1 
ATOM   5188  C  CB    . PRO   A  1  707  ? -20.722 83.294  107.185 1.00 20.36 ? 705  PRO   A CB    1 
ATOM   5189  C  CG    . PRO   A  1  707  ? -20.720 81.827  107.481 1.00 18.75 ? 705  PRO   A CG    1 
ATOM   5190  C  CD    . PRO   A  1  707  ? -20.331 81.706  108.926 1.00 19.13 ? 705  PRO   A CD    1 
ATOM   5191  N  N     . TRP   A  1  708  ? -23.382 84.843  107.825 1.00 18.79 ? 706  TRP   A N     1 
ATOM   5192  C  CA    . TRP   A  1  708  ? -24.843 84.871  107.810 1.00 19.45 ? 706  TRP   A CA    1 
ATOM   5193  C  C     . TRP   A  1  708  ? -25.425 83.825  106.873 1.00 19.25 ? 706  TRP   A C     1 
ATOM   5194  O  O     . TRP   A  1  708  ? -26.564 83.397  107.068 1.00 22.57 ? 706  TRP   A O     1 
ATOM   5195  C  CB    . TRP   A  1  708  ? -25.371 86.260  107.420 1.00 19.15 ? 706  TRP   A CB    1 
ATOM   5196  C  CG    . TRP   A  1  708  ? -25.223 86.496  105.968 1.00 21.04 ? 706  TRP   A CG    1 
ATOM   5197  C  CD1   . TRP   A  1  708  ? -24.189 87.123  105.349 1.00 20.51 ? 706  TRP   A CD1   1 
ATOM   5198  C  CD2   . TRP   A  1  708  ? -26.117 86.069  104.932 1.00 20.19 ? 706  TRP   A CD2   1 
ATOM   5199  N  NE1   . TRP   A  1  708  ? -24.375 87.114  103.990 1.00 20.58 ? 706  TRP   A NE1   1 
ATOM   5200  C  CE2   . TRP   A  1  708  ? -25.551 86.468  103.708 1.00 18.97 ? 706  TRP   A CE2   1 
ATOM   5201  C  CE3   . TRP   A  1  708  ? -27.345 85.396  104.922 1.00 19.93 ? 706  TRP   A CE3   1 
ATOM   5202  C  CZ2   . TRP   A  1  708  ? -26.159 86.213  102.483 1.00 18.24 ? 706  TRP   A CZ2   1 
ATOM   5203  C  CZ3   . TRP   A  1  708  ? -27.944 85.131  103.700 1.00 20.79 ? 706  TRP   A CZ3   1 
ATOM   5204  C  CH2   . TRP   A  1  708  ? -27.355 85.552  102.499 1.00 21.17 ? 706  TRP   A CH2   1 
ATOM   5205  N  N     . ASN   A  1  709  ? -24.666 83.386  105.874 1.00 18.46 ? 707  ASN   A N     1 
ATOM   5206  C  CA    . ASN   A  1  709  ? -25.311 82.774  104.719 1.00 19.52 ? 707  ASN   A CA    1 
ATOM   5207  C  C     . ASN   A  1  709  ? -25.655 81.311  104.926 1.00 21.20 ? 707  ASN   A C     1 
ATOM   5208  O  O     . ASN   A  1  709  ? -26.525 80.791  104.224 1.00 20.46 ? 707  ASN   A O     1 
ATOM   5209  C  CB    . ASN   A  1  709  ? -24.443 82.948  103.484 1.00 19.84 ? 707  ASN   A CB    1 
ATOM   5210  C  CG    . ASN   A  1  709  ? -23.214 82.102  103.541 1.00 21.01 ? 707  ASN   A CG    1 
ATOM   5211  O  OD1   . ASN   A  1  709  ? -22.337 82.328  104.367 1.00 22.25 ? 707  ASN   A OD1   1 
ATOM   5212  N  ND2   . ASN   A  1  709  ? -23.137 81.108  102.669 1.00 21.32 ? 707  ASN   A ND2   1 
ATOM   5213  N  N     . PHE   A  1  710  ? -24.972 80.629  105.837 1.00 19.86 ? 708  PHE   A N     1 
ATOM   5214  C  CA    . PHE   A  1  710  ? -25.361 79.303  106.297 1.00 20.43 ? 708  PHE   A CA    1 
ATOM   5215  C  C     . PHE   A  1  710  ? -25.559 79.475  107.795 1.00 21.01 ? 708  PHE   A C     1 
ATOM   5216  O  O     . PHE   A  1  710  ? -24.735 79.029  108.606 1.00 21.21 ? 708  PHE   A O     1 
ATOM   5217  C  CB    . PHE   A  1  710  ? -24.293 78.254  105.995 1.00 21.16 ? 708  PHE   A CB    1 
ATOM   5218  C  CG    . PHE   A  1  710  ? -24.026 78.048  104.521 1.00 24.43 ? 708  PHE   A CG    1 
ATOM   5219  C  CD1   . PHE   A  1  710  ? -25.061 78.044  103.601 1.00 24.11 ? 708  PHE   A CD1   1 
ATOM   5220  C  CD2   . PHE   A  1  710  ? -22.726 77.848  104.063 1.00 25.98 ? 708  PHE   A CD2   1 
ATOM   5221  C  CE1   . PHE   A  1  710  ? -24.812 77.839  102.251 1.00 24.16 ? 708  PHE   A CE1   1 
ATOM   5222  C  CE2   . PHE   A  1  710  ? -22.465 77.646  102.711 1.00 24.25 ? 708  PHE   A CE2   1 
ATOM   5223  C  CZ    . PHE   A  1  710  ? -23.509 77.647  101.806 1.00 27.50 ? 708  PHE   A CZ    1 
ATOM   5224  N  N     . PRO   A  1  711  ? -26.647 80.141  108.193 1.00 19.59 ? 709  PRO   A N     1 
ATOM   5225  C  CA    . PRO   A  1  711  ? -26.738 80.677  109.555 1.00 20.00 ? 709  PRO   A CA    1 
ATOM   5226  C  C     . PRO   A  1  711  ? -26.979 79.636  110.616 1.00 20.87 ? 709  PRO   A C     1 
ATOM   5227  O  O     . PRO   A  1  711  ? -26.849 79.954  111.802 1.00 20.78 ? 709  PRO   A O     1 
ATOM   5228  C  CB    . PRO   A  1  711  ? -27.932 81.625  109.466 1.00 21.05 ? 709  PRO   A CB    1 
ATOM   5229  C  CG    . PRO   A  1  711  ? -28.805 80.973  108.445 1.00 20.66 ? 709  PRO   A CG    1 
ATOM   5230  C  CD    . PRO   A  1  711  ? -27.842 80.465  107.398 1.00 19.85 ? 709  PRO   A CD    1 
ATOM   5231  N  N     . LEU   A  1  712  ? -27.359 78.425  110.247 1.00 20.62 ? 710  LEU   A N     1 
ATOM   5232  C  CA    . LEU   A  1  712  ? -27.438 77.338  111.204 1.00 18.59 ? 710  LEU   A CA    1 
ATOM   5233  C  C     . LEU   A  1  712  ? -26.360 76.293  110.986 1.00 18.92 ? 710  LEU   A C     1 
ATOM   5234  O  O     . LEU   A  1  712  ? -25.747 75.848  111.949 1.00 18.71 ? 710  LEU   A O     1 
ATOM   5235  C  CB    . LEU   A  1  712  ? -28.817 76.669  111.150 1.00 18.50 ? 710  LEU   A CB    1 
ATOM   5236  C  CG    . LEU   A  1  712  ? -28.972 75.537  112.161 1.00 22.31 ? 710  LEU   A CG    1 
ATOM   5237  C  CD1   . LEU   A  1  712  ? -28.869 76.079  113.587 1.00 20.00 ? 710  LEU   A CD1   1 
ATOM   5238  C  CD2   . LEU   A  1  712  ? -30.285 74.803  111.935 1.00 23.69 ? 710  LEU   A CD2   1 
ATOM   5239  N  N     . ALA   A  1  713  ? -26.065 75.933  109.739 1.00 20.05 ? 711  ALA   A N     1 
ATOM   5240  C  CA    . ALA   A  1  713  ? -25.172 74.803  109.506 1.00 18.31 ? 711  ALA   A CA    1 
ATOM   5241  C  C     . ALA   A  1  713  ? -23.739 75.117  109.921 1.00 18.95 ? 711  ALA   A C     1 
ATOM   5242  O  O     . ALA   A  1  713  ? -23.137 74.387  110.717 1.00 19.66 ? 711  ALA   A O     1 
ATOM   5243  C  CB    . ALA   A  1  713  ? -25.220 74.397  108.041 1.00 18.11 ? 711  ALA   A CB    1 
ATOM   5244  N  N     . ILE   A  1  714  ? -23.163 76.184  109.376 1.00 18.00 ? 712  ILE   A N     1 
ATOM   5245  C  CA    . ILE   A  1  714  ? -21.776 76.491  109.718 1.00 18.01 ? 712  ILE   A CA    1 
ATOM   5246  C  C     . ILE   A  1  714  ? -21.677 76.921  111.169 1.00 18.78 ? 712  ILE   A C     1 
ATOM   5247  O  O     . ILE   A  1  714  ? -20.731 76.562  111.886 1.00 18.98 ? 712  ILE   A O     1 
ATOM   5248  C  CB    . ILE   A  1  714  ? -21.219 77.546  108.755 1.00 19.14 ? 712  ILE   A CB    1 
ATOM   5249  C  CG1   . ILE   A  1  714  ? -21.097 76.914  107.363 1.00 21.91 ? 712  ILE   A CG1   1 
ATOM   5250  C  CG2   . ILE   A  1  714  ? -19.886 78.116  109.283 1.00 19.98 ? 712  ILE   A CG2   1 
ATOM   5251  C  CD1   . ILE   A  1  714  ? -20.161 77.618  106.459 1.00 28.70 ? 712  ILE   A CD1   1 
ATOM   5252  N  N     . PHE   A  1  715  ? -22.653 77.703  111.620 1.00 19.18 ? 713  PHE   A N     1 
ATOM   5253  C  CA    . PHE   A  1  715  ? -22.740 78.063  113.024 1.00 18.25 ? 713  PHE   A CA    1 
ATOM   5254  C  C     . PHE   A  1  715  ? -22.653 76.826  113.909 1.00 21.69 ? 713  PHE   A C     1 
ATOM   5255  O  O     . PHE   A  1  715  ? -21.818 76.749  114.818 1.00 19.38 ? 713  PHE   A O     1 
ATOM   5256  C  CB    . PHE   A  1  715  ? -24.068 78.785  113.248 1.00 20.86 ? 713  PHE   A CB    1 
ATOM   5257  C  CG    . PHE   A  1  715  ? -24.298 79.172  114.660 1.00 20.95 ? 713  PHE   A CG    1 
ATOM   5258  C  CD1   . PHE   A  1  715  ? -23.658 80.274  115.183 1.00 22.05 ? 713  PHE   A CD1   1 
ATOM   5259  C  CD2   . PHE   A  1  715  ? -25.132 78.421  115.484 1.00 21.07 ? 713  PHE   A CD2   1 
ATOM   5260  C  CE1   . PHE   A  1  715  ? -23.858 80.640  116.495 1.00 22.97 ? 713  PHE   A CE1   1 
ATOM   5261  C  CE2   . PHE   A  1  715  ? -25.317 78.764  116.793 1.00 21.31 ? 713  PHE   A CE2   1 
ATOM   5262  C  CZ    . PHE   A  1  715  ? -24.700 79.888  117.307 1.00 24.78 ? 713  PHE   A CZ    1 
ATOM   5263  N  N     . THR   A  1  716  ? -23.515 75.843  113.655 1.00 19.47 ? 714  THR   A N     1 
ATOM   5264  C  CA    . THR   A  1  716  ? -23.542 74.632  114.470 1.00 19.62 ? 714  THR   A CA    1 
ATOM   5265  C  C     . THR   A  1  716  ? -22.269 73.826  114.303 1.00 19.44 ? 714  THR   A C     1 
ATOM   5266  O  O     . THR   A  1  716  ? -21.733 73.297  115.280 1.00 19.19 ? 714  THR   A O     1 
ATOM   5267  C  CB    . THR   A  1  716  ? -24.749 73.786  114.069 1.00 21.84 ? 714  THR   A CB    1 
ATOM   5268  O  OG1   . THR   A  1  716  ? -25.938 74.533  114.327 1.00 21.05 ? 714  THR   A OG1   1 
ATOM   5269  C  CG2   . THR   A  1  716  ? -24.805 72.486  114.849 1.00 22.10 ? 714  THR   A CG2   1 
ATOM   5270  N  N     . GLY   A  1  717  ? -21.776 73.721  113.071 1.00 17.84 ? 715  GLY   A N     1 
ATOM   5271  C  CA    . GLY   A  1  717  ? -20.587 72.921  112.827 1.00 17.98 ? 715  GLY   A CA    1 
ATOM   5272  C  C     . GLY   A  1  717  ? -19.394 73.388  113.640 1.00 18.20 ? 715  GLY   A C     1 
ATOM   5273  O  O     . GLY   A  1  717  ? -18.744 72.596  114.319 1.00 19.74 ? 715  GLY   A O     1 
ATOM   5274  N  N     . GLN   A  1  718  ? -19.085 74.683  113.574 1.00 18.17 ? 716  GLN   A N     1 
ATOM   5275  C  CA    . GLN   A  1  718  ? -17.919 75.181  114.300 1.00 17.65 ? 716  GLN   A CA    1 
ATOM   5276  C  C     . GLN   A  1  718  ? -18.084 74.964  115.791 1.00 20.39 ? 716  GLN   A C     1 
ATOM   5277  O  O     . GLN   A  1  718  ? -17.173 74.477  116.468 1.00 19.56 ? 716  GLN   A O     1 
ATOM   5278  C  CB    . GLN   A  1  718  ? -17.718 76.665  114.018 1.00 17.77 ? 716  GLN   A CB    1 
ATOM   5279  C  CG    . GLN   A  1  718  ? -17.406 76.957  112.570 1.00 17.25 ? 716  GLN   A CG    1 
ATOM   5280  C  CD    . GLN   A  1  718  ? -17.000 78.391  112.333 1.00 20.91 ? 716  GLN   A CD    1 
ATOM   5281  O  OE1   . GLN   A  1  718  ? -16.041 78.657  111.614 1.00 20.84 ? 716  GLN   A OE1   1 
ATOM   5282  N  NE2   . GLN   A  1  718  ? -17.724 79.326  112.930 1.00 20.03 ? 716  GLN   A NE2   1 
ATOM   5283  N  N     . ILE   A  1  719  ? -19.255 75.316  116.319 1.00 19.98 ? 717  ILE   A N     1 
ATOM   5284  C  CA    . ILE   A  1  719  ? -19.493 75.202  117.751 1.00 19.37 ? 717  ILE   A CA    1 
ATOM   5285  C  C     . ILE   A  1  719  ? -19.474 73.747  118.192 1.00 18.98 ? 717  ILE   A C     1 
ATOM   5286  O  O     . ILE   A  1  719  ? -18.901 73.409  119.233 1.00 19.87 ? 717  ILE   A O     1 
ATOM   5287  C  CB    . ILE   A  1  719  ? -20.826 75.884  118.103 1.00 22.30 ? 717  ILE   A CB    1 
ATOM   5288  C  CG1   . ILE   A  1  719  ? -20.700 77.390  117.940 1.00 20.28 ? 717  ILE   A CG1   1 
ATOM   5289  C  CG2   . ILE   A  1  719  ? -21.296 75.501  119.491 1.00 25.62 ? 717  ILE   A CG2   1 
ATOM   5290  C  CD1   . ILE   A  1  719  ? -22.034 78.016  117.806 1.00 26.12 ? 717  ILE   A CD1   1 
ATOM   5291  N  N     . ALA   A  1  720  ? -20.121 72.867  117.423 1.00 19.70 ? 718  ALA   A N     1 
ATOM   5292  C  CA    . ALA   A  1  720  ? -20.178 71.463  117.815 1.00 19.96 ? 718  ALA   A CA    1 
ATOM   5293  C  C     . ALA   A  1  720  ? -18.782 70.874  117.873 1.00 18.23 ? 718  ALA   A C     1 
ATOM   5294  O  O     . ALA   A  1  720  ? -18.443 70.168  118.824 1.00 18.79 ? 718  ALA   A O     1 
ATOM   5295  C  CB    . ALA   A  1  720  ? -21.036 70.675  116.822 1.00 19.93 ? 718  ALA   A CB    1 
ATOM   5296  N  N     . ALA   A  1  721  ? -17.965 71.173  116.866 1.00 18.89 ? 719  ALA   A N     1 
ATOM   5297  C  CA    . ALA   A  1  721  ? -16.601 70.666  116.827 1.00 17.39 ? 719  ALA   A CA    1 
ATOM   5298  C  C     . ALA   A  1  721  ? -15.811 71.150  118.033 1.00 18.12 ? 719  ALA   A C     1 
ATOM   5299  O  O     . ALA   A  1  721  ? -15.179 70.358  118.741 1.00 18.46 ? 719  ALA   A O     1 
ATOM   5300  C  CB    . ALA   A  1  721  ? -15.941 71.140  115.539 1.00 18.39 ? 719  ALA   A CB    1 
ATOM   5301  N  N     . ALA   A  1  722  ? -15.873 72.452  118.309 1.00 18.25 ? 720  ALA   A N     1 
ATOM   5302  C  CA    . ALA   A  1  722  ? -15.116 72.989  119.431 1.00 17.86 ? 720  ALA   A CA    1 
ATOM   5303  C  C     . ALA   A  1  722  ? -15.586 72.387  120.749 1.00 21.01 ? 720  ALA   A C     1 
ATOM   5304  O  O     . ALA   A  1  722  ? -14.769 71.977  121.587 1.00 20.11 ? 720  ALA   A O     1 
ATOM   5305  C  CB    . ALA   A  1  722  ? -15.203 74.515  119.435 1.00 20.31 ? 720  ALA   A CB    1 
ATOM   5306  N  N     . LEU   A  1  723  ? -16.902 72.297  120.937 1.00 19.45 ? 721  LEU   A N     1 
ATOM   5307  C  CA    . LEU   A  1  723  ? -17.450 71.744  122.167 1.00 19.91 ? 721  LEU   A CA    1 
ATOM   5308  C  C     . LEU   A  1  723  ? -17.064 70.286  122.342 1.00 20.78 ? 721  LEU   A C     1 
ATOM   5309  O  O     . LEU   A  1  723  ? -16.682 69.860  123.432 1.00 19.99 ? 721  LEU   A O     1 
ATOM   5310  C  CB    . LEU   A  1  723  ? -18.968 71.854  122.145 1.00 21.95 ? 721  LEU   A CB    1 
ATOM   5311  C  CG    . LEU   A  1  723  ? -19.582 73.232  122.321 1.00 20.35 ? 721  LEU   A CG    1 
ATOM   5312  C  CD1   . LEU   A  1  723  ? -21.066 73.085  122.080 1.00 21.92 ? 721  LEU   A CD1   1 
ATOM   5313  C  CD2   . LEU   A  1  723  ? -19.309 73.755  123.722 1.00 22.45 ? 721  LEU   A CD2   1 
ATOM   5314  N  N     . VAL   A  1  724  ? -17.218 69.484  121.292 1.00 21.31 ? 722  VAL   A N     1 
ATOM   5315  C  CA    . VAL   A  1  724  ? -16.988 68.061  121.470 1.00 20.37 ? 722  VAL   A CA    1 
ATOM   5316  C  C     . VAL   A  1  724  ? -15.506 67.784  121.688 1.00 19.12 ? 722  VAL   A C     1 
ATOM   5317  O  O     . VAL   A  1  724  ? -15.144 66.801  122.342 1.00 21.52 ? 722  VAL   A O     1 
ATOM   5318  C  CB    . VAL   A  1  724  ? -17.611 67.258  120.315 1.00 19.14 ? 722  VAL   A CB    1 
ATOM   5319  C  CG1   . VAL   A  1  724  ? -16.698 67.268  119.078 1.00 21.39 ? 722  VAL   A CG1   1 
ATOM   5320  C  CG2   . VAL   A  1  724  ? -17.971 65.851  120.774 1.00 20.88 ? 722  VAL   A CG2   1 
ATOM   5321  N  N     . ALA   A  1  725  ? -14.634 68.655  121.176 1.00 19.90 ? 723  ALA   A N     1 
ATOM   5322  C  CA    . ALA   A  1  725  ? -13.213 68.569  121.483 1.00 21.90 ? 723  ALA   A CA    1 
ATOM   5323  C  C     . ALA   A  1  725  ? -12.899 68.990  122.911 1.00 22.39 ? 723  ALA   A C     1 
ATOM   5324  O  O     . ALA   A  1  725  ? -11.722 68.971  123.293 1.00 23.67 ? 723  ALA   A O     1 
ATOM   5325  C  CB    . ALA   A  1  725  ? -12.407 69.412  120.497 1.00 20.39 ? 723  ALA   A CB    1 
ATOM   5326  N  N     . GLY   A  1  726  ? -13.902 69.372  123.699 1.00 21.23 ? 724  GLY   A N     1 
ATOM   5327  C  CA    . GLY   A  1  726  ? -13.685 69.716  125.086 1.00 22.11 ? 724  GLY   A CA    1 
ATOM   5328  C  C     . GLY   A  1  726  ? -13.440 71.176  125.381 1.00 22.35 ? 724  GLY   A C     1 
ATOM   5329  O  O     . GLY   A  1  726  ? -13.004 71.499  126.497 1.00 24.07 ? 724  GLY   A O     1 
ATOM   5330  N  N     . ASN   A  1  727  ? -13.713 72.063  124.438 1.00 21.68 ? 725  ASN   A N     1 
ATOM   5331  C  CA    . ASN   A  1  727  ? -13.502 73.495  124.599 1.00 22.52 ? 725  ASN   A CA    1 
ATOM   5332  C  C     . ASN   A  1  727  ? -14.816 74.190  124.888 1.00 23.30 ? 725  ASN   A C     1 
ATOM   5333  O  O     . ASN   A  1  727  ? -15.814 73.933  124.195 1.00 23.45 ? 725  ASN   A O     1 
ATOM   5334  C  CB    . ASN   A  1  727  ? -12.939 74.078  123.311 1.00 22.29 ? 725  ASN   A CB    1 
ATOM   5335  C  CG    . ASN   A  1  727  ? -11.717 73.362  122.841 1.00 22.02 ? 725  ASN   A CG    1 
ATOM   5336  O  OD1   . ASN   A  1  727  ? -10.632 73.552  123.375 1.00 23.69 ? 725  ASN   A OD1   1 
ATOM   5337  N  ND2   . ASN   A  1  727  ? -11.878 72.532  121.823 1.00 20.33 ? 725  ASN   A ND2   1 
ATOM   5338  N  N     . PRO   A  1  728  ? -14.860 75.096  125.856 1.00 22.27 ? 726  PRO   A N     1 
ATOM   5339  C  CA    . PRO   A  1  728  ? -16.023 75.976  125.957 1.00 23.42 ? 726  PRO   A CA    1 
ATOM   5340  C  C     . PRO   A  1  728  ? -15.996 76.965  124.810 1.00 23.30 ? 726  PRO   A C     1 
ATOM   5341  O  O     . PRO   A  1  728  ? -14.937 77.318  124.284 1.00 24.24 ? 726  PRO   A O     1 
ATOM   5342  C  CB    . PRO   A  1  728  ? -15.817 76.684  127.298 1.00 23.01 ? 726  PRO   A CB    1 
ATOM   5343  C  CG    . PRO   A  1  728  ? -14.351 76.726  127.462 1.00 24.07 ? 726  PRO   A CG    1 
ATOM   5344  C  CD    . PRO   A  1  728  ? -13.796 75.482  126.798 1.00 23.10 ? 726  PRO   A CD    1 
ATOM   5345  N  N     . VAL   A  1  729  ? -17.182 77.403  124.411 1.00 23.24 ? 727  VAL   A N     1 
ATOM   5346  C  CA    . VAL   A  1  729  ? -17.360 78.137  123.169 1.00 21.88 ? 727  VAL   A CA    1 
ATOM   5347  C  C     . VAL   A  1  729  ? -18.023 79.474  123.437 1.00 22.40 ? 727  VAL   A C     1 
ATOM   5348  O  O     . VAL   A  1  729  ? -18.989 79.565  124.199 1.00 23.14 ? 727  VAL   A O     1 
ATOM   5349  C  CB    . VAL   A  1  729  ? -18.177 77.310  122.155 1.00 20.55 ? 727  VAL   A CB    1 
ATOM   5350  C  CG1   . VAL   A  1  729  ? -18.618 78.176  120.973 1.00 22.11 ? 727  VAL   A CG1   1 
ATOM   5351  C  CG2   . VAL   A  1  729  ? -17.348 76.132  121.680 1.00 22.59 ? 727  VAL   A CG2   1 
ATOM   5352  N  N     . LEU   A  1  730  ? -17.501 80.505  122.791 1.00 21.73 ? 728  LEU   A N     1 
ATOM   5353  C  CA    . LEU   A  1  730  ? -18.147 81.798  122.667 1.00 22.21 ? 728  LEU   A CA    1 
ATOM   5354  C  C     . LEU   A  1  730  ? -18.631 81.840  121.232 1.00 20.73 ? 728  LEU   A C     1 
ATOM   5355  O  O     . LEU   A  1  730  ? -17.816 81.846  120.307 1.00 21.80 ? 728  LEU   A O     1 
ATOM   5356  C  CB    . LEU   A  1  730  ? -17.152 82.926  122.931 1.00 24.66 ? 728  LEU   A CB    1 
ATOM   5357  C  CG    . LEU   A  1  730  ? -16.496 82.982  124.319 1.00 22.22 ? 728  LEU   A CG    1 
ATOM   5358  C  CD1   . LEU   A  1  730  ? -17.529 82.707  125.397 1.00 23.57 ? 728  LEU   A CD1   1 
ATOM   5359  C  CD2   . LEU   A  1  730  ? -15.327 82.023  124.448 1.00 23.22 ? 728  LEU   A CD2   1 
ATOM   5360  N  N     . ALA   A  1  731  ? -19.947 81.834  121.052 1.00 21.54 ? 729  ALA   A N     1 
ATOM   5361  C  CA    . ALA   A  1  731  ? -20.559 81.738  119.734 1.00 21.58 ? 729  ALA   A CA    1 
ATOM   5362  C  C     . ALA   A  1  731  ? -21.008 83.128  119.319 1.00 21.94 ? 729  ALA   A C     1 
ATOM   5363  O  O     . ALA   A  1  731  ? -21.926 83.695  119.917 1.00 24.43 ? 729  ALA   A O     1 
ATOM   5364  C  CB    . ALA   A  1  731  ? -21.737 80.769  119.759 1.00 23.03 ? 729  ALA   A CB    1 
ATOM   5365  N  N     . LYS   A  1  732  ? -20.371 83.670  118.284 1.00 20.92 ? 730  LYS   A N     1 
ATOM   5366  C  CA    . LYS   A  1  732  ? -20.694 84.997  117.775 1.00 21.90 ? 730  LYS   A CA    1 
ATOM   5367  C  C     . LYS   A  1  732  ? -21.292 84.810  116.392 1.00 22.03 ? 730  LYS   A C     1 
ATOM   5368  O  O     . LYS   A  1  732  ? -20.556 84.727  115.400 1.00 21.38 ? 730  LYS   A O     1 
ATOM   5369  C  CB    . LYS   A  1  732  ? -19.432 85.858  117.713 1.00 25.10 ? 730  LYS   A CB    1 
ATOM   5370  C  CG    . LYS   A  1  732  ? -19.651 87.329  118.011 1.00 24.94 ? 730  LYS   A CG    1 
ATOM   5371  C  CD    . LYS   A  1  732  ? -20.629 87.964  117.027 1.00 22.07 ? 730  LYS   A CD    1 
ATOM   5372  C  CE    . LYS   A  1  732  ? -20.029 88.066  115.635 1.00 21.49 ? 730  LYS   A CE    1 
ATOM   5373  N  NZ    . LYS   A  1  732  ? -21.000 88.681  114.685 1.00 24.22 ? 730  LYS   A NZ    1 
ATOM   5374  N  N     . PRO   A  1  733  ? -22.613 84.733  116.269 1.00 21.19 ? 731  PRO   A N     1 
ATOM   5375  C  CA    . PRO   A  1  733  ? -23.223 84.565  114.950 1.00 21.32 ? 731  PRO   A CA    1 
ATOM   5376  C  C     . PRO   A  1  733  ? -23.205 85.881  114.198 1.00 18.67 ? 731  PRO   A C     1 
ATOM   5377  O  O     . PRO   A  1  733  ? -23.078 86.960  114.781 1.00 22.00 ? 731  PRO   A O     1 
ATOM   5378  C  CB    . PRO   A  1  733  ? -24.662 84.177  115.286 1.00 22.15 ? 731  PRO   A CB    1 
ATOM   5379  C  CG    . PRO   A  1  733  ? -24.929 84.904  116.574 1.00 21.74 ? 731  PRO   A CG    1 
ATOM   5380  C  CD    . PRO   A  1  733  ? -23.620 84.851  117.339 1.00 21.87 ? 731  PRO   A CD    1 
ATOM   5381  N  N     . ALA   A  1  734  ? -23.354 85.777  112.882 1.00 20.92 ? 732  ALA   A N     1 
ATOM   5382  C  CA    . ALA   A  1  734  ? -23.392 86.974  112.060 1.00 20.02 ? 732  ALA   A CA    1 
ATOM   5383  C  C     . ALA   A  1  734  ? -24.518 87.889  112.517 1.00 21.68 ? 732  ALA   A C     1 
ATOM   5384  O  O     . ALA   A  1  734  ? -25.589 87.432  112.935 1.00 23.76 ? 732  ALA   A O     1 
ATOM   5385  C  CB    . ALA   A  1  734  ? -23.628 86.580  110.607 1.00 21.36 ? 732  ALA   A CB    1 
ATOM   5386  N  N     . GLU   A  1  735  ? -24.278 89.194  112.426 1.00 22.72 ? 733  GLU   A N     1 
ATOM   5387  C  CA    . GLU   A  1  735  ? -25.282 90.150  112.873 1.00 24.35 ? 733  GLU   A CA    1 
ATOM   5388  C  C     . GLU   A  1  735  ? -26.584 90.035  112.090 1.00 25.00 ? 733  GLU   A C     1 
ATOM   5389  O  O     . GLU   A  1  735  ? -27.643 90.402  112.613 1.00 24.19 ? 733  GLU   A O     1 
ATOM   5390  C  CB    . GLU   A  1  735  ? -24.734 91.577  112.815 1.00 26.37 ? 733  GLU   A CB    1 
ATOM   5391  C  CG    . GLU   A  1  735  ? -24.206 92.014  111.455 1.00 27.37 ? 733  GLU   A CG    1 
ATOM   5392  C  CD    . GLU   A  1  735  ? -22.724 91.703  111.265 1.00 29.71 ? 733  GLU   A CD    1 
ATOM   5393  O  OE1   . GLU   A  1  735  ? -22.222 90.748  111.895 1.00 27.93 ? 733  GLU   A OE1   1 
ATOM   5394  O  OE2   . GLU   A  1  735  ? -22.065 92.415  110.478 1.00 28.15 ? 733  GLU   A OE2   1 
ATOM   5395  N  N     . GLU   A  1  736  ? -26.535 89.517  110.863 1.00 23.62 ? 734  GLU   A N     1 
ATOM   5396  C  CA    . GLU   A  1  736  ? -27.743 89.443  110.057 1.00 21.41 ? 734  GLU   A CA    1 
ATOM   5397  C  C     . GLU   A  1  736  ? -28.676 88.335  110.514 1.00 24.24 ? 734  GLU   A C     1 
ATOM   5398  O  O     . GLU   A  1  736  ? -29.893 88.455  110.342 1.00 24.49 ? 734  GLU   A O     1 
ATOM   5399  C  CB    . GLU   A  1  736  ? -27.393 89.228  108.584 1.00 22.60 ? 734  GLU   A CB    1 
ATOM   5400  C  CG    . GLU   A  1  736  ? -26.600 90.354  107.945 1.00 26.39 ? 734  GLU   A CG    1 
ATOM   5401  C  CD    . GLU   A  1  736  ? -25.099 90.132  108.019 1.00 27.84 ? 734  GLU   A CD    1 
ATOM   5402  O  OE1   . GLU   A  1  736  ? -24.646 89.326  108.860 1.00 24.98 ? 734  GLU   A OE1   1 
ATOM   5403  O  OE2   . GLU   A  1  736  ? -24.369 90.752  107.219 1.00 26.71 ? 734  GLU   A OE2   1 
ATOM   5404  N  N     . THR   A  1  737  ? -28.144 87.254  111.085 1.00 22.84 ? 735  THR   A N     1 
ATOM   5405  C  CA    . THR   A  1  737  ? -28.920 86.036  111.328 1.00 23.82 ? 735  THR   A CA    1 
ATOM   5406  C  C     . THR   A  1  737  ? -28.746 85.510  112.752 1.00 21.96 ? 735  THR   A C     1 
ATOM   5407  O  O     . THR   A  1  737  ? -28.391 84.346  112.958 1.00 22.95 ? 735  THR   A O     1 
ATOM   5408  C  CB    . THR   A  1  737  ? -28.543 84.973  110.302 1.00 20.56 ? 735  THR   A CB    1 
ATOM   5409  O  OG1   . THR   A  1  737  ? -27.120 84.760  110.346 1.00 21.77 ? 735  THR   A OG1   1 
ATOM   5410  C  CG2   . THR   A  1  737  ? -28.929 85.424  108.905 1.00 19.83 ? 735  THR   A CG2   1 
ATOM   5411  N  N     . PRO   A  1  738  ? -29.052 86.327  113.769 1.00 22.44 ? 736  PRO   A N     1 
ATOM   5412  C  CA    . PRO   A  1  738  ? -28.881 85.862  115.154 1.00 21.61 ? 736  PRO   A CA    1 
ATOM   5413  C  C     . PRO   A  1  738  ? -29.975 84.931  115.644 1.00 23.39 ? 736  PRO   A C     1 
ATOM   5414  O  O     . PRO   A  1  738  ? -29.739 84.183  116.605 1.00 23.39 ? 736  PRO   A O     1 
ATOM   5415  C  CB    . PRO   A  1  738  ? -28.912 87.165  115.961 1.00 27.03 ? 736  PRO   A CB    1 
ATOM   5416  C  CG    . PRO   A  1  738  ? -29.843 88.024  115.182 1.00 23.78 ? 736  PRO   A CG    1 
ATOM   5417  C  CD    . PRO   A  1  738  ? -29.582 87.703  113.724 1.00 23.33 ? 736  PRO   A CD    1 
ATOM   5418  N  N     . LEU   A  1  739  ? -31.162 84.952  115.037 1.00 21.51 ? 737  LEU   A N     1 
ATOM   5419  C  CA    . LEU   A  1  739  ? -32.282 84.220  115.622 1.00 22.32 ? 737  LEU   A CA    1 
ATOM   5420  C  C     . LEU   A  1  739  ? -32.094 82.716  115.486 1.00 20.52 ? 737  LEU   A C     1 
ATOM   5421  O  O     . LEU   A  1  739  ? -32.283 81.970  116.452 1.00 22.94 ? 737  LEU   A O     1 
ATOM   5422  C  CB    . LEU   A  1  739  ? -33.598 84.655  114.988 1.00 22.53 ? 737  LEU   A CB    1 
ATOM   5423  C  CG    . LEU   A  1  739  ? -33.913 86.137  115.112 1.00 23.56 ? 737  LEU   A CG    1 
ATOM   5424  C  CD1   . LEU   A  1  739  ? -35.196 86.431  114.343 1.00 22.03 ? 737  LEU   A CD1   1 
ATOM   5425  C  CD2   . LEU   A  1  739  ? -34.059 86.542  116.571 1.00 24.88 ? 737  LEU   A CD2   1 
ATOM   5426  N  N     . ILE   A  1  740  ? -31.737 82.247  114.292 1.00 20.29 ? 738  ILE   A N     1 
ATOM   5427  C  CA    . ILE   A  1  740  ? -31.556 80.810  114.122 1.00 20.89 ? 738  ILE   A CA    1 
ATOM   5428  C  C     . ILE   A  1  740  ? -30.351 80.342  114.923 1.00 20.14 ? 738  ILE   A C     1 
ATOM   5429  O  O     . ILE   A  1  740  ? -30.333 79.220  115.442 1.00 21.86 ? 738  ILE   A O     1 
ATOM   5430  C  CB    . ILE   A  1  740  ? -31.475 80.457  112.626 1.00 23.45 ? 738  ILE   A CB    1 
ATOM   5431  C  CG1   . ILE   A  1  740  ? -31.427 78.945  112.421 1.00 21.75 ? 738  ILE   A CG1   1 
ATOM   5432  C  CG2   . ILE   A  1  740  ? -30.263 81.097  112.005 1.00 21.08 ? 738  ILE   A CG2   1 
ATOM   5433  C  CD1   . ILE   A  1  740  ? -32.649 78.211  112.925 1.00 24.19 ? 738  ILE   A CD1   1 
ATOM   5434  N  N     . ALA   A  1  741  ? -29.350 81.205  115.072 1.00 21.00 ? 739  ALA   A N     1 
ATOM   5435  C  CA    . ALA   A  1  741  ? -28.212 80.878  115.919 1.00 22.90 ? 739  ALA   A CA    1 
ATOM   5436  C  C     . ALA   A  1  741  ? -28.637 80.733  117.373 1.00 22.11 ? 739  ALA   A C     1 
ATOM   5437  O  O     . ALA   A  1  741  ? -28.218 79.795  118.059 1.00 24.34 ? 739  ALA   A O     1 
ATOM   5438  C  CB    . ALA   A  1  741  ? -27.148 81.958  115.777 1.00 23.98 ? 739  ALA   A CB    1 
ATOM   5439  N  N     . ALA   A  1  742  ? -29.488 81.640  117.855 1.00 23.06 ? 740  ALA   A N     1 
ATOM   5440  C  CA    . ALA   A  1  742  ? -29.956 81.527  119.229 1.00 20.55 ? 740  ALA   A CA    1 
ATOM   5441  C  C     . ALA   A  1  742  ? -30.756 80.251  119.419 1.00 22.97 ? 740  ALA   A C     1 
ATOM   5442  O  O     . ALA   A  1  742  ? -30.659 79.594  120.461 1.00 24.43 ? 740  ALA   A O     1 
ATOM   5443  C  CB    . ALA   A  1  742  ? -30.795 82.747  119.603 1.00 21.66 ? 740  ALA   A CB    1 
ATOM   5444  N  N     . GLU   A  1  743  ? -31.535 79.872  118.409 1.00 22.00 ? 741  GLU   A N     1 
ATOM   5445  C  CA    . GLU   A  1  743  ? -32.282 78.628  118.494 1.00 23.69 ? 741  GLU   A CA    1 
ATOM   5446  C  C     . GLU   A  1  743  ? -31.345 77.425  118.485 1.00 21.60 ? 741  GLU   A C     1 
ATOM   5447  O  O     . GLU   A  1  743  ? -31.557 76.463  119.234 1.00 23.41 ? 741  GLU   A O     1 
ATOM   5448  C  CB    . GLU   A  1  743  ? -33.300 78.576  117.354 1.00 23.47 ? 741  GLU   A CB    1 
ATOM   5449  C  CG    . GLU   A  1  743  ? -34.085 77.286  117.247 1.00 25.82 ? 741  GLU   A CG    1 
ATOM   5450  C  CD    . GLU   A  1  743  ? -35.002 77.002  118.427 1.00 24.18 ? 741  GLU   A CD    1 
ATOM   5451  O  OE1   . GLU   A  1  743  ? -35.153 77.848  119.341 1.00 25.14 ? 741  GLU   A OE1   1 
ATOM   5452  O  OE2   . GLU   A  1  743  ? -35.562 75.888  118.436 1.00 28.83 ? 741  GLU   A OE2   1 
ATOM   5453  N  N     . GLY   A  1  744  ? -30.292 77.471  117.663 1.00 22.19 ? 742  GLY   A N     1 
ATOM   5454  C  CA    . GLY   A  1  744  ? -29.300 76.406  117.686 1.00 21.26 ? 742  GLY   A CA    1 
ATOM   5455  C  C     . GLY   A  1  744  ? -28.623 76.272  119.038 1.00 20.79 ? 742  GLY   A C     1 
ATOM   5456  O  O     . GLY   A  1  744  ? -28.441 75.160  119.542 1.00 23.67 ? 742  GLY   A O     1 
ATOM   5457  N  N     . VAL   A  1  745  ? -28.269 77.402  119.657 1.00 22.00 ? 743  VAL   A N     1 
ATOM   5458  C  CA    . VAL   A  1  745  ? -27.700 77.372  121.005 1.00 23.14 ? 743  VAL   A CA    1 
ATOM   5459  C  C     . VAL   A  1  745  ? -28.710 76.825  122.007 1.00 25.13 ? 743  VAL   A C     1 
ATOM   5460  O  O     . VAL   A  1  745  ? -28.364 76.042  122.902 1.00 26.37 ? 743  VAL   A O     1 
ATOM   5461  C  CB    . VAL   A  1  745  ? -27.191 78.769  121.412 1.00 24.28 ? 743  VAL   A CB    1 
ATOM   5462  C  CG1   . VAL   A  1  745  ? -26.877 78.818  122.909 1.00 26.52 ? 743  VAL   A CG1   1 
ATOM   5463  C  CG2   . VAL   A  1  745  ? -25.957 79.145  120.608 1.00 27.15 ? 743  VAL   A CG2   1 
ATOM   5464  N  N     . ARG   A  1  746  ? -29.974 77.242  121.887 1.00 25.76 ? 744  ARG   A N     1 
ATOM   5465  C  CA    . ARG   A  1  746  ? -30.999 76.714  122.779 1.00 24.49 ? 744  ARG   A CA    1 
ATOM   5466  C  C     . ARG   A  1  746  ? -31.098 75.199  122.651 1.00 24.06 ? 744  ARG   A C     1 
ATOM   5467  O  O     . ARG   A  1  746  ? -31.202 74.487  123.656 1.00 25.79 ? 744  ARG   A O     1 
ATOM   5468  C  CB    . ARG   A  1  746  ? -32.347 77.373  122.479 1.00 26.52 ? 744  ARG   A CB    1 
ATOM   5469  C  CG    . ARG   A  1  746  ? -33.442 77.042  123.489 1.00 25.89 ? 744  ARG   A CG    1 
ATOM   5470  C  CD    . ARG   A  1  746  ? -34.843 77.306  122.935 1.00 27.07 ? 744  ARG   A CD    1 
ATOM   5471  N  NE    . ARG   A  1  746  ? -35.165 76.437  121.811 1.00 28.38 ? 744  ARG   A NE    1 
ATOM   5472  C  CZ    . ARG   A  1  746  ? -35.460 75.147  121.917 1.00 28.03 ? 744  ARG   A CZ    1 
ATOM   5473  N  NH1   . ARG   A  1  746  ? -35.480 74.535  123.090 1.00 32.67 ? 744  ARG   A NH1   1 
ATOM   5474  N  NH2   . ARG   A  1  746  ? -35.732 74.451  120.816 1.00 28.77 ? 744  ARG   A NH2   1 
ATOM   5475  N  N     . ILE   A  1  747  ? -31.045 74.691  121.421 1.00 22.35 ? 745  ILE   A N     1 
ATOM   5476  C  CA    . ILE   A  1  747  ? -31.106 73.250  121.192 1.00 22.86 ? 745  ILE   A CA    1 
ATOM   5477  C  C     . ILE   A  1  747  ? -29.895 72.546  121.798 1.00 22.44 ? 745  ILE   A C     1 
ATOM   5478  O  O     . ILE   A  1  747  ? -30.027 71.507  122.454 1.00 23.75 ? 745  ILE   A O     1 
ATOM   5479  C  CB    . ILE   A  1  747  ? -31.279 72.956  119.694 1.00 22.81 ? 745  ILE   A CB    1 
ATOM   5480  C  CG1   . ILE   A  1  747  ? -32.714 73.318  119.293 1.00 23.59 ? 745  ILE   A CG1   1 
ATOM   5481  C  CG2   . ILE   A  1  747  ? -30.917 71.499  119.384 1.00 26.01 ? 745  ILE   A CG2   1 
ATOM   5482  C  CD1   . ILE   A  1  747  ? -32.932 73.401  117.807 1.00 24.08 ? 745  ILE   A CD1   1 
ATOM   5483  N  N     . LEU   A  1  748  ? -28.691 73.084  121.567 1.00 22.44 ? 746  LEU   A N     1 
ATOM   5484  C  CA    . LEU   A  1  748  ? -27.491 72.478  122.132 1.00 23.39 ? 746  LEU   A CA    1 
ATOM   5485  C  C     . LEU   A  1  748  ? -27.546 72.467  123.651 1.00 24.34 ? 746  LEU   A C     1 
ATOM   5486  O  O     . LEU   A  1  748  ? -27.179 71.474  124.291 1.00 24.32 ? 746  LEU   A O     1 
ATOM   5487  C  CB    . LEU   A  1  748  ? -26.260 73.231  121.641 1.00 21.99 ? 746  LEU   A CB    1 
ATOM   5488  C  CG    . LEU   A  1  748  ? -25.797 72.769  120.268 1.00 23.47 ? 746  LEU   A CG    1 
ATOM   5489  C  CD1   . LEU   A  1  748  ? -24.895 73.817  119.633 1.00 24.53 ? 746  LEU   A CD1   1 
ATOM   5490  C  CD2   . LEU   A  1  748  ? -25.066 71.449  120.398 1.00 26.18 ? 746  LEU   A CD2   1 
ATOM   5491  N  N     . ARG   A  1  749  ? -28.023 73.559  124.243 1.00 23.32 ? 747  ARG   A N     1 
ATOM   5492  C  CA    . ARG   A  1  749  ? -28.173 73.603  125.691 1.00 23.97 ? 747  ARG   A CA    1 
ATOM   5493  C  C     . ARG   A  1  749  ? -29.212 72.593  126.171 1.00 25.72 ? 747  ARG   A C     1 
ATOM   5494  O  O     . ARG   A  1  749  ? -28.995 71.900  127.173 1.00 28.10 ? 747  ARG   A O     1 
ATOM   5495  C  CB    . ARG   A  1  749  ? -28.502 75.028  126.140 1.00 27.13 ? 747  ARG   A CB    1 
ATOM   5496  C  CG    . ARG   A  1  749  ? -27.286 75.956  126.128 1.00 32.14 ? 747  ARG   A CG    1 
ATOM   5497  C  CD    . ARG   A  1  749  ? -27.637 77.347  126.615 1.00 36.40 ? 747  ARG   A CD    1 
ATOM   5498  N  NE    . ARG   A  1  749  ? -26.470 78.196  126.845 1.00 31.58 ? 747  ARG   A NE    1 
ATOM   5499  C  CZ    . ARG   A  1  749  ? -26.515 79.324  127.543 1.00 35.05 ? 747  ARG   A CZ    1 
ATOM   5500  N  NH1   . ARG   A  1  749  ? -27.645 79.757  128.078 1.00 32.87 ? 747  ARG   A NH1   1 
ATOM   5501  N  NH2   . ARG   A  1  749  ? -25.398 80.030  127.721 1.00 32.18 ? 747  ARG   A NH2   1 
ATOM   5502  N  N     . GLU   A  1  750  ? -30.333 72.470  125.456 1.00 24.22 ? 748  GLU   A N     1 
ATOM   5503  C  CA    . GLU   A  1  750  ? -31.313 71.448  125.816 1.00 28.25 ? 748  GLU   A CA    1 
ATOM   5504  C  C     . GLU   A  1  750  ? -30.715 70.048  125.716 1.00 26.51 ? 748  GLU   A C     1 
ATOM   5505  O  O     . GLU   A  1  750  ? -31.016 69.172  126.537 1.00 27.41 ? 748  GLU   A O     1 
ATOM   5506  C  CB    . GLU   A  1  750  ? -32.547 71.566  124.922 1.00 25.18 ? 748  GLU   A CB    1 
ATOM   5507  C  CG    . GLU   A  1  750  ? -33.624 70.559  125.259 1.00 30.37 ? 748  GLU   A CG    1 
ATOM   5508  C  CD    . GLU   A  1  750  ? -34.798 70.615  124.308 1.00 32.65 ? 748  GLU   A CD    1 
ATOM   5509  O  OE1   . GLU   A  1  750  ? -35.018 71.675  123.686 1.00 39.54 ? 748  GLU   A OE1   1 
ATOM   5510  O  OE2   . GLU   A  1  750  ? -35.488 69.585  124.174 1.00 31.82 ? 748  GLU   A OE2   1 
ATOM   5511  N  N     . ALA   A  1  751  ? -29.844 69.829  124.732 1.00 24.23 ? 749  ALA   A N     1 
ATOM   5512  C  CA    . ALA   A  1  751  ? -29.194 68.540  124.545 1.00 26.07 ? 749  ALA   A CA    1 
ATOM   5513  C  C     . ALA   A  1  751  ? -28.163 68.243  125.622 1.00 26.84 ? 749  ALA   A C     1 
ATOM   5514  O  O     . ALA   A  1  751  ? -27.630 67.128  125.657 1.00 28.02 ? 749  ALA   A O     1 
ATOM   5515  C  CB    . ALA   A  1  751  ? -28.524 68.490  123.172 1.00 23.19 ? 749  ALA   A CB    1 
ATOM   5516  N  N     . GLY   A  1  752  ? -27.850 69.211  126.476 1.00 25.13 ? 750  GLY   A N     1 
ATOM   5517  C  CA    . GLY   A  1  752  ? -27.010 68.970  127.633 1.00 27.36 ? 750  GLY   A CA    1 
ATOM   5518  C  C     . GLY   A  1  752  ? -25.729 69.771  127.668 1.00 26.02 ? 750  GLY   A C     1 
ATOM   5519  O  O     . GLY   A  1  752  ? -24.962 69.618  128.626 1.00 28.40 ? 750  GLY   A O     1 
ATOM   5520  N  N     . ILE   A  1  753  ? -25.444 70.613  126.679 1.00 26.47 ? 751  ILE   A N     1 
ATOM   5521  C  CA    . ILE   A  1  753  ? -24.266 71.472  126.745 1.00 27.31 ? 751  ILE   A CA    1 
ATOM   5522  C  C     . ILE   A  1  753  ? -24.506 72.480  127.857 1.00 25.20 ? 751  ILE   A C     1 
ATOM   5523  O  O     . ILE   A  1  753  ? -25.478 73.245  127.788 1.00 26.58 ? 751  ILE   A O     1 
ATOM   5524  C  CB    . ILE   A  1  753  ? -24.020 72.203  125.420 1.00 23.70 ? 751  ILE   A CB    1 
ATOM   5525  C  CG1   . ILE   A  1  753  ? -23.837 71.202  124.285 1.00 23.19 ? 751  ILE   A CG1   1 
ATOM   5526  C  CG2   . ILE   A  1  753  ? -22.794 73.089  125.546 1.00 26.06 ? 751  ILE   A CG2   1 
ATOM   5527  C  CD1   . ILE   A  1  753  ? -22.558 70.405  124.370 1.00 23.73 ? 751  ILE   A CD1   1 
ATOM   5528  N  N     . PRO   A  1  754  ? -23.665 72.525  128.887 1.00 27.70 ? 752  PRO   A N     1 
ATOM   5529  C  CA    . PRO   A  1  754  ? -23.887 73.488  129.968 1.00 28.44 ? 752  PRO   A CA    1 
ATOM   5530  C  C     . PRO   A  1  754  ? -23.791 74.918  129.461 1.00 28.04 ? 752  PRO   A C     1 
ATOM   5531  O  O     . PRO   A  1  754  ? -23.062 75.217  128.511 1.00 26.47 ? 752  PRO   A O     1 
ATOM   5532  C  CB    . PRO   A  1  754  ? -22.754 73.183  130.958 1.00 30.84 ? 752  PRO   A CB    1 
ATOM   5533  C  CG    . PRO   A  1  754  ? -22.187 71.868  130.552 1.00 27.80 ? 752  PRO   A CG    1 
ATOM   5534  C  CD    . PRO   A  1  754  ? -22.440 71.739  129.085 1.00 25.19 ? 752  PRO   A CD    1 
ATOM   5535  N  N     . ALA   A  1  755  ? -24.542 75.809  130.118 1.00 28.51 ? 753  ALA   A N     1 
ATOM   5536  C  CA    . ALA   A  1  755  ? -24.507 77.226  129.761 1.00 26.10 ? 753  ALA   A CA    1 
ATOM   5537  C  C     . ALA   A  1  755  ? -23.093 77.791  129.832 1.00 28.50 ? 753  ALA   A C     1 
ATOM   5538  O  O     . ALA   A  1  755  ? -22.741 78.688  129.058 1.00 29.23 ? 753  ALA   A O     1 
ATOM   5539  C  CB    . ALA   A  1  755  ? -25.430 78.018  130.690 1.00 30.43 ? 753  ALA   A CB    1 
ATOM   5540  N  N     . SER   A  1  756  ? -22.272 77.282  130.749 1.00 27.45 ? 754  SER   A N     1 
ATOM   5541  C  CA    . SER   A  1  756  ? -20.914 77.789  130.871 1.00 28.00 ? 754  SER   A CA    1 
ATOM   5542  C  C     . SER   A  1  756  ? -20.052 77.359  129.693 1.00 28.10 ? 754  SER   A C     1 
ATOM   5543  O  O     . SER   A  1  756  ? -19.078 78.041  129.358 1.00 28.97 ? 754  SER   A O     1 
ATOM   5544  C  CB    . SER   A  1  756  ? -20.297 77.297  132.173 1.00 29.20 ? 754  SER   A CB    1 
ATOM   5545  O  OG    . SER   A  1  756  ? -20.239 75.882  132.213 1.00 31.63 ? 754  SER   A OG    1 
ATOM   5546  N  N     . ALA   A  1  757  ? -20.399 76.241  129.050 1.00 27.12 ? 755  ALA   A N     1 
ATOM   5547  C  CA    . ALA   A  1  757  ? -19.640 75.734  127.916 1.00 24.15 ? 755  ALA   A CA    1 
ATOM   5548  C  C     . ALA   A  1  757  ? -20.067 76.340  126.591 1.00 27.05 ? 755  ALA   A C     1 
ATOM   5549  O  O     . ALA   A  1  757  ? -19.319 76.239  125.616 1.00 25.07 ? 755  ALA   A O     1 
ATOM   5550  C  CB    . ALA   A  1  757  ? -19.792 74.213  127.818 1.00 25.13 ? 755  ALA   A CB    1 
ATOM   5551  N  N     . LEU   A  1  758  ? -21.244 76.954  126.521 1.00 22.84 ? 756  LEU   A N     1 
ATOM   5552  C  CA    . LEU   A  1  758  ? -21.741 77.490  125.257 1.00 22.27 ? 756  LEU   A CA    1 
ATOM   5553  C  C     . LEU   A  1  758  ? -22.462 78.796  125.555 1.00 25.37 ? 756  LEU   A C     1 
ATOM   5554  O  O     . LEU   A  1  758  ? -23.585 78.790  126.061 1.00 27.18 ? 756  LEU   A O     1 
ATOM   5555  C  CB    . LEU   A  1  758  ? -22.660 76.500  124.566 1.00 24.63 ? 756  LEU   A CB    1 
ATOM   5556  C  CG    . LEU   A  1  758  ? -23.260 77.004  123.258 1.00 24.90 ? 756  LEU   A CG    1 
ATOM   5557  C  CD1   . LEU   A  1  758  ? -22.177 77.525  122.303 1.00 23.89 ? 756  LEU   A CD1   1 
ATOM   5558  C  CD2   . LEU   A  1  758  ? -24.055 75.888  122.619 1.00 24.67 ? 756  LEU   A CD2   1 
ATOM   5559  N  N     . GLN   A  1  759  ? -21.807 79.902  125.246 1.00 24.22 ? 757  GLN   A N     1 
ATOM   5560  C  CA    . GLN   A  1  759  ? -22.371 81.225  125.424 1.00 24.58 ? 757  GLN   A CA    1 
ATOM   5561  C  C     . GLN   A  1  759  ? -22.614 81.846  124.059 1.00 25.30 ? 757  GLN   A C     1 
ATOM   5562  O  O     . GLN   A  1  759  ? -21.747 81.797  123.180 1.00 26.60 ? 757  GLN   A O     1 
ATOM   5563  C  CB    . GLN   A  1  759  ? -21.433 82.096  126.257 1.00 25.24 ? 757  GLN   A CB    1 
ATOM   5564  C  CG    . GLN   A  1  759  ? -21.237 81.571  127.656 1.00 26.58 ? 757  GLN   A CG    1 
ATOM   5565  C  CD    . GLN   A  1  759  ? -20.235 82.388  128.424 1.00 26.33 ? 757  GLN   A CD    1 
ATOM   5566  O  OE1   . GLN   A  1  759  ? -20.591 83.361  129.095 1.00 27.43 ? 757  GLN   A OE1   1 
ATOM   5567  N  NE2   . GLN   A  1  759  ? -18.964 82.012  128.317 1.00 26.65 ? 757  GLN   A NE2   1 
ATOM   5568  N  N     . LEU   A  1  760  ? -23.801 82.392  123.875 1.00 25.37 ? 758  LEU   A N     1 
ATOM   5569  C  CA    . LEU   A  1  760  ? -24.186 83.039  122.632 1.00 25.18 ? 758  LEU   A CA    1 
ATOM   5570  C  C     . LEU   A  1  760  ? -24.000 84.536  122.799 1.00 25.50 ? 758  LEU   A C     1 
ATOM   5571  O  O     . LEU   A  1  760  ? -24.513 85.123  123.751 1.00 25.47 ? 758  LEU   A O     1 
ATOM   5572  C  CB    . LEU   A  1  760  ? -25.647 82.743  122.310 1.00 24.92 ? 758  LEU   A CB    1 
ATOM   5573  C  CG    . LEU   A  1  760  ? -26.158 83.453  121.057 1.00 26.59 ? 758  LEU   A CG    1 
ATOM   5574  C  CD1   . LEU   A  1  760  ? -25.683 82.733  119.800 1.00 25.07 ? 758  LEU   A CD1   1 
ATOM   5575  C  CD2   . LEU   A  1  760  ? -27.672 83.577  121.080 1.00 26.64 ? 758  LEU   A CD2   1 
ATOM   5576  N  N     . LEU   A  1  761  ? -23.261 85.149  121.882 1.00 24.99 ? 759  LEU   A N     1 
ATOM   5577  C  CA    A LEU   A  1  761  ? -22.941 86.573  121.946 0.43 26.08 ? 759  LEU   A CA    1 
ATOM   5578  C  CA    B LEU   A  1  761  ? -22.937 86.575  121.945 0.57 26.09 ? 759  LEU   A CA    1 
ATOM   5579  C  C     . LEU   A  1  761  ? -23.340 87.224  120.630 1.00 25.57 ? 759  LEU   A C     1 
ATOM   5580  O  O     . LEU   A  1  761  ? -22.509 87.399  119.730 1.00 24.57 ? 759  LEU   A O     1 
ATOM   5581  C  CB    A LEU   A  1  761  ? -21.462 86.775  122.272 0.43 25.68 ? 759  LEU   A CB    1 
ATOM   5582  C  CB    B LEU   A  1  761  ? -21.450 86.804  122.222 0.57 25.69 ? 759  LEU   A CB    1 
ATOM   5583  C  CG    A LEU   A  1  761  ? -21.072 86.050  123.563 0.43 25.22 ? 759  LEU   A CG    1 
ATOM   5584  C  CG    B LEU   A  1  761  ? -20.817 86.245  123.500 0.57 25.10 ? 759  LEU   A CG    1 
ATOM   5585  C  CD1   A LEU   A  1  761  ? -19.578 85.846  123.664 0.43 25.29 ? 759  LEU   A CD1   1 
ATOM   5586  C  CD1   B LEU   A  1  761  ? -21.740 86.410  124.706 0.57 24.63 ? 759  LEU   A CD1   1 
ATOM   5587  C  CD2   A LEU   A  1  761  ? -21.595 86.805  124.775 0.43 25.46 ? 759  LEU   A CD2   1 
ATOM   5588  C  CD2   B LEU   A  1  761  ? -20.404 84.791  123.309 0.57 25.09 ? 759  LEU   A CD2   1 
ATOM   5589  N  N     . PRO   A  1  762  ? -24.609 87.589  120.480 1.00 24.02 ? 760  PRO   A N     1 
ATOM   5590  C  CA    . PRO   A  1  762  ? -25.039 88.252  119.244 1.00 25.74 ? 760  PRO   A CA    1 
ATOM   5591  C  C     . PRO   A  1  762  ? -24.399 89.623  119.114 1.00 27.62 ? 760  PRO   A C     1 
ATOM   5592  O  O     . PRO   A  1  762  ? -24.043 90.267  120.103 1.00 27.58 ? 760  PRO   A O     1 
ATOM   5593  C  CB    . PRO   A  1  762  ? -26.558 88.382  119.421 1.00 24.01 ? 760  PRO   A CB    1 
ATOM   5594  C  CG    . PRO   A  1  762  ? -26.911 87.404  120.491 1.00 24.92 ? 760  PRO   A CG    1 
ATOM   5595  C  CD    . PRO   A  1  762  ? -25.734 87.347  121.399 1.00 23.52 ? 760  PRO   A CD    1 
ATOM   5596  N  N     . GLY   A  1  763  ? -24.263 90.074  117.882 1.00 24.21 ? 761  GLY   A N     1 
ATOM   5597  C  CA    . GLY   A  1  763  ? -23.751 91.399  117.616 1.00 27.00 ? 761  GLY   A CA    1 
ATOM   5598  C  C     . GLY   A  1  763  ? -22.947 91.401  116.335 1.00 26.81 ? 761  GLY   A C     1 
ATOM   5599  O  O     . GLY   A  1  763  ? -22.878 90.403  115.621 1.00 24.34 ? 761  GLY   A O     1 
ATOM   5600  N  N     . ASP   A  1  764  ? -22.318 92.541  116.069 1.00 28.47 ? 762  ASP   A N     1 
ATOM   5601  C  CA    . ASP   A  1  764  ? -21.634 92.738  114.799 1.00 29.90 ? 762  ASP   A CA    1 
ATOM   5602  C  C     . ASP   A  1  764  ? -20.159 92.347  114.924 1.00 29.35 ? 762  ASP   A C     1 
ATOM   5603  O  O     . ASP   A  1  764  ? -19.759 91.635  115.850 1.00 26.06 ? 762  ASP   A O     1 
ATOM   5604  C  CB    . ASP   A  1  764  ? -21.880 94.158  114.273 1.00 33.02 ? 762  ASP   A CB    1 
ATOM   5605  C  CG    . ASP   A  1  764  ? -21.351 95.232  115.209 1.00 33.93 ? 762  ASP   A CG    1 
ATOM   5606  O  OD1   . ASP   A  1  764  ? -20.483 94.928  116.050 1.00 35.79 ? 762  ASP   A OD1   1 
ATOM   5607  O  OD2   . ASP   A  1  764  ? -21.820 96.386  115.114 1.00 43.41 ? 762  ASP   A OD2   1 
ATOM   5608  N  N     . GLY   A  1  765  ? -19.335 92.814  113.985 1.00 27.27 ? 763  GLY   A N     1 
ATOM   5609  C  CA    . GLY   A  1  765  ? -17.923 92.476  113.994 1.00 26.49 ? 763  GLY   A CA    1 
ATOM   5610  C  C     . GLY   A  1  765  ? -17.185 92.969  115.221 1.00 28.48 ? 763  GLY   A C     1 
ATOM   5611  O  O     . GLY   A  1  765  ? -16.134 92.417  115.564 1.00 30.55 ? 763  GLY   A O     1 
ATOM   5612  N  N     . ARG   A  1  766  ? -17.713 93.996  115.891 1.00 29.41 ? 764  ARG   A N     1 
ATOM   5613  C  CA    . ARG   A  1  766  ? -17.096 94.477  117.122 1.00 30.11 ? 764  ARG   A CA    1 
ATOM   5614  C  C     . ARG   A  1  766  ? -17.139 93.416  118.206 1.00 30.14 ? 764  ARG   A C     1 
ATOM   5615  O  O     . ARG   A  1  766  ? -16.218 93.320  119.025 1.00 29.67 ? 764  ARG   A O     1 
ATOM   5616  C  CB    . ARG   A  1  766  ? -17.835 95.706  117.636 1.00 36.15 ? 764  ARG   A CB    1 
ATOM   5617  C  CG    . ARG   A  1  766  ? -17.645 96.964  116.848 1.00 39.50 ? 764  ARG   A CG    1 
ATOM   5618  C  CD    . ARG   A  1  766  ? -18.573 98.000  117.427 1.00 38.17 ? 764  ARG   A CD    1 
ATOM   5619  N  NE    . ARG   A  1  766  ? -19.963 97.595  117.260 1.00 42.05 ? 764  ARG   A NE    1 
ATOM   5620  C  CZ    . ARG   A  1  766  ? -20.945 97.919  118.089 1.00 43.40 ? 764  ARG   A CZ    1 
ATOM   5621  N  NH1   . ARG   A  1  766  ? -20.717 98.607  119.195 1.00 49.20 ? 764  ARG   A NH1   1 
ATOM   5622  N  NH2   . ARG   A  1  766  ? -22.187 97.541  117.801 1.00 45.72 ? 764  ARG   A NH2   1 
ATOM   5623  N  N     . VAL   A  1  767  ? -18.235 92.659  118.273 1.00 26.51 ? 765  VAL   A N     1 
ATOM   5624  C  CA    . VAL   A  1  767  ? -18.318 91.592  119.262 1.00 28.75 ? 765  VAL   A CA    1 
ATOM   5625  C  C     . VAL   A  1  767  ? -17.341 90.485  118.910 1.00 25.47 ? 765  VAL   A C     1 
ATOM   5626  O  O     . VAL   A  1  767  ? -16.640 89.956  119.778 1.00 27.10 ? 765  VAL   A O     1 
ATOM   5627  C  CB    . VAL   A  1  767  ? -19.766 91.083  119.389 1.00 24.77 ? 765  VAL   A CB    1 
ATOM   5628  C  CG1   . VAL   A  1  767  ? -19.864 90.015  120.468 1.00 27.75 ? 765  VAL   A CG1   1 
ATOM   5629  C  CG2   . VAL   A  1  767  ? -20.707 92.236  119.693 1.00 29.27 ? 765  VAL   A CG2   1 
ATOM   5630  N  N     . GLY   A  1  768  ? -17.273 90.121  117.626 1.00 26.89 ? 766  GLY   A N     1 
ATOM   5631  C  CA    . GLY   A  1  768  ? -16.281 89.153  117.198 1.00 25.14 ? 766  GLY   A CA    1 
ATOM   5632  C  C     . GLY   A  1  768  ? -14.870 89.606  117.510 1.00 23.44 ? 766  GLY   A C     1 
ATOM   5633  O  O     . GLY   A  1  768  ? -14.060 88.838  118.023 1.00 24.69 ? 766  GLY   A O     1 
ATOM   5634  N  N     . ALA   A  1  769  ? -14.566 90.872  117.224 1.00 25.54 ? 767  ALA   A N     1 
ATOM   5635  C  CA    . ALA   A  1  769  ? -13.215 91.371  117.462 1.00 28.46 ? 767  ALA   A CA    1 
ATOM   5636  C  C     . ALA   A  1  769  ? -12.894 91.393  118.951 1.00 26.05 ? 767  ALA   A C     1 
ATOM   5637  O  O     . ALA   A  1  769  ? -11.777 91.052  119.356 1.00 28.10 ? 767  ALA   A O     1 
ATOM   5638  C  CB    . ALA   A  1  769  ? -13.054 92.765  116.857 1.00 28.47 ? 767  ALA   A CB    1 
ATOM   5639  N  N     . ALA   A  1  770  ? -13.867 91.784  119.777 1.00 26.78 ? 768  ALA   A N     1 
ATOM   5640  C  CA    . ALA   A  1  770  ? -13.641 91.806  121.219 1.00 27.25 ? 768  ALA   A CA    1 
ATOM   5641  C  C     . ALA   A  1  770  ? -13.359 90.406  121.739 1.00 26.92 ? 768  ALA   A C     1 
ATOM   5642  O  O     . ALA   A  1  770  ? -12.532 90.220  122.641 1.00 27.79 ? 768  ALA   A O     1 
ATOM   5643  C  CB    . ALA   A  1  770  ? -14.852 92.406  121.926 1.00 27.67 ? 768  ALA   A CB    1 
ATOM   5644  N  N     . LEU   A  1  771  ? -14.033 89.405  121.170 1.00 25.51 ? 769  LEU   A N     1 
ATOM   5645  C  CA    . LEU   A  1  771  ? -13.814 88.027  121.585 1.00 27.40 ? 769  LEU   A CA    1 
ATOM   5646  C  C     . LEU   A  1  771  ? -12.440 87.545  121.150 1.00 26.88 ? 769  LEU   A C     1 
ATOM   5647  O  O     . LEU   A  1  771  ? -11.713 86.922  121.929 1.00 27.37 ? 769  LEU   A O     1 
ATOM   5648  C  CB    . LEU   A  1  771  ? -14.913 87.134  121.001 1.00 24.77 ? 769  LEU   A CB    1 
ATOM   5649  C  CG    . LEU   A  1  771  ? -16.323 87.402  121.532 1.00 24.65 ? 769  LEU   A CG    1 
ATOM   5650  C  CD1   . LEU   A  1  771  ? -17.354 86.581  120.741 1.00 25.91 ? 769  LEU   A CD1   1 
ATOM   5651  C  CD2   . LEU   A  1  771  ? -16.394 87.106  123.017 1.00 27.94 ? 769  LEU   A CD2   1 
ATOM   5652  N  N     . VAL   A  1  772  ? -12.074 87.823  119.897 1.00 25.81 ? 770  VAL   A N     1 
ATOM   5653  C  CA    . VAL   A  1  772  ? -10.770 87.415  119.384 1.00 24.86 ? 770  VAL   A CA    1 
ATOM   5654  C  C     . VAL   A  1  772  ? -9.654  88.008  120.233 1.00 27.23 ? 770  VAL   A C     1 
ATOM   5655  O  O     . VAL   A  1  772  ? -8.670  87.332  120.545 1.00 29.01 ? 770  VAL   A O     1 
ATOM   5656  C  CB    . VAL   A  1  772  ? -10.638 87.803  117.899 1.00 23.91 ? 770  VAL   A CB    1 
ATOM   5657  C  CG1   . VAL   A  1  772  ? -9.200  87.659  117.435 1.00 26.08 ? 770  VAL   A CG1   1 
ATOM   5658  C  CG2   . VAL   A  1  772  ? -11.548 86.931  117.044 1.00 23.48 ? 770  VAL   A CG2   1 
ATOM   5659  N  N     . ALA   A  1  773  ? -9.795  89.272  120.623 1.00 28.01 ? 771  ALA   A N     1 
ATOM   5660  C  CA    . ALA   A  1  773  ? -8.743  89.972  121.352 1.00 27.08 ? 771  ALA   A CA    1 
ATOM   5661  C  C     . ALA   A  1  773  ? -8.688  89.611  122.831 1.00 32.62 ? 771  ALA   A C     1 
ATOM   5662  O  O     . ALA   A  1  773  ? -7.719  89.985  123.502 1.00 34.68 ? 771  ALA   A O     1 
ATOM   5663  C  CB    . ALA   A  1  773  ? -8.932  91.481  121.207 1.00 31.50 ? 771  ALA   A CB    1 
ATOM   5664  N  N     . ALA   A  1  774  ? -9.687  88.904  123.353 1.00 31.22 ? 772  ALA   A N     1 
ATOM   5665  C  CA    . ALA   A  1  774  ? -9.731  88.613  124.782 1.00 31.63 ? 772  ALA   A CA    1 
ATOM   5666  C  C     . ALA   A  1  774  ? -8.589  87.684  125.173 1.00 29.38 ? 772  ALA   A C     1 
ATOM   5667  O  O     . ALA   A  1  774  ? -8.265  86.730  124.464 1.00 30.29 ? 772  ALA   A O     1 
ATOM   5668  C  CB    . ALA   A  1  774  ? -11.078 87.996  125.154 1.00 32.82 ? 772  ALA   A CB    1 
ATOM   5669  N  N     . ALA   A  1  775  ? -7.971  87.970  126.324 1.00 36.48 ? 773  ALA   A N     1 
ATOM   5670  C  CA    . ALA   A  1  775  ? -6.715  87.312  126.663 1.00 36.61 ? 773  ALA   A CA    1 
ATOM   5671  C  C     . ALA   A  1  775  ? -6.867  85.804  126.826 1.00 29.77 ? 773  ALA   A C     1 
ATOM   5672  O  O     . ALA   A  1  775  ? -5.925  85.058  126.547 1.00 32.33 ? 773  ALA   A O     1 
ATOM   5673  C  CB    . ALA   A  1  775  ? -6.113  87.935  127.922 1.00 35.85 ? 773  ALA   A CB    1 
ATOM   5674  N  N     . GLU   A  1  776  ? -8.029  85.333  127.271 1.00 28.74 ? 774  GLU   A N     1 
ATOM   5675  C  CA    . GLU   A  1  776  ? -8.210  83.907  127.511 1.00 26.98 ? 774  GLU   A CA    1 
ATOM   5676  C  C     . GLU   A  1  776  ? -8.658  83.140  126.272 1.00 27.36 ? 774  GLU   A C     1 
ATOM   5677  O  O     . GLU   A  1  776  ? -8.829  81.920  126.343 1.00 28.09 ? 774  GLU   A O     1 
ATOM   5678  C  CB    . GLU   A  1  776  ? -9.197  83.674  128.657 1.00 30.16 ? 774  GLU   A CB    1 
ATOM   5679  C  CG    . GLU   A  1  776  ? -8.811  84.350  129.967 1.00 32.98 ? 774  GLU   A CG    1 
ATOM   5680  C  CD    . GLU   A  1  776  ? -9.368  85.762  130.104 1.00 40.65 ? 774  GLU   A CD    1 
ATOM   5681  O  OE1   . GLU   A  1  776  ? -9.910  86.312  129.119 1.00 34.11 ? 774  GLU   A OE1   1 
ATOM   5682  O  OE2   . GLU   A  1  776  ? -9.258  86.328  131.213 1.00 42.03 ? 774  GLU   A OE2   1 
ATOM   5683  N  N     . THR   A  1  777  ? -8.839  83.813  125.144 1.00 24.24 ? 775  THR   A N     1 
ATOM   5684  C  CA    . THR   A  1  777  ? -9.237  83.127  123.921 1.00 24.31 ? 775  THR   A CA    1 
ATOM   5685  C  C     . THR   A  1  777  ? -8.104  82.229  123.449 1.00 26.57 ? 775  THR   A C     1 
ATOM   5686  O  O     . THR   A  1  777  ? -6.985  82.697  123.207 1.00 28.43 ? 775  THR   A O     1 
ATOM   5687  C  CB    . THR   A  1  777  ? -9.598  84.154  122.859 1.00 23.96 ? 775  THR   A CB    1 
ATOM   5688  O  OG1   . THR   A  1  777  ? -10.806 84.804  123.255 1.00 25.30 ? 775  THR   A OG1   1 
ATOM   5689  C  CG2   . THR   A  1  777  ? -9.787  83.462  121.498 1.00 22.67 ? 775  THR   A CG2   1 
ATOM   5690  N  N     . ALA   A  1  778  ? -8.387  80.933  123.351 1.00 23.33 ? 776  ALA   A N     1 
ATOM   5691  C  CA    . ALA   A  1  778  ? -7.367  79.935  123.075 1.00 22.15 ? 776  ALA   A CA    1 
ATOM   5692  C  C     . ALA   A  1  778  ? -7.386  79.453  121.635 1.00 22.81 ? 776  ALA   A C     1 
ATOM   5693  O  O     . ALA   A  1  778  ? -6.469  78.741  121.223 1.00 22.82 ? 776  ALA   A O     1 
ATOM   5694  C  CB    . ALA   A  1  778  ? -7.540  78.738  124.020 1.00 23.66 ? 776  ALA   A CB    1 
ATOM   5695  N  N     . GLY   A  1  779  ? -8.404  79.815  120.872 1.00 21.40 ? 777  GLY   A N     1 
ATOM   5696  C  CA    . GLY   A  1  779  ? -8.489  79.437  119.483 1.00 20.63 ? 777  GLY   A CA    1 
ATOM   5697  C  C     . GLY   A  1  779  ? -9.660  80.155  118.866 1.00 20.03 ? 777  GLY   A C     1 
ATOM   5698  O  O     . GLY   A  1  779  ? -10.589 80.582  119.562 1.00 21.11 ? 777  GLY   A O     1 
ATOM   5699  N  N     . VAL   A  1  780  ? -9.596  80.299  117.552 1.00 20.25 ? 778  VAL   A N     1 
ATOM   5700  C  CA    . VAL   A  1  780  ? -10.609 81.024  116.807 1.00 19.73 ? 778  VAL   A CA    1 
ATOM   5701  C  C     . VAL   A  1  780  ? -11.009 80.181  115.610 1.00 19.16 ? 778  VAL   A C     1 
ATOM   5702  O  O     . VAL   A  1  780  ? -10.150 79.725  114.848 1.00 19.34 ? 778  VAL   A O     1 
ATOM   5703  C  CB    . VAL   A  1  780  ? -10.116 82.416  116.369 1.00 21.57 ? 778  VAL   A CB    1 
ATOM   5704  C  CG1   . VAL   A  1  780  ? -11.223 83.163  115.648 1.00 20.23 ? 778  VAL   A CG1   1 
ATOM   5705  C  CG2   . VAL   A  1  780  ? -9.658  83.219  117.584 1.00 21.54 ? 778  VAL   A CG2   1 
ATOM   5706  N  N     . MET   A  1  781  ? -12.301 79.953  115.463 1.00 18.60 ? 779  MET   A N     1 
ATOM   5707  C  CA    . MET   A  1  781  ? -12.851 79.296  114.288 1.00 17.18 ? 779  MET   A CA    1 
ATOM   5708  C  C     . MET   A  1  781  ? -13.669 80.353  113.576 1.00 18.68 ? 779  MET   A C     1 
ATOM   5709  O  O     . MET   A  1  781  ? -14.676 80.830  114.111 1.00 18.87 ? 779  MET   A O     1 
ATOM   5710  C  CB    . MET   A  1  781  ? -13.720 78.115  114.700 1.00 20.79 ? 779  MET   A CB    1 
ATOM   5711  C  CG    . MET   A  1  781  ? -12.966 77.102  115.519 1.00 19.02 ? 779  MET   A CG    1 
ATOM   5712  S  SD    . MET   A  1  781  ? -14.063 75.836  116.126 1.00 20.05 ? 779  MET   A SD    1 
ATOM   5713  C  CE    . MET   A  1  781  ? -14.309 74.887  114.633 1.00 19.53 ? 779  MET   A CE    1 
ATOM   5714  N  N     . PHE   A  1  782  ? -13.213 80.740  112.393 1.00 20.20 ? 780  PHE   A N     1 
ATOM   5715  C  CA    . PHE   A  1  782  ? -13.820 81.797  111.613 1.00 18.61 ? 780  PHE   A CA    1 
ATOM   5716  C  C     . PHE   A  1  782  ? -14.250 81.245  110.266 1.00 19.34 ? 780  PHE   A C     1 
ATOM   5717  O  O     . PHE   A  1  782  ? -13.456 80.604  109.566 1.00 18.43 ? 780  PHE   A O     1 
ATOM   5718  C  CB    . PHE   A  1  782  ? -12.829 82.935  111.358 1.00 18.89 ? 780  PHE   A CB    1 
ATOM   5719  C  CG    . PHE   A  1  782  ? -13.379 83.994  110.448 1.00 19.02 ? 780  PHE   A CG    1 
ATOM   5720  C  CD1   . PHE   A  1  782  ? -14.246 84.952  110.941 1.00 20.29 ? 780  PHE   A CD1   1 
ATOM   5721  C  CD2   . PHE   A  1  782  ? -13.062 84.011  109.097 1.00 19.71 ? 780  PHE   A CD2   1 
ATOM   5722  C  CE1   . PHE   A  1  782  ? -14.770 85.912  110.122 1.00 20.93 ? 780  PHE   A CE1   1 
ATOM   5723  C  CE2   . PHE   A  1  782  ? -13.589 84.974  108.271 1.00 19.97 ? 780  PHE   A CE2   1 
ATOM   5724  C  CZ    . PHE   A  1  782  ? -14.435 85.927  108.784 1.00 19.32 ? 780  PHE   A CZ    1 
ATOM   5725  N  N     . THR   A  1  783  ? -15.493 81.518  109.901 1.00 17.53 ? 781  THR   A N     1 
ATOM   5726  C  CA    . THR   A  1  783  ? -15.956 81.328  108.537 1.00 18.78 ? 781  THR   A CA    1 
ATOM   5727  C  C     . THR   A  1  783  ? -16.598 82.634  108.109 1.00 17.19 ? 781  THR   A C     1 
ATOM   5728  O  O     . THR   A  1  783  ? -17.434 83.184  108.827 1.00 18.83 ? 781  THR   A O     1 
ATOM   5729  C  CB    . THR   A  1  783  ? -16.933 80.156  108.435 1.00 19.26 ? 781  THR   A CB    1 
ATOM   5730  O  OG1   . THR   A  1  783  ? -16.295 78.973  108.929 1.00 18.60 ? 781  THR   A OG1   1 
ATOM   5731  C  CG2   . THR   A  1  783  ? -17.335 79.927  106.992 1.00 19.44 ? 781  THR   A CG2   1 
ATOM   5732  N  N     . GLY   A  1  784  ? -16.172 83.150  106.964 1.00 18.73 ? 782  GLY   A N     1 
ATOM   5733  C  CA    . GLY   A  1  784  ? -16.599 84.470  106.554 1.00 18.73 ? 782  GLY   A CA    1 
ATOM   5734  C  C     . GLY   A  1  784  ? -15.720 84.955  105.424 1.00 16.85 ? 782  GLY   A C     1 
ATOM   5735  O  O     . GLY   A  1  784  ? -15.047 84.159  104.765 1.00 20.36 ? 782  GLY   A O     1 
ATOM   5736  N  N     . SER   A  1  785  ? -15.716 86.267  105.229 1.00 19.70 ? 783  SER   A N     1 
ATOM   5737  C  CA    . SER   A  1  785  ? -14.973 86.829  104.112 1.00 20.64 ? 783  SER   A CA    1 
ATOM   5738  C  C     . SER   A  1  785  ? -13.470 86.793  104.372 1.00 21.27 ? 783  SER   A C     1 
ATOM   5739  O  O     . SER   A  1  785  ? -12.999 86.860  105.514 1.00 20.98 ? 783  SER   A O     1 
ATOM   5740  C  CB    . SER   A  1  785  ? -15.414 88.265  103.859 1.00 23.85 ? 783  SER   A CB    1 
ATOM   5741  O  OG    . SER   A  1  785  ? -15.097 89.078  104.966 1.00 23.88 ? 783  SER   A OG    1 
ATOM   5742  N  N     . THR   A  1  786  ? -12.710 86.680  103.281 1.00 21.67 ? 784  THR   A N     1 
ATOM   5743  C  CA    . THR   A  1  786  ? -11.257 86.678  103.385 1.00 21.92 ? 784  THR   A CA    1 
ATOM   5744  C  C     . THR   A  1  786  ? -10.744 87.958  104.032 1.00 21.29 ? 784  THR   A C     1 
ATOM   5745  O  O     . THR   A  1  786  ? -9.799  87.927  104.831 1.00 21.69 ? 784  THR   A O     1 
ATOM   5746  C  CB    . THR   A  1  786  ? -10.657 86.492  101.996 1.00 22.79 ? 784  THR   A CB    1 
ATOM   5747  O  OG1   . THR   A  1  786  ? -11.162 85.279  101.436 1.00 23.19 ? 784  THR   A OG1   1 
ATOM   5748  C  CG2   . THR   A  1  786  ? -9.144  86.432  102.086 1.00 24.56 ? 784  THR   A CG2   1 
ATOM   5749  N  N     . GLU   A  1  787  ? -11.380 89.090  103.725 1.00 24.59 ? 785  GLU   A N     1 
ATOM   5750  C  CA    . GLU   A  1  787  ? -10.928 90.365  104.263 1.00 22.58 ? 785  GLU   A CA    1 
ATOM   5751  C  C     . GLU   A  1  787  ? -11.084 90.415  105.779 1.00 23.26 ? 785  GLU   A C     1 
ATOM   5752  O  O     . GLU   A  1  787  ? -10.210 90.926  106.487 1.00 23.03 ? 785  GLU   A O     1 
ATOM   5753  C  CB    . GLU   A  1  787  ? -11.697 91.510  103.601 1.00 27.27 ? 785  GLU   A CB    1 
ATOM   5754  N  N     . VAL   A  1  788  ? -12.185 89.876  106.297 1.00 22.71 ? 786  VAL   A N     1 
ATOM   5755  C  CA    . VAL   A  1  788  ? -12.358 89.859  107.747 1.00 21.98 ? 786  VAL   A CA    1 
ATOM   5756  C  C     . VAL   A  1  788  ? -11.392 88.875  108.391 1.00 23.76 ? 786  VAL   A C     1 
ATOM   5757  O  O     . VAL   A  1  788  ? -10.788 89.166  109.431 1.00 22.14 ? 786  VAL   A O     1 
ATOM   5758  C  CB    . VAL   A  1  788  ? -13.825 89.579  108.117 1.00 22.47 ? 786  VAL   A CB    1 
ATOM   5759  C  CG1   . VAL   A  1  788  ? -13.947 89.265  109.599 1.00 23.82 ? 786  VAL   A CG1   1 
ATOM   5760  C  CG2   . VAL   A  1  788  ? -14.681 90.787  107.770 1.00 23.57 ? 786  VAL   A CG2   1 
ATOM   5761  N  N     . ALA   A  1  789  ? -11.211 87.703  107.778 1.00 20.70 ? 787  ALA   A N     1 
ATOM   5762  C  CA    . ALA   A  1  789  ? -10.234 86.751  108.291 1.00 21.69 ? 787  ALA   A CA    1 
ATOM   5763  C  C     . ALA   A  1  789  ? -8.862  87.392  108.407 1.00 19.83 ? 787  ALA   A C     1 
ATOM   5764  O  O     . ALA   A  1  789  ? -8.131  87.145  109.371 1.00 19.46 ? 787  ALA   A O     1 
ATOM   5765  C  CB    . ALA   A  1  789  ? -10.174 85.531  107.378 1.00 17.52 ? 787  ALA   A CB    1 
ATOM   5766  N  N     . ARG   A  1  790  ? -8.507  88.244  107.444 1.00 21.56 ? 788  ARG   A N     1 
ATOM   5767  C  CA    . ARG   A  1  790  ? -7.209  88.903  107.478 1.00 21.82 ? 788  ARG   A CA    1 
ATOM   5768  C  C     . ARG   A  1  790  ? -7.096  89.849  108.669 1.00 21.20 ? 788  ARG   A C     1 
ATOM   5769  O  O     . ARG   A  1  790  ? -6.031  89.952  109.287 1.00 22.40 ? 788  ARG   A O     1 
ATOM   5770  C  CB    . ARG   A  1  790  ? -6.994  89.637  106.155 1.00 25.24 ? 788  ARG   A CB    1 
ATOM   5771  C  CG    . ARG   A  1  790  ? -5.633  90.278  105.998 1.00 23.47 ? 788  ARG   A CG    1 
ATOM   5772  C  CD    . ARG   A  1  790  ? -5.443  90.799  104.569 1.00 24.42 ? 788  ARG   A CD    1 
ATOM   5773  N  NE    . ARG   A  1  790  ? -5.389  89.715  103.591 1.00 22.94 ? 788  ARG   A NE    1 
ATOM   5774  C  CZ    . ARG   A  1  790  ? -6.218  89.563  102.565 1.00 20.74 ? 788  ARG   A CZ    1 
ATOM   5775  N  NH1   . ARG   A  1  790  ? -7.190  90.426  102.321 1.00 25.94 ? 788  ARG   A NH1   1 
ATOM   5776  N  NH2   . ARG   A  1  790  ? -6.057  88.519  101.755 1.00 25.88 ? 788  ARG   A NH2   1 
ATOM   5777  N  N     . LEU   A  1  791  ? -8.193  90.536  109.017 1.00 22.88 ? 789  LEU   A N     1 
ATOM   5778  C  CA    . LEU   A  1  791  ? -8.195  91.363  110.218 1.00 23.80 ? 789  LEU   A CA    1 
ATOM   5779  C  C     . LEU   A  1  791  ? -8.027  90.509  111.466 1.00 23.06 ? 789  LEU   A C     1 
ATOM   5780  O  O     . LEU   A  1  791  ? -7.304  90.884  112.393 1.00 23.75 ? 789  LEU   A O     1 
ATOM   5781  C  CB    . LEU   A  1  791  ? -9.497  92.152  110.297 1.00 22.95 ? 789  LEU   A CB    1 
ATOM   5782  C  CG    . LEU   A  1  791  ? -9.755  93.184  109.195 1.00 27.55 ? 789  LEU   A CG    1 
ATOM   5783  C  CD1   . LEU   A  1  791  ? -11.165 93.726  109.285 1.00 30.06 ? 789  LEU   A CD1   1 
ATOM   5784  C  CD2   . LEU   A  1  791  ? -8.746  94.304  109.291 1.00 29.59 ? 789  LEU   A CD2   1 
ATOM   5785  N  N     . ILE   A  1  792  ? -8.707  89.364  111.515 1.00 21.46 ? 790  ILE   A N     1 
ATOM   5786  C  CA    . ILE   A  1  792  ? -8.561  88.469  112.660 1.00 22.69 ? 790  ILE   A CA    1 
ATOM   5787  C  C     . ILE   A  1  792  ? -7.139  87.935  112.745 1.00 23.78 ? 790  ILE   A C     1 
ATOM   5788  O  O     . ILE   A  1  792  ? -6.547  87.878  113.830 1.00 24.12 ? 790  ILE   A O     1 
ATOM   5789  C  CB    . ILE   A  1  792  ? -9.614  87.348  112.594 1.00 21.93 ? 790  ILE   A CB    1 
ATOM   5790  C  CG1   . ILE   A  1  792  ? -10.996 87.947  112.815 1.00 23.62 ? 790  ILE   A CG1   1 
ATOM   5791  C  CG2   . ILE   A  1  792  ? -9.305  86.245  113.609 1.00 25.73 ? 790  ILE   A CG2   1 
ATOM   5792  C  CD1   . ILE   A  1  792  ? -12.127 87.004  112.517 1.00 21.54 ? 790  ILE   A CD1   1 
ATOM   5793  N  N     . GLN   A  1  793  ? -6.568  87.546  111.604 1.00 21.35 ? 791  GLN   A N     1 
ATOM   5794  C  CA    . GLN   A  1  793  ? -5.187  87.085  111.568 1.00 22.21 ? 791  GLN   A CA    1 
ATOM   5795  C  C     . GLN   A  1  793  ? -4.246  88.138  112.138 1.00 23.01 ? 791  GLN   A C     1 
ATOM   5796  O  O     . GLN   A  1  793  ? -3.334  87.816  112.909 1.00 23.30 ? 791  GLN   A O     1 
ATOM   5797  C  CB    . GLN   A  1  793  ? -4.820  86.743  110.123 1.00 23.21 ? 791  GLN   A CB    1 
ATOM   5798  C  CG    . GLN   A  1  793  ? -3.361  86.413  109.888 1.00 23.22 ? 791  GLN   A CG    1 
ATOM   5799  C  CD    . GLN   A  1  793  ? -2.993  86.470  108.407 1.00 25.71 ? 791  GLN   A CD    1 
ATOM   5800  O  OE1   . GLN   A  1  793  ? -3.436  87.362  107.679 1.00 28.68 ? 791  GLN   A OE1   1 
ATOM   5801  N  NE2   . GLN   A  1  793  ? -2.207  85.503  107.951 1.00 25.53 ? 791  GLN   A NE2   1 
ATOM   5802  N  N     . ALA   A  1  794  ? -4.473  89.406  111.792 1.00 24.13 ? 792  ALA   A N     1 
ATOM   5803  C  CA    . ALA   A  1  794  ? -3.628  90.471  112.318 1.00 27.56 ? 792  ALA   A CA    1 
ATOM   5804  C  C     . ALA   A  1  794  ? -3.805  90.620  113.824 1.00 26.38 ? 792  ALA   A C     1 
ATOM   5805  O  O     . ALA   A  1  794  ? -2.826  90.815  114.549 1.00 28.96 ? 792  ALA   A O     1 
ATOM   5806  C  CB    . ALA   A  1  794  ? -3.949  91.781  111.605 1.00 26.99 ? 792  ALA   A CB    1 
ATOM   5807  N  N     . GLN   A  1  795  ? -5.047  90.525  114.303 1.00 25.32 ? 793  GLN   A N     1 
ATOM   5808  C  CA    . GLN   A  1  795  ? -5.320  90.583  115.737 1.00 25.85 ? 793  GLN   A CA    1 
ATOM   5809  C  C     . GLN   A  1  795  ? -4.552  89.498  116.478 1.00 29.93 ? 793  GLN   A C     1 
ATOM   5810  O  O     . GLN   A  1  795  ? -3.894  89.760  117.493 1.00 29.91 ? 793  GLN   A O     1 
ATOM   5811  C  CB    . GLN   A  1  795  ? -6.817  90.371  115.956 1.00 33.66 ? 793  GLN   A CB    1 
ATOM   5812  C  CG    . GLN   A  1  795  ? -7.570  91.475  116.655 1.00 39.38 ? 793  GLN   A CG    1 
ATOM   5813  C  CD    . GLN   A  1  795  ? -9.060  91.163  116.751 1.00 34.63 ? 793  GLN   A CD    1 
ATOM   5814  O  OE1   . GLN   A  1  795  ? -9.608  90.435  115.918 1.00 39.03 ? 793  GLN   A OE1   1 
ATOM   5815  N  NE2   . GLN   A  1  795  ? -9.715  91.701  117.766 1.00 30.11 ? 793  GLN   A NE2   1 
ATOM   5816  N  N     . LEU   A  1  796  ? -4.631  88.265  115.981 1.00 25.45 ? 794  LEU   A N     1 
ATOM   5817  C  CA    . LEU   A  1  796  ? -3.999  87.136  116.649 1.00 27.21 ? 794  LEU   A CA    1 
ATOM   5818  C  C     . LEU   A  1  796  ? -2.481  87.151  116.540 1.00 25.51 ? 794  LEU   A C     1 
ATOM   5819  O  O     . LEU   A  1  796  ? -1.811  86.488  117.340 1.00 29.91 ? 794  LEU   A O     1 
ATOM   5820  C  CB    . LEU   A  1  796  ? -4.547  85.826  116.084 1.00 24.40 ? 794  LEU   A CB    1 
ATOM   5821  C  CG    . LEU   A  1  796  ? -5.998  85.497  116.420 1.00 23.19 ? 794  LEU   A CG    1 
ATOM   5822  C  CD1   . LEU   A  1  796  ? -6.440  84.189  115.782 1.00 24.59 ? 794  LEU   A CD1   1 
ATOM   5823  C  CD2   . LEU   A  1  796  ? -6.163  85.441  117.934 1.00 25.78 ? 794  LEU   A CD2   1 
ATOM   5824  N  N     . ALA   A  1  797  ? -1.917  87.864  115.567 1.00 27.22 ? 795  ALA   A N     1 
ATOM   5825  C  CA    . ALA   A  1  797  ? -0.466  87.878  115.441 1.00 28.45 ? 795  ALA   A CA    1 
ATOM   5826  C  C     . ALA   A  1  797  ? 0.194   88.539  116.645 1.00 32.67 ? 795  ALA   A C     1 
ATOM   5827  O  O     . ALA   A  1  797  ? 1.373   88.289  116.910 1.00 40.12 ? 795  ALA   A O     1 
ATOM   5828  C  CB    . ALA   A  1  797  ? -0.049  88.560  114.138 1.00 30.39 ? 795  ALA   A CB    1 
ATOM   5829  N  N     . ASP   A  1  798  ? -0.555  89.357  117.387 1.00 34.08 ? 796  ASP   A N     1 
ATOM   5830  C  CA    . ASP   A  1  798  ? -0.053  89.949  118.622 1.00 37.11 ? 796  ASP   A CA    1 
ATOM   5831  C  C     . ASP   A  1  798  ? 0.022   88.938  119.751 1.00 40.86 ? 796  ASP   A C     1 
ATOM   5832  O  O     . ASP   A  1  798  ? 0.701   89.193  120.751 1.00 37.45 ? 796  ASP   A O     1 
ATOM   5833  C  CB    . ASP   A  1  798  ? -1.004  91.054  119.078 1.00 31.39 ? 796  ASP   A CB    1 
ATOM   5834  C  CG    . ASP   A  1  798  ? -1.036  92.222  118.127 1.00 46.65 ? 796  ASP   A CG    1 
ATOM   5835  O  OD1   . ASP   A  1  798  ? -0.013  92.456  117.453 1.00 47.50 ? 796  ASP   A OD1   1 
ATOM   5836  O  OD2   . ASP   A  1  798  ? -2.082  92.903  118.052 1.00 51.10 ? 796  ASP   A OD2   1 
ATOM   5837  N  N     . ARG   A  1  799  ? -0.657  87.807  119.612 1.00 32.58 ? 797  ARG   A N     1 
ATOM   5838  C  CA    . ARG   A  1  799  ? -1.038  86.977  120.738 1.00 31.03 ? 797  ARG   A CA    1 
ATOM   5839  C  C     . ARG   A  1  799  ? -0.235  85.685  120.768 1.00 29.02 ? 797  ARG   A C     1 
ATOM   5840  O  O     . ARG   A  1  799  ? 0.104   85.114  119.729 1.00 27.93 ? 797  ARG   A O     1 
ATOM   5841  C  CB    . ARG   A  1  799  ? -2.516  86.626  120.612 1.00 37.92 ? 797  ARG   A CB    1 
ATOM   5842  C  CG    . ARG   A  1  799  ? -3.365  87.824  120.245 1.00 38.53 ? 797  ARG   A CG    1 
ATOM   5843  C  CD    . ARG   A  1  799  ? -3.702  88.595  121.486 1.00 41.25 ? 797  ARG   A CD    1 
ATOM   5844  N  NE    . ARG   A  1  799  ? -4.315  87.709  122.466 1.00 43.28 ? 797  ARG   A NE    1 
ATOM   5845  C  CZ    . ARG   A  1  799  ? -5.544  87.225  122.362 1.00 38.95 ? 797  ARG   A CZ    1 
ATOM   5846  N  NH1   . ARG   A  1  799  ? -6.325  87.535  121.340 1.00 44.30 ? 797  ARG   A NH1   1 
ATOM   5847  N  NH2   . ARG   A  1  799  ? -6.002  86.410  123.307 1.00 46.06 ? 797  ARG   A NH2   1 
ATOM   5848  N  N     . LEU   A  1  800  ? 0.057   85.226  121.979 1.00 27.83 ? 798  LEU   A N     1 
ATOM   5849  C  CA    . LEU   A  1  800  ? 0.570   83.886  122.197 1.00 29.25 ? 798  LEU   A CA    1 
ATOM   5850  C  C     . LEU   A  1  800  ? -0.223  83.246  123.323 1.00 26.39 ? 798  LEU   A C     1 
ATOM   5851  O  O     . LEU   A  1  800  ? -0.719  83.929  124.220 1.00 31.11 ? 798  LEU   A O     1 
ATOM   5852  C  CB    . LEU   A  1  800  ? 2.048   83.899  122.599 1.00 28.63 ? 798  LEU   A CB    1 
ATOM   5853  C  CG    . LEU   A  1  800  ? 3.050   84.354  121.542 1.00 29.61 ? 798  LEU   A CG    1 
ATOM   5854  C  CD1   . LEU   A  1  800  ? 4.433   84.495  122.157 1.00 30.98 ? 798  LEU   A CD1   1 
ATOM   5855  C  CD2   . LEU   A  1  800  ? 3.073   83.366  120.394 1.00 28.98 ? 798  LEU   A CD2   1 
ATOM   5856  N  N     . SER   A  1  801  ? -0.336  81.924  123.264 1.00 28.65 ? 799  SER   A N     1 
ATOM   5857  C  CA    . SER   A  1  801  ? -0.925  81.163  124.349 1.00 30.02 ? 799  SER   A CA    1 
ATOM   5858  C  C     . SER   A  1  801  ? -0.042  81.277  125.589 1.00 35.02 ? 799  SER   A C     1 
ATOM   5859  O  O     . SER   A  1  801  ? 1.100   81.742  125.514 1.00 33.28 ? 799  SER   A O     1 
ATOM   5860  C  CB    . SER   A  1  801  ? -1.008  79.695  123.943 1.00 32.36 ? 799  SER   A CB    1 
ATOM   5861  O  OG    . SER   A  1  801  ? 0.294   79.139  123.918 1.00 31.15 ? 799  SER   A OG    1 
ATOM   5862  N  N     . PRO   A  1  802  ? -0.547  80.859  126.755 1.00 30.14 ? 800  PRO   A N     1 
ATOM   5863  C  CA    . PRO   A  1  802  ? 0.325   80.796  127.942 1.00 33.56 ? 800  PRO   A CA    1 
ATOM   5864  C  C     . PRO   A  1  802  ? 1.564   79.940  127.744 1.00 35.45 ? 800  PRO   A C     1 
ATOM   5865  O  O     . PRO   A  1  802  ? 2.589   80.190  128.392 1.00 39.79 ? 800  PRO   A O     1 
ATOM   5866  C  CB    . PRO   A  1  802  ? -0.600  80.226  129.023 1.00 37.13 ? 800  PRO   A CB    1 
ATOM   5867  C  CG    . PRO   A  1  802  ? -1.966  80.665  128.600 1.00 36.74 ? 800  PRO   A CG    1 
ATOM   5868  C  CD    . PRO   A  1  802  ? -1.959  80.603  127.096 1.00 30.98 ? 800  PRO   A CD    1 
ATOM   5869  N  N     . ALA   A  1  803  ? 1.503   78.937  126.873 1.00 35.70 ? 801  ALA   A N     1 
ATOM   5870  C  CA    . ALA   A  1  803  ? 2.675   78.155  126.515 1.00 38.97 ? 801  ALA   A CA    1 
ATOM   5871  C  C     . ALA   A  1  803  ? 3.593   78.879  125.539 1.00 40.91 ? 801  ALA   A C     1 
ATOM   5872  O  O     . ALA   A  1  803  ? 4.617   78.313  125.145 1.00 39.35 ? 801  ALA   A O     1 
ATOM   5873  C  CB    . ALA   A  1  803  ? 2.251   76.810  125.917 1.00 41.40 ? 801  ALA   A CB    1 
ATOM   5874  N  N     . GLY   A  1  804  ? 3.249   80.097  125.132 1.00 37.79 ? 802  GLY   A N     1 
ATOM   5875  C  CA    . GLY   A  1  804  ? 4.068   80.836  124.185 1.00 30.05 ? 802  GLY   A CA    1 
ATOM   5876  C  C     . GLY   A  1  804  ? 3.978   80.378  122.743 1.00 32.28 ? 802  GLY   A C     1 
ATOM   5877  O  O     . GLY   A  1  804  ? 4.973   80.454  122.015 1.00 33.43 ? 802  GLY   A O     1 
ATOM   5878  N  N     . ARG   A  1  805  ? 2.812   79.927  122.297 1.00 31.41 ? 803  ARG   A N     1 
ATOM   5879  C  CA    . ARG   A  1  805  ? 2.637   79.444  120.937 1.00 31.92 ? 803  ARG   A CA    1 
ATOM   5880  C  C     . ARG   A  1  805  ? 1.461   80.153  120.284 1.00 24.90 ? 803  ARG   A C     1 
ATOM   5881  O  O     . ARG   A  1  805  ? 0.602   80.705  120.978 1.00 25.57 ? 803  ARG   A O     1 
ATOM   5882  C  CB    . ARG   A  1  805  ? 2.417   77.923  120.928 1.00 33.45 ? 803  ARG   A CB    1 
ATOM   5883  C  CG    . ARG   A  1  805  ? 3.593   77.141  121.518 1.00 32.29 ? 803  ARG   A CG    1 
ATOM   5884  C  CD    . ARG   A  1  805  ? 4.908   77.464  120.796 1.00 33.20 ? 803  ARG   A CD    1 
ATOM   5885  N  NE    . ARG   A  1  805  ? 6.050   76.771  121.391 1.00 29.76 ? 803  ARG   A NE    1 
ATOM   5886  C  CZ    . ARG   A  1  805  ? 6.897   77.310  122.257 1.00 35.51 ? 803  ARG   A CZ    1 
ATOM   5887  N  NH1   . ARG   A  1  805  ? 6.787   78.572  122.645 1.00 34.90 ? 803  ARG   A NH1   1 
ATOM   5888  N  NH2   . ARG   A  1  805  ? 7.882   76.564  122.752 1.00 43.41 ? 803  ARG   A NH2   1 
ATOM   5889  N  N     . PRO   A  1  806  ? 1.408   80.187  118.946 1.00 27.37 ? 804  PRO   A N     1 
ATOM   5890  C  CA    . PRO   A  1  806  ? 0.331   80.925  118.272 1.00 25.29 ? 804  PRO   A CA    1 
ATOM   5891  C  C     . PRO   A  1  806  ? -1.042  80.374  118.624 1.00 23.43 ? 804  PRO   A C     1 
ATOM   5892  O  O     . PRO   A  1  806  ? -1.218  79.171  118.835 1.00 24.29 ? 804  PRO   A O     1 
ATOM   5893  C  CB    . PRO   A  1  806  ? 0.636   80.716  116.785 1.00 25.09 ? 804  PRO   A CB    1 
ATOM   5894  C  CG    . PRO   A  1  806  ? 2.110   80.482  116.745 1.00 27.18 ? 804  PRO   A CG    1 
ATOM   5895  C  CD    . PRO   A  1  806  ? 2.407   79.690  117.985 1.00 27.13 ? 804  PRO   A CD    1 
ATOM   5896  N  N     . ILE   A  1  807  ? -2.017  81.277  118.687 1.00 21.65 ? 805  ILE   A N     1 
ATOM   5897  C  CA    . ILE   A  1  807  ? -3.415  80.909  118.897 1.00 22.19 ? 805  ILE   A CA    1 
ATOM   5898  C  C     . ILE   A  1  807  ? -3.947  80.315  117.602 1.00 20.90 ? 805  ILE   A C     1 
ATOM   5899  O  O     . ILE   A  1  807  ? -3.940  80.994  116.568 1.00 22.24 ? 805  ILE   A O     1 
ATOM   5900  C  CB    . ILE   A  1  807  ? -4.251  82.128  119.292 1.00 22.42 ? 805  ILE   A CB    1 
ATOM   5901  C  CG1   . ILE   A  1  807  ? -3.675  82.785  120.546 1.00 26.16 ? 805  ILE   A CG1   1 
ATOM   5902  C  CG2   . ILE   A  1  807  ? -5.719  81.727  119.474 1.00 24.47 ? 805  ILE   A CG2   1 
ATOM   5903  C  CD1   . ILE   A  1  807  ? -3.700  81.905  121.769 1.00 29.84 ? 805  ILE   A CD1   1 
ATOM   5904  N  N     . PRO   A  1  808  ? -4.394  79.060  117.601 1.00 20.73 ? 806  PRO   A N     1 
ATOM   5905  C  CA    . PRO   A  1  808  ? -4.875  78.453  116.357 1.00 19.41 ? 806  PRO   A CA    1 
ATOM   5906  C  C     . PRO   A  1  808  ? -6.050  79.217  115.768 1.00 19.82 ? 806  PRO   A C     1 
ATOM   5907  O  O     . PRO   A  1  808  ? -6.977  79.623  116.475 1.00 20.49 ? 806  PRO   A O     1 
ATOM   5908  C  CB    . PRO   A  1  808  ? -5.299  77.049  116.794 1.00 21.60 ? 806  PRO   A CB    1 
ATOM   5909  C  CG    . PRO   A  1  808  ? -4.507  76.778  118.011 1.00 23.61 ? 806  PRO   A CG    1 
ATOM   5910  C  CD    . PRO   A  1  808  ? -4.384  78.102  118.715 1.00 21.97 ? 806  PRO   A CD    1 
ATOM   5911  N  N     . LEU   A  1  809  ? -6.006  79.381  114.449 1.00 19.66 ? 807  LEU   A N     1 
ATOM   5912  C  CA    . LEU   A  1  809  ? -7.069  80.023  113.694 1.00 20.37 ? 807  LEU   A CA    1 
ATOM   5913  C  C     . LEU   A  1  809  ? -7.444  79.094  112.553 1.00 20.52 ? 807  LEU   A C     1 
ATOM   5914  O  O     . LEU   A  1  809  ? -6.588  78.740  111.734 1.00 20.58 ? 807  LEU   A O     1 
ATOM   5915  C  CB    . LEU   A  1  809  ? -6.590  81.357  113.116 1.00 21.23 ? 807  LEU   A CB    1 
ATOM   5916  C  CG    . LEU   A  1  809  ? -7.556  82.032  112.140 1.00 20.81 ? 807  LEU   A CG    1 
ATOM   5917  C  CD1   . LEU   A  1  809  ? -8.861  82.376  112.839 1.00 20.80 ? 807  LEU   A CD1   1 
ATOM   5918  C  CD2   . LEU   A  1  809  ? -6.920  83.273  111.539 1.00 24.29 ? 807  LEU   A CD2   1 
ATOM   5919  N  N     . ILE   A  1  810  ? -8.702  78.663  112.522 1.00 18.26 ? 808  ILE   A N     1 
ATOM   5920  C  CA    . ILE   A  1  810  ? -9.289  78.071  111.332 1.00 18.75 ? 808  ILE   A CA    1 
ATOM   5921  C  C     . ILE   A  1  810  ? -10.041 79.196  110.661 1.00 17.52 ? 808  ILE   A C     1 
ATOM   5922  O  O     . ILE   A  1  810  ? -10.941 79.781  111.268 1.00 19.75 ? 808  ILE   A O     1 
ATOM   5923  C  CB    . ILE   A  1  810  ? -10.242 76.915  111.673 1.00 17.32 ? 808  ILE   A CB    1 
ATOM   5924  C  CG1   . ILE   A  1  810  ? -9.547  75.845  112.507 1.00 19.13 ? 808  ILE   A CG1   1 
ATOM   5925  C  CG2   . ILE   A  1  810  ? -10.789 76.302  110.380 1.00 20.79 ? 808  ILE   A CG2   1 
ATOM   5926  C  CD1   . ILE   A  1  810  ? -10.389 74.586  112.710 1.00 22.46 ? 808  ILE   A CD1   1 
ATOM   5927  N  N     . ALA   A  1  811  ? -9.662  79.527  109.430 1.00 17.86 ? 809  ALA   A N     1 
ATOM   5928  C  CA    . ALA   A  1  811  ? -10.259 80.656  108.724 1.00 17.34 ? 809  ALA   A CA    1 
ATOM   5929  C  C     . ALA   A  1  811  ? -10.691 80.140  107.360 1.00 19.03 ? 809  ALA   A C     1 
ATOM   5930  O  O     . ALA   A  1  811  ? -9.858  79.948  106.470 1.00 18.29 ? 809  ALA   A O     1 
ATOM   5931  C  CB    . ALA   A  1  811  ? -9.285  81.816  108.592 1.00 20.11 ? 809  ALA   A CB    1 
ATOM   5932  N  N     . GLU   A  1  812  ? -11.989 79.915  107.210 1.00 16.34 ? 810  GLU   A N     1 
ATOM   5933  C  CA    . GLU   A  1  812  ? -12.572 79.354  106.000 1.00 16.30 ? 810  GLU   A CA    1 
ATOM   5934  C  C     . GLU   A  1  812  ? -13.274 80.492  105.287 1.00 17.79 ? 810  GLU   A C     1 
ATOM   5935  O  O     . GLU   A  1  812  ? -14.210 81.084  105.832 1.00 18.29 ? 810  GLU   A O     1 
ATOM   5936  C  CB    . GLU   A  1  812  ? -13.505 78.209  106.376 1.00 19.83 ? 810  GLU   A CB    1 
ATOM   5937  C  CG    . GLU   A  1  812  ? -12.742 77.084  107.092 1.00 19.32 ? 810  GLU   A CG    1 
ATOM   5938  C  CD    . GLU   A  1  812  ? -11.591 76.541  106.248 1.00 23.95 ? 810  GLU   A CD    1 
ATOM   5939  O  OE1   . GLU   A  1  812  ? -11.862 75.724  105.340 1.00 20.94 ? 810  GLU   A OE1   1 
ATOM   5940  O  OE2   . GLU   A  1  812  ? -10.422 76.945  106.465 1.00 21.22 ? 810  GLU   A OE2   1 
ATOM   5941  N  N     . THR   A  1  813  ? -12.786 80.830  104.096 1.00 17.58 ? 811  THR   A N     1 
ATOM   5942  C  CA    . THR   A  1  813  ? -13.090 82.126  103.514 1.00 16.92 ? 811  THR   A CA    1 
ATOM   5943  C  C     . THR   A  1  813  ? -13.694 82.026  102.114 1.00 18.72 ? 811  THR   A C     1 
ATOM   5944  O  O     . THR   A  1  813  ? -14.291 81.000  101.769 1.00 19.00 ? 811  THR   A O     1 
ATOM   5945  C  CB    . THR   A  1  813  ? -11.861 83.045  103.604 1.00 17.53 ? 811  THR   A CB    1 
ATOM   5946  O  OG1   . THR   A  1  813  ? -10.703 82.366  103.095 1.00 19.95 ? 811  THR   A OG1   1 
ATOM   5947  C  CG2   . THR   A  1  813  ? -11.580 83.390  105.059 1.00 19.01 ? 811  THR   A CG2   1 
ATOM   5948  N  N     . GLY   A  1  814  ? -13.566 83.080  101.317 1.00 18.76 ? 812  GLY   A N     1 
ATOM   5949  C  CA    . GLY   A  1  814  ? -14.321 83.190  100.084 1.00 19.60 ? 812  GLY   A CA    1 
ATOM   5950  C  C     . GLY   A  1  814  ? -13.794 82.338  98.945  1.00 19.27 ? 812  GLY   A C     1 
ATOM   5951  O  O     . GLY   A  1  814  ? -12.758 81.680  99.024  1.00 19.34 ? 812  GLY   A O     1 
ATOM   5952  N  N     . GLY   A  1  815  ? -14.548 82.362  97.847  1.00 18.90 ? 813  GLY   A N     1 
ATOM   5953  C  CA    . GLY   A  1  815  ? -14.167 81.641  96.653  1.00 19.47 ? 813  GLY   A CA    1 
ATOM   5954  C  C     . GLY   A  1  815  ? -14.350 82.509  95.425  1.00 17.90 ? 813  GLY   A C     1 
ATOM   5955  O  O     . GLY   A  1  815  ? -15.026 83.538  95.455  1.00 20.36 ? 813  GLY   A O     1 
ATOM   5956  N  N     . GLN   A  1  816  ? -13.697 82.101  94.351  1.00 17.45 ? 814  GLN   A N     1 
ATOM   5957  C  CA    . GLN   A  1  816  ? -13.940 82.658  93.022  1.00 18.09 ? 814  GLN   A CA    1 
ATOM   5958  C  C     . GLN   A  1  816  ? -14.096 81.457  92.100  1.00 16.36 ? 814  GLN   A C     1 
ATOM   5959  O  O     . GLN   A  1  816  ? -13.241 81.146  91.271  1.00 18.66 ? 814  GLN   A O     1 
ATOM   5960  C  CB    . GLN   A  1  816  ? -12.798 83.562  92.584  1.00 18.04 ? 814  GLN   A CB    1 
ATOM   5961  C  CG    . GLN   A  1  816  ? -13.098 84.345  91.325  1.00 21.38 ? 814  GLN   A CG    1 
ATOM   5962  C  CD    . GLN   A  1  816  ? -14.173 85.385  91.544  1.00 23.04 ? 814  GLN   A CD    1 
ATOM   5963  O  OE1   . GLN   A  1  816  ? -15.361 85.071  91.562  1.00 23.04 ? 814  GLN   A OE1   1 
ATOM   5964  N  NE2   . GLN   A  1  816  ? -13.759 86.636  91.732  1.00 25.60 ? 814  GLN   A NE2   1 
ATOM   5965  N  N     . ASN   A  1  817  ? -15.192 80.749  92.298  1.00 16.22 ? 815  ASN   A N     1 
ATOM   5966  C  CA    . ASN   A  1  817  ? -15.276 79.364  91.878  1.00 15.36 ? 815  ASN   A CA    1 
ATOM   5967  C  C     . ASN   A  1  817  ? -15.623 79.275  90.404  1.00 16.10 ? 815  ASN   A C     1 
ATOM   5968  O  O     . ASN   A  1  817  ? -16.552 79.940  89.932  1.00 15.90 ? 815  ASN   A O     1 
ATOM   5969  C  CB    . ASN   A  1  817  ? -16.339 78.673  92.718  1.00 14.99 ? 815  ASN   A CB    1 
ATOM   5970  C  CG    . ASN   A  1  817  ? -16.129 78.914  94.199  1.00 14.46 ? 815  ASN   A CG    1 
ATOM   5971  O  OD1   . ASN   A  1  817  ? -15.030 78.684  94.726  1.00 15.32 ? 815  ASN   A OD1   1 
ATOM   5972  N  ND2   . ASN   A  1  817  ? -17.159 79.403  94.877  1.00 15.67 ? 815  ASN   A ND2   1 
ATOM   5973  N  N     . ALA   A  1  818  ? -14.885 78.435  89.686  1.00 14.61 ? 816  ALA   A N     1 
ATOM   5974  C  CA    . ALA   A  1  818  ? -15.059 78.262  88.257  1.00 15.72 ? 816  ALA   A CA    1 
ATOM   5975  C  C     . ALA   A  1  818  ? -15.630 76.890  87.950  1.00 13.34 ? 816  ALA   A C     1 
ATOM   5976  O  O     . ALA   A  1  818  ? -15.498 75.938  88.724  1.00 14.26 ? 816  ALA   A O     1 
ATOM   5977  C  CB    . ALA   A  1  818  ? -13.712 78.387  87.547  1.00 14.79 ? 816  ALA   A CB    1 
ATOM   5978  N  N     . MET   A  1  819  ? -16.288 76.812  86.796  1.00 14.90 ? 817  MET   A N     1 
ATOM   5979  C  CA    . MET   A  1  819  ? -16.663 75.549  86.196  1.00 13.90 ? 817  MET   A CA    1 
ATOM   5980  C  C     . MET   A  1  819  ? -16.185 75.575  84.754  1.00 15.51 ? 817  MET   A C     1 
ATOM   5981  O  O     . MET   A  1  819  ? -16.432 76.547  84.036  1.00 15.88 ? 817  MET   A O     1 
ATOM   5982  C  CB    . MET   A  1  819  ? -18.170 75.324  86.241  1.00 14.89 ? 817  MET   A CB    1 
ATOM   5983  C  CG    . MET   A  1  819  ? -18.573 74.057  85.505  1.00 15.29 ? 817  MET   A CG    1 
ATOM   5984  S  SD    . MET   A  1  819  ? -20.361 73.898  85.386  1.00 17.66 ? 817  MET   A SD    1 
ATOM   5985  C  CE    . MET   A  1  819  ? -20.794 73.593  87.096  1.00 20.37 ? 817  MET   A CE    1 
ATOM   5986  N  N     . ILE   A  1  820  ? -15.485 74.527  84.342  1.00 14.63 ? 818  ILE   A N     1 
ATOM   5987  C  CA    . ILE   A  1  820  ? -15.019 74.395  82.970  1.00 14.30 ? 818  ILE   A CA    1 
ATOM   5988  C  C     . ILE   A  1  820  ? -15.906 73.388  82.263  1.00 14.19 ? 818  ILE   A C     1 
ATOM   5989  O  O     . ILE   A  1  820  ? -16.166 72.302  82.782  1.00 15.21 ? 818  ILE   A O     1 
ATOM   5990  C  CB    . ILE   A  1  820  ? -13.545 73.974  82.927  1.00 14.69 ? 818  ILE   A CB    1 
ATOM   5991  C  CG1   . ILE   A  1  820  ? -12.703 75.087  83.529  1.00 16.91 ? 818  ILE   A CG1   1 
ATOM   5992  C  CG2   . ILE   A  1  820  ? -13.128 73.694  81.479  1.00 16.38 ? 818  ILE   A CG2   1 
ATOM   5993  C  CD1   . ILE   A  1  820  ? -11.218 74.798  83.552  1.00 15.90 ? 818  ILE   A CD1   1 
ATOM   5994  N  N     . VAL   A  1  821  ? -16.384 73.755  81.082  1.00 15.88 ? 819  VAL   A N     1 
ATOM   5995  C  CA    . VAL   A  1  821  ? -17.282 72.912  80.310  1.00 16.62 ? 819  VAL   A CA    1 
ATOM   5996  C  C     . VAL   A  1  821  ? -16.666 72.749  78.935  1.00 16.81 ? 819  VAL   A C     1 
ATOM   5997  O  O     . VAL   A  1  821  ? -16.334 73.746  78.284  1.00 19.08 ? 819  VAL   A O     1 
ATOM   5998  C  CB    . VAL   A  1  821  ? -18.664 73.576  80.181  1.00 15.53 ? 819  VAL   A CB    1 
ATOM   5999  C  CG1   . VAL   A  1  821  ? -19.583 72.719  79.328  1.00 17.66 ? 819  VAL   A CG1   1 
ATOM   6000  C  CG2   . VAL   A  1  821  ? -19.247 73.837  81.563  1.00 16.69 ? 819  VAL   A CG2   1 
ATOM   6001  N  N     . ASP   A  1  822  ? -16.496 71.508  78.497  1.00 16.65 ? 820  ASP   A N     1 
ATOM   6002  C  CA    . ASP   A  1  822  ? -15.954 71.297  77.166  1.00 16.76 ? 820  ASP   A CA    1 
ATOM   6003  C  C     . ASP   A  1  822  ? -17.068 70.868  76.222  1.00 17.87 ? 820  ASP   A C     1 
ATOM   6004  O  O     . ASP   A  1  822  ? -18.236 70.777  76.599  1.00 17.98 ? 820  ASP   A O     1 
ATOM   6005  C  CB    . ASP   A  1  822  ? -14.730 70.376  77.187  1.00 18.30 ? 820  ASP   A CB    1 
ATOM   6006  C  CG    . ASP   A  1  822  ? -15.072 68.909  77.396  1.00 16.70 ? 820  ASP   A CG    1 
ATOM   6007  O  OD1   . ASP   A  1  822  ? -16.251 68.489  77.343  1.00 17.59 ? 820  ASP   A OD1   1 
ATOM   6008  O  OD2   . ASP   A  1  822  ? -14.096 68.160  77.631  1.00 18.73 ? 820  ASP   A OD2   1 
ATOM   6009  N  N     . SER   A  1  823  ? -16.696 70.613  74.966  1.00 18.06 ? 821  SER   A N     1 
ATOM   6010  C  CA    . SER   A  1  823  ? -17.694 70.299  73.951  1.00 18.94 ? 821  SER   A CA    1 
ATOM   6011  C  C     . SER   A  1  823  ? -18.277 68.898  74.077  1.00 21.72 ? 821  SER   A C     1 
ATOM   6012  O  O     . SER   A  1  823  ? -19.177 68.558  73.303  1.00 22.97 ? 821  SER   A O     1 
ATOM   6013  C  CB    . SER   A  1  823  ? -17.105 70.500  72.556  1.00 22.38 ? 821  SER   A CB    1 
ATOM   6014  O  OG    . SER   A  1  823  ? -15.941 69.716  72.394  1.00 24.91 ? 821  SER   A OG    1 
ATOM   6015  N  N     . SER   A  1  824  ? -17.805 68.073  75.013  1.00 18.31 ? 822  SER   A N     1 
ATOM   6016  C  CA    . SER   A  1  824  ? -18.374 66.753  75.213  1.00 18.00 ? 822  SER   A CA    1 
ATOM   6017  C  C     . SER   A  1  824  ? -19.506 66.751  76.230  1.00 19.96 ? 822  SER   A C     1 
ATOM   6018  O  O     . SER   A  1  824  ? -20.229 65.757  76.331  1.00 19.91 ? 822  SER   A O     1 
ATOM   6019  C  CB    . SER   A  1  824  ? -17.292 65.769  75.670  1.00 17.03 ? 822  SER   A CB    1 
ATOM   6020  O  OG    . SER   A  1  824  ? -16.883 66.039  77.008  1.00 17.37 ? 822  SER   A OG    1 
ATOM   6021  N  N     . ALA   A  1  825  ? -19.652 67.830  76.996  1.00 19.83 ? 823  ALA   A N     1 
ATOM   6022  C  CA    . ALA   A  1  825  ? -20.662 67.904  78.037  1.00 19.91 ? 823  ALA   A CA    1 
ATOM   6023  C  C     . ALA   A  1  825  ? -22.048 68.038  77.421  1.00 18.62 ? 823  ALA   A C     1 
ATOM   6024  O  O     . ALA   A  1  825  ? -22.207 68.540  76.308  1.00 21.25 ? 823  ALA   A O     1 
ATOM   6025  C  CB    . ALA   A  1  825  ? -20.381 69.122  78.916  1.00 18.60 ? 823  ALA   A CB    1 
ATOM   6026  N  N     . LEU   A  1  826  ? -23.055 67.571  78.146  1.00 20.22 ? 824  LEU   A N     1 
ATOM   6027  C  CA    . LEU   A  1  826  ? -24.435 67.669  77.689  1.00 21.48 ? 824  LEU   A CA    1 
ATOM   6028  C  C     . LEU   A  1  826  ? -25.001 69.017  78.125  1.00 22.71 ? 824  LEU   A C     1 
ATOM   6029  O  O     . LEU   A  1  826  ? -25.083 69.302  79.326  1.00 20.58 ? 824  LEU   A O     1 
ATOM   6030  C  CB    . LEU   A  1  826  ? -25.263 66.520  78.258  1.00 25.12 ? 824  LEU   A CB    1 
ATOM   6031  C  CG    . LEU   A  1  826  ? -26.704 66.440  77.743  1.00 32.90 ? 824  LEU   A CG    1 
ATOM   6032  C  CD1   . LEU   A  1  826  ? -26.724 66.224  76.230  1.00 34.68 ? 824  LEU   A CD1   1 
ATOM   6033  C  CD2   . LEU   A  1  826  ? -27.490 65.344  78.449  1.00 38.36 ? 824  LEU   A CD2   1 
ATOM   6034  N  N     . ALA   A  1  827  ? -25.389 69.844  77.152  1.00 20.51 ? 825  ALA   A N     1 
ATOM   6035  C  CA    . ALA   A  1  827  ? -25.752 71.227  77.450  1.00 19.83 ? 825  ALA   A CA    1 
ATOM   6036  C  C     . ALA   A  1  827  ? -26.846 71.319  78.509  1.00 19.58 ? 825  ALA   A C     1 
ATOM   6037  O  O     . ALA   A  1  827  ? -26.751 72.140  79.428  1.00 18.71 ? 825  ALA   A O     1 
ATOM   6038  C  CB    . ALA   A  1  827  ? -26.166 71.952  76.170  1.00 21.83 ? 825  ALA   A CB    1 
ATOM   6039  N  N     . GLU   A  1  828  ? -27.885 70.485  78.404  1.00 19.96 ? 826  GLU   A N     1 
ATOM   6040  C  CA    . GLU   A  1  828  ? -28.991 70.549  79.357  1.00 21.58 ? 826  GLU   A CA    1 
ATOM   6041  C  C     . GLU   A  1  828  ? -28.510 70.271  80.773  1.00 20.04 ? 826  GLU   A C     1 
ATOM   6042  O  O     . GLU   A  1  828  ? -28.967 70.906  81.732  1.00 19.69 ? 826  GLU   A O     1 
ATOM   6043  C  CB    . GLU   A  1  828  ? -30.082 69.545  78.973  1.00 23.12 ? 826  GLU   A CB    1 
ATOM   6044  C  CG    . GLU   A  1  828  ? -30.912 69.945  77.747  1.00 29.03 ? 826  GLU   A CG    1 
ATOM   6045  C  CD    . GLU   A  1  828  ? -30.198 69.723  76.418  1.00 35.51 ? 826  GLU   A CD    1 
ATOM   6046  O  OE1   . GLU   A  1  828  ? -29.081 69.161  76.404  1.00 31.93 ? 826  GLU   A OE1   1 
ATOM   6047  O  OE2   . GLU   A  1  828  ? -30.765 70.113  75.373  1.00 42.28 ? 826  GLU   A OE2   1 
ATOM   6048  N  N     . GLN   A  1  829  ? -27.589 69.319  80.918  1.00 20.02 ? 827  GLN   A N     1 
ATOM   6049  C  CA    . GLN   A  1  829  ? -27.047 68.992  82.229  1.00 20.32 ? 827  GLN   A CA    1 
ATOM   6050  C  C     . GLN   A  1  829  ? -26.195 70.136  82.755  1.00 18.32 ? 827  GLN   A C     1 
ATOM   6051  O  O     . GLN   A  1  829  ? -26.302 70.520  83.931  1.00 18.33 ? 827  GLN   A O     1 
ATOM   6052  C  CB    . GLN   A  1  829  ? -26.214 67.716  82.109  1.00 23.76 ? 827  GLN   A CB    1 
ATOM   6053  C  CG    . GLN   A  1  829  ? -25.750 67.153  83.420  1.00 28.71 ? 827  GLN   A CG    1 
ATOM   6054  C  CD    . GLN   A  1  829  ? -24.940 65.881  83.254  1.00 33.08 ? 827  GLN   A CD    1 
ATOM   6055  O  OE1   . GLN   A  1  829  ? -24.658 65.189  84.234  1.00 38.37 ? 827  GLN   A OE1   1 
ATOM   6056  N  NE2   . GLN   A  1  829  ? -24.550 65.571  82.017  1.00 26.39 ? 827  GLN   A NE2   1 
ATOM   6057  N  N     . VAL   A  1  830  ? -25.342 70.691  81.895  1.00 18.39 ? 828  VAL   A N     1 
ATOM   6058  C  CA    . VAL   A  1  830  ? -24.538 71.847  82.263  1.00 18.18 ? 828  VAL   A CA    1 
ATOM   6059  C  C     . VAL   A  1  830  ? -25.430 72.973  82.748  1.00 17.32 ? 828  VAL   A C     1 
ATOM   6060  O  O     . VAL   A  1  830  ? -25.204 73.554  83.816  1.00 16.34 ? 828  VAL   A O     1 
ATOM   6061  C  CB    . VAL   A  1  830  ? -23.689 72.298  81.065  1.00 16.72 ? 828  VAL   A CB    1 
ATOM   6062  C  CG1   . VAL   A  1  830  ? -23.060 73.648  81.341  1.00 18.35 ? 828  VAL   A CG1   1 
ATOM   6063  C  CG2   . VAL   A  1  830  ? -22.623 71.251  80.740  1.00 20.36 ? 828  VAL   A CG2   1 
ATOM   6064  N  N     . VAL   A  1  831  ? -26.457 73.307  81.963  1.00 16.60 ? 829  VAL   A N     1 
ATOM   6065  C  CA    . VAL   A  1  831  ? -27.266 74.471  82.295  1.00 15.64 ? 829  VAL   A CA    1 
ATOM   6066  C  C     . VAL   A  1  831  ? -27.953 74.279  83.634  1.00 16.46 ? 829  VAL   A C     1 
ATOM   6067  O  O     . VAL   A  1  831  ? -27.971 75.190  84.464  1.00 16.07 ? 829  VAL   A O     1 
ATOM   6068  C  CB    . VAL   A  1  831  ? -28.259 74.784  81.168  1.00 16.34 ? 829  VAL   A CB    1 
ATOM   6069  C  CG1   . VAL   A  1  831  ? -29.249 75.828  81.644  1.00 17.45 ? 829  VAL   A CG1   1 
ATOM   6070  C  CG2   . VAL   A  1  831  ? -27.499 75.292  79.952  1.00 18.62 ? 829  VAL   A CG2   1 
ATOM   6071  N  N     . GLY   A  1  832  ? -28.508 73.091  83.880  1.00 15.63 ? 830  GLY   A N     1 
ATOM   6072  C  CA    . GLY   A  1  832  ? -29.129 72.847  85.172  1.00 15.34 ? 830  GLY   A CA    1 
ATOM   6073  C  C     . GLY   A  1  832  ? -28.145 73.010  86.313  1.00 15.42 ? 830  GLY   A C     1 
ATOM   6074  O  O     . GLY   A  1  832  ? -28.440 73.662  87.321  1.00 16.63 ? 830  GLY   A O     1 
ATOM   6075  N  N     . ASP   A  1  833  ? -26.937 72.471  86.143  1.00 15.45 ? 831  ASP   A N     1 
ATOM   6076  C  CA    . ASP   A  1  833  ? -25.950 72.570  87.209  1.00 14.58 ? 831  ASP   A CA    1 
ATOM   6077  C  C     . ASP   A  1  833  ? -25.432 73.987  87.373  1.00 15.94 ? 831  ASP   A C     1 
ATOM   6078  O  O     . ASP   A  1  833  ? -25.074 74.386  88.484  1.00 15.52 ? 831  ASP   A O     1 
ATOM   6079  C  CB    . ASP   A  1  833  ? -24.796 71.618  86.931  1.00 16.36 ? 831  ASP   A CB    1 
ATOM   6080  C  CG    . ASP   A  1  833  ? -25.192 70.192  87.118  1.00 16.15 ? 831  ASP   A CG    1 
ATOM   6081  O  OD1   . ASP   A  1  833  ? -26.267 69.951  87.715  1.00 20.09 ? 831  ASP   A OD1   1 
ATOM   6082  O  OD2   . ASP   A  1  833  ? -24.451 69.310  86.645  1.00 17.74 ? 831  ASP   A OD2   1 
ATOM   6083  N  N     . VAL   A  1  834  ? -25.369 74.745  86.281  1.00 15.08 ? 832  VAL   A N     1 
ATOM   6084  C  CA    . VAL   A  1  834  ? -24.928 76.134  86.336  1.00 16.54 ? 832  VAL   A CA    1 
ATOM   6085  C  C     . VAL   A  1  834  ? -25.978 77.003  87.011  1.00 16.00 ? 832  VAL   A C     1 
ATOM   6086  O  O     . VAL   A  1  834  ? -25.666 77.810  87.894  1.00 16.25 ? 832  VAL   A O     1 
ATOM   6087  C  CB    . VAL   A  1  834  ? -24.615 76.635  84.918  1.00 15.83 ? 832  VAL   A CB    1 
ATOM   6088  C  CG1   . VAL   A  1  834  ? -24.463 78.142  84.893  1.00 17.09 ? 832  VAL   A CG1   1 
ATOM   6089  C  CG2   . VAL   A  1  834  ? -23.350 75.941  84.403  1.00 17.31 ? 832  VAL   A CG2   1 
ATOM   6090  N  N     . ILE   A  1  835  ? -27.240 76.863  86.590  1.00 16.43 ? 833  ILE   A N     1 
ATOM   6091  C  CA    . ILE   A  1  835  ? -28.316 77.646  87.184  1.00 16.31 ? 833  ILE   A CA    1 
ATOM   6092  C  C     . ILE   A  1  835  ? -28.378 77.397  88.684  1.00 16.13 ? 833  ILE   A C     1 
ATOM   6093  O  O     . ILE   A  1  835  ? -28.479 78.335  89.485  1.00 18.61 ? 833  ILE   A O     1 
ATOM   6094  C  CB    . ILE   A  1  835  ? -29.654 77.337  86.486  1.00 17.04 ? 833  ILE   A CB    1 
ATOM   6095  C  CG1   . ILE   A  1  835  ? -29.691 77.917  85.068  1.00 18.77 ? 833  ILE   A CG1   1 
ATOM   6096  C  CG2   . ILE   A  1  835  ? -30.831 77.859  87.323  1.00 20.20 ? 833  ILE   A CG2   1 
ATOM   6097  C  CD1   . ILE   A  1  835  ? -29.852 79.425  85.016  1.00 21.07 ? 833  ILE   A CD1   1 
ATOM   6098  N  N     . THR   A  1  836  ? -28.281 76.136  89.088  1.00 17.37 ? 834  THR   A N     1 
ATOM   6099  C  CA    . THR   A  1  836  ? -28.276 75.811  90.509  1.00 19.37 ? 834  THR   A CA    1 
ATOM   6100  C  C     . THR   A  1  836  ? -27.036 76.369  91.197  1.00 17.06 ? 834  THR   A C     1 
ATOM   6101  O  O     . THR   A  1  836  ? -27.134 77.035  92.229  1.00 18.03 ? 834  THR   A O     1 
ATOM   6102  C  CB    . THR   A  1  836  ? -28.367 74.294  90.679  1.00 21.90 ? 834  THR   A CB    1 
ATOM   6103  O  OG1   . THR   A  1  836  ? -29.626 73.846  90.167  1.00 26.25 ? 834  THR   A OG1   1 
ATOM   6104  C  CG2   . THR   A  1  836  ? -28.263 73.901  92.130  1.00 23.44 ? 834  THR   A CG2   1 
ATOM   6105  N  N     . SER   A  1  837  ? -25.858 76.135  90.624  1.00 16.72 ? 835  SER   A N     1 
ATOM   6106  C  CA    . SER   A  1  837  ? -24.626 76.518  91.313  1.00 15.67 ? 835  SER   A CA    1 
ATOM   6107  C  C     . SER   A  1  837  ? -24.481 78.026  91.410  1.00 15.91 ? 835  SER   A C     1 
ATOM   6108  O  O     . SER   A  1  837  ? -23.943 78.535  92.392  1.00 17.26 ? 835  SER   A O     1 
ATOM   6109  C  CB    . SER   A  1  837  ? -23.403 75.934  90.606  1.00 17.56 ? 835  SER   A CB    1 
ATOM   6110  O  OG    . SER   A  1  837  ? -23.430 74.523  90.642  1.00 16.99 ? 835  SER   A OG    1 
ATOM   6111  N  N     . ALA   A  1  838  ? -24.919 78.756  90.393  1.00 14.85 ? 836  ALA   A N     1 
ATOM   6112  C  CA    . ALA   A  1  838  ? -24.711 80.194  90.392  1.00 14.95 ? 836  ALA   A CA    1 
ATOM   6113  C  C     . ALA   A  1  838  ? -25.794 80.951  91.139  1.00 16.58 ? 836  ALA   A C     1 
ATOM   6114  O  O     . ALA   A  1  838  ? -25.511 81.994  91.739  1.00 17.69 ? 836  ALA   A O     1 
ATOM   6115  C  CB    . ALA   A  1  838  ? -24.658 80.720  88.955  1.00 17.51 ? 836  ALA   A CB    1 
ATOM   6116  N  N     . PHE   A  1  839  ? -27.034 80.480  91.092  1.00 16.58 ? 837  PHE   A N     1 
ATOM   6117  C  CA    . PHE   A  1  839  ? -28.143 81.314  91.518  1.00 16.57 ? 837  PHE   A CA    1 
ATOM   6118  C  C     . PHE   A  1  839  ? -28.943 80.763  92.677  1.00 18.20 ? 837  PHE   A C     1 
ATOM   6119  O  O     . PHE   A  1  839  ? -29.747 81.511  93.245  1.00 18.51 ? 837  PHE   A O     1 
ATOM   6120  C  CB    . PHE   A  1  839  ? -29.068 81.628  90.340  1.00 17.02 ? 837  PHE   A CB    1 
ATOM   6121  C  CG    . PHE   A  1  839  ? -28.351 82.227  89.184  1.00 16.39 ? 837  PHE   A CG    1 
ATOM   6122  C  CD1   . PHE   A  1  839  ? -27.629 83.398  89.331  1.00 17.35 ? 837  PHE   A CD1   1 
ATOM   6123  C  CD2   . PHE   A  1  839  ? -28.372 81.605  87.947  1.00 17.23 ? 837  PHE   A CD2   1 
ATOM   6124  C  CE1   . PHE   A  1  839  ? -26.953 83.947  88.260  1.00 18.48 ? 837  PHE   A CE1   1 
ATOM   6125  C  CE2   . PHE   A  1  839  ? -27.694 82.145  86.880  1.00 21.34 ? 837  PHE   A CE2   1 
ATOM   6126  C  CZ    . PHE   A  1  839  ? -26.986 83.320  87.035  1.00 18.70 ? 837  PHE   A CZ    1 
ATOM   6127  N  N     . ASP   A  1  840  ? -28.761 79.498  93.044  1.00 18.25 ? 838  ASP   A N     1 
ATOM   6128  C  CA    . ASP   A  1  840  ? -29.346 79.002  94.281  1.00 19.03 ? 838  ASP   A CA    1 
ATOM   6129  C  C     . ASP   A  1  840  ? -28.941 79.921  95.424  1.00 19.33 ? 838  ASP   A C     1 
ATOM   6130  O  O     . ASP   A  1  840  ? -27.799 80.389  95.493  1.00 19.02 ? 838  ASP   A O     1 
ATOM   6131  C  CB    . ASP   A  1  840  ? -28.833 77.584  94.540  1.00 21.84 ? 838  ASP   A CB    1 
ATOM   6132  C  CG    . ASP   A  1  840  ? -29.435 76.945  95.764  1.00 26.97 ? 838  ASP   A CG    1 
ATOM   6133  O  OD1   . ASP   A  1  840  ? -28.937 77.212  96.877  1.00 25.96 ? 838  ASP   A OD1   1 
ATOM   6134  O  OD2   . ASP   A  1  840  ? -30.399 76.166  95.602  1.00 32.88 ? 838  ASP   A OD2   1 
ATOM   6135  N  N     . SER   A  1  841  ? -29.896 80.225  96.297  1.00 18.94 ? 839  SER   A N     1 
ATOM   6136  C  CA    . SER   A  1  841  ? -29.642 81.123  97.423  1.00 18.21 ? 839  SER   A CA    1 
ATOM   6137  C  C     . SER   A  1  841  ? -29.161 82.493  96.958  1.00 17.46 ? 839  SER   A C     1 
ATOM   6138  O  O     . SER   A  1  841  ? -28.418 83.175  97.667  1.00 17.60 ? 839  SER   A O     1 
ATOM   6139  C  CB    . SER   A  1  841  ? -28.664 80.505  98.432  1.00 21.64 ? 839  SER   A CB    1 
ATOM   6140  O  OG    . SER   A  1  841  ? -29.087 79.206  98.810  1.00 26.68 ? 839  SER   A OG    1 
ATOM   6141  N  N     . ALA   A  1  842  ? -29.582 82.897  95.758  1.00 18.49 ? 840  ALA   A N     1 
ATOM   6142  C  CA    . ALA   A  1  842  ? -29.136 84.143  95.144  1.00 16.03 ? 840  ALA   A CA    1 
ATOM   6143  C  C     . ALA   A  1  842  ? -27.611 84.238  95.116  1.00 16.11 ? 840  ALA   A C     1 
ATOM   6144  O  O     . ALA   A  1  842  ? -27.032 85.303  95.315  1.00 19.50 ? 840  ALA   A O     1 
ATOM   6145  C  CB    . ALA   A  1  842  ? -29.775 85.371  95.798  1.00 18.47 ? 840  ALA   A CB    1 
ATOM   6146  N  N     . GLY   A  1  843  ? -26.957 83.106  94.846  1.00 16.81 ? 841  GLY   A N     1 
ATOM   6147  C  CA    . GLY   A  1  843  ? -25.505 83.090  94.786  1.00 16.95 ? 841  GLY   A CA    1 
ATOM   6148  C  C     . GLY   A  1  843  ? -24.819 83.309  96.112  1.00 16.96 ? 841  GLY   A C     1 
ATOM   6149  O  O     . GLY   A  1  843  ? -23.602 83.499  96.141  1.00 16.97 ? 841  GLY   A O     1 
ATOM   6150  N  N     . GLN   A  1  844  ? -25.557 83.274  97.213  1.00 16.86 ? 842  GLN   A N     1 
ATOM   6151  C  CA    . GLN   A  1  844  ? -24.979 83.530  98.524  1.00 16.55 ? 842  GLN   A CA    1 
ATOM   6152  C  C     . GLN   A  1  844  ? -24.586 82.231  99.213  1.00 18.26 ? 842  GLN   A C     1 
ATOM   6153  O  O     . GLN   A  1  844  ? -24.967 81.916  100.339 1.00 19.36 ? 842  GLN   A O     1 
ATOM   6154  C  CB    . GLN   A  1  844  ? -25.939 84.371  99.352  1.00 18.45 ? 842  GLN   A CB    1 
ATOM   6155  C  CG    . GLN   A  1  844  ? -26.169 85.733  98.720  1.00 18.01 ? 842  GLN   A CG    1 
ATOM   6156  C  CD    . GLN   A  1  844  ? -27.381 86.436  99.279  1.00 17.25 ? 842  GLN   A CD    1 
ATOM   6157  O  OE1   . GLN   A  1  844  ? -27.283 87.540  99.802  1.00 18.73 ? 842  GLN   A OE1   1 
ATOM   6158  N  NE2   . GLN   A  1  844  ? -28.541 85.800  99.158  1.00 19.58 ? 842  GLN   A NE2   1 
ATOM   6159  N  N     . ARG   A  1  845  ? -23.823 81.444  98.465  1.00 18.38 ? 843  ARG   A N     1 
ATOM   6160  C  CA    . ARG   A  1  845  ? -23.100 80.299  98.978  1.00 19.16 ? 843  ARG   A CA    1 
ATOM   6161  C  C     . ARG   A  1  845  ? -21.640 80.559  98.681  1.00 17.56 ? 843  ARG   A C     1 
ATOM   6162  O  O     . ARG   A  1  845  ? -21.302 81.071  97.612  1.00 18.02 ? 843  ARG   A O     1 
ATOM   6163  C  CB    . ARG   A  1  845  ? -23.508 79.016  98.264  1.00 19.34 ? 843  ARG   A CB    1 
ATOM   6164  C  CG    . ARG   A  1  845  ? -24.948 78.584  98.475  1.00 18.98 ? 843  ARG   A CG    1 
ATOM   6165  C  CD    . ARG   A  1  845  ? -25.222 77.318  97.689  1.00 23.14 ? 843  ARG   A CD    1 
ATOM   6166  N  NE    . ARG   A  1  845  ? -26.559 76.796  97.930  1.00 27.20 ? 843  ARG   A NE    1 
ATOM   6167  C  CZ    . ARG   A  1  845  ? -26.843 75.889  98.854  1.00 30.93 ? 843  ARG   A CZ    1 
ATOM   6168  N  NH1   . ARG   A  1  845  ? -25.902 75.383  99.638  1.00 31.43 ? 843  ARG   A NH1   1 
ATOM   6169  N  NH2   . ARG   A  1  845  ? -28.100 75.477  98.993  1.00 33.80 ? 843  ARG   A NH2   1 
ATOM   6170  N  N     . CYS   A  1  846  ? -20.774 80.224  99.629  1.00 17.82 ? 844  CYS   A N     1 
ATOM   6171  C  CA    . CYS   A  1  846  ? -19.355 80.410  99.373  1.00 17.07 ? 844  CYS   A CA    1 
ATOM   6172  C  C     . CYS   A  1  846  ? -18.893 79.545  98.212  1.00 16.82 ? 844  CYS   A C     1 
ATOM   6173  O  O     . CYS   A  1  846  ? -17.926 79.884  97.524  1.00 15.38 ? 844  CYS   A O     1 
ATOM   6174  C  CB    . CYS   A  1  846  ? -18.565 80.077  100.631 1.00 17.49 ? 844  CYS   A CB    1 
ATOM   6175  S  SG    . CYS   A  1  846  ? -18.929 78.444  101.334 1.00 21.08 ? 844  CYS   A SG    1 
ATOM   6176  N  N     . SER   A  1  847  ? -19.573 78.432  97.994  1.00 15.23 ? 845  SER   A N     1 
ATOM   6177  C  CA    . SER   A  1  847  ? -19.288 77.483  96.928  1.00 14.19 ? 845  SER   A CA    1 
ATOM   6178  C  C     . SER   A  1  847  ? -19.890 77.880  95.590  1.00 15.56 ? 845  SER   A C     1 
ATOM   6179  O  O     . SER   A  1  847  ? -19.686 77.153  94.604  1.00 15.53 ? 845  SER   A O     1 
ATOM   6180  C  CB    . SER   A  1  847  ? -19.885 76.145  97.326  1.00 14.30 ? 845  SER   A CB    1 
ATOM   6181  O  OG    . SER   A  1  847  ? -21.251 76.357  97.653  1.00 17.98 ? 845  SER   A OG    1 
ATOM   6182  N  N     . ALA   A  1  848  ? -20.643 78.982  95.530  1.00 15.29 ? 846  ALA   A N     1 
ATOM   6183  C  CA    . ALA   A  1  848  ? -21.425 79.289  94.336  1.00 14.83 ? 846  ALA   A CA    1 
ATOM   6184  C  C     . ALA   A  1  848  ? -20.524 79.454  93.120  1.00 15.77 ? 846  ALA   A C     1 
ATOM   6185  O  O     . ALA   A  1  848  ? -19.384 79.913  93.206  1.00 15.72 ? 846  ALA   A O     1 
ATOM   6186  C  CB    . ALA   A  1  848  ? -22.232 80.571  94.552  1.00 16.33 ? 846  ALA   A CB    1 
ATOM   6187  N  N     . LEU   A  1  849  ? -21.053 79.069  91.969  1.00 15.47 ? 847  LEU   A N     1 
ATOM   6188  C  CA    . LEU   A  1  849  ? -20.324 79.230  90.723  1.00 15.49 ? 847  LEU   A CA    1 
ATOM   6189  C  C     . LEU   A  1  849  ? -20.258 80.703  90.358  1.00 16.20 ? 847  LEU   A C     1 
ATOM   6190  O  O     . LEU   A  1  849  ? -21.293 81.363  90.220  1.00 16.23 ? 847  LEU   A O     1 
ATOM   6191  C  CB    . LEU   A  1  849  ? -21.058 78.466  89.635  1.00 16.34 ? 847  LEU   A CB    1 
ATOM   6192  C  CG    . LEU   A  1  849  ? -20.486 78.654  88.234  1.00 15.32 ? 847  LEU   A CG    1 
ATOM   6193  C  CD1   . LEU   A  1  849  ? -19.049 78.166  88.191  1.00 15.72 ? 847  LEU   A CD1   1 
ATOM   6194  C  CD2   . LEU   A  1  849  ? -21.342 77.898  87.227  1.00 16.71 ? 847  LEU   A CD2   1 
ATOM   6195  N  N     . ARG   A  1  850  ? -19.043 81.218  90.199  1.00 15.63 ? 848  ARG   A N     1 
ATOM   6196  C  CA    . ARG   A  1  850  ? -18.828 82.607  89.833  1.00 17.51 ? 848  ARG   A CA    1 
ATOM   6197  C  C     . ARG   A  1  850  ? -18.384 82.780  88.394  1.00 17.41 ? 848  ARG   A C     1 
ATOM   6198  O  O     . ARG   A  1  850  ? -18.665 83.817  87.797  1.00 17.55 ? 848  ARG   A O     1 
ATOM   6199  C  CB    . ARG   A  1  850  ? -17.760 83.240  90.736  1.00 18.17 ? 848  ARG   A CB    1 
ATOM   6200  C  CG    . ARG   A  1  850  ? -18.018 83.045  92.213  1.00 17.80 ? 848  ARG   A CG    1 
ATOM   6201  C  CD    . ARG   A  1  850  ? -19.406 83.523  92.589  1.00 18.55 ? 848  ARG   A CD    1 
ATOM   6202  N  NE    . ARG   A  1  850  ? -19.581 83.490  94.032  1.00 17.56 ? 848  ARG   A NE    1 
ATOM   6203  C  CZ    . ARG   A  1  850  ? -20.725 83.746  94.645  1.00 17.56 ? 848  ARG   A CZ    1 
ATOM   6204  N  NH1   . ARG   A  1  850  ? -21.820 84.055  93.963  1.00 16.83 ? 848  ARG   A NH1   1 
ATOM   6205  N  NH2   . ARG   A  1  850  ? -20.770 83.694  95.972  1.00 18.72 ? 848  ARG   A NH2   1 
ATOM   6206  N  N     . VAL   A  1  851  ? -17.651 81.816  87.845  1.00 16.99 ? 849  VAL   A N     1 
ATOM   6207  C  CA    . VAL   A  1  851  ? -17.057 81.944  86.519  1.00 18.06 ? 849  VAL   A CA    1 
ATOM   6208  C  C     . VAL   A  1  851  ? -17.308 80.648  85.772  1.00 16.74 ? 849  VAL   A C     1 
ATOM   6209  O  O     . VAL   A  1  851  ? -16.714 79.612  86.103  1.00 17.51 ? 849  VAL   A O     1 
ATOM   6210  C  CB    . VAL   A  1  851  ? -15.552 82.236  86.566  1.00 21.08 ? 849  VAL   A CB    1 
ATOM   6211  C  CG1   . VAL   A  1  851  ? -15.042 82.501  85.150  1.00 23.87 ? 849  VAL   A CG1   1 
ATOM   6212  C  CG2   . VAL   A  1  851  ? -15.235 83.400  87.490  1.00 24.84 ? 849  VAL   A CG2   1 
ATOM   6213  N  N     . LEU   A  1  852  ? -18.166 80.706  84.757  1.00 15.86 ? 850  LEU   A N     1 
ATOM   6214  C  CA    . LEU   A  1  852  ? -18.407 79.575  83.877  1.00 15.32 ? 850  LEU   A CA    1 
ATOM   6215  C  C     . LEU   A  1  852  ? -17.508 79.726  82.659  1.00 15.35 ? 850  LEU   A C     1 
ATOM   6216  O  O     . LEU   A  1  852  ? -17.485 80.785  82.024  1.00 16.51 ? 850  LEU   A O     1 
ATOM   6217  C  CB    . LEU   A  1  852  ? -19.865 79.585  83.433  1.00 15.95 ? 850  LEU   A CB    1 
ATOM   6218  C  CG    . LEU   A  1  852  ? -20.258 78.533  82.404  1.00 15.43 ? 850  LEU   A CG    1 
ATOM   6219  C  CD1   . LEU   A  1  852  ? -20.123 77.135  82.988  1.00 15.44 ? 850  LEU   A CD1   1 
ATOM   6220  C  CD2   . LEU   A  1  852  ? -21.701 78.801  81.950  1.00 16.76 ? 850  LEU   A CD2   1 
ATOM   6221  N  N     . CYS   A  1  853  ? -16.747 78.679  82.352  1.00 16.56 ? 851  CYS   A N     1 
ATOM   6222  C  CA    . CYS   A  1  853  ? -15.785 78.717  81.255  1.00 16.52 ? 851  CYS   A CA    1 
ATOM   6223  C  C     . CYS   A  1  853  ? -16.246 77.726  80.206  1.00 14.67 ? 851  CYS   A C     1 
ATOM   6224  O  O     . CYS   A  1  853  ? -16.281 76.521  80.458  1.00 15.93 ? 851  CYS   A O     1 
ATOM   6225  C  CB    . CYS   A  1  853  ? -14.389 78.356  81.739  1.00 16.58 ? 851  CYS   A CB    1 
ATOM   6226  S  SG    . CYS   A  1  853  ? -13.858 79.263  83.183  1.00 19.14 ? 851  CYS   A SG    1 
ATOM   6227  N  N     . LEU   A  1  854  ? -16.600 78.231  79.034  1.00 15.73 ? 852  LEU   A N     1 
ATOM   6228  C  CA    . LEU   A  1  854  ? -17.230 77.437  77.991  1.00 15.79 ? 852  LEU   A CA    1 
ATOM   6229  C  C     . LEU   A  1  854  ? -16.275 77.293  76.823  1.00 16.60 ? 852  LEU   A C     1 
ATOM   6230  O  O     . LEU   A  1  854  ? -15.755 78.291  76.311  1.00 18.15 ? 852  LEU   A O     1 
ATOM   6231  C  CB    . LEU   A  1  854  ? -18.498 78.123  77.495  1.00 16.58 ? 852  LEU   A CB    1 
ATOM   6232  C  CG    . LEU   A  1  854  ? -19.592 78.303  78.546  1.00 18.06 ? 852  LEU   A CG    1 
ATOM   6233  C  CD1   . LEU   A  1  854  ? -20.774 79.068  77.954  1.00 16.86 ? 852  LEU   A CD1   1 
ATOM   6234  C  CD2   . LEU   A  1  854  ? -20.021 76.945  79.080  1.00 19.22 ? 852  LEU   A CD2   1 
ATOM   6235  N  N     . GLN   A  1  855  ? -16.074 76.057  76.385  1.00 16.49 ? 853  GLN   A N     1 
ATOM   6236  C  CA    . GLN   A  1  855  ? -15.270 75.853  75.195  1.00 17.34 ? 853  GLN   A CA    1 
ATOM   6237  C  C     . GLN   A  1  855  ? -15.939 76.542  74.014  1.00 17.27 ? 853  GLN   A C     1 
ATOM   6238  O  O     . GLN   A  1  855  ? -17.163 76.493  73.852  1.00 18.42 ? 853  GLN   A O     1 
ATOM   6239  C  CB    . GLN   A  1  855  ? -15.096 74.369  74.918  1.00 16.50 ? 853  GLN   A CB    1 
ATOM   6240  C  CG    . GLN   A  1  855  ? -14.036 74.131  73.860  1.00 18.99 ? 853  GLN   A CG    1 
ATOM   6241  C  CD    . GLN   A  1  855  ? -13.930 72.688  73.460  1.00 20.57 ? 853  GLN   A CD    1 
ATOM   6242  O  OE1   . GLN   A  1  855  ? -13.965 71.792  74.301  1.00 21.93 ? 853  GLN   A OE1   1 
ATOM   6243  N  NE2   . GLN   A  1  855  ? -13.784 72.449  72.157  1.00 25.01 ? 853  GLN   A NE2   1 
ATOM   6244  N  N     . GLU   A  1  856  ? -15.116 77.207  73.203  1.00 19.31 ? 854  GLU   A N     1 
ATOM   6245  C  CA    . GLU   A  1  856  ? -15.627 78.150  72.214  1.00 21.08 ? 854  GLU   A CA    1 
ATOM   6246  C  C     . GLU   A  1  856  ? -16.665 77.514  71.302  1.00 22.45 ? 854  GLU   A C     1 
ATOM   6247  O  O     . GLU   A  1  856  ? -17.687 78.134  70.996  1.00 23.61 ? 854  GLU   A O     1 
ATOM   6248  C  CB    . GLU   A  1  856  ? -14.463 78.717  71.401  1.00 22.08 ? 854  GLU   A CB    1 
ATOM   6249  C  CG    . GLU   A  1  856  ? -14.891 79.625  70.262  1.00 25.47 ? 854  GLU   A CG    1 
ATOM   6250  C  CD    . GLU   A  1  856  ? -15.632 80.862  70.730  1.00 34.33 ? 854  GLU   A CD    1 
ATOM   6251  O  OE1   . GLU   A  1  856  ? -15.299 81.386  71.815  1.00 28.63 ? 854  GLU   A OE1   1 
ATOM   6252  O  OE2   . GLU   A  1  856  ? -16.547 81.313  70.008  1.00 34.90 ? 854  GLU   A OE2   1 
ATOM   6253  N  N     . ASP   A  1  857  ? -16.444 76.260  70.891  1.00 20.01 ? 855  ASP   A N     1 
ATOM   6254  C  CA    . ASP   A  1  857  ? -17.307 75.624  69.899  1.00 23.73 ? 855  ASP   A CA    1 
ATOM   6255  C  C     . ASP   A  1  857  ? -18.726 75.393  70.404  1.00 24.12 ? 855  ASP   A C     1 
ATOM   6256  O  O     . ASP   A  1  857  ? -19.648 75.255  69.592  1.00 26.72 ? 855  ASP   A O     1 
ATOM   6257  C  CB    . ASP   A  1  857  ? -16.700 74.297  69.443  1.00 29.55 ? 855  ASP   A CB    1 
ATOM   6258  N  N     . VAL   A  1  858  ? -18.928 75.338  71.718  1.00 19.86 ? 856  VAL   A N     1 
ATOM   6259  C  CA    . VAL   A  1  858  ? -20.251 75.122  72.287  1.00 20.69 ? 856  VAL   A CA    1 
ATOM   6260  C  C     . VAL   A  1  858  ? -20.747 76.317  73.070  1.00 17.72 ? 856  VAL   A C     1 
ATOM   6261  O  O     . VAL   A  1  858  ? -21.867 76.267  73.607  1.00 18.32 ? 856  VAL   A O     1 
ATOM   6262  C  CB    . VAL   A  1  858  ? -20.305 73.843  73.142  1.00 21.04 ? 856  VAL   A CB    1 
ATOM   6263  C  CG1   . VAL   A  1  858  ? -20.037 72.630  72.267  1.00 22.97 ? 856  VAL   A CG1   1 
ATOM   6264  C  CG2   . VAL   A  1  858  ? -19.289 73.933  74.295  1.00 20.01 ? 856  VAL   A CG2   1 
ATOM   6265  N  N     . ALA   A  1  859  ? -19.963 77.395  73.143  1.00 19.30 ? 857  ALA   A N     1 
ATOM   6266  C  CA    . ALA   A  1  859  ? -20.286 78.484  74.059  1.00 18.26 ? 857  ALA   A CA    1 
ATOM   6267  C  C     . ALA   A  1  859  ? -21.599 79.160  73.689  1.00 20.38 ? 857  ALA   A C     1 
ATOM   6268  O  O     . ALA   A  1  859  ? -22.421 79.442  74.567  1.00 18.80 ? 857  ALA   A O     1 
ATOM   6269  C  CB    . ALA   A  1  859  ? -19.151 79.503  74.103  1.00 18.88 ? 857  ALA   A CB    1 
ATOM   6270  N  N     . ASP   A  1  860  ? -21.825 79.410  72.397  1.00 20.65 ? 858  ASP   A N     1 
ATOM   6271  C  CA    . ASP   A  1  860  ? -23.037 80.115  71.992  1.00 22.28 ? 858  ASP   A CA    1 
ATOM   6272  C  C     . ASP   A  1  860  ? -24.281 79.303  72.315  1.00 20.44 ? 858  ASP   A C     1 
ATOM   6273  O  O     . ASP   A  1  860  ? -25.267 79.837  72.836  1.00 22.04 ? 858  ASP   A O     1 
ATOM   6274  C  CB    . ASP   A  1  860  ? -22.992 80.443  70.501  1.00 23.44 ? 858  ASP   A CB    1 
ATOM   6275  C  CG    . ASP   A  1  860  ? -22.032 81.569  70.182  1.00 29.33 ? 858  ASP   A CG    1 
ATOM   6276  O  OD1   . ASP   A  1  860  ? -21.795 82.427  71.060  1.00 32.33 ? 858  ASP   A OD1   1 
ATOM   6277  O  OD2   . ASP   A  1  860  ? -21.521 81.599  69.042  1.00 43.78 ? 858  ASP   A OD2   1 
ATOM   6278  N  N     . ARG   A  1  861  ? -24.263 78.006  72.003  1.00 20.01 ? 859  ARG   A N     1 
ATOM   6279  C  CA    . ARG   A  1  861  ? -25.425 77.174  72.273  1.00 20.68 ? 859  ARG   A CA    1 
ATOM   6280  C  C     . ARG   A  1  861  ? -25.708 77.101  73.769  1.00 19.18 ? 859  ARG   A C     1 
ATOM   6281  O  O     . ARG   A  1  861  ? -26.857 77.237  74.204  1.00 18.79 ? 859  ARG   A O     1 
ATOM   6282  C  CB    . ARG   A  1  861  ? -25.230 75.776  71.682  1.00 27.19 ? 859  ARG   A CB    1 
ATOM   6283  N  N     . ILE   A  1  862  ? -24.670 76.881  74.575  1.00 18.50 ? 860  ILE   A N     1 
ATOM   6284  C  CA    . ILE   A  1  862  ? -24.888 76.781  76.013  1.00 18.55 ? 860  ILE   A CA    1 
ATOM   6285  C  C     . ILE   A  1  862  ? -25.346 78.113  76.579  1.00 17.74 ? 860  ILE   A C     1 
ATOM   6286  O  O     . ILE   A  1  862  ? -26.265 78.167  77.403  1.00 16.54 ? 860  ILE   A O     1 
ATOM   6287  C  CB    . ILE   A  1  862  ? -23.629 76.255  76.722  1.00 18.54 ? 860  ILE   A CB    1 
ATOM   6288  C  CG1   . ILE   A  1  862  ? -23.413 74.792  76.343  1.00 19.77 ? 860  ILE   A CG1   1 
ATOM   6289  C  CG2   . ILE   A  1  862  ? -23.777 76.427  78.232  1.00 18.07 ? 860  ILE   A CG2   1 
ATOM   6290  C  CD1   . ILE   A  1  862  ? -22.047 74.252  76.764  1.00 21.69 ? 860  ILE   A CD1   1 
ATOM   6291  N  N     . LEU   A  1  863  ? -24.728 79.205  76.139  1.00 17.73 ? 861  LEU   A N     1 
ATOM   6292  C  CA    A LEU   A  1  863  ? -25.113 80.524  76.632  0.43 17.98 ? 861  LEU   A CA    1 
ATOM   6293  C  CA    B LEU   A  1  863  ? -25.113 80.519  76.636  0.57 17.97 ? 861  LEU   A CA    1 
ATOM   6294  C  C     . LEU   A  1  863  ? -26.566 80.833  76.305  1.00 17.62 ? 861  LEU   A C     1 
ATOM   6295  O  O     . LEU   A  1  863  ? -27.296 81.373  77.142  1.00 17.21 ? 861  LEU   A O     1 
ATOM   6296  C  CB    A LEU   A  1  863  ? -24.193 81.599  76.052  0.43 19.72 ? 861  LEU   A CB    1 
ATOM   6297  C  CB    B LEU   A  1  863  ? -24.179 81.573  76.051  0.57 19.72 ? 861  LEU   A CB    1 
ATOM   6298  C  CG    A LEU   A  1  863  ? -23.014 82.042  76.915  0.43 22.49 ? 861  LEU   A CG    1 
ATOM   6299  C  CG    B LEU   A  1  863  ? -24.267 82.964  76.654  0.57 20.26 ? 861  LEU   A CG    1 
ATOM   6300  C  CD1   A LEU   A  1  863  ? -22.107 82.964  76.127  0.43 19.95 ? 861  LEU   A CD1   1 
ATOM   6301  C  CD1   B LEU   A  1  863  ? -24.213 82.883  78.173  0.57 18.46 ? 861  LEU   A CD1   1 
ATOM   6302  C  CD2   A LEU   A  1  863  ? -23.518 82.736  78.168  0.43 21.71 ? 861  LEU   A CD2   1 
ATOM   6303  C  CD2   B LEU   A  1  863  ? -23.128 83.790  76.106  0.57 22.70 ? 861  LEU   A CD2   1 
ATOM   6304  N  N     . THR   A  1  864  ? -27.002 80.508  75.086  1.00 18.13 ? 862  THR   A N     1 
ATOM   6305  C  CA    . THR   A  1  864  ? -28.402 80.717  74.738  1.00 17.97 ? 862  THR   A CA    1 
ATOM   6306  C  C     . THR   A  1  864  ? -29.308 79.921  75.664  1.00 16.44 ? 862  THR   A C     1 
ATOM   6307  O  O     . THR   A  1  864  ? -30.296 80.445  76.191  1.00 16.30 ? 862  THR   A O     1 
ATOM   6308  C  CB    . THR   A  1  864  ? -28.638 80.314  73.285  1.00 18.90 ? 862  THR   A CB    1 
ATOM   6309  O  OG1   . THR   A  1  864  ? -27.888 81.185  72.440  1.00 21.61 ? 862  THR   A OG1   1 
ATOM   6310  C  CG2   . THR   A  1  864  ? -30.122 80.420  72.934  1.00 19.85 ? 862  THR   A CG2   1 
ATOM   6311  N  N     . MET   A  1  865  ? -28.974 78.649  75.891  1.00 16.15 ? 863  MET   A N     1 
ATOM   6312  C  CA    . MET   A  1  865  ? -29.782 77.832  76.785  1.00 16.62 ? 863  MET   A CA    1 
ATOM   6313  C  C     . MET   A  1  865  ? -29.728 78.366  78.206  1.00 14.90 ? 863  MET   A C     1 
ATOM   6314  O  O     . MET   A  1  865  ? -30.739 78.384  78.911  1.00 14.76 ? 863  MET   A O     1 
ATOM   6315  C  CB    . MET   A  1  865  ? -29.281 76.395  76.752  1.00 17.97 ? 863  MET   A CB    1 
ATOM   6316  C  CG    . MET   A  1  865  ? -30.178 75.412  77.470  1.00 21.51 ? 863  MET   A CG    1 
ATOM   6317  S  SD    . MET   A  1  865  ? -29.477 73.763  77.314  1.00 23.63 ? 863  MET   A SD    1 
ATOM   6318  C  CE    . MET   A  1  865  ? -29.036 73.913  75.568  1.00 19.26 ? 863  MET   A CE    1 
ATOM   6319  N  N     . LEU   A  1  866  ? -28.555 78.822  78.636  1.00 15.20 ? 864  LEU   A N     1 
ATOM   6320  C  CA    . LEU   A  1  866  ? -28.423 79.347  79.988  1.00 15.94 ? 864  LEU   A CA    1 
ATOM   6321  C  C     . LEU   A  1  866  ? -29.296 80.581  80.184  1.00 14.72 ? 864  LEU   A C     1 
ATOM   6322  O  O     . LEU   A  1  866  ? -29.972 80.722  81.207  1.00 15.84 ? 864  LEU   A O     1 
ATOM   6323  C  CB    . LEU   A  1  866  ? -26.956 79.680  80.239  1.00 16.14 ? 864  LEU   A CB    1 
ATOM   6324  C  CG    . LEU   A  1  866  ? -26.655 80.236  81.623  1.00 20.16 ? 864  LEU   A CG    1 
ATOM   6325  C  CD1   . LEU   A  1  866  ? -27.123 79.269  82.693  1.00 20.45 ? 864  LEU   A CD1   1 
ATOM   6326  C  CD2   . LEU   A  1  866  ? -25.170 80.525  81.758  1.00 22.47 ? 864  LEU   A CD2   1 
ATOM   6327  N  N     . LYS   A  1  867  ? -29.267 81.505  79.223  1.00 16.14 ? 865  LYS   A N     1 
ATOM   6328  C  CA    . LYS   A  1  867  ? -30.090 82.704  79.330  1.00 17.61 ? 865  LYS   A CA    1 
ATOM   6329  C  C     . LYS   A  1  867  ? -31.568 82.351  79.335  1.00 16.29 ? 865  LYS   A C     1 
ATOM   6330  O  O     . LYS   A  1  867  ? -32.352 82.944  80.083  1.00 16.49 ? 865  LYS   A O     1 
ATOM   6331  C  CB    . LYS   A  1  867  ? -29.763 83.672  78.195  1.00 18.54 ? 865  LYS   A CB    1 
ATOM   6332  C  CG    . LYS   A  1  867  ? -28.362 84.262  78.311  1.00 19.42 ? 865  LYS   A CG    1 
ATOM   6333  C  CD    . LYS   A  1  867  ? -28.019 85.130  77.117  1.00 20.08 ? 865  LYS   A CD    1 
ATOM   6334  C  CE    . LYS   A  1  867  ? -26.602 85.662  77.245  1.00 24.68 ? 865  LYS   A CE    1 
ATOM   6335  N  NZ    . LYS   A  1  867  ? -26.123 86.305  75.990  1.00 29.80 ? 865  LYS   A NZ    1 
ATOM   6336  N  N     . GLY   A  1  868  ? -31.970 81.380  78.512  1.00 16.44 ? 866  GLY   A N     1 
ATOM   6337  C  CA    . GLY   A  1  868  ? -33.357 80.951  78.528  1.00 16.84 ? 866  GLY   A CA    1 
ATOM   6338  C  C     . GLY   A  1  868  ? -33.750 80.373  79.871  1.00 15.82 ? 866  GLY   A C     1 
ATOM   6339  O  O     . GLY   A  1  868  ? -34.838 80.644  80.383  1.00 16.57 ? 866  GLY   A O     1 
ATOM   6340  N  N     . ALA   A  1  869  ? -32.857 79.593  80.473  1.00 15.32 ? 867  ALA   A N     1 
ATOM   6341  C  CA    . ALA   A  1  869  ? -33.146 79.003  81.772  1.00 15.01 ? 867  ALA   A CA    1 
ATOM   6342  C  C     . ALA   A  1  869  ? -33.191 80.072  82.855  1.00 16.09 ? 867  ALA   A C     1 
ATOM   6343  O  O     . ALA   A  1  869  ? -34.001 79.989  83.786  1.00 15.94 ? 867  ALA   A O     1 
ATOM   6344  C  CB    . ALA   A  1  869  ? -32.080 77.969  82.120  1.00 15.73 ? 867  ALA   A CB    1 
ATOM   6345  N  N     . LEU   A  1  870  ? -32.311 81.068  82.752  1.00 16.01 ? 868  LEU   A N     1 
ATOM   6346  C  CA    . LEU   A  1  870  ? -32.292 82.158  83.720  1.00 16.54 ? 868  LEU   A CA    1 
ATOM   6347  C  C     . LEU   A  1  870  ? -33.660 82.807  83.820  1.00 18.14 ? 868  LEU   A C     1 
ATOM   6348  O  O     . LEU   A  1  870  ? -34.142 83.103  84.916  1.00 17.89 ? 868  LEU   A O     1 
ATOM   6349  C  CB    . LEU   A  1  870  ? -31.254 83.195  83.282  1.00 17.22 ? 868  LEU   A CB    1 
ATOM   6350  C  CG    . LEU   A  1  870  ? -31.008 84.405  84.183  1.00 19.92 ? 868  LEU   A CG    1 
ATOM   6351  C  CD1   . LEU   A  1  870  ? -30.018 84.027  85.264  1.00 22.26 ? 868  LEU   A CD1   1 
ATOM   6352  C  CD2   . LEU   A  1  870  ? -30.500 85.602  83.391  1.00 23.51 ? 868  LEU   A CD2   1 
ATOM   6353  N  N     . HIS   A  1  871  ? -34.311 83.015  82.681  1.00 16.68 ? 869  HIS   A N     1 
ATOM   6354  C  CA    . HIS   A  1  871  ? -35.571 83.738  82.674  1.00 18.98 ? 869  HIS   A CA    1 
ATOM   6355  C  C     . HIS   A  1  871  ? -36.741 82.917  83.183  1.00 18.06 ? 869  HIS   A C     1 
ATOM   6356  O  O     . HIS   A  1  871  ? -37.843 83.458  83.325  1.00 20.42 ? 869  HIS   A O     1 
ATOM   6357  C  CB    . HIS   A  1  871  ? -35.843 84.312  81.290  1.00 19.69 ? 869  HIS   A CB    1 
ATOM   6358  C  CG    . HIS   A  1  871  ? -34.938 85.450  80.959  1.00 21.77 ? 869  HIS   A CG    1 
ATOM   6359  N  ND1   . HIS   A  1  871  ? -35.060 86.689  81.553  1.00 25.30 ? 869  HIS   A ND1   1 
ATOM   6360  C  CD2   . HIS   A  1  871  ? -33.852 85.522  80.157  1.00 20.19 ? 869  HIS   A CD2   1 
ATOM   6361  C  CE1   . HIS   A  1  871  ? -34.107 87.484  81.103  1.00 25.59 ? 869  HIS   A CE1   1 
ATOM   6362  N  NE2   . HIS   A  1  871  ? -33.358 86.800  80.257  1.00 23.80 ? 869  HIS   A NE2   1 
ATOM   6363  N  N     . GLU   A  1  872  ? -36.532 81.647  83.475  1.00 15.56 ? 870  GLU   A N     1 
ATOM   6364  C  CA    . GLU   A  1  872  ? -37.577 80.836  84.078  1.00 18.42 ? 870  GLU   A CA    1 
ATOM   6365  C  C     . GLU   A  1  872  ? -37.515 80.826  85.597  1.00 19.04 ? 870  GLU   A C     1 
ATOM   6366  O  O     . GLU   A  1  872  ? -38.325 80.140  86.230  1.00 17.69 ? 870  GLU   A O     1 
ATOM   6367  C  CB    . GLU   A  1  872  ? -37.490 79.403  83.559  1.00 18.04 ? 870  GLU   A CB    1 
ATOM   6368  C  CG    . GLU   A  1  872  ? -37.670 79.299  82.057  1.00 20.08 ? 870  GLU   A CG    1 
ATOM   6369  C  CD    . GLU   A  1  872  ? -39.045 79.728  81.606  1.00 19.64 ? 870  GLU   A CD    1 
ATOM   6370  O  OE1   . GLU   A  1  872  ? -39.988 79.665  82.423  1.00 21.40 ? 870  GLU   A OE1   1 
ATOM   6371  O  OE2   . GLU   A  1  872  ? -39.187 80.125  80.424  1.00 20.95 ? 870  GLU   A OE2   1 
ATOM   6372  N  N     . LEU   A  1  873  ? -36.589 81.566  86.198  1.00 17.03 ? 871  LEU   A N     1 
ATOM   6373  C  CA    . LEU   A  1  873  ? -36.481 81.590  87.647  1.00 17.03 ? 871  LEU   A CA    1 
ATOM   6374  C  C     . LEU   A  1  873  ? -37.466 82.585  88.240  1.00 18.10 ? 871  LEU   A C     1 
ATOM   6375  O  O     . LEU   A  1  873  ? -37.673 83.677  87.703  1.00 20.54 ? 871  LEU   A O     1 
ATOM   6376  C  CB    . LEU   A  1  873  ? -35.067 81.982  88.065  1.00 17.62 ? 871  LEU   A CB    1 
ATOM   6377  C  CG    . LEU   A  1  873  ? -33.988 81.032  87.575  1.00 18.50 ? 871  LEU   A CG    1 
ATOM   6378  C  CD1   . LEU   A  1  873  ? -32.610 81.594  87.929  1.00 19.89 ? 871  LEU   A CD1   1 
ATOM   6379  C  CD2   . LEU   A  1  873  ? -34.174 79.665  88.210  1.00 20.52 ? 871  LEU   A CD2   1 
ATOM   6380  N  N     . HIS   A  1  874  ? -38.061 82.197  89.363  1.00 18.15 ? 872  HIS   A N     1 
ATOM   6381  C  CA    . HIS   A  1  874  ? -38.978 83.041  90.111  1.00 17.42 ? 872  HIS   A CA    1 
ATOM   6382  C  C     . HIS   A  1  874  ? -38.224 83.604  91.310  1.00 17.01 ? 872  HIS   A C     1 
ATOM   6383  O  O     . HIS   A  1  874  ? -37.748 82.846  92.165  1.00 18.24 ? 872  HIS   A O     1 
ATOM   6384  C  CB    . HIS   A  1  874  ? -40.174 82.203  90.562  1.00 19.01 ? 872  HIS   A CB    1 
ATOM   6385  C  CG    . HIS   A  1  874  ? -41.218 82.958  91.329  1.00 22.38 ? 872  HIS   A CG    1 
ATOM   6386  N  ND1   . HIS   A  1  874  ? -41.202 84.327  91.490  1.00 33.02 ? 872  HIS   A ND1   1 
ATOM   6387  C  CD2   . HIS   A  1  874  ? -42.331 82.518  91.964  1.00 28.22 ? 872  HIS   A CD2   1 
ATOM   6388  C  CE1   . HIS   A  1  874  ? -42.251 84.697  92.207  1.00 24.28 ? 872  HIS   A CE1   1 
ATOM   6389  N  NE2   . HIS   A  1  874  ? -42.947 83.617  92.512  1.00 29.78 ? 872  HIS   A NE2   1 
ATOM   6390  N  N     . ILE   A  1  875  ? -38.114 84.927  91.358  1.00 17.32 ? 873  ILE   A N     1 
ATOM   6391  C  CA    . ILE   A  1  875  ? -37.423 85.644  92.422  1.00 19.28 ? 873  ILE   A CA    1 
ATOM   6392  C  C     . ILE   A  1  875  ? -38.474 86.307  93.298  1.00 23.38 ? 873  ILE   A C     1 
ATOM   6393  O  O     . ILE   A  1  875  ? -39.359 87.015  92.798  1.00 21.43 ? 873  ILE   A O     1 
ATOM   6394  C  CB    . ILE   A  1  875  ? -36.445 86.692  91.858  1.00 20.83 ? 873  ILE   A CB    1 
ATOM   6395  C  CG1   . ILE   A  1  875  ? -35.180 86.049  91.289  1.00 25.15 ? 873  ILE   A CG1   1 
ATOM   6396  C  CG2   . ILE   A  1  875  ? -35.988 87.634  92.956  1.00 21.57 ? 873  ILE   A CG2   1 
ATOM   6397  C  CD1   . ILE   A  1  875  ? -35.361 85.084  90.135  1.00 24.86 ? 873  ILE   A CD1   1 
ATOM   6398  N  N     . GLY   A  1  876  ? -38.380 86.090  94.602  1.00 19.83 ? 874  GLY   A N     1 
ATOM   6399  C  CA    . GLY   A  1  876  ? -39.326 86.738  95.486  1.00 20.01 ? 874  GLY   A CA    1 
ATOM   6400  C  C     . GLY   A  1  876  ? -39.119 86.326  96.924  1.00 19.23 ? 874  GLY   A C     1 
ATOM   6401  O  O     . GLY   A  1  876  ? -38.160 85.629  97.270  1.00 19.59 ? 874  GLY   A O     1 
ATOM   6402  N  N     . ARG   A  1  877  ? -40.039 86.790  97.767  1.00 19.65 ? 875  ARG   A N     1 
ATOM   6403  C  CA    . ARG   A  1  877  ? -40.029 86.397  99.165  1.00 19.75 ? 875  ARG   A CA    1 
ATOM   6404  C  C     . ARG   A  1  877  ? -40.185 84.886  99.254  1.00 19.81 ? 875  ARG   A C     1 
ATOM   6405  O  O     . ARG   A  1  877  ? -41.016 84.290  98.562  1.00 20.66 ? 875  ARG   A O     1 
ATOM   6406  C  CB    . ARG   A  1  877  ? -41.173 87.097  99.896  1.00 24.45 ? 875  ARG   A CB    1 
ATOM   6407  C  CG    . ARG   A  1  877  ? -40.969 87.193  101.387 1.00 24.10 ? 875  ARG   A CG    1 
ATOM   6408  C  CD    . ARG   A  1  877  ? -42.087 87.990  102.017 1.00 27.08 ? 875  ARG   A CD    1 
ATOM   6409  N  NE    . ARG   A  1  877  ? -43.259 87.171  102.274 1.00 25.41 ? 875  ARG   A NE    1 
ATOM   6410  C  CZ    . ARG   A  1  877  ? -44.327 87.604  102.927 1.00 32.52 ? 875  ARG   A CZ    1 
ATOM   6411  N  NH1   . ARG   A  1  877  ? -44.406 88.851  103.364 1.00 33.44 ? 875  ARG   A NH1   1 
ATOM   6412  N  NH2   . ARG   A  1  877  ? -45.333 86.764  103.157 1.00 30.90 ? 875  ARG   A NH2   1 
ATOM   6413  N  N     . THR   A  1  878  ? -39.378 84.263  100.103 1.00 20.58 ? 876  THR   A N     1 
ATOM   6414  C  CA    . THR   A  1  878  ? -39.126 82.836  99.988  1.00 19.11 ? 876  THR   A CA    1 
ATOM   6415  C  C     . THR   A  1  878  ? -40.122 81.974  100.738 1.00 19.70 ? 876  THR   A C     1 
ATOM   6416  O  O     . THR   A  1  878  ? -39.942 80.753  100.784 1.00 20.04 ? 876  THR   A O     1 
ATOM   6417  C  CB    . THR   A  1  878  ? -37.712 82.513  100.457 1.00 18.26 ? 876  THR   A CB    1 
ATOM   6418  O  OG1   . THR   A  1  878  ? -37.496 83.128  101.728 1.00 23.53 ? 876  THR   A OG1   1 
ATOM   6419  C  CG2   . THR   A  1  878  ? -36.708 83.030  99.468  1.00 24.02 ? 876  THR   A CG2   1 
ATOM   6420  N  N     . ASP   A  1  879  ? -41.163 82.564  101.310 1.00 18.87 ? 877  ASP   A N     1 
ATOM   6421  C  CA    . ASP   A  1  879  ? -42.203 81.779  101.957 1.00 22.05 ? 877  ASP   A CA    1 
ATOM   6422  C  C     . ASP   A  1  879  ? -43.240 81.241  100.970 1.00 20.57 ? 877  ASP   A C     1 
ATOM   6423  O  O     . ASP   A  1  879  ? -44.384 80.976  101.361 1.00 20.18 ? 877  ASP   A O     1 
ATOM   6424  C  CB    . ASP   A  1  879  ? -42.858 82.576  103.086 1.00 20.48 ? 877  ASP   A CB    1 
ATOM   6425  C  CG    . ASP   A  1  879  ? -43.607 83.796  102.581 1.00 28.17 ? 877  ASP   A CG    1 
ATOM   6426  O  OD1   . ASP   A  1  879  ? -43.182 84.400  101.571 1.00 28.83 ? 877  ASP   A OD1   1 
ATOM   6427  O  OD2   . ASP   A  1  879  ? -44.631 84.148  103.195 1.00 26.53 ? 877  ASP   A OD2   1 
ATOM   6428  N  N     . ARG   A  1  880  ? -42.845 81.060  99.712  1.00 20.51 ? 878  ARG   A N     1 
ATOM   6429  C  CA    . ARG   A  1  880  ? -43.662 80.409  98.699  1.00 19.68 ? 878  ARG   A CA    1 
ATOM   6430  C  C     . ARG   A  1  880  ? -42.800 79.353  98.031  1.00 19.33 ? 878  ARG   A C     1 
ATOM   6431  O  O     . ARG   A  1  880  ? -41.672 79.642  97.623  1.00 18.89 ? 878  ARG   A O     1 
ATOM   6432  C  CB    . ARG   A  1  880  ? -44.125 81.400  97.631  1.00 24.60 ? 878  ARG   A CB    1 
ATOM   6433  C  CG    . ARG   A  1  880  ? -45.176 82.398  98.093  1.00 26.39 ? 878  ARG   A CG    1 
ATOM   6434  C  CD    . ARG   A  1  880  ? -45.576 83.291  96.919  1.00 34.17 ? 878  ARG   A CD    1 
ATOM   6435  N  NE    . ARG   A  1  880  ? -46.512 84.337  97.311  1.00 49.87 ? 878  ARG   A NE    1 
ATOM   6436  C  CZ    . ARG   A  1  880  ? -47.770 84.401  96.900  1.00 51.72 ? 878  ARG   A CZ    1 
ATOM   6437  N  NH1   . ARG   A  1  880  ? -48.273 83.498  96.072  1.00 56.69 ? 878  ARG   A NH1   1 
ATOM   6438  N  NH2   . ARG   A  1  880  ? -48.541 85.400  97.323  1.00 53.30 ? 878  ARG   A NH2   1 
ATOM   6439  N  N     . LEU   A  1  881  ? -43.338 78.137  97.914  1.00 18.31 ? 879  LEU   A N     1 
ATOM   6440  C  CA    . LEU   A  1  881  ? -42.601 77.044  97.284  1.00 17.43 ? 879  LEU   A CA    1 
ATOM   6441  C  C     . LEU   A  1  881  ? -42.180 77.386  95.860  1.00 17.56 ? 879  LEU   A C     1 
ATOM   6442  O  O     . LEU   A  1  881  ? -41.144 76.900  95.383  1.00 17.85 ? 879  LEU   A O     1 
ATOM   6443  C  CB    . LEU   A  1  881  ? -43.461 75.781  97.291  1.00 18.56 ? 879  LEU   A CB    1 
ATOM   6444  C  CG    . LEU   A  1  881  ? -42.854 74.499  96.742  1.00 19.27 ? 879  LEU   A CG    1 
ATOM   6445  C  CD1   . LEU   A  1  881  ? -41.662 74.086  97.601  1.00 22.09 ? 879  LEU   A CD1   1 
ATOM   6446  C  CD2   . LEU   A  1  881  ? -43.913 73.413  96.713  1.00 22.45 ? 879  LEU   A CD2   1 
ATOM   6447  N  N     . SER   A  1  882  ? -42.954 78.224  95.173  1.00 17.70 ? 880  SER   A N     1 
ATOM   6448  C  CA    . SER   A  1  882  ? -42.651 78.536  93.788  1.00 18.52 ? 880  SER   A CA    1 
ATOM   6449  C  C     . SER   A  1  882  ? -41.466 79.470  93.640  1.00 19.14 ? 880  SER   A C     1 
ATOM   6450  O  O     . SER   A  1  882  ? -41.034 79.712  92.509  1.00 19.86 ? 880  SER   A O     1 
ATOM   6451  C  CB    . SER   A  1  882  ? -43.873 79.171  93.133  1.00 19.08 ? 880  SER   A CB    1 
ATOM   6452  O  OG    . SER   A  1  882  ? -44.198 80.370  93.804  1.00 23.18 ? 880  SER   A OG    1 
ATOM   6453  N  N     . VAL   A  1  883  ? -40.923 79.997  94.733  1.00 19.40 ? 881  VAL   A N     1 
ATOM   6454  C  CA    . VAL   A  1  883  ? -39.798 80.918  94.628  1.00 19.51 ? 881  VAL   A CA    1 
ATOM   6455  C  C     . VAL   A  1  883  ? -38.498 80.138  94.512  1.00 18.98 ? 881  VAL   A C     1 
ATOM   6456  O  O     . VAL   A  1  883  ? -38.196 79.268  95.336  1.00 21.91 ? 881  VAL   A O     1 
ATOM   6457  C  CB    . VAL   A  1  883  ? -39.768 81.897  95.808  1.00 21.25 ? 881  VAL   A CB    1 
ATOM   6458  C  CG1   . VAL   A  1  883  ? -38.439 82.650  95.823  1.00 19.30 ? 881  VAL   A CG1   1 
ATOM   6459  C  CG2   . VAL   A  1  883  ? -40.906 82.869  95.674  1.00 19.79 ? 881  VAL   A CG2   1 
ATOM   6460  N  N     . ASP   A  1  884  ? -37.721 80.459  93.486  1.00 16.20 ? 882  ASP   A N     1 
ATOM   6461  C  CA    . ASP   A  1  884  ? -36.446 79.799  93.249  1.00 17.82 ? 882  ASP   A CA    1 
ATOM   6462  C  C     . ASP   A  1  884  ? -35.294 80.550  93.885  1.00 20.34 ? 882  ASP   A C     1 
ATOM   6463  O  O     . ASP   A  1  884  ? -34.350 79.935  94.388  1.00 23.61 ? 882  ASP   A O     1 
ATOM   6464  C  CB    . ASP   A  1  884  ? -36.200 79.727  91.748  1.00 19.75 ? 882  ASP   A CB    1 
ATOM   6465  C  CG    . ASP   A  1  884  ? -37.280 78.969  91.043  1.00 17.37 ? 882  ASP   A CG    1 
ATOM   6466  O  OD1   . ASP   A  1  884  ? -37.484 77.799  91.415  1.00 20.58 ? 882  ASP   A OD1   1 
ATOM   6467  O  OD2   . ASP   A  1  884  ? -37.907 79.554  90.148  1.00 18.87 ? 882  ASP   A OD2   1 
ATOM   6468  N  N     . VAL   A  1  885  ? -35.351 81.872  93.844  1.00 18.52 ? 883  VAL   A N     1 
ATOM   6469  C  CA    . VAL   A  1  885  ? -34.239 82.714  94.241  1.00 19.52 ? 883  VAL   A CA    1 
ATOM   6470  C  C     . VAL   A  1  885  ? -34.787 83.760  95.189  1.00 18.28 ? 883  VAL   A C     1 
ATOM   6471  O  O     . VAL   A  1  885  ? -35.709 84.500  94.834  1.00 18.16 ? 883  VAL   A O     1 
ATOM   6472  C  CB    . VAL   A  1  885  ? -33.578 83.376  93.027  1.00 20.30 ? 883  VAL   A CB    1 
ATOM   6473  C  CG1   . VAL   A  1  885  ? -32.478 84.318  93.478  1.00 21.68 ? 883  VAL   A CG1   1 
ATOM   6474  C  CG2   . VAL   A  1  885  ? -33.022 82.305  92.083  1.00 21.19 ? 883  VAL   A CG2   1 
ATOM   6475  N  N     . GLY   A  1  886  ? -34.241 83.806  96.394  1.00 18.72 ? 884  GLY   A N     1 
ATOM   6476  C  CA    . GLY   A  1  886  ? -34.667 84.772  97.368  1.00 17.65 ? 884  GLY   A CA    1 
ATOM   6477  C  C     . GLY   A  1  886  ? -33.861 86.046  97.310  1.00 17.42 ? 884  GLY   A C     1 
ATOM   6478  O  O     . GLY   A  1  886  ? -33.153 86.337  96.336  1.00 18.00 ? 884  GLY   A O     1 
ATOM   6479  N  N     . PRO   A  1  887  ? -33.955 86.831  98.375  1.00 17.58 ? 885  PRO   A N     1 
ATOM   6480  C  CA    . PRO   A  1  887  ? -33.312 88.144  98.397  1.00 17.99 ? 885  PRO   A CA    1 
ATOM   6481  C  C     . PRO   A  1  887  ? -31.839 88.008  98.739  1.00 18.39 ? 885  PRO   A C     1 
ATOM   6482  O  O     . PRO   A  1  887  ? -31.357 86.960  99.177  1.00 18.52 ? 885  PRO   A O     1 
ATOM   6483  C  CB    . PRO   A  1  887  ? -34.043 88.848  99.543  1.00 18.14 ? 885  PRO   A CB    1 
ATOM   6484  C  CG    . PRO   A  1  887  ? -34.381 87.727  100.495 1.00 20.64 ? 885  PRO   A CG    1 
ATOM   6485  C  CD    . PRO   A  1  887  ? -34.742 86.572  99.596  1.00 19.42 ? 885  PRO   A CD    1 
ATOM   6486  N  N     . VAL   A  1  888  ? -31.125 89.099  98.523  1.00 19.28 ? 886  VAL   A N     1 
ATOM   6487  C  CA    . VAL   A  1  888  ? -29.832 89.246  99.161  1.00 18.53 ? 886  VAL   A CA    1 
ATOM   6488  C  C     . VAL   A  1  888  ? -30.028 89.765  100.585 1.00 19.41 ? 886  VAL   A C     1 
ATOM   6489  O  O     . VAL   A  1  888  ? -31.056 90.356  100.933 1.00 20.29 ? 886  VAL   A O     1 
ATOM   6490  C  CB    . VAL   A  1  888  ? -28.863 90.112  98.333  1.00 20.60 ? 886  VAL   A CB    1 
ATOM   6491  C  CG1   . VAL   A  1  888  ? -28.670 89.481  96.939  1.00 21.32 ? 886  VAL   A CG1   1 
ATOM   6492  C  CG2   . VAL   A  1  888  ? -29.361 91.533  98.207  1.00 23.34 ? 886  VAL   A CG2   1 
ATOM   6493  N  N     . ILE   A  1  889  ? -29.033 89.513  101.435 1.00 20.05 ? 887  ILE   A N     1 
ATOM   6494  C  CA    . ILE   A  1  889  ? -29.285 89.583  102.874 1.00 21.01 ? 887  ILE   A CA    1 
ATOM   6495  C  C     . ILE   A  1  889  ? -29.553 91.006  103.351 1.00 22.11 ? 887  ILE   A C     1 
ATOM   6496  O  O     . ILE   A  1  889  ? -30.340 91.213  104.285 1.00 21.21 ? 887  ILE   A O     1 
ATOM   6497  C  CB    . ILE   A  1  889  ? -28.158 88.893  103.668 1.00 20.68 ? 887  ILE   A CB    1 
ATOM   6498  C  CG1   . ILE   A  1  889  ? -28.518 88.798  105.161 1.00 21.05 ? 887  ILE   A CG1   1 
ATOM   6499  C  CG2   . ILE   A  1  889  ? -26.816 89.608  103.452 1.00 20.61 ? 887  ILE   A CG2   1 
ATOM   6500  C  CD1   . ILE   A  1  889  ? -29.787 88.001  105.449 1.00 22.30 ? 887  ILE   A CD1   1 
ATOM   6501  N  N     . THR   A  1  890  ? -28.911 92.006  102.750 1.00 20.59 ? 888  THR   A N     1 
ATOM   6502  C  CA    . THR   A  1  890  ? -29.065 93.379  103.216 1.00 21.06 ? 888  THR   A CA    1 
ATOM   6503  C  C     . THR   A  1  890  ? -29.014 94.331  102.036 1.00 20.60 ? 888  THR   A C     1 
ATOM   6504  O  O     . THR   A  1  890  ? -28.558 93.982  100.943 1.00 21.90 ? 888  THR   A O     1 
ATOM   6505  C  CB    . THR   A  1  890  ? -27.928 93.807  104.157 1.00 23.13 ? 888  THR   A CB    1 
ATOM   6506  O  OG1   . THR   A  1  890  ? -26.674 93.700  103.467 1.00 24.16 ? 888  THR   A OG1   1 
ATOM   6507  C  CG2   . THR   A  1  890  ? -27.896 92.973  105.434 1.00 25.76 ? 888  THR   A CG2   1 
ATOM   6508  N  N     . SER   A  1  891  ? -29.450 95.568  102.292 1.00 23.86 ? 889  SER   A N     1 
ATOM   6509  C  CA    A SER   A  1  891  ? -29.314 96.625  101.294 0.37 25.75 ? 889  SER   A CA    1 
ATOM   6510  C  CA    B SER   A  1  891  ? -29.314 96.603  101.276 0.63 25.71 ? 889  SER   A CA    1 
ATOM   6511  C  C     . SER   A  1  891  ? -27.851 96.864  100.955 1.00 26.02 ? 889  SER   A C     1 
ATOM   6512  O  O     . SER   A  1  891  ? -27.514 97.165  99.806  1.00 26.82 ? 889  SER   A O     1 
ATOM   6513  C  CB    A SER   A  1  891  ? -29.940 97.920  101.813 0.37 28.48 ? 889  SER   A CB    1 
ATOM   6514  C  CB    B SER   A  1  891  ? -29.991 97.890  101.742 0.63 28.50 ? 889  SER   A CB    1 
ATOM   6515  O  OG    A SER   A  1  891  ? -31.318 97.758  102.084 0.37 30.08 ? 889  SER   A OG    1 
ATOM   6516  O  OG    B SER   A  1  891  ? -29.454 98.304  102.980 0.63 31.42 ? 889  SER   A OG    1 
ATOM   6517  N  N     . GLU   A  1  892  ? -26.971 96.743  101.950 1.00 24.22 ? 890  GLU   A N     1 
ATOM   6518  C  CA    . GLU   A  1  892  ? -25.549 96.945  101.712 1.00 25.95 ? 890  GLU   A CA    1 
ATOM   6519  C  C     . GLU   A  1  892  ? -25.000 95.874  100.783 1.00 28.47 ? 890  GLU   A C     1 
ATOM   6520  O  O     . GLU   A  1  892  ? -24.221 96.172  99.871  1.00 27.64 ? 890  GLU   A O     1 
ATOM   6521  C  CB    . GLU   A  1  892  ? -24.791 96.954  103.041 1.00 27.89 ? 890  GLU   A CB    1 
ATOM   6522  C  CG    . GLU   A  1  892  ? -25.080 98.166  103.939 1.00 33.91 ? 890  GLU   A CG    1 
ATOM   6523  C  CD    . GLU   A  1  892  ? -26.451 98.128  104.611 1.00 43.48 ? 890  GLU   A CD    1 
ATOM   6524  O  OE1   . GLU   A  1  892  ? -26.988 97.023  104.844 1.00 31.91 ? 890  GLU   A OE1   1 
ATOM   6525  O  OE2   . GLU   A  1  892  ? -26.990 99.215  104.913 1.00 46.51 ? 890  GLU   A OE2   1 
ATOM   6526  N  N     . ALA   A  1  893  ? -25.388 94.619  101.009 1.00 25.20 ? 891  ALA   A N     1 
ATOM   6527  C  CA    . ALA   A  1  893  ? -24.998 93.562  100.084 1.00 24.00 ? 891  ALA   A CA    1 
ATOM   6528  C  C     . ALA   A  1  893  ? -25.554 93.833  98.696  1.00 25.38 ? 891  ALA   A C     1 
ATOM   6529  O  O     . ALA   A  1  893  ? -24.836 93.709  97.698  1.00 25.84 ? 891  ALA   A O     1 
ATOM   6530  C  CB    . ALA   A  1  893  ? -25.447 92.200  100.614 1.00 23.22 ? 891  ALA   A CB    1 
ATOM   6531  N  N     . LYS   A  1  894  ? -26.824 94.241  98.622  1.00 22.53 ? 892  LYS   A N     1 
ATOM   6532  C  CA    . LYS   A  1  894  ? -27.432 94.591  97.343  1.00 23.76 ? 892  LYS   A CA    1 
ATOM   6533  C  C     . LYS   A  1  894  ? -26.648 95.688  96.637  1.00 26.69 ? 892  LYS   A C     1 
ATOM   6534  O  O     . LYS   A  1  894  ? -26.350 95.580  95.444  1.00 25.92 ? 892  LYS   A O     1 
ATOM   6535  C  CB    . LYS   A  1  894  ? -28.881 95.026  97.559  1.00 21.98 ? 892  LYS   A CB    1 
ATOM   6536  C  CG    . LYS   A  1  894  ? -29.580 95.516  96.310  1.00 24.52 ? 892  LYS   A CG    1 
ATOM   6537  C  CD    . LYS   A  1  894  ? -31.042 95.841  96.589  1.00 25.77 ? 892  LYS   A CD    1 
ATOM   6538  C  CE    . LYS   A  1  894  ? -31.737 96.395  95.345  1.00 28.49 ? 892  LYS   A CE    1 
ATOM   6539  N  NZ    . LYS   A  1  894  ? -33.100 96.901  95.647  1.00 41.99 ? 892  LYS   A NZ    1 
ATOM   6540  N  N     . ASP   A  1  895  ? -26.311 96.761  97.359  1.00 24.52 ? 893  ASP   A N     1 
ATOM   6541  C  CA    . ASP   A  1  895  ? -25.587 97.868  96.741  1.00 29.81 ? 893  ASP   A CA    1 
ATOM   6542  C  C     . ASP   A  1  895  ? -24.219 97.424  96.246  1.00 26.09 ? 893  ASP   A C     1 
ATOM   6543  O  O     . ASP   A  1  895  ? -23.770 97.844  95.172  1.00 29.53 ? 893  ASP   A O     1 
ATOM   6544  C  CB    . ASP   A  1  895  ? -25.435 99.021  97.735  1.00 28.46 ? 893  ASP   A CB    1 
ATOM   6545  C  CG    . ASP   A  1  895  ? -26.763 99.652  98.114  1.00 33.47 ? 893  ASP   A CG    1 
ATOM   6546  O  OD1   . ASP   A  1  895  ? -27.745 99.507  97.351  1.00 41.01 ? 893  ASP   A OD1   1 
ATOM   6547  O  OD2   . ASP   A  1  895  ? -26.818 100.307 99.179  1.00 37.83 ? 893  ASP   A OD2   1 
ATOM   6548  N  N     . ASN   A  1  896  ? -23.534 96.585  97.023  1.00 25.17 ? 894  ASN   A N     1 
ATOM   6549  C  CA    . ASN   A  1  896  ? -22.216 96.114  96.615  1.00 24.73 ? 894  ASN   A CA    1 
ATOM   6550  C  C     . ASN   A  1  896  ? -22.302 95.270  95.351  1.00 27.94 ? 894  ASN   A C     1 
ATOM   6551  O  O     . ASN   A  1  896  ? -21.477 95.414  94.439  1.00 26.42 ? 894  ASN   A O     1 
ATOM   6552  C  CB    . ASN   A  1  896  ? -21.578 95.302  97.739  1.00 26.58 ? 894  ASN   A CB    1 
ATOM   6553  C  CG    . ASN   A  1  896  ? -20.260 94.678  97.326  1.00 38.24 ? 894  ASN   A CG    1 
ATOM   6554  O  OD1   . ASN   A  1  896  ? -20.204 93.510  96.928  1.00 42.67 ? 894  ASN   A OD1   1 
ATOM   6555  N  ND2   . ASN   A  1  896  ? -19.190 95.459  97.408  1.00 38.03 ? 894  ASN   A ND2   1 
ATOM   6556  N  N     . ILE   A  1  897  ? -23.286 94.372  95.288  1.00 24.97 ? 895  ILE   A N     1 
ATOM   6557  C  CA    . ILE   A  1  897  ? -23.438 93.533  94.108  1.00 24.88 ? 895  ILE   A CA    1 
ATOM   6558  C  C     . ILE   A  1  897  ? -23.799 94.385  92.902  1.00 25.50 ? 895  ILE   A C     1 
ATOM   6559  O  O     . ILE   A  1  897  ? -23.228 94.228  91.818  1.00 24.73 ? 895  ILE   A O     1 
ATOM   6560  C  CB    . ILE   A  1  897  ? -24.494 92.447  94.370  1.00 21.30 ? 895  ILE   A CB    1 
ATOM   6561  C  CG1   . ILE   A  1  897  ? -24.076 91.557  95.542  1.00 23.96 ? 895  ILE   A CG1   1 
ATOM   6562  C  CG2   . ILE   A  1  897  ? -24.724 91.622  93.115  1.00 24.56 ? 895  ILE   A CG2   1 
ATOM   6563  C  CD1   . ILE   A  1  897  ? -25.253 90.802  96.169  1.00 21.11 ? 895  ILE   A CD1   1 
ATOM   6564  N  N     . GLU   A  1  898  ? -24.748 95.306  93.073  1.00 23.83 ? 896  GLU   A N     1 
ATOM   6565  C  CA    . GLU   A  1  898  ? -25.183 96.123  91.947  1.00 25.16 ? 896  GLU   A CA    1 
ATOM   6566  C  C     . GLU   A  1  898  ? -24.069 97.026  91.437  1.00 27.37 ? 896  GLU   A C     1 
ATOM   6567  O  O     . GLU   A  1  898  ? -23.981 97.274  90.229  1.00 27.34 ? 896  GLU   A O     1 
ATOM   6568  C  CB    . GLU   A  1  898  ? -26.443 96.910  92.312  1.00 26.54 ? 896  GLU   A CB    1 
ATOM   6569  C  CG    . GLU   A  1  898  ? -27.658 96.008  92.472  1.00 28.19 ? 896  GLU   A CG    1 
ATOM   6570  C  CD    . GLU   A  1  898  ? -28.929 96.768  92.801  1.00 33.45 ? 896  GLU   A CD    1 
ATOM   6571  O  OE1   . GLU   A  1  898  ? -28.837 97.856  93.405  1.00 39.35 ? 896  GLU   A OE1   1 
ATOM   6572  O  OE2   . GLU   A  1  898  ? -30.019 96.267  92.455  1.00 46.39 ? 896  GLU   A OE2   1 
ATOM   6573  N  N     . LYS   A  1  899  ? -23.214 97.523  92.331  1.00 25.17 ? 897  LYS   A N     1 
ATOM   6574  C  CA    . LYS   A  1  899  ? -22.078 98.323  91.893  1.00 27.00 ? 897  LYS   A CA    1 
ATOM   6575  C  C     . LYS   A  1  899  ? -21.184 97.516  90.967  1.00 28.38 ? 897  LYS   A C     1 
ATOM   6576  O  O     . LYS   A  1  899  ? -20.690 98.032  89.957  1.00 28.54 ? 897  LYS   A O     1 
ATOM   6577  C  CB    . LYS   A  1  899  ? -21.278 98.799  93.106  1.00 29.63 ? 897  LYS   A CB    1 
ATOM   6578  N  N     . HIS   A  1  900  ? -20.974 96.242  91.295  1.00 24.76 ? 898  HIS   A N     1 
ATOM   6579  C  CA    . HIS   A  1  900  ? -20.169 95.384  90.436  1.00 26.96 ? 898  HIS   A CA    1 
ATOM   6580  C  C     . HIS   A  1  900  ? -20.833 95.197  89.081  1.00 24.44 ? 898  HIS   A C     1 
ATOM   6581  O  O     . HIS   A  1  900  ? -20.180 95.306  88.038  1.00 27.82 ? 898  HIS   A O     1 
ATOM   6582  C  CB    . HIS   A  1  900  ? -19.962 94.032  91.104  1.00 23.32 ? 898  HIS   A CB    1 
ATOM   6583  C  CG    . HIS   A  1  900  ? -19.356 93.012  90.196  1.00 24.77 ? 898  HIS   A CG    1 
ATOM   6584  N  ND1   . HIS   A  1  900  ? -18.020 93.018  89.861  1.00 25.38 ? 898  HIS   A ND1   1 
ATOM   6585  C  CD2   . HIS   A  1  900  ? -19.911 91.978  89.521  1.00 25.09 ? 898  HIS   A CD2   1 
ATOM   6586  C  CE1   . HIS   A  1  900  ? -17.773 92.015  89.038  1.00 25.57 ? 898  HIS   A CE1   1 
ATOM   6587  N  NE2   . HIS   A  1  900  ? -18.903 91.370  88.815  1.00 23.27 ? 898  HIS   A NE2   1 
ATOM   6588  N  N     . ILE   A  1  901  ? -22.133 94.903  89.079  1.00 22.57 ? 899  ILE   A N     1 
ATOM   6589  C  CA    . ILE   A  1  901  ? -22.837 94.705  87.817  1.00 25.68 ? 899  ILE   A CA    1 
ATOM   6590  C  C     . ILE   A  1  901  ? -22.711 95.937  86.935  1.00 26.77 ? 899  ILE   A C     1 
ATOM   6591  O  O     . ILE   A  1  901  ? -22.465 95.831  85.728  1.00 29.48 ? 899  ILE   A O     1 
ATOM   6592  C  CB    . ILE   A  1  901  ? -24.306 94.332  88.074  1.00 21.41 ? 899  ILE   A CB    1 
ATOM   6593  C  CG1   . ILE   A  1  901  ? -24.387 93.005  88.831  1.00 25.61 ? 899  ILE   A CG1   1 
ATOM   6594  C  CG2   . ILE   A  1  901  ? -25.081 94.277  86.759  1.00 26.16 ? 899  ILE   A CG2   1 
ATOM   6595  C  CD1   . ILE   A  1  901  ? -25.787 92.671  89.332  1.00 21.81 ? 899  ILE   A CD1   1 
ATOM   6596  N  N     . GLU   A  1  902  ? -22.870 97.125  87.522  1.00 29.29 ? 900  GLU   A N     1 
ATOM   6597  C  CA    . GLU   A  1  902  ? -22.820 98.345  86.722  1.00 30.56 ? 900  GLU   A CA    1 
ATOM   6598  C  C     . GLU   A  1  902  ? -21.406 98.647  86.243  1.00 30.35 ? 900  GLU   A C     1 
ATOM   6599  O  O     . GLU   A  1  902  ? -21.222 99.159  85.133  1.00 36.48 ? 900  GLU   A O     1 
ATOM   6600  C  CB    . GLU   A  1  902  ? -23.418 99.521  87.494  1.00 35.92 ? 900  GLU   A CB    1 
ATOM   6601  C  CG    . GLU   A  1  902  ? -24.918 99.401  87.671  1.00 37.89 ? 900  GLU   A CG    1 
ATOM   6602  C  CD    . GLU   A  1  902  ? -25.615 99.062  86.368  1.00 40.06 ? 900  GLU   A CD    1 
ATOM   6603  O  OE1   . GLU   A  1  902  ? -25.387 99.777  85.369  1.00 41.85 ? 900  GLU   A OE1   1 
ATOM   6604  O  OE2   . GLU   A  1  902  ? -26.377 98.068  86.339  1.00 40.80 ? 900  GLU   A OE2   1 
ATOM   6605  N  N     . ARG   A  1  903  ? -20.398 98.348  87.062  1.00 31.24 ? 901  ARG   A N     1 
ATOM   6606  C  CA    . ARG   A  1  903  ? -19.019 98.451  86.594  1.00 32.89 ? 901  ARG   A CA    1 
ATOM   6607  C  C     . ARG   A  1  903  ? -18.804 97.586  85.358  1.00 37.03 ? 901  ARG   A C     1 
ATOM   6608  O  O     . ARG   A  1  903  ? -18.287 98.057  84.338  1.00 38.17 ? 901  ARG   A O     1 
ATOM   6609  C  CB    . ARG   A  1  903  ? -18.047 98.064  87.708  1.00 36.07 ? 901  ARG   A CB    1 
ATOM   6610  N  N     . MET   A  1  904  ? -19.219 96.316  85.425  1.00 32.81 ? 902  MET   A N     1 
ATOM   6611  C  CA    . MET   A  1  904  ? -19.106 95.433  84.267  1.00 33.00 ? 902  MET   A CA    1 
ATOM   6612  C  C     . MET   A  1  904  ? -19.886 95.982  83.080  1.00 32.65 ? 902  MET   A C     1 
ATOM   6613  O  O     . MET   A  1  904  ? -19.397 95.985  81.945  1.00 32.72 ? 902  MET   A O     1 
ATOM   6614  C  CB    . MET   A  1  904  ? -19.615 94.037  84.623  1.00 28.36 ? 902  MET   A CB    1 
ATOM   6615  C  CG    . MET   A  1  904  ? -18.814 93.338  85.682  1.00 26.90 ? 902  MET   A CG    1 
ATOM   6616  S  SD    . MET   A  1  904  ? -17.120 93.065  85.133  1.00 39.02 ? 902  MET   A SD    1 
ATOM   6617  C  CE    . MET   A  1  904  ? -16.231 94.269  86.119  1.00 40.08 ? 902  MET   A CE    1 
ATOM   6618  N  N     . ARG   A  1  905  ? -21.116 96.438  83.324  1.00 30.33 ? 903  ARG   A N     1 
ATOM   6619  C  CA    . ARG   A  1  905  ? -21.916 96.996  82.241  1.00 31.11 ? 903  ARG   A CA    1 
ATOM   6620  C  C     . ARG   A  1  905  ? -21.242 98.222  81.645  1.00 39.57 ? 903  ARG   A C     1 
ATOM   6621  O  O     . ARG   A  1  905  ? -21.263 98.419  80.425  1.00 35.18 ? 903  ARG   A O     1 
ATOM   6622  C  CB    . ARG   A  1  905  ? -23.316 97.338  82.748  1.00 31.99 ? 903  ARG   A CB    1 
ATOM   6623  C  CG    . ARG   A  1  905  ? -24.361 97.414  81.656  1.00 38.93 ? 903  ARG   A CG    1 
ATOM   6624  C  CD    . ARG   A  1  905  ? -25.624 98.062  82.167  1.00 39.67 ? 903  ARG   A CD    1 
ATOM   6625  N  NE    . ARG   A  1  905  ? -26.133 97.427  83.377  1.00 36.98 ? 903  ARG   A NE    1 
ATOM   6626  C  CZ    . ARG   A  1  905  ? -26.994 96.418  83.389  1.00 34.67 ? 903  ARG   A CZ    1 
ATOM   6627  N  NH1   . ARG   A  1  905  ? -27.405 95.846  82.267  1.00 34.79 ? 903  ARG   A NH1   1 
ATOM   6628  N  NH2   . ARG   A  1  905  ? -27.461 95.978  84.554  1.00 36.85 ? 903  ARG   A NH2   1 
ATOM   6629  N  N     . GLY   A  1  906  ? -20.623 99.047  82.494  1.00 35.70 ? 904  GLY   A N     1 
ATOM   6630  C  CA    . GLY   A  1  906  ? -19.912 100.218 82.020  1.00 42.26 ? 904  GLY   A CA    1 
ATOM   6631  C  C     . GLY   A  1  906  ? -18.692 99.901  81.180  1.00 44.76 ? 904  GLY   A C     1 
ATOM   6632  O  O     . GLY   A  1  906  ? -18.289 100.731 80.359  1.00 50.49 ? 904  GLY   A O     1 
ATOM   6633  N  N     . LEU   A  1  907  ? -18.095 98.724  81.364  1.00 42.52 ? 905  LEU   A N     1 
ATOM   6634  C  CA    . LEU   A  1  907  ? -16.959 98.298  80.553  1.00 42.67 ? 905  LEU   A CA    1 
ATOM   6635  C  C     . LEU   A  1  907  ? -17.376 97.702  79.215  1.00 41.10 ? 905  LEU   A C     1 
ATOM   6636  O  O     . LEU   A  1  907  ? -16.505 97.279  78.449  1.00 42.93 ? 905  LEU   A O     1 
ATOM   6637  C  CB    . LEU   A  1  907  ? -16.099 97.290  81.323  1.00 39.51 ? 905  LEU   A CB    1 
ATOM   6638  C  CG    . LEU   A  1  907  ? -15.481 97.809  82.621  1.00 43.16 ? 905  LEU   A CG    1 
ATOM   6639  C  CD1   . LEU   A  1  907  ? -14.525 96.787  83.214  1.00 46.32 ? 905  LEU   A CD1   1 
ATOM   6640  C  CD2   . LEU   A  1  907  ? -14.780 99.138  82.382  1.00 49.76 ? 905  LEU   A CD2   1 
ATOM   6641  N  N     . GLY   A  1  908  ? -18.673 97.658  78.920  1.00 37.12 ? 906  GLY   A N     1 
ATOM   6642  C  CA    . GLY   A  1  908  ? -19.161 97.104  77.678  1.00 37.39 ? 906  GLY   A CA    1 
ATOM   6643  C  C     . GLY   A  1  908  ? -19.521 95.637  77.725  1.00 30.31 ? 906  GLY   A C     1 
ATOM   6644  O  O     . GLY   A  1  908  ? -19.967 95.095  76.707  1.00 31.35 ? 906  GLY   A O     1 
ATOM   6645  N  N     . ARG   A  1  909  ? -19.360 94.978  78.867  1.00 31.25 ? 907  ARG   A N     1 
ATOM   6646  C  CA    . ARG   A  1  909  ? -19.654 93.555  78.948  1.00 26.39 ? 907  ARG   A CA    1 
ATOM   6647  C  C     . ARG   A  1  909  ? -21.151 93.312  78.801  1.00 29.63 ? 907  ARG   A C     1 
ATOM   6648  O  O     . ARG   A  1  909  ? -21.977 94.085  79.298  1.00 30.70 ? 907  ARG   A O     1 
ATOM   6649  C  CB    . ARG   A  1  909  ? -19.160 92.996  80.280  1.00 27.01 ? 907  ARG   A CB    1 
ATOM   6650  C  CG    . ARG   A  1  909  ? -17.701 93.301  80.585  1.00 30.70 ? 907  ARG   A CG    1 
ATOM   6651  C  CD    . ARG   A  1  909  ? -16.760 92.669  79.565  1.00 34.39 ? 907  ARG   A CD    1 
ATOM   6652  N  NE    . ARG   A  1  909  ? -15.363 92.768  79.977  1.00 33.22 ? 907  ARG   A NE    1 
ATOM   6653  C  CZ    . ARG   A  1  909  ? -14.505 93.678  79.532  1.00 44.73 ? 907  ARG   A CZ    1 
ATOM   6654  N  NH1   . ARG   A  1  909  ? -14.868 94.602  78.655  1.00 42.11 ? 907  ARG   A NH1   1 
ATOM   6655  N  NH2   . ARG   A  1  909  ? -13.251 93.661  79.979  1.00 42.45 ? 907  ARG   A NH2   1 
ATOM   6656  N  N     . LYS   A  1  910  ? -21.498 92.235  78.097  1.00 23.39 ? 908  LYS   A N     1 
ATOM   6657  C  CA    . LYS   A  1  910  ? -22.895 91.868  77.917  1.00 23.91 ? 908  LYS   A CA    1 
ATOM   6658  C  C     . LYS   A  1  910  ? -23.475 91.358  79.232  1.00 22.96 ? 908  LYS   A C     1 
ATOM   6659  O  O     . LYS   A  1  910  ? -22.929 90.440  79.851  1.00 22.45 ? 908  LYS   A O     1 
ATOM   6660  C  CB    . LYS   A  1  910  ? -23.018 90.788  76.844  1.00 27.30 ? 908  LYS   A CB    1 
ATOM   6661  C  CG    . LYS   A  1  910  ? -22.921 91.300  75.423  1.00 34.80 ? 908  LYS   A CG    1 
ATOM   6662  C  CD    . LYS   A  1  910  ? -23.318 90.219  74.430  1.00 36.54 ? 908  LYS   A CD    1 
ATOM   6663  C  CE    . LYS   A  1  910  ? -24.728 89.723  74.697  1.00 37.62 ? 908  LYS   A CE    1 
ATOM   6664  N  NZ    . LYS   A  1  910  ? -25.229 88.879  73.573  1.00 45.45 ? 908  LYS   A NZ    1 
ATOM   6665  N  N     . VAL   A  1  911  ? -24.590 91.949  79.652  1.00 23.62 ? 909  VAL   A N     1 
ATOM   6666  C  CA    . VAL   A  1  911  ? -25.224 91.647  80.932  1.00 22.78 ? 909  VAL   A CA    1 
ATOM   6667  C  C     . VAL   A  1  911  ? -26.656 91.212  80.659  1.00 24.01 ? 909  VAL   A C     1 
ATOM   6668  O  O     . VAL   A  1  911  ? -27.434 91.963  80.056  1.00 25.46 ? 909  VAL   A O     1 
ATOM   6669  C  CB    . VAL   A  1  911  ? -25.197 92.861  81.875  1.00 25.67 ? 909  VAL   A CB    1 
ATOM   6670  C  CG1   . VAL   A  1  911  ? -25.894 92.527  83.191  1.00 25.10 ? 909  VAL   A CG1   1 
ATOM   6671  C  CG2   . VAL   A  1  911  ? -23.762 93.328  82.116  1.00 25.04 ? 909  VAL   A CG2   1 
ATOM   6672  N  N     . GLU   A  1  912  ? -26.996 90.004  81.096  1.00 21.19 ? 910  GLU   A N     1 
ATOM   6673  C  CA    . GLU   A  1  912  ? -28.349 89.471  81.025  1.00 23.70 ? 910  GLU   A CA    1 
ATOM   6674  C  C     . GLU   A  1  912  ? -28.913 89.442  82.439  1.00 21.74 ? 910  GLU   A C     1 
ATOM   6675  O  O     . GLU   A  1  912  ? -28.255 88.939  83.355  1.00 21.11 ? 910  GLU   A O     1 
ATOM   6676  C  CB    . GLU   A  1  912  ? -28.315 88.045  80.468  1.00 23.09 ? 910  GLU   A CB    1 
ATOM   6677  C  CG    . GLU   A  1  912  ? -29.679 87.445  80.175  1.00 22.69 ? 910  GLU   A CG    1 
ATOM   6678  C  CD    . GLU   A  1  912  ? -30.276 88.007  78.900  1.00 26.96 ? 910  GLU   A CD    1 
ATOM   6679  O  OE1   . GLU   A  1  912  ? -29.526 88.635  78.126  1.00 27.60 ? 910  GLU   A OE1   1 
ATOM   6680  O  OE2   . GLU   A  1  912  ? -31.491 87.828  78.675  1.00 26.03 ? 910  GLU   A OE2   1 
ATOM   6681  N  N     . GLN   A  1  913  ? -30.112 89.999  82.627  1.00 21.38 ? 911  GLN   A N     1 
ATOM   6682  C  CA    . GLN   A  1  913  ? -30.722 90.016  83.948  1.00 24.23 ? 911  GLN   A CA    1 
ATOM   6683  C  C     . GLN   A  1  913  ? -32.197 89.671  83.859  1.00 25.66 ? 911  GLN   A C     1 
ATOM   6684  O  O     . GLN   A  1  913  ? -32.881 90.081  82.921  1.00 26.28 ? 911  GLN   A O     1 
ATOM   6685  C  CB    . GLN   A  1  913  ? -30.585 91.390  84.617  1.00 23.69 ? 911  GLN   A CB    1 
ATOM   6686  C  CG    . GLN   A  1  913  ? -29.161 91.776  84.951  1.00 26.33 ? 911  GLN   A CG    1 
ATOM   6687  C  CD    . GLN   A  1  913  ? -29.105 93.001  85.839  1.00 27.19 ? 911  GLN   A CD    1 
ATOM   6688  O  OE1   . GLN   A  1  913  ? -29.564 94.079  85.457  1.00 29.95 ? 911  GLN   A OE1   1 
ATOM   6689  N  NE2   . GLN   A  1  913  ? -28.565 92.839  87.035  1.00 25.70 ? 911  GLN   A NE2   1 
ATOM   6690  N  N     . ILE   A  1  914  ? -32.668 88.910  84.845  1.00 25.53 ? 912  ILE   A N     1 
ATOM   6691  C  CA    . ILE   A  1  914  ? -34.092 88.658  85.015  1.00 23.45 ? 912  ILE   A CA    1 
ATOM   6692  C  C     . ILE   A  1  914  ? -34.783 89.962  85.378  1.00 26.66 ? 912  ILE   A C     1 
ATOM   6693  O  O     . ILE   A  1  914  ? -34.235 90.792  86.114  1.00 25.84 ? 912  ILE   A O     1 
ATOM   6694  C  CB    . ILE   A  1  914  ? -34.272 87.640  86.155  1.00 27.72 ? 912  ILE   A CB    1 
ATOM   6695  C  CG1   . ILE   A  1  914  ? -33.761 86.267  85.749  1.00 30.03 ? 912  ILE   A CG1   1 
ATOM   6696  C  CG2   . ILE   A  1  914  ? -35.720 87.561  86.613  1.00 41.36 ? 912  ILE   A CG2   1 
ATOM   6697  C  CD1   . ILE   A  1  914  ? -33.858 85.290  86.878  1.00 30.56 ? 912  ILE   A CD1   1 
ATOM   6698  N  N     . GLY   A  1  915  ? -35.999 90.152  84.869  1.00 29.08 ? 913  GLY   A N     1 
ATOM   6699  C  CA    . GLY   A  1  915  ? -36.829 91.243  85.346  1.00 28.07 ? 913  GLY   A CA    1 
ATOM   6700  C  C     . GLY   A  1  915  ? -37.478 90.840  86.655  1.00 28.74 ? 913  GLY   A C     1 
ATOM   6701  O  O     . GLY   A  1  915  ? -38.016 89.735  86.780  1.00 35.35 ? 913  GLY   A O     1 
ATOM   6702  N  N     . LEU   A  1  916  ? -37.412 91.725  87.642  1.00 28.03 ? 914  LEU   A N     1 
ATOM   6703  C  CA    . LEU   A  1  916  ? -37.956 91.436  88.959  1.00 29.97 ? 914  LEU   A CA    1 
ATOM   6704  C  C     . LEU   A  1  916  ? -39.385 91.944  89.080  1.00 30.38 ? 914  LEU   A C     1 
ATOM   6705  O  O     . LEU   A  1  916  ? -39.750 92.978  88.514  1.00 33.74 ? 914  LEU   A O     1 
ATOM   6706  C  CB    . LEU   A  1  916  ? -37.110 92.093  90.045  1.00 28.74 ? 914  LEU   A CB    1 
ATOM   6707  C  CG    . LEU   A  1  916  ? -35.668 91.605  90.129  1.00 28.67 ? 914  LEU   A CG    1 
ATOM   6708  C  CD1   . LEU   A  1  916  ? -34.970 92.275  91.294  1.00 32.25 ? 914  LEU   A CD1   1 
ATOM   6709  C  CD2   . LEU   A  1  916  ? -35.641 90.092  90.274  1.00 32.47 ? 914  LEU   A CD2   1 
ATOM   6710  N  N     . ALA   A  1  917  ? -40.187 91.212  89.848  1.00 27.03 ? 915  ALA   A N     1 
ATOM   6711  C  CA    . ALA   A  1  917  ? -41.559 91.619  90.095  1.00 28.71 ? 915  ALA   A CA    1 
ATOM   6712  C  C     . ALA   A  1  917  ? -41.593 92.821  91.034  1.00 30.61 ? 915  ALA   A C     1 
ATOM   6713  O  O     . ALA   A  1  917  ? -40.664 93.072  91.808  1.00 30.28 ? 915  ALA   A O     1 
ATOM   6714  C  CB    . ALA   A  1  917  ? -42.352 90.465  90.706  1.00 32.05 ? 915  ALA   A CB    1 
ATOM   6715  N  N     . SER   A  1  918  ? -42.695 93.572  90.961  1.00 28.10 ? 916  SER   A N     1 
ATOM   6716  C  CA    . SER   A  1  918  ? -42.836 94.757  91.801  1.00 32.69 ? 916  SER   A CA    1 
ATOM   6717  C  C     . SER   A  1  918  ? -42.804 94.404  93.281  1.00 30.01 ? 916  SER   A C     1 
ATOM   6718  O  O     . SER   A  1  918  ? -42.372 95.221  94.102  1.00 28.66 ? 916  SER   A O     1 
ATOM   6719  C  CB    . SER   A  1  918  ? -44.137 95.482  91.460  1.00 31.81 ? 916  SER   A CB    1 
ATOM   6720  O  OG    . SER   A  1  918  ? -45.235 94.594  91.579  1.00 37.59 ? 916  SER   A OG    1 
ATOM   6721  N  N     . GLU   A  1  919  ? -43.238 93.189  93.634  1.00 32.73 ? 917  GLU   A N     1 
ATOM   6722  C  CA    . GLU   A  1  919  ? -43.285 92.764  95.028  1.00 29.18 ? 917  GLU   A CA    1 
ATOM   6723  C  C     . GLU   A  1  919  ? -41.906 92.718  95.669  1.00 30.15 ? 917  GLU   A C     1 
ATOM   6724  O  O     . GLU   A  1  919  ? -41.808 92.734  96.899  1.00 29.10 ? 917  GLU   A O     1 
ATOM   6725  C  CB    . GLU   A  1  919  ? -43.937 91.381  95.135  1.00 31.35 ? 917  GLU   A CB    1 
ATOM   6726  C  CG    . GLU   A  1  919  ? -45.453 91.361  94.961  1.00 35.82 ? 917  GLU   A CG    1 
ATOM   6727  C  CD    . GLU   A  1  919  ? -45.895 91.470  93.512  1.00 44.13 ? 917  GLU   A CD    1 
ATOM   6728  O  OE1   . GLU   A  1  919  ? -45.027 91.534  92.615  1.00 39.98 ? 917  GLU   A OE1   1 
ATOM   6729  O  OE2   . GLU   A  1  919  ? -47.120 91.488  93.268  1.00 48.61 ? 917  GLU   A OE2   1 
ATOM   6730  N  N     . THR   A  1  920  ? -40.841 92.658  94.870  1.00 28.29 ? 918  THR   A N     1 
ATOM   6731  C  CA    . THR   A  1  920  ? -39.502 92.619  95.443  1.00 25.81 ? 918  THR   A CA    1 
ATOM   6732  C  C     . THR   A  1  920  ? -39.104 93.949  96.066  1.00 24.71 ? 918  THR   A C     1 
ATOM   6733  O  O     . THR   A  1  920  ? -38.159 93.988  96.858  1.00 24.54 ? 918  THR   A O     1 
ATOM   6734  C  CB    . THR   A  1  920  ? -38.479 92.201  94.383  1.00 25.56 ? 918  THR   A CB    1 
ATOM   6735  O  OG1   . THR   A  1  920  ? -38.464 93.159  93.318  1.00 26.77 ? 918  THR   A OG1   1 
ATOM   6736  C  CG2   . THR   A  1  920  ? -38.819 90.826  93.824  1.00 24.21 ? 918  THR   A CG2   1 
ATOM   6737  N  N     . GLY   A  1  921  ? -39.816 95.033  95.739  1.00 27.55 ? 919  GLY   A N     1 
ATOM   6738  C  CA    . GLY   A  1  921  ? -39.432 96.348  96.229  1.00 28.41 ? 919  GLY   A CA    1 
ATOM   6739  C  C     . GLY   A  1  921  ? -39.420 96.468  97.741  1.00 25.76 ? 919  GLY   A C     1 
ATOM   6740  O  O     . GLY   A  1  921  ? -38.695 97.298  98.292  1.00 28.42 ? 919  GLY   A O     1 
ATOM   6741  N  N     . VAL   A  1  922  ? -40.210 95.643  98.434  1.00 26.80 ? 920  VAL   A N     1 
ATOM   6742  C  CA    . VAL   A  1  922  ? -40.241 95.693  99.895  1.00 26.69 ? 920  VAL   A CA    1 
ATOM   6743  C  C     . VAL   A  1  922  ? -39.067 94.973  100.539 1.00 26.48 ? 920  VAL   A C     1 
ATOM   6744  O  O     . VAL   A  1  922  ? -38.885 95.079  101.757 1.00 27.26 ? 920  VAL   A O     1 
ATOM   6745  C  CB    . VAL   A  1  922  ? -41.568 95.167  100.470 1.00 25.02 ? 920  VAL   A CB    1 
ATOM   6746  C  CG1   . VAL   A  1  922  ? -42.709 96.088  100.073 1.00 24.95 ? 920  VAL   A CG1   1 
ATOM   6747  C  CG2   . VAL   A  1  922  ? -41.829 93.757  99.981  1.00 25.57 ? 920  VAL   A CG2   1 
ATOM   6748  N  N     . GLY   A  1  923  ? -38.269 94.243  99.762  1.00 23.34 ? 921  GLY   A N     1 
ATOM   6749  C  CA    . GLY   A  1  923  ? -37.073 93.627  100.297 1.00 24.39 ? 921  GLY   A CA    1 
ATOM   6750  C  C     . GLY   A  1  923  ? -35.836 94.050  99.535  1.00 22.06 ? 921  GLY   A C     1 
ATOM   6751  O  O     . GLY   A  1  923  ? -35.861 95.050  98.812  1.00 24.84 ? 921  GLY   A O     1 
ATOM   6752  N  N     . THR   A  1  924  ? -34.745 93.309  99.689  1.00 20.41 ? 922  THR   A N     1 
ATOM   6753  C  CA    . THR   A  1  924  ? -33.481 93.639  99.036  1.00 21.46 ? 922  THR   A CA    1 
ATOM   6754  C  C     . THR   A  1  924  ? -33.136 92.508  98.077  1.00 22.24 ? 922  THR   A C     1 
ATOM   6755  O  O     . THR   A  1  924  ? -32.567 91.492  98.484  1.00 23.74 ? 922  THR   A O     1 
ATOM   6756  C  CB    . THR   A  1  924  ? -32.376 93.881  100.059 1.00 21.94 ? 922  THR   A CB    1 
ATOM   6757  O  OG1   . THR   A  1  924  ? -32.305 92.783  100.980 1.00 22.35 ? 922  THR   A OG1   1 
ATOM   6758  C  CG2   . THR   A  1  924  ? -32.671 95.155  100.828 1.00 26.27 ? 922  THR   A CG2   1 
ATOM   6759  N  N     . PHE   A  1  925  ? -33.472 92.689  96.806  1.00 20.75 ? 923  PHE   A N     1 
ATOM   6760  C  CA    . PHE   A  1  925  ? -33.260 91.661  95.803  1.00 17.45 ? 923  PHE   A CA    1 
ATOM   6761  C  C     . PHE   A  1  925  ? -32.316 92.160  94.722  1.00 21.06 ? 923  PHE   A C     1 
ATOM   6762  O  O     . PHE   A  1  925  ? -32.326 93.336  94.341  1.00 23.19 ? 923  PHE   A O     1 
ATOM   6763  C  CB    . PHE   A  1  925  ? -34.571 91.259  95.119  1.00 18.15 ? 923  PHE   A CB    1 
ATOM   6764  C  CG    . PHE   A  1  925  ? -35.531 90.542  96.016  1.00 21.43 ? 923  PHE   A CG    1 
ATOM   6765  C  CD1   . PHE   A  1  925  ? -36.377 91.252  96.853  1.00 20.72 ? 923  PHE   A CD1   1 
ATOM   6766  C  CD2   . PHE   A  1  925  ? -35.600 89.163  96.013  1.00 18.86 ? 923  PHE   A CD2   1 
ATOM   6767  C  CE1   . PHE   A  1  925  ? -37.283 90.592  97.666  1.00 21.34 ? 923  PHE   A CE1   1 
ATOM   6768  C  CE2   . PHE   A  1  925  ? -36.498 88.497  96.827  1.00 20.27 ? 923  PHE   A CE2   1 
ATOM   6769  C  CZ    . PHE   A  1  925  ? -37.341 89.217  97.654  1.00 19.17 ? 923  PHE   A CZ    1 
ATOM   6770  N  N     . VAL   A  1  926  ? -31.517 91.227  94.217  1.00 20.50 ? 924  VAL   A N     1 
ATOM   6771  C  CA    . VAL   A  1  926  ? -30.709 91.426  93.029  1.00 20.75 ? 924  VAL   A CA    1 
ATOM   6772  C  C     . VAL   A  1  926  ? -31.137 90.353  92.028  1.00 19.41 ? 924  VAL   A C     1 
ATOM   6773  O  O     . VAL   A  1  926  ? -31.174 89.178  92.385  1.00 20.41 ? 924  VAL   A O     1 
ATOM   6774  C  CB    . VAL   A  1  926  ? -29.204 91.313  93.321  1.00 19.63 ? 924  VAL   A CB    1 
ATOM   6775  C  CG1   . VAL   A  1  926  ? -28.400 91.410  92.036  1.00 22.86 ? 924  VAL   A CG1   1 
ATOM   6776  C  CG2   . VAL   A  1  926  ? -28.789 92.412  94.294  1.00 22.81 ? 924  VAL   A CG2   1 
ATOM   6777  N  N     . PRO   A  1  927  ? -31.482 90.710  90.804  1.00 20.28 ? 925  PRO   A N     1 
ATOM   6778  C  CA    . PRO   A  1  927  ? -31.882 89.691  89.843  1.00 21.66 ? 925  PRO   A CA    1 
ATOM   6779  C  C     . PRO   A  1  927  ? -30.695 88.831  89.464  1.00 20.43 ? 925  PRO   A C     1 
ATOM   6780  O  O     . PRO   A  1  927  ? -29.566 89.334  89.334  1.00 21.46 ? 925  PRO   A O     1 
ATOM   6781  C  CB    . PRO   A  1  927  ? -32.366 90.512  88.643  1.00 24.41 ? 925  PRO   A CB    1 
ATOM   6782  C  CG    . PRO   A  1  927  ? -31.617 91.788  88.739  1.00 27.80 ? 925  PRO   A CG    1 
ATOM   6783  C  CD    . PRO   A  1  927  ? -31.457 92.057  90.210  1.00 23.91 ? 925  PRO   A CD    1 
ATOM   6784  N  N     . PRO   A  1  928  ? -30.902 87.526  89.330  1.00 21.17 ? 926  PRO   A N     1 
ATOM   6785  C  CA    . PRO   A  1  928  ? -29.873 86.679  88.730  1.00 19.71 ? 926  PRO   A CA    1 
ATOM   6786  C  C     . PRO   A  1  928  ? -29.364 87.308  87.446  1.00 17.91 ? 926  PRO   A C     1 
ATOM   6787  O  O     . PRO   A  1  928  ? -30.136 87.789  86.610  1.00 20.01 ? 926  PRO   A O     1 
ATOM   6788  C  CB    . PRO   A  1  928  ? -30.616 85.365  88.477  1.00 19.46 ? 926  PRO   A CB    1 
ATOM   6789  C  CG    . PRO   A  1  928  ? -31.596 85.314  89.604  1.00 20.95 ? 926  PRO   A CG    1 
ATOM   6790  C  CD    . PRO   A  1  928  ? -32.062 86.743  89.787  1.00 22.37 ? 926  PRO   A CD    1 
ATOM   6791  N  N     . THR   A  1  929  ? -28.047 87.322  87.312  1.00 17.97 ? 927  THR   A N     1 
ATOM   6792  C  CA    . THR   A  1  929  ? -27.354 88.108  86.311  1.00 20.02 ? 927  THR   A CA    1 
ATOM   6793  C  C     . THR   A  1  929  ? -26.276 87.245  85.680  1.00 18.67 ? 927  THR   A C     1 
ATOM   6794  O  O     . THR   A  1  929  ? -25.580 86.507  86.374  1.00 19.44 ? 927  THR   A O     1 
ATOM   6795  C  CB    . THR   A  1  929  ? -26.719 89.330  86.993  1.00 20.68 ? 927  THR   A CB    1 
ATOM   6796  O  OG1   . THR   A  1  929  ? -27.762 90.135  87.558  1.00 22.39 ? 927  THR   A OG1   1 
ATOM   6797  C  CG2   . THR   A  1  929  ? -25.909 90.169  86.008  1.00 22.55 ? 927  THR   A CG2   1 
ATOM   6798  N  N     . ILE   A  1  930  ? -26.160 87.323  84.361  1.00 18.33 ? 928  ILE   A N     1 
ATOM   6799  C  CA    . ILE   A  1  930  ? -25.080 86.671  83.632  1.00 18.89 ? 928  ILE   A CA    1 
ATOM   6800  C  C     . ILE   A  1  930  ? -24.267 87.762  82.966  1.00 20.27 ? 928  ILE   A C     1 
ATOM   6801  O  O     . ILE   A  1  930  ? -24.826 88.599  82.249  1.00 21.65 ? 928  ILE   A O     1 
ATOM   6802  C  CB    . ILE   A  1  930  ? -25.617 85.694  82.572  1.00 18.08 ? 928  ILE   A CB    1 
ATOM   6803  C  CG1   . ILE   A  1  930  ? -26.386 84.548  83.226  1.00 21.51 ? 928  ILE   A CG1   1 
ATOM   6804  C  CG2   . ILE   A  1  930  ? -24.464 85.161  81.715  1.00 22.59 ? 928  ILE   A CG2   1 
ATOM   6805  C  CD1   . ILE   A  1  930  ? -27.187 83.720  82.233  1.00 22.07 ? 928  ILE   A CD1   1 
ATOM   6806  N  N     . ILE   A  1  931  ? -22.959 87.758  83.201  1.00 20.02 ? 929  ILE   A N     1 
ATOM   6807  C  CA    . ILE   A  1  931  ? -22.048 88.763  82.665  1.00 21.46 ? 929  ILE   A CA    1 
ATOM   6808  C  C     . ILE   A  1  931  ? -21.007 88.048  81.820  1.00 21.48 ? 929  ILE   A C     1 
ATOM   6809  O  O     . ILE   A  1  931  ? -20.317 87.147  82.305  1.00 21.32 ? 929  ILE   A O     1 
ATOM   6810  C  CB    . ILE   A  1  931  ? -21.372 89.574  83.778  1.00 23.14 ? 929  ILE   A CB    1 
ATOM   6811  C  CG1   . ILE   A  1  931  ? -22.420 90.296  84.631  1.00 22.49 ? 929  ILE   A CG1   1 
ATOM   6812  C  CG2   . ILE   A  1  931  ? -20.388 90.567  83.175  1.00 23.99 ? 929  ILE   A CG2   1 
ATOM   6813  C  CD1   . ILE   A  1  931  ? -21.815 91.187  85.701  1.00 24.87 ? 929  ILE   A CD1   1 
ATOM   6814  N  N     . GLU   A  1  932  ? -20.891 88.442  80.562  1.00 22.00 ? 930  GLU   A N     1 
ATOM   6815  C  CA    . GLU   A  1  932  ? -19.933 87.821  79.662  1.00 21.35 ? 930  GLU   A CA    1 
ATOM   6816  C  C     . GLU   A  1  932  ? -18.625 88.597  79.723  1.00 20.90 ? 930  GLU   A C     1 
ATOM   6817  O  O     . GLU   A  1  932  ? -18.582 89.787  79.395  1.00 23.86 ? 930  GLU   A O     1 
ATOM   6818  C  CB    . GLU   A  1  932  ? -20.506 87.785  78.251  1.00 20.12 ? 930  GLU   A CB    1 
ATOM   6819  C  CG    . GLU   A  1  932  ? -21.660 86.806  78.129  1.00 22.50 ? 930  GLU   A CG    1 
ATOM   6820  C  CD    . GLU   A  1  932  ? -22.426 86.970  76.844  1.00 26.35 ? 930  GLU   A CD    1 
ATOM   6821  O  OE1   . GLU   A  1  932  ? -21.796 86.917  75.769  1.00 27.69 ? 930  GLU   A OE1   1 
ATOM   6822  O  OE2   . GLU   A  1  932  ? -23.659 87.157  76.914  1.00 25.16 ? 930  GLU   A OE2   1 
ATOM   6823  N  N     . LEU   A  1  933  ? -17.575 87.935  80.174  1.00 22.33 ? 931  LEU   A N     1 
ATOM   6824  C  CA    . LEU   A  1  933  ? -16.275 88.562  80.330  1.00 23.68 ? 931  LEU   A CA    1 
ATOM   6825  C  C     . LEU   A  1  933  ? -15.362 88.201  79.170  1.00 28.15 ? 931  LEU   A C     1 
ATOM   6826  O  O     . LEU   A  1  933  ? -15.537 87.181  78.498  1.00 26.39 ? 931  LEU   A O     1 
ATOM   6827  C  CB    . LEU   A  1  933  ? -15.618 88.124  81.641  1.00 28.15 ? 931  LEU   A CB    1 
ATOM   6828  C  CG    . LEU   A  1  933  ? -16.343 88.520  82.932  1.00 27.50 ? 931  LEU   A CG    1 
ATOM   6829  C  CD1   . LEU   A  1  933  ? -15.508 88.117  84.131  1.00 32.87 ? 931  LEU   A CD1   1 
ATOM   6830  C  CD2   . LEU   A  1  933  ? -16.632 90.011  82.953  1.00 32.28 ? 931  LEU   A CD2   1 
ATOM   6831  N  N     . GLU   A  1  934  ? -14.358 89.055  78.959  1.00 29.08 ? 932  GLU   A N     1 
ATOM   6832  C  CA    . GLU   A  1  934  ? -13.323 88.773  77.972  1.00 36.25 ? 932  GLU   A CA    1 
ATOM   6833  C  C     . GLU   A  1  934  ? -12.231 87.886  78.561  1.00 37.34 ? 932  GLU   A C     1 
ATOM   6834  O  O     . GLU   A  1  934  ? -11.820 86.900  77.940  1.00 43.02 ? 932  GLU   A O     1 
ATOM   6835  C  CB    . GLU   A  1  934  ? -12.739 90.081  77.436  1.00 39.49 ? 932  GLU   A CB    1 
ATOM   6836  N  N     . LYS   A  1  935  ? -11.765 88.212  79.764  1.00 37.05 ? 933  LYS   A N     1 
ATOM   6837  C  CA    . LYS   A  1  935  ? -10.715 87.459  80.435  1.00 41.28 ? 933  LYS   A CA    1 
ATOM   6838  C  C     . LYS   A  1  935  ? -11.099 87.246  81.891  1.00 41.27 ? 933  LYS   A C     1 
ATOM   6839  O  O     . LYS   A  1  935  ? -11.834 88.046  82.475  1.00 36.69 ? 933  LYS   A O     1 
ATOM   6840  C  CB    . LYS   A  1  935  ? -9.376  88.205  80.387  1.00 40.46 ? 933  LYS   A CB    1 
ATOM   6841  N  N     . LEU   A  1  936  ? -10.587 86.159  82.474  1.00 38.38 ? 934  LEU   A N     1 
ATOM   6842  C  CA    . LEU   A  1  936  ? -10.826 85.894  83.889  1.00 40.84 ? 934  LEU   A CA    1 
ATOM   6843  C  C     . LEU   A  1  936  ? -10.253 86.988  84.779  1.00 43.92 ? 934  LEU   A C     1 
ATOM   6844  O  O     . LEU   A  1  936  ? -10.731 87.173  85.905  1.00 42.23 ? 934  LEU   A O     1 
ATOM   6845  C  CB    . LEU   A  1  936  ? -10.250 84.532  84.281  1.00 40.67 ? 934  LEU   A CB    1 
ATOM   6846  C  CG    . LEU   A  1  936  ? -11.153 83.625  85.125  1.00 44.85 ? 934  LEU   A CG    1 
ATOM   6847  C  CD1   . LEU   A  1  936  ? -10.627 82.199  85.116  1.00 38.28 ? 934  LEU   A CD1   1 
ATOM   6848  C  CD2   . LEU   A  1  936  ? -11.286 84.133  86.556  1.00 41.15 ? 934  LEU   A CD2   1 
ATOM   6849  N  N     . SER   A  1  937  ? -9.255  87.728  84.295  1.00 46.40 ? 935  SER   A N     1 
ATOM   6850  C  CA    . SER   A  1  937  ? -8.690  88.835  85.055  1.00 45.09 ? 935  SER   A CA    1 
ATOM   6851  C  C     . SER   A  1  937  ? -9.645  90.017  85.189  1.00 41.24 ? 935  SER   A C     1 
ATOM   6852  O  O     . SER   A  1  937  ? -9.356  90.935  85.964  1.00 44.90 ? 935  SER   A O     1 
ATOM   6853  C  CB    . SER   A  1  937  ? -7.366  89.279  84.427  1.00 46.80 ? 935  SER   A CB    1 
ATOM   6854  O  OG    . SER   A  1  937  ? -7.527  89.547  83.045  1.00 47.55 ? 935  SER   A OG    1 
ATOM   6855  N  N     . ASP   A  1  938  ? -10.766 90.023  84.460  1.00 43.10 ? 936  ASP   A N     1 
ATOM   6856  C  CA    . ASP   A  1  938  ? -11.774 91.062  84.649  1.00 40.47 ? 936  ASP   A CA    1 
ATOM   6857  C  C     . ASP   A  1  938  ? -12.369 91.040  86.050  1.00 44.72 ? 936  ASP   A C     1 
ATOM   6858  O  O     . ASP   A  1  938  ? -12.949 92.043  86.480  1.00 41.11 ? 936  ASP   A O     1 
ATOM   6859  C  CB    . ASP   A  1  938  ? -12.906 90.905  83.631  1.00 46.36 ? 936  ASP   A CB    1 
ATOM   6860  C  CG    . ASP   A  1  938  ? -12.435 91.068  82.204  1.00 47.27 ? 936  ASP   A CG    1 
ATOM   6861  O  OD1   . ASP   A  1  938  ? -11.244 91.392  82.003  1.00 48.64 ? 936  ASP   A OD1   1 
ATOM   6862  O  OD2   . ASP   A  1  938  ? -13.258 90.864  81.286  1.00 46.22 ? 936  ASP   A OD2   1 
ATOM   6863  N  N     . LEU   A  1  939  ? -12.258 89.922  86.761  1.00 39.78 ? 937  LEU   A N     1 
ATOM   6864  C  CA    . LEU   A  1  939  ? -12.740 89.833  88.130  1.00 39.68 ? 937  LEU   A CA    1 
ATOM   6865  C  C     . LEU   A  1  939  ? -11.626 90.174  89.106  1.00 45.18 ? 937  LEU   A C     1 
ATOM   6866  O  O     . LEU   A  1  939  ? -10.466 89.801  88.904  1.00 44.85 ? 937  LEU   A O     1 
ATOM   6867  C  CB    . LEU   A  1  939  ? -13.256 88.428  88.427  1.00 39.74 ? 937  LEU   A CB    1 
ATOM   6868  C  CG    . LEU   A  1  939  ? -14.511 88.012  87.670  1.00 38.59 ? 937  LEU   A CG    1 
ATOM   6869  C  CD1   . LEU   A  1  939  ? -15.110 86.789  88.324  1.00 35.94 ? 937  LEU   A CD1   1 
ATOM   6870  C  CD2   . LEU   A  1  939  ? -15.516 89.152  87.635  1.00 38.12 ? 937  LEU   A CD2   1 
ATOM   6871  N  N     . GLN   A  1  940  ? -11.989 90.882  90.174  1.00 40.18 ? 938  GLN   A N     1 
ATOM   6872  C  CA    . GLN   A  1  940  ? -11.041 91.276  91.210  1.00 40.13 ? 938  GLN   A CA    1 
ATOM   6873  C  C     . GLN   A  1  940  ? -11.222 90.455  92.482  1.00 44.70 ? 938  GLN   A C     1 
ATOM   6874  O  O     . GLN   A  1  940  ? -10.315 89.719  92.884  1.00 52.52 ? 938  GLN   A O     1 
ATOM   6875  C  CB    . GLN   A  1  940  ? -11.176 92.775  91.506  1.00 42.38 ? 938  GLN   A CB    1 
ATOM   6876  N  N     . ARG   A  1  941  ? -12.382 90.566  93.126  1.00 39.20 ? 939  ARG   A N     1 
ATOM   6877  C  CA    . ARG   A  1  941  ? -12.670 89.841  94.354  1.00 34.33 ? 939  ARG   A CA    1 
ATOM   6878  C  C     . ARG   A  1  941  ? -14.004 89.119  94.217  1.00 28.50 ? 939  ARG   A C     1 
ATOM   6879  O  O     . ARG   A  1  941  ? -14.763 89.331  93.268  1.00 31.33 ? 939  ARG   A O     1 
ATOM   6880  C  CB    . ARG   A  1  941  ? -12.689 90.774  95.574  1.00 37.27 ? 939  ARG   A CB    1 
ATOM   6881  N  N     . GLU   A  1  942  ? -14.262 88.234  95.178  1.00 28.19 ? 940  GLU   A N     1 
ATOM   6882  C  CA    . GLU   A  1  942  ? -15.528 87.519  95.245  1.00 24.76 ? 940  GLU   A CA    1 
ATOM   6883  C  C     . GLU   A  1  942  ? -16.682 88.510  95.272  1.00 22.66 ? 940  GLU   A C     1 
ATOM   6884  O  O     . GLU   A  1  942  ? -16.669 89.474  96.042  1.00 25.86 ? 940  GLU   A O     1 
ATOM   6885  C  CB    . GLU   A  1  942  ? -15.539 86.683  96.522  1.00 23.20 ? 940  GLU   A CB    1 
ATOM   6886  C  CG    . GLU   A  1  942  ? -16.841 85.959  96.814  1.00 21.36 ? 940  GLU   A CG    1 
ATOM   6887  C  CD    . GLU   A  1  942  ? -16.840 85.363  98.203  1.00 22.34 ? 940  GLU   A CD    1 
ATOM   6888  O  OE1   . GLU   A  1  942  ? -16.631 86.133  99.164  1.00 26.06 ? 940  GLU   A OE1   1 
ATOM   6889  O  OE2   . GLU   A  1  942  ? -17.021 84.138  98.343  1.00 21.57 ? 940  GLU   A OE2   1 
ATOM   6890  N  N     . VAL   A  1  943  ? -17.674 88.286  94.413  1.00 21.61 ? 941  VAL   A N     1 
ATOM   6891  C  CA    . VAL   A  1  943  ? -18.921 89.045  94.426  1.00 20.37 ? 941  VAL   A CA    1 
ATOM   6892  C  C     . VAL   A  1  943  ? -19.998 88.097  94.931  1.00 24.60 ? 941  VAL   A C     1 
ATOM   6893  O  O     . VAL   A  1  943  ? -20.418 87.179  94.217  1.00 20.49 ? 941  VAL   A O     1 
ATOM   6894  C  CB    . VAL   A  1  943  ? -19.261 89.622  93.045  1.00 25.27 ? 941  VAL   A CB    1 
ATOM   6895  C  CG1   . VAL   A  1  943  ? -20.606 90.342  93.074  1.00 24.95 ? 941  VAL   A CG1   1 
ATOM   6896  C  CG2   . VAL   A  1  943  ? -18.156 90.571  92.604  1.00 29.53 ? 941  VAL   A CG2   1 
ATOM   6897  N  N     . PHE   A  1  944  ? -20.420 88.302  96.176  1.00 23.29 ? 942  PHE   A N     1 
ATOM   6898  C  CA    . PHE   A  1  944  ? -21.230 87.320  96.893  1.00 20.62 ? 942  PHE   A CA    1 
ATOM   6899  C  C     . PHE   A  1  944  ? -22.693 87.616  96.599  1.00 21.58 ? 942  PHE   A C     1 
ATOM   6900  O  O     . PHE   A  1  944  ? -23.425 88.201  97.401  1.00 23.01 ? 942  PHE   A O     1 
ATOM   6901  C  CB    . PHE   A  1  944  ? -20.925 87.386  98.383  1.00 20.21 ? 942  PHE   A CB    1 
ATOM   6902  C  CG    . PHE   A  1  944  ? -21.317 86.154  99.139  1.00 19.80 ? 942  PHE   A CG    1 
ATOM   6903  C  CD1   . PHE   A  1  944  ? -20.637 84.967  98.945  1.00 18.25 ? 942  PHE   A CD1   1 
ATOM   6904  C  CD2   . PHE   A  1  944  ? -22.335 86.189  100.074 1.00 19.10 ? 942  PHE   A CD2   1 
ATOM   6905  C  CE1   . PHE   A  1  944  ? -20.989 83.835  99.657  1.00 17.86 ? 942  PHE   A CE1   1 
ATOM   6906  C  CE2   . PHE   A  1  944  ? -22.680 85.051  100.789 1.00 18.32 ? 942  PHE   A CE2   1 
ATOM   6907  C  CZ    . PHE   A  1  944  ? -22.016 83.875  100.569 1.00 18.41 ? 942  PHE   A CZ    1 
ATOM   6908  N  N     . GLY   A  1  945  ? -23.120 87.215  95.409  1.00 20.36 ? 943  GLY   A N     1 
ATOM   6909  C  CA    . GLY   A  1  945  ? -24.458 87.501  94.956  1.00 20.06 ? 943  GLY   A CA    1 
ATOM   6910  C  C     . GLY   A  1  945  ? -24.771 86.699  93.716  1.00 19.56 ? 943  GLY   A C     1 
ATOM   6911  O  O     . GLY   A  1  945  ? -23.982 85.853  93.286  1.00 19.71 ? 943  GLY   A O     1 
ATOM   6912  N  N     . PRO   A  1  946  ? -25.942 86.937  93.120  1.00 18.42 ? 944  PRO   A N     1 
ATOM   6913  C  CA    . PRO   A  1  946  ? -26.400 86.090  92.006  1.00 18.89 ? 944  PRO   A CA    1 
ATOM   6914  C  C     . PRO   A  1  946  ? -25.846 86.572  90.670  1.00 18.05 ? 944  PRO   A C     1 
ATOM   6915  O  O     . PRO   A  1  946  ? -26.582 86.986  89.771  1.00 19.41 ? 944  PRO   A O     1 
ATOM   6916  C  CB    . PRO   A  1  946  ? -27.921 86.237  92.095  1.00 17.04 ? 944  PRO   A CB    1 
ATOM   6917  C  CG    . PRO   A  1  946  ? -28.101 87.667  92.565  1.00 21.05 ? 944  PRO   A CG    1 
ATOM   6918  C  CD    . PRO   A  1  946  ? -26.964 87.915  93.538  1.00 19.41 ? 944  PRO   A CD    1 
ATOM   6919  N  N     . VAL   A  1  947  ? -24.527 86.511  90.537  1.00 18.13 ? 945  VAL   A N     1 
ATOM   6920  C  CA    . VAL   A  1  947  ? -23.834 87.071  89.389  1.00 19.81 ? 945  VAL   A CA    1 
ATOM   6921  C  C     . VAL   A  1  947  ? -22.897 86.017  88.828  1.00 19.49 ? 945  VAL   A C     1 
ATOM   6922  O  O     . VAL   A  1  947  ? -21.850 85.724  89.419  1.00 20.14 ? 945  VAL   A O     1 
ATOM   6923  C  CB    . VAL   A  1  947  ? -23.075 88.359  89.729  1.00 21.33 ? 945  VAL   A CB    1 
ATOM   6924  C  CG1   . VAL   A  1  947  ? -22.510 88.959  88.464  1.00 21.36 ? 945  VAL   A CG1   1 
ATOM   6925  C  CG2   . VAL   A  1  947  ? -24.015 89.349  90.407  1.00 21.07 ? 945  VAL   A CG2   1 
ATOM   6926  N  N     . LEU   A  1  948  ? -23.264 85.463  87.684  1.00 17.87 ? 946  LEU   A N     1 
ATOM   6927  C  CA    . LEU   A  1  948  ? -22.460 84.478  86.992  1.00 17.88 ? 946  LEU   A CA    1 
ATOM   6928  C  C     . LEU   A  1  948  ? -21.681 85.187  85.900  1.00 18.24 ? 946  LEU   A C     1 
ATOM   6929  O  O     . LEU   A  1  948  ? -22.254 85.948  85.116  1.00 20.81 ? 946  LEU   A O     1 
ATOM   6930  C  CB    . LEU   A  1  948  ? -23.375 83.437  86.361  1.00 18.31 ? 946  LEU   A CB    1 
ATOM   6931  C  CG    . LEU   A  1  948  ? -22.610 82.405  85.543  1.00 17.34 ? 946  LEU   A CG    1 
ATOM   6932  C  CD1   . LEU   A  1  948  ? -21.662 81.617  86.426  1.00 20.14 ? 946  LEU   A CD1   1 
ATOM   6933  C  CD2   . LEU   A  1  948  ? -23.602 81.502  84.849  1.00 20.14 ? 946  LEU   A CD2   1 
ATOM   6934  N  N     . HIS   A  1  949  ? -20.384 84.942  85.849  1.00 19.33 ? 947  HIS   A N     1 
ATOM   6935  C  CA    . HIS   A  1  949  ? -19.557 85.464  84.779  1.00 19.02 ? 947  HIS   A CA    1 
ATOM   6936  C  C     . HIS   A  1  949  ? -19.236 84.323  83.835  1.00 19.16 ? 947  HIS   A C     1 
ATOM   6937  O  O     . HIS   A  1  949  ? -19.091 83.178  84.263  1.00 18.86 ? 947  HIS   A O     1 
ATOM   6938  C  CB    . HIS   A  1  949  ? -18.282 86.080  85.335  1.00 19.19 ? 947  HIS   A CB    1 
ATOM   6939  C  CG    . HIS   A  1  949  ? -18.540 87.095  86.399  1.00 20.42 ? 947  HIS   A CG    1 
ATOM   6940  N  ND1   . HIS   A  1  949  ? -18.728 86.753  87.721  1.00 21.68 ? 947  HIS   A ND1   1 
ATOM   6941  C  CD2   . HIS   A  1  949  ? -18.697 88.437  86.327  1.00 22.85 ? 947  HIS   A CD2   1 
ATOM   6942  C  CE1   . HIS   A  1  949  ? -18.960 87.848  88.423  1.00 25.57 ? 947  HIS   A CE1   1 
ATOM   6943  N  NE2   . HIS   A  1  949  ? -18.945 88.882  87.601  1.00 23.74 ? 947  HIS   A NE2   1 
ATOM   6944  N  N     . VAL   A  1  950  ? -19.180 84.631  82.543  1.00 18.94 ? 948  VAL   A N     1 
ATOM   6945  C  CA    . VAL   A  1  950  ? -18.997 83.620  81.511  1.00 20.15 ? 948  VAL   A CA    1 
ATOM   6946  C  C     . VAL   A  1  950  ? -17.796 84.005  80.673  1.00 22.83 ? 948  VAL   A C     1 
ATOM   6947  O  O     . VAL   A  1  950  ? -17.712 85.135  80.176  1.00 23.70 ? 948  VAL   A O     1 
ATOM   6948  C  CB    . VAL   A  1  950  ? -20.251 83.456  80.632  1.00 18.48 ? 948  VAL   A CB    1 
ATOM   6949  C  CG1   . VAL   A  1  950  ? -19.983 82.438  79.506  1.00 19.82 ? 948  VAL   A CG1   1 
ATOM   6950  C  CG2   . VAL   A  1  950  ? -21.435 83.021  81.478  1.00 19.76 ? 948  VAL   A CG2   1 
ATOM   6951  N  N     . ILE   A  1  951  ? -16.856 83.076  80.534  1.00 19.15 ? 949  ILE   A N     1 
ATOM   6952  C  CA    . ILE   A  1  951  ? -15.727 83.273  79.642  1.00 22.51 ? 949  ILE   A CA    1 
ATOM   6953  C  C     . ILE   A  1  951  ? -15.664 82.097  78.683  1.00 22.43 ? 949  ILE   A C     1 
ATOM   6954  O  O     . ILE   A  1  951  ? -16.173 81.008  78.954  1.00 20.27 ? 949  ILE   A O     1 
ATOM   6955  C  CB    . ILE   A  1  951  ? -14.395 83.464  80.379  1.00 23.55 ? 949  ILE   A CB    1 
ATOM   6956  C  CG1   . ILE   A  1  951  ? -14.069 82.239  81.211  1.00 24.99 ? 949  ILE   A CG1   1 
ATOM   6957  C  CG2   . ILE   A  1  951  ? -14.447 84.702  81.266  1.00 29.00 ? 949  ILE   A CG2   1 
ATOM   6958  C  CD1   . ILE   A  1  951  ? -12.786 82.392  81.987  1.00 35.05 ? 949  ILE   A CD1   1 
ATOM   6959  N  N     . ARG   A  1  952  ? -15.047 82.341  77.538  1.00 20.33 ? 950  ARG   A N     1 
ATOM   6960  C  CA    . ARG   A  1  952  ? -14.924 81.342  76.494  1.00 19.96 ? 950  ARG   A CA    1 
ATOM   6961  C  C     . ARG   A  1  952  ? -13.454 80.992  76.336  1.00 19.52 ? 950  ARG   A C     1 
ATOM   6962  O  O     . ARG   A  1  952  ? -12.574 81.830  76.549  1.00 22.32 ? 950  ARG   A O     1 
ATOM   6963  C  CB    . ARG   A  1  952  ? -15.463 81.892  75.177  1.00 22.67 ? 950  ARG   A CB    1 
ATOM   6964  C  CG    . ARG   A  1  952  ? -16.832 82.528  75.321  1.00 25.66 ? 950  ARG   A CG    1 
ATOM   6965  C  CD    . ARG   A  1  952  ? -17.111 83.464  74.167  1.00 27.95 ? 950  ARG   A CD    1 
ATOM   6966  N  NE    . ARG   A  1  952  ? -17.460 82.739  72.953  1.00 27.75 ? 950  ARG   A NE    1 
ATOM   6967  C  CZ    . ARG   A  1  952  ? -18.695 82.605  72.488  1.00 27.96 ? 950  ARG   A CZ    1 
ATOM   6968  N  NH1   . ARG   A  1  952  ? -19.734 83.130  73.120  1.00 29.88 ? 950  ARG   A NH1   1 
ATOM   6969  N  NH2   . ARG   A  1  952  ? -18.895 81.919  71.367  1.00 27.93 ? 950  ARG   A NH2   1 
ATOM   6970  N  N     . TYR   A  1  953  ? -13.193 79.744  75.971  1.00 18.36 ? 951  TYR   A N     1 
ATOM   6971  C  CA    . TYR   A  1  953  ? -11.815 79.329  75.775  1.00 19.14 ? 951  TYR   A CA    1 
ATOM   6972  C  C     . TYR   A  1  953  ? -11.726 78.383  74.588  1.00 17.78 ? 951  TYR   A C     1 
ATOM   6973  O  O     . TYR   A  1  953  ? -12.654 77.620  74.302  1.00 20.41 ? 951  TYR   A O     1 
ATOM   6974  C  CB    . TYR   A  1  953  ? -11.228 78.684  77.047  1.00 18.71 ? 951  TYR   A CB    1 
ATOM   6975  C  CG    . TYR   A  1  953  ? -11.776 77.311  77.328  1.00 18.09 ? 951  TYR   A CG    1 
ATOM   6976  C  CD1   . TYR   A  1  953  ? -12.998 77.136  77.980  1.00 17.20 ? 951  TYR   A CD1   1 
ATOM   6977  C  CD2   . TYR   A  1  953  ? -11.080 76.180  76.917  1.00 19.42 ? 951  TYR   A CD2   1 
ATOM   6978  C  CE1   . TYR   A  1  953  ? -13.493 75.881  78.224  1.00 17.99 ? 951  TYR   A CE1   1 
ATOM   6979  C  CE2   . TYR   A  1  953  ? -11.564 74.927  77.156  1.00 16.49 ? 951  TYR   A CE2   1 
ATOM   6980  C  CZ    . TYR   A  1  953  ? -12.777 74.780  77.809  1.00 18.42 ? 951  TYR   A CZ    1 
ATOM   6981  O  OH    . TYR   A  1  953  ? -13.277 73.532  78.039  1.00 18.24 ? 951  TYR   A OH    1 
ATOM   6982  N  N     . ARG   A  1  954  ? -10.591 78.460  73.894  1.00 22.38 ? 952  ARG   A N     1 
ATOM   6983  C  CA    . ARG   A  1  954  ? -10.266 77.508  72.844  1.00 21.92 ? 952  ARG   A CA    1 
ATOM   6984  C  C     . ARG   A  1  954  ? -9.686  76.254  73.481  1.00 20.57 ? 952  ARG   A C     1 
ATOM   6985  O  O     . ARG   A  1  954  ? -8.947  76.331  74.465  1.00 20.85 ? 952  ARG   A O     1 
ATOM   6986  C  CB    . ARG   A  1  954  ? -9.241  78.117  71.886  1.00 24.89 ? 952  ARG   A CB    1 
ATOM   6987  N  N     . ARG   A  1  955  ? -10.032 75.094  72.914  1.00 22.10 ? 953  ARG   A N     1 
ATOM   6988  C  CA    . ARG   A  1  955  ? -9.652  73.820  73.524  1.00 20.46 ? 953  ARG   A CA    1 
ATOM   6989  C  C     . ARG   A  1  955  ? -8.154  73.739  73.799  1.00 19.93 ? 953  ARG   A C     1 
ATOM   6990  O  O     . ARG   A  1  955  ? -7.735  73.257  74.858  1.00 22.35 ? 953  ARG   A O     1 
ATOM   6991  C  CB    . ARG   A  1  955  ? -10.103 72.649  72.647  1.00 27.47 ? 953  ARG   A CB    1 
ATOM   6992  C  CG    . ARG   A  1  955  ? -9.595  71.278  73.113  1.00 35.41 ? 953  ARG   A CG    1 
ATOM   6993  C  CD    . ARG   A  1  955  ? -9.947  71.051  74.571  1.00 38.78 ? 953  ARG   A CD    1 
ATOM   6994  N  NE    . ARG   A  1  955  ? -9.520  69.769  75.125  1.00 46.57 ? 953  ARG   A NE    1 
ATOM   6995  C  CZ    . ARG   A  1  955  ? -8.387  69.572  75.789  1.00 40.32 ? 953  ARG   A CZ    1 
ATOM   6996  N  NH1   . ARG   A  1  955  ? -7.488  70.535  75.927  1.00 30.30 ? 953  ARG   A NH1   1 
ATOM   6997  N  NH2   . ARG   A  1  955  ? -8.152  68.380  76.332  1.00 40.01 ? 953  ARG   A NH2   1 
ATOM   6998  N  N     . ASP   A  1  956  ? -7.326  74.204  72.865  1.00 21.16 ? 954  ASP   A N     1 
ATOM   6999  C  CA    . ASP   A  1  956  ? -5.888  74.101  73.078  1.00 21.00 ? 954  ASP   A CA    1 
ATOM   7000  C  C     . ASP   A  1  956  ? -5.417  74.949  74.246  1.00 23.22 ? 954  ASP   A C     1 
ATOM   7001  O  O     . ASP   A  1  956  ? -4.313  74.720  74.754  1.00 23.06 ? 954  ASP   A O     1 
ATOM   7002  C  CB    . ASP   A  1  956  ? -5.119  74.491  71.819  1.00 23.75 ? 954  ASP   A CB    1 
ATOM   7003  C  CG    . ASP   A  1  956  ? -5.286  73.485  70.702  1.00 26.49 ? 954  ASP   A CG    1 
ATOM   7004  O  OD1   . ASP   A  1  956  ? -5.669  72.334  70.995  1.00 30.48 ? 954  ASP   A OD1   1 
ATOM   7005  O  OD2   . ASP   A  1  956  ? -5.034  73.849  69.533  1.00 34.92 ? 954  ASP   A OD2   1 
ATOM   7006  N  N     . ASP   A  1  957  ? -6.212  75.924  74.672  1.00 20.74 ? 955  ASP   A N     1 
ATOM   7007  C  CA    . ASP   A  1  957  ? -5.848  76.805  75.769  1.00 21.88 ? 955  ASP   A CA    1 
ATOM   7008  C  C     . ASP   A  1  957  ? -6.404  76.337  77.106  1.00 20.71 ? 955  ASP   A C     1 
ATOM   7009  O  O     . ASP   A  1  957  ? -6.391  77.107  78.067  1.00 21.32 ? 955  ASP   A O     1 
ATOM   7010  C  CB    . ASP   A  1  957  ? -6.326  78.233  75.486  1.00 24.09 ? 955  ASP   A CB    1 
ATOM   7011  C  CG    . ASP   A  1  957  ? -5.670  78.836  74.263  1.00 30.80 ? 955  ASP   A CG    1 
ATOM   7012  O  OD1   . ASP   A  1  957  ? -4.514  78.468  73.960  1.00 28.25 ? 955  ASP   A OD1   1 
ATOM   7013  O  OD2   . ASP   A  1  957  ? -6.311  79.678  73.606  1.00 32.21 ? 955  ASP   A OD2   1 
ATOM   7014  N  N     . LEU   A  1  958  ? -6.894  75.098  77.185  1.00 18.73 ? 956  LEU   A N     1 
ATOM   7015  C  CA    . LEU   A  1  958  ? -7.454  74.594  78.434  1.00 18.56 ? 956  LEU   A CA    1 
ATOM   7016  C  C     . LEU   A  1  958  ? -6.455  74.697  79.578  1.00 18.53 ? 956  LEU   A C     1 
ATOM   7017  O  O     . LEU   A  1  958  ? -6.807  75.121  80.685  1.00 17.63 ? 956  LEU   A O     1 
ATOM   7018  C  CB    . LEU   A  1  958  ? -7.884  73.144  78.249  1.00 18.71 ? 956  LEU   A CB    1 
ATOM   7019  C  CG    . LEU   A  1  958  ? -8.399  72.471  79.519  1.00 17.75 ? 956  LEU   A CG    1 
ATOM   7020  C  CD1   . LEU   A  1  958  ? -9.596  73.214  80.111  1.00 19.61 ? 956  LEU   A CD1   1 
ATOM   7021  C  CD2   . LEU   A  1  958  ? -8.740  71.014  79.245  1.00 21.36 ? 956  LEU   A CD2   1 
ATOM   7022  N  N     . ASP   A  1  959  ? -5.194  74.333  79.335  1.00 16.56 ? 957  ASP   A N     1 
ATOM   7023  C  CA    . ASP   A  1  959  ? -4.237  74.355  80.428  1.00 16.89 ? 957  ASP   A CA    1 
ATOM   7024  C  C     . ASP   A  1  959  ? -3.971  75.781  80.887  1.00 17.68 ? 957  ASP   A C     1 
ATOM   7025  O  O     . ASP   A  1  959  ? -3.837  76.038  82.089  1.00 18.08 ? 957  ASP   A O     1 
ATOM   7026  C  CB    . ASP   A  1  959  ? -2.934  73.681  80.010  1.00 20.46 ? 957  ASP   A CB    1 
ATOM   7027  C  CG    . ASP   A  1  959  ? -2.040  73.407  81.187  1.00 21.96 ? 957  ASP   A CG    1 
ATOM   7028  O  OD1   . ASP   A  1  959  ? -2.489  72.718  82.123  1.00 21.29 ? 957  ASP   A OD1   1 
ATOM   7029  O  OD2   . ASP   A  1  959  ? -0.896  73.895  81.196  1.00 27.51 ? 957  ASP   A OD2   1 
ATOM   7030  N  N     . ARG   A  1  960  ? -3.879  76.718  79.942  1.00 17.86 ? 958  ARG   A N     1 
ATOM   7031  C  CA    . ARG   A  1  960  ? -3.750  78.124  80.311  1.00 21.18 ? 958  ARG   A CA    1 
ATOM   7032  C  C     . ARG   A  1  960  ? -4.962  78.577  81.112  1.00 20.94 ? 958  ARG   A C     1 
ATOM   7033  O  O     . ARG   A  1  960  ? -4.831  79.339  82.079  1.00 22.05 ? 958  ARG   A O     1 
ATOM   7034  C  CB    . ARG   A  1  960  ? -3.571  78.974  79.050  1.00 21.77 ? 958  ARG   A CB    1 
ATOM   7035  C  CG    . ARG   A  1  960  ? -3.302  80.459  79.296  1.00 25.51 ? 958  ARG   A CG    1 
ATOM   7036  C  CD    . ARG   A  1  960  ? -4.590  81.280  79.358  1.00 38.27 ? 958  ARG   A CD    1 
ATOM   7037  N  NE    . ARG   A  1  960  ? -5.434  81.104  78.180  1.00 38.77 ? 958  ARG   A NE    1 
ATOM   7038  C  CZ    . ARG   A  1  960  ? -6.759  81.184  78.190  1.00 39.29 ? 958  ARG   A CZ    1 
ATOM   7039  N  NH1   . ARG   A  1  960  ? -7.430  81.413  79.307  1.00 41.78 ? 958  ARG   A NH1   1 
ATOM   7040  N  NH2   . ARG   A  1  960  ? -7.427  81.027  77.050  1.00 47.11 ? 958  ARG   A NH2   1 
ATOM   7041  N  N     . LEU   A  1  961  ? -6.149  78.118  80.723  1.00 19.04 ? 959  LEU   A N     1 
ATOM   7042  C  CA    . LEU   A  1  961  ? -7.355  78.487  81.452  1.00 19.29 ? 959  LEU   A CA    1 
ATOM   7043  C  C     . LEU   A  1  961  ? -7.288  78.007  82.893  1.00 20.61 ? 959  LEU   A C     1 
ATOM   7044  O  O     . LEU   A  1  961  ? -7.626  78.754  83.817  1.00 20.06 ? 959  LEU   A O     1 
ATOM   7045  C  CB    . LEU   A  1  961  ? -8.574  77.902  80.756  1.00 17.89 ? 959  LEU   A CB    1 
ATOM   7046  C  CG    . LEU   A  1  961  ? -9.876  78.031  81.542  1.00 18.63 ? 959  LEU   A CG    1 
ATOM   7047  C  CD1   . LEU   A  1  961  ? -10.263 79.497  81.693  1.00 24.16 ? 959  LEU   A CD1   1 
ATOM   7048  C  CD2   . LEU   A  1  961  ? -10.963 77.223  80.859  1.00 21.66 ? 959  LEU   A CD2   1 
ATOM   7049  N  N     . VAL   A  1  962  ? -6.857  76.762  83.112  1.00 17.65 ? 960  VAL   A N     1 
ATOM   7050  C  CA    . VAL   A  1  962  ? -6.708  76.278  84.480  1.00 16.95 ? 960  VAL   A CA    1 
ATOM   7051  C  C     . VAL   A  1  962  ? -5.720  77.142  85.250  1.00 21.26 ? 960  VAL   A C     1 
ATOM   7052  O  O     . VAL   A  1  962  ? -5.932  77.441  86.431  1.00 19.66 ? 960  VAL   A O     1 
ATOM   7053  C  CB    . VAL   A  1  962  ? -6.328  74.787  84.499  1.00 20.31 ? 960  VAL   A CB    1 
ATOM   7054  C  CG1   . VAL   A  1  962  ? -6.029  74.338  85.931  1.00 22.41 ? 960  VAL   A CG1   1 
ATOM   7055  C  CG2   . VAL   A  1  962  ? -7.455  73.952  83.900  1.00 19.41 ? 960  VAL   A CG2   1 
ATOM   7056  N  N     . ASP   A  1  963  ? -4.631  77.565  84.597  1.00 20.09 ? 961  ASP   A N     1 
ATOM   7057  C  CA    . ASP   A  1  963  ? -3.717  78.521  85.218  1.00 21.46 ? 961  ASP   A CA    1 
ATOM   7058  C  C     . ASP   A  1  963  ? -4.450  79.799  85.603  1.00 22.18 ? 961  ASP   A C     1 
ATOM   7059  O  O     . ASP   A  1  963  ? -4.262  80.328  86.705  1.00 25.17 ? 961  ASP   A O     1 
ATOM   7060  C  CB    . ASP   A  1  963  ? -2.580  78.880  84.260  1.00 23.79 ? 961  ASP   A CB    1 
ATOM   7061  C  CG    . ASP   A  1  963  ? -1.592  77.759  84.053  1.00 29.57 ? 961  ASP   A CG    1 
ATOM   7062  O  OD1   . ASP   A  1  963  ? -1.501  76.852  84.905  1.00 33.67 ? 961  ASP   A OD1   1 
ATOM   7063  O  OD2   . ASP   A  1  963  ? -0.889  77.805  83.018  1.00 36.94 ? 961  ASP   A OD2   1 
ATOM   7064  N  N     . ASP   A  1  964  ? -5.279  80.318  84.691  1.00 21.35 ? 962  ASP   A N     1 
ATOM   7065  C  CA    . ASP   A  1  964  ? -6.023  81.543  84.969  1.00 24.22 ? 962  ASP   A CA    1 
ATOM   7066  C  C     . ASP   A  1  964  ? -6.946  81.372  86.168  1.00 27.09 ? 962  ASP   A C     1 
ATOM   7067  O  O     . ASP   A  1  964  ? -7.077  82.282  86.997  1.00 26.90 ? 962  ASP   A O     1 
ATOM   7068  C  CB    . ASP   A  1  964  ? -6.835  81.958  83.742  1.00 25.64 ? 962  ASP   A CB    1 
ATOM   7069  C  CG    . ASP   A  1  964  ? -5.961  82.443  82.604  1.00 29.87 ? 962  ASP   A CG    1 
ATOM   7070  O  OD1   . ASP   A  1  964  ? -4.755  82.675  82.837  1.00 33.99 ? 962  ASP   A OD1   1 
ATOM   7071  O  OD2   . ASP   A  1  964  ? -6.488  82.578  81.479  1.00 38.23 ? 962  ASP   A OD2   1 
ATOM   7072  N  N     . VAL   A  1  965  ? -7.612  80.223  86.268  1.00 22.45 ? 963  VAL   A N     1 
ATOM   7073  C  CA    . VAL   A  1  965  ? -8.473  79.975  87.420  1.00 21.25 ? 963  VAL   A CA    1 
ATOM   7074  C  C     . VAL   A  1  965  ? -7.644  79.962  88.694  1.00 24.50 ? 963  VAL   A C     1 
ATOM   7075  O  O     . VAL   A  1  965  ? -7.995  80.604  89.691  1.00 25.10 ? 963  VAL   A O     1 
ATOM   7076  C  CB    . VAL   A  1  965  ? -9.252  78.662  87.236  1.00 18.53 ? 963  VAL   A CB    1 
ATOM   7077  C  CG1   . VAL   A  1  965  ? -9.991  78.299  88.508  1.00 19.76 ? 963  VAL   A CG1   1 
ATOM   7078  C  CG2   . VAL   A  1  965  ? -10.216 78.767  86.066  1.00 20.21 ? 963  VAL   A CG2   1 
ATOM   7079  N  N     . ASN   A  1  966  ? -6.522  79.240  88.674  1.00 20.65 ? 964  ASN   A N     1 
ATOM   7080  C  CA    . ASN   A  1  966  ? -5.641  79.200  89.837  1.00 21.55 ? 964  ASN   A CA    1 
ATOM   7081  C  C     . ASN   A  1  966  ? -5.102  80.581  90.173  1.00 26.25 ? 964  ASN   A C     1 
ATOM   7082  O  O     . ASN   A  1  966  ? -4.875  80.890  91.349  1.00 23.28 ? 964  ASN   A O     1 
ATOM   7083  C  CB    . ASN   A  1  966  ? -4.475  78.234  89.595  1.00 21.40 ? 964  ASN   A CB    1 
ATOM   7084  C  CG    . ASN   A  1  966  ? -4.909  76.774  89.597  1.00 21.72 ? 964  ASN   A CG    1 
ATOM   7085  O  OD1   . ASN   A  1  966  ? -5.951  76.431  90.150  1.00 19.99 ? 964  ASN   A OD1   1 
ATOM   7086  N  ND2   . ASN   A  1  966  ? -4.100  75.908  88.987  1.00 19.97 ? 964  ASN   A ND2   1 
ATOM   7087  N  N     . ALA   A  1  967  ? -4.921  81.429  89.157  1.00 23.98 ? 965  ALA   A N     1 
ATOM   7088  C  CA    . ALA   A  1  967  ? -4.242  82.708  89.333  1.00 27.16 ? 965  ALA   A CA    1 
ATOM   7089  C  C     . ALA   A  1  967  ? -5.034  83.699  90.172  1.00 25.14 ? 965  ALA   A C     1 
ATOM   7090  O  O     . ALA   A  1  967  ? -4.460  84.697  90.620  1.00 30.16 ? 965  ALA   A O     1 
ATOM   7091  C  CB    . ALA   A  1  967  ? -3.919  83.327  87.972  1.00 29.88 ? 965  ALA   A CB    1 
ATOM   7092  N  N     . THR   A  1  968  ? -6.328  83.467  90.394  1.00 22.53 ? 966  THR   A N     1 
ATOM   7093  C  CA    . THR   A  1  968  ? -7.065  84.361  91.281  1.00 21.81 ? 966  THR   A CA    1 
ATOM   7094  C  C     . THR   A  1  968  ? -6.550  84.289  92.707  1.00 22.10 ? 966  THR   A C     1 
ATOM   7095  O  O     . THR   A  1  968  ? -6.781  85.223  93.483  1.00 24.42 ? 966  THR   A O     1 
ATOM   7096  C  CB    . THR   A  1  968  ? -8.553  84.016  91.306  1.00 23.77 ? 966  THR   A CB    1 
ATOM   7097  O  OG1   . THR   A  1  968  ? -8.738  82.774  92.004  1.00 21.92 ? 966  THR   A OG1   1 
ATOM   7098  C  CG2   . THR   A  1  968  ? -9.117  83.911  89.890  1.00 21.61 ? 966  THR   A CG2   1 
ATOM   7099  N  N     . GLY   A  1  969  ? -5.889  83.198  93.076  1.00 21.53 ? 967  GLY   A N     1 
ATOM   7100  C  CA    . GLY   A  1  969  ? -5.479  82.977  94.444  1.00 22.39 ? 967  GLY   A CA    1 
ATOM   7101  C  C     . GLY   A  1  969  ? -6.510  82.280  95.298  1.00 20.68 ? 967  GLY   A C     1 
ATOM   7102  O  O     . GLY   A  1  969  ? -6.174  81.819  96.398  1.00 18.93 ? 967  GLY   A O     1 
ATOM   7103  N  N     . TYR   A  1  970  ? -7.752  82.192  94.831  1.00 18.84 ? 968  TYR   A N     1 
ATOM   7104  C  CA    . TYR   A  1  970  ? -8.769  81.432  95.527  1.00 17.66 ? 968  TYR   A CA    1 
ATOM   7105  C  C     . TYR   A  1  970  ? -8.612  79.950  95.211  1.00 16.76 ? 968  TYR   A C     1 
ATOM   7106  O  O     . TYR   A  1  970  ? -7.812  79.546  94.365  1.00 20.89 ? 968  TYR   A O     1 
ATOM   7107  C  CB    . TYR   A  1  970  ? -10.158 81.913  95.121  1.00 19.16 ? 968  TYR   A CB    1 
ATOM   7108  C  CG    . TYR   A  1  970  ? -10.482 83.316  95.580  1.00 19.91 ? 968  TYR   A CG    1 
ATOM   7109  C  CD1   . TYR   A  1  970  ? -11.008 83.547  96.844  1.00 21.69 ? 968  TYR   A CD1   1 
ATOM   7110  C  CD2   . TYR   A  1  970  ? -10.289 84.406  94.740  1.00 22.02 ? 968  TYR   A CD2   1 
ATOM   7111  C  CE1   . TYR   A  1  970  ? -11.326 84.833  97.267  1.00 22.54 ? 968  TYR   A CE1   1 
ATOM   7112  C  CE2   . TYR   A  1  970  ? -10.597 85.689  95.153  1.00 23.06 ? 968  TYR   A CE2   1 
ATOM   7113  C  CZ    . TYR   A  1  970  ? -11.113 85.896  96.419  1.00 25.25 ? 968  TYR   A CZ    1 
ATOM   7114  O  OH    . TYR   A  1  970  ? -11.430 87.172  96.834  1.00 31.24 ? 968  TYR   A OH    1 
ATOM   7115  N  N     . GLY   A  1  971  ? -9.401  79.133  95.892  1.00 15.97 ? 969  GLY   A N     1 
ATOM   7116  C  CA    . GLY   A  1  971  ? -9.265  77.705  95.717  1.00 15.37 ? 969  GLY   A CA    1 
ATOM   7117  C  C     . GLY   A  1  971  ? -10.304 76.949  96.507  1.00 15.73 ? 969  GLY   A C     1 
ATOM   7118  O  O     . GLY   A  1  971  ? -9.978  76.025  97.255  1.00 16.01 ? 969  GLY   A O     1 
ATOM   7119  N  N     . LEU   A  1  972  ? -11.568 77.327  96.337  1.00 14.97 ? 970  LEU   A N     1 
ATOM   7120  C  CA    . LEU   A  1  972  ? -12.636 76.729  97.125  1.00 14.53 ? 970  LEU   A CA    1 
ATOM   7121  C  C     . LEU   A  1  972  ? -13.301 75.605  96.336  1.00 14.97 ? 970  LEU   A C     1 
ATOM   7122  O  O     . LEU   A  1  972  ? -12.878 74.453  96.436  1.00 15.41 ? 970  LEU   A O     1 
ATOM   7123  C  CB    . LEU   A  1  972  ? -13.625 77.800  97.579  1.00 15.98 ? 970  LEU   A CB    1 
ATOM   7124  C  CG    . LEU   A  1  972  ? -14.645 77.339  98.620  1.00 16.30 ? 970  LEU   A CG    1 
ATOM   7125  C  CD1   . LEU   A  1  972  ? -13.959 76.645  99.795  1.00 16.54 ? 970  LEU   A CD1   1 
ATOM   7126  C  CD2   . LEU   A  1  972  ? -15.429 78.539  99.122  1.00 18.91 ? 970  LEU   A CD2   1 
ATOM   7127  N  N     . THR   A  1  973  ? -14.331 75.907  95.544  1.00 14.45 ? 971  THR   A N     1 
ATOM   7128  C  CA    . THR   A  1  973  ? -14.950 74.878  94.724  1.00 15.12 ? 971  THR   A CA    1 
ATOM   7129  C  C     . THR   A  1  973  ? -14.569 75.043  93.263  1.00 14.59 ? 971  THR   A C     1 
ATOM   7130  O  O     . THR   A  1  973  ? -14.197 76.123  92.802  1.00 15.10 ? 971  THR   A O     1 
ATOM   7131  C  CB    . THR   A  1  973  ? -16.473 74.888  94.857  1.00 14.79 ? 971  THR   A CB    1 
ATOM   7132  O  OG1   . THR   A  1  973  ? -16.966 76.168  94.451  1.00 14.48 ? 971  THR   A OG1   1 
ATOM   7133  C  CG2   . THR   A  1  973  ? -16.885 74.587  96.275  1.00 15.83 ? 971  THR   A CG2   1 
ATOM   7134  N  N     . PHE   A  1  974  ? -14.673 73.937  92.538  1.00 14.35 ? 972  PHE   A N     1 
ATOM   7135  C  CA    . PHE   A  1  974  ? -14.344 73.920  91.128  1.00 13.98 ? 972  PHE   A CA    1 
ATOM   7136  C  C     . PHE   A  1  974  ? -15.139 72.810  90.477  1.00 12.68 ? 972  PHE   A C     1 
ATOM   7137  O  O     . PHE   A  1  974  ? -15.229 71.702  91.006  1.00 15.22 ? 972  PHE   A O     1 
ATOM   7138  C  CB    . PHE   A  1  974  ? -12.855 73.650  90.907  1.00 14.37 ? 972  PHE   A CB    1 
ATOM   7139  C  CG    . PHE   A  1  974  ? -12.519 73.448  89.471  1.00 13.84 ? 972  PHE   A CG    1 
ATOM   7140  C  CD1   . PHE   A  1  974  ? -12.357 74.536  88.634  1.00 13.67 ? 972  PHE   A CD1   1 
ATOM   7141  C  CD2   . PHE   A  1  974  ? -12.436 72.170  88.944  1.00 13.93 ? 972  PHE   A CD2   1 
ATOM   7142  C  CE1   . PHE   A  1  974  ? -12.081 74.356  87.293  1.00 15.79 ? 972  PHE   A CE1   1 
ATOM   7143  C  CE2   . PHE   A  1  974  ? -12.160 71.980  87.600  1.00 14.24 ? 972  PHE   A CE2   1 
ATOM   7144  C  CZ    . PHE   A  1  974  ? -11.980 73.068  86.782  1.00 15.26 ? 972  PHE   A CZ    1 
ATOM   7145  N  N     . GLY   A  1  975  ? -15.702 73.107  89.313  1.00 13.77 ? 973  GLY   A N     1 
ATOM   7146  C  CA    . GLY   A  1  975  ? -16.482 72.140  88.575  1.00 14.14 ? 973  GLY   A CA    1 
ATOM   7147  C  C     . GLY   A  1  975  ? -15.905 71.882  87.200  1.00 13.88 ? 973  GLY   A C     1 
ATOM   7148  O  O     . GLY   A  1  975  ? -15.339 72.771  86.566  1.00 13.57 ? 973  GLY   A O     1 
ATOM   7149  N  N     . LEU   A  1  976  ? -16.085 70.654  86.734  1.00 12.98 ? 974  LEU   A N     1 
ATOM   7150  C  CA    . LEU   A  1  976  ? -15.681 70.293  85.385  1.00 13.42 ? 974  LEU   A CA    1 
ATOM   7151  C  C     . LEU   A  1  976  ? -16.774 69.435  84.790  1.00 13.63 ? 974  LEU   A C     1 
ATOM   7152  O  O     . LEU   A  1  976  ? -17.175 68.439  85.395  1.00 14.31 ? 974  LEU   A O     1 
ATOM   7153  C  CB    . LEU   A  1  976  ? -14.384 69.495  85.431  1.00 14.56 ? 974  LEU   A CB    1 
ATOM   7154  C  CG    . LEU   A  1  976  ? -13.941 68.867  84.117  1.00 14.95 ? 974  LEU   A CG    1 
ATOM   7155  C  CD1   . LEU   A  1  976  ? -13.594 69.951  83.107  1.00 16.72 ? 974  LEU   A CD1   1 
ATOM   7156  C  CD2   . LEU   A  1  976  ? -12.759 67.962  84.395  1.00 16.97 ? 974  LEU   A CD2   1 
ATOM   7157  N  N     . HIS   A  1  977  ? -17.264 69.826  83.618  1.00 13.51 ? 975  HIS   A N     1 
ATOM   7158  C  CA    . HIS   A  1  977  ? -18.225 69.029  82.875  1.00 14.20 ? 975  HIS   A CA    1 
ATOM   7159  C  C     . HIS   A  1  977  ? -17.524 68.548  81.616  1.00 14.85 ? 975  HIS   A C     1 
ATOM   7160  O  O     . HIS   A  1  977  ? -17.212 69.342  80.723  1.00 14.82 ? 975  HIS   A O     1 
ATOM   7161  C  CB    . HIS   A  1  977  ? -19.475 69.833  82.526  1.00 15.12 ? 975  HIS   A CB    1 
ATOM   7162  C  CG    . HIS   A  1  977  ? -20.560 69.722  83.543  1.00 17.83 ? 975  HIS   A CG    1 
ATOM   7163  N  ND1   . HIS   A  1  977  ? -21.685 68.953  83.344  1.00 23.36 ? 975  HIS   A ND1   1 
ATOM   7164  C  CD2   . HIS   A  1  977  ? -20.676 70.252  84.783  1.00 23.26 ? 975  HIS   A CD2   1 
ATOM   7165  C  CE1   . HIS   A  1  977  ? -22.460 69.034  84.411  1.00 21.09 ? 975  HIS   A CE1   1 
ATOM   7166  N  NE2   . HIS   A  1  977  ? -21.872 69.816  85.296  1.00 21.88 ? 975  HIS   A NE2   1 
ATOM   7167  N  N     . THR   A  1  978  ? -17.280 67.249  81.568  1.00 12.73 ? 976  THR   A N     1 
ATOM   7168  C  CA    . THR   A  1  978  ? -16.678 66.614  80.412  1.00 14.35 ? 976  THR   A CA    1 
ATOM   7169  C  C     . THR   A  1  978  ? -16.961 65.137  80.537  1.00 14.16 ? 976  THR   A C     1 
ATOM   7170  O  O     . THR   A  1  978  ? -17.119 64.608  81.640  1.00 16.67 ? 976  THR   A O     1 
ATOM   7171  C  CB    . THR   A  1  978  ? -15.161 66.831  80.364  1.00 15.07 ? 976  THR   A CB    1 
ATOM   7172  O  OG1   . THR   A  1  978  ? -14.626 66.155  79.225  1.00 15.50 ? 976  THR   A OG1   1 
ATOM   7173  C  CG2   . THR   A  1  978  ? -14.496 66.246  81.580  1.00 15.59 ? 976  THR   A CG2   1 
ATOM   7174  N  N     . ARG   A  1  979  ? -16.993 64.472  79.396  1.00 15.11 ? 977  ARG   A N     1 
ATOM   7175  C  CA    . ARG   A  1  979  ? -17.053 63.026  79.384  1.00 16.85 ? 977  ARG   A CA    1 
ATOM   7176  C  C     . ARG   A  1  979  ? -15.687 62.392  79.183  1.00 16.31 ? 977  ARG   A C     1 
ATOM   7177  O  O     . ARG   A  1  979  ? -15.590 61.163  79.173  1.00 19.01 ? 977  ARG   A O     1 
ATOM   7178  C  CB    . ARG   A  1  979  ? -17.989 62.579  78.274  1.00 17.05 ? 977  ARG   A CB    1 
ATOM   7179  C  CG    . ARG   A  1  979  ? -19.395 63.076  78.477  1.00 19.78 ? 977  ARG   A CG    1 
ATOM   7180  C  CD    . ARG   A  1  979  ? -20.243 62.750  77.292  1.00 28.82 ? 977  ARG   A CD    1 
ATOM   7181  N  NE    . ARG   A  1  979  ? -21.641 63.038  77.569  1.00 28.70 ? 977  ARG   A NE    1 
ATOM   7182  C  CZ    . ARG   A  1  979  ? -22.639 62.690  76.772  1.00 37.00 ? 977  ARG   A CZ    1 
ATOM   7183  N  NH1   . ARG   A  1  979  ? -22.417 62.067  75.625  1.00 27.93 ? 977  ARG   A NH1   1 
ATOM   7184  N  NH2   . ARG   A  1  979  ? -23.888 62.965  77.140  1.00 33.54 ? 977  ARG   A NH2   1 
ATOM   7185  N  N     . LEU   A  1  980  ? -14.637 63.187  79.016  1.00 14.13 ? 978  LEU   A N     1 
ATOM   7186  C  CA    . LEU   A  1  980  ? -13.370 62.685  78.494  1.00 14.19 ? 978  LEU   A CA    1 
ATOM   7187  C  C     . LEU   A  1  980  ? -12.362 62.486  79.623  1.00 14.28 ? 978  LEU   A C     1 
ATOM   7188  O  O     . LEU   A  1  980  ? -11.977 63.449  80.295  1.00 14.91 ? 978  LEU   A O     1 
ATOM   7189  C  CB    . LEU   A  1  980  ? -12.811 63.654  77.461  1.00 15.09 ? 978  LEU   A CB    1 
ATOM   7190  C  CG    . LEU   A  1  980  ? -13.766 63.981  76.314  1.00 16.18 ? 978  LEU   A CG    1 
ATOM   7191  C  CD1   . LEU   A  1  980  ? -13.117 64.985  75.391  1.00 17.10 ? 978  LEU   A CD1   1 
ATOM   7192  C  CD2   . LEU   A  1  980  ? -14.171 62.712  75.547  1.00 16.64 ? 978  LEU   A CD2   1 
ATOM   7193  N  N     . ASP   A  1  981  ? -11.901 61.241  79.797  1.00 15.69 ? 979  ASP   A N     1 
ATOM   7194  C  CA    . ASP   A  1  981  ? -10.968 60.941  80.882  1.00 14.33 ? 979  ASP   A CA    1 
ATOM   7195  C  C     . ASP   A  1  981  ? -9.687  61.752  80.776  1.00 15.73 ? 979  ASP   A C     1 
ATOM   7196  O  O     . ASP   A  1  981  ? -9.118  62.137  81.803  1.00 15.48 ? 979  ASP   A O     1 
ATOM   7197  C  CB    . ASP   A  1  981  ? -10.604 59.458  80.887  1.00 17.59 ? 979  ASP   A CB    1 
ATOM   7198  C  CG    . ASP   A  1  981  ? -11.715 58.585  81.375  1.00 17.31 ? 979  ASP   A CG    1 
ATOM   7199  O  OD1   . ASP   A  1  981  ? -12.669 59.111  81.988  1.00 20.66 ? 979  ASP   A OD1   1 
ATOM   7200  O  OD2   . ASP   A  1  981  ? -11.619 57.359  81.142  1.00 21.05 ? 979  ASP   A OD2   1 
ATOM   7201  N  N     . GLU   A  1  982  ? -9.182  61.979  79.559  1.00 14.90 ? 980  GLU   A N     1 
ATOM   7202  C  CA    . GLU   A  1  982  ? -7.950  62.751  79.438  1.00 15.63 ? 980  GLU   A CA    1 
ATOM   7203  C  C     . GLU   A  1  982  ? -8.146  64.158  79.987  1.00 15.44 ? 980  GLU   A C     1 
ATOM   7204  O  O     . GLU   A  1  982  ? -7.274  64.698  80.674  1.00 15.70 ? 980  GLU   A O     1 
ATOM   7205  C  CB    . GLU   A  1  982  ? -7.490  62.815  77.984  1.00 16.53 ? 980  GLU   A CB    1 
ATOM   7206  C  CG    . GLU   A  1  982  ? -6.276  63.712  77.816  1.00 17.96 ? 980  GLU   A CG    1 
ATOM   7207  C  CD    . GLU   A  1  982  ? -6.012  64.092  76.380  1.00 22.47 ? 980  GLU   A CD    1 
ATOM   7208  O  OE1   . GLU   A  1  982  ? -6.931  64.603  75.710  1.00 25.77 ? 980  GLU   A OE1   1 
ATOM   7209  O  OE2   . GLU   A  1  982  ? -4.868  63.898  75.916  1.00 20.29 ? 980  GLU   A OE2   1 
ATOM   7210  N  N     . THR   A  1  983  ? -9.308  64.749  79.725  1.00 14.11 ? 981  THR   A N     1 
ATOM   7211  C  CA    . THR   A  1  983  ? -9.567  66.095  80.205  1.00 14.65 ? 981  THR   A CA    1 
ATOM   7212  C  C     . THR   A  1  983  ? -9.773  66.094  81.711  1.00 14.66 ? 981  THR   A C     1 
ATOM   7213  O  O     . THR   A  1  983  ? -9.281  66.988  82.407  1.00 14.57 ? 981  THR   A O     1 
ATOM   7214  C  CB    . THR   A  1  983  ? -10.799 66.637  79.487  1.00 15.43 ? 981  THR   A CB    1 
ATOM   7215  O  OG1   . THR   A  1  983  ? -10.515 66.737  78.088  1.00 17.88 ? 981  THR   A OG1   1 
ATOM   7216  C  CG2   . THR   A  1  983  ? -11.197 68.007  80.027  1.00 16.90 ? 981  THR   A CG2   1 
ATOM   7217  N  N     . ILE   A  1  984  ? -10.470 65.082  82.240  1.00 14.30 ? 982  ILE   A N     1 
ATOM   7218  C  CA    . ILE   A  1  984  ? -10.613 64.969  83.692  1.00 15.18 ? 982  ILE   A CA    1 
ATOM   7219  C  C     . ILE   A  1  984  ? -9.248  64.870  84.360  1.00 14.20 ? 982  ILE   A C     1 
ATOM   7220  O  O     . ILE   A  1  984  ? -8.972  65.559  85.350  1.00 14.38 ? 982  ILE   A O     1 
ATOM   7221  C  CB    . ILE   A  1  984  ? -11.504 63.773  84.063  1.00 14.13 ? 982  ILE   A CB    1 
ATOM   7222  C  CG1   . ILE   A  1  984  ? -12.926 64.013  83.575  1.00 15.79 ? 982  ILE   A CG1   1 
ATOM   7223  C  CG2   . ILE   A  1  984  ? -11.475 63.529  85.574  1.00 16.41 ? 982  ILE   A CG2   1 
ATOM   7224  C  CD1   . ILE   A  1  984  ? -13.810 62.797  83.701  1.00 19.21 ? 982  ILE   A CD1   1 
ATOM   7225  N  N     . ALA   A  1  985  ? -8.382  63.994  83.839  1.00 13.86 ? 983  ALA   A N     1 
ATOM   7226  C  CA    . ALA   A  1  985  ? -7.078  63.799  84.464  1.00 15.22 ? 983  ALA   A CA    1 
ATOM   7227  C  C     . ALA   A  1  985  ? -6.261  65.076  84.392  1.00 14.81 ? 983  ALA   A C     1 
ATOM   7228  O  O     . ALA   A  1  985  ? -5.651  65.492  85.383  1.00 16.33 ? 983  ALA   A O     1 
ATOM   7229  C  CB    . ALA   A  1  985  ? -6.343  62.645  83.781  1.00 16.57 ? 983  ALA   A CB    1 
ATOM   7230  N  N     . HIS   A  1  986  ? -6.268  65.727  83.233  1.00 15.13 ? 984  HIS   A N     1 
ATOM   7231  C  CA    . HIS   A  1  986  ? -5.519  66.964  83.064  1.00 16.64 ? 984  HIS   A CA    1 
ATOM   7232  C  C     . HIS   A  1  986  ? -6.024  68.026  84.024  1.00 17.60 ? 984  HIS   A C     1 
ATOM   7233  O  O     . HIS   A  1  986  ? -5.271  68.569  84.835  1.00 16.67 ? 984  HIS   A O     1 
ATOM   7234  C  CB    . HIS   A  1  986  ? -5.685  67.429  81.619  1.00 17.18 ? 984  HIS   A CB    1 
ATOM   7235  C  CG    . HIS   A  1  986  ? -5.130  68.791  81.329  1.00 18.26 ? 984  HIS   A CG    1 
ATOM   7236  N  ND1   . HIS   A  1  986  ? -5.325  69.417  80.118  1.00 23.67 ? 984  HIS   A ND1   1 
ATOM   7237  C  CD2   . HIS   A  1  986  ? -4.381  69.641  82.072  1.00 18.73 ? 984  HIS   A CD2   1 
ATOM   7238  C  CE1   . HIS   A  1  986  ? -4.723  70.594  80.128  1.00 23.08 ? 984  HIS   A CE1   1 
ATOM   7239  N  NE2   . HIS   A  1  986  ? -4.155  70.761  81.308  1.00 18.36 ? 984  HIS   A NE2   1 
ATOM   7240  N  N     . VAL   A  1  987  ? -7.314  68.323  83.954  1.00 15.94 ? 985  VAL   A N     1 
ATOM   7241  C  CA    . VAL   A  1  987  ? -7.845  69.443  84.717  1.00 15.55 ? 985  VAL   A CA    1 
ATOM   7242  C  C     . VAL   A  1  987  ? -7.737  69.177  86.209  1.00 15.63 ? 985  VAL   A C     1 
ATOM   7243  O  O     . VAL   A  1  987  ? -7.341  70.056  86.980  1.00 16.27 ? 985  VAL   A O     1 
ATOM   7244  C  CB    . VAL   A  1  987  ? -9.287  69.750  84.290  1.00 14.06 ? 985  VAL   A CB    1 
ATOM   7245  C  CG1   . VAL   A  1  987  ? -9.888  70.791  85.225  1.00 15.28 ? 985  VAL   A CG1   1 
ATOM   7246  C  CG2   . VAL   A  1  987  ? -9.298  70.257  82.858  1.00 18.50 ? 985  VAL   A CG2   1 
ATOM   7247  N  N     . THR   A  1  988  ? -8.100  67.974  86.651  1.00 15.77 ? 986  THR   A N     1 
ATOM   7248  C  CA    . THR   A  1  988  ? -8.071  67.754  88.095  1.00 17.38 ? 986  THR   A CA    1 
ATOM   7249  C  C     . THR   A  1  988  ? -6.654  67.699  88.640  1.00 21.30 ? 986  THR   A C     1 
ATOM   7250  O  O     . THR   A  1  988  ? -6.448  67.980  89.826  1.00 20.78 ? 986  THR   A O     1 
ATOM   7251  C  CB    . THR   A  1  988  ? -8.856  66.512  88.514  1.00 18.73 ? 986  THR   A CB    1 
ATOM   7252  O  OG1   . THR   A  1  988  ? -8.281  65.353  87.918  1.00 19.20 ? 986  THR   A OG1   1 
ATOM   7253  C  CG2   . THR   A  1  988  ? -10.311 66.617  88.094  1.00 19.38 ? 986  THR   A CG2   1 
ATOM   7254  N  N     . SER   A  1  989  ? -5.673  67.365  87.812  1.00 16.63 ? 987  SER   A N     1 
ATOM   7255  C  CA    A SER   A  1  989  ? -4.304  67.353  88.300  0.68 19.80 ? 987  SER   A CA    1 
ATOM   7256  C  CA    B SER   A  1  989  ? -4.291  67.352  88.270  0.32 19.82 ? 987  SER   A CA    1 
ATOM   7257  C  C     . SER   A  1  989  ? -3.705  68.750  88.365  1.00 22.84 ? 987  SER   A C     1 
ATOM   7258  O  O     . SER   A  1  989  ? -2.761  68.963  89.131  1.00 28.24 ? 987  SER   A O     1 
ATOM   7259  C  CB    A SER   A  1  989  ? -3.440  66.417  87.450  0.68 20.85 ? 987  SER   A CB    1 
ATOM   7260  C  CB    B SER   A  1  989  ? -3.431  66.504  87.332  0.32 20.77 ? 987  SER   A CB    1 
ATOM   7261  O  OG    A SER   A  1  989  ? -3.235  66.937  86.152  0.68 22.99 ? 987  SER   A OG    1 
ATOM   7262  O  OG    B SER   A  1  989  ? -2.059  66.610  87.668  0.32 22.81 ? 987  SER   A OG    1 
ATOM   7263  N  N     . ARG   A  1  990  ? -4.247  69.702  87.611  1.00 17.22 ? 988  ARG   A N     1 
ATOM   7264  C  CA    . ARG   A  1  990  ? -3.689  71.046  87.524  1.00 19.42 ? 988  ARG   A CA    1 
ATOM   7265  C  C     . ARG   A  1  990  ? -4.453  72.075  88.334  1.00 17.99 ? 988  ARG   A C     1 
ATOM   7266  O  O     . ARG   A  1  990  ? -3.863  73.070  88.762  1.00 18.83 ? 988  ARG   A O     1 
ATOM   7267  C  CB    . ARG   A  1  990  ? -3.633  71.494  86.061  1.00 19.66 ? 988  ARG   A CB    1 
ATOM   7268  C  CG    . ARG   A  1  990  ? -2.872  70.528  85.175  1.00 27.65 ? 988  ARG   A CG    1 
ATOM   7269  C  CD    . ARG   A  1  990  ? -1.377  70.718  85.281  1.00 30.02 ? 988  ARG   A CD    1 
ATOM   7270  N  NE    . ARG   A  1  990  ? -0.897  71.646  84.265  1.00 27.06 ? 988  ARG   A NE    1 
ATOM   7271  C  CZ    . ARG   A  1  990  ? 0.354   72.072  84.178  1.00 26.39 ? 988  ARG   A CZ    1 
ATOM   7272  N  NH1   . ARG   A  1  990  ? 1.263   71.732  85.078  1.00 30.44 ? 988  ARG   A NH1   1 
ATOM   7273  N  NH2   . ARG   A  1  990  ? 0.703   72.853  83.158  1.00 27.44 ? 988  ARG   A NH2   1 
ATOM   7274  N  N     . ILE   A  1  991  ? -5.754  71.873  88.536  1.00 16.59 ? 989  ILE   A N     1 
ATOM   7275  C  CA    . ILE   A  1  991  ? -6.533  72.797  89.341  1.00 16.43 ? 989  ILE   A CA    1 
ATOM   7276  C  C     . ILE   A  1  991  ? -6.067  72.713  90.785  1.00 17.55 ? 989  ILE   A C     1 
ATOM   7277  O  O     . ILE   A  1  991  ? -5.648  71.654  91.267  1.00 18.44 ? 989  ILE   A O     1 
ATOM   7278  C  CB    . ILE   A  1  991  ? -8.032  72.466  89.207  1.00 16.15 ? 989  ILE   A CB    1 
ATOM   7279  C  CG1   . ILE   A  1  991  ? -8.881  73.607  89.760  1.00 18.86 ? 989  ILE   A CG1   1 
ATOM   7280  C  CG2   . ILE   A  1  991  ? -8.348  71.160  89.896  1.00 17.38 ? 989  ILE   A CG2   1 
ATOM   7281  C  CD1   . ILE   A  1  991  ? -8.831  74.828  88.884  1.00 20.30 ? 989  ILE   A CD1   1 
ATOM   7282  N  N     . LYS   A  1  992  ? -6.126  73.843  91.480  1.00 16.09 ? 990  LYS   A N     1 
ATOM   7283  C  CA    . LYS   A  1  992  ? -5.755  73.923  92.887  1.00 17.41 ? 990  LYS   A CA    1 
ATOM   7284  C  C     . LYS   A  1  992  ? -6.956  74.452  93.662  1.00 16.02 ? 990  LYS   A C     1 
ATOM   7285  O  O     . LYS   A  1  992  ? -7.074  75.651  93.924  1.00 19.14 ? 990  LYS   A O     1 
ATOM   7286  C  CB    . LYS   A  1  992  ? -4.531  74.811  93.048  1.00 17.84 ? 990  LYS   A CB    1 
ATOM   7287  C  CG    . LYS   A  1  992  ? -3.303  74.272  92.326  1.00 21.29 ? 990  LYS   A CG    1 
ATOM   7288  C  CD    . LYS   A  1  992  ? -2.068  75.119  92.596  1.00 32.87 ? 990  LYS   A CD    1 
ATOM   7289  C  CE    . LYS   A  1  992  ? -2.329  76.583  92.305  1.00 38.68 ? 990  LYS   A CE    1 
ATOM   7290  N  NZ    . LYS   A  1  992  ? -1.189  77.439  92.739  1.00 45.64 ? 990  LYS   A NZ    1 
ATOM   7291  N  N     . ALA   A  1  993  ? -7.846  73.543  94.034  1.00 16.80 ? 991  ALA   A N     1 
ATOM   7292  C  CA    . ALA   A  1  993  ? -9.033  73.904  94.793  1.00 14.94 ? 991  ALA   A CA    1 
ATOM   7293  C  C     . ALA   A  1  993  ? -9.372  72.761  95.728  1.00 16.17 ? 991  ALA   A C     1 
ATOM   7294  O  O     . ALA   A  1  993  ? -9.039  71.602  95.474  1.00 17.92 ? 991  ALA   A O     1 
ATOM   7295  C  CB    . ALA   A  1  993  ? -10.213 74.212  93.873  1.00 16.25 ? 991  ALA   A CB    1 
ATOM   7296  N  N     . GLY   A  1  994  ? -10.083 73.094  96.805  1.00 14.69 ? 992  GLY   A N     1 
ATOM   7297  C  CA    . GLY   A  1  994  ? -10.320 72.108  97.837  1.00 15.74 ? 992  GLY   A CA    1 
ATOM   7298  C  C     . GLY   A  1  994  ? -11.465 71.161  97.558  1.00 13.73 ? 992  GLY   A C     1 
ATOM   7299  O  O     . GLY   A  1  994  ? -11.483 70.046  98.083  1.00 14.55 ? 992  GLY   A O     1 
ATOM   7300  N  N     . ASN   A  1  995  ? -12.445 71.585  96.765  1.00 13.70 ? 993  ASN   A N     1 
ATOM   7301  C  CA    . ASN   A  1  995  ? -13.625 70.774  96.500  1.00 14.37 ? 993  ASN   A CA    1 
ATOM   7302  C  C     . ASN   A  1  995  ? -13.853 70.763  95.004  1.00 14.45 ? 993  ASN   A C     1 
ATOM   7303  O  O     . ASN   A  1  995  ? -14.153 71.799  94.410  1.00 14.37 ? 993  ASN   A O     1 
ATOM   7304  C  CB    . ASN   A  1  995  ? -14.841 71.321  97.235  1.00 14.59 ? 993  ASN   A CB    1 
ATOM   7305  C  CG    . ASN   A  1  995  ? -14.852 70.898  98.674  1.00 15.05 ? 993  ASN   A CG    1 
ATOM   7306  O  OD1   . ASN   A  1  995  ? -14.207 71.513  99.523  1.00 15.91 ? 993  ASN   A OD1   1 
ATOM   7307  N  ND2   . ASN   A  1  995  ? -15.558 69.813  98.956  1.00 15.21 ? 993  ASN   A ND2   1 
ATOM   7308  N  N     . LEU   A  1  996  ? -13.669 69.604  94.402  1.00 12.77 ? 994  LEU   A N     1 
ATOM   7309  C  CA    . LEU   A  1  996  ? -13.839 69.443  92.973  1.00 13.70 ? 994  LEU   A CA    1 
ATOM   7310  C  C     . LEU   A  1  996  ? -15.109 68.663  92.716  1.00 12.64 ? 994  LEU   A C     1 
ATOM   7311  O  O     . LEU   A  1  996  ? -15.472 67.774  93.485  1.00 13.53 ? 994  LEU   A O     1 
ATOM   7312  C  CB    . LEU   A  1  996  ? -12.675 68.649  92.388  1.00 14.24 ? 994  LEU   A CB    1 
ATOM   7313  C  CG    . LEU   A  1  996  ? -11.284 69.091  92.841  1.00 15.75 ? 994  LEU   A CG    1 
ATOM   7314  C  CD1   . LEU   A  1  996  ? -10.215 68.236  92.165  1.00 19.23 ? 994  LEU   A CD1   1 
ATOM   7315  C  CD2   . LEU   A  1  996  ? -11.067 70.564  92.557  1.00 16.83 ? 994  LEU   A CD2   1 
ATOM   7316  N  N     . TYR   A  1  997  ? -15.760 68.980  91.601  1.00 13.12 ? 995  TYR   A N     1 
ATOM   7317  C  CA    . TYR   A  1  997  ? -17.021 68.341  91.255  1.00 13.76 ? 995  TYR   A CA    1 
ATOM   7318  C  C     . TYR   A  1  997  ? -17.007 68.063  89.769  1.00 13.52 ? 995  TYR   A C     1 
ATOM   7319  O  O     . TYR   A  1  997  ? -16.733 68.960  88.971  1.00 14.78 ? 995  TYR   A O     1 
ATOM   7320  C  CB    . TYR   A  1  997  ? -18.198 69.253  91.579  1.00 14.52 ? 995  TYR   A CB    1 
ATOM   7321  C  CG    . TYR   A  1  997  ? -18.229 69.667  93.017  1.00 14.28 ? 995  TYR   A CG    1 
ATOM   7322  C  CD1   . TYR   A  1  997  ? -17.565 70.811  93.431  1.00 14.68 ? 995  TYR   A CD1   1 
ATOM   7323  C  CD2   . TYR   A  1  997  ? -18.912 68.919  93.958  1.00 15.50 ? 995  TYR   A CD2   1 
ATOM   7324  C  CE1   . TYR   A  1  997  ? -17.573 71.199  94.751  1.00 17.26 ? 995  TYR   A CE1   1 
ATOM   7325  C  CE2   . TYR   A  1  997  ? -18.928 69.306  95.287  1.00 15.79 ? 995  TYR   A CE2   1 
ATOM   7326  C  CZ    . TYR   A  1  997  ? -18.261 70.446  95.662  1.00 18.00 ? 995  TYR   A CZ    1 
ATOM   7327  O  OH    . TYR   A  1  997  ? -18.290 70.832  96.988  1.00 21.17 ? 995  TYR   A OH    1 
ATOM   7328  N  N     . ILE   A  1  998  ? -17.267 66.820  89.406  1.00 12.52 ? 996  ILE   A N     1 
ATOM   7329  C  CA    A ILE   A  1  998  ? -17.203 66.382  88.018  0.45 13.82 ? 996  ILE   A CA    1 
ATOM   7330  C  CA    B ILE   A  1  998  ? -17.208 66.397  88.016  0.55 13.81 ? 996  ILE   A CA    1 
ATOM   7331  C  C     . ILE   A  1  998  ? -18.610 66.017  87.577  1.00 13.04 ? 996  ILE   A C     1 
ATOM   7332  O  O     . ILE   A  1  998  ? -19.228 65.113  88.150  1.00 14.04 ? 996  ILE   A O     1 
ATOM   7333  C  CB    A ILE   A  1  998  ? -16.243 65.196  87.841  0.45 14.16 ? 996  ILE   A CB    1 
ATOM   7334  C  CB    B ILE   A  1  998  ? -16.208 65.252  87.813  0.55 14.14 ? 996  ILE   A CB    1 
ATOM   7335  C  CG1   A ILE   A  1  998  ? -14.891 65.495  88.492  0.45 17.09 ? 996  ILE   A CG1   1 
ATOM   7336  C  CG1   B ILE   A  1  998  ? -14.800 65.723  88.187  0.55 17.25 ? 996  ILE   A CG1   1 
ATOM   7337  C  CG2   A ILE   A  1  998  ? -16.071 64.887  86.356  0.45 15.41 ? 996  ILE   A CG2   1 
ATOM   7338  C  CG2   B ILE   A  1  998  ? -16.276 64.748  86.371  0.55 15.27 ? 996  ILE   A CG2   1 
ATOM   7339  C  CD1   A ILE   A  1  998  ? -14.155 66.620  87.825  0.45 16.31 ? 996  ILE   A CD1   1 
ATOM   7340  C  CD1   B ILE   A  1  998  ? -13.789 64.623  88.208  0.55 17.09 ? 996  ILE   A CD1   1 
ATOM   7341  N  N     . ASN   A  1  999  ? -19.096 66.712  86.546  1.00 13.00 ? 997  ASN   A N     1 
ATOM   7342  C  CA    . ASN   A  1  999  ? -20.384 66.416  85.917  1.00 13.91 ? 997  ASN   A CA    1 
ATOM   7343  C  C     . ASN   A  1  999  ? -21.560 66.565  86.872  1.00 13.49 ? 997  ASN   A C     1 
ATOM   7344  O  O     . ASN   A  1  999  ? -22.527 65.806  86.814  1.00 14.35 ? 997  ASN   A O     1 
ATOM   7345  C  CB    . ASN   A  1  999  ? -20.359 65.050  85.239  1.00 13.11 ? 997  ASN   A CB    1 
ATOM   7346  C  CG    . ASN   A  1  999  ? -19.398 65.027  84.091  1.00 13.74 ? 997  ASN   A CG    1 
ATOM   7347  O  OD1   . ASN   A  1  999  ? -19.196 66.047  83.434  1.00 15.25 ? 997  ASN   A OD1   1 
ATOM   7348  N  ND2   . ASN   A  1  999  ? -18.773 63.893  83.859  1.00 16.04 ? 997  ASN   A ND2   1 
ATOM   7349  N  N     . ARG   A  1  1000 ? -21.477 67.561  87.745  1.00 13.53 ? 998  ARG   A N     1 
ATOM   7350  C  CA    . ARG   A  1  1000 ? -22.548 67.848  88.691  1.00 14.12 ? 998  ARG   A CA    1 
ATOM   7351  C  C     . ARG   A  1  1000 ? -22.404 69.301  89.120  1.00 14.28 ? 998  ARG   A C     1 
ATOM   7352  O  O     . ARG   A  1  1000 ? -21.499 70.011  88.683  1.00 15.94 ? 998  ARG   A O     1 
ATOM   7353  C  CB    . ARG   A  1  1000 ? -22.497 66.893  89.879  1.00 14.16 ? 998  ARG   A CB    1 
ATOM   7354  C  CG    . ARG   A  1  1000 ? -21.109 66.824  90.515  1.00 14.22 ? 998  ARG   A CG    1 
ATOM   7355  C  CD    . ARG   A  1  1000 ? -21.202 66.442  91.975  1.00 14.90 ? 998  ARG   A CD    1 
ATOM   7356  N  NE    . ARG   A  1  1000 ? -21.843 67.505  92.734  1.00 13.43 ? 998  ARG   A NE    1 
ATOM   7357  C  CZ    . ARG   A  1  1000 ? -22.141 67.431  94.021  1.00 16.18 ? 998  ARG   A CZ    1 
ATOM   7358  N  NH1   . ARG   A  1  1000 ? -21.854 66.354  94.736  1.00 17.14 ? 998  ARG   A NH1   1 
ATOM   7359  N  NH2   . ARG   A  1  1000 ? -22.730 68.467  94.611  1.00 16.95 ? 998  ARG   A NH2   1 
ATOM   7360  N  N     . ASN   A  1  1001 ? -23.323 69.758  89.961  1.00 13.81 ? 999  ASN   A N     1 
ATOM   7361  C  CA    . ASN   A  1  1001 ? -23.166 71.109  90.472  1.00 14.12 ? 999  ASN   A CA    1 
ATOM   7362  C  C     . ASN   A  1  1001 ? -21.992 71.171  91.452  1.00 15.12 ? 999  ASN   A C     1 
ATOM   7363  O  O     . ASN   A  1  1001 ? -21.413 70.155  91.843  1.00 15.18 ? 999  ASN   A O     1 
ATOM   7364  C  CB    . ASN   A  1  1001 ? -24.478 71.625  91.077  1.00 17.32 ? 999  ASN   A CB    1 
ATOM   7365  C  CG    . ASN   A  1  1001 ? -24.852 70.931  92.357  1.00 17.60 ? 999  ASN   A CG    1 
ATOM   7366  O  OD1   . ASN   A  1  1001 ? -24.029 70.735  93.242  1.00 17.80 ? 999  ASN   A OD1   1 
ATOM   7367  N  ND2   . ASN   A  1  1001 ? -26.136 70.604  92.488  1.00 22.59 ? 999  ASN   A ND2   1 
ATOM   7368  N  N     . ILE   A  1  1002 ? -21.640 72.387  91.845  1.00 14.59 ? 1000 ILE   A N     1 
ATOM   7369  C  CA    . ILE   A  1  1002 ? -20.468 72.586  92.681  1.00 15.72 ? 1000 ILE   A CA    1 
ATOM   7370  C  C     . ILE   A  1  1002 ? -20.836 73.041  94.084  1.00 15.47 ? 1000 ILE   A C     1 
ATOM   7371  O  O     . ILE   A  1  1002 ? -19.991 73.578  94.787  1.00 17.40 ? 1000 ILE   A O     1 
ATOM   7372  C  CB    . ILE   A  1  1002 ? -19.442 73.523  92.028  1.00 14.34 ? 1000 ILE   A CB    1 
ATOM   7373  C  CG1   . ILE   A  1  1002 ? -19.989 74.948  91.912  1.00 15.73 ? 1000 ILE   A CG1   1 
ATOM   7374  C  CG2   . ILE   A  1  1002 ? -19.052 72.981  90.661  1.00 14.42 ? 1000 ILE   A CG2   1 
ATOM   7375  C  CD1   . ILE   A  1  1002 ? -18.940 75.931  91.492  1.00 15.58 ? 1000 ILE   A CD1   1 
ATOM   7376  N  N     A ILE   A  1  1003 ? -22.077 72.843  94.513  0.47 16.21 ? 1001 ILE   A N     1 
ATOM   7377  N  N     B ILE   A  1  1003 ? -22.085 72.804  94.503  0.53 16.18 ? 1001 ILE   A N     1 
ATOM   7378  C  CA    A ILE   A  1  1003 ? -22.481 73.341  95.820  0.47 18.25 ? 1001 ILE   A CA    1 
ATOM   7379  C  CA    B ILE   A  1  1003 ? -22.634 73.341  95.745  0.53 18.29 ? 1001 ILE   A CA    1 
ATOM   7380  C  C     A ILE   A  1  1003 ? -22.525 72.236  96.869  0.47 20.49 ? 1001 ILE   A C     1 
ATOM   7381  C  C     B ILE   A  1  1003 ? -23.276 72.226  96.569  0.53 16.27 ? 1001 ILE   A C     1 
ATOM   7382  O  O     A ILE   A  1  1003 ? -23.066 72.439  97.962  0.47 20.26 ? 1001 ILE   A O     1 
ATOM   7383  O  O     B ILE   A  1  1003 ? -23.433 71.091  96.121  0.53 18.49 ? 1001 ILE   A O     1 
ATOM   7384  C  CB    A ILE   A  1  1003 ? -23.777 74.163  95.757  0.47 17.24 ? 1001 ILE   A CB    1 
ATOM   7385  C  CB    B ILE   A  1  1003 ? -23.649 74.482  95.511  0.53 17.37 ? 1001 ILE   A CB    1 
ATOM   7386  C  CG1   A ILE   A  1  1003 ? -24.921 73.360  95.137  0.47 17.67 ? 1001 ILE   A CG1   1 
ATOM   7387  C  CG1   B ILE   A  1  1003 ? -24.888 73.974  94.765  0.53 14.97 ? 1001 ILE   A CG1   1 
ATOM   7388  C  CG2   A ILE   A  1  1003 ? -23.534 75.440  94.966  0.47 15.89 ? 1001 ILE   A CG2   1 
ATOM   7389  C  CG2   B ILE   A  1  1003 ? -23.002 75.636  94.775  0.53 15.57 ? 1001 ILE   A CG2   1 
ATOM   7390  C  CD1   A ILE   A  1  1003 ? -26.256 74.076  95.217  0.47 19.73 ? 1001 ILE   A CD1   1 
ATOM   7391  C  CD1   B ILE   A  1  1003 ? -26.091 74.910  94.876  0.53 21.04 ? 1001 ILE   A CD1   1 
ATOM   7392  N  N     A GLY   A  1  1004 ? -21.922 71.085  96.579  0.47 18.00 ? 1002 GLY   A N     1 
ATOM   7393  N  N     B GLY   A  1  1004 ? -23.644 72.575  97.798  0.53 18.59 ? 1002 GLY   A N     1 
ATOM   7394  C  CA    A GLY   A  1  1004 ? -21.982 69.958  97.486  0.47 17.28 ? 1002 GLY   A CA    1 
ATOM   7395  C  CA    B GLY   A  1  1004 ? -24.249 71.606  98.696  0.53 17.06 ? 1002 GLY   A CA    1 
ATOM   7396  C  C     A GLY   A  1  1004 ? -21.055 70.132  98.666  0.47 17.19 ? 1002 GLY   A C     1 
ATOM   7397  C  C     B GLY   A  1  1004 ? -23.337 70.470  99.118  0.53 17.61 ? 1002 GLY   A C     1 
ATOM   7398  O  O     A GLY   A  1  1004 ? -19.844 70.349  98.493  0.47 17.25 ? 1002 GLY   A O     1 
ATOM   7399  O  O     B GLY   A  1  1004 ? -23.771 69.310  99.140  0.53 19.07 ? 1002 GLY   A O     1 
ATOM   7400  N  N     A ALA   A  1  1005 ? -21.596 70.036  99.867  0.47 17.73 ? 1003 ALA   A N     1 
ATOM   7401  N  N     B ALA   A  1  1005 ? -22.087 70.773  99.459  0.53 18.09 ? 1003 ALA   A N     1 
ATOM   7402  C  CA    A ALA   A  1  1005 ? -20.804 70.092  101.083 0.47 17.50 ? 1003 ALA   A CA    1 
ATOM   7403  C  CA    B ALA   A  1  1005 ? -21.171 69.739  99.923  0.53 17.54 ? 1003 ALA   A CA    1 
ATOM   7404  C  C     A ALA   A  1  1005 ? -21.285 69.044  102.059 0.47 18.91 ? 1003 ALA   A C     1 
ATOM   7405  C  C     B ALA   A  1  1005 ? -21.731 69.067  101.170 0.53 17.60 ? 1003 ALA   A C     1 
ATOM   7406  O  O     A ALA   A  1  1005 ? -21.298 69.258  103.276 0.47 18.54 ? 1003 ALA   A O     1 
ATOM   7407  O  O     B ALA   A  1  1005 ? -22.301 69.724  102.048 0.53 20.96 ? 1003 ALA   A O     1 
ATOM   7408  C  CB    A ALA   A  1  1005 ? -20.844 71.478  101.715 0.47 18.62 ? 1003 ALA   A CB    1 
ATOM   7409  C  CB    B ALA   A  1  1005 ? -19.808 70.349  100.245 0.53 18.76 ? 1003 ALA   A CB    1 
ATOM   7410  N  N     A VAL   A  1  1006 ? -21.700 67.896  101.525 0.47 17.03 ? 1004 VAL   A N     1 
ATOM   7411  N  N     B VAL   A  1  1006 ? -21.567 67.745  101.242 0.53 17.08 ? 1004 VAL   A N     1 
ATOM   7412  C  CA    A VAL   A  1  1006 ? -22.260 66.818  102.324 0.47 16.78 ? 1004 VAL   A CA    1 
ATOM   7413  C  CA    B VAL   A  1  1006 ? -22.170 66.926  102.288 0.53 16.72 ? 1004 VAL   A CA    1 
ATOM   7414  C  C     A VAL   A  1  1006 ? -21.228 66.371  103.344 0.47 16.53 ? 1004 VAL   A C     1 
ATOM   7415  C  C     B VAL   A  1  1006 ? -21.116 66.597  103.333 0.53 16.62 ? 1004 VAL   A C     1 
ATOM   7416  O  O     A VAL   A  1  1006 ? -20.203 65.772  102.998 0.47 14.54 ? 1004 VAL   A O     1 
ATOM   7417  O  O     B VAL   A  1  1006 ? -19.976 66.264  102.999 0.53 16.19 ? 1004 VAL   A O     1 
ATOM   7418  C  CB    A VAL   A  1  1006 ? -22.735 65.643  101.456 0.47 18.22 ? 1004 VAL   A CB    1 
ATOM   7419  C  CB    B VAL   A  1  1006 ? -22.784 65.646  101.689 0.53 17.85 ? 1004 VAL   A CB    1 
ATOM   7420  C  CG1   A VAL   A  1  1006 ? -23.269 64.537  102.344 0.47 18.27 ? 1004 VAL   A CG1   1 
ATOM   7421  C  CG1   B VAL   A  1  1006 ? -23.216 64.686  102.786 0.53 18.49 ? 1004 VAL   A CG1   1 
ATOM   7422  C  CG2   A VAL   A  1  1006 ? -23.799 66.113  100.477 0.47 18.24 ? 1004 VAL   A CG2   1 
ATOM   7423  C  CG2   B VAL   A  1  1006 ? -23.958 66.001  100.784 0.53 18.11 ? 1004 VAL   A CG2   1 
ATOM   7424  N  N     . VAL   A  1  1007 ? -21.500 66.688  104.607 1.00 16.04 ? 1005 VAL   A N     1 
ATOM   7425  C  CA    . VAL   A  1  1007 ? -20.568 66.427  105.689 1.00 16.92 ? 1005 VAL   A CA    1 
ATOM   7426  C  C     . VAL   A  1  1007 ? -20.090 64.985  105.632 1.00 17.51 ? 1005 VAL   A C     1 
ATOM   7427  O  O     . VAL   A  1  1007 ? -20.884 64.054  105.471 1.00 17.83 ? 1005 VAL   A O     1 
ATOM   7428  C  CB    . VAL   A  1  1007 ? -21.273 66.738  107.018 1.00 17.39 ? 1005 VAL   A CB    1 
ATOM   7429  C  CG1   . VAL   A  1  1007 ? -20.407 66.311  108.176 1.00 18.62 ? 1005 VAL   A CG1   1 
ATOM   7430  C  CG2   . VAL   A  1  1007 ? -21.603 68.212  107.089 1.00 17.88 ? 1005 VAL   A CG2   1 
ATOM   7431  N  N     . GLY   A  1  1008 ? -18.776 64.794  105.749 1.00 16.56 ? 1006 GLY   A N     1 
ATOM   7432  C  CA    . GLY   A  1  1008 ? -18.197 63.465  105.734 1.00 17.75 ? 1006 GLY   A CA    1 
ATOM   7433  C  C     . GLY   A  1  1008 ? -18.241 62.774  104.394 1.00 17.17 ? 1006 GLY   A C     1 
ATOM   7434  O  O     . GLY   A  1  1008 ? -17.806 61.624  104.287 1.00 18.43 ? 1006 GLY   A O     1 
ATOM   7435  N  N     . VAL   A  1  1009 ? -18.747 63.438  103.365 1.00 16.69 ? 1007 VAL   A N     1 
ATOM   7436  C  CA    . VAL   A  1  1009 ? -18.828 62.884  102.022 1.00 16.90 ? 1007 VAL   A CA    1 
ATOM   7437  C  C     . VAL   A  1  1009 ? -18.083 63.764  101.037 1.00 16.62 ? 1007 VAL   A C     1 
ATOM   7438  O  O     . VAL   A  1  1009 ? -17.246 63.286  100.264 1.00 17.39 ? 1007 VAL   A O     1 
ATOM   7439  C  CB    . VAL   A  1  1009 ? -20.293 62.683  101.583 1.00 16.75 ? 1007 VAL   A CB    1 
ATOM   7440  C  CG1   . VAL   A  1  1009 ? -20.353 62.103  100.180 1.00 17.53 ? 1007 VAL   A CG1   1 
ATOM   7441  C  CG2   . VAL   A  1  1009 ? -21.021 61.767  102.556 1.00 18.40 ? 1007 VAL   A CG2   1 
ATOM   7442  N  N     . GLN   A  1  1010 ? -18.356 65.067  101.067 1.00 15.53 ? 1008 GLN   A N     1 
ATOM   7443  C  CA    . GLN   A  1  1010 ? -17.470 66.072  100.493 1.00 14.97 ? 1008 GLN   A CA    1 
ATOM   7444  C  C     . GLN   A  1  1010 ? -17.023 66.967  101.639 1.00 15.02 ? 1008 GLN   A C     1 
ATOM   7445  O  O     . GLN   A  1  1010 ? -17.561 68.067  101.811 1.00 18.17 ? 1008 GLN   A O     1 
ATOM   7446  C  CB    . GLN   A  1  1010 ? -18.137 66.902  99.401  1.00 15.37 ? 1008 GLN   A CB    1 
ATOM   7447  C  CG    . GLN   A  1  1010 ? -18.684 66.078  98.240  1.00 16.32 ? 1008 GLN   A CG    1 
ATOM   7448  C  CD    . GLN   A  1  1010 ? -20.176 65.846  98.331  1.00 17.75 ? 1008 GLN   A CD    1 
ATOM   7449  O  OE1   . GLN   A  1  1010 ? -20.925 66.684  98.847  1.00 17.41 ? 1008 GLN   A OE1   1 
ATOM   7450  N  NE2   . GLN   A  1  1010 ? -20.623 64.704  97.821  1.00 17.95 ? 1008 GLN   A NE2   1 
ATOM   7451  N  N     . PRO   A  1  1011 ? -16.063 66.524  102.450 1.00 16.43 ? 1009 PRO   A N     1 
ATOM   7452  C  CA    . PRO   A  1  1011 ? -15.451 67.428  103.435 1.00 17.53 ? 1009 PRO   A CA    1 
ATOM   7453  C  C     . PRO   A  1  1011 ? -15.098 68.721  102.731 1.00 16.30 ? 1009 PRO   A C     1 
ATOM   7454  O  O     . PRO   A  1  1011 ? -14.579 68.720  101.607 1.00 14.66 ? 1009 PRO   A O     1 
ATOM   7455  C  CB    . PRO   A  1  1011 ? -14.198 66.668  103.872 1.00 16.39 ? 1009 PRO   A CB    1 
ATOM   7456  C  CG    . PRO   A  1  1011 ? -14.567 65.230  103.692 1.00 17.59 ? 1009 PRO   A CG    1 
ATOM   7457  C  CD    . PRO   A  1  1011 ? -15.431 65.193  102.448 1.00 15.01 ? 1009 PRO   A CD    1 
ATOM   7458  N  N     . PHE   A  1  1012 ? -15.471 69.832  103.338 1.00 16.06 ? 1010 PHE   A N     1 
ATOM   7459  C  CA    . PHE   A  1  1012 ? -15.551 71.077  102.607 1.00 14.66 ? 1010 PHE   A CA    1 
ATOM   7460  C  C     . PHE   A  1  1012 ? -14.525 72.074  103.099 1.00 15.82 ? 1010 PHE   A C     1 
ATOM   7461  O  O     . PHE   A  1  1012 ? -14.401 72.304  104.304 1.00 16.70 ? 1010 PHE   A O     1 
ATOM   7462  C  CB    . PHE   A  1  1012 ? -16.941 71.691  102.718 1.00 15.63 ? 1010 PHE   A CB    1 
ATOM   7463  C  CG    . PHE   A  1  1012 ? -17.101 72.883  101.860 1.00 14.69 ? 1010 PHE   A CG    1 
ATOM   7464  C  CD1   . PHE   A  1  1012 ? -17.367 72.730  100.511 1.00 17.28 ? 1010 PHE   A CD1   1 
ATOM   7465  C  CD2   . PHE   A  1  1012 ? -16.960 74.163  102.381 1.00 16.91 ? 1010 PHE   A CD2   1 
ATOM   7466  C  CE1   . PHE   A  1  1012 ? -17.484 73.827  99.693  1.00 17.42 ? 1010 PHE   A CE1   1 
ATOM   7467  C  CE2   . PHE   A  1  1012 ? -17.090 75.272  101.561 1.00 17.92 ? 1010 PHE   A CE2   1 
ATOM   7468  C  CZ    . PHE   A  1  1012 ? -17.359 75.104  100.221 1.00 17.12 ? 1010 PHE   A CZ    1 
ATOM   7469  N  N     . GLY   A  1  1013 ? -13.831 72.682  102.171 1.00 15.23 ? 1011 GLY   A N     1 
ATOM   7470  C  CA    . GLY   A  1  1013 ? -12.950 73.780  102.496 1.00 15.76 ? 1011 GLY   A CA    1 
ATOM   7471  C  C     . GLY   A  1  1013 ? -11.854 73.872  101.469 1.00 15.04 ? 1011 GLY   A C     1 
ATOM   7472  O  O     . GLY   A  1  1013 ? -11.440 72.887  100.870 1.00 16.99 ? 1011 GLY   A O     1 
ATOM   7473  N  N     . GLY   A  1  1014 ? -11.366 75.086  101.283 1.00 16.56 ? 1012 GLY   A N     1 
ATOM   7474  C  CA    . GLY   A  1  1014 ? -10.400 75.332  100.245 1.00 19.18 ? 1012 GLY   A CA    1 
ATOM   7475  C  C     . GLY   A  1  1014 ? -9.062  75.827  100.736 1.00 17.36 ? 1012 GLY   A C     1 
ATOM   7476  O  O     . GLY   A  1  1014 ? -8.722  75.748  101.924 1.00 17.93 ? 1012 GLY   A O     1 
ATOM   7477  N  N     . ARG   A  1  1015 ? -8.299  76.356  99.802  1.00 15.84 ? 1013 ARG   A N     1 
ATOM   7478  C  CA    . ARG   A  1  1015 ? -6.911  76.715  100.015 1.00 17.03 ? 1013 ARG   A CA    1 
ATOM   7479  C  C     . ARG   A  1  1015 ? -6.697  78.121  99.487  1.00 16.87 ? 1013 ARG   A C     1 
ATOM   7480  O  O     . ARG   A  1  1015 ? -7.601  78.733  98.913  1.00 16.06 ? 1013 ARG   A O     1 
ATOM   7481  C  CB    . ARG   A  1  1015 ? -5.993  75.744  99.270  1.00 18.07 ? 1013 ARG   A CB    1 
ATOM   7482  C  CG    . ARG   A  1  1015 ? -6.255  75.748  97.767  1.00 18.46 ? 1013 ARG   A CG    1 
ATOM   7483  C  CD    . ARG   A  1  1015 ? -5.134  75.086  96.966  1.00 22.05 ? 1013 ARG   A CD    1 
ATOM   7484  N  NE    . ARG   A  1  1015 ? -3.826  75.266  97.581  1.00 26.31 ? 1013 ARG   A NE    1 
ATOM   7485  C  CZ    . ARG   A  1  1015 ? -3.090  76.364  97.478  1.00 30.02 ? 1013 ARG   A CZ    1 
ATOM   7486  N  NH1   . ARG   A  1  1015 ? -3.497  77.403  96.768  1.00 25.94 ? 1013 ARG   A NH1   1 
ATOM   7487  N  NH2   . ARG   A  1  1015 ? -1.919  76.422  98.113  1.00 25.64 ? 1013 ARG   A NH2   1 
ATOM   7488  N  N     . GLY   A  1  1016 ? -5.471  78.617  99.638  1.00 18.05 ? 1014 GLY   A N     1 
ATOM   7489  C  CA    . GLY   A  1  1016 ? -5.203  79.955  99.157  1.00 17.99 ? 1014 GLY   A CA    1 
ATOM   7490  C  C     . GLY   A  1  1016 ? -6.052  80.955  99.911  1.00 18.22 ? 1014 GLY   A C     1 
ATOM   7491  O  O     . GLY   A  1  1016 ? -6.228  80.865  101.131 1.00 19.14 ? 1014 GLY   A O     1 
ATOM   7492  N  N     . LEU   A  1  1017 ? -6.620  81.903  99.168  1.00 17.31 ? 1015 LEU   A N     1 
ATOM   7493  C  CA    . LEU   A  1  1017 ? -7.502  82.907  99.746  1.00 17.36 ? 1015 LEU   A CA    1 
ATOM   7494  C  C     . LEU   A  1  1017 ? -8.794  82.314  100.276 1.00 18.42 ? 1015 LEU   A C     1 
ATOM   7495  O  O     . LEU   A  1  1017 ? -9.584  83.043  100.882 1.00 18.89 ? 1015 LEU   A O     1 
ATOM   7496  C  CB    . LEU   A  1  1017 ? -7.845  83.964  98.698  1.00 18.98 ? 1015 LEU   A CB    1 
ATOM   7497  C  CG    . LEU   A  1  1017 ? -6.653  84.759  98.178  1.00 19.52 ? 1015 LEU   A CG    1 
ATOM   7498  C  CD1   . LEU   A  1  1017 ? -7.106  85.659  97.033  1.00 20.48 ? 1015 LEU   A CD1   1 
ATOM   7499  C  CD2   . LEU   A  1  1017 ? -6.010  85.573  99.307  1.00 21.51 ? 1015 LEU   A CD2   1 
ATOM   7500  N  N     . SER   A  1  1018 ? -9.030  81.021  100.054 1.00 15.55 ? 1016 SER   A N     1 
ATOM   7501  C  CA    . SER   A  1  1018 ? -10.280 80.388  100.442 1.00 16.89 ? 1016 SER   A CA    1 
ATOM   7502  C  C     . SER   A  1  1018 ? -10.222 79.666  101.775 1.00 15.09 ? 1016 SER   A C     1 
ATOM   7503  O  O     . SER   A  1  1018 ? -11.270 79.237  102.267 1.00 17.93 ? 1016 SER   A O     1 
ATOM   7504  C  CB    . SER   A  1  1018 ? -10.706 79.381  99.376  1.00 15.83 ? 1016 SER   A CB    1 
ATOM   7505  O  OG    . SER   A  1  1018 ? -10.924 80.061  98.165  1.00 16.20 ? 1016 SER   A OG    1 
ATOM   7506  N  N     . GLY   A  1  1019 ? -9.047  79.491  102.360 1.00 16.03 ? 1017 GLY   A N     1 
ATOM   7507  C  CA    . GLY   A  1  1019 ? -9.047  78.801  103.624 1.00 18.64 ? 1017 GLY   A CA    1 
ATOM   7508  C  C     . GLY   A  1  1019 ? -7.679  78.437  104.131 1.00 17.99 ? 1017 GLY   A C     1 
ATOM   7509  O  O     . GLY   A  1  1019 ? -6.721  78.322  103.366 1.00 18.48 ? 1017 GLY   A O     1 
ATOM   7510  N  N     . THR   A  1  1020 ? -7.591  78.278  105.441 1.00 18.35 ? 1018 THR   A N     1 
ATOM   7511  C  CA    . THR   A  1  1020 ? -6.427  77.689  106.069 1.00 17.92 ? 1018 THR   A CA    1 
ATOM   7512  C  C     . THR   A  1  1020 ? -6.560  76.189  106.192 1.00 16.13 ? 1018 THR   A C     1 
ATOM   7513  O  O     . THR   A  1  1020 ? -5.548  75.504  106.358 1.00 18.19 ? 1018 THR   A O     1 
ATOM   7514  C  CB    . THR   A  1  1020 ? -6.288  78.233  107.497 1.00 17.95 ? 1018 THR   A CB    1 
ATOM   7515  O  OG1   . THR   A  1  1020 ? -7.488  77.943  108.242 1.00 17.30 ? 1018 THR   A OG1   1 
ATOM   7516  C  CG2   . THR   A  1  1020 ? -6.060  79.734  107.471 1.00 21.95 ? 1018 THR   A CG2   1 
ATOM   7517  N  N     . GLY   A  1  1021 ? -7.783  75.677  106.171 1.00 17.90 ? 1019 GLY   A N     1 
ATOM   7518  C  CA    . GLY   A  1  1021 ? -8.032  74.329  106.605 1.00 18.69 ? 1019 GLY   A CA    1 
ATOM   7519  C  C     . GLY   A  1  1021 ? -7.804  74.215  108.098 1.00 18.20 ? 1019 GLY   A C     1 
ATOM   7520  O  O     . GLY   A  1  1021 ? -7.504  75.201  108.777 1.00 18.15 ? 1019 GLY   A O     1 
ATOM   7521  N  N     . PRO   A  1  1022 ? -8.009  73.017  108.651 1.00 18.64 ? 1020 PRO   A N     1 
ATOM   7522  C  CA    . PRO   A  1  1022 ? -8.513  71.812  107.986 1.00 18.67 ? 1020 PRO   A CA    1 
ATOM   7523  C  C     . PRO   A  1  1022 ? -9.982  71.943  107.591 1.00 19.13 ? 1020 PRO   A C     1 
ATOM   7524  O  O     . PRO   A  1  1022 ? -10.699 72.846  108.020 1.00 19.73 ? 1020 PRO   A O     1 
ATOM   7525  C  CB    . PRO   A  1  1022 ? -8.327  70.731  109.058 1.00 17.85 ? 1020 PRO   A CB    1 
ATOM   7526  C  CG    . PRO   A  1  1022 ? -8.514  71.471  110.344 1.00 19.98 ? 1020 PRO   A CG    1 
ATOM   7527  C  CD    . PRO   A  1  1022 ? -7.850  72.809  110.103 1.00 17.18 ? 1020 PRO   A CD    1 
ATOM   7528  N  N     . LYS   A  1  1023 ? -10.432 71.018  106.750 1.00 17.56 ? 1021 LYS   A N     1 
ATOM   7529  C  CA    . LYS   A  1  1023 ? -11.792 71.066  106.230 1.00 16.07 ? 1021 LYS   A CA    1 
ATOM   7530  C  C     . LYS   A  1  1023 ? -12.821 70.790  107.311 1.00 16.86 ? 1021 LYS   A C     1 
ATOM   7531  O  O     . LYS   A  1  1023 ? -12.724 69.803  108.045 1.00 17.61 ? 1021 LYS   A O     1 
ATOM   7532  C  CB    . LYS   A  1  1023 ? -11.966 70.003  105.155 1.00 16.49 ? 1021 LYS   A CB    1 
ATOM   7533  C  CG    . LYS   A  1  1023 ? -11.319 70.317  103.820 1.00 15.94 ? 1021 LYS   A CG    1 
ATOM   7534  C  CD    . LYS   A  1  1023 ? -11.491 69.119  102.909 1.00 15.96 ? 1021 LYS   A CD    1 
ATOM   7535  C  CE    . LYS   A  1  1023 ? -11.101 69.415  101.465 1.00 16.67 ? 1021 LYS   A CE    1 
ATOM   7536  N  NZ    . LYS   A  1  1023 ? -12.147 70.194  100.771 1.00 16.07 ? 1021 LYS   A NZ    1 
ATOM   7537  N  N     . ALA   A  1  1024 ? -13.839 71.643  107.364 1.00 17.90 ? 1022 ALA   A N     1 
ATOM   7538  C  CA    . ALA   A  1  1024 ? -15.047 71.302  108.091 1.00 19.44 ? 1022 ALA   A CA    1 
ATOM   7539  C  C     . ALA   A  1  1024 ? -15.670 70.052  107.487 1.00 17.99 ? 1022 ALA   A C     1 
ATOM   7540  O  O     . ALA   A  1  1024 ? -15.613 69.824  106.271 1.00 18.16 ? 1022 ALA   A O     1 
ATOM   7541  C  CB    . ALA   A  1  1024 ? -16.044 72.459  108.025 1.00 18.14 ? 1022 ALA   A CB    1 
ATOM   7542  N  N     . GLY   A  1  1025 ? -16.266 69.230  108.347 1.00 17.40 ? 1023 GLY   A N     1 
ATOM   7543  C  CA    . GLY   A  1  1025 ? -16.915 68.033  107.861 1.00 17.16 ? 1023 GLY   A CA    1 
ATOM   7544  C  C     . GLY   A  1  1025 ? -15.948 66.986  107.385 1.00 17.02 ? 1023 GLY   A C     1 
ATOM   7545  O  O     . GLY   A  1  1025 ? -16.335 66.074  106.642 1.00 17.51 ? 1023 GLY   A O     1 
ATOM   7546  N  N     . GLY   A  1  1026 ? -14.686 67.113  107.785 1.00 15.92 ? 1024 GLY   A N     1 
ATOM   7547  C  CA    . GLY   A  1  1026 ? -13.662 66.158  107.461 1.00 15.85 ? 1024 GLY   A CA    1 
ATOM   7548  C  C     . GLY   A  1  1026 ? -12.922 65.708  108.705 1.00 17.04 ? 1024 GLY   A C     1 
ATOM   7549  O  O     . GLY   A  1  1026 ? -13.101 66.234  109.809 1.00 16.55 ? 1024 GLY   A O     1 
ATOM   7550  N  N     . PRO   A  1  1027 ? -12.039 64.726  108.524 1.00 15.74 ? 1025 PRO   A N     1 
ATOM   7551  C  CA    . PRO   A  1  1027 ? -11.480 64.004  109.668 1.00 17.09 ? 1025 PRO   A CA    1 
ATOM   7552  C  C     . PRO   A  1  1027 ? -10.318 64.706  110.348 1.00 14.60 ? 1025 PRO   A C     1 
ATOM   7553  O  O     . PRO   A  1  1027 ? -9.890  64.247  111.408 1.00 16.52 ? 1025 PRO   A O     1 
ATOM   7554  C  CB    . PRO   A  1  1027 ? -11.029 62.680  109.043 1.00 17.50 ? 1025 PRO   A CB    1 
ATOM   7555  C  CG    . PRO   A  1  1027 ? -10.723 63.045  107.607 1.00 17.97 ? 1025 PRO   A CG    1 
ATOM   7556  C  CD    . PRO   A  1  1027 ? -11.741 64.080  107.235 1.00 15.95 ? 1025 PRO   A CD    1 
ATOM   7557  N  N     . LEU   A  1  1028 ? -9.786  65.776  109.772 1.00 15.51 ? 1026 LEU   A N     1 
ATOM   7558  C  CA    . LEU   A  1  1028 ? -8.698  66.506  110.413 1.00 16.27 ? 1026 LEU   A CA    1 
ATOM   7559  C  C     . LEU   A  1  1028 ? -9.188  67.654  111.271 1.00 16.59 ? 1026 LEU   A C     1 
ATOM   7560  O  O     . LEU   A  1  1028 ? -8.389  68.278  111.974 1.00 18.35 ? 1026 LEU   A O     1 
ATOM   7561  C  CB    . LEU   A  1  1028 ? -7.730  67.055  109.362 1.00 16.87 ? 1026 LEU   A CB    1 
ATOM   7562  C  CG    . LEU   A  1  1028 ? -6.952  66.007  108.572 1.00 20.11 ? 1026 LEU   A CG    1 
ATOM   7563  C  CD1   . LEU   A  1  1028 ? -6.127  66.700  107.510 1.00 19.22 ? 1026 LEU   A CD1   1 
ATOM   7564  C  CD2   . LEU   A  1  1028 ? -6.076  65.211  109.489 1.00 29.97 ? 1026 LEU   A CD2   1 
ATOM   7565  N  N     . TYR   A  1  1029 ? -10.492 67.916  111.259 1.00 16.32 ? 1027 TYR   A N     1 
ATOM   7566  C  CA    . TYR   A  1  1029 ? -11.025 69.132  111.858 1.00 17.11 ? 1027 TYR   A CA    1 
ATOM   7567  C  C     . TYR   A  1  1029 ? -10.858 69.127  113.366 1.00 15.88 ? 1027 TYR   A C     1 
ATOM   7568  O  O     . TYR   A  1  1029 ? -10.335 70.088  113.945 1.00 18.04 ? 1027 TYR   A O     1 
ATOM   7569  C  CB    . TYR   A  1  1029 ? -12.493 69.206  111.504 1.00 17.62 ? 1027 TYR   A CB    1 
ATOM   7570  C  CG    . TYR   A  1  1029 ? -13.136 70.549  111.585 1.00 17.59 ? 1027 TYR   A CG    1 
ATOM   7571  C  CD1   . TYR   A  1  1029 ? -12.753 71.578  110.743 1.00 17.73 ? 1027 TYR   A CD1   1 
ATOM   7572  C  CD2   . TYR   A  1  1029 ? -14.185 70.767  112.460 1.00 16.62 ? 1027 TYR   A CD2   1 
ATOM   7573  C  CE1   . TYR   A  1  1029 ? -13.395 72.799  110.776 1.00 18.00 ? 1027 TYR   A CE1   1 
ATOM   7574  C  CE2   . TYR   A  1  1029 ? -14.828 71.979  112.502 1.00 17.82 ? 1027 TYR   A CE2   1 
ATOM   7575  C  CZ    . TYR   A  1  1029 ? -14.434 72.989  111.658 1.00 17.66 ? 1027 TYR   A CZ    1 
ATOM   7576  O  OH    . TYR   A  1  1029 ? -15.115 74.187  111.708 1.00 19.60 ? 1027 TYR   A OH    1 
ATOM   7577  N  N     . LEU   A  1  1030 ? -11.334 68.070  114.028 1.00 17.55 ? 1028 LEU   A N     1 
ATOM   7578  C  CA    . LEU   A  1  1030 ? -11.298 68.078  115.488 1.00 16.72 ? 1028 LEU   A CA    1 
ATOM   7579  C  C     . LEU   A  1  1030 ? -9.877  68.172  116.006 1.00 17.72 ? 1028 LEU   A C     1 
ATOM   7580  O  O     . LEU   A  1  1030 ? -9.647  68.745  117.075 1.00 19.65 ? 1028 LEU   A O     1 
ATOM   7581  C  CB    . LEU   A  1  1030 ? -11.967 66.834  116.062 1.00 19.27 ? 1028 LEU   A CB    1 
ATOM   7582  C  CG    . LEU   A  1  1030 ? -13.447 66.647  115.761 1.00 19.64 ? 1028 LEU   A CG    1 
ATOM   7583  C  CD1   . LEU   A  1  1030 ? -13.945 65.388  116.456 1.00 24.18 ? 1028 LEU   A CD1   1 
ATOM   7584  C  CD2   . LEU   A  1  1030 ? -14.255 67.860  116.198 1.00 21.06 ? 1028 LEU   A CD2   1 
ATOM   7585  N  N     . GLY   A  1  1031 ? -8.912  67.620  115.270 1.00 18.07 ? 1029 GLY   A N     1 
ATOM   7586  C  CA    . GLY   A  1  1031 ? -7.540  67.619  115.737 1.00 19.34 ? 1029 GLY   A CA    1 
ATOM   7587  C  C     . GLY   A  1  1031 ? -6.930  68.995  115.856 1.00 19.86 ? 1029 GLY   A C     1 
ATOM   7588  O  O     . GLY   A  1  1031 ? -5.948  69.166  116.585 1.00 21.76 ? 1029 GLY   A O     1 
ATOM   7589  N  N     . ARG   A  1  1032 ? -7.484  69.982  115.157 1.00 17.51 ? 1030 ARG   A N     1 
ATOM   7590  C  CA    . ARG   A  1  1032 ? -7.017  71.353  115.272 1.00 17.86 ? 1030 ARG   A CA    1 
ATOM   7591  C  C     . ARG   A  1  1032 ? -7.496  72.020  116.555 1.00 19.86 ? 1030 ARG   A C     1 
ATOM   7592  O  O     . ARG   A  1  1032 ? -6.965  73.069  116.940 1.00 21.85 ? 1030 ARG   A O     1 
ATOM   7593  C  CB    . ARG   A  1  1032 ? -7.517  72.149  114.066 1.00 20.98 ? 1030 ARG   A CB    1 
ATOM   7594  C  CG    . ARG   A  1  1032 ? -6.875  73.511  113.895 1.00 17.94 ? 1030 ARG   A CG    1 
ATOM   7595  C  CD    . ARG   A  1  1032 ? -5.420  73.385  113.506 1.00 18.92 ? 1030 ARG   A CD    1 
ATOM   7596  N  NE    . ARG   A  1  1032 ? -4.917  74.679  113.071 1.00 20.68 ? 1030 ARG   A NE    1 
ATOM   7597  C  CZ    . ARG   A  1  1032 ? -3.879  75.306  113.607 1.00 22.66 ? 1030 ARG   A CZ    1 
ATOM   7598  N  NH1   . ARG   A  1  1032 ? -3.195  74.782  114.611 1.00 24.80 ? 1030 ARG   A NH1   1 
ATOM   7599  N  NH2   . ARG   A  1  1032 ? -3.527  76.496  113.128 1.00 22.68 ? 1030 ARG   A NH2   1 
ATOM   7600  N  N     . LEU   A  1  1033 ? -8.480  71.433  117.226 1.00 18.30 ? 1031 LEU   A N     1 
ATOM   7601  C  CA    . LEU   A  1  1033 ? -9.125  72.054  118.367 1.00 18.29 ? 1031 LEU   A CA    1 
ATOM   7602  C  C     . LEU   A  1  1033 ? -8.658  71.462  119.682 1.00 20.77 ? 1031 LEU   A C     1 
ATOM   7603  O  O     . LEU   A  1  1033 ? -9.270  71.712  120.719 1.00 21.80 ? 1031 LEU   A O     1 
ATOM   7604  C  CB    . LEU   A  1  1033 ? -10.643 71.924  118.229 1.00 19.04 ? 1031 LEU   A CB    1 
ATOM   7605  C  CG    . LEU   A  1  1033 ? -11.142 72.339  116.844 1.00 20.60 ? 1031 LEU   A CG    1 
ATOM   7606  C  CD1   . LEU   A  1  1033 ? -12.637 72.106  116.723 1.00 19.87 ? 1031 LEU   A CD1   1 
ATOM   7607  C  CD2   . LEU   A  1  1033 ? -10.794 73.791  116.570 1.00 22.45 ? 1031 LEU   A CD2   1 
ATOM   7608  N  N     . VAL   A  1  1034 ? -7.595  70.664  119.647 1.00 21.15 ? 1032 VAL   A N     1 
ATOM   7609  C  CA    . VAL   A  1  1034 ? -6.967  70.117  120.834 1.00 21.49 ? 1032 VAL   A CA    1 
ATOM   7610  C  C     . VAL   A  1  1034 ? -5.483  70.426  120.742 1.00 22.70 ? 1032 VAL   A C     1 
ATOM   7611  O  O     . VAL   A  1  1034 ? -4.959  70.760  119.679 1.00 22.45 ? 1032 VAL   A O     1 
ATOM   7612  C  CB    . VAL   A  1  1034 ? -7.213  68.602  120.985 1.00 20.16 ? 1032 VAL   A CB    1 
ATOM   7613  C  CG1   . VAL   A  1  1034 ? -8.688  68.333  121.296 1.00 22.37 ? 1032 VAL   A CG1   1 
ATOM   7614  C  CG2   . VAL   A  1  1034 ? -6.771  67.861  119.716 1.00 21.30 ? 1032 VAL   A CG2   1 
ATOM   7615  N  N     . THR   A  1  1035 ? -4.803  70.327  121.884 1.00 23.19 ? 1033 THR   A N     1 
ATOM   7616  C  CA    . THR   A  1  1035 ? -3.392  70.690  121.910 1.00 23.61 ? 1033 THR   A CA    1 
ATOM   7617  C  C     . THR   A  1  1035 ? -2.508  69.624  121.281 1.00 29.40 ? 1033 THR   A C     1 
ATOM   7618  O  O     . THR   A  1  1035 ? -1.459  69.954  120.721 1.00 32.52 ? 1033 THR   A O     1 
ATOM   7619  C  CB    . THR   A  1  1035 ? -2.948  70.984  123.340 1.00 28.18 ? 1033 THR   A CB    1 
ATOM   7620  O  OG1   . THR   A  1  1035 ? -3.236  69.856  124.170 1.00 35.09 ? 1033 THR   A OG1   1 
ATOM   7621  C  CG2   . THR   A  1  1035 ? -3.684  72.188  123.870 1.00 26.87 ? 1033 THR   A CG2   1 
ATOM   7622  N  N     . THR   A  1  1036 ? -2.902  68.357  121.367 1.00 23.11 ? 1034 THR   A N     1 
ATOM   7623  C  CA    . THR   A  1  1036 ? -2.179  67.251  120.750 1.00 25.90 ? 1034 THR   A CA    1 
ATOM   7624  C  C     . THR   A  1  1036 ? -3.171  66.553  119.837 1.00 24.70 ? 1034 THR   A C     1 
ATOM   7625  O  O     . THR   A  1  1036 ? -4.146  65.965  120.313 1.00 26.16 ? 1034 THR   A O     1 
ATOM   7626  C  CB    . THR   A  1  1036 ? -1.667  66.286  121.817 1.00 31.89 ? 1034 THR   A CB    1 
ATOM   7627  O  OG1   . THR   A  1  1036 ? -0.780  66.980  122.702 1.00 33.56 ? 1034 THR   A OG1   1 
ATOM   7628  C  CG2   . THR   A  1  1036 ? -0.919  65.129  121.165 1.00 32.30 ? 1034 THR   A CG2   1 
ATOM   7629  N  N     . ALA   A  1  1037 ? -2.928  66.625  118.536 1.00 23.43 ? 1035 ALA   A N     1 
ATOM   7630  C  CA    . ALA   A  1  1037 ? -3.900  66.119  117.579 1.00 24.97 ? 1035 ALA   A CA    1 
ATOM   7631  C  C     . ALA   A  1  1037 ? -3.927  64.592  117.614 1.00 22.62 ? 1035 ALA   A C     1 
ATOM   7632  O  O     . ALA   A  1  1037 ? -2.875  63.952  117.674 1.00 23.23 ? 1035 ALA   A O     1 
ATOM   7633  C  CB    . ALA   A  1  1037 ? -3.567  66.605  116.169 1.00 26.09 ? 1035 ALA   A CB    1 
ATOM   7634  N  N     . PRO   A  1  1038 ? -5.106  63.987  117.602 1.00 21.70 ? 1036 PRO   A N     1 
ATOM   7635  C  CA    . PRO   A  1  1038 ? -5.198  62.529  117.512 1.00 20.90 ? 1036 PRO   A CA    1 
ATOM   7636  C  C     . PRO   A  1  1038 ? -4.934  62.077  116.083 1.00 21.36 ? 1036 PRO   A C     1 
ATOM   7637  O  O     . PRO   A  1  1038 ? -4.836  62.874  115.157 1.00 20.55 ? 1036 PRO   A O     1 
ATOM   7638  C  CB    . PRO   A  1  1038 ? -6.658  62.262  117.879 1.00 25.51 ? 1036 PRO   A CB    1 
ATOM   7639  C  CG    . PRO   A  1  1038 ? -7.376  63.463  117.343 1.00 24.15 ? 1036 PRO   A CG    1 
ATOM   7640  C  CD    . PRO   A  1  1038 ? -6.434  64.628  117.592 1.00 22.40 ? 1036 PRO   A CD    1 
ATOM   7641  N  N     . VAL   A  1  1039 ? -4.824  60.764  115.927 1.00 21.29 ? 1037 VAL   A N     1 
ATOM   7642  C  CA    . VAL   A  1  1039 ? -4.727  60.159  114.606 1.00 19.89 ? 1037 VAL   A CA    1 
ATOM   7643  C  C     . VAL   A  1  1039 ? -6.140  59.993  114.072 1.00 18.87 ? 1037 VAL   A C     1 
ATOM   7644  O  O     . VAL   A  1  1039 ? -6.912  59.195  114.613 1.00 20.20 ? 1037 VAL   A O     1 
ATOM   7645  C  CB    . VAL   A  1  1039 ? -3.998  58.810  114.666 1.00 20.64 ? 1037 VAL   A CB    1 
ATOM   7646  C  CG1   . VAL   A  1  1039 ? -3.932  58.201  113.284 1.00 22.18 ? 1037 VAL   A CG1   1 
ATOM   7647  C  CG2   . VAL   A  1  1039 ? -2.596  58.986  115.260 1.00 24.51 ? 1037 VAL   A CG2   1 
ATOM   7648  N  N     . PRO   A  1  1040 ? -6.515  60.695  113.011 1.00 18.86 ? 1038 PRO   A N     1 
ATOM   7649  C  CA    . PRO   A  1  1040 ? -7.869  60.567  112.503 1.00 19.62 ? 1038 PRO   A CA    1 
ATOM   7650  C  C     . PRO   A  1  1040 ? -8.119  59.169  111.968 1.00 17.60 ? 1038 PRO   A C     1 
ATOM   7651  O  O     . PRO   A  1  1040 ? -7.179  58.453  111.582 1.00 17.48 ? 1038 PRO   A O     1 
ATOM   7652  C  CB    . PRO   A  1  1040 ? -7.926  61.604  111.370 1.00 20.03 ? 1038 PRO   A CB    1 
ATOM   7653  C  CG    . PRO   A  1  1040 ? -6.837  62.552  111.666 1.00 21.77 ? 1038 PRO   A CG    1 
ATOM   7654  C  CD    . PRO   A  1  1040 ? -5.752  61.734  112.305 1.00 21.01 ? 1038 PRO   A CD    1 
ATOM   7655  N  N     . PRO   A  1  1041 ? -9.376  58.745  111.917 1.00 17.47 ? 1039 PRO   A N     1 
ATOM   7656  C  CA    . PRO   A  1  1041 ? -9.691  57.473  111.268 1.00 16.52 ? 1039 PRO   A CA    1 
ATOM   7657  C  C     . PRO   A  1  1041 ? -9.175  57.481  109.840 1.00 17.64 ? 1039 PRO   A C     1 
ATOM   7658  O  O     . PRO   A  1  1041 ? -9.223  58.505  109.151 1.00 18.17 ? 1039 PRO   A O     1 
ATOM   7659  C  CB    . PRO   A  1  1041 ? -11.226 57.429  111.294 1.00 19.18 ? 1039 PRO   A CB    1 
ATOM   7660  C  CG    . PRO   A  1  1041 ? -11.623 58.409  112.349 1.00 23.48 ? 1039 PRO   A CG    1 
ATOM   7661  C  CD    . PRO   A  1  1041 ? -10.586 59.476  112.338 1.00 20.68 ? 1039 PRO   A CD    1 
ATOM   7662  N  N     . GLN   A  1  1042 ? -8.643  56.336  109.416 1.00 16.60 ? 1040 GLN   A N     1 
ATOM   7663  C  CA    . GLN   A  1  1042 ? -8.182  56.088  108.053 1.00 17.01 ? 1040 GLN   A CA    1 
ATOM   7664  C  C     . GLN   A  1  1042 ? -7.009  56.960  107.634 1.00 17.28 ? 1040 GLN   A C     1 
ATOM   7665  O  O     . GLN   A  1  1042 ? -6.639  56.952  106.460 1.00 17.80 ? 1040 GLN   A O     1 
ATOM   7666  C  CB    . GLN   A  1  1042 ? -9.313  56.215  107.024 1.00 19.47 ? 1040 GLN   A CB    1 
ATOM   7667  C  CG    . GLN   A  1  1042 ? -10.538 55.381  107.340 1.00 26.46 ? 1040 GLN   A CG    1 
ATOM   7668  C  CD    . GLN   A  1  1042 ? -11.606 55.526  106.267 1.00 30.13 ? 1040 GLN   A CD    1 
ATOM   7669  O  OE1   . GLN   A  1  1042 ? -11.775 54.650  105.424 1.00 42.52 ? 1040 GLN   A OE1   1 
ATOM   7670  N  NE2   . GLN   A  1  1042 ? -12.310 56.651  106.281 1.00 35.15 ? 1040 GLN   A NE2   1 
ATOM   7671  N  N     . HIS   A  1  1043 ? -6.400  57.693  108.564 1.00 16.13 ? 1041 HIS   A N     1 
ATOM   7672  C  CA    . HIS   A  1  1043 ? -5.393  58.701  108.241 1.00 15.37 ? 1041 HIS   A CA    1 
ATOM   7673  C  C     . HIS   A  1  1043 ? -4.008  58.069  108.285 1.00 16.13 ? 1041 HIS   A C     1 
ATOM   7674  O  O     . HIS   A  1  1043 ? -3.404  57.936  109.354 1.00 16.64 ? 1041 HIS   A O     1 
ATOM   7675  C  CB    . HIS   A  1  1043 ? -5.498  59.863  109.217 1.00 16.95 ? 1041 HIS   A CB    1 
ATOM   7676  C  CG    . HIS   A  1  1043 ? -4.537  60.976  108.948 1.00 17.89 ? 1041 HIS   A CG    1 
ATOM   7677  N  ND1   . HIS   A  1  1043 ? -4.828  62.032  108.113 1.00 16.60 ? 1041 HIS   A ND1   1 
ATOM   7678  C  CD2   . HIS   A  1  1043 ? -3.296  61.214  109.437 1.00 16.61 ? 1041 HIS   A CD2   1 
ATOM   7679  C  CE1   . HIS   A  1  1043 ? -3.803  62.866  108.086 1.00 18.18 ? 1041 HIS   A CE1   1 
ATOM   7680  N  NE2   . HIS   A  1  1043 ? -2.858  62.390  108.879 1.00 17.54 ? 1041 HIS   A NE2   1 
ATOM   7681  N  N     . SER   A  1  1044 ? -3.524  57.652  107.123 1.00 16.42 ? 1042 SER   A N     1 
ATOM   7682  C  CA    . SER   A  1  1044 ? -2.173  57.124  106.978 1.00 14.85 ? 1042 SER   A CA    1 
ATOM   7683  C  C     . SER   A  1  1044 ? -1.897  57.055  105.487 1.00 14.95 ? 1042 SER   A C     1 
ATOM   7684  O  O     . SER   A  1  1044 ? -2.796  57.222  104.660 1.00 16.94 ? 1042 SER   A O     1 
ATOM   7685  C  CB    . SER   A  1  1044 ? -2.027  55.737  107.606 1.00 17.20 ? 1042 SER   A CB    1 
ATOM   7686  O  OG    . SER   A  1  1044 ? -2.820  54.794  106.912 1.00 16.97 ? 1042 SER   A OG    1 
ATOM   7687  N  N     . SER   A  1  1045 ? -0.637  56.800  105.154 1.00 15.12 ? 1043 SER   A N     1 
ATOM   7688  C  CA    . SER   A  1  1045 ? -0.272  56.600  103.766 1.00 15.03 ? 1043 SER   A CA    1 
ATOM   7689  C  C     . SER   A  1  1045 ? 0.938   55.692  103.716 1.00 14.59 ? 1043 SER   A C     1 
ATOM   7690  O  O     . SER   A  1  1045 ? 1.872   55.850  104.501 1.00 16.10 ? 1043 SER   A O     1 
ATOM   7691  C  CB    . SER   A  1  1045 ? 0.098   57.933  103.119 1.00 16.57 ? 1043 SER   A CB    1 
ATOM   7692  O  OG    . SER   A  1  1045 ? 0.544   57.711  101.791 1.00 17.74 ? 1043 SER   A OG    1 
ATOM   7693  N  N     . VAL   A  1  1046 ? 0.917   54.740  102.780 1.00 15.64 ? 1044 VAL   A N     1 
ATOM   7694  C  CA    . VAL   A  1  1046 ? 2.078   53.876  102.591 1.00 16.59 ? 1044 VAL   A CA    1 
ATOM   7695  C  C     . VAL   A  1  1046 ? 3.140   54.518  101.731 1.00 14.74 ? 1044 VAL   A C     1 
ATOM   7696  O  O     . VAL   A  1  1046 ? 4.217   53.938  101.561 1.00 18.69 ? 1044 VAL   A O     1 
ATOM   7697  C  CB    . VAL   A  1  1046 ? 1.736   52.503  101.988 1.00 19.43 ? 1044 VAL   A CB    1 
ATOM   7698  C  CG1   . VAL   A  1  1046 ? 0.809   51.754  102.927 1.00 19.68 ? 1044 VAL   A CG1   1 
ATOM   7699  C  CG2   . VAL   A  1  1046 ? 1.126   52.661  100.612 1.00 18.47 ? 1044 VAL   A CG2   1 
ATOM   7700  N  N     . HIS   A  1  1047 ? 2.882   55.699  101.203 1.00 14.46 ? 1045 HIS   A N     1 
ATOM   7701  C  CA    . HIS   A  1  1047 ? 3.806   56.338  100.286 1.00 16.77 ? 1045 HIS   A CA    1 
ATOM   7702  C  C     . HIS   A  1  1047 ? 4.749   57.258  101.032 1.00 16.01 ? 1045 HIS   A C     1 
ATOM   7703  O  O     . HIS   A  1  1047 ? 4.365   57.921  102.000 1.00 17.17 ? 1045 HIS   A O     1 
ATOM   7704  C  CB    . HIS   A  1  1047 ? 3.003   57.090  99.238  1.00 19.71 ? 1045 HIS   A CB    1 
ATOM   7705  C  CG    . HIS   A  1  1047 ? 2.028   56.205  98.533  1.00 22.52 ? 1045 HIS   A CG    1 
ATOM   7706  N  ND1   . HIS   A  1  1047 ? 2.425   55.224  97.647  1.00 26.35 ? 1045 HIS   A ND1   1 
ATOM   7707  C  CD2   . HIS   A  1  1047 ? 0.682   56.105  98.629  1.00 25.43 ? 1045 HIS   A CD2   1 
ATOM   7708  C  CE1   . HIS   A  1  1047 ? 1.359   54.586  97.198  1.00 25.19 ? 1045 HIS   A CE1   1 
ATOM   7709  N  NE2   . HIS   A  1  1047 ? 0.290   55.097  97.782  1.00 26.61 ? 1045 HIS   A NE2   1 
ATOM   7710  N  N     . THR   A  1  1048 ? 5.998   57.270  100.596 1.00 16.27 ? 1046 THR   A N     1 
ATOM   7711  C  CA    . THR   A  1  1048 ? 7.018   58.107  101.199 1.00 18.56 ? 1046 THR   A CA    1 
ATOM   7712  C  C     . THR   A  1  1048 ? 7.509   59.077  100.143 1.00 16.84 ? 1046 THR   A C     1 
ATOM   7713  O  O     . THR   A  1  1048 ? 7.840   58.669  99.027  1.00 17.59 ? 1046 THR   A O     1 
ATOM   7714  C  CB    . THR   A  1  1048 ? 8.175   57.265  101.713 1.00 16.79 ? 1046 THR   A CB    1 
ATOM   7715  O  OG1   . THR   A  1  1048 ? 7.664   56.228  102.554 1.00 19.23 ? 1046 THR   A OG1   1 
ATOM   7716  C  CG2   . THR   A  1  1048 ? 9.114   58.141  102.531 1.00 18.39 ? 1046 THR   A CG2   1 
ATOM   7717  N  N     . ASP   A  1  1049 ? 7.533   60.346  100.491 1.00 16.99 ? 1047 ASP   A N     1 
ATOM   7718  C  CA    . ASP   A  1  1049 ? 7.964   61.345  99.541  1.00 15.68 ? 1047 ASP   A CA    1 
ATOM   7719  C  C     . ASP   A  1  1049 ? 9.424   61.087  99.167  1.00 16.59 ? 1047 ASP   A C     1 
ATOM   7720  O  O     . ASP   A  1  1049 ? 10.265  60.888  100.056 1.00 16.08 ? 1047 ASP   A O     1 
ATOM   7721  C  CB    . ASP   A  1  1049 ? 7.796   62.731  100.153 1.00 15.49 ? 1047 ASP   A CB    1 
ATOM   7722  C  CG    . ASP   A  1  1049 ? 8.220   63.821  99.208  1.00 17.96 ? 1047 ASP   A CG    1 
ATOM   7723  O  OD1   . ASP   A  1  1049 ? 9.444   64.049  99.087  1.00 16.99 ? 1047 ASP   A OD1   1 
ATOM   7724  O  OD2   . ASP   A  1  1049 ? 7.341   64.410  98.546  1.00 17.40 ? 1047 ASP   A OD2   1 
ATOM   7725  N  N     . PRO   A  1  1050 ? 9.756   61.047  97.874  1.00 14.74 ? 1048 PRO   A N     1 
ATOM   7726  C  CA    . PRO   A  1  1050 ? 11.119  60.669  97.481  1.00 15.94 ? 1048 PRO   A CA    1 
ATOM   7727  C  C     . PRO   A  1  1050 ? 12.136  61.755  97.754  1.00 15.59 ? 1048 PRO   A C     1 
ATOM   7728  O  O     . PRO   A  1  1050 ? 13.329  61.458  97.919  1.00 15.95 ? 1048 PRO   A O     1 
ATOM   7729  C  CB    . PRO   A  1  1050 ? 10.980  60.383  95.977  1.00 17.81 ? 1048 PRO   A CB    1 
ATOM   7730  C  CG    . PRO   A  1  1050 ? 9.830   61.247  95.549  1.00 17.90 ? 1048 PRO   A CG    1 
ATOM   7731  C  CD    . PRO   A  1  1050 ? 8.869   61.214  96.710  1.00 16.05 ? 1048 PRO   A CD    1 
ATOM   7732  N  N     . VAL   A  1  1051 ? 11.703  63.012  97.781  1.00 15.27 ? 1049 VAL   A N     1 
ATOM   7733  C  CA    . VAL   A  1  1051 ? 12.618  64.091  98.114  1.00 15.27 ? 1049 VAL   A CA    1 
ATOM   7734  C  C     . VAL   A  1  1051 ? 12.930  64.054  99.595  1.00 15.27 ? 1049 VAL   A C     1 
ATOM   7735  O  O     . VAL   A  1  1051 ? 14.072  64.278  100.005 1.00 17.01 ? 1049 VAL   A O     1 
ATOM   7736  C  CB    . VAL   A  1  1051 ? 12.052  65.445  97.662  1.00 15.88 ? 1049 VAL   A CB    1 
ATOM   7737  C  CG1   . VAL   A  1  1051 ? 13.035  66.559  97.970  1.00 19.85 ? 1049 VAL   A CG1   1 
ATOM   7738  C  CG2   . VAL   A  1  1051 ? 11.749  65.405  96.167  1.00 17.70 ? 1049 VAL   A CG2   1 
ATOM   7739  N  N     . LEU   A  1  1052 ? 11.922  63.753  100.421 1.00 14.60 ? 1050 LEU   A N     1 
ATOM   7740  C  CA    . LEU   A  1  1052 ? 12.189  63.469  101.824 1.00 15.14 ? 1050 LEU   A CA    1 
ATOM   7741  C  C     . LEU   A  1  1052 ? 13.256  62.391  101.955 1.00 16.73 ? 1050 LEU   A C     1 
ATOM   7742  O  O     . LEU   A  1  1052 ? 14.214  62.543  102.715 1.00 15.05 ? 1050 LEU   A O     1 
ATOM   7743  C  CB    . LEU   A  1  1052 ? 10.897  63.050  102.523 1.00 15.22 ? 1050 LEU   A CB    1 
ATOM   7744  C  CG    . LEU   A  1  1052 ? 10.965  62.648  104.005 1.00 14.87 ? 1050 LEU   A CG    1 
ATOM   7745  C  CD1   . LEU   A  1  1052 ? 11.525  61.221  104.242 1.00 16.16 ? 1050 LEU   A CD1   1 
ATOM   7746  C  CD2   . LEU   A  1  1052 ? 11.737  63.693  104.813 1.00 15.99 ? 1050 LEU   A CD2   1 
ATOM   7747  N  N     . LEU   A  1  1053 ? 13.101  61.282  101.222 1.00 15.17 ? 1051 LEU   A N     1 
ATOM   7748  C  CA    . LEU   A  1  1053 ? 14.080  60.205  101.320 1.00 15.42 ? 1051 LEU   A CA    1 
ATOM   7749  C  C     . LEU   A  1  1053 ? 15.459  60.682  100.898 1.00 15.30 ? 1051 LEU   A C     1 
ATOM   7750  O  O     . LEU   A  1  1053 ? 16.455  60.361  101.547 1.00 16.42 ? 1051 LEU   A O     1 
ATOM   7751  C  CB    . LEU   A  1  1053 ? 13.645  59.001  100.481 1.00 18.07 ? 1051 LEU   A CB    1 
ATOM   7752  C  CG    . LEU   A  1  1053 ? 12.425  58.253  101.021 1.00 17.02 ? 1051 LEU   A CG    1 
ATOM   7753  C  CD1   . LEU   A  1  1053 ? 11.948  57.215  100.003 1.00 18.65 ? 1051 LEU   A CD1   1 
ATOM   7754  C  CD2   . LEU   A  1  1053 ? 12.738  57.595  102.339 1.00 19.16 ? 1051 LEU   A CD2   1 
ATOM   7755  N  N     . ASP   A  1  1054 ? 15.537  61.460  99.820  1.00 15.05 ? 1052 ASP   A N     1 
ATOM   7756  C  CA    . ASP   A  1  1054 ? 16.829  61.990  99.400  1.00 17.06 ? 1052 ASP   A CA    1 
ATOM   7757  C  C     . ASP   A  1  1054 ? 17.414  62.891  100.468 1.00 15.42 ? 1052 ASP   A C     1 
ATOM   7758  O  O     . ASP   A  1  1054 ? 18.621  62.872  100.706 1.00 16.44 ? 1052 ASP   A O     1 
ATOM   7759  C  CB    . ASP   A  1  1054 ? 16.690  62.764  98.093  1.00 15.77 ? 1052 ASP   A CB    1 
ATOM   7760  C  CG    . ASP   A  1  1054 ? 16.423  61.864  96.911  1.00 20.30 ? 1052 ASP   A CG    1 
ATOM   7761  O  OD1   . ASP   A  1  1054 ? 16.553  60.629  97.068  1.00 18.96 ? 1052 ASP   A OD1   1 
ATOM   7762  O  OD2   . ASP   A  1  1054 ? 16.085  62.411  95.842  1.00 24.33 ? 1052 ASP   A OD2   1 
ATOM   7763  N  N     . PHE   A  1  1055 ? 16.571  63.692  101.115 1.00 14.46 ? 1053 PHE   A N     1 
ATOM   7764  C  CA    . PHE   A  1  1055 ? 17.053  64.573  102.169 1.00 15.57 ? 1053 PHE   A CA    1 
ATOM   7765  C  C     . PHE   A  1  1055 ? 17.562  63.774  103.356 1.00 15.60 ? 1053 PHE   A C     1 
ATOM   7766  O  O     . PHE   A  1  1055 ? 18.608  64.103  103.932 1.00 15.97 ? 1053 PHE   A O     1 
ATOM   7767  C  CB    . PHE   A  1  1055 ? 15.925  65.509  102.588 1.00 15.61 ? 1053 PHE   A CB    1 
ATOM   7768  C  CG    . PHE   A  1  1055 ? 16.309  66.476  103.663 1.00 16.04 ? 1053 PHE   A CG    1 
ATOM   7769  C  CD1   . PHE   A  1  1055 ? 17.367  67.349  103.487 1.00 18.46 ? 1053 PHE   A CD1   1 
ATOM   7770  C  CD2   . PHE   A  1  1055 ? 15.599  66.520  104.847 1.00 17.88 ? 1053 PHE   A CD2   1 
ATOM   7771  C  CE1   . PHE   A  1  1055 ? 17.712  68.255  104.487 1.00 20.51 ? 1053 PHE   A CE1   1 
ATOM   7772  C  CE2   . PHE   A  1  1055 ? 15.940  67.422  105.848 1.00 19.21 ? 1053 PHE   A CE2   1 
ATOM   7773  C  CZ    . PHE   A  1  1055 ? 17.001  68.281  105.667 1.00 21.17 ? 1053 PHE   A CZ    1 
ATOM   7774  N  N     . ALA   A  1  1056 ? 16.844  62.715  103.736 1.00 16.39 ? 1054 ALA   A N     1 
ATOM   7775  C  CA    . ALA   A  1  1056 ? 17.319  61.867  104.826 1.00 16.08 ? 1054 ALA   A CA    1 
ATOM   7776  C  C     . ALA   A  1  1056 ? 18.693  61.281  104.521 1.00 18.10 ? 1054 ALA   A C     1 
ATOM   7777  O  O     . ALA   A  1  1056 ? 19.568  61.244  105.394 1.00 18.68 ? 1054 ALA   A O     1 
ATOM   7778  C  CB    . ALA   A  1  1056 ? 16.313  60.760  105.127 1.00 17.92 ? 1054 ALA   A CB    1 
ATOM   7779  N  N     . LYS   A  1  1057 ? 18.914  60.820  103.291 1.00 17.68 ? 1055 LYS   A N     1 
ATOM   7780  C  CA    . LYS   A  1  1057 ? 20.234  60.292  102.959 1.00 19.75 ? 1055 LYS   A CA    1 
ATOM   7781  C  C     . LYS   A  1  1057 ? 21.288  61.386  102.981 1.00 18.70 ? 1055 LYS   A C     1 
ATOM   7782  O  O     . LYS   A  1  1057 ? 22.437  61.143  103.378 1.00 19.34 ? 1055 LYS   A O     1 
ATOM   7783  C  CB    . LYS   A  1  1057 ? 20.206  59.626  101.585 1.00 21.53 ? 1055 LYS   A CB    1 
ATOM   7784  C  CG    . LYS   A  1  1057 ? 19.508  58.291  101.582 1.00 21.72 ? 1055 LYS   A CG    1 
ATOM   7785  C  CD    . LYS   A  1  1057 ? 19.664  57.599  100.238 1.00 20.99 ? 1055 LYS   A CD    1 
ATOM   7786  C  CE    . LYS   A  1  1057 ? 19.052  58.413  99.113  1.00 21.47 ? 1055 LYS   A CE    1 
ATOM   7787  N  NZ    . LYS   A  1  1057 ? 18.890  57.573  97.903  1.00 23.76 ? 1055 LYS   A NZ    1 
ATOM   7788  N  N     . TRP   A  1  1058 ? 20.929  62.584  102.515 1.00 17.63 ? 1056 TRP   A N     1 
ATOM   7789  C  CA    . TRP   A  1  1058 ? 21.847  63.715  102.577 1.00 20.50 ? 1056 TRP   A CA    1 
ATOM   7790  C  C     . TRP   A  1  1058 ? 22.212  64.044  104.020 1.00 18.91 ? 1056 TRP   A C     1 
ATOM   7791  O  O     . TRP   A  1  1058 ? 23.384  64.274  104.333 1.00 21.06 ? 1056 TRP   A O     1 
ATOM   7792  C  CB    . TRP   A  1  1058 ? 21.233  64.923  101.870 1.00 20.69 ? 1056 TRP   A CB    1 
ATOM   7793  C  CG    . TRP   A  1  1058 ? 22.063  66.175  101.961 1.00 21.52 ? 1056 TRP   A CG    1 
ATOM   7794  C  CD1   . TRP   A  1  1058 ? 23.081  66.558  101.124 1.00 24.24 ? 1056 TRP   A CD1   1 
ATOM   7795  C  CD2   . TRP   A  1  1058 ? 21.944  67.209  102.944 1.00 22.90 ? 1056 TRP   A CD2   1 
ATOM   7796  N  NE1   . TRP   A  1  1058 ? 23.591  67.771  101.528 1.00 24.85 ? 1056 TRP   A NE1   1 
ATOM   7797  C  CE2   . TRP   A  1  1058 ? 22.912  68.190  102.642 1.00 24.50 ? 1056 TRP   A CE2   1 
ATOM   7798  C  CE3   . TRP   A  1  1058 ? 21.108  67.402  104.047 1.00 22.38 ? 1056 TRP   A CE3   1 
ATOM   7799  C  CZ2   . TRP   A  1  1058 ? 23.072  69.345  103.413 1.00 25.06 ? 1056 TRP   A CZ2   1 
ATOM   7800  C  CZ3   . TRP   A  1  1058 ? 21.265  68.546  104.811 1.00 24.59 ? 1056 TRP   A CZ3   1 
ATOM   7801  C  CH2   . TRP   A  1  1058 ? 22.244  69.503  104.491 1.00 25.82 ? 1056 TRP   A CH2   1 
ATOM   7802  N  N     . LEU   A  1  1059 ? 21.222  64.040  104.915 1.00 18.85 ? 1057 LEU   A N     1 
ATOM   7803  C  CA    . LEU   A  1  1059 ? 21.486  64.317  106.321 1.00 19.27 ? 1057 LEU   A CA    1 
ATOM   7804  C  C     . LEU   A  1  1059 ? 22.446  63.301  106.903 1.00 20.72 ? 1057 LEU   A C     1 
ATOM   7805  O  O     . LEU   A  1  1059 ? 23.364  63.663  107.647 1.00 22.04 ? 1057 LEU   A O     1 
ATOM   7806  C  CB    . LEU   A  1  1059 ? 20.176  64.283  107.104 1.00 18.50 ? 1057 LEU   A CB    1 
ATOM   7807  C  CG    . LEU   A  1  1059 ? 19.298  65.510  106.939 1.00 18.20 ? 1057 LEU   A CG    1 
ATOM   7808  C  CD1   . LEU   A  1  1059 ? 17.922  65.228  107.527 1.00 17.25 ? 1057 LEU   A CD1   1 
ATOM   7809  C  CD2   . LEU   A  1  1059 ? 19.936  66.686  107.665 1.00 20.27 ? 1057 LEU   A CD2   1 
ATOM   7810  N  N     . ASP   A  1  1060 ? 22.247  62.023  106.587 1.00 18.85 ? 1058 ASP   A N     1 
ATOM   7811  C  CA    . ASP   A  1  1060 ? 23.186  61.004  107.046 1.00 22.68 ? 1058 ASP   A CA    1 
ATOM   7812  C  C     . ASP   A  1  1060 ? 24.577  61.239  106.474 1.00 23.04 ? 1058 ASP   A C     1 
ATOM   7813  O  O     . ASP   A  1  1060 ? 25.577  61.120  107.193 1.00 26.30 ? 1058 ASP   A O     1 
ATOM   7814  C  CB    . ASP   A  1  1060 ? 22.681  59.611  106.680 1.00 22.32 ? 1058 ASP   A CB    1 
ATOM   7815  C  CG    . ASP   A  1  1060 ? 21.858  58.983  107.787 1.00 24.23 ? 1058 ASP   A CG    1 
ATOM   7816  O  OD1   . ASP   A  1  1060 ? 22.150  59.254  108.979 1.00 28.24 ? 1058 ASP   A OD1   1 
ATOM   7817  O  OD2   . ASP   A  1  1060 ? 20.931  58.215  107.475 1.00 30.43 ? 1058 ASP   A OD2   1 
ATOM   7818  N  N     . GLY   A  1  1061 ? 24.667  61.603  105.195 1.00 23.95 ? 1059 GLY   A N     1 
ATOM   7819  C  CA    . GLY   A  1  1061 ? 25.970  61.891  104.617 1.00 22.77 ? 1059 GLY   A CA    1 
ATOM   7820  C  C     . GLY   A  1  1061 ? 26.656  63.078  105.265 1.00 26.95 ? 1059 GLY   A C     1 
ATOM   7821  O  O     . GLY   A  1  1061 ? 27.892  63.130  105.324 1.00 27.07 ? 1059 GLY   A O     1 
ATOM   7822  N  N     . LYS   A  1  1062 ? 25.875  64.043  105.757 1.00 25.44 ? 1060 LYS   A N     1 
ATOM   7823  C  CA    . LYS   A  1  1062 ? 26.413  65.184  106.486 1.00 25.70 ? 1060 LYS   A CA    1 
ATOM   7824  C  C     . LYS   A  1  1062 ? 26.751  64.857  107.933 1.00 27.55 ? 1060 LYS   A C     1 
ATOM   7825  O  O     . LYS   A  1  1062 ? 27.358  65.692  108.610 1.00 31.73 ? 1060 LYS   A O     1 
ATOM   7826  C  CB    . LYS   A  1  1062 ? 25.428  66.358  106.450 1.00 28.61 ? 1060 LYS   A CB    1 
ATOM   7827  C  CG    . LYS   A  1  1062 ? 25.321  67.061  105.102 1.00 26.01 ? 1060 LYS   A CG    1 
ATOM   7828  C  CD    . LYS   A  1  1062 ? 26.673  67.626  104.669 1.00 34.26 ? 1060 LYS   A CD    1 
ATOM   7829  C  CE    . LYS   A  1  1062 ? 26.590  68.296  103.305 1.00 37.66 ? 1060 LYS   A CE    1 
ATOM   7830  N  NZ    . LYS   A  1  1062 ? 27.895  68.894  102.896 1.00 41.88 ? 1060 LYS   A NZ    1 
ATOM   7831  N  N     . GLY   A  1  1063 ? 26.386  63.676  108.420 1.00 23.96 ? 1061 GLY   A N     1 
ATOM   7832  C  CA    . GLY   A  1  1063 ? 26.591  63.321  109.808 1.00 27.12 ? 1061 GLY   A CA    1 
ATOM   7833  C  C     . GLY   A  1  1063 ? 25.472  63.715  110.747 1.00 29.45 ? 1061 GLY   A C     1 
ATOM   7834  O  O     . GLY   A  1  1063 ? 25.612  63.526  111.964 1.00 29.54 ? 1061 GLY   A O     1 
ATOM   7835  N  N     . ALA   A  1  1064 ? 24.365  64.247  110.226 1.00 23.92 ? 1062 ALA   A N     1 
ATOM   7836  C  CA    . ALA   A  1  1064 ? 23.223  64.658  111.046 1.00 23.43 ? 1062 ALA   A CA    1 
ATOM   7837  C  C     . ALA   A  1  1064 ? 22.326  63.442  111.286 1.00 24.26 ? 1062 ALA   A C     1 
ATOM   7838  O  O     . ALA   A  1  1064 ? 21.203  63.334  110.789 1.00 21.21 ? 1062 ALA   A O     1 
ATOM   7839  C  CB    . ALA   A  1  1064 ? 22.484  65.810  110.380 1.00 22.85 ? 1062 ALA   A CB    1 
ATOM   7840  N  N     . ARG   A  1  1065 ? 22.850  62.512  112.083 1.00 23.94 ? 1063 ARG   A N     1 
ATOM   7841  C  CA    . ARG   A  1  1065 ? 22.242  61.191  112.193 1.00 19.13 ? 1063 ARG   A CA    1 
ATOM   7842  C  C     . ARG   A  1  1065 ? 20.867  61.253  112.851 1.00 21.82 ? 1063 ARG   A C     1 
ATOM   7843  O  O     . ARG   A  1  1065 ? 19.912  60.625  112.380 1.00 22.86 ? 1063 ARG   A O     1 
ATOM   7844  C  CB    . ARG   A  1  1065 ? 23.167  60.248  112.963 1.00 24.11 ? 1063 ARG   A CB    1 
ATOM   7845  N  N     . ALA   A  1  1066 ? 20.743  61.984  113.960 1.00 21.91 ? 1064 ALA   A N     1 
ATOM   7846  C  CA    . ALA   A  1  1066 ? 19.439  62.081  114.603 1.00 20.14 ? 1064 ALA   A CA    1 
ATOM   7847  C  C     . ALA   A  1  1066 ? 18.425  62.749  113.687 1.00 19.62 ? 1064 ALA   A C     1 
ATOM   7848  O  O     . ALA   A  1  1066 ? 17.255  62.358  113.659 1.00 20.61 ? 1064 ALA   A O     1 
ATOM   7849  C  CB    . ALA   A  1  1066 ? 19.548  62.849  115.917 1.00 21.65 ? 1064 ALA   A CB    1 
ATOM   7850  N  N     . GLU   A  1  1067 ? 18.855  63.769  112.940 1.00 19.77 ? 1065 GLU   A N     1 
ATOM   7851  C  CA    . GLU   A  1  1067 ? 17.937  64.460  112.042 1.00 18.78 ? 1065 GLU   A CA    1 
ATOM   7852  C  C     . GLU   A  1  1067 ? 17.528  63.565  110.884 1.00 20.34 ? 1065 GLU   A C     1 
ATOM   7853  O  O     . GLU   A  1  1067 ? 16.368  63.585  110.466 1.00 18.83 ? 1065 GLU   A O     1 
ATOM   7854  C  CB    . GLU   A  1  1067 ? 18.564  65.757  111.541 1.00 19.69 ? 1065 GLU   A CB    1 
ATOM   7855  C  CG    . GLU   A  1  1067 ? 18.656  66.852  112.611 1.00 19.47 ? 1065 GLU   A CG    1 
ATOM   7856  C  CD    . GLU   A  1  1067 ? 19.815  66.666  113.570 1.00 25.51 ? 1065 GLU   A CD    1 
ATOM   7857  O  OE1   . GLU   A  1  1067 ? 20.696  65.809  113.319 1.00 22.08 ? 1065 GLU   A OE1   1 
ATOM   7858  O  OE2   . GLU   A  1  1067 ? 19.842  67.390  114.586 1.00 29.00 ? 1065 GLU   A OE2   1 
ATOM   7859  N  N     . ALA   A  1  1068 ? 18.463  62.766  110.368 1.00 18.91 ? 1066 ALA   A N     1 
ATOM   7860  C  CA    . ALA   A  1  1068 ? 18.121  61.812  109.317 1.00 18.34 ? 1066 ALA   A CA    1 
ATOM   7861  C  C     . ALA   A  1  1068 ? 17.082  60.815  109.806 1.00 18.78 ? 1066 ALA   A C     1 
ATOM   7862  O  O     . ALA   A  1  1068 ? 16.158  60.455  109.066 1.00 17.66 ? 1066 ALA   A O     1 
ATOM   7863  C  CB    . ALA   A  1  1068 ? 19.376  61.077  108.847 1.00 20.19 ? 1066 ALA   A CB    1 
ATOM   7864  N  N     . GLU   A  1  1069 ? 17.215  60.355  111.049 1.00 19.84 ? 1067 GLU   A N     1 
ATOM   7865  C  CA    . GLU   A  1  1069 ? 16.212  59.461  111.609 1.00 19.06 ? 1067 GLU   A CA    1 
ATOM   7866  C  C     . GLU   A  1  1069 ? 14.873  60.168  111.761 1.00 20.09 ? 1067 GLU   A C     1 
ATOM   7867  O  O     . GLU   A  1  1069 ? 13.818  59.588  111.470 1.00 20.73 ? 1067 GLU   A O     1 
ATOM   7868  C  CB    . GLU   A  1  1069 ? 16.691  58.934  112.958 1.00 21.66 ? 1067 GLU   A CB    1 
ATOM   7869  C  CG    . GLU   A  1  1069 ? 15.662  58.106  113.698 1.00 26.12 ? 1067 GLU   A CG    1 
ATOM   7870  C  CD    . GLU   A  1  1069 ? 15.490  56.716  113.112 1.00 35.22 ? 1067 GLU   A CD    1 
ATOM   7871  O  OE1   . GLU   A  1  1069 ? 16.254  56.357  112.189 1.00 39.19 ? 1067 GLU   A OE1   1 
ATOM   7872  O  OE2   . GLU   A  1  1069 ? 14.591  55.980  113.578 1.00 45.50 ? 1067 GLU   A OE2   1 
ATOM   7873  N  N     . ALA   A  1  1070 ? 14.895  61.420  112.224 1.00 19.18 ? 1068 ALA   A N     1 
ATOM   7874  C  CA    . ALA   A  1  1070 ? 13.660  62.181  112.338 1.00 18.41 ? 1068 ALA   A CA    1 
ATOM   7875  C  C     . ALA   A  1  1070 ? 13.043  62.387  110.968 1.00 17.21 ? 1068 ALA   A C     1 
ATOM   7876  O  O     . ALA   A  1  1070 ? 11.814  62.389  110.822 1.00 18.40 ? 1068 ALA   A O     1 
ATOM   7877  C  CB    . ALA   A  1  1070 ? 13.942  63.529  113.005 1.00 19.90 ? 1068 ALA   A CB    1 
ATOM   7878  N  N     . ALA   A  1  1071 ? 13.886  62.564  109.951 1.00 17.37 ? 1069 ALA   A N     1 
ATOM   7879  C  CA    . ALA   A  1  1071 ? 13.375  62.737  108.599 1.00 15.21 ? 1069 ALA   A CA    1 
ATOM   7880  C  C     . ALA   A  1  1071 ? 12.705  61.461  108.114 1.00 16.06 ? 1069 ALA   A C     1 
ATOM   7881  O  O     . ALA   A  1  1071 ? 11.586  61.502  107.597 1.00 15.47 ? 1069 ALA   A O     1 
ATOM   7882  C  CB    . ALA   A  1  1071 ? 14.505  63.162  107.666 1.00 16.56 ? 1069 ALA   A CB    1 
ATOM   7883  N  N     . ARG   A  1  1072 ? 13.357  60.308  108.304 1.00 16.95 ? 1070 ARG   A N     1 
ATOM   7884  C  CA    . ARG   A  1  1072 ? 12.717  59.048  107.936 1.00 17.03 ? 1070 ARG   A CA    1 
ATOM   7885  C  C     . ARG   A  1  1072 ? 11.404  58.855  108.684 1.00 17.72 ? 1070 ARG   A C     1 
ATOM   7886  O  O     . ARG   A  1  1072 ? 10.410  58.410  108.101 1.00 18.19 ? 1070 ARG   A O     1 
ATOM   7887  C  CB    . ARG   A  1  1072 ? 13.662  57.874  108.181 1.00 19.09 ? 1070 ARG   A CB    1 
ATOM   7888  C  CG    . ARG   A  1  1072 ? 14.806  57.827  107.197 1.00 21.09 ? 1070 ARG   A CG    1 
ATOM   7889  C  CD    . ARG   A  1  1072 ? 15.600  56.552  107.372 1.00 22.75 ? 1070 ARG   A CD    1 
ATOM   7890  N  NE    . ARG   A  1  1072 ? 16.348  56.579  108.620 1.00 24.02 ? 1070 ARG   A NE    1 
ATOM   7891  C  CZ    . ARG   A  1  1072 ? 17.564  57.091  108.746 1.00 25.14 ? 1070 ARG   A CZ    1 
ATOM   7892  N  NH1   . ARG   A  1  1072 ? 18.207  57.605  107.708 1.00 25.31 ? 1070 ARG   A NH1   1 
ATOM   7893  N  NH2   . ARG   A  1  1072 ? 18.143  57.095  109.943 1.00 25.02 ? 1070 ARG   A NH2   1 
ATOM   7894  N  N     . ASN   A  1  1073 ? 11.372  59.202  109.971 1.00 17.31 ? 1071 ASN   A N     1 
ATOM   7895  C  CA    . ASN   A  1  1073 ? 10.136  59.075  110.735 1.00 18.17 ? 1071 ASN   A CA    1 
ATOM   7896  C  C     . ASN   A  1  1073 ? 9.051   59.980  110.177 1.00 18.11 ? 1071 ASN   A C     1 
ATOM   7897  O  O     . ASN   A  1  1073 ? 7.886   59.577  110.088 1.00 18.17 ? 1071 ASN   A O     1 
ATOM   7898  C  CB    . ASN   A  1  1073 ? 10.395  59.377  112.210 1.00 18.51 ? 1071 ASN   A CB    1 
ATOM   7899  C  CG    . ASN   A  1  1073 ? 11.175  58.274  112.893 1.00 25.65 ? 1071 ASN   A CG    1 
ATOM   7900  O  OD1   . ASN   A  1  1073 ? 11.265  57.153  112.384 1.00 28.85 ? 1071 ASN   A OD1   1 
ATOM   7901  N  ND2   . ASN   A  1  1073 ? 11.741  58.583  114.047 1.00 28.44 ? 1071 ASN   A ND2   1 
ATOM   7902  N  N     . ALA   A  1  1074 ? 9.416   61.211  109.799 1.00 16.84 ? 1072 ALA   A N     1 
ATOM   7903  C  CA    . ALA   A  1  1074 ? 8.445   62.106  109.181 1.00 16.92 ? 1072 ALA   A CA    1 
ATOM   7904  C  C     . ALA   A  1  1074 ? 7.954   61.534  107.866 1.00 16.21 ? 1072 ALA   A C     1 
ATOM   7905  O  O     . ALA   A  1  1074 ? 6.766   61.635  107.543 1.00 15.98 ? 1072 ALA   A O     1 
ATOM   7906  C  CB    . ALA   A  1  1074 ? 9.073   63.482  108.957 1.00 20.21 ? 1072 ALA   A CB    1 
ATOM   7907  N  N     . GLY   A  1  1075 ? 8.855   60.930  107.091 1.00 15.78 ? 1073 GLY   A N     1 
ATOM   7908  C  CA    . GLY   A  1  1075 ? 8.436   60.323  105.839 1.00 15.90 ? 1073 GLY   A CA    1 
ATOM   7909  C  C     . GLY   A  1  1075 ? 7.361   59.274  106.038 1.00 16.23 ? 1073 GLY   A C     1 
ATOM   7910  O  O     . GLY   A  1  1075 ? 6.408   59.198  105.262 1.00 17.20 ? 1073 GLY   A O     1 
ATOM   7911  N  N     . SER   A  1  1076 ? 7.508   58.448  107.074 1.00 17.61 ? 1074 SER   A N     1 
ATOM   7912  C  CA    . SER   A  1  1076 ? 6.532   57.405  107.367 1.00 16.63 ? 1074 SER   A CA    1 
ATOM   7913  C  C     . SER   A  1  1076 ? 5.271   57.978  107.984 1.00 18.94 ? 1074 SER   A C     1 
ATOM   7914  O  O     . SER   A  1  1076 ? 4.163   57.539  107.654 1.00 20.02 ? 1074 SER   A O     1 
ATOM   7915  C  CB    . SER   A  1  1076 ? 7.124   56.398  108.353 1.00 20.98 ? 1074 SER   A CB    1 
ATOM   7916  O  OG    . SER   A  1  1076 ? 8.133   55.631  107.750 1.00 28.04 ? 1074 SER   A OG    1 
ATOM   7917  N  N     . SER   A  1  1077 ? 5.427   58.946  108.891 1.00 17.77 ? 1075 SER   A N     1 
ATOM   7918  C  CA    A SER   A  1  1077 ? 4.278   59.498  109.600 0.52 18.84 ? 1075 SER   A CA    1 
ATOM   7919  C  CA    B SER   A  1  1077 ? 4.289   59.514  109.608 0.48 18.85 ? 1075 SER   A CA    1 
ATOM   7920  C  C     . SER   A  1  1077 ? 3.401   60.351  108.696 1.00 17.22 ? 1075 SER   A C     1 
ATOM   7921  O  O     . SER   A  1  1077 ? 2.202   60.504  108.963 1.00 19.01 ? 1075 SER   A O     1 
ATOM   7922  C  CB    A SER   A  1  1077 ? 4.755   60.320  110.796 0.52 19.21 ? 1075 SER   A CB    1 
ATOM   7923  C  CB    B SER   A  1  1077 ? 4.805   60.370  110.766 0.48 19.18 ? 1075 SER   A CB    1 
ATOM   7924  O  OG    A SER   A  1  1077 ? 5.238   59.472  111.818 0.52 23.80 ? 1075 SER   A OG    1 
ATOM   7925  O  OG    B SER   A  1  1077 ? 3.751   61.078  111.392 0.48 22.40 ? 1075 SER   A OG    1 
ATOM   7926  N  N     . SER   A  1  1078 ? 3.967   60.912  107.646 1.00 16.11 ? 1076 SER   A N     1 
ATOM   7927  C  CA    . SER   A  1  1078 ? 3.196   61.735  106.734 1.00 16.76 ? 1076 SER   A CA    1 
ATOM   7928  C  C     . SER   A  1  1078 ? 2.056   60.932  106.122 1.00 16.01 ? 1076 SER   A C     1 
ATOM   7929  O  O     . SER   A  1  1078 ? 2.213   59.765  105.762 1.00 16.61 ? 1076 SER   A O     1 
ATOM   7930  C  CB    . SER   A  1  1078 ? 4.114   62.221  105.624 1.00 15.01 ? 1076 SER   A CB    1 
ATOM   7931  O  OG    . SER   A  1  1078 ? 3.353   62.898  104.639 1.00 14.59 ? 1076 SER   A OG    1 
ATOM   7932  N  N     . ALA   A  1  1079 ? 0.896   61.563  106.002 1.00 14.54 ? 1077 ALA   A N     1 
ATOM   7933  C  CA    . ALA   A  1  1079 ? -0.223  60.942  105.316 1.00 14.64 ? 1077 ALA   A CA    1 
ATOM   7934  C  C     . ALA   A  1  1079 ? -0.366  61.443  103.892 1.00 14.33 ? 1077 ALA   A C     1 
ATOM   7935  O  O     . ALA   A  1  1079 ? -1.372  61.164  103.237 1.00 14.46 ? 1077 ALA   A O     1 
ATOM   7936  C  CB    . ALA   A  1  1079 ? -1.518  61.131  106.104 1.00 15.65 ? 1077 ALA   A CB    1 
ATOM   7937  N  N     . LEU   A  1  1080 ? 0.623   62.172  103.389 1.00 14.16 ? 1078 LEU   A N     1 
ATOM   7938  C  CA    . LEU   A  1  1080 ? 0.643   62.550  101.988 1.00 14.26 ? 1078 LEU   A CA    1 
ATOM   7939  C  C     . LEU   A  1  1080 ? 0.398   61.326  101.121 1.00 13.84 ? 1078 LEU   A C     1 
ATOM   7940  O  O     . LEU   A  1  1080 ? 1.056   60.291  101.282 1.00 14.89 ? 1078 LEU   A O     1 
ATOM   7941  C  CB    . LEU   A  1  1080 ? 2.020   63.122  101.660 1.00 13.72 ? 1078 LEU   A CB    1 
ATOM   7942  C  CG    . LEU   A  1  1080 ? 2.250   63.408  100.183 1.00 14.88 ? 1078 LEU   A CG    1 
ATOM   7943  C  CD1   . LEU   A  1  1080 ? 1.404   64.599  99.756  1.00 17.68 ? 1078 LEU   A CD1   1 
ATOM   7944  C  CD2   . LEU   A  1  1080 ? 3.726   63.681  99.944  1.00 15.60 ? 1078 LEU   A CD2   1 
ATOM   7945  N  N     . GLY   A  1  1081 ? -0.544  61.442  100.193 1.00 13.53 ? 1079 GLY   A N     1 
ATOM   7946  C  CA    . GLY   A  1  1081 ? -0.848  60.329  99.319  1.00 14.67 ? 1079 GLY   A CA    1 
ATOM   7947  C  C     . GLY   A  1  1081 ? -2.042  59.509  99.751  1.00 15.37 ? 1079 GLY   A C     1 
ATOM   7948  O  O     . GLY   A  1  1081 ? -2.451  58.603  99.007  1.00 16.18 ? 1079 GLY   A O     1 
ATOM   7949  N  N     . LEU   A  1  1082 ? -2.581  59.769  100.939 1.00 15.00 ? 1080 LEU   A N     1 
ATOM   7950  C  CA    A LEU   A  1  1082 ? -3.855  59.183  101.330 0.50 14.16 ? 1080 LEU   A CA    1 
ATOM   7951  C  CA    B LEU   A  1  1082 ? -3.857  59.188  101.333 0.50 14.16 ? 1080 LEU   A CA    1 
ATOM   7952  C  C     . LEU   A  1  1082 ? -4.865  59.407  100.217 1.00 15.51 ? 1080 LEU   A C     1 
ATOM   7953  O  O     . LEU   A  1  1082 ? -4.956  60.500  99.657  1.00 15.62 ? 1080 LEU   A O     1 
ATOM   7954  C  CB    A LEU   A  1  1082 ? -4.344  59.854  102.610 0.50 14.52 ? 1080 LEU   A CB    1 
ATOM   7955  C  CB    B LEU   A  1  1082 ? -4.340  59.874  102.609 0.50 14.51 ? 1080 LEU   A CB    1 
ATOM   7956  C  CG    A LEU   A  1  1082 ? -5.699  59.365  103.123 0.50 15.04 ? 1080 LEU   A CG    1 
ATOM   7957  C  CG    B LEU   A  1  1082 ? -5.683  59.435  103.196 0.50 15.06 ? 1080 LEU   A CG    1 
ATOM   7958  C  CD1   A LEU   A  1  1082 ? -5.660  57.879  103.395 0.50 14.92 ? 1080 LEU   A CD1   1 
ATOM   7959  C  CD1   B LEU   A  1  1082 ? -5.655  59.602  104.700 0.50 14.08 ? 1080 LEU   A CD1   1 
ATOM   7960  C  CD2   A LEU   A  1  1082 ? -6.091  60.124  104.375 0.50 15.34 ? 1080 LEU   A CD2   1 
ATOM   7961  C  CD2   B LEU   A  1  1082 ? -6.834  60.240  102.599 0.50 14.89 ? 1080 LEU   A CD2   1 
ATOM   7962  N  N     . ASP   A  1  1083 ? -5.609  58.358  99.885  1.00 15.90 ? 1081 ASP   A N     1 
ATOM   7963  C  CA    . ASP   A  1  1083 ? -6.519  58.427  98.743  1.00 17.27 ? 1081 ASP   A CA    1 
ATOM   7964  C  C     . ASP   A  1  1083 ? -7.677  57.491  99.063  1.00 17.61 ? 1081 ASP   A C     1 
ATOM   7965  O  O     . ASP   A  1  1083 ? -7.543  56.272  98.942  1.00 21.21 ? 1081 ASP   A O     1 
ATOM   7966  C  CB    . ASP   A  1  1083 ? -5.786  57.998  97.478  1.00 19.74 ? 1081 ASP   A CB    1 
ATOM   7967  C  CG    . ASP   A  1  1083 ? -6.640  58.106  96.233  1.00 25.63 ? 1081 ASP   A CG    1 
ATOM   7968  O  OD1   . ASP   A  1  1083 ? -7.726  58.717  96.300  1.00 29.48 ? 1081 ASP   A OD1   1 
ATOM   7969  O  OD2   . ASP   A  1  1083 ? -6.209  57.582  95.185  1.00 33.19 ? 1081 ASP   A OD2   1 
ATOM   7970  N  N     . LEU   A  1  1084 ? -8.801  58.065  99.479  1.00 17.54 ? 1082 LEU   A N     1 
ATOM   7971  C  CA    . LEU   A  1  1084 ? -9.903  57.284  100.005 1.00 17.87 ? 1082 LEU   A CA    1 
ATOM   7972  C  C     . LEU   A  1  1084 ? -11.165 57.589  99.229  1.00 18.96 ? 1082 LEU   A C     1 
ATOM   7973  O  O     . LEU   A  1  1084 ? -11.332 58.686  98.697  1.00 18.96 ? 1082 LEU   A O     1 
ATOM   7974  C  CB    . LEU   A  1  1084 ? -10.192 57.660  101.449 1.00 19.61 ? 1082 LEU   A CB    1 
ATOM   7975  C  CG    . LEU   A  1  1084 ? -9.096  57.416  102.467 1.00 22.28 ? 1082 LEU   A CG    1 
ATOM   7976  C  CD1   . LEU   A  1  1084 ? -9.510  58.051  103.778 1.00 22.80 ? 1082 LEU   A CD1   1 
ATOM   7977  C  CD2   . LEU   A  1  1084 ? -8.865  55.929  102.637 1.00 20.98 ? 1082 LEU   A CD2   1 
ATOM   7978  N  N     . GLU   A  1  1085 ? -12.049 56.605  99.176  1.00 17.96 ? 1083 GLU   A N     1 
ATOM   7979  C  CA    . GLU   A  1  1085 ? -13.408 56.821  98.712  1.00 17.58 ? 1083 GLU   A CA    1 
ATOM   7980  C  C     . GLU   A  1  1085 ? -14.312 56.821  99.929  1.00 17.90 ? 1083 GLU   A C     1 
ATOM   7981  O  O     . GLU   A  1  1085 ? -14.259 55.896  100.748 1.00 20.34 ? 1083 GLU   A O     1 
ATOM   7982  C  CB    . GLU   A  1  1085 ? -13.869 55.756  97.721  1.00 18.03 ? 1083 GLU   A CB    1 
ATOM   7983  C  CG    . GLU   A  1  1085 ? -15.330 56.000  97.338  1.00 20.29 ? 1083 GLU   A CG    1 
ATOM   7984  C  CD    . GLU   A  1  1085 ? -15.836 55.177  96.169  1.00 25.71 ? 1083 GLU   A CD    1 
ATOM   7985  O  OE1   . GLU   A  1  1085 ? -15.025 54.523  95.484  1.00 28.43 ? 1083 GLU   A OE1   1 
ATOM   7986  O  OE2   . GLU   A  1  1085 ? -17.074 55.187  95.948  1.00 27.54 ? 1083 GLU   A OE2   1 
ATOM   7987  N  N     . LEU   A  1  1086 ? -15.109 57.868  100.062 1.00 18.65 ? 1084 LEU   A N     1 
ATOM   7988  C  CA    . LEU   A  1  1086 ? -15.970 58.020  101.221 1.00 17.70 ? 1084 LEU   A CA    1 
ATOM   7989  C  C     . LEU   A  1  1086 ? -17.368 57.492  100.908 1.00 19.30 ? 1084 LEU   A C     1 
ATOM   7990  O  O     . LEU   A  1  1086 ? -17.867 57.684  99.802  1.00 19.04 ? 1084 LEU   A O     1 
ATOM   7991  C  CB    . LEU   A  1  1086 ? -16.060 59.492  101.609 1.00 17.81 ? 1084 LEU   A CB    1 
ATOM   7992  C  CG    . LEU   A  1  1086 ? -14.711 60.151  101.927 1.00 19.35 ? 1084 LEU   A CG    1 
ATOM   7993  C  CD1   . LEU   A  1  1086 ? -14.898 61.598  102.321 1.00 20.87 ? 1084 LEU   A CD1   1 
ATOM   7994  C  CD2   . LEU   A  1  1086 ? -13.975 59.391  103.018 1.00 22.17 ? 1084 LEU   A CD2   1 
ATOM   7995  N  N     . PRO   A  1  1087 ? -17.990 56.815  101.864 1.00 19.34 ? 1085 PRO   A N     1 
ATOM   7996  C  CA    . PRO   A  1  1087 ? -19.345 56.298  101.644 1.00 22.68 ? 1085 PRO   A CA    1 
ATOM   7997  C  C     . PRO   A  1  1087 ? -20.308 57.429  101.348 1.00 18.52 ? 1085 PRO   A C     1 
ATOM   7998  O  O     . PRO   A  1  1087 ? -20.262 58.494  101.965 1.00 21.97 ? 1085 PRO   A O     1 
ATOM   7999  C  CB    . PRO   A  1  1087 ? -19.693 55.627  102.976 1.00 24.63 ? 1085 PRO   A CB    1 
ATOM   8000  C  CG    . PRO   A  1  1087 ? -18.380 55.365  103.633 1.00 25.51 ? 1085 PRO   A CG    1 
ATOM   8001  C  CD    . PRO   A  1  1087 ? -17.439 56.433  103.172 1.00 19.36 ? 1085 PRO   A CD    1 
ATOM   8002  N  N     . GLY   A  1  1088 ? -21.193 57.186  100.393 1.00 19.50 ? 1086 GLY   A N     1 
ATOM   8003  C  CA    . GLY   A  1  1088 ? -22.186 58.160  100.035 1.00 21.62 ? 1086 GLY   A CA    1 
ATOM   8004  C  C     . GLY   A  1  1088 ? -23.279 57.543  99.192  1.00 17.45 ? 1086 GLY   A C     1 
ATOM   8005  O  O     . GLY   A  1  1088 ? -23.472 56.327  99.152  1.00 17.07 ? 1086 GLY   A O     1 
ATOM   8006  N  N     . PRO   A  1  1089 ? -23.995 58.384  98.473  1.00 19.73 ? 1087 PRO   A N     1 
ATOM   8007  C  CA    . PRO   A  1  1089 ? -25.107 57.890  97.665  1.00 18.28 ? 1087 PRO   A CA    1 
ATOM   8008  C  C     . PRO   A  1  1089 ? -24.602 57.132  96.449  1.00 18.69 ? 1087 PRO   A C     1 
ATOM   8009  O  O     . PRO   A  1  1089 ? -23.474 57.318  95.975  1.00 18.25 ? 1087 PRO   A O     1 
ATOM   8010  C  CB    . PRO   A  1  1089 ? -25.812 59.179  97.238  1.00 21.38 ? 1087 PRO   A CB    1 
ATOM   8011  C  CG    . PRO   A  1  1089 ? -24.659 60.181  97.154  1.00 21.42 ? 1087 PRO   A CG    1 
ATOM   8012  C  CD    . PRO   A  1  1089 ? -23.795 59.835  98.339  1.00 18.89 ? 1087 PRO   A CD    1 
ATOM   8013  N  N     . VAL   A  1  1090 ? -25.473 56.264  95.936  1.00 17.75 ? 1088 VAL   A N     1 
ATOM   8014  C  CA    . VAL   A  1  1090 ? -25.192 55.621  94.664  1.00 16.12 ? 1088 VAL   A CA    1 
ATOM   8015  C  C     . VAL   A  1  1090 ? -25.076 56.667  93.559  1.00 16.71 ? 1088 VAL   A C     1 
ATOM   8016  O  O     . VAL   A  1  1090 ? -25.577 57.795  93.662  1.00 16.65 ? 1088 VAL   A O     1 
ATOM   8017  C  CB    . VAL   A  1  1090 ? -26.248 54.565  94.306  1.00 17.68 ? 1088 VAL   A CB    1 
ATOM   8018  C  CG1   . VAL   A  1  1090 ? -26.323 53.510  95.389  1.00 19.89 ? 1088 VAL   A CG1   1 
ATOM   8019  C  CG2   . VAL   A  1  1090 ? -27.616 55.208  94.116  1.00 18.06 ? 1088 VAL   A CG2   1 
ATOM   8020  N  N     . GLY   A  1  1091 ? -24.405 56.279  92.483  1.00 16.98 ? 1089 GLY   A N     1 
ATOM   8021  C  CA    . GLY   A  1  1091 ? -24.323 57.156  91.336  1.00 17.15 ? 1089 GLY   A CA    1 
ATOM   8022  C  C     . GLY   A  1  1091 ? -23.373 58.304  91.527  1.00 16.81 ? 1089 GLY   A C     1 
ATOM   8023  O  O     . GLY   A  1  1091 ? -23.404 59.272  90.765  1.00 14.76 ? 1089 GLY   A O     1 
ATOM   8024  N  N     . GLU   A  1  1092 ? -22.526 58.218  92.543  1.00 15.39 ? 1090 GLU   A N     1 
ATOM   8025  C  CA    . GLU   A  1  1092 ? -21.540 59.241  92.808  1.00 16.74 ? 1090 GLU   A CA    1 
ATOM   8026  C  C     . GLU   A  1  1092 ? -20.332 58.549  93.408  1.00 16.27 ? 1090 GLU   A C     1 
ATOM   8027  O  O     . GLU   A  1  1092 ? -20.459 57.547  94.117  1.00 17.79 ? 1090 GLU   A O     1 
ATOM   8028  C  CB    . GLU   A  1  1092 ? -22.104 60.239  93.818  1.00 20.63 ? 1090 GLU   A CB    1 
ATOM   8029  C  CG    . GLU   A  1  1092 ? -21.577 61.652  93.721  1.00 24.45 ? 1090 GLU   A CG    1 
ATOM   8030  C  CD    . GLU   A  1  1092 ? -22.381 62.583  94.606  1.00 24.28 ? 1090 GLU   A CD    1 
ATOM   8031  O  OE1   . GLU   A  1  1092 ? -22.221 62.478  95.833  1.00 19.84 ? 1090 GLU   A OE1   1 
ATOM   8032  O  OE2   . GLU   A  1  1092 ? -23.197 63.382  94.087  1.00 25.53 ? 1090 GLU   A OE2   1 
ATOM   8033  N  N     . ARG   A  1  1093 ? -19.156 59.064  93.088  1.00 15.33 ? 1091 ARG   A N     1 
ATOM   8034  C  CA    . ARG   A  1  1093 ? -17.929 58.632  93.743  1.00 16.09 ? 1091 ARG   A CA    1 
ATOM   8035  C  C     . ARG   A  1  1093 ? -17.353 59.846  94.440  1.00 15.21 ? 1091 ARG   A C     1 
ATOM   8036  O  O     . ARG   A  1  1093 ? -17.136 60.889  93.814  1.00 15.93 ? 1091 ARG   A O     1 
ATOM   8037  C  CB    . ARG   A  1  1093 ? -16.924 58.047  92.754  1.00 21.19 ? 1091 ARG   A CB    1 
ATOM   8038  C  CG    . ARG   A  1  1093 ? -17.171 56.587  92.458  1.00 27.99 ? 1091 ARG   A CG    1 
ATOM   8039  C  CD    . ARG   A  1  1093 ? -15.898 55.912  91.953  1.00 39.78 ? 1091 ARG   A CD    1 
ATOM   8040  N  NE    . ARG   A  1  1093 ? -15.340 56.629  90.814  1.00 49.29 ? 1091 ARG   A NE    1 
ATOM   8041  C  CZ    . ARG   A  1  1093 ? -15.714 56.442  89.555  1.00 45.85 ? 1091 ARG   A CZ    1 
ATOM   8042  N  NH1   . ARG   A  1  1093 ? -16.629 55.539  89.235  1.00 43.34 ? 1091 ARG   A NH1   1 
ATOM   8043  N  NH2   . ARG   A  1  1093 ? -15.158 57.179  88.595  1.00 44.74 ? 1091 ARG   A NH2   1 
ATOM   8044  N  N     . ASN   A  1  1094 ? -17.129 59.712  95.734  1.00 15.12 ? 1092 ASN   A N     1 
ATOM   8045  C  CA    . ASN   A  1  1094 ? -16.708 60.831  96.551  1.00 14.24 ? 1092 ASN   A CA    1 
ATOM   8046  C  C     . ASN   A  1  1094 ? -15.350 60.484  97.115  1.00 15.04 ? 1092 ASN   A C     1 
ATOM   8047  O  O     . ASN   A  1  1094 ? -15.217 59.524  97.879  1.00 16.38 ? 1092 ASN   A O     1 
ATOM   8048  C  CB    . ASN   A  1  1094 ? -17.753 61.101  97.618  1.00 15.20 ? 1092 ASN   A CB    1 
ATOM   8049  C  CG    . ASN   A  1  1094 ? -18.967 61.753  97.028  1.00 15.12 ? 1092 ASN   A CG    1 
ATOM   8050  O  OD1   . ASN   A  1  1094 ? -18.872 62.883  96.573  1.00 15.99 ? 1092 ASN   A OD1   1 
ATOM   8051  N  ND2   . ASN   A  1  1094 ? -20.106 61.050  96.998  1.00 16.60 ? 1092 ASN   A ND2   1 
ATOM   8052  N  N     . LEU   A  1  1095 ? -14.349 61.230  96.682  1.00 14.37 ? 1093 LEU   A N     1 
ATOM   8053  C  CA    . LEU   A  1  1095 ? -12.961 60.896  96.941  1.00 15.06 ? 1093 LEU   A CA    1 
ATOM   8054  C  C     . LEU   A  1  1095 ? -12.344 61.951  97.836  1.00 15.28 ? 1093 LEU   A C     1 
ATOM   8055  O  O     . LEU   A  1  1095 ? -12.707 63.125  97.792  1.00 16.04 ? 1093 LEU   A O     1 
ATOM   8056  C  CB    . LEU   A  1  1095 ? -12.165 60.838  95.644  1.00 16.43 ? 1093 LEU   A CB    1 
ATOM   8057  C  CG    . LEU   A  1  1095 ? -12.803 59.912  94.609  1.00 18.61 ? 1093 LEU   A CG    1 
ATOM   8058  C  CD1   . LEU   A  1  1095 ? -11.966 59.889  93.351  1.00 23.30 ? 1093 LEU   A CD1   1 
ATOM   8059  C  CD2   . LEU   A  1  1095 ? -12.981 58.503  95.164  1.00 22.13 ? 1093 LEU   A CD2   1 
ATOM   8060  N  N     . TYR   A  1  1096 ? -11.394 61.511  98.647  1.00 15.76 ? 1094 TYR   A N     1 
ATOM   8061  C  CA    . TYR   A  1  1096 ? -10.756 62.373  99.627  1.00 14.01 ? 1094 TYR   A CA    1 
ATOM   8062  C  C     . TYR   A  1  1096 ? -9.284  62.035  99.586  1.00 13.67 ? 1094 TYR   A C     1 
ATOM   8063  O  O     . TYR   A  1  1096 ? -8.918  60.870  99.760  1.00 15.71 ? 1094 TYR   A O     1 
ATOM   8064  C  CB    . TYR   A  1  1096 ? -11.341 62.081  100.998 1.00 15.52 ? 1094 TYR   A CB    1 
ATOM   8065  C  CG    . TYR   A  1  1096 ? -10.649 62.769  102.141 1.00 16.00 ? 1094 TYR   A CG    1 
ATOM   8066  C  CD1   . TYR   A  1  1096 ? -10.962 64.076  102.492 1.00 15.71 ? 1094 TYR   A CD1   1 
ATOM   8067  C  CD2   . TYR   A  1  1096 ? -9.689  62.105  102.886 1.00 16.85 ? 1094 TYR   A CD2   1 
ATOM   8068  C  CE1   . TYR   A  1  1096 ? -10.330 64.696  103.570 1.00 16.13 ? 1094 TYR   A CE1   1 
ATOM   8069  C  CE2   . TYR   A  1  1096 ? -9.055  62.717  103.964 1.00 16.96 ? 1094 TYR   A CE2   1 
ATOM   8070  C  CZ    . TYR   A  1  1096 ? -9.375  64.010  104.292 1.00 15.92 ? 1094 TYR   A CZ    1 
ATOM   8071  O  OH    . TYR   A  1  1096 ? -8.766  64.618  105.361 1.00 16.40 ? 1094 TYR   A OH    1 
ATOM   8072  N  N     . THR   A  1  1097 ? -8.457  63.033  99.312  1.00 14.84 ? 1095 THR   A N     1 
ATOM   8073  C  CA    . THR   A  1  1097 ? -7.042  62.790  99.092  1.00 14.92 ? 1095 THR   A CA    1 
ATOM   8074  C  C     . THR   A  1  1097 ? -6.233  63.845  99.830  1.00 17.22 ? 1095 THR   A C     1 
ATOM   8075  O  O     . THR   A  1  1097 ? -6.693  64.970  100.038 1.00 16.22 ? 1095 THR   A O     1 
ATOM   8076  C  CB    . THR   A  1  1097 ? -6.714  62.853  97.599  1.00 18.07 ? 1095 THR   A CB    1 
ATOM   8077  O  OG1   . THR   A  1  1097 ? -7.100  64.126  97.078  1.00 21.89 ? 1095 THR   A OG1   1 
ATOM   8078  C  CG2   . THR   A  1  1097 ? -7.463  61.790  96.839  1.00 20.08 ? 1095 THR   A CG2   1 
ATOM   8079  N  N     . LEU   A  1  1098 ? -5.019  63.473  100.226 1.00 14.70 ? 1096 LEU   A N     1 
ATOM   8080  C  CA    . LEU   A  1  1098 ? -4.095  64.392  100.876 1.00 15.43 ? 1096 LEU   A CA    1 
ATOM   8081  C  C     . LEU   A  1  1098 ? -2.938  64.678  99.938  1.00 13.19 ? 1096 LEU   A C     1 
ATOM   8082  O  O     . LEU   A  1  1098 ? -2.231  63.759  99.509  1.00 13.63 ? 1096 LEU   A O     1 
ATOM   8083  C  CB    . LEU   A  1  1098 ? -3.581  63.829  102.197 1.00 15.18 ? 1096 LEU   A CB    1 
ATOM   8084  C  CG    . LEU   A  1  1098 ? -4.701  63.643  103.224 1.00 13.97 ? 1096 LEU   A CG    1 
ATOM   8085  C  CD1   . LEU   A  1  1098 ? -4.093  63.149  104.519 1.00 15.81 ? 1096 LEU   A CD1   1 
ATOM   8086  C  CD2   . LEU   A  1  1098 ? -5.517  64.921  103.458 1.00 15.65 ? 1096 LEU   A CD2   1 
ATOM   8087  N  N     . HIS   A  1  1099 ? -2.742  65.950  99.637  1.00 14.20 ? 1097 HIS   A N     1 
ATOM   8088  C  CA    . HIS   A  1  1099 ? -1.690  66.417  98.753  1.00 14.14 ? 1097 HIS   A CA    1 
ATOM   8089  C  C     . HIS   A  1  1099 ? -0.772  67.349  99.520  1.00 15.01 ? 1097 HIS   A C     1 
ATOM   8090  O  O     . HIS   A  1  1099 ? -1.040  67.727  100.658 1.00 15.39 ? 1097 HIS   A O     1 
ATOM   8091  C  CB    . HIS   A  1  1099 ? -2.307  67.215  97.603  1.00 16.24 ? 1097 HIS   A CB    1 
ATOM   8092  C  CG    . HIS   A  1  1099 ? -3.281  66.434  96.786  1.00 17.72 ? 1097 HIS   A CG    1 
ATOM   8093  N  ND1   . HIS   A  1  1099 ? -2.969  65.938  95.540  1.00 23.30 ? 1097 HIS   A ND1   1 
ATOM   8094  C  CD2   . HIS   A  1  1099 ? -4.551  66.045  97.043  1.00 19.21 ? 1097 HIS   A CD2   1 
ATOM   8095  C  CE1   . HIS   A  1  1099 ? -4.011  65.287  95.056  1.00 23.43 ? 1097 HIS   A CE1   1 
ATOM   8096  N  NE2   . HIS   A  1  1099 ? -4.984  65.341  95.946  1.00 21.15 ? 1097 HIS   A NE2   1 
ATOM   8097  N  N     . ALA   A  1  1100 ? 0.305   67.752  98.858  1.00 15.10 ? 1098 ALA   A N     1 
ATOM   8098  C  CA    . ALA   A  1  1100 ? 1.133   68.804  99.409  1.00 15.86 ? 1098 ALA   A CA    1 
ATOM   8099  C  C     . ALA   A  1  1100 ? 0.345   70.105  99.473  1.00 17.51 ? 1098 ALA   A C     1 
ATOM   8100  O  O     . ALA   A  1  1100 ? -0.567  70.347  98.676  1.00 17.81 ? 1098 ALA   A O     1 
ATOM   8101  C  CB    . ALA   A  1  1100 ? 2.345   69.005  98.509  1.00 16.31 ? 1098 ALA   A CB    1 
ATOM   8102  N  N     . ARG   A  1  1101 ? 0.694   70.946  100.444 1.00 16.50 ? 1099 ARG   A N     1 
ATOM   8103  C  CA    A ARG   A  1  1101 ? 0.091   72.273  100.508 0.49 17.49 ? 1099 ARG   A CA    1 
ATOM   8104  C  CA    B ARG   A  1  1101 ? 0.098   72.274  100.515 0.51 17.48 ? 1099 ARG   A CA    1 
ATOM   8105  C  C     . ARG   A  1  1101 ? 0.661   73.196  99.440  1.00 17.05 ? 1099 ARG   A C     1 
ATOM   8106  O  O     . ARG   A  1  1101 ? -0.074  73.991  98.848  1.00 19.09 ? 1099 ARG   A O     1 
ATOM   8107  C  CB    A ARG   A  1  1101 ? 0.295   72.891  101.890 0.49 20.15 ? 1099 ARG   A CB    1 
ATOM   8108  C  CB    B ARG   A  1  1101 ? 0.335   72.866  101.900 0.51 20.16 ? 1099 ARG   A CB    1 
ATOM   8109  C  CG    A ARG   A  1  1101 ? -0.447  72.180  102.999 0.49 20.18 ? 1099 ARG   A CG    1 
ATOM   8110  C  CG    B ARG   A  1  1101 ? -0.561  72.284  102.968 0.51 20.29 ? 1099 ARG   A CG    1 
ATOM   8111  C  CD    A ARG   A  1  1101 ? -0.357  72.943  104.310 0.49 16.77 ? 1099 ARG   A CD    1 
ATOM   8112  C  CD    B ARG   A  1  1101 ? -1.448  73.372  103.532 0.51 19.79 ? 1099 ARG   A CD    1 
ATOM   8113  N  NE    A ARG   A  1  1101 ? -1.270  74.077  104.383 0.49 17.10 ? 1099 ARG   A NE    1 
ATOM   8114  N  NE    B ARG   A  1  1101 ? -2.476  72.863  104.429 0.51 19.43 ? 1099 ARG   A NE    1 
ATOM   8115  C  CZ    A ARG   A  1  1101 ? -2.527  73.997  104.799 0.49 20.45 ? 1099 ARG   A CZ    1 
ATOM   8116  C  CZ    B ARG   A  1  1101 ? -3.208  73.632  105.224 0.51 20.36 ? 1099 ARG   A CZ    1 
ATOM   8117  N  NH1   A ARG   A  1  1101 ? -3.053  72.850  105.194 0.49 20.53 ? 1099 ARG   A NH1   1 
ATOM   8118  N  NH1   B ARG   A  1  1101 ? -3.018  74.942  105.289 0.51 19.23 ? 1099 ARG   A NH1   1 
ATOM   8119  N  NH2   A ARG   A  1  1101 ? -3.277  75.095  104.810 0.49 20.86 ? 1099 ARG   A NH2   1 
ATOM   8120  N  NH2   B ARG   A  1  1101 ? -4.146  73.074  105.984 0.51 20.09 ? 1099 ARG   A NH2   1 
ATOM   8121  N  N     . GLY   A  1  1102 ? 1.955   73.109  99.184  1.00 16.95 ? 1100 GLY   A N     1 
ATOM   8122  C  CA    . GLY   A  1  1102 ? 2.572   74.008  98.233  1.00 20.10 ? 1100 GLY   A CA    1 
ATOM   8123  C  C     . GLY   A  1  1102 ? 3.943   74.403  98.721  1.00 16.72 ? 1100 GLY   A C     1 
ATOM   8124  O  O     . GLY   A  1  1102 ? 4.765   73.535  99.027  1.00 18.51 ? 1100 GLY   A O     1 
ATOM   8125  N  N     . ARG   A  1  1103 ? 4.211   75.701  98.810  1.00 17.34 ? 1101 ARG   A N     1 
ATOM   8126  C  CA    . ARG   A  1  1103 ? 5.498   76.175  99.298  1.00 16.89 ? 1101 ARG   A CA    1 
ATOM   8127  C  C     . ARG   A  1  1103 ? 5.323   76.631  100.738 1.00 16.38 ? 1101 ARG   A C     1 
ATOM   8128  O  O     . ARG   A  1  1103 ? 4.490   77.503  101.026 1.00 18.31 ? 1101 ARG   A O     1 
ATOM   8129  C  CB    . ARG   A  1  1103 ? 6.081   77.295  98.433  1.00 19.27 ? 1101 ARG   A CB    1 
ATOM   8130  C  CG    . ARG   A  1  1103 ? 7.538   77.595  98.812  1.00 21.94 ? 1101 ARG   A CG    1 
ATOM   8131  C  CD    . ARG   A  1  1103 ? 8.294   78.448  97.796  1.00 24.67 ? 1101 ARG   A CD    1 
ATOM   8132  N  NE    . ARG   A  1  1103 ? 8.366   77.816  96.481  1.00 28.21 ? 1101 ARG   A NE    1 
ATOM   8133  C  CZ    . ARG   A  1  1103 ? 9.387   77.103  96.016  1.00 33.37 ? 1101 ARG   A CZ    1 
ATOM   8134  N  NH1   . ARG   A  1  1103 ? 10.472  76.861  96.749  1.00 25.85 ? 1101 ARG   A NH1   1 
ATOM   8135  N  NH2   . ARG   A  1  1103 ? 9.319   76.617  94.778  1.00 32.80 ? 1101 ARG   A NH2   1 
ATOM   8136  N  N     . ILE   A  1  1104 ? 6.075   76.013  101.634 1.00 15.68 ? 1102 ILE   A N     1 
ATOM   8137  C  CA    . ILE   A  1  1104 ? 6.010   76.325  103.053 1.00 16.17 ? 1102 ILE   A CA    1 
ATOM   8138  C  C     . ILE   A  1  1104 ? 7.130   77.298  103.373 1.00 16.61 ? 1102 ILE   A C     1 
ATOM   8139  O  O     . ILE   A  1  1104 ? 8.287   77.069  102.996 1.00 16.55 ? 1102 ILE   A O     1 
ATOM   8140  C  CB    . ILE   A  1  1104 ? 6.139   75.049  103.900 1.00 16.94 ? 1102 ILE   A CB    1 
ATOM   8141  C  CG1   . ILE   A  1  1104 ? 5.106   74.000  103.460 1.00 17.33 ? 1102 ILE   A CG1   1 
ATOM   8142  C  CG2   . ILE   A  1  1104 ? 5.991   75.386  105.388 1.00 17.10 ? 1102 ILE   A CG2   1 
ATOM   8143  C  CD1   . ILE   A  1  1104 ? 3.675   74.421  103.653 1.00 18.80 ? 1102 ILE   A CD1   1 
ATOM   8144  N  N     . LEU   A  1  1105 ? 6.791   78.389  104.056 1.00 15.53 ? 1103 LEU   A N     1 
ATOM   8145  C  CA    . LEU   A  1  1105 ? 7.805   79.298  104.567 1.00 17.59 ? 1103 LEU   A CA    1 
ATOM   8146  C  C     . LEU   A  1  1105 ? 8.452   78.687  105.803 1.00 15.24 ? 1103 LEU   A C     1 
ATOM   8147  O  O     . LEU   A  1  1105 ? 7.760   78.377  106.778 1.00 18.19 ? 1103 LEU   A O     1 
ATOM   8148  C  CB    . LEU   A  1  1105 ? 7.154   80.629  104.925 1.00 19.55 ? 1103 LEU   A CB    1 
ATOM   8149  C  CG    . LEU   A  1  1105 ? 8.086   81.669  105.555 1.00 20.64 ? 1103 LEU   A CG    1 
ATOM   8150  C  CD1   . LEU   A  1  1105 ? 9.180   82.082  104.574 1.00 21.89 ? 1103 LEU   A CD1   1 
ATOM   8151  C  CD2   . LEU   A  1  1105 ? 7.279   82.872  106.014 1.00 22.39 ? 1103 LEU   A CD2   1 
ATOM   8152  N  N     . LEU   A  1  1106 ? 9.767   78.525  105.776 1.00 16.08 ? 1104 LEU   A N     1 
ATOM   8153  C  CA    . LEU   A  1  1106 ? 10.508  78.041  106.931 1.00 17.56 ? 1104 LEU   A CA    1 
ATOM   8154  C  C     . LEU   A  1  1106 ? 11.250  79.204  107.559 1.00 21.36 ? 1104 LEU   A C     1 
ATOM   8155  O  O     . LEU   A  1  1106 ? 12.004  79.906  106.879 1.00 18.90 ? 1104 LEU   A O     1 
ATOM   8156  C  CB    . LEU   A  1  1106 ? 11.527  76.977  106.545 1.00 17.08 ? 1104 LEU   A CB    1 
ATOM   8157  C  CG    . LEU   A  1  1106 ? 10.994  75.739  105.843 1.00 22.60 ? 1104 LEU   A CG    1 
ATOM   8158  C  CD1   . LEU   A  1  1106 ? 12.041  74.639  105.833 1.00 19.01 ? 1104 LEU   A CD1   1 
ATOM   8159  C  CD2   . LEU   A  1  1106 ? 9.702   75.244  106.444 1.00 22.21 ? 1104 LEU   A CD2   1 
ATOM   8160  N  N     . VAL   A  1  1107 ? 11.047  79.389  108.854 1.00 18.01 ? 1105 VAL   A N     1 
ATOM   8161  C  CA    . VAL   A  1  1107 ? 11.752  80.421  109.601 1.00 17.58 ? 1105 VAL   A CA    1 
ATOM   8162  C  C     . VAL   A  1  1107 ? 12.512  79.706  110.707 1.00 18.47 ? 1105 VAL   A C     1 
ATOM   8163  O  O     . VAL   A  1  1107 ? 12.025  79.609  111.840 1.00 19.38 ? 1105 VAL   A O     1 
ATOM   8164  C  CB    . VAL   A  1  1107 ? 10.777  81.486  110.125 1.00 18.81 ? 1105 VAL   A CB    1 
ATOM   8165  C  CG1   . VAL   A  1  1107 ? 11.547  82.656  110.715 1.00 21.37 ? 1105 VAL   A CG1   1 
ATOM   8166  C  CG2   . VAL   A  1  1107 ? 9.850   81.942  108.990 1.00 20.76 ? 1105 VAL   A CG2   1 
ATOM   8167  N  N     . PRO   A  1  1108 ? 13.679  79.158  110.410 1.00 17.31 ? 1106 PRO   A N     1 
ATOM   8168  C  CA    . PRO   A  1  1108 ? 14.430  78.404  111.411 1.00 20.34 ? 1106 PRO   A CA    1 
ATOM   8169  C  C     . PRO   A  1  1108 ? 15.264  79.344  112.259 1.00 21.30 ? 1106 PRO   A C     1 
ATOM   8170  O  O     . PRO   A  1  1108 ? 15.473  80.509  111.922 1.00 21.25 ? 1106 PRO   A O     1 
ATOM   8171  C  CB    . PRO   A  1  1108 ? 15.347  77.528  110.554 1.00 19.81 ? 1106 PRO   A CB    1 
ATOM   8172  C  CG    . PRO   A  1  1108 ? 15.585  78.366  109.329 1.00 19.71 ? 1106 PRO   A CG    1 
ATOM   8173  C  CD    . PRO   A  1  1108 ? 14.276  79.049  109.066 1.00 21.18 ? 1106 PRO   A CD    1 
ATOM   8174  N  N     . ALA   A  1  1109 ? 15.729  78.813  113.381 1.00 17.89 ? 1107 ALA   A N     1 
ATOM   8175  C  CA    . ALA   A  1  1109 ? 16.689  79.502  114.228 1.00 21.38 ? 1107 ALA   A CA    1 
ATOM   8176  C  C     . ALA   A  1  1109 ? 18.002  78.758  114.355 1.00 24.77 ? 1107 ALA   A C     1 
ATOM   8177  O  O     . ALA   A  1  1109 ? 19.053  79.391  114.485 1.00 25.43 ? 1107 ALA   A O     1 
ATOM   8178  C  CB    . ALA   A  1  1109 ? 16.108  79.729  115.635 1.00 21.30 ? 1107 ALA   A CB    1 
ATOM   8179  N  N     . THR   A  1  1110 ? 17.973  77.433  114.320 1.00 20.03 ? 1108 THR   A N     1 
ATOM   8180  C  CA    . THR   A  1  1110 ? 19.156  76.611  114.458 1.00 20.14 ? 1108 THR   A CA    1 
ATOM   8181  C  C     . THR   A  1  1110 ? 19.230  75.656  113.280 1.00 19.98 ? 1108 THR   A C     1 
ATOM   8182  O  O     . THR   A  1  1110 ? 18.237  75.393  112.595 1.00 18.96 ? 1108 THR   A O     1 
ATOM   8183  C  CB    . THR   A  1  1110 ? 19.141  75.795  115.756 1.00 21.42 ? 1108 THR   A CB    1 
ATOM   8184  O  OG1   . THR   A  1  1110 ? 18.045  74.870  115.730 1.00 20.82 ? 1108 THR   A OG1   1 
ATOM   8185  C  CG2   . THR   A  1  1110 ? 18.982  76.717  116.956 1.00 21.80 ? 1108 THR   A CG2   1 
ATOM   8186  N  N     . GLU   A  1  1111 ? 20.428  75.130  113.057 1.00 21.57 ? 1109 GLU   A N     1 
ATOM   8187  C  CA    . GLU   A  1  1111 ? 20.608  74.143  111.998 1.00 19.10 ? 1109 GLU   A CA    1 
ATOM   8188  C  C     . GLU   A  1  1111 ? 19.720  72.926  112.225 1.00 20.39 ? 1109 GLU   A C     1 
ATOM   8189  O  O     . GLU   A  1  1111 ? 19.049  72.456  111.300 1.00 19.84 ? 1109 GLU   A O     1 
ATOM   8190  C  CB    . GLU   A  1  1111 ? 22.075  73.739  111.926 1.00 22.54 ? 1109 GLU   A CB    1 
ATOM   8191  C  CG    . GLU   A  1  1111 ? 22.307  72.534  111.041 1.00 22.16 ? 1109 GLU   A CG    1 
ATOM   8192  C  CD    . GLU   A  1  1111 ? 23.774  72.232  110.867 1.00 24.90 ? 1109 GLU   A CD    1 
ATOM   8193  O  OE1   . GLU   A  1  1111 ? 24.451  73.020  110.179 1.00 28.57 ? 1109 GLU   A OE1   1 
ATOM   8194  O  OE2   . GLU   A  1  1111 ? 24.240  71.220  111.420 1.00 30.33 ? 1109 GLU   A OE2   1 
ATOM   8195  N  N     . SER   A  1  1112 ? 19.693  72.400  113.451 1.00 20.09 ? 1110 SER   A N     1 
ATOM   8196  C  CA    . SER   A  1  1112 ? 18.843  71.243  113.721 1.00 19.40 ? 1110 SER   A CA    1 
ATOM   8197  C  C     . SER   A  1  1112 ? 17.376  71.584  113.515 1.00 20.32 ? 1110 SER   A C     1 
ATOM   8198  O  O     . SER   A  1  1112 ? 16.620  70.789  112.947 1.00 19.85 ? 1110 SER   A O     1 
ATOM   8199  C  CB    . SER   A  1  1112 ? 19.076  70.712  115.135 1.00 23.95 ? 1110 SER   A CB    1 
ATOM   8200  O  OG    . SER   A  1  1112 ? 18.327  69.525  115.343 1.00 22.55 ? 1110 SER   A OG    1 
ATOM   8201  N  N     . GLY   A  1  1113 ? 16.956  72.769  113.959 1.00 19.02 ? 1111 GLY   A N     1 
ATOM   8202  C  CA    . GLY   A  1  1113 ? 15.590  73.188  113.710 1.00 17.33 ? 1111 GLY   A CA    1 
ATOM   8203  C  C     . GLY   A  1  1113 ? 15.277  73.251  112.229 1.00 16.56 ? 1111 GLY   A C     1 
ATOM   8204  O  O     . GLY   A  1  1113 ? 14.214  72.802  111.787 1.00 17.76 ? 1111 GLY   A O     1 
ATOM   8205  N  N     . LEU   A  1  1114 ? 16.208  73.792  111.439 1.00 17.80 ? 1112 LEU   A N     1 
ATOM   8206  C  CA    . LEU   A  1  1114 ? 16.012  73.838  109.995 1.00 18.41 ? 1112 LEU   A CA    1 
ATOM   8207  C  C     . LEU   A  1  1114 ? 15.869  72.439  109.421 1.00 16.55 ? 1112 LEU   A C     1 
ATOM   8208  O  O     . LEU   A  1  1114 ? 14.989  72.198  108.589 1.00 16.13 ? 1112 LEU   A O     1 
ATOM   8209  C  CB    . LEU   A  1  1114 ? 17.181  74.557  109.322 1.00 18.48 ? 1112 LEU   A CB    1 
ATOM   8210  C  CG    . LEU   A  1  1114 ? 17.149  74.518  107.791 1.00 19.59 ? 1112 LEU   A CG    1 
ATOM   8211  C  CD1   . LEU   A  1  1114 ? 15.829  75.076  107.246 1.00 20.87 ? 1112 LEU   A CD1   1 
ATOM   8212  C  CD2   . LEU   A  1  1114 ? 18.341  75.274  107.224 1.00 22.53 ? 1112 LEU   A CD2   1 
ATOM   8213  N  N     . TYR   A  1  1115 ? 16.718  71.505  109.851 1.00 17.75 ? 1113 TYR   A N     1 
ATOM   8214  C  CA    . TYR   A  1  1115 ? 16.629  70.152  109.315 1.00 17.97 ? 1113 TYR   A CA    1 
ATOM   8215  C  C     . TYR   A  1  1115 ? 15.294  69.512  109.675 1.00 17.41 ? 1113 TYR   A C     1 
ATOM   8216  O  O     . TYR   A  1  1115 ? 14.694  68.811  108.854 1.00 16.58 ? 1113 TYR   A O     1 
ATOM   8217  C  CB    . TYR   A  1  1115 ? 17.782  69.302  109.834 1.00 17.25 ? 1113 TYR   A CB    1 
ATOM   8218  C  CG    . TYR   A  1  1115 ? 19.154  69.708  109.334 1.00 16.97 ? 1113 TYR   A CG    1 
ATOM   8219  C  CD1   . TYR   A  1  1115 ? 19.302  70.570  108.255 1.00 18.42 ? 1113 TYR   A CD1   1 
ATOM   8220  C  CD2   . TYR   A  1  1115 ? 20.299  69.229  109.952 1.00 20.47 ? 1113 TYR   A CD2   1 
ATOM   8221  C  CE1   . TYR   A  1  1115 ? 20.567  70.934  107.790 1.00 21.04 ? 1113 TYR   A CE1   1 
ATOM   8222  C  CE2   . TYR   A  1  1115 ? 21.559  69.578  109.491 1.00 19.58 ? 1113 TYR   A CE2   1 
ATOM   8223  C  CZ    . TYR   A  1  1115 ? 21.680  70.435  108.417 1.00 22.58 ? 1113 TYR   A CZ    1 
ATOM   8224  O  OH    . TYR   A  1  1115 ? 22.942  70.794  107.981 1.00 22.43 ? 1113 TYR   A OH    1 
ATOM   8225  N  N     . HIS   A  1  1116 ? 14.814  69.741  110.897 1.00 17.10 ? 1114 HIS   A N     1 
ATOM   8226  C  CA    . HIS   A  1  1116 ? 13.516  69.212  111.293 1.00 17.11 ? 1114 HIS   A CA    1 
ATOM   8227  C  C     . HIS   A  1  1116 ? 12.390  69.868  110.509 1.00 16.86 ? 1114 HIS   A C     1 
ATOM   8228  O  O     . HIS   A  1  1116 ? 11.426  69.201  110.114 1.00 17.04 ? 1114 HIS   A O     1 
ATOM   8229  C  CB    . HIS   A  1  1116 ? 13.301  69.411  112.794 1.00 19.23 ? 1114 HIS   A CB    1 
ATOM   8230  C  CG    . HIS   A  1  1116 ? 13.935  68.355  113.645 1.00 19.80 ? 1114 HIS   A CG    1 
ATOM   8231  N  ND1   . HIS   A  1  1116 ? 15.230  68.449  114.111 1.00 22.55 ? 1114 HIS   A ND1   1 
ATOM   8232  C  CD2   . HIS   A  1  1116 ? 13.448  67.186  114.124 1.00 21.11 ? 1114 HIS   A CD2   1 
ATOM   8233  C  CE1   . HIS   A  1  1116 ? 15.513  67.379  114.834 1.00 22.92 ? 1114 HIS   A CE1   1 
ATOM   8234  N  NE2   . HIS   A  1  1116 ? 14.450  66.599  114.857 1.00 25.77 ? 1114 HIS   A NE2   1 
ATOM   8235  N  N     . GLN   A  1  1117 ? 12.469  71.182  110.304 1.00 15.59 ? 1115 GLN   A N     1 
ATOM   8236  C  CA    . GLN   A  1  1117 ? 11.438  71.857  109.530 1.00 16.86 ? 1115 GLN   A CA    1 
ATOM   8237  C  C     . GLN   A  1  1117 ? 11.424  71.346  108.106 1.00 14.46 ? 1115 GLN   A C     1 
ATOM   8238  O  O     . GLN   A  1  1117 ? 10.355  71.109  107.528 1.00 15.70 ? 1115 GLN   A O     1 
ATOM   8239  C  CB    . GLN   A  1  1117 ? 11.693  73.359  109.513 1.00 17.10 ? 1115 GLN   A CB    1 
ATOM   8240  C  CG    . GLN   A  1  1117 ? 11.467  74.032  110.831 1.00 17.17 ? 1115 GLN   A CG    1 
ATOM   8241  C  CD    . GLN   A  1  1117 ? 11.737  75.513  110.751 1.00 20.35 ? 1115 GLN   A CD    1 
ATOM   8242  O  OE1   . GLN   A  1  1117 ? 12.318  75.992  109.774 1.00 18.77 ? 1115 GLN   A OE1   1 
ATOM   8243  N  NE2   . GLN   A  1  1117 ? 11.329  76.251  111.782 1.00 18.25 ? 1115 GLN   A NE2   1 
ATOM   8244  N  N     . LEU   A  1  1118 ? 12.607  71.216  107.508 1.00 14.81 ? 1116 LEU   A N     1 
ATOM   8245  C  CA    A LEU   A  1  1118 ? 12.684  70.733  106.140 0.51 16.08 ? 1116 LEU   A CA    1 
ATOM   8246  C  CA    B LEU   A  1  1118 ? 12.700  70.719  106.141 0.49 16.09 ? 1116 LEU   A CA    1 
ATOM   8247  C  C     . LEU   A  1  1118 ? 12.159  69.307  106.045 1.00 14.62 ? 1116 LEU   A C     1 
ATOM   8248  O  O     . LEU   A  1  1118 ? 11.444  68.967  105.097 1.00 15.66 ? 1116 LEU   A O     1 
ATOM   8249  C  CB    A LEU   A  1  1118 ? 14.128  70.845  105.650 0.51 16.81 ? 1116 LEU   A CB    1 
ATOM   8250  C  CB    B LEU   A  1  1118 ? 14.157  70.725  105.694 0.49 16.87 ? 1116 LEU   A CB    1 
ATOM   8251  C  CG    A LEU   A  1  1118 ? 14.430  70.643  104.171 0.51 17.24 ? 1116 LEU   A CG    1 
ATOM   8252  C  CG    B LEU   A  1  1118 ? 14.723  72.060  105.258 0.49 16.64 ? 1116 LEU   A CG    1 
ATOM   8253  C  CD1   A LEU   A  1  1118 ? 13.450  71.409  103.295 0.51 17.62 ? 1116 LEU   A CD1   1 
ATOM   8254  C  CD1   B LEU   A  1  1118 ? 16.222  71.918  105.167 0.49 15.97 ? 1116 LEU   A CD1   1 
ATOM   8255  C  CD2   A LEU   A  1  1118 ? 15.846  71.118  103.910 0.51 18.70 ? 1116 LEU   A CD2   1 
ATOM   8256  C  CD2   B LEU   A  1  1118 ? 14.130  72.449  103.915 0.49 17.75 ? 1116 LEU   A CD2   1 
ATOM   8257  N  N     . ALA   A  1  1119 ? 12.487  68.467  107.019 1.00 16.48 ? 1117 ALA   A N     1 
ATOM   8258  C  CA    . ALA   A  1  1119 ? 11.987  67.098  106.987 1.00 17.42 ? 1117 ALA   A CA    1 
ATOM   8259  C  C     . ALA   A  1  1119 ? 10.470  67.082  107.039 1.00 17.37 ? 1117 ALA   A C     1 
ATOM   8260  O  O     . ALA   A  1  1119 ? 9.821   66.370  106.265 1.00 16.36 ? 1117 ALA   A O     1 
ATOM   8261  C  CB    . ALA   A  1  1119 ? 12.566  66.301  108.150 1.00 19.06 ? 1117 ALA   A CB    1 
ATOM   8262  N  N     . ALA   A  1  1120 ? 9.883   67.891  107.922 1.00 15.98 ? 1118 ALA   A N     1 
ATOM   8263  C  CA    . ALA   A  1  1120 ? 8.429   67.924  108.025 1.00 15.82 ? 1118 ALA   A CA    1 
ATOM   8264  C  C     . ALA   A  1  1120 ? 7.810   68.383  106.715 1.00 16.22 ? 1118 ALA   A C     1 
ATOM   8265  O  O     . ALA   A  1  1120 ? 6.840   67.786  106.226 1.00 15.02 ? 1118 ALA   A O     1 
ATOM   8266  C  CB    . ALA   A  1  1120 ? 8.014   68.851  109.166 1.00 15.19 ? 1118 ALA   A CB    1 
ATOM   8267  N  N     . ALA   A  1  1121 ? 8.371   69.434  106.124 1.00 14.87 ? 1119 ALA   A N     1 
ATOM   8268  C  CA    . ALA   A  1  1121 ? 7.805   69.988  104.906 1.00 14.72 ? 1119 ALA   A CA    1 
ATOM   8269  C  C     . ALA   A  1  1121 ? 7.985   69.041  103.731 1.00 14.34 ? 1119 ALA   A C     1 
ATOM   8270  O  O     . ALA   A  1  1121 ? 7.067   68.865  102.927 1.00 14.79 ? 1119 ALA   A O     1 
ATOM   8271  C  CB    . ALA   A  1  1121 ? 8.458   71.335  104.613 1.00 16.22 ? 1119 ALA   A CB    1 
ATOM   8272  N  N     . LEU   A  1  1122 ? 9.170   68.454  103.594 1.00 14.52 ? 1120 LEU   A N     1 
ATOM   8273  C  CA    . LEU   A  1  1122 ? 9.420   67.556  102.469 1.00 13.95 ? 1120 LEU   A CA    1 
ATOM   8274  C  C     . LEU   A  1  1122 ? 8.625   66.267  102.594 1.00 14.89 ? 1120 LEU   A C     1 
ATOM   8275  O  O     . LEU   A  1  1122 ? 8.144   65.735  101.589 1.00 15.06 ? 1120 LEU   A O     1 
ATOM   8276  C  CB    . LEU   A  1  1122 ? 10.909  67.246  102.357 1.00 16.22 ? 1120 LEU   A CB    1 
ATOM   8277  C  CG    . LEU   A  1  1122 ? 11.823  68.423  102.033 1.00 16.12 ? 1120 LEU   A CG    1 
ATOM   8278  C  CD1   . LEU   A  1  1122 ? 13.248  67.944  102.038 1.00 17.74 ? 1120 LEU   A CD1   1 
ATOM   8279  C  CD2   . LEU   A  1  1122 ? 11.453  69.032  100.683 1.00 18.09 ? 1120 LEU   A CD2   1 
ATOM   8280  N  N     . ALA   A  1  1123 ? 8.488   65.742  103.813 1.00 14.81 ? 1121 ALA   A N     1 
ATOM   8281  C  CA    . ALA   A  1  1123 ? 7.727   64.515  104.020 1.00 13.64 ? 1121 ALA   A CA    1 
ATOM   8282  C  C     . ALA   A  1  1123 ? 6.279   64.677  103.607 1.00 14.91 ? 1121 ALA   A C     1 
ATOM   8283  O  O     . ALA   A  1  1123 ? 5.619   63.680  103.304 1.00 15.03 ? 1121 ALA   A O     1 
ATOM   8284  C  CB    . ALA   A  1  1123 ? 7.773   64.123  105.502 1.00 14.66 ? 1121 ALA   A CB    1 
ATOM   8285  N  N     . THR   A  1  1124 ? 5.773   65.905  103.608 1.00 14.16 ? 1122 THR   A N     1 
ATOM   8286  C  CA    . THR   A  1  1124 ? 4.405   66.191  103.222 1.00 13.45 ? 1122 THR   A CA    1 
ATOM   8287  C  C     . THR   A  1  1124 ? 4.329   66.750  101.808 1.00 14.49 ? 1122 THR   A C     1 
ATOM   8288  O  O     . THR   A  1  1124 ? 3.290   67.284  101.402 1.00 15.02 ? 1122 THR   A O     1 
ATOM   8289  C  CB    . THR   A  1  1124 ? 3.749   67.098  104.268 1.00 15.32 ? 1122 THR   A CB    1 
ATOM   8290  O  OG1   . THR   A  1  1124 ? 4.636   68.182  104.575 1.00 14.98 ? 1122 THR   A OG1   1 
ATOM   8291  C  CG2   . THR   A  1  1124 ? 3.491   66.302  105.542 1.00 16.76 ? 1122 THR   A CG2   1 
ATOM   8292  N  N     . GLY   A  1  1125 ? 5.410   66.596  101.036 1.00 14.01 ? 1123 GLY   A N     1 
ATOM   8293  C  CA    . GLY   A  1  1125 ? 5.382   66.857  99.609  1.00 15.67 ? 1123 GLY   A CA    1 
ATOM   8294  C  C     . GLY   A  1  1125 ? 5.619   68.293  99.216  1.00 13.91 ? 1123 GLY   A C     1 
ATOM   8295  O  O     . GLY   A  1  1125 ? 5.522   68.624  98.024  1.00 16.09 ? 1123 GLY   A O     1 
ATOM   8296  N  N     . ASN   A  1  1126 ? 5.918   69.159  100.169 1.00 14.81 ? 1124 ASN   A N     1 
ATOM   8297  C  CA    . ASN   A  1  1126 ? 5.978   70.581  99.904  1.00 15.47 ? 1124 ASN   A CA    1 
ATOM   8298  C  C     . ASN   A  1  1126 ? 7.352   71.001  99.418  1.00 14.15 ? 1124 ASN   A C     1 
ATOM   8299  O  O     . ASN   A  1  1126 ? 8.364   70.334  99.647  1.00 16.41 ? 1124 ASN   A O     1 
ATOM   8300  C  CB    . ASN   A  1  1126 ? 5.695   71.340  101.191 1.00 14.22 ? 1124 ASN   A CB    1 
ATOM   8301  C  CG    . ASN   A  1  1126 ? 4.323   71.056  101.714 1.00 14.71 ? 1124 ASN   A CG    1 
ATOM   8302  O  OD1   . ASN   A  1  1126 ? 3.334   71.448  101.103 1.00 17.13 ? 1124 ASN   A OD1   1 
ATOM   8303  N  ND2   . ASN   A  1  1126 ? 4.247   70.349  102.834 1.00 14.91 ? 1124 ASN   A ND2   1 
ATOM   8304  N  N     . SER   A  1  1127 ? 7.371   72.151  98.763  1.00 15.79 ? 1125 SER   A N     1 
ATOM   8305  C  CA    . SER   A  1  1127 ? 8.613   72.887  98.611  1.00 16.21 ? 1125 SER   A CA    1 
ATOM   8306  C  C     . SER   A  1  1127 ? 8.716   73.882  99.759  1.00 15.80 ? 1125 SER   A C     1 
ATOM   8307  O  O     . SER   A  1  1127 ? 7.786   74.045  100.548 1.00 16.33 ? 1125 SER   A O     1 
ATOM   8308  C  CB    . SER   A  1  1127 ? 8.643   73.614  97.272  1.00 17.58 ? 1125 SER   A CB    1 
ATOM   8309  O  OG    . SER   A  1  1127 ? 7.611   74.571  97.190  1.00 22.61 ? 1125 SER   A OG    1 
ATOM   8310  N  N     . VAL   A  1  1128 ? 9.862   74.544  99.870  1.00 17.12 ? 1126 VAL   A N     1 
ATOM   8311  C  CA    . VAL   A  1  1128 ? 10.074  75.473  100.971 1.00 16.72 ? 1126 VAL   A CA    1 
ATOM   8312  C  C     . VAL   A  1  1128 ? 10.736  76.740  100.470 1.00 18.68 ? 1126 VAL   A C     1 
ATOM   8313  O  O     . VAL   A  1  1128 ? 11.491  76.734  99.492  1.00 19.25 ? 1126 VAL   A O     1 
ATOM   8314  C  CB    . VAL   A  1  1128 ? 10.916  74.864  102.109 1.00 18.76 ? 1126 VAL   A CB    1 
ATOM   8315  C  CG1   . VAL   A  1  1128 ? 10.264  73.608  102.648 1.00 18.15 ? 1126 VAL   A CG1   1 
ATOM   8316  C  CG2   . VAL   A  1  1128 ? 12.325  74.566  101.611 1.00 18.98 ? 1126 VAL   A CG2   1 
ATOM   8317  N  N     . ALA   A  1  1129 ? 10.452  77.832  101.165 1.00 17.31 ? 1127 ALA   A N     1 
ATOM   8318  C  CA    . ALA   A  1  1129 ? 11.265  79.037  101.105 1.00 17.70 ? 1127 ALA   A CA    1 
ATOM   8319  C  C     . ALA   A  1  1129 ? 11.816  79.238  102.503 1.00 17.07 ? 1127 ALA   A C     1 
ATOM   8320  O  O     . ALA   A  1  1129 ? 11.045  79.379  103.459 1.00 19.79 ? 1127 ALA   A O     1 
ATOM   8321  C  CB    . ALA   A  1  1129 ? 10.437  80.247  100.690 1.00 22.98 ? 1127 ALA   A CB    1 
ATOM   8322  N  N     . ILE   A  1  1130 ? 13.133  79.225  102.626 1.00 18.18 ? 1128 ILE   A N     1 
ATOM   8323  C  CA    . ILE   A  1  1130 ? 13.787  79.334  103.921 1.00 18.44 ? 1128 ILE   A CA    1 
ATOM   8324  C  C     . ILE   A  1  1130 ? 14.180  80.782  104.138 1.00 23.05 ? 1128 ILE   A C     1 
ATOM   8325  O  O     . ILE   A  1  1130 ? 14.775  81.411  103.255 1.00 22.06 ? 1128 ILE   A O     1 
ATOM   8326  C  CB    . ILE   A  1  1130 ? 15.021  78.427  104.010 1.00 17.95 ? 1128 ILE   A CB    1 
ATOM   8327  C  CG1   . ILE   A  1  1130 ? 14.663  77.011  103.579 1.00 19.93 ? 1128 ILE   A CG1   1 
ATOM   8328  C  CG2   . ILE   A  1  1130 ? 15.567  78.434  105.437 1.00 19.70 ? 1128 ILE   A CG2   1 
ATOM   8329  C  CD1   . ILE   A  1  1130 ? 15.874  76.145  103.426 1.00 20.24 ? 1128 ILE   A CD1   1 
ATOM   8330  N  N     . ASP   A  1  1131 ? 13.876  81.300  105.323 1.00 20.58 ? 1129 ASP   A N     1 
ATOM   8331  C  CA    . ASP   A  1  1131 ? 14.241  82.662  105.679 1.00 21.43 ? 1129 ASP   A CA    1 
ATOM   8332  C  C     . ASP   A  1  1131 ? 15.745  82.860  105.557 1.00 22.44 ? 1129 ASP   A C     1 
ATOM   8333  O  O     . ASP   A  1  1131 ? 16.518  82.252  106.300 1.00 22.19 ? 1129 ASP   A O     1 
ATOM   8334  C  CB    . ASP   A  1  1131 ? 13.805  82.946  107.110 1.00 20.96 ? 1129 ASP   A CB    1 
ATOM   8335  C  CG    . ASP   A  1  1131 ? 14.163  84.334  107.552 1.00 28.73 ? 1129 ASP   A CG    1 
ATOM   8336  O  OD1   . ASP   A  1  1131 ? 14.248  85.220  106.677 1.00 22.94 ? 1129 ASP   A OD1   1 
ATOM   8337  O  OD2   . ASP   A  1  1131 ? 14.364  84.536  108.767 1.00 24.89 ? 1129 ASP   A OD2   1 
ATOM   8338  N  N     . ALA   A  1  1132 ? 16.166  83.704  104.616 1.00 23.11 ? 1130 ALA   A N     1 
ATOM   8339  C  CA    . ALA   A  1  1132 ? 17.585  83.961  104.428 1.00 27.04 ? 1130 ALA   A CA    1 
ATOM   8340  C  C     . ALA   A  1  1132 ? 18.189  84.705  105.608 1.00 28.64 ? 1130 ALA   A C     1 
ATOM   8341  O  O     . ALA   A  1  1132 ? 19.394  84.585  105.849 1.00 27.59 ? 1130 ALA   A O     1 
ATOM   8342  C  CB    . ALA   A  1  1132 ? 17.804  84.746  103.136 1.00 27.77 ? 1130 ALA   A CB    1 
ATOM   8343  N  N     . ALA   A  1  1133 ? 17.380  85.455  106.358 1.00 25.16 ? 1131 ALA   A N     1 
ATOM   8344  C  CA    . ALA   A  1  1133 ? 17.889  86.168  107.525 1.00 26.51 ? 1131 ALA   A CA    1 
ATOM   8345  C  C     . ALA   A  1  1133 ? 18.265  85.238  108.670 1.00 28.35 ? 1131 ALA   A C     1 
ATOM   8346  O  O     . ALA   A  1  1133 ? 18.839  85.702  109.658 1.00 28.25 ? 1131 ALA   A O     1 
ATOM   8347  C  CB    . ALA   A  1  1133 ? 16.869  87.209  107.993 1.00 28.89 ? 1131 ALA   A CB    1 
ATOM   8348  N  N     . SER   A  1  1134 ? 17.968  83.942  108.563 1.00 26.84 ? 1132 SER   A N     1 
ATOM   8349  C  CA    . SER   A  1  1134 ? 18.387  82.988  109.578 1.00 23.91 ? 1132 SER   A CA    1 
ATOM   8350  C  C     . SER   A  1  1134 ? 19.893  82.776  109.576 1.00 24.45 ? 1132 SER   A C     1 
ATOM   8351  O  O     . SER   A  1  1134 ? 20.432  82.257  110.557 1.00 24.76 ? 1132 SER   A O     1 
ATOM   8352  C  CB    . SER   A  1  1134 ? 17.710  81.641  109.326 1.00 24.27 ? 1132 SER   A CB    1 
ATOM   8353  O  OG    . SER   A  1  1134 ? 18.181  81.060  108.115 1.00 23.73 ? 1132 SER   A OG    1 
ATOM   8354  N  N     . GLY   A  1  1135 ? 20.568  83.138  108.486 1.00 26.83 ? 1133 GLY   A N     1 
ATOM   8355  C  CA    . GLY   A  1  1135 ? 21.995  82.921  108.373 1.00 25.58 ? 1133 GLY   A CA    1 
ATOM   8356  C  C     . GLY   A  1  1135 ? 22.401  81.471  108.295 1.00 26.80 ? 1133 GLY   A C     1 
ATOM   8357  O  O     . GLY   A  1  1135 ? 23.567  81.149  108.522 1.00 27.87 ? 1133 GLY   A O     1 
ATOM   8358  N  N     . LEU   A  1  1136 ? 21.469  80.577  107.970 1.00 23.12 ? 1134 LEU   A N     1 
ATOM   8359  C  CA    . LEU   A  1  1136 ? 21.742  79.148  108.000 1.00 24.77 ? 1134 LEU   A CA    1 
ATOM   8360  C  C     . LEU   A  1  1136 ? 22.081  78.578  106.629 1.00 24.89 ? 1134 LEU   A C     1 
ATOM   8361  O  O     . LEU   A  1  1136 ? 22.066  77.355  106.461 1.00 24.00 ? 1134 LEU   A O     1 
ATOM   8362  C  CB    . LEU   A  1  1136 ? 20.563  78.394  108.616 1.00 24.45 ? 1134 LEU   A CB    1 
ATOM   8363  C  CG    . LEU   A  1  1136 ? 20.333  78.635  110.107 1.00 23.16 ? 1134 LEU   A CG    1 
ATOM   8364  C  CD1   . LEU   A  1  1136 ? 19.035  77.966  110.555 1.00 22.86 ? 1134 LEU   A CD1   1 
ATOM   8365  C  CD2   . LEU   A  1  1136 ? 21.506  78.124  110.914 1.00 26.00 ? 1134 LEU   A CD2   1 
ATOM   8366  N  N     . GLN   A  1  1137 ? 22.403  79.437  105.656 1.00 25.55 ? 1135 GLN   A N     1 
ATOM   8367  C  CA    . GLN   A  1  1137 ? 22.711  78.960  104.308 1.00 27.90 ? 1135 GLN   A CA    1 
ATOM   8368  C  C     . GLN   A  1  1137 ? 23.779  77.868  104.313 1.00 24.77 ? 1135 GLN   A C     1 
ATOM   8369  O  O     . GLN   A  1  1137 ? 23.666  76.879  103.577 1.00 26.85 ? 1135 GLN   A O     1 
ATOM   8370  C  CB    . GLN   A  1  1137 ? 23.140  80.120  103.406 1.00 27.44 ? 1135 GLN   A CB    1 
ATOM   8371  C  CG    . GLN   A  1  1137 ? 22.014  81.025  102.941 1.00 27.51 ? 1135 GLN   A CG    1 
ATOM   8372  C  CD    . GLN   A  1  1137 ? 21.646  82.071  103.974 1.00 27.67 ? 1135 GLN   A CD    1 
ATOM   8373  O  OE1   . GLN   A  1  1137 ? 22.121  82.031  105.111 1.00 30.71 ? 1135 GLN   A OE1   1 
ATOM   8374  N  NE2   . GLN   A  1  1137 ? 20.803  83.017  103.583 1.00 32.48 ? 1135 GLN   A NE2   1 
ATOM   8375  N  N     . ALA   A  1  1138 ? 24.821  78.019  105.135 1.00 25.25 ? 1136 ALA   A N     1 
ATOM   8376  C  CA    . ALA   A  1  1138 ? 25.900  77.035  105.143 1.00 25.29 ? 1136 ALA   A CA    1 
ATOM   8377  C  C     . ALA   A  1  1138 ? 25.469  75.670  105.663 1.00 28.36 ? 1136 ALA   A C     1 
ATOM   8378  O  O     . ALA   A  1  1138 ? 26.223  74.705  105.510 1.00 32.76 ? 1136 ALA   A O     1 
ATOM   8379  C  CB    . ALA   A  1  1138 ? 27.100  77.538  105.953 1.00 27.38 ? 1136 ALA   A CB    1 
ATOM   8380  N  N     . SER   A  1  1139 ? 24.282  75.559  106.262 1.00 26.43 ? 1137 SER   A N     1 
ATOM   8381  C  CA    . SER   A  1  1139 ? 23.813  74.271  106.753 1.00 25.62 ? 1137 SER   A CA    1 
ATOM   8382  C  C     . SER   A  1  1139 ? 23.225  73.397  105.653 1.00 24.36 ? 1137 SER   A C     1 
ATOM   8383  O  O     . SER   A  1  1139 ? 22.964  72.217  105.905 1.00 26.53 ? 1137 SER   A O     1 
ATOM   8384  C  CB    . SER   A  1  1139 ? 22.765  74.469  107.859 1.00 25.79 ? 1137 SER   A CB    1 
ATOM   8385  O  OG    . SER   A  1  1139 ? 23.338  75.057  109.010 1.00 28.34 ? 1137 SER   A OG    1 
ATOM   8386  N  N     . LEU   A  1  1140 ? 23.005  73.939  104.460 1.00 23.16 ? 1138 LEU   A N     1 
ATOM   8387  C  CA    . LEU   A  1  1140 ? 22.364  73.217  103.366 1.00 25.62 ? 1138 LEU   A CA    1 
ATOM   8388  C  C     . LEU   A  1  1140 ? 23.264  73.136  102.143 1.00 27.48 ? 1138 LEU   A C     1 
ATOM   8389  O  O     . LEU   A  1  1140 ? 22.807  73.259  101.004 1.00 32.53 ? 1138 LEU   A O     1 
ATOM   8390  C  CB    . LEU   A  1  1140 ? 21.023  73.841  102.988 1.00 29.16 ? 1138 LEU   A CB    1 
ATOM   8391  C  CG    . LEU   A  1  1140 ? 19.791  73.546  103.834 1.00 32.78 ? 1138 LEU   A CG    1 
ATOM   8392  C  CD1   . LEU   A  1  1140 ? 18.570  73.948  103.039 1.00 30.24 ? 1138 LEU   A CD1   1 
ATOM   8393  C  CD2   . LEU   A  1  1140 ? 19.710  72.080  104.234 1.00 24.98 ? 1138 LEU   A CD2   1 
ATOM   8394  N  N     . LYS   A  1  1141 ? 24.556  72.925  102.362 1.00 28.06 ? 1139 LYS   A N     1 
ATOM   8395  C  CA    . LYS   A  1  1141 ? 25.501  72.840  101.259 1.00 33.46 ? 1139 LYS   A CA    1 
ATOM   8396  C  C     . LYS   A  1  1141 ? 25.428  71.470  100.591 1.00 31.58 ? 1139 LYS   A C     1 
ATOM   8397  O  O     . LYS   A  1  1141 ? 25.264  70.444  101.257 1.00 29.93 ? 1139 LYS   A O     1 
ATOM   8398  C  CB    . LYS   A  1  1141 ? 26.922  73.092  101.766 1.00 32.50 ? 1139 LYS   A CB    1 
ATOM   8399  N  N     . ASN   A  1  1142 ? 25.544  71.464  99.263  1.00 29.54 ? 1140 ASN   A N     1 
ATOM   8400  C  CA    . ASN   A  1  1142 ? 25.675  70.232  98.481  1.00 28.39 ? 1140 ASN   A CA    1 
ATOM   8401  C  C     . ASN   A  1  1142 ? 24.403  69.383  98.501  1.00 28.23 ? 1140 ASN   A C     1 
ATOM   8402  O  O     . ASN   A  1  1142 ? 24.472  68.152  98.490  1.00 26.35 ? 1140 ASN   A O     1 
ATOM   8403  C  CB    . ASN   A  1  1142 ? 26.890  69.395  98.897  1.00 33.24 ? 1140 ASN   A CB    1 
ATOM   8404  C  CG    . ASN   A  1  1142 ? 28.167  70.207  98.957  1.00 41.16 ? 1140 ASN   A CG    1 
ATOM   8405  O  OD1   . ASN   A  1  1142 ? 28.784  70.337  100.015 1.00 42.24 ? 1140 ASN   A OD1   1 
ATOM   8406  N  ND2   . ASN   A  1  1142 ? 28.574  70.756  97.818  1.00 38.83 ? 1140 ASN   A ND2   1 
ATOM   8407  N  N     . LEU   A  1  1143 ? 23.239  70.029  98.530  1.00 28.60 ? 1141 LEU   A N     1 
ATOM   8408  C  CA    . LEU   A  1  1143 ? 21.999  69.270  98.507  1.00 26.23 ? 1141 LEU   A CA    1 
ATOM   8409  C  C     . LEU   A  1  1143 ? 21.916  68.447  97.226  1.00 28.50 ? 1141 LEU   A C     1 
ATOM   8410  O  O     . LEU   A  1  1143 ? 22.393  68.874  96.170  1.00 27.05 ? 1141 LEU   A O     1 
ATOM   8411  C  CB    . LEU   A  1  1143 ? 20.790  70.200  98.547  1.00 25.15 ? 1141 LEU   A CB    1 
ATOM   8412  C  CG    . LEU   A  1  1143 ? 20.362  70.768  99.892  1.00 26.26 ? 1141 LEU   A CG    1 
ATOM   8413  C  CD1   . LEU   A  1  1143 ? 19.176  71.700  99.681  1.00 24.42 ? 1141 LEU   A CD1   1 
ATOM   8414  C  CD2   . LEU   A  1  1143 ? 20.025  69.648  100.871 1.00 25.13 ? 1141 LEU   A CD2   1 
ATOM   8415  N  N     . PRO   A  1  1144 ? 21.302  67.267  97.285  1.00 25.47 ? 1142 PRO   A N     1 
ATOM   8416  C  CA    . PRO   A  1  1144 ? 20.955  66.573  96.045  1.00 24.43 ? 1142 PRO   A CA    1 
ATOM   8417  C  C     . PRO   A  1  1144 ? 20.063  67.473  95.207  1.00 24.40 ? 1142 PRO   A C     1 
ATOM   8418  O  O     . PRO   A  1  1144 ? 19.275  68.266  95.733  1.00 22.55 ? 1142 PRO   A O     1 
ATOM   8419  C  CB    . PRO   A  1  1144 ? 20.184  65.339  96.533  1.00 29.04 ? 1142 PRO   A CB    1 
ATOM   8420  C  CG    . PRO   A  1  1144 ? 20.548  65.194  97.990  1.00 29.26 ? 1142 PRO   A CG    1 
ATOM   8421  C  CD    . PRO   A  1  1144 ? 20.789  66.579  98.481  1.00 27.34 ? 1142 PRO   A CD    1 
ATOM   8422  N  N     . GLN   A  1  1145 ? 20.197  67.349  93.885  1.00 25.49 ? 1143 GLN   A N     1 
ATOM   8423  C  CA    . GLN   A  1  1145 ? 19.404  68.177  92.982  1.00 26.99 ? 1143 GLN   A CA    1 
ATOM   8424  C  C     . GLN   A  1  1145 ? 17.910  68.056  93.264  1.00 24.14 ? 1143 GLN   A C     1 
ATOM   8425  O  O     . GLN   A  1  1145 ? 17.176  69.045  93.168  1.00 22.51 ? 1143 GLN   A O     1 
ATOM   8426  C  CB    . GLN   A  1  1145 ? 19.702  67.812  91.526  1.00 31.27 ? 1143 GLN   A CB    1 
ATOM   8427  N  N     . THR   A  1  1146 ? 17.436  66.850  93.604  1.00 23.69 ? 1144 THR   A N     1 
ATOM   8428  C  CA    . THR   A  1  1146 ? 16.008  66.670  93.866  1.00 24.59 ? 1144 THR   A CA    1 
ATOM   8429  C  C     . THR   A  1  1146 ? 15.548  67.521  95.039  1.00 22.03 ? 1144 THR   A C     1 
ATOM   8430  O  O     . THR   A  1  1146 ? 14.420  68.033  95.041  1.00 22.78 ? 1144 THR   A O     1 
ATOM   8431  C  CB    . THR   A  1  1146 ? 15.710  65.210  94.183  1.00 25.27 ? 1144 THR   A CB    1 
ATOM   8432  O  OG1   . THR   A  1  1146 ? 16.617  64.763  95.198  1.00 24.01 ? 1144 THR   A OG1   1 
ATOM   8433  C  CG2   . THR   A  1  1146 ? 15.830  64.344  92.940  1.00 24.01 ? 1144 THR   A CG2   1 
ATOM   8434  N  N     . VAL   A  1  1147 ? 16.391  67.648  96.065  1.00 21.54 ? 1145 VAL   A N     1 
ATOM   8435  C  CA    . VAL   A  1  1147 ? 16.028  68.480  97.205  1.00 20.90 ? 1145 VAL   A CA    1 
ATOM   8436  C  C     . VAL   A  1  1147 ? 16.205  69.951  96.864  1.00 21.19 ? 1145 VAL   A C     1 
ATOM   8437  O  O     . VAL   A  1  1147 ? 15.361  70.785  97.206  1.00 19.83 ? 1145 VAL   A O     1 
ATOM   8438  C  CB    . VAL   A  1  1147 ? 16.827  68.079  98.459  1.00 19.91 ? 1145 VAL   A CB    1 
ATOM   8439  C  CG1   . VAL   A  1  1147 ? 16.333  68.871  99.662  1.00 19.78 ? 1145 VAL   A CG1   1 
ATOM   8440  C  CG2   . VAL   A  1  1147 ? 16.720  66.583  98.734  1.00 21.88 ? 1145 VAL   A CG2   1 
ATOM   8441  N  N     . GLY   A  1  1148 ? 17.297  70.290  96.170  1.00 19.68 ? 1146 GLY   A N     1 
ATOM   8442  C  CA    . GLY   A  1  1148 ? 17.504  71.672  95.776  1.00 19.63 ? 1146 GLY   A CA    1 
ATOM   8443  C  C     . GLY   A  1  1148 ? 16.345  72.241  94.980  1.00 22.58 ? 1146 GLY   A C     1 
ATOM   8444  O  O     . GLY   A  1  1148 ? 16.004  73.417  95.127  1.00 22.77 ? 1146 GLY   A O     1 
ATOM   8445  N  N     . LEU   A  1  1149 ? 15.721  71.417  94.127  1.00 20.54 ? 1147 LEU   A N     1 
ATOM   8446  C  CA    . LEU   A  1  1149 ? 14.582  71.883  93.344  1.00 23.70 ? 1147 LEU   A CA    1 
ATOM   8447  C  C     . LEU   A  1  1149 ? 13.435  72.332  94.233  1.00 21.74 ? 1147 LEU   A C     1 
ATOM   8448  O  O     . LEU   A  1  1149 ? 12.625  73.174  93.828  1.00 24.71 ? 1147 LEU   A O     1 
ATOM   8449  C  CB    . LEU   A  1  1149 ? 14.093  70.777  92.410  1.00 24.78 ? 1147 LEU   A CB    1 
ATOM   8450  C  CG    . LEU   A  1  1149 ? 14.968  70.486  91.193  1.00 34.04 ? 1147 LEU   A CG    1 
ATOM   8451  C  CD1   . LEU   A  1  1149 ? 14.414  69.296  90.430  1.00 34.94 ? 1147 LEU   A CD1   1 
ATOM   8452  C  CD2   . LEU   A  1  1149 ? 15.034  71.721  90.306  1.00 33.73 ? 1147 LEU   A CD2   1 
ATOM   8453  N  N     . ARG   A  1  1150 ? 13.353  71.784  95.442  1.00 21.10 ? 1148 ARG   A N     1 
ATOM   8454  C  CA    . ARG   A  1  1150 ? 12.292  72.129  96.372  1.00 20.26 ? 1148 ARG   A CA    1 
ATOM   8455  C  C     . ARG   A  1  1150 ? 12.673  73.242  97.330  1.00 19.14 ? 1148 ARG   A C     1 
ATOM   8456  O  O     . ARG   A  1  1150 ? 11.813  73.704  98.081  1.00 20.23 ? 1148 ARG   A O     1 
ATOM   8457  C  CB    . ARG   A  1  1150 ? 11.923  70.907  97.197  1.00 18.06 ? 1148 ARG   A CB    1 
ATOM   8458  C  CG    . ARG   A  1  1150 ? 11.225  69.838  96.396  1.00 21.89 ? 1148 ARG   A CG    1 
ATOM   8459  C  CD    . ARG   A  1  1150 ? 10.003  69.403  97.141  1.00 20.55 ? 1148 ARG   A CD    1 
ATOM   8460  N  NE    . ARG   A  1  1150 ? 9.434   68.183  96.598  1.00 19.76 ? 1148 ARG   A NE    1 
ATOM   8461  C  CZ    . ARG   A  1  1150 ? 8.878   67.253  97.355  1.00 19.32 ? 1148 ARG   A CZ    1 
ATOM   8462  N  NH1   . ARG   A  1  1150 ? 8.783   67.405  98.668  1.00 16.98 ? 1148 ARG   A NH1   1 
ATOM   8463  N  NH2   . ARG   A  1  1150 ? 8.416   66.142  96.789  1.00 18.25 ? 1148 ARG   A NH2   1 
ATOM   8464  N  N     . VAL   A  1  1151 ? 13.923  73.684  97.324  1.00 19.26 ? 1149 VAL   A N     1 
ATOM   8465  C  CA    . VAL   A  1  1151 ? 14.426  74.620  98.323  1.00 19.81 ? 1149 VAL   A CA    1 
ATOM   8466  C  C     . VAL   A  1  1151 ? 14.721  75.948  97.643  1.00 24.83 ? 1149 VAL   A C     1 
ATOM   8467  O  O     . VAL   A  1  1151 ? 15.435  75.997  96.635  1.00 26.12 ? 1149 VAL   A O     1 
ATOM   8468  C  CB    . VAL   A  1  1151 ? 15.680  74.074  99.027  1.00 21.49 ? 1149 VAL   A CB    1 
ATOM   8469  C  CG1   . VAL   A  1  1151 ? 16.292  75.135  99.939  1.00 22.12 ? 1149 VAL   A CG1   1 
ATOM   8470  C  CG2   . VAL   A  1  1151 ? 15.346  72.831  99.825  1.00 20.24 ? 1149 VAL   A CG2   1 
ATOM   8471  N  N     . SER   A  1  1152 ? 14.169  77.020  98.190  1.00 20.73 ? 1150 SER   A N     1 
ATOM   8472  C  CA    . SER   A  1  1152 ? 14.570  78.367  97.836  1.00 24.20 ? 1150 SER   A CA    1 
ATOM   8473  C  C     . SER   A  1  1152 ? 14.866  79.111  99.126  1.00 23.47 ? 1150 SER   A C     1 
ATOM   8474  O  O     . SER   A  1  1152 ? 14.406  78.731  100.206 1.00 22.92 ? 1150 SER   A O     1 
ATOM   8475  C  CB    . SER   A  1  1152 ? 13.492  79.105  97.036  1.00 25.64 ? 1150 SER   A CB    1 
ATOM   8476  O  OG    . SER   A  1  1152 ? 12.294  79.224  97.777  1.00 29.88 ? 1150 SER   A OG    1 
ATOM   8477  N  N     . TRP   A  1  1153 ? 15.665  80.158  99.008  1.00 22.31 ? 1151 TRP   A N     1 
ATOM   8478  C  CA    . TRP   A  1  1153 ? 15.962  81.039  100.123 1.00 23.56 ? 1151 TRP   A CA    1 
ATOM   8479  C  C     . TRP   A  1  1153 ? 15.297  82.382  99.873  1.00 25.85 ? 1151 TRP   A C     1 
ATOM   8480  O  O     . TRP   A  1  1153 ? 15.301  82.888  98.745  1.00 29.23 ? 1151 TRP   A O     1 
ATOM   8481  C  CB    . TRP   A  1  1153 ? 17.466  81.217  100.268 1.00 24.98 ? 1151 TRP   A CB    1 
ATOM   8482  C  CG    . TRP   A  1  1153 ? 18.127  79.996  100.777 1.00 24.29 ? 1151 TRP   A CG    1 
ATOM   8483  C  CD1   . TRP   A  1  1153 ? 18.567  78.933  100.044 1.00 26.38 ? 1151 TRP   A CD1   1 
ATOM   8484  C  CD2   . TRP   A  1  1153 ? 18.400  79.684  102.145 1.00 23.16 ? 1151 TRP   A CD2   1 
ATOM   8485  N  NE1   . TRP   A  1  1153 ? 19.110  77.985  100.873 1.00 26.23 ? 1151 TRP   A NE1   1 
ATOM   8486  C  CE2   . TRP   A  1  1153 ? 19.023  78.422  102.170 1.00 24.90 ? 1151 TRP   A CE2   1 
ATOM   8487  C  CE3   . TRP   A  1  1153 ? 18.186  80.353  103.350 1.00 21.65 ? 1151 TRP   A CE3   1 
ATOM   8488  C  CZ2   . TRP   A  1  1153 ? 19.432  77.814  103.355 1.00 22.36 ? 1151 TRP   A CZ2   1 
ATOM   8489  C  CZ3   . TRP   A  1  1153 ? 18.602  79.754  104.527 1.00 24.28 ? 1151 TRP   A CZ3   1 
ATOM   8490  C  CH2   . TRP   A  1  1153 ? 19.213  78.494  104.522 1.00 25.46 ? 1151 TRP   A CH2   1 
ATOM   8491  N  N     . SER   A  1  1154 ? 14.707  82.953  100.919 1.00 24.36 ? 1152 SER   A N     1 
ATOM   8492  C  CA    . SER   A  1  1154 ? 13.887  84.146  100.770 1.00 24.68 ? 1152 SER   A CA    1 
ATOM   8493  C  C     . SER   A  1  1154 ? 14.401  85.235  101.695 1.00 27.92 ? 1152 SER   A C     1 
ATOM   8494  O  O     . SER   A  1  1154 ? 14.389  85.074  102.921 1.00 25.32 ? 1152 SER   A O     1 
ATOM   8495  C  CB    . SER   A  1  1154 ? 12.416  83.858  101.068 1.00 23.73 ? 1152 SER   A CB    1 
ATOM   8496  O  OG    . SER   A  1  1154 ? 11.658  85.047  100.942 1.00 25.78 ? 1152 SER   A OG    1 
ATOM   8497  N  N     . LYS   A  1  1155 ? 14.843  86.343  101.105 1.00 28.47 ? 1153 LYS   A N     1 
ATOM   8498  C  CA    . LYS   A  1  1155 ? 15.164  87.531  101.883 1.00 29.32 ? 1153 LYS   A CA    1 
ATOM   8499  C  C     . LYS   A  1  1155 ? 13.961  88.445  102.050 1.00 30.91 ? 1153 LYS   A C     1 
ATOM   8500  O  O     . LYS   A  1  1155 ? 13.871  89.171  103.046 1.00 41.92 ? 1153 LYS   A O     1 
ATOM   8501  C  CB    . LYS   A  1  1155 ? 16.322  88.294  101.229 1.00 30.01 ? 1153 LYS   A CB    1 
ATOM   8502  N  N     . ASP   A  1  1156 ? 13.026  88.412  101.105 1.00 28.63 ? 1154 ASP   A N     1 
ATOM   8503  C  CA    . ASP   A  1  1156 ? 11.835  89.250  101.114 1.00 29.62 ? 1154 ASP   A CA    1 
ATOM   8504  C  C     . ASP   A  1  1156 ? 10.662  88.285  101.008 1.00 29.50 ? 1154 ASP   A C     1 
ATOM   8505  O  O     . ASP   A  1  1156 ? 10.242  87.927  99.907  1.00 27.12 ? 1154 ASP   A O     1 
ATOM   8506  C  CB    . ASP   A  1  1156 ? 11.873  90.217  99.934  1.00 34.02 ? 1154 ASP   A CB    1 
ATOM   8507  C  CG    . ASP   A  1  1156 ? 10.677  91.152  99.899  1.00 41.75 ? 1154 ASP   A CG    1 
ATOM   8508  O  OD1   . ASP   A  1  1156 ? 9.817   91.068  100.804 1.00 40.74 ? 1154 ASP   A OD1   1 
ATOM   8509  O  OD2   . ASP   A  1  1156 ? 10.596  91.977  98.962  1.00 41.65 ? 1154 ASP   A OD2   1 
ATOM   8510  N  N     . TRP   A  1  1157 ? 10.135  87.864  102.160 1.00 28.55 ? 1155 TRP   A N     1 
ATOM   8511  C  CA    . TRP   A  1  1157 ? 9.089   86.845  102.157 1.00 24.50 ? 1155 TRP   A CA    1 
ATOM   8512  C  C     . TRP   A  1  1157 ? 7.900   87.267  101.309 1.00 27.06 ? 1155 TRP   A C     1 
ATOM   8513  O  O     . TRP   A  1  1157 ? 7.316   86.442  100.602 1.00 26.21 ? 1155 TRP   A O     1 
ATOM   8514  C  CB    . TRP   A  1  1157 ? 8.622   86.561  103.580 1.00 26.00 ? 1155 TRP   A CB    1 
ATOM   8515  C  CG    . TRP   A  1  1157 ? 9.687   86.133  104.529 1.00 23.89 ? 1155 TRP   A CG    1 
ATOM   8516  C  CD1   . TRP   A  1  1157 ? 10.965  85.751  104.239 1.00 21.94 ? 1155 TRP   A CD1   1 
ATOM   8517  C  CD2   . TRP   A  1  1157 ? 9.557   86.057  105.948 1.00 20.99 ? 1155 TRP   A CD2   1 
ATOM   8518  N  NE1   . TRP   A  1  1157 ? 11.635  85.430  105.396 1.00 23.98 ? 1155 TRP   A NE1   1 
ATOM   8519  C  CE2   . TRP   A  1  1157 ? 10.789  85.618  106.459 1.00 23.26 ? 1155 TRP   A CE2   1 
ATOM   8520  C  CE3   . TRP   A  1  1157 ? 8.508   86.322  106.837 1.00 22.64 ? 1155 TRP   A CE3   1 
ATOM   8521  C  CZ2   . TRP   A  1  1157 ? 11.006  85.433  107.823 1.00 24.48 ? 1155 TRP   A CZ2   1 
ATOM   8522  C  CZ3   . TRP   A  1  1157 ? 8.726   86.142  108.187 1.00 22.80 ? 1155 TRP   A CZ3   1 
ATOM   8523  C  CH2   . TRP   A  1  1157 ? 9.960   85.704  108.668 1.00 25.86 ? 1155 TRP   A CH2   1 
ATOM   8524  N  N     . ALA   A  1  1158 ? 7.517   88.546  101.368 1.00 26.77 ? 1156 ALA   A N     1 
ATOM   8525  C  CA    . ALA   A  1  1158 ? 6.350   88.994  100.615 1.00 29.22 ? 1156 ALA   A CA    1 
ATOM   8526  C  C     . ALA   A  1  1158 ? 6.554   88.883  99.112  1.00 33.21 ? 1156 ALA   A C     1 
ATOM   8527  O  O     . ALA   A  1  1158 ? 5.573   88.775  98.368  1.00 39.14 ? 1156 ALA   A O     1 
ATOM   8528  C  CB    . ALA   A  1  1158 ? 5.987   90.432  100.991 1.00 31.63 ? 1156 ALA   A CB    1 
ATOM   8529  N  N     . ALA   A  1  1159 ? 7.802   88.913  98.649  1.00 29.00 ? 1157 ALA   A N     1 
ATOM   8530  C  CA    . ALA   A  1  1159 ? 8.084   88.801  97.225  1.00 33.09 ? 1157 ALA   A CA    1 
ATOM   8531  C  C     . ALA   A  1  1159 ? 8.032   87.365  96.726  1.00 33.64 ? 1157 ALA   A C     1 
ATOM   8532  O  O     . ALA   A  1  1159 ? 7.811   87.146  95.531  1.00 33.82 ? 1157 ALA   A O     1 
ATOM   8533  C  CB    . ALA   A  1  1159 ? 9.464   89.392  96.921  1.00 32.24 ? 1157 ALA   A CB    1 
ATOM   8534  N  N     . ASP   A  1  1160 ? 8.217   86.387  97.609  1.00 31.89 ? 1158 ASP   A N     1 
ATOM   8535  C  CA    . ASP   A  1  1160 ? 8.406   84.998  97.213  1.00 31.17 ? 1158 ASP   A CA    1 
ATOM   8536  C  C     . ASP   A  1  1160 ? 7.195   84.119  97.495  1.00 26.60 ? 1158 ASP   A C     1 
ATOM   8537  O  O     . ASP   A  1  1160 ? 7.274   82.898  97.325  1.00 27.83 ? 1158 ASP   A O     1 
ATOM   8538  C  CB    . ASP   A  1  1160 ? 9.664   84.438  97.876  1.00 29.92 ? 1158 ASP   A CB    1 
ATOM   8539  C  CG    . ASP   A  1  1160 ? 10.900  85.233  97.515  1.00 35.14 ? 1158 ASP   A CG    1 
ATOM   8540  O  OD1   . ASP   A  1  1160 ? 10.907  85.836  96.419  1.00 40.64 ? 1158 ASP   A OD1   1 
ATOM   8541  O  OD2   . ASP   A  1  1160 ? 11.854  85.267  98.319  1.00 31.21 ? 1158 ASP   A OD2   1 
ATOM   8542  N  N     . GLY   A  1  1161 ? 6.080   84.706  97.916  1.00 24.69 ? 1159 GLY   A N     1 
ATOM   8543  C  CA    . GLY   A  1  1161 ? 4.858   83.969  98.117  1.00 27.40 ? 1159 GLY   A CA    1 
ATOM   8544  C  C     . GLY   A  1  1161 ? 4.094   83.770  96.822  1.00 27.85 ? 1159 GLY   A C     1 
ATOM   8545  O  O     . GLY   A  1  1161 ? 4.603   84.037  95.730  1.00 33.55 ? 1159 GLY   A O     1 
ATOM   8546  N  N     . PRO   A  1  1162 ? 2.848   83.292  96.917  1.00 26.60 ? 1160 PRO   A N     1 
ATOM   8547  C  CA    . PRO   A  1  1162 ? 2.122   82.941  98.141  1.00 25.34 ? 1160 PRO   A CA    1 
ATOM   8548  C  C     . PRO   A  1  1162 ? 2.668   81.669  98.749  1.00 27.27 ? 1160 PRO   A C     1 
ATOM   8549  O  O     . PRO   A  1  1162 ? 3.087   80.745  98.061  1.00 25.37 ? 1160 PRO   A O     1 
ATOM   8550  C  CB    . PRO   A  1  1162 ? 0.682   82.745  97.646  1.00 26.04 ? 1160 PRO   A CB    1 
ATOM   8551  C  CG    . PRO   A  1  1162 ? 0.848   82.270  96.230  1.00 29.91 ? 1160 PRO   A CG    1 
ATOM   8552  C  CD    . PRO   A  1  1162 ? 2.036   83.044  95.711  1.00 27.95 ? 1160 PRO   A CD    1 
ATOM   8553  N  N     . PHE   A  1  1163 ? 2.706   81.611  100.068 1.00 21.62 ? 1161 PHE   A N     1 
ATOM   8554  C  CA    . PHE   A  1  1163 ? 3.032   80.374  100.747 1.00 18.47 ? 1161 PHE   A CA    1 
ATOM   8555  C  C     . PHE   A  1  1163 ? 1.744   79.666  101.127 1.00 17.66 ? 1161 PHE   A C     1 
ATOM   8556  O  O     . PHE   A  1  1163 ? 0.645   80.215  101.011 1.00 21.55 ? 1161 PHE   A O     1 
ATOM   8557  C  CB    . PHE   A  1  1163 ? 3.901   80.675  101.963 1.00 17.45 ? 1161 PHE   A CB    1 
ATOM   8558  C  CG    . PHE   A  1  1163 ? 5.141   81.431  101.612 1.00 19.66 ? 1161 PHE   A CG    1 
ATOM   8559  C  CD1   . PHE   A  1  1163 ? 6.085   80.860  100.772 1.00 20.25 ? 1161 PHE   A CD1   1 
ATOM   8560  C  CD2   . PHE   A  1  1163 ? 5.356   82.718  102.082 1.00 19.34 ? 1161 PHE   A CD2   1 
ATOM   8561  C  CE1   . PHE   A  1  1163 ? 7.232   81.551  100.421 1.00 22.32 ? 1161 PHE   A CE1   1 
ATOM   8562  C  CE2   . PHE   A  1  1163 ? 6.500   83.415  101.730 1.00 22.98 ? 1161 PHE   A CE2   1 
ATOM   8563  C  CZ    . PHE   A  1  1163 ? 7.439   82.830  100.905 1.00 21.61 ? 1161 PHE   A CZ    1 
ATOM   8564  N  N     . ALA   A  1  1164 ? 1.880   78.403  101.528 1.00 18.08 ? 1162 ALA   A N     1 
ATOM   8565  C  CA    . ALA   A  1  1164 ? 0.725   77.609  101.914 1.00 17.47 ? 1162 ALA   A CA    1 
ATOM   8566  C  C     . ALA   A  1  1164 ? 0.795   77.188  103.369 1.00 17.39 ? 1162 ALA   A C     1 
ATOM   8567  O  O     . ALA   A  1  1164 ? -0.014  76.366  103.813 1.00 19.45 ? 1162 ALA   A O     1 
ATOM   8568  C  CB    . ALA   A  1  1164 ? 0.576   76.392  100.994 1.00 20.30 ? 1162 ALA   A CB    1 
ATOM   8569  N  N     . GLY   A  1  1165 ? 1.753   77.718  104.106 1.00 16.95 ? 1163 GLY   A N     1 
ATOM   8570  C  CA    . GLY   A  1  1165 ? 1.899   77.451  105.519 1.00 16.89 ? 1163 GLY   A CA    1 
ATOM   8571  C  C     . GLY   A  1  1165 ? 3.272   77.929  105.930 1.00 16.12 ? 1163 GLY   A C     1 
ATOM   8572  O  O     . GLY   A  1  1165 ? 4.065   78.390  105.108 1.00 16.95 ? 1163 GLY   A O     1 
ATOM   8573  N  N     . ALA   A  1  1166 ? 3.545   77.807  107.220 1.00 16.32 ? 1164 ALA   A N     1 
ATOM   8574  C  CA    . ALA   A  1  1166 ? 4.830   78.262  107.717 1.00 15.96 ? 1164 ALA   A CA    1 
ATOM   8575  C  C     . ALA   A  1  1166 ? 5.221   77.422  108.916 1.00 16.07 ? 1164 ALA   A C     1 
ATOM   8576  O  O     . ALA   A  1  1166 ? 4.363   76.967  109.679 1.00 19.26 ? 1164 ALA   A O     1 
ATOM   8577  C  CB    . ALA   A  1  1166 ? 4.795   79.743  108.111 1.00 18.41 ? 1164 ALA   A CB    1 
ATOM   8578  N  N     . LEU   A  1  1167 ? 6.524   77.208  109.056 1.00 15.55 ? 1165 LEU   A N     1 
ATOM   8579  C  CA    . LEU   A  1  1167 ? 7.098   76.579  110.232 1.00 15.71 ? 1165 LEU   A CA    1 
ATOM   8580  C  C     . LEU   A  1  1167 ? 8.094   77.553  110.822 1.00 18.14 ? 1165 LEU   A C     1 
ATOM   8581  O  O     . LEU   A  1  1167 ? 8.960   78.069  110.107 1.00 18.59 ? 1165 LEU   A O     1 
ATOM   8582  C  CB    . LEU   A  1  1167 ? 7.805   75.281  109.868 1.00 16.82 ? 1165 LEU   A CB    1 
ATOM   8583  C  CG    . LEU   A  1  1167 ? 6.903   74.233  109.219 1.00 16.38 ? 1165 LEU   A CG    1 
ATOM   8584  C  CD1   . LEU   A  1  1167 ? 7.732   73.037  108.786 1.00 18.78 ? 1165 LEU   A CD1   1 
ATOM   8585  C  CD2   . LEU   A  1  1167 ? 5.814   73.809  110.179 1.00 19.71 ? 1165 LEU   A CD2   1 
ATOM   8586  N  N     . VAL   A  1  1168 ? 7.970   77.795  112.119 1.00 17.65 ? 1166 VAL   A N     1 
ATOM   8587  C  CA    . VAL   A  1  1168 ? 8.771   78.794  112.807 1.00 17.80 ? 1166 VAL   A CA    1 
ATOM   8588  C  C     . VAL   A  1  1168 ? 9.459   78.141  113.988 1.00 18.56 ? 1166 VAL   A C     1 
ATOM   8589  O  O     . VAL   A  1  1168 ? 8.845   77.360  114.725 1.00 18.33 ? 1166 VAL   A O     1 
ATOM   8590  C  CB    . VAL   A  1  1168 ? 7.890   79.972  113.274 1.00 17.95 ? 1166 VAL   A CB    1 
ATOM   8591  C  CG1   . VAL   A  1  1168 ? 8.746   81.034  113.962 1.00 19.33 ? 1166 VAL   A CG1   1 
ATOM   8592  C  CG2   . VAL   A  1  1168 ? 7.125   80.562  112.089 1.00 20.28 ? 1166 VAL   A CG2   1 
ATOM   8593  N  N     . GLU   A  1  1169 ? 10.733  78.467  114.174 1.00 16.73 ? 1167 GLU   A N     1 
ATOM   8594  C  CA    . GLU   A  1  1169 ? 11.497  78.042  115.339 1.00 17.57 ? 1167 GLU   A CA    1 
ATOM   8595  C  C     . GLU   A  1  1169 ? 11.953  79.281  116.089 1.00 21.64 ? 1167 GLU   A C     1 
ATOM   8596  O  O     . GLU   A  1  1169 ? 12.487  80.214  115.482 1.00 20.51 ? 1167 GLU   A O     1 
ATOM   8597  C  CB    . GLU   A  1  1169 ? 12.733  77.256  114.913 1.00 18.10 ? 1167 GLU   A CB    1 
ATOM   8598  C  CG    . GLU   A  1  1169 ? 13.606  76.813  116.069 1.00 17.29 ? 1167 GLU   A CG    1 
ATOM   8599  C  CD    . GLU   A  1  1169 ? 14.940  76.270  115.596 1.00 19.11 ? 1167 GLU   A CD    1 
ATOM   8600  O  OE1   . GLU   A  1  1169 ? 15.225  76.382  114.381 1.00 19.47 ? 1167 GLU   A OE1   1 
ATOM   8601  O  OE2   . GLU   A  1  1169 ? 15.687  75.724  116.433 1.00 20.69 ? 1167 GLU   A OE2   1 
ATOM   8602  N  N     . GLY   A  1  1170 ? 11.766  79.288  117.396 1.00 18.86 ? 1168 GLY   A N     1 
ATOM   8603  C  CA    . GLY   A  1  1170 ? 12.320  80.366  118.187 1.00 22.16 ? 1168 GLY   A CA    1 
ATOM   8604  C  C     . GLY   A  1  1170 ? 11.706  80.396  119.565 1.00 22.34 ? 1168 GLY   A C     1 
ATOM   8605  O  O     . GLY   A  1  1170 ? 10.775  79.654  119.872 1.00 22.16 ? 1168 GLY   A O     1 
ATOM   8606  N  N     . ASP   A  1  1171 ? 12.238  81.297  120.386 1.00 21.72 ? 1169 ASP   A N     1 
ATOM   8607  C  CA    . ASP   A  1  1171 ? 11.608  81.550  121.672 1.00 23.01 ? 1169 ASP   A CA    1 
ATOM   8608  C  C     . ASP   A  1  1171 ? 10.305  82.321  121.470 1.00 23.10 ? 1169 ASP   A C     1 
ATOM   8609  O  O     . ASP   A  1  1171 ? 9.933   82.688  120.351 1.00 21.82 ? 1169 ASP   A O     1 
ATOM   8610  C  CB    . ASP   A  1  1171 ? 12.589  82.187  122.663 1.00 24.49 ? 1169 ASP   A CB    1 
ATOM   8611  C  CG    . ASP   A  1  1171 ? 13.057  83.582  122.254 1.00 28.93 ? 1169 ASP   A CG    1 
ATOM   8612  O  OD1   . ASP   A  1  1171 ? 12.441  84.221  121.378 1.00 26.38 ? 1169 ASP   A OD1   1 
ATOM   8613  O  OD2   . ASP   A  1  1171 ? 14.061  84.052  122.840 1.00 33.06 ? 1169 ASP   A OD2   1 
ATOM   8614  N  N     . ALA   A  1  1172 ? 9.585   82.550  122.569 1.00 23.32 ? 1170 ALA   A N     1 
ATOM   8615  C  CA    . ALA   A  1  1172 ? 8.242   83.109  122.471 1.00 24.74 ? 1170 ALA   A CA    1 
ATOM   8616  C  C     . ALA   A  1  1172 ? 8.239   84.458  121.760 1.00 25.26 ? 1170 ALA   A C     1 
ATOM   8617  O  O     . ALA   A  1  1172 ? 7.376   84.722  120.918 1.00 24.29 ? 1170 ALA   A O     1 
ATOM   8618  C  CB    . ALA   A  1  1172 ? 7.620   83.229  123.862 1.00 25.51 ? 1170 ALA   A CB    1 
ATOM   8619  N  N     . GLU   A  1  1173 ? 9.199   85.327  122.074 1.00 26.25 ? 1171 GLU   A N     1 
ATOM   8620  C  CA    . GLU   A  1  1173 ? 9.180   86.641  121.440 1.00 26.96 ? 1171 GLU   A CA    1 
ATOM   8621  C  C     . GLU   A  1  1173 ? 9.619   86.580  119.983 1.00 25.43 ? 1171 GLU   A C     1 
ATOM   8622  O  O     . GLU   A  1  1173 ? 9.122   87.355  119.159 1.00 27.20 ? 1171 GLU   A O     1 
ATOM   8623  C  CB    . GLU   A  1  1173 ? 9.982   87.655  122.250 1.00 30.64 ? 1171 GLU   A CB    1 
ATOM   8624  C  CG    . GLU   A  1  1173 ? 9.325   87.978  123.583 1.00 34.11 ? 1171 GLU   A CG    1 
ATOM   8625  C  CD    . GLU   A  1  1173 ? 7.859   88.391  123.446 1.00 35.14 ? 1171 GLU   A CD    1 
ATOM   8626  O  OE1   . GLU   A  1  1173 ? 7.510   89.098  122.471 1.00 36.61 ? 1171 GLU   A OE1   1 
ATOM   8627  O  OE2   . GLU   A  1  1173 ? 7.048   88.007  124.316 1.00 37.00 ? 1171 GLU   A OE2   1 
ATOM   8628  N  N     . ARG   A  1  1174 ? 10.524  85.661  119.641 1.00 22.60 ? 1172 ARG   A N     1 
ATOM   8629  C  CA    . ARG   A  1  1174 ? 10.836  85.443  118.232 1.00 24.51 ? 1172 ARG   A CA    1 
ATOM   8630  C  C     . ARG   A  1  1174 ? 9.608   84.953  117.482 1.00 24.50 ? 1172 ARG   A C     1 
ATOM   8631  O  O     . ARG   A  1  1174 ? 9.305   85.439  116.386 1.00 22.03 ? 1172 ARG   A O     1 
ATOM   8632  C  CB    . ARG   A  1  1174 ? 11.972  84.432  118.102 1.00 24.01 ? 1172 ARG   A CB    1 
ATOM   8633  C  CG    . ARG   A  1  1174 ? 12.304  84.041  116.668 1.00 23.86 ? 1172 ARG   A CG    1 
ATOM   8634  C  CD    . ARG   A  1  1174 ? 12.742  85.244  115.851 1.00 27.84 ? 1172 ARG   A CD    1 
ATOM   8635  N  NE    . ARG   A  1  1174 ? 13.073  84.867  114.482 1.00 23.62 ? 1172 ARG   A NE    1 
ATOM   8636  C  CZ    . ARG   A  1  1174 ? 13.118  85.713  113.461 1.00 26.40 ? 1172 ARG   A CZ    1 
ATOM   8637  N  NH1   . ARG   A  1  1174 ? 12.870  87.004  113.619 1.00 26.23 ? 1172 ARG   A NH1   1 
ATOM   8638  N  NH2   . ARG   A  1  1174 ? 13.414  85.252  112.250 1.00 24.83 ? 1172 ARG   A NH2   1 
ATOM   8639  N  N     . ILE   A  1  1175 ? 8.873   84.008  118.070 1.00 21.73 ? 1173 ILE   A N     1 
ATOM   8640  C  CA    . ILE   A  1  1175 ? 7.659   83.502  117.437 1.00 20.51 ? 1173 ILE   A CA    1 
ATOM   8641  C  C     . ILE   A  1  1175 ? 6.650   84.622  117.241 1.00 21.28 ? 1173 ILE   A C     1 
ATOM   8642  O  O     . ILE   A  1  1175 ? 6.036   84.747  116.173 1.00 21.92 ? 1173 ILE   A O     1 
ATOM   8643  C  CB    . ILE   A  1  1175 ? 7.072   82.347  118.268 1.00 22.05 ? 1173 ILE   A CB    1 
ATOM   8644  C  CG1   . ILE   A  1  1175 ? 8.011   81.141  118.214 1.00 22.37 ? 1173 ILE   A CG1   1 
ATOM   8645  C  CG2   . ILE   A  1  1175 ? 5.669   82.009  117.793 1.00 21.83 ? 1173 ILE   A CG2   1 
ATOM   8646  C  CD1   . ILE   A  1  1175 ? 7.656   80.037  119.184 1.00 23.59 ? 1173 ILE   A CD1   1 
ATOM   8647  N  N     . ARG   A  1  1176 ? 6.464   85.459  118.263 1.00 24.55 ? 1174 ARG   A N     1 
ATOM   8648  C  CA    . ARG   A  1  1176 ? 5.513   86.555  118.145 1.00 23.54 ? 1174 ARG   A CA    1 
ATOM   8649  C  C     . ARG   A  1  1176 ? 5.909   87.492  117.013 1.00 20.30 ? 1174 ARG   A C     1 
ATOM   8650  O  O     . ARG   A  1  1176 ? 5.076   87.862  116.174 1.00 23.14 ? 1174 ARG   A O     1 
ATOM   8651  C  CB    . ARG   A  1  1176 ? 5.407   87.311  119.471 1.00 22.14 ? 1174 ARG   A CB    1 
ATOM   8652  C  CG    . ARG   A  1  1176 ? 4.170   88.186  119.541 1.00 27.59 ? 1174 ARG   A CG    1 
ATOM   8653  C  CD    . ARG   A  1  1176 ? 4.258   89.192  120.678 1.00 30.31 ? 1174 ARG   A CD    1 
ATOM   8654  N  NE    . ARG   A  1  1176 ? 4.577   88.567  121.956 1.00 28.29 ? 1174 ARG   A NE    1 
ATOM   8655  C  CZ    . ARG   A  1  1176 ? 3.677   88.109  122.817 1.00 32.23 ? 1174 ARG   A CZ    1 
ATOM   8656  N  NH1   . ARG   A  1  1176 ? 2.383   88.130  122.542 1.00 32.82 ? 1174 ARG   A NH1   1 
ATOM   8657  N  NH2   . ARG   A  1  1176 ? 4.087   87.635  123.992 1.00 33.05 ? 1174 ARG   A NH2   1 
ATOM   8658  N  N     . ALA   A  1  1177 ? 7.190   87.847  116.948 1.00 23.00 ? 1175 ALA   A N     1 
ATOM   8659  C  CA    . ALA   A  1  1177 ? 7.675   88.741  115.900 1.00 25.01 ? 1175 ALA   A CA    1 
ATOM   8660  C  C     . ALA   A  1  1177 ? 7.485   88.127  114.522 1.00 22.05 ? 1175 ALA   A C     1 
ATOM   8661  O  O     . ALA   A  1  1177 ? 7.005   88.788  113.595 1.00 23.42 ? 1175 ALA   A O     1 
ATOM   8662  C  CB    . ALA   A  1  1177 ? 9.148   89.057  116.135 1.00 23.70 ? 1175 ALA   A CB    1 
ATOM   8663  N  N     . VAL   A  1  1178 ? 7.862   86.859  114.369 1.00 21.95 ? 1176 VAL   A N     1 
ATOM   8664  C  CA    . VAL   A  1  1178 ? 7.694   86.184  113.085 1.00 20.27 ? 1176 VAL   A CA    1 
ATOM   8665  C  C     . VAL   A  1  1178 ? 6.223   86.097  112.718 1.00 22.13 ? 1176 VAL   A C     1 
ATOM   8666  O  O     . VAL   A  1  1178 ? 5.846   86.313  111.559 1.00 22.08 ? 1176 VAL   A O     1 
ATOM   8667  C  CB    . VAL   A  1  1178 ? 8.362   84.800  113.110 1.00 19.55 ? 1176 VAL   A CB    1 
ATOM   8668  C  CG1   . VAL   A  1  1178 ? 7.996   84.033  111.855 1.00 20.46 ? 1176 VAL   A CG1   1 
ATOM   8669  C  CG2   . VAL   A  1  1178 ? 9.861   84.942  113.212 1.00 21.78 ? 1176 VAL   A CG2   1 
ATOM   8670  N  N     . ASN   A  1  1179 ? 5.368   85.775  113.693 1.00 22.90 ? 1177 ASN   A N     1 
ATOM   8671  C  CA    . ASN   A  1  1179 ? 3.938   85.668  113.422 1.00 21.92 ? 1177 ASN   A CA    1 
ATOM   8672  C  C     . ASN   A  1  1179 ? 3.388   86.992  112.905 1.00 23.71 ? 1177 ASN   A C     1 
ATOM   8673  O  O     . ASN   A  1  1179 ? 2.553   87.015  111.995 1.00 22.12 ? 1177 ASN   A O     1 
ATOM   8674  C  CB    . ASN   A  1  1179 ? 3.214   85.236  114.700 1.00 25.77 ? 1177 ASN   A CB    1 
ATOM   8675  C  CG    . ASN   A  1  1179 ? 1.998   84.380  114.435 1.00 29.73 ? 1177 ASN   A CG    1 
ATOM   8676  O  OD1   . ASN   A  1  1179 ? 1.814   83.848  113.335 1.00 34.47 ? 1177 ASN   A OD1   1 
ATOM   8677  N  ND2   . ASN   A  1  1179 ? 1.150   84.236  115.454 1.00 33.19 ? 1177 ASN   A ND2   1 
ATOM   8678  N  N     . LYS   A  1  1180 ? 3.866   88.109  113.456 1.00 24.44 ? 1178 LYS   A N     1 
ATOM   8679  C  CA    . LYS   A  1  1180 ? 3.458   89.419  112.961 1.00 25.37 ? 1178 LYS   A CA    1 
ATOM   8680  C  C     . LYS   A  1  1180 ? 3.938   89.646  111.532 1.00 22.74 ? 1178 LYS   A C     1 
ATOM   8681  O  O     . LYS   A  1  1180 ? 3.176   90.125  110.685 1.00 23.97 ? 1178 LYS   A O     1 
ATOM   8682  C  CB    . LYS   A  1  1180 ? 3.984   90.511  113.892 1.00 26.91 ? 1178 LYS   A CB    1 
ATOM   8683  C  CG    . LYS   A  1  1180 ? 3.298   90.517  115.250 1.00 28.79 ? 1178 LYS   A CG    1 
ATOM   8684  C  CD    . LYS   A  1  1180 ? 4.042   91.380  116.275 1.00 28.74 ? 1178 LYS   A CD    1 
ATOM   8685  C  CE    . LYS   A  1  1180 ? 4.160   92.838  115.836 1.00 36.77 ? 1178 LYS   A CE    1 
ATOM   8686  N  NZ    . LYS   A  1  1180 ? 4.881   93.670  116.853 1.00 41.86 ? 1178 LYS   A NZ    1 
ATOM   8687  N  N     . ALA   A  1  1181 ? 5.190   89.294  111.241 1.00 22.77 ? 1179 ALA   A N     1 
ATOM   8688  C  CA    . ALA   A  1  1181 ? 5.700   89.447  109.882 1.00 23.44 ? 1179 ALA   A CA    1 
ATOM   8689  C  C     . ALA   A  1  1181 ? 4.948   88.554  108.904 1.00 23.17 ? 1179 ALA   A C     1 
ATOM   8690  O  O     . ALA   A  1  1181 ? 4.669   88.961  107.771 1.00 22.25 ? 1179 ALA   A O     1 
ATOM   8691  C  CB    . ALA   A  1  1181 ? 7.195   89.147  109.841 1.00 21.67 ? 1179 ALA   A CB    1 
ATOM   8692  N  N     . ILE   A  1  1182 ? 4.601   87.337  109.324 1.00 21.22 ? 1180 ILE   A N     1 
ATOM   8693  C  CA    . ILE   A  1  1182 ? 3.856   86.441  108.444 1.00 21.70 ? 1180 ILE   A CA    1 
ATOM   8694  C  C     . ILE   A  1  1182 ? 2.465   86.985  108.184 1.00 22.35 ? 1180 ILE   A C     1 
ATOM   8695  O  O     . ILE   A  1  1182 ? 1.970   86.946  107.049 1.00 21.89 ? 1180 ILE   A O     1 
ATOM   8696  C  CB    . ILE   A  1  1182 ? 3.808   85.021  109.028 1.00 20.65 ? 1180 ILE   A CB    1 
ATOM   8697  C  CG1   . ILE   A  1  1182 ? 5.194   84.395  108.963 1.00 20.40 ? 1180 ILE   A CG1   1 
ATOM   8698  C  CG2   . ILE   A  1  1182 ? 2.781   84.176  108.283 1.00 21.97 ? 1180 ILE   A CG2   1 
ATOM   8699  C  CD1   . ILE   A  1  1182 ? 5.291   83.023  109.627 1.00 23.53 ? 1180 ILE   A CD1   1 
ATOM   8700  N  N     . ALA   A  1  1183 ? 1.810   87.494  109.225 1.00 20.87 ? 1181 ALA   A N     1 
ATOM   8701  C  CA    . ALA   A  1  1183 ? 0.463   88.014  109.043 1.00 22.00 ? 1181 ALA   A CA    1 
ATOM   8702  C  C     . ALA   A  1  1183 ? 0.455   89.174  108.062 1.00 24.49 ? 1181 ALA   A C     1 
ATOM   8703  O  O     . ALA   A  1  1183 ? -0.546  89.404  107.376 1.00 24.38 ? 1181 ALA   A O     1 
ATOM   8704  C  CB    . ALA   A  1  1183 ? -0.121  88.436  110.390 1.00 23.93 ? 1181 ALA   A CB    1 
ATOM   8705  N  N     . ALA   A  1  1184 ? 1.571   89.893  107.958 1.00 21.92 ? 1182 ALA   A N     1 
ATOM   8706  C  CA    . ALA   A  1  1184 ? 1.653   91.043  107.069 1.00 23.60 ? 1182 ALA   A CA    1 
ATOM   8707  C  C     . ALA   A  1  1184 ? 1.877   90.649  105.622 1.00 24.71 ? 1182 ALA   A C     1 
ATOM   8708  O  O     . ALA   A  1  1184 ? 1.805   91.517  104.747 1.00 23.61 ? 1182 ALA   A O     1 
ATOM   8709  C  CB    . ALA   A  1  1184 ? 2.776   91.985  107.518 1.00 23.94 ? 1182 ALA   A CB    1 
ATOM   8710  N  N     . LEU   A  1  1185 ? 2.154   89.380  105.350 1.00 21.21 ? 1183 LEU   A N     1 
ATOM   8711  C  CA    . LEU   A  1  1185 ? 2.366   88.965  103.975 1.00 21.75 ? 1183 LEU   A CA    1 
ATOM   8712  C  C     . LEU   A  1  1185 ? 1.076   89.117  103.182 1.00 23.26 ? 1183 LEU   A C     1 
ATOM   8713  O  O     . LEU   A  1  1185 ? -0.010  88.835  103.694 1.00 23.69 ? 1183 LEU   A O     1 
ATOM   8714  C  CB    . LEU   A  1  1185 ? 2.826   87.513  103.903 1.00 18.97 ? 1183 LEU   A CB    1 
ATOM   8715  C  CG    . LEU   A  1  1185 ? 4.132   87.228  104.635 1.00 21.49 ? 1183 LEU   A CG    1 
ATOM   8716  C  CD1   . LEU   A  1  1185 ? 4.466   85.746  104.578 1.00 20.73 ? 1183 LEU   A CD1   1 
ATOM   8717  C  CD2   . LEU   A  1  1185 ? 5.269   88.059  104.049 1.00 23.16 ? 1183 LEU   A CD2   1 
ATOM   8718  N  N     . PRO   A  1  1186 ? 1.164   89.552  101.933 1.00 23.87 ? 1184 PRO   A N     1 
ATOM   8719  C  CA    . PRO   A  1  1186 ? -0.039  89.674  101.113 1.00 23.06 ? 1184 PRO   A CA    1 
ATOM   8720  C  C     . PRO   A  1  1186 ? -0.634  88.308  100.829 1.00 20.55 ? 1184 PRO   A C     1 
ATOM   8721  O  O     . PRO   A  1  1186 ? 0.060   87.289  100.792 1.00 23.20 ? 1184 PRO   A O     1 
ATOM   8722  C  CB    . PRO   A  1  1186 ? 0.483   90.308  99.821  1.00 26.85 ? 1184 PRO   A CB    1 
ATOM   8723  C  CG    . PRO   A  1  1186 ? 1.909   89.848  99.741  1.00 31.57 ? 1184 PRO   A CG    1 
ATOM   8724  C  CD    . PRO   A  1  1186 ? 2.398   89.816  101.179 1.00 24.07 ? 1184 PRO   A CD    1 
ATOM   8725  N  N     . GLY   A  1  1187 ? -1.945  88.299  100.646 1.00 20.71 ? 1185 GLY   A N     1 
ATOM   8726  C  CA    . GLY   A  1  1187 ? -2.604  87.133  100.118 1.00 25.83 ? 1185 GLY   A CA    1 
ATOM   8727  C  C     . GLY   A  1  1187 ? -3.168  86.220  101.182 1.00 21.23 ? 1185 GLY   A C     1 
ATOM   8728  O  O     . GLY   A  1  1187 ? -3.869  86.653  102.101 1.00 22.75 ? 1185 GLY   A O     1 
ATOM   8729  N  N     . PRO   A  1  1188 ? -2.883  84.927  101.065 1.00 20.23 ? 1186 PRO   A N     1 
ATOM   8730  C  CA    . PRO   A  1  1188 ? -3.602  83.952  101.881 1.00 18.74 ? 1186 PRO   A CA    1 
ATOM   8731  C  C     . PRO   A  1  1188 ? -3.157  84.003  103.328 1.00 19.06 ? 1186 PRO   A C     1 
ATOM   8732  O  O     . PRO   A  1  1188 ? -2.009  84.315  103.645 1.00 19.55 ? 1186 PRO   A O     1 
ATOM   8733  C  CB    . PRO   A  1  1188 ? -3.238  82.613  101.237 1.00 22.65 ? 1186 PRO   A CB    1 
ATOM   8734  C  CG    . PRO   A  1  1188 ? -1.896  82.851  100.644 1.00 23.21 ? 1186 PRO   A CG    1 
ATOM   8735  C  CD    . PRO   A  1  1188 ? -1.931  84.282  100.150 1.00 21.44 ? 1186 PRO   A CD    1 
ATOM   8736  N  N     . LEU   A  1  1189 ? -4.100  83.709  104.208 1.00 18.89 ? 1187 LEU   A N     1 
ATOM   8737  C  CA    . LEU   A  1  1189 ? -3.744  83.430  105.585 1.00 18.90 ? 1187 LEU   A CA    1 
ATOM   8738  C  C     . LEU   A  1  1189 ? -2.900  82.164  105.615 1.00 18.99 ? 1187 LEU   A C     1 
ATOM   8739  O  O     . LEU   A  1  1189 ? -3.190  81.192  104.914 1.00 22.33 ? 1187 LEU   A O     1 
ATOM   8740  C  CB    . LEU   A  1  1189 ? -5.010  83.238  106.413 1.00 20.33 ? 1187 LEU   A CB    1 
ATOM   8741  C  CG    . LEU   A  1  1189 ? -5.721  84.524  106.860 1.00 20.97 ? 1187 LEU   A CG    1 
ATOM   8742  C  CD1   . LEU   A  1  1189 ? -6.405  85.258  105.705 1.00 22.94 ? 1187 LEU   A CD1   1 
ATOM   8743  C  CD2   . LEU   A  1  1189 ? -6.719  84.217  107.954 1.00 26.86 ? 1187 LEU   A CD2   1 
ATOM   8744  N  N     . LEU   A  1  1190 ? -1.813  82.197  106.374 1.00 18.86 ? 1188 LEU   A N     1 
ATOM   8745  C  CA    . LEU   A  1  1190 ? -0.920  81.054  106.467 1.00 20.06 ? 1188 LEU   A CA    1 
ATOM   8746  C  C     . LEU   A  1  1190 ? -1.181  80.314  107.766 1.00 17.71 ? 1188 LEU   A C     1 
ATOM   8747  O  O     . LEU   A  1  1190 ? -1.272  80.928  108.834 1.00 21.10 ? 1188 LEU   A O     1 
ATOM   8748  C  CB    . LEU   A  1  1190 ? 0.539   81.489  106.404 1.00 20.94 ? 1188 LEU   A CB    1 
ATOM   8749  C  CG    . LEU   A  1  1190 ? 0.940   82.197  105.113 1.00 20.18 ? 1188 LEU   A CG    1 
ATOM   8750  C  CD1   . LEU   A  1  1190 ? 2.449   82.300  105.072 1.00 25.81 ? 1188 LEU   A CD1   1 
ATOM   8751  C  CD2   . LEU   A  1  1190 ? 0.424   81.434  103.896 1.00 21.29 ? 1188 LEU   A CD2   1 
ATOM   8752  N  N     . LEU   A  1  1191 ? -1.310  78.999  107.667 1.00 18.61 ? 1189 LEU   A N     1 
ATOM   8753  C  CA    . LEU   A  1  1191 ? -1.342  78.159  108.856 1.00 18.51 ? 1189 LEU   A CA    1 
ATOM   8754  C  C     . LEU   A  1  1191 ? 0.087   78.038  109.358 1.00 18.26 ? 1189 LEU   A C     1 
ATOM   8755  O  O     . LEU   A  1  1191 ? 0.916   77.348  108.745 1.00 19.22 ? 1189 LEU   A O     1 
ATOM   8756  C  CB    . LEU   A  1  1191 ? -1.932  76.796  108.508 1.00 18.98 ? 1189 LEU   A CB    1 
ATOM   8757  C  CG    . LEU   A  1  1191 ? -2.504  75.985  109.671 1.00 18.27 ? 1189 LEU   A CG    1 
ATOM   8758  C  CD1   . LEU   A  1  1191 ? -3.329  74.839  109.118 1.00 19.01 ? 1189 LEU   A CD1   1 
ATOM   8759  C  CD2   . LEU   A  1  1191 ? -1.366  75.439  110.553 1.00 20.60 ? 1189 LEU   A CD2   1 
ATOM   8760  N  N     . VAL   A  1  1192 ? 0.370   78.709  110.471 1.00 18.53 ? 1190 VAL   A N     1 
ATOM   8761  C  CA    . VAL   A  1  1192 ? 1.706   78.790  111.038 1.00 17.07 ? 1190 VAL   A CA    1 
ATOM   8762  C  C     . VAL   A  1  1192 ? 1.800   77.801  112.186 1.00 18.03 ? 1190 VAL   A C     1 
ATOM   8763  O  O     . VAL   A  1  1192 ? 0.903   77.734  113.035 1.00 20.55 ? 1190 VAL   A O     1 
ATOM   8764  C  CB    . VAL   A  1  1192 ? 1.988   80.215  111.537 1.00 22.04 ? 1190 VAL   A CB    1 
ATOM   8765  C  CG1   . VAL   A  1  1192 ? 3.377   80.300  112.157 1.00 22.54 ? 1190 VAL   A CG1   1 
ATOM   8766  C  CG2   . VAL   A  1  1192 ? 1.837   81.202  110.399 1.00 23.17 ? 1190 VAL   A CG2   1 
ATOM   8767  N  N     . GLN   A  1  1193 ? 2.888   77.046  112.227 1.00 18.12 ? 1191 GLN   A N     1 
ATOM   8768  C  CA    . GLN   A  1  1193 ? 3.212   76.227  113.382 1.00 16.86 ? 1191 GLN   A CA    1 
ATOM   8769  C  C     . GLN   A  1  1193 ? 4.549   76.688  113.916 1.00 17.73 ? 1191 GLN   A C     1 
ATOM   8770  O  O     . GLN   A  1  1193 ? 5.507   76.854  113.148 1.00 18.90 ? 1191 GLN   A O     1 
ATOM   8771  C  CB    . GLN   A  1  1193 ? 3.329   74.763  113.005 1.00 16.04 ? 1191 GLN   A CB    1 
ATOM   8772  C  CG    . GLN   A  1  1193 ? 2.072   74.193  112.417 1.00 20.79 ? 1191 GLN   A CG    1 
ATOM   8773  C  CD    . GLN   A  1  1193 ? 2.132   72.694  112.346 1.00 19.48 ? 1191 GLN   A CD    1 
ATOM   8774  O  OE1   . GLN   A  1  1193 ? 2.040   72.010  113.368 1.00 21.06 ? 1191 GLN   A OE1   1 
ATOM   8775  N  NE2   . GLN   A  1  1193 ? 2.308   72.169  111.140 1.00 19.32 ? 1191 GLN   A NE2   1 
ATOM   8776  N  N     . ALA   A  1  1194 ? 4.621   76.872  115.226 1.00 16.62 ? 1192 ALA   A N     1 
ATOM   8777  C  CA    . ALA   A  1  1194 ? 5.824   77.365  115.859 1.00 17.01 ? 1192 ALA   A CA    1 
ATOM   8778  C  C     . ALA   A  1  1194 ? 6.274   76.391  116.936 1.00 17.79 ? 1192 ALA   A C     1 
ATOM   8779  O  O     . ALA   A  1  1194 ? 5.463   75.689  117.548 1.00 19.66 ? 1192 ALA   A O     1 
ATOM   8780  C  CB    . ALA   A  1  1194 ? 5.555   78.729  116.485 1.00 18.74 ? 1192 ALA   A CB    1 
ATOM   8781  N  N     . ALA   A  1  1195 ? 7.577   76.370  117.169 1.00 17.68 ? 1193 ALA   A N     1 
ATOM   8782  C  CA    . ALA   A  1  1195 ? 8.139   75.556  118.229 1.00 18.47 ? 1193 ALA   A CA    1 
ATOM   8783  C  C     . ALA   A  1  1195 ? 9.440   76.198  118.663 1.00 18.49 ? 1193 ALA   A C     1 
ATOM   8784  O  O     . ALA   A  1  1195 ? 10.102  76.881  117.879 1.00 20.11 ? 1193 ALA   A O     1 
ATOM   8785  C  CB    . ALA   A  1  1195 ? 8.402   74.129  117.732 1.00 19.88 ? 1193 ALA   A CB    1 
ATOM   8786  N  N     . SER   A  1  1196 ? 9.793   75.984  119.921 1.00 19.13 ? 1194 SER   A N     1 
ATOM   8787  C  CA    . SER   A  1  1196 ? 11.114  76.374  120.367 1.00 20.94 ? 1194 SER   A CA    1 
ATOM   8788  C  C     . SER   A  1  1196 ? 12.133  75.324  119.933 1.00 19.80 ? 1194 SER   A C     1 
ATOM   8789  O  O     . SER   A  1  1196 ? 11.791  74.199  119.563 1.00 19.63 ? 1194 SER   A O     1 
ATOM   8790  C  CB    . SER   A  1  1196 ? 11.136  76.478  121.887 1.00 24.11 ? 1194 SER   A CB    1 
ATOM   8791  O  OG    . SER   A  1  1196 ? 10.934  75.199  122.450 1.00 22.69 ? 1194 SER   A OG    1 
ATOM   8792  N  N     . SER   A  1  1197 ? 13.408  75.701  119.985 1.00 20.62 ? 1195 SER   A N     1 
ATOM   8793  C  CA    . SER   A  1  1197 ? 14.453  74.720  119.715 1.00 21.83 ? 1195 SER   A CA    1 
ATOM   8794  C  C     . SER   A  1  1197 ? 14.353  73.536  120.672 1.00 20.02 ? 1195 SER   A C     1 
ATOM   8795  O  O     . SER   A  1  1197 ? 14.521  72.380  120.262 1.00 21.22 ? 1195 SER   A O     1 
ATOM   8796  C  CB    . SER   A  1  1197 ? 15.825  75.381  119.823 1.00 22.20 ? 1195 SER   A CB    1 
ATOM   8797  O  OG    . SER   A  1  1197 ? 15.938  76.479  118.933 1.00 23.74 ? 1195 SER   A OG    1 
ATOM   8798  N  N     . GLY   A  1  1198 ? 14.082  73.806  121.950 1.00 21.91 ? 1196 GLY   A N     1 
ATOM   8799  C  CA    . GLY   A  1  1198 ? 13.955  72.721  122.912 1.00 23.50 ? 1196 GLY   A CA    1 
ATOM   8800  C  C     . GLY   A  1  1198 ? 12.766  71.824  122.626 1.00 25.34 ? 1196 GLY   A C     1 
ATOM   8801  O  O     . GLY   A  1  1198 ? 12.843  70.601  122.783 1.00 23.86 ? 1196 GLY   A O     1 
ATOM   8802  N  N     . GLU   A  1  1199 ? 11.656  72.415  122.181 1.00 21.94 ? 1197 GLU   A N     1 
ATOM   8803  C  CA    . GLU   A  1  1199 ? 10.495  71.620  121.813 1.00 23.96 ? 1197 GLU   A CA    1 
ATOM   8804  C  C     . GLU   A  1  1199 ? 10.808  70.724  120.624 1.00 23.18 ? 1197 GLU   A C     1 
ATOM   8805  O  O     . GLU   A  1  1199 ? 10.400  69.559  120.587 1.00 22.67 ? 1197 GLU   A O     1 
ATOM   8806  C  CB    . GLU   A  1  1199 ? 9.347   72.561  121.484 1.00 20.70 ? 1197 GLU   A CB    1 
ATOM   8807  C  CG    . GLU   A  1  1199 ? 8.020   71.909  121.275 1.00 26.89 ? 1197 GLU   A CG    1 
ATOM   8808  C  CD    . GLU   A  1  1199 ? 6.921   72.945  121.129 1.00 36.33 ? 1197 GLU   A CD    1 
ATOM   8809  O  OE1   . GLU   A  1  1199 ? 7.227   74.155  121.286 1.00 33.83 ? 1197 GLU   A OE1   1 
ATOM   8810  O  OE2   . GLU   A  1  1199 ? 5.762   72.555  120.868 1.00 45.92 ? 1197 GLU   A OE2   1 
ATOM   8811  N  N     . ILE   A  1  1200 ? 11.531  71.253  119.635 1.00 21.09 ? 1198 ILE   A N     1 
ATOM   8812  C  CA    . ILE   A  1  1200 ? 11.954  70.431  118.506 1.00 21.95 ? 1198 ILE   A CA    1 
ATOM   8813  C  C     . ILE   A  1  1200 ? 12.791  69.254  118.990 1.00 23.80 ? 1198 ILE   A C     1 
ATOM   8814  O  O     . ILE   A  1  1200 ? 12.639  68.126  118.509 1.00 22.95 ? 1198 ILE   A O     1 
ATOM   8815  C  CB    . ILE   A  1  1200 ? 12.701  71.295  117.470 1.00 20.19 ? 1198 ILE   A CB    1 
ATOM   8816  C  CG1   . ILE   A  1  1200 ? 11.733  72.289  116.826 1.00 20.75 ? 1198 ILE   A CG1   1 
ATOM   8817  C  CG2   . ILE   A  1  1200 ? 13.373  70.419  116.408 1.00 21.66 ? 1198 ILE   A CG2   1 
ATOM   8818  C  CD1   . ILE   A  1  1200 ? 12.394  73.295  115.929 1.00 21.78 ? 1198 ILE   A CD1   1 
ATOM   8819  N  N     . ALA   A  1  1201 ? 13.656  69.488  119.980 1.00 21.65 ? 1199 ALA   A N     1 
ATOM   8820  C  CA    . ALA   A  1  1201 ? 14.494  68.410  120.491 1.00 23.38 ? 1199 ALA   A CA    1 
ATOM   8821  C  C     . ALA   A  1  1201 ? 13.674  67.391  121.272 1.00 24.96 ? 1199 ALA   A C     1 
ATOM   8822  O  O     . ALA   A  1  1201 ? 13.942  66.184  121.202 1.00 24.90 ? 1199 ALA   A O     1 
ATOM   8823  C  CB    . ALA   A  1  1201 ? 15.599  68.986  121.374 1.00 25.35 ? 1199 ALA   A CB    1 
ATOM   8824  N  N     . ARG   A  1  1202 ? 12.675  67.853  122.021 1.00 21.97 ? 1200 ARG   A N     1 
ATOM   8825  C  CA    . ARG   A  1  1202 ? 11.932  66.980  122.921 1.00 23.61 ? 1200 ARG   A CA    1 
ATOM   8826  C  C     . ARG   A  1  1202 ? 10.779  66.265  122.235 1.00 25.99 ? 1200 ARG   A C     1 
ATOM   8827  O  O     . ARG   A  1  1202 ? 10.484  65.111  122.563 1.00 25.99 ? 1200 ARG   A O     1 
ATOM   8828  C  CB    . ARG   A  1  1202 ? 11.385  67.779  124.106 1.00 22.10 ? 1200 ARG   A CB    1 
ATOM   8829  C  CG    . ARG   A  1  1202 ? 12.462  68.262  125.060 1.00 22.91 ? 1200 ARG   A CG    1 
ATOM   8830  C  CD    . ARG   A  1  1202 ? 11.855  68.924  126.287 1.00 25.52 ? 1200 ARG   A CD    1 
ATOM   8831  N  NE    . ARG   A  1  1202 ? 11.019  70.056  125.915 1.00 28.09 ? 1200 ARG   A NE    1 
ATOM   8832  C  CZ    . ARG   A  1  1202 ? 11.407  71.325  125.916 1.00 27.43 ? 1200 ARG   A CZ    1 
ATOM   8833  N  NH1   . ARG   A  1  1202 ? 12.598  71.686  126.369 1.00 25.25 ? 1200 ARG   A NH1   1 
ATOM   8834  N  NH2   . ARG   A  1  1202 ? 10.581  72.254  125.440 1.00 30.27 ? 1200 ARG   A NH2   1 
ATOM   8835  N  N     . ASN   A  1  1203 ? 10.118  66.921  121.294 1.00 22.95 ? 1201 ASN   A N     1 
ATOM   8836  C  CA    . ASN   A  1  1203 ? 8.855   66.416  120.766 1.00 23.56 ? 1201 ASN   A CA    1 
ATOM   8837  C  C     . ASN   A  1  1203 ? 8.981   66.121  119.284 1.00 28.36 ? 1201 ASN   A C     1 
ATOM   8838  O  O     . ASN   A  1  1203 ? 9.070   67.063  118.474 1.00 25.21 ? 1201 ASN   A O     1 
ATOM   8839  C  CB    . ASN   A  1  1203 ? 7.751   67.441  121.005 1.00 24.18 ? 1201 ASN   A CB    1 
ATOM   8840  C  CG    . ASN   A  1  1203 ? 6.395   66.959  120.528 1.00 27.57 ? 1201 ASN   A CG    1 
ATOM   8841  O  OD1   . ASN   A  1  1203 ? 6.244   65.818  120.089 1.00 28.86 ? 1201 ASN   A OD1   1 
ATOM   8842  N  ND2   . ASN   A  1  1203 ? 5.396   67.829  120.619 1.00 30.29 ? 1201 ASN   A ND2   1 
ATOM   8843  N  N     . PRO   A  1  1204 ? 8.956   64.850  118.880 1.00 26.09 ? 1202 PRO   A N     1 
ATOM   8844  C  CA    . PRO   A  1  1204 ? 9.001   64.534  117.446 1.00 30.02 ? 1202 PRO   A CA    1 
ATOM   8845  C  C     . PRO   A  1  1204 ? 7.854   65.136  116.665 1.00 27.91 ? 1202 PRO   A C     1 
ATOM   8846  O  O     . PRO   A  1  1204 ? 7.983   65.323  115.453 1.00 27.36 ? 1202 PRO   A O     1 
ATOM   8847  C  CB    . PRO   A  1  1204 ? 8.959   62.999  117.422 1.00 33.62 ? 1202 PRO   A CB    1 
ATOM   8848  C  CG    . PRO   A  1  1204 ? 9.421   62.583  118.793 1.00 36.14 ? 1202 PRO   A CG    1 
ATOM   8849  C  CD    . PRO   A  1  1204 ? 8.885   63.641  119.715 1.00 29.82 ? 1202 PRO   A CD    1 
ATOM   8850  N  N     . ASP   A  1  1205 ? 6.740   65.454  117.324 1.00 27.27 ? 1203 ASP   A N     1 
ATOM   8851  C  CA    . ASP   A  1  1205 ? 5.583   66.054  116.673 1.00 26.53 ? 1203 ASP   A CA    1 
ATOM   8852  C  C     . ASP   A  1  1205 ? 5.483   67.549  116.940 1.00 26.82 ? 1203 ASP   A C     1 
ATOM   8853  O  O     . ASP   A  1  1205 ? 4.383   68.113  116.892 1.00 30.16 ? 1203 ASP   A O     1 
ATOM   8854  C  CB    . ASP   A  1  1205 ? 4.300   65.349  117.112 1.00 32.56 ? 1203 ASP   A CB    1 
ATOM   8855  C  CG    . ASP   A  1  1205 ? 4.296   63.876  116.762 1.00 35.06 ? 1203 ASP   A CG    1 
ATOM   8856  O  OD1   . ASP   A  1  1205 ? 5.046   63.475  115.843 1.00 32.97 ? 1203 ASP   A OD1   1 
ATOM   8857  O  OD2   . ASP   A  1  1205 ? 3.541   63.120  117.409 1.00 41.09 ? 1203 ASP   A OD2   1 
ATOM   8858  N  N     . ALA   A  1  1206 ? 6.611   68.194  117.247 1.00 23.48 ? 1204 ALA   A N     1 
ATOM   8859  C  CA    . ALA   A  1  1206 ? 6.616   69.638  117.460 1.00 23.41 ? 1204 ALA   A CA    1 
ATOM   8860  C  C     . ALA   A  1  1206 ? 5.924   70.358  116.312 1.00 23.34 ? 1204 ALA   A C     1 
ATOM   8861  O  O     . ALA   A  1  1206 ? 5.126   71.279  116.531 1.00 25.85 ? 1204 ALA   A O     1 
ATOM   8862  C  CB    . ALA   A  1  1206 ? 8.055   70.125  117.589 1.00 22.94 ? 1204 ALA   A CB    1 
ATOM   8863  N  N     . TYR   A  1  1207 ? 6.211   69.947  115.083 1.00 22.00 ? 1205 TYR   A N     1 
ATOM   8864  C  CA    . TYR   A  1  1207 ? 5.460   70.383  113.917 1.00 22.33 ? 1205 TYR   A CA    1 
ATOM   8865  C  C     . TYR   A  1  1207 ? 4.563   69.235  113.487 1.00 22.54 ? 1205 TYR   A C     1 
ATOM   8866  O  O     . TYR   A  1  1207 ? 5.048   68.153  113.142 1.00 28.19 ? 1205 TYR   A O     1 
ATOM   8867  C  CB    . TYR   A  1  1207 ? 6.398   70.773  112.780 1.00 19.70 ? 1205 TYR   A CB    1 
ATOM   8868  C  CG    . TYR   A  1  1207 ? 7.339   71.888  113.151 1.00 19.15 ? 1205 TYR   A CG    1 
ATOM   8869  C  CD1   . TYR   A  1  1207 ? 6.852   73.139  113.519 1.00 19.87 ? 1205 TYR   A CD1   1 
ATOM   8870  C  CD2   . TYR   A  1  1207 ? 8.710   71.692  113.141 1.00 19.90 ? 1205 TYR   A CD2   1 
ATOM   8871  C  CE1   . TYR   A  1  1207 ? 7.710   74.161  113.861 1.00 17.98 ? 1205 TYR   A CE1   1 
ATOM   8872  C  CE2   . TYR   A  1  1207 ? 9.575   72.711  113.481 1.00 21.67 ? 1205 TYR   A CE2   1 
ATOM   8873  C  CZ    . TYR   A  1  1207 ? 9.065   73.940  113.836 1.00 19.63 ? 1205 TYR   A CZ    1 
ATOM   8874  O  OH    . TYR   A  1  1207 ? 9.921   74.951  114.175 1.00 20.00 ? 1205 TYR   A OH    1 
ATOM   8875  N  N     . CYS   A  1  1208 ? 3.266   69.474  113.494 1.00 19.45 ? 1206 CYS   A N     1 
ATOM   8876  C  CA    . CYS   A  1  1208 ? 2.300   68.432  113.204 1.00 19.73 ? 1206 CYS   A CA    1 
ATOM   8877  C  C     . CYS   A  1  1208 ? 2.117   68.317  111.696 1.00 19.01 ? 1206 CYS   A C     1 
ATOM   8878  O  O     . CYS   A  1  1208 ? 1.836   69.309  111.016 1.00 18.38 ? 1206 CYS   A O     1 
ATOM   8879  C  CB    . CYS   A  1  1208 ? 0.981   68.771  113.891 1.00 22.50 ? 1206 CYS   A CB    1 
ATOM   8880  S  SG    . CYS   A  1  1208 ? -0.331  67.603  113.583 1.00 26.97 ? 1206 CYS   A SG    1 
ATOM   8881  N  N     . LEU   A  1  1209 ? 2.287   67.101  111.179 1.00 16.62 ? 1207 LEU   A N     1 
ATOM   8882  C  CA    . LEU   A  1  1209 ? 2.198   66.885  109.745 1.00 16.67 ? 1207 LEU   A CA    1 
ATOM   8883  C  C     . LEU   A  1  1209 ? 0.770   67.001  109.222 1.00 17.06 ? 1207 LEU   A C     1 
ATOM   8884  O  O     . LEU   A  1  1209 ? 0.593   67.173  108.012 1.00 17.88 ? 1207 LEU   A O     1 
ATOM   8885  C  CB    . LEU   A  1  1209 ? 2.803   65.528  109.367 1.00 17.59 ? 1207 LEU   A CB    1 
ATOM   8886  C  CG    . LEU   A  1  1209 ? 4.248   65.330  109.812 1.00 17.06 ? 1207 LEU   A CG    1 
ATOM   8887  C  CD1   . LEU   A  1  1209 ? 4.728   63.981  109.323 1.00 19.06 ? 1207 LEU   A CD1   1 
ATOM   8888  C  CD2   . LEU   A  1  1209 ? 5.139   66.445  109.287 1.00 20.14 ? 1207 LEU   A CD2   1 
ATOM   8889  N  N     . ASN   A  1  1210 ? -0.241  66.920  110.099 1.00 18.77 ? 1208 ASN   A N     1 
ATOM   8890  C  CA    . ASN   A  1  1210 ? -1.626  67.102  109.667 1.00 19.20 ? 1208 ASN   A CA    1 
ATOM   8891  C  C     . ASN   A  1  1210 ? -1.798  68.424  108.934 1.00 19.01 ? 1208 ASN   A C     1 
ATOM   8892  O  O     . ASN   A  1  1210 ? -2.588  68.525  107.995 1.00 20.78 ? 1208 ASN   A O     1 
ATOM   8893  C  CB    . ASN   A  1  1210 ? -2.587  67.115  110.868 1.00 21.79 ? 1208 ASN   A CB    1 
ATOM   8894  C  CG    . ASN   A  1  1210 ? -2.708  65.769  111.571 1.00 23.61 ? 1208 ASN   A CG    1 
ATOM   8895  O  OD1   . ASN   A  1  1210 ? -1.937  64.843  111.332 1.00 32.09 ? 1208 ASN   A OD1   1 
ATOM   8896  N  ND2   . ASN   A  1  1210 ? -3.680  65.676  112.476 1.00 32.58 ? 1208 ASN   A ND2   1 
ATOM   8897  N  N     . TRP   A  1  1211 ? -1.094  69.462  109.379 1.00 18.78 ? 1209 TRP   A N     1 
ATOM   8898  C  CA    . TRP   A  1  1211 ? -1.322  70.804  108.867 1.00 18.40 ? 1209 TRP   A CA    1 
ATOM   8899  C  C     . TRP   A  1  1211 ? -0.385  71.168  107.729 1.00 18.52 ? 1209 TRP   A C     1 
ATOM   8900  O  O     . TRP   A  1  1211 ? -0.418  72.309  107.260 1.00 22.22 ? 1209 TRP   A O     1 
ATOM   8901  C  CB    . TRP   A  1  1211 ? -1.240  71.836  109.998 1.00 19.67 ? 1209 TRP   A CB    1 
ATOM   8902  C  CG    . TRP   A  1  1211 ? -1.809  71.330  111.284 1.00 20.22 ? 1209 TRP   A CG    1 
ATOM   8903  C  CD1   . TRP   A  1  1211 ? -1.178  71.281  112.499 1.00 19.76 ? 1209 TRP   A CD1   1 
ATOM   8904  C  CD2   . TRP   A  1  1211 ? -3.113  70.768  111.487 1.00 18.85 ? 1209 TRP   A CD2   1 
ATOM   8905  N  NE1   . TRP   A  1  1211 ? -2.013  70.728  113.440 1.00 22.00 ? 1209 TRP   A NE1   1 
ATOM   8906  C  CE2   . TRP   A  1  1211 ? -3.205  70.407  112.844 1.00 20.05 ? 1209 TRP   A CE2   1 
ATOM   8907  C  CE3   . TRP   A  1  1211 ? -4.210  70.530  110.650 1.00 19.54 ? 1209 TRP   A CE3   1 
ATOM   8908  C  CZ2   . TRP   A  1  1211 ? -4.347  69.823  113.385 1.00 21.59 ? 1209 TRP   A CZ2   1 
ATOM   8909  C  CZ3   . TRP   A  1  1211 ? -5.351  69.953  111.195 1.00 21.65 ? 1209 TRP   A CZ3   1 
ATOM   8910  C  CH2   . TRP   A  1  1211 ? -5.403  69.601  112.546 1.00 22.06 ? 1209 TRP   A CH2   1 
ATOM   8911  N  N     . LEU   A  1  1212 ? 0.442   70.227  107.276 1.00 16.46 ? 1210 LEU   A N     1 
ATOM   8912  C  CA    . LEU   A  1  1212 ? 1.365   70.431  106.171 1.00 16.72 ? 1210 LEU   A CA    1 
ATOM   8913  C  C     . LEU   A  1  1212 ? 0.912   69.713  104.909 1.00 15.36 ? 1210 LEU   A C     1 
ATOM   8914  O  O     . LEU   A  1  1212 ? 1.611   69.750  103.889 1.00 15.11 ? 1210 LEU   A O     1 
ATOM   8915  C  CB    . LEU   A  1  1212 ? 2.767   69.975  106.577 1.00 15.16 ? 1210 LEU   A CB    1 
ATOM   8916  C  CG    . LEU   A  1  1212 ? 3.428   70.957  107.534 1.00 16.32 ? 1210 LEU   A CG    1 
ATOM   8917  C  CD1   . LEU   A  1  1212 ? 4.578   70.292  108.272 1.00 17.50 ? 1210 LEU   A CD1   1 
ATOM   8918  C  CD2   . LEU   A  1  1212 ? 3.910   72.168  106.742 1.00 19.77 ? 1210 LEU   A CD2   1 
ATOM   8919  N  N     . VAL   A  1  1213 ? -0.242  69.059  104.962 1.00 15.58 ? 1211 VAL   A N     1 
ATOM   8920  C  CA    . VAL   A  1  1213 ? -0.884  68.513  103.782 1.00 16.17 ? 1211 VAL   A CA    1 
ATOM   8921  C  C     . VAL   A  1  1213 ? -2.154  69.298  103.526 1.00 16.11 ? 1211 VAL   A C     1 
ATOM   8922  O  O     . VAL   A  1  1213 ? -2.684  69.998  104.394 1.00 17.07 ? 1211 VAL   A O     1 
ATOM   8923  C  CB    . VAL   A  1  1213 ? -1.180  67.002  103.882 1.00 15.67 ? 1211 VAL   A CB    1 
ATOM   8924  C  CG1   . VAL   A  1  1213 ? 0.115   66.205  103.917 1.00 17.18 ? 1211 VAL   A CG1   1 
ATOM   8925  C  CG2   . VAL   A  1  1213 ? -2.034  66.702  105.092 1.00 18.58 ? 1211 VAL   A CG2   1 
ATOM   8926  N  N     . GLU   A  1  1214 ? -2.638  69.172  102.304 1.00 16.09 ? 1212 GLU   A N     1 
ATOM   8927  C  CA    . GLU   A  1  1214 ? -3.846  69.834  101.850 1.00 17.93 ? 1212 GLU   A CA    1 
ATOM   8928  C  C     . GLU   A  1  1214 ? -4.859  68.755  101.515 1.00 15.38 ? 1212 GLU   A C     1 
ATOM   8929  O  O     . GLU   A  1  1214 ? -4.557  67.821  100.769 1.00 15.02 ? 1212 GLU   A O     1 
ATOM   8930  C  CB    . GLU   A  1  1214 ? -3.518  70.618  100.593 1.00 21.46 ? 1212 GLU   A CB    1 
ATOM   8931  C  CG    . GLU   A  1  1214 ? -4.596  71.518  100.090 1.00 29.15 ? 1212 GLU   A CG    1 
ATOM   8932  C  CD    . GLU   A  1  1214 ? -4.046  72.432  99.025  1.00 31.99 ? 1212 GLU   A CD    1 
ATOM   8933  O  OE1   . GLU   A  1  1214 ? -3.365  73.418  99.388  1.00 34.65 ? 1212 GLU   A OE1   1 
ATOM   8934  O  OE2   . GLU   A  1  1214 ? -4.250  72.135  97.833  1.00 35.62 ? 1212 GLU   A OE2   1 
ATOM   8935  N  N     . GLU   A  1  1215 ? -6.047  68.877  102.075 1.00 15.80 ? 1213 GLU   A N     1 
ATOM   8936  C  CA    . GLU   A  1  1215 ? -7.126  67.965  101.748 1.00 14.79 ? 1213 GLU   A CA    1 
ATOM   8937  C  C     . GLU   A  1  1215 ? -7.801  68.403  100.457 1.00 14.56 ? 1213 GLU   A C     1 
ATOM   8938  O  O     . GLU   A  1  1215 ? -8.051  69.594  100.232 1.00 15.80 ? 1213 GLU   A O     1 
ATOM   8939  C  CB    . GLU   A  1  1215 ? -8.170  68.002  102.851 1.00 15.12 ? 1213 GLU   A CB    1 
ATOM   8940  C  CG    . GLU   A  1  1215 ? -7.683  67.559  104.212 1.00 15.60 ? 1213 GLU   A CG    1 
ATOM   8941  C  CD    . GLU   A  1  1215 ? -8.648  67.956  105.297 1.00 14.03 ? 1213 GLU   A CD    1 
ATOM   8942  O  OE1   . GLU   A  1  1215 ? -8.630  69.148  105.682 1.00 17.63 ? 1213 GLU   A OE1   1 
ATOM   8943  O  OE2   . GLU   A  1  1215 ? -9.416  67.079  105.739 1.00 17.23 ? 1213 GLU   A OE2   1 
ATOM   8944  N  N     . VAL   A  1  1216 ? -8.109  67.434  99.614  1.00 14.80 ? 1214 VAL   A N     1 
ATOM   8945  C  CA    . VAL   A  1  1216 ? -8.875  67.681  98.401  1.00 15.46 ? 1214 VAL   A CA    1 
ATOM   8946  C  C     . VAL   A  1  1216 ? -10.023 66.692  98.361  1.00 14.77 ? 1214 VAL   A C     1 
ATOM   8947  O  O     . VAL   A  1  1216 ? -9.825  65.488  98.525  1.00 16.45 ? 1214 VAL   A O     1 
ATOM   8948  C  CB    . VAL   A  1  1216 ? -8.012  67.580  97.139  1.00 15.30 ? 1214 VAL   A CB    1 
ATOM   8949  C  CG1   . VAL   A  1  1216 ? -8.886  67.797  95.909  1.00 16.45 ? 1214 VAL   A CG1   1 
ATOM   8950  C  CG2   . VAL   A  1  1216 ? -6.894  68.613  97.206  1.00 18.52 ? 1214 VAL   A CG2   1 
ATOM   8951  N  N     . SER   A  1  1217 ? -11.224 67.208  98.196  1.00 14.67 ? 1215 SER   A N     1 
ATOM   8952  C  CA    . SER   A  1  1217 ? -12.408 66.392  98.014  1.00 15.09 ? 1215 SER   A CA    1 
ATOM   8953  C  C     . SER   A  1  1217 ? -12.809 66.481  96.555  1.00 13.90 ? 1215 SER   A C     1 
ATOM   8954  O  O     . SER   A  1  1217 ? -12.756 67.559  95.962  1.00 15.20 ? 1215 SER   A O     1 
ATOM   8955  C  CB    . SER   A  1  1217 ? -13.548 66.954  98.847  1.00 15.92 ? 1215 SER   A CB    1 
ATOM   8956  O  OG    . SER   A  1  1217 ? -14.801 66.448  98.424  1.00 17.87 ? 1215 SER   A OG    1 
ATOM   8957  N  N     . ALA   A  1  1218 ? -13.153 65.344  95.970  1.00 13.24 ? 1216 ALA   A N     1 
ATOM   8958  C  CA    . ALA   A  1  1218 ? -13.639 65.303  94.597  1.00 14.21 ? 1216 ALA   A CA    1 
ATOM   8959  C  C     . ALA   A  1  1218 ? -14.911 64.479  94.569  1.00 15.61 ? 1216 ALA   A C     1 
ATOM   8960  O  O     . ALA   A  1  1218 ? -14.935 63.347  95.056  1.00 16.82 ? 1216 ALA   A O     1 
ATOM   8961  C  CB    . ALA   A  1  1218 ? -12.601 64.698  93.653  1.00 15.26 ? 1216 ALA   A CB    1 
ATOM   8962  N  N     . SER   A  1  1219 ? -15.967 65.048  94.001  1.00 14.76 ? 1217 SER   A N     1 
ATOM   8963  C  CA    . SER   A  1  1219 ? -17.247 64.369  93.887  1.00 15.57 ? 1217 SER   A CA    1 
ATOM   8964  C  C     . SER   A  1  1219 ? -17.554 64.205  92.412  1.00 13.60 ? 1217 SER   A C     1 
ATOM   8965  O  O     . SER   A  1  1219 ? -17.689 65.195  91.686  1.00 15.42 ? 1217 SER   A O     1 
ATOM   8966  C  CB    . SER   A  1  1219 ? -18.346 65.169  94.575  1.00 15.29 ? 1217 SER   A CB    1 
ATOM   8967  O  OG    . SER   A  1  1219 ? -19.582 64.490  94.443  1.00 15.67 ? 1217 SER   A OG    1 
ATOM   8968  N  N     . ILE   A  1  1220 ? -17.648 62.960  91.975  1.00 14.07 ? 1218 ILE   A N     1 
ATOM   8969  C  CA    . ILE   A  1  1220 ? -17.844 62.625  90.573  1.00 13.59 ? 1218 ILE   A CA    1 
ATOM   8970  C  C     . ILE   A  1  1220 ? -19.237 62.041  90.426  1.00 14.45 ? 1218 ILE   A C     1 
ATOM   8971  O  O     . ILE   A  1  1220 ? -19.554 61.023  91.046  1.00 14.94 ? 1218 ILE   A O     1 
ATOM   8972  C  CB    . ILE   A  1  1220 ? -16.799 61.605  90.107  1.00 18.01 ? 1218 ILE   A CB    1 
ATOM   8973  C  CG1   . ILE   A  1  1220 ? -15.395 62.150  90.349  1.00 20.05 ? 1218 ILE   A CG1   1 
ATOM   8974  C  CG2   . ILE   A  1  1220 ? -17.011 61.308  88.643  1.00 19.23 ? 1218 ILE   A CG2   1 
ATOM   8975  C  CD1   . ILE   A  1  1220 ? -14.300 61.107  90.243  1.00 29.12 ? 1218 ILE   A CD1   1 
ATOM   8976  N  N     . ASN   A  1  1221 ? -20.045 62.655  89.569  1.00 14.09 ? 1219 ASN   A N     1 
ATOM   8977  C  CA    . ASN   A  1  1221 ? -21.370 62.130  89.253  1.00 15.68 ? 1219 ASN   A CA    1 
ATOM   8978  C  C     . ASN   A  1  1221 ? -21.179 61.006  88.243  1.00 14.20 ? 1219 ASN   A C     1 
ATOM   8979  O  O     . ASN   A  1  1221 ? -20.951 61.251  87.060  1.00 19.18 ? 1219 ASN   A O     1 
ATOM   8980  C  CB    . ASN   A  1  1221 ? -22.241 63.240  88.684  1.00 16.85 ? 1219 ASN   A CB    1 
ATOM   8981  C  CG    . ASN   A  1  1221 ? -23.570 62.731  88.183  1.00 16.25 ? 1219 ASN   A CG    1 
ATOM   8982  O  OD1   . ASN   A  1  1221 ? -23.943 61.585  88.421  1.00 15.29 ? 1219 ASN   A OD1   1 
ATOM   8983  N  ND2   . ASN   A  1  1221 ? -24.284 63.584  87.470  1.00 18.12 ? 1219 ASN   A ND2   1 
ATOM   8984  N  N     . THR   A  1  1222 ? -21.296 59.771  88.705  1.00 14.71 ? 1220 THR   A N     1 
ATOM   8985  C  CA    . THR   A  1  1222 ? -21.074 58.622  87.844  1.00 17.01 ? 1220 THR   A CA    1 
ATOM   8986  C  C     . THR   A  1  1222 ? -22.349 58.168  87.161  1.00 20.62 ? 1220 THR   A C     1 
ATOM   8987  O  O     . THR   A  1  1222 ? -22.324 57.178  86.425  1.00 24.32 ? 1220 THR   A O     1 
ATOM   8988  C  CB    . THR   A  1  1222 ? -20.454 57.471  88.637  1.00 20.67 ? 1220 THR   A CB    1 
ATOM   8989  O  OG1   . THR   A  1  1222 ? -21.326 57.113  89.714  1.00 19.81 ? 1220 THR   A OG1   1 
ATOM   8990  C  CG2   . THR   A  1  1222 ? -19.106 57.899  89.199  1.00 20.28 ? 1220 THR   A CG2   1 
ATOM   8991  N  N     . ALA   A  1  1223 ? -23.459 58.861  87.393  1.00 17.12 ? 1221 ALA   A N     1 
ATOM   8992  C  CA    . ALA   A  1  1223 ? -24.688 58.636  86.658  1.00 22.07 ? 1221 ALA   A CA    1 
ATOM   8993  C  C     . ALA   A  1  1223 ? -24.845 59.600  85.491  1.00 23.62 ? 1221 ALA   A C     1 
ATOM   8994  O  O     . ALA   A  1  1223 ? -25.884 59.573  84.824  1.00 28.58 ? 1221 ALA   A O     1 
ATOM   8995  C  CB    . ALA   A  1  1223 ? -25.888 58.779  87.595  1.00 20.89 ? 1221 ALA   A CB    1 
ATOM   8996  N  N     . ALA   A  1  1224 ? -23.847 60.458  85.239  1.00 24.40 ? 1222 ALA   A N     1 
ATOM   8997  C  CA    . ALA   A  1  1224 ? -24.014 61.546  84.278  1.00 27.91 ? 1222 ALA   A CA    1 
ATOM   8998  C  C     . ALA   A  1  1224 ? -24.225 61.033  82.859  1.00 31.14 ? 1222 ALA   A C     1 
ATOM   8999  O  O     . ALA   A  1  1224 ? -24.869 61.710  82.050  1.00 31.20 ? 1222 ALA   A O     1 
ATOM   9000  C  CB    . ALA   A  1  1224 ? -22.813 62.493  84.329  1.00 27.29 ? 1222 ALA   A CB    1 
ATOM   9001  N  N     . ALA   A  1  1225 ? -23.692 59.853  82.532  1.00 27.09 ? 1223 ALA   A N     1 
ATOM   9002  C  CA    . ALA   A  1  1225 ? -23.878 59.317  81.187  1.00 33.32 ? 1223 ALA   A CA    1 
ATOM   9003  C  C     . ALA   A  1  1225 ? -25.313 58.889  80.921  1.00 34.58 ? 1223 ALA   A C     1 
ATOM   9004  O  O     . ALA   A  1  1225 ? -25.652 58.600  79.767  1.00 34.59 ? 1223 ALA   A O     1 
ATOM   9005  C  CB    . ALA   A  1  1225 ? -22.912 58.160  80.919  1.00 33.35 ? 1223 ALA   A CB    1 
ATOM   9006  N  N     . GLY   A  1  1226 ? -26.157 58.851  81.946  1.00 29.50 ? 1224 GLY   A N     1 
ATOM   9007  C  CA    . GLY   A  1  1226 ? -27.563 58.520  81.794  1.00 32.23 ? 1224 GLY   A CA    1 
ATOM   9008  C  C     . GLY   A  1  1226 ? -28.002 57.319  82.596  1.00 34.82 ? 1224 GLY   A C     1 
ATOM   9009  O  O     . GLY   A  1  1226 ? -29.204 57.010  82.622  1.00 30.87 ? 1224 GLY   A O     1 
ATOM   9010  N  N     . GLY   A  1  1227 ? -27.080 56.630  83.255  1.00 25.78 ? 1225 GLY   A N     1 
ATOM   9011  C  CA    . GLY   A  1  1227 ? -27.434 55.472  84.052  1.00 31.76 ? 1225 GLY   A CA    1 
ATOM   9012  C  C     . GLY   A  1  1227 ? -26.326 55.165  85.030  1.00 30.50 ? 1225 GLY   A C     1 
ATOM   9013  O  O     . GLY   A  1  1227 ? -25.240 55.750  84.986  1.00 28.99 ? 1225 GLY   A O     1 
ATOM   9014  N  N     . ASN   A  1  1228 ? -26.618 54.222  85.915  1.00 25.95 ? 1226 ASN   A N     1 
ATOM   9015  C  CA    . ASN   A  1  1228 ? -25.703 53.805  86.969  1.00 26.06 ? 1226 ASN   A CA    1 
ATOM   9016  C  C     . ASN   A  1  1228 ? -25.214 52.399  86.632  1.00 31.25 ? 1226 ASN   A C     1 
ATOM   9017  O  O     . ASN   A  1  1228 ? -25.982 51.432  86.700  1.00 29.71 ? 1226 ASN   A O     1 
ATOM   9018  C  CB    . ASN   A  1  1228 ? -26.435 53.834  88.309  1.00 28.21 ? 1226 ASN   A CB    1 
ATOM   9019  C  CG    . ASN   A  1  1228 ? -25.519 53.570  89.493  1.00 30.97 ? 1226 ASN   A CG    1 
ATOM   9020  O  OD1   . ASN   A  1  1228 ? -24.584 52.771  89.415  1.00 31.58 ? 1226 ASN   A OD1   1 
ATOM   9021  N  ND2   . ASN   A  1  1228 ? -25.801 54.235  90.608  1.00 32.56 ? 1226 ASN   A ND2   1 
ATOM   9022  N  N     . ALA   A  1  1229 ? -23.931 52.291  86.272  1.00 29.67 ? 1227 ALA   A N     1 
ATOM   9023  C  CA    . ALA   A  1  1229 ? -23.371 50.997  85.895  1.00 29.03 ? 1227 ALA   A CA    1 
ATOM   9024  C  C     . ALA   A  1  1229 ? -23.415 50.010  87.055  1.00 29.14 ? 1227 ALA   A C     1 
ATOM   9025  O  O     . ALA   A  1  1229 ? -23.768 48.839  86.870  1.00 31.91 ? 1227 ALA   A O     1 
ATOM   9026  C  CB    . ALA   A  1  1229 ? -21.935 51.177  85.405  1.00 29.55 ? 1227 ALA   A CB    1 
ATOM   9027  N  N     . SER   A  1  1230 ? -23.053 50.459  88.259  1.00 31.08 ? 1228 SER   A N     1 
ATOM   9028  C  CA    . SER   A  1  1230 ? -23.022 49.546  89.399  1.00 32.30 ? 1228 SER   A CA    1 
ATOM   9029  C  C     . SER   A  1  1230 ? -24.413 49.001  89.711  1.00 36.14 ? 1228 SER   A C     1 
ATOM   9030  O  O     . SER   A  1  1230 ? -24.568 47.813  90.027  1.00 34.18 ? 1228 SER   A O     1 
ATOM   9031  C  CB    . SER   A  1  1230 ? -22.411 50.240  90.618  1.00 35.85 ? 1228 SER   A CB    1 
ATOM   9032  N  N     . LEU   A  1  1231 ? -25.442 49.842  89.601  1.00 30.44 ? 1229 LEU   A N     1 
ATOM   9033  C  CA    . LEU   A  1  1231 ? -26.801 49.393  89.881  1.00 36.17 ? 1229 LEU   A CA    1 
ATOM   9034  C  C     . LEU   A  1  1231 ? -27.391 48.517  88.779  1.00 36.60 ? 1229 LEU   A C     1 
ATOM   9035  O  O     . LEU   A  1  1231 ? -28.463 47.935  88.983  1.00 38.69 ? 1229 LEU   A O     1 
ATOM   9036  C  CB    . LEU   A  1  1231 ? -27.720 50.581  90.180  1.00 33.16 ? 1229 LEU   A CB    1 
ATOM   9037  C  CG    . LEU   A  1  1231 ? -27.660 51.198  91.583  1.00 33.95 ? 1229 LEU   A CG    1 
ATOM   9038  C  CD1   . LEU   A  1  1231 ? -28.720 52.276  91.737  1.00 30.46 ? 1229 LEU   A CD1   1 
ATOM   9039  C  CD2   . LEU   A  1  1231 ? -27.837 50.143  92.645  1.00 38.96 ? 1229 LEU   A CD2   1 
ATOM   9040  N  N     . MET   A  1  1232 ? -26.725 48.401  87.626  1.00 37.09 ? 1230 MET   A N     1 
ATOM   9041  C  CA    . MET   A  1  1232 ? -27.174 47.444  86.617  1.00 34.77 ? 1230 MET   A CA    1 
ATOM   9042  C  C     . MET   A  1  1232 ? -27.076 46.012  87.127  1.00 35.91 ? 1230 MET   A C     1 
ATOM   9043  O  O     . MET   A  1  1232 ? -27.788 45.127  86.639  1.00 36.76 ? 1230 MET   A O     1 
ATOM   9044  C  CB    . MET   A  1  1232 ? -26.360 47.602  85.330  1.00 37.04 ? 1230 MET   A CB    1 
ATOM   9045  C  CG    . MET   A  1  1232 ? -26.663 48.866  84.537  1.00 32.81 ? 1230 MET   A CG    1 
ATOM   9046  S  SD    . MET   A  1  1232 ? -25.533 49.042  83.130  1.00 41.64 ? 1230 MET   A SD    1 
ATOM   9047  C  CE    . MET   A  1  1232 ? -26.022 47.643  82.106  1.00 39.66 ? 1230 MET   A CE    1 
ATOM   9048  N  N     . ALA   A  1  1233 ? -26.206 45.770  88.106  1.00 37.05 ? 1231 ALA   A N     1 
ATOM   9049  C  CA    . ALA   A  1  1233 ? -26.037 44.459  88.716  1.00 39.49 ? 1231 ALA   A CA    1 
ATOM   9050  C  C     . ALA   A  1  1233 ? -26.946 44.241  89.919  1.00 46.21 ? 1231 ALA   A C     1 
ATOM   9051  O  O     . ALA   A  1  1233 ? -26.961 43.136  90.473  1.00 44.08 ? 1231 ALA   A O     1 
ATOM   9052  C  CB    . ALA   A  1  1233 ? -24.576 44.254  89.130  1.00 37.40 ? 1231 ALA   A CB    1 
ATOM   9053  N  N     . ILE   A  1  1234 ? -27.700 45.255  90.335  1.00 46.14 ? 1232 ILE   A N     1 
ATOM   9054  C  CA    . ILE   A  1  1234 ? -28.579 45.157  91.496  1.00 44.66 ? 1232 ILE   A CA    1 
ATOM   9055  C  C     . ILE   A  1  1234 ? -30.006 44.939  91.005  1.00 42.86 ? 1232 ILE   A C     1 
ATOM   9056  O  O     . ILE   A  1  1234 ? -30.658 45.861  90.499  1.00 33.00 ? 1232 ILE   A O     1 
ATOM   9057  C  CB    . ILE   A  1  1234 ? -28.462 46.381  92.414  1.00 41.41 ? 1232 ILE   A CB    1 
ATOM   9058  C  CG1   . ILE   A  1  1234 ? -27.034 46.488  92.961  1.00 42.14 ? 1232 ILE   A CG1   1 
ATOM   9059  C  CG2   . ILE   A  1  1234 ? -29.461 46.281  93.548  1.00 35.98 ? 1232 ILE   A CG2   1 
ATOM   9060  C  CD1   . ILE   A  1  1234 ? -26.925 47.204  94.293  1.00 38.90 ? 1232 ILE   A CD1   1 
ATOM   9061  N  N     . GLY   A  1  1235 ? -30.483 43.708  91.146  1.00 42.06 ? 1233 GLY   A N     1 
ATOM   9062  C  CA    . GLY   A  1  1235 ? -31.849 43.361  90.819  1.00 36.51 ? 1233 GLY   A CA    1 
ATOM   9063  C  C     . GLY   A  1  1235 ? -32.420 42.545  91.955  1.00 35.21 ? 1233 GLY   A C     1 
ATOM   9064  O  O     . GLY   A  1  1235 ? -31.687 41.828  92.638  1.00 38.85 ? 1233 GLY   A O     1 
ATOM   9065  O  OXT   . GLY   A  1  1235 ? -33.609 42.570  92.231  1.00 25.71 ? 1233 GLY   A OXT   1 
ATOM   9066  N  N     . ALA   B  1  16   ? 29.947  4.961   80.989  1.00 41.99 ? 14   ALA   B N     1 
ATOM   9067  C  CA    . ALA   B  1  16   ? 28.972  6.014   81.271  1.00 39.78 ? 14   ALA   B CA    1 
ATOM   9068  C  C     . ALA   B  1  16   ? 27.561  5.446   81.249  1.00 38.71 ? 14   ALA   B C     1 
ATOM   9069  O  O     . ALA   B  1  16   ? 27.230  4.641   80.380  1.00 43.08 ? 14   ALA   B O     1 
ATOM   9070  C  CB    . ALA   B  1  16   ? 29.097  7.147   80.258  1.00 35.63 ? 14   ALA   B CB    1 
ATOM   9071  N  N     . PRO   B  1  17   ? 26.728  5.865   82.201  1.00 37.77 ? 15   PRO   B N     1 
ATOM   9072  C  CA    . PRO   B  1  17   ? 25.339  5.393   82.215  1.00 34.33 ? 15   PRO   B CA    1 
ATOM   9073  C  C     . PRO   B  1  17   ? 24.594  5.861   80.974  1.00 32.45 ? 15   PRO   B C     1 
ATOM   9074  O  O     . PRO   B  1  17   ? 24.777  6.987   80.503  1.00 33.19 ? 15   PRO   B O     1 
ATOM   9075  C  CB    . PRO   B  1  17   ? 24.764  6.020   83.489  1.00 38.21 ? 15   PRO   B CB    1 
ATOM   9076  C  CG    . PRO   B  1  17   ? 25.642  7.198   83.765  1.00 42.55 ? 15   PRO   B CG    1 
ATOM   9077  C  CD    . PRO   B  1  17   ? 27.011  6.797   83.306  1.00 38.01 ? 15   PRO   B CD    1 
ATOM   9078  N  N     . ALA   B  1  18   ? 23.761  4.976   80.440  1.00 30.20 ? 16   ALA   B N     1 
ATOM   9079  C  CA    . ALA   B  1  18   ? 22.990  5.304   79.253  1.00 27.15 ? 16   ALA   B CA    1 
ATOM   9080  C  C     . ALA   B  1  18   ? 22.057  6.474   79.556  1.00 24.16 ? 16   ALA   B C     1 
ATOM   9081  O  O     . ALA   B  1  18   ? 21.493  6.549   80.653  1.00 24.83 ? 16   ALA   B O     1 
ATOM   9082  C  CB    . ALA   B  1  18   ? 22.162  4.098   78.815  1.00 28.71 ? 16   ALA   B CB    1 
ATOM   9083  N  N     . PRO   B  1  19   ? 21.884  7.404   78.622  1.00 23.08 ? 17   PRO   B N     1 
ATOM   9084  C  CA    . PRO   B  1  19   ? 21.046  8.579   78.897  1.00 21.38 ? 17   PRO   B CA    1 
ATOM   9085  C  C     . PRO   B  1  19   ? 19.624  8.181   79.263  1.00 21.04 ? 17   PRO   B C     1 
ATOM   9086  O  O     . PRO   B  1  19   ? 18.992  7.365   78.587  1.00 22.22 ? 17   PRO   B O     1 
ATOM   9087  C  CB    . PRO   B  1  19   ? 21.093  9.357   77.576  1.00 22.81 ? 17   PRO   B CB    1 
ATOM   9088  C  CG    . PRO   B  1  19   ? 22.396  8.971   76.977  1.00 24.90 ? 17   PRO   B CG    1 
ATOM   9089  C  CD    . PRO   B  1  19   ? 22.568  7.512   77.324  1.00 24.36 ? 17   PRO   B CD    1 
ATOM   9090  N  N     . PHE   B  1  20   ? 19.132  8.749   80.364  1.00 20.31 ? 18   PHE   B N     1 
ATOM   9091  C  CA    . PHE   B  1  20   ? 17.755  8.585   80.822  1.00 19.70 ? 18   PHE   B CA    1 
ATOM   9092  C  C     . PHE   B  1  20   ? 17.419  7.168   81.260  1.00 24.34 ? 18   PHE   B C     1 
ATOM   9093  O  O     . PHE   B  1  20   ? 16.245  6.862   81.464  1.00 24.30 ? 18   PHE   B O     1 
ATOM   9094  C  CB    . PHE   B  1  20   ? 16.740  9.074   79.787  1.00 20.79 ? 18   PHE   B CB    1 
ATOM   9095  C  CG    . PHE   B  1  20   ? 16.939  10.496  79.391  1.00 18.20 ? 18   PHE   B CG    1 
ATOM   9096  C  CD1   . PHE   B  1  20   ? 16.597  11.523  80.256  1.00 17.86 ? 18   PHE   B CD1   1 
ATOM   9097  C  CD2   . PHE   B  1  20   ? 17.469  10.809  78.153  1.00 20.04 ? 18   PHE   B CD2   1 
ATOM   9098  C  CE1   . PHE   B  1  20   ? 16.768  12.837  79.888  1.00 19.17 ? 18   PHE   B CE1   1 
ATOM   9099  C  CE2   . PHE   B  1  20   ? 17.638  12.124  77.779  1.00 19.92 ? 18   PHE   B CE2   1 
ATOM   9100  C  CZ    . PHE   B  1  20   ? 17.292  13.133  78.643  1.00 18.53 ? 18   PHE   B CZ    1 
ATOM   9101  N  N     . ALA   B  1  21   ? 18.415  6.298   81.415  1.00 25.54 ? 19   ALA   B N     1 
ATOM   9102  C  CA    . ALA   B  1  21   ? 18.137  4.920   81.803  1.00 26.78 ? 19   ALA   B CA    1 
ATOM   9103  C  C     . ALA   B  1  21   ? 17.613  4.812   83.230  1.00 30.05 ? 19   ALA   B C     1 
ATOM   9104  O  O     . ALA   B  1  21   ? 17.002  3.797   83.578  1.00 32.63 ? 19   ALA   B O     1 
ATOM   9105  C  CB    . ALA   B  1  21   ? 19.392  4.063   81.628  1.00 31.18 ? 19   ALA   B CB    1 
ATOM   9106  N  N     . ASP   B  1  22   ? 17.827  5.826   84.059  1.00 22.95 ? 20   ASP   B N     1 
ATOM   9107  C  CA    . ASP   B  1  22   ? 17.282  5.838   85.411  1.00 24.02 ? 20   ASP   B CA    1 
ATOM   9108  C  C     . ASP   B  1  22   ? 16.556  7.144   85.664  1.00 20.51 ? 20   ASP   B C     1 
ATOM   9109  O  O     . ASP   B  1  22   ? 16.671  7.744   86.737  1.00 23.12 ? 20   ASP   B O     1 
ATOM   9110  C  CB    . ASP   B  1  22   ? 18.370  5.594   86.453  1.00 30.05 ? 20   ASP   B CB    1 
ATOM   9111  N  N     . PHE   B  1  23   ? 15.796  7.607   84.670  1.00 18.36 ? 21   PHE   B N     1 
ATOM   9112  C  CA    . PHE   B  1  23   ? 15.234  8.949   84.755  1.00 17.58 ? 21   PHE   B CA    1 
ATOM   9113  C  C     . PHE   B  1  23   ? 14.278  9.086   85.932  1.00 16.68 ? 21   PHE   B C     1 
ATOM   9114  O  O     . PHE   B  1  23   ? 14.427  9.986   86.764  1.00 17.63 ? 21   PHE   B O     1 
ATOM   9115  C  CB    . PHE   B  1  23   ? 14.532  9.325   83.456  1.00 16.80 ? 21   PHE   B CB    1 
ATOM   9116  C  CG    . PHE   B  1  23   ? 13.847  10.642  83.534  1.00 17.89 ? 21   PHE   B CG    1 
ATOM   9117  C  CD1   . PHE   B  1  23   ? 14.584  11.796  83.687  1.00 17.09 ? 21   PHE   B CD1   1 
ATOM   9118  C  CD2   . PHE   B  1  23   ? 12.465  10.730  83.491  1.00 18.07 ? 21   PHE   B CD2   1 
ATOM   9119  C  CE1   . PHE   B  1  23   ? 13.953  13.035  83.787  1.00 16.01 ? 21   PHE   B CE1   1 
ATOM   9120  C  CE2   . PHE   B  1  23   ? 11.840  11.958  83.592  1.00 18.31 ? 21   PHE   B CE2   1 
ATOM   9121  C  CZ    . PHE   B  1  23   ? 12.585  13.104  83.744  1.00 16.86 ? 21   PHE   B CZ    1 
ATOM   9122  N  N     . ALA   B  1  24   ? 13.265  8.232   85.991  1.00 17.97 ? 22   ALA   B N     1 
ATOM   9123  C  CA    . ALA   B  1  24   ? 12.290  8.343   87.069  1.00 18.72 ? 22   ALA   B CA    1 
ATOM   9124  C  C     . ALA   B  1  24   ? 11.562  7.026   87.285  1.00 17.25 ? 22   ALA   B C     1 
ATOM   9125  O  O     . ALA   B  1  24   ? 10.333  6.973   87.160  1.00 19.17 ? 22   ALA   B O     1 
ATOM   9126  C  CB    . ALA   B  1  24   ? 11.277  9.445   86.758  1.00 20.11 ? 22   ALA   B CB    1 
ATOM   9127  N  N     . PRO   B  1  25   ? 12.266  5.952   87.625  1.00 19.04 ? 23   PRO   B N     1 
ATOM   9128  C  CA    . PRO   B  1  25   ? 11.598  4.671   87.819  1.00 22.02 ? 23   PRO   B CA    1 
ATOM   9129  C  C     . PRO   B  1  25   ? 10.626  4.762   88.978  1.00 21.93 ? 23   PRO   B C     1 
ATOM   9130  O  O     . PRO   B  1  25   ? 10.926  5.397   89.997  1.00 21.25 ? 23   PRO   B O     1 
ATOM   9131  C  CB    . PRO   B  1  25   ? 12.758  3.717   88.142  1.00 26.98 ? 23   PRO   B CB    1 
ATOM   9132  C  CG    . PRO   B  1  25   ? 13.816  4.594   88.702  1.00 24.30 ? 23   PRO   B CG    1 
ATOM   9133  C  CD    . PRO   B  1  25   ? 13.697  5.892   87.963  1.00 20.89 ? 23   PRO   B CD    1 
ATOM   9134  N  N     . PRO   B  1  26   ? 9.439   4.180   88.849  1.00 19.99 ? 24   PRO   B N     1 
ATOM   9135  C  CA    . PRO   B  1  26   ? 8.471   4.248   89.946  1.00 20.93 ? 24   PRO   B CA    1 
ATOM   9136  C  C     . PRO   B  1  26   ? 8.940   3.427   91.133  1.00 22.28 ? 24   PRO   B C     1 
ATOM   9137  O  O     . PRO   B  1  26   ? 9.755   2.509   91.008  1.00 22.20 ? 24   PRO   B O     1 
ATOM   9138  C  CB    . PRO   B  1  26   ? 7.200   3.649   89.335  1.00 24.22 ? 24   PRO   B CB    1 
ATOM   9139  C  CG    . PRO   B  1  26   ? 7.694   2.733   88.270  1.00 24.66 ? 24   PRO   B CG    1 
ATOM   9140  C  CD    . PRO   B  1  26   ? 8.945   3.376   87.717  1.00 22.27 ? 24   PRO   B CD    1 
ATOM   9141  N  N     . VAL   B  1  27   ? 8.406   3.783   92.305  1.00 21.72 ? 25   VAL   B N     1 
ATOM   9142  C  CA    . VAL   B  1  27   ? 8.726   3.048   93.525  1.00 20.21 ? 25   VAL   B CA    1 
ATOM   9143  C  C     . VAL   B  1  27   ? 8.376   1.576   93.373  1.00 22.59 ? 25   VAL   B C     1 
ATOM   9144  O  O     . VAL   B  1  27   ? 9.120   0.693   93.821  1.00 24.77 ? 25   VAL   B O     1 
ATOM   9145  C  CB    . VAL   B  1  27   ? 8.019   3.682   94.736  1.00 21.37 ? 25   VAL   B CB    1 
ATOM   9146  C  CG1   . VAL   B  1  27   ? 8.144   2.766   95.953  1.00 24.04 ? 25   VAL   B CG1   1 
ATOM   9147  C  CG2   . VAL   B  1  27   ? 8.604   5.043   95.029  1.00 22.80 ? 25   VAL   B CG2   1 
ATOM   9148  N  N     . ARG   B  1  28   ? 7.258   1.285   92.725  1.00 21.35 ? 26   ARG   B N     1 
ATOM   9149  C  CA    . ARG   B  1  28   ? 6.834   -0.091  92.528  1.00 23.18 ? 26   ARG   B CA    1 
ATOM   9150  C  C     . ARG   B  1  28   ? 6.063   -0.171  91.223  1.00 26.46 ? 26   ARG   B C     1 
ATOM   9151  O  O     . ARG   B  1  28   ? 5.592   0.852   90.712  1.00 22.11 ? 26   ARG   B O     1 
ATOM   9152  C  CB    . ARG   B  1  28   ? 5.958   -0.569  93.696  1.00 25.48 ? 26   ARG   B CB    1 
ATOM   9153  C  CG    . ARG   B  1  28   ? 4.592   0.112   93.755  1.00 25.63 ? 26   ARG   B CG    1 
ATOM   9154  C  CD    . ARG   B  1  28   ? 3.840   -0.230  95.036  1.00 26.76 ? 26   ARG   B CD    1 
ATOM   9155  N  NE    . ARG   B  1  28   ? 4.467   0.365   96.210  1.00 28.74 ? 26   ARG   B NE    1 
ATOM   9156  C  CZ    . ARG   B  1  28   ? 5.232   -0.294  97.070  1.00 32.02 ? 26   ARG   B CZ    1 
ATOM   9157  N  NH1   . ARG   B  1  28   ? 5.476   -1.587  96.930  1.00 32.32 ? 26   ARG   B NH1   1 
ATOM   9158  N  NH2   . ARG   B  1  28   ? 5.764   0.361   98.096  1.00 30.05 ? 26   ARG   B NH2   1 
ATOM   9159  N  N     . PRO   B  1  29   ? 5.940   -1.362  90.639  1.00 23.91 ? 27   PRO   B N     1 
ATOM   9160  C  CA    . PRO   B  1  29   ? 5.060   -1.505  89.478  1.00 24.66 ? 27   PRO   B CA    1 
ATOM   9161  C  C     . PRO   B  1  29   ? 3.649   -1.088  89.857  1.00 24.16 ? 27   PRO   B C     1 
ATOM   9162  O  O     . PRO   B  1  29   ? 3.153   -1.406  90.939  1.00 25.41 ? 27   PRO   B O     1 
ATOM   9163  C  CB    . PRO   B  1  29   ? 5.141   -3.002  89.151  1.00 25.56 ? 27   PRO   B CB    1 
ATOM   9164  C  CG    . PRO   B  1  29   ? 6.459   -3.434  89.726  1.00 29.98 ? 27   PRO   B CG    1 
ATOM   9165  C  CD    . PRO   B  1  29   ? 6.608   -2.630  90.983  1.00 25.43 ? 27   PRO   B CD    1 
ATOM   9166  N  N     . GLN   B  1  30   ? 3.015   -0.336  88.965  1.00 23.91 ? 28   GLN   B N     1 
ATOM   9167  C  CA    . GLN   B  1  30   ? 1.701   0.224   89.250  1.00 24.00 ? 28   GLN   B CA    1 
ATOM   9168  C  C     . GLN   B  1  30   ? 0.630   -0.832  89.012  1.00 21.99 ? 28   GLN   B C     1 
ATOM   9169  O  O     . GLN   B  1  30   ? 0.459   -1.311  87.884  1.00 24.39 ? 28   GLN   B O     1 
ATOM   9170  C  CB    . GLN   B  1  30   ? 1.463   1.442   88.364  1.00 21.51 ? 28   GLN   B CB    1 
ATOM   9171  C  CG    . GLN   B  1  30   ? 2.555   2.499   88.505  1.00 21.58 ? 28   GLN   B CG    1 
ATOM   9172  C  CD    . GLN   B  1  30   ? 2.552   3.146   89.875  1.00 21.87 ? 28   GLN   B CD    1 
ATOM   9173  O  OE1   . GLN   B  1  30   ? 1.681   3.957   90.185  1.00 22.10 ? 28   GLN   B OE1   1 
ATOM   9174  N  NE2   . GLN   B  1  30   ? 3.524   2.791   90.704  1.00 20.96 ? 28   GLN   B NE2   1 
ATOM   9175  N  N     . SER   B  1  31   ? -0.096  -1.179  90.070  1.00 23.53 ? 29   SER   B N     1 
ATOM   9176  C  CA    . SER   B  1  31   ? -1.196  -2.122  89.981  1.00 23.27 ? 29   SER   B CA    1 
ATOM   9177  C  C     . SER   B  1  31   ? -2.349  -1.509  89.194  1.00 22.95 ? 29   SER   B C     1 
ATOM   9178  O  O     . SER   B  1  31   ? -2.368  -0.317  88.881  1.00 22.17 ? 29   SER   B O     1 
ATOM   9179  C  CB    . SER   B  1  31   ? -1.710  -2.454  91.377  1.00 24.53 ? 29   SER   B CB    1 
ATOM   9180  O  OG    . SER   B  1  31   ? -2.289  -1.304  91.973  1.00 23.97 ? 29   SER   B OG    1 
ATOM   9181  N  N     . THR   B  1  32   ? -3.328  -2.354  88.877  1.00 26.25 ? 30   THR   B N     1 
ATOM   9182  C  CA    . THR   B  1  32   ? -4.543  -1.867  88.237  1.00 23.51 ? 30   THR   B CA    1 
ATOM   9183  C  C     . THR   B  1  32   ? -5.197  -0.769  89.068  1.00 22.06 ? 30   THR   B C     1 
ATOM   9184  O  O     . THR   B  1  32   ? -5.613  0.264   88.532  1.00 22.54 ? 30   THR   B O     1 
ATOM   9185  C  CB    . THR   B  1  32   ? -5.495  -3.042  88.032  1.00 25.05 ? 30   THR   B CB    1 
ATOM   9186  O  OG1   . THR   B  1  32   ? -4.884  -3.979  87.138  1.00 31.75 ? 30   THR   B OG1   1 
ATOM   9187  C  CG2   . THR   B  1  32   ? -6.829  -2.573  87.455  1.00 28.87 ? 30   THR   B CG2   1 
ATOM   9188  N  N     . LEU   B  1  33   ? -5.269  -0.958  90.385  1.00 23.82 ? 31   LEU   B N     1 
ATOM   9189  C  CA    . LEU   B  1  33   ? -5.897  0.053   91.228  1.00 23.42 ? 31   LEU   B CA    1 
ATOM   9190  C  C     . LEU   B  1  33   ? -5.069  1.325   91.280  1.00 21.00 ? 31   LEU   B C     1 
ATOM   9191  O  O     . LEU   B  1  33   ? -5.624  2.429   91.280  1.00 20.84 ? 31   LEU   B O     1 
ATOM   9192  C  CB    . LEU   B  1  33   ? -6.144  -0.497  92.631  1.00 21.53 ? 31   LEU   B CB    1 
ATOM   9193  C  CG    . LEU   B  1  33   ? -7.237  -1.558  92.630  1.00 21.98 ? 31   LEU   B CG    1 
ATOM   9194  C  CD1   . LEU   B  1  33   ? -7.347  -2.194  93.986  1.00 26.14 ? 31   LEU   B CD1   1 
ATOM   9195  C  CD2   . LEU   B  1  33   ? -8.564  -0.952  92.210  1.00 27.70 ? 31   LEU   B CD2   1 
ATOM   9196  N  N     . ARG   B  1  34   ? -3.741  1.199   91.333  1.00 19.86 ? 32   ARG   B N     1 
ATOM   9197  C  CA    . ARG   B  1  34   ? -2.918  2.401   91.318  1.00 21.25 ? 32   ARG   B CA    1 
ATOM   9198  C  C     . ARG   B  1  34   ? -3.052  3.123   89.988  1.00 18.54 ? 32   ARG   B C     1 
ATOM   9199  O  O     . ARG   B  1  34   ? -3.118  4.356   89.947  1.00 19.22 ? 32   ARG   B O     1 
ATOM   9200  C  CB    . ARG   B  1  34   ? -1.455  2.070   91.613  1.00 19.46 ? 32   ARG   B CB    1 
ATOM   9201  C  CG    . ARG   B  1  34   ? -1.168  1.651   93.052  1.00 20.99 ? 32   ARG   B CG    1 
ATOM   9202  C  CD    . ARG   B  1  34   ? -1.236  2.818   94.020  1.00 19.51 ? 32   ARG   B CD    1 
ATOM   9203  N  NE    . ARG   B  1  34   ? -0.209  3.814   93.752  1.00 20.99 ? 32   ARG   B NE    1 
ATOM   9204  C  CZ    . ARG   B  1  34   ? 1.007   3.799   94.281  1.00 21.38 ? 32   ARG   B CZ    1 
ATOM   9205  N  NH1   . ARG   B  1  34   ? 1.379   2.854   95.137  1.00 22.45 ? 32   ARG   B NH1   1 
ATOM   9206  N  NH2   . ARG   B  1  34   ? 1.871   4.750   93.942  1.00 22.20 ? 32   ARG   B NH2   1 
ATOM   9207  N  N     . ARG   B  1  35   ? -3.120  2.368   88.891  1.00 20.17 ? 33   ARG   B N     1 
ATOM   9208  C  CA    . ARG   B  1  35   ? -3.252  2.998   87.581  1.00 20.42 ? 33   ARG   B CA    1 
ATOM   9209  C  C     . ARG   B  1  35   ? -4.581  3.722   87.447  1.00 19.82 ? 33   ARG   B C     1 
ATOM   9210  O  O     . ARG   B  1  35   ? -4.659  4.765   86.789  1.00 19.89 ? 33   ARG   B O     1 
ATOM   9211  C  CB    . ARG   B  1  35   ? -3.119  1.946   86.482  1.00 21.97 ? 33   ARG   B CB    1 
ATOM   9212  C  CG    . ARG   B  1  35   ? -1.700  1.477   86.307  1.00 25.59 ? 33   ARG   B CG    1 
ATOM   9213  C  CD    . ARG   B  1  35   ? -1.605  0.390   85.249  1.00 31.33 ? 33   ARG   B CD    1 
ATOM   9214  N  NE    . ARG   B  1  35   ? -0.239  -0.110  85.174  1.00 35.77 ? 33   ARG   B NE    1 
ATOM   9215  C  CZ    . ARG   B  1  35   ? 0.749   0.508   84.542  1.00 44.00 ? 33   ARG   B CZ    1 
ATOM   9216  N  NH1   . ARG   B  1  35   ? 0.542   1.625   83.860  1.00 46.95 ? 33   ARG   B NH1   1 
ATOM   9217  N  NH2   . ARG   B  1  35   ? 1.977   -0.001  84.601  1.00 39.73 ? 33   ARG   B NH2   1 
ATOM   9218  N  N     . ALA   B  1  36   ? -5.639  3.181   88.053  1.00 19.95 ? 34   ALA   B N     1 
ATOM   9219  C  CA    . ALA   B  1  36   ? -6.928  3.856   87.988  1.00 22.16 ? 34   ALA   B CA    1 
ATOM   9220  C  C     . ALA   B  1  36   ? -6.891  5.174   88.741  1.00 21.46 ? 34   ALA   B C     1 
ATOM   9221  O  O     . ALA   B  1  36   ? -7.556  6.134   88.345  1.00 20.78 ? 34   ALA   B O     1 
ATOM   9222  C  CB    . ALA   B  1  36   ? -8.042  2.952   88.518  1.00 20.16 ? 34   ALA   B CB    1 
ATOM   9223  N  N     . ILE   B  1  37   ? -6.109  5.245   89.819  1.00 18.37 ? 35   ILE   B N     1 
ATOM   9224  C  CA    . ILE   B  1  37   ? -5.901  6.519   90.498  1.00 18.66 ? 35   ILE   B CA    1 
ATOM   9225  C  C     . ILE   B  1  37   ? -5.236  7.505   89.557  1.00 20.50 ? 35   ILE   B C     1 
ATOM   9226  O  O     . ILE   B  1  37   ? -5.731  8.615   89.334  1.00 17.30 ? 35   ILE   B O     1 
ATOM   9227  C  CB    . ILE   B  1  37   ? -5.064  6.308   91.768  1.00 18.27 ? 35   ILE   B CB    1 
ATOM   9228  C  CG1   . ILE   B  1  37   ? -5.849  5.472   92.766  1.00 18.10 ? 35   ILE   B CG1   1 
ATOM   9229  C  CG2   . ILE   B  1  37   ? -4.632  7.651   92.362  1.00 18.87 ? 35   ILE   B CG2   1 
ATOM   9230  C  CD1   . ILE   B  1  37   ? -4.951  4.914   93.878  1.00 18.88 ? 35   ILE   B CD1   1 
ATOM   9231  N  N     . THR   B  1  38   ? -4.097  7.110   88.987  1.00 17.82 ? 36   THR   B N     1 
ATOM   9232  C  CA    . THR   B  1  38   ? -3.352  8.027   88.140  1.00 18.49 ? 36   THR   B CA    1 
ATOM   9233  C  C     . THR   B  1  38   ? -4.190  8.492   86.961  1.00 19.12 ? 36   THR   B C     1 
ATOM   9234  O  O     . THR   B  1  38   ? -4.122  9.659   86.563  1.00 17.91 ? 36   THR   B O     1 
ATOM   9235  C  CB    . THR   B  1  38   ? -2.073  7.347   87.665  1.00 18.68 ? 36   THR   B CB    1 
ATOM   9236  O  OG1   . THR   B  1  38   ? -1.392  6.812   88.810  1.00 18.45 ? 36   THR   B OG1   1 
ATOM   9237  C  CG2   . THR   B  1  38   ? -1.165  8.340   86.953  1.00 20.95 ? 36   THR   B CG2   1 
ATOM   9238  N  N     . ALA   B  1  39   ? -5.001  7.595   86.408  1.00 19.46 ? 37   ALA   B N     1 
ATOM   9239  C  CA    . ALA   B  1  39   ? -5.803  7.947   85.243  1.00 20.59 ? 37   ALA   B CA    1 
ATOM   9240  C  C     . ALA   B  1  39   ? -6.786  9.065   85.554  1.00 20.69 ? 37   ALA   B C     1 
ATOM   9241  O  O     . ALA   B  1  39   ? -7.181  9.808   84.650  1.00 20.53 ? 37   ALA   B O     1 
ATOM   9242  C  CB    . ALA   B  1  39   ? -6.539  6.710   84.727  1.00 20.28 ? 37   ALA   B CB    1 
ATOM   9243  N  N     . ALA   B  1  40   ? -7.178  9.212   86.816  1.00 18.13 ? 38   ALA   B N     1 
ATOM   9244  C  CA    . ALA   B  1  40   ? -8.169  10.202  87.209  1.00 20.56 ? 38   ALA   B CA    1 
ATOM   9245  C  C     . ALA   B  1  40   ? -7.556  11.537  87.591  1.00 17.15 ? 38   ALA   B C     1 
ATOM   9246  O  O     . ALA   B  1  40   ? -8.301  12.485  87.861  1.00 19.35 ? 38   ALA   B O     1 
ATOM   9247  C  CB    . ALA   B  1  40   ? -8.987  9.682   88.394  1.00 21.15 ? 38   ALA   B CB    1 
ATOM   9248  N  N     . TYR   B  1  41   ? -6.223  11.631  87.603  1.00 16.88 ? 39   TYR   B N     1 
ATOM   9249  C  CA    . TYR   B  1  41   ? -5.535  12.755  88.229  1.00 17.00 ? 39   TYR   B CA    1 
ATOM   9250  C  C     . TYR   B  1  41   ? -6.126  14.091  87.787  1.00 17.26 ? 39   TYR   B C     1 
ATOM   9251  O  O     . TYR   B  1  41   ? -6.469  14.939  88.622  1.00 17.60 ? 39   TYR   B O     1 
ATOM   9252  C  CB    . TYR   B  1  41   ? -4.057  12.654  87.854  1.00 16.57 ? 39   TYR   B CB    1 
ATOM   9253  C  CG    . TYR   B  1  41   ? -3.058  13.351  88.744  1.00 16.22 ? 39   TYR   B CG    1 
ATOM   9254  C  CD1   . TYR   B  1  41   ? -3.376  14.493  89.472  1.00 16.27 ? 39   TYR   B CD1   1 
ATOM   9255  C  CD2   . TYR   B  1  41   ? -1.756  12.879  88.815  1.00 17.89 ? 39   TYR   B CD2   1 
ATOM   9256  C  CE1   . TYR   B  1  41   ? -2.421  15.130  90.255  1.00 15.65 ? 39   TYR   B CE1   1 
ATOM   9257  C  CE2   . TYR   B  1  41   ? -0.807  13.500  89.597  1.00 17.16 ? 39   TYR   B CE2   1 
ATOM   9258  C  CZ    . TYR   B  1  41   ? -1.141  14.627  90.304  1.00 16.03 ? 39   TYR   B CZ    1 
ATOM   9259  O  OH    . TYR   B  1  41   ? -0.193  15.245  91.072  1.00 16.58 ? 39   TYR   B OH    1 
ATOM   9260  N  N     . ARG   B  1  42   ? -6.265  14.294  86.477  1.00 17.96 ? 40   ARG   B N     1 
ATOM   9261  C  CA    . ARG   B  1  42   ? -6.757  15.558  85.948  1.00 17.44 ? 40   ARG   B CA    1 
ATOM   9262  C  C     . ARG   B  1  42   ? -7.956  15.341  85.043  1.00 18.32 ? 40   ARG   B C     1 
ATOM   9263  O  O     . ARG   B  1  42   ? -8.154  16.059  84.065  1.00 19.42 ? 40   ARG   B O     1 
ATOM   9264  C  CB    . ARG   B  1  42   ? -5.643  16.355  85.274  1.00 19.37 ? 40   ARG   B CB    1 
ATOM   9265  C  CG    . ARG   B  1  42   ? -4.559  16.692  86.273  1.00 18.70 ? 40   ARG   B CG    1 
ATOM   9266  C  CD    . ARG   B  1  42   ? -3.373  17.385  85.679  1.00 17.51 ? 40   ARG   B CD    1 
ATOM   9267  N  NE    . ARG   B  1  42   ? -2.290  17.321  86.645  1.00 16.91 ? 40   ARG   B NE    1 
ATOM   9268  C  CZ    . ARG   B  1  42   ? -2.091  18.195  87.625  1.00 17.35 ? 40   ARG   B CZ    1 
ATOM   9269  N  NH1   . ARG   B  1  42   ? -2.834  19.286  87.746  1.00 18.19 ? 40   ARG   B NH1   1 
ATOM   9270  N  NH2   . ARG   B  1  42   ? -1.115  17.974  88.499  1.00 17.02 ? 40   ARG   B NH2   1 
ATOM   9271  N  N     . ARG   B  1  43   ? -8.779  14.359  85.388  1.00 17.36 ? 41   ARG   B N     1 
ATOM   9272  C  CA    . ARG   B  1  43   ? -9.927  14.021  84.565  1.00 19.57 ? 41   ARG   B CA    1 
ATOM   9273  C  C     . ARG   B  1  43   ? -10.863 15.223  84.465  1.00 20.80 ? 41   ARG   B C     1 
ATOM   9274  O  O     . ARG   B  1  43   ? -11.062 15.943  85.451  1.00 18.70 ? 41   ARG   B O     1 
ATOM   9275  C  CB    . ARG   B  1  43   ? -10.663 12.840  85.195  1.00 17.83 ? 41   ARG   B CB    1 
ATOM   9276  C  CG    . ARG   B  1  43   ? -11.918 12.398  84.457  1.00 17.45 ? 41   ARG   B CG    1 
ATOM   9277  C  CD    . ARG   B  1  43   ? -12.332 11.032  84.953  1.00 20.10 ? 41   ARG   B CD    1 
ATOM   9278  N  NE    . ARG   B  1  43   ? -11.340 10.037  84.566  1.00 21.91 ? 41   ARG   B NE    1 
ATOM   9279  C  CZ    . ARG   B  1  43   ? -11.086 8.924   85.242  1.00 23.67 ? 41   ARG   B CZ    1 
ATOM   9280  N  NH1   . ARG   B  1  43   ? -11.737 8.626   86.353  1.00 21.82 ? 41   ARG   B NH1   1 
ATOM   9281  N  NH2   . ARG   B  1  43   ? -10.151 8.092   84.793  1.00 22.74 ? 41   ARG   B NH2   1 
ATOM   9282  N  N     . PRO   B  1  44   ? -11.421 15.498  83.292  1.00 19.31 ? 42   PRO   B N     1 
ATOM   9283  C  CA    . PRO   B  1  44   ? -12.342 16.630  83.169  1.00 19.12 ? 42   PRO   B CA    1 
ATOM   9284  C  C     . PRO   B  1  44   ? -13.454 16.548  84.200  1.00 19.16 ? 42   PRO   B C     1 
ATOM   9285  O  O     . PRO   B  1  44   ? -13.958 15.472  84.533  1.00 18.93 ? 42   PRO   B O     1 
ATOM   9286  C  CB    . PRO   B  1  44   ? -12.878 16.490  81.743  1.00 22.35 ? 42   PRO   B CB    1 
ATOM   9287  C  CG    . PRO   B  1  44   ? -11.708 15.880  81.009  1.00 23.72 ? 42   PRO   B CG    1 
ATOM   9288  C  CD    . PRO   B  1  44   ? -11.122 14.888  81.984  1.00 21.35 ? 42   PRO   B CD    1 
ATOM   9289  N  N     . GLU   B  1  45   ? -13.812 17.716  84.723  1.00 20.29 ? 43   GLU   B N     1 
ATOM   9290  C  CA    . GLU   B  1  45   ? -14.813 17.796  85.771  1.00 19.78 ? 43   GLU   B CA    1 
ATOM   9291  C  C     . GLU   B  1  45   ? -16.145 17.206  85.320  1.00 20.77 ? 43   GLU   B C     1 
ATOM   9292  O  O     . GLU   B  1  45   ? -16.834 16.540  86.099  1.00 22.48 ? 43   GLU   B O     1 
ATOM   9293  C  CB    . GLU   B  1  45   ? -14.936 19.258  86.191  1.00 24.53 ? 43   GLU   B CB    1 
ATOM   9294  C  CG    . GLU   B  1  45   ? -15.389 19.419  87.602  1.00 25.80 ? 43   GLU   B CG    1 
ATOM   9295  C  CD    . GLU   B  1  45   ? -14.839 20.664  88.256  1.00 18.84 ? 43   GLU   B CD    1 
ATOM   9296  O  OE1   . GLU   B  1  45   ? -14.022 21.389  87.649  1.00 18.27 ? 43   GLU   B OE1   1 
ATOM   9297  O  OE2   . GLU   B  1  45   ? -15.277 20.909  89.386  1.00 19.43 ? 43   GLU   B OE2   1 
ATOM   9298  N  N     . THR   B  1  46   ? -16.504 17.397  84.048  1.00 21.77 ? 44   THR   B N     1 
ATOM   9299  C  CA    . THR   B  1  46   ? -17.748 16.834  83.539  1.00 21.19 ? 44   THR   B CA    1 
ATOM   9300  C  C     . THR   B  1  46   ? -17.715 15.316  83.470  1.00 20.11 ? 44   THR   B C     1 
ATOM   9301  O  O     . THR   B  1  46   ? -18.776 14.689  83.443  1.00 23.76 ? 44   THR   B O     1 
ATOM   9302  C  CB    . THR   B  1  46   ? -18.041 17.387  82.148  1.00 22.89 ? 44   THR   B CB    1 
ATOM   9303  O  OG1   . THR   B  1  46   ? -16.874 17.220  81.331  1.00 23.14 ? 44   THR   B OG1   1 
ATOM   9304  C  CG2   . THR   B  1  46   ? -18.394 18.866  82.230  1.00 23.79 ? 44   THR   B CG2   1 
ATOM   9305  N  N     . GLU   B  1  47   ? -16.528 14.714  83.407  1.00 21.22 ? 45   GLU   B N     1 
ATOM   9306  C  CA    . GLU   B  1  47   ? -16.443 13.261  83.462  1.00 21.19 ? 45   GLU   B CA    1 
ATOM   9307  C  C     . GLU   B  1  47   ? -16.447 12.751  84.896  1.00 21.08 ? 45   GLU   B C     1 
ATOM   9308  O  O     . GLU   B  1  47   ? -16.924 11.641  85.159  1.00 24.42 ? 45   GLU   B O     1 
ATOM   9309  C  CB    . GLU   B  1  47   ? -15.184 12.781  82.739  1.00 22.05 ? 45   GLU   B CB    1 
ATOM   9310  C  CG    . GLU   B  1  47   ? -15.164 13.090  81.255  1.00 28.57 ? 45   GLU   B CG    1 
ATOM   9311  C  CD    . GLU   B  1  47   ? -13.869 12.655  80.615  1.00 31.70 ? 45   GLU   B CD    1 
ATOM   9312  O  OE1   . GLU   B  1  47   ? -13.264 11.683  81.116  1.00 34.72 ? 45   GLU   B OE1   1 
ATOM   9313  O  OE2   . GLU   B  1  47   ? -13.453 13.289  79.626  1.00 37.10 ? 45   GLU   B OE2   1 
ATOM   9314  N  N     . CYS   B  1  48   ? -15.933 13.550  85.834  1.00 18.77 ? 46   CYS   B N     1 
ATOM   9315  C  CA    . CYS   B  1  48   ? -15.859 13.103  87.222  1.00 20.43 ? 46   CYS   B CA    1 
ATOM   9316  C  C     . CYS   B  1  48   ? -17.229 13.072  87.875  1.00 20.18 ? 46   CYS   B C     1 
ATOM   9317  O  O     . CYS   B  1  48   ? -17.525 12.172  88.667  1.00 20.93 ? 46   CYS   B O     1 
ATOM   9318  C  CB    . CYS   B  1  48   ? -14.953 14.026  88.032  1.00 19.83 ? 46   CYS   B CB    1 
ATOM   9319  S  SG    . CYS   B  1  48   ? -13.241 13.985  87.566  1.00 19.94 ? 46   CYS   B SG    1 
ATOM   9320  N  N     . LEU   B  1  49   ? -18.047 14.061  87.598  1.00 20.85 ? 47   LEU   B N     1 
ATOM   9321  C  CA    . LEU   B  1  49   ? -19.239 14.262  88.416  1.00 21.35 ? 47   LEU   B CA    1 
ATOM   9322  C  C     . LEU   B  1  49   ? -20.345 13.224  88.268  1.00 23.31 ? 47   LEU   B C     1 
ATOM   9323  O  O     . LEU   B  1  49   ? -20.937 12.837  89.280  1.00 22.31 ? 47   LEU   B O     1 
ATOM   9324  C  CB    . LEU   B  1  49   ? -19.787 15.688  88.295  1.00 22.33 ? 47   LEU   B CB    1 
ATOM   9325  C  CG    . LEU   B  1  49   ? -19.287 16.630  89.404  1.00 20.77 ? 47   LEU   B CG    1 
ATOM   9326  C  CD1   . LEU   B  1  49   ? -19.821 16.194  90.761  1.00 22.67 ? 47   LEU   B CD1   1 
ATOM   9327  C  CD2   . LEU   B  1  49   ? -17.768 16.680  89.427  1.00 20.98 ? 47   LEU   B CD2   1 
ATOM   9328  N  N     . PRO   B  1  50   ? -20.688 12.762  87.066  1.00 23.55 ? 48   PRO   B N     1 
ATOM   9329  C  CA    . PRO   B  1  50   ? -21.847 11.859  86.942  1.00 25.66 ? 48   PRO   B CA    1 
ATOM   9330  C  C     . PRO   B  1  50   ? -21.719 10.615  87.809  1.00 25.82 ? 48   PRO   B C     1 
ATOM   9331  O  O     . PRO   B  1  50   ? -22.672 10.277  88.524  1.00 25.81 ? 48   PRO   B O     1 
ATOM   9332  C  CB    . PRO   B  1  50   ? -21.896 11.535  85.439  1.00 23.57 ? 48   PRO   B CB    1 
ATOM   9333  C  CG    . PRO   B  1  50   ? -21.363 12.775  84.817  1.00 22.10 ? 48   PRO   B CG    1 
ATOM   9334  C  CD    . PRO   B  1  50   ? -20.259 13.261  85.746  1.00 21.51 ? 48   PRO   B CD    1 
ATOM   9335  N  N     . PRO   B  1  51   ? -20.573 9.917   87.830  1.00 25.30 ? 49   PRO   B N     1 
ATOM   9336  C  CA    . PRO   B  1  51   ? -20.502 8.752   88.728  1.00 25.34 ? 49   PRO   B CA    1 
ATOM   9337  C  C     . PRO   B  1  51   ? -20.591 9.114   90.202  1.00 23.22 ? 49   PRO   B C     1 
ATOM   9338  O  O     . PRO   B  1  51   ? -21.131 8.327   90.988  1.00 25.64 ? 49   PRO   B O     1 
ATOM   9339  C  CB    . PRO   B  1  51   ? -19.172 8.081   88.366  1.00 27.72 ? 49   PRO   B CB    1 
ATOM   9340  C  CG    . PRO   B  1  51   ? -18.373 9.142   87.715  1.00 28.94 ? 49   PRO   B CG    1 
ATOM   9341  C  CD    . PRO   B  1  51   ? -19.361 10.010  86.993  1.00 23.80 ? 49   PRO   B CD    1 
ATOM   9342  N  N     . LEU   B  1  52   ? -20.101 10.292  90.597  1.00 23.85 ? 50   LEU   B N     1 
ATOM   9343  C  CA    . LEU   B  1  52   ? -20.240 10.722  91.986  1.00 21.80 ? 50   LEU   B CA    1 
ATOM   9344  C  C     . LEU   B  1  52   ? -21.692 11.036  92.319  1.00 24.11 ? 50   LEU   B C     1 
ATOM   9345  O  O     . LEU   B  1  52   ? -22.186 10.663  93.389  1.00 23.95 ? 50   LEU   B O     1 
ATOM   9346  C  CB    . LEU   B  1  52   ? -19.362 11.945  92.246  1.00 22.33 ? 50   LEU   B CB    1 
ATOM   9347  C  CG    . LEU   B  1  52   ? -17.864 11.761  92.013  1.00 20.62 ? 50   LEU   B CG    1 
ATOM   9348  C  CD1   . LEU   B  1  52   ? -17.165 13.101  92.089  1.00 21.21 ? 50   LEU   B CD1   1 
ATOM   9349  C  CD2   . LEU   B  1  52   ? -17.302 10.788  93.025  1.00 22.95 ? 50   LEU   B CD2   1 
ATOM   9350  N  N     . VAL   B  1  53   ? -22.386 11.736  91.418  1.00 23.97 ? 51   VAL   B N     1 
ATOM   9351  C  CA    . VAL   B  1  53   ? -23.810 12.000  91.621  1.00 24.41 ? 51   VAL   B CA    1 
ATOM   9352  C  C     . VAL   B  1  53   ? -24.561 10.696  91.845  1.00 29.13 ? 51   VAL   B C     1 
ATOM   9353  O  O     . VAL   B  1  53   ? -25.371 10.574  92.770  1.00 25.85 ? 51   VAL   B O     1 
ATOM   9354  C  CB    . VAL   B  1  53   ? -24.387 12.789  90.432  1.00 24.44 ? 51   VAL   B CB    1 
ATOM   9355  C  CG1   . VAL   B  1  53   ? -25.914 12.763  90.464  1.00 27.69 ? 51   VAL   B CG1   1 
ATOM   9356  C  CG2   . VAL   B  1  53   ? -23.898 14.206  90.453  1.00 25.77 ? 51   VAL   B CG2   1 
ATOM   9357  N  N     . GLU   B  1  54   ? -24.286 9.693   91.008  1.00 26.97 ? 52   GLU   B N     1 
ATOM   9358  C  CA    . GLU   B  1  54   ? -24.963 8.408   91.152  1.00 27.48 ? 52   GLU   B CA    1 
ATOM   9359  C  C     . GLU   B  1  54   ? -24.638 7.764   92.493  1.00 27.26 ? 52   GLU   B C     1 
ATOM   9360  O  O     . GLU   B  1  54   ? -25.532 7.285   93.199  1.00 27.94 ? 52   GLU   B O     1 
ATOM   9361  C  CB    . GLU   B  1  54   ? -24.585 7.483   89.993  1.00 31.37 ? 52   GLU   B CB    1 
ATOM   9362  N  N     . ALA   B  1  55   ? -23.357 7.761   92.874  1.00 26.36 ? 53   ALA   B N     1 
ATOM   9363  C  CA    . ALA   B  1  55   ? -22.972 7.150   94.142  1.00 30.73 ? 53   ALA   B CA    1 
ATOM   9364  C  C     . ALA   B  1  55   ? -23.538 7.908   95.338  1.00 27.23 ? 53   ALA   B C     1 
ATOM   9365  O  O     . ALA   B  1  55   ? -23.809 7.300   96.379  1.00 30.43 ? 53   ALA   B O     1 
ATOM   9366  C  CB    . ALA   B  1  55   ? -21.450 7.059   94.239  1.00 29.36 ? 53   ALA   B CB    1 
ATOM   9367  N  N     . ALA   B  1  56   ? -23.716 9.222   95.215  1.00 26.45 ? 54   ALA   B N     1 
ATOM   9368  C  CA    . ALA   B  1  56   ? -24.205 10.049  96.311  1.00 28.75 ? 54   ALA   B CA    1 
ATOM   9369  C  C     . ALA   B  1  56   ? -25.723 10.080  96.417  1.00 28.00 ? 54   ALA   B C     1 
ATOM   9370  O  O     . ALA   B  1  56   ? -26.249 10.665  97.371  1.00 31.88 ? 54   ALA   B O     1 
ATOM   9371  C  CB    . ALA   B  1  56   ? -23.684 11.479  96.170  1.00 29.03 ? 54   ALA   B CB    1 
ATOM   9372  N  N     . THR   B  1  57   ? -26.439 9.474   95.469  1.00 28.07 ? 55   THR   B N     1 
ATOM   9373  C  CA    . THR   B  1  57   ? -27.894 9.570   95.451  1.00 33.95 ? 55   THR   B CA    1 
ATOM   9374  C  C     . THR   B  1  57   ? -28.503 8.834   96.638  1.00 32.81 ? 55   THR   B C     1 
ATOM   9375  O  O     . THR   B  1  57   ? -28.070 7.737   97.001  1.00 33.92 ? 55   THR   B O     1 
ATOM   9376  C  CB    . THR   B  1  57   ? -28.434 8.996   94.141  1.00 34.40 ? 55   THR   B CB    1 
ATOM   9377  O  OG1   . THR   B  1  57   ? -28.039 9.842   93.058  1.00 33.75 ? 55   THR   B OG1   1 
ATOM   9378  C  CG2   . THR   B  1  57   ? -29.957 8.914   94.173  1.00 32.27 ? 55   THR   B CG2   1 
ATOM   9379  N  N     . GLN   B  1  58   ? -29.504 9.460   97.257  1.00 35.27 ? 56   GLN   B N     1 
ATOM   9380  C  CA    . GLN   B  1  58   ? -30.240 8.867   98.361  1.00 34.18 ? 56   GLN   B CA    1 
ATOM   9381  C  C     . GLN   B  1  58   ? -31.735 9.009   98.100  1.00 37.86 ? 56   GLN   B C     1 
ATOM   9382  O  O     . GLN   B  1  58   ? -32.175 9.875   97.339  1.00 34.22 ? 56   GLN   B O     1 
ATOM   9383  C  CB    . GLN   B  1  58   ? -29.867 9.516   99.702  1.00 36.73 ? 56   GLN   B CB    1 
ATOM   9384  C  CG    . GLN   B  1  58   ? -28.364 9.588   99.959  1.00 33.83 ? 56   GLN   B CG    1 
ATOM   9385  C  CD    . GLN   B  1  58   ? -28.032 9.643   101.431 1.00 38.99 ? 56   GLN   B CD    1 
ATOM   9386  O  OE1   . GLN   B  1  58   ? -28.254 8.677   102.160 1.00 42.09 ? 56   GLN   B OE1   1 
ATOM   9387  N  NE2   . GLN   B  1  58   ? -27.503 10.774  101.881 1.00 39.67 ? 56   GLN   B NE2   1 
ATOM   9388  N  N     . SER   B  1  59   ? -32.509 8.142   98.750  1.00 40.20 ? 57   SER   B N     1 
ATOM   9389  C  CA    . SER   B  1  59   ? -33.956 8.134   98.589  1.00 37.74 ? 57   SER   B CA    1 
ATOM   9390  C  C     . SER   B  1  59   ? -34.558 9.447   99.077  1.00 40.29 ? 57   SER   B C     1 
ATOM   9391  O  O     . SER   B  1  59   ? -33.959 10.181  99.866  1.00 36.55 ? 57   SER   B O     1 
ATOM   9392  C  CB    . SER   B  1  59   ? -34.558 7.010   99.426  1.00 39.73 ? 57   SER   B CB    1 
ATOM   9393  O  OG    . SER   B  1  59   ? -34.328 7.246   100.807 1.00 42.56 ? 57   SER   B OG    1 
ATOM   9394  N  N     . LYS   B  1  60   ? -35.774 9.735   98.606  1.00 39.65 ? 58   LYS   B N     1 
ATOM   9395  C  CA    . LYS   B  1  60   ? -36.488 10.913  99.091  1.00 39.82 ? 58   LYS   B CA    1 
ATOM   9396  C  C     . LYS   B  1  60   ? -36.645 10.870  100.605 1.00 39.89 ? 58   LYS   B C     1 
ATOM   9397  O  O     . LYS   B  1  60   ? -36.545 11.903  101.276 1.00 41.19 ? 58   LYS   B O     1 
ATOM   9398  C  CB    . LYS   B  1  60   ? -37.858 11.019  98.416  1.00 37.22 ? 58   LYS   B CB    1 
ATOM   9399  N  N     . GLU   B  1  61   ? -36.878 9.677   101.160 1.00 39.62 ? 59   GLU   B N     1 
ATOM   9400  C  CA    . GLU   B  1  61   ? -37.056 9.543   102.603 1.00 40.82 ? 59   GLU   B CA    1 
ATOM   9401  C  C     . GLU   B  1  61   ? -35.792 9.949   103.350 1.00 40.99 ? 59   GLU   B C     1 
ATOM   9402  O  O     . GLU   B  1  61   ? -35.840 10.756  104.285 1.00 38.86 ? 59   GLU   B O     1 
ATOM   9403  C  CB    . GLU   B  1  61   ? -37.446 8.104   102.947 1.00 46.30 ? 59   GLU   B CB    1 
ATOM   9404  N  N     . ILE   B  1  62   ? -34.645 9.397   102.946 1.00 39.77 ? 60   ILE   B N     1 
ATOM   9405  C  CA    . ILE   B  1  62   ? -33.385 9.744   103.597 1.00 36.01 ? 60   ILE   B CA    1 
ATOM   9406  C  C     . ILE   B  1  62   ? -33.067 11.221  103.396 1.00 35.93 ? 60   ILE   B C     1 
ATOM   9407  O  O     . ILE   B  1  62   ? -32.586 11.898  104.314 1.00 40.60 ? 60   ILE   B O     1 
ATOM   9408  C  CB    . ILE   B  1  62   ? -32.253 8.826   103.101 1.00 41.15 ? 60   ILE   B CB    1 
ATOM   9409  N  N     . ARG   B  1  63   ? -33.347 11.749  102.200 1.00 34.82 ? 61   ARG   B N     1 
ATOM   9410  C  CA    . ARG   B  1  63   ? -33.044 13.149  101.918 1.00 36.43 ? 61   ARG   B CA    1 
ATOM   9411  C  C     . ARG   B  1  63   ? -33.892 14.089  102.761 1.00 37.44 ? 61   ARG   B C     1 
ATOM   9412  O  O     . ARG   B  1  63   ? -33.392 15.103  103.260 1.00 38.62 ? 61   ARG   B O     1 
ATOM   9413  C  CB    . ARG   B  1  63   ? -33.211 13.443  100.428 1.00 38.77 ? 61   ARG   B CB    1 
ATOM   9414  C  CG    . ARG   B  1  63   ? -32.154 12.773  99.578  1.00 40.06 ? 61   ARG   B CG    1 
ATOM   9415  C  CD    . ARG   B  1  63   ? -32.207 13.223  98.131  1.00 43.35 ? 61   ARG   B CD    1 
ATOM   9416  N  NE    . ARG   B  1  63   ? -33.299 12.612  97.384  1.00 36.61 ? 61   ARG   B NE    1 
ATOM   9417  C  CZ    . ARG   B  1  63   ? -34.312 13.288  96.861  1.00 42.55 ? 61   ARG   B CZ    1 
ATOM   9418  N  NH1   . ARG   B  1  63   ? -34.427 14.596  97.021  1.00 45.50 ? 61   ARG   B NH1   1 
ATOM   9419  N  NH2   . ARG   B  1  63   ? -35.226 12.637  96.148  1.00 44.40 ? 61   ARG   B NH2   1 
ATOM   9420  N  N     . ASP   B  1  64   ? -35.184 13.787  102.914 1.00 33.74 ? 62   ASP   B N     1 
ATOM   9421  C  CA    . ASP   B  1  64   ? -36.010 14.588  103.808 1.00 36.95 ? 62   ASP   B CA    1 
ATOM   9422  C  C     . ASP   B  1  64   ? -35.523 14.472  105.245 1.00 31.99 ? 62   ASP   B C     1 
ATOM   9423  O  O     . ASP   B  1  64   ? -35.453 15.472  105.967 1.00 37.35 ? 62   ASP   B O     1 
ATOM   9424  C  CB    . ASP   B  1  64   ? -37.472 14.154  103.711 1.00 39.31 ? 62   ASP   B CB    1 
ATOM   9425  C  CG    . ASP   B  1  64   ? -38.071 14.415  102.346 1.00 43.81 ? 62   ASP   B CG    1 
ATOM   9426  O  OD1   . ASP   B  1  64   ? -37.594 15.331  101.643 1.00 41.04 ? 62   ASP   B OD1   1 
ATOM   9427  O  OD2   . ASP   B  1  64   ? -39.036 13.707  101.984 1.00 45.80 ? 62   ASP   B OD2   1 
ATOM   9428  N  N     . ALA   B  1  65   ? -35.197 13.252  105.681 1.00 32.39 ? 63   ALA   B N     1 
ATOM   9429  C  CA    . ALA   B  1  65   ? -34.723 13.054  107.047 1.00 33.26 ? 63   ALA   B CA    1 
ATOM   9430  C  C     . ALA   B  1  65   ? -33.407 13.783  107.288 1.00 39.09 ? 63   ALA   B C     1 
ATOM   9431  O  O     . ALA   B  1  65   ? -33.169 14.306  108.383 1.00 40.37 ? 63   ALA   B O     1 
ATOM   9432  C  CB    . ALA   B  1  65   ? -34.577 11.559  107.339 1.00 34.29 ? 63   ALA   B CB    1 
ATOM   9433  N  N     . ALA   B  1  66   ? -32.543 13.840  106.271 1.00 38.29 ? 64   ALA   B N     1 
ATOM   9434  C  CA    . ALA   B  1  66   ? -31.269 14.534  106.425 1.00 35.69 ? 64   ALA   B CA    1 
ATOM   9435  C  C     . ALA   B  1  66   ? -31.456 16.046  106.411 1.00 35.98 ? 64   ALA   B C     1 
ATOM   9436  O  O     . ALA   B  1  66   ? -30.777 16.768  107.148 1.00 37.41 ? 64   ALA   B O     1 
ATOM   9437  C  CB    . ALA   B  1  66   ? -30.296 14.087  105.337 1.00 32.90 ? 64   ALA   B CB    1 
ATOM   9438  N  N     . ALA   B  1  67   ? -32.386 16.545  105.593 1.00 35.93 ? 65   ALA   B N     1 
ATOM   9439  C  CA    . ALA   B  1  67   ? -32.637 17.982  105.574 1.00 35.28 ? 65   ALA   B CA    1 
ATOM   9440  C  C     . ALA   B  1  67   ? -33.187 18.458  106.915 1.00 41.01 ? 65   ALA   B C     1 
ATOM   9441  O  O     . ALA   B  1  67   ? -32.861 19.562  107.372 1.00 38.21 ? 65   ALA   B O     1 
ATOM   9442  C  CB    . ALA   B  1  67   ? -33.595 18.337  104.437 1.00 39.38 ? 65   ALA   B CB    1 
ATOM   9443  N  N     . SER   B  1  68   ? -34.019 17.633  107.559 1.00 42.23 ? 66   SER   B N     1 
ATOM   9444  C  CA    . SER   B  1  68   ? -34.535 17.966  108.884 1.00 39.90 ? 66   SER   B CA    1 
ATOM   9445  C  C     . SER   B  1  68   ? -33.427 17.919  109.930 1.00 41.49 ? 66   SER   B C     1 
ATOM   9446  O  O     . SER   B  1  68   ? -33.296 18.834  110.752 1.00 42.89 ? 66   SER   B O     1 
ATOM   9447  C  CB    . SER   B  1  68   ? -35.673 17.014  109.257 1.00 42.79 ? 66   SER   B CB    1 
ATOM   9448  N  N     . THR   B  1  69   ? -32.623 16.851  109.918 1.00 39.24 ? 67   THR   B N     1 
ATOM   9449  C  CA    . THR   B  1  69   ? -31.483 16.765  110.826 1.00 36.32 ? 67   THR   B CA    1 
ATOM   9450  C  C     . THR   B  1  69   ? -30.539 17.946  110.646 1.00 38.85 ? 67   THR   B C     1 
ATOM   9451  O  O     . THR   B  1  69   ? -30.065 18.527  111.630 1.00 36.57 ? 67   THR   B O     1 
ATOM   9452  C  CB    . THR   B  1  69   ? -30.734 15.453  110.606 1.00 36.21 ? 67   THR   B CB    1 
ATOM   9453  O  OG1   . THR   B  1  69   ? -31.571 14.353  110.982 1.00 38.46 ? 67   THR   B OG1   1 
ATOM   9454  C  CG2   . THR   B  1  69   ? -29.461 15.420  111.443 1.00 32.94 ? 67   THR   B CG2   1 
ATOM   9455  N  N     . ALA   B  1  70   ? -30.242 18.306  109.393 1.00 34.76 ? 68   ALA   B N     1 
ATOM   9456  C  CA    . ALA   B  1  70   ? -29.391 19.463  109.142 1.00 38.04 ? 68   ALA   B CA    1 
ATOM   9457  C  C     . ALA   B  1  70   ? -30.016 20.740  109.686 1.00 37.66 ? 68   ALA   B C     1 
ATOM   9458  O  O     . ALA   B  1  70   ? -29.315 21.583  110.259 1.00 36.49 ? 68   ALA   B O     1 
ATOM   9459  C  CB    . ALA   B  1  70   ? -29.093 19.594  107.647 1.00 35.78 ? 68   ALA   B CB    1 
ATOM   9460  N  N     . ARG   B  1  71   ? -31.334 20.905  109.513 1.00 41.76 ? 69   ARG   B N     1 
ATOM   9461  C  CA    A ARG   B  1  71   ? -32.011 22.089  110.037 0.46 39.55 ? 69   ARG   B CA    1 
ATOM   9462  C  CA    B ARG   B  1  71   ? -31.991 22.098  110.036 0.54 39.57 ? 69   ARG   B CA    1 
ATOM   9463  C  C     . ARG   B  1  71   ? -31.870 22.168  111.551 1.00 29.78 ? 69   ARG   B C     1 
ATOM   9464  O  O     . ARG   B  1  71   ? -31.545 23.225  112.105 1.00 39.00 ? 69   ARG   B O     1 
ATOM   9465  C  CB    A ARG   B  1  71   ? -33.489 22.064  109.643 0.46 39.92 ? 69   ARG   B CB    1 
ATOM   9466  C  CB    B ARG   B  1  71   ? -33.458 22.144  109.604 0.54 39.94 ? 69   ARG   B CB    1 
ATOM   9467  C  CG    A ARG   B  1  71   ? -34.356 23.054  110.414 0.46 38.59 ? 69   ARG   B CG    1 
ATOM   9468  C  CG    B ARG   B  1  71   ? -34.252 23.248  110.288 0.54 38.66 ? 69   ARG   B CG    1 
ATOM   9469  C  CD    A ARG   B  1  71   ? -34.720 24.265  109.568 0.46 38.29 ? 69   ARG   B CD    1 
ATOM   9470  C  CD    B ARG   B  1  71   ? -35.635 23.430  109.679 0.54 37.99 ? 69   ARG   B CD    1 
ATOM   9471  N  NE    A ARG   B  1  71   ? -35.521 23.892  108.409 0.46 39.51 ? 69   ARG   B NE    1 
ATOM   9472  N  NE    B ARG   B  1  71   ? -35.585 24.071  108.371 0.54 39.62 ? 69   ARG   B NE    1 
ATOM   9473  C  CZ    A ARG   B  1  71   ? -35.868 24.726  107.438 0.46 39.17 ? 69   ARG   B CZ    1 
ATOM   9474  C  CZ    B ARG   B  1  71   ? -35.466 25.378  108.181 0.54 40.33 ? 69   ARG   B CZ    1 
ATOM   9475  N  NH1   A ARG   B  1  71   ? -35.508 25.999  107.458 0.46 41.08 ? 69   ARG   B NH1   1 
ATOM   9476  N  NH1   B ARG   B  1  71   ? -35.364 26.218  109.198 0.54 37.36 ? 69   ARG   B NH1   1 
ATOM   9477  N  NH2   A ARG   B  1  71   ? -36.593 24.270  106.420 0.46 39.14 ? 69   ARG   B NH2   1 
ATOM   9478  N  NH2   B ARG   B  1  71   ? -35.445 25.854  106.938 0.54 42.15 ? 69   ARG   B NH2   1 
ATOM   9479  N  N     . LYS   B  1  72   ? -32.105 21.043  112.233 1.00 33.91 ? 70   LYS   B N     1 
ATOM   9480  C  CA    . LYS   B  1  72   ? -32.000 21.000  113.687 1.00 36.04 ? 70   LYS   B CA    1 
ATOM   9481  C  C     . LYS   B  1  72   ? -30.598 21.380  114.150 1.00 37.37 ? 70   LYS   B C     1 
ATOM   9482  O  O     . LYS   B  1  72   ? -30.435 22.064  115.166 1.00 40.03 ? 70   LYS   B O     1 
ATOM   9483  C  CB    . LYS   B  1  72   ? -32.373 19.603  114.180 1.00 37.56 ? 70   LYS   B CB    1 
ATOM   9484  C  CG    . LYS   B  1  72   ? -32.296 19.409  115.688 1.00 40.30 ? 70   LYS   B CG    1 
ATOM   9485  C  CD    . LYS   B  1  72   ? -32.776 18.012  116.079 1.00 35.99 ? 70   LYS   B CD    1 
ATOM   9486  C  CE    . LYS   B  1  72   ? -32.572 17.729  117.558 1.00 43.00 ? 70   LYS   B CE    1 
ATOM   9487  N  NZ    . LYS   B  1  72   ? -33.387 18.617  118.428 1.00 38.72 ? 70   LYS   B NZ    1 
ATOM   9488  N  N     . LEU   B  1  73   ? -29.571 20.955  113.410 1.00 37.93 ? 71   LEU   B N     1 
ATOM   9489  C  CA    . LEU   B  1  73   ? -28.205 21.305  113.785 1.00 36.65 ? 71   LEU   B CA    1 
ATOM   9490  C  C     . LEU   B  1  73   ? -27.923 22.781  113.539 1.00 33.89 ? 71   LEU   B C     1 
ATOM   9491  O  O     . LEU   B  1  73   ? -27.238 23.430  114.337 1.00 37.05 ? 71   LEU   B O     1 
ATOM   9492  C  CB    . LEU   B  1  73   ? -27.214 20.445  113.005 1.00 33.28 ? 71   LEU   B CB    1 
ATOM   9493  C  CG    . LEU   B  1  73   ? -27.304 18.935  113.211 1.00 33.68 ? 71   LEU   B CG    1 
ATOM   9494  C  CD1   . LEU   B  1  73   ? -26.445 18.209  112.171 1.00 31.68 ? 71   LEU   B CD1   1 
ATOM   9495  C  CD2   . LEU   B  1  73   ? -26.878 18.573  114.621 1.00 36.29 ? 71   LEU   B CD2   1 
ATOM   9496  N  N     . ILE   B  1  74   ? -28.440 23.326  112.437 1.00 36.57 ? 72   ILE   B N     1 
ATOM   9497  C  CA    . ILE   B  1  74   ? -28.137 24.705  112.070 1.00 34.31 ? 72   ILE   B CA    1 
ATOM   9498  C  C     . ILE   B  1  74   ? -28.856 25.683  112.992 1.00 41.78 ? 72   ILE   B C     1 
ATOM   9499  O  O     . ILE   B  1  74   ? -28.276 26.684  113.432 1.00 37.43 ? 72   ILE   B O     1 
ATOM   9500  C  CB    . ILE   B  1  74   ? -28.454 24.938  110.582 1.00 34.48 ? 72   ILE   B CB    1 
ATOM   9501  C  CG1   . ILE   B  1  74   ? -27.420 24.204  109.723 1.00 35.79 ? 72   ILE   B CG1   1 
ATOM   9502  C  CG2   . ILE   B  1  74   ? -28.453 26.422  110.253 1.00 35.43 ? 72   ILE   B CG2   1 
ATOM   9503  C  CD1   . ILE   B  1  74   ? -27.851 23.987  108.303 1.00 35.05 ? 72   ILE   B CD1   1 
ATOM   9504  N  N     . GLU   B  1  75   ? -30.126 25.414  113.294 1.00 39.28 ? 73   GLU   B N     1 
ATOM   9505  C  CA    . GLU   B  1  75   ? -30.839 26.229  114.272 1.00 43.77 ? 73   GLU   B CA    1 
ATOM   9506  C  C     . GLU   B  1  75   ? -30.120 26.208  115.616 1.00 42.41 ? 73   GLU   B C     1 
ATOM   9507  O  O     . GLU   B  1  75   ? -29.917 27.256  116.242 1.00 46.60 ? 73   GLU   B O     1 
ATOM   9508  C  CB    . GLU   B  1  75   ? -32.281 25.738  114.408 1.00 41.00 ? 73   GLU   B CB    1 
ATOM   9509  N  N     . ALA   B  1  76   ? -29.703 25.019  116.060 1.00 38.60 ? 74   ALA   B N     1 
ATOM   9510  C  CA    . ALA   B  1  76   ? -28.930 24.904  117.294 1.00 39.12 ? 74   ALA   B CA    1 
ATOM   9511  C  C     . ALA   B  1  76   ? -27.644 25.722  117.225 1.00 40.02 ? 74   ALA   B C     1 
ATOM   9512  O  O     . ALA   B  1  76   ? -27.292 26.431  118.176 1.00 42.84 ? 74   ALA   B O     1 
ATOM   9513  C  CB    . ALA   B  1  76   ? -28.626 23.433  117.582 1.00 36.64 ? 74   ALA   B CB    1 
ATOM   9514  N  N     . LEU   B  1  77   ? -26.923 25.631  116.104 1.00 39.05 ? 75   LEU   B N     1 
ATOM   9515  C  CA    . LEU   B  1  77   ? -25.691 26.398  115.948 1.00 42.12 ? 75   LEU   B CA    1 
ATOM   9516  C  C     . LEU   B  1  77   ? -25.965 27.895  116.006 1.00 42.45 ? 75   LEU   B C     1 
ATOM   9517  O  O     . LEU   B  1  77   ? -25.277 28.640  116.714 1.00 44.41 ? 75   LEU   B O     1 
ATOM   9518  C  CB    . LEU   B  1  77   ? -25.008 26.030  114.628 1.00 37.05 ? 75   LEU   B CB    1 
ATOM   9519  C  CG    . LEU   B  1  77   ? -24.211 24.728  114.593 1.00 37.86 ? 75   LEU   B CG    1 
ATOM   9520  C  CD1   . LEU   B  1  77   ? -23.718 24.447  113.185 1.00 34.06 ? 75   LEU   B CD1   1 
ATOM   9521  C  CD2   . LEU   B  1  77   ? -23.043 24.827  115.543 1.00 38.52 ? 75   LEU   B CD2   1 
ATOM   9522  N  N     . ARG   B  1  78   ? -26.965 28.359  115.258 1.00 37.30 ? 76   ARG   B N     1 
ATOM   9523  C  CA    . ARG   B  1  78   ? -27.265 29.783  115.221 1.00 41.67 ? 76   ARG   B CA    1 
ATOM   9524  C  C     . ARG   B  1  78   ? -27.980 30.275  116.469 1.00 41.36 ? 76   ARG   B C     1 
ATOM   9525  O  O     . ARG   B  1  78   ? -28.091 31.491  116.658 1.00 43.90 ? 76   ARG   B O     1 
ATOM   9526  C  CB    . ARG   B  1  78   ? -28.094 30.119  113.987 1.00 42.93 ? 76   ARG   B CB    1 
ATOM   9527  C  CG    . ARG   B  1  78   ? -27.282 30.100  112.719 1.00 42.44 ? 76   ARG   B CG    1 
ATOM   9528  C  CD    . ARG   B  1  78   ? -28.144 30.372  111.516 1.00 42.76 ? 76   ARG   B CD    1 
ATOM   9529  N  NE    . ARG   B  1  78   ? -27.354 30.941  110.435 1.00 43.65 ? 76   ARG   B NE    1 
ATOM   9530  C  CZ    . ARG   B  1  78   ? -27.834 31.236  109.237 1.00 48.71 ? 76   ARG   B CZ    1 
ATOM   9531  N  NH1   . ARG   B  1  78   ? -29.094 30.985  108.918 1.00 49.22 ? 76   ARG   B NH1   1 
ATOM   9532  N  NH2   . ARG   B  1  78   ? -27.031 31.800  108.338 1.00 46.24 ? 76   ARG   B NH2   1 
ATOM   9533  N  N     . GLY   B  1  79   ? -28.460 29.369  117.314 1.00 42.50 ? 77   GLY   B N     1 
ATOM   9534  C  CA    . GLY   B  1  79   ? -29.115 29.778  118.539 1.00 45.42 ? 77   GLY   B CA    1 
ATOM   9535  C  C     . GLY   B  1  79   ? -28.188 30.096  119.688 1.00 49.67 ? 77   GLY   B C     1 
ATOM   9536  O  O     . GLY   B  1  79   ? -28.649 30.638  120.695 1.00 39.92 ? 77   GLY   B O     1 
ATOM   9537  N  N     . LYS   B  1  80   ? -26.897 29.794  119.562 1.00 49.53 ? 78   LYS   B N     1 
ATOM   9538  C  CA    . LYS   B  1  80   ? -25.960 29.922  120.668 1.00 47.84 ? 78   LYS   B CA    1 
ATOM   9539  C  C     . LYS   B  1  80   ? -24.773 30.793  120.258 1.00 50.65 ? 78   LYS   B C     1 
ATOM   9540  O  O     . LYS   B  1  80   ? -24.659 31.233  119.108 1.00 49.85 ? 78   LYS   B O     1 
ATOM   9541  C  CB    . LYS   B  1  80   ? -25.525 28.544  121.185 1.00 50.46 ? 78   LYS   B CB    1 
ATOM   9542  C  CG    . LYS   B  1  80   ? -24.938 27.625  120.124 1.00 43.72 ? 78   LYS   B CG    1 
ATOM   9543  C  CD    . LYS   B  1  80   ? -24.922 26.175  120.603 1.00 44.58 ? 78   LYS   B CD    1 
ATOM   9544  C  CE    . LYS   B  1  80   ? -24.140 25.271  119.647 1.00 33.97 ? 78   LYS   B CE    1 
ATOM   9545  N  NZ    . LYS   B  1  80   ? -24.177 23.835  120.070 1.00 37.73 ? 78   LYS   B NZ    1 
ATOM   9546  N  N     . HIS   B  1  81   ? -23.887 31.035  121.224 1.00 62.74 ? 79   HIS   B N     1 
ATOM   9547  C  CA    . HIS   B  1  81   ? -22.728 31.920  121.063 1.00 61.73 ? 79   HIS   B CA    1 
ATOM   9548  C  C     . HIS   B  1  81   ? -23.150 33.354  120.747 1.00 57.16 ? 79   HIS   B C     1 
ATOM   9549  O  O     . HIS   B  1  81   ? -23.439 34.138  121.654 1.00 57.58 ? 79   HIS   B O     1 
ATOM   9550  C  CB    . HIS   B  1  81   ? -21.751 31.390  120.005 1.00 54.28 ? 79   HIS   B CB    1 
ATOM   9551  N  N     . GLY   B  1  85   ? -15.980 36.409  120.963 1.00 45.64 ? 83   GLY   B N     1 
ATOM   9552  C  CA    . GLY   B  1  85   ? -14.727 36.691  121.637 1.00 39.16 ? 83   GLY   B CA    1 
ATOM   9553  C  C     . GLY   B  1  85   ? -14.102 37.989  121.162 1.00 42.56 ? 83   GLY   B C     1 
ATOM   9554  O  O     . GLY   B  1  85   ? -14.166 39.012  121.849 1.00 37.20 ? 83   GLY   B O     1 
ATOM   9555  N  N     . VAL   B  1  86   ? -13.487 37.942  119.978 1.00 42.10 ? 84   VAL   B N     1 
ATOM   9556  C  CA    . VAL   B  1  86   ? -12.952 39.158  119.374 1.00 39.15 ? 84   VAL   B CA    1 
ATOM   9557  C  C     . VAL   B  1  86   ? -14.072 40.147  119.075 1.00 37.60 ? 84   VAL   B C     1 
ATOM   9558  O  O     . VAL   B  1  86   ? -13.884 41.364  119.186 1.00 37.19 ? 84   VAL   B O     1 
ATOM   9559  C  CB    . VAL   B  1  86   ? -12.121 38.820  118.120 1.00 36.49 ? 84   VAL   B CB    1 
ATOM   9560  N  N     . GLU   B  1  87   ? -15.253 39.644  118.708 1.00 39.99 ? 85   GLU   B N     1 
ATOM   9561  C  CA    . GLU   B  1  87   ? -16.380 40.525  118.410 1.00 43.18 ? 85   GLU   B CA    1 
ATOM   9562  C  C     . GLU   B  1  87   ? -16.781 41.350  119.627 1.00 37.95 ? 85   GLU   B C     1 
ATOM   9563  O  O     . GLU   B  1  87   ? -17.044 42.553  119.513 1.00 38.48 ? 85   GLU   B O     1 
ATOM   9564  C  CB    . GLU   B  1  87   ? -17.565 39.702  117.905 1.00 48.47 ? 85   GLU   B CB    1 
ATOM   9565  N  N     . GLY   B  1  88   ? -16.839 40.720  120.804 1.00 38.21 ? 86   GLY   B N     1 
ATOM   9566  C  CA    . GLY   B  1  88   ? -17.185 41.453  122.009 1.00 38.27 ? 86   GLY   B CA    1 
ATOM   9567  C  C     . GLY   B  1  88   ? -16.154 42.496  122.386 1.00 31.99 ? 86   GLY   B C     1 
ATOM   9568  O  O     . GLY   B  1  88   ? -16.503 43.564  122.900 1.00 32.92 ? 86   GLY   B O     1 
ATOM   9569  N  N     . LEU   B  1  89   ? -14.875 42.209  122.130 1.00 34.81 ? 87   LEU   B N     1 
ATOM   9570  C  CA    . LEU   B  1  89   ? -13.829 43.193  122.385 1.00 34.03 ? 87   LEU   B CA    1 
ATOM   9571  C  C     . LEU   B  1  89   ? -13.968 44.388  121.451 1.00 27.13 ? 87   LEU   B C     1 
ATOM   9572  O  O     . LEU   B  1  89   ? -13.876 45.542  121.889 1.00 29.78 ? 87   LEU   B O     1 
ATOM   9573  C  CB    . LEU   B  1  89   ? -12.463 42.534  122.220 1.00 35.05 ? 87   LEU   B CB    1 
ATOM   9574  C  CG    . LEU   B  1  89   ? -11.237 43.430  122.368 1.00 35.85 ? 87   LEU   B CG    1 
ATOM   9575  C  CD1   . LEU   B  1  89   ? -11.216 44.050  123.744 1.00 39.78 ? 87   LEU   B CD1   1 
ATOM   9576  C  CD2   . LEU   B  1  89   ? -9.972  42.625  122.111 1.00 39.43 ? 87   LEU   B CD2   1 
ATOM   9577  N  N     . VAL   B  1  90   ? -14.209 44.126  120.166 1.00 30.14 ? 88   VAL   B N     1 
ATOM   9578  C  CA    . VAL   B  1  90   ? -14.385 45.198  119.191 1.00 31.40 ? 88   VAL   B CA    1 
ATOM   9579  C  C     . VAL   B  1  90   ? -15.586 46.060  119.555 1.00 35.35 ? 88   VAL   B C     1 
ATOM   9580  O  O     . VAL   B  1  90   ? -15.539 47.292  119.449 1.00 34.89 ? 88   VAL   B O     1 
ATOM   9581  C  CB    . VAL   B  1  90   ? -14.499 44.607  117.773 1.00 33.82 ? 88   VAL   B CB    1 
ATOM   9582  C  CG1   . VAL   B  1  90   ? -14.945 45.670  116.774 1.00 37.05 ? 88   VAL   B CG1   1 
ATOM   9583  C  CG2   . VAL   B  1  90   ? -13.176 43.982  117.349 1.00 31.15 ? 88   VAL   B CG2   1 
ATOM   9584  N  N     . GLN   B  1  91   ? -16.674 45.432  120.009 1.00 35.05 ? 89   GLN   B N     1 
ATOM   9585  C  CA    . GLN   B  1  91   ? -17.862 46.196  120.373 1.00 36.02 ? 89   GLN   B CA    1 
ATOM   9586  C  C     . GLN   B  1  91   ? -17.633 47.014  121.638 1.00 33.45 ? 89   GLN   B C     1 
ATOM   9587  O  O     . GLN   B  1  91   ? -18.031 48.182  121.708 1.00 37.21 ? 89   GLN   B O     1 
ATOM   9588  C  CB    . GLN   B  1  91   ? -19.063 45.262  120.528 1.00 40.42 ? 89   GLN   B CB    1 
ATOM   9589  N  N     . GLU   B  1  92   ? -16.980 46.428  122.644 1.00 32.02 ? 90   GLU   B N     1 
ATOM   9590  C  CA    . GLU   B  1  92   ? -16.821 47.121  123.918 1.00 32.52 ? 90   GLU   B CA    1 
ATOM   9591  C  C     . GLU   B  1  92   ? -15.975 48.380  123.776 1.00 32.03 ? 90   GLU   B C     1 
ATOM   9592  O  O     . GLU   B  1  92   ? -16.267 49.406  124.401 1.00 34.55 ? 90   GLU   B O     1 
ATOM   9593  C  CB    . GLU   B  1  92   ? -16.220 46.188  124.970 1.00 36.24 ? 90   GLU   B CB    1 
ATOM   9594  C  CG    . GLU   B  1  92   ? -16.012 46.869  126.312 1.00 37.75 ? 90   GLU   B CG    1 
ATOM   9595  C  CD    . GLU   B  1  92   ? -15.335 45.984  127.345 1.00 38.04 ? 90   GLU   B CD    1 
ATOM   9596  O  OE1   . GLU   B  1  92   ? -15.024 44.814  127.028 1.00 44.98 ? 90   GLU   B OE1   1 
ATOM   9597  O  OE2   . GLU   B  1  92   ? -15.113 46.468  128.473 1.00 39.29 ? 90   GLU   B OE2   1 
ATOM   9598  N  N     . TYR   B  1  93   ? -14.926 48.330  122.959 1.00 32.57 ? 91   TYR   B N     1 
ATOM   9599  C  CA    . TYR   B  1  93   ? -14.046 49.477  122.789 1.00 31.38 ? 91   TYR   B CA    1 
ATOM   9600  C  C     . TYR   B  1  93   ? -14.272 50.211  121.476 1.00 30.40 ? 91   TYR   B C     1 
ATOM   9601  O  O     . TYR   B  1  93   ? -13.455 51.062  121.111 1.00 30.90 ? 91   TYR   B O     1 
ATOM   9602  C  CB    . TYR   B  1  93   ? -12.585 49.068  122.969 1.00 27.46 ? 91   TYR   B CB    1 
ATOM   9603  C  CG    . TYR   B  1  93   ? -12.305 48.671  124.393 1.00 28.53 ? 91   TYR   B CG    1 
ATOM   9604  C  CD1   . TYR   B  1  93   ? -12.002 49.630  125.349 1.00 26.71 ? 91   TYR   B CD1   1 
ATOM   9605  C  CD2   . TYR   B  1  93   ? -12.378 47.343  124.791 1.00 31.96 ? 91   TYR   B CD2   1 
ATOM   9606  C  CE1   . TYR   B  1  93   ? -11.766 49.281  126.660 1.00 27.42 ? 91   TYR   B CE1   1 
ATOM   9607  C  CE2   . TYR   B  1  93   ? -12.143 46.982  126.108 1.00 31.04 ? 91   TYR   B CE2   1 
ATOM   9608  C  CZ    . TYR   B  1  93   ? -11.838 47.958  127.035 1.00 30.79 ? 91   TYR   B CZ    1 
ATOM   9609  O  OH    . TYR   B  1  93   ? -11.603 47.614  128.348 1.00 33.18 ? 91   TYR   B OH    1 
ATOM   9610  N  N     . SER   B  1  94   ? -15.362 49.906  120.773 1.00 27.92 ? 92   SER   B N     1 
ATOM   9611  C  CA    . SER   B  1  94   ? -15.717 50.576  119.528 1.00 26.23 ? 92   SER   B CA    1 
ATOM   9612  C  C     . SER   B  1  94   ? -14.525 50.617  118.579 1.00 28.94 ? 92   SER   B C     1 
ATOM   9613  O  O     . SER   B  1  94   ? -14.159 51.661  118.034 1.00 28.65 ? 92   SER   B O     1 
ATOM   9614  C  CB    . SER   B  1  94   ? -16.277 51.972  119.788 1.00 30.92 ? 92   SER   B CB    1 
ATOM   9615  O  OG    . SER   B  1  94   ? -17.358 51.908  120.696 1.00 34.16 ? 92   SER   B OG    1 
ATOM   9616  N  N     . LEU   B  1  95   ? -13.897 49.461  118.407 1.00 23.86 ? 93   LEU   B N     1 
ATOM   9617  C  CA    . LEU   B  1  95   ? -12.725 49.377  117.558 1.00 23.04 ? 93   LEU   B CA    1 
ATOM   9618  C  C     . LEU   B  1  95   ? -13.134 49.288  116.097 1.00 24.65 ? 93   LEU   B C     1 
ATOM   9619  O  O     . LEU   B  1  95   ? -14.120 48.633  115.745 1.00 26.51 ? 93   LEU   B O     1 
ATOM   9620  C  CB    . LEU   B  1  95   ? -11.912 48.135  117.909 1.00 23.14 ? 93   LEU   B CB    1 
ATOM   9621  C  CG    . LEU   B  1  95   ? -11.389 48.048  119.338 1.00 26.55 ? 93   LEU   B CG    1 
ATOM   9622  C  CD1   . LEU   B  1  95   ? -10.483 46.844  119.480 1.00 25.17 ? 93   LEU   B CD1   1 
ATOM   9623  C  CD2   . LEU   B  1  95   ? -10.674 49.336  119.730 1.00 26.54 ? 93   LEU   B CD2   1 
ATOM   9624  N  N     . SER   B  1  96   ? -12.358 49.938  115.240 1.00 22.48 ? 94   SER   B N     1 
ATOM   9625  C  CA    . SER   B  1  96   ? -12.445 49.647  113.830 1.00 23.88 ? 94   SER   B CA    1 
ATOM   9626  C  C     . SER   B  1  96   ? -11.770 48.306  113.563 1.00 23.82 ? 94   SER   B C     1 
ATOM   9627  O  O     . SER   B  1  96   ? -11.075 47.752  114.422 1.00 21.84 ? 94   SER   B O     1 
ATOM   9628  C  CB    . SER   B  1  96   ? -11.725 50.729  113.036 1.00 22.19 ? 94   SER   B CB    1 
ATOM   9629  O  OG    . SER   B  1  96   ? -10.327 50.652  113.264 1.00 20.34 ? 94   SER   B OG    1 
ATOM   9630  N  N     . SER   B  1  97   ? -11.970 47.781  112.355 1.00 21.22 ? 95   SER   B N     1 
ATOM   9631  C  CA    . SER   B  1  97   ? -11.308 46.535  111.988 1.00 21.77 ? 95   SER   B CA    1 
ATOM   9632  C  C     . SER   B  1  97   ? -9.796  46.665  112.111 1.00 21.30 ? 95   SER   B C     1 
ATOM   9633  O  O     . SER   B  1  97   ? -9.138  45.811  112.714 1.00 20.81 ? 95   SER   B O     1 
ATOM   9634  C  CB    . SER   B  1  97   ? -11.705 46.115  110.576 1.00 26.11 ? 95   SER   B CB    1 
ATOM   9635  O  OG    . SER   B  1  97   ? -13.073 45.757  110.551 1.00 32.56 ? 95   SER   B OG    1 
ATOM   9636  N  N     . GLN   B  1  98   ? -9.229  47.741  111.561 1.00 19.86 ? 96   GLN   B N     1 
ATOM   9637  C  CA    . GLN   B  1  98   ? -7.782  47.924  111.632 1.00 18.79 ? 96   GLN   B CA    1 
ATOM   9638  C  C     . GLN   B  1  98   ? -7.311  48.059  113.074 1.00 18.07 ? 96   GLN   B C     1 
ATOM   9639  O  O     . GLN   B  1  98   ? -6.224  47.587  113.421 1.00 18.34 ? 96   GLN   B O     1 
ATOM   9640  C  CB    . GLN   B  1  98   ? -7.350  49.143  110.805 1.00 19.01 ? 96   GLN   B CB    1 
ATOM   9641  C  CG    . GLN   B  1  98   ? -7.388  48.926  109.301 1.00 18.44 ? 96   GLN   B CG    1 
ATOM   9642  C  CD    . GLN   B  1  98   ? -6.411  47.863  108.854 1.00 19.51 ? 96   GLN   B CD    1 
ATOM   9643  O  OE1   . GLN   B  1  98   ? -6.702  46.668  108.919 1.00 24.10 ? 96   GLN   B OE1   1 
ATOM   9644  N  NE2   . GLN   B  1  98   ? -5.236  48.289  108.392 1.00 19.29 ? 96   GLN   B NE2   1 
ATOM   9645  N  N     . GLU   B  1  99   ? -8.112  48.695  113.929 1.00 18.22 ? 97   GLU   B N     1 
ATOM   9646  C  CA    . GLU   B  1  99   ? -7.745  48.779  115.336 1.00 17.90 ? 97   GLU   B CA    1 
ATOM   9647  C  C     . GLU   B  1  99   ? -7.791  47.409  115.990 1.00 22.76 ? 97   GLU   B C     1 
ATOM   9648  O  O     . GLU   B  1  99   ? -6.911  47.068  116.783 1.00 20.54 ? 97   GLU   B O     1 
ATOM   9649  C  CB    . GLU   B  1  99   ? -8.667  49.756  116.058 1.00 21.63 ? 97   GLU   B CB    1 
ATOM   9650  C  CG    . GLU   B  1  99   ? -8.385  51.210  115.715 1.00 19.67 ? 97   GLU   B CG    1 
ATOM   9651  C  CD    . GLU   B  1  99   ? -9.479  52.143  116.204 1.00 21.36 ? 97   GLU   B CD    1 
ATOM   9652  O  OE1   . GLU   B  1  99   ? -10.470 51.654  116.800 1.00 22.55 ? 97   GLU   B OE1   1 
ATOM   9653  O  OE2   . GLU   B  1  99   ? -9.342  53.374  116.045 1.00 22.04 ? 97   GLU   B OE2   1 
ATOM   9654  N  N     . GLY   B  1  100  ? -8.807  46.608  115.667 1.00 19.50 ? 98   GLY   B N     1 
ATOM   9655  C  CA    . GLY   B  1  100  ? -8.848  45.252  116.184 1.00 22.21 ? 98   GLY   B CA    1 
ATOM   9656  C  C     . GLY   B  1  100  ? -7.640  44.446  115.753 1.00 21.00 ? 98   GLY   B C     1 
ATOM   9657  O  O     . GLY   B  1  100  ? -7.033  43.744  116.563 1.00 20.69 ? 98   GLY   B O     1 
ATOM   9658  N  N     . VAL   B  1  101  ? -7.261  44.553  114.477 1.00 19.64 ? 99   VAL   B N     1 
ATOM   9659  C  CA    . VAL   B  1  101  ? -6.088  43.831  113.991 1.00 19.45 ? 99   VAL   B CA    1 
ATOM   9660  C  C     . VAL   B  1  101  ? -4.834  44.327  114.699 1.00 19.58 ? 99   VAL   B C     1 
ATOM   9661  O  O     . VAL   B  1  101  ? -4.014  43.536  115.190 1.00 20.00 ? 99   VAL   B O     1 
ATOM   9662  C  CB    . VAL   B  1  101  ? -5.974  43.968  112.462 1.00 18.04 ? 99   VAL   B CB    1 
ATOM   9663  C  CG1   . VAL   B  1  101  ? -4.653  43.404  111.965 1.00 21.25 ? 99   VAL   B CG1   1 
ATOM   9664  C  CG2   . VAL   B  1  101  ? -7.133  43.261  111.788 1.00 20.08 ? 99   VAL   B CG2   1 
ATOM   9665  N  N     . ALA   B  1  102  ? -4.663  45.648  114.748 1.00 18.55 ? 100  ALA   B N     1 
ATOM   9666  C  CA    . ALA   B  1  102  ? -3.479  46.222  115.377 1.00 18.76 ? 100  ALA   B CA    1 
ATOM   9667  C  C     . ALA   B  1  102  ? -3.396  45.813  116.837 1.00 18.53 ? 100  ALA   B C     1 
ATOM   9668  O  O     . ALA   B  1  102  ? -2.311  45.503  117.343 1.00 19.25 ? 100  ALA   B O     1 
ATOM   9669  C  CB    . ALA   B  1  102  ? -3.534  47.746  115.274 1.00 18.72 ? 100  ALA   B CB    1 
ATOM   9670  N  N     . LEU   B  1  103  ? -4.538  45.803  117.532 1.00 17.41 ? 101  LEU   B N     1 
ATOM   9671  C  CA    . LEU   B  1  103  ? -4.548  45.424  118.937 1.00 18.94 ? 101  LEU   B CA    1 
ATOM   9672  C  C     . LEU   B  1  103  ? -4.114  43.979  119.117 1.00 21.77 ? 101  LEU   B C     1 
ATOM   9673  O  O     . LEU   B  1  103  ? -3.348  43.660  120.037 1.00 20.32 ? 101  LEU   B O     1 
ATOM   9674  C  CB    . LEU   B  1  103  ? -5.946  45.635  119.517 1.00 20.15 ? 101  LEU   B CB    1 
ATOM   9675  C  CG    . LEU   B  1  103  ? -6.131  45.151  120.949 1.00 20.54 ? 101  LEU   B CG    1 
ATOM   9676  C  CD1   . LEU   B  1  103  ? -5.248  45.962  121.874 1.00 24.62 ? 101  LEU   B CD1   1 
ATOM   9677  C  CD2   . LEU   B  1  103  ? -7.591  45.281  121.338 1.00 21.20 ? 101  LEU   B CD2   1 
ATOM   9678  N  N     . MET   B  1  104  ? -4.597  43.087  118.258 1.00 19.37 ? 102  MET   B N     1 
ATOM   9679  C  CA    . MET   B  1  104  ? -4.211  41.688  118.383 1.00 21.05 ? 102  MET   B CA    1 
ATOM   9680  C  C     . MET   B  1  104  ? -2.739  41.501  118.070 1.00 20.89 ? 102  MET   B C     1 
ATOM   9681  O  O     . MET   B  1  104  ? -2.069  40.679  118.703 1.00 21.55 ? 102  MET   B O     1 
ATOM   9682  C  CB    . MET   B  1  104  ? -5.081  40.805  117.493 1.00 22.21 ? 102  MET   B CB    1 
ATOM   9683  C  CG    . MET   B  1  104  ? -6.556  40.846  117.877 1.00 24.23 ? 102  MET   B CG    1 
ATOM   9684  S  SD    . MET   B  1  104  ? -6.867  40.412  119.611 1.00 31.61 ? 102  MET   B SD    1 
ATOM   9685  C  CE    . MET   B  1  104  ? -6.474  38.671  119.578 1.00 38.51 ? 102  MET   B CE    1 
ATOM   9686  N  N     . CYS   B  1  105  ? -2.214  42.264  117.113 1.00 18.64 ? 103  CYS   B N     1 
ATOM   9687  C  CA    . CYS   B  1  105  ? -0.778  42.228  116.853 1.00 20.25 ? 103  CYS   B CA    1 
ATOM   9688  C  C     . CYS   B  1  105  ? 0.003   42.676  118.072 1.00 19.19 ? 103  CYS   B C     1 
ATOM   9689  O  O     . CYS   B  1  105  ? 1.004   42.051  118.443 1.00 21.14 ? 103  CYS   B O     1 
ATOM   9690  C  CB    . CYS   B  1  105  ? -0.427  43.125  115.672 1.00 16.93 ? 103  CYS   B CB    1 
ATOM   9691  S  SG    . CYS   B  1  105  ? -1.000  42.505  114.113 1.00 19.69 ? 103  CYS   B SG    1 
ATOM   9692  N  N     . LEU   B  1  106  ? -0.412  43.786  118.686 1.00 18.62 ? 104  LEU   B N     1 
ATOM   9693  C  CA    . LEU   B  1  106  ? 0.230   44.234  119.915 1.00 18.11 ? 104  LEU   B CA    1 
ATOM   9694  C  C     . LEU   B  1  106  ? 0.133   43.171  120.995 1.00 20.09 ? 104  LEU   B C     1 
ATOM   9695  O  O     . LEU   B  1  106  ? 1.105   42.918  121.719 1.00 22.75 ? 104  LEU   B O     1 
ATOM   9696  C  CB    . LEU   B  1  106  ? -0.416  45.529  120.405 1.00 18.65 ? 104  LEU   B CB    1 
ATOM   9697  C  CG    . LEU   B  1  106  ? 0.101   46.000  121.768 1.00 20.01 ? 104  LEU   B CG    1 
ATOM   9698  C  CD1   . LEU   B  1  106  ? 1.534   46.477  121.652 1.00 25.19 ? 104  LEU   B CD1   1 
ATOM   9699  C  CD2   . LEU   B  1  106  ? -0.790  47.090  122.337 1.00 22.94 ? 104  LEU   B CD2   1 
ATOM   9700  N  N     . ALA   B  1  107  ? -1.038  42.545  121.131 1.00 19.98 ? 105  ALA   B N     1 
ATOM   9701  C  CA    . ALA   B  1  107  ? -1.206  41.521  122.157 1.00 21.68 ? 105  ALA   B CA    1 
ATOM   9702  C  C     . ALA   B  1  107  ? -0.290  40.337  121.889 1.00 23.52 ? 105  ALA   B C     1 
ATOM   9703  O  O     . ALA   B  1  107  ? 0.368   39.836  122.805 1.00 24.96 ? 105  ALA   B O     1 
ATOM   9704  C  CB    . ALA   B  1  107  ? -2.661  41.066  122.195 1.00 22.21 ? 105  ALA   B CB    1 
ATOM   9705  N  N     . GLU   B  1  108  ? -0.225  39.890  120.633 1.00 22.93 ? 106  GLU   B N     1 
ATOM   9706  C  CA    . GLU   B  1  108  ? 0.687   38.815  120.258 1.00 23.08 ? 106  GLU   B CA    1 
ATOM   9707  C  C     . GLU   B  1  108  ? 2.113   39.144  120.673 1.00 27.41 ? 106  GLU   B C     1 
ATOM   9708  O  O     . GLU   B  1  108  ? 2.820   38.306  121.245 1.00 26.28 ? 106  GLU   B O     1 
ATOM   9709  C  CB    . GLU   B  1  108  ? 0.616   38.595  118.744 1.00 24.24 ? 106  GLU   B CB    1 
ATOM   9710  C  CG    . GLU   B  1  108  ? 1.729   37.714  118.174 1.00 26.79 ? 106  GLU   B CG    1 
ATOM   9711  C  CD    . GLU   B  1  108  ? 1.851   37.802  116.652 1.00 30.28 ? 106  GLU   B CD    1 
ATOM   9712  O  OE1   . GLU   B  1  108  ? 0.939   38.353  115.995 1.00 27.23 ? 106  GLU   B OE1   1 
ATOM   9713  O  OE2   . GLU   B  1  108  ? 2.880   37.329  116.111 1.00 32.36 ? 106  GLU   B OE2   1 
ATOM   9714  N  N     . ALA   B  1  109  ? 2.547   40.374  120.409 1.00 22.68 ? 107  ALA   B N     1 
ATOM   9715  C  CA    . ALA   B  1  109  ? 3.910   40.758  120.756 1.00 24.32 ? 107  ALA   B CA    1 
ATOM   9716  C  C     . ALA   B  1  109  ? 4.102   40.789  122.267 1.00 23.86 ? 107  ALA   B C     1 
ATOM   9717  O  O     . ALA   B  1  109  ? 5.136   40.340  122.776 1.00 26.22 ? 107  ALA   B O     1 
ATOM   9718  C  CB    . ALA   B  1  109  ? 4.251   42.107  120.125 1.00 26.31 ? 107  ALA   B CB    1 
ATOM   9719  N  N     . LEU   B  1  110  ? 3.113   41.305  123.002 1.00 23.17 ? 108  LEU   B N     1 
ATOM   9720  C  CA    . LEU   B  1  110  ? 3.220   41.338  124.456 1.00 23.23 ? 108  LEU   B CA    1 
ATOM   9721  C  C     . LEU   B  1  110  ? 3.251   39.935  125.043 1.00 25.07 ? 108  LEU   B C     1 
ATOM   9722  O  O     . LEU   B  1  110  ? 3.895   39.708  126.077 1.00 27.11 ? 108  LEU   B O     1 
ATOM   9723  C  CB    . LEU   B  1  110  ? 2.069   42.152  125.053 1.00 24.81 ? 108  LEU   B CB    1 
ATOM   9724  C  CG    . LEU   B  1  110  ? 2.184   43.657  124.795 1.00 23.18 ? 108  LEU   B CG    1 
ATOM   9725  C  CD1   . LEU   B  1  110  ? 0.857   44.355  125.047 1.00 24.40 ? 108  LEU   B CD1   1 
ATOM   9726  C  CD2   . LEU   B  1  110  ? 3.274   44.258  125.676 1.00 25.92 ? 108  LEU   B CD2   1 
ATOM   9727  N  N     . LEU   B  1  111  ? 2.585   38.982  124.397 1.00 25.72 ? 109  LEU   B N     1 
ATOM   9728  C  CA    . LEU   B  1  111  ? 2.594   37.610  124.881 1.00 30.07 ? 109  LEU   B CA    1 
ATOM   9729  C  C     . LEU   B  1  111  ? 3.912   36.899  124.617 1.00 30.98 ? 109  LEU   B C     1 
ATOM   9730  O  O     . LEU   B  1  111  ? 4.151   35.841  125.207 1.00 34.70 ? 109  LEU   B O     1 
ATOM   9731  C  CB    . LEU   B  1  111  ? 1.441   36.826  124.267 1.00 30.17 ? 109  LEU   B CB    1 
ATOM   9732  C  CG    . LEU   B  1  111  ? 0.082   37.253  124.804 1.00 27.26 ? 109  LEU   B CG    1 
ATOM   9733  C  CD1   . LEU   B  1  111  ? -0.991  36.606  123.968 1.00 28.92 ? 109  LEU   B CD1   1 
ATOM   9734  C  CD2   . LEU   B  1  111  ? -0.065  36.877  126.270 1.00 32.44 ? 109  LEU   B CD2   1 
ATOM   9735  N  N     . ARG   B  1  112  ? 4.769   37.452  123.760 1.00 29.55 ? 110  ARG   B N     1 
ATOM   9736  C  CA    . ARG   B  1  112  ? 6.125   36.935  123.648 1.00 32.41 ? 110  ARG   B CA    1 
ATOM   9737  C  C     . ARG   B  1  112  ? 6.965   37.273  124.868 1.00 32.57 ? 110  ARG   B C     1 
ATOM   9738  O  O     . ARG   B  1  112  ? 8.040   36.692  125.037 1.00 35.56 ? 110  ARG   B O     1 
ATOM   9739  C  CB    . ARG   B  1  112  ? 6.792   37.431  122.362 1.00 32.82 ? 110  ARG   B CB    1 
ATOM   9740  C  CG    . ARG   B  1  112  ? 6.107   36.934  121.095 1.00 35.10 ? 110  ARG   B CG    1 
ATOM   9741  C  CD    . ARG   B  1  112  ? 6.952   37.156  119.850 1.00 43.35 ? 110  ARG   B CD    1 
ATOM   9742  N  NE    . ARG   B  1  112  ? 6.888   38.527  119.357 1.00 39.40 ? 110  ARG   B NE    1 
ATOM   9743  C  CZ    . ARG   B  1  112  ? 6.052   38.949  118.417 1.00 41.78 ? 110  ARG   B CZ    1 
ATOM   9744  N  NH1   . ARG   B  1  112  ? 5.168   38.136  117.862 1.00 43.92 ? 110  ARG   B NH1   1 
ATOM   9745  N  NH2   . ARG   B  1  112  ? 6.109   40.218  118.020 1.00 45.79 ? 110  ARG   B NH2   1 
ATOM   9746  N  N     . ILE   B  1  113  ? 6.504   38.186  125.717 1.00 30.38 ? 111  ILE   B N     1 
ATOM   9747  C  CA    . ILE   B  1  113  ? 7.127   38.413  127.017 1.00 29.95 ? 111  ILE   B CA    1 
ATOM   9748  C  C     . ILE   B  1  113  ? 6.591   37.346  127.961 1.00 32.69 ? 111  ILE   B C     1 
ATOM   9749  O  O     . ILE   B  1  113  ? 5.409   37.381  128.332 1.00 36.09 ? 111  ILE   B O     1 
ATOM   9750  C  CB    . ILE   B  1  113  ? 6.848   39.831  127.540 1.00 30.35 ? 111  ILE   B CB    1 
ATOM   9751  C  CG1   . ILE   B  1  113  ? 7.376   40.874  126.551 1.00 29.99 ? 111  ILE   B CG1   1 
ATOM   9752  C  CG2   . ILE   B  1  113  ? 7.462   40.021  128.927 1.00 32.43 ? 111  ILE   B CG2   1 
ATOM   9753  C  CD1   . ILE   B  1  113  ? 7.024   42.296  126.927 1.00 31.07 ? 111  ILE   B CD1   1 
ATOM   9754  N  N     . PRO   B  1  114  ? 7.415   36.375  128.367 1.00 41.06 ? 112  PRO   B N     1 
ATOM   9755  C  CA    . PRO   B  1  114  ? 6.879   35.248  129.144 1.00 36.30 ? 112  PRO   B CA    1 
ATOM   9756  C  C     . PRO   B  1  114  ? 6.522   35.603  130.575 1.00 35.17 ? 112  PRO   B C     1 
ATOM   9757  O  O     . PRO   B  1  114  ? 5.595   35.004  131.134 1.00 39.68 ? 112  PRO   B O     1 
ATOM   9758  C  CB    . PRO   B  1  114  ? 8.005   34.206  129.075 1.00 34.31 ? 112  PRO   B CB    1 
ATOM   9759  C  CG    . PRO   B  1  114  ? 9.240   35.013  128.871 1.00 38.84 ? 112  PRO   B CG    1 
ATOM   9760  C  CD    . PRO   B  1  114  ? 8.846   36.216  128.059 1.00 36.26 ? 112  PRO   B CD    1 
ATOM   9761  N  N     . ASP   B  1  115  ? 7.221   36.554  131.186 1.00 37.35 ? 113  ASP   B N     1 
ATOM   9762  C  CA    . ASP   B  1  115  ? 6.980   36.902  132.581 1.00 42.46 ? 113  ASP   B CA    1 
ATOM   9763  C  C     . ASP   B  1  115  ? 5.797   37.860  132.678 1.00 41.45 ? 113  ASP   B C     1 
ATOM   9764  O  O     . ASP   B  1  115  ? 5.838   38.963  132.120 1.00 40.68 ? 113  ASP   B O     1 
ATOM   9765  C  CB    . ASP   B  1  115  ? 8.233   37.532  133.183 1.00 40.19 ? 113  ASP   B CB    1 
ATOM   9766  C  CG    . ASP   B  1  115  ? 8.019   38.005  134.606 1.00 45.98 ? 113  ASP   B CG    1 
ATOM   9767  O  OD1   . ASP   B  1  115  ? 7.495   37.222  135.428 1.00 53.31 ? 113  ASP   B OD1   1 
ATOM   9768  O  OD2   . ASP   B  1  115  ? 8.385   39.160  134.906 1.00 49.11 ? 113  ASP   B OD2   1 
ATOM   9769  N  N     . THR   B  1  116  ? 4.750   37.440  133.393 1.00 40.33 ? 114  THR   B N     1 
ATOM   9770  C  CA    . THR   B  1  116  ? 3.548   38.261  133.519 1.00 42.98 ? 114  THR   B CA    1 
ATOM   9771  C  C     . THR   B  1  116  ? 3.862   39.627  134.120 1.00 43.67 ? 114  THR   B C     1 
ATOM   9772  O  O     . THR   B  1  116  ? 3.356   40.653  133.648 1.00 39.51 ? 114  THR   B O     1 
ATOM   9773  C  CB    . THR   B  1  116  ? 2.497   37.522  134.351 1.00 46.12 ? 114  THR   B CB    1 
ATOM   9774  O  OG1   . THR   B  1  116  ? 2.092   36.333  133.661 1.00 52.80 ? 114  THR   B OG1   1 
ATOM   9775  C  CG2   . THR   B  1  116  ? 1.272   38.402  134.589 1.00 46.93 ? 114  THR   B CG2   1 
ATOM   9776  N  N     . ALA   B  1  117  ? 4.699   39.665  135.158 1.00 43.28 ? 115  ALA   B N     1 
ATOM   9777  C  CA    . ALA   B  1  117  ? 5.002   40.937  135.806 1.00 42.27 ? 115  ALA   B CA    1 
ATOM   9778  C  C     . ALA   B  1  117  ? 5.731   41.881  134.859 1.00 36.89 ? 115  ALA   B C     1 
ATOM   9779  O  O     . ALA   B  1  117  ? 5.412   43.074  134.795 1.00 42.73 ? 115  ALA   B O     1 
ATOM   9780  C  CB    . ALA   B  1  117  ? 5.824   40.702  137.073 1.00 38.15 ? 115  ALA   B CB    1 
ATOM   9781  N  N     . THR   B  1  118  ? 6.716   41.367  134.119 1.00 37.47 ? 116  THR   B N     1 
ATOM   9782  C  CA    . THR   B  1  118  ? 7.441   42.205  133.170 1.00 37.30 ? 116  THR   B CA    1 
ATOM   9783  C  C     . THR   B  1  118  ? 6.512   42.710  132.078 1.00 38.15 ? 116  THR   B C     1 
ATOM   9784  O  O     . THR   B  1  118  ? 6.616   43.864  131.644 1.00 37.89 ? 116  THR   B O     1 
ATOM   9785  C  CB    . THR   B  1  118  ? 8.596   41.413  132.556 1.00 37.90 ? 116  THR   B CB    1 
ATOM   9786  O  OG1   . THR   B  1  118  ? 9.526   41.055  133.586 1.00 43.76 ? 116  THR   B OG1   1 
ATOM   9787  C  CG2   . THR   B  1  118  ? 9.314   42.234  131.497 1.00 37.74 ? 116  THR   B CG2   1 
ATOM   9788  N  N     . ARG   B  1  119  ? 5.594   41.856  131.628 1.00 36.30 ? 117  ARG   B N     1 
ATOM   9789  C  CA    . ARG   B  1  119  ? 4.649   42.248  130.588 1.00 35.15 ? 117  ARG   B CA    1 
ATOM   9790  C  C     . ARG   B  1  119  ? 3.673   43.293  131.110 1.00 36.01 ? 117  ARG   B C     1 
ATOM   9791  O  O     . ARG   B  1  119  ? 3.477   44.341  130.485 1.00 32.01 ? 117  ARG   B O     1 
ATOM   9792  C  CB    . ARG   B  1  119  ? 3.897   41.015  130.103 1.00 32.71 ? 117  ARG   B CB    1 
ATOM   9793  C  CG    . ARG   B  1  119  ? 2.987   41.264  128.909 1.00 30.57 ? 117  ARG   B CG    1 
ATOM   9794  C  CD    . ARG   B  1  119  ? 2.019   40.119  128.769 1.00 31.83 ? 117  ARG   B CD    1 
ATOM   9795  N  NE    . ARG   B  1  119  ? 2.725   38.851  128.630 1.00 33.47 ? 117  ARG   B NE    1 
ATOM   9796  C  CZ    . ARG   B  1  119  ? 2.357   37.725  129.227 1.00 40.92 ? 117  ARG   B CZ    1 
ATOM   9797  N  NH1   . ARG   B  1  119  ? 1.294   37.676  130.014 1.00 33.91 ? 117  ARG   B NH1   1 
ATOM   9798  N  NH2   . ARG   B  1  119  ? 3.079   36.625  129.039 1.00 42.48 ? 117  ARG   B NH2   1 
ATOM   9799  N  N     . ASP   B  1  120  ? 3.060   43.026  132.267 1.00 33.48 ? 118  ASP   B N     1 
ATOM   9800  C  CA    . ASP   B  1  120  ? 2.118   43.979  132.844 1.00 35.92 ? 118  ASP   B CA    1 
ATOM   9801  C  C     . ASP   B  1  120  ? 2.787   45.306  133.176 1.00 40.10 ? 118  ASP   B C     1 
ATOM   9802  O  O     . ASP   B  1  120  ? 2.158   46.363  133.048 1.00 36.16 ? 118  ASP   B O     1 
ATOM   9803  C  CB    . ASP   B  1  120  ? 1.436   43.373  134.072 1.00 38.51 ? 118  ASP   B CB    1 
ATOM   9804  C  CG    . ASP   B  1  120  ? 0.473   42.253  133.709 1.00 45.30 ? 118  ASP   B CG    1 
ATOM   9805  O  OD1   . ASP   B  1  120  ? 0.236   42.039  132.501 1.00 45.58 ? 118  ASP   B OD1   1 
ATOM   9806  O  OD2   . ASP   B  1  120  ? -0.047  41.584  134.628 1.00 48.83 ? 118  ASP   B OD2   1 
ATOM   9807  N  N     . ALA   B  1  121  ? 4.060   45.280  133.582 1.00 39.04 ? 119  ALA   B N     1 
ATOM   9808  C  CA    . ALA   B  1  121  ? 4.763   46.529  133.857 1.00 41.65 ? 119  ALA   B CA    1 
ATOM   9809  C  C     . ALA   B  1  121  ? 5.020   47.313  132.577 1.00 37.98 ? 119  ALA   B C     1 
ATOM   9810  O  O     . ALA   B  1  121  ? 4.878   48.540  132.556 1.00 38.72 ? 119  ALA   B O     1 
ATOM   9811  C  CB    . ALA   B  1  121  ? 6.068   46.260  134.608 1.00 37.79 ? 119  ALA   B CB    1 
ATOM   9812  N  N     . LEU   B  1  122  ? 5.400   46.625  131.498 1.00 36.75 ? 120  LEU   B N     1 
ATOM   9813  C  CA    . LEU   B  1  122  ? 5.613   47.313  130.230 1.00 35.97 ? 120  LEU   B CA    1 
ATOM   9814  C  C     . LEU   B  1  122  ? 4.317   47.930  129.719 1.00 33.90 ? 120  LEU   B C     1 
ATOM   9815  O  O     . LEU   B  1  122  ? 4.319   49.037  129.169 1.00 35.33 ? 120  LEU   B O     1 
ATOM   9816  C  CB    . LEU   B  1  122  ? 6.178   46.339  129.196 1.00 35.45 ? 120  LEU   B CB    1 
ATOM   9817  C  CG    . LEU   B  1  122  ? 6.550   46.972  127.857 1.00 36.78 ? 120  LEU   B CG    1 
ATOM   9818  C  CD1   . LEU   B  1  122  ? 7.808   47.817  128.004 1.00 40.10 ? 120  LEU   B CD1   1 
ATOM   9819  C  CD2   . LEU   B  1  122  ? 6.725   45.915  126.781 1.00 33.64 ? 120  LEU   B CD2   1 
ATOM   9820  N  N     . ILE   B  1  123  ? 3.201   47.221  129.893 1.00 30.68 ? 121  ILE   B N     1 
ATOM   9821  C  CA    . ILE   B  1  123  ? 1.902   47.739  129.472 1.00 34.23 ? 121  ILE   B CA    1 
ATOM   9822  C  C     . ILE   B  1  123  ? 1.568   49.016  130.229 1.00 39.03 ? 121  ILE   B C     1 
ATOM   9823  O  O     . ILE   B  1  123  ? 1.223   50.044  129.632 1.00 36.84 ? 121  ILE   B O     1 
ATOM   9824  C  CB    . ILE   B  1  123  ? 0.815   46.666  129.664 1.00 31.92 ? 121  ILE   B CB    1 
ATOM   9825  C  CG1   . ILE   B  1  123  ? 1.008   45.523  128.666 1.00 26.92 ? 121  ILE   B CG1   1 
ATOM   9826  C  CG2   . ILE   B  1  123  ? -0.578  47.278  129.535 1.00 32.74 ? 121  ILE   B CG2   1 
ATOM   9827  C  CD1   . ILE   B  1  123  ? 0.125   44.340  128.946 1.00 27.26 ? 121  ILE   B CD1   1 
ATOM   9828  N  N     . ARG   B  1  124  ? 1.674   48.971  131.559 1.00 33.95 ? 122  ARG   B N     1 
ATOM   9829  C  CA    . ARG   B  1  124  ? 1.233   50.093  132.382 1.00 40.78 ? 122  ARG   B CA    1 
ATOM   9830  C  C     . ARG   B  1  124  ? 2.181   51.282  132.270 1.00 40.97 ? 122  ARG   B C     1 
ATOM   9831  O  O     . ARG   B  1  124  ? 1.738   52.436  132.292 1.00 48.79 ? 122  ARG   B O     1 
ATOM   9832  C  CB    . ARG   B  1  124  ? 1.085   49.651  133.838 1.00 43.51 ? 122  ARG   B CB    1 
ATOM   9833  N  N     . ASP   B  1  125  ? 3.484   51.026  132.143 1.00 42.63 ? 123  ASP   B N     1 
ATOM   9834  C  CA    . ASP   B  1  125  ? 4.474   52.094  132.201 1.00 47.41 ? 123  ASP   B CA    1 
ATOM   9835  C  C     . ASP   B  1  125  ? 4.966   52.562  130.838 1.00 46.75 ? 123  ASP   B C     1 
ATOM   9836  O  O     . ASP   B  1  125  ? 5.486   53.680  130.741 1.00 49.45 ? 123  ASP   B O     1 
ATOM   9837  C  CB    . ASP   B  1  125  ? 5.680   51.667  133.049 1.00 49.02 ? 123  ASP   B CB    1 
ATOM   9838  C  CG    . ASP   B  1  125  ? 5.279   51.166  134.426 1.00 53.77 ? 123  ASP   B CG    1 
ATOM   9839  O  OD1   . ASP   B  1  125  ? 4.209   51.574  134.924 1.00 53.56 ? 123  ASP   B OD1   1 
ATOM   9840  O  OD2   . ASP   B  1  125  ? 6.037   50.362  135.010 1.00 59.81 ? 123  ASP   B OD2   1 
ATOM   9841  N  N     . LYS   B  1  126  ? 4.820   51.759  129.793 1.00 39.59 ? 124  LYS   B N     1 
ATOM   9842  C  CA    . LYS   B  1  126  ? 5.357   52.158  128.497 1.00 43.87 ? 124  LYS   B CA    1 
ATOM   9843  C  C     . LYS   B  1  126  ? 4.339   52.096  127.367 1.00 43.89 ? 124  LYS   B C     1 
ATOM   9844  O  O     . LYS   B  1  126  ? 4.308   53.003  126.532 1.00 45.96 ? 124  LYS   B O     1 
ATOM   9845  C  CB    . LYS   B  1  126  ? 6.597   51.316  128.141 1.00 44.53 ? 124  LYS   B CB    1 
ATOM   9846  N  N     . ILE   B  1  127  ? 3.510   51.053  127.314 1.00 37.47 ? 125  ILE   B N     1 
ATOM   9847  C  CA    . ILE   B  1  127  ? 2.606   50.887  126.177 1.00 36.30 ? 125  ILE   B CA    1 
ATOM   9848  C  C     . ILE   B  1  127  ? 1.392   51.796  126.306 1.00 39.59 ? 125  ILE   B C     1 
ATOM   9849  O  O     . ILE   B  1  127  ? 0.994   52.459  125.342 1.00 36.91 ? 125  ILE   B O     1 
ATOM   9850  C  CB    . ILE   B  1  127  ? 2.191   49.414  126.007 1.00 32.07 ? 125  ILE   B CB    1 
ATOM   9851  C  CG1   . ILE   B  1  127  ? 3.417   48.498  126.007 1.00 35.41 ? 125  ILE   B CG1   1 
ATOM   9852  C  CG2   . ILE   B  1  127  ? 1.390   49.245  124.720 1.00 31.57 ? 125  ILE   B CG2   1 
ATOM   9853  C  CD1   . ILE   B  1  127  ? 4.442   48.859  124.973 1.00 38.33 ? 125  ILE   B CD1   1 
ATOM   9854  N  N     . ALA   B  1  128  ? 0.773   51.819  127.489 1.00 33.24 ? 126  ALA   B N     1 
ATOM   9855  C  CA    . ALA   B  1  128  ? -0.443  52.600  127.689 1.00 34.13 ? 126  ALA   B CA    1 
ATOM   9856  C  C     . ALA   B  1  128  ? -0.205  54.094  127.531 1.00 41.75 ? 126  ALA   B C     1 
ATOM   9857  O  O     . ALA   B  1  128  ? -1.150  54.832  127.232 1.00 38.56 ? 126  ALA   B O     1 
ATOM   9858  C  CB    . ALA   B  1  128  ? -1.049  52.305  129.062 1.00 36.65 ? 126  ALA   B CB    1 
ATOM   9859  N  N     . ASP   B  1  129  ? 1.028   54.553  127.724 1.00 42.43 ? 127  ASP   B N     1 
ATOM   9860  C  CA    . ASP   B  1  129  ? 1.398   55.937  127.477 1.00 52.24 ? 127  ASP   B CA    1 
ATOM   9861  C  C     . ASP   B  1  129  ? 1.746   56.202  126.015 1.00 55.46 ? 127  ASP   B C     1 
ATOM   9862  O  O     . ASP   B  1  129  ? 2.460   57.169  125.722 1.00 64.27 ? 127  ASP   B O     1 
ATOM   9863  C  CB    . ASP   B  1  129  ? 2.553   56.356  128.393 1.00 51.79 ? 127  ASP   B CB    1 
ATOM   9864  N  N     . GLY   B  1  130  ? 1.274   55.358  125.099 1.00 54.90 ? 128  GLY   B N     1 
ATOM   9865  C  CA    . GLY   B  1  130  ? 1.442   55.596  123.678 1.00 55.15 ? 128  GLY   B CA    1 
ATOM   9866  C  C     . GLY   B  1  130  ? 2.781   55.184  123.100 1.00 55.80 ? 128  GLY   B C     1 
ATOM   9867  O  O     . GLY   B  1  130  ? 2.859   54.796  121.930 1.00 53.94 ? 128  GLY   B O     1 
ATOM   9868  N  N     . ASN   B  1  131  ? 3.845   55.263  123.898 1.00 61.11 ? 129  ASN   B N     1 
ATOM   9869  C  CA    . ASN   B  1  131  ? 5.182   54.949  123.407 1.00 60.55 ? 129  ASN   B CA    1 
ATOM   9870  C  C     . ASN   B  1  131  ? 5.324   53.462  123.101 1.00 57.69 ? 129  ASN   B C     1 
ATOM   9871  O  O     . ASN   B  1  131  ? 6.151   52.773  123.709 1.00 62.71 ? 129  ASN   B O     1 
ATOM   9872  C  CB    . ASN   B  1  131  ? 6.236   55.386  124.427 1.00 60.35 ? 129  ASN   B CB    1 
ATOM   9873  N  N     . TRP   B  1  132  ? 4.527   52.957  122.157 1.00 48.97 ? 130  TRP   B N     1 
ATOM   9874  C  CA    . TRP   B  1  132  ? 4.532   51.534  121.841 1.00 42.62 ? 130  TRP   B CA    1 
ATOM   9875  C  C     . TRP   B  1  132  ? 5.568   51.157  120.792 1.00 43.37 ? 130  TRP   B C     1 
ATOM   9876  O  O     . TRP   B  1  132  ? 6.027   50.009  120.771 1.00 50.17 ? 130  TRP   B O     1 
ATOM   9877  C  CB    . TRP   B  1  132  ? 3.135   51.068  121.402 1.00 39.69 ? 130  TRP   B CB    1 
ATOM   9878  C  CG    . TRP   B  1  132  ? 2.627   51.664  120.102 1.00 32.56 ? 130  TRP   B CG    1 
ATOM   9879  C  CD1   . TRP   B  1  132  ? 1.760   52.711  119.962 1.00 31.91 ? 130  TRP   B CD1   1 
ATOM   9880  C  CD2   . TRP   B  1  132  ? 2.947   51.230  118.770 1.00 29.06 ? 130  TRP   B CD2   1 
ATOM   9881  N  NE1   . TRP   B  1  132  ? 1.522   52.957  118.627 1.00 29.13 ? 130  TRP   B NE1   1 
ATOM   9882  C  CE2   . TRP   B  1  132  ? 2.238   52.063  117.877 1.00 26.23 ? 130  TRP   B CE2   1 
ATOM   9883  C  CE3   . TRP   B  1  132  ? 3.756   50.217  118.249 1.00 27.33 ? 130  TRP   B CE3   1 
ATOM   9884  C  CZ2   . TRP   B  1  132  ? 2.326   51.920  116.495 1.00 24.97 ? 130  TRP   B CZ2   1 
ATOM   9885  C  CZ3   . TRP   B  1  132  ? 3.843   50.076  116.878 1.00 27.02 ? 130  TRP   B CZ3   1 
ATOM   9886  C  CH2   . TRP   B  1  132  ? 3.126   50.921  116.015 1.00 26.36 ? 130  TRP   B CH2   1 
ATOM   9887  N  N     . LYS   B  1  133  ? 5.947   52.093  119.919 1.00 46.21 ? 131  LYS   B N     1 
ATOM   9888  C  CA    . LYS   B  1  133  ? 6.904   51.768  118.866 1.00 49.43 ? 131  LYS   B CA    1 
ATOM   9889  C  C     . LYS   B  1  133  ? 8.262   51.391  119.447 1.00 57.34 ? 131  LYS   B C     1 
ATOM   9890  O  O     . LYS   B  1  133  ? 8.944   50.499  118.927 1.00 57.98 ? 131  LYS   B O     1 
ATOM   9891  C  CB    . LYS   B  1  133  ? 7.033   52.945  117.898 1.00 45.88 ? 131  LYS   B CB    1 
ATOM   9892  N  N     . SER   B  1  134  ? 8.662   52.047  120.538 1.00 61.79 ? 132  SER   B N     1 
ATOM   9893  C  CA    . SER   B  1  134  ? 9.986   51.815  121.106 1.00 58.75 ? 132  SER   B CA    1 
ATOM   9894  C  C     . SER   B  1  134  ? 10.084  50.437  121.750 1.00 62.61 ? 132  SER   B C     1 
ATOM   9895  O  O     . SER   B  1  134  ? 11.008  49.668  121.460 1.00 64.05 ? 132  SER   B O     1 
ATOM   9896  C  CB    . SER   B  1  134  ? 10.307  52.907  122.126 1.00 53.78 ? 132  SER   B CB    1 
ATOM   9897  N  N     . HIS   B  1  135  ? 9.132   50.106  122.626 1.00 63.78 ? 133  HIS   B N     1 
ATOM   9898  C  CA    . HIS   B  1  135  ? 9.265   48.907  123.447 1.00 63.50 ? 133  HIS   B CA    1 
ATOM   9899  C  C     . HIS   B  1  135  ? 9.137   47.626  122.631 1.00 64.35 ? 133  HIS   B C     1 
ATOM   9900  O  O     . HIS   B  1  135  ? 9.707   46.596  123.009 1.00 66.09 ? 133  HIS   B O     1 
ATOM   9901  C  CB    . HIS   B  1  135  ? 8.237   48.931  124.578 1.00 59.76 ? 133  HIS   B CB    1 
ATOM   9902  N  N     . LEU   B  1  136  ? 8.400   47.661  121.524 1.00 60.86 ? 134  LEU   B N     1 
ATOM   9903  C  CA    . LEU   B  1  136  ? 8.167   46.456  120.735 1.00 55.16 ? 134  LEU   B CA    1 
ATOM   9904  C  C     . LEU   B  1  136  ? 8.387   46.716  119.247 1.00 52.86 ? 134  LEU   B C     1 
ATOM   9905  O  O     . LEU   B  1  136  ? 9.354   46.235  118.661 1.00 55.88 ? 134  LEU   B O     1 
ATOM   9906  C  CB    . LEU   B  1  136  ? 6.748   45.935  120.969 1.00 48.59 ? 134  LEU   B CB    1 
ATOM   9907  C  CG    . LEU   B  1  136  ? 6.301   45.764  122.422 1.00 44.93 ? 134  LEU   B CG    1 
ATOM   9908  C  CD1   . LEU   B  1  136  ? 4.814   45.506  122.488 1.00 36.35 ? 134  LEU   B CD1   1 
ATOM   9909  C  CD2   . LEU   B  1  136  ? 7.070   44.642  123.104 1.00 46.60 ? 134  LEU   B CD2   1 
ATOM   9910  N  N     . ARG   B  1  140  ? 11.754  44.167  114.379 1.00 36.35 ? 138  ARG   B N     1 
ATOM   9911  C  CA    . ARG   B  1  140  ? 10.699  43.467  113.657 1.00 43.92 ? 138  ARG   B CA    1 
ATOM   9912  C  C     . ARG   B  1  140  ? 9.361   44.176  113.850 1.00 43.23 ? 138  ARG   B C     1 
ATOM   9913  O  O     . ARG   B  1  140  ? 8.989   44.522  114.974 1.00 34.21 ? 138  ARG   B O     1 
ATOM   9914  C  CB    . ARG   B  1  140  ? 10.597  42.010  114.121 1.00 41.07 ? 138  ARG   B CB    1 
ATOM   9915  N  N     . SER   B  1  141  ? 8.647   44.386  112.744 1.00 32.30 ? 139  SER   B N     1 
ATOM   9916  C  CA    . SER   B  1  141  ? 7.364   45.066  112.793 1.00 27.06 ? 139  SER   B CA    1 
ATOM   9917  C  C     . SER   B  1  141  ? 6.423   44.355  113.758 1.00 28.97 ? 139  SER   B C     1 
ATOM   9918  O  O     . SER   B  1  141  ? 6.365   43.123  113.812 1.00 28.62 ? 139  SER   B O     1 
ATOM   9919  C  CB    . SER   B  1  141  ? 6.740   45.088  111.393 1.00 29.61 ? 139  SER   B CB    1 
ATOM   9920  O  OG    . SER   B  1  141  ? 5.426   45.640  111.414 1.00 29.04 ? 139  SER   B OG    1 
ATOM   9921  N  N     . LEU   B  1  142  ? 5.689   45.148  114.533 1.00 23.41 ? 140  LEU   B N     1 
ATOM   9922  C  CA    . LEU   B  1  142  ? 4.607   44.598  115.332 1.00 23.21 ? 140  LEU   B CA    1 
ATOM   9923  C  C     . LEU   B  1  142  ? 3.593   43.860  114.473 1.00 19.91 ? 140  LEU   B C     1 
ATOM   9924  O  O     . LEU   B  1  142  ? 2.872   42.991  114.972 1.00 20.96 ? 140  LEU   B O     1 
ATOM   9925  C  CB    . LEU   B  1  142  ? 3.886   45.752  116.025 1.00 22.89 ? 140  LEU   B CB    1 
ATOM   9926  C  CG    . LEU   B  1  142  ? 3.292   45.361  117.360 1.00 26.80 ? 140  LEU   B CG    1 
ATOM   9927  C  CD1   . LEU   B  1  142  ? 4.415   45.147  118.334 1.00 30.43 ? 140  LEU   B CD1   1 
ATOM   9928  C  CD2   . LEU   B  1  142  ? 2.393   46.442  117.849 1.00 27.31 ? 140  LEU   B CD2   1 
ATOM   9929  N  N     . PHE   B  1  143  ? 3.512   44.195  113.193 1.00 19.61 ? 141  PHE   B N     1 
ATOM   9930  C  CA    . PHE   B  1  143  ? 2.409   43.779  112.349 1.00 18.81 ? 141  PHE   B CA    1 
ATOM   9931  C  C     . PHE   B  1  143  ? 2.780   42.654  111.393 1.00 19.28 ? 141  PHE   B C     1 
ATOM   9932  O  O     . PHE   B  1  143  ? 2.051   42.411  110.430 1.00 20.23 ? 141  PHE   B O     1 
ATOM   9933  C  CB    . PHE   B  1  143  ? 1.846   45.003  111.623 1.00 18.87 ? 141  PHE   B CB    1 
ATOM   9934  C  CG    . PHE   B  1  143  ? 1.543   46.143  112.549 1.00 18.77 ? 141  PHE   B CG    1 
ATOM   9935  C  CD1   . PHE   B  1  143  ? 0.639   45.974  113.584 1.00 18.60 ? 141  PHE   B CD1   1 
ATOM   9936  C  CD2   . PHE   B  1  143  ? 2.160   47.379  112.405 1.00 17.53 ? 141  PHE   B CD2   1 
ATOM   9937  C  CE1   . PHE   B  1  143  ? 0.356   47.002  114.442 1.00 19.29 ? 141  PHE   B CE1   1 
ATOM   9938  C  CE2   . PHE   B  1  143  ? 1.888   48.410  113.276 1.00 18.81 ? 141  PHE   B CE2   1 
ATOM   9939  C  CZ    . PHE   B  1  143  ? 0.980   48.227  114.287 1.00 18.05 ? 141  PHE   B CZ    1 
ATOM   9940  N  N     . VAL   B  1  144  ? 3.877   41.940  111.666 1.00 20.70 ? 142  VAL   B N     1 
ATOM   9941  C  CA    . VAL   B  1  144  ? 4.328   40.852  110.798 1.00 21.04 ? 142  VAL   B CA    1 
ATOM   9942  C  C     . VAL   B  1  144  ? 3.222   39.836  110.541 1.00 21.21 ? 142  VAL   B C     1 
ATOM   9943  O  O     . VAL   B  1  144  ? 3.070   39.340  109.418 1.00 23.20 ? 142  VAL   B O     1 
ATOM   9944  C  CB    . VAL   B  1  144  ? 5.604   40.197  111.363 1.00 23.23 ? 142  VAL   B CB    1 
ATOM   9945  C  CG1   . VAL   B  1  144  ? 5.951   38.934  110.588 1.00 27.37 ? 142  VAL   B CG1   1 
ATOM   9946  C  CG2   . VAL   B  1  144  ? 6.745   41.175  111.302 1.00 26.95 ? 142  VAL   B CG2   1 
ATOM   9947  N  N     . ASN   B  1  145  ? 2.426   39.515  111.561 1.00 21.60 ? 143  ASN   B N     1 
ATOM   9948  C  CA    . ASN   B  1  145  ? 1.367   38.525  111.413 1.00 22.61 ? 143  ASN   B CA    1 
ATOM   9949  C  C     . ASN   B  1  145  ? -0.014  39.147  111.261 1.00 21.10 ? 143  ASN   B C     1 
ATOM   9950  O  O     . ASN   B  1  145  ? -1.023  38.481  111.522 1.00 22.43 ? 143  ASN   B O     1 
ATOM   9951  C  CB    . ASN   B  1  145  ? 1.385   37.534  112.574 1.00 27.46 ? 143  ASN   B CB    1 
ATOM   9952  C  CG    . ASN   B  1  145  ? 2.526   36.556  112.470 1.00 32.53 ? 143  ASN   B CG    1 
ATOM   9953  O  OD1   . ASN   B  1  145  ? 2.820   36.040  111.387 1.00 33.46 ? 143  ASN   B OD1   1 
ATOM   9954  N  ND2   . ASN   B  1  145  ? 3.181   36.293  113.589 1.00 30.74 ? 143  ASN   B ND2   1 
ATOM   9955  N  N     . ALA   B  1  146  ? -0.084  40.407  110.835 1.00 20.00 ? 144  ALA   B N     1 
ATOM   9956  C  CA    . ALA   B  1  146  ? -1.373  41.079  110.775 1.00 22.00 ? 144  ALA   B CA    1 
ATOM   9957  C  C     . ALA   B  1  146  ? -2.316  40.476  109.741 1.00 21.73 ? 144  ALA   B C     1 
ATOM   9958  O  O     . ALA   B  1  146  ? -3.534  40.616  109.884 1.00 22.82 ? 144  ALA   B O     1 
ATOM   9959  C  CB    . ALA   B  1  146  ? -1.177  42.571  110.508 1.00 21.36 ? 144  ALA   B CB    1 
ATOM   9960  N  N     . ALA   B  1  147  ? -1.802  39.823  108.702 1.00 22.72 ? 145  ALA   B N     1 
ATOM   9961  C  CA    . ALA   B  1  147  ? -2.706  39.160  107.769 1.00 21.78 ? 145  ALA   B CA    1 
ATOM   9962  C  C     . ALA   B  1  147  ? -3.495  38.072  108.478 1.00 24.56 ? 145  ALA   B C     1 
ATOM   9963  O  O     . ALA   B  1  147  ? -4.691  37.887  108.223 1.00 24.52 ? 145  ALA   B O     1 
ATOM   9964  C  CB    . ALA   B  1  147  ? -1.930  38.575  106.592 1.00 25.46 ? 145  ALA   B CB    1 
ATOM   9965  N  N     . THR   B  1  148  ? -2.844  37.361  109.393 1.00 22.77 ? 146  THR   B N     1 
ATOM   9966  C  CA    . THR   B  1  148  ? -3.534  36.333  110.162 1.00 23.12 ? 146  THR   B CA    1 
ATOM   9967  C  C     . THR   B  1  148  ? -4.562  36.955  111.097 1.00 22.87 ? 146  THR   B C     1 
ATOM   9968  O  O     . THR   B  1  148  ? -5.717  36.520  111.142 1.00 24.61 ? 146  THR   B O     1 
ATOM   9969  C  CB    . THR   B  1  148  ? -2.512  35.497  110.931 1.00 32.35 ? 146  THR   B CB    1 
ATOM   9970  O  OG1   . THR   B  1  148  ? -1.612  34.884  109.998 1.00 32.90 ? 146  THR   B OG1   1 
ATOM   9971  C  CG2   . THR   B  1  148  ? -3.213  34.421  111.748 1.00 33.47 ? 146  THR   B CG2   1 
ATOM   9972  N  N     . TRP   B  1  149  ? -4.168  37.991  111.840 1.00 22.48 ? 147  TRP   B N     1 
ATOM   9973  C  CA    . TRP   B  1  149  ? -5.132  38.667  112.696 1.00 22.29 ? 147  TRP   B CA    1 
ATOM   9974  C  C     . TRP   B  1  149  ? -6.226  39.346  111.887 1.00 20.51 ? 147  TRP   B C     1 
ATOM   9975  O  O     . TRP   B  1  149  ? -7.363  39.455  112.363 1.00 21.48 ? 147  TRP   B O     1 
ATOM   9976  C  CB    . TRP   B  1  149  ? -4.434  39.656  113.628 1.00 20.81 ? 147  TRP   B CB    1 
ATOM   9977  C  CG    . TRP   B  1  149  ? -3.563  38.969  114.619 1.00 21.73 ? 147  TRP   B CG    1 
ATOM   9978  C  CD1   . TRP   B  1  149  ? -2.209  39.046  114.698 1.00 23.74 ? 147  TRP   B CD1   1 
ATOM   9979  C  CD2   . TRP   B  1  149  ? -3.979  38.048  115.635 1.00 24.24 ? 147  TRP   B CD2   1 
ATOM   9980  N  NE1   . TRP   B  1  149  ? -1.753  38.252  115.722 1.00 22.70 ? 147  TRP   B NE1   1 
ATOM   9981  C  CE2   . TRP   B  1  149  ? -2.818  37.627  116.312 1.00 23.62 ? 147  TRP   B CE2   1 
ATOM   9982  C  CE3   . TRP   B  1  149  ? -5.221  37.557  116.053 1.00 26.55 ? 147  TRP   B CE3   1 
ATOM   9983  C  CZ2   . TRP   B  1  149  ? -2.859  36.737  117.390 1.00 27.28 ? 147  TRP   B CZ2   1 
ATOM   9984  C  CZ3   . TRP   B  1  149  ? -5.260  36.666  117.127 1.00 27.01 ? 147  TRP   B CZ3   1 
ATOM   9985  C  CH2   . TRP   B  1  149  ? -4.085  36.270  117.780 1.00 31.35 ? 147  TRP   B CH2   1 
ATOM   9986  N  N     . GLY   B  1  150  ? -5.908  39.812  110.678 1.00 20.94 ? 148  GLY   B N     1 
ATOM   9987  C  CA    . GLY   B  1  150  ? -6.950  40.339  109.814 1.00 22.68 ? 148  GLY   B CA    1 
ATOM   9988  C  C     . GLY   B  1  150  ? -8.014  39.303  109.517 1.00 21.53 ? 148  GLY   B C     1 
ATOM   9989  O  O     . GLY   B  1  150  ? -9.213  39.598  109.537 1.00 23.58 ? 148  GLY   B O     1 
ATOM   9990  N  N     . LEU   B  1  151  ? -7.590  38.067  109.256 1.00 24.56 ? 149  LEU   B N     1 
ATOM   9991  C  CA    A LEU   B  1  151  ? -8.554  36.989  109.059 0.47 26.98 ? 149  LEU   B CA    1 
ATOM   9992  C  CA    B LEU   B  1  151  ? -8.552  36.990  109.057 0.53 26.98 ? 149  LEU   B CA    1 
ATOM   9993  C  C     . LEU   B  1  151  ? -9.381  36.758  110.315 1.00 27.22 ? 149  LEU   B C     1 
ATOM   9994  O  O     . LEU   B  1  151  ? -10.599 36.560  110.240 1.00 30.52 ? 149  LEU   B O     1 
ATOM   9995  C  CB    A LEU   B  1  151  ? -7.828  35.706  108.658 0.47 27.66 ? 149  LEU   B CB    1 
ATOM   9996  C  CB    B LEU   B  1  151  ? -7.805  35.722  108.651 0.53 27.66 ? 149  LEU   B CB    1 
ATOM   9997  C  CG    A LEU   B  1  151  ? -7.832  35.354  107.173 0.47 26.91 ? 149  LEU   B CG    1 
ATOM   9998  C  CG    B LEU   B  1  151  ? -8.598  34.561  108.061 0.53 29.00 ? 149  LEU   B CG    1 
ATOM   9999  C  CD1   A LEU   B  1  151  ? -7.017  34.096  106.935 0.47 32.18 ? 149  LEU   B CD1   1 
ATOM   10000 C  CD1   B LEU   B  1  151  ? -9.578  35.065  107.017 0.53 28.40 ? 149  LEU   B CD1   1 
ATOM   10001 C  CD2   A LEU   B  1  151  ? -9.262  35.171  106.676 0.47 28.41 ? 149  LEU   B CD2   1 
ATOM   10002 C  CD2   B LEU   B  1  151  ? -7.627  33.578  107.442 0.53 29.52 ? 149  LEU   B CD2   1 
ATOM   10003 N  N     . VAL   B  1  152  ? -8.738  36.793  111.485 1.00 26.67 ? 150  VAL   B N     1 
ATOM   10004 C  CA    . VAL   B  1  152  ? -9.456  36.580  112.739 1.00 27.55 ? 150  VAL   B CA    1 
ATOM   10005 C  C     . VAL   B  1  152  ? -10.478 37.683  112.974 1.00 26.48 ? 150  VAL   B C     1 
ATOM   10006 O  O     . VAL   B  1  152  ? -11.607 37.425  113.408 1.00 29.50 ? 150  VAL   B O     1 
ATOM   10007 C  CB    . VAL   B  1  152  ? -8.463  36.474  113.911 1.00 23.17 ? 150  VAL   B CB    1 
ATOM   10008 C  CG1   . VAL   B  1  152  ? -9.210  36.484  115.234 1.00 30.26 ? 150  VAL   B CG1   1 
ATOM   10009 C  CG2   . VAL   B  1  152  ? -7.604  35.233  113.776 1.00 29.32 ? 150  VAL   B CG2   1 
ATOM   10010 N  N     . VAL   B  1  153  ? -10.098 38.929  112.698 1.00 25.67 ? 151  VAL   B N     1 
ATOM   10011 C  CA    . VAL   B  1  153  ? -10.933 40.068  113.058 1.00 25.67 ? 151  VAL   B CA    1 
ATOM   10012 C  C     . VAL   B  1  153  ? -12.016 40.321  112.014 1.00 27.31 ? 151  VAL   B C     1 
ATOM   10013 O  O     . VAL   B  1  153  ? -13.172 40.585  112.361 1.00 26.86 ? 151  VAL   B O     1 
ATOM   10014 C  CB    . VAL   B  1  153  ? -10.044 41.304  113.287 1.00 25.95 ? 151  VAL   B CB    1 
ATOM   10015 C  CG1   . VAL   B  1  153  ? -10.901 42.551  113.495 1.00 26.76 ? 151  VAL   B CG1   1 
ATOM   10016 C  CG2   . VAL   B  1  153  ? -9.118  41.066  114.468 1.00 23.35 ? 151  VAL   B CG2   1 
ATOM   10017 N  N     . THR   B  1  154  ? -11.669 40.250  110.732 1.00 25.84 ? 152  THR   B N     1 
ATOM   10018 C  CA    . THR   B  1  154  ? -12.573 40.638  109.659 1.00 27.13 ? 152  THR   B CA    1 
ATOM   10019 C  C     . THR   B  1  154  ? -13.074 39.464  108.838 1.00 31.30 ? 152  THR   B C     1 
ATOM   10020 O  O     . THR   B  1  154  ? -14.023 39.635  108.068 1.00 34.92 ? 152  THR   B O     1 
ATOM   10021 C  CB    . THR   B  1  154  ? -11.878 41.618  108.698 1.00 29.56 ? 152  THR   B CB    1 
ATOM   10022 O  OG1   . THR   B  1  154  ? -10.931 40.904  107.896 1.00 27.89 ? 152  THR   B OG1   1 
ATOM   10023 C  CG2   . THR   B  1  154  ? -11.152 42.707  109.461 1.00 29.86 ? 152  THR   B CG2   1 
ATOM   10024 N  N     . GLY   B  1  155  ? -12.460 38.291  108.963 1.00 27.91 ? 153  GLY   B N     1 
ATOM   10025 C  CA    . GLY   B  1  155  ? -12.798 37.180  108.102 1.00 29.06 ? 153  GLY   B CA    1 
ATOM   10026 C  C     . GLY   B  1  155  ? -12.249 37.287  106.702 1.00 31.44 ? 153  GLY   B C     1 
ATOM   10027 O  O     . GLY   B  1  155  ? -12.565 36.435  105.863 1.00 34.73 ? 153  GLY   B O     1 
ATOM   10028 N  N     . LYS   B  1  156  ? -11.442 38.303  106.418 1.00 28.56 ? 154  LYS   B N     1 
ATOM   10029 C  CA    . LYS   B  1  156  ? -10.877 38.522  105.098 1.00 31.01 ? 154  LYS   B CA    1 
ATOM   10030 C  C     . LYS   B  1  156  ? -9.362  38.408  105.177 1.00 30.35 ? 154  LYS   B C     1 
ATOM   10031 O  O     . LYS   B  1  156  ? -8.752  38.800  106.177 1.00 30.83 ? 154  LYS   B O     1 
ATOM   10032 C  CB    . LYS   B  1  156  ? -11.261 39.906  104.564 1.00 38.64 ? 154  LYS   B CB    1 
ATOM   10033 N  N     . LEU   B  1  157  ? -8.758  37.869  104.126 1.00 28.68 ? 155  LEU   B N     1 
ATOM   10034 C  CA    . LEU   B  1  157  ? -7.317  37.693  104.059 1.00 30.87 ? 155  LEU   B CA    1 
ATOM   10035 C  C     . LEU   B  1  157  ? -6.735  38.676  103.057 1.00 36.67 ? 155  LEU   B C     1 
ATOM   10036 O  O     . LEU   B  1  157  ? -7.254  38.818  101.947 1.00 37.80 ? 155  LEU   B O     1 
ATOM   10037 C  CB    . LEU   B  1  157  ? -6.966  36.271  103.624 1.00 33.55 ? 155  LEU   B CB    1 
ATOM   10038 C  CG    . LEU   B  1  157  ? -5.478  36.008  103.386 1.00 38.35 ? 155  LEU   B CG    1 
ATOM   10039 C  CD1   . LEU   B  1  157  ? -4.705  36.083  104.699 1.00 36.48 ? 155  LEU   B CD1   1 
ATOM   10040 C  CD2   . LEU   B  1  157  ? -5.262  34.663  102.701 1.00 38.01 ? 155  LEU   B CD2   1 
ATOM   10041 N  N     . THR   B  1  158  ? -5.666  39.354  103.450 1.00 37.40 ? 156  THR   B N     1 
ATOM   10042 C  CA    . THR   B  1  158  ? -4.832  40.085  102.514 1.00 38.33 ? 156  THR   B CA    1 
ATOM   10043 C  C     . THR   B  1  158  ? -3.464  39.423  102.476 1.00 36.09 ? 156  THR   B C     1 
ATOM   10044 O  O     . THR   B  1  158  ? -3.030  38.793  103.445 1.00 35.39 ? 156  THR   B O     1 
ATOM   10045 C  CB    . THR   B  1  158  ? -4.670  41.548  102.928 1.00 42.67 ? 156  THR   B CB    1 
ATOM   10046 O  OG1   . THR   B  1  158  ? -3.834  41.621  104.090 1.00 43.74 ? 156  THR   B OG1   1 
ATOM   10047 C  CG2   . THR   B  1  158  ? -6.022  42.168  103.243 1.00 42.41 ? 156  THR   B CG2   1 
ATOM   10048 N  N     . SER   B  1  159  ? -2.788  39.559  101.345 1.00 31.68 ? 157  SER   B N     1 
ATOM   10049 C  CA    A SER   B  1  159  ? -1.460  38.976  101.209 0.54 32.94 ? 157  SER   B CA    1 
ATOM   10050 C  CA    B SER   B  1  159  ? -1.464  38.968  101.228 0.46 32.93 ? 157  SER   B CA    1 
ATOM   10051 C  C     . SER   B  1  159  ? -0.420  39.780  101.979 1.00 34.15 ? 157  SER   B C     1 
ATOM   10052 O  O     . SER   B  1  159  ? 0.510   39.211  102.560 1.00 31.48 ? 157  SER   B O     1 
ATOM   10053 C  CB    A SER   B  1  159  ? -1.094  38.898  99.728  0.54 32.80 ? 157  SER   B CB    1 
ATOM   10054 C  CB    B SER   B  1  159  ? -1.071  38.831  99.757  0.46 32.79 ? 157  SER   B CB    1 
ATOM   10055 O  OG    A SER   B  1  159  ? -1.712  39.958  99.019  0.54 32.38 ? 157  SER   B OG    1 
ATOM   10056 O  OG    B SER   B  1  159  ? 0.210   38.245  99.638  0.46 29.59 ? 157  SER   B OG    1 
ATOM   10057 N  N     . THR   B  1  160  ? -0.560  41.096  101.987 1.00 28.06 ? 158  THR   B N     1 
ATOM   10058 C  CA    . THR   B  1  160  ? 0.360   41.963  102.693 1.00 21.81 ? 158  THR   B CA    1 
ATOM   10059 C  C     . THR   B  1  160  ? -0.438  42.899  103.586 1.00 22.27 ? 158  THR   B C     1 
ATOM   10060 O  O     . THR   B  1  160  ? -1.673  42.957  103.541 1.00 24.44 ? 158  THR   B O     1 
ATOM   10061 C  CB    . THR   B  1  160  ? 1.247   42.750  101.721 1.00 26.44 ? 158  THR   B CB    1 
ATOM   10062 O  OG1   . THR   B  1  160  ? 0.417   43.464  100.804 1.00 29.28 ? 158  THR   B OG1   1 
ATOM   10063 C  CG2   . THR   B  1  160  ? 2.168   41.806  100.948 1.00 28.19 ? 158  THR   B CG2   1 
ATOM   10064 N  N     . VAL   B  1  161  ? 0.304   43.655  104.381 1.00 17.56 ? 159  VAL   B N     1 
ATOM   10065 C  CA    . VAL   B  1  161  ? -0.193  44.335  105.563 1.00 20.89 ? 159  VAL   B CA    1 
ATOM   10066 C  C     . VAL   B  1  161  ? 0.017   45.822  105.349 1.00 18.75 ? 159  VAL   B C     1 
ATOM   10067 O  O     . VAL   B  1  161  ? 1.117   46.245  104.978 1.00 17.22 ? 159  VAL   B O     1 
ATOM   10068 C  CB    . VAL   B  1  161  ? 0.602   43.844  106.789 1.00 24.84 ? 159  VAL   B CB    1 
ATOM   10069 C  CG1   . VAL   B  1  161  ? 0.550   44.823  107.922 1.00 28.21 ? 159  VAL   B CG1   1 
ATOM   10070 C  CG2   . VAL   B  1  161  ? 0.111   42.457  107.204 1.00 32.91 ? 159  VAL   B CG2   1 
ATOM   10071 N  N     . ASN   B  1  162  ? -1.024  46.614  105.572 1.00 17.84 ? 160  ASN   B N     1 
ATOM   10072 C  CA    . ASN   B  1  162  ? -0.826  48.056  105.524 1.00 16.97 ? 160  ASN   B CA    1 
ATOM   10073 C  C     . ASN   B  1  162  ? -0.332  48.474  106.897 1.00 17.20 ? 160  ASN   B C     1 
ATOM   10074 O  O     . ASN   B  1  162  ? -1.104  48.793  107.800 1.00 17.75 ? 160  ASN   B O     1 
ATOM   10075 C  CB    . ASN   B  1  162  ? -2.085  48.792  105.105 1.00 18.20 ? 160  ASN   B CB    1 
ATOM   10076 C  CG    . ASN   B  1  162  ? -1.851  50.276  104.962 1.00 18.43 ? 160  ASN   B CG    1 
ATOM   10077 O  OD1   . ASN   B  1  162  ? -0.900  50.816  105.519 1.00 17.94 ? 160  ASN   B OD1   1 
ATOM   10078 N  ND2   . ASN   B  1  162  ? -2.700  50.940  104.209 1.00 20.36 ? 160  ASN   B ND2   1 
ATOM   10079 N  N     . ASP   B  1  163  ? 0.993   48.472  107.043 1.00 16.94 ? 161  ASP   B N     1 
ATOM   10080 C  CA    . ASP   B  1  163  ? 1.585   48.749  108.335 1.00 15.57 ? 161  ASP   B CA    1 
ATOM   10081 C  C     . ASP   B  1  163  ? 1.439   50.201  108.752 1.00 16.60 ? 161  ASP   B C     1 
ATOM   10082 O  O     . ASP   B  1  163  ? 1.455   50.483  109.946 1.00 17.00 ? 161  ASP   B O     1 
ATOM   10083 C  CB    . ASP   B  1  163  ? 3.043   48.290  108.375 1.00 16.93 ? 161  ASP   B CB    1 
ATOM   10084 C  CG    . ASP   B  1  163  ? 3.868   48.803  107.217 1.00 18.90 ? 161  ASP   B CG    1 
ATOM   10085 O  OD1   . ASP   B  1  163  ? 3.420   48.746  106.056 1.00 17.28 ? 161  ASP   B OD1   1 
ATOM   10086 O  OD2   . ASP   B  1  163  ? 5.009   49.229  107.479 1.00 21.88 ? 161  ASP   B OD2   1 
ATOM   10087 N  N     . ARG   B  1  164  ? 1.292   51.130  107.804 1.00 15.60 ? 162  ARG   B N     1 
ATOM   10088 C  CA    . ARG   B  1  164  ? 1.036   52.507  108.208 1.00 15.73 ? 162  ARG   B CA    1 
ATOM   10089 C  C     . ARG   B  1  164  ? -0.365  52.658  108.772 1.00 15.63 ? 162  ARG   B C     1 
ATOM   10090 O  O     . ARG   B  1  164  ? -0.569  53.379  109.748 1.00 15.06 ? 162  ARG   B O     1 
ATOM   10091 C  CB    . ARG   B  1  164  ? 1.265   53.463  107.039 1.00 16.66 ? 162  ARG   B CB    1 
ATOM   10092 C  CG    . ARG   B  1  164  ? 2.711   53.481  106.541 1.00 16.62 ? 162  ARG   B CG    1 
ATOM   10093 C  CD    . ARG   B  1  164  ? 3.714   53.533  107.678 1.00 23.60 ? 162  ARG   B CD    1 
ATOM   10094 N  NE    . ARG   B  1  164  ? 3.474   54.660  108.563 1.00 31.01 ? 162  ARG   B NE    1 
ATOM   10095 C  CZ    . ARG   B  1  164  ? 3.875   54.716  109.826 1.00 34.53 ? 162  ARG   B CZ    1 
ATOM   10096 N  NH1   . ARG   B  1  164  ? 4.535   53.712  110.387 1.00 34.95 ? 162  ARG   B NH1   1 
ATOM   10097 N  NH2   . ARG   B  1  164  ? 3.604   55.802  110.541 1.00 30.20 ? 162  ARG   B NH2   1 
ATOM   10098 N  N     . SER   B  1  165  ? -1.339  52.004  108.138 1.00 16.70 ? 163  SER   B N     1 
ATOM   10099 C  CA    . SER   B  1  165  ? -2.701  52.039  108.649 1.00 14.64 ? 163  SER   B CA    1 
ATOM   10100 C  C     . SER   B  1  165  ? -2.778  51.385  110.020 1.00 15.78 ? 163  SER   B C     1 
ATOM   10101 O  O     . SER   B  1  165  ? -3.471  51.872  110.916 1.00 15.75 ? 163  SER   B O     1 
ATOM   10102 C  CB    . SER   B  1  165  ? -3.597  51.295  107.665 1.00 15.28 ? 163  SER   B CB    1 
ATOM   10103 O  OG    . SER   B  1  165  ? -4.890  51.097  108.212 1.00 17.96 ? 163  SER   B OG    1 
ATOM   10104 N  N     . LEU   B  1  166  ? -2.071  50.266  110.186 1.00 16.70 ? 164  LEU   B N     1 
ATOM   10105 C  CA    . LEU   B  1  166  ? -2.100  49.569  111.467 1.00 16.37 ? 164  LEU   B CA    1 
ATOM   10106 C  C     . LEU   B  1  166  ? -1.397  50.371  112.548 1.00 17.54 ? 164  LEU   B C     1 
ATOM   10107 O  O     . LEU   B  1  166  ? -1.847  50.389  113.688 1.00 17.56 ? 164  LEU   B O     1 
ATOM   10108 C  CB    . LEU   B  1  166  ? -1.459  48.195  111.309 1.00 17.03 ? 164  LEU   B CB    1 
ATOM   10109 C  CG    . LEU   B  1  166  ? -2.363  47.246  110.541 1.00 16.76 ? 164  LEU   B CG    1 
ATOM   10110 C  CD1   . LEU   B  1  166  ? -1.642  45.979  110.233 1.00 21.52 ? 164  LEU   B CD1   1 
ATOM   10111 C  CD2   . LEU   B  1  166  ? -3.627  46.951  111.316 1.00 17.95 ? 164  LEU   B CD2   1 
ATOM   10112 N  N     . ALA   B  1  167  ? -0.268  51.005  112.217 1.00 15.72 ? 165  ALA   B N     1 
ATOM   10113 C  CA    . ALA   B  1  167  ? 0.405   51.856  113.191 1.00 15.03 ? 165  ALA   B CA    1 
ATOM   10114 C  C     . ALA   B  1  167  ? -0.497  53.003  113.625 1.00 16.45 ? 165  ALA   B C     1 
ATOM   10115 O  O     . ALA   B  1  167  ? -0.597  53.314  114.813 1.00 18.27 ? 165  ALA   B O     1 
ATOM   10116 C  CB    . ALA   B  1  167  ? 1.700   52.398  112.588 1.00 18.54 ? 165  ALA   B CB    1 
ATOM   10117 N  N     . ALA   B  1  168  ? -1.174  53.635  112.655 1.00 16.30 ? 166  ALA   B N     1 
ATOM   10118 C  CA    . ALA   B  1  168  ? -2.109  54.704  112.972 1.00 15.66 ? 166  ALA   B CA    1 
ATOM   10119 C  C     . ALA   B  1  168  ? -3.239  54.194  113.854 1.00 14.77 ? 166  ALA   B C     1 
ATOM   10120 O  O     . ALA   B  1  168  ? -3.613  54.838  114.832 1.00 17.52 ? 166  ALA   B O     1 
ATOM   10121 C  CB    . ALA   B  1  168  ? -2.672  55.272  111.665 1.00 17.39 ? 166  ALA   B CB    1 
ATOM   10122 N  N     . ALA   B  1  169  ? -3.766  53.013  113.520 1.00 16.40 ? 167  ALA   B N     1 
ATOM   10123 C  CA    . ALA   B  1  169  ? -4.871  52.447  114.286 1.00 16.14 ? 167  ALA   B CA    1 
ATOM   10124 C  C     . ALA   B  1  169  ? -4.446  52.108  115.707 1.00 19.14 ? 167  ALA   B C     1 
ATOM   10125 O  O     . ALA   B  1  169  ? -5.203  52.329  116.654 1.00 18.33 ? 167  ALA   B O     1 
ATOM   10126 C  CB    . ALA   B  1  169  ? -5.373  51.193  113.576 1.00 18.04 ? 167  ALA   B CB    1 
ATOM   10127 N  N     . LEU   B  1  170  ? -3.241  51.559  115.871 1.00 18.80 ? 168  LEU   B N     1 
ATOM   10128 C  CA    . LEU   B  1  170  ? -2.778  51.213  117.212 1.00 15.08 ? 168  LEU   B CA    1 
ATOM   10129 C  C     . LEU   B  1  170  ? -2.557  52.458  118.052 1.00 18.69 ? 168  LEU   B C     1 
ATOM   10130 O  O     . LEU   B  1  170  ? -2.954  52.505  119.218 1.00 18.59 ? 168  LEU   B O     1 
ATOM   10131 C  CB    . LEU   B  1  170  ? -1.500  50.384  117.110 1.00 18.34 ? 168  LEU   B CB    1 
ATOM   10132 C  CG    . LEU   B  1  170  ? -1.016  49.817  118.444 1.00 17.65 ? 168  LEU   B CG    1 
ATOM   10133 C  CD1   . LEU   B  1  170  ? -2.088  48.964  119.120 1.00 20.82 ? 168  LEU   B CD1   1 
ATOM   10134 C  CD2   . LEU   B  1  170  ? 0.225   49.025  118.188 1.00 21.29 ? 168  LEU   B CD2   1 
ATOM   10135 N  N     . THR   B  1  171  ? -1.919  53.478  117.473 1.00 18.77 ? 169  THR   B N     1 
ATOM   10136 C  CA    . THR   B  1  171  ? -1.787  54.746  118.178 1.00 18.08 ? 169  THR   B CA    1 
ATOM   10137 C  C     . THR   B  1  171  ? -3.149  55.301  118.559 1.00 18.92 ? 169  THR   B C     1 
ATOM   10138 O  O     . THR   B  1  171  ? -3.349  55.766  119.686 1.00 19.74 ? 169  THR   B O     1 
ATOM   10139 C  CB    . THR   B  1  171  ? -1.034  55.739  117.298 1.00 19.26 ? 169  THR   B CB    1 
ATOM   10140 O  OG1   . THR   B  1  171  ? 0.287   55.240  117.065 1.00 23.11 ? 169  THR   B OG1   1 
ATOM   10141 C  CG2   . THR   B  1  171  ? -0.955  57.092  117.961 1.00 19.89 ? 169  THR   B CG2   1 
ATOM   10142 N  N     . ARG   B  1  172  ? -4.104  55.249  117.626 1.00 18.59 ? 170  ARG   B N     1 
ATOM   10143 C  CA    . ARG   B  1  172  ? -5.413  55.822  117.902 1.00 18.37 ? 170  ARG   B CA    1 
ATOM   10144 C  C     . ARG   B  1  172  ? -6.104  55.075  119.033 1.00 19.84 ? 170  ARG   B C     1 
ATOM   10145 O  O     . ARG   B  1  172  ? -6.639  55.688  119.956 1.00 19.99 ? 170  ARG   B O     1 
ATOM   10146 C  CB    . ARG   B  1  172  ? -6.255  55.800  116.629 1.00 19.48 ? 170  ARG   B CB    1 
ATOM   10147 C  CG    . ARG   B  1  172  ? -7.521  56.623  116.748 1.00 17.80 ? 170  ARG   B CG    1 
ATOM   10148 C  CD    . ARG   B  1  172  ? -8.407  56.428  115.516 1.00 18.04 ? 170  ARG   B CD    1 
ATOM   10149 N  NE    . ARG   B  1  172  ? -7.676  56.546  114.259 1.00 16.76 ? 170  ARG   B NE    1 
ATOM   10150 C  CZ    . ARG   B  1  172  ? -7.384  55.524  113.470 1.00 17.02 ? 170  ARG   B CZ    1 
ATOM   10151 N  NH1   . ARG   B  1  172  ? -7.720  54.285  113.788 1.00 18.02 ? 170  ARG   B NH1   1 
ATOM   10152 N  NH2   . ARG   B  1  172  ? -6.707  55.745  112.349 1.00 17.41 ? 170  ARG   B NH2   1 
ATOM   10153 N  N     . LEU   B  1  173  ? -6.089  53.743  118.984 1.00 19.98 ? 171  LEU   B N     1 
ATOM   10154 C  CA    . LEU   B  1  173  ? -6.832  53.004  120.002 1.00 18.17 ? 171  LEU   B CA    1 
ATOM   10155 C  C     . LEU   B  1  173  ? -6.193  53.135  121.374 1.00 19.87 ? 171  LEU   B C     1 
ATOM   10156 O  O     . LEU   B  1  173  ? -6.902  53.193  122.377 1.00 20.25 ? 171  LEU   B O     1 
ATOM   10157 C  CB    . LEU   B  1  173  ? -6.997  51.542  119.596 1.00 19.66 ? 171  LEU   B CB    1 
ATOM   10158 C  CG    . LEU   B  1  173  ? -5.799  50.601  119.610 1.00 19.63 ? 171  LEU   B CG    1 
ATOM   10159 C  CD1   . LEU   B  1  173  ? -5.686  49.930  120.977 1.00 22.05 ? 171  LEU   B CD1   1 
ATOM   10160 C  CD2   . LEU   B  1  173  ? -5.968  49.563  118.540 1.00 21.40 ? 171  LEU   B CD2   1 
ATOM   10161 N  N     . ILE   B  1  174  ? -4.861  53.171  121.440 1.00 19.79 ? 172  ILE   B N     1 
ATOM   10162 C  CA    . ILE   B  1  174  ? -4.218  53.321  122.739 1.00 18.43 ? 172  ILE   B CA    1 
ATOM   10163 C  C     . ILE   B  1  174  ? -4.456  54.714  123.298 1.00 22.24 ? 172  ILE   B C     1 
ATOM   10164 O  O     . ILE   B  1  174  ? -4.736  54.877  124.489 1.00 24.05 ? 172  ILE   B O     1 
ATOM   10165 C  CB    . ILE   B  1  174  ? -2.719  52.991  122.651 1.00 19.55 ? 172  ILE   B CB    1 
ATOM   10166 C  CG1   . ILE   B  1  174  ? -2.510  51.531  122.257 1.00 22.44 ? 172  ILE   B CG1   1 
ATOM   10167 C  CG2   . ILE   B  1  174  ? -2.039  53.303  123.985 1.00 23.24 ? 172  ILE   B CG2   1 
ATOM   10168 C  CD1   . ILE   B  1  174  ? -1.056  51.183  121.989 1.00 23.81 ? 172  ILE   B CD1   1 
ATOM   10169 N  N     . SER   B  1  175  ? -4.330  55.745  122.455 1.00 20.83 ? 173  SER   B N     1 
ATOM   10170 C  CA    . SER   B  1  175  ? -4.560  57.095  122.950 1.00 21.74 ? 173  SER   B CA    1 
ATOM   10171 C  C     . SER   B  1  175  ? -6.015  57.304  123.336 1.00 22.05 ? 173  SER   B C     1 
ATOM   10172 O  O     . SER   B  1  175  ? -6.311  58.159  124.168 1.00 26.27 ? 173  SER   B O     1 
ATOM   10173 C  CB    . SER   B  1  175  ? -4.141  58.130  121.908 1.00 22.89 ? 173  SER   B CB    1 
ATOM   10174 O  OG    . SER   B  1  175  ? -2.758  58.025  121.613 1.00 27.56 ? 173  SER   B OG    1 
ATOM   10175 N  N     . ARG   B  1  176  ? -6.930  56.544  122.732 1.00 21.07 ? 174  ARG   B N     1 
ATOM   10176 C  CA    . ARG   B  1  176  ? -8.341  56.702  123.064 1.00 19.98 ? 174  ARG   B CA    1 
ATOM   10177 C  C     . ARG   B  1  176  ? -8.724  55.879  124.291 1.00 22.85 ? 174  ARG   B C     1 
ATOM   10178 O  O     . ARG   B  1  176  ? -9.457  56.363  125.159 1.00 25.79 ? 174  ARG   B O     1 
ATOM   10179 C  CB    . ARG   B  1  176  ? -9.183  56.290  121.849 1.00 22.83 ? 174  ARG   B CB    1 
ATOM   10180 C  CG    . ARG   B  1  176  ? -10.684 56.558  122.001 1.00 22.96 ? 174  ARG   B CG    1 
ATOM   10181 C  CD    . ARG   B  1  176  ? -11.430 56.225  120.700 1.00 21.99 ? 174  ARG   B CD    1 
ATOM   10182 N  NE    . ARG   B  1  176  ? -11.554 54.787  120.470 1.00 23.05 ? 174  ARG   B NE    1 
ATOM   10183 C  CZ    . ARG   B  1  176  ? -10.964 54.097  119.498 1.00 25.44 ? 174  ARG   B CZ    1 
ATOM   10184 N  NH1   . ARG   B  1  176  ? -10.215 54.684  118.563 1.00 22.92 ? 174  ARG   B NH1   1 
ATOM   10185 N  NH2   . ARG   B  1  176  ? -11.138 52.778  119.448 1.00 26.60 ? 174  ARG   B NH2   1 
ATOM   10186 N  N     . CYS   B  1  177  ? -8.238  54.637  124.375 1.00 23.42 ? 175  CYS   B N     1 
ATOM   10187 C  CA    . CYS   B  1  177  ? -8.727  53.692  125.368 1.00 23.63 ? 175  CYS   B CA    1 
ATOM   10188 C  C     . CYS   B  1  177  ? -7.697  53.263  126.396 1.00 26.67 ? 175  CYS   B C     1 
ATOM   10189 O  O     . CYS   B  1  177  ? -8.086  52.702  127.423 1.00 28.68 ? 175  CYS   B O     1 
ATOM   10190 C  CB    . CYS   B  1  177  ? -9.293  52.436  124.695 1.00 23.79 ? 175  CYS   B CB    1 
ATOM   10191 S  SG    . CYS   B  1  177  ? -10.586 52.770  123.463 1.00 31.68 ? 175  CYS   B SG    1 
ATOM   10192 N  N     . GLY   B  1  178  ? -6.411  53.469  126.142 1.00 25.46 ? 176  GLY   B N     1 
ATOM   10193 C  CA    . GLY   B  1  178  ? -5.457  53.295  127.224 1.00 26.08 ? 176  GLY   B CA    1 
ATOM   10194 C  C     . GLY   B  1  178  ? -5.184  51.847  127.609 1.00 26.27 ? 176  GLY   B C     1 
ATOM   10195 O  O     . GLY   B  1  178  ? -5.401  50.900  126.852 1.00 25.30 ? 176  GLY   B O     1 
ATOM   10196 N  N     . GLU   B  1  179  ? -4.691  51.698  128.838 1.00 27.51 ? 177  GLU   B N     1 
ATOM   10197 C  CA    . GLU   B  1  179  ? -4.360  50.371  129.349 1.00 28.56 ? 177  GLU   B CA    1 
ATOM   10198 C  C     . GLU   B  1  179  ? -5.525  49.386  129.335 1.00 22.33 ? 177  GLU   B C     1 
ATOM   10199 O  O     . GLU   B  1  179  ? -5.291  48.214  128.992 1.00 24.09 ? 177  GLU   B O     1 
ATOM   10200 C  CB    . GLU   B  1  179  ? -3.723  50.482  130.742 1.00 31.57 ? 177  GLU   B CB    1 
ATOM   10201 C  CG    . GLU   B  1  179  ? -3.307  49.138  131.311 1.00 34.56 ? 177  GLU   B CG    1 
ATOM   10202 C  CD    . GLU   B  1  179  ? -2.494  49.260  132.583 1.00 45.18 ? 177  GLU   B CD    1 
ATOM   10203 O  OE1   . GLU   B  1  179  ? -2.266  50.400  133.041 1.00 49.84 ? 177  GLU   B OE1   1 
ATOM   10204 O  OE2   . GLU   B  1  179  ? -2.080  48.210  133.120 1.00 51.34 ? 177  GLU   B OE2   1 
ATOM   10205 N  N     . PRO   B  1  180  ? -6.768  49.766  129.660 1.00 23.88 ? 178  PRO   B N     1 
ATOM   10206 C  CA    . PRO   B  1  180  ? -7.844  48.759  129.666 1.00 25.52 ? 178  PRO   B CA    1 
ATOM   10207 C  C     . PRO   B  1  180  ? -8.023  48.016  128.350 1.00 27.26 ? 178  PRO   B C     1 
ATOM   10208 O  O     . PRO   B  1  180  ? -8.304  46.813  128.365 1.00 27.20 ? 178  PRO   B O     1 
ATOM   10209 C  CB    . PRO   B  1  180  ? -9.082  49.572  130.067 1.00 30.15 ? 178  PRO   B CB    1 
ATOM   10210 C  CG    . PRO   B  1  180  ? -8.529  50.676  130.903 1.00 30.07 ? 178  PRO   B CG    1 
ATOM   10211 C  CD    . PRO   B  1  180  ? -7.229  51.044  130.234 1.00 26.82 ? 178  PRO   B CD    1 
ATOM   10212 N  N     . VAL   B  1  181  ? -7.856  48.678  127.204 1.00 22.93 ? 179  VAL   B N     1 
ATOM   10213 C  CA    . VAL   B  1  181  ? -8.034  47.939  125.963 1.00 23.58 ? 179  VAL   B CA    1 
ATOM   10214 C  C     . VAL   B  1  181  ? -6.849  47.015  125.700 1.00 22.98 ? 179  VAL   B C     1 
ATOM   10215 O  O     . VAL   B  1  181  ? -7.014  45.927  125.134 1.00 24.28 ? 179  VAL   B O     1 
ATOM   10216 C  CB    . VAL   B  1  181  ? -8.338  48.871  124.771 1.00 24.15 ? 179  VAL   B CB    1 
ATOM   10217 C  CG1   . VAL   B  1  181  ? -7.103  49.662  124.364 1.00 24.37 ? 179  VAL   B CG1   1 
ATOM   10218 C  CG2   . VAL   B  1  181  ? -8.839  48.056  123.601 1.00 25.99 ? 179  VAL   B CG2   1 
ATOM   10219 N  N     . ILE   B  1  182  ? -5.644  47.432  126.096 1.00 22.80 ? 180  ILE   B N     1 
ATOM   10220 C  CA    . ILE   B  1  182  ? -4.461  46.592  125.938 1.00 23.62 ? 180  ILE   B CA    1 
ATOM   10221 C  C     . ILE   B  1  182  ? -4.600  45.330  126.777 1.00 26.12 ? 180  ILE   B C     1 
ATOM   10222 O  O     . ILE   B  1  182  ? -4.334  44.217  126.306 1.00 25.92 ? 180  ILE   B O     1 
ATOM   10223 C  CB    . ILE   B  1  182  ? -3.192  47.380  126.303 1.00 24.29 ? 180  ILE   B CB    1 
ATOM   10224 C  CG1   . ILE   B  1  182  ? -3.025  48.589  125.385 1.00 23.01 ? 180  ILE   B CG1   1 
ATOM   10225 C  CG2   . ILE   B  1  182  ? -1.970  46.471  126.219 1.00 24.04 ? 180  ILE   B CG2   1 
ATOM   10226 C  CD1   . ILE   B  1  182  ? -2.031  49.609  125.923 1.00 26.01 ? 180  ILE   B CD1   1 
ATOM   10227 N  N     . ARG   B  1  183  ? -5.021  45.494  128.034 1.00 27.01 ? 181  ARG   B N     1 
ATOM   10228 C  CA    A ARG   B  1  183  ? -5.233  44.346  128.909 0.41 30.03 ? 181  ARG   B CA    1 
ATOM   10229 C  CA    B ARG   B  1  183  ? -5.236  44.348  128.911 0.59 30.03 ? 181  ARG   B CA    1 
ATOM   10230 C  C     . ARG   B  1  183  ? -6.257  43.386  128.314 1.00 29.33 ? 181  ARG   B C     1 
ATOM   10231 O  O     . ARG   B  1  183  ? -6.033  42.171  128.271 1.00 30.49 ? 181  ARG   B O     1 
ATOM   10232 C  CB    A ARG   B  1  183  ? -5.659  44.836  130.295 0.41 29.75 ? 181  ARG   B CB    1 
ATOM   10233 C  CB    B ARG   B  1  183  ? -5.681  44.840  130.289 0.59 29.70 ? 181  ARG   B CB    1 
ATOM   10234 C  CG    A ARG   B  1  183  ? -6.478  43.854  131.120 0.41 34.42 ? 181  ARG   B CG    1 
ATOM   10235 C  CG    B ARG   B  1  183  ? -6.478  43.835  131.108 0.59 34.45 ? 181  ARG   B CG    1 
ATOM   10236 C  CD    A ARG   B  1  183  ? -5.645  42.726  131.718 0.41 38.31 ? 181  ARG   B CD    1 
ATOM   10237 C  CD    B ARG   B  1  183  ? -5.593  42.960  131.985 0.59 38.69 ? 181  ARG   B CD    1 
ATOM   10238 N  NE    A ARG   B  1  183  ? -4.228  43.046  131.842 0.41 35.66 ? 181  ARG   B NE    1 
ATOM   10239 N  NE    B ARG   B  1  183  ? -4.842  41.967  131.224 0.59 33.97 ? 181  ARG   B NE    1 
ATOM   10240 C  CZ    A ARG   B  1  183  ? -3.257  42.337  131.283 0.41 36.07 ? 181  ARG   B CZ    1 
ATOM   10241 C  CZ    B ARG   B  1  183  ? -3.518  41.890  131.194 0.59 35.73 ? 181  ARG   B CZ    1 
ATOM   10242 N  NH1   A ARG   B  1  183  ? -3.517  41.257  130.564 0.41 34.09 ? 181  ARG   B NH1   1 
ATOM   10243 N  NH1   B ARG   B  1  183  ? -2.760  42.749  131.858 0.59 35.73 ? 181  ARG   B NH1   1 
ATOM   10244 N  NH2   A ARG   B  1  183  ? -1.993  42.714  131.459 0.41 36.92 ? 181  ARG   B NH2   1 
ATOM   10245 N  NH2   B ARG   B  1  183  ? -2.941  40.919  130.494 0.59 36.42 ? 181  ARG   B NH2   1 
ATOM   10246 N  N     . ARG   B  1  184  ? -7.385  43.916  127.833 1.00 28.74 ? 182  ARG   B N     1 
ATOM   10247 C  CA    . ARG   B  1  184  ? -8.398  43.063  127.218 1.00 28.70 ? 182  ARG   B CA    1 
ATOM   10248 C  C     . ARG   B  1  184  ? -7.858  42.364  125.979 1.00 30.06 ? 182  ARG   B C     1 
ATOM   10249 O  O     . ARG   B  1  184  ? -8.139  41.181  125.753 1.00 30.02 ? 182  ARG   B O     1 
ATOM   10250 C  CB    . ARG   B  1  184  ? -9.641  43.883  126.868 1.00 33.03 ? 182  ARG   B CB    1 
ATOM   10251 C  CG    . ARG   B  1  184  ? -10.525 44.220  128.060 1.00 36.36 ? 182  ARG   B CG    1 
ATOM   10252 C  CD    . ARG   B  1  184  ? -11.539 43.116  128.342 1.00 40.16 ? 182  ARG   B CD    1 
ATOM   10253 N  NE    . ARG   B  1  184  ? -12.718 43.214  127.487 1.00 36.43 ? 182  ARG   B NE    1 
ATOM   10254 C  CZ    . ARG   B  1  184  ? -13.105 42.289  126.617 1.00 36.30 ? 182  ARG   B CZ    1 
ATOM   10255 N  NH1   . ARG   B  1  184  ? -12.428 41.162  126.455 1.00 40.43 ? 182  ARG   B NH1   1 
ATOM   10256 N  NH2   . ARG   B  1  184  ? -14.201 42.499  125.893 1.00 36.98 ? 182  ARG   B NH2   1 
ATOM   10257 N  N     . GLY   B  1  185  ? -7.092  43.080  125.154 1.00 28.45 ? 183  GLY   B N     1 
ATOM   10258 C  CA    . GLY   B  1  185  ? -6.516  42.454  123.978 1.00 26.26 ? 183  GLY   B CA    1 
ATOM   10259 C  C     . GLY   B  1  185  ? -5.541  41.349  124.328 1.00 27.83 ? 183  GLY   B C     1 
ATOM   10260 O  O     . GLY   B  1  185  ? -5.550  40.282  123.711 1.00 25.98 ? 183  GLY   B O     1 
ATOM   10261 N  N     . VAL   B  1  186  ? -4.689  41.592  125.326 1.00 24.37 ? 184  VAL   B N     1 
ATOM   10262 C  CA    . VAL   B  1  186  ? -3.725  40.580  125.751 1.00 27.94 ? 184  VAL   B CA    1 
ATOM   10263 C  C     . VAL   B  1  186  ? -4.446  39.340  126.261 1.00 27.53 ? 184  VAL   B C     1 
ATOM   10264 O  O     . VAL   B  1  186  ? -4.129  38.210  125.872 1.00 27.09 ? 184  VAL   B O     1 
ATOM   10265 C  CB    . VAL   B  1  186  ? -2.771  41.161  126.808 1.00 26.01 ? 184  VAL   B CB    1 
ATOM   10266 C  CG1   . VAL   B  1  186  ? -2.004  40.043  127.501 1.00 28.36 ? 184  VAL   B CG1   1 
ATOM   10267 C  CG2   . VAL   B  1  186  ? -1.815  42.150  126.169 1.00 26.35 ? 184  VAL   B CG2   1 
ATOM   10268 N  N     . ASP   B  1  187  ? -5.431  39.536  127.137 1.00 27.09 ? 185  ASP   B N     1 
ATOM   10269 C  CA    . ASP   B  1  187  ? -6.198  38.404  127.649 1.00 29.73 ? 185  ASP   B CA    1 
ATOM   10270 C  C     . ASP   B  1  187  ? -6.895  37.660  126.523 1.00 31.37 ? 185  ASP   B C     1 
ATOM   10271 O  O     . ASP   B  1  187  ? -6.947  36.425  126.526 1.00 30.20 ? 185  ASP   B O     1 
ATOM   10272 C  CB    . ASP   B  1  187  ? -7.209  38.881  128.689 1.00 30.24 ? 185  ASP   B CB    1 
ATOM   10273 C  CG    . ASP   B  1  187  ? -6.538  39.436  129.931 1.00 34.98 ? 185  ASP   B CG    1 
ATOM   10274 O  OD1   . ASP   B  1  187  ? -5.326  39.181  130.112 1.00 37.59 ? 185  ASP   B OD1   1 
ATOM   10275 O  OD2   . ASP   B  1  187  ? -7.212  40.125  130.721 1.00 35.45 ? 185  ASP   B OD2   1 
ATOM   10276 N  N     . MET   B  1  188  ? -7.420  38.395  125.540 1.00 30.70 ? 186  MET   B N     1 
ATOM   10277 C  CA    . MET   B  1  188  ? -8.109  37.765  124.421 1.00 30.67 ? 186  MET   B CA    1 
ATOM   10278 C  C     . MET   B  1  188  ? -7.144  36.937  123.582 1.00 29.01 ? 186  MET   B C     1 
ATOM   10279 O  O     . MET   B  1  188  ? -7.430  35.782  123.244 1.00 31.34 ? 186  MET   B O     1 
ATOM   10280 C  CB    . MET   B  1  188  ? -8.774  38.841  123.566 1.00 32.20 ? 186  MET   B CB    1 
ATOM   10281 C  CG    . MET   B  1  188  ? -9.530  38.307  122.372 1.00 35.65 ? 186  MET   B CG    1 
ATOM   10282 S  SD    . MET   B  1  188  ? -10.889 37.245  122.883 1.00 52.66 ? 186  MET   B SD    1 
ATOM   10283 C  CE    . MET   B  1  188  ? -11.721 38.302  124.072 1.00 43.25 ? 186  MET   B CE    1 
ATOM   10284 N  N     . ALA   B  1  189  ? -5.996  37.515  123.227 1.00 29.60 ? 187  ALA   B N     1 
ATOM   10285 C  CA    . ALA   B  1  189  ? -5.029  36.780  122.419 1.00 28.96 ? 187  ALA   B CA    1 
ATOM   10286 C  C     . ALA   B  1  189  ? -4.491  35.573  123.176 1.00 30.25 ? 187  ALA   B C     1 
ATOM   10287 O  O     . ALA   B  1  189  ? -4.265  34.509  122.588 1.00 28.67 ? 187  ALA   B O     1 
ATOM   10288 C  CB    . ALA   B  1  189  ? -3.893  37.708  121.998 1.00 29.98 ? 187  ALA   B CB    1 
ATOM   10289 N  N     . MET   B  1  190  ? -4.288  35.720  124.485 1.00 27.64 ? 188  MET   B N     1 
ATOM   10290 C  CA    . MET   B  1  190  ? -3.824  34.601  125.298 1.00 30.18 ? 188  MET   B CA    1 
ATOM   10291 C  C     . MET   B  1  190  ? -4.799  33.431  125.224 1.00 32.64 ? 188  MET   B C     1 
ATOM   10292 O  O     . MET   B  1  190  ? -4.393  32.281  125.021 1.00 31.12 ? 188  MET   B O     1 
ATOM   10293 C  CB    . MET   B  1  190  ? -3.641  35.059  126.744 1.00 32.47 ? 188  MET   B CB    1 
ATOM   10294 C  CG    . MET   B  1  190  ? -2.872  34.082  127.596 1.00 37.28 ? 188  MET   B CG    1 
ATOM   10295 S  SD    . MET   B  1  190  ? -2.834  34.599  129.319 1.00 41.79 ? 188  MET   B SD    1 
ATOM   10296 C  CE    . MET   B  1  190  ? -2.202  36.271  129.175 1.00 36.30 ? 188  MET   B CE    1 
ATOM   10297 N  N     . ARG   B  1  191  ? -6.094  33.706  125.381 1.00 28.88 ? 189  ARG   B N     1 
ATOM   10298 C  CA    . ARG   B  1  191  ? -7.085  32.637  125.309 1.00 31.04 ? 189  ARG   B CA    1 
ATOM   10299 C  C     . ARG   B  1  191  ? -7.140  32.035  123.910 1.00 32.63 ? 189  ARG   B C     1 
ATOM   10300 O  O     . ARG   B  1  191  ? -7.179  30.809  123.752 1.00 32.14 ? 189  ARG   B O     1 
ATOM   10301 C  CB    . ARG   B  1  191  ? -8.460  33.160  125.732 1.00 30.63 ? 189  ARG   B CB    1 
ATOM   10302 N  N     . MET   B  1  192  ? -7.136  32.883  122.881 1.00 28.84 ? 190  MET   B N     1 
ATOM   10303 C  CA    . MET   B  1  192  ? -7.230  32.378  121.517 1.00 29.07 ? 190  MET   B CA    1 
ATOM   10304 C  C     . MET   B  1  192  ? -6.024  31.518  121.169 1.00 31.26 ? 190  MET   B C     1 
ATOM   10305 O  O     . MET   B  1  192  ? -6.165  30.397  120.664 1.00 29.36 ? 190  MET   B O     1 
ATOM   10306 C  CB    . MET   B  1  192  ? -7.361  33.540  120.531 1.00 30.89 ? 190  MET   B CB    1 
ATOM   10307 C  CG    . MET   B  1  192  ? -8.592  34.408  120.747 1.00 36.46 ? 190  MET   B CG    1 
ATOM   10308 S  SD    . MET   B  1  192  ? -8.830  35.568  119.390 1.00 45.51 ? 190  MET   B SD    1 
ATOM   10309 C  CE    . MET   B  1  192  ? -9.337  34.426  118.118 1.00 35.76 ? 190  MET   B CE    1 
ATOM   10310 N  N     . MET   B  1  193  ? -4.824  32.023  121.436 1.00 29.21 ? 191  MET   B N     1 
ATOM   10311 C  CA    A MET   B  1  193  ? -3.606  31.309  121.075 0.47 30.52 ? 191  MET   B CA    1 
ATOM   10312 C  CA    B MET   B  1  193  ? -3.636  31.279  121.053 0.53 30.49 ? 191  MET   B CA    1 
ATOM   10313 C  C     . MET   B  1  193  ? -3.296  30.163  122.026 1.00 31.40 ? 191  MET   B C     1 
ATOM   10314 O  O     . MET   B  1  193  ? -2.540  29.258  121.661 1.00 30.66 ? 191  MET   B O     1 
ATOM   10315 C  CB    A MET   B  1  193  ? -2.414  32.272  121.044 0.47 32.92 ? 191  MET   B CB    1 
ATOM   10316 C  CB    B MET   B  1  193  ? -2.448  32.219  120.873 0.53 32.98 ? 191  MET   B CB    1 
ATOM   10317 C  CG    A MET   B  1  193  ? -2.615  33.501  120.165 0.47 29.91 ? 191  MET   B CG    1 
ATOM   10318 C  CG    B MET   B  1  193  ? -2.577  33.081  119.640 0.53 31.26 ? 191  MET   B CG    1 
ATOM   10319 S  SD    A MET   B  1  193  ? -1.244  34.674  120.267 0.47 29.36 ? 191  MET   B SD    1 
ATOM   10320 S  SD    B MET   B  1  193  ? -1.045  33.917  119.240 0.53 31.98 ? 191  MET   B SD    1 
ATOM   10321 C  CE    A MET   B  1  193  ? -0.233  34.128  118.896 0.47 36.97 ? 191  MET   B CE    1 
ATOM   10322 C  CE    B MET   B  1  193  ? -0.893  35.026  120.637 0.53 31.27 ? 191  MET   B CE    1 
ATOM   10323 N  N     . GLY   B  1  194  ? -3.847  30.191  123.234 1.00 30.35 ? 192  GLY   B N     1 
ATOM   10324 C  CA    . GLY   B  1  194  ? -3.536  29.165  124.204 1.00 32.34 ? 192  GLY   B CA    1 
ATOM   10325 C  C     . GLY   B  1  194  ? -4.586  28.081  124.307 1.00 28.15 ? 192  GLY   B C     1 
ATOM   10326 O  O     . GLY   B  1  194  ? -4.280  26.962  124.732 1.00 30.53 ? 192  GLY   B O     1 
ATOM   10327 N  N     . GLU   B  1  195  ? -5.827  28.395  123.931 1.00 28.62 ? 193  GLU   B N     1 
ATOM   10328 C  CA    . GLU   B  1  195  ? -6.949  27.494  124.177 1.00 31.88 ? 193  GLU   B CA    1 
ATOM   10329 C  C     . GLU   B  1  195  ? -7.842  27.237  122.974 1.00 30.53 ? 193  GLU   B C     1 
ATOM   10330 O  O     . GLU   B  1  195  ? -8.525  26.207  122.958 1.00 28.02 ? 193  GLU   B O     1 
ATOM   10331 C  CB    . GLU   B  1  195  ? -7.824  28.005  125.335 1.00 33.14 ? 193  GLU   B CB    1 
ATOM   10332 C  CG    . GLU   B  1  195  ? -7.079  28.230  126.639 1.00 41.21 ? 193  GLU   B CG    1 
ATOM   10333 C  CD    . GLU   B  1  195  ? -7.914  28.983  127.658 1.00 44.72 ? 193  GLU   B CD    1 
ATOM   10334 O  OE1   . GLU   B  1  195  ? -9.140  28.745  127.717 1.00 50.12 ? 193  GLU   B OE1   1 
ATOM   10335 O  OE2   . GLU   B  1  195  ? -7.345  29.824  128.388 1.00 50.85 ? 193  GLU   B OE2   1 
ATOM   10336 N  N     . GLN   B  1  196  ? -7.876  28.121  121.979 1.00 29.46 ? 194  GLN   B N     1 
ATOM   10337 C  CA    . GLN   B  1  196  ? -8.739  27.938  120.817 1.00 29.54 ? 194  GLN   B CA    1 
ATOM   10338 C  C     . GLN   B  1  196  ? -7.968  27.466  119.590 1.00 31.01 ? 194  GLN   B C     1 
ATOM   10339 O  O     . GLN   B  1  196  ? -8.336  26.460  118.978 1.00 34.64 ? 194  GLN   B O     1 
ATOM   10340 C  CB    . GLN   B  1  196  ? -9.503  29.231  120.504 1.00 31.66 ? 194  GLN   B CB    1 
ATOM   10341 N  N     . PHE   B  1  197  ? -6.897  28.169  119.220 1.00 28.86 ? 195  PHE   B N     1 
ATOM   10342 C  CA    . PHE   B  1  197  ? -6.108  27.751  118.066 1.00 30.03 ? 195  PHE   B CA    1 
ATOM   10343 C  C     . PHE   B  1  197  ? -5.364  26.459  118.347 1.00 31.26 ? 195  PHE   B C     1 
ATOM   10344 O  O     . PHE   B  1  197  ? -5.040  25.712  117.417 1.00 30.87 ? 195  PHE   B O     1 
ATOM   10345 C  CB    . PHE   B  1  197  ? -5.109  28.841  117.687 1.00 32.50 ? 195  PHE   B CB    1 
ATOM   10346 C  CG    . PHE   B  1  197  ? -5.749  30.132  117.264 1.00 31.03 ? 195  PHE   B CG    1 
ATOM   10347 C  CD1   . PHE   B  1  197  ? -7.017  30.143  116.710 1.00 34.65 ? 195  PHE   B CD1   1 
ATOM   10348 C  CD2   . PHE   B  1  197  ? -5.079  31.333  117.425 1.00 33.06 ? 195  PHE   B CD2   1 
ATOM   10349 C  CE1   . PHE   B  1  197  ? -7.604  31.333  116.316 1.00 37.74 ? 195  PHE   B CE1   1 
ATOM   10350 C  CE2   . PHE   B  1  197  ? -5.662  32.525  117.038 1.00 36.35 ? 195  PHE   B CE2   1 
ATOM   10351 C  CZ    . PHE   B  1  197  ? -6.925  32.522  116.486 1.00 32.97 ? 195  PHE   B CZ    1 
ATOM   10352 N  N     . VAL   B  1  198  ? -5.053  26.198  119.610 1.00 29.34 ? 196  VAL   B N     1 
ATOM   10353 C  CA    . VAL   B  1  198  ? -4.447  24.945  120.023 1.00 27.40 ? 196  VAL   B CA    1 
ATOM   10354 C  C     . VAL   B  1  198  ? -5.218  24.432  121.223 1.00 26.61 ? 196  VAL   B C     1 
ATOM   10355 O  O     . VAL   B  1  198  ? -5.820  25.200  121.981 1.00 29.01 ? 196  VAL   B O     1 
ATOM   10356 C  CB    . VAL   B  1  198  ? -2.949  25.085  120.384 1.00 24.75 ? 196  VAL   B CB    1 
ATOM   10357 C  CG1   . VAL   B  1  198  ? -2.144  25.507  119.182 1.00 29.05 ? 196  VAL   B CG1   1 
ATOM   10358 C  CG2   . VAL   B  1  198  ? -2.768  26.069  121.532 1.00 30.11 ? 196  VAL   B CG2   1 
ATOM   10359 N  N     . THR   B  1  199  ? -5.213  23.117  121.388 1.00 28.47 ? 197  THR   B N     1 
ATOM   10360 C  CA    A THR   B  1  199  ? -5.765  22.540  122.601 0.63 27.85 ? 197  THR   B CA    1 
ATOM   10361 C  CA    B THR   B  1  199  ? -5.771  22.553  122.606 0.37 27.84 ? 197  THR   B CA    1 
ATOM   10362 C  C     . THR   B  1  199  ? -4.841  22.752  123.791 1.00 27.95 ? 197  THR   B C     1 
ATOM   10363 O  O     . THR   B  1  199  ? -5.306  22.753  124.932 1.00 30.61 ? 197  THR   B O     1 
ATOM   10364 C  CB    A THR   B  1  199  ? -6.057  21.059  122.371 0.63 27.53 ? 197  THR   B CB    1 
ATOM   10365 C  CB    B THR   B  1  199  ? -6.087  21.073  122.414 0.37 27.51 ? 197  THR   B CB    1 
ATOM   10366 O  OG1   A THR   B  1  199  ? -6.738  20.911  121.119 0.63 26.40 ? 197  THR   B OG1   1 
ATOM   10367 O  OG1   B THR   B  1  199  ? -6.577  20.521  123.642 0.37 29.39 ? 197  THR   B OG1   1 
ATOM   10368 C  CG2   A THR   B  1  199  ? -6.941  20.507  123.473 0.63 29.16 ? 197  THR   B CG2   1 
ATOM   10369 C  CG2   B THR   B  1  199  ? -4.847  20.332  121.996 0.37 24.39 ? 197  THR   B CG2   1 
ATOM   10370 N  N     . GLY   B  1  200  ? -3.552  22.946  123.542 1.00 24.54 ? 198  GLY   B N     1 
ATOM   10371 C  CA    . GLY   B  1  200  ? -2.594  23.220  124.591 1.00 26.67 ? 198  GLY   B CA    1 
ATOM   10372 C  C     . GLY   B  1  200  ? -1.252  23.530  123.974 1.00 26.94 ? 198  GLY   B C     1 
ATOM   10373 O  O     . GLY   B  1  200  ? -1.010  23.239  122.798 1.00 25.27 ? 198  GLY   B O     1 
ATOM   10374 N  N     . GLU   B  1  201  ? -0.383  24.142  124.783 1.00 28.08 ? 199  GLU   B N     1 
ATOM   10375 C  CA    . GLU   B  1  201  ? 0.964   24.453  124.315 1.00 30.27 ? 199  GLU   B CA    1 
ATOM   10376 C  C     . GLU   B  1  201  ? 1.868   23.232  124.323 1.00 29.12 ? 199  GLU   B C     1 
ATOM   10377 O  O     . GLU   B  1  201  ? 2.819   23.165  123.538 1.00 35.97 ? 199  GLU   B O     1 
ATOM   10378 C  CB    . GLU   B  1  201  ? 1.590   25.548  125.176 1.00 36.34 ? 199  GLU   B CB    1 
ATOM   10379 C  CG    . GLU   B  1  201  ? 0.944   26.904  125.014 1.00 44.04 ? 199  GLU   B CG    1 
ATOM   10380 C  CD    . GLU   B  1  201  ? 1.723   27.989  125.722 1.00 53.86 ? 199  GLU   B CD    1 
ATOM   10381 O  OE1   . GLU   B  1  201  ? 2.647   27.644  126.495 1.00 45.79 ? 199  GLU   B OE1   1 
ATOM   10382 O  OE2   . GLU   B  1  201  ? 1.416   29.179  125.501 1.00 56.84 ? 199  GLU   B OE2   1 
ATOM   10383 N  N     . THR   B  1  202  ? 1.608   22.281  125.209 1.00 24.97 ? 200  THR   B N     1 
ATOM   10384 C  CA    . THR   B  1  202  ? 2.374   21.052  125.300 1.00 26.03 ? 200  THR   B CA    1 
ATOM   10385 C  C     . THR   B  1  202  ? 1.400   19.889  125.244 1.00 27.01 ? 200  THR   B C     1 
ATOM   10386 O  O     . THR   B  1  202  ? 0.199   20.050  125.490 1.00 25.11 ? 200  THR   B O     1 
ATOM   10387 C  CB    . THR   B  1  202  ? 3.124   20.958  126.629 1.00 29.18 ? 200  THR   B CB    1 
ATOM   10388 O  OG1   . THR   B  1  202  ? 2.180   20.806  127.695 1.00 28.36 ? 200  THR   B OG1   1 
ATOM   10389 C  CG2   . THR   B  1  202  ? 3.951   22.210  126.874 1.00 33.81 ? 200  THR   B CG2   1 
ATOM   10390 N  N     . ILE   B  1  203  ? 1.926   18.709  124.915 1.00 22.30 ? 201  ILE   B N     1 
ATOM   10391 C  CA    . ILE   B  1  203  ? 1.059   17.539  124.832 1.00 24.39 ? 201  ILE   B CA    1 
ATOM   10392 C  C     . ILE   B  1  203  ? 0.484   17.215  126.204 1.00 28.37 ? 201  ILE   B C     1 
ATOM   10393 O  O     . ILE   B  1  203  ? -0.682  16.825  126.330 1.00 24.13 ? 201  ILE   B O     1 
ATOM   10394 C  CB    . ILE   B  1  203  ? 1.791   16.350  124.181 1.00 23.23 ? 201  ILE   B CB    1 
ATOM   10395 C  CG1   . ILE   B  1  203  ? 0.807   15.203  123.922 1.00 24.03 ? 201  ILE   B CG1   1 
ATOM   10396 C  CG2   . ILE   B  1  203  ? 2.961   15.875  125.051 1.00 26.23 ? 201  ILE   B CG2   1 
ATOM   10397 C  CD1   . ILE   B  1  203  ? -0.280  15.545  122.891 1.00 22.44 ? 201  ILE   B CD1   1 
ATOM   10398 N  N     . ARG   B  1  204  ? 1.280   17.431  127.255 1.00 26.17 ? 202  ARG   B N     1 
ATOM   10399 C  CA    . ARG   B  1  204  ? 0.815   17.275  128.630 1.00 29.72 ? 202  ARG   B CA    1 
ATOM   10400 C  C     . ARG   B  1  204  ? -0.454  18.084  128.873 1.00 24.95 ? 202  ARG   B C     1 
ATOM   10401 O  O     . ARG   B  1  204  ? -1.459  17.564  129.382 1.00 27.24 ? 202  ARG   B O     1 
ATOM   10402 C  CB    . ARG   B  1  204  ? 1.927   17.775  129.556 1.00 33.84 ? 202  ARG   B CB    1 
ATOM   10403 C  CG    . ARG   B  1  204  ? 2.008   17.113  130.888 1.00 44.08 ? 202  ARG   B CG    1 
ATOM   10404 C  CD    . ARG   B  1  204  ? 3.324   17.471  131.573 1.00 35.42 ? 202  ARG   B CD    1 
ATOM   10405 N  NE    . ARG   B  1  204  ? 3.416   18.883  131.930 1.00 29.53 ? 202  ARG   B NE    1 
ATOM   10406 C  CZ    . ARG   B  1  204  ? 2.777   19.434  132.953 1.00 35.31 ? 202  ARG   B CZ    1 
ATOM   10407 N  NH1   . ARG   B  1  204  ? 1.922   18.742  133.688 1.00 34.58 ? 202  ARG   B NH1   1 
ATOM   10408 N  NH2   . ARG   B  1  204  ? 3.005   20.711  133.250 1.00 32.22 ? 202  ARG   B NH2   1 
ATOM   10409 N  N     . GLU   B  1  205  ? -0.413  19.370  128.522 1.00 25.68 ? 203  GLU   B N     1 
ATOM   10410 C  CA    . GLU   B  1  205  ? -1.547  20.256  128.740 1.00 26.63 ? 203  GLU   B CA    1 
ATOM   10411 C  C     . GLU   B  1  205  ? -2.723  19.852  127.865 1.00 26.74 ? 203  GLU   B C     1 
ATOM   10412 O  O     . GLU   B  1  205  ? -3.868  19.819  128.330 1.00 27.93 ? 203  GLU   B O     1 
ATOM   10413 C  CB    . GLU   B  1  205  ? -1.133  21.694  128.434 1.00 28.45 ? 203  GLU   B CB    1 
ATOM   10414 C  CG    . GLU   B  1  205  ? -2.210  22.731  128.711 1.00 29.35 ? 203  GLU   B CG    1 
ATOM   10415 C  CD    . GLU   B  1  205  ? -1.714  24.155  128.515 1.00 40.92 ? 203  GLU   B CD    1 
ATOM   10416 O  OE1   . GLU   B  1  205  ? -1.268  24.488  127.398 1.00 38.40 ? 203  GLU   B OE1   1 
ATOM   10417 O  OE2   . GLU   B  1  205  ? -1.762  24.945  129.482 1.00 50.95 ? 203  GLU   B OE2   1 
ATOM   10418 N  N     . ALA   B  1  206  ? -2.450  19.528  126.605 1.00 22.96 ? 204  ALA   B N     1 
ATOM   10419 C  CA    . ALA   B  1  206  ? -3.503  19.120  125.686 1.00 22.30 ? 204  ALA   B CA    1 
ATOM   10420 C  C     . ALA   B  1  206  ? -4.224  17.892  126.210 1.00 24.66 ? 204  ALA   B C     1 
ATOM   10421 O  O     . ALA   B  1  206  ? -5.460  17.837  126.216 1.00 24.63 ? 204  ALA   B O     1 
ATOM   10422 C  CB    . ALA   B  1  206  ? -2.885  18.821  124.325 1.00 23.07 ? 204  ALA   B CB    1 
ATOM   10423 N  N     . LEU   B  1  207  ? -3.459  16.900  126.672 1.00 23.08 ? 205  LEU   B N     1 
ATOM   10424 C  CA    . LEU   B  1  207  ? -4.054  15.682  127.209 1.00 24.63 ? 205  LEU   B CA    1 
ATOM   10425 C  C     . LEU   B  1  207  ? -4.909  15.974  128.433 1.00 27.68 ? 205  LEU   B C     1 
ATOM   10426 O  O     . LEU   B  1  207  ? -6.006  15.421  128.578 1.00 27.99 ? 205  LEU   B O     1 
ATOM   10427 C  CB    . LEU   B  1  207  ? -2.959  14.669  127.542 1.00 26.02 ? 205  LEU   B CB    1 
ATOM   10428 C  CG    . LEU   B  1  207  ? -2.305  14.041  126.311 1.00 29.08 ? 205  LEU   B CG    1 
ATOM   10429 C  CD1   . LEU   B  1  207  ? -1.045  13.279  126.692 1.00 28.59 ? 205  LEU   B CD1   1 
ATOM   10430 C  CD2   . LEU   B  1  207  ? -3.291  13.121  125.610 1.00 25.64 ? 205  LEU   B CD2   1 
ATOM   10431 N  N     . LYS   B  1  208  ? -4.423  16.834  129.334 1.00 23.97 ? 206  LYS   B N     1 
ATOM   10432 C  CA    . LYS   B  1  208  ? -5.205  17.173  130.519 1.00 26.53 ? 206  LYS   B CA    1 
ATOM   10433 C  C     . LYS   B  1  208  ? -6.505  17.877  130.140 1.00 27.03 ? 206  LYS   B C     1 
ATOM   10434 O  O     . LYS   B  1  208  ? -7.561  17.609  130.726 1.00 29.68 ? 206  LYS   B O     1 
ATOM   10435 C  CB    . LYS   B  1  208  ? -4.370  18.030  131.475 1.00 29.88 ? 206  LYS   B CB    1 
ATOM   10436 N  N     . ARG   B  1  209  ? -6.455  18.763  129.149 1.00 27.78 ? 207  ARG   B N     1 
ATOM   10437 C  CA    . ARG   B  1  209  ? -7.651  19.486  128.739 1.00 27.34 ? 207  ARG   B CA    1 
ATOM   10438 C  C     . ARG   B  1  209  ? -8.610  18.625  127.934 1.00 31.91 ? 207  ARG   B C     1 
ATOM   10439 O  O     . ARG   B  1  209  ? -9.761  19.026  127.736 1.00 31.37 ? 207  ARG   B O     1 
ATOM   10440 C  CB    . ARG   B  1  209  ? -7.267  20.714  127.928 1.00 29.09 ? 207  ARG   B CB    1 
ATOM   10441 C  CG    . ARG   B  1  209  ? -6.502  21.738  128.737 1.00 31.38 ? 207  ARG   B CG    1 
ATOM   10442 C  CD    . ARG   B  1  209  ? -6.147  22.912  127.876 1.00 31.54 ? 207  ARG   B CD    1 
ATOM   10443 N  NE    . ARG   B  1  209  ? -5.564  24.007  128.636 1.00 40.49 ? 207  ARG   B NE    1 
ATOM   10444 C  CZ    . ARG   B  1  209  ? -5.071  25.104  128.080 1.00 41.16 ? 207  ARG   B CZ    1 
ATOM   10445 N  NH1   . ARG   B  1  209  ? -5.057  25.263  126.766 1.00 32.98 ? 207  ARG   B NH1   1 
ATOM   10446 N  NH2   . ARG   B  1  209  ? -4.582  26.063  128.862 1.00 45.25 ? 207  ARG   B NH2   1 
ATOM   10447 N  N     . SER   B  1  210  ? -8.171  17.453  127.486 1.00 26.12 ? 208  SER   B N     1 
ATOM   10448 C  CA    . SER   B  1  210  ? -9.018  16.598  126.669 1.00 26.41 ? 208  SER   B CA    1 
ATOM   10449 C  C     . SER   B  1  210  ? -9.997  15.773  127.491 1.00 29.32 ? 208  SER   B C     1 
ATOM   10450 O  O     . SER   B  1  210  ? -10.955 15.233  126.930 1.00 28.92 ? 208  SER   B O     1 
ATOM   10451 C  CB    . SER   B  1  210  ? -8.134  15.687  125.822 1.00 23.54 ? 208  SER   B CB    1 
ATOM   10452 O  OG    . SER   B  1  210  ? -7.342  16.460  124.920 1.00 28.89 ? 208  SER   B OG    1 
ATOM   10453 N  N     . LYS   B  1  211  ? -9.786  15.670  128.802 1.00 27.46 ? 209  LYS   B N     1 
ATOM   10454 C  CA    . LYS   B  1  211  ? -10.634 14.807  129.615 1.00 27.81 ? 209  LYS   B CA    1 
ATOM   10455 C  C     . LYS   B  1  211  ? -12.091 15.251  129.566 1.00 27.62 ? 209  LYS   B C     1 
ATOM   10456 O  O     . LYS   B  1  211  ? -12.997 14.413  129.537 1.00 31.61 ? 209  LYS   B O     1 
ATOM   10457 C  CB    . LYS   B  1  211  ? -10.127 14.790  131.056 1.00 31.33 ? 209  LYS   B CB    1 
ATOM   10458 C  CG    . LYS   B  1  211  ? -8.624  14.587  131.183 1.00 36.79 ? 209  LYS   B CG    1 
ATOM   10459 C  CD    . LYS   B  1  211  ? -8.141  13.323  130.472 1.00 37.13 ? 209  LYS   B CD    1 
ATOM   10460 C  CE    . LYS   B  1  211  ? -6.645  13.113  130.702 1.00 44.50 ? 209  LYS   B CE    1 
ATOM   10461 N  NZ    . LYS   B  1  211  ? -6.059  12.000  129.896 1.00 41.40 ? 209  LYS   B NZ    1 
ATOM   10462 N  N     . GLU   B  1  212  ? -12.332 16.565  129.534 1.00 30.12 ? 210  GLU   B N     1 
ATOM   10463 C  CA    . GLU   B  1  212  ? -13.697 17.076  129.629 1.00 34.30 ? 210  GLU   B CA    1 
ATOM   10464 C  C     . GLU   B  1  212  ? -14.569 16.540  128.500 1.00 31.19 ? 210  GLU   B C     1 
ATOM   10465 O  O     . GLU   B  1  212  ? -15.651 15.993  128.744 1.00 30.99 ? 210  GLU   B O     1 
ATOM   10466 C  CB    . GLU   B  1  212  ? -13.688 18.605  129.616 1.00 37.26 ? 210  GLU   B CB    1 
ATOM   10467 C  CG    . GLU   B  1  212  ? -15.074 19.229  129.644 1.00 47.39 ? 210  GLU   B CG    1 
ATOM   10468 C  CD    . GLU   B  1  212  ? -15.057 20.707  129.294 1.00 56.09 ? 210  GLU   B CD    1 
ATOM   10469 O  OE1   . GLU   B  1  212  ? -14.031 21.370  129.555 1.00 64.91 ? 210  GLU   B OE1   1 
ATOM   10470 O  OE2   . GLU   B  1  212  ? -16.068 21.203  128.748 1.00 63.31 ? 210  GLU   B OE2   1 
ATOM   10471 N  N     . LEU   B  1  213  ? -14.111 16.682  127.255 1.00 28.54 ? 211  LEU   B N     1 
ATOM   10472 C  CA    . LEU   B  1  213  ? -14.908 16.217  126.124 1.00 28.43 ? 211  LEU   B CA    1 
ATOM   10473 C  C     . LEU   B  1  213  ? -14.814 14.709  125.930 1.00 29.85 ? 211  LEU   B C     1 
ATOM   10474 O  O     . LEU   B  1  213  ? -15.768 14.097  125.443 1.00 28.35 ? 211  LEU   B O     1 
ATOM   10475 C  CB    . LEU   B  1  213  ? -14.565 16.990  124.849 1.00 25.25 ? 211  LEU   B CB    1 
ATOM   10476 C  CG    . LEU   B  1  213  ? -14.962 18.470  124.896 1.00 30.92 ? 211  LEU   B CG    1 
ATOM   10477 C  CD1   . LEU   B  1  213  ? -14.723 19.166  123.569 1.00 31.34 ? 211  LEU   B CD1   1 
ATOM   10478 C  CD2   . LEU   B  1  213  ? -16.413 18.622  125.315 1.00 33.03 ? 211  LEU   B CD2   1 
ATOM   10479 N  N     . GLU   B  1  214  ? -13.696 14.088  126.316 1.00 26.70 ? 212  GLU   B N     1 
ATOM   10480 C  CA    . GLU   B  1  214  ? -13.635 12.630  126.280 1.00 25.19 ? 212  GLU   B CA    1 
ATOM   10481 C  C     . GLU   B  1  214  ? -14.709 12.018  127.166 1.00 28.67 ? 212  GLU   B C     1 
ATOM   10482 O  O     . GLU   B  1  214  ? -15.349 11.032  126.783 1.00 29.14 ? 212  GLU   B O     1 
ATOM   10483 C  CB    . GLU   B  1  214  ? -12.251 12.126  126.678 1.00 27.90 ? 212  GLU   B CB    1 
ATOM   10484 C  CG    . GLU   B  1  214  ? -11.215 12.369  125.605 1.00 25.68 ? 212  GLU   B CG    1 
ATOM   10485 C  CD    . GLU   B  1  214  ? -9.882  11.726  125.909 1.00 28.40 ? 212  GLU   B CD    1 
ATOM   10486 O  OE1   . GLU   B  1  214  ? -9.598  11.455  127.091 1.00 31.87 ? 212  GLU   B OE1   1 
ATOM   10487 O  OE2   . GLU   B  1  214  ? -9.110  11.502  124.954 1.00 28.38 ? 212  GLU   B OE2   1 
ATOM   10488 N  N     . GLU   B  1  215  ? -14.935 12.599  128.349 1.00 29.08 ? 213  GLU   B N     1 
ATOM   10489 C  CA    . GLU   B  1  215  ? -15.990 12.098  129.223 1.00 29.76 ? 213  GLU   B CA    1 
ATOM   10490 C  C     . GLU   B  1  215  ? -17.362 12.214  128.573 1.00 31.46 ? 213  GLU   B C     1 
ATOM   10491 O  O     . GLU   B  1  215  ? -18.268 11.442  128.906 1.00 31.56 ? 213  GLU   B O     1 
ATOM   10492 C  CB    . GLU   B  1  215  ? -15.966 12.835  130.563 1.00 31.92 ? 213  GLU   B CB    1 
ATOM   10493 C  CG    . GLU   B  1  215  ? -14.767 12.498  131.441 1.00 34.27 ? 213  GLU   B CG    1 
ATOM   10494 C  CD    . GLU   B  1  215  ? -14.812 13.200  132.785 1.00 44.66 ? 213  GLU   B CD    1 
ATOM   10495 O  OE1   . GLU   B  1  215  ? -15.895 13.220  133.410 1.00 55.06 ? 213  GLU   B OE1   1 
ATOM   10496 O  OE2   . GLU   B  1  215  ? -13.768 13.736  133.213 1.00 52.35 ? 213  GLU   B OE2   1 
ATOM   10497 N  N     . LYS   B  1  216  ? -17.539 13.167  127.653 1.00 28.95 ? 214  LYS   B N     1 
ATOM   10498 C  CA    . LYS   B  1  216  ? -18.805 13.300  126.947 1.00 30.83 ? 214  LYS   B CA    1 
ATOM   10499 C  C     . LYS   B  1  216  ? -18.912 12.367  125.749 1.00 34.56 ? 214  LYS   B C     1 
ATOM   10500 O  O     . LYS   B  1  216  ? -20.003 12.232  125.188 1.00 33.03 ? 214  LYS   B O     1 
ATOM   10501 C  CB    . LYS   B  1  216  ? -19.023 14.749  126.499 1.00 31.60 ? 214  LYS   B CB    1 
ATOM   10502 N  N     . GLY   B  1  217  ? -17.820 11.713  125.355 1.00 28.38 ? 215  GLY   B N     1 
ATOM   10503 C  CA    . GLY   B  1  217  ? -17.838 10.795  124.234 1.00 26.84 ? 215  GLY   B CA    1 
ATOM   10504 C  C     . GLY   B  1  217  ? -17.026 11.243  123.040 1.00 30.02 ? 215  GLY   B C     1 
ATOM   10505 O  O     . GLY   B  1  217  ? -17.044 10.556  122.011 1.00 29.50 ? 215  GLY   B O     1 
ATOM   10506 N  N     . PHE   B  1  218  ? -16.349 12.383  123.121 1.00 26.63 ? 216  PHE   B N     1 
ATOM   10507 C  CA    . PHE   B  1  218  ? -15.414 12.748  122.071 1.00 25.56 ? 216  PHE   B CA    1 
ATOM   10508 C  C     . PHE   B  1  218  ? -14.126 11.949  122.228 1.00 25.32 ? 216  PHE   B C     1 
ATOM   10509 O  O     . PHE   B  1  218  ? -13.828 11.396  123.288 1.00 24.92 ? 216  PHE   B O     1 
ATOM   10510 C  CB    . PHE   B  1  218  ? -15.060 14.236  122.138 1.00 25.75 ? 216  PHE   B CB    1 
ATOM   10511 C  CG    . PHE   B  1  218  ? -16.189 15.158  121.774 1.00 27.82 ? 216  PHE   B CG    1 
ATOM   10512 C  CD1   . PHE   B  1  218  ? -17.174 15.476  122.698 1.00 28.14 ? 216  PHE   B CD1   1 
ATOM   10513 C  CD2   . PHE   B  1  218  ? -16.252 15.726  120.516 1.00 28.30 ? 216  PHE   B CD2   1 
ATOM   10514 C  CE1   . PHE   B  1  218  ? -18.200 16.338  122.364 1.00 30.61 ? 216  PHE   B CE1   1 
ATOM   10515 C  CE2   . PHE   B  1  218  ? -17.278 16.586  120.177 1.00 30.41 ? 216  PHE   B CE2   1 
ATOM   10516 C  CZ    . PHE   B  1  218  ? -18.251 16.891  121.100 1.00 30.51 ? 216  PHE   B CZ    1 
ATOM   10517 N  N     . SER   B  1  219  ? -13.362 11.890  121.145 1.00 23.25 ? 217  SER   B N     1 
ATOM   10518 C  CA    . SER   B  1  219  ? -11.995 11.397  121.173 1.00 25.59 ? 217  SER   B CA    1 
ATOM   10519 C  C     . SER   B  1  219  ? -11.105 12.456  120.546 1.00 21.97 ? 217  SER   B C     1 
ATOM   10520 O  O     . SER   B  1  219  ? -11.573 13.515  120.120 1.00 21.47 ? 217  SER   B O     1 
ATOM   10521 C  CB    . SER   B  1  219  ? -11.857 10.062  120.436 1.00 23.53 ? 217  SER   B CB    1 
ATOM   10522 O  OG    . SER   B  1  219  ? -12.269 10.197  119.087 1.00 26.10 ? 217  SER   B OG    1 
ATOM   10523 N  N     . TYR   B  1  220  ? -9.804  12.170  120.485 1.00 22.64 ? 218  TYR   B N     1 
ATOM   10524 C  CA    . TYR   B  1  220  ? -8.841  13.166  120.053 1.00 20.73 ? 218  TYR   B CA    1 
ATOM   10525 C  C     . TYR   B  1  220  ? -7.824  12.558  119.104 1.00 20.09 ? 218  TYR   B C     1 
ATOM   10526 O  O     . TYR   B  1  220  ? -7.498  11.373  119.185 1.00 21.64 ? 218  TYR   B O     1 
ATOM   10527 C  CB    . TYR   B  1  220  ? -8.095  13.775  121.256 1.00 19.38 ? 218  TYR   B CB    1 
ATOM   10528 C  CG    . TYR   B  1  220  ? -8.889  14.867  121.920 1.00 20.16 ? 218  TYR   B CG    1 
ATOM   10529 C  CD1   . TYR   B  1  220  ? -9.860  14.569  122.868 1.00 21.31 ? 218  TYR   B CD1   1 
ATOM   10530 C  CD2   . TYR   B  1  220  ? -8.706  16.192  121.564 1.00 20.56 ? 218  TYR   B CD2   1 
ATOM   10531 C  CE1   . TYR   B  1  220  ? -10.606 15.570  123.467 1.00 23.24 ? 218  TYR   B CE1   1 
ATOM   10532 C  CE2   . TYR   B  1  220  ? -9.443  17.200  122.158 1.00 23.32 ? 218  TYR   B CE2   1 
ATOM   10533 C  CZ    . TYR   B  1  220  ? -10.397 16.879  123.101 1.00 20.88 ? 218  TYR   B CZ    1 
ATOM   10534 O  OH    . TYR   B  1  220  ? -11.131 17.880  123.688 1.00 27.78 ? 218  TYR   B OH    1 
ATOM   10535 N  N     . SER   B  1  221  ? -7.320  13.407  118.220 1.00 18.88 ? 219  SER   B N     1 
ATOM   10536 C  CA    . SER   B  1  221  ? -6.139  13.127  117.416 1.00 18.96 ? 219  SER   B CA    1 
ATOM   10537 C  C     . SER   B  1  221  ? -5.259  14.361  117.498 1.00 20.11 ? 219  SER   B C     1 
ATOM   10538 O  O     . SER   B  1  221  ? -5.681  15.446  117.092 1.00 21.02 ? 219  SER   B O     1 
ATOM   10539 C  CB    . SER   B  1  221  ? -6.521  12.870  115.961 1.00 20.55 ? 219  SER   B CB    1 
ATOM   10540 O  OG    . SER   B  1  221  ? -5.360  12.607  115.200 1.00 19.78 ? 219  SER   B OG    1 
ATOM   10541 N  N     . TYR   B  1  222  ? -4.052  14.204  118.038 1.00 19.20 ? 220  TYR   B N     1 
ATOM   10542 C  CA    . TYR   B  1  222  ? -3.192  15.353  118.300 1.00 18.33 ? 220  TYR   B CA    1 
ATOM   10543 C  C     . TYR   B  1  222  ? -2.270  15.663  117.134 1.00 20.38 ? 220  TYR   B C     1 
ATOM   10544 O  O     . TYR   B  1  222  ? -1.686  14.766  116.525 1.00 19.38 ? 220  TYR   B O     1 
ATOM   10545 C  CB    . TYR   B  1  222  ? -2.374  15.128  119.569 1.00 17.66 ? 220  TYR   B CB    1 
ATOM   10546 C  CG    . TYR   B  1  222  ? -3.293  15.014  120.734 1.00 16.82 ? 220  TYR   B CG    1 
ATOM   10547 C  CD1   . TYR   B  1  222  ? -3.889  16.144  121.273 1.00 19.15 ? 220  TYR   B CD1   1 
ATOM   10548 C  CD2   . TYR   B  1  222  ? -3.622  13.777  121.267 1.00 18.42 ? 220  TYR   B CD2   1 
ATOM   10549 C  CE1   . TYR   B  1  222  ? -4.774  16.049  122.317 1.00 19.40 ? 220  TYR   B CE1   1 
ATOM   10550 C  CE2   . TYR   B  1  222  ? -4.503  13.669  122.325 1.00 18.62 ? 220  TYR   B CE2   1 
ATOM   10551 C  CZ    . TYR   B  1  222  ? -5.070  14.813  122.848 1.00 19.51 ? 220  TYR   B CZ    1 
ATOM   10552 O  OH    . TYR   B  1  222  ? -5.963  14.717  123.874 1.00 21.27 ? 220  TYR   B OH    1 
ATOM   10553 N  N     . ASP   B  1  223  ? -2.129  16.955  116.852 1.00 19.17 ? 221  ASP   B N     1 
ATOM   10554 C  CA    . ASP   B  1  223  ? -1.295  17.478  115.778 1.00 20.90 ? 221  ASP   B CA    1 
ATOM   10555 C  C     . ASP   B  1  223  ? -0.202  18.321  116.421 1.00 20.32 ? 221  ASP   B C     1 
ATOM   10556 O  O     . ASP   B  1  223  ? -0.479  19.404  116.946 1.00 22.45 ? 221  ASP   B O     1 
ATOM   10557 C  CB    . ASP   B  1  223  ? -2.167  18.328  114.862 1.00 21.50 ? 221  ASP   B CB    1 
ATOM   10558 C  CG    . ASP   B  1  223  ? -1.366  19.201  113.921 1.00 25.09 ? 221  ASP   B CG    1 
ATOM   10559 O  OD1   . ASP   B  1  223  ? -0.209  18.853  113.607 1.00 24.50 ? 221  ASP   B OD1   1 
ATOM   10560 O  OD2   . ASP   B  1  223  ? -1.907  20.245  113.508 1.00 28.71 ? 221  ASP   B OD2   1 
ATOM   10561 N  N     . MET   B  1  224  ? 1.037   17.831  116.377 1.00 20.13 ? 222  MET   B N     1 
ATOM   10562 C  CA    . MET   B  1  224  ? 2.160   18.540  116.982 1.00 24.29 ? 222  MET   B CA    1 
ATOM   10563 C  C     . MET   B  1  224  ? 2.710   19.646  116.092 1.00 24.78 ? 222  MET   B C     1 
ATOM   10564 O  O     . MET   B  1  224  ? 3.782   20.189  116.390 1.00 26.27 ? 222  MET   B O     1 
ATOM   10565 C  CB    . MET   B  1  224  ? 3.269   17.561  117.391 1.00 23.00 ? 222  MET   B CB    1 
ATOM   10566 C  CG    . MET   B  1  224  ? 2.805   16.459  118.332 1.00 20.84 ? 222  MET   B CG    1 
ATOM   10567 S  SD    . MET   B  1  224  ? 1.904   17.099  119.748 1.00 25.68 ? 222  MET   B SD    1 
ATOM   10568 C  CE    . MET   B  1  224  ? 3.176   18.121  120.486 1.00 29.24 ? 222  MET   B CE    1 
ATOM   10569 N  N     . LEU   B  1  225  ? 2.010   19.973  115.013 1.00 24.54 ? 223  LEU   B N     1 
ATOM   10570 C  CA    . LEU   B  1  225  ? 2.225   21.121  114.135 1.00 23.60 ? 223  LEU   B CA    1 
ATOM   10571 C  C     . LEU   B  1  225  ? 3.380   20.952  113.152 1.00 29.55 ? 223  LEU   B C     1 
ATOM   10572 O  O     . LEU   B  1  225  ? 3.615   21.869  112.356 1.00 29.39 ? 223  LEU   B O     1 
ATOM   10573 C  CB    . LEU   B  1  225  ? 2.371   22.456  114.883 1.00 29.33 ? 223  LEU   B CB    1 
ATOM   10574 C  CG    . LEU   B  1  225  ? 1.254   22.762  115.880 1.00 31.22 ? 223  LEU   B CG    1 
ATOM   10575 C  CD1   . LEU   B  1  225  ? 1.519   24.074  116.592 1.00 37.01 ? 223  LEU   B CD1   1 
ATOM   10576 C  CD2   . LEU   B  1  225  ? -0.102  22.781  115.196 1.00 26.80 ? 223  LEU   B CD2   1 
ATOM   10577 N  N     . GLY   B  1  226  ? 4.095   19.831  113.164 1.00 24.71 ? 224  GLY   B N     1 
ATOM   10578 C  CA    . GLY   B  1  226  ? 5.189   19.651  112.221 1.00 27.41 ? 224  GLY   B CA    1 
ATOM   10579 C  C     . GLY   B  1  226  ? 4.685   19.597  110.789 1.00 22.85 ? 224  GLY   B C     1 
ATOM   10580 O  O     . GLY   B  1  226  ? 3.671   18.966  110.485 1.00 22.53 ? 224  GLY   B O     1 
ATOM   10581 N  N     . GLU   B  1  227  ? 5.406   20.272  109.897 1.00 21.02 ? 225  GLU   B N     1 
ATOM   10582 C  CA    . GLU   B  1  227  ? 4.996   20.314  108.502 1.00 20.56 ? 225  GLU   B CA    1 
ATOM   10583 C  C     . GLU   B  1  227  ? 6.127   20.916  107.691 1.00 17.85 ? 225  GLU   B C     1 
ATOM   10584 O  O     . GLU   B  1  227  ? 6.829   21.808  108.173 1.00 19.49 ? 225  GLU   B O     1 
ATOM   10585 C  CB    . GLU   B  1  227  ? 3.745   21.190  108.364 1.00 22.51 ? 225  GLU   B CB    1 
ATOM   10586 C  CG    . GLU   B  1  227  ? 3.201   21.306  106.976 1.00 26.77 ? 225  GLU   B CG    1 
ATOM   10587 C  CD    . GLU   B  1  227  ? 1.872   22.034  106.949 1.00 30.53 ? 225  GLU   B CD    1 
ATOM   10588 O  OE1   . GLU   B  1  227  ? 1.299   22.297  108.033 1.00 26.60 ? 225  GLU   B OE1   1 
ATOM   10589 O  OE2   . GLU   B  1  227  ? 1.406   22.346  105.841 1.00 31.23 ? 225  GLU   B OE2   1 
ATOM   10590 N  N     . ALA   B  1  228  ? 6.290   20.425  106.463 1.00 16.90 ? 226  ALA   B N     1 
ATOM   10591 C  CA    . ALA   B  1  228  ? 7.147   21.063  105.466 1.00 17.61 ? 226  ALA   B CA    1 
ATOM   10592 C  C     . ALA   B  1  228  ? 8.541   21.361  106.015 1.00 17.70 ? 226  ALA   B C     1 
ATOM   10593 O  O     . ALA   B  1  228  ? 8.995   22.508  106.041 1.00 19.33 ? 226  ALA   B O     1 
ATOM   10594 C  CB    . ALA   B  1  228  ? 6.494   22.328  104.911 1.00 19.85 ? 226  ALA   B CB    1 
ATOM   10595 N  N     . ALA   B  1  229  ? 9.203   20.307  106.492 1.00 16.78 ? 227  ALA   B N     1 
ATOM   10596 C  CA    . ALA   B  1  229  ? 10.600  20.432  106.883 1.00 16.03 ? 227  ALA   B CA    1 
ATOM   10597 C  C     . ALA   B  1  229  ? 11.401  21.049  105.745 1.00 14.69 ? 227  ALA   B C     1 
ATOM   10598 O  O     . ALA   B  1  229  ? 11.246  20.670  104.584 1.00 16.59 ? 227  ALA   B O     1 
ATOM   10599 C  CB    . ALA   B  1  229  ? 11.160  19.050  107.213 1.00 17.04 ? 227  ALA   B CB    1 
ATOM   10600 N  N     . THR   B  1  230  ? 12.222  22.041  106.081 1.00 16.06 ? 228  THR   B N     1 
ATOM   10601 C  CA    . THR   B  1  230  ? 13.096  22.675  105.106 1.00 15.71 ? 228  THR   B CA    1 
ATOM   10602 C  C     . THR   B  1  230  ? 14.499  22.100  105.153 1.00 17.15 ? 228  THR   B C     1 
ATOM   10603 O  O     . THR   B  1  230  ? 15.186  22.053  104.124 1.00 16.52 ? 228  THR   B O     1 
ATOM   10604 C  CB    . THR   B  1  230  ? 13.165  24.183  105.380 1.00 17.30 ? 228  THR   B CB    1 
ATOM   10605 O  OG1   . THR   B  1  230  ? 11.830  24.699  105.478 1.00 20.89 ? 228  THR   B OG1   1 
ATOM   10606 C  CG2   . THR   B  1  230  ? 13.903  24.926  104.259 1.00 16.82 ? 228  THR   B CG2   1 
ATOM   10607 N  N     . THR   B  1  231  ? 14.926  21.642  106.320 1.00 15.75 ? 229  THR   B N     1 
ATOM   10608 C  CA    . THR   B  1  231  ? 16.272  21.139  106.511 1.00 15.21 ? 229  THR   B CA    1 
ATOM   10609 C  C     . THR   B  1  231  ? 16.191  19.782  107.186 1.00 15.24 ? 229  THR   B C     1 
ATOM   10610 O  O     . THR   B  1  231  ? 15.163  19.407  107.749 1.00 15.62 ? 229  THR   B O     1 
ATOM   10611 C  CB    . THR   B  1  231  ? 17.093  22.064  107.403 1.00 16.57 ? 229  THR   B CB    1 
ATOM   10612 O  OG1   . THR   B  1  231  ? 16.579  21.996  108.741 1.00 17.20 ? 229  THR   B OG1   1 
ATOM   10613 C  CG2   . THR   B  1  231  ? 17.028  23.505  106.912 1.00 18.00 ? 229  THR   B CG2   1 
ATOM   10614 N  N     . ALA   B  1  232  ? 17.307  19.057  107.138 1.00 15.54 ? 230  ALA   B N     1 
ATOM   10615 C  CA    . ALA   B  1  232  ? 17.384  17.791  107.857 1.00 17.23 ? 230  ALA   B CA    1 
ATOM   10616 C  C     . ALA   B  1  232  ? 17.106  17.991  109.339 1.00 16.73 ? 230  ALA   B C     1 
ATOM   10617 O  O     . ALA   B  1  232  ? 16.445  17.159  109.973 1.00 17.64 ? 230  ALA   B O     1 
ATOM   10618 C  CB    . ALA   B  1  232  ? 18.758  17.154  107.645 1.00 18.81 ? 230  ALA   B CB    1 
ATOM   10619 N  N     . ALA   B  1  233  ? 17.586  19.102  109.909 1.00 17.13 ? 231  ALA   B N     1 
ATOM   10620 C  CA    . ALA   B  1  233  ? 17.364  19.356  111.328 1.00 17.58 ? 231  ALA   B CA    1 
ATOM   10621 C  C     . ALA   B  1  233  ? 15.885  19.542  111.630 1.00 16.45 ? 231  ALA   B C     1 
ATOM   10622 O  O     . ALA   B  1  233  ? 15.403  19.097  112.682 1.00 17.19 ? 231  ALA   B O     1 
ATOM   10623 C  CB    . ALA   B  1  233  ? 18.163  20.574  111.795 1.00 19.06 ? 231  ALA   B CB    1 
ATOM   10624 N  N     . ASP   B  1  234  ? 15.152  20.213  110.733 1.00 15.90 ? 232  ASP   B N     1 
ATOM   10625 C  CA    . ASP   B  1  234  ? 13.715  20.360  110.935 1.00 16.33 ? 232  ASP   B CA    1 
ATOM   10626 C  C     . ASP   B  1  234  ? 13.063  18.995  111.005 1.00 15.49 ? 232  ASP   B C     1 
ATOM   10627 O  O     . ASP   B  1  234  ? 12.260  18.714  111.902 1.00 16.59 ? 232  ASP   B O     1 
ATOM   10628 C  CB    . ASP   B  1  234  ? 13.078  21.089  109.750 1.00 17.02 ? 232  ASP   B CB    1 
ATOM   10629 C  CG    . ASP   B  1  234  ? 13.430  22.539  109.675 1.00 21.60 ? 232  ASP   B CG    1 
ATOM   10630 O  OD1   . ASP   B  1  234  ? 13.754  23.157  110.705 1.00 22.67 ? 232  ASP   B OD1   1 
ATOM   10631 O  OD2   . ASP   B  1  234  ? 13.346  23.065  108.546 1.00 21.62 ? 232  ASP   B OD2   1 
ATOM   10632 N  N     . ALA   B  1  235  ? 13.382  18.143  110.032 1.00 15.45 ? 233  ALA   B N     1 
ATOM   10633 C  CA    . ALA   B  1  235  ? 12.740  16.843  109.944 1.00 15.90 ? 233  ALA   B CA    1 
ATOM   10634 C  C     . ALA   B  1  235  ? 13.072  15.993  111.156 1.00 15.85 ? 233  ALA   B C     1 
ATOM   10635 O  O     . ALA   B  1  235  ? 12.214  15.273  111.679 1.00 16.28 ? 233  ALA   B O     1 
ATOM   10636 C  CB    . ALA   B  1  235  ? 13.170  16.149  108.654 1.00 16.37 ? 233  ALA   B CB    1 
ATOM   10637 N  N     . GLU   B  1  236  ? 14.320  16.060  111.620 1.00 16.19 ? 234  GLU   B N     1 
ATOM   10638 C  CA    . GLU   B  1  236  ? 14.699  15.286  112.792 1.00 16.78 ? 234  GLU   B CA    1 
ATOM   10639 C  C     . GLU   B  1  236  ? 13.958  15.783  114.020 1.00 16.84 ? 234  GLU   B C     1 
ATOM   10640 O  O     . GLU   B  1  236  ? 13.490  14.986  114.845 1.00 17.88 ? 234  GLU   B O     1 
ATOM   10641 C  CB    . GLU   B  1  236  ? 16.209  15.370  112.994 1.00 19.20 ? 234  GLU   B CB    1 
ATOM   10642 C  CG    . GLU   B  1  236  ? 16.721  14.360  113.985 1.00 22.94 ? 234  GLU   B CG    1 
ATOM   10643 C  CD    . GLU   B  1  236  ? 18.228  14.394  114.119 1.00 32.36 ? 234  GLU   B CD    1 
ATOM   10644 O  OE1   . GLU   B  1  236  ? 18.864  15.254  113.476 1.00 33.94 ? 234  GLU   B OE1   1 
ATOM   10645 O  OE2   . GLU   B  1  236  ? 18.770  13.555  114.866 1.00 34.41 ? 234  GLU   B OE2   1 
ATOM   10646 N  N     . ARG   B  1  237  ? 13.825  17.100  114.147 1.00 17.30 ? 235  ARG   B N     1 
ATOM   10647 C  CA    . ARG   B  1  237  ? 13.095  17.662  115.269 1.00 18.25 ? 235  ARG   B CA    1 
ATOM   10648 C  C     . ARG   B  1  237  ? 11.631  17.243  115.236 1.00 17.72 ? 235  ARG   B C     1 
ATOM   10649 O  O     . ARG   B  1  237  ? 11.079  16.810  116.252 1.00 17.71 ? 235  ARG   B O     1 
ATOM   10650 C  CB    . ARG   B  1  237  ? 13.215  19.184  115.266 1.00 20.55 ? 235  ARG   B CB    1 
ATOM   10651 C  CG    . ARG   B  1  237  ? 12.511  19.804  116.448 1.00 23.45 ? 235  ARG   B CG    1 
ATOM   10652 C  CD    . ARG   B  1  237  ? 12.433  21.308  116.388 1.00 29.66 ? 235  ARG   B CD    1 
ATOM   10653 N  NE    . ARG   B  1  237  ? 11.745  21.785  117.582 1.00 34.08 ? 235  ARG   B NE    1 
ATOM   10654 C  CZ    . ARG   B  1  237  ? 11.779  23.030  118.032 1.00 36.19 ? 235  ARG   B CZ    1 
ATOM   10655 N  NH1   . ARG   B  1  237  ? 12.468  23.972  117.407 1.00 39.76 ? 235  ARG   B NH1   1 
ATOM   10656 N  NH2   . ARG   B  1  237  ? 11.112  23.336  119.142 1.00 37.30 ? 235  ARG   B NH2   1 
ATOM   10657 N  N     . TYR   B  1  238  ? 10.981  17.371  114.075 1.00 16.36 ? 236  TYR   B N     1 
ATOM   10658 C  CA    . TYR   B  1  238  ? 9.573   16.992  113.990 1.00 16.01 ? 236  TYR   B CA    1 
ATOM   10659 C  C     . TYR   B  1  238  ? 9.395   15.516  114.302 1.00 16.96 ? 236  TYR   B C     1 
ATOM   10660 O  O     . TYR   B  1  238  ? 8.428   15.126  114.971 1.00 16.61 ? 236  TYR   B O     1 
ATOM   10661 C  CB    . TYR   B  1  238  ? 9.011   17.303  112.606 1.00 15.77 ? 236  TYR   B CB    1 
ATOM   10662 C  CG    . TYR   B  1  238  ? 8.918   18.772  112.277 1.00 18.85 ? 236  TYR   B CG    1 
ATOM   10663 C  CD1   . TYR   B  1  238  ? 8.659   19.720  113.255 1.00 21.02 ? 236  TYR   B CD1   1 
ATOM   10664 C  CD2   . TYR   B  1  238  ? 9.098   19.205  110.979 1.00 18.92 ? 236  TYR   B CD2   1 
ATOM   10665 C  CE1   . TYR   B  1  238  ? 8.575   21.076  112.934 1.00 24.78 ? 236  TYR   B CE1   1 
ATOM   10666 C  CE2   . TYR   B  1  238  ? 9.010   20.541  110.644 1.00 19.97 ? 236  TYR   B CE2   1 
ATOM   10667 C  CZ    . TYR   B  1  238  ? 8.749   21.471  111.620 1.00 24.66 ? 236  TYR   B CZ    1 
ATOM   10668 O  OH    . TYR   B  1  238  ? 8.681   22.808  111.274 1.00 26.15 ? 236  TYR   B OH    1 
ATOM   10669 N  N     . TYR   B  1  239  ? 10.330  14.684  113.846 1.00 16.69 ? 237  TYR   B N     1 
ATOM   10670 C  CA    . TYR   B  1  239  ? 10.275  13.268  114.181 1.00 16.97 ? 237  TYR   B CA    1 
ATOM   10671 C  C     . TYR   B  1  239  ? 10.312  13.070  115.686 1.00 18.16 ? 237  TYR   B C     1 
ATOM   10672 O  O     . TYR   B  1  239  ? 9.497   12.327  116.250 1.00 18.36 ? 237  TYR   B O     1 
ATOM   10673 C  CB    . TYR   B  1  239  ? 11.448  12.520  113.552 1.00 17.50 ? 237  TYR   B CB    1 
ATOM   10674 C  CG    . TYR   B  1  239  ? 11.526  11.081  114.024 1.00 18.48 ? 237  TYR   B CG    1 
ATOM   10675 C  CD1   . TYR   B  1  239  ? 10.790  10.093  113.402 1.00 19.41 ? 237  TYR   B CD1   1 
ATOM   10676 C  CD2   . TYR   B  1  239  ? 12.297  10.717  115.123 1.00 26.33 ? 237  TYR   B CD2   1 
ATOM   10677 C  CE1   . TYR   B  1  239  ? 10.842  8.794   113.820 1.00 20.35 ? 237  TYR   B CE1   1 
ATOM   10678 C  CE2   . TYR   B  1  239  ? 12.341  9.399   115.563 1.00 26.17 ? 237  TYR   B CE2   1 
ATOM   10679 C  CZ    . TYR   B  1  239  ? 11.606  8.448   114.900 1.00 24.07 ? 237  TYR   B CZ    1 
ATOM   10680 O  OH    . TYR   B  1  239  ? 11.630  7.135   115.301 1.00 31.42 ? 237  TYR   B OH    1 
ATOM   10681 N  N     . ARG   B  1  240  ? 11.283  13.698  116.354 1.00 18.12 ? 238  ARG   B N     1 
ATOM   10682 C  CA    . ARG   B  1  240  ? 11.407  13.528  117.795 1.00 19.29 ? 238  ARG   B CA    1 
ATOM   10683 C  C     . ARG   B  1  240  ? 10.188  14.074  118.513 1.00 17.95 ? 238  ARG   B C     1 
ATOM   10684 O  O     . ARG   B  1  240  ? 9.758   13.517  119.526 1.00 19.91 ? 238  ARG   B O     1 
ATOM   10685 C  CB    . ARG   B  1  240  ? 12.671  14.218  118.294 1.00 20.00 ? 238  ARG   B CB    1 
ATOM   10686 C  CG    . ARG   B  1  240  ? 13.940  13.584  117.788 1.00 22.36 ? 238  ARG   B CG    1 
ATOM   10687 C  CD    . ARG   B  1  240  ? 14.052  12.141  118.226 1.00 24.52 ? 238  ARG   B CD    1 
ATOM   10688 N  NE    . ARG   B  1  240  ? 15.235  11.522  117.645 1.00 29.44 ? 238  ARG   B NE    1 
ATOM   10689 C  CZ    . ARG   B  1  240  ? 15.499  10.225  117.692 1.00 34.94 ? 238  ARG   B CZ    1 
ATOM   10690 N  NH1   . ARG   B  1  240  ? 14.677  9.373   118.285 1.00 30.75 ? 238  ARG   B NH1   1 
ATOM   10691 N  NH2   . ARG   B  1  240  ? 16.616  9.771   117.131 1.00 39.48 ? 238  ARG   B NH2   1 
ATOM   10692 N  N     . ASP   B  1  241  ? 9.610   15.158  117.995 1.00 18.66 ? 239  ASP   B N     1 
ATOM   10693 C  CA    . ASP   B  1  241  ? 8.394   15.702  118.589 1.00 20.22 ? 239  ASP   B CA    1 
ATOM   10694 C  C     . ASP   B  1  241  ? 7.236   14.718  118.463 1.00 17.73 ? 239  ASP   B C     1 
ATOM   10695 O  O     . ASP   B  1  241  ? 6.462   14.538  119.406 1.00 18.86 ? 239  ASP   B O     1 
ATOM   10696 C  CB    . ASP   B  1  241  ? 8.049   17.050  117.953 1.00 23.68 ? 239  ASP   B CB    1 
ATOM   10697 C  CG    . ASP   B  1  241  ? 8.998   18.173  118.387 1.00 27.79 ? 239  ASP   B CG    1 
ATOM   10698 O  OD1   . ASP   B  1  241  ? 9.847   17.963  119.290 1.00 30.10 ? 239  ASP   B OD1   1 
ATOM   10699 O  OD2   . ASP   B  1  241  ? 8.885   19.276  117.816 1.00 35.18 ? 239  ASP   B OD2   1 
ATOM   10700 N  N     . TYR   B  1  242  ? 7.099   14.068  117.303 1.00 17.52 ? 240  TYR   B N     1 
ATOM   10701 C  CA    . TYR   B  1  242  ? 6.066   13.051  117.165 1.00 17.24 ? 240  TYR   B CA    1 
ATOM   10702 C  C     . TYR   B  1  242  ? 6.331   11.879  118.093 1.00 17.60 ? 240  TYR   B C     1 
ATOM   10703 O  O     . TYR   B  1  242  ? 5.406   11.338  118.711 1.00 17.37 ? 240  TYR   B O     1 
ATOM   10704 C  CB    . TYR   B  1  242  ? 6.042   12.518  115.744 1.00 17.10 ? 240  TYR   B CB    1 
ATOM   10705 C  CG    . TYR   B  1  242  ? 5.471   13.431  114.693 1.00 16.20 ? 240  TYR   B CG    1 
ATOM   10706 C  CD1   . TYR   B  1  242  ? 4.387   14.273  114.947 1.00 17.96 ? 240  TYR   B CD1   1 
ATOM   10707 C  CD2   . TYR   B  1  242  ? 6.003   13.420  113.427 1.00 16.69 ? 240  TYR   B CD2   1 
ATOM   10708 C  CE1   . TYR   B  1  242  ? 3.864   15.088  113.945 1.00 18.45 ? 240  TYR   B CE1   1 
ATOM   10709 C  CE2   . TYR   B  1  242  ? 5.491   14.213  112.429 1.00 17.17 ? 240  TYR   B CE2   1 
ATOM   10710 C  CZ    . TYR   B  1  242  ? 4.434   15.048  112.686 1.00 18.72 ? 240  TYR   B CZ    1 
ATOM   10711 O  OH    . TYR   B  1  242  ? 3.961   15.813  111.630 1.00 18.65 ? 240  TYR   B OH    1 
ATOM   10712 N  N     . GLU   B  1  243  ? 7.591   11.452  118.177 1.00 17.03 ? 241  GLU   B N     1 
ATOM   10713 C  CA    . GLU   B  1  243  ? 7.937   10.316  119.020 1.00 17.76 ? 241  GLU   B CA    1 
ATOM   10714 C  C     . GLU   B  1  243  ? 7.584   10.608  120.467 1.00 16.84 ? 241  GLU   B C     1 
ATOM   10715 O  O     . GLU   B  1  243  ? 6.965   9.786   121.155 1.00 17.79 ? 241  GLU   B O     1 
ATOM   10716 C  CB    . GLU   B  1  243  ? 9.436   10.053  118.886 1.00 18.84 ? 241  GLU   B CB    1 
ATOM   10717 C  CG    . GLU   B  1  243  ? 9.959   8.931   119.753 1.00 23.62 ? 241  GLU   B CG    1 
ATOM   10718 C  CD    . GLU   B  1  243  ? 11.474  8.845   119.714 1.00 25.47 ? 241  GLU   B CD    1 
ATOM   10719 O  OE1   . GLU   B  1  243  ? 12.129  9.898   119.585 1.00 28.31 ? 241  GLU   B OE1   1 
ATOM   10720 O  OE2   . GLU   B  1  243  ? 12.011  7.724   119.799 1.00 29.99 ? 241  GLU   B OE2   1 
ATOM   10721 N  N     . SER   B  1  244  ? 7.977   11.788  120.945 1.00 17.87 ? 242  SER   B N     1 
ATOM   10722 C  CA    A SER   B  1  244  ? 7.668   12.187  122.311 0.67 18.34 ? 242  SER   B CA    1 
ATOM   10723 C  CA    B SER   B  1  244  ? 7.666   12.173  122.316 0.33 18.36 ? 242  SER   B CA    1 
ATOM   10724 C  C     . SER   B  1  244  ? 6.163   12.259  122.537 1.00 17.24 ? 242  SER   B C     1 
ATOM   10725 O  O     . SER   B  1  244  ? 5.656   11.818  123.575 1.00 18.01 ? 242  SER   B O     1 
ATOM   10726 C  CB    A SER   B  1  244  ? 8.316   13.543  122.573 0.67 19.91 ? 242  SER   B CB    1 
ATOM   10727 C  CB    B SER   B  1  244  ? 8.336   13.504  122.651 0.33 19.91 ? 242  SER   B CB    1 
ATOM   10728 O  OG    A SER   B  1  244  ? 8.032   14.015  123.867 0.67 23.58 ? 242  SER   B OG    1 
ATOM   10729 O  OG    B SER   B  1  244  ? 9.746   13.378  122.621 0.33 17.71 ? 242  SER   B OG    1 
ATOM   10730 N  N     . ALA   B  1  245  ? 5.432   12.816  121.571 1.00 18.01 ? 243  ALA   B N     1 
ATOM   10731 C  CA    . ALA   B  1  245  ? 3.987   12.910  121.726 1.00 19.03 ? 243  ALA   B CA    1 
ATOM   10732 C  C     . ALA   B  1  245  ? 3.342   11.530  121.747 1.00 19.81 ? 243  ALA   B C     1 
ATOM   10733 O  O     . ALA   B  1  245  ? 2.395   11.301  122.505 1.00 19.69 ? 243  ALA   B O     1 
ATOM   10734 C  CB    . ALA   B  1  245  ? 3.392   13.755  120.606 1.00 18.75 ? 243  ALA   B CB    1 
ATOM   10735 N  N     . ILE   B  1  246  ? 3.830   10.597  120.920 1.00 18.82 ? 244  ILE   B N     1 
ATOM   10736 C  CA    . ILE   B  1  246  ? 3.268   9.245   120.934 1.00 19.70 ? 244  ILE   B CA    1 
ATOM   10737 C  C     . ILE   B  1  246  ? 3.405   8.604   122.307 1.00 20.47 ? 244  ILE   B C     1 
ATOM   10738 O  O     . ILE   B  1  246  ? 2.469   7.970   122.806 1.00 21.72 ? 244  ILE   B O     1 
ATOM   10739 C  CB    . ILE   B  1  246  ? 3.887   8.376   119.829 1.00 18.87 ? 244  ILE   B CB    1 
ATOM   10740 C  CG1   . ILE   B  1  246  ? 3.410   8.859   118.471 1.00 19.50 ? 244  ILE   B CG1   1 
ATOM   10741 C  CG2   . ILE   B  1  246  ? 3.494   6.908   120.033 1.00 20.40 ? 244  ILE   B CG2   1 
ATOM   10742 C  CD1   . ILE   B  1  246  ? 4.108   8.178   117.315 1.00 21.68 ? 244  ILE   B CD1   1 
ATOM   10743 N  N     . HIS   B  1  247  ? 4.573   8.736   122.935 1.00 20.35 ? 245  HIS   B N     1 
ATOM   10744 C  CA    . HIS   B  1  247  ? 4.712   8.213   124.290 1.00 19.56 ? 245  HIS   B CA    1 
ATOM   10745 C  C     . HIS   B  1  247  ? 3.695   8.838   125.230 1.00 20.24 ? 245  HIS   B C     1 
ATOM   10746 O  O     . HIS   B  1  247  ? 3.077   8.134   126.035 1.00 22.09 ? 245  HIS   B O     1 
ATOM   10747 C  CB    . HIS   B  1  247  ? 6.134   8.410   124.811 1.00 20.42 ? 245  HIS   B CB    1 
ATOM   10748 C  CG    . HIS   B  1  247  ? 7.132   7.504   124.166 1.00 22.29 ? 245  HIS   B CG    1 
ATOM   10749 N  ND1   . HIS   B  1  247  ? 7.117   6.139   124.348 1.00 21.90 ? 245  HIS   B ND1   1 
ATOM   10750 C  CD2   . HIS   B  1  247  ? 8.174   7.765   123.344 1.00 23.59 ? 245  HIS   B CD2   1 
ATOM   10751 C  CE1   . HIS   B  1  247  ? 8.104   5.596   123.659 1.00 24.33 ? 245  HIS   B CE1   1 
ATOM   10752 N  NE2   . HIS   B  1  247  ? 8.760   6.561   123.041 1.00 25.33 ? 245  HIS   B NE2   1 
ATOM   10753 N  N     . ALA   B  1  248  ? 3.493   10.155  125.130 1.00 18.40 ? 246  ALA   B N     1 
ATOM   10754 C  CA    . ALA   B  1  248  ? 2.567   10.809  126.048 1.00 20.23 ? 246  ALA   B CA    1 
ATOM   10755 C  C     . ALA   B  1  248  ? 1.130   10.412  125.740 1.00 19.82 ? 246  ALA   B C     1 
ATOM   10756 O  O     . ALA   B  1  248  ? 0.348   10.109  126.648 1.00 20.72 ? 246  ALA   B O     1 
ATOM   10757 C  CB    . ALA   B  1  248  ? 2.724   12.324  125.942 1.00 21.04 ? 246  ALA   B CB    1 
ATOM   10758 N  N     . ILE   B  1  249  ? 0.771   10.400  124.457 1.00 19.96 ? 247  ILE   B N     1 
ATOM   10759 C  CA    . ILE   B  1  249  ? -0.586  10.037  124.062 1.00 20.07 ? 247  ILE   B CA    1 
ATOM   10760 C  C     . ILE   B  1  249  ? -0.848  8.571   124.354 1.00 19.84 ? 247  ILE   B C     1 
ATOM   10761 O  O     . ILE   B  1  249  ? -1.933  8.197   124.813 1.00 21.61 ? 247  ILE   B O     1 
ATOM   10762 C  CB    . ILE   B  1  249  ? -0.798  10.354  122.576 1.00 18.80 ? 247  ILE   B CB    1 
ATOM   10763 C  CG1   . ILE   B  1  249  ? -0.683  11.849  122.302 1.00 18.91 ? 247  ILE   B CG1   1 
ATOM   10764 C  CG2   . ILE   B  1  249  ? -2.160  9.813   122.108 1.00 21.70 ? 247  ILE   B CG2   1 
ATOM   10765 C  CD1   . ILE   B  1  249  ? -0.391  12.160  120.843 1.00 19.15 ? 247  ILE   B CD1   1 
ATOM   10766 N  N     . GLY   B  1  250  ? 0.141   7.715   124.085 1.00 21.41 ? 248  GLY   B N     1 
ATOM   10767 C  CA    . GLY   B  1  250  ? -0.034  6.297   124.328 1.00 22.72 ? 248  GLY   B CA    1 
ATOM   10768 C  C     . GLY   B  1  250  ? -0.197  5.977   125.798 1.00 25.92 ? 248  GLY   B C     1 
ATOM   10769 O  O     . GLY   B  1  250  ? -1.036  5.155   126.176 1.00 25.05 ? 248  GLY   B O     1 
ATOM   10770 N  N     . LYS   B  1  251  ? 0.591   6.626   126.653 1.00 23.05 ? 249  LYS   B N     1 
ATOM   10771 C  CA    . LYS   B  1  251  ? 0.425   6.402   128.083 1.00 26.34 ? 249  LYS   B CA    1 
ATOM   10772 C  C     . LYS   B  1  251  ? -0.926  6.921   128.561 1.00 23.17 ? 249  LYS   B C     1 
ATOM   10773 O  O     . LYS   B  1  251  ? -1.600  6.267   129.366 1.00 26.06 ? 249  LYS   B O     1 
ATOM   10774 C  CB    . LYS   B  1  251  ? 1.577   7.046   128.857 1.00 26.22 ? 249  LYS   B CB    1 
ATOM   10775 N  N     . ALA   B  1  252  ? -1.351  8.078   128.044 1.00 24.94 ? 250  ALA   B N     1 
ATOM   10776 C  CA    . ALA   B  1  252  ? -2.645  8.631   128.431 1.00 23.99 ? 250  ALA   B CA    1 
ATOM   10777 C  C     . ALA   B  1  252  ? -3.789  7.773   127.912 1.00 25.45 ? 250  ALA   B C     1 
ATOM   10778 O  O     . ALA   B  1  252  ? -4.822  7.639   128.579 1.00 28.36 ? 250  ALA   B O     1 
ATOM   10779 C  CB    . ALA   B  1  252  ? -2.782  10.064  127.922 1.00 24.58 ? 250  ALA   B CB    1 
ATOM   10780 N  N     . SER   B  1  253  ? -3.628  7.195   126.719 1.00 24.14 ? 251  SER   B N     1 
ATOM   10781 C  CA    . SER   B  1  253  ? -4.645  6.286   126.198 1.00 25.40 ? 251  SER   B CA    1 
ATOM   10782 C  C     . SER   B  1  253  ? -4.915  5.154   127.177 1.00 24.78 ? 251  SER   B C     1 
ATOM   10783 O  O     . SER   B  1  253  ? -6.074  4.783   127.410 1.00 28.15 ? 251  SER   B O     1 
ATOM   10784 C  CB    . SER   B  1  253  ? -4.197  5.710   124.862 1.00 24.24 ? 251  SER   B CB    1 
ATOM   10785 O  OG    . SER   B  1  253  ? -5.181  4.818   124.368 1.00 26.38 ? 251  SER   B OG    1 
ATOM   10786 N  N     . ALA   B  1  254  ? -3.853  4.591   127.758 1.00 24.48 ? 252  ALA   B N     1 
ATOM   10787 C  CA    . ALA   B  1  254  ? -3.963  3.595   128.824 1.00 28.04 ? 252  ALA   B CA    1 
ATOM   10788 C  C     . ALA   B  1  254  ? -4.827  2.407   128.409 1.00 29.62 ? 252  ALA   B C     1 
ATOM   10789 O  O     . ALA   B  1  254  ? -5.671  1.927   129.168 1.00 31.52 ? 252  ALA   B O     1 
ATOM   10790 C  CB    . ALA   B  1  254  ? -4.434  4.217   130.140 1.00 29.86 ? 252  ALA   B CB    1 
ATOM   10791 N  N     . GLY   B  1  255  ? -4.621  1.936   127.181 1.00 30.52 ? 253  GLY   B N     1 
ATOM   10792 C  CA    . GLY   B  1  255  ? -5.328  0.766   126.712 1.00 29.01 ? 253  GLY   B CA    1 
ATOM   10793 C  C     . GLY   B  1  255  ? -6.749  1.004   126.254 1.00 31.34 ? 253  GLY   B C     1 
ATOM   10794 O  O     . GLY   B  1  255  ? -7.481  0.031   126.046 1.00 33.64 ? 253  GLY   B O     1 
ATOM   10795 N  N     . ARG   B  1  256  ? -7.171  2.260   126.096 1.00 27.22 ? 254  ARG   B N     1 
ATOM   10796 C  CA    . ARG   B  1  256  ? -8.519  2.532   125.610 1.00 28.87 ? 254  ARG   B CA    1 
ATOM   10797 C  C     . ARG   B  1  256  ? -8.722  2.112   124.168 1.00 27.63 ? 254  ARG   B C     1 
ATOM   10798 O  O     . ARG   B  1  256  ? -9.872  2.043   123.717 1.00 28.98 ? 254  ARG   B O     1 
ATOM   10799 C  CB    . ARG   B  1  256  ? -8.869  4.009   125.768 1.00 28.06 ? 254  ARG   B CB    1 
ATOM   10800 C  CG    . ARG   B  1  256  ? -9.372  4.348   127.163 1.00 27.00 ? 254  ARG   B CG    1 
ATOM   10801 C  CD    . ARG   B  1  256  ? -9.676  5.814   127.271 1.00 26.87 ? 254  ARG   B CD    1 
ATOM   10802 N  NE    . ARG   B  1  256  ? -8.446  6.598   127.309 1.00 27.24 ? 254  ARG   B NE    1 
ATOM   10803 C  CZ    . ARG   B  1  256  ? -8.391  7.913   127.173 1.00 26.82 ? 254  ARG   B CZ    1 
ATOM   10804 N  NH1   . ARG   B  1  256  ? -9.468  8.622   126.886 1.00 28.94 ? 254  ARG   B NH1   1 
ATOM   10805 N  NH2   . ARG   B  1  256  ? -7.223  8.533   127.331 1.00 29.11 ? 254  ARG   B NH2   1 
ATOM   10806 N  N     . GLY   B  1  257  ? -7.649  1.834   123.439 1.00 27.87 ? 255  GLY   B N     1 
ATOM   10807 C  CA    . GLY   B  1  257  ? -7.767  1.401   122.065 1.00 27.47 ? 255  GLY   B CA    1 
ATOM   10808 C  C     . GLY   B  1  257  ? -7.912  2.560   121.105 1.00 25.00 ? 255  GLY   B C     1 
ATOM   10809 O  O     . GLY   B  1  257  ? -7.986  3.733   121.473 1.00 26.59 ? 255  GLY   B O     1 
ATOM   10810 N  N     . ILE   B  1  258  ? -7.988  2.202   119.825 1.00 25.68 ? 256  ILE   B N     1 
ATOM   10811 C  CA    . ILE   B  1  258  ? -7.882  3.206   118.774 1.00 24.47 ? 256  ILE   B CA    1 
ATOM   10812 C  C     . ILE   B  1  258  ? -9.162  4.007   118.558 1.00 23.56 ? 256  ILE   B C     1 
ATOM   10813 O  O     . ILE   B  1  258  ? -9.111  5.069   117.933 1.00 24.89 ? 256  ILE   B O     1 
ATOM   10814 C  CB    . ILE   B  1  258  ? -7.434  2.556   117.459 1.00 27.40 ? 256  ILE   B CB    1 
ATOM   10815 C  CG1   . ILE   B  1  258  ? -8.478  1.541   116.998 1.00 27.48 ? 256  ILE   B CG1   1 
ATOM   10816 C  CG2   . ILE   B  1  258  ? -6.089  1.871   117.637 1.00 27.44 ? 256  ILE   B CG2   1 
ATOM   10817 C  CD1   . ILE   B  1  258  ? -8.176  0.938   115.651 1.00 29.08 ? 256  ILE   B CD1   1 
ATOM   10818 N  N     . TYR   B  1  259  ? -10.306 3.537   119.052 1.00 24.18 ? 257  TYR   B N     1 
ATOM   10819 C  CA    . TYR   B  1  259  ? -11.574 4.227   118.825 1.00 25.79 ? 257  TYR   B CA    1 
ATOM   10820 C  C     . TYR   B  1  259  ? -11.917 5.178   119.967 1.00 25.76 ? 257  TYR   B C     1 
ATOM   10821 O  O     . TYR   B  1  259  ? -12.115 6.377   119.747 1.00 25.37 ? 257  TYR   B O     1 
ATOM   10822 C  CB    . TYR   B  1  259  ? -12.690 3.198   118.599 1.00 27.79 ? 257  TYR   B CB    1 
ATOM   10823 C  CG    . TYR   B  1  259  ? -12.323 2.229   117.504 1.00 26.75 ? 257  TYR   B CG    1 
ATOM   10824 C  CD1   . TYR   B  1  259  ? -12.197 2.664   116.194 1.00 27.25 ? 257  TYR   B CD1   1 
ATOM   10825 C  CD2   . TYR   B  1  259  ? -12.072 0.890   117.780 1.00 30.80 ? 257  TYR   B CD2   1 
ATOM   10826 C  CE1   . TYR   B  1  259  ? -11.838 1.796   115.181 1.00 27.96 ? 257  TYR   B CE1   1 
ATOM   10827 C  CE2   . TYR   B  1  259  ? -11.715 0.011   116.765 1.00 25.23 ? 257  TYR   B CE2   1 
ATOM   10828 C  CZ    . TYR   B  1  259  ? -11.597 0.476   115.471 1.00 30.41 ? 257  TYR   B CZ    1 
ATOM   10829 O  OH    . TYR   B  1  259  ? -11.239 -0.376  114.452 1.00 29.31 ? 257  TYR   B OH    1 
ATOM   10830 N  N     . GLU   B  1  260  ? -11.992 4.653   121.191 1.00 25.62 ? 258  GLU   B N     1 
ATOM   10831 C  CA    . GLU   B  1  260  ? -12.253 5.506   122.342 1.00 28.78 ? 258  GLU   B CA    1 
ATOM   10832 C  C     . GLU   B  1  260  ? -11.046 6.374   122.661 1.00 31.13 ? 258  GLU   B C     1 
ATOM   10833 O  O     . GLU   B  1  260  ? -11.193 7.549   123.021 1.00 31.18 ? 258  GLU   B O     1 
ATOM   10834 C  CB    . GLU   B  1  260  ? -12.613 4.645   123.551 1.00 29.19 ? 258  GLU   B CB    1 
ATOM   10835 C  CG    . GLU   B  1  260  ? -12.799 5.437   124.832 1.00 39.79 ? 258  GLU   B CG    1 
ATOM   10836 C  CD    . GLU   B  1  260  ? -13.107 4.557   126.028 1.00 39.04 ? 258  GLU   B CD    1 
ATOM   10837 O  OE1   . GLU   B  1  260  ? -13.427 3.364   125.826 1.00 42.90 ? 258  GLU   B OE1   1 
ATOM   10838 O  OE2   . GLU   B  1  260  ? -13.028 5.064   127.170 1.00 44.16 ? 258  GLU   B OE2   1 
ATOM   10839 N  N     . GLY   B  1  261  ? -9.849  5.818   122.512 1.00 26.14 ? 259  GLY   B N     1 
ATOM   10840 C  CA    . GLY   B  1  261  ? -8.648  6.471   122.967 1.00 25.18 ? 259  GLY   B CA    1 
ATOM   10841 C  C     . GLY   B  1  261  ? -8.095  7.436   121.946 1.00 23.64 ? 259  GLY   B C     1 
ATOM   10842 O  O     . GLY   B  1  261  ? -8.438  7.404   120.755 1.00 23.97 ? 259  GLY   B O     1 
ATOM   10843 N  N     . PRO   B  1  262  ? -7.201  8.307   122.401 1.00 22.67 ? 260  PRO   B N     1 
ATOM   10844 C  CA    . PRO   B  1  262  ? -6.636  9.328   121.520 1.00 22.87 ? 260  PRO   B CA    1 
ATOM   10845 C  C     . PRO   B  1  262  ? -5.643  8.739   120.532 1.00 23.99 ? 260  PRO   B C     1 
ATOM   10846 O  O     . PRO   B  1  262  ? -5.082  7.658   120.725 1.00 24.32 ? 260  PRO   B O     1 
ATOM   10847 C  CB    . PRO   B  1  262  ? -5.920  10.267  122.495 1.00 23.65 ? 260  PRO   B CB    1 
ATOM   10848 C  CG    . PRO   B  1  262  ? -5.538  9.370   123.637 1.00 24.64 ? 260  PRO   B CG    1 
ATOM   10849 C  CD    . PRO   B  1  262  ? -6.695  8.416   123.780 1.00 23.13 ? 260  PRO   B CD    1 
ATOM   10850 N  N     . GLY   B  1  263  ? -5.424  9.490   119.462 1.00 20.91 ? 261  GLY   B N     1 
ATOM   10851 C  CA    . GLY   B  1  263  ? -4.415  9.135   118.492 1.00 21.32 ? 261  GLY   B CA    1 
ATOM   10852 C  C     . GLY   B  1  263  ? -3.563  10.329  118.129 1.00 18.26 ? 261  GLY   B C     1 
ATOM   10853 O  O     . GLY   B  1  263  ? -3.677  11.400  118.740 1.00 20.07 ? 261  GLY   B O     1 
ATOM   10854 N  N     . ILE   B  1  264  ? -2.719  10.158  117.122 1.00 18.78 ? 262  ILE   B N     1 
ATOM   10855 C  CA    . ILE   B  1  264  ? -1.848  11.224  116.649 1.00 17.44 ? 262  ILE   B CA    1 
ATOM   10856 C  C     . ILE   B  1  264  ? -1.987  11.333  115.142 1.00 18.81 ? 262  ILE   B C     1 
ATOM   10857 O  O     . ILE   B  1  264  ? -2.298  10.355  114.456 1.00 19.51 ? 262  ILE   B O     1 
ATOM   10858 C  CB    . ILE   B  1  264  ? -0.380  10.971  117.068 1.00 19.31 ? 262  ILE   B CB    1 
ATOM   10859 C  CG1   . ILE   B  1  264  ? 0.469   12.220  116.846 1.00 18.31 ? 262  ILE   B CG1   1 
ATOM   10860 C  CG2   . ILE   B  1  264  ? 0.200   9.793   116.299 1.00 20.53 ? 262  ILE   B CG2   1 
ATOM   10861 C  CD1   . ILE   B  1  264  ? 1.901   12.097  117.360 1.00 20.15 ? 262  ILE   B CD1   1 
ATOM   10862 N  N     . SER   B  1  265  ? -1.791  12.545  114.637 1.00 16.28 ? 263  SER   B N     1 
ATOM   10863 C  CA    . SER   B  1  265  ? -1.770  12.813  113.209 1.00 17.21 ? 263  SER   B CA    1 
ATOM   10864 C  C     . SER   B  1  265  ? -0.401  13.358  112.842 1.00 17.63 ? 263  SER   B C     1 
ATOM   10865 O  O     . SER   B  1  265  ? 0.159   14.183  113.568 1.00 21.97 ? 263  SER   B O     1 
ATOM   10866 C  CB    . SER   B  1  265  ? -2.822  13.849  112.833 1.00 19.24 ? 263  SER   B CB    1 
ATOM   10867 O  OG    . SER   B  1  265  ? -4.120  13.279  112.865 1.00 20.40 ? 263  SER   B OG    1 
ATOM   10868 N  N     . ILE   B  1  266  ? 0.138   12.894  111.719 1.00 16.00 ? 264  ILE   B N     1 
ATOM   10869 C  CA    . ILE   B  1  266  ? 1.443   13.328  111.249 1.00 16.98 ? 264  ILE   B CA    1 
ATOM   10870 C  C     . ILE   B  1  266  ? 1.322   13.787  109.809 1.00 16.48 ? 264  ILE   B C     1 
ATOM   10871 O  O     . ILE   B  1  266  ? 0.386   13.436  109.093 1.00 17.35 ? 264  ILE   B O     1 
ATOM   10872 C  CB    . ILE   B  1  266  ? 2.508   12.220  111.354 1.00 17.81 ? 264  ILE   B CB    1 
ATOM   10873 C  CG1   . ILE   B  1  266  ? 2.194   11.074  110.395 1.00 20.80 ? 264  ILE   B CG1   1 
ATOM   10874 C  CG2   . ILE   B  1  266  ? 2.594   11.706  112.783 1.00 19.36 ? 264  ILE   B CG2   1 
ATOM   10875 C  CD1   . ILE   B  1  266  ? 3.338   10.100  110.218 1.00 23.36 ? 264  ILE   B CD1   1 
ATOM   10876 N  N     . LYS   B  1  267  ? 2.305   14.568  109.387 1.00 15.97 ? 265  LYS   B N     1 
ATOM   10877 C  CA    . LYS   B  1  267  ? 2.437   14.978  108.003 1.00 15.84 ? 265  LYS   B CA    1 
ATOM   10878 C  C     . LYS   B  1  267  ? 3.758   14.441  107.487 1.00 15.26 ? 265  LYS   B C     1 
ATOM   10879 O  O     . LYS   B  1  267  ? 4.806   14.666  108.102 1.00 16.43 ? 265  LYS   B O     1 
ATOM   10880 C  CB    . LYS   B  1  267  ? 2.391   16.497  107.886 1.00 16.17 ? 265  LYS   B CB    1 
ATOM   10881 C  CG    . LYS   B  1  267  ? 0.987   17.050  108.036 1.00 18.50 ? 265  LYS   B CG    1 
ATOM   10882 C  CD    . LYS   B  1  267  ? 0.994   18.563  107.987 1.00 23.18 ? 265  LYS   B CD    1 
ATOM   10883 C  CE    . LYS   B  1  267  ? -0.419  19.125  108.109 1.00 22.92 ? 265  LYS   B CE    1 
ATOM   10884 N  NZ    . LYS   B  1  267  ? -1.120  18.652  109.328 1.00 24.41 ? 265  LYS   B NZ    1 
ATOM   10885 N  N     . LEU   B  1  268  ? 3.705   13.703  106.379 1.00 15.11 ? 266  LEU   B N     1 
ATOM   10886 C  CA    . LEU   B  1  268  ? 4.942   13.179  105.808 1.00 15.68 ? 266  LEU   B CA    1 
ATOM   10887 C  C     . LEU   B  1  268  ? 5.918   14.289  105.453 1.00 15.98 ? 266  LEU   B C     1 
ATOM   10888 O  O     . LEU   B  1  268  ? 7.132   14.094  105.568 1.00 15.89 ? 266  LEU   B O     1 
ATOM   10889 C  CB    . LEU   B  1  268  ? 4.659   12.284  104.603 1.00 15.09 ? 266  LEU   B CB    1 
ATOM   10890 C  CG    . LEU   B  1  268  ? 3.777   11.079  104.937 1.00 16.33 ? 266  LEU   B CG    1 
ATOM   10891 C  CD1   . LEU   B  1  268  ? 3.595   10.225  103.713 1.00 20.18 ? 266  LEU   B CD1   1 
ATOM   10892 C  CD2   . LEU   B  1  268  ? 4.367   10.251  106.059 1.00 19.40 ? 266  LEU   B CD2   1 
ATOM   10893 N  N     . SER   B  1  269  ? 5.423   15.465  105.060 1.00 15.16 ? 267  SER   B N     1 
ATOM   10894 C  CA    . SER   B  1  269  ? 6.343   16.554  104.747 1.00 15.50 ? 267  SER   B CA    1 
ATOM   10895 C  C     . SER   B  1  269  ? 7.111   17.036  105.969 1.00 14.88 ? 267  SER   B C     1 
ATOM   10896 O  O     . SER   B  1  269  ? 8.146   17.691  105.805 1.00 15.79 ? 267  SER   B O     1 
ATOM   10897 C  CB    . SER   B  1  269  ? 5.605   17.737  104.130 1.00 16.69 ? 267  SER   B CB    1 
ATOM   10898 O  OG    . SER   B  1  269  ? 4.797   18.366  105.116 1.00 16.67 ? 267  SER   B OG    1 
ATOM   10899 N  N     . ALA   B  1  270  ? 6.628   16.754  107.176 1.00 14.03 ? 268  ALA   B N     1 
ATOM   10900 C  CA    . ALA   B  1  270  ? 7.393   17.091  108.365 1.00 15.13 ? 268  ALA   B CA    1 
ATOM   10901 C  C     . ALA   B  1  270  ? 8.613   16.201  108.523 1.00 16.39 ? 268  ALA   B C     1 
ATOM   10902 O  O     . ALA   B  1  270  ? 9.547   16.570  109.245 1.00 16.42 ? 268  ALA   B O     1 
ATOM   10903 C  CB    . ALA   B  1  270  ? 6.521   16.926  109.609 1.00 16.95 ? 268  ALA   B CB    1 
ATOM   10904 N  N     . LEU   B  1  271  ? 8.615   15.027  107.898 1.00 14.77 ? 269  LEU   B N     1 
ATOM   10905 C  CA    . LEU   B  1  271  ? 9.597   14.008  108.233 1.00 17.35 ? 269  LEU   B CA    1 
ATOM   10906 C  C     . LEU   B  1  271  ? 10.746  13.942  107.250 1.00 15.29 ? 269  LEU   B C     1 
ATOM   10907 O  O     . LEU   B  1  271  ? 11.663  13.138  107.448 1.00 17.23 ? 269  LEU   B O     1 
ATOM   10908 C  CB    . LEU   B  1  271  ? 8.933   12.646  108.371 1.00 17.54 ? 269  LEU   B CB    1 
ATOM   10909 C  CG    . LEU   B  1  271  ? 7.949   12.605  109.536 1.00 17.80 ? 269  LEU   B CG    1 
ATOM   10910 C  CD1   . LEU   B  1  271  ? 7.189   11.297  109.482 1.00 21.35 ? 269  LEU   B CD1   1 
ATOM   10911 C  CD2   . LEU   B  1  271  ? 8.678   12.764  110.862 1.00 17.84 ? 269  LEU   B CD2   1 
ATOM   10912 N  N     . HIS   B  1  272  ? 10.734  14.780  106.216 1.00 16.02 ? 270  HIS   B N     1 
ATOM   10913 C  CA    . HIS   B  1  272  ? 11.863  14.780  105.313 1.00 16.16 ? 270  HIS   B CA    1 
ATOM   10914 C  C     . HIS   B  1  272  ? 11.845  16.085  104.544 1.00 14.91 ? 270  HIS   B C     1 
ATOM   10915 O  O     . HIS   B  1  272  ? 10.765  16.531  104.145 1.00 16.57 ? 270  HIS   B O     1 
ATOM   10916 C  CB    . HIS   B  1  272  ? 11.749  13.613  104.340 1.00 18.35 ? 270  HIS   B CB    1 
ATOM   10917 C  CG    . HIS   B  1  272  ? 13.035  13.303  103.664 1.00 17.33 ? 270  HIS   B CG    1 
ATOM   10918 N  ND1   . HIS   B  1  272  ? 13.517  14.051  102.612 1.00 19.11 ? 270  HIS   B ND1   1 
ATOM   10919 C  CD2   . HIS   B  1  272  ? 13.972  12.364  103.926 1.00 22.43 ? 270  HIS   B CD2   1 
ATOM   10920 C  CE1   . HIS   B  1  272  ? 14.689  13.570  102.239 1.00 19.50 ? 270  HIS   B CE1   1 
ATOM   10921 N  NE2   . HIS   B  1  272  ? 14.988  12.546  103.020 1.00 22.78 ? 270  HIS   B NE2   1 
ATOM   10922 N  N     . PRO   B  1  273  ? 12.996  16.721  104.315 1.00 15.68 ? 271  PRO   B N     1 
ATOM   10923 C  CA    . PRO   B  1  273  ? 12.996  18.000  103.588 1.00 15.49 ? 271  PRO   B CA    1 
ATOM   10924 C  C     . PRO   B  1  273  ? 12.784  17.863  102.094 1.00 15.15 ? 271  PRO   B C     1 
ATOM   10925 O  O     . PRO   B  1  273  ? 12.561  18.882  101.436 1.00 16.34 ? 271  PRO   B O     1 
ATOM   10926 C  CB    . PRO   B  1  273  ? 14.383  18.576  103.896 1.00 17.13 ? 271  PRO   B CB    1 
ATOM   10927 C  CG    . PRO   B  1  273  ? 15.218  17.387  104.201 1.00 18.87 ? 271  PRO   B CG    1 
ATOM   10928 C  CD    . PRO   B  1  273  ? 14.315  16.407  104.889 1.00 16.73 ? 271  PRO   B CD    1 
ATOM   10929 N  N     . ARG   B  1  274  ? 12.856  16.655  101.541 1.00 15.01 ? 272  ARG   B N     1 
ATOM   10930 C  CA    . ARG   B  1  274  ? 12.634  16.454  100.115 1.00 15.52 ? 272  ARG   B CA    1 
ATOM   10931 C  C     . ARG   B  1  274  ? 11.530  15.433  99.904  1.00 17.14 ? 272  ARG   B C     1 
ATOM   10932 O  O     . ARG   B  1  274  ? 11.707  14.437  99.193  1.00 16.92 ? 272  ARG   B O     1 
ATOM   10933 C  CB    . ARG   B  1  274  ? 13.925  15.995  99.427  1.00 16.38 ? 272  ARG   B CB    1 
ATOM   10934 C  CG    . ARG   B  1  274  ? 15.061  17.009  99.481  1.00 17.20 ? 272  ARG   B CG    1 
ATOM   10935 C  CD    . ARG   B  1  274  ? 14.666  18.360  98.889  1.00 17.23 ? 272  ARG   B CD    1 
ATOM   10936 N  NE    . ARG   B  1  274  ? 14.184  18.257  97.516  1.00 17.08 ? 272  ARG   B NE    1 
ATOM   10937 C  CZ    . ARG   B  1  274  ? 14.969  18.159  96.451  1.00 16.88 ? 272  ARG   B CZ    1 
ATOM   10938 N  NH1   . ARG   B  1  274  ? 16.284  18.055  96.568  1.00 17.19 ? 272  ARG   B NH1   1 
ATOM   10939 N  NH2   . ARG   B  1  274  ? 14.424  18.173  95.239  1.00 17.75 ? 272  ARG   B NH2   1 
ATOM   10940 N  N     . TYR   B  1  275  ? 10.381  15.673  100.522 1.00 15.44 ? 273  TYR   B N     1 
ATOM   10941 C  CA    . TYR   B  1  275  ? 9.233   14.793  100.360 1.00 15.65 ? 273  TYR   B CA    1 
ATOM   10942 C  C     . TYR   B  1  275  ? 8.572   15.153  99.035  1.00 16.03 ? 273  TYR   B C     1 
ATOM   10943 O  O     . TYR   B  1  275  ? 7.741   16.055  98.949  1.00 16.11 ? 273  TYR   B O     1 
ATOM   10944 C  CB    . TYR   B  1  275  ? 8.289   14.926  101.547 1.00 16.41 ? 273  TYR   B CB    1 
ATOM   10945 C  CG    . TYR   B  1  275  ? 7.028   14.127  101.391 1.00 15.49 ? 273  TYR   B CG    1 
ATOM   10946 C  CD1   . TYR   B  1  275  ? 7.077   12.795  100.998 1.00 16.80 ? 273  TYR   B CD1   1 
ATOM   10947 C  CD2   . TYR   B  1  275  ? 5.792   14.700  101.623 1.00 15.81 ? 273  TYR   B CD2   1 
ATOM   10948 C  CE1   . TYR   B  1  275  ? 5.922   12.058  100.835 1.00 17.42 ? 273  TYR   B CE1   1 
ATOM   10949 C  CE2   . TYR   B  1  275  ? 4.637   13.980  101.460 1.00 15.30 ? 273  TYR   B CE2   1 
ATOM   10950 C  CZ    . TYR   B  1  275  ? 4.710   12.658  101.066 1.00 16.97 ? 273  TYR   B CZ    1 
ATOM   10951 O  OH    . TYR   B  1  275  ? 3.567   11.933  100.889 1.00 17.96 ? 273  TYR   B OH    1 
ATOM   10952 N  N     . SER   B  1  276  ? 8.955   14.443  97.979  1.00 14.55 ? 274  SER   B N     1 
ATOM   10953 C  CA    A SER   B  1  276  ? 8.411   14.720  96.659  0.66 15.16 ? 274  SER   B CA    1 
ATOM   10954 C  CA    B SER   B  1  276  ? 8.459   14.741  96.644  0.34 15.22 ? 274  SER   B CA    1 
ATOM   10955 C  C     . SER   B  1  276  ? 8.674   13.523  95.764  1.00 15.52 ? 274  SER   B C     1 
ATOM   10956 O  O     . SER   B  1  276  ? 9.574   12.718  96.013  1.00 16.08 ? 274  SER   B O     1 
ATOM   10957 C  CB    A SER   B  1  276  ? 9.042   15.967  96.041  0.66 18.16 ? 274  SER   B CB    1 
ATOM   10958 C  CB    B SER   B  1  276  ? 9.190   15.941  96.032  0.34 18.09 ? 274  SER   B CB    1 
ATOM   10959 O  OG    A SER   B  1  276  ? 10.384  15.703  95.696  0.66 17.89 ? 274  SER   B OG    1 
ATOM   10960 O  OG    B SER   B  1  276  ? 8.970   16.008  94.635  0.34 18.82 ? 274  SER   B OG    1 
ATOM   10961 N  N     . ARG   B  1  277  ? 7.849   13.411  94.725  1.00 14.33 ? 275  ARG   B N     1 
ATOM   10962 C  CA    . ARG   B  1  277  ? 8.030   12.330  93.773  1.00 15.34 ? 275  ARG   B CA    1 
ATOM   10963 C  C     . ARG   B  1  277  ? 9.401   12.396  93.125  1.00 14.97 ? 275  ARG   B C     1 
ATOM   10964 O  O     . ARG   B  1  277  ? 10.002  11.355  92.850  1.00 16.01 ? 275  ARG   B O     1 
ATOM   10965 C  CB    . ARG   B  1  277  ? 6.920   12.382  92.725  1.00 15.38 ? 275  ARG   B CB    1 
ATOM   10966 C  CG    . ARG   B  1  277  ? 7.086   11.422  91.553  1.00 16.40 ? 275  ARG   B CG    1 
ATOM   10967 C  CD    . ARG   B  1  277  ? 7.128   9.972   92.018  1.00 16.07 ? 275  ARG   B CD    1 
ATOM   10968 N  NE    . ARG   B  1  277  ? 7.288   9.041   90.907  1.00 16.11 ? 275  ARG   B NE    1 
ATOM   10969 C  CZ    . ARG   B  1  277  ? 8.460   8.668   90.411  1.00 16.04 ? 275  ARG   B CZ    1 
ATOM   10970 N  NH1   . ARG   B  1  277  ? 9.598   9.189   90.854  1.00 18.01 ? 275  ARG   B NH1   1 
ATOM   10971 N  NH2   . ARG   B  1  277  ? 8.491   7.733   89.461  1.00 17.17 ? 275  ARG   B NH2   1 
ATOM   10972 N  N     . ALA   B  1  278  ? 9.919   13.603  92.903  1.00 15.20 ? 276  ALA   B N     1 
ATOM   10973 C  CA    . ALA   B  1  278  ? 11.241  13.732  92.300  1.00 16.05 ? 276  ALA   B CA    1 
ATOM   10974 C  C     . ALA   B  1  278  ? 12.313  13.084  93.158  1.00 16.49 ? 276  ALA   B C     1 
ATOM   10975 O  O     . ALA   B  1  278  ? 13.370  12.689  92.644  1.00 18.02 ? 276  ALA   B O     1 
ATOM   10976 C  CB    . ALA   B  1  278  ? 11.574  15.205  92.062  1.00 17.06 ? 276  ALA   B CB    1 
ATOM   10977 N  N     . GLN   B  1  279  ? 12.075  12.980  94.460  1.00 15.16 ? 277  GLN   B N     1 
ATOM   10978 C  CA    . GLN   B  1  279  ? 13.022  12.365  95.382  1.00 15.65 ? 277  GLN   B CA    1 
ATOM   10979 C  C     . GLN   B  1  279  ? 12.464  11.075  95.973  1.00 15.58 ? 277  GLN   B C     1 
ATOM   10980 O  O     . GLN   B  1  279  ? 12.722  10.749  97.129  1.00 16.01 ? 277  GLN   B O     1 
ATOM   10981 C  CB    . GLN   B  1  279  ? 13.446  13.343  96.478  1.00 16.63 ? 277  GLN   B CB    1 
ATOM   10982 C  CG    . GLN   B  1  279  ? 14.080  14.607  95.919  1.00 16.10 ? 277  GLN   B CG    1 
ATOM   10983 C  CD    . GLN   B  1  279  ? 15.372  14.308  95.174  1.00 19.98 ? 277  GLN   B CD    1 
ATOM   10984 O  OE1   . GLN   B  1  279  ? 16.041  13.301  95.426  1.00 22.54 ? 277  GLN   B OE1   1 
ATOM   10985 N  NE2   . GLN   B  1  279  ? 15.721  15.177  94.240  1.00 17.24 ? 277  GLN   B NE2   1 
ATOM   10986 N  N     . ALA   B  1  280  ? 11.705  10.326  95.172  1.00 17.11 ? 278  ALA   B N     1 
ATOM   10987 C  CA    . ALA   B  1  280  ? 11.010  9.156   95.690  1.00 17.60 ? 278  ALA   B CA    1 
ATOM   10988 C  C     . ALA   B  1  280  ? 11.974  8.167   96.336  1.00 17.68 ? 278  ALA   B C     1 
ATOM   10989 O  O     . ALA   B  1  280  ? 11.649  7.557   97.358  1.00 17.83 ? 278  ALA   B O     1 
ATOM   10990 C  CB    . ALA   B  1  280  ? 10.212  8.483   94.572  1.00 18.89 ? 278  ALA   B CB    1 
ATOM   10991 N  N     . ALA   B  1  281  ? 13.167  7.996   95.762  1.00 16.99 ? 279  ALA   B N     1 
ATOM   10992 C  CA    . ALA   B  1  281  ? 14.109  7.047   96.350  1.00 18.82 ? 279  ALA   B CA    1 
ATOM   10993 C  C     . ALA   B  1  281  ? 14.500  7.473   97.759  1.00 17.41 ? 279  ALA   B C     1 
ATOM   10994 O  O     . ALA   B  1  281  ? 14.555  6.643   98.674  1.00 18.63 ? 279  ALA   B O     1 
ATOM   10995 C  CB    . ALA   B  1  281  ? 15.352  6.899   95.470  1.00 19.49 ? 279  ALA   B CB    1 
ATOM   10996 N  N     . ARG   B  1  282  ? 14.760  8.764   97.959  1.00 16.84 ? 280  ARG   B N     1 
ATOM   10997 C  CA    . ARG   B  1  282  ? 15.101  9.233   99.296  1.00 16.34 ? 280  ARG   B CA    1 
ATOM   10998 C  C     . ARG   B  1  282  ? 13.909  9.142   100.231 1.00 16.37 ? 280  ARG   B C     1 
ATOM   10999 O  O     . ARG   B  1  282  ? 14.070  8.858   101.421 1.00 18.01 ? 280  ARG   B O     1 
ATOM   11000 C  CB    . ARG   B  1  282  ? 15.621  10.666  99.243  1.00 19.24 ? 280  ARG   B CB    1 
ATOM   11001 C  CG    . ARG   B  1  282  ? 16.964  10.804  98.553  1.00 19.46 ? 280  ARG   B CG    1 
ATOM   11002 C  CD    . ARG   B  1  282  ? 17.502  12.198  98.793  1.00 21.61 ? 280  ARG   B CD    1 
ATOM   11003 N  NE    . ARG   B  1  282  ? 17.814  12.385  100.205 1.00 21.31 ? 280  ARG   B NE    1 
ATOM   11004 C  CZ    . ARG   B  1  282  ? 17.970  13.563  100.787 1.00 18.51 ? 280  ARG   B CZ    1 
ATOM   11005 N  NH1   . ARG   B  1  282  ? 17.844  14.692  100.106 1.00 20.24 ? 280  ARG   B NH1   1 
ATOM   11006 N  NH2   . ARG   B  1  282  ? 18.255  13.612  102.086 1.00 19.33 ? 280  ARG   B NH2   1 
ATOM   11007 N  N     . VAL   B  1  283  ? 12.709  9.385   99.714  1.00 15.98 ? 281  VAL   B N     1 
ATOM   11008 C  CA    . VAL   B  1  283  ? 11.512  9.251   100.535 1.00 17.41 ? 281  VAL   B CA    1 
ATOM   11009 C  C     . VAL   B  1  283  ? 11.381  7.824   101.043 1.00 16.91 ? 281  VAL   B C     1 
ATOM   11010 O  O     . VAL   B  1  283  ? 11.203  7.588   102.246 1.00 17.83 ? 281  VAL   B O     1 
ATOM   11011 C  CB    . VAL   B  1  283  ? 10.280  9.710   99.741  1.00 15.95 ? 281  VAL   B CB    1 
ATOM   11012 C  CG1   . VAL   B  1  283  ? 9.000   9.311   100.450 1.00 18.50 ? 281  VAL   B CG1   1 
ATOM   11013 C  CG2   . VAL   B  1  283  ? 10.334  11.213  99.582  1.00 17.31 ? 281  VAL   B CG2   1 
ATOM   11014 N  N     . MET   B  1  284  ? 11.510  6.846   100.145 1.00 17.31 ? 282  MET   B N     1 
ATOM   11015 C  CA    . MET   B  1  284  ? 11.370  5.462   100.567 1.00 17.67 ? 282  MET   B CA    1 
ATOM   11016 C  C     . MET   B  1  284  ? 12.536  5.028   101.444 1.00 19.72 ? 282  MET   B C     1 
ATOM   11017 O  O     . MET   B  1  284  ? 12.354  4.215   102.358 1.00 21.30 ? 282  MET   B O     1 
ATOM   11018 C  CB    . MET   B  1  284  ? 11.236  4.550   99.350  1.00 18.87 ? 282  MET   B CB    1 
ATOM   11019 C  CG    . MET   B  1  284  ? 10.017  4.860   98.491  1.00 18.81 ? 282  MET   B CG    1 
ATOM   11020 S  SD    . MET   B  1  284  ? 8.454   4.779   99.380  1.00 22.40 ? 282  MET   B SD    1 
ATOM   11021 C  CE    . MET   B  1  284  ? 8.351   3.018   99.676  1.00 25.88 ? 282  MET   B CE    1 
ATOM   11022 N  N     . GLY   B  1  285  ? 13.730  5.563   101.192 1.00 19.04 ? 283  GLY   B N     1 
ATOM   11023 C  CA    . GLY   B  1  285  ? 14.899  5.127   101.937 1.00 20.59 ? 283  GLY   B CA    1 
ATOM   11024 C  C     . GLY   B  1  285  ? 15.054  5.789   103.285 1.00 20.46 ? 283  GLY   B C     1 
ATOM   11025 O  O     . GLY   B  1  285  ? 15.603  5.183   104.211 1.00 22.59 ? 283  GLY   B O     1 
ATOM   11026 N  N     . GLU   B  1  286  ? 14.581  7.028   103.419 1.00 18.27 ? 284  GLU   B N     1 
ATOM   11027 C  CA    . GLU   B  1  286  ? 14.837  7.852   104.590 1.00 16.85 ? 284  GLU   B CA    1 
ATOM   11028 C  C     . GLU   B  1  286  ? 13.580  8.277   105.321 1.00 20.68 ? 284  GLU   B C     1 
ATOM   11029 O  O     . GLU   B  1  286  ? 13.571  8.287   106.556 1.00 22.88 ? 284  GLU   B O     1 
ATOM   11030 C  CB    . GLU   B  1  286  ? 15.615  9.106   104.181 1.00 19.77 ? 284  GLU   B CB    1 
ATOM   11031 C  CG    . GLU   B  1  286  ? 16.850  8.795   103.345 1.00 21.19 ? 284  GLU   B CG    1 
ATOM   11032 C  CD    . GLU   B  1  286  ? 17.489  10.041  102.756 1.00 23.80 ? 284  GLU   B CD    1 
ATOM   11033 O  OE1   . GLU   B  1  286  ? 17.285  11.149  103.304 1.00 23.73 ? 284  GLU   B OE1   1 
ATOM   11034 O  OE2   . GLU   B  1  286  ? 18.194  9.904   101.737 1.00 25.08 ? 284  GLU   B OE2   1 
ATOM   11035 N  N     . LEU   B  1  287  ? 12.527  8.649   104.597 1.00 18.67 ? 285  LEU   B N     1 
ATOM   11036 C  CA    . LEU   B  1  287  ? 11.294  9.062   105.252 1.00 19.24 ? 285  LEU   B CA    1 
ATOM   11037 C  C     . LEU   B  1  287  ? 10.529  7.855   105.764 1.00 21.33 ? 285  LEU   B C     1 
ATOM   11038 O  O     . LEU   B  1  287  ? 10.107  7.829   106.922 1.00 18.70 ? 285  LEU   B O     1 
ATOM   11039 C  CB    . LEU   B  1  287  ? 10.443  9.880   104.280 1.00 18.55 ? 285  LEU   B CB    1 
ATOM   11040 C  CG    . LEU   B  1  287  ? 9.406   10.857  104.853 1.00 19.54 ? 285  LEU   B CG    1 
ATOM   11041 C  CD1   . LEU   B  1  287  ? 8.849   11.696  103.740 1.00 19.08 ? 285  LEU   B CD1   1 
ATOM   11042 C  CD2   . LEU   B  1  287  ? 8.268   10.161  105.562 1.00 19.74 ? 285  LEU   B CD2   1 
ATOM   11043 N  N     . LEU   B  1  288  ? 10.345  6.850   104.916 1.00 18.43 ? 286  LEU   B N     1 
ATOM   11044 C  CA    . LEU   B  1  288  ? 9.571   5.673   105.306 1.00 18.60 ? 286  LEU   B CA    1 
ATOM   11045 C  C     . LEU   B  1  288  ? 10.045  5.037   106.606 1.00 20.05 ? 286  LEU   B C     1 
ATOM   11046 O  O     . LEU   B  1  288  ? 9.200   4.772   107.475 1.00 19.11 ? 286  LEU   B O     1 
ATOM   11047 C  CB    . LEU   B  1  288  ? 9.499   4.690   104.129 1.00 22.22 ? 286  LEU   B CB    1 
ATOM   11048 C  CG    . LEU   B  1  288  ? 8.911   3.325   104.474 1.00 23.59 ? 286  LEU   B CG    1 
ATOM   11049 C  CD1   . LEU   B  1  288  ? 7.473   3.455   104.959 1.00 22.26 ? 286  LEU   B CD1   1 
ATOM   11050 C  CD2   . LEU   B  1  288  ? 8.994   2.405   103.277 1.00 29.27 ? 286  LEU   B CD2   1 
ATOM   11051 N  N     . PRO   B  1  289  ? 11.340  4.786   106.823 1.00 19.87 ? 287  PRO   B N     1 
ATOM   11052 C  CA    . PRO   B  1  289  ? 11.750  4.201   108.113 1.00 19.89 ? 287  PRO   B CA    1 
ATOM   11053 C  C     . PRO   B  1  289  ? 11.337  5.028   109.314 1.00 19.36 ? 287  PRO   B C     1 
ATOM   11054 O  O     . PRO   B  1  289  ? 11.072  4.464   110.382 1.00 20.16 ? 287  PRO   B O     1 
ATOM   11055 C  CB    . PRO   B  1  289  ? 13.274  4.108   107.984 1.00 24.71 ? 287  PRO   B CB    1 
ATOM   11056 C  CG    . PRO   B  1  289  ? 13.494  3.959   106.507 1.00 25.20 ? 287  PRO   B CG    1 
ATOM   11057 C  CD    . PRO   B  1  289  ? 12.472  4.859   105.878 1.00 21.96 ? 287  PRO   B CD    1 
ATOM   11058 N  N     . ARG   B  1  290  ? 11.275  6.351   109.170 1.00 18.22 ? 288  ARG   B N     1 
ATOM   11059 C  CA    A ARG   B  1  290  ? 10.815  7.191   110.268 0.48 19.47 ? 288  ARG   B CA    1 
ATOM   11060 C  CA    B ARG   B  1  290  ? 10.814  7.193   110.267 0.52 19.47 ? 288  ARG   B CA    1 
ATOM   11061 C  C     . ARG   B  1  290  ? 9.331   6.985   110.545 1.00 17.62 ? 288  ARG   B C     1 
ATOM   11062 O  O     . ARG   B  1  290  ? 8.921   6.883   111.708 1.00 18.78 ? 288  ARG   B O     1 
ATOM   11063 C  CB    A ARG   B  1  290  ? 11.141  8.650   109.970 0.48 20.53 ? 288  ARG   B CB    1 
ATOM   11064 C  CB    B ARG   B  1  290  ? 11.128  8.657   109.972 0.52 20.52 ? 288  ARG   B CB    1 
ATOM   11065 C  CG    A ARG   B  1  290  ? 12.639  8.861   109.854 0.48 22.82 ? 288  ARG   B CG    1 
ATOM   11066 C  CG    B ARG   B  1  290  ? 12.605  8.976   110.139 0.52 23.37 ? 288  ARG   B CG    1 
ATOM   11067 C  CD    A ARG   B  1  290  ? 12.991  10.141  109.143 0.48 24.29 ? 288  ARG   B CD    1 
ATOM   11068 C  CD    B ARG   B  1  290  ? 12.963  10.314  109.531 0.52 23.92 ? 288  ARG   B CD    1 
ATOM   11069 N  NE    A ARG   B  1  290  ? 14.432  10.251  108.958 0.48 23.28 ? 288  ARG   B NE    1 
ATOM   11070 N  NE    B ARG   B  1  290  ? 14.194  10.860  110.091 0.52 22.93 ? 288  ARG   B NE    1 
ATOM   11071 C  CZ    A ARG   B  1  290  ? 15.012  11.091  108.115 0.48 23.69 ? 288  ARG   B CZ    1 
ATOM   11072 C  CZ    B ARG   B  1  290  ? 14.753  12.002  109.711 0.52 25.26 ? 288  ARG   B CZ    1 
ATOM   11073 N  NH1   A ARG   B  1  290  ? 14.299  11.906  107.353 0.48 18.01 ? 288  ARG   B NH1   1 
ATOM   11074 N  NH1   B ARG   B  1  290  ? 14.210  12.760  108.772 0.52 24.15 ? 288  ARG   B NH1   1 
ATOM   11075 N  NH2   A ARG   B  1  290  ? 16.340  11.106  108.025 0.48 24.37 ? 288  ARG   B NH2   1 
ATOM   11076 N  NH2   B ARG   B  1  290  ? 15.876  12.402  110.296 0.52 27.27 ? 288  ARG   B NH2   1 
ATOM   11077 N  N     . VAL   B  1  291  ? 8.511   6.907   109.493 1.00 19.57 ? 289  VAL   B N     1 
ATOM   11078 C  CA    . VAL   B  1  291  ? 7.092   6.659   109.726 1.00 18.19 ? 289  VAL   B CA    1 
ATOM   11079 C  C     . VAL   B  1  291  ? 6.905   5.292   110.350 1.00 18.17 ? 289  VAL   B C     1 
ATOM   11080 O  O     . VAL   B  1  291  ? 6.097   5.113   111.275 1.00 19.80 ? 289  VAL   B O     1 
ATOM   11081 C  CB    . VAL   B  1  291  ? 6.286   6.787   108.426 1.00 20.49 ? 289  VAL   B CB    1 
ATOM   11082 C  CG1   . VAL   B  1  291  ? 4.798   6.659   108.741 1.00 23.32 ? 289  VAL   B CG1   1 
ATOM   11083 C  CG2   . VAL   B  1  291  ? 6.589   8.094   107.742 1.00 21.17 ? 289  VAL   B CG2   1 
ATOM   11084 N  N     . LYS   B  1  292  ? 7.652   4.302   109.859 1.00 18.73 ? 290  LYS   B N     1 
ATOM   11085 C  CA    . LYS   B  1  292  ? 7.535   2.965   110.426 1.00 19.32 ? 290  LYS   B CA    1 
ATOM   11086 C  C     . LYS   B  1  292  ? 7.849   2.981   111.916 1.00 20.02 ? 290  LYS   B C     1 
ATOM   11087 O  O     . LYS   B  1  292  ? 7.140   2.358   112.715 1.00 20.88 ? 290  LYS   B O     1 
ATOM   11088 C  CB    . LYS   B  1  292  ? 8.456   1.992   109.689 1.00 22.11 ? 290  LYS   B CB    1 
ATOM   11089 C  CG    . LYS   B  1  292  ? 8.270   0.525   110.112 1.00 24.73 ? 290  LYS   B CG    1 
ATOM   11090 C  CD    . LYS   B  1  292  ? 9.195   0.114   111.236 1.00 33.43 ? 290  LYS   B CD    1 
ATOM   11091 C  CE    . LYS   B  1  292  ? 8.897   -1.316  111.695 1.00 31.97 ? 290  LYS   B CE    1 
ATOM   11092 N  NZ    . LYS   B  1  292  ? 9.257   -2.330  110.671 1.00 31.97 ? 290  LYS   B NZ    1 
ATOM   11093 N  N     . ALA   B  1  293  ? 8.905   3.700   112.307 1.00 19.38 ? 291  ALA   B N     1 
ATOM   11094 C  CA    . ALA   B  1  293  ? 9.264   3.756   113.719 1.00 20.36 ? 291  ALA   B CA    1 
ATOM   11095 C  C     . ALA   B  1  293  ? 8.146   4.376   114.544 1.00 22.15 ? 291  ALA   B C     1 
ATOM   11096 O  O     . ALA   B  1  293  ? 7.815   3.885   115.632 1.00 21.60 ? 291  ALA   B O     1 
ATOM   11097 C  CB    . ALA   B  1  293  ? 10.563  4.538   113.889 1.00 21.79 ? 291  ALA   B CB    1 
ATOM   11098 N  N     . LEU   B  1  294  ? 7.563   5.470   114.051 1.00 18.42 ? 292  LEU   B N     1 
ATOM   11099 C  CA    . LEU   B  1  294  ? 6.446   6.082   114.757 1.00 20.03 ? 292  LEU   B CA    1 
ATOM   11100 C  C     . LEU   B  1  294  ? 5.248   5.146   114.796 1.00 19.54 ? 292  LEU   B C     1 
ATOM   11101 O  O     . LEU   B  1  294  ? 4.571   5.038   115.822 1.00 20.62 ? 292  LEU   B O     1 
ATOM   11102 C  CB    . LEU   B  1  294  ? 6.063   7.401   114.096 1.00 17.97 ? 292  LEU   B CB    1 
ATOM   11103 C  CG    . LEU   B  1  294  ? 7.172   8.449   114.081 1.00 19.35 ? 292  LEU   B CG    1 
ATOM   11104 C  CD1   . LEU   B  1  294  ? 6.723   9.646   113.292 1.00 18.51 ? 292  LEU   B CD1   1 
ATOM   11105 C  CD2   . LEU   B  1  294  ? 7.546   8.844   115.499 1.00 20.60 ? 292  LEU   B CD2   1 
ATOM   11106 N  N     . ALA   B  1  295  ? 4.963   4.466   113.685 1.00 19.38 ? 293  ALA   B N     1 
ATOM   11107 C  CA    . ALA   B  1  295  ? 3.827   3.554   113.655 1.00 20.35 ? 293  ALA   B CA    1 
ATOM   11108 C  C     . ALA   B  1  295  ? 4.032   2.402   114.626 1.00 23.10 ? 293  ALA   B C     1 
ATOM   11109 O  O     . ALA   B  1  295  ? 3.088   1.966   115.293 1.00 21.50 ? 293  ALA   B O     1 
ATOM   11110 C  CB    . ALA   B  1  295  ? 3.612   3.043   112.226 1.00 22.02 ? 293  ALA   B CB    1 
ATOM   11111 N  N     . LEU   B  1  296  ? 5.264   1.907   114.729 1.00 21.46 ? 294  LEU   B N     1 
ATOM   11112 C  CA    . LEU   B  1  296  ? 5.554   0.843   115.682 1.00 23.04 ? 294  LEU   B CA    1 
ATOM   11113 C  C     . LEU   B  1  296  ? 5.301   1.305   117.109 1.00 23.27 ? 294  LEU   B C     1 
ATOM   11114 O  O     . LEU   B  1  296  ? 4.744   0.557   117.921 1.00 23.96 ? 294  LEU   B O     1 
ATOM   11115 C  CB    . LEU   B  1  296  ? 6.997   0.384   115.503 1.00 25.02 ? 294  LEU   B CB    1 
ATOM   11116 C  CG    . LEU   B  1  296  ? 7.453   -0.804  116.340 1.00 28.58 ? 294  LEU   B CG    1 
ATOM   11117 C  CD1   . LEU   B  1  296  ? 6.493   -1.977  116.164 1.00 30.36 ? 294  LEU   B CD1   1 
ATOM   11118 C  CD2   . LEU   B  1  296  ? 8.875   -1.191  115.945 1.00 34.54 ? 294  LEU   B CD2   1 
ATOM   11119 N  N     . LEU   B  1  297  ? 5.689   2.542   117.432 1.00 21.31 ? 295  LEU   B N     1 
ATOM   11120 C  CA    . LEU   B  1  297  ? 5.380   3.077   118.757 1.00 22.19 ? 295  LEU   B CA    1 
ATOM   11121 C  C     . LEU   B  1  297  ? 3.873   3.182   118.968 1.00 22.09 ? 295  LEU   B C     1 
ATOM   11122 O  O     . LEU   B  1  297  ? 3.349   2.796   120.022 1.00 21.96 ? 295  LEU   B O     1 
ATOM   11123 C  CB    . LEU   B  1  297  ? 6.035   4.449   118.932 1.00 21.25 ? 295  LEU   B CB    1 
ATOM   11124 C  CG    . LEU   B  1  297  ? 7.546   4.508   119.146 1.00 27.14 ? 295  LEU   B CG    1 
ATOM   11125 C  CD1   . LEU   B  1  297  ? 7.985   5.965   119.179 1.00 26.19 ? 295  LEU   B CD1   1 
ATOM   11126 C  CD2   . LEU   B  1  297  ? 7.952   3.799   120.431 1.00 29.58 ? 295  LEU   B CD2   1 
ATOM   11127 N  N     . ALA   B  1  298  ? 3.155   3.712   117.978 1.00 21.67 ? 296  ALA   B N     1 
ATOM   11128 C  CA    . ALA   B  1  298  ? 1.704   3.797   118.098 1.00 20.72 ? 296  ALA   B CA    1 
ATOM   11129 C  C     . ALA   B  1  298  ? 1.084   2.417   118.257 1.00 24.52 ? 296  ALA   B C     1 
ATOM   11130 O  O     . ALA   B  1  298  ? 0.151   2.233   119.049 1.00 24.22 ? 296  ALA   B O     1 
ATOM   11131 C  CB    . ALA   B  1  298  ? 1.116   4.500   116.877 1.00 20.55 ? 296  ALA   B CB    1 
ATOM   11132 N  N     . LYS   B  1  299  ? 1.589   1.433   117.512 1.00 22.40 ? 297  LYS   B N     1 
ATOM   11133 C  CA    . LYS   B  1  299  ? 1.072   0.076   117.652 1.00 23.87 ? 297  LYS   B CA    1 
ATOM   11134 C  C     . LYS   B  1  299  ? 1.291   -0.447  119.061 1.00 27.19 ? 297  LYS   B C     1 
ATOM   11135 O  O     . LYS   B  1  299  ? 0.395   -1.070  119.647 1.00 27.60 ? 297  LYS   B O     1 
ATOM   11136 C  CB    . LYS   B  1  299  ? 1.750   -0.850  116.646 1.00 27.51 ? 297  LYS   B CB    1 
ATOM   11137 C  CG    . LYS   B  1  299  ? 1.490   -2.319  116.942 1.00 29.68 ? 297  LYS   B CG    1 
ATOM   11138 C  CD    . LYS   B  1  299  ? 2.529   -3.207  116.302 1.00 37.67 ? 297  LYS   B CD    1 
ATOM   11139 C  CE    . LYS   B  1  299  ? 2.103   -4.660  116.372 1.00 37.22 ? 297  LYS   B CE    1 
ATOM   11140 N  NZ    . LYS   B  1  299  ? 1.884   -5.099  117.771 1.00 40.29 ? 297  LYS   B NZ    1 
ATOM   11141 N  N     . ASN   B  1  300  ? 2.479   -0.209  119.621 1.00 25.10 ? 298  ASN   B N     1 
ATOM   11142 C  CA    . ASN   B  1  300  ? 2.780   -0.724  120.952 1.00 26.13 ? 298  ASN   B CA    1 
ATOM   11143 C  C     . ASN   B  1  300  ? 1.839   -0.151  121.999 1.00 27.11 ? 298  ASN   B C     1 
ATOM   11144 O  O     . ASN   B  1  300  ? 1.482   -0.847  122.955 1.00 28.17 ? 298  ASN   B O     1 
ATOM   11145 C  CB    . ASN   B  1  300  ? 4.245   -0.453  121.304 1.00 27.93 ? 298  ASN   B CB    1 
ATOM   11146 C  CG    . ASN   B  1  300  ? 5.209   -1.300  120.475 1.00 31.09 ? 298  ASN   B CG    1 
ATOM   11147 O  OD1   . ASN   B  1  300  ? 4.832   -2.345  119.946 1.00 38.02 ? 298  ASN   B OD1   1 
ATOM   11148 N  ND2   . ASN   B  1  300  ? 6.458   -0.853  120.369 1.00 39.56 ? 298  ASN   B ND2   1 
ATOM   11149 N  N     . TYR   B  1  301  ? 1.405   1.094   121.826 1.00 23.97 ? 299  TYR   B N     1 
ATOM   11150 C  CA    . TYR   B  1  301  ? 0.436   1.700   122.728 1.00 23.96 ? 299  TYR   B CA    1 
ATOM   11151 C  C     . TYR   B  1  301  ? -0.998  1.464   122.291 1.00 21.40 ? 299  TYR   B C     1 
ATOM   11152 O  O     . TYR   B  1  301  ? -1.918  1.853   123.014 1.00 26.45 ? 299  TYR   B O     1 
ATOM   11153 C  CB    . TYR   B  1  301  ? 0.673   3.207   122.826 1.00 22.49 ? 299  TYR   B CB    1 
ATOM   11154 C  CG    . TYR   B  1  301  ? 1.914   3.596   123.596 1.00 23.29 ? 299  TYR   B CG    1 
ATOM   11155 C  CD1   . TYR   B  1  301  ? 1.986   3.420   124.974 1.00 23.06 ? 299  TYR   B CD1   1 
ATOM   11156 C  CD2   . TYR   B  1  301  ? 3.004   4.154   122.946 1.00 24.05 ? 299  TYR   B CD2   1 
ATOM   11157 C  CE1   . TYR   B  1  301  ? 3.123   3.780   125.681 1.00 22.68 ? 299  TYR   B CE1   1 
ATOM   11158 C  CE2   . TYR   B  1  301  ? 4.137   4.523   123.634 1.00 24.14 ? 299  TYR   B CE2   1 
ATOM   11159 C  CZ    . TYR   B  1  301  ? 4.191   4.334   124.999 1.00 23.52 ? 299  TYR   B CZ    1 
ATOM   11160 O  OH    . TYR   B  1  301  ? 5.315   4.699   125.687 1.00 25.18 ? 299  TYR   B OH    1 
ATOM   11161 N  N     . ASP   B  1  302  ? -1.196  0.843   121.130 1.00 22.18 ? 300  ASP   B N     1 
ATOM   11162 C  CA    . ASP   B  1  302  ? -2.503  0.663   120.503 1.00 25.12 ? 300  ASP   B CA    1 
ATOM   11163 C  C     . ASP   B  1  302  ? -3.272  1.981   120.403 1.00 22.31 ? 300  ASP   B C     1 
ATOM   11164 O  O     . ASP   B  1  302  ? -4.398  2.127   120.885 1.00 24.94 ? 300  ASP   B O     1 
ATOM   11165 C  CB    . ASP   B  1  302  ? -3.329  -0.443  121.162 1.00 24.98 ? 300  ASP   B CB    1 
ATOM   11166 C  CG    . ASP   B  1  302  ? -4.422  -0.955  120.243 1.00 27.59 ? 300  ASP   B CG    1 
ATOM   11167 O  OD1   . ASP   B  1  302  ? -4.257  -0.830  119.004 1.00 29.19 ? 300  ASP   B OD1   1 
ATOM   11168 O  OD2   . ASP   B  1  302  ? -5.441  -1.452  120.748 1.00 33.56 ? 300  ASP   B OD2   1 
ATOM   11169 N  N     . ILE   B  1  303  ? -2.624  2.955   119.775 1.00 20.80 ? 301  ILE   B N     1 
ATOM   11170 C  CA    . ILE   B  1  303  ? -3.263  4.218   119.440 1.00 20.64 ? 301  ILE   B CA    1 
ATOM   11171 C  C     . ILE   B  1  303  ? -3.302  4.341   117.923 1.00 23.14 ? 301  ILE   B C     1 
ATOM   11172 O  O     . ILE   B  1  303  ? -2.580  3.652   117.197 1.00 21.42 ? 301  ILE   B O     1 
ATOM   11173 C  CB    . ILE   B  1  303  ? -2.559  5.445   120.064 1.00 21.21 ? 301  ILE   B CB    1 
ATOM   11174 C  CG1   . ILE   B  1  303  ? -1.200  5.674   119.402 1.00 22.18 ? 301  ILE   B CG1   1 
ATOM   11175 C  CG2   . ILE   B  1  303  ? -2.389  5.273   121.561 1.00 21.35 ? 301  ILE   B CG2   1 
ATOM   11176 C  CD1   . ILE   B  1  303  ? -0.531  6.980   119.816 1.00 24.34 ? 301  ILE   B CD1   1 
ATOM   11177 N  N     . GLY   B  1  304  ? -4.152  5.247   117.446 1.00 20.46 ? 302  GLY   B N     1 
ATOM   11178 C  CA    . GLY   B  1  304  ? -4.189  5.542   116.024 1.00 19.85 ? 302  GLY   B CA    1 
ATOM   11179 C  C     . GLY   B  1  304  ? -3.054  6.477   115.632 1.00 20.04 ? 302  GLY   B C     1 
ATOM   11180 O  O     . GLY   B  1  304  ? -2.658  7.364   116.388 1.00 20.87 ? 302  GLY   B O     1 
ATOM   11181 N  N     . LEU   B  1  305  ? -2.525  6.265   114.431 1.00 17.60 ? 303  LEU   B N     1 
ATOM   11182 C  CA    . LEU   B  1  305  ? -1.534  7.156   113.843 1.00 19.88 ? 303  LEU   B CA    1 
ATOM   11183 C  C     . LEU   B  1  305  ? -2.018  7.449   112.436 1.00 20.10 ? 303  LEU   B C     1 
ATOM   11184 O  O     . LEU   B  1  305  ? -2.079  6.543   111.598 1.00 20.60 ? 303  LEU   B O     1 
ATOM   11185 C  CB    . LEU   B  1  305  ? -0.141  6.527   113.818 1.00 20.14 ? 303  LEU   B CB    1 
ATOM   11186 C  CG    . LEU   B  1  305  ? 0.949   7.438   113.231 1.00 20.91 ? 303  LEU   B CG    1 
ATOM   11187 C  CD1   . LEU   B  1  305  ? 2.238   7.320   114.018 1.00 23.71 ? 303  LEU   B CD1   1 
ATOM   11188 C  CD2   . LEU   B  1  305  ? 1.198   7.128   111.762 1.00 24.65 ? 303  LEU   B CD2   1 
ATOM   11189 N  N     . ASN   B  1  306  ? -2.359  8.702   112.185 1.00 17.64 ? 304  ASN   B N     1 
ATOM   11190 C  CA    . ASN   B  1  306  ? -2.985  9.112   110.941 1.00 17.57 ? 304  ASN   B CA    1 
ATOM   11191 C  C     . ASN   B  1  306  ? -2.000  9.915   110.106 1.00 16.61 ? 304  ASN   B C     1 
ATOM   11192 O  O     . ASN   B  1  306  ? -1.306  10.798  110.626 1.00 18.33 ? 304  ASN   B O     1 
ATOM   11193 C  CB    . ASN   B  1  306  ? -4.200  9.984   111.231 1.00 19.44 ? 304  ASN   B CB    1 
ATOM   11194 C  CG    . ASN   B  1  306  ? -4.772  10.568  109.987 1.00 19.20 ? 304  ASN   B CG    1 
ATOM   11195 O  OD1   . ASN   B  1  306  ? -5.499  9.896   109.250 1.00 21.04 ? 304  ASN   B OD1   1 
ATOM   11196 N  ND2   . ASN   B  1  306  ? -4.417  11.812  109.700 1.00 19.37 ? 304  ASN   B ND2   1 
ATOM   11197 N  N     . ILE   B  1  307  ? -1.949  9.618   108.815 1.00 17.75 ? 305  ILE   B N     1 
ATOM   11198 C  CA    . ILE   B  1  307  ? -1.147  10.389  107.876 1.00 16.82 ? 305  ILE   B CA    1 
ATOM   11199 C  C     . ILE   B  1  307  ? -2.049  11.435  107.235 1.00 17.95 ? 305  ILE   B C     1 
ATOM   11200 O  O     . ILE   B  1  307  ? -2.958  11.104  106.458 1.00 17.07 ? 305  ILE   B O     1 
ATOM   11201 C  CB    . ILE   B  1  307  ? -0.502  9.493   106.814 1.00 18.48 ? 305  ILE   B CB    1 
ATOM   11202 C  CG1   . ILE   B  1  307  ? 0.450   8.499   107.470 1.00 19.61 ? 305  ILE   B CG1   1 
ATOM   11203 C  CG2   . ILE   B  1  307  ? 0.205   10.346  105.757 1.00 19.83 ? 305  ILE   B CG2   1 
ATOM   11204 C  CD1   . ILE   B  1  307  ? 1.045   7.532   106.470 1.00 22.77 ? 305  ILE   B CD1   1 
ATOM   11205 N  N     . ASP   B  1  308  ? -1.810  12.700  107.573 1.00 17.65 ? 306  ASP   B N     1 
ATOM   11206 C  CA    . ASP   B  1  308  ? -2.569  13.788  106.975 1.00 17.35 ? 306  ASP   B CA    1 
ATOM   11207 C  C     . ASP   B  1  308  ? -2.277  13.864  105.486 1.00 17.69 ? 306  ASP   B C     1 
ATOM   11208 O  O     . ASP   B  1  308  ? -1.194  13.501  105.023 1.00 17.64 ? 306  ASP   B O     1 
ATOM   11209 C  CB    . ASP   B  1  308  ? -2.186  15.126  107.616 1.00 17.06 ? 306  ASP   B CB    1 
ATOM   11210 C  CG    . ASP   B  1  308  ? -2.660  15.257  109.054 1.00 18.30 ? 306  ASP   B CG    1 
ATOM   11211 O  OD1   . ASP   B  1  308  ? -3.496  14.455  109.509 1.00 19.05 ? 306  ASP   B OD1   1 
ATOM   11212 O  OD2   . ASP   B  1  308  ? -2.177  16.186  109.738 1.00 17.84 ? 306  ASP   B OD2   1 
ATOM   11213 N  N     . ALA   B  1  309  ? -3.244  14.360  104.733 1.00 15.94 ? 307  ALA   B N     1 
ATOM   11214 C  CA    . ALA   B  1  309  ? -3.086  14.489  103.293 1.00 14.94 ? 307  ALA   B CA    1 
ATOM   11215 C  C     . ALA   B  1  309  ? -2.678  15.910  102.956 1.00 14.74 ? 307  ALA   B C     1 
ATOM   11216 O  O     . ALA   B  1  309  ? -3.192  16.870  103.536 1.00 16.48 ? 307  ALA   B O     1 
ATOM   11217 C  CB    . ALA   B  1  309  ? -4.388  14.149  102.582 1.00 16.97 ? 307  ALA   B CB    1 
ATOM   11218 N  N     . GLU   B  1  310  ? -1.725  16.038  102.037 1.00 15.39 ? 308  GLU   B N     1 
ATOM   11219 C  CA    . GLU   B  1  310  ? -1.151  17.343  101.736 1.00 14.33 ? 308  GLU   B CA    1 
ATOM   11220 C  C     . GLU   B  1  310  ? -1.425  17.720  100.284 1.00 14.15 ? 308  GLU   B C     1 
ATOM   11221 O  O     . GLU   B  1  310  ? -2.554  17.554  99.813  1.00 14.67 ? 308  GLU   B O     1 
ATOM   11222 C  CB    . GLU   B  1  310  ? 0.332   17.341  102.120 1.00 14.08 ? 308  GLU   B CB    1 
ATOM   11223 C  CG    . GLU   B  1  310  ? 0.513   17.061  103.618 1.00 16.21 ? 308  GLU   B CG    1 
ATOM   11224 C  CD    . GLU   B  1  310  ? 1.958   17.133  104.065 1.00 16.27 ? 308  GLU   B CD    1 
ATOM   11225 O  OE1   . GLU   B  1  310  ? 2.442   18.264  104.246 1.00 18.11 ? 308  GLU   B OE1   1 
ATOM   11226 O  OE2   . GLU   B  1  310  ? 2.581   16.063  104.252 1.00 16.90 ? 308  GLU   B OE2   1 
ATOM   11227 N  N     . GLU   B  1  311  ? -0.429  18.216  99.568  1.00 14.13 ? 309  GLU   B N     1 
ATOM   11228 C  CA    . GLU   B  1  311  ? -0.673  18.686  98.217  1.00 13.21 ? 309  GLU   B CA    1 
ATOM   11229 C  C     . GLU   B  1  311  ? -0.987  17.525  97.287  1.00 15.66 ? 309  GLU   B C     1 
ATOM   11230 O  O     . GLU   B  1  311  ? -0.631  16.372  97.533  1.00 14.97 ? 309  GLU   B O     1 
ATOM   11231 C  CB    . GLU   B  1  311  ? 0.555   19.417  97.687  1.00 14.21 ? 309  GLU   B CB    1 
ATOM   11232 C  CG    . GLU   B  1  311  ? 0.853   20.719  98.424  1.00 18.08 ? 309  GLU   B CG    1 
ATOM   11233 C  CD    . GLU   B  1  311  ? 1.779   20.552  99.610  1.00 19.51 ? 309  GLU   B CD    1 
ATOM   11234 O  OE1   . GLU   B  1  311  ? 1.952   19.415  100.111 1.00 17.53 ? 309  GLU   B OE1   1 
ATOM   11235 O  OE2   . GLU   B  1  311  ? 2.349   21.583  100.041 1.00 24.76 ? 309  GLU   B OE2   1 
ATOM   11236 N  N     . ALA   B  1  312  ? -1.658  17.857  96.182  1.00 14.10 ? 310  ALA   B N     1 
ATOM   11237 C  CA    . ALA   B  1  312  ? -2.097  16.829  95.253  1.00 14.16 ? 310  ALA   B CA    1 
ATOM   11238 C  C     . ALA   B  1  312  ? -0.925  16.035  94.697  1.00 15.20 ? 310  ALA   B C     1 
ATOM   11239 O  O     . ALA   B  1  312  ? -1.059  14.833  94.460  1.00 15.12 ? 310  ALA   B O     1 
ATOM   11240 C  CB    . ALA   B  1  312  ? -2.889  17.458  94.102  1.00 14.46 ? 310  ALA   B CB    1 
ATOM   11241 N  N     . ASP   B  1  313  ? 0.231   16.675  94.504  1.00 14.49 ? 311  ASP   B N     1 
ATOM   11242 C  CA    . ASP   B  1  313  ? 1.377   15.967  93.935  1.00 15.31 ? 311  ASP   B CA    1 
ATOM   11243 C  C     . ASP   B  1  313  ? 2.089   15.065  94.932  1.00 16.51 ? 311  ASP   B C     1 
ATOM   11244 O  O     . ASP   B  1  313  ? 3.098   14.454  94.569  1.00 16.21 ? 311  ASP   B O     1 
ATOM   11245 C  CB    . ASP   B  1  313  ? 2.354   16.894  93.194  1.00 16.37 ? 311  ASP   B CB    1 
ATOM   11246 C  CG    . ASP   B  1  313  ? 3.037   17.907  94.091  1.00 17.96 ? 311  ASP   B CG    1 
ATOM   11247 O  OD1   . ASP   B  1  313  ? 2.885   17.866  95.329  1.00 17.58 ? 311  ASP   B OD1   1 
ATOM   11248 O  OD2   . ASP   B  1  313  ? 3.774   18.759  93.528  1.00 20.45 ? 311  ASP   B OD2   1 
ATOM   11249 N  N     . ARG   B  1  314  ? 1.584   14.961  96.160  1.00 14.38 ? 312  ARG   B N     1 
ATOM   11250 C  CA    . ARG   B  1  314  ? 2.109   14.038  97.154  1.00 15.55 ? 312  ARG   B CA    1 
ATOM   11251 C  C     . ARG   B  1  314  ? 1.180   12.874  97.419  1.00 15.36 ? 312  ARG   B C     1 
ATOM   11252 O  O     . ARG   B  1  314  ? 1.570   11.939  98.124  1.00 16.92 ? 312  ARG   B O     1 
ATOM   11253 C  CB    . ARG   B  1  314  ? 2.381   14.774  98.467  1.00 14.10 ? 312  ARG   B CB    1 
ATOM   11254 C  CG    . ARG   B  1  314  ? 3.661   15.571  98.371  1.00 14.82 ? 312  ARG   B CG    1 
ATOM   11255 C  CD    . ARG   B  1  314  ? 3.716   16.695  99.393  1.00 14.90 ? 312  ARG   B CD    1 
ATOM   11256 N  NE    . ARG   B  1  314  ? 5.088   17.165  99.553  1.00 15.19 ? 312  ARG   B NE    1 
ATOM   11257 C  CZ    . ARG   B  1  314  ? 5.448   18.167  100.340 1.00 14.75 ? 312  ARG   B CZ    1 
ATOM   11258 N  NH1   . ARG   B  1  314  ? 4.554   18.906  100.972 1.00 16.32 ? 312  ARG   B NH1   1 
ATOM   11259 N  NH2   . ARG   B  1  314  ? 6.743   18.414  100.522 1.00 17.86 ? 312  ARG   B NH2   1 
ATOM   11260 N  N     . LEU   B  1  315  ? -0.035  12.909  96.873  1.00 15.11 ? 313  LEU   B N     1 
ATOM   11261 C  CA    . LEU   B  1  315  ? -1.021  11.882  97.171  1.00 15.98 ? 313  LEU   B CA    1 
ATOM   11262 C  C     . LEU   B  1  315  ? -0.489  10.499  96.817  1.00 16.90 ? 313  LEU   B C     1 
ATOM   11263 O  O     . LEU   B  1  315  ? -0.444  9.596   97.662  1.00 16.75 ? 313  LEU   B O     1 
ATOM   11264 C  CB    . LEU   B  1  315  ? -2.312  12.186  96.406  1.00 15.65 ? 313  LEU   B CB    1 
ATOM   11265 C  CG    . LEU   B  1  315  ? -3.608  11.536  96.888  1.00 17.44 ? 313  LEU   B CG    1 
ATOM   11266 C  CD1   . LEU   B  1  315  ? -4.767  12.018  96.025  1.00 17.70 ? 313  LEU   B CD1   1 
ATOM   11267 C  CD2   . LEU   B  1  315  ? -3.550  10.015  96.839  1.00 19.76 ? 313  LEU   B CD2   1 
ATOM   11268 N  N     . GLU   B  1  316  ? -0.116  10.299  95.555  1.00 16.71 ? 314  GLU   B N     1 
ATOM   11269 C  CA    . GLU   B  1  316  ? 0.217   8.947   95.130  1.00 16.54 ? 314  GLU   B CA    1 
ATOM   11270 C  C     . GLU   B  1  316  ? 1.518   8.473   95.759  1.00 16.72 ? 314  GLU   B C     1 
ATOM   11271 O  O     . GLU   B  1  316  ? 1.638   7.302   96.132  1.00 17.74 ? 314  GLU   B O     1 
ATOM   11272 C  CB    . GLU   B  1  316  ? 0.229   8.862   93.609  1.00 16.99 ? 314  GLU   B CB    1 
ATOM   11273 C  CG    . GLU   B  1  316  ? -1.185  9.010   93.051  1.00 15.68 ? 314  GLU   B CG    1 
ATOM   11274 C  CD    . GLU   B  1  316  ? -1.263  8.889   91.543  1.00 19.42 ? 314  GLU   B CD    1 
ATOM   11275 O  OE1   . GLU   B  1  316  ? -0.625  7.980   90.973  1.00 19.53 ? 314  GLU   B OE1   1 
ATOM   11276 O  OE2   . GLU   B  1  316  ? -1.984  9.700   90.933  1.00 20.46 ? 314  GLU   B OE2   1 
ATOM   11277 N  N     . LEU   B  1  317  ? 2.488   9.375   95.921  1.00 17.04 ? 315  LEU   B N     1 
ATOM   11278 C  CA    . LEU   B  1  317  ? 3.693   9.034   96.666  1.00 17.16 ? 315  LEU   B CA    1 
ATOM   11279 C  C     . LEU   B  1  317  ? 3.359   8.508   98.054  1.00 17.44 ? 315  LEU   B C     1 
ATOM   11280 O  O     . LEU   B  1  317  ? 3.897   7.479   98.483  1.00 18.63 ? 315  LEU   B O     1 
ATOM   11281 C  CB    . LEU   B  1  317  ? 4.594   10.258  96.751  1.00 18.98 ? 315  LEU   B CB    1 
ATOM   11282 C  CG    . LEU   B  1  317  ? 5.900   10.043  97.505  1.00 19.44 ? 315  LEU   B CG    1 
ATOM   11283 C  CD1   . LEU   B  1  317  ? 6.660   8.852   96.942  1.00 22.11 ? 315  LEU   B CD1   1 
ATOM   11284 C  CD2   . LEU   B  1  317  ? 6.734   11.293  97.410  1.00 20.52 ? 315  LEU   B CD2   1 
ATOM   11285 N  N     . SER   B  1  318  ? 2.420   9.158   98.750  1.00 16.02 ? 316  SER   B N     1 
ATOM   11286 C  CA    . SER   B  1  318  ? 2.084   8.707   100.098 1.00 16.58 ? 316  SER   B CA    1 
ATOM   11287 C  C     . SER   B  1  318  ? 1.506   7.295   100.096 1.00 16.43 ? 316  SER   B C     1 
ATOM   11288 O  O     . SER   B  1  318  ? 1.658   6.564   101.085 1.00 17.36 ? 316  SER   B O     1 
ATOM   11289 C  CB    . SER   B  1  318  ? 1.131   9.689   100.783 1.00 16.71 ? 316  SER   B CB    1 
ATOM   11290 O  OG    . SER   B  1  318  ? -0.180  9.583   100.256 1.00 17.17 ? 316  SER   B OG    1 
ATOM   11291 N  N     . LEU   B  1  319  ? 0.853   6.893   99.005  1.00 16.92 ? 317  LEU   B N     1 
ATOM   11292 C  CA    . LEU   B  1  319  ? 0.303   5.544   98.932  1.00 16.81 ? 317  LEU   B CA    1 
ATOM   11293 C  C     . LEU   B  1  319  ? 1.400   4.492   98.934  1.00 18.79 ? 317  LEU   B C     1 
ATOM   11294 O  O     . LEU   B  1  319  ? 1.192   3.381   99.434  1.00 18.63 ? 317  LEU   B O     1 
ATOM   11295 C  CB    . LEU   B  1  319  ? -0.557  5.389   97.679  1.00 18.04 ? 317  LEU   B CB    1 
ATOM   11296 C  CG    . LEU   B  1  319  ? -1.801  6.270   97.618  1.00 18.18 ? 317  LEU   B CG    1 
ATOM   11297 C  CD1   . LEU   B  1  319  ? -2.463  6.088   96.248  1.00 18.82 ? 317  LEU   B CD1   1 
ATOM   11298 C  CD2   . LEU   B  1  319  ? -2.761  5.940   98.739  1.00 21.56 ? 317  LEU   B CD2   1 
ATOM   11299 N  N     . ASP   B  1  320  ? 2.565   4.816   98.377  1.00 19.08 ? 318  ASP   B N     1 
ATOM   11300 C  CA    . ASP   B  1  320  ? 3.659   3.858   98.416  1.00 21.77 ? 318  ASP   B CA    1 
ATOM   11301 C  C     . ASP   B  1  320  ? 4.133   3.613   99.835  1.00 18.47 ? 318  ASP   B C     1 
ATOM   11302 O  O     . ASP   B  1  320  ? 4.553   2.498   100.164 1.00 21.85 ? 318  ASP   B O     1 
ATOM   11303 C  CB    . ASP   B  1  320  ? 4.787   4.335   97.526  1.00 20.54 ? 318  ASP   B CB    1 
ATOM   11304 C  CG    . ASP   B  1  320  ? 4.469   4.124   96.072  1.00 20.52 ? 318  ASP   B CG    1 
ATOM   11305 O  OD1   . ASP   B  1  320  ? 4.136   2.977   95.718  1.00 22.65 ? 318  ASP   B OD1   1 
ATOM   11306 O  OD2   . ASP   B  1  320  ? 4.502   5.097   95.305  1.00 23.01 ? 318  ASP   B OD2   1 
ATOM   11307 N  N     . LEU   B  1  321  ? 4.054   4.626   100.695 1.00 17.58 ? 319  LEU   B N     1 
ATOM   11308 C  CA    . LEU   B  1  321  ? 4.386   4.404   102.096 1.00 19.13 ? 319  LEU   B CA    1 
ATOM   11309 C  C     . LEU   B  1  321  ? 3.288   3.632   102.798 1.00 18.52 ? 319  LEU   B C     1 
ATOM   11310 O  O     . LEU   B  1  321  ? 3.567   2.698   103.556 1.00 21.42 ? 319  LEU   B O     1 
ATOM   11311 C  CB    . LEU   B  1  321  ? 4.643   5.733   102.802 1.00 21.06 ? 319  LEU   B CB    1 
ATOM   11312 C  CG    . LEU   B  1  321  ? 5.995   6.348   102.457 1.00 19.70 ? 319  LEU   B CG    1 
ATOM   11313 C  CD1   . LEU   B  1  321  ? 5.915   7.189   101.195 1.00 21.95 ? 319  LEU   B CD1   1 
ATOM   11314 C  CD2   . LEU   B  1  321  ? 6.472   7.184   103.620 1.00 22.38 ? 319  LEU   B CD2   1 
ATOM   11315 N  N     . LEU   B  1  322  ? 2.032   3.990   102.539 1.00 19.34 ? 320  LEU   B N     1 
ATOM   11316 C  CA    . LEU   B  1  322  ? 0.927   3.271   103.156 1.00 19.89 ? 320  LEU   B CA    1 
ATOM   11317 C  C     . LEU   B  1  322  ? 0.990   1.791   102.817 1.00 19.31 ? 320  LEU   B C     1 
ATOM   11318 O  O     . LEU   B  1  322  ? 0.764   0.936   103.686 1.00 21.19 ? 320  LEU   B O     1 
ATOM   11319 C  CB    . LEU   B  1  322  ? -0.387  3.853   102.656 1.00 18.87 ? 320  LEU   B CB    1 
ATOM   11320 C  CG    . LEU   B  1  322  ? -1.623  3.183   103.250 1.00 21.39 ? 320  LEU   B CG    1 
ATOM   11321 C  CD1   . LEU   B  1  322  ? -1.649  3.382   104.762 1.00 20.91 ? 320  LEU   B CD1   1 
ATOM   11322 C  CD2   . LEU   B  1  322  ? -2.870  3.745   102.597 1.00 20.41 ? 320  LEU   B CD2   1 
ATOM   11323 N  N     . GLU   B  1  323  ? 1.303   1.476   101.555 1.00 20.94 ? 321  GLU   B N     1 
ATOM   11324 C  CA    . GLU   B  1  323  ? 1.429   0.088   101.114 1.00 19.23 ? 321  GLU   B CA    1 
ATOM   11325 C  C     . GLU   B  1  323  ? 2.438   -0.672  101.966 1.00 20.17 ? 321  GLU   B C     1 
ATOM   11326 O  O     . GLU   B  1  323  ? 2.146   -1.763  102.470 1.00 23.80 ? 321  GLU   B O     1 
ATOM   11327 C  CB    . GLU   B  1  323  ? 1.844   0.053   99.642  1.00 24.66 ? 321  GLU   B CB    1 
ATOM   11328 C  CG    . GLU   B  1  323  ? 2.159   -1.336  99.092  1.00 27.86 ? 321  GLU   B CG    1 
ATOM   11329 C  CD    . GLU   B  1  323  ? 0.943   -2.038  98.512  1.00 29.57 ? 321  GLU   B CD    1 
ATOM   11330 O  OE1   . GLU   B  1  323  ? -0.084  -1.369  98.279  1.00 26.05 ? 321  GLU   B OE1   1 
ATOM   11331 O  OE2   . GLU   B  1  323  ? 1.010   -3.266  98.298  1.00 28.74 ? 321  GLU   B OE2   1 
ATOM   11332 N  N     . VAL   B  1  324  ? 3.640   -0.113  102.125 1.00 20.09 ? 322  VAL   B N     1 
ATOM   11333 C  CA    . VAL   B  1  324  ? 4.673   -0.789  102.900 1.00 23.06 ? 322  VAL   B CA    1 
ATOM   11334 C  C     . VAL   B  1  324  ? 4.231   -0.959  104.346 1.00 20.46 ? 322  VAL   B C     1 
ATOM   11335 O  O     . VAL   B  1  324  ? 4.386   -2.034  104.937 1.00 23.48 ? 322  VAL   B O     1 
ATOM   11336 C  CB    . VAL   B  1  324  ? 6.015   -0.043  102.784 1.00 23.27 ? 322  VAL   B CB    1 
ATOM   11337 C  CG1   . VAL   B  1  324  ? 7.029   -0.631  103.755 1.00 23.03 ? 322  VAL   B CG1   1 
ATOM   11338 C  CG2   . VAL   B  1  324  ? 6.529   -0.105  101.353 1.00 25.81 ? 322  VAL   B CG2   1 
ATOM   11339 N  N     . LEU   B  1  325  ? 3.652   0.085   104.934 1.00 20.22 ? 323  LEU   B N     1 
ATOM   11340 C  CA    . LEU   B  1  325  ? 3.279   0.007   106.342 1.00 22.67 ? 323  LEU   B CA    1 
ATOM   11341 C  C     . LEU   B  1  325  ? 2.220   -1.062  106.582 1.00 19.41 ? 323  LEU   B C     1 
ATOM   11342 O  O     . LEU   B  1  325  ? 2.273   -1.785  107.583 1.00 20.81 ? 323  LEU   B O     1 
ATOM   11343 C  CB    . LEU   B  1  325  ? 2.801   1.372   106.826 1.00 21.15 ? 323  LEU   B CB    1 
ATOM   11344 C  CG    . LEU   B  1  325  ? 3.895   2.435   106.817 1.00 22.66 ? 323  LEU   B CG    1 
ATOM   11345 C  CD1   . LEU   B  1  325  ? 3.284   3.807   107.010 1.00 23.94 ? 323  LEU   B CD1   1 
ATOM   11346 C  CD2   . LEU   B  1  325  ? 4.900   2.147   107.909 1.00 22.24 ? 323  LEU   B CD2   1 
ATOM   11347 N  N     . CYS   B  1  326  ? 1.251   -1.188  105.668 1.00 22.03 ? 324  CYS   B N     1 
ATOM   11348 C  CA    . CYS   B  1  326  ? 0.196   -2.179  105.854 1.00 20.85 ? 324  CYS   B CA    1 
ATOM   11349 C  C     . CYS   B  1  326  ? 0.691   -3.603  105.650 1.00 23.07 ? 324  CYS   B C     1 
ATOM   11350 O  O     . CYS   B  1  326  ? 0.066   -4.537  106.161 1.00 22.74 ? 324  CYS   B O     1 
ATOM   11351 C  CB    . CYS   B  1  326  ? -0.993  -1.900  104.932 1.00 20.87 ? 324  CYS   B CB    1 
ATOM   11352 S  SG    . CYS   B  1  326  ? -1.883  -0.402  105.369 1.00 24.99 ? 324  CYS   B SG    1 
ATOM   11353 N  N     . LEU   B  1  327  ? 1.797   -3.786  104.933 1.00 22.51 ? 325  LEU   B N     1 
ATOM   11354 C  CA    . LEU   B  1  327  ? 2.376   -5.104  104.713 1.00 24.63 ? 325  LEU   B CA    1 
ATOM   11355 C  C     . LEU   B  1  327  ? 3.494   -5.430  105.691 1.00 26.94 ? 325  LEU   B C     1 
ATOM   11356 O  O     . LEU   B  1  327  ? 4.053   -6.532  105.633 1.00 27.48 ? 325  LEU   B O     1 
ATOM   11357 C  CB    . LEU   B  1  327  ? 2.891   -5.215  103.276 1.00 23.53 ? 325  LEU   B CB    1 
ATOM   11358 C  CG    . LEU   B  1  327  ? 1.790   -5.148  102.216 1.00 27.25 ? 325  LEU   B CG    1 
ATOM   11359 C  CD1   . LEU   B  1  327  ? 2.387   -5.104  100.823 1.00 32.80 ? 325  LEU   B CD1   1 
ATOM   11360 C  CD2   . LEU   B  1  327  ? 0.859   -6.327  102.363 1.00 33.88 ? 325  LEU   B CD2   1 
ATOM   11361 N  N     . ASP   B  1  328  ? 3.820   -4.512  106.595 1.00 25.06 ? 326  ASP   B N     1 
ATOM   11362 C  CA    . ASP   B  1  328  ? 4.935   -4.698  107.518 1.00 26.86 ? 326  ASP   B CA    1 
ATOM   11363 C  C     . ASP   B  1  328  ? 4.464   -5.535  108.700 1.00 24.42 ? 326  ASP   B C     1 
ATOM   11364 O  O     . ASP   B  1  328  ? 3.666   -5.070  109.522 1.00 25.97 ? 326  ASP   B O     1 
ATOM   11365 C  CB    . ASP   B  1  328  ? 5.435   -3.334  107.980 1.00 24.78 ? 326  ASP   B CB    1 
ATOM   11366 C  CG    . ASP   B  1  328  ? 6.717   -3.422  108.788 1.00 31.37 ? 326  ASP   B CG    1 
ATOM   11367 O  OD1   . ASP   B  1  328  ? 6.966   -4.469  109.419 1.00 28.33 ? 326  ASP   B OD1   1 
ATOM   11368 O  OD2   . ASP   B  1  328  ? 7.478   -2.433  108.791 1.00 32.40 ? 326  ASP   B OD2   1 
ATOM   11369 N  N     . GLY   B  1  329  ? 4.972   -6.768  108.800 1.00 28.04 ? 327  GLY   B N     1 
ATOM   11370 C  CA    . GLY   B  1  329  ? 4.589   -7.665  109.878 1.00 28.29 ? 327  GLY   B CA    1 
ATOM   11371 C  C     . GLY   B  1  329  ? 4.886   -7.146  111.271 1.00 27.79 ? 327  GLY   B C     1 
ATOM   11372 O  O     . GLY   B  1  329  ? 4.262   -7.600  112.235 1.00 27.63 ? 327  GLY   B O     1 
ATOM   11373 N  N     . ASP   B  1  330  ? 5.821   -6.202  111.406 1.00 27.39 ? 328  ASP   B N     1 
ATOM   11374 C  CA    . ASP   B  1  330  ? 6.043   -5.588  112.710 1.00 26.20 ? 328  ASP   B CA    1 
ATOM   11375 C  C     . ASP   B  1  330  ? 4.803   -4.871  113.219 1.00 30.74 ? 328  ASP   B C     1 
ATOM   11376 O  O     . ASP   B  1  330  ? 4.665   -4.677  114.431 1.00 31.47 ? 328  ASP   B O     1 
ATOM   11377 C  CB    . ASP   B  1  330  ? 7.220   -4.606  112.659 1.00 28.65 ? 328  ASP   B CB    1 
ATOM   11378 C  CG    . ASP   B  1  330  ? 8.559   -5.301  112.487 1.00 33.12 ? 328  ASP   B CG    1 
ATOM   11379 O  OD1   . ASP   B  1  330  ? 8.643   -6.522  112.742 1.00 34.62 ? 328  ASP   B OD1   1 
ATOM   11380 O  OD2   . ASP   B  1  330  ? 9.537   -4.626  112.103 1.00 32.48 ? 328  ASP   B OD2   1 
ATOM   11381 N  N     . LEU   B  1  331  ? 3.897   -4.476  112.323 1.00 25.52 ? 329  LEU   B N     1 
ATOM   11382 C  CA    . LEU   B  1  331  ? 2.668   -3.798  112.703 1.00 27.23 ? 329  LEU   B CA    1 
ATOM   11383 C  C     . LEU   B  1  331  ? 1.475   -4.742  112.736 1.00 22.72 ? 329  LEU   B C     1 
ATOM   11384 O  O     . LEU   B  1  331  ? 0.329   -4.281  112.723 1.00 26.55 ? 329  LEU   B O     1 
ATOM   11385 C  CB    . LEU   B  1  331  ? 2.411   -2.620  111.768 1.00 24.55 ? 329  LEU   B CB    1 
ATOM   11386 C  CG    . LEU   B  1  331  ? 3.579   -1.634  111.713 1.00 22.88 ? 329  LEU   B CG    1 
ATOM   11387 C  CD1   . LEU   B  1  331  ? 3.320   -0.541  110.692 1.00 23.49 ? 329  LEU   B CD1   1 
ATOM   11388 C  CD2   . LEU   B  1  331  ? 3.824   -1.035  113.094 1.00 22.86 ? 329  LEU   B CD2   1 
ATOM   11389 N  N     . SER   B  1  332  ? 1.737   -6.047  112.802 1.00 27.10 ? 330  SER   B N     1 
ATOM   11390 C  CA    . SER   B  1  332  ? 0.706   -7.078  112.732 1.00 28.47 ? 330  SER   B CA    1 
ATOM   11391 C  C     . SER   B  1  332  ? -0.472  -6.803  113.663 1.00 28.83 ? 330  SER   B C     1 
ATOM   11392 O  O     . SER   B  1  332  ? -0.295  -6.551  114.858 1.00 30.69 ? 330  SER   B O     1 
ATOM   11393 C  CB    . SER   B  1  332  ? 1.336   -8.418  113.109 1.00 34.17 ? 330  SER   B CB    1 
ATOM   11394 O  OG    . SER   B  1  332  ? 0.384   -9.460  113.005 1.00 36.98 ? 330  SER   B OG    1 
ATOM   11395 N  N     . GLY   B  1  333  ? -1.681  -6.871  113.105 1.00 27.24 ? 331  GLY   B N     1 
ATOM   11396 C  CA    . GLY   B  1  333  ? -2.899  -6.771  113.883 1.00 31.50 ? 331  GLY   B CA    1 
ATOM   11397 C  C     . GLY   B  1  333  ? -3.250  -5.386  114.378 1.00 30.02 ? 331  GLY   B C     1 
ATOM   11398 O  O     . GLY   B  1  333  ? -4.252  -5.235  115.089 1.00 33.86 ? 331  GLY   B O     1 
ATOM   11399 N  N     . TRP   B  1  334  ? -2.467  -4.373  114.034 1.00 28.78 ? 332  TRP   B N     1 
ATOM   11400 C  CA    . TRP   B  1  334  ? -2.724  -3.012  114.481 1.00 28.33 ? 332  TRP   B CA    1 
ATOM   11401 C  C     . TRP   B  1  334  ? -3.690  -2.354  113.509 1.00 23.33 ? 332  TRP   B C     1 
ATOM   11402 O  O     . TRP   B  1  334  ? -3.400  -2.235  112.315 1.00 26.17 ? 332  TRP   B O     1 
ATOM   11403 C  CB    . TRP   B  1  334  ? -1.405  -2.251  114.550 1.00 30.24 ? 332  TRP   B CB    1 
ATOM   11404 C  CG    . TRP   B  1  334  ? -1.515  -0.797  114.864 1.00 27.74 ? 332  TRP   B CG    1 
ATOM   11405 C  CD1   . TRP   B  1  334  ? -2.088  -0.224  115.967 1.00 26.92 ? 332  TRP   B CD1   1 
ATOM   11406 C  CD2   . TRP   B  1  334  ? -0.989  0.273   114.081 1.00 25.72 ? 332  TRP   B CD2   1 
ATOM   11407 N  NE1   . TRP   B  1  334  ? -1.957  1.147   115.907 1.00 24.88 ? 332  TRP   B NE1   1 
ATOM   11408 C  CE2   . TRP   B  1  334  ? -1.287  1.475   114.757 1.00 23.87 ? 332  TRP   B CE2   1 
ATOM   11409 C  CE3   . TRP   B  1  334  ? -0.300  0.333   112.867 1.00 24.26 ? 332  TRP   B CE3   1 
ATOM   11410 C  CZ2   . TRP   B  1  334  ? -0.916  2.719   114.258 1.00 21.59 ? 332  TRP   B CZ2   1 
ATOM   11411 C  CZ3   . TRP   B  1  334  ? 0.066   1.570   112.374 1.00 26.98 ? 332  TRP   B CZ3   1 
ATOM   11412 C  CH2   . TRP   B  1  334  ? -0.243  2.748   113.069 1.00 25.08 ? 332  TRP   B CH2   1 
ATOM   11413 N  N     . ASN   B  1  335  ? -4.847  -1.948  114.008 1.00 24.96 ? 333  ASN   B N     1 
ATOM   11414 C  CA    . ASN   B  1  335  ? -5.850  -1.325  113.161 1.00 25.97 ? 333  ASN   B CA    1 
ATOM   11415 C  C     . ASN   B  1  335  ? -5.820  0.189   113.259 1.00 23.58 ? 333  ASN   B C     1 
ATOM   11416 O  O     . ASN   B  1  335  ? -6.760  0.855   112.815 1.00 24.53 ? 333  ASN   B O     1 
ATOM   11417 C  CB    . ASN   B  1  335  ? -7.233  -1.883  113.482 1.00 27.24 ? 333  ASN   B CB    1 
ATOM   11418 C  CG    . ASN   B  1  335  ? -7.359  -3.338  113.084 1.00 32.38 ? 333  ASN   B CG    1 
ATOM   11419 O  OD1   . ASN   B  1  335  ? -6.715  -3.775  112.127 1.00 27.61 ? 333  ASN   B OD1   1 
ATOM   11420 N  ND2   . ASN   B  1  335  ? -8.180  -4.096  113.810 1.00 31.47 ? 333  ASN   B ND2   1 
ATOM   11421 N  N     . GLY   B  1  336  ? -4.763  0.742   113.836 1.00 23.34 ? 334  GLY   B N     1 
ATOM   11422 C  CA    . GLY   B  1  336  ? -4.678  2.165   114.050 1.00 23.99 ? 334  GLY   B CA    1 
ATOM   11423 C  C     . GLY   B  1  336  ? -4.032  2.963   112.955 1.00 21.68 ? 334  GLY   B C     1 
ATOM   11424 O  O     . GLY   B  1  336  ? -3.932  4.183   113.096 1.00 21.38 ? 334  GLY   B O     1 
ATOM   11425 N  N     . MET   B  1  337  ? -3.599  2.337   111.863 1.00 23.06 ? 335  MET   B N     1 
ATOM   11426 C  CA    . MET   B  1  337  ? -3.044  3.108   110.760 1.00 21.21 ? 335  MET   B CA    1 
ATOM   11427 C  C     . MET   B  1  337  ? -4.155  3.933   110.134 1.00 21.63 ? 335  MET   B C     1 
ATOM   11428 O  O     . MET   B  1  337  ? -5.184  3.389   109.715 1.00 21.38 ? 335  MET   B O     1 
ATOM   11429 C  CB    . MET   B  1  337  ? -2.444  2.182   109.710 1.00 24.84 ? 335  MET   B CB    1 
ATOM   11430 C  CG    . MET   B  1  337  ? -1.791  2.924   108.554 1.00 25.07 ? 335  MET   B CG    1 
ATOM   11431 S  SD    . MET   B  1  337  ? -0.177  3.571   109.018 1.00 36.58 ? 335  MET   B SD    1 
ATOM   11432 C  CE    . MET   B  1  337  ? -0.481  5.333   108.968 1.00 28.82 ? 335  MET   B CE    1 
ATOM   11433 N  N     . GLY   B  1  338  ? -3.943  5.241   110.070 1.00 19.15 ? 336  GLY   B N     1 
ATOM   11434 C  CA    . GLY   B  1  338  ? -4.924  6.158   109.533 1.00 20.96 ? 336  GLY   B CA    1 
ATOM   11435 C  C     . GLY   B  1  338  ? -4.394  6.883   108.315 1.00 20.18 ? 336  GLY   B C     1 
ATOM   11436 O  O     . GLY   B  1  338  ? -3.197  7.125   108.184 1.00 19.43 ? 336  GLY   B O     1 
ATOM   11437 N  N     . PHE   B  1  339  ? -5.300  7.209   107.408 1.00 18.62 ? 337  PHE   B N     1 
ATOM   11438 C  CA    . PHE   B  1  339  ? -4.878  7.823   106.165 1.00 18.44 ? 337  PHE   B CA    1 
ATOM   11439 C  C     . PHE   B  1  339  ? -6.000  8.726   105.694 1.00 17.82 ? 337  PHE   B C     1 
ATOM   11440 O  O     . PHE   B  1  339  ? -7.157  8.302   105.642 1.00 19.90 ? 337  PHE   B O     1 
ATOM   11441 C  CB    . PHE   B  1  339  ? -4.575  6.739   105.125 1.00 19.79 ? 337  PHE   B CB    1 
ATOM   11442 C  CG    . PHE   B  1  339  ? -3.865  7.239   103.902 1.00 20.02 ? 337  PHE   B CG    1 
ATOM   11443 C  CD1   . PHE   B  1  339  ? -2.480  7.322   103.860 1.00 20.36 ? 337  PHE   B CD1   1 
ATOM   11444 C  CD2   . PHE   B  1  339  ? -4.586  7.586   102.773 1.00 18.05 ? 337  PHE   B CD2   1 
ATOM   11445 C  CE1   . PHE   B  1  339  ? -1.836  7.776   102.706 1.00 19.81 ? 337  PHE   B CE1   1 
ATOM   11446 C  CE2   . PHE   B  1  339  ? -3.952  8.029   101.626 1.00 20.05 ? 337  PHE   B CE2   1 
ATOM   11447 C  CZ    . PHE   B  1  339  ? -2.582  8.120   101.591 1.00 21.21 ? 337  PHE   B CZ    1 
ATOM   11448 N  N     . VAL   B  1  340  ? -5.660  9.963   105.373 1.00 17.45 ? 338  VAL   B N     1 
ATOM   11449 C  CA    . VAL   B  1  340  ? -6.635  10.949  104.933 1.00 17.35 ? 338  VAL   B CA    1 
ATOM   11450 C  C     . VAL   B  1  340  ? -6.774  10.858  103.428 1.00 17.87 ? 338  VAL   B C     1 
ATOM   11451 O  O     . VAL   B  1  340  ? -5.783  10.702  102.709 1.00 16.56 ? 338  VAL   B O     1 
ATOM   11452 C  CB    . VAL   B  1  340  ? -6.178  12.364  105.323 1.00 19.30 ? 338  VAL   B CB    1 
ATOM   11453 C  CG1   . VAL   B  1  340  ? -7.165  13.395  104.808 1.00 18.37 ? 338  VAL   B CG1   1 
ATOM   11454 C  CG2   . VAL   B  1  340  ? -6.003  12.469  106.822 1.00 18.08 ? 338  VAL   B CG2   1 
ATOM   11455 N  N     . VAL   B  1  341  ? -8.000  10.978  102.946 1.00 17.53 ? 339  VAL   B N     1 
ATOM   11456 C  CA    A VAL   B  1  341  ? -8.272  11.148  101.526 0.57 17.94 ? 339  VAL   B CA    1 
ATOM   11457 C  CA    B VAL   B  1  341  ? -8.268  11.149  101.526 0.43 17.93 ? 339  VAL   B CA    1 
ATOM   11458 C  C     . VAL   B  1  341  ? -9.119  12.397  101.356 1.00 16.46 ? 339  VAL   B C     1 
ATOM   11459 O  O     . VAL   B  1  341  ? -10.067 12.626  102.122 1.00 17.28 ? 339  VAL   B O     1 
ATOM   11460 C  CB    A VAL   B  1  341  ? -8.958  9.913   100.908 0.57 19.00 ? 339  VAL   B CB    1 
ATOM   11461 C  CB    B VAL   B  1  341  ? -8.946  9.913   100.904 0.43 18.99 ? 339  VAL   B CB    1 
ATOM   11462 C  CG1   A VAL   B  1  341  ? -8.043  8.715   100.991 0.57 20.07 ? 339  VAL   B CG1   1 
ATOM   11463 C  CG1   B VAL   B  1  341  ? -8.771  9.928   99.390  0.43 17.79 ? 339  VAL   B CG1   1 
ATOM   11464 C  CG2   A VAL   B  1  341  ? -10.282 9.630   101.597 0.57 21.56 ? 339  VAL   B CG2   1 
ATOM   11465 C  CG2   B VAL   B  1  341  ? -8.372  8.641   101.499 0.43 20.51 ? 339  VAL   B CG2   1 
ATOM   11466 N  N     . GLN   B  1  342  ? -8.782  13.193  100.351 1.00 16.18 ? 340  GLN   B N     1 
ATOM   11467 C  CA    . GLN   B  1  342  ? -9.365  14.511  100.126 1.00 16.82 ? 340  GLN   B CA    1 
ATOM   11468 C  C     . GLN   B  1  342  ? -10.428 14.421  99.043  1.00 17.60 ? 340  GLN   B C     1 
ATOM   11469 O  O     . GLN   B  1  342  ? -10.118 14.189  97.870  1.00 17.63 ? 340  GLN   B O     1 
ATOM   11470 C  CB    . GLN   B  1  342  ? -8.274  15.502  99.738  1.00 16.13 ? 340  GLN   B CB    1 
ATOM   11471 C  CG    . GLN   B  1  342  ? -7.256  15.723  100.834 1.00 14.29 ? 340  GLN   B CG    1 
ATOM   11472 C  CD    . GLN   B  1  342  ? -5.882  16.057  100.269 1.00 16.01 ? 340  GLN   B CD    1 
ATOM   11473 O  OE1   . GLN   B  1  342  ? -5.418  15.420  99.327  1.00 16.68 ? 340  GLN   B OE1   1 
ATOM   11474 N  NE2   . GLN   B  1  342  ? -5.229  17.064  100.840 1.00 15.88 ? 340  GLN   B NE2   1 
ATOM   11475 N  N     . ALA   B  1  343  ? -11.679 14.627  99.441  1.00 16.41 ? 341  ALA   B N     1 
ATOM   11476 C  CA    . ALA   B  1  343  ? -12.792 14.515  98.510  1.00 15.18 ? 341  ALA   B CA    1 
ATOM   11477 C  C     . ALA   B  1  343  ? -12.825 15.646  97.493  1.00 16.14 ? 341  ALA   B C     1 
ATOM   11478 O  O     . ALA   B  1  343  ? -13.499 15.508  96.468  1.00 17.40 ? 341  ALA   B O     1 
ATOM   11479 C  CB    . ALA   B  1  343  ? -14.111 14.430  99.270  1.00 17.65 ? 341  ALA   B CB    1 
ATOM   11480 N  N     . TYR   B  1  344  ? -12.109 16.753  97.725  1.00 17.18 ? 342  TYR   B N     1 
ATOM   11481 C  CA    . TYR   B  1  344  ? -12.021 17.733  96.653  1.00 15.63 ? 342  TYR   B CA    1 
ATOM   11482 C  C     . TYR   B  1  344  ? -11.151 17.259  95.506  1.00 16.19 ? 342  TYR   B C     1 
ATOM   11483 O  O     . TYR   B  1  344  ? -11.081 17.945  94.490  1.00 17.11 ? 342  TYR   B O     1 
ATOM   11484 C  CB    . TYR   B  1  344  ? -11.606 19.137  97.138  1.00 16.70 ? 342  TYR   B CB    1 
ATOM   11485 C  CG    . TYR   B  1  344  ? -10.161 19.406  97.554  1.00 15.71 ? 342  TYR   B CG    1 
ATOM   11486 C  CD1   . TYR   B  1  344  ? -9.193  18.407  97.603  1.00 15.77 ? 342  TYR   B CD1   1 
ATOM   11487 C  CD2   . TYR   B  1  344  ? -9.788  20.687  97.923  1.00 16.14 ? 342  TYR   B CD2   1 
ATOM   11488 C  CE1   . TYR   B  1  344  ? -7.886  18.689  97.998  1.00 15.44 ? 342  TYR   B CE1   1 
ATOM   11489 C  CE2   . TYR   B  1  344  ? -8.511  20.972  98.326  1.00 17.01 ? 342  TYR   B CE2   1 
ATOM   11490 C  CZ    . TYR   B  1  344  ? -7.567  19.979  98.358  1.00 16.07 ? 342  TYR   B CZ    1 
ATOM   11491 O  OH    . TYR   B  1  344  ? -6.294  20.306  98.781  1.00 15.02 ? 342  TYR   B OH    1 
ATOM   11492 N  N     . GLY   B  1  345  ? -10.507 16.106  95.647  1.00 16.17 ? 343  GLY   B N     1 
ATOM   11493 C  CA    . GLY   B  1  345  ? -9.598  15.592  94.644  1.00 16.71 ? 343  GLY   B CA    1 
ATOM   11494 C  C     . GLY   B  1  345  ? -10.323 14.617  93.733  1.00 17.67 ? 343  GLY   B C     1 
ATOM   11495 O  O     . GLY   B  1  345  ? -11.150 13.823  94.181  1.00 17.18 ? 343  GLY   B O     1 
ATOM   11496 N  N     . LYS   B  1  346  ? -9.988  14.690  92.445  1.00 16.32 ? 344  LYS   B N     1 
ATOM   11497 C  CA    . LYS   B  1  346  ? -10.639 13.851  91.448  1.00 17.33 ? 344  LYS   B CA    1 
ATOM   11498 C  C     . LYS   B  1  346  ? -10.295 12.383  91.613  1.00 18.52 ? 344  LYS   B C     1 
ATOM   11499 O  O     . LYS   B  1  346  ? -11.043 11.524  91.134  1.00 18.09 ? 344  LYS   B O     1 
ATOM   11500 C  CB    . LYS   B  1  346  ? -10.233 14.319  90.060  1.00 17.97 ? 344  LYS   B CB    1 
ATOM   11501 C  CG    . LYS   B  1  346  ? -10.698 15.724  89.771  1.00 18.08 ? 344  LYS   B CG    1 
ATOM   11502 C  CD    . LYS   B  1  346  ? -10.184 16.215  88.465  1.00 18.62 ? 344  LYS   B CD    1 
ATOM   11503 C  CE    . LYS   B  1  346  ? -10.849 17.536  88.149  1.00 18.05 ? 344  LYS   B CE    1 
ATOM   11504 N  NZ    . LYS   B  1  346  ? -10.297 18.139  86.898  1.00 17.33 ? 344  LYS   B NZ    1 
ATOM   11505 N  N     . ARG   B  1  347  ? -9.179  12.076  92.258  1.00 16.83 ? 345  ARG   B N     1 
ATOM   11506 C  CA    . ARG   B  1  347  ? -8.791  10.688  92.424  1.00 18.31 ? 345  ARG   B CA    1 
ATOM   11507 C  C     . ARG   B  1  347  ? -9.427  10.037  93.635  1.00 17.26 ? 345  ARG   B C     1 
ATOM   11508 O  O     . ARG   B  1  347  ? -9.295  8.820   93.796  1.00 19.28 ? 345  ARG   B O     1 
ATOM   11509 C  CB    . ARG   B  1  347  ? -7.268  10.584  92.511  1.00 17.48 ? 345  ARG   B CB    1 
ATOM   11510 C  CG    . ARG   B  1  347  ? -6.601  10.959  91.210  1.00 16.60 ? 345  ARG   B CG    1 
ATOM   11511 C  CD    . ARG   B  1  347  ? -5.125  11.231  91.412  1.00 15.69 ? 345  ARG   B CD    1 
ATOM   11512 N  NE    . ARG   B  1  347  ? -4.903  12.479  92.130  1.00 15.30 ? 345  ARG   B NE    1 
ATOM   11513 C  CZ    . ARG   B  1  347  ? -3.721  12.843  92.596  1.00 15.48 ? 345  ARG   B CZ    1 
ATOM   11514 N  NH1   . ARG   B  1  347  ? -2.647  12.096  92.402  1.00 16.43 ? 345  ARG   B NH1   1 
ATOM   11515 N  NH2   . ARG   B  1  347  ? -3.606  13.996  93.252  1.00 15.40 ? 345  ARG   B NH2   1 
ATOM   11516 N  N     . CYS   B  1  348  ? -10.144 10.811  94.455  1.00 17.85 ? 346  CYS   B N     1 
ATOM   11517 C  CA    . CYS   B  1  348  ? -10.613 10.340  95.758  1.00 18.91 ? 346  CYS   B CA    1 
ATOM   11518 C  C     . CYS   B  1  348  ? -11.295 8.977   95.733  1.00 19.66 ? 346  CYS   B C     1 
ATOM   11519 O  O     . CYS   B  1  348  ? -10.881 8.096   96.499  1.00 20.77 ? 346  CYS   B O     1 
ATOM   11520 C  CB    . CYS   B  1  348  ? -11.483 11.413  96.427  1.00 18.68 ? 346  CYS   B CB    1 
ATOM   11521 S  SG    . CYS   B  1  348  ? -11.784 11.046  98.176  1.00 23.17 ? 346  CYS   B SG    1 
ATOM   11522 N  N     . PRO   B  1  349  ? -12.326 8.730   94.919  1.00 19.99 ? 347  PRO   B N     1 
ATOM   11523 C  CA    . PRO   B  1  349  ? -12.950 7.402   94.953  1.00 21.21 ? 347  PRO   B CA    1 
ATOM   11524 C  C     . PRO   B  1  349  ? -12.010 6.291   94.533  1.00 18.45 ? 347  PRO   B C     1 
ATOM   11525 O  O     . PRO   B  1  349  ? -12.103 5.181   95.071  1.00 20.09 ? 347  PRO   B O     1 
ATOM   11526 C  CB    . PRO   B  1  349  ? -14.150 7.538   94.005  1.00 22.95 ? 347  PRO   B CB    1 
ATOM   11527 C  CG    . PRO   B  1  349  ? -13.833 8.674   93.149  1.00 22.84 ? 347  PRO   B CG    1 
ATOM   11528 C  CD    . PRO   B  1  349  ? -12.940 9.605   93.906  1.00 21.02 ? 347  PRO   B CD    1 
ATOM   11529 N  N     . PHE   B  1  350  ? -11.094 6.568   93.607  1.00 19.48 ? 348  PHE   B N     1 
ATOM   11530 C  CA    . PHE   B  1  350  ? -10.133 5.558   93.175  1.00 20.26 ? 348  PHE   B CA    1 
ATOM   11531 C  C     . PHE   B  1  350  ? -9.087  5.297   94.245  1.00 19.02 ? 348  PHE   B C     1 
ATOM   11532 O  O     . PHE   B  1  350  ? -8.655  4.152   94.432  1.00 20.31 ? 348  PHE   B O     1 
ATOM   11533 C  CB    . PHE   B  1  350  ? -9.517  5.995   91.853  1.00 18.56 ? 348  PHE   B CB    1 
ATOM   11534 C  CG    . PHE   B  1  350  ? -10.550 6.379   90.860  1.00 20.86 ? 348  PHE   B CG    1 
ATOM   11535 C  CD1   . PHE   B  1  350  ? -11.254 5.401   90.182  1.00 22.66 ? 348  PHE   B CD1   1 
ATOM   11536 C  CD2   . PHE   B  1  350  ? -10.881 7.705   90.663  1.00 19.68 ? 348  PHE   B CD2   1 
ATOM   11537 C  CE1   . PHE   B  1  350  ? -12.248 5.743   89.286  1.00 24.93 ? 348  PHE   B CE1   1 
ATOM   11538 C  CE2   . PHE   B  1  350  ? -11.867 8.058   89.773  1.00 22.08 ? 348  PHE   B CE2   1 
ATOM   11539 C  CZ    . PHE   B  1  350  ? -12.557 7.075   89.089  1.00 22.82 ? 348  PHE   B CZ    1 
ATOM   11540 N  N     . VAL   B  1  351  ? -8.700  6.339   94.983  1.00 19.53 ? 349  VAL   B N     1 
ATOM   11541 C  CA    . VAL   B  1  351  ? -7.816  6.149   96.130  1.00 17.83 ? 349  VAL   B CA    1 
ATOM   11542 C  C     . VAL   B  1  351  ? -8.504  5.299   97.183  1.00 18.61 ? 349  VAL   B C     1 
ATOM   11543 O  O     . VAL   B  1  351  ? -7.893  4.403   97.774  1.00 19.68 ? 349  VAL   B O     1 
ATOM   11544 C  CB    . VAL   B  1  351  ? -7.382  7.510   96.695  1.00 16.92 ? 349  VAL   B CB    1 
ATOM   11545 C  CG1   . VAL   B  1  351  ? -6.535  7.302   97.961  1.00 19.22 ? 349  VAL   B CG1   1 
ATOM   11546 C  CG2   . VAL   B  1  351  ? -6.592  8.268   95.656  1.00 19.04 ? 349  VAL   B CG2   1 
ATOM   11547 N  N     . LEU   B  1  352  ? -9.790  5.566   97.432  1.00 19.18 ? 350  LEU   B N     1 
ATOM   11548 C  CA    . LEU   B  1  352  ? -10.537 4.757   98.386  1.00 20.65 ? 350  LEU   B CA    1 
ATOM   11549 C  C     . LEU   B  1  352  ? -10.595 3.301   97.949  1.00 20.30 ? 350  LEU   B C     1 
ATOM   11550 O  O     . LEU   B  1  352  ? -10.433 2.395   98.774  1.00 22.27 ? 350  LEU   B O     1 
ATOM   11551 C  CB    . LEU   B  1  352  ? -11.942 5.316   98.579  1.00 20.17 ? 350  LEU   B CB    1 
ATOM   11552 C  CG    . LEU   B  1  352  ? -11.994 6.644   99.332  1.00 20.76 ? 350  LEU   B CG    1 
ATOM   11553 C  CD1   . LEU   B  1  352  ? -13.414 7.135   99.369  1.00 22.65 ? 350  LEU   B CD1   1 
ATOM   11554 C  CD2   . LEU   B  1  352  ? -11.463 6.455   100.751 1.00 23.66 ? 350  LEU   B CD2   1 
ATOM   11555 N  N     . ASP   B  1  353  ? -10.833 3.058   96.654  1.00 22.03 ? 351  ASP   B N     1 
ATOM   11556 C  CA    . ASP   B  1  353  ? -10.811 1.687   96.146  1.00 21.80 ? 351  ASP   B CA    1 
ATOM   11557 C  C     . ASP   B  1  353  ? -9.471  1.031   96.429  1.00 18.81 ? 351  ASP   B C     1 
ATOM   11558 O  O     . ASP   B  1  353  ? -9.415  -0.135  96.834  1.00 21.70 ? 351  ASP   B O     1 
ATOM   11559 C  CB    . ASP   B  1  353  ? -11.057 1.666   94.637  1.00 22.16 ? 351  ASP   B CB    1 
ATOM   11560 C  CG    . ASP   B  1  353  ? -12.476 2.018   94.263  1.00 24.60 ? 351  ASP   B CG    1 
ATOM   11561 O  OD1   . ASP   B  1  353  ? -13.375 1.878   95.111  1.00 26.16 ? 351  ASP   B OD1   1 
ATOM   11562 O  OD2   . ASP   B  1  353  ? -12.676 2.440   93.105  1.00 30.51 ? 351  ASP   B OD2   1 
ATOM   11563 N  N     . PHE   B  1  354  ? -8.380  1.760   96.198  1.00 22.14 ? 352  PHE   B N     1 
ATOM   11564 C  CA    . PHE   B  1  354  ? -7.053  1.236   96.492  1.00 20.24 ? 352  PHE   B CA    1 
ATOM   11565 C  C     . PHE   B  1  354  ? -6.897  0.921   97.975  1.00 19.35 ? 352  PHE   B C     1 
ATOM   11566 O  O     . PHE   B  1  354  ? -6.399  -0.149  98.342  1.00 21.28 ? 352  PHE   B O     1 
ATOM   11567 C  CB    . PHE   B  1  354  ? -5.989  2.238   96.048  1.00 20.98 ? 352  PHE   B CB    1 
ATOM   11568 C  CG    . PHE   B  1  354  ? -4.612  1.900   96.550  1.00 19.85 ? 352  PHE   B CG    1 
ATOM   11569 C  CD1   . PHE   B  1  354  ? -3.816  1.003   95.857  1.00 21.34 ? 352  PHE   B CD1   1 
ATOM   11570 C  CD2   . PHE   B  1  354  ? -4.131  2.454   97.731  1.00 20.34 ? 352  PHE   B CD2   1 
ATOM   11571 C  CE1   . PHE   B  1  354  ? -2.550  0.660   96.336  1.00 20.54 ? 352  PHE   B CE1   1 
ATOM   11572 C  CE2   . PHE   B  1  354  ? -2.879  2.117   98.214  1.00 23.88 ? 352  PHE   B CE2   1 
ATOM   11573 C  CZ    . PHE   B  1  354  ? -2.087  1.223   97.517  1.00 21.82 ? 352  PHE   B CZ    1 
ATOM   11574 N  N     . ILE   B  1  355  ? -7.327  1.842   98.844  1.00 20.47 ? 353  ILE   B N     1 
ATOM   11575 C  CA    . ILE   B  1  355  ? -7.169  1.649   100.286 1.00 20.70 ? 353  ILE   B CA    1 
ATOM   11576 C  C     . ILE   B  1  355  ? -8.026  0.495   100.776 1.00 21.11 ? 353  ILE   B C     1 
ATOM   11577 O  O     . ILE   B  1  355  ? -7.583  -0.326  101.588 1.00 21.67 ? 353  ILE   B O     1 
ATOM   11578 C  CB    . ILE   B  1  355  ? -7.496  2.948   101.042 1.00 20.45 ? 353  ILE   B CB    1 
ATOM   11579 C  CG1   . ILE   B  1  355  ? -6.473  4.026   100.697 1.00 22.65 ? 353  ILE   B CG1   1 
ATOM   11580 C  CG2   . ILE   B  1  355  ? -7.564  2.693   102.563 1.00 20.74 ? 353  ILE   B CG2   1 
ATOM   11581 C  CD1   . ILE   B  1  355  ? -6.883  5.390   101.186 1.00 21.69 ? 353  ILE   B CD1   1 
ATOM   11582 N  N     . ILE   B  1  356  ? -9.275  0.426   100.311 1.00 22.38 ? 354  ILE   B N     1 
ATOM   11583 C  CA    . ILE   B  1  356  ? -10.153 -0.661  100.726 1.00 23.74 ? 354  ILE   B CA    1 
ATOM   11584 C  C     . ILE   B  1  356  ? -9.563  -1.999  100.313 1.00 23.23 ? 354  ILE   B C     1 
ATOM   11585 O  O     . ILE   B  1  356  ? -9.573  -2.966  101.084 1.00 22.70 ? 354  ILE   B O     1 
ATOM   11586 C  CB    . ILE   B  1  356  ? -11.568 -0.445  100.162 1.00 24.73 ? 354  ILE   B CB    1 
ATOM   11587 C  CG1   . ILE   B  1  356  ? -12.241 0.731   100.872 1.00 26.31 ? 354  ILE   B CG1   1 
ATOM   11588 C  CG2   . ILE   B  1  356  ? -12.394 -1.708  100.297 1.00 24.60 ? 354  ILE   B CG2   1 
ATOM   11589 C  CD1   . ILE   B  1  356  ? -13.441 1.281   100.125 1.00 26.33 ? 354  ILE   B CD1   1 
ATOM   11590 N  N     . ASP   B  1  357  ? -9.021  -2.070  99.095  1.00 22.97 ? 355  ASP   B N     1 
ATOM   11591 C  CA    . ASP   B  1  357  ? -8.390  -3.305  98.652  1.00 23.91 ? 355  ASP   B CA    1 
ATOM   11592 C  C     . ASP   B  1  357  ? -7.145  -3.613  99.470  1.00 21.50 ? 355  ASP   B C     1 
ATOM   11593 O  O     . ASP   B  1  357  ? -6.932  -4.764  99.861  1.00 21.28 ? 355  ASP   B O     1 
ATOM   11594 C  CB    . ASP   B  1  357  ? -8.055  -3.224  97.168  1.00 22.50 ? 355  ASP   B CB    1 
ATOM   11595 C  CG    . ASP   B  1  357  ? -7.192  -4.380  96.708  1.00 23.88 ? 355  ASP   B CG    1 
ATOM   11596 O  OD1   . ASP   B  1  357  ? -7.739  -5.487  96.518  1.00 26.55 ? 355  ASP   B OD1   1 
ATOM   11597 O  OD2   . ASP   B  1  357  ? -5.973  -4.182  96.539  1.00 24.71 ? 355  ASP   B OD2   1 
ATOM   11598 N  N     . LEU   B  1  358  ? -6.309  -2.601  99.728  1.00 21.32 ? 356  LEU   B N     1 
ATOM   11599 C  CA    . LEU   B  1  358  ? -5.130  -2.811  100.562 1.00 19.21 ? 356  LEU   B CA    1 
ATOM   11600 C  C     . LEU   B  1  358  ? -5.524  -3.337  101.934 1.00 19.83 ? 356  LEU   B C     1 
ATOM   11601 O  O     . LEU   B  1  358  ? -4.906  -4.276  102.450 1.00 22.86 ? 356  LEU   B O     1 
ATOM   11602 C  CB    . LEU   B  1  358  ? -4.362  -1.499  100.695 1.00 19.80 ? 356  LEU   B CB    1 
ATOM   11603 C  CG    . LEU   B  1  358  ? -3.140  -1.509  101.619 1.00 20.30 ? 356  LEU   B CG    1 
ATOM   11604 C  CD1   . LEU   B  1  358  ? -2.139  -2.569  101.200 1.00 23.24 ? 356  LEU   B CD1   1 
ATOM   11605 C  CD2   . LEU   B  1  358  ? -2.497  -0.137  101.595 1.00 20.88 ? 356  LEU   B CD2   1 
ATOM   11606 N  N     . ALA   B  1  359  ? -6.574  -2.765  102.527 1.00 21.47 ? 357  ALA   B N     1 
ATOM   11607 C  CA    . ALA   B  1  359  ? -7.028  -3.232  103.829 1.00 21.69 ? 357  ALA   B CA    1 
ATOM   11608 C  C     . ALA   B  1  359  ? -7.443  -4.693  103.759 1.00 23.89 ? 357  ALA   B C     1 
ATOM   11609 O  O     . ALA   B  1  359  ? -7.072  -5.499  104.620 1.00 25.76 ? 357  ALA   B O     1 
ATOM   11610 C  CB    . ALA   B  1  359  ? -8.201  -2.372  104.299 1.00 25.92 ? 357  ALA   B CB    1 
ATOM   11611 N  N     . ARG   B  1  360  ? -8.186  -5.054  102.710 1.00 23.24 ? 358  ARG   B N     1 
ATOM   11612 C  CA    A ARG   B  1  360  ? -8.668  -6.425  102.561 0.50 24.95 ? 358  ARG   B CA    1 
ATOM   11613 C  CA    B ARG   B  1  360  ? -8.668  -6.423  102.573 0.50 24.94 ? 358  ARG   B CA    1 
ATOM   11614 C  C     . ARG   B  1  360  ? -7.514  -7.406  102.420 1.00 22.43 ? 358  ARG   B C     1 
ATOM   11615 O  O     . ARG   B  1  360  ? -7.497  -8.462  103.063 1.00 24.91 ? 358  ARG   B O     1 
ATOM   11616 C  CB    A ARG   B  1  360  ? -9.579  -6.528  101.339 0.50 26.46 ? 358  ARG   B CB    1 
ATOM   11617 C  CB    B ARG   B  1  360  ? -9.623  -6.518  101.384 0.50 26.45 ? 358  ARG   B CB    1 
ATOM   11618 C  CG    A ARG   B  1  360  ? -10.934 -5.902  101.520 0.50 28.10 ? 358  ARG   B CG    1 
ATOM   11619 C  CG    B ARG   B  1  360  ? -11.017 -6.964  101.760 0.50 30.06 ? 358  ARG   B CG    1 
ATOM   11620 C  CD    A ARG   B  1  360  ? -11.918 -6.466  100.517 0.50 31.53 ? 358  ARG   B CD    1 
ATOM   11621 C  CD    B ARG   B  1  360  ? -11.869 -7.209  100.526 0.50 31.50 ? 358  ARG   B CD    1 
ATOM   11622 N  NE    A ARG   B  1  360  ? -13.284 -6.066  100.829 0.50 31.59 ? 358  ARG   B NE    1 
ATOM   11623 N  NE    B ARG   B  1  360  ? -12.357 -5.975  99.920  0.50 31.53 ? 358  ARG   B NE    1 
ATOM   11624 C  CZ    A ARG   B  1  360  ? -13.977 -5.170  100.140 0.50 32.97 ? 358  ARG   B CZ    1 
ATOM   11625 C  CZ    B ARG   B  1  360  ? -13.546 -5.444  100.170 0.50 33.15 ? 358  ARG   B CZ    1 
ATOM   11626 N  NH1   A ARG   B  1  360  ? -13.471 -4.580  99.069  0.50 35.82 ? 358  ARG   B NH1   1 
ATOM   11627 N  NH1   B ARG   B  1  360  ? -14.367 -5.976  101.063 0.50 36.96 ? 358  ARG   B NH1   1 
ATOM   11628 N  NH2   A ARG   B  1  360  ? -15.212 -4.865  100.530 0.50 34.85 ? 358  ARG   B NH2   1 
ATOM   11629 N  NH2   B ARG   B  1  360  ? -13.931 -4.364  99.498  0.50 35.68 ? 358  ARG   B NH2   1 
ATOM   11630 N  N     . ARG   B  1  361  ? -6.539  -7.081  101.572 1.00 23.34 ? 359  ARG   B N     1 
ATOM   11631 C  CA    . ARG   B  1  361  ? -5.479  -8.050  101.324 1.00 27.19 ? 359  ARG   B CA    1 
ATOM   11632 C  C     . ARG   B  1  361  ? -4.411  -8.081  102.408 1.00 23.41 ? 359  ARG   B C     1 
ATOM   11633 O  O     . ARG   B  1  361  ? -3.695  -9.080  102.512 1.00 25.01 ? 359  ARG   B O     1 
ATOM   11634 C  CB    . ARG   B  1  361  ? -4.863  -7.858  99.939  1.00 31.68 ? 359  ARG   B CB    1 
ATOM   11635 C  CG    . ARG   B  1  361  ? -4.128  -6.568  99.758  1.00 30.18 ? 359  ARG   B CG    1 
ATOM   11636 C  CD    . ARG   B  1  361  ? -3.743  -6.400  98.287  1.00 23.56 ? 359  ARG   B CD    1 
ATOM   11637 N  NE    . ARG   B  1  361  ? -3.559  -4.993  97.963  1.00 22.96 ? 359  ARG   B NE    1 
ATOM   11638 C  CZ    . ARG   B  1  361  ? -2.408  -4.344  98.046  1.00 21.69 ? 359  ARG   B CZ    1 
ATOM   11639 N  NH1   . ARG   B  1  361  ? -1.297  -4.952  98.427  1.00 24.17 ? 359  ARG   B NH1   1 
ATOM   11640 N  NH2   . ARG   B  1  361  ? -2.368  -3.053  97.731  1.00 20.99 ? 359  ARG   B NH2   1 
ATOM   11641 N  N     . SER   B  1  362  ? -4.304  -7.038  103.235 1.00 22.91 ? 360  SER   B N     1 
ATOM   11642 C  CA    . SER   B  1  362  ? -3.286  -6.985  104.274 1.00 23.81 ? 360  SER   B CA    1 
ATOM   11643 C  C     . SER   B  1  362  ? -3.803  -7.392  105.648 1.00 24.02 ? 360  SER   B C     1 
ATOM   11644 O  O     . SER   B  1  362  ? -2.997  -7.538  106.574 1.00 25.84 ? 360  SER   B O     1 
ATOM   11645 C  CB    . SER   B  1  362  ? -2.670  -5.579  104.350 1.00 25.77 ? 360  SER   B CB    1 
ATOM   11646 O  OG    . SER   B  1  362  ? -3.620  -4.634  104.812 1.00 23.90 ? 360  SER   B OG    1 
ATOM   11647 N  N     . GLY   B  1  363  ? -5.110  -7.559  105.818 1.00 23.71 ? 361  GLY   B N     1 
ATOM   11648 C  CA    . GLY   B  1  363  ? -5.632  -7.898  107.129 1.00 24.81 ? 361  GLY   B CA    1 
ATOM   11649 C  C     . GLY   B  1  363  ? -5.517  -6.770  108.128 1.00 24.63 ? 361  GLY   B C     1 
ATOM   11650 O  O     . GLY   B  1  363  ? -5.295  -7.015  109.318 1.00 26.98 ? 361  GLY   B O     1 
ATOM   11651 N  N     . ARG   B  1  364  ? -5.662  -5.537  107.666 1.00 23.05 ? 362  ARG   B N     1 
ATOM   11652 C  CA    . ARG   B  1  364  ? -5.582  -4.346  108.496 1.00 26.99 ? 362  ARG   B CA    1 
ATOM   11653 C  C     . ARG   B  1  364  ? -6.860  -3.567  108.266 1.00 27.09 ? 362  ARG   B C     1 
ATOM   11654 O  O     . ARG   B  1  364  ? -7.205  -3.277  107.118 1.00 28.25 ? 362  ARG   B O     1 
ATOM   11655 C  CB    . ARG   B  1  364  ? -4.438  -3.444  108.027 1.00 26.17 ? 362  ARG   B CB    1 
ATOM   11656 C  CG    . ARG   B  1  364  ? -3.048  -4.040  108.101 1.00 24.78 ? 362  ARG   B CG    1 
ATOM   11657 C  CD    . ARG   B  1  364  ? -2.544  -4.092  109.526 1.00 24.75 ? 362  ARG   B CD    1 
ATOM   11658 N  NE    . ARG   B  1  364  ? -1.276  -4.805  109.592 1.00 25.58 ? 362  ARG   B NE    1 
ATOM   11659 C  CZ    . ARG   B  1  364  ? -0.088  -4.245  109.400 1.00 22.40 ? 362  ARG   B CZ    1 
ATOM   11660 N  NH1   . ARG   B  1  364  ? 0.041   -2.943  109.190 1.00 24.11 ? 362  ARG   B NH1   1 
ATOM   11661 N  NH2   . ARG   B  1  364  ? 1.000   -5.007  109.439 1.00 26.75 ? 362  ARG   B NH2   1 
ATOM   11662 N  N     . ARG   B  1  365  ? -7.564  -3.226  109.331 1.00 25.87 ? 363  ARG   B N     1 
ATOM   11663 C  CA    . ARG   B  1  365  ? -8.580  -2.201  109.191 1.00 24.32 ? 363  ARG   B CA    1 
ATOM   11664 C  C     . ARG   B  1  365  ? -7.845  -0.877  109.158 1.00 22.09 ? 363  ARG   B C     1 
ATOM   11665 O  O     . ARG   B  1  365  ? -7.105  -0.557  110.086 1.00 23.01 ? 363  ARG   B O     1 
ATOM   11666 C  CB    . ARG   B  1  365  ? -9.578  -2.238  110.341 1.00 26.66 ? 363  ARG   B CB    1 
ATOM   11667 C  CG    . ARG   B  1  365  ? -10.815 -1.391  110.074 1.00 27.69 ? 363  ARG   B CG    1 
ATOM   11668 C  CD    . ARG   B  1  365  ? -11.923 -1.760  111.060 1.00 29.62 ? 363  ARG   B CD    1 
ATOM   11669 N  NE    . ARG   B  1  365  ? -13.208 -1.159  110.723 1.00 31.81 ? 363  ARG   B NE    1 
ATOM   11670 C  CZ    . ARG   B  1  365  ? -13.927 -0.411  111.551 1.00 30.01 ? 363  ARG   B CZ    1 
ATOM   11671 N  NH1   . ARG   B  1  365  ? -13.514 -0.148  112.781 1.00 28.74 ? 363  ARG   B NH1   1 
ATOM   11672 N  NH2   . ARG   B  1  365  ? -15.094 0.075   111.139 1.00 26.37 ? 363  ARG   B NH2   1 
ATOM   11673 N  N     . ILE   B  1  366  ? -7.979  -0.151  108.069 1.00 22.70 ? 364  ILE   B N     1 
ATOM   11674 C  CA    . ILE   B  1  366  ? -7.328  1.140   107.924 1.00 22.10 ? 364  ILE   B CA    1 
ATOM   11675 C  C     . ILE   B  1  366  ? -8.337  2.201   108.314 1.00 25.14 ? 364  ILE   B C     1 
ATOM   11676 O  O     . ILE   B  1  366  ? -9.504  2.140   107.903 1.00 23.15 ? 364  ILE   B O     1 
ATOM   11677 C  CB    . ILE   B  1  366  ? -6.828  1.343   106.482 1.00 21.97 ? 364  ILE   B CB    1 
ATOM   11678 C  CG1   . ILE   B  1  366  ? -5.842  0.234   106.114 1.00 24.58 ? 364  ILE   B CG1   1 
ATOM   11679 C  CG2   . ILE   B  1  366  ? -6.200  2.717   106.317 1.00 20.60 ? 364  ILE   B CG2   1 
ATOM   11680 C  CD1   . ILE   B  1  366  ? -5.383  0.262   104.674 1.00 25.57 ? 364  ILE   B CD1   1 
ATOM   11681 N  N     . MET   B  1  367  ? -7.908  3.148   109.143 1.00 22.56 ? 365  MET   B N     1 
ATOM   11682 C  CA    . MET   B  1  367  ? -8.763  4.269   109.494 1.00 23.23 ? 365  MET   B CA    1 
ATOM   11683 C  C     . MET   B  1  367  ? -8.653  5.278   108.373 1.00 23.11 ? 365  MET   B C     1 
ATOM   11684 O  O     . MET   B  1  367  ? -7.547  5.698   108.023 1.00 22.84 ? 365  MET   B O     1 
ATOM   11685 C  CB    . MET   B  1  367  ? -8.298  4.884   110.807 1.00 20.95 ? 365  MET   B CB    1 
ATOM   11686 C  CG    . MET   B  1  367  ? -8.100  3.856   111.890 1.00 20.24 ? 365  MET   B CG    1 
ATOM   11687 S  SD    . MET   B  1  367  ? -7.638  4.598   113.465 1.00 24.17 ? 365  MET   B SD    1 
ATOM   11688 C  CE    . MET   B  1  367  ? -9.159  4.644   114.415 1.00 28.98 ? 365  MET   B CE    1 
ATOM   11689 N  N     . VAL   B  1  368  ? -9.779  5.651   107.785 1.00 20.18 ? 366  VAL   B N     1 
ATOM   11690 C  CA    . VAL   B  1  368  ? -9.765  6.507   106.612 1.00 20.71 ? 366  VAL   B CA    1 
ATOM   11691 C  C     . VAL   B  1  368  ? -10.481 7.794   106.963 1.00 21.50 ? 366  VAL   B C     1 
ATOM   11692 O  O     . VAL   B  1  368  ? -11.702 7.801   107.168 1.00 21.77 ? 366  VAL   B O     1 
ATOM   11693 C  CB    . VAL   B  1  368  ? -10.406 5.837   105.395 1.00 22.50 ? 366  VAL   B CB    1 
ATOM   11694 C  CG1   . VAL   B  1  368  ? -10.367 6.793   104.234 1.00 22.05 ? 366  VAL   B CG1   1 
ATOM   11695 C  CG2   . VAL   B  1  368  ? -9.680  4.550   105.060 1.00 23.65 ? 366  VAL   B CG2   1 
ATOM   11696 N  N     . ARG   B  1  369  ? -9.731  8.885   107.039 1.00 19.75 ? 367  ARG   B N     1 
ATOM   11697 C  CA    . ARG   B  1  369  ? -10.326 10.182  107.301 1.00 19.10 ? 367  ARG   B CA    1 
ATOM   11698 C  C     . ARG   B  1  369  ? -10.715 10.785  105.970 1.00 19.12 ? 367  ARG   B C     1 
ATOM   11699 O  O     . ARG   B  1  369  ? -9.856  11.092  105.141 1.00 19.38 ? 367  ARG   B O     1 
ATOM   11700 C  CB    . ARG   B  1  369  ? -9.383  11.111  108.063 1.00 17.79 ? 367  ARG   B CB    1 
ATOM   11701 C  CG    . ARG   B  1  369  ? -10.072 12.416  108.412 1.00 21.02 ? 367  ARG   B CG    1 
ATOM   11702 C  CD    . ARG   B  1  369  ? -9.083  13.475  108.774 1.00 19.40 ? 367  ARG   B CD    1 
ATOM   11703 N  NE    . ARG   B  1  369  ? -8.391  13.143  110.009 1.00 19.06 ? 367  ARG   B NE    1 
ATOM   11704 C  CZ    . ARG   B  1  369  ? -7.180  13.574  110.322 1.00 19.45 ? 367  ARG   B CZ    1 
ATOM   11705 N  NH1   . ARG   B  1  369  ? -6.500  14.371  109.512 1.00 19.04 ? 367  ARG   B NH1   1 
ATOM   11706 N  NH2   . ARG   B  1  369  ? -6.637  13.183  111.473 1.00 20.26 ? 367  ARG   B NH2   1 
ATOM   11707 N  N     . LEU   B  1  370  ? -12.008 10.946  105.764 1.00 19.13 ? 368  LEU   B N     1 
ATOM   11708 C  CA    . LEU   B  1  370  ? -12.500 11.629  104.587 1.00 19.51 ? 368  LEU   B CA    1 
ATOM   11709 C  C     . LEU   B  1  370  ? -12.631 13.102  104.923 1.00 18.74 ? 368  LEU   B C     1 
ATOM   11710 O  O     . LEU   B  1  370  ? -13.351 13.474  105.858 1.00 20.27 ? 368  LEU   B O     1 
ATOM   11711 C  CB    . LEU   B  1  370  ? -13.844 11.048  104.164 1.00 19.08 ? 368  LEU   B CB    1 
ATOM   11712 C  CG    . LEU   B  1  370  ? -14.386 11.643  102.868 1.00 20.65 ? 368  LEU   B CG    1 
ATOM   11713 C  CD1   . LEU   B  1  370  ? -13.523 11.249  101.680 1.00 22.40 ? 368  LEU   B CD1   1 
ATOM   11714 C  CD2   . LEU   B  1  370  ? -15.822 11.176  102.679 1.00 21.47 ? 368  LEU   B CD2   1 
ATOM   11715 N  N     . VAL   B  1  371  ? -11.903 13.929  104.187 1.00 17.39 ? 369  VAL   B N     1 
ATOM   11716 C  CA    . VAL   B  1  371  ? -11.958 15.368  104.329 1.00 18.03 ? 369  VAL   B CA    1 
ATOM   11717 C  C     . VAL   B  1  371  ? -12.341 15.924  102.985 1.00 18.01 ? 369  VAL   B C     1 
ATOM   11718 O  O     . VAL   B  1  371  ? -12.314 15.226  101.973 1.00 19.49 ? 369  VAL   B O     1 
ATOM   11719 C  CB    . VAL   B  1  371  ? -10.614 15.956  104.790 1.00 17.00 ? 369  VAL   B CB    1 
ATOM   11720 C  CG1   . VAL   B  1  371  ? -10.159 15.275  106.056 1.00 19.06 ? 369  VAL   B CG1   1 
ATOM   11721 C  CG2   . VAL   B  1  371  ? -9.569  15.807  103.703 1.00 19.31 ? 369  VAL   B CG2   1 
ATOM   11722 N  N     . LYS   B  1  372  ? -12.650 17.211  102.963 1.00 17.28 ? 370  LYS   B N     1 
ATOM   11723 C  CA    . LYS   B  1  372  ? -12.770 17.852  101.666 1.00 19.17 ? 370  LYS   B CA    1 
ATOM   11724 C  C     . LYS   B  1  372  ? -11.390 18.206  101.112 1.00 17.30 ? 370  LYS   B C     1 
ATOM   11725 O  O     . LYS   B  1  372  ? -10.961 17.653  100.096 1.00 18.20 ? 370  LYS   B O     1 
ATOM   11726 C  CB    . LYS   B  1  372  ? -13.787 18.998  101.720 1.00 19.16 ? 370  LYS   B CB    1 
ATOM   11727 C  CG    . LYS   B  1  372  ? -15.168 18.408  102.000 1.00 19.64 ? 370  LYS   B CG    1 
ATOM   11728 C  CD    . LYS   B  1  372  ? -16.288 19.416  102.069 1.00 20.27 ? 370  LYS   B CD    1 
ATOM   11729 C  CE    . LYS   B  1  372  ? -17.576 18.725  102.526 1.00 22.00 ? 370  LYS   B CE    1 
ATOM   11730 N  NZ    . LYS   B  1  372  ? -18.642 19.732  102.804 1.00 21.70 ? 370  LYS   B NZ    1 
ATOM   11731 N  N     . GLY   B  1  373  ? -10.659 19.073  101.783 1.00 17.37 ? 371  GLY   B N     1 
ATOM   11732 C  CA    . GLY   B  1  373  ? -9.271  19.320  101.429 1.00 16.03 ? 371  GLY   B CA    1 
ATOM   11733 C  C     . GLY   B  1  373  ? -8.874  20.751  101.747 1.00 17.19 ? 371  GLY   B C     1 
ATOM   11734 O  O     . GLY   B  1  373  ? -9.647  21.687  101.619 1.00 18.54 ? 371  GLY   B O     1 
ATOM   11735 N  N     . ALA   B  1  374  ? -7.610  20.929  102.141 1.00 15.24 ? 372  ALA   B N     1 
ATOM   11736 C  CA    . ALA   B  1  374  ? -7.165  22.183  102.729 1.00 16.96 ? 372  ALA   B CA    1 
ATOM   11737 C  C     . ALA   B  1  374  ? -6.344  23.052  101.799 1.00 16.13 ? 372  ALA   B C     1 
ATOM   11738 O  O     . ALA   B  1  374  ? -5.955  24.149  102.198 1.00 18.97 ? 372  ALA   B O     1 
ATOM   11739 C  CB    . ALA   B  1  374  ? -6.336  21.917  103.981 1.00 18.33 ? 372  ALA   B CB    1 
ATOM   11740 N  N     . TYR   B  1  375  ? -6.071  22.608  100.574 1.00 15.54 ? 373  TYR   B N     1 
ATOM   11741 C  CA    . TYR   B  1  375  ? -5.110  23.303  99.728  1.00 14.98 ? 373  TYR   B CA    1 
ATOM   11742 C  C     . TYR   B  1  375  ? -5.748  23.826  98.452  1.00 15.15 ? 373  TYR   B C     1 
ATOM   11743 O  O     . TYR   B  1  375  ? -5.070  23.983  97.443  1.00 15.58 ? 373  TYR   B O     1 
ATOM   11744 C  CB    . TYR   B  1  375  ? -3.943  22.390  99.365  1.00 16.08 ? 373  TYR   B CB    1 
ATOM   11745 C  CG    . TYR   B  1  375  ? -3.220  21.800  100.549 1.00 17.21 ? 373  TYR   B CG    1 
ATOM   11746 C  CD1   . TYR   B  1  375  ? -3.767  20.744  101.274 1.00 16.39 ? 373  TYR   B CD1   1 
ATOM   11747 C  CD2   . TYR   B  1  375  ? -1.962  22.270  100.920 1.00 18.64 ? 373  TYR   B CD2   1 
ATOM   11748 C  CE1   . TYR   B  1  375  ? -3.100  20.207  102.354 1.00 16.81 ? 373  TYR   B CE1   1 
ATOM   11749 C  CE2   . TYR   B  1  375  ? -1.285  21.725  101.981 1.00 20.68 ? 373  TYR   B CE2   1 
ATOM   11750 C  CZ    . TYR   B  1  375  ? -1.857  20.699  102.692 1.00 18.30 ? 373  TYR   B CZ    1 
ATOM   11751 O  OH    . TYR   B  1  375  ? -1.180  20.153  103.745 1.00 20.22 ? 373  TYR   B OH    1 
ATOM   11752 N  N     . TRP   B  1  376  ? -7.044  24.117  98.486  1.00 15.56 ? 374  TRP   B N     1 
ATOM   11753 C  CA    . TRP   B  1  376  ? -7.766  24.321  97.236  1.00 14.68 ? 374  TRP   B CA    1 
ATOM   11754 C  C     . TRP   B  1  376  ? -7.182  25.465  96.411  1.00 15.47 ? 374  TRP   B C     1 
ATOM   11755 O  O     . TRP   B  1  376  ? -6.852  25.285  95.236  1.00 15.67 ? 374  TRP   B O     1 
ATOM   11756 C  CB    . TRP   B  1  376  ? -9.251  24.530  97.513  1.00 14.61 ? 374  TRP   B CB    1 
ATOM   11757 C  CG    . TRP   B  1  376  ? -9.994  24.695  96.232  1.00 17.20 ? 374  TRP   B CG    1 
ATOM   11758 C  CD1   . TRP   B  1  376  ? -10.375 23.706  95.367  1.00 15.69 ? 374  TRP   B CD1   1 
ATOM   11759 C  CD2   . TRP   B  1  376  ? -10.391 25.925  95.634  1.00 17.06 ? 374  TRP   B CD2   1 
ATOM   11760 N  NE1   . TRP   B  1  376  ? -11.017 24.249  94.280  1.00 15.77 ? 374  TRP   B NE1   1 
ATOM   11761 C  CE2   . TRP   B  1  376  ? -11.042 25.610  94.421  1.00 16.45 ? 374  TRP   B CE2   1 
ATOM   11762 C  CE3   . TRP   B  1  376  ? -10.296 27.265  96.026  1.00 19.58 ? 374  TRP   B CE3   1 
ATOM   11763 C  CZ2   . TRP   B  1  376  ? -11.555 26.583  93.575  1.00 15.92 ? 374  TRP   B CZ2   1 
ATOM   11764 C  CZ3   . TRP   B  1  376  ? -10.824 28.232  95.202  1.00 19.51 ? 374  TRP   B CZ3   1 
ATOM   11765 C  CH2   . TRP   B  1  376  ? -11.459 27.887  93.988  1.00 19.29 ? 374  TRP   B CH2   1 
ATOM   11766 N  N     . ASP   B  1  377  ? -7.060  26.656  97.000  1.00 16.27 ? 375  ASP   B N     1 
ATOM   11767 C  CA    A ASP   B  1  377  ? -6.549  27.814  96.267  0.60 18.55 ? 375  ASP   B CA    1 
ATOM   11768 C  CA    B ASP   B  1  377  ? -6.584  27.776  96.205  0.40 18.55 ? 375  ASP   B CA    1 
ATOM   11769 C  C     . ASP   B  1  377  ? -5.181  27.523  95.683  1.00 15.81 ? 375  ASP   B C     1 
ATOM   11770 O  O     . ASP   B  1  377  ? -4.870  27.925  94.555  1.00 16.28 ? 375  ASP   B O     1 
ATOM   11771 C  CB    A ASP   B  1  377  ? -6.411  29.009  97.213  0.60 21.09 ? 375  ASP   B CB    1 
ATOM   11772 C  CB    B ASP   B  1  377  ? -6.691  29.103  96.962  0.40 21.57 ? 375  ASP   B CB    1 
ATOM   11773 C  CG    A ASP   B  1  377  ? -7.737  29.528  97.706  0.60 26.39 ? 375  ASP   B CG    1 
ATOM   11774 C  CG    B ASP   B  1  377  ? -6.055  29.054  98.334  0.40 22.30 ? 375  ASP   B CG    1 
ATOM   11775 O  OD1   A ASP   B  1  377  ? -8.662  29.631  96.893  0.60 33.72 ? 375  ASP   B OD1   1 
ATOM   11776 O  OD1   B ASP   B  1  377  ? -4.878  28.660  98.439  0.40 26.38 ? 375  ASP   B OD1   1 
ATOM   11777 O  OD2   A ASP   B  1  377  ? -7.846  29.852  98.904  0.60 36.05 ? 375  ASP   B OD2   1 
ATOM   11778 O  OD2   B ASP   B  1  377  ? -6.732  29.440  99.309  0.40 30.85 ? 375  ASP   B OD2   1 
ATOM   11779 N  N     . ALA   B  1  378  ? -4.338  26.845  96.463  1.00 15.11 ? 376  ALA   B N     1 
ATOM   11780 C  CA    . ALA   B  1  378  ? -2.981  26.573  96.016  1.00 13.98 ? 376  ALA   B CA    1 
ATOM   11781 C  C     . ALA   B  1  378  ? -2.974  25.586  94.864  1.00 14.64 ? 376  ALA   B C     1 
ATOM   11782 O  O     . ALA   B  1  378  ? -2.124  25.684  93.970  1.00 14.76 ? 376  ALA   B O     1 
ATOM   11783 C  CB    . ALA   B  1  378  ? -2.148  26.038  97.180  1.00 16.27 ? 376  ALA   B CB    1 
ATOM   11784 N  N     . GLU   B  1  379  ? -3.904  24.633  94.871  1.00 14.53 ? 377  GLU   B N     1 
ATOM   11785 C  CA    . GLU   B  1  379  ? -3.958  23.664  93.787  1.00 13.71 ? 377  GLU   B CA    1 
ATOM   11786 C  C     . GLU   B  1  379  ? -4.415  24.323  92.501  1.00 16.42 ? 377  GLU   B C     1 
ATOM   11787 O  O     . GLU   B  1  379  ? -3.934  23.977  91.419  1.00 14.93 ? 377  GLU   B O     1 
ATOM   11788 C  CB    . GLU   B  1  379  ? -4.886  22.502  94.146  1.00 15.08 ? 377  GLU   B CB    1 
ATOM   11789 C  CG    . GLU   B  1  379  ? -4.466  21.669  95.357  1.00 16.47 ? 377  GLU   B CG    1 
ATOM   11790 C  CD    . GLU   B  1  379  ? -3.174  20.883  95.203  1.00 18.28 ? 377  GLU   B CD    1 
ATOM   11791 O  OE1   . GLU   B  1  379  ? -2.549  20.864  94.116  1.00 18.49 ? 377  GLU   B OE1   1 
ATOM   11792 O  OE2   . GLU   B  1  379  ? -2.803  20.240  96.205  1.00 17.84 ? 377  GLU   B OE2   1 
ATOM   11793 N  N     . ILE   B  1  380  ? -5.342  25.278  92.589  1.00 14.24 ? 378  ILE   B N     1 
ATOM   11794 C  CA    . ILE   B  1  380  ? -5.748  25.999  91.386  1.00 14.39 ? 378  ILE   B CA    1 
ATOM   11795 C  C     . ILE   B  1  380  ? -4.561  26.750  90.806  1.00 15.14 ? 378  ILE   B C     1 
ATOM   11796 O  O     . ILE   B  1  380  ? -4.267  26.666  89.608  1.00 14.23 ? 378  ILE   B O     1 
ATOM   11797 C  CB    . ILE   B  1  380  ? -6.905  26.959  91.703  1.00 14.36 ? 378  ILE   B CB    1 
ATOM   11798 C  CG1   . ILE   B  1  380  ? -8.103  26.205  92.278  1.00 14.82 ? 378  ILE   B CG1   1 
ATOM   11799 C  CG2   . ILE   B  1  380  ? -7.288  27.727  90.470  1.00 15.60 ? 378  ILE   B CG2   1 
ATOM   11800 C  CD1   . ILE   B  1  380  ? -8.627  25.098  91.357  1.00 16.27 ? 378  ILE   B CD1   1 
ATOM   11801 N  N     . LYS   B  1  381  ? -3.869  27.505  91.657  1.00 14.76 ? 379  LYS   B N     1 
ATOM   11802 C  CA    . LYS   B  1  381  ? -2.739  28.296  91.192  1.00 13.19 ? 379  LYS   B CA    1 
ATOM   11803 C  C     . LYS   B  1  381  ? -1.666  27.410  90.588  1.00 13.75 ? 379  LYS   B C     1 
ATOM   11804 O  O     . LYS   B  1  381  ? -1.127  27.719  89.522  1.00 14.34 ? 379  LYS   B O     1 
ATOM   11805 C  CB    . LYS   B  1  381  ? -2.153  29.110  92.342  1.00 14.21 ? 379  LYS   B CB    1 
ATOM   11806 C  CG    . LYS   B  1  381  ? -0.929  29.900  91.931  1.00 14.83 ? 379  LYS   B CG    1 
ATOM   11807 C  CD    . LYS   B  1  381  ? -0.492  30.793  93.064  1.00 13.26 ? 379  LYS   B CD    1 
ATOM   11808 C  CE    . LYS   B  1  381  ? 0.647   31.673  92.595  1.00 15.45 ? 379  LYS   B CE    1 
ATOM   11809 N  NZ    . LYS   B  1  381  ? 1.105   32.579  93.697  1.00 14.23 ? 379  LYS   B NZ    1 
ATOM   11810 N  N     . ARG   B  1  382  ? -1.362  26.294  91.250  1.00 14.52 ? 380  ARG   B N     1 
ATOM   11811 C  CA    A ARG   B  1  382  ? -0.252  25.467  90.796  0.54 13.86 ? 380  ARG   B CA    1 
ATOM   11812 C  CA    B ARG   B  1  382  ? -0.261  25.446  90.808  0.46 13.91 ? 380  ARG   B CA    1 
ATOM   11813 C  C     . ARG   B  1  382  ? -0.539  24.872  89.426  1.00 13.38 ? 380  ARG   B C     1 
ATOM   11814 O  O     . ARG   B  1  382  ? 0.334   24.860  88.554  1.00 14.55 ? 380  ARG   B O     1 
ATOM   11815 C  CB    A ARG   B  1  382  ? 0.022   24.362  91.814  0.54 15.82 ? 380  ARG   B CB    1 
ATOM   11816 C  CB    B ARG   B  1  382  ? -0.067  24.315  91.819  0.46 15.80 ? 380  ARG   B CB    1 
ATOM   11817 C  CG    A ARG   B  1  382  ? 1.140   23.419  91.403  0.54 19.18 ? 380  ARG   B CG    1 
ATOM   11818 C  CG    B ARG   B  1  382  ? 1.220   23.530  91.649  0.46 19.48 ? 380  ARG   B CG    1 
ATOM   11819 C  CD    A ARG   B  1  382  ? 2.445   24.177  91.181  0.54 16.79 ? 380  ARG   B CD    1 
ATOM   11820 C  CD    B ARG   B  1  382  ? 2.413   24.375  92.050  0.46 24.12 ? 380  ARG   B CD    1 
ATOM   11821 N  NE    A ARG   B  1  382  ? 3.571   23.273  90.974  0.54 21.12 ? 380  ARG   B NE    1 
ATOM   11822 N  NE    B ARG   B  1  382  ? 3.207   24.794  90.904  0.46 22.90 ? 380  ARG   B NE    1 
ATOM   11823 C  CZ    A ARG   B  1  382  ? 4.285   22.724  91.949  0.54 27.46 ? 380  ARG   B CZ    1 
ATOM   11824 C  CZ    B ARG   B  1  382  ? 4.170   25.704  90.953  0.46 23.20 ? 380  ARG   B CZ    1 
ATOM   11825 N  NH1   A ARG   B  1  382  ? 4.020   22.966  93.225  0.54 23.66 ? 380  ARG   B NH1   1 
ATOM   11826 N  NH1   B ARG   B  1  382  ? 4.460   26.346  92.075  0.46 20.19 ? 380  ARG   B NH1   1 
ATOM   11827 N  NH2   A ARG   B  1  382  ? 5.291   21.913  91.638  0.54 29.54 ? 380  ARG   B NH2   1 
ATOM   11828 N  NH2   B ARG   B  1  382  ? 4.863   25.976  89.848  0.46 24.31 ? 380  ARG   B NH2   1 
ATOM   11829 N  N     . ALA   B  1  383  ? -1.754  24.387  89.212  1.00 13.73 ? 381  ALA   B N     1 
ATOM   11830 C  CA    . ALA   B  1  383  ? -2.076  23.796  87.923  1.00 12.22 ? 381  ALA   B CA    1 
ATOM   11831 C  C     . ALA   B  1  383  ? -2.034  24.847  86.832  1.00 14.11 ? 381  ALA   B C     1 
ATOM   11832 O  O     . ALA   B  1  383  ? -1.565  24.575  85.720  1.00 14.66 ? 381  ALA   B O     1 
ATOM   11833 C  CB    . ALA   B  1  383  ? -3.453  23.155  87.997  1.00 14.26 ? 381  ALA   B CB    1 
ATOM   11834 N  N     . GLN   B  1  384  ? -2.481  26.067  87.147  1.00 13.45 ? 382  GLN   B N     1 
ATOM   11835 C  CA    . GLN   B  1  384  ? -2.387  27.152  86.177  1.00 13.36 ? 382  GLN   B CA    1 
ATOM   11836 C  C     . GLN   B  1  384  ? -0.941  27.498  85.877  1.00 13.80 ? 382  GLN   B C     1 
ATOM   11837 O  O     . GLN   B  1  384  ? -0.570  27.645  84.713  1.00 15.17 ? 382  GLN   B O     1 
ATOM   11838 C  CB    . GLN   B  1  384  ? -3.142  28.381  86.670  1.00 13.84 ? 382  GLN   B CB    1 
ATOM   11839 C  CG    . GLN   B  1  384  ? -4.632  28.209  86.608  1.00 13.75 ? 382  GLN   B CG    1 
ATOM   11840 C  CD    . GLN   B  1  384  ? -5.357  29.438  87.018  1.00 14.70 ? 382  GLN   B CD    1 
ATOM   11841 O  OE1   . GLN   B  1  384  ? -4.789  30.321  87.651  1.00 17.33 ? 382  GLN   B OE1   1 
ATOM   11842 N  NE2   . GLN   B  1  384  ? -6.641  29.500  86.691  1.00 14.40 ? 382  GLN   B NE2   1 
ATOM   11843 N  N     . LEU   B  1  385  ? -0.115  27.656  86.918  1.00 13.40 ? 383  LEU   B N     1 
ATOM   11844 C  CA    . LEU   B  1  385  ? 1.295   27.975  86.702  1.00 13.64 ? 383  LEU   B CA    1 
ATOM   11845 C  C     . LEU   B  1  385  ? 1.968   26.925  85.845  1.00 14.74 ? 383  LEU   B C     1 
ATOM   11846 O  O     . LEU   B  1  385  ? 2.819   27.250  85.006  1.00 14.19 ? 383  LEU   B O     1 
ATOM   11847 C  CB    . LEU   B  1  385  ? 2.034   28.060  88.036  1.00 15.55 ? 383  LEU   B CB    1 
ATOM   11848 C  CG    . LEU   B  1  385  ? 1.722   29.254  88.922  1.00 18.17 ? 383  LEU   B CG    1 
ATOM   11849 C  CD1   . LEU   B  1  385  ? 2.492   29.086  90.206  1.00 18.57 ? 383  LEU   B CD1   1 
ATOM   11850 C  CD2   . LEU   B  1  385  ? 2.098   30.555  88.228  1.00 21.16 ? 383  LEU   B CD2   1 
ATOM   11851 N  N     . ASP   B  1  386  ? 1.631   25.660  86.063  1.00 14.94 ? 384  ASP   B N     1 
ATOM   11852 C  CA    . ASP   B  1  386  ? 2.330   24.566  85.412  1.00 13.76 ? 384  ASP   B CA    1 
ATOM   11853 C  C     . ASP   B  1  386  ? 1.752   24.229  84.054  1.00 15.20 ? 384  ASP   B C     1 
ATOM   11854 O  O     . ASP   B  1  386  ? 2.274   23.344  83.375  1.00 15.87 ? 384  ASP   B O     1 
ATOM   11855 C  CB    . ASP   B  1  386  ? 2.381   23.333  86.325  1.00 16.13 ? 384  ASP   B CB    1 
ATOM   11856 C  CG    . ASP   B  1  386  ? 3.281   23.540  87.538  1.00 19.95 ? 384  ASP   B CG    1 
ATOM   11857 O  OD1   . ASP   B  1  386  ? 3.999   24.565  87.605  1.00 20.71 ? 384  ASP   B OD1   1 
ATOM   11858 O  OD2   . ASP   B  1  386  ? 3.272   22.668  88.430  1.00 22.38 ? 384  ASP   B OD2   1 
ATOM   11859 N  N     . GLY   B  1  387  ? 0.677   24.897  83.650  1.00 13.39 ? 385  GLY   B N     1 
ATOM   11860 C  CA    . GLY   B  1  387  ? 0.109   24.664  82.339  1.00 14.57 ? 385  GLY   B CA    1 
ATOM   11861 C  C     . GLY   B  1  387  ? -0.400  23.252  82.166  1.00 16.25 ? 385  GLY   B C     1 
ATOM   11862 O  O     . GLY   B  1  387  ? -0.290  22.680  81.074  1.00 17.08 ? 385  GLY   B O     1 
ATOM   11863 N  N     . LEU   B  1  388  ? -0.955  22.671  83.219  1.00 15.82 ? 386  LEU   B N     1 
ATOM   11864 C  CA    . LEU   B  1  388  ? -1.346  21.274  83.144  1.00 16.28 ? 386  LEU   B CA    1 
ATOM   11865 C  C     . LEU   B  1  388  ? -2.748  21.121  82.561  1.00 16.57 ? 386  LEU   B C     1 
ATOM   11866 O  O     . LEU   B  1  388  ? -3.490  22.087  82.376  1.00 16.53 ? 386  LEU   B O     1 
ATOM   11867 C  CB    . LEU   B  1  388  ? -1.187  20.603  84.503  1.00 16.10 ? 386  LEU   B CB    1 
ATOM   11868 C  CG    . LEU   B  1  388  ? 0.272   20.663  84.939  1.00 15.52 ? 386  LEU   B CG    1 
ATOM   11869 C  CD1   . LEU   B  1  388  ? 0.490   19.995  86.297  1.00 18.23 ? 386  LEU   B CD1   1 
ATOM   11870 C  CD2   . LEU   B  1  388  ? 1.213   20.059  83.887  1.00 18.68 ? 386  LEU   B CD2   1 
ATOM   11871 N  N     . ALA   B  1  389  ? -3.109  19.875  82.259  1.00 16.67 ? 387  ALA   B N     1 
ATOM   11872 C  CA    . ALA   B  1  389  ? -4.291  19.649  81.434  1.00 16.62 ? 387  ALA   B CA    1 
ATOM   11873 C  C     . ALA   B  1  389  ? -5.558  20.101  82.141  1.00 16.96 ? 387  ALA   B C     1 
ATOM   11874 O  O     . ALA   B  1  389  ? -6.498  20.590  81.505  1.00 20.30 ? 387  ALA   B O     1 
ATOM   11875 C  CB    . ALA   B  1  389  ? -4.394  18.173  81.048  1.00 21.36 ? 387  ALA   B CB    1 
ATOM   11876 N  N     . ASP   B  1  390  ? -5.603  19.940  83.452  1.00 17.03 ? 388  ASP   B N     1 
ATOM   11877 C  CA    . ASP   B  1  390  ? -6.780  20.296  84.226  1.00 15.81 ? 388  ASP   B CA    1 
ATOM   11878 C  C     . ASP   B  1  390  ? -6.315  20.387  85.668  1.00 14.63 ? 388  ASP   B C     1 
ATOM   11879 O  O     . ASP   B  1  390  ? -5.144  20.149  85.974  1.00 16.10 ? 388  ASP   B O     1 
ATOM   11880 C  CB    . ASP   B  1  390  ? -7.883  19.248  84.021  1.00 17.03 ? 388  ASP   B CB    1 
ATOM   11881 C  CG    . ASP   B  1  390  ? -9.286  19.808  84.203  1.00 18.82 ? 388  ASP   B CG    1 
ATOM   11882 O  OD1   . ASP   B  1  390  ? -9.528  20.567  85.165  1.00 18.25 ? 388  ASP   B OD1   1 
ATOM   11883 O  OD2   . ASP   B  1  390  ? -10.157 19.477  83.374  1.00 23.36 ? 388  ASP   B OD2   1 
ATOM   11884 N  N     . PHE   B  1  391  ? -7.230  20.708  86.542  1.00 15.32 ? 389  PHE   B N     1 
ATOM   11885 C  CA    . PHE   B  1  391  ? -6.951  20.723  87.963  1.00 14.30 ? 389  PHE   B CA    1 
ATOM   11886 C  C     . PHE   B  1  391  ? -7.038  19.320  88.547  1.00 15.43 ? 389  PHE   B C     1 
ATOM   11887 O  O     . PHE   B  1  391  ? -7.760  18.467  88.027  1.00 17.05 ? 389  PHE   B O     1 
ATOM   11888 C  CB    . PHE   B  1  391  ? -7.962  21.633  88.647  1.00 16.17 ? 389  PHE   B CB    1 
ATOM   11889 C  CG    . PHE   B  1  391  ? -7.937  23.013  88.093  1.00 14.53 ? 389  PHE   B CG    1 
ATOM   11890 C  CD1   . PHE   B  1  391  ? -6.888  23.852  88.413  1.00 14.75 ? 389  PHE   B CD1   1 
ATOM   11891 C  CD2   . PHE   B  1  391  ? -8.893  23.446  87.189  1.00 15.98 ? 389  PHE   B CD2   1 
ATOM   11892 C  CE1   . PHE   B  1  391  ? -6.805  25.125  87.889  1.00 14.98 ? 389  PHE   B CE1   1 
ATOM   11893 C  CE2   . PHE   B  1  391  ? -8.823  24.725  86.661  1.00 15.83 ? 389  PHE   B CE2   1 
ATOM   11894 C  CZ    . PHE   B  1  391  ? -7.777  25.563  87.003  1.00 14.90 ? 389  PHE   B CZ    1 
ATOM   11895 N  N     . PRO   B  1  392  ? -6.310  19.054  89.630  1.00 14.80 ? 390  PRO   B N     1 
ATOM   11896 C  CA    . PRO   B  1  392  ? -6.457  17.773  90.324  1.00 13.86 ? 390  PRO   B CA    1 
ATOM   11897 C  C     . PRO   B  1  392  ? -7.522  17.833  91.401  1.00 15.94 ? 390  PRO   B C     1 
ATOM   11898 O  O     . PRO   B  1  392  ? -7.681  16.874  92.163  1.00 16.29 ? 390  PRO   B O     1 
ATOM   11899 C  CB    . PRO   B  1  392  ? -5.075  17.612  90.958  1.00 15.84 ? 390  PRO   B CB    1 
ATOM   11900 C  CG    . PRO   B  1  392  ? -4.728  19.028  91.364  1.00 15.87 ? 390  PRO   B CG    1 
ATOM   11901 C  CD    . PRO   B  1  392  ? -5.235  19.883  90.220  1.00 14.71 ? 390  PRO   B CD    1 
ATOM   11902 N  N     . VAL   B  1  393  ? -8.210  18.965  91.483  1.00 16.34 ? 391  VAL   B N     1 
ATOM   11903 C  CA    . VAL   B  1  393  ? -9.308  19.163  92.410  1.00 16.67 ? 391  VAL   B CA    1 
ATOM   11904 C  C     . VAL   B  1  393  ? -10.486 19.712  91.620  1.00 16.31 ? 391  VAL   B C     1 
ATOM   11905 O  O     . VAL   B  1  393  ? -10.338 20.198  90.494  1.00 15.50 ? 391  VAL   B O     1 
ATOM   11906 C  CB    . VAL   B  1  393  ? -8.931  20.125  93.558  1.00 16.84 ? 391  VAL   B CB    1 
ATOM   11907 C  CG1   . VAL   B  1  393  ? -7.788  19.550  94.385  1.00 15.25 ? 391  VAL   B CG1   1 
ATOM   11908 C  CG2   . VAL   B  1  393  ? -8.551  21.477  93.003  1.00 16.40 ? 391  VAL   B CG2   1 
ATOM   11909 N  N     . PHE   B  1  394  ? -11.663 19.636  92.230  1.00 15.95 ? 392  PHE   B N     1 
ATOM   11910 C  CA    . PHE   B  1  394  ? -12.838 20.263  91.650  1.00 15.72 ? 392  PHE   B CA    1 
ATOM   11911 C  C     . PHE   B  1  394  ? -12.722 21.778  91.730  1.00 16.82 ? 392  PHE   B C     1 
ATOM   11912 O  O     . PHE   B  1  394  ? -11.927 22.329  92.500  1.00 17.01 ? 392  PHE   B O     1 
ATOM   11913 C  CB    . PHE   B  1  394  ? -14.110 19.741  92.319  1.00 16.31 ? 392  PHE   B CB    1 
ATOM   11914 C  CG    . PHE   B  1  394  ? -14.248 18.264  92.197  1.00 16.46 ? 392  PHE   B CG    1 
ATOM   11915 C  CD1   . PHE   B  1  394  ? -14.496 17.697  90.959  1.00 18.29 ? 392  PHE   B CD1   1 
ATOM   11916 C  CD2   . PHE   B  1  394  ? -14.050 17.437  93.279  1.00 17.23 ? 392  PHE   B CD2   1 
ATOM   11917 C  CE1   . PHE   B  1  394  ? -14.574 16.337  90.816  1.00 18.16 ? 392  PHE   B CE1   1 
ATOM   11918 C  CE2   . PHE   B  1  394  ? -14.123 16.079  93.139  1.00 16.76 ? 392  PHE   B CE2   1 
ATOM   11919 C  CZ    . PHE   B  1  394  ? -14.386 15.526  91.900  1.00 19.38 ? 392  PHE   B CZ    1 
ATOM   11920 N  N     . THR   B  1  395  ? -13.501 22.454  90.880  1.00 16.93 ? 393  THR   B N     1 
ATOM   11921 C  CA    . THR   B  1  395  ? -13.508 23.906  90.840  1.00 16.46 ? 393  THR   B CA    1 
ATOM   11922 C  C     . THR   B  1  395  ? -14.805 24.524  91.321  1.00 15.56 ? 393  THR   B C     1 
ATOM   11923 O  O     . THR   B  1  395  ? -14.842 25.744  91.494  1.00 18.20 ? 393  THR   B O     1 
ATOM   11924 C  CB    . THR   B  1  395  ? -13.202 24.437  89.435  1.00 16.95 ? 393  THR   B CB    1 
ATOM   11925 O  OG1   . THR   B  1  395  ? -14.198 23.971  88.525  1.00 18.07 ? 393  THR   B OG1   1 
ATOM   11926 C  CG2   . THR   B  1  395  ? -11.840 23.966  88.973  1.00 17.83 ? 393  THR   B CG2   1 
ATOM   11927 N  N     . ARG   B  1  396  ? -15.858 23.737  91.508  1.00 17.46 ? 394  ARG   B N     1 
ATOM   11928 C  CA    . ARG   B  1  396  ? -17.084 24.205  92.137  1.00 19.30 ? 394  ARG   B CA    1 
ATOM   11929 C  C     . ARG   B  1  396  ? -17.199 23.531  93.487  1.00 18.93 ? 394  ARG   B C     1 
ATOM   11930 O  O     . ARG   B  1  396  ? -17.040 22.309  93.595  1.00 19.47 ? 394  ARG   B O     1 
ATOM   11931 C  CB    . ARG   B  1  396  ? -18.321 23.881  91.302  1.00 19.31 ? 394  ARG   B CB    1 
ATOM   11932 C  CG    . ARG   B  1  396  ? -18.336 24.591  89.982  1.00 21.16 ? 394  ARG   B CG    1 
ATOM   11933 C  CD    . ARG   B  1  396  ? -19.705 24.416  89.334  1.00 24.08 ? 394  ARG   B CD    1 
ATOM   11934 N  NE    . ARG   B  1  396  ? -19.659 24.860  87.950  1.00 25.90 ? 394  ARG   B NE    1 
ATOM   11935 C  CZ    . ARG   B  1  396  ? -20.503 25.721  87.400  1.00 29.66 ? 394  ARG   B CZ    1 
ATOM   11936 N  NH1   . ARG   B  1  396  ? -21.561 26.170  88.058  1.00 31.40 ? 394  ARG   B NH1   1 
ATOM   11937 N  NH2   . ARG   B  1  396  ? -20.282 26.139  86.154  1.00 27.67 ? 394  ARG   B NH2   1 
ATOM   11938 N  N     . LYS   B  1  397  ? -17.495 24.327  94.512  1.00 19.24 ? 395  LYS   B N     1 
ATOM   11939 C  CA    . LYS   B  1  397  ? -17.510 23.790  95.861  1.00 20.38 ? 395  LYS   B CA    1 
ATOM   11940 C  C     . LYS   B  1  397  ? -18.568 22.706  96.002  1.00 19.49 ? 395  LYS   B C     1 
ATOM   11941 O  O     . LYS   B  1  397  ? -18.370 21.713  96.708  1.00 21.44 ? 395  LYS   B O     1 
ATOM   11942 C  CB    . LYS   B  1  397  ? -17.726 24.940  96.839  1.00 23.82 ? 395  LYS   B CB    1 
ATOM   11943 C  CG    . LYS   B  1  397  ? -17.422 24.593  98.258  1.00 22.82 ? 395  LYS   B CG    1 
ATOM   11944 C  CD    . LYS   B  1  397  ? -18.650 24.133  98.968  1.00 24.70 ? 395  LYS   B CD    1 
ATOM   11945 C  CE    . LYS   B  1  397  ? -18.323 23.847  100.412 1.00 24.34 ? 395  LYS   B CE    1 
ATOM   11946 N  NZ    . LYS   B  1  397  ? -19.523 23.326  101.097 1.00 23.46 ? 395  LYS   B NZ    1 
ATOM   11947 N  N     . ILE   B  1  398  ? -19.693 22.868  95.309  1.00 21.94 ? 396  ILE   B N     1 
ATOM   11948 C  CA    . ILE   B  1  398  ? -20.747 21.863  95.352  1.00 25.39 ? 396  ILE   B CA    1 
ATOM   11949 C  C     . ILE   B  1  398  ? -20.261 20.526  94.798  1.00 17.75 ? 396  ILE   B C     1 
ATOM   11950 O  O     . ILE   B  1  398  ? -20.753 19.462  95.196  1.00 21.84 ? 396  ILE   B O     1 
ATOM   11951 C  CB    . ILE   B  1  398  ? -21.987 22.409  94.618  1.00 26.32 ? 396  ILE   B CB    1 
ATOM   11952 C  CG1   . ILE   B  1  398  ? -23.217 21.605  94.981  1.00 32.02 ? 396  ILE   B CG1   1 
ATOM   11953 C  CG2   . ILE   B  1  398  ? -21.759 22.429  93.111  1.00 24.69 ? 396  ILE   B CG2   1 
ATOM   11954 C  CD1   . ILE   B  1  398  ? -24.486 22.327  94.666  1.00 33.61 ? 396  ILE   B CD1   1 
ATOM   11955 N  N     . HIS   B  1  399  ? -19.269 20.551  93.902  1.00 20.05 ? 397  HIS   B N     1 
ATOM   11956 C  CA    . HIS   B  1  399  ? -18.726 19.302  93.378  1.00 19.39 ? 397  HIS   B CA    1 
ATOM   11957 C  C     . HIS   B  1  399  ? -17.949 18.554  94.442  1.00 18.45 ? 397  HIS   B C     1 
ATOM   11958 O  O     . HIS   B  1  399  ? -18.053 17.329  94.551  1.00 20.36 ? 397  HIS   B O     1 
ATOM   11959 C  CB    . HIS   B  1  399  ? -17.825 19.596  92.191  1.00 19.06 ? 397  HIS   B CB    1 
ATOM   11960 C  CG    . HIS   B  1  399  ? -18.569 20.099  91.001  1.00 20.90 ? 397  HIS   B CG    1 
ATOM   11961 N  ND1   . HIS   B  1  399  ? -17.934 20.616  89.896  1.00 20.12 ? 397  HIS   B ND1   1 
ATOM   11962 C  CD2   . HIS   B  1  399  ? -19.897 20.158  90.741  1.00 22.81 ? 397  HIS   B CD2   1 
ATOM   11963 C  CE1   . HIS   B  1  399  ? -18.839 20.971  89.000  1.00 22.30 ? 397  HIS   B CE1   1 
ATOM   11964 N  NE2   . HIS   B  1  399  ? -20.037 20.704  89.488  1.00 22.97 ? 397  HIS   B NE2   1 
ATOM   11965 N  N     . THR   B  1  400  ? -17.153 19.276  95.228  1.00 19.08 ? 398  THR   B N     1 
ATOM   11966 C  CA    . THR   B  1  400  ? -16.477 18.651  96.355  1.00 18.72 ? 398  THR   B CA    1 
ATOM   11967 C  C     . THR   B  1  400  ? -17.481 18.066  97.336  1.00 17.00 ? 398  THR   B C     1 
ATOM   11968 O  O     . THR   B  1  400  ? -17.278 16.966  97.858  1.00 20.54 ? 398  THR   B O     1 
ATOM   11969 C  CB    . THR   B  1  400  ? -15.588 19.688  97.024  1.00 18.37 ? 398  THR   B CB    1 
ATOM   11970 O  OG1   . THR   B  1  400  ? -14.518 19.979  96.126  1.00 17.31 ? 398  THR   B OG1   1 
ATOM   11971 C  CG2   . THR   B  1  400  ? -15.023 19.157  98.318  1.00 20.60 ? 398  THR   B CG2   1 
ATOM   11972 N  N     . ASP   B  1  401  ? -18.593 18.773  97.572  1.00 20.07 ? 399  ASP   B N     1 
ATOM   11973 C  CA    . ASP   B  1  401  ? -19.610 18.255  98.483  1.00 22.46 ? 399  ASP   B CA    1 
ATOM   11974 C  C     . ASP   B  1  401  ? -20.213 16.967  97.948  1.00 18.94 ? 399  ASP   B C     1 
ATOM   11975 O  O     . ASP   B  1  401  ? -20.406 16.003  98.695  1.00 21.53 ? 399  ASP   B O     1 
ATOM   11976 C  CB    . ASP   B  1  401  ? -20.711 19.295  98.713  1.00 24.11 ? 399  ASP   B CB    1 
ATOM   11977 C  CG    . ASP   B  1  401  ? -20.242 20.474  99.534  1.00 29.22 ? 399  ASP   B CG    1 
ATOM   11978 O  OD1   . ASP   B  1  401  ? -19.256 20.321  100.295 1.00 25.42 ? 399  ASP   B OD1   1 
ATOM   11979 O  OD2   . ASP   B  1  401  ? -20.854 21.557  99.420  1.00 26.45 ? 399  ASP   B OD2   1 
ATOM   11980 N  N     . VAL   B  1  402  ? -20.518 16.933  96.649  1.00 20.19 ? 400  VAL   B N     1 
ATOM   11981 C  CA    . VAL   B  1  402  ? -21.041 15.711  96.052  1.00 22.26 ? 400  VAL   B CA    1 
ATOM   11982 C  C     . VAL   B  1  402  ? -20.003 14.605  96.117  1.00 17.84 ? 400  VAL   B C     1 
ATOM   11983 O  O     . VAL   B  1  402  ? -20.317 13.455  96.458  1.00 21.26 ? 400  VAL   B O     1 
ATOM   11984 C  CB    . VAL   B  1  402  ? -21.508 15.973  94.610  1.00 21.50 ? 400  VAL   B CB    1 
ATOM   11985 C  CG1   . VAL   B  1  402  ? -21.877 14.665  93.933  1.00 25.70 ? 400  VAL   B CG1   1 
ATOM   11986 C  CG2   . VAL   B  1  402  ? -22.676 16.950  94.607  1.00 24.19 ? 400  VAL   B CG2   1 
ATOM   11987 N  N     . SER   B  1  403  ? -18.748 14.936  95.796  1.00 20.21 ? 401  SER   B N     1 
ATOM   11988 C  CA    . SER   B  1  403  ? -17.671 13.954  95.887  1.00 22.71 ? 401  SER   B CA    1 
ATOM   11989 C  C     . SER   B  1  403  ? -17.552 13.392  97.298  1.00 17.76 ? 401  SER   B C     1 
ATOM   11990 O  O     . SER   B  1  403  ? -17.410 12.180  97.487  1.00 20.44 ? 401  SER   B O     1 
ATOM   11991 C  CB    . SER   B  1  403  ? -16.357 14.603  95.456  1.00 19.54 ? 401  SER   B CB    1 
ATOM   11992 O  OG    . SER   B  1  403  ? -15.268 13.719  95.655  1.00 19.69 ? 401  SER   B OG    1 
ATOM   11993 N  N     . TYR   B  1  404  ? -17.639 14.260  98.305  1.00 21.03 ? 402  TYR   B N     1 
ATOM   11994 C  CA    . TYR   B  1  404  ? -17.555 13.805  99.688  1.00 21.69 ? 402  TYR   B CA    1 
ATOM   11995 C  C     . TYR   B  1  404  ? -18.675 12.822  100.003 1.00 20.29 ? 402  TYR   B C     1 
ATOM   11996 O  O     . TYR   B  1  404  ? -18.443 11.751  100.575 1.00 21.97 ? 402  TYR   B O     1 
ATOM   11997 C  CB    . TYR   B  1  404  ? -17.630 15.020  100.607 1.00 21.72 ? 402  TYR   B CB    1 
ATOM   11998 C  CG    . TYR   B  1  404  ? -17.270 14.734  102.046 1.00 20.21 ? 402  TYR   B CG    1 
ATOM   11999 C  CD1   . TYR   B  1  404  ? -18.175 14.136  102.910 1.00 23.35 ? 402  TYR   B CD1   1 
ATOM   12000 C  CD2   . TYR   B  1  404  ? -16.020 15.071  102.538 1.00 20.18 ? 402  TYR   B CD2   1 
ATOM   12001 C  CE1   . TYR   B  1  404  ? -17.845 13.887  104.230 1.00 23.14 ? 402  TYR   B CE1   1 
ATOM   12002 C  CE2   . TYR   B  1  404  ? -15.681 14.820  103.855 1.00 20.39 ? 402  TYR   B CE2   1 
ATOM   12003 C  CZ    . TYR   B  1  404  ? -16.600 14.225  104.694 1.00 23.35 ? 402  TYR   B CZ    1 
ATOM   12004 O  OH    . TYR   B  1  404  ? -16.288 13.967  106.010 1.00 23.63 ? 402  TYR   B OH    1 
ATOM   12005 N  N     . ILE   B  1  405  ? -19.906 13.172  99.625  1.00 24.05 ? 403  ILE   B N     1 
ATOM   12006 C  CA    . ILE   B  1  405  ? -21.042 12.307  99.926  1.00 24.77 ? 403  ILE   B CA    1 
ATOM   12007 C  C     . ILE   B  1  405  ? -20.932 10.986  99.174  1.00 21.85 ? 403  ILE   B C     1 
ATOM   12008 O  O     . ILE   B  1  405  ? -21.201 9.915   99.729  1.00 24.78 ? 403  ILE   B O     1 
ATOM   12009 C  CB    . ILE   B  1  405  ? -22.368 13.049  99.669  1.00 26.35 ? 403  ILE   B CB    1 
ATOM   12010 C  CG1   . ILE   B  1  405  ? -22.498 14.234  100.633 1.00 27.76 ? 403  ILE   B CG1   1 
ATOM   12011 C  CG2   . ILE   B  1  405  ? -23.543 12.109  99.812  1.00 25.87 ? 403  ILE   B CG2   1 
ATOM   12012 C  CD1   . ILE   B  1  405  ? -23.616 15.202  100.291 1.00 35.67 ? 403  ILE   B CD1   1 
ATOM   12013 N  N     . ALA   B  1  406  ? -20.492 11.037  97.909  1.00 23.05 ? 404  ALA   B N     1 
ATOM   12014 C  CA    . ALA   B  1  406  ? -20.296 9.810   97.141  1.00 25.47 ? 404  ALA   B CA    1 
ATOM   12015 C  C     . ALA   B  1  406  ? -19.220 8.938   97.763  1.00 22.93 ? 404  ALA   B C     1 
ATOM   12016 O  O     . ALA   B  1  406  ? -19.348 7.709   97.819  1.00 25.65 ? 404  ALA   B O     1 
ATOM   12017 C  CB    . ALA   B  1  406  ? -19.908 10.160  95.706  1.00 23.00 ? 404  ALA   B CB    1 
ATOM   12018 N  N     . CYS   B  1  407  ? -18.137 9.561   98.226  1.00 21.40 ? 405  CYS   B N     1 
ATOM   12019 C  CA    . CYS   B  1  407  ? -17.063 8.806   98.854  1.00 24.04 ? 405  CYS   B CA    1 
ATOM   12020 C  C     . CYS   B  1  407  ? -17.476 8.287   100.223 1.00 20.55 ? 405  CYS   B C     1 
ATOM   12021 O  O     . CYS   B  1  407  ? -17.065 7.191   100.614 1.00 24.64 ? 405  CYS   B O     1 
ATOM   12022 C  CB    . CYS   B  1  407  ? -15.803 9.660   98.911  1.00 20.85 ? 405  CYS   B CB    1 
ATOM   12023 S  SG    . CYS   B  1  407  ? -15.070 9.909   97.258  1.00 26.09 ? 405  CYS   B SG    1 
ATOM   12024 N  N     . ALA   B  1  408  ? -18.308 9.045   100.946 1.00 23.06 ? 406  ALA   B N     1 
ATOM   12025 C  CA    . ALA   B  1  408  ? -18.889 8.539   102.185 1.00 25.12 ? 406  ALA   B CA    1 
ATOM   12026 C  C     . ALA   B  1  408  ? -19.741 7.307   101.924 1.00 22.90 ? 406  ALA   B C     1 
ATOM   12027 O  O     . ALA   B  1  408  ? -19.711 6.349   102.699 1.00 27.77 ? 406  ALA   B O     1 
ATOM   12028 C  CB    . ALA   B  1  408  ? -19.726 9.629   102.848 1.00 27.35 ? 406  ALA   B CB    1 
ATOM   12029 N  N     . ALA   B  1  409  ? -20.489 7.304   100.815 1.00 25.73 ? 407  ALA   B N     1 
ATOM   12030 C  CA    . ALA   B  1  409  ? -21.290 6.132   100.488 1.00 28.25 ? 407  ALA   B CA    1 
ATOM   12031 C  C     . ALA   B  1  409  ? -20.402 4.919   100.264 1.00 24.97 ? 407  ALA   B C     1 
ATOM   12032 O  O     . ALA   B  1  409  ? -20.714 3.818   100.731 1.00 30.33 ? 407  ALA   B O     1 
ATOM   12033 C  CB    . ALA   B  1  409  ? -22.162 6.411   99.265  1.00 25.65 ? 407  ALA   B CB    1 
ATOM   12034 N  N     . LYS   B  1  410  ? -19.272 5.114   99.581  1.00 25.84 ? 408  LYS   B N     1 
ATOM   12035 C  CA    . LYS   B  1  410  ? -18.320 4.027   99.393  1.00 23.96 ? 408  LYS   B CA    1 
ATOM   12036 C  C     . LYS   B  1  410  ? -17.745 3.573   100.726 1.00 28.08 ? 408  LYS   B C     1 
ATOM   12037 O  O     . LYS   B  1  410  ? -17.629 2.369   100.988 1.00 29.25 ? 408  LYS   B O     1 
ATOM   12038 C  CB    . LYS   B  1  410  ? -17.196 4.480   98.461  1.00 25.30 ? 408  LYS   B CB    1 
ATOM   12039 C  CG    . LYS   B  1  410  ? -16.203 3.382   98.101  1.00 27.10 ? 408  LYS   B CG    1 
ATOM   12040 C  CD    . LYS   B  1  410  ? -15.012 3.918   97.320  1.00 28.62 ? 408  LYS   B CD    1 
ATOM   12041 C  CE    . LYS   B  1  410  ? -15.385 4.398   95.921  1.00 28.78 ? 408  LYS   B CE    1 
ATOM   12042 N  NZ    . LYS   B  1  410  ? -15.700 3.266   94.989  1.00 29.96 ? 408  LYS   B NZ    1 
ATOM   12043 N  N     . LEU   B  1  411  ? -17.376 4.527   101.583 1.00 27.14 ? 409  LEU   B N     1 
ATOM   12044 C  CA    . LEU   B  1  411  ? -16.813 4.168   102.879 1.00 28.68 ? 409  LEU   B CA    1 
ATOM   12045 C  C     . LEU   B  1  411  ? -17.840 3.476   103.762 1.00 28.84 ? 409  LEU   B C     1 
ATOM   12046 O  O     . LEU   B  1  411  ? -17.518 2.486   104.421 1.00 27.62 ? 409  LEU   B O     1 
ATOM   12047 C  CB    . LEU   B  1  411  ? -16.248 5.404   103.569 1.00 25.37 ? 409  LEU   B CB    1 
ATOM   12048 C  CG    . LEU   B  1  411  ? -14.899 5.869   103.028 1.00 26.30 ? 409  LEU   B CG    1 
ATOM   12049 C  CD1   . LEU   B  1  411  ? -14.580 7.266   103.522 1.00 25.72 ? 409  LEU   B CD1   1 
ATOM   12050 C  CD2   . LEU   B  1  411  ? -13.804 4.898   103.427 1.00 25.33 ? 409  LEU   B CD2   1 
ATOM   12051 N  N     . LEU   B  1  412  ? -19.075 3.988   103.793 1.00 28.68 ? 410  LEU   B N     1 
ATOM   12052 C  CA    . LEU   B  1  412  ? -20.094 3.395   104.653 1.00 26.23 ? 410  LEU   B CA    1 
ATOM   12053 C  C     . LEU   B  1  412  ? -20.457 1.989   104.202 1.00 27.72 ? 410  LEU   B C     1 
ATOM   12054 O  O     . LEU   B  1  412  ? -20.893 1.173   105.018 1.00 32.18 ? 410  LEU   B O     1 
ATOM   12055 C  CB    . LEU   B  1  412  ? -21.333 4.288   104.711 1.00 32.02 ? 410  LEU   B CB    1 
ATOM   12056 C  CG    . LEU   B  1  412  ? -21.173 5.564   105.542 1.00 30.06 ? 410  LEU   B CG    1 
ATOM   12057 C  CD1   . LEU   B  1  412  ? -22.335 6.505   105.314 1.00 36.88 ? 410  LEU   B CD1   1 
ATOM   12058 C  CD2   . LEU   B  1  412  ? -21.040 5.225   107.019 1.00 33.56 ? 410  LEU   B CD2   1 
ATOM   12059 N  N     . ALA   B  1  413  ? -20.284 1.688   102.917 1.00 30.08 ? 411  ALA   B N     1 
ATOM   12060 C  CA    . ALA   B  1  413  ? -20.473 0.329   102.433 1.00 32.42 ? 411  ALA   B CA    1 
ATOM   12061 C  C     . ALA   B  1  413  ? -19.280 -0.563  102.730 1.00 33.00 ? 411  ALA   B C     1 
ATOM   12062 O  O     . ALA   B  1  413  ? -19.335 -1.764  102.448 1.00 34.05 ? 411  ALA   B O     1 
ATOM   12063 C  CB    . ALA   B  1  413  ? -20.750 0.336   100.929 1.00 31.78 ? 411  ALA   B CB    1 
ATOM   12064 N  N     . ALA   B  1  414  ? -18.207 -0.013  103.302 1.00 28.36 ? 412  ALA   B N     1 
ATOM   12065 C  CA    . ALA   B  1  414  ? -17.007 -0.788  103.582 1.00 25.67 ? 412  ALA   B CA    1 
ATOM   12066 C  C     . ALA   B  1  414  ? -16.599 -0.717  105.053 1.00 31.22 ? 412  ALA   B C     1 
ATOM   12067 O  O     . ALA   B  1  414  ? -15.425 -0.928  105.370 1.00 30.79 ? 412  ALA   B O     1 
ATOM   12068 C  CB    . ALA   B  1  414  ? -15.849 -0.348  102.681 1.00 31.10 ? 412  ALA   B CB    1 
ATOM   12069 N  N     . THR   B  1  415  ? -17.542 -0.434  105.964 1.00 29.40 ? 413  THR   B N     1 
ATOM   12070 C  CA    . THR   B  1  415  ? -17.181 -0.290  107.375 1.00 29.06 ? 413  THR   B CA    1 
ATOM   12071 C  C     . THR   B  1  415  ? -16.662 -1.587  107.973 1.00 29.41 ? 413  THR   B C     1 
ATOM   12072 O  O     . THR   B  1  415  ? -16.012 -1.557  109.027 1.00 30.39 ? 413  THR   B O     1 
ATOM   12073 C  CB    . THR   B  1  415  ? -18.354 0.227   108.209 1.00 28.92 ? 413  THR   B CB    1 
ATOM   12074 O  OG1   . THR   B  1  415  ? -19.408 -0.743  108.200 1.00 33.15 ? 413  THR   B OG1   1 
ATOM   12075 C  CG2   . THR   B  1  415  ? -18.874 1.546   107.661 1.00 31.85 ? 413  THR   B CG2   1 
ATOM   12076 N  N     . ASP   B  1  416  ? -16.936 -2.724  107.336 1.00 32.97 ? 414  ASP   B N     1 
ATOM   12077 C  CA    . ASP   B  1  416  ? -16.337 -3.978  107.768 1.00 32.07 ? 414  ASP   B CA    1 
ATOM   12078 C  C     . ASP   B  1  416  ? -14.859 -4.060  107.422 1.00 29.57 ? 414  ASP   B C     1 
ATOM   12079 O  O     . ASP   B  1  416  ? -14.176 -4.968  107.903 1.00 35.67 ? 414  ASP   B O     1 
ATOM   12080 C  CB    . ASP   B  1  416  ? -17.089 -5.154  107.136 1.00 28.88 ? 414  ASP   B CB    1 
ATOM   12081 N  N     . VAL   B  1  417  ? -14.344 -3.126  106.623 1.00 30.23 ? 415  VAL   B N     1 
ATOM   12082 C  CA    . VAL   B  1  417  ? -13.016 -3.244  106.029 1.00 26.45 ? 415  VAL   B CA    1 
ATOM   12083 C  C     . VAL   B  1  417  ? -12.145 -2.055  106.417 1.00 28.24 ? 415  VAL   B C     1 
ATOM   12084 O  O     . VAL   B  1  417  ? -10.927 -2.178  106.566 1.00 26.84 ? 415  VAL   B O     1 
ATOM   12085 C  CB    . VAL   B  1  417  ? -13.152 -3.359  104.498 1.00 31.90 ? 415  VAL   B CB    1 
ATOM   12086 C  CG1   . VAL   B  1  417  ? -11.797 -3.424  103.841 1.00 25.94 ? 415  VAL   B CG1   1 
ATOM   12087 C  CG2   . VAL   B  1  417  ? -13.990 -4.586  104.135 1.00 31.15 ? 415  VAL   B CG2   1 
ATOM   12088 N  N     . VAL   B  1  418  ? -12.756 -0.884  106.539 1.00 26.11 ? 416  VAL   B N     1 
ATOM   12089 C  CA    . VAL   B  1  418  ? -12.046 0.322   106.929 1.00 25.26 ? 416  VAL   B CA    1 
ATOM   12090 C  C     . VAL   B  1  418  ? -12.885 1.000   107.994 1.00 27.44 ? 416  VAL   B C     1 
ATOM   12091 O  O     . VAL   B  1  418  ? -14.067 0.700   108.172 1.00 25.75 ? 416  VAL   B O     1 
ATOM   12092 C  CB    . VAL   B  1  418  ? -11.797 1.280   105.744 1.00 25.18 ? 416  VAL   B CB    1 
ATOM   12093 C  CG1   . VAL   B  1  418  ? -10.796 0.672   104.770 1.00 23.18 ? 416  VAL   B CG1   1 
ATOM   12094 C  CG2   . VAL   B  1  418  ? -13.118 1.605   105.032 1.00 25.73 ? 416  VAL   B CG2   1 
ATOM   12095 N  N     . PHE   B  1  419  ? -12.250 1.911   108.718 1.00 24.05 ? 417  PHE   B N     1 
ATOM   12096 C  CA    . PHE   B  1  419  ? -12.946 2.673   109.744 1.00 24.06 ? 417  PHE   B CA    1 
ATOM   12097 C  C     . PHE   B  1  419  ? -13.129 4.082   109.203 1.00 22.99 ? 417  PHE   B C     1 
ATOM   12098 O  O     . PHE   B  1  419  ? -12.173 4.877   109.200 1.00 22.20 ? 417  PHE   B O     1 
ATOM   12099 C  CB    . PHE   B  1  419  ? -12.123 2.687   111.034 1.00 25.80 ? 417  PHE   B CB    1 
ATOM   12100 C  CG    . PHE   B  1  419  ? -12.719 3.518   112.114 1.00 25.65 ? 417  PHE   B CG    1 
ATOM   12101 C  CD1   . PHE   B  1  419  ? -13.998 3.271   112.579 1.00 26.52 ? 417  PHE   B CD1   1 
ATOM   12102 C  CD2   . PHE   B  1  419  ? -11.997 4.551   112.671 1.00 26.06 ? 417  PHE   B CD2   1 
ATOM   12103 C  CE1   . PHE   B  1  419  ? -14.541 4.050   113.589 1.00 27.34 ? 417  PHE   B CE1   1 
ATOM   12104 C  CE2   . PHE   B  1  419  ? -12.531 5.329   113.671 1.00 25.00 ? 417  PHE   B CE2   1 
ATOM   12105 C  CZ    . PHE   B  1  419  ? -13.801 5.085   114.129 1.00 24.55 ? 417  PHE   B CZ    1 
ATOM   12106 N  N     . PRO   B  1  420  ? -14.308 4.432   108.697 1.00 23.29 ? 418  PRO   B N     1 
ATOM   12107 C  CA    . PRO   B  1  420  ? -14.479 5.755   108.096 1.00 20.83 ? 418  PRO   B CA    1 
ATOM   12108 C  C     . PRO   B  1  420  ? -14.557 6.837   109.157 1.00 22.46 ? 418  PRO   B C     1 
ATOM   12109 O  O     . PRO   B  1  420  ? -15.213 6.681   110.187 1.00 22.61 ? 418  PRO   B O     1 
ATOM   12110 C  CB    . PRO   B  1  420  ? -15.806 5.629   107.333 1.00 24.38 ? 418  PRO   B CB    1 
ATOM   12111 C  CG    . PRO   B  1  420  ? -16.048 4.160   107.213 1.00 24.52 ? 418  PRO   B CG    1 
ATOM   12112 C  CD    . PRO   B  1  420  ? -15.492 3.587   108.484 1.00 22.83 ? 418  PRO   B CD    1 
ATOM   12113 N  N     . GLN   B  1  421  ? -13.866 7.940   108.897 1.00 22.38 ? 419  GLN   B N     1 
ATOM   12114 C  CA    . GLN   B  1  421  ? -13.817 9.075   109.811 1.00 23.46 ? 419  GLN   B CA    1 
ATOM   12115 C  C     . GLN   B  1  421  ? -14.210 10.302  109.003 1.00 21.60 ? 419  GLN   B C     1 
ATOM   12116 O  O     . GLN   B  1  421  ? -13.444 10.772  108.156 1.00 20.24 ? 419  GLN   B O     1 
ATOM   12117 C  CB    . GLN   B  1  421  ? -12.420 9.219   110.410 1.00 21.11 ? 419  GLN   B CB    1 
ATOM   12118 C  CG    . GLN   B  1  421  ? -11.968 7.953   111.098 1.00 21.38 ? 419  GLN   B CG    1 
ATOM   12119 C  CD    . GLN   B  1  421  ? -10.469 7.913   111.304 1.00 21.27 ? 419  GLN   B CD    1 
ATOM   12120 O  OE1   . GLN   B  1  421  ? -9.705  7.973   110.358 1.00 22.30 ? 419  GLN   B OE1   1 
ATOM   12121 N  NE2   . GLN   B  1  421  ? -10.048 7.804   112.554 1.00 20.61 ? 419  GLN   B NE2   1 
ATOM   12122 N  N     . PHE   B  1  422  ? -15.415 10.807  109.244 1.00 22.48 ? 420  PHE   B N     1 
ATOM   12123 C  CA    . PHE   B  1  422  ? -15.974 11.859  108.404 1.00 19.96 ? 420  PHE   B CA    1 
ATOM   12124 C  C     . PHE   B  1  422  ? -15.676 13.208  109.040 1.00 20.36 ? 420  PHE   B C     1 
ATOM   12125 O  O     . PHE   B  1  422  ? -16.404 13.697  109.910 1.00 22.29 ? 420  PHE   B O     1 
ATOM   12126 C  CB    . PHE   B  1  422  ? -17.461 11.607  108.179 1.00 22.62 ? 420  PHE   B CB    1 
ATOM   12127 C  CG    . PHE   B  1  422  ? -17.744 10.277  107.527 1.00 25.01 ? 420  PHE   B CG    1 
ATOM   12128 C  CD1   . PHE   B  1  422  ? -17.363 10.040  106.218 1.00 25.73 ? 420  PHE   B CD1   1 
ATOM   12129 C  CD2   . PHE   B  1  422  ? -18.385 9.265   108.223 1.00 25.32 ? 420  PHE   B CD2   1 
ATOM   12130 C  CE1   . PHE   B  1  422  ? -17.617 8.822   105.614 1.00 27.12 ? 420  PHE   B CE1   1 
ATOM   12131 C  CE2   . PHE   B  1  422  ? -18.639 8.043   107.618 1.00 27.99 ? 420  PHE   B CE2   1 
ATOM   12132 C  CZ    . PHE   B  1  422  ? -18.257 7.829   106.313 1.00 26.82 ? 420  PHE   B CZ    1 
ATOM   12133 N  N     . ALA   B  1  423  ? -14.574 13.808  108.595 1.00 20.07 ? 421  ALA   B N     1 
ATOM   12134 C  CA    . ALA   B  1  423  ? -14.152 15.117  109.067 1.00 21.38 ? 421  ALA   B CA    1 
ATOM   12135 C  C     . ALA   B  1  423  ? -14.904 16.178  108.280 1.00 20.86 ? 421  ALA   B C     1 
ATOM   12136 O  O     . ALA   B  1  423  ? -14.678 16.342  107.076 1.00 23.96 ? 421  ALA   B O     1 
ATOM   12137 C  CB    . ALA   B  1  423  ? -12.649 15.276  108.848 1.00 19.54 ? 421  ALA   B CB    1 
ATOM   12138 N  N     . THR   B  1  424  ? -15.779 16.922  108.953 1.00 24.79 ? 422  THR   B N     1 
ATOM   12139 C  CA    . THR   B  1  424  ? -16.481 18.022  108.306 1.00 22.06 ? 422  THR   B CA    1 
ATOM   12140 C  C     . THR   B  1  424  ? -17.119 18.892  109.379 1.00 21.94 ? 422  THR   B C     1 
ATOM   12141 O  O     . THR   B  1  424  ? -17.533 18.402  110.431 1.00 24.56 ? 422  THR   B O     1 
ATOM   12142 C  CB    . THR   B  1  424  ? -17.559 17.520  107.332 1.00 25.85 ? 422  THR   B CB    1 
ATOM   12143 O  OG1   . THR   B  1  424  ? -18.178 18.640  106.690 1.00 24.44 ? 422  THR   B OG1   1 
ATOM   12144 C  CG2   . THR   B  1  424  ? -18.627 16.708  108.073 1.00 25.68 ? 422  THR   B CG2   1 
ATOM   12145 N  N     . HIS   B  1  425  ? -17.166 20.190  109.109 1.00 23.20 ? 423  HIS   B N     1 
ATOM   12146 C  CA    . HIS   B  1  425  ? -17.898 21.126  109.949 1.00 23.92 ? 423  HIS   B CA    1 
ATOM   12147 C  C     . HIS   B  1  425  ? -19.233 21.512  109.340 1.00 26.05 ? 423  HIS   B C     1 
ATOM   12148 O  O     . HIS   B  1  425  ? -19.931 22.369  109.891 1.00 27.55 ? 423  HIS   B O     1 
ATOM   12149 C  CB    . HIS   B  1  425  ? -17.062 22.383  110.180 1.00 24.51 ? 423  HIS   B CB    1 
ATOM   12150 C  CG    . HIS   B  1  425  ? -15.793 22.127  110.928 1.00 23.22 ? 423  HIS   B CG    1 
ATOM   12151 N  ND1   . HIS   B  1  425  ? -14.587 22.674  110.551 1.00 26.10 ? 423  HIS   B ND1   1 
ATOM   12152 C  CD2   . HIS   B  1  425  ? -15.542 21.371  112.022 1.00 24.93 ? 423  HIS   B CD2   1 
ATOM   12153 C  CE1   . HIS   B  1  425  ? -13.647 22.276  111.391 1.00 25.33 ? 423  HIS   B CE1   1 
ATOM   12154 N  NE2   . HIS   B  1  425  ? -14.199 21.481  112.288 1.00 23.83 ? 423  HIS   B NE2   1 
ATOM   12155 N  N     . ASN   B  1  426  ? -19.593 20.905  108.212 1.00 26.19 ? 424  ASN   B N     1 
ATOM   12156 C  CA    . ASN   B  1  426  ? -20.788 21.265  107.462 1.00 25.98 ? 424  ASN   B CA    1 
ATOM   12157 C  C     . ASN   B  1  426  ? -21.945 20.403  107.954 1.00 27.59 ? 424  ASN   B C     1 
ATOM   12158 O  O     . ASN   B  1  426  ? -21.940 19.180  107.777 1.00 26.00 ? 424  ASN   B O     1 
ATOM   12159 C  CB    . ASN   B  1  426  ? -20.523 21.037  105.977 1.00 25.65 ? 424  ASN   B CB    1 
ATOM   12160 C  CG    . ASN   B  1  426  ? -21.595 21.627  105.099 1.00 27.11 ? 424  ASN   B CG    1 
ATOM   12161 O  OD1   . ASN   B  1  426  ? -22.788 21.455  105.357 1.00 28.56 ? 424  ASN   B OD1   1 
ATOM   12162 N  ND2   . ASN   B  1  426  ? -21.181 22.328  104.051 1.00 28.09 ? 424  ASN   B ND2   1 
ATOM   12163 N  N     . ALA   B  1  427  ? -22.936 21.044  108.583 1.00 29.40 ? 425  ALA   B N     1 
ATOM   12164 C  CA    . ALA   B  1  427  ? -24.064 20.308  109.141 1.00 30.36 ? 425  ALA   B CA    1 
ATOM   12165 C  C     . ALA   B  1  427  ? -24.877 19.609  108.060 1.00 25.57 ? 425  ALA   B C     1 
ATOM   12166 O  O     . ALA   B  1  427  ? -25.479 18.559  108.319 1.00 28.56 ? 425  ALA   B O     1 
ATOM   12167 C  CB    . ALA   B  1  427  ? -24.956 21.247  109.956 1.00 32.45 ? 425  ALA   B CB    1 
ATOM   12168 N  N     . GLN   B  1  428  ? -24.900 20.160  106.845 1.00 27.14 ? 426  GLN   B N     1 
ATOM   12169 C  CA    . GLN   B  1  428  ? -25.586 19.468  105.762 1.00 30.20 ? 426  GLN   B CA    1 
ATOM   12170 C  C     . GLN   B  1  428  ? -24.848 18.191  105.382 1.00 28.59 ? 426  GLN   B C     1 
ATOM   12171 O  O     . GLN   B  1  428  ? -25.457 17.123  105.258 1.00 27.48 ? 426  GLN   B O     1 
ATOM   12172 C  CB    . GLN   B  1  428  ? -25.774 20.392  104.561 1.00 29.04 ? 426  GLN   B CB    1 
ATOM   12173 C  CG    . GLN   B  1  428  ? -26.824 19.893  103.569 1.00 30.54 ? 426  GLN   B CG    1 
ATOM   12174 C  CD    . GLN   B  1  428  ? -26.313 18.772  102.679 1.00 30.23 ? 426  GLN   B CD    1 
ATOM   12175 O  OE1   . GLN   B  1  428  ? -25.135 18.738  102.324 1.00 31.48 ? 426  GLN   B OE1   1 
ATOM   12176 N  NE2   . GLN   B  1  428  ? -27.193 17.843  102.325 1.00 32.37 ? 426  GLN   B NE2   1 
ATOM   12177 N  N     . THR   B  1  429  ? -23.526 18.280  105.204 1.00 28.26 ? 427  THR   B N     1 
ATOM   12178 C  CA    . THR   B  1  429  ? -22.735 17.092  104.901 1.00 30.17 ? 427  THR   B CA    1 
ATOM   12179 C  C     . THR   B  1  429  ? -22.894 16.043  105.991 1.00 25.86 ? 427  THR   B C     1 
ATOM   12180 O  O     . THR   B  1  429  ? -23.116 14.857  105.708 1.00 26.56 ? 427  THR   B O     1 
ATOM   12181 C  CB    . THR   B  1  429  ? -21.264 17.483  104.781 1.00 24.61 ? 427  THR   B CB    1 
ATOM   12182 O  OG1   . THR   B  1  429  ? -21.135 18.616  103.918 1.00 25.35 ? 427  THR   B OG1   1 
ATOM   12183 C  CG2   . THR   B  1  429  ? -20.455 16.328  104.237 1.00 29.60 ? 427  THR   B CG2   1 
ATOM   12184 N  N     . LEU   B  1  430  ? -22.777 16.471  107.252 1.00 28.47 ? 428  LEU   B N     1 
ATOM   12185 C  CA    . LEU   B  1  430  ? -22.913 15.561  108.383 1.00 26.22 ? 428  LEU   B CA    1 
ATOM   12186 C  C     . LEU   B  1  430  ? -24.272 14.873  108.366 1.00 27.44 ? 428  LEU   B C     1 
ATOM   12187 O  O     . LEU   B  1  430  ? -24.359 13.646  108.482 1.00 27.88 ? 428  LEU   B O     1 
ATOM   12188 C  CB    . LEU   B  1  430  ? -22.731 16.345  109.684 1.00 30.58 ? 428  LEU   B CB    1 
ATOM   12189 C  CG    . LEU   B  1  430  ? -22.574 15.658  111.048 1.00 32.39 ? 428  LEU   B CG    1 
ATOM   12190 C  CD1   . LEU   B  1  430  ? -22.206 16.713  112.056 1.00 30.50 ? 428  LEU   B CD1   1 
ATOM   12191 C  CD2   . LEU   B  1  430  ? -23.819 14.922  111.519 1.00 34.99 ? 428  LEU   B CD2   1 
ATOM   12192 N  N     . ALA   B  1  431  ? -25.346 15.657  108.229 1.00 32.81 ? 429  ALA   B N     1 
ATOM   12193 C  CA    . ALA   B  1  431  ? -26.692 15.091  108.257 1.00 31.50 ? 429  ALA   B CA    1 
ATOM   12194 C  C     . ALA   B  1  431  ? -26.883 14.069  107.144 1.00 31.81 ? 429  ALA   B C     1 
ATOM   12195 O  O     . ALA   B  1  431  ? -27.501 13.019  107.358 1.00 33.68 ? 429  ALA   B O     1 
ATOM   12196 C  CB    . ALA   B  1  431  ? -27.733 16.204  108.155 1.00 33.03 ? 429  ALA   B CB    1 
ATOM   12197 N  N     . ALA   B  1  432  ? -26.336 14.349  105.955 1.00 31.49 ? 430  ALA   B N     1 
ATOM   12198 C  CA    . ALA   B  1  432  ? -26.455 13.404  104.848 1.00 28.62 ? 430  ALA   B CA    1 
ATOM   12199 C  C     . ALA   B  1  432  ? -25.795 12.076  105.191 1.00 30.93 ? 430  ALA   B C     1 
ATOM   12200 O  O     . ALA   B  1  432  ? -26.358 11.009  104.931 1.00 32.46 ? 430  ALA   B O     1 
ATOM   12201 C  CB    . ALA   B  1  432  ? -25.845 13.996  103.576 1.00 30.52 ? 430  ALA   B CB    1 
ATOM   12202 N  N     . ILE   B  1  433  ? -24.603 12.122  105.788 1.00 31.12 ? 431  ILE   B N     1 
ATOM   12203 C  CA    . ILE   B  1  433  ? -23.899 10.887  106.120 1.00 32.61 ? 431  ILE   B CA    1 
ATOM   12204 C  C     . ILE   B  1  433  ? -24.551 10.188  107.305 1.00 27.08 ? 431  ILE   B C     1 
ATOM   12205 O  O     . ILE   B  1  433  ? -24.638 8.955   107.343 1.00 29.01 ? 431  ILE   B O     1 
ATOM   12206 C  CB    . ILE   B  1  433  ? -22.414 11.184  106.372 1.00 28.74 ? 431  ILE   B CB    1 
ATOM   12207 C  CG1   . ILE   B  1  433  ? -21.771 11.683  105.084 1.00 34.43 ? 431  ILE   B CG1   1 
ATOM   12208 C  CG2   . ILE   B  1  433  ? -21.697 9.950   106.916 1.00 33.49 ? 431  ILE   B CG2   1 
ATOM   12209 C  CD1   . ILE   B  1  433  ? -20.379 12.115  105.281 1.00 35.34 ? 431  ILE   B CD1   1 
ATOM   12210 N  N     . TYR   B  1  434  ? -24.977 10.960  108.306 1.00 30.92 ? 432  TYR   B N     1 
ATOM   12211 C  CA    . TYR   B  1  434  ? -25.656 10.388  109.463 1.00 28.59 ? 432  TYR   B CA    1 
ATOM   12212 C  C     . TYR   B  1  434  ? -26.839 9.530   109.035 1.00 31.13 ? 432  TYR   B C     1 
ATOM   12213 O  O     . TYR   B  1  434  ? -27.006 8.402   109.512 1.00 31.54 ? 432  TYR   B O     1 
ATOM   12214 C  CB    . TYR   B  1  434  ? -26.085 11.530  110.384 1.00 33.71 ? 432  TYR   B CB    1 
ATOM   12215 C  CG    . TYR   B  1  434  ? -27.014 11.143  111.502 1.00 31.65 ? 432  TYR   B CG    1 
ATOM   12216 C  CD1   . TYR   B  1  434  ? -26.549 10.448  112.613 1.00 33.94 ? 432  TYR   B CD1   1 
ATOM   12217 C  CD2   . TYR   B  1  434  ? -28.357 11.495  111.461 1.00 33.62 ? 432  TYR   B CD2   1 
ATOM   12218 C  CE1   . TYR   B  1  434  ? -27.399 10.110  113.649 1.00 37.02 ? 432  TYR   B CE1   1 
ATOM   12219 C  CE2   . TYR   B  1  434  ? -29.210 11.164  112.490 1.00 34.27 ? 432  TYR   B CE2   1 
ATOM   12220 C  CZ    . TYR   B  1  434  ? -28.729 10.468  113.577 1.00 36.93 ? 432  TYR   B CZ    1 
ATOM   12221 O  OH    . TYR   B  1  434  ? -29.588 10.137  114.594 1.00 37.19 ? 432  TYR   B OH    1 
ATOM   12222 N  N     . HIS   B  1  435  ? -27.634 10.020  108.087 1.00 34.30 ? 433  HIS   B N     1 
ATOM   12223 C  CA    . HIS   B  1  435  ? -28.774 9.240   107.626 1.00 36.49 ? 433  HIS   B CA    1 
ATOM   12224 C  C     . HIS   B  1  435  ? -28.367 8.190   106.604 1.00 32.73 ? 433  HIS   B C     1 
ATOM   12225 O  O     . HIS   B  1  435  ? -28.902 7.076   106.612 1.00 34.68 ? 433  HIS   B O     1 
ATOM   12226 C  CB    . HIS   B  1  435  ? -29.865 10.163  107.101 1.00 38.87 ? 433  HIS   B CB    1 
ATOM   12227 C  CG    . HIS   B  1  435  ? -30.572 10.899  108.189 1.00 36.14 ? 433  HIS   B CG    1 
ATOM   12228 N  ND1   . HIS   B  1  435  ? -31.546 10.312  108.966 1.00 35.73 ? 433  HIS   B ND1   1 
ATOM   12229 C  CD2   . HIS   B  1  435  ? -30.423 12.159  108.658 1.00 35.08 ? 433  HIS   B CD2   1 
ATOM   12230 C  CE1   . HIS   B  1  435  ? -31.980 11.185  109.856 1.00 42.27 ? 433  HIS   B CE1   1 
ATOM   12231 N  NE2   . HIS   B  1  435  ? -31.316 12.314  109.690 1.00 33.01 ? 433  HIS   B NE2   1 
ATOM   12232 N  N     . MET   B  1  436  ? -27.406 8.516   105.734 1.00 32.19 ? 434  MET   B N     1 
ATOM   12233 C  CA    . MET   B  1  436  ? -26.897 7.509   104.815 1.00 32.49 ? 434  MET   B CA    1 
ATOM   12234 C  C     . MET   B  1  436  ? -26.393 6.281   105.556 1.00 29.87 ? 434  MET   B C     1 
ATOM   12235 O  O     . MET   B  1  436  ? -26.509 5.159   105.051 1.00 35.35 ? 434  MET   B O     1 
ATOM   12236 C  CB    . MET   B  1  436  ? -25.776 8.106   103.975 1.00 32.38 ? 434  MET   B CB    1 
ATOM   12237 C  CG    . MET   B  1  436  ? -25.104 7.108   103.076 1.00 33.51 ? 434  MET   B CG    1 
ATOM   12238 S  SD    . MET   B  1  436  ? -23.679 7.885   102.314 1.00 37.96 ? 434  MET   B SD    1 
ATOM   12239 C  CE    . MET   B  1  436  ? -24.504 9.022   101.215 1.00 32.74 ? 434  MET   B CE    1 
ATOM   12240 N  N     . ALA   B  1  437  ? -25.833 6.469   106.757 1.00 30.39 ? 435  ALA   B N     1 
ATOM   12241 C  CA    . ALA   B  1  437  ? -25.298 5.348   107.521 1.00 33.17 ? 435  ALA   B CA    1 
ATOM   12242 C  C     . ALA   B  1  437  ? -26.390 4.462   108.103 1.00 37.54 ? 435  ALA   B C     1 
ATOM   12243 O  O     . ALA   B  1  437  ? -26.098 3.336   108.522 1.00 37.16 ? 435  ALA   B O     1 
ATOM   12244 C  CB    . ALA   B  1  437  ? -24.401 5.861   108.646 1.00 35.36 ? 435  ALA   B CB    1 
ATOM   12245 N  N     . GLY   B  1  438  ? -27.625 4.941   108.148 1.00 38.53 ? 436  GLY   B N     1 
ATOM   12246 C  CA    . GLY   B  1  438  ? -28.721 4.133   108.630 1.00 35.06 ? 436  GLY   B CA    1 
ATOM   12247 C  C     . GLY   B  1  438  ? -28.825 4.123   110.143 1.00 44.23 ? 436  GLY   B C     1 
ATOM   12248 O  O     . GLY   B  1  438  ? -28.109 4.824   110.870 1.00 42.00 ? 436  GLY   B O     1 
ATOM   12249 N  N     . LYS   B  1  439  ? -29.742 3.280   110.619 1.00 40.08 ? 437  LYS   B N     1 
ATOM   12250 C  CA    . LYS   B  1  439  ? -30.077 3.240   112.036 1.00 39.80 ? 437  LYS   B CA    1 
ATOM   12251 C  C     . LYS   B  1  439  ? -29.079 2.432   112.857 1.00 41.18 ? 437  LYS   B C     1 
ATOM   12252 O  O     . LYS   B  1  439  ? -28.964 2.654   114.068 1.00 48.35 ? 437  LYS   B O     1 
ATOM   12253 C  CB    . LYS   B  1  439  ? -31.482 2.661   112.221 1.00 40.12 ? 437  LYS   B CB    1 
ATOM   12254 N  N     . ASP   B  1  440  ? -28.364 1.495   112.238 1.00 37.17 ? 438  ASP   B N     1 
ATOM   12255 C  CA    . ASP   B  1  440  ? -27.489 0.599   112.984 1.00 41.70 ? 438  ASP   B CA    1 
ATOM   12256 C  C     . ASP   B  1  440  ? -26.157 1.295   113.228 1.00 42.06 ? 438  ASP   B C     1 
ATOM   12257 O  O     . ASP   B  1  440  ? -25.493 1.723   112.278 1.00 44.70 ? 438  ASP   B O     1 
ATOM   12258 C  CB    . ASP   B  1  440  ? -27.272 -0.694  112.202 1.00 41.22 ? 438  ASP   B CB    1 
ATOM   12259 N  N     . PHE   B  1  441  ? -25.768 1.418   114.495 1.00 37.48 ? 439  PHE   B N     1 
ATOM   12260 C  CA    . PHE   B  1  441  ? -24.499 2.056   114.808 1.00 34.23 ? 439  PHE   B CA    1 
ATOM   12261 C  C     . PHE   B  1  441  ? -23.911 1.495   116.093 1.00 37.48 ? 439  PHE   B C     1 
ATOM   12262 O  O     . PHE   B  1  441  ? -24.630 1.148   117.035 1.00 36.29 ? 439  PHE   B O     1 
ATOM   12263 C  CB    . PHE   B  1  441  ? -24.604 3.577   114.936 1.00 35.24 ? 439  PHE   B CB    1 
ATOM   12264 C  CG    . PHE   B  1  441  ? -23.282 4.230   115.205 1.00 35.73 ? 439  PHE   B CG    1 
ATOM   12265 C  CD1   . PHE   B  1  441  ? -22.399 4.458   114.169 1.00 32.10 ? 439  PHE   B CD1   1 
ATOM   12266 C  CD2   . PHE   B  1  441  ? -22.897 4.556   116.498 1.00 33.48 ? 439  PHE   B CD2   1 
ATOM   12267 C  CE1   . PHE   B  1  441  ? -21.164 5.029   114.403 1.00 31.50 ? 439  PHE   B CE1   1 
ATOM   12268 C  CE2   . PHE   B  1  441  ? -21.664 5.126   116.739 1.00 32.88 ? 439  PHE   B CE2   1 
ATOM   12269 C  CZ    . PHE   B  1  441  ? -20.797 5.358   115.686 1.00 32.97 ? 439  PHE   B CZ    1 
ATOM   12270 N  N     . HIS   B  1  442  ? -22.585 1.424   116.114 1.00 37.07 ? 440  HIS   B N     1 
ATOM   12271 C  CA    . HIS   B  1  442  ? -21.829 1.154   117.322 1.00 35.18 ? 440  HIS   B CA    1 
ATOM   12272 C  C     . HIS   B  1  442  ? -20.524 1.925   117.218 1.00 32.89 ? 440  HIS   B C     1 
ATOM   12273 O  O     . HIS   B  1  442  ? -20.079 2.277   116.122 1.00 33.45 ? 440  HIS   B O     1 
ATOM   12274 C  CB    . HIS   B  1  442  ? -21.538 -0.339  117.459 1.00 34.89 ? 440  HIS   B CB    1 
ATOM   12275 C  CG    . HIS   B  1  442  ? -20.867 -0.928  116.259 1.00 39.55 ? 440  HIS   B CG    1 
ATOM   12276 N  ND1   . HIS   B  1  442  ? -19.505 -0.855  116.058 1.00 41.15 ? 440  HIS   B ND1   1 
ATOM   12277 C  CD2   . HIS   B  1  442  ? -21.373 -1.581  115.185 1.00 39.83 ? 440  HIS   B CD2   1 
ATOM   12278 C  CE1   . HIS   B  1  442  ? -19.199 -1.449  114.918 1.00 38.85 ? 440  HIS   B CE1   1 
ATOM   12279 N  NE2   . HIS   B  1  442  ? -20.314 -1.900  114.370 1.00 41.81 ? 440  HIS   B NE2   1 
ATOM   12280 N  N     . VAL   B  1  443  ? -19.915 2.195   118.374 1.00 32.51 ? 441  VAL   B N     1 
ATOM   12281 C  CA    . VAL   B  1  443  ? -18.581 2.782   118.368 1.00 34.26 ? 441  VAL   B CA    1 
ATOM   12282 C  C     . VAL   B  1  443  ? -17.623 1.812   117.700 1.00 30.61 ? 441  VAL   B C     1 
ATOM   12283 O  O     . VAL   B  1  443  ? -17.605 0.616   118.009 1.00 31.42 ? 441  VAL   B O     1 
ATOM   12284 C  CB    . VAL   B  1  443  ? -18.134 3.137   119.792 1.00 36.82 ? 441  VAL   B CB    1 
ATOM   12285 C  CG1   . VAL   B  1  443  ? -16.650 3.468   119.800 1.00 34.34 ? 441  VAL   B CG1   1 
ATOM   12286 C  CG2   . VAL   B  1  443  ? -18.942 4.314   120.319 1.00 36.00 ? 441  VAL   B CG2   1 
ATOM   12287 N  N     . GLY   B  1  444  ? -16.832 2.320   116.762 1.00 31.33 ? 442  GLY   B N     1 
ATOM   12288 C  CA    . GLY   B  1  444  ? -15.969 1.489   115.954 1.00 30.02 ? 442  GLY   B CA    1 
ATOM   12289 C  C     . GLY   B  1  444  ? -16.481 1.238   114.552 1.00 31.42 ? 442  GLY   B C     1 
ATOM   12290 O  O     . GLY   B  1  444  ? -15.713 0.759   113.708 1.00 28.28 ? 442  GLY   B O     1 
ATOM   12291 N  N     . LYS   B  1  445  ? -17.751 1.539   114.280 1.00 29.82 ? 443  LYS   B N     1 
ATOM   12292 C  CA    . LYS   B  1  445  ? -18.260 1.403   112.919 1.00 28.39 ? 443  LYS   B CA    1 
ATOM   12293 C  C     . LYS   B  1  445  ? -17.756 2.542   112.041 1.00 30.04 ? 443  LYS   B C     1 
ATOM   12294 O  O     . LYS   B  1  445  ? -17.160 2.309   110.987 1.00 28.95 ? 443  LYS   B O     1 
ATOM   12295 C  CB    . LYS   B  1  445  ? -19.792 1.339   112.923 1.00 28.26 ? 443  LYS   B CB    1 
ATOM   12296 C  CG    . LYS   B  1  445  ? -20.396 1.055   111.553 1.00 30.71 ? 443  LYS   B CG    1 
ATOM   12297 C  CD    . LYS   B  1  445  ? -21.899 0.853   111.636 1.00 37.13 ? 443  LYS   B CD    1 
ATOM   12298 C  CE    . LYS   B  1  445  ? -22.488 0.552   110.270 1.00 41.92 ? 443  LYS   B CE    1 
ATOM   12299 N  NZ    . LYS   B  1  445  ? -23.949 0.271   110.371 1.00 40.40 ? 443  LYS   B NZ    1 
ATOM   12300 N  N     . TYR   B  1  446  ? -17.988 3.777   112.471 1.00 26.17 ? 444  TYR   B N     1 
ATOM   12301 C  CA    . TYR   B  1  446  ? -17.441 4.969   111.842 1.00 26.65 ? 444  TYR   B CA    1 
ATOM   12302 C  C     . TYR   B  1  446  ? -17.497 6.073   112.888 1.00 25.97 ? 444  TYR   B C     1 
ATOM   12303 O  O     . TYR   B  1  446  ? -18.126 5.927   113.937 1.00 25.88 ? 444  TYR   B O     1 
ATOM   12304 C  CB    . TYR   B  1  446  ? -18.216 5.349   110.572 1.00 27.21 ? 444  TYR   B CB    1 
ATOM   12305 C  CG    . TYR   B  1  446  ? -19.637 5.796   110.828 1.00 33.17 ? 444  TYR   B CG    1 
ATOM   12306 C  CD1   . TYR   B  1  446  ? -19.933 7.128   111.104 1.00 27.67 ? 444  TYR   B CD1   1 
ATOM   12307 C  CD2   . TYR   B  1  446  ? -20.685 4.888   110.779 1.00 29.07 ? 444  TYR   B CD2   1 
ATOM   12308 C  CE1   . TYR   B  1  446  ? -21.232 7.533   111.345 1.00 36.96 ? 444  TYR   B CE1   1 
ATOM   12309 C  CE2   . TYR   B  1  446  ? -21.983 5.283   111.016 1.00 34.01 ? 444  TYR   B CE2   1 
ATOM   12310 C  CZ    . TYR   B  1  446  ? -22.251 6.608   111.296 1.00 32.72 ? 444  TYR   B CZ    1 
ATOM   12311 O  OH    . TYR   B  1  446  ? -23.551 7.000   111.533 1.00 41.47 ? 444  TYR   B OH    1 
ATOM   12312 N  N     . GLU   B  1  447  ? -16.833 7.181   112.599 1.00 25.58 ? 445  GLU   B N     1 
ATOM   12313 C  CA    . GLU   B  1  447  ? -16.932 8.333   113.472 1.00 25.87 ? 445  GLU   B CA    1 
ATOM   12314 C  C     . GLU   B  1  447  ? -16.957 9.592   112.632 1.00 22.32 ? 445  GLU   B C     1 
ATOM   12315 O  O     . GLU   B  1  447  ? -16.652 9.585   111.434 1.00 22.58 ? 445  GLU   B O     1 
ATOM   12316 C  CB    . GLU   B  1  447  ? -15.767 8.394   114.460 1.00 23.61 ? 445  GLU   B CB    1 
ATOM   12317 C  CG    . GLU   B  1  447  ? -14.446 8.636   113.777 1.00 20.86 ? 445  GLU   B CG    1 
ATOM   12318 C  CD    . GLU   B  1  447  ? -13.285 8.587   114.745 1.00 21.85 ? 445  GLU   B CD    1 
ATOM   12319 O  OE1   . GLU   B  1  447  ? -13.483 8.176   115.905 1.00 24.32 ? 445  GLU   B OE1   1 
ATOM   12320 O  OE2   . GLU   B  1  447  ? -12.172 8.963   114.318 1.00 22.24 ? 445  GLU   B OE2   1 
ATOM   12321 N  N     . PHE   B  1  448  ? -17.322 10.687  113.270 1.00 24.12 ? 446  PHE   B N     1 
ATOM   12322 C  CA    . PHE   B  1  448  ? -17.106 11.998  112.694 1.00 22.73 ? 446  PHE   B CA    1 
ATOM   12323 C  C     . PHE   B  1  448  ? -15.821 12.574  113.265 1.00 19.66 ? 446  PHE   B C     1 
ATOM   12324 O  O     . PHE   B  1  448  ? -15.273 12.071  114.247 1.00 22.94 ? 446  PHE   B O     1 
ATOM   12325 C  CB    . PHE   B  1  448  ? -18.280 12.917  112.999 1.00 28.32 ? 446  PHE   B CB    1 
ATOM   12326 C  CG    . PHE   B  1  448  ? -19.548 12.485  112.345 1.00 25.31 ? 446  PHE   B CG    1 
ATOM   12327 C  CD1   . PHE   B  1  448  ? -19.804 12.816  111.025 1.00 28.36 ? 446  PHE   B CD1   1 
ATOM   12328 C  CD2   . PHE   B  1  448  ? -20.475 11.726  113.039 1.00 27.58 ? 446  PHE   B CD2   1 
ATOM   12329 C  CE1   . PHE   B  1  448  ? -20.972 12.406  110.412 1.00 26.01 ? 446  PHE   B CE1   1 
ATOM   12330 C  CE2   . PHE   B  1  448  ? -21.645 11.311  112.430 1.00 31.32 ? 446  PHE   B CE2   1 
ATOM   12331 C  CZ    . PHE   B  1  448  ? -21.893 11.654  111.118 1.00 28.64 ? 446  PHE   B CZ    1 
ATOM   12332 N  N     . GLN   B  1  449  ? -15.319 13.612  112.609 1.00 22.48 ? 447  GLN   B N     1 
ATOM   12333 C  CA    . GLN   B  1  449  ? -14.160 14.332  113.112 1.00 20.57 ? 447  GLN   B CA    1 
ATOM   12334 C  C     . GLN   B  1  449  ? -14.378 15.821  112.920 1.00 20.65 ? 447  GLN   B C     1 
ATOM   12335 O  O     . GLN   B  1  449  ? -15.104 16.255  112.019 1.00 21.53 ? 447  GLN   B O     1 
ATOM   12336 C  CB    . GLN   B  1  449  ? -12.851 13.896  112.444 1.00 20.06 ? 447  GLN   B CB    1 
ATOM   12337 C  CG    . GLN   B  1  449  ? -12.555 12.418  112.567 1.00 20.41 ? 447  GLN   B CG    1 
ATOM   12338 C  CD    . GLN   B  1  449  ? -11.094 12.129  112.391 1.00 20.49 ? 447  GLN   B CD    1 
ATOM   12339 O  OE1   . GLN   B  1  449  ? -10.358 12.973  111.900 1.00 23.95 ? 447  GLN   B OE1   1 
ATOM   12340 N  NE2   . GLN   B  1  449  ? -10.659 10.938  112.803 1.00 19.86 ? 447  GLN   B NE2   1 
ATOM   12341 N  N     . CYS   B  1  450  ? -13.752 16.606  113.791 1.00 20.80 ? 448  CYS   B N     1 
ATOM   12342 C  CA    . CYS   B  1  450  ? -13.814 18.050  113.661 1.00 19.85 ? 448  CYS   B CA    1 
ATOM   12343 C  C     . CYS   B  1  450  ? -12.515 18.628  114.186 1.00 20.11 ? 448  CYS   B C     1 
ATOM   12344 O  O     . CYS   B  1  450  ? -11.689 17.926  114.774 1.00 21.34 ? 448  CYS   B O     1 
ATOM   12345 C  CB    . CYS   B  1  450  ? -15.000 18.636  114.438 1.00 22.28 ? 448  CYS   B CB    1 
ATOM   12346 S  SG    . CYS   B  1  450  ? -14.817 18.596  116.243 1.00 24.40 ? 448  CYS   B SG    1 
ATOM   12347 N  N     . LEU   B  1  451  ? -12.359 19.922  113.979 1.00 21.01 ? 449  LEU   B N     1 
ATOM   12348 C  CA    . LEU   B  1  451  ? -11.177 20.634  114.427 1.00 21.64 ? 449  LEU   B CA    1 
ATOM   12349 C  C     . LEU   B  1  451  ? -11.437 21.233  115.799 1.00 24.70 ? 449  LEU   B C     1 
ATOM   12350 O  O     . LEU   B  1  451  ? -12.519 21.760  116.068 1.00 25.75 ? 449  LEU   B O     1 
ATOM   12351 C  CB    . LEU   B  1  451  ? -10.866 21.751  113.438 1.00 23.14 ? 449  LEU   B CB    1 
ATOM   12352 C  CG    . LEU   B  1  451  ? -9.605  22.574  113.627 1.00 28.04 ? 449  LEU   B CG    1 
ATOM   12353 C  CD1   . LEU   B  1  451  ? -8.371  21.675  113.666 1.00 26.95 ? 449  LEU   B CD1   1 
ATOM   12354 C  CD2   . LEU   B  1  451  ? -9.516  23.574  112.487 1.00 30.94 ? 449  LEU   B CD2   1 
ATOM   12355 N  N     . HIS   B  1  452  ? -10.439 21.136  116.671 1.00 21.01 ? 450  HIS   B N     1 
ATOM   12356 C  CA    . HIS   B  1  452  ? -10.527 21.767  117.974 1.00 26.42 ? 450  HIS   B CA    1 
ATOM   12357 C  C     . HIS   B  1  452  ? -10.833 23.250  117.828 1.00 24.33 ? 450  HIS   B C     1 
ATOM   12358 O  O     . HIS   B  1  452  ? -10.267 23.931  116.974 1.00 24.82 ? 450  HIS   B O     1 
ATOM   12359 C  CB    . HIS   B  1  452  ? -9.189  21.620  118.690 1.00 22.77 ? 450  HIS   B CB    1 
ATOM   12360 C  CG    . HIS   B  1  452  ? -9.085  22.468  119.913 1.00 23.32 ? 450  HIS   B CG    1 
ATOM   12361 N  ND1   . HIS   B  1  452  ? -9.594  22.079  121.134 1.00 26.00 ? 450  HIS   B ND1   1 
ATOM   12362 C  CD2   . HIS   B  1  452  ? -8.576  23.707  120.091 1.00 23.64 ? 450  HIS   B CD2   1 
ATOM   12363 C  CE1   . HIS   B  1  452  ? -9.375  23.034  122.020 1.00 27.91 ? 450  HIS   B CE1   1 
ATOM   12364 N  NE2   . HIS   B  1  452  ? -8.764  24.035  121.412 1.00 25.00 ? 450  HIS   B NE2   1 
ATOM   12365 N  N     . GLY   B  1  453  ? -11.721 23.750  118.689 1.00 30.73 ? 451  GLY   B N     1 
ATOM   12366 C  CA    . GLY   B  1  453  ? -12.010 25.171  118.707 1.00 38.69 ? 451  GLY   B CA    1 
ATOM   12367 C  C     . GLY   B  1  453  ? -12.694 25.690  117.466 1.00 40.26 ? 451  GLY   B C     1 
ATOM   12368 O  O     . GLY   B  1  453  ? -12.657 26.894  117.200 1.00 39.90 ? 451  GLY   B O     1 
ATOM   12369 N  N     . MET   B  1  454  ? -13.296 24.804  116.681 1.00 32.05 ? 452  MET   B N     1 
ATOM   12370 C  CA    . MET   B  1  454  ? -14.095 25.197  115.531 1.00 30.90 ? 452  MET   B CA    1 
ATOM   12371 C  C     . MET   B  1  454  ? -15.319 24.299  115.476 1.00 30.79 ? 452  MET   B C     1 
ATOM   12372 O  O     . MET   B  1  454  ? -16.445 24.775  115.300 1.00 34.17 ? 452  MET   B O     1 
ATOM   12373 C  CB    . MET   B  1  454  ? -13.287 25.063  114.236 1.00 27.41 ? 452  MET   B CB    1 
ATOM   12374 C  CG    . MET   B  1  454  ? -14.123 25.242  112.974 1.00 29.80 ? 452  MET   B CG    1 
ATOM   12375 S  SD    . MET   B  1  454  ? -15.023 26.797  113.021 1.00 39.48 ? 452  MET   B SD    1 
ATOM   12376 C  CE    . MET   B  1  454  ? -13.651 27.948  112.988 1.00 38.04 ? 452  MET   B CE    1 
ATOM   12377 N  N     . GLY   B  1  455  ? -15.107 22.996  115.656 1.00 25.08 ? 453  GLY   B N     1 
ATOM   12378 C  CA    . GLY   B  1  455  ? -16.147 22.013  115.437 1.00 27.95 ? 453  GLY   B CA    1 
ATOM   12379 C  C     . GLY   B  1  455  ? -16.989 21.650  116.634 1.00 32.00 ? 453  GLY   B C     1 
ATOM   12380 O  O     . GLY   B  1  455  ? -18.017 20.988  116.469 1.00 30.39 ? 453  GLY   B O     1 
ATOM   12381 N  N     . GLU   B  1  456  ? -16.579 22.047  117.840 1.00 30.35 ? 454  GLU   B N     1 
ATOM   12382 C  CA    . GLU   B  1  456  ? -17.327 21.654  119.033 1.00 32.30 ? 454  GLU   B CA    1 
ATOM   12383 C  C     . GLU   B  1  456  ? -18.776 22.115  119.024 1.00 31.67 ? 454  GLU   B C     1 
ATOM   12384 O  O     . GLU   B  1  456  ? -19.653 21.301  119.359 1.00 33.95 ? 454  GLU   B O     1 
ATOM   12385 C  CB    . GLU   B  1  456  ? -16.591 22.068  120.311 1.00 37.88 ? 454  GLU   B CB    1 
ATOM   12386 C  CG    . GLU   B  1  456  ? -15.281 21.351  120.528 1.00 38.66 ? 454  GLU   B CG    1 
ATOM   12387 C  CD    . GLU   B  1  456  ? -14.119 22.122  119.960 1.00 40.11 ? 454  GLU   B CD    1 
ATOM   12388 O  OE1   . GLU   B  1  456  ? -14.332 22.875  118.984 1.00 36.70 ? 454  GLU   B OE1   1 
ATOM   12389 O  OE2   . GLU   B  1  456  ? -12.999 21.987  120.498 1.00 34.11 ? 454  GLU   B OE2   1 
ATOM   12390 N  N     . PRO   B  1  457  ? -19.104 23.369  118.679 1.00 32.21 ? 455  PRO   B N     1 
ATOM   12391 C  CA    . PRO   B  1  457  ? -20.522 23.765  118.655 1.00 33.89 ? 455  PRO   B CA    1 
ATOM   12392 C  C     . PRO   B  1  457  ? -21.394 22.849  117.819 1.00 36.37 ? 455  PRO   B C     1 
ATOM   12393 O  O     . PRO   B  1  457  ? -22.499 22.490  118.248 1.00 33.93 ? 455  PRO   B O     1 
ATOM   12394 C  CB    . PRO   B  1  457  ? -20.474 25.187  118.088 1.00 32.66 ? 455  PRO   B CB    1 
ATOM   12395 C  CG    . PRO   B  1  457  ? -19.150 25.697  118.516 1.00 36.80 ? 455  PRO   B CG    1 
ATOM   12396 C  CD    . PRO   B  1  457  ? -18.223 24.522  118.414 1.00 34.28 ? 455  PRO   B CD    1 
ATOM   12397 N  N     . LEU   B  1  458  ? -20.927 22.452  116.636 1.00 34.45 ? 456  LEU   B N     1 
ATOM   12398 C  CA    . LEU   B  1  458  ? -21.696 21.503  115.841 1.00 33.15 ? 456  LEU   B CA    1 
ATOM   12399 C  C     . LEU   B  1  458  ? -21.761 20.152  116.531 1.00 31.24 ? 456  LEU   B C     1 
ATOM   12400 O  O     . LEU   B  1  458  ? -22.840 19.577  116.703 1.00 30.85 ? 456  LEU   B O     1 
ATOM   12401 C  CB    . LEU   B  1  458  ? -21.092 21.368  114.444 1.00 30.86 ? 456  LEU   B CB    1 
ATOM   12402 C  CG    . LEU   B  1  458  ? -21.803 20.364  113.537 1.00 28.82 ? 456  LEU   B CG    1 
ATOM   12403 C  CD1   . LEU   B  1  458  ? -23.280 20.718  113.379 1.00 33.94 ? 456  LEU   B CD1   1 
ATOM   12404 C  CD2   . LEU   B  1  458  ? -21.128 20.290  112.178 1.00 31.21 ? 456  LEU   B CD2   1 
ATOM   12405 N  N     . TYR   B  1  459  ? -20.617 19.646  116.973 1.00 28.00 ? 457  TYR   B N     1 
ATOM   12406 C  CA    . TYR   B  1  459  ? -20.560 18.274  117.448 1.00 28.04 ? 457  TYR   B CA    1 
ATOM   12407 C  C     . TYR   B  1  459  ? -21.051 18.095  118.877 1.00 28.38 ? 457  TYR   B C     1 
ATOM   12408 O  O     . TYR   B  1  459  ? -21.316 16.958  119.273 1.00 28.27 ? 457  TYR   B O     1 
ATOM   12409 C  CB    . TYR   B  1  459  ? -19.169 17.689  117.203 1.00 29.45 ? 457  TYR   B CB    1 
ATOM   12410 C  CG    . TYR   B  1  459  ? -19.028 17.319  115.756 1.00 28.89 ? 457  TYR   B CG    1 
ATOM   12411 C  CD1   . TYR   B  1  459  ? -19.573 16.136  115.280 1.00 25.94 ? 457  TYR   B CD1   1 
ATOM   12412 C  CD2   . TYR   B  1  459  ? -18.407 18.172  114.851 1.00 25.26 ? 457  TYR   B CD2   1 
ATOM   12413 C  CE1   . TYR   B  1  459  ? -19.485 15.800  113.947 1.00 26.55 ? 457  TYR   B CE1   1 
ATOM   12414 C  CE2   . TYR   B  1  459  ? -18.304 17.835  113.506 1.00 26.45 ? 457  TYR   B CE2   1 
ATOM   12415 C  CZ    . TYR   B  1  459  ? -18.838 16.644  113.068 1.00 23.14 ? 457  TYR   B CZ    1 
ATOM   12416 O  OH    . TYR   B  1  459  ? -18.748 16.296  111.734 1.00 24.16 ? 457  TYR   B OH    1 
ATOM   12417 N  N     . GLU   B  1  460  ? -21.188 19.179  119.642 1.00 30.54 ? 458  GLU   B N     1 
ATOM   12418 C  CA    . GLU   B  1  460  ? -21.951 19.108  120.882 1.00 32.92 ? 458  GLU   B CA    1 
ATOM   12419 C  C     . GLU   B  1  460  ? -23.403 18.727  120.617 1.00 38.55 ? 458  GLU   B C     1 
ATOM   12420 O  O     . GLU   B  1  460  ? -24.068 18.186  121.510 1.00 36.77 ? 458  GLU   B O     1 
ATOM   12421 C  CB    . GLU   B  1  460  ? -21.864 20.443  121.625 1.00 34.14 ? 458  GLU   B CB    1 
ATOM   12422 N  N     . GLU   B  1  461  ? -23.898 18.974  119.404 1.00 34.82 ? 459  GLU   B N     1 
ATOM   12423 C  CA    . GLU   B  1  461  ? -25.237 18.574  118.994 1.00 37.24 ? 459  GLU   B CA    1 
ATOM   12424 C  C     . GLU   B  1  461  ? -25.273 17.180  118.384 1.00 37.75 ? 459  GLU   B C     1 
ATOM   12425 O  O     . GLU   B  1  461  ? -26.318 16.768  117.868 1.00 33.78 ? 459  GLU   B O     1 
ATOM   12426 C  CB    . GLU   B  1  461  ? -25.805 19.579  117.990 1.00 32.93 ? 459  GLU   B CB    1 
ATOM   12427 C  CG    . GLU   B  1  461  ? -25.611 21.030  118.378 1.00 32.29 ? 459  GLU   B CG    1 
ATOM   12428 C  CD    . GLU   B  1  461  ? -26.395 21.403  119.619 1.00 43.49 ? 459  GLU   B CD    1 
ATOM   12429 O  OE1   . GLU   B  1  461  ? -27.329 20.655  119.974 1.00 43.91 ? 459  GLU   B OE1   1 
ATOM   12430 O  OE2   . GLU   B  1  461  ? -26.074 22.442  120.236 1.00 45.41 ? 459  GLU   B OE2   1 
ATOM   12431 N  N     . VAL   B  1  462  ? -24.158 16.451  118.428 1.00 34.10 ? 460  VAL   B N     1 
ATOM   12432 C  CA    . VAL   B  1  462  ? -24.025 15.149  117.789 1.00 30.05 ? 460  VAL   B CA    1 
ATOM   12433 C  C     . VAL   B  1  462  ? -23.624 14.078  118.792 1.00 33.69 ? 460  VAL   B C     1 
ATOM   12434 O  O     . VAL   B  1  462  ? -24.252 13.016  118.875 1.00 34.90 ? 460  VAL   B O     1 
ATOM   12435 C  CB    . VAL   B  1  462  ? -23.022 15.201  116.610 1.00 32.23 ? 460  VAL   B CB    1 
ATOM   12436 C  CG1   . VAL   B  1  462  ? -22.807 13.814  116.017 1.00 29.24 ? 460  VAL   B CG1   1 
ATOM   12437 C  CG2   . VAL   B  1  462  ? -23.496 16.183  115.554 1.00 29.68 ? 460  VAL   B CG2   1 
ATOM   12438 N  N     . VAL   B  1  463  ? -22.564 14.336  119.561 1.00 29.44 ? 461  VAL   B N     1 
ATOM   12439 C  CA    . VAL   B  1  463  ? -22.098 13.377  120.548 1.00 28.63 ? 461  VAL   B CA    1 
ATOM   12440 C  C     . VAL   B  1  463  ? -23.073 13.339  121.715 1.00 31.26 ? 461  VAL   B C     1 
ATOM   12441 O  O     . VAL   B  1  463  ? -23.583 14.377  122.163 1.00 36.33 ? 461  VAL   B O     1 
ATOM   12442 C  CB    . VAL   B  1  463  ? -20.676 13.745  121.006 1.00 29.46 ? 461  VAL   B CB    1 
ATOM   12443 C  CG1   . VAL   B  1  463  ? -20.176 12.753  122.027 1.00 31.64 ? 461  VAL   B CG1   1 
ATOM   12444 C  CG2   . VAL   B  1  463  ? -19.732 13.798  119.800 1.00 30.77 ? 461  VAL   B CG2   1 
ATOM   12445 N  N     . GLY   B  1  464  ? -23.339 12.139  122.211 1.00 37.33 ? 462  GLY   B N     1 
ATOM   12446 C  CA    . GLY   B  1  464  ? -24.187 11.989  123.375 1.00 35.55 ? 462  GLY   B CA    1 
ATOM   12447 C  C     . GLY   B  1  464  ? -25.471 11.249  123.080 1.00 40.15 ? 462  GLY   B C     1 
ATOM   12448 O  O     . GLY   B  1  464  ? -26.067 11.431  122.015 1.00 39.47 ? 462  GLY   B O     1 
ATOM   12449 N  N     . ARG   B  1  465  ? -25.902 10.405  124.023 1.00 40.17 ? 463  ARG   B N     1 
ATOM   12450 C  CA    . ARG   B  1  465  ? -27.167 9.694   123.865 1.00 41.74 ? 463  ARG   B CA    1 
ATOM   12451 C  C     . ARG   B  1  465  ? -28.332 10.660  123.693 1.00 44.02 ? 463  ARG   B C     1 
ATOM   12452 O  O     . ARG   B  1  465  ? -29.308 10.338  123.006 1.00 47.61 ? 463  ARG   B O     1 
ATOM   12453 C  CB    . ARG   B  1  465  ? -27.402 8.768   125.058 1.00 49.80 ? 463  ARG   B CB    1 
ATOM   12454 N  N     . GLY   B  1  466  ? -28.242 11.848  124.288 1.00 42.57 ? 464  GLY   B N     1 
ATOM   12455 C  CA    . GLY   B  1  466  ? -29.249 12.877  124.134 1.00 46.03 ? 464  GLY   B CA    1 
ATOM   12456 C  C     . GLY   B  1  466  ? -29.164 13.681  122.862 1.00 47.22 ? 464  GLY   B C     1 
ATOM   12457 O  O     . GLY   B  1  466  ? -29.953 14.609  122.663 1.00 43.86 ? 464  GLY   B O     1 
ATOM   12458 N  N     . LYS   B  1  467  ? -28.210 13.355  121.991 1.00 44.27 ? 465  LYS   B N     1 
ATOM   12459 C  CA    . LYS   B  1  467  ? -28.064 14.029  120.710 1.00 40.96 ? 465  LYS   B CA    1 
ATOM   12460 C  C     . LYS   B  1  467  ? -28.198 13.005  119.592 1.00 41.94 ? 465  LYS   B C     1 
ATOM   12461 O  O     . LYS   B  1  467  ? -29.152 12.220  119.578 1.00 41.04 ? 465  LYS   B O     1 
ATOM   12462 C  CB    . LYS   B  1  467  ? -26.712 14.741  120.639 1.00 36.42 ? 465  LYS   B CB    1 
ATOM   12463 C  CG    . LYS   B  1  467  ? -26.533 15.823  121.695 1.00 42.31 ? 465  LYS   B CG    1 
ATOM   12464 C  CD    . LYS   B  1  467  ? -27.525 16.955  121.496 1.00 44.79 ? 465  LYS   B CD    1 
ATOM   12465 C  CE    . LYS   B  1  467  ? -27.380 18.016  122.576 1.00 45.48 ? 465  LYS   B CE    1 
ATOM   12466 N  NZ    . LYS   B  1  467  ? -28.148 19.247  122.232 1.00 47.50 ? 465  LYS   B NZ    1 
ATOM   12467 N  N     . LEU   B  1  468  ? -27.254 12.994  118.651 1.00 36.01 ? 466  LEU   B N     1 
ATOM   12468 C  CA    . LEU   B  1  468  ? -27.278 11.986  117.601 1.00 34.19 ? 466  LEU   B CA    1 
ATOM   12469 C  C     . LEU   B  1  468  ? -26.604 10.689  118.014 1.00 29.85 ? 466  LEU   B C     1 
ATOM   12470 O  O     . LEU   B  1  468  ? -26.681 9.703   117.271 1.00 33.20 ? 466  LEU   B O     1 
ATOM   12471 C  CB    . LEU   B  1  468  ? -26.660 12.525  116.307 1.00 33.90 ? 466  LEU   B CB    1 
ATOM   12472 C  CG    . LEU   B  1  468  ? -27.384 13.752  115.754 1.00 36.88 ? 466  LEU   B CG    1 
ATOM   12473 C  CD1   . LEU   B  1  468  ? -26.866 14.137  114.378 1.00 37.03 ? 466  LEU   B CD1   1 
ATOM   12474 C  CD2   . LEU   B  1  468  ? -28.891 13.488  115.729 1.00 37.45 ? 466  LEU   B CD2   1 
ATOM   12475 N  N     . ASP   B  1  469  ? -25.956 10.665  119.177 1.00 32.71 ? 467  ASP   B N     1 
ATOM   12476 C  CA    . ASP   B  1  469  ? -25.290 9.467   119.682 1.00 38.98 ? 467  ASP   B CA    1 
ATOM   12477 C  C     . ASP   B  1  469  ? -24.239 8.958   118.701 1.00 31.84 ? 467  ASP   B C     1 
ATOM   12478 O  O     . ASP   B  1  469  ? -24.101 7.754   118.476 1.00 31.96 ? 467  ASP   B O     1 
ATOM   12479 C  CB    . ASP   B  1  469  ? -26.285 8.373   120.072 1.00 37.13 ? 467  ASP   B CB    1 
ATOM   12480 C  CG    . ASP   B  1  469  ? -25.771 7.500   121.190 1.00 44.01 ? 467  ASP   B CG    1 
ATOM   12481 O  OD1   . ASP   B  1  469  ? -24.672 7.790   121.711 1.00 42.00 ? 467  ASP   B OD1   1 
ATOM   12482 O  OD2   . ASP   B  1  469  ? -26.465 6.527   121.551 1.00 50.15 ? 467  ASP   B OD2   1 
ATOM   12483 N  N     . ARG   B  1  470  ? -23.495 9.892   118.112 1.00 34.35 ? 468  ARG   B N     1 
ATOM   12484 C  CA    . ARG   B  1  470  ? -22.404 9.587   117.210 1.00 31.24 ? 468  ARG   B CA    1 
ATOM   12485 C  C     . ARG   B  1  470  ? -21.109 10.188  117.738 1.00 31.07 ? 468  ARG   B C     1 
ATOM   12486 O  O     . ARG   B  1  470  ? -21.093 11.343  118.178 1.00 30.58 ? 468  ARG   B O     1 
ATOM   12487 C  CB    . ARG   B  1  470  ? -22.684 10.137  115.804 1.00 31.59 ? 468  ARG   B CB    1 
ATOM   12488 C  CG    . ARG   B  1  470  ? -23.870 9.470   115.119 1.00 31.65 ? 468  ARG   B CG    1 
ATOM   12489 C  CD    . ARG   B  1  470  ? -23.685 7.962   115.074 1.00 29.02 ? 468  ARG   B CD    1 
ATOM   12490 N  NE    . ARG   B  1  470  ? -24.807 7.278   114.437 1.00 33.47 ? 468  ARG   B NE    1 
ATOM   12491 C  CZ    . ARG   B  1  470  ? -25.866 6.815   115.085 1.00 40.04 ? 468  ARG   B CZ    1 
ATOM   12492 N  NH1   . ARG   B  1  470  ? -25.998 6.971   116.393 1.00 35.30 ? 468  ARG   B NH1   1 
ATOM   12493 N  NH2   . ARG   B  1  470  ? -26.817 6.179   114.405 1.00 39.92 ? 468  ARG   B NH2   1 
ATOM   12494 N  N     . PRO   B  1  471  ? -20.017 9.438   117.706 1.00 27.94 ? 469  PRO   B N     1 
ATOM   12495 C  CA    . PRO   B  1  471  ? -18.752 9.948   118.234 1.00 27.01 ? 469  PRO   B CA    1 
ATOM   12496 C  C     . PRO   B  1  471  ? -18.109 10.934  117.274 1.00 26.19 ? 469  PRO   B C     1 
ATOM   12497 O  O     . PRO   B  1  471  ? -18.352 10.938  116.064 1.00 24.59 ? 469  PRO   B O     1 
ATOM   12498 C  CB    . PRO   B  1  471  ? -17.898 8.683   118.346 1.00 24.75 ? 469  PRO   B CB    1 
ATOM   12499 C  CG    . PRO   B  1  471  ? -18.400 7.825   117.259 1.00 31.01 ? 469  PRO   B CG    1 
ATOM   12500 C  CD    . PRO   B  1  471  ? -19.881 8.057   117.224 1.00 29.27 ? 469  PRO   B CD    1 
ATOM   12501 N  N     . CYS   B  1  472  ? -17.270 11.787  117.850 1.00 26.58 ? 470  CYS   B N     1 
ATOM   12502 C  CA    . CYS   B  1  472  ? -16.504 12.738  117.070 1.00 24.35 ? 470  CYS   B CA    1 
ATOM   12503 C  C     . CYS   B  1  472  ? -15.094 12.799  117.634 1.00 23.15 ? 470  CYS   B C     1 
ATOM   12504 O  O     . CYS   B  1  472  ? -14.911 12.943  118.850 1.00 24.88 ? 470  CYS   B O     1 
ATOM   12505 C  CB    . CYS   B  1  472  ? -17.143 14.123  117.103 1.00 26.19 ? 470  CYS   B CB    1 
ATOM   12506 S  SG    . CYS   B  1  472  ? -16.234 15.284  116.105 1.00 27.96 ? 470  CYS   B SG    1 
ATOM   12507 N  N     . ARG   B  1  473  ? -14.107 12.659  116.756 1.00 23.61 ? 471  ARG   B N     1 
ATOM   12508 C  CA    . ARG   B  1  473  ? -12.706 12.795  117.126 1.00 24.30 ? 471  ARG   B CA    1 
ATOM   12509 C  C     . ARG   B  1  473  ? -12.249 14.210  116.815 1.00 23.26 ? 471  ARG   B C     1 
ATOM   12510 O  O     . ARG   B  1  473  ? -12.405 14.689  115.685 1.00 23.46 ? 471  ARG   B O     1 
ATOM   12511 C  CB    . ARG   B  1  473  ? -11.827 11.794  116.379 1.00 20.37 ? 471  ARG   B CB    1 
ATOM   12512 C  CG    . ARG   B  1  473  ? -10.361 11.832  116.848 1.00 21.82 ? 471  ARG   B CG    1 
ATOM   12513 C  CD    . ARG   B  1  473  ? -9.548  10.719  116.207 1.00 20.63 ? 471  ARG   B CD    1 
ATOM   12514 N  NE    . ARG   B  1  473  ? -10.223 9.433   116.327 1.00 21.72 ? 471  ARG   B NE    1 
ATOM   12515 C  CZ    . ARG   B  1  473  ? -10.168 8.657   117.400 1.00 23.87 ? 471  ARG   B CZ    1 
ATOM   12516 N  NH1   . ARG   B  1  473  ? -9.406  8.967   118.438 1.00 24.26 ? 471  ARG   B NH1   1 
ATOM   12517 N  NH2   . ARG   B  1  473  ? -10.895 7.544   117.438 1.00 25.43 ? 471  ARG   B NH2   1 
ATOM   12518 N  N     . ILE   B  1  474  ? -11.677 14.867  117.816 1.00 21.68 ? 472  ILE   B N     1 
ATOM   12519 C  CA    . ILE   B  1  474  ? -11.240 16.249  117.684 1.00 20.98 ? 472  ILE   B CA    1 
ATOM   12520 C  C     . ILE   B  1  474  ? -9.780  16.266  117.251 1.00 22.00 ? 472  ILE   B C     1 
ATOM   12521 O  O     . ILE   B  1  474  ? -8.912  15.716  117.939 1.00 21.50 ? 472  ILE   B O     1 
ATOM   12522 C  CB    . ILE   B  1  474  ? -11.425 16.997  119.009 1.00 21.92 ? 472  ILE   B CB    1 
ATOM   12523 C  CG1   . ILE   B  1  474  ? -12.909 17.027  119.389 1.00 22.35 ? 472  ILE   B CG1   1 
ATOM   12524 C  CG2   . ILE   B  1  474  ? -10.862 18.393  118.900 1.00 22.62 ? 472  ILE   B CG2   1 
ATOM   12525 C  CD1   . ILE   B  1  474  ? -13.152 17.594  120.765 1.00 23.34 ? 472  ILE   B CD1   1 
ATOM   12526 N  N     . TYR   B  1  475  ? -9.517  16.880  116.105 1.00 19.84 ? 473  TYR   B N     1 
ATOM   12527 C  CA    . TYR   B  1  475  ? -8.159  17.134  115.637 1.00 19.42 ? 473  TYR   B CA    1 
ATOM   12528 C  C     . TYR   B  1  475  ? -7.625  18.295  116.457 1.00 20.71 ? 473  TYR   B C     1 
ATOM   12529 O  O     . TYR   B  1  475  ? -8.143  19.415  116.380 1.00 21.21 ? 473  TYR   B O     1 
ATOM   12530 C  CB    . TYR   B  1  475  ? -8.188  17.486  114.156 1.00 19.43 ? 473  TYR   B CB    1 
ATOM   12531 C  CG    . TYR   B  1  475  ? -6.837  17.542  113.491 1.00 19.14 ? 473  TYR   B CG    1 
ATOM   12532 C  CD1   . TYR   B  1  475  ? -6.084  18.709  113.504 1.00 21.82 ? 473  TYR   B CD1   1 
ATOM   12533 C  CD2   . TYR   B  1  475  ? -6.320  16.431  112.839 1.00 19.71 ? 473  TYR   B CD2   1 
ATOM   12534 C  CE1   . TYR   B  1  475  ? -4.852  18.769  112.889 1.00 21.73 ? 473  TYR   B CE1   1 
ATOM   12535 C  CE2   . TYR   B  1  475  ? -5.089  16.484  112.214 1.00 17.83 ? 473  TYR   B CE2   1 
ATOM   12536 C  CZ    . TYR   B  1  475  ? -4.360  17.653  112.250 1.00 20.22 ? 473  TYR   B CZ    1 
ATOM   12537 O  OH    . TYR   B  1  475  ? -3.127  17.725  111.650 1.00 21.31 ? 473  TYR   B OH    1 
ATOM   12538 N  N     . ALA   B  1  476  ? -6.605  18.022  117.260 1.00 20.47 ? 474  ALA   B N     1 
ATOM   12539 C  CA    . ALA   B  1  476  ? -6.188  18.932  118.321 1.00 20.97 ? 474  ALA   B CA    1 
ATOM   12540 C  C     . ALA   B  1  476  ? -4.768  19.417  118.076 1.00 21.49 ? 474  ALA   B C     1 
ATOM   12541 O  O     . ALA   B  1  476  ? -3.799  18.684  118.353 1.00 21.58 ? 474  ALA   B O     1 
ATOM   12542 C  CB    . ALA   B  1  476  ? -6.291  18.204  119.653 1.00 22.90 ? 474  ALA   B CB    1 
ATOM   12543 N  N     . PRO   B  1  477  ? -4.593  20.629  117.556 1.00 21.21 ? 475  PRO   B N     1 
ATOM   12544 C  CA    . PRO   B  1  477  ? -3.246  21.184  117.427 1.00 20.66 ? 475  PRO   B CA    1 
ATOM   12545 C  C     . PRO   B  1  477  ? -2.645  21.416  118.796 1.00 20.88 ? 475  PRO   B C     1 
ATOM   12546 O  O     . PRO   B  1  477  ? -3.328  21.824  119.737 1.00 21.47 ? 475  PRO   B O     1 
ATOM   12547 C  CB    . PRO   B  1  477  ? -3.479  22.515  116.708 1.00 21.89 ? 475  PRO   B CB    1 
ATOM   12548 C  CG    . PRO   B  1  477  ? -4.832  22.393  116.074 1.00 23.96 ? 475  PRO   B CG    1 
ATOM   12549 C  CD    . PRO   B  1  477  ? -5.620  21.525  116.999 1.00 21.76 ? 475  PRO   B CD    1 
ATOM   12550 N  N     . VAL   B  1  478  ? -1.346  21.172  118.892 1.00 19.84 ? 476  VAL   B N     1 
ATOM   12551 C  CA    . VAL   B  1  478  ? -0.606  21.314  120.133 1.00 19.62 ? 476  VAL   B CA    1 
ATOM   12552 C  C     . VAL   B  1  478  ? 0.679   22.041  119.799 1.00 22.78 ? 476  VAL   B C     1 
ATOM   12553 O  O     . VAL   B  1  478  ? 1.455   21.569  118.966 1.00 24.22 ? 476  VAL   B O     1 
ATOM   12554 C  CB    . VAL   B  1  478  ? -0.288  19.948  120.768 1.00 20.19 ? 476  VAL   B CB    1 
ATOM   12555 C  CG1   . VAL   B  1  478  ? 0.473   20.134  122.067 1.00 23.42 ? 476  VAL   B CG1   1 
ATOM   12556 C  CG2   . VAL   B  1  478  ? -1.566  19.146  120.992 1.00 21.52 ? 476  VAL   B CG2   1 
ATOM   12557 N  N     . GLY   B  1  479  ? 0.912   23.170  120.445 1.00 25.45 ? 477  GLY   B N     1 
ATOM   12558 C  CA    . GLY   B  1  479  ? 2.155   23.874  120.219 1.00 29.12 ? 477  GLY   B CA    1 
ATOM   12559 C  C     . GLY   B  1  479  ? 2.060   25.325  120.632 1.00 31.40 ? 477  GLY   B C     1 
ATOM   12560 O  O     . GLY   B  1  479  ? 1.033   25.801  121.120 1.00 26.17 ? 477  GLY   B O     1 
ATOM   12561 N  N     . THR   B  1  480  ? 3.165   26.021  120.387 1.00 34.11 ? 478  THR   B N     1 
ATOM   12562 C  CA    . THR   B  1  480  ? 3.387   27.375  120.859 1.00 40.12 ? 478  THR   B CA    1 
ATOM   12563 C  C     . THR   B  1  480  ? 2.713   28.381  119.930 1.00 41.41 ? 478  THR   B C     1 
ATOM   12564 O  O     . THR   B  1  480  ? 2.165   28.036  118.877 1.00 39.16 ? 478  THR   B O     1 
ATOM   12565 C  CB    . THR   B  1  480  ? 4.887   27.648  120.918 1.00 37.03 ? 478  THR   B CB    1 
ATOM   12566 O  OG1   . THR   B  1  480  ? 5.427   27.544  119.593 1.00 45.80 ? 478  THR   B OG1   1 
ATOM   12567 C  CG2   . THR   B  1  480  ? 5.572   26.635  121.803 1.00 35.74 ? 478  THR   B CG2   1 
ATOM   12568 N  N     . HIS   B  1  481  ? 2.772   29.655  120.327 1.00 44.38 ? 479  HIS   B N     1 
ATOM   12569 C  CA    . HIS   B  1  481  ? 2.208   30.722  119.506 1.00 40.61 ? 479  HIS   B CA    1 
ATOM   12570 C  C     . HIS   B  1  481  ? 2.929   30.833  118.169 1.00 46.85 ? 479  HIS   B C     1 
ATOM   12571 O  O     . HIS   B  1  481  ? 2.288   30.980  117.120 1.00 42.70 ? 479  HIS   B O     1 
ATOM   12572 C  CB    . HIS   B  1  481  ? 2.282   32.048  120.260 1.00 40.97 ? 479  HIS   B CB    1 
ATOM   12573 C  CG    . HIS   B  1  481  ? 1.500   32.060  121.536 1.00 43.81 ? 479  HIS   B CG    1 
ATOM   12574 N  ND1   . HIS   B  1  481  ? 1.397   33.178  122.335 1.00 46.96 ? 479  HIS   B ND1   1 
ATOM   12575 C  CD2   . HIS   B  1  481  ? 0.780   31.090  122.150 1.00 41.73 ? 479  HIS   B CD2   1 
ATOM   12576 C  CE1   . HIS   B  1  481  ? 0.648   32.897  123.387 1.00 48.30 ? 479  HIS   B CE1   1 
ATOM   12577 N  NE2   . HIS   B  1  481  ? 0.261   31.637  123.299 1.00 51.11 ? 479  HIS   B NE2   1 
ATOM   12578 N  N     . GLU   B  1  482  ? 4.263   30.769  118.185 1.00 44.56 ? 480  GLU   B N     1 
ATOM   12579 C  CA    . GLU   B  1  482  ? 5.024   30.882  116.944 1.00 41.69 ? 480  GLU   B CA    1 
ATOM   12580 C  C     . GLU   B  1  482  ? 4.681   29.751  115.984 1.00 40.82 ? 480  GLU   B C     1 
ATOM   12581 O  O     . GLU   B  1  482  ? 4.543   29.971  114.775 1.00 47.21 ? 480  GLU   B O     1 
ATOM   12582 C  CB    . GLU   B  1  482  ? 6.523   30.899  117.249 1.00 45.60 ? 480  GLU   B CB    1 
ATOM   12583 N  N     . THR   B  1  483  ? 4.518   28.536  116.508 1.00 45.77 ? 481  THR   B N     1 
ATOM   12584 C  CA    . THR   B  1  483  ? 4.236   27.392  115.648 1.00 47.86 ? 481  THR   B CA    1 
ATOM   12585 C  C     . THR   B  1  483  ? 2.818   27.452  115.086 1.00 44.29 ? 481  THR   B C     1 
ATOM   12586 O  O     . THR   B  1  483  ? 2.604   27.223  113.889 1.00 46.13 ? 481  THR   B O     1 
ATOM   12587 C  CB    . THR   B  1  483  ? 4.476   26.089  116.415 1.00 49.25 ? 481  THR   B CB    1 
ATOM   12588 N  N     . LEU   B  1  484  ? 1.833   27.769  115.933 1.00 42.95 ? 482  LEU   B N     1 
ATOM   12589 C  CA    . LEU   B  1  484  ? 0.446   27.764  115.472 1.00 43.10 ? 482  LEU   B CA    1 
ATOM   12590 C  C     . LEU   B  1  484  ? 0.181   28.850  114.434 1.00 40.61 ? 482  LEU   B C     1 
ATOM   12591 O  O     . LEU   B  1  484  ? -0.607  28.640  113.503 1.00 41.87 ? 482  LEU   B O     1 
ATOM   12592 C  CB    . LEU   B  1  484  ? -0.521  27.864  116.657 1.00 40.88 ? 482  LEU   B CB    1 
ATOM   12593 C  CG    . LEU   B  1  484  ? -0.671  29.189  117.411 1.00 41.33 ? 482  LEU   B CG    1 
ATOM   12594 C  CD1   . LEU   B  1  484  ? -1.720  30.102  116.776 1.00 39.47 ? 482  LEU   B CD1   1 
ATOM   12595 C  CD2   . LEU   B  1  484  ? -1.011  28.938  118.866 1.00 38.37 ? 482  LEU   B CD2   1 
ATOM   12596 N  N     . LEU   B  1  485  ? 0.824   30.011  114.570 1.00 39.52 ? 483  LEU   B N     1 
ATOM   12597 C  CA    . LEU   B  1  485  ? 0.614   31.086  113.609 1.00 45.04 ? 483  LEU   B CA    1 
ATOM   12598 C  C     . LEU   B  1  485  ? 1.121   30.733  112.217 1.00 41.52 ? 483  LEU   B C     1 
ATOM   12599 O  O     . LEU   B  1  485  ? 0.658   31.327  111.237 1.00 38.30 ? 483  LEU   B O     1 
ATOM   12600 C  CB    . LEU   B  1  485  ? 1.291   32.370  114.099 1.00 42.44 ? 483  LEU   B CB    1 
ATOM   12601 C  CG    . LEU   B  1  485  ? 0.630   33.106  115.267 1.00 40.12 ? 483  LEU   B CG    1 
ATOM   12602 C  CD1   . LEU   B  1  485  ? 1.511   34.249  115.730 1.00 40.15 ? 483  LEU   B CD1   1 
ATOM   12603 C  CD2   . LEU   B  1  485  ? -0.756  33.617  114.879 1.00 40.56 ? 483  LEU   B CD2   1 
ATOM   12604 N  N     . ALA   B  1  486  ? 2.038   29.765  112.110 1.00 42.17 ? 484  ALA   B N     1 
ATOM   12605 C  CA    . ALA   B  1  486  ? 2.719   29.510  110.842 1.00 36.60 ? 484  ALA   B CA    1 
ATOM   12606 C  C     . ALA   B  1  486  ? 1.770   29.015  109.755 1.00 45.65 ? 484  ALA   B C     1 
ATOM   12607 O  O     . ALA   B  1  486  ? 2.031   29.226  108.565 1.00 47.91 ? 484  ALA   B O     1 
ATOM   12608 C  CB    . ALA   B  1  486  ? 3.865   28.520  111.051 1.00 41.96 ? 484  ALA   B CB    1 
ATOM   12609 N  N     . TYR   B  1  487  ? 0.674   28.345  110.131 1.00 42.51 ? 485  TYR   B N     1 
ATOM   12610 C  CA    . TYR   B  1  487  ? -0.277  27.874  109.129 1.00 40.24 ? 485  TYR   B CA    1 
ATOM   12611 C  C     . TYR   B  1  487  ? -1.722  28.145  109.532 1.00 40.22 ? 485  TYR   B C     1 
ATOM   12612 O  O     . TYR   B  1  487  ? -2.637  27.467  109.041 1.00 33.44 ? 485  TYR   B O     1 
ATOM   12613 C  CB    . TYR   B  1  487  ? -0.071  26.391  108.795 1.00 41.13 ? 485  TYR   B CB    1 
ATOM   12614 C  CG    . TYR   B  1  487  ? 1.212   26.110  108.041 1.00 46.35 ? 485  TYR   B CG    1 
ATOM   12615 C  CD1   . TYR   B  1  487  ? 1.310   26.368  106.678 1.00 49.62 ? 485  TYR   B CD1   1 
ATOM   12616 C  CD2   . TYR   B  1  487  ? 2.324   25.586  108.691 1.00 46.73 ? 485  TYR   B CD2   1 
ATOM   12617 C  CE1   . TYR   B  1  487  ? 2.483   26.115  105.981 1.00 51.62 ? 485  TYR   B CE1   1 
ATOM   12618 C  CE2   . TYR   B  1  487  ? 3.501   25.327  108.004 1.00 48.46 ? 485  TYR   B CE2   1 
ATOM   12619 C  CZ    . TYR   B  1  487  ? 3.575   25.595  106.650 1.00 54.05 ? 485  TYR   B CZ    1 
ATOM   12620 O  OH    . TYR   B  1  487  ? 4.744   25.340  105.964 1.00 57.23 ? 485  TYR   B OH    1 
ATOM   12621 N  N     . LEU   B  1  488  ? -1.952  29.122  110.410 1.00 42.82 ? 486  LEU   B N     1 
ATOM   12622 C  CA    . LEU   B  1  488  ? -3.319  29.444  110.798 1.00 38.72 ? 486  LEU   B CA    1 
ATOM   12623 C  C     . LEU   B  1  488  ? -4.123  29.997  109.628 1.00 39.76 ? 486  LEU   B C     1 
ATOM   12624 O  O     . LEU   B  1  488  ? -5.341  29.796  109.565 1.00 31.31 ? 486  LEU   B O     1 
ATOM   12625 C  CB    . LEU   B  1  488  ? -3.313  30.422  111.971 1.00 39.14 ? 486  LEU   B CB    1 
ATOM   12626 C  CG    . LEU   B  1  488  ? -4.689  30.775  112.527 1.00 37.11 ? 486  LEU   B CG    1 
ATOM   12627 C  CD1   . LEU   B  1  488  ? -5.482  29.502  112.773 1.00 45.80 ? 486  LEU   B CD1   1 
ATOM   12628 C  CD2   . LEU   B  1  488  ? -4.532  31.566  113.810 1.00 29.56 ? 486  LEU   B CD2   1 
ATOM   12629 N  N     . VAL   B  1  489  ? -3.467  30.686  108.691 1.00 38.98 ? 487  VAL   B N     1 
ATOM   12630 C  CA    . VAL   B  1  489  ? -4.175  31.228  107.532 1.00 32.52 ? 487  VAL   B CA    1 
ATOM   12631 C  C     . VAL   B  1  489  ? -4.921  30.121  106.800 1.00 36.33 ? 487  VAL   B C     1 
ATOM   12632 O  O     . VAL   B  1  489  ? -6.132  30.208  106.566 1.00 43.21 ? 487  VAL   B O     1 
ATOM   12633 C  CB    . VAL   B  1  489  ? -3.205  31.975  106.602 1.00 34.93 ? 487  VAL   B CB    1 
ATOM   12634 C  CG1   . VAL   B  1  489  ? -3.897  32.309  105.281 1.00 36.12 ? 487  VAL   B CG1   1 
ATOM   12635 C  CG2   . VAL   B  1  489  ? -2.691  33.236  107.289 1.00 37.32 ? 487  VAL   B CG2   1 
ATOM   12636 N  N     . ARG   B  1  490  ? -4.203  29.054  106.439 1.00 41.08 ? 488  ARG   B N     1 
ATOM   12637 C  CA    . ARG   B  1  490  ? -4.835  27.936  105.746 1.00 40.51 ? 488  ARG   B CA    1 
ATOM   12638 C  C     . ARG   B  1  490  ? -5.929  27.308  106.600 1.00 39.13 ? 488  ARG   B C     1 
ATOM   12639 O  O     . ARG   B  1  490  ? -6.980  26.908  106.084 1.00 39.39 ? 488  ARG   B O     1 
ATOM   12640 C  CB    . ARG   B  1  490  ? -3.778  26.896  105.369 1.00 40.00 ? 488  ARG   B CB    1 
ATOM   12641 C  CG    . ARG   B  1  490  ? -4.315  25.697  104.593 1.00 39.47 ? 488  ARG   B CG    1 
ATOM   12642 C  CD    . ARG   B  1  490  ? -3.250  24.610  104.471 1.00 35.17 ? 488  ARG   B CD    1 
ATOM   12643 N  NE    . ARG   B  1  490  ? -2.909  24.039  105.772 1.00 34.63 ? 488  ARG   B NE    1 
ATOM   12644 C  CZ    . ARG   B  1  490  ? -1.711  23.561  106.084 1.00 33.01 ? 488  ARG   B CZ    1 
ATOM   12645 N  NH1   . ARG   B  1  490  ? -0.701  23.618  105.231 1.00 29.19 ? 488  ARG   B NH1   1 
ATOM   12646 N  NH2   . ARG   B  1  490  ? -1.521  23.024  107.286 1.00 28.54 ? 488  ARG   B NH2   1 
ATOM   12647 N  N     . ARG   B  1  491  ? -5.711  27.240  107.917 1.00 36.49 ? 489  ARG   B N     1 
ATOM   12648 C  CA    . ARG   B  1  491  ? -6.681  26.595  108.793 1.00 42.70 ? 489  ARG   B CA    1 
ATOM   12649 C  C     . ARG   B  1  491  ? -7.990  27.370  108.827 1.00 43.79 ? 489  ARG   B C     1 
ATOM   12650 O  O     . ARG   B  1  491  ? -9.073  26.773  108.851 1.00 40.07 ? 489  ARG   B O     1 
ATOM   12651 C  CB    . ARG   B  1  491  ? -6.098  26.462  110.203 1.00 40.68 ? 489  ARG   B CB    1 
ATOM   12652 N  N     . LEU   B  1  492  ? -7.908  28.702  108.803 1.00 46.14 ? 490  LEU   B N     1 
ATOM   12653 C  CA    . LEU   B  1  492  ? -9.074  29.566  108.938 1.00 48.13 ? 490  LEU   B CA    1 
ATOM   12654 C  C     . LEU   B  1  492  ? -9.816  29.767  107.619 1.00 48.64 ? 490  LEU   B C     1 
ATOM   12655 O  O     . LEU   B  1  492  ? -11.053 29.811  107.606 1.00 35.63 ? 490  LEU   B O     1 
ATOM   12656 C  CB    . LEU   B  1  492  ? -8.650  30.919  109.518 1.00 43.64 ? 490  LEU   B CB    1 
ATOM   12657 N  N     . LEU   B  1  493  ? -9.088  29.897  106.511 1.00 45.80 ? 491  LEU   B N     1 
ATOM   12658 C  CA    . LEU   B  1  493  ? -9.714  30.113  105.212 1.00 32.51 ? 491  LEU   B CA    1 
ATOM   12659 C  C     . LEU   B  1  493  ? -10.523 28.886  104.805 1.00 43.30 ? 491  LEU   B C     1 
ATOM   12660 O  O     . LEU   B  1  493  ? -11.644 29.005  104.312 1.00 49.57 ? 491  LEU   B O     1 
ATOM   12661 C  CB    . LEU   B  1  493  ? -8.662  30.445  104.144 1.00 39.22 ? 491  LEU   B CB    1 
ATOM   12662 N  N     . ALA   B  1  497  ? -12.975 31.982  103.509 1.00 40.06 ? 495  ALA   B N     1 
ATOM   12663 C  CA    . ALA   B  1  497  ? -13.715 31.822  102.260 1.00 44.99 ? 495  ALA   B CA    1 
ATOM   12664 C  C     . ALA   B  1  497  ? -15.220 31.983  102.447 1.00 38.46 ? 495  ALA   B C     1 
ATOM   12665 O  O     . ALA   B  1  497  ? -15.813 31.380  103.341 1.00 41.58 ? 495  ALA   B O     1 
ATOM   12666 C  CB    . ALA   B  1  497  ? -13.406 30.478  101.623 1.00 35.71 ? 495  ALA   B CB    1 
ATOM   12667 N  N     . ASN   B  1  498  ? -15.828 32.788  101.570 1.00 41.38 ? 496  ASN   B N     1 
ATOM   12668 C  CA    . ASN   B  1  498  ? -17.267 33.027  101.639 1.00 43.04 ? 496  ASN   B CA    1 
ATOM   12669 C  C     . ASN   B  1  498  ? -18.070 31.756  101.377 1.00 40.02 ? 496  ASN   B C     1 
ATOM   12670 O  O     . ASN   B  1  498  ? -19.203 31.629  101.852 1.00 41.01 ? 496  ASN   B O     1 
ATOM   12671 C  CB    . ASN   B  1  498  ? -17.660 34.120  100.643 1.00 39.99 ? 496  ASN   B CB    1 
ATOM   12672 N  N     . SER   B  1  499  ? -17.510 30.813  100.624 1.00 36.75 ? 497  SER   B N     1 
ATOM   12673 C  CA    . SER   B  1  499  ? -18.201 29.571  100.303 1.00 33.04 ? 497  SER   B CA    1 
ATOM   12674 C  C     . SER   B  1  499  ? -18.164 28.561  101.439 1.00 31.91 ? 497  SER   B C     1 
ATOM   12675 O  O     . SER   B  1  499  ? -18.807 27.512  101.332 1.00 31.49 ? 497  SER   B O     1 
ATOM   12676 C  CB    . SER   B  1  499  ? -17.549 28.937  99.076  1.00 36.04 ? 497  SER   B CB    1 
ATOM   12677 O  OG    . SER   B  1  499  ? -16.156 28.795  99.296  1.00 36.92 ? 497  SER   B OG    1 
ATOM   12678 N  N     . SER   B  1  500  ? -17.419 28.842  102.503 1.00 30.52 ? 498  SER   B N     1 
ATOM   12679 C  CA    . SER   B  1  500  ? -17.248 27.891  103.588 1.00 30.48 ? 498  SER   B CA    1 
ATOM   12680 C  C     . SER   B  1  500  ? -18.458 27.908  104.514 1.00 35.08 ? 498  SER   B C     1 
ATOM   12681 O  O     . SER   B  1  500  ? -19.046 28.961  104.774 1.00 38.53 ? 498  SER   B O     1 
ATOM   12682 C  CB    . SER   B  1  500  ? -15.987 28.229  104.385 1.00 33.95 ? 498  SER   B CB    1 
ATOM   12683 N  N     . PHE   B  1  501  ? -18.831 26.723  105.002 1.00 29.06 ? 499  PHE   B N     1 
ATOM   12684 C  CA    . PHE   B  1  501  ? -19.848 26.638  106.047 1.00 33.19 ? 499  PHE   B CA    1 
ATOM   12685 C  C     . PHE   B  1  501  ? -19.444 27.459  107.269 1.00 38.48 ? 499  PHE   B C     1 
ATOM   12686 O  O     . PHE   B  1  501  ? -20.297 28.068  107.922 1.00 46.48 ? 499  PHE   B O     1 
ATOM   12687 C  CB    . PHE   B  1  501  ? -20.082 25.171  106.422 1.00 32.41 ? 499  PHE   B CB    1 
ATOM   12688 C  CG    . PHE   B  1  501  ? -21.319 24.932  107.254 1.00 35.10 ? 499  PHE   B CG    1 
ATOM   12689 C  CD1   . PHE   B  1  501  ? -21.291 25.079  108.631 1.00 40.42 ? 499  PHE   B CD1   1 
ATOM   12690 C  CD2   . PHE   B  1  501  ? -22.503 24.531  106.655 1.00 33.88 ? 499  PHE   B CD2   1 
ATOM   12691 C  CE1   . PHE   B  1  501  ? -22.432 24.850  109.394 1.00 38.22 ? 499  PHE   B CE1   1 
ATOM   12692 C  CE2   . PHE   B  1  501  ? -23.643 24.299  107.411 1.00 39.73 ? 499  PHE   B CE2   1 
ATOM   12693 C  CZ    . PHE   B  1  501  ? -23.605 24.459  108.781 1.00 38.98 ? 499  PHE   B CZ    1 
ATOM   12694 N  N     . VAL   B  1  502  ? -18.141 27.508  107.573 1.00 43.66 ? 500  VAL   B N     1 
ATOM   12695 C  CA    . VAL   B  1  502  ? -17.660 28.260  108.733 1.00 47.42 ? 500  VAL   B CA    1 
ATOM   12696 C  C     . VAL   B  1  502  ? -18.047 29.732  108.627 1.00 50.11 ? 500  VAL   B C     1 
ATOM   12697 O  O     . VAL   B  1  502  ? -18.409 30.369  109.624 1.00 51.83 ? 500  VAL   B O     1 
ATOM   12698 C  CB    . VAL   B  1  502  ? -16.141 28.070  108.909 1.00 42.81 ? 500  VAL   B CB    1 
ATOM   12699 N  N     . HIS   B  1  503  ? -17.982 30.294  107.419 1.00 42.68 ? 501  HIS   B N     1 
ATOM   12700 C  CA    . HIS   B  1  503  ? -18.394 31.676  107.212 1.00 44.47 ? 501  HIS   B CA    1 
ATOM   12701 C  C     . HIS   B  1  503  ? -19.901 31.804  107.022 1.00 48.75 ? 501  HIS   B C     1 
ATOM   12702 O  O     . HIS   B  1  503  ? -20.498 32.786  107.477 1.00 45.44 ? 501  HIS   B O     1 
ATOM   12703 C  CB    . HIS   B  1  503  ? -17.646 32.263  106.011 1.00 44.76 ? 501  HIS   B CB    1 
ATOM   12704 C  CG    . HIS   B  1  503  ? -18.262 33.510  105.455 1.00 45.13 ? 501  HIS   B CG    1 
ATOM   12705 N  ND1   . HIS   B  1  503  ? -19.270 33.486  104.515 1.00 47.36 ? 501  HIS   B ND1   1 
ATOM   12706 C  CD2   . HIS   B  1  503  ? -17.998 34.817  105.689 1.00 46.08 ? 501  HIS   B CD2   1 
ATOM   12707 C  CE1   . HIS   B  1  503  ? -19.609 34.724  104.204 1.00 49.22 ? 501  HIS   B CE1   1 
ATOM   12708 N  NE2   . HIS   B  1  503  ? -18.851 35.551  104.902 1.00 48.46 ? 501  HIS   B NE2   1 
ATOM   12709 N  N     . ARG   B  1  504  ? -20.532 30.818  106.379 1.00 43.12 ? 502  ARG   B N     1 
ATOM   12710 C  CA    . ARG   B  1  504  ? -21.931 30.957  105.992 1.00 40.56 ? 502  ARG   B CA    1 
ATOM   12711 C  C     . ARG   B  1  504  ? -22.877 30.806  107.175 1.00 42.73 ? 502  ARG   B C     1 
ATOM   12712 O  O     . ARG   B  1  504  ? -23.937 31.441  107.199 1.00 43.41 ? 502  ARG   B O     1 
ATOM   12713 C  CB    . ARG   B  1  504  ? -22.270 29.957  104.888 1.00 38.78 ? 502  ARG   B CB    1 
ATOM   12714 C  CG    . ARG   B  1  504  ? -21.645 30.318  103.551 1.00 40.98 ? 502  ARG   B CG    1 
ATOM   12715 C  CD    . ARG   B  1  504  ? -21.621 29.139  102.587 1.00 36.13 ? 502  ARG   B CD    1 
ATOM   12716 N  NE    . ARG   B  1  504  ? -22.941 28.574  102.345 1.00 35.47 ? 502  ARG   B NE    1 
ATOM   12717 C  CZ    . ARG   B  1  504  ? -23.884 29.157  101.617 1.00 38.01 ? 502  ARG   B CZ    1 
ATOM   12718 N  NH1   . ARG   B  1  504  ? -23.710 30.360  101.093 1.00 36.81 ? 502  ARG   B NH1   1 
ATOM   12719 N  NH2   . ARG   B  1  504  ? -25.029 28.515  101.405 1.00 36.97 ? 502  ARG   B NH2   1 
ATOM   12720 N  N     . ILE   B  1  505  ? -22.526 29.966  108.152 1.00 40.27 ? 503  ILE   B N     1 
ATOM   12721 C  CA    . ILE   B  1  505  ? -23.381 29.799  109.324 1.00 43.49 ? 503  ILE   B CA    1 
ATOM   12722 C  C     . ILE   B  1  505  ? -23.545 31.117  110.071 1.00 46.61 ? 503  ILE   B C     1 
ATOM   12723 O  O     . ILE   B  1  505  ? -24.594 31.371  110.678 1.00 43.30 ? 503  ILE   B O     1 
ATOM   12724 C  CB    . ILE   B  1  505  ? -22.845 28.669  110.227 1.00 43.45 ? 503  ILE   B CB    1 
ATOM   12725 N  N     . ASN   B  1  506  ? -22.533 31.983  110.020 1.00 45.06 ? 504  ASN   B N     1 
ATOM   12726 C  CA    . ASN   B  1  506  ? -22.553 33.262  110.715 1.00 50.76 ? 504  ASN   B CA    1 
ATOM   12727 C  C     . ASN   B  1  506  ? -22.959 34.426  109.821 1.00 51.22 ? 504  ASN   B C     1 
ATOM   12728 O  O     . ASN   B  1  506  ? -22.921 35.576  110.267 1.00 51.99 ? 504  ASN   B O     1 
ATOM   12729 C  CB    . ASN   B  1  506  ? -21.198 33.535  111.370 1.00 50.38 ? 504  ASN   B CB    1 
ATOM   12730 C  CG    . ASN   B  1  506  ? -20.958 32.663  112.583 1.00 51.63 ? 504  ASN   B CG    1 
ATOM   12731 O  OD1   . ASN   B  1  506  ? -21.865 32.433  113.383 1.00 51.61 ? 504  ASN   B OD1   1 
ATOM   12732 N  ND2   . ASN   B  1  506  ? -19.736 32.162  112.722 1.00 55.48 ? 504  ASN   B ND2   1 
ATOM   12733 N  N     . ASP   B  1  507  ? -23.347 34.160  108.576 1.00 46.17 ? 505  ASP   B N     1 
ATOM   12734 C  CA    . ASP   B  1  507  ? -23.808 35.218  107.692 1.00 49.69 ? 505  ASP   B CA    1 
ATOM   12735 C  C     . ASP   B  1  507  ? -25.327 35.241  107.732 1.00 54.96 ? 505  ASP   B C     1 
ATOM   12736 O  O     . ASP   B  1  507  ? -25.964 34.301  107.229 1.00 51.45 ? 505  ASP   B O     1 
ATOM   12737 C  CB    . ASP   B  1  507  ? -23.317 34.973  106.267 1.00 51.12 ? 505  ASP   B CB    1 
ATOM   12738 C  CG    . ASP   B  1  507  ? -23.298 36.238  105.432 1.00 55.18 ? 505  ASP   B CG    1 
ATOM   12739 O  OD1   . ASP   B  1  507  ? -24.172 37.106  105.641 1.00 61.34 ? 505  ASP   B OD1   1 
ATOM   12740 O  OD2   . ASP   B  1  507  ? -22.403 36.368  104.571 1.00 64.61 ? 505  ASP   B OD2   1 
ATOM   12741 N  N     . PRO   B  1  508  ? -25.952 36.268  108.318 1.00 57.86 ? 506  PRO   B N     1 
ATOM   12742 C  CA    . PRO   B  1  508  ? -27.421 36.277  108.410 1.00 54.28 ? 506  PRO   B CA    1 
ATOM   12743 C  C     . PRO   B  1  508  ? -28.113 36.372  107.065 1.00 56.23 ? 506  PRO   B C     1 
ATOM   12744 O  O     . PRO   B  1  508  ? -29.302 36.039  106.975 1.00 61.28 ? 506  PRO   B O     1 
ATOM   12745 C  CB    . PRO   B  1  508  ? -27.719 37.507  109.282 1.00 61.61 ? 506  PRO   B CB    1 
ATOM   12746 C  CG    . PRO   B  1  508  ? -26.411 37.862  109.931 1.00 60.94 ? 506  PRO   B CG    1 
ATOM   12747 C  CD    . PRO   B  1  508  ? -25.353 37.449  108.958 1.00 54.54 ? 506  PRO   B CD    1 
ATOM   12748 N  N     . LYS   B  1  509  ? -27.413 36.816  106.020 1.00 57.21 ? 507  LYS   B N     1 
ATOM   12749 C  CA    . LYS   B  1  509  ? -27.977 36.866  104.678 1.00 56.39 ? 507  LYS   B CA    1 
ATOM   12750 C  C     . LYS   B  1  509  ? -28.167 35.486  104.064 1.00 60.25 ? 507  LYS   B C     1 
ATOM   12751 O  O     . LYS   B  1  509  ? -28.710 35.391  102.957 1.00 65.03 ? 507  LYS   B O     1 
ATOM   12752 C  CB    . LYS   B  1  509  ? -27.094 37.728  103.772 1.00 50.68 ? 507  LYS   B CB    1 
ATOM   12753 N  N     . VAL   B  1  510  ? -27.740 34.427  104.745 1.00 59.85 ? 508  VAL   B N     1 
ATOM   12754 C  CA    . VAL   B  1  510  ? -27.878 33.057  104.266 1.00 55.17 ? 508  VAL   B CA    1 
ATOM   12755 C  C     . VAL   B  1  510  ? -28.891 32.354  105.155 1.00 53.70 ? 508  VAL   B C     1 
ATOM   12756 O  O     . VAL   B  1  510  ? -28.715 32.291  106.378 1.00 57.62 ? 508  VAL   B O     1 
ATOM   12757 C  CB    . VAL   B  1  510  ? -26.530 32.320  104.278 1.00 50.76 ? 508  VAL   B CB    1 
ATOM   12758 C  CG1   . VAL   B  1  510  ? -26.675 30.942  103.648 1.00 52.51 ? 508  VAL   B CG1   1 
ATOM   12759 C  CG2   . VAL   B  1  510  ? -25.467 33.145  103.565 1.00 48.48 ? 508  VAL   B CG2   1 
ATOM   12760 N  N     . SER   B  1  511  ? -29.948 31.826  104.548 1.00 51.47 ? 509  SER   B N     1 
ATOM   12761 C  CA    . SER   B  1  511  ? -30.995 31.166  105.310 1.00 53.65 ? 509  SER   B CA    1 
ATOM   12762 C  C     . SER   B  1  511  ? -30.586 29.739  105.652 1.00 53.51 ? 509  SER   B C     1 
ATOM   12763 O  O     . SER   B  1  511  ? -29.654 29.174  105.071 1.00 52.35 ? 509  SER   B O     1 
ATOM   12764 C  CB    . SER   B  1  511  ? -32.294 31.124  104.506 1.00 55.17 ? 509  SER   B CB    1 
ATOM   12765 O  OG    . SER   B  1  511  ? -32.193 30.217  103.422 1.00 53.21 ? 509  SER   B OG    1 
ATOM   12766 N  N     . ILE   B  1  512  ? -31.304 29.155  106.614 1.00 49.18 ? 510  ILE   B N     1 
ATOM   12767 C  CA    . ILE   B  1  512  ? -31.131 27.736  106.891 1.00 49.75 ? 510  ILE   B CA    1 
ATOM   12768 C  C     . ILE   B  1  512  ? -31.575 26.889  105.704 1.00 53.31 ? 510  ILE   B C     1 
ATOM   12769 O  O     . ILE   B  1  512  ? -31.087 25.767  105.530 1.00 50.50 ? 510  ILE   B O     1 
ATOM   12770 C  CB    . ILE   B  1  512  ? -31.821 27.320  108.204 1.00 40.09 ? 510  ILE   B CB    1 
ATOM   12771 N  N     . ASP   B  1  513  ? -32.482 27.407  104.871 1.00 49.64 ? 511  ASP   B N     1 
ATOM   12772 C  CA    . ASP   B  1  513  ? -32.878 26.688  103.665 1.00 48.97 ? 511  ASP   B CA    1 
ATOM   12773 C  C     . ASP   B  1  513  ? -31.707 26.550  102.699 1.00 43.91 ? 511  ASP   B C     1 
ATOM   12774 O  O     . ASP   B  1  513  ? -31.465 25.466  102.156 1.00 43.92 ? 511  ASP   B O     1 
ATOM   12775 C  CB    . ASP   B  1  513  ? -34.058 27.389  102.987 1.00 50.82 ? 511  ASP   B CB    1 
ATOM   12776 C  CG    . ASP   B  1  513  ? -35.391 27.043  103.626 1.00 52.31 ? 511  ASP   B CG    1 
ATOM   12777 O  OD1   . ASP   B  1  513  ? -35.497 25.970  104.260 1.00 52.16 ? 511  ASP   B OD1   1 
ATOM   12778 O  OD2   . ASP   B  1  513  ? -36.340 27.844  103.485 1.00 59.66 ? 511  ASP   B OD2   1 
ATOM   12779 N  N     . GLU   B  1  514  ? -30.974 27.642  102.467 1.00 43.88 ? 512  GLU   B N     1 
ATOM   12780 C  CA    . GLU   B  1  514  ? -29.805 27.571  101.595 1.00 48.47 ? 512  GLU   B CA    1 
ATOM   12781 C  C     . GLU   B  1  514  ? -28.754 26.625  102.162 1.00 43.68 ? 512  GLU   B C     1 
ATOM   12782 O  O     . GLU   B  1  514  ? -28.072 25.918  101.412 1.00 41.63 ? 512  GLU   B O     1 
ATOM   12783 C  CB    . GLU   B  1  514  ? -29.206 28.964  101.399 1.00 44.71 ? 512  GLU   B CB    1 
ATOM   12784 C  CG    . GLU   B  1  514  ? -30.190 30.015  100.917 1.00 54.51 ? 512  GLU   B CG    1 
ATOM   12785 C  CD    . GLU   B  1  514  ? -29.558 31.390  100.806 1.00 56.71 ? 512  GLU   B CD    1 
ATOM   12786 O  OE1   . GLU   B  1  514  ? -28.457 31.492  100.226 1.00 63.53 ? 512  GLU   B OE1   1 
ATOM   12787 O  OE2   . GLU   B  1  514  ? -30.155 32.367  101.310 1.00 60.13 ? 512  GLU   B OE2   1 
ATOM   12788 N  N     . LEU   B  1  515  ? -28.616 26.591  103.488 1.00 42.17 ? 513  LEU   B N     1 
ATOM   12789 C  CA    . LEU   B  1  515  ? -27.574 25.773  104.099 1.00 41.77 ? 513  LEU   B CA    1 
ATOM   12790 C  C     . LEU   B  1  515  ? -27.905 24.288  104.036 1.00 38.49 ? 513  LEU   B C     1 
ATOM   12791 O  O     . LEU   B  1  515  ? -26.994 23.454  104.030 1.00 38.88 ? 513  LEU   B O     1 
ATOM   12792 C  CB    . LEU   B  1  515  ? -27.342 26.215  105.545 1.00 37.04 ? 513  LEU   B CB    1 
ATOM   12793 C  CG    . LEU   B  1  515  ? -26.729 27.602  105.741 1.00 34.85 ? 513  LEU   B CG    1 
ATOM   12794 C  CD1   . LEU   B  1  515  ? -26.756 27.957  107.222 1.00 42.24 ? 513  LEU   B CD1   1 
ATOM   12795 C  CD2   . LEU   B  1  515  ? -25.305 27.656  105.204 1.00 36.73 ? 513  LEU   B CD2   1 
ATOM   12796 N  N     . ILE   B  1  516  ? -29.189 23.937  103.994 1.00 35.91 ? 514  ILE   B N     1 
ATOM   12797 C  CA    . ILE   B  1  516  ? -29.611 22.543  103.936 1.00 32.68 ? 514  ILE   B CA    1 
ATOM   12798 C  C     . ILE   B  1  516  ? -29.860 22.074  102.508 1.00 32.94 ? 514  ILE   B C     1 
ATOM   12799 O  O     . ILE   B  1  516  ? -30.290 20.936  102.305 1.00 36.02 ? 514  ILE   B O     1 
ATOM   12800 C  CB    . ILE   B  1  516  ? -30.819 22.257  104.845 1.00 38.02 ? 514  ILE   B CB    1 
ATOM   12801 C  CG1   . ILE   B  1  516  ? -32.080 22.929  104.279 1.00 37.70 ? 514  ILE   B CG1   1 
ATOM   12802 C  CG2   . ILE   B  1  516  ? -30.544 22.729  106.267 1.00 38.84 ? 514  ILE   B CG2   1 
ATOM   12803 C  CD1   . ILE   B  1  516  ? -33.329 22.712  105.128 1.00 39.25 ? 514  ILE   B CD1   1 
ATOM   12804 N  N     . ALA   B  1  517  ? -29.612 22.929  101.520 1.00 37.75 ? 515  ALA   B N     1 
ATOM   12805 C  CA    . ALA   B  1  517  ? -29.716 22.517  100.128 1.00 39.29 ? 515  ALA   B CA    1 
ATOM   12806 C  C     . ALA   B  1  517  ? -28.836 21.300  99.874  1.00 34.98 ? 515  ALA   B C     1 
ATOM   12807 O  O     . ALA   B  1  517  ? -27.682 21.243  100.308 1.00 34.52 ? 515  ALA   B O     1 
ATOM   12808 C  CB    . ALA   B  1  517  ? -29.278 23.659  99.214  1.00 33.78 ? 515  ALA   B CB    1 
ATOM   12809 N  N     . ASP   B  1  518  ? -29.397 20.319  99.172  1.00 33.89 ? 516  ASP   B N     1 
ATOM   12810 C  CA    . ASP   B  1  518  ? -28.725 19.064  98.879  1.00 34.95 ? 516  ASP   B CA    1 
ATOM   12811 C  C     . ASP   B  1  518  ? -27.812 19.263  97.674  1.00 29.48 ? 516  ASP   B C     1 
ATOM   12812 O  O     . ASP   B  1  518  ? -28.295 19.423  96.546  1.00 31.60 ? 516  ASP   B O     1 
ATOM   12813 C  CB    . ASP   B  1  518  ? -29.761 17.969  98.615  1.00 32.39 ? 516  ASP   B CB    1 
ATOM   12814 C  CG    . ASP   B  1  518  ? -29.135 16.593  98.416  1.00 37.19 ? 516  ASP   B CG    1 
ATOM   12815 O  OD1   . ASP   B  1  518  ? -27.888 16.486  98.339  1.00 31.77 ? 516  ASP   B OD1   1 
ATOM   12816 O  OD2   . ASP   B  1  518  ? -29.897 15.607  98.333  1.00 38.41 ? 516  ASP   B OD2   1 
ATOM   12817 N  N     . PRO   B  1  519  ? -26.492 19.259  97.871  1.00 26.02 ? 517  PRO   B N     1 
ATOM   12818 C  CA    . PRO   B  1  519  ? -25.584 19.439  96.731  1.00 28.86 ? 517  PRO   B CA    1 
ATOM   12819 C  C     . PRO   B  1  519  ? -25.788 18.404  95.642  1.00 28.08 ? 517  PRO   B C     1 
ATOM   12820 O  O     . PRO   B  1  519  ? -25.638 18.726  94.457  1.00 27.31 ? 517  PRO   B O     1 
ATOM   12821 C  CB    . PRO   B  1  519  ? -24.189 19.339  97.369  1.00 28.65 ? 517  PRO   B CB    1 
ATOM   12822 C  CG    . PRO   B  1  519  ? -24.401 18.610  98.645  1.00 30.77 ? 517  PRO   B CG    1 
ATOM   12823 C  CD    . PRO   B  1  519  ? -25.776 18.980  99.126  1.00 25.75 ? 517  PRO   B CD    1 
ATOM   12824 N  N     . VAL   B  1  520  ? -26.146 17.173  96.014  1.00 27.90 ? 518  VAL   B N     1 
ATOM   12825 C  CA    . VAL   B  1  520  ? -26.339 16.112  95.029  1.00 28.61 ? 518  VAL   B CA    1 
ATOM   12826 C  C     . VAL   B  1  520  ? -27.465 16.471  94.067  1.00 30.49 ? 518  VAL   B C     1 
ATOM   12827 O  O     . VAL   B  1  520  ? -27.314 16.379  92.841  1.00 28.72 ? 518  VAL   B O     1 
ATOM   12828 C  CB    . VAL   B  1  520  ? -26.591 14.767  95.730  1.00 30.17 ? 518  VAL   B CB    1 
ATOM   12829 C  CG1   . VAL   B  1  520  ? -26.646 13.639  94.708  1.00 32.81 ? 518  VAL   B CG1   1 
ATOM   12830 C  CG2   . VAL   B  1  520  ? -25.528 14.514  96.790  1.00 29.06 ? 518  VAL   B CG2   1 
ATOM   12831 N  N     . GLU   B  1  521  ? -28.607 16.899  94.606  1.00 29.45 ? 519  GLU   B N     1 
ATOM   12832 C  CA    . GLU   B  1  521  ? -29.729 17.243  93.741  1.00 31.10 ? 519  GLU   B CA    1 
ATOM   12833 C  C     . GLU   B  1  521  ? -29.485 18.536  92.978  1.00 31.17 ? 519  GLU   B C     1 
ATOM   12834 O  O     . GLU   B  1  521  ? -29.948 18.676  91.839  1.00 31.91 ? 519  GLU   B O     1 
ATOM   12835 C  CB    . GLU   B  1  521  ? -31.025 17.298  94.548  1.00 32.78 ? 519  GLU   B CB    1 
ATOM   12836 C  CG    . GLU   B  1  521  ? -31.397 15.960  95.147  1.00 34.46 ? 519  GLU   B CG    1 
ATOM   12837 C  CD    . GLU   B  1  521  ? -31.447 14.842  94.112  1.00 39.16 ? 519  GLU   B CD    1 
ATOM   12838 O  OE1   . GLU   B  1  521  ? -31.799 15.112  92.943  1.00 39.53 ? 519  GLU   B OE1   1 
ATOM   12839 O  OE2   . GLU   B  1  521  ? -31.136 13.686  94.472  1.00 45.12 ? 519  GLU   B OE2   1 
ATOM   12840 N  N     . VAL   B  1  522  ? -28.760 19.483  93.568  1.00 30.64 ? 520  VAL   B N     1 
ATOM   12841 C  CA    . VAL   B  1  522  ? -28.440 20.701  92.836  1.00 29.64 ? 520  VAL   B CA    1 
ATOM   12842 C  C     . VAL   B  1  522  ? -27.535 20.392  91.650  1.00 34.68 ? 520  VAL   B C     1 
ATOM   12843 O  O     . VAL   B  1  522  ? -27.767 20.877  90.535  1.00 32.29 ? 520  VAL   B O     1 
ATOM   12844 C  CB    . VAL   B  1  522  ? -27.856 21.774  93.772  1.00 32.39 ? 520  VAL   B CB    1 
ATOM   12845 C  CG1   . VAL   B  1  522  ? -27.476 23.013  92.982  1.00 33.51 ? 520  VAL   B CG1   1 
ATOM   12846 C  CG2   . VAL   B  1  522  ? -28.862 22.125  94.857  1.00 38.90 ? 520  VAL   B CG2   1 
ATOM   12847 N  N     . VAL   B  1  523  ? -26.509 19.559  91.859  1.00 28.31 ? 521  VAL   B N     1 
ATOM   12848 C  CA    . VAL   B  1  523  ? -25.628 19.180  90.757  1.00 26.72 ? 521  VAL   B CA    1 
ATOM   12849 C  C     . VAL   B  1  523  ? -26.389 18.388  89.701  1.00 27.81 ? 521  VAL   B C     1 
ATOM   12850 O  O     . VAL   B  1  523  ? -26.216 18.608  88.495  1.00 27.45 ? 521  VAL   B O     1 
ATOM   12851 C  CB    . VAL   B  1  523  ? -24.393 18.416  91.272  1.00 29.14 ? 521  VAL   B CB    1 
ATOM   12852 C  CG1   . VAL   B  1  523  ? -23.656 17.767  90.115  1.00 27.23 ? 521  VAL   B CG1   1 
ATOM   12853 C  CG2   . VAL   B  1  523  ? -23.467 19.353  92.033  1.00 31.09 ? 521  VAL   B CG2   1 
ATOM   12854 N  N     . ARG   B  1  524  ? -27.226 17.443  90.133  1.00 29.29 ? 522  ARG   B N     1 
ATOM   12855 C  CA    . ARG   B  1  524  ? -27.963 16.619  89.181  1.00 33.53 ? 522  ARG   B CA    1 
ATOM   12856 C  C     . ARG   B  1  524  ? -28.799 17.468  88.231  1.00 32.79 ? 522  ARG   B C     1 
ATOM   12857 O  O     . ARG   B  1  524  ? -28.969 17.108  87.060  1.00 34.79 ? 522  ARG   B O     1 
ATOM   12858 C  CB    . ARG   B  1  524  ? -28.857 15.636  89.930  1.00 31.75 ? 522  ARG   B CB    1 
ATOM   12859 C  CG    . ARG   B  1  524  ? -29.617 14.696  89.023  1.00 33.62 ? 522  ARG   B CG    1 
ATOM   12860 C  CD    . ARG   B  1  524  ? -30.796 14.070  89.744  1.00 35.63 ? 522  ARG   B CD    1 
ATOM   12861 N  NE    . ARG   B  1  524  ? -30.414 13.543  91.047  1.00 35.91 ? 522  ARG   B NE    1 
ATOM   12862 C  CZ    . ARG   B  1  524  ? -29.752 12.408  91.231  1.00 38.60 ? 522  ARG   B CZ    1 
ATOM   12863 N  NH1   . ARG   B  1  524  ? -29.360 11.662  90.209  1.00 38.04 ? 522  ARG   B NH1   1 
ATOM   12864 N  NH2   . ARG   B  1  524  ? -29.472 12.013  92.471  1.00 37.10 ? 522  ARG   B NH2   1 
ATOM   12865 N  N     . ALA   B  1  525  ? -29.302 18.604  88.703  1.00 30.89 ? 523  ALA   B N     1 
ATOM   12866 C  CA    . ALA   B  1  525  ? -30.224 19.422  87.928  1.00 35.91 ? 523  ALA   B CA    1 
ATOM   12867 C  C     . ALA   B  1  525  ? -29.530 20.487  87.094  1.00 37.15 ? 523  ALA   B C     1 
ATOM   12868 O  O     . ALA   B  1  525  ? -30.213 21.240  86.392  1.00 37.39 ? 523  ALA   B O     1 
ATOM   12869 C  CB    . ALA   B  1  525  ? -31.268 20.067  88.847  1.00 37.00 ? 523  ALA   B CB    1 
ATOM   12870 N  N     . MET   B  1  526  ? -28.203 20.570  87.148  1.00 34.09 ? 524  MET   B N     1 
ATOM   12871 C  CA    A MET   B  1  526  ? -27.482 21.542  86.344  0.53 35.42 ? 524  MET   B CA    1 
ATOM   12872 C  CA    B MET   B  1  526  ? -27.495 21.548  86.344  0.47 35.43 ? 524  MET   B CA    1 
ATOM   12873 C  C     . MET   B  1  526  ? -27.553 21.152  84.869  1.00 33.82 ? 524  MET   B C     1 
ATOM   12874 O  O     . MET   B  1  526  ? -27.621 19.966  84.536  1.00 34.01 ? 524  MET   B O     1 
ATOM   12875 C  CB    A MET   B  1  526  ? -26.022 21.605  86.782  0.53 36.52 ? 524  MET   B CB    1 
ATOM   12876 C  CB    B MET   B  1  526  ? -26.044 21.657  86.802  0.47 36.54 ? 524  MET   B CB    1 
ATOM   12877 C  CG    A MET   B  1  526  ? -25.827 22.222  88.153  0.53 39.07 ? 524  MET   B CG    1 
ATOM   12878 C  CG    B MET   B  1  526  ? -25.838 22.680  87.908  0.47 39.53 ? 524  MET   B CG    1 
ATOM   12879 S  SD    A MET   B  1  526  ? -26.475 23.904  88.229  0.53 42.50 ? 524  MET   B SD    1 
ATOM   12880 S  SD    B MET   B  1  526  ? -24.235 22.536  88.712  0.47 41.34 ? 524  MET   B SD    1 
ATOM   12881 C  CE    A MET   B  1  526  ? -25.401 24.744  87.066  0.53 38.78 ? 524  MET   B CE    1 
ATOM   12882 C  CE    B MET   B  1  526  ? -24.019 24.191  89.359  0.47 42.97 ? 524  MET   B CE    1 
ATOM   12883 N  N     . PRO   B  1  527  ? -27.546 22.135  83.962  1.00 35.65 ? 525  PRO   B N     1 
ATOM   12884 C  CA    . PRO   B  1  527  ? -27.658 21.795  82.532  1.00 41.61 ? 525  PRO   B CA    1 
ATOM   12885 C  C     . PRO   B  1  527  ? -26.523 20.918  82.040  1.00 38.91 ? 525  PRO   B C     1 
ATOM   12886 O  O     . PRO   B  1  527  ? -26.753 19.979  81.266  1.00 34.59 ? 525  PRO   B O     1 
ATOM   12887 C  CB    . PRO   B  1  527  ? -27.679 23.167  81.845  1.00 43.20 ? 525  PRO   B CB    1 
ATOM   12888 C  CG    . PRO   B  1  527  ? -26.996 24.078  82.808  1.00 45.50 ? 525  PRO   B CG    1 
ATOM   12889 C  CD    . PRO   B  1  527  ? -27.373 23.583  84.172  1.00 42.99 ? 525  PRO   B CD    1 
ATOM   12890 N  N     . VAL   B  1  528  ? -25.301 21.192  82.482  1.00 34.42 ? 526  VAL   B N     1 
ATOM   12891 C  CA    . VAL   B  1  528  ? -24.142 20.365  82.184  1.00 31.13 ? 526  VAL   B CA    1 
ATOM   12892 C  C     . VAL   B  1  528  ? -23.606 19.886  83.524  1.00 27.74 ? 526  VAL   B C     1 
ATOM   12893 O  O     . VAL   B  1  528  ? -22.971 20.657  84.256  1.00 31.43 ? 526  VAL   B O     1 
ATOM   12894 C  CB    . VAL   B  1  528  ? -23.067 21.139  81.410  1.00 30.11 ? 526  VAL   B CB    1 
ATOM   12895 C  CG1   . VAL   B  1  528  ? -21.827 20.274  81.213  1.00 28.69 ? 526  VAL   B CG1   1 
ATOM   12896 C  CG2   . VAL   B  1  528  ? -23.615 21.605  80.072  1.00 31.35 ? 526  VAL   B CG2   1 
ATOM   12897 N  N     . VAL   B  1  529  ? -23.861 18.623  83.850  1.00 27.35 ? 527  VAL   B N     1 
ATOM   12898 C  CA    . VAL   B  1  529  ? -23.427 18.104  85.140  1.00 26.35 ? 527  VAL   B CA    1 
ATOM   12899 C  C     . VAL   B  1  529  ? -21.909 18.153  85.216  1.00 26.03 ? 527  VAL   B C     1 
ATOM   12900 O  O     . VAL   B  1  529  ? -21.205 17.638  84.338  1.00 26.72 ? 527  VAL   B O     1 
ATOM   12901 C  CB    . VAL   B  1  529  ? -23.963 16.693  85.366  1.00 23.20 ? 527  VAL   B CB    1 
ATOM   12902 C  CG1   . VAL   B  1  529  ? -23.350 16.098  86.615  1.00 23.32 ? 527  VAL   B CG1   1 
ATOM   12903 C  CG2   . VAL   B  1  529  ? -25.488 16.713  85.482  1.00 26.08 ? 527  VAL   B CG2   1 
ATOM   12904 N  N     . GLY   B  1  530  ? -21.397 18.796  86.260  1.00 23.21 ? 528  GLY   B N     1 
ATOM   12905 C  CA    . GLY   B  1  530  ? -19.970 18.818  86.486  1.00 24.10 ? 528  GLY   B CA    1 
ATOM   12906 C  C     . GLY   B  1  530  ? -19.198 19.843  85.692  1.00 22.07 ? 528  GLY   B C     1 
ATOM   12907 O  O     . GLY   B  1  530  ? -17.981 19.717  85.580  1.00 21.37 ? 528  GLY   B O     1 
ATOM   12908 N  N     . ALA   B  1  531  ? -19.858 20.854  85.134  1.00 22.03 ? 529  ALA   B N     1 
ATOM   12909 C  CA    . ALA   B  1  531  ? -19.137 21.889  84.410  1.00 20.80 ? 529  ALA   B CA    1 
ATOM   12910 C  C     . ALA   B  1  531  ? -18.186 22.617  85.347  1.00 20.40 ? 529  ALA   B C     1 
ATOM   12911 O  O     . ALA   B  1  531  ? -18.510 22.869  86.512  1.00 23.21 ? 529  ALA   B O     1 
ATOM   12912 C  CB    . ALA   B  1  531  ? -20.117 22.889  83.797  1.00 26.50 ? 529  ALA   B CB    1 
ATOM   12913 N  N     . LYS   B  1  532  ? -17.002 22.936  84.831  1.00 19.37 ? 530  LYS   B N     1 
ATOM   12914 C  CA    . LYS   B  1  532  ? -16.021 23.713  85.576  1.00 21.10 ? 530  LYS   B CA    1 
ATOM   12915 C  C     . LYS   B  1  532  ? -16.635 25.037  86.017  1.00 20.39 ? 530  LYS   B C     1 
ATOM   12916 O  O     . LYS   B  1  532  ? -17.560 25.561  85.387  1.00 21.37 ? 530  LYS   B O     1 
ATOM   12917 C  CB    . LYS   B  1  532  ? -14.813 23.971  84.666  1.00 22.90 ? 530  LYS   B CB    1 
ATOM   12918 C  CG    . LYS   B  1  532  ? -13.761 24.942  85.184  1.00 23.51 ? 530  LYS   B CG    1 
ATOM   12919 C  CD    . LYS   B  1  532  ? -12.709 25.223  84.115  1.00 23.45 ? 530  LYS   B CD    1 
ATOM   12920 C  CE    . LYS   B  1  532  ? -13.260 26.030  82.943  1.00 21.69 ? 530  LYS   B CE    1 
ATOM   12921 N  NZ    . LYS   B  1  532  ? -13.687 27.410  83.335  1.00 21.96 ? 530  LYS   B NZ    1 
ATOM   12922 N  N     . HIS   B  1  533  ? -16.127 25.570  87.120  1.00 18.41 ? 531  HIS   B N     1 
ATOM   12923 C  CA    . HIS   B  1  533  ? -16.510 26.909  87.538  1.00 20.17 ? 531  HIS   B CA    1 
ATOM   12924 C  C     . HIS   B  1  533  ? -16.309 27.892  86.392  1.00 20.19 ? 531  HIS   B C     1 
ATOM   12925 O  O     . HIS   B  1  533  ? -15.263 27.903  85.739  1.00 20.76 ? 531  HIS   B O     1 
ATOM   12926 C  CB    . HIS   B  1  533  ? -15.647 27.315  88.726  1.00 19.85 ? 531  HIS   B CB    1 
ATOM   12927 C  CG    . HIS   B  1  533  ? -16.206 28.449  89.519  1.00 23.55 ? 531  HIS   B CG    1 
ATOM   12928 N  ND1   . HIS   B  1  533  ? -16.322 29.724  89.012  1.00 22.78 ? 531  HIS   B ND1   1 
ATOM   12929 C  CD2   . HIS   B  1  533  ? -16.679 28.501  90.786  1.00 28.59 ? 531  HIS   B CD2   1 
ATOM   12930 C  CE1   . HIS   B  1  533  ? -16.860 30.511  89.928  1.00 28.69 ? 531  HIS   B CE1   1 
ATOM   12931 N  NE2   . HIS   B  1  533  ? -17.081 29.794  91.015  1.00 36.15 ? 531  HIS   B NE2   1 
ATOM   12932 N  N     . ASP   B  1  534  ? -17.329 28.720  86.153  1.00 21.83 ? 532  ASP   B N     1 
ATOM   12933 C  CA    . ASP   B  1  534  ? -17.278 29.698  85.071  1.00 24.62 ? 532  ASP   B CA    1 
ATOM   12934 C  C     . ASP   B  1  534  ? -16.169 30.724  85.248  1.00 24.54 ? 532  ASP   B C     1 
ATOM   12935 O  O     . ASP   B  1  534  ? -15.728 31.321  84.261  1.00 26.55 ? 532  ASP   B O     1 
ATOM   12936 C  CB    . ASP   B  1  534  ? -18.614 30.445  84.986  1.00 27.40 ? 532  ASP   B CB    1 
ATOM   12937 C  CG    . ASP   B  1  534  ? -19.718 29.595  84.414  1.00 40.78 ? 532  ASP   B CG    1 
ATOM   12938 O  OD1   . ASP   B  1  534  ? -19.433 28.809  83.485  1.00 44.91 ? 532  ASP   B OD1   1 
ATOM   12939 O  OD2   . ASP   B  1  534  ? -20.867 29.714  84.892  1.00 49.83 ? 532  ASP   B OD2   1 
ATOM   12940 N  N     . ARG   B  1  535  ? -15.712 30.955  86.474  1.00 19.85 ? 533  ARG   B N     1 
ATOM   12941 C  CA    . ARG   B  1  535  ? -14.789 32.044  86.751  1.00 22.31 ? 533  ARG   B CA    1 
ATOM   12942 C  C     . ARG   B  1  535  ? -13.386 31.555  87.073  1.00 22.77 ? 533  ARG   B C     1 
ATOM   12943 O  O     . ARG   B  1  535  ? -12.571 32.333  87.571  1.00 23.89 ? 533  ARG   B O     1 
ATOM   12944 C  CB    . ARG   B  1  535  ? -15.330 32.922  87.881  1.00 26.42 ? 533  ARG   B CB    1 
ATOM   12945 N  N     . ILE   B  1  536  ? -13.096 30.283  86.820  1.00 18.96 ? 534  ILE   B N     1 
ATOM   12946 C  CA    . ILE   B  1  536  ? -11.767 29.715  87.010  1.00 16.70 ? 534  ILE   B CA    1 
ATOM   12947 C  C     . ILE   B  1  536  ? -11.313 29.169  85.670  1.00 17.31 ? 534  ILE   B C     1 
ATOM   12948 O  O     . ILE   B  1  536  ? -11.954 28.271  85.110  1.00 19.78 ? 534  ILE   B O     1 
ATOM   12949 C  CB    . ILE   B  1  536  ? -11.767 28.612  88.073  1.00 17.62 ? 534  ILE   B CB    1 
ATOM   12950 C  CG1   . ILE   B  1  536  ? -12.218 29.193  89.412  1.00 18.89 ? 534  ILE   B CG1   1 
ATOM   12951 C  CG2   . ILE   B  1  536  ? -10.363 28.014  88.195  1.00 18.89 ? 534  ILE   B CG2   1 
ATOM   12952 C  CD1   . ILE   B  1  536  ? -12.331 28.162  90.480  1.00 24.19 ? 534  ILE   B CD1   1 
ATOM   12953 N  N     . ALA   B  1  537  ? -10.228 29.721  85.148  1.00 16.87 ? 535  ALA   B N     1 
ATOM   12954 C  CA    . ALA   B  1  537  ? -9.753  29.316  83.837  1.00 17.55 ? 535  ALA   B CA    1 
ATOM   12955 C  C     . ALA   B  1  537  ? -8.974  28.013  83.941  1.00 15.83 ? 535  ALA   B C     1 
ATOM   12956 O  O     . ALA   B  1  537  ? -8.158  27.832  84.847  1.00 16.15 ? 535  ALA   B O     1 
ATOM   12957 C  CB    . ALA   B  1  537  ? -8.845  30.399  83.260  1.00 19.03 ? 535  ALA   B CB    1 
ATOM   12958 N  N     . LEU   B  1  538  ? -9.246  27.093  83.027  1.00 16.33 ? 536  LEU   B N     1 
ATOM   12959 C  CA    . LEU   B  1  538  ? -8.307  26.007  82.839  1.00 15.91 ? 536  LEU   B CA    1 
ATOM   12960 C  C     . LEU   B  1  538  ? -6.936  26.597  82.527  1.00 17.10 ? 536  LEU   B C     1 
ATOM   12961 O  O     . LEU   B  1  538  ? -6.834  27.685  81.946  1.00 16.98 ? 536  LEU   B O     1 
ATOM   12962 C  CB    . LEU   B  1  538  ? -8.727  25.138  81.658  1.00 17.74 ? 536  LEU   B CB    1 
ATOM   12963 C  CG    . LEU   B  1  538  ? -9.889  24.182  81.899  1.00 19.03 ? 536  LEU   B CG    1 
ATOM   12964 C  CD1   . LEU   B  1  538  ? -10.303 23.535  80.584  1.00 22.59 ? 536  LEU   B CD1   1 
ATOM   12965 C  CD2   . LEU   B  1  538  ? -9.506  23.128  82.934  1.00 20.33 ? 536  LEU   B CD2   1 
ATOM   12966 N  N     . PRO   B  1  539  ? -5.864  25.892  82.878  1.00 15.28 ? 537  PRO   B N     1 
ATOM   12967 C  CA    . PRO   B  1  539  ? -4.528  26.410  82.564  1.00 15.25 ? 537  PRO   B CA    1 
ATOM   12968 C  C     . PRO   B  1  539  ? -4.375  26.772  81.105  1.00 14.57 ? 537  PRO   B C     1 
ATOM   12969 O  O     . PRO   B  1  539  ? -3.815  27.831  80.802  1.00 15.12 ? 537  PRO   B O     1 
ATOM   12970 C  CB    . PRO   B  1  539  ? -3.597  25.284  83.029  1.00 17.23 ? 537  PRO   B CB    1 
ATOM   12971 C  CG    . PRO   B  1  539  ? -4.385  24.615  84.133  1.00 15.67 ? 537  PRO   B CG    1 
ATOM   12972 C  CD    . PRO   B  1  539  ? -5.824  24.672  83.702  1.00 15.58 ? 537  PRO   B CD    1 
ATOM   12973 N  N     . ALA   B  1  540  ? -4.917  25.965  80.197  1.00 14.62 ? 538  ALA   B N     1 
ATOM   12974 C  CA    . ALA   B  1  540  ? -4.792  26.281  78.781  1.00 16.03 ? 538  ALA   B CA    1 
ATOM   12975 C  C     . ALA   B  1  540  ? -5.500  27.574  78.411  1.00 17.17 ? 538  ALA   B C     1 
ATOM   12976 O  O     . ALA   B  1  540  ? -5.181  28.167  77.374  1.00 17.08 ? 538  ALA   B O     1 
ATOM   12977 C  CB    . ALA   B  1  540  ? -5.344  25.140  77.923  1.00 17.35 ? 538  ALA   B CB    1 
ATOM   12978 N  N     . GLU   B  1  541  ? -6.449  28.020  79.234  1.00 17.07 ? 539  GLU   B N     1 
ATOM   12979 C  CA    . GLU   B  1  541  ? -7.335  29.125  78.886  1.00 16.53 ? 539  GLU   B CA    1 
ATOM   12980 C  C     . GLU   B  1  541  ? -7.026  30.400  79.675  1.00 15.50 ? 539  GLU   B C     1 
ATOM   12981 O  O     . GLU   B  1  541  ? -7.846  31.321  79.693  1.00 17.76 ? 539  GLU   B O     1 
ATOM   12982 C  CB    . GLU   B  1  541  ? -8.801  28.676  78.994  1.00 19.31 ? 539  GLU   B CB    1 
ATOM   12983 C  CG    . GLU   B  1  541  ? -9.084  27.519  77.988  1.00 22.54 ? 539  GLU   B CG    1 
ATOM   12984 C  CD    . GLU   B  1  541  ? -10.448 26.827  78.104  1.00 30.83 ? 539  GLU   B CD    1 
ATOM   12985 O  OE1   . GLU   B  1  541  ? -11.289 27.228  78.928  1.00 31.51 ? 539  GLU   B OE1   1 
ATOM   12986 O  OE2   . GLU   B  1  541  ? -10.673 25.857  77.347  1.00 34.51 ? 539  GLU   B OE2   1 
ATOM   12987 N  N     . LEU   B  1  542  ? -5.831  30.506  80.274  1.00 14.57 ? 540  LEU   B N     1 
ATOM   12988 C  CA    . LEU   B  1  542  ? -5.516  31.679  81.094  1.00 16.75 ? 540  LEU   B CA    1 
ATOM   12989 C  C     . LEU   B  1  542  ? -5.639  32.979  80.319  1.00 16.45 ? 540  LEU   B C     1 
ATOM   12990 O  O     . LEU   B  1  542  ? -5.924  34.026  80.909  1.00 18.52 ? 540  LEU   B O     1 
ATOM   12991 C  CB    . LEU   B  1  542  ? -4.085  31.609  81.606  1.00 17.33 ? 540  LEU   B CB    1 
ATOM   12992 C  CG    . LEU   B  1  542  ? -3.744  30.701  82.763  1.00 19.41 ? 540  LEU   B CG    1 
ATOM   12993 C  CD1   . LEU   B  1  542  ? -2.330  31.024  83.211  1.00 16.71 ? 540  LEU   B CD1   1 
ATOM   12994 C  CD2   . LEU   B  1  542  ? -4.728  30.866  83.904  1.00 19.26 ? 540  LEU   B CD2   1 
ATOM   12995 N  N     . PHE   B  1  543  ? -5.396  32.948  79.012  1.00 15.57 ? 541  PHE   B N     1 
ATOM   12996 C  CA    . PHE   B  1  543  ? -5.390  34.155  78.198  1.00 16.26 ? 541  PHE   B CA    1 
ATOM   12997 C  C     . PHE   B  1  543  ? -6.648  34.293  77.369  1.00 16.55 ? 541  PHE   B C     1 
ATOM   12998 O  O     . PHE   B  1  543  ? -6.728  35.183  76.513  1.00 18.47 ? 541  PHE   B O     1 
ATOM   12999 C  CB    . PHE   B  1  543  ? -4.123  34.206  77.348  1.00 15.62 ? 541  PHE   B CB    1 
ATOM   13000 C  CG    . PHE   B  1  543  ? -2.908  33.945  78.148  1.00 17.07 ? 541  PHE   B CG    1 
ATOM   13001 C  CD1   . PHE   B  1  543  ? -2.627  34.739  79.244  1.00 19.18 ? 541  PHE   B CD1   1 
ATOM   13002 C  CD2   . PHE   B  1  543  ? -2.091  32.873  77.868  1.00 15.84 ? 541  PHE   B CD2   1 
ATOM   13003 C  CE1   . PHE   B  1  543  ? -1.527  34.491  80.026  1.00 19.03 ? 541  PHE   B CE1   1 
ATOM   13004 C  CE2   . PHE   B  1  543  ? -0.976  32.620  78.648  1.00 17.04 ? 541  PHE   B CE2   1 
ATOM   13005 C  CZ    . PHE   B  1  543  ? -0.697  33.434  79.728  1.00 17.93 ? 541  PHE   B CZ    1 
ATOM   13006 N  N     . GLY   B  1  544  ? -7.632  33.435  77.616  1.00 17.35 ? 542  GLY   B N     1 
ATOM   13007 C  CA    . GLY   B  1  544  ? -8.911  33.563  76.949  1.00 17.71 ? 542  GLY   B CA    1 
ATOM   13008 C  C     . GLY   B  1  544  ? -8.769  33.439  75.450  1.00 20.27 ? 542  GLY   B C     1 
ATOM   13009 O  O     . GLY   B  1  544  ? -8.034  32.590  74.931  1.00 21.49 ? 542  GLY   B O     1 
ATOM   13010 N  N     . ASP   B  1  545  ? -9.485  34.305  74.732  1.00 21.23 ? 543  ASP   B N     1 
ATOM   13011 C  CA    . ASP   B  1  545  ? -9.516  34.233  73.278  1.00 22.06 ? 543  ASP   B CA    1 
ATOM   13012 C  C     . ASP   B  1  545  ? -8.221  34.702  72.632  1.00 23.46 ? 543  ASP   B C     1 
ATOM   13013 O  O     . ASP   B  1  545  ? -8.038  34.479  71.430  1.00 23.62 ? 543  ASP   B O     1 
ATOM   13014 C  CB    . ASP   B  1  545  ? -10.669 35.083  72.740  1.00 24.96 ? 543  ASP   B CB    1 
ATOM   13015 C  CG    . ASP   B  1  545  ? -12.021 34.624  73.250  1.00 39.57 ? 543  ASP   B CG    1 
ATOM   13016 O  OD1   . ASP   B  1  545  ? -12.196 33.404  73.471  1.00 41.49 ? 543  ASP   B OD1   1 
ATOM   13017 O  OD2   . ASP   B  1  545  ? -12.911 35.486  73.424  1.00 51.26 ? 543  ASP   B OD2   1 
ATOM   13018 N  N     . ALA   B  1  546  ? -7.339  35.359  73.384  1.00 19.83 ? 544  ALA   B N     1 
ATOM   13019 C  CA    . ALA   B  1  546  ? -6.130  35.915  72.779  1.00 17.80 ? 544  ALA   B CA    1 
ATOM   13020 C  C     . ALA   B  1  546  ? -5.212  34.823  72.257  1.00 18.51 ? 544  ALA   B C     1 
ATOM   13021 O  O     . ALA   B  1  546  ? -4.659  34.941  71.158  1.00 18.57 ? 544  ALA   B O     1 
ATOM   13022 C  CB    . ALA   B  1  546  ? -5.385  36.795  73.782  1.00 21.83 ? 544  ALA   B CB    1 
ATOM   13023 N  N     . ARG   B  1  547  ? -5.014  33.765  73.035  1.00 17.51 ? 545  ARG   B N     1 
ATOM   13024 C  CA    . ARG   B  1  547  ? -4.100  32.707  72.628  1.00 17.56 ? 545  ARG   B CA    1 
ATOM   13025 C  C     . ARG   B  1  547  ? -4.228  31.567  73.617  1.00 16.87 ? 545  ARG   B C     1 
ATOM   13026 O  O     . ARG   B  1  547  ? -4.789  31.717  74.704  1.00 16.25 ? 545  ARG   B O     1 
ATOM   13027 C  CB    . ARG   B  1  547  ? -2.645  33.174  72.569  1.00 21.68 ? 545  ARG   B CB    1 
ATOM   13028 C  CG    . ARG   B  1  547  ? -2.126  33.619  73.892  1.00 17.47 ? 545  ARG   B CG    1 
ATOM   13029 C  CD    . ARG   B  1  547  ? -0.698  34.107  73.729  1.00 18.65 ? 545  ARG   B CD    1 
ATOM   13030 N  NE    . ARG   B  1  547  ? -0.373  34.987  74.833  1.00 16.80 ? 545  ARG   B NE    1 
ATOM   13031 C  CZ    . ARG   B  1  547  ? 0.414   34.662  75.849  1.00 17.04 ? 545  ARG   B CZ    1 
ATOM   13032 N  NH1   . ARG   B  1  547  ? 1.044   33.499  75.895  1.00 16.82 ? 545  ARG   B NH1   1 
ATOM   13033 N  NH2   . ARG   B  1  547  ? 0.577   35.532  76.838  1.00 18.50 ? 545  ARG   B NH2   1 
ATOM   13034 N  N     . THR   B  1  548  ? -3.754  30.415  73.194  1.00 14.97 ? 546  THR   B N     1 
ATOM   13035 C  CA    . THR   B  1  548  ? -3.746  29.232  74.028  1.00 14.91 ? 546  THR   B CA    1 
ATOM   13036 C  C     . THR   B  1  548  ? -2.448  29.202  74.818  1.00 13.92 ? 546  THR   B C     1 
ATOM   13037 O  O     . THR   B  1  548  ? -1.362  29.349  74.252  1.00 14.18 ? 546  THR   B O     1 
ATOM   13038 C  CB    . THR   B  1  548  ? -3.831  28.009  73.131  1.00 15.74 ? 546  THR   B CB    1 
ATOM   13039 O  OG1   . THR   B  1  548  ? -5.038  28.098  72.354  1.00 20.05 ? 546  THR   B OG1   1 
ATOM   13040 C  CG2   . THR   B  1  548  ? -3.822  26.744  73.969  1.00 18.28 ? 546  THR   B CG2   1 
ATOM   13041 N  N     . ASN   B  1  549  ? -2.563  29.017  76.124  1.00 13.67 ? 547  ASN   B N     1 
ATOM   13042 C  CA    . ASN   B  1  549  ? -1.397  28.938  76.976  1.00 13.32 ? 547  ASN   B CA    1 
ATOM   13043 C  C     . ASN   B  1  549  ? -0.623  27.673  76.639  1.00 14.25 ? 547  ASN   B C     1 
ATOM   13044 O  O     . ASN   B  1  549  ? -1.201  26.647  76.275  1.00 15.38 ? 547  ASN   B O     1 
ATOM   13045 C  CB    . ASN   B  1  549  ? -1.870  28.914  78.426  1.00 14.46 ? 547  ASN   B CB    1 
ATOM   13046 C  CG    . ASN   B  1  549  ? -0.749  29.066  79.405  1.00 13.48 ? 547  ASN   B CG    1 
ATOM   13047 O  OD1   . ASN   B  1  549  ? 0.347   29.513  79.063  1.00 14.38 ? 547  ASN   B OD1   1 
ATOM   13048 N  ND2   . ASN   B  1  549  ? -1.017  28.703  80.650  1.00 14.23 ? 547  ASN   B ND2   1 
ATOM   13049 N  N     . SER   B  1  550  ? 0.699   27.760  76.699  1.00 13.10 ? 548  SER   B N     1 
ATOM   13050 C  CA    . SER   B  1  550  ? 1.486   26.551  76.533  1.00 13.73 ? 548  SER   B CA    1 
ATOM   13051 C  C     . SER   B  1  550  ? 1.146   25.573  77.643  1.00 15.18 ? 548  SER   B C     1 
ATOM   13052 O  O     . SER   B  1  550  ? 0.765   25.962  78.752  1.00 15.05 ? 548  SER   B O     1 
ATOM   13053 C  CB    . SER   B  1  550  ? 2.970   26.871  76.595  1.00 12.66 ? 548  SER   B CB    1 
ATOM   13054 O  OG    . SER   B  1  550  ? 3.310   27.421  77.851  1.00 13.55 ? 548  SER   B OG    1 
ATOM   13055 N  N     . ALA   B  1  551  ? 1.288   24.293  77.333  1.00 15.37 ? 549  ALA   B N     1 
ATOM   13056 C  CA    . ALA   B  1  551  ? 1.059   23.228  78.295  1.00 17.70 ? 549  ALA   B CA    1 
ATOM   13057 C  C     . ALA   B  1  551  ? 2.377   22.642  78.771  1.00 15.55 ? 549  ALA   B C     1 
ATOM   13058 O  O     . ALA   B  1  551  ? 3.333   22.507  78.001  1.00 15.75 ? 549  ALA   B O     1 
ATOM   13059 C  CB    . ALA   B  1  551  ? 0.216   22.114  77.687  1.00 16.35 ? 549  ALA   B CB    1 
ATOM   13060 N  N     . GLY   B  1  552  ? 2.430   22.311  80.051  1.00 15.11 ? 550  GLY   B N     1 
ATOM   13061 C  CA    . GLY   B  1  552  ? 3.550   21.614  80.626  1.00 16.47 ? 550  GLY   B CA    1 
ATOM   13062 C  C     . GLY   B  1  552  ? 3.305   20.123  80.678  1.00 15.03 ? 550  GLY   B C     1 
ATOM   13063 O  O     . GLY   B  1  552  ? 2.454   19.570  79.974  1.00 17.51 ? 550  GLY   B O     1 
ATOM   13064 N  N     . LEU   B  1  553  ? 4.069   19.462  81.534  1.00 16.58 ? 551  LEU   B N     1 
ATOM   13065 C  CA    . LEU   B  1  553  ? 3.954   18.032  81.733  1.00 16.83 ? 551  LEU   B CA    1 
ATOM   13066 C  C     . LEU   B  1  553  ? 3.999   17.814  83.229  1.00 16.00 ? 551  LEU   B C     1 
ATOM   13067 O  O     . LEU   B  1  553  ? 4.759   18.482  83.926  1.00 18.63 ? 551  LEU   B O     1 
ATOM   13068 C  CB    . LEU   B  1  553  ? 5.135   17.293  81.089  1.00 18.72 ? 551  LEU   B CB    1 
ATOM   13069 C  CG    . LEU   B  1  553  ? 5.178   17.302  79.560  1.00 19.27 ? 551  LEU   B CG    1 
ATOM   13070 C  CD1   . LEU   B  1  553  ? 6.491   16.742  79.092  1.00 22.26 ? 551  LEU   B CD1   1 
ATOM   13071 C  CD2   . LEU   B  1  553  ? 4.030   16.492  78.985  1.00 21.41 ? 551  LEU   B CD2   1 
ATOM   13072 N  N     . ASP   B  1  554  ? 3.186   16.888  83.718  1.00 16.29 ? 552  ASP   B N     1 
ATOM   13073 C  CA    . ASP   B  1  554  ? 3.069   16.675  85.156  1.00 17.08 ? 552  ASP   B CA    1 
ATOM   13074 C  C     . ASP   B  1  554  ? 4.081   15.615  85.572  1.00 16.51 ? 552  ASP   B C     1 
ATOM   13075 O  O     . ASP   B  1  554  ? 3.869   14.422  85.355  1.00 16.93 ? 552  ASP   B O     1 
ATOM   13076 C  CB    . ASP   B  1  554  ? 1.652   16.249  85.498  1.00 18.60 ? 552  ASP   B CB    1 
ATOM   13077 C  CG    . ASP   B  1  554  ? 1.451   16.058  86.979  1.00 19.10 ? 552  ASP   B CG    1 
ATOM   13078 O  OD1   . ASP   B  1  554  ? 2.417   16.213  87.760  1.00 18.97 ? 552  ASP   B OD1   1 
ATOM   13079 O  OD2   . ASP   B  1  554  ? 0.317   15.740  87.363  1.00 20.08 ? 552  ASP   B OD2   1 
ATOM   13080 N  N     . LEU   B  1  555  ? 5.173   16.049  86.181  1.00 16.63 ? 553  LEU   B N     1 
ATOM   13081 C  CA    . LEU   B  1  555  ? 6.223   15.121  86.575  1.00 17.81 ? 553  LEU   B CA    1 
ATOM   13082 C  C     . LEU   B  1  555  ? 5.910   14.395  87.874  1.00 18.44 ? 553  LEU   B C     1 
ATOM   13083 O  O     . LEU   B  1  555  ? 6.781   13.699  88.401  1.00 17.85 ? 553  LEU   B O     1 
ATOM   13084 C  CB    . LEU   B  1  555  ? 7.566   15.839  86.664  1.00 18.17 ? 553  LEU   B CB    1 
ATOM   13085 C  CG    . LEU   B  1  555  ? 8.012   16.557  85.390  1.00 17.52 ? 553  LEU   B CG    1 
ATOM   13086 C  CD1   . LEU   B  1  555  ? 9.413   17.120  85.593  1.00 22.00 ? 553  LEU   B CD1   1 
ATOM   13087 C  CD2   . LEU   B  1  555  ? 7.963   15.605  84.197  1.00 21.06 ? 553  LEU   B CD2   1 
ATOM   13088 N  N     . SER   B  1  556  ? 4.693   14.536  88.395  1.00 17.02 ? 554  SER   B N     1 
ATOM   13089 C  CA    . SER   B  1  556  ? 4.215   13.685  89.473  1.00 17.37 ? 554  SER   B CA    1 
ATOM   13090 C  C     . SER   B  1  556  ? 3.274   12.611  88.971  1.00 18.78 ? 554  SER   B C     1 
ATOM   13091 O  O     . SER   B  1  556  ? 2.801   11.797  89.760  1.00 18.39 ? 554  SER   B O     1 
ATOM   13092 C  CB    . SER   B  1  556  ? 3.509   14.518  90.553  1.00 18.11 ? 554  SER   B CB    1 
ATOM   13093 O  OG    . SER   B  1  556  ? 2.239   14.949  90.086  1.00 18.90 ? 554  SER   B OG    1 
ATOM   13094 N  N     . ASN   B  1  557  ? 2.995   12.581  87.677  1.00 16.87 ? 555  ASN   B N     1 
ATOM   13095 C  CA    . ASN   B  1  557  ? 2.062   11.632  87.100  1.00 16.46 ? 555  ASN   B CA    1 
ATOM   13096 C  C     . ASN   B  1  557  ? 2.848   10.445  86.551  1.00 18.04 ? 555  ASN   B C     1 
ATOM   13097 O  O     . ASN   B  1  557  ? 3.685   10.616  85.663  1.00 17.47 ? 555  ASN   B O     1 
ATOM   13098 C  CB    . ASN   B  1  557  ? 1.270   12.340  86.004  1.00 16.72 ? 555  ASN   B CB    1 
ATOM   13099 C  CG    . ASN   B  1  557  ? 0.266   11.440  85.331  1.00 18.58 ? 555  ASN   B CG    1 
ATOM   13100 O  OD1   . ASN   B  1  557  ? 0.591   10.341  84.898  1.00 19.09 ? 555  ASN   B OD1   1 
ATOM   13101 N  ND2   . ASN   B  1  557  ? -0.982  11.900  85.245  1.00 19.07 ? 555  ASN   B ND2   1 
ATOM   13102 N  N     . GLU   B  1  558  ? 2.589   9.248   87.090  1.00 18.46 ? 556  GLU   B N     1 
ATOM   13103 C  CA    . GLU   B  1  558  ? 3.378   8.084   86.693  1.00 20.29 ? 556  GLU   B CA    1 
ATOM   13104 C  C     . GLU   B  1  558  ? 3.209   7.749   85.224  1.00 20.16 ? 556  GLU   B C     1 
ATOM   13105 O  O     . GLU   B  1  558  ? 4.152   7.258   84.599  1.00 20.59 ? 556  GLU   B O     1 
ATOM   13106 C  CB    . GLU   B  1  558  ? 3.041   6.849   87.526  1.00 23.30 ? 556  GLU   B CB    1 
ATOM   13107 C  CG    . GLU   B  1  558  ? 3.456   6.924   88.957  1.00 22.02 ? 556  GLU   B CG    1 
ATOM   13108 C  CD    . GLU   B  1  558  ? 4.964   7.036   89.206  1.00 23.21 ? 556  GLU   B CD    1 
ATOM   13109 O  OE1   . GLU   B  1  558  ? 5.821   6.830   88.316  1.00 20.89 ? 556  GLU   B OE1   1 
ATOM   13110 O  OE2   . GLU   B  1  558  ? 5.292   7.337   90.354  1.00 21.13 ? 556  GLU   B OE2   1 
ATOM   13111 N  N     . GLU   B  1  559  ? 2.016   7.953   84.660  1.00 19.19 ? 557  GLU   B N     1 
ATOM   13112 C  CA    . GLU   B  1  559  ? 1.858   7.737   83.227  1.00 18.64 ? 557  GLU   B CA    1 
ATOM   13113 C  C     . GLU   B  1  559  ? 2.761   8.686   82.466  1.00 19.44 ? 557  GLU   B C     1 
ATOM   13114 O  O     . GLU   B  1  559  ? 3.451   8.291   81.520  1.00 20.80 ? 557  GLU   B O     1 
ATOM   13115 C  CB    . GLU   B  1  559  ? 0.414   7.986   82.797  1.00 25.17 ? 557  GLU   B CB    1 
ATOM   13116 C  CG    . GLU   B  1  559  ? -0.610  7.015   83.298  1.00 28.28 ? 557  GLU   B CG    1 
ATOM   13117 C  CD    . GLU   B  1  559  ? -1.995  7.345   82.764  1.00 36.30 ? 557  GLU   B CD    1 
ATOM   13118 O  OE1   . GLU   B  1  559  ? -2.085  7.942   81.668  1.00 39.86 ? 557  GLU   B OE1   1 
ATOM   13119 O  OE2   . GLU   B  1  559  ? -2.989  7.021   83.443  1.00 34.60 ? 557  GLU   B OE2   1 
ATOM   13120 N  N     . THR   B  1  560  ? 2.765   9.953   82.875  1.00 17.73 ? 558  THR   B N     1 
ATOM   13121 C  CA    . THR   B  1  560  ? 3.609   10.933  82.209  1.00 17.22 ? 558  THR   B CA    1 
ATOM   13122 C  C     . THR   B  1  560  ? 5.073   10.572  82.363  1.00 17.65 ? 558  THR   B C     1 
ATOM   13123 O  O     . THR   B  1  560  ? 5.838   10.641  81.396  1.00 17.82 ? 558  THR   B O     1 
ATOM   13124 C  CB    . THR   B  1  560  ? 3.350   12.325  82.774  1.00 16.79 ? 558  THR   B CB    1 
ATOM   13125 O  OG1   . THR   B  1  560  ? 1.963   12.639  82.613  1.00 18.89 ? 558  THR   B OG1   1 
ATOM   13126 C  CG2   . THR   B  1  560  ? 4.178   13.365  82.027  1.00 19.52 ? 558  THR   B CG2   1 
ATOM   13127 N  N     . LEU   B  1  561  ? 5.484   10.175  83.569  1.00 16.39 ? 559  LEU   B N     1 
ATOM   13128 C  CA    . LEU   B  1  561  ? 6.883   9.818   83.777  1.00 15.89 ? 559  LEU   B CA    1 
ATOM   13129 C  C     . LEU   B  1  561  ? 7.279   8.617   82.933  1.00 19.01 ? 559  LEU   B C     1 
ATOM   13130 O  O     . LEU   B  1  561  ? 8.379   8.582   82.371  1.00 17.22 ? 559  LEU   B O     1 
ATOM   13131 C  CB    . LEU   B  1  561  ? 7.159   9.553   85.256  1.00 17.75 ? 559  LEU   B CB    1 
ATOM   13132 C  CG    . LEU   B  1  561  ? 7.093   10.814  86.109  1.00 15.77 ? 559  LEU   B CG    1 
ATOM   13133 C  CD1   . LEU   B  1  561  ? 7.249   10.426  87.566  1.00 17.97 ? 559  LEU   B CD1   1 
ATOM   13134 C  CD2   . LEU   B  1  561  ? 8.179   11.803  85.705  1.00 17.76 ? 559  LEU   B CD2   1 
ATOM   13135 N  N     . ALA   B  1  562  ? 6.390   7.633   82.816  1.00 17.78 ? 560  ALA   B N     1 
ATOM   13136 C  CA    . ALA   B  1  562  ? 6.719   6.454   82.029  1.00 18.65 ? 560  ALA   B CA    1 
ATOM   13137 C  C     . ALA   B  1  562  ? 6.823   6.799   80.553  1.00 21.70 ? 560  ALA   B C     1 
ATOM   13138 O  O     . ALA   B  1  562  ? 7.752   6.354   79.865  1.00 20.58 ? 560  ALA   B O     1 
ATOM   13139 C  CB    . ALA   B  1  562  ? 5.674   5.368   82.264  1.00 18.96 ? 560  ALA   B CB    1 
ATOM   13140 N  N     . SER   B  1  563  ? 5.880   7.585   80.038  1.00 18.31 ? 561  SER   B N     1 
ATOM   13141 C  CA    . SER   B  1  563  ? 5.949   7.928   78.623  1.00 17.89 ? 561  SER   B CA    1 
ATOM   13142 C  C     . SER   B  1  563  ? 7.105   8.878   78.356  1.00 18.88 ? 561  SER   B C     1 
ATOM   13143 O  O     . SER   B  1  563  ? 7.795   8.766   77.334  1.00 19.39 ? 561  SER   B O     1 
ATOM   13144 C  CB    . SER   B  1  563  ? 4.615   8.503   78.140  1.00 21.11 ? 561  SER   B CB    1 
ATOM   13145 O  OG    . SER   B  1  563  ? 4.327   9.742   78.749  1.00 24.23 ? 561  SER   B OG    1 
ATOM   13146 N  N     . LEU   B  1  564  ? 7.350   9.806   79.278  1.00 16.75 ? 562  LEU   B N     1 
ATOM   13147 C  CA    . LEU   B  1  564  ? 8.463   10.723  79.108  1.00 16.78 ? 562  LEU   B CA    1 
ATOM   13148 C  C     . LEU   B  1  564  ? 9.788   9.979   79.122  1.00 18.62 ? 562  LEU   B C     1 
ATOM   13149 O  O     . LEU   B  1  564  ? 10.667  10.258  78.298  1.00 19.04 ? 562  LEU   B O     1 
ATOM   13150 C  CB    . LEU   B  1  564  ? 8.413   11.804  80.185  1.00 18.98 ? 562  LEU   B CB    1 
ATOM   13151 C  CG    . LEU   B  1  564  ? 9.476   12.881  80.125  1.00 19.90 ? 562  LEU   B CG    1 
ATOM   13152 C  CD1   . LEU   B  1  564  ? 9.428   13.578  78.781  1.00 19.86 ? 562  LEU   B CD1   1 
ATOM   13153 C  CD2   . LEU   B  1  564  ? 9.250   13.862  81.258  1.00 20.94 ? 562  LEU   B CD2   1 
ATOM   13154 N  N     . THR   B  1  565  ? 9.941   9.014   80.034  1.00 18.38 ? 563  THR   B N     1 
ATOM   13155 C  CA    . THR   B  1  565  ? 11.147  8.192   80.059  1.00 17.64 ? 563  THR   B CA    1 
ATOM   13156 C  C     . THR   B  1  565  ? 11.435  7.617   78.683  1.00 19.98 ? 563  THR   B C     1 
ATOM   13157 O  O     . THR   B  1  565  ? 12.564  7.692   78.186  1.00 19.26 ? 563  THR   B O     1 
ATOM   13158 C  CB    . THR   B  1  565  ? 10.978  7.050   81.063  1.00 18.63 ? 563  THR   B CB    1 
ATOM   13159 O  OG1   . THR   B  1  565  ? 10.879  7.581   82.392  1.00 19.31 ? 563  THR   B OG1   1 
ATOM   13160 C  CG2   . THR   B  1  565  ? 12.179  6.114   81.013  1.00 20.31 ? 563  THR   B CG2   1 
ATOM   13161 N  N     . GLU   B  1  566  ? 10.417  7.036   78.051  1.00 18.15 ? 564  GLU   B N     1 
ATOM   13162 C  CA    . GLU   B  1  566  ? 10.622  6.434   76.737  1.00 18.26 ? 564  GLU   B CA    1 
ATOM   13163 C  C     . GLU   B  1  566  ? 10.980  7.485   75.700  1.00 17.96 ? 564  GLU   B C     1 
ATOM   13164 O  O     . GLU   B  1  566  ? 11.890  7.279   74.893  1.00 18.79 ? 564  GLU   B O     1 
ATOM   13165 C  CB    . GLU   B  1  566  ? 9.391   5.630   76.320  1.00 21.58 ? 564  GLU   B CB    1 
ATOM   13166 C  CG    . GLU   B  1  566  ? 9.188   4.393   77.193  1.00 27.79 ? 564  GLU   B CG    1 
ATOM   13167 C  CD    . GLU   B  1  566  ? 10.501  3.702   77.552  1.00 37.08 ? 564  GLU   B CD    1 
ATOM   13168 O  OE1   . GLU   B  1  566  ? 11.240  3.294   76.629  1.00 43.10 ? 564  GLU   B OE1   1 
ATOM   13169 O  OE2   . GLU   B  1  566  ? 10.796  3.570   78.763  1.00 36.27 ? 564  GLU   B OE2   1 
ATOM   13170 N  N     . ALA   B  1  567  ? 10.282  8.621   75.709  1.00 16.22 ? 565  ALA   B N     1 
ATOM   13171 C  CA    . ALA   B  1  567  ? 10.581  9.669   74.740  1.00 19.82 ? 565  ALA   B CA    1 
ATOM   13172 C  C     . ALA   B  1  567  ? 11.971  10.243  74.962  1.00 17.61 ? 565  ALA   B C     1 
ATOM   13173 O  O     . ALA   B  1  567  ? 12.668  10.588  73.997  1.00 17.21 ? 565  ALA   B O     1 
ATOM   13174 C  CB    . ALA   B  1  567  ? 9.540   10.780  74.840  1.00 18.82 ? 565  ALA   B CB    1 
ATOM   13175 N  N     . LEU   B  1  568  ? 12.392  10.357  76.221  1.00 16.06 ? 566  LEU   B N     1 
ATOM   13176 C  CA    . LEU   B  1  568  ? 13.719  10.887  76.498  1.00 16.23 ? 566  LEU   B CA    1 
ATOM   13177 C  C     . LEU   B  1  568  ? 14.788  9.912   76.036  1.00 17.98 ? 566  LEU   B C     1 
ATOM   13178 O  O     . LEU   B  1  568  ? 15.762  10.305  75.384  1.00 17.37 ? 566  LEU   B O     1 
ATOM   13179 C  CB    . LEU   B  1  568  ? 13.869  11.184  77.990  1.00 16.12 ? 566  LEU   B CB    1 
ATOM   13180 C  CG    . LEU   B  1  568  ? 12.943  12.280  78.521  1.00 15.53 ? 566  LEU   B CG    1 
ATOM   13181 C  CD1   . LEU   B  1  568  ? 13.015  12.325  80.029  1.00 17.86 ? 566  LEU   B CD1   1 
ATOM   13182 C  CD2   . LEU   B  1  568  ? 13.285  13.628  77.912  1.00 18.44 ? 566  LEU   B CD2   1 
ATOM   13183 N  N     . ARG   B  1  569  ? 14.614  8.629   76.356  1.00 17.63 ? 567  ARG   B N     1 
ATOM   13184 C  CA    . ARG   B  1  569  ? 15.544  7.616   75.875  1.00 19.16 ? 567  ARG   B CA    1 
ATOM   13185 C  C     . ARG   B  1  569  ? 15.631  7.640   74.359  1.00 19.75 ? 567  ARG   B C     1 
ATOM   13186 O  O     . ARG   B  1  569  ? 16.729  7.616   73.790  1.00 20.94 ? 567  ARG   B O     1 
ATOM   13187 C  CB    . ARG   B  1  569  ? 15.114  6.238   76.372  1.00 20.91 ? 567  ARG   B CB    1 
ATOM   13188 C  CG    . ARG   B  1  569  ? 15.391  6.048   77.844  1.00 28.13 ? 567  ARG   B CG    1 
ATOM   13189 C  CD    . ARG   B  1  569  ? 14.926  4.693   78.331  1.00 27.31 ? 567  ARG   B CD    1 
ATOM   13190 N  NE    . ARG   B  1  569  ? 15.036  4.606   79.782  1.00 30.43 ? 567  ARG   B NE    1 
ATOM   13191 C  CZ    . ARG   B  1  569  ? 14.506  3.635   80.515  1.00 34.61 ? 567  ARG   B CZ    1 
ATOM   13192 N  NH1   . ARG   B  1  569  ? 13.801  2.661   79.964  1.00 36.55 ? 567  ARG   B NH1   1 
ATOM   13193 N  NH2   . ARG   B  1  569  ? 14.681  3.649   81.835  1.00 39.38 ? 567  ARG   B NH2   1 
ATOM   13194 N  N     . GLU   B  1  570  ? 14.480  7.689   73.687  1.00 18.35 ? 568  GLU   B N     1 
ATOM   13195 C  CA    . GLU   B  1  570  ? 14.474  7.723   72.232  1.00 18.67 ? 568  GLU   B CA    1 
ATOM   13196 C  C     . GLU   B  1  570  ? 15.155  8.972   71.702  1.00 20.66 ? 568  GLU   B C     1 
ATOM   13197 O  O     . GLU   B  1  570  ? 15.787  8.926   70.643  1.00 21.09 ? 568  GLU   B O     1 
ATOM   13198 C  CB    . GLU   B  1  570  ? 13.037  7.652   71.720  1.00 20.66 ? 568  GLU   B CB    1 
ATOM   13199 C  CG    . GLU   B  1  570  ? 12.396  6.285   71.946  1.00 23.59 ? 568  GLU   B CG    1 
ATOM   13200 C  CD    . GLU   B  1  570  ? 10.878  6.335   71.974  1.00 34.45 ? 568  GLU   B CD    1 
ATOM   13201 O  OE1   . GLU   B  1  570  ? 10.299  7.383   71.610  1.00 32.76 ? 568  GLU   B OE1   1 
ATOM   13202 O  OE2   . GLU   B  1  570  ? 10.264  5.324   72.373  1.00 37.57 ? 568  GLU   B OE2   1 
ATOM   13203 N  N     . SER   B  1  571  ? 15.044  10.090  72.419  1.00 19.25 ? 569  SER   B N     1 
ATOM   13204 C  CA    . SER   B  1  571  ? 15.668  11.314  71.937  1.00 17.54 ? 569  SER   B CA    1 
ATOM   13205 C  C     . SER   B  1  571  ? 17.176  11.172  71.921  1.00 22.73 ? 569  SER   B C     1 
ATOM   13206 O  O     . SER   B  1  571  ? 17.844  11.718  71.037  1.00 22.64 ? 569  SER   B O     1 
ATOM   13207 C  CB    . SER   B  1  571  ? 15.253  12.511  72.794  1.00 19.66 ? 569  SER   B CB    1 
ATOM   13208 O  OG    . SER   B  1  571  ? 15.942  12.531  74.044  1.00 18.58 ? 569  SER   B OG    1 
ATOM   13209 N  N     . ALA   B  1  572  ? 17.724  10.399  72.854  1.00 20.52 ? 570  ALA   B N     1 
ATOM   13210 C  CA    . ALA   B  1  572  ? 19.167  10.238  72.908  1.00 19.82 ? 570  ALA   B CA    1 
ATOM   13211 C  C     . ALA   B  1  572  ? 19.680  9.323   71.805  1.00 23.87 ? 570  ALA   B C     1 
ATOM   13212 O  O     . ALA   B  1  572  ? 20.871  9.375   71.476  1.00 27.24 ? 570  ALA   B O     1 
ATOM   13213 C  CB    . ALA   B  1  572  ? 19.593  9.750   74.292  1.00 22.13 ? 570  ALA   B CB    1 
ATOM   13214 N  N     . ALA   B  1  573  ? 18.811  8.508   71.211  1.00 20.88 ? 571  ALA   B N     1 
ATOM   13215 C  CA    . ALA   B  1  573  ? 19.213  7.649   70.105  1.00 25.25 ? 571  ALA   B CA    1 
ATOM   13216 C  C     . ALA   B  1  573  ? 19.149  8.341   68.750  1.00 24.46 ? 571  ALA   B C     1 
ATOM   13217 O  O     . ALA   B  1  573  ? 19.585  7.757   67.751  1.00 25.51 ? 571  ALA   B O     1 
ATOM   13218 C  CB    . ALA   B  1  573  ? 18.351  6.385   70.070  1.00 25.23 ? 571  ALA   B CB    1 
ATOM   13219 N  N     . MET   B  1  574  ? 18.626  9.558   68.686  1.00 21.22 ? 572  MET   B N     1 
ATOM   13220 C  CA    . MET   B  1  574  ? 18.509  10.254  67.418  1.00 18.98 ? 572  MET   B CA    1 
ATOM   13221 C  C     . MET   B  1  574  ? 19.830  10.905  67.050  1.00 20.32 ? 572  MET   B C     1 
ATOM   13222 O  O     . MET   B  1  574  ? 20.617  11.296  67.915  1.00 21.42 ? 572  MET   B O     1 
ATOM   13223 C  CB    . MET   B  1  574  ? 17.450  11.343  67.523  1.00 20.83 ? 572  MET   B CB    1 
ATOM   13224 C  CG    . MET   B  1  574  ? 16.058  10.793  67.711  1.00 22.20 ? 572  MET   B CG    1 
ATOM   13225 S  SD    . MET   B  1  574  ? 14.905  12.074  68.206  1.00 23.93 ? 572  MET   B SD    1 
ATOM   13226 C  CE    . MET   B  1  574  ? 13.387  11.118  68.264  1.00 23.95 ? 572  MET   B CE    1 
ATOM   13227 N  N     . LYS   B  1  575  ? 20.056  11.048  65.748  1.00 18.95 ? 573  LYS   B N     1 
ATOM   13228 C  CA    . LYS   B  1  575  ? 21.239  11.748  65.254  1.00 18.28 ? 573  LYS   B CA    1 
ATOM   13229 C  C     . LYS   B  1  575  ? 20.896  13.226  65.200  1.00 17.91 ? 573  LYS   B C     1 
ATOM   13230 O  O     . LYS   B  1  575  ? 20.178  13.676  64.304  1.00 18.78 ? 573  LYS   B O     1 
ATOM   13231 C  CB    . LYS   B  1  575  ? 21.643  11.224  63.882  1.00 20.32 ? 573  LYS   B CB    1 
ATOM   13232 C  CG    . LYS   B  1  575  ? 22.873  11.905  63.301  1.00 23.95 ? 573  LYS   B CG    1 
ATOM   13233 C  CD    . LYS   B  1  575  ? 23.266  11.274  61.976  1.00 30.00 ? 573  LYS   B CD    1 
ATOM   13234 C  CE    . LYS   B  1  575  ? 24.664  11.698  61.538  1.00 42.59 ? 573  LYS   B CE    1 
ATOM   13235 N  NZ    . LYS   B  1  575  ? 24.659  12.976  60.772  1.00 43.19 ? 573  LYS   B NZ    1 
ATOM   13236 N  N     . TRP   B  1  576  ? 21.391  13.974  66.179  1.00 18.31 ? 574  TRP   B N     1 
ATOM   13237 C  CA    . TRP   B  1  576  ? 21.154  15.401  66.263  1.00 16.25 ? 574  TRP   B CA    1 
ATOM   13238 C  C     . TRP   B  1  576  ? 22.296  16.138  65.597  1.00 15.78 ? 574  TRP   B C     1 
ATOM   13239 O  O     . TRP   B  1  576  ? 23.467  15.923  65.925  1.00 18.03 ? 574  TRP   B O     1 
ATOM   13240 C  CB    . TRP   B  1  576  ? 21.074  15.842  67.717  1.00 16.57 ? 574  TRP   B CB    1 
ATOM   13241 C  CG    . TRP   B  1  576  ? 19.894  15.305  68.445  1.00 15.67 ? 574  TRP   B CG    1 
ATOM   13242 C  CD1   . TRP   B  1  576  ? 19.901  14.326  69.394  1.00 18.14 ? 574  TRP   B CD1   1 
ATOM   13243 C  CD2   . TRP   B  1  576  ? 18.534  15.714  68.292  1.00 16.74 ? 574  TRP   B CD2   1 
ATOM   13244 N  NE1   . TRP   B  1  576  ? 18.621  14.107  69.854  1.00 18.65 ? 574  TRP   B NE1   1 
ATOM   13245 C  CE2   . TRP   B  1  576  ? 17.766  14.950  69.193  1.00 18.42 ? 574  TRP   B CE2   1 
ATOM   13246 C  CE3   . TRP   B  1  576  ? 17.896  16.661  67.491  1.00 16.54 ? 574  TRP   B CE3   1 
ATOM   13247 C  CZ2   . TRP   B  1  576  ? 16.389  15.102  69.315  1.00 19.13 ? 574  TRP   B CZ2   1 
ATOM   13248 C  CZ3   . TRP   B  1  576  ? 16.523  16.823  67.622  1.00 17.36 ? 574  TRP   B CZ3   1 
ATOM   13249 C  CH2   . TRP   B  1  576  ? 15.785  16.040  68.525  1.00 18.42 ? 574  TRP   B CH2   1 
ATOM   13250 N  N     . THR   B  1  577  ? 21.951  17.011  64.668  1.00 16.80 ? 575  THR   B N     1 
ATOM   13251 C  CA    . THR   B  1  577  ? 22.944  17.768  63.936  1.00 15.61 ? 575  THR   B CA    1 
ATOM   13252 C  C     . THR   B  1  577  ? 22.497  19.213  63.886  1.00 16.35 ? 575  THR   B C     1 
ATOM   13253 O  O     . THR   B  1  577  ? 21.326  19.534  64.076  1.00 16.16 ? 575  THR   B O     1 
ATOM   13254 C  CB    . THR   B  1  577  ? 23.117  17.246  62.503  1.00 18.22 ? 575  THR   B CB    1 
ATOM   13255 O  OG1   . THR   B  1  577  ? 21.900  17.447  61.777  1.00 21.36 ? 575  THR   B OG1   1 
ATOM   13256 C  CG2   . THR   B  1  577  ? 23.480  15.762  62.503  1.00 19.95 ? 575  THR   B CG2   1 
ATOM   13257 N  N     . ALA   B  1  578  ? 23.453  20.091  63.618  1.00 15.62 ? 576  ALA   B N     1 
ATOM   13258 C  CA    . ALA   B  1  578  ? 23.157  21.490  63.357  1.00 16.32 ? 576  ALA   B CA    1 
ATOM   13259 C  C     . ALA   B  1  578  ? 24.097  21.904  62.249  1.00 15.07 ? 576  ALA   B C     1 
ATOM   13260 O  O     . ALA   B  1  578  ? 25.306  21.702  62.377  1.00 17.35 ? 576  ALA   B O     1 
ATOM   13261 C  CB    . ALA   B  1  578  ? 23.399  22.337  64.602  1.00 15.24 ? 576  ALA   B CB    1 
ATOM   13262 N  N     . LEU   B  1  579  ? 23.549  22.425  61.162  1.00 16.02 ? 577  LEU   B N     1 
ATOM   13263 C  CA    . LEU   B  1  579  ? 24.310  22.750  59.969  1.00 16.16 ? 577  LEU   B CA    1 
ATOM   13264 C  C     . LEU   B  1  579  ? 24.057  24.200  59.613  1.00 15.74 ? 577  LEU   B C     1 
ATOM   13265 O  O     . LEU   B  1  579  ? 23.038  24.772  60.005  1.00 15.28 ? 577  LEU   B O     1 
ATOM   13266 C  CB    . LEU   B  1  579  ? 23.831  21.885  58.790  1.00 18.69 ? 577  LEU   B CB    1 
ATOM   13267 C  CG    . LEU   B  1  579  ? 23.667  20.394  59.058  1.00 21.67 ? 577  LEU   B CG    1 
ATOM   13268 C  CD1   . LEU   B  1  579  ? 23.076  19.665  57.851  1.00 24.19 ? 577  LEU   B CD1   1 
ATOM   13269 C  CD2   . LEU   B  1  579  ? 25.020  19.857  59.411  1.00 20.69 ? 577  LEU   B CD2   1 
ATOM   13270 N  N     . PRO   B  1  580  ? 24.941  24.807  58.838  1.00 15.16 ? 578  PRO   B N     1 
ATOM   13271 C  CA    . PRO   B  1  580  ? 24.611  26.102  58.238  1.00 15.01 ? 578  PRO   B CA    1 
ATOM   13272 C  C     . PRO   B  1  580  ? 23.537  25.881  57.197  1.00 14.28 ? 578  PRO   B C     1 
ATOM   13273 O  O     . PRO   B  1  580  ? 23.794  25.359  56.111  1.00 17.08 ? 578  PRO   B O     1 
ATOM   13274 C  CB    . PRO   B  1  580  ? 25.933  26.557  57.606  1.00 17.15 ? 578  PRO   B CB    1 
ATOM   13275 C  CG    . PRO   B  1  580  ? 26.991  25.643  58.192  1.00 17.89 ? 578  PRO   B CG    1 
ATOM   13276 C  CD    . PRO   B  1  580  ? 26.280  24.351  58.445  1.00 16.59 ? 578  PRO   B CD    1 
ATOM   13277 N  N     . GLN   B  1  581  ? 22.317  26.196  57.563  1.00 14.17 ? 579  GLN   B N     1 
ATOM   13278 C  CA    . GLN   B  1  581  ? 21.156  25.945  56.720  1.00 15.91 ? 579  GLN   B CA    1 
ATOM   13279 C  C     . GLN   B  1  581  ? 20.844  27.219  55.963  1.00 17.22 ? 579  GLN   B C     1 
ATOM   13280 O  O     . GLN   B  1  581  ? 20.095  28.075  56.437  1.00 16.65 ? 579  GLN   B O     1 
ATOM   13281 C  CB    . GLN   B  1  581  ? 19.982  25.523  57.577  1.00 16.22 ? 579  GLN   B CB    1 
ATOM   13282 C  CG    . GLN   B  1  581  ? 20.205  24.240  58.295  1.00 17.46 ? 579  GLN   B CG    1 
ATOM   13283 C  CD    . GLN   B  1  581  ? 20.132  23.033  57.385  1.00 20.75 ? 579  GLN   B CD    1 
ATOM   13284 O  OE1   . GLN   B  1  581  ? 19.903  23.150  56.168  1.00 20.76 ? 579  GLN   B OE1   1 
ATOM   13285 N  NE2   . GLN   B  1  581  ? 20.296  21.856  57.974  1.00 26.21 ? 579  GLN   B NE2   1 
ATOM   13286 N  N     . LEU   B  1  582  ? 21.417  27.334  54.774  1.00 16.20 ? 580  LEU   B N     1 
ATOM   13287 C  CA    . LEU   B  1  582  ? 21.156  28.484  53.935  1.00 16.82 ? 580  LEU   B CA    1 
ATOM   13288 C  C     . LEU   B  1  582  ? 19.898  28.224  53.109  1.00 18.71 ? 580  LEU   B C     1 
ATOM   13289 O  O     . LEU   B  1  582  ? 19.339  27.120  53.109  1.00 18.77 ? 580  LEU   B O     1 
ATOM   13290 C  CB    . LEU   B  1  582  ? 22.374  28.810  53.064  1.00 18.54 ? 580  LEU   B CB    1 
ATOM   13291 C  CG    . LEU   B  1  582  ? 23.460  29.633  53.796  1.00 20.96 ? 580  LEU   B CG    1 
ATOM   13292 C  CD1   . LEU   B  1  582  ? 24.124  28.900  54.968  1.00 21.52 ? 580  LEU   B CD1   1 
ATOM   13293 C  CD2   . LEU   B  1  582  ? 24.513  30.128  52.813  1.00 25.61 ? 580  LEU   B CD2   1 
ATOM   13294 N  N     . ALA   B  1  583  ? 19.431  29.271  52.429  1.00 17.10 ? 581  ALA   B N     1 
ATOM   13295 C  CA    . ALA   B  1  583  ? 18.220  29.130  51.632  1.00 19.06 ? 581  ALA   B CA    1 
ATOM   13296 C  C     . ALA   B  1  583  ? 18.372  28.033  50.592  1.00 22.17 ? 581  ALA   B C     1 
ATOM   13297 O  O     . ALA   B  1  583  ? 17.410  27.316  50.297  1.00 24.61 ? 581  ALA   B O     1 
ATOM   13298 C  CB    . ALA   B  1  583  ? 17.891  30.457  50.955  1.00 22.61 ? 581  ALA   B CB    1 
ATOM   13299 N  N     . THR   B  1  584  ? 19.577  27.868  50.057  1.00 19.46 ? 582  THR   B N     1 
ATOM   13300 C  CA    . THR   B  1  584  ? 19.859  26.921  48.990  1.00 21.46 ? 582  THR   B CA    1 
ATOM   13301 C  C     . THR   B  1  584  ? 20.211  25.535  49.507  1.00 18.71 ? 582  THR   B C     1 
ATOM   13302 O  O     . THR   B  1  584  ? 20.505  24.643  48.705  1.00 19.80 ? 582  THR   B O     1 
ATOM   13303 C  CB    . THR   B  1  584  ? 21.009  27.460  48.135  1.00 22.97 ? 582  THR   B CB    1 
ATOM   13304 O  OG1   . THR   B  1  584  ? 22.055  27.901  49.007  1.00 24.10 ? 582  THR   B OG1   1 
ATOM   13305 C  CG2   . THR   B  1  584  ? 20.536  28.629  47.303  1.00 31.00 ? 582  THR   B CG2   1 
ATOM   13306 N  N     . GLY   B  1  585  ? 20.186  25.325  50.819  1.00 19.66 ? 583  GLY   B N     1 
ATOM   13307 C  CA    . GLY   B  1  585  ? 20.530  24.045  51.387  1.00 19.43 ? 583  GLY   B CA    1 
ATOM   13308 C  C     . GLY   B  1  585  ? 21.637  24.183  52.408  1.00 18.93 ? 583  GLY   B C     1 
ATOM   13309 O  O     . GLY   B  1  585  ? 22.180  25.272  52.620  1.00 20.38 ? 583  GLY   B O     1 
ATOM   13310 N  N     . PRO   B  1  586  ? 21.989  23.080  53.061  1.00 17.99 ? 584  PRO   B N     1 
ATOM   13311 C  CA    . PRO   B  1  586  ? 23.060  23.135  54.055  1.00 16.01 ? 584  PRO   B CA    1 
ATOM   13312 C  C     . PRO   B  1  586  ? 24.408  23.301  53.390  1.00 18.72 ? 584  PRO   B C     1 
ATOM   13313 O  O     . PRO   B  1  586  ? 24.689  22.706  52.348  1.00 20.23 ? 584  PRO   B O     1 
ATOM   13314 C  CB    . PRO   B  1  586  ? 22.964  21.782  54.763  1.00 19.41 ? 584  PRO   B CB    1 
ATOM   13315 C  CG    . PRO   B  1  586  ? 22.382  20.884  53.738  1.00 22.98 ? 584  PRO   B CG    1 
ATOM   13316 C  CD    . PRO   B  1  586  ? 21.392  21.740  52.986  1.00 21.35 ? 584  PRO   B CD    1 
ATOM   13317 N  N     . ALA   B  1  587  ? 25.237  24.124  54.012  1.00 18.36 ? 585  ALA   B N     1 
ATOM   13318 C  CA    . ALA   B  1  587  ? 26.580  24.392  53.534  1.00 17.22 ? 585  ALA   B CA    1 
ATOM   13319 C  C     . ALA   B  1  587  ? 27.580  23.544  54.297  1.00 18.33 ? 585  ALA   B C     1 
ATOM   13320 O  O     . ALA   B  1  587  ? 27.352  23.136  55.438  1.00 18.31 ? 585  ALA   B O     1 
ATOM   13321 C  CB    . ALA   B  1  587  ? 26.918  25.871  53.719  1.00 19.49 ? 585  ALA   B CB    1 
ATOM   13322 N  N     . ALA   B  1  588  ? 28.710  23.297  53.645  1.00 19.36 ? 586  ALA   B N     1 
ATOM   13323 C  CA    . ALA   B  1  588  ? 29.815  22.627  54.299  1.00 18.86 ? 586  ALA   B CA    1 
ATOM   13324 C  C     . ALA   B  1  588  ? 30.480  23.562  55.296  1.00 19.19 ? 586  ALA   B C     1 
ATOM   13325 O  O     . ALA   B  1  588  ? 30.414  24.790  55.184  1.00 20.86 ? 586  ALA   B O     1 
ATOM   13326 C  CB    . ALA   B  1  588  ? 30.861  22.221  53.272  1.00 18.47 ? 586  ALA   B CB    1 
ATOM   13327 N  N     . GLY   B  1  589  ? 31.140  22.965  56.277  1.00 20.01 ? 587  GLY   B N     1 
ATOM   13328 C  CA    . GLY   B  1  589  ? 31.871  23.759  57.241  1.00 20.45 ? 587  GLY   B CA    1 
ATOM   13329 C  C     . GLY   B  1  589  ? 32.672  22.875  58.166  1.00 20.52 ? 587  GLY   B C     1 
ATOM   13330 O  O     . GLY   B  1  589  ? 32.749  21.659  57.982  1.00 22.19 ? 587  GLY   B O     1 
ATOM   13331 N  N     . GLU   B  1  590  ? 33.261  23.508  59.178  1.00 20.84 ? 588  GLU   B N     1 
ATOM   13332 C  CA    . GLU   B  1  590  ? 34.017  22.781  60.186  1.00 21.43 ? 588  GLU   B CA    1 
ATOM   13333 C  C     . GLU   B  1  590  ? 33.055  22.130  61.168  1.00 20.33 ? 588  GLU   B C     1 
ATOM   13334 O  O     . GLU   B  1  590  ? 32.164  22.786  61.709  1.00 19.31 ? 588  GLU   B O     1 
ATOM   13335 C  CB    . GLU   B  1  590  ? 34.950  23.735  60.928  1.00 25.79 ? 588  GLU   B CB    1 
ATOM   13336 C  CG    . GLU   B  1  590  ? 36.098  24.252  60.070  1.00 35.29 ? 588  GLU   B CG    1 
ATOM   13337 C  CD    . GLU   B  1  590  ? 37.040  23.143  59.632  1.00 38.40 ? 588  GLU   B CD    1 
ATOM   13338 O  OE1   . GLU   B  1  590  ? 37.327  22.241  60.450  1.00 44.24 ? 588  GLU   B OE1   1 
ATOM   13339 O  OE2   . GLU   B  1  590  ? 37.490  23.169  58.467  1.00 49.16 ? 588  GLU   B OE2   1 
ATOM   13340 N  N     . THR   B  1  591  ? 33.242  20.841  61.405  1.00 20.42 ? 589  THR   B N     1 
ATOM   13341 C  CA    . THR   B  1  591  ? 32.314  20.060  62.205  1.00 22.33 ? 589  THR   B CA    1 
ATOM   13342 C  C     . THR   B  1  591  ? 32.980  19.603  63.494  1.00 20.36 ? 589  THR   B C     1 
ATOM   13343 O  O     . THR   B  1  591  ? 34.152  19.201  63.502  1.00 21.66 ? 589  THR   B O     1 
ATOM   13344 C  CB    . THR   B  1  591  ? 31.830  18.851  61.408  1.00 20.77 ? 589  THR   B CB    1 
ATOM   13345 O  OG1   . THR   B  1  591  ? 31.189  19.306  60.212  1.00 23.36 ? 589  THR   B OG1   1 
ATOM   13346 C  CG2   . THR   B  1  591  ? 30.841  18.053  62.211  1.00 22.70 ? 589  THR   B CG2   1 
ATOM   13347 N  N     . ARG   B  1  592  ? 32.236  19.686  64.588  1.00 19.83 ? 590  ARG   B N     1 
ATOM   13348 C  CA    . ARG   B  1  592  ? 32.713  19.156  65.851  1.00 22.91 ? 590  ARG   B CA    1 
ATOM   13349 C  C     . ARG   B  1  592  ? 31.546  18.543  66.606  1.00 19.91 ? 590  ARG   B C     1 
ATOM   13350 O  O     . ARG   B  1  592  ? 30.373  18.781  66.296  1.00 19.26 ? 590  ARG   B O     1 
ATOM   13351 C  CB    . ARG   B  1  592  ? 33.367  20.248  66.691  1.00 23.12 ? 590  ARG   B CB    1 
ATOM   13352 C  CG    . ARG   B  1  592  ? 32.403  21.336  67.079  1.00 23.54 ? 590  ARG   B CG    1 
ATOM   13353 C  CD    . ARG   B  1  592  ? 32.949  22.137  68.227  1.00 29.26 ? 590  ARG   B CD    1 
ATOM   13354 N  NE    . ARG   B  1  592  ? 32.104  23.288  68.506  1.00 28.42 ? 590  ARG   B NE    1 
ATOM   13355 C  CZ    . ARG   B  1  592  ? 31.092  23.282  69.360  1.00 27.76 ? 590  ARG   B CZ    1 
ATOM   13356 N  NH1   . ARG   B  1  592  ? 30.755  22.189  70.029  1.00 27.05 ? 590  ARG   B NH1   1 
ATOM   13357 N  NH2   . ARG   B  1  592  ? 30.401  24.403  69.548  1.00 28.05 ? 590  ARG   B NH2   1 
ATOM   13358 N  N     . THR   B  1  593  ? 31.880  17.755  67.620  1.00 22.76 ? 591  THR   B N     1 
ATOM   13359 C  CA    . THR   B  1  593  ? 30.857  17.140  68.440  1.00 21.21 ? 591  THR   B CA    1 
ATOM   13360 C  C     . THR   B  1  593  ? 30.342  18.131  69.465  1.00 19.81 ? 591  THR   B C     1 
ATOM   13361 O  O     . THR   B  1  593  ? 31.021  19.088  69.847  1.00 21.97 ? 591  THR   B O     1 
ATOM   13362 C  CB    . THR   B  1  593  ? 31.411  15.918  69.165  1.00 23.82 ? 591  THR   B CB    1 
ATOM   13363 O  OG1   . THR   B  1  593  ? 32.517  16.317  69.980  1.00 27.78 ? 591  THR   B OG1   1 
ATOM   13364 C  CG2   . THR   B  1  593  ? 31.866  14.878  68.159  1.00 28.52 ? 591  THR   B CG2   1 
ATOM   13365 N  N     . VAL   B  1  594  ? 29.109  17.900  69.887  1.00 18.11 ? 592  VAL   B N     1 
ATOM   13366 C  CA    . VAL   B  1  594  ? 28.480  18.615  70.982  1.00 17.79 ? 592  VAL   B CA    1 
ATOM   13367 C  C     . VAL   B  1  594  ? 28.363  17.619  72.119  1.00 19.16 ? 592  VAL   B C     1 
ATOM   13368 O  O     . VAL   B  1  594  ? 27.785  16.538  71.947  1.00 19.57 ? 592  VAL   B O     1 
ATOM   13369 C  CB    . VAL   B  1  594  ? 27.105  19.144  70.558  1.00 17.77 ? 592  VAL   B CB    1 
ATOM   13370 C  CG1   . VAL   B  1  594  ? 26.431  19.864  71.707  1.00 19.18 ? 592  VAL   B CG1   1 
ATOM   13371 C  CG2   . VAL   B  1  594  ? 27.255  20.062  69.352  1.00 20.65 ? 592  VAL   B CG2   1 
ATOM   13372 N  N     . LEU   B  1  595  ? 28.948  17.959  73.264  1.00 18.67 ? 593  LEU   B N     1 
ATOM   13373 C  CA    . LEU   B  1  595  ? 29.053  17.058  74.401  1.00 18.08 ? 593  LEU   B CA    1 
ATOM   13374 C  C     . LEU   B  1  595  ? 28.141  17.528  75.520  1.00 17.38 ? 593  LEU   B C     1 
ATOM   13375 O  O     . LEU   B  1  595  ? 27.935  18.726  75.714  1.00 21.01 ? 593  LEU   B O     1 
ATOM   13376 C  CB    . LEU   B  1  595  ? 30.485  17.020  74.932  1.00 19.98 ? 593  LEU   B CB    1 
ATOM   13377 C  CG    . LEU   B  1  595  ? 31.529  16.606  73.895  1.00 21.66 ? 593  LEU   B CG    1 
ATOM   13378 C  CD1   . LEU   B  1  595  ? 32.907  16.605  74.546  1.00 24.22 ? 593  LEU   B CD1   1 
ATOM   13379 C  CD2   . LEU   B  1  595  ? 31.208  15.246  73.268  1.00 20.58 ? 593  LEU   B CD2   1 
ATOM   13380 N  N     . ASN   B  1  596  ? 27.616  16.574  76.263  1.00 16.33 ? 594  ASN   B N     1 
ATOM   13381 C  CA    . ASN   B  1  596  ? 26.786  16.894  77.408  1.00 16.57 ? 594  ASN   B CA    1 
ATOM   13382 C  C     . ASN   B  1  596  ? 27.645  17.605  78.449  1.00 15.50 ? 594  ASN   B C     1 
ATOM   13383 O  O     . ASN   B  1  596  ? 28.660  17.043  78.891  1.00 16.16 ? 594  ASN   B O     1 
ATOM   13384 C  CB    . ASN   B  1  596  ? 26.277  15.569  77.957  1.00 16.16 ? 594  ASN   B CB    1 
ATOM   13385 C  CG    . ASN   B  1  596  ? 25.261  15.732  79.055  1.00 16.75 ? 594  ASN   B CG    1 
ATOM   13386 O  OD1   . ASN   B  1  596  ? 25.304  16.680  79.835  1.00 16.60 ? 594  ASN   B OD1   1 
ATOM   13387 N  ND2   . ASN   B  1  596  ? 24.341  14.779  79.137  1.00 18.57 ? 594  ASN   B ND2   1 
ATOM   13388 N  N     . PRO   B  1  597  ? 27.308  18.831  78.848  1.00 14.74 ? 595  PRO   B N     1 
ATOM   13389 C  CA    . PRO   B  1  597  ? 28.147  19.522  79.837  1.00 15.61 ? 595  PRO   B CA    1 
ATOM   13390 C  C     . PRO   B  1  597  ? 28.224  18.796  81.152  1.00 15.52 ? 595  PRO   B C     1 
ATOM   13391 O  O     . PRO   B  1  597  ? 29.189  18.998  81.898  1.00 15.86 ? 595  PRO   B O     1 
ATOM   13392 C  CB    . PRO   B  1  597  ? 27.476  20.893  79.991  1.00 16.07 ? 595  PRO   B CB    1 
ATOM   13393 C  CG    . PRO   B  1  597  ? 26.047  20.678  79.511  1.00 15.43 ? 595  PRO   B CG    1 
ATOM   13394 C  CD    . PRO   B  1  597  ? 26.153  19.645  78.425  1.00 14.83 ? 595  PRO   B CD    1 
ATOM   13395 N  N     . GLY   B  1  598  ? 27.234  17.964  81.473  1.00 15.57 ? 596  GLY   B N     1 
ATOM   13396 C  CA    . GLY   B  1  598  ? 27.283  17.206  82.706  1.00 15.76 ? 596  GLY   B CA    1 
ATOM   13397 C  C     . GLY   B  1  598  ? 28.051  15.915  82.615  1.00 17.23 ? 596  GLY   B C     1 
ATOM   13398 O  O     . GLY   B  1  598  ? 28.294  15.275  83.638  1.00 18.31 ? 596  GLY   B O     1 
ATOM   13399 N  N     . ASP   B  1  599  ? 28.455  15.517  81.415  1.00 16.71 ? 597  ASP   B N     1 
ATOM   13400 C  CA    . ASP   B  1  599  ? 29.224  14.296  81.228  1.00 17.70 ? 597  ASP   B CA    1 
ATOM   13401 C  C     . ASP   B  1  599  ? 29.760  14.318  79.809  1.00 18.81 ? 597  ASP   B C     1 
ATOM   13402 O  O     . ASP   B  1  599  ? 29.047  13.985  78.860  1.00 17.99 ? 597  ASP   B O     1 
ATOM   13403 C  CB    . ASP   B  1  599  ? 28.335  13.075  81.454  1.00 17.44 ? 597  ASP   B CB    1 
ATOM   13404 C  CG    . ASP   B  1  599  ? 29.100  11.784  81.459  1.00 19.60 ? 597  ASP   B CG    1 
ATOM   13405 O  OD1   . ASP   B  1  599  ? 30.243  11.764  80.954  1.00 18.71 ? 597  ASP   B OD1   1 
ATOM   13406 O  OD2   . ASP   B  1  599  ? 28.543  10.792  81.967  1.00 22.30 ? 597  ASP   B OD2   1 
ATOM   13407 N  N     . HIS   B  1  600  ? 31.023  14.701  79.650  1.00 17.42 ? 598  HIS   B N     1 
ATOM   13408 C  CA    . HIS   B  1  600  ? 31.563  14.826  78.307  1.00 19.48 ? 598  HIS   B CA    1 
ATOM   13409 C  C     . HIS   B  1  600  ? 31.644  13.501  77.567  1.00 18.27 ? 598  HIS   B C     1 
ATOM   13410 O  O     . HIS   B  1  600  ? 31.858  13.513  76.353  1.00 21.17 ? 598  HIS   B O     1 
ATOM   13411 C  CB    . HIS   B  1  600  ? 32.914  15.538  78.332  1.00 20.29 ? 598  HIS   B CB    1 
ATOM   13412 C  CG    . HIS   B  1  600  ? 32.802  16.987  78.674  1.00 19.68 ? 598  HIS   B CG    1 
ATOM   13413 N  ND1   . HIS   B  1  600  ? 33.896  17.818  78.777  1.00 24.30 ? 598  HIS   B ND1   1 
ATOM   13414 C  CD2   . HIS   B  1  600  ? 31.718  17.759  78.920  1.00 19.65 ? 598  HIS   B CD2   1 
ATOM   13415 C  CE1   . HIS   B  1  600  ? 33.492  19.038  79.083  1.00 27.51 ? 598  HIS   B CE1   1 
ATOM   13416 N  NE2   . HIS   B  1  600  ? 32.173  19.031  79.173  1.00 21.95 ? 598  HIS   B NE2   1 
ATOM   13417 N  N     . ARG   B  1  601  ? 31.474  12.370  78.253  1.00 19.53 ? 599  ARG   B N     1 
ATOM   13418 C  CA    . ARG   B  1  601  ? 31.403  11.094  77.556  1.00 19.86 ? 599  ARG   B CA    1 
ATOM   13419 C  C     . ARG   B  1  601  ? 30.115  10.956  76.758  1.00 19.31 ? 599  ARG   B C     1 
ATOM   13420 O  O     . ARG   B  1  601  ? 30.050  10.130  75.843  1.00 22.13 ? 599  ARG   B O     1 
ATOM   13421 C  CB    . ARG   B  1  601  ? 31.519  9.953   78.560  1.00 22.43 ? 599  ARG   B CB    1 
ATOM   13422 C  CG    . ARG   B  1  601  ? 32.823  9.983   79.345  1.00 23.87 ? 599  ARG   B CG    1 
ATOM   13423 C  CD    . ARG   B  1  601  ? 32.786  9.018   80.510  1.00 27.16 ? 599  ARG   B CD    1 
ATOM   13424 N  NE    . ARG   B  1  601  ? 31.697  9.325   81.425  1.00 25.14 ? 599  ARG   B NE    1 
ATOM   13425 C  CZ    . ARG   B  1  601  ? 31.350  8.571   82.459  1.00 29.49 ? 599  ARG   B CZ    1 
ATOM   13426 N  NH1   . ARG   B  1  601  ? 32.026  7.477   82.773  1.00 28.06 ? 599  ARG   B NH1   1 
ATOM   13427 N  NH2   . ARG   B  1  601  ? 30.295  8.919   83.191  1.00 24.68 ? 599  ARG   B NH2   1 
ATOM   13428 N  N     . ASP   B  1  602  ? 29.094  11.743  77.085  1.00 18.61 ? 600  ASP   B N     1 
ATOM   13429 C  CA    . ASP   B  1  602  ? 27.791  11.653  76.437  1.00 19.04 ? 600  ASP   B CA    1 
ATOM   13430 C  C     . ASP   B  1  602  ? 27.811  12.595  75.240  1.00 19.54 ? 600  ASP   B C     1 
ATOM   13431 O  O     . ASP   B  1  602  ? 27.711  13.814  75.387  1.00 19.88 ? 600  ASP   B O     1 
ATOM   13432 C  CB    . ASP   B  1  602  ? 26.704  12.020  77.440  1.00 20.88 ? 600  ASP   B CB    1 
ATOM   13433 C  CG    . ASP   B  1  602  ? 25.319  11.908  76.858  1.00 22.41 ? 600  ASP   B CG    1 
ATOM   13434 O  OD1   . ASP   B  1  602  ? 25.161  11.188  75.846  1.00 23.40 ? 600  ASP   B OD1   1 
ATOM   13435 O  OD2   . ASP   B  1  602  ? 24.398  12.553  77.411  1.00 22.87 ? 600  ASP   B OD2   1 
ATOM   13436 N  N     . VAL   B  1  603  ? 27.979  12.032  74.050  1.00 18.65 ? 601  VAL   B N     1 
ATOM   13437 C  CA    . VAL   B  1  603  ? 27.978  12.825  72.828  1.00 19.33 ? 601  VAL   B CA    1 
ATOM   13438 C  C     . VAL   B  1  603  ? 26.532  13.077  72.434  1.00 20.15 ? 601  VAL   B C     1 
ATOM   13439 O  O     . VAL   B  1  603  ? 25.765  12.136  72.200  1.00 21.67 ? 601  VAL   B O     1 
ATOM   13440 C  CB    . VAL   B  1  603  ? 28.738  12.111  71.707  1.00 20.62 ? 601  VAL   B CB    1 
ATOM   13441 C  CG1   . VAL   B  1  603  ? 28.689  12.942  70.432  1.00 21.60 ? 601  VAL   B CG1   1 
ATOM   13442 C  CG2   . VAL   B  1  603  ? 30.185  11.837  72.142  1.00 20.86 ? 601  VAL   B CG2   1 
ATOM   13443 N  N     . VAL   B  1  604  ? 26.153  14.346  72.382  1.00 17.58 ? 602  VAL   B N     1 
ATOM   13444 C  CA    . VAL   B  1  604  ? 24.773  14.687  72.080  1.00 16.81 ? 602  VAL   B CA    1 
ATOM   13445 C  C     . VAL   B  1  604  ? 24.547  14.778  70.585  1.00 16.57 ? 602  VAL   B C     1 
ATOM   13446 O  O     . VAL   B  1  604  ? 23.513  14.342  70.080  1.00 17.82 ? 602  VAL   B O     1 
ATOM   13447 C  CB    . VAL   B  1  604  ? 24.379  15.986  72.794  1.00 15.88 ? 602  VAL   B CB    1 
ATOM   13448 C  CG1   . VAL   B  1  604  ? 22.902  16.243  72.601  1.00 16.48 ? 602  VAL   B CG1   1 
ATOM   13449 C  CG2   . VAL   B  1  604  ? 24.714  15.868  74.279  1.00 17.17 ? 602  VAL   B CG2   1 
ATOM   13450 N  N     . GLY   B  1  605  ? 25.510  15.312  69.854  1.00 16.71 ? 603  GLY   B N     1 
ATOM   13451 C  CA    . GLY   B  1  605  ? 25.320  15.470  68.434  1.00 17.74 ? 603  GLY   B CA    1 
ATOM   13452 C  C     . GLY   B  1  605  ? 26.529  16.111  67.816  1.00 17.03 ? 603  GLY   B C     1 
ATOM   13453 O  O     . GLY   B  1  605  ? 27.619  16.086  68.386  1.00 18.47 ? 603  GLY   B O     1 
ATOM   13454 N  N     . SER   B  1  606  ? 26.316  16.713  66.657  1.00 16.69 ? 604  SER   B N     1 
ATOM   13455 C  CA    A SER   B  1  606  ? 27.405  17.302  65.897  0.28 18.16 ? 604  SER   B CA    1 
ATOM   13456 C  CA    B SER   B  1  606  ? 27.402  17.294  65.885  0.31 18.16 ? 604  SER   B CA    1 
ATOM   13457 C  CA    C SER   B  1  606  ? 27.390  17.272  65.852  0.41 18.14 ? 604  SER   B CA    1 
ATOM   13458 C  C     . SER   B  1  606  ? 26.940  18.613  65.296  1.00 17.92 ? 604  SER   B C     1 
ATOM   13459 O  O     . SER   B  1  606  ? 25.785  18.750  64.877  1.00 19.99 ? 604  SER   B O     1 
ATOM   13460 C  CB    A SER   B  1  606  ? 27.878  16.367  64.782  0.28 22.00 ? 604  SER   B CB    1 
ATOM   13461 C  CB    B SER   B  1  606  ? 27.844  16.354  64.759  0.31 22.00 ? 604  SER   B CB    1 
ATOM   13462 C  CB    C SER   B  1  606  ? 27.688  16.314  64.694  0.41 21.92 ? 604  SER   B CB    1 
ATOM   13463 O  OG    A SER   B  1  606  ? 26.877  16.212  63.798  0.28 21.43 ? 604  SER   B OG    1 
ATOM   13464 O  OG    B SER   B  1  606  ? 28.395  15.159  65.285  0.31 25.48 ? 604  SER   B OG    1 
ATOM   13465 O  OG    C SER   B  1  606  ? 28.478  16.928  63.703  0.41 21.38 ? 604  SER   B OG    1 
ATOM   13466 N  N     . VAL   B  1  607  ? 27.842  19.583  65.271  1.00 16.05 ? 605  VAL   B N     1 
ATOM   13467 C  CA    . VAL   B  1  607  ? 27.548  20.891  64.708  1.00 15.12 ? 605  VAL   B CA    1 
ATOM   13468 C  C     . VAL   B  1  607  ? 28.551  21.192  63.613  1.00 16.17 ? 605  VAL   B C     1 
ATOM   13469 O  O     . VAL   B  1  607  ? 29.759  20.997  63.787  1.00 16.29 ? 605  VAL   B O     1 
ATOM   13470 C  CB    . VAL   B  1  607  ? 27.520  22.009  65.768  1.00 15.33 ? 605  VAL   B CB    1 
ATOM   13471 C  CG1   . VAL   B  1  607  ? 28.843  22.067  66.560  1.00 15.79 ? 605  VAL   B CG1   1 
ATOM   13472 C  CG2   . VAL   B  1  607  ? 27.228  23.344  65.096  1.00 16.16 ? 605  VAL   B CG2   1 
ATOM   13473 N  N     . THR   B  1  608  ? 28.048  21.649  62.482  1.00 16.02 ? 606  THR   B N     1 
ATOM   13474 C  CA    . THR   B  1  608  ? 28.876  22.157  61.412  1.00 16.27 ? 606  THR   B CA    1 
ATOM   13475 C  C     . THR   B  1  608  ? 28.747  23.668  61.436  1.00 16.46 ? 606  THR   B C     1 
ATOM   13476 O  O     . THR   B  1  608  ? 27.644  24.203  61.305  1.00 16.47 ? 606  THR   B O     1 
ATOM   13477 C  CB    . THR   B  1  608  ? 28.389  21.579  60.091  1.00 18.21 ? 606  THR   B CB    1 
ATOM   13478 O  OG1   . THR   B  1  608  ? 28.549  20.161  60.135  1.00 18.83 ? 606  THR   B OG1   1 
ATOM   13479 C  CG2   . THR   B  1  608  ? 29.191  22.131  58.939  1.00 19.23 ? 606  THR   B CG2   1 
ATOM   13480 N  N     . GLU   B  1  609  ? 29.861  24.346  61.635  1.00 17.06 ? 607  GLU   B N     1 
ATOM   13481 C  CA    . GLU   B  1  609  ? 29.812  25.776  61.841  1.00 18.45 ? 607  GLU   B CA    1 
ATOM   13482 C  C     . GLU   B  1  609  ? 29.992  26.521  60.524  1.00 16.29 ? 607  GLU   B C     1 
ATOM   13483 O  O     . GLU   B  1  609  ? 30.526  26.002  59.541  1.00 18.84 ? 607  GLU   B O     1 
ATOM   13484 C  CB    . GLU   B  1  609  ? 30.792  26.190  62.943  1.00 21.38 ? 607  GLU   B CB    1 
ATOM   13485 C  CG    . GLU   B  1  609  ? 30.380  25.561  64.281  1.00 21.47 ? 607  GLU   B CG    1 
ATOM   13486 C  CD    . GLU   B  1  609  ? 31.212  26.001  65.466  1.00 26.81 ? 607  GLU   B CD    1 
ATOM   13487 O  OE1   . GLU   B  1  609  ? 32.423  26.245  65.283  1.00 31.27 ? 607  GLU   B OE1   1 
ATOM   13488 O  OE2   . GLU   B  1  609  ? 30.658  26.100  66.580  1.00 24.88 ? 607  GLU   B OE2   1 
ATOM   13489 N  N     . THR   B  1  610  ? 29.505  27.748  60.515  1.00 16.34 ? 608  THR   B N     1 
ATOM   13490 C  CA    . THR   B  1  610  ? 29.335  28.518  59.295  1.00 16.52 ? 608  THR   B CA    1 
ATOM   13491 C  C     . THR   B  1  610  ? 30.600  29.306  59.012  1.00 17.40 ? 608  THR   B C     1 
ATOM   13492 O  O     . THR   B  1  610  ? 31.128  29.977  59.901  1.00 18.11 ? 608  THR   B O     1 
ATOM   13493 C  CB    . THR   B  1  610  ? 28.196  29.509  59.508  1.00 16.56 ? 608  THR   B CB    1 
ATOM   13494 O  OG1   . THR   B  1  610  ? 27.021  28.818  59.962  1.00 15.94 ? 608  THR   B OG1   1 
ATOM   13495 C  CG2   . THR   B  1  610  ? 27.887  30.228  58.207  1.00 17.13 ? 608  THR   B CG2   1 
ATOM   13496 N  N     . SER   B  1  611  ? 31.067  29.258  57.775  1.00 17.38 ? 609  SER   B N     1 
ATOM   13497 C  CA    . SER   B  1  611  ? 32.156  30.146  57.399  1.00 18.18 ? 609  SER   B CA    1 
ATOM   13498 C  C     . SER   B  1  611  ? 31.654  31.580  57.323  1.00 21.08 ? 609  SER   B C     1 
ATOM   13499 O  O     . SER   B  1  611  ? 30.471  31.838  57.088  1.00 17.74 ? 609  SER   B O     1 
ATOM   13500 C  CB    . SER   B  1  611  ? 32.719  29.741  56.041  1.00 20.30 ? 609  SER   B CB    1 
ATOM   13501 O  OG    . SER   B  1  611  ? 31.826  30.091  55.000  1.00 20.58 ? 609  SER   B OG    1 
ATOM   13502 N  N     . GLU   B  1  612  ? 32.566  32.530  57.529  1.00 19.97 ? 610  GLU   B N     1 
ATOM   13503 C  CA    . GLU   B  1  612  ? 32.180  33.928  57.391  1.00 21.07 ? 610  GLU   B CA    1 
ATOM   13504 C  C     . GLU   B  1  612  ? 31.676  34.231  55.985  1.00 21.82 ? 610  GLU   B C     1 
ATOM   13505 O  O     . GLU   B  1  612  ? 30.756  35.042  55.817  1.00 21.66 ? 610  GLU   B O     1 
ATOM   13506 C  CB    . GLU   B  1  612  ? 33.334  34.848  57.802  1.00 25.34 ? 610  GLU   B CB    1 
ATOM   13507 C  CG    . GLU   B  1  612  ? 33.658  34.761  59.293  1.00 27.63 ? 610  GLU   B CG    1 
ATOM   13508 C  CD    . GLU   B  1  612  ? 34.878  35.585  59.683  1.00 34.78 ? 610  GLU   B CD    1 
ATOM   13509 O  OE1   . GLU   B  1  612  ? 35.264  36.487  58.905  1.00 50.04 ? 610  GLU   B OE1   1 
ATOM   13510 O  OE2   . GLU   B  1  612  ? 35.451  35.325  60.764  1.00 37.86 ? 610  GLU   B OE2   1 
ATOM   13511 N  N     . GLU   B  1  613  ? 32.240  33.574  54.971  1.00 21.50 ? 611  GLU   B N     1 
ATOM   13512 C  CA    . GLU   B  1  613  ? 31.743  33.764  53.613  1.00 21.31 ? 611  GLU   B CA    1 
ATOM   13513 C  C     . GLU   B  1  613  ? 30.303  33.280  53.486  1.00 20.38 ? 611  GLU   B C     1 
ATOM   13514 O  O     . GLU   B  1  613  ? 29.481  33.921  52.824  1.00 21.52 ? 611  GLU   B O     1 
ATOM   13515 C  CB    . GLU   B  1  613  ? 32.652  33.058  52.602  1.00 24.06 ? 611  GLU   B CB    1 
ATOM   13516 N  N     . ASP   B  1  614  ? 29.979  32.142  54.099  1.00 18.85 ? 612  ASP   B N     1 
ATOM   13517 C  CA    . ASP   B  1  614  ? 28.606  31.661  54.004  1.00 17.82 ? 612  ASP   B CA    1 
ATOM   13518 C  C     . ASP   B  1  614  ? 27.660  32.489  54.857  1.00 18.05 ? 612  ASP   B C     1 
ATOM   13519 O  O     . ASP   B  1  614  ? 26.478  32.611  54.521  1.00 17.69 ? 612  ASP   B O     1 
ATOM   13520 C  CB    . ASP   B  1  614  ? 28.522  30.181  54.356  1.00 18.92 ? 612  ASP   B CB    1 
ATOM   13521 C  CG    . ASP   B  1  614  ? 29.023  29.294  53.230  1.00 23.00 ? 612  ASP   B CG    1 
ATOM   13522 O  OD1   . ASP   B  1  614  ? 28.969  29.726  52.053  1.00 27.72 ? 612  ASP   B OD1   1 
ATOM   13523 O  OD2   . ASP   B  1  614  ? 29.475  28.171  53.515  1.00 23.16 ? 612  ASP   B OD2   1 
ATOM   13524 N  N     . ALA   B  1  615  ? 28.149  33.071  55.952  1.00 17.68 ? 613  ALA   B N     1 
ATOM   13525 C  CA    . ALA   B  1  615  ? 27.323  34.007  56.702  1.00 15.99 ? 613  ALA   B CA    1 
ATOM   13526 C  C     . ALA   B  1  615  ? 26.919  35.181  55.825  1.00 17.43 ? 613  ALA   B C     1 
ATOM   13527 O  O     . ALA   B  1  615  ? 25.746  35.556  55.772  1.00 17.17 ? 613  ALA   B O     1 
ATOM   13528 C  CB    . ALA   B  1  615  ? 28.060  34.483  57.954  1.00 18.08 ? 613  ALA   B CB    1 
ATOM   13529 N  N     . ARG   B  1  616  ? 27.878  35.753  55.098  1.00 20.00 ? 614  ARG   B N     1 
ATOM   13530 C  CA    . ARG   B  1  616  ? 27.559  36.856  54.200  1.00 18.50 ? 614  ARG   B CA    1 
ATOM   13531 C  C     . ARG   B  1  616  ? 26.648  36.402  53.069  1.00 17.58 ? 614  ARG   B C     1 
ATOM   13532 O  O     . ARG   B  1  616  ? 25.723  37.126  52.677  1.00 18.66 ? 614  ARG   B O     1 
ATOM   13533 C  CB    . ARG   B  1  616  ? 28.848  37.483  53.670  1.00 21.65 ? 614  ARG   B CB    1 
ATOM   13534 C  CG    . ARG   B  1  616  ? 29.510  38.372  54.714  1.00 23.79 ? 614  ARG   B CG    1 
ATOM   13535 C  CD    . ARG   B  1  616  ? 30.686  39.123  54.120  1.00 29.37 ? 614  ARG   B CD    1 
ATOM   13536 N  NE    . ARG   B  1  616  ? 31.818  38.234  53.909  1.00 31.09 ? 614  ARG   B NE    1 
ATOM   13537 C  CZ    . ARG   B  1  616  ? 32.663  37.869  54.862  1.00 32.31 ? 614  ARG   B CZ    1 
ATOM   13538 N  NH1   . ARG   B  1  616  ? 32.531  38.304  56.106  1.00 30.42 ? 614  ARG   B NH1   1 
ATOM   13539 N  NH2   . ARG   B  1  616  ? 33.661  37.045  54.560  1.00 30.81 ? 614  ARG   B NH2   1 
ATOM   13540 N  N     . ARG   B  1  617  ? 26.894  35.207  52.534  1.00 17.33 ? 615  ARG   B N     1 
ATOM   13541 C  CA    . ARG   B  1  617  ? 26.009  34.678  51.505  1.00 18.68 ? 615  ARG   B CA    1 
ATOM   13542 C  C     . ARG   B  1  617  ? 24.588  34.547  52.035  1.00 17.45 ? 615  ARG   B C     1 
ATOM   13543 O  O     . ARG   B  1  617  ? 23.619  34.870  51.341  1.00 18.01 ? 615  ARG   B O     1 
ATOM   13544 C  CB    . ARG   B  1  617  ? 26.522  33.323  51.006  1.00 21.33 ? 615  ARG   B CB    1 
ATOM   13545 C  CG    . ARG   B  1  617  ? 25.706  32.760  49.848  1.00 23.93 ? 615  ARG   B CG    1 
ATOM   13546 C  CD    . ARG   B  1  617  ? 26.477  31.701  49.069  1.00 28.93 ? 615  ARG   B CD    1 
ATOM   13547 N  NE    . ARG   B  1  617  ? 26.642  30.451  49.801  1.00 32.81 ? 615  ARG   B NE    1 
ATOM   13548 C  CZ    . ARG   B  1  617  ? 25.811  29.420  49.717  1.00 38.51 ? 615  ARG   B CZ    1 
ATOM   13549 N  NH1   . ARG   B  1  617  ? 24.722  29.469  48.962  1.00 36.19 ? 615  ARG   B NH1   1 
ATOM   13550 N  NH2   . ARG   B  1  617  ? 26.074  28.316  50.412  1.00 38.49 ? 615  ARG   B NH2   1 
ATOM   13551 N  N     . ALA   B  1  618  ? 24.442  34.088  53.276  1.00 16.81 ? 616  ALA   B N     1 
ATOM   13552 C  CA    . ALA   B  1  618  ? 23.107  33.943  53.840  1.00 14.87 ? 616  ALA   B CA    1 
ATOM   13553 C  C     . ALA   B  1  618  ? 22.380  35.278  53.893  1.00 16.03 ? 616  ALA   B C     1 
ATOM   13554 O  O     . ALA   B  1  618  ? 21.177  35.353  53.617  1.00 16.16 ? 616  ALA   B O     1 
ATOM   13555 C  CB    . ALA   B  1  618  ? 23.211  33.326  55.229  1.00 15.73 ? 616  ALA   B CB    1 
ATOM   13556 N  N     . VAL   B  1  619  ? 23.078  36.342  54.283  1.00 16.96 ? 617  VAL   B N     1 
ATOM   13557 C  CA    . VAL   B  1  619  ? 22.420  37.640  54.357  1.00 15.50 ? 617  VAL   B CA    1 
ATOM   13558 C  C     . VAL   B  1  619  ? 21.978  38.080  52.974  1.00 16.47 ? 617  VAL   B C     1 
ATOM   13559 O  O     . VAL   B  1  619  ? 20.889  38.635  52.801  1.00 18.45 ? 617  VAL   B O     1 
ATOM   13560 C  CB    . VAL   B  1  619  ? 23.317  38.681  55.050  1.00 15.55 ? 617  VAL   B CB    1 
ATOM   13561 C  CG1   . VAL   B  1  619  ? 22.626  40.037  55.102  1.00 18.44 ? 617  VAL   B CG1   1 
ATOM   13562 C  CG2   . VAL   B  1  619  ? 23.661  38.217  56.453  1.00 18.17 ? 617  VAL   B CG2   1 
ATOM   13563 N  N     . ARG   B  1  620  ? 22.813  37.828  51.965  1.00 18.15 ? 618  ARG   B N     1 
ATOM   13564 C  CA    . ARG   B  1  620  ? 22.429  38.158  50.600  1.00 19.99 ? 618  ARG   B CA    1 
ATOM   13565 C  C     . ARG   B  1  620  ? 21.193  37.377  50.181  1.00 16.96 ? 618  ARG   B C     1 
ATOM   13566 O  O     . ARG   B  1  620  ? 20.279  37.931  49.561  1.00 18.01 ? 618  ARG   B O     1 
ATOM   13567 C  CB    . ARG   B  1  620  ? 23.594  37.865  49.658  1.00 21.76 ? 618  ARG   B CB    1 
ATOM   13568 C  CG    . ARG   B  1  620  ? 23.971  39.032  48.773  1.00 39.16 ? 618  ARG   B CG    1 
ATOM   13569 C  CD    . ARG   B  1  620  ? 25.192  38.719  47.917  1.00 36.68 ? 618  ARG   B CD    1 
ATOM   13570 N  NE    . ARG   B  1  620  ? 26.343  38.342  48.728  1.00 38.22 ? 618  ARG   B NE    1 
ATOM   13571 C  CZ    . ARG   B  1  620  ? 26.903  37.140  48.727  1.00 41.80 ? 618  ARG   B CZ    1 
ATOM   13572 N  NH1   . ARG   B  1  620  ? 26.460  36.169  47.940  1.00 40.58 ? 618  ARG   B NH1   1 
ATOM   13573 N  NH2   . ARG   B  1  620  ? 27.939  36.908  49.529  1.00 32.30 ? 618  ARG   B NH2   1 
ATOM   13574 N  N     . LEU   B  1  621  ? 21.147  36.086  50.512  1.00 16.76 ? 619  LEU   B N     1 
ATOM   13575 C  CA    . LEU   B  1  621  ? 19.978  35.282  50.186  1.00 17.41 ? 619  LEU   B CA    1 
ATOM   13576 C  C     . LEU   B  1  621  ? 18.745  35.793  50.910  1.00 17.84 ? 619  LEU   B C     1 
ATOM   13577 O  O     . LEU   B  1  621  ? 17.645  35.792  50.345  1.00 18.92 ? 619  LEU   B O     1 
ATOM   13578 C  CB    . LEU   B  1  621  ? 20.226  33.818  50.545  1.00 18.01 ? 619  LEU   B CB    1 
ATOM   13579 C  CG    . LEU   B  1  621  ? 21.277  33.100  49.692  1.00 19.33 ? 619  LEU   B CG    1 
ATOM   13580 C  CD1   . LEU   B  1  621  ? 21.645  31.739  50.289  1.00 21.69 ? 619  LEU   B CD1   1 
ATOM   13581 C  CD2   . LEU   B  1  621  ? 20.783  32.947  48.247  1.00 23.60 ? 619  LEU   B CD2   1 
ATOM   13582 N  N     . ALA   B  1  622  ? 18.904  36.216  52.170  1.00 16.80 ? 620  ALA   B N     1 
ATOM   13583 C  CA    . ALA   B  1  622  ? 17.782  36.787  52.908  1.00 17.25 ? 620  ALA   B CA    1 
ATOM   13584 C  C     . ALA   B  1  622  ? 17.309  38.084  52.260  1.00 16.07 ? 620  ALA   B C     1 
ATOM   13585 O  O     . ALA   B  1  622  ? 16.102  38.325  52.139  1.00 16.33 ? 620  ALA   B O     1 
ATOM   13586 C  CB    . ALA   B  1  622  ? 18.177  37.017  54.370  1.00 16.63 ? 620  ALA   B CB    1 
ATOM   13587 N  N     . ALA   B  1  623  ? 18.247  38.926  51.827  1.00 15.64 ? 621  ALA   B N     1 
ATOM   13588 C  CA    . ALA   B  1  623  ? 17.858  40.173  51.177  1.00 16.12 ? 621  ALA   B CA    1 
ATOM   13589 C  C     . ALA   B  1  623  ? 17.092  39.898  49.891  1.00 17.50 ? 621  ALA   B C     1 
ATOM   13590 O  O     . ALA   B  1  623  ? 16.071  40.544  49.617  1.00 18.42 ? 621  ALA   B O     1 
ATOM   13591 C  CB    . ALA   B  1  623  ? 19.099  41.016  50.903  1.00 17.67 ? 621  ALA   B CB    1 
ATOM   13592 N  N     . ASP   B  1  624  ? 17.534  38.899  49.122  1.00 18.32 ? 622  ASP   B N     1 
ATOM   13593 C  CA    . ASP   B  1  624  ? 16.866  38.580  47.864  1.00 18.88 ? 622  ASP   B CA    1 
ATOM   13594 C  C     . ASP   B  1  624  ? 15.423  38.165  48.098  1.00 20.54 ? 622  ASP   B C     1 
ATOM   13595 O  O     . ASP   B  1  624  ? 14.532  38.516  47.314  1.00 26.40 ? 622  ASP   B O     1 
ATOM   13596 C  CB    . ASP   B  1  624  ? 17.609  37.448  47.155  1.00 23.90 ? 622  ASP   B CB    1 
ATOM   13597 C  CG    . ASP   B  1  624  ? 18.974  37.857  46.651  1.00 29.90 ? 622  ASP   B CG    1 
ATOM   13598 O  OD1   . ASP   B  1  624  ? 19.249  39.071  46.551  1.00 35.54 ? 622  ASP   B OD1   1 
ATOM   13599 O  OD2   . ASP   B  1  624  ? 19.776  36.947  46.347  1.00 34.36 ? 622  ASP   B OD2   1 
ATOM   13600 N  N     . ALA   B  1  625  ? 15.175  37.417  49.161  1.00 24.56 ? 623  ALA   B N     1 
ATOM   13601 C  CA    . ALA   B  1  625  ? 13.849  36.894  49.441  1.00 28.74 ? 623  ALA   B CA    1 
ATOM   13602 C  C     . ALA   B  1  625  ? 13.047  37.789  50.368  1.00 24.32 ? 623  ALA   B C     1 
ATOM   13603 O  O     . ALA   B  1  625  ? 11.900  37.462  50.693  1.00 23.00 ? 623  ALA   B O     1 
ATOM   13604 C  CB    . ALA   B  1  625  ? 13.964  35.507  50.053  1.00 34.96 ? 623  ALA   B CB    1 
ATOM   13605 N  N     . ALA   B  1  626  ? 13.616  38.902  50.810  1.00 19.32 ? 624  ALA   B N     1 
ATOM   13606 C  CA    . ALA   B  1  626  ? 12.887  39.768  51.733  1.00 18.50 ? 624  ALA   B CA    1 
ATOM   13607 C  C     . ALA   B  1  626  ? 11.544  40.227  51.183  1.00 18.49 ? 624  ALA   B C     1 
ATOM   13608 O  O     . ALA   B  1  626  ? 10.548  40.169  51.926  1.00 19.39 ? 624  ALA   B O     1 
ATOM   13609 C  CB    . ALA   B  1  626  ? 13.780  40.919  52.207  1.00 17.85 ? 624  ALA   B CB    1 
ATOM   13610 N  N     . PRO   B  1  627  ? 11.422  40.660  49.926  1.00 18.45 ? 625  PRO   B N     1 
ATOM   13611 C  CA    . PRO   B  1  627  ? 10.094  41.083  49.457  1.00 19.35 ? 625  PRO   B CA    1 
ATOM   13612 C  C     . PRO   B  1  627  ? 9.067   39.970  49.469  1.00 19.36 ? 625  PRO   B C     1 
ATOM   13613 O  O     . PRO   B  1  627  ? 7.896   40.229  49.774  1.00 19.41 ? 625  PRO   B O     1 
ATOM   13614 C  CB    . PRO   B  1  627  ? 10.359  41.591  48.031  1.00 21.37 ? 625  PRO   B CB    1 
ATOM   13615 C  CG    . PRO   B  1  627  ? 11.810  41.895  47.989  1.00 27.17 ? 625  PRO   B CG    1 
ATOM   13616 C  CD    . PRO   B  1  627  ? 12.474  40.932  48.927  1.00 20.29 ? 625  PRO   B CD    1 
ATOM   13617 N  N     . ASP   B  1  628  ? 9.454   38.739  49.129  1.00 19.11 ? 626  ASP   B N     1 
ATOM   13618 C  CA    . ASP   B  1  628  ? 8.466   37.666  49.079  1.00 20.89 ? 626  ASP   B CA    1 
ATOM   13619 C  C     . ASP   B  1  628  ? 7.927   37.350  50.465  1.00 19.99 ? 626  ASP   B C     1 
ATOM   13620 O  O     . ASP   B  1  628  ? 6.734   37.067  50.623  1.00 21.11 ? 626  ASP   B O     1 
ATOM   13621 C  CB    . ASP   B  1  628  ? 9.054   36.407  48.446  1.00 21.07 ? 626  ASP   B CB    1 
ATOM   13622 C  CG    . ASP   B  1  628  ? 9.403   36.594  46.987  1.00 28.71 ? 626  ASP   B CG    1 
ATOM   13623 O  OD1   . ASP   B  1  628  ? 8.750   37.422  46.313  1.00 30.20 ? 626  ASP   B OD1   1 
ATOM   13624 O  OD2   . ASP   B  1  628  ? 10.341  35.916  46.532  1.00 35.66 ? 626  ASP   B OD2   1 
ATOM   13625 N  N     . TRP   B  1  629  ? 8.786   37.392  51.482  1.00 16.82 ? 627  TRP   B N     1 
ATOM   13626 C  CA    . TRP   B  1  629  ? 8.307   37.131  52.832  1.00 16.93 ? 627  TRP   B CA    1 
ATOM   13627 C  C     . TRP   B  1  629  ? 7.477   38.294  53.354  1.00 16.37 ? 627  TRP   B C     1 
ATOM   13628 O  O     . TRP   B  1  629  ? 6.434   38.083  53.984  1.00 16.60 ? 627  TRP   B O     1 
ATOM   13629 C  CB    . TRP   B  1  629  ? 9.482   36.817  53.751  1.00 16.30 ? 627  TRP   B CB    1 
ATOM   13630 C  CG    . TRP   B  1  629  ? 9.042   36.534  55.136  1.00 13.64 ? 627  TRP   B CG    1 
ATOM   13631 C  CD1   . TRP   B  1  629  ? 9.407   37.220  56.264  1.00 15.17 ? 627  TRP   B CD1   1 
ATOM   13632 C  CD2   . TRP   B  1  629  ? 8.139   35.507  55.566  1.00 14.64 ? 627  TRP   B CD2   1 
ATOM   13633 N  NE1   . TRP   B  1  629  ? 8.794   36.677  57.361  1.00 15.04 ? 627  TRP   B NE1   1 
ATOM   13634 C  CE2   . TRP   B  1  629  ? 8.009   35.627  56.965  1.00 13.67 ? 627  TRP   B CE2   1 
ATOM   13635 C  CE3   . TRP   B  1  629  ? 7.421   34.501  54.907  1.00 16.23 ? 627  TRP   B CE3   1 
ATOM   13636 C  CZ2   . TRP   B  1  629  ? 7.192   34.785  57.709  1.00 14.81 ? 627  TRP   B CZ2   1 
ATOM   13637 C  CZ3   . TRP   B  1  629  ? 6.613   33.668  55.656  1.00 16.39 ? 627  TRP   B CZ3   1 
ATOM   13638 C  CH2   . TRP   B  1  629  ? 6.505   33.813  57.040  1.00 16.86 ? 627  TRP   B CH2   1 
ATOM   13639 N  N     . ALA   B  1  630  ? 7.901   39.526  53.072  1.00 16.21 ? 628  ALA   B N     1 
ATOM   13640 C  CA    . ALA   B  1  630  ? 7.122   40.688  53.485  1.00 17.08 ? 628  ALA   B CA    1 
ATOM   13641 C  C     . ALA   B  1  630  ? 5.726   40.656  52.888  1.00 16.67 ? 628  ALA   B C     1 
ATOM   13642 O  O     . ALA   B  1  630  ? 4.774   41.149  53.503  1.00 19.61 ? 628  ALA   B O     1 
ATOM   13643 C  CB    . ALA   B  1  630  ? 7.837   41.969  53.066  1.00 18.76 ? 628  ALA   B CB    1 
ATOM   13644 N  N     . ALA   B  1  631  ? 5.586   40.074  51.694  1.00 17.57 ? 629  ALA   B N     1 
ATOM   13645 C  CA    . ALA   B  1  631  ? 4.298   40.005  51.018  1.00 18.28 ? 629  ALA   B CA    1 
ATOM   13646 C  C     . ALA   B  1  631  ? 3.382   38.932  51.579  1.00 18.94 ? 629  ALA   B C     1 
ATOM   13647 O  O     . ALA   B  1  631  ? 2.191   38.931  51.253  1.00 20.27 ? 629  ALA   B O     1 
ATOM   13648 C  CB    . ALA   B  1  631  ? 4.519   39.750  49.526  1.00 20.49 ? 629  ALA   B CB    1 
ATOM   13649 N  N     . VAL   B  1  632  ? 3.883   38.044  52.429  1.00 17.08 ? 630  VAL   B N     1 
ATOM   13650 C  CA    . VAL   B  1  632  ? 2.976   37.095  53.072  1.00 16.41 ? 630  VAL   B CA    1 
ATOM   13651 C  C     . VAL   B  1  632  ? 2.165   37.862  54.102  1.00 17.93 ? 630  VAL   B C     1 
ATOM   13652 O  O     . VAL   B  1  632  ? 2.765   38.538  54.959  1.00 18.34 ? 630  VAL   B O     1 
ATOM   13653 C  CB    . VAL   B  1  632  ? 3.770   35.960  53.735  1.00 18.03 ? 630  VAL   B CB    1 
ATOM   13654 C  CG1   . VAL   B  1  632  ? 2.820   35.055  54.508  1.00 17.06 ? 630  VAL   B CG1   1 
ATOM   13655 C  CG2   . VAL   B  1  632  ? 4.545   35.180  52.702  1.00 17.55 ? 630  VAL   B CG2   1 
ATOM   13656 N  N     . PRO   B  1  633  ? 0.839   37.813  54.058  1.00 17.39 ? 631  PRO   B N     1 
ATOM   13657 C  CA    . PRO   B  1  633  ? 0.045   38.645  54.950  1.00 19.27 ? 631  PRO   B CA    1 
ATOM   13658 C  C     . PRO   B  1  633  ? 0.394   38.375  56.399  1.00 17.26 ? 631  PRO   B C     1 
ATOM   13659 O  O     . PRO   B  1  633  ? 0.666   37.230  56.782  1.00 16.32 ? 631  PRO   B O     1 
ATOM   13660 C  CB    . PRO   B  1  633  ? -1.387  38.200  54.650  1.00 18.82 ? 631  PRO   B CB    1 
ATOM   13661 C  CG    . PRO   B  1  633  ? -1.343  37.783  53.205  1.00 20.20 ? 631  PRO   B CG    1 
ATOM   13662 C  CD    . PRO   B  1  633  ? 0.012   37.106  53.067  1.00 16.63 ? 631  PRO   B CD    1 
ATOM   13663 N  N     . PRO   B  1  634  ? 0.378   39.406  57.234  1.00 16.39 ? 632  PRO   B N     1 
ATOM   13664 C  CA    . PRO   B  1  634  ? 0.677   39.203  58.660  1.00 16.90 ? 632  PRO   B CA    1 
ATOM   13665 C  C     . PRO   B  1  634  ? -0.099  38.070  59.301  1.00 16.88 ? 632  PRO   B C     1 
ATOM   13666 O  O     . PRO   B  1  634  ? 0.483   37.319  60.091  1.00 15.96 ? 632  PRO   B O     1 
ATOM   13667 C  CB    . PRO   B  1  634  ? 0.348   40.565  59.287  1.00 18.65 ? 632  PRO   B CB    1 
ATOM   13668 C  CG    . PRO   B  1  634  ? 0.543   41.535  58.177  1.00 21.21 ? 632  PRO   B CG    1 
ATOM   13669 C  CD    . PRO   B  1  634  ? 0.161   40.822  56.901  1.00 18.34 ? 632  PRO   B CD    1 
ATOM   13670 N  N     . SER   B  1  635  ? -1.384  37.909  58.993  1.00 17.56 ? 633  SER   B N     1 
ATOM   13671 C  CA    . SER   B  1  635  ? -2.131  36.830  59.626  1.00 18.58 ? 633  SER   B CA    1 
ATOM   13672 C  C     . SER   B  1  635  ? -1.601  35.467  59.208  1.00 16.79 ? 633  SER   B C     1 
ATOM   13673 O  O     . SER   B  1  635  ? -1.627  34.524  60.007  1.00 16.56 ? 633  SER   B O     1 
ATOM   13674 C  CB    . SER   B  1  635  ? -3.621  36.942  59.300  1.00 21.33 ? 633  SER   B CB    1 
ATOM   13675 O  OG    . SER   B  1  635  ? -3.836  36.775  57.914  1.00 29.91 ? 633  SER   B OG    1 
ATOM   13676 N  N     . GLU   B  1  636  ? -1.106  35.348  57.972  1.00 16.87 ? 634  GLU   B N     1 
ATOM   13677 C  CA    . GLU   B  1  636  ? -0.530  34.081  57.538  1.00 15.76 ? 634  GLU   B CA    1 
ATOM   13678 C  C     . GLU   B  1  636  ? 0.856   33.873  58.132  1.00 16.08 ? 634  GLU   B C     1 
ATOM   13679 O  O     . GLU   B  1  636  ? 1.218   32.742  58.474  1.00 15.43 ? 634  GLU   B O     1 
ATOM   13680 C  CB    . GLU   B  1  636  ? -0.476  34.001  56.011  1.00 16.47 ? 634  GLU   B CB    1 
ATOM   13681 C  CG    . GLU   B  1  636  ? 0.148   32.695  55.501  1.00 28.93 ? 634  GLU   B CG    1 
ATOM   13682 C  CD    . GLU   B  1  636  ? -0.432  31.449  56.179  1.00 33.35 ? 634  GLU   B CD    1 
ATOM   13683 O  OE1   . GLU   B  1  636  ? -1.680  31.344  56.268  1.00 31.36 ? 634  GLU   B OE1   1 
ATOM   13684 O  OE2   . GLU   B  1  636  ? 0.361   30.583  56.636  1.00 29.48 ? 634  GLU   B OE2   1 
ATOM   13685 N  N     . ARG   B  1  637  ? 1.635   34.944  58.288  1.00 13.69 ? 635  ARG   B N     1 
ATOM   13686 C  CA    . ARG   B  1  637  ? 2.893   34.792  59.009  1.00 14.54 ? 635  ARG   B CA    1 
ATOM   13687 C  C     . ARG   B  1  637  ? 2.627   34.355  60.440  1.00 13.77 ? 635  ARG   B C     1 
ATOM   13688 O  O     . ARG   B  1  637  ? 3.288   33.444  60.956  1.00 14.98 ? 635  ARG   B O     1 
ATOM   13689 C  CB    . ARG   B  1  637  ? 3.689   36.091  58.967  1.00 14.41 ? 635  ARG   B CB    1 
ATOM   13690 C  CG    . ARG   B  1  637  ? 3.940   36.578  57.551  1.00 14.83 ? 635  ARG   B CG    1 
ATOM   13691 C  CD    . ARG   B  1  637  ? 5.003   37.651  57.506  1.00 15.17 ? 635  ARG   B CD    1 
ATOM   13692 N  NE    . ARG   B  1  637  ? 4.628   38.803  58.311  1.00 15.79 ? 635  ARG   B NE    1 
ATOM   13693 C  CZ    . ARG   B  1  637  ? 4.392   40.021  57.844  1.00 16.38 ? 635  ARG   B CZ    1 
ATOM   13694 N  NH1   . ARG   B  1  637  ? 4.311   40.265  56.546  1.00 21.36 ? 635  ARG   B NH1   1 
ATOM   13695 N  NH2   . ARG   B  1  637  ? 4.251   41.026  58.702  1.00 16.52 ? 635  ARG   B NH2   1 
ATOM   13696 N  N     . ALA   B  1  638  ? 1.608   34.947  61.067  1.00 12.92 ? 636  ALA   B N     1 
ATOM   13697 C  CA    . ALA   B  1  638  ? 1.230   34.562  62.418  1.00 13.69 ? 636  ALA   B CA    1 
ATOM   13698 C  C     . ALA   B  1  638  ? 0.769   33.113  62.470  1.00 13.44 ? 636  ALA   B C     1 
ATOM   13699 O  O     . ALA   B  1  638  ? 1.041   32.401  63.440  1.00 13.57 ? 636  ALA   B O     1 
ATOM   13700 C  CB    . ALA   B  1  638  ? 0.153   35.513  62.948  1.00 13.62 ? 636  ALA   B CB    1 
ATOM   13701 N  N     . ALA   B  1  639  ? 0.077   32.650  61.425  1.00 14.39 ? 637  ALA   B N     1 
ATOM   13702 C  CA    . ALA   B  1  639  ? -0.362  31.259  61.405  1.00 14.55 ? 637  ALA   B CA    1 
ATOM   13703 C  C     . ALA   B  1  639  ? 0.818   30.303  61.368  1.00 14.11 ? 637  ALA   B C     1 
ATOM   13704 O  O     . ALA   B  1  639  ? 0.739   29.208  61.929  1.00 14.22 ? 637  ALA   B O     1 
ATOM   13705 C  CB    . ALA   B  1  639  ? -1.280  31.002  60.211  1.00 14.49 ? 637  ALA   B CB    1 
ATOM   13706 N  N     . CYS   B  1  640  ? 1.919   30.695  60.721  1.00 13.91 ? 638  CYS   B N     1 
ATOM   13707 C  CA    . CYS   B  1  640  ? 3.133   29.881  60.766  1.00 13.67 ? 638  CYS   B CA    1 
ATOM   13708 C  C     . CYS   B  1  640  ? 3.644   29.763  62.187  1.00 12.38 ? 638  CYS   B C     1 
ATOM   13709 O  O     . CYS   B  1  640  ? 4.042   28.679  62.625  1.00 13.84 ? 638  CYS   B O     1 
ATOM   13710 C  CB    . CYS   B  1  640  ? 4.242   30.496  59.906  1.00 12.32 ? 638  CYS   B CB    1 
ATOM   13711 S  SG    . CYS   B  1  640  ? 3.925   30.464  58.167  1.00 15.80 ? 638  CYS   B SG    1 
ATOM   13712 N  N     . LEU   B  1  641  ? 3.668   30.879  62.917  1.00 12.33 ? 639  LEU   B N     1 
ATOM   13713 C  CA    . LEU   B  1  641  ? 4.118   30.822  64.299  1.00 13.17 ? 639  LEU   B CA    1 
ATOM   13714 C  C     . LEU   B  1  641  ? 3.217   29.918  65.116  1.00 12.94 ? 639  LEU   B C     1 
ATOM   13715 O  O     . LEU   B  1  641  ? 3.700   29.120  65.930  1.00 13.21 ? 639  LEU   B O     1 
ATOM   13716 C  CB    . LEU   B  1  641  ? 4.126   32.218  64.914  1.00 13.48 ? 639  LEU   B CB    1 
ATOM   13717 C  CG    . LEU   B  1  641  ? 5.380   33.068  64.731  1.00 13.91 ? 639  LEU   B CG    1 
ATOM   13718 C  CD1   . LEU   B  1  641  ? 5.763   33.316  63.271  1.00 18.12 ? 639  LEU   B CD1   1 
ATOM   13719 C  CD2   . LEU   B  1  641  ? 5.212   34.373  65.476  1.00 12.93 ? 639  LEU   B CD2   1 
ATOM   13720 N  N     . ASP   B  1  642  ? 1.898   30.037  64.929  1.00 12.90 ? 640  ASP   B N     1 
ATOM   13721 C  CA    . ASP   B  1  642  ? 0.987   29.185  65.680  1.00 13.70 ? 640  ASP   B CA    1 
ATOM   13722 C  C     . ASP   B  1  642  ? 1.172   27.722  65.318  1.00 12.87 ? 640  ASP   B C     1 
ATOM   13723 O  O     . ASP   B  1  642  ? 1.104   26.849  66.188  1.00 13.61 ? 640  ASP   B O     1 
ATOM   13724 C  CB    . ASP   B  1  642  ? -0.459  29.599  65.445  1.00 14.11 ? 640  ASP   B CB    1 
ATOM   13725 C  CG    . ASP   B  1  642  ? -0.865  30.806  66.240  1.00 16.44 ? 640  ASP   B CG    1 
ATOM   13726 O  OD1   . ASP   B  1  642  ? -0.236  31.107  67.272  1.00 16.07 ? 640  ASP   B OD1   1 
ATOM   13727 O  OD2   . ASP   B  1  642  ? -1.864  31.440  65.843  1.00 16.80 ? 640  ASP   B OD2   1 
ATOM   13728 N  N     . ARG   B  1  643  ? 1.415   27.425  64.038  1.00 13.61 ? 641  ARG   B N     1 
ATOM   13729 C  CA    . ARG   B  1  643  ? 1.682   26.037  63.679  1.00 15.32 ? 641  ARG   B CA    1 
ATOM   13730 C  C     . ARG   B  1  643  ? 2.969   25.548  64.321  1.00 13.81 ? 641  ARG   B C     1 
ATOM   13731 O  O     . ARG   B  1  643  ? 3.040   24.413  64.804  1.00 13.85 ? 641  ARG   B O     1 
ATOM   13732 C  CB    . ARG   B  1  643  ? 1.746   25.878  62.164  1.00 14.91 ? 641  ARG   B CB    1 
ATOM   13733 C  CG    . ARG   B  1  643  ? 0.366   25.749  61.545  1.00 16.46 ? 641  ARG   B CG    1 
ATOM   13734 C  CD    . ARG   B  1  643  ? 0.434   25.377  60.072  1.00 18.31 ? 641  ARG   B CD    1 
ATOM   13735 N  NE    . ARG   B  1  643  ? 1.126   26.401  59.298  1.00 18.41 ? 641  ARG   B NE    1 
ATOM   13736 C  CZ    . ARG   B  1  643  ? 0.542   27.439  58.720  1.00 18.71 ? 641  ARG   B CZ    1 
ATOM   13737 N  NH1   . ARG   B  1  643  ? -0.767  27.630  58.803  1.00 19.91 ? 641  ARG   B NH1   1 
ATOM   13738 N  NH2   . ARG   B  1  643  ? 1.287   28.304  58.035  1.00 21.22 ? 641  ARG   B NH2   1 
ATOM   13739 N  N     . ALA   B  1  644  ? 3.991   26.400  64.362  1.00 12.46 ? 642  ALA   B N     1 
ATOM   13740 C  CA    . ALA   B  1  644  ? 5.233   25.986  65.000  1.00 13.14 ? 642  ALA   B CA    1 
ATOM   13741 C  C     . ALA   B  1  644  ? 5.019   25.710  66.477  1.00 13.96 ? 642  ALA   B C     1 
ATOM   13742 O  O     . ALA   B  1  644  ? 5.595   24.767  67.031  1.00 13.31 ? 642  ALA   B O     1 
ATOM   13743 C  CB    . ALA   B  1  644  ? 6.307   27.046  64.795  1.00 13.34 ? 642  ALA   B CB    1 
ATOM   13744 N  N     . ALA   B  1  645  ? 4.159   26.504  67.126  1.00 13.42 ? 643  ALA   B N     1 
ATOM   13745 C  CA    . ALA   B  1  645  ? 3.895   26.285  68.540  1.00 13.15 ? 643  ALA   B CA    1 
ATOM   13746 C  C     . ALA   B  1  645  ? 3.217   24.947  68.757  1.00 12.19 ? 643  ALA   B C     1 
ATOM   13747 O  O     . ALA   B  1  645  ? 3.529   24.241  69.726  1.00 14.36 ? 643  ALA   B O     1 
ATOM   13748 C  CB    . ALA   B  1  645  ? 3.049   27.428  69.099  1.00 13.98 ? 643  ALA   B CB    1 
ATOM   13749 N  N     . GLU   B  1  646  ? 2.298   24.578  67.854  1.00 13.48 ? 644  GLU   B N     1 
ATOM   13750 C  CA    . GLU   B  1  646  ? 1.636   23.280  67.952  1.00 14.89 ? 644  GLU   B CA    1 
ATOM   13751 C  C     . GLU   B  1  646  ? 2.644   22.153  67.834  1.00 14.22 ? 644  GLU   B C     1 
ATOM   13752 O  O     . GLU   B  1  646  ? 2.568   21.154  68.560  1.00 14.63 ? 644  GLU   B O     1 
ATOM   13753 C  CB    . GLU   B  1  646  ? 0.593   23.131  66.840  1.00 16.85 ? 644  GLU   B CB    1 
ATOM   13754 C  CG    . GLU   B  1  646  ? -0.620  24.019  66.979  1.00 21.00 ? 644  GLU   B CG    1 
ATOM   13755 C  CD    . GLU   B  1  646  ? -1.335  23.824  68.291  1.00 28.76 ? 644  GLU   B CD    1 
ATOM   13756 O  OE1   . GLU   B  1  646  ? -1.630  22.665  68.648  1.00 34.37 ? 644  GLU   B OE1   1 
ATOM   13757 O  OE2   . GLU   B  1  646  ? -1.591  24.835  68.976  1.00 29.23 ? 644  GLU   B OE2   1 
ATOM   13758 N  N     . LEU   B  1  647  ? 3.602   22.293  66.916  1.00 14.83 ? 645  LEU   B N     1 
ATOM   13759 C  CA    . LEU   B  1  647  ? 4.599   21.242  66.744  1.00 15.38 ? 645  LEU   B CA    1 
ATOM   13760 C  C     . LEU   B  1  647  ? 5.514   21.158  67.954  1.00 14.43 ? 645  LEU   B C     1 
ATOM   13761 O  O     . LEU   B  1  647  ? 5.815   20.061  68.432  1.00 15.84 ? 645  LEU   B O     1 
ATOM   13762 C  CB    . LEU   B  1  647  ? 5.416   21.497  65.483  1.00 14.47 ? 645  LEU   B CB    1 
ATOM   13763 C  CG    . LEU   B  1  647  ? 4.645   21.482  64.169  1.00 15.52 ? 645  LEU   B CG    1 
ATOM   13764 C  CD1   . LEU   B  1  647  ? 5.591   21.775  63.028  1.00 16.43 ? 645  LEU   B CD1   1 
ATOM   13765 C  CD2   . LEU   B  1  647  ? 3.972   20.131  63.962  1.00 18.58 ? 645  LEU   B CD2   1 
ATOM   13766 N  N     . MET   B  1  648  ? 5.941   22.301  68.488  1.00 13.21 ? 646  MET   B N     1 
ATOM   13767 C  CA    . MET   B  1  648  ? 6.773   22.253  69.686  1.00 12.69 ? 646  MET   B CA    1 
ATOM   13768 C  C     . MET   B  1  648  ? 6.005   21.658  70.856  1.00 13.97 ? 646  MET   B C     1 
ATOM   13769 O  O     . MET   B  1  648  ? 6.574   20.934  71.679  1.00 15.88 ? 646  MET   B O     1 
ATOM   13770 C  CB    . MET   B  1  648  ? 7.269   23.645  70.057  1.00 16.05 ? 646  MET   B CB    1 
ATOM   13771 C  CG    . MET   B  1  648  ? 8.333   24.152  69.138  1.00 14.91 ? 646  MET   B CG    1 
ATOM   13772 S  SD    . MET   B  1  648  ? 9.101   25.568  69.899  1.00 16.37 ? 646  MET   B SD    1 
ATOM   13773 C  CE    . MET   B  1  648  ? 10.160  26.080  68.556  1.00 19.54 ? 646  MET   B CE    1 
ATOM   13774 N  N     . GLN   B  1  649  ? 4.712   21.965  70.963  1.00 14.17 ? 647  GLN   B N     1 
ATOM   13775 C  CA    . GLN   B  1  649  ? 3.935   21.387  72.046  1.00 15.30 ? 647  GLN   B CA    1 
ATOM   13776 C  C     . GLN   B  1  649  ? 3.873   19.871  71.912  1.00 13.77 ? 647  GLN   B C     1 
ATOM   13777 O  O     . GLN   B  1  649  ? 4.082   19.143  72.889  1.00 16.63 ? 647  GLN   B O     1 
ATOM   13778 C  CB    . GLN   B  1  649  ? 2.535   21.984  72.038  1.00 14.23 ? 647  GLN   B CB    1 
ATOM   13779 C  CG    . GLN   B  1  649  ? 1.693   21.557  73.218  1.00 15.76 ? 647  GLN   B CG    1 
ATOM   13780 C  CD    . GLN   B  1  649  ? 2.143   22.216  74.492  1.00 14.85 ? 647  GLN   B CD    1 
ATOM   13781 O  OE1   . GLN   B  1  649  ? 1.842   23.383  74.737  1.00 15.98 ? 647  GLN   B OE1   1 
ATOM   13782 N  NE2   . GLN   B  1  649  ? 2.902   21.490  75.300  1.00 16.00 ? 647  GLN   B NE2   1 
ATOM   13783 N  N     . ALA   B  1  650  ? 3.581   19.381  70.708  1.00 15.24 ? 648  ALA   B N     1 
ATOM   13784 C  CA    . ALA   B  1  650  ? 3.441   17.943  70.504  1.00 16.57 ? 648  ALA   B CA    1 
ATOM   13785 C  C     . ALA   B  1  650  ? 4.765   17.220  70.674  1.00 17.83 ? 648  ALA   B C     1 
ATOM   13786 O  O     . ALA   B  1  650  ? 4.786   16.061  71.102  1.00 19.45 ? 648  ALA   B O     1 
ATOM   13787 C  CB    . ALA   B  1  650  ? 2.870   17.665  69.115  1.00 18.17 ? 648  ALA   B CB    1 
ATOM   13788 N  N     . ARG   B  1  651  ? 5.872   17.879  70.345  1.00 15.78 ? 649  ARG   B N     1 
ATOM   13789 C  CA    . ARG   B  1  651  ? 7.191   17.269  70.399  1.00 14.81 ? 649  ARG   B CA    1 
ATOM   13790 C  C     . ARG   B  1  651  ? 7.947   17.642  71.653  1.00 16.61 ? 649  ARG   B C     1 
ATOM   13791 O  O     . ARG   B  1  651  ? 9.137   17.337  71.770  1.00 16.61 ? 649  ARG   B O     1 
ATOM   13792 C  CB    . ARG   B  1  651  ? 7.965   17.660  69.153  1.00 17.14 ? 649  ARG   B CB    1 
ATOM   13793 C  CG    . ARG   B  1  651  ? 7.251   17.158  67.932  1.00 17.79 ? 649  ARG   B CG    1 
ATOM   13794 C  CD    . ARG   B  1  651  ? 7.852   17.702  66.677  1.00 18.20 ? 649  ARG   B CD    1 
ATOM   13795 N  NE    . ARG   B  1  651  ? 6.991   17.365  65.558  1.00 19.38 ? 649  ARG   B NE    1 
ATOM   13796 C  CZ    . ARG   B  1  651  ? 7.185   17.789  64.322  1.00 18.61 ? 649  ARG   B CZ    1 
ATOM   13797 N  NH1   . ARG   B  1  651  ? 8.261   18.497  63.996  1.00 17.78 ? 649  ARG   B NH1   1 
ATOM   13798 N  NH2   . ARG   B  1  651  ? 6.286   17.493  63.390  1.00 18.70 ? 649  ARG   B NH2   1 
ATOM   13799 N  N     . MET   B  1  652  ? 7.283   18.286  72.599  1.00 14.95 ? 650  MET   B N     1 
ATOM   13800 C  CA    . MET   B  1  652  ? 7.955   18.687  73.830  1.00 15.08 ? 650  MET   B CA    1 
ATOM   13801 C  C     . MET   B  1  652  ? 8.767   17.573  74.473  1.00 16.17 ? 650  MET   B C     1 
ATOM   13802 O  O     . MET   B  1  652  ? 9.907   17.838  74.873  1.00 16.91 ? 650  MET   B O     1 
ATOM   13803 C  CB    . MET   B  1  652  ? 6.944   19.300  74.806  1.00 15.36 ? 650  MET   B CB    1 
ATOM   13804 C  CG    . MET   B  1  652  ? 7.579   19.669  76.122  1.00 15.41 ? 650  MET   B CG    1 
ATOM   13805 S  SD    . MET   B  1  652  ? 6.385   20.375  77.273  1.00 18.25 ? 650  MET   B SD    1 
ATOM   13806 C  CE    . MET   B  1  652  ? 6.146   21.980  76.549  1.00 15.56 ? 650  MET   B CE    1 
ATOM   13807 N  N     . PRO   B  1  653  ? 8.279   16.337  74.602  1.00 15.11 ? 651  PRO   B N     1 
ATOM   13808 C  CA    . PRO   B  1  653  ? 9.109   15.316  75.261  1.00 18.11 ? 651  PRO   B CA    1 
ATOM   13809 C  C     . PRO   B  1  653  ? 10.450  15.111  74.587  1.00 18.01 ? 651  PRO   B C     1 
ATOM   13810 O  O     . PRO   B  1  653  ? 11.465  14.998  75.279  1.00 16.84 ? 651  PRO   B O     1 
ATOM   13811 C  CB    . PRO   B  1  653  ? 8.229   14.059  75.223  1.00 18.03 ? 651  PRO   B CB    1 
ATOM   13812 C  CG    . PRO   B  1  653  ? 6.818   14.599  75.218  1.00 16.52 ? 651  PRO   B CG    1 
ATOM   13813 C  CD    . PRO   B  1  653  ? 6.904   15.857  74.363  1.00 16.53 ? 651  PRO   B CD    1 
ATOM   13814 N  N     . THR   B  1  654  ? 10.483  15.093  73.255  1.00 16.24 ? 652  THR   B N     1 
ATOM   13815 C  CA    . THR   B  1  654  ? 11.747  14.938  72.540  1.00 17.09 ? 652  THR   B CA    1 
ATOM   13816 C  C     . THR   B  1  654  ? 12.619  16.176  72.699  1.00 18.19 ? 652  THR   B C     1 
ATOM   13817 O  O     . THR   B  1  654  ? 13.829  16.067  72.940  1.00 16.87 ? 652  THR   B O     1 
ATOM   13818 C  CB    . THR   B  1  654  ? 11.467  14.669  71.064  1.00 17.74 ? 652  THR   B CB    1 
ATOM   13819 O  OG1   . THR   B  1  654  ? 10.681  13.479  70.952  1.00 20.37 ? 652  THR   B OG1   1 
ATOM   13820 C  CG2   . THR   B  1  654  ? 12.774  14.500  70.281  1.00 19.54 ? 652  THR   B CG2   1 
ATOM   13821 N  N     . LEU   B  1  655  ? 12.026  17.365  72.570  1.00 15.99 ? 653  LEU   B N     1 
ATOM   13822 C  CA    . LEU   B  1  655  ? 12.784  18.595  72.770  1.00 15.91 ? 653  LEU   B CA    1 
ATOM   13823 C  C     . LEU   B  1  655  ? 13.390  18.646  74.164  1.00 17.20 ? 653  LEU   B C     1 
ATOM   13824 O  O     . LEU   B  1  655  ? 14.534  19.083  74.330  1.00 16.96 ? 653  LEU   B O     1 
ATOM   13825 C  CB    . LEU   B  1  655  ? 11.891  19.811  72.542  1.00 15.37 ? 653  LEU   B CB    1 
ATOM   13826 C  CG    . LEU   B  1  655  ? 11.256  19.873  71.157  1.00 18.52 ? 653  LEU   B CG    1 
ATOM   13827 C  CD1   . LEU   B  1  655  ? 10.330  21.064  71.070  1.00 18.42 ? 653  LEU   B CD1   1 
ATOM   13828 C  CD2   . LEU   B  1  655  ? 12.339  19.942  70.104  1.00 21.91 ? 653  LEU   B CD2   1 
ATOM   13829 N  N     . LEU   B  1  656  ? 12.644  18.193  75.175  1.00 16.92 ? 654  LEU   B N     1 
ATOM   13830 C  CA    . LEU   B  1  656  ? 13.173  18.155  76.540  1.00 16.91 ? 654  LEU   B CA    1 
ATOM   13831 C  C     . LEU   B  1  656  ? 14.437  17.334  76.601  1.00 18.35 ? 654  LEU   B C     1 
ATOM   13832 O  O     . LEU   B  1  656  ? 15.420  17.732  77.236  1.00 18.59 ? 654  LEU   B O     1 
ATOM   13833 C  CB    . LEU   B  1  656  ? 12.168  17.498  77.484  1.00 20.22 ? 654  LEU   B CB    1 
ATOM   13834 C  CG    . LEU   B  1  656  ? 10.809  18.129  77.657  1.00 24.55 ? 654  LEU   B CG    1 
ATOM   13835 C  CD1   . LEU   B  1  656  ? 10.086  17.457  78.793  1.00 23.04 ? 654  LEU   B CD1   1 
ATOM   13836 C  CD2   . LEU   B  1  656  ? 10.961  19.607  77.881  1.00 20.95 ? 654  LEU   B CD2   1 
ATOM   13837 N  N     . GLY   B  1  657  ? 14.410  16.155  75.991  1.00 17.01 ? 655  GLY   B N     1 
ATOM   13838 C  CA    . GLY   B  1  657  ? 15.570  15.291  76.033  1.00 19.67 ? 655  GLY   B CA    1 
ATOM   13839 C  C     . GLY   B  1  657  ? 16.790  15.974  75.466  1.00 19.12 ? 655  GLY   B C     1 
ATOM   13840 O  O     . GLY   B  1  657  ? 17.886  15.877  76.022  1.00 18.55 ? 655  GLY   B O     1 
ATOM   13841 N  N     . LEU   B  1  658  ? 16.612  16.702  74.367  1.00 16.84 ? 656  LEU   B N     1 
ATOM   13842 C  CA    . LEU   B  1  658  ? 17.747  17.388  73.782  1.00 14.64 ? 656  LEU   B CA    1 
ATOM   13843 C  C     . LEU   B  1  658  ? 18.223  18.519  74.680  1.00 15.65 ? 656  LEU   B C     1 
ATOM   13844 O  O     . LEU   B  1  658  ? 19.427  18.668  74.917  1.00 16.37 ? 656  LEU   B O     1 
ATOM   13845 C  CB    . LEU   B  1  658  ? 17.372  17.904  72.398  1.00 16.14 ? 656  LEU   B CB    1 
ATOM   13846 C  CG    . LEU   B  1  658  ? 18.524  18.566  71.651  1.00 14.81 ? 656  LEU   B CG    1 
ATOM   13847 C  CD1   . LEU   B  1  658  ? 19.741  17.652  71.509  1.00 16.38 ? 656  LEU   B CD1   1 
ATOM   13848 C  CD2   . LEU   B  1  658  ? 17.993  18.989  70.295  1.00 15.11 ? 656  LEU   B CD2   1 
ATOM   13849 N  N     . ILE   B  1  659  ? 17.300  19.311  75.215  1.00 15.29 ? 657  ILE   B N     1 
ATOM   13850 C  CA    . ILE   B  1  659  ? 17.692  20.436  76.054  1.00 13.89 ? 657  ILE   B CA    1 
ATOM   13851 C  C     . ILE   B  1  659  ? 18.370  19.947  77.323  1.00 14.37 ? 657  ILE   B C     1 
ATOM   13852 O  O     . ILE   B  1  659  ? 19.358  20.528  77.786  1.00 15.52 ? 657  ILE   B O     1 
ATOM   13853 C  CB    . ILE   B  1  659  ? 16.449  21.284  76.367  1.00 14.11 ? 657  ILE   B CB    1 
ATOM   13854 C  CG1   . ILE   B  1  659  ? 15.966  21.950  75.089  1.00 14.96 ? 657  ILE   B CG1   1 
ATOM   13855 C  CG2   . ILE   B  1  659  ? 16.739  22.311  77.449  1.00 17.55 ? 657  ILE   B CG2   1 
ATOM   13856 C  CD1   . ILE   B  1  659  ? 14.536  22.411  75.193  1.00 15.80 ? 657  ILE   B CD1   1 
ATOM   13857 N  N     . ILE   B  1  660  ? 17.849  18.869  77.905  1.00 14.34 ? 658  ILE   B N     1 
ATOM   13858 C  CA    . ILE   B  1  660  ? 18.445  18.317  79.115  1.00 14.03 ? 658  ILE   B CA    1 
ATOM   13859 C  C     . ILE   B  1  660  ? 19.903  17.965  78.873  1.00 15.94 ? 658  ILE   B C     1 
ATOM   13860 O  O     . ILE   B  1  660  ? 20.783  18.280  79.691  1.00 17.44 ? 658  ILE   B O     1 
ATOM   13861 C  CB    . ILE   B  1  660  ? 17.637  17.097  79.584  1.00 14.83 ? 658  ILE   B CB    1 
ATOM   13862 C  CG1   . ILE   B  1  660  ? 16.314  17.558  80.193  1.00 17.03 ? 658  ILE   B CG1   1 
ATOM   13863 C  CG2   . ILE   B  1  660  ? 18.446  16.244  80.571  1.00 16.81 ? 658  ILE   B CG2   1 
ATOM   13864 C  CD1   . ILE   B  1  660  ? 15.400  16.408  80.523  1.00 17.73 ? 658  ILE   B CD1   1 
ATOM   13865 N  N     . ARG   B  1  661  ? 20.179  17.313  77.751  1.00 14.92 ? 659  ARG   B N     1 
ATOM   13866 C  CA    . ARG   B  1  661  ? 21.523  16.808  77.515  1.00 14.73 ? 659  ARG   B CA    1 
ATOM   13867 C  C     . ARG   B  1  661  ? 22.450  17.858  76.919  1.00 15.81 ? 659  ARG   B C     1 
ATOM   13868 O  O     . ARG   B  1  661  ? 23.658  17.821  77.185  1.00 16.93 ? 659  ARG   B O     1 
ATOM   13869 C  CB    . ARG   B  1  661  ? 21.469  15.552  76.650  1.00 16.26 ? 659  ARG   B CB    1 
ATOM   13870 C  CG    . ARG   B  1  661  ? 20.987  14.356  77.434  1.00 19.07 ? 659  ARG   B CG    1 
ATOM   13871 C  CD    . ARG   B  1  661  ? 20.777  13.143  76.566  1.00 22.11 ? 659  ARG   B CD    1 
ATOM   13872 N  NE    . ARG   B  1  661  ? 22.003  12.699  75.909  1.00 19.27 ? 659  ARG   B NE    1 
ATOM   13873 C  CZ    . ARG   B  1  661  ? 22.144  12.584  74.596  1.00 20.78 ? 659  ARG   B CZ    1 
ATOM   13874 N  NH1   . ARG   B  1  661  ? 21.166  12.902  73.761  1.00 22.12 ? 659  ARG   B NH1   1 
ATOM   13875 N  NH2   . ARG   B  1  661  ? 23.290  12.116  74.101  1.00 20.91 ? 659  ARG   B NH2   1 
ATOM   13876 N  N     . GLU   B  1  662  ? 21.929  18.778  76.107  1.00 15.96 ? 660  GLU   B N     1 
ATOM   13877 C  CA    . GLU   B  1  662  ? 22.805  19.750  75.464  1.00 15.54 ? 660  GLU   B CA    1 
ATOM   13878 C  C     . GLU   B  1  662  ? 23.122  20.927  76.383  1.00 16.01 ? 660  GLU   B C     1 
ATOM   13879 O  O     . GLU   B  1  662  ? 24.249  21.433  76.376  1.00 16.63 ? 660  GLU   B O     1 
ATOM   13880 C  CB    . GLU   B  1  662  ? 22.181  20.250  74.157  1.00 17.55 ? 660  GLU   B CB    1 
ATOM   13881 C  CG    . GLU   B  1  662  ? 23.057  21.284  73.452  1.00 18.02 ? 660  GLU   B CG    1 
ATOM   13882 C  CD    . GLU   B  1  662  ? 22.491  21.769  72.122  1.00 16.47 ? 660  GLU   B CD    1 
ATOM   13883 O  OE1   . GLU   B  1  662  ? 21.258  21.935  71.995  1.00 17.64 ? 660  GLU   B OE1   1 
ATOM   13884 O  OE2   . GLU   B  1  662  ? 23.315  21.994  71.225  1.00 17.80 ? 660  GLU   B OE2   1 
ATOM   13885 N  N     . ALA   B  1  663  ? 22.155  21.377  77.184  1.00 14.34 ? 661  ALA   B N     1 
ATOM   13886 C  CA    . ALA   B  1  663  ? 22.284  22.634  77.902  1.00 14.80 ? 661  ALA   B CA    1 
ATOM   13887 C  C     . ALA   B  1  663  ? 22.342  22.462  79.413  1.00 16.46 ? 661  ALA   B C     1 
ATOM   13888 O  O     . ALA   B  1  663  ? 22.273  23.460  80.133  1.00 21.52 ? 661  ALA   B O     1 
ATOM   13889 C  CB    . ALA   B  1  663  ? 21.163  23.595  77.494  1.00 16.77 ? 661  ALA   B CB    1 
ATOM   13890 N  N     . GLY   B  1  664  ? 22.427  21.233  79.910  1.00 17.69 ? 662  GLY   B N     1 
ATOM   13891 C  CA    . GLY   B  1  664  ? 22.541  21.043  81.349  1.00 18.94 ? 662  GLY   B CA    1 
ATOM   13892 C  C     . GLY   B  1  664  ? 21.295  21.367  82.139  1.00 18.79 ? 662  GLY   B C     1 
ATOM   13893 O  O     . GLY   B  1  664  ? 21.385  21.690  83.326  1.00 19.31 ? 662  GLY   B O     1 
ATOM   13894 N  N     . LYS   B  1  665  ? 20.132  21.296  81.516  1.00 16.05 ? 663  LYS   B N     1 
ATOM   13895 C  CA    . LYS   B  1  665  ? 18.899  21.659  82.190  1.00 15.98 ? 663  LYS   B CA    1 
ATOM   13896 C  C     . LYS   B  1  665  ? 18.268  20.440  82.835  1.00 14.10 ? 663  LYS   B C     1 
ATOM   13897 O  O     . LYS   B  1  665  ? 18.334  19.327  82.312  1.00 15.21 ? 663  LYS   B O     1 
ATOM   13898 C  CB    . LYS   B  1  665  ? 17.899  22.220  81.184  1.00 16.17 ? 663  LYS   B CB    1 
ATOM   13899 C  CG    . LYS   B  1  665  ? 18.395  23.403  80.393  1.00 18.43 ? 663  LYS   B CG    1 
ATOM   13900 C  CD    . LYS   B  1  665  ? 18.780  24.539  81.306  1.00 19.31 ? 663  LYS   B CD    1 
ATOM   13901 C  CE    . LYS   B  1  665  ? 19.207  25.750  80.485  1.00 21.10 ? 663  LYS   B CE    1 
ATOM   13902 N  NZ    . LYS   B  1  665  ? 19.706  26.844  81.361  1.00 23.23 ? 663  LYS   B NZ    1 
ATOM   13903 N  N     . SER   B  1  666  ? 17.607  20.670  83.966  1.00 17.03 ? 664  SER   B N     1 
ATOM   13904 C  CA    . SER   B  1  666  ? 16.745  19.649  84.529  1.00 16.70 ? 664  SER   B CA    1 
ATOM   13905 C  C     . SER   B  1  666  ? 15.461  19.539  83.710  1.00 16.66 ? 664  SER   B C     1 
ATOM   13906 O  O     . SER   B  1  666  ? 15.131  20.403  82.896  1.00 17.28 ? 664  SER   B O     1 
ATOM   13907 C  CB    . SER   B  1  666  ? 16.339  20.026  85.945  1.00 20.53 ? 664  SER   B CB    1 
ATOM   13908 O  OG    . SER   B  1  666  ? 15.454  21.133  85.906  1.00 21.32 ? 664  SER   B OG    1 
ATOM   13909 N  N     . ALA   B  1  667  ? 14.727  18.451  83.941  1.00 17.07 ? 665  ALA   B N     1 
ATOM   13910 C  CA    . ALA   B  1  667  ? 13.473  18.247  83.227  1.00 16.47 ? 665  ALA   B CA    1 
ATOM   13911 C  C     . ALA   B  1  667  ? 12.510  19.412  83.435  1.00 17.00 ? 665  ALA   B C     1 
ATOM   13912 O  O     . ALA   B  1  667  ? 11.895  19.887  82.476  1.00 15.61 ? 665  ALA   B O     1 
ATOM   13913 C  CB    . ALA   B  1  667  ? 12.834  16.932  83.664  1.00 18.95 ? 665  ALA   B CB    1 
ATOM   13914 N  N     . LEU   B  1  668  ? 12.353  19.882  84.674  1.00 16.95 ? 666  LEU   B N     1 
ATOM   13915 C  CA    . LEU   B  1  668  ? 11.428  20.991  84.894  1.00 18.40 ? 666  LEU   B CA    1 
ATOM   13916 C  C     . LEU   B  1  668  ? 11.864  22.233  84.136  1.00 16.16 ? 666  LEU   B C     1 
ATOM   13917 O  O     . LEU   B  1  668  ? 11.030  22.954  83.574  1.00 16.68 ? 666  LEU   B O     1 
ATOM   13918 C  CB    . LEU   B  1  668  ? 11.290  21.311  86.383  1.00 20.49 ? 666  LEU   B CB    1 
ATOM   13919 C  CG    . LEU   B  1  668  ? 10.338  20.420  87.179  1.00 26.81 ? 666  LEU   B CG    1 
ATOM   13920 C  CD1   . LEU   B  1  668  ? 10.411  20.788  88.653  1.00 28.89 ? 666  LEU   B CD1   1 
ATOM   13921 C  CD2   . LEU   B  1  668  ? 8.906   20.528  86.656  1.00 27.54 ? 666  LEU   B CD2   1 
ATOM   13922 N  N     . ASN   B  1  669  ? 13.161  22.516  84.116  1.00 15.48 ? 667  ASN   B N     1 
ATOM   13923 C  CA    . ASN   B  1  669  ? 13.579  23.728  83.430  1.00 15.38 ? 667  ASN   B CA    1 
ATOM   13924 C  C     . ASN   B  1  669  ? 13.540  23.564  81.924  1.00 16.34 ? 667  ASN   B C     1 
ATOM   13925 O  O     . ASN   B  1  669  ? 13.335  24.549  81.207  1.00 17.07 ? 667  ASN   B O     1 
ATOM   13926 C  CB    . ASN   B  1  669  ? 14.927  24.186  83.957  1.00 21.50 ? 667  ASN   B CB    1 
ATOM   13927 C  CG    . ASN   B  1  669  ? 14.839  24.604  85.399  1.00 23.28 ? 667  ASN   B CG    1 
ATOM   13928 O  OD1   . ASN   B  1  669  ? 15.717  24.298  86.195  1.00 30.73 ? 667  ASN   B OD1   1 
ATOM   13929 N  ND2   . ASN   B  1  669  ? 13.736  25.273  85.756  1.00 24.21 ? 667  ASN   B ND2   1 
ATOM   13930 N  N     . ALA   B  1  670  ? 13.715  22.340  81.437  1.00 14.83 ? 668  ALA   B N     1 
ATOM   13931 C  CA    . ALA   B  1  670  ? 13.537  22.085  80.016  1.00 14.36 ? 668  ALA   B CA    1 
ATOM   13932 C  C     . ALA   B  1  670  ? 12.081  22.244  79.609  1.00 14.25 ? 668  ALA   B C     1 
ATOM   13933 O  O     . ALA   B  1  670  ? 11.788  22.768  78.530  1.00 14.87 ? 668  ALA   B O     1 
ATOM   13934 C  CB    . ALA   B  1  670  ? 14.045  20.682  79.668  1.00 15.19 ? 668  ALA   B CB    1 
ATOM   13935 N  N     . ILE   B  1  671  ? 11.152  21.781  80.453  1.00 14.43 ? 669  ILE   B N     1 
ATOM   13936 C  CA    . ILE   B  1  671  ? 9.734   22.030  80.204  1.00 14.57 ? 669  ILE   B CA    1 
ATOM   13937 C  C     . ILE   B  1  671  ? 9.468   23.522  80.123  1.00 14.22 ? 669  ILE   B C     1 
ATOM   13938 O  O     . ILE   B  1  671  ? 8.804   24.001  79.197  1.00 15.16 ? 669  ILE   B O     1 
ATOM   13939 C  CB    . ILE   B  1  671  ? 8.870   21.370  81.288  1.00 13.58 ? 669  ILE   B CB    1 
ATOM   13940 C  CG1   . ILE   B  1  671  ? 8.873   19.864  81.095  1.00 15.74 ? 669  ILE   B CG1   1 
ATOM   13941 C  CG2   . ILE   B  1  671  ? 7.453   21.913  81.196  1.00 16.90 ? 669  ILE   B CG2   1 
ATOM   13942 C  CD1   . ILE   B  1  671  ? 8.350   19.102  82.306  1.00 18.47 ? 669  ILE   B CD1   1 
ATOM   13943 N  N     . ALA   B  1  672  ? 9.994   24.277  81.085  1.00 14.32 ? 670  ALA   B N     1 
ATOM   13944 C  CA    . ALA   B  1  672  ? 9.794   25.718  81.084  1.00 15.56 ? 670  ALA   B CA    1 
ATOM   13945 C  C     . ALA   B  1  672  ? 10.374  26.339  79.824  1.00 15.50 ? 670  ALA   B C     1 
ATOM   13946 O  O     . ALA   B  1  672  ? 9.790   27.268  79.254  1.00 15.79 ? 670  ALA   B O     1 
ATOM   13947 C  CB    . ALA   B  1  672  ? 10.412  26.337  82.344  1.00 17.33 ? 670  ALA   B CB    1 
ATOM   13948 N  N     . GLU   B  1  673  ? 11.520  25.832  79.369  1.00 14.60 ? 671  GLU   B N     1 
ATOM   13949 C  CA    . GLU   B  1  673  ? 12.153  26.347  78.165  1.00 14.73 ? 671  GLU   B CA    1 
ATOM   13950 C  C     . GLU   B  1  673  ? 11.259  26.157  76.950  1.00 14.05 ? 671  GLU   B C     1 
ATOM   13951 O  O     . GLU   B  1  673  ? 11.044  27.097  76.171  1.00 14.55 ? 671  GLU   B O     1 
ATOM   13952 C  CB    . GLU   B  1  673  ? 13.455  25.585  77.957  1.00 16.62 ? 671  GLU   B CB    1 
ATOM   13953 C  CG    . GLU   B  1  673  ? 14.309  26.077  76.819  1.00 16.88 ? 671  GLU   B CG    1 
ATOM   13954 C  CD    . GLU   B  1  673  ? 15.059  27.351  77.135  1.00 17.35 ? 671  GLU   B CD    1 
ATOM   13955 O  OE1   . GLU   B  1  673  ? 15.251  27.699  78.333  1.00 19.52 ? 671  GLU   B OE1   1 
ATOM   13956 O  OE2   . GLU   B  1  673  ? 15.491  27.997  76.170  1.00 16.00 ? 671  GLU   B OE2   1 
ATOM   13957 N  N     . VAL   B  1  674  ? 10.752  24.938  76.757  1.00 12.78 ? 672  VAL   B N     1 
ATOM   13958 C  CA    . VAL   B  1  674  ? 9.896   24.685  75.608  1.00 12.70 ? 672  VAL   B CA    1 
ATOM   13959 C  C     . VAL   B  1  674  ? 8.597   25.467  75.727  1.00 12.49 ? 672  VAL   B C     1 
ATOM   13960 O  O     . VAL   B  1  674  ? 8.120   26.045  74.747  1.00 12.84 ? 672  VAL   B O     1 
ATOM   13961 C  CB    . VAL   B  1  674  ? 9.659   23.177  75.431  1.00 13.83 ? 672  VAL   B CB    1 
ATOM   13962 C  CG1   . VAL   B  1  674  ? 8.790   22.922  74.220  1.00 13.59 ? 672  VAL   B CG1   1 
ATOM   13963 C  CG2   . VAL   B  1  674  ? 10.989  22.466  75.275  1.00 15.46 ? 672  VAL   B CG2   1 
ATOM   13964 N  N     . ARG   B  1  675  ? 8.023   25.525  76.929  1.00 12.94 ? 673  ARG   B N     1 
ATOM   13965 C  CA    . ARG   B  1  675  ? 6.792   26.281  77.097  1.00 13.24 ? 673  ARG   B CA    1 
ATOM   13966 C  C     . ARG   B  1  675  ? 7.001   27.730  76.713  1.00 12.77 ? 673  ARG   B C     1 
ATOM   13967 O  O     . ARG   B  1  675  ? 6.154   28.329  76.051  1.00 12.73 ? 673  ARG   B O     1 
ATOM   13968 C  CB    . ARG   B  1  675  ? 6.315   26.220  78.540  1.00 13.23 ? 673  ARG   B CB    1 
ATOM   13969 C  CG    . ARG   B  1  675  ? 5.712   24.897  78.948  1.00 14.40 ? 673  ARG   B CG    1 
ATOM   13970 C  CD    . ARG   B  1  675  ? 5.093   25.034  80.333  1.00 13.33 ? 673  ARG   B CD    1 
ATOM   13971 N  NE    . ARG   B  1  675  ? 3.907   25.871  80.230  1.00 13.72 ? 673  ARG   B NE    1 
ATOM   13972 C  CZ    . ARG   B  1  675  ? 3.321   26.458  81.262  1.00 13.94 ? 673  ARG   B CZ    1 
ATOM   13973 N  NH1   . ARG   B  1  675  ? 3.774   26.304  82.491  1.00 15.38 ? 673  ARG   B NH1   1 
ATOM   13974 N  NH2   . ARG   B  1  675  ? 2.235   27.196  81.053  1.00 14.06 ? 673  ARG   B NH2   1 
ATOM   13975 N  N     . GLU   B  1  676  ? 8.131   28.307  77.109  1.00 12.29 ? 674  GLU   B N     1 
ATOM   13976 C  CA    . GLU   B  1  676  ? 8.384   29.703  76.806  1.00 12.49 ? 674  GLU   B CA    1 
ATOM   13977 C  C     . GLU   B  1  676  ? 8.503   29.921  75.306  1.00 12.30 ? 674  GLU   B C     1 
ATOM   13978 O  O     . GLU   B  1  676  ? 8.010   30.921  74.781  1.00 12.07 ? 674  GLU   B O     1 
ATOM   13979 C  CB    . GLU   B  1  676  ? 9.654   30.154  77.522  1.00 14.44 ? 674  GLU   B CB    1 
ATOM   13980 C  CG    . GLU   B  1  676  ? 9.944   31.627  77.386  1.00 15.47 ? 674  GLU   B CG    1 
ATOM   13981 C  CD    . GLU   B  1  676  ? 9.328   32.461  78.472  1.00 27.11 ? 674  GLU   B CD    1 
ATOM   13982 O  OE1   . GLU   B  1  676  ? 8.489   31.936  79.235  1.00 28.65 ? 674  GLU   B OE1   1 
ATOM   13983 O  OE2   . GLU   B  1  676  ? 9.694   33.651  78.564  1.00 26.07 ? 674  GLU   B OE2   1 
ATOM   13984 N  N     . ALA   B  1  677  ? 9.155   28.998  74.597  1.00 11.80 ? 675  ALA   B N     1 
ATOM   13985 C  CA    . ALA   B  1  677  ? 9.217   29.110  73.145  1.00 12.31 ? 675  ALA   B CA    1 
ATOM   13986 C  C     . ALA   B  1  677  ? 7.822   29.081  72.539  1.00 12.64 ? 675  ALA   B C     1 
ATOM   13987 O  O     . ALA   B  1  677  ? 7.499   29.895  71.663  1.00 12.70 ? 675  ALA   B O     1 
ATOM   13988 C  CB    . ALA   B  1  677  ? 10.075  27.978  72.569  1.00 13.38 ? 675  ALA   B CB    1 
ATOM   13989 N  N     . ILE   B  1  678  ? 6.987   28.141  73.000  1.00 11.45 ? 676  ILE   B N     1 
ATOM   13990 C  CA    . ILE   B  1  678  ? 5.606   28.055  72.542  1.00 11.27 ? 676  ILE   B CA    1 
ATOM   13991 C  C     . ILE   B  1  678  ? 4.882   29.359  72.811  1.00 11.59 ? 676  ILE   B C     1 
ATOM   13992 O  O     . ILE   B  1  678  ? 4.181   29.882  71.939  1.00 12.60 ? 676  ILE   B O     1 
ATOM   13993 C  CB    . ILE   B  1  678  ? 4.910   26.861  73.222  1.00 11.33 ? 676  ILE   B CB    1 
ATOM   13994 C  CG1   . ILE   B  1  678  ? 5.498   25.540  72.724  1.00 12.72 ? 676  ILE   B CG1   1 
ATOM   13995 C  CG2   . ILE   B  1  678  ? 3.366   26.921  73.054  1.00 12.95 ? 676  ILE   B CG2   1 
ATOM   13996 C  CD1   . ILE   B  1  678  ? 5.215   24.370  73.658  1.00 12.60 ? 676  ILE   B CD1   1 
ATOM   13997 N  N     . ASP   B  1  679  ? 5.073   29.914  74.002  1.00 11.82 ? 677  ASP   B N     1 
ATOM   13998 C  CA    . ASP   B  1  679  ? 4.370   31.136  74.357  1.00 11.93 ? 677  ASP   B CA    1 
ATOM   13999 C  C     . ASP   B  1  679  ? 4.849   32.317  73.532  1.00 12.08 ? 677  ASP   B C     1 
ATOM   14000 O  O     . ASP   B  1  679  ? 4.040   33.155  73.137  1.00 13.02 ? 677  ASP   B O     1 
ATOM   14001 C  CB    . ASP   B  1  679  ? 4.519   31.424  75.847  1.00 12.37 ? 677  ASP   B CB    1 
ATOM   14002 C  CG    . ASP   B  1  679  ? 3.770   30.435  76.719  1.00 14.17 ? 677  ASP   B CG    1 
ATOM   14003 O  OD1   . ASP   B  1  679  ? 2.701   29.948  76.307  1.00 15.96 ? 677  ASP   B OD1   1 
ATOM   14004 O  OD2   . ASP   B  1  679  ? 4.251   30.184  77.845  1.00 15.97 ? 677  ASP   B OD2   1 
ATOM   14005 N  N     . PHE   B  1  680  ? 6.155   32.414  73.259  1.00 11.71 ? 678  PHE   B N     1 
ATOM   14006 C  CA    . PHE   B  1  680  ? 6.609   33.482  72.377  1.00 11.44 ? 678  PHE   B CA    1 
ATOM   14007 C  C     . PHE   B  1  680  ? 5.942   33.366  71.022  1.00 12.70 ? 678  PHE   B C     1 
ATOM   14008 O  O     . PHE   B  1  680  ? 5.494   34.362  70.445  1.00 12.09 ? 678  PHE   B O     1 
ATOM   14009 C  CB    . PHE   B  1  680  ? 8.111   33.379  72.162  1.00 11.03 ? 678  PHE   B CB    1 
ATOM   14010 C  CG    . PHE   B  1  680  ? 8.942   34.033  73.218  1.00 12.52 ? 678  PHE   B CG    1 
ATOM   14011 C  CD1   . PHE   B  1  680  ? 8.708   35.331  73.618  1.00 12.62 ? 678  PHE   B CD1   1 
ATOM   14012 C  CD2   . PHE   B  1  680  ? 9.991   33.336  73.788  1.00 13.33 ? 678  PHE   B CD2   1 
ATOM   14013 C  CE1   . PHE   B  1  680  ? 9.520   35.930  74.590  1.00 13.31 ? 678  PHE   B CE1   1 
ATOM   14014 C  CE2   . PHE   B  1  680  ? 10.796  33.923  74.761  1.00 12.65 ? 678  PHE   B CE2   1 
ATOM   14015 C  CZ    . PHE   B  1  680  ? 10.563  35.219  75.151  1.00 13.63 ? 678  PHE   B CZ    1 
ATOM   14016 N  N     . LEU   B  1  681  ? 5.923   32.158  70.467  1.00 11.65 ? 679  LEU   B N     1 
ATOM   14017 C  CA    . LEU   B  1  681  ? 5.314   31.968  69.160  1.00 11.09 ? 679  LEU   B CA    1 
ATOM   14018 C  C     . LEU   B  1  681  ? 3.877   32.444  69.169  1.00 11.76 ? 679  LEU   B C     1 
ATOM   14019 O  O     . LEU   B  1  681  ? 3.462   33.217  68.293  1.00 12.41 ? 679  LEU   B O     1 
ATOM   14020 C  CB    . LEU   B  1  681  ? 5.397   30.492  68.779  1.00 11.75 ? 679  LEU   B CB    1 
ATOM   14021 C  CG    . LEU   B  1  681  ? 6.815   30.025  68.449  1.00 11.59 ? 679  LEU   B CG    1 
ATOM   14022 C  CD1   . LEU   B  1  681  ? 6.893   28.515  68.512  1.00 12.13 ? 679  LEU   B CD1   1 
ATOM   14023 C  CD2   . LEU   B  1  681  ? 7.218   30.528  67.083  1.00 13.39 ? 679  LEU   B CD2   1 
ATOM   14024 N  N     . ARG   B  1  682  ? 3.098   31.991  70.150  1.00 12.22 ? 680  ARG   B N     1 
ATOM   14025 C  CA    . ARG   B  1  682  ? 1.680   32.312  70.161  1.00 10.91 ? 680  ARG   B CA    1 
ATOM   14026 C  C     . ARG   B  1  682  ? 1.442   33.759  70.530  1.00 12.50 ? 680  ARG   B C     1 
ATOM   14027 O  O     . ARG   B  1  682  ? 0.483   34.361  70.044  1.00 12.47 ? 680  ARG   B O     1 
ATOM   14028 C  CB    . ARG   B  1  682  ? 0.932   31.382  71.105  1.00 11.73 ? 680  ARG   B CB    1 
ATOM   14029 C  CG    . ARG   B  1  682  ? 0.874   29.962  70.584  1.00 12.47 ? 680  ARG   B CG    1 
ATOM   14030 C  CD    . ARG   B  1  682  ? 0.236   29.087  71.611  1.00 13.47 ? 680  ARG   B CD    1 
ATOM   14031 N  NE    . ARG   B  1  682  ? 0.043   27.734  71.119  1.00 13.90 ? 680  ARG   B NE    1 
ATOM   14032 C  CZ    . ARG   B  1  682  ? -0.162  26.684  71.897  1.00 14.80 ? 680  ARG   B CZ    1 
ATOM   14033 N  NH1   . ARG   B  1  682  ? -0.173  26.790  73.216  1.00 15.57 ? 680  ARG   B NH1   1 
ATOM   14034 N  NH2   . ARG   B  1  682  ? -0.316  25.490  71.338  1.00 17.70 ? 680  ARG   B NH2   1 
ATOM   14035 N  N     . TYR   B  1  683  ? 2.282   34.320  71.391  1.00 11.84 ? 681  TYR   B N     1 
ATOM   14036 C  CA    . TYR   B  1  683  ? 2.114   35.713  71.774  1.00 11.99 ? 681  TYR   B CA    1 
ATOM   14037 C  C     . TYR   B  1  683  ? 2.442   36.634  70.606  1.00 11.74 ? 681  TYR   B C     1 
ATOM   14038 O  O     . TYR   B  1  683  ? 1.682   37.559  70.307  1.00 12.75 ? 681  TYR   B O     1 
ATOM   14039 C  CB    . TYR   B  1  683  ? 2.988   36.017  72.986  1.00 11.90 ? 681  TYR   B CB    1 
ATOM   14040 C  CG    . TYR   B  1  683  ? 2.946   37.455  73.395  1.00 11.68 ? 681  TYR   B CG    1 
ATOM   14041 C  CD1   . TYR   B  1  683  ? 1.872   37.949  74.123  1.00 13.17 ? 681  TYR   B CD1   1 
ATOM   14042 C  CD2   . TYR   B  1  683  ? 3.960   38.315  73.037  1.00 11.87 ? 681  TYR   B CD2   1 
ATOM   14043 C  CE1   . TYR   B  1  683  ? 1.822   39.270  74.494  1.00 13.79 ? 681  TYR   B CE1   1 
ATOM   14044 C  CE2   . TYR   B  1  683  ? 3.926   39.643  73.399  1.00 12.51 ? 681  TYR   B CE2   1 
ATOM   14045 C  CZ    . TYR   B  1  683  ? 2.857   40.105  74.129  1.00 12.50 ? 681  TYR   B CZ    1 
ATOM   14046 O  OH    . TYR   B  1  683  ? 2.816   41.429  74.473  1.00 15.36 ? 681  TYR   B OH    1 
ATOM   14047 N  N     . TYR   B  1  684  ? 3.577   36.411  69.941  1.00 11.24 ? 682  TYR   B N     1 
ATOM   14048 C  CA    . TYR   B  1  684  ? 3.878   37.292  68.822  1.00 11.34 ? 682  TYR   B CA    1 
ATOM   14049 C  C     . TYR   B  1  684  ? 2.887   37.097  67.686  1.00 12.65 ? 682  TYR   B C     1 
ATOM   14050 O  O     . TYR   B  1  684  ? 2.586   38.050  66.968  1.00 12.80 ? 682  TYR   B O     1 
ATOM   14051 C  CB    . TYR   B  1  684  ? 5.322   37.110  68.362  1.00 11.84 ? 682  TYR   B CB    1 
ATOM   14052 C  CG    . TYR   B  1  684  ? 6.319   37.498  69.419  1.00 11.67 ? 682  TYR   B CG    1 
ATOM   14053 C  CD1   . TYR   B  1  684  ? 6.153   38.644  70.181  1.00 12.61 ? 682  TYR   B CD1   1 
ATOM   14054 C  CD2   . TYR   B  1  684  ? 7.452   36.729  69.639  1.00 11.09 ? 682  TYR   B CD2   1 
ATOM   14055 C  CE1   . TYR   B  1  684  ? 7.074   38.997  71.157  1.00 12.17 ? 682  TYR   B CE1   1 
ATOM   14056 C  CE2   . TYR   B  1  684  ? 8.379   37.075  70.605  1.00 11.20 ? 682  TYR   B CE2   1 
ATOM   14057 C  CZ    . TYR   B  1  684  ? 8.185   38.206  71.353  1.00 12.55 ? 682  TYR   B CZ    1 
ATOM   14058 O  OH    . TYR   B  1  684  ? 9.090   38.525  72.331  1.00 12.71 ? 682  TYR   B OH    1 
ATOM   14059 N  N     . ALA   B  1  685  ? 2.350   35.886  67.527  1.00 11.02 ? 683  ALA   B N     1 
ATOM   14060 C  CA    . ALA   B  1  685  ? 1.300   35.681  66.536  1.00 11.69 ? 683  ALA   B CA    1 
ATOM   14061 C  C     . ALA   B  1  685  ? 0.082   36.516  66.883  1.00 12.23 ? 683  ALA   B C     1 
ATOM   14062 O  O     . ALA   B  1  685  ? -0.449  37.244  66.033  1.00 13.55 ? 683  ALA   B O     1 
ATOM   14063 C  CB    . ALA   B  1  685  ? 0.939   34.197  66.453  1.00 12.79 ? 683  ALA   B CB    1 
ATOM   14064 N  N     . GLU   B  1  686  ? -0.345  36.462  68.144  1.00 12.45 ? 684  GLU   B N     1 
ATOM   14065 C  CA    . GLU   B  1  686  ? -1.514  37.244  68.518  1.00 14.10 ? 684  GLU   B CA    1 
ATOM   14066 C  C     . GLU   B  1  686  ? -1.235  38.733  68.417  1.00 15.13 ? 684  GLU   B C     1 
ATOM   14067 O  O     . GLU   B  1  686  ? -2.069  39.488  67.912  1.00 13.58 ? 684  GLU   B O     1 
ATOM   14068 C  CB    . GLU   B  1  686  ? -1.987  36.877  69.915  1.00 16.83 ? 684  GLU   B CB    1 
ATOM   14069 C  CG    . GLU   B  1  686  ? -3.147  37.774  70.413  1.00 17.07 ? 684  GLU   B CG    1 
ATOM   14070 C  CD    . GLU   B  1  686  ? -4.435  37.668  69.583  1.00 21.94 ? 684  GLU   B CD    1 
ATOM   14071 O  OE1   . GLU   B  1  686  ? -4.573  36.773  68.710  1.00 20.43 ? 684  GLU   B OE1   1 
ATOM   14072 O  OE2   . GLU   B  1  686  ? -5.344  38.495  69.824  1.00 23.45 ? 684  GLU   B OE2   1 
ATOM   14073 N  N     . GLN   B  1  687  ? -0.065  39.178  68.873  1.00 12.48 ? 685  GLN   B N     1 
ATOM   14074 C  CA    . GLN   B  1  687  ? 0.221   40.603  68.784  1.00 12.62 ? 685  GLN   B CA    1 
ATOM   14075 C  C     . GLN   B  1  687  ? 0.238   41.058  67.335  1.00 13.28 ? 685  GLN   B C     1 
ATOM   14076 O  O     . GLN   B  1  687  ? -0.216  42.163  67.019  1.00 14.90 ? 685  GLN   B O     1 
ATOM   14077 C  CB    . GLN   B  1  687  ? 1.547   40.926  69.466  1.00 13.15 ? 685  GLN   B CB    1 
ATOM   14078 C  CG    . GLN   B  1  687  ? 1.507   40.744  70.978  1.00 14.62 ? 685  GLN   B CG    1 
ATOM   14079 C  CD    . GLN   B  1  687  ? 0.478   41.637  71.625  1.00 15.05 ? 685  GLN   B CD    1 
ATOM   14080 O  OE1   . GLN   B  1  687  ? 0.527   42.849  71.459  1.00 17.16 ? 685  GLN   B OE1   1 
ATOM   14081 N  NE2   . GLN   B  1  687  ? -0.471  41.045  72.351  1.00 19.33 ? 685  GLN   B NE2   1 
ATOM   14082 N  N     . THR   B  1  688  ? 0.740   40.207  66.440  1.00 12.39 ? 686  THR   B N     1 
ATOM   14083 C  CA    . THR   B  1  688  ? 0.672   40.515  65.017  1.00 13.30 ? 686  THR   B CA    1 
ATOM   14084 C  C     . THR   B  1  688  ? -0.765  40.684  64.556  1.00 13.76 ? 686  THR   B C     1 
ATOM   14085 O  O     . THR   B  1  688  ? -1.092  41.654  63.872  1.00 14.13 ? 686  THR   B O     1 
ATOM   14086 C  CB    . THR   B  1  688  ? 1.336   39.402  64.228  1.00 11.31 ? 686  THR   B CB    1 
ATOM   14087 O  OG1   . THR   B  1  688  ? 2.730   39.429  64.519  1.00 13.84 ? 686  THR   B OG1   1 
ATOM   14088 C  CG2   . THR   B  1  688  ? 1.138   39.628  62.733  1.00 14.17 ? 686  THR   B CG2   1 
ATOM   14089 N  N     . ARG   B  1  689  ? -1.631  39.729  64.894  1.00 12.81 ? 687  ARG   B N     1 
ATOM   14090 C  CA    . ARG   B  1  689  ? -3.032  39.819  64.490  1.00 13.24 ? 687  ARG   B CA    1 
ATOM   14091 C  C     . ARG   B  1  689  ? -3.705  41.061  65.049  1.00 13.94 ? 687  ARG   B C     1 
ATOM   14092 O  O     . ARG   B  1  689  ? -4.659  41.568  64.452  1.00 16.28 ? 687  ARG   B O     1 
ATOM   14093 C  CB    . ARG   B  1  689  ? -3.775  38.566  64.934  1.00 15.56 ? 687  ARG   B CB    1 
ATOM   14094 C  CG    . ARG   B  1  689  ? -3.388  37.328  64.147  1.00 16.78 ? 687  ARG   B CG    1 
ATOM   14095 C  CD    . ARG   B  1  689  ? -4.307  36.190  64.519  1.00 17.03 ? 687  ARG   B CD    1 
ATOM   14096 N  NE    . ARG   B  1  689  ? -4.137  35.782  65.905  1.00 17.11 ? 687  ARG   B NE    1 
ATOM   14097 C  CZ    . ARG   B  1  689  ? -3.373  34.770  66.297  1.00 18.07 ? 687  ARG   B CZ    1 
ATOM   14098 N  NH1   . ARG   B  1  689  ? -2.691  34.046  65.426  1.00 16.96 ? 687  ARG   B NH1   1 
ATOM   14099 N  NH2   . ARG   B  1  689  ? -3.304  34.472  67.590  1.00 17.79 ? 687  ARG   B NH2   1 
ATOM   14100 N  N     . ARG   B  1  690  ? -3.233  41.570  66.185  1.00 13.99 ? 688  ARG   B N     1 
ATOM   14101 C  CA    . ARG   B  1  690  ? -3.795  42.780  66.764  1.00 13.13 ? 688  ARG   B CA    1 
ATOM   14102 C  C     . ARG   B  1  690  ? -3.280  44.061  66.124  1.00 15.20 ? 688  ARG   B C     1 
ATOM   14103 O  O     . ARG   B  1  690  ? -3.907  45.111  66.305  1.00 15.02 ? 688  ARG   B O     1 
ATOM   14104 C  CB    . ARG   B  1  690  ? -3.473  42.829  68.262  1.00 14.57 ? 688  ARG   B CB    1 
ATOM   14105 C  CG    . ARG   B  1  690  ? -4.130  41.733  69.085  1.00 16.54 ? 688  ARG   B CG    1 
ATOM   14106 C  CD    . ARG   B  1  690  ? -5.639  41.984  69.299  1.00 19.38 ? 688  ARG   B CD    1 
ATOM   14107 N  NE    . ARG   B  1  690  ? -5.901  43.241  69.998  1.00 22.59 ? 688  ARG   B NE    1 
ATOM   14108 C  CZ    . ARG   B  1  690  ? -6.506  44.289  69.464  1.00 22.30 ? 688  ARG   B CZ    1 
ATOM   14109 N  NH1   . ARG   B  1  690  ? -7.013  44.245  68.241  1.00 20.50 ? 688  ARG   B NH1   1 
ATOM   14110 N  NH2   . ARG   B  1  690  ? -6.628  45.403  70.183  1.00 19.50 ? 688  ARG   B NH2   1 
ATOM   14111 N  N     . THR   B  1  691  ? -2.151  44.022  65.429  1.00 14.62 ? 689  THR   B N     1 
ATOM   14112 C  CA    . THR   B  1  691  ? -1.509  45.292  65.087  1.00 14.55 ? 689  THR   B CA    1 
ATOM   14113 C  C     . THR   B  1  691  ? -1.104  45.461  63.629  1.00 16.23 ? 689  THR   B C     1 
ATOM   14114 O  O     . THR   B  1  691  ? -1.294  46.539  63.075  1.00 19.24 ? 689  THR   B O     1 
ATOM   14115 C  CB    . THR   B  1  691  ? -0.265  45.525  65.950  1.00 14.70 ? 689  THR   B CB    1 
ATOM   14116 O  OG1   . THR   B  1  691  ? 0.642   44.422  65.793  1.00 15.53 ? 689  THR   B OG1   1 
ATOM   14117 C  CG2   . THR   B  1  691  ? -0.645  45.685  67.401  1.00 16.49 ? 689  THR   B CG2   1 
ATOM   14118 N  N     . LEU   B  1  692  ? -0.495  44.461  63.010  1.00 15.01 ? 690  LEU   B N     1 
ATOM   14119 C  CA    . LEU   B  1  692  ? 0.269   44.746  61.803  1.00 14.51 ? 690  LEU   B CA    1 
ATOM   14120 C  C     . LEU   B  1  692  ? -0.620  44.892  60.575  1.00 15.93 ? 690  LEU   B C     1 
ATOM   14121 O  O     . LEU   B  1  692  ? -1.452  44.030  60.287  1.00 18.62 ? 690  LEU   B O     1 
ATOM   14122 C  CB    . LEU   B  1  692  ? 1.339   43.689  61.562  1.00 15.70 ? 690  LEU   B CB    1 
ATOM   14123 C  CG    . LEU   B  1  692  ? 2.395   43.658  62.664  1.00 17.39 ? 690  LEU   B CG    1 
ATOM   14124 C  CD1   . LEU   B  1  692  ? 3.512   42.722  62.243  1.00 19.63 ? 690  LEU   B CD1   1 
ATOM   14125 C  CD2   . LEU   B  1  692  ? 2.945   45.052  62.971  1.00 18.24 ? 690  LEU   B CD2   1 
ATOM   14126 N  N     . GLY   B  1  693  ? -0.416  45.987  59.856  1.00 16.18 ? 691  GLY   B N     1 
ATOM   14127 C  CA    . GLY   B  1  693  ? -1.124  46.262  58.637  1.00 17.12 ? 691  GLY   B CA    1 
ATOM   14128 C  C     . GLY   B  1  693  ? -0.157  46.675  57.554  1.00 19.07 ? 691  GLY   B C     1 
ATOM   14129 O  O     . GLY   B  1  693  ? 1.062   46.640  57.728  1.00 19.21 ? 691  GLY   B O     1 
ATOM   14130 N  N     . PRO   B  1  694  ? -0.696  47.101  56.415  1.00 19.87 ? 692  PRO   B N     1 
ATOM   14131 C  CA    . PRO   B  1  694  ? 0.163   47.336  55.245  1.00 21.48 ? 692  PRO   B CA    1 
ATOM   14132 C  C     . PRO   B  1  694  ? 1.214   48.408  55.458  1.00 22.68 ? 692  PRO   B C     1 
ATOM   14133 O  O     . PRO   B  1  694  ? 2.299   48.323  54.866  1.00 25.23 ? 692  PRO   B O     1 
ATOM   14134 C  CB    . PRO   B  1  694  ? -0.839  47.698  54.134  1.00 26.21 ? 692  PRO   B CB    1 
ATOM   14135 C  CG    . PRO   B  1  694  ? -2.133  48.000  54.836  1.00 28.62 ? 692  PRO   B CG    1 
ATOM   14136 C  CD    . PRO   B  1  694  ? -2.132  47.230  56.118  1.00 21.52 ? 692  PRO   B CD    1 
ATOM   14137 N  N     . GLY   B  1  695  ? 0.945   49.407  56.286  1.00 21.91 ? 693  GLY   B N     1 
ATOM   14138 C  CA    . GLY   B  1  695  ? 1.894   50.472  56.503  1.00 21.60 ? 693  GLY   B CA    1 
ATOM   14139 C  C     . GLY   B  1  695  ? 3.000   50.168  57.478  1.00 20.75 ? 693  GLY   B C     1 
ATOM   14140 O  O     . GLY   B  1  695  ? 3.857   51.023  57.714  1.00 24.94 ? 693  GLY   B O     1 
ATOM   14141 N  N     . HIS   B  1  696  ? 3.000   48.981  58.085  1.00 20.18 ? 694  HIS   B N     1 
ATOM   14142 C  CA    . HIS   B  1  696  ? 4.066   48.598  59.009  1.00 17.05 ? 694  HIS   B CA    1 
ATOM   14143 C  C     . HIS   B  1  696  ? 5.023   47.689  58.248  1.00 17.23 ? 694  HIS   B C     1 
ATOM   14144 O  O     . HIS   B  1  696  ? 5.015   46.465  58.383  1.00 22.87 ? 694  HIS   B O     1 
ATOM   14145 C  CB    . HIS   B  1  696  ? 3.484   47.918  60.234  1.00 18.40 ? 694  HIS   B CB    1 
ATOM   14146 C  CG    . HIS   B  1  696  ? 2.362   48.685  60.848  1.00 15.53 ? 694  HIS   B CG    1 
ATOM   14147 N  ND1   . HIS   B  1  696  ? 1.076   48.198  60.909  1.00 17.99 ? 694  HIS   B ND1   1 
ATOM   14148 C  CD2   . HIS   B  1  696  ? 2.321   49.928  61.384  1.00 18.52 ? 694  HIS   B CD2   1 
ATOM   14149 C  CE1   . HIS   B  1  696  ? 0.296   49.095  61.484  1.00 19.03 ? 694  HIS   B CE1   1 
ATOM   14150 N  NE2   . HIS   B  1  696  ? 1.023   50.160  61.768  1.00 20.65 ? 694  HIS   B NE2   1 
ATOM   14151 N  N     . GLY   B  1  697  ? 5.858   48.313  57.430  1.00 19.84 ? 695  GLY   B N     1 
ATOM   14152 C  CA    . GLY   B  1  697  ? 6.769   47.585  56.580  1.00 18.70 ? 695  GLY   B CA    1 
ATOM   14153 C  C     . GLY   B  1  697  ? 7.894   46.968  57.373  1.00 16.96 ? 695  GLY   B C     1 
ATOM   14154 O  O     . GLY   B  1  697  ? 8.328   47.503  58.390  1.00 19.29 ? 695  GLY   B O     1 
ATOM   14155 N  N     . PRO   B  1  698  ? 8.413   45.842  56.907  1.00 18.39 ? 696  PRO   B N     1 
ATOM   14156 C  CA    . PRO   B  1  698  ? 9.530   45.207  57.613  1.00 17.75 ? 696  PRO   B CA    1 
ATOM   14157 C  C     . PRO   B  1  698  ? 10.819  45.990  57.431  1.00 17.43 ? 696  PRO   B C     1 
ATOM   14158 O  O     . PRO   B  1  698  ? 10.969  46.817  56.529  1.00 18.02 ? 696  PRO   B O     1 
ATOM   14159 C  CB    . PRO   B  1  698  ? 9.643   43.838  56.940  1.00 24.38 ? 696  PRO   B CB    1 
ATOM   14160 C  CG    . PRO   B  1  698  ? 9.149   44.088  55.565  1.00 27.55 ? 696  PRO   B CG    1 
ATOM   14161 C  CD    . PRO   B  1  698  ? 8.015   45.085  55.712  1.00 23.28 ? 696  PRO   B CD    1 
ATOM   14162 N  N     . LEU   B  1  699  ? 11.759  45.725  58.332  1.00 15.28 ? 697  LEU   B N     1 
ATOM   14163 C  CA    . LEU   B  1  699  ? 13.090  46.307  58.183  1.00 15.13 ? 697  LEU   B CA    1 
ATOM   14164 C  C     . LEU   B  1  699  ? 13.851  45.670  57.027  1.00 15.12 ? 697  LEU   B C     1 
ATOM   14165 O  O     . LEU   B  1  699  ? 14.563  46.362  56.295  1.00 16.59 ? 697  LEU   B O     1 
ATOM   14166 C  CB    . LEU   B  1  699  ? 13.876  46.116  59.475  1.00 15.72 ? 697  LEU   B CB    1 
ATOM   14167 C  CG    . LEU   B  1  699  ? 13.298  46.727  60.751  1.00 18.17 ? 697  LEU   B CG    1 
ATOM   14168 C  CD1   . LEU   B  1  699  ? 14.169  46.346  61.933  1.00 17.34 ? 697  LEU   B CD1   1 
ATOM   14169 C  CD2   . LEU   B  1  699  ? 13.190  48.241  60.622  1.00 21.79 ? 697  LEU   B CD2   1 
ATOM   14170 N  N     . GLY   B  1  700  ? 13.743  44.350  56.873  1.00 14.88 ? 698  GLY   B N     1 
ATOM   14171 C  CA    . GLY   B  1  700  ? 14.604  43.608  55.983  1.00 15.91 ? 698  GLY   B CA    1 
ATOM   14172 C  C     . GLY   B  1  700  ? 15.279  42.506  56.770  1.00 14.85 ? 698  GLY   B C     1 
ATOM   14173 O  O     . GLY   B  1  700  ? 14.837  42.144  57.859  1.00 14.95 ? 698  GLY   B O     1 
ATOM   14174 N  N     . PRO   B  1  701  ? 16.371  41.959  56.254  1.00 15.46 ? 699  PRO   B N     1 
ATOM   14175 C  CA    . PRO   B  1  701  ? 17.020  40.842  56.947  1.00 13.69 ? 699  PRO   B CA    1 
ATOM   14176 C  C     . PRO   B  1  701  ? 17.404  41.226  58.364  1.00 13.97 ? 699  PRO   B C     1 
ATOM   14177 O  O     . PRO   B  1  701  ? 18.047  42.251  58.598  1.00 15.00 ? 699  PRO   B O     1 
ATOM   14178 C  CB    . PRO   B  1  701  ? 18.267  40.575  56.095  1.00 15.28 ? 699  PRO   B CB    1 
ATOM   14179 C  CG    . PRO   B  1  701  ? 17.863  41.058  54.727  1.00 15.57 ? 699  PRO   B CG    1 
ATOM   14180 C  CD    . PRO   B  1  701  ? 17.081  42.308  55.012  1.00 15.78 ? 699  PRO   B CD    1 
ATOM   14181 N  N     . ILE   B  1  702  ? 16.994  40.400  59.313  1.00 13.68 ? 700  ILE   B N     1 
ATOM   14182 C  CA    A ILE   B  1  702  ? 17.310  40.618  60.716  0.65 13.44 ? 700  ILE   B CA    1 
ATOM   14183 C  CA    B ILE   B  1  702  ? 17.288  40.608  60.727  0.35 13.45 ? 700  ILE   B CA    1 
ATOM   14184 C  C     . ILE   B  1  702  ? 18.219  39.499  61.181  1.00 14.67 ? 700  ILE   B C     1 
ATOM   14185 O  O     . ILE   B  1  702  ? 17.946  38.315  60.945  1.00 14.10 ? 700  ILE   B O     1 
ATOM   14186 C  CB    A ILE   B  1  702  ? 16.048  40.715  61.582  0.65 11.90 ? 700  ILE   B CB    1 
ATOM   14187 C  CB    B ILE   B  1  702  ? 16.009  40.612  61.582  0.35 11.97 ? 700  ILE   B CB    1 
ATOM   14188 C  CG1   A ILE   B  1  702  ? 15.376  42.066  61.351  0.65 13.37 ? 700  ILE   B CG1   1 
ATOM   14189 C  CG1   B ILE   B  1  702  ? 15.049  41.701  61.117  0.35 13.47 ? 700  ILE   B CG1   1 
ATOM   14190 C  CG2   A ILE   B  1  702  ? 16.412  40.501  63.054  0.65 12.96 ? 700  ILE   B CG2   1 
ATOM   14191 C  CG2   B ILE   B  1  702  ? 16.355  40.794  63.062  0.35 13.17 ? 700  ILE   B CG2   1 
ATOM   14192 C  CD1   A ILE   B  1  702  ? 14.094  42.252  62.114  0.65 13.47 ? 700  ILE   B CD1   1 
ATOM   14193 C  CD1   B ILE   B  1  702  ? 15.581  43.092  61.244  0.35 14.02 ? 700  ILE   B CD1   1 
ATOM   14194 N  N     . VAL   B  1  703  ? 19.313  39.883  61.813  1.00 12.83 ? 701  VAL   B N     1 
ATOM   14195 C  CA    . VAL   B  1  703  ? 20.241  38.940  62.402  1.00 13.50 ? 701  VAL   B CA    1 
ATOM   14196 C  C     . VAL   B  1  703  ? 19.827  38.742  63.850  1.00 12.31 ? 701  VAL   B C     1 
ATOM   14197 O  O     . VAL   B  1  703  ? 19.745  39.710  64.616  1.00 13.03 ? 701  VAL   B O     1 
ATOM   14198 C  CB    . VAL   B  1  703  ? 21.664  39.485  62.303  1.00 13.03 ? 701  VAL   B CB    1 
ATOM   14199 C  CG1   . VAL   B  1  703  ? 22.614  38.629  63.134  1.00 14.44 ? 701  VAL   B CG1   1 
ATOM   14200 C  CG2   . VAL   B  1  703  ? 22.076  39.509  60.848  1.00 15.07 ? 701  VAL   B CG2   1 
ATOM   14201 N  N     . CYS   B  1  704  ? 19.529  37.499  64.220  1.00 12.25 ? 702  CYS   B N     1 
ATOM   14202 C  CA    . CYS   B  1  704  ? 19.101  37.166  65.571  1.00 12.68 ? 702  CYS   B CA    1 
ATOM   14203 C  C     . CYS   B  1  704  ? 20.219  36.376  66.213  1.00 13.93 ? 702  CYS   B C     1 
ATOM   14204 O  O     . CYS   B  1  704  ? 20.552  35.286  65.749  1.00 12.68 ? 702  CYS   B O     1 
ATOM   14205 C  CB    . CYS   B  1  704  ? 17.821  36.335  65.547  1.00 12.48 ? 702  CYS   B CB    1 
ATOM   14206 S  SG    . CYS   B  1  704  ? 16.429  37.195  64.845  1.00 13.22 ? 702  CYS   B SG    1 
ATOM   14207 N  N     . ILE   B  1  705  ? 20.803  36.934  67.263  1.00 11.55 ? 703  ILE   B N     1 
ATOM   14208 C  CA    . ILE   B  1  705  ? 21.944  36.339  67.939  1.00 13.03 ? 703  ILE   B CA    1 
ATOM   14209 C  C     . ILE   B  1  705  ? 21.503  36.059  69.361  1.00 12.24 ? 703  ILE   B C     1 
ATOM   14210 O  O     . ILE   B  1  705  ? 20.972  36.950  70.032  1.00 12.80 ? 703  ILE   B O     1 
ATOM   14211 C  CB    . ILE   B  1  705  ? 23.154  37.285  67.904  1.00 13.41 ? 703  ILE   B CB    1 
ATOM   14212 C  CG1   . ILE   B  1  705  ? 23.719  37.358  66.492  1.00 14.78 ? 703  ILE   B CG1   1 
ATOM   14213 C  CG2   . ILE   B  1  705  ? 24.193  36.823  68.878  1.00 13.72 ? 703  ILE   B CG2   1 
ATOM   14214 C  CD1   . ILE   B  1  705  ? 24.653  38.531  66.289  1.00 15.21 ? 703  ILE   B CD1   1 
ATOM   14215 N  N     . SER   B  1  706  ? 21.680  34.822  69.796  1.00 12.91 ? 704  SER   B N     1 
ATOM   14216 C  CA    . SER   B  1  706  ? 21.029  34.358  71.007  1.00 13.94 ? 704  SER   B CA    1 
ATOM   14217 C  C     . SER   B  1  706  ? 22.029  33.726  71.956  1.00 13.72 ? 704  SER   B C     1 
ATOM   14218 O  O     . SER   B  1  706  ? 23.101  33.277  71.542  1.00 14.18 ? 704  SER   B O     1 
ATOM   14219 C  CB    . SER   B  1  706  ? 19.913  33.358  70.659  1.00 13.85 ? 704  SER   B CB    1 
ATOM   14220 O  OG    . SER   B  1  706  ? 20.397  32.317  69.835  1.00 12.92 ? 704  SER   B OG    1 
ATOM   14221 N  N     . PRO   B  1  707  ? 21.710  33.696  73.242  1.00 13.09 ? 705  PRO   B N     1 
ATOM   14222 C  CA    . PRO   B  1  707  ? 22.619  33.155  74.251  1.00 13.81 ? 705  PRO   B CA    1 
ATOM   14223 C  C     . PRO   B  1  707  ? 22.411  31.655  74.407  1.00 14.31 ? 705  PRO   B C     1 
ATOM   14224 O  O     . PRO   B  1  707  ? 21.411  31.081  73.972  1.00 14.64 ? 705  PRO   B O     1 
ATOM   14225 C  CB    . PRO   B  1  707  ? 22.144  33.880  75.516  1.00 15.40 ? 705  PRO   B CB    1 
ATOM   14226 C  CG    . PRO   B  1  707  ? 20.682  33.991  75.329  1.00 13.79 ? 705  PRO   B CG    1 
ATOM   14227 C  CD    . PRO   B  1  707  ? 20.487  34.252  73.842  1.00 13.93 ? 705  PRO   B CD    1 
ATOM   14228 N  N     . TRP   B  1  708  ? 23.371  31.025  75.069  1.00 12.63 ? 706  TRP   B N     1 
ATOM   14229 C  CA    . TRP   B  1  708  ? 23.249  29.585  75.225  1.00 13.66 ? 706  TRP   B CA    1 
ATOM   14230 C  C     . TRP   B  1  708  ? 22.241  29.195  76.291  1.00 13.78 ? 706  TRP   B C     1 
ATOM   14231 O  O     . TRP   B  1  708  ? 21.726  28.078  76.252  1.00 13.94 ? 706  TRP   B O     1 
ATOM   14232 C  CB    . TRP   B  1  708  ? 24.609  28.956  75.560  1.00 14.08 ? 706  TRP   B CB    1 
ATOM   14233 C  CG    . TRP   B  1  708  ? 24.996  29.207  76.979  1.00 13.88 ? 706  TRP   B CG    1 
ATOM   14234 C  CD1   . TRP   B  1  708  ? 25.771  30.221  77.453  1.00 16.20 ? 706  TRP   B CD1   1 
ATOM   14235 C  CD2   . TRP   B  1  708  ? 24.586  28.441  78.116  1.00 14.39 ? 706  TRP   B CD2   1 
ATOM   14236 N  NE1   . TRP   B  1  708  ? 25.863  30.141  78.822  1.00 16.07 ? 706  TRP   B NE1   1 
ATOM   14237 C  CE2   . TRP   B  1  708  ? 25.130  29.062  79.253  1.00 13.74 ? 706  TRP   B CE2   1 
ATOM   14238 C  CE3   . TRP   B  1  708  ? 23.812  27.289  78.279  1.00 14.97 ? 706  TRP   B CE3   1 
ATOM   14239 C  CZ2   . TRP   B  1  708  ? 24.925  28.569  80.539  1.00 14.63 ? 706  TRP   B CZ2   1 
ATOM   14240 C  CZ3   . TRP   B  1  708  ? 23.591  26.809  79.555  1.00 15.49 ? 706  TRP   B CZ3   1 
ATOM   14241 C  CH2   . TRP   B  1  708  ? 24.152  27.440  80.666  1.00 14.74 ? 706  TRP   B CH2   1 
ATOM   14242 N  N     . ASN   B  1  709  ? 21.969  30.072  77.258  1.00 13.11 ? 707  ASN   B N     1 
ATOM   14243 C  CA    . ASN   B  1  709  ? 21.407  29.597  78.518  1.00 13.83 ? 707  ASN   B CA    1 
ATOM   14244 C  C     . ASN   B  1  709  ? 19.909  29.380  78.465  1.00 15.41 ? 707  ASN   B C     1 
ATOM   14245 O  O     . ASN   B  1  709  ? 19.387  28.608  79.275  1.00 15.42 ? 707  ASN   B O     1 
ATOM   14246 C  CB    . ASN   B  1  709  ? 21.754  30.567  79.643  1.00 14.03 ? 707  ASN   B CB    1 
ATOM   14247 C  CG    . ASN   B  1  709  ? 20.994  31.851  79.533  1.00 14.20 ? 707  ASN   B CG    1 
ATOM   14248 O  OD1   . ASN   B  1  709  ? 21.243  32.642  78.636  1.00 16.99 ? 707  ASN   B OD1   1 
ATOM   14249 N  ND2   . ASN   B  1  709  ? 20.040  32.062  80.431  1.00 16.38 ? 707  ASN   B ND2   1 
ATOM   14250 N  N     . PHE   B  1  710  ? 19.216  30.038  77.538  1.00 14.08 ? 708  PHE   B N     1 
ATOM   14251 C  CA    . PHE   B  1  710  ? 17.826  29.749  77.202  1.00 13.78 ? 708  PHE   B CA    1 
ATOM   14252 C  C     . PHE   B  1  710  ? 17.859  29.375  75.726  1.00 14.44 ? 708  PHE   B C     1 
ATOM   14253 O  O     . PHE   B  1  710  ? 17.441  30.147  74.853  1.00 14.60 ? 708  PHE   B O     1 
ATOM   14254 C  CB    . PHE   B  1  710  ? 16.904  30.938  77.469  1.00 14.37 ? 708  PHE   B CB    1 
ATOM   14255 C  CG    . PHE   B  1  710  ? 16.849  31.369  78.920  1.00 15.39 ? 708  PHE   B CG    1 
ATOM   14256 C  CD1   . PHE   B  1  710  ? 16.788  30.433  79.948  1.00 17.24 ? 708  PHE   B CD1   1 
ATOM   14257 C  CD2   . PHE   B  1  710  ? 16.834  32.714  79.250  1.00 17.70 ? 708  PHE   B CD2   1 
ATOM   14258 C  CE1   . PHE   B  1  710  ? 16.710  30.835  81.278  1.00 17.55 ? 708  PHE   B CE1   1 
ATOM   14259 C  CE2   . PHE   B  1  710  ? 16.756  33.126  80.574  1.00 18.54 ? 708  PHE   B CE2   1 
ATOM   14260 C  CZ    . PHE   B  1  710  ? 16.699  32.183  81.592  1.00 20.42 ? 708  PHE   B CZ    1 
ATOM   14261 N  N     . PRO   B  1  711  ? 18.367  28.182  75.417  1.00 15.18 ? 709  PRO   B N     1 
ATOM   14262 C  CA    . PRO   B  1  711  ? 18.802  27.889  74.046  1.00 14.63 ? 709  PRO   B CA    1 
ATOM   14263 C  C     . PRO   B  1  711  ? 17.673  27.659  73.062  1.00 14.56 ? 709  PRO   B C     1 
ATOM   14264 O  O     . PRO   B  1  711  ? 17.928  27.649  71.855  1.00 14.32 ? 709  PRO   B O     1 
ATOM   14265 C  CB    . PRO   B  1  711  ? 19.643  26.619  74.220  1.00 14.77 ? 709  PRO   B CB    1 
ATOM   14266 C  CG    . PRO   B  1  711  ? 18.974  25.938  75.380  1.00 14.71 ? 709  PRO   B CG    1 
ATOM   14267 C  CD    . PRO   B  1  711  ? 18.628  27.058  76.329  1.00 14.19 ? 709  PRO   B CD    1 
ATOM   14268 N  N     . LEU   B  1  712  ? 16.452  27.427  73.529  1.00 12.83 ? 710  LEU   B N     1 
ATOM   14269 C  CA    . LEU   B  1  712  ? 15.306  27.375  72.639  1.00 13.26 ? 710  LEU   B CA    1 
ATOM   14270 C  C     . LEU   B  1  712  ? 14.386  28.564  72.829  1.00 13.46 ? 710  LEU   B C     1 
ATOM   14271 O  O     . LEU   B  1  712  ? 13.890  29.109  71.850  1.00 13.39 ? 710  LEU   B O     1 
ATOM   14272 C  CB    . LEU   B  1  712  ? 14.514  26.077  72.837  1.00 13.77 ? 710  LEU   B CB    1 
ATOM   14273 C  CG    . LEU   B  1  712  ? 13.334  25.904  71.878  1.00 11.80 ? 710  LEU   B CG    1 
ATOM   14274 C  CD1   . LEU   B  1  712  ? 13.780  25.813  70.428  1.00 13.95 ? 710  LEU   B CD1   1 
ATOM   14275 C  CD2   . LEU   B  1  712  ? 12.517  24.675  72.258  1.00 16.64 ? 710  LEU   B CD2   1 
ATOM   14276 N  N     . ALA   B  1  713  ? 14.189  29.024  74.059  1.00 12.85 ? 711  ALA   B N     1 
ATOM   14277 C  CA    . ALA   B  1  713  ? 13.163  30.034  74.299  1.00 13.94 ? 711  ALA   B CA    1 
ATOM   14278 C  C     . ALA   B  1  713  ? 13.552  31.387  73.718  1.00 13.15 ? 711  ALA   B C     1 
ATOM   14279 O  O     . ALA   B  1  713  ? 12.808  31.968  72.927  1.00 13.86 ? 711  ALA   B O     1 
ATOM   14280 C  CB    . ALA   B  1  713  ? 12.869  30.140  75.791  1.00 14.84 ? 711  ALA   B CB    1 
ATOM   14281 N  N     . ILE   B  1  714  ? 14.711  31.920  74.102  1.00 13.95 ? 712  ILE   B N     1 
ATOM   14282 C  CA    . ILE   B  1  714  ? 15.097  33.222  73.567  1.00 13.45 ? 712  ILE   B CA    1 
ATOM   14283 C  C     . ILE   B  1  714  ? 15.404  33.115  72.085  1.00 14.40 ? 712  ILE   B C     1 
ATOM   14284 O  O     . ILE   B  1  714  ? 15.047  33.999  71.294  1.00 13.30 ? 712  ILE   B O     1 
ATOM   14285 C  CB    . ILE   B  1  714  ? 16.261  33.810  74.372  1.00 13.49 ? 712  ILE   B CB    1 
ATOM   14286 C  CG1   . ILE   B  1  714  ? 15.706  34.229  75.730  1.00 16.45 ? 712  ILE   B CG1   1 
ATOM   14287 C  CG2   . ILE   B  1  714  ? 16.900  34.969  73.601  1.00 14.26 ? 712  ILE   B CG2   1 
ATOM   14288 C  CD1   . ILE   B  1  714  ? 16.633  35.044  76.552  1.00 23.63 ? 712  ILE   B CD1   1 
ATOM   14289 N  N     . PHE   B  1  715  ? 16.068  32.027  71.692  1.00 12.44 ? 713  PHE   B N     1 
ATOM   14290 C  CA    . PHE   B  1  715  ? 16.317  31.749  70.286  1.00 12.75 ? 713  PHE   B CA    1 
ATOM   14291 C  C     . PHE   B  1  715  ? 15.028  31.871  69.480  1.00 12.72 ? 713  PHE   B C     1 
ATOM   14292 O  O     . PHE   B  1  715  ? 14.961  32.620  68.495  1.00 12.64 ? 713  PHE   B O     1 
ATOM   14293 C  CB    . PHE   B  1  715  ? 16.896  30.339  70.161  1.00 12.90 ? 713  PHE   B CB    1 
ATOM   14294 C  CG    . PHE   B  1  715  ? 17.129  29.923  68.750  1.00 11.58 ? 713  PHE   B CG    1 
ATOM   14295 C  CD1   . PHE   B  1  715  ? 18.248  30.368  68.076  1.00 12.08 ? 713  PHE   B CD1   1 
ATOM   14296 C  CD2   . PHE   B  1  715  ? 16.227  29.102  68.090  1.00 13.40 ? 713  PHE   B CD2   1 
ATOM   14297 C  CE1   . PHE   B  1  715  ? 18.481  29.990  66.780  1.00 14.05 ? 713  PHE   B CE1   1 
ATOM   14298 C  CE2   . PHE   B  1  715  ? 16.443  28.737  66.777  1.00 13.89 ? 713  PHE   B CE2   1 
ATOM   14299 C  CZ    . PHE   B  1  715  ? 17.570  29.185  66.118  1.00 13.02 ? 713  PHE   B CZ    1 
ATOM   14300 N  N     . THR   B  1  716  ? 13.976  31.162  69.912  1.00 11.99 ? 714  THR   B N     1 
ATOM   14301 C  CA    . THR   B  1  716  ? 12.714  31.159  69.184  1.00 12.83 ? 714  THR   B CA    1 
ATOM   14302 C  C     . THR   B  1  716  ? 12.026  32.508  69.272  1.00 13.09 ? 714  THR   B C     1 
ATOM   14303 O  O     . THR   B  1  716  ? 11.466  32.983  68.284  1.00 12.65 ? 714  THR   B O     1 
ATOM   14304 C  CB    . THR   B  1  716  ? 11.805  30.074  69.755  1.00 12.63 ? 714  THR   B CB    1 
ATOM   14305 O  OG1   . THR   B  1  716  ? 12.408  28.797  69.546  1.00 13.95 ? 714  THR   B OG1   1 
ATOM   14306 C  CG2   . THR   B  1  716  ? 10.440  30.104  69.094  1.00 14.16 ? 714  THR   B CG2   1 
ATOM   14307 N  N     . GLY   B  1  717  ? 12.048  33.137  70.442  1.00 12.20 ? 715  GLY   B N     1 
ATOM   14308 C  CA    . GLY   B  1  717  ? 11.357  34.407  70.591  1.00 12.75 ? 715  GLY   B CA    1 
ATOM   14309 C  C     . GLY   B  1  717  ? 11.859  35.469  69.633  1.00 12.28 ? 715  GLY   B C     1 
ATOM   14310 O  O     . GLY   B  1  717  ? 11.071  36.130  68.953  1.00 12.96 ? 715  GLY   B O     1 
ATOM   14311 N  N     . GLN   B  1  718  ? 13.177  35.650  69.554  1.00 11.49 ? 716  GLN   B N     1 
ATOM   14312 C  CA    . GLN   B  1  718  ? 13.683  36.702  68.684  1.00 11.89 ? 716  GLN   B CA    1 
ATOM   14313 C  C     . GLN   B  1  718  ? 13.333  36.407  67.236  1.00 12.49 ? 716  GLN   B C     1 
ATOM   14314 O  O     . GLN   B  1  718  ? 12.870  37.283  66.502  1.00 12.09 ? 716  GLN   B O     1 
ATOM   14315 C  CB    . GLN   B  1  718  ? 15.199  36.834  68.822  1.00 11.15 ? 716  GLN   B CB    1 
ATOM   14316 C  CG    . GLN   B  1  718  ? 15.632  37.201  70.243  1.00 11.69 ? 716  GLN   B CG    1 
ATOM   14317 C  CD    . GLN   B  1  718  ? 17.103  37.493  70.348  1.00 12.70 ? 716  GLN   B CD    1 
ATOM   14318 O  OE1   . GLN   B  1  718  ? 17.496  38.489  70.955  1.00 14.11 ? 716  GLN   B OE1   1 
ATOM   14319 N  NE2   . GLN   B  1  718  ? 17.930  36.642  69.755  1.00 13.98 ? 716  GLN   B NE2   1 
ATOM   14320 N  N     . ILE   B  1  719  ? 13.557  35.165  66.817  1.00 11.69 ? 717  ILE   B N     1 
ATOM   14321 C  CA    . ILE   B  1  719  ? 13.316  34.774  65.435  1.00 12.22 ? 717  ILE   B CA    1 
ATOM   14322 C  C     . ILE   B  1  719  ? 11.846  34.907  65.097  1.00 12.05 ? 717  ILE   B C     1 
ATOM   14323 O  O     . ILE   B  1  719  ? 11.485  35.414  64.030  1.00 12.58 ? 717  ILE   B O     1 
ATOM   14324 C  CB    . ILE   B  1  719  ? 13.801  33.335  65.222  1.00 13.64 ? 717  ILE   B CB    1 
ATOM   14325 C  CG1   . ILE   B  1  719  ? 15.313  33.283  65.327  1.00 13.29 ? 717  ILE   B CG1   1 
ATOM   14326 C  CG2   . ILE   B  1  719  ? 13.299  32.790  63.904  1.00 17.56 ? 717  ILE   B CG2   1 
ATOM   14327 C  CD1   . ILE   B  1  719  ? 15.777  31.883  65.493  1.00 20.31 ? 717  ILE   B CD1   1 
ATOM   14328 N  N     . ALA   B  1  720  ? 10.978  34.439  65.994  1.00 11.78 ? 718  ALA   B N     1 
ATOM   14329 C  CA    . ALA   B  1  720  ? 9.552   34.472  65.736  1.00 12.19 ? 718  ALA   B CA    1 
ATOM   14330 C  C     . ALA   B  1  720  ? 9.077   35.896  65.555  1.00 12.30 ? 718  ALA   B C     1 
ATOM   14331 O  O     . ALA   B  1  720  ? 8.277   36.190  64.648  1.00 12.38 ? 718  ALA   B O     1 
ATOM   14332 C  CB    . ALA   B  1  720  ? 8.806   33.811  66.888  1.00 13.61 ? 718  ALA   B CB    1 
ATOM   14333 N  N     . ALA   B  1  721  ? 9.537   36.790  66.425  1.00 11.79 ? 719  ALA   B N     1 
ATOM   14334 C  CA    . ALA   B  1  721  ? 9.123   38.175  66.323  1.00 12.75 ? 719  ALA   B CA    1 
ATOM   14335 C  C     . ALA   B  1  721  ? 9.592   38.782  65.019  1.00 11.73 ? 719  ALA   B C     1 
ATOM   14336 O  O     . ALA   B  1  721  ? 8.824   39.453  64.322  1.00 12.45 ? 719  ALA   B O     1 
ATOM   14337 C  CB    . ALA   B  1  721  ? 9.663   38.954  67.521  1.00 13.40 ? 719  ALA   B CB    1 
ATOM   14338 N  N     . ALA   B  1  722  ? 10.856  38.561  64.678  1.00 11.58 ? 720  ALA   B N     1 
ATOM   14339 C  CA    . ALA   B  1  722  ? 11.371  39.141  63.447  1.00 10.85 ? 720  ALA   B CA    1 
ATOM   14340 C  C     . ALA   B  1  722  ? 10.612  38.605  62.243  1.00 12.67 ? 720  ALA   B C     1 
ATOM   14341 O  O     . ALA   B  1  722  ? 10.209  39.369  61.359  1.00 12.83 ? 720  ALA   B O     1 
ATOM   14342 C  CB    . ALA   B  1  722  ? 12.863  38.853  63.333  1.00 11.75 ? 720  ALA   B CB    1 
ATOM   14343 N  N     . LEU   B  1  723  ? 10.398  37.290  62.207  1.00 12.21 ? 721  LEU   B N     1 
ATOM   14344 C  CA    . LEU   B  1  723  ? 9.686   36.688  61.085  1.00 12.84 ? 721  LEU   B CA    1 
ATOM   14345 C  C     . LEU   B  1  723  ? 8.272   37.219  60.980  1.00 13.59 ? 721  LEU   B C     1 
ATOM   14346 O  O     . LEU   B  1  723  ? 7.799   37.542  59.883  1.00 12.93 ? 721  LEU   B O     1 
ATOM   14347 C  CB    . LEU   B  1  723  ? 9.612   35.180  61.272  1.00 12.60 ? 721  LEU   B CB    1 
ATOM   14348 C  CG    . LEU   B  1  723  ? 10.909  34.424  61.024  1.00 13.05 ? 721  LEU   B CG    1 
ATOM   14349 C  CD1   . LEU   B  1  723  ? 10.719  32.998  61.493  1.00 13.60 ? 721  LEU   B CD1   1 
ATOM   14350 C  CD2   . LEU   B  1  723  ? 11.285  34.489  59.553  1.00 14.73 ? 721  LEU   B CD2   1 
ATOM   14351 N  N     . VAL   B  1  724  ? 7.548   37.246  62.097  1.00 12.44 ? 722  VAL   B N     1 
ATOM   14352 C  CA    . VAL   B  1  724  ? 6.141   37.602  62.016  1.00 11.71 ? 722  VAL   B CA    1 
ATOM   14353 C  C     . VAL   B  1  724  ? 5.984   39.072  61.661  1.00 13.10 ? 722  VAL   B C     1 
ATOM   14354 O  O     . VAL   B  1  724  ? 4.987   39.468  61.042  1.00 13.99 ? 722  VAL   B O     1 
ATOM   14355 C  CB    . VAL   B  1  724  ? 5.374   37.169  63.282  1.00 11.25 ? 722  VAL   B CB    1 
ATOM   14356 C  CG1   . VAL   B  1  724  ? 5.571   38.167  64.425  1.00 13.74 ? 722  VAL   B CG1   1 
ATOM   14357 C  CG2   . VAL   B  1  724  ? 3.903   36.952  62.953  1.00 13.10 ? 722  VAL   B CG2   1 
ATOM   14358 N  N     . ALA   B  1  725  ? 6.977   39.890  61.999  1.00 13.95 ? 723  ALA   B N     1 
ATOM   14359 C  CA    . ALA   B  1  725  ? 6.996   41.280  61.571  1.00 13.53 ? 723  ALA   B CA    1 
ATOM   14360 C  C     . ALA   B  1  725  ? 7.336   41.421  60.093  1.00 15.34 ? 723  ALA   B C     1 
ATOM   14361 O  O     . ALA   B  1  725  ? 7.356   42.545  59.582  1.00 16.41 ? 723  ALA   B O     1 
ATOM   14362 C  CB    . ALA   B  1  725  ? 7.943   42.089  62.459  1.00 13.50 ? 723  ALA   B CB    1 
ATOM   14363 N  N     . GLY   B  1  726  ? 7.603   40.322  59.403  1.00 13.11 ? 724  GLY   B N     1 
ATOM   14364 C  CA    . GLY   B  1  726  ? 7.797   40.349  57.971  1.00 13.86 ? 724  GLY   B CA    1 
ATOM   14365 C  C     . GLY   B  1  726  ? 9.238   40.374  57.527  1.00 15.20 ? 724  GLY   B C     1 
ATOM   14366 O  O     . GLY   B  1  726  ? 9.496   40.684  56.359  1.00 15.78 ? 724  GLY   B O     1 
ATOM   14367 N  N     . ASN   B  1  727  ? 10.185  40.061  58.418  1.00 13.01 ? 725  ASN   B N     1 
ATOM   14368 C  CA    . ASN   B  1  727  ? 11.600  40.106  58.125  1.00 13.56 ? 725  ASN   B CA    1 
ATOM   14369 C  C     . ASN   B  1  727  ? 12.134  38.702  57.965  1.00 13.19 ? 725  ASN   B C     1 
ATOM   14370 O  O     . ASN   B  1  727  ? 11.847  37.835  58.799  1.00 14.40 ? 725  ASN   B O     1 
ATOM   14371 C  CB    . ASN   B  1  727  ? 12.341  40.762  59.285  1.00 14.06 ? 725  ASN   B CB    1 
ATOM   14372 C  CG    . ASN   B  1  727  ? 11.782  42.110  59.643  1.00 15.79 ? 725  ASN   B CG    1 
ATOM   14373 O  OD1   . ASN   B  1  727  ? 12.066  43.099  58.974  1.00 14.77 ? 725  ASN   B OD1   1 
ATOM   14374 N  ND2   . ASN   B  1  727  ? 10.978  42.163  60.699  1.00 13.05 ? 725  ASN   B ND2   1 
ATOM   14375 N  N     . PRO   B  1  728  ? 12.943  38.448  56.948  1.00 12.32 ? 726  PRO   B N     1 
ATOM   14376 C  CA    . PRO   B  1  728  ? 13.677  37.190  56.904  1.00 13.77 ? 726  PRO   B CA    1 
ATOM   14377 C  C     . PRO   B  1  728  ? 14.753  37.249  57.964  1.00 14.96 ? 726  PRO   B C     1 
ATOM   14378 O  O     . PRO   B  1  728  ? 15.241  38.325  58.319  1.00 14.51 ? 726  PRO   B O     1 
ATOM   14379 C  CB    . PRO   B  1  728  ? 14.296  37.194  55.506  1.00 15.19 ? 726  PRO   B CB    1 
ATOM   14380 C  CG    . PRO   B  1  728  ? 14.472  38.648  55.184  1.00 16.40 ? 726  PRO   B CG    1 
ATOM   14381 C  CD    . PRO   B  1  728  ? 13.351  39.385  55.891  1.00 14.01 ? 726  PRO   B CD    1 
ATOM   14382 N  N     . VAL   B  1  729  ? 15.114  36.079  58.470  1.00 12.43 ? 727  VAL   B N     1 
ATOM   14383 C  CA    . VAL   B  1  729  ? 15.961  35.987  59.649  1.00 12.31 ? 727  VAL   B CA    1 
ATOM   14384 C  C     . VAL   B  1  729  ? 17.206  35.171  59.366  1.00 13.99 ? 727  VAL   B C     1 
ATOM   14385 O  O     . VAL   B  1  729  ? 17.153  34.105  58.737  1.00 13.53 ? 727  VAL   B O     1 
ATOM   14386 C  CB    . VAL   B  1  729  ? 15.189  35.370  60.826  1.00 12.59 ? 727  VAL   B CB    1 
ATOM   14387 C  CG1   . VAL   B  1  729  ? 16.145  34.977  61.953  1.00 13.51 ? 727  VAL   B CG1   1 
ATOM   14388 C  CG2   . VAL   B  1  729  ? 14.154  36.341  61.326  1.00 14.30 ? 727  VAL   B CG2   1 
ATOM   14389 N  N     . LEU   B  1  730  ? 18.327  35.659  59.884  1.00 12.41 ? 728  LEU   B N     1 
ATOM   14390 C  CA    . LEU   B  1  730  ? 19.560  34.896  59.970  1.00 12.41 ? 728  LEU   B CA    1 
ATOM   14391 C  C     . LEU   B  1  730  ? 19.714  34.561  61.441  1.00 12.18 ? 728  LEU   B C     1 
ATOM   14392 O  O     . LEU   B  1  730  ? 19.927  35.452  62.262  1.00 13.97 ? 728  LEU   B O     1 
ATOM   14393 C  CB    . LEU   B  1  730  ? 20.745  35.730  59.497  1.00 13.66 ? 728  LEU   B CB    1 
ATOM   14394 C  CG    . LEU   B  1  730  ? 20.767  36.234  58.052  1.00 14.99 ? 728  LEU   B CG    1 
ATOM   14395 C  CD1   . LEU   B  1  730  ? 20.358  35.120  57.082  1.00 15.76 ? 728  LEU   B CD1   1 
ATOM   14396 C  CD2   . LEU   B  1  730  ? 19.912  37.492  57.855  1.00 15.22 ? 728  LEU   B CD2   1 
ATOM   14397 N  N     . ALA   B  1  731  ? 19.588  33.295  61.777  1.00 12.82 ? 729  ALA   B N     1 
ATOM   14398 C  CA    . ALA   B  1  731  ? 19.573  32.858  63.167  1.00 12.62 ? 729  ALA   B CA    1 
ATOM   14399 C  C     . ALA   B  1  731  ? 20.945  32.320  63.522  1.00 13.94 ? 729  ALA   B C     1 
ATOM   14400 O  O     . ALA   B  1  731  ? 21.384  31.311  62.965  1.00 12.76 ? 729  ALA   B O     1 
ATOM   14401 C  CB    . ALA   B  1  731  ? 18.500  31.795  63.371  1.00 15.24 ? 729  ALA   B CB    1 
ATOM   14402 N  N     . LYS   B  1  732  ? 21.623  33.006  64.442  1.00 13.02 ? 730  LYS   B N     1 
ATOM   14403 C  CA    . LYS   B  1  732  ? 22.961  32.630  64.882  1.00 12.87 ? 730  LYS   B CA    1 
ATOM   14404 C  C     . LYS   B  1  732  ? 22.870  32.198  66.336  1.00 12.12 ? 730  LYS   B C     1 
ATOM   14405 O  O     . LYS   B  1  732  ? 22.889  33.048  67.245  1.00 13.40 ? 730  LYS   B O     1 
ATOM   14406 C  CB    . LYS   B  1  732  ? 23.928  33.806  64.719  1.00 12.95 ? 730  LYS   B CB    1 
ATOM   14407 C  CG    . LYS   B  1  732  ? 25.364  33.413  64.398  1.00 13.95 ? 730  LYS   B CG    1 
ATOM   14408 C  CD    . LYS   B  1  732  ? 25.975  32.511  65.455  1.00 13.86 ? 730  LYS   B CD    1 
ATOM   14409 C  CE    . LYS   B  1  732  ? 26.321  33.279  66.721  1.00 14.65 ? 730  LYS   B CE    1 
ATOM   14410 N  NZ    . LYS   B  1  732  ? 26.885  32.335  67.726  1.00 13.82 ? 730  LYS   B NZ    1 
ATOM   14411 N  N     . PRO   B  1  733  ? 22.746  30.908  66.606  1.00 12.60 ? 731  PRO   B N     1 
ATOM   14412 C  CA    . PRO   B  1  733  ? 22.626  30.447  67.989  1.00 13.81 ? 731  PRO   B CA    1 
ATOM   14413 C  C     . PRO   B  1  733  ? 23.985  30.425  68.650  1.00 12.77 ? 731  PRO   B C     1 
ATOM   14414 O  O     . PRO   B  1  733  ? 25.031  30.387  67.997  1.00 13.28 ? 731  PRO   B O     1 
ATOM   14415 C  CB    . PRO   B  1  733  ? 22.108  29.017  67.828  1.00 15.33 ? 731  PRO   B CB    1 
ATOM   14416 C  CG    . PRO   B  1  733  ? 22.731  28.569  66.518  1.00 14.80 ? 731  PRO   B CG    1 
ATOM   14417 C  CD    . PRO   B  1  733  ? 22.712  29.800  65.633  1.00 12.90 ? 731  PRO   B CD    1 
ATOM   14418 N  N     . ALA   B  1  734  ? 23.951  30.426  69.975  1.00 13.47 ? 732  ALA   B N     1 
ATOM   14419 C  CA    . ALA   B  1  734  ? 25.187  30.348  70.739  1.00 13.75 ? 732  ALA   B CA    1 
ATOM   14420 C  C     . ALA   B  1  734  ? 25.966  29.099  70.352  1.00 14.19 ? 732  ALA   B C     1 
ATOM   14421 O  O     . ALA   B  1  734  ? 25.402  28.047  70.026  1.00 15.11 ? 732  ALA   B O     1 
ATOM   14422 C  CB    . ALA   B  1  734  ? 24.865  30.283  72.228  1.00 14.55 ? 732  ALA   B CB    1 
ATOM   14423 N  N     . GLU   B  1  735  ? 27.288  29.222  70.390  1.00 14.14 ? 733  GLU   B N     1 
ATOM   14424 C  CA    . GLU   B  1  735  ? 28.120  28.100  69.982  1.00 15.70 ? 733  GLU   B CA    1 
ATOM   14425 C  C     . GLU   B  1  735  ? 27.949  26.897  70.898  1.00 15.16 ? 733  GLU   B C     1 
ATOM   14426 O  O     . GLU   B  1  735  ? 28.151  25.764  70.456  1.00 15.43 ? 733  GLU   B O     1 
ATOM   14427 C  CB    . GLU   B  1  735  ? 29.588  28.522  69.897  1.00 16.75 ? 733  GLU   B CB    1 
ATOM   14428 C  CG    . GLU   B  1  735  ? 30.140  29.139  71.169  1.00 19.73 ? 733  GLU   B CG    1 
ATOM   14429 C  CD    . GLU   B  1  735  ? 30.045  30.668  71.203  1.00 20.94 ? 733  GLU   B CD    1 
ATOM   14430 O  OE1   . GLU   B  1  735  ? 29.078  31.253  70.669  1.00 20.82 ? 733  GLU   B OE1   1 
ATOM   14431 O  OE2   . GLU   B  1  735  ? 30.962  31.295  71.776  1.00 23.22 ? 733  GLU   B OE2   1 
ATOM   14432 N  N     . GLU   B  1  736  ? 27.533  27.119  72.145  1.00 14.84 ? 734  GLU   B N     1 
ATOM   14433 C  CA    . GLU   B  1  736  ? 27.397  26.009  73.076  1.00 14.60 ? 734  GLU   B CA    1 
ATOM   14434 C  C     . GLU   B  1  736  ? 26.167  25.158  72.790  1.00 14.49 ? 734  GLU   B C     1 
ATOM   14435 O  O     . GLU   B  1  736  ? 26.145  23.978  73.153  1.00 16.56 ? 734  GLU   B O     1 
ATOM   14436 C  CB    . GLU   B  1  736  ? 27.298  26.534  74.508  1.00 13.93 ? 734  GLU   B CB    1 
ATOM   14437 C  CG    . GLU   B  1  736  ? 28.546  27.241  75.000  1.00 17.14 ? 734  GLU   B CG    1 
ATOM   14438 C  CD    . GLU   B  1  736  ? 28.504  28.747  74.789  1.00 17.51 ? 734  GLU   B CD    1 
ATOM   14439 O  OE1   . GLU   B  1  736  ? 27.747  29.239  73.923  1.00 17.01 ? 734  GLU   B OE1   1 
ATOM   14440 O  OE2   . GLU   B  1  736  ? 29.247  29.453  75.497  1.00 23.44 ? 734  GLU   B OE2   1 
ATOM   14441 N  N     . THR   B  1  737  ? 25.127  25.720  72.170  1.00 14.43 ? 735  THR   B N     1 
ATOM   14442 C  CA    . THR   B  1  737  ? 23.821  25.053  72.112  1.00 15.19 ? 735  THR   B CA    1 
ATOM   14443 C  C     . THR   B  1  737  ? 23.214  25.120  70.721  1.00 14.53 ? 735  THR   B C     1 
ATOM   14444 O  O     . THR   B  1  737  ? 22.071  25.539  70.543  1.00 15.42 ? 735  THR   B O     1 
ATOM   14445 C  CB    . THR   B  1  737  ? 22.872  25.644  73.152  1.00 13.27 ? 735  THR   B CB    1 
ATOM   14446 O  OG1   . THR   B  1  737  ? 22.829  27.068  72.983  1.00 14.13 ? 735  THR   B OG1   1 
ATOM   14447 C  CG2   . THR   B  1  737  ? 23.352  25.306  74.558  1.00 15.35 ? 735  THR   B CG2   1 
ATOM   14448 N  N     . PRO   B  1  738  ? 23.936  24.655  69.711  1.00 13.03 ? 736  PRO   B N     1 
ATOM   14449 C  CA    . PRO   B  1  738  ? 23.401  24.724  68.349  1.00 13.92 ? 736  PRO   B CA    1 
ATOM   14450 C  C     . PRO   B  1  738  ? 22.342  23.678  68.054  1.00 14.20 ? 736  PRO   B C     1 
ATOM   14451 O  O     . PRO   B  1  738  ? 21.567  23.877  67.112  1.00 13.94 ? 736  PRO   B O     1 
ATOM   14452 C  CB    . PRO   B  1  738  ? 24.647  24.464  67.492  1.00 14.61 ? 736  PRO   B CB    1 
ATOM   14453 C  CG    . PRO   B  1  738  ? 25.424  23.495  68.342  1.00 15.49 ? 736  PRO   B CG    1 
ATOM   14454 C  CD    . PRO   B  1  738  ? 25.260  24.004  69.744  1.00 14.95 ? 736  PRO   B CD    1 
ATOM   14455 N  N     . LEU   B  1  739  ? 22.301  22.561  68.785  1.00 13.31 ? 737  LEU   B N     1 
ATOM   14456 C  CA    . LEU   B  1  739  ? 21.433  21.467  68.360  1.00 14.37 ? 737  LEU   B CA    1 
ATOM   14457 C  C     . LEU   B  1  739  ? 19.972  21.811  68.570  1.00 14.08 ? 737  LEU   B C     1 
ATOM   14458 O  O     . LEU   B  1  739  ? 19.146  21.596  67.680  1.00 14.05 ? 737  LEU   B O     1 
ATOM   14459 C  CB    . LEU   B  1  739  ? 21.789  20.178  69.089  1.00 13.64 ? 737  LEU   B CB    1 
ATOM   14460 C  CG    . LEU   B  1  739  ? 23.229  19.739  68.866  1.00 13.84 ? 737  LEU   B CG    1 
ATOM   14461 C  CD1   . LEU   B  1  739  ? 23.449  18.525  69.729  1.00 15.29 ? 737  LEU   B CD1   1 
ATOM   14462 C  CD2   . LEU   B  1  739  ? 23.486  19.427  67.393  1.00 16.43 ? 737  LEU   B CD2   1 
ATOM   14463 N  N     . ILE   B  1  740  ? 19.627  22.341  69.742  1.00 13.62 ? 738  ILE   B N     1 
ATOM   14464 C  CA    . ILE   B  1  740  ? 18.222  22.675  69.951  1.00 13.68 ? 738  ILE   B CA    1 
ATOM   14465 C  C     . ILE   B  1  740  ? 17.815  23.833  69.055  1.00 13.50 ? 738  ILE   B C     1 
ATOM   14466 O  O     . ILE   B  1  740  ? 16.659  23.924  68.640  1.00 13.92 ? 738  ILE   B O     1 
ATOM   14467 C  CB    . ILE   B  1  740  ? 17.920  22.928  71.441  1.00 16.39 ? 738  ILE   B CB    1 
ATOM   14468 C  CG1   . ILE   B  1  740  ? 16.411  23.078  71.679  1.00 15.88 ? 738  ILE   B CG1   1 
ATOM   14469 C  CG2   . ILE   B  1  740  ? 18.678  24.139  71.923  1.00 15.88 ? 738  ILE   B CG2   1 
ATOM   14470 C  CD1   . ILE   B  1  740  ? 15.613  21.828  71.376  1.00 17.73 ? 738  ILE   B CD1   1 
ATOM   14471 N  N     . ALA   B  1  741  ? 18.746  24.742  68.748  1.00 12.00 ? 739  ALA   B N     1 
ATOM   14472 C  CA    . ALA   B  1  741  ? 18.430  25.822  67.828  1.00 12.72 ? 739  ALA   B CA    1 
ATOM   14473 C  C     . ALA   B  1  741  ? 18.136  25.270  66.448  1.00 13.45 ? 739  ALA   B C     1 
ATOM   14474 O  O     . ALA   B  1  741  ? 17.172  25.692  65.800  1.00 13.78 ? 739  ALA   B O     1 
ATOM   14475 C  CB    . ALA   B  1  741  ? 19.596  26.800  67.761  1.00 14.55 ? 739  ALA   B CB    1 
ATOM   14476 N  N     . ALA   B  1  742  ? 18.946  24.313  65.988  1.00 13.45 ? 740  ALA   B N     1 
ATOM   14477 C  CA    . ALA   B  1  742  ? 18.678  23.688  64.703  1.00 13.48 ? 740  ALA   B CA    1 
ATOM   14478 C  C     . ALA   B  1  742  ? 17.300  23.055  64.700  1.00 13.41 ? 740  ALA   B C     1 
ATOM   14479 O  O     . ALA   B  1  742  ? 16.574  23.135  63.701  1.00 13.87 ? 740  ALA   B O     1 
ATOM   14480 C  CB    . ALA   B  1  742  ? 19.742  22.640  64.393  1.00 15.79 ? 740  ALA   B CB    1 
ATOM   14481 N  N     . GLU   B  1  743  ? 16.916  22.441  65.817  1.00 14.73 ? 741  GLU   B N     1 
ATOM   14482 C  CA    . GLU   B  1  743  ? 15.599  21.828  65.891  1.00 14.41 ? 741  GLU   B CA    1 
ATOM   14483 C  C     . GLU   B  1  743  ? 14.511  22.888  65.859  1.00 13.67 ? 741  GLU   B C     1 
ATOM   14484 O  O     . GLU   B  1  743  ? 13.484  22.707  65.195  1.00 14.64 ? 741  GLU   B O     1 
ATOM   14485 C  CB    . GLU   B  1  743  ? 15.519  20.962  67.144  1.00 14.98 ? 741  GLU   B CB    1 
ATOM   14486 C  CG    . GLU   B  1  743  ? 14.189  20.293  67.313  1.00 15.28 ? 741  GLU   B CG    1 
ATOM   14487 C  CD    . GLU   B  1  743  ? 13.894  19.228  66.287  1.00 17.65 ? 741  GLU   B CD    1 
ATOM   14488 O  OE1   . GLU   B  1  743  ? 14.771  18.871  65.471  1.00 17.17 ? 741  GLU   B OE1   1 
ATOM   14489 O  OE2   . GLU   B  1  743  ? 12.749  18.727  66.310  1.00 21.02 ? 741  GLU   B OE2   1 
ATOM   14490 N  N     . GLY   B  1  744  ? 14.734  24.022  66.524  1.00 13.92 ? 742  GLY   B N     1 
ATOM   14491 C  CA    . GLY   B  1  744  ? 13.788  25.120  66.419  1.00 14.72 ? 742  GLY   B CA    1 
ATOM   14492 C  C     . GLY   B  1  744  ? 13.595  25.574  64.983  1.00 12.21 ? 742  GLY   B C     1 
ATOM   14493 O  O     . GLY   B  1  744  ? 12.471  25.825  64.548  1.00 13.22 ? 742  GLY   B O     1 
ATOM   14494 N  N     . VAL   B  1  745  ? 14.685  25.688  64.226  1.00 13.02 ? 743  VAL   B N     1 
ATOM   14495 C  CA    . VAL   B  1  745  ? 14.563  26.110  62.836  1.00 12.60 ? 743  VAL   B CA    1 
ATOM   14496 C  C     . VAL   B  1  745  ? 13.851  25.047  62.013  1.00 14.02 ? 743  VAL   B C     1 
ATOM   14497 O  O     . VAL   B  1  745  ? 13.024  25.373  61.152  1.00 14.02 ? 743  VAL   B O     1 
ATOM   14498 C  CB    . VAL   B  1  745  ? 15.941  26.484  62.266  1.00 14.82 ? 743  VAL   B CB    1 
ATOM   14499 C  CG1   . VAL   B  1  745  ? 15.874  26.599  60.737  1.00 13.85 ? 743  VAL   B CG1   1 
ATOM   14500 C  CG2   . VAL   B  1  745  ? 16.374  27.785  62.874  1.00 14.87 ? 743  VAL   B CG2   1 
ATOM   14501 N  N     . ARG   B  1  746  ? 14.149  23.763  62.255  1.00 13.92 ? 744  ARG   B N     1 
ATOM   14502 C  CA    . ARG   B  1  746  ? 13.421  22.699  61.560  1.00 14.46 ? 744  ARG   B CA    1 
ATOM   14503 C  C     . ARG   B  1  746  ? 11.923  22.850  61.776  1.00 12.81 ? 744  ARG   B C     1 
ATOM   14504 O  O     . ARG   B  1  746  ? 11.130  22.675  60.847  1.00 13.58 ? 744  ARG   B O     1 
ATOM   14505 C  CB    . ARG   B  1  746  ? 13.820  21.317  62.085  1.00 14.16 ? 744  ARG   B CB    1 
ATOM   14506 C  CG    . ARG   B  1  746  ? 15.204  20.862  61.732  1.00 16.35 ? 744  ARG   B CG    1 
ATOM   14507 C  CD    . ARG   B  1  746  ? 15.401  19.448  62.245  1.00 15.39 ? 744  ARG   B CD    1 
ATOM   14508 N  NE    . ARG   B  1  746  ? 16.798  19.079  62.107  1.00 16.81 ? 744  ARG   B NE    1 
ATOM   14509 C  CZ    . ARG   B  1  746  ? 17.702  19.163  63.069  1.00 14.79 ? 744  ARG   B CZ    1 
ATOM   14510 N  NH1   . ARG   B  1  746  ? 17.353  19.331  64.333  1.00 16.08 ? 744  ARG   B NH1   1 
ATOM   14511 N  NH2   . ARG   B  1  746  ? 18.988  19.075  62.750  1.00 17.07 ? 744  ARG   B NH2   1 
ATOM   14512 N  N     . ILE   B  1  747  ? 11.522  23.135  63.009  1.00 13.49 ? 745  ILE   B N     1 
ATOM   14513 C  CA    . ILE   B  1  747  ? 10.105  23.208  63.338  1.00 12.99 ? 745  ILE   B CA    1 
ATOM   14514 C  C     . ILE   B  1  747  ? 9.469   24.432  62.703  1.00 14.46 ? 745  ILE   B C     1 
ATOM   14515 O  O     . ILE   B  1  747  ? 8.369   24.352  62.142  1.00 13.01 ? 745  ILE   B O     1 
ATOM   14516 C  CB    . ILE   B  1  747  ? 9.924   23.178  64.865  1.00 13.12 ? 745  ILE   B CB    1 
ATOM   14517 C  CG1   . ILE   B  1  747  ? 10.161  21.755  65.361  1.00 15.32 ? 745  ILE   B CG1   1 
ATOM   14518 C  CG2   . ILE   B  1  747  ? 8.527   23.655  65.231  1.00 14.20 ? 745  ILE   B CG2   1 
ATOM   14519 C  CD1   . ILE   B  1  747  ? 10.267  21.641  66.856  1.00 16.43 ? 745  ILE   B CD1   1 
ATOM   14520 N  N     . LEU   B  1  748  ? 10.150  25.580  62.750  1.00 13.10 ? 746  LEU   B N     1 
ATOM   14521 C  CA    . LEU   B  1  748  ? 9.603   26.768  62.100  1.00 12.68 ? 746  LEU   B CA    1 
ATOM   14522 C  C     . LEU   B  1  748  ? 9.487   26.573  60.599  1.00 13.53 ? 746  LEU   B C     1 
ATOM   14523 O  O     . LEU   B  1  748  ? 8.505   26.993  59.992  1.00 13.26 ? 746  LEU   B O     1 
ATOM   14524 C  CB    . LEU   B  1  748  ? 10.448  27.992  62.411  1.00 13.56 ? 746  LEU   B CB    1 
ATOM   14525 C  CG    . LEU   B  1  748  ? 10.119  28.618  63.764  1.00 16.04 ? 746  LEU   B CG    1 
ATOM   14526 C  CD1   . LEU   B  1  748  ? 11.270  29.501  64.252  1.00 17.75 ? 746  LEU   B CD1   1 
ATOM   14527 C  CD2   . LEU   B  1  748  ? 8.871   29.437  63.625  1.00 18.83 ? 746  LEU   B CD2   1 
ATOM   14528 N  N     . ARG   B  1  749  ? 10.494  25.969  59.972  1.00 13.12 ? 747  ARG   B N     1 
ATOM   14529 C  CA    . ARG   B  1  749  ? 10.375  25.688  58.546  1.00 13.79 ? 747  ARG   B CA    1 
ATOM   14530 C  C     . ARG   B  1  749  ? 9.240   24.714  58.275  1.00 13.65 ? 747  ARG   B C     1 
ATOM   14531 O  O     . ARG   B  1  749  ? 8.472   24.901  57.322  1.00 14.07 ? 747  ARG   B O     1 
ATOM   14532 C  CB    . ARG   B  1  749  ? 11.692  25.149  58.008  1.00 13.35 ? 747  ARG   B CB    1 
ATOM   14533 C  CG    . ARG   B  1  749  ? 12.733  26.218  57.825  1.00 14.45 ? 747  ARG   B CG    1 
ATOM   14534 C  CD    . ARG   B  1  749  ? 13.922  25.615  57.120  1.00 17.12 ? 747  ARG   B CD    1 
ATOM   14535 N  NE    . ARG   B  1  749  ? 14.946  26.608  56.841  1.00 16.80 ? 747  ARG   B NE    1 
ATOM   14536 C  CZ    . ARG   B  1  749  ? 15.981  26.379  56.053  1.00 20.96 ? 747  ARG   B CZ    1 
ATOM   14537 N  NH1   . ARG   B  1  749  ? 16.136  25.213  55.450  1.00 21.07 ? 747  ARG   B NH1   1 
ATOM   14538 N  NH2   . ARG   B  1  749  ? 16.876  27.344  55.860  1.00 21.26 ? 747  ARG   B NH2   1 
ATOM   14539 N  N     . GLU   B  1  750  ? 9.105   23.677  59.110  1.00 12.77 ? 748  GLU   B N     1 
ATOM   14540 C  CA    . GLU   B  1  750  ? 8.026   22.718  58.906  1.00 13.73 ? 748  GLU   B CA    1 
ATOM   14541 C  C     . GLU   B  1  750  ? 6.674   23.400  59.022  1.00 12.79 ? 748  GLU   B C     1 
ATOM   14542 O  O     . GLU   B  1  750  ? 5.728   23.048  58.313  1.00 15.11 ? 748  GLU   B O     1 
ATOM   14543 C  CB    . GLU   B  1  750  ? 8.134   21.590  59.930  1.00 13.98 ? 748  GLU   B CB    1 
ATOM   14544 C  CG    . GLU   B  1  750  ? 7.075   20.536  59.763  1.00 15.99 ? 748  GLU   B CG    1 
ATOM   14545 C  CD    . GLU   B  1  750  ? 7.288   19.354  60.682  1.00 17.83 ? 748  GLU   B CD    1 
ATOM   14546 O  OE1   . GLU   B  1  750  ? 8.353   19.281  61.322  1.00 18.03 ? 748  GLU   B OE1   1 
ATOM   14547 O  OE2   . GLU   B  1  750  ? 6.378   18.508  60.762  1.00 21.11 ? 748  GLU   B OE2   1 
ATOM   14548 N  N     . ALA   B  1  751  ? 6.587   24.408  59.872  1.00 13.51 ? 749  ALA   B N     1 
ATOM   14549 C  CA    . ALA   B  1  751  ? 5.356   25.136  60.118  1.00 13.33 ? 749  ALA   B CA    1 
ATOM   14550 C  C     . ALA   B  1  751  ? 5.038   26.138  59.027  1.00 15.57 ? 749  ALA   B C     1 
ATOM   14551 O  O     . ALA   B  1  751  ? 3.971   26.749  59.072  1.00 16.27 ? 749  ALA   B O     1 
ATOM   14552 C  CB    . ALA   B  1  751  ? 5.479   25.864  61.450  1.00 14.43 ? 749  ALA   B CB    1 
ATOM   14553 N  N     . GLY   B  1  752  ? 5.917   26.324  58.053  1.00 14.69 ? 750  GLY   B N     1 
ATOM   14554 C  CA    . GLY   B  1  752  ? 5.614   27.156  56.905  1.00 14.83 ? 750  GLY   B CA    1 
ATOM   14555 C  C     . GLY   B  1  752  ? 6.577   28.295  56.671  1.00 15.15 ? 750  GLY   B C     1 
ATOM   14556 O  O     . GLY   B  1  752  ? 6.408   29.020  55.684  1.00 16.15 ? 750  GLY   B O     1 
ATOM   14557 N  N     . ILE   B  1  753  ? 7.572   28.524  57.524  1.00 14.62 ? 751  ILE   B N     1 
ATOM   14558 C  CA    . ILE   B  1  753  ? 8.526   29.600  57.268  1.00 14.49 ? 751  ILE   B CA    1 
ATOM   14559 C  C     . ILE   B  1  753  ? 9.427   29.160  56.122  1.00 15.83 ? 751  ILE   B C     1 
ATOM   14560 O  O     . ILE   B  1  753  ? 10.083  28.117  56.222  1.00 15.79 ? 751  ILE   B O     1 
ATOM   14561 C  CB    . ILE   B  1  753  ? 9.368   29.912  58.516  1.00 12.58 ? 751  ILE   B CB    1 
ATOM   14562 C  CG1   . ILE   B  1  753  ? 8.481   30.272  59.707  1.00 14.81 ? 751  ILE   B CG1   1 
ATOM   14563 C  CG2   . ILE   B  1  753  ? 10.349  31.028  58.199  1.00 16.08 ? 751  ILE   B CG2   1 
ATOM   14564 C  CD1   . ILE   B  1  753  ? 7.643   31.521  59.487  1.00 13.98 ? 751  ILE   B CD1   1 
ATOM   14565 N  N     . PRO   B  1  754  ? 9.471   29.906  55.021  1.00 16.07 ? 752  PRO   B N     1 
ATOM   14566 C  CA    . PRO   B  1  754  ? 10.283  29.490  53.872  1.00 15.36 ? 752  PRO   B CA    1 
ATOM   14567 C  C     . PRO   B  1  754  ? 11.757  29.443  54.232  1.00 14.90 ? 752  PRO   B C     1 
ATOM   14568 O  O     . PRO   B  1  754  ? 12.232  30.179  55.098  1.00 15.85 ? 752  PRO   B O     1 
ATOM   14569 C  CB    . PRO   B  1  754  ? 10.015  30.585  52.831  1.00 17.95 ? 752  PRO   B CB    1 
ATOM   14570 C  CG    . PRO   B  1  754  ? 8.738   31.238  53.265  1.00 20.70 ? 752  PRO   B CG    1 
ATOM   14571 C  CD    . PRO   B  1  754  ? 8.680   31.117  54.753  1.00 14.94 ? 752  PRO   B CD    1 
ATOM   14572 N  N     . ALA   B  1  755  ? 12.484  28.554  53.551  1.00 17.77 ? 753  ALA   B N     1 
ATOM   14573 C  CA    . ALA   B  1  755  ? 13.903  28.408  53.846  1.00 19.36 ? 753  ALA   B CA    1 
ATOM   14574 C  C     . ALA   B  1  755  ? 14.652  29.712  53.631  1.00 16.57 ? 753  ALA   B C     1 
ATOM   14575 O  O     . ALA   B  1  755  ? 15.590  30.025  54.375  1.00 18.94 ? 753  ALA   B O     1 
ATOM   14576 C  CB    . ALA   B  1  755  ? 14.501  27.292  52.992  1.00 22.80 ? 753  ALA   B CB    1 
ATOM   14577 N  N     . SER   B  1  756  ? 14.234  30.512  52.651  1.00 15.71 ? 754  SER   B N     1 
ATOM   14578 C  CA    . SER   B  1  756  ? 14.903  31.783  52.434  1.00 16.39 ? 754  SER   B CA    1 
ATOM   14579 C  C     . SER   B  1  756  ? 14.584  32.796  53.518  1.00 16.22 ? 754  SER   B C     1 
ATOM   14580 O  O     . SER   B  1  756  ? 15.324  33.776  53.665  1.00 16.88 ? 754  SER   B O     1 
ATOM   14581 C  CB    . SER   B  1  756  ? 14.528  32.347  51.078  1.00 19.10 ? 754  SER   B CB    1 
ATOM   14582 O  OG    . SER   B  1  756  ? 13.134  32.552  51.034  1.00 22.69 ? 754  SER   B OG    1 
ATOM   14583 N  N     . ALA   B  1  757  ? 13.489  32.604  54.250  1.00 14.07 ? 755  ALA   B N     1 
ATOM   14584 C  CA    . ALA   B  1  757  ? 13.147  33.505  55.332  1.00 12.66 ? 755  ALA   B CA    1 
ATOM   14585 C  C     . ALA   B  1  757  ? 13.772  33.115  56.659  1.00 13.56 ? 755  ALA   B C     1 
ATOM   14586 O  O     . ALA   B  1  757  ? 13.757  33.923  57.583  1.00 14.32 ? 755  ALA   B O     1 
ATOM   14587 C  CB    . ALA   B  1  757  ? 11.624  33.599  55.500  1.00 13.60 ? 755  ALA   B CB    1 
ATOM   14588 N  N     . LEU   B  1  758  ? 14.319  31.908  56.789  1.00 13.79 ? 756  LEU   B N     1 
ATOM   14589 C  CA    . LEU   B  1  758  ? 14.879  31.503  58.075  1.00 13.42 ? 756  LEU   B CA    1 
ATOM   14590 C  C     . LEU   B  1  758  ? 16.067  30.599  57.795  1.00 13.44 ? 756  LEU   B C     1 
ATOM   14591 O  O     . LEU   B  1  758  ? 15.904  29.432  57.427  1.00 15.11 ? 756  LEU   B O     1 
ATOM   14592 C  CB    . LEU   B  1  758  ? 13.861  30.790  58.940  1.00 13.35 ? 756  LEU   B CB    1 
ATOM   14593 C  CG    . LEU   B  1  758  ? 14.441  30.251  60.241  1.00 13.37 ? 756  LEU   B CG    1 
ATOM   14594 C  CD1   . LEU   B  1  758  ? 15.046  31.368  61.110  1.00 13.65 ? 756  LEU   B CD1   1 
ATOM   14595 C  CD2   . LEU   B  1  758  ? 13.329  29.537  60.997  1.00 14.22 ? 756  LEU   B CD2   1 
ATOM   14596 N  N     . GLN   B  1  759  ? 17.254  31.152  57.958  1.00 13.13 ? 757  GLN   B N     1 
ATOM   14597 C  CA    . GLN   B  1  759  ? 18.493  30.424  57.768  1.00 13.15 ? 757  GLN   B CA    1 
ATOM   14598 C  C     . GLN   B  1  759  ? 19.196  30.326  59.110  1.00 13.74 ? 757  GLN   B C     1 
ATOM   14599 O  O     . GLN   B  1  759  ? 19.166  31.271  59.902  1.00 14.66 ? 757  GLN   B O     1 
ATOM   14600 C  CB    . GLN   B  1  759  ? 19.361  31.160  56.758  1.00 13.08 ? 757  GLN   B CB    1 
ATOM   14601 C  CG    . GLN   B  1  759  ? 18.747  31.169  55.354  1.00 14.36 ? 757  GLN   B CG    1 
ATOM   14602 C  CD    . GLN   B  1  759  ? 19.525  32.041  54.421  1.00 14.65 ? 757  GLN   B CD    1 
ATOM   14603 O  OE1   . GLN   B  1  759  ? 20.388  31.568  53.687  1.00 17.32 ? 757  GLN   B OE1   1 
ATOM   14604 N  NE2   . GLN   B  1  759  ? 19.258  33.332  54.462  1.00 14.97 ? 757  GLN   B NE2   1 
ATOM   14605 N  N     . LEU   B  1  760  ? 19.809  29.177  59.358  1.00 13.57 ? 758  LEU   B N     1 
ATOM   14606 C  CA    . LEU   B  1  760  ? 20.516  28.903  60.601  1.00 13.17 ? 758  LEU   B CA    1 
ATOM   14607 C  C     . LEU   B  1  760  ? 22.007  28.935  60.317  1.00 14.64 ? 758  LEU   B C     1 
ATOM   14608 O  O     . LEU   B  1  760  ? 22.479  28.213  59.441  1.00 15.13 ? 758  LEU   B O     1 
ATOM   14609 C  CB    . LEU   B  1  760  ? 20.167  27.505  61.101  1.00 13.95 ? 758  LEU   B CB    1 
ATOM   14610 C  CG    . LEU   B  1  760  ? 20.865  27.121  62.406  1.00 13.38 ? 758  LEU   B CG    1 
ATOM   14611 C  CD1   . LEU   B  1  760  ? 20.170  27.789  63.570  1.00 16.46 ? 758  LEU   B CD1   1 
ATOM   14612 C  CD2   . LEU   B  1  760  ? 20.913  25.607  62.590  1.00 16.23 ? 758  LEU   B CD2   1 
ATOM   14613 N  N     . LEU   B  1  761  ? 22.758  29.728  61.087  1.00 14.05 ? 759  LEU   B N     1 
ATOM   14614 C  CA    . LEU   B  1  761  ? 24.200  29.878  60.908  1.00 13.77 ? 759  LEU   B CA    1 
ATOM   14615 C  C     . LEU   B  1  761  ? 24.867  29.526  62.229  1.00 13.11 ? 759  LEU   B C     1 
ATOM   14616 O  O     . LEU   B  1  761  ? 25.134  30.413  63.055  1.00 14.38 ? 759  LEU   B O     1 
ATOM   14617 C  CB    . LEU   B  1  761  ? 24.572  31.296  60.489  1.00 15.20 ? 759  LEU   B CB    1 
ATOM   14618 C  CG    . LEU   B  1  761  ? 24.056  31.840  59.145  1.00 15.93 ? 759  LEU   B CG    1 
ATOM   14619 C  CD1   . LEU   B  1  761  ? 24.130  30.810  58.008  1.00 17.52 ? 759  LEU   B CD1   1 
ATOM   14620 C  CD2   . LEU   B  1  761  ? 22.644  32.413  59.282  1.00 17.59 ? 759  LEU   B CD2   1 
ATOM   14621 N  N     . PRO   B  1  762  ? 25.117  28.253  62.489  1.00 13.83 ? 760  PRO   B N     1 
ATOM   14622 C  CA    . PRO   B  1  762  ? 25.817  27.902  63.726  1.00 13.75 ? 760  PRO   B CA    1 
ATOM   14623 C  C     . PRO   B  1  762  ? 27.234  28.430  63.691  1.00 14.80 ? 760  PRO   B C     1 
ATOM   14624 O  O     . PRO   B  1  762  ? 27.835  28.622  62.630  1.00 15.30 ? 760  PRO   B O     1 
ATOM   14625 C  CB    . PRO   B  1  762  ? 25.819  26.369  63.719  1.00 14.57 ? 760  PRO   B CB    1 
ATOM   14626 C  CG    . PRO   B  1  762  ? 24.765  25.973  62.739  1.00 15.28 ? 760  PRO   B CG    1 
ATOM   14627 C  CD    . PRO   B  1  762  ? 24.777  27.064  61.697  1.00 14.00 ? 760  PRO   B CD    1 
ATOM   14628 N  N     . GLY   B  1  763  ? 27.773  28.638  64.875  1.00 14.68 ? 761  GLY   B N     1 
ATOM   14629 C  CA    . GLY   B  1  763  ? 29.161  29.019  65.008  1.00 14.50 ? 761  GLY   B CA    1 
ATOM   14630 C  C     . GLY   B  1  763  ? 29.322  29.950  66.187  1.00 14.28 ? 761  GLY   B C     1 
ATOM   14631 O  O     . GLY   B  1  763  ? 28.412  30.136  66.994  1.00 16.25 ? 761  GLY   B O     1 
ATOM   14632 N  N     . ASP   B  1  764  ? 30.522  30.495  66.293  1.00 17.49 ? 762  ASP   B N     1 
ATOM   14633 C  CA    . ASP   B  1  764  ? 30.868  31.279  67.461  1.00 17.08 ? 762  ASP   B CA    1 
ATOM   14634 C  C     . ASP   B  1  764  ? 30.640  32.757  67.160  1.00 18.02 ? 762  ASP   B C     1 
ATOM   14635 O  O     . ASP   B  1  764  ? 29.943  33.118  66.204  1.00 17.10 ? 762  ASP   B O     1 
ATOM   14636 C  CB    . ASP   B  1  764  ? 32.276  30.917  67.939  1.00 18.81 ? 762  ASP   B CB    1 
ATOM   14637 C  CG    . ASP   B  1  764  ? 33.370  31.356  66.972  1.00 22.90 ? 762  ASP   B CG    1 
ATOM   14638 O  OD1   . ASP   B  1  764  ? 33.127  32.146  66.036  1.00 20.44 ? 762  ASP   B OD1   1 
ATOM   14639 O  OD2   . ASP   B  1  764  ? 34.520  30.896  67.158  1.00 29.46 ? 762  ASP   B OD2   1 
ATOM   14640 N  N     . GLY   B  1  765  ? 31.205  33.627  67.995  1.00 17.70 ? 763  GLY   B N     1 
ATOM   14641 C  CA    . GLY   B  1  765  ? 30.961  35.043  67.847  1.00 17.30 ? 763  GLY   B CA    1 
ATOM   14642 C  C     . GLY   B  1  765  ? 31.428  35.616  66.530  1.00 17.35 ? 763  GLY   B C     1 
ATOM   14643 O  O     . GLY   B  1  765  ? 30.915  36.652  66.106  1.00 17.26 ? 763  GLY   B O     1 
ATOM   14644 N  N     . ARG   B  1  766  ? 32.405  34.977  65.881  1.00 17.56 ? 764  ARG   B N     1 
ATOM   14645 C  CA    . ARG   B  1  766  ? 32.849  35.444  64.571  1.00 17.42 ? 764  ARG   B CA    1 
ATOM   14646 C  C     . ARG   B  1  766  ? 31.742  35.319  63.542  1.00 16.04 ? 764  ARG   B C     1 
ATOM   14647 O  O     . ARG   B  1  766  ? 31.636  36.152  62.635  1.00 17.25 ? 764  ARG   B O     1 
ATOM   14648 C  CB    . ARG   B  1  766  ? 34.062  34.638  64.102  1.00 16.76 ? 764  ARG   B CB    1 
ATOM   14649 C  CG    . ARG   B  1  766  ? 35.286  34.759  64.996  1.00 21.96 ? 764  ARG   B CG    1 
ATOM   14650 C  CD    . ARG   B  1  766  ? 36.329  33.702  64.624  1.00 28.65 ? 764  ARG   B CD    1 
ATOM   14651 N  NE    . ARG   B  1  766  ? 35.804  32.351  64.790  1.00 34.10 ? 764  ARG   B NE    1 
ATOM   14652 C  CZ    . ARG   B  1  766  ? 36.446  31.244  64.439  1.00 40.05 ? 764  ARG   B CZ    1 
ATOM   14653 N  NH1   . ARG   B  1  766  ? 37.649  31.287  63.889  1.00 39.57 ? 764  ARG   B NH1   1 
ATOM   14654 N  NH2   . ARG   B  1  766  ? 35.863  30.064  64.639  1.00 40.08 ? 764  ARG   B NH2   1 
ATOM   14655 N  N     . VAL   B  1  767  ? 30.908  34.289  63.671  1.00 15.51 ? 765  VAL   B N     1 
ATOM   14656 C  CA    . VAL   B  1  767  ? 29.783  34.147  62.763  1.00 16.02 ? 765  VAL   B CA    1 
ATOM   14657 C  C     . VAL   B  1  767  ? 28.764  35.234  63.046  1.00 14.85 ? 765  VAL   B C     1 
ATOM   14658 O  O     . VAL   B  1  767  ? 28.244  35.874  62.121  1.00 15.84 ? 765  VAL   B O     1 
ATOM   14659 C  CB    . VAL   B  1  767  ? 29.188  32.734  62.872  1.00 15.04 ? 765  VAL   B CB    1 
ATOM   14660 C  CG1   . VAL   B  1  767  ? 27.986  32.595  61.953  1.00 15.24 ? 765  VAL   B CG1   1 
ATOM   14661 C  CG2   . VAL   B  1  767  ? 30.236  31.709  62.528  1.00 16.88 ? 765  VAL   B CG2   1 
ATOM   14662 N  N     . GLY   B  1  768  ? 28.497  35.494  64.328  1.00 14.40 ? 766  GLY   B N     1 
ATOM   14663 C  CA    . GLY   B  1  768  ? 27.603  36.586  64.657  1.00 15.21 ? 766  GLY   B CA    1 
ATOM   14664 C  C     . GLY   B  1  768  ? 28.118  37.911  64.130  1.00 15.00 ? 766  GLY   B C     1 
ATOM   14665 O  O     . GLY   B  1  768  ? 27.368  38.696  63.549  1.00 15.38 ? 766  GLY   B O     1 
ATOM   14666 N  N     . ALA   B  1  769  ? 29.415  38.159  64.291  1.00 15.97 ? 767  ALA   B N     1 
ATOM   14667 C  CA    . ALA   B  1  769  ? 29.967  39.432  63.838  1.00 16.11 ? 767  ALA   B CA    1 
ATOM   14668 C  C     . ALA   B  1  769  ? 29.887  39.563  62.321  1.00 15.31 ? 767  ALA   B C     1 
ATOM   14669 O  O     . ALA   B  1  769  ? 29.581  40.643  61.802  1.00 16.87 ? 767  ALA   B O     1 
ATOM   14670 C  CB    . ALA   B  1  769  ? 31.404  39.579  64.334  1.00 16.88 ? 767  ALA   B CB    1 
ATOM   14671 N  N     . ALA   B  1  770  ? 30.147  38.471  61.598  1.00 15.84 ? 768  ALA   B N     1 
ATOM   14672 C  CA    . ALA   B  1  770  ? 30.069  38.526  60.146  1.00 15.76 ? 768  ALA   B CA    1 
ATOM   14673 C  C     . ALA   B  1  770  ? 28.650  38.820  59.682  1.00 15.98 ? 768  ALA   B C     1 
ATOM   14674 O  O     . ALA   B  1  770  ? 28.445  39.537  58.694  1.00 18.51 ? 768  ALA   B O     1 
ATOM   14675 C  CB    . ALA   B  1  770  ? 30.557  37.215  59.545  1.00 17.16 ? 768  ALA   B CB    1 
ATOM   14676 N  N     . LEU   B  1  771  ? 27.657  38.274  60.381  1.00 15.10 ? 769  LEU   B N     1 
ATOM   14677 C  CA    . LEU   B  1  771  ? 26.268  38.558  60.037  1.00 14.85 ? 769  LEU   B CA    1 
ATOM   14678 C  C     . LEU   B  1  771  ? 25.930  40.012  60.316  1.00 14.99 ? 769  LEU   B C     1 
ATOM   14679 O  O     . LEU   B  1  771  ? 25.305  40.685  59.490  1.00 17.18 ? 769  LEU   B O     1 
ATOM   14680 C  CB    . LEU   B  1  771  ? 25.337  37.646  60.833  1.00 14.86 ? 769  LEU   B CB    1 
ATOM   14681 C  CG    . LEU   B  1  771  ? 25.381  36.184  60.410  1.00 14.54 ? 769  LEU   B CG    1 
ATOM   14682 C  CD1   . LEU   B  1  771  ? 24.616  35.335  61.413  1.00 17.05 ? 769  LEU   B CD1   1 
ATOM   14683 C  CD2   . LEU   B  1  771  ? 24.830  36.005  58.995  1.00 15.65 ? 769  LEU   B CD2   1 
ATOM   14684 N  N     . VAL   B  1  772  ? 26.334  40.511  61.485  1.00 15.09 ? 770  VAL   B N     1 
ATOM   14685 C  CA    . VAL   B  1  772  ? 26.044  41.893  61.867  1.00 14.63 ? 770  VAL   B CA    1 
ATOM   14686 C  C     . VAL   B  1  772  ? 26.638  42.870  60.866  1.00 18.85 ? 770  VAL   B C     1 
ATOM   14687 O  O     . VAL   B  1  772  ? 26.021  43.890  60.529  1.00 19.39 ? 770  VAL   B O     1 
ATOM   14688 C  CB    . VAL   B  1  772  ? 26.566  42.152  63.290  1.00 15.64 ? 770  VAL   B CB    1 
ATOM   14689 C  CG1   . VAL   B  1  772  ? 26.579  43.639  63.608  1.00 17.03 ? 770  VAL   B CG1   1 
ATOM   14690 C  CG2   . VAL   B  1  772  ? 25.715  41.393  64.295  1.00 16.22 ? 770  VAL   B CG2   1 
ATOM   14691 N  N     . ALA   B  1  773  ? 27.853  42.582  60.385  1.00 17.06 ? 771  ALA   B N     1 
ATOM   14692 C  CA    . ALA   B  1  773  ? 28.552  43.505  59.504  1.00 18.23 ? 771  ALA   B CA    1 
ATOM   14693 C  C     . ALA   B  1  773  ? 28.069  43.436  58.066  1.00 22.09 ? 771  ALA   B C     1 
ATOM   14694 O  O     . ALA   B  1  773  ? 28.437  44.305  57.268  1.00 22.37 ? 771  ALA   B O     1 
ATOM   14695 C  CB    . ALA   B  1  773  ? 30.055  43.224  59.547  1.00 20.63 ? 771  ALA   B CB    1 
ATOM   14696 N  N     . ALA   B  1  774  ? 27.268  42.434  57.717  1.00 18.16 ? 772  ALA   B N     1 
ATOM   14697 C  CA    . ALA   B  1  774  ? 26.894  42.222  56.324  1.00 18.39 ? 772  ALA   B CA    1 
ATOM   14698 C  C     . ALA   B  1  774  ? 26.080  43.397  55.799  1.00 20.18 ? 772  ALA   B C     1 
ATOM   14699 O  O     . ALA   B  1  774  ? 25.275  43.998  56.512  1.00 20.11 ? 772  ALA   B O     1 
ATOM   14700 C  CB    . ALA   B  1  774  ? 26.099  40.928  56.176  1.00 20.53 ? 772  ALA   B CB    1 
ATOM   14701 N  N     . ALA   B  1  775  ? 26.290  43.709  54.516  1.00 23.04 ? 773  ALA   B N     1 
ATOM   14702 C  CA    . ALA   B  1  775  ? 25.759  44.944  53.948  1.00 23.79 ? 773  ALA   B CA    1 
ATOM   14703 C  C     . ALA   B  1  775  ? 24.240  45.020  54.062  1.00 20.23 ? 773  ALA   B C     1 
ATOM   14704 O  O     . ALA   B  1  775  ? 23.679  46.094  54.301  1.00 23.13 ? 773  ALA   B O     1 
ATOM   14705 C  CB    . ALA   B  1  775  ? 26.186  45.054  52.486  1.00 27.20 ? 773  ALA   B CB    1 
ATOM   14706 N  N     . GLU   B  1  776  ? 23.559  43.899  53.888  1.00 19.93 ? 774  GLU   B N     1 
ATOM   14707 C  CA    . GLU   B  1  776  ? 22.108  43.906  53.807  1.00 18.04 ? 774  GLU   B CA    1 
ATOM   14708 C  C     . GLU   B  1  776  ? 21.421  43.705  55.151  1.00 17.00 ? 774  GLU   B C     1 
ATOM   14709 O  O     . GLU   B  1  776  ? 20.195  43.696  55.204  1.00 16.84 ? 774  GLU   B O     1 
ATOM   14710 C  CB    . GLU   B  1  776  ? 21.628  42.845  52.818  1.00 19.12 ? 774  GLU   B CB    1 
ATOM   14711 C  CG    . GLU   B  1  776  ? 22.205  42.998  51.409  1.00 23.61 ? 774  GLU   B CG    1 
ATOM   14712 C  CD    . GLU   B  1  776  ? 23.536  42.260  51.216  1.00 30.00 ? 774  GLU   B CD    1 
ATOM   14713 O  OE1   . GLU   B  1  776  ? 24.078  41.668  52.185  1.00 25.57 ? 774  GLU   B OE1   1 
ATOM   14714 O  OE2   . GLU   B  1  776  ? 24.057  42.278  50.081  1.00 34.35 ? 774  GLU   B OE2   1 
ATOM   14715 N  N     . THR   B  1  777  ? 22.167  43.532  56.230  1.00 16.03 ? 775  THR   B N     1 
ATOM   14716 C  CA    . THR   B  1  777  ? 21.545  43.382  57.534  1.00 15.99 ? 775  THR   B CA    1 
ATOM   14717 C  C     . THR   B  1  777  ? 20.816  44.663  57.898  1.00 15.84 ? 775  THR   B C     1 
ATOM   14718 O  O     . THR   B  1  777  ? 21.391  45.754  57.854  1.00 16.74 ? 775  THR   B O     1 
ATOM   14719 C  CB    . THR   B  1  777  ? 22.628  43.065  58.549  1.00 16.38 ? 775  THR   B CB    1 
ATOM   14720 O  OG1   . THR   B  1  777  ? 23.131  41.762  58.250  1.00 18.97 ? 775  THR   B OG1   1 
ATOM   14721 C  CG2   . THR   B  1  777  ? 22.075  43.086  59.950  1.00 16.18 ? 775  THR   B CG2   1 
ATOM   14722 N  N     . ALA   B  1  778  ? 19.527  44.532  58.212  1.00 13.11 ? 776  ALA   B N     1 
ATOM   14723 C  CA    . ALA   B  1  778  ? 18.652  45.670  58.426  1.00 14.23 ? 776  ALA   B CA    1 
ATOM   14724 C  C     . ALA   B  1  778  ? 18.265  45.840  59.880  1.00 14.67 ? 776  ALA   B C     1 
ATOM   14725 O  O     . ALA   B  1  778  ? 17.607  46.826  60.225  1.00 16.00 ? 776  ALA   B O     1 
ATOM   14726 C  CB    . ALA   B  1  778  ? 17.377  45.522  57.583  1.00 14.26 ? 776  ALA   B CB    1 
ATOM   14727 N  N     . GLY   B  1  779  ? 18.638  44.902  60.734  1.00 13.66 ? 777  GLY   B N     1 
ATOM   14728 C  CA    . GLY   B  1  779  ? 18.316  44.992  62.137  1.00 14.94 ? 777  GLY   B CA    1 
ATOM   14729 C  C     . GLY   B  1  779  ? 18.980  43.841  62.840  1.00 12.63 ? 777  GLY   B C     1 
ATOM   14730 O  O     . GLY   B  1  779  ? 19.281  42.815  62.221  1.00 13.87 ? 777  GLY   B O     1 
ATOM   14731 N  N     . VAL   B  1  780  ? 19.254  44.012  64.127  1.00 13.21 ? 778  VAL   B N     1 
ATOM   14732 C  CA    . VAL   B  1  780  ? 19.896  42.972  64.908  1.00 12.55 ? 778  VAL   B CA    1 
ATOM   14733 C  C     . VAL   B  1  780  ? 19.129  42.807  66.205  1.00 13.41 ? 778  VAL   B C     1 
ATOM   14734 O  O     . VAL   B  1  780  ? 18.803  43.795  66.875  1.00 13.64 ? 778  VAL   B O     1 
ATOM   14735 C  CB    . VAL   B  1  780  ? 21.375  43.292  65.199  1.00 13.84 ? 778  VAL   B CB    1 
ATOM   14736 C  CG1   . VAL   B  1  780  ? 21.978  42.203  66.073  1.00 14.93 ? 778  VAL   B CG1   1 
ATOM   14737 C  CG2   . VAL   B  1  780  ? 22.151  43.441  63.911  1.00 14.82 ? 778  VAL   B CG2   1 
ATOM   14738 N  N     . MET   B  1  781  ? 18.830  41.567  66.545  1.00 12.26 ? 779  MET   B N     1 
ATOM   14739 C  CA    . MET   B  1  781  ? 18.244  41.226  67.830  1.00 12.85 ? 779  MET   B CA    1 
ATOM   14740 C  C     . MET   B  1  781  ? 19.277  40.402  68.559  1.00 13.02 ? 779  MET   B C     1 
ATOM   14741 O  O     . MET   B  1  781  ? 19.654  39.319  68.105  1.00 13.55 ? 779  MET   B O     1 
ATOM   14742 C  CB    . MET   B  1  781  ? 16.953  40.443  67.642  1.00 12.82 ? 779  MET   B CB    1 
ATOM   14743 C  CG    . MET   B  1  781  ? 15.973  41.191  66.777  1.00 13.91 ? 779  MET   B CG    1 
ATOM   14744 S  SD    . MET   B  1  781  ? 14.514  40.236  66.412  1.00 13.37 ? 779  MET   B SD    1 
ATOM   14745 C  CE    . MET   B  1  781  ? 13.669  40.317  67.978  1.00 13.61 ? 779  MET   B CE    1 
ATOM   14746 N  N     . PHE   B  1  782  ? 19.781  40.948  69.649  1.00 12.42 ? 780  PHE   B N     1 
ATOM   14747 C  CA    . PHE   B  1  782  ? 20.846  40.326  70.402  1.00 12.71 ? 780  PHE   B CA    1 
ATOM   14748 C  C     . PHE   B  1  782  ? 20.388  40.115  71.831  1.00 11.12 ? 780  PHE   B C     1 
ATOM   14749 O  O     . PHE   B  1  782  ? 19.838  41.025  72.453  1.00 13.14 ? 780  PHE   B O     1 
ATOM   14750 C  CB    . PHE   B  1  782  ? 22.077  41.219  70.433  1.00 13.33 ? 780  PHE   B CB    1 
ATOM   14751 C  CG    . PHE   B  1  782  ? 23.145  40.701  71.319  1.00 12.13 ? 780  PHE   B CG    1 
ATOM   14752 C  CD1   . PHE   B  1  782  ? 23.948  39.656  70.890  1.00 13.53 ? 780  PHE   B CD1   1 
ATOM   14753 C  CD2   . PHE   B  1  782  ? 23.334  41.224  72.596  1.00 13.50 ? 780  PHE   B CD2   1 
ATOM   14754 C  CE1   . PHE   B  1  782  ? 24.920  39.143  71.688  1.00 14.91 ? 780  PHE   B CE1   1 
ATOM   14755 C  CE2   . PHE   B  1  782  ? 24.332  40.713  73.409  1.00 14.38 ? 780  PHE   B CE2   1 
ATOM   14756 C  CZ    . PHE   B  1  782  ? 25.130  39.679  72.946  1.00 13.26 ? 780  PHE   B CZ    1 
ATOM   14757 N  N     . THR   B  1  783  ? 20.623  38.922  72.343  1.00 11.53 ? 781  THR   B N     1 
ATOM   14758 C  CA    . THR   B  1  783  ? 20.510  38.663  73.764  1.00 13.56 ? 781  THR   B CA    1 
ATOM   14759 C  C     . THR   B  1  783  ? 21.785  37.957  74.179  1.00 13.99 ? 781  THR   B C     1 
ATOM   14760 O  O     . THR   B  1  783  ? 22.198  36.988  73.535  1.00 13.82 ? 781  THR   B O     1 
ATOM   14761 C  CB    . THR   B  1  783  ? 19.272  37.820  74.078  1.00 13.20 ? 781  THR   B CB    1 
ATOM   14762 O  OG1   . THR   B  1  783  ? 18.114  38.506  73.612  1.00 13.84 ? 781  THR   B OG1   1 
ATOM   14763 C  CG2   . THR   B  1  783  ? 19.155  37.640  75.572  1.00 14.52 ? 781  THR   B CG2   1 
ATOM   14764 N  N     . GLY   B  1  784  ? 22.418  38.452  75.233  1.00 13.29 ? 782  GLY   B N     1 
ATOM   14765 C  CA    . GLY   B  1  784  ? 23.724  37.959  75.600  1.00 13.33 ? 782  GLY   B CA    1 
ATOM   14766 C  C     . GLY   B  1  784  ? 24.382  38.937  76.541  1.00 14.79 ? 782  GLY   B C     1 
ATOM   14767 O  O     . GLY   B  1  784  ? 23.722  39.773  77.139  1.00 14.90 ? 782  GLY   B O     1 
ATOM   14768 N  N     . SER   B  1  785  ? 25.694  38.838  76.614  1.00 15.34 ? 783  SER   B N     1 
ATOM   14769 C  CA    . SER   B  1  785  ? 26.413  39.676  77.559  1.00 16.82 ? 783  SER   B CA    1 
ATOM   14770 C  C     . SER   B  1  785  ? 26.459  41.123  77.080  1.00 17.56 ? 783  SER   B C     1 
ATOM   14771 O  O     . SER   B  1  785  ? 26.469  41.415  75.880  1.00 16.09 ? 783  SER   B O     1 
ATOM   14772 C  CB    . SER   B  1  785  ? 27.829  39.144  77.764  1.00 17.78 ? 783  SER   B CB    1 
ATOM   14773 O  OG    . SER   B  1  785  ? 28.569  39.220  76.571  1.00 17.64 ? 783  SER   B OG    1 
ATOM   14774 N  N     . THR   B  1  786  ? 26.503  42.046  78.048  1.00 17.18 ? 784  THR   B N     1 
ATOM   14775 C  CA    . THR   B  1  786  ? 26.631  43.457  77.712  1.00 17.54 ? 784  THR   B CA    1 
ATOM   14776 C  C     . THR   B  1  786  ? 27.896  43.719  76.907  1.00 17.06 ? 784  THR   B C     1 
ATOM   14777 O  O     . THR   B  1  786  ? 27.893  44.528  75.972  1.00 19.12 ? 784  THR   B O     1 
ATOM   14778 C  CB    . THR   B  1  786  ? 26.596  44.294  78.997  1.00 18.38 ? 784  THR   B CB    1 
ATOM   14779 O  OG1   . THR   B  1  786  ? 25.447  43.923  79.770  1.00 20.48 ? 784  THR   B OG1   1 
ATOM   14780 C  CG2   . THR   B  1  786  ? 26.496  45.761  78.658  1.00 23.72 ? 784  THR   B CG2   1 
ATOM   14781 N  N     . GLU   B  1  787  ? 28.985  43.019  77.234  1.00 20.03 ? 785  GLU   B N     1 
ATOM   14782 C  CA    . GLU   B  1  787  ? 30.248  43.228  76.533  1.00 19.08 ? 785  GLU   B CA    1 
ATOM   14783 C  C     . GLU   B  1  787  ? 30.112  42.936  75.044  1.00 18.37 ? 785  GLU   B C     1 
ATOM   14784 O  O     . GLU   B  1  787  ? 30.608  43.693  74.199  1.00 19.02 ? 785  GLU   B O     1 
ATOM   14785 C  CB    . GLU   B  1  787  ? 31.351  42.356  77.153  1.00 23.40 ? 785  GLU   B CB    1 
ATOM   14786 N  N     . VAL   B  1  788  ? 29.446  41.830  74.703  1.00 16.67 ? 786  VAL   B N     1 
ATOM   14787 C  CA    . VAL   B  1  788  ? 29.280  41.478  73.300  1.00 17.32 ? 786  VAL   B CA    1 
ATOM   14788 C  C     . VAL   B  1  788  ? 28.327  42.450  72.622  1.00 14.93 ? 786  VAL   B C     1 
ATOM   14789 O  O     . VAL   B  1  788  ? 28.535  42.851  71.475  1.00 16.34 ? 786  VAL   B O     1 
ATOM   14790 C  CB    . VAL   B  1  788  ? 28.806  40.021  73.186  1.00 18.10 ? 786  VAL   B CB    1 
ATOM   14791 C  CG1   . VAL   B  1  788  ? 28.376  39.718  71.764  1.00 16.53 ? 786  VAL   B CG1   1 
ATOM   14792 C  CG2   . VAL   B  1  788  ? 29.939  39.082  73.603  1.00 18.41 ? 786  VAL   B CG2   1 
ATOM   14793 N  N     . ALA   B  1  789  ? 27.267  42.849  73.327  1.00 15.22 ? 787  ALA   B N     1 
ATOM   14794 C  CA    . ALA   B  1  789  ? 26.323  43.805  72.766  1.00 14.63 ? 787  ALA   B CA    1 
ATOM   14795 C  C     . ALA   B  1  789  ? 27.029  45.085  72.344  1.00 14.52 ? 787  ALA   B C     1 
ATOM   14796 O  O     . ALA   B  1  789  ? 26.700  45.668  71.308  1.00 15.98 ? 787  ALA   B O     1 
ATOM   14797 C  CB    . ALA   B  1  789  ? 25.227  44.115  73.782  1.00 13.36 ? 787  ALA   B CB    1 
ATOM   14798 N  N     . ARG   B  1  790  ? 28.008  45.539  73.138  1.00 15.99 ? 788  ARG   B N     1 
ATOM   14799 C  CA    . ARG   B  1  790  ? 28.713  46.769  72.780  1.00 16.15 ? 788  ARG   B CA    1 
ATOM   14800 C  C     . ARG   B  1  790  ? 29.484  46.609  71.481  1.00 18.12 ? 788  ARG   B C     1 
ATOM   14801 O  O     . ARG   B  1  790  ? 29.587  47.554  70.690  1.00 19.25 ? 788  ARG   B O     1 
ATOM   14802 C  CB    . ARG   B  1  790  ? 29.712  47.144  73.864  1.00 21.55 ? 788  ARG   B CB    1 
ATOM   14803 C  CG    . ARG   B  1  790  ? 29.120  47.667  75.099  1.00 24.19 ? 788  ARG   B CG    1 
ATOM   14804 C  CD    . ARG   B  1  790  ? 30.234  48.253  75.949  1.00 28.18 ? 788  ARG   B CD    1 
ATOM   14805 N  NE    . ARG   B  1  790  ? 29.757  48.420  77.308  1.00 36.28 ? 788  ARG   B NE    1 
ATOM   14806 C  CZ    . ARG   B  1  790  ? 28.987  49.423  77.699  1.00 35.42 ? 788  ARG   B CZ    1 
ATOM   14807 N  NH1   . ARG   B  1  790  ? 28.644  50.396  76.864  1.00 31.20 ? 788  ARG   B NH1   1 
ATOM   14808 N  NH2   . ARG   B  1  790  ? 28.551  49.449  78.954  1.00 39.71 ? 788  ARG   B NH2   1 
ATOM   14809 N  N     . LEU   B  1  791  ? 30.046  45.425  71.245  1.00 17.88 ? 789  LEU   B N     1 
ATOM   14810 C  CA    . LEU   B  1  791  ? 30.773  45.207  69.999  1.00 18.08 ? 789  LEU   B CA    1 
ATOM   14811 C  C     . LEU   B  1  791  ? 29.832  45.264  68.809  1.00 18.28 ? 789  LEU   B C     1 
ATOM   14812 O  O     . LEU   B  1  791  ? 30.152  45.860  67.775  1.00 18.95 ? 789  LEU   B O     1 
ATOM   14813 C  CB    . LEU   B  1  791  ? 31.469  43.853  70.043  1.00 17.78 ? 789  LEU   B CB    1 
ATOM   14814 C  CG    . LEU   B  1  791  ? 32.483  43.677  71.169  1.00 22.70 ? 789  LEU   B CG    1 
ATOM   14815 C  CD1   . LEU   B  1  791  ? 33.073  42.274  71.117  1.00 21.28 ? 789  LEU   B CD1   1 
ATOM   14816 C  CD2   . LEU   B  1  791  ? 33.574  44.754  71.085  1.00 23.98 ? 789  LEU   B CD2   1 
ATOM   14817 N  N     . ILE   B  1  792  ? 28.649  44.661  68.953  1.00 17.41 ? 790  ILE   B N     1 
ATOM   14818 C  CA    . ILE   B  1  792  ? 27.653  44.694  67.889  1.00 17.48 ? 790  ILE   B CA    1 
ATOM   14819 C  C     . ILE   B  1  792  ? 27.195  46.118  67.644  1.00 16.35 ? 790  ILE   B C     1 
ATOM   14820 O  O     . ILE   B  1  792  ? 27.062  46.561  66.495  1.00 17.56 ? 790  ILE   B O     1 
ATOM   14821 C  CB    . ILE   B  1  792  ? 26.481  43.787  68.288  1.00 14.74 ? 790  ILE   B CB    1 
ATOM   14822 C  CG1   . ILE   B  1  792  ? 26.963  42.341  68.288  1.00 15.75 ? 790  ILE   B CG1   1 
ATOM   14823 C  CG2   . ILE   B  1  792  ? 25.286  44.024  67.381  1.00 16.21 ? 790  ILE   B CG2   1 
ATOM   14824 C  CD1   . ILE   B  1  792  ? 25.980  41.365  68.855  1.00 16.19 ? 790  ILE   B CD1   1 
ATOM   14825 N  N     . GLN   B  1  793  ? 26.931  46.847  68.726  1.00 16.01 ? 791  GLN   B N     1 
ATOM   14826 C  CA    . GLN   B  1  793  ? 26.507  48.231  68.616  1.00 16.60 ? 791  GLN   B CA    1 
ATOM   14827 C  C     . GLN   B  1  793  ? 27.530  49.053  67.851  1.00 17.44 ? 791  GLN   B C     1 
ATOM   14828 O  O     . GLN   B  1  793  ? 27.168  49.861  66.983  1.00 18.08 ? 791  GLN   B O     1 
ATOM   14829 C  CB    . GLN   B  1  793  ? 26.312  48.786  70.020  1.00 17.81 ? 791  GLN   B CB    1 
ATOM   14830 C  CG    . GLN   B  1  793  ? 25.907  50.225  70.069  1.00 19.37 ? 791  GLN   B CG    1 
ATOM   14831 C  CD    . GLN   B  1  793  ? 26.219  50.832  71.407  1.00 22.44 ? 791  GLN   B CD    1 
ATOM   14832 O  OE1   . GLN   B  1  793  ? 27.252  50.530  72.013  1.00 23.31 ? 791  GLN   B OE1   1 
ATOM   14833 N  NE2   . GLN   B  1  793  ? 25.331  51.683  71.886  1.00 24.91 ? 791  GLN   B NE2   1 
ATOM   14834 N  N     . ALA   B  1  794  ? 28.815  48.834  68.136  1.00 18.64 ? 792  ALA   B N     1 
ATOM   14835 C  CA    . ALA   B  1  794  ? 29.859  49.562  67.426  1.00 20.23 ? 792  ALA   B CA    1 
ATOM   14836 C  C     . ALA   B  1  794  ? 29.874  49.206  65.944  1.00 19.79 ? 792  ALA   B C     1 
ATOM   14837 O  O     . ALA   B  1  794  ? 30.009  50.096  65.091  1.00 21.64 ? 792  ALA   B O     1 
ATOM   14838 C  CB    . ALA   B  1  794  ? 31.222  49.312  68.076  1.00 22.49 ? 792  ALA   B CB    1 
ATOM   14839 N  N     . GLN   B  1  795  ? 29.745  47.912  65.615  1.00 18.74 ? 793  GLN   B N     1 
ATOM   14840 C  CA    . GLN   B  1  795  ? 29.673  47.506  64.211  1.00 19.65 ? 793  GLN   B CA    1 
ATOM   14841 C  C     . GLN   B  1  795  ? 28.535  48.226  63.500  1.00 18.95 ? 793  GLN   B C     1 
ATOM   14842 O  O     . GLN   B  1  795  ? 28.693  48.725  62.378  1.00 20.20 ? 793  GLN   B O     1 
ATOM   14843 C  CB    . GLN   B  1  795  ? 29.426  45.997  64.095  1.00 23.51 ? 793  GLN   B CB    1 
ATOM   14844 C  CG    . GLN   B  1  795  ? 30.560  45.044  64.406  1.00 26.95 ? 793  GLN   B CG    1 
ATOM   14845 C  CD    . GLN   B  1  795  ? 30.151  43.581  64.185  1.00 29.33 ? 793  GLN   B CD    1 
ATOM   14846 O  OE1   . GLN   B  1  795  ? 29.514  42.967  65.040  1.00 28.82 ? 793  GLN   B OE1   1 
ATOM   14847 N  NE2   . GLN   B  1  795  ? 30.513  43.027  63.041  1.00 25.12 ? 793  GLN   B NE2   1 
ATOM   14848 N  N     . LEU   B  1  796  ? 27.364  48.264  64.134  1.00 17.68 ? 794  LEU   B N     1 
ATOM   14849 C  CA    . LEU   B  1  796  ? 26.186  48.781  63.456  1.00 17.42 ? 794  LEU   B CA    1 
ATOM   14850 C  C     . LEU   B  1  796  ? 26.261  50.281  63.262  1.00 19.82 ? 794  LEU   B C     1 
ATOM   14851 O  O     . LEU   B  1  796  ? 25.738  50.797  62.270  1.00 21.34 ? 794  LEU   B O     1 
ATOM   14852 C  CB    . LEU   B  1  796  ? 24.937  48.441  64.256  1.00 16.39 ? 794  LEU   B CB    1 
ATOM   14853 C  CG    . LEU   B  1  796  ? 24.525  46.974  64.231  1.00 17.48 ? 794  LEU   B CG    1 
ATOM   14854 C  CD1   . LEU   B  1  796  ? 23.277  46.803  65.073  1.00 17.41 ? 794  LEU   B CD1   1 
ATOM   14855 C  CD2   . LEU   B  1  796  ? 24.249  46.541  62.809  1.00 17.01 ? 794  LEU   B CD2   1 
ATOM   14856 N  N     . ALA   B  1  797  ? 26.901  50.988  64.191  1.00 19.99 ? 795  ALA   B N     1 
ATOM   14857 C  CA    . ALA   B  1  797  ? 26.967  52.438  64.108  1.00 22.33 ? 795  ALA   B CA    1 
ATOM   14858 C  C     . ALA   B  1  797  ? 27.805  52.896  62.930  1.00 25.00 ? 795  ALA   B C     1 
ATOM   14859 O  O     . ALA   B  1  797  ? 27.713  54.059  62.534  1.00 26.78 ? 795  ALA   B O     1 
ATOM   14860 C  CB    . ALA   B  1  797  ? 27.538  53.009  65.403  1.00 23.47 ? 795  ALA   B CB    1 
ATOM   14861 N  N     . ASP   B  1  798  ? 28.600  52.002  62.346  1.00 23.91 ? 796  ASP   B N     1 
ATOM   14862 C  CA    . ASP   B  1  798  ? 29.316  52.356  61.129  1.00 27.55 ? 796  ASP   B CA    1 
ATOM   14863 C  C     . ASP   B  1  798  ? 28.399  52.393  59.918  1.00 27.32 ? 796  ASP   B C     1 
ATOM   14864 O  O     . ASP   B  1  798  ? 28.776  52.962  58.890  1.00 30.44 ? 796  ASP   B O     1 
ATOM   14865 C  CB    . ASP   B  1  798  ? 30.451  51.364  60.883  1.00 26.06 ? 796  ASP   B CB    1 
ATOM   14866 N  N     . ARG   B  1  799  ? 27.205  51.820  60.022  1.00 22.53 ? 797  ARG   B N     1 
ATOM   14867 C  CA    . ARG   B  1  799  ? 26.333  51.602  58.883  1.00 28.40 ? 797  ARG   B CA    1 
ATOM   14868 C  C     . ARG   B  1  799  ? 25.063  52.428  59.018  1.00 25.05 ? 797  ARG   B C     1 
ATOM   14869 O  O     . ARG   B  1  799  ? 24.698  52.894  60.099  1.00 22.13 ? 797  ARG   B O     1 
ATOM   14870 C  CB    . ARG   B  1  799  ? 25.952  50.117  58.758  1.00 30.17 ? 797  ARG   B CB    1 
ATOM   14871 C  CG    . ARG   B  1  799  ? 27.139  49.155  58.628  1.00 36.39 ? 797  ARG   B CG    1 
ATOM   14872 C  CD    . ARG   B  1  799  ? 26.755  47.842  57.924  1.00 33.16 ? 797  ARG   B CD    1 
ATOM   14873 N  NE    . ARG   B  1  799  ? 26.013  46.913  58.773  1.00 32.06 ? 797  ARG   B NE    1 
ATOM   14874 C  CZ    . ARG   B  1  799  ? 24.723  46.630  58.633  1.00 35.34 ? 797  ARG   B CZ    1 
ATOM   14875 N  NH1   . ARG   B  1  799  ? 23.993  47.174  57.673  1.00 30.88 ? 797  ARG   B NH1   1 
ATOM   14876 N  NH2   . ARG   B  1  799  ? 24.151  45.773  59.476  1.00 29.92 ? 797  ARG   B NH2   1 
ATOM   14877 N  N     . LEU   B  1  800  ? 24.392  52.601  57.890  1.00 23.66 ? 798  LEU   B N     1 
ATOM   14878 C  CA    . LEU   B  1  800  ? 23.051  53.145  57.841  1.00 23.10 ? 798  LEU   B CA    1 
ATOM   14879 C  C     . LEU   B  1  800  ? 22.229  52.262  56.921  1.00 24.70 ? 798  LEU   B C     1 
ATOM   14880 O  O     . LEU   B  1  800  ? 22.773  51.571  56.054  1.00 25.47 ? 798  LEU   B O     1 
ATOM   14881 C  CB    . LEU   B  1  800  ? 23.034  54.562  57.271  1.00 24.98 ? 798  LEU   B CB    1 
ATOM   14882 C  CG    . LEU   B  1  800  ? 23.668  55.660  58.116  1.00 26.48 ? 798  LEU   B CG    1 
ATOM   14883 C  CD1   . LEU   B  1  800  ? 23.665  56.947  57.309  1.00 31.08 ? 798  LEU   B CD1   1 
ATOM   14884 C  CD2   . LEU   B  1  800  ? 22.901  55.822  59.422  1.00 22.76 ? 798  LEU   B CD2   1 
ATOM   14885 N  N     . SER   B  1  801  ? 20.919  52.275  57.133  1.00 24.47 ? 799  SER   B N     1 
ATOM   14886 C  CA    . SER   B  1  801  ? 20.012  51.646  56.198  1.00 25.47 ? 799  SER   B CA    1 
ATOM   14887 C  C     . SER   B  1  801  ? 20.092  52.379  54.862  1.00 29.36 ? 799  SER   B C     1 
ATOM   14888 O  O     . SER   B  1  801  ? 20.628  53.486  54.784  1.00 29.52 ? 799  SER   B O     1 
ATOM   14889 C  CB    . SER   B  1  801  ? 18.592  51.774  56.722  1.00 26.85 ? 799  SER   B CB    1 
ATOM   14890 O  OG    . SER   B  1  801  ? 18.174  53.120  56.606  1.00 25.54 ? 799  SER   B OG    1 
ATOM   14891 N  N     . PRO   B  1  802  ? 19.580  51.772  53.788  1.00 31.59 ? 800  PRO   B N     1 
ATOM   14892 C  CA    . PRO   B  1  802  ? 19.500  52.505  52.513  1.00 33.33 ? 800  PRO   B CA    1 
ATOM   14893 C  C     . PRO   B  1  802  ? 18.698  53.790  52.611  1.00 32.24 ? 800  PRO   B C     1 
ATOM   14894 O  O     . PRO   B  1  802  ? 18.926  54.711  51.815  1.00 34.09 ? 800  PRO   B O     1 
ATOM   14895 C  CB    . PRO   B  1  802  ? 18.855  51.491  51.561  1.00 31.43 ? 800  PRO   B CB    1 
ATOM   14896 C  CG    . PRO   B  1  802  ? 19.252  50.157  52.133  1.00 32.14 ? 800  PRO   B CG    1 
ATOM   14897 C  CD    . PRO   B  1  802  ? 19.211  50.352  53.635  1.00 27.56 ? 800  PRO   B CD    1 
ATOM   14898 N  N     . ALA   B  1  803  ? 17.779  53.886  53.570  1.00 31.09 ? 801  ALA   B N     1 
ATOM   14899 C  CA    . ALA   B  1  803  ? 17.066  55.121  53.866  1.00 31.31 ? 801  ALA   B CA    1 
ATOM   14900 C  C     . ALA   B  1  803  ? 17.903  56.120  54.658  1.00 31.48 ? 801  ALA   B C     1 
ATOM   14901 O  O     . ALA   B  1  803  ? 17.416  57.216  54.949  1.00 36.11 ? 801  ALA   B O     1 
ATOM   14902 C  CB    . ALA   B  1  803  ? 15.777  54.807  54.628  1.00 33.29 ? 801  ALA   B CB    1 
ATOM   14903 N  N     . GLY   B  1  804  ? 19.139  55.776  55.014  1.00 27.39 ? 802  GLY   B N     1 
ATOM   14904 C  CA    . GLY   B  1  804  ? 19.987  56.692  55.750  1.00 28.12 ? 802  GLY   B CA    1 
ATOM   14905 C  C     . GLY   B  1  804  ? 19.700  56.792  57.231  1.00 26.95 ? 802  GLY   B C     1 
ATOM   14906 O  O     . GLY   B  1  804  ? 19.898  57.858  57.821  1.00 27.62 ? 802  GLY   B O     1 
ATOM   14907 N  N     . ARG   B  1  805  ? 19.251  55.714  57.857  1.00 26.90 ? 803  ARG   B N     1 
ATOM   14908 C  CA    . ARG   B  1  805  ? 18.855  55.733  59.255  1.00 22.90 ? 803  ARG   B CA    1 
ATOM   14909 C  C     . ARG   B  1  805  ? 19.564  54.623  60.013  1.00 21.51 ? 803  ARG   B C     1 
ATOM   14910 O  O     . ARG   B  1  805  ? 20.013  53.640  59.414  1.00 21.47 ? 803  ARG   B O     1 
ATOM   14911 C  CB    . ARG   B  1  805  ? 17.338  55.550  59.388  1.00 25.93 ? 803  ARG   B CB    1 
ATOM   14912 C  CG    . ARG   B  1  805  ? 16.539  56.659  58.737  1.00 30.33 ? 803  ARG   B CG    1 
ATOM   14913 C  CD    . ARG   B  1  805  ? 16.889  58.014  59.342  1.00 34.22 ? 803  ARG   B CD    1 
ATOM   14914 N  NE    . ARG   B  1  805  ? 16.162  59.092  58.679  1.00 37.70 ? 803  ARG   B NE    1 
ATOM   14915 C  CZ    . ARG   B  1  805  ? 16.678  59.885  57.751  1.00 31.10 ? 803  ARG   B CZ    1 
ATOM   14916 N  NH1   . ARG   B  1  805  ? 17.949  59.794  57.391  1.00 32.88 ? 803  ARG   B NH1   1 
ATOM   14917 N  NH2   . ARG   B  1  805  ? 15.897  60.791  57.165  1.00 38.82 ? 803  ARG   B NH2   1 
ATOM   14918 N  N     . PRO   B  1  806  ? 19.683  54.749  61.334  1.00 20.94 ? 804  PRO   B N     1 
ATOM   14919 C  CA    . PRO   B  1  806  ? 20.392  53.721  62.103  1.00 19.13 ? 804  PRO   B CA    1 
ATOM   14920 C  C     . PRO   B  1  806  ? 19.732  52.359  61.972  1.00 17.69 ? 804  PRO   B C     1 
ATOM   14921 O  O     . PRO   B  1  806  ? 18.504  52.233  61.914  1.00 19.12 ? 804  PRO   B O     1 
ATOM   14922 C  CB    . PRO   B  1  806  ? 20.318  54.239  63.543  1.00 20.61 ? 804  PRO   B CB    1 
ATOM   14923 C  CG    . PRO   B  1  806  ? 20.163  55.717  63.386  1.00 24.17 ? 804  PRO   B CG    1 
ATOM   14924 C  CD    . PRO   B  1  806  ? 19.292  55.888  62.183  1.00 23.32 ? 804  PRO   B CD    1 
ATOM   14925 N  N     . ILE   B  1  807  ? 20.577  51.334  61.936  1.00 17.19 ? 805  ILE   B N     1 
ATOM   14926 C  CA    . ILE   B  1  807  ? 20.116  49.950  61.965  1.00 16.90 ? 805  ILE   B CA    1 
ATOM   14927 C  C     . ILE   B  1  807  ? 19.631  49.650  63.379  1.00 17.05 ? 805  ILE   B C     1 
ATOM   14928 O  O     . ILE   B  1  807  ? 20.406  49.794  64.335  1.00 17.06 ? 805  ILE   B O     1 
ATOM   14929 C  CB    . ILE   B  1  807  ? 21.249  48.998  61.578  1.00 16.55 ? 805  ILE   B CB    1 
ATOM   14930 C  CG1   . ILE   B  1  807  ? 21.845  49.365  60.208  1.00 21.59 ? 805  ILE   B CG1   1 
ATOM   14931 C  CG2   . ILE   B  1  807  ? 20.758  47.558  61.642  1.00 17.57 ? 805  ILE   B CG2   1 
ATOM   14932 C  CD1   . ILE   B  1  807  ? 20.892  49.222  59.058  1.00 24.32 ? 805  ILE   B CD1   1 
ATOM   14933 N  N     . PRO   B  1  808  ? 18.376  49.244  63.561  1.00 14.94 ? 806  PRO   B N     1 
ATOM   14934 C  CA    . PRO   B  1  808  ? 17.870  48.974  64.914  1.00 15.66 ? 806  PRO   B CA    1 
ATOM   14935 C  C     . PRO   B  1  808  ? 18.588  47.803  65.557  1.00 16.19 ? 806  PRO   B C     1 
ATOM   14936 O  O     . PRO   B  1  808  ? 18.858  46.779  64.921  1.00 14.75 ? 806  PRO   B O     1 
ATOM   14937 C  CB    . PRO   B  1  808  ? 16.395  48.637  64.684  1.00 16.35 ? 806  PRO   B CB    1 
ATOM   14938 C  CG    . PRO   B  1  808  ? 16.055  49.307  63.379  1.00 20.31 ? 806  PRO   B CG    1 
ATOM   14939 C  CD    . PRO   B  1  808  ? 17.313  49.193  62.550  1.00 15.52 ? 806  PRO   B CD    1 
ATOM   14940 N  N     . LEU   B  1  809  ? 18.868  47.963  66.846  1.00 13.94 ? 807  LEU   B N     1 
ATOM   14941 C  CA    . LEU   B  1  809  ? 19.465  46.918  67.658  1.00 14.73 ? 807  LEU   B CA    1 
ATOM   14942 C  C     . LEU   B  1  809  ? 18.609  46.775  68.898  1.00 13.55 ? 807  LEU   B C     1 
ATOM   14943 O  O     . LEU   B  1  809  ? 18.385  47.754  69.613  1.00 14.90 ? 807  LEU   B O     1 
ATOM   14944 C  CB    . LEU   B  1  809  ? 20.882  47.309  68.063  1.00 14.68 ? 807  LEU   B CB    1 
ATOM   14945 C  CG    . LEU   B  1  809  ? 21.555  46.427  69.112  1.00 14.60 ? 807  LEU   B CG    1 
ATOM   14946 C  CD1   . LEU   B  1  809  ? 21.744  45.006  68.580  1.00 15.04 ? 807  LEU   B CD1   1 
ATOM   14947 C  CD2   . LEU   B  1  809  ? 22.893  47.045  69.497  1.00 17.62 ? 807  LEU   B CD2   1 
ATOM   14948 N  N     . ILE   B  1  810  ? 18.121  45.571  69.145  1.00 13.08 ? 808  ILE   B N     1 
ATOM   14949 C  CA    . ILE   B  1  810  ? 17.569  45.231  70.444  1.00 13.87 ? 808  ILE   B CA    1 
ATOM   14950 C  C     . ILE   B  1  810  ? 18.668  44.454  71.117  1.00 13.58 ? 808  ILE   B C     1 
ATOM   14951 O  O     . ILE   B  1  810  ? 19.120  43.440  70.583  1.00 14.76 ? 808  ILE   B O     1 
ATOM   14952 C  CB    . ILE   B  1  810  ? 16.301  44.376  70.338  1.00 13.28 ? 808  ILE   B CB    1 
ATOM   14953 C  CG1   . ILE   B  1  810  ? 15.270  45.053  69.456  1.00 14.00 ? 808  ILE   B CG1   1 
ATOM   14954 C  CG2   . ILE   B  1  810  ? 15.715  44.145  71.747  1.00 16.47 ? 808  ILE   B CG2   1 
ATOM   14955 C  CD1   . ILE   B  1  810  ? 13.935  44.308  69.432  1.00 14.72 ? 808  ILE   B CD1   1 
ATOM   14956 N  N     . ALA   B  1  811  ? 19.135  44.938  72.260  1.00 14.11 ? 809  ALA   B N     1 
ATOM   14957 C  CA    . ALA   B  1  811  ? 20.257  44.301  72.943  1.00 13.17 ? 809  ALA   B CA    1 
ATOM   14958 C  C     . ALA   B  1  811  ? 19.841  44.083  74.389  1.00 15.54 ? 809  ALA   B C     1 
ATOM   14959 O  O     . ALA   B  1  811  ? 19.800  45.033  75.180  1.00 14.94 ? 809  ALA   B O     1 
ATOM   14960 C  CB    . ALA   B  1  811  ? 21.532  45.124  72.838  1.00 15.63 ? 809  ALA   B CB    1 
ATOM   14961 N  N     . GLU   B  1  812  ? 19.524  42.844  74.713  1.00 13.10 ? 810  GLU   B N     1 
ATOM   14962 C  CA    . GLU   B  1  812  ? 19.016  42.463  76.025  1.00 13.87 ? 810  GLU   B CA    1 
ATOM   14963 C  C     . GLU   B  1  812  ? 20.141  41.712  76.708  1.00 14.67 ? 810  GLU   B C     1 
ATOM   14964 O  O     . GLU   B  1  812  ? 20.579  40.655  76.232  1.00 15.32 ? 810  GLU   B O     1 
ATOM   14965 C  CB    . GLU   B  1  812  ? 17.747  41.636  75.861  1.00 15.62 ? 810  GLU   B CB    1 
ATOM   14966 C  CG    . GLU   B  1  812  ? 16.675  42.446  75.123  1.00 15.27 ? 810  GLU   B CG    1 
ATOM   14967 C  CD    . GLU   B  1  812  ? 16.301  43.723  75.886  1.00 16.02 ? 810  GLU   B CD    1 
ATOM   14968 O  OE1   . GLU   B  1  812  ? 15.570  43.624  76.895  1.00 17.04 ? 810  GLU   B OE1   1 
ATOM   14969 O  OE2   . GLU   B  1  812  ? 16.736  44.823  75.481  1.00 17.44 ? 810  GLU   B OE2   1 
ATOM   14970 N  N     . THR   B  1  813  ? 20.653  42.303  77.786  1.00 14.15 ? 811  THR   B N     1 
ATOM   14971 C  CA    . THR   B  1  813  ? 21.974  41.962  78.277  1.00 13.64 ? 811  THR   B CA    1 
ATOM   14972 C  C     . THR   B  1  813  ? 21.932  41.500  79.730  1.00 14.03 ? 811  THR   B C     1 
ATOM   14973 O  O     . THR   B  1  813  ? 20.909  40.994  80.184  1.00 14.28 ? 811  THR   B O     1 
ATOM   14974 C  CB    . THR   B  1  813  ? 22.937  43.113  77.968  1.00 14.44 ? 811  THR   B CB    1 
ATOM   14975 O  OG1   . THR   B  1  813  ? 22.357  44.360  78.370  1.00 14.40 ? 811  THR   B OG1   1 
ATOM   14976 C  CG2   . THR   B  1  813  ? 23.168  43.168  76.455  1.00 17.46 ? 811  THR   B CG2   1 
ATOM   14977 N  N     . GLY   B  1  814  ? 23.029  41.633  80.456  1.00 15.04 ? 812  GLY   B N     1 
ATOM   14978 C  CA    . GLY   B  1  814  ? 23.161  40.938  81.720  1.00 15.90 ? 812  GLY   B CA    1 
ATOM   14979 C  C     . GLY   B  1  814  ? 22.418  41.596  82.864  1.00 15.19 ? 812  GLY   B C     1 
ATOM   14980 O  O     . GLY   B  1  814  ? 21.755  42.618  82.726  1.00 16.83 ? 812  GLY   B O     1 
ATOM   14981 N  N     . GLY   B  1  815  ? 22.543  40.976  84.033  1.00 15.44 ? 813  GLY   B N     1 
ATOM   14982 C  CA    . GLY   B  1  815  ? 21.938  41.507  85.236  1.00 14.49 ? 813  GLY   B CA    1 
ATOM   14983 C  C     . GLY   B  1  815  ? 22.880  41.323  86.407  1.00 14.62 ? 813  GLY   B C     1 
ATOM   14984 O  O     . GLY   B  1  815  ? 23.853  40.577  86.336  1.00 17.47 ? 813  GLY   B O     1 
ATOM   14985 N  N     . GLN   B  1  816  ? 22.613  42.074  87.461  1.00 13.82 ? 814  GLN   B N     1 
ATOM   14986 C  CA    . GLN   B  1  816  ? 23.279  41.915  88.751  1.00 14.56 ? 814  GLN   B CA    1 
ATOM   14987 C  C     . GLN   B  1  816  ? 22.164  41.957  89.788  1.00 12.65 ? 814  GLN   B C     1 
ATOM   14988 O  O     . GLN   B  1  816  ? 22.000  42.920  90.538  1.00 14.90 ? 814  GLN   B O     1 
ATOM   14989 C  CB    . GLN   B  1  816  ? 24.331  42.999  88.992  1.00 14.27 ? 814  GLN   B CB    1 
ATOM   14990 C  CG    . GLN   B  1  816  ? 25.231  42.696  90.164  1.00 15.03 ? 814  GLN   B CG    1 
ATOM   14991 C  CD    . GLN   B  1  816  ? 26.097  41.481  89.901  1.00 15.13 ? 814  GLN   B CD    1 
ATOM   14992 O  OE1   . GLN   B  1  816  ? 25.654  40.337  90.056  1.00 16.69 ? 814  GLN   B OE1   1 
ATOM   14993 N  NE2   . GLN   B  1  816  ? 27.349  41.719  89.499  1.00 16.16 ? 814  GLN   B NE2   1 
ATOM   14994 N  N     . ASN   B  1  817  ? 21.383  40.896  89.825  1.00 12.28 ? 815  ASN   B N     1 
ATOM   14995 C  CA    . ASN   B  1  817  ? 20.033  40.973  90.351  1.00 12.31 ? 815  ASN   B CA    1 
ATOM   14996 C  C     . ASN   B  1  817  ? 20.024  40.734  91.844  1.00 13.03 ? 815  ASN   B C     1 
ATOM   14997 O  O     . ASN   B  1  817  ? 20.642  39.779  92.334  1.00 14.03 ? 815  ASN   B O     1 
ATOM   14998 C  CB    . ASN   B  1  817  ? 19.167  39.929  89.676  1.00 13.78 ? 815  ASN   B CB    1 
ATOM   14999 C  CG    . ASN   B  1  817  ? 19.294  39.986  88.182  1.00 12.56 ? 815  ASN   B CG    1 
ATOM   15000 O  OD1   . ASN   B  1  817  ? 19.100  41.041  87.570  1.00 12.79 ? 815  ASN   B OD1   1 
ATOM   15001 N  ND2   . ASN   B  1  817  ? 19.671  38.875  87.594  1.00 12.66 ? 815  ASN   B ND2   1 
ATOM   15002 N  N     . ALA   B  1  818  ? 19.290  41.578  92.552  1.00 12.86 ? 816  ALA   B N     1 
ATOM   15003 C  CA    . ALA   B  1  818  ? 19.237  41.515  93.999  1.00 12.54 ? 816  ALA   B CA    1 
ATOM   15004 C  C     . ALA   B  1  818  ? 17.850  41.110  94.454  1.00 11.46 ? 816  ALA   B C     1 
ATOM   15005 O  O     . ALA   B  1  818  ? 16.857  41.253  93.738  1.00 12.83 ? 816  ALA   B O     1 
ATOM   15006 C  CB    . ALA   B  1  818  ? 19.557  42.882  94.608  1.00 13.62 ? 816  ALA   B CB    1 
ATOM   15007 N  N     . MET   B  1  819  ? 17.801  40.580  95.666  1.00 12.35 ? 817  MET   B N     1 
ATOM   15008 C  CA    . MET   B  1  819  ? 16.561  40.339  96.372  1.00 12.84 ? 817  MET   B CA    1 
ATOM   15009 C  C     . MET   B  1  819  ? 16.757  40.919  97.756  1.00 12.85 ? 817  MET   B C     1 
ATOM   15010 O  O     . MET   B  1  819  ? 17.752  40.607  98.423  1.00 13.96 ? 817  MET   B O     1 
ATOM   15011 C  CB    . MET   B  1  819  ? 16.252  38.858  96.504  1.00 13.21 ? 817  MET   B CB    1 
ATOM   15012 C  CG    . MET   B  1  819  ? 14.985  38.607  97.315  1.00 15.21 ? 817  MET   B CG    1 
ATOM   15013 S  SD    . MET   B  1  819  ? 14.706  36.857  97.667  1.00 16.66 ? 817  MET   B SD    1 
ATOM   15014 C  CE    . MET   B  1  819  ? 14.142  36.323  96.055  1.00 17.91 ? 817  MET   B CE    1 
ATOM   15015 N  N     . ILE   B  1  820  ? 15.837  41.779  98.169  1.00 12.86 ? 818  ILE   B N     1 
ATOM   15016 C  CA    . ILE   B  1  820  ? 15.879  42.369  99.499  1.00 12.91 ? 818  ILE   B CA    1 
ATOM   15017 C  C     . ILE   B  1  820  ? 14.852  41.659  100.347 1.00 12.68 ? 818  ILE   B C     1 
ATOM   15018 O  O     . ILE   B  1  820  ? 13.703  41.495  99.925  1.00 14.36 ? 818  ILE   B O     1 
ATOM   15019 C  CB    . ILE   B  1  820  ? 15.601  43.877  99.448  1.00 13.53 ? 818  ILE   B CB    1 
ATOM   15020 C  CG1   . ILE   B  1  820  ? 16.710  44.559  98.657  1.00 14.70 ? 818  ILE   B CG1   1 
ATOM   15021 C  CG2   . ILE   B  1  820  ? 15.526  44.446  100.871 1.00 14.91 ? 818  ILE   B CG2   1 
ATOM   15022 C  CD1   . ILE   B  1  820  ? 16.538  46.043  98.547  1.00 16.79 ? 818  ILE   B CD1   1 
ATOM   15023 N  N     . VAL   B  1  821  ? 15.265  41.232  101.538 1.00 14.16 ? 819  VAL   B N     1 
ATOM   15024 C  CA    . VAL   B  1  821  ? 14.426  40.466  102.449 1.00 15.25 ? 819  VAL   B CA    1 
ATOM   15025 C  C     . VAL   B  1  821  ? 14.429  41.200  103.774 1.00 14.61 ? 819  VAL   B C     1 
ATOM   15026 O  O     . VAL   B  1  821  ? 15.500  41.424  104.352 1.00 15.96 ? 819  VAL   B O     1 
ATOM   15027 C  CB    . VAL   B  1  821  ? 14.978  39.049  102.657 1.00 14.35 ? 819  VAL   B CB    1 
ATOM   15028 C  CG1   . VAL   B  1  821  ? 14.096  38.279  103.639 1.00 16.57 ? 819  VAL   B CG1   1 
ATOM   15029 C  CG2   . VAL   B  1  821  ? 15.098  38.338  101.324 1.00 14.43 ? 819  VAL   B CG2   1 
ATOM   15030 N  N     . ASP   B  1  822  ? 13.253  41.571  104.256 1.00 14.67 ? 820  ASP   B N     1 
ATOM   15031 C  CA    . ASP   B  1  822  ? 13.195  42.214  105.557 1.00 16.02 ? 820  ASP   B CA    1 
ATOM   15032 C  C     . ASP   B  1  822  ? 12.782  41.211  106.632 1.00 17.95 ? 820  ASP   B C     1 
ATOM   15033 O  O     . ASP   B  1  822  ? 12.549  40.028  106.370 1.00 16.85 ? 820  ASP   B O     1 
ATOM   15034 C  CB    . ASP   B  1  822  ? 12.385  43.518  105.520 1.00 16.53 ? 820  ASP   B CB    1 
ATOM   15035 C  CG    . ASP   B  1  822  ? 10.892  43.300  105.469 1.00 18.63 ? 820  ASP   B CG    1 
ATOM   15036 O  OD1   . ASP   B  1  822  ? 10.403  42.176  105.685 1.00 16.63 ? 820  ASP   B OD1   1 
ATOM   15037 O  OD2   . ASP   B  1  822  ? 10.194  44.306  105.231 1.00 18.51 ? 820  ASP   B OD2   1 
ATOM   15038 N  N     . SER   B  1  823  ? 12.701  41.698  107.869 1.00 17.08 ? 821  SER   B N     1 
ATOM   15039 C  CA    . SER   B  1  823  ? 12.402  40.810  108.980 1.00 17.67 ? 821  SER   B CA    1 
ATOM   15040 C  C     . SER   B  1  823  ? 10.950  40.359  109.016 1.00 19.63 ? 821  SER   B C     1 
ATOM   15041 O  O     . SER   B  1  823  ? 10.603  39.522  109.855 1.00 22.31 ? 821  SER   B O     1 
ATOM   15042 C  CB    . SER   B  1  823  ? 12.783  41.477  110.298 1.00 18.31 ? 821  SER   B CB    1 
ATOM   15043 O  OG    . SER   B  1  823  ? 12.042  42.670  110.480 1.00 22.13 ? 821  SER   B OG    1 
ATOM   15044 N  N     . SER   B  1  824  ? 10.090  40.868  108.140 1.00 16.52 ? 822  SER   B N     1 
ATOM   15045 C  CA    . SER   B  1  824  ? 8.720   40.390  108.122 1.00 17.20 ? 822  SER   B CA    1 
ATOM   15046 C  C     . SER   B  1  824  ? 8.527   39.206  107.189 1.00 19.58 ? 822  SER   B C     1 
ATOM   15047 O  O     . SER   B  1  824  ? 7.472   38.566  107.226 1.00 19.79 ? 822  SER   B O     1 
ATOM   15048 C  CB    . SER   B  1  824  ? 7.759   41.519  107.727 1.00 18.35 ? 822  SER   B CB    1 
ATOM   15049 O  OG    . SER   B  1  824  ? 7.849   41.808  106.345 1.00 16.80 ? 822  SER   B OG    1 
ATOM   15050 N  N     . ALA   B  1  825  ? 9.521   38.901  106.362 1.00 16.53 ? 823  ALA   B N     1 
ATOM   15051 C  CA    . ALA   B  1  825  ? 9.381   37.843  105.379 1.00 17.34 ? 823  ALA   B CA    1 
ATOM   15052 C  C     . ALA   B  1  825  ? 9.396   36.483  106.060 1.00 18.85 ? 823  ALA   B C     1 
ATOM   15053 O  O     . ALA   B  1  825  ? 9.969   36.309  107.140 1.00 19.61 ? 823  ALA   B O     1 
ATOM   15054 C  CB    . ALA   B  1  825  ? 10.540  37.926  104.392 1.00 18.34 ? 823  ALA   B CB    1 
ATOM   15055 N  N     . LEU   B  1  826  ? 8.764   35.512  105.416 1.00 19.78 ? 824  LEU   B N     1 
ATOM   15056 C  CA    . LEU   B  1  826  ? 8.717   34.155  105.940 1.00 18.91 ? 824  LEU   B CA    1 
ATOM   15057 C  C     . LEU   B  1  826  ? 9.964   33.424  105.465 1.00 19.09 ? 824  LEU   B C     1 
ATOM   15058 O  O     . LEU   B  1  826  ? 10.157  33.245  104.260 1.00 18.42 ? 824  LEU   B O     1 
ATOM   15059 C  CB    . LEU   B  1  826  ? 7.462   33.442  105.451 1.00 22.67 ? 824  LEU   B CB    1 
ATOM   15060 C  CG    . LEU   B  1  826  ? 7.288   32.035  106.021 1.00 28.26 ? 824  LEU   B CG    1 
ATOM   15061 C  CD1   . LEU   B  1  826  ? 7.288   32.061  107.546 1.00 31.16 ? 824  LEU   B CD1   1 
ATOM   15062 C  CD2   . LEU   B  1  826  ? 6.002   31.432  105.495 1.00 35.31 ? 824  LEU   B CD2   1 
ATOM   15063 N  N     . ALA   B  1  827  ? 10.804  33.010  106.414 1.00 19.42 ? 825  ALA   B N     1 
ATOM   15064 C  CA    . ALA   B  1  827  ? 12.110  32.456  106.068 1.00 16.72 ? 825  ALA   B CA    1 
ATOM   15065 C  C     . ALA   B  1  827  ? 11.992  31.289  105.097 1.00 18.68 ? 825  ALA   B C     1 
ATOM   15066 O  O     . ALA   B  1  827  ? 12.751  31.212  104.121 1.00 17.17 ? 825  ALA   B O     1 
ATOM   15067 C  CB    . ALA   B  1  827  ? 12.852  32.041  107.335 1.00 17.94 ? 825  ALA   B CB    1 
ATOM   15068 N  N     . GLU   B  1  828  ? 11.045  30.378  105.338 1.00 18.52 ? 826  GLU   B N     1 
ATOM   15069 C  CA    . GLU   B  1  828  ? 10.900  29.224  104.453 1.00 18.67 ? 826  GLU   B CA    1 
ATOM   15070 C  C     . GLU   B  1  828  ? 10.584  29.657  103.031 1.00 18.64 ? 826  GLU   B C     1 
ATOM   15071 O  O     . GLU   B  1  828  ? 11.064  29.052  102.065 1.00 18.06 ? 826  GLU   B O     1 
ATOM   15072 C  CB    . GLU   B  1  828  ? 9.797   28.299  104.962 1.00 21.81 ? 826  GLU   B CB    1 
ATOM   15073 C  CG    . GLU   B  1  828  ? 10.177  27.468  106.172 1.00 23.83 ? 826  GLU   B CG    1 
ATOM   15074 C  CD    . GLU   B  1  828  ? 10.073  28.220  107.493 1.00 24.21 ? 826  GLU   B CD    1 
ATOM   15075 O  OE1   . GLU   B  1  828  ? 9.747   29.433  107.507 1.00 25.50 ? 826  GLU   B OE1   1 
ATOM   15076 O  OE2   . GLU   B  1  828  ? 10.315  27.579  108.539 1.00 27.59 ? 826  GLU   B OE2   1 
ATOM   15077 N  N     . GLN   B  1  829  ? 9.766   30.699  102.880 1.00 16.92 ? 827  GLN   B N     1 
ATOM   15078 C  CA    . GLN   B  1  829  ? 9.417   31.152  101.539 1.00 17.40 ? 827  GLN   B CA    1 
ATOM   15079 C  C     . GLN   B  1  829  ? 10.617  31.802  100.873 1.00 17.63 ? 827  GLN   B C     1 
ATOM   15080 O  O     . GLN   B  1  829  ? 10.905  31.542  99.701  1.00 16.37 ? 827  GLN   B O     1 
ATOM   15081 C  CB    . GLN   B  1  829  ? 8.242   32.127  101.617 1.00 22.36 ? 827  GLN   B CB    1 
ATOM   15082 N  N     . VAL   B  1  830  ? 11.331  32.639  101.616 1.00 16.53 ? 828  VAL   B N     1 
ATOM   15083 C  CA    . VAL   B  1  830  ? 12.567  33.229  101.122 1.00 15.08 ? 828  VAL   B CA    1 
ATOM   15084 C  C     . VAL   B  1  830  ? 13.522  32.143  100.656 1.00 16.59 ? 828  VAL   B C     1 
ATOM   15085 O  O     . VAL   B  1  830  ? 14.079  32.205  99.557  1.00 15.50 ? 828  VAL   B O     1 
ATOM   15086 C  CB    . VAL   B  1  830  ? 13.214  34.082  102.226 1.00 15.01 ? 828  VAL   B CB    1 
ATOM   15087 C  CG1   . VAL   B  1  830  ? 14.608  34.515  101.805 1.00 16.79 ? 828  VAL   B CG1   1 
ATOM   15088 C  CG2   . VAL   B  1  830  ? 12.345  35.268  102.567 1.00 17.13 ? 828  VAL   B CG2   1 
ATOM   15089 N  N     . VAL   B  1  831  ? 13.760  31.150  101.511 1.00 16.15 ? 829  VAL   B N     1 
ATOM   15090 C  CA    . VAL   B  1  831  ? 14.755  30.139  101.187 1.00 14.30 ? 829  VAL   B CA    1 
ATOM   15091 C  C     . VAL   B  1  831  ? 14.380  29.400  99.909  1.00 16.23 ? 829  VAL   B C     1 
ATOM   15092 O  O     . VAL   B  1  831  ? 15.223  29.192  99.032  1.00 16.16 ? 829  VAL   B O     1 
ATOM   15093 C  CB    . VAL   B  1  831  ? 14.966  29.196  102.384 1.00 15.15 ? 829  VAL   B CB    1 
ATOM   15094 C  CG1   . VAL   B  1  831  ? 15.694  27.935  101.952 1.00 15.92 ? 829  VAL   B CG1   1 
ATOM   15095 C  CG2   . VAL   B  1  831  ? 15.738  29.920  103.466 1.00 16.91 ? 829  VAL   B CG2   1 
ATOM   15096 N  N     . GLY   B  1  832  ? 13.118  29.009  99.766  1.00 15.76 ? 830  GLY   B N     1 
ATOM   15097 C  CA    . GLY   B  1  832  ? 12.725  28.332  98.543  1.00 15.01 ? 830  GLY   B CA    1 
ATOM   15098 C  C     . GLY   B  1  832  ? 12.907  29.209  97.321  1.00 15.31 ? 830  GLY   B C     1 
ATOM   15099 O  O     . GLY   B  1  832  ? 13.367  28.748  96.273  1.00 17.00 ? 830  GLY   B O     1 
ATOM   15100 N  N     . ASP   B  1  833  ? 12.573  30.492  97.447  1.00 14.16 ? 831  ASP   B N     1 
ATOM   15101 C  CA    . ASP   B  1  833  ? 12.704  31.394  96.308  1.00 16.85 ? 831  ASP   B CA    1 
ATOM   15102 C  C     . ASP   B  1  833  ? 14.155  31.729  96.022  1.00 15.05 ? 831  ASP   B C     1 
ATOM   15103 O  O     . ASP   B  1  833  ? 14.516  31.969  94.868  1.00 15.01 ? 831  ASP   B O     1 
ATOM   15104 C  CB    . ASP   B  1  833  ? 11.880  32.659  96.536  1.00 16.26 ? 831  ASP   B CB    1 
ATOM   15105 C  CG    . ASP   B  1  833  ? 10.403  32.383  96.541  1.00 15.38 ? 831  ASP   B CG    1 
ATOM   15106 O  OD1   . ASP   B  1  833  ? 10.004  31.319  96.019  1.00 18.27 ? 831  ASP   B OD1   1 
ATOM   15107 O  OD2   . ASP   B  1  833  ? 9.635   33.221  97.049  1.00 17.65 ? 831  ASP   B OD2   1 
ATOM   15108 N  N     . VAL   B  1  834  ? 14.999  31.764  97.052  1.00 14.34 ? 832  VAL   B N     1 
ATOM   15109 C  CA    . VAL   B  1  834  ? 16.417  31.979  96.822  1.00 14.95 ? 832  VAL   B CA    1 
ATOM   15110 C  C     . VAL   B  1  834  ? 17.022  30.788  96.113  1.00 15.09 ? 832  VAL   B C     1 
ATOM   15111 O  O     . VAL   B  1  834  ? 17.829  30.941  95.186  1.00 15.05 ? 832  VAL   B O     1 
ATOM   15112 C  CB    . VAL   B  1  834  ? 17.120  32.268  98.155  1.00 14.02 ? 832  VAL   B CB    1 
ATOM   15113 C  CG1   . VAL   B  1  834  ? 18.627  32.118  98.007  1.00 15.03 ? 832  VAL   B CG1   1 
ATOM   15114 C  CG2   . VAL   B  1  834  ? 16.772  33.663  98.619  1.00 16.55 ? 832  VAL   B CG2   1 
ATOM   15115 N  N     . ILE   B  1  835  ? 16.677  29.582  96.547  1.00 15.06 ? 833  ILE   B N     1 
ATOM   15116 C  CA    . ILE   B  1  835  ? 17.256  28.405  95.917  1.00 17.94 ? 833  ILE   B CA    1 
ATOM   15117 C  C     . ILE   B  1  835  ? 16.879  28.363  94.447  1.00 17.78 ? 833  ILE   B C     1 
ATOM   15118 O  O     . ILE   B  1  835  ? 17.734  28.191  93.569  1.00 20.03 ? 833  ILE   B O     1 
ATOM   15119 C  CB    . ILE   B  1  835  ? 16.833  27.136  96.661  1.00 18.13 ? 833  ILE   B CB    1 
ATOM   15120 C  CG1   . ILE   B  1  835  ? 17.526  27.104  98.014  1.00 22.46 ? 833  ILE   B CG1   1 
ATOM   15121 C  CG2   . ILE   B  1  835  ? 17.157  25.893  95.818  1.00 22.30 ? 833  ILE   B CG2   1 
ATOM   15122 C  CD1   . ILE   B  1  835  ? 17.276  25.848  98.747  1.00 25.15 ? 833  ILE   B CD1   1 
ATOM   15123 N  N     . THR   B  1  836  ? 15.600  28.571  94.157  1.00 15.62 ? 834  THR   B N     1 
ATOM   15124 C  CA    . THR   B  1  836  ? 15.145  28.618  92.777  1.00 16.14 ? 834  THR   B CA    1 
ATOM   15125 C  C     . THR   B  1  836  ? 15.865  29.716  92.006  1.00 17.74 ? 834  THR   B C     1 
ATOM   15126 O  O     . THR   B  1  836  ? 16.374  29.490  90.902  1.00 21.83 ? 834  THR   B O     1 
ATOM   15127 C  CB    . THR   B  1  836  ? 13.640  28.874  92.774  1.00 18.30 ? 834  THR   B CB    1 
ATOM   15128 O  OG1   . THR   B  1  836  ? 12.963  27.761  93.373  1.00 23.57 ? 834  THR   B OG1   1 
ATOM   15129 C  CG2   . THR   B  1  836  ? 13.132  29.051  91.355  1.00 21.48 ? 834  THR   B CG2   1 
ATOM   15130 N  N     . SER   B  1  837  ? 15.931  30.912  92.578  1.00 14.08 ? 835  SER   B N     1 
ATOM   15131 C  CA    . SER   B  1  837  ? 16.417  32.046  91.802  1.00 13.98 ? 835  SER   B CA    1 
ATOM   15132 C  C     . SER   B  1  837  ? 17.927  32.017  91.639  1.00 13.85 ? 835  SER   B C     1 
ATOM   15133 O  O     . SER   B  1  837  ? 18.449  32.431  90.603  1.00 14.69 ? 835  SER   B O     1 
ATOM   15134 C  CB    . SER   B  1  837  ? 16.023  33.358  92.468  1.00 14.41 ? 835  SER   B CB    1 
ATOM   15135 O  OG    . SER   B  1  837  ? 14.613  33.442  92.615  1.00 14.34 ? 835  SER   B OG    1 
ATOM   15136 N  N     . ALA   B  1  838  ? 18.649  31.592  92.668  1.00 13.85 ? 836  ALA   B N     1 
ATOM   15137 C  CA    . ALA   B  1  838  ? 20.098  31.663  92.628  1.00 14.08 ? 836  ALA   B CA    1 
ATOM   15138 C  C     . ALA   B  1  838  ? 20.737  30.419  92.051  1.00 14.65 ? 836  ALA   B C     1 
ATOM   15139 O  O     . ALA   B  1  838  ? 21.780  30.524  91.401  1.00 16.79 ? 836  ALA   B O     1 
ATOM   15140 C  CB    . ALA   B  1  838  ? 20.653  31.856  94.040  1.00 13.73 ? 836  ALA   B CB    1 
ATOM   15141 N  N     . PHE   B  1  839  ? 20.168  29.245  92.290  1.00 16.22 ? 837  PHE   B N     1 
ATOM   15142 C  CA    . PHE   B  1  839  ? 20.896  28.013  92.045  1.00 17.52 ? 837  PHE   B CA    1 
ATOM   15143 C  C     . PHE   B  1  839  ? 20.249  27.091  91.034  1.00 19.23 ? 837  PHE   B C     1 
ATOM   15144 O  O     . PHE   B  1  839  ? 20.941  26.227  90.482  1.00 19.61 ? 837  PHE   B O     1 
ATOM   15145 C  CB    . PHE   B  1  839  ? 21.148  27.265  93.360  1.00 17.86 ? 837  PHE   B CB    1 
ATOM   15146 C  CG    . PHE   B  1  839  ? 21.867  28.089  94.376  1.00 16.97 ? 837  PHE   B CG    1 
ATOM   15147 C  CD1   . PHE   B  1  839  ? 23.142  28.590  94.113  1.00 16.81 ? 837  PHE   B CD1   1 
ATOM   15148 C  CD2   . PHE   B  1  839  ? 21.283  28.378  95.591  1.00 19.12 ? 837  PHE   B CD2   1 
ATOM   15149 C  CE1   . PHE   B  1  839  ? 23.802  29.357  95.038  1.00 16.09 ? 837  PHE   B CE1   1 
ATOM   15150 C  CE2   . PHE   B  1  839  ? 21.954  29.147  96.533  1.00 19.00 ? 837  PHE   B CE2   1 
ATOM   15151 C  CZ    . PHE   B  1  839  ? 23.223  29.629  96.253  1.00 17.75 ? 837  PHE   B CZ    1 
ATOM   15152 N  N     . ASP   B  1  840  ? 18.962  27.238  90.775  1.00 19.63 ? 838  ASP   B N     1 
ATOM   15153 C  CA    . ASP   B  1  840  ? 18.360  26.528  89.663  1.00 20.63 ? 838  ASP   B CA    1 
ATOM   15154 C  C     . ASP   B  1  840  ? 19.130  26.858  88.388  1.00 21.16 ? 838  ASP   B C     1 
ATOM   15155 O  O     . ASP   B  1  840  ? 19.585  27.990  88.186  1.00 18.85 ? 838  ASP   B O     1 
ATOM   15156 C  CB    . ASP   B  1  840  ? 16.898  26.962  89.560  1.00 27.43 ? 838  ASP   B CB    1 
ATOM   15157 C  CG    . ASP   B  1  840  ? 16.148  26.279  88.459  1.00 33.49 ? 838  ASP   B CG    1 
ATOM   15158 O  OD1   . ASP   B  1  840  ? 16.439  26.562  87.279  1.00 37.00 ? 838  ASP   B OD1   1 
ATOM   15159 O  OD2   . ASP   B  1  840  ? 15.245  25.479  88.779  1.00 41.14 ? 838  ASP   B OD2   1 
ATOM   15160 N  N     . SER   B  1  841  ? 19.317  25.850  87.543  1.00 18.92 ? 839  SER   B N     1 
ATOM   15161 C  CA    . SER   B  1  841  ? 20.102  25.999  86.317  1.00 18.97 ? 839  SER   B CA    1 
ATOM   15162 C  C     . SER   B  1  841  ? 21.530  26.414  86.614  1.00 16.84 ? 839  SER   B C     1 
ATOM   15163 O  O     . SER   B  1  841  ? 22.204  27.006  85.770  1.00 15.32 ? 839  SER   B O     1 
ATOM   15164 C  CB    . SER   B  1  841  ? 19.452  26.947  85.305  1.00 20.74 ? 839  SER   B CB    1 
ATOM   15165 O  OG    . SER   B  1  841  ? 18.119  26.533  85.062  1.00 22.87 ? 839  SER   B OG    1 
ATOM   15166 N  N     . ALA   B  1  842  ? 21.993  26.081  87.819  1.00 15.59 ? 840  ALA   B N     1 
ATOM   15167 C  CA    . ALA   B  1  842  ? 23.306  26.484  88.301  1.00 14.18 ? 840  ALA   B CA    1 
ATOM   15168 C  C     . ALA   B  1  842  ? 23.512  27.984  88.135  1.00 14.32 ? 840  ALA   B C     1 
ATOM   15169 O  O     . ALA   B  1  842  ? 24.599  28.451  87.796  1.00 14.53 ? 840  ALA   B O     1 
ATOM   15170 C  CB    . ALA   B  1  842  ? 24.428  25.667  87.661  1.00 15.95 ? 840  ALA   B CB    1 
ATOM   15171 N  N     . GLY   B  1  843  ? 22.444  28.743  88.384  1.00 14.01 ? 841  GLY   B N     1 
ATOM   15172 C  CA    . GLY   B  1  843  ? 22.539  30.184  88.300  1.00 14.09 ? 841  GLY   B CA    1 
ATOM   15173 C  C     . GLY   B  1  843  ? 22.720  30.714  86.904  1.00 13.65 ? 841  GLY   B C     1 
ATOM   15174 O  O     . GLY   B  1  843  ? 23.057  31.888  86.741  1.00 14.50 ? 841  GLY   B O     1 
ATOM   15175 N  N     . GLN   B  1  844  ? 22.513  29.876  85.894  1.00 13.20 ? 842  GLN   B N     1 
ATOM   15176 C  CA    . GLN   B  1  844  ? 22.744  30.263  84.500  1.00 13.60 ? 842  GLN   B CA    1 
ATOM   15177 C  C     . GLN   B  1  844  ? 21.462  30.780  83.854  1.00 14.45 ? 842  GLN   B C     1 
ATOM   15178 O  O     . GLN   B  1  844  ? 20.986  30.307  82.823  1.00 15.15 ? 842  GLN   B O     1 
ATOM   15179 C  CB    . GLN   B  1  844  ? 23.364  29.114  83.727  1.00 13.43 ? 842  GLN   B CB    1 
ATOM   15180 C  CG    . GLN   B  1  844  ? 24.729  28.797  84.301  1.00 13.36 ? 842  GLN   B CG    1 
ATOM   15181 C  CD    . GLN   B  1  844  ? 25.303  27.504  83.798  1.00 13.98 ? 842  GLN   B CD    1 
ATOM   15182 O  OE1   . GLN   B  1  844  ? 26.378  27.485  83.213  1.00 13.93 ? 842  GLN   B OE1   1 
ATOM   15183 N  NE2   . GLN   B  1  844  ? 24.610  26.408  84.059  1.00 16.09 ? 842  GLN   B NE2   1 
ATOM   15184 N  N     . ARG   B  1  845  ? 20.904  31.782  84.519  1.00 14.36 ? 843  ARG   B N     1 
ATOM   15185 C  CA    A ARG   B  1  845  ? 19.795  32.568  84.005  0.52 13.66 ? 843  ARG   B CA    1 
ATOM   15186 C  CA    B ARG   B  1  845  ? 19.796  32.566  84.001  0.48 13.66 ? 843  ARG   B CA    1 
ATOM   15187 C  C     . ARG   B  1  845  ? 20.183  34.028  84.127  1.00 12.31 ? 843  ARG   B C     1 
ATOM   15188 O  O     . ARG   B  1  845  ? 20.755  34.439  85.134  1.00 12.97 ? 843  ARG   B O     1 
ATOM   15189 C  CB    A ARG   B  1  845  ? 18.546  32.376  84.838  0.52 15.81 ? 843  ARG   B CB    1 
ATOM   15190 C  CB    B ARG   B  1  845  ? 18.520  32.331  84.806  0.48 15.81 ? 843  ARG   B CB    1 
ATOM   15191 C  CG    A ARG   B  1  845  ? 17.910  31.017  84.750  0.52 16.82 ? 843  ARG   B CG    1 
ATOM   15192 C  CG    B ARG   B  1  845  ? 18.044  30.887  84.853  0.48 16.56 ? 843  ARG   B CG    1 
ATOM   15193 C  CD    A ARG   B  1  845  ? 16.508  31.155  85.292  0.52 20.25 ? 843  ARG   B CD    1 
ATOM   15194 C  CD    B ARG   B  1  845  ? 16.809  30.790  85.750  0.48 18.55 ? 843  ARG   B CD    1 
ATOM   15195 N  NE    A ARG   B  1  845  ? 15.770  29.902  85.286  0.52 21.71 ? 843  ARG   B NE    1 
ATOM   15196 N  NE    B ARG   B  1  845  ? 16.154  29.492  85.658  0.48 18.73 ? 843  ARG   B NE    1 
ATOM   15197 C  CZ    A ARG   B  1  845  ? 15.671  29.097  86.331  0.52 20.73 ? 843  ARG   B CZ    1 
ATOM   15198 C  CZ    B ARG   B  1  845  ? 15.163  29.206  84.825  0.48 23.33 ? 843  ARG   B CZ    1 
ATOM   15199 N  NH1   A ARG   B  1  845  ? 16.298  29.359  87.469  0.52 21.19 ? 843  ARG   B NH1   1 
ATOM   15200 N  NH1   B ARG   B  1  845  ? 14.676  30.111  83.990  0.48 23.76 ? 843  ARG   B NH1   1 
ATOM   15201 N  NH2   A ARG   B  1  845  ? 14.918  28.005  86.239  0.52 23.15 ? 843  ARG   B NH2   1 
ATOM   15202 N  NH2   B ARG   B  1  845  ? 14.646  27.981  84.830  0.48 27.59 ? 843  ARG   B NH2   1 
ATOM   15203 N  N     . CYS   B  1  846  ? 19.875  34.821  83.107  1.00 13.76 ? 844  CYS   B N     1 
ATOM   15204 C  CA    . CYS   B  1  846  ? 20.154  36.244  83.233  1.00 13.84 ? 844  CYS   B CA    1 
ATOM   15205 C  C     . CYS   B  1  846  ? 19.408  36.850  84.410  1.00 11.53 ? 844  CYS   B C     1 
ATOM   15206 O  O     . CYS   B  1  846  ? 19.869  37.829  85.005  1.00 14.01 ? 844  CYS   B O     1 
ATOM   15207 C  CB    . CYS   B  1  846  ? 19.744  36.940  81.947  1.00 14.79 ? 844  CYS   B CB    1 
ATOM   15208 S  SG    . CYS   B  1  846  ? 18.084  36.584  81.372  1.00 14.37 ? 844  CYS   B SG    1 
ATOM   15209 N  N     . SER   B  1  847  ? 18.248  36.294  84.733  1.00 12.70 ? 845  SER   B N     1 
ATOM   15210 C  CA    . SER   B  1  847  ? 17.382  36.730  85.817  1.00 12.62 ? 845  SER   B CA    1 
ATOM   15211 C  C     . SER   B  1  847  ? 17.823  36.214  87.178  1.00 12.81 ? 845  SER   B C     1 
ATOM   15212 O  O     . SER   B  1  847  ? 17.185  36.561  88.176  1.00 12.82 ? 845  SER   B O     1 
ATOM   15213 C  CB    . SER   B  1  847  ? 15.991  36.177  85.534  1.00 12.92 ? 845  SER   B CB    1 
ATOM   15214 O  OG    . SER   B  1  847  ? 16.112  34.789  85.289  1.00 14.18 ? 845  SER   B OG    1 
ATOM   15215 N  N     . ALA   B  1  848  ? 18.875  35.398  87.240  1.00 12.93 ? 846  ALA   B N     1 
ATOM   15216 C  CA    . ALA   B  1  848  ? 19.202  34.698  88.472  1.00 12.68 ? 846  ALA   B CA    1 
ATOM   15217 C  C     . ALA   B  1  848  ? 19.553  35.666  89.588  1.00 12.86 ? 846  ALA   B C     1 
ATOM   15218 O  O     . ALA   B  1  848  ? 20.118  36.742  89.369  1.00 13.09 ? 846  ALA   B O     1 
ATOM   15219 C  CB    . ALA   B  1  848  ? 20.408  33.789  88.247  1.00 13.34 ? 846  ALA   B CB    1 
ATOM   15220 N  N     . LEU   B  1  849  ? 19.224  35.244  90.806  1.00 12.76 ? 847  LEU   B N     1 
ATOM   15221 C  CA    . LEU   B  1  849  ? 19.557  36.022  91.986  1.00 13.64 ? 847  LEU   B CA    1 
ATOM   15222 C  C     . LEU   B  1  849  ? 21.058  36.005  92.240  1.00 12.86 ? 847  LEU   B C     1 
ATOM   15223 O  O     . LEU   B  1  849  ? 21.645  34.939  92.441  1.00 14.84 ? 847  LEU   B O     1 
ATOM   15224 C  CB    . LEU   B  1  849  ? 18.803  35.441  93.167  1.00 13.98 ? 847  LEU   B CB    1 
ATOM   15225 C  CG    . LEU   B  1  849  ? 19.188  36.069  94.503  1.00 13.37 ? 847  LEU   B CG    1 
ATOM   15226 C  CD1   . LEU   B  1  849  ? 18.895  37.563  94.527  1.00 14.93 ? 847  LEU   B CD1   1 
ATOM   15227 C  CD2   . LEU   B  1  849  ? 18.426  35.341  95.598  1.00 14.65 ? 847  LEU   B CD2   1 
ATOM   15228 N  N     . ARG   B  1  850  ? 21.671  37.187  92.228  1.00 13.06 ? 848  ARG   B N     1 
ATOM   15229 C  CA    . ARG   B  1  850  ? 23.101  37.324  92.457  1.00 12.17 ? 848  ARG   B CA    1 
ATOM   15230 C  C     . ARG   B  1  850  ? 23.439  37.879  93.824  1.00 13.54 ? 848  ARG   B C     1 
ATOM   15231 O  O     . ARG   B  1  850  ? 24.511  37.585  94.350  1.00 14.38 ? 848  ARG   B O     1 
ATOM   15232 C  CB    . ARG   B  1  850  ? 23.720  38.260  91.410  1.00 13.73 ? 848  ARG   B CB    1 
ATOM   15233 C  CG    . ARG   B  1  850  ? 23.390  37.886  89.989  1.00 13.70 ? 848  ARG   B CG    1 
ATOM   15234 C  CD    . ARG   B  1  850  ? 23.763  36.462  89.719  1.00 13.43 ? 848  ARG   B CD    1 
ATOM   15235 N  NE    . ARG   B  1  850  ? 23.581  36.135  88.312  1.00 13.66 ? 848  ARG   B NE    1 
ATOM   15236 C  CZ    . ARG   B  1  850  ? 23.709  34.912  87.820  1.00 13.53 ? 848  ARG   B CZ    1 
ATOM   15237 N  NH1   . ARG   B  1  850  ? 23.970  33.878  88.604  1.00 15.02 ? 848  ARG   B NH1   1 
ATOM   15238 N  NH2   . ARG   B  1  850  ? 23.522  34.717  86.513  1.00 13.95 ? 848  ARG   B NH2   1 
ATOM   15239 N  N     . VAL   B  1  851  ? 22.567  38.695  94.399  1.00 13.44 ? 849  VAL   B N     1 
ATOM   15240 C  CA    . VAL   B  1  851  ? 22.865  39.383  95.646  1.00 13.45 ? 849  VAL   B CA    1 
ATOM   15241 C  C     . VAL   B  1  851  ? 21.637  39.282  96.535  1.00 14.66 ? 849  VAL   B C     1 
ATOM   15242 O  O     . VAL   B  1  851  ? 20.608  39.902  96.256  1.00 14.61 ? 849  VAL   B O     1 
ATOM   15243 C  CB    . VAL   B  1  851  ? 23.249  40.853  95.434  1.00 15.01 ? 849  VAL   B CB    1 
ATOM   15244 C  CG1   . VAL   B  1  851  ? 23.650  41.460  96.777  1.00 17.90 ? 849  VAL   B CG1   1 
ATOM   15245 C  CG2   . VAL   B  1  851  ? 24.394  40.978  94.425  1.00 18.03 ? 849  VAL   B CG2   1 
ATOM   15246 N  N     . LEU   B  1  852  ? 21.735  38.502  97.603  1.00 14.79 ? 850  LEU   B N     1 
ATOM   15247 C  CA    . LEU   B  1  852  ? 20.662  38.360  98.573  1.00 14.16 ? 850  LEU   B CA    1 
ATOM   15248 C  C     . LEU   B  1  852  ? 20.947  39.330  99.707  1.00 13.42 ? 850  LEU   B C     1 
ATOM   15249 O  O     . LEU   B  1  852  ? 22.004  39.245  100.341 1.00 14.04 ? 850  LEU   B O     1 
ATOM   15250 C  CB    . LEU   B  1  852  ? 20.637  36.929  99.105  1.00 14.53 ? 850  LEU   B CB    1 
ATOM   15251 C  CG    . LEU   B  1  852  ? 19.591  36.675  100.187 1.00 13.83 ? 850  LEU   B CG    1 
ATOM   15252 C  CD1   . LEU   B  1  852  ? 18.171  36.967  99.690  1.00 15.52 ? 850  LEU   B CD1   1 
ATOM   15253 C  CD2   . LEU   B  1  852  ? 19.699  35.238  100.671 1.00 16.04 ? 850  LEU   B CD2   1 
ATOM   15254 N  N     . CYS   B  1  853  ? 20.033  40.265  99.936  1.00 13.52 ? 851  CYS   B N     1 
ATOM   15255 C  CA    . CYS   B  1  853  ? 20.201  41.303  100.947 1.00 14.53 ? 851  CYS   B CA    1 
ATOM   15256 C  C     . CYS   B  1  853  ? 19.254  40.993  102.093 1.00 13.98 ? 851  CYS   B C     1 
ATOM   15257 O  O     . CYS   B  1  853  ? 18.031  41.046  101.939 1.00 15.35 ? 851  CYS   B O     1 
ATOM   15258 C  CB    . CYS   B  1  853  ? 19.905  42.681  100.374 1.00 14.52 ? 851  CYS   B CB    1 
ATOM   15259 S  SG    . CYS   B  1  853  ? 20.844  43.035  98.891  1.00 17.20 ? 851  CYS   B SG    1 
ATOM   15260 N  N     . LEU   B  1  854  ? 19.816  40.680  103.249 1.00 14.54 ? 852  LEU   B N     1 
ATOM   15261 C  CA    . LEU   B  1  854  ? 19.029  40.207  104.376 1.00 15.49 ? 852  LEU   B CA    1 
ATOM   15262 C  C     . LEU   B  1  854  ? 19.094  41.236  105.488 1.00 14.75 ? 852  LEU   B C     1 
ATOM   15263 O  O     . LEU   B  1  854  ? 20.184  41.664  105.880 1.00 15.83 ? 852  LEU   B O     1 
ATOM   15264 C  CB    . LEU   B  1  854  ? 19.606  38.897  104.904 1.00 15.68 ? 852  LEU   B CB    1 
ATOM   15265 C  CG    . LEU   B  1  854  ? 19.632  37.768  103.884 1.00 14.30 ? 852  LEU   B CG    1 
ATOM   15266 C  CD1   . LEU   B  1  854  ? 20.354  36.579  104.524 1.00 16.85 ? 852  LEU   B CD1   1 
ATOM   15267 C  CD2   . LEU   B  1  854  ? 18.214  37.410  103.493 1.00 17.44 ? 852  LEU   B CD2   1 
ATOM   15268 N  N     . GLN   B  1  855  ? 17.936  41.614  106.006 1.00 15.48 ? 853  GLN   B N     1 
ATOM   15269 C  CA    . GLN   B  1  855  ? 17.941  42.495  107.159 1.00 15.49 ? 853  GLN   B CA    1 
ATOM   15270 C  C     . GLN   B  1  855  ? 18.717  41.817  108.283 1.00 18.62 ? 853  GLN   B C     1 
ATOM   15271 O  O     . GLN   B  1  855  ? 18.604  40.605  108.491 1.00 16.88 ? 853  GLN   B O     1 
ATOM   15272 C  CB    . GLN   B  1  855  ? 16.518  42.772  107.605 1.00 15.92 ? 853  GLN   B CB    1 
ATOM   15273 C  CG    . GLN   B  1  855  ? 16.448  43.900  108.615 1.00 19.28 ? 853  GLN   B CG    1 
ATOM   15274 C  CD    . GLN   B  1  855  ? 15.041  44.229  109.034 1.00 21.75 ? 853  GLN   B CD    1 
ATOM   15275 O  OE1   . GLN   B  1  855  ? 14.132  44.272  108.214 1.00 22.88 ? 853  GLN   B OE1   1 
ATOM   15276 N  NE2   . GLN   B  1  855  ? 14.854  44.481  110.322 1.00 24.63 ? 853  GLN   B NE2   1 
ATOM   15277 N  N     . GLU   B  1  856  ? 19.536  42.608  108.980 1.00 17.57 ? 854  GLU   B N     1 
ATOM   15278 C  CA    . GLU   B  1  856  ? 20.538  42.047  109.882 1.00 19.40 ? 854  GLU   B CA    1 
ATOM   15279 C  C     . GLU   B  1  856  ? 19.917  41.120  110.921 1.00 18.52 ? 854  GLU   B C     1 
ATOM   15280 O  O     . GLU   B  1  856  ? 20.508  40.091  111.272 1.00 20.66 ? 854  GLU   B O     1 
ATOM   15281 C  CB    . GLU   B  1  856  ? 21.305  43.186  110.558 1.00 22.68 ? 854  GLU   B CB    1 
ATOM   15282 N  N     . ASP   B  1  857  ? 18.722  41.458  111.411 1.00 20.02 ? 855  ASP   B N     1 
ATOM   15283 C  CA    . ASP   B  1  857  ? 18.134  40.731  112.533 1.00 22.27 ? 855  ASP   B CA    1 
ATOM   15284 C  C     . ASP   B  1  857  ? 17.649  39.342  112.151 1.00 21.03 ? 855  ASP   B C     1 
ATOM   15285 O  O     . ASP   B  1  857  ? 17.427  38.508  113.034 1.00 24.02 ? 855  ASP   B O     1 
ATOM   15286 C  CB    . ASP   B  1  857  ? 16.966  41.522  113.127 1.00 28.81 ? 855  ASP   B CB    1 
ATOM   15287 N  N     . VAL   B  1  858  ? 17.447  39.076  110.865 1.00 16.92 ? 856  VAL   B N     1 
ATOM   15288 C  CA    . VAL   B  1  858  ? 16.999  37.766  110.418 1.00 17.57 ? 856  VAL   B CA    1 
ATOM   15289 C  C     . VAL   B  1  858  ? 18.034  37.051  109.585 1.00 13.87 ? 856  VAL   B C     1 
ATOM   15290 O  O     . VAL   B  1  858  ? 17.802  35.903  109.192 1.00 16.54 ? 856  VAL   B O     1 
ATOM   15291 C  CB    . VAL   B  1  858  ? 15.655  37.828  109.673 1.00 18.00 ? 856  VAL   B CB    1 
ATOM   15292 C  CG1   . VAL   B  1  858  ? 14.554  38.295  110.610 1.00 21.49 ? 856  VAL   B CG1   1 
ATOM   15293 C  CG2   . VAL   B  1  858  ? 15.768  38.738  108.452 1.00 18.17 ? 856  VAL   B CG2   1 
ATOM   15294 N  N     . ALA   B  1  859  ? 19.175  37.685  109.312 1.00 15.69 ? 857  ALA   B N     1 
ATOM   15295 C  CA    . ALA   B  1  859  ? 20.136  37.126  108.365 1.00 17.00 ? 857  ALA   B CA    1 
ATOM   15296 C  C     . ALA   B  1  859  ? 20.640  35.755  108.800 1.00 15.84 ? 857  ALA   B C     1 
ATOM   15297 O  O     . ALA   B  1  859  ? 20.665  34.819  108.003 1.00 17.13 ? 857  ALA   B O     1 
ATOM   15298 C  CB    . ALA   B  1  859  ? 21.295  38.095  108.143 1.00 17.46 ? 857  ALA   B CB    1 
ATOM   15299 N  N     . ASP   B  1  860  ? 21.044  35.615  110.062 1.00 18.17 ? 858  ASP   B N     1 
ATOM   15300 C  CA    . ASP   B  1  860  ? 21.624  34.349  110.499 1.00 18.22 ? 858  ASP   B CA    1 
ATOM   15301 C  C     . ASP   B  1  860  ? 20.628  33.207  110.388 1.00 17.10 ? 858  ASP   B C     1 
ATOM   15302 O  O     . ASP   B  1  860  ? 20.974  32.116  109.918 1.00 17.19 ? 858  ASP   B O     1 
ATOM   15303 C  CB    . ASP   B  1  860  ? 22.127  34.463  111.936 1.00 17.65 ? 858  ASP   B CB    1 
ATOM   15304 C  CG    . ASP   B  1  860  ? 23.335  35.354  112.060 1.00 24.34 ? 858  ASP   B CG    1 
ATOM   15305 O  OD1   . ASP   B  1  860  ? 24.118  35.445  111.092 1.00 28.79 ? 858  ASP   B OD1   1 
ATOM   15306 O  OD2   . ASP   B  1  860  ? 23.509  35.961  113.135 1.00 29.30 ? 858  ASP   B OD2   1 
ATOM   15307 N  N     . ARG   B  1  861  ? 19.378  33.437  110.801 1.00 16.65 ? 859  ARG   B N     1 
ATOM   15308 C  CA    . ARG   B  1  861  ? 18.394  32.367  110.746 1.00 18.48 ? 859  ARG   B CA    1 
ATOM   15309 C  C     . ARG   B  1  861  ? 18.079  31.985  109.306 1.00 17.03 ? 859  ARG   B C     1 
ATOM   15310 O  O     . ARG   B  1  861  ? 17.964  30.798  108.983 1.00 17.62 ? 859  ARG   B O     1 
ATOM   15311 C  CB    . ARG   B  1  861  ? 17.124  32.766  111.495 1.00 22.01 ? 859  ARG   B CB    1 
ATOM   15312 C  CG    . ARG   B  1  861  ? 16.072  31.686  111.459 1.00 29.53 ? 859  ARG   B CG    1 
ATOM   15313 C  CD    . ARG   B  1  861  ? 14.965  31.895  112.469 1.00 37.09 ? 859  ARG   B CD    1 
ATOM   15314 N  NE    . ARG   B  1  861  ? 13.910  30.913  112.244 1.00 45.84 ? 859  ARG   B NE    1 
ATOM   15315 C  CZ    . ARG   B  1  861  ? 12.892  31.093  111.415 1.00 41.04 ? 859  ARG   B CZ    1 
ATOM   15316 N  NH1   . ARG   B  1  861  ? 12.714  32.241  110.779 1.00 37.68 ? 859  ARG   B NH1   1 
ATOM   15317 N  NH2   . ARG   B  1  861  ? 12.034  30.095  111.214 1.00 41.16 ? 859  ARG   B NH2   1 
ATOM   15318 N  N     . ILE   B  1  862  ? 17.968  32.977  108.420 1.00 15.76 ? 860  ILE   B N     1 
ATOM   15319 C  CA    . ILE   B  1  862  ? 17.723  32.657  107.018 1.00 16.76 ? 860  ILE   B CA    1 
ATOM   15320 C  C     . ILE   B  1  862  ? 18.908  31.923  106.415 1.00 14.96 ? 860  ILE   B C     1 
ATOM   15321 O  O     . ILE   B  1  862  ? 18.732  30.949  105.675 1.00 16.15 ? 860  ILE   B O     1 
ATOM   15322 C  CB    . ILE   B  1  862  ? 17.360  33.929  106.244 1.00 16.34 ? 860  ILE   B CB    1 
ATOM   15323 C  CG1   . ILE   B  1  862  ? 15.975  34.386  106.700 1.00 18.53 ? 860  ILE   B CG1   1 
ATOM   15324 C  CG2   . ILE   B  1  862  ? 17.408  33.680  104.736 1.00 15.38 ? 860  ILE   B CG2   1 
ATOM   15325 C  CD1   . ILE   B  1  862  ? 15.582  35.754  106.180 1.00 20.85 ? 860  ILE   B CD1   1 
ATOM   15326 N  N     . LEU   B  1  863  ? 20.122  32.369  106.714 1.00 16.28 ? 861  LEU   B N     1 
ATOM   15327 C  CA    . LEU   B  1  863  ? 21.287  31.713  106.135 1.00 16.59 ? 861  LEU   B CA    1 
ATOM   15328 C  C     . LEU   B  1  863  ? 21.421  30.288  106.644 1.00 17.49 ? 861  LEU   B C     1 
ATOM   15329 O  O     . LEU   B  1  863  ? 21.792  29.386  105.885 1.00 16.38 ? 861  LEU   B O     1 
ATOM   15330 C  CB    . LEU   B  1  863  ? 22.554  32.505  106.429 1.00 16.88 ? 861  LEU   B CB    1 
ATOM   15331 C  CG    . LEU   B  1  863  ? 22.622  33.821  105.666 1.00 19.40 ? 861  LEU   B CG    1 
ATOM   15332 C  CD1   . LEU   B  1  863  ? 23.757  34.666  106.213 1.00 20.99 ? 861  LEU   B CD1   1 
ATOM   15333 C  CD2   . LEU   B  1  863  ? 22.793  33.560  104.166 1.00 20.89 ? 861  LEU   B CD2   1 
ATOM   15334 N  N     . THR   B  1  864  ? 21.122  30.062  107.923 1.00 16.21 ? 862  THR   B N     1 
ATOM   15335 C  CA    . THR   B  1  864  ? 21.171  28.696  108.425 1.00 16.76 ? 862  THR   B CA    1 
ATOM   15336 C  C     . THR   B  1  864  ? 20.172  27.828  107.683 1.00 18.02 ? 862  THR   B C     1 
ATOM   15337 O  O     . THR   B  1  864  ? 20.486  26.707  107.276 1.00 18.04 ? 862  THR   B O     1 
ATOM   15338 C  CB    . THR   B  1  864  ? 20.874  28.677  109.922 1.00 20.29 ? 862  THR   B CB    1 
ATOM   15339 O  OG1   . THR   B  1  864  ? 21.919  29.357  110.613 1.00 22.58 ? 862  THR   B OG1   1 
ATOM   15340 C  CG2   . THR   B  1  864  ? 20.772  27.235  110.430 1.00 23.74 ? 862  THR   B CG2   1 
ATOM   15341 N  N     . MET   B  1  865  ? 18.966  28.345  107.465 1.00 15.20 ? 863  MET   B N     1 
ATOM   15342 C  CA    . MET   B  1  865  ? 17.956  27.562  106.777 1.00 15.76 ? 863  MET   B CA    1 
ATOM   15343 C  C     . MET   B  1  865  ? 18.335  27.348  105.321 1.00 16.30 ? 863  MET   B C     1 
ATOM   15344 O  O     . MET   B  1  865  ? 18.159  26.252  104.777 1.00 16.03 ? 863  MET   B O     1 
ATOM   15345 C  CB    . MET   B  1  865  ? 16.619  28.289  106.865 1.00 16.64 ? 863  MET   B CB    1 
ATOM   15346 C  CG    . MET   B  1  865  ? 15.471  27.501  106.323 1.00 18.10 ? 863  MET   B CG    1 
ATOM   15347 S  SD    . MET   B  1  865  ? 13.931  28.392  106.470 1.00 20.25 ? 863  MET   B SD    1 
ATOM   15348 C  CE    . MET   B  1  865  ? 13.849  28.600  108.245 1.00 22.64 ? 863  MET   B CE    1 
ATOM   15349 N  N     . LEU   B  1  866  ? 18.848  28.395  104.677 1.00 15.39 ? 864  LEU   B N     1 
ATOM   15350 C  CA    . LEU   B  1  866  ? 19.279  28.276  103.290 1.00 15.14 ? 864  LEU   B CA    1 
ATOM   15351 C  C     . LEU   B  1  866  ? 20.345  27.205  103.152 1.00 16.07 ? 864  LEU   B C     1 
ATOM   15352 O  O     . LEU   B  1  866  ? 20.266  26.342  102.275 1.00 16.12 ? 864  LEU   B O     1 
ATOM   15353 C  CB    . LEU   B  1  866  ? 19.825  29.621  102.822 1.00 16.11 ? 864  LEU   B CB    1 
ATOM   15354 C  CG    . LEU   B  1  866  ? 20.454  29.606  101.429 1.00 15.06 ? 864  LEU   B CG    1 
ATOM   15355 C  CD1   . LEU   B  1  866  ? 19.460  29.149  100.379 1.00 17.57 ? 864  LEU   B CD1   1 
ATOM   15356 C  CD2   . LEU   B  1  866  ? 20.982  30.999  101.098 1.00 18.00 ? 864  LEU   B CD2   1 
ATOM   15357 N  N     . LYS   B  1  867  ? 21.340  27.226  104.036 1.00 15.61 ? 865  LYS   B N     1 
ATOM   15358 C  CA    . LYS   B  1  867  ? 22.406  26.243  103.929 1.00 16.68 ? 865  LYS   B CA    1 
ATOM   15359 C  C     . LYS   B  1  867  ? 21.887  24.837  104.185 1.00 17.26 ? 865  LYS   B C     1 
ATOM   15360 O  O     . LYS   B  1  867  ? 22.292  23.891  103.504 1.00 16.56 ? 865  LYS   B O     1 
ATOM   15361 C  CB    . LYS   B  1  867  ? 23.552  26.622  104.858 1.00 17.74 ? 865  LYS   B CB    1 
ATOM   15362 C  CG    . LYS   B  1  867  ? 24.271  27.871  104.351 1.00 21.07 ? 865  LYS   B CG    1 
ATOM   15363 C  CD    . LYS   B  1  867  ? 25.146  28.490  105.405 1.00 24.80 ? 865  LYS   B CD    1 
ATOM   15364 C  CE    . LYS   B  1  867  ? 25.688  29.830  104.926 1.00 28.22 ? 865  LYS   B CE    1 
ATOM   15365 N  NZ    . LYS   B  1  867  ? 26.508  30.487  105.987 1.00 32.19 ? 865  LYS   B NZ    1 
ATOM   15366 N  N     . GLY   B  1  868  ? 20.953  24.688  105.129 1.00 16.59 ? 866  GLY   B N     1 
ATOM   15367 C  CA    . GLY   B  1  868  ? 20.363  23.378  105.356 1.00 16.87 ? 866  GLY   B CA    1 
ATOM   15368 C  C     . GLY   B  1  868  ? 19.582  22.889  104.154 1.00 16.93 ? 866  GLY   B C     1 
ATOM   15369 O  O     . GLY   B  1  868  ? 19.630  21.708  103.801 1.00 18.21 ? 866  GLY   B O     1 
ATOM   15370 N  N     . ALA   B  1  869  ? 18.859  23.793  103.499 1.00 16.97 ? 867  ALA   B N     1 
ATOM   15371 C  CA    . ALA   B  1  869  ? 18.137  23.429  102.292 1.00 16.95 ? 867  ALA   B CA    1 
ATOM   15372 C  C     . ALA   B  1  869  ? 19.099  23.092  101.158 1.00 15.88 ? 867  ALA   B C     1 
ATOM   15373 O  O     . ALA   B  1  869  ? 18.863  22.144  100.402 1.00 15.83 ? 867  ALA   B O     1 
ATOM   15374 C  CB    . ALA   B  1  869  ? 17.193  24.564  101.892 1.00 17.82 ? 867  ALA   B CB    1 
ATOM   15375 N  N     . LEU   B  1  870  ? 20.203  23.837  101.042 1.00 15.09 ? 868  LEU   B N     1 
ATOM   15376 C  CA    . LEU   B  1  870  ? 21.178  23.540  99.992  1.00 17.10 ? 868  LEU   B CA    1 
ATOM   15377 C  C     . LEU   B  1  870  ? 21.792  22.161  100.165 1.00 16.54 ? 868  LEU   B C     1 
ATOM   15378 O  O     . LEU   B  1  870  ? 22.133  21.510  99.175  1.00 17.61 ? 868  LEU   B O     1 
ATOM   15379 C  CB    . LEU   B  1  870  ? 22.290  24.586  99.977  1.00 18.00 ? 868  LEU   B CB    1 
ATOM   15380 C  CG    . LEU   B  1  870  ? 21.884  25.934  99.400  1.00 18.94 ? 868  LEU   B CG    1 
ATOM   15381 C  CD1   . LEU   B  1  870  ? 22.998  26.941  99.557  1.00 20.43 ? 868  LEU   B CD1   1 
ATOM   15382 C  CD2   . LEU   B  1  870  ? 21.535  25.744  97.925  1.00 21.52 ? 868  LEU   B CD2   1 
ATOM   15383 N  N     . HIS   B  1  871  ? 21.940  21.700  101.404 1.00 15.50 ? 869  HIS   B N     1 
ATOM   15384 C  CA    A HIS   B  1  871  ? 22.515  20.379  101.616 0.52 17.33 ? 869  HIS   B CA    1 
ATOM   15385 C  CA    B HIS   B  1  871  ? 22.498  20.379  101.656 0.48 17.33 ? 869  HIS   B CA    1 
ATOM   15386 C  C     . HIS   B  1  871  ? 21.620  19.274  101.090 1.00 18.26 ? 869  HIS   B C     1 
ATOM   15387 O  O     . HIS   B  1  871  ? 22.092  18.146  100.913 1.00 19.87 ? 869  HIS   B O     1 
ATOM   15388 C  CB    A HIS   B  1  871  ? 22.856  20.154  103.091 0.52 18.68 ? 869  HIS   B CB    1 
ATOM   15389 C  CB    B HIS   B  1  871  ? 22.679  20.188  103.164 0.48 18.57 ? 869  HIS   B CB    1 
ATOM   15390 C  CG    A HIS   B  1  871  ? 24.194  20.696  103.482 0.52 22.21 ? 869  HIS   B CG    1 
ATOM   15391 C  CG    B HIS   B  1  871  ? 23.302  18.882  103.537 0.48 21.09 ? 869  HIS   B CG    1 
ATOM   15392 N  ND1   A HIS   B  1  871  ? 24.357  21.943  104.047 0.52 21.75 ? 869  HIS   B ND1   1 
ATOM   15393 N  ND1   B HIS   B  1  871  ? 24.651  18.635  103.397 0.48 26.00 ? 869  HIS   B ND1   1 
ATOM   15394 C  CD2   A HIS   B  1  871  ? 25.436  20.168  103.368 0.52 24.38 ? 869  HIS   B CD2   1 
ATOM   15395 C  CD2   B HIS   B  1  871  ? 22.761  17.746  104.035 0.48 24.96 ? 869  HIS   B CD2   1 
ATOM   15396 C  CE1   A HIS   B  1  871  ? 25.640  22.154  104.277 0.52 24.29 ? 869  HIS   B CE1   1 
ATOM   15397 C  CE1   B HIS   B  1  871  ? 24.914  17.405  103.798 0.48 22.97 ? 869  HIS   B CE1   1 
ATOM   15398 N  NE2   A HIS   B  1  871  ? 26.316  21.097  103.865 0.52 22.34 ? 869  HIS   B NE2   1 
ATOM   15399 N  NE2   B HIS   B  1  871  ? 23.785  16.844  104.191 0.48 26.32 ? 869  HIS   B NE2   1 
ATOM   15400 N  N     . GLU   B  1  872  ? 20.358  19.571  100.811 1.00 15.73 ? 870  GLU   B N     1 
ATOM   15401 C  CA    . GLU   B  1  872  ? 19.445  18.563  100.306 1.00 17.11 ? 870  GLU   B CA    1 
ATOM   15402 C  C     . GLU   B  1  872  ? 19.381  18.518  98.793  1.00 16.49 ? 870  GLU   B C     1 
ATOM   15403 O  O     . GLU   B  1  872  ? 18.624  17.708  98.248  1.00 17.64 ? 870  GLU   B O     1 
ATOM   15404 C  CB    . GLU   B  1  872  ? 18.044  18.795  100.869 1.00 17.00 ? 870  GLU   B CB    1 
ATOM   15405 C  CG    . GLU   B  1  872  ? 18.029  18.795  102.375 1.00 18.19 ? 870  GLU   B CG    1 
ATOM   15406 C  CD    . GLU   B  1  872  ? 18.464  17.472  102.965 1.00 18.91 ? 870  GLU   B CD    1 
ATOM   15407 O  OE1   . GLU   B  1  872  ? 18.327  16.442  102.275 1.00 21.81 ? 870  GLU   B OE1   1 
ATOM   15408 O  OE2   . GLU   B  1  872  ? 18.939  17.449  104.117 1.00 20.54 ? 870  GLU   B OE2   1 
ATOM   15409 N  N     . LEU   B  1  873  ? 20.147  19.354  98.104  1.00 16.61 ? 871  LEU   B N     1 
ATOM   15410 C  CA    . LEU   B  1  873  ? 20.086  19.371  96.653  1.00 16.79 ? 871  LEU   B CA    1 
ATOM   15411 C  C     . LEU   B  1  873  ? 20.983  18.299  96.065  1.00 17.96 ? 871  LEU   B C     1 
ATOM   15412 O  O     . LEU   B  1  873  ? 22.049  17.979  96.594  1.00 19.41 ? 871  LEU   B O     1 
ATOM   15413 C  CB    . LEU   B  1  873  ? 20.535  20.717  96.099  1.00 17.13 ? 871  LEU   B CB    1 
ATOM   15414 C  CG    . LEU   B  1  873  ? 19.681  21.897  96.528  1.00 19.25 ? 871  LEU   B CG    1 
ATOM   15415 C  CD1   . LEU   B  1  873  ? 20.147  23.127  95.769  1.00 21.18 ? 871  LEU   B CD1   1 
ATOM   15416 C  CD2   . LEU   B  1  873  ? 18.198  21.622  96.277  1.00 18.11 ? 871  LEU   B CD2   1 
ATOM   15417 N  N     . HIS   B  1  874  ? 20.545  17.763  94.939  1.00 17.46 ? 872  HIS   B N     1 
ATOM   15418 C  CA    . HIS   B  1  874  ? 21.314  16.790  94.191  1.00 18.83 ? 872  HIS   B CA    1 
ATOM   15419 C  C     . HIS   B  1  874  ? 21.894  17.495  92.969  1.00 16.14 ? 872  HIS   B C     1 
ATOM   15420 O  O     . HIS   B  1  874  ? 21.148  18.025  92.139  1.00 16.59 ? 872  HIS   B O     1 
ATOM   15421 C  CB    . HIS   B  1  874  ? 20.390  15.643  93.795  1.00 19.08 ? 872  HIS   B CB    1 
ATOM   15422 C  CG    . HIS   B  1  874  ? 21.050  14.566  93.000  1.00 18.99 ? 872  HIS   B CG    1 
ATOM   15423 N  ND1   . HIS   B  1  874  ? 20.363  13.461  92.546  1.00 25.63 ? 872  HIS   B ND1   1 
ATOM   15424 C  CD2   . HIS   B  1  874  ? 22.322  14.427  92.556  1.00 22.85 ? 872  HIS   B CD2   1 
ATOM   15425 C  CE1   . HIS   B  1  874  ? 21.187  12.680  91.870  1.00 24.82 ? 872  HIS   B CE1   1 
ATOM   15426 N  NE2   . HIS   B  1  874  ? 22.381  13.245  91.858  1.00 27.04 ? 872  HIS   B NE2   1 
ATOM   15427 N  N     . ILE   B  1  875  ? 23.217  17.509  92.872  1.00 16.56 ? 873  ILE   B N     1 
ATOM   15428 C  CA    . ILE   B  1  875  ? 23.932  18.117  91.757  1.00 17.98 ? 873  ILE   B CA    1 
ATOM   15429 C  C     . ILE   B  1  875  ? 24.456  16.992  90.885  1.00 18.05 ? 873  ILE   B C     1 
ATOM   15430 O  O     . ILE   B  1  875  ? 25.102  16.067  91.387  1.00 18.64 ? 873  ILE   B O     1 
ATOM   15431 C  CB    . ILE   B  1  875  ? 25.103  18.976  92.256  1.00 19.06 ? 873  ILE   B CB    1 
ATOM   15432 C  CG1   . ILE   B  1  875  ? 24.610  20.052  93.228  1.00 24.14 ? 873  ILE   B CG1   1 
ATOM   15433 C  CG2   . ILE   B  1  875  ? 25.856  19.568  91.062  1.00 20.48 ? 873  ILE   B CG2   1 
ATOM   15434 C  CD1   . ILE   B  1  875  ? 25.648  20.468  94.239  1.00 27.87 ? 873  ILE   B CD1   1 
ATOM   15435 N  N     . GLY   B  1  876  ? 24.189  17.063  89.588  1.00 15.46 ? 874  GLY   B N     1 
ATOM   15436 C  CA    . GLY   B  1  876  ? 24.713  16.031  88.723  1.00 15.86 ? 874  GLY   B CA    1 
ATOM   15437 C  C     . GLY   B  1  876  ? 24.170  16.142  87.316  1.00 15.52 ? 874  GLY   B C     1 
ATOM   15438 O  O     . GLY   B  1  876  ? 23.548  17.135  86.937  1.00 16.36 ? 874  GLY   B O     1 
ATOM   15439 N  N     . ARG   B  1  877  ? 24.449  15.090  86.548  1.00 17.61 ? 875  ARG   B N     1 
ATOM   15440 C  CA    . ARG   B  1  877  ? 23.972  15.018  85.177  1.00 16.24 ? 875  ARG   B CA    1 
ATOM   15441 C  C     . ARG   B  1  877  ? 22.455  15.005  85.193  1.00 16.35 ? 875  ARG   B C     1 
ATOM   15442 O  O     . ARG   B  1  877  ? 21.842  14.271  85.968  1.00 17.63 ? 875  ARG   B O     1 
ATOM   15443 C  CB    . ARG   B  1  877  ? 24.519  13.758  84.511  1.00 19.53 ? 875  ARG   B CB    1 
ATOM   15444 C  CG    . ARG   B  1  877  ? 24.464  13.819  83.007  1.00 20.83 ? 875  ARG   B CG    1 
ATOM   15445 C  CD    . ARG   B  1  877  ? 25.131  12.604  82.415  1.00 26.08 ? 875  ARG   B CD    1 
ATOM   15446 N  NE    . ARG   B  1  877  ? 24.249  11.452  82.370  1.00 23.72 ? 875  ARG   B NE    1 
ATOM   15447 C  CZ    . ARG   B  1  877  ? 24.559  10.318  81.760  1.00 29.52 ? 875  ARG   B CZ    1 
ATOM   15448 N  NH1   . ARG   B  1  877  ? 25.761  10.128  81.231  1.00 27.19 ? 875  ARG   B NH1   1 
ATOM   15449 N  NH2   . ARG   B  1  877  ? 23.642  9.358   81.666  1.00 30.36 ? 875  ARG   B NH2   1 
ATOM   15450 N  N     . THR   B  1  878  ? 21.844  15.811  84.332  1.00 15.29 ? 876  THR   B N     1 
ATOM   15451 C  CA    . THR   B  1  878  ? 20.444  16.180  84.511  1.00 16.83 ? 876  THR   B CA    1 
ATOM   15452 C  C     . THR   B  1  878  ? 19.444  15.196  83.912  1.00 15.66 ? 876  THR   B C     1 
ATOM   15453 O  O     . THR   B  1  878  ? 18.242  15.485  83.904  1.00 17.02 ? 876  THR   B O     1 
ATOM   15454 C  CB    . THR   B  1  878  ? 20.210  17.576  83.950  1.00 16.25 ? 876  THR   B CB    1 
ATOM   15455 O  OG1   . THR   B  1  878  ? 20.743  17.635  82.624  1.00 19.09 ? 876  THR   B OG1   1 
ATOM   15456 C  CG2   . THR   B  1  878  ? 20.903  18.610  84.818  1.00 19.53 ? 876  THR   B CG2   1 
ATOM   15457 N  N     . ASP   B  1  879  ? 19.886  14.040  83.429  1.00 15.29 ? 877  ASP   B N     1 
ATOM   15458 C  CA    . ASP   B  1  879  ? 18.975  13.045  82.884  1.00 17.07 ? 877  ASP   B CA    1 
ATOM   15459 C  C     . ASP   B  1  879  ? 18.401  12.135  83.956  1.00 17.23 ? 877  ASP   B C     1 
ATOM   15460 O  O     . ASP   B  1  879  ? 18.063  10.981  83.676  1.00 18.46 ? 877  ASP   B O     1 
ATOM   15461 C  CB    . ASP   B  1  879  ? 19.646  12.253  81.763  1.00 19.44 ? 877  ASP   B CB    1 
ATOM   15462 C  CG    . ASP   B  1  879  ? 20.824  11.430  82.257  1.00 21.22 ? 877  ASP   B CG    1 
ATOM   15463 O  OD1   . ASP   B  1  879  ? 21.514  11.850  83.215  1.00 24.41 ? 877  ASP   B OD1   1 
ATOM   15464 O  OD2   . ASP   B  1  879  ? 21.059  10.362  81.685  1.00 21.65 ? 877  ASP   B OD2   1 
ATOM   15465 N  N     . ARG   B  1  880  ? 18.298  12.630  85.183  1.00 18.12 ? 878  ARG   B N     1 
ATOM   15466 C  CA    . ARG   B  1  880  ? 17.602  11.956  86.270  1.00 18.75 ? 878  ARG   B CA    1 
ATOM   15467 C  C     . ARG   B  1  880  ? 16.679  12.972  86.908  1.00 15.52 ? 878  ARG   B C     1 
ATOM   15468 O  O     . ARG   B  1  880  ? 17.096  14.104  87.181  1.00 16.99 ? 878  ARG   B O     1 
ATOM   15469 C  CB    . ARG   B  1  880  ? 18.577  11.451  87.339  1.00 20.57 ? 878  ARG   B CB    1 
ATOM   15470 C  CG    . ARG   B  1  880  ? 19.411  10.238  86.968  1.00 25.71 ? 878  ARG   B CG    1 
ATOM   15471 C  CD    . ARG   B  1  880  ? 20.293  9.840   88.151  1.00 32.13 ? 878  ARG   B CD    1 
ATOM   15472 N  NE    . ARG   B  1  880  ? 21.309  8.868   87.770  1.00 46.50 ? 878  ARG   B NE    1 
ATOM   15473 C  CZ    . ARG   B  1  880  ? 21.230  7.569   88.018  1.00 51.50 ? 878  ARG   B CZ    1 
ATOM   15474 N  NH1   . ARG   B  1  880  ? 20.202  7.053   88.675  1.00 53.02 ? 878  ARG   B NH1   1 
ATOM   15475 N  NH2   . ARG   B  1  880  ? 22.206  6.768   87.599  1.00 48.35 ? 878  ARG   B NH2   1 
ATOM   15476 N  N     . LEU   B  1  881  ? 15.427  12.563  87.143  1.00 16.02 ? 879  LEU   B N     1 
ATOM   15477 C  CA    . LEU   B  1  881  ? 14.451  13.458  87.754  1.00 16.10 ? 879  LEU   B CA    1 
ATOM   15478 C  C     . LEU   B  1  881  ? 14.913  13.939  89.120  1.00 15.70 ? 879  LEU   B C     1 
ATOM   15479 O  O     . LEU   B  1  881  ? 14.589  15.060  89.528  1.00 16.78 ? 879  LEU   B O     1 
ATOM   15480 C  CB    . LEU   B  1  881  ? 13.115  12.741  87.877  1.00 17.36 ? 879  LEU   B CB    1 
ATOM   15481 C  CG    . LEU   B  1  881  ? 11.953  13.538  88.470  1.00 17.07 ? 879  LEU   B CG    1 
ATOM   15482 C  CD1   . LEU   B  1  881  ? 11.595  14.693  87.560  1.00 19.40 ? 879  LEU   B CD1   1 
ATOM   15483 C  CD2   . LEU   B  1  881  ? 10.760  12.622  88.697  1.00 20.03 ? 879  LEU   B CD2   1 
ATOM   15484 N  N     . SER   B  1  882  ? 15.706  13.134  89.822  1.00 15.23 ? 880  SER   B N     1 
ATOM   15485 C  CA    . SER   B  1  882  ? 16.155  13.512  91.150  1.00 15.30 ? 880  SER   B CA    1 
ATOM   15486 C  C     . SER   B  1  882  ? 17.219  14.601  91.147  1.00 16.89 ? 880  SER   B C     1 
ATOM   15487 O  O     . SER   B  1  882  ? 17.594  15.057  92.227  1.00 18.09 ? 880  SER   B O     1 
ATOM   15488 C  CB    . SER   B  1  882  ? 16.712  12.284  91.855  1.00 18.01 ? 880  SER   B CB    1 
ATOM   15489 O  OG    . SER   B  1  882  ? 17.912  11.879  91.224  1.00 20.34 ? 880  SER   B OG    1 
ATOM   15490 N  N     . VAL   B  1  883  ? 17.721  15.028  89.994  1.00 16.42 ? 881  VAL   B N     1 
ATOM   15491 C  CA    . VAL   B  1  883  ? 18.778  16.035  89.962  1.00 17.34 ? 881  VAL   B CA    1 
ATOM   15492 C  C     . VAL   B  1  883  ? 18.168  17.424  90.028  1.00 16.70 ? 881  VAL   B C     1 
ATOM   15493 O  O     . VAL   B  1  883  ? 17.256  17.755  89.261  1.00 18.89 ? 881  VAL   B O     1 
ATOM   15494 C  CB    . VAL   B  1  883  ? 19.684  15.871  88.733  1.00 17.75 ? 881  VAL   B CB    1 
ATOM   15495 C  CG1   . VAL   B  1  883  ? 20.599  17.079  88.596  1.00 18.40 ? 881  VAL   B CG1   1 
ATOM   15496 C  CG2   . VAL   B  1  883  ? 20.495  14.630  88.890  1.00 18.30 ? 881  VAL   B CG2   1 
ATOM   15497 N  N     . ASP   B  1  884  ? 18.661  18.234  90.953  1.00 16.51 ? 882  ASP   B N     1 
ATOM   15498 C  CA    . ASP   B  1  884  ? 18.179  19.589  91.156  1.00 17.15 ? 882  ASP   B CA    1 
ATOM   15499 C  C     . ASP   B  1  884  ? 19.027  20.632  90.454  1.00 19.62 ? 882  ASP   B C     1 
ATOM   15500 O  O     . ASP   B  1  884  ? 18.481  21.609  89.931  1.00 23.43 ? 882  ASP   B O     1 
ATOM   15501 C  CB    . ASP   B  1  884  ? 18.190  19.889  92.648  1.00 17.99 ? 882  ASP   B CB    1 
ATOM   15502 C  CG    . ASP   B  1  884  ? 17.343  18.914  93.427  1.00 18.80 ? 882  ASP   B CG    1 
ATOM   15503 O  OD1   . ASP   B  1  884  ? 16.131  18.805  93.111  1.00 18.09 ? 882  ASP   B OD1   1 
ATOM   15504 O  OD2   . ASP   B  1  884  ? 17.891  18.251  94.334  1.00 18.02 ? 882  ASP   B OD2   1 
ATOM   15505 N  N     . VAL   B  1  885  ? 20.345  20.458  90.453  1.00 17.37 ? 883  VAL   B N     1 
ATOM   15506 C  CA    . VAL   B  1  885  ? 21.278  21.450  89.937  1.00 17.00 ? 883  VAL   B CA    1 
ATOM   15507 C  C     . VAL   B  1  885  ? 22.167  20.740  88.931  1.00 16.29 ? 883  VAL   B C     1 
ATOM   15508 O  O     . VAL   B  1  885  ? 22.824  19.745  89.270  1.00 16.42 ? 883  VAL   B O     1 
ATOM   15509 C  CB    . VAL   B  1  885  ? 22.134  22.062  91.057  1.00 18.65 ? 883  VAL   B CB    1 
ATOM   15510 C  CG1   . VAL   B  1  885  ? 23.145  23.040  90.479  1.00 19.56 ? 883  VAL   B CG1   1 
ATOM   15511 C  CG2   . VAL   B  1  885  ? 21.253  22.755  92.100  1.00 23.48 ? 883  VAL   B CG2   1 
ATOM   15512 N  N     . GLY   B  1  886  ? 22.188  21.245  87.707  1.00 16.40 ? 884  GLY   B N     1 
ATOM   15513 C  CA    . GLY   B  1  886  ? 22.995  20.678  86.661  1.00 16.08 ? 884  GLY   B CA    1 
ATOM   15514 C  C     . GLY   B  1  886  ? 24.341  21.348  86.546  1.00 15.22 ? 884  GLY   B C     1 
ATOM   15515 O  O     . GLY   B  1  886  ? 24.758  22.130  87.405  1.00 14.87 ? 884  GLY   B O     1 
ATOM   15516 N  N     . PRO   B  1  887  ? 25.038  21.041  85.461  1.00 14.68 ? 885  PRO   B N     1 
ATOM   15517 C  CA    . PRO   B  1  887  ? 26.394  21.545  85.251  1.00 14.57 ? 885  PRO   B CA    1 
ATOM   15518 C  C     . PRO   B  1  887  ? 26.397  22.987  84.769  1.00 14.42 ? 885  PRO   B C     1 
ATOM   15519 O  O     . PRO   B  1  887  ? 25.394  23.535  84.311  1.00 14.10 ? 885  PRO   B O     1 
ATOM   15520 C  CB    . PRO   B  1  887  ? 26.896  20.643  84.120  1.00 14.43 ? 885  PRO   B CB    1 
ATOM   15521 C  CG    . PRO   B  1  887  ? 25.650  20.339  83.330  1.00 14.24 ? 885  PRO   B CG    1 
ATOM   15522 C  CD    . PRO   B  1  887  ? 24.593  20.147  84.380  1.00 16.21 ? 885  PRO   B CD    1 
ATOM   15523 N  N     . VAL   B  1  888  ? 27.578  23.576  84.830  1.00 13.93 ? 886  VAL   B N     1 
ATOM   15524 C  CA    . VAL   B  1  888  ? 27.816  24.791  84.076  1.00 15.36 ? 886  VAL   B CA    1 
ATOM   15525 C  C     . VAL   B  1  888  ? 28.195  24.414  82.650  1.00 14.56 ? 886  VAL   B C     1 
ATOM   15526 O  O     . VAL   B  1  888  ? 28.631  23.296  82.370  1.00 14.95 ? 886  VAL   B O     1 
ATOM   15527 C  CB    . VAL   B  1  888  ? 28.854  25.709  84.742  1.00 17.11 ? 886  VAL   B CB    1 
ATOM   15528 C  CG1   . VAL   B  1  888  ? 28.367  26.101  86.152  1.00 16.37 ? 886  VAL   B CG1   1 
ATOM   15529 C  CG2   . VAL   B  1  888  ? 30.191  25.055  84.792  1.00 23.08 ? 886  VAL   B CG2   1 
ATOM   15530 N  N     . ILE   B  1  889  ? 27.982  25.352  81.728  1.00 14.10 ? 887  ILE   B N     1 
ATOM   15531 C  CA    . ILE   B  1  889  ? 27.892  24.956  80.325  1.00 14.30 ? 887  ILE   B CA    1 
ATOM   15532 C  C     . ILE   B  1  889  ? 29.232  24.500  79.750  1.00 15.05 ? 887  ILE   B C     1 
ATOM   15533 O  O     . ILE   B  1  889  ? 29.272  23.617  78.886  1.00 15.23 ? 887  ILE   B O     1 
ATOM   15534 C  CB    . ILE   B  1  889  ? 27.254  26.078  79.496  1.00 13.88 ? 887  ILE   B CB    1 
ATOM   15535 C  CG1   . ILE   B  1  889  ? 27.016  25.607  78.054  1.00 14.88 ? 887  ILE   B CG1   1 
ATOM   15536 C  CG2   . ILE   B  1  889  ? 28.118  27.342  79.532  1.00 16.55 ? 887  ILE   B CG2   1 
ATOM   15537 C  CD1   . ILE   B  1  889  ? 26.112  24.413  77.934  1.00 16.51 ? 887  ILE   B CD1   1 
ATOM   15538 N  N     . THR   B  1  890  ? 30.339  25.094  80.176  1.00 13.38 ? 888  THR   B N     1 
ATOM   15539 C  CA    . THR   B  1  890  ? 31.636  24.770  79.600  1.00 16.48 ? 888  THR   B CA    1 
ATOM   15540 C  C     . THR   B  1  890  ? 32.697  24.874  80.673  1.00 15.96 ? 888  THR   B C     1 
ATOM   15541 O  O     . THR   B  1  890  ? 32.500  25.481  81.726  1.00 15.21 ? 888  THR   B O     1 
ATOM   15542 C  CB    . THR   B  1  890  ? 32.070  25.774  78.520  1.00 16.89 ? 888  THR   B CB    1 
ATOM   15543 O  OG1   . THR   B  1  890  ? 32.070  27.098  79.073  1.00 18.66 ? 888  THR   B OG1   1 
ATOM   15544 C  CG2   . THR   B  1  890  ? 31.154  25.719  77.295  1.00 18.07 ? 888  THR   B CG2   1 
ATOM   15545 N  N     . SER   B  1  891  ? 33.857  24.309  80.361  1.00 16.74 ? 889  SER   B N     1 
ATOM   15546 C  CA    A SER   B  1  891  ? 35.014  24.463  81.237  0.37 15.70 ? 889  SER   B CA    1 
ATOM   15547 C  CA    B SER   B  1  891  ? 34.993  24.467  81.258  0.37 15.69 ? 889  SER   B CA    1 
ATOM   15548 C  CA    C SER   B  1  891  ? 35.003  24.463  81.246  0.26 15.72 ? 889  SER   B CA    1 
ATOM   15549 C  C     . SER   B  1  891  ? 35.414  25.926  81.353  1.00 16.57 ? 889  SER   B C     1 
ATOM   15550 O  O     . SER   B  1  891  ? 35.832  26.379  82.421  1.00 17.31 ? 889  SER   B O     1 
ATOM   15551 C  CB    A SER   B  1  891  ? 36.190  23.643  80.705  0.37 18.82 ? 889  SER   B CB    1 
ATOM   15552 C  CB    B SER   B  1  891  ? 36.160  23.595  80.796  0.37 18.82 ? 889  SER   B CB    1 
ATOM   15553 C  CB    C SER   B  1  891  ? 36.169  23.602  80.760  0.26 18.82 ? 889  SER   B CB    1 
ATOM   15554 O  OG    A SER   B  1  891  ? 35.929  22.257  80.787  0.37 20.14 ? 889  SER   B OG    1 
ATOM   15555 O  OG    B SER   B  1  891  ? 36.651  24.040  79.548  0.37 18.72 ? 889  SER   B OG    1 
ATOM   15556 O  OG    C SER   B  1  891  ? 37.260  23.679  81.661  0.26 19.35 ? 889  SER   B OG    1 
ATOM   15557 N  N     . GLU   B  1  892  ? 35.296  26.681  80.254  1.00 16.07 ? 890  GLU   B N     1 
ATOM   15558 C  CA    . GLU   B  1  892  ? 35.636  28.098  80.297  1.00 18.25 ? 890  GLU   B CA    1 
ATOM   15559 C  C     . GLU   B  1  892  ? 34.723  28.834  81.261  1.00 16.93 ? 890  GLU   B C     1 
ATOM   15560 O  O     . GLU   B  1  892  ? 35.178  29.678  82.044  1.00 18.34 ? 890  GLU   B O     1 
ATOM   15561 C  CB    . GLU   B  1  892  ? 35.519  28.713  78.903  1.00 21.19 ? 890  GLU   B CB    1 
ATOM   15562 N  N     . ALA   B  1  893  ? 33.426  28.533  81.214  1.00 16.84 ? 891  ALA   B N     1 
ATOM   15563 C  CA    . ALA   B  1  893  ? 32.503  29.159  82.148  1.00 16.18 ? 891  ALA   B CA    1 
ATOM   15564 C  C     . ALA   B  1  893  ? 32.858  28.779  83.574  1.00 16.15 ? 891  ALA   B C     1 
ATOM   15565 O  O     . ALA   B  1  893  ? 32.893  29.634  84.469  1.00 17.06 ? 891  ALA   B O     1 
ATOM   15566 C  CB    . ALA   B  1  893  ? 31.073  28.734  81.823  1.00 18.21 ? 891  ALA   B CB    1 
ATOM   15567 N  N     . LYS   B  1  894  ? 33.125  27.492  83.800  1.00 15.54 ? 892  LYS   B N     1 
ATOM   15568 C  CA    A LYS   B  1  894  ? 33.517  27.037  85.129  0.36 16.10 ? 892  LYS   B CA    1 
ATOM   15569 C  CA    B LYS   B  1  894  ? 33.514  27.042  85.130  0.64 16.08 ? 892  LYS   B CA    1 
ATOM   15570 C  C     . LYS   B  1  894  ? 34.741  27.796  85.623  1.00 17.32 ? 892  LYS   B C     1 
ATOM   15571 O  O     . LYS   B  1  894  ? 34.777  28.271  86.760  1.00 16.86 ? 892  LYS   B O     1 
ATOM   15572 C  CB    A LYS   B  1  894  ? 33.782  25.532  85.103  0.36 16.53 ? 892  LYS   B CB    1 
ATOM   15573 C  CB    B LYS   B  1  894  ? 33.773  25.538  85.112  0.64 16.50 ? 892  LYS   B CB    1 
ATOM   15574 C  CG    A LYS   B  1  894  ? 34.343  24.964  86.392  0.36 17.59 ? 892  LYS   B CG    1 
ATOM   15575 C  CG    B LYS   B  1  894  ? 34.222  24.979  86.433  0.64 17.46 ? 892  LYS   B CG    1 
ATOM   15576 C  CD    A LYS   B  1  894  ? 34.645  23.476  86.240  0.36 20.50 ? 892  LYS   B CD    1 
ATOM   15577 C  CD    B LYS   B  1  894  ? 34.307  23.464  86.371  0.64 20.42 ? 892  LYS   B CD    1 
ATOM   15578 C  CE    A LYS   B  1  894  ? 35.478  22.945  87.397  0.36 24.05 ? 892  LYS   B CE    1 
ATOM   15579 C  CE    B LYS   B  1  894  ? 34.876  22.898  87.661  0.64 21.50 ? 892  LYS   B CE    1 
ATOM   15580 N  NZ    A LYS   B  1  894  ? 34.749  23.024  88.690  0.36 23.99 ? 892  LYS   B NZ    1 
ATOM   15581 N  NZ    B LYS   B  1  894  ? 34.750  21.423  87.732  0.64 28.43 ? 892  LYS   B NZ    1 
ATOM   15582 N  N     . ASP   B  1  895  ? 35.756  27.929  84.766  1.00 16.84 ? 893  ASP   B N     1 
ATOM   15583 C  CA    . ASP   B  1  895  ? 36.956  28.658  85.161  1.00 17.74 ? 893  ASP   B CA    1 
ATOM   15584 C  C     . ASP   B  1  895  ? 36.643  30.109  85.489  1.00 17.20 ? 893  ASP   B C     1 
ATOM   15585 O  O     . ASP   B  1  895  ? 37.228  30.684  86.415  1.00 18.62 ? 893  ASP   B O     1 
ATOM   15586 C  CB    . ASP   B  1  895  ? 37.993  28.593  84.042  1.00 20.61 ? 893  ASP   B CB    1 
ATOM   15587 C  CG    . ASP   B  1  895  ? 38.566  27.215  83.869  1.00 22.16 ? 893  ASP   B CG    1 
ATOM   15588 O  OD1   . ASP   B  1  895  ? 38.423  26.385  84.792  1.00 24.54 ? 893  ASP   B OD1   1 
ATOM   15589 O  OD2   . ASP   B  1  895  ? 39.177  26.972  82.809  1.00 25.62 ? 893  ASP   B OD2   1 
ATOM   15590 N  N     . ASN   B  1  896  ? 35.747  30.719  84.720  1.00 16.35 ? 894  ASN   B N     1 
ATOM   15591 C  CA    . ASN   B  1  896  ? 35.382  32.113  84.931  1.00 17.00 ? 894  ASN   B CA    1 
ATOM   15592 C  C     . ASN   B  1  896  ? 34.720  32.283  86.295  1.00 17.23 ? 894  ASN   B C     1 
ATOM   15593 O  O     . ASN   B  1  896  ? 35.087  33.166  87.083  1.00 17.56 ? 894  ASN   B O     1 
ATOM   15594 C  CB    . ASN   B  1  896  ? 34.459  32.512  83.776  1.00 18.72 ? 894  ASN   B CB    1 
ATOM   15595 C  CG    . ASN   B  1  896  ? 33.999  33.946  83.832  1.00 25.76 ? 894  ASN   B CG    1 
ATOM   15596 O  OD1   . ASN   B  1  896  ? 33.448  34.402  84.827  1.00 27.16 ? 894  ASN   B OD1   1 
ATOM   15597 N  ND2   . ASN   B  1  896  ? 34.183  34.660  82.727  1.00 30.64 ? 894  ASN   B ND2   1 
ATOM   15598 N  N     . ILE   B  1  897  ? 33.773  31.399  86.604  1.00 16.25 ? 895  ILE   B N     1 
ATOM   15599 C  CA    . ILE   B  1  897  ? 33.090  31.436  87.890  1.00 16.31 ? 895  ILE   B CA    1 
ATOM   15600 C  C     . ILE   B  1  897  ? 34.081  31.176  89.015  1.00 16.06 ? 895  ILE   B C     1 
ATOM   15601 O  O     . ILE   B  1  897  ? 34.094  31.873  90.034  1.00 17.18 ? 895  ILE   B O     1 
ATOM   15602 C  CB    . ILE   B  1  897  ? 31.956  30.399  87.895  1.00 16.19 ? 895  ILE   B CB    1 
ATOM   15603 C  CG1   . ILE   B  1  897  ? 30.909  30.734  86.830  1.00 15.58 ? 895  ILE   B CG1   1 
ATOM   15604 C  CG2   . ILE   B  1  897  ? 31.356  30.269  89.298  1.00 17.82 ? 895  ILE   B CG2   1 
ATOM   15605 C  CD1   . ILE   B  1  897  ? 30.112  29.516  86.375  1.00 16.30 ? 895  ILE   B CD1   1 
ATOM   15606 N  N     . GLU   B  1  898  ? 34.919  30.158  88.848  1.00 17.16 ? 896  GLU   B N     1 
ATOM   15607 C  CA    . GLU   B  1  898  ? 35.866  29.825  89.900  1.00 16.66 ? 896  GLU   B CA    1 
ATOM   15608 C  C     . GLU   B  1  898  ? 36.889  30.928  90.115  1.00 17.64 ? 896  GLU   B C     1 
ATOM   15609 O  O     . GLU   B  1  898  ? 37.338  31.132  91.248  1.00 17.24 ? 896  GLU   B O     1 
ATOM   15610 C  CB    . GLU   B  1  898  ? 36.524  28.484  89.603  1.00 18.18 ? 896  GLU   B CB    1 
ATOM   15611 C  CG    . GLU   B  1  898  ? 35.533  27.349  89.843  1.00 19.91 ? 896  GLU   B CG    1 
ATOM   15612 C  CD    . GLU   B  1  898  ? 36.094  25.992  89.539  1.00 27.16 ? 896  GLU   B CD    1 
ATOM   15613 O  OE1   . GLU   B  1  898  ? 37.186  25.923  88.945  1.00 28.23 ? 896  GLU   B OE1   1 
ATOM   15614 O  OE2   . GLU   B  1  898  ? 35.439  24.995  89.906  1.00 33.17 ? 896  GLU   B OE2   1 
ATOM   15615 N  N     . LYS   B  1  899  ? 37.246  31.670  89.064  1.00 16.81 ? 897  LYS   B N     1 
ATOM   15616 C  CA    . LYS   B  1  899  ? 38.180  32.772  89.251  1.00 17.80 ? 897  LYS   B CA    1 
ATOM   15617 C  C     . LYS   B  1  899  ? 37.572  33.829  90.152  1.00 16.15 ? 897  LYS   B C     1 
ATOM   15618 O  O     . LYS   B  1  899  ? 38.245  34.373  91.039  1.00 17.14 ? 897  LYS   B O     1 
ATOM   15619 C  CB    . LYS   B  1  899  ? 38.551  33.373  87.899  1.00 21.36 ? 897  LYS   B CB    1 
ATOM   15620 C  CG    . LYS   B  1  899  ? 39.498  34.546  88.033  1.00 22.50 ? 897  LYS   B CG    1 
ATOM   15621 C  CD    . LYS   B  1  899  ? 40.069  34.981  86.697  1.00 29.39 ? 897  LYS   B CD    1 
ATOM   15622 C  CE    . LYS   B  1  899  ? 39.087  35.812  85.913  1.00 29.10 ? 897  LYS   B CE    1 
ATOM   15623 N  NZ    . LYS   B  1  899  ? 39.790  36.680  84.918  1.00 29.16 ? 897  LYS   B NZ    1 
ATOM   15624 N  N     . HIS   B  1  900  ? 36.284  34.088  89.983  1.00 15.52 ? 898  HIS   B N     1 
ATOM   15625 C  CA    . HIS   B  1  900  ? 35.611  35.039  90.851  1.00 16.58 ? 898  HIS   B CA    1 
ATOM   15626 C  C     . HIS   B  1  900  ? 35.569  34.522  92.281  1.00 16.51 ? 898  HIS   B C     1 
ATOM   15627 O  O     . HIS   B  1  900  ? 35.872  35.258  93.228  1.00 16.52 ? 898  HIS   B O     1 
ATOM   15628 C  CB    . HIS   B  1  900  ? 34.200  35.288  90.342  1.00 15.54 ? 898  HIS   B CB    1 
ATOM   15629 C  CG    . HIS   B  1  900  ? 33.358  36.023  91.322  1.00 17.06 ? 898  HIS   B CG    1 
ATOM   15630 N  ND1   . HIS   B  1  900  ? 33.554  37.354  91.609  1.00 19.91 ? 898  HIS   B ND1   1 
ATOM   15631 C  CD2   . HIS   B  1  900  ? 32.335  35.609  92.106  1.00 16.73 ? 898  HIS   B CD2   1 
ATOM   15632 C  CE1   . HIS   B  1  900  ? 32.667  37.739  92.511  1.00 17.90 ? 898  HIS   B CE1   1 
ATOM   15633 N  NE2   . HIS   B  1  900  ? 31.923  36.697  92.836  1.00 16.93 ? 898  HIS   B NE2   1 
ATOM   15634 N  N     . ILE   B  1  901  ? 35.196  33.255  92.454  1.00 17.03 ? 899  ILE   B N     1 
ATOM   15635 C  CA    . ILE   B  1  901  ? 35.110  32.689  93.795  1.00 17.12 ? 899  ILE   B CA    1 
ATOM   15636 C  C     . ILE   B  1  901  ? 36.455  32.797  94.492  1.00 18.00 ? 899  ILE   B C     1 
ATOM   15637 O  O     . ILE   B  1  901  ? 36.546  33.211  95.655  1.00 17.86 ? 899  ILE   B O     1 
ATOM   15638 C  CB    . ILE   B  1  901  ? 34.626  31.234  93.723  1.00 16.51 ? 899  ILE   B CB    1 
ATOM   15639 C  CG1   . ILE   B  1  901  ? 33.193  31.178  93.198  1.00 15.05 ? 899  ILE   B CG1   1 
ATOM   15640 C  CG2   . ILE   B  1  901  ? 34.738  30.578  95.088  1.00 18.06 ? 899  ILE   B CG2   1 
ATOM   15641 C  CD1   . ILE   B  1  901  ? 32.724  29.762  92.902  1.00 18.89 ? 899  ILE   B CD1   1 
ATOM   15642 N  N     . GLU   B  1  902  ? 37.525  32.444  93.780  1.00 18.57 ? 900  GLU   B N     1 
ATOM   15643 C  CA    . GLU   B  1  902  ? 38.849  32.474  94.385  1.00 18.81 ? 900  GLU   B CA    1 
ATOM   15644 C  C     . GLU   B  1  902  ? 39.315  33.899  94.628  1.00 18.24 ? 900  GLU   B C     1 
ATOM   15645 O  O     . GLU   B  1  902  ? 40.058  34.143  95.584  1.00 19.79 ? 900  GLU   B O     1 
ATOM   15646 C  CB    . GLU   B  1  902  ? 39.848  31.699  93.526  1.00 20.16 ? 900  GLU   B CB    1 
ATOM   15647 C  CG    . GLU   B  1  902  ? 39.579  30.194  93.493  1.00 26.29 ? 900  GLU   B CG    1 
ATOM   15648 C  CD    . GLU   B  1  902  ? 39.349  29.601  94.884  1.00 30.85 ? 900  GLU   B CD    1 
ATOM   15649 O  OE1   . GLU   B  1  902  ? 40.210  29.800  95.769  1.00 30.63 ? 900  GLU   B OE1   1 
ATOM   15650 O  OE2   . GLU   B  1  902  ? 38.303  28.945  95.090  1.00 33.65 ? 900  GLU   B OE2   1 
ATOM   15651 N  N     . ARG   B  1  903  ? 38.900  34.847  93.788  1.00 19.63 ? 901  ARG   B N     1 
ATOM   15652 C  CA    . ARG   B  1  903  ? 39.217  36.245  94.056  1.00 20.33 ? 901  ARG   B CA    1 
ATOM   15653 C  C     . ARG   B  1  903  ? 38.563  36.700  95.352  1.00 22.40 ? 901  ARG   B C     1 
ATOM   15654 O  O     . ARG   B  1  903  ? 39.205  37.340  96.195  1.00 23.41 ? 901  ARG   B O     1 
ATOM   15655 C  CB    . ARG   B  1  903  ? 38.765  37.129  92.899  1.00 22.59 ? 901  ARG   B CB    1 
ATOM   15656 C  CG    . ARG   B  1  903  ? 39.281  38.548  93.020  1.00 30.56 ? 901  ARG   B CG    1 
ATOM   15657 C  CD    . ARG   B  1  903  ? 38.816  39.398  91.859  1.00 37.98 ? 901  ARG   B CD    1 
ATOM   15658 N  NE    . ARG   B  1  903  ? 37.662  40.209  92.221  1.00 43.17 ? 901  ARG   B NE    1 
ATOM   15659 C  CZ    . ARG   B  1  903  ? 37.746  41.436  92.717  1.00 37.53 ? 901  ARG   B CZ    1 
ATOM   15660 N  NH1   . ARG   B  1  903  ? 38.918  42.026  92.904  1.00 43.15 ? 901  ARG   B NH1   1 
ATOM   15661 N  NH2   . ARG   B  1  903  ? 36.629  42.087  93.028  1.00 45.35 ? 901  ARG   B NH2   1 
ATOM   15662 N  N     . MET   B  1  904  ? 37.286  36.364  95.531  1.00 19.60 ? 902  MET   B N     1 
ATOM   15663 C  CA    . MET   B  1  904  ? 36.593  36.726  96.760  1.00 18.61 ? 902  MET   B CA    1 
ATOM   15664 C  C     . MET   B  1  904  ? 37.237  36.050  97.956  1.00 22.51 ? 902  MET   B C     1 
ATOM   15665 O  O     . MET   B  1  904  ? 37.430  36.677  99.007  1.00 21.72 ? 902  MET   B O     1 
ATOM   15666 C  CB    . MET   B  1  904  ? 35.127  36.322  96.665  1.00 18.68 ? 902  MET   B CB    1 
ATOM   15667 C  CG    . MET   B  1  904  ? 34.370  37.021  95.550  1.00 19.24 ? 902  MET   B CG    1 
ATOM   15668 S  SD    . MET   B  1  904  ? 34.259  38.791  95.885  1.00 28.36 ? 902  MET   B SD    1 
ATOM   15669 C  CE    . MET   B  1  904  ? 35.411  39.435  94.678  1.00 32.37 ? 902  MET   B CE    1 
ATOM   15670 N  N     . ARG   B  1  905  ? 37.576  34.770  97.813  1.00 20.17 ? 903  ARG   B N     1 
ATOM   15671 C  CA    . ARG   B  1  905  ? 38.226  34.059  98.904  1.00 20.86 ? 903  ARG   B CA    1 
ATOM   15672 C  C     . ARG   B  1  905  ? 39.553  34.714  99.252  1.00 24.31 ? 903  ARG   B C     1 
ATOM   15673 O  O     . ARG   B  1  905  ? 39.860  34.934  100.431 1.00 24.23 ? 903  ARG   B O     1 
ATOM   15674 C  CB    . ARG   B  1  905  ? 38.442  32.599  98.512  1.00 23.99 ? 903  ARG   B CB    1 
ATOM   15675 C  CG    . ARG   B  1  905  ? 38.622  31.664  99.688  1.00 32.31 ? 903  ARG   B CG    1 
ATOM   15676 C  CD    . ARG   B  1  905  ? 39.076  30.293  99.225  1.00 32.43 ? 903  ARG   B CD    1 
ATOM   15677 N  NE    . ARG   B  1  905  ? 38.205  29.711  98.211  1.00 29.10 ? 903  ARG   B NE    1 
ATOM   15678 C  CZ    . ARG   B  1  905  ? 37.121  28.990  98.471  1.00 25.93 ? 903  ARG   B CZ    1 
ATOM   15679 N  NH1   . ARG   B  1  905  ? 36.679  28.826  99.709  1.00 30.99 ? 903  ARG   B NH1   1 
ATOM   15680 N  NH2   . ARG   B  1  905  ? 36.470  28.409  97.468  1.00 30.98 ? 903  ARG   B NH2   1 
ATOM   15681 N  N     . GLY   B  1  906  ? 40.334  35.075  98.236  1.00 22.55 ? 904  GLY   B N     1 
ATOM   15682 C  CA    . GLY   B  1  906  ? 41.635  35.673  98.490  1.00 25.37 ? 904  GLY   B CA    1 
ATOM   15683 C  C     . GLY   B  1  906  ? 41.559  37.055  99.096  1.00 24.90 ? 904  GLY   B C     1 
ATOM   15684 O  O     . GLY   B  1  906  ? 42.526  37.494  99.728  1.00 28.69 ? 904  GLY   B O     1 
ATOM   15685 N  N     . LEU   B  1  907  ? 40.439  37.747  98.918  1.00 25.08 ? 905  LEU   B N     1 
ATOM   15686 C  CA    . LEU   B  1  907  ? 40.196  39.036  99.548  1.00 29.55 ? 905  LEU   B CA    1 
ATOM   15687 C  C     . LEU   B  1  907  ? 39.660  38.908  100.964 1.00 26.88 ? 905  LEU   B C     1 
ATOM   15688 O  O     . LEU   B  1  907  ? 39.395  39.932  101.602 1.00 27.57 ? 905  LEU   B O     1 
ATOM   15689 C  CB    . LEU   B  1  907  ? 39.220  39.859  98.714  1.00 29.60 ? 905  LEU   B CB    1 
ATOM   15690 C  CG    . LEU   B  1  907  ? 39.750  40.325  97.359  1.00 35.84 ? 905  LEU   B CG    1 
ATOM   15691 C  CD1   . LEU   B  1  907  ? 38.700  41.157  96.645  1.00 38.50 ? 905  LEU   B CD1   1 
ATOM   15692 C  CD2   . LEU   B  1  907  ? 41.044  41.103  97.533  1.00 37.21 ? 905  LEU   B CD2   1 
ATOM   15693 N  N     . GLY   B  1  908  ? 39.503  37.689  101.465 1.00 24.79 ? 906  GLY   B N     1 
ATOM   15694 C  CA    . GLY   B  1  908  ? 39.063  37.476  102.826 1.00 24.92 ? 906  GLY   B CA    1 
ATOM   15695 C  C     . GLY   B  1  908  ? 37.572  37.346  103.011 1.00 28.60 ? 906  GLY   B C     1 
ATOM   15696 O  O     . GLY   B  1  908  ? 37.114  37.253  104.155 1.00 26.41 ? 906  GLY   B O     1 
ATOM   15697 N  N     . ARG   B  1  909  ? 36.797  37.334  101.932 1.00 22.19 ? 907  ARG   B N     1 
ATOM   15698 C  CA    . ARG   B  1  909  ? 35.363  37.177  102.072 1.00 21.42 ? 907  ARG   B CA    1 
ATOM   15699 C  C     . ARG   B  1  909  ? 35.037  35.747  102.472 1.00 21.75 ? 907  ARG   B C     1 
ATOM   15700 O  O     . ARG   B  1  909  ? 35.717  34.793  102.084 1.00 24.73 ? 907  ARG   B O     1 
ATOM   15701 C  CB    . ARG   B  1  909  ? 34.671  37.479  100.745 1.00 21.55 ? 907  ARG   B CB    1 
ATOM   15702 C  CG    . ARG   B  1  909  ? 34.880  38.896  100.236 1.00 26.25 ? 907  ARG   B CG    1 
ATOM   15703 C  CD    . ARG   B  1  909  ? 34.234  39.926  101.155 1.00 33.55 ? 907  ARG   B CD    1 
ATOM   15704 N  NE    . ARG   B  1  909  ? 34.421  41.289  100.664 1.00 38.43 ? 907  ARG   B NE    1 
ATOM   15705 C  CZ    . ARG   B  1  909  ? 35.391  42.102  101.058 1.00 45.33 ? 907  ARG   B CZ    1 
ATOM   15706 N  NH1   . ARG   B  1  909  ? 36.282  41.727  101.963 1.00 46.77 ? 907  ARG   B NH1   1 
ATOM   15707 N  NH2   . ARG   B  1  909  ? 35.466  43.324  100.536 1.00 47.72 ? 907  ARG   B NH2   1 
ATOM   15708 N  N     . LYS   B  1  910  ? 33.980  35.600  103.250 1.00 19.67 ? 908  LYS   B N     1 
ATOM   15709 C  CA    . LYS   B  1  910  ? 33.533  34.272  103.630 1.00 20.98 ? 908  LYS   B CA    1 
ATOM   15710 C  C     . LYS   B  1  910  ? 32.891  33.600  102.422 1.00 19.31 ? 908  LYS   B C     1 
ATOM   15711 O  O     . LYS   B  1  910  ? 31.946  34.133  101.824 1.00 20.06 ? 908  LYS   B O     1 
ATOM   15712 C  CB    . LYS   B  1  910  ? 32.543  34.359  104.786 1.00 23.70 ? 908  LYS   B CB    1 
ATOM   15713 C  CG    . LYS   B  1  910  ? 32.097  33.003  105.310 1.00 30.20 ? 908  LYS   B CG    1 
ATOM   15714 C  CD    . LYS   B  1  910  ? 31.050  33.151  106.406 1.00 34.56 ? 908  LYS   B CD    1 
ATOM   15715 C  CE    . LYS   B  1  910  ? 30.739  31.804  107.047 1.00 45.51 ? 908  LYS   B CE    1 
ATOM   15716 N  NZ    . LYS   B  1  910  ? 29.580  31.859  107.988 1.00 45.29 ? 908  LYS   B NZ    1 
ATOM   15717 N  N     . VAL   B  1  911  ? 33.411  32.436  102.060 1.00 17.96 ? 909  VAL   B N     1 
ATOM   15718 C  CA    . VAL   B  1  911  ? 32.956  31.670  100.911 1.00 17.93 ? 909  VAL   B CA    1 
ATOM   15719 C  C     . VAL   B  1  911  ? 32.601  30.277  101.400 1.00 19.51 ? 909  VAL   B C     1 
ATOM   15720 O  O     . VAL   B  1  911  ? 33.426  29.609  102.039 1.00 20.79 ? 909  VAL   B O     1 
ATOM   15721 C  CB    . VAL   B  1  911  ? 34.058  31.590  99.842  1.00 18.35 ? 909  VAL   B CB    1 
ATOM   15722 C  CG1   . VAL   B  1  911  ? 33.637  30.675  98.711  1.00 19.31 ? 909  VAL   B CG1   1 
ATOM   15723 C  CG2   . VAL   B  1  911  ? 34.421  32.985  99.340  1.00 19.74 ? 909  VAL   B CG2   1 
ATOM   15724 N  N     . GLU   B  1  912  ? 31.383  29.845  101.113 1.00 17.69 ? 910  GLU   B N     1 
ATOM   15725 C  CA    . GLU   B  1  912  ? 30.932  28.511  101.478 1.00 18.72 ? 910  GLU   B CA    1 
ATOM   15726 C  C     . GLU   B  1  912  ? 30.369  27.828  100.248 1.00 19.44 ? 910  GLU   B C     1 
ATOM   15727 O  O     . GLU   B  1  912  ? 29.604  28.430  99.494  1.00 18.57 ? 910  GLU   B O     1 
ATOM   15728 C  CB    . GLU   B  1  912  ? 29.854  28.577  102.552 1.00 22.64 ? 910  GLU   B CB    1 
ATOM   15729 C  CG    . GLU   B  1  912  ? 30.368  29.122  103.864 1.00 26.49 ? 910  GLU   B CG    1 
ATOM   15730 C  CD    . GLU   B  1  912  ? 29.251  29.374  104.846 1.00 37.26 ? 910  GLU   B CD    1 
ATOM   15731 O  OE1   . GLU   B  1  912  ? 28.783  28.402  105.472 1.00 39.24 ? 910  GLU   B OE1   1 
ATOM   15732 O  OE2   . GLU   B  1  912  ? 28.825  30.541  104.965 1.00 44.78 ? 910  GLU   B OE2   1 
ATOM   15733 N  N     . GLN   B  1  913  ? 30.752  26.572  100.046 1.00 17.63 ? 911  GLN   B N     1 
ATOM   15734 C  CA    . GLN   B  1  913  ? 30.239  25.781  98.942  1.00 18.47 ? 911  GLN   B CA    1 
ATOM   15735 C  C     . GLN   B  1  913  ? 29.605  24.523  99.492  1.00 22.13 ? 911  GLN   B C     1 
ATOM   15736 O  O     . GLN   B  1  913  ? 30.147  23.891  100.402 1.00 23.94 ? 911  GLN   B O     1 
ATOM   15737 C  CB    . GLN   B  1  913  ? 31.333  25.435  97.945  1.00 20.69 ? 911  GLN   B CB    1 
ATOM   15738 C  CG    . GLN   B  1  913  ? 31.928  26.682  97.330  1.00 21.50 ? 911  GLN   B CG    1 
ATOM   15739 C  CD    . GLN   B  1  913  ? 32.909  26.366  96.242  1.00 24.55 ? 911  GLN   B CD    1 
ATOM   15740 O  OE1   . GLN   B  1  913  ? 33.913  25.697  96.476  1.00 33.74 ? 911  GLN   B OE1   1 
ATOM   15741 N  NE2   . GLN   B  1  913  ? 32.623  26.829  95.035  1.00 22.36 ? 911  GLN   B NE2   1 
ATOM   15742 N  N     . ILE   B  1  914  ? 28.443  24.185  98.952  1.00 21.49 ? 912  ILE   B N     1 
ATOM   15743 C  CA    . ILE   B  1  914  ? 27.643  23.097  99.488  1.00 27.27 ? 912  ILE   B CA    1 
ATOM   15744 C  C     . ILE   B  1  914  ? 27.253  22.156  98.369  1.00 24.44 ? 912  ILE   B C     1 
ATOM   15745 O  O     . ILE   B  1  914  ? 26.636  22.583  97.392  1.00 23.13 ? 912  ILE   B O     1 
ATOM   15746 C  CB    . ILE   B  1  914  ? 26.397  23.643  100.217 1.00 27.37 ? 912  ILE   B CB    1 
ATOM   15747 C  CG1   . ILE   B  1  914  ? 26.809  24.458  101.450 1.00 29.87 ? 912  ILE   B CG1   1 
ATOM   15748 C  CG2   . ILE   B  1  914  ? 25.482  22.505  100.613 1.00 26.79 ? 912  ILE   B CG2   1 
ATOM   15749 C  CD1   . ILE   B  1  914  ? 25.706  25.353  102.012 1.00 25.59 ? 912  ILE   B CD1   1 
ATOM   15750 N  N     . LEU   B  1  916  ? 30.066  18.303  96.052  1.00 46.38 ? 914  LEU   B N     1 
ATOM   15751 C  CA    . LEU   B  1  916  ? 29.823  17.667  94.761  1.00 37.88 ? 914  LEU   B CA    1 
ATOM   15752 C  C     . LEU   B  1  916  ? 30.176  16.187  94.801  1.00 43.41 ? 914  LEU   B C     1 
ATOM   15753 O  O     . LEU   B  1  916  ? 31.207  15.803  95.354  1.00 38.86 ? 914  LEU   B O     1 
ATOM   15754 C  CB    . LEU   B  1  916  ? 30.655  18.327  93.659  1.00 41.40 ? 914  LEU   B CB    1 
ATOM   15755 C  CG    . LEU   B  1  916  ? 30.344  19.749  93.199  1.00 38.16 ? 914  LEU   B CG    1 
ATOM   15756 C  CD1   . LEU   B  1  916  ? 31.152  20.069  91.953  1.00 36.15 ? 914  LEU   B CD1   1 
ATOM   15757 C  CD2   . LEU   B  1  916  ? 28.866  19.907  92.934  1.00 37.93 ? 914  LEU   B CD2   1 
ATOM   15758 N  N     . ALA   B  1  917  ? 29.323  15.364  94.194  1.00 37.54 ? 915  ALA   B N     1 
ATOM   15759 C  CA    . ALA   B  1  917  ? 29.597  13.941  94.071  1.00 40.10 ? 915  ALA   B CA    1 
ATOM   15760 C  C     . ALA   B  1  917  ? 30.749  13.708  93.096  1.00 42.76 ? 915  ALA   B C     1 
ATOM   15761 O  O     . ALA   B  1  917  ? 31.045  14.539  92.231  1.00 39.96 ? 915  ALA   B O     1 
ATOM   15762 C  CB    . ALA   B  1  917  ? 28.353  13.205  93.573  1.00 35.53 ? 915  ALA   B CB    1 
ATOM   15763 N  N     . SER   B  1  918  ? 31.402  12.552  93.243  1.00 42.29 ? 916  SER   B N     1 
ATOM   15764 C  CA    . SER   B  1  918  ? 32.505  12.210  92.349  1.00 44.28 ? 916  SER   B CA    1 
ATOM   15765 C  C     . SER   B  1  918  ? 32.045  12.123  90.899  1.00 41.17 ? 916  SER   B C     1 
ATOM   15766 O  O     . SER   B  1  918  ? 32.819  12.430  89.983  1.00 37.49 ? 916  SER   B O     1 
ATOM   15767 C  CB    . SER   B  1  918  ? 33.144  10.891  92.785  1.00 43.69 ? 916  SER   B CB    1 
ATOM   15768 O  OG    . SER   B  1  918  ? 32.186  9.846   92.795  1.00 49.64 ? 916  SER   B OG    1 
ATOM   15769 N  N     . GLU   B  1  919  ? 30.786  11.725  90.675  1.00 37.90 ? 917  GLU   B N     1 
ATOM   15770 C  CA    . GLU   B  1  919  ? 30.250  11.615  89.323  1.00 39.65 ? 917  GLU   B CA    1 
ATOM   15771 C  C     . GLU   B  1  919  ? 30.326  12.927  88.561  1.00 38.53 ? 917  GLU   B C     1 
ATOM   15772 O  O     . GLU   B  1  919  ? 30.248  12.919  87.329  1.00 36.28 ? 917  GLU   B O     1 
ATOM   15773 C  CB    . GLU   B  1  919  ? 28.792  11.147  89.352  1.00 38.71 ? 917  GLU   B CB    1 
ATOM   15774 C  CG    . GLU   B  1  919  ? 28.606  9.667   89.659  1.00 50.42 ? 917  GLU   B CG    1 
ATOM   15775 C  CD    . GLU   B  1  919  ? 28.841  9.337   91.122  1.00 50.93 ? 917  GLU   B CD    1 
ATOM   15776 O  OE1   . GLU   B  1  919  ? 28.716  10.252  91.967  1.00 46.41 ? 917  GLU   B OE1   1 
ATOM   15777 O  OE2   . GLU   B  1  919  ? 29.155  8.165   91.425  1.00 50.24 ? 917  GLU   B OE2   1 
ATOM   15778 N  N     . THR   B  1  920  ? 30.469  14.053  89.260  1.00 33.49 ? 918  THR   B N     1 
ATOM   15779 C  CA    . THR   B  1  920  ? 30.552  15.332  88.568  1.00 29.09 ? 918  THR   B CA    1 
ATOM   15780 C  C     . THR   B  1  920  ? 31.856  15.488  87.792  1.00 30.77 ? 918  THR   B C     1 
ATOM   15781 O  O     . THR   B  1  920  ? 31.909  16.305  86.869  1.00 27.96 ? 918  THR   B O     1 
ATOM   15782 C  CB    . THR   B  1  920  ? 30.339  16.500  89.546  1.00 33.78 ? 918  THR   B CB    1 
ATOM   15783 O  OG1   . THR   B  1  920  ? 31.315  16.454  90.597  1.00 31.52 ? 918  THR   B OG1   1 
ATOM   15784 C  CG2   . THR   B  1  920  ? 28.939  16.462  90.147  1.00 25.57 ? 918  THR   B CG2   1 
ATOM   15785 N  N     . GLY   B  1  921  ? 32.893  14.710  88.126  1.00 29.87 ? 919  GLY   B N     1 
ATOM   15786 C  CA    . GLY   B  1  921  ? 34.206  14.887  87.522  1.00 29.87 ? 919  GLY   B CA    1 
ATOM   15787 C  C     . GLY   B  1  921  ? 34.232  14.745  86.011  1.00 28.38 ? 919  GLY   B C     1 
ATOM   15788 O  O     . GLY   B  1  921  ? 35.121  15.305  85.359  1.00 33.22 ? 919  GLY   B O     1 
ATOM   15789 N  N     . VAL   B  1  922  ? 33.281  14.003  85.438  1.00 21.96 ? 920  VAL   B N     1 
ATOM   15790 C  CA    . VAL   B  1  922  ? 33.206  13.823  83.989  1.00 21.04 ? 920  VAL   B CA    1 
ATOM   15791 C  C     . VAL   B  1  922  ? 32.554  14.997  83.275  1.00 21.42 ? 920  VAL   B C     1 
ATOM   15792 O  O     . VAL   B  1  922  ? 32.580  15.050  82.038  1.00 18.97 ? 920  VAL   B O     1 
ATOM   15793 C  CB    . VAL   B  1  922  ? 32.450  12.519  83.670  1.00 22.59 ? 920  VAL   B CB    1 
ATOM   15794 C  CG1   . VAL   B  1  922  ? 33.229  11.312  84.189  1.00 21.95 ? 920  VAL   B CG1   1 
ATOM   15795 C  CG2   . VAL   B  1  922  ? 31.052  12.549  84.275  1.00 24.45 ? 920  VAL   B CG2   1 
ATOM   15796 N  N     . GLY   B  1  923  ? 31.963  15.932  84.010  1.00 17.98 ? 921  GLY   B N     1 
ATOM   15797 C  CA    . GLY   B  1  923  ? 31.378  17.118  83.416  1.00 18.94 ? 921  GLY   B CA    1 
ATOM   15798 C  C     . GLY   B  1  923  ? 31.930  18.364  84.070  1.00 19.38 ? 921  GLY   B C     1 
ATOM   15799 O  O     . GLY   B  1  923  ? 32.911  18.289  84.816  1.00 20.44 ? 921  GLY   B O     1 
ATOM   15800 N  N     . THR   B  1  924  ? 31.323  19.511  83.822  1.00 16.17 ? 922  THR   B N     1 
ATOM   15801 C  CA    . THR   B  1  924  ? 31.807  20.779  84.364  1.00 15.94 ? 922  THR   B CA    1 
ATOM   15802 C  C     . THR   B  1  924  ? 30.757  21.287  85.342  1.00 16.66 ? 922  THR   B C     1 
ATOM   15803 O  O     . THR   B  1  924  ? 29.717  21.795  84.929  1.00 16.76 ? 922  THR   B O     1 
ATOM   15804 C  CB    . THR   B  1  924  ? 32.055  21.788  83.249  1.00 15.08 ? 922  THR   B CB    1 
ATOM   15805 O  OG1   . THR   B  1  924  ? 30.916  21.826  82.394  1.00 16.77 ? 922  THR   B OG1   1 
ATOM   15806 C  CG2   . THR   B  1  924  ? 33.257  21.364  82.417  1.00 17.75 ? 922  THR   B CG2   1 
ATOM   15807 N  N     . PHE   B  1  925  ? 31.023  21.137  86.634  1.00 16.27 ? 923  PHE   B N     1 
ATOM   15808 C  CA    . PHE   B  1  925  ? 30.094  21.542  87.673  1.00 16.47 ? 923  PHE   B CA    1 
ATOM   15809 C  C     . PHE   B  1  925  ? 30.753  22.533  88.609  1.00 16.16 ? 923  PHE   B C     1 
ATOM   15810 O  O     . PHE   B  1  925  ? 31.946  22.434  88.910  1.00 17.31 ? 923  PHE   B O     1 
ATOM   15811 C  CB    . PHE   B  1  925  ? 29.636  20.345  88.504  1.00 16.22 ? 923  PHE   B CB    1 
ATOM   15812 C  CG    . PHE   B  1  925  ? 28.768  19.383  87.758  1.00 16.36 ? 923  PHE   B CG    1 
ATOM   15813 C  CD1   . PHE   B  1  925  ? 29.334  18.407  86.966  1.00 16.82 ? 923  PHE   B CD1   1 
ATOM   15814 C  CD2   . PHE   B  1  925  ? 27.386  19.447  87.858  1.00 15.60 ? 923  PHE   B CD2   1 
ATOM   15815 C  CE1   . PHE   B  1  925  ? 28.545  17.504  86.271  1.00 17.78 ? 923  PHE   B CE1   1 
ATOM   15816 C  CE2   . PHE   B  1  925  ? 26.584  18.547  87.160  1.00 16.07 ? 923  PHE   B CE2   1 
ATOM   15817 C  CZ    . PHE   B  1  925  ? 27.174  17.564  86.381  1.00 15.98 ? 923  PHE   B CZ    1 
ATOM   15818 N  N     . VAL   B  1  926  ? 29.947  23.478  89.078  1.00 15.82 ? 924  VAL   B N     1 
ATOM   15819 C  CA    . VAL   B  1  926  ? 30.290  24.353  90.184  1.00 16.78 ? 924  VAL   B CA    1 
ATOM   15820 C  C     . VAL   B  1  926  ? 29.177  24.189  91.213  1.00 15.56 ? 924  VAL   B C     1 
ATOM   15821 O  O     . VAL   B  1  926  ? 28.006  24.285  90.852  1.00 15.55 ? 924  VAL   B O     1 
ATOM   15822 C  CB    . VAL   B  1  926  ? 30.389  25.825  89.746  1.00 15.73 ? 924  VAL   B CB    1 
ATOM   15823 C  CG1   . VAL   B  1  926  ? 30.632  26.726  90.946  1.00 16.55 ? 924  VAL   B CG1   1 
ATOM   15824 C  CG2   . VAL   B  1  926  ? 31.503  25.988  88.724  1.00 18.48 ? 924  VAL   B CG2   1 
ATOM   15825 N  N     . PRO   B  1  927  ? 29.483  23.907  92.470  1.00 18.33 ? 925  PRO   B N     1 
ATOM   15826 C  CA    . PRO   B  1  927  ? 28.422  23.726  93.440  1.00 17.83 ? 925  PRO   B CA    1 
ATOM   15827 C  C     . PRO   B  1  927  ? 27.853  25.068  93.848  1.00 16.37 ? 925  PRO   B C     1 
ATOM   15828 O  O     . PRO   B  1  927  ? 28.533  26.101  93.726  1.00 16.82 ? 925  PRO   B O     1 
ATOM   15829 C  CB    . PRO   B  1  927  ? 29.147  23.075  94.623  1.00 20.59 ? 925  PRO   B CB    1 
ATOM   15830 C  CG    . PRO   B  1  927  ? 30.515  23.648  94.559  1.00 18.90 ? 925  PRO   B CG    1 
ATOM   15831 C  CD    . PRO   B  1  927  ? 30.816  23.812  93.080  1.00 19.77 ? 925  PRO   B CD    1 
ATOM   15832 N  N     . PRO   B  1  928  ? 26.617  25.084  94.338  1.00 16.99 ? 926  PRO   B N     1 
ATOM   15833 C  CA    . PRO   B  1  928  ? 26.075  26.295  94.954  1.00 17.13 ? 926  PRO   B CA    1 
ATOM   15834 C  C     . PRO   B  1  928  ? 27.065  26.906  95.932  1.00 16.79 ? 926  PRO   B C     1 
ATOM   15835 O  O     . PRO   B  1  928  ? 27.619  26.230  96.813  1.00 16.88 ? 926  PRO   B O     1 
ATOM   15836 C  CB    . PRO   B  1  928  ? 24.819  25.787  95.671  1.00 18.18 ? 926  PRO   B CB    1 
ATOM   15837 C  CG    . PRO   B  1  928  ? 24.374  24.632  94.834  1.00 20.82 ? 926  PRO   B CG    1 
ATOM   15838 C  CD    . PRO   B  1  928  ? 25.642  23.981  94.327  1.00 19.39 ? 926  PRO   B CD    1 
ATOM   15839 N  N     . THR   B  1  929  ? 27.286  28.196  95.766  1.00 16.35 ? 927  THR   B N     1 
ATOM   15840 C  CA    . THR   B  1  929  ? 28.310  28.925  96.484  1.00 15.42 ? 927  THR   B CA    1 
ATOM   15841 C  C     . THR   B  1  929  ? 27.674  30.164  97.081  1.00 15.31 ? 927  THR   B C     1 
ATOM   15842 O  O     . THR   B  1  929  ? 26.886  30.848  96.425  1.00 16.41 ? 927  THR   B O     1 
ATOM   15843 C  CB    . THR   B  1  929  ? 29.435  29.320  95.521  1.00 15.61 ? 927  THR   B CB    1 
ATOM   15844 O  OG1   . THR   B  1  929  ? 30.011  28.132  94.960  1.00 16.73 ? 927  THR   B OG1   1 
ATOM   15845 C  CG2   . THR   B  1  929  ? 30.521  30.122  96.232  1.00 16.81 ? 927  THR   B CG2   1 
ATOM   15846 N  N     . ILE   B  1  930  ? 28.002  30.437  98.336  1.00 15.73 ? 928  ILE   B N     1 
ATOM   15847 C  CA    . ILE   B  1  930  ? 27.519  31.612  99.045  1.00 16.92 ? 928  ILE   B CA    1 
ATOM   15848 C  C     . ILE   B  1  930  ? 28.729  32.413  99.481  1.00 17.21 ? 928  ILE   B C     1 
ATOM   15849 O  O     . ILE   B  1  930  ? 29.633  31.879  100.140 1.00 16.26 ? 928  ILE   B O     1 
ATOM   15850 C  CB    . ILE   B  1  930  ? 26.654  31.235  100.260 1.00 16.78 ? 928  ILE   B CB    1 
ATOM   15851 C  CG1   . ILE   B  1  930  ? 25.453  30.403  99.820  1.00 17.71 ? 928  ILE   B CG1   1 
ATOM   15852 C  CG2   . ILE   B  1  930  ? 26.198  32.498  100.977 1.00 18.41 ? 928  ILE   B CG2   1 
ATOM   15853 C  CD1   . ILE   B  1  930  ? 24.637  29.857  100.979 1.00 22.39 ? 928  ILE   B CD1   1 
ATOM   15854 N  N     . ILE   B  1  931  ? 28.751  33.685  99.113  1.00 16.79 ? 929  ILE   B N     1 
ATOM   15855 C  CA    . ILE   B  1  931  ? 29.856  34.575  99.417  1.00 15.31 ? 929  ILE   B CA    1 
ATOM   15856 C  C     . ILE   B  1  931  ? 29.299  35.762  100.174 1.00 17.01 ? 929  ILE   B C     1 
ATOM   15857 O  O     . ILE   B  1  931  ? 28.390  36.434  99.681  1.00 17.37 ? 929  ILE   B O     1 
ATOM   15858 C  CB    . ILE   B  1  931  ? 30.554  35.056  98.140  1.00 16.72 ? 929  ILE   B CB    1 
ATOM   15859 C  CG1   . ILE   B  1  931  ? 31.003  33.855  97.303  1.00 18.73 ? 929  ILE   B CG1   1 
ATOM   15860 C  CG2   . ILE   B  1  931  ? 31.724  35.963  98.509  1.00 16.73 ? 929  ILE   B CG2   1 
ATOM   15861 C  CD1   . ILE   B  1  931  ? 31.844  34.233  96.104  1.00 18.86 ? 929  ILE   B CD1   1 
ATOM   15862 N  N     . GLU   B  1  932  ? 29.837  36.037  101.357 1.00 16.20 ? 930  GLU   B N     1 
ATOM   15863 C  CA    . GLU   B  1  932  ? 29.381  37.190  102.112 1.00 17.67 ? 930  GLU   B CA    1 
ATOM   15864 C  C     . GLU   B  1  932  ? 30.168  38.411  101.677 1.00 17.50 ? 930  GLU   B C     1 
ATOM   15865 O  O     . GLU   B  1  932  ? 31.403  38.391  101.672 1.00 18.27 ? 930  GLU   B O     1 
ATOM   15866 C  CB    . GLU   B  1  932  ? 29.539  36.953  103.611 1.00 21.98 ? 930  GLU   B CB    1 
ATOM   15867 C  CG    . GLU   B  1  932  ? 28.648  35.841  104.086 1.00 24.67 ? 930  GLU   B CG    1 
ATOM   15868 C  CD    . GLU   B  1  932  ? 28.369  35.886  105.567 1.00 39.37 ? 930  GLU   B CD    1 
ATOM   15869 O  OE1   . GLU   B  1  932  ? 29.093  36.599  106.302 1.00 41.48 ? 930  GLU   B OE1   1 
ATOM   15870 O  OE2   . GLU   B  1  932  ? 27.420  35.199  105.993 1.00 33.38 ? 930  GLU   B OE2   1 
ATOM   15871 N  N     . LEU   B  1  933  ? 29.460  39.460  101.294 1.00 19.66 ? 931  LEU   B N     1 
ATOM   15872 C  CA    . LEU   B  1  933  ? 30.097  40.706  100.915 1.00 17.84 ? 931  LEU   B CA    1 
ATOM   15873 C  C     . LEU   B  1  933  ? 29.943  41.727  102.030 1.00 22.54 ? 931  LEU   B C     1 
ATOM   15874 O  O     . LEU   B  1  933  ? 28.976  41.700  102.793 1.00 25.36 ? 931  LEU   B O     1 
ATOM   15875 C  CB    . LEU   B  1  933  ? 29.461  41.272  99.651  1.00 19.84 ? 931  LEU   B CB    1 
ATOM   15876 C  CG    . LEU   B  1  933  ? 29.474  40.367  98.427  1.00 23.07 ? 931  LEU   B CG    1 
ATOM   15877 C  CD1   . LEU   B  1  933  ? 28.750  41.085  97.303  1.00 26.51 ? 931  LEU   B CD1   1 
ATOM   15878 C  CD2   . LEU   B  1  933  ? 30.902  40.009  98.040  1.00 29.74 ? 931  LEU   B CD2   1 
ATOM   15879 N  N     . GLU   B  1  934  ? 30.903  42.644  102.099 1.00 24.02 ? 932  GLU   B N     1 
ATOM   15880 C  CA    . GLU   B  1  934  ? 30.744  43.793  102.978 1.00 25.71 ? 932  GLU   B CA    1 
ATOM   15881 C  C     . GLU   B  1  934  ? 29.895  44.868  102.316 1.00 26.44 ? 932  GLU   B C     1 
ATOM   15882 O  O     . GLU   B  1  934  ? 29.134  45.570  102.987 1.00 30.37 ? 932  GLU   B O     1 
ATOM   15883 C  CB    . GLU   B  1  934  ? 32.115  44.354  103.360 1.00 30.89 ? 932  GLU   B CB    1 
ATOM   15884 N  N     . LYS   B  1  935  ? 29.999  44.995  100.998 1.00 24.59 ? 933  LYS   B N     1 
ATOM   15885 C  CA    . LYS   B  1  935  ? 29.285  46.028  100.274 1.00 24.28 ? 933  LYS   B CA    1 
ATOM   15886 C  C     . LYS   B  1  935  ? 29.011  45.486  98.885  1.00 21.78 ? 933  LYS   B C     1 
ATOM   15887 O  O     . LYS   B  1  935  ? 29.788  44.686  98.356  1.00 23.88 ? 933  LYS   B O     1 
ATOM   15888 C  CB    . LYS   B  1  935  ? 30.123  47.308  100.174 1.00 29.84 ? 933  LYS   B CB    1 
ATOM   15889 N  N     . LEU   B  1  936  ? 27.895  45.921  98.302  1.00 22.24 ? 934  LEU   B N     1 
ATOM   15890 C  CA    . LEU   B  1  936  ? 27.561  45.466  96.960  1.00 23.40 ? 934  LEU   B CA    1 
ATOM   15891 C  C     . LEU   B  1  936  ? 28.649  45.832  95.959  1.00 24.49 ? 934  LEU   B C     1 
ATOM   15892 O  O     . LEU   B  1  936  ? 28.891  45.082  95.007  1.00 23.78 ? 934  LEU   B O     1 
ATOM   15893 C  CB    . LEU   B  1  936  ? 26.217  46.045  96.537  1.00 25.11 ? 934  LEU   B CB    1 
ATOM   15894 C  CG    . LEU   B  1  936  ? 25.288  45.078  95.811  1.00 26.08 ? 934  LEU   B CG    1 
ATOM   15895 C  CD1   . LEU   B  1  936  ? 23.846  45.481  96.048  1.00 26.80 ? 934  LEU   B CD1   1 
ATOM   15896 C  CD2   . LEU   B  1  936  ? 25.613  45.060  94.342  1.00 27.95 ? 934  LEU   B CD2   1 
ATOM   15897 N  N     . SER   B  1  937  ? 29.327  46.959  96.167  1.00 21.28 ? 935  SER   B N     1 
ATOM   15898 C  CA    . SER   B  1  937  ? 30.391  47.363  95.260  1.00 24.02 ? 935  SER   B CA    1 
ATOM   15899 C  C     . SER   B  1  937  ? 31.579  46.409  95.271  1.00 24.41 ? 935  SER   B C     1 
ATOM   15900 O  O     . SER   B  1  937  ? 32.457  46.547  94.413  1.00 24.42 ? 935  SER   B O     1 
ATOM   15901 C  CB    . SER   B  1  937  ? 30.839  48.793  95.563  1.00 24.62 ? 935  SER   B CB    1 
ATOM   15902 O  OG    . SER   B  1  937  ? 31.301  48.904  96.895  1.00 28.59 ? 935  SER   B OG    1 
ATOM   15903 N  N     . ASP   B  1  938  ? 31.628  45.450  96.208  1.00 22.01 ? 936  ASP   B N     1 
ATOM   15904 C  CA    . ASP   B  1  938  ? 32.618  44.380  96.118  1.00 23.71 ? 936  ASP   B CA    1 
ATOM   15905 C  C     . ASP   B  1  938  ? 32.454  43.582  94.836  1.00 21.35 ? 936  ASP   B C     1 
ATOM   15906 O  O     . ASP   B  1  938  ? 33.409  42.964  94.360  1.00 24.75 ? 936  ASP   B O     1 
ATOM   15907 C  CB    . ASP   B  1  938  ? 32.470  43.402  97.287  1.00 27.92 ? 936  ASP   B CB    1 
ATOM   15908 C  CG    . ASP   B  1  938  ? 32.863  44.002  98.624  1.00 34.66 ? 936  ASP   B CG    1 
ATOM   15909 O  OD1   . ASP   B  1  938  ? 33.431  45.116  98.661  1.00 33.22 ? 936  ASP   B OD1   1 
ATOM   15910 O  OD2   . ASP   B  1  938  ? 32.587  43.343  99.649  1.00 39.56 ? 936  ASP   B OD2   1 
ATOM   15911 N  N     . LEU   B  1  939  ? 31.251  43.556  94.285  1.00 20.92 ? 937  LEU   B N     1 
ATOM   15912 C  CA    . LEU   B  1  939  ? 30.940  42.760  93.112  1.00 24.25 ? 937  LEU   B CA    1 
ATOM   15913 C  C     . LEU   B  1  939  ? 31.001  43.687  91.906  1.00 23.99 ? 937  LEU   B C     1 
ATOM   15914 O  O     . LEU   B  1  939  ? 30.268  44.682  91.853  1.00 30.57 ? 937  LEU   B O     1 
ATOM   15915 C  CB    . LEU   B  1  939  ? 29.538  42.178  93.288  1.00 22.79 ? 937  LEU   B CB    1 
ATOM   15916 C  CG    . LEU   B  1  939  ? 28.974  41.132  92.338  1.00 27.89 ? 937  LEU   B CG    1 
ATOM   15917 C  CD1   . LEU   B  1  939  ? 29.888  39.927  92.237  1.00 27.34 ? 937  LEU   B CD1   1 
ATOM   15918 C  CD2   . LEU   B  1  939  ? 27.626  40.729  92.884  1.00 22.99 ? 937  LEU   B CD2   1 
ATOM   15919 N  N     . GLN   B  1  940  ? 31.866  43.361  90.941  1.00 20.64 ? 938  GLN   B N     1 
ATOM   15920 C  CA    . GLN   B  1  940  ? 32.154  44.247  89.817  1.00 25.70 ? 938  GLN   B CA    1 
ATOM   15921 C  C     . GLN   B  1  940  ? 31.705  43.720  88.463  1.00 23.11 ? 938  GLN   B C     1 
ATOM   15922 O  O     . GLN   B  1  940  ? 31.794  44.456  87.475  1.00 23.72 ? 938  GLN   B O     1 
ATOM   15923 C  CB    . GLN   B  1  940  ? 33.658  44.557  89.744  1.00 32.32 ? 938  GLN   B CB    1 
ATOM   15924 N  N     . ARG   B  1  941  ? 31.235  42.482  88.378  1.00 18.94 ? 939  ARG   B N     1 
ATOM   15925 C  CA    . ARG   B  1  941  ? 30.851  41.919  87.097  1.00 19.24 ? 939  ARG   B CA    1 
ATOM   15926 C  C     . ARG   B  1  941  ? 29.775  40.879  87.345  1.00 16.43 ? 939  ARG   B C     1 
ATOM   15927 O  O     . ARG   B  1  941  ? 29.674  40.317  88.433  1.00 15.98 ? 939  ARG   B O     1 
ATOM   15928 C  CB    . ARG   B  1  941  ? 32.047  41.286  86.364  1.00 22.48 ? 939  ARG   B CB    1 
ATOM   15929 C  CG    . ARG   B  1  941  ? 32.644  40.056  87.046  1.00 20.86 ? 939  ARG   B CG    1 
ATOM   15930 C  CD    . ARG   B  1  941  ? 33.979  39.701  86.398  1.00 21.90 ? 939  ARG   B CD    1 
ATOM   15931 N  NE    . ARG   B  1  941  ? 34.574  38.489  86.952  1.00 22.62 ? 939  ARG   B NE    1 
ATOM   15932 C  CZ    . ARG   B  1  941  ? 34.353  37.264  86.491  1.00 21.85 ? 939  ARG   B CZ    1 
ATOM   15933 N  NH1   . ARG   B  1  941  ? 33.470  37.036  85.530  1.00 22.60 ? 939  ARG   B NH1   1 
ATOM   15934 N  NH2   . ARG   B  1  941  ? 35.054  36.246  86.988  1.00 22.04 ? 939  ARG   B NH2   1 
ATOM   15935 N  N     . GLU   B  1  942  ? 28.982  40.620  86.311  1.00 17.23 ? 940  GLU   B N     1 
ATOM   15936 C  CA    . GLU   B  1  942  ? 28.006  39.544  86.361  1.00 15.76 ? 940  GLU   B CA    1 
ATOM   15937 C  C     . GLU   B  1  942  ? 28.755  38.225  86.327  1.00 17.05 ? 940  GLU   B C     1 
ATOM   15938 O  O     . GLU   B  1  942  ? 29.522  37.964  85.398  1.00 20.98 ? 940  GLU   B O     1 
ATOM   15939 C  CB    . GLU   B  1  942  ? 27.071  39.646  85.156  1.00 17.12 ? 940  GLU   B CB    1 
ATOM   15940 C  CG    . GLU   B  1  942  ? 26.075  38.499  85.055  1.00 16.78 ? 940  GLU   B CG    1 
ATOM   15941 C  CD    . GLU   B  1  942  ? 25.351  38.478  83.719  1.00 16.79 ? 940  GLU   B CD    1 
ATOM   15942 O  OE1   . GLU   B  1  942  ? 26.029  38.658  82.688  1.00 20.03 ? 940  GLU   B OE1   1 
ATOM   15943 O  OE2   . GLU   B  1  942  ? 24.122  38.305  83.701  1.00 15.40 ? 940  GLU   B OE2   1 
ATOM   15944 N  N     . VAL   B  1  943  ? 28.562  37.411  87.350  1.00 14.34 ? 941  VAL   B N     1 
ATOM   15945 C  CA    . VAL   B  1  943  ? 29.182  36.098  87.440  1.00 14.80 ? 941  VAL   B CA    1 
ATOM   15946 C  C     . VAL   B  1  943  ? 28.089  35.082  87.164  1.00 15.80 ? 941  VAL   B C     1 
ATOM   15947 O  O     . VAL   B  1  943  ? 27.173  34.888  87.973  1.00 14.57 ? 941  VAL   B O     1 
ATOM   15948 C  CB    . VAL   B  1  943  ? 29.848  35.875  88.804  1.00 16.62 ? 941  VAL   B CB    1 
ATOM   15949 C  CG1   . VAL   B  1  943  ? 30.483  34.494  88.846  1.00 17.54 ? 941  VAL   B CG1   1 
ATOM   15950 C  CG2   . VAL   B  1  943  ? 30.888  36.953  89.052  1.00 20.96 ? 941  VAL   B CG2   1 
ATOM   15951 N  N     . PHE   B  1  944  ? 28.177  34.445  86.004  1.00 15.23 ? 942  PHE   B N     1 
ATOM   15952 C  CA    . PHE   B  1  944  ? 27.052  33.711  85.443  1.00 14.65 ? 942  PHE   B CA    1 
ATOM   15953 C  C     . PHE   B  1  944  ? 27.156  32.252  85.873  1.00 14.31 ? 942  PHE   B C     1 
ATOM   15954 O  O     . PHE   B  1  944  ? 27.493  31.351  85.112  1.00 16.21 ? 942  PHE   B O     1 
ATOM   15955 C  CB    . PHE   B  1  944  ? 27.046  33.879  83.929  1.00 14.75 ? 942  PHE   B CB    1 
ATOM   15956 C  CG    . PHE   B  1  944  ? 25.714  33.628  83.298  1.00 14.32 ? 942  PHE   B CG    1 
ATOM   15957 C  CD1   . PHE   B  1  944  ? 24.671  34.532  83.448  1.00 14.42 ? 942  PHE   B CD1   1 
ATOM   15958 C  CD2   . PHE   B  1  944  ? 25.506  32.483  82.540  1.00 14.34 ? 942  PHE   B CD2   1 
ATOM   15959 C  CE1   . PHE   B  1  944  ? 23.452  34.301  82.861  1.00 15.67 ? 942  PHE   B CE1   1 
ATOM   15960 C  CE2   . PHE   B  1  944  ? 24.267  32.247  81.936  1.00 15.12 ? 942  PHE   B CE2   1 
ATOM   15961 C  CZ    . PHE   B  1  944  ? 23.243  33.161  82.110  1.00 16.38 ? 942  PHE   B CZ    1 
ATOM   15962 N  N     . GLY   B  1  945  ? 26.880  32.035  87.148  1.00 13.68 ? 943  GLY   B N     1 
ATOM   15963 C  CA    . GLY   B  1  945  ? 26.999  30.724  87.720  1.00 16.04 ? 943  GLY   B CA    1 
ATOM   15964 C  C     . GLY   B  1  945  ? 26.304  30.686  89.055  1.00 15.23 ? 943  GLY   B C     1 
ATOM   15965 O  O     . GLY   B  1  945  ? 25.617  31.631  89.450  1.00 15.07 ? 943  GLY   B O     1 
ATOM   15966 N  N     . PRO   B  1  946  ? 26.474  29.592  89.783  1.00 14.35 ? 944  PRO   B N     1 
ATOM   15967 C  CA    . PRO   B  1  946  ? 25.673  29.380  91.003  1.00 14.27 ? 944  PRO   B CA    1 
ATOM   15968 C  C     . PRO   B  1  946  ? 26.330  30.028  92.215  1.00 13.85 ? 944  PRO   B C     1 
ATOM   15969 O  O     . PRO   B  1  946  ? 26.700  29.363  93.179  1.00 16.34 ? 944  PRO   B O     1 
ATOM   15970 C  CB    . PRO   B  1  946  ? 25.631  27.854  91.102  1.00 14.99 ? 944  PRO   B CB    1 
ATOM   15971 C  CG    . PRO   B  1  946  ? 26.972  27.442  90.572  1.00 15.85 ? 944  PRO   B CG    1 
ATOM   15972 C  CD    . PRO   B  1  946  ? 27.272  28.407  89.432  1.00 14.44 ? 944  PRO   B CD    1 
ATOM   15973 N  N     . VAL   B  1  947  ? 26.500  31.339  92.146  1.00 14.75 ? 945  VAL   B N     1 
ATOM   15974 C  CA    . VAL   B  1  947  ? 27.254  32.078  93.140  1.00 14.10 ? 945  VAL   B CA    1 
ATOM   15975 C  C     . VAL   B  1  947  ? 26.345  33.156  93.688  1.00 16.52 ? 945  VAL   B C     1 
ATOM   15976 O  O     . VAL   B  1  947  ? 26.061  34.148  93.001  1.00 16.80 ? 945  VAL   B O     1 
ATOM   15977 C  CB    . VAL   B  1  947  ? 28.543  32.675  92.569  1.00 15.52 ? 945  VAL   B CB    1 
ATOM   15978 C  CG1   . VAL   B  1  947  ? 29.333  33.351  93.687  1.00 16.44 ? 945  VAL   B CG1   1 
ATOM   15979 C  CG2   . VAL   B  1  947  ? 29.368  31.595  91.890  1.00 17.04 ? 945  VAL   B CG2   1 
ATOM   15980 N  N     . LEU   B  1  948  ? 25.890  32.961  94.922  1.00 14.17 ? 946  LEU   B N     1 
ATOM   15981 C  CA    . LEU   B  1  948  ? 25.007  33.896  95.591  1.00 14.48 ? 946  LEU   B CA    1 
ATOM   15982 C  C     . LEU   B  1  948  ? 25.840  34.741  96.533  1.00 14.67 ? 946  LEU   B C     1 
ATOM   15983 O  O     . LEU   B  1  948  ? 26.581  34.205  97.360  1.00 16.51 ? 946  LEU   B O     1 
ATOM   15984 C  CB    . LEU   B  1  948  ? 23.973  33.132  96.409  1.00 14.40 ? 946  LEU   B CB    1 
ATOM   15985 C  CG    . LEU   B  1  948  ? 23.019  34.034  97.184  1.00 15.28 ? 946  LEU   B CG    1 
ATOM   15986 C  CD1   . LEU   B  1  948  ? 22.204  34.881  96.221  1.00 15.46 ? 946  LEU   B CD1   1 
ATOM   15987 C  CD2   . LEU   B  1  948  ? 22.131  33.167  98.042  1.00 18.73 ? 946  LEU   B CD2   1 
ATOM   15988 N  N     . HIS   B  1  949  ? 25.726  36.043  96.409  1.00 13.85 ? 947  HIS   B N     1 
ATOM   15989 C  CA    . HIS   B  1  949  ? 26.393  36.956  97.313  1.00 13.64 ? 947  HIS   B CA    1 
ATOM   15990 C  C     . HIS   B  1  949  ? 25.401  37.432  98.350  1.00 16.53 ? 947  HIS   B C     1 
ATOM   15991 O  O     . HIS   B  1  949  ? 24.220  37.603  98.059  1.00 17.63 ? 947  HIS   B O     1 
ATOM   15992 C  CB    . HIS   B  1  949  ? 26.957  38.122  96.520  1.00 15.85 ? 947  HIS   B CB    1 
ATOM   15993 C  CG    . HIS   B  1  949  ? 27.852  37.671  95.421  1.00 14.57 ? 947  HIS   B CG    1 
ATOM   15994 N  ND1   . HIS   B  1  949  ? 27.381  37.319  94.173  1.00 15.05 ? 947  HIS   B ND1   1 
ATOM   15995 C  CD2   . HIS   B  1  949  ? 29.183  37.442  95.403  1.00 15.59 ? 947  HIS   B CD2   1 
ATOM   15996 C  CE1   . HIS   B  1  949  ? 28.395  36.922  93.423  1.00 15.40 ? 947  HIS   B CE1   1 
ATOM   15997 N  NE2   . HIS   B  1  949  ? 29.497  36.984  94.146  1.00 16.24 ? 947  HIS   B NE2   1 
ATOM   15998 N  N     . VAL   B  1  950  ? 25.870  37.595  99.576  1.00 16.03 ? 948  VAL   B N     1 
ATOM   15999 C  CA    . VAL   B  1  950  ? 24.991  37.943  100.681 1.00 17.81 ? 948  VAL   B CA    1 
ATOM   16000 C  C     . VAL   B  1  950  ? 25.440  39.260  101.279 1.00 16.85 ? 948  VAL   B C     1 
ATOM   16001 O  O     . VAL   B  1  950  ? 26.624  39.442  101.586 1.00 16.98 ? 948  VAL   B O     1 
ATOM   16002 C  CB    . VAL   B  1  950  ? 24.947  36.837  101.745 1.00 17.08 ? 948  VAL   B CB    1 
ATOM   16003 C  CG1   . VAL   B  1  950  ? 24.170  37.328  102.966 1.00 20.02 ? 948  VAL   B CG1   1 
ATOM   16004 C  CG2   . VAL   B  1  950  ? 24.323  35.578  101.159 1.00 17.95 ? 948  VAL   B CG2   1 
ATOM   16005 N  N     . ILE   B  1  951  ? 24.496  40.167  101.444 1.00 15.40 ? 949  ILE   B N     1 
ATOM   16006 C  CA    . ILE   B  1  951  ? 24.703  41.438  102.118 1.00 16.84 ? 949  ILE   B CA    1 
ATOM   16007 C  C     . ILE   B  1  951  ? 23.737  41.486  103.285 1.00 15.55 ? 949  ILE   B C     1 
ATOM   16008 O  O     . ILE   B  1  951  ? 22.581  41.071  103.159 1.00 16.98 ? 949  ILE   B O     1 
ATOM   16009 C  CB    . ILE   B  1  951  ? 24.397  42.595  101.146 1.00 19.50 ? 949  ILE   B CB    1 
ATOM   16010 C  CG1   . ILE   B  1  951  ? 25.465  42.660  100.062 1.00 25.01 ? 949  ILE   B CG1   1 
ATOM   16011 C  CG2   . ILE   B  1  951  ? 24.276  43.930  101.895 1.00 26.82 ? 949  ILE   B CG2   1 
ATOM   16012 C  CD1   . ILE   B  1  951  ? 25.241  43.777  99.105  1.00 32.42 ? 949  ILE   B CD1   1 
ATOM   16013 N  N     . ARG   B  1  952  ? 24.210  41.954  104.424 1.00 16.33 ? 950  ARG   B N     1 
ATOM   16014 C  CA    A ARG   B  1  952  ? 23.350  42.203  105.568 0.60 17.27 ? 950  ARG   B CA    1 
ATOM   16015 C  CA    B ARG   B  1  952  ? 23.354  42.204  105.573 0.40 17.30 ? 950  ARG   B CA    1 
ATOM   16016 C  C     . ARG   B  1  952  ? 23.136  43.705  105.689 1.00 17.32 ? 950  ARG   B C     1 
ATOM   16017 O  O     . ARG   B  1  952  ? 24.059  44.492  105.476 1.00 21.98 ? 950  ARG   B O     1 
ATOM   16018 C  CB    A ARG   B  1  952  ? 23.999  41.661  106.844 0.60 17.77 ? 950  ARG   B CB    1 
ATOM   16019 C  CB    B ARG   B  1  952  ? 24.019  41.685  106.848 0.40 17.78 ? 950  ARG   B CB    1 
ATOM   16020 C  CG    A ARG   B  1  952  ? 24.255  40.165  106.785 0.60 19.76 ? 950  ARG   B CG    1 
ATOM   16021 C  CG    B ARG   B  1  952  ? 24.496  40.251  106.734 0.40 20.03 ? 950  ARG   B CG    1 
ATOM   16022 C  CD    A ARG   B  1  952  ? 25.415  39.771  107.684 0.60 23.40 ? 950  ARG   B CD    1 
ATOM   16023 C  CD    B ARG   B  1  952  ? 25.404  39.888  107.894 0.40 23.29 ? 950  ARG   B CD    1 
ATOM   16024 N  NE    A ARG   B  1  952  ? 25.770  38.364  107.540 0.60 25.06 ? 950  ARG   B NE    1 
ATOM   16025 N  NE    B ARG   B  1  952  ? 24.670  39.809  109.149 0.40 24.07 ? 950  ARG   B NE    1 
ATOM   16026 C  CZ    A ARG   B  1  952  ? 25.407  37.413  108.389 0.60 24.15 ? 950  ARG   B CZ    1 
ATOM   16027 C  CZ    B ARG   B  1  952  ? 24.347  38.675  109.755 0.40 24.10 ? 950  ARG   B CZ    1 
ATOM   16028 N  NH1   A ARG   B  1  952  ? 24.646  37.677  109.437 0.60 24.60 ? 950  ARG   B NH1   1 
ATOM   16029 N  NH1   B ARG   B  1  952  ? 24.682  37.500  109.247 0.40 24.30 ? 950  ARG   B NH1   1 
ATOM   16030 N  NH2   A ARG   B  1  952  ? 25.833  36.169  108.190 0.60 24.25 ? 950  ARG   B NH2   1 
ATOM   16031 N  NH2   B ARG   B  1  952  ? 23.675  38.722  110.903 0.40 21.56 ? 950  ARG   B NH2   1 
ATOM   16032 N  N     . TYR   B  1  953  ? 21.912  44.106  106.015 1.00 16.42 ? 951  TYR   B N     1 
ATOM   16033 C  CA    . TYR   B  1  953  ? 21.654  45.533  106.102 1.00 17.62 ? 951  TYR   B CA    1 
ATOM   16034 C  C     . TYR   B  1  953  ? 20.799  45.849  107.318 1.00 17.90 ? 951  TYR   B C     1 
ATOM   16035 O  O     . TYR   B  1  953  ? 20.002  45.024  107.772 1.00 18.89 ? 951  TYR   B O     1 
ATOM   16036 C  CB    . TYR   B  1  953  ? 20.984  46.068  104.822 1.00 17.65 ? 951  TYR   B CB    1 
ATOM   16037 C  CG    . TYR   B  1  953  ? 19.552  45.644  104.675 1.00 14.96 ? 951  TYR   B CG    1 
ATOM   16038 C  CD1   . TYR   B  1  953  ? 19.221  44.412  104.119 1.00 14.21 ? 951  TYR   B CD1   1 
ATOM   16039 C  CD2   . TYR   B  1  953  ? 18.519  46.470  105.100 1.00 14.93 ? 951  TYR   B CD2   1 
ATOM   16040 C  CE1   . TYR   B  1  953  ? 17.904  44.025  103.994 1.00 15.52 ? 951  TYR   B CE1   1 
ATOM   16041 C  CE2   . TYR   B  1  953  ? 17.206  46.084  104.974 1.00 17.83 ? 951  TYR   B CE2   1 
ATOM   16042 C  CZ    . TYR   B  1  953  ? 16.908  44.863  104.417 1.00 17.91 ? 951  TYR   B CZ    1 
ATOM   16043 O  OH    . TYR   B  1  953  ? 15.594  44.494  104.321 1.00 17.42 ? 951  TYR   B OH    1 
ATOM   16044 N  N     . ARG   B  1  954  ? 20.963  47.070  107.827 1.00 21.09 ? 952  ARG   B N     1 
ATOM   16045 C  CA    . ARG   B  1  954  ? 20.091  47.602  108.862 1.00 23.97 ? 952  ARG   B CA    1 
ATOM   16046 C  C     . ARG   B  1  954  ? 18.887  48.231  108.185 1.00 20.08 ? 952  ARG   B C     1 
ATOM   16047 O  O     . ARG   B  1  954  ? 19.025  48.888  107.149 1.00 19.45 ? 952  ARG   B O     1 
ATOM   16048 C  CB    . ARG   B  1  954  ? 20.820  48.672  109.677 1.00 22.89 ? 952  ARG   B CB    1 
ATOM   16049 N  N     . ARG   B  1  955  ? 17.701  48.034  108.776 1.00 21.81 ? 953  ARG   B N     1 
ATOM   16050 C  CA    . ARG   B  1  955  ? 16.478  48.526  108.147 1.00 23.64 ? 953  ARG   B CA    1 
ATOM   16051 C  C     . ARG   B  1  955  ? 16.539  50.026  107.874 1.00 23.94 ? 953  ARG   B C     1 
ATOM   16052 O  O     . ARG   B  1  955  ? 16.020  50.499  106.856 1.00 23.03 ? 953  ARG   B O     1 
ATOM   16053 C  CB    . ARG   B  1  955  ? 15.252  48.162  108.987 1.00 29.74 ? 953  ARG   B CB    1 
ATOM   16054 C  CG    . ARG   B  1  955  ? 13.912  48.598  108.384 1.00 32.21 ? 953  ARG   B CG    1 
ATOM   16055 C  CD    . ARG   B  1  955  ? 13.743  48.167  106.922 1.00 29.51 ? 953  ARG   B CD    1 
ATOM   16056 N  NE    . ARG   B  1  955  ? 12.452  48.583  106.386 1.00 32.11 ? 953  ARG   B NE    1 
ATOM   16057 C  CZ    . ARG   B  1  955  ? 12.145  49.829  106.045 1.00 34.28 ? 953  ARG   B CZ    1 
ATOM   16058 N  NH1   . ARG   B  1  955  ? 13.029  50.810  106.142 1.00 32.48 ? 953  ARG   B NH1   1 
ATOM   16059 N  NH2   . ARG   B  1  955  ? 10.917  50.097  105.599 1.00 29.13 ? 953  ARG   B NH2   1 
ATOM   16060 N  N     . ASP   B  1  956  ? 17.170  50.798  108.761 1.00 22.80 ? 954  ASP   B N     1 
ATOM   16061 C  CA    A ASP   B  1  956  ? 17.282  52.238  108.536 0.49 24.70 ? 954  ASP   B CA    1 
ATOM   16062 C  CA    B ASP   B  1  956  ? 17.240  52.233  108.505 0.51 24.70 ? 954  ASP   B CA    1 
ATOM   16063 C  C     . ASP   B  1  956  ? 18.130  52.577  107.319 1.00 25.33 ? 954  ASP   B C     1 
ATOM   16064 O  O     . ASP   B  1  956  ? 18.083  53.720  106.846 1.00 27.19 ? 954  ASP   B O     1 
ATOM   16065 C  CB    A ASP   B  1  956  ? 17.853  52.931  109.776 0.49 24.82 ? 954  ASP   B CB    1 
ATOM   16066 C  CB    B ASP   B  1  956  ? 17.593  53.039  109.767 0.51 24.69 ? 954  ASP   B CB    1 
ATOM   16067 C  CG    A ASP   B  1  956  ? 16.934  52.827  110.973 0.49 29.82 ? 954  ASP   B CG    1 
ATOM   16068 C  CG    B ASP   B  1  956  ? 18.940  52.664  110.372 0.51 23.69 ? 954  ASP   B CG    1 
ATOM   16069 O  OD1   A ASP   B  1  956  ? 15.706  52.724  110.773 0.49 31.79 ? 954  ASP   B OD1   1 
ATOM   16070 O  OD1   B ASP   B  1  956  ? 19.760  51.997  109.711 0.51 28.90 ? 954  ASP   B OD1   1 
ATOM   16071 O  OD2   A ASP   B  1  956  ? 17.441  52.849  112.114 0.49 31.36 ? 954  ASP   B OD2   1 
ATOM   16072 O  OD2   B ASP   B  1  956  ? 19.178  53.053  111.537 0.51 30.44 ? 954  ASP   B OD2   1 
ATOM   16073 N  N     . ASP   B  1  957  ? 18.904  51.619  106.817 1.00 20.83 ? 955  ASP   B N     1 
ATOM   16074 C  CA    . ASP   B  1  957  ? 19.745  51.803  105.646 1.00 22.86 ? 955  ASP   B CA    1 
ATOM   16075 C  C     . ASP   B  1  957  ? 19.090  51.282  104.376 1.00 19.11 ? 955  ASP   B C     1 
ATOM   16076 O  O     . ASP   B  1  957  ? 19.762  51.178  103.354 1.00 19.77 ? 955  ASP   B O     1 
ATOM   16077 C  CB    . ASP   B  1  957  ? 21.084  51.089  105.834 1.00 25.09 ? 955  ASP   B CB    1 
ATOM   16078 C  CG    . ASP   B  1  957  ? 21.983  51.781  106.831 1.00 33.43 ? 955  ASP   B CG    1 
ATOM   16079 O  OD1   . ASP   B  1  957  ? 21.840  53.010  107.009 1.00 33.11 ? 955  ASP   B OD1   1 
ATOM   16080 O  OD2   . ASP   B  1  957  ? 22.837  51.092  107.429 1.00 36.16 ? 955  ASP   B OD2   1 
ATOM   16081 N  N     . LEU   B  1  958  ? 17.801  50.941  104.425 1.00 18.08 ? 956  LEU   B N     1 
ATOM   16082 C  CA    . LEU   B  1  958  ? 17.150  50.335  103.266 1.00 16.75 ? 956  LEU   B CA    1 
ATOM   16083 C  C     . LEU   B  1  958  ? 17.263  51.218  102.032 1.00 18.06 ? 956  LEU   B C     1 
ATOM   16084 O  O     . LEU   B  1  958  ? 17.552  50.728  100.935 1.00 17.09 ? 956  LEU   B O     1 
ATOM   16085 C  CB    . LEU   B  1  958  ? 15.681  50.073  103.577 1.00 18.12 ? 956  LEU   B CB    1 
ATOM   16086 C  CG    . LEU   B  1  958  ? 14.844  49.498  102.434 1.00 16.97 ? 956  LEU   B CG    1 
ATOM   16087 C  CD1   . LEU   B  1  958  ? 15.428  48.181  101.961 1.00 19.50 ? 956  LEU   B CD1   1 
ATOM   16088 C  CD2   . LEU   B  1  958  ? 13.426  49.307  102.913 1.00 20.47 ? 956  LEU   B CD2   1 
ATOM   16089 N  N     . ASP   B  1  959  ? 17.029  52.518  102.182 1.00 17.06 ? 957  ASP   B N     1 
ATOM   16090 C  CA    . ASP   B  1  959  ? 17.064  53.387  101.013 1.00 15.24 ? 957  ASP   B CA    1 
ATOM   16091 C  C     . ASP   B  1  959  ? 18.452  53.414  100.390 1.00 16.09 ? 957  ASP   B C     1 
ATOM   16092 O  O     . ASP   B  1  959  ? 18.589  53.367  99.161  1.00 17.16 ? 957  ASP   B O     1 
ATOM   16093 C  CB    . ASP   B  1  959  ? 16.575  54.783  101.375 1.00 16.62 ? 957  ASP   B CB    1 
ATOM   16094 C  CG    . ASP   B  1  959  ? 16.141  55.560  100.167 1.00 19.24 ? 957  ASP   B CG    1 
ATOM   16095 O  OD1   . ASP   B  1  959  ? 15.412  54.987  99.331  1.00 18.47 ? 957  ASP   B OD1   1 
ATOM   16096 O  OD2   . ASP   B  1  959  ? 16.528  56.731  100.045 1.00 19.00 ? 957  ASP   B OD2   1 
ATOM   16097 N  N     . ARG   B  1  960  ? 19.490  53.469  101.222 1.00 16.24 ? 958  ARG   B N     1 
ATOM   16098 C  CA    . ARG   B  1  960  ? 20.852  53.419  100.715 1.00 16.71 ? 958  ARG   B CA    1 
ATOM   16099 C  C     . ARG   B  1  960  ? 21.134  52.078  100.061 1.00 16.83 ? 958  ARG   B C     1 
ATOM   16100 O  O     . ARG   B  1  960  ? 21.862  52.006  99.068  1.00 16.36 ? 958  ARG   B O     1 
ATOM   16101 C  CB    . ARG   B  1  960  ? 21.836  53.669  101.860 1.00 20.47 ? 958  ARG   B CB    1 
ATOM   16102 N  N     . LEU   B  1  961  ? 20.598  50.999  100.626 1.00 15.23 ? 959  LEU   B N     1 
ATOM   16103 C  CA    . LEU   B  1  961  ? 20.778  49.694  100.006 1.00 15.25 ? 959  LEU   B CA    1 
ATOM   16104 C  C     . LEU   B  1  961  ? 20.178  49.664  98.608  1.00 15.30 ? 959  LEU   B C     1 
ATOM   16105 O  O     . LEU   B  1  961  ? 20.774  49.100  97.682  1.00 16.02 ? 959  LEU   B O     1 
ATOM   16106 C  CB    . LEU   B  1  961  ? 20.151  48.605  100.873 1.00 14.78 ? 959  LEU   B CB    1 
ATOM   16107 C  CG    . LEU   B  1  961  ? 20.135  47.205  100.263 1.00 16.26 ? 959  LEU   B CG    1 
ATOM   16108 C  CD1   . LEU   B  1  961  ? 21.559  46.665  100.093 1.00 18.88 ? 959  LEU   B CD1   1 
ATOM   16109 C  CD2   . LEU   B  1  961  ? 19.278  46.254  101.074 1.00 18.45 ? 959  LEU   B CD2   1 
ATOM   16110 N  N     . VAL   B  1  962  ? 18.992  50.251  98.436  1.00 13.85 ? 960  VAL   B N     1 
ATOM   16111 C  CA    . VAL   B  1  962  ? 18.406  50.313  97.102  1.00 14.51 ? 960  VAL   B CA    1 
ATOM   16112 C  C     . VAL   B  1  962  ? 19.330  51.067  96.158  1.00 15.34 ? 960  VAL   B C     1 
ATOM   16113 O  O     . VAL   B  1  962  ? 19.525  50.659  95.009  1.00 15.22 ? 960  VAL   B O     1 
ATOM   16114 C  CB    . VAL   B  1  962  ? 16.997  50.922  97.155  1.00 15.89 ? 960  VAL   B CB    1 
ATOM   16115 C  CG1   . VAL   B  1  962  ? 16.499  51.196  95.751  1.00 16.96 ? 960  VAL   B CG1   1 
ATOM   16116 C  CG2   . VAL   B  1  962  ? 16.050  49.981  97.885  1.00 16.79 ? 960  VAL   B CG2   1 
ATOM   16117 N  N     . ASP   B  1  963  ? 19.924  52.170  96.629  1.00 15.30 ? 961  ASP   B N     1 
ATOM   16118 C  CA    . ASP   B  1  963  ? 20.925  52.867  95.822  1.00 16.90 ? 961  ASP   B CA    1 
ATOM   16119 C  C     . ASP   B  1  963  ? 22.063  51.943  95.438  1.00 16.33 ? 961  ASP   B C     1 
ATOM   16120 O  O     . ASP   B  1  963  ? 22.543  51.976  94.298  1.00 18.37 ? 961  ASP   B O     1 
ATOM   16121 C  CB    . ASP   B  1  963  ? 21.530  54.028  96.601  1.00 18.14 ? 961  ASP   B CB    1 
ATOM   16122 C  CG    . ASP   B  1  963  ? 20.588  55.150  96.784  1.00 22.68 ? 961  ASP   B CG    1 
ATOM   16123 O  OD1   . ASP   B  1  963  ? 19.590  55.212  96.046  1.00 23.11 ? 961  ASP   B OD1   1 
ATOM   16124 O  OD2   . ASP   B  1  963  ? 20.870  55.986  97.667  1.00 23.88 ? 961  ASP   B OD2   1 
ATOM   16125 N  N     . ASP   B  1  964  ? 22.541  51.139  96.392  1.00 15.10 ? 962  ASP   B N     1 
ATOM   16126 C  CA    . ASP   B  1  964  ? 23.648  50.232  96.116  1.00 16.60 ? 962  ASP   B CA    1 
ATOM   16127 C  C     . ASP   B  1  964  ? 23.267  49.232  95.043  1.00 17.23 ? 962  ASP   B C     1 
ATOM   16128 O  O     . ASP   B  1  964  ? 24.077  48.916  94.166  1.00 17.21 ? 962  ASP   B O     1 
ATOM   16129 C  CB    . ASP   B  1  964  ? 24.046  49.489  97.388  1.00 16.71 ? 962  ASP   B CB    1 
ATOM   16130 C  CG    . ASP   B  1  964  ? 24.681  50.389  98.417  1.00 20.74 ? 962  ASP   B CG    1 
ATOM   16131 O  OD1   . ASP   B  1  964  ? 25.012  51.550  98.088  1.00 21.34 ? 962  ASP   B OD1   1 
ATOM   16132 O  OD2   . ASP   B  1  964  ? 24.833  49.918  99.564  1.00 27.18 ? 962  ASP   B OD2   1 
ATOM   16133 N  N     . VAL   B  1  965  ? 22.032  48.733  95.085  1.00 14.40 ? 963  VAL   B N     1 
ATOM   16134 C  CA    . VAL   B  1  965  ? 21.580  47.826  94.039  1.00 13.47 ? 963  VAL   B CA    1 
ATOM   16135 C  C     . VAL   B  1  965  ? 21.568  48.547  92.698  1.00 14.91 ? 963  VAL   B C     1 
ATOM   16136 O  O     . VAL   B  1  965  ? 22.083  48.038  91.695  1.00 15.93 ? 963  VAL   B O     1 
ATOM   16137 C  CB    . VAL   B  1  965  ? 20.202  47.239  94.396  1.00 14.23 ? 963  VAL   B CB    1 
ATOM   16138 C  CG1   . VAL   B  1  965  ? 19.691  46.396  93.256  1.00 14.62 ? 963  VAL   B CG1   1 
ATOM   16139 C  CG2   . VAL   B  1  965  ? 20.291  46.397  95.658  1.00 16.65 ? 963  VAL   B CG2   1 
ATOM   16140 N  N     . ASN   B  1  966  ? 21.020  49.762  92.669  1.00 14.85 ? 964  ASN   B N     1 
ATOM   16141 C  CA    . ASN   B  1  966  ? 20.958  50.495  91.407  1.00 15.35 ? 964  ASN   B CA    1 
ATOM   16142 C  C     . ASN   B  1  966  ? 22.344  50.892  90.918  1.00 15.88 ? 964  ASN   B C     1 
ATOM   16143 O  O     . ASN   B  1  966  ? 22.553  51.049  89.710  1.00 18.45 ? 964  ASN   B O     1 
ATOM   16144 C  CB    . ASN   B  1  966  ? 20.123  51.760  91.573  1.00 14.68 ? 964  ASN   B CB    1 
ATOM   16145 C  CG    . ASN   B  1  966  ? 18.643  51.480  91.761  1.00 15.26 ? 964  ASN   B CG    1 
ATOM   16146 O  OD1   . ASN   B  1  966  ? 18.133  50.440  91.352  1.00 16.27 ? 964  ASN   B OD1   1 
ATOM   16147 N  ND2   . ASN   B  1  966  ? 17.943  52.429  92.357  1.00 16.81 ? 964  ASN   B ND2   1 
ATOM   16148 N  N     . ALA   B  1  967  ? 23.298  51.060  91.834  1.00 15.74 ? 965  ALA   B N     1 
ATOM   16149 C  CA    . ALA   B  1  967  ? 24.593  51.615  91.476  1.00 17.06 ? 965  ALA   B CA    1 
ATOM   16150 C  C     . ALA   B  1  967  ? 25.422  50.679  90.616  1.00 16.83 ? 965  ALA   B C     1 
ATOM   16151 O  O     . ALA   B  1  967  ? 26.432  51.121  90.064  1.00 17.94 ? 965  ALA   B O     1 
ATOM   16152 C  CB    . ALA   B  1  967  ? 25.376  51.986  92.742  1.00 16.92 ? 965  ALA   B CB    1 
ATOM   16153 N  N     . THR   B  1  968  ? 25.042  49.402  90.494  1.00 14.64 ? 966  THR   B N     1 
ATOM   16154 C  CA    . THR   B  1  968  ? 25.796  48.515  89.614  1.00 16.37 ? 966  THR   B CA    1 
ATOM   16155 C  C     . THR   B  1  968  ? 25.642  48.908  88.152  1.00 15.87 ? 966  THR   B C     1 
ATOM   16156 O  O     . THR   B  1  968  ? 26.457  48.491  87.319  1.00 17.49 ? 966  THR   B O     1 
ATOM   16157 C  CB    . THR   B  1  968  ? 25.328  47.070  89.750  1.00 15.80 ? 966  THR   B CB    1 
ATOM   16158 O  OG1   . THR   B  1  968  ? 24.047  46.943  89.124  1.00 15.89 ? 966  THR   B OG1   1 
ATOM   16159 C  CG2   . THR   B  1  968  ? 25.239  46.649  91.206  1.00 17.16 ? 966  THR   B CG2   1 
ATOM   16160 N  N     . GLY   B  1  969  ? 24.622  49.699  87.825  1.00 16.34 ? 967  GLY   B N     1 
ATOM   16161 C  CA    . GLY   B  1  969  ? 24.315  50.029  86.457  1.00 16.30 ? 967  GLY   B CA    1 
ATOM   16162 C  C     . GLY   B  1  969  ? 23.404  49.040  85.774  1.00 16.06 ? 967  GLY   B C     1 
ATOM   16163 O  O     . GLY   B  1  969  ? 22.864  49.353  84.708  1.00 15.53 ? 967  GLY   B O     1 
ATOM   16164 N  N     . TYR   B  1  970  ? 23.218  47.858  86.349  1.00 15.30 ? 968  TYR   B N     1 
ATOM   16165 C  CA    A TYR   B  1  970  ? 22.275  46.902  85.801  0.57 13.91 ? 968  TYR   B CA    1 
ATOM   16166 C  CA    B TYR   B  1  970  ? 22.278  46.886  85.820  0.43 13.94 ? 968  TYR   B CA    1 
ATOM   16167 C  C     . TYR   B  1  970  ? 20.868  47.195  86.314  1.00 14.13 ? 968  TYR   B C     1 
ATOM   16168 O  O     . TYR   B  1  970  ? 20.658  48.004  87.220  1.00 16.26 ? 968  TYR   B O     1 
ATOM   16169 C  CB    A TYR   B  1  970  ? 22.690  45.488  86.190  0.57 14.36 ? 968  TYR   B CB    1 
ATOM   16170 C  CB    B TYR   B  1  970  ? 22.678  45.485  86.271  0.43 14.36 ? 968  TYR   B CB    1 
ATOM   16171 C  CG    A TYR   B  1  970  ? 23.848  44.957  85.385  0.57 15.96 ? 968  TYR   B CG    1 
ATOM   16172 C  CG    B TYR   B  1  970  ? 24.036  45.063  85.776  0.43 14.81 ? 968  TYR   B CG    1 
ATOM   16173 C  CD1   A TYR   B  1  970  ? 23.673  44.564  84.065  0.57 15.12 ? 968  TYR   B CD1   1 
ATOM   16174 C  CD1   B TYR   B  1  970  ? 24.180  44.444  84.542  0.43 15.68 ? 968  TYR   B CD1   1 
ATOM   16175 C  CD2   A TYR   B  1  970  ? 25.111  44.832  85.946  0.57 16.12 ? 968  TYR   B CD2   1 
ATOM   16176 C  CD2   B TYR   B  1  970  ? 25.176  45.285  86.534  0.43 14.06 ? 968  TYR   B CD2   1 
ATOM   16177 C  CE1   A TYR   B  1  970  ? 24.737  44.059  83.313  0.57 17.44 ? 968  TYR   B CE1   1 
ATOM   16178 C  CE1   B TYR   B  1  970  ? 25.415  44.051  84.079  0.43 18.27 ? 968  TYR   B CE1   1 
ATOM   16179 C  CE2   A TYR   B  1  970  ? 26.175  44.331  85.209  0.57 16.58 ? 968  TYR   B CE2   1 
ATOM   16180 C  CE2   B TYR   B  1  970  ? 26.417  44.895  86.077  0.43 18.59 ? 968  TYR   B CE2   1 
ATOM   16181 C  CZ    A TYR   B  1  970  ? 25.982  43.945  83.894  0.57 18.05 ? 968  TYR   B CZ    1 
ATOM   16182 C  CZ    B TYR   B  1  970  ? 26.529  44.280  84.851  0.43 18.50 ? 968  TYR   B CZ    1 
ATOM   16183 O  OH    A TYR   B  1  970  ? 27.041  43.446  83.164  0.57 18.45 ? 968  TYR   B OH    1 
ATOM   16184 O  OH    B TYR   B  1  970  ? 27.765  43.890  84.390  0.43 20.50 ? 968  TYR   B OH    1 
ATOM   16185 N  N     . GLY   B  1  971  ? 19.893  46.532  85.709  1.00 13.59 ? 969  GLY   B N     1 
ATOM   16186 C  CA    . GLY   B  1  971  ? 18.527  46.740  86.114  1.00 14.01 ? 969  GLY   B CA    1 
ATOM   16187 C  C     . GLY   B  1  971  ? 17.622  45.738  85.449  1.00 12.29 ? 969  GLY   B C     1 
ATOM   16188 O  O     . GLY   B  1  971  ? 16.682  46.116  84.744  1.00 13.08 ? 969  GLY   B O     1 
ATOM   16189 N  N     . LEU   B  1  972  ? 17.877  44.462  85.697  1.00 11.96 ? 970  LEU   B N     1 
ATOM   16190 C  CA    . LEU   B  1  972  ? 17.124  43.395  85.058  1.00 12.46 ? 970  LEU   B CA    1 
ATOM   16191 C  C     . LEU   B  1  972  ? 16.042  42.894  86.007  1.00 11.69 ? 970  LEU   B C     1 
ATOM   16192 O  O     . LEU   B  1  972  ? 14.916  43.393  85.956  1.00 12.82 ? 970  LEU   B O     1 
ATOM   16193 C  CB    . LEU   B  1  972  ? 18.069  42.295  84.573  1.00 13.90 ? 970  LEU   B CB    1 
ATOM   16194 C  CG    . LEU   B  1  972  ? 17.417  41.223  83.711  1.00 12.19 ? 970  LEU   B CG    1 
ATOM   16195 C  CD1   . LEU   B  1  972  ? 16.706  41.852  82.519  1.00 15.35 ? 970  LEU   B CD1   1 
ATOM   16196 C  CD2   . LEU   B  1  972  ? 18.491  40.257  83.243  1.00 14.53 ? 970  LEU   B CD2   1 
ATOM   16197 N  N     . THR   B  1  973  ? 16.352  41.931  86.879  1.00 11.85 ? 971  THR   B N     1 
ATOM   16198 C  CA    . THR   B  1  973  ? 15.352  41.448  87.818  1.00 11.86 ? 971  THR   B CA    1 
ATOM   16199 C  C     . THR   B  1  973  ? 15.670  41.918  89.225  1.00 10.65 ? 971  THR   B C     1 
ATOM   16200 O  O     . THR   B  1  973  ? 16.812  42.207  89.575  1.00 12.93 ? 971  THR   B O     1 
ATOM   16201 C  CB    . THR   B  1  973  ? 15.227  39.923  87.810  1.00 11.00 ? 971  THR   B CB    1 
ATOM   16202 O  OG1   . THR   B  1  973  ? 16.497  39.348  88.144  1.00 12.29 ? 971  THR   B OG1   1 
ATOM   16203 C  CG2   . THR   B  1  973  ? 14.766  39.441  86.439  1.00 13.94 ? 971  THR   B CG2   1 
ATOM   16204 N  N     . PHE   B  1  974  ? 14.621  41.968  90.031  1.00 11.47 ? 972  PHE   B N     1 
ATOM   16205 C  CA    . PHE   B  1  974  ? 14.766  42.407  91.402  1.00 11.65 ? 972  PHE   B CA    1 
ATOM   16206 C  C     . PHE   B  1  974  ? 13.635  41.799  92.208  1.00 12.10 ? 972  PHE   B C     1 
ATOM   16207 O  O     . PHE   B  1  974  ? 12.479  41.826  91.786  1.00 12.39 ? 972  PHE   B O     1 
ATOM   16208 C  CB    . PHE   B  1  974  ? 14.661  43.927  91.503  1.00 10.93 ? 972  PHE   B CB    1 
ATOM   16209 C  CG    . PHE   B  1  974  ? 14.597  44.402  92.920  1.00 11.91 ? 972  PHE   B CG    1 
ATOM   16210 C  CD1   . PHE   B  1  974  ? 15.753  44.524  93.666  1.00 14.06 ? 972  PHE   B CD1   1 
ATOM   16211 C  CD2   . PHE   B  1  974  ? 13.374  44.666  93.516  1.00 12.82 ? 972  PHE   B CD2   1 
ATOM   16212 C  CE1   . PHE   B  1  974  ? 15.710  44.919  94.987  1.00 14.12 ? 972  PHE   B CE1   1 
ATOM   16213 C  CE2   . PHE   B  1  974  ? 13.318  45.070  94.836  1.00 13.54 ? 972  PHE   B CE2   1 
ATOM   16214 C  CZ    . PHE   B  1  974  ? 14.481  45.193  95.568  1.00 13.65 ? 972  PHE   B CZ    1 
ATOM   16215 N  N     . GLY   B  1  975  ? 13.964  41.301  93.392  1.00 12.22 ? 973  GLY   B N     1 
ATOM   16216 C  CA    . GLY   B  1  975  ? 12.977  40.707  94.271  1.00 12.11 ? 973  GLY   B CA    1 
ATOM   16217 C  C     . GLY   B  1  975  ? 12.903  41.410  95.610  1.00 12.53 ? 973  GLY   B C     1 
ATOM   16218 O  O     . GLY   B  1  975  ? 13.899  41.918  96.120  1.00 12.96 ? 973  GLY   B O     1 
ATOM   16219 N  N     . LEU   B  1  976  ? 11.713  41.401  96.189  1.00 12.52 ? 974  LEU   B N     1 
ATOM   16220 C  CA    . LEU   B  1  976  ? 11.519  41.938  97.524  1.00 12.93 ? 974  LEU   B CA    1 
ATOM   16221 C  C     . LEU   B  1  976  ? 10.632  40.960  98.268  1.00 14.09 ? 974  LEU   B C     1 
ATOM   16222 O  O     . LEU   B  1  976  ? 9.548   40.616  97.794  1.00 14.16 ? 974  LEU   B O     1 
ATOM   16223 C  CB    . LEU   B  1  976  ? 10.822  43.299  97.439  1.00 14.59 ? 974  LEU   B CB    1 
ATOM   16224 C  CG    . LEU   B  1  976  ? 10.427  43.919  98.785  1.00 15.79 ? 974  LEU   B CG    1 
ATOM   16225 C  CD1   . LEU   B  1  976  ? 11.651  44.231  99.634  1.00 17.36 ? 974  LEU   B CD1   1 
ATOM   16226 C  CD2   . LEU   B  1  976  ? 9.615   45.171  98.547  1.00 16.10 ? 974  LEU   B CD2   1 
ATOM   16227 N  N     . HIS   B  1  977  ? 11.093  40.510  99.428  1.00 12.83 ? 975  HIS   B N     1 
ATOM   16228 C  CA    . HIS   B  1  977  ? 10.284  39.691  100.318 1.00 14.07 ? 975  HIS   B CA    1 
ATOM   16229 C  C     . HIS   B  1  977  ? 9.977   40.515  101.555 1.00 14.41 ? 975  HIS   B C     1 
ATOM   16230 O  O     . HIS   B  1  977  ? 10.874  40.833  102.342 1.00 14.51 ? 975  HIS   B O     1 
ATOM   16231 C  CB    . HIS   B  1  977  ? 10.985  38.393  100.696 1.00 15.42 ? 975  HIS   B CB    1 
ATOM   16232 C  CG    . HIS   B  1  977  ? 10.702  37.270  99.758  1.00 15.64 ? 975  HIS   B CG    1 
ATOM   16233 N  ND1   . HIS   B  1  977  ? 9.903   36.199  100.097 1.00 22.76 ? 975  HIS   B ND1   1 
ATOM   16234 C  CD2   . HIS   B  1  977  ? 11.095  37.061  98.481  1.00 20.49 ? 975  HIS   B CD2   1 
ATOM   16235 C  CE1   . HIS   B  1  977  ? 9.837   35.368  99.073  1.00 20.18 ? 975  HIS   B CE1   1 
ATOM   16236 N  NE2   . HIS   B  1  977  ? 10.543  35.871  98.080  1.00 21.88 ? 975  HIS   B NE2   1 
ATOM   16237 N  N     . THR   B  1  978  ? 8.711   40.860  101.707 1.00 14.23 ? 976  THR   B N     1 
ATOM   16238 C  CA    . THR   B  1  978  ? 8.243   41.616  102.853 1.00 14.07 ? 976  THR   B CA    1 
ATOM   16239 C  C     . THR   B  1  978  ? 6.740   41.471  102.904 1.00 14.74 ? 976  THR   B C     1 
ATOM   16240 O  O     . THR   B  1  978  ? 6.088   41.270  101.877 1.00 16.30 ? 976  THR   B O     1 
ATOM   16241 C  CB    . THR   B  1  978  ? 8.597   43.099  102.749 1.00 16.48 ? 976  THR   B CB    1 
ATOM   16242 O  OG1   . THR   B  1  978  ? 8.062   43.778  103.884 1.00 16.33 ? 976  THR   B OG1   1 
ATOM   16243 C  CG2   . THR   B  1  978  ? 7.977   43.702  101.519 1.00 17.85 ? 976  THR   B CG2   1 
ATOM   16244 N  N     . ARG   B  1  979  ? 6.195   41.584  104.102 1.00 16.57 ? 977  ARG   B N     1 
ATOM   16245 C  CA    . ARG   B  1  979  ? 4.754   41.622  104.237 1.00 16.89 ? 977  ARG   B CA    1 
ATOM   16246 C  C     . ARG   B  1  979  ? 4.223   43.035  104.358 1.00 17.70 ? 977  ARG   B C     1 
ATOM   16247 O  O     . ARG   B  1  979  ? 3.012   43.207  104.485 1.00 17.95 ? 977  ARG   B O     1 
ATOM   16248 C  CB    . ARG   B  1  979  ? 4.315   40.785  105.431 1.00 20.04 ? 977  ARG   B CB    1 
ATOM   16249 C  CG    . ARG   B  1  979  ? 4.572   39.312  105.206 1.00 26.95 ? 977  ARG   B CG    1 
ATOM   16250 C  CD    . ARG   B  1  979  ? 4.372   38.524  106.470 1.00 32.15 ? 977  ARG   B CD    1 
ATOM   16251 N  NE    . ARG   B  1  979  ? 4.287   37.096  106.196 1.00 40.33 ? 977  ARG   B NE    1 
ATOM   16252 C  CZ    . ARG   B  1  979  ? 4.015   36.178  107.112 1.00 43.45 ? 977  ARG   B CZ    1 
ATOM   16253 N  NH1   . ARG   B  1  979  ? 3.798   36.509  108.376 1.00 36.03 ? 977  ARG   B NH1   1 
ATOM   16254 N  NH2   . ARG   B  1  979  ? 3.959   34.898  106.750 1.00 38.50 ? 977  ARG   B NH2   1 
ATOM   16255 N  N     . LEU   B  1  980  ? 5.085   44.048  104.315 1.00 15.14 ? 978  LEU   B N     1 
ATOM   16256 C  CA    . LEU   B  1  980  ? 4.729   45.390  104.760 1.00 14.72 ? 978  LEU   B CA    1 
ATOM   16257 C  C     . LEU   B  1  980  ? 4.536   46.293  103.555 1.00 16.21 ? 978  LEU   B C     1 
ATOM   16258 O  O     . LEU   B  1  980  ? 5.483   46.525  102.794 1.00 15.78 ? 978  LEU   B O     1 
ATOM   16259 C  CB    . LEU   B  1  980  ? 5.822   45.955  105.660 1.00 15.48 ? 978  LEU   B CB    1 
ATOM   16260 C  CG    . LEU   B  1  980  ? 6.191   45.056  106.834 1.00 17.94 ? 978  LEU   B CG    1 
ATOM   16261 C  CD1   . LEU   B  1  980  ? 7.320   45.677  107.665 1.00 19.60 ? 978  LEU   B CD1   1 
ATOM   16262 C  CD2   . LEU   B  1  980  ? 4.964   44.800  107.691 1.00 18.75 ? 978  LEU   B CD2   1 
ATOM   16263 N  N     . ASP   B  1  981  ? 3.325   46.832  103.413 1.00 14.98 ? 979  ASP   B N     1 
ATOM   16264 C  CA    . ASP   B  1  981  ? 3.021   47.653  102.245 1.00 15.14 ? 979  ASP   B CA    1 
ATOM   16265 C  C     . ASP   B  1  981  ? 3.913   48.878  102.157 1.00 16.21 ? 979  ASP   B C     1 
ATOM   16266 O  O     . ASP   B  1  981  ? 4.229   49.318  101.051 1.00 15.72 ? 979  ASP   B O     1 
ATOM   16267 C  CB    . ASP   B  1  981  ? 1.566   48.111  102.262 1.00 17.21 ? 979  ASP   B CB    1 
ATOM   16268 C  CG    . ASP   B  1  981  ? 0.592   47.002  101.979 1.00 17.94 ? 979  ASP   B CG    1 
ATOM   16269 O  OD1   . ASP   B  1  981  ? 0.981   45.962  101.428 1.00 19.68 ? 979  ASP   B OD1   1 
ATOM   16270 O  OD2   . ASP   B  1  981  ? -0.592  47.187  102.328 1.00 22.00 ? 979  ASP   B OD2   1 
ATOM   16271 N  N     . GLU   B  1  982  ? 4.296   49.473  103.287 1.00 16.29 ? 980  GLU   B N     1 
ATOM   16272 C  CA    . GLU   B  1  982  ? 5.154   50.652  103.210 1.00 16.63 ? 980  GLU   B CA    1 
ATOM   16273 C  C     . GLU   B  1  982  ? 6.504   50.294  102.613 1.00 15.49 ? 980  GLU   B C     1 
ATOM   16274 O  O     . GLU   B  1  982  ? 7.074   51.061  101.831 1.00 16.06 ? 980  GLU   B O     1 
ATOM   16275 C  CB    . GLU   B  1  982  ? 5.348   51.283  104.588 1.00 17.80 ? 980  GLU   B CB    1 
ATOM   16276 C  CG    . GLU   B  1  982  ? 6.253   52.503  104.537 1.00 21.68 ? 980  GLU   B CG    1 
ATOM   16277 C  CD    . GLU   B  1  982  ? 6.789   52.919  105.891 1.00 25.67 ? 980  GLU   B CD    1 
ATOM   16278 O  OE1   . GLU   B  1  982  ? 7.185   52.035  106.685 1.00 28.40 ? 980  GLU   B OE1   1 
ATOM   16279 O  OE2   . GLU   B  1  982  ? 6.825   54.134  106.159 1.00 23.98 ? 980  GLU   B OE2   1 
ATOM   16280 N  N     . THR   B  1  983  ? 7.026   49.128  102.972 1.00 14.43 ? 981  THR   B N     1 
ATOM   16281 C  CA    . THR   B  1  983  ? 8.304   48.710  102.423 1.00 14.89 ? 981  THR   B CA    1 
ATOM   16282 C  C     . THR   B  1  983  ? 8.172   48.399  100.941 1.00 15.06 ? 981  THR   B C     1 
ATOM   16283 O  O     . THR   B  1  983  ? 9.054   48.750  100.147 1.00 14.97 ? 981  THR   B O     1 
ATOM   16284 C  CB    . THR   B  1  983  ? 8.815   47.512  103.218 1.00 16.97 ? 981  THR   B CB    1 
ATOM   16285 O  OG1   . THR   B  1  983  ? 9.061   47.939  104.560 1.00 16.66 ? 981  THR   B OG1   1 
ATOM   16286 C  CG2   . THR   B  1  983  ? 10.107  46.985  102.633 1.00 16.31 ? 981  THR   B CG2   1 
ATOM   16287 N  N     . ILE   B  1  984  ? 7.061   47.768  100.551 1.00 13.73 ? 982  ILE   B N     1 
ATOM   16288 C  CA    . ILE   B  1  984  ? 6.811   47.510  99.137  1.00 14.19 ? 982  ILE   B CA    1 
ATOM   16289 C  C     . ILE   B  1  984  ? 6.766   48.814  98.359  1.00 14.74 ? 982  ILE   B C     1 
ATOM   16290 O  O     . ILE   B  1  984  ? 7.427   48.958  97.323  1.00 14.65 ? 982  ILE   B O     1 
ATOM   16291 C  CB    . ILE   B  1  984  ? 5.523   46.691  98.951  1.00 14.61 ? 982  ILE   B CB    1 
ATOM   16292 C  CG1   . ILE   B  1  984  ? 5.686   45.311  99.574  1.00 18.31 ? 982  ILE   B CG1   1 
ATOM   16293 C  CG2   . ILE   B  1  984  ? 5.187   46.551  97.465  1.00 16.27 ? 982  ILE   B CG2   1 
ATOM   16294 C  CD1   . ILE   B  1  984  ? 4.394   44.551  99.682  1.00 18.68 ? 982  ILE   B CD1   1 
ATOM   16295 N  N     . ALA   B  1  985  ? 5.997   49.790  98.848  1.00 14.51 ? 983  ALA   B N     1 
ATOM   16296 C  CA    . ALA   B  1  985  ? 5.901   51.055  98.125  1.00 15.26 ? 983  ALA   B CA    1 
ATOM   16297 C  C     . ALA   B  1  985  ? 7.257   51.740  98.048  1.00 14.86 ? 983  ALA   B C     1 
ATOM   16298 O  O     . ALA   B  1  985  ? 7.652   52.240  96.990  1.00 16.14 ? 983  ALA   B O     1 
ATOM   16299 C  CB    . ALA   B  1  985  ? 4.867   51.961  98.790  1.00 14.92 ? 983  ALA   B CB    1 
ATOM   16300 N  N     . HIS   B  1  986  ? 7.987   51.763  99.161  1.00 15.00 ? 984  HIS   B N     1 
ATOM   16301 C  CA    . HIS   B  1  986  ? 9.281   52.434  99.173  1.00 16.82 ? 984  HIS   B CA    1 
ATOM   16302 C  C     . HIS   B  1  986  ? 10.223  51.763  98.188  1.00 15.34 ? 984  HIS   B C     1 
ATOM   16303 O  O     . HIS   B  1  986  ? 10.760  52.399  97.276  1.00 15.90 ? 984  HIS   B O     1 
ATOM   16304 C  CB    . HIS   B  1  986  ? 9.848   52.395  100.594 1.00 17.44 ? 984  HIS   B CB    1 
ATOM   16305 C  CG    . HIS   B  1  986  ? 11.249  52.917  100.722 1.00 16.68 ? 984  HIS   B CG    1 
ATOM   16306 N  ND1   . HIS   B  1  986  ? 11.860  53.069  101.947 1.00 22.50 ? 984  HIS   B ND1   1 
ATOM   16307 C  CD2   . HIS   B  1  986  ? 12.161  53.310  99.799  1.00 19.32 ? 984  HIS   B CD2   1 
ATOM   16308 C  CE1   . HIS   B  1  986  ? 13.086  53.532  101.775 1.00 22.75 ? 984  HIS   B CE1   1 
ATOM   16309 N  NE2   . HIS   B  1  986  ? 13.297  53.678  100.480 1.00 19.37 ? 984  HIS   B NE2   1 
ATOM   16310 N  N     . VAL   B  1  987  ? 10.413  50.461  98.342  1.00 14.18 ? 985  VAL   B N     1 
ATOM   16311 C  CA    . VAL   B  1  987  ? 11.418  49.785  97.536  1.00 14.55 ? 985  VAL   B CA    1 
ATOM   16312 C  C     . VAL   B  1  987  ? 11.047  49.814  96.061  1.00 15.67 ? 985  VAL   B C     1 
ATOM   16313 O  O     . VAL   B  1  987  ? 11.897  50.082  95.208  1.00 17.23 ? 985  VAL   B O     1 
ATOM   16314 C  CB    . VAL   B  1  987  ? 11.641  48.360  98.057  1.00 15.09 ? 985  VAL   B CB    1 
ATOM   16315 C  CG1   . VAL   B  1  987  ? 12.525  47.582  97.101  1.00 17.16 ? 985  VAL   B CG1   1 
ATOM   16316 C  CG2   . VAL   B  1  987  ? 12.264  48.418  99.444  1.00 15.63 ? 985  VAL   B CG2   1 
ATOM   16317 N  N     . THR   B  1  988  ? 9.784   49.538  95.728  1.00 14.95 ? 986  THR   B N     1 
ATOM   16318 C  CA    . THR   B  1  988  ? 9.427   49.527  94.311  1.00 15.59 ? 986  THR   B CA    1 
ATOM   16319 C  C     . THR   B  1  988  ? 9.464   50.928  93.707  1.00 17.01 ? 986  THR   B C     1 
ATOM   16320 O  O     . THR   B  1  988  ? 9.705   51.062  92.504  1.00 22.48 ? 986  THR   B O     1 
ATOM   16321 C  CB    . THR   B  1  988  ? 8.087   48.829  94.049  1.00 18.04 ? 986  THR   B CB    1 
ATOM   16322 O  OG1   . THR   B  1  988  ? 7.034   49.537  94.697  1.00 19.49 ? 986  THR   B OG1   1 
ATOM   16323 C  CG2   . THR   B  1  988  ? 8.112   47.387  94.518  1.00 19.10 ? 986  THR   B CG2   1 
ATOM   16324 N  N     . SER   B  1  989  ? 9.267   51.974  94.510  1.00 17.09 ? 987  SER   B N     1 
ATOM   16325 C  CA    . SER   B  1  989  ? 9.381   53.332  93.982  1.00 19.38 ? 987  SER   B CA    1 
ATOM   16326 C  C     . SER   B  1  989  ? 10.823  53.730  93.690  1.00 20.46 ? 987  SER   B C     1 
ATOM   16327 O  O     . SER   B  1  989  ? 11.046  54.639  92.882  1.00 25.96 ? 987  SER   B O     1 
ATOM   16328 C  CB    . SER   B  1  989  ? 8.726   54.360  94.915  1.00 21.40 ? 987  SER   B CB    1 
ATOM   16329 O  OG    . SER   B  1  989  ? 9.438   54.537  96.132  1.00 27.94 ? 987  SER   B OG    1 
ATOM   16330 N  N     . ARG   B  1  990  ? 11.801  53.074  94.310  1.00 16.73 ? 988  ARG   B N     1 
ATOM   16331 C  CA    . ARG   B  1  990  ? 13.188  53.515  94.236  1.00 16.27 ? 988  ARG   B CA    1 
ATOM   16332 C  C     . ARG   B  1  990  ? 14.082  52.579  93.440  1.00 15.28 ? 988  ARG   B C     1 
ATOM   16333 O  O     . ARG   B  1  990  ? 15.112  53.014  92.920  1.00 16.21 ? 988  ARG   B O     1 
ATOM   16334 C  CB    . ARG   B  1  990  ? 13.766  53.675  95.647  1.00 19.07 ? 988  ARG   B CB    1 
ATOM   16335 C  CG    . ARG   B  1  990  ? 12.915  54.513  96.588  1.00 27.53 ? 988  ARG   B CG    1 
ATOM   16336 C  CD    . ARG   B  1  990  ? 13.097  55.989  96.356  1.00 24.51 ? 988  ARG   B CD    1 
ATOM   16337 N  NE    . ARG   B  1  990  ? 14.215  56.524  97.124  1.00 19.04 ? 988  ARG   B NE    1 
ATOM   16338 C  CZ    . ARG   B  1  990  ? 14.638  57.775  97.021  1.00 19.00 ? 988  ARG   B CZ    1 
ATOM   16339 N  NH1   . ARG   B  1  990  ? 14.097  58.617  96.157  1.00 22.26 ? 988  ARG   B NH1   1 
ATOM   16340 N  NH2   . ARG   B  1  990  ? 15.628  58.190  97.801  1.00 20.57 ? 988  ARG   B NH2   1 
ATOM   16341 N  N     . ILE   B  1  991  ? 13.734  51.300  93.352  1.00 14.74 ? 989  ILE   B N     1 
ATOM   16342 C  CA    . ILE   B  1  991  ? 14.521  50.370  92.558  1.00 14.54 ? 989  ILE   B CA    1 
ATOM   16343 C  C     . ILE   B  1  991  ? 14.355  50.708  91.080  1.00 15.57 ? 989  ILE   B C     1 
ATOM   16344 O  O     . ILE   B  1  991  ? 13.311  51.215  90.641  1.00 16.92 ? 989  ILE   B O     1 
ATOM   16345 C  CB    . ILE   B  1  991  ? 14.077  48.930  92.867  1.00 15.03 ? 989  ILE   B CB    1 
ATOM   16346 C  CG1   . ILE   B  1  991  ? 15.074  47.918  92.321  1.00 18.29 ? 989  ILE   B CG1   1 
ATOM   16347 C  CG2   . ILE   B  1  991  ? 12.705  48.659  92.269  1.00 18.39 ? 989  ILE   B CG2   1 
ATOM   16348 C  CD1   . ILE   B  1  991  ? 16.397  47.978  93.036  1.00 21.04 ? 989  ILE   B CD1   1 
ATOM   16349 N  N     . LYS   B  1  992  ? 15.398  50.454  90.308  1.00 14.88 ? 990  LYS   B N     1 
ATOM   16350 C  CA    . LYS   B  1  992  ? 15.374  50.753  88.879  1.00 14.84 ? 990  LYS   B CA    1 
ATOM   16351 C  C     . LYS   B  1  992  ? 15.699  49.463  88.151  1.00 15.25 ? 990  LYS   B C     1 
ATOM   16352 O  O     . LYS   B  1  992  ? 16.823  49.237  87.730  1.00 19.55 ? 990  LYS   B O     1 
ATOM   16353 C  CB    . LYS   B  1  992  ? 16.391  51.843  88.582  1.00 16.30 ? 990  LYS   B CB    1 
ATOM   16354 C  CG    . LYS   B  1  992  ? 16.056  53.188  89.242  1.00 19.36 ? 990  LYS   B CG    1 
ATOM   16355 C  CD    . LYS   B  1  992  ? 17.145  54.221  88.946  1.00 26.93 ? 990  LYS   B CD    1 
ATOM   16356 C  CE    . LYS   B  1  992  ? 17.372  54.389  87.443  1.00 32.90 ? 990  LYS   B CE    1 
ATOM   16357 N  NZ    . LYS   B  1  992  ? 18.559  55.244  87.131  1.00 37.78 ? 990  LYS   B NZ    1 
ATOM   16358 N  N     . ALA   B  1  993  ? 14.702  48.603  88.013  1.00 15.17 ? 991  ALA   B N     1 
ATOM   16359 C  CA    . ALA   B  1  993  ? 14.873  47.341  87.319  1.00 13.39 ? 991  ALA   B CA    1 
ATOM   16360 C  C     . ALA   B  1  993  ? 13.629  47.081  86.492  1.00 13.61 ? 991  ALA   B C     1 
ATOM   16361 O  O     . ALA   B  1  993  ? 12.533  47.544  86.824  1.00 14.71 ? 991  ALA   B O     1 
ATOM   16362 C  CB    . ALA   B  1  993  ? 15.115  46.178  88.289  1.00 15.56 ? 991  ALA   B CB    1 
ATOM   16363 N  N     . GLY   B  1  994  ? 13.805  46.328  85.410  1.00 12.17 ? 992  GLY   B N     1 
ATOM   16364 C  CA    . GLY   B  1  994  ? 12.687  46.133  84.510  1.00 13.19 ? 992  GLY   B CA    1 
ATOM   16365 C  C     . GLY   B  1  994  ? 11.688  45.092  84.952  1.00 11.49 ? 992  GLY   B C     1 
ATOM   16366 O  O     . GLY   B  1  994  ? 10.547  45.128  84.495  1.00 12.01 ? 992  GLY   B O     1 
ATOM   16367 N  N     . ASN   B  1  995  ? 12.092  44.151  85.798  1.00 12.16 ? 993  ASN   B N     1 
ATOM   16368 C  CA    . ASN   B  1  995  ? 11.227  43.063  86.235  1.00 11.66 ? 993  ASN   B CA    1 
ATOM   16369 C  C     . ASN   B  1  995  ? 11.334  42.958  87.740  1.00 11.59 ? 993  ASN   B C     1 
ATOM   16370 O  O     . ASN   B  1  995  ? 12.396  42.615  88.267  1.00 12.91 ? 993  ASN   B O     1 
ATOM   16371 C  CB    . ASN   B  1  995  ? 11.623  41.749  85.574  1.00 11.95 ? 993  ASN   B CB    1 
ATOM   16372 C  CG    . ASN   B  1  995  ? 11.075  41.646  84.187  1.00 11.88 ? 993  ASN   B CG    1 
ATOM   16373 O  OD1   . ASN   B  1  995  ? 11.658  42.158  83.230  1.00 12.50 ? 993  ASN   B OD1   1 
ATOM   16374 N  ND2   . ASN   B  1  995  ? 9.899   41.044  84.077  1.00 13.23 ? 993  ASN   B ND2   1 
ATOM   16375 N  N     . LEU   B  1  996  ? 10.238  43.256  88.409  1.00 12.08 ? 994  LEU   B N     1 
ATOM   16376 C  CA    . LEU   B  1  996  ? 10.169  43.240  89.855  1.00 12.49 ? 994  LEU   B CA    1 
ATOM   16377 C  C     . LEU   B  1  996  ? 9.323   42.057  90.279  1.00 12.28 ? 994  LEU   B C     1 
ATOM   16378 O  O     . LEU   B  1  996  ? 8.358   41.697  89.598  1.00 12.63 ? 994  LEU   B O     1 
ATOM   16379 C  CB    . LEU   B  1  996  ? 9.517   44.514  90.362  1.00 13.14 ? 994  LEU   B CB    1 
ATOM   16380 C  CG    . LEU   B  1  996  ? 10.092  45.816  89.802  1.00 14.54 ? 994  LEU   B CG    1 
ATOM   16381 C  CD1   . LEU   B  1  996  ? 9.366   47.022  90.423  1.00 16.26 ? 994  LEU   B CD1   1 
ATOM   16382 C  CD2   . LEU   B  1  996  ? 11.582  45.898  90.002  1.00 15.14 ? 994  LEU   B CD2   1 
ATOM   16383 N  N     . TYR   B  1  997  ? 9.652   41.488  91.437  1.00 11.79 ? 995  TYR   B N     1 
ATOM   16384 C  CA    . TYR   B  1  997  ? 8.955   40.316  91.946  1.00 13.21 ? 995  TYR   B CA    1 
ATOM   16385 C  C     . TYR   B  1  997  ? 8.795   40.493  93.439  1.00 11.85 ? 995  TYR   B C     1 
ATOM   16386 O  O     . TYR   B  1  997  ? 9.776   40.750  94.140  1.00 13.82 ? 995  TYR   B O     1 
ATOM   16387 C  CB    . TYR   B  1  997  ? 9.741   39.031  91.671  1.00 13.02 ? 995  TYR   B CB    1 
ATOM   16388 C  CG    . TYR   B  1  997  ? 10.101  38.862  90.215  1.00 13.38 ? 995  TYR   B CG    1 
ATOM   16389 C  CD1   . TYR   B  1  997  ? 11.234  39.456  89.705  1.00 12.93 ? 995  TYR   B CD1   1 
ATOM   16390 C  CD2   . TYR   B  1  997  ? 9.301   38.134  89.350  1.00 14.46 ? 995  TYR   B CD2   1 
ATOM   16391 C  CE1   . TYR   B  1  997  ? 11.568  39.335  88.381  1.00 15.05 ? 995  TYR   B CE1   1 
ATOM   16392 C  CE2   . TYR   B  1  997  ? 9.644   38.003  88.014  1.00 13.09 ? 995  TYR   B CE2   1 
ATOM   16393 C  CZ    . TYR   B  1  997  ? 10.780  38.606  87.546  1.00 14.42 ? 995  TYR   B CZ    1 
ATOM   16394 O  OH    . TYR   B  1  997  ? 11.149  38.493  86.218  1.00 15.78 ? 995  TYR   B OH    1 
ATOM   16395 N  N     . ILE   B  1  998  ? 7.570   40.365  93.918  1.00 12.39 ? 996  ILE   B N     1 
ATOM   16396 C  CA    . ILE   B  1  998  ? 7.267   40.574  95.324  1.00 12.69 ? 996  ILE   B CA    1 
ATOM   16397 C  C     . ILE   B  1  998  ? 6.819   39.243  95.910  1.00 14.25 ? 996  ILE   B C     1 
ATOM   16398 O  O     . ILE   B  1  998  ? 5.804   38.676  95.485  1.00 13.90 ? 996  ILE   B O     1 
ATOM   16399 C  CB    . ILE   B  1  998  ? 6.171   41.633  95.505  1.00 13.94 ? 996  ILE   B CB    1 
ATOM   16400 C  CG1   . ILE   B  1  998  ? 6.548   42.934  94.787  1.00 18.18 ? 996  ILE   B CG1   1 
ATOM   16401 C  CG2   . ILE   B  1  998  ? 5.899   41.857  96.993  1.00 16.24 ? 996  ILE   B CG2   1 
ATOM   16402 C  CD1   . ILE   B  1  998  ? 7.800   43.533  95.231  1.00 21.75 ? 996  ILE   B CD1   1 
ATOM   16403 N  N     . ASN   B  1  999  ? 7.566   38.767  96.907  1.00 13.23 ? 997  ASN   B N     1 
ATOM   16404 C  CA    . ASN   B  1  999  ? 7.203   37.576  97.674  1.00 13.96 ? 997  ASN   B CA    1 
ATOM   16405 C  C     . ASN   B  1  999  ? 7.160   36.324  96.811  1.00 13.94 ? 997  ASN   B C     1 
ATOM   16406 O  O     . ASN   B  1  999  ? 6.344   35.431  97.020  1.00 14.47 ? 997  ASN   B O     1 
ATOM   16407 C  CB    . ASN   B  1  999  ? 5.915   37.786  98.458  1.00 12.72 ? 997  ASN   B CB    1 
ATOM   16408 C  CG    . ASN   B  1  999  ? 6.080   38.824  99.528  1.00 14.58 ? 997  ASN   B CG    1 
ATOM   16409 O  OD1   . ASN   B  1  999  ? 7.166   38.957  100.095 1.00 14.95 ? 997  ASN   B OD1   1 
ATOM   16410 N  ND2   . ASN   B  1  999  ? 5.017   39.567  99.814  1.00 15.59 ? 997  ASN   B ND2   1 
ATOM   16411 N  N     . ARG   B  1  1000 ? 8.077   36.246  95.860  1.00 13.88 ? 998  ARG   B N     1 
ATOM   16412 C  CA    . ARG   B  1  1000 ? 8.206   35.086  94.993  1.00 12.10 ? 998  ARG   B CA    1 
ATOM   16413 C  C     . ARG   B  1  1000 ? 9.626   35.066  94.444  1.00 13.68 ? 998  ARG   B C     1 
ATOM   16414 O  O     . ARG   B  1  1000 ? 10.449  35.928  94.759  1.00 15.29 ? 998  ARG   B O     1 
ATOM   16415 C  CB    . ARG   B  1  1000 ? 7.195   35.150  93.852  1.00 13.18 ? 998  ARG   B CB    1 
ATOM   16416 C  CG    . ARG   B  1  1000 ? 7.195   36.493  93.125  1.00 13.15 ? 998  ARG   B CG    1 
ATOM   16417 C  CD    . ARG   B  1  1000 ? 6.686   36.349  91.700  1.00 13.41 ? 998  ARG   B CD    1 
ATOM   16418 N  NE    . ARG   B  1  1000 ? 7.584   35.513  90.917  1.00 12.50 ? 998  ARG   B NE    1 
ATOM   16419 C  CZ    . ARG   B  1  1000 ? 7.301   35.090  89.694  1.00 13.36 ? 998  ARG   B CZ    1 
ATOM   16420 N  NH1   . ARG   B  1  1000 ? 6.185   35.456  89.082  1.00 14.16 ? 998  ARG   B NH1   1 
ATOM   16421 N  NH2   . ARG   B  1  1000 ? 8.149   34.272  89.078  1.00 15.05 ? 998  ARG   B NH2   1 
ATOM   16422 N  N     . ASN   B  1  1001 ? 9.915   34.068  93.615  1.00 12.61 ? 999  ASN   B N     1 
ATOM   16423 C  CA    . ASN   B  1  1001 ? 11.221  34.025  92.991  1.00 12.87 ? 999  ASN   B CA    1 
ATOM   16424 C  C     . ASN   B  1  1001 ? 11.333  35.137  91.946  1.00 13.53 ? 999  ASN   B C     1 
ATOM   16425 O  O     . ASN   B  1  1001 ? 10.349  35.787  91.582  1.00 13.57 ? 999  ASN   B O     1 
ATOM   16426 C  CB    . ASN   B  1  1001 ? 11.496  32.632  92.412  1.00 14.37 ? 999  ASN   B CB    1 
ATOM   16427 C  CG    . ASN   B  1  1001 ? 10.655  32.314  91.193  1.00 15.68 ? 999  ASN   B CG    1 
ATOM   16428 O  OD1   . ASN   B  1  1001 ? 10.515  33.123  90.287  1.00 15.37 ? 999  ASN   B OD1   1 
ATOM   16429 N  ND2   . ASN   B  1  1001 ? 10.112  31.103  91.156  1.00 25.08 ? 999  ASN   B ND2   1 
ATOM   16430 N  N     . ILE   B  1  1002 ? 12.551  35.363  91.471  1.00 12.58 ? 1000 ILE   B N     1 
ATOM   16431 C  CA    . ILE   B  1  1002 ? 12.802  36.470  90.558  1.00 13.13 ? 1000 ILE   B CA    1 
ATOM   16432 C  C     . ILE   B  1  1002 ? 13.108  35.998  89.143  1.00 14.71 ? 1000 ILE   B C     1 
ATOM   16433 O  O     . ILE   B  1  1002 ? 13.731  36.721  88.378  1.00 15.24 ? 1000 ILE   B O     1 
ATOM   16434 C  CB    . ILE   B  1  1002 ? 13.873  37.437  91.085  1.00 12.92 ? 1000 ILE   B CB    1 
ATOM   16435 C  CG1   . ILE   B  1  1002 ? 15.265  36.783  91.091  1.00 12.92 ? 1000 ILE   B CG1   1 
ATOM   16436 C  CG2   . ILE   B  1  1002 ? 13.478  37.938  92.463  1.00 13.68 ? 1000 ILE   B CG2   1 
ATOM   16437 C  CD1   . ILE   B  1  1002 ? 16.380  37.781  91.313  1.00 13.47 ? 1000 ILE   B CD1   1 
ATOM   16438 N  N     . ILE   B  1  1003 ? 12.697  34.794  88.785  1.00 15.02 ? 1001 ILE   B N     1 
ATOM   16439 C  CA    . ILE   B  1  1003 ? 13.051  34.271  87.476  1.00 15.93 ? 1001 ILE   B CA    1 
ATOM   16440 C  C     . ILE   B  1  1003 ? 11.863  34.228  86.521  1.00 20.42 ? 1001 ILE   B C     1 
ATOM   16441 O  O     . ILE   B  1  1003 ? 11.975  33.664  85.427  1.00 21.00 ? 1001 ILE   B O     1 
ATOM   16442 C  CB    . ILE   B  1  1003 ? 13.791  32.936  87.592  1.00 16.81 ? 1001 ILE   B CB    1 
ATOM   16443 C  CG1   . ILE   B  1  1003 ? 12.943  31.942  88.370  1.00 24.00 ? 1001 ILE   B CG1   1 
ATOM   16444 C  CG2   . ILE   B  1  1003 ? 15.135  33.169  88.292  1.00 16.82 ? 1001 ILE   B CG2   1 
ATOM   16445 C  CD1   . ILE   B  1  1003 ? 13.464  30.563  88.285  1.00 29.66 ? 1001 ILE   B CD1   1 
ATOM   16446 N  N     . GLY   B  1  1004 ? 10.744  34.857  86.885  1.00 17.38 ? 1002 GLY   B N     1 
ATOM   16447 C  CA    . GLY   B  1  1004 ? 9.546   34.813  86.064  1.00 17.93 ? 1002 GLY   B CA    1 
ATOM   16448 C  C     . GLY   B  1  1004 ? 9.687   35.619  84.790  1.00 17.86 ? 1002 GLY   B C     1 
ATOM   16449 O  O     . GLY   B  1  1004 ? 9.980   36.827  84.828  1.00 19.17 ? 1002 GLY   B O     1 
ATOM   16450 N  N     . ALA   B  1  1005 ? 9.475   34.975  83.662  1.00 16.71 ? 1003 ALA   B N     1 
ATOM   16451 C  CA    . ALA   B  1  1005 ? 9.500   35.647  82.386  1.00 19.19 ? 1003 ALA   B CA    1 
ATOM   16452 C  C     . ALA   B  1  1005 ? 8.338   35.151  81.563  1.00 19.10 ? 1003 ALA   B C     1 
ATOM   16453 O  O     . ALA   B  1  1005 ? 8.448   34.965  80.347  1.00 17.54 ? 1003 ALA   B O     1 
ATOM   16454 C  CB    . ALA   B  1  1005 ? 10.832  35.423  81.669  1.00 16.79 ? 1003 ALA   B CB    1 
ATOM   16455 N  N     . VAL   B  1  1006 ? 7.197   34.921  82.216  1.00 13.79 ? 1004 VAL   B N     1 
ATOM   16456 C  CA    . VAL   B  1  1006 ? 6.066   34.366  81.492  1.00 15.89 ? 1004 VAL   B CA    1 
ATOM   16457 C  C     . VAL   B  1  1006 ? 5.648   35.349  80.414  1.00 13.95 ? 1004 VAL   B C     1 
ATOM   16458 O  O     . VAL   B  1  1006 ? 5.324   36.508  80.695  1.00 13.64 ? 1004 VAL   B O     1 
ATOM   16459 C  CB    . VAL   B  1  1006 ? 4.925   34.017  82.441  1.00 14.82 ? 1004 VAL   B CB    1 
ATOM   16460 C  CG1   . VAL   B  1  1006 ? 3.706   33.547  81.629  1.00 15.97 ? 1004 VAL   B CG1   1 
ATOM   16461 C  CG2   . VAL   B  1  1006 ? 5.389   32.923  83.416  1.00 16.54 ? 1004 VAL   B CG2   1 
ATOM   16462 N  N     . VAL   B  1  1007 ? 5.674   34.877  79.166  1.00 14.88 ? 1005 VAL   B N     1 
ATOM   16463 C  CA    . VAL   B  1  1007 ? 5.402   35.731  78.023  1.00 13.86 ? 1005 VAL   B CA    1 
ATOM   16464 C  C     . VAL   B  1  1007 ? 4.040   36.392  78.179  1.00 14.32 ? 1005 VAL   B C     1 
ATOM   16465 O  O     . VAL   B  1  1007 ? 3.032   35.739  78.484  1.00 13.56 ? 1005 VAL   B O     1 
ATOM   16466 C  CB    . VAL   B  1  1007 ? 5.490   34.885  76.750  1.00 14.02 ? 1005 VAL   B CB    1 
ATOM   16467 C  CG1   . VAL   B  1  1007 ? 5.119   35.714  75.559  1.00 14.85 ? 1005 VAL   B CG1   1 
ATOM   16468 C  CG2   . VAL   B  1  1007 ? 6.889   34.343  76.585  1.00 15.96 ? 1005 VAL   B CG2   1 
ATOM   16469 N  N     . GLY   B  1  1008 ? 4.003   37.707  77.976  1.00 13.37 ? 1006 GLY   B N     1 
ATOM   16470 C  CA    . GLY   B  1  1008 ? 2.763   38.452  78.063  1.00 14.44 ? 1006 GLY   B CA    1 
ATOM   16471 C  C     . GLY   B  1  1008 ? 2.199   38.580  79.459  1.00 15.23 ? 1006 GLY   B C     1 
ATOM   16472 O  O     . GLY   B  1  1008 ? 1.110   39.146  79.628  1.00 16.74 ? 1006 GLY   B O     1 
ATOM   16473 N  N     . VAL   B  1  1009 ? 2.889   38.048  80.460  1.00 13.54 ? 1007 VAL   B N     1 
ATOM   16474 C  CA    . VAL   B  1  1009 ? 2.473   38.126  81.854  1.00 14.80 ? 1007 VAL   B CA    1 
ATOM   16475 C  C     . VAL   B  1  1009 ? 3.517   38.850  82.696  1.00 14.43 ? 1007 VAL   B C     1 
ATOM   16476 O  O     . VAL   B  1  1009 ? 3.198   39.803  83.412  1.00 14.30 ? 1007 VAL   B O     1 
ATOM   16477 C  CB    . VAL   B  1  1009 ? 2.168   36.727  82.427  1.00 14.78 ? 1007 VAL   B CB    1 
ATOM   16478 C  CG1   . VAL   B  1  1009 ? 1.699   36.832  83.878  1.00 15.21 ? 1007 VAL   B CG1   1 
ATOM   16479 C  CG2   . VAL   B  1  1009 ? 1.106   36.041  81.568  1.00 14.70 ? 1007 VAL   B CG2   1 
ATOM   16480 N  N     . GLN   B  1  1010 ? 4.782   38.435  82.588  1.00 13.89 ? 1008 GLN   B N     1 
ATOM   16481 C  CA    . GLN   B  1  1010 ? 5.928   39.259  82.969  1.00 13.58 ? 1008 GLN   B CA    1 
ATOM   16482 C  C     . GLN   B  1  1010 ? 6.734   39.539  81.705  1.00 13.60 ? 1008 GLN   B C     1 
ATOM   16483 O  O     . GLN   B  1  1010 ? 7.753   38.883  81.464  1.00 14.65 ? 1008 GLN   B O     1 
ATOM   16484 C  CB    . GLN   B  1  1010 ? 6.810   38.589  84.023  1.00 15.21 ? 1008 GLN   B CB    1 
ATOM   16485 C  CG    . GLN   B  1  1010 ? 6.087   38.221  85.297  1.00 15.33 ? 1008 GLN   B CG    1 
ATOM   16486 C  CD    . GLN   B  1  1010 ? 5.667   36.767  85.327  1.00 15.51 ? 1008 GLN   B CD    1 
ATOM   16487 O  OE1   . GLN   B  1  1010 ? 6.380   35.881  84.860  1.00 15.37 ? 1008 GLN   B OE1   1 
ATOM   16488 N  NE2   . GLN   B  1  1010 ? 4.514   36.512  85.918  1.00 15.20 ? 1008 GLN   B NE2   1 
ATOM   16489 N  N     . PRO   B  1  1011 ? 6.301   40.490  80.871  1.00 13.28 ? 1009 PRO   B N     1 
ATOM   16490 C  CA    . PRO   B  1  1011 ? 7.166   40.968  79.784  1.00 14.94 ? 1009 PRO   B CA    1 
ATOM   16491 C  C     . PRO   B  1  1011 ? 8.540   41.246  80.357  1.00 12.44 ? 1009 PRO   B C     1 
ATOM   16492 O  O     . PRO   B  1  1011 ? 8.678   41.864  81.415  1.00 11.79 ? 1009 PRO   B O     1 
ATOM   16493 C  CB    . PRO   B  1  1011 ? 6.476   42.257  79.332  1.00 12.89 ? 1009 PRO   B CB    1 
ATOM   16494 C  CG    . PRO   B  1  1011 ? 5.053   42.017  79.637  1.00 14.07 ? 1009 PRO   B CG    1 
ATOM   16495 C  CD    . PRO   B  1  1011 ? 5.061   41.275  80.954  1.00 14.33 ? 1009 PRO   B CD    1 
ATOM   16496 N  N     . PHE   B  1  1012 ? 9.554   40.722  79.706  1.00 11.43 ? 1010 PHE   B N     1 
ATOM   16497 C  CA    . PHE   B  1  1012 ? 10.833  40.547  80.356  1.00 11.89 ? 1010 PHE   B CA    1 
ATOM   16498 C  C     . PHE   B  1  1012 ? 11.887  41.420  79.694  1.00 12.46 ? 1010 PHE   B C     1 
ATOM   16499 O  O     . PHE   B  1  1012 ? 12.030  41.416  78.469  1.00 13.57 ? 1010 PHE   B O     1 
ATOM   16500 C  CB    . PHE   B  1  1012 ? 11.276  39.086  80.334  1.00 12.74 ? 1010 PHE   B CB    1 
ATOM   16501 C  CG    . PHE   B  1  1012 ? 12.500  38.863  81.135  1.00 11.83 ? 1010 PHE   B CG    1 
ATOM   16502 C  CD1   . PHE   B  1  1012 ? 12.413  38.699  82.501  1.00 14.23 ? 1010 PHE   B CD1   1 
ATOM   16503 C  CD2   . PHE   B  1  1012 ? 13.748  38.906  80.551  1.00 13.35 ? 1010 PHE   B CD2   1 
ATOM   16504 C  CE1   . PHE   B  1  1012 ? 13.556  38.529  83.263  1.00 13.28 ? 1010 PHE   B CE1   1 
ATOM   16505 C  CE2   . PHE   B  1  1012 ? 14.902  38.749  81.313  1.00 14.25 ? 1010 PHE   B CE2   1 
ATOM   16506 C  CZ    . PHE   B  1  1012 ? 14.799  38.556  82.671  1.00 13.97 ? 1010 PHE   B CZ    1 
ATOM   16507 N  N     . GLY   B  1  1013 ? 12.625  42.141  80.503  1.00 11.93 ? 1011 GLY   B N     1 
ATOM   16508 C  CA    . GLY   B  1  1013 ? 13.739  42.912  79.989  1.00 12.70 ? 1011 GLY   B CA    1 
ATOM   16509 C  C     . GLY   B  1  1013 ? 13.998  44.086  80.895  1.00 11.60 ? 1011 GLY   B C     1 
ATOM   16510 O  O     . GLY   B  1  1013 ? 13.097  44.615  81.543  1.00 13.08 ? 1011 GLY   B O     1 
ATOM   16511 N  N     . GLY   B  1  1014 ? 15.254  44.498  80.924  1.00 13.12 ? 1012 GLY   B N     1 
ATOM   16512 C  CA    . GLY   B  1  1014 ? 15.645  45.546  81.832  1.00 15.43 ? 1012 GLY   B CA    1 
ATOM   16513 C  C     . GLY   B  1  1014 ? 16.205  46.775  81.174  1.00 15.07 ? 1012 GLY   B C     1 
ATOM   16514 O  O     . GLY   B  1  1014 ? 16.080  46.979  79.962  1.00 16.92 ? 1012 GLY   B O     1 
ATOM   16515 N  N     . ARG   B  1  1015 ? 16.835  47.601  81.992  1.00 14.41 ? 1013 ARG   B N     1 
ATOM   16516 C  CA    . ARG   B  1  1015 ? 17.317  48.913  81.614  1.00 15.34 ? 1013 ARG   B CA    1 
ATOM   16517 C  C     . ARG   B  1  1015 ? 18.777  49.019  82.018  1.00 15.20 ? 1013 ARG   B C     1 
ATOM   16518 O  O     . ARG   B  1  1015 ? 19.354  48.088  82.584  1.00 14.18 ? 1013 ARG   B O     1 
ATOM   16519 C  CB    . ARG   B  1  1015 ? 16.490  49.993  82.324  1.00 14.72 ? 1013 ARG   B CB    1 
ATOM   16520 C  CG    . ARG   B  1  1015 ? 16.518  49.829  83.846  1.00 15.70 ? 1013 ARG   B CG    1 
ATOM   16521 C  CD    . ARG   B  1  1015 ? 16.456  51.167  84.578  1.00 20.76 ? 1013 ARG   B CD    1 
ATOM   16522 N  NE    . ARG   B  1  1015 ? 17.759  51.831  84.558  1.00 23.42 ? 1013 ARG   B NE    1 
ATOM   16523 C  CZ    . ARG   B  1  1015 ? 18.776  51.516  85.350  1.00 22.44 ? 1013 ARG   B CZ    1 
ATOM   16524 N  NH1   . ARG   B  1  1015 ? 18.675  50.566  86.270  1.00 21.90 ? 1013 ARG   B NH1   1 
ATOM   16525 N  NH2   . ARG   B  1  1015 ? 19.932  52.162  85.210  1.00 23.48 ? 1013 ARG   B NH2   1 
ATOM   16526 N  N     . GLY   B  1  1016 ? 19.371  50.173  81.736  1.00 15.41 ? 1014 GLY   B N     1 
ATOM   16527 C  CA    . GLY   B  1  1016 ? 20.773  50.358  82.071  1.00 14.76 ? 1014 GLY   B CA    1 
ATOM   16528 C  C     . GLY   B  1  1016 ? 21.630  49.379  81.301  1.00 15.38 ? 1014 GLY   B C     1 
ATOM   16529 O  O     . GLY   B  1  1016 ? 21.418  49.152  80.103  1.00 16.18 ? 1014 GLY   B O     1 
ATOM   16530 N  N     . LEU   B  1  1017 ? 22.582  48.760  81.993  1.00 14.41 ? 1015 LEU   B N     1 
ATOM   16531 C  CA    . LEU   B  1  1017 ? 23.434  47.763  81.372  1.00 15.89 ? 1015 LEU   B CA    1 
ATOM   16532 C  C     . LEU   B  1  1017 ? 22.695  46.493  81.036  1.00 14.63 ? 1015 LEU   B C     1 
ATOM   16533 O  O     . LEU   B  1  1017 ? 23.304  45.604  80.433  1.00 14.85 ? 1015 LEU   B O     1 
ATOM   16534 C  CB    . LEU   B  1  1017 ? 24.596  47.416  82.298  1.00 15.40 ? 1015 LEU   B CB    1 
ATOM   16535 C  CG    . LEU   B  1  1017 ? 25.507  48.589  82.651  1.00 16.80 ? 1015 LEU   B CG    1 
ATOM   16536 C  CD1   . LEU   B  1  1017 ? 26.534  48.138  83.676  1.00 18.66 ? 1015 LEU   B CD1   1 
ATOM   16537 C  CD2   . LEU   B  1  1017 ? 26.195  49.065  81.394  1.00 19.44 ? 1015 LEU   B CD2   1 
ATOM   16538 N  N     . SER   B  1  1018 ? 21.421  46.379  81.409  1.00 12.49 ? 1016 SER   B N     1 
ATOM   16539 C  CA    . SER   B  1  1018 ? 20.666  45.161  81.180  1.00 12.48 ? 1016 SER   B CA    1 
ATOM   16540 C  C     . SER   B  1  1018 ? 19.842  45.175  79.908  1.00 13.01 ? 1016 SER   B C     1 
ATOM   16541 O  O     . SER   B  1  1018 ? 19.328  44.127  79.531  1.00 13.39 ? 1016 SER   B O     1 
ATOM   16542 C  CB    . SER   B  1  1018 ? 19.699  44.910  82.343  1.00 12.98 ? 1016 SER   B CB    1 
ATOM   16543 O  OG    . SER   B  1  1018 ? 20.442  44.735  83.536  1.00 13.23 ? 1016 SER   B OG    1 
ATOM   16544 N  N     . GLY   B  1  1019 ? 19.679  46.309  79.251  1.00 13.01 ? 1017 GLY   B N     1 
ATOM   16545 C  CA    . GLY   B  1  1019 ? 18.865  46.245  78.056  1.00 14.33 ? 1017 GLY   B CA    1 
ATOM   16546 C  C     . GLY   B  1  1019 ? 18.633  47.569  77.389  1.00 13.47 ? 1017 GLY   B C     1 
ATOM   16547 O  O     . GLY   B  1  1019 ? 18.668  48.617  78.034  1.00 14.81 ? 1017 GLY   B O     1 
ATOM   16548 N  N     . THR   B  1  1020 ? 18.385  47.520  76.080  1.00 14.60 ? 1018 THR   B N     1 
ATOM   16549 C  CA    . THR   B  1  1020 ? 17.829  48.644  75.346  1.00 13.77 ? 1018 THR   B CA    1 
ATOM   16550 C  C     . THR   B  1  1020 ? 16.315  48.656  75.381  1.00 13.64 ? 1018 THR   B C     1 
ATOM   16551 O  O     . THR   B  1  1020 ? 15.710  49.715  75.183  1.00 14.87 ? 1018 THR   B O     1 
ATOM   16552 C  CB    . THR   B  1  1020 ? 18.228  48.544  73.869  1.00 13.50 ? 1018 THR   B CB    1 
ATOM   16553 O  OG1   . THR   B  1  1020 ? 17.820  47.273  73.334  1.00 13.85 ? 1018 THR   B OG1   1 
ATOM   16554 C  CG2   . THR   B  1  1020 ? 19.733  48.676  73.705  1.00 14.16 ? 1018 THR   B CG2   1 
ATOM   16555 N  N     . GLY   B  1  1021 ? 15.693  47.510  75.598  1.00 14.43 ? 1019 GLY   B N     1 
ATOM   16556 C  CA    . GLY   B  1  1021 ? 14.289  47.375  75.314  1.00 13.54 ? 1019 GLY   B CA    1 
ATOM   16557 C  C     . GLY   B  1  1021 ? 14.075  47.403  73.811  1.00 13.89 ? 1019 GLY   B C     1 
ATOM   16558 O  O     . GLY   B  1  1021 ? 15.021  47.555  73.031  1.00 13.35 ? 1019 GLY   B O     1 
ATOM   16559 N  N     . PRO   B  1  1022 ? 12.835  47.250  73.378  1.00 12.79 ? 1020 PRO   B N     1 
ATOM   16560 C  CA    . PRO   B  1  1022 ? 11.654  46.975  74.200  1.00 13.25 ? 1020 PRO   B CA    1 
ATOM   16561 C  C     . PRO   B  1  1022 ? 11.701  45.554  74.761  1.00 14.25 ? 1020 PRO   B C     1 
ATOM   16562 O  O     . PRO   B  1  1022 ? 12.490  44.720  74.317  1.00 15.47 ? 1020 PRO   B O     1 
ATOM   16563 C  CB    . PRO   B  1  1022 ? 10.508  47.151  73.201  1.00 16.54 ? 1020 PRO   B CB    1 
ATOM   16564 C  CG    . PRO   B  1  1022 ? 11.101  46.725  71.904  1.00 15.45 ? 1020 PRO   B CG    1 
ATOM   16565 C  CD    . PRO   B  1  1022 ? 12.514  47.247  71.940  1.00 13.27 ? 1020 PRO   B CD    1 
ATOM   16566 N  N     . LYS   B  1  1023 ? 10.853  45.274  75.749  1.00 12.94 ? 1021 LYS   B N     1 
ATOM   16567 C  CA    . LYS   B  1  1023 ? 10.862  43.970  76.390  1.00 13.28 ? 1021 LYS   B CA    1 
ATOM   16568 C  C     . LYS   B  1  1023 ? 10.380  42.879  75.451  1.00 13.12 ? 1021 LYS   B C     1 
ATOM   16569 O  O     . LYS   B  1  1023 ? 9.327   43.004  74.814  1.00 13.37 ? 1021 LYS   B O     1 
ATOM   16570 C  CB    . LYS   B  1  1023 ? 9.909   43.977  77.571  1.00 12.29 ? 1021 LYS   B CB    1 
ATOM   16571 C  CG    . LYS   B  1  1023 ? 10.366  44.752  78.769  1.00 11.98 ? 1021 LYS   B CG    1 
ATOM   16572 C  CD    . LYS   B  1  1023 ? 9.229   44.728  79.765  1.00 11.17 ? 1021 LYS   B CD    1 
ATOM   16573 C  CE    . LYS   B  1  1023 ? 9.620   45.268  81.134  1.00 13.50 ? 1021 LYS   B CE    1 
ATOM   16574 N  NZ    . LYS   B  1  1023 ? 10.337  44.219  81.903  1.00 12.70 ? 1021 LYS   B NZ    1 
ATOM   16575 N  N     . ALA   B  1  1024 ? 11.117  41.779  75.416  1.00 13.51 ? 1022 ALA   B N     1 
ATOM   16576 C  CA    . ALA   B  1  1024 ? 10.614  40.550  74.830  1.00 12.81 ? 1022 ALA   B CA    1 
ATOM   16577 C  C     . ALA   B  1  1024 ? 9.373   40.096  75.581  1.00 13.90 ? 1022 ALA   B C     1 
ATOM   16578 O  O     . ALA   B  1  1024 ? 9.232   40.315  76.788  1.00 13.66 ? 1022 ALA   B O     1 
ATOM   16579 C  CB    . ALA   B  1  1024 ? 11.709  39.477  74.886  1.00 14.76 ? 1022 ALA   B CB    1 
ATOM   16580 N  N     . GLY   B  1  1025 ? 8.448   39.482  74.855  1.00 12.02 ? 1023 GLY   B N     1 
ATOM   16581 C  CA    . GLY   B  1  1025 ? 7.247   38.996  75.498  1.00 13.95 ? 1023 GLY   B CA    1 
ATOM   16582 C  C     . GLY   B  1  1025 ? 6.347   40.103  75.960  1.00 12.83 ? 1023 GLY   B C     1 
ATOM   16583 O  O     . GLY   B  1  1025 ? 5.471   39.878  76.788  1.00 13.17 ? 1023 GLY   B O     1 
ATOM   16584 N  N     . GLY   B  1  1026 ? 6.524   41.295  75.405  1.00 13.36 ? 1024 GLY   B N     1 
ATOM   16585 C  CA    . GLY   B  1  1026 ? 5.698   42.431  75.721  1.00 13.09 ? 1024 GLY   B CA    1 
ATOM   16586 C  C     . GLY   B  1  1026 ? 5.200   43.096  74.456  1.00 13.70 ? 1024 GLY   B C     1 
ATOM   16587 O  O     . GLY   B  1  1026 ? 5.619   42.784  73.337  1.00 13.02 ? 1024 GLY   B O     1 
ATOM   16588 N  N     . PRO   B  1  1027 ? 4.305   44.061  74.625  1.00 13.62 ? 1025 PRO   B N     1 
ATOM   16589 C  CA    . PRO   B  1  1027 ? 3.549   44.586  73.485  1.00 12.80 ? 1025 PRO   B CA    1 
ATOM   16590 C  C     . PRO   B  1  1027 ? 4.292   45.607  72.646  1.00 12.54 ? 1025 PRO   B C     1 
ATOM   16591 O  O     . PRO   B  1  1027 ? 3.792   45.968  71.576  1.00 12.71 ? 1025 PRO   B O     1 
ATOM   16592 C  CB    . PRO   B  1  1027 ? 2.322   45.218  74.155  1.00 13.80 ? 1025 PRO   B CB    1 
ATOM   16593 C  CG    . PRO   B  1  1027 ? 2.799   45.581  75.531  1.00 15.77 ? 1025 PRO   B CG    1 
ATOM   16594 C  CD    . PRO   B  1  1027 ? 3.757   44.495  75.919  1.00 13.99 ? 1025 PRO   B CD    1 
ATOM   16595 N  N     . LEU   B  1  1028 ? 5.448   46.090  73.085  1.00 12.95 ? 1026 LEU   B N     1 
ATOM   16596 C  CA    . LEU   B  1  1028 ? 6.207   47.044  72.288  1.00 12.87 ? 1026 LEU   B CA    1 
ATOM   16597 C  C     . LEU   B  1  1028 ? 7.196   46.366  71.361  1.00 13.86 ? 1026 LEU   B C     1 
ATOM   16598 O  O     . LEU   B  1  1028 ? 7.786   47.035  70.513  1.00 15.09 ? 1026 LEU   B O     1 
ATOM   16599 C  CB    . LEU   B  1  1028 ? 6.978   48.004  73.197  1.00 13.44 ? 1026 LEU   B CB    1 
ATOM   16600 C  CG    . LEU   B  1  1028 ? 6.105   48.807  74.146  1.00 17.18 ? 1026 LEU   B CG    1 
ATOM   16601 C  CD1   . LEU   B  1  1028 ? 6.954   49.796  74.910  1.00 18.29 ? 1026 LEU   B CD1   1 
ATOM   16602 C  CD2   . LEU   B  1  1028 ? 5.076   49.532  73.364  1.00 22.16 ? 1026 LEU   B CD2   1 
ATOM   16603 N  N     . TYR   B  1  1029 ? 7.374   45.059  71.503  1.00 12.06 ? 1027 TYR   B N     1 
ATOM   16604 C  CA    . TYR   B  1  1029 ? 8.502   44.383  70.877  1.00 12.29 ? 1027 TYR   B CA    1 
ATOM   16605 C  C     . TYR   B  1  1029 ? 8.391   44.392  69.364  1.00 12.05 ? 1027 TYR   B C     1 
ATOM   16606 O  O     . TYR   B  1  1029 ? 9.352   44.741  68.675  1.00 12.31 ? 1027 TYR   B O     1 
ATOM   16607 C  CB    . TYR   B  1  1029 ? 8.515   42.953  71.373  1.00 12.44 ? 1027 TYR   B CB    1 
ATOM   16608 C  CG    . TYR   B  1  1029 ? 9.785   42.174  71.231  1.00 12.94 ? 1027 TYR   B CG    1 
ATOM   16609 C  CD1   . TYR   B  1  1029 ? 10.928  42.511  71.953  1.00 11.89 ? 1027 TYR   B CD1   1 
ATOM   16610 C  CD2   . TYR   B  1  1029 ? 9.810   41.011  70.474  1.00 13.30 ? 1027 TYR   B CD2   1 
ATOM   16611 C  CE1   . TYR   B  1  1029 ? 12.069  41.744  71.865  1.00 13.16 ? 1027 TYR   B CE1   1 
ATOM   16612 C  CE2   . TYR   B  1  1029 ? 10.946  40.241  70.401  1.00 12.22 ? 1027 TYR   B CE2   1 
ATOM   16613 C  CZ    . TYR   B  1  1029 ? 12.062  40.603  71.096  1.00 11.34 ? 1027 TYR   B CZ    1 
ATOM   16614 O  OH    . TYR   B  1  1029 ? 13.150  39.784  71.018  1.00 13.79 ? 1027 TYR   B OH    1 
ATOM   16615 N  N     . LEU   B  1  1030 ? 7.241   43.972  68.824  1.00 12.13 ? 1028 LEU   B N     1 
ATOM   16616 C  CA    . LEU   B  1  1030 ? 7.153   43.817  67.375  1.00 12.13 ? 1028 LEU   B CA    1 
ATOM   16617 C  C     . LEU   B  1  1030 ? 7.326   45.145  66.671  1.00 13.48 ? 1028 LEU   B C     1 
ATOM   16618 O  O     . LEU   B  1  1030 ? 7.852   45.195  65.555  1.00 13.39 ? 1028 LEU   B O     1 
ATOM   16619 C  CB    . LEU   B  1  1030 ? 5.816   43.196  66.985  1.00 13.30 ? 1028 LEU   B CB    1 
ATOM   16620 C  CG    . LEU   B  1  1030 ? 5.567   41.755  67.421  1.00 14.88 ? 1028 LEU   B CG    1 
ATOM   16621 C  CD1   . LEU   B  1  1030 ? 4.229   41.270  66.905  1.00 17.57 ? 1028 LEU   B CD1   1 
ATOM   16622 C  CD2   . LEU   B  1  1030 ? 6.688   40.854  66.902  1.00 16.58 ? 1028 LEU   B CD2   1 
ATOM   16623 N  N     . GLY   B  1  1031 ? 6.920   46.238  67.311  1.00 14.20 ? 1029 GLY   B N     1 
ATOM   16624 C  CA    . GLY   B  1  1031 ? 7.005   47.539  66.675  1.00 13.77 ? 1029 GLY   B CA    1 
ATOM   16625 C  C     . GLY   B  1  1031 ? 8.421   48.001  66.415  1.00 13.90 ? 1029 GLY   B C     1 
ATOM   16626 O  O     . GLY   B  1  1031 ? 8.625   48.924  65.622  1.00 15.46 ? 1029 GLY   B O     1 
ATOM   16627 N  N     . ARG   B  1  1032 ? 9.398   47.397  67.075  1.00 12.62 ? 1030 ARG   B N     1 
ATOM   16628 C  CA    . ARG   B  1  1032 ? 10.782  47.724  66.801  1.00 11.80 ? 1030 ARG   B CA    1 
ATOM   16629 C  C     . ARG   B  1  1032 ? 11.283  47.060  65.531  1.00 14.02 ? 1030 ARG   B C     1 
ATOM   16630 O  O     . ARG   B  1  1032 ? 12.360  47.416  65.028  1.00 15.00 ? 1030 ARG   B O     1 
ATOM   16631 C  CB    . ARG   B  1  1032 ? 11.621  47.287  68.007  1.00 13.56 ? 1030 ARG   B CB    1 
ATOM   16632 C  CG    . ARG   B  1  1032 ? 13.048  47.782  67.996  1.00 14.82 ? 1030 ARG   B CG    1 
ATOM   16633 C  CD    . ARG   B  1  1032 ? 13.107  49.274  68.249  1.00 15.52 ? 1030 ARG   B CD    1 
ATOM   16634 N  NE    . ARG   B  1  1032 ? 14.482  49.709  68.440  1.00 16.13 ? 1030 ARG   B NE    1 
ATOM   16635 C  CZ    . ARG   B  1  1032 ? 15.075  50.671  67.749  1.00 18.72 ? 1030 ARG   B CZ    1 
ATOM   16636 N  NH1   . ARG   B  1  1032 ? 14.448  51.315  66.777  1.00 19.20 ? 1030 ARG   B NH1   1 
ATOM   16637 N  NH2   . ARG   B  1  1032 ? 16.329  50.997  68.046  1.00 19.44 ? 1030 ARG   B NH2   1 
ATOM   16638 N  N     . LEU   B  1  1033 ? 10.544  46.085  65.011  1.00 13.74 ? 1031 LEU   B N     1 
ATOM   16639 C  CA    . LEU   B  1  1033 ? 10.990  45.252  63.909  1.00 13.44 ? 1031 LEU   B CA    1 
ATOM   16640 C  C     . LEU   B  1  1033 ? 10.313  45.630  62.605  1.00 13.36 ? 1031 LEU   B C     1 
ATOM   16641 O  O     . LEU   B  1  1033 ? 10.358  44.859  61.639  1.00 14.54 ? 1031 LEU   B O     1 
ATOM   16642 C  CB    . LEU   B  1  1033 ? 10.746  43.784  64.249  1.00 13.89 ? 1031 LEU   B CB    1 
ATOM   16643 C  CG    . LEU   B  1  1033 ? 11.292  43.402  65.624  1.00 13.46 ? 1031 LEU   B CG    1 
ATOM   16644 C  CD1   . LEU   B  1  1033 ? 10.964  41.971  65.951  1.00 14.07 ? 1031 LEU   B CD1   1 
ATOM   16645 C  CD2   . LEU   B  1  1033 ? 12.792  43.623  65.715  1.00 15.37 ? 1031 LEU   B CD2   1 
ATOM   16646 N  N     . VAL   B  1  1034 ? 9.658   46.786  62.576  1.00 13.70 ? 1032 VAL   B N     1 
ATOM   16647 C  CA    . VAL   B  1  1034 ? 9.041   47.332  61.380  1.00 15.14 ? 1032 VAL   B CA    1 
ATOM   16648 C  C     . VAL   B  1  1034 ? 9.467   48.785  61.285  1.00 16.77 ? 1032 VAL   B C     1 
ATOM   16649 O  O     . VAL   B  1  1034 ? 9.929   49.379  62.256  1.00 18.02 ? 1032 VAL   B O     1 
ATOM   16650 C  CB    . VAL   B  1  1034 ? 7.510   47.208  61.419  1.00 14.97 ? 1032 VAL   B CB    1 
ATOM   16651 C  CG1   . VAL   B  1  1034 ? 7.093   45.746  61.297  1.00 16.89 ? 1032 VAL   B CG1   1 
ATOM   16652 C  CG2   . VAL   B  1  1034 ? 6.959   47.810  62.704  1.00 15.98 ? 1032 VAL   B CG2   1 
ATOM   16653 N  N     . THR   B  1  1035 ? 9.327   49.361  60.094  1.00 17.43 ? 1033 THR   B N     1 
ATOM   16654 C  CA    . THR   B  1  1035 ? 9.853   50.708  59.919  1.00 20.38 ? 1033 THR   B CA    1 
ATOM   16655 C  C     . THR   B  1  1035 ? 8.930   51.779  60.471  1.00 20.04 ? 1033 THR   B C     1 
ATOM   16656 O  O     . THR   B  1  1035 ? 9.387   52.898  60.725  1.00 24.55 ? 1033 THR   B O     1 
ATOM   16657 C  CB    . THR   B  1  1035 ? 10.191  50.982  58.457  1.00 24.52 ? 1033 THR   B CB    1 
ATOM   16658 O  OG1   . THR   B  1  1035 ? 9.101   50.555  57.639  1.00 28.40 ? 1033 THR   B OG1   1 
ATOM   16659 C  CG2   . THR   B  1  1035 ? 11.445  50.222  58.063  1.00 27.15 ? 1033 THR   B CG2   1 
ATOM   16660 N  N     . THR   B  1  1036 ? 7.653   51.463  60.665  1.00 16.62 ? 1034 THR   B N     1 
ATOM   16661 C  CA    . THR   B  1  1036 ? 6.700   52.345  61.319  1.00 21.05 ? 1034 THR   B CA    1 
ATOM   16662 C  C     . THR   B  1  1036 ? 6.014   51.517  62.391  1.00 20.59 ? 1034 THR   B C     1 
ATOM   16663 O  O     . THR   B  1  1036 ? 5.386   50.501  62.079  1.00 18.87 ? 1034 THR   B O     1 
ATOM   16664 C  CB    . THR   B  1  1036 ? 5.665   52.843  60.314  1.00 24.76 ? 1034 THR   B CB    1 
ATOM   16665 O  OG1   . THR   B  1  1036 ? 6.336   53.430  59.192  1.00 31.30 ? 1034 THR   B OG1   1 
ATOM   16666 C  CG2   . THR   B  1  1036 ? 4.741   53.876  60.960  1.00 28.26 ? 1034 THR   B CG2   1 
ATOM   16667 N  N     . ALA   B  1  1037 ? 6.149   51.930  63.648  1.00 18.97 ? 1035 ALA   B N     1 
ATOM   16668 C  CA    . ALA   B  1  1037 ? 5.617   51.117  64.735  1.00 17.02 ? 1035 ALA   B CA    1 
ATOM   16669 C  C     . ALA   B  1  1037 ? 4.098   51.247  64.796  1.00 17.67 ? 1035 ALA   B C     1 
ATOM   16670 O  O     . ALA   B  1  1037 ? 3.563   52.350  64.667  1.00 18.55 ? 1035 ALA   B O     1 
ATOM   16671 C  CB    . ALA   B  1  1037 ? 6.222   51.547  66.069  1.00 19.91 ? 1035 ALA   B CB    1 
ATOM   16672 N  N     . PRO   B  1  1038 ? 3.385   50.148  64.992  1.00 15.07 ? 1036 PRO   B N     1 
ATOM   16673 C  CA    . PRO   B  1  1038 ? 1.947   50.225  65.238  1.00 15.94 ? 1036 PRO   B CA    1 
ATOM   16674 C  C     . PRO   B  1  1038 ? 1.680   50.691  66.660  1.00 14.90 ? 1036 PRO   B C     1 
ATOM   16675 O  O     . PRO   B  1  1038 ? 2.569   50.789  67.502  1.00 15.47 ? 1036 PRO   B O     1 
ATOM   16676 C  CB    . PRO   B  1  1038 ? 1.492   48.773  65.068  1.00 16.76 ? 1036 PRO   B CB    1 
ATOM   16677 C  CG    . PRO   B  1  1038 ? 2.662   47.977  65.522  1.00 18.31 ? 1036 PRO   B CG    1 
ATOM   16678 C  CD    . PRO   B  1  1038 ? 3.889   48.764  65.063  1.00 15.66 ? 1036 PRO   B CD    1 
ATOM   16679 N  N     . VAL   B  1  1039 ? 0.404   50.957  66.922  1.00 15.76 ? 1037 VAL   B N     1 
ATOM   16680 C  CA    . VAL   B  1  1039 ? -0.077  51.241  68.268  1.00 15.79 ? 1037 VAL   B CA    1 
ATOM   16681 C  C     . VAL   B  1  1039 ? -0.355  49.897  68.939  1.00 16.51 ? 1037 VAL   B C     1 
ATOM   16682 O  O     . VAL   B  1  1039 ? -1.252  49.173  68.488  1.00 15.50 ? 1037 VAL   B O     1 
ATOM   16683 C  CB    . VAL   B  1  1039 ? -1.342  52.100  68.233  1.00 16.67 ? 1037 VAL   B CB    1 
ATOM   16684 C  CG1   . VAL   B  1  1039 ? -1.817  52.330  69.659  1.00 19.51 ? 1037 VAL   B CG1   1 
ATOM   16685 C  CG2   . VAL   B  1  1039 ? -1.040  53.414  67.526  1.00 19.21 ? 1037 VAL   B CG2   1 
ATOM   16686 N  N     . PRO   B  1  1040 ? 0.385   49.521  69.967  1.00 15.40 ? 1038 PRO   B N     1 
ATOM   16687 C  CA    . PRO   B  1  1040 ? 0.177   48.207  70.558  1.00 15.34 ? 1038 PRO   B CA    1 
ATOM   16688 C  C     . PRO   B  1  1040 ? -1.169  48.123  71.249  1.00 14.21 ? 1038 PRO   B C     1 
ATOM   16689 O  O     . PRO   B  1  1040 ? -1.760  49.148  71.625  1.00 14.60 ? 1038 PRO   B O     1 
ATOM   16690 C  CB    . PRO   B  1  1040 ? 1.322   48.101  71.575  1.00 16.67 ? 1038 PRO   B CB    1 
ATOM   16691 C  CG    . PRO   B  1  1040 ? 2.361   49.072  71.089  1.00 18.95 ? 1038 PRO   B CG    1 
ATOM   16692 C  CD    . PRO   B  1  1040 ? 1.579   50.200  70.505  1.00 16.62 ? 1038 PRO   B CD    1 
ATOM   16693 N  N     . PRO   B  1  1041 ? -1.690  46.915  71.436  1.00 15.75 ? 1039 PRO   B N     1 
ATOM   16694 C  CA    . PRO   B  1  1041 ? -2.906  46.752  72.229  1.00 15.99 ? 1039 PRO   B CA    1 
ATOM   16695 C  C     . PRO   B  1  1041 ? -2.742  47.402  73.593  1.00 14.21 ? 1039 PRO   B C     1 
ATOM   16696 O  O     . PRO   B  1  1041 ? -1.673  47.324  74.209  1.00 16.81 ? 1039 PRO   B O     1 
ATOM   16697 C  CB    . PRO   B  1  1041 ? -3.044  45.232  72.356  1.00 16.54 ? 1039 PRO   B CB    1 
ATOM   16698 C  CG    . PRO   B  1  1041 ? -2.268  44.688  71.189  1.00 19.71 ? 1039 PRO   B CG    1 
ATOM   16699 C  CD    . PRO   B  1  1041 ? -1.121  45.624  71.011  1.00 17.54 ? 1039 PRO   B CD    1 
ATOM   16700 N  N     . GLN   B  1  1042 ? -3.795  48.082  74.040  1.00 15.15 ? 1040 GLN   B N     1 
ATOM   16701 C  CA    . GLN   B  1  1042 ? -3.865  48.682  75.369  1.00 16.83 ? 1040 GLN   B CA    1 
ATOM   16702 C  C     . GLN   B  1  1042 ? -2.858  49.804  75.584  1.00 15.65 ? 1040 GLN   B C     1 
ATOM   16703 O  O     . GLN   B  1  1042 ? -2.675  50.255  76.718  1.00 15.95 ? 1040 GLN   B O     1 
ATOM   16704 C  CB    . GLN   B  1  1042 ? -3.708  47.628  76.479  1.00 18.74 ? 1040 GLN   B CB    1 
ATOM   16705 C  CG    . GLN   B  1  1042 ? -4.683  46.471  76.383  1.00 23.07 ? 1040 GLN   B CG    1 
ATOM   16706 C  CD    . GLN   B  1  1042 ? -4.446  45.451  77.485  1.00 27.47 ? 1040 GLN   B CD    1 
ATOM   16707 O  OE1   . GLN   B  1  1042 ? -5.316  45.216  78.316  1.00 40.71 ? 1040 GLN   B OE1   1 
ATOM   16708 N  NE2   . GLN   B  1  1042 ? -3.252  44.858  77.505  1.00 35.25 ? 1040 GLN   B NE2   1 
ATOM   16709 N  N     . HIS   B  1  1043 ? -2.177  50.265  74.544  1.00 14.92 ? 1041 HIS   B N     1 
ATOM   16710 C  CA    . HIS   B  1  1043 ? -1.072  51.201  74.719  1.00 14.97 ? 1041 HIS   B CA    1 
ATOM   16711 C  C     . HIS   B  1  1043 ? -1.613  52.620  74.641  1.00 14.61 ? 1041 HIS   B C     1 
ATOM   16712 O  O     . HIS   B  1  1043 ? -1.710  53.215  73.569  1.00 16.54 ? 1041 HIS   B O     1 
ATOM   16713 C  CB    . HIS   B  1  1043 ? -0.027  50.946  73.649  1.00 15.73 ? 1041 HIS   B CB    1 
ATOM   16714 C  CG    . HIS   B  1  1043 ? 1.172   51.835  73.737  1.00 15.76 ? 1041 HIS   B CG    1 
ATOM   16715 N  ND1   . HIS   B  1  1043 ? 2.252   51.558  74.548  1.00 16.85 ? 1041 HIS   B ND1   1 
ATOM   16716 C  CD2   . HIS   B  1  1043 ? 1.465   52.994  73.103  1.00 17.00 ? 1041 HIS   B CD2   1 
ATOM   16717 C  CE1   . HIS   B  1  1043 ? 3.165   52.502  74.401  1.00 15.34 ? 1041 HIS   B CE1   1 
ATOM   16718 N  NE2   . HIS   B  1  1043 ? 2.719   53.376  73.516  1.00 15.39 ? 1041 HIS   B NE2   1 
ATOM   16719 N  N     . SER   B  1  1044 ? -1.972  53.171  75.795  1.00 13.47 ? 1042 SER   B N     1 
ATOM   16720 C  CA    . SER   B  1  1044 ? -2.414  54.551  75.883  1.00 13.76 ? 1042 SER   B CA    1 
ATOM   16721 C  C     . SER   B  1  1044 ? -2.362  54.944  77.342  1.00 13.41 ? 1042 SER   B C     1 
ATOM   16722 O  O     . SER   B  1  1044 ? -2.209  54.106  78.232  1.00 14.43 ? 1042 SER   B O     1 
ATOM   16723 C  CB    . SER   B  1  1044 ? -3.841  54.727  75.358  1.00 15.10 ? 1042 SER   B CB    1 
ATOM   16724 O  OG    . SER   B  1  1044 ? -4.769  54.087  76.212  1.00 16.14 ? 1042 SER   B OG    1 
ATOM   16725 N  N     . SER   B  1  1045 ? -2.523  56.233  77.581  1.00 13.94 ? 1043 SER   B N     1 
ATOM   16726 C  CA    . SER   B  1  1045 ? -2.575  56.727  78.941  1.00 13.13 ? 1043 SER   B CA    1 
ATOM   16727 C  C     . SER   B  1  1045 ? -3.422  57.980  78.948  1.00 15.00 ? 1043 SER   B C     1 
ATOM   16728 O  O     . SER   B  1  1045 ? -3.372  58.772  78.007  1.00 15.75 ? 1043 SER   B O     1 
ATOM   16729 C  CB    . SER   B  1  1045 ? -1.164  57.086  79.389  1.00 14.77 ? 1043 SER   B CB    1 
ATOM   16730 O  OG    . SER   B  1  1045 ? -1.186  57.722  80.643  1.00 15.78 ? 1043 SER   B OG    1 
ATOM   16731 N  N     . VAL   B  1  1046 ? -4.214  58.157  80.009  1.00 14.42 ? 1044 VAL   B N     1 
ATOM   16732 C  CA    . VAL   B  1  1046 ? -4.989  59.389  80.138  1.00 15.87 ? 1044 VAL   B CA    1 
ATOM   16733 C  C     . VAL   B  1  1046 ? -4.182  60.516  80.749  1.00 17.47 ? 1044 VAL   B C     1 
ATOM   16734 O  O     . VAL   B  1  1046 ? -4.673  61.649  80.815  1.00 17.88 ? 1044 VAL   B O     1 
ATOM   16735 C  CB    . VAL   B  1  1046 ? -6.295  59.189  80.931  1.00 18.61 ? 1044 VAL   B CB    1 
ATOM   16736 C  CG1   . VAL   B  1  1046 ? -7.129  58.104  80.260  1.00 21.98 ? 1044 VAL   B CG1   1 
ATOM   16737 C  CG2   . VAL   B  1  1046 ? -5.983  58.825  82.355  1.00 19.12 ? 1044 VAL   B CG2   1 
ATOM   16738 N  N     . HIS   B  1  1047 ? -2.953  60.246  81.164  1.00 16.52 ? 1045 HIS   B N     1 
ATOM   16739 C  CA    A HIS   B  1  1047 ? -2.168  61.258  81.832  0.53 18.06 ? 1045 HIS   B CA    1 
ATOM   16740 C  CA    B HIS   B  1  1047 ? -2.095  61.208  81.850  0.47 18.08 ? 1045 HIS   B CA    1 
ATOM   16741 C  C     . HIS   B  1  1047 ? -1.350  62.043  80.824  1.00 16.07 ? 1045 HIS   B C     1 
ATOM   16742 O  O     . HIS   B  1  1047 ? -0.871  61.507  79.823  1.00 17.77 ? 1045 HIS   B O     1 
ATOM   16743 C  CB    A HIS   B  1  1047 ? -1.292  60.595  82.883  0.53 17.87 ? 1045 HIS   B CB    1 
ATOM   16744 C  CB    B HIS   B  1  1047 ? -1.060  60.449  82.690  0.47 17.39 ? 1045 HIS   B CB    1 
ATOM   16745 C  CG    A HIS   B  1  1047 ? -2.074  59.714  83.798  0.53 16.05 ? 1045 HIS   B CG    1 
ATOM   16746 C  CG    B HIS   B  1  1047 ? 0.116   61.280  83.124  0.47 17.88 ? 1045 HIS   B CG    1 
ATOM   16747 N  ND1   A HIS   B  1  1047 ? -2.896  60.217  84.781  0.53 19.73 ? 1045 HIS   B ND1   1 
ATOM   16748 N  ND1   B HIS   B  1  1047 ? 0.031   62.233  84.116  0.47 20.24 ? 1045 HIS   B ND1   1 
ATOM   16749 C  CD2   A HIS   B  1  1047 ? -2.206  58.367  83.846  0.53 19.81 ? 1045 HIS   B CD2   1 
ATOM   16750 C  CD2   B HIS   B  1  1047 ? 1.409   61.278  82.715  0.47 18.37 ? 1045 HIS   B CD2   1 
ATOM   16751 C  CE1   A HIS   B  1  1047 ? -3.482  59.216  85.414  0.53 23.13 ? 1045 HIS   B CE1   1 
ATOM   16752 C  CE1   B HIS   B  1  1047 ? 1.215   62.795  84.288  0.47 19.84 ? 1045 HIS   B CE1   1 
ATOM   16753 N  NE2   A HIS   B  1  1047 ? -3.083  58.084  84.864  0.53 21.58 ? 1045 HIS   B NE2   1 
ATOM   16754 N  NE2   B HIS   B  1  1047 ? 2.069   62.233  83.451  0.47 20.83 ? 1045 HIS   B NE2   1 
ATOM   16755 N  N     . THR   B  1  1048 ? -1.231  63.335  81.089  1.00 14.87 ? 1046 THR   B N     1 
ATOM   16756 C  CA    . THR   B  1  1048 ? -0.435  64.216  80.253  1.00 17.23 ? 1046 THR   B CA    1 
ATOM   16757 C  C     . THR   B  1  1048 ? 0.685   64.775  81.112  1.00 16.53 ? 1046 THR   B C     1 
ATOM   16758 O  O     . THR   B  1  1048 ? 0.439   65.309  82.198  1.00 17.55 ? 1046 THR   B O     1 
ATOM   16759 C  CB    . THR   B  1  1048 ? -1.276  65.362  79.712  1.00 19.71 ? 1046 THR   B CB    1 
ATOM   16760 O  OG1   . THR   B  1  1048 ? -2.454  64.835  79.089  1.00 18.03 ? 1046 THR   B OG1   1 
ATOM   16761 C  CG2   . THR   B  1  1048 ? -0.477  66.147  78.680  1.00 21.18 ? 1046 THR   B CG2   1 
ATOM   16762 N  N     . ASP   B  1  1049 ? 1.903   64.650  80.628  1.00 16.92 ? 1047 ASP   B N     1 
ATOM   16763 C  CA    . ASP   B  1  1049 ? 3.020   65.156  81.392  1.00 16.87 ? 1047 ASP   B CA    1 
ATOM   16764 C  C     . ASP   B  1  1049 ? 2.848   66.658  81.615  1.00 15.90 ? 1047 ASP   B C     1 
ATOM   16765 O  O     . ASP   B  1  1049 ? 2.576   67.395  80.661  1.00 16.66 ? 1047 ASP   B O     1 
ATOM   16766 C  CB    . ASP   B  1  1049 ? 4.309   64.869  80.640  1.00 15.56 ? 1047 ASP   B CB    1 
ATOM   16767 C  CG    . ASP   B  1  1049 ? 5.520   65.304  81.417  1.00 16.76 ? 1047 ASP   B CG    1 
ATOM   16768 O  OD1   . ASP   B  1  1049 ? 5.844   66.499  81.336  1.00 16.96 ? 1047 ASP   B OD1   1 
ATOM   16769 O  OD2   . ASP   B  1  1049 ? 6.074   64.464  82.148  1.00 17.39 ? 1047 ASP   B OD2   1 
ATOM   16770 N  N     . PRO   B  1  1050 ? 2.966   67.144  82.854  1.00 18.09 ? 1048 PRO   B N     1 
ATOM   16771 C  CA    . PRO   B  1  1050 ? 2.716   68.568  83.093  1.00 19.20 ? 1048 PRO   B CA    1 
ATOM   16772 C  C     . PRO   B  1  1050 ? 3.797   69.460  82.524  1.00 17.90 ? 1048 PRO   B C     1 
ATOM   16773 O  O     . PRO   B  1  1050 ? 3.514   70.611  82.181  1.00 19.53 ? 1048 PRO   B O     1 
ATOM   16774 C  CB    . PRO   B  1  1050 ? 2.647   68.661  84.626  1.00 21.69 ? 1048 PRO   B CB    1 
ATOM   16775 C  CG    . PRO   B  1  1050 ? 3.446   67.520  85.093  1.00 20.90 ? 1048 PRO   B CG    1 
ATOM   16776 C  CD    . PRO   B  1  1050 ? 3.179   66.412  84.108  1.00 19.30 ? 1048 PRO   B CD    1 
ATOM   16777 N  N     . VAL   B  1  1051 ? 5.031   68.965  82.423  1.00 18.29 ? 1049 VAL   B N     1 
ATOM   16778 C  CA    . VAL   B  1  1051 ? 6.094   69.782  81.847  1.00 17.82 ? 1049 VAL   B CA    1 
ATOM   16779 C  C     . VAL   B  1  1051 ? 5.903   69.901  80.347  1.00 16.61 ? 1049 VAL   B C     1 
ATOM   16780 O  O     . VAL   B  1  1051 ? 6.111   70.970  79.761  1.00 18.37 ? 1049 VAL   B O     1 
ATOM   16781 C  CB    . VAL   B  1  1051 ? 7.469   69.217  82.221  1.00 20.11 ? 1049 VAL   B CB    1 
ATOM   16782 C  CG1   . VAL   B  1  1051 ? 8.563   70.064  81.574  1.00 22.13 ? 1049 VAL   B CG1   1 
ATOM   16783 C  CG2   . VAL   B  1  1051 ? 7.622   69.184  83.739  1.00 21.79 ? 1049 VAL   B CG2   1 
ATOM   16784 N  N     . LEU   B  1  1052 ? 5.478   68.814  79.707  1.00 16.54 ? 1050 LEU   B N     1 
ATOM   16785 C  CA    . LEU   B  1  1052 ? 5.037   68.906  78.322  1.00 15.65 ? 1050 LEU   B CA    1 
ATOM   16786 C  C     . LEU   B  1  1052 ? 3.996   70.004  78.161  1.00 18.70 ? 1050 LEU   B C     1 
ATOM   16787 O  O     . LEU   B  1  1052 ? 4.087   70.831  77.250  1.00 17.77 ? 1050 LEU   B O     1 
ATOM   16788 C  CB    . LEU   B  1  1052 ? 4.487   67.556  77.855  1.00 16.50 ? 1050 LEU   B CB    1 
ATOM   16789 C  CG    . LEU   B  1  1052 ? 3.966   67.403  76.414  1.00 15.38 ? 1050 LEU   B CG    1 
ATOM   16790 C  CD1   . LEU   B  1  1052 ? 2.563   67.980  76.192  1.00 17.44 ? 1050 LEU   B CD1   1 
ATOM   16791 C  CD2   . LEU   B  1  1052 ? 4.949   67.976  75.392  1.00 15.91 ? 1050 LEU   B CD2   1 
ATOM   16792 N  N     . LEU   B  1  1053 ? 2.999   70.034  79.048  1.00 18.36 ? 1051 LEU   B N     1 
ATOM   16793 C  CA    . LEU   B  1  1053 ? 1.963   71.055  78.936  1.00 20.06 ? 1051 LEU   B CA    1 
ATOM   16794 C  C     . LEU   B  1  1053 ? 2.549   72.459  79.037  1.00 19.55 ? 1051 LEU   B C     1 
ATOM   16795 O  O     . LEU   B  1  1053 ? 2.189   73.345  78.257  1.00 20.89 ? 1051 LEU   B O     1 
ATOM   16796 C  CB    . LEU   B  1  1053 ? 0.886   70.849  80.003  1.00 22.09 ? 1051 LEU   B CB    1 
ATOM   16797 C  CG    . LEU   B  1  1053 ? -0.051  69.663  79.763  1.00 24.77 ? 1051 LEU   B CG    1 
ATOM   16798 C  CD1   . LEU   B  1  1053 ? -0.900  69.413  81.000  1.00 24.87 ? 1051 LEU   B CD1   1 
ATOM   16799 C  CD2   . LEU   B  1  1053 ? -0.927  69.890  78.541  1.00 26.06 ? 1051 LEU   B CD2   1 
ATOM   16800 N  N     . ASP   B  1  1054 ? 3.454   72.677  79.990  1.00 19.58 ? 1052 ASP   B N     1 
ATOM   16801 C  CA    . ASP   B  1  1054 ? 4.084   73.989  80.113  1.00 21.45 ? 1052 ASP   B CA    1 
ATOM   16802 C  C     . ASP   B  1  1054 ? 4.910   74.321  78.877  1.00 18.31 ? 1052 ASP   B C     1 
ATOM   16803 O  O     . ASP   B  1  1054 ? 4.965   75.479  78.450  1.00 21.56 ? 1052 ASP   B O     1 
ATOM   16804 C  CB    . ASP   B  1  1054 ? 4.965   74.019  81.356  1.00 22.85 ? 1052 ASP   B CB    1 
ATOM   16805 C  CG    . ASP   B  1  1054 ? 4.166   74.016  82.636  1.00 28.58 ? 1052 ASP   B CG    1 
ATOM   16806 O  OD1   . ASP   B  1  1054 ? 2.940   74.224  82.571  1.00 26.46 ? 1052 ASP   B OD1   1 
ATOM   16807 O  OD2   . ASP   B  1  1054 ? 4.768   73.806  83.709  1.00 29.56 ? 1052 ASP   B OD2   1 
ATOM   16808 N  N     . PHE   B  1  1055 ? 5.547   73.312  78.283  1.00 19.28 ? 1053 PHE   B N     1 
ATOM   16809 C  CA    . PHE   B  1  1055 ? 6.325   73.538  77.073  1.00 19.05 ? 1053 PHE   B CA    1 
ATOM   16810 C  C     . PHE   B  1  1055 ? 5.426   73.950  75.916  1.00 18.94 ? 1053 PHE   B C     1 
ATOM   16811 O  O     . PHE   B  1  1055 ? 5.751   74.875  75.163  1.00 20.65 ? 1053 PHE   B O     1 
ATOM   16812 C  CB    . PHE   B  1  1055 ? 7.109   72.270  76.745  1.00 19.92 ? 1053 PHE   B CB    1 
ATOM   16813 C  CG    . PHE   B  1  1055 ? 8.028   72.405  75.566  1.00 18.55 ? 1053 PHE   B CG    1 
ATOM   16814 C  CD1   . PHE   B  1  1055 ? 9.014   73.380  75.549  1.00 20.37 ? 1053 PHE   B CD1   1 
ATOM   16815 C  CD2   . PHE   B  1  1055 ? 7.910   71.542  74.484  1.00 17.57 ? 1053 PHE   B CD2   1 
ATOM   16816 C  CE1   . PHE   B  1  1055 ? 9.868   73.504  74.461  1.00 22.27 ? 1053 PHE   B CE1   1 
ATOM   16817 C  CE2   . PHE   B  1  1055 ? 8.761   71.663  73.392  1.00 20.15 ? 1053 PHE   B CE2   1 
ATOM   16818 C  CZ    . PHE   B  1  1055 ? 9.733   72.648  73.385  1.00 20.44 ? 1053 PHE   B CZ    1 
ATOM   16819 N  N     . ALA   B  1  1056 ? 4.266   73.299  75.784  1.00 18.96 ? 1054 ALA   B N     1 
ATOM   16820 C  CA    . ALA   B  1  1056 ? 3.340   73.657  74.717  1.00 20.34 ? 1054 ALA   B CA    1 
ATOM   16821 C  C     . ALA   B  1  1056 ? 2.848   75.091  74.868  1.00 20.01 ? 1054 ALA   B C     1 
ATOM   16822 O  O     . ALA   B  1  1056 ? 2.742   75.823  73.879  1.00 21.63 ? 1054 ALA   B O     1 
ATOM   16823 C  CB    . ALA   B  1  1056 ? 2.164   72.679  74.683  1.00 22.23 ? 1054 ALA   B CB    1 
ATOM   16824 N  N     . LYS   B  1  1057 ? 2.547   75.515  76.097  1.00 21.78 ? 1055 LYS   B N     1 
ATOM   16825 C  CA    . LYS   B  1  1057 ? 2.132   76.900  76.298  1.00 23.18 ? 1055 LYS   B CA    1 
ATOM   16826 C  C     . LYS   B  1  1057 ? 3.252   77.864  75.936  1.00 25.99 ? 1055 LYS   B C     1 
ATOM   16827 O  O     . LYS   B  1  1057 ? 3.006   78.920  75.341  1.00 27.01 ? 1055 LYS   B O     1 
ATOM   16828 C  CB    . LYS   B  1  1057 ? 1.684   77.124  77.739  1.00 25.32 ? 1055 LYS   B CB    1 
ATOM   16829 C  CG    . LYS   B  1  1057 ? 0.333   76.523  78.049  1.00 30.78 ? 1055 LYS   B CG    1 
ATOM   16830 C  CD    . LYS   B  1  1057 ? -0.050  76.771  79.492  1.00 26.11 ? 1055 LYS   B CD    1 
ATOM   16831 C  CE    . LYS   B  1  1057 ? 1.009   76.254  80.441  1.00 27.92 ? 1055 LYS   B CE    1 
ATOM   16832 N  NZ    . LYS   B  1  1057 ? 0.497   76.233  81.840  1.00 31.27 ? 1055 LYS   B NZ    1 
ATOM   16833 N  N     . TRP   B  1  1058 ? 4.492   77.514  76.290  1.00 23.65 ? 1056 TRP   B N     1 
ATOM   16834 C  CA    . TRP   B  1  1058 ? 5.631   78.350  75.927  1.00 25.84 ? 1056 TRP   B CA    1 
ATOM   16835 C  C     . TRP   B  1  1058 ? 5.776   78.453  74.415  1.00 24.25 ? 1056 TRP   B C     1 
ATOM   16836 O  O     . TRP   B  1  1058 ? 5.971   79.550  73.879  1.00 27.20 ? 1056 TRP   B O     1 
ATOM   16837 C  CB    . TRP   B  1  1058 ? 6.893   77.792  76.579  1.00 23.81 ? 1056 TRP   B CB    1 
ATOM   16838 C  CG    . TRP   B  1  1058 ? 8.159   78.528  76.239  1.00 25.03 ? 1056 TRP   B CG    1 
ATOM   16839 C  CD1   . TRP   B  1  1058 ? 8.601   79.703  76.782  1.00 31.85 ? 1056 TRP   B CD1   1 
ATOM   16840 C  CD2   . TRP   B  1  1058 ? 9.150   78.125  75.291  1.00 24.24 ? 1056 TRP   B CD2   1 
ATOM   16841 N  NE1   . TRP   B  1  1058 ? 9.805   80.057  76.222  1.00 30.85 ? 1056 TRP   B NE1   1 
ATOM   16842 C  CE2   . TRP   B  1  1058 ? 10.164  79.107  75.305  1.00 28.79 ? 1056 TRP   B CE2   1 
ATOM   16843 C  CE3   . TRP   B  1  1058 ? 9.280   77.030  74.433  1.00 25.14 ? 1056 TRP   B CE3   1 
ATOM   16844 C  CZ2   . TRP   B  1  1058 ? 11.294  79.022  74.493  1.00 26.60 ? 1056 TRP   B CZ2   1 
ATOM   16845 C  CZ3   . TRP   B  1  1058 ? 10.402  76.953  73.619  1.00 27.16 ? 1056 TRP   B CZ3   1 
ATOM   16846 C  CH2   . TRP   B  1  1058 ? 11.393  77.942  73.661  1.00 26.58 ? 1056 TRP   B CH2   1 
ATOM   16847 N  N     . LEU   B  1  1059 ? 5.662   77.326  73.707  1.00 21.85 ? 1057 LEU   B N     1 
ATOM   16848 C  CA    . LEU   B  1  1059 ? 5.681   77.358  72.248  1.00 24.10 ? 1057 LEU   B CA    1 
ATOM   16849 C  C     . LEU   B  1  1059 ? 4.551   78.221  71.700  1.00 27.50 ? 1057 LEU   B C     1 
ATOM   16850 O  O     . LEU   B  1  1059 ? 4.760   79.015  70.773  1.00 27.06 ? 1057 LEU   B O     1 
ATOM   16851 C  CB    . LEU   B  1  1059 ? 5.589   75.940  71.687  1.00 22.36 ? 1057 LEU   B CB    1 
ATOM   16852 C  CG    . LEU   B  1  1059 ? 6.794   75.049  71.982  1.00 20.20 ? 1057 LEU   B CG    1 
ATOM   16853 C  CD1   . LEU   B  1  1059 ? 6.517   73.625  71.542  1.00 22.46 ? 1057 LEU   B CD1   1 
ATOM   16854 C  CD2   . LEU   B  1  1059 ? 8.045   75.594  71.289  1.00 26.47 ? 1057 LEU   B CD2   1 
ATOM   16855 N  N     . ASP   B  1  1060 ? 3.340   78.062  72.253  1.00 24.98 ? 1058 ASP   B N     1 
ATOM   16856 C  CA    . ASP   B  1  1060 ? 2.212   78.918  71.883  1.00 28.03 ? 1058 ASP   B CA    1 
ATOM   16857 C  C     . ASP   B  1  1060 ? 2.603   80.384  71.986  1.00 30.72 ? 1058 ASP   B C     1 
ATOM   16858 O  O     . ASP   B  1  1060 ? 2.365   81.175  71.066  1.00 32.96 ? 1058 ASP   B O     1 
ATOM   16859 C  CB    . ASP   B  1  1060 ? 1.037   78.689  72.846  1.00 29.58 ? 1058 ASP   B CB    1 
ATOM   16860 C  CG    . ASP   B  1  1060 ? 0.238   77.427  72.560  1.00 34.17 ? 1058 ASP   B CG    1 
ATOM   16861 O  OD1   . ASP   B  1  1060 ? 0.173   76.986  71.396  1.00 31.89 ? 1058 ASP   B OD1   1 
ATOM   16862 O  OD2   . ASP   B  1  1060 ? -0.369  76.899  73.527  1.00 32.96 ? 1058 ASP   B OD2   1 
ATOM   16863 N  N     . GLY   B  1  1061 ? 3.184   80.763  73.126  1.00 29.79 ? 1059 GLY   B N     1 
ATOM   16864 C  CA    . GLY   B  1  1061 ? 3.477   82.163  73.376  1.00 32.32 ? 1059 GLY   B CA    1 
ATOM   16865 C  C     . GLY   B  1  1061 ? 4.463   82.750  72.387  1.00 34.02 ? 1059 GLY   B C     1 
ATOM   16866 O  O     . GLY   B  1  1061 ? 4.361   83.923  72.023  1.00 33.69 ? 1059 GLY   B O     1 
ATOM   16867 N  N     . LYS   B  1  1062 ? 5.431   81.954  71.938  1.00 31.08 ? 1060 LYS   B N     1 
ATOM   16868 C  CA    . LYS   B  1  1062 ? 6.407   82.444  70.974  1.00 34.85 ? 1060 LYS   B CA    1 
ATOM   16869 C  C     . LYS   B  1  1062 ? 5.979   82.230  69.525  1.00 38.10 ? 1060 LYS   B C     1 
ATOM   16870 O  O     . LYS   B  1  1062 ? 6.785   82.446  68.615  1.00 41.31 ? 1060 LYS   B O     1 
ATOM   16871 C  CB    . LYS   B  1  1062 ? 7.800   81.866  71.253  1.00 37.29 ? 1060 LYS   B CB    1 
ATOM   16872 C  CG    . LYS   B  1  1062 ? 7.966   80.398  70.948  1.00 37.45 ? 1060 LYS   B CG    1 
ATOM   16873 C  CD    . LYS   B  1  1062 ? 9.360   79.925  71.364  1.00 32.90 ? 1060 LYS   B CD    1 
ATOM   16874 C  CE    . LYS   B  1  1062 ? 10.454  80.758  70.701  1.00 33.49 ? 1060 LYS   B CE    1 
ATOM   16875 N  NZ    . LYS   B  1  1062 ? 11.760  80.604  71.392  1.00 39.15 ? 1060 LYS   B NZ    1 
ATOM   16876 N  N     . GLY   B  1  1063 ? 4.730   81.831  69.289  1.00 33.69 ? 1061 GLY   B N     1 
ATOM   16877 C  CA    . GLY   B  1  1063 ? 4.218   81.706  67.941  1.00 35.60 ? 1061 GLY   B CA    1 
ATOM   16878 C  C     . GLY   B  1  1063 ? 4.627   80.455  67.199  1.00 36.13 ? 1061 GLY   B C     1 
ATOM   16879 O  O     . GLY   B  1  1063 ? 4.312   80.332  66.008  1.00 34.25 ? 1061 GLY   B O     1 
ATOM   16880 N  N     . ALA   B  1  1064 ? 5.313   79.520  67.857  1.00 31.48 ? 1062 ALA   B N     1 
ATOM   16881 C  CA    . ALA   B  1  1064 ? 5.731   78.271  67.222  1.00 30.81 ? 1062 ALA   B CA    1 
ATOM   16882 C  C     . ALA   B  1  1064 ? 4.528   77.327  67.145  1.00 29.25 ? 1062 ALA   B C     1 
ATOM   16883 O  O     . ALA   B  1  1064 ? 4.420   76.329  67.863  1.00 25.09 ? 1062 ALA   B O     1 
ATOM   16884 C  CB    . ALA   B  1  1064 ? 6.904   77.657  67.976  1.00 31.06 ? 1062 ALA   B CB    1 
ATOM   16885 N  N     . ARG   B  1  1065 ? 3.613   77.661  66.230  1.00 30.73 ? 1063 ARG   B N     1 
ATOM   16886 C  CA    . ARG   B  1  1065 ? 2.300   77.017  66.210  1.00 29.27 ? 1063 ARG   B CA    1 
ATOM   16887 C  C     . ARG   B  1  1065 ? 2.401   75.545  65.829  1.00 28.31 ? 1063 ARG   B C     1 
ATOM   16888 O  O     . ARG   B  1  1065 ? 1.774   74.685  66.463  1.00 27.20 ? 1063 ARG   B O     1 
ATOM   16889 C  CB    . ARG   B  1  1065 ? 1.360   77.768  65.263  1.00 34.35 ? 1063 ARG   B CB    1 
ATOM   16890 N  N     . ALA   B  1  1066 ? 3.177   75.230  64.790  1.00 24.85 ? 1064 ALA   B N     1 
ATOM   16891 C  CA    . ALA   B  1  1066 ? 3.333   73.834  64.405  1.00 24.52 ? 1064 ALA   B CA    1 
ATOM   16892 C  C     . ALA   B  1  1066 ? 3.950   73.028  65.538  1.00 24.17 ? 1064 ALA   B C     1 
ATOM   16893 O  O     . ALA   B  1  1066 ? 3.519   71.907  65.822  1.00 24.47 ? 1064 ALA   B O     1 
ATOM   16894 C  CB    . ALA   B  1  1066 ? 4.196   73.723  63.149  1.00 29.40 ? 1064 ALA   B CB    1 
ATOM   16895 N  N     . GLU   B  1  1067 ? 4.961   73.587  66.201  1.00 22.34 ? 1065 GLU   B N     1 
ATOM   16896 C  CA    . GLU   B  1  1067 ? 5.631   72.843  67.261  1.00 23.68 ? 1065 GLU   B CA    1 
ATOM   16897 C  C     . GLU   B  1  1067 ? 4.728   72.674  68.477  1.00 21.05 ? 1065 GLU   B C     1 
ATOM   16898 O  O     . GLU   B  1  1067 ? 4.748   71.624  69.130  1.00 20.58 ? 1065 GLU   B O     1 
ATOM   16899 C  CB    . GLU   B  1  1067 ? 6.934   73.545  67.640  1.00 23.00 ? 1065 GLU   B CB    1 
ATOM   16900 C  CG    . GLU   B  1  1067 ? 7.997   73.509  66.544  1.00 24.85 ? 1065 GLU   B CG    1 
ATOM   16901 C  CD    . GLU   B  1  1067 ? 7.768   74.521  65.436  1.00 27.92 ? 1065 GLU   B CD    1 
ATOM   16902 O  OE1   . GLU   B  1  1067 ? 6.877   75.393  65.563  1.00 27.96 ? 1065 GLU   B OE1   1 
ATOM   16903 O  OE2   . GLU   B  1  1067 ? 8.497   74.443  64.425  1.00 27.76 ? 1065 GLU   B OE2   1 
ATOM   16904 N  N     . ALA   B  1  1068 ? 3.955   73.705  68.812  1.00 21.10 ? 1066 ALA   B N     1 
ATOM   16905 C  CA    . ALA   B  1  1068 ? 3.018   73.590  69.925  1.00 24.02 ? 1066 ALA   B CA    1 
ATOM   16906 C  C     . ALA   B  1  1068 ? 1.993   72.499  69.659  1.00 22.86 ? 1066 ALA   B C     1 
ATOM   16907 O  O     . ALA   B  1  1068 ? 1.650   71.730  70.563  1.00 19.72 ? 1066 ALA   B O     1 
ATOM   16908 C  CB    . ALA   B  1  1068 ? 2.317   74.924  70.155  1.00 21.72 ? 1066 ALA   B CB    1 
ATOM   16909 N  N     . GLU   B  1  1069 ? 1.503   72.414  68.419  1.00 20.39 ? 1067 GLU   B N     1 
ATOM   16910 C  CA    . GLU   B  1  1069 ? 0.583   71.344  68.050  1.00 23.27 ? 1067 GLU   B CA    1 
ATOM   16911 C  C     . GLU   B  1  1069 ? 1.251   69.978  68.154  1.00 23.66 ? 1067 GLU   B C     1 
ATOM   16912 O  O     . GLU   B  1  1069 ? 0.654   69.017  68.657  1.00 21.47 ? 1067 GLU   B O     1 
ATOM   16913 C  CB    . GLU   B  1  1069 ? 0.068   71.581  66.629  1.00 24.34 ? 1067 GLU   B CB    1 
ATOM   16914 C  CG    . GLU   B  1  1069 ? -0.790  70.462  66.060  1.00 30.24 ? 1067 GLU   B CG    1 
ATOM   16915 C  CD    . GLU   B  1  1069 ? -2.171  70.387  66.700  1.00 36.91 ? 1067 GLU   B CD    1 
ATOM   16916 O  OE1   . GLU   B  1  1069 ? -2.519  71.283  67.499  1.00 36.17 ? 1067 GLU   B OE1   1 
ATOM   16917 O  OE2   . GLU   B  1  1069 ? -2.911  69.426  66.403  1.00 41.09 ? 1067 GLU   B OE2   1 
ATOM   16918 N  N     . ALA   B  1  1070 ? 2.493   69.866  67.676  1.00 22.65 ? 1068 ALA   B N     1 
ATOM   16919 C  CA    . ALA   B  1  1070 ? 3.225   68.617  67.843  1.00 22.43 ? 1068 ALA   B CA    1 
ATOM   16920 C  C     . ALA   B  1  1070 ? 3.402   68.286  69.319  1.00 17.16 ? 1068 ALA   B C     1 
ATOM   16921 O  O     . ALA   B  1  1070 ? 3.292   67.121  69.716  1.00 20.37 ? 1068 ALA   B O     1 
ATOM   16922 C  CB    . ALA   B  1  1070 ? 4.584   68.698  67.140  1.00 23.85 ? 1068 ALA   B CB    1 
ATOM   16923 N  N     . ALA   B  1  1071 ? 3.650   69.302  70.148  1.00 18.32 ? 1069 ALA   B N     1 
ATOM   16924 C  CA    . ALA   B  1  1071 ? 3.811   69.056  71.576  1.00 17.71 ? 1069 ALA   B CA    1 
ATOM   16925 C  C     . ALA   B  1  1071 ? 2.523   68.512  72.179  1.00 18.44 ? 1069 ALA   B C     1 
ATOM   16926 O  O     . ALA   B  1  1071 ? 2.541   67.507  72.905  1.00 17.05 ? 1069 ALA   B O     1 
ATOM   16927 C  CB    . ALA   B  1  1071 ? 4.262   70.324  72.295  1.00 18.44 ? 1069 ALA   B CB    1 
ATOM   16928 N  N     . ARG   B  1  1072 ? 1.392   69.155  71.881  1.00 17.73 ? 1070 ARG   B N     1 
ATOM   16929 C  CA    A ARG   B  1  1072 ? 0.114   68.680  72.408  0.54 18.40 ? 1070 ARG   B CA    1 
ATOM   16930 C  CA    B ARG   B  1  1072 ? 0.124   68.675  72.421  0.46 18.41 ? 1070 ARG   B CA    1 
ATOM   16931 C  C     . ARG   B  1  1072 ? -0.187  67.272  71.923  1.00 20.06 ? 1070 ARG   B C     1 
ATOM   16932 O  O     . ARG   B  1  1072 ? -0.631  66.417  72.701  1.00 18.21 ? 1070 ARG   B O     1 
ATOM   16933 C  CB    A ARG   B  1  1072 ? -1.012  69.628  71.999  0.54 19.07 ? 1070 ARG   B CB    1 
ATOM   16934 C  CB    B ARG   B  1  1072 ? -1.005  69.651  72.089  0.46 19.10 ? 1070 ARG   B CB    1 
ATOM   16935 C  CG    A ARG   B  1  1072 ? -1.009  70.940  72.746  0.54 21.60 ? 1070 ARG   B CG    1 
ATOM   16936 C  CG    B ARG   B  1  1072 ? -0.750  71.030  72.651  0.46 21.46 ? 1070 ARG   B CG    1 
ATOM   16937 C  CD    A ARG   B  1  1072 ? -2.228  71.765  72.373  0.54 21.89 ? 1070 ARG   B CD    1 
ATOM   16938 C  CD    B ARG   B  1  1072 ? -2.008  71.872  72.748  0.46 21.85 ? 1070 ARG   B CD    1 
ATOM   16939 N  NE    A ARG   B  1  1072 ? -2.183  72.195  70.981  0.54 22.70 ? 1070 ARG   B NE    1 
ATOM   16940 N  NE    B ARG   B  1  1072 ? -1.678  73.212  73.212  0.46 22.24 ? 1070 ARG   B NE    1 
ATOM   16941 C  CZ    A ARG   B  1  1072 ? -1.710  73.368  70.584  0.54 26.37 ? 1070 ARG   B CZ    1 
ATOM   16942 C  CZ    B ARG   B  1  1072 ? -1.473  73.535  74.481  0.46 22.39 ? 1070 ARG   B CZ    1 
ATOM   16943 N  NH1   A ARG   B  1  1072 ? -1.250  74.254  71.452  0.54 24.52 ? 1070 ARG   B NH1   1 
ATOM   16944 N  NH1   B ARG   B  1  1072 ? -1.626  72.650  75.455  0.46 26.70 ? 1070 ARG   B NH1   1 
ATOM   16945 N  NH2   A ARG   B  1  1072 ? -1.698  73.658  69.286  0.54 22.18 ? 1070 ARG   B NH2   1 
ATOM   16946 N  NH2   B ARG   B  1  1072 ? -1.096  74.772  74.780  0.46 23.19 ? 1070 ARG   B NH2   1 
ATOM   16947 N  N     . ASN   B  1  1073 ? 0.068   67.007  70.638  1.00 18.85 ? 1071 ASN   B N     1 
ATOM   16948 C  CA    . ASN   B  1  1073 ? -0.169  65.675  70.096  1.00 19.78 ? 1071 ASN   B CA    1 
ATOM   16949 C  C     . ASN   B  1  1073 ? 0.698   64.637  70.786  1.00 19.52 ? 1071 ASN   B C     1 
ATOM   16950 O  O     . ASN   B  1  1073 ? 0.236   63.527  71.078  1.00 20.25 ? 1071 ASN   B O     1 
ATOM   16951 C  CB    . ASN   B  1  1073 ? 0.071   65.672  68.591  1.00 21.68 ? 1071 ASN   B CB    1 
ATOM   16952 C  CG    . ASN   B  1  1073 ? -1.033  66.368  67.840  1.00 27.61 ? 1071 ASN   B CG    1 
ATOM   16953 O  OD1   . ASN   B  1  1073 ? -2.128  66.567  68.370  1.00 28.21 ? 1071 ASN   B OD1   1 
ATOM   16954 N  ND2   . ASN   B  1  1073 ? -0.758  66.749  66.601  1.00 30.29 ? 1071 ASN   B ND2   1 
ATOM   16955 N  N     . ALA   B  1  1074 ? 1.967   64.974  71.038  1.00 17.41 ? 1072 ALA   B N     1 
ATOM   16956 C  CA    . ALA   B  1  1074 ? 2.840   64.053  71.754  1.00 18.69 ? 1072 ALA   B CA    1 
ATOM   16957 C  C     . ALA   B  1  1074 ? 2.342   63.829  73.172  1.00 15.75 ? 1072 ALA   B C     1 
ATOM   16958 O  O     . ALA   B  1  1074 ? 2.363   62.700  73.673  1.00 16.66 ? 1072 ALA   B O     1 
ATOM   16959 C  CB    . ALA   B  1  1074 ? 4.270   64.593  71.779  1.00 19.05 ? 1072 ALA   B CB    1 
ATOM   16960 N  N     . GLY   B  1  1075 ? 1.917   64.895  73.843  1.00 16.17 ? 1073 GLY   B N     1 
ATOM   16961 C  CA    . GLY   B  1  1075 ? 1.404   64.738  75.194  1.00 17.98 ? 1073 GLY   B CA    1 
ATOM   16962 C  C     . GLY   B  1  1075 ? 0.241   63.769  75.251  1.00 17.87 ? 1073 GLY   B C     1 
ATOM   16963 O  O     . GLY   B  1  1075 ? 0.115   62.987  76.198  1.00 18.23 ? 1073 GLY   B O     1 
ATOM   16964 N  N     . SER   B  1  1076 ? -0.605  63.789  74.223  1.00 18.47 ? 1074 SER   B N     1 
ATOM   16965 C  CA    . SER   B  1  1076 ? -1.770  62.916  74.211  1.00 17.80 ? 1074 SER   B CA    1 
ATOM   16966 C  C     . SER   B  1  1076 ? -1.410  61.499  73.790  1.00 17.97 ? 1074 SER   B C     1 
ATOM   16967 O  O     . SER   B  1  1076 ? -1.882  60.538  74.403  1.00 19.57 ? 1074 SER   B O     1 
ATOM   16968 C  CB    . SER   B  1  1076 ? -2.837  63.492  73.286  1.00 19.93 ? 1074 SER   B CB    1 
ATOM   16969 O  OG    . SER   B  1  1076 ? -3.422  64.648  73.862  1.00 22.39 ? 1074 SER   B OG    1 
ATOM   16970 N  N     . SER   B  1  1077 ? -0.548  61.335  72.779  1.00 17.70 ? 1075 SER   B N     1 
ATOM   16971 C  CA    A SER   B  1  1077 ? -0.221  60.007  72.264  0.31 20.25 ? 1075 SER   B CA    1 
ATOM   16972 C  CA    B SER   B  1  1077 ? -0.284  59.981  72.313  0.69 20.25 ? 1075 SER   B CA    1 
ATOM   16973 C  C     . SER   B  1  1077 ? 0.709   59.240  73.196  1.00 17.92 ? 1075 SER   B C     1 
ATOM   16974 O  O     . SER   B  1  1077 ? 0.713   58.002  73.180  1.00 21.02 ? 1075 SER   B O     1 
ATOM   16975 C  CB    A SER   B  1  1077 ? 0.426   60.133  70.887  0.31 22.61 ? 1075 SER   B CB    1 
ATOM   16976 C  CB    B SER   B  1  1077 ? 0.165   59.976  70.855  0.69 23.24 ? 1075 SER   B CB    1 
ATOM   16977 O  OG    A SER   B  1  1077 ? -0.395  60.873  70.003  0.31 23.08 ? 1075 SER   B OG    1 
ATOM   16978 O  OG    B SER   B  1  1077 ? 1.480   60.461  70.737  0.69 21.70 ? 1075 SER   B OG    1 
ATOM   16979 N  N     . SER   B  1  1078 ? 1.517   59.955  73.974  1.00 15.53 ? 1076 SER   B N     1 
ATOM   16980 C  CA    . SER   B  1  1078 ? 2.396   59.316  74.941  1.00 16.21 ? 1076 SER   B CA    1 
ATOM   16981 C  C     . SER   B  1  1078 ? 1.608   58.353  75.809  1.00 15.12 ? 1076 SER   B C     1 
ATOM   16982 O  O     . SER   B  1  1078 ? 0.493   58.656  76.244  1.00 15.81 ? 1076 SER   B O     1 
ATOM   16983 C  CB    . SER   B  1  1078 ? 2.977   60.383  75.853  1.00 16.03 ? 1076 SER   B CB    1 
ATOM   16984 O  OG    . SER   B  1  1078 ? 3.698   59.772  76.914  1.00 14.93 ? 1076 SER   B OG    1 
ATOM   16985 N  N     . ALA   B  1  1079 ? 2.180   57.184  76.055  1.00 13.83 ? 1077 ALA   B N     1 
ATOM   16986 C  CA    . ALA   B  1  1079 ? 1.559   56.223  76.947  1.00 14.76 ? 1077 ALA   B CA    1 
ATOM   16987 C  C     . ALA   B  1  1079 ? 2.192   56.251  78.318  1.00 14.14 ? 1077 ALA   B C     1 
ATOM   16988 O  O     . ALA   B  1  1079 ? 1.958   55.348  79.115  1.00 13.72 ? 1077 ALA   B O     1 
ATOM   16989 C  CB    . ALA   B  1  1079 ? 1.576   54.815  76.354  1.00 15.89 ? 1077 ALA   B CB    1 
ATOM   16990 N  N     . LEU   B  1  1080 ? 3.000   57.267  78.598  1.00 13.21 ? 1078 LEU   B N     1 
ATOM   16991 C  CA    . LEU   B  1  1080 ? 3.543   57.440  79.938  1.00 13.14 ? 1078 LEU   B CA    1 
ATOM   16992 C  C     . LEU   B  1  1080 ? 2.421   57.396  80.961  1.00 13.57 ? 1078 LEU   B C     1 
ATOM   16993 O  O     . LEU   B  1  1080 ? 1.424   58.111  80.838  1.00 14.87 ? 1078 LEU   B O     1 
ATOM   16994 C  CB    . LEU   B  1  1080 ? 4.214   58.806  80.015  1.00 13.43 ? 1078 LEU   B CB    1 
ATOM   16995 C  CG    . LEU   B  1  1080 ? 4.675   59.220  81.407  1.00 13.26 ? 1078 LEU   B CG    1 
ATOM   16996 C  CD1   . LEU   B  1  1080 ? 5.851   58.379  81.866  1.00 14.63 ? 1078 LEU   B CD1   1 
ATOM   16997 C  CD2   . LEU   B  1  1080 ? 5.022   60.698  81.406  1.00 14.69 ? 1078 LEU   B CD2   1 
ATOM   16998 N  N     . GLY   B  1  1081 ? 2.592   56.560  81.979  1.00 12.56 ? 1079 GLY   B N     1 
ATOM   16999 C  CA    . GLY   B  1  1081 ? 1.585   56.432  83.009  1.00 14.41 ? 1079 GLY   B CA    1 
ATOM   17000 C  C     . GLY   B  1  1081 ? 0.644   55.266  82.812  1.00 15.14 ? 1079 GLY   B C     1 
ATOM   17001 O  O     . GLY   B  1  1081 ? -0.210  55.026  83.680  1.00 16.58 ? 1079 GLY   B O     1 
ATOM   17002 N  N     . LEU   B  1  1082 ? 0.755   54.558  81.694  1.00 14.21 ? 1080 LEU   B N     1 
ATOM   17003 C  CA    A LEU   B  1  1082 ? 0.012   53.319  81.523  0.42 14.40 ? 1080 LEU   B CA    1 
ATOM   17004 C  CA    B LEU   B  1  1082 ? 0.008   53.321  81.526  0.58 14.38 ? 1080 LEU   B CA    1 
ATOM   17005 C  C     . LEU   B  1  1082 ? 0.280   52.414  82.712  1.00 14.68 ? 1080 LEU   B C     1 
ATOM   17006 O  O     . LEU   B  1  1082 ? 1.413   52.288  83.163  1.00 15.58 ? 1080 LEU   B O     1 
ATOM   17007 C  CB    A LEU   B  1  1082 ? 0.470   52.637  80.234  0.42 14.55 ? 1080 LEU   B CB    1 
ATOM   17008 C  CB    B LEU   B  1  1082 ? 0.452   52.640  80.235  0.58 14.54 ? 1080 LEU   B CB    1 
ATOM   17009 C  CG    A LEU   B  1  1082 ? -0.114  51.261  79.902  0.42 14.42 ? 1080 LEU   B CG    1 
ATOM   17010 C  CG    B LEU   B  1  1082 ? -0.139  51.275  79.869  0.58 14.39 ? 1080 LEU   B CG    1 
ATOM   17011 C  CD1   A LEU   B  1  1082 ? -1.611  51.339  79.841  0.42 19.10 ? 1080 LEU   B CD1   1 
ATOM   17012 C  CD1   B LEU   B  1  1082 ? -0.024  51.087  78.376  0.58 15.89 ? 1080 LEU   B CD1   1 
ATOM   17013 C  CD2   A LEU   B  1  1082 ? 0.431   50.742  78.583  0.42 16.63 ? 1080 LEU   B CD2   1 
ATOM   17014 C  CD2   B LEU   B  1  1082 ? 0.571   50.133  80.590  0.58 14.64 ? 1080 LEU   B CD2   1 
ATOM   17015 N  N     . ASP   B  1  1083 ? -0.774  51.786  83.225  1.00 16.14 ? 1081 ASP   B N     1 
ATOM   17016 C  CA    . ASP   B  1  1083 ? -0.659  51.002  84.451  1.00 19.60 ? 1081 ASP   B CA    1 
ATOM   17017 C  C     . ASP   B  1  1083 ? -1.718  49.910  84.359  1.00 17.28 ? 1081 ASP   B C     1 
ATOM   17018 O  O     . ASP   B  1  1083 ? -2.889  50.151  84.666  1.00 21.53 ? 1081 ASP   B O     1 
ATOM   17019 C  CB    . ASP   B  1  1083 ? -0.879  51.907  85.654  1.00 21.00 ? 1081 ASP   B CB    1 
ATOM   17020 C  CG    . ASP   B  1  1083 ? -0.673  51.194  86.973  1.00 32.44 ? 1081 ASP   B CG    1 
ATOM   17021 O  OD1   . ASP   B  1  1083 ? -0.158  50.059  86.975  1.00 34.41 ? 1081 ASP   B OD1   1 
ATOM   17022 O  OD2   . ASP   B  1  1083 ? -1.034  51.779  88.018  1.00 36.41 ? 1081 ASP   B OD2   1 
ATOM   17023 N  N     . LEU   B  1  1084 ? -1.307  48.729  83.913  1.00 16.64 ? 1082 LEU   B N     1 
ATOM   17024 C  CA    . LEU   B  1  1084 ? -2.220  47.653  83.568  1.00 18.17 ? 1082 LEU   B CA    1 
ATOM   17025 C  C     . LEU   B  1  1084 ? -1.944  46.447  84.445  1.00 17.71 ? 1082 LEU   B C     1 
ATOM   17026 O  O     . LEU   B  1  1084 ? -0.807  46.205  84.859  1.00 16.79 ? 1082 LEU   B O     1 
ATOM   17027 C  CB    . LEU   B  1  1084 ? -1.999  47.194  82.124  1.00 20.19 ? 1082 LEU   B CB    1 
ATOM   17028 C  CG    . LEU   B  1  1084 ? -2.343  48.169  81.005  1.00 24.34 ? 1082 LEU   B CG    1 
ATOM   17029 C  CD1   . LEU   B  1  1084 ? -1.966  47.568  79.669  1.00 25.41 ? 1082 LEU   B CD1   1 
ATOM   17030 C  CD2   . LEU   B  1  1084 ? -3.820  48.553  81.058  1.00 26.31 ? 1082 LEU   B CD2   1 
ATOM   17031 N  N     . GLU   B  1  1085 ? -2.985  45.681  84.709  1.00 16.22 ? 1083 GLU   B N     1 
ATOM   17032 C  CA    . GLU   B  1  1085 ? -2.828  44.330  85.207  1.00 15.03 ? 1083 GLU   B CA    1 
ATOM   17033 C  C     . GLU   B  1  1085 ? -3.005  43.371  84.043  1.00 16.09 ? 1083 GLU   B C     1 
ATOM   17034 O  O     . GLU   B  1  1085 ? -3.989  43.462  83.301  1.00 18.43 ? 1083 GLU   B O     1 
ATOM   17035 C  CB    . GLU   B  1  1085 ? -3.826  44.009  86.318  1.00 17.53 ? 1083 GLU   B CB    1 
ATOM   17036 C  CG    . GLU   B  1  1085 ? -3.560  42.606  86.836  1.00 19.49 ? 1083 GLU   B CG    1 
ATOM   17037 C  CD    . GLU   B  1  1085 ? -4.352  42.224  88.053  1.00 24.54 ? 1083 GLU   B CD    1 
ATOM   17038 O  OE1   . GLU   B  1  1085 ? -4.990  43.105  88.669  1.00 26.93 ? 1083 GLU   B OE1   1 
ATOM   17039 O  OE2   . GLU   B  1  1085 ? -4.328  41.018  88.390  1.00 24.66 ? 1083 GLU   B OE2   1 
ATOM   17040 N  N     . LEU   B  1  1086 ? -2.058  42.487  83.872  1.00 16.15 ? 1084 LEU   B N     1 
ATOM   17041 C  CA    . LEU   B  1  1086 ? -2.076  41.534  82.780  1.00 15.58 ? 1084 LEU   B CA    1 
ATOM   17042 C  C     . LEU   B  1  1086 ? -2.727  40.228  83.227  1.00 18.21 ? 1084 LEU   B C     1 
ATOM   17043 O  O     . LEU   B  1  1086 ? -2.552  39.810  84.374  1.00 18.99 ? 1084 LEU   B O     1 
ATOM   17044 C  CB    . LEU   B  1  1086 ? -0.658  41.247  82.325  1.00 17.60 ? 1084 LEU   B CB    1 
ATOM   17045 C  CG    . LEU   B  1  1086 ? 0.090   42.487  81.861  1.00 16.93 ? 1084 LEU   B CG    1 
ATOM   17046 C  CD1   . LEU   B  1  1086 ? 1.470   42.099  81.388  1.00 18.92 ? 1084 LEU   B CD1   1 
ATOM   17047 C  CD2   . LEU   B  1  1086 ? -0.675  43.171  80.739  1.00 21.44 ? 1084 LEU   B CD2   1 
ATOM   17048 N  N     . PRO   B  1  1087 ? -3.466  39.588  82.328  1.00 16.52 ? 1085 PRO   B N     1 
ATOM   17049 C  CA    . PRO   B  1  1087 ? -4.091  38.305  82.661  1.00 17.83 ? 1085 PRO   B CA    1 
ATOM   17050 C  C     . PRO   B  1  1087 ? -3.031  37.268  82.967  1.00 17.56 ? 1085 PRO   B C     1 
ATOM   17051 O  O     . PRO   B  1  1087 ? -2.000  37.188  82.299  1.00 18.92 ? 1085 PRO   B O     1 
ATOM   17052 C  CB    . PRO   B  1  1087 ? -4.848  37.941  81.378  1.00 19.98 ? 1085 PRO   B CB    1 
ATOM   17053 C  CG    . PRO   B  1  1087 ? -5.120  39.236  80.726  1.00 22.59 ? 1085 PRO   B CG    1 
ATOM   17054 C  CD    . PRO   B  1  1087 ? -3.948  40.124  81.040  1.00 18.02 ? 1085 PRO   B CD    1 
ATOM   17055 N  N     . GLY   B  1  1088 ? -3.276  36.484  84.001  1.00 17.61 ? 1086 GLY   B N     1 
ATOM   17056 C  CA    . GLY   B  1  1088 ? -2.345  35.460  84.384  1.00 18.78 ? 1086 GLY   B CA    1 
ATOM   17057 C  C     . GLY   B  1  1088 ? -2.975  34.519  85.380  1.00 15.88 ? 1086 GLY   B C     1 
ATOM   17058 O  O     . GLY   B  1  1088 ? -4.198  34.443  85.516  1.00 17.39 ? 1086 GLY   B O     1 
ATOM   17059 N  N     . PRO   B  1  1089 ? -2.143  33.789  86.105  1.00 16.28 ? 1087 PRO   B N     1 
ATOM   17060 C  CA    . PRO   B  1  1089 ? -2.670  32.814  87.059  1.00 17.06 ? 1087 PRO   B CA    1 
ATOM   17061 C  C     . PRO   B  1  1089 ? -3.294  33.489  88.266  1.00 15.81 ? 1087 PRO   B C     1 
ATOM   17062 O  O     . PRO   B  1  1089 ? -2.991  34.634  88.616  1.00 17.17 ? 1087 PRO   B O     1 
ATOM   17063 C  CB    . PRO   B  1  1089 ? -1.424  32.024  87.468  1.00 18.03 ? 1087 PRO   B CB    1 
ATOM   17064 C  CG    . PRO   B  1  1089 ? -0.306  33.028  87.311  1.00 20.19 ? 1087 PRO   B CG    1 
ATOM   17065 C  CD    . PRO   B  1  1089 ? -0.670  33.811  86.085  1.00 17.71 ? 1087 PRO   B CD    1 
ATOM   17066 N  N     . VAL   B  1  1090 ? -4.184  32.742  88.923  1.00 15.35 ? 1088 VAL   B N     1 
ATOM   17067 C  CA    . VAL   B  1  1090 ? -4.707  33.204  90.193  1.00 16.53 ? 1088 VAL   B CA    1 
ATOM   17068 C  C     . VAL   B  1  1090 ? -3.575  33.262  91.207  1.00 16.02 ? 1088 VAL   B C     1 
ATOM   17069 O  O     . VAL   B  1  1090 ? -2.522  32.635  91.046  1.00 15.67 ? 1088 VAL   B O     1 
ATOM   17070 C  CB    . VAL   B  1  1090 ? -5.847  32.319  90.716  1.00 17.19 ? 1088 VAL   B CB    1 
ATOM   17071 C  CG1   . VAL   B  1  1090 ? -6.990  32.284  89.731  1.00 17.07 ? 1088 VAL   B CG1   1 
ATOM   17072 C  CG2   . VAL   B  1  1090 ? -5.344  30.908  91.018  1.00 18.47 ? 1088 VAL   B CG2   1 
ATOM   17073 N  N     . GLY   B  1  1091 ? -3.803  34.029  92.268  1.00 16.66 ? 1089 GLY   B N     1 
ATOM   17074 C  CA    . GLY   B  1  1091 ? -2.815  34.127  93.321  1.00 16.57 ? 1089 GLY   B CA    1 
ATOM   17075 C  C     . GLY   B  1  1091 ? -1.602  34.930  92.951  1.00 15.84 ? 1089 GLY   B C     1 
ATOM   17076 O  O     . GLY   B  1  1091 ? -0.581  34.858  93.639  1.00 15.21 ? 1089 GLY   B O     1 
ATOM   17077 N  N     . GLU   B  1  1092 ? -1.677  35.682  91.862  1.00 15.60 ? 1090 GLU   B N     1 
ATOM   17078 C  CA    . GLU   B  1  1092 ? -0.596  36.549  91.449  1.00 14.58 ? 1090 GLU   B CA    1 
ATOM   17079 C  C     . GLU   B  1  1092 ? -1.230  37.776  90.833  1.00 15.46 ? 1090 GLU   B C     1 
ATOM   17080 O  O     . GLU   B  1  1092 ? -2.287  37.682  90.201  1.00 18.01 ? 1090 GLU   B O     1 
ATOM   17081 C  CB    . GLU   B  1  1092 ? 0.236   35.850  90.376  1.00 19.02 ? 1090 GLU   B CB    1 
ATOM   17082 C  CG    . GLU   B  1  1092 ? 1.710   35.829  90.626  1.00 25.01 ? 1090 GLU   B CG    1 
ATOM   17083 C  CD    . GLU   B  1  1092 ? 2.444   34.949  89.628  1.00 22.63 ? 1090 GLU   B CD    1 
ATOM   17084 O  OE1   . GLU   B  1  1092 ? 2.280   35.169  88.407  1.00 19.24 ? 1090 GLU   B OE1   1 
ATOM   17085 O  OE2   . GLU   B  1  1092 ? 3.163   34.023  90.064  1.00 23.73 ? 1090 GLU   B OE2   1 
ATOM   17086 N  N     . ARG   B  1  1093 ? -0.607  38.926  91.031  1.00 15.26 ? 1091 ARG   B N     1 
ATOM   17087 C  CA    . ARG   B  1  1093 ? -0.972  40.129  90.296  1.00 14.39 ? 1091 ARG   B CA    1 
ATOM   17088 C  C     . ARG   B  1  1093 ? 0.223   40.513  89.458  1.00 14.60 ? 1091 ARG   B C     1 
ATOM   17089 O  O     . ARG   B  1  1093 ? 1.324   40.701  89.984  1.00 15.24 ? 1091 ARG   B O     1 
ATOM   17090 C  CB    . ARG   B  1  1093 ? -1.360  41.280  91.222  1.00 17.58 ? 1091 ARG   B CB    1 
ATOM   17091 C  CG    . ARG   B  1  1093 ? -2.748  41.134  91.809  1.00 25.83 ? 1091 ARG   B CG    1 
ATOM   17092 C  CD    . ARG   B  1  1093 ? -3.297  42.482  92.273  1.00 33.77 ? 1091 ARG   B CD    1 
ATOM   17093 N  NE    . ARG   B  1  1093 ? -2.406  43.117  93.234  1.00 37.29 ? 1091 ARG   B NE    1 
ATOM   17094 C  CZ    . ARG   B  1  1093 ? -2.484  42.955  94.548  1.00 45.53 ? 1091 ARG   B CZ    1 
ATOM   17095 N  NH1   . ARG   B  1  1093 ? -3.430  42.210  95.097  1.00 45.53 ? 1091 ARG   B NH1   1 
ATOM   17096 N  NH2   . ARG   B  1  1093 ? -1.586  43.551  95.331  1.00 42.84 ? 1091 ARG   B NH2   1 
ATOM   17097 N  N     . ASN   B  1  1094 ? 0.017   40.581  88.161  1.00 12.80 ? 1092 ASN   B N     1 
ATOM   17098 C  CA    . ASN   B  1  1094 ? 1.092   40.828  87.223  1.00 13.69 ? 1092 ASN   B CA    1 
ATOM   17099 C  C     . ASN   B  1  1094 ? 0.809   42.164  86.572  1.00 14.78 ? 1092 ASN   B C     1 
ATOM   17100 O  O     . ASN   B  1  1094 ? -0.194  42.320  85.864  1.00 15.59 ? 1092 ASN   B O     1 
ATOM   17101 C  CB    . ASN   B  1  1094 ? 1.175   39.679  86.235  1.00 13.84 ? 1092 ASN   B CB    1 
ATOM   17102 C  CG    . ASN   B  1  1094 ? 1.772   38.461  86.885  1.00 14.29 ? 1092 ASN   B CG    1 
ATOM   17103 O  OD1   . ASN   B  1  1094 ? 2.964   38.462  87.175  1.00 13.79 ? 1092 ASN   B OD1   1 
ATOM   17104 N  ND2   . ASN   B  1  1094 ? 0.960   37.447  87.157  1.00 14.85 ? 1092 ASN   B ND2   1 
ATOM   17105 N  N     . LEU   B  1  1095 ? 1.659   43.130  86.856  1.00 13.33 ? 1093 LEU   B N     1 
ATOM   17106 C  CA    . LEU   B  1  1095 ? 1.416   44.514  86.525  1.00 13.52 ? 1093 LEU   B CA    1 
ATOM   17107 C  C     . LEU   B  1  1095 ? 2.425   44.965  85.490  1.00 12.52 ? 1093 LEU   B C     1 
ATOM   17108 O  O     . LEU   B  1  1095 ? 3.566   44.502  85.456  1.00 13.67 ? 1093 LEU   B O     1 
ATOM   17109 C  CB    . LEU   B  1  1095 ? 1.550   45.396  87.756  1.00 15.08 ? 1093 LEU   B CB    1 
ATOM   17110 C  CG    . LEU   B  1  1095 ? 0.675   44.934  88.928  1.00 18.33 ? 1093 LEU   B CG    1 
ATOM   17111 C  CD1   . LEU   B  1  1095 ? 0.896   45.848  90.137  1.00 22.83 ? 1093 LEU   B CD1   1 
ATOM   17112 C  CD2   . LEU   B  1  1095 ? -0.802  44.876  88.541  1.00 19.24 ? 1093 LEU   B CD2   1 
ATOM   17113 N  N     . TYR   B  1  1096 ? 1.993   45.892  84.652  1.00 12.76 ? 1094 TYR   B N     1 
ATOM   17114 C  CA    . TYR   B  1  1096 ? 2.818   46.373  83.564  1.00 13.46 ? 1094 TYR   B CA    1 
ATOM   17115 C  C     . TYR   B  1  1096 ? 2.597   47.866  83.484  1.00 12.61 ? 1094 TYR   B C     1 
ATOM   17116 O  O     . TYR   B  1  1096 ? 1.457   48.324  83.367  1.00 13.43 ? 1094 TYR   B O     1 
ATOM   17117 C  CB    . TYR   B  1  1096 ? 2.421   45.684  82.259  1.00 14.47 ? 1094 TYR   B CB    1 
ATOM   17118 C  CG    . TYR   B  1  1096 ? 3.079   46.214  81.011  1.00 13.52 ? 1094 TYR   B CG    1 
ATOM   17119 C  CD1   . TYR   B  1  1096 ? 4.320   45.755  80.586  1.00 13.78 ? 1094 TYR   B CD1   1 
ATOM   17120 C  CD2   . TYR   B  1  1096 ? 2.427   47.148  80.231  1.00 15.04 ? 1094 TYR   B CD2   1 
ATOM   17121 C  CE1   . TYR   B  1  1096 ? 4.900   46.235  79.421  1.00 14.34 ? 1094 TYR   B CE1   1 
ATOM   17122 C  CE2   . TYR   B  1  1096 ? 2.994   47.630  79.065  1.00 14.61 ? 1094 TYR   B CE2   1 
ATOM   17123 C  CZ    . TYR   B  1  1096 ? 4.223   47.164  78.664  1.00 13.85 ? 1094 TYR   B CZ    1 
ATOM   17124 O  OH    . TYR   B  1  1096 ? 4.783   47.660  77.508  1.00 14.61 ? 1094 TYR   B OH    1 
ATOM   17125 N  N     . THR   B  1  1097 ? 3.682   48.625  83.565  1.00 13.24 ? 1095 THR   B N     1 
ATOM   17126 C  CA    . THR   B  1  1097 ? 3.581   50.064  83.692  1.00 13.49 ? 1095 THR   B CA    1 
ATOM   17127 C  C     . THR   B  1  1097 ? 4.620   50.720  82.802  1.00 12.91 ? 1095 THR   B C     1 
ATOM   17128 O  O     . THR   B  1  1097 ? 5.698   50.171  82.565  1.00 14.03 ? 1095 THR   B O     1 
ATOM   17129 C  CB    . THR   B  1  1097 ? 3.822   50.504  85.136  1.00 16.29 ? 1095 THR   B CB    1 
ATOM   17130 O  OG1   . THR   B  1  1097 ? 5.125   50.092  85.558  1.00 20.56 ? 1095 THR   B OG1   1 
ATOM   17131 C  CG2   . THR   B  1  1097 ? 2.813   49.876  86.040  1.00 17.77 ? 1095 THR   B CG2   1 
ATOM   17132 N  N     . LEU   B  1  1098 ? 4.287   51.905  82.316  1.00 13.59 ? 1096 LEU   B N     1 
ATOM   17133 C  CA    . LEU   B  1  1098 ? 5.197   52.680  81.482  1.00 12.16 ? 1096 LEU   B CA    1 
ATOM   17134 C  C     . LEU   B  1  1098 ? 5.617   53.928  82.231  1.00 12.07 ? 1096 LEU   B C     1 
ATOM   17135 O  O     . LEU   B  1  1098 ? 4.785   54.758  82.619  1.00 13.56 ? 1096 LEU   B O     1 
ATOM   17136 C  CB    . LEU   B  1  1098 ? 4.560   53.055  80.149  1.00 12.37 ? 1096 LEU   B CB    1 
ATOM   17137 C  CG    . LEU   B  1  1098 ? 4.206   51.846  79.294  1.00 12.61 ? 1096 LEU   B CG    1 
ATOM   17138 C  CD1   . LEU   B  1  1098 ? 3.572   52.346  78.006  1.00 13.96 ? 1096 LEU   B CD1   1 
ATOM   17139 C  CD2   . LEU   B  1  1098 ? 5.420   50.980  78.993  1.00 14.39 ? 1096 LEU   B CD2   1 
ATOM   17140 N  N     . HIS   B  1  1099 ? 6.924   54.064  82.397  1.00 12.45 ? 1097 HIS   B N     1 
ATOM   17141 C  CA    . HIS   B  1  1099 ? 7.538   55.171  83.101  1.00 13.64 ? 1097 HIS   B CA    1 
ATOM   17142 C  C     . HIS   B  1  1099 ? 8.399   55.939  82.122  1.00 13.40 ? 1097 HIS   B C     1 
ATOM   17143 O  O     . HIS   B  1  1099 ? 8.636   55.496  80.995  1.00 13.83 ? 1097 HIS   B O     1 
ATOM   17144 C  CB    . HIS   B  1  1099 ? 8.440   54.636  84.207  1.00 15.11 ? 1097 HIS   B CB    1 
ATOM   17145 C  CG    . HIS   B  1  1099 ? 7.722   53.783  85.197  1.00 17.02 ? 1097 HIS   B CG    1 
ATOM   17146 N  ND1   . HIS   B  1  1099 ? 7.339   54.248  86.436  1.00 19.77 ? 1097 HIS   B ND1   1 
ATOM   17147 C  CD2   . HIS   B  1  1099 ? 7.312   52.496  85.131  1.00 20.10 ? 1097 HIS   B CD2   1 
ATOM   17148 C  CE1   . HIS   B  1  1099 ? 6.734   53.276  87.098  1.00 21.22 ? 1097 HIS   B CE1   1 
ATOM   17149 N  NE2   . HIS   B  1  1099 ? 6.699   52.205  86.326  1.00 20.31 ? 1097 HIS   B NE2   1 
ATOM   17150 N  N     . ALA   B  1  1100 ? 8.886   57.088  82.570  1.00 14.74 ? 1098 ALA   B N     1 
ATOM   17151 C  CA    . ALA   B  1  1100 ? 9.889   57.784  81.777  1.00 15.30 ? 1098 ALA   B CA    1 
ATOM   17152 C  C     . ALA   B  1  1100 ? 11.126  56.912  81.638  1.00 15.41 ? 1098 ALA   B C     1 
ATOM   17153 O  O     . ALA   B  1  1100 ? 11.440  56.106  82.516  1.00 16.63 ? 1098 ALA   B O     1 
ATOM   17154 C  CB    . ALA   B  1  1100 ? 10.279  59.097  82.448  1.00 16.86 ? 1098 ALA   B CB    1 
ATOM   17155 N  N     . ARG   B  1  1101 ? 11.820  57.065  80.506  1.00 15.14 ? 1099 ARG   B N     1 
ATOM   17156 C  CA    . ARG   B  1  1101 ? 13.123  56.426  80.340  1.00 15.62 ? 1099 ARG   B CA    1 
ATOM   17157 C  C     . ARG   B  1  1101 ? 14.168  57.020  81.276  1.00 15.17 ? 1099 ARG   B C     1 
ATOM   17158 O  O     . ARG   B  1  1101 ? 14.991  56.289  81.832  1.00 16.69 ? 1099 ARG   B O     1 
ATOM   17159 C  CB    . ARG   B  1  1101 ? 13.583  56.530  78.886  1.00 18.09 ? 1099 ARG   B CB    1 
ATOM   17160 C  CG    . ARG   B  1  1101 ? 12.993  55.474  77.968  1.00 19.08 ? 1099 ARG   B CG    1 
ATOM   17161 C  CD    . ARG   B  1  1101 ? 13.810  54.193  77.987  1.00 18.77 ? 1099 ARG   B CD    1 
ATOM   17162 N  NE    . ARG   B  1  1101 ? 13.254  53.204  77.070  1.00 19.63 ? 1099 ARG   B NE    1 
ATOM   17163 C  CZ    . ARG   B  1  1101 ? 13.970  52.322  76.386  1.00 17.87 ? 1099 ARG   B CZ    1 
ATOM   17164 N  NH1   . ARG   B  1  1101 ? 15.290  52.240  76.515  1.00 16.32 ? 1099 ARG   B NH1   1 
ATOM   17165 N  NH2   . ARG   B  1  1101 ? 13.355  51.510  75.535  1.00 20.53 ? 1099 ARG   B NH2   1 
ATOM   17166 N  N     . GLY   B  1  1102 ? 14.147  58.329  81.475  1.00 14.04 ? 1100 GLY   B N     1 
ATOM   17167 C  CA    . GLY   B  1  1102 ? 15.176  58.969  82.263  1.00 16.90 ? 1100 GLY   B CA    1 
ATOM   17168 C  C     . GLY   B  1  1102 ? 15.614  60.246  81.585  1.00 16.91 ? 1100 GLY   B C     1 
ATOM   17169 O  O     . GLY   B  1  1102 ? 14.793  61.123  81.305  1.00 17.35 ? 1100 GLY   B O     1 
ATOM   17170 N  N     . ARG   B  1  1103 ? 16.905  60.373  81.315  1.00 16.55 ? 1101 ARG   B N     1 
ATOM   17171 C  CA    . ARG   B  1  1103 ? 17.419  61.540  80.618  1.00 16.55 ? 1101 ARG   B CA    1 
ATOM   17172 C  C     . ARG   B  1  1103 ? 17.756  61.145  79.187  1.00 16.22 ? 1101 ARG   B C     1 
ATOM   17173 O  O     . ARG   B  1  1103 ? 18.480  60.169  78.961  1.00 17.59 ? 1101 ARG   B O     1 
ATOM   17174 C  CB    . ARG   B  1  1103 ? 18.647  62.118  81.323  1.00 17.27 ? 1101 ARG   B CB    1 
ATOM   17175 C  CG    . ARG   B  1  1103 ? 19.147  63.383  80.640  1.00 18.78 ? 1101 ARG   B CG    1 
ATOM   17176 C  CD    . ARG   B  1  1103 ? 20.148  64.149  81.492  1.00 24.38 ? 1101 ARG   B CD    1 
ATOM   17177 N  NE    . ARG   B  1  1103 ? 19.481  64.925  82.531  1.00 30.13 ? 1101 ARG   B NE    1 
ATOM   17178 C  CZ    . ARG   B  1  1103 ? 19.596  64.705  83.831  1.00 34.70 ? 1101 ARG   B CZ    1 
ATOM   17179 N  NH1   . ARG   B  1  1103 ? 20.374  63.743  84.303  1.00 43.05 ? 1101 ARG   B NH1   1 
ATOM   17180 N  NH2   . ARG   B  1  1103 ? 18.920  65.477  84.680  1.00 30.59 ? 1101 ARG   B NH2   1 
ATOM   17181 N  N     . ILE   B  1  1104 ? 17.213  61.886  78.232  1.00 15.01 ? 1102 ILE   B N     1 
ATOM   17182 C  CA    . ILE   B  1  1104 ? 17.396  61.593  76.815  1.00 14.62 ? 1102 ILE   B CA    1 
ATOM   17183 C  C     . ILE   B  1  1104 ? 18.418  62.573  76.261  1.00 14.79 ? 1102 ILE   B C     1 
ATOM   17184 O  O     . ILE   B  1  1104 ? 18.315  63.787  76.482  1.00 15.73 ? 1102 ILE   B O     1 
ATOM   17185 C  CB    . ILE   B  1  1104 ? 16.067  61.692  76.049  1.00 13.85 ? 1102 ILE   B CB    1 
ATOM   17186 C  CG1   . ILE   B  1  1104 ? 14.978  60.838  76.728  1.00 15.81 ? 1102 ILE   B CG1   1 
ATOM   17187 C  CG2   . ILE   B  1  1104 ? 16.244  61.283  74.587  1.00 15.10 ? 1102 ILE   B CG2   1 
ATOM   17188 C  CD1   . ILE   B  1  1104 ? 15.294  59.370  76.791  1.00 16.69 ? 1102 ILE   B CD1   1 
ATOM   17189 N  N     . LEU   B  1  1105 ? 19.392  62.050  75.528  1.00 14.27 ? 1103 LEU   B N     1 
ATOM   17190 C  CA    . LEU   B  1  1105 ? 20.339  62.892  74.816  1.00 16.13 ? 1103 LEU   B CA    1 
ATOM   17191 C  C     . LEU   B  1  1105 ? 19.668  63.426  73.556  1.00 14.46 ? 1103 LEU   B C     1 
ATOM   17192 O  O     . LEU   B  1  1105 ? 19.148  62.652  72.750  1.00 14.71 ? 1103 LEU   B O     1 
ATOM   17193 C  CB    . LEU   B  1  1105 ? 21.560  62.056  74.456  1.00 16.37 ? 1103 LEU   B CB    1 
ATOM   17194 C  CG    . LEU   B  1  1105 ? 22.605  62.732  73.572  1.00 16.65 ? 1103 LEU   B CG    1 
ATOM   17195 C  CD1   . LEU   B  1  1105 ? 23.222  63.922  74.288  1.00 17.03 ? 1103 LEU   B CD1   1 
ATOM   17196 C  CD2   . LEU   B  1  1105 ? 23.660  61.707  73.170  1.00 17.34 ? 1103 LEU   B CD2   1 
ATOM   17197 N  N     . LEU   B  1  1106 ? 19.640  64.738  73.407  1.00 14.81 ? 1104 LEU   B N     1 
ATOM   17198 C  CA    . LEU   B  1  1106 ? 19.045  65.371  72.245  1.00 15.63 ? 1104 LEU   B CA    1 
ATOM   17199 C  C     . LEU   B  1  1106 ? 20.175  65.920  71.399  1.00 15.72 ? 1104 LEU   B C     1 
ATOM   17200 O  O     . LEU   B  1  1106 ? 21.012  66.679  71.898  1.00 17.28 ? 1104 LEU   B O     1 
ATOM   17201 C  CB    . LEU   B  1  1106 ? 18.127  66.521  72.662  1.00 16.80 ? 1104 LEU   B CB    1 
ATOM   17202 C  CG    . LEU   B  1  1106 ? 16.650  66.176  72.810  1.00 21.51 ? 1104 LEU   B CG    1 
ATOM   17203 C  CD1   . LEU   B  1  1106 ? 16.417  64.864  73.523  1.00 22.59 ? 1104 LEU   B CD1   1 
ATOM   17204 C  CD2   . LEU   B  1  1106 ? 15.901  67.318  73.478  1.00 16.90 ? 1104 LEU   B CD2   1 
ATOM   17205 N  N     . VAL   B  1  1107 ? 20.198  65.527  70.133  1.00 14.18 ? 1105 VAL   B N     1 
ATOM   17206 C  CA    . VAL   B  1  1107 ? 21.213  66.018  69.206  1.00 16.45 ? 1105 VAL   B CA    1 
ATOM   17207 C  C     . VAL   B  1  1107 ? 20.457  66.699  68.078  1.00 15.76 ? 1105 VAL   B C     1 
ATOM   17208 O  O     . VAL   B  1  1107 ? 20.250  66.100  67.013  1.00 17.15 ? 1105 VAL   B O     1 
ATOM   17209 C  CB    . VAL   B  1  1107 ? 22.125  64.890  68.704  1.00 15.65 ? 1105 VAL   B CB    1 
ATOM   17210 C  CG1   . VAL   B  1  1107 ? 23.304  65.488  67.931  1.00 17.74 ? 1105 VAL   B CG1   1 
ATOM   17211 C  CG2   . VAL   B  1  1107 ? 22.619  64.059  69.868  1.00 16.38 ? 1105 VAL   B CG2   1 
ATOM   17212 N  N     . PRO   B  1  1108 ? 20.003  67.925  68.281  1.00 14.83 ? 1106 PRO   B N     1 
ATOM   17213 C  CA    . PRO   B  1  1108 ? 19.252  68.617  67.242  1.00 17.53 ? 1106 PRO   B CA    1 
ATOM   17214 C  C     . PRO   B  1  1108 ? 20.192  69.248  66.234  1.00 18.25 ? 1106 PRO   B C     1 
ATOM   17215 O  O     . PRO   B  1  1108 ? 21.385  69.439  66.480  1.00 20.67 ? 1106 PRO   B O     1 
ATOM   17216 C  CB    . PRO   B  1  1108 ? 18.536  69.718  68.029  1.00 17.83 ? 1106 PRO   B CB    1 
ATOM   17217 C  CG    . PRO   B  1  1108 ? 19.519  70.044  69.121  1.00 18.31 ? 1106 PRO   B CG    1 
ATOM   17218 C  CD    . PRO   B  1  1108 ? 20.058  68.702  69.533  1.00 18.04 ? 1106 PRO   B CD    1 
ATOM   17219 N  N     . ALA   B  1  1109 ? 19.615  69.606  65.096  1.00 17.88 ? 1107 ALA   B N     1 
ATOM   17220 C  CA    . ALA   B  1  1109 ? 20.290  70.419  64.095  1.00 19.36 ? 1107 ALA   B CA    1 
ATOM   17221 C  C     . ALA   B  1  1109 ? 19.658  71.789  63.952  1.00 22.07 ? 1107 ALA   B C     1 
ATOM   17222 O  O     . ALA   B  1  1109 ? 20.359  72.780  63.740  1.00 23.56 ? 1107 ALA   B O     1 
ATOM   17223 C  CB    . ALA   B  1  1109 ? 20.254  69.705  62.740  1.00 19.95 ? 1107 ALA   B CB    1 
ATOM   17224 N  N     . THR   B  1  1110 ? 18.340  71.865  64.085  1.00 20.28 ? 1108 THR   B N     1 
ATOM   17225 C  CA    . THR   B  1  1110 ? 17.606  73.097  63.866  1.00 20.60 ? 1108 THR   B CA    1 
ATOM   17226 C  C     . THR   B  1  1110 ? 16.742  73.391  65.079  1.00 19.91 ? 1108 THR   B C     1 
ATOM   17227 O  O     . THR   B  1  1110 ? 16.444  72.507  65.889  1.00 19.17 ? 1108 THR   B O     1 
ATOM   17228 C  CB    . THR   B  1  1110 ? 16.687  73.005  62.638  1.00 22.05 ? 1108 THR   B CB    1 
ATOM   17229 O  OG1   . THR   B  1  1110 ? 15.673  72.013  62.862  1.00 21.33 ? 1108 THR   B OG1   1 
ATOM   17230 C  CG2   . THR   B  1  1110 ? 17.482  72.629  61.392  1.00 24.20 ? 1108 THR   B CG2   1 
ATOM   17231 N  N     . GLU   B  1  1111 ? 16.316  74.648  65.175  1.00 20.62 ? 1109 GLU   B N     1 
ATOM   17232 C  CA    . GLU   B  1  1111 ? 15.461  75.049  66.286  1.00 21.05 ? 1109 GLU   B CA    1 
ATOM   17233 C  C     . GLU   B  1  1111 ? 14.163  74.252  66.292  1.00 21.55 ? 1109 GLU   B C     1 
ATOM   17234 O  O     . GLU   B  1  1111 ? 13.755  73.722  67.331  1.00 20.12 ? 1109 GLU   B O     1 
ATOM   17235 C  CB    . GLU   B  1  1111 ? 15.177  76.540  66.193  1.00 20.99 ? 1109 GLU   B CB    1 
ATOM   17236 C  CG    . GLU   B  1  1111 ? 14.098  77.002  67.138  1.00 23.72 ? 1109 GLU   B CG    1 
ATOM   17237 C  CD    . GLU   B  1  1111 ? 13.930  78.504  67.106  1.00 26.94 ? 1109 GLU   B CD    1 
ATOM   17238 O  OE1   . GLU   B  1  1111 ? 14.774  79.202  67.698  1.00 26.70 ? 1109 GLU   B OE1   1 
ATOM   17239 O  OE2   . GLU   B  1  1111 ? 12.964  78.978  66.475  1.00 30.23 ? 1109 GLU   B OE2   1 
ATOM   17240 N  N     . SER   B  1  1112 ? 13.502  74.158  65.137  1.00 20.81 ? 1110 SER   B N     1 
ATOM   17241 C  CA    . SER   B  1  1112 ? 12.271  73.382  65.067  1.00 19.63 ? 1110 SER   B CA    1 
ATOM   17242 C  C     . SER   B  1  1112 ? 12.523  71.932  65.438  1.00 20.08 ? 1110 SER   B C     1 
ATOM   17243 O  O     . SER   B  1  1112 ? 11.723  71.317  66.153  1.00 20.25 ? 1110 SER   B O     1 
ATOM   17244 C  CB    . SER   B  1  1112 ? 11.671  73.462  63.668  1.00 23.83 ? 1110 SER   B CB    1 
ATOM   17245 O  OG    . SER   B  1  1112 ? 10.447  72.749  63.628  1.00 24.32 ? 1110 SER   B OG    1 
ATOM   17246 N  N     . GLY   B  1  1113 ? 13.634  71.365  64.965  1.00 19.33 ? 1111 GLY   B N     1 
ATOM   17247 C  CA    . GLY   B  1  1113 ? 13.946  69.992  65.324  1.00 17.87 ? 1111 GLY   B CA    1 
ATOM   17248 C  C     . GLY   B  1  1113 ? 14.101  69.823  66.821  1.00 18.03 ? 1111 GLY   B C     1 
ATOM   17249 O  O     . GLY   B  1  1113 ? 13.581  68.871  67.407  1.00 17.23 ? 1111 GLY   B O     1 
ATOM   17250 N  N     . LEU   B  1  1114 ? 14.803  70.757  67.461  1.00 17.97 ? 1112 LEU   B N     1 
ATOM   17251 C  CA    . LEU   B  1  1114 ? 14.947  70.718  68.911  1.00 17.16 ? 1112 LEU   B CA    1 
ATOM   17252 C  C     . LEU   B  1  1114 ? 13.591  70.797  69.600  1.00 17.69 ? 1112 LEU   B C     1 
ATOM   17253 O  O     . LEU   B  1  1114 ? 13.342  70.068  70.563  1.00 16.20 ? 1112 LEU   B O     1 
ATOM   17254 C  CB    . LEU   B  1  1114 ? 15.843  71.861  69.379  1.00 18.70 ? 1112 LEU   B CB    1 
ATOM   17255 C  CG    . LEU   B  1  1114 ? 15.898  72.085  70.885  1.00 18.19 ? 1112 LEU   B CG    1 
ATOM   17256 C  CD1   . LEU   B  1  1114 ? 16.400  70.837  71.579  1.00 19.37 ? 1112 LEU   B CD1   1 
ATOM   17257 C  CD2   . LEU   B  1  1114 ? 16.778  73.286  71.210  1.00 22.98 ? 1112 LEU   B CD2   1 
ATOM   17258 N  N     . TYR   B  1  1115 ? 12.705  71.674  69.125  1.00 17.97 ? 1113 TYR   B N     1 
ATOM   17259 C  CA    . TYR   B  1  1115 ? 11.390  71.772  69.753  1.00 18.02 ? 1113 TYR   B CA    1 
ATOM   17260 C  C     . TYR   B  1  1115 ? 10.625  70.464  69.617  1.00 18.07 ? 1113 TYR   B C     1 
ATOM   17261 O  O     . TYR   B  1  1115 ? 9.967   70.025  70.565  1.00 17.81 ? 1113 TYR   B O     1 
ATOM   17262 C  CB    . TYR   B  1  1115 ? 10.588  72.910  69.135  1.00 19.26 ? 1113 TYR   B CB    1 
ATOM   17263 C  CG    . TYR   B  1  1115 ? 11.106  74.300  69.427  1.00 17.96 ? 1113 TYR   B CG    1 
ATOM   17264 C  CD1   . TYR   B  1  1115 ? 12.052  74.530  70.415  1.00 19.26 ? 1113 TYR   B CD1   1 
ATOM   17265 C  CD2   . TYR   B  1  1115 ? 10.635  75.383  68.708  1.00 23.89 ? 1113 TYR   B CD2   1 
ATOM   17266 C  CE1   . TYR   B  1  1115 ? 12.518  75.815  70.665  1.00 21.88 ? 1113 TYR   B CE1   1 
ATOM   17267 C  CE2   . TYR   B  1  1115 ? 11.085  76.658  68.956  1.00 24.43 ? 1113 TYR   B CE2   1 
ATOM   17268 C  CZ    . TYR   B  1  1115 ? 12.025  76.869  69.936  1.00 26.27 ? 1113 TYR   B CZ    1 
ATOM   17269 O  OH    . TYR   B  1  1115 ? 12.478  78.149  70.172  1.00 27.99 ? 1113 TYR   B OH    1 
ATOM   17270 N  N     . HIS   B  1  1116 ? 10.712  69.822  68.451  1.00 16.29 ? 1114 HIS   B N     1 
ATOM   17271 C  CA    . HIS   B  1  1116 ? 10.060  68.532  68.267  1.00 16.91 ? 1114 HIS   B CA    1 
ATOM   17272 C  C     . HIS   B  1  1116 ? 10.699  67.464  69.138  1.00 17.74 ? 1114 HIS   B C     1 
ATOM   17273 O  O     . HIS   B  1  1116 ? 10.003  66.606  69.693  1.00 18.02 ? 1114 HIS   B O     1 
ATOM   17274 C  CB    . HIS   B  1  1116 ? 10.111  68.111  66.802  1.00 17.45 ? 1114 HIS   B CB    1 
ATOM   17275 C  CG    . HIS   B  1  1116 ? 9.080   68.772  65.943  1.00 20.71 ? 1114 HIS   B CG    1 
ATOM   17276 N  ND1   . HIS   B  1  1116 ? 9.298   69.974  65.302  1.00 21.97 ? 1114 HIS   B ND1   1 
ATOM   17277 C  CD2   . HIS   B  1  1116 ? 7.825   68.389  65.608  1.00 19.94 ? 1114 HIS   B CD2   1 
ATOM   17278 C  CE1   . HIS   B  1  1116 ? 8.218   70.307  64.617  1.00 23.80 ? 1114 HIS   B CE1   1 
ATOM   17279 N  NE2   . HIS   B  1  1116 ? 7.312   69.362  64.783  1.00 23.27 ? 1114 HIS   B NE2   1 
ATOM   17280 N  N     . GLN   B  1  1117 ? 12.031  67.472  69.251  1.00 16.35 ? 1115 GLN   B N     1 
ATOM   17281 C  CA    . GLN   B  1  1117 ? 12.683  66.494  70.111  1.00 15.17 ? 1115 GLN   B CA    1 
ATOM   17282 C  C     . GLN   B  1  1117 ? 12.283  66.700  71.559  1.00 14.62 ? 1115 GLN   B C     1 
ATOM   17283 O  O     . GLN   B  1  1117 ? 12.029  65.732  72.286  1.00 15.44 ? 1115 GLN   B O     1 
ATOM   17284 C  CB    . GLN   B  1  1117 ? 14.200  66.616  69.984  1.00 16.03 ? 1115 GLN   B CB    1 
ATOM   17285 C  CG    . GLN   B  1  1117 ? 14.733  66.148  68.658  1.00 15.56 ? 1115 GLN   B CG    1 
ATOM   17286 C  CD    . GLN   B  1  1117 ? 16.228  66.329  68.572  1.00 16.43 ? 1115 GLN   B CD    1 
ATOM   17287 O  OE1   . GLN   B  1  1117 ? 16.823  67.008  69.402  1.00 17.41 ? 1115 GLN   B OE1   1 
ATOM   17288 N  NE2   . GLN   B  1  1117 ? 16.840  65.721  67.568  1.00 17.31 ? 1115 GLN   B NE2   1 
ATOM   17289 N  N     . LEU   B  1  1118 ? 12.271  67.951  72.001  1.00 15.28 ? 1116 LEU   B N     1 
ATOM   17290 C  CA    . LEU   B  1  1118 ? 11.859  68.248  73.364  1.00 15.63 ? 1116 LEU   B CA    1 
ATOM   17291 C  C     . LEU   B  1  1118 ? 10.431  67.808  73.605  1.00 16.32 ? 1116 LEU   B C     1 
ATOM   17292 O  O     . LEU   B  1  1118 ? 10.121  67.249  74.659  1.00 17.34 ? 1116 LEU   B O     1 
ATOM   17293 C  CB    . LEU   B  1  1118 ? 11.970  69.742  73.631  1.00 17.47 ? 1116 LEU   B CB    1 
ATOM   17294 C  CG    . LEU   B  1  1118 ? 13.373  70.247  73.899  1.00 22.62 ? 1116 LEU   B CG    1 
ATOM   17295 C  CD1   . LEU   B  1  1118 ? 13.353  71.765  73.857  1.00 21.93 ? 1116 LEU   B CD1   1 
ATOM   17296 C  CD2   . LEU   B  1  1118 ? 13.846  69.753  75.253  1.00 20.77 ? 1116 LEU   B CD2   1 
ATOM   17297 N  N     . ALA   B  1  1119 ? 9.543   68.067  72.650  1.00 17.53 ? 1117 ALA   B N     1 
ATOM   17298 C  CA    . ALA   B  1  1119 ? 8.154   67.654  72.820  1.00 16.85 ? 1117 ALA   B CA    1 
ATOM   17299 C  C     . ALA   B  1  1119 ? 8.069   66.155  73.038  1.00 17.74 ? 1117 ALA   B C     1 
ATOM   17300 O  O     . ALA   B  1  1119 ? 7.415   65.686  73.979  1.00 15.70 ? 1117 ALA   B O     1 
ATOM   17301 C  CB    . ALA   B  1  1119 ? 7.344   68.057  71.592  1.00 17.39 ? 1117 ALA   B CB    1 
ATOM   17302 N  N     . ALA   B  1  1120 ? 8.761   65.387  72.199  1.00 14.62 ? 1118 ALA   B N     1 
ATOM   17303 C  CA    . ALA   B  1  1120 ? 8.709   63.938  72.321  1.00 13.86 ? 1118 ALA   B CA    1 
ATOM   17304 C  C     . ALA   B  1  1120 ? 9.252   63.495  73.666  1.00 14.64 ? 1118 ALA   B C     1 
ATOM   17305 O  O     . ALA   B  1  1120 ? 8.662   62.641  74.340  1.00 15.77 ? 1118 ALA   B O     1 
ATOM   17306 C  CB    . ALA   B  1  1120 ? 9.500   63.284  71.193  1.00 16.03 ? 1118 ALA   B CB    1 
ATOM   17307 N  N     . ALA   B  1  1121 ? 10.393  64.058  74.074  1.00 13.43 ? 1119 ALA   B N     1 
ATOM   17308 C  CA    . ALA   B  1  1121 ? 11.008  63.620  75.319  1.00 13.38 ? 1119 ALA   B CA    1 
ATOM   17309 C  C     . ALA   B  1  1121 ? 10.203  64.058  76.536  1.00 12.86 ? 1119 ALA   B C     1 
ATOM   17310 O  O     . ALA   B  1  1121 ? 10.043  63.280  77.485  1.00 13.78 ? 1119 ALA   B O     1 
ATOM   17311 C  CB    . ALA   B  1  1121 ? 12.445  64.134  75.398  1.00 16.37 ? 1119 ALA   B CB    1 
ATOM   17312 N  N     . LEU   B  1  1122 ? 9.701   65.291  76.535  1.00 14.13 ? 1120 LEU   B N     1 
ATOM   17313 C  CA    . LEU   B  1  1122 ? 8.937   65.757  77.692  1.00 14.14 ? 1120 LEU   B CA    1 
ATOM   17314 C  C     . LEU   B  1  1122 ? 7.609   65.031  77.812  1.00 14.33 ? 1120 LEU   B C     1 
ATOM   17315 O  O     . LEU   B  1  1122 ? 7.175   64.712  78.924  1.00 14.96 ? 1120 LEU   B O     1 
ATOM   17316 C  CB    . LEU   B  1  1122 ? 8.695   67.258  77.631  1.00 15.68 ? 1120 LEU   B CB    1 
ATOM   17317 C  CG    . LEU   B  1  1122 ? 9.950   68.121  77.665  1.00 17.45 ? 1120 LEU   B CG    1 
ATOM   17318 C  CD1   . LEU   B  1  1122 ? 9.578   69.552  77.351  1.00 18.03 ? 1120 LEU   B CD1   1 
ATOM   17319 C  CD2   . LEU   B  1  1122 ? 10.639  68.034  79.020  1.00 18.58 ? 1120 LEU   B CD2   1 
ATOM   17320 N  N     . ALA   B  1  1123 ? 6.965   64.751  76.681  1.00 14.08 ? 1121 ALA   B N     1 
ATOM   17321 C  CA    . ALA   B  1  1123 ? 5.667   64.083  76.713  1.00 13.85 ? 1121 ALA   B CA    1 
ATOM   17322 C  C     . ALA   B  1  1123 ? 5.771   62.699  77.317  1.00 14.99 ? 1121 ALA   B C     1 
ATOM   17323 O  O     . ALA   B  1  1123 ? 4.765   62.164  77.804  1.00 14.32 ? 1121 ALA   B O     1 
ATOM   17324 C  CB    . ALA   B  1  1123 ? 5.131   63.940  75.296  1.00 14.60 ? 1121 ALA   B CB    1 
ATOM   17325 N  N     . THR   B  1  1124 ? 6.955   62.100  77.268  1.00 13.01 ? 1122 THR   B N     1 
ATOM   17326 C  CA    . THR   B  1  1124 ? 7.192   60.785  77.823  1.00 12.87 ? 1122 THR   B CA    1 
ATOM   17327 C  C     . THR   B  1  1124 ? 7.873   60.860  79.184  1.00 12.02 ? 1122 THR   B C     1 
ATOM   17328 O  O     . THR   B  1  1124 ? 8.393   59.854  79.669  1.00 15.55 ? 1122 THR   B O     1 
ATOM   17329 C  CB    . THR   B  1  1124 ? 7.960   59.928  76.817  1.00 14.56 ? 1122 THR   B CB    1 
ATOM   17330 O  OG1   . THR   B  1  1124 ? 9.033   60.696  76.246  1.00 13.99 ? 1122 THR   B OG1   1 
ATOM   17331 C  CG2   . THR   B  1  1124 ? 7.030   59.495  75.686  1.00 13.56 ? 1122 THR   B CG2   1 
ATOM   17332 N  N     . GLY   B  1  1125 ? 7.858   62.037  79.806  1.00 12.90 ? 1123 GLY   B N     1 
ATOM   17333 C  CA    . GLY   B  1  1125 ? 8.277   62.194  81.187  1.00 13.69 ? 1123 GLY   B CA    1 
ATOM   17334 C  C     . GLY   B  1  1125 ? 9.760   62.354  81.399  1.00 14.89 ? 1123 GLY   B C     1 
ATOM   17335 O  O     . GLY   B  1  1125 ? 10.209  62.355  82.552  1.00 14.55 ? 1123 GLY   B O     1 
ATOM   17336 N  N     . ASN   B  1  1126 ? 10.527  62.504  80.336  1.00 13.98 ? 1124 ASN   B N     1 
ATOM   17337 C  CA    . ASN   B  1  1126 ? 11.974  62.474  80.430  1.00 13.07 ? 1124 ASN   B CA    1 
ATOM   17338 C  C     . ASN   B  1  1126 ? 12.529  63.861  80.675  1.00 14.97 ? 1124 ASN   B C     1 
ATOM   17339 O  O     . ASN   B  1  1126 ? 11.905  64.880  80.383  1.00 15.31 ? 1124 ASN   B O     1 
ATOM   17340 C  CB    . ASN   B  1  1126 ? 12.566  61.928  79.141  1.00 13.65 ? 1124 ASN   B CB    1 
ATOM   17341 C  CG    . ASN   B  1  1126 ? 12.108  60.533  78.858  1.00 11.86 ? 1124 ASN   B CG    1 
ATOM   17342 O  OD1   . ASN   B  1  1126 ? 12.465  59.608  79.570  1.00 14.83 ? 1124 ASN   B OD1   1 
ATOM   17343 N  ND2   . ASN   B  1  1126 ? 11.292  60.371  77.826  1.00 14.26 ? 1124 ASN   B ND2   1 
ATOM   17344 N  N     . SER   B  1  1127 ? 13.737  63.875  81.225  1.00 15.36 ? 1125 SER   B N     1 
ATOM   17345 C  CA    . SER   B  1  1127 ? 14.572  65.055  81.152  1.00 15.32 ? 1125 SER   B CA    1 
ATOM   17346 C  C     . SER   B  1  1127 ? 15.468  64.899  79.932  1.00 15.70 ? 1125 SER   B C     1 
ATOM   17347 O  O     . SER   B  1  1127 ? 15.497  63.850  79.291  1.00 15.82 ? 1125 SER   B O     1 
ATOM   17348 C  CB    . SER   B  1  1127 ? 15.411  65.194  82.418  1.00 17.76 ? 1125 SER   B CB    1 
ATOM   17349 O  OG    . SER   B  1  1127 ? 16.227  64.052  82.609  1.00 20.65 ? 1125 SER   B OG    1 
ATOM   17350 N  N     . VAL   B  1  1128 ? 16.188  65.960  79.594  1.00 16.91 ? 1126 VAL   B N     1 
ATOM   17351 C  CA    . VAL   B  1  1128 ? 17.013  65.937  78.394  1.00 15.83 ? 1126 VAL   B CA    1 
ATOM   17352 C  C     . VAL   B  1  1128 ? 18.362  66.566  78.679  1.00 16.29 ? 1126 VAL   B C     1 
ATOM   17353 O  O     . VAL   B  1  1128 ? 18.495  67.463  79.521  1.00 18.40 ? 1126 VAL   B O     1 
ATOM   17354 C  CB    . VAL   B  1  1128 ? 16.355  66.648  77.193  1.00 16.60 ? 1126 VAL   B CB    1 
ATOM   17355 C  CG1   . VAL   B  1  1128 ? 15.047  65.959  76.828  1.00 16.63 ? 1126 VAL   B CG1   1 
ATOM   17356 C  CG2   . VAL   B  1  1128 ? 16.117  68.113  77.523  1.00 18.31 ? 1126 VAL   B CG2   1 
ATOM   17357 N  N     . ALA   B  1  1129 ? 19.357  66.099  77.937  1.00 16.21 ? 1127 ALA   B N     1 
ATOM   17358 C  CA    . ALA   B  1  1129 ? 20.622  66.799  77.787  1.00 17.59 ? 1127 ALA   B CA    1 
ATOM   17359 C  C     . ALA   B  1  1129 ? 20.738  67.135  76.315  1.00 14.88 ? 1127 ALA   B C     1 
ATOM   17360 O  O     . ALA   B  1  1129 ? 20.718  66.234  75.472  1.00 15.76 ? 1127 ALA   B O     1 
ATOM   17361 C  CB    . ALA   B  1  1129 ? 21.784  65.911  78.220  1.00 19.37 ? 1127 ALA   B CB    1 
ATOM   17362 N  N     . ILE   B  1  1130 ? 20.818  68.417  76.003  1.00 15.79 ? 1128 ILE   B N     1 
ATOM   17363 C  CA    . ILE   B  1  1130 ? 20.868  68.876  74.626  1.00 15.86 ? 1128 ILE   B CA    1 
ATOM   17364 C  C     . ILE   B  1  1130 ? 22.317  69.110  74.236  1.00 16.48 ? 1128 ILE   B C     1 
ATOM   17365 O  O     . ILE   B  1  1130 ? 23.069  69.775  74.962  1.00 17.01 ? 1128 ILE   B O     1 
ATOM   17366 C  CB    . ILE   B  1  1130 ? 20.053  70.161  74.425  1.00 16.21 ? 1128 ILE   B CB    1 
ATOM   17367 C  CG1   . ILE   B  1  1130 ? 18.631  70.001  74.981  1.00 16.64 ? 1128 ILE   B CG1   1 
ATOM   17368 C  CG2   . ILE   B  1  1130 ? 19.968  70.471  72.943  1.00 16.87 ? 1128 ILE   B CG2   1 
ATOM   17369 C  CD1   . ILE   B  1  1130 ? 17.931  71.325  75.134  1.00 17.32 ? 1128 ILE   B CD1   1 
ATOM   17370 N  N     . ASP   B  1  1131 ? 22.691  68.599  73.072  1.00 16.04 ? 1129 ASP   B N     1 
ATOM   17371 C  CA    . ASP   B  1  1131 ? 24.039  68.784  72.559  1.00 16.45 ? 1129 ASP   B CA    1 
ATOM   17372 C  C     . ASP   B  1  1131 ? 24.365  70.264  72.431  1.00 17.75 ? 1129 ASP   B C     1 
ATOM   17373 O  O     . ASP   B  1  1131 ? 23.775  70.969  71.610  1.00 17.39 ? 1129 ASP   B O     1 
ATOM   17374 C  CB    . ASP   B  1  1131 ? 24.137  68.109  71.203  1.00 16.43 ? 1129 ASP   B CB    1 
ATOM   17375 C  CG    . ASP   B  1  1131 ? 25.482  68.299  70.570  1.00 17.32 ? 1129 ASP   B CG    1 
ATOM   17376 O  OD1   . ASP   B  1  1131 ? 26.460  68.428  71.325  1.00 19.09 ? 1129 ASP   B OD1   1 
ATOM   17377 O  OD2   . ASP   B  1  1131 ? 25.531  68.327  69.335  1.00 19.15 ? 1129 ASP   B OD2   1 
ATOM   17378 N  N     . ALA   B  1  1132 ? 25.332  70.736  73.223  1.00 18.70 ? 1130 ALA   B N     1 
ATOM   17379 C  CA    . ALA   B  1  1132 ? 25.699  72.145  73.167  1.00 17.37 ? 1130 ALA   B CA    1 
ATOM   17380 C  C     . ALA   B  1  1132 ? 26.298  72.511  71.820  1.00 19.16 ? 1130 ALA   B C     1 
ATOM   17381 O  O     . ALA   B  1  1132 ? 26.202  73.668  71.391  1.00 20.95 ? 1130 ALA   B O     1 
ATOM   17382 C  CB    . ALA   B  1  1132 ? 26.675  72.479  74.292  1.00 18.35 ? 1130 ALA   B CB    1 
ATOM   17383 N  N     . ALA   B  1  1133 ? 26.902  71.545  71.131  1.00 18.96 ? 1131 ALA   B N     1 
ATOM   17384 C  CA    . ALA   B  1  1133 ? 27.504  71.853  69.843  1.00 22.88 ? 1131 ALA   B CA    1 
ATOM   17385 C  C     . ALA   B  1  1133 ? 26.468  72.193  68.786  1.00 23.15 ? 1131 ALA   B C     1 
ATOM   17386 O  O     . ALA   B  1  1133 ? 26.838  72.650  67.700  1.00 23.67 ? 1131 ALA   B O     1 
ATOM   17387 C  CB    . ALA   B  1  1133 ? 28.403  70.702  69.383  1.00 21.44 ? 1131 ALA   B CB    1 
ATOM   17388 N  N     . SER   B  1  1134 ? 25.181  71.984  69.077  1.00 19.37 ? 1132 SER   B N     1 
ATOM   17389 C  CA    . SER   B  1  1134 ? 24.149  72.401  68.143  1.00 21.27 ? 1132 SER   B CA    1 
ATOM   17390 C  C     . SER   B  1  1134 ? 24.086  73.913  68.004  1.00 17.85 ? 1132 SER   B C     1 
ATOM   17391 O  O     . SER   B  1  1134 ? 23.567  74.400  67.001  1.00 21.35 ? 1132 SER   B O     1 
ATOM   17392 C  CB    . SER   B  1  1134 ? 22.781  71.890  68.607  1.00 19.66 ? 1132 SER   B CB    1 
ATOM   17393 O  OG    . SER   B  1  1134 ? 22.392  72.525  69.818  1.00 20.31 ? 1132 SER   B OG    1 
ATOM   17394 N  N     . GLY   B  1  1135 ? 24.580  74.654  68.992  1.00 20.42 ? 1133 GLY   B N     1 
ATOM   17395 C  CA    . GLY   B  1  1135 ? 24.517  76.103  68.945  1.00 19.65 ? 1133 GLY   B CA    1 
ATOM   17396 C  C     . GLY   B  1  1135 ? 23.129  76.688  69.095  1.00 22.52 ? 1133 GLY   B C     1 
ATOM   17397 O  O     . GLY   B  1  1135 ? 22.921  77.856  68.754  1.00 25.39 ? 1133 GLY   B O     1 
ATOM   17398 N  N     . LEU   B  1  1136 ? 22.174  75.917  69.615  1.00 21.23 ? 1134 LEU   B N     1 
ATOM   17399 C  CA    . LEU   B  1  1136 ? 20.773  76.316  69.652  1.00 20.20 ? 1134 LEU   B CA    1 
ATOM   17400 C  C     . LEU   B  1  1136 ? 20.350  76.867  71.007  1.00 23.23 ? 1134 LEU   B C     1 
ATOM   17401 O  O     . LEU   B  1  1136 ? 19.148  76.947  71.281  1.00 23.05 ? 1134 LEU   B O     1 
ATOM   17402 C  CB    . LEU   B  1  1136 ? 19.893  75.131  69.262  1.00 20.45 ? 1134 LEU   B CB    1 
ATOM   17403 C  CG    . LEU   B  1  1136 ? 20.070  74.627  67.834  1.00 21.47 ? 1134 LEU   B CG    1 
ATOM   17404 C  CD1   . LEU   B  1  1136 ? 19.267  73.356  67.612  1.00 21.76 ? 1134 LEU   B CD1   1 
ATOM   17405 C  CD2   . LEU   B  1  1136 ? 19.655  75.707  66.847  1.00 23.94 ? 1134 LEU   B CD2   1 
ATOM   17406 N  N     . GLN   B  1  1137 ? 21.306  77.256  71.852  1.00 21.71 ? 1135 GLN   B N     1 
ATOM   17407 C  CA    . GLN   B  1  1137 ? 20.984  77.711  73.202  1.00 22.14 ? 1135 GLN   B CA    1 
ATOM   17408 C  C     . GLN   B  1  1137 ? 19.983  78.865  73.203  1.00 27.67 ? 1135 GLN   B C     1 
ATOM   17409 O  O     . GLN   B  1  1137 ? 19.086  78.915  74.054  1.00 27.68 ? 1135 GLN   B O     1 
ATOM   17410 C  CB    . GLN   B  1  1137 ? 22.265  78.103  73.940  1.00 27.29 ? 1135 GLN   B CB    1 
ATOM   17411 C  CG    . GLN   B  1  1137 ? 23.147  76.921  74.329  1.00 25.05 ? 1135 GLN   B CG    1 
ATOM   17412 C  CD    . GLN   B  1  1137 ? 24.091  76.465  73.219  1.00 23.93 ? 1135 GLN   B CD    1 
ATOM   17413 O  OE1   . GLN   B  1  1137 ? 23.951  76.848  72.057  1.00 23.59 ? 1135 GLN   B OE1   1 
ATOM   17414 N  NE2   . GLN   B  1  1137 ? 25.057  75.628  73.584  1.00 25.84 ? 1135 GLN   B NE2   1 
ATOM   17415 N  N     . ALA   B  1  1138 ? 20.111  79.796  72.253  1.00 24.45 ? 1136 ALA   B N     1 
ATOM   17416 C  CA    . ALA   B  1  1138 ? 19.215  80.950  72.210  1.00 26.68 ? 1136 ALA   B CA    1 
ATOM   17417 C  C     . ALA   B  1  1138 ? 17.778  80.561  71.893  1.00 29.57 ? 1136 ALA   B C     1 
ATOM   17418 O  O     . ALA   B  1  1138 ? 16.869  81.368  72.113  1.00 29.86 ? 1136 ALA   B O     1 
ATOM   17419 C  CB    . ALA   B  1  1138 ? 19.710  81.983  71.195  1.00 26.79 ? 1136 ALA   B CB    1 
ATOM   17420 N  N     . SER   B  1  1139 ? 17.554  79.350  71.380  1.00 26.04 ? 1137 SER   B N     1 
ATOM   17421 C  CA    . SER   B  1  1139 ? 16.208  78.896  71.058  1.00 24.81 ? 1137 SER   B CA    1 
ATOM   17422 C  C     . SER   B  1  1139 ? 15.376  78.606  72.299  1.00 27.48 ? 1137 SER   B C     1 
ATOM   17423 O  O     . SER   B  1  1139 ? 14.146  78.541  72.200  1.00 26.12 ? 1137 SER   B O     1 
ATOM   17424 C  CB    . SER   B  1  1139 ? 16.284  77.641  70.188  1.00 25.74 ? 1137 SER   B CB    1 
ATOM   17425 O  OG    . SER   B  1  1139 ? 16.800  77.947  68.908  1.00 27.85 ? 1137 SER   B OG    1 
ATOM   17426 N  N     . LEU   B  1  1140 ? 16.013  78.421  73.455  1.00 27.32 ? 1138 LEU   B N     1 
ATOM   17427 C  CA    . LEU   B  1  1140 ? 15.324  78.146  74.710  1.00 27.61 ? 1138 LEU   B CA    1 
ATOM   17428 C  C     . LEU   B  1  1140 ? 15.342  79.346  75.650  1.00 29.48 ? 1138 LEU   B C     1 
ATOM   17429 O  O     . LEU   B  1  1140 ? 15.271  79.186  76.870  1.00 33.55 ? 1138 LEU   B O     1 
ATOM   17430 C  CB    . LEU   B  1  1140 ? 15.890  76.904  75.394  1.00 25.92 ? 1138 LEU   B CB    1 
ATOM   17431 C  CG    . LEU   B  1  1140 ? 15.682  75.615  74.606  1.00 27.23 ? 1138 LEU   B CG    1 
ATOM   17432 C  CD1   . LEU   B  1  1140 ? 16.089  74.397  75.424  1.00 24.94 ? 1138 LEU   B CD1   1 
ATOM   17433 C  CD2   . LEU   B  1  1140 ? 14.238  75.498  74.128  1.00 29.18 ? 1138 LEU   B CD2   1 
ATOM   17434 N  N     . LYS   B  1  1141 ? 15.443  80.550  75.099  1.00 33.27 ? 1139 LYS   B N     1 
ATOM   17435 C  CA    . LYS   B  1  1141 ? 15.398  81.748  75.925  1.00 35.61 ? 1139 LYS   B CA    1 
ATOM   17436 C  C     . LYS   B  1  1141 ? 14.018  81.887  76.559  1.00 37.10 ? 1139 LYS   B C     1 
ATOM   17437 O  O     . LYS   B  1  1141 ? 12.996  81.633  75.915  1.00 36.01 ? 1139 LYS   B O     1 
ATOM   17438 C  CB    . LYS   B  1  1141 ? 15.703  82.983  75.076  1.00 35.56 ? 1139 LYS   B CB    1 
ATOM   17439 N  N     . ASN   B  1  1142 ? 13.998  82.263  77.840  1.00 37.60 ? 1140 ASN   B N     1 
ATOM   17440 C  CA    . ASN   B  1  1142 ? 12.758  82.508  78.583  1.00 35.06 ? 1140 ASN   B CA    1 
ATOM   17441 C  C     . ASN   B  1  1142 ? 11.917  81.244  78.757  1.00 35.23 ? 1140 ASN   B C     1 
ATOM   17442 O  O     . ASN   B  1  1142 ? 10.698  81.313  78.917  1.00 32.04 ? 1140 ASN   B O     1 
ATOM   17443 C  CB    . ASN   B  1  1142 ? 11.933  83.651  77.983  1.00 39.12 ? 1140 ASN   B CB    1 
ATOM   17444 N  N     . LEU   B  1  1143 ? 12.558  80.083  78.728  1.00 33.60 ? 1141 LEU   B N     1 
ATOM   17445 C  CA    . LEU   B  1  1143 ? 11.845  78.844  78.982  1.00 29.86 ? 1141 LEU   B CA    1 
ATOM   17446 C  C     . LEU   B  1  1143 ? 11.273  78.870  80.399  1.00 30.47 ? 1141 LEU   B C     1 
ATOM   17447 O  O     . LEU   B  1  1143 ? 11.940  79.340  81.326  1.00 35.83 ? 1141 LEU   B O     1 
ATOM   17448 C  CB    . LEU   B  1  1143 ? 12.821  77.675  78.847  1.00 28.33 ? 1141 LEU   B CB    1 
ATOM   17449 C  CG    . LEU   B  1  1143 ? 12.273  76.275  78.633  1.00 28.79 ? 1141 LEU   B CG    1 
ATOM   17450 C  CD1   . LEU   B  1  1143 ? 11.547  76.171  77.302  1.00 26.83 ? 1141 LEU   B CD1   1 
ATOM   17451 C  CD2   . LEU   B  1  1143 ? 13.422  75.298  78.697  1.00 24.86 ? 1141 LEU   B CD2   1 
ATOM   17452 N  N     . PRO   B  1  1144 ? 10.044  78.393  80.603  1.00 30.76 ? 1142 PRO   B N     1 
ATOM   17453 C  CA    . PRO   B  1  1144 ? 9.509   78.298  81.968  1.00 34.26 ? 1142 PRO   B CA    1 
ATOM   17454 C  C     . PRO   B  1  1144 ? 10.394  77.413  82.834  1.00 31.72 ? 1142 PRO   B C     1 
ATOM   17455 O  O     . PRO   B  1  1144 ? 10.954  76.422  82.364  1.00 26.40 ? 1142 PRO   B O     1 
ATOM   17456 C  CB    . PRO   B  1  1144 ? 8.128   77.657  81.766  1.00 33.05 ? 1142 PRO   B CB    1 
ATOM   17457 C  CG    . PRO   B  1  1144 ? 7.793   77.885  80.332  1.00 33.19 ? 1142 PRO   B CG    1 
ATOM   17458 C  CD    . PRO   B  1  1144 ? 9.100   77.884  79.596  1.00 30.09 ? 1142 PRO   B CD    1 
ATOM   17459 N  N     . GLN   B  1  1145 ? 10.501  77.776  84.119  1.00 31.91 ? 1143 GLN   B N     1 
ATOM   17460 C  CA    . GLN   B  1  1145 ? 11.353  77.029  85.042  1.00 29.19 ? 1143 GLN   B CA    1 
ATOM   17461 C  C     . GLN   B  1  1145 ? 10.952  75.563  85.129  1.00 25.32 ? 1143 GLN   B C     1 
ATOM   17462 O  O     . GLN   B  1  1145 ? 11.816  74.696  85.293  1.00 26.04 ? 1143 GLN   B O     1 
ATOM   17463 C  CB    . GLN   B  1  1145 ? 11.330  77.666  86.434  1.00 33.12 ? 1143 GLN   B CB    1 
ATOM   17464 N  N     . THR   B  1  1146 ? 9.652   75.263  85.027  1.00 27.73 ? 1144 THR   B N     1 
ATOM   17465 C  CA    . THR   B  1  1146 ? 9.230   73.867  85.041  1.00 28.07 ? 1144 THR   B CA    1 
ATOM   17466 C  C     . THR   B  1  1146 ? 9.891   73.093  83.915  1.00 26.33 ? 1144 THR   B C     1 
ATOM   17467 O  O     . THR   B  1  1146 ? 10.318  71.946  84.100  1.00 29.17 ? 1144 THR   B O     1 
ATOM   17468 C  CB    . THR   B  1  1146 ? 7.714   73.770  84.898  1.00 28.79 ? 1144 THR   B CB    1 
ATOM   17469 O  OG1   . THR   B  1  1146 ? 7.293   74.566  83.782  1.00 33.39 ? 1144 THR   B OG1   1 
ATOM   17470 C  CG2   . THR   B  1  1146 ? 7.024   74.249  86.166  1.00 35.70 ? 1144 THR   B CG2   1 
ATOM   17471 N  N     . VAL   B  1  1147 ? 9.990   73.707  82.739  1.00 24.16 ? 1145 VAL   B N     1 
ATOM   17472 C  CA    . VAL   B  1  1147 ? 10.649  73.031  81.633  1.00 21.79 ? 1145 VAL   B CA    1 
ATOM   17473 C  C     . VAL   B  1  1147 ? 12.161  73.077  81.799  1.00 23.47 ? 1145 VAL   B C     1 
ATOM   17474 O  O     . VAL   B  1  1147 ? 12.850  72.076  81.579  1.00 23.71 ? 1145 VAL   B O     1 
ATOM   17475 C  CB    . VAL   B  1  1147 ? 10.193  73.615  80.286  1.00 20.88 ? 1145 VAL   B CB    1 
ATOM   17476 C  CG1   . VAL   B  1  1147 ? 10.774  72.790  79.142  1.00 24.20 ? 1145 VAL   B CG1   1 
ATOM   17477 C  CG2   . VAL   B  1  1147 ? 8.665   73.667  80.212  1.00 22.41 ? 1145 VAL   B CG2   1 
ATOM   17478 N  N     . GLY   B  1  1148 ? 12.699  74.233  82.194  1.00 23.74 ? 1146 GLY   B N     1 
ATOM   17479 C  CA    . GLY   B  1  1148 ? 14.140  74.348  82.347  1.00 23.12 ? 1146 GLY   B CA    1 
ATOM   17480 C  C     . GLY   B  1  1148 ? 14.726  73.369  83.342  1.00 25.28 ? 1146 GLY   B C     1 
ATOM   17481 O  O     . GLY   B  1  1148 ? 15.860  72.911  83.174  1.00 24.63 ? 1146 GLY   B O     1 
ATOM   17482 N  N     . LEU   B  1  1149 ? 13.969  73.025  84.385  1.00 25.59 ? 1147 LEU   B N     1 
ATOM   17483 C  CA    . LEU   B  1  1149 ? 14.443  72.051  85.359  1.00 23.24 ? 1147 LEU   B CA    1 
ATOM   17484 C  C     . LEU   B  1  1149 ? 14.685  70.685  84.735  1.00 24.11 ? 1147 LEU   B C     1 
ATOM   17485 O  O     . LEU   B  1  1149 ? 15.452  69.891  85.290  1.00 25.94 ? 1147 LEU   B O     1 
ATOM   17486 C  CB    . LEU   B  1  1149 ? 13.446  71.921  86.516  1.00 35.05 ? 1147 LEU   B CB    1 
ATOM   17487 N  N     . ARG   B  1  1150 ? 14.045  70.390  83.604  1.00 21.68 ? 1148 ARG   B N     1 
ATOM   17488 C  CA    . ARG   B  1  1150 ? 14.258  69.132  82.900  1.00 20.62 ? 1148 ARG   B CA    1 
ATOM   17489 C  C     . ARG   B  1  1150 ? 15.305  69.239  81.807  1.00 19.00 ? 1148 ARG   B C     1 
ATOM   17490 O  O     . ARG   B  1  1150 ? 15.571  68.239  81.135  1.00 19.23 ? 1148 ARG   B O     1 
ATOM   17491 C  CB    . ARG   B  1  1150 ? 12.961  68.670  82.242  1.00 20.07 ? 1148 ARG   B CB    1 
ATOM   17492 C  CG    . ARG   B  1  1150 ? 11.888  68.220  83.198  1.00 24.23 ? 1148 ARG   B CG    1 
ATOM   17493 C  CD    . ARG   B  1  1150 ? 11.482  66.807  82.875  1.00 23.43 ? 1148 ARG   B CD    1 
ATOM   17494 N  NE    . ARG   B  1  1150 ? 10.225  66.459  83.517  1.00 21.82 ? 1148 ARG   B NE    1 
ATOM   17495 C  CZ    . ARG   B  1  1150 ? 9.164   65.997  82.875  1.00 21.51 ? 1148 ARG   B CZ    1 
ATOM   17496 N  NH1   . ARG   B  1  1150 ? 9.190   65.766  81.569  1.00 18.68 ? 1148 ARG   B NH1   1 
ATOM   17497 N  NH2   . ARG   B  1  1150 ? 8.052   65.753  83.562  1.00 18.77 ? 1148 ARG   B NH2   1 
ATOM   17498 N  N     . VAL   B  1  1151 ? 15.874  70.417  81.588  1.00 20.94 ? 1149 VAL   B N     1 
ATOM   17499 C  CA    . VAL   B  1  1151 ? 16.733  70.669  80.440  1.00 19.87 ? 1149 VAL   B CA    1 
ATOM   17500 C  C     . VAL   B  1  1151 ? 18.139  70.951  80.934  1.00 20.54 ? 1149 VAL   B C     1 
ATOM   17501 O  O     . VAL   B  1  1151 ? 18.344  71.822  81.785  1.00 23.94 ? 1149 VAL   B O     1 
ATOM   17502 C  CB    . VAL   B  1  1151 ? 16.224  71.852  79.599  1.00 20.87 ? 1149 VAL   B CB    1 
ATOM   17503 C  CG1   . VAL   B  1  1151 ? 17.251  72.233  78.526  1.00 24.00 ? 1149 VAL   B CG1   1 
ATOM   17504 C  CG2   . VAL   B  1  1151 ? 14.890  71.520  78.968  1.00 23.76 ? 1149 VAL   B CG2   1 
ATOM   17505 N  N     . SER   B  1  1152 ? 19.105  70.224  80.394  1.00 19.17 ? 1150 SER   B N     1 
ATOM   17506 C  CA    . SER   B  1  1152 ? 20.496  70.595  80.559  1.00 19.41 ? 1150 SER   B CA    1 
ATOM   17507 C  C     . SER   B  1  1152 ? 21.129  70.636  79.182  1.00 19.90 ? 1150 SER   B C     1 
ATOM   17508 O  O     . SER   B  1  1152 ? 20.596  70.090  78.212  1.00 19.85 ? 1150 SER   B O     1 
ATOM   17509 C  CB    . SER   B  1  1152 ? 21.243  69.634  81.488  1.00 22.45 ? 1150 SER   B CB    1 
ATOM   17510 O  OG    . SER   B  1  1152 ? 21.252  68.326  80.960  1.00 28.15 ? 1150 SER   B OG    1 
ATOM   17511 N  N     . TRP   B  1  1153 ? 22.262  71.317  79.099  1.00 20.91 ? 1151 TRP   B N     1 
ATOM   17512 C  CA    . TRP   B  1  1153 ? 23.045  71.390  77.881  1.00 20.30 ? 1151 TRP   B CA    1 
ATOM   17513 C  C     . TRP   B  1  1153 ? 24.344  70.648  78.127  1.00 21.28 ? 1151 TRP   B C     1 
ATOM   17514 O  O     . TRP   B  1  1153 ? 24.978  70.832  79.170  1.00 23.94 ? 1151 TRP   B O     1 
ATOM   17515 C  CB    . TRP   B  1  1153 ? 23.324  72.845  77.515  1.00 20.15 ? 1151 TRP   B CB    1 
ATOM   17516 C  CG    . TRP   B  1  1153 ? 22.087  73.537  77.033  1.00 19.79 ? 1151 TRP   B CG    1 
ATOM   17517 C  CD1   . TRP   B  1  1153 ? 21.138  74.160  77.800  1.00 24.79 ? 1151 TRP   B CD1   1 
ATOM   17518 C  CD2   . TRP   B  1  1153 ? 21.652  73.658  75.679  1.00 20.41 ? 1151 TRP   B CD2   1 
ATOM   17519 N  NE1   . TRP   B  1  1153 ? 20.147  74.669  76.995  1.00 23.79 ? 1151 TRP   B NE1   1 
ATOM   17520 C  CE2   . TRP   B  1  1153 ? 20.435  74.371  75.689  1.00 20.68 ? 1151 TRP   B CE2   1 
ATOM   17521 C  CE3   . TRP   B  1  1153 ? 22.173  73.234  74.451  1.00 21.09 ? 1151 TRP   B CE3   1 
ATOM   17522 C  CZ2   . TRP   B  1  1153 ? 19.742  74.673  74.521  1.00 22.02 ? 1151 TRP   B CZ2   1 
ATOM   17523 C  CZ3   . TRP   B  1  1153 ? 21.484  73.536  73.300  1.00 20.47 ? 1151 TRP   B CZ3   1 
ATOM   17524 C  CH2   . TRP   B  1  1153 ? 20.275  74.243  73.342  1.00 22.52 ? 1151 TRP   B CH2   1 
ATOM   17525 N  N     . SER   B  1  1154 ? 24.720  69.792  77.188  1.00 17.07 ? 1152 SER   B N     1 
ATOM   17526 C  CA    . SER   B  1  1154 ? 25.893  68.951  77.369  1.00 17.93 ? 1152 SER   B CA    1 
ATOM   17527 C  C     . SER   B  1  1154 ? 26.950  69.294  76.338  1.00 17.73 ? 1152 SER   B C     1 
ATOM   17528 O  O     . SER   B  1  1154 ? 26.696  69.229  75.132  1.00 17.93 ? 1152 SER   B O     1 
ATOM   17529 C  CB    . SER   B  1  1154 ? 25.547  67.474  77.272  1.00 19.93 ? 1152 SER   B CB    1 
ATOM   17530 O  OG    . SER   B  1  1154 ? 26.749  66.735  77.352  1.00 17.88 ? 1152 SER   B OG    1 
ATOM   17531 N  N     . LYS   B  1  1155 ? 28.142  69.638  76.822  1.00 18.49 ? 1153 LYS   B N     1 
ATOM   17532 C  CA    . LYS   B  1  1155 ? 29.331  69.763  75.994  1.00 19.86 ? 1153 LYS   B CA    1 
ATOM   17533 C  C     . LYS   B  1  1155 ? 30.212  68.533  76.110  1.00 20.27 ? 1153 LYS   B C     1 
ATOM   17534 O  O     . LYS   B  1  1155 ? 31.350  68.541  75.630  1.00 21.40 ? 1153 LYS   B O     1 
ATOM   17535 C  CB    . LYS   B  1  1155 ? 30.120  71.011  76.395  1.00 23.93 ? 1153 LYS   B CB    1 
ATOM   17536 N  N     . ASP   B  1  1156 ? 29.728  67.492  76.772  1.00 16.68 ? 1154 ASP   B N     1 
ATOM   17537 C  CA    . ASP   B  1  1156 ? 30.528  66.295  77.000  1.00 16.98 ? 1154 ASP   B CA    1 
ATOM   17538 C  C     . ASP   B  1  1156 ? 29.523  65.167  77.245  1.00 17.46 ? 1154 ASP   B C     1 
ATOM   17539 O  O     . ASP   B  1  1156 ? 29.135  64.914  78.387  1.00 17.37 ? 1154 ASP   B O     1 
ATOM   17540 C  CB    . ASP   B  1  1156 ? 31.434  66.499  78.191  1.00 16.90 ? 1154 ASP   B CB    1 
ATOM   17541 C  CG    . ASP   B  1  1156 ? 32.437  65.391  78.354  1.00 17.78 ? 1154 ASP   B CG    1 
ATOM   17542 O  OD1   . ASP   B  1  1156 ? 32.142  64.241  77.967  1.00 16.58 ? 1154 ASP   B OD1   1 
ATOM   17543 O  OD2   . ASP   B  1  1156 ? 33.526  65.701  78.875  1.00 18.73 ? 1154 ASP   B OD2   1 
ATOM   17544 N  N     . TRP   B  1  1157 ? 29.123  64.500  76.164  1.00 14.27 ? 1155 TRP   B N     1 
ATOM   17545 C  CA    . TRP   B  1  1157 ? 28.042  63.523  76.283  1.00 14.62 ? 1155 TRP   B CA    1 
ATOM   17546 C  C     . TRP   B  1  1157 ? 28.434  62.390  77.212  1.00 18.31 ? 1155 TRP   B C     1 
ATOM   17547 O  O     . TRP   B  1  1157 ? 27.624  61.934  78.025  1.00 17.45 ? 1155 TRP   B O     1 
ATOM   17548 C  CB    . TRP   B  1  1157 ? 27.666  62.946  74.927  1.00 17.44 ? 1155 TRP   B CB    1 
ATOM   17549 C  CG    . TRP   B  1  1157 ? 27.236  63.930  73.915  1.00 15.75 ? 1155 TRP   B CG    1 
ATOM   17550 C  CD1   . TRP   B  1  1157 ? 26.990  65.263  74.095  1.00 16.35 ? 1155 TRP   B CD1   1 
ATOM   17551 C  CD2   . TRP   B  1  1157 ? 26.989  63.654  72.543  1.00 15.14 ? 1155 TRP   B CD2   1 
ATOM   17552 N  NE1   . TRP   B  1  1157 ? 26.621  65.835  72.904  1.00 16.53 ? 1155 TRP   B NE1   1 
ATOM   17553 C  CE2   . TRP   B  1  1157 ? 26.629  64.868  71.929  1.00 14.73 ? 1155 TRP   B CE2   1 
ATOM   17554 C  CE3   . TRP   B  1  1157 ? 27.068  62.495  71.760  1.00 16.22 ? 1155 TRP   B CE3   1 
ATOM   17555 C  CZ2   . TRP   B  1  1157 ? 26.314  64.953  70.579  1.00 16.93 ? 1155 TRP   B CZ2   1 
ATOM   17556 C  CZ3   . TRP   B  1  1157 ? 26.771  62.581  70.423  1.00 17.88 ? 1155 TRP   B CZ3   1 
ATOM   17557 C  CH2   . TRP   B  1  1157 ? 26.400  63.803  69.842  1.00 17.71 ? 1155 TRP   B CH2   1 
ATOM   17558 N  N     . ALA   B  1  1158 ? 29.677  61.924  77.105  1.00 16.25 ? 1156 ALA   B N     1 
ATOM   17559 C  CA    . ALA   B  1  1158 ? 30.091  60.764  77.879  1.00 16.27 ? 1156 ALA   B CA    1 
ATOM   17560 C  C     . ALA   B  1  1158 ? 30.171  61.085  79.358  1.00 17.93 ? 1156 ALA   B C     1 
ATOM   17561 O  O     . ALA   B  1  1158 ? 29.927  60.209  80.189  1.00 22.69 ? 1156 ALA   B O     1 
ATOM   17562 C  CB    . ALA   B  1  1158 ? 31.448  60.267  77.382  1.00 15.73 ? 1156 ALA   B CB    1 
ATOM   17563 N  N     . ALA   B  1  1159 ? 30.526  62.320  79.706  1.00 17.01 ? 1157 ALA   B N     1 
ATOM   17564 C  CA    . ALA   B  1  1159 ? 30.599  62.695  81.108  1.00 17.88 ? 1157 ALA   B CA    1 
ATOM   17565 C  C     . ALA   B  1  1159 ? 29.231  62.975  81.710  1.00 20.58 ? 1157 ALA   B C     1 
ATOM   17566 O  O     . ALA   B  1  1159 ? 29.073  62.853  82.926  1.00 21.88 ? 1157 ALA   B O     1 
ATOM   17567 C  CB    . ALA   B  1  1159 ? 31.490  63.922  81.286  1.00 19.56 ? 1157 ALA   B CB    1 
ATOM   17568 N  N     . ASP   B  1  1160 ? 28.245  63.330  80.890  1.00 19.83 ? 1158 ASP   B N     1 
ATOM   17569 C  CA    . ASP   B  1  1160 ? 26.965  63.818  81.381  1.00 20.73 ? 1158 ASP   B CA    1 
ATOM   17570 C  C     . ASP   B  1  1160 ? 25.892  62.744  81.399  1.00 20.00 ? 1158 ASP   B C     1 
ATOM   17571 O  O     . ASP   B  1  1160 ? 24.758  63.022  81.810  1.00 23.58 ? 1158 ASP   B O     1 
ATOM   17572 C  CB    . ASP   B  1  1160 ? 26.522  65.025  80.553  1.00 20.19 ? 1158 ASP   B CB    1 
ATOM   17573 C  CG    . ASP   B  1  1160 ? 27.434  66.220  80.748  1.00 20.68 ? 1158 ASP   B CG    1 
ATOM   17574 O  OD1   . ASP   B  1  1160 ? 28.218  66.223  81.731  1.00 25.41 ? 1158 ASP   B OD1   1 
ATOM   17575 O  OD2   . ASP   B  1  1160 ? 27.386  67.154  79.924  1.00 23.18 ? 1158 ASP   B OD2   1 
ATOM   17576 N  N     . GLY   B  1  1161 ? 26.211  61.539  80.953  1.00 18.39 ? 1159 GLY   B N     1 
ATOM   17577 C  CA    . GLY   B  1  1161 ? 25.308  60.425  81.055  1.00 22.04 ? 1159 GLY   B CA    1 
ATOM   17578 C  C     . GLY   B  1  1161 ? 25.296  59.839  82.455  1.00 23.74 ? 1159 GLY   B C     1 
ATOM   17579 O  O     . GLY   B  1  1161 ? 25.821  60.425  83.407  1.00 25.28 ? 1159 GLY   B O     1 
ATOM   17580 N  N     . PRO   B  1  1162 ? 24.706  58.654  82.606  1.00 25.36 ? 1160 PRO   B N     1 
ATOM   17581 C  CA    . PRO   B  1  1162 ? 24.117  57.828  81.557  1.00 21.24 ? 1160 PRO   B CA    1 
ATOM   17582 C  C     . PRO   B  1  1162 ? 22.794  58.396  81.093  1.00 21.00 ? 1160 PRO   B C     1 
ATOM   17583 O  O     . PRO   B  1  1162 ? 21.987  58.957  81.834  1.00 22.47 ? 1160 PRO   B O     1 
ATOM   17584 C  CB    . PRO   B  1  1162 ? 23.932  56.473  82.254  1.00 26.58 ? 1160 PRO   B CB    1 
ATOM   17585 C  CG    . PRO   B  1  1162 ? 23.643  56.845  83.677  1.00 28.30 ? 1160 PRO   B CG    1 
ATOM   17586 C  CD    . PRO   B  1  1162 ? 24.547  58.036  83.938  1.00 28.86 ? 1160 PRO   B CD    1 
ATOM   17587 N  N     . PHE   B  1  1163 ? 22.578  58.254  79.802  1.00 16.26 ? 1161 PHE   B N     1 
ATOM   17588 C  CA    . PHE   B  1  1163 ? 21.306  58.572  79.191  1.00 16.03 ? 1161 PHE   B CA    1 
ATOM   17589 C  C     . PHE   B  1  1163 ? 20.502  57.294  79.035  1.00 14.65 ? 1161 PHE   B C     1 
ATOM   17590 O  O     . PHE   B  1  1163 ? 20.977  56.193  79.302  1.00 16.06 ? 1161 PHE   B O     1 
ATOM   17591 C  CB    . PHE   B  1  1163 ? 21.544  59.283  77.859  1.00 17.18 ? 1161 PHE   B CB    1 
ATOM   17592 C  CG    . PHE   B  1  1163 ? 22.387  60.505  78.000  1.00 16.26 ? 1161 PHE   B CG    1 
ATOM   17593 C  CD1   . PHE   B  1  1163 ? 21.971  61.553  78.806  1.00 20.91 ? 1161 PHE   B CD1   1 
ATOM   17594 C  CD2   . PHE   B  1  1163 ? 23.613  60.598  77.368  1.00 18.28 ? 1161 PHE   B CD2   1 
ATOM   17595 C  CE1   . PHE   B  1  1163 ? 22.744  62.677  78.969  1.00 20.95 ? 1161 PHE   B CE1   1 
ATOM   17596 C  CE2   . PHE   B  1  1163 ? 24.390  61.728  77.514  1.00 18.67 ? 1161 PHE   B CE2   1 
ATOM   17597 C  CZ    . PHE   B  1  1163 ? 23.951  62.772  78.312  1.00 18.30 ? 1161 PHE   B CZ    1 
ATOM   17598 N  N     . ALA   B  1  1164 ? 19.244  57.456  78.637  1.00 16.86 ? 1162 ALA   B N     1 
ATOM   17599 C  CA    . ALA   B  1  1164 ? 18.363  56.312  78.445  1.00 17.24 ? 1162 ALA   B CA    1 
ATOM   17600 C  C     . ALA   B  1  1164 ? 17.794  56.271  77.038  1.00 17.57 ? 1162 ALA   B C     1 
ATOM   17601 O  O     . ALA   B  1  1164 ? 16.849  55.522  76.777  1.00 18.28 ? 1162 ALA   B O     1 
ATOM   17602 C  CB    . ALA   B  1  1164 ? 17.240  56.319  79.485  1.00 17.79 ? 1162 ALA   B CB    1 
ATOM   17603 N  N     . GLY   B  1  1165 ? 18.338  57.070  76.138  1.00 15.02 ? 1163 GLY   B N     1 
ATOM   17604 C  CA    . GLY   B  1  1165 ? 17.910  57.104  74.761  1.00 15.56 ? 1163 GLY   B CA    1 
ATOM   17605 C  C     . GLY   B  1  1165 ? 18.496  58.342  74.132  1.00 15.13 ? 1163 GLY   B C     1 
ATOM   17606 O  O     . GLY   B  1  1165 ? 19.102  59.174  74.803  1.00 14.76 ? 1163 GLY   B O     1 
ATOM   17607 N  N     . ALA   B  1  1166 ? 18.304  58.460  72.823  1.00 15.71 ? 1164 ALA   B N     1 
ATOM   17608 C  CA    . ALA   B  1  1166 ? 18.812  59.631  72.133  1.00 14.19 ? 1164 ALA   B CA    1 
ATOM   17609 C  C     . ALA   B  1  1166 ? 17.923  59.947  70.953  1.00 15.33 ? 1164 ALA   B C     1 
ATOM   17610 O  O     . ALA   B  1  1166 ? 17.442  59.043  70.271  1.00 16.89 ? 1164 ALA   B O     1 
ATOM   17611 C  CB    . ALA   B  1  1166 ? 20.242  59.403  71.640  1.00 16.09 ? 1164 ALA   B CB    1 
ATOM   17612 N  N     . LEU   B  1  1167 ? 17.720  61.235  70.711  1.00 14.13 ? 1165 LEU   B N     1 
ATOM   17613 C  CA    . LEU   B  1  1167 ? 17.018  61.699  69.526  1.00 14.06 ? 1165 LEU   B CA    1 
ATOM   17614 C  C     . LEU   B  1  1167 ? 17.996  62.530  68.726  1.00 17.02 ? 1165 LEU   B C     1 
ATOM   17615 O  O     . LEU   B  1  1167 ? 18.659  63.409  69.280  1.00 16.56 ? 1165 LEU   B O     1 
ATOM   17616 C  CB    . LEU   B  1  1167 ? 15.808  62.551  69.897  1.00 15.14 ? 1165 LEU   B CB    1 
ATOM   17617 C  CG    . LEU   B  1  1167 ? 14.812  61.861  70.828  1.00 14.03 ? 1165 LEU   B CG    1 
ATOM   17618 C  CD1   . LEU   B  1  1167 ? 13.676  62.799  71.167  1.00 16.91 ? 1165 LEU   B CD1   1 
ATOM   17619 C  CD2   . LEU   B  1  1167 ? 14.266  60.598  70.155  1.00 18.08 ? 1165 LEU   B CD2   1 
ATOM   17620 N  N     . VAL   B  1  1168 ? 18.095  62.236  67.437  1.00 15.82 ? 1166 VAL   B N     1 
ATOM   17621 C  CA    . VAL   B  1  1168 ? 19.105  62.837  66.583  1.00 16.83 ? 1166 VAL   B CA    1 
ATOM   17622 C  C     . VAL   B  1  1168 ? 18.407  63.435  65.375  1.00 16.91 ? 1166 VAL   B C     1 
ATOM   17623 O  O     . VAL   B  1  1168 ? 17.516  62.807  64.793  1.00 17.12 ? 1166 VAL   B O     1 
ATOM   17624 C  CB    . VAL   B  1  1168 ? 20.146  61.794  66.141  1.00 16.81 ? 1166 VAL   B CB    1 
ATOM   17625 C  CG1   . VAL   B  1  1168 ? 21.204  62.444  65.245  1.00 17.08 ? 1166 VAL   B CG1   1 
ATOM   17626 C  CG2   . VAL   B  1  1168 ? 20.783  61.118  67.360  1.00 16.13 ? 1166 VAL   B CG2   1 
ATOM   17627 N  N     . GLU   B  1  1169 ? 18.794  64.649  65.016  1.00 16.37 ? 1167 GLU   B N     1 
ATOM   17628 C  CA    . GLU   B  1  1169 ? 18.329  65.300  63.804  1.00 17.24 ? 1167 GLU   B CA    1 
ATOM   17629 C  C     . GLU   B  1  1169 ? 19.536  65.575  62.921  1.00 19.07 ? 1167 GLU   B C     1 
ATOM   17630 O  O     . GLU   B  1  1169 ? 20.551  66.077  63.404  1.00 19.18 ? 1167 GLU   B O     1 
ATOM   17631 C  CB    . GLU   B  1  1169 ? 17.654  66.626  64.142  1.00 17.07 ? 1167 GLU   B CB    1 
ATOM   17632 C  CG    . GLU   B  1  1169 ? 17.187  67.406  62.935  1.00 17.86 ? 1167 GLU   B CG    1 
ATOM   17633 C  CD    . GLU   B  1  1169 ? 16.793  68.826  63.281  1.00 20.19 ? 1167 GLU   B CD    1 
ATOM   17634 O  OE1   . GLU   B  1  1169 ? 17.031  69.259  64.426  1.00 19.75 ? 1167 GLU   B OE1   1 
ATOM   17635 O  OE2   . GLU   B  1  1169 ? 16.228  69.511  62.406  1.00 21.58 ? 1167 GLU   B OE2   1 
ATOM   17636 N  N     . GLY   B  1  1170 ? 19.430  65.244  61.646  1.00 18.44 ? 1168 GLY   B N     1 
ATOM   17637 C  CA    . GLY   B  1  1170 ? 20.497  65.564  60.721  1.00 19.69 ? 1168 GLY   B CA    1 
ATOM   17638 C  C     . GLY   B  1  1170 ? 20.347  64.795  59.430  1.00 23.71 ? 1168 GLY   B C     1 
ATOM   17639 O  O     . GLY   B  1  1170 ? 19.460  63.959  59.276  1.00 21.06 ? 1168 GLY   B O     1 
ATOM   17640 N  N     . ASP   B  1  1171 ? 21.243  65.108  58.495  1.00 23.10 ? 1169 ASP   B N     1 
ATOM   17641 C  CA    . ASP   B  1  1171 ? 21.296  64.340  57.263  1.00 23.15 ? 1169 ASP   B CA    1 
ATOM   17642 C  C     . ASP   B  1  1171 ? 21.976  62.999  57.523  1.00 21.27 ? 1169 ASP   B C     1 
ATOM   17643 O  O     . ASP   B  1  1171 ? 22.443  62.715  58.631  1.00 20.95 ? 1169 ASP   B O     1 
ATOM   17644 C  CB    . ASP   B  1  1171 ? 21.921  65.145  56.118  1.00 23.22 ? 1169 ASP   B CB    1 
ATOM   17645 C  CG    . ASP   B  1  1171 ? 23.386  65.495  56.345  1.00 25.90 ? 1169 ASP   B CG    1 
ATOM   17646 O  OD1   . ASP   B  1  1171 ? 24.019  65.025  57.319  1.00 24.93 ? 1169 ASP   B OD1   1 
ATOM   17647 O  OD2   . ASP   B  1  1171 ? 23.918  66.267  55.516  1.00 32.95 ? 1169 ASP   B OD2   1 
ATOM   17648 N  N     . ALA   B  1  1172 ? 22.022  62.155  56.492  1.00 22.76 ? 1170 ALA   B N     1 
ATOM   17649 C  CA    . ALA   B  1  1172 ? 22.538  60.802  56.672  1.00 23.67 ? 1170 ALA   B CA    1 
ATOM   17650 C  C     . ALA   B  1  1172 ? 23.933  60.809  57.285  1.00 22.37 ? 1170 ALA   B C     1 
ATOM   17651 O  O     . ALA   B  1  1172 ? 24.212  60.062  58.229  1.00 23.36 ? 1170 ALA   B O     1 
ATOM   17652 C  CB    . ALA   B  1  1172 ? 22.535  60.048  55.341  1.00 24.41 ? 1170 ALA   B CB    1 
ATOM   17653 N  N     . GLU   B  1  1173 ? 24.832  61.655  56.772  1.00 22.22 ? 1171 GLU   B N     1 
ATOM   17654 C  CA    . GLU   B  1  1173 ? 26.190  61.612  57.303  1.00 23.85 ? 1171 GLU   B CA    1 
ATOM   17655 C  C     . GLU   B  1  1173 ? 26.270  62.153  58.727  1.00 22.18 ? 1171 GLU   B C     1 
ATOM   17656 O  O     . GLU   B  1  1173 ? 27.076  61.664  59.525  1.00 21.96 ? 1171 GLU   B O     1 
ATOM   17657 C  CB    . GLU   B  1  1173 ? 27.180  62.283  56.352  1.00 31.19 ? 1171 GLU   B CB    1 
ATOM   17658 C  CG    . GLU   B  1  1173 ? 27.472  61.435  55.108  1.00 37.46 ? 1171 GLU   B CG    1 
ATOM   17659 C  CD    . GLU   B  1  1173 ? 27.768  59.962  55.425  1.00 37.17 ? 1171 GLU   B CD    1 
ATOM   17660 O  OE1   . GLU   B  1  1173 ? 28.598  59.677  56.316  1.00 36.85 ? 1171 GLU   B OE1   1 
ATOM   17661 O  OE2   . GLU   B  1  1173 ? 27.163  59.080  54.776  1.00 41.21 ? 1171 GLU   B OE2   1 
ATOM   17662 N  N     . ARG   B  1  1174 ? 25.437  63.138  59.068  1.00 21.18 ? 1172 ARG   B N     1 
ATOM   17663 C  CA    . ARG   B  1  1174 ? 25.372  63.600  60.452  1.00 20.82 ? 1172 ARG   B CA    1 
ATOM   17664 C  C     . ARG   B  1  1174 ? 24.860  62.489  61.358  1.00 18.05 ? 1172 ARG   B C     1 
ATOM   17665 O  O     . ARG   B  1  1174 ? 25.423  62.227  62.424  1.00 19.81 ? 1172 ARG   B O     1 
ATOM   17666 C  CB    . ARG   B  1  1174 ? 24.458  64.822  60.528  1.00 21.48 ? 1172 ARG   B CB    1 
ATOM   17667 C  CG    . ARG   B  1  1174 ? 24.203  65.329  61.936  1.00 21.55 ? 1172 ARG   B CG    1 
ATOM   17668 C  CD    . ARG   B  1  1174 ? 25.491  65.762  62.600  1.00 23.81 ? 1172 ARG   B CD    1 
ATOM   17669 N  NE    . ARG   B  1  1174 ? 25.245  66.285  63.937  1.00 23.00 ? 1172 ARG   B NE    1 
ATOM   17670 C  CZ    . ARG   B  1  1174 ? 26.165  66.374  64.886  1.00 20.91 ? 1172 ARG   B CZ    1 
ATOM   17671 N  NH1   . ARG   B  1  1174 ? 27.421  66.011  64.669  1.00 23.14 ? 1172 ARG   B NH1   1 
ATOM   17672 N  NH2   . ARG   B  1  1174 ? 25.820  66.841  66.083  1.00 23.11 ? 1172 ARG   B NH2   1 
ATOM   17673 N  N     . ILE   B  1  1175 ? 23.798  61.816  60.925  1.00 17.97 ? 1173 ILE   B N     1 
ATOM   17674 C  CA    . ILE   B  1  1175 ? 23.248  60.708  61.698  1.00 18.29 ? 1173 ILE   B CA    1 
ATOM   17675 C  C     . ILE   B  1  1175 ? 24.309  59.643  61.934  1.00 17.80 ? 1173 ILE   B C     1 
ATOM   17676 O  O     . ILE   B  1  1175 ? 24.483  59.154  63.056  1.00 17.85 ? 1173 ILE   B O     1 
ATOM   17677 C  CB    . ILE   B  1  1175 ? 22.001  60.142  61.000  1.00 18.14 ? 1173 ILE   B CB    1 
ATOM   17678 C  CG1   . ILE   B  1  1175 ? 20.847  61.144  61.091  1.00 19.20 ? 1173 ILE   B CG1   1 
ATOM   17679 C  CG2   . ILE   B  1  1175 ? 21.618  58.808  61.605  1.00 17.92 ? 1173 ILE   B CG2   1 
ATOM   17680 C  CD1   . ILE   B  1  1175 ? 19.694  60.818  60.183  1.00 20.59 ? 1173 ILE   B CD1   1 
ATOM   17681 N  N     . ARG   B  1  1176 ? 25.033  59.256  60.879  1.00 19.55 ? 1174 ARG   B N     1 
ATOM   17682 C  CA    . ARG   B  1  1176 ? 26.060  58.230  61.040  1.00 18.83 ? 1174 ARG   B CA    1 
ATOM   17683 C  C     . ARG   B  1  1176 ? 27.112  58.666  62.051  1.00 18.91 ? 1174 ARG   B C     1 
ATOM   17684 O  O     . ARG   B  1  1176 ? 27.510  57.895  62.924  1.00 18.72 ? 1174 ARG   B O     1 
ATOM   17685 C  CB    . ARG   B  1  1176 ? 26.724  57.930  59.695  1.00 21.20 ? 1174 ARG   B CB    1 
ATOM   17686 C  CG    . ARG   B  1  1176 ? 27.620  56.705  59.733  1.00 25.11 ? 1174 ARG   B CG    1 
ATOM   17687 C  CD    . ARG   B  1  1176 ? 28.559  56.607  58.518  1.00 28.06 ? 1174 ARG   B CD    1 
ATOM   17688 N  NE    . ARG   B  1  1176 ? 27.876  56.776  57.240  1.00 28.53 ? 1174 ARG   B NE    1 
ATOM   17689 C  CZ    . ARG   B  1  1176 ? 27.375  55.785  56.512  1.00 31.63 ? 1174 ARG   B CZ    1 
ATOM   17690 N  NH1   . ARG   B  1  1176 ? 27.414  54.531  56.930  1.00 32.59 ? 1174 ARG   B NH1   1 
ATOM   17691 N  NH2   . ARG   B  1  1176 ? 26.838  56.059  55.325  1.00 32.26 ? 1174 ARG   B NH2   1 
ATOM   17692 N  N     . ALA   B  1  1177 ? 27.579  59.912  61.940  1.00 19.17 ? 1175 ALA   B N     1 
ATOM   17693 C  CA    . ALA   B  1  1177 ? 28.608  60.396  62.851  1.00 19.54 ? 1175 ALA   B CA    1 
ATOM   17694 C  C     . ALA   B  1  1177 ? 28.108  60.426  64.290  1.00 17.64 ? 1175 ALA   B C     1 
ATOM   17695 O  O     . ALA   B  1  1177 ? 28.830  60.050  65.220  1.00 18.61 ? 1175 ALA   B O     1 
ATOM   17696 C  CB    . ALA   B  1  1177 ? 29.050  61.793  62.422  1.00 20.32 ? 1175 ALA   B CB    1 
ATOM   17697 N  N     . VAL   B  1  1178 ? 26.873  60.877  64.489  1.00 18.81 ? 1176 VAL   B N     1 
ATOM   17698 C  CA    . VAL   B  1  1178 ? 26.325  60.936  65.839  1.00 17.29 ? 1176 VAL   B CA    1 
ATOM   17699 C  C     . VAL   B  1  1178 ? 26.116  59.532  66.376  1.00 16.79 ? 1176 VAL   B C     1 
ATOM   17700 O  O     . VAL   B  1  1178 ? 26.408  59.239  67.540  1.00 18.33 ? 1176 VAL   B O     1 
ATOM   17701 C  CB    . VAL   B  1  1178 ? 25.024  61.754  65.831  1.00 19.75 ? 1176 VAL   B CB    1 
ATOM   17702 C  CG1   . VAL   B  1  1178 ? 24.316  61.653  67.168  1.00 19.04 ? 1176 VAL   B CG1   1 
ATOM   17703 C  CG2   . VAL   B  1  1178 ? 25.317  63.203  65.504  1.00 19.49 ? 1176 VAL   B CG2   1 
ATOM   17704 N  N     . ASN   B  1  1179 ? 25.628  58.636  65.527  1.00 17.31 ? 1177 ASN   B N     1 
ATOM   17705 C  CA    . ASN   B  1  1179 ? 25.402  57.265  65.957  1.00 18.71 ? 1177 ASN   B CA    1 
ATOM   17706 C  C     . ASN   B  1  1179 ? 26.707  56.605  66.374  1.00 17.41 ? 1177 ASN   B C     1 
ATOM   17707 O  O     . ASN   B  1  1179 ? 26.766  55.899  67.389  1.00 18.62 ? 1177 ASN   B O     1 
ATOM   17708 C  CB    . ASN   B  1  1179 ? 24.734  56.497  64.820  1.00 17.68 ? 1177 ASN   B CB    1 
ATOM   17709 C  CG    . ASN   B  1  1179 ? 24.013  55.263  65.295  1.00 20.82 ? 1177 ASN   B CG    1 
ATOM   17710 O  OD1   . ASN   B  1  1179 ? 23.570  55.185  66.441  1.00 21.83 ? 1177 ASN   B OD1   1 
ATOM   17711 N  ND2   . ASN   B  1  1179 ? 23.866  54.294  64.402  1.00 19.80 ? 1177 ASN   B ND2   1 
ATOM   17712 N  N     . LYS   B  1  1180 ? 27.783  56.856  65.624  1.00 18.35 ? 1178 LYS   B N     1 
ATOM   17713 C  CA    . LYS   B  1  1180 ? 29.083  56.331  66.020  1.00 18.79 ? 1178 LYS   B CA    1 
ATOM   17714 C  C     . LYS   B  1  1180 ? 29.513  56.889  67.366  1.00 16.54 ? 1178 LYS   B C     1 
ATOM   17715 O  O     . LYS   B  1  1180 ? 30.028  56.152  68.214  1.00 19.55 ? 1178 LYS   B O     1 
ATOM   17716 C  CB    . LYS   B  1  1180 ? 30.133  56.655  64.956  1.00 20.89 ? 1178 LYS   B CB    1 
ATOM   17717 C  CG    . LYS   B  1  1180 ? 29.950  55.905  63.657  1.00 26.56 ? 1178 LYS   B CG    1 
ATOM   17718 C  CD    . LYS   B  1  1180 ? 31.132  56.130  62.707  1.00 30.41 ? 1178 LYS   B CD    1 
ATOM   17719 C  CE    . LYS   B  1  1180 ? 32.311  55.248  63.076  1.00 39.88 ? 1178 LYS   B CE    1 
ATOM   17720 N  NZ    . LYS   B  1  1180 ? 31.986  53.799  62.894  1.00 39.64 ? 1178 LYS   B NZ    1 
ATOM   17721 N  N     . ALA   B  1  1181 ? 29.320  58.197  67.577  1.00 17.98 ? 1179 ALA   B N     1 
ATOM   17722 C  CA    . ALA   B  1  1181 ? 29.696  58.793  68.855  1.00 17.85 ? 1179 ALA   B CA    1 
ATOM   17723 C  C     . ALA   B  1  1181 ? 28.864  58.213  69.986  1.00 17.37 ? 1179 ALA   B C     1 
ATOM   17724 O  O     . ALA   B  1  1181 ? 29.380  57.945  71.073  1.00 18.61 ? 1179 ALA   B O     1 
ATOM   17725 C  CB    . ALA   B  1  1181 ? 29.528  60.311  68.795  1.00 17.60 ? 1179 ALA   B CB    1 
ATOM   17726 N  N     . ILE   B  1  1182 ? 27.571  58.004  69.742  1.00 16.78 ? 1180 ILE   B N     1 
ATOM   17727 C  CA    . ILE   B  1  1182 ? 26.725  57.427  70.777  1.00 18.01 ? 1180 ILE   B CA    1 
ATOM   17728 C  C     . ILE   B  1  1182 ? 27.152  56.002  71.093  1.00 17.11 ? 1180 ILE   B C     1 
ATOM   17729 O  O     . ILE   B  1  1182 ? 27.183  55.594  72.257  1.00 18.25 ? 1180 ILE   B O     1 
ATOM   17730 C  CB    . ILE   B  1  1182 ? 25.251  57.507  70.357  1.00 18.33 ? 1180 ILE   B CB    1 
ATOM   17731 C  CG1   . ILE   B  1  1182 ? 24.789  58.954  70.417  1.00 18.18 ? 1180 ILE   B CG1   1 
ATOM   17732 C  CG2   . ILE   B  1  1182 ? 24.396  56.611  71.247  1.00 20.33 ? 1180 ILE   B CG2   1 
ATOM   17733 C  CD1   . ILE   B  1  1182 ? 23.410  59.179  69.826  1.00 17.87 ? 1180 ILE   B CD1   1 
ATOM   17734 N  N     . ALA   B  1  1183 ? 27.490  55.215  70.064  1.00 19.08 ? 1181 ALA   B N     1 
ATOM   17735 C  CA    . ALA   B  1  1183 ? 27.918  53.845  70.324  1.00 20.53 ? 1181 ALA   B CA    1 
ATOM   17736 C  C     . ALA   B  1  1183 ? 29.175  53.795  71.174  1.00 20.48 ? 1181 ALA   B C     1 
ATOM   17737 O  O     . ALA   B  1  1183 ? 29.407  52.808  71.881  1.00 23.51 ? 1181 ALA   B O     1 
ATOM   17738 C  CB    . ALA   B  1  1183 ? 28.124  53.079  69.017  1.00 20.36 ? 1181 ALA   B CB    1 
ATOM   17739 N  N     . ALA   B  1  1184 ? 29.995  54.844  71.129  1.00 18.96 ? 1182 ALA   B N     1 
ATOM   17740 C  CA    . ALA   B  1  1184 ? 31.207  54.904  71.929  1.00 21.83 ? 1182 ALA   B CA    1 
ATOM   17741 C  C     . ALA   B  1  1184 ? 30.978  55.438  73.337  1.00 20.41 ? 1182 ALA   B C     1 
ATOM   17742 O  O     . ALA   B  1  1184 ? 31.934  55.527  74.110  1.00 21.31 ? 1182 ALA   B O     1 
ATOM   17743 C  CB    . ALA   B  1  1184 ? 32.279  55.743  71.219  1.00 22.90 ? 1182 ALA   B CB    1 
ATOM   17744 N  N     . LEU   B  1  1185 ? 29.752  55.814  73.695  1.00 18.46 ? 1183 LEU   B N     1 
ATOM   17745 C  CA    . LEU   B  1  1185 ? 29.537  56.307  75.045  1.00 17.46 ? 1183 LEU   B CA    1 
ATOM   17746 C  C     . LEU   B  1  1185 ? 29.638  55.151  76.036  1.00 19.76 ? 1183 LEU   B C     1 
ATOM   17747 O  O     . LEU   B  1  1185 ? 29.204  54.032  75.739  1.00 22.11 ? 1183 LEU   B O     1 
ATOM   17748 C  CB    . LEU   B  1  1185 ? 28.164  56.958  75.176  1.00 17.12 ? 1183 LEU   B CB    1 
ATOM   17749 C  CG    . LEU   B  1  1185 ? 27.941  58.189  74.307  1.00 18.38 ? 1183 LEU   B CG    1 
ATOM   17750 C  CD1   . LEU   B  1  1185 ? 26.498  58.629  74.431  1.00 17.84 ? 1183 LEU   B CD1   1 
ATOM   17751 C  CD2   . LEU   B  1  1185 ? 28.907  59.309  74.696  1.00 18.89 ? 1183 LEU   B CD2   1 
ATOM   17752 N  N     . PRO   B  1  1186 ? 30.205  55.384  77.210  1.00 20.57 ? 1184 PRO   B N     1 
ATOM   17753 C  CA    . PRO   B  1  1186 ? 30.226  54.341  78.233  1.00 20.69 ? 1184 PRO   B CA    1 
ATOM   17754 C  C     . PRO   B  1  1186 ? 28.833  54.150  78.805  1.00 18.71 ? 1184 PRO   B C     1 
ATOM   17755 O  O     . PRO   B  1  1186 ? 27.944  54.986  78.652  1.00 22.44 ? 1184 PRO   B O     1 
ATOM   17756 C  CB    . PRO   B  1  1186 ? 31.169  54.915  79.293  1.00 26.18 ? 1184 PRO   B CB    1 
ATOM   17757 C  CG    . PRO   B  1  1186 ? 30.982  56.395  79.168  1.00 26.66 ? 1184 PRO   B CG    1 
ATOM   17758 C  CD    . PRO   B  1  1186 ? 30.738  56.665  77.705  1.00 23.40 ? 1184 PRO   B CD    1 
ATOM   17759 N  N     . GLY   B  1  1187 ? 28.661  53.020  79.475  1.00 19.98 ? 1185 GLY   B N     1 
ATOM   17760 C  CA    . GLY   B  1  1187 ? 27.428  52.739  80.162  1.00 18.61 ? 1185 GLY   B CA    1 
ATOM   17761 C  C     . GLY   B  1  1187 ? 26.415  52.048  79.280  1.00 18.84 ? 1185 GLY   B C     1 
ATOM   17762 O  O     . GLY   B  1  1187 ? 26.742  51.203  78.448  1.00 21.49 ? 1185 GLY   B O     1 
ATOM   17763 N  N     . PRO   B  1  1188 ? 25.151  52.386  79.471  1.00 16.41 ? 1186 PRO   B N     1 
ATOM   17764 C  CA    . PRO   B  1  1188 ? 24.087  51.682  78.750  1.00 17.54 ? 1186 PRO   B CA    1 
ATOM   17765 C  C     . PRO   B  1  1188 ? 24.167  51.897  77.247  1.00 18.55 ? 1186 PRO   B C     1 
ATOM   17766 O  O     . PRO   B  1  1188 ? 24.608  52.939  76.757  1.00 18.30 ? 1186 PRO   B O     1 
ATOM   17767 C  CB    . PRO   B  1  1188 ? 22.801  52.290  79.318  1.00 21.19 ? 1186 PRO   B CB    1 
ATOM   17768 C  CG    . PRO   B  1  1188 ? 23.214  53.605  79.884  1.00 25.30 ? 1186 PRO   B CG    1 
ATOM   17769 C  CD    . PRO   B  1  1188 ? 24.645  53.467  80.328  1.00 18.42 ? 1186 PRO   B CD    1 
ATOM   17770 N  N     . LEU   B  1  1189 ? 23.739  50.881  76.512  1.00 15.74 ? 1187 LEU   B N     1 
ATOM   17771 C  CA    . LEU   B  1  1189 ? 23.551  51.024  75.076  1.00 15.05 ? 1187 LEU   B CA    1 
ATOM   17772 C  C     . LEU   B  1  1189 ? 22.309  51.856  74.827  1.00 15.99 ? 1187 LEU   B C     1 
ATOM   17773 O  O     . LEU   B  1  1189 ? 21.215  51.480  75.258  1.00 18.47 ? 1187 LEU   B O     1 
ATOM   17774 C  CB    . LEU   B  1  1189 ? 23.364  49.654  74.438  1.00 17.08 ? 1187 LEU   B CB    1 
ATOM   17775 C  CG    . LEU   B  1  1189 ? 24.632  48.858  74.158  1.00 18.70 ? 1187 LEU   B CG    1 
ATOM   17776 C  CD1   . LEU   B  1  1189 ? 25.178  48.231  75.432  1.00 26.10 ? 1187 LEU   B CD1   1 
ATOM   17777 C  CD2   . LEU   B  1  1189 ? 24.322  47.805  73.109  1.00 20.59 ? 1187 LEU   B CD2   1 
ATOM   17778 N  N     . LEU   B  1  1190 ? 22.453  52.979  74.134  1.00 15.37 ? 1188 LEU   B N     1 
ATOM   17779 C  CA    . LEU   B  1  1190 ? 21.327  53.887  73.976  1.00 16.72 ? 1188 LEU   B CA    1 
ATOM   17780 C  C     . LEU   B  1  1190 ? 20.466  53.496  72.789  1.00 16.57 ? 1188 LEU   B C     1 
ATOM   17781 O  O     . LEU   B  1  1190 ? 20.970  53.189  71.704  1.00 16.72 ? 1188 LEU   B O     1 
ATOM   17782 C  CB    . LEU   B  1  1190 ? 21.790  55.328  73.790  1.00 15.37 ? 1188 LEU   B CB    1 
ATOM   17783 C  CG    . LEU   B  1  1190 ? 22.642  55.910  74.906  1.00 15.42 ? 1188 LEU   B CG    1 
ATOM   17784 C  CD1   . LEU   B  1  1190 ? 22.716  57.409  74.672  1.00 16.54 ? 1188 LEU   B CD1   1 
ATOM   17785 C  CD2   . LEU   B  1  1190 ? 22.045  55.591  76.271  1.00 17.90 ? 1188 LEU   B CD2   1 
ATOM   17786 N  N     . LEU   B  1  1191 ? 19.160  53.524  73.006  1.00 16.36 ? 1189 LEU   B N     1 
ATOM   17787 C  CA    . LEU   B  1  1191 ? 18.203  53.400  71.913  1.00 15.21 ? 1189 LEU   B CA    1 
ATOM   17788 C  C     . LEU   B  1  1191 ? 18.130  54.743  71.186  1.00 15.37 ? 1189 LEU   B C     1 
ATOM   17789 O  O     . LEU   B  1  1191 ? 17.602  55.727  71.719  1.00 17.46 ? 1189 LEU   B O     1 
ATOM   17790 C  CB    . LEU   B  1  1191 ? 16.845  52.963  72.454  1.00 15.57 ? 1189 LEU   B CB    1 
ATOM   17791 C  CG    . LEU   B  1  1191 ? 15.899  52.316  71.440  1.00 15.84 ? 1189 LEU   B CG    1 
ATOM   17792 C  CD1   . LEU   B  1  1191 ? 14.749  51.669  72.190  1.00 16.47 ? 1189 LEU   B CD1   1 
ATOM   17793 C  CD2   . LEU   B  1  1191 ? 15.363  53.332  70.436  1.00 15.37 ? 1189 LEU   B CD2   1 
ATOM   17794 N  N     . VAL   B  1  1192 ? 18.664  54.775  69.970  1.00 15.66 ? 1190 VAL   B N     1 
ATOM   17795 C  CA    . VAL   B  1  1192 ? 18.816  55.996  69.188  1.00 16.59 ? 1190 VAL   B CA    1 
ATOM   17796 C  C     . VAL   B  1  1192 ? 17.697  56.072  68.165  1.00 16.62 ? 1190 VAL   B C     1 
ATOM   17797 O  O     . VAL   B  1  1192 ? 17.419  55.095  67.456  1.00 17.51 ? 1190 VAL   B O     1 
ATOM   17798 C  CB    . VAL   B  1  1192 ? 20.177  56.017  68.472  1.00 16.00 ? 1190 VAL   B CB    1 
ATOM   17799 C  CG1   . VAL   B  1  1192 ? 20.331  57.263  67.597  1.00 16.63 ? 1190 VAL   B CG1   1 
ATOM   17800 C  CG2   . VAL   B  1  1192 ? 21.331  55.919  69.475  1.00 17.75 ? 1190 VAL   B CG2   1 
ATOM   17801 N  N     . GLN   B  1  1193 ? 17.093  57.245  68.056  1.00 15.30 ? 1191 GLN   B N     1 
ATOM   17802 C  CA    . GLN   B  1  1193 ? 16.144  57.544  67.000  1.00 14.15 ? 1191 GLN   B CA    1 
ATOM   17803 C  C     . GLN   B  1  1193 ? 16.659  58.743  66.229  1.00 16.01 ? 1191 GLN   B C     1 
ATOM   17804 O  O     . GLN   B  1  1193 ? 17.015  59.766  66.826  1.00 16.73 ? 1191 GLN   B O     1 
ATOM   17805 C  CB    . GLN   B  1  1193 ? 14.789  57.886  67.598  1.00 16.20 ? 1191 GLN   B CB    1 
ATOM   17806 C  CG    . GLN   B  1  1193 ? 14.261  56.821  68.510  1.00 16.92 ? 1191 GLN   B CG    1 
ATOM   17807 C  CD    . GLN   B  1  1193 ? 12.795  57.012  68.744  1.00 17.72 ? 1191 GLN   B CD    1 
ATOM   17808 O  OE1   . GLN   B  1  1193 ? 11.997  56.932  67.817  1.00 17.86 ? 1191 GLN   B OE1   1 
ATOM   17809 N  NE2   . GLN   B  1  1193 ? 12.431  57.291  69.981  1.00 16.59 ? 1191 GLN   B NE2   1 
ATOM   17810 N  N     . ALA   B  1  1194 ? 16.686  58.620  64.909  1.00 16.74 ? 1192 ALA   B N     1 
ATOM   17811 C  CA    . ALA   B  1  1194 ? 17.225  59.667  64.063  1.00 17.00 ? 1192 ALA   B CA    1 
ATOM   17812 C  C     . ALA   B  1  1194 ? 16.208  60.040  63.004  1.00 18.70 ? 1192 ALA   B C     1 
ATOM   17813 O  O     . ALA   B  1  1194 ? 15.409  59.211  62.556  1.00 20.52 ? 1192 ALA   B O     1 
ATOM   17814 C  CB    . ALA   B  1  1194 ? 18.519  59.222  63.393  1.00 18.73 ? 1192 ALA   B CB    1 
ATOM   17815 N  N     . ALA   B  1  1195 ? 16.240  61.306  62.619  1.00 18.28 ? 1193 ALA   B N     1 
ATOM   17816 C  CA    . ALA   B  1  1195 ? 15.378  61.787  61.558  1.00 18.34 ? 1193 ALA   B CA    1 
ATOM   17817 C  C     . ALA   B  1  1195 ? 16.060  62.989  60.939  1.00 21.04 ? 1193 ALA   B C     1 
ATOM   17818 O  O     . ALA   B  1  1195 ? 16.845  63.676  61.592  1.00 19.86 ? 1193 ALA   B O     1 
ATOM   17819 C  CB    . ALA   B  1  1195 ? 14.010  62.206  62.104  1.00 19.90 ? 1193 ALA   B CB    1 
ATOM   17820 N  N     . SER   B  1  1196 ? 15.778  63.219  59.666  1.00 20.20 ? 1194 SER   B N     1 
ATOM   17821 C  CA    . SER   B  1  1196 ? 16.216  64.452  59.042  1.00 20.45 ? 1194 SER   B CA    1 
ATOM   17822 C  C     . SER   B  1  1196 ? 15.275  65.586  59.425  1.00 21.14 ? 1194 SER   B C     1 
ATOM   17823 O  O     . SER   B  1  1196 ? 14.149  65.370  59.888  1.00 21.82 ? 1194 SER   B O     1 
ATOM   17824 C  CB    . SER   B  1  1196 ? 16.177  64.300  57.527  1.00 23.54 ? 1194 SER   B CB    1 
ATOM   17825 O  OG    . SER   B  1  1196 ? 14.842  64.081  57.121  1.00 25.09 ? 1194 SER   B OG    1 
ATOM   17826 N  N     . SER   B  1  1197 ? 15.748  66.816  59.213  1.00 22.08 ? 1195 SER   B N     1 
ATOM   17827 C  CA    . SER   B  1  1197 ? 14.885  67.974  59.415  1.00 21.95 ? 1195 SER   B CA    1 
ATOM   17828 C  C     . SER   B  1  1197 ? 13.622  67.874  58.574  1.00 21.97 ? 1195 SER   B C     1 
ATOM   17829 O  O     . SER   B  1  1197 ? 12.527  68.196  59.046  1.00 23.37 ? 1195 SER   B O     1 
ATOM   17830 C  CB    . SER   B  1  1197 ? 15.640  69.253  59.074  1.00 23.95 ? 1195 SER   B CB    1 
ATOM   17831 O  OG    . SER   B  1  1197 ? 16.806  69.367  59.861  1.00 24.55 ? 1195 SER   B OG    1 
ATOM   17832 N  N     . GLY   B  1  1198 ? 13.755  67.437  57.321  1.00 23.67 ? 1196 GLY   B N     1 
ATOM   17833 C  CA    . GLY   B  1  1198 ? 12.579  67.293  56.481  1.00 27.18 ? 1196 GLY   B CA    1 
ATOM   17834 C  C     . GLY   B  1  1198 ? 11.620  66.249  57.015  1.00 28.59 ? 1196 GLY   B C     1 
ATOM   17835 O  O     . GLY   B  1  1198 ? 10.401  66.427  56.966  1.00 26.57 ? 1196 GLY   B O     1 
ATOM   17836 N  N     . GLU   B  1  1199 ? 12.164  65.159  57.559  1.00 23.59 ? 1197 GLU   B N     1 
ATOM   17837 C  CA    . GLU   B  1  1199 ? 11.330  64.106  58.123  1.00 26.73 ? 1197 GLU   B CA    1 
ATOM   17838 C  C     . GLU   B  1  1199 ? 10.563  64.612  59.338  1.00 27.55 ? 1197 GLU   B C     1 
ATOM   17839 O  O     . GLU   B  1  1199 ? 9.374   64.316  59.502  1.00 25.15 ? 1197 GLU   B O     1 
ATOM   17840 C  CB    . GLU   B  1  1199 ? 12.227  62.927  58.493  1.00 27.87 ? 1197 GLU   B CB    1 
ATOM   17841 C  CG    . GLU   B  1  1199 ? 11.506  61.670  58.901  1.00 35.77 ? 1197 GLU   B CG    1 
ATOM   17842 C  CD    . GLU   B  1  1199 ? 12.472  60.531  59.155  1.00 38.41 ? 1197 GLU   B CD    1 
ATOM   17843 O  OE1   . GLU   B  1  1199 ? 13.682  60.692  58.860  1.00 37.40 ? 1197 GLU   B OE1   1 
ATOM   17844 O  OE2   . GLU   B  1  1199 ? 12.025  59.479  59.655  1.00 46.18 ? 1197 GLU   B OE2   1 
ATOM   17845 N  N     . ILE   B  1  1200 ? 11.223  65.394  60.191  1.00 22.35 ? 1198 ILE   B N     1 
ATOM   17846 C  CA    . ILE   B  1  1200 ? 10.545  65.979  61.343  1.00 22.72 ? 1198 ILE   B CA    1 
ATOM   17847 C  C     . ILE   B  1  1200 ? 9.397   66.873  60.892  1.00 25.71 ? 1198 ILE   B C     1 
ATOM   17848 O  O     . ILE   B  1  1200 ? 8.317   66.880  61.500  1.00 24.64 ? 1198 ILE   B O     1 
ATOM   17849 C  CB    . ILE   B  1  1200 ? 11.563  66.733  62.216  1.00 20.53 ? 1198 ILE   B CB    1 
ATOM   17850 C  CG1   . ILE   B  1  1200 ? 12.558  65.751  62.838  1.00 21.53 ? 1198 ILE   B CG1   1 
ATOM   17851 C  CG2   . ILE   B  1  1200 ? 10.859  67.547  63.284  1.00 20.66 ? 1198 ILE   B CG2   1 
ATOM   17852 C  CD1   . ILE   B  1  1200 ? 13.703  66.440  63.560  1.00 21.82 ? 1198 ILE   B CD1   1 
ATOM   17853 N  N     . ALA   B  1  1201 ? 9.603   67.629  59.811  1.00 25.67 ? 1199 ALA   B N     1 
ATOM   17854 C  CA    . ALA   B  1  1201 ? 8.563   68.534  59.337  1.00 28.44 ? 1199 ALA   B CA    1 
ATOM   17855 C  C     . ALA   B  1  1201 ? 7.396   67.773  58.716  1.00 28.22 ? 1199 ALA   B C     1 
ATOM   17856 O  O     . ALA   B  1  1201 ? 6.239   68.172  58.882  1.00 33.67 ? 1199 ALA   B O     1 
ATOM   17857 C  CB    . ALA   B  1  1201 ? 9.149   69.530  58.337  1.00 28.08 ? 1199 ALA   B CB    1 
ATOM   17858 N  N     . ARG   B  1  1202 ? 7.678   66.676  58.007  1.00 30.69 ? 1200 ARG   B N     1 
ATOM   17859 C  CA    . ARG   B  1  1202 ? 6.663   65.947  57.249  1.00 29.97 ? 1200 ARG   B CA    1 
ATOM   17860 C  C     . ARG   B  1  1202 ? 5.931   64.906  58.081  1.00 31.78 ? 1200 ARG   B C     1 
ATOM   17861 O  O     . ARG   B  1  1202 ? 4.733   64.685  57.878  1.00 32.63 ? 1200 ARG   B O     1 
ATOM   17862 C  CB    . ARG   B  1  1202 ? 7.299   65.217  56.061  1.00 32.70 ? 1200 ARG   B CB    1 
ATOM   17863 C  CG    . ARG   B  1  1202 ? 7.918   66.119  55.012  1.00 42.58 ? 1200 ARG   B CG    1 
ATOM   17864 C  CD    . ARG   B  1  1202 ? 8.431   65.312  53.829  1.00 46.34 ? 1200 ARG   B CD    1 
ATOM   17865 N  NE    . ARG   B  1  1202 ? 9.168   64.126  54.251  1.00 45.17 ? 1200 ARG   B NE    1 
ATOM   17866 C  CZ    . ARG   B  1  1202 ? 10.491  64.041  54.304  1.00 45.50 ? 1200 ARG   B CZ    1 
ATOM   17867 N  NH1   . ARG   B  1  1202 ? 11.264  65.058  53.956  1.00 47.08 ? 1200 ARG   B NH1   1 
ATOM   17868 N  NH2   . ARG   B  1  1202 ? 11.052  62.904  54.711  1.00 40.48 ? 1200 ARG   B NH2   1 
ATOM   17869 N  N     . ASN   B  1  1203 ? 6.627   64.251  59.002  1.00 26.27 ? 1201 ASN   B N     1 
ATOM   17870 C  CA    . ASN   B  1  1203 ? 6.111   63.048  59.639  1.00 27.52 ? 1201 ASN   B CA    1 
ATOM   17871 C  C     . ASN   B  1  1203 ? 5.896   63.303  61.120  1.00 25.32 ? 1201 ASN   B C     1 
ATOM   17872 O  O     . ASN   B  1  1203 ? 6.879   63.431  61.870  1.00 26.09 ? 1201 ASN   B O     1 
ATOM   17873 C  CB    . ASN   B  1  1203 ? 7.098   61.900  59.433  1.00 27.75 ? 1201 ASN   B CB    1 
ATOM   17874 C  CG    . ASN   B  1  1203 ? 6.657   60.614  60.104  1.00 28.43 ? 1201 ASN   B CG    1 
ATOM   17875 O  OD1   . ASN   B  1  1203 ? 5.540   60.511  60.616  1.00 33.46 ? 1201 ASN   B OD1   1 
ATOM   17876 N  ND2   . ASN   B  1  1203 ? 7.538   59.619  60.101  1.00 32.45 ? 1201 ASN   B ND2   1 
ATOM   17877 N  N     . PRO   B  1  1204 ? 4.646   63.363  61.589  1.00 28.82 ? 1202 PRO   B N     1 
ATOM   17878 C  CA    . PRO   B  1  1204 ? 4.410   63.560  63.029  1.00 29.62 ? 1202 PRO   B CA    1 
ATOM   17879 C  C     . PRO   B  1  1204 ? 4.997   62.460  63.890  1.00 26.37 ? 1202 PRO   B C     1 
ATOM   17880 O  O     . PRO   B  1  1204 ? 5.209   62.678  65.090  1.00 28.44 ? 1202 PRO   B O     1 
ATOM   17881 C  CB    . PRO   B  1  1204 ? 2.878   63.596  63.137  1.00 34.20 ? 1202 PRO   B CB    1 
ATOM   17882 C  CG    . PRO   B  1  1204 ? 2.396   63.921  61.762  1.00 33.69 ? 1202 PRO   B CG    1 
ATOM   17883 C  CD    . PRO   B  1  1204 ? 3.388   63.307  60.821  1.00 28.94 ? 1202 PRO   B CD    1 
ATOM   17884 N  N     . ASP   B  1  1205 ? 5.267   61.286  63.322  1.00 25.27 ? 1203 ASP   B N     1 
ATOM   17885 C  CA    . ASP   B  1  1205 ? 5.847   60.171  64.057  1.00 26.52 ? 1203 ASP   B CA    1 
ATOM   17886 C  C     . ASP   B  1  1205 ? 7.314   59.956  63.704  1.00 26.68 ? 1203 ASP   B C     1 
ATOM   17887 O  O     . ASP   B  1  1205 ? 7.823   58.837  63.795  1.00 25.88 ? 1203 ASP   B O     1 
ATOM   17888 C  CB    . ASP   B  1  1205 ? 5.034   58.893  63.855  1.00 30.45 ? 1203 ASP   B CB    1 
ATOM   17889 C  CG    . ASP   B  1  1205 ? 3.637   58.993  64.442  1.00 33.80 ? 1203 ASP   B CG    1 
ATOM   17890 O  OD1   . ASP   B  1  1205 ? 3.423   59.842  65.335  1.00 31.40 ? 1203 ASP   B OD1   1 
ATOM   17891 O  OD2   . ASP   B  1  1205 ? 2.753   58.224  64.008  1.00 39.22 ? 1203 ASP   B OD2   1 
ATOM   17892 N  N     . ALA   B  1  1206 ? 7.997   61.026  63.285  1.00 24.98 ? 1204 ALA   B N     1 
ATOM   17893 C  CA    . ALA   B  1  1206 ? 9.422   60.928  62.987  1.00 23.43 ? 1204 ALA   B CA    1 
ATOM   17894 C  C     . ALA   B  1  1206 ? 10.185  60.331  64.161  1.00 20.86 ? 1204 ALA   B C     1 
ATOM   17895 O  O     . ALA   B  1  1206 ? 11.077  59.497  63.979  1.00 23.61 ? 1204 ALA   B O     1 
ATOM   17896 C  CB    . ALA   B  1  1206 ? 9.969   62.313  62.637  1.00 25.21 ? 1204 ALA   B CB    1 
ATOM   17897 N  N     . TYR   B  1  1207 ? 9.842   60.744  65.374  1.00 19.62 ? 1205 TYR   B N     1 
ATOM   17898 C  CA    . TYR   B  1  1207 ? 10.330  60.111  66.585  1.00 19.38 ? 1205 TYR   B CA    1 
ATOM   17899 C  C     . TYR   B  1  1207 ? 9.183   59.344  67.215  1.00 19.70 ? 1205 TYR   B C     1 
ATOM   17900 O  O     . TYR   B  1  1207 ? 8.075   59.874  67.346  1.00 25.95 ? 1205 TYR   B O     1 
ATOM   17901 C  CB    . TYR   B  1  1207 ? 10.850  61.157  67.566  1.00 18.54 ? 1205 TYR   B CB    1 
ATOM   17902 C  CG    . TYR   B  1  1207 ? 12.015  61.932  67.015  1.00 17.98 ? 1205 TYR   B CG    1 
ATOM   17903 C  CD1   . TYR   B  1  1207 ? 13.179  61.285  66.644  1.00 17.23 ? 1205 TYR   B CD1   1 
ATOM   17904 C  CD2   . TYR   B  1  1207 ? 11.951  63.309  66.858  1.00 19.05 ? 1205 TYR   B CD2   1 
ATOM   17905 C  CE1   . TYR   B  1  1207 ? 14.260  61.988  66.146  1.00 16.44 ? 1205 TYR   B CE1   1 
ATOM   17906 C  CE2   . TYR   B  1  1207 ? 13.033  64.025  66.357  1.00 19.17 ? 1205 TYR   B CE2   1 
ATOM   17907 C  CZ    . TYR   B  1  1207 ? 14.180  63.351  65.998  1.00 17.99 ? 1205 TYR   B CZ    1 
ATOM   17908 O  OH    . TYR   B  1  1207 ? 15.263  64.047  65.496  1.00 17.60 ? 1205 TYR   B OH    1 
ATOM   17909 N  N     . CYS   B  1  1208 ? 9.453   58.107  67.594  1.00 15.91 ? 1206 CYS   B N     1 
ATOM   17910 C  CA    . CYS   B  1  1208 ? 8.432   57.213  68.115  1.00 15.38 ? 1206 CYS   B CA    1 
ATOM   17911 C  C     . CYS   B  1  1208 ? 8.439   57.282  69.636  1.00 16.44 ? 1206 CYS   B C     1 
ATOM   17912 O  O     . CYS   B  1  1208 ? 9.462   57.014  70.267  1.00 15.74 ? 1206 CYS   B O     1 
ATOM   17913 C  CB    . CYS   B  1  1208 ? 8.732   55.796  67.641  1.00 18.64 ? 1206 CYS   B CB    1 
ATOM   17914 S  SG    . CYS   B  1  1208 ? 7.503   54.615  68.191  1.00 21.32 ? 1206 CYS   B SG    1 
ATOM   17915 N  N     . LEU   B  1  1209 ? 7.288   57.621  70.226  1.00 15.33 ? 1207 LEU   B N     1 
ATOM   17916 C  CA    . LEU   B  1  1209 ? 7.208   57.712  71.681  1.00 14.22 ? 1207 LEU   B CA    1 
ATOM   17917 C  C     . LEU   B  1  1209 ? 7.271   56.348  72.347  1.00 14.00 ? 1207 LEU   B C     1 
ATOM   17918 O  O     . LEU   B  1  1209 ? 7.508   56.281  73.552  1.00 14.36 ? 1207 LEU   B O     1 
ATOM   17919 C  CB    . LEU   B  1  1209 ? 5.940   58.447  72.097  1.00 13.31 ? 1207 LEU   B CB    1 
ATOM   17920 C  CG    . LEU   B  1  1209 ? 5.767   59.828  71.473  1.00 17.08 ? 1207 LEU   B CG    1 
ATOM   17921 C  CD1   . LEU   B  1  1209 ? 4.555   60.500  72.088  1.00 17.84 ? 1207 LEU   B CD1   1 
ATOM   17922 C  CD2   . LEU   B  1  1209 ? 7.009   60.672  71.666  1.00 18.89 ? 1207 LEU   B CD2   1 
ATOM   17923 N  N     . ASN   B  1  1210 ? 7.070   55.262  71.592  1.00 14.34 ? 1208 ASN   B N     1 
ATOM   17924 C  CA    . ASN   B  1  1210 ? 7.119   53.933  72.186  1.00 17.91 ? 1208 ASN   B CA    1 
ATOM   17925 C  C     . ASN   B  1  1210 ? 8.479   53.677  72.814  1.00 14.98 ? 1208 ASN   B C     1 
ATOM   17926 O  O     . ASN   B  1  1210 ? 8.579   52.963  73.821  1.00 17.07 ? 1208 ASN   B O     1 
ATOM   17927 C  CB    . ASN   B  1  1210 ? 6.847   52.845  71.130  1.00 20.09 ? 1208 ASN   B CB    1 
ATOM   17928 C  CG    . ASN   B  1  1210 ? 5.445   52.931  70.511  1.00 19.46 ? 1208 ASN   B CG    1 
ATOM   17929 O  OD1   . ASN   B  1  1210 ? 4.733   53.910  70.692  1.00 24.22 ? 1208 ASN   B OD1   1 
ATOM   17930 N  ND2   . ASN   B  1  1210 ? 5.081   51.916  69.726  1.00 24.54 ? 1208 ASN   B ND2   1 
ATOM   17931 N  N     . TRP   B  1  1211 ? 9.535   54.262  72.247  1.00 14.81 ? 1209 TRP   B N     1 
ATOM   17932 C  CA    . TRP   B  1  1211 ? 10.892  53.983  72.694  1.00 13.85 ? 1209 TRP   B CA    1 
ATOM   17933 C  C     . TRP   B  1  1211 ? 11.368  54.960  73.750  1.00 15.53 ? 1209 TRP   B C     1 
ATOM   17934 O  O     . TRP   B  1  1211 ? 12.484  54.812  74.256  1.00 17.41 ? 1209 TRP   B O     1 
ATOM   17935 C  CB    . TRP   B  1  1211 ? 11.871  53.964  71.507  1.00 16.30 ? 1209 TRP   B CB    1 
ATOM   17936 C  CG    . TRP   B  1  1211 ? 11.294  53.290  70.309  1.00 16.95 ? 1209 TRP   B CG    1 
ATOM   17937 C  CD1   . TRP   B  1  1211 ? 11.247  53.785  69.045  1.00 18.11 ? 1209 TRP   B CD1   1 
ATOM   17938 C  CD2   . TRP   B  1  1211 ? 10.642  52.017  70.268  1.00 15.68 ? 1209 TRP   B CD2   1 
ATOM   17939 N  NE1   . TRP   B  1  1211 ? 10.615  52.899  68.213  1.00 19.22 ? 1209 TRP   B NE1   1 
ATOM   17940 C  CE2   . TRP   B  1  1211 ? 10.240  51.800  68.939  1.00 17.20 ? 1209 TRP   B CE2   1 
ATOM   17941 C  CE3   . TRP   B  1  1211 ? 10.374  51.031  71.222  1.00 17.30 ? 1209 TRP   B CE3   1 
ATOM   17942 C  CZ2   . TRP   B  1  1211 ? 9.559   50.650  68.540  1.00 17.99 ? 1209 TRP   B CZ2   1 
ATOM   17943 C  CZ3   . TRP   B  1  1211 ? 9.701   49.889  70.821  1.00 17.20 ? 1209 TRP   B CZ3   1 
ATOM   17944 C  CH2   . TRP   B  1  1211 ? 9.303   49.707  69.496  1.00 18.39 ? 1209 TRP   B CH2   1 
ATOM   17945 N  N     . LEU   B  1  1212 ? 10.553  55.946  74.091  1.00 14.14 ? 1210 LEU   B N     1 
ATOM   17946 C  CA    . LEU   B  1  1212 ? 10.923  56.973  75.044  1.00 12.56 ? 1210 LEU   B CA    1 
ATOM   17947 C  C     . LEU   B  1  1212 ? 10.313  56.742  76.410  1.00 14.07 ? 1210 LEU   B C     1 
ATOM   17948 O  O     . LEU   B  1  1212 ? 10.486  57.570  77.300  1.00 13.35 ? 1210 LEU   B O     1 
ATOM   17949 C  CB    . LEU   B  1  1212 ? 10.552  58.348  74.496  1.00 13.04 ? 1210 LEU   B CB    1 
ATOM   17950 C  CG    . LEU   B  1  1212 ? 11.453  58.799  73.345  1.00 12.69 ? 1210 LEU   B CG    1 
ATOM   17951 C  CD1   . LEU   B  1  1212 ? 10.818  59.951  72.614  1.00 16.20 ? 1210 LEU   B CD1   1 
ATOM   17952 C  CD2   . LEU   B  1  1212 ? 12.832  59.169  73.864  1.00 15.60 ? 1210 LEU   B CD2   1 
ATOM   17953 N  N     . VAL   B  1  1213 ? 9.618   55.629  76.589  1.00 13.35 ? 1211 VAL   B N     1 
ATOM   17954 C  CA    . VAL   B  1  1213 ? 9.171   55.199  77.902  1.00 14.04 ? 1211 VAL   B CA    1 
ATOM   17955 C  C     . VAL   B  1  1213 ? 9.913   53.921  78.246  1.00 13.16 ? 1211 VAL   B C     1 
ATOM   17956 O  O     . VAL   B  1  1213 ? 10.423  53.214  77.373  1.00 14.78 ? 1211 VAL   B O     1 
ATOM   17957 C  CB    . VAL   B  1  1213 ? 7.646   54.988  77.946  1.00 13.32 ? 1211 VAL   B CB    1 
ATOM   17958 C  CG1   . VAL   B  1  1213 ? 6.957   56.333  77.830  1.00 15.13 ? 1211 VAL   B CG1   1 
ATOM   17959 C  CG2   . VAL   B  1  1213 ? 7.219   54.062  76.830  1.00 14.58 ? 1211 VAL   B CG2   1 
ATOM   17960 N  N     . GLU   B  1  1214 ? 10.003  53.650  79.545  1.00 13.09 ? 1212 GLU   B N     1 
ATOM   17961 C  CA    . GLU   B  1  1214 ? 10.547  52.407  80.063  1.00 14.92 ? 1212 GLU   B CA    1 
ATOM   17962 C  C     . GLU   B  1  1214 ? 9.410   51.534  80.574  1.00 13.12 ? 1212 GLU   B C     1 
ATOM   17963 O  O     . GLU   B  1  1214 ? 8.571   51.981  81.359  1.00 13.95 ? 1212 GLU   B O     1 
ATOM   17964 C  CB    . GLU   B  1  1214 ? 11.547  52.662  81.194  1.00 18.65 ? 1212 GLU   B CB    1 
ATOM   17965 C  CG    . GLU   B  1  1214 ? 12.183  51.368  81.703  1.00 20.78 ? 1212 GLU   B CG    1 
ATOM   17966 C  CD    . GLU   B  1  1214 ? 13.028  51.526  82.962  1.00 23.87 ? 1212 GLU   B CD    1 
ATOM   17967 O  OE1   . GLU   B  1  1214 ? 13.517  52.639  83.240  1.00 23.18 ? 1212 GLU   B OE1   1 
ATOM   17968 O  OE2   . GLU   B  1  1214 ? 13.193  50.512  83.679  1.00 26.67 ? 1212 GLU   B OE2   1 
ATOM   17969 N  N     . GLU   B  1  1215 ? 9.406   50.287  80.136  1.00 12.44 ? 1213 GLU   B N     1 
ATOM   17970 C  CA    . GLU   B  1  1215 ? 8.451   49.317  80.632  1.00 13.22 ? 1213 GLU   B CA    1 
ATOM   17971 C  C     . GLU   B  1  1215 ? 8.949   48.729  81.939  1.00 12.35 ? 1213 GLU   B C     1 
ATOM   17972 O  O     . GLU   B  1  1215 ? 10.129  48.390  82.078  1.00 13.46 ? 1213 GLU   B O     1 
ATOM   17973 C  CB    . GLU   B  1  1215 ? 8.337   48.184  79.625  1.00 13.80 ? 1213 GLU   B CB    1 
ATOM   17974 C  CG    . GLU   B  1  1215 ? 7.862   48.576  78.245  1.00 14.10 ? 1213 GLU   B CG    1 
ATOM   17975 C  CD    . GLU   B  1  1215 ? 8.084   47.461  77.277  1.00 13.33 ? 1213 GLU   B CD    1 
ATOM   17976 O  OE1   . GLU   B  1  1215 ? 9.214   47.336  76.775  1.00 14.30 ? 1213 GLU   B OE1   1 
ATOM   17977 O  OE2   . GLU   B  1  1215 ? 7.132   46.706  77.026  1.00 14.97 ? 1213 GLU   B OE2   1 
ATOM   17978 N  N     . VAL   B  1  1216 ? 8.044   48.586  82.896  1.00 12.68 ? 1214 VAL   B N     1 
ATOM   17979 C  CA    . VAL   B  1  1216 ? 8.355   47.889  84.133  1.00 13.01 ? 1214 VAL   B CA    1 
ATOM   17980 C  C     . VAL   B  1  1216 ? 7.281   46.849  84.372  1.00 11.61 ? 1214 VAL   B C     1 
ATOM   17981 O  O     . VAL   B  1  1216 ? 6.082   47.152  84.328  1.00 13.22 ? 1214 VAL   B O     1 
ATOM   17982 C  CB    . VAL   B  1  1216 ? 8.473   48.842  85.332  1.00 12.89 ? 1214 VAL   B CB    1 
ATOM   17983 C  CG1   . VAL   B  1  1216 ? 8.685   48.054  86.629  1.00 15.19 ? 1214 VAL   B CG1   1 
ATOM   17984 C  CG2   . VAL   B  1  1216 ? 9.608   49.843  85.102  1.00 15.82 ? 1214 VAL   B CG2   1 
ATOM   17985 N  N     . SER   B  1  1217 ? 7.711   45.620  84.606  1.00 11.58 ? 1215 SER   B N     1 
ATOM   17986 C  CA    . SER   B  1  1217 ? 6.823   44.530  84.959  1.00 12.12 ? 1215 SER   B CA    1 
ATOM   17987 C  C     . SER   B  1  1217 ? 6.997   44.259  86.440  1.00 11.80 ? 1215 SER   B C     1 
ATOM   17988 O  O     . SER   B  1  1217 ? 8.120   44.227  86.936  1.00 13.38 ? 1215 SER   B O     1 
ATOM   17989 C  CB    . SER   B  1  1217 ? 7.235   43.289  84.175  1.00 13.90 ? 1215 SER   B CB    1 
ATOM   17990 O  OG    . SER   B  1  1217 ? 6.746   42.096  84.752  1.00 15.59 ? 1215 SER   B OG    1 
ATOM   17991 N  N     . ALA   B  1  1218 ? 5.896   44.043  87.142  1.00 11.77 ? 1216 ALA   B N     1 
ATOM   17992 C  CA    . ALA   B  1  1218 ? 5.964   43.675  88.545  1.00 13.39 ? 1216 ALA   B CA    1 
ATOM   17993 C  C     . ALA   B  1  1218 ? 5.044   42.491  88.759  1.00 13.59 ? 1216 ALA   B C     1 
ATOM   17994 O  O     . ALA   B  1  1218 ? 3.860   42.547  88.411  1.00 15.34 ? 1216 ALA   B O     1 
ATOM   17995 C  CB    . ALA   B  1  1218 ? 5.548   44.837  89.447  1.00 15.37 ? 1216 ALA   B CB    1 
ATOM   17996 N  N     . SER   B  1  1219 ? 5.571   41.425  89.338  1.00 12.81 ? 1217 SER   B N     1 
ATOM   17997 C  CA    . SER   B  1  1219 ? 4.780   40.242  89.626  1.00 12.53 ? 1217 SER   B CA    1 
ATOM   17998 C  C     . SER   B  1  1219 ? 4.692   40.079  91.133  1.00 12.56 ? 1217 SER   B C     1 
ATOM   17999 O  O     . SER   B  1  1219 ? 5.711   39.901  91.801  1.00 13.29 ? 1217 SER   B O     1 
ATOM   18000 C  CB    . SER   B  1  1219 ? 5.433   39.016  89.004  1.00 14.72 ? 1217 SER   B CB    1 
ATOM   18001 O  OG    . SER   B  1  1219 ? 4.648   37.862  89.254  1.00 14.82 ? 1217 SER   B OG    1 
ATOM   18002 N  N     . ILE   B  1  1220 ? 3.481   40.132  91.657  1.00 13.97 ? 1218 ILE   B N     1 
ATOM   18003 C  CA    . ILE   B  1  1220 ? 3.247   40.076  93.093  1.00 13.89 ? 1218 ILE   B CA    1 
ATOM   18004 C  C     . ILE   B  1  1220 ? 2.564   38.757  93.404  1.00 14.26 ? 1218 ILE   B C     1 
ATOM   18005 O  O     . ILE   B  1  1220 ? 1.477   38.483  92.889  1.00 14.85 ? 1218 ILE   B O     1 
ATOM   18006 C  CB    . ILE   B  1  1220 ? 2.375   41.251  93.545  1.00 16.83 ? 1218 ILE   B CB    1 
ATOM   18007 C  CG1   . ILE   B  1  1220 ? 3.046   42.569  93.169  1.00 20.12 ? 1218 ILE   B CG1   1 
ATOM   18008 C  CG2   . ILE   B  1  1220 ? 2.111   41.163  95.045  1.00 17.94 ? 1218 ILE   B CG2   1 
ATOM   18009 C  CD1   . ILE   B  1  1220 ? 2.081   43.718  93.044  1.00 30.92 ? 1218 ILE   B CD1   1 
ATOM   18010 N  N     . ASN   B  1  1221 ? 3.172   37.958  94.270  1.00 14.29 ? 1219 ASN   B N     1 
ATOM   18011 C  CA    . ASN   B  1  1221 ? 2.543   36.732  94.745  1.00 14.14 ? 1219 ASN   B CA    1 
ATOM   18012 C  C     . ASN   B  1  1221 ? 1.524   37.112  95.809  1.00 16.24 ? 1219 ASN   B C     1 
ATOM   18013 O  O     . ASN   B  1  1221 ? 1.895   37.457  96.935  1.00 17.30 ? 1219 ASN   B O     1 
ATOM   18014 C  CB    . ASN   B  1  1221 ? 3.620   35.828  95.337  1.00 14.97 ? 1219 ASN   B CB    1 
ATOM   18015 C  CG    . ASN   B  1  1221 ? 3.048   34.569  95.962  1.00 15.73 ? 1219 ASN   B CG    1 
ATOM   18016 O  OD1   . ASN   B  1  1221 ? 1.854   34.281  95.843  1.00 15.29 ? 1219 ASN   B OD1   1 
ATOM   18017 N  ND2   . ASN   B  1  1221 ? 3.901   33.812  96.644  1.00 18.15 ? 1219 ASN   B ND2   1 
ATOM   18018 N  N     . THR   B  1  1222 ? 0.243   37.039  95.473  1.00 15.39 ? 1220 THR   B N     1 
ATOM   18019 C  CA    . THR   B  1  1222 ? -0.816  37.419  96.396  1.00 15.99 ? 1220 THR   B CA    1 
ATOM   18020 C  C     . THR   B  1  1222 ? -1.334  36.243  97.202  1.00 19.46 ? 1220 THR   B C     1 
ATOM   18021 O  O     . THR   B  1  1222 ? -2.297  36.395  97.964  1.00 24.58 ? 1220 THR   B O     1 
ATOM   18022 C  CB    . THR   B  1  1222 ? -1.955  38.094  95.646  1.00 18.15 ? 1220 THR   B CB    1 
ATOM   18023 O  OG1   . THR   B  1  1222 ? -2.471  37.190  94.664  1.00 20.51 ? 1220 THR   B OG1   1 
ATOM   18024 C  CG2   . THR   B  1  1222 ? -1.454  39.358  94.957  1.00 20.62 ? 1220 THR   B CG2   1 
ATOM   18025 N  N     . ALA   B  1  1223 ? -0.709  35.080  97.068  1.00 17.77 ? 1221 ALA   B N     1 
ATOM   18026 C  CA    . ALA   B  1  1223 ? -0.996  33.943  97.924  1.00 22.03 ? 1221 ALA   B CA    1 
ATOM   18027 C  C     . ALA   B  1  1223 ? 0.036   33.783  99.031  1.00 26.76 ? 1221 ALA   B C     1 
ATOM   18028 O  O     . ALA   B  1  1223 ? -0.032  32.807  99.784  1.00 33.17 ? 1221 ALA   B O     1 
ATOM   18029 C  CB    . ALA   B  1  1223 ? -1.049  32.664  97.087  1.00 24.12 ? 1221 ALA   B CB    1 
ATOM   18030 N  N     . ALA   B  1  1224 ? 0.987   34.719  99.146  1.00 28.00 ? 1222 ALA   B N     1 
ATOM   18031 C  CA    . ALA   B  1  1224 ? 2.138   34.512  100.021 1.00 31.51 ? 1222 ALA   B CA    1 
ATOM   18032 C  C     . ALA   B  1  1224 ? 1.758   34.462  101.495 1.00 36.91 ? 1222 ALA   B C     1 
ATOM   18033 O  O     . ALA   B  1  1224 ? 2.512   33.895  102.293 1.00 32.90 ? 1222 ALA   B O     1 
ATOM   18034 C  CB    . ALA   B  1  1224 ? 3.213   35.578  99.781  1.00 27.06 ? 1222 ALA   B CB    1 
ATOM   18035 N  N     . ALA   B  1  1225 ? 0.611   35.033  101.877 1.00 33.01 ? 1223 ALA   B N     1 
ATOM   18036 C  CA    . ALA   B  1  1225 ? 0.174   34.970  103.268 1.00 32.73 ? 1223 ALA   B CA    1 
ATOM   18037 C  C     . ALA   B  1  1225 ? -0.382  33.606  103.658 1.00 38.69 ? 1223 ALA   B C     1 
ATOM   18038 O  O     . ALA   B  1  1225 ? -0.647  33.383  104.844 1.00 38.22 ? 1223 ALA   B O     1 
ATOM   18039 C  CB    . ALA   B  1  1225 ? -0.864  36.061  103.563 1.00 36.48 ? 1223 ALA   B CB    1 
ATOM   18040 N  N     . GLY   B  1  1226 ? -0.566  32.697  102.704 1.00 36.50 ? 1224 GLY   B N     1 
ATOM   18041 C  CA    . GLY   B  1  1226 ? -1.063  31.363  102.994 1.00 33.82 ? 1224 GLY   B CA    1 
ATOM   18042 C  C     . GLY   B  1  1226 ? -2.371  31.009  102.316 1.00 39.26 ? 1224 GLY   B C     1 
ATOM   18043 O  O     . GLY   B  1  1226 ? -2.883  29.903  102.542 1.00 35.93 ? 1224 GLY   B O     1 
ATOM   18044 N  N     . GLY   B  1  1227 ? -2.936  31.894  101.503 1.00 33.28 ? 1225 GLY   B N     1 
ATOM   18045 C  CA    . GLY   B  1  1227 ? -4.163  31.610  100.781 1.00 31.04 ? 1225 GLY   B CA    1 
ATOM   18046 C  C     . GLY   B  1  1227 ? -4.450  32.731  99.807  1.00 37.12 ? 1225 GLY   B C     1 
ATOM   18047 O  O     . GLY   B  1  1227 ? -3.723  33.724  99.735  1.00 35.27 ? 1225 GLY   B O     1 
ATOM   18048 N  N     . ASN   B  1  1228 ? -5.544  32.566  99.068  1.00 31.83 ? 1226 ASN   B N     1 
ATOM   18049 C  CA    . ASN   B  1  1228 ? -5.934  33.484  98.002  1.00 34.75 ? 1226 ASN   B CA    1 
ATOM   18050 C  C     . ASN   B  1  1228 ? -7.219  34.198  98.406  1.00 40.93 ? 1226 ASN   B C     1 
ATOM   18051 O  O     . ASN   B  1  1228 ? -8.264  33.558  98.573  1.00 44.61 ? 1226 ASN   B O     1 
ATOM   18052 C  CB    . ASN   B  1  1228 ? -6.139  32.708  96.699  1.00 34.13 ? 1226 ASN   B CB    1 
ATOM   18053 C  CG    . ASN   B  1  1228 ? -6.322  33.610  95.486  1.00 38.02 ? 1226 ASN   B CG    1 
ATOM   18054 O  OD1   . ASN   B  1  1228 ? -6.935  34.676  95.562  1.00 37.86 ? 1226 ASN   B OD1   1 
ATOM   18055 N  ND2   . ASN   B  1  1228 ? -5.795  33.172  94.351  1.00 31.67 ? 1226 ASN   B ND2   1 
ATOM   18056 N  N     . ALA   B  1  1229 ? -7.139  35.524  98.548  1.00 38.47 ? 1227 ALA   B N     1 
ATOM   18057 C  CA    . ALA   B  1  1229 ? -8.315  36.312  98.908  1.00 42.43 ? 1227 ALA   B CA    1 
ATOM   18058 C  C     . ALA   B  1  1229 ? -9.390  36.227  97.831  1.00 46.33 ? 1227 ALA   B C     1 
ATOM   18059 O  O     . ALA   B  1  1229 ? -10.574 36.026  98.130  1.00 42.70 ? 1227 ALA   B O     1 
ATOM   18060 C  CB    . ALA   B  1  1229 ? -7.913  37.769  99.129  1.00 35.84 ? 1227 ALA   B CB    1 
ATOM   18061 N  N     . SER   B  1  1230 ? -8.993  36.387  96.565  1.00 46.45 ? 1228 SER   B N     1 
ATOM   18062 C  CA    . SER   B  1  1230 ? -9.970  36.455  95.483  1.00 44.45 ? 1228 SER   B CA    1 
ATOM   18063 C  C     . SER   B  1  1230 ? -10.728 35.141  95.331  1.00 52.81 ? 1228 SER   B C     1 
ATOM   18064 O  O     . SER   B  1  1230 ? -11.947 35.141  95.120  1.00 55.65 ? 1228 SER   B O     1 
ATOM   18065 C  CB    . SER   B  1  1230 ? -9.279  36.848  94.176  1.00 42.69 ? 1228 SER   B CB    1 
ATOM   18066 N  N     . LEU   B  1  1231 ? -10.030 34.009  95.446  1.00 47.82 ? 1229 LEU   B N     1 
ATOM   18067 C  CA    . LEU   B  1  1231 ? -10.685 32.715  95.294  1.00 48.56 ? 1229 LEU   B CA    1 
ATOM   18068 C  C     . LEU   B  1  1231 ? -11.504 32.309  96.514  1.00 51.64 ? 1229 LEU   B C     1 
ATOM   18069 O  O     . LEU   B  1  1231 ? -12.261 31.334  96.432  1.00 52.66 ? 1229 LEU   B O     1 
ATOM   18070 C  CB    . LEU   B  1  1231 ? -9.671  31.623  94.949  1.00 45.90 ? 1229 LEU   B CB    1 
ATOM   18071 C  CG    . LEU   B  1  1231 ? -9.018  31.554  93.566  1.00 34.79 ? 1229 LEU   B CG    1 
ATOM   18072 C  CD1   . LEU   B  1  1231 ? -8.223  30.265  93.465  1.00 28.69 ? 1229 LEU   B CD1   1 
ATOM   18073 C  CD2   . LEU   B  1  1231 ? -10.035 31.633  92.443  1.00 38.36 ? 1229 LEU   B CD2   1 
ATOM   18074 N  N     . MET   B  1  1232 ? -11.370 33.022  97.636  1.00 47.73 ? 1230 MET   B N     1 
ATOM   18075 C  CA    . MET   B  1  1232 ? -12.264 32.790  98.767  1.00 46.38 ? 1230 MET   B CA    1 
ATOM   18076 C  C     . MET   B  1  1232 ? -13.714 33.074  98.383  1.00 51.44 ? 1230 MET   B C     1 
ATOM   18077 O  O     . MET   B  1  1232 ? -14.637 32.387  98.842  1.00 42.72 ? 1230 MET   B O     1 
ATOM   18078 C  CB    . MET   B  1  1232 ? -11.833 33.652  99.954  1.00 43.92 ? 1230 MET   B CB    1 
ATOM   18079 N  N     . ALA   B  1  1233 ? -13.932 34.076  97.530  1.00 56.86 ? 1231 ALA   B N     1 
ATOM   18080 C  CA    . ALA   B  1  1233 ? -15.264 34.407  97.037  1.00 65.00 ? 1231 ALA   B CA    1 
ATOM   18081 C  C     . ALA   B  1  1233 ? -15.703 33.536  95.866  1.00 65.43 ? 1231 ALA   B C     1 
ATOM   18082 O  O     . ALA   B  1  1233 ? -16.787 33.765  95.317  1.00 66.88 ? 1231 ALA   B O     1 
ATOM   18083 C  CB    . ALA   B  1  1233 ? -15.326 35.884  96.634  1.00 58.37 ? 1231 ALA   B CB    1 
ATOM   18084 N  N     . ILE   B  1  1234 ? -14.902 32.548  95.476  1.00 59.80 ? 1232 ILE   B N     1 
ATOM   18085 C  CA    . ILE   B  1  1234 ? -15.187 31.701  94.323  1.00 58.26 ? 1232 ILE   B CA    1 
ATOM   18086 C  C     . ILE   B  1  1234 ? -15.577 30.316  94.829  1.00 51.42 ? 1232 ILE   B C     1 
ATOM   18087 O  O     . ILE   B  1  1234 ? -14.731 29.554  95.314  1.00 45.92 ? 1232 ILE   B O     1 
ATOM   18088 C  CB    . ILE   B  1  1234 ? -14.004 31.649  93.345  1.00 52.12 ? 1232 ILE   B CB    1 
ATOM   18089 C  CG1   . ILE   B  1  1234 ? -13.859 33.000  92.637  1.00 54.94 ? 1232 ILE   B CG1   1 
ATOM   18090 C  CG2   . ILE   B  1  1234 ? -14.185 30.527  92.341  1.00 45.48 ? 1232 ILE   B CG2   1 
ATOM   18091 C  CD1   . ILE   B  1  1234 ? -13.110 32.943  91.328  1.00 42.84 ? 1232 ILE   B CD1   1 
ATOM   18092 N  N     . GLY   B  1  1235 ? -16.864 29.998  94.724  1.00 50.36 ? 1233 GLY   B N     1 
ATOM   18093 C  CA    . GLY   B  1  1235 ? -17.374 28.684  95.072  1.00 37.58 ? 1233 GLY   B CA    1 
ATOM   18094 C  C     . GLY   B  1  1235 ? -18.227 28.119  93.951  1.00 34.48 ? 1233 GLY   B C     1 
ATOM   18095 O  O     . GLY   B  1  1235 ? -18.955 28.849  93.275  1.00 49.64 ? 1233 GLY   B O     1 
ATOM   18096 O  OXT   . GLY   B  1  1235 ? -18.223 26.921  93.685  1.00 26.37 ? 1233 GLY   B OXT   1 
HETATM 18097 P  PA    A FAD   C  2  .    ? -38.058 43.571  82.015  0.47 18.69 ? 1301 FAD   A PA    1 
HETATM 18098 P  PA    B FAD   C  2  .    ? -37.974 43.598  82.521  0.53 15.60 ? 1301 FAD   A PA    1 
HETATM 18099 O  O1A   A FAD   C  2  .    ? -38.905 42.373  82.520  0.47 19.26 ? 1301 FAD   A O1A   1 
HETATM 18100 O  O1A   B FAD   C  2  .    ? -38.960 42.440  82.822  0.53 18.79 ? 1301 FAD   A O1A   1 
HETATM 18101 O  O2A   A FAD   C  2  .    ? -36.643 43.410  81.748  0.47 20.48 ? 1301 FAD   A O2A   1 
HETATM 18102 O  O2A   B FAD   C  2  .    ? -36.567 43.337  82.290  0.53 20.10 ? 1301 FAD   A O2A   1 
HETATM 18103 O  O5B   A FAD   C  2  .    ? -38.046 44.744  82.938  0.47 18.16 ? 1301 FAD   A O5B   1 
HETATM 18104 O  O5B   B FAD   C  2  .    ? -37.919 44.642  83.549  0.53 15.98 ? 1301 FAD   A O5B   1 
HETATM 18105 C  C5B   A FAD   C  2  .    ? -36.945 45.490  83.441  0.47 18.45 ? 1301 FAD   A C5B   1 
HETATM 18106 C  C5B   B FAD   C  2  .    ? -36.944 45.663  83.596  0.53 18.09 ? 1301 FAD   A C5B   1 
HETATM 18107 C  C4B   A FAD   C  2  .    ? -37.468 46.533  84.446  0.47 18.19 ? 1301 FAD   A C4B   1 
HETATM 18108 C  C4B   B FAD   C  2  .    ? -37.483 46.708  84.560  0.53 18.31 ? 1301 FAD   A C4B   1 
HETATM 18109 O  O4B   A FAD   C  2  .    ? -37.467 46.091  85.773  0.47 17.95 ? 1301 FAD   A O4B   1 
HETATM 18110 O  O4B   B FAD   C  2  .    ? -37.508 46.227  85.867  0.53 17.70 ? 1301 FAD   A O4B   1 
HETATM 18111 C  C3B   A FAD   C  2  .    ? -36.706 47.820  84.504  0.47 18.04 ? 1301 FAD   A C3B   1 
HETATM 18112 C  C3B   B FAD   C  2  .    ? -36.677 47.961  84.634  0.53 17.55 ? 1301 FAD   A C3B   1 
HETATM 18113 O  O3B   A FAD   C  2  .    ? -36.953 48.659  83.433  0.47 18.01 ? 1301 FAD   A O3B   1 
HETATM 18114 O  O3B   B FAD   C  2  .    ? -36.870 48.810  83.559  0.53 17.98 ? 1301 FAD   A O3B   1 
HETATM 18115 C  C2B   A FAD   C  2  .    ? -37.174 48.414  85.778  0.47 18.50 ? 1301 FAD   A C2B   1 
HETATM 18116 C  C2B   B FAD   C  2  .    ? -37.186 48.540  85.894  0.53 18.54 ? 1301 FAD   A C2B   1 
HETATM 18117 O  O2B   A FAD   C  2  .    ? -38.381 49.076  85.654  0.47 17.58 ? 1301 FAD   A O2B   1 
HETATM 18118 O  O2B   B FAD   C  2  .    ? -38.415 49.150  85.728  0.53 17.53 ? 1301 FAD   A O2B   1 
HETATM 18119 C  C1B   A FAD   C  2  .    ? -37.359 47.203  86.622  0.47 17.08 ? 1301 FAD   A C1B   1 
HETATM 18120 C  C1B   B FAD   C  2  .    ? -37.370 47.320  86.723  0.53 17.14 ? 1301 FAD   A C1B   1 
HETATM 18121 N  N9A   A FAD   C  2  .    ? -36.284 46.960  87.555  0.47 18.43 ? 1301 FAD   A N9A   1 
HETATM 18122 N  N9A   B FAD   C  2  .    ? -36.274 47.041  87.612  0.53 18.35 ? 1301 FAD   A N9A   1 
HETATM 18123 C  C8A   A FAD   C  2  .    ? -34.979 46.610  87.249  0.47 19.98 ? 1301 FAD   A C8A   1 
HETATM 18124 C  C8A   B FAD   C  2  .    ? -34.972 46.692  87.283  0.53 19.99 ? 1301 FAD   A C8A   1 
HETATM 18125 N  N7A   A FAD   C  2  .    ? -34.282 46.461  88.381  0.47 19.80 ? 1301 FAD   A N7A   1 
HETATM 18126 N  N7A   B FAD   C  2  .    ? -34.272 46.510  88.408  0.53 19.78 ? 1301 FAD   A N7A   1 
HETATM 18127 C  C5A   A FAD   C  2  .    ? -35.103 46.705  89.470  0.47 18.55 ? 1301 FAD   A C5A   1 
HETATM 18128 C  C5A   B FAD   C  2  .    ? -35.091 46.730  89.504  0.53 18.54 ? 1301 FAD   A C5A   1 
HETATM 18129 C  C6A   A FAD   C  2  .    ? -34.932 46.695  90.847  0.47 19.32 ? 1301 FAD   A C6A   1 
HETATM 18130 C  C6A   B FAD   C  2  .    ? -34.928 46.686  90.879  0.53 19.34 ? 1301 FAD   A C6A   1 
HETATM 18131 N  N6A   A FAD   C  2  .    ? -33.658 46.367  91.436  0.47 19.43 ? 1301 FAD   A N6A   1 
HETATM 18132 N  N6A   B FAD   C  2  .    ? -33.660 46.339  91.468  0.53 19.40 ? 1301 FAD   A N6A   1 
HETATM 18133 N  N1A   A FAD   C  2  .    ? -35.965 46.986  91.652  0.47 18.81 ? 1301 FAD   A N1A   1 
HETATM 18134 N  N1A   B FAD   C  2  .    ? -35.965 46.961  91.684  0.53 18.82 ? 1301 FAD   A N1A   1 
HETATM 18135 C  C2A   A FAD   C  2  .    ? -37.188 47.293  91.153  0.47 19.36 ? 1301 FAD   A C2A   1 
HETATM 18136 C  C2A   B FAD   C  2  .    ? -37.186 47.285  91.195  0.53 19.37 ? 1301 FAD   A C2A   1 
HETATM 18137 N  N3A   A FAD   C  2  .    ? -37.390 47.306  89.810  0.47 18.36 ? 1301 FAD   A N3A   1 
HETATM 18138 N  N3A   B FAD   C  2  .    ? -37.381 47.332  89.854  0.53 18.37 ? 1301 FAD   A N3A   1 
HETATM 18139 C  C4A   A FAD   C  2  .    ? -36.386 47.026  88.959  0.47 18.62 ? 1301 FAD   A C4A   1 
HETATM 18140 C  C4A   B FAD   C  2  .    ? -36.372 47.068  89.008  0.53 18.64 ? 1301 FAD   A C4A   1 
HETATM 18141 N  N1    A FAD   C  2  .    ? -40.766 53.799  80.937  0.47 17.25 ? 1301 FAD   A N1    1 
HETATM 18142 N  N1    B FAD   C  2  .    ? -41.180 53.699  81.368  0.53 12.98 ? 1301 FAD   A N1    1 
HETATM 18143 C  C2    A FAD   C  2  .    ? -41.288 54.841  81.757  0.47 15.44 ? 1301 FAD   A C2    1 
HETATM 18144 C  C2    B FAD   C  2  .    ? -41.418 54.974  81.952  0.53 15.51 ? 1301 FAD   A C2    1 
HETATM 18145 O  O2    A FAD   C  2  .    ? -40.737 55.116  82.939  0.47 14.47 ? 1301 FAD   A O2    1 
HETATM 18146 O  O2    B FAD   C  2  .    ? -40.884 55.280  83.138  0.53 15.62 ? 1301 FAD   A O2    1 
HETATM 18147 N  N3    A FAD   C  2  .    ? -42.290 55.653  81.301  0.47 14.79 ? 1301 FAD   A N3    1 
HETATM 18148 N  N3    B FAD   C  2  .    ? -42.210 55.896  81.305  0.53 15.62 ? 1301 FAD   A N3    1 
HETATM 18149 C  C4    A FAD   C  2  .    ? -42.886 55.419  80.099  0.47 17.02 ? 1301 FAD   A C4    1 
HETATM 18150 C  C4    B FAD   C  2  .    ? -42.780 55.620  80.086  0.53 17.36 ? 1301 FAD   A C4    1 
HETATM 18151 O  O4    A FAD   C  2  .    ? -43.877 56.250  79.698  0.47 14.54 ? 1301 FAD   A O4    1 
HETATM 18152 O  O4    B FAD   C  2  .    ? -43.560 56.561  79.484  0.53 16.56 ? 1301 FAD   A O4    1 
HETATM 18153 C  C4X   A FAD   C  2  .    ? -42.545 54.201  79.320  0.47 15.65 ? 1301 FAD   A C4X   1 
HETATM 18154 C  C4X   B FAD   C  2  .    ? -42.560 54.304  79.427  0.53 15.57 ? 1301 FAD   A C4X   1 
HETATM 18155 N  N5    A FAD   C  2  .    ? -43.264 53.800  78.205  0.47 16.70 ? 1301 FAD   A N5    1 
HETATM 18156 N  N5    B FAD   C  2  .    ? -43.111 53.956  78.195  0.53 16.42 ? 1301 FAD   A N5    1 
HETATM 18157 C  C5X   A FAD   C  2  .    ? -42.900 52.626  77.546  0.47 16.43 ? 1301 FAD   A C5X   1 
HETATM 18158 C  C5X   B FAD   C  2  .    ? -42.859 52.687  77.661  0.53 16.45 ? 1301 FAD   A C5X   1 
HETATM 18159 C  C6    A FAD   C  2  .    ? -43.604 52.216  76.411  0.47 15.13 ? 1301 FAD   A C6    1 
HETATM 18160 C  C6    B FAD   C  2  .    ? -43.398 52.308  76.422  0.53 14.72 ? 1301 FAD   A C6    1 
HETATM 18161 C  C7    A FAD   C  2  .    ? -43.251 51.051  75.750  0.47 16.59 ? 1301 FAD   A C7    1 
HETATM 18162 C  C7    B FAD   C  2  .    ? -43.140 51.041  75.913  0.53 16.64 ? 1301 FAD   A C7    1 
HETATM 18163 C  C7M   A FAD   C  2  .    ? -44.046 50.637  74.543  0.47 16.00 ? 1301 FAD   A C7M   1 
HETATM 18164 C  C7M   B FAD   C  2  .    ? -43.728 50.631  74.591  0.53 16.91 ? 1301 FAD   A C7M   1 
HETATM 18165 C  C8    A FAD   C  2  .    ? -42.191 50.281  76.199  0.47 17.14 ? 1301 FAD   A C8    1 
HETATM 18166 C  C8    B FAD   C  2  .    ? -42.347 50.142  76.606  0.53 16.18 ? 1301 FAD   A C8    1 
HETATM 18167 C  C8M   A FAD   C  2  .    ? -41.794 49.025  75.496  0.47 18.32 ? 1301 FAD   A C8M   1 
HETATM 18168 C  C8M   B FAD   C  2  .    ? -42.069 48.781  76.051  0.53 15.93 ? 1301 FAD   A C8M   1 
HETATM 18169 C  C9    A FAD   C  2  .    ? -41.479 50.680  77.325  0.47 16.33 ? 1301 FAD   A C9    1 
HETATM 18170 C  C9    B FAD   C  2  .    ? -41.800 50.505  77.832  0.53 16.94 ? 1301 FAD   A C9    1 
HETATM 18171 C  C9A   A FAD   C  2  .    ? -41.831 51.844  77.988  0.47 16.42 ? 1301 FAD   A C9A   1 
HETATM 18172 C  C9A   B FAD   C  2  .    ? -42.058 51.769  78.350  0.53 17.43 ? 1301 FAD   A C9A   1 
HETATM 18173 N  N10   A FAD   C  2  .    ? -41.095 52.237  79.135  0.47 16.65 ? 1301 FAD   A N10   1 
HETATM 18174 N  N10   B FAD   C  2  .    ? -41.483 52.116  79.600  0.53 17.54 ? 1301 FAD   A N10   1 
HETATM 18175 C  C10   A FAD   C  2  .    ? -41.448 53.409  79.811  0.47 15.48 ? 1301 FAD   A C10   1 
HETATM 18176 C  C10   B FAD   C  2  .    ? -41.731 53.373  80.152  0.53 15.27 ? 1301 FAD   A C10   1 
HETATM 18177 C  "C1'" A FAD   C  2  .    ? -39.953 51.424  79.601  0.47 18.31 ? 1301 FAD   A "C1'" 1 
HETATM 18178 C  "C1'" B FAD   C  2  .    ? -40.693 51.126  80.346  0.53 17.89 ? 1301 FAD   A "C1'" 1 
HETATM 18179 C  "C2'" A FAD   C  2  .    ? -40.423 50.376  80.589  0.47 20.12 ? 1301 FAD   A "C2'" 1 
HETATM 18180 C  "C2'" B FAD   C  2  .    ? -39.193 51.279  80.363  0.53 18.85 ? 1301 FAD   A "C2'" 1 
HETATM 18181 O  "O2'" A FAD   C  2  .    ? -40.915 51.011  81.697  0.47 17.53 ? 1301 FAD   A "O2'" 1 
HETATM 18182 O  "O2'" B FAD   C  2  .    ? -38.741 52.123  79.375  0.53 21.14 ? 1301 FAD   A "O2'" 1 
HETATM 18183 C  "C3'" A FAD   C  2  .    ? -39.275 49.419  80.952  0.47 19.02 ? 1301 FAD   A "C3'" 1 
HETATM 18184 C  "C3'" B FAD   C  2  .    ? -38.637 49.859  80.191  0.53 17.63 ? 1301 FAD   A "C3'" 1 
HETATM 18185 O  "O3'" A FAD   C  2  .    ? -38.232 50.118  81.526  0.47 19.18 ? 1301 FAD   A "O3'" 1 
HETATM 18186 O  "O3'" B FAD   C  2  .    ? -38.792 49.478  78.880  0.53 20.50 ? 1301 FAD   A "O3'" 1 
HETATM 18187 C  "C4'" A FAD   C  2  .    ? -38.734 48.635  79.767  0.47 19.44 ? 1301 FAD   A "C4'" 1 
HETATM 18188 C  "C4'" B FAD   C  2  .    ? -39.324 48.813  81.053  0.53 18.75 ? 1301 FAD   A "C4'" 1 
HETATM 18189 O  "O4'" A FAD   C  2  .    ? -39.719 48.416  78.832  0.47 21.69 ? 1301 FAD   A "O4'" 1 
HETATM 18190 O  "O4'" B FAD   C  2  .    ? -39.357 49.217  82.365  0.53 17.98 ? 1301 FAD   A "O4'" 1 
HETATM 18191 C  "C5'" A FAD   C  2  .    ? -38.138 47.296  80.189  0.47 19.42 ? 1301 FAD   A "C5'" 1 
HETATM 18192 C  "C5'" B FAD   C  2  .    ? -38.651 47.452  80.945  0.53 18.33 ? 1301 FAD   A "C5'" 1 
HETATM 18193 O  "O5'" A FAD   C  2  .    ? -39.105 46.595  80.938  0.47 19.46 ? 1301 FAD   A "O5'" 1 
HETATM 18194 O  "O5'" B FAD   C  2  .    ? -39.537 46.521  81.525  0.53 18.88 ? 1301 FAD   A "O5'" 1 
HETATM 18195 P  P     A FAD   C  2  .    ? -39.724 45.191  80.485  0.47 13.70 ? 1301 FAD   A P     1 
HETATM 18196 P  P     B FAD   C  2  .    ? -39.699 45.035  80.962  0.53 24.32 ? 1301 FAD   A P     1 
HETATM 18197 O  O1P   A FAD   C  2  .    ? -41.092 44.827  81.152  0.47 17.58 ? 1301 FAD   A O1P   1 
HETATM 18198 O  O1P   B FAD   C  2  .    ? -40.978 44.194  81.313  0.53 21.42 ? 1301 FAD   A O1P   1 
HETATM 18199 O  O2P   A FAD   C  2  .    ? -39.651 45.304  78.914  0.47 19.10 ? 1301 FAD   A O2P   1 
HETATM 18200 O  O2P   B FAD   C  2  .    ? -39.490 45.346  79.439  0.53 19.74 ? 1301 FAD   A O2P   1 
HETATM 18201 O  O3P   A FAD   C  2  .    ? -38.464 44.177  80.713  0.47 17.17 ? 1301 FAD   A O3P   1 
HETATM 18202 O  O3P   B FAD   C  2  .    ? -38.237 44.422  81.308  0.53 18.85 ? 1301 FAD   A O3P   1 
HETATM 18203 C  C1    . PEG   D  3  .    ? -51.842 76.572  73.488  1.00 33.15 ? 1302 PEG   A C1    1 
HETATM 18204 O  O1    . PEG   D  3  .    ? -51.828 77.857  74.079  1.00 43.01 ? 1302 PEG   A O1    1 
HETATM 18205 C  C2    . PEG   D  3  .    ? -50.885 76.508  72.318  1.00 30.27 ? 1302 PEG   A C2    1 
HETATM 18206 O  O2    . PEG   D  3  .    ? -49.544 76.566  72.759  1.00 37.03 ? 1302 PEG   A O2    1 
HETATM 18207 C  C3    . PEG   D  3  .    ? -48.595 76.623  71.718  1.00 27.94 ? 1302 PEG   A C3    1 
HETATM 18208 C  C4    . PEG   D  3  .    ? -47.227 76.274  72.255  1.00 26.21 ? 1302 PEG   A C4    1 
HETATM 18209 O  O4    . PEG   D  3  .    ? -46.698 77.364  72.979  1.00 37.71 ? 1302 PEG   A O4    1 
HETATM 18210 C  C     . FMT   E  4  .    ? -40.486 61.420  102.465 1.00 25.96 ? 1303 FMT   A C     1 
HETATM 18211 O  O1    . FMT   E  4  .    ? -39.665 61.081  103.332 1.00 31.91 ? 1303 FMT   A O1    1 
HETATM 18212 O  O2    . FMT   E  4  .    ? -41.734 61.538  102.545 1.00 30.67 ? 1303 FMT   A O2    1 
HETATM 18213 C  C02   . A1BDX F  5  .    ? -39.302 53.194  76.061  0.67 21.96 ? 1304 A1BDX A C02   1 
HETATM 18214 C  C03   . A1BDX F  5  .    ? -39.791 54.459  76.794  0.67 20.40 ? 1304 A1BDX A C03   1 
HETATM 18215 C  C04   . A1BDX F  5  .    ? -40.932 55.097  76.335  0.67 20.25 ? 1304 A1BDX A C04   1 
HETATM 18216 C  C05   . A1BDX F  5  .    ? -41.421 56.269  76.986  0.67 18.89 ? 1304 A1BDX A C05   1 
HETATM 18217 C  C06   . A1BDX F  5  .    ? -40.715 56.806  78.142  0.67 16.61 ? 1304 A1BDX A C06   1 
HETATM 18218 C  C08   . A1BDX F  5  .    ? -40.091 58.004  79.866  0.67 18.35 ? 1304 A1BDX A C08   1 
HETATM 18219 C  C09   . A1BDX F  5  .    ? -39.185 56.978  79.724  0.67 19.99 ? 1304 A1BDX A C09   1 
HETATM 18220 C  C10   . A1BDX F  5  .    ? -39.592 56.185  78.610  0.67 19.66 ? 1304 A1BDX A C10   1 
HETATM 18221 C  C11   . A1BDX F  5  .    ? -39.091 54.981  77.940  0.67 20.37 ? 1304 A1BDX A C11   1 
HETATM 18222 O  O01   . A1BDX F  5  .    ? -37.863 53.209  76.072  0.67 26.58 ? 1304 A1BDX A O01   1 
HETATM 18223 O  O07   . A1BDX F  5  .    ? -40.987 57.873  78.914  0.67 19.71 ? 1304 A1BDX A O07   1 
HETATM 18224 P  PA    . NAD   G  6  .    ? -18.304 88.337  106.998 1.00 20.80 ? 1305 NAD   A PA    1 
HETATM 18225 O  O1A   . NAD   G  6  .    ? -16.777 88.259  106.808 1.00 21.00 ? 1305 NAD   A O1A   1 
HETATM 18226 O  O2A   . NAD   G  6  .    ? -19.005 89.552  106.604 1.00 23.08 ? 1305 NAD   A O2A   1 
HETATM 18227 O  O5B   . NAD   G  6  .    ? -18.783 88.122  108.392 1.00 20.32 ? 1305 NAD   A O5B   1 
HETATM 18228 C  C5B   . NAD   G  6  .    ? -18.504 86.901  109.035 1.00 20.92 ? 1305 NAD   A C5B   1 
HETATM 18229 C  C4B   . NAD   G  6  .    ? -18.459 87.013  110.554 1.00 18.68 ? 1305 NAD   A C4B   1 
HETATM 18230 O  O4B   . NAD   G  6  .    ? -17.321 87.728  111.001 1.00 19.40 ? 1305 NAD   A O4B   1 
HETATM 18231 C  C3B   . NAD   G  6  .    ? -19.675 87.645  111.170 1.00 19.91 ? 1305 NAD   A C3B   1 
HETATM 18232 O  O3B   . NAD   G  6  .    ? -20.066 86.962  112.304 1.00 20.80 ? 1305 NAD   A O3B   1 
HETATM 18233 C  C2B   . NAD   G  6  .    ? -19.215 89.010  111.464 1.00 23.31 ? 1305 NAD   A C2B   1 
HETATM 18234 O  O2B   . NAD   G  6  .    ? -19.932 89.605  112.491 1.00 21.72 ? 1305 NAD   A O2B   1 
HETATM 18235 C  C1B   . NAD   G  6  .    ? -17.820 88.733  111.860 1.00 23.53 ? 1305 NAD   A C1B   1 
HETATM 18236 N  N9A   . NAD   G  6  .    ? -16.937 89.871  111.788 1.00 20.50 ? 1305 NAD   A N9A   1 
HETATM 18237 C  C8A   . NAD   G  6  .    ? -16.988 90.963  110.948 1.00 22.44 ? 1305 NAD   A C8A   1 
HETATM 18238 N  N7A   . NAD   G  6  .    ? -15.944 91.756  111.192 1.00 22.74 ? 1305 NAD   A N7A   1 
HETATM 18239 C  C5A   . NAD   G  6  .    ? -15.166 91.197  112.195 1.00 21.18 ? 1305 NAD   A C5A   1 
HETATM 18240 C  C6A   . NAD   G  6  .    ? -14.003 91.555  112.845 1.00 24.63 ? 1305 NAD   A C6A   1 
HETATM 18241 N  N6A   . NAD   G  6  .    ? -13.334 92.771  112.492 1.00 26.21 ? 1305 NAD   A N6A   1 
HETATM 18242 N  N1A   . NAD   G  6  .    ? -13.507 90.756  113.797 1.00 24.75 ? 1305 NAD   A N1A   1 
HETATM 18243 C  C2A   . NAD   G  6  .    ? -14.105 89.593  114.163 1.00 24.84 ? 1305 NAD   A C2A   1 
HETATM 18244 N  N3A   . NAD   G  6  .    ? -15.256 89.209  113.550 1.00 21.23 ? 1305 NAD   A N3A   1 
HETATM 18245 C  C4A   . NAD   G  6  .    ? -15.783 89.985  112.586 1.00 21.83 ? 1305 NAD   A C4A   1 
HETATM 18246 O  O3    . NAD   G  6  .    ? -19.021 87.267  106.208 1.00 20.83 ? 1305 NAD   A O3    1 
HETATM 18247 P  PN    . NAD   G  6  .    ? -20.561 86.961  105.899 1.00 21.72 ? 1305 NAD   A PN    1 
HETATM 18248 O  O1N   . NAD   G  6  .    ? -21.072 88.034  104.991 1.00 22.67 ? 1305 NAD   A O1N   1 
HETATM 18249 O  O2N   . NAD   G  6  .    ? -21.365 86.748  107.149 1.00 22.49 ? 1305 NAD   A O2N   1 
HETATM 18250 O  O5D   . NAD   G  6  .    ? -20.479 85.605  105.071 1.00 21.27 ? 1305 NAD   A O5D   1 
HETATM 18251 C  C5D   . NAD   G  6  .    ? -20.147 85.637  103.709 1.00 24.28 ? 1305 NAD   A C5D   1 
HETATM 18252 C  C4D   . NAD   G  6  .    ? -18.709 85.219  103.459 1.00 20.01 ? 1305 NAD   A C4D   1 
HETATM 18253 O  O4D   . NAD   G  6  .    ? -18.405 84.006  104.091 1.00 20.50 ? 1305 NAD   A O4D   1 
HETATM 18254 C  C3D   . NAD   G  6  .    ? -18.430 85.057  101.999 1.00 22.75 ? 1305 NAD   A C3D   1 
HETATM 18255 O  O3D   . NAD   G  6  .    ? -17.245 85.662  101.664 1.00 23.38 ? 1305 NAD   A O3D   1 
HETATM 18256 C  C2D   . NAD   G  6  .    ? -18.341 83.600  101.837 1.00 18.94 ? 1305 NAD   A C2D   1 
HETATM 18257 O  O2D   . NAD   G  6  .    ? -17.603 83.175  100.735 1.00 21.43 ? 1305 NAD   A O2D   1 
HETATM 18258 C  C1D   . NAD   G  6  .    ? -17.743 83.220  103.137 1.00 20.54 ? 1305 NAD   A C1D   1 
HETATM 18259 N  N1N   . NAD   G  6  .    ? -18.034 81.858  103.431 1.00 18.34 ? 1305 NAD   A N1N   1 
HETATM 18260 C  C2N   . NAD   G  6  .    ? -17.014 80.879  103.369 1.00 18.43 ? 1305 NAD   A C2N   1 
HETATM 18261 C  C3N   . NAD   G  6  .    ? -17.364 79.571  103.673 1.00 19.82 ? 1305 NAD   A C3N   1 
HETATM 18262 C  C7N   . NAD   G  6  .    ? -16.370 78.473  103.616 1.00 16.68 ? 1305 NAD   A C7N   1 
HETATM 18263 O  O7N   . NAD   G  6  .    ? -16.673 77.354  103.994 1.00 20.26 ? 1305 NAD   A O7N   1 
HETATM 18264 N  N7N   . NAD   G  6  .    ? -15.075 78.729  103.096 1.00 17.48 ? 1305 NAD   A N7N   1 
HETATM 18265 C  C4N   . NAD   G  6  .    ? -18.690 79.261  104.053 1.00 31.06 ? 1305 NAD   A C4N   1 
HETATM 18266 C  C5N   . NAD   G  6  .    ? -19.703 80.236  104.076 1.00 25.07 ? 1305 NAD   A C5N   1 
HETATM 18267 C  C6N   . NAD   G  6  .    ? -19.361 81.535  103.769 1.00 19.08 ? 1305 NAD   A C6N   1 
HETATM 18268 S  S     . SO4   H  7  .    ? -9.310  52.999  110.798 1.00 18.50 ? 1306 SO4   A S     1 
HETATM 18269 O  O1    . SO4   H  7  .    ? -8.211  53.213  109.810 1.00 19.90 ? 1306 SO4   A O1    1 
HETATM 18270 O  O2    . SO4   H  7  .    ? -10.341 52.137  110.165 1.00 23.43 ? 1306 SO4   A O2    1 
HETATM 18271 O  O3    . SO4   H  7  .    ? -8.756  52.323  112.026 1.00 17.72 ? 1306 SO4   A O3    1 
HETATM 18272 O  O4    . SO4   H  7  .    ? -9.852  54.343  111.148 1.00 22.80 ? 1306 SO4   A O4    1 
HETATM 18273 S  S     . SO4   I  7  .    ? -12.514 75.225  69.935  0.63 28.41 ? 1307 SO4   A S     1 
HETATM 18274 O  O1    . SO4   I  7  .    ? -11.332 75.344  70.835  0.63 28.85 ? 1307 SO4   A O1    1 
HETATM 18275 O  O2    . SO4   I  7  .    ? -12.694 76.499  69.171  0.63 36.75 ? 1307 SO4   A O2    1 
HETATM 18276 O  O3    . SO4   I  7  .    ? -12.263 74.099  68.979  0.63 36.00 ? 1307 SO4   A O3    1 
HETATM 18277 O  O4    . SO4   I  7  .    ? -13.757 74.940  70.721  0.63 23.45 ? 1307 SO4   A O4    1 
HETATM 18278 S  S     . SO4   J  7  .    ? -39.346 66.207  55.742  0.53 31.83 ? 1308 SO4   A S     1 
HETATM 18279 O  O1    . SO4   J  7  .    ? -37.960 66.292  55.176  0.53 39.97 ? 1308 SO4   A O1    1 
HETATM 18280 O  O2    . SO4   J  7  .    ? -40.316 66.661  54.698  0.53 26.35 ? 1308 SO4   A O2    1 
HETATM 18281 O  O3    . SO4   J  7  .    ? -39.638 64.788  56.130  0.53 26.36 ? 1308 SO4   A O3    1 
HETATM 18282 O  O4    . SO4   J  7  .    ? -39.440 67.056  56.975  0.53 30.53 ? 1308 SO4   A O4    1 
HETATM 18283 S  S     . SO4   K  7  .    ? 12.678  75.398  125.587 0.71 33.73 ? 1309 SO4   A S     1 
HETATM 18284 O  O1    . SO4   K  7  .    ? 13.416  75.829  124.353 0.71 34.81 ? 1309 SO4   A O1    1 
HETATM 18285 O  O2    . SO4   K  7  .    ? 11.290  74.957  125.237 0.71 33.29 ? 1309 SO4   A O2    1 
HETATM 18286 O  O3    . SO4   K  7  .    ? 13.414  74.252  126.212 0.71 39.51 ? 1309 SO4   A O3    1 
HETATM 18287 O  O4    . SO4   K  7  .    ? 12.597  76.541  126.556 0.71 46.10 ? 1309 SO4   A O4    1 
HETATM 18288 S  S     . SO4   L  7  .    ? -18.323 54.177  86.281  0.53 41.78 ? 1310 SO4   A S     1 
HETATM 18289 O  O1    . SO4   L  7  .    ? -17.527 53.140  85.548  0.53 40.36 ? 1310 SO4   A O1    1 
HETATM 18290 O  O2    . SO4   L  7  .    ? -19.625 54.386  85.571  0.53 37.95 ? 1310 SO4   A O2    1 
HETATM 18291 O  O3    . SO4   L  7  .    ? -18.573 53.718  87.685  0.53 41.05 ? 1310 SO4   A O3    1 
HETATM 18292 O  O4    . SO4   L  7  .    ? -17.569 55.471  86.319  0.53 35.12 ? 1310 SO4   A O4    1 
HETATM 18293 MG MG    . MG    M  8  .    ? -20.042 91.346  106.855 0.74 21.98 ? 1311 MG    A MG    1 
HETATM 18294 C  C1    . PEG   N  3  .    ? -0.571  62.948  96.662  1.00 31.23 ? 1312 PEG   A C1    1 
HETATM 18295 O  O1    . PEG   N  3  .    ? -1.501  61.938  96.340  1.00 34.25 ? 1312 PEG   A O1    1 
HETATM 18296 C  C2    . PEG   N  3  .    ? 0.729   62.694  95.943  1.00 36.15 ? 1312 PEG   A C2    1 
HETATM 18297 O  O2    . PEG   N  3  .    ? 1.392   61.597  96.511  1.00 43.40 ? 1312 PEG   A O2    1 
HETATM 18298 C  C3    . PEG   N  3  .    ? 2.296   60.987  95.619  1.00 39.03 ? 1312 PEG   A C3    1 
HETATM 18299 C  C4    . PEG   N  3  .    ? 2.483   59.532  95.977  1.00 38.33 ? 1312 PEG   A C4    1 
HETATM 18300 O  O4    . PEG   N  3  .    ? 1.862   58.699  95.021  1.00 47.69 ? 1312 PEG   A O4    1 
HETATM 18301 P  PA    A FAD   O  2  .    ? -17.210 23.301  103.845 0.68 20.67 ? 1301 FAD   B PA    1 
HETATM 18302 P  PA    B FAD   O  2  .    ? -17.163 23.214  103.924 0.32 20.89 ? 1301 FAD   B PA    1 
HETATM 18303 O  O1A   A FAD   O  2  .    ? -17.522 24.809  103.952 0.68 24.20 ? 1301 FAD   B O1A   1 
HETATM 18304 O  O1A   B FAD   O  2  .    ? -17.515 24.713  103.726 0.32 23.97 ? 1301 FAD   B O1A   1 
HETATM 18305 O  O2A   A FAD   O  2  .    ? -18.276 22.340  103.632 0.68 24.16 ? 1301 FAD   B O2A   1 
HETATM 18306 O  O2A   B FAD   O  2  .    ? -18.195 22.217  103.753 0.32 24.47 ? 1301 FAD   B O2A   1 
HETATM 18307 O  O5B   A FAD   O  2  .    ? -16.291 22.914  102.718 0.68 20.33 ? 1301 FAD   B O5B   1 
HETATM 18308 O  O5B   B FAD   O  2  .    ? -16.132 22.649  103.020 0.32 21.15 ? 1301 FAD   B O5B   1 
HETATM 18309 C  C5B   A FAD   O  2  .    ? -15.201 23.764  102.394 0.68 21.93 ? 1301 FAD   B C5B   1 
HETATM 18310 C  C5B   B FAD   O  2  .    ? -15.196 23.551  102.460 0.32 21.77 ? 1301 FAD   B C5B   1 
HETATM 18311 C  C4B   A FAD   O  2  .    ? -14.240 23.043  101.456 0.68 18.96 ? 1301 FAD   B C4B   1 
HETATM 18312 C  C4B   B FAD   O  2  .    ? -14.272 22.822  101.495 0.32 18.99 ? 1301 FAD   B C4B   1 
HETATM 18313 O  O4B   A FAD   O  2  .    ? -14.752 22.988  100.158 0.68 17.96 ? 1301 FAD   B O4B   1 
HETATM 18314 O  O4B   B FAD   O  2  .    ? -14.766 22.824  100.191 0.32 18.11 ? 1301 FAD   B O4B   1 
HETATM 18315 C  C3B   A FAD   O  2  .    ? -12.901 23.695  101.290 0.68 17.55 ? 1301 FAD   B C3B   1 
HETATM 18316 C  C3B   B FAD   O  2  .    ? -12.920 23.450  101.426 0.32 18.31 ? 1301 FAD   B C3B   1 
HETATM 18317 O  O3B   A FAD   O  2  .    ? -12.042 23.569  102.376 0.68 16.28 ? 1301 FAD   B O3B   1 
HETATM 18318 O  O3B   B FAD   O  2  .    ? -12.063 22.997  102.410 0.32 17.52 ? 1301 FAD   B O3B   1 
HETATM 18319 C  C2B   A FAD   O  2  .    ? -12.405 23.000  100.071 0.68 17.84 ? 1301 FAD   B C2B   1 
HETATM 18320 C  C2B   B FAD   O  2  .    ? -12.425 23.031  100.100 0.32 17.90 ? 1301 FAD   B C2B   1 
HETATM 18321 O  O2B   A FAD   O  2  .    ? -12.031 21.695  100.286 0.68 16.93 ? 1301 FAD   B O2B   1 
HETATM 18322 O  O2B   B FAD   O  2  .    ? -11.775 21.831  100.179 0.32 18.34 ? 1301 FAD   B O2B   1 
HETATM 18323 C  C1B   A FAD   O  2  .    ? -13.655 22.959  99.276  0.68 18.17 ? 1301 FAD   B C1B   1 
HETATM 18324 C  C1B   B FAD   O  2  .    ? -13.671 22.864  99.313  0.32 18.18 ? 1301 FAD   B C1B   1 
HETATM 18325 N  N9A   A FAD   O  2  .    ? -13.852 24.029  98.335  0.68 17.83 ? 1301 FAD   B N9A   1 
HETATM 18326 N  N9A   B FAD   O  2  .    ? -13.887 23.923  98.364  0.32 17.90 ? 1301 FAD   B N9A   1 
HETATM 18327 C  C8A   A FAD   O  2  .    ? -13.991 25.380  98.583  0.68 20.50 ? 1301 FAD   B C8A   1 
HETATM 18328 C  C8A   B FAD   O  2  .    ? -14.044 25.267  98.639  0.32 20.41 ? 1301 FAD   B C8A   1 
HETATM 18329 N  N7A   A FAD   O  2  .    ? -14.186 26.039  97.439  0.68 20.25 ? 1301 FAD   B N7A   1 
HETATM 18330 N  N7A   B FAD   O  2  .    ? -14.231 25.945  97.503  0.32 20.21 ? 1301 FAD   B N7A   1 
HETATM 18331 C  C5A   A FAD   O  2  .    ? -14.182 25.119  96.394  0.68 15.92 ? 1301 FAD   B C5A   1 
HETATM 18332 C  C5A   B FAD   O  2  .    ? -14.201 25.058  96.435  0.32 16.07 ? 1301 FAD   B C5A   1 
HETATM 18333 C  C6A   A FAD   O  2  .    ? -14.352 25.196  95.022  0.68 17.76 ? 1301 FAD   B C6A   1 
HETATM 18334 C  C6A   B FAD   O  2  .    ? -14.344 25.184  95.062  0.32 17.82 ? 1301 FAD   B C6A   1 
HETATM 18335 N  N6A   A FAD   O  2  .    ? -14.577 26.466  94.386  0.68 18.04 ? 1301 FAD   B N6A   1 
HETATM 18336 N  N6A   B FAD   O  2  .    ? -14.574 26.479  94.473  0.32 18.09 ? 1301 FAD   B N6A   1 
HETATM 18337 N  N1A   A FAD   O  2  .    ? -14.293 24.067  94.298  0.68 16.45 ? 1301 FAD   B N1A   1 
HETATM 18338 N  N1A   B FAD   O  2  .    ? -14.263 24.088  94.288  0.32 16.52 ? 1301 FAD   B N1A   1 
HETATM 18339 C  C2A   A FAD   O  2  .    ? -14.099 22.849  94.854  0.68 15.80 ? 1301 FAD   B C2A   1 
HETATM 18340 C  C2A   B FAD   O  2  .    ? -14.056 22.853  94.809  0.32 15.88 ? 1301 FAD   B C2A   1 
HETATM 18341 N  N3A   A FAD   O  2  .    ? -13.937 22.727  96.198  0.68 16.63 ? 1301 FAD   B N3A   1 
HETATM 18342 N  N3A   B FAD   O  2  .    ? -13.915 22.693  96.151  0.32 16.71 ? 1301 FAD   B N3A   1 
HETATM 18343 C  C4A   A FAD   O  2  .    ? -13.981 23.829  96.954  0.68 17.72 ? 1301 FAD   B C4A   1 
HETATM 18344 C  C4A   B FAD   O  2  .    ? -13.985 23.757  96.965  0.32 17.71 ? 1301 FAD   B C4A   1 
HETATM 18345 N  N1    A FAD   O  2  .    ? -7.689  18.617  104.667 0.68 14.66 ? 1301 FAD   B N1    1 
HETATM 18346 N  N1    B FAD   O  2  .    ? -7.392  18.980  104.941 0.32 16.07 ? 1301 FAD   B N1    1 
HETATM 18347 C  C2    A FAD   O  2  .    ? -6.520  18.125  104.047 0.68 17.27 ? 1301 FAD   B C2    1 
HETATM 18348 C  C2    B FAD   O  2  .    ? -6.398  18.325  104.143 0.32 16.87 ? 1301 FAD   B C2    1 
HETATM 18349 O  O2    A FAD   O  2  .    ? -6.264  18.563  102.818 0.68 15.02 ? 1301 FAD   B O2    1 
HETATM 18350 O  O2    B FAD   O  2  .    ? -6.086  18.847  102.936 0.32 16.75 ? 1301 FAD   B O2    1 
HETATM 18351 N  N3    A FAD   O  2  .    ? -5.689  17.227  104.662 0.68 16.29 ? 1301 FAD   B N3    1 
HETATM 18352 N  N3    B FAD   O  2  .    ? -5.729  17.215  104.612 0.32 16.31 ? 1301 FAD   B N3    1 
HETATM 18353 C  C4    A FAD   O  2  .    ? -5.947  16.782  105.927 0.68 16.14 ? 1301 FAD   B C4    1 
HETATM 18354 C  C4    B FAD   O  2  .    ? -6.026  16.671  105.840 0.32 16.41 ? 1301 FAD   B C4    1 
HETATM 18355 O  O4    A FAD   O  2  .    ? -5.128  15.882  106.512 0.68 19.16 ? 1301 FAD   B O4    1 
HETATM 18356 O  O4    B FAD   O  2  .    ? -5.344  15.566  106.264 0.32 14.32 ? 1301 FAD   B O4    1 
HETATM 18357 C  C4X   A FAD   O  2  .    ? -7.159  17.266  106.625 0.68 16.50 ? 1301 FAD   B C4X   1 
HETATM 18358 C  C4X   B FAD   O  2  .    ? -7.145  17.242  106.647 0.32 16.57 ? 1301 FAD   B C4X   1 
HETATM 18359 N  N5    A FAD   O  2  .    ? -7.494  16.835  107.899 0.68 17.16 ? 1301 FAD   B N5    1 
HETATM 18360 N  N5    B FAD   O  2  .    ? -7.579  16.671  107.840 0.32 17.27 ? 1301 FAD   B N5    1 
HETATM 18361 C  C5X   A FAD   O  2  .    ? -8.657  17.323  108.485 0.68 17.18 ? 1301 FAD   B C5X   1 
HETATM 18362 C  C5X   B FAD   O  2  .    ? -8.641  17.248  108.539 0.32 17.27 ? 1301 FAD   B C5X   1 
HETATM 18363 C  C6    A FAD   O  2  .    ? -8.998  16.896  109.779 0.68 17.12 ? 1301 FAD   B C6    1 
HETATM 18364 C  C6    B FAD   O  2  .    ? -9.075  16.684  109.748 0.32 17.28 ? 1301 FAD   B C6    1 
HETATM 18365 C  C7    A FAD   O  2  .    ? -10.169 17.382  110.350 0.68 18.63 ? 1301 FAD   B C7    1 
HETATM 18366 C  C7    B FAD   O  2  .    ? -10.137 17.257  110.438 0.32 18.79 ? 1301 FAD   B C7    1 
HETATM 18367 C  C7M   A FAD   O  2  .    ? -10.567 16.937  111.732 0.68 20.47 ? 1301 FAD   B C7M   1 
HETATM 18368 C  C7M   B FAD   O  2  .    ? -10.596 16.635  111.730 0.32 19.90 ? 1301 FAD   B C7M   1 
HETATM 18369 C  C8    A FAD   O  2  .    ? -10.974 18.268  109.668 0.68 17.06 ? 1301 FAD   B C8    1 
HETATM 18370 C  C8    B FAD   O  2  .    ? -10.765 18.387  109.950 0.32 17.84 ? 1301 FAD   B C8    1 
HETATM 18371 C  C8M   A FAD   O  2  .    ? -12.230 18.796  110.279 0.68 18.62 ? 1301 FAD   B C8M   1 
HETATM 18372 C  C8M   B FAD   O  2  .    ? -11.903 19.019  110.684 0.32 19.75 ? 1301 FAD   B C8M   1 
HETATM 18373 C  C9    A FAD   O  2  .    ? -10.642 18.697  108.389 0.68 18.71 ? 1301 FAD   B C9    1 
HETATM 18374 C  C9    B FAD   O  2  .    ? -10.339 18.959  108.756 0.32 17.87 ? 1301 FAD   B C9    1 
HETATM 18375 C  C9A   A FAD   O  2  .    ? -9.489  18.220  107.810 0.68 17.66 ? 1301 FAD   B C9A   1 
HETATM 18376 C  C9A   B FAD   O  2  .    ? -9.285  18.387  108.061 0.32 17.37 ? 1301 FAD   B C9A   1 
HETATM 18377 N  N10   A FAD   O  2  .    ? -9.146  18.681  106.512 0.68 17.93 ? 1301 FAD   B N10   1 
HETATM 18378 N  N10   B FAD   O  2  .    ? -8.862  18.982  106.843 0.32 16.54 ? 1301 FAD   B N10   1 
HETATM 18379 C  C10   A FAD   O  2  .    ? -7.999  18.189  105.918 0.68 17.57 ? 1301 FAD   B C10   1 
HETATM 18380 C  C10   B FAD   O  2  .    ? -7.798  18.416  106.131 0.32 16.69 ? 1301 FAD   B C10   1 
HETATM 18381 C  "C1'" A FAD   O  2  .    ? -10.059 19.582  105.762 0.68 18.00 ? 1301 FAD   B "C1'" 1 
HETATM 18382 C  "C1'" B FAD   O  2  .    ? -9.538  20.186  106.334 0.32 18.88 ? 1301 FAD   B "C1'" 1 
HETATM 18383 C  "C2'" A FAD   O  2  .    ? -9.743  21.053  105.566 0.68 18.96 ? 1301 FAD   B "C2'" 1 
HETATM 18384 C  "C2'" B FAD   O  2  .    ? -10.694 19.748  105.451 0.32 18.96 ? 1301 FAD   B "C2'" 1 
HETATM 18385 O  "O2'" A FAD   O  2  .    ? -8.817  21.515  106.475 0.68 19.00 ? 1301 FAD   B "O2'" 1 
HETATM 18386 O  "O2'" B FAD   O  2  .    ? -10.199 19.061  104.372 0.32 18.32 ? 1301 FAD   B "O2'" 1 
HETATM 18387 C  "C3'" A FAD   O  2  .    ? -11.061 21.824  105.706 0.68 19.65 ? 1301 FAD   B "C3'" 1 
HETATM 18388 C  "C3'" B FAD   O  2  .    ? -11.496 20.954  104.963 0.32 20.17 ? 1301 FAD   B "C3'" 1 
HETATM 18389 O  "O3'" A FAD   O  2  .    ? -11.431 21.873  107.031 0.68 20.00 ? 1301 FAD   B "O3'" 1 
HETATM 18390 O  "O3'" B FAD   O  2  .    ? -10.620 21.819  104.350 0.32 18.82 ? 1301 FAD   B "O3'" 1 
HETATM 18391 C  "C4'" A FAD   O  2  .    ? -12.199 21.189  104.931 0.68 21.20 ? 1301 FAD   B "C4'" 1 
HETATM 18392 C  "C4'" B FAD   O  2  .    ? -12.264 21.710  106.035 0.32 20.41 ? 1301 FAD   B "C4'" 1 
HETATM 18393 O  "O4'" A FAD   O  2  .    ? -11.881 21.201  103.594 0.68 18.02 ? 1301 FAD   B "O4'" 1 
HETATM 18394 O  "O4'" B FAD   O  2  .    ? -12.656 20.856  107.042 0.32 20.36 ? 1301 FAD   B "O4'" 1 
HETATM 18395 C  "C5'" A FAD   O  2  .    ? -13.501 21.930  105.165 0.68 20.60 ? 1301 FAD   B "C5'" 1 
HETATM 18396 C  "C5'" B FAD   O  2  .    ? -13.446 22.476  105.436 0.32 20.29 ? 1301 FAD   B "C5'" 1 
HETATM 18397 O  "O5'" A FAD   O  2  .    ? -14.604 21.133  104.777 0.68 18.41 ? 1301 FAD   B "O5'" 1 
HETATM 18398 O  "O5'" B FAD   O  2  .    ? -14.470 21.617  104.966 0.32 18.99 ? 1301 FAD   B "O5'" 1 
HETATM 18399 P  P     A FAD   O  2  .    ? -15.961 21.355  105.602 0.68 20.22 ? 1301 FAD   B P     1 
HETATM 18400 P  P     B FAD   O  2  .    ? -15.854 21.539  105.773 0.32 22.82 ? 1301 FAD   B P     1 
HETATM 18401 O  O1P   A FAD   O  2  .    ? -15.742 21.349  107.161 0.68 21.22 ? 1301 FAD   B O1P   1 
HETATM 18402 O  O1P   B FAD   O  2  .    ? -15.749 21.306  107.327 0.32 21.86 ? 1301 FAD   B O1P   1 
HETATM 18403 O  O2P   A FAD   O  2  .    ? -16.959 20.335  104.965 0.68 25.58 ? 1301 FAD   B O2P   1 
HETATM 18404 O  O2P   B FAD   O  2  .    ? -16.598 20.449  104.930 0.32 23.44 ? 1301 FAD   B O2P   1 
HETATM 18405 O  O3P   A FAD   O  2  .    ? -16.480 22.775  105.027 0.68 22.04 ? 1301 FAD   B O3P   1 
HETATM 18406 O  O3P   B FAD   O  2  .    ? -16.666 22.841  105.262 0.32 22.53 ? 1301 FAD   B O3P   1 
HETATM 18407 C  C1    . PGE   P  9  .    ? 1.663   60.507  87.113  1.00 40.40 ? 1302 PGE   B C1    1 
HETATM 18408 O  O1    . PGE   P  9  .    ? 0.430   59.855  86.883  1.00 40.76 ? 1302 PGE   B O1    1 
HETATM 18409 C  C2    . PGE   P  9  .    ? 2.640   60.171  86.014  1.00 36.47 ? 1302 PGE   B C2    1 
HETATM 18410 O  O2    . PGE   P  9  .    ? 3.227   58.917  86.269  1.00 40.90 ? 1302 PGE   B O2    1 
HETATM 18411 C  C3    . PGE   P  9  .    ? 3.951   58.350  85.204  1.00 29.33 ? 1302 PGE   B C3    1 
HETATM 18412 C  C4    . PGE   P  9  .    ? 4.441   56.947  85.485  1.00 29.85 ? 1302 PGE   B C4    1 
HETATM 18413 O  O4    . PGE   P  9  .    ? 1.817   54.611  87.593  1.00 38.56 ? 1302 PGE   B O4    1 
HETATM 18414 C  C6    . PGE   P  9  .    ? 2.405   54.077  86.429  1.00 35.64 ? 1302 PGE   B C6    1 
HETATM 18415 C  C5    . PGE   P  9  .    ? 3.695   54.836  86.182  1.00 33.18 ? 1302 PGE   B C5    1 
HETATM 18416 O  O3    . PGE   P  9  .    ? 3.357   56.174  85.924  1.00 35.00 ? 1302 PGE   B O3    1 
HETATM 18417 C  C     . FMT   Q  4  .    ? -1.005  17.053  82.887  1.00 13.07 ? 1303 FMT   B C     1 
HETATM 18418 O  O1    . FMT   Q  4  .    ? -1.228  15.829  83.025  1.00 35.05 ? 1303 FMT   B O1    1 
HETATM 18419 O  O2    . FMT   Q  4  .    ? -1.421  17.846  82.036  1.00 30.28 ? 1303 FMT   B O2    1 
HETATM 18420 O  OH2   . 1PE   R  10 .    ? 42.180  35.141  84.157  1.00 26.08 ? 1304 1PE   B OH2   1 
HETATM 18421 C  C12   . 1PE   R  10 .    ? 42.005  33.992  83.360  1.00 30.74 ? 1304 1PE   B C12   1 
HETATM 18422 C  C22   . 1PE   R  10 .    ? 41.114  34.271  82.178  1.00 35.22 ? 1304 1PE   B C22   1 
HETATM 18423 O  OH3   . 1PE   R  10 .    ? 39.848  34.720  82.592  1.00 36.45 ? 1304 1PE   B OH3   1 
HETATM 18424 C  C13   . 1PE   R  10 .    ? 37.720  35.573  81.961  1.00 37.86 ? 1304 1PE   B C13   1 
HETATM 18425 C  C23   . 1PE   R  10 .    ? 39.123  35.258  81.515  1.00 34.87 ? 1304 1PE   B C23   1 
HETATM 18426 O  OH4   . 1PE   R  10 .    ? 37.718  36.655  82.858  1.00 39.67 ? 1304 1PE   B OH4   1 
HETATM 18427 C  C14   . 1PE   R  10 .    ? 36.358  38.354  83.910  1.00 36.38 ? 1304 1PE   B C14   1 
HETATM 18428 C  C24   . 1PE   R  10 .    ? 36.400  37.064  83.135  1.00 34.52 ? 1304 1PE   B C24   1 
HETATM 18429 O  OH5   . 1PE   R  10 .    ? 37.534  38.574  84.648  1.00 34.85 ? 1304 1PE   B OH5   1 
HETATM 18430 C  C15   . 1PE   R  10 .    ? 38.834  40.219  85.830  1.00 37.58 ? 1304 1PE   B C15   1 
HETATM 18431 C  C25   . 1PE   R  10 .    ? 37.723  39.955  84.852  1.00 33.41 ? 1304 1PE   B C25   1 
HETATM 18432 O  OH6   . 1PE   R  10 .    ? 40.029  39.649  85.359  1.00 34.30 ? 1304 1PE   B OH6   1 
HETATM 18433 C  C16   . 1PE   R  10 .    ? 42.194  39.466  86.324  1.00 31.56 ? 1304 1PE   B C16   1 
HETATM 18434 C  C26   . 1PE   R  10 .    ? 41.159  40.391  85.739  1.00 31.81 ? 1304 1PE   B C26   1 
HETATM 18435 O  OH7   . 1PE   R  10 .    ? 42.098  38.199  85.705  1.00 29.08 ? 1304 1PE   B OH7   1 
HETATM 18436 C  C     . FMT   S  4  .    ? 31.567  46.086  78.597  1.00 32.12 ? 1305 FMT   B C     1 
HETATM 18437 O  O1    . FMT   S  4  .    ? 32.268  46.302  77.591  1.00 40.72 ? 1305 FMT   B O1    1 
HETATM 18438 O  O2    . FMT   S  4  .    ? 30.347  46.284  78.761  1.00 36.08 ? 1305 FMT   B O2    1 
HETATM 18439 C  C1    . PEG   T  3  .    ? 15.634  66.761  54.055  1.00 45.33 ? 1306 PEG   B C1    1 
HETATM 18440 O  O1    . PEG   T  3  .    ? 15.886  67.075  55.412  1.00 30.35 ? 1306 PEG   B O1    1 
HETATM 18441 C  C2    . PEG   T  3  .    ? 14.547  65.723  53.899  1.00 37.46 ? 1306 PEG   B C2    1 
HETATM 18442 O  O2    . PEG   T  3  .    ? 15.101  64.445  53.696  1.00 47.24 ? 1306 PEG   B O2    1 
HETATM 18443 C  C3    . PEG   T  3  .    ? 14.249  63.408  54.115  1.00 41.77 ? 1306 PEG   B C3    1 
HETATM 18444 C  C4    . PEG   T  3  .    ? 14.914  62.067  53.930  1.00 37.45 ? 1306 PEG   B C4    1 
HETATM 18445 O  O4    . PEG   T  3  .    ? 16.161  62.063  54.583  1.00 44.47 ? 1306 PEG   B O4    1 
HETATM 18446 C  C1    . PEG   U  3  .    ? -5.518  31.773  68.009  1.00 38.64 ? 1307 PEG   B C1    1 
HETATM 18447 O  O1    . PEG   U  3  .    ? -6.342  32.603  67.218  1.00 44.47 ? 1307 PEG   B O1    1 
HETATM 18448 C  C2    . PEG   U  3  .    ? -5.837  31.981  69.466  1.00 32.57 ? 1307 PEG   B C2    1 
HETATM 18449 O  O2    . PEG   U  3  .    ? -6.986  31.250  69.819  1.00 41.13 ? 1307 PEG   B O2    1 
HETATM 18450 C  C3    . PEG   U  3  .    ? -6.857  30.628  71.071  1.00 34.72 ? 1307 PEG   B C3    1 
HETATM 18451 C  C4    . PEG   U  3  .    ? -7.920  31.126  72.017  1.00 35.49 ? 1307 PEG   B C4    1 
HETATM 18452 O  O4    . PEG   U  3  .    ? -9.174  30.614  71.627  1.00 42.38 ? 1307 PEG   B O4    1 
HETATM 18453 C  C1    . PEG   V  3  .    ? 13.040  33.548  78.333  1.00 32.71 ? 1308 PEG   B C1    1 
HETATM 18454 O  O1    . PEG   V  3  .    ? 13.321  34.852  78.796  1.00 28.38 ? 1308 PEG   B O1    1 
HETATM 18455 C  C2    . PEG   V  3  .    ? 13.258  32.539  79.435  1.00 35.04 ? 1308 PEG   B C2    1 
HETATM 18456 O  O2    . PEG   V  3  .    ? 12.647  31.322  79.082  1.00 40.29 ? 1308 PEG   B O2    1 
HETATM 18457 C  C3    . PEG   V  3  .    ? 13.368  30.174  79.464  1.00 26.88 ? 1308 PEG   B C3    1 
HETATM 18458 C  C4    . PEG   V  3  .    ? 12.813  29.611  80.748  1.00 36.65 ? 1308 PEG   B C4    1 
HETATM 18459 O  O4    . PEG   V  3  .    ? 11.416  29.789  80.773  1.00 41.58 ? 1308 PEG   B O4    1 
HETATM 18460 C  C     . FMT   W  4  .    ? 11.020  49.371  77.714  0.58 14.95 ? 1309 FMT   B C     1 
HETATM 18461 O  O1    . FMT   W  4  .    ? 11.867  49.637  78.607  0.58 18.82 ? 1309 FMT   B O1    1 
HETATM 18462 O  O2    . FMT   W  4  .    ? 11.102  49.308  76.457  0.58 18.85 ? 1309 FMT   B O2    1 
HETATM 18463 C  C02   . A1BDX X  5  .    ? -7.562  20.962  109.739 0.76 23.42 ? 1310 A1BDX B C02   1 
HETATM 18464 C  C03   . A1BDX X  5  .    ? -6.426  20.207  109.025 0.76 18.41 ? 1310 A1BDX B C03   1 
HETATM 18465 C  C04   . A1BDX X  5  .    ? -5.983  19.014  109.556 0.76 20.02 ? 1310 A1BDX B C04   1 
HETATM 18466 C  C05   . A1BDX X  5  .    ? -4.936  18.275  108.926 0.76 19.43 ? 1310 A1BDX B C05   1 
HETATM 18467 C  C06   . A1BDX X  5  .    ? -4.324  18.794  107.709 0.76 17.64 ? 1310 A1BDX B C06   1 
HETATM 18468 C  C08   . A1BDX X  5  .    ? -3.087  19.080  105.921 0.76 17.45 ? 1310 A1BDX B C08   1 
HETATM 18469 C  C09   . A1BDX X  5  .    ? -3.939  20.153  106.016 0.76 19.50 ? 1310 A1BDX B C09   1 
HETATM 18470 C  C10   . A1BDX X  5  .    ? -4.758  19.978  107.173 0.76 17.35 ? 1310 A1BDX B C10   1 
HETATM 18471 C  C11   . A1BDX X  5  .    ? -5.832  20.729  107.824 0.76 21.28 ? 1310 A1BDX B C11   1 
HETATM 18472 O  O01   . A1BDX X  5  .    ? -7.182  22.344  109.841 0.76 31.35 ? 1310 A1BDX B O01   1 
HETATM 18473 O  O07   . A1BDX X  5  .    ? -3.342  18.287  106.948 0.76 18.62 ? 1310 A1BDX B O07   1 
HETATM 18474 P  PA    . NAD   Y  6  .    ? 27.437  35.784  75.093  1.00 14.68 ? 1311 NAD   B PA    1 
HETATM 18475 O  O1A   . NAD   Y  6  .    ? 27.504  37.314  75.056  1.00 15.62 ? 1311 NAD   B O1A   1 
HETATM 18476 O  O2A   . NAD   Y  6  .    ? 28.653  35.025  75.402  1.00 17.02 ? 1311 NAD   B O2A   1 
HETATM 18477 O  O5B   . NAD   Y  6  .    ? 27.052  35.231  73.745  1.00 14.48 ? 1311 NAD   B O5B   1 
HETATM 18478 C  C5B   . NAD   Y  6  .    ? 25.797  35.580  73.182  1.00 14.84 ? 1311 NAD   B C5B   1 
HETATM 18479 C  C4B   . NAD   Y  6  .    ? 25.779  35.403  71.664  1.00 15.04 ? 1311 NAD   B C4B   1 
HETATM 18480 O  O4B   . NAD   Y  6  .    ? 26.553  36.395  71.025  1.00 13.87 ? 1311 NAD   B O4B   1 
HETATM 18481 C  C3B   . NAD   Y  6  .    ? 26.232  34.052  71.185  1.00 13.85 ? 1311 NAD   B C3B   1 
HETATM 18482 O  O3B   . NAD   Y  6  .    ? 25.478  33.638  70.095  1.00 13.49 ? 1311 NAD   B O3B   1 
HETATM 18483 C  C2B   . NAD   Y  6  .    ? 27.612  34.357  70.749  1.00 14.74 ? 1311 NAD   B C2B   1 
HETATM 18484 O  O2B   . NAD   Y  6  .    ? 28.172  33.491  69.820  1.00 15.01 ? 1311 NAD   B O2B   1 
HETATM 18485 C  C1B   . NAD   Y  6  .    ? 27.440  35.704  70.169  1.00 14.55 ? 1311 NAD   B C1B   1 
HETATM 18486 N  N9A   . NAD   Y  6  .    ? 28.652  36.469  70.054  1.00 15.28 ? 1311 NAD   B N9A   1 
HETATM 18487 C  C8A   . NAD   Y  6  .    ? 29.789  36.402  70.838  1.00 17.45 ? 1311 NAD   B C8A   1 
HETATM 18488 N  N7A   . NAD   Y  6  .    ? 30.645  37.339  70.404  1.00 17.40 ? 1311 NAD   B N7A   1 
HETATM 18489 C  C5A   . NAD   Y  6  .    ? 30.105  38.045  69.346  1.00 17.43 ? 1311 NAD   B C5A   1 
HETATM 18490 C  C6A   . NAD   Y  6  .    ? 30.484  39.101  68.537  1.00 17.81 ? 1311 NAD   B C6A   1 
HETATM 18491 N  N6A   . NAD   Y  6  .    ? 31.782  39.699  68.714  1.00 21.35 ? 1311 NAD   B N6A   1 
HETATM 18492 N  N1A   . NAD   Y  6  .    ? 29.677  39.573  67.592  1.00 17.74 ? 1311 NAD   B N1A   1 
HETATM 18493 C  C2A   . NAD   Y  6  .    ? 28.445  39.040  67.392  1.00 17.39 ? 1311 NAD   B C2A   1 
HETATM 18494 N  N3A   . NAD   Y  6  .    ? 28.038  38.005  68.159  1.00 15.43 ? 1311 NAD   B N3A   1 
HETATM 18495 C  C4A   . NAD   Y  6  .    ? 28.810  37.510  69.138  1.00 14.05 ? 1311 NAD   B C4A   1 
HETATM 18496 O  O3    . NAD   Y  6  .    ? 26.342  35.277  75.997  1.00 13.92 ? 1311 NAD   B O3    1 
HETATM 18497 P  PN    . NAD   Y  6  .    ? 25.975  33.840  76.567  1.00 14.83 ? 1311 NAD   B PN    1 
HETATM 18498 O  O1N   . NAD   Y  6  .    ? 27.093  33.324  77.428  1.00 17.33 ? 1311 NAD   B O1N   1 
HETATM 18499 O  O2N   . NAD   Y  6  .    ? 25.602  32.938  75.432  1.00 15.15 ? 1311 NAD   B O2N   1 
HETATM 18500 O  O5D   . NAD   Y  6  .    ? 24.691  34.095  77.430  1.00 15.63 ? 1311 NAD   B O5D   1 
HETATM 18501 C  C5D   . NAD   Y  6  .    ? 24.809  34.589  78.747  1.00 17.03 ? 1311 NAD   B C5D   1 
HETATM 18502 C  C4D   . NAD   Y  6  .    ? 24.601  36.094  78.808  1.00 15.00 ? 1311 NAD   B C4D   1 
HETATM 18503 O  O4D   . NAD   Y  6  .    ? 23.363  36.416  78.220  1.00 14.95 ? 1311 NAD   B O4D   1 
HETATM 18504 C  C3D   . NAD   Y  6  .    ? 24.595  36.646  80.205  1.00 14.18 ? 1311 NAD   B C3D   1 
HETATM 18505 O  O3D   . NAD   Y  6  .    ? 25.263  37.855  80.265  1.00 16.19 ? 1311 NAD   B O3D   1 
HETATM 18506 C  C2D   . NAD   Y  6  .    ? 23.145  36.823  80.447  1.00 14.95 ? 1311 NAD   B C2D   1 
HETATM 18507 O  O2D   . NAD   Y  6  .    ? 22.787  37.701  81.465  1.00 15.01 ? 1311 NAD   B O2D   1 
HETATM 18508 C  C1D   . NAD   Y  6  .    ? 22.664  37.250  79.095  1.00 14.08 ? 1311 NAD   B C1D   1 
HETATM 18509 N  N1N   . NAD   Y  6  .    ? 21.255  37.034  78.946  1.00 14.01 ? 1311 NAD   B N1N   1 
HETATM 18510 C  C2N   . NAD   Y  6  .    ? 20.377  38.140  78.959  1.00 13.28 ? 1311 NAD   B C2N   1 
HETATM 18511 C  C3N   . NAD   Y  6  .    ? 19.039  37.870  78.884  1.00 14.38 ? 1311 NAD   B C3N   1 
HETATM 18512 C  C7N   . NAD   Y  6  .    ? 18.045  38.960  78.879  1.00 15.21 ? 1311 NAD   B C7N   1 
HETATM 18513 O  O7N   . NAD   Y  6  .    ? 16.887  38.690  78.626  1.00 15.77 ? 1311 NAD   B O7N   1 
HETATM 18514 N  N7N   . NAD   Y  6  .    ? 18.414  40.280  79.209  1.00 14.55 ? 1311 NAD   B N7N   1 
HETATM 18515 C  C4N   . NAD   Y  6  .    ? 18.596  36.544  78.700  1.00 28.32 ? 1311 NAD   B C4N   1 
HETATM 18516 C  C5N   . NAD   Y  6  .    ? 19.471  35.442  78.763  1.00 16.97 ? 1311 NAD   B C5N   1 
HETATM 18517 C  C6N   . NAD   Y  6  .    ? 20.819  35.710  78.847  1.00 13.62 ? 1311 NAD   B C6N   1 
HETATM 18518 S  S     . SO4   Z  7  .    ? -7.304  47.553  73.031  1.00 16.39 ? 1312 SO4   B S     1 
HETATM 18519 O  O1    . SO4   Z  7  .    ? -6.110  46.769  72.582  1.00 19.83 ? 1312 SO4   B O1    1 
HETATM 18520 O  O2    . SO4   Z  7  .    ? -8.036  48.040  71.832  1.00 15.67 ? 1312 SO4   B O2    1 
HETATM 18521 O  O3    . SO4   Z  7  .    ? -8.196  46.684  73.822  1.00 20.00 ? 1312 SO4   B O3    1 
HETATM 18522 O  O4    . SO4   Z  7  .    ? -6.829  48.693  73.855  1.00 19.59 ? 1312 SO4   B O4    1 
HETATM 18523 S  S     . SO4   AA 7  .    ? 0.067   20.425  136.188 0.83 42.32 ? 1313 SO4   B S     1 
HETATM 18524 O  O1    . SO4   AA 7  .    ? 1.454   20.875  135.842 0.83 46.47 ? 1313 SO4   B O1    1 
HETATM 18525 O  O2    . SO4   AA 7  .    ? -0.363  19.340  135.251 0.83 42.31 ? 1313 SO4   B O2    1 
HETATM 18526 O  O3    . SO4   AA 7  .    ? 0.044   19.911  137.595 0.83 44.81 ? 1313 SO4   B O3    1 
HETATM 18527 O  O4    . SO4   AA 7  .    ? -0.861  21.595  136.066 0.83 43.17 ? 1313 SO4   B O4    1 
HETATM 18528 MG MG    . MG    BA 8  .    ? 30.108  33.628  75.134  0.62 18.11 ? 1314 MG    B MG    1 
HETATM 18529 O  O     . HOH   CA 11 .    ? 1.283   94.073  116.864 1.00 38.12 ? 1401 HOH   A O     1 
HETATM 18530 O  O     . HOH   CA 11 .    ? -1.414  88.752  105.343 1.00 18.86 ? 1402 HOH   A O     1 
HETATM 18531 O  O     . HOH   CA 11 .    ? -10.754 91.298  114.285 1.00 32.46 ? 1403 HOH   A O     1 
HETATM 18532 O  O     . HOH   CA 11 .    ? -39.393 37.726  64.377  1.00 39.79 ? 1404 HOH   A O     1 
HETATM 18533 O  O     . HOH   CA 11 .    ? -32.366 56.013  85.782  1.00 26.24 ? 1405 HOH   A O     1 
HETATM 18534 O  O     . HOH   CA 11 .    ? -19.572 72.624  97.426  1.00 24.09 ? 1406 HOH   A O     1 
HETATM 18535 O  O     . HOH   CA 11 .    ? -51.400 73.886  68.097  1.00 32.06 ? 1407 HOH   A O     1 
HETATM 18536 O  O     . HOH   CA 11 .    ? -32.265 79.647  99.026  1.00 28.82 ? 1408 HOH   A O     1 
HETATM 18537 O  O     . HOH   CA 11 .    ? -10.443 63.253  48.578  1.00 41.98 ? 1409 HOH   A O     1 
HETATM 18538 O  O     . HOH   CA 11 .    ? -3.187  81.869  114.601 1.00 34.36 ? 1410 HOH   A O     1 
HETATM 18539 O  O     . HOH   CA 11 .    ? -57.609 67.330  61.557  1.00 29.36 ? 1411 HOH   A O     1 
HETATM 18540 O  O     . HOH   CA 11 .    ? -33.462 71.617  76.664  1.00 36.55 ? 1412 HOH   A O     1 
HETATM 18541 O  O     . HOH   CA 11 .    ? -0.838  91.775  115.194 1.00 39.64 ? 1413 HOH   A O     1 
HETATM 18542 O  O     . HOH   CA 11 .    ? -0.651  79.693  81.702  1.00 38.20 ? 1414 HOH   A O     1 
HETATM 18543 O  O     . HOH   CA 11 .    ? 9.707   76.669  125.364 1.00 44.82 ? 1415 HOH   A O     1 
HETATM 18544 O  O     . HOH   CA 11 .    ? 4.732   80.733  129.147 1.00 38.30 ? 1416 HOH   A O     1 
HETATM 18545 O  O     . HOH   CA 11 .    ? -36.146 85.495  104.150 1.00 29.49 ? 1417 HOH   A O     1 
HETATM 18546 O  O     . HOH   CA 11 .    ? -0.265  67.103  86.224  1.00 35.28 ? 1418 HOH   A O     1 
HETATM 18547 O  O     . HOH   CA 11 .    ? -36.396 64.712  62.372  1.00 37.40 ? 1419 HOH   A O     1 
HETATM 18548 O  O     . HOH   CA 11 .    ? -57.331 49.385  57.938  1.00 42.14 ? 1420 HOH   A O     1 
HETATM 18549 O  O     . HOH   CA 11 .    ? -0.618  71.919  119.663 1.00 38.69 ? 1421 HOH   A O     1 
HETATM 18550 O  O     . HOH   CA 11 .    ? -37.974 49.145  76.664  1.00 29.79 ? 1422 HOH   A O     1 
HETATM 18551 O  O     . HOH   CA 11 .    ? -37.164 67.196  91.138  1.00 34.86 ? 1423 HOH   A O     1 
HETATM 18552 O  O     . HOH   CA 11 .    ? -15.561 93.036  130.975 1.00 40.74 ? 1424 HOH   A O     1 
HETATM 18553 O  O     . HOH   CA 11 .    ? 8.621   90.628  102.838 1.00 40.62 ? 1425 HOH   A O     1 
HETATM 18554 O  O     . HOH   CA 11 .    ? -38.574 62.747  55.393  1.00 36.08 ? 1426 HOH   A O     1 
HETATM 18555 O  O     . HOH   CA 11 .    ? -46.258 26.002  85.962  1.00 39.75 ? 1427 HOH   A O     1 
HETATM 18556 O  O     . HOH   CA 11 .    ? -55.336 75.403  91.964  1.00 40.14 ? 1428 HOH   A O     1 
HETATM 18557 O  O     . HOH   CA 11 .    ? -25.475 60.697  127.649 1.00 35.77 ? 1429 HOH   A O     1 
HETATM 18558 O  O     . HOH   CA 11 .    ? -52.555 61.188  101.700 1.00 26.31 ? 1430 HOH   A O     1 
HETATM 18559 O  O     . HOH   CA 11 .    ? -20.801 55.017  115.447 1.00 36.54 ? 1431 HOH   A O     1 
HETATM 18560 O  O     . HOH   CA 11 .    ? -21.906 95.417  120.684 1.00 36.74 ? 1432 HOH   A O     1 
HETATM 18561 O  O     . HOH   CA 11 .    ? -43.267 80.537  89.650  1.00 29.56 ? 1433 HOH   A O     1 
HETATM 18562 O  O     . HOH   CA 11 .    ? -29.033 38.136  84.870  1.00 45.10 ? 1434 HOH   A O     1 
HETATM 18563 O  O     . HOH   CA 11 .    ? -0.600  63.688  109.648 1.00 22.36 ? 1435 HOH   A O     1 
HETATM 18564 O  O     . HOH   CA 11 .    ? -25.530 74.846  104.291 1.00 37.81 ? 1436 HOH   A O     1 
HETATM 18565 O  O     . HOH   CA 11 .    ? 21.547  68.066  116.211 1.00 30.92 ? 1437 HOH   A O     1 
HETATM 18566 O  O     . HOH   CA 11 .    ? -66.987 72.486  75.076  1.00 27.79 ? 1438 HOH   A O     1 
HETATM 18567 O  O     . HOH   CA 11 .    ? -21.582 66.296  69.992  1.00 46.83 ? 1439 HOH   A O     1 
HETATM 18568 O  O     . HOH   CA 11 .    ? -0.096  82.286  113.277 1.00 35.84 ? 1440 HOH   A O     1 
HETATM 18569 O  O     . HOH   CA 11 .    ? 4.563   74.453  119.835 1.00 39.04 ? 1441 HOH   A O     1 
HETATM 18570 O  O     . HOH   CA 11 .    ? -17.811 58.963  86.234  1.00 30.51 ? 1442 HOH   A O     1 
HETATM 18571 O  O     . HOH   CA 11 .    ? -54.998 33.709  71.269  1.00 33.24 ? 1443 HOH   A O     1 
HETATM 18572 O  O     . HOH   CA 11 .    ? -24.462 92.667  126.655 1.00 30.40 ? 1444 HOH   A O     1 
HETATM 18573 O  O     . HOH   CA 11 .    ? -38.885 67.209  69.247  1.00 32.41 ? 1445 HOH   A O     1 
HETATM 18574 O  O     . HOH   CA 11 .    ? -12.643 87.593  98.967  1.00 35.02 ? 1446 HOH   A O     1 
HETATM 18575 O  O     . HOH   CA 11 .    ? -17.206 80.431  67.770  1.00 41.65 ? 1447 HOH   A O     1 
HETATM 18576 O  O     . HOH   CA 11 .    ? 17.429  78.358  119.620 1.00 33.38 ? 1448 HOH   A O     1 
HETATM 18577 O  O     . HOH   CA 11 .    ? -43.414 33.432  102.247 1.00 35.75 ? 1449 HOH   A O     1 
HETATM 18578 O  O     . HOH   CA 11 .    ? -5.178  71.807  95.532  1.00 36.67 ? 1450 HOH   A O     1 
HETATM 18579 O  O     . HOH   CA 11 .    ? -35.801 56.235  77.846  1.00 38.40 ? 1451 HOH   A O     1 
HETATM 18580 O  O     . HOH   CA 11 .    ? -29.249 57.633  115.340 1.00 36.24 ? 1452 HOH   A O     1 
HETATM 18581 O  O     . HOH   CA 11 .    ? -14.344 61.485  107.466 1.00 24.96 ? 1453 HOH   A O     1 
HETATM 18582 O  O     . HOH   CA 11 .    ? -33.391 52.980  108.461 1.00 40.23 ? 1454 HOH   A O     1 
HETATM 18583 O  O     . HOH   CA 11 .    ? -11.938 68.635  76.431  1.00 25.69 ? 1455 HOH   A O     1 
HETATM 18584 O  O     . HOH   CA 11 .    ? -37.646 94.275  119.717 1.00 42.47 ? 1456 HOH   A O     1 
HETATM 18585 O  O     . HOH   CA 11 .    ? -44.865 30.287  96.155  1.00 40.53 ? 1457 HOH   A O     1 
HETATM 18586 O  O     . HOH   CA 11 .    ? -40.404 96.640  109.363 1.00 37.27 ? 1458 HOH   A O     1 
HETATM 18587 O  O     . HOH   CA 11 .    ? -25.237 66.921  86.494  1.00 30.24 ? 1459 HOH   A O     1 
HETATM 18588 O  O     . HOH   CA 11 .    ? -26.932 63.882  71.273  1.00 40.16 ? 1460 HOH   A O     1 
HETATM 18589 O  O     . HOH   CA 11 .    ? -4.123  79.202  103.680 1.00 21.82 ? 1461 HOH   A O     1 
HETATM 18590 O  O     . HOH   CA 11 .    ? 12.268  73.977  91.463  1.00 34.58 ? 1462 HOH   A O     1 
HETATM 18591 O  O     . HOH   CA 11 .    ? -1.265  50.265  57.786  1.00 26.51 ? 1463 HOH   A O     1 
HETATM 18592 O  O     . HOH   CA 11 .    ? -32.560 96.089  125.343 1.00 42.35 ? 1464 HOH   A O     1 
HETATM 18593 O  O     . HOH   CA 11 .    ? -38.676 38.161  87.495  1.00 35.57 ? 1465 HOH   A O     1 
HETATM 18594 O  O     . HOH   CA 11 .    ? -23.295 56.829  83.789  1.00 33.59 ? 1466 HOH   A O     1 
HETATM 18595 O  O     . HOH   CA 11 .    ? -14.457 75.728  109.817 1.00 20.47 ? 1467 HOH   A O     1 
HETATM 18596 O  O     . HOH   CA 11 .    ? -18.906 54.273  94.466  1.00 38.64 ? 1468 HOH   A O     1 
HETATM 18597 O  O     . HOH   CA 11 .    ? -24.913 65.193  94.496  1.00 31.23 ? 1469 HOH   A O     1 
HETATM 18598 O  O     . HOH   CA 11 .    ? -52.555 24.544  82.363  1.00 39.15 ? 1470 HOH   A O     1 
HETATM 18599 O  O     . HOH   CA 11 .    ? -41.350 63.188  73.517  1.00 28.38 ? 1471 HOH   A O     1 
HETATM 18600 O  O     . HOH   CA 11 .    ? -55.191 76.259  83.349  1.00 34.73 ? 1472 HOH   A O     1 
HETATM 18601 O  O     . HOH   CA 11 .    ? -21.611 47.243  57.942  1.00 31.46 ? 1473 HOH   A O     1 
HETATM 18602 O  O     . HOH   CA 11 .    ? -2.214  54.653  97.734  1.00 40.23 ? 1474 HOH   A O     1 
HETATM 18603 O  O     . HOH   CA 11 .    ? -48.486 54.621  61.131  1.00 24.91 ? 1475 HOH   A O     1 
HETATM 18604 O  O     . HOH   CA 11 .    ? 8.107   89.640  120.056 1.00 27.65 ? 1476 HOH   A O     1 
HETATM 18605 O  O     . HOH   CA 11 .    ? 25.331  79.942  107.136 1.00 31.55 ? 1477 HOH   A O     1 
HETATM 18606 O  O     . HOH   CA 11 .    ? 8.179   92.673  98.554  1.00 43.48 ? 1478 HOH   A O     1 
HETATM 18607 O  O     . HOH   CA 11 .    ? 9.240   79.165  121.847 1.00 32.22 ? 1479 HOH   A O     1 
HETATM 18608 O  O     . HOH   CA 11 .    ? -29.030 93.897  82.008  1.00 37.07 ? 1480 HOH   A O     1 
HETATM 18609 O  O     . HOH   CA 11 .    ? -50.295 32.747  91.511  1.00 37.13 ? 1481 HOH   A O     1 
HETATM 18610 O  O     . HOH   CA 11 .    ? -10.427 81.105  91.063  1.00 22.25 ? 1482 HOH   A O     1 
HETATM 18611 O  O     . HOH   CA 11 .    ? -6.377  68.529  92.320  1.00 29.14 ? 1483 HOH   A O     1 
HETATM 18612 O  O     . HOH   CA 11 .    ? -32.077 86.674  76.470  1.00 34.42 ? 1484 HOH   A O     1 
HETATM 18613 O  O     . HOH   CA 11 .    ? -47.229 75.629  66.852  1.00 33.39 ? 1485 HOH   A O     1 
HETATM 18614 O  O     . HOH   CA 11 .    ? 23.154  69.564  113.038 1.00 34.48 ? 1486 HOH   A O     1 
HETATM 18615 O  O     . HOH   CA 11 .    ? -4.899  43.586  57.813  1.00 33.67 ? 1487 HOH   A O     1 
HETATM 18616 O  O     . HOH   CA 11 .    ? -0.028  59.309  108.555 1.00 30.39 ? 1488 HOH   A O     1 
HETATM 18617 O  O     . HOH   CA 11 .    ? -68.638 56.630  82.603  1.00 29.35 ? 1489 HOH   A O     1 
HETATM 18618 O  O     . HOH   CA 11 .    ? 7.629   91.263  113.353 1.00 33.63 ? 1490 HOH   A O     1 
HETATM 18619 O  O     . HOH   CA 11 .    ? -31.527 58.433  115.436 1.00 41.21 ? 1491 HOH   A O     1 
HETATM 18620 O  O     . HOH   CA 11 .    ? 9.062   81.280  96.447  1.00 41.86 ? 1492 HOH   A O     1 
HETATM 18621 O  O     . HOH   CA 11 .    ? 4.122   73.611  116.157 1.00 27.69 ? 1493 HOH   A O     1 
HETATM 18622 O  O     . HOH   CA 11 .    ? -42.586 38.841  84.796  1.00 27.21 ? 1494 HOH   A O     1 
HETATM 18623 O  O     . HOH   CA 11 .    ? 14.386  61.051  94.481  1.00 27.74 ? 1495 HOH   A O     1 
HETATM 18624 O  O     . HOH   CA 11 .    ? -36.139 93.918  87.239  1.00 42.16 ? 1496 HOH   A O     1 
HETATM 18625 O  O     . HOH   CA 11 .    ? -55.047 56.571  64.630  1.00 17.43 ? 1497 HOH   A O     1 
HETATM 18626 O  O     . HOH   CA 11 .    ? -9.210  45.160  55.741  1.00 31.60 ? 1498 HOH   A O     1 
HETATM 18627 O  O     . HOH   CA 11 .    ? 14.110  86.738  110.068 1.00 31.31 ? 1499 HOH   A O     1 
HETATM 18628 O  O     . HOH   CA 11 .    ? -31.388 90.212  127.760 1.00 42.94 ? 1500 HOH   A O     1 
HETATM 18629 O  O     . HOH   CA 11 .    ? -36.162 52.025  69.224  1.00 36.08 ? 1501 HOH   A O     1 
HETATM 18630 O  O     . HOH   CA 11 .    ? -6.748  58.486  119.823 1.00 21.45 ? 1502 HOH   A O     1 
HETATM 18631 O  O     . HOH   CA 11 .    ? -33.717 93.310  86.016  1.00 35.52 ? 1503 HOH   A O     1 
HETATM 18632 O  O     . HOH   CA 11 .    ? -62.832 43.814  82.095  1.00 30.91 ? 1504 HOH   A O     1 
HETATM 18633 O  O     . HOH   CA 11 .    ? -13.948 74.323  105.894 1.00 20.73 ? 1505 HOH   A O     1 
HETATM 18634 O  O     . HOH   CA 11 .    ? -16.877 55.737  112.164 1.00 31.36 ? 1506 HOH   A O     1 
HETATM 18635 O  O     . HOH   CA 11 .    ? -10.830 49.376  49.911  1.00 41.25 ? 1507 HOH   A O     1 
HETATM 18636 O  O     . HOH   CA 11 .    ? -39.050 77.585  97.089  1.00 21.60 ? 1508 HOH   A O     1 
HETATM 18637 O  O     . HOH   CA 11 .    ? -65.331 47.944  85.441  1.00 35.32 ? 1509 HOH   A O     1 
HETATM 18638 O  O     . HOH   CA 11 .    ? -34.018 97.501  97.980  1.00 40.23 ? 1510 HOH   A O     1 
HETATM 18639 O  O     . HOH   CA 11 .    ? -49.342 66.699  93.899  1.00 20.05 ? 1511 HOH   A O     1 
HETATM 18640 O  O     . HOH   CA 11 .    ? -13.391 55.491  81.332  1.00 30.12 ? 1512 HOH   A O     1 
HETATM 18641 O  O     . HOH   CA 11 .    ? -37.876 62.404  81.412  1.00 25.36 ? 1513 HOH   A O     1 
HETATM 18642 O  O     . HOH   CA 11 .    ? -3.777  70.332  117.360 1.00 23.94 ? 1514 HOH   A O     1 
HETATM 18643 O  O     . HOH   CA 11 .    ? -23.134 80.392  110.108 1.00 26.87 ? 1515 HOH   A O     1 
HETATM 18644 O  O     . HOH   CA 11 .    ? -5.957  70.493  72.786  1.00 40.86 ? 1516 HOH   A O     1 
HETATM 18645 O  O     . HOH   CA 11 .    ? -11.770 63.215  113.061 1.00 18.26 ? 1517 HOH   A O     1 
HETATM 18646 O  O     . HOH   CA 11 .    ? -14.875 64.003  99.262  1.00 22.94 ? 1518 HOH   A O     1 
HETATM 18647 O  O     . HOH   CA 11 .    ? -11.981 73.008  128.331 1.00 28.26 ? 1519 HOH   A O     1 
HETATM 18648 O  O     . HOH   CA 11 .    ? -49.761 33.489  99.996  1.00 43.84 ? 1520 HOH   A O     1 
HETATM 18649 O  O     . HOH   CA 11 .    ? -48.874 33.541  89.282  1.00 36.74 ? 1521 HOH   A O     1 
HETATM 18650 O  O     . HOH   CA 11 .    ? -50.677 52.123  63.783  1.00 20.79 ? 1522 HOH   A O     1 
HETATM 18651 O  O     . HOH   CA 11 .    ? -33.510 61.112  114.216 1.00 40.26 ? 1523 HOH   A O     1 
HETATM 18652 O  O     . HOH   CA 11 .    ? -46.862 59.689  101.854 1.00 22.12 ? 1524 HOH   A O     1 
HETATM 18653 O  O     . HOH   CA 11 .    ? 20.861  57.419  105.009 1.00 32.13 ? 1525 HOH   A O     1 
HETATM 18654 O  O     . HOH   CA 11 .    ? -47.094 35.125  86.793  1.00 29.16 ? 1526 HOH   A O     1 
HETATM 18655 O  O     . HOH   CA 11 .    ? -44.129 62.316  69.978  1.00 23.79 ? 1527 HOH   A O     1 
HETATM 18656 O  O     . HOH   CA 11 .    ? -31.051 67.103  98.437  1.00 36.87 ? 1528 HOH   A O     1 
HETATM 18657 O  O     . HOH   CA 11 .    ? -33.370 70.805  81.246  1.00 37.19 ? 1529 HOH   A O     1 
HETATM 18658 O  O     . HOH   CA 11 .    ? -0.360  92.940  104.558 1.00 25.46 ? 1530 HOH   A O     1 
HETATM 18659 O  O     . HOH   CA 11 .    ? -38.726 65.266  96.429  1.00 27.35 ? 1531 HOH   A O     1 
HETATM 18660 O  O     . HOH   CA 11 .    ? -35.448 76.315  92.069  1.00 33.55 ? 1532 HOH   A O     1 
HETATM 18661 O  O     . HOH   CA 11 .    ? -20.596 88.897  102.581 1.00 40.76 ? 1533 HOH   A O     1 
HETATM 18662 O  O     . HOH   CA 11 .    ? -39.043 27.656  86.354  1.00 38.82 ? 1534 HOH   A O     1 
HETATM 18663 O  O     . HOH   CA 11 .    ? -43.105 48.437  59.956  1.00 26.64 ? 1535 HOH   A O     1 
HETATM 18664 O  O     . HOH   CA 11 .    ? -58.536 38.227  76.088  1.00 30.63 ? 1536 HOH   A O     1 
HETATM 18665 O  O     . HOH   CA 11 .    ? -5.764  53.599  110.622 1.00 16.19 ? 1537 HOH   A O     1 
HETATM 18666 O  O     . HOH   CA 11 .    ? 6.070   90.723  106.455 1.00 31.04 ? 1538 HOH   A O     1 
HETATM 18667 O  O     . HOH   CA 11 .    ? -18.475 79.322  127.168 1.00 23.51 ? 1539 HOH   A O     1 
HETATM 18668 O  O     . HOH   CA 11 .    ? -43.664 75.356  113.886 1.00 26.85 ? 1540 HOH   A O     1 
HETATM 18669 O  O     . HOH   CA 11 .    ? -14.706 48.713  75.758  1.00 30.69 ? 1541 HOH   A O     1 
HETATM 18670 O  O     . HOH   CA 11 .    ? -27.900 78.751  101.088 1.00 28.90 ? 1542 HOH   A O     1 
HETATM 18671 O  O     . HOH   CA 11 .    ? -22.173 54.528  86.122  1.00 35.18 ? 1543 HOH   A O     1 
HETATM 18672 O  O     . HOH   CA 11 .    ? -28.714 57.157  59.916  1.00 33.23 ? 1544 HOH   A O     1 
HETATM 18673 O  O     . HOH   CA 11 .    ? -13.432 59.245  122.359 1.00 26.19 ? 1545 HOH   A O     1 
HETATM 18674 O  O     . HOH   CA 11 .    ? -23.411 63.832  97.724  1.00 20.00 ? 1546 HOH   A O     1 
HETATM 18675 O  O     . HOH   CA 11 .    ? -39.365 61.268  74.388  1.00 31.54 ? 1547 HOH   A O     1 
HETATM 18676 O  O     . HOH   CA 11 .    ? -28.999 75.147  101.669 1.00 29.18 ? 1548 HOH   A O     1 
HETATM 18677 O  O     . HOH   CA 11 .    ? -10.724 49.569  109.847 1.00 21.67 ? 1549 HOH   A O     1 
HETATM 18678 O  O     . HOH   CA 11 .    ? -36.764 61.585  74.813  1.00 32.25 ? 1550 HOH   A O     1 
HETATM 18679 O  O     . HOH   CA 11 .    ? -51.964 47.534  68.820  1.00 28.21 ? 1551 HOH   A O     1 
HETATM 18680 O  O     . HOH   CA 11 .    ? -41.465 85.705  113.639 1.00 28.88 ? 1552 HOH   A O     1 
HETATM 18681 O  O     . HOH   CA 11 .    ? -4.924  70.250  76.391  1.00 33.90 ? 1553 HOH   A O     1 
HETATM 18682 O  O     . HOH   CA 11 .    ? -63.746 73.433  78.234  1.00 32.70 ? 1554 HOH   A O     1 
HETATM 18683 O  O     . HOH   CA 11 .    ? -21.241 55.112  94.692  1.00 32.16 ? 1555 HOH   A O     1 
HETATM 18684 O  O     . HOH   CA 11 .    ? -15.372 55.359  121.432 1.00 32.15 ? 1556 HOH   A O     1 
HETATM 18685 O  O     . HOH   CA 11 .    ? -23.875 83.044  111.834 1.00 20.76 ? 1557 HOH   A O     1 
HETATM 18686 O  O     . HOH   CA 11 .    ? -60.537 59.674  90.320  1.00 19.19 ? 1558 HOH   A O     1 
HETATM 18687 O  O     . HOH   CA 11 .    ? -6.468  54.734  105.065 1.00 31.04 ? 1559 HOH   A O     1 
HETATM 18688 O  O     . HOH   CA 11 .    ? 0.242   85.411  102.853 1.00 22.51 ? 1560 HOH   A O     1 
HETATM 18689 O  O     . HOH   CA 11 .    ? -37.492 64.097  66.854  1.00 28.72 ? 1561 HOH   A O     1 
HETATM 18690 O  O     . HOH   CA 11 .    ? -19.973 54.959  106.848 1.00 30.59 ? 1562 HOH   A O     1 
HETATM 18691 O  O     . HOH   CA 11 .    ? -0.604  60.026  94.776  1.00 36.69 ? 1563 HOH   A O     1 
HETATM 18692 O  O     . HOH   CA 11 .    ? -33.203 92.123  107.017 1.00 32.23 ? 1564 HOH   A O     1 
HETATM 18693 O  O     . HOH   CA 11 .    ? -44.947 63.554  84.150  1.00 17.11 ? 1565 HOH   A O     1 
HETATM 18694 O  O     . HOH   CA 11 .    ? -42.564 60.902  74.016  1.00 33.44 ? 1566 HOH   A O     1 
HETATM 18695 O  O     . HOH   CA 11 .    ? -25.934 61.908  75.871  1.00 34.82 ? 1567 HOH   A O     1 
HETATM 18696 O  O     . HOH   CA 11 .    ? -18.956 59.108  104.163 1.00 23.87 ? 1568 HOH   A O     1 
HETATM 18697 O  O     . HOH   CA 11 .    ? -61.922 57.530  63.546  1.00 28.66 ? 1569 HOH   A O     1 
HETATM 18698 O  O     . HOH   CA 11 .    ? -37.267 85.114  85.537  1.00 34.09 ? 1570 HOH   A O     1 
HETATM 18699 O  O     . HOH   CA 11 .    ? -11.923 71.832  76.556  1.00 31.51 ? 1571 HOH   A O     1 
HETATM 18700 O  O     . HOH   CA 11 .    ? -27.954 61.102  84.275  1.00 35.53 ? 1572 HOH   A O     1 
HETATM 18701 O  O     . HOH   CA 11 .    ? -32.555 79.383  96.267  1.00 29.16 ? 1573 HOH   A O     1 
HETATM 18702 O  O     . HOH   CA 11 .    ? -59.309 75.959  77.135  1.00 35.01 ? 1574 HOH   A O     1 
HETATM 18703 O  O     . HOH   CA 11 .    ? -7.272  50.391  76.574  1.00 25.88 ? 1575 HOH   A O     1 
HETATM 18704 O  O     . HOH   CA 11 .    ? 6.845   54.094  101.246 1.00 18.32 ? 1576 HOH   A O     1 
HETATM 18705 O  O     . HOH   CA 11 .    ? -56.569 38.793  63.686  1.00 43.29 ? 1577 HOH   A O     1 
HETATM 18706 O  O     . HOH   CA 11 .    ? -21.672 90.318  106.162 1.00 28.75 ? 1578 HOH   A O     1 
HETATM 18707 O  O     . HOH   CA 11 .    ? -60.344 51.128  62.034  1.00 33.58 ? 1579 HOH   A O     1 
HETATM 18708 O  O     . HOH   CA 11 .    ? -57.881 28.183  85.569  1.00 35.29 ? 1580 HOH   A O     1 
HETATM 18709 O  O     . HOH   CA 11 .    ? 20.489  58.450  110.863 1.00 30.43 ? 1581 HOH   A O     1 
HETATM 18710 O  O     . HOH   CA 11 .    ? 20.395  83.367  101.001 1.00 38.57 ? 1582 HOH   A O     1 
HETATM 18711 O  O     . HOH   CA 11 .    ? 13.815  87.029  98.422  1.00 38.74 ? 1583 HOH   A O     1 
HETATM 18712 O  O     . HOH   CA 11 .    ? -32.754 92.032  126.014 1.00 39.31 ? 1584 HOH   A O     1 
HETATM 18713 O  O     . HOH   CA 11 .    ? -25.961 70.038  131.033 1.00 37.56 ? 1585 HOH   A O     1 
HETATM 18714 O  O     . HOH   CA 11 .    ? -61.271 55.531  67.401  1.00 18.70 ? 1586 HOH   A O     1 
HETATM 18715 O  O     . HOH   CA 11 .    ? 11.789  81.814  97.889  1.00 37.97 ? 1587 HOH   A O     1 
HETATM 18716 O  O     . HOH   CA 11 .    ? -36.785 64.556  82.800  1.00 33.16 ? 1588 HOH   A O     1 
HETATM 18717 O  O     . HOH   CA 11 .    ? -1.376  77.944  114.357 1.00 24.89 ? 1589 HOH   A O     1 
HETATM 18718 O  O     . HOH   CA 11 .    ? -55.773 36.779  76.096  1.00 29.00 ? 1590 HOH   A O     1 
HETATM 18719 O  O     . HOH   CA 11 .    ? -12.976 93.766  130.427 1.00 47.15 ? 1591 HOH   A O     1 
HETATM 18720 O  O     . HOH   CA 11 .    ? -16.723 76.409  108.441 1.00 19.90 ? 1592 HOH   A O     1 
HETATM 18721 O  O     . HOH   CA 11 .    ? -23.206 60.426  115.621 1.00 21.31 ? 1593 HOH   A O     1 
HETATM 18722 O  O     . HOH   CA 11 .    ? -24.406 59.575  121.348 1.00 35.98 ? 1594 HOH   A O     1 
HETATM 18723 O  O     . HOH   CA 11 .    ? -12.527 77.023  102.999 1.00 17.74 ? 1595 HOH   A O     1 
HETATM 18724 O  O     . HOH   CA 11 .    ? -32.635 82.215  97.775  1.00 27.70 ? 1596 HOH   A O     1 
HETATM 18725 O  O     . HOH   CA 11 .    ? -2.458  74.468  84.256  1.00 31.03 ? 1597 HOH   A O     1 
HETATM 18726 O  O     . HOH   CA 11 .    ? -40.018 57.274  87.854  1.00 15.96 ? 1598 HOH   A O     1 
HETATM 18727 O  O     . HOH   CA 11 .    ? -3.468  57.475  68.009  1.00 32.08 ? 1599 HOH   A O     1 
HETATM 18728 O  O     . HOH   CA 11 .    ? -16.647 60.176  46.828  1.00 42.82 ? 1600 HOH   A O     1 
HETATM 18729 O  O     . HOH   CA 11 .    ? -10.787 69.087  133.390 1.00 34.21 ? 1601 HOH   A O     1 
HETATM 18730 O  O     . HOH   CA 11 .    ? -23.060 67.044  97.316  1.00 22.16 ? 1602 HOH   A O     1 
HETATM 18731 O  O     . HOH   CA 11 .    ? -8.387  59.970  94.058  1.00 35.45 ? 1603 HOH   A O     1 
HETATM 18732 O  O     . HOH   CA 11 .    ? -52.430 48.870  62.659  1.00 33.96 ? 1604 HOH   A O     1 
HETATM 18733 O  O     . HOH   CA 11 .    ? -44.809 63.364  81.315  1.00 15.01 ? 1605 HOH   A O     1 
HETATM 18734 O  O     . HOH   CA 11 .    ? -48.525 81.218  84.860  1.00 33.83 ? 1606 HOH   A O     1 
HETATM 18735 O  O     . HOH   CA 11 .    ? -24.005 63.459  91.560  1.00 20.94 ? 1607 HOH   A O     1 
HETATM 18736 O  O     . HOH   CA 11 .    ? -17.756 72.720  111.096 1.00 18.61 ? 1608 HOH   A O     1 
HETATM 18737 O  O     . HOH   CA 11 .    ? -45.494 89.205  106.032 1.00 31.97 ? 1609 HOH   A O     1 
HETATM 18738 O  O     . HOH   CA 11 .    ? -25.485 95.858  123.605 1.00 34.22 ? 1610 HOH   A O     1 
HETATM 18739 O  O     . HOH   CA 11 .    ? -38.128 62.299  105.203 1.00 34.21 ? 1611 HOH   A O     1 
HETATM 18740 O  O     . HOH   CA 11 .    ? 2.003   85.674  117.957 1.00 26.00 ? 1612 HOH   A O     1 
HETATM 18741 O  O     . HOH   CA 11 .    ? 17.863  58.875  95.562  1.00 28.23 ? 1613 HOH   A O     1 
HETATM 18742 O  O     . HOH   CA 11 .    ? -50.778 50.531  57.266  1.00 34.53 ? 1614 HOH   A O     1 
HETATM 18743 O  O     . HOH   CA 11 .    ? -9.663  64.924  76.294  1.00 21.11 ? 1615 HOH   A O     1 
HETATM 18744 O  O     . HOH   CA 11 .    ? -4.308  70.037  106.646 1.00 29.50 ? 1616 HOH   A O     1 
HETATM 18745 O  O     . HOH   CA 11 .    ? -19.992 59.608  78.957  1.00 29.91 ? 1617 HOH   A O     1 
HETATM 18746 O  O     . HOH   CA 11 .    ? -17.404 86.710  92.020  1.00 22.62 ? 1618 HOH   A O     1 
HETATM 18747 O  O     . HOH   CA 11 .    ? -31.500 60.123  105.299 1.00 24.45 ? 1619 HOH   A O     1 
HETATM 18748 O  O     . HOH   CA 11 .    ? -59.766 40.118  78.769  1.00 36.68 ? 1620 HOH   A O     1 
HETATM 18749 O  O     . HOH   CA 11 .    ? -51.512 55.262  75.710  1.00 16.64 ? 1621 HOH   A O     1 
HETATM 18750 O  O     . HOH   CA 11 .    ? -45.136 79.935  79.221  1.00 36.29 ? 1622 HOH   A O     1 
HETATM 18751 O  O     . HOH   CA 11 .    ? -8.655  80.494  74.564  1.00 28.95 ? 1623 HOH   A O     1 
HETATM 18752 O  O     . HOH   CA 11 .    ? -5.581  77.649  94.854  1.00 24.95 ? 1624 HOH   A O     1 
HETATM 18753 O  O     . HOH   CA 11 .    ? -16.190 91.400  104.259 1.00 33.08 ? 1625 HOH   A O     1 
HETATM 18754 O  O     . HOH   CA 11 .    ? -50.712 69.758  100.202 1.00 21.00 ? 1626 HOH   A O     1 
HETATM 18755 O  O     . HOH   CA 11 .    ? -70.174 61.159  84.960  1.00 35.02 ? 1627 HOH   A O     1 
HETATM 18756 O  O     . HOH   CA 11 .    ? -27.195 53.866  109.477 1.00 27.23 ? 1628 HOH   A O     1 
HETATM 18757 O  O     . HOH   CA 11 .    ? -34.302 69.431  76.092  1.00 27.75 ? 1629 HOH   A O     1 
HETATM 18758 O  O     . HOH   CA 11 .    ? -37.073 80.513  78.849  1.00 19.74 ? 1630 HOH   A O     1 
HETATM 18759 O  O     . HOH   CA 11 .    ? -61.904 58.223  70.020  1.00 18.91 ? 1631 HOH   A O     1 
HETATM 18760 O  O     . HOH   CA 11 .    ? -33.621 52.619  81.945  1.00 32.28 ? 1632 HOH   A O     1 
HETATM 18761 O  O     . HOH   CA 11 .    ? -20.506 54.968  91.070  1.00 37.80 ? 1633 HOH   A O     1 
HETATM 18762 O  O     . HOH   CA 11 .    ? -35.868 39.736  84.141  1.00 35.07 ? 1634 HOH   A O     1 
HETATM 18763 O  O     . HOH   CA 11 .    ? -39.198 52.721  105.236 1.00 36.00 ? 1635 HOH   A O     1 
HETATM 18764 O  O     . HOH   CA 11 .    ? -35.051 64.985  66.146  1.00 30.29 ? 1636 HOH   A O     1 
HETATM 18765 O  O     . HOH   CA 11 .    ? 0.277   85.099  111.548 1.00 28.17 ? 1637 HOH   A O     1 
HETATM 18766 O  O     . HOH   CA 11 .    ? -45.953 76.071  94.197  1.00 25.37 ? 1638 HOH   A O     1 
HETATM 18767 O  O     . HOH   CA 11 .    ? -11.283 92.179  123.956 1.00 36.07 ? 1639 HOH   A O     1 
HETATM 18768 O  O     . HOH   CA 11 .    ? -39.345 35.504  85.744  1.00 33.57 ? 1640 HOH   A O     1 
HETATM 18769 O  O     . HOH   CA 11 .    ? -34.529 76.599  96.033  1.00 32.46 ? 1641 HOH   A O     1 
HETATM 18770 O  O     . HOH   CA 11 .    ? -42.847 61.266  99.983  1.00 25.46 ? 1642 HOH   A O     1 
HETATM 18771 O  O     . HOH   CA 11 .    ? -31.359 46.753  88.079  1.00 31.37 ? 1643 HOH   A O     1 
HETATM 18772 O  O     . HOH   CA 11 .    ? -3.271  60.297  95.192  1.00 38.28 ? 1644 HOH   A O     1 
HETATM 18773 O  O     . HOH   CA 11 .    ? -44.558 41.520  104.028 1.00 32.89 ? 1645 HOH   A O     1 
HETATM 18774 O  O     . HOH   CA 11 .    ? -21.977 88.707  108.863 1.00 26.23 ? 1646 HOH   A O     1 
HETATM 18775 O  O     . HOH   CA 11 .    ? -26.368 56.502  107.774 1.00 20.04 ? 1647 HOH   A O     1 
HETATM 18776 O  O     . HOH   CA 11 .    ? -5.952  79.666  70.955  1.00 45.29 ? 1648 HOH   A O     1 
HETATM 18777 O  O     . HOH   CA 11 .    ? -4.078  79.228  110.944 1.00 29.40 ? 1649 HOH   A O     1 
HETATM 18778 O  O     . HOH   CA 11 .    ? -19.053 70.074  87.596  1.00 25.80 ? 1650 HOH   A O     1 
HETATM 18779 O  O     . HOH   CA 11 .    ? -10.808 67.769  107.920 1.00 17.27 ? 1651 HOH   A O     1 
HETATM 18780 O  O     . HOH   CA 11 .    ? -60.781 68.113  94.206  1.00 37.51 ? 1652 HOH   A O     1 
HETATM 18781 O  O     . HOH   CA 11 .    ? -56.451 34.604  86.255  1.00 23.92 ? 1653 HOH   A O     1 
HETATM 18782 O  O     . HOH   CA 11 .    ? 1.683   64.267  118.960 1.00 41.18 ? 1654 HOH   A O     1 
HETATM 18783 O  O     . HOH   CA 11 .    ? -32.857 70.334  100.118 1.00 37.06 ? 1655 HOH   A O     1 
HETATM 18784 O  O     . HOH   CA 11 .    ? -59.531 54.280  74.536  1.00 17.56 ? 1656 HOH   A O     1 
HETATM 18785 O  O     . HOH   CA 11 .    ? -19.957 93.760  111.440 1.00 31.12 ? 1657 HOH   A O     1 
HETATM 18786 O  O     . HOH   CA 11 .    ? 4.760   67.180  95.898  1.00 26.94 ? 1658 HOH   A O     1 
HETATM 18787 O  O     . HOH   CA 11 .    ? -22.009 42.956  60.723  1.00 35.57 ? 1659 HOH   A O     1 
HETATM 18788 O  O     . HOH   CA 11 .    ? -20.691 47.530  54.669  1.00 33.75 ? 1660 HOH   A O     1 
HETATM 18789 O  O     . HOH   CA 11 .    ? -9.220  77.718  131.649 1.00 35.50 ? 1661 HOH   A O     1 
HETATM 18790 O  O     . HOH   CA 11 .    ? -41.055 49.046  63.848  1.00 25.32 ? 1662 HOH   A O     1 
HETATM 18791 O  O     . HOH   CA 11 .    ? -12.428 79.262  94.412  1.00 16.24 ? 1663 HOH   A O     1 
HETATM 18792 O  O     . HOH   CA 11 .    ? -34.899 80.386  120.179 1.00 24.38 ? 1664 HOH   A O     1 
HETATM 18793 O  O     . HOH   CA 11 .    ? -14.299 64.671  51.189  1.00 38.11 ? 1665 HOH   A O     1 
HETATM 18794 O  O     . HOH   CA 11 .    ? -22.401 67.561  81.162  1.00 26.20 ? 1666 HOH   A O     1 
HETATM 18795 O  O     . HOH   CA 11 .    ? -12.969 63.267  131.716 1.00 39.55 ? 1667 HOH   A O     1 
HETATM 18796 O  O     . HOH   CA 11 .    ? -27.602 82.249  129.521 1.00 29.88 ? 1668 HOH   A O     1 
HETATM 18797 O  O     . HOH   CA 11 .    ? -28.339 62.024  101.980 1.00 17.59 ? 1669 HOH   A O     1 
HETATM 18798 O  O     . HOH   CA 11 .    ? -36.748 63.318  95.840  1.00 26.35 ? 1670 HOH   A O     1 
HETATM 18799 O  O     . HOH   CA 11 .    ? -63.999 76.025  75.816  1.00 45.26 ? 1671 HOH   A O     1 
HETATM 18800 O  O     . HOH   CA 11 .    ? -59.754 60.791  75.723  1.00 16.57 ? 1672 HOH   A O     1 
HETATM 18801 O  O     . HOH   CA 11 .    ? -5.237  54.523  108.057 1.00 19.65 ? 1673 HOH   A O     1 
HETATM 18802 O  O     . HOH   CA 11 .    ? -26.449 82.580  112.377 1.00 22.21 ? 1674 HOH   A O     1 
HETATM 18803 O  O     . HOH   CA 11 .    ? -13.566 77.820  110.980 1.00 19.81 ? 1675 HOH   A O     1 
HETATM 18804 O  O     . HOH   CA 11 .    ? -21.279 56.747  53.372  1.00 32.71 ? 1676 HOH   A O     1 
HETATM 18805 O  O     . HOH   CA 11 .    ? -44.493 73.751  74.862  1.00 26.46 ? 1677 HOH   A O     1 
HETATM 18806 O  O     . HOH   CA 11 .    ? -20.188 59.166  76.197  1.00 21.92 ? 1678 HOH   A O     1 
HETATM 18807 O  O     . HOH   CA 11 .    ? -46.240 29.539  89.246  1.00 35.16 ? 1679 HOH   A O     1 
HETATM 18808 O  O     . HOH   CA 11 .    ? 11.889  75.601  94.728  1.00 32.69 ? 1680 HOH   A O     1 
HETATM 18809 O  O     . HOH   CA 11 .    ? -34.840 67.146  125.109 1.00 34.77 ? 1681 HOH   A O     1 
HETATM 18810 O  O     . HOH   CA 11 .    ? -10.763 63.071  72.666  1.00 29.84 ? 1682 HOH   A O     1 
HETATM 18811 O  O     . HOH   CA 11 .    ? -6.529  82.652  103.122 1.00 20.27 ? 1683 HOH   A O     1 
HETATM 18812 O  O     . HOH   CA 11 .    ? -18.156 82.521  96.514  1.00 19.93 ? 1684 HOH   A O     1 
HETATM 18813 O  O     . HOH   CA 11 .    ? -18.994 61.403  85.216  1.00 22.43 ? 1685 HOH   A O     1 
HETATM 18814 O  O     . HOH   CA 11 .    ? -7.303  80.414  127.973 1.00 32.89 ? 1686 HOH   A O     1 
HETATM 18815 O  O     . HOH   CA 11 .    ? -4.275  73.055  116.794 1.00 25.90 ? 1687 HOH   A O     1 
HETATM 18816 O  O     . HOH   CA 11 .    ? -53.049 63.677  98.168  1.00 21.17 ? 1688 HOH   A O     1 
HETATM 18817 O  O     . HOH   CA 11 .    ? -51.189 69.847  93.763  1.00 21.74 ? 1689 HOH   A O     1 
HETATM 18818 O  O     . HOH   CA 11 .    ? -26.997 89.319  77.490  1.00 30.32 ? 1690 HOH   A O     1 
HETATM 18819 O  O     . HOH   CA 11 .    ? -16.397 75.463  105.896 1.00 22.46 ? 1691 HOH   A O     1 
HETATM 18820 O  O     . HOH   CA 11 .    ? 22.996  65.768  114.727 1.00 25.64 ? 1692 HOH   A O     1 
HETATM 18821 O  O     . HOH   CA 11 .    ? -32.445 48.513  83.945  1.00 31.73 ? 1693 HOH   A O     1 
HETATM 18822 O  O     . HOH   CA 11 .    ? -52.393 78.314  87.436  1.00 29.03 ? 1694 HOH   A O     1 
HETATM 18823 O  O     . HOH   CA 11 .    ? -27.648 73.540  129.364 1.00 33.42 ? 1695 HOH   A O     1 
HETATM 18824 O  O     . HOH   CA 11 .    ? 0.054   76.597  123.046 1.00 33.59 ? 1696 HOH   A O     1 
HETATM 18825 O  O     . HOH   CA 11 .    ? 10.786  67.517  116.442 1.00 27.17 ? 1697 HOH   A O     1 
HETATM 18826 O  O     . HOH   CA 11 .    ? -35.567 73.259  83.442  1.00 25.25 ? 1698 HOH   A O     1 
HETATM 18827 O  O     . HOH   CA 11 .    ? -43.156 85.280  97.249  1.00 24.96 ? 1699 HOH   A O     1 
HETATM 18828 O  O     . HOH   CA 11 .    ? -31.072 81.486  128.914 1.00 40.29 ? 1700 HOH   A O     1 
HETATM 18829 O  O     . HOH   CA 11 .    ? -2.600  53.842  104.395 1.00 26.70 ? 1701 HOH   A O     1 
HETATM 18830 O  O     . HOH   CA 11 .    ? -35.361 63.348  115.890 1.00 33.31 ? 1702 HOH   A O     1 
HETATM 18831 O  O     . HOH   CA 11 .    ? -49.481 49.773  104.531 1.00 42.72 ? 1703 HOH   A O     1 
HETATM 18832 O  O     . HOH   CA 11 .    ? -60.275 47.122  88.476  1.00 25.93 ? 1704 HOH   A O     1 
HETATM 18833 O  O     . HOH   CA 11 .    ? -33.446 48.900  75.068  1.00 27.97 ? 1705 HOH   A O     1 
HETATM 18834 O  O     . HOH   CA 11 .    ? -23.522 63.775  105.983 1.00 18.50 ? 1706 HOH   A O     1 
HETATM 18835 O  O     . HOH   CA 11 .    ? -26.654 85.735  137.119 1.00 39.60 ? 1707 HOH   A O     1 
HETATM 18836 O  O     . HOH   CA 11 .    ? -17.895 92.620  95.842  1.00 42.56 ? 1708 HOH   A O     1 
HETATM 18837 O  O     . HOH   CA 11 .    ? -31.917 88.885  108.449 1.00 28.53 ? 1709 HOH   A O     1 
HETATM 18838 O  O     . HOH   CA 11 .    ? 5.532   63.006  97.110  1.00 19.39 ? 1710 HOH   A O     1 
HETATM 18839 O  O     . HOH   CA 11 .    ? -6.664  66.754  74.095  1.00 39.04 ? 1711 HOH   A O     1 
HETATM 18840 O  O     . HOH   CA 11 .    ? -22.381 95.820  129.367 1.00 41.42 ? 1712 HOH   A O     1 
HETATM 18841 O  O     . HOH   CA 11 .    ? -36.547 95.000  93.811  1.00 32.46 ? 1713 HOH   A O     1 
HETATM 18842 O  O     . HOH   CA 11 .    ? 5.502   80.663  96.849  1.00 34.77 ? 1714 HOH   A O     1 
HETATM 18843 O  O     . HOH   CA 11 .    ? -11.817 88.479  128.648 1.00 32.90 ? 1715 HOH   A O     1 
HETATM 18844 O  O     . HOH   CA 11 .    ? -31.430 71.800  82.405  1.00 32.18 ? 1716 HOH   A O     1 
HETATM 18845 O  O     . HOH   CA 11 .    ? -32.548 59.732  109.363 1.00 30.62 ? 1717 HOH   A O     1 
HETATM 18846 O  O     . HOH   CA 11 .    ? -36.648 58.910  94.076  1.00 17.29 ? 1718 HOH   A O     1 
HETATM 18847 O  O     . HOH   CA 11 .    ? -12.638 77.215  90.879  1.00 15.74 ? 1719 HOH   A O     1 
HETATM 18848 O  O     . HOH   CA 11 .    ? -47.356 60.328  85.009  1.00 14.97 ? 1720 HOH   A O     1 
HETATM 18849 O  O     . HOH   CA 11 .    ? -1.785  77.795  121.096 1.00 27.38 ? 1721 HOH   A O     1 
HETATM 18850 O  O     . HOH   CA 11 .    ? -27.891 55.944  90.401  1.00 29.38 ? 1722 HOH   A O     1 
HETATM 18851 O  O     . HOH   CA 11 .    ? -55.230 29.737  79.752  1.00 31.29 ? 1723 HOH   A O     1 
HETATM 18852 O  O     . HOH   CA 11 .    ? -52.643 54.034  100.063 1.00 26.98 ? 1724 HOH   A O     1 
HETATM 18853 O  O     . HOH   CA 11 .    ? -56.836 46.034  70.948  1.00 20.69 ? 1725 HOH   A O     1 
HETATM 18854 O  O     . HOH   CA 11 .    ? -31.450 84.211  99.086  1.00 22.02 ? 1726 HOH   A O     1 
HETATM 18855 O  O     . HOH   CA 11 .    ? -22.868 58.845  75.808  1.00 29.25 ? 1727 HOH   A O     1 
HETATM 18856 O  O     . HOH   CA 11 .    ? -67.441 60.125  69.677  1.00 27.35 ? 1728 HOH   A O     1 
HETATM 18857 O  O     . HOH   CA 11 .    ? -1.668  76.878  87.611  1.00 27.28 ? 1729 HOH   A O     1 
HETATM 18858 O  O     . HOH   CA 11 .    ? -38.933 49.449  102.198 1.00 29.62 ? 1730 HOH   A O     1 
HETATM 18859 O  O     . HOH   CA 11 .    ? -6.040  76.079  111.037 1.00 18.00 ? 1731 HOH   A O     1 
HETATM 18860 O  O     . HOH   CA 11 .    ? -23.964 61.057  63.488  1.00 30.66 ? 1732 HOH   A O     1 
HETATM 18861 O  O     . HOH   CA 11 .    ? -9.941  74.332  104.022 1.00 20.12 ? 1733 HOH   A O     1 
HETATM 18862 O  O     . HOH   CA 11 .    ? -4.113  78.211  122.462 1.00 22.90 ? 1734 HOH   A O     1 
HETATM 18863 O  O     . HOH   CA 11 .    ? -65.821 58.953  75.694  1.00 19.95 ? 1735 HOH   A O     1 
HETATM 18864 O  O     . HOH   CA 11 .    ? -20.181 78.646  70.051  1.00 24.06 ? 1736 HOH   A O     1 
HETATM 18865 O  O     . HOH   CA 11 .    ? 16.858  69.134  117.595 1.00 26.72 ? 1737 HOH   A O     1 
HETATM 18866 O  O     . HOH   CA 11 .    ? -20.679 100.701 89.445  1.00 38.01 ? 1738 HOH   A O     1 
HETATM 18867 O  O     . HOH   CA 11 .    ? -49.796 48.650  55.914  1.00 39.24 ? 1739 HOH   A O     1 
HETATM 18868 O  O     . HOH   CA 11 .    ? -58.477 72.762  80.070  1.00 34.19 ? 1740 HOH   A O     1 
HETATM 18869 O  O     . HOH   CA 11 .    ? -46.449 30.700  85.280  1.00 27.49 ? 1741 HOH   A O     1 
HETATM 18870 O  O     . HOH   CA 11 .    ? -45.891 78.236  95.996  1.00 20.25 ? 1742 HOH   A O     1 
HETATM 18871 O  O     . HOH   CA 11 .    ? -56.232 55.767  94.826  1.00 19.30 ? 1743 HOH   A O     1 
HETATM 18872 O  O     . HOH   CA 11 .    ? 13.467  86.634  120.650 1.00 35.75 ? 1744 HOH   A O     1 
HETATM 18873 O  O     . HOH   CA 11 .    ? -20.466 90.863  108.915 1.00 27.34 ? 1745 HOH   A O     1 
HETATM 18874 O  O     . HOH   CA 11 .    ? -47.998 64.209  96.615  1.00 22.53 ? 1746 HOH   A O     1 
HETATM 18875 O  O     . HOH   CA 11 .    ? -49.676 78.162  77.499  1.00 30.35 ? 1747 HOH   A O     1 
HETATM 18876 O  O     . HOH   CA 11 .    ? -35.365 40.510  91.939  1.00 24.01 ? 1748 HOH   A O     1 
HETATM 18877 O  O     . HOH   CA 11 .    ? -7.365  84.949  86.531  1.00 35.25 ? 1749 HOH   A O     1 
HETATM 18878 O  O     . HOH   CA 11 .    ? -41.585 64.119  103.400 1.00 21.47 ? 1750 HOH   A O     1 
HETATM 18879 O  O     . HOH   CA 11 .    ? -59.284 51.943  65.912  1.00 19.65 ? 1751 HOH   A O     1 
HETATM 18880 O  O     . HOH   CA 11 .    ? -44.848 59.146  55.077  1.00 29.91 ? 1752 HOH   A O     1 
HETATM 18881 O  O     . HOH   CA 11 .    ? -53.854 55.544  68.317  1.00 16.94 ? 1753 HOH   A O     1 
HETATM 18882 O  O     . HOH   CA 11 .    ? -26.567 50.287  96.446  1.00 26.50 ? 1754 HOH   A O     1 
HETATM 18883 O  O     . HOH   CA 11 .    ? -27.489 58.716  76.048  1.00 36.75 ? 1755 HOH   A O     1 
HETATM 18884 O  O     . HOH   CA 11 .    ? -46.498 32.122  70.119  1.00 32.22 ? 1756 HOH   A O     1 
HETATM 18885 O  O     . HOH   CA 11 .    ? -3.937  57.688  72.742  1.00 21.17 ? 1757 HOH   A O     1 
HETATM 18886 O  O     . HOH   CA 11 .    ? 24.849  77.319  109.173 1.00 32.59 ? 1758 HOH   A O     1 
HETATM 18887 O  O     . HOH   CA 11 .    ? -18.247 57.433  97.115  1.00 19.28 ? 1759 HOH   A O     1 
HETATM 18888 O  O     . HOH   CA 11 .    ? -41.581 71.521  64.108  1.00 25.31 ? 1760 HOH   A O     1 
HETATM 18889 O  O     . HOH   CA 11 .    ? -42.064 67.815  90.969  1.00 17.99 ? 1761 HOH   A O     1 
HETATM 18890 O  O     . HOH   CA 11 .    ? -31.960 82.412  75.300  1.00 20.77 ? 1762 HOH   A O     1 
HETATM 18891 O  O     . HOH   CA 11 .    ? -25.974 63.727  104.558 1.00 20.69 ? 1763 HOH   A O     1 
HETATM 18892 O  O     . HOH   CA 11 .    ? -51.890 72.885  105.456 1.00 31.53 ? 1764 HOH   A O     1 
HETATM 18893 O  O     . HOH   CA 11 .    ? -42.536 77.849  75.702  1.00 25.44 ? 1765 HOH   A O     1 
HETATM 18894 O  O     . HOH   CA 11 .    ? -24.977 88.168  79.079  1.00 23.79 ? 1766 HOH   A O     1 
HETATM 18895 O  O     . HOH   CA 11 .    ? -0.549  66.028  94.282  1.00 31.03 ? 1767 HOH   A O     1 
HETATM 18896 O  O     . HOH   CA 11 .    ? -0.554  77.329  116.934 1.00 24.45 ? 1768 HOH   A O     1 
HETATM 18897 O  O     . HOH   CA 11 .    ? -46.615 67.394  59.538  1.00 23.82 ? 1769 HOH   A O     1 
HETATM 18898 O  O     . HOH   CA 11 .    ? -60.437 61.403  92.535  1.00 23.48 ? 1770 HOH   A O     1 
HETATM 18899 O  O     . HOH   CA 11 .    ? -22.626 96.666  78.689  1.00 39.83 ? 1771 HOH   A O     1 
HETATM 18900 O  O     . HOH   CA 11 .    ? -26.015 50.755  105.011 1.00 34.90 ? 1772 HOH   A O     1 
HETATM 18901 O  O     . HOH   CA 11 .    ? 5.422   74.113  95.623  1.00 41.93 ? 1773 HOH   A O     1 
HETATM 18902 O  O     . HOH   CA 11 .    ? 16.793  71.497  119.031 1.00 26.94 ? 1774 HOH   A O     1 
HETATM 18903 O  O     . HOH   CA 11 .    ? -38.102 41.063  71.449  1.00 27.77 ? 1775 HOH   A O     1 
HETATM 18904 O  O     . HOH   CA 11 .    ? -20.918 70.818  75.529  1.00 23.29 ? 1776 HOH   A O     1 
HETATM 18905 O  O     . HOH   CA 11 .    ? -1.296  83.763  117.812 1.00 25.27 ? 1777 HOH   A O     1 
HETATM 18906 O  O     . HOH   CA 11 .    ? -29.051 76.568  72.721  1.00 26.64 ? 1778 HOH   A O     1 
HETATM 18907 O  O     . HOH   CA 11 .    ? -49.924 68.639  91.854  1.00 20.67 ? 1779 HOH   A O     1 
HETATM 18908 O  O     . HOH   CA 11 .    ? -32.251 61.753  111.409 1.00 22.97 ? 1780 HOH   A O     1 
HETATM 18909 O  O     . HOH   CA 11 .    ? -41.823 79.698  79.843  1.00 27.58 ? 1781 HOH   A O     1 
HETATM 18910 O  O     . HOH   CA 11 .    ? -46.886 82.213  101.389 1.00 25.52 ? 1782 HOH   A O     1 
HETATM 18911 O  O     . HOH   CA 11 .    ? 3.860   57.841  104.734 1.00 19.57 ? 1783 HOH   A O     1 
HETATM 18912 O  O     . HOH   CA 11 .    ? -23.503 54.417  101.171 1.00 26.11 ? 1784 HOH   A O     1 
HETATM 18913 O  O     . HOH   CA 11 .    ? -2.805  55.964  99.627  1.00 28.44 ? 1785 HOH   A O     1 
HETATM 18914 O  O     . HOH   CA 11 .    ? -33.566 45.810  84.557  1.00 25.35 ? 1786 HOH   A O     1 
HETATM 18915 O  O     . HOH   CA 11 .    ? -4.711  71.218  126.700 1.00 39.53 ? 1787 HOH   A O     1 
HETATM 18916 O  O     . HOH   CA 11 .    ? -20.041 76.554  67.217  1.00 36.20 ? 1788 HOH   A O     1 
HETATM 18917 O  O     . HOH   CA 11 .    ? -50.108 56.781  71.620  1.00 24.71 ? 1789 HOH   A O     1 
HETATM 18918 O  O     . HOH   CA 11 .    ? -35.636 51.803  85.203  1.00 18.55 ? 1790 HOH   A O     1 
HETATM 18919 O  O     . HOH   CA 11 .    ? -41.246 71.548  114.146 1.00 31.64 ? 1791 HOH   A O     1 
HETATM 18920 O  O     . HOH   CA 11 .    ? -61.724 70.375  82.785  1.00 20.11 ? 1792 HOH   A O     1 
HETATM 18921 O  O     . HOH   CA 11 .    ? 9.220   57.108  97.252  1.00 28.28 ? 1793 HOH   A O     1 
HETATM 18922 O  O     . HOH   CA 11 .    ? -23.346 64.166  70.561  1.00 44.93 ? 1794 HOH   A O     1 
HETATM 18923 O  O     . HOH   CA 11 .    ? -47.975 57.761  86.103  1.00 16.04 ? 1795 HOH   A O     1 
HETATM 18924 O  O     . HOH   CA 11 .    ? -39.644 78.231  99.761  1.00 21.25 ? 1796 HOH   A O     1 
HETATM 18925 O  O     . HOH   CA 11 .    ? 8.987   55.302  104.765 1.00 25.21 ? 1797 HOH   A O     1 
HETATM 18926 O  O     . HOH   CA 11 .    ? -61.310 52.984  90.964  1.00 26.01 ? 1798 HOH   A O     1 
HETATM 18927 O  O     . HOH   CA 11 .    ? -31.814 59.153  62.957  1.00 29.12 ? 1799 HOH   A O     1 
HETATM 18928 O  O     . HOH   CA 11 .    ? 15.003  83.048  111.010 1.00 23.30 ? 1800 HOH   A O     1 
HETATM 18929 O  O     . HOH   CA 11 .    ? -25.490 62.566  109.899 1.00 21.16 ? 1801 HOH   A O     1 
HETATM 18930 O  O     . HOH   CA 11 .    ? -44.341 31.162  68.814  1.00 34.06 ? 1802 HOH   A O     1 
HETATM 18931 O  O     . HOH   CA 11 .    ? -1.215  58.500  110.901 1.00 29.37 ? 1803 HOH   A O     1 
HETATM 18932 O  O     . HOH   CA 11 .    ? -51.285 64.879  94.664  1.00 19.40 ? 1804 HOH   A O     1 
HETATM 18933 O  O     . HOH   CA 11 .    ? -47.651 49.115  95.674  1.00 19.61 ? 1805 HOH   A O     1 
HETATM 18934 O  O     . HOH   CA 11 .    ? 1.445   73.212  115.759 1.00 29.41 ? 1806 HOH   A O     1 
HETATM 18935 O  O     . HOH   CA 11 .    ? -12.542 64.223  129.587 1.00 32.61 ? 1807 HOH   A O     1 
HETATM 18936 O  O     . HOH   CA 11 .    ? -21.119 74.199  104.613 1.00 37.43 ? 1808 HOH   A O     1 
HETATM 18937 O  O     . HOH   CA 11 .    ? -1.134  73.332  88.727  1.00 32.89 ? 1809 HOH   A O     1 
HETATM 18938 O  O     . HOH   CA 11 .    ? -3.466  90.580  100.606 1.00 24.57 ? 1810 HOH   A O     1 
HETATM 18939 O  O     . HOH   CA 11 .    ? -7.053  41.995  66.251  1.00 24.92 ? 1811 HOH   A O     1 
HETATM 18940 O  O     . HOH   CA 11 .    ? -24.861 88.826  99.749  1.00 21.48 ? 1812 HOH   A O     1 
HETATM 18941 O  O     . HOH   CA 11 .    ? -28.285 60.395  124.777 1.00 36.74 ? 1813 HOH   A O     1 
HETATM 18942 O  O     . HOH   CA 11 .    ? -2.154  85.342  113.016 1.00 25.61 ? 1814 HOH   A O     1 
HETATM 18943 O  O     . HOH   CA 11 .    ? 20.402  62.014  98.804  1.00 24.28 ? 1815 HOH   A O     1 
HETATM 18944 O  O     . HOH   CA 11 .    ? -45.878 65.207  91.652  1.00 16.44 ? 1816 HOH   A O     1 
HETATM 18945 O  O     . HOH   CA 11 .    ? -32.029 88.479  95.042  1.00 21.53 ? 1817 HOH   A O     1 
HETATM 18946 O  O     . HOH   CA 11 .    ? -45.992 72.545  64.157  1.00 17.98 ? 1818 HOH   A O     1 
HETATM 18947 O  O     . HOH   CA 11 .    ? -46.221 24.496  82.263  1.00 36.14 ? 1819 HOH   A O     1 
HETATM 18948 O  O     . HOH   CA 11 .    ? -64.686 59.548  92.660  1.00 31.82 ? 1820 HOH   A O     1 
HETATM 18949 O  O     . HOH   CA 11 .    ? -65.483 71.400  80.321  1.00 25.19 ? 1821 HOH   A O     1 
HETATM 18950 O  O     . HOH   CA 11 .    ? -3.088  62.513  77.481  1.00 20.64 ? 1822 HOH   A O     1 
HETATM 18951 O  O     . HOH   CA 11 .    ? -44.266 55.741  94.870  1.00 16.82 ? 1823 HOH   A O     1 
HETATM 18952 O  O     . HOH   CA 11 .    ? -0.385  52.775  62.950  1.00 26.31 ? 1824 HOH   A O     1 
HETATM 18953 O  O     . HOH   CA 11 .    ? 24.488  67.790  94.764  1.00 41.86 ? 1825 HOH   A O     1 
HETATM 18954 O  O     . HOH   CA 11 .    ? -4.256  76.200  124.449 1.00 28.20 ? 1826 HOH   A O     1 
HETATM 18955 O  O     . HOH   CA 11 .    ? -38.925 32.097  96.644  1.00 36.69 ? 1827 HOH   A O     1 
HETATM 18956 O  O     . HOH   CA 11 .    ? -9.572  56.071  82.446  1.00 30.00 ? 1828 HOH   A O     1 
HETATM 18957 O  O     . HOH   CA 11 .    ? -27.249 64.730  99.948  1.00 23.86 ? 1829 HOH   A O     1 
HETATM 18958 O  O     . HOH   CA 11 .    ? -28.617 61.954  116.613 1.00 22.62 ? 1830 HOH   A O     1 
HETATM 18959 O  O     . HOH   CA 11 .    ? 16.447  57.823  102.601 1.00 20.54 ? 1831 HOH   A O     1 
HETATM 18960 O  O     . HOH   CA 11 .    ? 10.608  54.861  108.664 1.00 38.69 ? 1832 HOH   A O     1 
HETATM 18961 O  O     . HOH   CA 11 .    ? -41.545 28.031  70.068  1.00 36.91 ? 1833 HOH   A O     1 
HETATM 18962 O  O     . HOH   CA 11 .    ? -0.722  83.740  109.448 1.00 27.14 ? 1834 HOH   A O     1 
HETATM 18963 O  O     . HOH   CA 11 .    ? 7.102   57.474  112.120 1.00 32.74 ? 1835 HOH   A O     1 
HETATM 18964 O  O     . HOH   CA 11 .    ? -30.484 81.045  122.790 1.00 30.75 ? 1836 HOH   A O     1 
HETATM 18965 O  O     . HOH   CA 11 .    ? -42.462 47.605  81.018  1.00 20.63 ? 1837 HOH   A O     1 
HETATM 18966 O  O     . HOH   CA 11 .    ? -62.366 55.009  63.142  1.00 33.11 ? 1838 HOH   A O     1 
HETATM 18967 O  O     . HOH   CA 11 .    ? -46.814 81.052  93.293  1.00 40.94 ? 1839 HOH   A O     1 
HETATM 18968 O  O     . HOH   CA 11 .    ? -24.710 92.646  105.080 1.00 35.56 ? 1840 HOH   A O     1 
HETATM 18969 O  O     . HOH   CA 11 .    ? -5.986  65.116  114.052 1.00 21.86 ? 1841 HOH   A O     1 
HETATM 18970 O  O     . HOH   CA 11 .    ? -43.984 25.286  76.084  1.00 38.90 ? 1842 HOH   A O     1 
HETATM 18971 O  O     . HOH   CA 11 .    ? -46.611 54.350  89.492  1.00 17.45 ? 1843 HOH   A O     1 
HETATM 18972 O  O     . HOH   CA 11 .    ? -16.575 60.238  106.321 1.00 23.68 ? 1844 HOH   A O     1 
HETATM 18973 O  O     . HOH   CA 11 .    ? -13.482 55.243  103.307 1.00 33.12 ? 1845 HOH   A O     1 
HETATM 18974 O  O     . HOH   CA 11 .    ? -49.891 49.055  99.600  1.00 24.37 ? 1846 HOH   A O     1 
HETATM 18975 O  O     . HOH   CA 11 .    ? -24.353 47.925  98.422  1.00 41.05 ? 1847 HOH   A O     1 
HETATM 18976 O  O     . HOH   CA 11 .    ? -1.644  79.283  99.797  1.00 24.58 ? 1848 HOH   A O     1 
HETATM 18977 O  O     . HOH   CA 11 .    ? -0.650  70.066  95.938  1.00 31.69 ? 1849 HOH   A O     1 
HETATM 18978 O  O     . HOH   CA 11 .    ? -1.653  58.147  96.411  1.00 33.66 ? 1850 HOH   A O     1 
HETATM 18979 O  O     . HOH   CA 11 .    ? -49.144 83.200  108.772 1.00 30.61 ? 1851 HOH   A O     1 
HETATM 18980 O  O     . HOH   CA 11 .    ? -50.405 66.431  106.098 1.00 28.55 ? 1852 HOH   A O     1 
HETATM 18981 O  O     . HOH   CA 11 .    ? -15.008 67.203  73.028  1.00 22.20 ? 1853 HOH   A O     1 
HETATM 18982 O  O     . HOH   CA 11 .    ? -45.487 62.588  92.423  1.00 16.07 ? 1854 HOH   A O     1 
HETATM 18983 O  O     . HOH   CA 11 .    ? -41.988 55.445  104.601 1.00 37.53 ? 1855 HOH   A O     1 
HETATM 18984 O  O     . HOH   CA 11 .    ? 18.366  62.214  94.307  1.00 32.89 ? 1856 HOH   A O     1 
HETATM 18985 O  O     . HOH   CA 11 .    ? -57.235 60.186  60.907  1.00 18.77 ? 1857 HOH   A O     1 
HETATM 18986 O  O     . HOH   CA 11 .    ? -34.800 66.540  101.420 1.00 23.28 ? 1858 HOH   A O     1 
HETATM 18987 O  O     . HOH   CA 11 .    ? -53.822 43.284  65.369  1.00 38.99 ? 1859 HOH   A O     1 
HETATM 18988 O  O     . HOH   CA 11 .    ? -31.159 91.318  80.444  1.00 30.68 ? 1860 HOH   A O     1 
HETATM 18989 O  O     . HOH   CA 11 .    ? -55.952 36.950  92.530  1.00 35.16 ? 1861 HOH   A O     1 
HETATM 18990 O  O     . HOH   CA 11 .    ? -30.823 91.013  106.993 1.00 26.80 ? 1862 HOH   A O     1 
HETATM 18991 O  O     . HOH   CA 11 .    ? -57.654 57.848  101.002 1.00 25.09 ? 1863 HOH   A O     1 
HETATM 18992 O  O     . HOH   CA 11 .    ? -52.433 72.687  64.165  1.00 27.21 ? 1864 HOH   A O     1 
HETATM 18993 O  O     . HOH   CA 11 .    ? -16.164 94.539  91.222  1.00 39.71 ? 1865 HOH   A O     1 
HETATM 18994 O  O     . HOH   CA 11 .    ? -19.959 88.791  74.918  1.00 34.24 ? 1866 HOH   A O     1 
HETATM 18995 O  O     . HOH   CA 11 .    ? -25.921 58.772  53.231  1.00 48.74 ? 1867 HOH   A O     1 
HETATM 18996 O  O     . HOH   CA 11 .    ? -1.526  83.690  115.061 1.00 30.90 ? 1868 HOH   A O     1 
HETATM 18997 O  O     . HOH   CA 11 .    ? -20.402 66.089  80.950  1.00 27.21 ? 1869 HOH   A O     1 
HETATM 18998 O  O     . HOH   CA 11 .    ? 10.635  57.343  105.563 1.00 25.11 ? 1870 HOH   A O     1 
HETATM 18999 O  O     . HOH   CA 11 .    ? -66.806 68.109  71.924  1.00 32.70 ? 1871 HOH   A O     1 
HETATM 19000 O  O     . HOH   CA 11 .    ? 14.834  75.835  93.943  1.00 37.38 ? 1872 HOH   A O     1 
HETATM 19001 O  O     . HOH   CA 11 .    ? 5.015   55.169  96.686  1.00 25.44 ? 1873 HOH   A O     1 
HETATM 19002 O  O     . HOH   CA 11 .    ? 7.707   88.781  126.885 1.00 38.10 ? 1874 HOH   A O     1 
HETATM 19003 O  O     . HOH   CA 11 .    ? -20.738 81.429  115.635 1.00 19.75 ? 1875 HOH   A O     1 
HETATM 19004 O  O     . HOH   CA 11 .    ? 13.795  82.090  113.930 1.00 23.38 ? 1876 HOH   A O     1 
HETATM 19005 O  O     . HOH   CA 11 .    ? -64.610 44.992  77.908  1.00 33.93 ? 1877 HOH   A O     1 
HETATM 19006 O  O     . HOH   CA 11 .    ? -34.134 90.583  122.060 1.00 32.69 ? 1878 HOH   A O     1 
HETATM 19007 O  O     . HOH   CA 11 .    ? -58.300 65.359  94.171  1.00 26.87 ? 1879 HOH   A O     1 
HETATM 19008 O  O     . HOH   CA 11 .    ? -8.168  74.835  70.308  1.00 32.61 ? 1880 HOH   A O     1 
HETATM 19009 O  O     . HOH   CA 11 .    ? -5.544  67.963  77.776  1.00 29.12 ? 1881 HOH   A O     1 
HETATM 19010 O  O     . HOH   CA 11 .    ? -48.371 75.087  95.405  1.00 22.29 ? 1882 HOH   A O     1 
HETATM 19011 O  O     . HOH   CA 11 .    ? -31.180 60.900  90.371  1.00 22.20 ? 1883 HOH   A O     1 
HETATM 19012 O  O     . HOH   CA 11 .    ? -36.939 51.750  60.875  1.00 28.74 ? 1884 HOH   A O     1 
HETATM 19013 O  O     . HOH   CA 11 .    ? -60.131 50.458  90.641  1.00 33.95 ? 1885 HOH   A O     1 
HETATM 19014 O  O     . HOH   CA 11 .    ? -41.218 90.579  98.534  1.00 24.53 ? 1886 HOH   A O     1 
HETATM 19015 O  O     . HOH   CA 11 .    ? -65.216 54.522  90.661  1.00 32.47 ? 1887 HOH   A O     1 
HETATM 19016 O  O     . HOH   CA 11 .    ? -23.779 65.535  129.711 1.00 42.04 ? 1888 HOH   A O     1 
HETATM 19017 O  O     . HOH   CA 11 .    ? 2.491   83.892  126.575 1.00 36.84 ? 1889 HOH   A O     1 
HETATM 19018 O  O     . HOH   CA 11 .    ? -18.861 97.468  126.542 1.00 40.22 ? 1890 HOH   A O     1 
HETATM 19019 O  O     . HOH   CA 11 .    ? -62.127 61.823  68.075  1.00 23.69 ? 1891 HOH   A O     1 
HETATM 19020 O  O     . HOH   CA 11 .    ? 9.639   67.938  93.844  1.00 37.36 ? 1892 HOH   A O     1 
HETATM 19021 O  O     . HOH   CA 11 .    ? 17.158  80.410  96.685  1.00 31.24 ? 1893 HOH   A O     1 
HETATM 19022 O  O     . HOH   CA 11 .    ? -19.047 59.688  69.877  1.00 21.76 ? 1894 HOH   A O     1 
HETATM 19023 O  O     . HOH   CA 11 .    ? -6.992  70.539  93.934  1.00 23.45 ? 1895 HOH   A O     1 
HETATM 19024 O  O     . HOH   CA 11 .    ? -39.204 88.738  90.627  1.00 30.60 ? 1896 HOH   A O     1 
HETATM 19025 O  O     . HOH   CA 11 .    ? 10.076  63.111  112.860 1.00 30.35 ? 1897 HOH   A O     1 
HETATM 19026 O  O     . HOH   CA 11 .    ? -47.566 70.675  111.026 1.00 33.39 ? 1898 HOH   A O     1 
HETATM 19027 O  O     . HOH   CA 11 .    ? -5.777  72.434  67.265  1.00 44.98 ? 1899 HOH   A O     1 
HETATM 19028 O  O     . HOH   CA 11 .    ? -32.427 92.962  103.752 1.00 25.33 ? 1900 HOH   A O     1 
HETATM 19029 O  O     . HOH   CA 11 .    ? -44.282 69.402  108.905 1.00 34.88 ? 1901 HOH   A O     1 
HETATM 19030 O  O     . HOH   CA 11 .    ? -38.863 57.921  75.339  1.00 34.63 ? 1902 HOH   A O     1 
HETATM 19031 O  O     . HOH   CA 11 .    ? -55.226 47.755  69.702  1.00 21.96 ? 1903 HOH   A O     1 
HETATM 19032 O  O     . HOH   CA 11 .    ? -47.084 48.963  92.955  1.00 18.73 ? 1904 HOH   A O     1 
HETATM 19033 O  O     . HOH   CA 11 .    ? -3.336  89.973  108.617 1.00 23.71 ? 1905 HOH   A O     1 
HETATM 19034 O  O     . HOH   CA 11 .    ? -27.717 70.930  89.872  1.00 27.25 ? 1906 HOH   A O     1 
HETATM 19035 O  O     . HOH   CA 11 .    ? -46.676 66.560  93.692  1.00 18.56 ? 1907 HOH   A O     1 
HETATM 19036 O  O     . HOH   CA 11 .    ? -45.395 86.856  111.755 1.00 44.79 ? 1908 HOH   A O     1 
HETATM 19037 O  O     . HOH   CA 11 .    ? -53.324 56.830  55.039  1.00 33.09 ? 1909 HOH   A O     1 
HETATM 19038 O  O     . HOH   CA 11 .    ? -16.125 68.027  96.560  1.00 16.00 ? 1910 HOH   A O     1 
HETATM 19039 O  O     . HOH   CA 11 .    ? -28.658 77.182  103.067 1.00 33.05 ? 1911 HOH   A O     1 
HETATM 19040 O  O     . HOH   CA 11 .    ? -7.568  37.664  63.690  1.00 38.25 ? 1912 HOH   A O     1 
HETATM 19041 O  O     . HOH   CA 11 .    ? -34.638 77.509  84.867  1.00 24.15 ? 1913 HOH   A O     1 
HETATM 19042 O  O     . HOH   CA 11 .    ? 14.076  87.875  105.873 1.00 34.50 ? 1914 HOH   A O     1 
HETATM 19043 O  O     . HOH   CA 11 .    ? -30.684 50.257  104.594 1.00 28.85 ? 1915 HOH   A O     1 
HETATM 19044 O  O     . HOH   CA 11 .    ? -42.726 28.903  86.318  1.00 36.26 ? 1916 HOH   A O     1 
HETATM 19045 O  O     . HOH   CA 11 .    ? -3.077  77.399  71.830  1.00 37.73 ? 1917 HOH   A O     1 
HETATM 19046 O  O     . HOH   CA 11 .    ? -20.169 86.651  91.434  1.00 21.35 ? 1918 HOH   A O     1 
HETATM 19047 O  O     . HOH   CA 11 .    ? -11.474 58.429  125.358 1.00 34.09 ? 1919 HOH   A O     1 
HETATM 19048 O  O     . HOH   CA 11 .    ? -8.853  60.117  106.912 1.00 20.09 ? 1920 HOH   A O     1 
HETATM 19049 O  O     . HOH   CA 11 .    ? 18.062  57.394  104.936 1.00 28.68 ? 1921 HOH   A O     1 
HETATM 19050 O  O     . HOH   CA 11 .    ? -42.102 24.112  74.330  1.00 45.98 ? 1922 HOH   A O     1 
HETATM 19051 O  O     . HOH   CA 11 .    ? -29.496 62.610  61.729  1.00 38.37 ? 1923 HOH   A O     1 
HETATM 19052 O  O     . HOH   CA 11 .    ? -8.758  65.091  113.809 1.00 18.69 ? 1924 HOH   A O     1 
HETATM 19053 O  O     . HOH   CA 11 .    ? -38.373 36.509  82.360  1.00 33.02 ? 1925 HOH   A O     1 
HETATM 19054 O  O     . HOH   CA 11 .    ? -66.321 61.565  75.568  1.00 16.78 ? 1926 HOH   A O     1 
HETATM 19055 O  O     . HOH   CA 11 .    ? -1.866  95.525  117.136 1.00 39.65 ? 1927 HOH   A O     1 
HETATM 19056 O  O     . HOH   CA 11 .    ? -33.285 78.009  73.980  1.00 26.43 ? 1928 HOH   A O     1 
HETATM 19057 O  O     . HOH   CA 11 .    ? -48.808 61.701  56.713  1.00 21.70 ? 1929 HOH   A O     1 
HETATM 19058 O  O     . HOH   CA 11 .    ? -52.456 61.950  94.498  1.00 19.60 ? 1930 HOH   A O     1 
HETATM 19059 O  O     . HOH   CA 11 .    ? -58.172 57.871  62.911  1.00 18.12 ? 1931 HOH   A O     1 
HETATM 19060 O  O     . HOH   CA 11 .    ? -63.742 71.010  70.733  1.00 26.58 ? 1932 HOH   A O     1 
HETATM 19061 O  O     . HOH   CA 11 .    ? -49.546 54.427  59.073  1.00 29.12 ? 1933 HOH   A O     1 
HETATM 19062 O  O     . HOH   CA 11 .    ? -35.723 43.659  79.129  1.00 25.45 ? 1934 HOH   A O     1 
HETATM 19063 O  O     . HOH   CA 11 .    ? -15.656 43.929  76.723  1.00 41.73 ? 1935 HOH   A O     1 
HETATM 19064 O  O     . HOH   CA 11 .    ? 15.805  61.632  115.926 1.00 33.99 ? 1936 HOH   A O     1 
HETATM 19065 O  O     . HOH   CA 11 .    ? -21.980 52.854  104.042 1.00 35.61 ? 1937 HOH   A O     1 
HETATM 19066 O  O     . HOH   CA 11 .    ? -32.786 92.472  110.096 1.00 30.90 ? 1938 HOH   A O     1 
HETATM 19067 O  O     . HOH   CA 11 .    ? -18.457 60.894  66.796  1.00 26.97 ? 1939 HOH   A O     1 
HETATM 19068 O  O     . HOH   CA 11 .    ? -18.408 73.813  131.825 1.00 34.96 ? 1940 HOH   A O     1 
HETATM 19069 O  O     . HOH   CA 11 .    ? -20.104 52.268  78.061  1.00 25.64 ? 1941 HOH   A O     1 
HETATM 19070 O  O     . HOH   CA 11 .    ? -42.695 66.245  63.548  1.00 32.23 ? 1942 HOH   A O     1 
HETATM 19071 O  O     . HOH   CA 11 .    ? 12.528  67.278  93.133  1.00 29.12 ? 1943 HOH   A O     1 
HETATM 19072 O  O     . HOH   CA 11 .    ? -38.465 61.531  91.642  1.00 18.00 ? 1944 HOH   A O     1 
HETATM 19073 O  O     . HOH   CA 11 .    ? -21.543 59.375  122.261 1.00 27.88 ? 1945 HOH   A O     1 
HETATM 19074 O  O     . HOH   CA 11 .    ? -19.453 90.847  76.798  1.00 28.31 ? 1946 HOH   A O     1 
HETATM 19075 O  O     . HOH   CA 11 .    ? -34.294 75.556  83.066  1.00 26.30 ? 1947 HOH   A O     1 
HETATM 19076 O  O     . HOH   CA 11 .    ? -11.868 59.707  84.596  1.00 26.70 ? 1948 HOH   A O     1 
HETATM 19077 O  O     . HOH   CA 11 .    ? -49.729 75.856  101.406 1.00 23.59 ? 1949 HOH   A O     1 
HETATM 19078 O  O     . HOH   CA 11 .    ? -1.984  77.862  105.113 1.00 19.30 ? 1950 HOH   A O     1 
HETATM 19079 O  O     . HOH   CA 11 .    ? -41.782 70.827  95.143  1.00 24.78 ? 1951 HOH   A O     1 
HETATM 19080 O  O     . HOH   CA 11 .    ? -48.229 66.122  57.748  1.00 24.09 ? 1952 HOH   A O     1 
HETATM 19081 O  O     . HOH   CA 11 .    ? -19.481 91.818  105.038 1.00 30.90 ? 1953 HOH   A O     1 
HETATM 19082 O  O     . HOH   CA 11 .    ? -41.765 29.665  89.128  1.00 36.86 ? 1954 HOH   A O     1 
HETATM 19083 O  O     . HOH   CA 11 .    ? -3.346  77.860  101.291 1.00 25.38 ? 1955 HOH   A O     1 
HETATM 19084 O  O     . HOH   CA 11 .    ? -48.359 82.837  111.209 1.00 30.86 ? 1956 HOH   A O     1 
HETATM 19085 O  O     . HOH   CA 11 .    ? -47.905 59.220  82.636  1.00 14.44 ? 1957 HOH   A O     1 
HETATM 19086 O  O     . HOH   CA 11 .    ? -63.217 54.099  72.048  1.00 26.25 ? 1958 HOH   A O     1 
HETATM 19087 O  O     . HOH   CA 11 .    ? -32.178 75.105  126.207 1.00 27.96 ? 1959 HOH   A O     1 
HETATM 19088 O  O     . HOH   CA 11 .    ? -34.342 82.374  118.371 1.00 22.05 ? 1960 HOH   A O     1 
HETATM 19089 O  O     . HOH   CA 11 .    ? -33.720 83.647  123.163 1.00 28.05 ? 1961 HOH   A O     1 
HETATM 19090 O  O     . HOH   CA 11 .    ? -4.740  59.166  118.227 1.00 22.24 ? 1962 HOH   A O     1 
HETATM 19091 O  O     . HOH   CA 11 .    ? -64.587 43.048  86.021  1.00 28.62 ? 1963 HOH   A O     1 
HETATM 19092 O  O     . HOH   CA 11 .    ? -46.167 65.112  106.977 1.00 40.13 ? 1964 HOH   A O     1 
HETATM 19093 O  O     . HOH   CA 11 .    ? -37.922 65.283  88.243  1.00 33.65 ? 1965 HOH   A O     1 
HETATM 19094 O  O     . HOH   CA 11 .    ? -17.254 88.864  99.282  1.00 38.18 ? 1966 HOH   A O     1 
HETATM 19095 O  O     . HOH   CA 11 .    ? -50.334 37.983  99.653  1.00 33.81 ? 1967 HOH   A O     1 
HETATM 19096 O  O     . HOH   CA 11 .    ? 12.437  91.409  96.924  1.00 45.95 ? 1968 HOH   A O     1 
HETATM 19097 O  O     . HOH   CA 11 .    ? -65.622 64.735  81.210  1.00 19.90 ? 1969 HOH   A O     1 
HETATM 19098 O  O     . HOH   CA 11 .    ? -23.411 86.416  73.530  1.00 33.93 ? 1970 HOH   A O     1 
HETATM 19099 O  O     . HOH   CA 11 .    ? -7.353  62.346  106.929 1.00 19.04 ? 1971 HOH   A O     1 
HETATM 19100 O  O     . HOH   CA 11 .    ? 11.220  89.229  104.360 1.00 38.62 ? 1972 HOH   A O     1 
HETATM 19101 O  O     . HOH   CA 11 .    ? -46.325 56.014  87.232  1.00 15.07 ? 1973 HOH   A O     1 
HETATM 19102 O  O     . HOH   CA 11 .    ? -23.005 53.845  92.544  1.00 30.26 ? 1974 HOH   A O     1 
HETATM 19103 O  O     . HOH   CA 11 .    ? -3.429  87.643  104.693 1.00 27.17 ? 1975 HOH   A O     1 
HETATM 19104 O  O     . HOH   CA 11 .    ? -69.777 65.115  73.683  1.00 27.19 ? 1976 HOH   A O     1 
HETATM 19105 O  O     . HOH   CA 11 .    ? 6.592   61.056  103.056 1.00 16.95 ? 1977 HOH   A O     1 
HETATM 19106 O  O     . HOH   CA 11 .    ? -57.666 64.696  90.814  1.00 26.10 ? 1978 HOH   A O     1 
HETATM 19107 O  O     . HOH   CA 11 .    ? 3.908   60.465  100.896 1.00 24.06 ? 1979 HOH   A O     1 
HETATM 19108 O  O     . HOH   CA 11 .    ? -36.062 37.560  83.221  1.00 34.87 ? 1980 HOH   A O     1 
HETATM 19109 O  O     . HOH   CA 11 .    ? -54.506 37.499  88.960  1.00 28.84 ? 1981 HOH   A O     1 
HETATM 19110 O  O     . HOH   CA 11 .    ? 16.064  65.166  119.664 1.00 30.69 ? 1982 HOH   A O     1 
HETATM 19111 O  O     . HOH   CA 11 .    ? -22.366 54.631  97.201  1.00 31.23 ? 1983 HOH   A O     1 
HETATM 19112 O  O     . HOH   CA 11 .    ? 18.589  73.204  117.929 1.00 25.21 ? 1984 HOH   A O     1 
HETATM 19113 O  O     . HOH   CA 11 .    ? -10.208 82.320  77.989  1.00 37.70 ? 1985 HOH   A O     1 
HETATM 19114 O  O     . HOH   CA 11 .    ? -36.989 68.307  83.061  1.00 27.45 ? 1986 HOH   A O     1 
HETATM 19115 O  O     . HOH   CA 11 .    ? -60.987 68.650  68.468  1.00 22.18 ? 1987 HOH   A O     1 
HETATM 19116 O  O     . HOH   CA 11 .    ? 25.445  64.377  102.416 1.00 26.46 ? 1988 HOH   A O     1 
HETATM 19117 O  O     . HOH   CA 11 .    ? -57.209 53.459  96.010  1.00 24.41 ? 1989 HOH   A O     1 
HETATM 19118 O  O     . HOH   CA 11 .    ? -44.405 31.664  83.837  1.00 26.99 ? 1990 HOH   A O     1 
HETATM 19119 O  O     . HOH   CA 11 .    ? -27.828 69.239  73.882  1.00 39.56 ? 1991 HOH   A O     1 
HETATM 19120 O  O     . HOH   CA 11 .    ? -38.509 50.532  98.168  1.00 23.65 ? 1992 HOH   A O     1 
HETATM 19121 O  O     . HOH   CA 11 .    ? -17.228 53.265  76.135  1.00 29.82 ? 1993 HOH   A O     1 
HETATM 19122 O  O     . HOH   CA 11 .    ? -54.241 79.332  81.344  1.00 31.75 ? 1994 HOH   A O     1 
HETATM 19123 O  O     . HOH   CA 11 .    ? -59.591 62.961  77.420  1.00 20.64 ? 1995 HOH   A O     1 
HETATM 19124 O  O     . HOH   CA 11 .    ? -16.127 46.993  53.654  1.00 30.67 ? 1996 HOH   A O     1 
HETATM 19125 O  O     . HOH   CA 11 .    ? -45.278 65.439  52.734  1.00 34.17 ? 1997 HOH   A O     1 
HETATM 19126 O  O     . HOH   CA 11 .    ? -63.865 52.936  89.680  1.00 31.22 ? 1998 HOH   A O     1 
HETATM 19127 O  O     . HOH   CA 11 .    ? -37.453 45.500  103.952 1.00 29.72 ? 1999 HOH   A O     1 
HETATM 19128 O  O     . HOH   CA 11 .    ? -14.034 41.942  71.084  1.00 28.37 ? 2000 HOH   A O     1 
HETATM 19129 O  O     . HOH   CA 11 .    ? -38.632 73.260  90.084  1.00 31.87 ? 2001 HOH   A O     1 
HETATM 19130 O  O     . HOH   CA 11 .    ? -24.224 67.325  105.075 1.00 21.86 ? 2002 HOH   A O     1 
HETATM 19131 O  O     . HOH   CA 11 .    ? -32.703 60.605  73.328  1.00 33.67 ? 2003 HOH   A O     1 
HETATM 19132 O  O     . HOH   CA 11 .    ? -59.676 38.527  82.439  1.00 31.22 ? 2004 HOH   A O     1 
HETATM 19133 O  O     . HOH   CA 11 .    ? -0.439  86.596  105.614 1.00 24.36 ? 2005 HOH   A O     1 
HETATM 19134 O  O     . HOH   CA 11 .    ? -9.723  63.920  96.042  1.00 20.54 ? 2006 HOH   A O     1 
HETATM 19135 O  O     . HOH   CA 11 .    ? -38.130 72.899  87.320  1.00 31.46 ? 2007 HOH   A O     1 
HETATM 19136 O  O     . HOH   CA 11 .    ? -31.519 35.141  72.356  1.00 44.42 ? 2008 HOH   A O     1 
HETATM 19137 O  O     . HOH   CA 11 .    ? 2.283   84.002  101.518 1.00 23.22 ? 2009 HOH   A O     1 
HETATM 19138 O  O     . HOH   CA 11 .    ? -22.924 83.370  91.365  1.00 19.51 ? 2010 HOH   A O     1 
HETATM 19139 O  O     . HOH   CA 11 .    ? -9.336  87.211  88.769  1.00 42.73 ? 2011 HOH   A O     1 
HETATM 19140 O  O     . HOH   CA 11 .    ? -32.372 98.082  123.721 1.00 41.27 ? 2012 HOH   A O     1 
HETATM 19141 O  O     . HOH   CA 11 .    ? -49.336 47.666  97.152  1.00 22.29 ? 2013 HOH   A O     1 
HETATM 19142 O  O     . HOH   CA 11 .    ? -50.016 72.321  100.973 1.00 21.90 ? 2014 HOH   A O     1 
HETATM 19143 O  O     . HOH   CA 11 .    ? -60.526 40.981  80.986  1.00 37.01 ? 2015 HOH   A O     1 
HETATM 19144 O  O     . HOH   CA 11 .    ? -62.050 68.038  89.245  1.00 33.56 ? 2016 HOH   A O     1 
HETATM 19145 O  O     . HOH   CA 11 .    ? -64.594 70.784  83.183  1.00 36.70 ? 2017 HOH   A O     1 
HETATM 19146 O  O     . HOH   CA 11 .    ? -53.564 39.855  66.042  1.00 34.98 ? 2018 HOH   A O     1 
HETATM 19147 O  O     . HOH   CA 11 .    ? -41.794 88.718  96.657  1.00 25.74 ? 2019 HOH   A O     1 
HETATM 19148 O  O     . HOH   CA 11 .    ? 2.684   64.942  112.972 1.00 29.91 ? 2020 HOH   A O     1 
HETATM 19149 O  O     . HOH   CA 11 .    ? -44.825 61.087  85.335  1.00 16.36 ? 2021 HOH   A O     1 
HETATM 19150 O  O     . HOH   CA 11 .    ? -46.066 33.534  82.418  1.00 32.56 ? 2022 HOH   A O     1 
HETATM 19151 O  O     . HOH   CA 11 .    ? -64.237 40.166  74.081  1.00 39.36 ? 2023 HOH   A O     1 
HETATM 19152 O  O     . HOH   CA 11 .    ? -0.377  74.028  96.029  1.00 37.03 ? 2024 HOH   A O     1 
HETATM 19153 O  O     . HOH   CA 11 .    ? -22.144 67.447  73.692  1.00 38.09 ? 2025 HOH   A O     1 
HETATM 19154 O  O     . HOH   CA 11 .    ? -30.844 86.851  101.964 1.00 29.86 ? 2026 HOH   A O     1 
HETATM 19155 O  O     . HOH   CA 11 .    ? -7.788  42.452  61.986  1.00 26.60 ? 2027 HOH   A O     1 
HETATM 19156 O  O     . HOH   CA 11 .    ? -16.219 53.857  100.534 1.00 35.93 ? 2028 HOH   A O     1 
HETATM 19157 O  O     . HOH   CA 11 .    ? -34.427 50.225  83.283  1.00 29.78 ? 2029 HOH   A O     1 
HETATM 19158 O  O     . HOH   CA 11 .    ? -12.773 65.905  112.608 1.00 16.97 ? 2030 HOH   A O     1 
HETATM 19159 O  O     . HOH   CA 11 .    ? -35.123 94.918  96.074  1.00 27.79 ? 2031 HOH   A O     1 
HETATM 19160 O  O     . HOH   CA 11 .    ? -20.926 43.709  70.119  1.00 41.65 ? 2032 HOH   A O     1 
HETATM 19161 O  O     . HOH   CA 11 .    ? -8.413  87.479  92.926  1.00 39.49 ? 2033 HOH   A O     1 
HETATM 19162 O  O     . HOH   CA 11 .    ? -50.197 27.450  77.131  1.00 34.09 ? 2034 HOH   A O     1 
HETATM 19163 O  O     . HOH   CA 11 .    ? -17.843 85.477  77.359  1.00 27.91 ? 2035 HOH   A O     1 
HETATM 19164 O  O     . HOH   CA 11 .    ? -4.289  72.934  76.963  1.00 27.89 ? 2036 HOH   A O     1 
HETATM 19165 O  O     . HOH   CA 11 .    ? -7.612  50.792  52.975  1.00 27.08 ? 2037 HOH   A O     1 
HETATM 19166 O  O     . HOH   CA 11 .    ? -40.037 39.408  98.424  1.00 33.29 ? 2038 HOH   A O     1 
HETATM 19167 O  O     . HOH   CA 11 .    ? -19.895 90.755  97.554  1.00 37.20 ? 2039 HOH   A O     1 
HETATM 19168 O  O     . HOH   CA 11 .    ? -40.725 81.652  110.558 1.00 28.37 ? 2040 HOH   A O     1 
HETATM 19169 O  O     . HOH   CA 11 .    ? -8.128  72.427  100.449 1.00 25.81 ? 2041 HOH   A O     1 
HETATM 19170 O  O     . HOH   CA 11 .    ? -28.224 69.388  85.694  1.00 29.67 ? 2042 HOH   A O     1 
HETATM 19171 O  O     . HOH   CA 11 .    ? -22.638 98.520  100.132 1.00 35.19 ? 2043 HOH   A O     1 
HETATM 19172 O  O     . HOH   CA 11 .    ? -19.735 84.989  75.417  1.00 31.22 ? 2044 HOH   A O     1 
HETATM 19173 O  O     . HOH   CA 11 .    ? -53.713 68.796  93.293  1.00 24.14 ? 2045 HOH   A O     1 
HETATM 19174 O  O     . HOH   CA 11 .    ? -54.436 47.508  67.162  1.00 28.69 ? 2046 HOH   A O     1 
HETATM 19175 O  O     . HOH   CA 11 .    ? -48.993 29.493  73.715  1.00 37.50 ? 2047 HOH   A O     1 
HETATM 19176 O  O     . HOH   CA 11 .    ? -25.810 94.021  78.131  1.00 31.80 ? 2048 HOH   A O     1 
HETATM 19177 O  O     . HOH   CA 11 .    ? -67.900 37.271  75.445  1.00 36.10 ? 2049 HOH   A O     1 
HETATM 19178 O  O     . HOH   CA 11 .    ? -8.264  77.184  91.843  1.00 22.55 ? 2050 HOH   A O     1 
HETATM 19179 O  O     . HOH   CA 11 .    ? 10.449  67.087  111.749 1.00 35.40 ? 2051 HOH   A O     1 
HETATM 19180 O  O     . HOH   CA 11 .    ? -3.528  82.296  97.330  1.00 24.33 ? 2052 HOH   A O     1 
HETATM 19181 O  O     . HOH   CA 11 .    ? -25.299 79.168  94.895  1.00 20.88 ? 2053 HOH   A O     1 
HETATM 19182 O  O     . HOH   CA 11 .    ? -45.373 63.475  105.205 1.00 38.11 ? 2054 HOH   A O     1 
HETATM 19183 O  O     . HOH   CA 11 .    ? -34.330 56.535  105.233 1.00 23.43 ? 2055 HOH   A O     1 
HETATM 19184 O  O     . HOH   CA 11 .    ? -38.144 67.657  97.991  1.00 26.15 ? 2056 HOH   A O     1 
HETATM 19185 O  O     . HOH   CA 11 .    ? -1.804  79.807  88.047  1.00 37.07 ? 2057 HOH   A O     1 
HETATM 19186 O  O     . HOH   CA 11 .    ? 8.373   68.205  114.444 1.00 31.00 ? 2058 HOH   A O     1 
HETATM 19187 O  O     . HOH   CA 11 .    ? -39.454 76.608  93.107  1.00 22.99 ? 2059 HOH   A O     1 
HETATM 19188 O  O     . HOH   CA 11 .    ? -23.502 62.683  66.249  1.00 37.71 ? 2060 HOH   A O     1 
HETATM 19189 O  O     . HOH   CA 11 .    ? -40.883 80.158  87.488  1.00 20.11 ? 2061 HOH   A O     1 
HETATM 19190 O  O     . HOH   CA 11 .    ? -44.243 89.017  112.776 1.00 44.17 ? 2062 HOH   A O     1 
HETATM 19191 O  O     . HOH   CA 11 .    ? -13.553 54.197  77.215  1.00 24.59 ? 2063 HOH   A O     1 
HETATM 19192 O  O     . HOH   CA 11 .    ? -36.984 49.897  100.552 1.00 27.22 ? 2064 HOH   A O     1 
HETATM 19193 O  O     . HOH   CA 11 .    ? 1.014   74.776  107.237 1.00 27.16 ? 2065 HOH   A O     1 
HETATM 19194 O  O     . HOH   CA 11 .    ? -27.085 51.951  98.524  1.00 22.78 ? 2066 HOH   A O     1 
HETATM 19195 O  O     . HOH   CA 11 .    ? -59.101 42.688  89.212  1.00 29.55 ? 2067 HOH   A O     1 
HETATM 19196 O  O     . HOH   CA 11 .    ? -33.886 98.791  101.387 1.00 47.43 ? 2068 HOH   A O     1 
HETATM 19197 O  O     . HOH   CA 11 .    ? -9.864  39.972  61.161  1.00 41.33 ? 2069 HOH   A O     1 
HETATM 19198 O  O     . HOH   CA 11 .    ? -14.247 85.022  76.966  1.00 30.54 ? 2070 HOH   A O     1 
HETATM 19199 O  O     . HOH   CA 11 .    ? -39.234 66.784  94.257  1.00 25.98 ? 2071 HOH   A O     1 
HETATM 19200 O  O     . HOH   CA 11 .    ? -7.165  93.632  113.161 1.00 31.94 ? 2072 HOH   A O     1 
HETATM 19201 O  O     . HOH   CA 11 .    ? -38.523 70.392  81.644  1.00 21.88 ? 2073 HOH   A O     1 
HETATM 19202 O  O     . HOH   CA 11 .    ? -29.793 83.457  101.191 1.00 24.50 ? 2074 HOH   A O     1 
HETATM 19203 O  O     . HOH   CA 11 .    ? -25.542 88.335  116.009 1.00 22.68 ? 2075 HOH   A O     1 
HETATM 19204 O  O     . HOH   CA 11 .    ? -22.595 48.217  83.075  1.00 35.03 ? 2076 HOH   A O     1 
HETATM 19205 O  O     . HOH   CA 11 .    ? -52.095 86.928  103.604 1.00 40.76 ? 2077 HOH   A O     1 
HETATM 19206 O  O     . HOH   CA 11 .    ? 2.344   86.524  125.967 1.00 38.29 ? 2078 HOH   A O     1 
HETATM 19207 O  O     . HOH   CA 11 .    ? -29.161 66.899  96.426  1.00 39.37 ? 2079 HOH   A O     1 
HETATM 19208 O  O     . HOH   CA 11 .    ? -38.895 71.167  84.180  1.00 24.56 ? 2080 HOH   A O     1 
HETATM 19209 O  O     . HOH   CA 11 .    ? 2.225   76.493  116.741 1.00 24.05 ? 2081 HOH   A O     1 
HETATM 19210 O  O     . HOH   CA 11 .    ? -29.046 54.941  111.307 1.00 35.28 ? 2082 HOH   A O     1 
HETATM 19211 O  O     . HOH   CA 11 .    ? -36.975 60.551  96.146  1.00 19.17 ? 2083 HOH   A O     1 
HETATM 19212 O  O     . HOH   CA 11 .    ? -33.342 98.256  93.138  1.00 45.09 ? 2084 HOH   A O     1 
HETATM 19213 O  O     . HOH   CA 11 .    ? -43.964 59.429  87.364  1.00 14.81 ? 2085 HOH   A O     1 
HETATM 19214 O  O     . HOH   CA 11 .    ? -53.634 72.346  68.065  1.00 25.77 ? 2086 HOH   A O     1 
HETATM 19215 O  O     . HOH   CA 11 .    ? 22.634  76.220  114.523 1.00 25.22 ? 2087 HOH   A O     1 
HETATM 19216 O  O     . HOH   CA 11 .    ? -34.285 96.459  112.457 1.00 43.28 ? 2088 HOH   A O     1 
HETATM 19217 O  O     . HOH   CA 11 .    ? -9.342  60.561  84.185  1.00 22.92 ? 2089 HOH   A O     1 
HETATM 19218 O  O     . HOH   CA 11 .    ? -14.097 55.719  111.333 1.00 32.60 ? 2090 HOH   A O     1 
HETATM 19219 O  O     . HOH   CA 11 .    ? -31.391 41.433  98.141  1.00 35.71 ? 2091 HOH   A O     1 
HETATM 19220 O  O     . HOH   CA 11 .    ? -30.792 95.912  104.803 1.00 31.88 ? 2092 HOH   A O     1 
HETATM 19221 O  O     . HOH   CA 11 .    ? -42.349 56.743  89.291  1.00 17.65 ? 2093 HOH   A O     1 
HETATM 19222 O  O     . HOH   CA 11 .    ? -40.483 64.832  61.985  1.00 30.21 ? 2094 HOH   A O     1 
HETATM 19223 O  O     . HOH   CA 11 .    ? 8.601   64.973  94.176  1.00 28.79 ? 2095 HOH   A O     1 
HETATM 19224 O  O     . HOH   CA 11 .    ? -36.718 69.510  119.121 1.00 31.47 ? 2096 HOH   A O     1 
HETATM 19225 O  O     . HOH   CA 11 .    ? -59.146 58.395  76.725  1.00 17.08 ? 2097 HOH   A O     1 
HETATM 19226 O  O     . HOH   CA 11 .    ? -28.628 94.974  88.952  1.00 34.27 ? 2098 HOH   A O     1 
HETATM 19227 O  O     . HOH   CA 11 .    ? -14.185 95.309  119.415 1.00 34.28 ? 2099 HOH   A O     1 
HETATM 19228 O  O     . HOH   CA 11 .    ? 22.635  72.931  98.157  1.00 34.65 ? 2100 HOH   A O     1 
HETATM 19229 O  O     . HOH   CA 11 .    ? -47.940 53.848  104.079 1.00 41.12 ? 2101 HOH   A O     1 
HETATM 19230 O  O     . HOH   CA 11 .    ? -33.109 40.874  94.943  1.00 41.51 ? 2102 HOH   A O     1 
HETATM 19231 O  O     . HOH   CA 11 .    ? -15.004 53.128  75.581  1.00 29.48 ? 2103 HOH   A O     1 
HETATM 19232 O  O     . HOH   CA 11 .    ? -47.934 80.061  95.790  1.00 35.12 ? 2104 HOH   A O     1 
HETATM 19233 O  O     . HOH   CA 11 .    ? -4.769  82.236  124.976 1.00 37.88 ? 2105 HOH   A O     1 
HETATM 19234 O  O     . HOH   CA 11 .    ? 6.970   84.649  94.221  1.00 41.64 ? 2106 HOH   A O     1 
HETATM 19235 O  O     . HOH   CA 11 .    ? -8.477  81.931  104.859 1.00 19.46 ? 2107 HOH   A O     1 
HETATM 19236 O  O     . HOH   CA 11 .    ? -39.526 88.579  119.016 1.00 32.74 ? 2108 HOH   A O     1 
HETATM 19237 O  O     . HOH   CA 11 .    ? -26.658 97.014  88.998  1.00 36.88 ? 2109 HOH   A O     1 
HETATM 19238 O  O     . HOH   CA 11 .    ? 14.007  78.398  120.779 1.00 29.66 ? 2110 HOH   A O     1 
HETATM 19239 O  O     . HOH   CA 11 .    ? 1.144   62.257  111.115 1.00 29.68 ? 2111 HOH   A O     1 
HETATM 19240 O  O     . HOH   CA 11 .    ? -31.241 74.203  87.688  1.00 33.13 ? 2112 HOH   A O     1 
HETATM 19241 O  O     . HOH   CA 11 .    ? -67.699 64.292  85.145  1.00 31.08 ? 2113 HOH   A O     1 
HETATM 19242 O  O     . HOH   CA 11 .    ? -25.610 68.077  90.432  1.00 26.77 ? 2114 HOH   A O     1 
HETATM 19243 O  O     . HOH   CA 11 .    ? -1.639  80.336  111.734 1.00 28.40 ? 2115 HOH   A O     1 
HETATM 19244 O  O     . HOH   CA 11 .    ? -49.729 35.498  87.744  1.00 29.00 ? 2116 HOH   A O     1 
HETATM 19245 O  O     . HOH   CA 11 .    ? -25.137 82.680  72.410  1.00 31.49 ? 2117 HOH   A O     1 
HETATM 19246 O  O     . HOH   CA 11 .    ? -20.957 73.630  99.516  1.00 28.41 ? 2118 HOH   A O     1 
HETATM 19247 O  O     . HOH   CA 11 .    ? 1.109   66.395  96.451  1.00 22.35 ? 2119 HOH   A O     1 
HETATM 19248 O  O     . HOH   CA 11 .    ? 2.667   74.287  109.225 1.00 26.31 ? 2120 HOH   A O     1 
HETATM 19249 O  O     . HOH   CA 11 .    ? 19.130  81.947  113.106 1.00 29.40 ? 2121 HOH   A O     1 
HETATM 19250 O  O     . HOH   CA 11 .    ? -35.461 97.758  115.941 1.00 37.51 ? 2122 HOH   A O     1 
HETATM 19251 O  O     . HOH   CA 11 .    ? -13.139 69.081  73.791  1.00 31.72 ? 2123 HOH   A O     1 
HETATM 19252 O  O     . HOH   CA 11 .    ? -6.590  76.675  128.195 1.00 37.92 ? 2124 HOH   A O     1 
HETATM 19253 O  O     . HOH   CA 11 .    ? -44.966 85.730  99.743  1.00 39.10 ? 2125 HOH   A O     1 
HETATM 19254 O  O     . HOH   CA 11 .    ? -26.510 84.240  74.020  1.00 31.37 ? 2126 HOH   A O     1 
HETATM 19255 O  O     . HOH   CA 11 .    ? -3.512  56.573  95.261  1.00 39.12 ? 2127 HOH   A O     1 
HETATM 19256 O  O     . HOH   CA 11 .    ? 10.803  61.108  115.068 1.00 33.35 ? 2128 HOH   A O     1 
HETATM 19257 O  O     . HOH   CA 11 .    ? -55.192 26.587  91.567  1.00 34.13 ? 2129 HOH   A O     1 
HETATM 19258 O  O     . HOH   CA 11 .    ? -35.431 66.373  94.341  1.00 40.58 ? 2130 HOH   A O     1 
HETATM 19259 O  O     . HOH   CA 11 .    ? -23.002 75.094  99.564  1.00 23.80 ? 2131 HOH   A O     1 
HETATM 19260 O  O     . HOH   CA 11 .    ? -1.732  54.458  101.677 1.00 22.67 ? 2132 HOH   A O     1 
HETATM 19261 O  O     . HOH   CA 11 .    ? -42.709 77.616  78.333  1.00 22.71 ? 2133 HOH   A O     1 
HETATM 19262 O  O     . HOH   CA 11 .    ? -27.458 61.910  88.864  1.00 20.18 ? 2134 HOH   A O     1 
HETATM 19263 O  O     . HOH   CA 11 .    ? -24.828 69.258  74.384  1.00 27.84 ? 2135 HOH   A O     1 
HETATM 19264 O  O     . HOH   CA 11 .    ? -47.337 97.728  103.192 1.00 45.44 ? 2136 HOH   A O     1 
HETATM 19265 O  O     . HOH   CA 11 .    ? -32.272 52.349  85.909  1.00 27.04 ? 2137 HOH   A O     1 
HETATM 19266 O  O     . HOH   CA 11 .    ? -62.636 67.550  66.275  1.00 28.81 ? 2138 HOH   A O     1 
HETATM 19267 O  O     . HOH   CA 11 .    ? -1.380  70.077  116.181 1.00 24.84 ? 2139 HOH   A O     1 
HETATM 19268 O  O     . HOH   CA 11 .    ? -20.011 79.000  114.743 1.00 19.61 ? 2140 HOH   A O     1 
HETATM 19269 O  O     . HOH   CA 11 .    ? -64.542 47.873  76.298  1.00 33.19 ? 2141 HOH   A O     1 
HETATM 19270 O  O     . HOH   CA 11 .    ? -28.241 64.933  64.190  1.00 43.74 ? 2142 HOH   A O     1 
HETATM 19271 O  O     . HOH   CA 11 .    ? -39.368 86.407  89.217  1.00 27.69 ? 2143 HOH   A O     1 
HETATM 19272 O  O     . HOH   CA 11 .    ? -32.457 64.494  121.794 1.00 27.89 ? 2144 HOH   A O     1 
HETATM 19273 O  O     . HOH   CA 11 .    ? -46.998 34.822  100.715 1.00 37.24 ? 2145 HOH   A O     1 
HETATM 19274 O  O     . HOH   CA 11 .    ? -9.050  51.943  107.352 1.00 29.04 ? 2146 HOH   A O     1 
HETATM 19275 O  O     . HOH   CA 11 .    ? -15.204 59.026  126.447 1.00 28.65 ? 2147 HOH   A O     1 
HETATM 19276 O  O     . HOH   CA 11 .    ? -17.279 54.917  78.292  1.00 31.81 ? 2148 HOH   A O     1 
HETATM 19277 O  O     . HOH   CA 11 .    ? -20.996 58.218  97.168  1.00 22.30 ? 2149 HOH   A O     1 
HETATM 19278 O  O     . HOH   CA 11 .    ? -57.033 39.208  91.116  1.00 36.98 ? 2150 HOH   A O     1 
HETATM 19279 O  O     . HOH   CA 11 .    ? -18.515 68.858  104.427 1.00 21.76 ? 2151 HOH   A O     1 
HETATM 19280 O  O     . HOH   CA 11 .    ? -22.980 94.561  118.036 1.00 31.77 ? 2152 HOH   A O     1 
HETATM 19281 O  O     . HOH   CA 11 .    ? -39.739 84.701  103.604 1.00 28.60 ? 2153 HOH   A O     1 
HETATM 19282 O  O     . HOH   CA 11 .    ? -7.254  64.653  94.234  1.00 36.62 ? 2154 HOH   A O     1 
HETATM 19283 O  O     . HOH   CA 11 .    ? -2.193  77.932  75.608  1.00 26.26 ? 2155 HOH   A O     1 
HETATM 19284 O  O     . HOH   CA 11 .    ? -30.773 59.303  81.801  1.00 39.95 ? 2156 HOH   A O     1 
HETATM 19285 O  O     . HOH   CA 11 .    ? -30.905 66.279  126.651 1.00 36.08 ? 2157 HOH   A O     1 
HETATM 19286 O  O     . HOH   CA 11 .    ? -3.704  82.115  109.870 1.00 30.41 ? 2158 HOH   A O     1 
HETATM 19287 O  O     . HOH   CA 11 .    ? -9.091  83.743  80.965  1.00 39.70 ? 2159 HOH   A O     1 
HETATM 19288 O  O     . HOH   CA 11 .    ? -31.056 83.733  123.188 1.00 23.83 ? 2160 HOH   A O     1 
HETATM 19289 O  O     . HOH   CA 11 .    ? -65.675 69.165  69.113  1.00 30.46 ? 2161 HOH   A O     1 
HETATM 19290 O  O     . HOH   CA 11 .    ? -43.067 49.874  55.665  1.00 30.76 ? 2162 HOH   A O     1 
HETATM 19291 O  O     . HOH   CA 11 .    ? -40.412 96.941  103.376 1.00 37.40 ? 2163 HOH   A O     1 
HETATM 19292 O  O     . HOH   CA 11 .    ? 10.212  81.255  125.089 1.00 30.36 ? 2164 HOH   A O     1 
HETATM 19293 O  O     . HOH   CA 11 .    ? -22.396 76.820  70.124  1.00 23.59 ? 2165 HOH   A O     1 
HETATM 19294 O  O     . HOH   CA 11 .    ? -36.044 44.335  66.551  1.00 37.61 ? 2166 HOH   A O     1 
HETATM 19295 O  O     . HOH   CA 11 .    ? -26.706 39.324  77.307  1.00 39.45 ? 2167 HOH   A O     1 
HETATM 19296 O  O     . HOH   CA 11 .    ? -37.941 40.465  74.243  1.00 32.03 ? 2168 HOH   A O     1 
HETATM 19297 O  O     . HOH   CA 11 .    ? -34.292 55.220  71.092  1.00 37.73 ? 2169 HOH   A O     1 
HETATM 19298 O  O     . HOH   CA 11 .    ? -37.463 65.904  109.152 1.00 37.53 ? 2170 HOH   A O     1 
HETATM 19299 O  O     . HOH   CA 11 .    ? -43.242 77.448  67.852  1.00 27.24 ? 2171 HOH   A O     1 
HETATM 19300 O  O     . HOH   CA 11 .    ? -41.568 88.589  93.838  1.00 29.16 ? 2172 HOH   A O     1 
HETATM 19301 O  O     . HOH   CA 11 .    ? -14.063 86.562  100.712 1.00 25.03 ? 2173 HOH   A O     1 
HETATM 19302 O  O     . HOH   CA 11 .    ? -43.764 85.326  94.719  1.00 36.68 ? 2174 HOH   A O     1 
HETATM 19303 O  O     . HOH   CA 11 .    ? 23.298  58.364  103.376 1.00 32.91 ? 2175 HOH   A O     1 
HETATM 19304 O  O     . HOH   CA 11 .    ? -22.972 55.093  88.419  1.00 35.27 ? 2176 HOH   A O     1 
HETATM 19305 O  O     . HOH   CA 11 .    ? -25.490 59.302  114.256 1.00 24.43 ? 2177 HOH   A O     1 
HETATM 19306 O  O     . HOH   CA 11 .    ? -38.229 40.460  64.635  1.00 45.78 ? 2178 HOH   A O     1 
HETATM 19307 O  O     . HOH   CA 11 .    ? -33.060 57.333  72.275  1.00 34.16 ? 2179 HOH   A O     1 
HETATM 19308 O  O     . HOH   CA 11 .    ? -67.252 57.589  90.183  1.00 37.80 ? 2180 HOH   A O     1 
HETATM 19309 O  O     . HOH   CA 11 .    ? 28.430  64.162  112.333 1.00 31.10 ? 2181 HOH   A O     1 
HETATM 19310 O  O     . HOH   CA 11 .    ? -0.993  77.483  126.502 1.00 38.62 ? 2182 HOH   A O     1 
HETATM 19311 O  O     . HOH   CA 11 .    ? -28.485 42.146  92.749  1.00 47.63 ? 2183 HOH   A O     1 
HETATM 19312 O  O     . HOH   CA 11 .    ? -45.248 57.533  102.028 1.00 27.01 ? 2184 HOH   A O     1 
HETATM 19313 O  O     . HOH   CA 11 .    ? 2.466   77.875  97.962  1.00 24.45 ? 2185 HOH   A O     1 
HETATM 19314 O  O     . HOH   CA 11 .    ? -18.225 49.553  78.845  1.00 38.85 ? 2186 HOH   A O     1 
HETATM 19315 O  O     . HOH   CA 11 .    ? -39.758 61.555  94.297  1.00 20.45 ? 2187 HOH   A O     1 
HETATM 19316 O  O     . HOH   CA 11 .    ? -48.653 78.305  74.927  1.00 29.83 ? 2188 HOH   A O     1 
HETATM 19317 O  O     . HOH   CA 11 .    ? -11.512 43.658  74.069  1.00 27.61 ? 2189 HOH   A O     1 
HETATM 19318 O  O     . HOH   CA 11 .    ? -4.667  50.735  56.487  1.00 33.84 ? 2190 HOH   A O     1 
HETATM 19319 O  O     . HOH   CA 11 .    ? -2.505  62.584  113.094 1.00 35.25 ? 2191 HOH   A O     1 
HETATM 19320 O  O     . HOH   CA 11 .    ? -36.383 71.434  121.115 1.00 36.02 ? 2192 HOH   A O     1 
HETATM 19321 O  O     . HOH   CA 11 .    ? -4.549  54.937  61.410  1.00 33.66 ? 2193 HOH   A O     1 
HETATM 19322 O  O     . HOH   CA 11 .    ? -2.997  75.910  77.276  1.00 20.91 ? 2194 HOH   A O     1 
HETATM 19323 O  O     . HOH   CA 11 .    ? -37.142 88.012  83.124  1.00 32.52 ? 2195 HOH   A O     1 
HETATM 19324 O  O     . HOH   CA 11 .    ? -61.295 61.730  62.538  1.00 30.63 ? 2196 HOH   A O     1 
HETATM 19325 O  O     . HOH   CA 11 .    ? -64.696 55.279  80.648  1.00 24.70 ? 2197 HOH   A O     1 
HETATM 19326 O  O     . HOH   CA 11 .    ? -37.008 37.941  102.355 1.00 42.62 ? 2198 HOH   A O     1 
HETATM 19327 O  O     . HOH   CA 11 .    ? -47.676 84.929  101.582 1.00 35.92 ? 2199 HOH   A O     1 
HETATM 19328 O  O     . HOH   CA 11 .    ? -5.197  55.731  101.117 1.00 29.97 ? 2200 HOH   A O     1 
HETATM 19329 O  O     . HOH   CA 11 .    ? -49.016 65.475  54.049  1.00 25.12 ? 2201 HOH   A O     1 
HETATM 19330 O  O     . HOH   CA 11 .    ? -11.288 54.007  100.306 1.00 26.46 ? 2202 HOH   A O     1 
HETATM 19331 O  O     . HOH   CA 11 .    ? -43.711 90.479  99.856  1.00 28.64 ? 2203 HOH   A O     1 
HETATM 19332 O  O     . HOH   CA 11 .    ? -26.897 62.879  86.330  1.00 21.82 ? 2204 HOH   A O     1 
HETATM 19333 O  O     . HOH   CA 11 .    ? -0.328  67.585  117.564 1.00 34.00 ? 2205 HOH   A O     1 
HETATM 19334 O  O     . HOH   CA 11 .    ? -56.265 25.351  88.289  1.00 37.87 ? 2206 HOH   A O     1 
HETATM 19335 O  O     . HOH   CA 11 .    ? 5.524   58.627  97.221  1.00 29.46 ? 2207 HOH   A O     1 
HETATM 19336 O  O     . HOH   CA 11 .    ? -31.115 70.235  129.274 1.00 41.74 ? 2208 HOH   A O     1 
HETATM 19337 O  O     . HOH   CA 11 .    ? -64.144 47.684  73.807  1.00 36.84 ? 2209 HOH   A O     1 
HETATM 19338 O  O     . HOH   CA 11 .    ? -11.723 53.200  102.868 1.00 40.30 ? 2210 HOH   A O     1 
HETATM 19339 O  O     . HOH   CA 11 .    ? -36.232 80.636  75.615  1.00 24.47 ? 2211 HOH   A O     1 
HETATM 19340 O  O     . HOH   CA 11 .    ? -53.553 49.398  60.247  1.00 28.68 ? 2212 HOH   A O     1 
HETATM 19341 O  O     . HOH   CA 11 .    ? 21.514  72.763  115.731 1.00 26.10 ? 2213 HOH   A O     1 
HETATM 19342 O  O     . HOH   CA 11 .    ? -12.481 81.796  72.562  1.00 38.52 ? 2214 HOH   A O     1 
HETATM 19343 O  O     . HOH   CA 11 .    ? 0.302   64.229  107.101 1.00 17.96 ? 2215 HOH   A O     1 
HETATM 19344 O  O     . HOH   CA 11 .    ? -49.955 72.989  62.710  1.00 20.27 ? 2216 HOH   A O     1 
HETATM 19345 O  O     . HOH   CA 11 .    ? -43.855 37.398  104.655 1.00 37.93 ? 2217 HOH   A O     1 
HETATM 19346 O  O     . HOH   CA 11 .    ? -12.891 53.596  110.404 1.00 34.30 ? 2218 HOH   A O     1 
HETATM 19347 O  O     . HOH   CA 11 .    ? -60.546 63.825  100.842 1.00 42.23 ? 2219 HOH   A O     1 
HETATM 19348 O  O     . HOH   CA 11 .    ? -55.197 41.893  96.585  1.00 32.15 ? 2220 HOH   A O     1 
HETATM 19349 O  O     . HOH   CA 11 .    ? 18.273  75.209  96.487  1.00 36.06 ? 2221 HOH   A O     1 
HETATM 19350 O  O     . HOH   CA 11 .    ? -45.685 55.021  91.973  1.00 16.27 ? 2222 HOH   A O     1 
HETATM 19351 O  O     . HOH   CA 11 .    ? -37.574 86.076  101.764 1.00 24.75 ? 2223 HOH   A O     1 
HETATM 19352 O  O     . HOH   CA 11 .    ? -2.208  90.896  105.448 1.00 28.88 ? 2224 HOH   A O     1 
HETATM 19353 O  O     . HOH   CA 11 .    ? 12.213  65.207  118.448 1.00 34.68 ? 2225 HOH   A O     1 
HETATM 19354 O  O     . HOH   CA 11 .    ? -26.998 79.870  69.953  1.00 38.95 ? 2226 HOH   A O     1 
HETATM 19355 O  O     . HOH   CA 11 .    ? -16.347 43.140  71.913  1.00 38.14 ? 2227 HOH   A O     1 
HETATM 19356 O  O     . HOH   CA 11 .    ? -40.900 70.487  92.712  1.00 27.24 ? 2228 HOH   A O     1 
HETATM 19357 O  O     . HOH   CA 11 .    ? -27.361 90.365  115.553 1.00 24.69 ? 2229 HOH   A O     1 
HETATM 19358 O  O     . HOH   CA 11 .    ? -56.370 68.834  99.986  1.00 36.26 ? 2230 HOH   A O     1 
HETATM 19359 O  O     . HOH   CA 11 .    ? 6.963   55.223  98.697  1.00 19.33 ? 2231 HOH   A O     1 
HETATM 19360 O  O     . HOH   CA 11 .    ? -18.441 39.607  68.425  1.00 40.58 ? 2232 HOH   A O     1 
HETATM 19361 O  O     . HOH   CA 11 .    ? -40.033 37.983  84.947  1.00 28.93 ? 2233 HOH   A O     1 
HETATM 19362 O  O     . HOH   CA 11 .    ? -15.075 55.394  51.015  1.00 38.36 ? 2234 HOH   A O     1 
HETATM 19363 O  O     . HOH   CA 11 .    ? -65.674 72.497  71.727  1.00 39.31 ? 2235 HOH   A O     1 
HETATM 19364 O  O     . HOH   CA 11 .    ? -10.460 63.748  115.457 1.00 20.95 ? 2236 HOH   A O     1 
HETATM 19365 O  O     . HOH   CA 11 .    ? -66.342 68.793  83.856  1.00 29.63 ? 2237 HOH   A O     1 
HETATM 19366 O  O     . HOH   CA 11 .    ? -63.400 45.039  67.648  1.00 37.62 ? 2238 HOH   A O     1 
HETATM 19367 O  O     . HOH   CA 11 .    ? -63.095 62.228  97.706  1.00 31.88 ? 2239 HOH   A O     1 
HETATM 19368 O  O     . HOH   CA 11 .    ? -3.486  75.113  101.814 1.00 29.26 ? 2240 HOH   A O     1 
HETATM 19369 O  O     . HOH   CA 11 .    ? -54.235 45.159  91.861  1.00 28.60 ? 2241 HOH   A O     1 
HETATM 19370 O  O     . HOH   CA 11 .    ? -20.193 69.182  70.591  1.00 42.04 ? 2242 HOH   A O     1 
HETATM 19371 O  O     . HOH   CA 11 .    ? -23.390 89.106  102.030 1.00 26.95 ? 2243 HOH   A O     1 
HETATM 19372 O  O     . HOH   CA 11 .    ? -11.173 84.101  133.947 1.00 44.14 ? 2244 HOH   A O     1 
HETATM 19373 O  O     . HOH   CA 11 .    ? -34.298 42.556  70.011  1.00 38.73 ? 2245 HOH   A O     1 
HETATM 19374 O  O     . HOH   CA 11 .    ? -43.155 56.310  91.859  1.00 15.91 ? 2246 HOH   A O     1 
HETATM 19375 O  O     . HOH   CA 11 .    ? -56.638 40.316  67.521  1.00 35.42 ? 2247 HOH   A O     1 
HETATM 19376 O  O     . HOH   CA 11 .    ? -10.837 86.942  91.308  1.00 34.12 ? 2248 HOH   A O     1 
HETATM 19377 O  O     . HOH   CA 11 .    ? 10.998  85.151  124.430 1.00 26.58 ? 2249 HOH   A O     1 
HETATM 19378 O  O     . HOH   CA 11 .    ? 10.656  64.947  114.209 1.00 41.00 ? 2250 HOH   A O     1 
HETATM 19379 O  O     . HOH   CA 11 .    ? -52.132 30.024  72.939  1.00 37.73 ? 2251 HOH   A O     1 
HETATM 19380 O  O     . HOH   CA 11 .    ? -47.010 77.140  91.996  1.00 24.18 ? 2252 HOH   A O     1 
HETATM 19381 O  O     . HOH   CA 11 .    ? -52.014 77.508  101.431 1.00 37.91 ? 2253 HOH   A O     1 
HETATM 19382 O  O     . HOH   CA 11 .    ? -25.590 88.121  132.690 1.00 39.46 ? 2254 HOH   A O     1 
HETATM 19383 O  O     . HOH   CA 11 .    ? 1.773   86.190  98.616  1.00 37.92 ? 2255 HOH   A O     1 
HETATM 19384 O  O     . HOH   CA 11 .    ? -41.657 64.614  58.377  1.00 25.13 ? 2256 HOH   A O     1 
HETATM 19385 O  O     . HOH   CA 11 .    ? -61.280 41.740  66.966  1.00 42.81 ? 2257 HOH   A O     1 
HETATM 19386 O  O     . HOH   CA 11 .    ? -36.663 82.599  120.671 1.00 29.42 ? 2258 HOH   A O     1 
HETATM 19387 O  O     . HOH   CA 11 .    ? -5.664  90.711  119.701 1.00 37.74 ? 2259 HOH   A O     1 
HETATM 19388 O  O     . HOH   CA 11 .    ? -18.943 59.740  108.058 1.00 32.69 ? 2260 HOH   A O     1 
HETATM 19389 O  O     . HOH   CA 11 .    ? -64.285 58.234  67.034  1.00 34.97 ? 2261 HOH   A O     1 
HETATM 19390 O  O     . HOH   CA 11 .    ? -49.581 54.376  73.837  1.00 18.82 ? 2262 HOH   A O     1 
HETATM 19391 O  O     . HOH   CA 11 .    ? 1.189   57.199  107.489 1.00 18.95 ? 2263 HOH   A O     1 
HETATM 19392 O  O     . HOH   CA 11 .    ? -26.840 92.140  131.996 1.00 44.92 ? 2264 HOH   A O     1 
HETATM 19393 O  O     . HOH   CA 11 .    ? -53.017 37.350  61.024  1.00 44.22 ? 2265 HOH   A O     1 
HETATM 19394 O  O     . HOH   CA 11 .    ? -26.010 69.645  95.644  1.00 30.94 ? 2266 HOH   A O     1 
HETATM 19395 O  O     . HOH   CA 11 .    ? 4.363   86.014  100.840 1.00 27.11 ? 2267 HOH   A O     1 
HETATM 19396 O  O     . HOH   CA 11 .    ? -30.295 54.430  57.664  1.00 39.16 ? 2268 HOH   A O     1 
HETATM 19397 O  O     . HOH   CA 11 .    ? -56.919 32.320  87.694  1.00 24.75 ? 2269 HOH   A O     1 
HETATM 19398 O  O     . HOH   CA 11 .    ? -56.828 73.396  96.148  1.00 33.34 ? 2270 HOH   A O     1 
HETATM 19399 O  O     . HOH   CA 11 .    ? -12.201 39.972  68.309  1.00 41.21 ? 2271 HOH   A O     1 
HETATM 19400 O  O     . HOH   CA 11 .    ? -18.122 53.998  98.501  1.00 30.23 ? 2272 HOH   A O     1 
HETATM 19401 O  O     . HOH   CA 11 .    ? -45.940 79.805  71.398  1.00 39.26 ? 2273 HOH   A O     1 
HETATM 19402 O  O     . HOH   CA 11 .    ? -10.574 64.244  124.991 1.00 39.54 ? 2274 HOH   A O     1 
HETATM 19403 O  O     . HOH   CA 11 .    ? -11.024 66.744  127.265 1.00 36.30 ? 2275 HOH   A O     1 
HETATM 19404 O  O     . HOH   CA 11 .    ? 13.235  57.110  116.204 1.00 41.75 ? 2276 HOH   A O     1 
HETATM 19405 O  O     . HOH   CA 11 .    ? -17.033 54.574  117.004 1.00 35.78 ? 2277 HOH   A O     1 
HETATM 19406 O  O     . HOH   CA 11 .    ? 22.286  65.447  92.843  1.00 44.23 ? 2278 HOH   A O     1 
HETATM 19407 O  O     . HOH   CA 11 .    ? -30.744 91.293  111.220 1.00 33.33 ? 2279 HOH   A O     1 
HETATM 19408 O  O     . HOH   CA 11 .    ? -31.681 94.306  126.995 1.00 34.40 ? 2280 HOH   A O     1 
HETATM 19409 O  O     . HOH   CA 11 .    ? -32.271 98.414  99.296  1.00 42.71 ? 2281 HOH   A O     1 
HETATM 19410 O  O     . HOH   CA 11 .    ? -46.222 29.617  66.150  1.00 43.42 ? 2282 HOH   A O     1 
HETATM 19411 O  O     . HOH   CA 11 .    ? -21.414 52.985  88.491  1.00 36.15 ? 2283 HOH   A O     1 
HETATM 19412 O  O     . HOH   CA 11 .    ? -3.847  79.018  93.485  1.00 34.98 ? 2284 HOH   A O     1 
HETATM 19413 O  O     . HOH   CA 11 .    ? -30.115 62.898  91.677  1.00 33.34 ? 2285 HOH   A O     1 
HETATM 19414 O  O     . HOH   CA 11 .    ? -20.539 54.694  98.815  1.00 28.51 ? 2286 HOH   A O     1 
HETATM 19415 O  O     . HOH   CA 11 .    ? -2.124  80.063  97.184  1.00 26.34 ? 2287 HOH   A O     1 
HETATM 19416 O  O     . HOH   CA 11 .    ? -58.554 45.686  91.871  1.00 40.20 ? 2288 HOH   A O     1 
HETATM 19417 O  O     . HOH   CA 11 .    ? -28.865 83.993  72.991  1.00 42.58 ? 2289 HOH   A O     1 
HETATM 19418 O  O     . HOH   CA 11 .    ? -0.878  74.743  116.558 1.00 32.33 ? 2290 HOH   A O     1 
HETATM 19419 O  O     . HOH   CA 11 .    ? -18.404 92.348  107.605 1.00 33.60 ? 2291 HOH   A O     1 
HETATM 19420 O  O     . HOH   CA 11 .    ? -29.647 58.604  79.024  1.00 32.08 ? 2292 HOH   A O     1 
HETATM 19421 O  O     . HOH   CA 11 .    ? -62.073 59.960  95.695  1.00 25.07 ? 2293 HOH   A O     1 
HETATM 19422 O  O     . HOH   CA 11 .    ? -53.785 44.927  59.911  1.00 41.71 ? 2294 HOH   A O     1 
HETATM 19423 O  O     . HOH   CA 11 .    ? -14.219 58.139  109.772 1.00 35.25 ? 2295 HOH   A O     1 
HETATM 19424 O  O     . HOH   CA 11 .    ? 14.785  82.449  119.178 1.00 28.49 ? 2296 HOH   A O     1 
HETATM 19425 O  O     . HOH   CA 11 .    ? 2.609   66.632  120.342 1.00 38.55 ? 2297 HOH   A O     1 
HETATM 19426 O  O     . HOH   CA 11 .    ? 21.031  71.218  94.778  1.00 36.49 ? 2298 HOH   A O     1 
HETATM 19427 O  O     . HOH   CA 11 .    ? -44.228 76.390  74.476  1.00 30.81 ? 2299 HOH   A O     1 
HETATM 19428 O  O     . HOH   CA 11 .    ? -51.252 79.554  78.542  1.00 35.89 ? 2300 HOH   A O     1 
HETATM 19429 O  O     . HOH   CA 11 .    ? -40.777 46.930  59.552  1.00 36.89 ? 2301 HOH   A O     1 
HETATM 19430 O  O     . HOH   CA 11 .    ? -22.907 67.594  129.618 1.00 35.97 ? 2302 HOH   A O     1 
HETATM 19431 O  O     . HOH   CA 11 .    ? -0.441  79.558  94.804  1.00 46.69 ? 2303 HOH   A O     1 
HETATM 19432 O  O     . HOH   CA 11 .    ? -44.685 92.765  88.791  1.00 37.73 ? 2304 HOH   A O     1 
HETATM 19433 O  O     . HOH   CA 11 .    ? 12.792  88.851  116.049 1.00 33.34 ? 2305 HOH   A O     1 
HETATM 19434 O  O     . HOH   CA 11 .    ? -66.062 64.359  87.895  1.00 30.46 ? 2306 HOH   A O     1 
HETATM 19435 O  O     . HOH   CA 11 .    ? -41.659 24.446  81.352  1.00 46.37 ? 2307 HOH   A O     1 
HETATM 19436 O  O     . HOH   CA 11 .    ? 20.347  75.433  99.715  1.00 41.38 ? 2308 HOH   A O     1 
HETATM 19437 O  O     . HOH   CA 11 .    ? 13.675  78.596  123.053 1.00 38.22 ? 2309 HOH   A O     1 
HETATM 19438 O  O     . HOH   CA 11 .    ? -14.964 48.391  51.446  1.00 39.75 ? 2310 HOH   A O     1 
HETATM 19439 O  O     . HOH   CA 11 .    ? -21.200 50.225  108.426 1.00 38.51 ? 2311 HOH   A O     1 
HETATM 19440 O  O     . HOH   CA 11 .    ? -45.346 92.476  98.590  1.00 38.90 ? 2312 HOH   A O     1 
HETATM 19441 O  O     . HOH   CA 11 .    ? -44.417 91.230  111.114 1.00 33.61 ? 2313 HOH   A O     1 
HETATM 19442 O  O     . HOH   CA 11 .    ? -46.745 78.436  117.108 1.00 36.06 ? 2314 HOH   A O     1 
HETATM 19443 O  O     . HOH   CA 11 .    ? -67.950 51.018  77.430  1.00 43.91 ? 2315 HOH   A O     1 
HETATM 19444 O  O     . HOH   CA 11 .    ? 7.754   79.470  125.425 1.00 42.59 ? 2316 HOH   A O     1 
HETATM 19445 O  O     . HOH   CA 11 .    ? -50.510 54.697  104.636 1.00 39.93 ? 2317 HOH   A O     1 
HETATM 19446 O  O     . HOH   CA 11 .    ? -39.610 47.079  103.742 1.00 31.53 ? 2318 HOH   A O     1 
HETATM 19447 O  O     . HOH   CA 11 .    ? -57.885 72.402  88.082  1.00 37.36 ? 2319 HOH   A O     1 
HETATM 19448 O  O     . HOH   CA 11 .    ? -32.663 44.741  103.127 1.00 38.51 ? 2320 HOH   A O     1 
HETATM 19449 O  O     . HOH   CA 11 .    ? -65.134 36.328  72.541  1.00 42.81 ? 2321 HOH   A O     1 
HETATM 19450 O  O     . HOH   CA 11 .    ? -0.677  52.648  58.910  1.00 34.01 ? 2322 HOH   A O     1 
HETATM 19451 O  O     . HOH   CA 11 .    ? -6.490  62.324  69.070  1.00 44.53 ? 2323 HOH   A O     1 
HETATM 19452 O  O     . HOH   CA 11 .    ? -37.454 75.439  97.398  1.00 27.62 ? 2324 HOH   A O     1 
HETATM 19453 O  O     . HOH   CA 11 .    ? -23.506 75.939  133.247 1.00 31.74 ? 2325 HOH   A O     1 
HETATM 19454 O  O     . HOH   CA 11 .    ? -33.284 60.304  82.677  1.00 41.86 ? 2326 HOH   A O     1 
HETATM 19455 O  O     . HOH   CA 11 .    ? -3.302  85.596  124.587 1.00 35.61 ? 2327 HOH   A O     1 
HETATM 19456 O  O     . HOH   CA 11 .    ? -34.863 75.651  125.912 1.00 31.96 ? 2328 HOH   A O     1 
HETATM 19457 O  O     . HOH   CA 11 .    ? 18.969  71.180  91.816  1.00 43.30 ? 2329 HOH   A O     1 
HETATM 19458 O  O     . HOH   CA 11 .    ? -23.217 100.036 120.349 1.00 43.62 ? 2330 HOH   A O     1 
HETATM 19459 O  O     . HOH   CA 11 .    ? 11.319  74.675  128.682 1.00 35.93 ? 2331 HOH   A O     1 
HETATM 19460 O  O     . HOH   CA 11 .    ? 12.485  63.498  120.643 1.00 36.62 ? 2332 HOH   A O     1 
HETATM 19461 O  O     . HOH   CA 11 .    ? -62.215 67.251  60.520  1.00 35.01 ? 2333 HOH   A O     1 
HETATM 19462 O  O     . HOH   CA 11 .    ? -5.882  74.987  102.947 1.00 27.98 ? 2334 HOH   A O     1 
HETATM 19463 O  O     . HOH   CA 11 .    ? -64.879 59.693  98.812  1.00 43.55 ? 2335 HOH   A O     1 
HETATM 19464 O  O     . HOH   CA 11 .    ? -68.909 52.986  85.034  1.00 39.59 ? 2336 HOH   A O     1 
HETATM 19465 O  O     . HOH   CA 11 .    ? -47.480 33.150  85.143  1.00 35.16 ? 2337 HOH   A O     1 
HETATM 19466 O  O     . HOH   CA 11 .    ? -42.466 85.294  105.131 1.00 32.39 ? 2338 HOH   A O     1 
HETATM 19467 O  O     . HOH   CA 11 .    ? 19.340  64.440  93.024  1.00 31.70 ? 2339 HOH   A O     1 
HETATM 19468 O  O     . HOH   CA 11 .    ? -45.960 78.345  89.851  1.00 23.43 ? 2340 HOH   A O     1 
HETATM 19469 O  O     . HOH   CA 11 .    ? 8.033   69.728  125.041 1.00 42.07 ? 2341 HOH   A O     1 
HETATM 19470 O  O     . HOH   CA 11 .    ? -35.228 70.644  82.498  1.00 38.43 ? 2342 HOH   A O     1 
HETATM 19471 O  O     . HOH   CA 11 .    ? -40.824 48.910  56.203  1.00 44.70 ? 2343 HOH   A O     1 
HETATM 19472 O  O     . HOH   CA 11 .    ? -33.664 46.118  65.805  1.00 41.10 ? 2344 HOH   A O     1 
HETATM 19473 O  O     . HOH   CA 11 .    ? -27.023 60.625  122.519 1.00 31.11 ? 2345 HOH   A O     1 
HETATM 19474 O  O     . HOH   CA 11 .    ? -10.127 66.774  74.340  1.00 31.87 ? 2346 HOH   A O     1 
HETATM 19475 O  O     . HOH   CA 11 .    ? -35.574 60.010  88.477  1.00 30.04 ? 2347 HOH   A O     1 
HETATM 19476 O  O     . HOH   CA 11 .    ? -31.326 78.205  90.848  1.00 31.02 ? 2348 HOH   A O     1 
HETATM 19477 O  O     . HOH   CA 11 .    ? 16.711  87.029  111.582 1.00 39.74 ? 2349 HOH   A O     1 
HETATM 19478 O  O     . HOH   CA 11 .    ? 5.446   71.011  95.951  1.00 34.96 ? 2350 HOH   A O     1 
HETATM 19479 O  O     . HOH   CA 11 .    ? -40.011 47.476  106.434 1.00 37.73 ? 2351 HOH   A O     1 
HETATM 19480 O  O     . HOH   CA 11 .    ? -31.880 67.779  101.160 1.00 32.79 ? 2352 HOH   A O     1 
HETATM 19481 O  O     . HOH   CA 11 .    ? -39.037 78.441  69.754  1.00 33.04 ? 2353 HOH   A O     1 
HETATM 19482 O  O     . HOH   CA 11 .    ? -52.568 41.692  101.374 1.00 37.92 ? 2354 HOH   A O     1 
HETATM 19483 O  O     . HOH   CA 11 .    ? 25.976  74.279  97.850  1.00 42.28 ? 2355 HOH   A O     1 
HETATM 19484 O  O     . HOH   CA 11 .    ? -28.930 32.750  74.661  1.00 43.15 ? 2356 HOH   A O     1 
HETATM 19485 O  O     . HOH   CA 11 .    ? -34.217 59.119  106.078 1.00 27.66 ? 2357 HOH   A O     1 
HETATM 19486 O  O     . HOH   CA 11 .    ? -37.105 74.950  64.220  1.00 37.86 ? 2358 HOH   A O     1 
HETATM 19487 O  O     . HOH   CA 11 .    ? -26.194 74.478  132.508 1.00 33.38 ? 2359 HOH   A O     1 
HETATM 19488 O  O     . HOH   CA 11 .    ? -3.909  59.998  68.375  1.00 42.80 ? 2360 HOH   A O     1 
HETATM 19489 O  O     . HOH   CA 11 .    ? -31.588 38.612  99.445  1.00 45.28 ? 2361 HOH   A O     1 
HETATM 19490 O  O     . HOH   CA 11 .    ? -24.021 100.466 100.731 1.00 39.85 ? 2362 HOH   A O     1 
HETATM 19491 O  O     . HOH   CA 11 .    ? -60.654 59.626  62.019  1.00 32.25 ? 2363 HOH   A O     1 
HETATM 19492 O  O     . HOH   CA 11 .    ? -9.083  41.242  69.353  1.00 35.08 ? 2364 HOH   A O     1 
HETATM 19493 O  O     . HOH   CA 11 .    ? -19.093 54.691  118.276 1.00 36.87 ? 2365 HOH   A O     1 
HETATM 19494 O  O     . HOH   CA 11 .    ? -9.294  73.125  131.563 1.00 37.83 ? 2366 HOH   A O     1 
HETATM 19495 O  O     . HOH   CA 11 .    ? -11.607 59.796  106.415 1.00 31.41 ? 2367 HOH   A O     1 
HETATM 19496 O  O     . HOH   CA 11 .    ? 0.847   69.598  87.466  1.00 31.65 ? 2368 HOH   A O     1 
HETATM 19497 O  O     . HOH   CA 11 .    ? -46.237 63.248  53.752  1.00 37.16 ? 2369 HOH   A O     1 
HETATM 19498 O  O     . HOH   CA 11 .    ? -50.504 24.130  80.749  1.00 41.34 ? 2370 HOH   A O     1 
HETATM 19499 O  O     . HOH   CA 11 .    ? -10.073 94.869  117.203 1.00 43.53 ? 2371 HOH   A O     1 
HETATM 19500 O  O     . HOH   CA 11 .    ? -52.738 57.050  73.636  1.00 27.51 ? 2372 HOH   A O     1 
HETATM 19501 O  O     . HOH   CA 11 .    ? -67.353 65.996  69.800  1.00 43.65 ? 2373 HOH   A O     1 
HETATM 19502 O  O     . HOH   CA 11 .    ? -48.543 27.181  74.763  1.00 41.44 ? 2374 HOH   A O     1 
HETATM 19503 O  O     . HOH   CA 11 .    ? -40.178 67.701  89.054  1.00 29.25 ? 2375 HOH   A O     1 
HETATM 19504 O  O     . HOH   CA 11 .    ? -3.845  57.834  63.177  1.00 42.09 ? 2376 HOH   A O     1 
HETATM 19505 O  O     . HOH   CA 11 .    ? -30.598 49.294  86.310  1.00 37.31 ? 2377 HOH   A O     1 
HETATM 19506 O  O     . HOH   CA 11 .    ? -31.103 59.395  60.187  1.00 43.94 ? 2378 HOH   A O     1 
HETATM 19507 O  O     . HOH   CA 11 .    ? -19.517 70.715  132.554 1.00 36.45 ? 2379 HOH   A O     1 
HETATM 19508 O  O     . HOH   CA 11 .    ? -1.683  92.056  108.933 1.00 32.12 ? 2380 HOH   A O     1 
HETATM 19509 O  O     . HOH   CA 11 .    ? -53.199 40.544  62.986  1.00 39.92 ? 2381 HOH   A O     1 
HETATM 19510 O  O     . HOH   CA 11 .    ? -11.188 40.971  57.630  1.00 42.69 ? 2382 HOH   A O     1 
HETATM 19511 O  O     . HOH   CA 11 .    ? -61.056 68.976  91.894  1.00 38.75 ? 2383 HOH   A O     1 
HETATM 19512 O  O     . HOH   CA 11 .    ? -28.766 57.483  88.434  1.00 30.57 ? 2384 HOH   A O     1 
HETATM 19513 O  O     . HOH   CA 11 .    ? -64.131 51.130  73.153  1.00 33.84 ? 2385 HOH   A O     1 
HETATM 19514 O  O     . HOH   CA 11 .    ? -22.753 74.122  69.697  1.00 32.37 ? 2386 HOH   A O     1 
HETATM 19515 O  O     . HOH   CA 11 .    ? -7.696  72.944  103.349 1.00 29.92 ? 2387 HOH   A O     1 
HETATM 19516 O  O     . HOH   CA 11 .    ? -47.673 63.969  55.998  1.00 29.40 ? 2388 HOH   A O     1 
HETATM 19517 O  O     . HOH   CA 11 .    ? -51.874 55.251  70.345  1.00 24.24 ? 2389 HOH   A O     1 
HETATM 19518 O  O     . HOH   CA 11 .    ? -18.868 59.593  110.902 1.00 26.90 ? 2390 HOH   A O     1 
HETATM 19519 O  O     . HOH   CA 11 .    ? -27.198 91.994  76.725  1.00 36.51 ? 2391 HOH   A O     1 
HETATM 19520 O  O     . HOH   CA 11 .    ? -22.093 73.916  134.184 1.00 42.10 ? 2392 HOH   A O     1 
HETATM 19521 O  O     . HOH   CA 11 .    ? -44.637 61.575  104.206 1.00 45.61 ? 2393 HOH   A O     1 
HETATM 19522 O  O     . HOH   CA 11 .    ? -26.066 67.578  93.914  1.00 34.29 ? 2394 HOH   A O     1 
HETATM 19523 O  O     . HOH   CA 11 .    ? -41.963 89.443  115.618 1.00 44.91 ? 2395 HOH   A O     1 
HETATM 19524 O  O     . HOH   CA 11 .    ? -44.631 69.525  111.147 1.00 38.71 ? 2396 HOH   A O     1 
HETATM 19525 O  O     . HOH   CA 11 .    ? -46.386 80.364  74.739  1.00 43.99 ? 2397 HOH   A O     1 
HETATM 19526 O  O     . HOH   CA 11 .    ? -15.479 57.740  105.995 1.00 30.82 ? 2398 HOH   A O     1 
HETATM 19527 O  O     . HOH   CA 11 .    ? -41.160 66.756  70.682  1.00 30.55 ? 2399 HOH   A O     1 
HETATM 19528 O  O     . HOH   CA 11 .    ? -26.988 65.369  102.621 1.00 26.73 ? 2400 HOH   A O     1 
HETATM 19529 O  O     . HOH   CA 11 .    ? -28.600 67.227  93.105  1.00 41.42 ? 2401 HOH   A O     1 
HETATM 19530 O  O     . HOH   CA 11 .    ? 7.131   91.544  118.266 1.00 38.66 ? 2402 HOH   A O     1 
HETATM 19531 O  O     . HOH   CA 11 .    ? -55.226 57.604  102.129 1.00 28.96 ? 2403 HOH   A O     1 
HETATM 19532 O  O     . HOH   CA 11 .    ? -64.456 63.360  68.431  1.00 33.67 ? 2404 HOH   A O     1 
HETATM 19533 O  O     . HOH   CA 11 .    ? -51.182 68.334  107.761 1.00 39.23 ? 2405 HOH   A O     1 
HETATM 19534 O  O     . HOH   CA 11 .    ? -7.283  65.925  92.443  1.00 35.77 ? 2406 HOH   A O     1 
HETATM 19535 O  O     . HOH   CA 11 .    ? -37.880 70.902  86.365  1.00 34.93 ? 2407 HOH   A O     1 
HETATM 19536 O  O     . HOH   CA 11 .    ? -27.533 51.280  109.449 1.00 36.45 ? 2408 HOH   A O     1 
HETATM 19537 O  O     . HOH   CA 11 .    ? 7.423   62.511  112.285 1.00 33.00 ? 2409 HOH   A O     1 
HETATM 19538 O  O     . HOH   CA 11 .    ? 12.406  88.407  118.692 1.00 37.80 ? 2410 HOH   A O     1 
HETATM 19539 O  O     . HOH   CA 11 .    ? -55.302 27.767  81.669  1.00 38.28 ? 2411 HOH   A O     1 
HETATM 19540 O  O     . HOH   CA 11 .    ? -10.273 93.682  113.867 1.00 35.27 ? 2412 HOH   A O     1 
HETATM 19541 O  O     . HOH   CA 11 .    ? -46.783 31.001  72.744  1.00 37.23 ? 2413 HOH   A O     1 
HETATM 19542 O  O     . HOH   CA 11 .    ? -26.535 48.283  101.721 1.00 42.40 ? 2414 HOH   A O     1 
HETATM 19543 O  O     . HOH   CA 11 .    ? -61.314 72.656  81.780  1.00 37.84 ? 2415 HOH   A O     1 
HETATM 19544 O  O     . HOH   CA 11 .    ? -11.481 64.061  51.072  1.00 41.37 ? 2416 HOH   A O     1 
HETATM 19545 O  O     . HOH   CA 11 .    ? -58.206 46.796  63.858  1.00 44.54 ? 2417 HOH   A O     1 
HETATM 19546 O  O     . HOH   CA 11 .    ? -38.266 68.567  88.049  1.00 38.45 ? 2418 HOH   A O     1 
HETATM 19547 O  O     . HOH   CA 11 .    ? -33.141 84.214  76.831  1.00 29.11 ? 2419 HOH   A O     1 
HETATM 19548 O  O     . HOH   CA 11 .    ? -9.287  67.185  129.351 1.00 35.38 ? 2420 HOH   A O     1 
HETATM 19549 O  O     . HOH   CA 11 .    ? -10.141 90.394  127.627 1.00 40.13 ? 2421 HOH   A O     1 
HETATM 19550 O  O     . HOH   CA 11 .    ? 7.758   66.435  111.732 1.00 40.89 ? 2422 HOH   A O     1 
HETATM 19551 O  O     . HOH   CA 11 .    ? -34.825 39.139  94.614  1.00 34.00 ? 2423 HOH   A O     1 
HETATM 19552 O  O     . HOH   CA 11 .    ? -31.527 76.336  74.254  1.00 31.66 ? 2424 HOH   A O     1 
HETATM 19553 O  O     . HOH   CA 11 .    ? -59.872 64.200  92.135  1.00 29.06 ? 2425 HOH   A O     1 
HETATM 19554 O  O     . HOH   CA 11 .    ? -39.278 35.761  88.623  1.00 30.39 ? 2426 HOH   A O     1 
HETATM 19555 O  O     . HOH   CA 11 .    ? -34.079 61.260  86.411  1.00 37.41 ? 2427 HOH   A O     1 
HETATM 19556 O  O     . HOH   CA 11 .    ? -47.814 85.516  112.053 1.00 41.26 ? 2428 HOH   A O     1 
HETATM 19557 O  O     . HOH   CA 11 .    ? -63.056 61.114  93.301  1.00 32.58 ? 2429 HOH   A O     1 
HETATM 19558 O  O     . HOH   CA 11 .    ? -58.773 30.765  86.430  1.00 30.93 ? 2430 HOH   A O     1 
HETATM 19559 O  O     . HOH   CA 11 .    ? -44.088 88.142  92.990  1.00 41.50 ? 2431 HOH   A O     1 
HETATM 19560 O  O     . HOH   CA 11 .    ? -48.440 30.783  68.870  1.00 40.57 ? 2432 HOH   A O     1 
HETATM 19561 O  O     . HOH   CA 11 .    ? -23.304 55.223  52.054  1.00 40.98 ? 2433 HOH   A O     1 
HETATM 19562 O  O     . HOH   CA 11 .    ? -46.213 56.924  54.392  1.00 38.56 ? 2434 HOH   A O     1 
HETATM 19563 O  O     . HOH   CA 11 .    ? -44.991 88.188  99.340  1.00 37.62 ? 2435 HOH   A O     1 
HETATM 19564 O  O     . HOH   CA 11 .    ? -1.830  89.125  97.163  1.00 39.78 ? 2436 HOH   A O     1 
HETATM 19565 O  O     . HOH   CA 11 .    ? -27.814 63.875  90.530  1.00 33.75 ? 2437 HOH   A O     1 
HETATM 19566 O  O     . HOH   CA 11 .    ? 4.806   60.584  98.166  1.00 24.24 ? 2438 HOH   A O     1 
HETATM 19567 O  O     . HOH   CA 11 .    ? -31.902 74.234  83.600  1.00 30.95 ? 2439 HOH   A O     1 
HETATM 19568 O  O     . HOH   CA 11 .    ? -67.473 62.364  68.541  1.00 42.27 ? 2440 HOH   A O     1 
HETATM 19569 O  O     . HOH   CA 11 .    ? -21.464 99.354  98.017  1.00 40.63 ? 2441 HOH   A O     1 
HETATM 19570 O  O     . HOH   CA 11 .    ? -29.240 60.871  120.799 1.00 36.42 ? 2442 HOH   A O     1 
HETATM 19571 O  O     . HOH   CA 11 .    ? -24.486 47.225  57.982  1.00 41.39 ? 2443 HOH   A O     1 
HETATM 19572 O  O     . HOH   CA 11 .    ? -21.227 92.964  107.019 1.00 31.61 ? 2444 HOH   A O     1 
HETATM 19573 O  O     . HOH   CA 11 .    ? 15.872  83.364  116.179 1.00 36.45 ? 2445 HOH   A O     1 
HETATM 19574 O  O     . HOH   CA 11 .    ? 12.393  64.102  116.455 1.00 36.56 ? 2446 HOH   A O     1 
HETATM 19575 O  O     . HOH   CA 11 .    ? 22.503  78.931  100.087 1.00 40.96 ? 2447 HOH   A O     1 
HETATM 19576 O  O     . HOH   CA 11 .    ? -20.161 52.826  105.557 1.00 38.10 ? 2448 HOH   A O     1 
HETATM 19577 O  O     . HOH   CA 11 .    ? -24.803 65.634  96.734  1.00 32.59 ? 2449 HOH   A O     1 
HETATM 19578 O  O     . HOH   CA 11 .    ? -45.246 85.022  90.069  1.00 45.04 ? 2450 HOH   A O     1 
HETATM 19579 O  O     . HOH   CA 11 .    ? -45.408 28.847  86.838  1.00 33.40 ? 2451 HOH   A O     1 
HETATM 19580 O  O     . HOH   CA 11 .    ? -52.608 48.449  57.756  1.00 39.49 ? 2452 HOH   A O     1 
HETATM 19581 O  O     . HOH   CA 11 .    ? -10.050 66.905  132.155 1.00 36.48 ? 2453 HOH   A O     1 
HETATM 19582 O  O     . HOH   CA 11 .    ? -39.295 70.358  118.466 1.00 41.67 ? 2454 HOH   A O     1 
HETATM 19583 O  O     . HOH   CA 11 .    ? -34.710 76.239  87.167  1.00 28.16 ? 2455 HOH   A O     1 
HETATM 19584 O  O     . HOH   CA 11 .    ? -6.931  55.142  82.592  1.00 28.31 ? 2456 HOH   A O     1 
HETATM 19585 O  O     . HOH   CA 11 .    ? -43.756 87.672  115.376 1.00 48.02 ? 2457 HOH   A O     1 
HETATM 19586 O  O     . HOH   CA 11 .    ? -67.069 54.693  82.023  1.00 32.93 ? 2458 HOH   A O     1 
HETATM 19587 O  O     . HOH   CA 11 .    ? -41.847 80.150  72.930  1.00 39.45 ? 2459 HOH   A O     1 
HETATM 19588 O  O     . HOH   CA 11 .    ? -35.068 54.985  107.231 1.00 32.46 ? 2460 HOH   A O     1 
HETATM 19589 O  O     . HOH   CA 11 .    ? 18.567  77.941  96.420  1.00 39.72 ? 2461 HOH   A O     1 
HETATM 19590 O  O     . HOH   CA 11 .    ? -35.385 73.581  86.487  1.00 31.99 ? 2462 HOH   A O     1 
HETATM 19591 O  O     . HOH   CA 11 .    ? -10.714 78.627  92.260  1.00 19.03 ? 2463 HOH   A O     1 
HETATM 19592 O  O     . HOH   CA 11 .    ? -23.049 71.209  73.881  1.00 34.70 ? 2464 HOH   A O     1 
HETATM 19593 O  O     . HOH   CA 11 .    ? 3.668   76.407  95.214  1.00 40.40 ? 2465 HOH   A O     1 
HETATM 19594 O  O     . HOH   CA 11 .    ? 22.911  62.380  99.389  1.00 37.13 ? 2466 HOH   A O     1 
HETATM 19595 O  O     . HOH   CA 11 .    ? -3.630  68.379  92.825  1.00 38.58 ? 2467 HOH   A O     1 
HETATM 19596 O  O     . HOH   CA 11 .    ? -52.307 74.121  61.831  1.00 20.66 ? 2468 HOH   A O     1 
HETATM 19597 O  O     . HOH   CA 11 .    ? -24.280 77.538  68.321  1.00 39.17 ? 2469 HOH   A O     1 
HETATM 19598 O  O     . HOH   CA 11 .    ? -58.634 74.679  94.626  1.00 38.53 ? 2470 HOH   A O     1 
HETATM 19599 O  O     . HOH   CA 11 .    ? -56.227 31.966  92.225  1.00 38.37 ? 2471 HOH   A O     1 
HETATM 19600 O  O     . HOH   CA 11 .    ? -60.110 52.596  95.869  1.00 39.67 ? 2472 HOH   A O     1 
HETATM 19601 O  O     . HOH   CA 11 .    ? -54.077 42.719  60.718  1.00 46.15 ? 2473 HOH   A O     1 
HETATM 19602 O  O     . HOH   CA 11 .    ? -66.595 72.712  77.775  1.00 40.48 ? 2474 HOH   A O     1 
HETATM 19603 O  O     . HOH   CA 11 .    ? -2.716  56.889  70.606  1.00 32.13 ? 2475 HOH   A O     1 
HETATM 19604 O  O     . HOH   CA 11 .    ? 16.955  83.830  112.802 1.00 34.15 ? 2476 HOH   A O     1 
HETATM 19605 O  O     . HOH   CA 11 .    ? -28.735 80.446  131.592 1.00 39.61 ? 2477 HOH   A O     1 
HETATM 19606 O  O     . HOH   CA 11 .    ? 6.563   66.991  93.647  1.00 33.39 ? 2478 HOH   A O     1 
HETATM 19607 O  O     . HOH   CA 11 .    ? 2.115   83.825  129.208 1.00 43.85 ? 2479 HOH   A O     1 
HETATM 19608 O  O     . HOH   CA 11 .    ? -42.041 64.010  106.049 1.00 37.24 ? 2480 HOH   A O     1 
HETATM 19609 O  O     . HOH   CA 11 .    ? -3.638  69.572  94.773  1.00 44.60 ? 2481 HOH   A O     1 
HETATM 19610 O  O     . HOH   CA 11 .    ? -52.949 66.306  101.798 1.00 34.55 ? 2482 HOH   A O     1 
HETATM 19611 O  O     . HOH   CA 11 .    ? -63.523 49.005  71.903  1.00 37.86 ? 2483 HOH   A O     1 
HETATM 19612 O  O     . HOH   CA 11 .    ? -35.723 39.926  71.086  1.00 40.12 ? 2484 HOH   A O     1 
HETATM 19613 O  O     . HOH   CA 11 .    ? -41.882 48.790  107.981 1.00 44.60 ? 2485 HOH   A O     1 
HETATM 19614 O  O     . HOH   CA 11 .    ? -31.857 42.686  72.047  1.00 43.49 ? 2486 HOH   A O     1 
HETATM 19615 O  O     . HOH   CA 11 .    ? -16.946 57.435  109.997 1.00 38.42 ? 2487 HOH   A O     1 
HETATM 19616 O  O     . HOH   CA 11 .    ? -66.999 66.058  83.141  1.00 24.22 ? 2488 HOH   A O     1 
HETATM 19617 O  O     . HOH   CA 11 .    ? 8.403   73.351  128.361 1.00 43.95 ? 2489 HOH   A O     1 
HETATM 19618 O  O     . HOH   CA 11 .    ? -54.482 78.192  85.719  1.00 38.64 ? 2490 HOH   A O     1 
HETATM 19619 O  O     . HOH   CA 11 .    ? -14.789 52.010  112.321 1.00 39.65 ? 2491 HOH   A O     1 
HETATM 19620 O  O     . HOH   CA 11 .    ? -36.227 63.222  90.244  1.00 36.45 ? 2492 HOH   A O     1 
HETATM 19621 O  O     . HOH   CA 11 .    ? -8.523  61.463  86.694  1.00 36.13 ? 2493 HOH   A O     1 
HETATM 19622 O  O     . HOH   CA 11 .    ? -53.206 45.608  94.446  1.00 32.64 ? 2494 HOH   A O     1 
HETATM 19623 O  O     . HOH   CA 11 .    ? -28.026 49.212  104.191 1.00 38.78 ? 2495 HOH   A O     1 
HETATM 19624 O  O     . HOH   CA 11 .    ? -50.781 81.113  83.826  1.00 40.47 ? 2496 HOH   A O     1 
HETATM 19625 O  O     . HOH   CA 11 .    ? 16.089  66.390  90.044  1.00 37.72 ? 2497 HOH   A O     1 
HETATM 19626 O  O     . HOH   CA 11 .    ? -17.268 96.996  91.942  1.00 36.74 ? 2498 HOH   A O     1 
HETATM 19627 O  O     . HOH   CA 11 .    ? -22.957 91.282  103.678 1.00 37.61 ? 2499 HOH   A O     1 
HETATM 19628 O  O     . HOH   CA 11 .    ? -27.226 59.398  116.144 1.00 34.74 ? 2500 HOH   A O     1 
HETATM 19629 O  O     . HOH   CA 11 .    ? -63.989 65.200  66.393  1.00 32.58 ? 2501 HOH   A O     1 
HETATM 19630 O  O     . HOH   CA 11 .    ? -56.714 44.287  92.333  1.00 34.60 ? 2502 HOH   A O     1 
HETATM 19631 O  O     . HOH   CA 11 .    ? -38.367 91.124  122.596 1.00 45.93 ? 2503 HOH   A O     1 
HETATM 19632 O  O     . HOH   CA 11 .    ? -6.847  86.796  88.442  1.00 43.32 ? 2504 HOH   A O     1 
HETATM 19633 O  O     . HOH   CA 11 .    ? -58.026 32.453  90.105  1.00 27.50 ? 2505 HOH   A O     1 
HETATM 19634 O  O     . HOH   CA 11 .    ? -5.999  62.649  93.367  1.00 45.07 ? 2506 HOH   A O     1 
HETATM 19635 O  O     . HOH   CA 11 .    ? -35.362 39.177  89.684  1.00 36.33 ? 2507 HOH   A O     1 
HETATM 19636 O  O     . HOH   CA 11 .    ? 2.081   74.959  119.286 1.00 40.18 ? 2508 HOH   A O     1 
HETATM 19637 O  O     . HOH   CA 11 .    ? -44.504 83.483  85.903  1.00 39.34 ? 2509 HOH   A O     1 
HETATM 19638 O  O     . HOH   CA 11 .    ? 20.186  61.684  96.208  1.00 30.56 ? 2510 HOH   A O     1 
HETATM 19639 O  O     . HOH   CA 11 .    ? -56.506 74.642  79.218  1.00 31.49 ? 2511 HOH   A O     1 
HETATM 19640 O  O     . HOH   CA 11 .    ? 18.624  89.234  111.270 1.00 41.84 ? 2512 HOH   A O     1 
HETATM 19641 O  O     . HOH   CA 11 .    ? -37.415 63.074  114.025 1.00 33.72 ? 2513 HOH   A O     1 
HETATM 19642 O  O     . HOH   CA 11 .    ? -27.111 93.277  110.034 1.00 39.32 ? 2514 HOH   A O     1 
HETATM 19643 O  O     . HOH   CA 11 .    ? -14.754 57.864  123.945 1.00 40.75 ? 2515 HOH   A O     1 
HETATM 19644 O  O     . HOH   CA 11 .    ? -25.727 65.020  91.599  1.00 33.83 ? 2516 HOH   A O     1 
HETATM 19645 O  O     . HOH   CA 11 .    ? -57.462 41.653  91.238  1.00 40.40 ? 2517 HOH   A O     1 
HETATM 19646 O  O     . HOH   CA 11 .    ? -30.467 79.505  125.394 1.00 38.52 ? 2518 HOH   A O     1 
HETATM 19647 O  O     . HOH   CA 11 .    ? 10.964  90.787  119.510 1.00 41.28 ? 2519 HOH   A O     1 
HETATM 19648 O  O     . HOH   CA 11 .    ? -52.533 64.075  100.651 1.00 29.38 ? 2520 HOH   A O     1 
HETATM 19649 O  O     . HOH   CA 11 .    ? -33.695 81.036  122.471 1.00 29.35 ? 2521 HOH   A O     1 
HETATM 19650 O  O     . HOH   CA 11 .    ? -42.922 80.122  74.902  1.00 40.36 ? 2522 HOH   A O     1 
HETATM 19651 O  O     . HOH   CA 11 .    ? -25.152 97.335  125.856 1.00 40.73 ? 2523 HOH   A O     1 
HETATM 19652 O  O     . HOH   CA 11 .    ? 6.357   81.496  127.094 1.00 34.15 ? 2524 HOH   A O     1 
HETATM 19653 O  O     . HOH   CA 11 .    ? -38.077 74.324  93.184  1.00 35.37 ? 2525 HOH   A O     1 
HETATM 19654 O  O     . HOH   CA 11 .    ? -33.782 80.669  74.358  1.00 27.71 ? 2526 HOH   A O     1 
HETATM 19655 O  O     . HOH   CA 11 .    ? 3.153   74.284  87.443  1.00 44.74 ? 2527 HOH   A O     1 
HETATM 19656 O  O     . HOH   CA 11 .    ? -49.589 59.677  55.006  1.00 36.76 ? 2528 HOH   A O     1 
HETATM 19657 O  O     . HOH   CA 11 .    ? 15.791  80.537  123.438 1.00 40.59 ? 2529 HOH   A O     1 
HETATM 19658 O  O     . HOH   CA 11 .    ? -48.768 81.282  87.467  1.00 40.72 ? 2530 HOH   A O     1 
HETATM 19659 O  O     . HOH   CA 11 .    ? -36.148 90.336  123.557 1.00 39.10 ? 2531 HOH   A O     1 
HETATM 19660 O  O     . HOH   CA 11 .    ? -24.490 97.106  121.017 1.00 41.97 ? 2532 HOH   A O     1 
HETATM 19661 O  O     . HOH   CA 11 .    ? 3.667   64.848  96.151  1.00 25.63 ? 2533 HOH   A O     1 
HETATM 19662 O  O     . HOH   CA 11 .    ? -14.707 96.084  114.312 1.00 44.13 ? 2534 HOH   A O     1 
HETATM 19663 O  O     . HOH   CA 11 .    ? -54.885 25.026  80.805  1.00 46.46 ? 2535 HOH   A O     1 
HETATM 19664 O  O     . HOH   CA 11 .    ? -28.519 75.794  129.749 1.00 41.44 ? 2536 HOH   A O     1 
HETATM 19665 O  O     . HOH   CA 11 .    ? -13.166 52.294  99.407  1.00 41.71 ? 2537 HOH   A O     1 
HETATM 19666 O  O     . HOH   CA 11 .    ? -25.890 83.092  69.538  1.00 41.58 ? 2538 HOH   A O     1 
HETATM 19667 O  O     . HOH   CA 11 .    ? -48.311 56.700  55.915  1.00 31.92 ? 2539 HOH   A O     1 
HETATM 19668 O  O     . HOH   CA 11 .    ? -46.861 76.210  117.400 1.00 37.11 ? 2540 HOH   A O     1 
HETATM 19669 O  O     . HOH   CA 11 .    ? -18.635 74.490  109.128 1.00 21.75 ? 2541 HOH   A O     1 
HETATM 19670 O  O     . HOH   CA 11 .    ? -56.379 49.407  97.536  1.00 38.20 ? 2542 HOH   A O     1 
HETATM 19671 O  O     . HOH   CA 11 .    ? -53.206 68.950  100.695 1.00 28.62 ? 2543 HOH   A O     1 
HETATM 19672 O  O     . HOH   CA 11 .    ? -41.125 68.456  93.394  1.00 28.71 ? 2544 HOH   A O     1 
HETATM 19673 O  O     . HOH   CA 11 .    ? -25.570 62.071  102.067 1.00 28.23 ? 2545 HOH   A O     1 
HETATM 19674 O  O     . HOH   CA 11 .    ? -13.496 60.340  86.671  1.00 37.27 ? 2546 HOH   A O     1 
HETATM 19675 O  O     . HOH   CA 11 .    ? -62.516 53.933  65.613  1.00 31.10 ? 2547 HOH   A O     1 
HETATM 19676 O  O     . HOH   CA 11 .    ? 10.671  79.572  128.532 1.00 33.64 ? 2548 HOH   A O     1 
HETATM 19677 O  O     . HOH   CA 11 .    ? -45.469 94.606  97.642  1.00 41.01 ? 2549 HOH   A O     1 
HETATM 19678 O  O     . HOH   CA 11 .    ? -9.360  73.626  129.103 1.00 37.31 ? 2550 HOH   A O     1 
HETATM 19679 O  O     . HOH   CA 11 .    ? -2.183  73.918  118.512 1.00 37.62 ? 2551 HOH   A O     1 
HETATM 19680 O  O     . HOH   CA 11 .    ? -8.855  57.626  84.189  1.00 35.96 ? 2552 HOH   A O     1 
HETATM 19681 O  O     . HOH   CA 11 .    ? -0.889  60.960  112.262 1.00 34.56 ? 2553 HOH   A O     1 
HETATM 19682 O  O     . HOH   CA 11 .    ? 2.075   79.821  93.590  1.00 46.25 ? 2554 HOH   A O     1 
HETATM 19683 O  O     . HOH   CA 11 .    ? -10.732 66.023  72.338  1.00 39.84 ? 2555 HOH   A O     1 
HETATM 19684 O  O     . HOH   CA 11 .    ? -56.970 73.017  98.767  1.00 38.13 ? 2556 HOH   A O     1 
HETATM 19685 O  O     . HOH   CA 11 .    ? 18.084  64.478  90.273  1.00 38.46 ? 2557 HOH   A O     1 
HETATM 19686 O  O     . HOH   CA 11 .    ? -8.819  52.830  100.869 1.00 40.38 ? 2558 HOH   A O     1 
HETATM 19687 O  O     . HOH   CA 11 .    ? 2.888   64.187  93.637  1.00 36.18 ? 2559 HOH   A O     1 
HETATM 19688 O  O     . HOH   CA 11 .    ? -33.635 62.392  89.429  1.00 42.27 ? 2560 HOH   A O     1 
HETATM 19689 O  O     . HOH   CA 11 .    ? -58.743 55.573  100.919 1.00 38.24 ? 2561 HOH   A O     1 
HETATM 19690 O  O     . HOH   CA 11 .    ? -42.871 42.397  107.568 1.00 45.78 ? 2562 HOH   A O     1 
HETATM 19691 O  O     . HOH   CA 11 .    ? -52.172 73.140  102.508 1.00 28.99 ? 2563 HOH   A O     1 
HETATM 19692 O  O     . HOH   CA 11 .    ? -46.904 80.881  89.653  1.00 36.04 ? 2564 HOH   A O     1 
HETATM 19693 O  O     . HOH   CA 11 .    ? -60.324 45.067  90.115  1.00 31.71 ? 2565 HOH   A O     1 
HETATM 19694 O  O     . HOH   CA 11 .    ? -69.786 61.739  72.408  1.00 26.34 ? 2566 HOH   A O     1 
HETATM 19695 O  O     . HOH   CA 11 .    ? -66.769 47.691  73.381  1.00 32.27 ? 2567 HOH   A O     1 
HETATM 19696 O  O     . HOH   CA 11 .    ? -36.780 82.426  77.127  1.00 36.55 ? 2568 HOH   A O     1 
HETATM 19697 O  O     . HOH   CA 11 .    ? -51.704 81.145  87.730  1.00 42.72 ? 2569 HOH   A O     1 
HETATM 19698 O  O     . HOH   CA 11 .    ? 0.666   71.325  117.266 1.00 35.82 ? 2570 HOH   A O     1 
HETATM 19699 O  O     . HOH   CA 11 .    ? -7.538  64.454  67.500  1.00 49.87 ? 2571 HOH   A O     1 
HETATM 19700 O  O     . HOH   CA 11 .    ? -21.498 92.725  100.863 1.00 43.47 ? 2572 HOH   A O     1 
HETATM 19701 O  O     . HOH   CA 11 .    ? 21.334  81.163  99.201  1.00 41.90 ? 2573 HOH   A O     1 
HETATM 19702 O  O     . HOH   CA 11 .    ? -14.055 96.318  116.967 1.00 39.61 ? 2574 HOH   A O     1 
HETATM 19703 O  O     . HOH   CA 11 .    ? -28.839 77.722  70.193  1.00 33.82 ? 2575 HOH   A O     1 
HETATM 19704 O  O     . HOH   CA 11 .    ? -4.180  79.929  124.765 1.00 32.66 ? 2576 HOH   A O     1 
HETATM 19705 O  O     . HOH   CA 11 .    ? 24.806  62.960  100.352 1.00 39.30 ? 2577 HOH   A O     1 
HETATM 19706 O  O     . HOH   CA 11 .    ? 22.859  70.205  115.621 1.00 30.06 ? 2578 HOH   A O     1 
HETATM 19707 O  O     . HOH   CA 11 .    ? -51.902 43.288  103.148 1.00 41.57 ? 2579 HOH   A O     1 
HETATM 19708 O  O     . HOH   CA 11 .    ? -29.152 61.864  81.645  1.00 46.87 ? 2580 HOH   A O     1 
HETATM 19709 O  O     . HOH   CA 11 .    ? -64.661 67.685  89.256  1.00 40.92 ? 2581 HOH   A O     1 
HETATM 19710 O  O     . HOH   CA 11 .    ? -32.164 75.442  85.283  1.00 32.37 ? 2582 HOH   A O     1 
HETATM 19711 O  O     . HOH   CA 11 .    ? -29.480 92.412  108.735 1.00 32.91 ? 2583 HOH   A O     1 
HETATM 19712 O  O     . HOH   CA 11 .    ? -8.579  76.701  129.260 1.00 38.85 ? 2584 HOH   A O     1 
HETATM 19713 O  O     . HOH   CA 11 .    ? 2.975   68.653  94.556  1.00 39.29 ? 2585 HOH   A O     1 
HETATM 19714 O  O     . HOH   CA 11 .    ? -2.370  91.793  98.155  1.00 31.54 ? 2586 HOH   A O     1 
HETATM 19715 O  O     . HOH   CA 11 .    ? -0.605  86.098  96.699  1.00 41.58 ? 2587 HOH   A O     1 
HETATM 19716 O  O     . HOH   CA 11 .    ? -26.917 66.540  97.960  1.00 34.12 ? 2588 HOH   A O     1 
HETATM 19717 O  O     . HOH   CA 11 .    ? -19.511 48.095  50.746  1.00 41.14 ? 2589 HOH   A O     1 
HETATM 19718 O  O     . HOH   CA 11 .    ? -44.775 82.634  88.713  1.00 37.85 ? 2590 HOH   A O     1 
HETATM 19719 O  O     . HOH   CA 11 .    ? 6.600   62.737  94.613  1.00 26.65 ? 2591 HOH   A O     1 
HETATM 19720 O  O     . HOH   CA 11 .    ? -47.993 37.493  100.421 1.00 33.95 ? 2592 HOH   A O     1 
HETATM 19721 O  O     . HOH   CA 11 .    ? 2.538   71.235  95.311  1.00 41.17 ? 2593 HOH   A O     1 
HETATM 19722 O  O     . HOH   CA 11 .    ? -33.691 76.513  89.732  1.00 40.33 ? 2594 HOH   A O     1 
HETATM 19723 O  O     . HOH   CA 11 .    ? -32.438 65.595  124.505 1.00 32.70 ? 2595 HOH   A O     1 
HETATM 19724 O  O     . HOH   CA 11 .    ? -9.504  62.317  93.924  1.00 29.94 ? 2596 HOH   A O     1 
HETATM 19725 O  O     . HOH   CA 11 .    ? -49.180 77.712  93.662  1.00 38.02 ? 2597 HOH   A O     1 
HETATM 19726 O  O     . HOH   CA 11 .    ? -54.679 54.774  102.061 1.00 38.57 ? 2598 HOH   A O     1 
HETATM 19727 O  O     . HOH   CA 11 .    ? -18.717 46.883  52.945  1.00 35.69 ? 2599 HOH   A O     1 
HETATM 19728 O  O     . HOH   CA 11 .    ? -29.446 95.372  108.069 1.00 47.54 ? 2600 HOH   A O     1 
HETATM 19729 O  O     . HOH   CA 11 .    ? -20.934 52.846  100.913 1.00 37.22 ? 2601 HOH   A O     1 
HETATM 19730 O  O     . HOH   CA 11 .    ? -30.801 86.710  74.404  1.00 44.24 ? 2602 HOH   A O     1 
HETATM 19731 O  O     . HOH   CA 11 .    ? -14.802 65.777  48.716  1.00 42.02 ? 2603 HOH   A O     1 
HETATM 19732 O  O     . HOH   CA 11 .    ? -31.932 54.639  110.626 1.00 40.40 ? 2604 HOH   A O     1 
HETATM 19733 O  O     . HOH   CA 11 .    ? -55.510 46.275  65.103  1.00 36.85 ? 2605 HOH   A O     1 
HETATM 19734 O  O     . HOH   CA 11 .    ? -24.660 52.179  99.972  1.00 30.02 ? 2606 HOH   A O     1 
HETATM 19735 O  O     . HOH   CA 11 .    ? -10.097 49.159  106.929 1.00 39.18 ? 2607 HOH   A O     1 
HETATM 19736 O  O     . HOH   CA 11 .    ? -43.997 28.708  90.415  1.00 38.55 ? 2608 HOH   A O     1 
HETATM 19737 O  O     . HOH   CA 11 .    ? -8.288  49.030  51.197  1.00 39.66 ? 2609 HOH   A O     1 
HETATM 19738 O  O     . HOH   CA 11 .    ? -52.583 66.380  104.762 1.00 35.26 ? 2610 HOH   A O     1 
HETATM 19739 O  O     . HOH   CA 11 .    ? -18.653 73.904  106.088 1.00 24.23 ? 2611 HOH   A O     1 
HETATM 19740 O  O     . HOH   CA 11 .    ? -31.086 84.104  73.302  1.00 34.44 ? 2612 HOH   A O     1 
HETATM 19741 O  O     . HOH   CA 11 .    ? 23.835  58.124  100.471 1.00 34.33 ? 2613 HOH   A O     1 
HETATM 19742 O  O     . HOH   CA 11 .    ? -30.153 60.227  85.787  1.00 32.33 ? 2614 HOH   A O     1 
HETATM 19743 O  O     . HOH   CA 11 .    ? -65.164 56.594  69.318  1.00 35.44 ? 2615 HOH   A O     1 
HETATM 19744 O  O     . HOH   CA 11 .    ? -41.847 80.091  69.974  1.00 35.25 ? 2616 HOH   A O     1 
HETATM 19745 O  O     . HOH   CA 11 .    ? -62.648 55.541  69.743  1.00 25.50 ? 2617 HOH   A O     1 
HETATM 19746 O  O     . HOH   CA 11 .    ? -32.772 58.684  84.669  1.00 36.44 ? 2618 HOH   A O     1 
HETATM 19747 O  O     . HOH   CA 11 .    ? -18.698 70.810  69.084  1.00 38.39 ? 2619 HOH   A O     1 
HETATM 19748 O  O     . HOH   CA 11 .    ? -33.269 58.368  113.352 1.00 37.73 ? 2620 HOH   A O     1 
HETATM 19749 O  O     . HOH   CA 11 .    ? -54.930 41.615  99.634  1.00 43.97 ? 2621 HOH   A O     1 
HETATM 19750 O  O     . HOH   CA 11 .    ? -47.164 35.123  103.204 1.00 40.05 ? 2622 HOH   A O     1 
HETATM 19751 O  O     . HOH   CA 11 .    ? -3.585  83.423  112.218 1.00 29.59 ? 2623 HOH   A O     1 
HETATM 19752 O  O     . HOH   CA 11 .    ? -63.463 57.728  96.222  1.00 36.12 ? 2624 HOH   A O     1 
HETATM 19753 O  O     . HOH   CA 11 .    ? -3.900  87.777  96.667  1.00 40.22 ? 2625 HOH   A O     1 
HETATM 19754 O  O     . HOH   CA 11 .    ? -54.544 80.215  84.104  1.00 44.37 ? 2626 HOH   A O     1 
HETATM 19755 O  O     . HOH   CA 11 .    ? -22.094 68.590  131.899 1.00 39.25 ? 2627 HOH   A O     1 
HETATM 19756 O  O     . HOH   CA 11 .    ? -23.119 52.256  97.335  1.00 36.95 ? 2628 HOH   A O     1 
HETATM 19757 O  O     . HOH   CA 11 .    ? -29.414 59.968  88.497  1.00 21.29 ? 2629 HOH   A O     1 
HETATM 19758 O  O     . HOH   CA 11 .    ? 0.439   63.931  92.804  1.00 43.46 ? 2630 HOH   A O     1 
HETATM 19759 O  O     . HOH   CA 11 .    ? -20.406 74.762  101.764 1.00 32.78 ? 2631 HOH   A O     1 
HETATM 19760 O  O     . HOH   CA 11 .    ? -39.366 29.875  95.427  1.00 45.77 ? 2632 HOH   A O     1 
HETATM 19761 O  O     . HOH   CA 11 .    ? -2.694  84.904  96.574  1.00 34.52 ? 2633 HOH   A O     1 
HETATM 19762 O  O     . HOH   CA 11 .    ? -7.521  69.410  129.889 1.00 41.81 ? 2634 HOH   A O     1 
HETATM 19763 O  O     . HOH   CA 11 .    ? -51.877 47.202  96.419  1.00 27.10 ? 2635 HOH   A O     1 
HETATM 19764 O  O     . HOH   CA 11 .    ? -19.322 57.612  106.521 1.00 30.09 ? 2636 HOH   A O     1 
HETATM 19765 O  O     . HOH   CA 11 .    ? -58.578 59.698  102.875 1.00 40.03 ? 2637 HOH   A O     1 
HETATM 19766 O  O     . HOH   CA 11 .    ? -61.526 70.693  85.519  1.00 33.36 ? 2638 HOH   A O     1 
HETATM 19767 O  O     . HOH   CA 11 .    ? -56.688 76.221  76.871  1.00 28.23 ? 2639 HOH   A O     1 
HETATM 19768 O  O     . HOH   CA 11 .    ? -61.929 51.048  66.353  1.00 34.53 ? 2640 HOH   A O     1 
HETATM 19769 O  O     . HOH   CA 11 .    ? -1.950  75.109  120.770 1.00 37.18 ? 2641 HOH   A O     1 
HETATM 19770 O  O     . HOH   CA 11 .    ? -15.142 39.398  70.341  1.00 42.33 ? 2642 HOH   A O     1 
HETATM 19771 O  O     . HOH   CA 11 .    ? -12.542 61.854  104.990 1.00 29.42 ? 2643 HOH   A O     1 
HETATM 19772 O  O     . HOH   CA 11 .    ? -66.831 39.347  73.659  1.00 38.08 ? 2644 HOH   A O     1 
HETATM 19773 O  O     . HOH   CA 11 .    ? 3.963   92.978  99.306  1.00 45.57 ? 2645 HOH   A O     1 
HETATM 19774 O  O     . HOH   CA 11 .    ? 5.326   70.454  86.840  1.00 38.42 ? 2646 HOH   A O     1 
HETATM 19775 O  O     . HOH   CA 11 .    ? -24.117 50.520  95.327  1.00 35.28 ? 2647 HOH   A O     1 
HETATM 19776 O  O     . HOH   CA 11 .    ? -61.802 52.927  93.804  1.00 38.16 ? 2648 HOH   A O     1 
HETATM 19777 O  O     . HOH   CA 11 .    ? -54.983 52.911  100.382 1.00 32.74 ? 2649 HOH   A O     1 
HETATM 19778 O  O     . HOH   CA 11 .    ? -8.599  70.777  132.105 1.00 42.07 ? 2650 HOH   A O     1 
HETATM 19779 O  O     . HOH   CA 11 .    ? 12.448  62.567  92.992  1.00 30.54 ? 2651 HOH   A O     1 
HETATM 19780 O  O     . HOH   CA 11 .    ? -46.238 39.067  104.315 1.00 31.72 ? 2652 HOH   A O     1 
HETATM 19781 O  O     . HOH   CA 11 .    ? 12.129  91.111  115.656 1.00 46.70 ? 2653 HOH   A O     1 
HETATM 19782 O  O     . HOH   CA 11 .    ? -35.427 39.274  104.233 1.00 43.45 ? 2654 HOH   A O     1 
HETATM 19783 O  O     . HOH   CA 11 .    ? -23.763 72.513  71.602  1.00 42.17 ? 2655 HOH   A O     1 
HETATM 19784 O  O     . HOH   CA 11 .    ? -34.953 63.884  121.423 1.00 39.00 ? 2656 HOH   A O     1 
HETATM 19785 O  O     . HOH   CA 11 .    ? -42.387 26.351  84.914  1.00 43.50 ? 2657 HOH   A O     1 
HETATM 19786 O  O     . HOH   CA 11 .    ? 3.561   69.204  88.271  1.00 31.20 ? 2658 HOH   A O     1 
HETATM 19787 O  O     . HOH   CA 11 .    ? -56.917 52.603  98.612  1.00 32.10 ? 2659 HOH   A O     1 
HETATM 19788 O  O     . HOH   CA 11 .    ? -42.225 61.929  52.821  1.00 43.97 ? 2660 HOH   A O     1 
HETATM 19789 O  O     . HOH   CA 11 .    ? -57.135 28.190  92.236  1.00 35.77 ? 2661 HOH   A O     1 
HETATM 19790 O  O     . HOH   CA 11 .    ? -25.280 62.763  99.622  1.00 27.72 ? 2662 HOH   A O     1 
HETATM 19791 O  O     . HOH   CA 11 .    ? -56.579 76.394  80.752  1.00 37.92 ? 2663 HOH   A O     1 
HETATM 19792 O  O     . HOH   CA 11 .    ? -22.124 64.726  132.124 1.00 42.03 ? 2664 HOH   A O     1 
HETATM 19793 O  O     . HOH   CA 11 .    ? -9.050  43.126  57.895  1.00 37.86 ? 2665 HOH   A O     1 
HETATM 19794 O  O     . HOH   CA 11 .    ? -39.414 71.897  95.590  1.00 32.91 ? 2666 HOH   A O     1 
HETATM 19795 O  O     . HOH   CA 11 .    ? -18.830 92.753  101.443 1.00 48.28 ? 2667 HOH   A O     1 
HETATM 19796 O  O     . HOH   CA 11 .    ? -55.147 42.438  62.810  1.00 43.83 ? 2668 HOH   A O     1 
HETATM 19797 O  O     . HOH   CA 11 .    ? -38.068 69.329  95.549  1.00 34.64 ? 2669 HOH   A O     1 
HETATM 19798 O  O     . HOH   CA 11 .    ? 11.089  64.652  93.068  1.00 31.34 ? 2670 HOH   A O     1 
HETATM 19799 O  O     . HOH   CA 11 .    ? -70.000 54.437  86.712  1.00 44.95 ? 2671 HOH   A O     1 
HETATM 19800 O  O     . HOH   CA 11 .    ? 22.595  63.142  95.065  1.00 38.62 ? 2672 HOH   A O     1 
HETATM 19801 O  O     . HOH   CA 11 .    ? -68.092 63.265  89.739  1.00 45.93 ? 2673 HOH   A O     1 
HETATM 19802 O  O     . HOH   CA 11 .    ? -31.860 61.568  121.759 1.00 34.72 ? 2674 HOH   A O     1 
HETATM 19803 O  O     . HOH   CA 11 .    ? 13.786  66.031  90.457  1.00 36.84 ? 2675 HOH   A O     1 
HETATM 19804 O  O     . HOH   CA 11 .    ? -33.297 78.169  70.974  1.00 38.65 ? 2676 HOH   A O     1 
HETATM 19805 O  O     . HOH   CA 11 .    ? -33.152 57.336  110.876 1.00 35.22 ? 2677 HOH   A O     1 
HETATM 19806 O  O     . HOH   CA 11 .    ? -33.503 88.271  129.204 1.00 38.00 ? 2678 HOH   A O     1 
HETATM 19807 O  O     . HOH   CA 11 .    ? -47.455 59.339  55.489  1.00 36.81 ? 2679 HOH   A O     1 
HETATM 19808 O  O     . HOH   CA 11 .    ? 6.610   59.976  94.157  1.00 37.69 ? 2680 HOH   A O     1 
HETATM 19809 O  O     . HOH   CA 11 .    ? -56.669 71.447  100.498 1.00 42.20 ? 2681 HOH   A O     1 
HETATM 19810 O  O     . HOH   CA 11 .    ? -35.621 39.407  73.461  1.00 39.97 ? 2682 HOH   A O     1 
HETATM 19811 O  O     . HOH   CA 11 .    ? -37.256 34.481  89.851  1.00 35.77 ? 2683 HOH   A O     1 
HETATM 19812 O  O     . HOH   CA 11 .    ? -34.756 78.692  126.466 1.00 37.41 ? 2684 HOH   A O     1 
HETATM 19813 O  O     . HOH   CA 11 .    ? -39.702 83.295  76.334  1.00 38.86 ? 2685 HOH   A O     1 
HETATM 19814 O  O     . HOH   CA 11 .    ? -68.247 70.275  69.125  1.00 33.44 ? 2686 HOH   A O     1 
HETATM 19815 O  O     . HOH   CA 11 .    ? -47.666 37.918  102.869 1.00 36.70 ? 2687 HOH   A O     1 
HETATM 19816 O  O     . HOH   CA 11 .    ? -55.998 78.739  77.318  1.00 31.70 ? 2688 HOH   A O     1 
HETATM 19817 O  O     . HOH   CA 11 .    ? -36.768 32.151  90.637  1.00 33.41 ? 2689 HOH   A O     1 
HETATM 19818 O  O     . HOH   CA 11 .    ? -36.136 81.156  70.144  1.00 42.78 ? 2690 HOH   A O     1 
HETATM 19819 O  O     . HOH   CA 11 .    ? -54.084 71.294  102.341 1.00 35.38 ? 2691 HOH   A O     1 
HETATM 19820 O  O     . HOH   CA 11 .    ? -35.332 56.548  109.517 1.00 38.78 ? 2692 HOH   A O     1 
HETATM 19821 O  O     . HOH   CA 11 .    ? -53.895 47.598  98.190  1.00 33.51 ? 2693 HOH   A O     1 
HETATM 19822 O  O     . HOH   CA 11 .    ? -33.973 81.266  71.486  1.00 35.43 ? 2694 HOH   A O     1 
HETATM 19823 O  O     . HOH   CA 11 .    ? 13.495  63.166  90.482  1.00 35.93 ? 2695 HOH   A O     1 
HETATM 19824 O  O     . HOH   DA 11 .    ? 8.389   31.476  81.253  1.00 33.51 ? 1401 HOH   B O     1 
HETATM 19825 O  O     . HOH   DA 11 .    ? 30.344  42.176  66.772  1.00 26.99 ? 1402 HOH   B O     1 
HETATM 19826 O  O     . HOH   DA 11 .    ? -11.287 27.792  81.016  1.00 26.33 ? 1403 HOH   B O     1 
HETATM 19827 O  O     . HOH   DA 11 .    ? 29.266  42.354  84.008  1.00 26.89 ? 1404 HOH   B O     1 
HETATM 19828 O  O     . HOH   DA 11 .    ? 8.275   16.060  92.552  1.00 31.67 ? 1405 HOH   B O     1 
HETATM 19829 O  O     . HOH   DA 11 .    ? 3.407   21.160  136.889 1.00 35.56 ? 1406 HOH   B O     1 
HETATM 19830 O  O     . HOH   DA 11 .    ? -0.809  47.906  87.161  1.00 35.31 ? 1407 HOH   B O     1 
HETATM 19831 O  O     . HOH   DA 11 .    ? 0.368   77.698  69.262  1.00 32.59 ? 1408 HOH   B O     1 
HETATM 19832 O  O     . HOH   DA 11 .    ? -4.420  26.721  99.540  1.00 25.54 ? 1409 HOH   B O     1 
HETATM 19833 O  O     . HOH   DA 11 .    ? 10.323  35.842  78.523  1.00 34.38 ? 1410 HOH   B O     1 
HETATM 19834 O  O     . HOH   DA 11 .    ? -7.331  34.369  66.144  1.00 40.45 ? 1411 HOH   B O     1 
HETATM 19835 O  O     . HOH   DA 11 .    ? 3.961   55.362  72.362  1.00 24.33 ? 1412 HOH   B O     1 
HETATM 19836 O  O     . HOH   DA 11 .    ? -0.121  18.691  80.278  1.00 24.94 ? 1413 HOH   B O     1 
HETATM 19837 O  O     . HOH   DA 11 .    ? -2.460  29.417  57.381  1.00 34.05 ? 1414 HOH   B O     1 
HETATM 19838 O  O     . HOH   DA 11 .    ? 21.080  39.959  47.767  1.00 38.67 ? 1415 HOH   B O     1 
HETATM 19839 O  O     . HOH   DA 11 .    ? 3.962   72.237  85.293  1.00 37.20 ? 1416 HOH   B O     1 
HETATM 19840 O  O     . HOH   DA 11 .    ? -14.643 -7.281  107.575 1.00 39.36 ? 1417 HOH   B O     1 
HETATM 19841 O  O     . HOH   DA 11 .    ? -2.051  62.480  69.408  1.00 33.35 ? 1418 HOH   B O     1 
HETATM 19842 O  O     . HOH   DA 11 .    ? 28.537  50.932  74.528  1.00 39.00 ? 1419 HOH   B O     1 
HETATM 19843 O  O     . HOH   DA 11 .    ? -2.688  5.036   84.773  1.00 30.63 ? 1420 HOH   B O     1 
HETATM 19844 O  O     . HOH   DA 11 .    ? 12.199  6.479   117.554 1.00 36.48 ? 1421 HOH   B O     1 
HETATM 19845 O  O     . HOH   DA 11 .    ? -0.520  73.328  77.494  1.00 30.03 ? 1422 HOH   B O     1 
HETATM 19846 O  O     . HOH   DA 11 .    ? -14.460 9.598   118.233 1.00 32.07 ? 1423 HOH   B O     1 
HETATM 19847 O  O     . HOH   DA 11 .    ? 18.820  21.299  55.025  1.00 32.40 ? 1424 HOH   B O     1 
HETATM 19848 O  O     . HOH   DA 11 .    ? -4.254  23.958  107.797 1.00 42.06 ? 1425 HOH   B O     1 
HETATM 19849 O  O     . HOH   DA 11 .    ? 6.818   51.369  57.388  1.00 29.38 ? 1426 HOH   B O     1 
HETATM 19850 O  O     . HOH   DA 11 .    ? 33.280  19.507  87.394  1.00 22.42 ? 1427 HOH   B O     1 
HETATM 19851 O  O     . HOH   DA 11 .    ? 2.086   17.272  112.187 1.00 30.50 ? 1428 HOH   B O     1 
HETATM 19852 O  O     . HOH   DA 11 .    ? 27.361  13.267  66.433  1.00 31.11 ? 1429 HOH   B O     1 
HETATM 19853 O  O     . HOH   DA 11 .    ? -22.176 28.957  86.815  1.00 41.69 ? 1430 HOH   B O     1 
HETATM 19854 O  O     . HOH   DA 11 .    ? -13.768 28.990  97.503  1.00 36.04 ? 1431 HOH   B O     1 
HETATM 19855 O  O     . HOH   DA 11 .    ? -10.395 -2.444  115.483 1.00 33.40 ? 1432 HOH   B O     1 
HETATM 19856 O  O     . HOH   DA 11 .    ? 13.915  58.163  60.520  1.00 35.86 ? 1433 HOH   B O     1 
HETATM 19857 O  O     . HOH   DA 11 .    ? 30.708  26.190  52.731  1.00 37.62 ? 1434 HOH   B O     1 
HETATM 19858 O  O     . HOH   DA 11 .    ? 3.381   56.271  62.641  1.00 39.25 ? 1435 HOH   B O     1 
HETATM 19859 O  O     . HOH   DA 11 .    ? 0.814   -10.202 110.690 1.00 30.42 ? 1436 HOH   B O     1 
HETATM 19860 O  O     . HOH   DA 11 .    ? 16.497  14.536  109.216 1.00 26.80 ? 1437 HOH   B O     1 
HETATM 19861 O  O     . HOH   DA 11 .    ? -1.164  22.420  71.064  1.00 31.35 ? 1438 HOH   B O     1 
HETATM 19862 O  O     . HOH   DA 11 .    ? 15.288  21.833  88.280  1.00 33.51 ? 1439 HOH   B O     1 
HETATM 19863 O  O     . HOH   DA 11 .    ? -14.173 54.141  117.858 1.00 26.83 ? 1440 HOH   B O     1 
HETATM 19864 O  O     . HOH   DA 11 .    ? 25.941  65.547  54.257  1.00 39.71 ? 1441 HOH   B O     1 
HETATM 19865 O  O     . HOH   DA 11 .    ? -25.998 6.545   111.494 1.00 40.50 ? 1442 HOH   B O     1 
HETATM 19866 O  O     . HOH   DA 11 .    ? -11.524 -4.525  97.518  1.00 36.54 ? 1443 HOH   B O     1 
HETATM 19867 O  O     . HOH   DA 11 .    ? -17.857 0.490   99.365  1.00 34.03 ? 1444 HOH   B O     1 
HETATM 19868 O  O     . HOH   DA 11 .    ? -4.486  45.426  89.457  1.00 39.14 ? 1445 HOH   B O     1 
HETATM 19869 O  O     . HOH   DA 11 .    ? -5.646  -1.408  123.242 1.00 37.89 ? 1446 HOH   B O     1 
HETATM 19870 O  O     . HOH   DA 11 .    ? -19.892 28.010  91.110  1.00 36.74 ? 1447 HOH   B O     1 
HETATM 19871 O  O     . HOH   DA 11 .    ? -8.820  45.371  108.598 1.00 31.80 ? 1448 HOH   B O     1 
HETATM 19872 O  O     . HOH   DA 11 .    ? 3.451   21.579  102.291 1.00 29.49 ? 1449 HOH   B O     1 
HETATM 19873 O  O     . HOH   DA 11 .    ? 6.290   15.785  124.219 1.00 34.44 ? 1450 HOH   B O     1 
HETATM 19874 O  O     . HOH   DA 11 .    ? 26.437  41.871  49.399  1.00 43.45 ? 1451 HOH   B O     1 
HETATM 19875 O  O     . HOH   DA 11 .    ? -8.767  24.289  76.885  1.00 33.35 ? 1452 HOH   B O     1 
HETATM 19876 O  O     . HOH   DA 11 .    ? 22.536  35.066  115.275 1.00 27.35 ? 1453 HOH   B O     1 
HETATM 19877 O  O     . HOH   DA 11 .    ? 6.903   19.504  116.281 1.00 28.42 ? 1454 HOH   B O     1 
HETATM 19878 O  O     . HOH   DA 11 .    ? -10.005 -4.487  106.966 1.00 26.96 ? 1455 HOH   B O     1 
HETATM 19879 O  O     . HOH   DA 11 .    ? -0.552  27.067  68.415  1.00 16.95 ? 1456 HOH   B O     1 
HETATM 19880 O  O     . HOH   DA 11 .    ? 9.449   25.981  55.032  1.00 20.36 ? 1457 HOH   B O     1 
HETATM 19881 O  O     . HOH   DA 11 .    ? 34.034  62.568  78.087  1.00 16.95 ? 1458 HOH   B O     1 
HETATM 19882 O  O     . HOH   DA 11 .    ? 10.394  51.402  75.229  1.00 21.05 ? 1459 HOH   B O     1 
HETATM 19883 O  O     . HOH   DA 11 .    ? -10.438 25.493  102.740 1.00 33.31 ? 1460 HOH   B O     1 
HETATM 19884 O  O     . HOH   DA 11 .    ? -17.258 15.469  79.543  1.00 37.46 ? 1461 HOH   B O     1 
HETATM 19885 O  O     . HOH   DA 11 .    ? 23.253  18.504  80.203  1.00 24.36 ? 1462 HOH   B O     1 
HETATM 19886 O  O     . HOH   DA 11 .    ? -5.680  39.624  90.022  1.00 39.73 ? 1463 HOH   B O     1 
HETATM 19887 O  O     . HOH   DA 11 .    ? 7.287   32.744  97.884  1.00 30.87 ? 1464 HOH   B O     1 
HETATM 19888 O  O     . HOH   DA 11 .    ? 5.974   32.040  78.914  1.00 19.47 ? 1465 HOH   B O     1 
HETATM 19889 O  O     . HOH   DA 11 .    ? -28.839 17.738  84.496  1.00 38.48 ? 1466 HOH   B O     1 
HETATM 19890 O  O     . HOH   DA 11 .    ? -22.728 9.699   121.860 1.00 40.33 ? 1467 HOH   B O     1 
HETATM 19891 O  O     . HOH   DA 11 .    ? 11.176  24.849  107.928 1.00 27.12 ? 1468 HOH   B O     1 
HETATM 19892 O  O     . HOH   DA 11 .    ? -22.689 19.314  101.944 1.00 29.30 ? 1469 HOH   B O     1 
HETATM 19893 O  O     . HOH   DA 11 .    ? 13.879  41.544  76.730  1.00 17.11 ? 1470 HOH   B O     1 
HETATM 19894 O  O     . HOH   DA 11 .    ? 25.537  8.734   75.297  1.00 38.61 ? 1471 HOH   B O     1 
HETATM 19895 O  O     . HOH   DA 11 .    ? -12.220 4.058   129.361 1.00 42.98 ? 1472 HOH   B O     1 
HETATM 19896 O  O     . HOH   DA 11 .    ? 27.800  39.685  50.322  1.00 40.03 ? 1473 HOH   B O     1 
HETATM 19897 O  O     . HOH   DA 11 .    ? -29.088 22.944  89.862  1.00 40.88 ? 1474 HOH   B O     1 
HETATM 19898 O  O     . HOH   DA 11 .    ? 33.115  18.040  89.751  1.00 37.98 ? 1475 HOH   B O     1 
HETATM 19899 O  O     . HOH   DA 11 .    ? 14.645  55.030  110.594 1.00 34.98 ? 1476 HOH   B O     1 
HETATM 19900 O  O     . HOH   DA 11 .    ? 18.658  62.232  57.205  1.00 33.43 ? 1477 HOH   B O     1 
HETATM 19901 O  O     . HOH   DA 11 .    ? 17.534  12.911  116.997 1.00 26.88 ? 1478 HOH   B O     1 
HETATM 19902 O  O     . HOH   DA 11 .    ? 18.702  67.339  82.274  1.00 24.30 ? 1479 HOH   B O     1 
HETATM 19903 O  O     . HOH   DA 11 .    ? 32.911  29.813  61.718  1.00 26.54 ? 1480 HOH   B O     1 
HETATM 19904 O  O     . HOH   DA 11 .    ? 32.462  19.125  57.896  1.00 31.01 ? 1481 HOH   B O     1 
HETATM 19905 O  O     . HOH   DA 11 .    ? -11.968 -4.450  109.077 1.00 31.48 ? 1482 HOH   B O     1 
HETATM 19906 O  O     . HOH   DA 11 .    ? 1.483   20.603  103.863 1.00 24.79 ? 1483 HOH   B O     1 
HETATM 19907 O  O     . HOH   DA 11 .    ? -5.819  5.319   121.943 1.00 23.91 ? 1484 HOH   B O     1 
HETATM 19908 O  O     . HOH   DA 11 .    ? -14.662 15.292  78.594  1.00 36.63 ? 1485 HOH   B O     1 
HETATM 19909 O  O     . HOH   DA 11 .    ? 8.010   8.223   72.389  1.00 36.76 ? 1486 HOH   B O     1 
HETATM 19910 O  O     . HOH   DA 11 .    ? 3.203   18.424  88.784  1.00 24.75 ? 1487 HOH   B O     1 
HETATM 19911 O  O     . HOH   DA 11 .    ? 3.351   33.903  86.456  1.00 18.71 ? 1488 HOH   B O     1 
HETATM 19912 O  O     . HOH   DA 11 .    ? 1.454   57.339  87.233  1.00 36.43 ? 1489 HOH   B O     1 
HETATM 19913 O  O     . HOH   DA 11 .    ? 18.390  38.633  115.405 1.00 31.71 ? 1490 HOH   B O     1 
HETATM 19914 O  O     . HOH   DA 11 .    ? 34.710  27.220  100.051 1.00 38.49 ? 1491 HOH   B O     1 
HETATM 19915 O  O     . HOH   DA 11 .    ? -4.777  27.111  70.002  1.00 29.89 ? 1492 HOH   B O     1 
HETATM 19916 O  O     . HOH   DA 11 .    ? 16.379  2.739   104.269 1.00 37.71 ? 1493 HOH   B O     1 
HETATM 19917 O  O     . HOH   DA 11 .    ? 18.779  24.916  54.304  1.00 22.73 ? 1494 HOH   B O     1 
HETATM 19918 O  O     . HOH   DA 11 .    ? 3.553   7.976   92.134  1.00 20.33 ? 1495 HOH   B O     1 
HETATM 19919 O  O     . HOH   DA 11 .    ? 6.038   50.034  87.960  1.00 32.23 ? 1496 HOH   B O     1 
HETATM 19920 O  O     . HOH   DA 11 .    ? -4.432  64.208  80.838  1.00 16.48 ? 1497 HOH   B O     1 
HETATM 19921 O  O     . HOH   DA 11 .    ? 11.037  18.387  64.421  1.00 24.64 ? 1498 HOH   B O     1 
HETATM 19922 O  O     . HOH   DA 11 .    ? 12.161  13.047  110.302 1.00 25.77 ? 1499 HOH   B O     1 
HETATM 19923 O  O     . HOH   DA 11 .    ? -4.715  59.862  125.254 1.00 29.18 ? 1500 HOH   B O     1 
HETATM 19924 O  O     . HOH   DA 11 .    ? 14.889  40.473  72.792  1.00 16.71 ? 1501 HOH   B O     1 
HETATM 19925 O  O     . HOH   DA 11 .    ? 40.005  24.530  82.821  1.00 40.54 ? 1502 HOH   B O     1 
HETATM 19926 O  O     . HOH   DA 11 .    ? -4.798  -1.896  96.756  1.00 22.22 ? 1503 HOH   B O     1 
HETATM 19927 O  O     . HOH   DA 11 .    ? 20.649  55.144  107.838 1.00 37.42 ? 1504 HOH   B O     1 
HETATM 19928 O  O     . HOH   DA 11 .    ? -6.161  40.354  62.739  1.00 30.11 ? 1505 HOH   B O     1 
HETATM 19929 O  O     . HOH   DA 11 .    ? -5.901  37.386  77.578  1.00 28.51 ? 1506 HOH   B O     1 
HETATM 19930 O  O     . HOH   DA 11 .    ? 5.309   51.386  109.573 1.00 35.28 ? 1507 HOH   B O     1 
HETATM 19931 O  O     . HOH   DA 11 .    ? -10.293 39.821  127.023 1.00 38.05 ? 1508 HOH   B O     1 
HETATM 19932 O  O     . HOH   DA 11 .    ? 11.566  -1.943  109.576 1.00 43.57 ? 1509 HOH   B O     1 
HETATM 19933 O  O     . HOH   DA 11 .    ? 4.025   21.564  118.685 1.00 30.27 ? 1510 HOH   B O     1 
HETATM 19934 O  O     . HOH   DA 11 .    ? 34.081  54.494  75.114  1.00 33.80 ? 1511 HOH   B O     1 
HETATM 19935 O  O     . HOH   DA 11 .    ? -21.257 15.807  82.513  1.00 27.59 ? 1512 HOH   B O     1 
HETATM 19936 O  O     . HOH   DA 11 .    ? 8.304   -0.837  106.931 1.00 34.88 ? 1513 HOH   B O     1 
HETATM 19937 O  O     . HOH   DA 11 .    ? 38.709  26.155  80.398  1.00 34.59 ? 1514 HOH   B O     1 
HETATM 19938 O  O     . HOH   DA 11 .    ? 28.769  69.319  79.588  1.00 24.62 ? 1515 HOH   B O     1 
HETATM 19939 O  O     . HOH   DA 11 .    ? 4.902   32.391  89.051  1.00 30.79 ? 1516 HOH   B O     1 
HETATM 19940 O  O     . HOH   DA 11 .    ? 18.626  13.171  95.301  1.00 27.11 ? 1517 HOH   B O     1 
HETATM 19941 O  O     . HOH   DA 11 .    ? 10.816  46.459  106.534 1.00 29.29 ? 1518 HOH   B O     1 
HETATM 19942 O  O     . HOH   DA 11 .    ? 10.943  19.391  61.417  1.00 27.56 ? 1519 HOH   B O     1 
HETATM 19943 O  O     . HOH   DA 11 .    ? 6.508   5.910   92.147  1.00 21.07 ? 1520 HOH   B O     1 
HETATM 19944 O  O     . HOH   DA 11 .    ? 2.339   21.909  130.038 1.00 29.43 ? 1521 HOH   B O     1 
HETATM 19945 O  O     . HOH   DA 11 .    ? 1.488   13.282  101.658 1.00 18.84 ? 1522 HOH   B O     1 
HETATM 19946 O  O     . HOH   DA 11 .    ? 38.173  34.087  102.536 1.00 27.88 ? 1523 HOH   B O     1 
HETATM 19947 O  O     . HOH   DA 11 .    ? -12.653 20.113  83.691  1.00 21.95 ? 1524 HOH   B O     1 
HETATM 19948 O  O     . HOH   DA 11 .    ? 5.520   43.865  58.308  1.00 31.07 ? 1525 HOH   B O     1 
HETATM 19949 O  O     . HOH   DA 11 .    ? 21.019  5.637   68.188  1.00 39.87 ? 1526 HOH   B O     1 
HETATM 19950 O  O     . HOH   DA 11 .    ? -4.830  6.871   81.616  1.00 37.91 ? 1527 HOH   B O     1 
HETATM 19951 O  O     . HOH   DA 11 .    ? 21.498  79.777  69.775  1.00 32.97 ? 1528 HOH   B O     1 
HETATM 19952 O  O     . HOH   DA 11 .    ? 28.872  68.469  72.298  1.00 34.40 ? 1529 HOH   B O     1 
HETATM 19953 O  O     . HOH   DA 11 .    ? -18.266 31.551  93.177  1.00 45.56 ? 1530 HOH   B O     1 
HETATM 19954 O  O     . HOH   DA 11 .    ? 11.883  11.212  71.389  1.00 20.02 ? 1531 HOH   B O     1 
HETATM 19955 O  O     . HOH   DA 11 .    ? 2.460   44.046  70.191  1.00 14.56 ? 1532 HOH   B O     1 
HETATM 19956 O  O     . HOH   DA 11 .    ? 10.755  79.861  67.533  1.00 40.03 ? 1533 HOH   B O     1 
HETATM 19957 O  O     . HOH   DA 11 .    ? 18.314  7.603   100.521 1.00 34.89 ? 1534 HOH   B O     1 
HETATM 19958 O  O     . HOH   DA 11 .    ? 25.434  53.352  96.254  1.00 35.23 ? 1535 HOH   B O     1 
HETATM 19959 O  O     . HOH   DA 11 .    ? 8.997   23.345  108.744 1.00 29.31 ? 1536 HOH   B O     1 
HETATM 19960 O  O     . HOH   DA 11 .    ? -31.332 16.183  102.082 1.00 35.83 ? 1537 HOH   B O     1 
HETATM 19961 O  O     . HOH   DA 11 .    ? 4.671   65.247  68.539  1.00 37.56 ? 1538 HOH   B O     1 
HETATM 19962 O  O     . HOH   DA 11 .    ? 17.995  23.297  88.004  1.00 26.50 ? 1539 HOH   B O     1 
HETATM 19963 O  O     . HOH   DA 11 .    ? 9.845   49.146  55.575  1.00 33.75 ? 1540 HOH   B O     1 
HETATM 19964 O  O     . HOH   DA 11 .    ? 18.788  31.481  73.061  1.00 18.67 ? 1541 HOH   B O     1 
HETATM 19965 O  O     . HOH   DA 11 .    ? 0.920   38.951  107.989 1.00 23.90 ? 1542 HOH   B O     1 
HETATM 19966 O  O     . HOH   DA 11 .    ? 14.791  20.920  92.370  1.00 28.04 ? 1543 HOH   B O     1 
HETATM 19967 O  O     . HOH   DA 11 .    ? -7.214  8.592   110.841 1.00 21.48 ? 1544 HOH   B O     1 
HETATM 19968 O  O     . HOH   DA 11 .    ? -10.551 11.108  129.498 1.00 38.13 ? 1545 HOH   B O     1 
HETATM 19969 O  O     . HOH   DA 11 .    ? -5.898  39.463  106.522 1.00 27.72 ? 1546 HOH   B O     1 
HETATM 19970 O  O     . HOH   DA 11 .    ? 14.784  56.008  74.597  1.00 24.44 ? 1547 HOH   B O     1 
HETATM 19971 O  O     . HOH   DA 11 .    ? -10.765 46.575  74.305  1.00 17.98 ? 1548 HOH   B O     1 
HETATM 19972 O  O     . HOH   DA 11 .    ? -9.531  10.187  122.729 1.00 25.47 ? 1549 HOH   B O     1 
HETATM 19973 O  O     . HOH   DA 11 .    ? 31.406  37.827  106.358 1.00 33.52 ? 1550 HOH   B O     1 
HETATM 19974 O  O     . HOH   DA 11 .    ? 32.301  26.858  68.474  1.00 35.03 ? 1551 HOH   B O     1 
HETATM 19975 O  O     . HOH   DA 11 .    ? -36.864 8.478   96.582  1.00 43.27 ? 1552 HOH   B O     1 
HETATM 19976 O  O     . HOH   DA 11 .    ? 39.116  26.957  87.506  1.00 32.36 ? 1553 HOH   B O     1 
HETATM 19977 O  O     . HOH   DA 11 .    ? -1.457  15.475  130.965 1.00 32.81 ? 1554 HOH   B O     1 
HETATM 19978 O  O     . HOH   DA 11 .    ? -4.280  18.859  97.928  1.00 15.39 ? 1555 HOH   B O     1 
HETATM 19979 O  O     . HOH   DA 11 .    ? -4.518  38.059  93.273  1.00 36.66 ? 1556 HOH   B O     1 
HETATM 19980 O  O     . HOH   DA 11 .    ? 8.293   24.963  105.439 1.00 36.39 ? 1557 HOH   B O     1 
HETATM 19981 O  O     . HOH   DA 11 .    ? 19.522  19.633  105.449 1.00 17.85 ? 1558 HOH   B O     1 
HETATM 19982 O  O     . HOH   DA 11 .    ? 9.657   30.806  109.742 1.00 37.42 ? 1559 HOH   B O     1 
HETATM 19983 O  O     . HOH   DA 11 .    ? 22.177  45.600  90.385  1.00 16.08 ? 1560 HOH   B O     1 
HETATM 19984 O  O     . HOH   DA 11 .    ? 17.158  55.072  97.027  1.00 25.17 ? 1561 HOH   B O     1 
HETATM 19985 O  O     . HOH   DA 11 .    ? 25.697  55.281  77.234  1.00 23.10 ? 1562 HOH   B O     1 
HETATM 19986 O  O     . HOH   DA 11 .    ? -6.646  12.399  125.113 1.00 27.75 ? 1563 HOH   B O     1 
HETATM 19987 O  O     . HOH   DA 11 .    ? 4.191   42.219  84.151  1.00 20.90 ? 1564 HOH   B O     1 
HETATM 19988 O  O     . HOH   DA 11 .    ? 26.446  20.676  55.617  1.00 31.42 ? 1565 HOH   B O     1 
HETATM 19989 O  O     . HOH   DA 11 .    ? 33.462  67.917  80.288  1.00 21.22 ? 1566 HOH   B O     1 
HETATM 19990 O  O     . HOH   DA 11 .    ? -29.052 13.119  98.419  1.00 43.24 ? 1567 HOH   B O     1 
HETATM 19991 O  O     . HOH   DA 11 .    ? 5.910   -5.549  116.577 1.00 37.00 ? 1568 HOH   B O     1 
HETATM 19992 O  O     . HOH   DA 11 .    ? -2.555  45.438  102.390 1.00 30.04 ? 1569 HOH   B O     1 
HETATM 19993 O  O     . HOH   DA 11 .    ? 17.860  11.689  105.959 1.00 37.46 ? 1570 HOH   B O     1 
HETATM 19994 O  O     . HOH   DA 11 .    ? -6.784  11.348  127.453 1.00 33.35 ? 1571 HOH   B O     1 
HETATM 19995 O  O     . HOH   DA 11 .    ? 5.850   25.664  86.092  1.00 31.64 ? 1572 HOH   B O     1 
HETATM 19996 O  O     . HOH   DA 11 .    ? -4.800  44.139  80.891  1.00 30.67 ? 1573 HOH   B O     1 
HETATM 19997 O  O     . HOH   DA 11 .    ? -6.645  52.582  106.931 1.00 28.45 ? 1574 HOH   B O     1 
HETATM 19998 O  O     . HOH   DA 11 .    ? 9.849   71.226  61.566  1.00 28.62 ? 1575 HOH   B O     1 
HETATM 19999 O  O     . HOH   DA 11 .    ? -5.287  51.665  75.319  1.00 19.48 ? 1576 HOH   B O     1 
HETATM 20000 O  O     . HOH   DA 11 .    ? -4.881  2.271   123.769 1.00 26.06 ? 1577 HOH   B O     1 
HETATM 20001 O  O     . HOH   DA 11 .    ? 21.264  50.579  87.461  1.00 21.68 ? 1578 HOH   B O     1 
HETATM 20002 O  O     . HOH   DA 11 .    ? -6.427  51.093  72.845  1.00 14.83 ? 1579 HOH   B O     1 
HETATM 20003 O  O     . HOH   DA 11 .    ? 29.707  27.413  56.028  1.00 21.56 ? 1580 HOH   B O     1 
HETATM 20004 O  O     . HOH   DA 11 .    ? -0.367  -7.071  106.743 1.00 26.05 ? 1581 HOH   B O     1 
HETATM 20005 O  O     . HOH   DA 11 .    ? 34.460  26.325  63.611  1.00 39.01 ? 1582 HOH   B O     1 
HETATM 20006 O  O     . HOH   DA 11 .    ? 13.918  81.182  69.214  1.00 37.13 ? 1583 HOH   B O     1 
HETATM 20007 O  O     . HOH   DA 11 .    ? 3.936   -8.629  104.038 1.00 32.68 ? 1584 HOH   B O     1 
HETATM 20008 O  O     . HOH   DA 11 .    ? 18.799  6.029   74.183  1.00 26.02 ? 1585 HOH   B O     1 
HETATM 20009 O  O     . HOH   DA 11 .    ? -2.396  48.910  63.426  1.00 17.29 ? 1586 HOH   B O     1 
HETATM 20010 O  O     . HOH   DA 11 .    ? 16.130  10.599  112.205 1.00 38.32 ? 1587 HOH   B O     1 
HETATM 20011 O  O     . HOH   DA 11 .    ? 23.114  48.629  106.523 1.00 30.91 ? 1588 HOH   B O     1 
HETATM 20012 O  O     . HOH   DA 11 .    ? 10.020  50.845  64.466  1.00 22.21 ? 1589 HOH   B O     1 
HETATM 20013 O  O     . HOH   DA 11 .    ? 33.335  12.236  74.574  1.00 30.13 ? 1590 HOH   B O     1 
HETATM 20014 O  O     . HOH   DA 11 .    ? 10.954  6.001   121.500 1.00 29.09 ? 1591 HOH   B O     1 
HETATM 20015 O  O     . HOH   DA 11 .    ? -7.978  20.291  79.336  1.00 35.52 ? 1592 HOH   B O     1 
HETATM 20016 O  O     . HOH   DA 11 .    ? 19.530  51.143  77.266  1.00 17.77 ? 1593 HOH   B O     1 
HETATM 20017 O  O     . HOH   DA 11 .    ? -18.161 26.001  82.851  1.00 33.77 ? 1594 HOH   B O     1 
HETATM 20018 O  O     . HOH   DA 11 .    ? 28.289  18.813  57.876  1.00 32.64 ? 1595 HOH   B O     1 
HETATM 20019 O  O     . HOH   DA 11 .    ? -2.416  39.566  87.003  1.00 17.37 ? 1596 HOH   B O     1 
HETATM 20020 O  O     . HOH   DA 11 .    ? 3.854   14.195  72.727  1.00 34.23 ? 1597 HOH   B O     1 
HETATM 20021 O  O     . HOH   DA 11 .    ? 24.009  19.151  97.927  1.00 30.24 ? 1598 HOH   B O     1 
HETATM 20022 O  O     . HOH   DA 11 .    ? 12.008  70.319  60.535  1.00 35.14 ? 1599 HOH   B O     1 
HETATM 20023 O  O     . HOH   DA 11 .    ? 12.508  54.618  84.675  1.00 35.30 ? 1600 HOH   B O     1 
HETATM 20024 O  O     . HOH   DA 11 .    ? 0.656   19.749  111.274 1.00 26.33 ? 1601 HOH   B O     1 
HETATM 20025 O  O     . HOH   DA 11 .    ? -30.075 11.918  96.130  1.00 39.39 ? 1602 HOH   B O     1 
HETATM 20026 O  O     . HOH   DA 11 .    ? 15.902  43.124  50.185  1.00 30.79 ? 1603 HOH   B O     1 
HETATM 20027 O  O     . HOH   DA 11 .    ? -14.087 -0.162  96.643  1.00 34.57 ? 1604 HOH   B O     1 
HETATM 20028 O  O     . HOH   DA 11 .    ? 7.674   65.372  63.581  1.00 27.12 ? 1605 HOH   B O     1 
HETATM 20029 O  O     . HOH   DA 11 .    ? 11.759  0.896   93.940  1.00 39.33 ? 1606 HOH   B O     1 
HETATM 20030 O  O     . HOH   DA 11 .    ? 2.527   30.759  79.909  1.00 16.72 ? 1607 HOH   B O     1 
HETATM 20031 O  O     . HOH   DA 11 .    ? 23.378  2.735   81.801  1.00 42.70 ? 1608 HOH   B O     1 
HETATM 20032 O  O     . HOH   DA 11 .    ? -13.131 8.944   124.170 1.00 31.73 ? 1609 HOH   B O     1 
HETATM 20033 O  O     . HOH   DA 11 .    ? 2.697   45.994  53.666  1.00 36.45 ? 1610 HOH   B O     1 
HETATM 20034 O  O     . HOH   DA 11 .    ? -1.473  14.692  85.713  1.00 22.46 ? 1611 HOH   B O     1 
HETATM 20035 O  O     . HOH   DA 11 .    ? 12.069  21.475  101.190 1.00 23.42 ? 1612 HOH   B O     1 
HETATM 20036 O  O     . HOH   DA 11 .    ? 17.334  27.562  82.748  1.00 25.05 ? 1613 HOH   B O     1 
HETATM 20037 O  O     . HOH   DA 11 .    ? 6.483   33.850  86.562  1.00 18.59 ? 1614 HOH   B O     1 
HETATM 20038 O  O     . HOH   DA 11 .    ? -4.983  30.874  77.211  1.00 17.10 ? 1615 HOH   B O     1 
HETATM 20039 O  O     . HOH   DA 11 .    ? 14.915  39.004  76.880  1.00 15.19 ? 1616 HOH   B O     1 
HETATM 20040 O  O     . HOH   DA 11 .    ? -2.515  41.936  61.521  1.00 21.81 ? 1617 HOH   B O     1 
HETATM 20041 O  O     . HOH   DA 11 .    ? 7.437   49.218  106.410 1.00 21.04 ? 1618 HOH   B O     1 
HETATM 20042 O  O     . HOH   DA 11 .    ? 31.688  38.524  83.971  1.00 26.27 ? 1619 HOH   B O     1 
HETATM 20043 O  O     . HOH   DA 11 .    ? 4.757   35.613  117.146 1.00 45.45 ? 1620 HOH   B O     1 
HETATM 20044 O  O     . HOH   DA 11 .    ? 6.173   21.605  89.153  1.00 37.69 ? 1621 HOH   B O     1 
HETATM 20045 O  O     . HOH   DA 11 .    ? -32.175 17.379  91.199  1.00 34.49 ? 1622 HOH   B O     1 
HETATM 20046 O  O     . HOH   DA 11 .    ? 29.577  31.232  49.952  1.00 39.74 ? 1623 HOH   B O     1 
HETATM 20047 O  O     . HOH   DA 11 .    ? 30.934  15.002  64.519  1.00 40.32 ? 1624 HOH   B O     1 
HETATM 20048 O  O     . HOH   DA 11 .    ? 23.239  65.193  82.007  1.00 34.48 ? 1625 HOH   B O     1 
HETATM 20049 O  O     . HOH   DA 11 .    ? 13.363  10.457  91.202  1.00 22.03 ? 1626 HOH   B O     1 
HETATM 20050 O  O     . HOH   DA 11 .    ? 31.157  28.949  77.399  1.00 25.90 ? 1627 HOH   B O     1 
HETATM 20051 O  O     . HOH   DA 11 .    ? 22.732  48.596  77.861  1.00 18.61 ? 1628 HOH   B O     1 
HETATM 20052 O  O     . HOH   DA 11 .    ? 0.757   42.284  75.920  1.00 22.39 ? 1629 HOH   B O     1 
HETATM 20053 O  O     . HOH   DA 11 .    ? 17.021  41.083  71.289  1.00 16.14 ? 1630 HOH   B O     1 
HETATM 20054 O  O     . HOH   DA 11 .    ? 1.249   22.318  110.691 1.00 33.75 ? 1631 HOH   B O     1 
HETATM 20055 O  O     . HOH   DA 11 .    ? 9.264   -5.635  108.765 1.00 39.03 ? 1632 HOH   B O     1 
HETATM 20056 O  O     . HOH   DA 11 .    ? 15.263  53.646  81.505  1.00 20.79 ? 1633 HOH   B O     1 
HETATM 20057 O  O     . HOH   DA 11 .    ? 25.443  69.531  81.443  1.00 35.86 ? 1634 HOH   B O     1 
HETATM 20058 O  O     . HOH   DA 11 .    ? 31.472  53.963  67.768  1.00 25.62 ? 1635 HOH   B O     1 
HETATM 20059 O  O     . HOH   DA 11 .    ? 15.248  16.956  87.710  1.00 20.05 ? 1636 HOH   B O     1 
HETATM 20060 O  O     . HOH   DA 11 .    ? -4.782  34.554  56.796  1.00 41.09 ? 1637 HOH   B O     1 
HETATM 20061 O  O     . HOH   DA 11 .    ? 23.236  56.085  98.883  1.00 27.40 ? 1638 HOH   B O     1 
HETATM 20062 O  O     . HOH   DA 11 .    ? -5.656  55.281  78.420  1.00 23.61 ? 1639 HOH   B O     1 
HETATM 20063 O  O     . HOH   DA 11 .    ? 1.432   13.674  104.508 1.00 16.99 ? 1640 HOH   B O     1 
HETATM 20064 O  O     . HOH   DA 11 .    ? 19.523  5.509   76.752  1.00 28.65 ? 1641 HOH   B O     1 
HETATM 20065 O  O     . HOH   DA 11 .    ? 5.005   36.105  48.840  1.00 33.14 ? 1642 HOH   B O     1 
HETATM 20066 O  O     . HOH   DA 11 .    ? 4.653   49.388  68.390  1.00 21.33 ? 1643 HOH   B O     1 
HETATM 20067 O  O     . HOH   DA 11 .    ? 6.166   5.879   85.852  1.00 20.90 ? 1644 HOH   B O     1 
HETATM 20068 O  O     . HOH   DA 11 .    ? 13.428  58.326  64.423  1.00 24.45 ? 1645 HOH   B O     1 
HETATM 20069 O  O     . HOH   DA 11 .    ? 4.688   30.695  54.529  1.00 31.61 ? 1646 HOH   B O     1 
HETATM 20070 O  O     . HOH   DA 11 .    ? 38.331  32.794  83.641  1.00 29.38 ? 1647 HOH   B O     1 
HETATM 20071 O  O     . HOH   DA 11 .    ? 2.082   20.382  92.257  1.00 32.71 ? 1648 HOH   B O     1 
HETATM 20072 O  O     . HOH   DA 11 .    ? 6.219   19.796  93.773  1.00 38.65 ? 1649 HOH   B O     1 
HETATM 20073 O  O     . HOH   DA 11 .    ? 15.535  7.202   107.999 1.00 32.39 ? 1650 HOH   B O     1 
HETATM 20074 O  O     . HOH   DA 11 .    ? 10.206  24.727  103.360 1.00 27.62 ? 1651 HOH   B O     1 
HETATM 20075 O  O     . HOH   DA 11 .    ? -13.729 18.189  105.397 1.00 23.34 ? 1652 HOH   B O     1 
HETATM 20076 O  O     . HOH   DA 11 .    ? 13.751  3.578   84.338  1.00 38.93 ? 1653 HOH   B O     1 
HETATM 20077 O  O     . HOH   DA 11 .    ? -3.503  10.795  84.226  1.00 23.27 ? 1654 HOH   B O     1 
HETATM 20078 O  O     . HOH   DA 11 .    ? 14.188  33.732  83.767  1.00 21.40 ? 1655 HOH   B O     1 
HETATM 20079 O  O     . HOH   DA 11 .    ? 0.851   28.899  82.830  1.00 14.54 ? 1656 HOH   B O     1 
HETATM 20080 O  O     . HOH   DA 11 .    ? 9.892   50.682  89.866  1.00 25.76 ? 1657 HOH   B O     1 
HETATM 20081 O  O     . HOH   DA 11 .    ? -0.408  56.145  86.099  1.00 32.56 ? 1658 HOH   B O     1 
HETATM 20082 O  O     . HOH   DA 11 .    ? 26.521  22.079  75.124  1.00 19.25 ? 1659 HOH   B O     1 
HETATM 20083 O  O     . HOH   DA 11 .    ? 24.023  68.865  67.192  1.00 21.85 ? 1660 HOH   B O     1 
HETATM 20084 O  O     . HOH   DA 11 .    ? 32.381  33.197  70.541  1.00 25.61 ? 1661 HOH   B O     1 
HETATM 20085 O  O     . HOH   DA 11 .    ? -8.127  27.179  99.625  1.00 27.74 ? 1662 HOH   B O     1 
HETATM 20086 O  O     . HOH   DA 11 .    ? -2.173  35.787  100.568 1.00 31.96 ? 1663 HOH   B O     1 
HETATM 20087 O  O     . HOH   DA 11 .    ? -6.486  0.474   86.010  1.00 26.24 ? 1664 HOH   B O     1 
HETATM 20088 O  O     . HOH   DA 11 .    ? 19.804  24.457  46.128  1.00 21.12 ? 1665 HOH   B O     1 
HETATM 20089 O  O     . HOH   DA 11 .    ? 22.733  9.634   69.570  1.00 39.54 ? 1666 HOH   B O     1 
HETATM 20090 O  O     . HOH   DA 11 .    ? -8.998  24.083  100.615 1.00 18.56 ? 1667 HOH   B O     1 
HETATM 20091 O  O     . HOH   DA 11 .    ? 6.622   77.562  64.013  1.00 35.75 ? 1668 HOH   B O     1 
HETATM 20092 O  O     . HOH   DA 11 .    ? 10.754  38.460  95.577  1.00 25.63 ? 1669 HOH   B O     1 
HETATM 20093 O  O     . HOH   DA 11 .    ? 31.507  60.147  65.214  1.00 25.70 ? 1670 HOH   B O     1 
HETATM 20094 O  O     . HOH   DA 11 .    ? 12.988  51.241  86.249  1.00 27.83 ? 1671 HOH   B O     1 
HETATM 20095 O  O     . HOH   DA 11 .    ? 4.334   44.233  136.957 1.00 43.03 ? 1672 HOH   B O     1 
HETATM 20096 O  O     . HOH   DA 11 .    ? 1.669   10.037  78.926  1.00 28.29 ? 1673 HOH   B O     1 
HETATM 20097 O  O     . HOH   DA 11 .    ? 1.163   15.134  115.864 1.00 21.31 ? 1674 HOH   B O     1 
HETATM 20098 O  O     . HOH   DA 11 .    ? 36.228  20.732  89.860  1.00 39.19 ? 1675 HOH   B O     1 
HETATM 20099 O  O     . HOH   DA 11 .    ? 14.109  25.807  110.500 1.00 33.30 ? 1676 HOH   B O     1 
HETATM 20100 O  O     . HOH   DA 11 .    ? 21.387  30.290  71.287  1.00 13.51 ? 1677 HOH   B O     1 
HETATM 20101 O  O     . HOH   DA 11 .    ? 3.113   33.046  108.497 1.00 42.48 ? 1678 HOH   B O     1 
HETATM 20102 O  O     . HOH   DA 11 .    ? 31.543  59.276  71.940  1.00 22.88 ? 1679 HOH   B O     1 
HETATM 20103 O  O     . HOH   DA 11 .    ? 16.931  42.983  79.146  1.00 14.40 ? 1680 HOH   B O     1 
HETATM 20104 O  O     . HOH   DA 11 .    ? 11.531  37.440  72.069  1.00 13.86 ? 1681 HOH   B O     1 
HETATM 20105 O  O     . HOH   DA 11 .    ? 2.465   39.572  98.487  1.00 20.66 ? 1682 HOH   B O     1 
HETATM 20106 O  O     . HOH   DA 11 .    ? 20.722  37.590  112.225 1.00 20.94 ? 1683 HOH   B O     1 
HETATM 20107 O  O     . HOH   DA 11 .    ? 17.224  49.043  58.759  1.00 20.32 ? 1684 HOH   B O     1 
HETATM 20108 O  O     . HOH   DA 11 .    ? -1.436  38.299  79.920  1.00 22.07 ? 1685 HOH   B O     1 
HETATM 20109 O  O     . HOH   DA 11 .    ? -11.944 18.330  126.334 1.00 26.83 ? 1686 HOH   B O     1 
HETATM 20110 O  O     . HOH   DA 11 .    ? -7.367  15.751  81.515  1.00 32.26 ? 1687 HOH   B O     1 
HETATM 20111 O  O     . HOH   DA 11 .    ? -11.156 20.293  122.507 1.00 29.27 ? 1688 HOH   B O     1 
HETATM 20112 O  O     . HOH   DA 11 .    ? 18.022  52.674  66.458  1.00 21.64 ? 1689 HOH   B O     1 
HETATM 20113 O  O     . HOH   DA 11 .    ? -5.364  39.963  72.075  1.00 26.17 ? 1690 HOH   B O     1 
HETATM 20114 O  O     . HOH   DA 11 .    ? 7.698   41.099  122.488 1.00 40.81 ? 1691 HOH   B O     1 
HETATM 20115 O  O     . HOH   DA 11 .    ? 30.917  38.077  77.218  1.00 35.54 ? 1692 HOH   B O     1 
HETATM 20116 O  O     . HOH   DA 11 .    ? -0.241  4.438   88.283  1.00 21.97 ? 1693 HOH   B O     1 
HETATM 20117 O  O     . HOH   DA 11 .    ? 19.021  70.577  58.929  1.00 32.44 ? 1694 HOH   B O     1 
HETATM 20118 O  O     . HOH   DA 11 .    ? -18.438 8.259   121.858 1.00 31.94 ? 1695 HOH   B O     1 
HETATM 20119 O  O     . HOH   DA 11 .    ? 32.225  9.080   74.653  1.00 38.61 ? 1696 HOH   B O     1 
HETATM 20120 O  O     . HOH   DA 11 .    ? 1.398   6.302   91.557  1.00 19.49 ? 1697 HOH   B O     1 
HETATM 20121 O  O     . HOH   DA 11 .    ? 22.674  67.422  64.370  1.00 23.33 ? 1698 HOH   B O     1 
HETATM 20122 O  O     . HOH   DA 11 .    ? 11.628  16.594  67.513  1.00 30.80 ? 1699 HOH   B O     1 
HETATM 20123 O  O     . HOH   DA 11 .    ? 37.401  23.898  84.633  1.00 35.25 ? 1700 HOH   B O     1 
HETATM 20124 O  O     . HOH   DA 11 .    ? -11.094 27.399  110.518 1.00 36.01 ? 1701 HOH   B O     1 
HETATM 20125 O  O     . HOH   DA 11 .    ? 28.332  37.265  82.581  1.00 29.71 ? 1702 HOH   B O     1 
HETATM 20126 O  O     . HOH   DA 11 .    ? 19.944  43.599  87.558  1.00 13.06 ? 1703 HOH   B O     1 
HETATM 20127 O  O     . HOH   DA 11 .    ? 13.916  72.226  60.831  1.00 27.64 ? 1704 HOH   B O     1 
HETATM 20128 O  O     . HOH   DA 11 .    ? 32.427  47.573  91.922  1.00 33.67 ? 1705 HOH   B O     1 
HETATM 20129 O  O     . HOH   DA 11 .    ? -5.896  -6.329  111.868 1.00 30.88 ? 1706 HOH   B O     1 
HETATM 20130 O  O     . HOH   DA 11 .    ? 3.794   29.706  84.478  1.00 20.70 ? 1707 HOH   B O     1 
HETATM 20131 O  O     . HOH   DA 11 .    ? 3.489   33.722  92.722  1.00 19.54 ? 1708 HOH   B O     1 
HETATM 20132 O  O     . HOH   DA 11 .    ? 18.337  9.350   92.053  1.00 35.20 ? 1709 HOH   B O     1 
HETATM 20133 O  O     . HOH   DA 11 .    ? -1.541  32.759  68.955  1.00 14.13 ? 1710 HOH   B O     1 
HETATM 20134 O  O     . HOH   DA 11 .    ? 25.237  54.929  61.919  1.00 21.37 ? 1711 HOH   B O     1 
HETATM 20135 O  O     . HOH   DA 11 .    ? 29.301  32.320  76.249  1.00 22.84 ? 1712 HOH   B O     1 
HETATM 20136 O  O     . HOH   DA 11 .    ? -0.669  24.116  74.080  1.00 18.69 ? 1713 HOH   B O     1 
HETATM 20137 O  O     . HOH   DA 11 .    ? -14.230 -7.784  103.060 1.00 34.41 ? 1714 HOH   B O     1 
HETATM 20138 O  O     . HOH   DA 11 .    ? -2.074  11.302  101.114 1.00 16.91 ? 1715 HOH   B O     1 
HETATM 20139 O  O     . HOH   DA 11 .    ? 2.448   53.736  69.268  1.00 28.69 ? 1716 HOH   B O     1 
HETATM 20140 O  O     . HOH   DA 11 .    ? -4.444  -0.190  110.343 1.00 23.89 ? 1717 HOH   B O     1 
HETATM 20141 O  O     . HOH   DA 11 .    ? -24.343 23.957  104.076 1.00 39.73 ? 1718 HOH   B O     1 
HETATM 20142 O  O     . HOH   DA 11 .    ? -2.806  62.864  85.301  1.00 24.96 ? 1719 HOH   B O     1 
HETATM 20143 O  O     . HOH   DA 11 .    ? 15.154  4.042   98.272  1.00 29.97 ? 1720 HOH   B O     1 
HETATM 20144 O  O     . HOH   DA 11 .    ? 33.755  18.563  70.822  1.00 38.43 ? 1721 HOH   B O     1 
HETATM 20145 O  O     . HOH   DA 11 .    ? 17.694  23.922  110.270 1.00 22.71 ? 1722 HOH   B O     1 
HETATM 20146 O  O     . HOH   DA 11 .    ? 31.557  30.341  74.231  1.00 36.23 ? 1723 HOH   B O     1 
HETATM 20147 O  O     . HOH   DA 11 .    ? 15.721  52.951  57.723  1.00 31.14 ? 1724 HOH   B O     1 
HETATM 20148 O  O     . HOH   DA 11 .    ? 18.637  45.156  53.550  1.00 25.64 ? 1725 HOH   B O     1 
HETATM 20149 O  O     . HOH   DA 11 .    ? 12.292  2.173   111.132 1.00 29.26 ? 1726 HOH   B O     1 
HETATM 20150 O  O     . HOH   DA 11 .    ? 28.839  22.896  76.318  1.00 19.39 ? 1727 HOH   B O     1 
HETATM 20151 O  O     . HOH   DA 11 .    ? 29.993  35.491  50.566  1.00 30.83 ? 1728 HOH   B O     1 
HETATM 20152 O  O     . HOH   DA 11 .    ? -0.106  28.162  122.083 1.00 39.51 ? 1729 HOH   B O     1 
HETATM 20153 O  O     . HOH   DA 11 .    ? -25.765 7.390   98.370  1.00 34.99 ? 1730 HOH   B O     1 
HETATM 20154 O  O     . HOH   DA 11 .    ? 30.000  50.162  71.270  1.00 27.62 ? 1731 HOH   B O     1 
HETATM 20155 O  O     . HOH   DA 11 .    ? 27.004  32.944  104.561 1.00 34.01 ? 1732 HOH   B O     1 
HETATM 20156 O  O     . HOH   DA 11 .    ? -5.396  9.943   114.739 1.00 24.11 ? 1733 HOH   B O     1 
HETATM 20157 O  O     . HOH   DA 11 .    ? 31.004  21.444  79.718  1.00 18.85 ? 1734 HOH   B O     1 
HETATM 20158 O  O     . HOH   DA 11 .    ? 3.475   -3.499  92.623  1.00 35.06 ? 1735 HOH   B O     1 
HETATM 20159 O  O     . HOH   DA 11 .    ? 4.805   62.921  83.973  1.00 19.41 ? 1736 HOH   B O     1 
HETATM 20160 O  O     . HOH   DA 11 .    ? 18.160  43.841  91.259  1.00 13.35 ? 1737 HOH   B O     1 
HETATM 20161 O  O     . HOH   DA 11 .    ? 15.573  55.664  92.611  1.00 29.50 ? 1738 HOH   B O     1 
HETATM 20162 O  O     . HOH   DA 11 .    ? 20.531  27.760  71.117  1.00 15.07 ? 1739 HOH   B O     1 
HETATM 20163 O  O     . HOH   DA 11 .    ? -2.482  24.261  76.323  1.00 22.78 ? 1740 HOH   B O     1 
HETATM 20164 O  O     . HOH   DA 11 .    ? -9.489  19.332  80.753  1.00 34.08 ? 1741 HOH   B O     1 
HETATM 20165 O  O     . HOH   DA 11 .    ? -2.398  42.906  58.011  1.00 26.72 ? 1742 HOH   B O     1 
HETATM 20166 O  O     . HOH   DA 11 .    ? 2.136   41.595  53.928  1.00 26.45 ? 1743 HOH   B O     1 
HETATM 20167 O  O     . HOH   DA 11 .    ? 12.677  50.098  64.805  1.00 21.95 ? 1744 HOH   B O     1 
HETATM 20168 O  O     . HOH   DA 11 .    ? -7.873  30.002  75.720  1.00 21.94 ? 1745 HOH   B O     1 
HETATM 20169 O  O     . HOH   DA 11 .    ? 23.309  52.660  70.367  1.00 27.68 ? 1746 HOH   B O     1 
HETATM 20170 O  O     . HOH   DA 11 .    ? 29.441  60.355  58.802  1.00 26.54 ? 1747 HOH   B O     1 
HETATM 20171 O  O     . HOH   DA 11 .    ? 30.538  40.359  57.178  1.00 23.64 ? 1748 HOH   B O     1 
HETATM 20172 O  O     . HOH   DA 11 .    ? 0.828   55.643  110.277 1.00 27.05 ? 1749 HOH   B O     1 
HETATM 20173 O  O     . HOH   DA 11 .    ? 4.386   77.652  79.967  1.00 27.86 ? 1750 HOH   B O     1 
HETATM 20174 O  O     . HOH   DA 11 .    ? 27.205  38.139  89.705  1.00 17.80 ? 1751 HOH   B O     1 
HETATM 20175 O  O     . HOH   DA 11 .    ? 7.426   45.077  74.876  1.00 13.51 ? 1752 HOH   B O     1 
HETATM 20176 O  O     . HOH   DA 11 .    ? -15.221 18.850  79.924  1.00 33.83 ? 1753 HOH   B O     1 
HETATM 20177 O  O     . HOH   DA 11 .    ? 3.927   19.809  96.913  1.00 36.35 ? 1754 HOH   B O     1 
HETATM 20178 O  O     . HOH   DA 11 .    ? 22.634  37.407  85.788  1.00 14.62 ? 1755 HOH   B O     1 
HETATM 20179 O  O     . HOH   DA 11 .    ? -0.022  12.495  93.546  1.00 15.98 ? 1756 HOH   B O     1 
HETATM 20180 O  O     . HOH   DA 11 .    ? 5.552   55.811  104.442 1.00 22.92 ? 1757 HOH   B O     1 
HETATM 20181 O  O     . HOH   DA 11 .    ? 8.534   23.444  84.530  1.00 30.67 ? 1758 HOH   B O     1 
HETATM 20182 O  O     . HOH   DA 11 .    ? 15.501  38.369  74.346  1.00 14.07 ? 1759 HOH   B O     1 
HETATM 20183 O  O     . HOH   DA 11 .    ? 27.771  67.610  67.972  1.00 26.48 ? 1760 HOH   B O     1 
HETATM 20184 O  O     . HOH   DA 11 .    ? 5.297   69.487  62.962  1.00 34.96 ? 1761 HOH   B O     1 
HETATM 20185 O  O     . HOH   DA 11 .    ? 1.531   65.802  65.480  1.00 36.55 ? 1762 HOH   B O     1 
HETATM 20186 O  O     . HOH   DA 11 .    ? 7.719   74.485  61.820  1.00 36.90 ? 1763 HOH   B O     1 
HETATM 20187 O  O     . HOH   DA 11 .    ? 22.844  54.395  53.496  1.00 35.36 ? 1764 HOH   B O     1 
HETATM 20188 O  O     . HOH   DA 11 .    ? -29.864 18.478  103.388 1.00 30.13 ? 1765 HOH   B O     1 
HETATM 20189 O  O     . HOH   DA 11 .    ? 11.701  12.104  121.117 1.00 27.17 ? 1766 HOH   B O     1 
HETATM 20190 O  O     . HOH   DA 11 .    ? -18.157 2.135   95.275  1.00 42.51 ? 1767 HOH   B O     1 
HETATM 20191 O  O     . HOH   DA 11 .    ? 8.060   13.921  71.529  1.00 23.10 ? 1768 HOH   B O     1 
HETATM 20192 O  O     . HOH   DA 11 .    ? 25.765  8.769   78.701  1.00 34.65 ? 1769 HOH   B O     1 
HETATM 20193 O  O     . HOH   DA 11 .    ? 7.773   56.817  87.218  1.00 30.08 ? 1770 HOH   B O     1 
HETATM 20194 O  O     . HOH   DA 11 .    ? 24.033  21.834  97.139  1.00 26.79 ? 1771 HOH   B O     1 
HETATM 20195 O  O     . HOH   DA 11 .    ? 22.198  12.266  71.325  1.00 24.36 ? 1772 HOH   B O     1 
HETATM 20196 O  O     . HOH   DA 11 .    ? 6.891   42.741  49.483  1.00 26.03 ? 1773 HOH   B O     1 
HETATM 20197 O  O     . HOH   DA 11 .    ? -7.877  35.864  80.448  1.00 35.86 ? 1774 HOH   B O     1 
HETATM 20198 O  O     . HOH   DA 11 .    ? -11.220 2.026   121.352 1.00 25.14 ? 1775 HOH   B O     1 
HETATM 20199 O  O     . HOH   DA 11 .    ? 0.833   30.950  74.599  1.00 15.98 ? 1776 HOH   B O     1 
HETATM 20200 O  O     . HOH   DA 11 .    ? 20.543  22.801  86.195  1.00 31.76 ? 1777 HOH   B O     1 
HETATM 20201 O  O     . HOH   DA 11 .    ? 27.896  29.727  82.925  1.00 16.40 ? 1778 HOH   B O     1 
HETATM 20202 O  O     . HOH   DA 11 .    ? 3.465   -4.364  97.871  1.00 40.00 ? 1779 HOH   B O     1 
HETATM 20203 O  O     . HOH   DA 11 .    ? -2.225  2.771   125.610 1.00 24.78 ? 1780 HOH   B O     1 
HETATM 20204 O  O     . HOH   DA 11 .    ? -4.864  50.553  78.311  1.00 26.86 ? 1781 HOH   B O     1 
HETATM 20205 O  O     . HOH   DA 11 .    ? 11.523  34.596  51.842  1.00 28.54 ? 1782 HOH   B O     1 
HETATM 20206 O  O     . HOH   DA 11 .    ? 29.836  20.464  76.604  1.00 28.41 ? 1783 HOH   B O     1 
HETATM 20207 O  O     . HOH   DA 11 .    ? -11.930 27.655  101.961 1.00 36.64 ? 1784 HOH   B O     1 
HETATM 20208 O  O     . HOH   DA 11 .    ? 12.420  37.396  107.634 1.00 22.18 ? 1785 HOH   B O     1 
HETATM 20209 O  O     . HOH   DA 11 .    ? 1.623   20.761  89.468  1.00 19.80 ? 1786 HOH   B O     1 
HETATM 20210 O  O     . HOH   DA 11 .    ? 33.155  26.453  58.975  1.00 22.96 ? 1787 HOH   B O     1 
HETATM 20211 O  O     . HOH   DA 11 .    ? 11.915  21.091  58.770  1.00 18.49 ? 1788 HOH   B O     1 
HETATM 20212 O  O     . HOH   DA 11 .    ? 5.376   7.366   94.069  1.00 21.21 ? 1789 HOH   B O     1 
HETATM 20213 O  O     . HOH   DA 11 .    ? 31.181  52.547  65.341  1.00 28.63 ? 1790 HOH   B O     1 
HETATM 20214 O  O     . HOH   DA 11 .    ? 18.545  34.536  46.003  1.00 35.23 ? 1791 HOH   B O     1 
HETATM 20215 O  O     . HOH   DA 11 .    ? -17.022 5.098   116.291 1.00 26.82 ? 1792 HOH   B O     1 
HETATM 20216 O  O     . HOH   DA 11 .    ? 32.773  46.091  67.050  1.00 29.19 ? 1793 HOH   B O     1 
HETATM 20217 O  O     . HOH   DA 11 .    ? 11.107  41.468  54.300  1.00 17.72 ? 1794 HOH   B O     1 
HETATM 20218 O  O     . HOH   DA 11 .    ? -10.474 31.946  80.086  1.00 29.10 ? 1795 HOH   B O     1 
HETATM 20219 O  O     . HOH   DA 11 .    ? 12.971  55.869  65.499  1.00 26.94 ? 1796 HOH   B O     1 
HETATM 20220 O  O     . HOH   DA 11 .    ? 26.827  52.739  75.179  1.00 25.76 ? 1797 HOH   B O     1 
HETATM 20221 O  O     . HOH   DA 11 .    ? 8.997   61.968  84.968  1.00 24.88 ? 1798 HOH   B O     1 
HETATM 20222 O  O     . HOH   DA 11 .    ? 10.694  53.044  104.417 1.00 30.30 ? 1799 HOH   B O     1 
HETATM 20223 O  O     . HOH   DA 11 .    ? -13.733 11.988  91.030  1.00 18.60 ? 1800 HOH   B O     1 
HETATM 20224 O  O     . HOH   DA 11 .    ? 2.616   6.100   80.118  1.00 27.06 ? 1801 HOH   B O     1 
HETATM 20225 O  O     . HOH   DA 11 .    ? 32.795  28.614  52.916  1.00 33.08 ? 1802 HOH   B O     1 
HETATM 20226 O  O     . HOH   DA 11 .    ? -19.065 24.151  114.837 1.00 29.43 ? 1803 HOH   B O     1 
HETATM 20227 O  O     . HOH   DA 11 .    ? 33.669  37.807  61.862  1.00 26.07 ? 1804 HOH   B O     1 
HETATM 20228 O  O     . HOH   DA 11 .    ? -4.744  10.977  100.196 1.00 17.23 ? 1805 HOH   B O     1 
HETATM 20229 O  O     . HOH   DA 11 .    ? 11.836  49.755  88.272  1.00 19.06 ? 1806 HOH   B O     1 
HETATM 20230 O  O     . HOH   DA 11 .    ? 2.552   11.797  94.230  1.00 17.97 ? 1807 HOH   B O     1 
HETATM 20231 O  O     . HOH   DA 11 .    ? 18.941  8.399   83.867  1.00 25.06 ? 1808 HOH   B O     1 
HETATM 20232 O  O     . HOH   DA 11 .    ? 1.402   15.274  82.148  1.00 19.78 ? 1809 HOH   B O     1 
HETATM 20233 O  O     . HOH   DA 11 .    ? 28.106  13.473  85.723  1.00 25.60 ? 1810 HOH   B O     1 
HETATM 20234 O  O     . HOH   DA 11 .    ? 36.896  28.234  92.856  1.00 30.00 ? 1811 HOH   B O     1 
HETATM 20235 O  O     . HOH   DA 11 .    ? 14.350  45.747  78.112  1.00 16.67 ? 1812 HOH   B O     1 
HETATM 20236 O  O     . HOH   DA 11 .    ? -17.235 16.291  130.953 1.00 40.89 ? 1813 HOH   B O     1 
HETATM 20237 O  O     . HOH   DA 11 .    ? -10.191 32.458  88.912  1.00 22.03 ? 1814 HOH   B O     1 
HETATM 20238 O  O     . HOH   DA 11 .    ? 19.114  79.275  68.306  1.00 29.21 ? 1815 HOH   B O     1 
HETATM 20239 O  O     . HOH   DA 11 .    ? 27.534  31.956  73.681  1.00 20.55 ? 1816 HOH   B O     1 
HETATM 20240 O  O     . HOH   DA 11 .    ? 8.373   14.979  90.222  1.00 22.37 ? 1817 HOH   B O     1 
HETATM 20241 O  O     . HOH   DA 11 .    ? -10.942 12.215  79.443  1.00 42.55 ? 1818 HOH   B O     1 
HETATM 20242 O  O     . HOH   DA 11 .    ? 15.110  54.144  66.334  1.00 25.27 ? 1819 HOH   B O     1 
HETATM 20243 O  O     . HOH   DA 11 .    ? -6.310  12.846  99.043  1.00 15.74 ? 1820 HOH   B O     1 
HETATM 20244 O  O     . HOH   DA 11 .    ? -14.835 6.300   117.373 1.00 26.10 ? 1821 HOH   B O     1 
HETATM 20245 O  O     . HOH   DA 11 .    ? 21.604  53.341  66.930  1.00 22.83 ? 1822 HOH   B O     1 
HETATM 20246 O  O     . HOH   DA 11 .    ? 32.930  58.074  73.946  1.00 28.99 ? 1823 HOH   B O     1 
HETATM 20247 O  O     . HOH   DA 11 .    ? 10.723  9.341   69.740  1.00 29.26 ? 1824 HOH   B O     1 
HETATM 20248 O  O     . HOH   DA 11 .    ? -1.057  -8.759  101.841 1.00 27.69 ? 1825 HOH   B O     1 
HETATM 20249 O  O     . HOH   DA 11 .    ? 8.523   35.801  102.432 1.00 24.37 ? 1826 HOH   B O     1 
HETATM 20250 O  O     . HOH   DA 11 .    ? 18.626  50.465  69.941  1.00 24.18 ? 1827 HOH   B O     1 
HETATM 20251 O  O     . HOH   DA 11 .    ? -1.520  67.248  75.158  1.00 26.42 ? 1828 HOH   B O     1 
HETATM 20252 O  O     . HOH   DA 11 .    ? 9.039   4.097   80.802  1.00 24.68 ? 1829 HOH   B O     1 
HETATM 20253 O  O     . HOH   DA 11 .    ? 11.751  45.445  108.906 1.00 35.22 ? 1830 HOH   B O     1 
HETATM 20254 O  O     . HOH   DA 11 .    ? 18.441  13.634  74.301  1.00 22.88 ? 1831 HOH   B O     1 
HETATM 20255 O  O     . HOH   DA 11 .    ? 18.487  66.224  55.610  1.00 33.20 ? 1832 HOH   B O     1 
HETATM 20256 O  O     . HOH   DA 11 .    ? -2.746  60.108  119.827 1.00 27.91 ? 1833 HOH   B O     1 
HETATM 20257 O  O     . HOH   DA 11 .    ? 25.965  47.437  99.870  1.00 29.47 ? 1834 HOH   B O     1 
HETATM 20258 O  O     . HOH   DA 11 .    ? 15.299  62.129  84.333  1.00 37.06 ? 1835 HOH   B O     1 
HETATM 20259 O  O     . HOH   DA 11 .    ? -2.678  21.527  91.455  1.00 16.47 ? 1836 HOH   B O     1 
HETATM 20260 O  O     . HOH   DA 11 .    ? 14.480  22.646  101.538 1.00 20.35 ? 1837 HOH   B O     1 
HETATM 20261 O  O     . HOH   DA 11 .    ? 22.673  23.796  84.572  1.00 17.99 ? 1838 HOH   B O     1 
HETATM 20262 O  O     . HOH   DA 11 .    ? -2.552  14.574  80.972  1.00 41.82 ? 1839 HOH   B O     1 
HETATM 20263 O  O     . HOH   DA 11 .    ? -13.675 12.668  93.680  1.00 18.03 ? 1840 HOH   B O     1 
HETATM 20264 O  O     . HOH   DA 11 .    ? 5.713   15.293  94.528  1.00 17.32 ? 1841 HOH   B O     1 
HETATM 20265 O  O     . HOH   DA 11 .    ? -6.845  6.569   118.333 1.00 21.49 ? 1842 HOH   B O     1 
HETATM 20266 O  O     . HOH   DA 11 .    ? 0.239   20.343  69.770  1.00 23.87 ? 1843 HOH   B O     1 
HETATM 20267 O  O     . HOH   DA 11 .    ? 15.423  10.175  89.318  1.00 19.13 ? 1844 HOH   B O     1 
HETATM 20268 O  O     . HOH   DA 11 .    ? -4.845  37.361  98.320  1.00 34.18 ? 1845 HOH   B O     1 
HETATM 20269 O  O     . HOH   DA 11 .    ? 37.332  31.272  81.432  1.00 26.50 ? 1846 HOH   B O     1 
HETATM 20270 O  O     . HOH   DA 11 .    ? 17.182  28.706  110.591 1.00 24.47 ? 1847 HOH   B O     1 
HETATM 20271 O  O     . HOH   DA 11 .    ? 25.127  13.961  64.940  1.00 29.52 ? 1848 HOH   B O     1 
HETATM 20272 O  O     . HOH   DA 11 .    ? -3.124  -2.186  94.443  1.00 25.52 ? 1849 HOH   B O     1 
HETATM 20273 O  O     . HOH   DA 11 .    ? -6.818  14.394  91.298  1.00 17.36 ? 1850 HOH   B O     1 
HETATM 20274 O  O     . HOH   DA 11 .    ? 23.133  12.621  67.964  1.00 23.06 ? 1851 HOH   B O     1 
HETATM 20275 O  O     . HOH   DA 11 .    ? -3.081  31.090  63.397  1.00 24.96 ? 1852 HOH   B O     1 
HETATM 20276 O  O     . HOH   DA 11 .    ? -7.178  34.888  128.800 1.00 39.11 ? 1853 HOH   B O     1 
HETATM 20277 O  O     . HOH   DA 11 .    ? 23.217  52.070  62.271  1.00 20.27 ? 1854 HOH   B O     1 
HETATM 20278 O  O     . HOH   DA 11 .    ? -8.106  12.580  96.893  1.00 18.03 ? 1855 HOH   B O     1 
HETATM 20279 O  O     . HOH   DA 11 .    ? 19.402  54.824  93.323  1.00 23.73 ? 1856 HOH   B O     1 
HETATM 20280 O  O     . HOH   DA 11 .    ? 19.545  19.312  66.188  1.00 14.67 ? 1857 HOH   B O     1 
HETATM 20281 O  O     . HOH   DA 11 .    ? -0.420  75.643  67.861  1.00 31.47 ? 1858 HOH   B O     1 
HETATM 20282 O  O     . HOH   DA 11 .    ? 0.194   27.052  94.570  1.00 20.02 ? 1859 HOH   B O     1 
HETATM 20283 O  O     . HOH   DA 11 .    ? 3.281   41.128  116.965 1.00 27.10 ? 1860 HOH   B O     1 
HETATM 20284 O  O     . HOH   DA 11 .    ? 15.856  48.588  70.554  1.00 14.06 ? 1861 HOH   B O     1 
HETATM 20285 O  O     . HOH   DA 11 .    ? -11.414 20.546  87.969  1.00 21.21 ? 1862 HOH   B O     1 
HETATM 20286 O  O     . HOH   DA 11 .    ? -25.151 10.497  87.331  1.00 30.86 ? 1863 HOH   B O     1 
HETATM 20287 O  O     . HOH   DA 11 .    ? 15.399  26.838  80.951  1.00 28.42 ? 1864 HOH   B O     1 
HETATM 20288 O  O     . HOH   DA 11 .    ? 20.008  50.671  66.922  1.00 24.55 ? 1865 HOH   B O     1 
HETATM 20289 O  O     . HOH   DA 11 .    ? 2.626   70.025  64.010  1.00 32.78 ? 1866 HOH   B O     1 
HETATM 20290 O  O     . HOH   DA 11 .    ? -0.344  40.289  77.578  1.00 23.64 ? 1867 HOH   B O     1 
HETATM 20291 O  O     . HOH   DA 11 .    ? 9.562   43.742  109.911 1.00 25.94 ? 1868 HOH   B O     1 
HETATM 20292 O  O     . HOH   DA 11 .    ? -2.956  54.941  83.400  1.00 30.26 ? 1869 HOH   B O     1 
HETATM 20293 O  O     . HOH   DA 11 .    ? 7.674   65.960  68.357  1.00 29.98 ? 1870 HOH   B O     1 
HETATM 20294 O  O     . HOH   DA 11 .    ? 5.091   3.563   92.843  1.00 22.31 ? 1871 HOH   B O     1 
HETATM 20295 O  O     . HOH   DA 11 .    ? -1.271  60.549  77.211  1.00 20.19 ? 1872 HOH   B O     1 
HETATM 20296 O  O     . HOH   DA 11 .    ? 20.185  52.598  69.122  1.00 19.62 ? 1873 HOH   B O     1 
HETATM 20297 O  O     . HOH   DA 11 .    ? 23.665  26.173  50.441  1.00 25.81 ? 1874 HOH   B O     1 
HETATM 20298 O  O     . HOH   DA 11 .    ? 22.034  24.647  108.275 1.00 25.15 ? 1875 HOH   B O     1 
HETATM 20299 O  O     . HOH   DA 11 .    ? -1.655  31.627  125.291 1.00 40.19 ? 1876 HOH   B O     1 
HETATM 20300 O  O     . HOH   DA 11 .    ? 6.250   -3.993  104.363 1.00 30.82 ? 1877 HOH   B O     1 
HETATM 20301 O  O     . HOH   DA 11 .    ? 1.325   49.376  89.207  1.00 35.05 ? 1878 HOH   B O     1 
HETATM 20302 O  O     . HOH   DA 11 .    ? 11.786  38.192  47.267  1.00 32.14 ? 1879 HOH   B O     1 
HETATM 20303 O  O     . HOH   DA 11 .    ? -23.398 3.509   101.322 1.00 38.10 ? 1880 HOH   B O     1 
HETATM 20304 O  O     . HOH   DA 11 .    ? 39.509  29.663  87.601  1.00 21.72 ? 1881 HOH   B O     1 
HETATM 20305 O  O     . HOH   DA 11 .    ? 9.668   2.507   117.155 1.00 26.90 ? 1882 HOH   B O     1 
HETATM 20306 O  O     . HOH   DA 11 .    ? 20.963  47.664  55.899  1.00 29.95 ? 1883 HOH   B O     1 
HETATM 20307 O  O     . HOH   DA 11 .    ? 26.158  39.858  52.698  1.00 24.75 ? 1884 HOH   B O     1 
HETATM 20308 O  O     . HOH   DA 11 .    ? 13.078  36.917  76.971  1.00 16.95 ? 1885 HOH   B O     1 
HETATM 20309 O  O     . HOH   DA 11 .    ? -6.238  34.531  83.648  1.00 23.06 ? 1886 HOH   B O     1 
HETATM 20310 O  O     . HOH   DA 11 .    ? -8.260  2.628   92.156  1.00 21.52 ? 1887 HOH   B O     1 
HETATM 20311 O  O     . HOH   DA 11 .    ? 26.832  48.992  94.417  1.00 25.54 ? 1888 HOH   B O     1 
HETATM 20312 O  O     . HOH   DA 11 .    ? 19.665  33.144  67.261  1.00 13.53 ? 1889 HOH   B O     1 
HETATM 20313 O  O     . HOH   DA 11 .    ? 23.389  33.101  91.326  1.00 16.66 ? 1890 HOH   B O     1 
HETATM 20314 O  O     . HOH   DA 11 .    ? 4.729   22.088  83.619  1.00 20.88 ? 1891 HOH   B O     1 
HETATM 20315 O  O     . HOH   DA 11 .    ? 16.729  53.064  63.870  1.00 25.11 ? 1892 HOH   B O     1 
HETATM 20316 O  O     . HOH   DA 11 .    ? 12.336  6.204   84.350  1.00 22.12 ? 1893 HOH   B O     1 
HETATM 20317 O  O     . HOH   DA 11 .    ? 26.489  22.646  50.244  1.00 32.38 ? 1894 HOH   B O     1 
HETATM 20318 O  O     . HOH   DA 11 .    ? 10.181  66.631  86.281  1.00 36.20 ? 1895 HOH   B O     1 
HETATM 20319 O  O     . HOH   DA 11 .    ? 2.830   35.540  121.101 1.00 33.07 ? 1896 HOH   B O     1 
HETATM 20320 O  O     . HOH   DA 11 .    ? 8.313   40.786  86.623  1.00 14.19 ? 1897 HOH   B O     1 
HETATM 20321 O  O     . HOH   DA 11 .    ? 0.861   10.614  129.323 1.00 26.30 ? 1898 HOH   B O     1 
HETATM 20322 O  O     . HOH   DA 11 .    ? -4.284  30.862  94.588  1.00 27.05 ? 1899 HOH   B O     1 
HETATM 20323 O  O     . HOH   DA 11 .    ? 3.746   10.660  92.103  1.00 17.08 ? 1900 HOH   B O     1 
HETATM 20324 O  O     . HOH   DA 11 .    ? 12.021  7.984   90.260  1.00 21.72 ? 1901 HOH   B O     1 
HETATM 20325 O  O     . HOH   DA 11 .    ? 25.324  53.892  73.559  1.00 22.20 ? 1902 HOH   B O     1 
HETATM 20326 O  O     . HOH   DA 11 .    ? 29.433  58.252  82.088  1.00 36.58 ? 1903 HOH   B O     1 
HETATM 20327 O  O     . HOH   DA 11 .    ? -9.881  6.240   86.837  1.00 24.61 ? 1904 HOH   B O     1 
HETATM 20328 O  O     . HOH   DA 11 .    ? 27.135  23.120  88.433  1.00 16.85 ? 1905 HOH   B O     1 
HETATM 20329 O  O     . HOH   DA 11 .    ? -11.521 -1.874  96.353  1.00 27.03 ? 1906 HOH   B O     1 
HETATM 20330 O  O     . HOH   DA 11 .    ? 2.615   33.006  78.263  1.00 14.28 ? 1907 HOH   B O     1 
HETATM 20331 O  O     . HOH   DA 11 .    ? -4.560  53.898  130.524 1.00 35.49 ? 1908 HOH   B O     1 
HETATM 20332 O  O     . HOH   DA 11 .    ? -2.812  26.484  60.288  1.00 33.34 ? 1909 HOH   B O     1 
HETATM 20333 O  O     . HOH   DA 11 .    ? -0.554  39.680  131.179 1.00 37.72 ? 1910 HOH   B O     1 
HETATM 20334 O  O     . HOH   DA 11 .    ? -1.325  50.982  64.751  1.00 17.23 ? 1911 HOH   B O     1 
HETATM 20335 O  O     . HOH   DA 11 .    ? -6.123  -7.245  115.495 1.00 34.17 ? 1912 HOH   B O     1 
HETATM 20336 O  O     . HOH   DA 11 .    ? -4.536  55.813  81.461  1.00 28.89 ? 1913 HOH   B O     1 
HETATM 20337 O  O     . HOH   DA 11 .    ? 2.129   29.961  54.588  1.00 34.48 ? 1914 HOH   B O     1 
HETATM 20338 O  O     . HOH   DA 11 .    ? 2.265   63.317  78.164  1.00 16.71 ? 1915 HOH   B O     1 
HETATM 20339 O  O     . HOH   DA 11 .    ? -6.965  35.349  69.021  1.00 32.34 ? 1916 HOH   B O     1 
HETATM 20340 O  O     . HOH   DA 11 .    ? 1.069   9.543   89.423  1.00 20.84 ? 1917 HOH   B O     1 
HETATM 20341 O  O     . HOH   DA 11 .    ? -4.916  37.032  89.583  1.00 30.13 ? 1918 HOH   B O     1 
HETATM 20342 O  O     . HOH   DA 11 .    ? -8.453  -8.680  105.662 1.00 22.75 ? 1919 HOH   B O     1 
HETATM 20343 O  O     . HOH   DA 11 .    ? 6.664   8.153   74.872  1.00 25.37 ? 1920 HOH   B O     1 
HETATM 20344 O  O     . HOH   DA 11 .    ? 22.956  72.861  64.723  1.00 30.37 ? 1921 HOH   B O     1 
HETATM 20345 O  O     . HOH   DA 11 .    ? 25.017  23.757  81.567  1.00 25.81 ? 1922 HOH   B O     1 
HETATM 20346 O  O     . HOH   DA 11 .    ? 4.583   46.726  69.021  1.00 14.04 ? 1923 HOH   B O     1 
HETATM 20347 O  O     . HOH   DA 11 .    ? -0.093  19.591  93.840  1.00 19.01 ? 1924 HOH   B O     1 
HETATM 20348 O  O     . HOH   DA 11 .    ? 6.096   16.331  121.499 1.00 29.50 ? 1925 HOH   B O     1 
HETATM 20349 O  O     . HOH   DA 11 .    ? 10.625  29.503  94.007  1.00 24.58 ? 1926 HOH   B O     1 
HETATM 20350 O  O     . HOH   DA 11 .    ? 7.146   37.939  102.684 1.00 27.04 ? 1927 HOH   B O     1 
HETATM 20351 O  O     . HOH   DA 11 .    ? 35.537  38.883  90.395  1.00 34.58 ? 1928 HOH   B O     1 
HETATM 20352 O  O     . HOH   DA 11 .    ? -3.481  66.275  76.940  1.00 25.22 ? 1929 HOH   B O     1 
HETATM 20353 O  O     . HOH   DA 11 .    ? 1.013   -0.642  92.566  1.00 25.48 ? 1930 HOH   B O     1 
HETATM 20354 O  O     . HOH   DA 11 .    ? 26.924  35.504  90.728  1.00 15.83 ? 1931 HOH   B O     1 
HETATM 20355 O  O     . HOH   DA 11 .    ? -1.141  55.589  72.229  1.00 28.57 ? 1932 HOH   B O     1 
HETATM 20356 O  O     . HOH   DA 11 .    ? 0.095   47.847  76.297  1.00 18.55 ? 1933 HOH   B O     1 
HETATM 20357 O  O     . HOH   DA 11 .    ? -5.074  42.692  72.601  1.00 28.56 ? 1934 HOH   B O     1 
HETATM 20358 O  O     . HOH   DA 11 .    ? -23.169 32.254  116.987 1.00 52.89 ? 1935 HOH   B O     1 
HETATM 20359 O  O     . HOH   DA 11 .    ? -26.996 14.978  100.505 1.00 38.81 ? 1936 HOH   B O     1 
HETATM 20360 O  O     . HOH   DA 11 .    ? 21.890  46.393  76.523  1.00 17.02 ? 1937 HOH   B O     1 
HETATM 20361 O  O     . HOH   DA 11 .    ? 21.352  7.154   83.370  1.00 32.29 ? 1938 HOH   B O     1 
HETATM 20362 O  O     . HOH   DA 11 .    ? 26.116  20.343  52.734  1.00 27.74 ? 1939 HOH   B O     1 
HETATM 20363 O  O     . HOH   DA 11 .    ? 29.759  33.274  73.327  1.00 23.30 ? 1940 HOH   B O     1 
HETATM 20364 O  O     . HOH   DA 11 .    ? -1.763  49.390  101.085 1.00 28.06 ? 1941 HOH   B O     1 
HETATM 20365 O  O     . HOH   DA 11 .    ? 15.822  16.175  85.123  1.00 18.71 ? 1942 HOH   B O     1 
HETATM 20366 O  O     . HOH   DA 11 .    ? 3.879   17.603  75.205  1.00 26.00 ? 1943 HOH   B O     1 
HETATM 20367 O  O     . HOH   DA 11 .    ? -1.358  66.801  83.722  1.00 26.61 ? 1944 HOH   B O     1 
HETATM 20368 O  O     . HOH   DA 11 .    ? 16.954  34.328  55.860  1.00 15.47 ? 1945 HOH   B O     1 
HETATM 20369 O  O     . HOH   DA 11 .    ? -1.183  20.880  89.333  1.00 16.33 ? 1946 HOH   B O     1 
HETATM 20370 O  O     . HOH   DA 11 .    ? 9.780   52.247  107.690 1.00 42.90 ? 1947 HOH   B O     1 
HETATM 20371 O  O     . HOH   DA 11 .    ? -7.264  27.882  74.024  1.00 24.89 ? 1948 HOH   B O     1 
HETATM 20372 O  O     . HOH   DA 11 .    ? 19.991  54.235  81.030  1.00 20.52 ? 1949 HOH   B O     1 
HETATM 20373 O  O     . HOH   DA 11 .    ? 19.389  16.239  63.529  1.00 18.84 ? 1950 HOH   B O     1 
HETATM 20374 O  O     . HOH   DA 11 .    ? -10.758 52.453  128.192 1.00 34.76 ? 1951 HOH   B O     1 
HETATM 20375 O  O     . HOH   DA 11 .    ? -3.152  11.077  103.564 1.00 17.11 ? 1952 HOH   B O     1 
HETATM 20376 O  O     . HOH   DA 11 .    ? -22.472 20.675  88.121  1.00 30.84 ? 1953 HOH   B O     1 
HETATM 20377 O  O     . HOH   DA 11 .    ? 15.970  69.837  55.008  1.00 40.89 ? 1954 HOH   B O     1 
HETATM 20378 O  O     . HOH   DA 11 .    ? 23.218  11.716  89.676  1.00 36.44 ? 1955 HOH   B O     1 
HETATM 20379 O  O     . HOH   DA 11 .    ? 4.506   36.126  103.585 1.00 45.33 ? 1956 HOH   B O     1 
HETATM 20380 O  O     . HOH   DA 11 .    ? 22.378  54.373  92.872  1.00 25.41 ? 1957 HOH   B O     1 
HETATM 20381 O  O     . HOH   DA 11 .    ? 17.762  53.888  82.667  1.00 23.77 ? 1958 HOH   B O     1 
HETATM 20382 O  O     . HOH   DA 11 .    ? 27.080  18.491  61.856  1.00 21.75 ? 1959 HOH   B O     1 
HETATM 20383 O  O     . HOH   DA 11 .    ? 9.220   19.079  103.501 1.00 21.10 ? 1960 HOH   B O     1 
HETATM 20384 O  O     . HOH   DA 11 .    ? 26.997  42.645  104.527 1.00 26.54 ? 1961 HOH   B O     1 
HETATM 20385 O  O     . HOH   DA 11 .    ? 6.725   -8.205  107.162 1.00 35.53 ? 1962 HOH   B O     1 
HETATM 20386 O  O     . HOH   DA 11 .    ? 18.776  30.663  88.342  1.00 17.24 ? 1963 HOH   B O     1 
HETATM 20387 O  O     . HOH   DA 11 .    ? -0.850  55.985  121.465 1.00 33.44 ? 1964 HOH   B O     1 
HETATM 20388 O  O     . HOH   DA 11 .    ? 16.225  21.682  99.590  1.00 20.07 ? 1965 HOH   B O     1 
HETATM 20389 O  O     . HOH   DA 11 .    ? -16.474 25.442  106.686 1.00 32.50 ? 1966 HOH   B O     1 
HETATM 20390 O  O     A HOH   DA 11 .    ? 0.317   63.559  84.379  0.53 22.20 ? 1967 HOH   B O     1 
HETATM 20391 O  O     . HOH   DA 11 .    ? 18.372  66.947  58.247  1.00 29.55 ? 1968 HOH   B O     1 
HETATM 20392 O  O     . HOH   DA 11 .    ? -1.604  5.561   91.989  1.00 19.02 ? 1969 HOH   B O     1 
HETATM 20393 O  O     . HOH   DA 11 .    ? 0.652   -7.780  109.261 1.00 29.79 ? 1970 HOH   B O     1 
HETATM 20394 O  O     . HOH   DA 11 .    ? 10.012  70.363  86.390  1.00 35.57 ? 1971 HOH   B O     1 
HETATM 20395 O  O     . HOH   DA 11 .    ? 6.414   81.927  75.294  1.00 31.77 ? 1972 HOH   B O     1 
HETATM 20396 O  O     . HOH   DA 11 .    ? 41.030  34.676  91.089  1.00 21.94 ? 1973 HOH   B O     1 
HETATM 20397 O  O     . HOH   DA 11 .    ? 26.900  59.244  78.332  1.00 19.21 ? 1974 HOH   B O     1 
HETATM 20398 O  O     . HOH   DA 11 .    ? 12.320  53.918  90.489  1.00 33.14 ? 1975 HOH   B O     1 
HETATM 20399 O  O     . HOH   DA 11 .    ? 14.618  16.842  91.796  1.00 21.06 ? 1976 HOH   B O     1 
HETATM 20400 O  O     . HOH   DA 11 .    ? 18.151  15.110  97.298  1.00 24.79 ? 1977 HOH   B O     1 
HETATM 20401 O  O     . HOH   DA 11 .    ? 29.614  45.947  84.866  1.00 37.02 ? 1978 HOH   B O     1 
HETATM 20402 O  O     . HOH   DA 11 .    ? 28.476  46.570  87.655  1.00 25.15 ? 1979 HOH   B O     1 
HETATM 20403 O  O     . HOH   DA 11 .    ? 1.265   38.886  105.244 1.00 31.04 ? 1980 HOH   B O     1 
HETATM 20404 O  O     . HOH   DA 11 .    ? 5.781   48.196  110.308 1.00 33.02 ? 1981 HOH   B O     1 
HETATM 20405 O  O     . HOH   DA 11 .    ? 5.498   12.026  77.611  1.00 29.03 ? 1982 HOH   B O     1 
HETATM 20406 O  O     . HOH   DA 11 .    ? -28.331 16.720  104.633 1.00 38.98 ? 1983 HOH   B O     1 
HETATM 20407 O  O     . HOH   DA 11 .    ? 16.908  33.922  48.383  1.00 29.38 ? 1984 HOH   B O     1 
HETATM 20408 O  O     . HOH   DA 11 .    ? -1.772  25.570  79.892  1.00 19.82 ? 1985 HOH   B O     1 
HETATM 20409 O  O     . HOH   DA 11 .    ? 24.952  30.163  108.303 1.00 33.63 ? 1986 HOH   B O     1 
HETATM 20410 O  O     . HOH   DA 11 .    ? 18.135  23.555  84.972  1.00 18.03 ? 1987 HOH   B O     1 
HETATM 20411 O  O     . HOH   DA 11 .    ? -15.390 47.294  113.626 1.00 31.22 ? 1988 HOH   B O     1 
HETATM 20412 O  O     . HOH   DA 11 .    ? -5.228  16.443  96.716  1.00 15.70 ? 1989 HOH   B O     1 
HETATM 20413 O  O     . HOH   DA 11 .    ? -9.726  10.538  82.320  1.00 38.00 ? 1990 HOH   B O     1 
HETATM 20414 O  O     . HOH   DA 11 .    ? 25.342  53.996  54.139  1.00 42.33 ? 1991 HOH   B O     1 
HETATM 20415 O  O     . HOH   DA 11 .    ? 29.262  32.526  103.023 1.00 26.45 ? 1992 HOH   B O     1 
HETATM 20416 O  O     . HOH   DA 11 .    ? 24.708  57.543  78.110  1.00 22.11 ? 1993 HOH   B O     1 
HETATM 20417 O  O     . HOH   DA 11 .    ? 30.361  20.378  73.515  1.00 30.15 ? 1994 HOH   B O     1 
HETATM 20418 O  O     . HOH   DA 11 .    ? 22.567  11.961  87.400  1.00 27.84 ? 1995 HOH   B O     1 
HETATM 20419 O  O     . HOH   DA 11 .    ? 1.900   40.446  114.163 1.00 24.94 ? 1996 HOH   B O     1 
HETATM 20420 O  O     . HOH   DA 11 .    ? 32.787  45.377  74.776  1.00 27.07 ? 1997 HOH   B O     1 
HETATM 20421 O  O     . HOH   DA 11 .    ? 43.560  36.938  87.752  1.00 26.09 ? 1998 HOH   B O     1 
HETATM 20422 O  O     . HOH   DA 11 .    ? 15.133  49.006  57.071  1.00 25.23 ? 1999 HOH   B O     1 
HETATM 20423 O  O     . HOH   DA 11 .    ? 7.320   20.717  102.034 1.00 26.47 ? 2000 HOH   B O     1 
HETATM 20424 O  O     . HOH   DA 11 .    ? 11.437  26.324  101.479 1.00 26.16 ? 2001 HOH   B O     1 
HETATM 20425 O  O     . HOH   DA 11 .    ? -5.668  12.691  84.241  1.00 26.19 ? 2002 HOH   B O     1 
HETATM 20426 O  O     . HOH   DA 11 .    ? 4.809   18.020  91.016  1.00 21.56 ? 2003 HOH   B O     1 
HETATM 20427 O  O     . HOH   DA 11 .    ? 14.784  7.085   68.763  1.00 28.21 ? 2004 HOH   B O     1 
HETATM 20428 O  O     . HOH   DA 11 .    ? 0.189   36.581  108.651 1.00 33.55 ? 2005 HOH   B O     1 
HETATM 20429 O  O     . HOH   DA 11 .    ? 5.946   51.961  93.759  1.00 37.64 ? 2006 HOH   B O     1 
HETATM 20430 O  O     . HOH   DA 11 .    ? 13.883  34.692  111.532 1.00 36.98 ? 2007 HOH   B O     1 
HETATM 20431 O  O     . HOH   DA 11 .    ? 4.831   60.477  67.692  1.00 35.87 ? 2008 HOH   B O     1 
HETATM 20432 O  O     . HOH   DA 11 .    ? 10.494  16.426  121.562 1.00 32.11 ? 2009 HOH   B O     1 
HETATM 20433 O  O     . HOH   DA 11 .    ? 12.356  2.290   92.076  1.00 34.86 ? 2010 HOH   B O     1 
HETATM 20434 O  O     . HOH   DA 11 .    ? -32.660 16.415  98.255  1.00 39.93 ? 2011 HOH   B O     1 
HETATM 20435 O  O     . HOH   DA 11 .    ? -14.737 7.399   119.951 1.00 26.45 ? 2012 HOH   B O     1 
HETATM 20436 O  O     . HOH   DA 11 .    ? 23.415  51.910  83.647  1.00 24.46 ? 2013 HOH   B O     1 
HETATM 20437 O  O     . HOH   DA 11 .    ? -5.223  8.797   131.122 1.00 43.11 ? 2014 HOH   B O     1 
HETATM 20438 O  O     . HOH   DA 11 .    ? -5.541  -1.980  116.768 1.00 30.42 ? 2015 HOH   B O     1 
HETATM 20439 O  O     . HOH   DA 11 .    ? -0.454  45.217  77.387  1.00 34.20 ? 2016 HOH   B O     1 
HETATM 20440 O  O     . HOH   DA 11 .    ? 21.209  53.884  83.372  1.00 25.29 ? 2017 HOH   B O     1 
HETATM 20441 O  O     . HOH   DA 11 .    ? 27.708  10.899  84.663  1.00 27.59 ? 2018 HOH   B O     1 
HETATM 20442 O  O     . HOH   DA 11 .    ? -23.886 23.328  84.170  1.00 35.31 ? 2019 HOH   B O     1 
HETATM 20443 O  O     . HOH   DA 11 .    ? 23.765  31.733  110.127 1.00 27.07 ? 2020 HOH   B O     1 
HETATM 20444 O  O     . HOH   DA 11 .    ? -3.095  33.907  62.341  1.00 20.44 ? 2021 HOH   B O     1 
HETATM 20445 O  O     . HOH   DA 11 .    ? -20.569 25.360  94.306  1.00 26.38 ? 2022 HOH   B O     1 
HETATM 20446 O  O     . HOH   DA 11 .    ? 11.686  3.338   73.839  1.00 40.12 ? 2023 HOH   B O     1 
HETATM 20447 O  O     . HOH   DA 11 .    ? 12.512  47.064  79.581  1.00 27.74 ? 2024 HOH   B O     1 
HETATM 20448 O  O     . HOH   DA 11 .    ? 13.043  25.975  95.836  1.00 28.24 ? 2025 HOH   B O     1 
HETATM 20449 O  O     . HOH   DA 11 .    ? 19.852  22.587  74.358  1.00 27.40 ? 2026 HOH   B O     1 
HETATM 20450 O  O     . HOH   DA 11 .    ? 25.397  33.392  109.630 1.00 37.88 ? 2027 HOH   B O     1 
HETATM 20451 O  O     . HOH   DA 11 .    ? -10.737 1.859   91.132  1.00 24.61 ? 2028 HOH   B O     1 
HETATM 20452 O  O     . HOH   DA 11 .    ? 5.087   42.826  70.561  1.00 13.74 ? 2029 HOH   B O     1 
HETATM 20453 O  O     . HOH   DA 11 .    ? 17.824  68.703  84.312  1.00 34.23 ? 2030 HOH   B O     1 
HETATM 20454 O  O     . HOH   DA 11 .    ? -25.000 16.948  81.877  1.00 31.98 ? 2031 HOH   B O     1 
HETATM 20455 O  O     . HOH   DA 11 .    ? -4.634  44.784  108.501 1.00 27.66 ? 2032 HOH   B O     1 
HETATM 20456 O  O     . HOH   DA 11 .    ? 3.796   19.504  60.164  1.00 32.73 ? 2033 HOH   B O     1 
HETATM 20457 O  O     . HOH   DA 11 .    ? 8.788   6.175   84.925  1.00 19.77 ? 2034 HOH   B O     1 
HETATM 20458 O  O     . HOH   DA 11 .    ? 32.858  38.033  104.168 1.00 30.23 ? 2035 HOH   B O     1 
HETATM 20459 O  O     . HOH   DA 11 .    ? 4.569   18.824  123.901 1.00 27.41 ? 2036 HOH   B O     1 
HETATM 20460 O  O     . HOH   DA 11 .    ? 32.715  37.012  82.143  1.00 41.74 ? 2037 HOH   B O     1 
HETATM 20461 O  O     . HOH   DA 11 .    ? 33.181  23.141  64.330  1.00 28.98 ? 2038 HOH   B O     1 
HETATM 20462 O  O     . HOH   DA 11 .    ? 20.276  75.344  62.535  1.00 38.92 ? 2039 HOH   B O     1 
HETATM 20463 O  O     . HOH   DA 11 .    ? -18.350 6.334   95.550  1.00 33.10 ? 2040 HOH   B O     1 
HETATM 20464 O  O     . HOH   DA 11 .    ? -5.734  35.737  87.518  1.00 29.45 ? 2041 HOH   B O     1 
HETATM 20465 O  O     . HOH   DA 11 .    ? -4.480  42.608  108.101 1.00 31.82 ? 2042 HOH   B O     1 
HETATM 20466 O  O     . HOH   DA 11 .    ? 0.276   11.356  80.728  1.00 32.21 ? 2043 HOH   B O     1 
HETATM 20467 O  O     . HOH   DA 11 .    ? -7.940  -0.667  119.658 1.00 27.24 ? 2044 HOH   B O     1 
HETATM 20468 O  O     A HOH   DA 11 .    ? 1.777   60.943  80.675  0.53 19.19 ? 2045 HOH   B O     1 
HETATM 20469 O  O     . HOH   DA 11 .    ? 0.930   80.855  75.414  1.00 40.81 ? 2046 HOH   B O     1 
HETATM 20470 O  O     . HOH   DA 11 .    ? 6.122   12.307  126.333 1.00 20.41 ? 2047 HOH   B O     1 
HETATM 20471 O  O     . HOH   DA 11 .    ? 0.556   0.280   96.009  1.00 24.78 ? 2048 HOH   B O     1 
HETATM 20472 O  O     . HOH   DA 11 .    ? 28.894  24.154  50.942  1.00 29.62 ? 2049 HOH   B O     1 
HETATM 20473 O  O     . HOH   DA 11 .    ? 18.341  53.345  75.723  1.00 17.27 ? 2050 HOH   B O     1 
HETATM 20474 O  O     . HOH   DA 11 .    ? 5.052   76.470  84.659  1.00 40.42 ? 2051 HOH   B O     1 
HETATM 20475 O  O     . HOH   DA 11 .    ? 35.522  20.141  85.315  1.00 35.25 ? 2052 HOH   B O     1 
HETATM 20476 O  O     . HOH   DA 11 .    ? 1.467   46.544  98.688  1.00 25.52 ? 2053 HOH   B O     1 
HETATM 20477 O  O     . HOH   DA 11 .    ? 26.106  27.683  66.972  1.00 16.27 ? 2054 HOH   B O     1 
HETATM 20478 O  O     . HOH   DA 11 .    ? -6.197  41.744  83.825  1.00 32.00 ? 2055 HOH   B O     1 
HETATM 20479 O  O     . HOH   DA 11 .    ? 37.474  29.850  102.243 1.00 38.24 ? 2056 HOH   B O     1 
HETATM 20480 O  O     . HOH   DA 11 .    ? 24.573  51.031  66.925  1.00 21.58 ? 2057 HOH   B O     1 
HETATM 20481 O  O     . HOH   DA 11 .    ? 30.483  34.376  84.335  1.00 25.43 ? 2058 HOH   B O     1 
HETATM 20482 O  O     . HOH   DA 11 .    ? 9.356   29.520  98.129  1.00 28.33 ? 2059 HOH   B O     1 
HETATM 20483 O  O     . HOH   DA 11 .    ? 36.688  21.696  83.623  1.00 32.60 ? 2060 HOH   B O     1 
HETATM 20484 O  O     . HOH   DA 11 .    ? 4.770   47.598  86.887  1.00 18.65 ? 2061 HOH   B O     1 
HETATM 20485 O  O     . HOH   DA 11 .    ? 30.589  51.907  74.311  1.00 36.88 ? 2062 HOH   B O     1 
HETATM 20486 O  O     . HOH   DA 11 .    ? 2.499   49.094  75.958  1.00 17.77 ? 2063 HOH   B O     1 
HETATM 20487 O  O     . HOH   DA 11 .    ? 8.053   31.911  93.656  1.00 24.38 ? 2064 HOH   B O     1 
HETATM 20488 O  O     . HOH   DA 11 .    ? 23.995  67.662  80.563  1.00 34.75 ? 2065 HOH   B O     1 
HETATM 20489 O  O     . HOH   DA 11 .    ? 18.443  48.042  89.748  1.00 19.22 ? 2066 HOH   B O     1 
HETATM 20490 O  O     . HOH   DA 11 .    ? -9.435  45.737  130.750 1.00 32.74 ? 2067 HOH   B O     1 
HETATM 20491 O  O     . HOH   DA 11 .    ? 28.860  22.831  72.060  1.00 28.80 ? 2068 HOH   B O     1 
HETATM 20492 O  O     . HOH   DA 11 .    ? 28.414  59.462  84.099  1.00 38.96 ? 2069 HOH   B O     1 
HETATM 20493 O  O     . HOH   DA 11 .    ? -0.597  18.083  91.301  1.00 21.55 ? 2070 HOH   B O     1 
HETATM 20494 O  O     . HOH   DA 11 .    ? -3.587  46.046  106.687 1.00 22.89 ? 2071 HOH   B O     1 
HETATM 20495 O  O     . HOH   DA 11 .    ? -28.797 7.953   116.499 1.00 40.39 ? 2072 HOH   B O     1 
HETATM 20496 O  O     . HOH   DA 11 .    ? -16.357 4.637   92.575  1.00 38.74 ? 2073 HOH   B O     1 
HETATM 20497 O  O     . HOH   DA 11 .    ? 28.001  25.751  67.560  1.00 18.20 ? 2074 HOH   B O     1 
HETATM 20498 O  O     . HOH   DA 11 .    ? -1.828  36.832  87.145  1.00 18.67 ? 2075 HOH   B O     1 
HETATM 20499 O  O     . HOH   DA 11 .    ? -13.543 53.984  122.356 1.00 31.49 ? 2076 HOH   B O     1 
HETATM 20500 O  O     . HOH   DA 11 .    ? 11.331  18.393  97.484  1.00 28.80 ? 2077 HOH   B O     1 
HETATM 20501 O  O     . HOH   DA 11 .    ? 4.869   49.286  54.073  1.00 40.59 ? 2078 HOH   B O     1 
HETATM 20502 O  O     . HOH   DA 11 .    ? -12.360 34.872  86.275  1.00 36.83 ? 2079 HOH   B O     1 
HETATM 20503 O  O     . HOH   DA 11 .    ? 2.085   62.196  68.547  1.00 34.35 ? 2080 HOH   B O     1 
HETATM 20504 O  O     . HOH   DA 11 .    ? 4.912   57.822  68.647  1.00 22.82 ? 2081 HOH   B O     1 
HETATM 20505 O  O     . HOH   DA 11 .    ? 13.043  23.663  88.970  1.00 38.89 ? 2082 HOH   B O     1 
HETATM 20506 O  O     . HOH   DA 11 .    ? -30.830 21.186  83.598  1.00 41.12 ? 2083 HOH   B O     1 
HETATM 20507 O  O     . HOH   DA 11 .    ? 4.625   -3.569  95.047  1.00 35.49 ? 2084 HOH   B O     1 
HETATM 20508 O  O     . HOH   DA 11 .    ? -14.777 39.985  124.472 1.00 37.71 ? 2085 HOH   B O     1 
HETATM 20509 O  O     . HOH   DA 11 .    ? 9.151   32.136  83.441  1.00 31.92 ? 2086 HOH   B O     1 
HETATM 20510 O  O     . HOH   DA 11 .    ? 30.807  67.369  82.181  1.00 29.14 ? 2087 HOH   B O     1 
HETATM 20511 O  O     . HOH   DA 11 .    ? 10.446  33.587  109.200 1.00 24.75 ? 2088 HOH   B O     1 
HETATM 20512 O  O     . HOH   DA 11 .    ? 32.358  29.309  64.436  1.00 22.11 ? 2089 HOH   B O     1 
HETATM 20513 O  O     . HOH   DA 11 .    ? -15.462 10.413  89.606  1.00 20.07 ? 2090 HOH   B O     1 
HETATM 20514 O  O     . HOH   DA 11 .    ? 18.509  63.699  54.797  1.00 36.43 ? 2091 HOH   B O     1 
HETATM 20515 O  O     . HOH   DA 11 .    ? 32.875  25.667  101.752 1.00 28.58 ? 2092 HOH   B O     1 
HETATM 20516 O  O     . HOH   DA 11 .    ? -24.211 -1.804  112.337 1.00 43.38 ? 2093 HOH   B O     1 
HETATM 20517 O  O     . HOH   DA 11 .    ? 17.818  76.495  63.571  1.00 29.28 ? 2094 HOH   B O     1 
HETATM 20518 O  O     . HOH   DA 11 .    ? 18.883  52.174  79.736  1.00 18.75 ? 2095 HOH   B O     1 
HETATM 20519 O  O     . HOH   DA 11 .    ? 30.910  51.246  79.670  1.00 29.78 ? 2096 HOH   B O     1 
HETATM 20520 O  O     . HOH   DA 11 .    ? 16.114  53.713  104.628 1.00 26.83 ? 2097 HOH   B O     1 
HETATM 20521 O  O     . HOH   DA 11 .    ? 2.903   23.177  58.814  1.00 30.64 ? 2098 HOH   B O     1 
HETATM 20522 O  O     . HOH   DA 11 .    ? -2.837  20.647  110.477 1.00 32.59 ? 2099 HOH   B O     1 
HETATM 20523 O  O     . HOH   DA 11 .    ? -4.177  52.784  79.854  1.00 31.05 ? 2100 HOH   B O     1 
HETATM 20524 O  O     . HOH   DA 11 .    ? -4.874  56.400  126.921 1.00 38.09 ? 2101 HOH   B O     1 
HETATM 20525 O  O     . HOH   DA 11 .    ? 18.047  23.444  61.253  1.00 19.28 ? 2102 HOH   B O     1 
HETATM 20526 O  O     . HOH   DA 11 .    ? 24.759  16.216  94.924  1.00 24.52 ? 2103 HOH   B O     1 
HETATM 20527 O  O     . HOH   DA 11 .    ? 1.826   30.706  95.755  1.00 19.95 ? 2104 HOH   B O     1 
HETATM 20528 O  O     . HOH   DA 11 .    ? 12.996  48.199  81.972  1.00 23.12 ? 2105 HOH   B O     1 
HETATM 20529 O  O     . HOH   DA 11 .    ? 28.147  44.481  89.556  1.00 22.99 ? 2106 HOH   B O     1 
HETATM 20530 O  O     . HOH   DA 11 .    ? 17.325  34.236  68.230  1.00 13.02 ? 2107 HOH   B O     1 
HETATM 20531 O  O     . HOH   DA 11 .    ? -28.318 5.893   101.442 1.00 41.61 ? 2108 HOH   B O     1 
HETATM 20532 O  O     . HOH   DA 11 .    ? 1.274   22.582  63.456  1.00 23.58 ? 2109 HOH   B O     1 
HETATM 20533 O  O     . HOH   DA 11 .    ? 26.755  65.846  57.678  1.00 37.87 ? 2110 HOH   B O     1 
HETATM 20534 O  O     . HOH   DA 11 .    ? -6.146  35.705  92.299  1.00 27.15 ? 2111 HOH   B O     1 
HETATM 20535 O  O     . HOH   DA 11 .    ? -8.062  48.240  76.419  1.00 28.45 ? 2112 HOH   B O     1 
HETATM 20536 O  O     . HOH   DA 11 .    ? -16.422 22.108  82.133  1.00 25.37 ? 2113 HOH   B O     1 
HETATM 20537 O  O     . HOH   DA 11 .    ? 20.544  22.124  60.832  1.00 16.97 ? 2114 HOH   B O     1 
HETATM 20538 O  O     . HOH   DA 11 .    ? 7.824   58.185  85.014  1.00 22.70 ? 2115 HOH   B O     1 
HETATM 20539 O  O     . HOH   DA 11 .    ? 7.946   62.798  66.078  1.00 32.02 ? 2116 HOH   B O     1 
HETATM 20540 O  O     . HOH   DA 11 .    ? -14.335 9.550   87.197  1.00 23.38 ? 2117 HOH   B O     1 
HETATM 20541 O  O     . HOH   DA 11 .    ? 14.830  58.410  54.495  1.00 41.45 ? 2118 HOH   B O     1 
HETATM 20542 O  O     . HOH   DA 11 .    ? 24.825  53.406  68.334  1.00 22.30 ? 2119 HOH   B O     1 
HETATM 20543 O  O     . HOH   DA 11 .    ? -11.981 22.066  85.414  1.00 21.82 ? 2120 HOH   B O     1 
HETATM 20544 O  O     . HOH   DA 11 .    ? -16.142 52.239  123.292 1.00 35.30 ? 2121 HOH   B O     1 
HETATM 20545 O  O     . HOH   DA 11 .    ? -7.856  24.157  124.876 1.00 33.25 ? 2122 HOH   B O     1 
HETATM 20546 O  O     . HOH   DA 11 .    ? -2.671  30.581  70.524  1.00 17.97 ? 2123 HOH   B O     1 
HETATM 20547 O  O     . HOH   DA 11 .    ? 8.227   37.556  78.944  1.00 16.93 ? 2124 HOH   B O     1 
HETATM 20548 O  O     . HOH   DA 11 .    ? -2.706  14.660  98.583  1.00 16.23 ? 2125 HOH   B O     1 
HETATM 20549 O  O     . HOH   DA 11 .    ? 22.867  72.977  81.384  1.00 28.98 ? 2126 HOH   B O     1 
HETATM 20550 O  O     . HOH   DA 11 .    ? 30.990  34.623  77.052  1.00 28.46 ? 2127 HOH   B O     1 
HETATM 20551 O  O     . HOH   DA 11 .    ? 31.431  62.439  74.867  1.00 18.90 ? 2128 HOH   B O     1 
HETATM 20552 O  O     . HOH   DA 11 .    ? -23.097 25.796  103.128 1.00 36.95 ? 2129 HOH   B O     1 
HETATM 20553 O  O     . HOH   DA 11 .    ? -5.534  23.152  80.455  1.00 19.96 ? 2130 HOH   B O     1 
HETATM 20554 O  O     . HOH   DA 11 .    ? 29.397  41.704  79.778  1.00 26.49 ? 2131 HOH   B O     1 
HETATM 20555 O  O     . HOH   DA 11 .    ? 28.014  33.754  80.137  1.00 33.95 ? 2132 HOH   B O     1 
HETATM 20556 O  O     . HOH   DA 11 .    ? 17.383  44.248  111.712 1.00 33.50 ? 2133 HOH   B O     1 
HETATM 20557 O  O     . HOH   DA 11 .    ? -3.443  52.430  82.306  1.00 25.55 ? 2134 HOH   B O     1 
HETATM 20558 O  O     . HOH   DA 11 .    ? 16.710  51.473  59.772  1.00 25.36 ? 2135 HOH   B O     1 
HETATM 20559 O  O     . HOH   DA 11 .    ? -1.927  28.255  62.536  1.00 26.69 ? 2136 HOH   B O     1 
HETATM 20560 O  O     . HOH   DA 11 .    ? 22.454  61.626  82.872  1.00 33.93 ? 2137 HOH   B O     1 
HETATM 20561 O  O     . HOH   DA 11 .    ? -2.433  -7.366  110.293 1.00 24.21 ? 2138 HOH   B O     1 
HETATM 20562 O  O     . HOH   DA 11 .    ? 28.007  9.157   73.697  1.00 31.58 ? 2139 HOH   B O     1 
HETATM 20563 O  O     . HOH   DA 11 .    ? 2.455   49.011  98.779  1.00 21.75 ? 2140 HOH   B O     1 
HETATM 20564 O  O     . HOH   DA 11 .    ? 11.529  18.167  94.684  1.00 30.59 ? 2141 HOH   B O     1 
HETATM 20565 O  O     . HOH   DA 11 .    ? 16.708  46.967  54.440  1.00 32.41 ? 2142 HOH   B O     1 
HETATM 20566 O  O     . HOH   DA 11 .    ? 34.932  32.494  54.958  1.00 27.72 ? 2143 HOH   B O     1 
HETATM 20567 O  O     . HOH   DA 11 .    ? 15.757  10.414  95.396  1.00 22.78 ? 2144 HOH   B O     1 
HETATM 20568 O  O     . HOH   DA 11 .    ? -10.809 36.405  76.235  1.00 38.51 ? 2145 HOH   B O     1 
HETATM 20569 O  O     . HOH   DA 11 .    ? 3.059   31.456  98.115  1.00 24.10 ? 2146 HOH   B O     1 
HETATM 20570 O  O     . HOH   DA 11 .    ? 29.195  35.604  78.194  1.00 35.19 ? 2147 HOH   B O     1 
HETATM 20571 O  O     . HOH   DA 11 .    ? -7.021  44.036  73.640  1.00 30.35 ? 2148 HOH   B O     1 
HETATM 20572 O  O     . HOH   DA 11 .    ? 21.962  25.269  82.383  1.00 19.75 ? 2149 HOH   B O     1 
HETATM 20573 O  O     . HOH   DA 11 .    ? 35.726  31.572  103.586 1.00 32.04 ? 2150 HOH   B O     1 
HETATM 20574 O  O     . HOH   DA 11 .    ? 35.386  25.668  77.502  1.00 25.17 ? 2151 HOH   B O     1 
HETATM 20575 O  O     . HOH   DA 11 .    ? 34.687  17.021  67.466  1.00 30.32 ? 2152 HOH   B O     1 
HETATM 20576 O  O     . HOH   DA 11 .    ? -9.625  0.802   112.334 1.00 23.90 ? 2153 HOH   B O     1 
HETATM 20577 O  O     . HOH   DA 11 .    ? 8.410   -0.731  98.599  1.00 36.79 ? 2154 HOH   B O     1 
HETATM 20578 O  O     . HOH   DA 11 .    ? 33.976  22.676  77.959  1.00 24.70 ? 2155 HOH   B O     1 
HETATM 20579 O  O     . HOH   DA 11 .    ? 34.910  19.321  59.571  1.00 34.49 ? 2156 HOH   B O     1 
HETATM 20580 O  O     . HOH   DA 11 .    ? 4.867   43.013  55.769  1.00 28.87 ? 2157 HOH   B O     1 
HETATM 20581 O  O     . HOH   DA 11 .    ? 9.936   22.150  102.449 1.00 30.75 ? 2158 HOH   B O     1 
HETATM 20582 O  O     . HOH   DA 11 .    ? -8.700  31.647  86.705  1.00 18.18 ? 2159 HOH   B O     1 
HETATM 20583 O  O     . HOH   DA 11 .    ? 2.834   54.293  66.708  1.00 31.70 ? 2160 HOH   B O     1 
HETATM 20584 O  O     . HOH   DA 11 .    ? -1.057  13.630  100.544 1.00 16.51 ? 2161 HOH   B O     1 
HETATM 20585 O  O     . HOH   DA 11 .    ? 29.912  24.215  103.286 1.00 38.60 ? 2162 HOH   B O     1 
HETATM 20586 O  O     . HOH   DA 11 .    ? 29.644  8.932   86.031  1.00 38.02 ? 2163 HOH   B O     1 
HETATM 20587 O  O     . HOH   DA 11 .    ? 9.880   53.244  65.414  1.00 23.49 ? 2164 HOH   B O     1 
HETATM 20588 O  O     . HOH   DA 11 .    ? -5.639  46.666  84.015  1.00 26.03 ? 2165 HOH   B O     1 
HETATM 20589 O  O     . HOH   DA 11 .    ? -4.985  49.397  103.259 1.00 37.49 ? 2166 HOH   B O     1 
HETATM 20590 O  O     . HOH   DA 11 .    ? 18.727  35.589  112.660 1.00 19.31 ? 2167 HOH   B O     1 
HETATM 20591 O  O     . HOH   DA 11 .    ? 5.486   18.741  87.263  1.00 24.39 ? 2168 HOH   B O     1 
HETATM 20592 O  O     . HOH   DA 11 .    ? 4.655   56.267  74.809  1.00 16.60 ? 2169 HOH   B O     1 
HETATM 20593 O  O     . HOH   DA 11 .    ? 2.804   45.051  67.651  1.00 16.02 ? 2170 HOH   B O     1 
HETATM 20594 O  O     . HOH   DA 11 .    ? 7.567   54.408  64.258  1.00 29.16 ? 2171 HOH   B O     1 
HETATM 20595 O  O     . HOH   DA 11 .    ? 6.015   31.440  120.422 1.00 50.53 ? 2172 HOH   B O     1 
HETATM 20596 O  O     . HOH   DA 11 .    ? -7.492  13.319  94.292  1.00 16.07 ? 2173 HOH   B O     1 
HETATM 20597 O  O     . HOH   DA 11 .    ? 27.195  39.552  104.448 1.00 30.62 ? 2174 HOH   B O     1 
HETATM 20598 O  O     . HOH   DA 11 .    ? 9.384   -0.233  90.073  1.00 38.26 ? 2175 HOH   B O     1 
HETATM 20599 O  O     . HOH   DA 11 .    ? 17.979  76.067  78.367  1.00 35.34 ? 2176 HOH   B O     1 
HETATM 20600 O  O     . HOH   DA 11 .    ? 16.343  82.287  79.583  1.00 47.49 ? 2177 HOH   B O     1 
HETATM 20601 O  O     . HOH   DA 11 .    ? 22.771  9.773   84.843  1.00 38.49 ? 2178 HOH   B O     1 
HETATM 20602 O  O     . HOH   DA 11 .    ? 16.093  56.025  63.701  1.00 25.13 ? 2179 HOH   B O     1 
HETATM 20603 O  O     . HOH   DA 11 .    ? 2.719   44.289  58.252  1.00 29.63 ? 2180 HOH   B O     1 
HETATM 20604 O  O     . HOH   DA 11 .    ? 34.309  13.098  80.716  1.00 31.18 ? 2181 HOH   B O     1 
HETATM 20605 O  O     . HOH   DA 11 .    ? 17.001  7.905   89.638  1.00 35.71 ? 2182 HOH   B O     1 
HETATM 20606 O  O     . HOH   DA 11 .    ? -2.181  57.693  75.019  1.00 17.06 ? 2183 HOH   B O     1 
HETATM 20607 O  O     . HOH   DA 11 .    ? 12.097  77.613  64.035  1.00 32.39 ? 2184 HOH   B O     1 
HETATM 20608 O  O     . HOH   DA 11 .    ? 5.191   24.254  119.227 1.00 40.04 ? 2185 HOH   B O     1 
HETATM 20609 O  O     . HOH   DA 11 .    ? 19.064  58.543  82.065  1.00 24.72 ? 2186 HOH   B O     1 
HETATM 20610 O  O     . HOH   DA 11 .    ? 14.391  9.184   93.382  1.00 22.31 ? 2187 HOH   B O     1 
HETATM 20611 O  O     . HOH   DA 11 .    ? 22.497  12.063  79.585  1.00 33.43 ? 2188 HOH   B O     1 
HETATM 20612 O  O     . HOH   DA 11 .    ? -10.370 18.438  130.814 1.00 36.10 ? 2189 HOH   B O     1 
HETATM 20613 O  O     . HOH   DA 11 .    ? 9.703   18.530  100.893 1.00 21.83 ? 2190 HOH   B O     1 
HETATM 20614 O  O     . HOH   DA 11 .    ? -13.824 49.073  110.485 1.00 31.91 ? 2191 HOH   B O     1 
HETATM 20615 O  O     . HOH   DA 11 .    ? 16.088  14.130  106.675 1.00 25.43 ? 2192 HOH   B O     1 
HETATM 20616 O  O     . HOH   DA 11 .    ? 14.290  35.411  81.508  1.00 24.25 ? 2193 HOH   B O     1 
HETATM 20617 O  O     . HOH   DA 11 .    ? 9.913   77.003  64.663  1.00 39.05 ? 2194 HOH   B O     1 
HETATM 20618 O  O     . HOH   DA 11 .    ? -2.905  64.546  83.175  1.00 16.36 ? 2195 HOH   B O     1 
HETATM 20619 O  O     . HOH   DA 11 .    ? 24.889  18.063  100.023 1.00 32.55 ? 2196 HOH   B O     1 
HETATM 20620 O  O     . HOH   DA 11 .    ? -19.820 24.079  112.276 1.00 34.33 ? 2197 HOH   B O     1 
HETATM 20621 O  O     . HOH   DA 11 .    ? -1.963  -0.829  108.811 1.00 27.94 ? 2198 HOH   B O     1 
HETATM 20622 O  O     . HOH   DA 11 .    ? 2.473   19.033  77.086  1.00 26.79 ? 2199 HOH   B O     1 
HETATM 20623 O  O     . HOH   DA 11 .    ? -29.063 17.570  117.190 1.00 34.98 ? 2200 HOH   B O     1 
HETATM 20624 O  O     . HOH   DA 11 .    ? 20.035  19.124  60.003  1.00 24.27 ? 2201 HOH   B O     1 
HETATM 20625 O  O     . HOH   DA 11 .    ? 28.136  30.937  80.509  1.00 21.88 ? 2202 HOH   B O     1 
HETATM 20626 O  O     . HOH   DA 11 .    ? -2.055  2.738   83.039  1.00 42.12 ? 2203 HOH   B O     1 
HETATM 20627 O  O     . HOH   DA 11 .    ? 22.789  51.426  64.898  1.00 19.72 ? 2204 HOH   B O     1 
HETATM 20628 O  O     . HOH   DA 11 .    ? 22.533  50.241  53.439  1.00 38.72 ? 2205 HOH   B O     1 
HETATM 20629 O  O     . HOH   DA 11 .    ? -4.462  46.509  132.801 1.00 44.42 ? 2206 HOH   B O     1 
HETATM 20630 O  O     . HOH   DA 11 .    ? -0.779  -7.684  99.399  1.00 26.25 ? 2207 HOH   B O     1 
HETATM 20631 O  O     . HOH   DA 11 .    ? -24.288 10.391  126.489 1.00 41.23 ? 2208 HOH   B O     1 
HETATM 20632 O  O     . HOH   DA 11 .    ? 27.811  65.375  84.526  1.00 40.26 ? 2209 HOH   B O     1 
HETATM 20633 O  O     . HOH   DA 11 .    ? 7.171   66.367  86.310  1.00 33.07 ? 2210 HOH   B O     1 
HETATM 20634 O  O     . HOH   DA 11 .    ? 35.502  33.207  80.523  1.00 32.37 ? 2211 HOH   B O     1 
HETATM 20635 O  O     . HOH   DA 11 .    ? -6.447  9.132   81.871  1.00 32.64 ? 2212 HOH   B O     1 
HETATM 20636 O  O     . HOH   DA 11 .    ? 5.438   53.434  113.185 1.00 39.11 ? 2213 HOH   B O     1 
HETATM 20637 O  O     . HOH   DA 11 .    ? 4.075   77.340  62.928  1.00 36.86 ? 2214 HOH   B O     1 
HETATM 20638 O  O     . HOH   DA 11 .    ? 27.999  49.113  97.695  1.00 34.10 ? 2215 HOH   B O     1 
HETATM 20639 O  O     . HOH   DA 11 .    ? -12.362 8.023   126.791 1.00 29.62 ? 2216 HOH   B O     1 
HETATM 20640 O  O     . HOH   DA 11 .    ? 19.071  54.601  103.922 1.00 23.72 ? 2217 HOH   B O     1 
HETATM 20641 O  O     . HOH   DA 11 .    ? 15.362  49.601  78.797  1.00 24.80 ? 2218 HOH   B O     1 
HETATM 20642 O  O     . HOH   DA 11 .    ? 23.875  50.127  102.356 1.00 36.64 ? 2219 HOH   B O     1 
HETATM 20643 O  O     . HOH   DA 11 .    ? -6.327  47.984  78.600  1.00 36.02 ? 2220 HOH   B O     1 
HETATM 20644 O  O     . HOH   DA 11 .    ? -3.036  40.004  57.709  1.00 22.75 ? 2221 HOH   B O     1 
HETATM 20645 O  O     . HOH   DA 11 .    ? 20.618  30.621  112.954 1.00 34.69 ? 2222 HOH   B O     1 
HETATM 20646 O  O     . HOH   DA 11 .    ? 17.828  49.931  111.516 1.00 32.96 ? 2223 HOH   B O     1 
HETATM 20647 O  O     . HOH   DA 11 .    ? 13.991  75.796  62.717  1.00 27.14 ? 2224 HOH   B O     1 
HETATM 20648 O  O     . HOH   DA 11 .    ? 27.073  56.668  80.932  1.00 30.97 ? 2225 HOH   B O     1 
HETATM 20649 O  O     . HOH   DA 11 .    ? -1.152  37.852  76.178  1.00 27.83 ? 2226 HOH   B O     1 
HETATM 20650 O  O     . HOH   DA 11 .    ? -5.881  15.623  94.246  1.00 16.28 ? 2227 HOH   B O     1 
HETATM 20651 O  O     . HOH   DA 11 .    ? 26.332  13.146  87.769  1.00 28.22 ? 2228 HOH   B O     1 
HETATM 20652 O  O     . HOH   DA 11 .    ? 32.383  70.235  73.421  1.00 34.31 ? 2229 HOH   B O     1 
HETATM 20653 O  O     . HOH   DA 11 .    ? 34.174  41.502  90.726  1.00 32.86 ? 2230 HOH   B O     1 
HETATM 20654 O  O     . HOH   DA 11 .    ? 36.994  37.631  88.763  1.00 19.69 ? 2231 HOH   B O     1 
HETATM 20655 O  O     . HOH   DA 11 .    ? -21.606 1.815   120.789 1.00 42.51 ? 2232 HOH   B O     1 
HETATM 20656 O  O     . HOH   DA 11 .    ? 35.292  31.556  58.208  1.00 29.91 ? 2233 HOH   B O     1 
HETATM 20657 O  O     . HOH   DA 11 .    ? -34.495 13.318  110.856 1.00 37.12 ? 2234 HOH   B O     1 
HETATM 20658 O  O     . HOH   DA 11 .    ? 23.814  23.510  106.519 1.00 35.68 ? 2235 HOH   B O     1 
HETATM 20659 O  O     . HOH   DA 11 .    ? 20.012  20.559  108.985 1.00 20.72 ? 2236 HOH   B O     1 
HETATM 20660 O  O     . HOH   DA 11 .    ? 16.179  52.150  79.355  1.00 20.78 ? 2237 HOH   B O     1 
HETATM 20661 O  O     . HOH   DA 11 .    ? -19.538 28.974  88.138  1.00 31.16 ? 2238 HOH   B O     1 
HETATM 20662 O  O     . HOH   DA 11 .    ? 21.952  15.111  80.892  1.00 21.88 ? 2239 HOH   B O     1 
HETATM 20663 O  O     . HOH   DA 11 .    ? 28.867  65.502  62.110  1.00 29.76 ? 2240 HOH   B O     1 
HETATM 20664 O  O     . HOH   DA 11 .    ? 30.828  20.005  56.067  1.00 27.75 ? 2241 HOH   B O     1 
HETATM 20665 O  O     . HOH   DA 11 .    ? 5.343   66.634  61.454  1.00 38.61 ? 2242 HOH   B O     1 
HETATM 20666 O  O     . HOH   DA 11 .    ? 7.823   28.739  80.952  1.00 26.88 ? 2243 HOH   B O     1 
HETATM 20667 O  O     . HOH   DA 11 .    ? -7.665  10.606  112.578 1.00 20.50 ? 2244 HOH   B O     1 
HETATM 20668 O  O     . HOH   DA 11 .    ? 3.652   67.224  60.035  1.00 41.47 ? 2245 HOH   B O     1 
HETATM 20669 O  O     . HOH   DA 11 .    ? 31.684  37.195  51.112  1.00 40.82 ? 2246 HOH   B O     1 
HETATM 20670 O  O     . HOH   DA 11 .    ? 13.281  18.853  87.322  1.00 22.44 ? 2247 HOH   B O     1 
HETATM 20671 O  O     . HOH   DA 11 .    ? 8.812   45.880  131.878 1.00 38.82 ? 2248 HOH   B O     1 
HETATM 20672 O  O     . HOH   DA 11 .    ? -2.647  42.271  73.996  1.00 30.46 ? 2249 HOH   B O     1 
HETATM 20673 O  O     . HOH   DA 11 .    ? 10.443  37.646  77.386  1.00 22.98 ? 2250 HOH   B O     1 
HETATM 20674 O  O     . HOH   DA 11 .    ? 5.674   70.298  60.909  1.00 39.54 ? 2251 HOH   B O     1 
HETATM 20675 O  O     . HOH   DA 11 .    ? -29.606 12.029  87.247  1.00 45.47 ? 2252 HOH   B O     1 
HETATM 20676 O  O     . HOH   DA 11 .    ? 42.112  37.778  95.616  1.00 30.75 ? 2253 HOH   B O     1 
HETATM 20677 O  O     . HOH   DA 11 .    ? -9.570  14.369  114.434 1.00 30.14 ? 2254 HOH   B O     1 
HETATM 20678 O  O     . HOH   DA 11 .    ? 18.117  10.777  113.945 1.00 45.70 ? 2255 HOH   B O     1 
HETATM 20679 O  O     . HOH   DA 11 .    ? 32.240  40.432  90.410  1.00 29.90 ? 2256 HOH   B O     1 
HETATM 20680 O  O     . HOH   DA 11 .    ? 18.215  14.683  105.027 1.00 39.23 ? 2257 HOH   B O     1 
HETATM 20681 O  O     . HOH   DA 11 .    ? 19.429  78.168  76.944  1.00 40.58 ? 2258 HOH   B O     1 
HETATM 20682 O  O     . HOH   DA 11 .    ? 12.588  29.596  50.309  1.00 24.46 ? 2259 HOH   B O     1 
HETATM 20683 O  O     . HOH   DA 11 .    ? 7.119   35.937  108.643 1.00 38.38 ? 2260 HOH   B O     1 
HETATM 20684 O  O     . HOH   DA 11 .    ? -4.996  -3.698  91.597  1.00 29.32 ? 2261 HOH   B O     1 
HETATM 20685 O  O     . HOH   DA 11 .    ? 17.861  74.781  81.497  1.00 36.97 ? 2262 HOH   B O     1 
HETATM 20686 O  O     . HOH   DA 11 .    ? 42.431  32.371  96.156  1.00 40.94 ? 2263 HOH   B O     1 
HETATM 20687 O  O     . HOH   DA 11 .    ? 24.662  63.202  54.187  1.00 29.96 ? 2264 HOH   B O     1 
HETATM 20688 O  O     . HOH   DA 11 .    ? 23.728  17.222  82.438  1.00 22.46 ? 2265 HOH   B O     1 
HETATM 20689 O  O     . HOH   DA 11 .    ? -0.419  25.469  102.862 1.00 44.36 ? 2266 HOH   B O     1 
HETATM 20690 O  O     . HOH   DA 11 .    ? 25.575  75.367  76.552  1.00 30.55 ? 2267 HOH   B O     1 
HETATM 20691 O  O     . HOH   DA 11 .    ? -2.746  29.959  96.728  1.00 30.09 ? 2268 HOH   B O     1 
HETATM 20692 O  O     . HOH   DA 11 .    ? 31.510  35.199  74.412  1.00 31.33 ? 2269 HOH   B O     1 
HETATM 20693 O  O     . HOH   DA 11 .    ? 16.140  51.339  53.666  1.00 37.86 ? 2270 HOH   B O     1 
HETATM 20694 O  O     . HOH   DA 11 .    ? -27.945 14.440  86.046  1.00 37.63 ? 2271 HOH   B O     1 
HETATM 20695 O  O     . HOH   DA 11 .    ? 33.228  38.184  71.751  1.00 37.56 ? 2272 HOH   B O     1 
HETATM 20696 O  O     . HOH   DA 11 .    ? -31.842 14.369  114.008 1.00 38.66 ? 2273 HOH   B O     1 
HETATM 20697 O  O     . HOH   DA 11 .    ? -23.084 21.855  101.720 1.00 32.78 ? 2274 HOH   B O     1 
HETATM 20698 O  O     . HOH   DA 11 .    ? -12.789 31.833  83.645  1.00 35.26 ? 2275 HOH   B O     1 
HETATM 20699 O  O     . HOH   DA 11 .    ? 5.525   -3.317  99.438  1.00 39.43 ? 2276 HOH   B O     1 
HETATM 20700 O  O     . HOH   DA 11 .    ? 2.418   3.944   84.489  1.00 31.77 ? 2277 HOH   B O     1 
HETATM 20701 O  O     . HOH   DA 11 .    ? 26.519  41.273  80.997  1.00 25.27 ? 2278 HOH   B O     1 
HETATM 20702 O  O     . HOH   DA 11 .    ? -6.777  39.176  67.219  1.00 29.92 ? 2279 HOH   B O     1 
HETATM 20703 O  O     . HOH   DA 11 .    ? -16.613 8.359   127.556 1.00 42.98 ? 2280 HOH   B O     1 
HETATM 20704 O  O     . HOH   DA 11 .    ? 14.816  56.972  71.900  1.00 22.75 ? 2281 HOH   B O     1 
HETATM 20705 O  O     . HOH   DA 11 .    ? 8.883   30.841  88.367  1.00 30.19 ? 2282 HOH   B O     1 
HETATM 20706 O  O     . HOH   DA 11 .    ? 12.265  58.030  93.774  1.00 30.12 ? 2283 HOH   B O     1 
HETATM 20707 O  O     . HOH   DA 11 .    ? 4.580   0.475   86.459  1.00 32.44 ? 2284 HOH   B O     1 
HETATM 20708 O  O     . HOH   DA 11 .    ? -15.054 19.516  82.371  1.00 27.40 ? 2285 HOH   B O     1 
HETATM 20709 O  O     . HOH   DA 11 .    ? 20.652  62.803  53.824  1.00 33.00 ? 2286 HOH   B O     1 
HETATM 20710 O  O     . HOH   DA 11 .    ? -14.334 44.763  113.166 1.00 40.05 ? 2287 HOH   B O     1 
HETATM 20711 O  O     . HOH   DA 11 .    ? 15.919  8.203   110.697 1.00 33.34 ? 2288 HOH   B O     1 
HETATM 20712 O  O     . HOH   DA 11 .    ? -2.872  21.285  133.759 1.00 50.49 ? 2289 HOH   B O     1 
HETATM 20713 O  O     . HOH   DA 11 .    ? 32.982  26.265  54.349  1.00 37.73 ? 2290 HOH   B O     1 
HETATM 20714 O  O     . HOH   DA 11 .    ? 24.000  31.694  46.963  1.00 37.55 ? 2291 HOH   B O     1 
HETATM 20715 O  O     . HOH   DA 11 .    ? 7.710   -8.927  111.055 1.00 35.50 ? 2292 HOH   B O     1 
HETATM 20716 O  O     . HOH   DA 11 .    ? -9.228  8.187   81.853  1.00 39.12 ? 2293 HOH   B O     1 
HETATM 20717 O  O     . HOH   DA 11 .    ? 26.334  51.981  55.566  1.00 35.03 ? 2294 HOH   B O     1 
HETATM 20718 O  O     . HOH   DA 11 .    ? 6.326   24.900  83.525  1.00 26.05 ? 2295 HOH   B O     1 
HETATM 20719 O  O     . HOH   DA 11 .    ? -5.566  37.591  85.759  1.00 28.83 ? 2296 HOH   B O     1 
HETATM 20720 O  O     . HOH   DA 11 .    ? 37.834  23.040  89.967  1.00 41.81 ? 2297 HOH   B O     1 
HETATM 20721 O  O     . HOH   DA 11 .    ? 3.231   23.739  103.752 1.00 44.14 ? 2298 HOH   B O     1 
HETATM 20722 O  O     . HOH   DA 11 .    ? 23.390  24.618  47.558  1.00 32.65 ? 2299 HOH   B O     1 
HETATM 20723 O  O     . HOH   DA 11 .    ? -30.794 5.765   99.782  1.00 40.31 ? 2300 HOH   B O     1 
HETATM 20724 O  O     . HOH   DA 11 .    ? -17.023 49.549  116.377 1.00 41.78 ? 2301 HOH   B O     1 
HETATM 20725 O  O     . HOH   DA 11 .    ? -6.131  37.628  96.129  1.00 39.11 ? 2302 HOH   B O     1 
HETATM 20726 O  O     . HOH   DA 11 .    ? -1.172  22.818  96.820  1.00 27.72 ? 2303 HOH   B O     1 
HETATM 20727 O  O     . HOH   DA 11 .    ? -14.632 26.963  101.304 1.00 29.71 ? 2304 HOH   B O     1 
HETATM 20728 O  O     . HOH   DA 11 .    ? 5.970   27.993  87.742  1.00 36.25 ? 2305 HOH   B O     1 
HETATM 20729 O  O     . HOH   DA 11 .    ? 34.473  24.890  67.254  1.00 43.00 ? 2306 HOH   B O     1 
HETATM 20730 O  O     . HOH   DA 11 .    ? 35.420  17.244  82.928  1.00 40.50 ? 2307 HOH   B O     1 
HETATM 20731 O  O     . HOH   DA 11 .    ? -1.088  44.424  75.293  1.00 29.41 ? 2308 HOH   B O     1 
HETATM 20732 O  O     . HOH   DA 11 .    ? -2.626  -5.368  89.345  1.00 34.29 ? 2309 HOH   B O     1 
HETATM 20733 O  O     . HOH   DA 11 .    ? 30.071  49.299  81.687  1.00 45.26 ? 2310 HOH   B O     1 
HETATM 20734 O  O     . HOH   DA 11 .    ? 26.243  13.230  90.663  1.00 39.17 ? 2311 HOH   B O     1 
HETATM 20735 O  O     . HOH   DA 11 .    ? 23.854  21.027  107.013 1.00 36.73 ? 2312 HOH   B O     1 
HETATM 20736 O  O     . HOH   DA 11 .    ? 22.795  67.712  59.358  1.00 27.88 ? 2313 HOH   B O     1 
HETATM 20737 O  O     . HOH   DA 11 .    ? 0.309   21.350  131.744 1.00 32.32 ? 2314 HOH   B O     1 
HETATM 20738 O  O     . HOH   DA 11 .    ? 16.919  24.883  52.257  1.00 27.29 ? 2315 HOH   B O     1 
HETATM 20739 O  O     . HOH   DA 11 .    ? -0.818  43.990  55.840  1.00 30.43 ? 2316 HOH   B O     1 
HETATM 20740 O  O     . HOH   DA 11 .    ? 28.242  41.669  53.080  1.00 32.09 ? 2317 HOH   B O     1 
HETATM 20741 O  O     . HOH   DA 11 .    ? 14.770  19.729  89.293  1.00 37.12 ? 2318 HOH   B O     1 
HETATM 20742 O  O     . HOH   DA 11 .    ? -21.184 8.364   120.457 1.00 40.19 ? 2319 HOH   B O     1 
HETATM 20743 O  O     . HOH   DA 11 .    ? 34.701  6.340   81.476  1.00 42.47 ? 2320 HOH   B O     1 
HETATM 20744 O  O     . HOH   DA 11 .    ? -2.892  22.954  79.257  1.00 22.30 ? 2321 HOH   B O     1 
HETATM 20745 O  O     . HOH   DA 11 .    ? 9.596   68.644  54.817  1.00 42.88 ? 2322 HOH   B O     1 
HETATM 20746 O  O     . HOH   DA 11 .    ? 9.285   23.914  121.693 1.00 35.48 ? 2323 HOH   B O     1 
HETATM 20747 O  O     . HOH   DA 11 .    ? 23.178  8.292   73.403  1.00 38.51 ? 2324 HOH   B O     1 
HETATM 20748 O  O     . HOH   DA 11 .    ? 6.096   17.301  114.771 1.00 29.01 ? 2325 HOH   B O     1 
HETATM 20749 O  O     . HOH   DA 11 .    ? 18.105  8.640   106.969 1.00 44.45 ? 2326 HOH   B O     1 
HETATM 20750 O  O     . HOH   DA 11 .    ? -22.041 7.945   85.760  1.00 36.99 ? 2327 HOH   B O     1 
HETATM 20751 O  O     . HOH   DA 11 .    ? 26.851  73.325  78.385  1.00 38.51 ? 2328 HOH   B O     1 
HETATM 20752 O  O     . HOH   DA 11 .    ? -10.903 29.247  99.700  1.00 46.78 ? 2329 HOH   B O     1 
HETATM 20753 O  O     . HOH   DA 11 .    ? -3.337  -2.390  84.800  1.00 39.74 ? 2330 HOH   B O     1 
HETATM 20754 O  O     . HOH   DA 11 .    ? 15.037  29.120  49.062  1.00 30.17 ? 2331 HOH   B O     1 
HETATM 20755 O  O     . HOH   DA 11 .    ? -7.285  56.171  127.682 1.00 36.63 ? 2332 HOH   B O     1 
HETATM 20756 O  O     . HOH   DA 11 .    ? 31.761  45.554  61.437  1.00 42.04 ? 2333 HOH   B O     1 
HETATM 20757 O  O     . HOH   DA 11 .    ? -4.045  -4.529  93.950  1.00 34.68 ? 2334 HOH   B O     1 
HETATM 20758 O  O     . HOH   DA 11 .    ? 0.992   56.038  65.664  1.00 38.51 ? 2335 HOH   B O     1 
HETATM 20759 O  O     . HOH   DA 11 .    ? 26.352  47.220  102.562 1.00 35.71 ? 2336 HOH   B O     1 
HETATM 20760 O  O     . HOH   DA 11 .    ? 25.108  24.405  49.583  1.00 38.36 ? 2337 HOH   B O     1 
HETATM 20761 O  O     . HOH   DA 11 .    ? 5.543   21.038  85.814  1.00 40.88 ? 2338 HOH   B O     1 
HETATM 20762 O  O     . HOH   DA 11 .    ? 34.387  16.309  61.982  1.00 36.97 ? 2339 HOH   B O     1 
HETATM 20763 O  O     . HOH   DA 11 .    ? 32.831  20.334  72.278  1.00 36.16 ? 2340 HOH   B O     1 
HETATM 20764 O  O     . HOH   DA 11 .    ? 10.644  10.234  122.892 1.00 31.57 ? 2341 HOH   B O     1 
HETATM 20765 O  O     . HOH   DA 11 .    ? 7.435   33.912  51.191  1.00 31.14 ? 2342 HOH   B O     1 
HETATM 20766 O  O     . HOH   DA 11 .    ? 4.223   25.621  128.556 1.00 36.20 ? 2343 HOH   B O     1 
HETATM 20767 O  O     . HOH   DA 11 .    ? 9.138   0.733   119.300 1.00 37.24 ? 2344 HOH   B O     1 
HETATM 20768 O  O     . HOH   DA 11 .    ? -2.340  60.575  123.664 1.00 38.86 ? 2345 HOH   B O     1 
HETATM 20769 O  O     . HOH   DA 11 .    ? 2.718   57.392  70.581  1.00 28.75 ? 2346 HOH   B O     1 
HETATM 20770 O  O     . HOH   DA 11 .    ? 17.917  46.459  111.685 1.00 37.53 ? 2347 HOH   B O     1 
HETATM 20771 O  O     . HOH   DA 11 .    ? 11.396  43.858  50.822  1.00 35.31 ? 2348 HOH   B O     1 
HETATM 20772 O  O     . HOH   DA 11 .    ? 21.706  58.919  96.351  1.00 40.66 ? 2349 HOH   B O     1 
HETATM 20773 O  O     . HOH   DA 11 .    ? 39.416  29.604  80.796  1.00 34.85 ? 2350 HOH   B O     1 
HETATM 20774 O  O     . HOH   DA 11 .    ? -6.329  39.874  85.993  1.00 31.65 ? 2351 HOH   B O     1 
HETATM 20775 O  O     . HOH   DA 11 .    ? 6.080   17.518  96.184  1.00 29.81 ? 2352 HOH   B O     1 
HETATM 20776 O  O     . HOH   DA 11 .    ? -33.235 16.745  121.177 1.00 36.06 ? 2353 HOH   B O     1 
HETATM 20777 O  O     . HOH   DA 11 .    ? 15.915  35.539  113.132 1.00 34.03 ? 2354 HOH   B O     1 
HETATM 20778 O  O     . HOH   DA 11 .    ? 27.658  71.695  80.956  1.00 43.70 ? 2355 HOH   B O     1 
HETATM 20779 O  O     . HOH   DA 11 .    ? -1.515  37.763  73.363  1.00 21.19 ? 2356 HOH   B O     1 
HETATM 20780 O  O     . HOH   DA 11 .    ? 19.037  60.406  54.156  1.00 38.40 ? 2357 HOH   B O     1 
HETATM 20781 O  O     . HOH   DA 11 .    ? 10.945  50.765  108.887 1.00 44.19 ? 2358 HOH   B O     1 
HETATM 20782 O  O     . HOH   DA 11 .    ? 16.555  56.338  94.714  1.00 32.23 ? 2359 HOH   B O     1 
HETATM 20783 O  O     . HOH   DA 11 .    ? 1.854   24.744  95.089  1.00 35.89 ? 2360 HOH   B O     1 
HETATM 20784 O  O     . HOH   DA 11 .    ? 12.324  39.895  132.099 1.00 41.06 ? 2361 HOH   B O     1 
HETATM 20785 O  O     . HOH   DA 11 .    ? 7.394   -6.898  105.315 1.00 44.90 ? 2362 HOH   B O     1 
HETATM 20786 O  O     . HOH   DA 11 .    ? 13.039  35.225  109.230 1.00 33.04 ? 2363 HOH   B O     1 
HETATM 20787 O  O     . HOH   DA 11 .    ? 4.323   29.739  81.852  1.00 23.15 ? 2364 HOH   B O     1 
HETATM 20788 O  O     . HOH   DA 11 .    ? 1.351   22.104  95.126  1.00 34.26 ? 2365 HOH   B O     1 
HETATM 20789 O  O     . HOH   DA 11 .    ? 7.506   24.002  89.027  1.00 39.17 ? 2366 HOH   B O     1 
HETATM 20790 O  O     . HOH   DA 11 .    ? -22.662 4.102   96.086  1.00 40.69 ? 2367 HOH   B O     1 
HETATM 20791 O  O     . HOH   DA 11 .    ? -7.256  37.139  66.186  1.00 35.54 ? 2368 HOH   B O     1 
HETATM 20792 O  O     . HOH   DA 11 .    ? 12.433  46.667  111.341 1.00 39.16 ? 2369 HOH   B O     1 
HETATM 20793 O  O     . HOH   DA 11 .    ? -0.216  -1.954  94.614  1.00 29.34 ? 2370 HOH   B O     1 
HETATM 20794 O  O     . HOH   DA 11 .    ? 9.364   48.860  108.386 1.00 35.96 ? 2371 HOH   B O     1 
HETATM 20795 O  O     . HOH   DA 11 .    ? 14.227  53.506  86.475  1.00 40.10 ? 2372 HOH   B O     1 
HETATM 20796 O  O     . HOH   DA 11 .    ? 29.987  70.974  72.544  1.00 32.77 ? 2373 HOH   B O     1 
HETATM 20797 O  O     . HOH   DA 11 .    ? 30.508  42.313  55.362  1.00 34.15 ? 2374 HOH   B O     1 
HETATM 20798 O  O     . HOH   DA 11 .    ? -2.811  69.410  75.390  1.00 34.30 ? 2375 HOH   B O     1 
HETATM 20799 O  O     . HOH   DA 11 .    ? 39.624  38.343  88.528  1.00 31.06 ? 2376 HOH   B O     1 
HETATM 20800 O  O     . HOH   DA 11 .    ? 28.439  64.859  59.220  1.00 39.74 ? 2377 HOH   B O     1 
HETATM 20801 O  O     . HOH   DA 11 .    ? -16.502 52.096  115.511 1.00 42.90 ? 2378 HOH   B O     1 
HETATM 20802 O  O     . HOH   DA 11 .    ? 40.500  30.283  90.076  1.00 24.85 ? 2379 HOH   B O     1 
HETATM 20803 O  O     . HOH   DA 11 .    ? -6.888  8.220   116.158 1.00 26.21 ? 2380 HOH   B O     1 
HETATM 20804 O  O     . HOH   DA 11 .    ? 7.111   19.383  97.200  1.00 35.65 ? 2381 HOH   B O     1 
HETATM 20805 O  O     . HOH   DA 11 .    ? 4.837   67.127  63.778  1.00 40.60 ? 2382 HOH   B O     1 
HETATM 20806 O  O     . HOH   DA 11 .    ? 11.682  26.948  119.047 1.00 44.17 ? 2383 HOH   B O     1 
HETATM 20807 O  O     . HOH   DA 11 .    ? 32.737  58.780  67.151  1.00 28.04 ? 2384 HOH   B O     1 
HETATM 20808 O  O     . HOH   DA 11 .    ? 33.039  40.408  61.245  1.00 36.45 ? 2385 HOH   B O     1 
HETATM 20809 O  O     . HOH   DA 11 .    ? 21.231  6.300   73.110  1.00 35.49 ? 2386 HOH   B O     1 
HETATM 20810 O  O     . HOH   DA 11 .    ? 38.931  26.649  91.892  1.00 36.47 ? 2387 HOH   B O     1 
HETATM 20811 O  O     . HOH   DA 11 .    ? 9.493   19.183  98.496  1.00 32.16 ? 2388 HOH   B O     1 
HETATM 20812 O  O     . HOH   DA 11 .    ? 6.746   30.981  90.193  1.00 38.47 ? 2389 HOH   B O     1 
HETATM 20813 O  O     . HOH   DA 11 .    ? 21.644  14.672  100.781 1.00 38.83 ? 2390 HOH   B O     1 
HETATM 20814 O  O     . HOH   DA 11 .    ? 4.780   4.562   78.636  1.00 36.16 ? 2391 HOH   B O     1 
HETATM 20815 O  O     . HOH   DA 11 .    ? 14.046  52.082  63.374  1.00 28.13 ? 2392 HOH   B O     1 
HETATM 20816 O  O     . HOH   DA 11 .    ? 30.683  32.142  83.389  1.00 32.89 ? 2393 HOH   B O     1 
HETATM 20817 O  O     . HOH   DA 11 .    ? 2.157   4.002   81.834  1.00 34.87 ? 2394 HOH   B O     1 
HETATM 20818 O  O     . HOH   DA 11 .    ? -6.776  2.880   84.705  1.00 33.33 ? 2395 HOH   B O     1 
HETATM 20819 O  O     . HOH   DA 11 .    ? 4.627   43.472  50.864  1.00 28.63 ? 2396 HOH   B O     1 
HETATM 20820 O  O     . HOH   DA 11 .    ? 29.690  73.344  72.305  1.00 32.59 ? 2397 HOH   B O     1 
HETATM 20821 O  O     . HOH   DA 11 .    ? 11.990  -1.692  112.811 1.00 46.26 ? 2398 HOH   B O     1 
HETATM 20822 O  O     . HOH   DA 11 .    ? 5.170   44.656  53.521  1.00 29.10 ? 2399 HOH   B O     1 
HETATM 20823 O  O     . HOH   DA 11 .    ? 32.852  35.228  72.173  1.00 32.26 ? 2400 HOH   B O     1 
HETATM 20824 O  O     . HOH   DA 11 .    ? -13.287 9.599   129.266 1.00 39.36 ? 2401 HOH   B O     1 
HETATM 20825 O  O     . HOH   DA 11 .    ? 7.408   28.157  102.177 1.00 42.62 ? 2402 HOH   B O     1 
HETATM 20826 O  O     . HOH   DA 11 .    ? -2.663  41.382  77.835  1.00 32.60 ? 2403 HOH   B O     1 
HETATM 20827 O  O     . HOH   DA 11 .    ? 13.464  57.514  56.990  1.00 43.88 ? 2404 HOH   B O     1 
HETATM 20828 O  O     . HOH   DA 11 .    ? 32.673  20.968  76.237  1.00 36.06 ? 2405 HOH   B O     1 
HETATM 20829 O  O     . HOH   DA 11 .    ? 33.183  23.044  102.083 1.00 45.62 ? 2406 HOH   B O     1 
HETATM 20830 O  O     . HOH   DA 11 .    ? -7.778  12.652  82.411  1.00 37.34 ? 2407 HOH   B O     1 
HETATM 20831 O  O     . HOH   DA 11 .    ? 15.365  52.666  51.229  1.00 45.79 ? 2408 HOH   B O     1 
HETATM 20832 O  O     . HOH   DA 11 .    ? 19.552  45.551  89.580  1.00 14.73 ? 2409 HOH   B O     1 
HETATM 20833 O  O     . HOH   DA 11 .    ? 3.374   49.532  96.422  1.00 33.73 ? 2410 HOH   B O     1 
HETATM 20834 O  O     . HOH   DA 11 .    ? 23.511  68.778  62.022  1.00 30.03 ? 2411 HOH   B O     1 
HETATM 20835 O  O     . HOH   DA 11 .    ? 42.583  35.166  93.245  1.00 34.24 ? 2412 HOH   B O     1 
HETATM 20836 O  O     . HOH   DA 11 .    ? 32.758  42.418  66.581  1.00 29.31 ? 2413 HOH   B O     1 
HETATM 20837 O  O     . HOH   DA 11 .    ? 8.598   -3.184  105.455 1.00 37.14 ? 2414 HOH   B O     1 
HETATM 20838 O  O     . HOH   DA 11 .    ? -4.293  63.953  69.572  1.00 38.44 ? 2415 HOH   B O     1 
HETATM 20839 O  O     . HOH   DA 11 .    ? -2.038  26.415  64.454  1.00 29.72 ? 2416 HOH   B O     1 
HETATM 20840 O  O     . HOH   DA 11 .    ? 34.410  38.368  66.613  1.00 40.96 ? 2417 HOH   B O     1 
HETATM 20841 O  O     . HOH   DA 11 .    ? 42.423  32.274  99.233  1.00 35.37 ? 2418 HOH   B O     1 
HETATM 20842 O  O     . HOH   DA 11 .    ? 18.079  7.079   97.902  1.00 35.56 ? 2419 HOH   B O     1 
HETATM 20843 O  O     . HOH   DA 11 .    ? -2.488  51.964  100.728 1.00 27.47 ? 2420 HOH   B O     1 
HETATM 20844 O  O     . HOH   DA 11 .    ? 27.545  51.084  95.518  1.00 34.68 ? 2421 HOH   B O     1 
HETATM 20845 O  O     . HOH   DA 11 .    ? -5.346  51.847  101.882 1.00 38.81 ? 2422 HOH   B O     1 
HETATM 20846 O  O     . HOH   DA 11 .    ? 20.591  68.675  58.171  1.00 37.09 ? 2423 HOH   B O     1 
HETATM 20847 O  O     A HOH   DA 11 .    ? 2.279   62.216  83.312  0.53 20.89 ? 2424 HOH   B O     1 
HETATM 20848 O  O     . HOH   DA 11 .    ? 15.272  4.333   72.484  1.00 38.34 ? 2425 HOH   B O     1 
HETATM 20849 O  O     . HOH   DA 11 .    ? 39.084  41.010  88.950  1.00 31.34 ? 2426 HOH   B O     1 
HETATM 20850 O  O     . HOH   DA 11 .    ? 12.335  7.064   123.656 1.00 45.39 ? 2427 HOH   B O     1 
HETATM 20851 O  O     . HOH   DA 11 .    ? 1.845   43.710  55.660  1.00 32.89 ? 2428 HOH   B O     1 
HETATM 20852 O  O     . HOH   DA 11 .    ? 31.814  32.561  75.117  1.00 27.73 ? 2429 HOH   B O     1 
HETATM 20853 O  O     . HOH   DA 11 .    ? -10.568 30.128  75.936  1.00 33.48 ? 2430 HOH   B O     1 
HETATM 20854 O  O     . HOH   DA 11 .    ? 9.112   64.173  86.710  1.00 38.06 ? 2431 HOH   B O     1 
HETATM 20855 O  O     . HOH   DA 11 .    ? 0.245   18.346  71.862  1.00 31.95 ? 2432 HOH   B O     1 
HETATM 20856 O  O     . HOH   DA 11 .    ? 33.285  15.827  64.696  1.00 39.57 ? 2433 HOH   B O     1 
HETATM 20857 O  O     . HOH   DA 11 .    ? 25.288  68.149  58.804  1.00 39.21 ? 2434 HOH   B O     1 
HETATM 20858 O  O     . HOH   DA 11 .    ? -0.696  3.791   81.147  1.00 41.62 ? 2435 HOH   B O     1 
HETATM 20859 O  O     . HOH   DA 11 .    ? -3.568  48.019  87.598  1.00 37.92 ? 2436 HOH   B O     1 
HETATM 20860 O  O     . HOH   DA 11 .    ? 30.832  58.965  60.460  1.00 33.09 ? 2437 HOH   B O     1 
HETATM 20861 O  O     . HOH   DA 11 .    ? 14.418  55.762  61.660  1.00 37.08 ? 2438 HOH   B O     1 
HETATM 20862 O  O     . HOH   DA 11 .    ? 0.299   4.794   85.755  1.00 29.09 ? 2439 HOH   B O     1 
HETATM 20863 O  O     . HOH   DA 11 .    ? 0.252   24.384  98.820  1.00 35.70 ? 2440 HOH   B O     1 
HETATM 20864 O  O     . HOH   DA 11 .    ? 33.159  41.694  53.746  1.00 43.75 ? 2441 HOH   B O     1 
HETATM 20865 O  O     . HOH   DA 11 .    ? 6.274   23.973  124.654 1.00 36.99 ? 2442 HOH   B O     1 
HETATM 20866 O  O     . HOH   DA 11 .    ? 6.176   60.683  87.692  1.00 33.68 ? 2443 HOH   B O     1 
HETATM 20867 O  O     . HOH   DA 11 .    ? 3.826   30.057  94.041  1.00 33.06 ? 2444 HOH   B O     1 
HETATM 20868 O  O     . HOH   DA 11 .    ? -18.648 17.477  78.058  1.00 45.13 ? 2445 HOH   B O     1 
HETATM 20869 O  O     . HOH   DA 11 .    ? -22.208 26.107  91.736  1.00 38.52 ? 2446 HOH   B O     1 
HETATM 20870 O  O     . HOH   DA 11 .    ? 1.919   24.290  129.454 1.00 39.96 ? 2447 HOH   B O     1 
HETATM 20871 O  O     . HOH   DA 11 .    ? 21.226  18.663  110.671 1.00 35.01 ? 2448 HOH   B O     1 
HETATM 20872 O  O     . HOH   DA 11 .    ? 4.904   31.866  92.585  1.00 34.78 ? 2449 HOH   B O     1 
HETATM 20873 O  O     . HOH   DA 11 .    ? 7.496   25.685  103.443 1.00 40.08 ? 2450 HOH   B O     1 
HETATM 20874 O  O     . HOH   DA 11 .    ? 10.276  74.782  60.482  1.00 42.03 ? 2451 HOH   B O     1 
HETATM 20875 O  O     . HOH   DA 11 .    ? 1.269   14.602  79.487  1.00 28.63 ? 2452 HOH   B O     1 
HETATM 20876 O  O     . HOH   DA 11 .    ? 7.095   49.874  90.076  1.00 37.39 ? 2453 HOH   B O     1 
HETATM 20877 O  O     . HOH   DA 11 .    ? 16.592  26.262  109.505 1.00 24.61 ? 2454 HOH   B O     1 
HETATM 20878 O  O     . HOH   DA 11 .    ? 0.005   19.118  75.693  1.00 39.59 ? 2455 HOH   B O     1 
HETATM 20879 O  O     . HOH   DA 11 .    ? 33.573  55.681  67.029  1.00 40.48 ? 2456 HOH   B O     1 
HETATM 20880 O  O     . HOH   DA 11 .    ? 21.209  11.575  98.764  1.00 39.92 ? 2457 HOH   B O     1 
HETATM 20881 O  O     . HOH   DA 11 .    ? -13.104 -7.965  105.854 1.00 35.89 ? 2458 HOH   B O     1 
HETATM 20882 O  O     . HOH   DA 11 .    ? -7.436  22.548  78.399  1.00 30.13 ? 2459 HOH   B O     1 
HETATM 20883 O  O     . HOH   DA 11 .    ? -16.369 6.825   122.100 1.00 36.67 ? 2460 HOH   B O     1 
HETATM 20884 O  O     . HOH   DA 11 .    ? 21.813  77.977  77.862  1.00 40.84 ? 2461 HOH   B O     1 
HETATM 20885 O  O     . HOH   DA 11 .    ? -2.840  28.485  68.745  1.00 23.42 ? 2462 HOH   B O     1 
HETATM 20886 O  O     . HOH   DA 11 .    ? 30.213  31.041  78.823  1.00 30.59 ? 2463 HOH   B O     1 
HETATM 20887 O  O     . HOH   DA 11 .    ? -21.692 25.821  96.653  1.00 38.53 ? 2464 HOH   B O     1 
HETATM 20888 O  O     . HOH   DA 11 .    ? 26.369  69.092  61.615  1.00 39.11 ? 2465 HOH   B O     1 
HETATM 20889 O  O     . HOH   DA 11 .    ? 25.833  17.536  96.793  1.00 37.20 ? 2466 HOH   B O     1 
HETATM 20890 O  O     . HOH   DA 11 .    ? -8.099  -2.585  117.314 1.00 39.05 ? 2467 HOH   B O     1 
HETATM 20891 O  O     . HOH   DA 11 .    ? -1.678  38.105  132.744 1.00 41.23 ? 2468 HOH   B O     1 
HETATM 20892 O  O     . HOH   DA 11 .    ? -12.140 30.299  81.375  1.00 34.81 ? 2469 HOH   B O     1 
HETATM 20893 O  O     . HOH   DA 11 .    ? -8.089  37.677  79.069  1.00 36.66 ? 2470 HOH   B O     1 
HETATM 20894 O  O     . HOH   DA 11 .    ? 12.110  21.363  98.378  1.00 30.10 ? 2471 HOH   B O     1 
HETATM 20895 O  O     . HOH   DA 11 .    ? 20.586  58.491  52.725  1.00 41.04 ? 2472 HOH   B O     1 
HETATM 20896 O  O     . HOH   DA 11 .    ? 5.622   11.005  75.080  1.00 31.73 ? 2473 HOH   B O     1 
HETATM 20897 O  O     B HOH   DA 11 .    ? -3.822  60.229  84.914  0.47 23.44 ? 2474 HOH   B O     1 
HETATM 20898 O  O     . HOH   DA 11 .    ? 40.605  31.264  84.116  1.00 38.54 ? 2475 HOH   B O     1 
HETATM 20899 O  O     . HOH   DA 11 .    ? 12.557  18.353  91.744  1.00 33.18 ? 2476 HOH   B O     1 
HETATM 20900 O  O     . HOH   DA 11 .    ? 32.447  27.750  74.165  1.00 35.96 ? 2477 HOH   B O     1 
HETATM 20901 O  O     . HOH   DA 11 .    ? -17.947 7.143   92.826  1.00 31.99 ? 2478 HOH   B O     1 
HETATM 20902 O  O     . HOH   DA 11 .    ? 8.467   58.042  94.829  1.00 38.55 ? 2479 HOH   B O     1 
HETATM 20903 O  O     . HOH   DA 11 .    ? 32.756  41.073  58.793  1.00 34.42 ? 2480 HOH   B O     1 
HETATM 20904 O  O     . HOH   DA 11 .    ? -4.150  40.199  60.423  1.00 27.53 ? 2481 HOH   B O     1 
HETATM 20905 O  O     . HOH   DA 11 .    ? 22.232  67.715  84.654  1.00 44.38 ? 2482 HOH   B O     1 
HETATM 20906 O  O     . HOH   DA 11 .    ? 4.684   77.678  82.773  1.00 37.18 ? 2483 HOH   B O     1 
HETATM 20907 O  O     . HOH   DA 11 .    ? 23.867  32.702  115.207 1.00 34.97 ? 2484 HOH   B O     1 
HETATM 20908 O  O     . HOH   DA 11 .    ? -15.513 7.879   124.376 1.00 36.52 ? 2485 HOH   B O     1 
HETATM 20909 O  O     . HOH   DA 11 .    ? 6.264   16.010  91.843  1.00 26.93 ? 2486 HOH   B O     1 
HETATM 20910 O  O     . HOH   DA 11 .    ? 11.630  17.570  89.278  1.00 34.46 ? 2487 HOH   B O     1 
HETATM 20911 O  O     . HOH   DA 11 .    ? 24.836  70.559  65.066  1.00 33.08 ? 2488 HOH   B O     1 
HETATM 20912 O  O     . HOH   DA 11 .    ? 31.617  32.478  80.773  1.00 36.38 ? 2489 HOH   B O     1 
HETATM 20913 O  O     . HOH   DA 11 .    ? 1.640   11.549  76.586  1.00 36.74 ? 2490 HOH   B O     1 
HETATM 20914 O  O     . HOH   DA 11 .    ? 20.220  69.085  85.374  1.00 46.84 ? 2491 HOH   B O     1 
HETATM 20915 O  O     . HOH   DA 11 .    ? 10.184  53.254  88.915  1.00 35.12 ? 2492 HOH   B O     1 
HETATM 20916 O  O     . HOH   DA 11 .    ? -31.624 18.325  84.205  1.00 48.24 ? 2493 HOH   B O     1 
HETATM 20917 O  O     . HOH   DA 11 .    ? -10.711 -6.592  105.540 1.00 29.33 ? 2494 HOH   B O     1 
HETATM 20918 O  O     . HOH   DA 11 .    ? -15.342 7.114   86.307  1.00 36.31 ? 2495 HOH   B O     1 
HETATM 20919 O  O     . HOH   DA 11 .    ? 20.222  23.139  109.592 1.00 31.59 ? 2496 HOH   B O     1 
HETATM 20920 O  O     . HOH   DA 11 .    ? 24.681  55.217  94.793  1.00 38.84 ? 2497 HOH   B O     1 
HETATM 20921 O  O     . HOH   DA 11 .    ? 35.456  29.632  53.594  1.00 42.88 ? 2498 HOH   B O     1 
HETATM 20922 O  O     . HOH   DA 11 .    ? 11.354  0.851   113.467 1.00 37.73 ? 2499 HOH   B O     1 
HETATM 20923 O  O     . HOH   DA 11 .    ? 7.068   2.481   79.725  1.00 39.54 ? 2500 HOH   B O     1 
HETATM 20924 O  O     . HOH   DA 11 .    ? 33.523  47.225  64.743  1.00 41.44 ? 2501 HOH   B O     1 
HETATM 20925 O  O     . HOH   DA 11 .    ? 23.303  71.529  61.435  1.00 38.56 ? 2502 HOH   B O     1 
HETATM 20926 O  O     . HOH   DA 11 .    ? -11.363 -5.399  111.880 1.00 38.51 ? 2503 HOH   B O     1 
HETATM 20927 O  O     . HOH   DA 11 .    ? 4.210   34.559  119.275 1.00 45.99 ? 2504 HOH   B O     1 
HETATM 20928 O  O     . HOH   DA 11 .    ? 30.551  63.366  58.756  1.00 44.25 ? 2505 HOH   B O     1 
HETATM 20929 O  O     . HOH   DA 11 .    ? 35.922  22.516  64.707  1.00 40.31 ? 2506 HOH   B O     1 
HETATM 20930 O  O     . HOH   DA 11 .    ? 1.011   31.592  82.416  1.00 24.44 ? 2507 HOH   B O     1 
HETATM 20931 O  O     . HOH   DA 11 .    ? 14.520  22.095  94.780  1.00 37.78 ? 2508 HOH   B O     1 
HETATM 20932 O  O     . HOH   DA 11 .    ? 14.759  1.966   99.882  1.00 39.27 ? 2509 HOH   B O     1 
HETATM 20933 O  O     . HOH   DA 11 .    ? 0.730   55.742  69.906  1.00 32.97 ? 2510 HOH   B O     1 
HETATM 20934 O  O     . HOH   DA 11 .    ? 13.822  25.164  100.507 1.00 22.45 ? 2511 HOH   B O     1 
HETATM 20935 O  O     . HOH   DA 11 .    ? 1.958   44.707  96.739  1.00 29.38 ? 2512 HOH   B O     1 
HETATM 20936 O  O     . HOH   DA 11 .    ? 6.922   18.913  89.583  1.00 31.26 ? 2513 HOH   B O     1 
HETATM 20937 O  O     . HOH   DA 11 .    ? 1.426   64.752  86.884  1.00 40.24 ? 2514 HOH   B O     1 
HETATM 20938 O  O     . HOH   DA 11 .    ? 14.696  22.225  97.468  1.00 24.21 ? 2515 HOH   B O     1 
HETATM 20939 O  O     . HOH   DA 11 .    ? 22.618  56.908  53.392  1.00 40.73 ? 2516 HOH   B O     1 
HETATM 20940 O  O     . HOH   DA 11 .    ? 21.973  14.388  98.363  1.00 40.47 ? 2517 HOH   B O     1 
HETATM 20941 O  O     . HOH   DA 11 .    ? 14.676  51.281  55.915  1.00 33.17 ? 2518 HOH   B O     1 
HETATM 20942 O  O     . HOH   DA 11 .    ? 11.270  53.534  86.826  1.00 42.01 ? 2519 HOH   B O     1 
HETATM 20943 O  O     . HOH   DA 11 .    ? -16.531 3.833   123.313 1.00 38.70 ? 2520 HOH   B O     1 
HETATM 20944 O  O     . HOH   DA 11 .    ? -32.954 18.209  100.740 1.00 41.19 ? 2521 HOH   B O     1 
HETATM 20945 O  O     . HOH   DA 11 .    ? -4.295  68.576  73.713  1.00 39.05 ? 2522 HOH   B O     1 
HETATM 20946 O  O     . HOH   DA 11 .    ? 11.960  43.914  53.284  1.00 28.32 ? 2523 HOH   B O     1 
HETATM 20947 O  O     . HOH   DA 11 .    ? 3.154   13.363  77.394  1.00 32.20 ? 2524 HOH   B O     1 
HETATM 20948 O  O     . HOH   DA 11 .    ? 10.450  0.835   106.900 1.00 36.73 ? 2525 HOH   B O     1 
HETATM 20949 O  O     . HOH   DA 11 .    ? -8.052  17.441  79.461  1.00 36.19 ? 2526 HOH   B O     1 
HETATM 20950 O  O     . HOH   DA 11 .    ? 19.819  34.210  114.767 1.00 24.89 ? 2527 HOH   B O     1 
HETATM 20951 O  O     . HOH   DA 11 .    ? 34.463  26.502  56.688  1.00 28.19 ? 2528 HOH   B O     1 
HETATM 20952 O  O     . HOH   DA 11 .    ? 18.756  48.475  56.338  1.00 31.01 ? 2529 HOH   B O     1 
HETATM 20953 O  O     . HOH   DA 11 .    ? 9.295   3.997   83.547  1.00 27.13 ? 2530 HOH   B O     1 
HETATM 20954 O  O     . HOH   DA 11 .    ? -2.283  26.134  101.064 1.00 40.36 ? 2531 HOH   B O     1 
HETATM 20955 O  O     . HOH   DA 11 .    ? 11.682  3.827   121.017 1.00 41.14 ? 2532 HOH   B O     1 
HETATM 20956 O  O     . HOH   DA 11 .    ? 13.395  36.581  74.019  1.00 16.74 ? 2533 HOH   B O     1 
HETATM 20957 O  O     . HOH   DA 11 .    ? -19.624 32.010  88.056  1.00 42.61 ? 2534 HOH   B O     1 
HETATM 20958 O  O     . HOH   DA 11 .    ? 4.928   56.058  66.736  1.00 34.46 ? 2535 HOH   B O     1 
HETATM 20959 O  O     . HOH   DA 11 .    ? 16.122  76.903  61.747  1.00 40.13 ? 2536 HOH   B O     1 
HETATM 20960 O  O     . HOH   DA 11 .    ? 6.559   60.954  84.994  1.00 23.51 ? 2537 HOH   B O     1 
HETATM 20961 O  O     . HOH   DA 11 .    ? -13.440 55.409  124.794 1.00 42.63 ? 2538 HOH   B O     1 
HETATM 20962 O  O     . HOH   DA 11 .    ? 15.621  59.713  92.489  1.00 39.01 ? 2539 HOH   B O     1 
HETATM 20963 O  O     . HOH   DA 11 .    ? 20.545  46.605  51.664  1.00 43.73 ? 2540 HOH   B O     1 
HETATM 20964 O  O     . HOH   DA 11 .    ? -5.058  3.375   82.922  1.00 43.18 ? 2541 HOH   B O     1 
HETATM 20965 O  O     . HOH   DA 11 .    ? 6.057   30.544  97.969  1.00 39.60 ? 2542 HOH   B O     1 
HETATM 20966 O  O     . HOH   DA 11 .    ? 18.005  3.732   73.159  1.00 36.11 ? 2543 HOH   B O     1 
HETATM 20967 O  O     . HOH   DA 11 .    ? 8.830   47.900  110.526 1.00 40.56 ? 2544 HOH   B O     1 
HETATM 20968 O  O     . HOH   DA 11 .    ? 5.101   3.322   85.607  1.00 31.62 ? 2545 HOH   B O     1 
HETATM 20969 O  O     . HOH   DA 11 .    ? 11.517  2.630   84.358  1.00 36.45 ? 2546 HOH   B O     1 
HETATM 20970 O  O     . HOH   DA 11 .    ? 34.413  27.683  61.074  1.00 27.14 ? 2547 HOH   B O     1 
HETATM 20971 O  O     . HOH   DA 11 .    ? -0.759  18.656  67.853  1.00 38.75 ? 2548 HOH   B O     1 
HETATM 20972 O  O     . HOH   DA 11 .    ? 21.635  19.850  106.970 1.00 26.21 ? 2549 HOH   B O     1 
HETATM 20973 O  O     . HOH   DA 11 .    ? -16.085 -0.467  98.323  1.00 40.91 ? 2550 HOH   B O     1 
HETATM 20974 O  O     . HOH   DA 11 .    ? 1.982   -7.550  98.613  1.00 39.57 ? 2551 HOH   B O     1 
HETATM 20975 O  O     . HOH   DA 11 .    ? 18.146  9.267   95.538  1.00 33.70 ? 2552 HOH   B O     1 
HETATM 20976 O  O     . HOH   DA 11 .    ? -13.784 17.290  78.386  1.00 39.16 ? 2553 HOH   B O     1 
HETATM 20977 O  O     . HOH   DA 11 .    ? 3.981   55.064  114.662 1.00 44.77 ? 2554 HOH   B O     1 
HETATM 20978 O  O     . HOH   DA 11 .    ? 26.750  24.715  106.113 1.00 40.40 ? 2555 HOH   B O     1 
HETATM 20979 O  O     . HOH   DA 11 .    ? 18.605  78.735  65.187  1.00 39.81 ? 2556 HOH   B O     1 
HETATM 20980 O  O     . HOH   DA 11 .    ? 14.615  44.151  52.709  1.00 32.87 ? 2557 HOH   B O     1 
HETATM 20981 O  O     . HOH   DA 11 .    ? 18.295  3.164   77.524  1.00 37.67 ? 2558 HOH   B O     1 
HETATM 20982 O  O     . HOH   DA 11 .    ? 30.143  64.359  71.104  1.00 36.38 ? 2559 HOH   B O     1 
HETATM 20983 O  O     . HOH   DA 11 .    ? 20.286  67.562  53.796  1.00 43.68 ? 2560 HOH   B O     1 
HETATM 20984 O  O     . HOH   DA 11 .    ? -2.061  19.443  78.180  1.00 38.00 ? 2561 HOH   B O     1 
HETATM 20985 O  O     . HOH   DA 11 .    ? -10.788 33.604  83.585  1.00 41.35 ? 2562 HOH   B O     1 
HETATM 20986 O  O     . HOH   DA 11 .    ? 8.702   64.865  66.020  1.00 30.65 ? 2563 HOH   B O     1 
HETATM 20987 O  O     . HOH   DA 11 .    ? 7.462   28.089  83.552  1.00 36.93 ? 2564 HOH   B O     1 
HETATM 20988 O  O     . HOH   DA 11 .    ? -20.009 3.867   95.603  1.00 42.05 ? 2565 HOH   B O     1 
HETATM 20989 O  O     . HOH   DA 11 .    ? 5.382   30.326  86.403  1.00 37.61 ? 2566 HOH   B O     1 
HETATM 20990 O  O     . HOH   DA 11 .    ? 8.771   24.622  86.753  1.00 37.12 ? 2567 HOH   B O     1 
HETATM 20991 O  O     . HOH   DA 11 .    ? -22.691 24.527  82.168  1.00 43.39 ? 2568 HOH   B O     1 
HETATM 20992 O  O     . HOH   DA 11 .    ? 41.682  37.123  89.794  1.00 28.59 ? 2569 HOH   B O     1 
HETATM 20993 O  O     . HOH   DA 11 .    ? 6.539   63.489  69.051  1.00 38.53 ? 2570 HOH   B O     1 
HETATM 20994 O  O     . HOH   DA 11 .    ? 31.523  69.674  79.980  1.00 32.44 ? 2571 HOH   B O     1 
HETATM 20995 O  O     . HOH   DA 11 .    ? 15.332  73.076  58.316  1.00 38.31 ? 2572 HOH   B O     1 
HETATM 20996 O  O     . HOH   DA 11 .    ? 18.103  4.717   97.244  1.00 43.46 ? 2573 HOH   B O     1 
HETATM 20997 O  O     . HOH   DA 11 .    ? 12.639  55.689  105.248 1.00 30.31 ? 2574 HOH   B O     1 
HETATM 20998 O  O     . HOH   DA 11 .    ? -0.676  80.201  77.126  1.00 42.36 ? 2575 HOH   B O     1 
HETATM 20999 O  O     . HOH   DA 11 .    ? -10.970 47.140  77.068  1.00 35.64 ? 2576 HOH   B O     1 
HETATM 21000 O  O     . HOH   DA 11 .    ? -9.335  -0.138  86.428  1.00 42.22 ? 2577 HOH   B O     1 
HETATM 21001 O  O     . HOH   DA 11 .    ? 23.310  13.875  96.327  1.00 40.66 ? 2578 HOH   B O     1 
HETATM 21002 O  O     . HOH   DA 11 .    ? -7.702  47.251  133.023 1.00 42.20 ? 2579 HOH   B O     1 
HETATM 21003 O  O     . HOH   DA 11 .    ? 30.316  24.081  74.228  1.00 24.50 ? 2580 HOH   B O     1 
HETATM 21004 O  O     . HOH   DA 11 .    ? 26.275  52.355  83.634  1.00 31.37 ? 2581 HOH   B O     1 
HETATM 21005 O  O     . HOH   DA 11 .    ? 4.578   64.163  86.402  1.00 33.99 ? 2582 HOH   B O     1 
HETATM 21006 O  O     . HOH   DA 11 .    ? 11.993  50.721  54.422  1.00 43.95 ? 2583 HOH   B O     1 
HETATM 21007 O  O     . HOH   DA 11 .    ? -8.556  33.716  85.030  1.00 30.71 ? 2584 HOH   B O     1 
HETATM 21008 O  O     . HOH   DA 11 .    ? 14.876  4.774   69.787  1.00 41.85 ? 2585 HOH   B O     1 
HETATM 21009 O  O     . HOH   DA 11 .    ? 12.324  0.584   108.870 1.00 36.39 ? 2586 HOH   B O     1 
HETATM 21010 O  O     . HOH   DA 11 .    ? 22.373  82.168  68.917  1.00 41.11 ? 2587 HOH   B O     1 
HETATM 21011 O  O     . HOH   DA 11 .    ? -19.781 0.922   97.491  1.00 41.44 ? 2588 HOH   B O     1 
HETATM 21012 O  O     . HOH   DA 11 .    ? -7.225  25.128  74.788  1.00 31.77 ? 2589 HOH   B O     1 
HETATM 21013 O  O     . HOH   DA 11 .    ? -0.046  49.773  98.866  1.00 36.79 ? 2590 HOH   B O     1 
HETATM 21014 O  O     . HOH   DA 11 .    ? 15.751  48.795  52.883  1.00 42.76 ? 2591 HOH   B O     1 
HETATM 21015 O  O     . HOH   DA 11 .    ? 12.853  74.862  60.656  1.00 37.22 ? 2592 HOH   B O     1 
HETATM 21016 O  O     . HOH   DA 11 .    ? 10.319  59.908  86.171  1.00 38.32 ? 2593 HOH   B O     1 
HETATM 21017 O  O     . HOH   DA 11 .    ? 41.572  30.545  82.022  1.00 38.28 ? 2594 HOH   B O     1 
HETATM 21018 O  O     . HOH   DA 11 .    ? 11.622  1.739   115.788 1.00 34.97 ? 2595 HOH   B O     1 
HETATM 21019 O  O     . HOH   DA 11 .    ? 9.995   25.721  99.439  1.00 41.83 ? 2596 HOH   B O     1 
HETATM 21020 O  O     . HOH   DA 11 .    ? 13.668  24.739  97.999  1.00 27.67 ? 2597 HOH   B O     1 
HETATM 21021 O  O     . HOH   DA 11 .    ? 7.888   31.316  85.830  1.00 33.68 ? 2598 HOH   B O     1 
HETATM 21022 O  O     . HOH   DA 11 .    ? 19.873  11.060  96.202  1.00 34.38 ? 2599 HOH   B O     1 
HETATM 21023 O  O     . HOH   DA 11 .    ? -6.456  36.245  61.412  1.00 41.51 ? 2600 HOH   B O     1 
HETATM 21024 O  O     . HOH   DA 11 .    ? -8.923  3.864   84.712  1.00 34.62 ? 2601 HOH   B O     1 
HETATM 21025 O  O     . HOH   DA 11 .    ? 14.946  55.906  104.099 1.00 28.19 ? 2602 HOH   B O     1 
HETATM 21026 O  O     . HOH   DA 11 .    ? -9.841  34.957  89.851  1.00 39.93 ? 2603 HOH   B O     1 
HETATM 21027 O  O     . HOH   DA 11 .    ? 2.883   10.251  74.597  1.00 39.36 ? 2604 HOH   B O     1 
HETATM 21028 O  O     . HOH   DA 11 .    ? 22.439  50.467  68.537  1.00 24.87 ? 2605 HOH   B O     1 
HETATM 21029 O  O     . HOH   DA 11 .    ? -5.839  38.379  61.529  1.00 38.12 ? 2606 HOH   B O     1 
HETATM 21030 O  O     . HOH   DA 11 .    ? -7.731  36.995  83.663  1.00 33.85 ? 2607 HOH   B O     1 
HETATM 21031 O  O     . HOH   DA 11 .    ? -16.339 7.939   90.678  1.00 28.64 ? 2608 HOH   B O     1 
HETATM 21032 O  O     . HOH   DA 11 .    ? 5.644   55.844  94.234  1.00 40.04 ? 2609 HOH   B O     1 
HETATM 21033 O  O     . HOH   DA 11 .    ? 32.313  60.089  62.463  1.00 32.08 ? 2610 HOH   B O     1 
HETATM 21034 O  O     . HOH   DA 11 .    ? 12.758  59.676  85.487  1.00 38.29 ? 2611 HOH   B O     1 
HETATM 21035 O  O     . HOH   DA 11 .    ? -25.434 13.131  86.503  1.00 33.86 ? 2612 HOH   B O     1 
HETATM 21036 O  O     . HOH   DA 11 .    ? 3.471   47.923  89.085  1.00 32.12 ? 2613 HOH   B O     1 
HETATM 21037 O  O     . HOH   DA 11 .    ? 14.769  7.092   91.694  1.00 36.90 ? 2614 HOH   B O     1 
HETATM 21038 O  O     . HOH   DA 11 .    ? 14.183  52.027  60.804  1.00 40.92 ? 2615 HOH   B O     1 
HETATM 21039 O  O     . HOH   DA 11 .    ? 27.216  55.010  83.271  1.00 36.21 ? 2616 HOH   B O     1 
HETATM 21040 O  O     . HOH   DA 11 .    ? 8.953   -4.842  116.879 1.00 45.04 ? 2617 HOH   B O     1 
HETATM 21041 O  O     . HOH   DA 11 .    ? 8.838   44.598  50.071  1.00 38.50 ? 2618 HOH   B O     1 
HETATM 21042 O  O     . HOH   DA 11 .    ? -16.609 -8.264  106.090 1.00 32.75 ? 2619 HOH   B O     1 
HETATM 21043 O  O     . HOH   DA 11 .    ? -3.089  37.944  77.752  1.00 29.98 ? 2620 HOH   B O     1 
HETATM 21044 O  O     . HOH   DA 11 .    ? 8.076   52.778  112.988 1.00 47.38 ? 2621 HOH   B O     1 
HETATM 21045 O  O     . HOH   DA 11 .    ? 34.965  38.687  64.289  1.00 37.05 ? 2622 HOH   B O     1 
HETATM 21046 O  O     . HOH   DA 11 .    ? -4.306  23.481  72.300  1.00 40.91 ? 2623 HOH   B O     1 
HETATM 21047 O  O     . HOH   DA 11 .    ? -11.129 3.949   86.674  1.00 32.31 ? 2624 HOH   B O     1 
HETATM 21048 O  O     . HOH   DA 11 .    ? -0.372  57.048  67.615  1.00 33.81 ? 2625 HOH   B O     1 
HETATM 21049 O  O     . HOH   DA 11 .    ? 24.015  76.473  78.470  1.00 42.23 ? 2626 HOH   B O     1 
HETATM 21050 O  O     . HOH   DA 11 .    ? -5.754  34.108  61.806  1.00 41.66 ? 2627 HOH   B O     1 
HETATM 21051 O  O     . HOH   DA 11 .    ? -0.132  28.923  96.425  1.00 22.56 ? 2628 HOH   B O     1 
HETATM 21052 O  O     . HOH   DA 11 .    ? 9.317   17.238  89.690  1.00 29.63 ? 2629 HOH   B O     1 
HETATM 21053 O  O     . HOH   DA 11 .    ? 6.247   12.080  72.726  1.00 35.28 ? 2630 HOH   B O     1 
HETATM 21054 O  O     . HOH   DA 11 .    ? -5.186  -0.581  84.082  1.00 40.88 ? 2631 HOH   B O     1 
HETATM 21055 O  O     . HOH   DA 11 .    ? 33.416  19.574  53.980  1.00 32.09 ? 2632 HOH   B O     1 
HETATM 21056 O  O     . HOH   DA 11 .    ? 21.945  5.025   70.560  1.00 40.06 ? 2633 HOH   B O     1 
HETATM 21057 O  O     . HOH   DA 11 .    ? 6.215   -4.690  101.683 1.00 38.07 ? 2634 HOH   B O     1 
HETATM 21058 O  O     . HOH   DA 11 .    ? -23.491 14.366  82.086  1.00 30.17 ? 2635 HOH   B O     1 
HETATM 21059 O  O     . HOH   DA 11 .    ? -13.010 -0.170  121.200 1.00 40.23 ? 2636 HOH   B O     1 
HETATM 21060 O  O     . HOH   DA 11 .    ? -18.401 22.294  80.503  1.00 38.62 ? 2637 HOH   B O     1 
HETATM 21061 O  O     . HOH   DA 11 .    ? -11.637 2.086   88.643  1.00 35.11 ? 2638 HOH   B O     1 
HETATM 21062 O  O     . HOH   DA 11 .    ? -21.246 16.662  79.840  1.00 37.86 ? 2639 HOH   B O     1 
HETATM 21063 O  O     . HOH   DA 11 .    ? 3.119   15.143  75.295  1.00 29.55 ? 2640 HOH   B O     1 
HETATM 21064 O  O     . HOH   DA 11 .    ? 0.529   19.972  64.386  1.00 36.88 ? 2641 HOH   B O     1 
HETATM 21065 O  O     . HOH   DA 11 .    ? 5.339   31.768  52.139  1.00 34.13 ? 2642 HOH   B O     1 
HETATM 21066 O  O     . HOH   DA 11 .    ? 36.063  28.596  56.058  1.00 41.67 ? 2643 HOH   B O     1 
HETATM 21067 O  O     . HOH   DA 11 .    ? 1.707   44.350  78.482  1.00 26.06 ? 2644 HOH   B O     1 
HETATM 21068 O  O     . HOH   DA 11 .    ? 28.582  51.187  83.720  1.00 42.51 ? 2645 HOH   B O     1 
HETATM 21069 O  O     . HOH   DA 11 .    ? -7.235  -5.038  91.362  1.00 38.56 ? 2646 HOH   B O     1 
HETATM 21070 O  O     . HOH   DA 11 .    ? -1.368  23.381  63.767  1.00 29.85 ? 2647 HOH   B O     1 
HETATM 21071 O  O     . HOH   DA 11 .    ? 13.763  44.629  49.316  1.00 38.98 ? 2648 HOH   B O     1 
HETATM 21072 O  O     . HOH   DA 11 .    ? 11.402  0.629   86.557  1.00 41.17 ? 2649 HOH   B O     1 
HETATM 21073 O  O     . HOH   DA 11 .    ? 2.004   22.012  60.919  1.00 30.00 ? 2650 HOH   B O     1 
HETATM 21074 O  O     . HOH   DA 11 .    ? -6.618  17.878  77.702  1.00 37.12 ? 2651 HOH   B O     1 
HETATM 21075 O  O     . HOH   DA 11 .    ? 9.420   10.247  67.799  1.00 35.84 ? 2652 HOH   B O     1 
HETATM 21076 O  O     . HOH   DA 11 .    ? 2.108   31.944  84.855  1.00 21.05 ? 2653 HOH   B O     1 
HETATM 21077 O  O     . HOH   DA 11 .    ? -5.673  39.781  75.800  1.00 41.64 ? 2654 HOH   B O     1 
HETATM 21078 O  O     . HOH   DA 11 .    ? 14.409  1.383   90.526  1.00 44.17 ? 2655 HOH   B O     1 
HETATM 21079 O  O     . HOH   DA 11 .    ? 41.034  27.930  91.103  1.00 38.65 ? 2656 HOH   B O     1 
HETATM 21080 O  O     . HOH   DA 11 .    ? -7.951  38.989  59.209  1.00 44.42 ? 2657 HOH   B O     1 
HETATM 21081 O  O     . HOH   DA 11 .    ? -8.630  35.391  87.264  1.00 39.58 ? 2658 HOH   B O     1 
HETATM 21082 O  O     . HOH   DA 11 .    ? -19.486 20.303  78.611  1.00 40.36 ? 2659 HOH   B O     1 
HETATM 21083 O  O     . HOH   DA 11 .    ? 32.350  25.348  50.735  1.00 37.37 ? 2660 HOH   B O     1 
HETATM 21084 O  O     . HOH   DA 11 .    ? 10.500  1.700   121.457 1.00 43.44 ? 2661 HOH   B O     1 
HETATM 21085 O  O     . HOH   DA 11 .    ? 22.176  31.362  45.198  1.00 37.81 ? 2662 HOH   B O     1 
HETATM 21086 O  O     . HOH   DA 11 .    ? -4.942  23.724  74.948  1.00 27.87 ? 2663 HOH   B O     1 
HETATM 21087 O  O     . HOH   DA 11 .    ? 5.820   1.599   81.848  1.00 42.78 ? 2664 HOH   B O     1 
HETATM 21088 O  O     . HOH   DA 11 .    ? 8.572   31.061  49.534  1.00 41.65 ? 2665 HOH   B O     1 
HETATM 21089 O  O     . HOH   DA 11 .    ? -9.584  -2.832  85.616  1.00 44.34 ? 2666 HOH   B O     1 
HETATM 21090 O  O     . HOH   DA 11 .    ? 11.130  60.308  92.340  1.00 37.50 ? 2667 HOH   B O     1 
HETATM 21091 O  O     . HOH   DA 11 .    ? -2.597  23.436  61.364  1.00 38.96 ? 2668 HOH   B O     1 
HETATM 21092 O  O     . HOH   DA 11 .    ? 19.370  31.887  45.204  1.00 38.79 ? 2669 HOH   B O     1 
HETATM 21093 O  O     . HOH   DA 11 .    ? 33.519  43.938  58.883  1.00 43.84 ? 2670 HOH   B O     1 
HETATM 21094 O  O     . HOH   DA 11 .    ? 32.824  23.169  74.728  1.00 37.81 ? 2671 HOH   B O     1 
HETATM 21095 O  O     . HOH   DA 11 .    ? -5.370  21.375  76.456  1.00 35.29 ? 2672 HOH   B O     1 
HETATM 21096 O  O     . HOH   DA 11 .    ? 22.727  29.324  43.852  1.00 40.25 ? 2673 HOH   B O     1 
HETATM 21097 O  O     . HOH   DA 11 .    ? -24.964 13.036  83.796  1.00 33.92 ? 2674 HOH   B O     1 
HETATM 21098 O  O     . HOH   DA 11 .    ? 6.929   2.144   84.113  1.00 34.17 ? 2675 HOH   B O     1 
HETATM 21099 O  O     . HOH   DA 11 .    ? 0.699   27.500  98.649  1.00 36.14 ? 2676 HOH   B O     1 
HETATM 21100 O  O     . HOH   DA 11 .    ? -20.479 24.193  80.383  1.00 40.15 ? 2677 HOH   B O     1 
HETATM 21101 O  O     . HOH   DA 11 .    ? 32.626  62.570  61.493  1.00 40.32 ? 2678 HOH   B O     1 
HETATM 21102 O  O     . HOH   DA 11 .    ? -16.023 5.824   89.031  1.00 37.90 ? 2679 HOH   B O     1 
HETATM 21103 O  O     . HOH   DA 11 .    ? -24.611 10.892  82.920  1.00 42.97 ? 2680 HOH   B O     1 
HETATM 21104 O  O     . HOH   DA 11 .    ? 18.008  1.925   75.190  1.00 44.51 ? 2681 HOH   B O     1 
HETATM 21105 O  O     . HOH   DA 11 .    ? -16.847 23.873  78.419  1.00 46.44 ? 2682 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   ? 0.5392 0.5862 0.6197 0.0886  -0.0095 -0.1110 14   ALA A N   
2     C CA  . ALA A 16   ? 0.5346 0.5798 0.6065 0.0851  -0.0073 -0.1045 14   ALA A CA  
3     C C   . ALA A 16   ? 0.5205 0.5722 0.5840 0.0839  -0.0026 -0.0984 14   ALA A C   
4     O O   . ALA A 16   ? 0.4716 0.5342 0.5326 0.0870  -0.0004 -0.1015 14   ALA A O   
5     C CB  . ALA A 16   ? 0.5540 0.6033 0.6230 0.0867  -0.0081 -0.1097 14   ALA A CB  
6     N N   . PRO A 17   ? 0.5084 0.5539 0.5678 0.0796  -0.0010 -0.0898 15   PRO A N   
7     C CA  . PRO A 17   ? 0.4304 0.4814 0.4824 0.0782  0.0032  -0.0837 15   PRO A CA  
8     C C   . PRO A 17   ? 0.4460 0.5065 0.4904 0.0795  0.0057  -0.0847 15   PRO A C   
9     O O   . PRO A 17   ? 0.3825 0.4418 0.4251 0.0793  0.0045  -0.0867 15   PRO A O   
10    C CB  . PRO A 17   ? 0.4564 0.4976 0.5065 0.0733  0.0035  -0.0753 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.5114 0.5441 0.5651 0.0720  0.0001  -0.0770 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.4683 0.5017 0.5300 0.0757  -0.0032 -0.0853 15   PRO A CD  
13    N N   . ALA A 18   ? 0.3690 0.4394 0.4092 0.0807  0.0090  -0.0831 16   ALA A N   
14    C CA  . ALA A 18   ? 0.3451 0.4260 0.3785 0.0821  0.0114  -0.0838 16   ALA A CA  
15    C C   . ALA A 18   ? 0.3099 0.3862 0.3371 0.0782  0.0125  -0.0771 16   ALA A C   
16    O O   . ALA A 18   ? 0.2974 0.3661 0.3241 0.0746  0.0131  -0.0703 16   ALA A O   
17    C CB  . ALA A 18   ? 0.3975 0.4897 0.4281 0.0837  0.0148  -0.0821 16   ALA A CB  
18    N N   . PRO A 19   ? 0.2869 0.3680 0.3096 0.0790  0.0127  -0.0790 17   PRO A N   
19    C CA  . PRO A 19   ? 0.2800 0.3566 0.2974 0.0755  0.0135  -0.0730 17   PRO A CA  
20    C C   . PRO A 19   ? 0.2670 0.3464 0.2796 0.0731  0.0170  -0.0649 17   PRO A C   
21    O O   . PRO A 19   ? 0.3164 0.4064 0.3264 0.0749  0.0195  -0.0644 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3227 0.4067 0.3365 0.0777  0.0133  -0.0776 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.3410 0.4290 0.3602 0.0819  0.0110  -0.0869 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.3036 0.3939 0.3265 0.0832  0.0118  -0.0872 17   PRO A CD  
25    N N   . PHE A 20   ? 0.2501 0.3201 0.2619 0.0691  0.0171  -0.0585 18   PHE A N   
26    C CA  . PHE A 20   ? 0.2791 0.3498 0.2870 0.0664  0.0199  -0.0505 18   PHE A CA  
27    C C   . PHE A 20   ? 0.2899 0.3635 0.2999 0.0667  0.0214  -0.0483 18   PHE A C   
28    O O   . PHE A 20   ? 0.2964 0.3728 0.3035 0.0650  0.0239  -0.0422 18   PHE A O   
29    C CB  . PHE A 20   ? 0.2656 0.3450 0.2672 0.0665  0.0220  -0.0482 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.2628 0.3394 0.2620 0.0660  0.0206  -0.0497 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2646 0.3319 0.2627 0.0624  0.0200  -0.0452 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.2697 0.3534 0.2679 0.0691  0.0198  -0.0559 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.2698 0.3347 0.2659 0.0619  0.0188  -0.0465 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.2999 0.3811 0.2959 0.0686  0.0184  -0.0573 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.3129 0.3846 0.3079 0.0649  0.0179  -0.0525 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.2908 0.3639 0.3063 0.0689  0.0200  -0.0531 19   ALA A N   
37    C CA  . ALA A 21   ? 0.2819 0.3577 0.2998 0.0693  0.0214  -0.0512 19   ALA A CA  
38    C C   . ALA A 21   ? 0.3564 0.4231 0.3751 0.0654  0.0216  -0.0444 19   ALA A C   
39    O O   . ALA A 21   ? 0.3491 0.4185 0.3683 0.0649  0.0233  -0.0408 19   ALA A O   
40    C CB  . ALA A 21   ? 0.3243 0.4013 0.3484 0.0726  0.0194  -0.0583 19   ALA A CB  
41    N N   . ASP A 22   ? 0.2871 0.3437 0.3061 0.0627  0.0198  -0.0427 20   ASP A N   
42    C CA  . ASP A 22   ? 0.3327 0.3809 0.3522 0.0590  0.0198  -0.0367 20   ASP A CA  
43    C C   . ASP A 22   ? 0.2464 0.2905 0.2614 0.0560  0.0202  -0.0324 20   ASP A C   
44    O O   . ASP A 22   ? 0.2852 0.3204 0.3012 0.0532  0.0189  -0.0297 20   ASP A O   
45    C CB  . ASP A 22   ? 0.3725 0.4119 0.3979 0.0585  0.0169  -0.0386 20   ASP A CB  
46    C CG  . ASP A 22   ? 0.5274 0.5700 0.5580 0.0613  0.0164  -0.0423 20   ASP A CG  
47    O OD1 . ASP A 22   ? 0.5664 0.6174 0.5959 0.0629  0.0186  -0.0420 20   ASP A OD1 
48    O OD2 . ASP A 22   ? 0.6636 0.7006 0.6999 0.0618  0.0136  -0.0455 20   ASP A OD2 
49    N N   . PHE A 23   ? 0.2216 0.2726 0.2319 0.0566  0.0219  -0.0317 21   PHE A N   
50    C CA  . PHE A 23   ? 0.2161 0.2635 0.2226 0.0543  0.0219  -0.0288 21   PHE A CA  
51    C C   . PHE A 23   ? 0.2259 0.2672 0.2316 0.0506  0.0226  -0.0221 21   PHE A C   
52    O O   . PHE A 23   ? 0.2399 0.2730 0.2458 0.0482  0.0212  -0.0208 21   PHE A O   
53    C CB  . PHE A 23   ? 0.2271 0.2836 0.2289 0.0556  0.0236  -0.0287 21   PHE A CB  
54    C CG  . PHE A 23   ? 0.2130 0.2662 0.2111 0.0532  0.0238  -0.0251 21   PHE A CG  
55    C CD1 . PHE A 23   ? 0.2385 0.2848 0.2369 0.0523  0.0216  -0.0274 21   PHE A CD1 
56    C CD2 . PHE A 23   ? 0.2240 0.2809 0.2188 0.0516  0.0259  -0.0194 21   PHE A CD2 
57    C CE1 . PHE A 23   ? 0.2494 0.2927 0.2446 0.0501  0.0217  -0.0242 21   PHE A CE1 
58    C CE2 . PHE A 23   ? 0.2432 0.2969 0.2352 0.0494  0.0259  -0.0162 21   PHE A CE2 
59    C CZ  . PHE A 23   ? 0.2560 0.3029 0.2481 0.0487  0.0238  -0.0188 21   PHE A CZ  
60    N N   . ALA A 24   ? 0.2227 0.2684 0.2277 0.0500  0.0248  -0.0179 22   ALA A N   
61    C CA  . ALA A 24   ? 0.2295 0.2702 0.2339 0.0467  0.0254  -0.0119 22   ALA A CA  
62    C C   . ALA A 24   ? 0.2310 0.2755 0.2369 0.0465  0.0271  -0.0085 22   ALA A C   
63    O O   . ALA A 24   ? 0.2246 0.2721 0.2287 0.0451  0.0288  -0.0037 22   ALA A O   
64    C CB  . ALA A 24   ? 0.2635 0.3052 0.2638 0.0452  0.0263  -0.0086 22   ALA A CB  
65    N N   . PRO A 25   ? 0.2522 0.2966 0.2619 0.0478  0.0266  -0.0108 23   PRO A N   
66    C CA  . PRO A 25   ? 0.2737 0.3222 0.2850 0.0477  0.0282  -0.0077 23   PRO A CA  
67    C C   . PRO A 25   ? 0.2545 0.2971 0.2660 0.0443  0.0283  -0.0020 23   PRO A C   
68    O O   . PRO A 25   ? 0.2509 0.2850 0.2631 0.0423  0.0267  -0.0017 23   PRO A O   
69    C CB  . PRO A 25   ? 0.2851 0.3324 0.3009 0.0496  0.0269  -0.0118 23   PRO A CB  
70    C CG  . PRO A 25   ? 0.2844 0.3231 0.3015 0.0489  0.0243  -0.0146 23   PRO A CG  
71    C CD  . PRO A 25   ? 0.2698 0.3091 0.2830 0.0489  0.0242  -0.0156 23   PRO A CD  
72    N N   . PRO A 26   ? 0.2426 0.2898 0.2537 0.0434  0.0302  0.0026  24   PRO A N   
73    C CA  . PRO A 26   ? 0.2438 0.2856 0.2555 0.0402  0.0302  0.0076  24   PRO A CA  
74    C C   . PRO A 26   ? 0.2281 0.2648 0.2436 0.0395  0.0291  0.0073  24   PRO A C   
75    O O   . PRO A 26   ? 0.2446 0.2834 0.2625 0.0415  0.0288  0.0044  24   PRO A O   
76    C CB  . PRO A 26   ? 0.2689 0.3182 0.2803 0.0399  0.0324  0.0121  24   PRO A CB  
77    C CG  . PRO A 26   ? 0.3293 0.3878 0.3410 0.0431  0.0336  0.0093  24   PRO A CG  
78    C CD  . PRO A 26   ? 0.2557 0.3137 0.2660 0.0453  0.0324  0.0034  24   PRO A CD  
79    N N   . VAL A 27   ? 0.2274 0.2574 0.2433 0.0366  0.0283  0.0104  25   VAL A N   
80    C CA  . VAL A 27   ? 0.2419 0.2672 0.2611 0.0355  0.0272  0.0110  25   VAL A CA  
81    C C   . VAL A 27   ? 0.2603 0.2912 0.2822 0.0366  0.0285  0.0122  25   VAL A C   
82    O O   . VAL A 27   ? 0.2650 0.2950 0.2899 0.0376  0.0277  0.0103  25   VAL A O   
83    C CB  . VAL A 27   ? 0.2352 0.2543 0.2541 0.0323  0.0265  0.0145  25   VAL A CB  
84    C CG1 . VAL A 27   ? 0.2698 0.2857 0.2920 0.0312  0.0256  0.0157  25   VAL A CG1 
85    C CG2 . VAL A 27   ? 0.2526 0.2660 0.2693 0.0313  0.0251  0.0129  25   VAL A CG2 
86    N N   . ARG A 28   ? 0.2615 0.2985 0.2827 0.0365  0.0303  0.0154  26   ARG A N   
87    C CA  . ARG A 28   ? 0.2671 0.3103 0.2909 0.0374  0.0317  0.0171  26   ARG A CA  
88    C C   . ARG A 28   ? 0.3089 0.3613 0.3309 0.0385  0.0338  0.0189  26   ARG A C   
89    O O   . ARG A 28   ? 0.2659 0.3185 0.2849 0.0378  0.0341  0.0200  26   ARG A O   
90    C CB  . ARG A 28   ? 0.3162 0.3560 0.3425 0.0347  0.0315  0.0215  26   ARG A CB  
91    C CG  . ARG A 28   ? 0.3217 0.3611 0.3467 0.0324  0.0321  0.0259  26   ARG A CG  
92    C CD  . ARG A 28   ? 0.3270 0.3618 0.3548 0.0297  0.0313  0.0292  26   ARG A CD  
93    N NE  . ARG A 28   ? 0.3706 0.3970 0.3979 0.0283  0.0293  0.0276  26   ARG A NE  
94    C CZ  . ARG A 28   ? 0.4188 0.4416 0.4480 0.0283  0.0281  0.0259  26   ARG A CZ  
95    N NH1 . ARG A 28   ? 0.4105 0.4368 0.4425 0.0298  0.0285  0.0254  26   ARG A NH1 
96    N NH2 . ARG A 28   ? 0.3304 0.3463 0.3588 0.0269  0.0263  0.0248  26   ARG A NH2 
97    N N   . PRO A 29   ? 0.2688 0.3293 0.2926 0.0402  0.0354  0.0192  27   PRO A N   
98    C CA  . PRO A 29   ? 0.2673 0.3375 0.2896 0.0409  0.0375  0.0220  27   PRO A CA  
99    C C   . PRO A 29   ? 0.2629 0.3313 0.2854 0.0379  0.0378  0.0281  27   PRO A C   
100   O O   . PRO A 29   ? 0.2688 0.3322 0.2941 0.0357  0.0371  0.0307  27   PRO A O   
101   C CB  . PRO A 29   ? 0.2903 0.3685 0.3154 0.0428  0.0388  0.0218  27   PRO A CB  
102   C CG  . PRO A 29   ? 0.3055 0.3790 0.3329 0.0442  0.0373  0.0170  27   PRO A CG  
103   C CD  . PRO A 29   ? 0.3009 0.3627 0.3282 0.0416  0.0352  0.0173  27   PRO A CD  
104   N N   . GLN A 30   ? 0.2650 0.3379 0.2850 0.0378  0.0387  0.0302  28   GLN A N   
105   C CA  . GLN A 30   ? 0.2703 0.3409 0.2909 0.0349  0.0386  0.0356  28   GLN A CA  
106   C C   . GLN A 30   ? 0.2892 0.3667 0.3132 0.0342  0.0400  0.0410  28   GLN A C   
107   O O   . GLN A 30   ? 0.2928 0.3805 0.3163 0.0358  0.0418  0.0423  28   GLN A O   
108   C CB  . GLN A 30   ? 0.2661 0.3386 0.2830 0.0351  0.0388  0.0359  28   GLN A CB  
109   C CG  . GLN A 30   ? 0.2370 0.3029 0.2508 0.0358  0.0373  0.0306  28   GLN A CG  
110   C CD  . GLN A 30   ? 0.2626 0.3175 0.2774 0.0333  0.0355  0.0307  28   GLN A CD  
111   O OE1 . GLN A 30   ? 0.2358 0.2873 0.2504 0.0312  0.0350  0.0337  28   GLN A OE1 
112   N NE2 . GLN A 30   ? 0.2422 0.2918 0.2582 0.0336  0.0343  0.0274  28   GLN A NE2 
113   N N   . SER A 31   ? 0.2585 0.3309 0.2862 0.0318  0.0392  0.0442  29   SER A N   
114   C CA  . SER A 31   ? 0.2242 0.3022 0.2559 0.0307  0.0403  0.0496  29   SER A CA  
115   C C   . SER A 31   ? 0.2573 0.3398 0.2890 0.0295  0.0409  0.0548  29   SER A C   
116   O O   . SER A 31   ? 0.2406 0.3204 0.2694 0.0292  0.0404  0.0542  29   SER A O   
117   C CB  . SER A 31   ? 0.2456 0.3161 0.2813 0.0283  0.0389  0.0514  29   SER A CB  
118   O OG  . SER A 31   ? 0.2220 0.2853 0.2576 0.0260  0.0374  0.0528  29   SER A OG  
119   N N   . THR A 32   ? 0.2488 0.3384 0.2842 0.0288  0.0421  0.0602  30   THR A N   
120   C CA  . THR A 32   ? 0.2277 0.3215 0.2646 0.0272  0.0425  0.0662  30   THR A CA  
121   C C   . THR A 32   ? 0.2204 0.3044 0.2584 0.0247  0.0404  0.0674  30   THR A C   
122   O O   . THR A 32   ? 0.2324 0.3165 0.2687 0.0242  0.0401  0.0689  30   THR A O   
123   C CB  . THR A 32   ? 0.2536 0.3550 0.2957 0.0263  0.0436  0.0722  30   THR A CB  
124   O OG1 . THR A 32   ? 0.3262 0.4376 0.3671 0.0289  0.0456  0.0708  30   THR A OG1 
125   C CG2 . THR A 32   ? 0.3026 0.4086 0.3469 0.0246  0.0437  0.0790  30   THR A CG2 
126   N N   . LEU A 33   ? 0.2033 0.2788 0.2440 0.0231  0.0389  0.0665  31   LEU A N   
127   C CA  . LEU A 33   ? 0.1972 0.2639 0.2393 0.0208  0.0369  0.0671  31   LEU A CA  
128   C C   . LEU A 33   ? 0.2138 0.2749 0.2506 0.0215  0.0361  0.0623  31   LEU A C   
129   O O   . LEU A 33   ? 0.2138 0.2714 0.2504 0.0203  0.0351  0.0635  31   LEU A O   
130   C CB  . LEU A 33   ? 0.2118 0.2718 0.2579 0.0192  0.0354  0.0668  31   LEU A CB  
131   C CG  . LEU A 33   ? 0.2333 0.2974 0.2859 0.0176  0.0356  0.0725  31   LEU A CG  
132   C CD1 . LEU A 33   ? 0.2371 0.2959 0.2931 0.0166  0.0344  0.0712  31   LEU A CD1 
133   C CD2 . LEU A 33   ? 0.3038 0.3676 0.3602 0.0155  0.0346  0.0775  31   LEU A CD2 
134   N N   . ARG A 34   ? 0.1982 0.2583 0.2313 0.0235  0.0364  0.0570  32   ARG A N   
135   C CA  . ARG A 34   ? 0.2039 0.2591 0.2323 0.0242  0.0356  0.0526  32   ARG A CA  
136   C C   . ARG A 34   ? 0.1949 0.2561 0.2202 0.0253  0.0366  0.0536  32   ARG A C   
137   O O   . ARG A 34   ? 0.2080 0.2652 0.2311 0.0247  0.0357  0.0528  32   ARG A O   
138   C CB  . ARG A 34   ? 0.2198 0.2729 0.2457 0.0261  0.0355  0.0469  32   ARG A CB  
139   C CG  . ARG A 34   ? 0.2290 0.2745 0.2571 0.0248  0.0341  0.0453  32   ARG A CG  
140   C CD  . ARG A 34   ? 0.2156 0.2524 0.2425 0.0231  0.0323  0.0441  32   ARG A CD  
141   N NE  . ARG A 34   ? 0.2307 0.2648 0.2532 0.0243  0.0319  0.0398  32   ARG A NE  
142   C CZ  . ARG A 34   ? 0.2435 0.2735 0.2647 0.0251  0.0310  0.0356  32   ARG A CZ  
143   N NH1 . ARG A 34   ? 0.2484 0.2765 0.2721 0.0248  0.0305  0.0351  32   ARG A NH1 
144   N NH2 . ARG A 34   ? 0.2583 0.2861 0.2761 0.0260  0.0305  0.0322  32   ARG A NH2 
145   N N   . ARG A 35   ? 0.2054 0.2766 0.2305 0.0269  0.0384  0.0554  33   ARG A N   
146   C CA  . ARG A 35   ? 0.2156 0.2938 0.2377 0.0280  0.0394  0.0564  33   ARG A CA  
147   C C   . ARG A 35   ? 0.2073 0.2853 0.2317 0.0258  0.0388  0.0621  33   ARG A C   
148   O O   . ARG A 35   ? 0.2228 0.3017 0.2444 0.0261  0.0387  0.0622  33   ARG A O   
149   C CB  . ARG A 35   ? 0.2560 0.3462 0.2778 0.0301  0.0415  0.0574  33   ARG A CB  
150   C CG  . ARG A 35   ? 0.2578 0.3491 0.2769 0.0329  0.0419  0.0509  33   ARG A CG  
151   C CD  . ARG A 35   ? 0.3008 0.4046 0.3202 0.0351  0.0440  0.0517  33   ARG A CD  
152   C CZ  . ARG A 35   ? 0.3946 0.4979 0.4061 0.0418  0.0433  0.0343  33   ARG A CZ  
153   N N   . ALA A 36   ? 0.2168 0.2934 0.2467 0.0236  0.0383  0.0668  34   ALA A N   
154   C CA  . ALA A 36   ? 0.2302 0.3058 0.2635 0.0214  0.0374  0.0721  34   ALA A CA  
155   C C   . ALA A 36   ? 0.2238 0.2894 0.2558 0.0204  0.0355  0.0694  34   ALA A C   
156   O O   . ALA A 36   ? 0.2340 0.2995 0.2663 0.0195  0.0349  0.0718  34   ALA A O   
157   C CB  . ALA A 36   ? 0.2349 0.3106 0.2751 0.0193  0.0370  0.0772  34   ALA A CB  
158   N N   . ILE A 37   ? 0.1874 0.2452 0.2181 0.0204  0.0346  0.0643  35   ILE A N   
159   C CA  . ILE A 37   ? 0.1800 0.2293 0.2088 0.0196  0.0329  0.0611  35   ILE A CA  
160   C C   . ILE A 37   ? 0.1889 0.2402 0.2123 0.0212  0.0334  0.0586  35   ILE A C   
161   O O   . ILE A 37   ? 0.2002 0.2496 0.2231 0.0205  0.0326  0.0597  35   ILE A O   
162   C CB  . ILE A 37   ? 0.1941 0.2359 0.2222 0.0195  0.0320  0.0564  35   ILE A CB  
163   C CG1 . ILE A 37   ? 0.1902 0.2294 0.2239 0.0177  0.0312  0.0589  35   ILE A CG1 
164   C CG2 . ILE A 37   ? 0.1745 0.2087 0.2000 0.0190  0.0306  0.0529  35   ILE A CG2 
165   C CD1 . ILE A 37   ? 0.1979 0.2316 0.2311 0.0177  0.0305  0.0548  35   ILE A CD1 
166   N N   . THR A 38   ? 0.1921 0.2473 0.2116 0.0235  0.0346  0.0550  36   THR A N   
167   C CA  . THR A 38   ? 0.2008 0.2576 0.2153 0.0252  0.0348  0.0519  36   THR A CA  
168   C C   . THR A 38   ? 0.2164 0.2803 0.2306 0.0252  0.0355  0.0563  36   THR A C   
169   O O   . THR A 38   ? 0.2137 0.2764 0.2254 0.0253  0.0349  0.0553  36   THR A O   
170   C CB  . THR A 38   ? 0.2025 0.2632 0.2139 0.0278  0.0358  0.0473  36   THR A CB  
171   O OG1 . THR A 38   ? 0.2099 0.2642 0.2224 0.0275  0.0350  0.0441  36   THR A OG1 
172   C CG2 . THR A 38   ? 0.2324 0.2936 0.2390 0.0294  0.0356  0.0432  36   THR A CG2 
173   N N   . ALA A 39   ? 0.2060 0.2775 0.2233 0.0249  0.0366  0.0614  37   ALA A N   
174   C CA  . ALA A 39   ? 0.2055 0.2849 0.2230 0.0248  0.0372  0.0664  37   ALA A CA  
175   C C   . ALA A 39   ? 0.2346 0.3087 0.2547 0.0227  0.0356  0.0697  37   ALA A C   
176   O O   . ALA A 39   ? 0.2572 0.3359 0.2763 0.0228  0.0357  0.0724  37   ALA A O   
177   C CB  . ALA A 39   ? 0.2261 0.3146 0.2472 0.0247  0.0386  0.0719  37   ALA A CB  
178   N N   . ALA A 40   ? 0.2020 0.2670 0.2257 0.0208  0.0340  0.0693  38   ALA A N   
179   C CA  . ALA A 40   ? 0.2172 0.2769 0.2441 0.0188  0.0323  0.0720  38   ALA A CA  
180   C C   . ALA A 40   ? 0.2108 0.2631 0.2341 0.0190  0.0311  0.0670  38   ALA A C   
181   O O   . ALA A 40   ? 0.2177 0.2656 0.2436 0.0175  0.0296  0.0684  38   ALA A O   
182   C CB  . ALA A 40   ? 0.2160 0.2705 0.2495 0.0166  0.0310  0.0742  38   ALA A CB  
183   N N   . TYR A 41   ? 0.1911 0.2422 0.2091 0.0207  0.0317  0.0613  39   TYR A N   
184   C CA  . TYR A 41   ? 0.2018 0.2453 0.2168 0.0207  0.0305  0.0563  39   TYR A CA  
185   C C   . TYR A 41   ? 0.2105 0.2530 0.2253 0.0201  0.0296  0.0579  39   TYR A C   
186   O O   . TYR A 41   ? 0.2074 0.2428 0.2238 0.0187  0.0281  0.0569  39   TYR A O   
187   C CB  . TYR A 41   ? 0.1897 0.2347 0.1993 0.0229  0.0313  0.0510  39   TYR A CB  
188   C CG  . TYR A 41   ? 0.1972 0.2341 0.2044 0.0229  0.0303  0.0454  39   TYR A CG  
189   C CD1 . TYR A 41   ? 0.1958 0.2261 0.2035 0.0215  0.0288  0.0448  39   TYR A CD1 
190   C CD2 . TYR A 41   ? 0.2090 0.2453 0.2137 0.0244  0.0306  0.0409  39   TYR A CD2 
191   C CE1 . TYR A 41   ? 0.1954 0.2192 0.2008 0.0215  0.0279  0.0400  39   TYR A CE1 
192   C CE2 . TYR A 41   ? 0.2274 0.2569 0.2303 0.0243  0.0295  0.0364  39   TYR A CE2 
193   C CZ  . TYR A 41   ? 0.2071 0.2306 0.2102 0.0228  0.0283  0.0361  39   TYR A CZ  
194   O OH  . TYR A 41   ? 0.2098 0.2272 0.2111 0.0226  0.0273  0.0320  39   TYR A OH  
195   N N   . ARG A 42   ? 0.2082 0.2583 0.2212 0.0211  0.0304  0.0603  40   ARG A N   
196   C CA  . ARG A 42   ? 0.2302 0.2801 0.2429 0.0207  0.0296  0.0619  40   ARG A CA  
197   C C   . ARG A 42   ? 0.2101 0.2676 0.2263 0.0201  0.0299  0.0690  40   ARG A C   
198   O O   . ARG A 42   ? 0.2565 0.3185 0.2710 0.0206  0.0299  0.0709  40   ARG A O   
199   C CB  . ARG A 42   ? 0.2556 0.3066 0.2621 0.0225  0.0298  0.0574  40   ARG A CB  
200   C CG  . ARG A 42   ? 0.2434 0.2863 0.2477 0.0227  0.0291  0.0512  40   ARG A CG  
201   C CD  . ARG A 42   ? 0.2608 0.3047 0.2596 0.0245  0.0293  0.0465  40   ARG A CD  
202   N NE  . ARG A 42   ? 0.2451 0.2827 0.2426 0.0247  0.0289  0.0412  40   ARG A NE  
203   C CZ  . ARG A 42   ? 0.2240 0.2537 0.2217 0.0235  0.0276  0.0388  40   ARG A CZ  
204   N NH1 . ARG A 42   ? 0.2452 0.2722 0.2440 0.0224  0.0266  0.0404  40   ARG A NH1 
205   N NH2 . ARG A 42   ? 0.2256 0.2503 0.2226 0.0236  0.0272  0.0349  40   ARG A NH2 
206   N N   . ARG A 43   ? 0.2297 0.2886 0.2510 0.0189  0.0300  0.0731  41   ARG A N   
207   C CA  . ARG A 43   ? 0.2404 0.3068 0.2661 0.0181  0.0302  0.0806  41   ARG A CA  
208   C C   . ARG A 43   ? 0.2503 0.3138 0.2792 0.0167  0.0285  0.0837  41   ARG A C   
209   O O   . ARG A 43   ? 0.2441 0.2986 0.2753 0.0156  0.0268  0.0815  41   ARG A O   
210   C CB  . ARG A 43   ? 0.2583 0.3242 0.2900 0.0166  0.0302  0.0840  41   ARG A CB  
211   C CG  . ARG A 43   ? 0.2332 0.3062 0.2709 0.0153  0.0301  0.0924  41   ARG A CG  
212   C CD  . ARG A 43   ? 0.2689 0.3434 0.3114 0.0144  0.0305  0.0951  41   ARG A CD  
213   N NE  . ARG A 43   ? 0.2525 0.3328 0.2902 0.0163  0.0327  0.0923  41   ARG A NE  
214   C CZ  . ARG A 43   ? 0.2350 0.3144 0.2744 0.0163  0.0333  0.0912  41   ARG A CZ  
215   N NH1 . ARG A 43   ? 0.2570 0.3300 0.3024 0.0143  0.0318  0.0925  41   ARG A NH1 
216   N NH2 . ARG A 43   ? 0.2600 0.3451 0.2950 0.0183  0.0353  0.0885  41   ARG A NH2 
217   N N   . PRO A 44   ? 0.2617 0.3330 0.2910 0.0168  0.0287  0.0888  42   PRO A N   
218   C CA  . PRO A 44   ? 0.2571 0.3260 0.2902 0.0155  0.0269  0.0922  42   PRO A CA  
219   C C   . PRO A 44   ? 0.2127 0.2748 0.2542 0.0133  0.0249  0.0948  42   PRO A C   
220   O O   . PRO A 44   ? 0.2504 0.3138 0.2964 0.0123  0.0251  0.0978  42   PRO A O   
221   C CB  . PRO A 44   ? 0.2583 0.3387 0.2918 0.0158  0.0277  0.0989  42   PRO A CB  
222   C CG  . PRO A 44   ? 0.3035 0.3914 0.3298 0.0181  0.0300  0.0958  42   PRO A CG  
223   C CD  . PRO A 44   ? 0.2734 0.3566 0.2993 0.0183  0.0307  0.0914  42   PRO A CD  
224   N N   . GLU A 45   ? 0.2563 0.3110 0.3000 0.0125  0.0229  0.0932  43   GLU A N   
225   C CA  . GLU A 45   ? 0.2659 0.3134 0.3175 0.0106  0.0208  0.0943  43   GLU A CA  
226   C C   . GLU A 45   ? 0.2627 0.3150 0.3227 0.0090  0.0199  0.1027  43   GLU A C   
227   O O   . GLU A 45   ? 0.2815 0.3305 0.3483 0.0076  0.0188  0.1042  43   GLU A O   
228   C CB  . GLU A 45   ? 0.2716 0.3120 0.3238 0.0103  0.0189  0.0912  43   GLU A CB  
229   C CG  . GLU A 45   ? 0.3048 0.3361 0.3619 0.0091  0.0171  0.0880  43   GLU A CG  
230   C CD  . GLU A 45   ? 0.2714 0.2959 0.3258 0.0096  0.0161  0.0821  43   GLU A CD  
231   O OE1 . GLU A 45   ? 0.2488 0.2747 0.2967 0.0108  0.0169  0.0797  43   GLU A OE1 
232   O OE2 . GLU A 45   ? 0.2429 0.2607 0.3018 0.0086  0.0144  0.0797  43   GLU A OE2 
233   N N   . THR A 46   ? 0.2554 0.3159 0.3156 0.0091  0.0203  0.1084  44   THR A N   
234   C CA  . THR A 46   ? 0.3035 0.3694 0.3720 0.0075  0.0195  0.1172  44   THR A CA  
235   C C   . THR A 46   ? 0.2959 0.3671 0.3658 0.0072  0.0210  0.1199  44   THR A C   
236   O O   . THR A 46   ? 0.3145 0.3875 0.3929 0.0055  0.0199  0.1262  44   THR A O   
237   C CB  . THR A 46   ? 0.2559 0.3306 0.3233 0.0078  0.0198  0.1229  44   THR A CB  
238   O OG1 . THR A 46   ? 0.3185 0.4007 0.3764 0.0099  0.0225  0.1205  44   THR A OG1 
239   C CG2 . THR A 46   ? 0.2822 0.3515 0.3506 0.0077  0.0177  0.1217  44   THR A CG2 
240   N N   . GLU A 47   ? 0.2584 0.3322 0.3205 0.0090  0.0235  0.1153  45   GLU A N   
241   C CA  . GLU A 47   ? 0.2843 0.3631 0.3474 0.0089  0.0250  0.1172  45   GLU A CA  
242   C C   . GLU A 47   ? 0.2644 0.3345 0.3307 0.0081  0.0242  0.1132  45   GLU A C   
243   O O   . GLU A 47   ? 0.2864 0.3588 0.3573 0.0072  0.0244  0.1164  45   GLU A O   
244   C CB  . GLU A 47   ? 0.3067 0.3931 0.3606 0.0113  0.0279  0.1140  45   GLU A CB  
245   C CG  . GLU A 47   ? 0.4203 0.5164 0.4705 0.0124  0.0288  0.1173  45   GLU A CG  
246   C CD  . GLU A 47   ? 0.4507 0.5545 0.4922 0.0150  0.0314  0.1134  45   GLU A CD  
247   O OE1 . GLU A 47   ? 0.4632 0.5659 0.5025 0.0158  0.0326  0.1093  45   GLU A OE1 
248   O OE2 . GLU A 47   ? 0.5774 0.6884 0.6144 0.0162  0.0321  0.1142  45   GLU A OE2 
249   N N   . CYS A 48   ? 0.2174 0.2778 0.2811 0.0084  0.0231  0.1063  46   CYS A N   
250   C CA  . CYS A 48   ? 0.2293 0.2818 0.2955 0.0077  0.0222  0.1022  46   CYS A CA  
251   C C   . CYS A 48   ? 0.1905 0.2388 0.2672 0.0055  0.0196  0.1061  46   CYS A C   
252   O O   . CYS A 48   ? 0.2264 0.2724 0.3074 0.0045  0.0192  0.1061  46   CYS A O   
253   C CB  . CYS A 48   ? 0.2378 0.2821 0.2985 0.0086  0.0218  0.0942  46   CYS A CB  
254   S SG  . CYS A 48   ? 0.2547 0.3019 0.3040 0.0112  0.0244  0.0883  46   CYS A SG  
255   N N   . LEU A 49   ? 0.2261 0.2731 0.3074 0.0046  0.0177  0.1092  47   LEU A N   
256   C CA  . LEU A 49   ? 0.2605 0.3014 0.3520 0.0027  0.0147  0.1109  47   LEU A CA  
257   C C   . LEU A 49   ? 0.2434 0.2882 0.3442 0.0009  0.0139  0.1181  47   LEU A C   
258   O O   . LEU A 49   ? 0.2526 0.2920 0.3601 -0.0003 0.0121  0.1171  47   LEU A O   
259   C CB  . LEU A 49   ? 0.2668 0.3041 0.3612 0.0023  0.0126  0.1113  47   LEU A CB  
260   C CG  . LEU A 49   ? 0.2590 0.2870 0.3508 0.0029  0.0114  0.1033  47   LEU A CG  
261   C CD1 . LEU A 49   ? 0.2586 0.2799 0.3567 0.0018  0.0095  0.1004  47   LEU A CD1 
262   C CD2 . LEU A 49   ? 0.2509 0.2790 0.3313 0.0048  0.0138  0.0970  47   LEU A CD2 
263   N N   . PRO A 50   ? 0.2675 0.3218 0.3696 0.0007  0.0150  0.1255  48   PRO A N   
264   C CA  . PRO A 50   ? 0.2665 0.3246 0.3787 -0.0013 0.0139  0.1333  48   PRO A CA  
265   C C   . PRO A 50   ? 0.2786 0.3348 0.3926 -0.0017 0.0143  0.1313  48   PRO A C   
266   O O   . PRO A 50   ? 0.2891 0.3411 0.4129 -0.0035 0.0119  0.1332  48   PRO A O   
267   C CB  . PRO A 50   ? 0.2746 0.3449 0.3844 -0.0009 0.0160  0.1404  48   PRO A CB  
268   C CG  . PRO A 50   ? 0.2839 0.3547 0.3870 0.0004  0.0164  0.1382  48   PRO A CG  
269   C CD  . PRO A 50   ? 0.2486 0.3106 0.3443 0.0019  0.0168  0.1280  48   PRO A CD  
270   N N   . PRO A 51   ? 0.2546 0.3135 0.3602 -0.0002 0.0171  0.1274  49   PRO A N   
271   C CA  . PRO A 51   ? 0.2925 0.3493 0.4007 -0.0007 0.0172  0.1255  49   PRO A CA  
272   C C   . PRO A 51   ? 0.2323 0.2779 0.3429 -0.0012 0.0149  0.1191  49   PRO A C   
273   O O   . PRO A 51   ? 0.2606 0.3035 0.3775 -0.0024 0.0136  0.1194  49   PRO A O   
274   C CB  . PRO A 51   ? 0.2803 0.3423 0.3784 0.0014  0.0206  0.1222  49   PRO A CB  
275   C CG  . PRO A 51   ? 0.2926 0.3553 0.3822 0.0031  0.0217  0.1188  49   PRO A CG  
276   C CD  . PRO A 51   ? 0.2974 0.3616 0.3919 0.0021  0.0201  0.1243  49   PRO A CD  
277   N N   . LEU A 52   ? 0.2511 0.2907 0.3570 -0.0003 0.0143  0.1133  50   LEU A N   
278   C CA  . LEU A 52   ? 0.2352 0.2652 0.3436 -0.0007 0.0121  0.1074  50   LEU A CA  
279   C C   . LEU A 52   ? 0.2075 0.2340 0.3278 -0.0026 0.0086  0.1109  50   LEU A C   
280   O O   . LEU A 52   ? 0.2298 0.2513 0.3562 -0.0036 0.0066  0.1088  50   LEU A O   
281   C CB  . LEU A 52   ? 0.2250 0.2503 0.3254 0.0007  0.0124  0.1006  50   LEU A CB  
282   C CG  . LEU A 52   ? 0.2311 0.2586 0.3202 0.0026  0.0153  0.0962  50   LEU A CG  
283   C CD1 . LEU A 52   ? 0.2212 0.2447 0.3038 0.0038  0.0153  0.0909  50   LEU A CD1 
284   C CD2 . LEU A 52   ? 0.2456 0.2703 0.3330 0.0028  0.0158  0.0919  50   LEU A CD2 
285   N N   . VAL A 53   ? 0.2384 0.2678 0.3627 -0.0032 0.0077  0.1164  51   VAL A N   
286   C CA  . VAL A 53   ? 0.2523 0.2790 0.3892 -0.0050 0.0042  0.1207  51   VAL A CA  
287   C C   . VAL A 53   ? 0.2418 0.2710 0.3871 -0.0066 0.0035  0.1256  51   VAL A C   
288   O O   . VAL A 53   ? 0.2732 0.2970 0.4277 -0.0079 0.0006  0.1246  51   VAL A O   
289   C CB  . VAL A 53   ? 0.2236 0.2545 0.3632 -0.0054 0.0036  0.1269  51   VAL A CB  
290   C CG1 . VAL A 53   ? 0.2982 0.3272 0.4521 -0.0074 -0.0001 0.1326  51   VAL A CG1 
291   C CG2 . VAL A 53   ? 0.2505 0.2776 0.3832 -0.0039 0.0037  0.1215  51   VAL A CG2 
292   N N   . GLU A 54   ? 0.2457 0.2835 0.3882 -0.0066 0.0061  0.1305  52   GLU A N   
293   C CA  . GLU A 54   ? 0.2750 0.3161 0.4251 -0.0081 0.0058  0.1355  52   GLU A CA  
294   C C   . GLU A 54   ? 0.2524 0.2873 0.4025 -0.0080 0.0052  0.1291  52   GLU A C   
295   O O   . GLU A 54   ? 0.2755 0.3070 0.4357 -0.0096 0.0025  0.1304  52   GLU A O   
296   C CB  . GLU A 54   ? 0.2945 0.3466 0.4398 -0.0076 0.0091  0.1410  52   GLU A CB  
297   N N   . ALA A 55   ? 0.2412 0.2744 0.3805 -0.0062 0.0074  0.1220  53   ALA A N   
298   C CA  . ALA A 55   ? 0.2711 0.2994 0.4097 -0.0061 0.0071  0.1162  53   ALA A CA  
299   C C   . ALA A 55   ? 0.2176 0.2368 0.3619 -0.0068 0.0037  0.1112  53   ALA A C   
300   O O   . ALA A 55   ? 0.2577 0.2732 0.4064 -0.0075 0.0022  0.1087  53   ALA A O   
301   C CB  . ALA A 55   ? 0.2645 0.2931 0.3905 -0.0041 0.0101  0.1102  53   ALA A CB  
302   N N   . ALA A 56   ? 0.2312 0.2470 0.3753 -0.0065 0.0024  0.1095  54   ALA A N   
303   C CA  . ALA A 56   ? 0.2608 0.2685 0.4097 -0.0068 -0.0008 0.1041  54   ALA A CA  
304   C C   . ALA A 56   ? 0.2986 0.3045 0.4617 -0.0086 -0.0045 0.1086  54   ALA A C   
305   O O   . ALA A 56   ? 0.2731 0.2726 0.4417 -0.0088 -0.0075 0.1040  54   ALA A O   
306   C CB  . ALA A 56   ? 0.2120 0.2169 0.3540 -0.0054 -0.0004 0.0996  54   ALA A CB  
307   N N   . THR A 57   ? 0.2814 0.2931 0.4508 -0.0099 -0.0045 0.1173  55   THR A N   
308   C CA  . THR A 57   ? 0.2828 0.2935 0.4663 -0.0116 -0.0082 0.1220  55   THR A CA  
309   C C   . THR A 57   ? 0.2690 0.2759 0.4606 -0.0127 -0.0108 0.1192  55   THR A C   
310   O O   . THR A 57   ? 0.2894 0.2980 0.4789 -0.0129 -0.0092 0.1195  55   THR A O   
311   C CB  . THR A 57   ? 0.3043 0.3249 0.4901 -0.0124 -0.0074 0.1300  55   THR A CB  
312   O OG1 . THR A 57   ? 0.3122 0.3360 0.4916 -0.0114 -0.0057 0.1322  55   THR A OG1 
313   C CG2 . THR A 57   ? 0.3472 0.3690 0.5468 -0.0140 -0.0114 0.1331  55   THR A CG2 
314   N N   . GLN A 58   ? 0.2627 0.2648 0.4638 -0.0133 -0.0148 0.1162  56   GLN A N   
315   C CA  . GLN A 58   ? 0.2455 0.2446 0.4557 -0.0142 -0.0178 0.1136  56   GLN A CA  
316   C C   . GLN A 58   ? 0.2639 0.2649 0.4873 -0.0155 -0.0218 0.1167  56   GLN A C   
317   O O   . GLN A 58   ? 0.2850 0.2880 0.5103 -0.0155 -0.0224 0.1196  56   GLN A O   
318   C CB  . GLN A 58   ? 0.2691 0.2595 0.4780 -0.0134 -0.0192 0.1049  56   GLN A CB  
319   C CG  . GLN A 58   ? 0.2678 0.2582 0.4620 -0.0118 -0.0154 0.0998  56   GLN A CG  
320   C CD  . GLN A 58   ? 0.2462 0.2310 0.4384 -0.0110 -0.0167 0.0903  56   GLN A CD  
321   O OE1 . GLN A 58   ? 0.2801 0.2642 0.4756 -0.0116 -0.0177 0.0885  56   GLN A OE1 
322   N NE2 . GLN A 58   ? 0.2767 0.2581 0.4635 -0.0097 -0.0169 0.0842  56   GLN A NE2 
323   N N   . SER A 59   ? 0.2872 0.2877 0.5200 -0.0165 -0.0244 0.1161  57   SER A N   
324   C CA  . SER A 59   ? 0.2595 0.2621 0.5058 -0.0177 -0.0284 0.1192  57   SER A CA  
325   C C   . SER A 59   ? 0.3202 0.3172 0.5718 -0.0173 -0.0317 0.1144  57   SER A C   
326   O O   . SER A 59   ? 0.2801 0.2707 0.5266 -0.0161 -0.0316 0.1073  57   SER A O   
327   C CB  . SER A 59   ? 0.3019 0.3039 0.5570 -0.0187 -0.0308 0.1183  57   SER A CB  
328   O OG  . SER A 59   ? 0.3053 0.2996 0.5611 -0.0181 -0.0327 0.1097  57   SER A OG  
329   N N   . LYS A 60   ? 0.2967 0.2965 0.5591 -0.0182 -0.0347 0.1184  58   LYS A N   
330   C CA  . LYS A 60   ? 0.2869 0.2820 0.5563 -0.0179 -0.0383 0.1140  58   LYS A CA  
331   C C   . LYS A 60   ? 0.3082 0.2966 0.5824 -0.0174 -0.0413 0.1055  58   LYS A C   
332   O O   . LYS A 60   ? 0.3200 0.3029 0.5929 -0.0163 -0.0425 0.0987  58   LYS A O   
333   C CB  . LYS A 60   ? 0.2919 0.2917 0.5739 -0.0192 -0.0415 0.1202  58   LYS A CB  
334   C CG  . LYS A 60   ? 0.3348 0.3305 0.6247 -0.0189 -0.0453 0.1163  58   LYS A CG  
335   C CD  . LYS A 60   ? 0.4312 0.4246 0.7112 -0.0176 -0.0431 0.1142  58   LYS A CD  
336   C CE  . LYS A 60   ? 0.4760 0.4677 0.7645 -0.0176 -0.0466 0.1130  58   LYS A CE  
337   N NZ  . LYS A 60   ? 0.4793 0.4648 0.7760 -0.0170 -0.0506 0.1046  58   LYS A NZ  
338   N N   . GLU A 61   ? 0.3009 0.2899 0.5805 -0.0182 -0.0425 0.1055  59   GLU A N   
339   C CA  . GLU A 61   ? 0.3406 0.3239 0.6247 -0.0177 -0.0454 0.0972  59   GLU A CA  
340   C C   . GLU A 61   ? 0.3513 0.3294 0.6233 -0.0163 -0.0428 0.0902  59   GLU A C   
341   O O   . GLU A 61   ? 0.3304 0.3032 0.6039 -0.0152 -0.0450 0.0823  59   GLU A O   
342   C CB  . GLU A 61   ? 0.3204 0.3060 0.6112 -0.0188 -0.0467 0.0991  59   GLU A CB  
343   N N   . ILE A 62   ? 0.3109 0.2909 0.5713 -0.0161 -0.0383 0.0929  60   ILE A N   
344   C CA  . ILE A 62   ? 0.2930 0.2684 0.5419 -0.0148 -0.0358 0.0868  60   ILE A CA  
345   C C   . ILE A 62   ? 0.3332 0.3056 0.5775 -0.0135 -0.0355 0.0838  60   ILE A C   
346   O O   . ILE A 62   ? 0.3194 0.2865 0.5606 -0.0122 -0.0360 0.0761  60   ILE A O   
347   C CB  . ILE A 62   ? 0.2937 0.2723 0.5319 -0.0148 -0.0311 0.0909  60   ILE A CB  
348   C CG1 . ILE A 62   ? 0.3210 0.3005 0.5627 -0.0157 -0.0317 0.0909  60   ILE A CG1 
349   C CG2 . ILE A 62   ? 0.3082 0.2829 0.5338 -0.0133 -0.0281 0.0864  60   ILE A CG2 
350   C CD1 . ILE A 62   ? 0.3697 0.3527 0.6020 -0.0158 -0.0274 0.0947  60   ILE A CD1 
351   N N   . ARG A 63   ? 0.2923 0.2683 0.5360 -0.0137 -0.0345 0.0897  61   ARG A N   
352   C CA  . ARG A 63   ? 0.2877 0.2612 0.5272 -0.0125 -0.0342 0.0872  61   ARG A CA  
353   C C   . ARG A 63   ? 0.3092 0.2781 0.5576 -0.0120 -0.0385 0.0805  61   ARG A C   
354   O O   . ARG A 63   ? 0.2890 0.2535 0.5328 -0.0105 -0.0385 0.0741  61   ARG A O   
355   C CB  . ARG A 63   ? 0.2874 0.2663 0.5257 -0.0130 -0.0327 0.0952  61   ARG A CB  
356   C CG  . ARG A 63   ? 0.3676 0.3509 0.5947 -0.0129 -0.0280 0.1003  61   ARG A CG  
357   C CD  . ARG A 63   ? 0.4309 0.4199 0.6553 -0.0131 -0.0263 0.1072  61   ARG A CD  
358   N NE  . ARG A 63   ? 0.4534 0.4486 0.6872 -0.0146 -0.0279 0.1142  61   ARG A NE  
359   C CZ  . ARG A 63   ? 0.4799 0.4765 0.7232 -0.0153 -0.0309 0.1166  61   ARG A CZ  
360   N NH1 . ARG A 63   ? 0.4941 0.4861 0.7387 -0.0145 -0.0327 0.1125  61   ARG A NH1 
361   N NH2 . ARG A 63   ? 0.4412 0.4440 0.6931 -0.0168 -0.0323 0.1235  61   ARG A NH2 
362   N N   . ASP A 64   ? 0.3316 0.3019 0.5931 -0.0130 -0.0424 0.0815  62   ASP A N   
363   C CA  . ASP A 64   ? 0.3195 0.2860 0.5904 -0.0124 -0.0468 0.0746  62   ASP A CA  
364   C C   . ASP A 64   ? 0.3007 0.2625 0.5692 -0.0113 -0.0475 0.0655  62   ASP A C   
365   O O   . ASP A 64   ? 0.3203 0.2784 0.5892 -0.0099 -0.0491 0.0579  62   ASP A O   
366   C CB  . ASP A 64   ? 0.3266 0.2960 0.6125 -0.0138 -0.0509 0.0781  62   ASP A CB  
367   C CG  . ASP A 64   ? 0.3459 0.3199 0.6357 -0.0147 -0.0510 0.0863  62   ASP A CG  
368   O OD1 . ASP A 64   ? 0.3803 0.3549 0.6614 -0.0142 -0.0481 0.0886  62   ASP A OD1 
369   O OD2 . ASP A 64   ? 0.4318 0.4091 0.7337 -0.0160 -0.0540 0.0906  62   ASP A OD2 
370   N N   . ALA A 65   ? 0.2664 0.2289 0.5327 -0.0119 -0.0463 0.0660  63   ALA A N   
371   C CA  . ALA A 65   ? 0.2988 0.2574 0.5624 -0.0110 -0.0468 0.0575  63   ALA A CA  
372   C C   . ALA A 65   ? 0.3331 0.2885 0.5838 -0.0095 -0.0436 0.0533  63   ALA A C   
373   O O   . ALA A 65   ? 0.3049 0.2568 0.5546 -0.0082 -0.0449 0.0447  63   ALA A O   
374   C CB  . ALA A 65   ? 0.3249 0.2851 0.5883 -0.0121 -0.0459 0.0598  63   ALA A CB  
375   N N   . ALA A 66   ? 0.3095 0.2668 0.5505 -0.0096 -0.0395 0.0592  64   ALA A N   
376   C CA  . ALA A 66   ? 0.3102 0.2683 0.5362 -0.0080 -0.0359 0.0545  64   ALA A CA  
377   C C   . ALA A 66   ? 0.2937 0.2492 0.5210 -0.0067 -0.0375 0.0501  64   ALA A C   
378   O O   . ALA A 66   ? 0.2824 0.2371 0.5022 -0.0052 -0.0368 0.0422  64   ALA A O   
379   C CB  . ALA A 66   ? 0.2960 0.2582 0.5114 -0.0082 -0.0314 0.0615  64   ALA A CB  
380   N N   . ALA A 67   ? 0.2484 0.2028 0.4855 -0.0073 -0.0397 0.0552  65   ALA A N   
381   C CA  . ALA A 67   ? 0.2895 0.2416 0.5288 -0.0061 -0.0415 0.0511  65   ALA A CA  
382   C C   . ALA A 67   ? 0.2859 0.2350 0.5320 -0.0051 -0.0452 0.0414  65   ALA A C   
383   O O   . ALA A 67   ? 0.3112 0.2588 0.5531 -0.0034 -0.0452 0.0343  65   ALA A O   
384   C CB  . ALA A 67   ? 0.3041 0.2594 0.5508 -0.0070 -0.0429 0.0577  65   ALA A CB  
385   N N   . SER A 68   ? 0.2993 0.2493 0.5550 -0.0060 -0.0481 0.0405  66   SER A N   
386   C CA  . SER A 68   ? 0.3377 0.2857 0.6000 -0.0050 -0.0518 0.0310  66   SER A CA  
387   C C   . SER A 68   ? 0.3461 0.2923 0.5985 -0.0037 -0.0499 0.0235  66   SER A C   
388   O O   . SER A 68   ? 0.3161 0.2615 0.5674 -0.0021 -0.0511 0.0147  66   SER A O   
389   C CB  . SER A 68   ? 0.3490 0.2986 0.6232 -0.0062 -0.0553 0.0321  66   SER A CB  
390   O OG  . SER A 68   ? 0.4332 0.3814 0.7125 -0.0051 -0.0584 0.0225  66   SER A OG  
391   N N   . THR A 69   ? 0.3267 0.2756 0.5691 -0.0044 -0.0463 0.0263  67   THR A N   
392   C CA  . THR A 69   ? 0.2956 0.2464 0.5256 -0.0033 -0.0439 0.0194  67   THR A CA  
393   C C   . THR A 69   ? 0.2617 0.2133 0.4802 -0.0018 -0.0411 0.0164  67   THR A C   
394   O O   . THR A 69   ? 0.2796 0.2318 0.4933 -0.0004 -0.0412 0.0081  67   THR A O   
395   C CB  . THR A 69   ? 0.2729 0.2263 0.4951 -0.0043 -0.0407 0.0238  67   THR A CB  
396   O OG1 . THR A 69   ? 0.2892 0.2419 0.5220 -0.0055 -0.0435 0.0251  67   THR A OG1 
397   C CG2 . THR A 69   ? 0.2640 0.2195 0.4724 -0.0032 -0.0378 0.0177  67   THR A CG2 
398   N N   . ALA A 70   ? 0.2779 0.2301 0.4919 -0.0021 -0.0386 0.0230  68   ALA A N   
399   C CA  . ALA A 70   ? 0.2974 0.2504 0.5009 -0.0008 -0.0360 0.0205  68   ALA A CA  
400   C C   . ALA A 70   ? 0.3032 0.2542 0.5130 0.0005  -0.0391 0.0140  68   ALA A C   
401   O O   . ALA A 70   ? 0.3026 0.2545 0.5047 0.0019  -0.0379 0.0074  68   ALA A O   
402   C CB  . ALA A 70   ? 0.2701 0.2243 0.4690 -0.0014 -0.0333 0.0290  68   ALA A CB  
403   N N   . ARG A 71   ? 0.3096 0.2580 0.5339 0.0001  -0.0431 0.0158  69   ARG A N   
404   C CA  . ARG A 71   ? 0.2960 0.2423 0.5278 0.0015  -0.0464 0.0093  69   ARG A CA  
405   C C   . ARG A 71   ? 0.3206 0.2676 0.5524 0.0027  -0.0480 -0.0010 69   ARG A C   
406   O O   . ARG A 71   ? 0.3359 0.2837 0.5640 0.0043  -0.0480 -0.0082 69   ARG A O   
407   C CB  . ARG A 71   ? 0.3299 0.2732 0.5788 0.0007  -0.0508 0.0133  69   ARG A CB  
408   C CG  . ARG A 71   ? 0.3875 0.3302 0.6458 0.0020  -0.0549 0.0055  69   ARG A CG  
409   C CD  . ARG A 71   ? 0.3771 0.3214 0.6482 0.0009  -0.0583 0.0101  69   ARG A CD  
410   N NE  . ARG A 71   ? 0.3778 0.3224 0.6466 0.0005  -0.0568 0.0168  69   ARG A NE  
411   C CZ  . ARG A 71   ? 0.3817 0.3256 0.6488 0.0019  -0.0569 0.0135  69   ARG A CZ  
412   N NH1 . ARG A 71   ? 0.4086 0.3517 0.6758 0.0039  -0.0582 0.0036  69   ARG A NH1 
413   N NH2 . ARG A 71   ? 0.3893 0.3338 0.6544 0.0014  -0.0555 0.0203  69   ARG A NH2 
414   N N   . LYS A 72   ? 0.3067 0.2539 0.5423 0.0019  -0.0493 -0.0019 70   LYS A N   
415   C CA  . LYS A 72   ? 0.3384 0.2870 0.5736 0.0030  -0.0508 -0.0115 70   LYS A CA  
416   C C   . LYS A 72   ? 0.3678 0.3199 0.5867 0.0040  -0.0468 -0.0158 70   LYS A C   
417   O O   . LYS A 72   ? 0.3302 0.2840 0.5472 0.0056  -0.0475 -0.0242 70   LYS A O   
418   C CB  . LYS A 72   ? 0.3389 0.2874 0.5798 0.0018  -0.0524 -0.0105 70   LYS A CB  
419   C CG  . LYS A 72   ? 0.3997 0.3504 0.6391 0.0028  -0.0537 -0.0201 70   LYS A CG  
420   C CD  . LYS A 72   ? 0.4202 0.3705 0.6677 0.0016  -0.0561 -0.0193 70   LYS A CD  
421   C CE  . LYS A 72   ? 0.4997 0.4525 0.7466 0.0028  -0.0579 -0.0293 70   LYS A CE  
422   N NZ  . LYS A 72   ? 0.6021 0.5542 0.8591 0.0018  -0.0611 -0.0295 70   LYS A NZ  
423   N N   . LEU A 73   ? 0.3124 0.2661 0.5199 0.0031  -0.0425 -0.0099 71   LEU A N   
424   C CA  . LEU A 73   ? 0.3116 0.2684 0.5041 0.0039  -0.0387 -0.0130 71   LEU A CA  
425   C C   . LEU A 73   ? 0.3214 0.2784 0.5101 0.0052  -0.0380 -0.0159 71   LEU A C   
426   O O   . LEU A 73   ? 0.3394 0.2990 0.5213 0.0064  -0.0371 -0.0226 71   LEU A O   
427   C CB  . LEU A 73   ? 0.3061 0.2639 0.4885 0.0027  -0.0346 -0.0055 71   LEU A CB  
428   C CG  . LEU A 73   ? 0.2654 0.2237 0.4490 0.0015  -0.0345 -0.0025 71   LEU A CG  
429   C CD1 . LEU A 73   ? 0.2681 0.2275 0.4426 0.0006  -0.0304 0.0051  71   LEU A CD1 
430   C CD2 . LEU A 73   ? 0.3163 0.2770 0.4961 0.0020  -0.0349 -0.0097 71   LEU A CD2 
431   N N   . ILE A 74   ? 0.2721 0.2268 0.4652 0.0050  -0.0383 -0.0107 72   ILE A N   
432   C CA  . ILE A 74   ? 0.2962 0.2511 0.4857 0.0062  -0.0375 -0.0128 72   ILE A CA  
433   C C   . ILE A 74   ? 0.3174 0.2721 0.5151 0.0078  -0.0411 -0.0215 72   ILE A C   
434   O O   . ILE A 74   ? 0.3267 0.2834 0.5184 0.0091  -0.0401 -0.0269 72   ILE A O   
435   C CB  . ILE A 74   ? 0.2885 0.2413 0.4807 0.0055  -0.0369 -0.0045 72   ILE A CB  
436   C CG1 . ILE A 74   ? 0.3324 0.2868 0.5136 0.0044  -0.0327 0.0026  72   ILE A CG1 
437   C CG2 . ILE A 74   ? 0.3031 0.2556 0.4947 0.0068  -0.0371 -0.0069 72   ILE A CG2 
438   C CD1 . ILE A 74   ? 0.3224 0.2756 0.5071 0.0034  -0.0323 0.0117  72   ILE A CD1 
439   N N   . GLU A 75   ? 0.3322 0.2847 0.5439 0.0076  -0.0454 -0.0230 73   GLU A N   
440   C CA  . GLU A 75   ? 0.3510 0.3036 0.5712 0.0093  -0.0491 -0.0320 73   GLU A CA  
441   C C   . GLU A 75   ? 0.3863 0.3433 0.5989 0.0104  -0.0483 -0.0406 73   GLU A C   
442   O O   . GLU A 75   ? 0.3413 0.3006 0.5527 0.0121  -0.0488 -0.0480 73   GLU A O   
443   C CB  . GLU A 75   ? 0.3917 0.3409 0.6290 0.0088  -0.0541 -0.0317 73   GLU A CB  
444   C CG  . GLU A 75   ? 0.4107 0.3562 0.6577 0.0083  -0.0558 -0.0251 73   GLU A CG  
445   C CD  . GLU A 75   ? 0.5163 0.4600 0.7780 0.0070  -0.0598 -0.0215 73   GLU A CD  
446   O OE1 . GLU A 75   ? 0.4966 0.4410 0.7616 0.0065  -0.0612 -0.0236 73   GLU A OE1 
447   O OE2 . GLU A 75   ? 0.4950 0.4389 0.7638 0.0063  -0.0613 -0.0162 73   GLU A OE2 
448   N N   . ALA A 76   ? 0.3601 0.3188 0.5673 0.0094  -0.0468 -0.0396 74   ALA A N   
449   C CA  . ALA A 76   ? 0.3545 0.3179 0.5534 0.0103  -0.0457 -0.0468 74   ALA A CA  
450   C C   . ALA A 76   ? 0.3986 0.3652 0.5835 0.0109  -0.0417 -0.0474 74   ALA A C   
451   O O   . ALA A 76   ? 0.4319 0.4026 0.6127 0.0122  -0.0416 -0.0548 74   ALA A O   
452   C CB  . ALA A 76   ? 0.3839 0.3482 0.5798 0.0089  -0.0449 -0.0443 74   ALA A CB  
453   N N   . LEU A 77   ? 0.3705 0.3356 0.5481 0.0098  -0.0384 -0.0396 75   LEU A N   
454   C CA  . LEU A 77   ? 0.3492 0.3168 0.5141 0.0103  -0.0347 -0.0397 75   LEU A CA  
455   C C   . LEU A 77   ? 0.4099 0.3781 0.5776 0.0119  -0.0358 -0.0446 75   LEU A C   
456   O O   . LEU A 77   ? 0.4228 0.3951 0.5837 0.0130  -0.0347 -0.0503 75   LEU A O   
457   C CB  . LEU A 77   ? 0.3627 0.3282 0.5211 0.0090  -0.0314 -0.0305 75   LEU A CB  
458   C CG  . LEU A 77   ? 0.3824 0.3489 0.5325 0.0078  -0.0287 -0.0262 75   LEU A CG  
459   C CD1 . LEU A 77   ? 0.3432 0.3081 0.4881 0.0069  -0.0258 -0.0179 75   LEU A CD1 
460   C CD2 . LEU A 77   ? 0.3564 0.3273 0.4959 0.0083  -0.0266 -0.0311 75   LEU A CD2 
461   N N   . ARG A 78   ? 0.3450 0.3094 0.5228 0.0120  -0.0382 -0.0423 76   ARG A N   
462   C CA  . ARG A 78   ? 0.3741 0.3387 0.5554 0.0136  -0.0394 -0.0466 76   ARG A CA  
463   C C   . ARG A 78   ? 0.3823 0.3496 0.5704 0.0153  -0.0427 -0.0568 76   ARG A C   
464   O O   . ARG A 78   ? 0.4528 0.4225 0.6401 0.0169  -0.0428 -0.0622 76   ARG A O   
465   C CB  . ARG A 78   ? 0.3493 0.3091 0.5400 0.0132  -0.0412 -0.0409 76   ARG A CB  
466   C CG  . ARG A 78   ? 0.3907 0.3494 0.5731 0.0121  -0.0377 -0.0322 76   ARG A CG  
467   C CD  . ARG A 78   ? 0.3168 0.2718 0.5082 0.0118  -0.0394 -0.0267 76   ARG A CD  
468   N NE  . ARG A 78   ? 0.3374 0.2926 0.5195 0.0114  -0.0360 -0.0207 76   ARG A NE  
469   C CZ  . ARG A 78   ? 0.3313 0.2841 0.5178 0.0110  -0.0365 -0.0146 76   ARG A CZ  
470   N NH1 . ARG A 78   ? 0.3654 0.3152 0.5659 0.0109  -0.0404 -0.0130 76   ARG A NH1 
471   N NH2 . ARG A 78   ? 0.3769 0.3305 0.5540 0.0107  -0.0333 -0.0101 76   ARG A NH2 
472   N N   . GLY A 79   ? 0.3969 0.3643 0.5918 0.0151  -0.0453 -0.0597 77   GLY A N   
473   C CA  . GLY A 79   ? 0.4427 0.4131 0.6444 0.0169  -0.0486 -0.0698 77   GLY A CA  
474   C C   . GLY A 79   ? 0.5188 0.4961 0.7100 0.0177  -0.0466 -0.0763 77   GLY A C   
475   O O   . GLY A 79   ? 0.5523 0.5333 0.7481 0.0194  -0.0491 -0.0853 77   GLY A O   
476   N N   . LYS A 80   ? 0.5311 0.5104 0.7086 0.0166  -0.0423 -0.0720 78   LYS A N   
477   C CA  . LYS A 80   ? 0.5454 0.5315 0.7126 0.0171  -0.0403 -0.0770 78   LYS A CA  
478   C C   . LYS A 80   ? 0.5384 0.5269 0.6931 0.0170  -0.0362 -0.0745 78   LYS A C   
479   O O   . LYS A 80   ? 0.6005 0.5946 0.7455 0.0170  -0.0340 -0.0771 78   LYS A O   
480   C CB  . LYS A 80   ? 0.5418 0.5292 0.7051 0.0158  -0.0397 -0.0753 78   LYS A CB  
481   C CG  . LYS A 80   ? 0.5528 0.5365 0.7096 0.0138  -0.0366 -0.0654 78   LYS A CG  
482   C CD  . LYS A 80   ? 0.4877 0.4721 0.6431 0.0127  -0.0366 -0.0640 78   LYS A CD  
483   C CE  . LYS A 80   ? 0.4750 0.4561 0.6242 0.0109  -0.0336 -0.0545 78   LYS A CE  
484   N NZ  . LYS A 80   ? 0.3683 0.3502 0.5163 0.0098  -0.0336 -0.0531 78   LYS A NZ  
485   N N   . HIS A 81   ? 0.5965 0.5810 0.7513 0.0167  -0.0351 -0.0694 79   HIS A N   
486   C CA  . HIS A 81   ? 0.6794 0.6653 0.8229 0.0164  -0.0313 -0.0662 79   HIS A CA  
487   C C   . HIS A 81   ? 0.7038 0.6965 0.8415 0.0178  -0.0304 -0.0732 79   HIS A C   
488   O O   . HIS A 81   ? 0.7572 0.7518 0.9014 0.0195  -0.0327 -0.0797 79   HIS A O   
489   C CB  . HIS A 81   ? 0.6927 0.6736 0.8395 0.0164  -0.0312 -0.0611 79   HIS A CB  
490   N N   . SER A 84   ? 0.5540 0.5611 0.6397 0.0158  -0.0140 -0.0636 82   SER A N   
491   C CA  . SER A 84   ? 0.5659 0.5779 0.6568 0.0176  -0.0160 -0.0716 82   SER A CA  
492   C C   . SER A 84   ? 0.5114 0.5318 0.5945 0.0178  -0.0142 -0.0750 82   SER A C   
493   O O   . SER A 84   ? 0.4622 0.4872 0.5473 0.0192  -0.0148 -0.0805 82   SER A O   
494   C CB  . SER A 84   ? 0.5312 0.5435 0.6305 0.0183  -0.0192 -0.0764 82   SER A CB  
495   N N   . GLY A 85   ? 0.4991 0.5217 0.5737 0.0163  -0.0120 -0.0716 83   GLY A N   
496   C CA  . GLY A 85   ? 0.4107 0.4416 0.4778 0.0161  -0.0102 -0.0737 83   GLY A CA  
497   C C   . GLY A 85   ? 0.3460 0.3775 0.4094 0.0162  -0.0084 -0.0722 83   GLY A C   
498   O O   . GLY A 85   ? 0.3542 0.3920 0.4177 0.0173  -0.0085 -0.0772 83   GLY A O   
499   N N   . VAL A 86   ? 0.3826 0.4078 0.4429 0.0151  -0.0068 -0.0654 84   VAL A N   
500   C CA  . VAL A 86   ? 0.3698 0.3949 0.4271 0.0151  -0.0053 -0.0638 84   VAL A CA  
501   C C   . VAL A 86   ? 0.3663 0.3901 0.4313 0.0169  -0.0072 -0.0678 84   VAL A C   
502   O O   . VAL A 86   ? 0.2977 0.3259 0.3620 0.0177  -0.0067 -0.0708 84   VAL A O   
503   C CB  . VAL A 86   ? 0.4052 0.4239 0.4581 0.0137  -0.0035 -0.0560 84   VAL A CB  
504   C CG1 . VAL A 86   ? 0.4533 0.4708 0.5046 0.0140  -0.0024 -0.0545 84   VAL A CG1 
505   C CG2 . VAL A 86   ? 0.4380 0.4590 0.4830 0.0121  -0.0016 -0.0526 84   VAL A CG2 
506   N N   . GLU A 87   ? 0.3631 0.3812 0.4362 0.0175  -0.0094 -0.0679 85   GLU A N   
507   C CA  . GLU A 87   ? 0.3772 0.3938 0.4590 0.0191  -0.0116 -0.0717 85   GLU A CA  
508   C C   . GLU A 87   ? 0.3712 0.3956 0.4561 0.0208  -0.0129 -0.0803 85   GLU A C   
509   O O   . GLU A 87   ? 0.3787 0.4051 0.4662 0.0221  -0.0133 -0.0836 85   GLU A O   
510   C CB  . GLU A 87   ? 0.4470 0.4567 0.5376 0.0193  -0.0141 -0.0702 85   GLU A CB  
511   N N   . GLY A 88   ? 0.3433 0.3725 0.4278 0.0209  -0.0136 -0.0841 86   GLY A N   
512   C CA  . GLY A 88   ? 0.3541 0.3917 0.4410 0.0226  -0.0148 -0.0926 86   GLY A CA  
513   C C   . GLY A 88   ? 0.2999 0.3452 0.3793 0.0226  -0.0124 -0.0936 86   GLY A C   
514   O O   . GLY A 88   ? 0.3213 0.3724 0.4038 0.0243  -0.0131 -0.0998 86   GLY A O   
515   N N   . LEU A 89   ? 0.3167 0.3623 0.3868 0.0207  -0.0095 -0.0875 87   LEU A N   
516   C CA  . LEU A 89   ? 0.3248 0.3772 0.3879 0.0203  -0.0072 -0.0873 87   LEU A CA  
517   C C   . LEU A 89   ? 0.2747 0.3243 0.3400 0.0210  -0.0069 -0.0867 87   LEU A C   
518   O O   . LEU A 89   ? 0.2681 0.3242 0.3336 0.0221  -0.0067 -0.0911 87   LEU A O   
519   C CB  . LEU A 89   ? 0.3375 0.3895 0.3914 0.0180  -0.0046 -0.0803 87   LEU A CB  
520   C CG  . LEU A 89   ? 0.3958 0.4567 0.4417 0.0170  -0.0023 -0.0798 87   LEU A CG  
521   C CD1 . LEU A 89   ? 0.3997 0.4576 0.4385 0.0147  -0.0004 -0.0722 87   LEU A CD1 
522   C CD2 . LEU A 89   ? 0.4368 0.5007 0.4819 0.0176  -0.0013 -0.0807 87   LEU A CD2 
523   N N   . VAL A 90   ? 0.2881 0.3283 0.3549 0.0204  -0.0069 -0.0812 88   VAL A N   
524   C CA  . VAL A 90   ? 0.2783 0.3151 0.3475 0.0210  -0.0069 -0.0802 88   VAL A CA  
525   C C   . VAL A 90   ? 0.3049 0.3441 0.3832 0.0234  -0.0094 -0.0876 88   VAL A C   
526   O O   . VAL A 90   ? 0.2792 0.3217 0.3581 0.0243  -0.0091 -0.0900 88   VAL A O   
527   C CB  . VAL A 90   ? 0.2919 0.3188 0.3624 0.0201  -0.0070 -0.0734 88   VAL A CB  
528   C CG1 . VAL A 90   ? 0.3016 0.3248 0.3768 0.0211  -0.0077 -0.0730 88   VAL A CG1 
529   C CG2 . VAL A 90   ? 0.2951 0.3204 0.3563 0.0180  -0.0043 -0.0666 88   VAL A CG2 
530   N N   . GLN A 91   ? 0.3138 0.3515 0.3996 0.0244  -0.0121 -0.0914 89   GLN A N   
531   C CA  . GLN A 91   ? 0.3128 0.3525 0.4083 0.0267  -0.0149 -0.0988 89   GLN A CA  
532   C C   . GLN A 91   ? 0.3158 0.3667 0.4094 0.0281  -0.0145 -0.1062 89   GLN A C   
533   O O   . GLN A 91   ? 0.3353 0.3895 0.4328 0.0297  -0.0151 -0.1107 89   GLN A O   
534   C CB  . GLN A 91   ? 0.3823 0.4177 0.4866 0.0274  -0.0180 -0.1011 89   GLN A CB  
535   N N   . GLU A 92   ? 0.3164 0.3739 0.4043 0.0274  -0.0134 -0.1075 90   GLU A N   
536   C CA  . GLU A 92   ? 0.3064 0.3757 0.3929 0.0287  -0.0132 -0.1149 90   GLU A CA  
537   C C   . GLU A 92   ? 0.2937 0.3684 0.3751 0.0287  -0.0109 -0.1142 90   GLU A C   
538   O O   . GLU A 92   ? 0.3044 0.3867 0.3887 0.0306  -0.0114 -0.1210 90   GLU A O   
539   C CB  . GLU A 92   ? 0.3148 0.3904 0.3952 0.0277  -0.0123 -0.1150 90   GLU A CB  
540   C CG  . GLU A 92   ? 0.3353 0.4245 0.4119 0.0286  -0.0114 -0.1210 90   GLU A CG  
541   C CD  . GLU A 92   ? 0.4268 0.5226 0.4984 0.0277  -0.0110 -0.1216 90   GLU A CD  
542   O OE1 . GLU A 92   ? 0.4246 0.5139 0.4953 0.0263  -0.0112 -0.1171 90   GLU A OE1 
543   O OE2 . GLU A 92   ? 0.4177 0.5255 0.4864 0.0285  -0.0104 -0.1266 90   GLU A OE2 
544   N N   . TYR A 93   ? 0.2820 0.3531 0.3560 0.0265  -0.0083 -0.1063 91   TYR A N   
545   C CA  . TYR A 93   ? 0.2801 0.3561 0.3489 0.0261  -0.0060 -0.1049 91   TYR A CA  
546   C C   . TYR A 93   ? 0.2716 0.3401 0.3434 0.0264  -0.0061 -0.1019 91   TYR A C   
547   O O   . TYR A 93   ? 0.2647 0.3357 0.3320 0.0257  -0.0041 -0.0995 91   TYR A O   
548   C CB  . TYR A 93   ? 0.2960 0.3746 0.3544 0.0236  -0.0031 -0.0986 91   TYR A CB  
549   C CG  . TYR A 93   ? 0.2633 0.3519 0.3183 0.0235  -0.0028 -0.1020 91   TYR A CG  
550   C CD1 . TYR A 93   ? 0.2634 0.3642 0.3162 0.0243  -0.0019 -0.1066 91   TYR A CD1 
551   C CD2 . TYR A 93   ? 0.2805 0.3668 0.3347 0.0227  -0.0035 -0.1007 91   TYR A CD2 
552   C CE1 . TYR A 93   ? 0.2735 0.3843 0.3232 0.0242  -0.0017 -0.1096 91   TYR A CE1 
553   C CE2 . TYR A 93   ? 0.3227 0.4185 0.3739 0.0226  -0.0033 -0.1038 91   TYR A CE2 
554   C CZ  . TYR A 93   ? 0.2603 0.3684 0.3090 0.0234  -0.0024 -0.1082 91   TYR A CZ  
555   O OH  . TYR A 93   ? 0.3625 0.4810 0.4081 0.0233  -0.0023 -0.1111 91   TYR A OH  
556   N N   . SER A 94   ? 0.2625 0.3225 0.3422 0.0273  -0.0085 -0.1019 92   SER A N   
557   C CA  . SER A 94   ? 0.2562 0.3093 0.3398 0.0276  -0.0090 -0.0992 92   SER A CA  
558   C C   . SER A 94   ? 0.2268 0.2763 0.3022 0.0255  -0.0063 -0.0911 92   SER A C   
559   O O   . SER A 94   ? 0.2498 0.2997 0.3239 0.0255  -0.0053 -0.0899 92   SER A O   
560   C CB  . SER A 94   ? 0.2626 0.3210 0.3514 0.0298  -0.0099 -0.1056 92   SER A CB  
561   O OG  . SER A 94   ? 0.3048 0.3675 0.4010 0.0319  -0.0125 -0.1139 92   SER A OG  
562   N N   . LEU A 95   ? 0.2188 0.2649 0.2888 0.0236  -0.0052 -0.0857 93   LEU A N   
563   C CA  . LEU A 95   ? 0.2328 0.2757 0.2951 0.0216  -0.0028 -0.0784 93   LEU A CA  
564   C C   . LEU A 95   ? 0.2138 0.2472 0.2790 0.0214  -0.0034 -0.0736 93   LEU A C   
565   O O   . LEU A 95   ? 0.2350 0.2626 0.3062 0.0219  -0.0054 -0.0732 93   LEU A O   
566   C CB  . LEU A 95   ? 0.1954 0.2383 0.2515 0.0198  -0.0015 -0.0746 93   LEU A CB  
567   C CG  . LEU A 95   ? 0.2015 0.2541 0.2537 0.0196  -0.0007 -0.0781 93   LEU A CG  
568   C CD1 . LEU A 95   ? 0.2624 0.3134 0.3084 0.0175  0.0006  -0.0730 93   LEU A CD1 
569   C CD2 . LEU A 95   ? 0.2146 0.2755 0.2630 0.0196  0.0009  -0.0797 93   LEU A CD2 
570   N N   . SER A 96   ? 0.1932 0.2253 0.2544 0.0207  -0.0019 -0.0697 94   SER A N   
571   C CA  . SER A 96   ? 0.2000 0.2237 0.2617 0.0201  -0.0020 -0.0639 94   SER A CA  
572   C C   . SER A 96   ? 0.2001 0.2200 0.2565 0.0184  -0.0009 -0.0585 94   SER A C   
573   O O   . SER A 96   ? 0.1896 0.2134 0.2413 0.0175  0.0002  -0.0588 94   SER A O   
574   C CB  . SER A 96   ? 0.2114 0.2353 0.2695 0.0197  -0.0006 -0.0614 94   SER A CB  
575   O OG  . SER A 96   ? 0.1845 0.2117 0.2342 0.0181  0.0018  -0.0587 94   SER A OG  
576   N N   . SER A 97   ? 0.1925 0.2052 0.2497 0.0179  -0.0011 -0.0534 95   SER A N   
577   C CA  . SER A 97   ? 0.1997 0.2089 0.2521 0.0164  0.0000  -0.0482 95   SER A CA  
578   C C   . SER A 97   ? 0.1916 0.2037 0.2354 0.0150  0.0024  -0.0458 95   SER A C   
579   O O   . SER A 97   ? 0.1949 0.2083 0.2344 0.0139  0.0033  -0.0445 95   SER A O   
580   C CB  . SER A 97   ? 0.2674 0.2693 0.3218 0.0163  -0.0005 -0.0432 95   SER A CB  
581   O OG  . SER A 97   ? 0.3580 0.3571 0.4205 0.0172  -0.0028 -0.0445 95   SER A OG  
582   N N   . GLN A 98   ? 0.1732 0.1863 0.2146 0.0149  0.0033  -0.0449 96   GLN A N   
583   C CA  . GLN A 98   ? 0.1766 0.1924 0.2107 0.0135  0.0054  -0.0424 96   GLN A CA  
584   C C   . GLN A 98   ? 0.1650 0.1885 0.1969 0.0131  0.0060  -0.0457 96   GLN A C   
585   O O   . GLN A 98   ? 0.1695 0.1947 0.1959 0.0117  0.0073  -0.0432 96   GLN A O   
586   C CB  . GLN A 98   ? 0.1746 0.1904 0.2074 0.0135  0.0060  -0.0412 96   GLN A CB  
587   C CG  . GLN A 98   ? 0.1983 0.2071 0.2311 0.0134  0.0058  -0.0367 96   GLN A CG  
588   C CD  . GLN A 98   ? 0.1883 0.1941 0.2158 0.0121  0.0070  -0.0319 96   GLN A CD  
589   O OE1 . GLN A 98   ? 0.2321 0.2353 0.2602 0.0119  0.0067  -0.0307 96   GLN A OE1 
590   N NE2 . GLN A 98   ? 0.2156 0.2217 0.2383 0.0111  0.0082  -0.0294 96   GLN A NE2 
591   N N   . GLU A 99   ? 0.1652 0.1937 0.2012 0.0144  0.0050  -0.0514 97   GLU A N   
592   C CA  . GLU A 99   ? 0.1534 0.1902 0.1874 0.0142  0.0055  -0.0548 97   GLU A CA  
593   C C   . GLU A 99   ? 0.1782 0.2143 0.2112 0.0136  0.0052  -0.0542 97   GLU A C   
594   O O   . GLU A 99   ? 0.1763 0.2172 0.2044 0.0124  0.0063  -0.0532 97   GLU A O   
595   C CB  . GLU A 99   ? 0.1596 0.2020 0.1988 0.0161  0.0043  -0.0616 97   GLU A CB  
596   C CG  . GLU A 99   ? 0.1613 0.2066 0.2003 0.0164  0.0050  -0.0623 97   GLU A CG  
597   C CD  . GLU A 99   ? 0.1644 0.2140 0.2098 0.0186  0.0036  -0.0690 97   GLU A CD  
598   O OE1 . GLU A 99   ? 0.1820 0.2317 0.2325 0.0198  0.0018  -0.0732 97   GLU A OE1 
599   O OE2 . GLU A 99   ? 0.1884 0.2414 0.2341 0.0191  0.0041  -0.0703 97   GLU A OE2 
600   N N   . GLY A 100  ? 0.1610 0.1916 0.1988 0.0144  0.0036  -0.0546 98   GLY A N   
601   C CA  . GLY A 100  ? 0.1673 0.1970 0.2045 0.0138  0.0033  -0.0538 98   GLY A CA  
602   C C   . GLY A 100  ? 0.1938 0.2208 0.2244 0.0119  0.0049  -0.0477 98   GLY A C   
603   O O   . GLY A 100  ? 0.1731 0.2035 0.2002 0.0109  0.0056  -0.0471 98   GLY A O   
604   N N   . VAL A 101  ? 0.1776 0.1988 0.2069 0.0115  0.0056  -0.0433 99   VAL A N   
605   C CA  . VAL A 101  ? 0.1736 0.1921 0.1972 0.0099  0.0070  -0.0379 99   VAL A CA  
606   C C   . VAL A 101  ? 0.1699 0.1945 0.1882 0.0087  0.0084  -0.0373 99   VAL A C   
607   O O   . VAL A 101  ? 0.1815 0.2075 0.1962 0.0075  0.0091  -0.0350 99   VAL A O   
608   C CB  . VAL A 101  ? 0.1699 0.1819 0.1933 0.0099  0.0073  -0.0339 99   VAL A CB  
609   C CG1 . VAL A 101  ? 0.1916 0.2017 0.2093 0.0085  0.0087  -0.0290 99   VAL A CG1 
610   C CG2 . VAL A 101  ? 0.1905 0.1970 0.2191 0.0108  0.0059  -0.0334 99   VAL A CG2 
611   N N   . ALA A 102  ? 0.1590 0.1878 0.1773 0.0090  0.0088  -0.0393 100  ALA A N   
612   C CA  . ALA A 102  ? 0.1761 0.2111 0.1899 0.0078  0.0101  -0.0382 100  ALA A CA  
613   C C   . ALA A 102  ? 0.1596 0.2018 0.1722 0.0074  0.0101  -0.0406 100  ALA A C   
614   O O   . ALA A 102  ? 0.1884 0.2338 0.1967 0.0058  0.0111  -0.0377 100  ALA A O   
615   C CB  . ALA A 102  ? 0.1727 0.2114 0.1875 0.0083  0.0104  -0.0404 100  ALA A CB  
616   N N   . LEU A 103  ? 0.1560 0.2011 0.1727 0.0088  0.0089  -0.0458 101  LEU A N   
617   C CA  . LEU A 103  ? 0.1630 0.2154 0.1789 0.0087  0.0087  -0.0486 101  LEU A CA  
618   C C   . LEU A 103  ? 0.1750 0.2245 0.1883 0.0075  0.0088  -0.0449 101  LEU A C   
619   O O   . LEU A 103  ? 0.2007 0.2560 0.2104 0.0063  0.0094  -0.0438 101  LEU A O   
620   C CB  . LEU A 103  ? 0.1735 0.2282 0.1952 0.0107  0.0070  -0.0552 101  LEU A CB  
621   C CG  . LEU A 103  ? 0.1712 0.2336 0.1925 0.0109  0.0065  -0.0589 101  LEU A CG  
622   C CD1 . LEU A 103  ? 0.2081 0.2811 0.2251 0.0101  0.0079  -0.0593 101  LEU A CD1 
623   C CD2 . LEU A 103  ? 0.1937 0.2570 0.2218 0.0130  0.0045  -0.0656 101  LEU A CD2 
624   N N   . MET A 104  ? 0.1746 0.2156 0.1900 0.0078  0.0081  -0.0430 102  MET A N   
625   C CA  . MET A 104  ? 0.1711 0.2094 0.1844 0.0067  0.0082  -0.0397 102  MET A CA  
626   C C   . MET A 104  ? 0.1984 0.2359 0.2063 0.0049  0.0096  -0.0341 102  MET A C   
627   O O   . MET A 104  ? 0.2146 0.2543 0.2198 0.0038  0.0099  -0.0320 102  MET A O   
628   C CB  . MET A 104  ? 0.1817 0.2116 0.1988 0.0074  0.0072  -0.0388 102  MET A CB  
629   C CG  . MET A 104  ? 0.2262 0.2567 0.2496 0.0091  0.0054  -0.0441 102  MET A CG  
630   S SD  . MET A 104  ? 0.2884 0.3278 0.3121 0.0093  0.0045  -0.0492 102  MET A SD  
631   C CE  . MET A 104  ? 0.3252 0.3611 0.3466 0.0080  0.0046  -0.0450 102  MET A CE  
632   N N   . CYS A 105  ? 0.1770 0.2118 0.1838 0.0047  0.0104  -0.0318 103  CYS A N   
633   C CA  . CYS A 105  ? 0.1922 0.2269 0.1947 0.0030  0.0115  -0.0270 103  CYS A CA  
634   C C   . CYS A 105  ? 0.2224 0.2661 0.2223 0.0019  0.0121  -0.0272 103  CYS A C   
635   O O   . CYS A 105  ? 0.2358 0.2808 0.2327 0.0004  0.0125  -0.0235 103  CYS A O   
636   C CB  . CYS A 105  ? 0.2130 0.2438 0.2153 0.0031  0.0120  -0.0252 103  CYS A CB  
637   S SG  . CYS A 105  ? 0.2116 0.2324 0.2161 0.0041  0.0115  -0.0236 103  CYS A SG  
638   N N   . LEU A 106  ? 0.1831 0.2335 0.1842 0.0026  0.0121  -0.0312 104  LEU A N   
639   C CA  . LEU A 106  ? 0.2132 0.2736 0.2118 0.0016  0.0127  -0.0316 104  LEU A CA  
640   C C   . LEU A 106  ? 0.2419 0.3061 0.2397 0.0012  0.0122  -0.0320 104  LEU A C   
641   O O   . LEU A 106  ? 0.2212 0.2904 0.2158 -0.0004 0.0127  -0.0289 104  LEU A O   
642   C CB  . LEU A 106  ? 0.1912 0.2586 0.1919 0.0028  0.0127  -0.0367 104  LEU A CB  
643   C CG  . LEU A 106  ? 0.2017 0.2811 0.2001 0.0020  0.0132  -0.0378 104  LEU A CG  
644   C CD1 . LEU A 106  ? 0.2692 0.3512 0.2640 -0.0001 0.0143  -0.0322 104  LEU A CD1 
645   C CD2 . LEU A 106  ? 0.2348 0.3215 0.2358 0.0037  0.0130  -0.0441 104  LEU A CD2 
646   N N   . ALA A 107  ? 0.1833 0.2454 0.1840 0.0027  0.0111  -0.0358 105  ALA A N   
647   C CA  . ALA A 107  ? 0.2123 0.2779 0.2125 0.0024  0.0105  -0.0366 105  ALA A CA  
648   C C   . ALA A 107  ? 0.2551 0.3159 0.2525 0.0008  0.0108  -0.0307 105  ALA A C   
649   O O   . ALA A 107  ? 0.2407 0.3070 0.2356 -0.0005 0.0109  -0.0288 105  ALA A O   
650   C CB  . ALA A 107  ? 0.2036 0.2664 0.2083 0.0042  0.0090  -0.0415 105  ALA A CB  
651   N N   . GLU A 108  ? 0.2141 0.2654 0.2123 0.0008  0.0109  -0.0277 106  GLU A N   
652   C CA  . GLU A 108  ? 0.2439 0.2904 0.2399 -0.0005 0.0112  -0.0224 106  GLU A CA  
653   C C   . GLU A 108  ? 0.2838 0.3351 0.2763 -0.0023 0.0120  -0.0184 106  GLU A C   
654   O O   . GLU A 108  ? 0.3201 0.3730 0.3108 -0.0036 0.0119  -0.0153 106  GLU A O   
655   C CB  . GLU A 108  ? 0.2392 0.2759 0.2363 0.0000  0.0113  -0.0203 106  GLU A CB  
656   C CG  . GLU A 108  ? 0.2524 0.2839 0.2476 -0.0010 0.0116  -0.0152 106  GLU A CG  
657   C CD  . GLU A 108  ? 0.2879 0.3121 0.2834 -0.0007 0.0120  -0.0130 106  GLU A CD  
658   O OE1 . GLU A 108  ? 0.2893 0.3106 0.2870 0.0006  0.0118  -0.0153 106  GLU A OE1 
659   O OE2 . GLU A 108  ? 0.3284 0.3498 0.3221 -0.0016 0.0123  -0.0091 106  GLU A OE2 
660   N N   . ALA A 109  ? 0.2610 0.3147 0.2529 -0.0026 0.0126  -0.0182 107  ALA A N   
661   C CA  . ALA A 109  ? 0.2810 0.3394 0.2705 -0.0045 0.0132  -0.0141 107  ALA A CA  
662   C C   . ALA A 109  ? 0.3109 0.3799 0.2988 -0.0054 0.0132  -0.0147 107  ALA A C   
663   O O   . ALA A 109  ? 0.3559 0.4280 0.3420 -0.0071 0.0133  -0.0103 107  ALA A O   
664   C CB  . ALA A 109  ? 0.3285 0.3875 0.3182 -0.0045 0.0139  -0.0142 107  ALA A CB  
665   N N   . LEU A 110  ? 0.2669 0.3423 0.2558 -0.0041 0.0131  -0.0201 108  LEU A N   
666   C CA  . LEU A 110  ? 0.2770 0.3636 0.2644 -0.0046 0.0130  -0.0213 108  LEU A CA  
667   C C   . LEU A 110  ? 0.3049 0.3909 0.2915 -0.0052 0.0123  -0.0196 108  LEU A C   
668   O O   . LEU A 110  ? 0.3326 0.4265 0.3170 -0.0066 0.0124  -0.0173 108  LEU A O   
669   C CB  . LEU A 110  ? 0.2406 0.3332 0.2299 -0.0027 0.0128  -0.0284 108  LEU A CB  
670   C CG  . LEU A 110  ? 0.2668 0.3636 0.2565 -0.0024 0.0136  -0.0301 108  LEU A CG  
671   C CD1 . LEU A 110  ? 0.2469 0.3475 0.2396 -0.0001 0.0130  -0.0377 108  LEU A CD1 
672   C CD2 . LEU A 110  ? 0.3414 0.4488 0.3281 -0.0043 0.0145  -0.0267 108  LEU A CD2 
673   N N   . LEU A 111  ? 0.2901 0.3672 0.2784 -0.0043 0.0116  -0.0204 109  LEU A N   
674   C CA  . LEU A 111  ? 0.3398 0.4158 0.3277 -0.0048 0.0109  -0.0188 109  LEU A CA  
675   C C   . LEU A 111  ? 0.4001 0.4726 0.3862 -0.0066 0.0112  -0.0120 109  LEU A C   
676   O O   . LEU A 111  ? 0.3974 0.4704 0.3828 -0.0073 0.0106  -0.0100 109  LEU A O   
677   C CB  . LEU A 111  ? 0.3185 0.3866 0.3095 -0.0031 0.0101  -0.0218 109  LEU A CB  
678   C CG  . LEU A 111  ? 0.2994 0.3718 0.2930 -0.0013 0.0093  -0.0288 109  LEU A CG  
679   C CD1 . LEU A 111  ? 0.3434 0.4070 0.3408 0.0002  0.0084  -0.0311 109  LEU A CD1 
680   C CD2 . LEU A 111  ? 0.3064 0.3886 0.2987 -0.0016 0.0087  -0.0309 109  LEU A CD2 
681   N N   . ARG A 112  ? 0.4024 0.4714 0.3881 -0.0074 0.0118  -0.0086 110  ARG A N   
682   C CA  . ARG A 112  ? 0.4345 0.5018 0.4190 -0.0093 0.0118  -0.0024 110  ARG A CA  
683   C C   . ARG A 112  ? 0.4705 0.5482 0.4531 -0.0111 0.0119  0.0005  110  ARG A C   
684   O O   . ARG A 112  ? 0.5020 0.5795 0.4842 -0.0128 0.0116  0.0059  110  ARG A O   
685   C CB  . ARG A 112  ? 0.4464 0.5066 0.4316 -0.0094 0.0122  -0.0001 110  ARG A CB  
686   C CG  . ARG A 112  ? 0.4310 0.4810 0.4177 -0.0078 0.0122  -0.0018 110  ARG A CG  
687   C CD  . ARG A 112  ? 0.4840 0.5292 0.4713 -0.0075 0.0127  -0.0012 110  ARG A CD  
688   N NE  . ARG A 112  ? 0.6189 0.6615 0.6059 -0.0090 0.0125  0.0039  110  ARG A NE  
689   C CZ  . ARG A 112  ? 0.6727 0.7073 0.6604 -0.0088 0.0123  0.0059  110  ARG A CZ  
690   N NH1 . ARG A 112  ? 0.6390 0.6675 0.6274 -0.0072 0.0122  0.0040  110  ARG A NH1 
691   N NH2 . ARG A 112  ? 0.6874 0.7202 0.6753 -0.0101 0.0119  0.0101  110  ARG A NH2 
692   N N   . ILE A 113  ? 0.4525 0.5399 0.4344 -0.0108 0.0122  -0.0029 111  ILE A N   
693   C CA  . ILE A 113  ? 0.4877 0.5869 0.4677 -0.0124 0.0123  -0.0006 111  ILE A CA  
694   C C   . ILE A 113  ? 0.5180 0.6209 0.4973 -0.0123 0.0115  -0.0015 111  ILE A C   
695   O O   . ILE A 113  ? 0.5005 0.6056 0.4802 -0.0106 0.0112  -0.0073 111  ILE A O   
696   C CB  . ILE A 113  ? 0.4207 0.5297 0.4002 -0.0119 0.0131  -0.0044 111  ILE A CB  
697   C CG1 . ILE A 113  ? 0.4120 0.5176 0.3923 -0.0122 0.0138  -0.0028 111  ILE A CG1 
698   C CG2 . ILE A 113  ? 0.4951 0.6178 0.4725 -0.0134 0.0132  -0.0023 111  ILE A CG2 
699   C CD1 . ILE A 113  ? 0.4485 0.5627 0.4287 -0.0115 0.0146  -0.0069 111  ILE A CD1 
700   N N   . PRO A 114  ? 0.6023 0.7058 0.5808 -0.0140 0.0109  0.0040  112  PRO A N   
701   C CA  . PRO A 114  ? 0.5797 0.6854 0.5578 -0.0139 0.0100  0.0033  112  PRO A CA  
702   C C   . PRO A 114  ? 0.5540 0.6727 0.5304 -0.0136 0.0099  -0.0002 112  PRO A C   
703   O O   . PRO A 114  ? 0.6205 0.7397 0.5973 -0.0121 0.0093  -0.0051 112  PRO A O   
704   C CB  . PRO A 114  ? 0.5844 0.6885 0.5623 -0.0160 0.0094  0.0108  112  PRO A CB  
705   C CG  . PRO A 114  ? 0.6343 0.7308 0.6135 -0.0167 0.0099  0.0142  112  PRO A CG  
706   C CD  . PRO A 114  ? 0.6151 0.7160 0.5940 -0.0161 0.0109  0.0110  112  PRO A CD  
707   N N   . ASP A 115  ? 0.5648 0.6944 0.5395 -0.0150 0.0104  0.0021  113  ASP A N   
708   C CA  . ASP A 115  ? 0.5933 0.7368 0.5661 -0.0148 0.0103  -0.0009 113  ASP A CA  
709   C C   . ASP A 115  ? 0.5381 0.6847 0.5115 -0.0125 0.0108  -0.0091 113  ASP A C   
710   O O   . ASP A 115  ? 0.5343 0.6799 0.5084 -0.0121 0.0117  -0.0102 113  ASP A O   
711   C CB  . ASP A 115  ? 0.5366 0.6916 0.5075 -0.0171 0.0108  0.0047  113  ASP A CB  
712   C CG  . ASP A 115  ? 0.6060 0.7768 0.5746 -0.0169 0.0108  0.0015  113  ASP A CG  
713   O OD1 . ASP A 115  ? 0.6404 0.8145 0.6082 -0.0165 0.0099  -0.0001 113  ASP A OD1 
714   O OD2 . ASP A 115  ? 0.6111 0.7915 0.5788 -0.0170 0.0118  0.0004  113  ASP A OD2 
715   N N   . THR A 116  ? 0.5161 0.6668 0.4897 -0.0109 0.0100  -0.0149 114  THR A N   
716   C CA  . THR A 116  ? 0.4999 0.6528 0.4751 -0.0084 0.0100  -0.0233 114  THR A CA  
717   C C   . THR A 116  ? 0.5210 0.6869 0.4947 -0.0085 0.0110  -0.0251 114  THR A C   
718   O O   . THR A 116  ? 0.4911 0.6557 0.4664 -0.0071 0.0116  -0.0290 114  THR A O   
719   C CB  . THR A 116  ? 0.4858 0.6411 0.4619 -0.0069 0.0086  -0.0290 114  THR A CB  
720   O OG1 . THR A 116  ? 0.5605 0.7032 0.5386 -0.0067 0.0077  -0.0277 114  THR A OG1 
721   C CG2 . THR A 116  ? 0.5070 0.6657 0.4856 -0.0043 0.0083  -0.0381 114  THR A CG2 
722   N N   . ALA A 117  ? 0.4781 0.6570 0.4489 -0.0100 0.0111  -0.0221 115  ALA A N   
723   C CA  . ALA A 117  ? 0.5180 0.7108 0.4873 -0.0101 0.0122  -0.0236 115  ALA A CA  
724   C C   . ALA A 117  ? 0.4387 0.6277 0.4084 -0.0112 0.0134  -0.0193 115  ALA A C   
725   O O   . ALA A 117  ? 0.4745 0.6690 0.4447 -0.0103 0.0143  -0.0230 115  ALA A O   
726   C CB  . ALA A 117  ? 0.5073 0.7148 0.4733 -0.0118 0.0121  -0.0198 115  ALA A CB  
727   N N   . THR A 118  ? 0.4366 0.6165 0.4065 -0.0132 0.0134  -0.0118 116  THR A N   
728   C CA  . THR A 118  ? 0.4676 0.6431 0.4384 -0.0143 0.0144  -0.0079 116  THR A CA  
729   C C   . THR A 118  ? 0.4230 0.5885 0.3963 -0.0121 0.0146  -0.0134 116  THR A C   
730   O O   . THR A 118  ? 0.4155 0.5831 0.3894 -0.0119 0.0155  -0.0144 116  THR A O   
731   C CB  . THR A 118  ? 0.4687 0.6357 0.4399 -0.0166 0.0140  0.0006  116  THR A CB  
732   O OG1 . THR A 118  ? 0.5696 0.7457 0.5389 -0.0187 0.0135  0.0059  116  THR A OG1 
733   C CG2 . THR A 118  ? 0.4412 0.6050 0.4135 -0.0179 0.0147  0.0048  116  THR A CG2 
734   N N   . ARG A 119  ? 0.4385 0.5934 0.4135 -0.0105 0.0137  -0.0167 117  ARG A N   
735   C CA  . ARG A 119  ? 0.4208 0.5662 0.3985 -0.0084 0.0137  -0.0216 117  ARG A CA  
736   C C   . ARG A 119  ? 0.3875 0.5416 0.3662 -0.0064 0.0140  -0.0292 117  ARG A C   
737   O O   . ARG A 119  ? 0.3918 0.5439 0.3721 -0.0055 0.0146  -0.0314 117  ARG A O   
738   C CB  . ARG A 119  ? 0.4019 0.5361 0.3814 -0.0073 0.0126  -0.0234 117  ARG A CB  
739   C CG  . ARG A 119  ? 0.3528 0.4761 0.3354 -0.0054 0.0125  -0.0272 117  ARG A CG  
740   C CD  . ARG A 119  ? 0.3775 0.4930 0.3624 -0.0041 0.0113  -0.0300 117  ARG A CD  
741   N NE  . ARG A 119  ? 0.3859 0.4960 0.3695 -0.0055 0.0109  -0.0244 117  ARG A NE  
742   C CZ  . ARG A 119  ? 0.4054 0.5170 0.3888 -0.0055 0.0100  -0.0251 117  ARG A CZ  
743   N NH1 . ARG A 119  ? 0.4099 0.5278 0.3944 -0.0040 0.0092  -0.0312 117  ARG A NH1 
744   N NH2 . ARG A 119  ? 0.5161 0.6228 0.4986 -0.0069 0.0097  -0.0196 117  ARG A NH2 
745   N N   . ASP A 120  ? 0.4045 0.5686 0.3825 -0.0055 0.0134  -0.0336 118  ASP A N   
746   C CA  . ASP A 120  ? 0.3981 0.5710 0.3773 -0.0033 0.0134  -0.0416 118  ASP A CA  
747   C C   . ASP A 120  ? 0.4336 0.6175 0.4113 -0.0041 0.0149  -0.0403 118  ASP A C   
748   O O   . ASP A 120  ? 0.4196 0.6064 0.3993 -0.0023 0.0152  -0.0458 118  ASP A O   
749   C CB  . ASP A 120  ? 0.4287 0.6106 0.4076 -0.0022 0.0124  -0.0467 118  ASP A CB  
750   C CG  . ASP A 120  ? 0.4877 0.6589 0.4688 -0.0013 0.0108  -0.0484 118  ASP A CG  
751   O OD1 . ASP A 120  ? 0.4969 0.6541 0.4796 -0.0015 0.0107  -0.0456 118  ASP A OD1 
752   O OD2 . ASP A 120  ? 0.4898 0.6668 0.4709 -0.0004 0.0097  -0.0526 118  ASP A OD2 
753   N N   . ALA A 121  ? 0.4191 0.6094 0.3937 -0.0068 0.0156  -0.0330 119  ALA A N   
754   C CA  . ALA A 121  ? 0.4282 0.6288 0.4017 -0.0079 0.0170  -0.0308 119  ALA A CA  
755   C C   . ALA A 121  ? 0.4108 0.6015 0.3864 -0.0079 0.0177  -0.0292 119  ALA A C   
756   O O   . ALA A 121  ? 0.4392 0.6356 0.4156 -0.0071 0.0185  -0.0321 119  ALA A O   
757   C CB  . ALA A 121  ? 0.4319 0.6405 0.4024 -0.0110 0.0174  -0.0223 119  ALA A CB  
758   N N   . LEU A 122  ? 0.4030 0.5793 0.3795 -0.0088 0.0172  -0.0248 120  LEU A N   
759   C CA  . LEU A 122  ? 0.4121 0.5786 0.3905 -0.0087 0.0176  -0.0237 120  LEU A CA  
760   C C   . LEU A 122  ? 0.4193 0.5824 0.4006 -0.0057 0.0174  -0.0317 120  LEU A C   
761   O O   . LEU A 122  ? 0.3869 0.5507 0.3695 -0.0052 0.0181  -0.0331 120  LEU A O   
762   C CB  . LEU A 122  ? 0.4596 0.6118 0.4385 -0.0098 0.0170  -0.0183 120  LEU A CB  
763   C CG  . LEU A 122  ? 0.4139 0.5575 0.3943 -0.0103 0.0175  -0.0155 120  LEU A CG  
764   C CD1 . LEU A 122  ? 0.4899 0.6420 0.4693 -0.0125 0.0184  -0.0103 120  LEU A CD1 
765   C CD2 . LEU A 122  ? 0.4033 0.5329 0.3844 -0.0109 0.0168  -0.0116 120  LEU A CD2 
766   N N   . ILE A 123  ? 0.3937 0.5531 0.3764 -0.0038 0.0163  -0.0370 121  ILE A N   
767   C CA  . ILE A 123  ? 0.3827 0.5388 0.3690 -0.0010 0.0157  -0.0447 121  ILE A CA  
768   C C   . ILE A 123  ? 0.3924 0.5620 0.3791 0.0002  0.0164  -0.0501 121  ILE A C   
769   O O   . ILE A 123  ? 0.3958 0.5644 0.3847 0.0013  0.0168  -0.0526 121  ILE A O   
770   C CB  . ILE A 123  ? 0.3637 0.5148 0.3518 0.0006  0.0142  -0.0492 121  ILE A CB  
771   C CG1 . ILE A 123  ? 0.3418 0.4787 0.3302 -0.0003 0.0137  -0.0443 121  ILE A CG1 
772   C CG2 . ILE A 123  ? 0.3339 0.4843 0.3266 0.0036  0.0133  -0.0577 121  ILE A CG2 
773   C CD1 . ILE A 123  ? 0.3422 0.4749 0.3322 0.0008  0.0122  -0.0473 121  ILE A CD1 
774   N N   . ARG A 124  ? 0.3770 0.5599 0.3615 0.0001  0.0164  -0.0518 122  ARG A N   
775   C CA  . ARG A 124  ? 0.3766 0.5734 0.3617 0.0017  0.0169  -0.0582 122  ARG A CA  
776   C C   . ARG A 124  ? 0.4465 0.6503 0.4304 0.0004  0.0185  -0.0546 122  ARG A C   
777   O O   . ARG A 124  ? 0.4613 0.6694 0.4474 0.0021  0.0189  -0.0597 122  ARG A O   
778   C CB  . ARG A 124  ? 0.4052 0.6155 0.3880 0.0018  0.0165  -0.0605 122  ARG A CB  
779   N N   . ASP A 125  ? 0.4791 0.6839 0.4599 -0.0026 0.0194  -0.0459 123  ASP A N   
780   C CA  . ASP A 125  ? 0.5331 0.7468 0.5128 -0.0042 0.0209  -0.0420 123  ASP A CA  
781   C C   . ASP A 125  ? 0.5513 0.7537 0.5328 -0.0050 0.0213  -0.0382 123  ASP A C   
782   O O   . ASP A 125  ? 0.5814 0.7895 0.5635 -0.0052 0.0223  -0.0382 123  ASP A O   
783   C CB  . ASP A 125  ? 0.6165 0.8397 0.5926 -0.0072 0.0214  -0.0344 123  ASP A CB  
784   C CG  . ASP A 125  ? 0.6288 0.8642 0.6028 -0.0066 0.0210  -0.0377 123  ASP A CG  
785   O OD1 . ASP A 125  ? 0.6643 0.9069 0.6394 -0.0039 0.0208  -0.0463 123  ASP A OD1 
786   O OD2 . ASP A 125  ? 0.5969 0.8348 0.5683 -0.0087 0.0208  -0.0319 123  ASP A OD2 
787   N N   . LYS A 126  ? 0.4736 0.6606 0.4558 -0.0055 0.0205  -0.0351 124  LYS A N   
788   C CA  . LYS A 126  ? 0.4356 0.6122 0.4191 -0.0065 0.0207  -0.0307 124  LYS A CA  
789   C C   . LYS A 126  ? 0.4993 0.6625 0.4858 -0.0043 0.0199  -0.0351 124  LYS A C   
790   O O   . LYS A 126  ? 0.5560 0.7168 0.5445 -0.0036 0.0203  -0.0364 124  LYS A O   
791   C CB  . LYS A 126  ? 0.5407 0.7115 0.5226 -0.0094 0.0205  -0.0220 124  LYS A CB  
792   N N   . ILE A 127  ? 0.4592 0.6140 0.4464 -0.0032 0.0188  -0.0370 125  ILE A N   
793   C CA  . ILE A 127  ? 0.3809 0.5228 0.3712 -0.0014 0.0180  -0.0400 125  ILE A CA  
794   C C   . ILE A 127  ? 0.4324 0.5780 0.4260 0.0013  0.0177  -0.0480 125  ILE A C   
795   O O   . ILE A 127  ? 0.4990 0.6387 0.4951 0.0023  0.0177  -0.0494 125  ILE A O   
796   C CB  . ILE A 127  ? 0.3806 0.5134 0.3711 -0.0010 0.0168  -0.0399 125  ILE A CB  
797   C CG1 . ILE A 127  ? 0.4495 0.5795 0.4371 -0.0036 0.0170  -0.0322 125  ILE A CG1 
798   C CG2 . ILE A 127  ? 0.3895 0.5090 0.3832 0.0005  0.0160  -0.0416 125  ILE A CG2 
799   C CD1 . ILE A 127  ? 0.4299 0.5532 0.4171 -0.0052 0.0175  -0.0264 125  ILE A CD1 
800   N N   . ALA A 128  ? 0.3943 0.5501 0.3882 0.0027  0.0174  -0.0536 126  ALA A N   
801   C CA  . ALA A 128  ? 0.3606 0.5193 0.3584 0.0056  0.0167  -0.0620 126  ALA A CA  
802   C C   . ALA A 128  ? 0.4559 0.6205 0.4547 0.0059  0.0178  -0.0632 126  ALA A C   
803   O O   . ALA A 128  ? 0.4282 0.5903 0.4311 0.0081  0.0172  -0.0686 126  ALA A O   
804   C CB  . ALA A 128  ? 0.3826 0.5524 0.3804 0.0069  0.0161  -0.0679 126  ALA A CB  
805   N N   . ASP A 129  ? 0.5948 0.7672 0.5903 0.0037  0.0193  -0.0579 127  ASP A N   
806   C CA  . ASP A 129  ? 0.6794 0.8582 0.6757 0.0037  0.0204  -0.0582 127  ASP A CA  
807   C C   . ASP A 129  ? 0.6962 0.8636 0.6931 0.0025  0.0206  -0.0531 127  ASP A C   
808   O O   . ASP A 129  ? 0.7792 0.9503 0.7747 0.0006  0.0217  -0.0483 127  ASP A O   
809   C CB  . ASP A 129  ? 0.6321 0.8264 0.6250 0.0018  0.0218  -0.0553 127  ASP A CB  
810   N N   . GLY A 130  ? 0.7036 0.8573 0.7028 0.0036  0.0195  -0.0540 128  GLY A N   
811   C CA  . GLY A 130  ? 0.7010 0.8433 0.7007 0.0027  0.0195  -0.0495 128  GLY A CA  
812   C C   . GLY A 130  ? 0.7244 0.8640 0.7206 -0.0003 0.0200  -0.0412 128  GLY A C   
813   O O   . GLY A 130  ? 0.7716 0.9147 0.7653 -0.0016 0.0200  -0.0388 128  GLY A O   
814   N N   . ASN A 131  ? 0.7391 0.8722 0.7356 -0.0015 0.0202  -0.0369 129  ASN A N   
815   C CA  . ASN A 131  ? 0.7126 0.8433 0.7068 -0.0043 0.0205  -0.0292 129  ASN A CA  
816   C C   . ASN A 131  ? 0.5784 0.7024 0.5708 -0.0050 0.0198  -0.0263 129  ASN A C   
817   O O   . ASN A 131  ? 0.6489 0.7759 0.6392 -0.0072 0.0200  -0.0211 129  ASN A O   
818   C CB  . ASN A 131  ? 0.7038 0.8476 0.6964 -0.0063 0.0216  -0.0260 129  ASN A CB  
819   N N   . TRP A 132  ? 0.5740 0.6893 0.5678 -0.0032 0.0189  -0.0297 130  TRP A N   
820   C CA  . TRP A 132  ? 0.4899 0.5981 0.4824 -0.0037 0.0182  -0.0271 130  TRP A CA  
821   C C   . TRP A 132  ? 0.4495 0.5495 0.4410 -0.0056 0.0182  -0.0206 130  TRP A C   
822   O O   . TRP A 132  ? 0.5327 0.6305 0.5227 -0.0069 0.0179  -0.0167 130  TRP A O   
823   C CB  . TRP A 132  ? 0.4426 0.5429 0.4373 -0.0014 0.0173  -0.0317 130  TRP A CB  
824   C CG  . TRP A 132  ? 0.3598 0.4511 0.3570 -0.0002 0.0169  -0.0327 130  TRP A CG  
825   C CD1 . TRP A 132  ? 0.3505 0.4431 0.3506 0.0016  0.0167  -0.0375 130  TRP A CD1 
826   C CD2 . TRP A 132  ? 0.2938 0.3739 0.2908 -0.0007 0.0166  -0.0288 130  TRP A CD2 
827   N NE1 . TRP A 132  ? 0.3459 0.4288 0.3476 0.0022  0.0163  -0.0366 130  TRP A NE1 
828   C CE2 . TRP A 132  ? 0.2885 0.3639 0.2881 0.0008  0.0163  -0.0313 130  TRP A CE2 
829   C CE3 . TRP A 132  ? 0.3135 0.3876 0.3085 -0.0022 0.0165  -0.0236 130  TRP A CE3 
830   C CZ2 . TRP A 132  ? 0.3007 0.3662 0.3007 0.0008  0.0159  -0.0287 130  TRP A CZ2 
831   C CZ3 . TRP A 132  ? 0.2981 0.3623 0.2937 -0.0021 0.0161  -0.0214 130  TRP A CZ3 
832   C CH2 . TRP A 132  ? 0.2981 0.3582 0.2959 -0.0006 0.0159  -0.0239 130  TRP A CH2 
833   N N   . LYS A 133  ? 0.5070 0.6028 0.4998 -0.0056 0.0183  -0.0196 131  LYS A N   
834   C CA  . LYS A 133  ? 0.5733 0.6612 0.5656 -0.0072 0.0180  -0.0141 131  LYS A CA  
835   C C   . LYS A 133  ? 0.6756 0.7697 0.6666 -0.0098 0.0183  -0.0085 131  LYS A C   
836   O O   . LYS A 133  ? 0.7454 0.8342 0.7359 -0.0112 0.0177  -0.0039 131  LYS A O   
837   C CB  . LYS A 133  ? 0.4980 0.5814 0.4920 -0.0065 0.0180  -0.0147 131  LYS A CB  
838   N N   . SER A 134  ? 0.7023 0.8081 0.6930 -0.0106 0.0191  -0.0088 132  SER A N   
839   C CA  . SER A 134  ? 0.7238 0.8365 0.7138 -0.0134 0.0193  -0.0029 132  SER A CA  
840   C C   . SER A 134  ? 0.7258 0.8393 0.7141 -0.0144 0.0188  0.0000  132  SER A C   
841   O O   . SER A 134  ? 0.7830 0.8969 0.7714 -0.0168 0.0184  0.0061  132  SER A O   
842   C CB  . SER A 134  ? 0.6741 0.8005 0.6640 -0.0138 0.0203  -0.0041 132  SER A CB  
843   N N   . HIS A 135  ? 0.7123 0.8260 0.6996 -0.0128 0.0187  -0.0041 133  HIS A N   
844   C CA  . HIS A 135  ? 0.7033 0.8191 0.6890 -0.0137 0.0183  -0.0018 133  HIS A CA  
845   C C   . HIS A 135  ? 0.7219 0.8256 0.7077 -0.0130 0.0174  -0.0014 133  HIS A C   
846   O O   . HIS A 135  ? 0.7285 0.8322 0.7134 -0.0142 0.0169  0.0019  133  HIS A O   
847   C CB  . HIS A 135  ? 0.6632 0.7895 0.6477 -0.0126 0.0187  -0.0066 133  HIS A CB  
848   C CG  . HIS A 135  ? 0.7218 0.8613 0.7060 -0.0130 0.0197  -0.0075 133  HIS A CG  
849   N ND1 . HIS A 135  ? 0.7054 0.8465 0.6911 -0.0115 0.0202  -0.0120 133  HIS A ND1 
850   C CD2 . HIS A 135  ? 0.6832 0.8354 0.6660 -0.0148 0.0202  -0.0044 133  HIS A CD2 
851   C CE1 . HIS A 135  ? 0.7065 0.8609 0.6917 -0.0122 0.0211  -0.0119 133  HIS A CE1 
852   N NE2 . HIS A 135  ? 0.7310 0.8925 0.7143 -0.0143 0.0212  -0.0072 133  HIS A NE2 
853   N N   . LEU A 136  ? 0.7351 0.8293 0.7222 -0.0113 0.0172  -0.0044 134  LEU A N   
854   C CA  . LEU A 136  ? 0.7569 0.8400 0.7441 -0.0106 0.0164  -0.0039 134  LEU A CA  
855   C C   . LEU A 136  ? 0.8067 0.8799 0.7953 -0.0100 0.0162  -0.0033 134  LEU A C   
856   O O   . LEU A 136  ? 0.7993 0.8640 0.7880 -0.0101 0.0156  -0.0010 134  LEU A O   
857   C CB  . LEU A 136  ? 0.7180 0.8003 0.7054 -0.0085 0.0162  -0.0093 134  LEU A CB  
858   C CG  . LEU A 136  ? 0.6313 0.7222 0.6175 -0.0087 0.0161  -0.0105 134  LEU A CG  
859   C CD1 . LEU A 136  ? 0.5444 0.6348 0.5317 -0.0063 0.0157  -0.0169 134  LEU A CD1 
860   C CD2 . LEU A 136  ? 0.5783 0.6666 0.5632 -0.0102 0.0156  -0.0057 134  LEU A CD2 
861   N N   . SER A 139  ? 0.5122 0.5565 0.5050 -0.0147 0.0129  0.0150  137  SER A N   
862   C CA  . SER A 139  ? 0.5159 0.5517 0.5097 -0.0145 0.0119  0.0168  137  SER A CA  
863   C C   . SER A 139  ? 0.5112 0.5403 0.5039 -0.0122 0.0122  0.0133  137  SER A C   
864   O O   . SER A 139  ? 0.4934 0.5152 0.4867 -0.0113 0.0116  0.0133  137  SER A O   
865   C CB  . SER A 139  ? 0.5067 0.5440 0.5013 -0.0161 0.0111  0.0210  137  SER A CB  
866   N N   . ARG A 140  ? 0.4046 0.4365 0.3959 -0.0111 0.0129  0.0103  138  ARG A N   
867   C CA  . ARG A 140  ? 0.3781 0.4046 0.3687 -0.0091 0.0131  0.0072  138  ARG A CA  
868   C C   . ARG A 140  ? 0.3751 0.4043 0.3655 -0.0077 0.0138  0.0029  138  ARG A C   
869   O O   . ARG A 140  ? 0.3758 0.4123 0.3658 -0.0081 0.0142  0.0016  138  ARG A O   
870   C CB  . ARG A 140  ? 0.4164 0.4433 0.4063 -0.0092 0.0129  0.0079  138  ARG A CB  
871   C CG  . ARG A 140  ? 0.4710 0.4939 0.4606 -0.0073 0.0132  0.0048  138  ARG A CG  
872   C CD  . ARG A 140  ? 0.5408 0.5660 0.5299 -0.0077 0.0130  0.0052  138  ARG A CD  
873   N NE  . ARG A 140  ? 0.6092 0.6310 0.5986 -0.0060 0.0130  0.0025  138  ARG A NE  
874   C CZ  . ARG A 140  ? 0.6038 0.6287 0.5935 -0.0051 0.0132  -0.0013 138  ARG A CZ  
875   N NH1 . ARG A 140  ? 0.5311 0.5627 0.5206 -0.0053 0.0135  -0.0031 138  ARG A NH1 
876   N NH2 . ARG A 140  ? 0.5613 0.5825 0.5520 -0.0037 0.0131  -0.0032 138  ARG A NH2 
877   N N   . SER A 141  ? 0.3423 0.3660 0.3332 -0.0062 0.0138  0.0008  139  SER A N   
878   C CA  . SER A 141  ? 0.2611 0.2864 0.2526 -0.0047 0.0142  -0.0033 139  SER A CA  
879   C C   . SER A 141  ? 0.2673 0.2953 0.2588 -0.0041 0.0143  -0.0056 139  SER A C   
880   O O   . SER A 141  ? 0.2805 0.3055 0.2717 -0.0040 0.0140  -0.0046 139  SER A O   
881   C CB  . SER A 141  ? 0.2867 0.3051 0.2789 -0.0031 0.0141  -0.0045 139  SER A CB  
882   O OG  . SER A 141  ? 0.2742 0.2938 0.2678 -0.0016 0.0142  -0.0082 139  SER A OG  
883   N N   . LEU A 142  ? 0.2802 0.3143 0.2723 -0.0036 0.0146  -0.0088 140  LEU A N   
884   C CA  . LEU A 142  ? 0.2314 0.2677 0.2241 -0.0026 0.0144  -0.0120 140  LEU A CA  
885   C C   . LEU A 142  ? 0.2205 0.2495 0.2148 -0.0010 0.0139  -0.0134 140  LEU A C   
886   O O   . LEU A 142  ? 0.2500 0.2789 0.2451 -0.0005 0.0135  -0.0149 140  LEU A O   
887   C CB  . LEU A 142  ? 0.2539 0.2973 0.2478 -0.0019 0.0146  -0.0161 140  LEU A CB  
888   C CG  . LEU A 142  ? 0.3079 0.3595 0.3014 -0.0021 0.0146  -0.0183 140  LEU A CG  
889   C CD1 . LEU A 142  ? 0.3734 0.4313 0.3645 -0.0042 0.0150  -0.0146 140  LEU A CD1 
890   C CD2 . LEU A 142  ? 0.3128 0.3699 0.3083 -0.0007 0.0146  -0.0235 140  LEU A CD2 
891   N N   . PHE A 143  ? 0.2062 0.2296 0.2012 -0.0004 0.0139  -0.0128 141  PHE A N   
892   C CA  . PHE A 143  ? 0.2118 0.2295 0.2088 0.0012  0.0134  -0.0143 141  PHE A CA  
893   C C   . PHE A 143  ? 0.2363 0.2473 0.2324 0.0012  0.0134  -0.0112 141  PHE A C   
894   O O   . PHE A 143  ? 0.2217 0.2280 0.2193 0.0024  0.0131  -0.0115 141  PHE A O   
895   C CB  . PHE A 143  ? 0.2042 0.2213 0.2029 0.0022  0.0134  -0.0162 141  PHE A CB  
896   C CG  . PHE A 143  ? 0.2046 0.2287 0.2042 0.0023  0.0135  -0.0194 141  PHE A CG  
897   C CD1 . PHE A 143  ? 0.1994 0.2274 0.2009 0.0031  0.0131  -0.0230 141  PHE A CD1 
898   C CD2 . PHE A 143  ? 0.2083 0.2359 0.2072 0.0017  0.0139  -0.0190 141  PHE A CD2 
899   C CE1 . PHE A 143  ? 0.2097 0.2449 0.2121 0.0034  0.0132  -0.0264 141  PHE A CE1 
900   C CE2 . PHE A 143  ? 0.2096 0.2445 0.2094 0.0018  0.0142  -0.0220 141  PHE A CE2 
901   C CZ  . PHE A 143  ? 0.1836 0.2225 0.1851 0.0027  0.0138  -0.0258 141  PHE A CZ  
902   N N   . VAL A 144  ? 0.2225 0.2337 0.2167 0.0000  0.0135  -0.0083 142  VAL A N   
903   C CA  . VAL A 144  ? 0.2349 0.2402 0.2283 0.0001  0.0134  -0.0056 142  VAL A CA  
904   C C   . VAL A 144  ? 0.2513 0.2533 0.2463 0.0012  0.0132  -0.0066 142  VAL A C   
905   O O   . VAL A 144  ? 0.2717 0.2688 0.2669 0.0020  0.0132  -0.0054 142  VAL A O   
906   C CB  . VAL A 144  ? 0.2477 0.2543 0.2396 -0.0015 0.0134  -0.0027 142  VAL A CB  
907   C CG1 . VAL A 144  ? 0.3036 0.3048 0.2953 -0.0011 0.0133  -0.0006 142  VAL A CG1 
908   C CG2 . VAL A 144  ? 0.3066 0.3151 0.2977 -0.0027 0.0134  -0.0009 142  VAL A CG2 
909   N N   . ASN A 145  ? 0.2100 0.2149 0.2062 0.0014  0.0129  -0.0086 143  ASN A N   
910   C CA  . ASN A 145  ? 0.2364 0.2383 0.2348 0.0024  0.0125  -0.0094 143  ASN A CA  
911   C C   . ASN A 145  ? 0.2485 0.2503 0.2501 0.0036  0.0120  -0.0125 143  ASN A C   
912   O O   . ASN A 145  ? 0.2244 0.2253 0.2288 0.0043  0.0113  -0.0139 143  ASN A O   
913   C CB  . ASN A 145  ? 0.2405 0.2448 0.2387 0.0018  0.0123  -0.0095 143  ASN A CB  
914   C CG  . ASN A 145  ? 0.2826 0.2857 0.2784 0.0007  0.0125  -0.0060 143  ASN A CG  
915   O OD1 . ASN A 145  ? 0.3335 0.3318 0.3291 0.0011  0.0127  -0.0038 143  ASN A OD1 
916   N ND2 . ASN A 145  ? 0.3195 0.3272 0.3138 -0.0005 0.0125  -0.0053 143  ASN A ND2 
917   N N   . ALA A 146  ? 0.2146 0.2173 0.2165 0.0040  0.0121  -0.0136 144  ALA A N   
918   C CA  . ALA A 146  ? 0.2114 0.2144 0.2170 0.0052  0.0114  -0.0168 144  ALA A CA  
919   C C   . ALA A 146  ? 0.2105 0.2082 0.2190 0.0062  0.0108  -0.0158 144  ALA A C   
920   O O   . ALA A 146  ? 0.2406 0.2381 0.2533 0.0072  0.0098  -0.0182 144  ALA A O   
921   C CB  . ALA A 146  ? 0.2050 0.2100 0.2105 0.0054  0.0116  -0.0179 144  ALA A CB  
922   N N   . ALA A 147  ? 0.2397 0.2333 0.2464 0.0061  0.0113  -0.0124 145  ALA A N   
923   C CA  . ALA A 147  ? 0.2548 0.2443 0.2642 0.0070  0.0108  -0.0110 145  ALA A CA  
924   C C   . ALA A 147  ? 0.2556 0.2449 0.2677 0.0071  0.0101  -0.0117 145  ALA A C   
925   O O   . ALA A 147  ? 0.2579 0.2455 0.2744 0.0078  0.0092  -0.0123 145  ALA A O   
926   C CB  . ALA A 147  ? 0.3171 0.3034 0.3238 0.0070  0.0115  -0.0075 145  ALA A CB  
927   N N   . THR A 148  ? 0.2312 0.2223 0.2411 0.0062  0.0105  -0.0116 146  THR A N   
928   C CA  . THR A 148  ? 0.2396 0.2310 0.2520 0.0062  0.0098  -0.0124 146  THR A CA  
929   C C   . THR A 148  ? 0.2153 0.2098 0.2315 0.0068  0.0087  -0.0168 146  THR A C   
930   O O   . THR A 148  ? 0.2350 0.2281 0.2560 0.0074  0.0075  -0.0179 146  THR A O   
931   C CB  . THR A 148  ? 0.2660 0.2593 0.2749 0.0051  0.0104  -0.0113 146  THR A CB  
932   O OG1 . THR A 148  ? 0.2966 0.2869 0.3027 0.0048  0.0112  -0.0077 146  THR A OG1 
933   C CG2 . THR A 148  ? 0.3125 0.3062 0.3238 0.0051  0.0096  -0.0121 146  THR A CG2 
934   N N   . TRP A 149  ? 0.2176 0.2167 0.2322 0.0065  0.0089  -0.0192 147  TRP A N   
935   C CA  . TRP A 149  ? 0.2249 0.2277 0.2433 0.0073  0.0078  -0.0239 147  TRP A CA  
936   C C   . TRP A 149  ? 0.1839 0.1839 0.2071 0.0085  0.0068  -0.0252 147  TRP A C   
937   O O   . TRP A 149  ? 0.2089 0.2097 0.2373 0.0094  0.0054  -0.0286 147  TRP A O   
938   C CB  . TRP A 149  ? 0.2164 0.2254 0.2319 0.0068  0.0084  -0.0261 147  TRP A CB  
939   C CG  . TRP A 149  ? 0.2123 0.2250 0.2242 0.0056  0.0090  -0.0253 147  TRP A CG  
940   C CD1 . TRP A 149  ? 0.2365 0.2509 0.2437 0.0043  0.0101  -0.0224 147  TRP A CD1 
941   C CD2 . TRP A 149  ? 0.2354 0.2505 0.2484 0.0055  0.0082  -0.0270 147  TRP A CD2 
942   N NE1 . TRP A 149  ? 0.2309 0.2488 0.2362 0.0034  0.0101  -0.0220 147  TRP A NE1 
943   C CE2 . TRP A 149  ? 0.2276 0.2461 0.2362 0.0042  0.0090  -0.0249 147  TRP A CE2 
944   C CE3 . TRP A 149  ? 0.2312 0.2460 0.2490 0.0065  0.0068  -0.0302 147  TRP A CE3 
945   C CZ2 . TRP A 149  ? 0.2620 0.2839 0.2703 0.0038  0.0085  -0.0258 147  TRP A CZ2 
946   C CZ3 . TRP A 149  ? 0.2907 0.3088 0.3083 0.0061  0.0063  -0.0314 147  TRP A CZ3 
947   C CH2 . TRP A 149  ? 0.3140 0.3358 0.3267 0.0048  0.0072  -0.0292 147  TRP A CH2 
948   N N   . GLY A 150  ? 0.1968 0.1937 0.2188 0.0086  0.0074  -0.0225 148  GLY A N   
949   C CA  . GLY A 150  ? 0.2316 0.2257 0.2583 0.0097  0.0064  -0.0228 148  GLY A CA  
950   C C   . GLY A 150  ? 0.2284 0.2188 0.2598 0.0101  0.0053  -0.0216 148  GLY A C   
951   O O   . GLY A 150  ? 0.2511 0.2408 0.2887 0.0110  0.0037  -0.0237 148  GLY A O   
952   N N   . LEU A 151  ? 0.2320 0.2203 0.2612 0.0094  0.0059  -0.0183 149  LEU A N   
953   C CA  A LEU A 151  ? 0.2674 0.2528 0.3012 0.0096  0.0049  -0.0169 149  LEU A CA  
954   C CA  B LEU A 151  ? 0.2673 0.2527 0.3011 0.0096  0.0049  -0.0169 149  LEU A CA  
955   C C   . LEU A 151  ? 0.2440 0.2316 0.2823 0.0099  0.0034  -0.0210 149  LEU A C   
956   O O   . LEU A 151  ? 0.2925 0.2784 0.3375 0.0105  0.0016  -0.0219 149  LEU A O   
957   C CB  A LEU A 151  ? 0.2989 0.2824 0.3291 0.0088  0.0060  -0.0128 149  LEU A CB  
958   C CB  B LEU A 151  ? 0.2993 0.2829 0.3294 0.0088  0.0060  -0.0128 149  LEU A CB  
959   C CG  A LEU A 151  ? 0.3001 0.2805 0.3293 0.0090  0.0067  -0.0084 149  LEU A CG  
960   C CG  B LEU A 151  ? 0.2950 0.2753 0.3287 0.0089  0.0055  -0.0095 149  LEU A CG  
961   C CD1 A LEU A 151  ? 0.2850 0.2646 0.3099 0.0084  0.0080  -0.0053 149  LEU A CD1 
962   C CD1 B LEU A 151  ? 0.2967 0.2749 0.3345 0.0097  0.0047  -0.0081 149  LEU A CD1 
963   C CD2 A LEU A 151  ? 0.2853 0.2634 0.3211 0.0096  0.0053  -0.0071 149  LEU A CD2 
964   C CD2 B LEU A 151  ? 0.3339 0.3131 0.3627 0.0084  0.0070  -0.0057 149  LEU A CD2 
965   N N   . VAL A 152  ? 0.2222 0.2139 0.2573 0.0094  0.0038  -0.0236 150  VAL A N   
966   C CA  . VAL A 152  ? 0.2586 0.2534 0.2974 0.0097  0.0024  -0.0280 150  VAL A CA  
967   C C   . VAL A 152  ? 0.2786 0.2747 0.3231 0.0110  0.0008  -0.0325 150  VAL A C   
968   O O   . VAL A 152  ? 0.3178 0.3135 0.3690 0.0117  -0.0011 -0.0353 150  VAL A O   
969   C CB  . VAL A 152  ? 0.2653 0.2652 0.2987 0.0089  0.0034  -0.0295 150  VAL A CB  
970   C CG1 . VAL A 152  ? 0.3100 0.3146 0.3470 0.0095  0.0019  -0.0350 150  VAL A CG1 
971   C CG2 . VAL A 152  ? 0.2840 0.2823 0.3134 0.0078  0.0044  -0.0254 150  VAL A CG2 
972   N N   . VAL A 153  ? 0.2468 0.2448 0.2892 0.0113  0.0015  -0.0335 151  VAL A N   
973   C CA  . VAL A 153  ? 0.2838 0.2840 0.3312 0.0126  0.0002  -0.0383 151  VAL A CA  
974   C C   . VAL A 153  ? 0.2671 0.2624 0.3210 0.0134  -0.0013 -0.0370 151  VAL A C   
975   O O   . VAL A 153  ? 0.3127 0.3080 0.3740 0.0145  -0.0034 -0.0406 151  VAL A O   
976   C CB  . VAL A 153  ? 0.2565 0.2612 0.2994 0.0125  0.0015  -0.0398 151  VAL A CB  
977   C CG1 . VAL A 153  ? 0.2845 0.2914 0.3328 0.0140  0.0001  -0.0446 151  VAL A CG1 
978   C CG2 . VAL A 153  ? 0.2546 0.2650 0.2921 0.0117  0.0026  -0.0412 151  VAL A CG2 
979   N N   . THR A 154  ? 0.2654 0.2568 0.3169 0.0129  -0.0003 -0.0319 152  THR A N   
980   C CA  . THR A 154  ? 0.2710 0.2588 0.3280 0.0136  -0.0015 -0.0301 152  THR A CA  
981   C C   . THR A 154  ? 0.3241 0.3073 0.3841 0.0133  -0.0021 -0.0255 152  THR A C   
982   O O   . THR A 154  ? 0.3441 0.3245 0.4101 0.0138  -0.0036 -0.0240 152  THR A O   
983   C CB  . THR A 154  ? 0.3042 0.2917 0.3569 0.0136  -0.0002 -0.0279 152  THR A CB  
984   O OG1 . THR A 154  ? 0.3101 0.2955 0.3567 0.0126  0.0016  -0.0228 152  THR A OG1 
985   C CG2 . THR A 154  ? 0.2946 0.2870 0.3436 0.0137  0.0008  -0.0317 152  THR A CG2 
986   N N   . GLY A 155  ? 0.2921 0.2747 0.3482 0.0123  -0.0010 -0.0229 153  GLY A N   
987   C CA  . GLY A 155  ? 0.2868 0.2658 0.3448 0.0119  -0.0012 -0.0179 153  GLY A CA  
988   C C   . GLY A 155  ? 0.3569 0.3340 0.4110 0.0116  0.0002  -0.0129 153  GLY A C   
989   O O   . GLY A 155  ? 0.3332 0.3080 0.3885 0.0113  0.0003  -0.0085 153  GLY A O   
990   N N   . LYS A 156  ? 0.3227 0.3012 0.3723 0.0118  0.0013  -0.0135 154  LYS A N   
991   C CA  . LYS A 156  ? 0.3394 0.3166 0.3852 0.0117  0.0025  -0.0095 154  LYS A CA  
992   C C   . LYS A 156  ? 0.3510 0.3294 0.3885 0.0111  0.0046  -0.0088 154  LYS A C   
993   O O   . LYS A 156  ? 0.3088 0.2898 0.3434 0.0108  0.0051  -0.0120 154  LYS A O   
994   C CB  . LYS A 156  ? 0.4171 0.3944 0.4651 0.0125  0.0018  -0.0105 154  LYS A CB  
995   N N   . LEU A 157  ? 0.3168 0.2938 0.3507 0.0108  0.0057  -0.0047 155  LEU A N   
996   C CA  . LEU A 157  ? 0.3516 0.3295 0.3785 0.0103  0.0075  -0.0039 155  LEU A CA  
997   C C   . LEU A 157  ? 0.4322 0.4103 0.4563 0.0106  0.0080  -0.0034 155  LEU A C   
998   O O   . LEU A 157  ? 0.4350 0.4120 0.4609 0.0112  0.0076  -0.0012 155  LEU A O   
999   C CB  . LEU A 157  ? 0.3388 0.3153 0.3637 0.0100  0.0083  -0.0002 155  LEU A CB  
1000  C CG  . LEU A 157  ? 0.3954 0.3723 0.4138 0.0096  0.0098  0.0009  155  LEU A CG  
1001  C CD1 . LEU A 157  ? 0.3829 0.3616 0.3988 0.0089  0.0102  -0.0018 155  LEU A CD1 
1002  C CD2 . LEU A 157  ? 0.4052 0.3811 0.4226 0.0096  0.0105  0.0042  155  LEU A CD2 
1003  N N   . THR A 158  ? 0.4826 0.4624 0.5024 0.0102  0.0088  -0.0053 156  THR A N   
1004  C CA  . THR A 158  ? 0.4895 0.4696 0.5060 0.0103  0.0094  -0.0047 156  THR A CA  
1005  C C   . THR A 158  ? 0.5088 0.4892 0.5198 0.0096  0.0107  -0.0037 156  THR A C   
1006  O O   . THR A 158  ? 0.5661 0.5480 0.5756 0.0089  0.0110  -0.0051 156  THR A O   
1007  C CB  . THR A 158  ? 0.5569 0.5393 0.5745 0.0105  0.0090  -0.0081 156  THR A CB  
1008  O OG1 . THR A 158  ? 0.5629 0.5452 0.5865 0.0112  0.0076  -0.0099 156  THR A OG1 
1009  C CG2 . THR A 158  ? 0.6019 0.5842 0.6173 0.0107  0.0093  -0.0072 156  THR A CG2 
1010  N N   . SER A 159  ? 0.3885 0.3677 0.3969 0.0099  0.0112  -0.0012 157  SER A N   
1011  C CA  . SER A 159  ? 0.3189 0.2978 0.3230 0.0095  0.0121  -0.0001 157  SER A CA  
1012  C C   . SER A 159  ? 0.3705 0.3510 0.3720 0.0086  0.0124  -0.0018 157  SER A C   
1013  O O   . SER A 159  ? 0.4384 0.4192 0.4378 0.0079  0.0128  -0.0016 157  SER A O   
1014  C CB  . SER A 159  ? 0.4307 0.4086 0.4330 0.0102  0.0125  0.0022  157  SER A CB  
1015  O OG  . SER A 159  ? 0.4894 0.4677 0.4923 0.0107  0.0120  0.0020  157  SER A OG  
1016  N N   . THR A 160  ? 0.3273 0.3090 0.3293 0.0087  0.0121  -0.0033 158  THR A N   
1017  C CA  . THR A 160  ? 0.2944 0.2782 0.2945 0.0079  0.0124  -0.0046 158  THR A CA  
1018  C C   . THR A 160  ? 0.2659 0.2523 0.2684 0.0078  0.0120  -0.0074 158  THR A C   
1019  O O   . THR A 160  ? 0.3081 0.2943 0.3141 0.0086  0.0113  -0.0084 158  THR A O   
1020  C CB  . THR A 160  ? 0.2974 0.2807 0.2956 0.0081  0.0124  -0.0041 158  THR A CB  
1021  O OG1 . THR A 160  ? 0.3299 0.3131 0.3303 0.0090  0.0119  -0.0047 158  THR A OG1 
1022  C CG2 . THR A 160  ? 0.3856 0.3668 0.3816 0.0084  0.0127  -0.0020 158  THR A CG2 
1023  N N   . VAL A 161  ? 0.2206 0.2099 0.2216 0.0068  0.0123  -0.0085 159  VAL A N   
1024  C CA  . VAL A 161  ? 0.2240 0.2173 0.2268 0.0066  0.0121  -0.0113 159  VAL A CA  
1025  C C   . VAL A 161  ? 0.2041 0.1994 0.2071 0.0067  0.0120  -0.0126 159  VAL A C   
1026  O O   . VAL A 161  ? 0.2023 0.1979 0.2029 0.0060  0.0124  -0.0113 159  VAL A O   
1027  C CB  . VAL A 161  ? 0.2452 0.2414 0.2459 0.0053  0.0126  -0.0112 159  VAL A CB  
1028  C CG1 . VAL A 161  ? 0.2565 0.2580 0.2581 0.0050  0.0125  -0.0140 159  VAL A CG1 
1029  C CG2 . VAL A 161  ? 0.2878 0.2822 0.2886 0.0053  0.0125  -0.0102 159  VAL A CG2 
1030  N N   . ASN A 162  ? 0.1891 0.1858 0.1954 0.0076  0.0115  -0.0151 160  ASN A N   
1031  C CA  . ASN A 162  ? 0.1875 0.1869 0.1942 0.0076  0.0114  -0.0167 160  ASN A CA  
1032  C C   . ASN A 162  ? 0.1822 0.1872 0.1881 0.0067  0.0119  -0.0185 160  ASN A C   
1033  O O   . ASN A 162  ? 0.1816 0.1901 0.1900 0.0073  0.0116  -0.0217 160  ASN A O   
1034  C CB  . ASN A 162  ? 0.1790 0.1778 0.1899 0.0091  0.0105  -0.0186 160  ASN A CB  
1035  C CG  . ASN A 162  ? 0.1888 0.1901 0.2002 0.0092  0.0105  -0.0199 160  ASN A CG  
1036  O OD1 . ASN A 162  ? 0.2033 0.2082 0.2125 0.0082  0.0112  -0.0202 160  ASN A OD1 
1037  N ND2 . ASN A 162  ? 0.2495 0.2492 0.2640 0.0104  0.0097  -0.0205 160  ASN A ND2 
1038  N N   . ASP A 163  ? 0.1703 0.1766 0.1729 0.0053  0.0126  -0.0165 161  ASP A N   
1039  C CA  . ASP A 163  ? 0.1785 0.1907 0.1801 0.0042  0.0131  -0.0173 161  ASP A CA  
1040  C C   . ASP A 163  ? 0.1747 0.1922 0.1775 0.0043  0.0132  -0.0198 161  ASP A C   
1041  O O   . ASP A 163  ? 0.1773 0.2008 0.1803 0.0039  0.0135  -0.0217 161  ASP A O   
1042  C CB  . ASP A 163  ? 0.2047 0.2168 0.2032 0.0026  0.0135  -0.0139 161  ASP A CB  
1043  C CG  . ASP A 163  ? 0.2282 0.2373 0.2257 0.0022  0.0135  -0.0117 161  ASP A CG  
1044  O OD1 . ASP A 163  ? 0.2145 0.2193 0.2126 0.0033  0.0131  -0.0117 161  ASP A OD1 
1045  O OD2 . ASP A 163  ? 0.2554 0.2665 0.2516 0.0008  0.0136  -0.0098 161  ASP A OD2 
1046  N N   . ARG A 164  ? 0.1785 0.1944 0.1824 0.0049  0.0130  -0.0199 162  ARG A N   
1047  C CA  A ARG A 164  ? 0.1686 0.1897 0.1741 0.0051  0.0131  -0.0224 162  ARG A CA  
1048  C CA  B ARG A 164  ? 0.1696 0.1906 0.1751 0.0051  0.0131  -0.0224 162  ARG A CA  
1049  C C   . ARG A 164  ? 0.1597 0.1826 0.1690 0.0067  0.0125  -0.0266 162  ARG A C   
1050  O O   . ARG A 164  ? 0.1697 0.1989 0.1801 0.0069  0.0127  -0.0296 162  ARG A O   
1051  C CB  A ARG A 164  ? 0.1933 0.2123 0.1989 0.0052  0.0129  -0.0213 162  ARG A CB  
1052  C CB  B ARG A 164  ? 0.1934 0.2121 0.1991 0.0053  0.0128  -0.0213 162  ARG A CB  
1053  C CG  A ARG A 164  ? 0.1907 0.2091 0.1933 0.0036  0.0133  -0.0179 162  ARG A CG  
1054  C CG  B ARG A 164  ? 0.2009 0.2178 0.2036 0.0038  0.0131  -0.0177 162  ARG A CG  
1055  C CD  A ARG A 164  ? 0.2409 0.2648 0.2421 0.0019  0.0139  -0.0170 162  ARG A CD  
1056  C CD  B ARG A 164  ? 0.2315 0.2543 0.2336 0.0023  0.0137  -0.0172 162  ARG A CD  
1057  N NE  A ARG A 164  ? 0.2974 0.3288 0.2998 0.0018  0.0144  -0.0195 162  ARG A NE  
1058  N NE  B ARG A 164  ? 0.2725 0.3017 0.2743 0.0016  0.0143  -0.0183 162  ARG A NE  
1059  C CZ  A ARG A 164  ? 0.2942 0.3322 0.2957 0.0007  0.0150  -0.0194 162  ARG A CZ  
1060  C CZ  B ARG A 164  ? 0.2835 0.3133 0.2835 0.0006  0.0145  -0.0164 162  ARG A CZ  
1061  N NH1 A ARG A 164  ? 0.3193 0.3569 0.3188 -0.0005 0.0151  -0.0169 162  ARG A NH1 
1062  N NH1 B ARG A 164  ? 0.3085 0.3326 0.3069 0.0001  0.0142  -0.0136 162  ARG A NH1 
1063  N NH2 A ARG A 164  ? 0.2778 0.3233 0.2806 0.0009  0.0154  -0.0221 162  ARG A NH2 
1064  N NH2 B ARG A 164  ? 0.3164 0.3529 0.3161 0.0000  0.0150  -0.0175 162  ARG A NH2 
1065  N N   . SER A 165  ? 0.1509 0.1686 0.1624 0.0079  0.0116  -0.0268 163  SER A N   
1066  C CA  . SER A 165  ? 0.1458 0.1646 0.1617 0.0094  0.0107  -0.0307 163  SER A CA  
1067  C C   . SER A 165  ? 0.1607 0.1838 0.1763 0.0091  0.0109  -0.0328 163  SER A C   
1068  O O   . SER A 165  ? 0.1511 0.1792 0.1696 0.0100  0.0105  -0.0370 163  SER A O   
1069  C CB  . SER A 165  ? 0.1719 0.1841 0.1905 0.0105  0.0097  -0.0295 163  SER A CB  
1070  O OG  . SER A 165  ? 0.1868 0.1996 0.2103 0.0117  0.0086  -0.0329 163  SER A OG  
1071  N N   . LEU A 166  ? 0.1577 0.1792 0.1703 0.0080  0.0114  -0.0300 164  LEU A N   
1072  C CA  . LEU A 166  ? 0.1628 0.1885 0.1748 0.0076  0.0115  -0.0316 164  LEU A CA  
1073  C C   . LEU A 166  ? 0.1538 0.1879 0.1639 0.0068  0.0124  -0.0329 164  LEU A C   
1074  O O   . LEU A 166  ? 0.1574 0.1974 0.1687 0.0072  0.0122  -0.0364 164  LEU A O   
1075  C CB  . LEU A 166  ? 0.1627 0.1847 0.1718 0.0066  0.0119  -0.0279 164  LEU A CB  
1076  C CG  . LEU A 166  ? 0.1570 0.1723 0.1684 0.0075  0.0110  -0.0270 164  LEU A CG  
1077  C CD1 . LEU A 166  ? 0.1883 0.2000 0.1964 0.0065  0.0115  -0.0232 164  LEU A CD1 
1078  C CD2 . LEU A 166  ? 0.1856 0.2021 0.2014 0.0087  0.0099  -0.0309 164  LEU A CD2 
1079  N N   . ALA A 167  ? 0.1539 0.1891 0.1613 0.0055  0.0132  -0.0301 165  ALA A N   
1080  C CA  . ALA A 167  ? 0.1705 0.2142 0.1764 0.0046  0.0140  -0.0307 165  ALA A CA  
1081  C C   . ALA A 167  ? 0.1610 0.2101 0.1701 0.0060  0.0138  -0.0356 165  ALA A C   
1082  O O   . ALA A 167  ? 0.1654 0.2228 0.1747 0.0060  0.0141  -0.0384 165  ALA A O   
1083  C CB  . ALA A 167  ? 0.1886 0.2318 0.1920 0.0029  0.0147  -0.0266 165  ALA A CB  
1084  N N   . ALA A 168  ? 0.1619 0.2069 0.1739 0.0072  0.0131  -0.0367 166  ALA A N   
1085  C CA  . ALA A 168  ? 0.1569 0.2065 0.1728 0.0088  0.0127  -0.0416 166  ALA A CA  
1086  C C   . ALA A 168  ? 0.1492 0.2009 0.1683 0.0103  0.0118  -0.0463 166  ALA A C   
1087  O O   . ALA A 168  ? 0.1682 0.2278 0.1891 0.0111  0.0118  -0.0508 166  ALA A O   
1088  C CB  . ALA A 168  ? 0.1595 0.2030 0.1781 0.0099  0.0119  -0.0414 166  ALA A CB  
1089  N N   . ALA A 169  ? 0.1563 0.2016 0.1764 0.0106  0.0110  -0.0454 167  ALA A N   
1090  C CA  . ALA A 169  ? 0.1456 0.1921 0.1694 0.0120  0.0098  -0.0498 167  ALA A CA  
1091  C C   . ALA A 169  ? 0.1594 0.2139 0.1808 0.0113  0.0104  -0.0514 167  ALA A C   
1092  O O   . ALA A 169  ? 0.1587 0.2187 0.1830 0.0126  0.0097  -0.0567 167  ALA A O   
1093  C CB  . ALA A 169  ? 0.1575 0.1954 0.1828 0.0122  0.0089  -0.0475 167  ALA A CB  
1094  N N   . LEU A 170  ? 0.1490 0.2041 0.1651 0.0093  0.0116  -0.0470 168  LEU A N   
1095  C CA  . LEU A 170  ? 0.1544 0.2175 0.1679 0.0085  0.0122  -0.0478 168  LEU A CA  
1096  C C   . LEU A 170  ? 0.1613 0.2349 0.1747 0.0087  0.0129  -0.0508 168  LEU A C   
1097  O O   . LEU A 170  ? 0.1592 0.2408 0.1735 0.0094  0.0127  -0.0552 168  LEU A O   
1098  C CB  . LEU A 170  ? 0.1840 0.2451 0.1926 0.0063  0.0131  -0.0418 168  LEU A CB  
1099  C CG  . LEU A 170  ? 0.1752 0.2438 0.1812 0.0053  0.0135  -0.0418 168  LEU A CG  
1100  C CD1 . LEU A 170  ? 0.1912 0.2599 0.1998 0.0066  0.0124  -0.0459 168  LEU A CD1 
1101  C CD2 . LEU A 170  ? 0.1978 0.2631 0.1998 0.0032  0.0141  -0.0356 168  LEU A CD2 
1102  N N   . THR A 171  ? 0.1657 0.2401 0.1781 0.0080  0.0137  -0.0487 169  THR A N   
1103  C CA  . THR A 171  ? 0.1781 0.2627 0.1907 0.0082  0.0145  -0.0515 169  THR A CA  
1104  C C   . THR A 171  ? 0.1581 0.2457 0.1758 0.0108  0.0134  -0.0587 169  THR A C   
1105  O O   . THR A 171  ? 0.1638 0.2615 0.1820 0.0115  0.0136  -0.0630 169  THR A O   
1106  C CB  . THR A 171  ? 0.1891 0.2721 0.2009 0.0073  0.0152  -0.0483 169  THR A CB  
1107  O OG1 . THR A 171  ? 0.2244 0.3046 0.2321 0.0050  0.0159  -0.0419 169  THR A OG1 
1108  C CG2 . THR A 171  ? 0.2061 0.2998 0.2185 0.0076  0.0160  -0.0511 169  THR A CG2 
1109  N N   . ARG A 172  ? 0.1565 0.2358 0.1784 0.0123  0.0121  -0.0600 170  ARG A N   
1110  C CA  . ARG A 172  ? 0.1441 0.2254 0.1720 0.0148  0.0107  -0.0667 170  ARG A CA  
1111  C C   . ARG A 172  ? 0.1581 0.2436 0.1877 0.0158  0.0098  -0.0713 170  ARG A C   
1112  O O   . ARG A 172  ? 0.1649 0.2588 0.1972 0.0173  0.0094  -0.0774 170  ARG A O   
1113  C CB  . ARG A 172  ? 0.1623 0.2332 0.1946 0.0159  0.0093  -0.0662 170  ARG A CB  
1114  C CG  . ARG A 172  ? 0.1424 0.2151 0.1816 0.0184  0.0078  -0.0725 170  ARG A CG  
1115  C CD  . ARG A 172  ? 0.1634 0.2260 0.2076 0.0194  0.0061  -0.0716 170  ARG A CD  
1116  N NE  . ARG A 172  ? 0.1495 0.2055 0.1905 0.0181  0.0069  -0.0654 170  ARG A NE  
1117  C CZ  . ARG A 172  ? 0.1459 0.1942 0.1844 0.0169  0.0070  -0.0603 170  ARG A CZ  
1118  N NH1 . ARG A 172  ? 0.1631 0.2088 0.2020 0.0168  0.0064  -0.0602 170  ARG A NH1 
1119  N NH2 . ARG A 172  ? 0.1626 0.2062 0.1984 0.0159  0.0077  -0.0554 170  ARG A NH2 
1120  N N   . LEU A 173  ? 0.1592 0.2391 0.1874 0.0150  0.0094  -0.0688 171  LEU A N   
1121  C CA  . LEU A 173  ? 0.1645 0.2475 0.1951 0.0161  0.0082  -0.0734 171  LEU A CA  
1122  C C   . LEU A 173  ? 0.1737 0.2687 0.2005 0.0154  0.0093  -0.0750 171  LEU A C   
1123  O O   . LEU A 173  ? 0.1699 0.2718 0.1993 0.0170  0.0084  -0.0812 171  LEU A O   
1124  C CB  . LEU A 173  ? 0.1852 0.2592 0.2157 0.0154  0.0074  -0.0701 171  LEU A CB  
1125  C CG  . LEU A 173  ? 0.1904 0.2632 0.2147 0.0131  0.0087  -0.0642 171  LEU A CG  
1126  C CD1 . LEU A 173  ? 0.2074 0.2878 0.2300 0.0129  0.0086  -0.0666 171  LEU A CD1 
1127  C CD2 . LEU A 173  ? 0.1859 0.2473 0.2107 0.0127  0.0081  -0.0598 171  LEU A CD2 
1128  N N   . ILE A 174  ? 0.1675 0.2652 0.1882 0.0131  0.0111  -0.0695 172  ILE A N   
1129  C CA  . ILE A 174  ? 0.1655 0.2754 0.1826 0.0123  0.0122  -0.0703 172  ILE A CA  
1130  C C   . ILE A 174  ? 0.1741 0.2944 0.1930 0.0136  0.0126  -0.0754 172  ILE A C   
1131  O O   . ILE A 174  ? 0.1749 0.3058 0.1941 0.0146  0.0125  -0.0804 172  ILE A O   
1132  C CB  . ILE A 174  ? 0.1695 0.2795 0.1806 0.0094  0.0137  -0.0626 172  ILE A CB  
1133  C CG1 . ILE A 174  ? 0.1894 0.2912 0.1988 0.0083  0.0133  -0.0586 172  ILE A CG1 
1134  C CG2 . ILE A 174  ? 0.2195 0.3435 0.2271 0.0084  0.0150  -0.0628 172  ILE A CG2 
1135  C CD1 . ILE A 174  ? 0.2296 0.3291 0.2342 0.0057  0.0144  -0.0509 172  ILE A CD1 
1136  N N   . SER A 175  ? 0.1846 0.3025 0.2048 0.0138  0.0130  -0.0744 173  SER A N   
1137  C CA  . SER A 175  ? 0.1634 0.2915 0.1855 0.0151  0.0135  -0.0792 173  SER A CA  
1138  C C   . SER A 175  ? 0.1879 0.3179 0.2164 0.0181  0.0117  -0.0878 173  SER A C   
1139  O O   . SER A 175  ? 0.2142 0.3554 0.2441 0.0195  0.0119  -0.0934 173  SER A O   
1140  C CB  . SER A 175  ? 0.2095 0.3337 0.2321 0.0146  0.0142  -0.0762 173  SER A CB  
1141  O OG  . SER A 175  ? 0.2713 0.3960 0.2885 0.0118  0.0157  -0.0690 173  SER A OG  
1142  N N   . ARG A 176  ? 0.1692 0.2887 0.2017 0.0192  0.0099  -0.0889 174  ARG A N   
1143  C CA  . ARG A 176  ? 0.1794 0.2997 0.2191 0.0221  0.0078  -0.0969 174  ARG A CA  
1144  C C   . ARG A 176  ? 0.2127 0.3391 0.2528 0.0228  0.0069  -0.1014 174  ARG A C   
1145  O O   . ARG A 176  ? 0.2337 0.3683 0.2777 0.0251  0.0059  -0.1091 174  ARG A O   
1146  C CB  . ARG A 176  ? 0.1946 0.3012 0.2394 0.0229  0.0060  -0.0957 174  ARG A CB  
1147  C CG  . ARG A 176  ? 0.2088 0.3148 0.2625 0.0258  0.0035  -0.1034 174  ARG A CG  
1148  C CD  . ARG A 176  ? 0.2127 0.3054 0.2713 0.0262  0.0018  -0.1008 174  ARG A CD  
1149  N NE  . ARG A 176  ? 0.2158 0.3006 0.2738 0.0252  0.0011  -0.0973 174  ARG A NE  
1150  C CZ  . ARG A 176  ? 0.2198 0.2957 0.2742 0.0233  0.0018  -0.0899 174  ARG A CZ  
1151  N NH1 . ARG A 176  ? 0.1893 0.2621 0.2406 0.0222  0.0032  -0.0848 174  ARG A NH1 
1152  N NH2 . ARG A 176  ? 0.2628 0.3332 0.3170 0.0226  0.0011  -0.0876 174  ARG A NH2 
1153  N N   . CYS A 177  ? 0.1949 0.3176 0.2308 0.0211  0.0072  -0.0968 175  CYS A N   
1154  C CA  . CYS A 177  ? 0.2135 0.3397 0.2504 0.0218  0.0060  -0.1007 175  CYS A CA  
1155  C C   . CYS A 177  ? 0.2162 0.3515 0.2461 0.0199  0.0075  -0.0981 175  CYS A C   
1156  O O   . CYS A 177  ? 0.2577 0.3989 0.2882 0.0207  0.0066  -0.1024 175  CYS A O   
1157  C CB  . CYS A 177  ? 0.2308 0.3443 0.2705 0.0216  0.0043  -0.0985 175  CYS A CB  
1158  S SG  . CYS A 177  ? 0.2762 0.3781 0.3245 0.0235  0.0022  -0.1004 175  CYS A SG  
1159  N N   . GLY A 178  ? 0.2394 0.3761 0.2633 0.0175  0.0096  -0.0912 176  GLY A N   
1160  C CA  . GLY A 178  ? 0.2225 0.3699 0.2405 0.0158  0.0111  -0.0888 176  GLY A CA  
1161  C C   . GLY A 178  ? 0.2072 0.3521 0.2225 0.0146  0.0106  -0.0860 176  GLY A C   
1162  O O   . GLY A 178  ? 0.2164 0.3495 0.2331 0.0143  0.0096  -0.0836 176  GLY A O   
1163  N N   . GLU A 179  ? 0.2218 0.3787 0.2332 0.0139  0.0113  -0.0864 177  GLU A N   
1164  C CA  . GLU A 179  ? 0.2211 0.3777 0.2296 0.0126  0.0110  -0.0836 177  GLU A CA  
1165  C C   . GLU A 179  ? 0.1961 0.3454 0.2092 0.0142  0.0087  -0.0880 177  GLU A C   
1166  O O   . GLU A 179  ? 0.2347 0.3759 0.2463 0.0129  0.0084  -0.0835 177  GLU A O   
1167  C CB  . GLU A 179  ? 0.2322 0.4048 0.2366 0.0119  0.0118  -0.0846 177  GLU A CB  
1168  C CG  . GLU A 179  ? 0.3308 0.5040 0.3315 0.0102  0.0116  -0.0806 177  GLU A CG  
1169  C CD  . GLU A 179  ? 0.4575 0.6331 0.4609 0.0122  0.0097  -0.0874 177  GLU A CD  
1170  O OE1 . GLU A 179  ? 0.5007 0.6824 0.5081 0.0147  0.0087  -0.0958 177  GLU A OE1 
1171  O OE2 . GLU A 179  ? 0.5286 0.7001 0.5306 0.0111  0.0090  -0.0846 177  GLU A OE2 
1172  N N   . PRO A 180  ? 0.2039 0.3555 0.2227 0.0170  0.0071  -0.0965 178  PRO A N   
1173  C CA  . PRO A 180  ? 0.2208 0.3656 0.2444 0.0183  0.0047  -0.1002 178  PRO A CA  
1174  C C   . PRO A 180  ? 0.2077 0.3366 0.2332 0.0175  0.0042  -0.0951 178  PRO A C   
1175  O O   . PRO A 180  ? 0.2253 0.3487 0.2512 0.0170  0.0032  -0.0937 178  PRO A O   
1176  C CB  . PRO A 180  ? 0.2596 0.4090 0.2901 0.0215  0.0030  -0.1100 178  PRO A CB  
1177  C CG  . PRO A 180  ? 0.2507 0.4147 0.2779 0.0217  0.0046  -0.1124 178  PRO A CG  
1178  C CD  . PRO A 180  ? 0.2096 0.3720 0.2309 0.0190  0.0071  -0.1036 178  PRO A CD  
1179  N N   . VAL A 181  ? 0.2035 0.3254 0.2299 0.0173  0.0049  -0.0921 179  VAL A N   
1180  C CA  . VAL A 181  ? 0.2089 0.3165 0.2368 0.0166  0.0044  -0.0872 179  VAL A CA  
1181  C C   . VAL A 181  ? 0.1956 0.2996 0.2172 0.0139  0.0059  -0.0789 179  VAL A C   
1182  O O   . VAL A 181  ? 0.1915 0.2864 0.2138 0.0133  0.0052  -0.0757 179  VAL A O   
1183  C CB  . VAL A 181  ? 0.2019 0.3031 0.2331 0.0173  0.0044  -0.0867 179  VAL A CB  
1184  C CG1 . VAL A 181  ? 0.2031 0.3072 0.2290 0.0157  0.0067  -0.0818 179  VAL A CG1 
1185  C CG2 . VAL A 181  ? 0.2582 0.3457 0.2925 0.0172  0.0034  -0.0831 179  VAL A CG2 
1186  N N   . ILE A 182  ? 0.2089 0.3202 0.2247 0.0123  0.0078  -0.0754 180  ILE A N   
1187  C CA  . ILE A 182  ? 0.2081 0.3165 0.2185 0.0097  0.0089  -0.0677 180  ILE A CA  
1188  C C   . ILE A 182  ? 0.2524 0.3626 0.2621 0.0094  0.0080  -0.0682 180  ILE A C   
1189  O O   . ILE A 182  ? 0.2202 0.3224 0.2288 0.0083  0.0078  -0.0637 180  ILE A O   
1190  C CB  . ILE A 182  ? 0.2112 0.3281 0.2166 0.0080  0.0108  -0.0639 180  ILE A CB  
1191  C CG1 . ILE A 182  ? 0.2159 0.3310 0.2225 0.0083  0.0116  -0.0636 180  ILE A CG1 
1192  C CG2 . ILE A 182  ? 0.2221 0.3357 0.2228 0.0054  0.0117  -0.0561 180  ILE A CG2 
1193  C CD1 . ILE A 182  ? 0.2614 0.3867 0.2642 0.0070  0.0133  -0.0613 180  ILE A CD1 
1194  N N   . ARG A 183  ? 0.2245 0.3456 0.2345 0.0105  0.0074  -0.0738 181  ARG A N   
1195  C CA  A ARG A 183  ? 0.2586 0.3824 0.2682 0.0104  0.0064  -0.0752 181  ARG A CA  
1196  C CA  B ARG A 183  ? 0.2580 0.3820 0.2677 0.0104  0.0064  -0.0753 181  ARG A CA  
1197  C C   . ARG A 183  ? 0.2613 0.3739 0.2757 0.0113  0.0046  -0.0764 181  ARG A C   
1198  O O   . ARG A 183  ? 0.2498 0.3580 0.2628 0.0102  0.0043  -0.0729 181  ARG A O   
1199  C CB  A ARG A 183  ? 0.2692 0.4068 0.2794 0.0119  0.0058  -0.0825 181  ARG A CB  
1200  C CB  B ARG A 183  ? 0.2666 0.4040 0.2774 0.0121  0.0057  -0.0830 181  ARG A CB  
1201  C CG  A ARG A 183  ? 0.3341 0.4751 0.3449 0.0123  0.0042  -0.0856 181  ARG A CG  
1202  C CG  B ARG A 183  ? 0.3362 0.4787 0.3466 0.0123  0.0044  -0.0857 181  ARG A CG  
1203  C CD  A ARG A 183  ? 0.3307 0.4701 0.3365 0.0098  0.0050  -0.0782 181  ARG A CD  
1204  C CD  B ARG A 183  ? 0.3688 0.5176 0.3725 0.0098  0.0058  -0.0794 181  ARG A CD  
1205  N NE  A ARG A 183  ? 0.3389 0.4853 0.3387 0.0078  0.0070  -0.0725 181  ARG A NE  
1206  N NE  B ARG A 183  ? 0.3217 0.4596 0.3238 0.0080  0.0059  -0.0723 181  ARG A NE  
1207  C CZ  A ARG A 183  ? 0.3649 0.5084 0.3606 0.0054  0.0079  -0.0647 181  ARG A CZ  
1208  C CZ  B ARG A 183  ? 0.3667 0.5052 0.3637 0.0056  0.0073  -0.0648 181  ARG A CZ  
1209  N NH1 A ARG A 183  ? 0.3555 0.4892 0.3518 0.0048  0.0071  -0.0616 181  ARG A NH1 
1210  N NH1 B ARG A 183  ? 0.3781 0.5272 0.3711 0.0044  0.0087  -0.0625 181  ARG A NH1 
1211  N NH2 A ARG A 183  ? 0.3805 0.5311 0.3718 0.0035  0.0095  -0.0598 181  ARG A NH2 
1212  N NH2 B ARG A 183  ? 0.3543 0.4830 0.3506 0.0043  0.0071  -0.0593 181  ARG A NH2 
1213  N N   . ARG A 184  ? 0.2348 0.3428 0.2553 0.0133  0.0033  -0.0812 182  ARG A N   
1214  C CA  . ARG A 184  ? 0.2377 0.3356 0.2637 0.0142  0.0014  -0.0822 182  ARG A CA  
1215  C C   . ARG A 184  ? 0.2574 0.3438 0.2816 0.0126  0.0023  -0.0745 182  ARG A C   
1216  O O   . ARG A 184  ? 0.2619 0.3420 0.2873 0.0121  0.0014  -0.0725 182  ARG A O   
1217  C CB  . ARG A 184  ? 0.2430 0.3389 0.2766 0.0166  -0.0002 -0.0886 182  ARG A CB  
1218  C CG  . ARG A 184  ? 0.3191 0.4246 0.3564 0.0186  -0.0019 -0.0975 182  ARG A CG  
1219  C CD  . ARG A 184  ? 0.3092 0.4102 0.3523 0.0196  -0.0045 -0.1009 182  ARG A CD  
1220  N NE  . ARG A 184  ? 0.3955 0.4878 0.4471 0.0211  -0.0065 -0.1034 182  ARG A NE  
1221  C CZ  . ARG A 184  ? 0.3815 0.4626 0.4366 0.0206  -0.0075 -0.0996 182  ARG A CZ  
1222  N NH1 . ARG A 184  ? 0.3697 0.4464 0.4207 0.0188  -0.0067 -0.0937 182  ARG A NH1 
1223  N NH2 . ARG A 184  ? 0.3158 0.3901 0.3789 0.0220  -0.0093 -0.1018 182  ARG A NH2 
1224  N N   . GLY A 185  ? 0.2278 0.3118 0.2493 0.0117  0.0039  -0.0702 183  GLY A N   
1225  C CA  . GLY A 185  ? 0.2273 0.3012 0.2466 0.0102  0.0047  -0.0631 183  GLY A CA  
1226  C C   . GLY A 185  ? 0.2280 0.3025 0.2423 0.0083  0.0055  -0.0581 183  GLY A C   
1227  O O   . GLY A 185  ? 0.2227 0.2893 0.2374 0.0077  0.0052  -0.0545 183  GLY A O   
1228  N N   . VAL A 186  ? 0.2222 0.3065 0.2321 0.0073  0.0065  -0.0576 184  VAL A N   
1229  C CA  . VAL A 186  ? 0.2530 0.3386 0.2585 0.0054  0.0071  -0.0526 184  VAL A CA  
1230  C C   . VAL A 186  ? 0.2542 0.3382 0.2618 0.0059  0.0055  -0.0546 184  VAL A C   
1231  O O   . VAL A 186  ? 0.2475 0.3255 0.2540 0.0048  0.0056  -0.0501 184  VAL A O   
1232  C CB  . VAL A 186  ? 0.2570 0.3545 0.2579 0.0043  0.0081  -0.0519 184  VAL A CB  
1233  C CG1 . VAL A 186  ? 0.2656 0.3659 0.2630 0.0026  0.0082  -0.0478 184  VAL A CG1 
1234  C CG2 . VAL A 186  ? 0.2566 0.3539 0.2551 0.0032  0.0097  -0.0478 184  VAL A CG2 
1235  N N   . ASP A 187  ? 0.2268 0.3164 0.2379 0.0076  0.0041  -0.0615 185  ASP A N   
1236  C CA  . ASP A 187  ? 0.2725 0.3611 0.2862 0.0081  0.0025  -0.0639 185  ASP A CA  
1237  C C   . ASP A 187  ? 0.2964 0.3727 0.3144 0.0084  0.0015  -0.0623 185  ASP A C   
1238  O O   . ASP A 187  ? 0.2881 0.3604 0.3062 0.0078  0.0010  -0.0600 185  ASP A O   
1239  C CB  . ASP A 187  ? 0.2650 0.3621 0.2823 0.0100  0.0009  -0.0724 185  ASP A CB  
1240  C CG  . ASP A 187  ? 0.3163 0.4272 0.3289 0.0096  0.0017  -0.0739 185  ASP A CG  
1241  O OD1 . ASP A 187  ? 0.3763 0.4899 0.3832 0.0075  0.0032  -0.0679 185  ASP A OD1 
1242  O OD2 . ASP A 187  ? 0.3502 0.4695 0.3652 0.0113  0.0008  -0.0810 185  ASP A OD2 
1243  N N   . MET A 188  ? 0.2606 0.3310 0.2822 0.0094  0.0014  -0.0631 186  MET A N   
1244  C CA  . MET A 188  ? 0.2896 0.3489 0.3153 0.0097  0.0006  -0.0610 186  MET A CA  
1245  C C   . MET A 188  ? 0.2894 0.3423 0.3108 0.0079  0.0021  -0.0533 186  MET A C   
1246  O O   . MET A 188  ? 0.2639 0.3111 0.2868 0.0076  0.0015  -0.0509 186  MET A O   
1247  C CB  . MET A 188  ? 0.3132 0.3686 0.3433 0.0110  0.0002  -0.0630 186  MET A CB  
1248  C CG  . MET A 188  ? 0.3707 0.4156 0.4056 0.0113  -0.0007 -0.0607 186  MET A CG  
1249  S SD  . MET A 188  ? 0.4719 0.5155 0.5143 0.0124  -0.0035 -0.0653 186  MET A SD  
1250  C CE  . MET A 188  ? 0.3555 0.4078 0.4022 0.0145  -0.0050 -0.0745 186  MET A CE  
1251  N N   . ALA A 189  ? 0.2564 0.3104 0.2730 0.0069  0.0039  -0.0495 187  ALA A N   
1252  C CA  . ALA A 189  ? 0.2692 0.3175 0.2821 0.0053  0.0051  -0.0427 187  ALA A CA  
1253  C C   . ALA A 189  ? 0.2678 0.3183 0.2780 0.0041  0.0051  -0.0404 187  ALA A C   
1254  O O   . ALA A 189  ? 0.2550 0.2992 0.2648 0.0035  0.0052  -0.0363 187  ALA A O   
1255  C CB  . ALA A 189  ? 0.2827 0.3327 0.2914 0.0044  0.0068  -0.0396 187  ALA A CB  
1256  N N   . MET A 190  ? 0.2489 0.3088 0.2573 0.0039  0.0048  -0.0430 188  MET A N   
1257  C CA  . MET A 190  ? 0.2669 0.3297 0.2729 0.0028  0.0046  -0.0408 188  MET A CA  
1258  C C   . MET A 190  ? 0.2567 0.3144 0.2666 0.0035  0.0031  -0.0422 188  MET A C   
1259  O O   . MET A 190  ? 0.2970 0.3508 0.3058 0.0025  0.0032  -0.0382 188  MET A O   
1260  C CB  . MET A 190  ? 0.2856 0.3604 0.2893 0.0027  0.0045  -0.0440 188  MET A CB  
1261  C CG  . MET A 190  ? 0.3685 0.4476 0.3689 0.0013  0.0044  -0.0410 188  MET A CG  
1262  S SD  . MET A 190  ? 0.4334 0.5279 0.4316 0.0014  0.0040  -0.0452 188  MET A SD  
1263  C CE  . MET A 190  ? 0.4044 0.5041 0.4004 0.0012  0.0056  -0.0451 188  MET A CE  
1264  N N   . ARG A 191  ? 0.2500 0.3079 0.2652 0.0051  0.0016  -0.0480 189  ARG A N   
1265  C CA  . ARG A 191  ? 0.3031 0.3561 0.3231 0.0058  0.0000  -0.0494 189  ARG A CA  
1266  C C   . ARG A 191  ? 0.2835 0.3258 0.3048 0.0054  0.0004  -0.0446 189  ARG A C   
1267  O O   . ARG A 191  ? 0.2799 0.3184 0.3019 0.0049  0.0001  -0.0418 189  ARG A O   
1268  C CB  . ARG A 191  ? 0.2880 0.3427 0.3143 0.0077  -0.0019 -0.0566 189  ARG A CB  
1269  N N   . MET A 192  ? 0.2278 0.2659 0.2498 0.0058  0.0012  -0.0434 190  MET A N   
1270  C CA  . MET A 192  ? 0.2591 0.2880 0.2826 0.0057  0.0016  -0.0391 190  MET A CA  
1271  C C   . MET A 192  ? 0.2957 0.3222 0.3143 0.0042  0.0030  -0.0331 190  MET A C   
1272  O O   . MET A 192  ? 0.2731 0.2944 0.2929 0.0039  0.0029  -0.0302 190  MET A O   
1273  C CB  . MET A 192  ? 0.3035 0.3292 0.3284 0.0064  0.0020  -0.0392 190  MET A CB  
1274  C CG  . MET A 192  ? 0.2637 0.2902 0.2948 0.0080  0.0003  -0.0448 190  MET A CG  
1275  S SD  . MET A 192  ? 0.4008 0.4231 0.4336 0.0087  0.0008  -0.0441 190  MET A SD  
1276  C CE  . MET A 192  ? 0.4061 0.4188 0.4419 0.0085  0.0006  -0.0391 190  MET A CE  
1277  N N   . MET A 193  ? 0.2688 0.2993 0.2821 0.0032  0.0043  -0.0311 191  MET A N   
1278  C CA  A MET A 193  ? 0.2894 0.3174 0.2987 0.0019  0.0055  -0.0255 191  MET A CA  
1279  C CA  B MET A 193  ? 0.2896 0.3175 0.2989 0.0019  0.0055  -0.0255 191  MET A CA  
1280  C C   . MET A 193  ? 0.2826 0.3134 0.2905 0.0011  0.0050  -0.0243 191  MET A C   
1281  O O   . MET A 193  ? 0.3193 0.3465 0.3254 0.0002  0.0056  -0.0198 191  MET A O   
1282  C CB  A MET A 193  ? 0.3069 0.3381 0.3118 0.0011  0.0068  -0.0235 191  MET A CB  
1283  C CB  B MET A 193  ? 0.3074 0.3379 0.3125 0.0011  0.0068  -0.0233 191  MET A CB  
1284  C CG  A MET A 193  ? 0.2732 0.3024 0.2792 0.0019  0.0073  -0.0247 191  MET A CG  
1285  C CG  B MET A 193  ? 0.2722 0.2982 0.2782 0.0018  0.0074  -0.0231 191  MET A CG  
1286  S SD  A MET A 193  ? 0.3117 0.3452 0.3132 0.0008  0.0087  -0.0226 191  MET A SD  
1287  S SD  B MET A 193  ? 0.3107 0.3377 0.3120 0.0006  0.0089  -0.0192 191  MET A SD  
1288  C CE  A MET A 193  ? 0.3760 0.4017 0.3754 0.0000  0.0096  -0.0164 191  MET A CE  
1289  C CE  B MET A 193  ? 0.3245 0.3621 0.3244 0.0003  0.0089  -0.0227 191  MET A CE  
1290  N N   . GLY A 194  ? 0.2929 0.3301 0.3018 0.0014  0.0039  -0.0283 192  GLY A N   
1291  C CA  . GLY A 194  ? 0.3070 0.3476 0.3145 0.0005  0.0034  -0.0273 192  GLY A CA  
1292  C C   . GLY A 194  ? 0.3215 0.3593 0.3334 0.0012  0.0019  -0.0292 192  GLY A C   
1293  O O   . GLY A 194  ? 0.3345 0.3725 0.3457 0.0005  0.0016  -0.0271 192  GLY A O   
1294  N N   . GLU A 195  ? 0.2598 0.2950 0.2767 0.0025  0.0009  -0.0331 193  GLU A N   
1295  C CA  . GLU A 195  ? 0.2573 0.2906 0.2795 0.0031  -0.0009 -0.0356 193  GLU A CA  
1296  C C   . GLU A 195  ? 0.2564 0.2815 0.2838 0.0039  -0.0014 -0.0349 193  GLU A C   
1297  O O   . GLU A 195  ? 0.2482 0.2708 0.2800 0.0041  -0.0027 -0.0353 193  GLU A O   
1298  C CB  . GLU A 195  ? 0.3074 0.3478 0.3324 0.0042  -0.0026 -0.0425 193  GLU A CB  
1299  C CG  . GLU A 195  ? 0.4240 0.4740 0.4441 0.0036  -0.0023 -0.0438 193  GLU A CG  
1300  C CD  . GLU A 195  ? 0.5104 0.5679 0.5333 0.0049  -0.0038 -0.0513 193  GLU A CD  
1301  O OE1 . GLU A 195  ? 0.5716 0.6267 0.6008 0.0061  -0.0057 -0.0554 193  GLU A OE1 
1302  O OE2 . GLU A 195  ? 0.6084 0.6743 0.6276 0.0048  -0.0031 -0.0530 193  GLU A OE2 
1303  N N   . GLN A 196  ? 0.2758 0.2973 0.3033 0.0043  -0.0005 -0.0338 194  GLN A N   
1304  C CA  . GLN A 196  ? 0.2890 0.3036 0.3217 0.0049  -0.0010 -0.0329 194  GLN A CA  
1305  C C   . GLN A 196  ? 0.3063 0.3150 0.3364 0.0043  0.0006  -0.0268 194  GLN A C   
1306  O O   . GLN A 196  ? 0.3115 0.3157 0.3444 0.0042  0.0003  -0.0242 194  GLN A O   
1307  C CB  . GLN A 196  ? 0.3091 0.3239 0.3450 0.0061  -0.0015 -0.0365 194  GLN A CB  
1308  N N   . PHE A 197  ? 0.2615 0.2705 0.2865 0.0039  0.0023  -0.0245 195  PHE A N   
1309  C CA  . PHE A 197  ? 0.2842 0.2883 0.3067 0.0034  0.0038  -0.0193 195  PHE A CA  
1310  C C   . PHE A 197  ? 0.3118 0.3158 0.3318 0.0025  0.0042  -0.0161 195  PHE A C   
1311  O O   . PHE A 197  ? 0.2985 0.2980 0.3179 0.0024  0.0050  -0.0122 195  PHE A O   
1312  C CB  . PHE A 197  ? 0.3092 0.3141 0.3273 0.0032  0.0052  -0.0181 195  PHE A CB  
1313  C CG  . PHE A 197  ? 0.3358 0.3405 0.3562 0.0041  0.0049  -0.0207 195  PHE A CG  
1314  C CD1 . PHE A 197  ? 0.3763 0.3772 0.4022 0.0051  0.0039  -0.0216 195  PHE A CD1 
1315  C CD2 . PHE A 197  ? 0.3540 0.3624 0.3714 0.0040  0.0056  -0.0221 195  PHE A CD2 
1316  C CE1 . PHE A 197  ? 0.3959 0.3965 0.4243 0.0059  0.0035  -0.0239 195  PHE A CE1 
1317  C CE2 . PHE A 197  ? 0.3801 0.3884 0.3998 0.0050  0.0053  -0.0246 195  PHE A CE2 
1318  C CZ  . PHE A 197  ? 0.3454 0.3497 0.3707 0.0059  0.0042  -0.0255 195  PHE A CZ  
1319  N N   . VAL A 198  ? 0.2549 0.2640 0.2732 0.0020  0.0037  -0.0177 196  VAL A N   
1320  C CA  . VAL A 198  ? 0.2460 0.2555 0.2627 0.0011  0.0038  -0.0150 196  VAL A CA  
1321  C C   . VAL A 198  ? 0.2324 0.2460 0.2518 0.0012  0.0021  -0.0185 196  VAL A C   
1322  O O   . VAL A 198  ? 0.2792 0.2971 0.2999 0.0017  0.0012  -0.0231 196  VAL A O   
1323  C CB  . VAL A 198  ? 0.2498 0.2622 0.2609 0.0001  0.0048  -0.0122 196  VAL A CB  
1324  C CG1 . VAL A 198  ? 0.2797 0.2878 0.2885 0.0000  0.0063  -0.0089 196  VAL A CG1 
1325  C CG2 . VAL A 198  ? 0.2711 0.2909 0.2802 -0.0002 0.0046  -0.0153 196  VAL A CG2 
1326  N N   . THR A 199  ? 0.2317 0.2440 0.2519 0.0008  0.0017  -0.0166 197  THR A N   
1327  C CA  . THR A 199  ? 0.2384 0.2550 0.2606 0.0007  0.0001  -0.0196 197  THR A CA  
1328  C C   . THR A 199  ? 0.2766 0.3004 0.2941 -0.0001 0.0002  -0.0202 197  THR A C   
1329  O O   . THR A 199  ? 0.3202 0.3500 0.3385 0.0001  -0.0010 -0.0243 197  THR A O   
1330  C CB  . THR A 199  ? 0.2630 0.2762 0.2876 0.0004  -0.0004 -0.0171 197  THR A CB  
1331  O OG1 . THR A 199  ? 0.2884 0.2956 0.3174 0.0010  -0.0004 -0.0161 197  THR A OG1 
1332  C CG2 . THR A 199  ? 0.3111 0.3284 0.3384 0.0004  -0.0023 -0.0205 197  THR A CG2 
1333  N N   . GLY A 200  ? 0.2529 0.2766 0.2657 -0.0010 0.0016  -0.0160 198  GLY A N   
1334  C CA  . GLY A 200  ? 0.2674 0.2983 0.2761 -0.0019 0.0018  -0.0157 198  GLY A CA  
1335  C C   . GLY A 200  ? 0.2528 0.2818 0.2577 -0.0027 0.0033  -0.0111 198  GLY A C   
1336  O O   . GLY A 200  ? 0.2333 0.2557 0.2387 -0.0025 0.0041  -0.0082 198  GLY A O   
1337  N N   . GLU A 201  ? 0.2493 0.2847 0.2507 -0.0036 0.0036  -0.0105 199  GLU A N   
1338  C CA  . GLU A 201  ? 0.2510 0.2853 0.2494 -0.0045 0.0047  -0.0061 199  GLU A CA  
1339  C C   . GLU A 201  ? 0.2835 0.3152 0.2812 -0.0054 0.0047  -0.0014 199  GLU A C   
1340  O O   . GLU A 201  ? 0.2944 0.3216 0.2913 -0.0057 0.0055  0.0022  199  GLU A O   
1341  C CB  . GLU A 201  ? 0.2933 0.3358 0.2886 -0.0054 0.0049  -0.0065 199  GLU A CB  
1342  C CG  . GLU A 201  ? 0.4361 0.4779 0.4290 -0.0064 0.0059  -0.0024 199  GLU A CG  
1343  C CD  . GLU A 201  ? 0.5865 0.6372 0.5770 -0.0072 0.0061  -0.0029 199  GLU A CD  
1344  O OE1 . GLU A 201  ? 0.5632 0.6214 0.5533 -0.0071 0.0054  -0.0059 199  GLU A OE1 
1345  O OE2 . GLU A 201  ? 0.6934 0.7438 0.6824 -0.0079 0.0069  -0.0004 199  GLU A OE2 
1346  N N   . THR A 202  ? 0.2599 0.2945 0.2582 -0.0057 0.0037  -0.0015 200  THR A N   
1347  C CA  . THR A 202  ? 0.2320 0.2646 0.2302 -0.0064 0.0034  0.0027  200  THR A CA  
1348  C C   . THR A 202  ? 0.2387 0.2687 0.2399 -0.0058 0.0026  0.0012  200  THR A C   
1349  O O   . THR A 202  ? 0.2354 0.2670 0.2387 -0.0050 0.0019  -0.0031 200  THR A O   
1350  C CB  . THR A 202  ? 0.2611 0.3013 0.2569 -0.0078 0.0027  0.0047  200  THR A CB  
1351  O OG1 . THR A 202  ? 0.3024 0.3491 0.2986 -0.0076 0.0017  0.0007  200  THR A OG1 
1352  C CG2 . THR A 202  ? 0.3041 0.3481 0.2972 -0.0088 0.0034  0.0064  200  THR A CG2 
1353  N N   . ILE A 203  ? 0.2257 0.2521 0.2277 -0.0060 0.0025  0.0047  201  ILE A N   
1354  C CA  . ILE A 203  ? 0.2292 0.2531 0.2343 -0.0055 0.0018  0.0037  201  ILE A CA  
1355  C C   . ILE A 203  ? 0.2404 0.2710 0.2459 -0.0058 0.0003  0.0009  201  ILE A C   
1356  O O   . ILE A 203  ? 0.2350 0.2651 0.2437 -0.0050 -0.0006 -0.0023 201  ILE A O   
1357  C CB  . ILE A 203  ? 0.2340 0.2533 0.2398 -0.0056 0.0020  0.0079  201  ILE A CB  
1358  C CG1 . ILE A 203  ? 0.2164 0.2327 0.2259 -0.0049 0.0015  0.0070  201  ILE A CG1 
1359  C CG2 . ILE A 203  ? 0.2501 0.2733 0.2540 -0.0069 0.0014  0.0113  201  ILE A CG2 
1360  C CD1 . ILE A 203  ? 0.2144 0.2265 0.2266 -0.0038 0.0019  0.0046  201  ILE A CD1 
1361  N N   . ARG A 204  ? 0.2280 0.2654 0.2305 -0.0068 -0.0001 0.0020  202  ARG A N   
1362  C CA  . ARG A 204  ? 0.2439 0.2888 0.2465 -0.0071 -0.0016 -0.0008 202  ARG A CA  
1363  C C   . ARG A 204  ? 0.2480 0.2961 0.2517 -0.0061 -0.0020 -0.0068 202  ARG A C   
1364  O O   . ARG A 204  ? 0.2449 0.2949 0.2513 -0.0055 -0.0034 -0.0106 202  ARG A O   
1365  C CB  . ARG A 204  ? 0.3128 0.3652 0.3118 -0.0085 -0.0018 0.0021  202  ARG A CB  
1366  C CG  . ARG A 204  ? 0.4013 0.4528 0.4006 -0.0094 -0.0024 0.0067  202  ARG A CG  
1367  C CD  . ARG A 204  ? 0.4162 0.4728 0.4124 -0.0109 -0.0024 0.0113  202  ARG A CD  
1368  N NE  . ARG A 204  ? 0.4274 0.4824 0.4245 -0.0116 -0.0031 0.0158  202  ARG A NE  
1369  C CZ  . ARG A 204  ? 0.4125 0.4597 0.4114 -0.0114 -0.0026 0.0190  202  ARG A CZ  
1370  N NH1 . ARG A 204  ? 0.3465 0.3869 0.3460 -0.0106 -0.0013 0.0184  202  ARG A NH1 
1371  N NH2 . ARG A 204  ? 0.3488 0.3953 0.3488 -0.0120 -0.0035 0.0227  202  ARG A NH2 
1372  N N   . GLU A 205  ? 0.2424 0.2912 0.2446 -0.0059 -0.0010 -0.0079 203  GLU A N   
1373  C CA  . GLU A 205  ? 0.2659 0.3171 0.2698 -0.0048 -0.0015 -0.0137 203  GLU A CA  
1374  C C   . GLU A 205  ? 0.2713 0.3152 0.2800 -0.0036 -0.0019 -0.0160 203  GLU A C   
1375  O O   . GLU A 205  ? 0.2528 0.2988 0.2649 -0.0027 -0.0033 -0.0210 203  GLU A O   
1376  C CB  . GLU A 205  ? 0.2676 0.3201 0.2690 -0.0048 -0.0002 -0.0138 203  GLU A CB  
1377  C CG  . GLU A 205  ? 0.3141 0.3701 0.3173 -0.0036 -0.0007 -0.0200 203  GLU A CG  
1378  C CD  . GLU A 205  ? 0.4001 0.4587 0.4005 -0.0037 0.0006  -0.0199 203  GLU A CD  
1379  O OE1 . GLU A 205  ? 0.3672 0.4192 0.3677 -0.0036 0.0017  -0.0177 203  GLU A OE1 
1380  O OE2 . GLU A 205  ? 0.4197 0.4875 0.4180 -0.0039 0.0004  -0.0221 203  GLU A OE2 
1381  N N   . ALA A 206  ? 0.2305 0.2664 0.2401 -0.0035 -0.0009 -0.0125 204  ALA A N   
1382  C CA  . ALA A 206  ? 0.2267 0.2561 0.2411 -0.0025 -0.0012 -0.0138 204  ALA A CA  
1383  C C   . ALA A 206  ? 0.2476 0.2774 0.2654 -0.0025 -0.0028 -0.0150 204  ALA A C   
1384  O O   . ALA A 206  ? 0.2515 0.2800 0.2740 -0.0017 -0.0040 -0.0186 204  ALA A O   
1385  C CB  . ALA A 206  ? 0.2389 0.2609 0.2531 -0.0025 0.0003  -0.0093 204  ALA A CB  
1386  N N   . LEU A 207  ? 0.2224 0.2541 0.2384 -0.0034 -0.0030 -0.0119 205  LEU A N   
1387  C CA  . LEU A 207  ? 0.2320 0.2643 0.2512 -0.0034 -0.0045 -0.0128 205  LEU A CA  
1388  C C   . LEU A 207  ? 0.2643 0.3034 0.2849 -0.0030 -0.0063 -0.0185 205  LEU A C   
1389  O O   . LEU A 207  ? 0.2515 0.2897 0.2770 -0.0025 -0.0079 -0.0215 205  LEU A O   
1390  C CB  . LEU A 207  ? 0.2407 0.2739 0.2575 -0.0044 -0.0043 -0.0083 205  LEU A CB  
1391  C CG  . LEU A 207  ? 0.2472 0.2732 0.2640 -0.0045 -0.0030 -0.0034 205  LEU A CG  
1392  C CD1 . LEU A 207  ? 0.2367 0.2645 0.2508 -0.0055 -0.0028 0.0009  205  LEU A CD1 
1393  C CD2 . LEU A 207  ? 0.2512 0.2721 0.2731 -0.0039 -0.0034 -0.0037 205  LEU A CD2 
1394  N N   . LYS A 208  ? 0.2570 0.3035 0.2737 -0.0033 -0.0062 -0.0201 206  LYS A N   
1395  C CA  . LYS A 208  ? 0.2790 0.3331 0.2968 -0.0027 -0.0079 -0.0260 206  LYS A CA  
1396  C C   . LYS A 208  ? 0.2791 0.3304 0.3020 -0.0014 -0.0088 -0.0313 206  LYS A C   
1397  O O   . LYS A 208  ? 0.3122 0.3655 0.3394 -0.0007 -0.0108 -0.0360 206  LYS A O   
1398  C CB  . LYS A 208  ? 0.3146 0.3775 0.3271 -0.0032 -0.0073 -0.0264 206  LYS A CB  
1399  N N   . ARG A 209  ? 0.2554 0.3019 0.2784 -0.0010 -0.0074 -0.0304 207  ARG A N   
1400  C CA  . ARG A 209  ? 0.2706 0.3143 0.2987 0.0003  -0.0082 -0.0349 207  ARG A CA  
1401  C C   . ARG A 209  ? 0.2872 0.3232 0.3215 0.0007  -0.0091 -0.0341 207  ARG A C   
1402  O O   . ARG A 209  ? 0.3591 0.3928 0.3989 0.0017  -0.0103 -0.0378 207  ARG A O   
1403  C CB  . ARG A 209  ? 0.2884 0.3299 0.3142 0.0006  -0.0065 -0.0338 207  ARG A CB  
1404  C CG  . ARG A 209  ? 0.3304 0.3801 0.3513 0.0004  -0.0059 -0.0356 207  ARG A CG  
1405  C CD  . ARG A 209  ? 0.3277 0.3749 0.3460 0.0004  -0.0040 -0.0334 207  ARG A CD  
1406  N NE  . ARG A 209  ? 0.3439 0.3994 0.3579 0.0001  -0.0034 -0.0348 207  ARG A NE  
1407  C CZ  . ARG A 209  ? 0.4011 0.4564 0.4123 -0.0001 -0.0019 -0.0333 207  ARG A CZ  
1408  N NH1 . ARG A 209  ? 0.3677 0.4148 0.3797 0.0000  -0.0008 -0.0304 207  ARG A NH1 
1409  N NH2 . ARG A 209  ? 0.4671 0.5309 0.4747 -0.0004 -0.0014 -0.0345 207  ARG A NH2 
1410  N N   . SER A 210  ? 0.2773 0.3095 0.3112 -0.0001 -0.0086 -0.0293 208  SER A N   
1411  C CA  . SER A 210  ? 0.2680 0.2935 0.3078 0.0001  -0.0093 -0.0280 208  SER A CA  
1412  C C   . SER A 210  ? 0.2964 0.3241 0.3414 0.0003  -0.0118 -0.0317 208  SER A C   
1413  O O   . SER A 210  ? 0.2765 0.2994 0.3280 0.0005  -0.0129 -0.0318 208  SER A O   
1414  C CB  . SER A 210  ? 0.2588 0.2797 0.2962 -0.0007 -0.0076 -0.0215 208  SER A CB  
1415  O OG  . SER A 210  ? 0.2787 0.2970 0.3123 -0.0008 -0.0055 -0.0185 208  SER A OG  
1416  N N   . LYS A 211  ? 0.2955 0.3306 0.3382 0.0001  -0.0129 -0.0346 209  LYS A N   
1417  C CA  . LYS A 211  ? 0.2926 0.3302 0.3399 0.0002  -0.0154 -0.0379 209  LYS A CA  
1418  C C   . LYS A 211  ? 0.3073 0.3434 0.3625 0.0014  -0.0176 -0.0435 209  LYS A C   
1419  O O   . LYS A 211  ? 0.3196 0.3529 0.3812 0.0014  -0.0194 -0.0444 209  LYS A O   
1420  C CB  . LYS A 211  ? 0.3556 0.4026 0.3985 0.0000  -0.0161 -0.0404 209  LYS A CB  
1421  N N   . GLU A 212  ? 0.2831 0.3209 0.3384 0.0023  -0.0175 -0.0473 210  GLU A N   
1422  C CA  . GLU A 212  ? 0.3506 0.3876 0.4138 0.0035  -0.0199 -0.0533 210  GLU A CA  
1423  C C   . GLU A 212  ? 0.3341 0.3623 0.4045 0.0035  -0.0205 -0.0505 210  GLU A C   
1424  O O   . GLU A 212  ? 0.3274 0.3543 0.4056 0.0038  -0.0231 -0.0533 210  GLU A O   
1425  C CB  . GLU A 212  ? 0.3639 0.4038 0.4256 0.0045  -0.0194 -0.0570 210  GLU A CB  
1426  C CG  . GLU A 212  ? 0.4622 0.5018 0.5325 0.0060  -0.0221 -0.0638 210  GLU A CG  
1427  C CD  . GLU A 212  ? 0.5613 0.6041 0.6300 0.0071  -0.0216 -0.0676 210  GLU A CD  
1428  O OE1 . GLU A 212  ? 0.6062 0.6498 0.6677 0.0066  -0.0189 -0.0640 210  GLU A OE1 
1429  O OE2 . GLU A 212  ? 0.7010 0.7457 0.7760 0.0085  -0.0239 -0.0743 210  GLU A OE2 
1430  N N   . LEU A 213  ? 0.3014 0.3238 0.3697 0.0030  -0.0182 -0.0449 211  LEU A N   
1431  C CA  . LEU A 213  ? 0.2846 0.2995 0.3596 0.0029  -0.0186 -0.0418 211  LEU A CA  
1432  C C   . LEU A 213  ? 0.3060 0.3184 0.3822 0.0019  -0.0186 -0.0372 211  LEU A C   
1433  O O   . LEU A 213  ? 0.2772 0.2852 0.3609 0.0018  -0.0199 -0.0361 211  LEU A O   
1434  C CB  . LEU A 213  ? 0.2751 0.2854 0.3479 0.0030  -0.0164 -0.0379 211  LEU A CB  
1435  C CG  . LEU A 213  ? 0.2999 0.3115 0.3744 0.0041  -0.0170 -0.0425 211  LEU A CG  
1436  C CD1 . LEU A 213  ? 0.3175 0.3243 0.3901 0.0041  -0.0149 -0.0384 211  LEU A CD1 
1437  C CD2 . LEU A 213  ? 0.3878 0.3987 0.4723 0.0049  -0.0203 -0.0477 211  LEU A CD2 
1438  N N   . GLU A 214  ? 0.2665 0.2817 0.3360 0.0011  -0.0172 -0.0346 212  GLU A N   
1439  C CA  . GLU A 214  ? 0.2854 0.2989 0.3567 0.0003  -0.0175 -0.0310 212  GLU A CA  
1440  C C   . GLU A 214  ? 0.3040 0.3195 0.3823 0.0005  -0.0207 -0.0356 212  GLU A C   
1441  O O   . GLU A 214  ? 0.3045 0.3166 0.3887 0.0000  -0.0217 -0.0334 212  GLU A O   
1442  C CB  . GLU A 214  ? 0.2525 0.2689 0.3157 -0.0004 -0.0157 -0.0276 212  GLU A CB  
1443  C CG  . GLU A 214  ? 0.2808 0.2939 0.3385 -0.0007 -0.0127 -0.0223 212  GLU A CG  
1444  C CD  . GLU A 214  ? 0.2888 0.3041 0.3399 -0.0015 -0.0113 -0.0187 212  GLU A CD  
1445  O OE1 . GLU A 214  ? 0.3334 0.3542 0.3828 -0.0018 -0.0124 -0.0207 212  GLU A OE1 
1446  O OE2 . GLU A 214  ? 0.3091 0.3209 0.3572 -0.0017 -0.0092 -0.0138 212  GLU A OE2 
1447  N N   . GLU A 215  ? 0.3085 0.3301 0.3868 0.0012  -0.0224 -0.0420 213  GLU A N   
1448  C CA  . GLU A 215  ? 0.3419 0.3659 0.4271 0.0015  -0.0257 -0.0473 213  GLU A CA  
1449  C C   . GLU A 215  ? 0.3760 0.3948 0.4717 0.0020  -0.0279 -0.0490 213  GLU A C   
1450  O O   . GLU A 215  ? 0.4020 0.4206 0.5051 0.0020  -0.0306 -0.0515 213  GLU A O   
1451  C CB  . GLU A 215  ? 0.3746 0.4070 0.4571 0.0024  -0.0270 -0.0542 213  GLU A CB  
1452  N N   . LYS A 216  ? 0.3580 0.3726 0.4546 0.0024  -0.0268 -0.0476 214  LYS A N   
1453  C CA  . LYS A 216  ? 0.3734 0.3827 0.4800 0.0028  -0.0287 -0.0481 214  LYS A CA  
1454  C C   . LYS A 216  ? 0.3945 0.3976 0.5042 0.0017  -0.0276 -0.0407 214  LYS A C   
1455  O O   . LYS A 216  ? 0.4399 0.4387 0.5587 0.0017  -0.0294 -0.0401 214  LYS A O   
1456  C CB  . LYS A 216  ? 0.3376 0.3462 0.4444 0.0038  -0.0283 -0.0504 214  LYS A CB  
1457  N N   . GLY A 217  ? 0.3005 0.3032 0.4031 0.0009  -0.0249 -0.0350 215  GLY A N   
1458  C CA  . GLY A 217  ? 0.2981 0.2959 0.4029 0.0000  -0.0236 -0.0281 215  GLY A CA  
1459  C C   . GLY A 217  ? 0.2860 0.2809 0.3847 -0.0001 -0.0203 -0.0227 215  GLY A C   
1460  O O   . GLY A 217  ? 0.3031 0.2945 0.4034 -0.0007 -0.0191 -0.0170 215  GLY A O   
1461  N N   . PHE A 218  ? 0.2572 0.2539 0.3493 0.0004  -0.0188 -0.0244 216  PHE A N   
1462  C CA  . PHE A 218  ? 0.2191 0.2136 0.3049 0.0004  -0.0157 -0.0195 216  PHE A CA  
1463  C C   . PHE A 218  ? 0.2295 0.2257 0.3076 -0.0002 -0.0136 -0.0162 216  PHE A C   
1464  O O   . PHE A 218  ? 0.2478 0.2477 0.3240 -0.0005 -0.0145 -0.0182 216  PHE A O   
1465  C CB  . PHE A 218  ? 0.2189 0.2148 0.3004 0.0011  -0.0149 -0.0224 216  PHE A CB  
1466  C CG  . PHE A 218  ? 0.2536 0.2471 0.3419 0.0018  -0.0165 -0.0248 216  PHE A CG  
1467  C CD1 . PHE A 218  ? 0.2872 0.2828 0.3820 0.0024  -0.0195 -0.0310 216  PHE A CD1 
1468  C CD2 . PHE A 218  ? 0.2280 0.2178 0.3165 0.0019  -0.0151 -0.0212 216  PHE A CD2 
1469  C CE1 . PHE A 218  ? 0.2865 0.2798 0.3883 0.0031  -0.0212 -0.0334 216  PHE A CE1 
1470  C CE2 . PHE A 218  ? 0.2729 0.2605 0.3680 0.0026  -0.0167 -0.0232 216  PHE A CE2 
1471  C CZ  . PHE A 218  ? 0.2520 0.2412 0.3540 0.0032  -0.0198 -0.0292 216  PHE A CZ  
1472  N N   . SER A 219  ? 0.2090 0.2026 0.2830 -0.0004 -0.0111 -0.0111 217  SER A N   
1473  C CA  . SER A 219  ? 0.2135 0.2085 0.2800 -0.0007 -0.0090 -0.0082 217  SER A CA  
1474  C C   . SER A 219  ? 0.2120 0.2063 0.2722 -0.0004 -0.0069 -0.0071 217  SER A C   
1475  O O   . SER A 219  ? 0.1859 0.1789 0.2477 0.0001  -0.0069 -0.0086 217  SER A O   
1476  C CB  . SER A 219  ? 0.2154 0.2080 0.2831 -0.0012 -0.0080 -0.0030 217  SER A CB  
1477  O OG  . SER A 219  ? 0.2290 0.2180 0.2991 -0.0010 -0.0069 0.0004  217  SER A OG  
1478  N N   . TYR A 220  ? 0.1844 0.1797 0.2380 -0.0006 -0.0051 -0.0046 218  TYR A N   
1479  C CA  . TYR A 220  ? 0.1993 0.1945 0.2469 -0.0004 -0.0032 -0.0037 218  TYR A CA  
1480  C C   . TYR A 220  ? 0.1843 0.1772 0.2284 -0.0005 -0.0011 0.0013  218  TYR A C   
1481  O O   . TYR A 220  ? 0.1925 0.1855 0.2368 -0.0008 -0.0010 0.0036  218  TYR A O   
1482  C CB  . TYR A 220  ? 0.2074 0.2074 0.2501 -0.0006 -0.0035 -0.0065 218  TYR A CB  
1483  C CG  . TYR A 220  ? 0.2075 0.2100 0.2523 -0.0002 -0.0049 -0.0117 218  TYR A CG  
1484  C CD1 . TYR A 220  ? 0.2418 0.2468 0.2913 -0.0001 -0.0072 -0.0157 218  TYR A CD1 
1485  C CD2 . TYR A 220  ? 0.2099 0.2123 0.2523 0.0002  -0.0041 -0.0128 218  TYR A CD2 
1486  C CE1 . TYR A 220  ? 0.2305 0.2380 0.2823 0.0005  -0.0087 -0.0210 218  TYR A CE1 
1487  C CE2 . TYR A 220  ? 0.2202 0.2251 0.2649 0.0008  -0.0054 -0.0178 218  TYR A CE2 
1488  C CZ  . TYR A 220  ? 0.2270 0.2345 0.2764 0.0010  -0.0077 -0.0220 218  TYR A CZ  
1489  O OH  . TYR A 220  ? 0.2420 0.2522 0.2940 0.0018  -0.0091 -0.0275 218  TYR A OH  
1490  N N   . SER A 221  ? 0.1929 0.1839 0.2341 -0.0001 0.0005  0.0027  219  SER A N   
1491  C CA  . SER A 221  ? 0.2017 0.1913 0.2386 0.0000  0.0024  0.0063  219  SER A CA  
1492  C C   . SER A 221  ? 0.1974 0.1880 0.2291 0.0001  0.0032  0.0053  219  SER A C   
1493  O O   . SER A 221  ? 0.2299 0.2197 0.2619 0.0005  0.0034  0.0039  219  SER A O   
1494  C CB  . SER A 221  ? 0.2081 0.1944 0.2471 0.0006  0.0036  0.0094  219  SER A CB  
1495  O OG  . SER A 221  ? 0.2274 0.2129 0.2624 0.0009  0.0053  0.0123  219  SER A OG  
1496  N N   . TYR A 222  ? 0.1594 0.1519 0.1868 -0.0003 0.0037  0.0062  220  TYR A N   
1497  C CA  . TYR A 222  ? 0.1782 0.1723 0.2011 -0.0005 0.0042  0.0053  220  TYR A CA  
1498  C C   . TYR A 222  ? 0.2166 0.2079 0.2367 -0.0001 0.0059  0.0080  220  TYR A C   
1499  O O   . TYR A 222  ? 0.2030 0.1925 0.2228 0.0001  0.0066  0.0108  220  TYR A O   
1500  C CB  . TYR A 222  ? 0.1934 0.1917 0.2136 -0.0014 0.0036  0.0050  220  TYR A CB  
1501  C CG  . TYR A 222  ? 0.1816 0.1836 0.2043 -0.0016 0.0018  0.0016  220  TYR A CG  
1502  C CD1 . TYR A 222  ? 0.1946 0.1994 0.2174 -0.0015 0.0011  -0.0023 220  TYR A CD1 
1503  C CD2 . TYR A 222  ? 0.1717 0.1744 0.1969 -0.0019 0.0008  0.0021  220  TYR A CD2 
1504  C CE1 . TYR A 222  ? 0.1899 0.1983 0.2154 -0.0015 -0.0006 -0.0060 220  TYR A CE1 
1505  C CE2 . TYR A 222  ? 0.1939 0.1999 0.2217 -0.0021 -0.0009 -0.0013 220  TYR A CE2 
1506  C CZ  . TYR A 222  ? 0.2002 0.2092 0.2282 -0.0018 -0.0017 -0.0054 220  TYR A CZ  
1507  O OH  . TYR A 222  ? 0.2223 0.2350 0.2531 -0.0018 -0.0036 -0.0094 220  TYR A OH  
1508  N N   . ASP A 223  ? 0.2370 0.2282 0.2553 0.0001  0.0064  0.0068  221  ASP A N   
1509  C CA  . ASP A 223  ? 0.2844 0.2733 0.3000 0.0005  0.0077  0.0086  221  ASP A CA  
1510  C C   . ASP A 223  ? 0.2706 0.2618 0.2823 -0.0001 0.0078  0.0082  221  ASP A C   
1511  O O   . ASP A 223  ? 0.2604 0.2538 0.2714 -0.0003 0.0075  0.0058  221  ASP A O   
1512  C CB  . ASP A 223  ? 0.2662 0.2530 0.2834 0.0013  0.0081  0.0077  221  ASP A CB  
1513  C CG  . ASP A 223  ? 0.3146 0.2997 0.3288 0.0017  0.0093  0.0089  221  ASP A CG  
1514  O OD1 . ASP A 223  ? 0.3596 0.3440 0.3714 0.0017  0.0100  0.0109  221  ASP A OD1 
1515  O OD2 . ASP A 223  ? 0.4487 0.4332 0.4633 0.0021  0.0095  0.0077  221  ASP A OD2 
1516  N N   . MET A 224  ? 0.2603 0.2514 0.2699 -0.0005 0.0082  0.0107  222  MET A N   
1517  C CA  . MET A 224  ? 0.2872 0.2805 0.2936 -0.0013 0.0082  0.0111  222  MET A CA  
1518  C C   . MET A 224  ? 0.3219 0.3134 0.3267 -0.0009 0.0091  0.0112  222  MET A C   
1519  O O   . MET A 224  ? 0.3476 0.3406 0.3501 -0.0015 0.0091  0.0119  222  MET A O   
1520  C CB  . MET A 224  ? 0.2721 0.2659 0.2779 -0.0019 0.0079  0.0139  222  MET A CB  
1521  C CG  . MET A 224  ? 0.3405 0.3364 0.3479 -0.0023 0.0069  0.0140  222  MET A CG  
1522  S SD  . MET A 224  ? 0.3516 0.3532 0.3588 -0.0031 0.0057  0.0108  222  MET A SD  
1523  C CE  . MET A 224  ? 0.4246 0.4303 0.4281 -0.0042 0.0057  0.0119  222  MET A CE  
1524  N N   . LEU A 225  ? 0.3132 0.3017 0.3192 0.0002  0.0097  0.0106  223  LEU A N   
1525  C CA  . LEU A 225  ? 0.3379 0.3250 0.3426 0.0007  0.0104  0.0101  223  LEU A CA  
1526  C C   . LEU A 225  ? 0.3984 0.3834 0.4012 0.0009  0.0111  0.0121  223  LEU A C   
1527  O O   . LEU A 225  ? 0.4249 0.4090 0.4264 0.0012  0.0115  0.0117  223  LEU A O   
1528  C CB  . LEU A 225  ? 0.3924 0.3825 0.3960 0.0001  0.0101  0.0077  223  LEU A CB  
1529  C CG  . LEU A 225  ? 0.3142 0.3058 0.3202 0.0004  0.0094  0.0048  223  LEU A CG  
1530  C CD1 . LEU A 225  ? 0.4061 0.4020 0.4108 -0.0002 0.0090  0.0023  223  LEU A CD1 
1531  C CD2 . LEU A 225  ? 0.3564 0.3448 0.3647 0.0014  0.0097  0.0043  223  LEU A CD2 
1532  N N   . GLY A 226  ? 0.3308 0.3150 0.3340 0.0009  0.0110  0.0141  224  GLY A N   
1533  C CA  . GLY A 226  ? 0.3677 0.3497 0.3700 0.0014  0.0114  0.0156  224  GLY A CA  
1534  C C   . GLY A 226  ? 0.3310 0.3105 0.3339 0.0028  0.0123  0.0155  224  GLY A C   
1535  O O   . GLY A 226  ? 0.3222 0.3013 0.3268 0.0034  0.0126  0.0155  224  GLY A O   
1536  N N   . GLU A 227  ? 0.3043 0.2824 0.3058 0.0034  0.0127  0.0155  225  GLU A N   
1537  C CA  . GLU A 227  ? 0.2597 0.2362 0.2613 0.0048  0.0136  0.0154  225  GLU A CA  
1538  C C   . GLU A 227  ? 0.2861 0.2615 0.2862 0.0053  0.0137  0.0152  225  GLU A C   
1539  O O   . GLU A 227  ? 0.2637 0.2395 0.2629 0.0044  0.0131  0.0149  225  GLU A O   
1540  C CB  . GLU A 227  ? 0.3206 0.2976 0.3226 0.0049  0.0138  0.0143  225  GLU A CB  
1541  C CG  . GLU A 227  ? 0.3786 0.3547 0.3808 0.0061  0.0147  0.0145  225  GLU A CG  
1542  C CD  . GLU A 227  ? 0.4526 0.4290 0.4557 0.0060  0.0146  0.0135  225  GLU A CD  
1543  O OE1 . GLU A 227  ? 0.3704 0.3478 0.3746 0.0051  0.0139  0.0125  225  GLU A OE1 
1544  O OE2 . GLU A 227  ? 0.4519 0.4278 0.4549 0.0068  0.0151  0.0137  225  GLU A OE2 
1545  N N   . ALA A 228  ? 0.2680 0.2425 0.2683 0.0067  0.0142  0.0153  226  ALA A N   
1546  C CA  . ALA A 228  ? 0.2707 0.2442 0.2699 0.0075  0.0143  0.0146  226  ALA A CA  
1547  C C   . ALA A 228  ? 0.2267 0.1995 0.2260 0.0067  0.0132  0.0148  226  ALA A C   
1548  O O   . ALA A 228  ? 0.2713 0.2439 0.2697 0.0061  0.0128  0.0142  226  ALA A O   
1549  C CB  . ALA A 228  ? 0.3125 0.2862 0.3103 0.0076  0.0147  0.0136  226  ALA A CB  
1550  N N   . ALA A 229  ? 0.2211 0.1937 0.2220 0.0066  0.0126  0.0158  227  ALA A N   
1551  C CA  . ALA A 229  ? 0.2262 0.1980 0.2281 0.0059  0.0114  0.0164  227  ALA A CA  
1552  C C   . ALA A 229  ? 0.2316 0.2020 0.2335 0.0070  0.0112  0.0151  227  ALA A C   
1553  O O   . ALA A 229  ? 0.2243 0.1944 0.2263 0.0087  0.0118  0.0140  227  ALA A O   
1554  C CB  . ALA A 229  ? 0.2282 0.1998 0.2324 0.0061  0.0108  0.0176  227  ALA A CB  
1555  N N   . THR A 230  ? 0.2334 0.2034 0.2356 0.0059  0.0102  0.0153  228  THR A N   
1556  C CA  . THR A 230  ? 0.2467 0.2152 0.2494 0.0067  0.0096  0.0140  228  THR A CA  
1557  C C   . THR A 230  ? 0.2171 0.1842 0.2232 0.0068  0.0080  0.0145  228  THR A C   
1558  O O   . THR A 230  ? 0.2216 0.1874 0.2290 0.0082  0.0074  0.0129  228  THR A O   
1559  C CB  . THR A 230  ? 0.2660 0.2350 0.2674 0.0054  0.0093  0.0140  228  THR A CB  
1560  O OG1 . THR A 230  ? 0.3493 0.3197 0.3483 0.0054  0.0106  0.0134  228  THR A OG1 
1561  C CG2 . THR A 230  ? 0.3298 0.2974 0.3318 0.0063  0.0087  0.0124  228  THR A CG2 
1562  N N   . THR A 231  ? 0.2120 0.1795 0.2198 0.0054  0.0071  0.0167  229  THR A N   
1563  C CA  . THR A 231  ? 0.2023 0.1683 0.2139 0.0052  0.0053  0.0178  229  THR A CA  
1564  C C   . THR A 231  ? 0.2076 0.1741 0.2207 0.0051  0.0051  0.0193  229  THR A C   
1565  O O   . THR A 231  ? 0.2182 0.1864 0.2292 0.0047  0.0063  0.0199  229  THR A O   
1566  C CB  . THR A 231  ? 0.2238 0.1903 0.2367 0.0030  0.0039  0.0199  229  THR A CB  
1567  O OG1 . THR A 231  ? 0.2404 0.2095 0.2520 0.0012  0.0042  0.0223  229  THR A OG1 
1568  C CG2 . THR A 231  ? 0.2306 0.1971 0.2417 0.0027  0.0042  0.0187  229  THR A CG2 
1569  N N   . ALA A 232  ? 0.2072 0.1722 0.2244 0.0056  0.0036  0.0197  230  ALA A N   
1570  C CA  . ALA A 232  ? 0.2198 0.1852 0.2390 0.0053  0.0031  0.0216  230  ALA A CA  
1571  C C   . ALA A 232  ? 0.2416 0.2092 0.2597 0.0029  0.0028  0.0246  230  ALA A C   
1572  O O   . ALA A 232  ? 0.2275 0.1968 0.2449 0.0025  0.0033  0.0256  230  ALA A O   
1573  C CB  . ALA A 232  ? 0.2242 0.1876 0.2487 0.0060  0.0010  0.0218  230  ALA A CB  
1574  N N   . ALA A 233  ? 0.2294 0.1977 0.2476 0.0011  0.0019  0.0261  231  ALA A N   
1575  C CA  . ALA A 233  ? 0.2536 0.2252 0.2707 -0.0012 0.0016  0.0290  231  ALA A CA  
1576  C C   . ALA A 233  ? 0.2462 0.2202 0.2589 -0.0013 0.0035  0.0277  231  ALA A C   
1577  O O   . ALA A 233  ? 0.2689 0.2457 0.2808 -0.0023 0.0036  0.0292  231  ALA A O   
1578  C CB  . ALA A 233  ? 0.2808 0.2534 0.2991 -0.0030 0.0004  0.0309  231  ALA A CB  
1579  N N   . ASP A 234  ? 0.2305 0.2037 0.2407 -0.0002 0.0049  0.0251  232  ASP A N   
1580  C CA  . ASP A 234  ? 0.2612 0.2363 0.2681 -0.0001 0.0065  0.0238  232  ASP A CA  
1581  C C   . ASP A 234  ? 0.2542 0.2292 0.2615 0.0008  0.0070  0.0236  232  ASP A C   
1582  O O   . ASP A 234  ? 0.2557 0.2330 0.2619 0.0001  0.0074  0.0239  232  ASP A O   
1583  C CB  . ASP A 234  ? 0.3234 0.2971 0.3284 0.0012  0.0077  0.0212  232  ASP A CB  
1584  C CG  . ASP A 234  ? 0.4189 0.3933 0.4228 0.0003  0.0075  0.0209  232  ASP A CG  
1585  O OD1 . ASP A 234  ? 0.3827 0.3593 0.3867 -0.0015 0.0067  0.0227  232  ASP A OD1 
1586  O OD2 . ASP A 234  ? 0.3829 0.3559 0.3857 0.0015  0.0082  0.0189  232  ASP A OD2 
1587  N N   . ALA A 235  ? 0.2194 0.1921 0.2285 0.0025  0.0071  0.0229  233  ALA A N   
1588  C CA  . ALA A 235  ? 0.2056 0.1784 0.2152 0.0034  0.0077  0.0228  233  ALA A CA  
1589  C C   . ALA A 235  ? 0.2359 0.2102 0.2472 0.0021  0.0066  0.0251  233  ALA A C   
1590  O O   . ALA A 235  ? 0.2185 0.1942 0.2294 0.0020  0.0071  0.0253  233  ALA A O   
1591  C CB  . ALA A 235  ? 0.2291 0.1999 0.2406 0.0055  0.0078  0.0215  233  ALA A CB  
1592  N N   . GLU A 236  ? 0.2168 0.1908 0.2303 0.0012  0.0050  0.0270  234  GLU A N   
1593  C CA  . GLU A 236  ? 0.2235 0.1994 0.2385 -0.0002 0.0038  0.0296  234  GLU A CA  
1594  C C   . GLU A 236  ? 0.2144 0.1941 0.2267 -0.0019 0.0041  0.0303  234  GLU A C   
1595  O O   . GLU A 236  ? 0.2259 0.2078 0.2382 -0.0025 0.0039  0.0312  234  GLU A O   
1596  C CB  . GLU A 236  ? 0.2783 0.2533 0.2969 -0.0010 0.0018  0.0319  234  GLU A CB  
1597  N N   . ARG A 237  ? 0.2246 0.2055 0.2347 -0.0027 0.0045  0.0296  235  ARG A N   
1598  C CA  . ARG A 237  ? 0.2405 0.2255 0.2480 -0.0040 0.0048  0.0295  235  ARG A CA  
1599  C C   . ARG A 237  ? 0.2541 0.2395 0.2602 -0.0032 0.0060  0.0273  235  ARG A C   
1600  O O   . ARG A 237  ? 0.2296 0.2182 0.2351 -0.0040 0.0057  0.0275  235  ARG A O   
1601  C CB  . ARG A 237  ? 0.2597 0.2459 0.2654 -0.0047 0.0051  0.0289  235  ARG A CB  
1602  C CG  . ARG A 237  ? 0.3336 0.3244 0.3367 -0.0058 0.0055  0.0281  235  ARG A CG  
1603  C CD  . ARG A 237  ? 0.4128 0.4056 0.4147 -0.0069 0.0055  0.0284  235  ARG A CD  
1604  N NE  . ARG A 237  ? 0.4712 0.4603 0.4729 -0.0057 0.0062  0.0265  235  ARG A NE  
1605  C CZ  . ARG A 237  ? 0.4996 0.4882 0.4994 -0.0047 0.0074  0.0236  235  ARG A CZ  
1606  N NH1 . ARG A 237  ? 0.5595 0.5509 0.5579 -0.0048 0.0080  0.0220  235  ARG A NH1 
1607  N NH2 . ARG A 237  ? 0.4471 0.4324 0.4467 -0.0036 0.0080  0.0223  235  ARG A NH2 
1608  N N   . TYR A 238  ? 0.2144 0.1969 0.2202 -0.0016 0.0071  0.0252  236  TYR A N   
1609  C CA  . TYR A 238  ? 0.2025 0.1853 0.2077 -0.0008 0.0080  0.0235  236  TYR A CA  
1610  C C   . TYR A 238  ? 0.2106 0.1936 0.2178 -0.0006 0.0076  0.0246  236  TYR A C   
1611  O O   . TYR A 238  ? 0.2142 0.1991 0.2214 -0.0010 0.0077  0.0240  236  TYR A O   
1612  C CB  . TYR A 238  ? 0.1872 0.1673 0.1921 0.0008  0.0093  0.0218  236  TYR A CB  
1613  C CG  . TYR A 238  ? 0.2141 0.1943 0.2170 0.0006  0.0097  0.0204  236  TYR A CG  
1614  C CD1 . TYR A 238  ? 0.2821 0.2651 0.2836 -0.0006 0.0096  0.0198  236  TYR A CD1 
1615  C CD2 . TYR A 238  ? 0.2242 0.2020 0.2268 0.0018  0.0103  0.0196  236  TYR A CD2 
1616  C CE1 . TYR A 238  ? 0.2882 0.2715 0.2882 -0.0007 0.0100  0.0185  236  TYR A CE1 
1617  C CE2 . TYR A 238  ? 0.2825 0.2603 0.2834 0.0016  0.0107  0.0184  236  TYR A CE2 
1618  C CZ  . TYR A 238  ? 0.2965 0.2770 0.2962 0.0004  0.0105  0.0179  236  TYR A CZ  
1619  O OH  . TYR A 238  ? 0.3293 0.3100 0.3276 0.0004  0.0109  0.0167  236  TYR A OH  
1620  N N   . TYR A 239  ? 0.1901 0.1713 0.1994 -0.0001 0.0071  0.0260  237  TYR A N   
1621  C CA  . TYR A 239  ? 0.1898 0.1713 0.2011 0.0001  0.0066  0.0272  237  TYR A CA  
1622  C C   . TYR A 239  ? 0.2108 0.1959 0.2219 -0.0016 0.0055  0.0286  237  TYR A C   
1623  O O   . TYR A 239  ? 0.1948 0.1814 0.2063 -0.0018 0.0055  0.0283  237  TYR A O   
1624  C CB  . TYR A 239  ? 0.2181 0.1973 0.2321 0.0009  0.0059  0.0283  237  TYR A CB  
1625  C CG  . TYR A 239  ? 0.2217 0.2015 0.2381 0.0011  0.0054  0.0296  237  TYR A CG  
1626  C CD1 . TYR A 239  ? 0.2166 0.1984 0.2340 -0.0003 0.0039  0.0318  237  TYR A CD1 
1627  C CD2 . TYR A 239  ? 0.2324 0.2111 0.2500 0.0027  0.0064  0.0286  237  TYR A CD2 
1628  C CE1 . TYR A 239  ? 0.2603 0.2428 0.2800 -0.0002 0.0033  0.0330  237  TYR A CE1 
1629  C CE2 . TYR A 239  ? 0.2379 0.2173 0.2578 0.0028  0.0059  0.0297  237  TYR A CE2 
1630  C CZ  . TYR A 239  ? 0.2438 0.2249 0.2647 0.0014  0.0043  0.0318  237  TYR A CZ  
1631  O OH  . TYR A 239  ? 0.3031 0.2850 0.3265 0.0016  0.0038  0.0329  237  TYR A OH  
1632  N N   . ARG A 240  ? 0.2034 0.1901 0.2142 -0.0030 0.0045  0.0303  238  ARG A N   
1633  C CA  . ARG A 240  ? 0.1966 0.1876 0.2071 -0.0046 0.0034  0.0320  238  ARG A CA  
1634  C C   . ARG A 240  ? 0.1962 0.1906 0.2042 -0.0051 0.0039  0.0298  238  ARG A C   
1635  O O   . ARG A 240  ? 0.1972 0.1951 0.2052 -0.0059 0.0033  0.0301  238  ARG A O   
1636  C CB  . ARG A 240  ? 0.2508 0.2435 0.2620 -0.0061 0.0021  0.0349  238  ARG A CB  
1637  C CG  . ARG A 240  ? 0.3081 0.3020 0.3172 -0.0068 0.0024  0.0344  238  ARG A CG  
1638  C CD  . ARG A 240  ? 0.2595 0.2558 0.2698 -0.0085 0.0009  0.0381  238  ARG A CD  
1639  N NE  . ARG A 240  ? 0.2908 0.2875 0.2998 -0.0091 0.0013  0.0377  238  ARG A NE  
1640  C CZ  . ARG A 240  ? 0.3497 0.3424 0.3604 -0.0085 0.0011  0.0379  238  ARG A CZ  
1641  N NH1 . ARG A 240  ? 0.2706 0.2590 0.2846 -0.0074 0.0004  0.0384  238  ARG A NH1 
1642  N NH2 . ARG A 240  ? 0.3563 0.3497 0.3656 -0.0090 0.0015  0.0373  238  ARG A NH2 
1643  N N   . ASP A 241  ? 0.1974 0.1909 0.2037 -0.0046 0.0050  0.0274  239  ASP A N   
1644  C CA  . ASP A 241  ? 0.1897 0.1861 0.1945 -0.0048 0.0054  0.0249  239  ASP A CA  
1645  C C   . ASP A 241  ? 0.2171 0.2124 0.2236 -0.0039 0.0056  0.0235  239  ASP A C   
1646  O O   . ASP A 241  ? 0.2116 0.2101 0.2181 -0.0044 0.0051  0.0223  239  ASP A O   
1647  C CB  . ASP A 241  ? 0.2650 0.2602 0.2682 -0.0043 0.0064  0.0227  239  ASP A CB  
1648  C CG  . ASP A 241  ? 0.3765 0.3740 0.3781 -0.0054 0.0061  0.0237  239  ASP A CG  
1649  O OD1 . ASP A 241  ? 0.4299 0.4305 0.4316 -0.0067 0.0051  0.0262  239  ASP A OD1 
1650  O OD2 . ASP A 241  ? 0.5019 0.4984 0.5025 -0.0050 0.0069  0.0222  239  ASP A OD2 
1651  N N   . TYR A 242  ? 0.1958 0.1869 0.2038 -0.0026 0.0064  0.0236  240  TYR A N   
1652  C CA  . TYR A 242  ? 0.1956 0.1859 0.2055 -0.0019 0.0066  0.0229  240  TYR A CA  
1653  C C   . TYR A 242  ? 0.1887 0.1810 0.2001 -0.0025 0.0055  0.0245  240  TYR A C   
1654  O O   . TYR A 242  ? 0.1754 0.1695 0.1879 -0.0027 0.0050  0.0235  240  TYR A O   
1655  C CB  . TYR A 242  ? 0.1884 0.1748 0.1996 -0.0003 0.0076  0.0233  240  TYR A CB  
1656  C CG  . TYR A 242  ? 0.1862 0.1708 0.1965 0.0005  0.0088  0.0217  240  TYR A CG  
1657  C CD1 . TYR A 242  ? 0.2094 0.1950 0.2192 0.0003  0.0089  0.0197  240  TYR A CD1 
1658  C CD2 . TYR A 242  ? 0.1929 0.1748 0.2031 0.0017  0.0096  0.0221  240  TYR A CD2 
1659  C CE1 . TYR A 242  ? 0.2109 0.1948 0.2202 0.0011  0.0099  0.0186  240  TYR A CE1 
1660  C CE2 . TYR A 242  ? 0.1956 0.1762 0.2049 0.0025  0.0106  0.0209  240  TYR A CE2 
1661  C CZ  . TYR A 242  ? 0.1806 0.1621 0.1896 0.0022  0.0108  0.0194  240  TYR A CZ  
1662  O OH  . TYR A 242  ? 0.1972 0.1774 0.2055 0.0030  0.0116  0.0185  240  TYR A OH  
1663  N N   . GLU A 243  ? 0.1677 0.1597 0.1795 -0.0028 0.0048  0.0270  241  GLU A N   
1664  C CA  . GLU A 243  ? 0.1822 0.1761 0.1957 -0.0034 0.0036  0.0288  241  GLU A CA  
1665  C C   . GLU A 243  ? 0.1712 0.1702 0.1834 -0.0049 0.0026  0.0285  241  GLU A C   
1666  O O   . GLU A 243  ? 0.1887 0.1898 0.2020 -0.0051 0.0019  0.0281  241  GLU A O   
1667  C CB  . GLU A 243  ? 0.1898 0.1823 0.2046 -0.0035 0.0029  0.0316  241  GLU A CB  
1668  C CG  . GLU A 243  ? 0.2376 0.2321 0.2543 -0.0042 0.0015  0.0340  241  GLU A CG  
1669  C CD  . GLU A 243  ? 0.2819 0.2756 0.3001 -0.0047 0.0004  0.0369  241  GLU A CD  
1670  O OE1 . GLU A 243  ? 0.3654 0.3589 0.3824 -0.0052 0.0003  0.0374  241  GLU A OE1 
1671  O OE2 . GLU A 243  ? 0.2476 0.2408 0.2687 -0.0045 -0.0006 0.0388  241  GLU A OE2 
1672  N N   . SER A 244  ? 0.1829 0.1845 0.1927 -0.0058 0.0025  0.0284  242  SER A N   
1673  C CA  . SER A 244  ? 0.1770 0.1846 0.1853 -0.0070 0.0016  0.0278  242  SER A CA  
1674  C C   . SER A 244  ? 0.1948 0.2035 0.2031 -0.0065 0.0018  0.0240  242  SER A C   
1675  O O   . SER A 244  ? 0.2162 0.2291 0.2247 -0.0071 0.0009  0.0231  242  SER A O   
1676  C CB  . SER A 244  ? 0.2027 0.2134 0.2085 -0.0081 0.0015  0.0286  242  SER A CB  
1677  O OG  . SER A 244  ? 0.2548 0.2635 0.2594 -0.0075 0.0027  0.0263  242  SER A OG  
1678  N N   . ALA A 245  ? 0.1876 0.1928 0.1961 -0.0055 0.0030  0.0219  243  ALA A N   
1679  C CA  . ALA A 245  ? 0.1808 0.1865 0.1903 -0.0050 0.0030  0.0185  243  ALA A CA  
1680  C C   . ALA A 245  ? 0.1888 0.1934 0.2014 -0.0046 0.0025  0.0186  243  ALA A C   
1681  O O   . ALA A 245  ? 0.1914 0.1987 0.2052 -0.0047 0.0016  0.0164  243  ALA A O   
1682  C CB  . ALA A 245  ? 0.2061 0.2082 0.2157 -0.0040 0.0042  0.0167  243  ALA A CB  
1683  N N   . ILE A 246  ? 0.1747 0.1756 0.1888 -0.0040 0.0030  0.0210  244  ILE A N   
1684  C CA  . ILE A 246  ? 0.1789 0.1791 0.1960 -0.0036 0.0025  0.0214  244  ILE A CA  
1685  C C   . ILE A 246  ? 0.2093 0.2140 0.2266 -0.0047 0.0010  0.0218  244  ILE A C   
1686  O O   . ILE A 246  ? 0.1902 0.1964 0.2096 -0.0047 0.0002  0.0203  244  ILE A O   
1687  C CB  . ILE A 246  ? 0.1708 0.1671 0.1894 -0.0027 0.0034  0.0239  244  ILE A CB  
1688  C CG1 . ILE A 246  ? 0.1828 0.1755 0.2016 -0.0016 0.0049  0.0231  244  ILE A CG1 
1689  C CG2 . ILE A 246  ? 0.2080 0.2045 0.2298 -0.0026 0.0028  0.0247  244  ILE A CG2 
1690  C CD1 . ILE A 246  ? 0.2067 0.1964 0.2262 -0.0005 0.0058  0.0250  244  ILE A CD1 
1691  N N   . HIS A 247  ? 0.1785 0.1858 0.1938 -0.0056 0.0004  0.0240  245  HIS A N   
1692  C CA  . HIS A 247  ? 0.1797 0.1921 0.1949 -0.0066 -0.0012 0.0246  245  HIS A CA  
1693  C C   . HIS A 247  ? 0.1915 0.2086 0.2058 -0.0070 -0.0019 0.0210  245  HIS A C   
1694  O O   . HIS A 247  ? 0.1869 0.2067 0.2026 -0.0072 -0.0030 0.0197  245  HIS A O   
1695  C CB  . HIS A 247  ? 0.2083 0.2232 0.2216 -0.0077 -0.0018 0.0279  245  HIS A CB  
1696  C CG  . HIS A 247  ? 0.2097 0.2210 0.2249 -0.0074 -0.0018 0.0314  245  HIS A CG  
1697  N ND1 . HIS A 247  ? 0.2123 0.2232 0.2302 -0.0073 -0.0026 0.0328  245  HIS A ND1 
1698  C CD2 . HIS A 247  ? 0.2432 0.2512 0.2585 -0.0072 -0.0013 0.0334  245  HIS A CD2 
1699  C CE1 . HIS A 247  ? 0.2687 0.2764 0.2883 -0.0068 -0.0026 0.0355  245  HIS A CE1 
1700  N NE2 . HIS A 247  ? 0.2377 0.2434 0.2558 -0.0067 -0.0018 0.0358  245  HIS A NE2 
1701  N N   . ALA A 248  ? 0.1886 0.2067 0.2006 -0.0070 -0.0013 0.0190  246  ALA A N   
1702  C CA  . ALA A 248  ? 0.1874 0.2105 0.1988 -0.0072 -0.0020 0.0151  246  ALA A CA  
1703  C C   . ALA A 248  ? 0.2006 0.2214 0.2155 -0.0063 -0.0023 0.0119  246  ALA A C   
1704  O O   . ALA A 248  ? 0.2007 0.2254 0.2169 -0.0065 -0.0036 0.0093  246  ALA A O   
1705  C CB  . ALA A 248  ? 0.1906 0.2151 0.1993 -0.0073 -0.0012 0.0137  246  ALA A CB  
1706  N N   . ILE A 249  ? 0.1903 0.2050 0.2070 -0.0054 -0.0011 0.0122  247  ILE A N   
1707  C CA  . ILE A 249  ? 0.1711 0.1833 0.1918 -0.0047 -0.0014 0.0099  247  ILE A CA  
1708  C C   . ILE A 249  ? 0.1864 0.1988 0.2100 -0.0048 -0.0024 0.0110  247  ILE A C   
1709  O O   . ILE A 249  ? 0.1943 0.2081 0.2211 -0.0048 -0.0037 0.0084  247  ILE A O   
1710  C CB  . ILE A 249  ? 0.1761 0.1824 0.1979 -0.0038 0.0001  0.0109  247  ILE A CB  
1711  C CG1 . ILE A 249  ? 0.1824 0.1887 0.2019 -0.0035 0.0009  0.0092  247  ILE A CG1 
1712  C CG2 . ILE A 249  ? 0.1868 0.1906 0.2134 -0.0032 -0.0002 0.0096  247  ILE A CG2 
1713  C CD1 . ILE A 249  ? 0.2049 0.2061 0.2239 -0.0028 0.0026  0.0112  247  ILE A CD1 
1714  N N   . GLY A 250  ? 0.1776 0.1886 0.2008 -0.0050 -0.0020 0.0148  248  GLY A N   
1715  C CA  . GLY A 250  ? 0.1813 0.1926 0.2073 -0.0051 -0.0030 0.0160  248  GLY A CA  
1716  C C   . GLY A 250  ? 0.1875 0.2048 0.2130 -0.0060 -0.0048 0.0147  248  GLY A C   
1717  O O   . GLY A 250  ? 0.1941 0.2124 0.2227 -0.0060 -0.0060 0.0136  248  GLY A O   
1718  N N   . LYS A 251  ? 0.1854 0.2071 0.2070 -0.0067 -0.0051 0.0149  249  LYS A N   
1719  C CA  . LYS A 251  ? 0.1971 0.2257 0.2179 -0.0075 -0.0069 0.0135  249  LYS A CA  
1720  C C   . LYS A 251  ? 0.2067 0.2376 0.2294 -0.0071 -0.0078 0.0083  249  LYS A C   
1721  O O   . LYS A 251  ? 0.2118 0.2465 0.2362 -0.0073 -0.0095 0.0064  249  LYS A O   
1722  C CB  . LYS A 251  ? 0.2061 0.2397 0.2225 -0.0084 -0.0068 0.0148  249  LYS A CB  
1723  C CG  . LYS A 251  ? 0.2145 0.2475 0.2297 -0.0091 -0.0066 0.0199  249  LYS A CG  
1724  C CD  . LYS A 251  ? 0.2317 0.2692 0.2430 -0.0100 -0.0065 0.0211  249  LYS A CD  
1725  C CE  . LYS A 251  ? 0.2258 0.2627 0.2366 -0.0108 -0.0065 0.0264  249  LYS A CE  
1726  N NZ  . LYS A 251  ? 0.2401 0.2815 0.2475 -0.0118 -0.0063 0.0276  249  LYS A NZ  
1727  N N   . ALA A 252  ? 0.1964 0.2252 0.2190 -0.0065 -0.0070 0.0057  250  ALA A N   
1728  C CA  . ALA A 252  ? 0.2183 0.2490 0.2434 -0.0060 -0.0081 0.0005  250  ALA A CA  
1729  C C   . ALA A 252  ? 0.2221 0.2484 0.2529 -0.0054 -0.0087 -0.0003 250  ALA A C   
1730  O O   . ALA A 252  ? 0.2287 0.2574 0.2629 -0.0053 -0.0104 -0.0042 250  ALA A O   
1731  C CB  . ALA A 252  ? 0.2499 0.2796 0.2737 -0.0055 -0.0070 -0.0017 250  ALA A CB  
1732  N N   . SER A 253  ? 0.2184 0.2385 0.2507 -0.0051 -0.0073 0.0031  251  SER A N   
1733  C CA  . SER A 253  ? 0.1959 0.2124 0.2337 -0.0048 -0.0078 0.0030  251  SER A CA  
1734  C C   . SER A 253  ? 0.2208 0.2405 0.2610 -0.0052 -0.0096 0.0026  251  SER A C   
1735  O O   . SER A 253  ? 0.2234 0.2431 0.2685 -0.0051 -0.0112 -0.0001 251  SER A O   
1736  C CB  . SER A 253  ? 0.2094 0.2203 0.2478 -0.0044 -0.0059 0.0072  251  SER A CB  
1737  O OG  . SER A 253  ? 0.2065 0.2148 0.2503 -0.0042 -0.0064 0.0076  251  SER A OG  
1738  N N   . ALA A 254  ? 0.2154 0.2379 0.2524 -0.0058 -0.0097 0.0051  252  ALA A N   
1739  C CA  . ALA A 254  ? 0.2266 0.2532 0.2651 -0.0064 -0.0116 0.0049  252  ALA A CA  
1740  C C   . ALA A 254  ? 0.2639 0.2873 0.3083 -0.0062 -0.0123 0.0052  252  ALA A C   
1741  O O   . ALA A 254  ? 0.2451 0.2710 0.2930 -0.0063 -0.0143 0.0023  252  ALA A O   
1742  C CB  . ALA A 254  ? 0.2613 0.2948 0.2985 -0.0066 -0.0134 0.0003  252  ALA A CB  
1743  N N   . GLY A 255  ? 0.2190 0.2369 0.2647 -0.0058 -0.0106 0.0086  253  GLY A N   
1744  C CA  . GLY A 255  ? 0.2444 0.2597 0.2956 -0.0057 -0.0110 0.0098  253  GLY A CA  
1745  C C   . GLY A 255  ? 0.2156 0.2283 0.2722 -0.0053 -0.0115 0.0075  253  GLY A C   
1746  O O   . GLY A 255  ? 0.2559 0.2671 0.3178 -0.0054 -0.0121 0.0084  253  GLY A O   
1747  N N   . ARG A 256  ? 0.2208 0.2329 0.2766 -0.0050 -0.0112 0.0049  254  ARG A N   
1748  C CA  . ARG A 256  ? 0.2120 0.2214 0.2736 -0.0047 -0.0118 0.0030  254  ARG A CA  
1749  C C   . ARG A 256  ? 0.2119 0.2164 0.2758 -0.0044 -0.0101 0.0071  254  ARG A C   
1750  O O   . ARG A 256  ? 0.2419 0.2443 0.3119 -0.0043 -0.0107 0.0068  254  ARG A O   
1751  C CB  . ARG A 256  ? 0.2130 0.2230 0.2734 -0.0043 -0.0121 -0.0008 254  ARG A CB  
1752  C CG  . ARG A 256  ? 0.2403 0.2553 0.3016 -0.0044 -0.0145 -0.0061 254  ARG A CG  
1753  C CD  . ARG A 256  ? 0.2788 0.2948 0.3385 -0.0039 -0.0146 -0.0099 254  ARG A CD  
1754  N NE  . ARG A 256  ? 0.2385 0.2567 0.2908 -0.0039 -0.0129 -0.0087 254  ARG A NE  
1755  C CZ  . ARG A 256  ? 0.2677 0.2867 0.3174 -0.0035 -0.0123 -0.0110 254  ARG A CZ  
1756  N NH1 . ARG A 256  ? 0.2938 0.3113 0.3477 -0.0029 -0.0131 -0.0145 254  ARG A NH1 
1757  N NH2 . ARG A 256  ? 0.2578 0.2795 0.3010 -0.0038 -0.0110 -0.0098 254  ARG A NH2 
1758  N N   . GLY A 257  ? 0.2089 0.2120 0.2686 -0.0041 -0.0079 0.0107  255  GLY A N   
1759  C CA  . GLY A 257  ? 0.2037 0.2032 0.2654 -0.0037 -0.0062 0.0144  255  GLY A CA  
1760  C C   . GLY A 257  ? 0.1853 0.1823 0.2459 -0.0031 -0.0048 0.0144  255  GLY A C   
1761  O O   . GLY A 257  ? 0.2011 0.1986 0.2596 -0.0031 -0.0051 0.0115  255  GLY A O   
1762  N N   . ILE A 258  ? 0.1808 0.1753 0.2431 -0.0027 -0.0032 0.0178  256  ILE A N   
1763  C CA  . ILE A 258  ? 0.1826 0.1749 0.2426 -0.0021 -0.0015 0.0185  256  ILE A CA  
1764  C C   . ILE A 258  ? 0.2022 0.1932 0.2666 -0.0022 -0.0024 0.0169  256  ILE A C   
1765  O O   . ILE A 258  ? 0.1879 0.1775 0.2502 -0.0017 -0.0014 0.0166  256  ILE A O   
1766  C CB  . ILE A 258  ? 0.1774 0.1685 0.2369 -0.0014 0.0007  0.0226  256  ILE A CB  
1767  C CG1 . ILE A 258  ? 0.1996 0.1905 0.2657 -0.0016 0.0004  0.0249  256  ILE A CG1 
1768  C CG2 . ILE A 258  ? 0.1903 0.1823 0.2456 -0.0012 0.0015  0.0239  256  ILE A CG2 
1769  C CD1 . ILE A 258  ? 0.2161 0.2068 0.2819 -0.0009 0.0026  0.0288  256  ILE A CD1 
1770  N N   . TYR A 259  ? 0.2107 0.2021 0.2816 -0.0027 -0.0044 0.0158  257  TYR A N   
1771  C CA  . TYR A 259  ? 0.2072 0.1971 0.2834 -0.0027 -0.0055 0.0143  257  TYR A CA  
1772  C C   . TYR A 259  ? 0.2268 0.2181 0.3032 -0.0028 -0.0076 0.0090  257  TYR A C   
1773  O O   . TYR A 259  ? 0.2461 0.2365 0.3218 -0.0024 -0.0076 0.0071  257  TYR A O   
1774  C CB  . TYR A 259  ? 0.2359 0.2251 0.3202 -0.0033 -0.0066 0.0165  257  TYR A CB  
1775  C CG  . TYR A 259  ? 0.2066 0.1955 0.2906 -0.0031 -0.0045 0.0217  257  TYR A CG  
1776  C CD1 . TYR A 259  ? 0.2312 0.2190 0.3127 -0.0025 -0.0023 0.0245  257  TYR A CD1 
1777  C CD2 . TYR A 259  ? 0.2069 0.1971 0.2931 -0.0034 -0.0047 0.0237  257  TYR A CD2 
1778  C CE1 . TYR A 259  ? 0.2376 0.2260 0.3187 -0.0021 -0.0003 0.0288  257  TYR A CE1 
1779  C CE2 . TYR A 259  ? 0.2281 0.2187 0.3141 -0.0031 -0.0027 0.0281  257  TYR A CE2 
1780  C CZ  . TYR A 259  ? 0.2257 0.2155 0.3091 -0.0024 -0.0005 0.0306  257  TYR A CZ  
1781  O OH  . TYR A 259  ? 0.2169 0.2079 0.3000 -0.0020 0.0015  0.0346  257  TYR A OH  
1782  N N   . GLU A 260  ? 0.2141 0.2080 0.2913 -0.0032 -0.0094 0.0064  258  GLU A N   
1783  C CA  . GLU A 260  ? 0.2639 0.2603 0.3411 -0.0032 -0.0114 0.0009  258  GLU A CA  
1784  C C   . GLU A 260  ? 0.2537 0.2522 0.3227 -0.0029 -0.0101 -0.0005 258  GLU A C   
1785  O O   . GLU A 260  ? 0.2968 0.2967 0.3649 -0.0025 -0.0108 -0.0044 258  GLU A O   
1786  C CB  . GLU A 260  ? 0.2824 0.2816 0.3629 -0.0036 -0.0138 -0.0016 258  GLU A CB  
1787  C CG  . GLU A 260  ? 0.4115 0.4140 0.4926 -0.0034 -0.0161 -0.0079 258  GLU A CG  
1788  C CD  . GLU A 260  ? 0.4647 0.4715 0.5468 -0.0038 -0.0182 -0.0107 258  GLU A CD  
1789  O OE1 . GLU A 260  ? 0.4832 0.4894 0.5685 -0.0043 -0.0186 -0.0082 258  GLU A OE1 
1790  O OE2 . GLU A 260  ? 0.4430 0.4542 0.5225 -0.0035 -0.0193 -0.0153 258  GLU A OE2 
1791  N N   . GLY A 261  ? 0.2076 0.2066 0.2711 -0.0030 -0.0083 0.0027  259  GLY A N   
1792  C CA  . GLY A 261  ? 0.1845 0.1859 0.2408 -0.0030 -0.0075 0.0019  259  GLY A CA  
1793  C C   . GLY A 261  ? 0.2021 0.2011 0.2545 -0.0025 -0.0053 0.0036  259  GLY A C   
1794  O O   . GLY A 261  ? 0.1983 0.1938 0.2527 -0.0021 -0.0042 0.0061  259  GLY A O   
1795  N N   . PRO A 262  ? 0.1842 0.1855 0.2309 -0.0025 -0.0048 0.0024  260  PRO A N   
1796  C CA  . PRO A 262  ? 0.2048 0.2042 0.2478 -0.0021 -0.0030 0.0035  260  PRO A CA  
1797  C C   . PRO A 262  ? 0.1972 0.1941 0.2375 -0.0020 -0.0011 0.0080  260  PRO A C   
1798  O O   . PRO A 262  ? 0.2229 0.2204 0.2630 -0.0022 -0.0010 0.0102  260  PRO A O   
1799  C CB  . PRO A 262  ? 0.1932 0.1968 0.2315 -0.0024 -0.0033 0.0010  260  PRO A CB  
1800  C CG  . PRO A 262  ? 0.2104 0.2180 0.2482 -0.0030 -0.0046 0.0007  260  PRO A CG  
1801  C CD  . PRO A 262  ? 0.2076 0.2141 0.2516 -0.0030 -0.0061 -0.0002 260  PRO A CD  
1802  N N   . GLY A 263  ? 0.1862 0.1804 0.2248 -0.0014 0.0005  0.0092  261  GLY A N   
1803  C CA  . GLY A 263  ? 0.1869 0.1792 0.2227 -0.0011 0.0023  0.0127  261  GLY A CA  
1804  C C   . GLY A 263  ? 0.1599 0.1517 0.1911 -0.0008 0.0034  0.0125  261  GLY A C   
1805  O O   . GLY A 263  ? 0.1761 0.1695 0.2058 -0.0010 0.0029  0.0098  261  GLY A O   
1806  N N   . ILE A 264  ? 0.1716 0.1613 0.2008 -0.0003 0.0049  0.0151  262  ILE A N   
1807  C CA  . ILE A 264  ? 0.1747 0.1636 0.1999 0.0000  0.0060  0.0152  262  ILE A CA  
1808  C C   . ILE A 264  ? 0.1924 0.1784 0.2182 0.0009  0.0074  0.0168  262  ILE A C   
1809  O O   . ILE A 264  ? 0.1935 0.1786 0.2219 0.0014  0.0079  0.0187  262  ILE A O   
1810  C CB  . ILE A 264  ? 0.1874 0.1772 0.2092 -0.0004 0.0062  0.0168  262  ILE A CB  
1811  C CG1 . ILE A 264  ? 0.2024 0.1922 0.2205 -0.0004 0.0068  0.0164  262  ILE A CG1 
1812  C CG2 . ILE A 264  ? 0.1960 0.1840 0.2187 0.0003  0.0070  0.0196  262  ILE A CG2 
1813  C CD1 . ILE A 264  ? 0.2198 0.2108 0.2353 -0.0010 0.0066  0.0180  262  ILE A CD1 
1814  N N   . SER A 265  ? 0.1652 0.1504 0.1887 0.0012  0.0081  0.0160  263  SER A N   
1815  C CA  . SER A 265  ? 0.1751 0.1582 0.1982 0.0022  0.0094  0.0174  263  SER A CA  
1816  C C   . SER A 265  ? 0.1909 0.1735 0.2098 0.0024  0.0102  0.0179  263  SER A C   
1817  O O   . SER A 265  ? 0.2458 0.2295 0.2623 0.0018  0.0098  0.0166  263  SER A O   
1818  C CB  . SER A 265  ? 0.2061 0.1885 0.2307 0.0024  0.0094  0.0161  263  SER A CB  
1819  O OG  . SER A 265  ? 0.2220 0.2043 0.2515 0.0022  0.0085  0.0161  263  SER A OG  
1820  N N   . ILE A 266  ? 0.1860 0.1674 0.2044 0.0034  0.0114  0.0197  264  ILE A N   
1821  C CA  . ILE A 266  ? 0.1856 0.1661 0.2008 0.0038  0.0120  0.0200  264  ILE A CA  
1822  C C   . ILE A 266  ? 0.1870 0.1665 0.2017 0.0049  0.0132  0.0203  264  ILE A C   
1823  O O   . ILE A 266  ? 0.1893 0.1688 0.2061 0.0055  0.0137  0.0212  264  ILE A O   
1824  C CB  . ILE A 266  ? 0.1827 0.1633 0.1980 0.0040  0.0119  0.0214  264  ILE A CB  
1825  C CG1 . ILE A 266  ? 0.2044 0.1849 0.2220 0.0051  0.0128  0.0229  264  ILE A CG1 
1826  C CG2 . ILE A 266  ? 0.2117 0.1939 0.2277 0.0029  0.0106  0.0214  264  ILE A CG2 
1827  C CD1 . ILE A 266  ? 0.2257 0.2061 0.2434 0.0058  0.0128  0.0239  264  ILE A CD1 
1828  N N   . LYS A 267  ? 0.1856 0.1643 0.1975 0.0052  0.0135  0.0198  265  LYS A N   
1829  C CA  . LYS A 267  ? 0.1661 0.1441 0.1770 0.0064  0.0145  0.0200  265  LYS A CA  
1830  C C   . LYS A 267  ? 0.1779 0.1555 0.1878 0.0073  0.0148  0.0204  265  LYS A C   
1831  O O   . LYS A 267  ? 0.1867 0.1637 0.1955 0.0067  0.0141  0.0201  265  LYS A O   
1832  C CB  . LYS A 267  ? 0.2137 0.1911 0.2226 0.0062  0.0145  0.0186  265  LYS A CB  
1833  C CG  . LYS A 267  ? 0.2066 0.1843 0.2172 0.0059  0.0143  0.0180  265  LYS A CG  
1834  C CD  . LYS A 267  ? 0.2444 0.2218 0.2531 0.0057  0.0142  0.0165  265  LYS A CD  
1835  C CE  . LYS A 267  ? 0.2923 0.2698 0.3034 0.0056  0.0139  0.0159  265  LYS A CE  
1836  N NZ  . LYS A 267  ? 0.3127 0.2911 0.3263 0.0047  0.0128  0.0150  265  LYS A NZ  
1837  N N   . LEU A 268  ? 0.1749 0.1530 0.1855 0.0087  0.0157  0.0212  266  LEU A N   
1838  C CA  . LEU A 268  ? 0.1844 0.1624 0.1946 0.0098  0.0159  0.0210  266  LEU A CA  
1839  C C   . LEU A 268  ? 0.1913 0.1680 0.1993 0.0100  0.0156  0.0197  266  LEU A C   
1840  O O   . LEU A 268  ? 0.2032 0.1791 0.2114 0.0102  0.0149  0.0193  266  LEU A O   
1841  C CB  . LEU A 268  ? 0.1967 0.1765 0.2079 0.0114  0.0171  0.0217  266  LEU A CB  
1842  C CG  . LEU A 268  ? 0.2039 0.1851 0.2179 0.0112  0.0173  0.0234  266  LEU A CG  
1843  C CD1 . LEU A 268  ? 0.2154 0.1992 0.2303 0.0128  0.0186  0.0243  266  LEU A CD1 
1844  C CD2 . LEU A 268  ? 0.2286 0.2091 0.2439 0.0105  0.0163  0.0236  266  LEU A CD2 
1845  N N   . SER A 269  ? 0.1791 0.1556 0.1854 0.0099  0.0159  0.0190  267  SER A N   
1846  C CA  . SER A 269  ? 0.2027 0.1781 0.2071 0.0100  0.0156  0.0177  267  SER A CA  
1847  C C   . SER A 269  ? 0.2159 0.1904 0.2200 0.0085  0.0144  0.0176  267  SER A C   
1848  O O   . SER A 269  ? 0.2165 0.1900 0.2199 0.0085  0.0139  0.0169  267  SER A O   
1849  C CB  . SER A 269  ? 0.2124 0.1881 0.2154 0.0101  0.0162  0.0171  267  SER A CB  
1850  O OG  . SER A 269  ? 0.2150 0.1905 0.2180 0.0087  0.0157  0.0170  267  SER A OG  
1851  N N   . ALA A 270  ? 0.1886 0.1637 0.1935 0.0072  0.0139  0.0183  268  ALA A N   
1852  C CA  . ALA A 270  ? 0.1954 0.1705 0.2000 0.0057  0.0128  0.0186  268  ALA A CA  
1853  C C   . ALA A 270  ? 0.1944 0.1690 0.2005 0.0059  0.0119  0.0196  268  ALA A C   
1854  O O   . ALA A 270  ? 0.2088 0.1833 0.2150 0.0048  0.0109  0.0202  268  ALA A O   
1855  C CB  . ALA A 270  ? 0.2094 0.1862 0.2144 0.0044  0.0124  0.0188  268  ALA A CB  
1856  N N   . LEU A 271  ? 0.1868 0.1612 0.1945 0.0071  0.0124  0.0199  269  LEU A N   
1857  C CA  . LEU A 271  ? 0.1893 0.1633 0.1992 0.0072  0.0115  0.0208  269  LEU A CA  
1858  C C   . LEU A 271  ? 0.2073 0.1800 0.2181 0.0087  0.0112  0.0199  269  LEU A C   
1859  O O   . LEU A 271  ? 0.2152 0.1873 0.2285 0.0090  0.0103  0.0205  269  LEU A O   
1860  C CB  . LEU A 271  ? 0.2040 0.1791 0.2156 0.0076  0.0118  0.0217  269  LEU A CB  
1861  C CG  . LEU A 271  ? 0.2132 0.1897 0.2247 0.0060  0.0115  0.0224  269  LEU A CG  
1862  C CD1 . LEU A 271  ? 0.2814 0.2588 0.2949 0.0065  0.0119  0.0231  269  LEU A CD1 
1863  C CD2 . LEU A 271  ? 0.2468 0.2237 0.2584 0.0045  0.0101  0.0235  269  LEU A CD2 
1864  N N   . HIS A 272  ? 0.2093 0.1817 0.2187 0.0097  0.0119  0.0184  270  HIS A N   
1865  C CA  . HIS A 272  ? 0.2092 0.1805 0.2197 0.0111  0.0114  0.0171  270  HIS A CA  
1866  C C   . HIS A 272  ? 0.1978 0.1687 0.2062 0.0114  0.0117  0.0156  270  HIS A C   
1867  O O   . HIS A 272  ? 0.2132 0.1852 0.2195 0.0116  0.0130  0.0153  270  HIS A O   
1868  C CB  . HIS A 272  ? 0.2052 0.1777 0.2170 0.0132  0.0122  0.0162  270  HIS A CB  
1869  C CG  . HIS A 272  ? 0.2159 0.1875 0.2300 0.0147  0.0113  0.0146  270  HIS A CG  
1870  N ND1 . HIS A 272  ? 0.2404 0.2116 0.2539 0.0159  0.0111  0.0124  270  HIS A ND1 
1871  C CD2 . HIS A 272  ? 0.2554 0.2265 0.2730 0.0154  0.0102  0.0146  270  HIS A CD2 
1872  C CE1 . HIS A 272  ? 0.2654 0.2358 0.2820 0.0171  0.0099  0.0109  270  HIS A CE1 
1873  N NE2 . HIS A 272  ? 0.2748 0.2451 0.2940 0.0169  0.0093  0.0122  270  HIS A NE2 
1874  N N   . PRO A 273  ? 0.2038 0.1732 0.2130 0.0114  0.0105  0.0147  271  PRO A N   
1875  C CA  . PRO A 273  ? 0.2028 0.1719 0.2101 0.0116  0.0107  0.0133  271  PRO A CA  
1876  C C   . PRO A 273  ? 0.2136 0.1837 0.2200 0.0139  0.0117  0.0112  271  PRO A C   
1877  O O   . PRO A 273  ? 0.2256 0.1959 0.2301 0.0141  0.0121  0.0101  271  PRO A O   
1878  C CB  . PRO A 273  ? 0.2132 0.1804 0.2226 0.0109  0.0089  0.0133  271  PRO A CB  
1879  C CG  . PRO A 273  ? 0.2456 0.2120 0.2585 0.0115  0.0078  0.0137  271  PRO A CG  
1880  C CD  . PRO A 273  ? 0.2185 0.1864 0.2310 0.0110  0.0087  0.0153  271  PRO A CD  
1881  N N   . ARG A 274  ? 0.1884 0.1597 0.1963 0.0155  0.0121  0.0106  272  ARG A N   
1882  C CA  . ARG A 274  ? 0.1898 0.1632 0.1967 0.0178  0.0131  0.0086  272  ARG A CA  
1883  C C   . ARG A 274  ? 0.2163 0.1926 0.2228 0.0185  0.0147  0.0097  272  ARG A C   
1884  O O   . ARG A 274  ? 0.2264 0.2048 0.2341 0.0203  0.0152  0.0087  272  ARG A O   
1885  C CB  . ARG A 274  ? 0.2085 0.1816 0.2181 0.0196  0.0120  0.0061  272  ARG A CB  
1886  C CG  . ARG A 274  ? 0.2141 0.1846 0.2249 0.0190  0.0102  0.0049  272  ARG A CG  
1887  C CD  . ARG A 274  ? 0.2243 0.1951 0.2319 0.0188  0.0107  0.0041  272  ARG A CD  
1888  N NE  . ARG A 274  ? 0.2334 0.2074 0.2391 0.0209  0.0120  0.0022  272  ARG A NE  
1889  C CZ  . ARG A 274  ? 0.2264 0.2015 0.2332 0.0231  0.0114  -0.0010 272  ARG A CZ  
1890  N NH1 . ARG A 274  ? 0.2298 0.2027 0.2403 0.0234  0.0094  -0.0028 272  ARG A NH1 
1891  N NH2 . ARG A 274  ? 0.2374 0.2163 0.2419 0.0249  0.0126  -0.0025 272  ARG A NH2 
1892  N N   . TYR A 275  ? 0.1908 0.1673 0.1959 0.0171  0.0155  0.0117  273  TYR A N   
1893  C CA  . TYR A 275  ? 0.1761 0.1551 0.1814 0.0174  0.0168  0.0133  273  TYR A CA  
1894  C C   . TYR A 275  ? 0.2066 0.1884 0.2100 0.0187  0.0181  0.0128  273  TYR A C   
1895  O O   . TYR A 275  ? 0.2040 0.1858 0.2058 0.0179  0.0185  0.0136  273  TYR A O   
1896  C CB  . TYR A 275  ? 0.2000 0.1779 0.2054 0.0153  0.0168  0.0153  273  TYR A CB  
1897  C CG  . TYR A 275  ? 0.1676 0.1477 0.1737 0.0155  0.0179  0.0171  273  TYR A CG  
1898  C CD1 . TYR A 275  ? 0.1881 0.1704 0.1959 0.0166  0.0185  0.0175  273  TYR A CD1 
1899  C CD2 . TYR A 275  ? 0.1790 0.1593 0.1845 0.0144  0.0183  0.0182  273  TYR A CD2 
1900  C CE1 . TYR A 275  ? 0.2041 0.1887 0.2130 0.0166  0.0195  0.0195  273  TYR A CE1 
1901  C CE2 . TYR A 275  ? 0.1854 0.1677 0.1924 0.0144  0.0191  0.0201  273  TYR A CE2 
1902  C CZ  . TYR A 275  ? 0.1864 0.1709 0.1950 0.0155  0.0198  0.0209  273  TYR A CZ  
1903  O OH  . TYR A 275  ? 0.2127 0.1995 0.2232 0.0154  0.0205  0.0230  273  TYR A OH  
1904  N N   . SER A 276  ? 0.1774 0.1621 0.1811 0.0208  0.0187  0.0116  274  SER A N   
1905  C CA  . SER A 276  ? 0.1632 0.1517 0.1651 0.0222  0.0199  0.0113  274  SER A CA  
1906  C C   . SER A 276  ? 0.1957 0.1884 0.1986 0.0244  0.0207  0.0104  274  SER A C   
1907  O O   . SER A 276  ? 0.2019 0.1940 0.2069 0.0252  0.0200  0.0090  274  SER A O   
1908  C CB  . SER A 276  ? 0.2266 0.2143 0.2267 0.0228  0.0193  0.0090  274  SER A CB  
1909  O OG  . SER A 276  ? 0.2783 0.2656 0.2795 0.0242  0.0183  0.0060  274  SER A OG  
1910  N N   . ARG A 277  ? 0.1849 0.1824 0.1865 0.0254  0.0221  0.0114  275  ARG A N   
1911  C CA  . ARG A 277  ? 0.1847 0.1877 0.1869 0.0277  0.0232  0.0106  275  ARG A CA  
1912  C C   . ARG A 277  ? 0.1986 0.2022 0.2010 0.0298  0.0223  0.0063  275  ARG A C   
1913  O O   . ARG A 277  ? 0.2019 0.2078 0.2061 0.0314  0.0224  0.0046  275  ARG A O   
1914  C CB  . ARG A 277  ? 0.2012 0.2099 0.2018 0.0283  0.0248  0.0127  275  ARG A CB  
1915  C CG  . ARG A 277  ? 0.1880 0.2039 0.1886 0.0308  0.0260  0.0117  275  ARG A CG  
1916  C CD  . ARG A 277  ? 0.2022 0.2193 0.2058 0.0311  0.0264  0.0124  275  ARG A CD  
1917  N NE  . ARG A 277  ? 0.1951 0.2198 0.1988 0.0336  0.0276  0.0113  275  ARG A NE  
1918  C CZ  . ARG A 277  ? 0.1948 0.2214 0.1989 0.0360  0.0272  0.0070  275  ARG A CZ  
1919  N NH1 . ARG A 277  ? 0.1941 0.2153 0.1988 0.0361  0.0254  0.0036  275  ARG A NH1 
1920  N NH2 . ARG A 277  ? 0.1953 0.2297 0.1997 0.0383  0.0285  0.0061  275  ARG A NH2 
1921  N N   . ALA A 278  ? 0.1997 0.2009 0.2005 0.0297  0.0213  0.0042  276  ALA A N   
1922  C CA  . ALA A 278  ? 0.2108 0.2125 0.2124 0.0317  0.0202  -0.0002 276  ALA A CA  
1923  C C   . ALA A 278  ? 0.1869 0.1847 0.1921 0.0316  0.0187  -0.0016 276  ALA A C   
1924  O O   . ALA A 278  ? 0.2367 0.2358 0.2439 0.0337  0.0178  -0.0051 276  ALA A O   
1925  C CB  . ALA A 278  ? 0.2206 0.2199 0.2203 0.0313  0.0192  -0.0018 276  ALA A CB  
1926  N N   . GLN A 279  ? 0.1963 0.1896 0.2025 0.0293  0.0182  0.0011  277  GLN A N   
1927  C CA  . GLN A 279  ? 0.1930 0.1826 0.2027 0.0288  0.0166  0.0007  277  GLN A CA  
1928  C C   . GLN A 279  ? 0.2191 0.2099 0.2305 0.0285  0.0174  0.0030  277  GLN A C   
1929  O O   . GLN A 279  ? 0.1972 0.1846 0.2107 0.0270  0.0164  0.0045  277  GLN A O   
1930  C CB  . GLN A 279  ? 0.2040 0.1881 0.2138 0.0263  0.0152  0.0019  277  GLN A CB  
1931  C CG  . GLN A 279  ? 0.2285 0.2112 0.2372 0.0265  0.0142  -0.0003 277  GLN A CG  
1932  C CD  . GLN A 279  ? 0.2629 0.2456 0.2745 0.0285  0.0127  -0.0042 277  GLN A CD  
1933  O OE1 . GLN A 279  ? 0.3754 0.3566 0.3908 0.0289  0.0115  -0.0047 277  GLN A OE1 
1934  N NE2 . GLN A 279  ? 0.2328 0.2175 0.2429 0.0300  0.0126  -0.0070 277  GLN A NE2 
1935  N N   . ALA A 280  ? 0.2066 0.2027 0.2172 0.0298  0.0192  0.0037  278  ALA A N   
1936  C CA  . ALA A 280  ? 0.2159 0.2134 0.2280 0.0292  0.0201  0.0064  278  ALA A CA  
1937  C C   . ALA A 280  ? 0.2025 0.1982 0.2184 0.0297  0.0189  0.0053  278  ALA A C   
1938  O O   . ALA A 280  ? 0.2061 0.2001 0.2236 0.0282  0.0187  0.0078  278  ALA A O   
1939  C CB  . ALA A 280  ? 0.2314 0.2357 0.2425 0.0308  0.0222  0.0071  278  ALA A CB  
1940  N N   . ALA A 281  ? 0.1895 0.1858 0.2073 0.0318  0.0179  0.0016  279  ALA A N   
1941  C CA  . ALA A 281  ? 0.2209 0.2156 0.2431 0.0324  0.0165  0.0006  279  ALA A CA  
1942  C C   . ALA A 281  ? 0.2190 0.2075 0.2427 0.0299  0.0147  0.0024  279  ALA A C   
1943  O O   . ALA A 281  ? 0.2235 0.2106 0.2498 0.0291  0.0141  0.0042  279  ALA A O   
1944  C CB  . ALA A 281  ? 0.2578 0.2541 0.2824 0.0353  0.0155  -0.0042 279  ALA A CB  
1945  N N   . ARG A 282  ? 0.2046 0.1897 0.2267 0.0286  0.0137  0.0023  280  ARG A N   
1946  C CA  . ARG A 282  ? 0.2042 0.1845 0.2274 0.0261  0.0121  0.0045  280  ARG A CA  
1947  C C   . ARG A 282  ? 0.1964 0.1765 0.2176 0.0239  0.0132  0.0082  280  ARG A C   
1948  O O   . ARG A 282  ? 0.2040 0.1818 0.2269 0.0222  0.0121  0.0102  280  ARG A O   
1949  C CB  . ARG A 282  ? 0.2155 0.1930 0.2374 0.0252  0.0111  0.0035  280  ARG A CB  
1950  C CG  . ARG A 282  ? 0.2479 0.2245 0.2728 0.0270  0.0093  -0.0001 280  ARG A CG  
1951  C CD  . ARG A 282  ? 0.2476 0.2209 0.2719 0.0255  0.0080  -0.0001 280  ARG A CD  
1952  N NE  . ARG A 282  ? 0.2461 0.2159 0.2718 0.0228  0.0067  0.0032  280  ARG A NE  
1953  C CZ  . ARG A 282  ? 0.2431 0.2105 0.2676 0.0208  0.0059  0.0046  280  ARG A CZ  
1954  N NH1 . ARG A 282  ? 0.2472 0.2147 0.2694 0.0210  0.0062  0.0030  280  ARG A NH1 
1955  N NH2 . ARG A 282  ? 0.2466 0.2121 0.2725 0.0184  0.0049  0.0077  280  ARG A NH2 
1956  N N   . VAL A 283  ? 0.2038 0.1865 0.2218 0.0238  0.0150  0.0091  281  VAL A N   
1957  C CA  . VAL A 283  ? 0.2002 0.1829 0.2170 0.0219  0.0159  0.0122  281  VAL A CA  
1958  C C   . VAL A 283  ? 0.2053 0.1892 0.2249 0.0221  0.0160  0.0136  281  VAL A C   
1959  O O   . VAL A 283  ? 0.2013 0.1833 0.2219 0.0203  0.0153  0.0156  281  VAL A O   
1960  C CB  . VAL A 283  ? 0.1857 0.1713 0.1996 0.0221  0.0177  0.0130  281  VAL A CB  
1961  C CG1 . VAL A 283  ? 0.2149 0.2008 0.2288 0.0205  0.0184  0.0160  281  VAL A CG1 
1962  C CG2 . VAL A 283  ? 0.2072 0.1910 0.2185 0.0214  0.0173  0.0121  281  VAL A CG2 
1963  N N   . MET A 284  ? 0.1907 0.1782 0.2117 0.0243  0.0169  0.0124  282  MET A N   
1964  C CA  . MET A 284  ? 0.1941 0.1830 0.2180 0.0245  0.0170  0.0136  282  MET A CA  
1965  C C   . MET A 284  ? 0.2249 0.2107 0.2521 0.0242  0.0150  0.0132  282  MET A C   
1966  O O   . MET A 284  ? 0.2492 0.2346 0.2785 0.0232  0.0146  0.0152  282  MET A O   
1967  C CB  . MET A 284  ? 0.2081 0.2024 0.2328 0.0271  0.0185  0.0123  282  MET A CB  
1968  C CG  . MET A 284  ? 0.2273 0.2256 0.2491 0.0273  0.0205  0.0133  282  MET A CG  
1969  S SD  . MET A 284  ? 0.2494 0.2469 0.2704 0.0246  0.0212  0.0176  282  MET A SD  
1970  C CE  . MET A 284  ? 0.2466 0.2461 0.2715 0.0248  0.0214  0.0193  282  MET A CE  
1971  N N   . GLY A 285  ? 0.1970 0.1807 0.2253 0.0250  0.0135  0.0109  283  GLY A N   
1972  C CA  . GLY A 285  ? 0.2151 0.1960 0.2475 0.0248  0.0114  0.0107  283  GLY A CA  
1973  C C   . GLY A 285  ? 0.2149 0.1920 0.2470 0.0220  0.0099  0.0133  283  GLY A C   
1974  O O   . GLY A 285  ? 0.2369 0.2125 0.2721 0.0212  0.0085  0.0148  283  GLY A O   
1975  N N   . GLU A 286  ? 0.2033 0.1794 0.2319 0.0206  0.0103  0.0139  284  GLU A N   
1976  C CA  . GLU A 286  ? 0.2118 0.1850 0.2400 0.0181  0.0089  0.0158  284  GLU A CA  
1977  C C   . GLU A 286  ? 0.2078 0.1816 0.2327 0.0161  0.0099  0.0180  284  GLU A C   
1978  O O   . GLU A 286  ? 0.2517 0.2245 0.2769 0.0141  0.0089  0.0202  284  GLU A O   
1979  C CB  . GLU A 286  ? 0.2121 0.1833 0.2395 0.0181  0.0080  0.0142  284  GLU A CB  
1980  C CG  . GLU A 286  ? 0.2601 0.2304 0.2914 0.0200  0.0066  0.0116  284  GLU A CG  
1981  C CD  . GLU A 286  ? 0.2561 0.2250 0.2866 0.0203  0.0059  0.0096  284  GLU A CD  
1982  O OE1 . GLU A 286  ? 0.2841 0.2517 0.3122 0.0183  0.0058  0.0111  284  GLU A OE1 
1983  O OE2 . GLU A 286  ? 0.3034 0.2728 0.3359 0.0226  0.0055  0.0063  284  GLU A OE2 
1984  N N   . LEU A 287  ? 0.1898 0.1653 0.2117 0.0165  0.0117  0.0175  285  LEU A N   
1985  C CA  A LEU A 287  ? 0.2021 0.1781 0.2217 0.0147  0.0124  0.0193  285  LEU A CA  
1986  C CA  B LEU A 287  ? 0.2027 0.1786 0.2222 0.0147  0.0124  0.0193  285  LEU A CA  
1987  C C   . LEU A 287  ? 0.2125 0.1901 0.2336 0.0145  0.0129  0.0209  285  LEU A C   
1988  O O   . LEU A 287  ? 0.2102 0.1874 0.2313 0.0127  0.0123  0.0225  285  LEU A O   
1989  C CB  A LEU A 287  ? 0.2031 0.1802 0.2197 0.0152  0.0139  0.0184  285  LEU A CB  
1990  C CB  B LEU A 287  ? 0.2034 0.1805 0.2200 0.0152  0.0139  0.0184  285  LEU A CB  
1991  C CG  A LEU A 287  ? 0.2153 0.1919 0.2294 0.0134  0.0142  0.0193  285  LEU A CG  
1992  C CG  B LEU A 287  ? 0.2174 0.1956 0.2326 0.0141  0.0149  0.0199  285  LEU A CG  
1993  C CD1 A LEU A 287  ? 0.2136 0.1912 0.2255 0.0143  0.0154  0.0183  285  LEU A CD1 
1994  C CD1 B LEU A 287  ? 0.2490 0.2258 0.2636 0.0119  0.0139  0.0209  285  LEU A CD1 
1995  C CD2 A LEU A 287  ? 0.2394 0.2172 0.2544 0.0125  0.0146  0.0210  285  LEU A CD2 
1996  C CD2 B LEU A 287  ? 0.2112 0.1905 0.2242 0.0147  0.0162  0.0192  285  LEU A CD2 
1997  N N   . LEU A 288  ? 0.2066 0.1864 0.2291 0.0163  0.0139  0.0204  286  LEU A N   
1998  C CA  . LEU A 288  ? 0.1991 0.1807 0.2236 0.0161  0.0144  0.0220  286  LEU A CA  
1999  C C   . LEU A 288  ? 0.2256 0.2059 0.2523 0.0148  0.0128  0.0234  286  LEU A C   
2000  O O   . LEU A 288  ? 0.2069 0.1877 0.2336 0.0134  0.0127  0.0250  286  LEU A O   
2001  C CB  . LEU A 288  ? 0.2419 0.2266 0.2679 0.0184  0.0156  0.0212  286  LEU A CB  
2002  C CG  . LEU A 288  ? 0.2805 0.2674 0.3092 0.0185  0.0160  0.0228  286  LEU A CG  
2003  C CD1 . LEU A 288  ? 0.2630 0.2508 0.2909 0.0170  0.0168  0.0248  286  LEU A CD1 
2004  C CD2 . LEU A 288  ? 0.3880 0.3784 0.4184 0.0210  0.0171  0.0215  286  LEU A CD2 
2005  N N   . PRO A 289  ? 0.2020 0.1807 0.2307 0.0152  0.0113  0.0230  287  PRO A N   
2006  C CA  . PRO A 289  ? 0.2036 0.1816 0.2345 0.0138  0.0097  0.0248  287  PRO A CA  
2007  C C   . PRO A 289  ? 0.2016 0.1788 0.2303 0.0114  0.0090  0.0263  287  PRO A C   
2008  O O   . PRO A 289  ? 0.1938 0.1717 0.2235 0.0101  0.0082  0.0280  287  PRO A O   
2009  C CB  . PRO A 289  ? 0.2307 0.2069 0.2646 0.0147  0.0081  0.0241  287  PRO A CB  
2010  C CG  . PRO A 289  ? 0.2869 0.2640 0.3211 0.0172  0.0091  0.0214  287  PRO A CG  
2011  C CD  . PRO A 289  ? 0.2332 0.2113 0.2633 0.0171  0.0109  0.0207  287  PRO A CD  
2012  N N   . ARG A 290  ? 0.1838 0.1601 0.2097 0.0108  0.0092  0.0255  288  ARG A N   
2013  C CA  . ARG A 290  ? 0.1871 0.1635 0.2108 0.0086  0.0087  0.0265  288  ARG A CA  
2014  C C   . ARG A 290  ? 0.1780 0.1560 0.2007 0.0080  0.0096  0.0268  288  ARG A C   
2015  O O   . ARG A 290  ? 0.1884 0.1674 0.2110 0.0064  0.0088  0.0278  288  ARG A O   
2016  C CB  . ARG A 290  ? 0.1931 0.1683 0.2143 0.0083  0.0087  0.0255  288  ARG A CB  
2017  C CG  . ARG A 290  ? 0.2290 0.2025 0.2520 0.0085  0.0073  0.0254  288  ARG A CG  
2018  C CD  . ARG A 290  ? 0.2717 0.2440 0.2925 0.0085  0.0075  0.0242  288  ARG A CD  
2019  N NE  . ARG A 290  ? 0.3117 0.2822 0.3351 0.0089  0.0060  0.0240  288  ARG A NE  
2020  C CZ  . ARG A 290  ? 0.3221 0.2913 0.3450 0.0097  0.0060  0.0223  288  ARG A CZ  
2021  N NH1 . ARG A 290  ? 0.2820 0.2517 0.3016 0.0100  0.0074  0.0208  288  ARG A NH1 
2022  N NH2 . ARG A 290  ? 0.3634 0.3308 0.3896 0.0101  0.0043  0.0220  288  ARG A NH2 
2023  N N   . VAL A 291  ? 0.1786 0.1571 0.2006 0.0091  0.0112  0.0259  289  VAL A N   
2024  C CA  . VAL A 291  ? 0.1799 0.1599 0.2021 0.0086  0.0119  0.0264  289  VAL A CA  
2025  C C   . VAL A 291  ? 0.1823 0.1635 0.2074 0.0084  0.0114  0.0277  289  VAL A C   
2026  O O   . VAL A 291  ? 0.1802 0.1622 0.2057 0.0071  0.0109  0.0283  289  VAL A O   
2027  C CB  . VAL A 291  ? 0.1906 0.1714 0.2124 0.0099  0.0136  0.0258  289  VAL A CB  
2028  C CG1 . VAL A 291  ? 0.1973 0.1793 0.2200 0.0090  0.0140  0.0266  289  VAL A CG1 
2029  C CG2 . VAL A 291  ? 0.2255 0.2053 0.2446 0.0101  0.0140  0.0245  289  VAL A CG2 
2030  N N   . LYS A 292  ? 0.1861 0.1675 0.2134 0.0097  0.0114  0.0279  290  LYS A N   
2031  C CA  . LYS A 292  ? 0.1708 0.1534 0.2010 0.0096  0.0108  0.0292  290  LYS A CA  
2032  C C   . LYS A 292  ? 0.2024 0.1848 0.2328 0.0078  0.0091  0.0302  290  LYS A C   
2033  O O   . LYS A 292  ? 0.1754 0.1590 0.2069 0.0069  0.0086  0.0311  290  LYS A O   
2034  C CB  . LYS A 292  ? 0.1834 0.1662 0.2161 0.0115  0.0110  0.0289  290  LYS A CB  
2035  C CG  . LYS A 292  ? 0.1937 0.1778 0.2297 0.0114  0.0103  0.0303  290  LYS A CG  
2036  C CD  . LYS A 292  ? 0.2106 0.1953 0.2496 0.0134  0.0104  0.0298  290  LYS A CD  
2037  C CE  . LYS A 292  ? 0.2378 0.2238 0.2801 0.0131  0.0096  0.0313  290  LYS A CE  
2038  N NZ  . LYS A 292  ? 0.2297 0.2169 0.2753 0.0152  0.0099  0.0306  290  LYS A NZ  
2039  N N   . ALA A 293  ? 0.1725 0.1535 0.2018 0.0073  0.0080  0.0303  291  ALA A N   
2040  C CA  . ALA A 293  ? 0.1720 0.1537 0.2013 0.0055  0.0063  0.0317  291  ALA A CA  
2041  C C   . ALA A 293  ? 0.1624 0.1456 0.1896 0.0040  0.0062  0.0314  291  ALA A C   
2042  O O   . ALA A 293  ? 0.1821 0.1671 0.2099 0.0028  0.0052  0.0323  291  ALA A O   
2043  C CB  . ALA A 293  ? 0.1870 0.1673 0.2160 0.0051  0.0051  0.0322  291  ALA A CB  
2044  N N   . LEU A 294  ? 0.1719 0.1546 0.1966 0.0040  0.0073  0.0299  292  LEU A N   
2045  C CA  . LEU A 294  ? 0.1636 0.1477 0.1869 0.0028  0.0072  0.0291  292  LEU A CA  
2046  C C   . LEU A 294  ? 0.1696 0.1548 0.1952 0.0029  0.0075  0.0291  292  LEU A C   
2047  O O   . LEU A 294  ? 0.1629 0.1498 0.1888 0.0018  0.0065  0.0289  292  LEU A O   
2048  C CB  . LEU A 294  ? 0.1787 0.1619 0.1995 0.0030  0.0082  0.0275  292  LEU A CB  
2049  C CG  . LEU A 294  ? 0.1736 0.1561 0.1922 0.0026  0.0078  0.0275  292  LEU A CG  
2050  C CD1 . LEU A 294  ? 0.1983 0.1796 0.2149 0.0031  0.0089  0.0259  292  LEU A CD1 
2051  C CD2 . LEU A 294  ? 0.2069 0.1917 0.2244 0.0008  0.0065  0.0280  292  LEU A CD2 
2052  N N   . ALA A 295  ? 0.1649 0.1493 0.1921 0.0043  0.0086  0.0293  293  ALA A N   
2053  C CA  . ALA A 295  ? 0.1712 0.1568 0.2012 0.0044  0.0089  0.0297  293  ALA A CA  
2054  C C   . ALA A 295  ? 0.1711 0.1580 0.2034 0.0038  0.0077  0.0309  293  ALA A C   
2055  O O   . ALA A 295  ? 0.1751 0.1634 0.2092 0.0030  0.0070  0.0308  293  ALA A O   
2056  C CB  . ALA A 295  ? 0.1793 0.1647 0.2106 0.0060  0.0105  0.0301  293  ALA A CB  
2057  N N   . LEU A 296  ? 0.1565 0.1431 0.1892 0.0042  0.0071  0.0318  294  LEU A N   
2058  C CA  . LEU A 296  ? 0.1648 0.1528 0.1998 0.0036  0.0057  0.0332  294  LEU A CA  
2059  C C   . LEU A 296  ? 0.1782 0.1679 0.2118 0.0018  0.0043  0.0330  294  LEU A C   
2060  O O   . LEU A 296  ? 0.1724 0.1640 0.2079 0.0012  0.0033  0.0334  294  LEU A O   
2061  C CB  . LEU A 296  ? 0.1679 0.1550 0.2037 0.0043  0.0051  0.0343  294  LEU A CB  
2062  C CG  . LEU A 296  ? 0.1800 0.1664 0.2182 0.0063  0.0062  0.0342  294  LEU A CG  
2063  C CD1 . LEU A 296  ? 0.1986 0.1837 0.2379 0.0070  0.0053  0.0347  294  LEU A CD1 
2064  C CD2 . LEU A 296  ? 0.2410 0.2291 0.2825 0.0066  0.0063  0.0351  294  LEU A CD2 
2065  N N   . LEU A 297  ? 0.1698 0.1596 0.2004 0.0011  0.0040  0.0322  295  LEU A N   
2066  C CA  . LEU A 297  ? 0.1792 0.1716 0.2083 -0.0005 0.0027  0.0318  295  LEU A CA  
2067  C C   . LEU A 297  ? 0.1707 0.1640 0.2003 -0.0008 0.0029  0.0298  295  LEU A C   
2068  O O   . LEU A 297  ? 0.1807 0.1767 0.2112 -0.0017 0.0016  0.0293  295  LEU A O   
2069  C CB  . LEU A 297  ? 0.2062 0.1988 0.2320 -0.0012 0.0025  0.0316  295  LEU A CB  
2070  C CG  . LEU A 297  ? 0.2315 0.2281 0.2556 -0.0028 0.0011  0.0316  295  LEU A CG  
2071  C CD1 . LEU A 297  ? 0.2777 0.2765 0.3034 -0.0035 -0.0005 0.0340  295  LEU A CD1 
2072  C CD2 . LEU A 297  ? 0.2918 0.2888 0.3129 -0.0034 0.0012  0.0315  295  LEU A CD2 
2073  N N   . ALA A 298  ? 0.1588 0.1502 0.1883 0.0000  0.0042  0.0286  296  ALA A N   
2074  C CA  . ALA A 298  ? 0.1722 0.1641 0.2034 -0.0002 0.0042  0.0270  296  ALA A CA  
2075  C C   . ALA A 298  ? 0.1826 0.1753 0.2177 -0.0002 0.0037  0.0278  296  ALA A C   
2076  O O   . ALA A 298  ? 0.1885 0.1828 0.2256 -0.0009 0.0026  0.0266  296  ALA A O   
2077  C CB  . ALA A 298  ? 0.1788 0.1685 0.2097 0.0006  0.0057  0.0263  296  ALA A CB  
2078  N N   . LYS A 299  ? 0.1693 0.1611 0.2060 0.0007  0.0044  0.0298  297  LYS A N   
2079  C CA  . LYS A 299  ? 0.1687 0.1616 0.2094 0.0008  0.0040  0.0309  297  LYS A CA  
2080  C C   . LYS A 299  ? 0.1886 0.1838 0.2296 -0.0003 0.0020  0.0309  297  LYS A C   
2081  O O   . LYS A 299  ? 0.1924 0.1891 0.2363 -0.0009 0.0011  0.0304  297  LYS A O   
2082  C CB  . LYS A 299  ? 0.1685 0.1605 0.2104 0.0021  0.0051  0.0327  297  LYS A CB  
2083  C CG  . LYS A 299  ? 0.1781 0.1715 0.2236 0.0021  0.0044  0.0341  297  LYS A CG  
2084  C CD  . LYS A 299  ? 0.2116 0.2047 0.2588 0.0037  0.0056  0.0355  297  LYS A CD  
2085  C CE  . LYS A 299  ? 0.2251 0.2197 0.2755 0.0036  0.0045  0.0369  297  LYS A CE  
2086  N NZ  . LYS A 299  ? 0.2984 0.2932 0.3511 0.0053  0.0057  0.0380  297  LYS A NZ  
2087  N N   . ASN A 300  ? 0.1807 0.1766 0.2192 -0.0008 0.0013  0.0315  298  ASN A N   
2088  C CA  . ASN A 300  ? 0.1661 0.1650 0.2049 -0.0018 -0.0005 0.0320  298  ASN A CA  
2089  C C   . ASN A 300  ? 0.1934 0.1949 0.2316 -0.0029 -0.0017 0.0295  298  ASN A C   
2090  O O   . ASN A 300  ? 0.2214 0.2255 0.2615 -0.0036 -0.0031 0.0291  298  ASN A O   
2091  C CB  . ASN A 300  ? 0.2034 0.2030 0.2401 -0.0022 -0.0012 0.0337  298  ASN A CB  
2092  C CG  . ASN A 300  ? 0.2905 0.2933 0.3283 -0.0032 -0.0031 0.0350  298  ASN A CG  
2093  O OD1 . ASN A 300  ? 0.3494 0.3520 0.3901 -0.0028 -0.0035 0.0366  298  ASN A OD1 
2094  N ND2 . ASN A 300  ? 0.2588 0.2651 0.2942 -0.0044 -0.0043 0.0341  298  ASN A ND2 
2095  N N   . TYR A 301  ? 0.1675 0.1687 0.2033 -0.0030 -0.0012 0.0276  299  TYR A N   
2096  C CA  . TYR A 301  ? 0.1860 0.1897 0.2216 -0.0038 -0.0022 0.0246  299  TYR A CA  
2097  C C   . TYR A 301  ? 0.1904 0.1926 0.2299 -0.0034 -0.0021 0.0230  299  TYR A C   
2098  O O   . TYR A 301  ? 0.2046 0.2088 0.2452 -0.0039 -0.0034 0.0203  299  TYR A O   
2099  C CB  . TYR A 301  ? 0.1872 0.1914 0.2190 -0.0040 -0.0018 0.0230  299  TYR A CB  
2100  C CG  . TYR A 301  ? 0.1811 0.1882 0.2093 -0.0048 -0.0024 0.0243  299  TYR A CG  
2101  C CD1 . TYR A 301  ? 0.2057 0.2179 0.2333 -0.0058 -0.0041 0.0236  299  TYR A CD1 
2102  C CD2 . TYR A 301  ? 0.1860 0.1912 0.2119 -0.0046 -0.0014 0.0261  299  TYR A CD2 
2103  C CE1 . TYR A 301  ? 0.2019 0.2174 0.2263 -0.0067 -0.0047 0.0253  299  TYR A CE1 
2104  C CE2 . TYR A 301  ? 0.1908 0.1987 0.2141 -0.0055 -0.0021 0.0276  299  TYR A CE2 
2105  C CZ  . TYR A 301  ? 0.2155 0.2288 0.2381 -0.0066 -0.0037 0.0275  299  TYR A CZ  
2106  O OH  . TYR A 301  ? 0.2227 0.2394 0.2428 -0.0076 -0.0044 0.0295  299  TYR A OH  
2107  N N   . ASP A 302  ? 0.1710 0.1701 0.2127 -0.0025 -0.0008 0.0247  300  ASP A N   
2108  C CA  . ASP A 302  ? 0.1652 0.1630 0.2111 -0.0022 -0.0005 0.0241  300  ASP A CA  
2109  C C   . ASP A 302  ? 0.1817 0.1787 0.2269 -0.0023 -0.0005 0.0215  300  ASP A C   
2110  O O   . ASP A 302  ? 0.1831 0.1809 0.2315 -0.0027 -0.0017 0.0193  300  ASP A O   
2111  C CB  . ASP A 302  ? 0.1707 0.1701 0.2211 -0.0028 -0.0021 0.0238  300  ASP A CB  
2112  C CG  . ASP A 302  ? 0.2368 0.2344 0.2922 -0.0024 -0.0015 0.0248  300  ASP A CG  
2113  O OD1 . ASP A 302  ? 0.2150 0.2108 0.2702 -0.0016 0.0004  0.0269  300  ASP A OD1 
2114  O OD2 . ASP A 302  ? 0.2538 0.2524 0.3136 -0.0030 -0.0030 0.0236  300  ASP A OD2 
2115  N N   . ILE A 303  ? 0.1659 0.1614 0.2074 -0.0018 0.0009  0.0217  301  ILE A N   
2116  C CA  . ILE A 303  ? 0.1746 0.1692 0.2155 -0.0017 0.0012  0.0196  301  ILE A CA  
2117  C C   . ILE A 303  ? 0.1761 0.1678 0.2173 -0.0008 0.0030  0.0214  301  ILE A C   
2118  O O   . ILE A 303  ? 0.1715 0.1622 0.2119 -0.0001 0.0042  0.0239  301  ILE A O   
2119  C CB  . ILE A 303  ? 0.1714 0.1676 0.2076 -0.0021 0.0010  0.0179  301  ILE A CB  
2120  C CG1 . ILE A 303  ? 0.1740 0.1688 0.2062 -0.0017 0.0024  0.0200  301  ILE A CG1 
2121  C CG2 . ILE A 303  ? 0.1926 0.1928 0.2281 -0.0030 -0.0008 0.0164  301  ILE A CG2 
2122  C CD1 . ILE A 303  ? 0.1940 0.1902 0.2221 -0.0021 0.0024  0.0187  301  ILE A CD1 
2123  N N   . GLY A 304  ? 0.1734 0.1639 0.2157 -0.0006 0.0032  0.0201  302  GLY A N   
2124  C CA  . GLY A 304  ? 0.1799 0.1682 0.2220 0.0002  0.0049  0.0217  302  GLY A CA  
2125  C C   . GLY A 304  ? 0.1790 0.1667 0.2159 0.0007  0.0060  0.0218  302  GLY A C   
2126  O O   . GLY A 304  ? 0.1740 0.1626 0.2078 0.0002  0.0055  0.0200  302  GLY A O   
2127  N N   . LEU A 305  ? 0.1600 0.1464 0.1960 0.0016  0.0077  0.0239  303  LEU A N   
2128  C CA  . LEU A 305  ? 0.1639 0.1493 0.1957 0.0022  0.0088  0.0239  303  LEU A CA  
2129  C C   . LEU A 305  ? 0.1743 0.1587 0.2068 0.0031  0.0101  0.0249  303  LEU A C   
2130  O O   . LEU A 305  ? 0.1755 0.1602 0.2097 0.0038  0.0111  0.0270  303  LEU A O   
2131  C CB  . LEU A 305  ? 0.1783 0.1638 0.2082 0.0026  0.0091  0.0252  303  LEU A CB  
2132  C CG  . LEU A 305  ? 0.2334 0.2178 0.2595 0.0031  0.0099  0.0250  303  LEU A CG  
2133  C CD1 . LEU A 305  ? 0.2680 0.2528 0.2928 0.0029  0.0092  0.0256  303  LEU A CD1 
2134  C CD2 . LEU A 305  ? 0.3071 0.2905 0.3330 0.0045  0.0115  0.0260  303  LEU A CD2 
2135  N N   . ASN A 306  ? 0.1693 0.1528 0.2005 0.0031  0.0102  0.0236  304  ASN A N   
2136  C CA  . ASN A 306  ? 0.1686 0.1514 0.2008 0.0038  0.0112  0.0247  304  ASN A CA  
2137  C C   . ASN A 306  ? 0.1636 0.1457 0.1916 0.0046  0.0125  0.0246  304  ASN A C   
2138  O O   . ASN A 306  ? 0.1866 0.1681 0.2114 0.0043  0.0121  0.0229  304  ASN A O   
2139  C CB  . ASN A 306  ? 0.1670 0.1494 0.2015 0.0032  0.0103  0.0231  304  ASN A CB  
2140  C CG  . ASN A 306  ? 0.1939 0.1756 0.2290 0.0038  0.0112  0.0243  304  ASN A CG  
2141  O OD1 . ASN A 306  ? 0.2317 0.2126 0.2639 0.0041  0.0116  0.0232  304  ASN A OD1 
2142  N ND2 . ASN A 306  ? 0.1744 0.1568 0.2134 0.0040  0.0115  0.0268  304  ASN A ND2 
2143  N N   . ILE A 307  ? 0.1681 0.1505 0.1961 0.0057  0.0138  0.0263  305  ILE A N   
2144  C CA  . ILE A 307  ? 0.1879 0.1699 0.2125 0.0066  0.0149  0.0261  305  ILE A CA  
2145  C C   . ILE A 307  ? 0.1745 0.1562 0.1995 0.0067  0.0151  0.0260  305  ILE A C   
2146  O O   . ILE A 307  ? 0.1769 0.1596 0.2046 0.0069  0.0155  0.0279  305  ILE A O   
2147  C CB  . ILE A 307  ? 0.2114 0.1948 0.2356 0.0080  0.0162  0.0276  305  ILE A CB  
2148  C CG1 . ILE A 307  ? 0.2340 0.2174 0.2582 0.0080  0.0158  0.0275  305  ILE A CG1 
2149  C CG2 . ILE A 307  ? 0.2237 0.2070 0.2446 0.0091  0.0171  0.0269  305  ILE A CG2 
2150  C CD1 . ILE A 307  ? 0.2616 0.2469 0.2866 0.0094  0.0169  0.0287  305  ILE A CD1 
2151  N N   . ASP A 308  ? 0.1790 0.1595 0.2015 0.0063  0.0146  0.0240  306  ASP A N   
2152  C CA  . ASP A 308  ? 0.1732 0.1533 0.1961 0.0064  0.0147  0.0237  306  ASP A CA  
2153  C C   . ASP A 308  ? 0.1747 0.1555 0.1959 0.0076  0.0161  0.0252  306  ASP A C   
2154  O O   . ASP A 308  ? 0.1936 0.1748 0.2123 0.0085  0.0169  0.0252  306  ASP A O   
2155  C CB  . ASP A 308  ? 0.2004 0.1794 0.2206 0.0059  0.0141  0.0212  306  ASP A CB  
2156  C CG  . ASP A 308  ? 0.2398 0.2189 0.2616 0.0048  0.0126  0.0193  306  ASP A CG  
2157  O OD1 . ASP A 308  ? 0.2315 0.2111 0.2571 0.0044  0.0119  0.0198  306  ASP A OD1 
2158  O OD2 . ASP A 308  ? 0.2417 0.2209 0.2612 0.0043  0.0122  0.0172  306  ASP A OD2 
2159  N N   . ALA A 309  ? 0.1632 0.1445 0.1863 0.0078  0.0163  0.0264  307  ALA A N   
2160  C CA  . ALA A 309  ? 0.1690 0.1519 0.1906 0.0090  0.0175  0.0279  307  ALA A CA  
2161  C C   . ALA A 309  ? 0.1810 0.1627 0.1993 0.0092  0.0175  0.0261  307  ALA A C   
2162  O O   . ALA A 309  ? 0.1906 0.1708 0.2096 0.0085  0.0166  0.0247  307  ALA A O   
2163  C CB  . ALA A 309  ? 0.1833 0.1679 0.2088 0.0090  0.0177  0.0309  307  ALA A CB  
2164  N N   . GLU A 310  ? 0.1763 0.1589 0.1913 0.0104  0.0185  0.0260  308  GLU A N   
2165  C CA  . GLU A 310  ? 0.1784 0.1600 0.1903 0.0106  0.0185  0.0242  308  GLU A CA  
2166  C C   . GLU A 310  ? 0.1710 0.1548 0.1821 0.0117  0.0193  0.0255  308  GLU A C   
2167  O O   . GLU A 310  ? 0.1876 0.1729 0.2015 0.0116  0.0194  0.0279  308  GLU A O   
2168  C CB  . GLU A 310  ? 0.1887 0.1692 0.1976 0.0108  0.0184  0.0222  308  GLU A CB  
2169  C CG  . GLU A 310  ? 0.2098 0.1888 0.2195 0.0096  0.0174  0.0213  308  GLU A CG  
2170  C CD  . GLU A 310  ? 0.2084 0.1864 0.2158 0.0095  0.0171  0.0198  308  GLU A CD  
2171  O OE1 . GLU A 310  ? 0.2346 0.2117 0.2401 0.0092  0.0167  0.0184  308  GLU A OE1 
2172  O OE2 . GLU A 310  ? 0.2147 0.1930 0.2225 0.0098  0.0171  0.0202  308  GLU A OE2 
2173  N N   . GLU A 311  ? 0.1874 0.1715 0.1950 0.0127  0.0198  0.0242  309  GLU A N   
2174  C CA  . GLU A 311  ? 0.1913 0.1779 0.1979 0.0138  0.0205  0.0252  309  GLU A CA  
2175  C C   . GLU A 311  ? 0.1774 0.1680 0.1850 0.0148  0.0216  0.0277  309  GLU A C   
2176  O O   . GLU A 311  ? 0.1772 0.1687 0.1855 0.0150  0.0220  0.0278  309  GLU A O   
2177  C CB  . GLU A 311  ? 0.2131 0.1994 0.2159 0.0147  0.0206  0.0228  309  GLU A CB  
2178  C CG  . GLU A 311  ? 0.2252 0.2083 0.2269 0.0137  0.0197  0.0207  309  GLU A CG  
2179  C CD  . GLU A 311  ? 0.2381 0.2188 0.2394 0.0129  0.0190  0.0190  309  GLU A CD  
2180  O OE1 . GLU A 311  ? 0.2119 0.1927 0.2142 0.0129  0.0191  0.0195  309  GLU A OE1 
2181  O OE2 . GLU A 311  ? 0.3176 0.2964 0.3174 0.0123  0.0184  0.0172  309  GLU A OE2 
2182  N N   . ALA A 312  ? 0.1813 0.1750 0.1892 0.0153  0.0221  0.0298  310  ALA A N   
2183  C CA  . ALA A 312  ? 0.1753 0.1739 0.1844 0.0162  0.0232  0.0327  310  ALA A CA  
2184  C C   . ALA A 312  ? 0.1703 0.1716 0.1768 0.0178  0.0242  0.0310  310  ALA A C   
2185  O O   . ALA A 312  ? 0.1841 0.1888 0.1920 0.0183  0.0250  0.0326  310  ALA A O   
2186  C CB  . ALA A 312  ? 0.1776 0.1796 0.1870 0.0165  0.0235  0.0353  310  ALA A CB  
2187  N N   . ASP A 313  ? 0.1885 0.1884 0.1916 0.0186  0.0240  0.0277  311  ASP A N   
2188  C CA  . ASP A 313  ? 0.1933 0.1957 0.1945 0.0204  0.0246  0.0257  311  ASP A CA  
2189  C C   . ASP A 313  ? 0.1814 0.1813 0.1838 0.0201  0.0242  0.0243  311  ASP A C   
2190  O O   . ASP A 313  ? 0.1990 0.2004 0.2006 0.0216  0.0245  0.0223  311  ASP A O   
2191  C CB  . ASP A 313  ? 0.2065 0.2090 0.2044 0.0216  0.0244  0.0226  311  ASP A CB  
2192  C CG  . ASP A 313  ? 0.2478 0.2446 0.2448 0.0205  0.0231  0.0201  311  ASP A CG  
2193  O OD1 . ASP A 313  ? 0.2319 0.2250 0.2306 0.0190  0.0224  0.0205  311  ASP A OD1 
2194  O OD2 . ASP A 313  ? 0.3112 0.3077 0.3061 0.0213  0.0227  0.0177  311  ASP A OD2 
2195  N N   . ARG A 314  ? 0.1713 0.1677 0.1759 0.0184  0.0235  0.0252  312  ARG A N   
2196  C CA  . ARG A 314  ? 0.1812 0.1756 0.1872 0.0180  0.0231  0.0245  312  ARG A CA  
2197  C C   . ARG A 314  ? 0.1826 0.1789 0.1919 0.0175  0.0235  0.0273  312  ARG A C   
2198  O O   . ARG A 314  ? 0.1789 0.1745 0.1896 0.0174  0.0233  0.0270  312  ARG A O   
2199  C CB  . ARG A 314  ? 0.1973 0.1867 0.2031 0.0164  0.0218  0.0230  312  ARG A CB  
2200  C CG  . ARG A 314  ? 0.2194 0.2069 0.2226 0.0169  0.0212  0.0202  312  ARG A CG  
2201  C CD  . ARG A 314  ? 0.2289 0.2127 0.2315 0.0153  0.0201  0.0193  312  ARG A CD  
2202  N NE  . ARG A 314  ? 0.2306 0.2125 0.2318 0.0155  0.0193  0.0170  312  ARG A NE  
2203  C CZ  . ARG A 314  ? 0.2043 0.1835 0.2047 0.0143  0.0184  0.0161  312  ARG A CZ  
2204  N NH1 . ARG A 314  ? 0.2228 0.2012 0.2232 0.0130  0.0182  0.0167  312  ARG A NH1 
2205  N NH2 . ARG A 314  ? 0.2355 0.2132 0.2354 0.0144  0.0176  0.0145  312  ARG A NH2 
2206  N N   . LEU A 315  ? 0.1750 0.1739 0.1859 0.0171  0.0241  0.0302  313  LEU A N   
2207  C CA  . LEU A 315  ? 0.1752 0.1757 0.1900 0.0164  0.0243  0.0332  313  LEU A CA  
2208  C C   . LEU A 315  ? 0.1966 0.2007 0.2119 0.0177  0.0253  0.0335  313  LEU A C   
2209  O O   . LEU A 315  ? 0.1858 0.1887 0.2032 0.0171  0.0249  0.0336  313  LEU A O   
2210  C CB  . LEU A 315  ? 0.1860 0.1895 0.2027 0.0161  0.0247  0.0367  313  LEU A CB  
2211  C CG  . LEU A 315  ? 0.1798 0.1834 0.2016 0.0146  0.0242  0.0400  313  LEU A CG  
2212  C CD1 . LEU A 315  ? 0.1927 0.1991 0.2167 0.0143  0.0243  0.0436  313  LEU A CD1 
2213  C CD2 . LEU A 315  ? 0.2324 0.2389 0.2564 0.0149  0.0249  0.0416  313  LEU A CD2 
2214  N N   . GLU A 316  ? 0.1816 0.1906 0.1951 0.0195  0.0265  0.0335  314  GLU A N   
2215  C CA  . GLU A 316  ? 0.1771 0.1907 0.1916 0.0208  0.0275  0.0338  314  GLU A CA  
2216  C C   . GLU A 316  ? 0.1930 0.2037 0.2068 0.0215  0.0269  0.0304  314  GLU A C   
2217  O O   . GLU A 316  ? 0.1901 0.2019 0.2061 0.0217  0.0271  0.0309  314  GLU A O   
2218  C CB  . GLU A 316  ? 0.1953 0.2158 0.2080 0.0227  0.0290  0.0345  314  GLU A CB  
2219  C CG  . GLU A 316  ? 0.2017 0.2257 0.2164 0.0217  0.0295  0.0391  314  GLU A CG  
2220  C CD  . GLU A 316  ? 0.1926 0.2246 0.2057 0.0234  0.0310  0.0405  314  GLU A CD  
2221  O OE1 . GLU A 316  ? 0.2110 0.2479 0.2233 0.0253  0.0320  0.0391  314  GLU A OE1 
2222  O OE2 . GLU A 316  ? 0.2060 0.2397 0.2187 0.0229  0.0310  0.0428  314  GLU A OE2 
2223  N N   . LEU A 317  ? 0.1922 0.1992 0.2035 0.0217  0.0261  0.0272  315  LEU A N   
2224  C CA  . LEU A 317  ? 0.1925 0.1964 0.2039 0.0220  0.0251  0.0244  315  LEU A CA  
2225  C C   . LEU A 317  ? 0.2026 0.2029 0.2165 0.0202  0.0242  0.0257  315  LEU A C   
2226  O O   . LEU A 317  ? 0.2019 0.2022 0.2175 0.0206  0.0240  0.0252  315  LEU A O   
2227  C CB  . LEU A 317  ? 0.2261 0.2261 0.2349 0.0220  0.0241  0.0216  315  LEU A CB  
2228  C CG  . LEU A 317  ? 0.2295 0.2260 0.2389 0.0221  0.0228  0.0191  315  LEU A CG  
2229  C CD1 . LEU A 317  ? 0.2689 0.2687 0.2795 0.0243  0.0233  0.0175  315  LEU A CD1 
2230  C CD2 . LEU A 317  ? 0.2663 0.2596 0.2735 0.0219  0.0218  0.0168  315  LEU A CD2 
2231  N N   . SER A 318  ? 0.1731 0.1709 0.1875 0.0183  0.0237  0.0272  316  SER A N   
2232  C CA  . SER A 318  ? 0.1823 0.1772 0.1990 0.0167  0.0227  0.0280  316  SER A CA  
2233  C C   . SER A 318  ? 0.1974 0.1953 0.2173 0.0168  0.0233  0.0303  316  SER A C   
2234  O O   . SER A 318  ? 0.1849 0.1813 0.2068 0.0160  0.0226  0.0304  316  SER A O   
2235  C CB  . SER A 318  ? 0.1688 0.1611 0.1858 0.0149  0.0219  0.0288  316  SER A CB  
2236  O OG  . SER A 318  ? 0.1806 0.1753 0.1997 0.0146  0.0225  0.0315  316  SER A OG  
2237  N N   . LEU A 319  ? 0.1833 0.1859 0.2041 0.0176  0.0246  0.0324  317  LEU A N   
2238  C CA  . LEU A 319  ? 0.1723 0.1785 0.1964 0.0178  0.0253  0.0348  317  LEU A CA  
2239  C C   . LEU A 319  ? 0.1966 0.2042 0.2209 0.0192  0.0256  0.0331  317  LEU A C   
2240  O O   . LEU A 319  ? 0.1882 0.1968 0.2155 0.0189  0.0256  0.0344  317  LEU A O   
2241  C CB  . LEU A 319  ? 0.1807 0.1926 0.2055 0.0185  0.0268  0.0377  317  LEU A CB  
2242  C CG  . LEU A 319  ? 0.1926 0.2038 0.2187 0.0170  0.0264  0.0402  317  LEU A CG  
2243  C CD1 . LEU A 319  ? 0.2047 0.2223 0.2314 0.0177  0.0278  0.0434  317  LEU A CD1 
2244  C CD2 . LEU A 319  ? 0.1910 0.1992 0.2211 0.0150  0.0252  0.0419  317  LEU A CD2 
2245  N N   . ASP A 320  ? 0.1932 0.2009 0.2148 0.0208  0.0257  0.0301  318  ASP A N   
2246  C CA  . ASP A 320  ? 0.2066 0.2151 0.2291 0.0223  0.0256  0.0282  318  ASP A CA  
2247  C C   . ASP A 320  ? 0.2032 0.2067 0.2271 0.0210  0.0240  0.0275  318  ASP A C   
2248  O O   . ASP A 320  ? 0.2217 0.2261 0.2481 0.0215  0.0239  0.0275  318  ASP A O   
2249  C CB  . ASP A 320  ? 0.2107 0.2204 0.2308 0.0244  0.0258  0.0248  318  ASP A CB  
2250  C CG  . ASP A 320  ? 0.2441 0.2607 0.2634 0.0262  0.0276  0.0253  318  ASP A CG  
2251  O OD1 . ASP A 320  ? 0.2649 0.2864 0.2863 0.0270  0.0286  0.0267  318  ASP A OD1 
2252  O OD2 . ASP A 320  ? 0.2857 0.3032 0.3022 0.0267  0.0279  0.0245  318  ASP A OD2 
2253  N N   . LEU A 321  ? 0.1825 0.1813 0.2050 0.0193  0.0228  0.0271  319  LEU A N   
2254  C CA  . LEU A 321  ? 0.1996 0.1946 0.2234 0.0179  0.0213  0.0270  319  LEU A CA  
2255  C C   . LEU A 321  ? 0.1867 0.1824 0.2134 0.0165  0.0212  0.0295  319  LEU A C   
2256  O O   . LEU A 321  ? 0.1958 0.1910 0.2246 0.0162  0.0205  0.0298  319  LEU A O   
2257  C CB  . LEU A 321  ? 0.1918 0.1826 0.2132 0.0166  0.0201  0.0258  319  LEU A CB  
2258  C CG  . LEU A 321  ? 0.2505 0.2398 0.2701 0.0176  0.0196  0.0233  319  LEU A CG  
2259  C CD1 . LEU A 321  ? 0.2924 0.2833 0.3095 0.0187  0.0206  0.0223  319  LEU A CD1 
2260  C CD2 . LEU A 321  ? 0.2834 0.2686 0.3020 0.0159  0.0180  0.0228  319  LEU A CD2 
2261  N N   . LEU A 322  ? 0.1978 0.1946 0.2249 0.0157  0.0218  0.0314  320  LEU A N   
2262  C CA  . LEU A 322  ? 0.1945 0.1919 0.2252 0.0144  0.0215  0.0337  320  LEU A CA  
2263  C C   . LEU A 322  ? 0.1941 0.1953 0.2276 0.0154  0.0223  0.0350  320  LEU A C   
2264  O O   . LEU A 322  ? 0.1968 0.1974 0.2329 0.0146  0.0215  0.0358  320  LEU A O   
2265  C CB  . LEU A 322  ? 0.1899 0.1882 0.2215 0.0136  0.0218  0.0356  320  LEU A CB  
2266  C CG  . LEU A 322  ? 0.2068 0.2054 0.2428 0.0121  0.0212  0.0380  320  LEU A CG  
2267  C CD1 . LEU A 322  ? 0.2169 0.2116 0.2534 0.0105  0.0194  0.0366  320  LEU A CD1 
2268  C CD2 . LEU A 322  ? 0.1946 0.1951 0.2323 0.0117  0.0217  0.0404  320  LEU A CD2 
2269  N N   . GLU A 323  ? 0.1728 0.1780 0.2055 0.0173  0.0238  0.0350  321  GLU A N   
2270  C CA  . GLU A 323  ? 0.1980 0.2078 0.2334 0.0185  0.0248  0.0361  321  GLU A CA  
2271  C C   . GLU A 323  ? 0.1998 0.2077 0.2361 0.0190  0.0238  0.0343  321  GLU A C   
2272  O O   . GLU A 323  ? 0.1980 0.2069 0.2375 0.0186  0.0236  0.0356  321  GLU A O   
2273  C CB  . GLU A 323  ? 0.2012 0.2163 0.2350 0.0207  0.0265  0.0357  321  GLU A CB  
2274  C CG  . GLU A 323  ? 0.2677 0.2880 0.3037 0.0225  0.0276  0.0358  321  GLU A CG  
2275  C CD  . GLU A 323  ? 0.3005 0.3271 0.3388 0.0225  0.0292  0.0394  321  GLU A CD  
2276  O OE1 . GLU A 323  ? 0.2989 0.3259 0.3372 0.0212  0.0294  0.0419  321  GLU A OE1 
2277  O OE2 . GLU A 323  ? 0.3407 0.3722 0.3814 0.0237  0.0301  0.0400  321  GLU A OE2 
2278  N N   . VAL A 324  ? 0.1905 0.1957 0.2244 0.0198  0.0231  0.0314  322  VAL A N   
2279  C CA  . VAL A 324  ? 0.2021 0.2055 0.2375 0.0202  0.0220  0.0299  322  VAL A CA  
2280  C C   . VAL A 324  ? 0.1822 0.1823 0.2191 0.0181  0.0204  0.0312  322  VAL A C   
2281  O O   . VAL A 324  ? 0.1986 0.1993 0.2384 0.0181  0.0199  0.0317  322  VAL A O   
2282  C CB  . VAL A 324  ? 0.2301 0.2311 0.2634 0.0213  0.0212  0.0269  322  VAL A CB  
2283  C CG1 . VAL A 324  ? 0.2403 0.2390 0.2758 0.0215  0.0197  0.0259  322  VAL A CG1 
2284  C CG2 . VAL A 324  ? 0.2404 0.2453 0.2725 0.0237  0.0226  0.0251  322  VAL A CG2 
2285  N N   . LEU A 325  ? 0.1752 0.1723 0.2104 0.0163  0.0197  0.0314  323  LEU A N   
2286  C CA  . LEU A 325  ? 0.1718 0.1664 0.2082 0.0143  0.0181  0.0322  323  LEU A CA  
2287  C C   . LEU A 325  ? 0.1743 0.1711 0.2143 0.0137  0.0183  0.0344  323  LEU A C   
2288  O O   . LEU A 325  ? 0.1846 0.1809 0.2267 0.0130  0.0173  0.0349  323  LEU A O   
2289  C CB  . LEU A 325  ? 0.1823 0.1741 0.2163 0.0128  0.0174  0.0317  323  LEU A CB  
2290  C CG  . LEU A 325  ? 0.1939 0.1831 0.2246 0.0130  0.0169  0.0297  323  LEU A CG  
2291  C CD1 . LEU A 325  ? 0.2188 0.2064 0.2470 0.0119  0.0168  0.0292  323  LEU A CD1 
2292  C CD2 . LEU A 325  ? 0.2256 0.2128 0.2567 0.0124  0.0153  0.0293  323  LEU A CD2 
2293  N N   . CYS A 326  ? 0.1849 0.1843 0.2259 0.0137  0.0195  0.0360  324  CYS A N   
2294  C CA  . CYS A 326  ? 0.1675 0.1690 0.2126 0.0129  0.0196  0.0384  324  CYS A CA  
2295  C C   . CYS A 326  ? 0.2146 0.2194 0.2623 0.0142  0.0203  0.0391  324  CYS A C   
2296  O O   . CYS A 326  ? 0.1991 0.2050 0.2505 0.0134  0.0198  0.0408  324  CYS A O   
2297  C CB  . CYS A 326  ? 0.1781 0.1818 0.2242 0.0126  0.0206  0.0405  324  CYS A CB  
2298  S SG  . CYS A 326  ? 0.2150 0.2148 0.2598 0.0108  0.0194  0.0398  324  CYS A SG  
2299  N N   . LEU A 327  ? 0.1791 0.1857 0.2254 0.0162  0.0212  0.0377  325  LEU A N   
2300  C CA  . LEU A 327  ? 0.1775 0.1875 0.2264 0.0177  0.0218  0.0379  325  LEU A CA  
2301  C C   . LEU A 327  ? 0.1772 0.1844 0.2266 0.0179  0.0203  0.0362  325  LEU A C   
2302  O O   . LEU A 327  ? 0.1923 0.2019 0.2444 0.0192  0.0205  0.0361  325  LEU A O   
2303  C CB  . LEU A 327  ? 0.1976 0.2121 0.2453 0.0201  0.0237  0.0370  325  LEU A CB  
2304  C CG  . LEU A 327  ? 0.2323 0.2511 0.2801 0.0200  0.0253  0.0394  325  LEU A CG  
2305  C CD1 . LEU A 327  ? 0.2674 0.2912 0.3134 0.0226  0.0271  0.0380  325  LEU A CD1 
2306  C CD2 . LEU A 327  ? 0.2643 0.2862 0.3165 0.0190  0.0257  0.0428  325  LEU A CD2 
2307  N N   . ASP A 328  ? 0.1875 0.1901 0.2348 0.0168  0.0187  0.0351  326  ASP A N   
2308  C CA  . ASP A 328  ? 0.1768 0.1769 0.2247 0.0168  0.0171  0.0339  326  ASP A CA  
2309  C C   . ASP A 328  ? 0.1922 0.1919 0.2428 0.0153  0.0158  0.0356  326  ASP A C   
2310  O O   . ASP A 328  ? 0.1800 0.1781 0.2301 0.0134  0.0150  0.0363  326  ASP A O   
2311  C CB  . ASP A 328  ? 0.1912 0.1873 0.2356 0.0160  0.0160  0.0325  326  ASP A CB  
2312  C CG  . ASP A 328  ? 0.2417 0.2356 0.2870 0.0162  0.0143  0.0316  326  ASP A CG  
2313  O OD1 . ASP A 328  ? 0.2350 0.2291 0.2831 0.0159  0.0133  0.0326  326  ASP A OD1 
2314  O OD2 . ASP A 328  ? 0.2652 0.2570 0.3086 0.0167  0.0139  0.0300  326  ASP A OD2 
2315  N N   . GLY A 329  ? 0.1751 0.1766 0.2291 0.0163  0.0156  0.0359  327  GLY A N   
2316  C CA  . GLY A 329  ? 0.1988 0.2005 0.2557 0.0150  0.0144  0.0375  327  GLY A CA  
2317  C C   . GLY A 329  ? 0.2131 0.2114 0.2688 0.0132  0.0123  0.0374  327  GLY A C   
2318  O O   . GLY A 329  ? 0.1953 0.1937 0.2526 0.0116  0.0112  0.0386  327  GLY A O   
2319  N N   . ASP A 330  ? 0.1869 0.1825 0.2400 0.0133  0.0115  0.0361  328  ASP A N   
2320  C CA  . ASP A 330  ? 0.1967 0.1901 0.2486 0.0115  0.0095  0.0363  328  ASP A CA  
2321  C C   . ASP A 330  ? 0.1715 0.1644 0.2213 0.0096  0.0094  0.0365  328  ASP A C   
2322  O O   . ASP A 330  ? 0.1876 0.1799 0.2369 0.0080  0.0078  0.0368  328  ASP A O   
2323  C CB  . ASP A 330  ? 0.2005 0.1913 0.2502 0.0118  0.0088  0.0352  328  ASP A CB  
2324  C CG  . ASP A 330  ? 0.2784 0.2692 0.3310 0.0134  0.0082  0.0349  328  ASP A CG  
2325  O OD1 . ASP A 330  ? 0.3058 0.2981 0.3619 0.0139  0.0078  0.0358  328  ASP A OD1 
2326  O OD2 . ASP A 330  ? 0.2422 0.2312 0.2939 0.0143  0.0080  0.0337  328  ASP A OD2 
2327  N N   . LEU A 331  ? 0.1596 0.1529 0.2083 0.0098  0.0109  0.0362  329  LEU A N   
2328  C CA  . LEU A 331  ? 0.1924 0.1853 0.2399 0.0083  0.0106  0.0360  329  LEU A CA  
2329  C C   . LEU A 331  ? 0.1859 0.1807 0.2370 0.0076  0.0107  0.0373  329  LEU A C   
2330  O O   . LEU A 331  ? 0.1875 0.1820 0.2386 0.0065  0.0104  0.0371  329  LEU A O   
2331  C CB  . LEU A 331  ? 0.1705 0.1625 0.2151 0.0087  0.0119  0.0351  329  LEU A CB  
2332  C CG  . LEU A 331  ? 0.1934 0.1831 0.2344 0.0088  0.0115  0.0337  329  LEU A CG  
2333  C CD1 . LEU A 331  ? 0.1974 0.1868 0.2360 0.0096  0.0129  0.0328  329  LEU A CD1 
2334  C CD2 . LEU A 331  ? 0.2013 0.1899 0.2407 0.0069  0.0099  0.0333  329  LEU A CD2 
2335  N N   . SER A 332  ? 0.1866 0.1834 0.2410 0.0084  0.0110  0.0385  330  SER A N   
2336  C CA  . SER A 332  ? 0.2204 0.2192 0.2787 0.0078  0.0112  0.0400  330  SER A CA  
2337  C C   . SER A 332  ? 0.1923 0.1906 0.2519 0.0060  0.0091  0.0398  330  SER A C   
2338  O O   . SER A 332  ? 0.2213 0.2186 0.2794 0.0054  0.0076  0.0390  330  SER A O   
2339  C CB  . SER A 332  ? 0.2180 0.2196 0.2797 0.0091  0.0120  0.0414  330  SER A CB  
2340  O OG  . SER A 332  ? 0.2507 0.2520 0.3135 0.0090  0.0105  0.0413  330  SER A OG  
2341  N N   . GLY A 333  ? 0.1807 0.1798 0.2434 0.0051  0.0089  0.0405  331  GLY A N   
2342  C CA  . GLY A 333  ? 0.1902 0.1891 0.2546 0.0034  0.0069  0.0399  331  GLY A CA  
2343  C C   . GLY A 333  ? 0.1883 0.1855 0.2505 0.0024  0.0061  0.0379  331  GLY A C   
2344  O O   . GLY A 333  ? 0.2328 0.2302 0.2968 0.0012  0.0044  0.0368  331  GLY A O   
2345  N N   . TRP A 334  ? 0.1800 0.1759 0.2386 0.0030  0.0073  0.0373  332  TRP A N   
2346  C CA  . TRP A 334  ? 0.1866 0.1810 0.2429 0.0023  0.0067  0.0353  332  TRP A CA  
2347  C C   . TRP A 334  ? 0.1619 0.1558 0.2189 0.0027  0.0080  0.0359  332  TRP A C   
2348  O O   . TRP A 334  ? 0.1832 0.1774 0.2390 0.0039  0.0098  0.0371  332  TRP A O   
2349  C CB  . TRP A 334  ? 0.1949 0.1880 0.2460 0.0026  0.0068  0.0341  332  TRP A CB  
2350  C CG  . TRP A 334  ? 0.1759 0.1677 0.2238 0.0021  0.0066  0.0322  332  TRP A CG  
2351  C CD1 . TRP A 334  ? 0.1589 0.1509 0.2066 0.0010  0.0052  0.0302  332  TRP A CD1 
2352  C CD2 . TRP A 334  ? 0.1696 0.1601 0.2141 0.0029  0.0080  0.0319  332  TRP A CD2 
2353  N NE1 . TRP A 334  ? 0.1732 0.1641 0.2176 0.0010  0.0056  0.0288  332  TRP A NE1 
2354  C CE2 . TRP A 334  ? 0.1690 0.1587 0.2113 0.0021  0.0073  0.0299  332  TRP A CE2 
2355  C CE3 . TRP A 334  ? 0.1927 0.1827 0.2358 0.0043  0.0096  0.0328  332  TRP A CE3 
2356  C CZ2 . TRP A 334  ? 0.1842 0.1725 0.2231 0.0026  0.0082  0.0291  332  TRP A CZ2 
2357  C CZ3 . TRP A 334  ? 0.2124 0.2010 0.2520 0.0048  0.0104  0.0318  332  TRP A CZ3 
2358  C CH2 . TRP A 334  ? 0.1943 0.1821 0.2320 0.0039  0.0098  0.0301  332  TRP A CH2 
2359  N N   . ASN A 335  ? 0.1570 0.1504 0.2164 0.0017  0.0070  0.0351  333  ASN A N   
2360  C CA  . ASN A 335  ? 0.1646 0.1576 0.2256 0.0019  0.0079  0.0360  333  ASN A CA  
2361  C C   . ASN A 335  ? 0.1752 0.1664 0.2328 0.0017  0.0077  0.0338  333  ASN A C   
2362  O O   . ASN A 335  ? 0.1802 0.1708 0.2398 0.0015  0.0078  0.0341  333  ASN A O   
2363  C CB  . ASN A 335  ? 0.1931 0.1869 0.2606 0.0009  0.0068  0.0371  333  ASN A CB  
2364  C CG  . ASN A 335  ? 0.2119 0.2080 0.2833 0.0012  0.0076  0.0403  333  ASN A CG  
2365  O OD1 . ASN A 335  ? 0.1859 0.1833 0.2554 0.0024  0.0095  0.0419  333  ASN A OD1 
2366  N ND2 . ASN A 335  ? 0.2468 0.2436 0.3241 0.0002  0.0062  0.0410  333  ASN A ND2 
2367  N N   . GLY A 336  ? 0.1721 0.1625 0.2251 0.0017  0.0074  0.0318  334  GLY A N   
2368  C CA  . GLY A 336  ? 0.1590 0.1482 0.2090 0.0015  0.0071  0.0295  334  GLY A CA  
2369  C C   . GLY A 336  ? 0.1706 0.1586 0.2169 0.0024  0.0088  0.0300  334  GLY A C   
2370  O O   . GLY A 336  ? 0.1753 0.1623 0.2194 0.0023  0.0086  0.0282  334  GLY A O   
2371  N N   . MET A 337  ? 0.1651 0.1537 0.2109 0.0035  0.0104  0.0320  335  MET A N   
2372  C CA  A MET A 337  ? 0.1769 0.1649 0.2194 0.0046  0.0119  0.0321  335  MET A CA  
2373  C CA  B MET A 337  ? 0.1770 0.1650 0.2195 0.0045  0.0119  0.0321  335  MET A CA  
2374  C C   . MET A 337  ? 0.1691 0.1570 0.2136 0.0044  0.0122  0.0327  335  MET A C   
2375  O O   . MET A 337  ? 0.1758 0.1649 0.2246 0.0042  0.0123  0.0347  335  MET A O   
2376  C CB  A MET A 337  ? 0.1914 0.1809 0.2336 0.0059  0.0135  0.0338  335  MET A CB  
2377  C CB  B MET A 337  ? 0.1913 0.1807 0.2334 0.0059  0.0134  0.0337  335  MET A CB  
2378  C CG  A MET A 337  ? 0.2120 0.2012 0.2505 0.0072  0.0148  0.0334  335  MET A CG  
2379  C CG  B MET A 337  ? 0.2216 0.2112 0.2609 0.0071  0.0150  0.0338  335  MET A CG  
2380  S SD  A MET A 337  ? 0.3048 0.2918 0.3386 0.0070  0.0141  0.0310  335  MET A SD  
2381  S SD  B MET A 337  ? 0.2367 0.2263 0.2728 0.0086  0.0158  0.0330  335  MET A SD  
2382  C CE  A MET A 337  ? 0.2702 0.2579 0.3044 0.0079  0.0141  0.0315  335  MET A CE  
2383  C CE  B MET A 337  ? 0.1924 0.1794 0.2258 0.0074  0.0140  0.0310  335  MET A CE  
2384  N N   . GLY A 338  ? 0.1737 0.1602 0.2152 0.0044  0.0123  0.0311  336  GLY A N   
2385  C CA  . GLY A 338  ? 0.1942 0.1802 0.2374 0.0043  0.0123  0.0315  336  GLY A CA  
2386  C C   . GLY A 338  ? 0.1828 0.1688 0.2225 0.0054  0.0138  0.0319  336  GLY A C   
2387  O O   . GLY A 338  ? 0.1697 0.1553 0.2052 0.0060  0.0145  0.0308  336  GLY A O   
2388  N N   . PHE A 339  ? 0.1699 0.1564 0.2116 0.0055  0.0143  0.0335  337  PHE A N   
2389  C CA  . PHE A 339  ? 0.1753 0.1625 0.2139 0.0066  0.0157  0.0341  337  PHE A CA  
2390  C C   . PHE A 339  ? 0.1772 0.1639 0.2181 0.0062  0.0153  0.0349  337  PHE A C   
2391  O O   . PHE A 339  ? 0.1731 0.1606 0.2192 0.0055  0.0147  0.0370  337  PHE A O   
2392  C CB  . PHE A 339  ? 0.1634 0.1536 0.2023 0.0077  0.0173  0.0366  337  PHE A CB  
2393  C CG  . PHE A 339  ? 0.1774 0.1690 0.2125 0.0091  0.0188  0.0367  337  PHE A CG  
2394  C CD1 . PHE A 339  ? 0.1792 0.1702 0.2101 0.0100  0.0193  0.0346  337  PHE A CD1 
2395  C CD2 . PHE A 339  ? 0.1740 0.1678 0.2102 0.0094  0.0196  0.0390  337  PHE A CD2 
2396  C CE1 . PHE A 339  ? 0.1871 0.1796 0.2148 0.0114  0.0205  0.0343  337  PHE A CE1 
2397  C CE2 . PHE A 339  ? 0.1985 0.1942 0.2311 0.0108  0.0209  0.0389  337  PHE A CE2 
2398  C CZ  . PHE A 339  ? 0.1920 0.1870 0.2203 0.0118  0.0214  0.0363  337  PHE A CZ  
2399  N N   . VAL A 340  ? 0.1709 0.1565 0.2085 0.0065  0.0155  0.0334  338  VAL A N   
2400  C CA  . VAL A 340  ? 0.1715 0.1566 0.2112 0.0063  0.0151  0.0340  338  VAL A CA  
2401  C C   . VAL A 340  ? 0.1541 0.1418 0.1935 0.0072  0.0166  0.0371  338  VAL A C   
2402  O O   . VAL A 340  ? 0.1744 0.1637 0.2096 0.0083  0.0180  0.0370  338  VAL A O   
2403  C CB  . VAL A 340  ? 0.1703 0.1532 0.2064 0.0062  0.0146  0.0309  338  VAL A CB  
2404  C CG1 . VAL A 340  ? 0.1929 0.1753 0.2315 0.0061  0.0141  0.0315  338  VAL A CG1 
2405  C CG2 . VAL A 340  ? 0.1869 0.1683 0.2231 0.0053  0.0132  0.0279  338  VAL A CG2 
2406  N N   . VAL A 341  ? 0.1703 0.1589 0.2144 0.0067  0.0161  0.0398  339  VAL A N   
2407  C CA  A VAL A 341  ? 0.1717 0.1632 0.2156 0.0074  0.0172  0.0429  339  VAL A CA  
2408  C CA  B VAL A 341  ? 0.1717 0.1632 0.2156 0.0074  0.0172  0.0429  339  VAL A CA  
2409  C C   . VAL A 341  ? 0.1825 0.1724 0.2285 0.0069  0.0161  0.0430  339  VAL A C   
2410  O O   . VAL A 341  ? 0.1873 0.1750 0.2382 0.0059  0.0143  0.0424  339  VAL A O   
2411  C CB  A VAL A 341  ? 0.1803 0.1759 0.2285 0.0073  0.0179  0.0474  339  VAL A CB  
2412  C CB  B VAL A 341  ? 0.1801 0.1756 0.2285 0.0073  0.0178  0.0474  339  VAL A CB  
2413  C CG1 A VAL A 341  ? 0.1881 0.1856 0.2340 0.0080  0.0191  0.0470  339  VAL A CG1 
2414  C CG1 B VAL A 341  ? 0.1931 0.1930 0.2392 0.0084  0.0195  0.0501  339  VAL A CG1 
2415  C CG2 A VAL A 341  ? 0.2005 0.1949 0.2561 0.0059  0.0161  0.0490  339  VAL A CG2 
2416  C CG2 B VAL A 341  ? 0.1979 0.1942 0.2461 0.0074  0.0183  0.0469  339  VAL A CG2 
2417  N N   . GLN A 342  ? 0.1719 0.1631 0.2145 0.0078  0.0171  0.0434  340  GLN A N   
2418  C CA  . GLN A 342  ? 0.1755 0.1651 0.2191 0.0075  0.0161  0.0431  340  GLN A CA  
2419  C C   . GLN A 342  ? 0.1740 0.1667 0.2220 0.0074  0.0162  0.0480  340  GLN A C   
2420  O O   . GLN A 342  ? 0.1928 0.1895 0.2383 0.0083  0.0177  0.0505  340  GLN A O   
2421  C CB  . GLN A 342  ? 0.1767 0.1658 0.2139 0.0085  0.0170  0.0405  340  GLN A CB  
2422  C CG  . GLN A 342  ? 0.1712 0.1575 0.2044 0.0085  0.0168  0.0361  340  GLN A CG  
2423  C CD  . GLN A 342  ? 0.1740 0.1609 0.2010 0.0097  0.0181  0.0345  340  GLN A CD  
2424  O OE1 . GLN A 342  ? 0.1842 0.1742 0.2094 0.0107  0.0194  0.0361  340  GLN A OE1 
2425  N NE2 . GLN A 342  ? 0.1782 0.1626 0.2021 0.0096  0.0176  0.0312  340  GLN A NE2 
2426  N N   . ALA A 343  ? 0.1635 0.1546 0.2184 0.0063  0.0143  0.0494  341  ALA A N   
2427  C CA  . ALA A 343  ? 0.1982 0.1921 0.2586 0.0058  0.0139  0.0547  341  ALA A CA  
2428  C C   . ALA A 343  ? 0.1909 0.1861 0.2492 0.0065  0.0143  0.0559  341  ALA A C   
2429  O O   . ALA A 343  ? 0.1921 0.1910 0.2536 0.0063  0.0144  0.0608  341  ALA A O   
2430  C CB  . ALA A 343  ? 0.2134 0.2046 0.2825 0.0045  0.0114  0.0553  341  ALA A CB  
2431  N N   . TYR A 344  ? 0.1749 0.1676 0.2282 0.0071  0.0144  0.0517  342  TYR A N   
2432  C CA  . TYR A 344  ? 0.1739 0.1682 0.2247 0.0078  0.0148  0.0529  342  TYR A CA  
2433  C C   . TYR A 344  ? 0.2042 0.2036 0.2494 0.0090  0.0171  0.0546  342  TYR A C   
2434  O O   . TYR A 344  ? 0.2044 0.2063 0.2476 0.0096  0.0176  0.0561  342  TYR A O   
2435  C CB  . TYR A 344  ? 0.1871 0.1776 0.2350 0.0080  0.0141  0.0484  342  TYR A CB  
2436  C CG  . TYR A 344  ? 0.1769 0.1660 0.2173 0.0088  0.0152  0.0437  342  TYR A CG  
2437  C CD1 . TYR A 344  ? 0.1839 0.1744 0.2203 0.0094  0.0167  0.0430  342  TYR A CD1 
2438  C CD2 . TYR A 344  ? 0.1819 0.1683 0.2199 0.0090  0.0146  0.0401  342  TYR A CD2 
2439  C CE1 . TYR A 344  ? 0.1915 0.1805 0.2221 0.0099  0.0173  0.0390  342  TYR A CE1 
2440  C CE2 . TYR A 344  ? 0.1815 0.1666 0.2134 0.0095  0.0154  0.0363  342  TYR A CE2 
2441  C CZ  . TYR A 344  ? 0.1825 0.1688 0.2109 0.0099  0.0167  0.0359  342  TYR A CZ  
2442  O OH  . TYR A 344  ? 0.1828 0.1677 0.2061 0.0103  0.0171  0.0323  342  TYR A OH  
2443  N N   . GLY A 345  ? 0.1846 0.1857 0.2276 0.0094  0.0184  0.0542  343  GLY A N   
2444  C CA  . GLY A 345  ? 0.1944 0.2003 0.2322 0.0108  0.0204  0.0549  343  GLY A CA  
2445  C C   . GLY A 345  ? 0.1913 0.2034 0.2325 0.0107  0.0212  0.0605  343  GLY A C   
2446  O O   . GLY A 345  ? 0.1929 0.2050 0.2397 0.0096  0.0206  0.0631  343  GLY A O   
2447  N N   . LYS A 346  ? 0.1938 0.2115 0.2317 0.0119  0.0226  0.0624  344  LYS A N   
2448  C CA  . LYS A 346  ? 0.1842 0.2091 0.2249 0.0119  0.0235  0.0682  344  LYS A CA  
2449  C C   . LYS A 346  ? 0.2045 0.2324 0.2454 0.0122  0.0248  0.0686  344  LYS A C   
2450  O O   . LYS A 346  ? 0.1973 0.2304 0.2424 0.0117  0.0252  0.0737  344  LYS A O   
2451  C CB  . LYS A 346  ? 0.1902 0.2212 0.2265 0.0133  0.0248  0.0694  344  LYS A CB  
2452  C CG  . LYS A 346  ? 0.2103 0.2389 0.2470 0.0129  0.0235  0.0697  344  LYS A CG  
2453  C CD  . LYS A 346  ? 0.2438 0.2783 0.2753 0.0144  0.0247  0.0702  344  LYS A CD  
2454  C CE  . LYS A 346  ? 0.2223 0.2554 0.2556 0.0138  0.0233  0.0719  344  LYS A CE  
2455  N NZ  . LYS A 346  ? 0.2407 0.2791 0.2684 0.0154  0.0243  0.0716  344  LYS A NZ  
2456  N N   . ARG A 347  ? 0.1837 0.2088 0.2204 0.0130  0.0253  0.0637  345  ARG A N   
2457  C CA  . ARG A 347  ? 0.1872 0.2149 0.2242 0.0135  0.0264  0.0637  345  ARG A CA  
2458  C C   . ARG A 347  ? 0.1946 0.2182 0.2371 0.0119  0.0251  0.0642  345  ARG A C   
2459  O O   . ARG A 347  ? 0.1842 0.2103 0.2281 0.0120  0.0258  0.0651  345  ARG A O   
2460  C CB  . ARG A 347  ? 0.1945 0.2212 0.2253 0.0151  0.0273  0.0583  345  ARG A CB  
2461  C CG  . ARG A 347  ? 0.1777 0.2100 0.2035 0.0170  0.0287  0.0578  345  ARG A CG  
2462  C CD  . ARG A 347  ? 0.1710 0.2006 0.1914 0.0184  0.0290  0.0520  345  ARG A CD  
2463  N NE  . ARG A 347  ? 0.1939 0.2165 0.2128 0.0177  0.0276  0.0489  345  ARG A NE  
2464  C CZ  . ARG A 347  ? 0.1895 0.2082 0.2048 0.0184  0.0273  0.0441  345  ARG A CZ  
2465  N NH1 . ARG A 347  ? 0.1991 0.2197 0.2121 0.0199  0.0281  0.0416  345  ARG A NH1 
2466  N NH2 . ARG A 347  ? 0.1759 0.1890 0.1902 0.0176  0.0261  0.0418  345  ARG A NH2 
2467  N N   . CYS A 348  ? 0.1841 0.2019 0.2301 0.0104  0.0231  0.0636  346  CYS A N   
2468  C CA  . CYS A 348  ? 0.1863 0.1996 0.2368 0.0091  0.0216  0.0627  346  CYS A CA  
2469  C C   . CYS A 348  ? 0.1910 0.2080 0.2469 0.0084  0.0219  0.0668  346  CYS A C   
2470  O O   . CYS A 348  ? 0.1901 0.2059 0.2459 0.0084  0.0220  0.0650  346  CYS A O   
2471  C CB  . CYS A 348  ? 0.1963 0.2045 0.2510 0.0077  0.0194  0.0622  346  CYS A CB  
2472  S SG  . CYS A 348  ? 0.2352 0.2374 0.2935 0.0065  0.0175  0.0587  346  CYS A SG  
2473  N N   . PRO A 349  ? 0.1877 0.2092 0.2485 0.0077  0.0219  0.0725  347  PRO A N   
2474  C CA  . PRO A 349  ? 0.1850 0.2100 0.2514 0.0069  0.0220  0.0766  347  PRO A CA  
2475  C C   . PRO A 349  ? 0.1722 0.2022 0.2344 0.0083  0.0243  0.0761  347  PRO A C   
2476  O O   . PRO A 349  ? 0.1969 0.2274 0.2621 0.0078  0.0243  0.0767  347  PRO A O   
2477  C CB  . PRO A 349  ? 0.1915 0.2212 0.2633 0.0060  0.0217  0.0832  347  PRO A CB  
2478  C CG  . PRO A 349  ? 0.2112 0.2418 0.2785 0.0069  0.0221  0.0827  347  PRO A CG  
2479  C CD  . PRO A 349  ? 0.2003 0.2244 0.2620 0.0076  0.0217  0.0759  347  PRO A CD  
2480  N N   . PHE A 350  ? 0.1905 0.2243 0.2462 0.0101  0.0261  0.0747  348  PHE A N   
2481  C CA  . PHE A 350  ? 0.1907 0.2297 0.2427 0.0118  0.0281  0.0736  348  PHE A CA  
2482  C C   . PHE A 350  ? 0.1785 0.2121 0.2273 0.0123  0.0279  0.0680  348  PHE A C   
2483  O O   . PHE A 350  ? 0.1928 0.2288 0.2417 0.0130  0.0288  0.0675  348  PHE A O   
2484  C CB  . PHE A 350  ? 0.1996 0.2445 0.2461 0.0136  0.0298  0.0735  348  PHE A CB  
2485  C CG  . PHE A 350  ? 0.2244 0.2745 0.2738 0.0129  0.0299  0.0793  348  PHE A CG  
2486  C CD1 . PHE A 350  ? 0.2152 0.2733 0.2685 0.0126  0.0309  0.0850  348  PHE A CD1 
2487  C CD2 . PHE A 350  ? 0.2216 0.2688 0.2705 0.0125  0.0288  0.0793  348  PHE A CD2 
2488  C CE1 . PHE A 350  ? 0.2390 0.3023 0.2955 0.0118  0.0308  0.0910  348  PHE A CE1 
2489  C CE2 . PHE A 350  ? 0.2354 0.2873 0.2875 0.0117  0.0286  0.0851  348  PHE A CE2 
2490  C CZ  . PHE A 350  ? 0.2582 0.3183 0.3142 0.0114  0.0295  0.0911  348  PHE A CZ  
2491  N N   . VAL A 351  ? 0.1738 0.2004 0.2202 0.0120  0.0266  0.0639  349  VAL A N   
2492  C CA  . VAL A 351  ? 0.1680 0.1894 0.2123 0.0121  0.0260  0.0592  349  VAL A CA  
2493  C C   . VAL A 351  ? 0.1905 0.2097 0.2404 0.0106  0.0248  0.0603  349  VAL A C   
2494  O O   . VAL A 351  ? 0.1886 0.2075 0.2381 0.0110  0.0251  0.0587  349  VAL A O   
2495  C CB  . VAL A 351  ? 0.1696 0.1848 0.2107 0.0119  0.0248  0.0552  349  VAL A CB  
2496  C CG1 . VAL A 351  ? 0.2019 0.2121 0.2414 0.0118  0.0240  0.0510  349  VAL A CG1 
2497  C CG2 . VAL A 351  ? 0.2221 0.2395 0.2576 0.0135  0.0259  0.0537  349  VAL A CG2 
2498  N N   . LEU A 352  ? 0.1933 0.2111 0.2489 0.0090  0.0233  0.0632  350  LEU A N   
2499  C CA  . LEU A 352  ? 0.1812 0.1973 0.2429 0.0075  0.0220  0.0644  350  LEU A CA  
2500  C C   . LEU A 352  ? 0.1888 0.2106 0.2528 0.0078  0.0233  0.0677  350  LEU A C   
2501  O O   . LEU A 352  ? 0.2011 0.2218 0.2670 0.0075  0.0229  0.0667  350  LEU A O   
2502  C CB  . LEU A 352  ? 0.1867 0.2005 0.2548 0.0058  0.0200  0.0669  350  LEU A CB  
2503  C CG  . LEU A 352  ? 0.1959 0.2035 0.2626 0.0054  0.0184  0.0629  350  LEU A CG  
2504  C CD1 . LEU A 352  ? 0.2391 0.2453 0.3130 0.0040  0.0164  0.0655  350  LEU A CD1 
2505  C CD2 . LEU A 352  ? 0.2238 0.2269 0.2894 0.0051  0.0173  0.0583  350  LEU A CD2 
2506  N N   . ASP A 353  ? 0.1860 0.2147 0.2502 0.0085  0.0249  0.0717  351  ASP A N   
2507  C CA  . ASP A 353  ? 0.1832 0.2184 0.2493 0.0089  0.0264  0.0748  351  ASP A CA  
2508  C C   . ASP A 353  ? 0.1772 0.2124 0.2384 0.0106  0.0276  0.0705  351  ASP A C   
2509  O O   . ASP A 353  ? 0.1829 0.2196 0.2466 0.0105  0.0278  0.0710  351  ASP A O   
2510  C CB  . ASP A 353  ? 0.1801 0.2236 0.2456 0.0097  0.0282  0.0792  351  ASP A CB  
2511  C CG  . ASP A 353  ? 0.2182 0.2632 0.2901 0.0080  0.0271  0.0849  351  ASP A CG  
2512  O OD1 . ASP A 353  ? 0.2428 0.2837 0.3212 0.0061  0.0251  0.0863  351  ASP A OD1 
2513  O OD2 . ASP A 353  ? 0.2587 0.3092 0.3294 0.0085  0.0282  0.0880  351  ASP A OD2 
2514  N N   . PHE A 354  ? 0.1881 0.2218 0.2428 0.0121  0.0282  0.0664  352  PHE A N   
2515  C CA  . PHE A 354  ? 0.1680 0.2012 0.2187 0.0137  0.0289  0.0622  352  PHE A CA  
2516  C C   . PHE A 354  ? 0.1804 0.2073 0.2327 0.0126  0.0273  0.0597  352  PHE A C   
2517  O O   . PHE A 354  ? 0.1835 0.2113 0.2364 0.0131  0.0276  0.0588  352  PHE A O   
2518  C CB  . PHE A 354  ? 0.1944 0.2263 0.2385 0.0152  0.0294  0.0583  352  PHE A CB  
2519  C CG  . PHE A 354  ? 0.1957 0.2252 0.2365 0.0165  0.0295  0.0536  352  PHE A CG  
2520  C CD1 . PHE A 354  ? 0.2158 0.2506 0.2552 0.0185  0.0310  0.0527  352  PHE A CD1 
2521  C CD2 . PHE A 354  ? 0.2237 0.2460 0.2632 0.0157  0.0279  0.0502  352  PHE A CD2 
2522  C CE1 . PHE A 354  ? 0.2336 0.2659 0.2708 0.0197  0.0307  0.0485  352  PHE A CE1 
2523  C CE2 . PHE A 354  ? 0.2253 0.2454 0.2623 0.0167  0.0277  0.0465  352  PHE A CE2 
2524  C CZ  . PHE A 354  ? 0.2217 0.2465 0.2578 0.0187  0.0291  0.0456  352  PHE A CZ  
2525  N N   . ILE A 355  ? 0.1733 0.1940 0.2263 0.0112  0.0254  0.0583  353  ILE A N   
2526  C CA  . ILE A 355  ? 0.1653 0.1806 0.2193 0.0102  0.0238  0.0556  353  ILE A CA  
2527  C C   . ILE A 355  ? 0.2191 0.2356 0.2793 0.0090  0.0231  0.0583  353  ILE A C   
2528  O O   . ILE A 355  ? 0.1926 0.2079 0.2533 0.0090  0.0227  0.0568  353  ILE A O   
2529  C CB  . ILE A 355  ? 0.1821 0.1916 0.2355 0.0090  0.0220  0.0534  353  ILE A CB  
2530  C CG1 . ILE A 355  ? 0.1950 0.2027 0.2421 0.0102  0.0226  0.0502  353  ILE A CG1 
2531  C CG2 . ILE A 355  ? 0.2066 0.2118 0.2620 0.0079  0.0202  0.0512  353  ILE A CG2 
2532  C CD1 . ILE A 355  ? 0.1970 0.2003 0.2436 0.0092  0.0211  0.0485  353  ILE A CD1 
2533  N N   . ILE A 356  ? 0.1902 0.2090 0.2556 0.0079  0.0228  0.0626  354  ILE A N   
2534  C CA  . ILE A 356  ? 0.1788 0.1990 0.2509 0.0066  0.0221  0.0655  354  ILE A CA  
2535  C C   . ILE A 356  ? 0.1845 0.2099 0.2562 0.0078  0.0238  0.0666  354  ILE A C   
2536  O O   . ILE A 356  ? 0.1890 0.2138 0.2634 0.0074  0.0232  0.0661  354  ILE A O   
2537  C CB  . ILE A 356  ? 0.2019 0.2241 0.2802 0.0053  0.0214  0.0704  354  ILE A CB  
2538  C CG1 . ILE A 356  ? 0.2029 0.2191 0.2830 0.0040  0.0191  0.0685  354  ILE A CG1 
2539  C CG2 . ILE A 356  ? 0.2159 0.2414 0.3014 0.0042  0.0211  0.0744  354  ILE A CG2 
2540  C CD1 . ILE A 356  ? 0.2155 0.2332 0.3005 0.0030  0.0185  0.0729  354  ILE A CD1 
2541  N N   . ASP A 357  ? 0.1843 0.2153 0.2527 0.0095  0.0260  0.0676  355  ASP A N   
2542  C CA  . ASP A 357  ? 0.1758 0.2122 0.2436 0.0109  0.0277  0.0680  355  ASP A CA  
2543  C C   . ASP A 357  ? 0.1808 0.2135 0.2450 0.0119  0.0274  0.0631  355  ASP A C   
2544  O O   . ASP A 357  ? 0.1887 0.2231 0.2550 0.0122  0.0276  0.0631  355  ASP A O   
2545  C CB  . ASP A 357  ? 0.2113 0.2549 0.2760 0.0127  0.0300  0.0694  355  ASP A CB  
2546  C CG  . ASP A 357  ? 0.2053 0.2547 0.2690 0.0146  0.0317  0.0688  355  ASP A CG  
2547  O OD1 . ASP A 357  ? 0.2599 0.3144 0.3284 0.0141  0.0324  0.0725  355  ASP A OD1 
2548  O OD2 . ASP A 357  ? 0.2220 0.2708 0.2808 0.0165  0.0324  0.0644  355  ASP A OD2 
2549  N N   . LEU A 358  ? 0.1926 0.2204 0.2518 0.0124  0.0268  0.0591  356  LEU A N   
2550  C CA  . LEU A 358  ? 0.1712 0.1953 0.2276 0.0131  0.0262  0.0549  356  LEU A CA  
2551  C C   . LEU A 358  ? 0.1726 0.1928 0.2326 0.0114  0.0243  0.0547  356  LEU A C   
2552  O O   . LEU A 358  ? 0.1819 0.2018 0.2422 0.0119  0.0241  0.0533  356  LEU A O   
2553  C CB  . LEU A 358  ? 0.1561 0.1757 0.2072 0.0135  0.0257  0.0513  356  LEU A CB  
2554  C CG  . LEU A 358  ? 0.1635 0.1788 0.2120 0.0139  0.0248  0.0474  356  LEU A CG  
2555  C CD1 . LEU A 358  ? 0.2062 0.2250 0.2540 0.0159  0.0259  0.0463  356  LEU A CD1 
2556  C CD2 . LEU A 358  ? 0.1897 0.2009 0.2334 0.0141  0.0243  0.0444  356  LEU A CD2 
2557  N N   . ALA A 359  ? 0.1841 0.2014 0.2472 0.0096  0.0228  0.0559  357  ALA A N   
2558  C CA  . ALA A 359  ? 0.1804 0.1946 0.2474 0.0080  0.0209  0.0555  357  ALA A CA  
2559  C C   . ALA A 359  ? 0.1707 0.1890 0.2426 0.0079  0.0214  0.0584  357  ALA A C   
2560  O O   . ALA A 359  ? 0.1909 0.2080 0.2642 0.0076  0.0204  0.0572  357  ALA A O   
2561  C CB  . ALA A 359  ? 0.2086 0.2196 0.2788 0.0062  0.0192  0.0562  357  ALA A CB  
2562  N N   . ARG A 360  ? 0.1843 0.2081 0.2589 0.0081  0.0228  0.0624  358  ARG A N   
2563  C CA  . ARG A 360  ? 0.1986 0.2272 0.2780 0.0081  0.0234  0.0654  358  ARG A CA  
2564  C C   . ARG A 360  ? 0.2076 0.2386 0.2841 0.0100  0.0247  0.0633  358  ARG A C   
2565  O O   . ARG A 360  ? 0.2277 0.2589 0.3069 0.0097  0.0241  0.0633  358  ARG A O   
2566  C CB  . ARG A 360  ? 0.2101 0.2450 0.2927 0.0079  0.0248  0.0704  358  ARG A CB  
2567  C CG  . ARG A 360  ? 0.2491 0.2821 0.3368 0.0058  0.0232  0.0734  358  ARG A CG  
2568  C CD  . ARG A 360  ? 0.2878 0.3279 0.3803 0.0054  0.0244  0.0795  358  ARG A CD  
2569  N NE  . ARG A 360  ? 0.3527 0.3910 0.4490 0.0038  0.0230  0.0821  358  ARG A NE  
2570  C CZ  . ARG A 360  ? 0.4304 0.4655 0.5338 0.0018  0.0206  0.0837  358  ARG A CZ  
2571  N NH1 . ARG A 360  ? 0.4683 0.5020 0.5757 0.0010  0.0194  0.0831  358  ARG A NH1 
2572  N NH2 . ARG A 360  ? 0.3692 0.4023 0.4760 0.0005  0.0193  0.0856  358  ARG A NH2 
2573  N N   . ARG A 361  ? 0.2110 0.2438 0.2821 0.0119  0.0263  0.0615  359  ARG A N   
2574  C CA  . ARG A 361  ? 0.2026 0.2378 0.2715 0.0140  0.0274  0.0592  359  ARG A CA  
2575  C C   . ARG A 361  ? 0.2110 0.2405 0.2788 0.0138  0.0257  0.0557  359  ARG A C   
2576  O O   . ARG A 361  ? 0.2349 0.2658 0.3043 0.0145  0.0257  0.0551  359  ARG A O   
2577  C CB  . ARG A 361  ? 0.2483 0.2858 0.3119 0.0161  0.0289  0.0572  359  ARG A CB  
2578  C CG  . ARG A 361  ? 0.2720 0.3172 0.3362 0.0169  0.0310  0.0604  359  ARG A CG  
2579  C CD  . ARG A 361  ? 0.2593 0.3070 0.3180 0.0193  0.0324  0.0575  359  ARG A CD  
2580  N NE  . ARG A 361  ? 0.2612 0.3044 0.3160 0.0189  0.0317  0.0559  359  ARG A NE  
2581  C CZ  . ARG A 361  ? 0.2528 0.2918 0.3032 0.0199  0.0312  0.0515  359  ARG A CZ  
2582  N NH1 . ARG A 361  ? 0.2382 0.2759 0.2879 0.0212  0.0309  0.0482  359  ARG A NH1 
2583  N NH2 . ARG A 361  ? 0.2267 0.2630 0.2738 0.0196  0.0309  0.0505  359  ARG A NH2 
2584  N N   . SER A 362  ? 0.1968 0.2203 0.2619 0.0128  0.0242  0.0534  360  SER A N   
2585  C CA  . SER A 362  ? 0.1874 0.2060 0.2509 0.0126  0.0226  0.0504  360  SER A CA  
2586  C C   . SER A 362  ? 0.1896 0.2061 0.2573 0.0106  0.0207  0.0512  360  SER A C   
2587  O O   . SER A 362  ? 0.2008 0.2147 0.2682 0.0105  0.0195  0.0494  360  SER A O   
2588  C CB  . SER A 362  ? 0.2118 0.2257 0.2706 0.0123  0.0218  0.0476  360  SER A CB  
2589  O OG  . SER A 362  ? 0.1901 0.2015 0.2501 0.0106  0.0208  0.0486  360  SER A OG  
2590  N N   . GLY A 363  ? 0.1960 0.2133 0.2678 0.0092  0.0203  0.0540  361  GLY A N   
2591  C CA  . GLY A 363  ? 0.2218 0.2367 0.2977 0.0073  0.0182  0.0542  361  GLY A CA  
2592  C C   . GLY A 363  ? 0.2375 0.2470 0.3110 0.0062  0.0163  0.0513  361  GLY A C   
2593  O O   . GLY A 363  ? 0.2409 0.2485 0.3171 0.0049  0.0144  0.0506  361  GLY A O   
2594  N N   . ARG A 364  ? 0.2054 0.2129 0.2740 0.0068  0.0168  0.0495  362  ARG A N   
2595  C CA  . ARG A 364  ? 0.2214 0.2244 0.2875 0.0058  0.0152  0.0467  362  ARG A CA  
2596  C C   . ARG A 364  ? 0.2002 0.2026 0.2689 0.0048  0.0147  0.0478  362  ARG A C   
2597  O O   . ARG A 364  ? 0.2108 0.2150 0.2793 0.0053  0.0160  0.0497  362  ARG A O   
2598  C CB  . ARG A 364  ? 0.2463 0.2477 0.3062 0.0070  0.0160  0.0444  362  ARG A CB  
2599  C CG  . ARG A 364  ? 0.2892 0.2914 0.3467 0.0084  0.0166  0.0434  362  ARG A CG  
2600  C CD  . ARG A 364  ? 0.2134 0.2129 0.2696 0.0077  0.0149  0.0413  362  ARG A CD  
2601  N NE  . ARG A 364  ? 0.1995 0.2003 0.2557 0.0090  0.0153  0.0412  362  ARG A NE  
2602  C CZ  . ARG A 364  ? 0.1945 0.1943 0.2474 0.0101  0.0156  0.0396  362  ARG A CZ  
2603  N NH1 . ARG A 364  ? 0.1936 0.1909 0.2425 0.0101  0.0155  0.0380  362  ARG A NH1 
2604  N NH2 . ARG A 364  ? 0.1950 0.1963 0.2490 0.0114  0.0159  0.0396  362  ARG A NH2 
2605  N N   . ARG A 365  ? 0.1883 0.1882 0.2596 0.0033  0.0125  0.0465  363  ARG A N   
2606  C CA  . ARG A 365  ? 0.1827 0.1815 0.2573 0.0023  0.0116  0.0471  363  ARG A CA  
2607  C C   . ARG A 365  ? 0.2085 0.2047 0.2779 0.0027  0.0117  0.0444  363  ARG A C   
2608  O O   . ARG A 365  ? 0.2123 0.2059 0.2802 0.0021  0.0102  0.0413  363  ARG A O   
2609  C CB  . ARG A 365  ? 0.1914 0.1888 0.2713 0.0008  0.0091  0.0462  363  ARG A CB  
2610  C CG  . ARG A 365  ? 0.1990 0.1953 0.2837 -0.0001 0.0079  0.0469  363  ARG A CG  
2611  C CD  . ARG A 365  ? 0.2380 0.2341 0.3301 -0.0015 0.0056  0.0471  363  ARG A CD  
2612  N NE  . ARG A 365  ? 0.2169 0.2119 0.3146 -0.0023 0.0043  0.0481  363  ARG A NE  
2613  C CZ  . ARG A 365  ? 0.2096 0.2020 0.3092 -0.0029 0.0021  0.0447  363  ARG A CZ  
2614  N NH1 . ARG A 365  ? 0.2547 0.2457 0.3510 -0.0029 0.0009  0.0403  363  ARG A NH1 
2615  N NH2 . ARG A 365  ? 0.1946 0.1859 0.2996 -0.0035 0.0009  0.0459  363  ARG A NH2 
2616  N N   . ILE A 366  ? 0.1835 0.1808 0.2499 0.0037  0.0135  0.0456  364  ILE A N   
2617  C CA  . ILE A 366  ? 0.1803 0.1754 0.2413 0.0042  0.0138  0.0432  364  ILE A CA  
2618  C C   . ILE A 366  ? 0.1731 0.1659 0.2365 0.0031  0.0122  0.0421  364  ILE A C   
2619  O O   . ILE A 366  ? 0.1739 0.1674 0.2425 0.0025  0.0117  0.0444  364  ILE A O   
2620  C CB  . ILE A 366  ? 0.1873 0.1847 0.2453 0.0056  0.0160  0.0448  364  ILE A CB  
2621  C CG1 . ILE A 366  ? 0.2230 0.2229 0.2790 0.0069  0.0174  0.0452  364  ILE A CG1 
2622  C CG2 . ILE A 366  ? 0.2020 0.1971 0.2550 0.0060  0.0162  0.0424  364  ILE A CG2 
2623  C CD1 . ILE A 366  ? 0.2045 0.2078 0.2581 0.0085  0.0195  0.0465  364  ILE A CD1 
2624  N N   . MET A 367  ? 0.1848 0.1750 0.2447 0.0029  0.0113  0.0386  365  MET A N   
2625  C CA  . MET A 367  ? 0.1833 0.1715 0.2449 0.0022  0.0098  0.0368  365  MET A CA  
2626  C C   . MET A 367  ? 0.1808 0.1687 0.2397 0.0029  0.0110  0.0375  365  MET A C   
2627  O O   . MET A 367  ? 0.2256 0.2132 0.2788 0.0038  0.0122  0.0364  365  MET A O   
2628  C CB  . MET A 367  ? 0.1845 0.1710 0.2431 0.0018  0.0085  0.0327  365  MET A CB  
2629  C CG  . MET A 367  ? 0.2042 0.1916 0.2645 0.0012  0.0074  0.0321  365  MET A CG  
2630  S SD  . MET A 367  ? 0.2131 0.1998 0.2700 0.0007  0.0057  0.0277  365  MET A SD  
2631  C CE  . MET A 367  ? 0.2561 0.2424 0.3192 -0.0003 0.0032  0.0253  365  MET A CE  
2632  N N   . VAL A 368  ? 0.1646 0.1528 0.2280 0.0026  0.0107  0.0396  366  VAL A N   
2633  C CA  . VAL A 368  ? 0.1740 0.1626 0.2354 0.0032  0.0119  0.0410  366  VAL A CA  
2634  C C   . VAL A 368  ? 0.1677 0.1538 0.2309 0.0027  0.0103  0.0389  366  VAL A C   
2635  O O   . VAL A 368  ? 0.1766 0.1621 0.2463 0.0018  0.0086  0.0397  366  VAL A O   
2636  C CB  . VAL A 368  ? 0.1900 0.1819 0.2551 0.0034  0.0129  0.0458  366  VAL A CB  
2637  C CG1 . VAL A 368  ? 0.2058 0.1985 0.2683 0.0041  0.0140  0.0471  366  VAL A CG1 
2638  C CG2 . VAL A 368  ? 0.2084 0.2034 0.2722 0.0040  0.0145  0.0476  366  VAL A CG2 
2639  N N   . ARG A 369  ? 0.1543 0.1390 0.2120 0.0032  0.0107  0.0361  367  ARG A N   
2640  C CA  . ARG A 369  ? 0.1804 0.1631 0.2393 0.0029  0.0093  0.0340  367  ARG A CA  
2641  C C   . ARG A 369  ? 0.1745 0.1579 0.2338 0.0034  0.0102  0.0367  367  ARG A C   
2642  O O   . ARG A 369  ? 0.1987 0.1830 0.2526 0.0043  0.0120  0.0372  367  ARG A O   
2643  C CB  . ARG A 369  ? 0.1824 0.1637 0.2357 0.0031  0.0093  0.0298  367  ARG A CB  
2644  C CG  . ARG A 369  ? 0.1910 0.1707 0.2460 0.0029  0.0079  0.0273  367  ARG A CG  
2645  C CD  . ARG A 369  ? 0.1959 0.1750 0.2448 0.0033  0.0084  0.0241  367  ARG A CD  
2646  N NE  . ARG A 369  ? 0.1861 0.1656 0.2325 0.0029  0.0079  0.0215  367  ARG A NE  
2647  C CZ  . ARG A 369  ? 0.2060 0.1857 0.2465 0.0031  0.0086  0.0199  367  ARG A CZ  
2648  N NH1 . ARG A 369  ? 0.2095 0.1887 0.2459 0.0038  0.0099  0.0203  367  ARG A NH1 
2649  N NH2 . ARG A 369  ? 0.2124 0.1930 0.2514 0.0026  0.0080  0.0182  367  ARG A NH2 
2650  N N   . LEU A 370  ? 0.1722 0.1553 0.2380 0.0027  0.0089  0.0385  368  LEU A N   
2651  C CA  . LEU A 370  ? 0.1649 0.1488 0.2320 0.0030  0.0094  0.0414  368  LEU A CA  
2652  C C   . LEU A 370  ? 0.1715 0.1529 0.2376 0.0031  0.0083  0.0380  368  LEU A C   
2653  O O   . LEU A 370  ? 0.1788 0.1582 0.2492 0.0025  0.0062  0.0354  368  LEU A O   
2654  C CB  . LEU A 370  ? 0.1929 0.1779 0.2683 0.0022  0.0083  0.0457  368  LEU A CB  
2655  C CG  . LEU A 370  ? 0.1959 0.1827 0.2732 0.0023  0.0087  0.0498  368  LEU A CG  
2656  C CD1 . LEU A 370  ? 0.2185 0.2091 0.2899 0.0034  0.0114  0.0525  368  LEU A CD1 
2657  C CD2 . LEU A 370  ? 0.2086 0.1961 0.2956 0.0012  0.0070  0.0539  368  LEU A CD2 
2658  N N   . VAL A 371  ? 0.1726 0.1543 0.2331 0.0040  0.0097  0.0378  369  VAL A N   
2659  C CA  . VAL A 371  ? 0.1642 0.1440 0.2235 0.0042  0.0089  0.0349  369  VAL A CA  
2660  C C   . VAL A 371  ? 0.1724 0.1535 0.2323 0.0046  0.0096  0.0383  369  VAL A C   
2661  O O   . VAL A 371  ? 0.1987 0.1826 0.2583 0.0049  0.0109  0.0424  369  VAL A O   
2662  C CB  . VAL A 371  ? 0.1700 0.1491 0.2216 0.0048  0.0099  0.0312  369  VAL A CB  
2663  C CG1 . VAL A 371  ? 0.1844 0.1631 0.2350 0.0043  0.0095  0.0285  369  VAL A CG1 
2664  C CG2 . VAL A 371  ? 0.1956 0.1765 0.2414 0.0057  0.0121  0.0330  369  VAL A CG2 
2665  N N   . LYS A 372  ? 0.1773 0.1567 0.2378 0.0047  0.0086  0.0366  370  LYS A N   
2666  C CA  . LYS A 372  ? 0.1870 0.1678 0.2468 0.0052  0.0093  0.0397  370  LYS A CA  
2667  C C   . LYS A 372  ? 0.2043 0.1863 0.2556 0.0063  0.0114  0.0386  370  LYS A C   
2668  O O   . LYS A 372  ? 0.2279 0.2129 0.2766 0.0069  0.0130  0.0416  370  LYS A O   
2669  C CB  . LYS A 372  ? 0.2027 0.1817 0.2680 0.0050  0.0073  0.0391  370  LYS A CB  
2670  C CG  . LYS A 372  ? 0.2006 0.1791 0.2754 0.0040  0.0053  0.0416  370  LYS A CG  
2671  C CD  . LYS A 372  ? 0.2211 0.1975 0.3029 0.0037  0.0029  0.0409  370  LYS A CD  
2672  C CE  . LYS A 372  ? 0.2033 0.1789 0.2951 0.0027  0.0006  0.0427  370  LYS A CE  
2673  N NZ  . LYS A 372  ? 0.2155 0.1887 0.3153 0.0025  -0.0022 0.0415  370  LYS A NZ  
2674  N N   . GLY A 373  ? 0.1835 0.1635 0.2306 0.0065  0.0113  0.0341  371  GLY A N   
2675  C CA  . GLY A 373  ? 0.1757 0.1564 0.2153 0.0074  0.0130  0.0328  371  GLY A CA  
2676  C C   . GLY A 373  ? 0.1918 0.1707 0.2283 0.0076  0.0126  0.0293  371  GLY A C   
2677  O O   . GLY A 373  ? 0.1964 0.1744 0.2361 0.0074  0.0115  0.0291  371  GLY A O   
2678  N N   . ALA A 374  ? 0.1788 0.1573 0.2097 0.0078  0.0135  0.0266  372  ALA A N   
2679  C CA  . ALA A 374  ? 0.1886 0.1656 0.2170 0.0078  0.0130  0.0231  372  ALA A CA  
2680  C C   . ALA A 374  ? 0.2168 0.1943 0.2407 0.0086  0.0140  0.0229  372  ALA A C   
2681  O O   . ALA A 374  ? 0.2193 0.1958 0.2412 0.0085  0.0136  0.0202  372  ALA A O   
2682  C CB  . ALA A 374  ? 0.2107 0.1872 0.2367 0.0073  0.0129  0.0202  372  ALA A CB  
2683  N N   . TYR A 375  ? 0.1937 0.1731 0.2157 0.0093  0.0151  0.0255  373  TYR A N   
2684  C CA  . TYR A 375  ? 0.1856 0.1656 0.2027 0.0102  0.0160  0.0249  373  TYR A CA  
2685  C C   . TYR A 375  ? 0.1629 0.1447 0.1810 0.0108  0.0162  0.0274  373  TYR A C   
2686  O O   . TYR A 375  ? 0.1946 0.1782 0.2090 0.0117  0.0172  0.0278  373  TYR A O   
2687  C CB  . TYR A 375  ? 0.2004 0.1817 0.2138 0.0108  0.0173  0.0249  373  TYR A CB  
2688  C CG  . TYR A 375  ? 0.1898 0.1696 0.2023 0.0103  0.0171  0.0230  373  TYR A CG  
2689  C CD1 . TYR A 375  ? 0.1835 0.1633 0.1991 0.0097  0.0168  0.0240  373  TYR A CD1 
2690  C CD2 . TYR A 375  ? 0.2321 0.2108 0.2409 0.0102  0.0171  0.0205  373  TYR A CD2 
2691  C CE1 . TYR A 375  ? 0.2060 0.1848 0.2208 0.0091  0.0165  0.0224  373  TYR A CE1 
2692  C CE2 . TYR A 375  ? 0.2484 0.2262 0.2566 0.0096  0.0169  0.0192  373  TYR A CE2 
2693  C CZ  . TYR A 375  ? 0.2504 0.2284 0.2614 0.0091  0.0166  0.0202  373  TYR A CZ  
2694  O OH  . TYR A 375  ? 0.2692 0.2466 0.2795 0.0085  0.0162  0.0190  373  TYR A OH  
2695  N N   . TRP A 376  ? 0.1660 0.1475 0.1892 0.0103  0.0151  0.0290  374  TRP A N   
2696  C CA  . TRP A 376  ? 0.2012 0.1851 0.2263 0.0107  0.0152  0.0326  374  TRP A CA  
2697  C C   . TRP A 376  ? 0.2000 0.1846 0.2210 0.0115  0.0156  0.0317  374  TRP A C   
2698  O O   . TRP A 376  ? 0.1918 0.1796 0.2102 0.0124  0.0166  0.0336  374  TRP A O   
2699  C CB  . TRP A 376  ? 0.2048 0.1877 0.2369 0.0100  0.0136  0.0344  374  TRP A CB  
2700  C CG  . TRP A 376  ? 0.1987 0.1845 0.2331 0.0103  0.0135  0.0388  374  TRP A CG  
2701  C CD1 . TRP A 376  ? 0.2122 0.2016 0.2483 0.0104  0.0142  0.0433  374  TRP A CD1 
2702  C CD2 . TRP A 376  ? 0.2053 0.1911 0.2404 0.0106  0.0128  0.0393  374  TRP A CD2 
2703  N NE1 . TRP A 376  ? 0.1985 0.1904 0.2363 0.0106  0.0139  0.0469  374  TRP A NE1 
2704  C CE2 . TRP A 376  ? 0.2052 0.1947 0.2425 0.0107  0.0130  0.0444  374  TRP A CE2 
2705  C CE3 . TRP A 376  ? 0.2413 0.2247 0.2757 0.0107  0.0120  0.0360  374  TRP A CE3 
2706  C CZ2 . TRP A 376  ? 0.2246 0.2154 0.2634 0.0110  0.0123  0.0465  374  TRP A CZ2 
2707  C CZ3 . TRP A 376  ? 0.2519 0.2362 0.2879 0.0110  0.0113  0.0379  374  TRP A CZ3 
2708  C CH2 . TRP A 376  ? 0.2456 0.2335 0.2837 0.0111  0.0114  0.0431  374  TRP A CH2 
2709  N N   . ASP A 377  ? 0.2123 0.1945 0.2329 0.0113  0.0148  0.0286  375  ASP A N   
2710  C CA  A ASP A 377  ? 0.2140 0.1966 0.2311 0.0120  0.0150  0.0276  375  ASP A CA  
2711  C CA  B ASP A 377  ? 0.2136 0.1964 0.2309 0.0120  0.0150  0.0279  375  ASP A CA  
2712  C C   . ASP A 377  ? 0.2065 0.1906 0.2178 0.0128  0.0163  0.0266  375  ASP A C   
2713  O O   . ASP A 377  ? 0.2058 0.1922 0.2146 0.0137  0.0168  0.0275  375  ASP A O   
2714  C CB  A ASP A 377  ? 0.2436 0.2234 0.2605 0.0115  0.0141  0.0238  375  ASP A CB  
2715  C CB  B ASP A 377  ? 0.2530 0.2334 0.2713 0.0116  0.0139  0.0250  375  ASP A CB  
2716  C CG  A ASP A 377  ? 0.2888 0.2673 0.3116 0.0110  0.0125  0.0238  375  ASP A CG  
2717  C CG  B ASP A 377  ? 0.2563 0.2345 0.2730 0.0110  0.0138  0.0212  375  ASP A CG  
2718  O OD1 A ASP A 377  ? 0.3794 0.3589 0.4061 0.0111  0.0120  0.0270  375  ASP A OD1 
2719  O OD1 B ASP A 377  ? 0.3136 0.2920 0.3268 0.0111  0.0147  0.0204  375  ASP A OD1 
2720  O OD2 A ASP A 377  ? 0.3781 0.3547 0.4018 0.0105  0.0118  0.0205  375  ASP A OD2 
2721  O OD2 B ASP A 377  ? 0.2799 0.2567 0.2991 0.0106  0.0127  0.0190  375  ASP A OD2 
2722  N N   . ALA A 378  ? 0.1975 0.1804 0.2069 0.0126  0.0168  0.0247  376  ALA A N   
2723  C CA  . ALA A 378  ? 0.1884 0.1722 0.1931 0.0134  0.0177  0.0233  376  ALA A CA  
2724  C C   . ALA A 378  ? 0.1926 0.1803 0.1966 0.0144  0.0187  0.0259  376  ALA A C   
2725  O O   . ALA A 378  ? 0.1991 0.1888 0.1997 0.0155  0.0194  0.0252  376  ALA A O   
2726  C CB  . ALA A 378  ? 0.2089 0.1907 0.2126 0.0128  0.0177  0.0212  376  ALA A CB  
2727  N N   . GLU A 379  ? 0.1913 0.1803 0.1988 0.0141  0.0189  0.0289  377  GLU A N   
2728  C CA  . GLU A 379  ? 0.1869 0.1804 0.1939 0.0151  0.0199  0.0316  377  GLU A CA  
2729  C C   . GLU A 379  ? 0.1752 0.1721 0.1817 0.0158  0.0200  0.0337  377  GLU A C   
2730  O O   . GLU A 379  ? 0.1964 0.1976 0.2001 0.0170  0.0210  0.0344  377  GLU A O   
2731  C CB  . GLU A 379  ? 0.1910 0.1855 0.2023 0.0144  0.0200  0.0347  377  GLU A CB  
2732  C CG  . GLU A 379  ? 0.2150 0.2068 0.2271 0.0137  0.0199  0.0330  377  GLU A CG  
2733  C CD  . GLU A 379  ? 0.2096 0.2024 0.2179 0.0147  0.0209  0.0311  377  GLU A CD  
2734  O OE1 . GLU A 379  ? 0.2110 0.2070 0.2163 0.0160  0.0217  0.0310  377  GLU A OE1 
2735  O OE2 . GLU A 379  ? 0.2039 0.1944 0.2126 0.0141  0.0206  0.0297  377  GLU A OE2 
2736  N N   . ILE A 380  ? 0.1905 0.1860 0.1998 0.0151  0.0190  0.0347  378  ILE A N   
2737  C CA  . ILE A 380  ? 0.1948 0.1935 0.2036 0.0157  0.0189  0.0369  378  ILE A CA  
2738  C C   . ILE A 380  ? 0.2080 0.2072 0.2115 0.0168  0.0193  0.0338  378  ILE A C   
2739  O O   . ILE A 380  ? 0.1943 0.1981 0.1951 0.0180  0.0200  0.0347  378  ILE A O   
2740  C CB  . ILE A 380  ? 0.2045 0.2009 0.2180 0.0147  0.0174  0.0383  378  ILE A CB  
2741  C CG1 . ILE A 380  ? 0.1929 0.1885 0.2126 0.0137  0.0167  0.0412  378  ILE A CG1 
2742  C CG2 . ILE A 380  ? 0.2059 0.2058 0.2191 0.0154  0.0172  0.0408  378  ILE A CG2 
2743  C CD1 . ILE A 380  ? 0.2194 0.2201 0.2406 0.0139  0.0175  0.0460  378  ILE A CD1 
2744  N N   . LYS A 381  ? 0.1865 0.1814 0.1886 0.0164  0.0187  0.0299  379  LYS A N   
2745  C CA  . LYS A 381  ? 0.1973 0.1922 0.1949 0.0172  0.0188  0.0268  379  LYS A CA  
2746  C C   . LYS A 381  ? 0.1931 0.1909 0.1874 0.0185  0.0199  0.0257  379  LYS A C   
2747  O O   . LYS A 381  ? 0.1936 0.1946 0.1850 0.0197  0.0201  0.0251  379  LYS A O   
2748  C CB  . LYS A 381  ? 0.1967 0.1869 0.1939 0.0163  0.0181  0.0233  379  LYS A CB  
2749  C CG  . LYS A 381  ? 0.1989 0.1888 0.1922 0.0170  0.0180  0.0203  379  LYS A CG  
2750  C CD  . LYS A 381  ? 0.1999 0.1857 0.1933 0.0160  0.0173  0.0175  379  LYS A CD  
2751  C CE  . LYS A 381  ? 0.2338 0.2195 0.2240 0.0165  0.0170  0.0149  379  LYS A CE  
2752  N NZ  . LYS A 381  ? 0.2042 0.1866 0.1945 0.0154  0.0164  0.0125  379  LYS A NZ  
2753  N N   . ARG A 382  ? 0.1987 0.1956 0.1936 0.0183  0.0203  0.0254  380  ARG A N   
2754  C CA  . ARG A 382  ? 0.2093 0.2084 0.2015 0.0195  0.0211  0.0237  380  ARG A CA  
2755  C C   . ARG A 382  ? 0.1825 0.1880 0.1737 0.0210  0.0220  0.0260  380  ARG A C   
2756  O O   . ARG A 382  ? 0.2061 0.2147 0.1943 0.0225  0.0224  0.0240  380  ARG A O   
2757  C CB  . ARG A 382  ? 0.2256 0.2228 0.2193 0.0190  0.0214  0.0235  380  ARG A CB  
2758  C CG  . ARG A 382  ? 0.2799 0.2787 0.2715 0.0203  0.0219  0.0213  380  ARG A CG  
2759  C CD  . ARG A 382  ? 0.4596 0.4546 0.4494 0.0202  0.0211  0.0175  380  ARG A CD  
2760  N NE  . ARG A 382  ? 0.4695 0.4668 0.4567 0.0216  0.0210  0.0155  380  ARG A NE  
2761  C CZ  . ARG A 382  ? 0.5232 0.5177 0.5090 0.0216  0.0201  0.0125  380  ARG A CZ  
2762  N NH1 . ARG A 382  ? 0.5951 0.5850 0.5819 0.0201  0.0193  0.0115  380  ARG A NH1 
2763  N NH2 . ARG A 382  ? 0.4442 0.4413 0.4280 0.0230  0.0199  0.0105  380  ARG A NH2 
2764  N N   . ALA A 383  ? 0.1992 0.2074 0.1934 0.0205  0.0223  0.0302  381  ALA A N   
2765  C CA  . ALA A 383  ? 0.1923 0.2076 0.1857 0.0217  0.0233  0.0330  381  ALA A CA  
2766  C C   . ALA A 383  ? 0.1923 0.2106 0.1832 0.0226  0.0230  0.0328  381  ALA A C   
2767  O O   . ALA A 383  ? 0.2124 0.2367 0.2006 0.0242  0.0238  0.0325  381  ALA A O   
2768  C CB  . ALA A 383  ? 0.2117 0.2290 0.2095 0.0207  0.0235  0.0382  381  ALA A CB  
2769  N N   . GLN A 384  ? 0.1912 0.2058 0.1831 0.0216  0.0219  0.0328  382  GLN A N   
2770  C CA  . GLN A 384  ? 0.2051 0.2223 0.1948 0.0224  0.0215  0.0325  382  GLN A CA  
2771  C C   . GLN A 384  ? 0.2108 0.2277 0.1962 0.0237  0.0215  0.0275  382  GLN A C   
2772  O O   . GLN A 384  ? 0.2302 0.2524 0.2128 0.0252  0.0218  0.0269  382  GLN A O   
2773  C CB  . GLN A 384  ? 0.1889 0.2020 0.1811 0.0211  0.0203  0.0333  382  GLN A CB  
2774  C CG  . GLN A 384  ? 0.2000 0.2143 0.1971 0.0201  0.0199  0.0384  382  GLN A CG  
2775  C CD  . GLN A 384  ? 0.2114 0.2221 0.2113 0.0191  0.0185  0.0389  382  GLN A CD  
2776  O OE1 . GLN A 384  ? 0.2379 0.2444 0.2364 0.0189  0.0179  0.0352  382  GLN A OE1 
2777  N NE2 . GLN A 384  ? 0.2264 0.2390 0.2306 0.0185  0.0179  0.0437  382  GLN A NE2 
2778  N N   . LEU A 385  ? 0.1977 0.2089 0.1830 0.0231  0.0211  0.0240  383  LEU A N   
2779  C CA  . LEU A 385  ? 0.2126 0.2230 0.1948 0.0241  0.0208  0.0194  383  LEU A CA  
2780  C C   . LEU A 385  ? 0.2078 0.2235 0.1881 0.0260  0.0216  0.0182  383  LEU A C   
2781  O O   . LEU A 385  ? 0.2221 0.2406 0.1998 0.0275  0.0213  0.0154  383  LEU A O   
2782  C CB  . LEU A 385  ? 0.2166 0.2206 0.1996 0.0230  0.0202  0.0167  383  LEU A CB  
2783  C CG  . LEU A 385  ? 0.2565 0.2555 0.2407 0.0215  0.0192  0.0162  383  LEU A CG  
2784  C CD1 . LEU A 385  ? 0.2503 0.2445 0.2351 0.0205  0.0189  0.0140  383  LEU A CD1 
2785  C CD2 . LEU A 385  ? 0.2836 0.2831 0.2658 0.0220  0.0185  0.0143  383  LEU A CD2 
2786  N N   . ASP A 386  ? 0.2125 0.2299 0.1942 0.0260  0.0225  0.0201  384  ASP A N   
2787  C CA  . ASP A 386  ? 0.2231 0.2454 0.2034 0.0278  0.0234  0.0186  384  ASP A CA  
2788  C C   . ASP A 386  ? 0.2292 0.2602 0.2083 0.0292  0.0243  0.0212  384  ASP A C   
2789  O O   . ASP A 386  ? 0.2383 0.2748 0.2161 0.0309  0.0251  0.0199  384  ASP A O   
2790  C CB  . ASP A 386  ? 0.2400 0.2602 0.2225 0.0273  0.0239  0.0192  384  ASP A CB  
2791  C CG  . ASP A 386  ? 0.3121 0.3253 0.2953 0.0264  0.0230  0.0160  384  ASP A CG  
2792  O OD1 . ASP A 386  ? 0.3173 0.3275 0.2992 0.0264  0.0220  0.0130  384  ASP A OD1 
2793  O OD2 . ASP A 386  ? 0.3269 0.3376 0.3120 0.0256  0.0232  0.0166  384  ASP A OD2 
2794  N N   . GLY A 387  ? 0.2189 0.2516 0.1986 0.0284  0.0242  0.0249  385  GLY A N   
2795  C CA  . GLY A 387  ? 0.2103 0.2519 0.1887 0.0296  0.0249  0.0279  385  GLY A CA  
2796  C C   . GLY A 387  ? 0.2304 0.2775 0.2103 0.0299  0.0263  0.0313  385  GLY A C   
2797  O O   . GLY A 387  ? 0.2468 0.3023 0.2246 0.0316  0.0272  0.0315  385  GLY A O   
2798  N N   . LEU A 388  ? 0.2227 0.2655 0.2061 0.0282  0.0264  0.0338  386  LEU A N   
2799  C CA  . LEU A 388  ? 0.2389 0.2864 0.2240 0.0284  0.0276  0.0367  386  LEU A CA  
2800  C C   . LEU A 388  ? 0.2340 0.2870 0.2218 0.0276  0.0280  0.0433  386  LEU A C   
2801  O O   . LEU A 388  ? 0.2543 0.3062 0.2431 0.0266  0.0271  0.0458  386  LEU A O   
2802  C CB  . LEU A 388  ? 0.2285 0.2694 0.2164 0.0272  0.0275  0.0357  386  LEU A CB  
2803  C CG  . LEU A 388  ? 0.2352 0.2718 0.2208 0.0282  0.0271  0.0296  386  LEU A CG  
2804  C CD1 . LEU A 388  ? 0.2533 0.2835 0.2414 0.0269  0.0269  0.0289  386  LEU A CD1 
2805  C CD2 . LEU A 388  ? 0.2516 0.2950 0.2345 0.0307  0.0280  0.0267  386  LEU A CD2 
2806  N N   . ALA A 389  ? 0.2539 0.3130 0.2430 0.0279  0.0293  0.0464  387  ALA A N   
2807  C CA  . ALA A 389  ? 0.2693 0.3356 0.2607 0.0274  0.0297  0.0531  387  ALA A CA  
2808  C C   . ALA A 389  ? 0.2400 0.3006 0.2368 0.0249  0.0285  0.0575  387  ALA A C   
2809  O O   . ALA A 389  ? 0.2745 0.3384 0.2733 0.0242  0.0280  0.0623  387  ALA A O   
2810  C CB  . ALA A 389  ? 0.2666 0.3405 0.2588 0.0281  0.0313  0.0554  387  ALA A CB  
2811  N N   . ASP A 390  ? 0.2141 0.2664 0.2135 0.0236  0.0279  0.0558  388  ASP A N   
2812  C CA  . ASP A 390  ? 0.2333 0.2805 0.2385 0.0214  0.0266  0.0594  388  ASP A CA  
2813  C C   . ASP A 390  ? 0.2149 0.2529 0.2209 0.0206  0.0259  0.0551  388  ASP A C   
2814  O O   . ASP A 390  ? 0.2197 0.2556 0.2219 0.0216  0.0264  0.0501  388  ASP A O   
2815  C CB  . ASP A 390  ? 0.2383 0.2909 0.2482 0.0206  0.0272  0.0657  388  ASP A CB  
2816  C CG  . ASP A 390  ? 0.2390 0.2894 0.2553 0.0186  0.0257  0.0710  388  ASP A CG  
2817  O OD1 . ASP A 390  ? 0.2617 0.3040 0.2803 0.0175  0.0241  0.0690  388  ASP A OD1 
2818  O OD2 . ASP A 390  ? 0.2972 0.3545 0.3166 0.0182  0.0259  0.0772  388  ASP A OD2 
2819  N N   . PHE A 391  ? 0.1957 0.2286 0.2067 0.0188  0.0247  0.0570  389  PHE A N   
2820  C CA  . PHE A 391  ? 0.2156 0.2405 0.2277 0.0179  0.0239  0.0533  389  PHE A CA  
2821  C C   . PHE A 391  ? 0.2058 0.2309 0.2204 0.0175  0.0245  0.0543  389  PHE A C   
2822  O O   . PHE A 391  ? 0.2098 0.2400 0.2273 0.0172  0.0250  0.0590  389  PHE A O   
2823  C CB  . PHE A 391  ? 0.2190 0.2386 0.2356 0.0164  0.0221  0.0544  389  PHE A CB  
2824  C CG  . PHE A 391  ? 0.1889 0.2082 0.2035 0.0167  0.0214  0.0535  389  PHE A CG  
2825  C CD1 . PHE A 391  ? 0.2034 0.2191 0.2135 0.0174  0.0213  0.0483  389  PHE A CD1 
2826  C CD2 . PHE A 391  ? 0.2050 0.2282 0.2223 0.0165  0.0209  0.0582  389  PHE A CD2 
2827  C CE1 . PHE A 391  ? 0.2181 0.2337 0.2263 0.0178  0.0207  0.0474  389  PHE A CE1 
2828  C CE2 . PHE A 391  ? 0.2168 0.2399 0.2320 0.0170  0.0203  0.0574  389  PHE A CE2 
2829  C CZ  . PHE A 391  ? 0.2125 0.2318 0.2232 0.0176  0.0202  0.0519  389  PHE A CZ  
2830  N N   . PRO A 392  ? 0.1919 0.2118 0.2052 0.0174  0.0244  0.0501  390  PRO A N   
2831  C CA  . PRO A 392  ? 0.2000 0.2195 0.2162 0.0168  0.0247  0.0509  390  PRO A CA  
2832  C C   . PRO A 392  ? 0.1928 0.2074 0.2147 0.0149  0.0232  0.0524  390  PRO A C   
2833  O O   . PRO A 392  ? 0.2000 0.2133 0.2246 0.0142  0.0231  0.0528  390  PRO A O   
2834  C CB  . PRO A 392  ? 0.1846 0.2007 0.1967 0.0176  0.0250  0.0455  390  PRO A CB  
2835  C CG  . PRO A 392  ? 0.1888 0.2000 0.1987 0.0173  0.0240  0.0422  390  PRO A CG  
2836  C CD  . PRO A 392  ? 0.1942 0.2091 0.2036 0.0177  0.0239  0.0447  390  PRO A CD  
2837  N N   . VAL A 393  ? 0.1927 0.2046 0.2168 0.0141  0.0219  0.0530  391  VAL A N   
2838  C CA  . VAL A 393  ? 0.1842 0.1918 0.2144 0.0125  0.0201  0.0541  391  VAL A CA  
2839  C C   . VAL A 393  ? 0.2038 0.2139 0.2384 0.0120  0.0193  0.0588  391  VAL A C   
2840  O O   . VAL A 393  ? 0.2098 0.2238 0.2418 0.0128  0.0199  0.0604  391  VAL A O   
2841  C CB  . VAL A 393  ? 0.1832 0.1843 0.2124 0.0121  0.0190  0.0492  391  VAL A CB  
2842  C CG1 . VAL A 393  ? 0.2074 0.2061 0.2332 0.0123  0.0196  0.0451  391  VAL A CG1 
2843  C CG2 . VAL A 393  ? 0.1994 0.2001 0.2250 0.0128  0.0189  0.0473  391  VAL A CG2 
2844  N N   . PHE A 394  ? 0.1950 0.2028 0.2368 0.0106  0.0177  0.0612  392  PHE A N   
2845  C CA  . PHE A 394  ? 0.1907 0.1996 0.2379 0.0099  0.0163  0.0655  392  PHE A CA  
2846  C C   . PHE A 394  ? 0.1914 0.1969 0.2372 0.0101  0.0153  0.0625  392  PHE A C   
2847  O O   . PHE A 394  ? 0.2015 0.2028 0.2433 0.0105  0.0154  0.0571  392  PHE A O   
2848  C CB  . PHE A 394  ? 0.2070 0.2137 0.2631 0.0083  0.0146  0.0681  392  PHE A CB  
2849  C CG  . PHE A 394  ? 0.1998 0.2102 0.2578 0.0080  0.0155  0.0714  392  PHE A CG  
2850  C CD1 . PHE A 394  ? 0.2257 0.2434 0.2838 0.0083  0.0167  0.0770  392  PHE A CD1 
2851  C CD2 . PHE A 394  ? 0.2051 0.2125 0.2644 0.0075  0.0154  0.0689  392  PHE A CD2 
2852  C CE1 . PHE A 394  ? 0.2028 0.2247 0.2625 0.0080  0.0178  0.0801  392  PHE A CE1 
2853  C CE2 . PHE A 394  ? 0.1975 0.2087 0.2586 0.0072  0.0163  0.0721  392  PHE A CE2 
2854  C CZ  . PHE A 394  ? 0.1904 0.2088 0.2518 0.0075  0.0176  0.0776  392  PHE A CZ  
2855  N N   . THR A 395  ? 0.1944 0.2019 0.2432 0.0100  0.0144  0.0663  393  THR A N   
2856  C CA  . THR A 395  ? 0.2141 0.2188 0.2621 0.0102  0.0134  0.0640  393  THR A CA  
2857  C C   . THR A 395  ? 0.2312 0.2324 0.2879 0.0091  0.0108  0.0654  393  THR A C   
2858  O O   . THR A 395  ? 0.2171 0.2153 0.2740 0.0093  0.0097  0.0628  393  THR A O   
2859  C CB  . THR A 395  ? 0.2245 0.2345 0.2683 0.0112  0.0143  0.0663  393  THR A CB  
2860  O OG1 . THR A 395  ? 0.2253 0.2407 0.2737 0.0107  0.0141  0.0733  393  THR A OG1 
2861  C CG2 . THR A 395  ? 0.2315 0.2444 0.2669 0.0126  0.0165  0.0635  393  THR A CG2 
2862  N N   . ARG A 396  ? 0.2209 0.2224 0.2850 0.0080  0.0097  0.0694  394  ARG A N   
2863  C CA  . ARG A 396  ? 0.2436 0.2411 0.3170 0.0070  0.0070  0.0700  394  ARG A CA  
2864  C C   . ARG A 396  ? 0.2217 0.2152 0.2981 0.0063  0.0062  0.0666  394  ARG A C   
2865  O O   . ARG A 396  ? 0.2188 0.2143 0.2947 0.0060  0.0073  0.0681  394  ARG A O   
2866  C CB  . ARG A 396  ? 0.2352 0.2364 0.3166 0.0060  0.0057  0.0776  394  ARG A CB  
2867  C CG  . ARG A 396  ? 0.2321 0.2376 0.3114 0.0066  0.0060  0.0814  394  ARG A CG  
2868  C CD  . ARG A 396  ? 0.2915 0.3001 0.3804 0.0054  0.0043  0.0892  394  ARG A CD  
2869  N NE  . ARG A 396  ? 0.3174 0.3320 0.4037 0.0058  0.0050  0.0940  394  ARG A NE  
2870  C CZ  . ARG A 396  ? 0.3791 0.3940 0.4708 0.0055  0.0030  0.0974  394  ARG A CZ  
2871  N NH1 . ARG A 396  ? 0.4093 0.4185 0.5101 0.0047  0.0000  0.0968  394  ARG A NH1 
2872  N NH2 . ARG A 396  ? 0.3414 0.3624 0.4295 0.0060  0.0038  0.1014  394  ARG A NH2 
2873  N N   . LYS A 397  ? 0.2328 0.2210 0.3122 0.0062  0.0044  0.0620  395  LYS A N   
2874  C CA  . LYS A 397  ? 0.2298 0.2146 0.3114 0.0057  0.0037  0.0580  395  LYS A CA  
2875  C C   . LYS A 397  ? 0.2290 0.2145 0.3189 0.0045  0.0024  0.0623  395  LYS A C   
2876  O O   . LYS A 397  ? 0.2157 0.2007 0.3053 0.0042  0.0029  0.0609  395  LYS A O   
2877  C CB  . LYS A 397  ? 0.2755 0.2555 0.3599 0.0058  0.0017  0.0525  395  LYS A CB  
2878  C CG  . LYS A 397  ? 0.2544 0.2315 0.3381 0.0057  0.0013  0.0470  395  LYS A CG  
2879  C CD  . LYS A 397  ? 0.2610 0.2362 0.3548 0.0048  -0.0012 0.0475  395  LYS A CD  
2880  C CE  . LYS A 397  ? 0.2433 0.2164 0.3359 0.0047  -0.0014 0.0419  395  LYS A CE  
2881  N NZ  . LYS A 397  ? 0.2607 0.2319 0.3636 0.0039  -0.0042 0.0417  395  LYS A NZ  
2882  N N   . ILE A 398  ? 0.2232 0.2101 0.3208 0.0039  0.0009  0.0678  396  ILE A N   
2883  C CA  . ILE A 398  ? 0.2242 0.2119 0.3309 0.0026  -0.0006 0.0723  396  ILE A CA  
2884  C C   . ILE A 398  ? 0.1975 0.1901 0.3003 0.0024  0.0018  0.0762  396  ILE A C   
2885  O O   . ILE A 398  ? 0.2246 0.2173 0.3325 0.0015  0.0012  0.0780  396  ILE A O   
2886  C CB  . ILE A 398  ? 0.2639 0.2521 0.3801 0.0019  -0.0031 0.0778  396  ILE A CB  
2887  C CG1 . ILE A 398  ? 0.2985 0.2858 0.4262 0.0004  -0.0055 0.0813  396  ILE A CG1 
2888  C CG2 . ILE A 398  ? 0.2418 0.2360 0.3544 0.0021  -0.0014 0.0840  396  ILE A CG2 
2889  C CD1 . ILE A 398  ? 0.3347 0.3208 0.4735 -0.0003 -0.0087 0.0851  396  ILE A CD1 
2890  N N   . HIS A 399  ? 0.2323 0.2290 0.3262 0.0034  0.0044  0.0771  397  HIS A N   
2891  C CA  . HIS A 399  ? 0.2305 0.2323 0.3203 0.0036  0.0068  0.0799  397  HIS A CA  
2892  C C   . HIS A 399  ? 0.1920 0.1911 0.2782 0.0038  0.0077  0.0748  397  HIS A C   
2893  O O   . HIS A 399  ? 0.2100 0.2110 0.2984 0.0032  0.0081  0.0770  397  HIS A O   
2894  C CB  . HIS A 399  ? 0.2207 0.2276 0.3018 0.0048  0.0093  0.0810  397  HIS A CB  
2895  C CG  . HIS A 399  ? 0.2016 0.2127 0.2861 0.0046  0.0087  0.0871  397  HIS A CG  
2896  N ND1 . HIS A 399  ? 0.2263 0.2422 0.3041 0.0057  0.0103  0.0882  397  HIS A ND1 
2897  C CD2 . HIS A 399  ? 0.2660 0.2775 0.3603 0.0033  0.0064  0.0926  397  HIS A CD2 
2898  C CE1 . HIS A 399  ? 0.2370 0.2563 0.3198 0.0051  0.0092  0.0942  397  HIS A CE1 
2899  N NE2 . HIS A 399  ? 0.2502 0.2668 0.3433 0.0036  0.0068  0.0972  397  HIS A NE2 
2900  N N   . THR A 400  ? 0.1978 0.1928 0.2787 0.0045  0.0078  0.0682  398  THR A N   
2901  C CA  . THR A 400  ? 0.1783 0.1706 0.2564 0.0045  0.0082  0.0634  398  THR A CA  
2902  C C   . THR A 400  ? 0.1940 0.1836 0.2808 0.0033  0.0060  0.0635  398  THR A C   
2903  O O   . THR A 400  ? 0.1838 0.1738 0.2705 0.0030  0.0065  0.0632  398  THR A O   
2904  C CB  . THR A 400  ? 0.2000 0.1886 0.2720 0.0053  0.0084  0.0569  398  THR A CB  
2905  O OG1 . THR A 400  ? 0.2033 0.1947 0.2672 0.0065  0.0105  0.0568  398  THR A OG1 
2906  C CG2 . THR A 400  ? 0.1888 0.1747 0.2586 0.0052  0.0085  0.0521  398  THR A CG2 
2907  N N   . ASP A 401  ? 0.1938 0.1808 0.2886 0.0026  0.0034  0.0640  399  ASP A N   
2908  C CA  . ASP A 401  ? 0.1908 0.1752 0.2948 0.0015  0.0009  0.0637  399  ASP A CA  
2909  C C   . ASP A 401  ? 0.1907 0.1787 0.2998 0.0005  0.0011  0.0700  399  ASP A C   
2910  O O   . ASP A 401  ? 0.1970 0.1841 0.3092 -0.0001 0.0005  0.0692  399  ASP A O   
2911  C CB  . ASP A 401  ? 0.2014 0.1825 0.3139 0.0012  -0.0022 0.0631  399  ASP A CB  
2912  C CG  . ASP A 401  ? 0.2613 0.2388 0.3700 0.0021  -0.0027 0.0560  399  ASP A CG  
2913  O OD1 . ASP A 401  ? 0.2484 0.2251 0.3501 0.0026  -0.0014 0.0511  399  ASP A OD1 
2914  O OD2 . ASP A 401  ? 0.2709 0.2466 0.3839 0.0022  -0.0045 0.0555  399  ASP A OD2 
2915  N N   . VAL A 402  ? 0.2155 0.2079 0.3258 0.0004  0.0018  0.0765  400  VAL A N   
2916  C CA  . VAL A 402  ? 0.2062 0.2031 0.3211 -0.0006 0.0022  0.0831  400  VAL A CA  
2917  C C   . VAL A 402  ? 0.1999 0.1997 0.3073 0.0000  0.0050  0.0820  400  VAL A C   
2918  O O   . VAL A 402  ? 0.2028 0.2038 0.3142 -0.0008 0.0049  0.0838  400  VAL A O   
2919  C CB  . VAL A 402  ? 0.2090 0.2112 0.3260 -0.0008 0.0026  0.0904  400  VAL A CB  
2920  C CG1 . VAL A 402  ? 0.2049 0.2133 0.3255 -0.0018 0.0035  0.0974  400  VAL A CG1 
2921  C CG2 . VAL A 402  ? 0.2533 0.2524 0.3794 -0.0016 -0.0006 0.0919  400  VAL A CG2 
2922  N N   . SER A 403  ? 0.2201 0.2213 0.3172 0.0014  0.0074  0.0791  401  SER A N   
2923  C CA  . SER A 403  ? 0.2103 0.2138 0.3004 0.0022  0.0099  0.0773  401  SER A CA  
2924  C C   . SER A 403  ? 0.2163 0.2154 0.3078 0.0018  0.0089  0.0728  401  SER A C   
2925  O O   . SER A 403  ? 0.1986 0.1997 0.2907 0.0015  0.0097  0.0741  401  SER A O   
2926  C CB  . SER A 403  ? 0.2219 0.2259 0.3016 0.0038  0.0120  0.0737  401  SER A CB  
2927  O OG  . SER A 403  ? 0.2044 0.2097 0.2779 0.0046  0.0139  0.0711  401  SER A OG  
2928  N N   . TYR A 404  ? 0.1965 0.1901 0.2889 0.0017  0.0071  0.0677  402  TYR A N   
2929  C CA  . TYR A 404  ? 0.1996 0.1896 0.2932 0.0013  0.0060  0.0631  402  TYR A CA  
2930  C C   . TYR A 404  ? 0.1928 0.1831 0.2958 -0.0001 0.0043  0.0665  402  TYR A C   
2931  O O   . TYR A 404  ? 0.1890 0.1799 0.2918 -0.0003 0.0048  0.0659  402  TYR A O   
2932  C CB  . TYR A 404  ? 0.1779 0.1630 0.2716 0.0015  0.0043  0.0574  402  TYR A CB  
2933  C CG  . TYR A 404  ? 0.1912 0.1734 0.2836 0.0014  0.0035  0.0518  402  TYR A CG  
2934  C CD1 . TYR A 404  ? 0.1856 0.1662 0.2858 0.0004  0.0013  0.0513  402  TYR A CD1 
2935  C CD2 . TYR A 404  ? 0.1834 0.1647 0.2672 0.0023  0.0049  0.0471  402  TYR A CD2 
2936  C CE1 . TYR A 404  ? 0.1997 0.1783 0.2988 0.0004  0.0005  0.0462  402  TYR A CE1 
2937  C CE2 . TYR A 404  ? 0.1759 0.1552 0.2586 0.0021  0.0042  0.0424  402  TYR A CE2 
2938  C CZ  . TYR A 404  ? 0.1802 0.1583 0.2703 0.0012  0.0020  0.0418  402  TYR A CZ  
2939  O OH  . TYR A 404  ? 0.2103 0.1872 0.2993 0.0011  0.0013  0.0372  402  TYR A OH  
2940  N N   . ILE A 405  ? 0.2002 0.1904 0.3122 -0.0010 0.0022  0.0702  403  ILE A N   
2941  C CA  . ILE A 405  ? 0.1944 0.1846 0.3166 -0.0024 0.0002  0.0734  403  ILE A CA  
2942  C C   . ILE A 405  ? 0.1964 0.1922 0.3184 -0.0028 0.0022  0.0793  403  ILE A C   
2943  O O   . ILE A 405  ? 0.2103 0.2064 0.3362 -0.0035 0.0017  0.0799  403  ILE A O   
2944  C CB  . ILE A 405  ? 0.2184 0.2068 0.3508 -0.0033 -0.0028 0.0762  403  ILE A CB  
2945  C CG1 . ILE A 405  ? 0.2540 0.2370 0.3867 -0.0028 -0.0048 0.0693  403  ILE A CG1 
2946  C CG2 . ILE A 405  ? 0.2458 0.2344 0.3898 -0.0049 -0.0051 0.0801  403  ILE A CG2 
2947  C CD1 . ILE A 405  ? 0.2953 0.2764 0.4358 -0.0031 -0.0073 0.0711  403  ILE A CD1 
2948  N N   . ALA A 406  ? 0.2113 0.2121 0.3285 -0.0021 0.0045  0.0834  404  ALA A N   
2949  C CA  . ALA A 406  ? 0.2084 0.2156 0.3244 -0.0022 0.0067  0.0885  404  ALA A CA  
2950  C C   . ALA A 406  ? 0.2019 0.2091 0.3114 -0.0014 0.0085  0.0845  404  ALA A C   
2951  O O   . ALA A 406  ? 0.2162 0.2263 0.3285 -0.0020 0.0090  0.0871  404  ALA A O   
2952  C CB  . ALA A 406  ? 0.2115 0.2244 0.3221 -0.0013 0.0089  0.0922  404  ALA A CB  
2953  N N   . CYS A 407  ? 0.2007 0.2049 0.3018 -0.0002 0.0094  0.0783  405  CYS A N   
2954  C CA  . CYS A 407  ? 0.1919 0.1959 0.2870 0.0006  0.0109  0.0746  405  CYS A CA  
2955  C C   . CYS A 407  ? 0.2007 0.2007 0.3007 -0.0004 0.0089  0.0718  405  CYS A C   
2956  O O   . CYS A 407  ? 0.1935 0.1948 0.2923 -0.0003 0.0097  0.0713  405  CYS A O   
2957  C CB  . CYS A 407  ? 0.1998 0.2018 0.2853 0.0020  0.0122  0.0693  405  CYS A CB  
2958  S SG  . CYS A 407  ? 0.2588 0.2667 0.3375 0.0035  0.0150  0.0722  405  CYS A SG  
2959  N N   . ALA A 408  ? 0.1987 0.1943 0.3047 -0.0012 0.0061  0.0698  406  ALA A N   
2960  C CA  . ALA A 408  ? 0.1953 0.1879 0.3071 -0.0022 0.0039  0.0673  406  ALA A CA  
2961  C C   . ALA A 408  ? 0.1856 0.1812 0.3054 -0.0034 0.0033  0.0728  406  ALA A C   
2962  O O   . ALA A 408  ? 0.2063 0.2014 0.3281 -0.0039 0.0027  0.0715  406  ALA A O   
2963  C CB  . ALA A 408  ? 0.2094 0.1972 0.3267 -0.0026 0.0008  0.0639  406  ALA A CB  
2964  N N   . ALA A 409  ? 0.2188 0.2178 0.3435 -0.0040 0.0033  0.0792  407  ALA A N   
2965  C CA  . ALA A 409  ? 0.2020 0.2047 0.3344 -0.0052 0.0030  0.0852  407  ALA A CA  
2966  C C   . ALA A 409  ? 0.2023 0.2095 0.3290 -0.0046 0.0058  0.0862  407  ALA A C   
2967  O O   . ALA A 409  ? 0.2221 0.2304 0.3535 -0.0054 0.0053  0.0876  407  ALA A O   
2968  C CB  . ALA A 409  ? 0.2259 0.2323 0.3638 -0.0060 0.0027  0.0923  407  ALA A CB  
2969  N N   . LYS A 410  ? 0.2123 0.2221 0.3292 -0.0030 0.0087  0.0851  408  LYS A N   
2970  C CA  . LYS A 410  ? 0.1878 0.2019 0.2991 -0.0021 0.0113  0.0853  408  LYS A CA  
2971  C C   . LYS A 410  ? 0.1827 0.1928 0.2918 -0.0019 0.0108  0.0798  408  LYS A C   
2972  O O   . LYS A 410  ? 0.2030 0.2154 0.3136 -0.0021 0.0113  0.0809  408  LYS A O   
2973  C CB  . LYS A 410  ? 0.2018 0.2188 0.3033 -0.0003 0.0141  0.0844  408  LYS A CB  
2974  C CG  . LYS A 410  ? 0.2210 0.2425 0.3165 0.0011  0.0168  0.0838  408  LYS A CG  
2975  C CD  . LYS A 410  ? 0.2416 0.2656 0.3282 0.0029  0.0191  0.0822  408  LYS A CD  
2976  C CE  . LYS A 410  ? 0.2223 0.2518 0.3098 0.0030  0.0199  0.0875  408  LYS A CE  
2977  N NZ  . LYS A 410  ? 0.2800 0.3175 0.3706 0.0028  0.0214  0.0933  408  LYS A NZ  
2978  N N   . LEU A 411  ? 0.1822 0.1868 0.2876 -0.0015 0.0097  0.0739  409  LEU A N   
2979  C CA  . LEU A 411  ? 0.1806 0.1818 0.2840 -0.0014 0.0090  0.0687  409  LEU A CA  
2980  C C   . LEU A 411  ? 0.1712 0.1711 0.2838 -0.0030 0.0065  0.0695  409  LEU A C   
2981  O O   . LEU A 411  ? 0.1795 0.1796 0.2919 -0.0031 0.0065  0.0682  409  LEU A O   
2982  C CB  . LEU A 411  ? 0.1906 0.1870 0.2891 -0.0009 0.0082  0.0628  409  LEU A CB  
2983  C CG  . LEU A 411  ? 0.1880 0.1854 0.2766 0.0007  0.0107  0.0609  409  LEU A CG  
2984  C CD1 . LEU A 411  ? 0.2006 0.1939 0.2854 0.0011  0.0098  0.0563  409  LEU A CD1 
2985  C CD2 . LEU A 411  ? 0.1876 0.1861 0.2712 0.0014  0.0121  0.0589  409  LEU A CD2 
2986  N N   . LEU A 412  ? 0.1744 0.1727 0.2954 -0.0041 0.0041  0.0714  410  LEU A N   
2987  C CA  . LEU A 412  ? 0.1858 0.1824 0.3161 -0.0055 0.0013  0.0715  410  LEU A CA  
2988  C C   . LEU A 412  ? 0.2165 0.2176 0.3518 -0.0064 0.0020  0.0770  410  LEU A C   
2989  O O   . LEU A 412  ? 0.2405 0.2406 0.3821 -0.0074 0.0001  0.0766  410  LEU A O   
2990  C CB  . LEU A 412  ? 0.2111 0.2045 0.3500 -0.0065 -0.0018 0.0717  410  LEU A CB  
2991  C CG  . LEU A 412  ? 0.1976 0.1861 0.3336 -0.0059 -0.0033 0.0648  410  LEU A CG  
2992  C CD1 . LEU A 412  ? 0.2594 0.2453 0.4039 -0.0066 -0.0061 0.0654  410  LEU A CD1 
2993  C CD2 . LEU A 412  ? 0.2387 0.2248 0.3743 -0.0059 -0.0047 0.0591  410  LEU A CD2 
2994  N N   . ALA A 413  ? 0.1887 0.1951 0.3211 -0.0059 0.0047  0.0821  411  ALA A N   
2995  C CA  . ALA A 413  ? 0.1904 0.2022 0.3265 -0.0064 0.0058  0.0872  411  ALA A CA  
2996  C C   . ALA A 413  ? 0.2315 0.2448 0.3608 -0.0053 0.0078  0.0844  411  ALA A C   
2997  O O   . ALA A 413  ? 0.2325 0.2502 0.3643 -0.0056 0.0088  0.0880  411  ALA A O   
2998  C CB  . ALA A 413  ? 0.2037 0.2217 0.3398 -0.0063 0.0078  0.0938  411  ALA A CB  
2999  N N   . ALA A 414  ? 0.2066 0.2163 0.3278 -0.0041 0.0083  0.0783  412  ALA A N   
3000  C CA  . ALA A 414  ? 0.2183 0.2294 0.3325 -0.0029 0.0102  0.0758  412  ALA A CA  
3001  C C   . ALA A 414  ? 0.2058 0.2119 0.3180 -0.0029 0.0086  0.0697  412  ALA A C   
3002  O O   . ALA A 414  ? 0.1952 0.2010 0.3003 -0.0018 0.0099  0.0665  412  ALA A O   
3003  C CB  . ALA A 414  ? 0.2356 0.2492 0.3408 -0.0011 0.0131  0.0753  412  ALA A CB  
3004  N N   . THR A 415  ? 0.2011 0.2036 0.3200 -0.0042 0.0056  0.0681  413  THR A N   
3005  C CA  . THR A 415  ? 0.2115 0.2101 0.3286 -0.0043 0.0039  0.0623  413  THR A CA  
3006  C C   . THR A 415  ? 0.2140 0.2140 0.3302 -0.0042 0.0043  0.0617  413  THR A C   
3007  O O   . THR A 415  ? 0.2356 0.2333 0.3482 -0.0039 0.0035  0.0570  413  THR A O   
3008  C CB  . THR A 415  ? 0.2422 0.2372 0.3671 -0.0055 0.0004  0.0603  413  THR A CB  
3009  O OG1 . THR A 415  ? 0.2658 0.2624 0.4005 -0.0069 -0.0010 0.0644  413  THR A OG1 
3010  C CG2 . THR A 415  ? 0.2373 0.2304 0.3628 -0.0054 -0.0001 0.0602  413  THR A CG2 
3011  N N   . ASP A 416  ? 0.2161 0.2203 0.3357 -0.0044 0.0055  0.0664  414  ASP A N   
3012  C CA  . ASP A 416  ? 0.2180 0.2239 0.3363 -0.0041 0.0060  0.0657  414  ASP A CA  
3013  C C   . ASP A 416  ? 0.2152 0.2219 0.3239 -0.0024 0.0085  0.0635  414  ASP A C   
3014  O O   . ASP A 416  ? 0.2895 0.2958 0.3957 -0.0021 0.0084  0.0611  414  ASP A O   
3015  C CB  . ASP A 416  ? 0.2551 0.2657 0.3799 -0.0048 0.0066  0.0713  414  ASP A CB  
3016  C CG  . ASP A 416  ? 0.3336 0.3491 0.4567 -0.0041 0.0094  0.0760  414  ASP A CG  
3017  O OD1 . ASP A 416  ? 0.3342 0.3490 0.4557 -0.0039 0.0097  0.0766  414  ASP A OD1 
3018  O OD2 . ASP A 416  ? 0.4258 0.4464 0.5491 -0.0036 0.0112  0.0791  414  ASP A OD2 
3019  N N   . VAL A 417  ? 0.2148 0.2224 0.3182 -0.0013 0.0104  0.0641  415  VAL A N   
3020  C CA  . VAL A 417  ? 0.2356 0.2443 0.3308 0.0004  0.0127  0.0622  415  VAL A CA  
3021  C C   . VAL A 417  ? 0.1985 0.2036 0.2871 0.0011  0.0127  0.0582  415  VAL A C   
3022  O O   . VAL A 417  ? 0.2117 0.2165 0.2940 0.0023  0.0138  0.0557  415  VAL A O   
3023  C CB  . VAL A 417  ? 0.3065 0.3210 0.4005 0.0015  0.0154  0.0661  415  VAL A CB  
3024  C CG1 . VAL A 417  ? 0.3186 0.3372 0.4187 0.0009  0.0156  0.0699  415  VAL A CG1 
3025  C CG2 . VAL A 417  ? 0.2475 0.2633 0.3420 0.0014  0.0160  0.0688  415  VAL A CG2 
3026  N N   . VAL A 418  ? 0.1800 0.1824 0.2700 0.0004  0.0114  0.0575  416  VAL A N   
3027  C CA  . VAL A 418  ? 0.1750 0.1739 0.2594 0.0009  0.0111  0.0535  416  VAL A CA  
3028  C C   . VAL A 418  ? 0.1811 0.1764 0.2696 -0.0004 0.0083  0.0508  416  VAL A C   
3029  O O   . VAL A 418  ? 0.1925 0.1878 0.2886 -0.0015 0.0066  0.0525  416  VAL A O   
3030  C CB  . VAL A 418  ? 0.1817 0.1816 0.2627 0.0017  0.0127  0.0548  416  VAL A CB  
3031  C CG1 . VAL A 418  ? 0.2158 0.2196 0.2922 0.0032  0.0153  0.0563  416  VAL A CG1 
3032  C CG2 . VAL A 418  ? 0.2149 0.2157 0.3023 0.0008  0.0119  0.0585  416  VAL A CG2 
3033  N N   . PHE A 419  ? 0.1763 0.1687 0.2599 -0.0001 0.0078  0.0464  417  PHE A N   
3034  C CA  . PHE A 419  ? 0.1779 0.1675 0.2645 -0.0009 0.0052  0.0431  417  PHE A CA  
3035  C C   . PHE A 419  ? 0.1703 0.1584 0.2551 -0.0006 0.0054  0.0423  417  PHE A C   
3036  O O   . PHE A 419  ? 0.1864 0.1735 0.2643 0.0002  0.0064  0.0399  417  PHE A O   
3037  C CB  . PHE A 419  ? 0.1756 0.1640 0.2580 -0.0008 0.0044  0.0386  417  PHE A CB  
3038  C CG  . PHE A 419  ? 0.1844 0.1707 0.2687 -0.0014 0.0020  0.0344  417  PHE A CG  
3039  C CD1 . PHE A 419  ? 0.1889 0.1746 0.2812 -0.0024 -0.0004 0.0340  417  PHE A CD1 
3040  C CD2 . PHE A 419  ? 0.1763 0.1615 0.2546 -0.0010 0.0021  0.0306  417  PHE A CD2 
3041  C CE1 . PHE A 419  ? 0.1942 0.1785 0.2886 -0.0027 -0.0028 0.0295  417  PHE A CE1 
3042  C CE2 . PHE A 419  ? 0.1870 0.1711 0.2670 -0.0014 -0.0001 0.0265  417  PHE A CE2 
3043  C CZ  . PHE A 419  ? 0.1851 0.1688 0.2730 -0.0022 -0.0025 0.0257  417  PHE A CZ  
3044  N N   . PRO A 420  ? 0.1671 0.1547 0.2581 -0.0012 0.0044  0.0445  418  PRO A N   
3045  C CA  . PRO A 420  ? 0.1832 0.1695 0.2727 -0.0008 0.0045  0.0441  418  PRO A CA  
3046  C C   . PRO A 420  ? 0.1773 0.1607 0.2660 -0.0009 0.0026  0.0387  418  PRO A C   
3047  O O   . PRO A 420  ? 0.1848 0.1672 0.2783 -0.0016 0.0003  0.0361  418  PRO A O   
3048  C CB  . PRO A 420  ? 0.1724 0.1595 0.2703 -0.0016 0.0035  0.0484  418  PRO A CB  
3049  C CG  . PRO A 420  ? 0.1537 0.1436 0.2558 -0.0022 0.0038  0.0522  418  PRO A CG  
3050  C CD  . PRO A 420  ? 0.1749 0.1638 0.2749 -0.0022 0.0031  0.0483  418  PRO A CD  
3051  N N   . GLN A 421  ? 0.1705 0.1530 0.2534 -0.0001 0.0036  0.0368  419  GLN A N   
3052  C CA  . GLN A 421  ? 0.1661 0.1466 0.2475 0.0000  0.0022  0.0318  419  GLN A CA  
3053  C C   . GLN A 421  ? 0.1612 0.1407 0.2430 0.0003  0.0023  0.0324  419  GLN A C   
3054  O O   . GLN A 421  ? 0.1885 0.1686 0.2647 0.0011  0.0043  0.0337  419  GLN A O   
3055  C CB  . GLN A 421  ? 0.1583 0.1391 0.2314 0.0005  0.0034  0.0288  419  GLN A CB  
3056  C CG  . GLN A 421  ? 0.1847 0.1668 0.2572 0.0002  0.0034  0.0288  419  GLN A CG  
3057  C CD  . GLN A 421  ? 0.1733 0.1559 0.2378 0.0008  0.0050  0.0276  419  GLN A CD  
3058  O OE1 . GLN A 421  ? 0.1946 0.1777 0.2550 0.0015  0.0070  0.0296  419  GLN A OE1 
3059  N NE2 . GLN A 421  ? 0.1888 0.1717 0.2516 0.0005  0.0039  0.0243  419  GLN A NE2 
3060  N N   . PHE A 422  ? 0.1585 0.1366 0.2474 -0.0002 0.0000  0.0314  420  PHE A N   
3061  C CA  . PHE A 422  ? 0.1532 0.1303 0.2440 0.0001  -0.0003 0.0327  420  PHE A CA  
3062  C C   . PHE A 422  ? 0.1592 0.1348 0.2466 0.0006  -0.0009 0.0275  420  PHE A C   
3063  O O   . PHE A 422  ? 0.1769 0.1514 0.2691 0.0004  -0.0033 0.0237  420  PHE A O   
3064  C CB  . PHE A 422  ? 0.1815 0.1580 0.2830 -0.0008 -0.0025 0.0353  420  PHE A CB  
3065  C CG  . PHE A 422  ? 0.1910 0.1696 0.2960 -0.0014 -0.0018 0.0409  420  PHE A CG  
3066  C CD1 . PHE A 422  ? 0.2117 0.1928 0.3134 -0.0011 0.0006  0.0458  420  PHE A CD1 
3067  C CD2 . PHE A 422  ? 0.1879 0.1664 0.2992 -0.0023 -0.0035 0.0410  420  PHE A CD2 
3068  C CE1 . PHE A 422  ? 0.2025 0.1864 0.3072 -0.0016 0.0014  0.0509  420  PHE A CE1 
3069  C CE2 . PHE A 422  ? 0.2039 0.1848 0.3186 -0.0029 -0.0028 0.0462  420  PHE A CE2 
3070  C CZ  . PHE A 422  ? 0.2069 0.1906 0.3181 -0.0026 -0.0002 0.0512  420  PHE A CZ  
3071  N N   . ALA A 423  ? 0.1666 0.1426 0.2460 0.0014  0.0012  0.0272  421  ALA A N   
3072  C CA  . ALA A 423  ? 0.1787 0.1539 0.2541 0.0019  0.0010  0.0227  421  ALA A CA  
3073  C C   . ALA A 423  ? 0.2024 0.1765 0.2813 0.0022  0.0003  0.0236  421  ALA A C   
3074  O O   . ALA A 423  ? 0.2080 0.1826 0.2848 0.0025  0.0018  0.0273  421  ALA A O   
3075  C CB  . ALA A 423  ? 0.1870 0.1632 0.2530 0.0025  0.0034  0.0224  421  ALA A CB  
3076  N N   . THR A 424  ? 0.1843 0.1571 0.2688 0.0021  -0.0021 0.0202  422  THR A N   
3077  C CA  . THR A 424  ? 0.2011 0.1726 0.2891 0.0024  -0.0030 0.0206  422  THR A CA  
3078  C C   . THR A 424  ? 0.1954 0.1659 0.2878 0.0026  -0.0055 0.0150  422  THR A C   
3079  O O   . THR A 424  ? 0.2129 0.1836 0.3094 0.0023  -0.0073 0.0120  422  THR A O   
3080  C CB  . THR A 424  ? 0.2197 0.1909 0.3153 0.0019  -0.0037 0.0262  422  THR A CB  
3081  O OG1 . THR A 424  ? 0.2199 0.1901 0.3184 0.0022  -0.0046 0.0268  422  THR A OG1 
3082  C CG2 . THR A 424  ? 0.2407 0.2112 0.3456 0.0011  -0.0064 0.0258  422  THR A CG2 
3083  N N   . HIS A 425  ? 0.1962 0.1661 0.2880 0.0033  -0.0057 0.0134  423  HIS A N   
3084  C CA  . HIS A 425  ? 0.1978 0.1669 0.2948 0.0037  -0.0082 0.0082  423  HIS A CA  
3085  C C   . HIS A 425  ? 0.2232 0.1903 0.3300 0.0036  -0.0104 0.0103  423  HIS A C   
3086  O O   . HIS A 425  ? 0.2476 0.2140 0.3600 0.0041  -0.0127 0.0060  423  HIS A O   
3087  C CB  . HIS A 425  ? 0.2144 0.1844 0.3046 0.0045  -0.0071 0.0044  423  HIS A CB  
3088  C CG  . HIS A 425  ? 0.2113 0.1834 0.2927 0.0045  -0.0053 0.0022  423  HIS A CG  
3089  N ND1 . HIS A 425  ? 0.2579 0.2308 0.3307 0.0048  -0.0029 0.0027  423  HIS A ND1 
3090  C CD2 . HIS A 425  ? 0.2259 0.1995 0.3063 0.0041  -0.0056 -0.0001 423  HIS A CD2 
3091  C CE1 . HIS A 425  ? 0.2546 0.2294 0.3217 0.0045  -0.0019 0.0009  423  HIS A CE1 
3092  N NE2 . HIS A 425  ? 0.2201 0.1955 0.2915 0.0042  -0.0035 -0.0008 423  HIS A NE2 
3093  N N   . ASN A 426  ? 0.2089 0.1756 0.3184 0.0030  -0.0099 0.0167  424  ASN A N   
3094  C CA  . ASN A 426  ? 0.2268 0.1921 0.3455 0.0028  -0.0118 0.0200  424  ASN A CA  
3095  C C   . ASN A 426  ? 0.2281 0.1923 0.3574 0.0020  -0.0147 0.0205  424  ASN A C   
3096  O O   . ASN A 426  ? 0.2215 0.1866 0.3514 0.0012  -0.0140 0.0242  424  ASN A O   
3097  C CB  . ASN A 426  ? 0.2360 0.2025 0.3515 0.0026  -0.0096 0.0269  424  ASN A CB  
3098  C CG  . ASN A 426  ? 0.2252 0.1907 0.3493 0.0023  -0.0115 0.0312  424  ASN A CG  
3099  O OD1 . ASN A 426  ? 0.2498 0.2139 0.3845 0.0017  -0.0143 0.0318  424  ASN A OD1 
3100  N ND2 . ASN A 426  ? 0.2501 0.2166 0.3702 0.0027  -0.0099 0.0345  424  ASN A ND2 
3101  N N   . ALA A 427  ? 0.2189 0.1813 0.3571 0.0023  -0.0180 0.0165  425  ALA A N   
3102  C CA  . ALA A 427  ? 0.2352 0.1964 0.3843 0.0016  -0.0211 0.0160  425  ALA A CA  
3103  C C   . ALA A 427  ? 0.2107 0.1714 0.3675 0.0004  -0.0218 0.0239  425  ALA A C   
3104  O O   . ALA A 427  ? 0.2250 0.1855 0.3886 -0.0005 -0.0234 0.0255  425  ALA A O   
3105  C CB  . ALA A 427  ? 0.2734 0.2329 0.4309 0.0024  -0.0247 0.0097  425  ALA A CB  
3106  N N   . GLN A 428  ? 0.2233 0.1842 0.3795 0.0004  -0.0208 0.0292  426  GLN A N   
3107  C CA  . GLN A 428  ? 0.2640 0.2256 0.4266 -0.0008 -0.0211 0.0375  426  GLN A CA  
3108  C C   . GLN A 428  ? 0.2227 0.1871 0.3787 -0.0015 -0.0182 0.0417  426  GLN A C   
3109  O O   . GLN A 428  ? 0.2242 0.1893 0.3868 -0.0026 -0.0191 0.0458  426  GLN A O   
3110  C CB  . GLN A 428  ? 0.2277 0.1897 0.3903 -0.0006 -0.0206 0.0419  426  GLN A CB  
3111  C CG  . GLN A 428  ? 0.2423 0.2050 0.4146 -0.0019 -0.0220 0.0503  426  GLN A CG  
3112  C CD  . GLN A 428  ? 0.3053 0.2718 0.4731 -0.0028 -0.0192 0.0571  426  GLN A CD  
3113  O OE1 . GLN A 428  ? 0.3076 0.2766 0.4638 -0.0022 -0.0157 0.0571  426  GLN A OE1 
3114  N NE2 . GLN A 428  ? 0.2732 0.2405 0.4508 -0.0042 -0.0209 0.0629  426  GLN A NE2 
3115  N N   . THR A 429  ? 0.2237 0.1899 0.3672 -0.0007 -0.0147 0.0407  427  THR A N   
3116  C CA  . THR A 429  ? 0.2169 0.1859 0.3538 -0.0011 -0.0119 0.0437  427  THR A CA  
3117  C C   . THR A 429  ? 0.2308 0.1992 0.3708 -0.0016 -0.0131 0.0409  427  THR A C   
3118  O O   . THR A 429  ? 0.2209 0.1909 0.3639 -0.0025 -0.0129 0.0453  427  THR A O   
3119  C CB  . THR A 429  ? 0.2304 0.2005 0.3541 0.0000  -0.0087 0.0411  427  THR A CB  
3120  O OG1 . THR A 429  ? 0.2305 0.2008 0.3515 0.0006  -0.0079 0.0425  427  THR A OG1 
3121  C CG2 . THR A 429  ? 0.2387 0.2119 0.3562 -0.0002 -0.0058 0.0449  427  THR A CG2 
3122  N N   . LEU A 430  ? 0.2105 0.1772 0.3499 -0.0010 -0.0145 0.0336  428  LEU A N   
3123  C CA  . LEU A 430  ? 0.2415 0.2080 0.3834 -0.0014 -0.0158 0.0302  428  LEU A CA  
3124  C C   . LEU A 430  ? 0.2380 0.2036 0.3927 -0.0026 -0.0188 0.0333  428  LEU A C   
3125  O O   . LEU A 430  ? 0.2279 0.1946 0.3844 -0.0034 -0.0187 0.0357  428  LEU A O   
3126  C CB  . LEU A 430  ? 0.2057 0.1712 0.3461 -0.0005 -0.0173 0.0219  428  LEU A CB  
3127  C CG  . LEU A 430  ? 0.2573 0.2234 0.3970 -0.0005 -0.0182 0.0165  428  LEU A CG  
3128  C CD1 . LEU A 430  ? 0.2982 0.2645 0.4341 0.0006  -0.0188 0.0090  428  LEU A CD1 
3129  C CD2 . LEU A 430  ? 0.2862 0.2512 0.4378 -0.0013 -0.0217 0.0162  428  LEU A CD2 
3130  N N   . ALA A 431  ? 0.2449 0.2084 0.4092 -0.0027 -0.0217 0.0333  429  ALA A N   
3131  C CA  . ALA A 431  ? 0.2541 0.2163 0.4320 -0.0038 -0.0251 0.0360  429  ALA A CA  
3132  C C   . ALA A 431  ? 0.2294 0.1938 0.4094 -0.0051 -0.0238 0.0451  429  ALA A C   
3133  O O   . ALA A 431  ? 0.2260 0.1907 0.4132 -0.0062 -0.0252 0.0474  429  ALA A O   
3134  C CB  . ALA A 431  ? 0.2506 0.2101 0.4383 -0.0036 -0.0284 0.0348  429  ALA A CB  
3135  N N   . ALA A 432  ? 0.2355 0.2019 0.4095 -0.0049 -0.0210 0.0502  430  ALA A N   
3136  C CA  . ALA A 432  ? 0.2427 0.2125 0.4181 -0.0060 -0.0194 0.0588  430  ALA A CA  
3137  C C   . ALA A 432  ? 0.2253 0.1973 0.3956 -0.0063 -0.0174 0.0592  430  ALA A C   
3138  O O   . ALA A 432  ? 0.2438 0.2176 0.4202 -0.0076 -0.0179 0.0645  430  ALA A O   
3139  C CB  . ALA A 432  ? 0.2469 0.2192 0.4147 -0.0055 -0.0165 0.0630  430  ALA A CB  
3140  N N   . ILE A 433  ? 0.2241 0.1962 0.3837 -0.0053 -0.0153 0.0538  431  ILE A N   
3141  C CA  . ILE A 433  ? 0.2063 0.1806 0.3607 -0.0054 -0.0134 0.0541  431  ILE A CA  
3142  C C   . ILE A 433  ? 0.2241 0.1967 0.3856 -0.0061 -0.0161 0.0508  431  ILE A C   
3143  O O   . ILE A 433  ? 0.2236 0.1981 0.3874 -0.0069 -0.0158 0.0538  431  ILE A O   
3144  C CB  . ILE A 433  ? 0.2211 0.1959 0.3620 -0.0041 -0.0104 0.0499  431  ILE A CB  
3145  C CG1 . ILE A 433  ? 0.2848 0.2619 0.4192 -0.0035 -0.0075 0.0541  431  ILE A CG1 
3146  C CG2 . ILE A 433  ? 0.2298 0.2062 0.3660 -0.0042 -0.0089 0.0488  431  ILE A CG2 
3147  C CD1 . ILE A 433  ? 0.2786 0.2558 0.4011 -0.0022 -0.0051 0.0500  431  ILE A CD1 
3148  N N   . TYR A 434  ? 0.2363 0.2058 0.4016 -0.0057 -0.0189 0.0443  432  TYR A N   
3149  C CA  . TYR A 434  ? 0.2272 0.1954 0.4000 -0.0063 -0.0219 0.0406  432  TYR A CA  
3150  C C   . TYR A 434  ? 0.2409 0.2092 0.4261 -0.0078 -0.0241 0.0465  432  TYR A C   
3151  O O   . TYR A 434  ? 0.2629 0.2320 0.4516 -0.0086 -0.0249 0.0468  432  TYR A O   
3152  C CB  . TYR A 434  ? 0.2461 0.2115 0.4224 -0.0054 -0.0249 0.0331  432  TYR A CB  
3153  C CG  . TYR A 434  ? 0.2571 0.2210 0.4436 -0.0059 -0.0288 0.0290  432  TYR A CG  
3154  C CD1 . TYR A 434  ? 0.2698 0.2349 0.4533 -0.0059 -0.0288 0.0251  432  TYR A CD1 
3155  C CD2 . TYR A 434  ? 0.3037 0.2651 0.5034 -0.0063 -0.0327 0.0287  432  TYR A CD2 
3156  C CE1 . TYR A 434  ? 0.2690 0.2331 0.4619 -0.0062 -0.0326 0.0209  432  TYR A CE1 
3157  C CE2 . TYR A 434  ? 0.2925 0.2526 0.5021 -0.0066 -0.0366 0.0245  432  TYR A CE2 
3158  C CZ  . TYR A 434  ? 0.3330 0.2945 0.5391 -0.0066 -0.0365 0.0205  432  TYR A CZ  
3159  O OH  . TYR A 434  ? 0.3449 0.3053 0.5610 -0.0068 -0.0405 0.0159  432  TYR A OH  
3160  N N   . HIS A 435  ? 0.2413 0.2091 0.4335 -0.0084 -0.0252 0.0514  433  HIS A N   
3161  C CA  . HIS A 435  ? 0.2547 0.2229 0.4593 -0.0100 -0.0274 0.0578  433  HIS A CA  
3162  C C   . HIS A 435  ? 0.2571 0.2298 0.4581 -0.0108 -0.0242 0.0657  433  HIS A C   
3163  O O   . HIS A 435  ? 0.2476 0.2216 0.4561 -0.0122 -0.0253 0.0697  433  HIS A O   
3164  C CB  . HIS A 435  ? 0.2793 0.2455 0.4939 -0.0104 -0.0301 0.0604  433  HIS A CB  
3165  C CG  . HIS A 435  ? 0.2994 0.2615 0.5217 -0.0098 -0.0342 0.0530  433  HIS A CG  
3166  N ND1 . HIS A 435  ? 0.3186 0.2786 0.5540 -0.0107 -0.0384 0.0516  433  HIS A ND1 
3167  C CD2 . HIS A 435  ? 0.2670 0.2269 0.4856 -0.0083 -0.0347 0.0461  433  HIS A CD2 
3168  C CE1 . HIS A 435  ? 0.3004 0.2572 0.5400 -0.0097 -0.0414 0.0439  433  HIS A CE1 
3169  N NE2 . HIS A 435  ? 0.2630 0.2199 0.4925 -0.0082 -0.0392 0.0405  433  HIS A NE2 
3170  N N   . MET A 436  ? 0.2384 0.2137 0.4280 -0.0099 -0.0203 0.0676  434  MET A N   
3171  C CA  . MET A 436  ? 0.2545 0.2347 0.4395 -0.0103 -0.0171 0.0740  434  MET A CA  
3172  C C   . MET A 436  ? 0.2273 0.2085 0.4096 -0.0105 -0.0163 0.0718  434  MET A C   
3173  O O   . MET A 436  ? 0.2523 0.2369 0.4375 -0.0114 -0.0155 0.0773  434  MET A O   
3174  C CB  . MET A 436  ? 0.2504 0.2330 0.4230 -0.0090 -0.0133 0.0746  434  MET A CB  
3175  C CG  . MET A 436  ? 0.2410 0.2293 0.4089 -0.0092 -0.0099 0.0809  434  MET A CG  
3176  S SD  . MET A 436  ? 0.2600 0.2505 0.4128 -0.0073 -0.0058 0.0795  434  MET A SD  
3177  C CE  . MET A 436  ? 0.2801 0.2705 0.4364 -0.0074 -0.0067 0.0830  434  MET A CE  
3178  N N   . ALA A 437  ? 0.2241 0.2028 0.4009 -0.0095 -0.0166 0.0640  435  ALA A N   
3179  C CA  . ALA A 437  ? 0.2675 0.2472 0.4407 -0.0095 -0.0158 0.0618  435  ALA A CA  
3180  C C   . ALA A 437  ? 0.3004 0.2791 0.4855 -0.0109 -0.0192 0.0621  435  ALA A C   
3181  O O   . ALA A 437  ? 0.2929 0.2737 0.4778 -0.0114 -0.0185 0.0634  435  ALA A O   
3182  C CB  . ALA A 437  ? 0.2760 0.2539 0.4402 -0.0082 -0.0153 0.0537  435  ALA A CB  
3183  N N   . GLY A 438  ? 0.3203 0.2960 0.5161 -0.0115 -0.0229 0.0609  436  GLY A N   
3184  C CA  . GLY A 438  ? 0.3352 0.3100 0.5439 -0.0129 -0.0265 0.0618  436  GLY A CA  
3185  C C   . GLY A 438  ? 0.3367 0.3093 0.5460 -0.0125 -0.0288 0.0537  436  GLY A C   
3186  O O   . GLY A 438  ? 0.3132 0.2851 0.5130 -0.0111 -0.0277 0.0473  436  GLY A O   
3187  N N   . LYS A 439  ? 0.3867 0.3586 0.6078 -0.0137 -0.0321 0.0542  437  LYS A N   
3188  C CA  . LYS A 439  ? 0.4366 0.4064 0.6611 -0.0134 -0.0352 0.0464  437  LYS A CA  
3189  C C   . LYS A 439  ? 0.3872 0.3592 0.6038 -0.0132 -0.0334 0.0440  437  LYS A C   
3190  O O   . LYS A 439  ? 0.4804 0.4517 0.6948 -0.0124 -0.0349 0.0365  437  LYS A O   
3191  C CB  . LYS A 439  ? 0.5104 0.4783 0.7516 -0.0149 -0.0400 0.0475  437  LYS A CB  
3192  N N   . ASP A 440  ? 0.3716 0.3468 0.5840 -0.0137 -0.0303 0.0502  438  ASP A N   
3193  C CA  . ASP A 440  ? 0.4297 0.4071 0.6349 -0.0134 -0.0286 0.0483  438  ASP A CA  
3194  C C   . ASP A 440  ? 0.4176 0.3954 0.6084 -0.0118 -0.0256 0.0440  438  ASP A C   
3195  O O   . ASP A 440  ? 0.4171 0.3961 0.6002 -0.0112 -0.0223 0.0474  438  ASP A O   
3196  C CB  . ASP A 440  ? 0.4488 0.4298 0.6542 -0.0144 -0.0262 0.0562  438  ASP A CB  
3197  C CG  . ASP A 440  ? 0.5150 0.4962 0.7344 -0.0162 -0.0292 0.0599  438  ASP A CG  
3198  O OD1 . ASP A 440  ? 0.4733 0.4516 0.7022 -0.0166 -0.0334 0.0559  438  ASP A OD1 
3199  O OD2 . ASP A 440  ? 0.5348 0.5194 0.7559 -0.0171 -0.0275 0.0667  438  ASP A OD2 
3200  N N   . PHE A 441  ? 0.3122 0.2892 0.4996 -0.0111 -0.0269 0.0366  439  PHE A N   
3201  C CA  . PHE A 441  ? 0.2970 0.2746 0.4714 -0.0097 -0.0243 0.0327  439  PHE A CA  
3202  C C   . PHE A 441  ? 0.3108 0.2900 0.4807 -0.0094 -0.0246 0.0281  439  PHE A C   
3203  O O   . PHE A 441  ? 0.3273 0.3061 0.5040 -0.0099 -0.0278 0.0245  439  PHE A O   
3204  C CB  . PHE A 441  ? 0.2509 0.2264 0.4236 -0.0087 -0.0253 0.0276  439  PHE A CB  
3205  C CG  . PHE A 441  ? 0.2567 0.2332 0.4163 -0.0075 -0.0225 0.0245  439  PHE A CG  
3206  C CD1 . PHE A 441  ? 0.2380 0.2150 0.3899 -0.0070 -0.0190 0.0287  439  PHE A CD1 
3207  C CD2 . PHE A 441  ? 0.2649 0.2422 0.4198 -0.0068 -0.0233 0.0178  439  PHE A CD2 
3208  C CE1 . PHE A 441  ? 0.2265 0.2044 0.3670 -0.0059 -0.0165 0.0261  439  PHE A CE1 
3209  C CE2 . PHE A 441  ? 0.2476 0.2260 0.3909 -0.0058 -0.0208 0.0157  439  PHE A CE2 
3210  C CZ  . PHE A 441  ? 0.2236 0.2021 0.3600 -0.0054 -0.0174 0.0199  439  PHE A CZ  
3211  N N   . HIS A 442  ? 0.2811 0.2619 0.4396 -0.0087 -0.0213 0.0283  440  HIS A N   
3212  C CA  . HIS A 442  ? 0.3014 0.2838 0.4538 -0.0083 -0.0213 0.0239  440  HIS A CA  
3213  C C   . HIS A 442  ? 0.2985 0.2814 0.4389 -0.0071 -0.0185 0.0222  440  HIS A C   
3214  O O   . HIS A 442  ? 0.2463 0.2289 0.3824 -0.0067 -0.0159 0.0260  440  HIS A O   
3215  C CB  . HIS A 442  ? 0.2915 0.2760 0.4443 -0.0089 -0.0204 0.0275  440  HIS A CB  
3216  C CG  . HIS A 442  ? 0.2452 0.2310 0.3929 -0.0087 -0.0167 0.0337  440  HIS A CG  
3217  N ND1 . HIS A 442  ? 0.2918 0.2780 0.4454 -0.0094 -0.0161 0.0398  440  HIS A ND1 
3218  C CD2 . HIS A 442  ? 0.2906 0.2780 0.4284 -0.0079 -0.0136 0.0345  440  HIS A CD2 
3219  C CE1 . HIS A 442  ? 0.2622 0.2504 0.4093 -0.0089 -0.0126 0.0439  440  HIS A CE1 
3220  N NE2 . HIS A 442  ? 0.2668 0.2554 0.4044 -0.0079 -0.0112 0.0406  440  HIS A NE2 
3221  N N   . VAL A 443  ? 0.3117 0.2957 0.4470 -0.0066 -0.0192 0.0166  441  VAL A N   
3222  C CA  . VAL A 443  ? 0.3224 0.3072 0.4466 -0.0057 -0.0166 0.0153  441  VAL A CA  
3223  C C   . VAL A 443  ? 0.2749 0.2608 0.3935 -0.0056 -0.0135 0.0203  441  VAL A C   
3224  O O   . VAL A 443  ? 0.2920 0.2792 0.4125 -0.0061 -0.0137 0.0221  441  VAL A O   
3225  C CB  . VAL A 443  ? 0.3437 0.3304 0.4637 -0.0053 -0.0180 0.0090  441  VAL A CB  
3226  C CG1 . VAL A 443  ? 0.3555 0.3436 0.4644 -0.0046 -0.0153 0.0089  441  VAL A CG1 
3227  C CG2 . VAL A 443  ? 0.4188 0.4049 0.5432 -0.0049 -0.0206 0.0037  441  VAL A CG2 
3228  N N   . GLY A 444  ? 0.2646 0.2500 0.3767 -0.0050 -0.0108 0.0225  442  GLY A N   
3229  C CA  . GLY A 444  ? 0.2343 0.2208 0.3420 -0.0047 -0.0079 0.0273  442  GLY A CA  
3230  C C   . GLY A 444  ? 0.2011 0.1873 0.3129 -0.0049 -0.0067 0.0326  442  GLY A C   
3231  O O   . GLY A 444  ? 0.2098 0.1973 0.3173 -0.0044 -0.0040 0.0362  442  GLY A O   
3232  N N   . LYS A 445  ? 0.1942 0.1792 0.3144 -0.0055 -0.0087 0.0334  443  LYS A N   
3233  C CA  . LYS A 445  ? 0.1922 0.1776 0.3163 -0.0058 -0.0076 0.0391  443  LYS A CA  
3234  C C   . LYS A 445  ? 0.2101 0.1948 0.3284 -0.0049 -0.0056 0.0397  443  LYS A C   
3235  O O   . LYS A 445  ? 0.2117 0.1982 0.3260 -0.0044 -0.0029 0.0437  443  LYS A O   
3236  C CB  . LYS A 445  ? 0.2226 0.2068 0.3583 -0.0069 -0.0105 0.0403  443  LYS A CB  
3237  C CG  . LYS A 445  ? 0.2653 0.2510 0.4056 -0.0074 -0.0094 0.0472  443  LYS A CG  
3238  C CD  . LYS A 445  ? 0.3298 0.3146 0.4826 -0.0087 -0.0124 0.0493  443  LYS A CD  
3239  C CE  . LYS A 445  ? 0.3337 0.3215 0.4910 -0.0095 -0.0110 0.0571  443  LYS A CE  
3240  N NZ  . LYS A 445  ? 0.4211 0.4081 0.5914 -0.0110 -0.0141 0.0601  443  LYS A NZ  
3241  N N   . TYR A 446  ? 0.1918 0.1744 0.3097 -0.0046 -0.0069 0.0356  444  TYR A N   
3242  C CA  . TYR A 446  ? 0.1959 0.1778 0.3076 -0.0038 -0.0053 0.0352  444  TYR A CA  
3243  C C   . TYR A 446  ? 0.2086 0.1887 0.3189 -0.0034 -0.0071 0.0289  444  TYR A C   
3244  O O   . TYR A 446  ? 0.1911 0.1710 0.3060 -0.0039 -0.0096 0.0253  444  TYR A O   
3245  C CB  . TYR A 446  ? 0.1847 0.1664 0.3013 -0.0040 -0.0051 0.0398  444  TYR A CB  
3246  C CG  . TYR A 446  ? 0.2175 0.1970 0.3435 -0.0046 -0.0083 0.0384  444  TYR A CG  
3247  C CD1 . TYR A 446  ? 0.3028 0.2822 0.4392 -0.0058 -0.0106 0.0406  444  TYR A CD1 
3248  C CD2 . TYR A 446  ? 0.2659 0.2434 0.3909 -0.0041 -0.0092 0.0349  444  TYR A CD2 
3249  C CE1 . TYR A 446  ? 0.2528 0.2300 0.3987 -0.0063 -0.0139 0.0392  444  TYR A CE1 
3250  C CE2 . TYR A 446  ? 0.3163 0.2917 0.4503 -0.0045 -0.0122 0.0334  444  TYR A CE2 
3251  C CZ  . TYR A 446  ? 0.3037 0.2788 0.4482 -0.0056 -0.0147 0.0354  444  TYR A CZ  
3252  O OH  . TYR A 446  ? 0.4110 0.3838 0.5651 -0.0059 -0.0180 0.0336  444  TYR A OH  
3253  N N   . GLU A 447  ? 0.1741 0.1536 0.2785 -0.0027 -0.0058 0.0274  445  GLU A N   
3254  C CA  . GLU A 447  ? 0.1802 0.1586 0.2839 -0.0023 -0.0075 0.0218  445  GLU A CA  
3255  C C   . GLU A 447  ? 0.1939 0.1711 0.2959 -0.0017 -0.0066 0.0224  445  GLU A C   
3256  O O   . GLU A 447  ? 0.1865 0.1640 0.2861 -0.0015 -0.0045 0.0268  445  GLU A O   
3257  C CB  . GLU A 447  ? 0.1874 0.1672 0.2831 -0.0019 -0.0067 0.0178  445  GLU A CB  
3258  C CG  . GLU A 447  ? 0.1919 0.1722 0.2785 -0.0012 -0.0037 0.0197  445  GLU A CG  
3259  C CD  . GLU A 447  ? 0.1922 0.1740 0.2716 -0.0010 -0.0031 0.0168  445  GLU A CD  
3260  O OE1 . GLU A 447  ? 0.2100 0.1931 0.2911 -0.0014 -0.0048 0.0139  445  GLU A OE1 
3261  O OE2 . GLU A 447  ? 0.1925 0.1745 0.2648 -0.0005 -0.0010 0.0175  445  GLU A OE2 
3262  N N   . PHE A 448  ? 0.1808 0.1570 0.2840 -0.0014 -0.0083 0.0176  446  PHE A N   
3263  C CA  . PHE A 448  ? 0.1799 0.1552 0.2798 -0.0007 -0.0074 0.0170  446  PHE A CA  
3264  C C   . PHE A 448  ? 0.1634 0.1399 0.2537 -0.0001 -0.0059 0.0136  446  PHE A C   
3265  O O   . PHE A 448  ? 0.1916 0.1696 0.2788 -0.0002 -0.0060 0.0111  446  PHE A O   
3266  C CB  . PHE A 448  ? 0.2007 0.1744 0.3083 -0.0006 -0.0103 0.0138  446  PHE A CB  
3267  C CG  . PHE A 448  ? 0.2113 0.1837 0.3291 -0.0013 -0.0120 0.0177  446  PHE A CG  
3268  C CD1 . PHE A 448  ? 0.1999 0.1717 0.3187 -0.0013 -0.0109 0.0229  446  PHE A CD1 
3269  C CD2 . PHE A 448  ? 0.2224 0.1944 0.3490 -0.0020 -0.0148 0.0165  446  PHE A CD2 
3270  C CE1 . PHE A 448  ? 0.2593 0.2303 0.3878 -0.0021 -0.0125 0.0273  446  PHE A CE1 
3271  C CE2 . PHE A 448  ? 0.2565 0.2271 0.3932 -0.0028 -0.0165 0.0206  446  PHE A CE2 
3272  C CZ  . PHE A 448  ? 0.2326 0.2029 0.3703 -0.0029 -0.0153 0.0262  446  PHE A CZ  
3273  N N   . GLN A 449  ? 0.1759 0.1519 0.2616 0.0006  -0.0045 0.0137  447  GLN A N   
3274  C CA  . GLN A 449  ? 0.1796 0.1567 0.2571 0.0011  -0.0033 0.0105  447  GLN A CA  
3275  C C   . GLN A 449  ? 0.2011 0.1774 0.2783 0.0016  -0.0036 0.0082  447  GLN A C   
3276  O O   . GLN A 449  ? 0.2032 0.1779 0.2846 0.0018  -0.0039 0.0104  447  GLN A O   
3277  C CB  . GLN A 449  ? 0.1751 0.1529 0.2448 0.0012  -0.0005 0.0136  447  GLN A CB  
3278  C CG  . GLN A 449  ? 0.1646 0.1433 0.2344 0.0008  0.0000  0.0159  447  GLN A CG  
3279  C CD  . GLN A 449  ? 0.1964 0.1760 0.2583 0.0011  0.0023  0.0174  447  GLN A CD  
3280  O OE1 . GLN A 449  ? 0.2097 0.1890 0.2667 0.0017  0.0037  0.0175  447  GLN A OE1 
3281  N NE2 . GLN A 449  ? 0.1856 0.1662 0.2468 0.0008  0.0026  0.0184  447  GLN A NE2 
3282  N N   . CYS A 450  ? 0.1809 0.1587 0.2534 0.0020  -0.0036 0.0038  448  CYS A N   
3283  C CA  . CYS A 450  ? 0.1824 0.1599 0.2540 0.0026  -0.0038 0.0012  448  CYS A CA  
3284  C C   . CYS A 450  ? 0.1983 0.1780 0.2614 0.0028  -0.0022 -0.0009 448  CYS A C   
3285  O O   . CYS A 450  ? 0.2031 0.1844 0.2618 0.0024  -0.0015 -0.0008 448  CYS A O   
3286  C CB  . CYS A 450  ? 0.2106 0.1882 0.2896 0.0028  -0.0067 -0.0034 448  CYS A CB  
3287  S SG  . CYS A 450  ? 0.2302 0.2116 0.3076 0.0029  -0.0080 -0.0097 448  CYS A SG  
3288  N N   . LEU A 451  ? 0.1953 0.1750 0.2564 0.0033  -0.0019 -0.0026 449  LEU A N   
3289  C CA  . LEU A 451  ? 0.2326 0.2144 0.2863 0.0034  -0.0006 -0.0045 449  LEU A CA  
3290  C C   . LEU A 451  ? 0.2158 0.2009 0.2703 0.0036  -0.0022 -0.0102 449  LEU A C   
3291  O O   . LEU A 451  ? 0.2204 0.2054 0.2808 0.0041  -0.0041 -0.0134 449  LEU A O   
3292  C CB  . LEU A 451  ? 0.2414 0.2219 0.2925 0.0039  0.0006  -0.0033 449  LEU A CB  
3293  C CG  . LEU A 451  ? 0.2716 0.2542 0.3157 0.0040  0.0019  -0.0050 449  LEU A CG  
3294  C CD1 . LEU A 451  ? 0.2824 0.2658 0.3205 0.0035  0.0035  -0.0024 449  LEU A CD1 
3295  C CD2 . LEU A 451  ? 0.2679 0.2490 0.3111 0.0046  0.0027  -0.0041 449  LEU A CD2 
3296  N N   . HIS A 452  ? 0.2098 0.1981 0.2586 0.0032  -0.0015 -0.0114 450  HIS A N   
3297  C CA  . HIS A 452  ? 0.2250 0.2177 0.2733 0.0034  -0.0026 -0.0166 450  HIS A CA  
3298  C C   . HIS A 452  ? 0.2511 0.2444 0.3000 0.0042  -0.0028 -0.0196 450  HIS A C   
3299  O O   . HIS A 452  ? 0.2687 0.2602 0.3145 0.0043  -0.0013 -0.0173 450  HIS A O   
3300  C CB  . HIS A 452  ? 0.2240 0.2203 0.2651 0.0028  -0.0013 -0.0161 450  HIS A CB  
3301  C CG  . HIS A 452  ? 0.2004 0.2023 0.2396 0.0029  -0.0020 -0.0208 450  HIS A CG  
3302  N ND1 . HIS A 452  ? 0.2243 0.2303 0.2656 0.0029  -0.0037 -0.0246 450  HIS A ND1 
3303  C CD2 . HIS A 452  ? 0.2499 0.2546 0.2855 0.0031  -0.0013 -0.0226 450  HIS A CD2 
3304  C CE1 . HIS A 452  ? 0.2515 0.2630 0.2902 0.0032  -0.0039 -0.0284 450  HIS A CE1 
3305  N NE2 . HIS A 452  ? 0.2467 0.2574 0.2821 0.0033  -0.0024 -0.0272 450  HIS A NE2 
3306  N N   . GLY A 453  ? 0.2780 0.2741 0.3309 0.0048  -0.0048 -0.0249 451  GLY A N   
3307  C CA  . GLY A 453  ? 0.3062 0.3035 0.3599 0.0056  -0.0051 -0.0283 451  GLY A CA  
3308  C C   . GLY A 453  ? 0.4013 0.3938 0.4596 0.0061  -0.0053 -0.0264 451  GLY A C   
3309  O O   . GLY A 453  ? 0.3933 0.3860 0.4508 0.0067  -0.0049 -0.0275 451  GLY A O   
3310  N N   . MET A 454  ? 0.3015 0.2900 0.3649 0.0059  -0.0060 -0.0233 452  MET A N   
3311  C CA  . MET A 454  ? 0.2620 0.2463 0.3304 0.0062  -0.0065 -0.0208 452  MET A CA  
3312  C C   . MET A 454  ? 0.2762 0.2581 0.3534 0.0060  -0.0086 -0.0200 452  MET A C   
3313  O O   . MET A 454  ? 0.2935 0.2738 0.3784 0.0066  -0.0107 -0.0217 452  MET A O   
3314  C CB  . MET A 454  ? 0.2697 0.2516 0.3328 0.0058  -0.0040 -0.0149 452  MET A CB  
3315  C CG  . MET A 454  ? 0.2941 0.2723 0.3623 0.0060  -0.0044 -0.0114 452  MET A CG  
3316  S SD  . MET A 454  ? 0.3636 0.3415 0.4364 0.0070  -0.0059 -0.0151 452  MET A SD  
3317  C CE  . MET A 454  ? 0.3758 0.3560 0.4388 0.0072  -0.0034 -0.0156 452  MET A CE  
3318  N N   . GLY A 455  ? 0.2590 0.2406 0.3354 0.0052  -0.0083 -0.0174 453  GLY A N   
3319  C CA  . GLY A 455  ? 0.2625 0.2417 0.3470 0.0049  -0.0101 -0.0155 453  GLY A CA  
3320  C C   . GLY A 455  ? 0.2631 0.2441 0.3537 0.0050  -0.0128 -0.0204 453  GLY A C   
3321  O O   . GLY A 455  ? 0.2694 0.2481 0.3682 0.0047  -0.0148 -0.0193 453  GLY A O   
3322  N N   . GLU A 456  ? 0.2926 0.2778 0.3795 0.0054  -0.0130 -0.0256 454  GLU A N   
3323  C CA  . GLU A 456  ? 0.2997 0.2872 0.3919 0.0055  -0.0157 -0.0306 454  GLU A CA  
3324  C C   . GLU A 456  ? 0.3232 0.3090 0.4262 0.0063  -0.0189 -0.0342 454  GLU A C   
3325  O O   . GLU A 456  ? 0.3021 0.2873 0.4124 0.0061  -0.0213 -0.0354 454  GLU A O   
3326  C CB  . GLU A 456  ? 0.3270 0.3204 0.4129 0.0059  -0.0153 -0.0356 454  GLU A CB  
3327  C CG  . GLU A 456  ? 0.3746 0.3698 0.4513 0.0050  -0.0128 -0.0322 454  GLU A CG  
3328  C CD  . GLU A 456  ? 0.3693 0.3652 0.4382 0.0050  -0.0102 -0.0303 454  GLU A CD  
3329  O OE1 . GLU A 456  ? 0.3440 0.3374 0.4145 0.0055  -0.0099 -0.0297 454  GLU A OE1 
3330  O OE2 . GLU A 456  ? 0.3504 0.3494 0.4119 0.0045  -0.0086 -0.0294 454  GLU A OE2 
3331  N N   . PRO A 457  ? 0.3128 0.2980 0.4179 0.0072  -0.0194 -0.0364 455  PRO A N   
3332  C CA  . PRO A 457  ? 0.3365 0.3197 0.4532 0.0080  -0.0228 -0.0396 455  PRO A CA  
3333  C C   . PRO A 457  ? 0.2925 0.2709 0.4174 0.0071  -0.0241 -0.0344 455  PRO A C   
3334  O O   . PRO A 457  ? 0.3274 0.3050 0.4621 0.0072  -0.0273 -0.0371 455  PRO A O   
3335  C CB  . PRO A 457  ? 0.3329 0.3157 0.4491 0.0089  -0.0223 -0.0408 455  PRO A CB  
3336  C CG  . PRO A 457  ? 0.3546 0.3415 0.4593 0.0090  -0.0194 -0.0417 455  PRO A CG  
3337  C CD  . PRO A 457  ? 0.3224 0.3089 0.4203 0.0077  -0.0171 -0.0364 455  PRO A CD  
3338  N N   . LEU A 458  ? 0.2804 0.2560 0.4019 0.0062  -0.0218 -0.0270 456  LEU A N   
3339  C CA  . LEU A 458  ? 0.2672 0.2393 0.3961 0.0053  -0.0228 -0.0214 456  LEU A CA  
3340  C C   . LEU A 458  ? 0.2769 0.2500 0.4069 0.0045  -0.0234 -0.0212 456  LEU A C   
3341  O O   . LEU A 458  ? 0.2687 0.2401 0.4086 0.0041  -0.0263 -0.0215 456  LEU A O   
3342  C CB  . LEU A 458  ? 0.2707 0.2409 0.3944 0.0047  -0.0199 -0.0139 456  LEU A CB  
3343  C CG  . LEU A 458  ? 0.2712 0.2389 0.4009 0.0036  -0.0202 -0.0071 456  LEU A CG  
3344  C CD1 . LEU A 458  ? 0.2807 0.2459 0.4237 0.0036  -0.0239 -0.0075 456  LEU A CD1 
3345  C CD2 . LEU A 458  ? 0.2961 0.2632 0.4197 0.0033  -0.0172 -0.0005 456  LEU A CD2 
3346  N N   . TYR A 459  ? 0.2473 0.2228 0.3676 0.0041  -0.0209 -0.0206 457  TYR A N   
3347  C CA  . TYR A 459  ? 0.2576 0.2339 0.3787 0.0033  -0.0212 -0.0192 457  TYR A CA  
3348  C C   . TYR A 459  ? 0.2570 0.2358 0.3823 0.0037  -0.0241 -0.0260 457  TYR A C   
3349  O O   . TYR A 459  ? 0.2794 0.2583 0.4085 0.0030  -0.0252 -0.0253 457  TYR A O   
3350  C CB  . TYR A 459  ? 0.2428 0.2204 0.3531 0.0027  -0.0178 -0.0153 457  TYR A CB  
3351  C CG  . TYR A 459  ? 0.2306 0.2054 0.3402 0.0022  -0.0158 -0.0080 457  TYR A CG  
3352  C CD1 . TYR A 459  ? 0.2265 0.1998 0.3417 0.0013  -0.0163 -0.0033 457  TYR A CD1 
3353  C CD2 . TYR A 459  ? 0.2257 0.1999 0.3298 0.0026  -0.0136 -0.0059 457  TYR A CD2 
3354  C CE1 . TYR A 459  ? 0.2450 0.2168 0.3597 0.0009  -0.0145 0.0033  457  TYR A CE1 
3355  C CE2 . TYR A 459  ? 0.2074 0.1798 0.3108 0.0022  -0.0119 0.0006  457  TYR A CE2 
3356  C CZ  . TYR A 459  ? 0.2392 0.2107 0.3479 0.0013  -0.0124 0.0051  457  TYR A CZ  
3357  O OH  . TYR A 459  ? 0.2267 0.1974 0.3347 0.0010  -0.0106 0.0115  457  TYR A OH  
3358  N N   . GLU A 460  ? 0.2749 0.2563 0.4003 0.0048  -0.0253 -0.0328 458  GLU A N   
3359  C CA  . GLU A 460  ? 0.2994 0.2833 0.4311 0.0054  -0.0286 -0.0397 458  GLU A CA  
3360  C C   . GLU A 460  ? 0.3425 0.3227 0.4879 0.0054  -0.0322 -0.0400 458  GLU A C   
3361  O O   . GLU A 460  ? 0.3411 0.3228 0.4932 0.0057  -0.0353 -0.0452 458  GLU A O   
3362  C CB  . GLU A 460  ? 0.3877 0.3761 0.5159 0.0068  -0.0289 -0.0470 458  GLU A CB  
3363  C CG  . GLU A 460  ? 0.4278 0.4214 0.5445 0.0066  -0.0265 -0.0480 458  GLU A CG  
3364  C CD  . GLU A 460  ? 0.5850 0.5842 0.6981 0.0079  -0.0267 -0.0549 458  GLU A CD  
3365  O OE1 . GLU A 460  ? 0.5915 0.5899 0.7088 0.0089  -0.0277 -0.0579 458  GLU A OE1 
3366  O OE2 . GLU A 460  ? 0.6420 0.6468 0.7483 0.0078  -0.0258 -0.0573 458  GLU A OE2 
3367  N N   . GLU A 461  ? 0.2816 0.2573 0.4316 0.0049  -0.0320 -0.0346 459  GLU A N   
3368  C CA  . GLU A 461  ? 0.3444 0.3164 0.5077 0.0045  -0.0353 -0.0329 459  GLU A CA  
3369  C C   . GLU A 461  ? 0.3112 0.2813 0.4760 0.0029  -0.0345 -0.0256 459  GLU A C   
3370  O O   . GLU A 461  ? 0.3110 0.2781 0.4867 0.0022  -0.0369 -0.0226 459  GLU A O   
3371  C CB  . GLU A 461  ? 0.2909 0.2597 0.4592 0.0049  -0.0358 -0.0307 459  GLU A CB  
3372  C CG  . GLU A 461  ? 0.3241 0.2948 0.4906 0.0065  -0.0363 -0.0375 459  GLU A CG  
3373  C CD  . GLU A 461  ? 0.3622 0.3350 0.5366 0.0077  -0.0402 -0.0464 459  GLU A CD  
3374  O OE1 . GLU A 461  ? 0.4122 0.3832 0.5973 0.0072  -0.0434 -0.0468 459  GLU A OE1 
3375  O OE2 . GLU A 461  ? 0.3919 0.3685 0.5622 0.0091  -0.0401 -0.0531 459  GLU A OE2 
3376  N N   . VAL A 462  ? 0.2918 0.2639 0.4464 0.0023  -0.0313 -0.0227 460  VAL A N   
3377  C CA  . VAL A 462  ? 0.2556 0.2265 0.4100 0.0009  -0.0300 -0.0156 460  VAL A CA  
3378  C C   . VAL A 462  ? 0.2826 0.2562 0.4344 0.0005  -0.0301 -0.0177 460  VAL A C   
3379  O O   . VAL A 462  ? 0.2905 0.2632 0.4496 -0.0003 -0.0319 -0.0159 460  VAL A O   
3380  C CB  . VAL A 462  ? 0.2748 0.2453 0.4198 0.0006  -0.0259 -0.0092 460  VAL A CB  
3381  C CG1 . VAL A 462  ? 0.2480 0.2183 0.3924 -0.0006 -0.0244 -0.0026 460  VAL A CG1 
3382  C CG2 . VAL A 462  ? 0.2836 0.2516 0.4318 0.0009  -0.0259 -0.0066 460  VAL A CG2 
3383  N N   . VAL A 463  ? 0.2951 0.2721 0.4368 0.0011  -0.0284 -0.0212 461  VAL A N   
3384  C CA  . VAL A 463  ? 0.2832 0.2633 0.4212 0.0007  -0.0283 -0.0228 461  VAL A CA  
3385  C C   . VAL A 463  ? 0.3413 0.3230 0.4876 0.0011  -0.0322 -0.0295 461  VAL A C   
3386  O O   . VAL A 463  ? 0.3616 0.3441 0.5118 0.0022  -0.0344 -0.0355 461  VAL A O   
3387  C CB  . VAL A 463  ? 0.2715 0.2552 0.3969 0.0012  -0.0255 -0.0245 461  VAL A CB  
3388  C CG1 . VAL A 463  ? 0.2975 0.2848 0.4192 0.0008  -0.0256 -0.0263 461  VAL A CG1 
3389  C CG2 . VAL A 463  ? 0.2901 0.2722 0.4079 0.0009  -0.0218 -0.0182 461  VAL A CG2 
3390  N N   . GLY A 464  ? 0.3406 0.3229 0.4899 0.0003  -0.0333 -0.0287 462  GLY A N   
3391  C CA  . GLY A 464  ? 0.3848 0.3692 0.5409 0.0007  -0.0371 -0.0354 462  GLY A CA  
3392  C C   . GLY A 464  ? 0.3858 0.3667 0.5558 0.0000  -0.0405 -0.0341 462  GLY A C   
3393  O O   . GLY A 464  ? 0.3341 0.3110 0.5103 -0.0003 -0.0407 -0.0299 462  GLY A O   
3394  N N   . ARG A 465  ? 0.3793 0.3620 0.5548 -0.0002 -0.0432 -0.0377 463  ARG A N   
3395  C CA  . ARG A 465  ? 0.4180 0.3975 0.6073 -0.0009 -0.0468 -0.0366 463  ARG A CA  
3396  C C   . ARG A 465  ? 0.4233 0.4003 0.6234 -0.0001 -0.0501 -0.0405 463  ARG A C   
3397  O O   . ARG A 465  ? 0.4843 0.4574 0.6960 -0.0009 -0.0524 -0.0371 463  ARG A O   
3398  C CB  . ARG A 465  ? 0.4404 0.4227 0.6330 -0.0012 -0.0493 -0.0406 463  ARG A CB  
3399  N N   . GLY A 466  ? 0.3595 0.3389 0.5564 0.0015  -0.0505 -0.0475 464  GLY A N   
3400  C CA  . GLY A 466  ? 0.3879 0.3650 0.5946 0.0025  -0.0536 -0.0514 464  GLY A CA  
3401  C C   . GLY A 466  ? 0.4327 0.4060 0.6391 0.0023  -0.0517 -0.0456 464  GLY A C   
3402  O O   . GLY A 466  ? 0.4347 0.4055 0.6503 0.0030  -0.0543 -0.0478 464  GLY A O   
3403  N N   . LYS A 467  ? 0.3670 0.3399 0.5632 0.0014  -0.0473 -0.0383 465  LYS A N   
3404  C CA  . LYS A 467  ? 0.2931 0.2627 0.4884 0.0012  -0.0453 -0.0322 465  LYS A CA  
3405  C C   . LYS A 467  ? 0.3421 0.3091 0.5401 -0.0006 -0.0441 -0.0227 465  LYS A C   
3406  O O   . LYS A 467  ? 0.3906 0.3558 0.5999 -0.0015 -0.0471 -0.0212 465  LYS A O   
3407  C CB  . LYS A 467  ? 0.3370 0.3089 0.5181 0.0019  -0.0413 -0.0322 465  LYS A CB  
3408  C CG  . LYS A 467  ? 0.3351 0.3105 0.5135 0.0036  -0.0422 -0.0412 465  LYS A CG  
3409  C CD  . LYS A 467  ? 0.3860 0.3590 0.5751 0.0046  -0.0455 -0.0448 465  LYS A CD  
3410  C CE  . LYS A 467  ? 0.4064 0.3834 0.5922 0.0065  -0.0461 -0.0538 465  LYS A CE  
3411  N NZ  . LYS A 467  ? 0.3626 0.3373 0.5586 0.0076  -0.0491 -0.0573 465  LYS A NZ  
3412  N N   . LEU A 468  ? 0.3197 0.2869 0.5079 -0.0011 -0.0399 -0.0164 466  LEU A N   
3413  C CA  . LEU A 468  ? 0.3094 0.2752 0.4990 -0.0026 -0.0384 -0.0075 466  LEU A CA  
3414  C C   . LEU A 468  ? 0.2965 0.2646 0.4803 -0.0033 -0.0367 -0.0060 466  LEU A C   
3415  O O   . LEU A 468  ? 0.3195 0.2872 0.5052 -0.0045 -0.0357 0.0009  466  LEU A O   
3416  C CB  . LEU A 468  ? 0.3416 0.3066 0.5247 -0.0026 -0.0350 -0.0013 466  LEU A CB  
3417  C CG  . LEU A 468  ? 0.3193 0.2819 0.5079 -0.0020 -0.0364 -0.0018 466  LEU A CG  
3418  C CD1 . LEU A 468  ? 0.3413 0.3035 0.5243 -0.0022 -0.0331 0.0053  466  LEU A CD1 
3419  C CD2 . LEU A 468  ? 0.3651 0.3250 0.5698 -0.0026 -0.0409 -0.0016 466  LEU A CD2 
3420  N N   . ASP A 469  ? 0.3097 0.2808 0.4867 -0.0025 -0.0365 -0.0121 467  ASP A N   
3421  C CA  . ASP A 469  ? 0.2956 0.2692 0.4670 -0.0031 -0.0351 -0.0112 467  ASP A CA  
3422  C C   . ASP A 469  ? 0.2701 0.2438 0.4328 -0.0037 -0.0309 -0.0038 467  ASP A C   
3423  O O   . ASP A 469  ? 0.2631 0.2372 0.4267 -0.0046 -0.0302 0.0007  467  ASP A O   
3424  C CB  . ASP A 469  ? 0.3268 0.3000 0.5088 -0.0040 -0.0384 -0.0114 467  ASP A CB  
3425  C CG  . ASP A 469  ? 0.3876 0.3642 0.5644 -0.0042 -0.0380 -0.0136 467  ASP A CG  
3426  O OD1 . ASP A 469  ? 0.3627 0.3421 0.5291 -0.0034 -0.0362 -0.0172 467  ASP A OD1 
3427  O OD2 . ASP A 469  ? 0.4241 0.4004 0.6071 -0.0052 -0.0395 -0.0116 467  ASP A OD2 
3428  N N   . ARG A 470  ? 0.2729 0.2465 0.4276 -0.0030 -0.0282 -0.0028 468  ARG A N   
3429  C CA  . ARG A 470  ? 0.2422 0.2164 0.3876 -0.0032 -0.0242 0.0028  468  ARG A CA  
3430  C C   . ARG A 470  ? 0.2526 0.2290 0.3863 -0.0023 -0.0220 -0.0007 468  ARG A C   
3431  O O   . ARG A 470  ? 0.2433 0.2201 0.3758 -0.0014 -0.0228 -0.0056 468  ARG A O   
3432  C CB  . ARG A 470  ? 0.2495 0.2216 0.3965 -0.0034 -0.0228 0.0087  468  ARG A CB  
3433  C CG  . ARG A 470  ? 0.2399 0.2103 0.3987 -0.0045 -0.0248 0.0136  468  ARG A CG  
3434  C CD  . ARG A 470  ? 0.2374 0.2093 0.3968 -0.0055 -0.0239 0.0181  468  ARG A CD  
3435  N NE  . ARG A 470  ? 0.2654 0.2362 0.4365 -0.0067 -0.0259 0.0230  468  ARG A NE  
3436  C CZ  . ARG A 470  ? 0.2601 0.2301 0.4415 -0.0074 -0.0294 0.0211  468  ARG A CZ  
3437  N NH1 . ARG A 470  ? 0.2799 0.2505 0.4612 -0.0069 -0.0313 0.0142  468  ARG A NH1 
3438  N NH2 . ARG A 470  ? 0.3058 0.2749 0.4981 -0.0086 -0.0311 0.0265  468  ARG A NH2 
3439  N N   . PRO A 471  ? 0.2179 0.1960 0.3433 -0.0025 -0.0193 0.0018  469  PRO A N   
3440  C CA  . PRO A 471  ? 0.2134 0.1937 0.3282 -0.0018 -0.0175 -0.0012 469  PRO A CA  
3441  C C   . PRO A 471  ? 0.2372 0.2165 0.3458 -0.0013 -0.0149 0.0010  469  PRO A C   
3442  O O   . PRO A 471  ? 0.2171 0.1945 0.3273 -0.0015 -0.0137 0.0059  469  PRO A O   
3443  C CB  . PRO A 471  ? 0.2202 0.2022 0.3301 -0.0023 -0.0158 0.0016  469  PRO A CB  
3444  C CG  . PRO A 471  ? 0.2444 0.2246 0.3594 -0.0030 -0.0152 0.0079  469  PRO A CG  
3445  C CD  . PRO A 471  ? 0.2249 0.2032 0.3510 -0.0034 -0.0182 0.0072  469  PRO A CD  
3446  N N   . CYS A 472  ? 0.2118 0.1930 0.3132 -0.0006 -0.0141 -0.0028 470  CYS A N   
3447  C CA  . CYS A 472  ? 0.2147 0.1951 0.3097 -0.0001 -0.0117 -0.0013 470  CYS A CA  
3448  C C   . CYS A 472  ? 0.1927 0.1757 0.2778 0.0000  -0.0098 -0.0025 470  CYS A C   
3449  O O   . CYS A 472  ? 0.2223 0.2082 0.3059 0.0001  -0.0109 -0.0070 470  CYS A O   
3450  C CB  . CYS A 472  ? 0.2265 0.2063 0.3245 0.0006  -0.0131 -0.0052 470  CYS A CB  
3451  S SG  . CYS A 472  ? 0.2331 0.2120 0.3237 0.0012  -0.0104 -0.0035 470  CYS A SG  
3452  N N   . ARG A 473  ? 0.1928 0.1752 0.2717 0.0001  -0.0071 0.0016  471  ARG A N   
3453  C CA  . ARG A 473  ? 0.1898 0.1742 0.2599 0.0002  -0.0053 0.0011  471  ARG A CA  
3454  C C   . ARG A 473  ? 0.1994 0.1837 0.2652 0.0008  -0.0043 -0.0004 471  ARG A C   
3455  O O   . ARG A 473  ? 0.2036 0.1857 0.2699 0.0011  -0.0033 0.0022  471  ARG A O   
3456  C CB  . ARG A 473  ? 0.1990 0.1828 0.2653 0.0000  -0.0031 0.0060  471  ARG A CB  
3457  C CG  . ARG A 473  ? 0.1909 0.1767 0.2492 0.0000  -0.0017 0.0057  471  ARG A CG  
3458  C CD  . ARG A 473  ? 0.2047 0.1899 0.2605 -0.0001 0.0000  0.0101  471  ARG A CD  
3459  N NE  . ARG A 473  ? 0.1924 0.1776 0.2535 -0.0005 -0.0009 0.0116  471  ARG A NE  
3460  C CZ  . ARG A 473  ? 0.2082 0.1954 0.2700 -0.0010 -0.0021 0.0103  471  ARG A CZ  
3461  N NH1 . ARG A 473  ? 0.2217 0.2112 0.2786 -0.0011 -0.0023 0.0079  471  ARG A NH1 
3462  N NH2 . ARG A 473  ? 0.2093 0.1963 0.2767 -0.0014 -0.0032 0.0116  471  ARG A NH2 
3463  N N   . ILE A 474  ? 0.1944 0.1816 0.2560 0.0009  -0.0045 -0.0042 472  ILE A N   
3464  C CA  . ILE A 474  ? 0.2018 0.1895 0.2594 0.0014  -0.0037 -0.0061 472  ILE A CA  
3465  C C   . ILE A 474  ? 0.1949 0.1828 0.2448 0.0013  -0.0013 -0.0031 472  ILE A C   
3466  O O   . ILE A 474  ? 0.2072 0.1973 0.2530 0.0008  -0.0009 -0.0029 472  ILE A O   
3467  C CB  . ILE A 474  ? 0.1953 0.1869 0.2527 0.0016  -0.0053 -0.0119 472  ILE A CB  
3468  C CG1 . ILE A 474  ? 0.2411 0.2323 0.3071 0.0019  -0.0080 -0.0153 472  ILE A CG1 
3469  C CG2 . ILE A 474  ? 0.2136 0.2065 0.2668 0.0021  -0.0043 -0.0136 472  ILE A CG2 
3470  C CD1 . ILE A 474  ? 0.2509 0.2468 0.3174 0.0022  -0.0099 -0.0215 472  ILE A CD1 
3471  N N   . TYR A 475  ? 0.2007 0.1863 0.2489 0.0017  0.0002  -0.0008 473  TYR A N   
3472  C CA  . TYR A 475  ? 0.2054 0.1909 0.2467 0.0017  0.0022  0.0014  473  TYR A CA  
3473  C C   . TYR A 475  ? 0.1995 0.1878 0.2369 0.0017  0.0022  -0.0019 473  TYR A C   
3474  O O   . TYR A 475  ? 0.2031 0.1913 0.2418 0.0021  0.0017  -0.0043 473  TYR A O   
3475  C CB  . TYR A 475  ? 0.2093 0.1919 0.2505 0.0022  0.0036  0.0046  473  TYR A CB  
3476  C CG  . TYR A 475  ? 0.2198 0.2020 0.2549 0.0024  0.0056  0.0070  473  TYR A CG  
3477  C CD1 . TYR A 475  ? 0.2693 0.2522 0.3001 0.0025  0.0062  0.0056  473  TYR A CD1 
3478  C CD2 . TYR A 475  ? 0.2314 0.2129 0.2655 0.0024  0.0067  0.0104  473  TYR A CD2 
3479  C CE1 . TYR A 475  ? 0.2850 0.2673 0.3108 0.0027  0.0078  0.0076  473  TYR A CE1 
3480  C CE2 . TYR A 475  ? 0.2239 0.2049 0.2530 0.0027  0.0082  0.0121  473  TYR A CE2 
3481  C CZ  . TYR A 475  ? 0.2795 0.2609 0.3047 0.0028  0.0087  0.0107  473  TYR A CZ  
3482  O OH  . TYR A 475  ? 0.2916 0.2725 0.3125 0.0031  0.0100  0.0122  473  TYR A OH  
3483  N N   . ALA A 476  ? 0.1964 0.1873 0.2292 0.0012  0.0026  -0.0019 474  ALA A N   
3484  C CA  . ALA A 476  ? 0.1898 0.1848 0.2196 0.0010  0.0022  -0.0052 474  ALA A CA  
3485  C C   . ALA A 476  ? 0.2059 0.2013 0.2297 0.0007  0.0038  -0.0031 474  ALA A C   
3486  O O   . ALA A 476  ? 0.2028 0.1991 0.2237 0.0001  0.0043  -0.0009 474  ALA A O   
3487  C CB  . ALA A 476  ? 0.2343 0.2331 0.2646 0.0004  0.0009  -0.0070 474  ALA A CB  
3488  N N   . PRO A 477  ? 0.2212 0.2162 0.2434 0.0010  0.0045  -0.0038 475  PRO A N   
3489  C CA  . PRO A 477  ? 0.2298 0.2254 0.2468 0.0007  0.0058  -0.0020 475  PRO A CA  
3490  C C   . PRO A 477  ? 0.2079 0.2088 0.2221 -0.0001 0.0053  -0.0035 475  PRO A C   
3491  O O   . PRO A 477  ? 0.2013 0.2061 0.2169 -0.0001 0.0042  -0.0070 475  PRO A O   
3492  C CB  . PRO A 477  ? 0.2243 0.2186 0.2412 0.0013  0.0063  -0.0032 475  PRO A CB  
3493  C CG  . PRO A 477  ? 0.2738 0.2656 0.2960 0.0020  0.0055  -0.0042 475  PRO A CG  
3494  C CD  . PRO A 477  ? 0.2259 0.2196 0.2515 0.0018  0.0040  -0.0061 475  PRO A CD  
3495  N N   . VAL A 478  ? 0.1891 0.1906 0.1996 -0.0008 0.0060  -0.0006 476  VAL A N   
3496  C CA  . VAL A 478  ? 0.2177 0.2247 0.2255 -0.0018 0.0056  -0.0008 476  VAL A CA  
3497  C C   . VAL A 478  ? 0.2545 0.2615 0.2587 -0.0023 0.0066  0.0014  476  VAL A C   
3498  O O   . VAL A 478  ? 0.2855 0.2886 0.2891 -0.0023 0.0074  0.0045  476  VAL A O   
3499  C CB  . VAL A 478  ? 0.2327 0.2406 0.2407 -0.0024 0.0050  0.0012  476  VAL A CB  
3500  C CG1 . VAL A 478  ? 0.2399 0.2539 0.2450 -0.0035 0.0045  0.0016  476  VAL A CG1 
3501  C CG2 . VAL A 478  ? 0.2364 0.2438 0.2484 -0.0020 0.0039  -0.0009 476  VAL A CG2 
3502  N N   . GLY A 479  ? 0.2483 0.2599 0.2507 -0.0027 0.0066  -0.0002 477  GLY A N   
3503  C CA  . GLY A 479  ? 0.2810 0.2929 0.2805 -0.0034 0.0074  0.0023  477  GLY A CA  
3504  C C   . GLY A 479  ? 0.2557 0.2725 0.2537 -0.0037 0.0075  0.0000  477  GLY A C   
3505  O O   . GLY A 479  ? 0.2561 0.2758 0.2553 -0.0031 0.0070  -0.0039 477  GLY A O   
3506  N N   . THR A 480  ? 0.3007 0.3185 0.2963 -0.0045 0.0080  0.0025  478  THR A N   
3507  C CA  . THR A 480  ? 0.3019 0.3249 0.2959 -0.0050 0.0083  0.0011  478  THR A CA  
3508  C C   . THR A 480  ? 0.3481 0.3679 0.3430 -0.0039 0.0089  -0.0012 478  THR A C   
3509  O O   . THR A 480  ? 0.3455 0.3591 0.3420 -0.0029 0.0092  -0.0011 478  THR A O   
3510  C CB  . THR A 480  ? 0.3388 0.3633 0.3308 -0.0064 0.0085  0.0052  478  THR A CB  
3511  O OG1 . THR A 480  ? 0.3987 0.4162 0.3911 -0.0060 0.0090  0.0075  478  THR A OG1 
3512  C CG2 . THR A 480  ? 0.3704 0.3984 0.3618 -0.0075 0.0078  0.0079  478  THR A CG2 
3513  N N   . HIS A 481  ? 0.3741 0.3987 0.3680 -0.0041 0.0091  -0.0030 479  HIS A N   
3514  C CA  . HIS A 481  ? 0.4109 0.4330 0.4056 -0.0031 0.0096  -0.0051 479  HIS A CA  
3515  C C   . HIS A 481  ? 0.4419 0.4578 0.4361 -0.0030 0.0103  -0.0021 479  HIS A C   
3516  O O   . HIS A 481  ? 0.4218 0.4327 0.4175 -0.0019 0.0105  -0.0030 479  HIS A O   
3517  C CB  . HIS A 481  ? 0.3612 0.3902 0.3546 -0.0035 0.0099  -0.0071 479  HIS A CB  
3518  C CG  . HIS A 481  ? 0.4147 0.4507 0.4087 -0.0032 0.0092  -0.0110 479  HIS A CG  
3519  N ND1 . HIS A 481  ? 0.3900 0.4335 0.3830 -0.0034 0.0093  -0.0134 479  HIS A ND1 
3520  C CD2 . HIS A 481  ? 0.3726 0.4096 0.3683 -0.0027 0.0082  -0.0132 479  HIS A CD2 
3521  C CE1 . HIS A 481  ? 0.3986 0.4477 0.3925 -0.0029 0.0085  -0.0171 479  HIS A CE1 
3522  N NE2 . HIS A 481  ? 0.4132 0.4583 0.4089 -0.0025 0.0078  -0.0172 479  HIS A NE2 
3523  N N   . GLU A 482  ? 0.4500 0.4663 0.4424 -0.0042 0.0105  0.0015  480  GLU A N   
3524  C CA  . GLU A 482  ? 0.5055 0.5162 0.4977 -0.0041 0.0109  0.0040  480  GLU A CA  
3525  C C   . GLU A 482  ? 0.4891 0.4936 0.4827 -0.0030 0.0110  0.0045  480  GLU A C   
3526  O O   . GLU A 482  ? 0.5000 0.5001 0.4941 -0.0021 0.0114  0.0044  480  GLU A O   
3527  C CB  . GLU A 482  ? 0.5020 0.5142 0.4931 -0.0056 0.0107  0.0078  480  GLU A CB  
3528  N N   . THR A 483  ? 0.4349 0.4396 0.4292 -0.0032 0.0105  0.0052  481  THR A N   
3529  C CA  . THR A 483  ? 0.4407 0.4403 0.4364 -0.0023 0.0106  0.0061  481  THR A CA  
3530  C C   . THR A 483  ? 0.4242 0.4216 0.4219 -0.0010 0.0107  0.0036  481  THR A C   
3531  O O   . THR A 483  ? 0.4428 0.4357 0.4413 -0.0001 0.0112  0.0043  481  THR A O   
3532  C CB  . THR A 483  ? 0.4310 0.4319 0.4272 -0.0028 0.0100  0.0073  481  THR A CB  
3533  O OG1 . THR A 483  ? 0.5173 0.5208 0.5121 -0.0041 0.0096  0.0099  481  THR A OG1 
3534  C CG2 . THR A 483  ? 0.4865 0.4823 0.4841 -0.0019 0.0102  0.0087  481  THR A CG2 
3535  N N   . LEU A 484  ? 0.3751 0.3758 0.3739 -0.0009 0.0102  0.0005  482  LEU A N   
3536  C CA  . LEU A 484  ? 0.3812 0.3797 0.3830 0.0003  0.0100  -0.0017 482  LEU A CA  
3537  C C   . LEU A 484  ? 0.4044 0.4006 0.4063 0.0010  0.0105  -0.0023 482  LEU A C   
3538  O O   . LEU A 484  ? 0.4001 0.3927 0.4043 0.0019  0.0106  -0.0022 482  LEU A O   
3539  C CB  . LEU A 484  ? 0.3748 0.3774 0.3785 0.0003  0.0090  -0.0052 482  LEU A CB  
3540  C CG  . LEU A 484  ? 0.4027 0.4106 0.4055 0.0001  0.0089  -0.0082 482  LEU A CG  
3541  C CD1 . LEU A 484  ? 0.3887 0.3951 0.3941 0.0013  0.0087  -0.0110 482  LEU A CD1 
3542  C CD2 . LEU A 484  ? 0.4248 0.4387 0.4278 -0.0003 0.0080  -0.0105 482  LEU A CD2 
3543  N N   . LEU A 485  ? 0.4264 0.4249 0.4262 0.0006  0.0109  -0.0026 483  LEU A N   
3544  C CA  . LEU A 485  ? 0.4008 0.3975 0.4008 0.0013  0.0113  -0.0034 483  LEU A CA  
3545  C C   . LEU A 485  ? 0.4212 0.4131 0.4205 0.0017  0.0119  -0.0007 483  LEU A C   
3546  O O   . LEU A 485  ? 0.3998 0.3895 0.3999 0.0025  0.0121  -0.0011 483  LEU A O   
3547  C CB  . LEU A 485  ? 0.4003 0.4012 0.3984 0.0006  0.0115  -0.0044 483  LEU A CB  
3548  C CG  . LEU A 485  ? 0.3900 0.3966 0.3890 0.0005  0.0109  -0.0079 483  LEU A CG  
3549  C CD1 . LEU A 485  ? 0.4007 0.4124 0.3974 -0.0005 0.0113  -0.0078 483  LEU A CD1 
3550  C CD2 . LEU A 485  ? 0.3558 0.3612 0.3581 0.0018  0.0104  -0.0111 483  LEU A CD2 
3551  N N   . ALA A 486  ? 0.4319 0.4225 0.4299 0.0013  0.0121  0.0019  484  ALA A N   
3552  C CA  . ALA A 486  ? 0.4390 0.4259 0.4360 0.0018  0.0126  0.0040  484  ALA A CA  
3553  C C   . ALA A 486  ? 0.4564 0.4402 0.4552 0.0030  0.0129  0.0040  484  ALA A C   
3554  O O   . ALA A 486  ? 0.4411 0.4231 0.4393 0.0037  0.0133  0.0044  484  ALA A O   
3555  C CB  . ALA A 486  ? 0.4731 0.4592 0.4693 0.0013  0.0126  0.0063  484  ALA A CB  
3556  N N   . TYR A 487  ? 0.4304 0.4138 0.4315 0.0033  0.0126  0.0038  485  TYR A N   
3557  C CA  . TYR A 487  ? 0.3798 0.3608 0.3831 0.0043  0.0127  0.0045  485  TYR A CA  
3558  C C   . TYR A 487  ? 0.3994 0.3810 0.4063 0.0045  0.0119  0.0027  485  TYR A C   
3559  O O   . TYR A 487  ? 0.3627 0.3429 0.3726 0.0050  0.0117  0.0036  485  TYR A O   
3560  C CB  . TYR A 487  ? 0.4389 0.4183 0.4424 0.0046  0.0131  0.0069  485  TYR A CB  
3561  C CG  . TYR A 487  ? 0.4758 0.4543 0.4764 0.0047  0.0137  0.0083  485  TYR A CG  
3562  C CD1 . TYR A 487  ? 0.5183 0.4954 0.5178 0.0055  0.0142  0.0090  485  TYR A CD1 
3563  C CD2 . TYR A 487  ? 0.4719 0.4512 0.4714 0.0039  0.0135  0.0090  485  TYR A CD2 
3564  C CE1 . TYR A 487  ? 0.5852 0.5615 0.5827 0.0057  0.0145  0.0097  485  TYR A CE1 
3565  C CE2 . TYR A 487  ? 0.5244 0.5028 0.5223 0.0040  0.0137  0.0101  485  TYR A CE2 
3566  C CZ  . TYR A 487  ? 0.6117 0.5885 0.6086 0.0049  0.0141  0.0103  485  TYR A CZ  
3567  O OH  . TYR A 487  ? 0.6458 0.6216 0.6416 0.0051  0.0141  0.0110  485  TYR A OH  
3568  N N   . LEU A 488  ? 0.3734 0.3575 0.3806 0.0042  0.0114  0.0000  486  LEU A N   
3569  C CA  . LEU A 488  ? 0.3177 0.3028 0.3290 0.0045  0.0103  -0.0025 486  LEU A CA  
3570  C C   . LEU A 488  ? 0.3282 0.3109 0.3423 0.0054  0.0101  -0.0022 486  LEU A C   
3571  O O   . LEU A 488  ? 0.3219 0.3039 0.3406 0.0058  0.0091  -0.0030 486  LEU A O   
3572  C CB  . LEU A 488  ? 0.3538 0.3428 0.3646 0.0041  0.0098  -0.0058 486  LEU A CB  
3573  C CG  . LEU A 488  ? 0.4490 0.4395 0.4643 0.0045  0.0085  -0.0092 486  LEU A CG  
3574  C CD1 . LEU A 488  ? 0.3978 0.3874 0.4158 0.0044  0.0078  -0.0086 486  LEU A CD1 
3575  C CD2 . LEU A 488  ? 0.3378 0.3334 0.3521 0.0042  0.0081  -0.0128 486  LEU A CD2 
3576  N N   . VAL A 489  ? 0.3676 0.3492 0.3794 0.0057  0.0109  -0.0011 487  VAL A N   
3577  C CA  . VAL A 489  ? 0.3262 0.3060 0.3405 0.0065  0.0107  -0.0004 487  VAL A CA  
3578  C C   . VAL A 489  ? 0.3348 0.3126 0.3517 0.0069  0.0106  0.0023  487  VAL A C   
3579  O O   . VAL A 489  ? 0.3359 0.3129 0.3575 0.0073  0.0097  0.0025  487  VAL A O   
3580  C CB  . VAL A 489  ? 0.3457 0.3251 0.3566 0.0068  0.0115  0.0004  487  VAL A CB  
3581  C CG1 . VAL A 489  ? 0.3640 0.3416 0.3770 0.0077  0.0114  0.0021  487  VAL A CG1 
3582  C CG2 . VAL A 489  ? 0.3550 0.3368 0.3648 0.0065  0.0113  -0.0025 487  VAL A CG2 
3583  N N   . ARG A 490  ? 0.3438 0.3210 0.3582 0.0068  0.0115  0.0047  488  ARG A N   
3584  C CA  . ARG A 490  ? 0.3303 0.3063 0.3470 0.0071  0.0116  0.0075  488  ARG A CA  
3585  C C   . ARG A 490  ? 0.3722 0.3484 0.3940 0.0068  0.0104  0.0068  488  ARG A C   
3586  O O   . ARG A 490  ? 0.3732 0.3484 0.3993 0.0070  0.0098  0.0084  488  ARG A O   
3587  C CB  . ARG A 490  ? 0.3813 0.3572 0.3946 0.0071  0.0127  0.0095  488  ARG A CB  
3588  C CG  . ARG A 490  ? 0.3718 0.3474 0.3873 0.0075  0.0131  0.0126  488  ARG A CG  
3589  C CD  . ARG A 490  ? 0.3832 0.3590 0.3959 0.0076  0.0140  0.0140  488  ARG A CD  
3590  N NE  . ARG A 490  ? 0.3749 0.3510 0.3875 0.0068  0.0136  0.0129  488  ARG A NE  
3591  C CZ  . ARG A 490  ? 0.3842 0.3605 0.3936 0.0066  0.0140  0.0126  488  ARG A CZ  
3592  N NH1 . ARG A 490  ? 0.3951 0.3711 0.4014 0.0070  0.0147  0.0130  488  ARG A NH1 
3593  N NH2 . ARG A 490  ? 0.3602 0.3372 0.3701 0.0058  0.0135  0.0119  488  ARG A NH2 
3594  N N   . ARG A 491  ? 0.3648 0.3422 0.3861 0.0062  0.0099  0.0044  489  ARG A N   
3595  C CA  . ARG A 491  ? 0.3562 0.3339 0.3823 0.0059  0.0086  0.0032  489  ARG A CA  
3596  C C   . ARG A 491  ? 0.4478 0.4254 0.4791 0.0063  0.0072  0.0010  489  ARG A C   
3597  O O   . ARG A 491  ? 0.4289 0.4056 0.4658 0.0063  0.0059  0.0013  489  ARG A O   
3598  C CB  . ARG A 491  ? 0.4021 0.3820 0.4261 0.0052  0.0084  0.0011  489  ARG A CB  
3599  N N   . LEU A 492  ? 0.3982 0.3766 0.4281 0.0066  0.0071  -0.0012 490  LEU A N   
3600  C CA  . LEU A 492  ? 0.3861 0.3643 0.4213 0.0071  0.0056  -0.0036 490  LEU A CA  
3601  C C   . LEU A 492  ? 0.4106 0.3864 0.4496 0.0075  0.0053  -0.0005 490  LEU A C   
3602  O O   . LEU A 492  ? 0.3790 0.3540 0.4248 0.0078  0.0036  -0.0011 490  LEU A O   
3603  C CB  . LEU A 492  ? 0.3729 0.3531 0.4055 0.0073  0.0058  -0.0067 490  LEU A CB  
3604  C CG  . LEU A 492  ? 0.3835 0.3673 0.4130 0.0069  0.0059  -0.0101 490  LEU A CG  
3605  C CD1 . LEU A 492  ? 0.3937 0.3795 0.4200 0.0070  0.0065  -0.0119 490  LEU A CD1 
3606  C CD2 . LEU A 492  ? 0.4279 0.4134 0.4624 0.0070  0.0042  -0.0139 490  LEU A CD2 
3607  N N   . LEU A 493  ? 0.3746 0.3496 0.4099 0.0077  0.0067  0.0030  491  LEU A N   
3608  C CA  . LEU A 493  ? 0.3397 0.3133 0.3782 0.0081  0.0065  0.0064  491  LEU A CA  
3609  C C   . LEU A 493  ? 0.3981 0.3710 0.4415 0.0078  0.0058  0.0092  491  LEU A C   
3610  O O   . LEU A 493  ? 0.4439 0.4160 0.4925 0.0079  0.0049  0.0117  491  LEU A O   
3611  C CB  . LEU A 493  ? 0.4021 0.3759 0.4351 0.0084  0.0082  0.0092  491  LEU A CB  
3612  C CG  . LEU A 493  ? 0.4687 0.4430 0.4976 0.0087  0.0087  0.0071  491  LEU A CG  
3613  C CD1 . LEU A 493  ? 0.4421 0.4165 0.4677 0.0092  0.0099  0.0101  491  LEU A CD1 
3614  C CD2 . LEU A 493  ? 0.4537 0.4280 0.4871 0.0090  0.0072  0.0045  491  LEU A CD2 
3615  N N   . GLU A 494  ? 0.4262 0.3995 0.4681 0.0073  0.0062  0.0091  492  GLU A N   
3616  C CA  . GLU A 494  ? 0.4496 0.4225 0.4960 0.0069  0.0057  0.0119  492  GLU A CA  
3617  C C   . GLU A 494  ? 0.4227 0.3946 0.4776 0.0068  0.0033  0.0108  492  GLU A C   
3618  O O   . GLU A 494  ? 0.3921 0.3634 0.4525 0.0067  0.0026  0.0143  492  GLU A O   
3619  C CB  . GLU A 494  ? 0.3664 0.3400 0.4103 0.0064  0.0062  0.0110  492  GLU A CB  
3620  N N   . ASN A 495  ? 0.3894 0.3616 0.4460 0.0070  0.0021  0.0060  493  ASN A N   
3621  C CA  . ASN A 495  ? 0.4200 0.3913 0.4851 0.0071  -0.0005 0.0039  493  ASN A CA  
3622  C C   . ASN A 495  ? 0.4382 0.4092 0.5053 0.0078  -0.0014 0.0013  493  ASN A C   
3623  O O   . ASN A 495  ? 0.4236 0.3941 0.4979 0.0081  -0.0037 -0.0016 493  ASN A O   
3624  C CB  . ASN A 495  ? 0.4102 0.3825 0.4772 0.0068  -0.0016 -0.0001 493  ASN A CB  
3625  N N   . GLY A 496  ? 0.4503 0.4218 0.5118 0.0082  0.0001  0.0021  494  GLY A N   
3626  C CA  . GLY A 496  ? 0.4785 0.4501 0.5413 0.0089  -0.0006 -0.0007 494  GLY A CA  
3627  C C   . GLY A 496  ? 0.5305 0.5011 0.5942 0.0092  -0.0005 0.0029  494  GLY A C   
3628  O O   . GLY A 496  ? 0.5154 0.4859 0.5813 0.0098  -0.0013 0.0009  494  GLY A O   
3629  N N   . ALA A 497  ? 0.4511 0.4213 0.5131 0.0089  0.0007  0.0082  495  ALA A N   
3630  C CA  . ALA A 497  ? 0.4666 0.4365 0.5297 0.0092  0.0007  0.0120  495  ALA A CA  
3631  C C   . ALA A 497  ? 0.4085 0.3769 0.4815 0.0092  -0.0018 0.0134  495  ALA A C   
3632  O O   . ALA A 497  ? 0.3997 0.3673 0.4789 0.0089  -0.0034 0.0125  495  ALA A O   
3633  C CB  . ALA A 497  ? 0.3818 0.3526 0.4406 0.0090  0.0026  0.0172  495  ALA A CB  
3634  N N   . ASN A 498  ? 0.4175 0.3858 0.4926 0.0096  -0.0023 0.0158  496  ASN A N   
3635  C CA  . ASN A 498  ? 0.3902 0.3572 0.4756 0.0097  -0.0050 0.0173  496  ASN A CA  
3636  C C   . ASN A 498  ? 0.3867 0.3533 0.4779 0.0088  -0.0058 0.0218  496  ASN A C   
3637  O O   . ASN A 498  ? 0.4155 0.3805 0.5163 0.0087  -0.0085 0.0217  496  ASN A O   
3638  C CB  . ASN A 498  ? 0.4572 0.4244 0.5433 0.0101  -0.0052 0.0200  496  ASN A CB  
3639  N N   . SER A 499  ? 0.4018 0.3699 0.4877 0.0084  -0.0038 0.0258  497  SER A N   
3640  C CA  . SER A 499  ? 0.4024 0.3709 0.4931 0.0075  -0.0042 0.0305  497  SER A CA  
3641  C C   . SER A 499  ? 0.3137 0.2815 0.4054 0.0071  -0.0045 0.0275  497  SER A C   
3642  O O   . SER A 499  ? 0.3601 0.3278 0.4575 0.0063  -0.0054 0.0307  497  SER A O   
3643  C CB  . SER A 499  ? 0.4450 0.4164 0.5297 0.0074  -0.0018 0.0358  497  SER A CB  
3644  O OG  . SER A 499  ? 0.4679 0.4402 0.5423 0.0079  0.0007  0.0331  497  SER A OG  
3645  N N   . SER A 500  ? 0.3072 0.2747 0.3937 0.0074  -0.0038 0.0218  498  SER A N   
3646  C CA  . SER A 500  ? 0.2924 0.2598 0.3789 0.0070  -0.0040 0.0190  498  SER A CA  
3647  C C   . SER A 500  ? 0.3413 0.3070 0.4377 0.0069  -0.0071 0.0163  498  SER A C   
3648  O O   . SER A 500  ? 0.3192 0.2839 0.4205 0.0075  -0.0089 0.0133  498  SER A O   
3649  C CB  . SER A 500  ? 0.3613 0.3295 0.4395 0.0074  -0.0025 0.0140  498  SER A CB  
3650  O OG  . SER A 500  ? 0.3848 0.3543 0.4543 0.0075  0.0002  0.0162  498  SER A OG  
3651  N N   . PHE A 501  ? 0.2891 0.2547 0.3890 0.0062  -0.0077 0.0172  499  PHE A N   
3652  C CA  . PHE A 501  ? 0.2853 0.2494 0.3952 0.0060  -0.0109 0.0145  499  PHE A CA  
3653  C C   . PHE A 501  ? 0.3511 0.3153 0.4607 0.0068  -0.0120 0.0067  499  PHE A C   
3654  O O   . PHE A 501  ? 0.3457 0.3087 0.4637 0.0073  -0.0148 0.0037  499  PHE A O   
3655  C CB  . PHE A 501  ? 0.2650 0.2293 0.3771 0.0051  -0.0111 0.0160  499  PHE A CB  
3656  C CG  . PHE A 501  ? 0.2584 0.2213 0.3808 0.0050  -0.0144 0.0127  499  PHE A CG  
3657  C CD1 . PHE A 501  ? 0.2873 0.2485 0.4207 0.0045  -0.0170 0.0163  499  PHE A CD1 
3658  C CD2 . PHE A 501  ? 0.3328 0.2963 0.4543 0.0054  -0.0152 0.0060  499  PHE A CD2 
3659  C CE1 . PHE A 501  ? 0.3270 0.2867 0.4708 0.0044  -0.0204 0.0130  499  PHE A CE1 
3660  C CE2 . PHE A 501  ? 0.2879 0.2504 0.4192 0.0054  -0.0186 0.0024  499  PHE A CE2 
3661  C CZ  . PHE A 501  ? 0.3192 0.2794 0.4618 0.0049  -0.0212 0.0058  499  PHE A CZ  
3662  N N   . VAL A 502  ? 0.3598 0.3258 0.4603 0.0070  -0.0099 0.0034  500  VAL A N   
3663  C CA  . VAL A 502  ? 0.3528 0.3201 0.4526 0.0078  -0.0109 -0.0038 500  VAL A CA  
3664  C C   . VAL A 502  ? 0.3928 0.3600 0.4931 0.0087  -0.0113 -0.0062 500  VAL A C   
3665  O O   . VAL A 502  ? 0.4896 0.4577 0.5937 0.0095  -0.0131 -0.0121 500  VAL A O   
3666  C CB  . VAL A 502  ? 0.3785 0.3483 0.4688 0.0076  -0.0087 -0.0060 500  VAL A CB  
3667  N N   . HIS A 503  ? 0.3696 0.3364 0.4663 0.0087  -0.0098 -0.0021 501  HIS A N   
3668  C CA  . HIS A 503  ? 0.3259 0.2923 0.4245 0.0096  -0.0105 -0.0038 501  HIS A CA  
3669  C C   . HIS A 503  ? 0.4041 0.3683 0.5147 0.0098  -0.0137 -0.0031 501  HIS A C   
3670  O O   . HIS A 503  ? 0.3562 0.3202 0.4721 0.0107  -0.0158 -0.0077 501  HIS A O   
3671  C CB  . HIS A 503  ? 0.3846 0.3513 0.4763 0.0096  -0.0082 0.0005  501  HIS A CB  
3672  C CG  . HIS A 503  ? 0.4116 0.3779 0.5054 0.0104  -0.0089 -0.0004 501  HIS A CG  
3673  N ND1 . HIS A 503  ? 0.4127 0.3774 0.5125 0.0104  -0.0102 0.0041  501  HIS A ND1 
3674  C CD2 . HIS A 503  ? 0.4301 0.3977 0.5209 0.0112  -0.0087 -0.0050 501  HIS A CD2 
3675  C CE1 . HIS A 503  ? 0.4101 0.3749 0.5106 0.0112  -0.0107 0.0021  501  HIS A CE1 
3676  N NE2 . HIS A 503  ? 0.4388 0.4053 0.5339 0.0117  -0.0098 -0.0035 501  HIS A NE2 
3677  N N   . ARG A 504  ? 0.3145 0.2772 0.4301 0.0090  -0.0144 0.0026  502  ARG A N   
3678  C CA  . ARG A 504  ? 0.3379 0.2985 0.4656 0.0090  -0.0176 0.0045  502  ARG A CA  
3679  C C   . ARG A 504  ? 0.3667 0.3264 0.5034 0.0093  -0.0207 -0.0010 502  ARG A C   
3680  O O   . ARG A 504  ? 0.3529 0.3109 0.4992 0.0099  -0.0237 -0.0031 502  ARG A O   
3681  C CB  . ARG A 504  ? 0.3662 0.3261 0.4964 0.0078  -0.0172 0.0128  502  ARG A CB  
3682  C CG  . ARG A 504  ? 0.3585 0.3197 0.4815 0.0078  -0.0147 0.0180  502  ARG A CG  
3683  C CD  . ARG A 504  ? 0.3700 0.3323 0.4922 0.0067  -0.0134 0.0254  502  ARG A CD  
3684  N NE  . ARG A 504  ? 0.4033 0.3644 0.5373 0.0059  -0.0162 0.0291  502  ARG A NE  
3685  C CZ  . ARG A 504  ? 0.4388 0.3991 0.5808 0.0058  -0.0182 0.0333  502  ARG A CZ  
3686  N NH1 . ARG A 504  ? 0.4654 0.4261 0.6049 0.0064  -0.0177 0.0340  502  ARG A NH1 
3687  N NH2 . ARG A 504  ? 0.4418 0.4010 0.5949 0.0048  -0.0208 0.0370  502  ARG A NH2 
3688  N N   . ILE A 505  ? 0.3823 0.3430 0.5164 0.0089  -0.0203 -0.0036 503  ILE A N   
3689  C CA  . ILE A 505  ? 0.3719 0.3324 0.5140 0.0093  -0.0233 -0.0095 503  ILE A CA  
3690  C C   . ILE A 505  ? 0.4220 0.3837 0.5651 0.0108  -0.0245 -0.0171 503  ILE A C   
3691  O O   . ILE A 505  ? 0.4490 0.4099 0.6024 0.0116  -0.0279 -0.0215 503  ILE A O   
3692  C CB  . ILE A 505  ? 0.4308 0.3929 0.5684 0.0087  -0.0223 -0.0110 503  ILE A CB  
3693  C CG1 . ILE A 505  ? 0.4695 0.4316 0.6162 0.0091  -0.0256 -0.0169 503  ILE A CG1 
3694  C CG2 . ILE A 505  ? 0.4629 0.4281 0.5883 0.0091  -0.0193 -0.0143 503  ILE A CG2 
3695  C CD1 . ILE A 505  ? 0.3662 0.3255 0.5240 0.0082  -0.0283 -0.0130 503  ILE A CD1 
3696  N N   . ASN A 506  ? 0.4019 0.3659 0.5350 0.0113  -0.0218 -0.0187 504  ASN A N   
3697  C CA  . ASN A 506  ? 0.4625 0.4286 0.5954 0.0127  -0.0225 -0.0256 504  ASN A CA  
3698  C C   . ASN A 506  ? 0.4491 0.4135 0.5867 0.0135  -0.0236 -0.0244 504  ASN A C   
3699  O O   . ASN A 506  ? 0.5116 0.4778 0.6499 0.0147  -0.0242 -0.0300 504  ASN A O   
3700  C CB  . ASN A 506  ? 0.5054 0.4751 0.6257 0.0128  -0.0192 -0.0277 504  ASN A CB  
3701  C CG  . ASN A 506  ? 0.5120 0.4842 0.6284 0.0124  -0.0187 -0.0306 504  ASN A CG  
3702  O OD1 . ASN A 506  ? 0.5919 0.5644 0.7153 0.0127  -0.0212 -0.0344 504  ASN A OD1 
3703  N ND2 . ASN A 506  ? 0.6309 0.6051 0.7364 0.0117  -0.0155 -0.0288 504  ASN A ND2 
3704  N N   . ASP A 507  ? 0.3986 0.3601 0.5395 0.0127  -0.0237 -0.0173 505  ASP A N   
3705  C CA  . ASP A 507  ? 0.4253 0.3853 0.5708 0.0133  -0.0249 -0.0155 505  ASP A CA  
3706  C C   . ASP A 507  ? 0.4482 0.4057 0.6086 0.0137  -0.0292 -0.0169 505  ASP A C   
3707  O O   . ASP A 507  ? 0.3943 0.3496 0.5614 0.0127  -0.0307 -0.0122 505  ASP A O   
3708  C CB  . ASP A 507  ? 0.4096 0.3686 0.5511 0.0123  -0.0229 -0.0068 505  ASP A CB  
3709  C CG  . ASP A 507  ? 0.4588 0.4171 0.6026 0.0129  -0.0235 -0.0049 505  ASP A CG  
3710  O OD1 . ASP A 507  ? 0.5288 0.4861 0.6819 0.0139  -0.0265 -0.0085 505  ASP A OD1 
3711  O OD2 . ASP A 507  ? 0.5119 0.4709 0.6484 0.0125  -0.0211 -0.0001 505  ASP A OD2 
3712  N N   . PRO A 508  ? 0.5200 0.4778 0.6864 0.0152  -0.0315 -0.0230 506  PRO A N   
3713  C CA  . PRO A 508  ? 0.5311 0.4863 0.7128 0.0158  -0.0360 -0.0247 506  PRO A CA  
3714  C C   . PRO A 508  ? 0.4398 0.3917 0.6292 0.0150  -0.0375 -0.0167 506  PRO A C   
3715  O O   . PRO A 508  ? 0.5472 0.4964 0.7494 0.0147  -0.0412 -0.0156 506  PRO A O   
3716  C CB  . PRO A 508  ? 0.5803 0.5372 0.7648 0.0178  -0.0375 -0.0332 506  PRO A CB  
3717  C CG  . PRO A 508  ? 0.6164 0.5775 0.7867 0.0181  -0.0337 -0.0366 506  PRO A CG  
3718  C CD  . PRO A 508  ? 0.5084 0.4691 0.6683 0.0165  -0.0301 -0.0287 506  PRO A CD  
3719  N N   . LYS A 509  ? 0.4394 0.3916 0.6216 0.0145  -0.0350 -0.0110 507  LYS A N   
3720  C CA  . LYS A 509  ? 0.4415 0.3916 0.6300 0.0137  -0.0362 -0.0029 507  LYS A CA  
3721  C C   . LYS A 509  ? 0.4845 0.4340 0.6734 0.0119  -0.0356 0.0049  507  LYS A C   
3722  O O   . LYS A 509  ? 0.4944 0.4428 0.6896 0.0110  -0.0368 0.0123  507  LYS A O   
3723  C CB  . LYS A 509  ? 0.5187 0.4702 0.6990 0.0140  -0.0337 0.0001  507  LYS A CB  
3724  N N   . VAL A 510  ? 0.4346 0.3854 0.6171 0.0113  -0.0337 0.0038  508  VAL A N   
3725  C CA  . VAL A 510  ? 0.4003 0.3510 0.5831 0.0096  -0.0330 0.0106  508  VAL A CA  
3726  C C   . VAL A 510  ? 0.3837 0.3324 0.5782 0.0093  -0.0365 0.0083  508  VAL A C   
3727  O O   . VAL A 510  ? 0.4178 0.3670 0.6117 0.0100  -0.0370 0.0008  508  VAL A O   
3728  C CB  . VAL A 510  ? 0.4013 0.3545 0.5697 0.0092  -0.0287 0.0113  508  VAL A CB  
3729  C CG1 . VAL A 510  ? 0.3824 0.3359 0.5516 0.0076  -0.0280 0.0181  508  VAL A CG1 
3730  C CG2 . VAL A 510  ? 0.3856 0.3407 0.5432 0.0095  -0.0255 0.0131  508  VAL A CG2 
3731  N N   . SER A 511  ? 0.3462 0.2932 0.5517 0.0082  -0.0390 0.0147  509  SER A N   
3732  C CA  . SER A 511  ? 0.3459 0.2907 0.5641 0.0078  -0.0427 0.0131  509  SER A CA  
3733  C C   . SER A 511  ? 0.3334 0.2794 0.5473 0.0066  -0.0411 0.0150  509  SER A C   
3734  O O   . SER A 511  ? 0.3743 0.3224 0.5772 0.0058  -0.0373 0.0196  509  SER A O   
3735  C CB  . SER A 511  ? 0.4348 0.3773 0.6672 0.0069  -0.0463 0.0199  509  SER A CB  
3736  O OG  . SER A 511  ? 0.3646 0.3086 0.5941 0.0052  -0.0443 0.0299  509  SER A OG  
3737  N N   . ILE A 512  ? 0.3423 0.2868 0.5654 0.0065  -0.0441 0.0111  510  ILE A N   
3738  C CA  . ILE A 512  ? 0.3274 0.2727 0.5486 0.0052  -0.0431 0.0132  510  ILE A CA  
3739  C C   . ILE A 512  ? 0.3998 0.3452 0.6242 0.0034  -0.0427 0.0240  510  ILE A C   
3740  O O   . ILE A 512  ? 0.3572 0.3048 0.5736 0.0024  -0.0396 0.0282  510  ILE A O   
3741  C CB  . ILE A 512  ? 0.3532 0.2969 0.5845 0.0056  -0.0469 0.0065  510  ILE A CB  
3742  C CG1 . ILE A 512  ? 0.3469 0.2920 0.5727 0.0075  -0.0467 -0.0042 510  ILE A CG1 
3743  C CG2 . ILE A 512  ? 0.3601 0.3045 0.5908 0.0041  -0.0463 0.0094  510  ILE A CG2 
3744  C CD1 . ILE A 512  ? 0.3931 0.3376 0.6279 0.0081  -0.0503 -0.0118 510  ILE A CD1 
3745  N N   . ASP A 513  ? 0.3763 0.3199 0.6128 0.0029  -0.0458 0.0289  511  ASP A N   
3746  C CA  . ASP A 513  ? 0.3897 0.3359 0.6279 0.0010  -0.0450 0.0394  511  ASP A CA  
3747  C C   . ASP A 513  ? 0.3828 0.3311 0.6076 0.0010  -0.0403 0.0446  511  ASP A C   
3748  O O   . ASP A 513  ? 0.3676 0.3184 0.5888 -0.0003 -0.0382 0.0514  511  ASP A O   
3749  C CB  . ASP A 513  ? 0.4260 0.3738 0.6750 0.0002  -0.0482 0.0426  511  ASP A CB  
3750  C CG  . ASP A 513  ? 0.5023 0.4502 0.7648 -0.0004 -0.0527 0.0388  511  ASP A CG  
3751  O OD1 . ASP A 513  ? 0.5101 0.4583 0.7748 -0.0012 -0.0532 0.0386  511  ASP A OD1 
3752  O OD2 . ASP A 513  ? 0.6492 0.5969 0.9201 0.0001  -0.0559 0.0360  511  ASP A OD2 
3753  N N   . GLU A 514  ? 0.3483 0.2971 0.5645 0.0024  -0.0385 0.0408  512  GLU A N   
3754  C CA  . GLU A 514  ? 0.3439 0.2960 0.5459 0.0024  -0.0340 0.0442  512  GLU A CA  
3755  C C   . GLU A 514  ? 0.3603 0.3142 0.5510 0.0023  -0.0307 0.0418  512  GLU A C   
3756  O O   . GLU A 514  ? 0.3635 0.3204 0.5461 0.0017  -0.0275 0.0471  512  GLU A O   
3757  C CB  . GLU A 514  ? 0.4204 0.3723 0.6164 0.0039  -0.0331 0.0400  512  GLU A CB  
3758  C CG  . GLU A 514  ? 0.4744 0.4255 0.6785 0.0040  -0.0354 0.0446  512  GLU A CG  
3759  C CD  . GLU A 514  ? 0.5337 0.4846 0.7324 0.0055  -0.0347 0.0398  512  GLU A CD  
3760  O OE1 . GLU A 514  ? 0.5226 0.4717 0.7232 0.0068  -0.0361 0.0314  512  GLU A OE1 
3761  O OE2 . GLU A 514  ? 0.6979 0.6509 0.8903 0.0055  -0.0326 0.0443  512  GLU A OE2 
3762  N N   . LEU A 515  ? 0.3834 0.3360 0.5736 0.0030  -0.0314 0.0337  513  LEU A N   
3763  C CA  . LEU A 515  ? 0.3377 0.2921 0.5172 0.0030  -0.0284 0.0312  513  LEU A CA  
3764  C C   . LEU A 515  ? 0.3091 0.2643 0.4922 0.0015  -0.0285 0.0362  513  LEU A C   
3765  O O   . LEU A 515  ? 0.3199 0.2773 0.4936 0.0012  -0.0254 0.0376  513  LEU A O   
3766  C CB  . LEU A 515  ? 0.3517 0.3052 0.5296 0.0041  -0.0293 0.0214  513  LEU A CB  
3767  C CG  . LEU A 515  ? 0.3532 0.3070 0.5245 0.0056  -0.0283 0.0160  513  LEU A CG  
3768  C CD1 . LEU A 515  ? 0.3608 0.3145 0.5338 0.0067  -0.0300 0.0064  513  LEU A CD1 
3769  C CD2 . LEU A 515  ? 0.3460 0.3024 0.5026 0.0057  -0.0238 0.0176  513  LEU A CD2 
3770  N N   . ILE A 516  ? 0.2978 0.2513 0.4947 0.0006  -0.0320 0.0391  514  ILE A N   
3771  C CA  . ILE A 516  ? 0.3073 0.2615 0.5087 -0.0009 -0.0324 0.0440  514  ILE A CA  
3772  C C   . ILE A 516  ? 0.3131 0.2698 0.5163 -0.0022 -0.0314 0.0545  514  ILE A C   
3773  O O   . ILE A 516  ? 0.3144 0.2723 0.5228 -0.0036 -0.0318 0.0597  514  ILE A O   
3774  C CB  . ILE A 516  ? 0.3038 0.2551 0.5193 -0.0013 -0.0369 0.0408  514  ILE A CB  
3775  C CG1 . ILE A 516  ? 0.3717 0.3207 0.6014 -0.0016 -0.0409 0.0439  514  ILE A CG1 
3776  C CG2 . ILE A 516  ? 0.3244 0.2744 0.5371 0.0001  -0.0377 0.0301  514  ILE A CG2 
3777  C CD1 . ILE A 516  ? 0.3784 0.3261 0.6219 -0.0022 -0.0454 0.0407  514  ILE A CD1 
3778  N N   . ALA A 517  ? 0.2751 0.2332 0.4742 -0.0017 -0.0300 0.0577  515  ALA A N   
3779  C CA  . ALA A 517  ? 0.3232 0.2848 0.5223 -0.0028 -0.0286 0.0675  515  ALA A CA  
3780  C C   . ALA A 517  ? 0.3144 0.2798 0.5044 -0.0033 -0.0250 0.0704  515  ALA A C   
3781  O O   . ALA A 517  ? 0.2981 0.2640 0.4766 -0.0024 -0.0222 0.0655  515  ALA A O   
3782  C CB  . ALA A 517  ? 0.3380 0.3010 0.5308 -0.0020 -0.0271 0.0691  515  ALA A CB  
3783  N N   . ASP A 518  ? 0.2852 0.2535 0.4808 -0.0048 -0.0252 0.0785  516  ASP A N   
3784  C CA  . ASP A 518  ? 0.2693 0.2415 0.4581 -0.0054 -0.0221 0.0818  516  ASP A CA  
3785  C C   . ASP A 518  ? 0.2752 0.2524 0.4530 -0.0048 -0.0183 0.0860  516  ASP A C   
3786  O O   . ASP A 518  ? 0.2886 0.2691 0.4700 -0.0055 -0.0185 0.0935  516  ASP A O   
3787  C CB  . ASP A 518  ? 0.2970 0.2707 0.4975 -0.0072 -0.0241 0.0889  516  ASP A CB  
3788  C CG  . ASP A 518  ? 0.3091 0.2872 0.5039 -0.0078 -0.0211 0.0923  516  ASP A CG  
3789  O OD1 . ASP A 518  ? 0.3093 0.2891 0.4912 -0.0067 -0.0176 0.0890  516  ASP A OD1 
3790  O OD2 . ASP A 518  ? 0.3812 0.3615 0.5848 -0.0094 -0.0225 0.0980  516  ASP A OD2 
3791  N N   . PRO A 519  ? 0.2834 0.2616 0.4480 -0.0036 -0.0149 0.0815  517  PRO A N   
3792  C CA  . PRO A 519  ? 0.2810 0.2639 0.4354 -0.0030 -0.0115 0.0848  517  PRO A CA  
3793  C C   . PRO A 519  ? 0.2481 0.2371 0.4033 -0.0039 -0.0100 0.0934  517  PRO A C   
3794  O O   . PRO A 519  ? 0.2699 0.2635 0.4215 -0.0037 -0.0085 0.0983  517  PRO A O   
3795  C CB  . PRO A 519  ? 0.2843 0.2663 0.4261 -0.0017 -0.0087 0.0779  517  PRO A CB  
3796  C CG  . PRO A 519  ? 0.3202 0.2991 0.4654 -0.0021 -0.0100 0.0734  517  PRO A CG  
3797  C CD  . PRO A 519  ? 0.2575 0.2329 0.4163 -0.0029 -0.0142 0.0736  517  PRO A CD  
3798  N N   . VAL A 520  ? 0.2868 0.2765 0.4471 -0.0050 -0.0105 0.0956  518  VAL A N   
3799  C CA  . VAL A 520  ? 0.2516 0.2480 0.4130 -0.0060 -0.0089 0.1038  518  VAL A CA  
3800  C C   . VAL A 520  ? 0.3061 0.3052 0.4772 -0.0072 -0.0110 0.1120  518  VAL A C   
3801  O O   . VAL A 520  ? 0.2975 0.3030 0.4652 -0.0072 -0.0090 0.1183  518  VAL A O   
3802  C CB  . VAL A 520  ? 0.2777 0.2740 0.4435 -0.0070 -0.0093 0.1040  518  VAL A CB  
3803  C CG1 . VAL A 520  ? 0.3073 0.3111 0.4742 -0.0079 -0.0076 0.1126  518  VAL A CG1 
3804  C CG2 . VAL A 520  ? 0.2791 0.2729 0.4352 -0.0058 -0.0074 0.0961  518  VAL A CG2 
3805  N N   . GLU A 521  ? 0.3043 0.2986 0.4877 -0.0081 -0.0150 0.1120  519  GLU A N   
3806  C CA  . GLU A 521  ? 0.3233 0.3218 0.5152 -0.0092 -0.0172 0.1175  519  GLU A CA  
3807  C C   . GLU A 521  ? 0.3634 0.3621 0.5512 -0.0082 -0.0168 0.1182  519  GLU A C   
3808  O O   . GLU A 521  ? 0.3518 0.3570 0.5415 -0.0089 -0.0168 0.1243  519  GLU A O   
3809  C CB  . GLU A 521  ? 0.3395 0.3344 0.5449 -0.0103 -0.0217 0.1152  519  GLU A CB  
3810  C CG  . GLU A 521  ? 0.3587 0.3546 0.5691 -0.0114 -0.0223 0.1158  519  GLU A CG  
3811  C CD  . GLU A 521  ? 0.4300 0.4349 0.6397 -0.0124 -0.0203 0.1238  519  GLU A CD  
3812  O OE1 . GLU A 521  ? 0.4819 0.4926 0.6942 -0.0129 -0.0205 0.1297  519  GLU A OE1 
3813  O OE2 . GLU A 521  ? 0.4384 0.4451 0.6451 -0.0126 -0.0184 0.1244  519  GLU A OE2 
3814  N N   . VAL A 522  ? 0.3136 0.3061 0.4960 -0.0067 -0.0166 0.1119  520  VAL A N   
3815  C CA  . VAL A 522  ? 0.2707 0.2638 0.4482 -0.0057 -0.0160 0.1117  520  VAL A CA  
3816  C C   . VAL A 522  ? 0.3822 0.3828 0.5486 -0.0051 -0.0121 0.1158  520  VAL A C   
3817  O O   . VAL A 522  ? 0.3523 0.3572 0.5190 -0.0052 -0.0120 0.1215  520  VAL A O   
3818  C CB  . VAL A 522  ? 0.3423 0.3294 0.5146 -0.0041 -0.0163 0.1016  520  VAL A CB  
3819  C CG1 . VAL A 522  ? 0.3109 0.2992 0.4772 -0.0030 -0.0154 0.1015  520  VAL A CG1 
3820  C CG2 . VAL A 522  ? 0.3583 0.3389 0.5426 -0.0045 -0.0205 0.0976  520  VAL A CG2 
3821  N N   . VAL A 523  ? 0.3099 0.3126 0.4665 -0.0044 -0.0089 0.1128  521  VAL A N   
3822  C CA  . VAL A 523  ? 0.3028 0.3129 0.4492 -0.0037 -0.0052 0.1161  521  VAL A CA  
3823  C C   . VAL A 523  ? 0.3299 0.3474 0.4822 -0.0051 -0.0052 0.1263  521  VAL A C   
3824  O O   . VAL A 523  ? 0.3277 0.3518 0.4762 -0.0048 -0.0038 0.1314  521  VAL A O   
3825  C CB  . VAL A 523  ? 0.2442 0.2544 0.3799 -0.0026 -0.0021 0.1104  521  VAL A CB  
3826  C CG1 . VAL A 523  ? 0.3072 0.3259 0.4345 -0.0019 0.0013  0.1144  521  VAL A CG1 
3827  C CG2 . VAL A 523  ? 0.2932 0.2978 0.4214 -0.0011 -0.0017 0.1014  521  VAL A CG2 
3828  N N   . ARG A 524  ? 0.3084 0.3255 0.4703 -0.0066 -0.0069 0.1295  522  ARG A N   
3829  C CA  . ARG A 524  ? 0.3331 0.3592 0.4998 -0.0079 -0.0069 0.1367  522  ARG A CA  
3830  C C   . ARG A 524  ? 0.3659 0.3961 0.5379 -0.0085 -0.0088 0.1412  522  ARG A C   
3831  O O   . ARG A 524  ? 0.4098 0.4494 0.5811 -0.0089 -0.0076 0.1474  522  ARG A O   
3832  C CB  . ARG A 524  ? 0.3648 0.3896 0.5418 -0.0095 -0.0092 0.1368  522  ARG A CB  
3833  C CG  . ARG A 524  ? 0.3847 0.4189 0.5679 -0.0109 -0.0095 0.1443  522  ARG A CG  
3834  C CD  . ARG A 524  ? 0.4261 0.4583 0.6217 -0.0125 -0.0127 0.1445  522  ARG A CD  
3835  N NE  . ARG A 524  ? 0.4354 0.4615 0.6292 -0.0122 -0.0123 0.1391  522  ARG A NE  
3836  C CZ  . ARG A 524  ? 0.3525 0.3818 0.5408 -0.0120 -0.0095 0.1398  522  ARG A CZ  
3837  N NH1 . ARG A 524  ? 0.4230 0.4616 0.6064 -0.0118 -0.0067 0.1453  522  ARG A NH1 
3838  N NH2 . ARG A 524  ? 0.4184 0.4417 0.6062 -0.0119 -0.0096 0.1347  522  ARG A NH2 
3839  N N   . ALA A 525  ? 0.3443 0.3680 0.5217 -0.0085 -0.0117 0.1380  523  ALA A N   
3840  C CA  . ALA A 525  ? 0.3721 0.3989 0.5564 -0.0093 -0.0140 0.1420  523  ALA A CA  
3841  C C   . ALA A 525  ? 0.4192 0.4478 0.5950 -0.0079 -0.0124 0.1425  523  ALA A C   
3842  O O   . ALA A 525  ? 0.4320 0.4638 0.6124 -0.0085 -0.0140 0.1462  523  ALA A O   
3843  C CB  . ALA A 525  ? 0.3905 0.4099 0.5863 -0.0100 -0.0183 0.1384  523  ALA A CB  
3844  N N   . MET A 526  ? 0.3691 0.3957 0.5329 -0.0062 -0.0094 0.1389  524  MET A N   
3845  C CA  A MET A 526  ? 0.3833 0.4116 0.5388 -0.0048 -0.0079 0.1390  524  MET A CA  
3846  C CA  B MET A 526  ? 0.3833 0.4115 0.5390 -0.0048 -0.0079 0.1391  524  MET A CA  
3847  C C   . MET A 526  ? 0.4003 0.4401 0.5532 -0.0051 -0.0062 0.1462  524  MET A C   
3848  O O   . MET A 526  ? 0.3836 0.4301 0.5366 -0.0058 -0.0048 0.1499  524  MET A O   
3849  C CB  A MET A 526  ? 0.4182 0.4437 0.5610 -0.0029 -0.0048 0.1323  524  MET A CB  
3850  C CB  B MET A 526  ? 0.4181 0.4430 0.5613 -0.0029 -0.0050 0.1320  524  MET A CB  
3851  C CG  A MET A 526  ? 0.4229 0.4387 0.5659 -0.0023 -0.0061 0.1229  524  MET A CG  
3852  C CG  B MET A 526  ? 0.4227 0.4380 0.5664 -0.0022 -0.0067 0.1231  524  MET A CG  
3853  S SD  A MET A 526  ? 0.4806 0.4907 0.6290 -0.0020 -0.0093 0.1208  524  MET A SD  
3854  S SD  B MET A 526  ? 0.3941 0.4064 0.5237 -0.0004 -0.0035 0.1128  524  MET A SD  
3855  C CE  A MET A 526  ? 0.4362 0.4520 0.5721 -0.0004 -0.0065 0.1208  524  MET A CE  
3856  C CE  B MET A 526  ? 0.4162 0.4197 0.5472 0.0004  -0.0058 0.1047  524  MET A CE  
3857  N N   . PRO A 527  ? 0.4544 0.4970 0.6049 -0.0046 -0.0064 0.1481  525  PRO A N   
3858  C CA  . PRO A 527  ? 0.4615 0.5158 0.6098 -0.0048 -0.0050 0.1548  525  PRO A CA  
3859  C C   . PRO A 527  ? 0.4271 0.4882 0.5640 -0.0036 -0.0009 0.1552  525  PRO A C   
3860  O O   . PRO A 527  ? 0.4062 0.4769 0.5438 -0.0041 0.0002  0.1602  525  PRO A O   
3861  C CB  . PRO A 527  ? 0.4456 0.4999 0.5926 -0.0042 -0.0061 0.1553  525  PRO A CB  
3862  C CG  . PRO A 527  ? 0.4454 0.4891 0.5887 -0.0028 -0.0064 0.1481  525  PRO A CG  
3863  C CD  . PRO A 527  ? 0.4375 0.4735 0.5875 -0.0036 -0.0079 0.1443  525  PRO A CD  
3864  N N   . VAL A 528  ? 0.4233 0.4800 0.5500 -0.0018 0.0013  0.1500  526  VAL A N   
3865  C CA  . VAL A 528  ? 0.3652 0.4272 0.4814 -0.0005 0.0050  0.1485  526  VAL A CA  
3866  C C   . VAL A 528  ? 0.3473 0.4011 0.4618 -0.0002 0.0054  0.1406  526  VAL A C   
3867  O O   . VAL A 528  ? 0.3759 0.4217 0.4871 0.0007  0.0049  0.1328  526  VAL A O   
3868  C CB  . VAL A 528  ? 0.3941 0.4600 0.4985 0.0016  0.0072  0.1449  526  VAL A CB  
3869  C CG1 . VAL A 528  ? 0.4266 0.4978 0.5207 0.0030  0.0108  0.1416  526  VAL A CG1 
3870  C CG2 . VAL A 528  ? 0.4220 0.4962 0.5283 0.0012  0.0066  0.1529  526  VAL A CG2 
3871  N N   . VAL A 529  ? 0.3298 0.3860 0.4469 -0.0010 0.0063  0.1427  527  VAL A N   
3872  C CA  . VAL A 529  ? 0.3191 0.3681 0.4350 -0.0008 0.0065  0.1358  527  VAL A CA  
3873  C C   . VAL A 529  ? 0.3236 0.3725 0.4264 0.0014  0.0095  0.1281  527  VAL A C   
3874  O O   . VAL A 529  ? 0.3416 0.3986 0.4373 0.0024  0.0122  0.1294  527  VAL A O   
3875  C CB  . VAL A 529  ? 0.2767 0.3289 0.3985 -0.0021 0.0067  0.1403  527  VAL A CB  
3876  C CG1 . VAL A 529  ? 0.3086 0.3546 0.4274 -0.0017 0.0074  0.1328  527  VAL A CG1 
3877  C CG2 . VAL A 529  ? 0.3651 0.4159 0.5009 -0.0043 0.0032  0.1460  527  VAL A CG2 
3878  N N   . GLY A 530  ? 0.2937 0.3338 0.3938 0.0020  0.0088  0.1199  528  GLY A N   
3879  C CA  . GLY A 530  ? 0.2864 0.3255 0.3754 0.0038  0.0112  0.1126  528  GLY A CA  
3880  C C   . GLY A 530  ? 0.2617 0.3030 0.3427 0.0054  0.0123  0.1104  528  GLY A C   
3881  O O   . GLY A 530  ? 0.2731 0.3159 0.3447 0.0069  0.0146  0.1058  528  GLY A O   
3882  N N   . ALA A 531  ? 0.2836 0.3251 0.3682 0.0050  0.0106  0.1136  529  ALA A N   
3883  C CA  . ALA A 531  ? 0.2695 0.3129 0.3466 0.0064  0.0114  0.1114  529  ALA A CA  
3884  C C   . ALA A 531  ? 0.2467 0.2824 0.3176 0.0075  0.0116  0.1022  529  ALA A C   
3885  O O   . ALA A 531  ? 0.2970 0.3249 0.3721 0.0069  0.0100  0.0984  529  ALA A O   
3886  C CB  . ALA A 531  ? 0.2854 0.3295 0.3685 0.0057  0.0091  0.1164  529  ALA A CB  
3887  N N   . LYS A 532  ? 0.2606 0.2992 0.3220 0.0092  0.0136  0.0986  530  LYS A N   
3888  C CA  . LYS A 532  ? 0.2843 0.3168 0.3397 0.0102  0.0139  0.0906  530  LYS A CA  
3889  C C   . LYS A 532  ? 0.2891 0.3154 0.3489 0.0096  0.0114  0.0892  530  LYS A C   
3890  O O   . LYS A 532  ? 0.2662 0.2944 0.3316 0.0090  0.0098  0.0944  530  LYS A O   
3891  C CB  . LYS A 532  ? 0.3224 0.3601 0.3683 0.0120  0.0158  0.0885  530  LYS A CB  
3892  C CG  . LYS A 532  ? 0.3654 0.3976 0.4050 0.0130  0.0161  0.0808  530  LYS A CG  
3893  C CD  . LYS A 532  ? 0.2973 0.3349 0.3285 0.0148  0.0177  0.0790  530  LYS A CD  
3894  C CE  . LYS A 532  ? 0.3159 0.3587 0.3479 0.0149  0.0170  0.0835  530  LYS A CE  
3895  N NZ  . LYS A 532  ? 0.3201 0.3568 0.3547 0.0144  0.0150  0.0818  530  LYS A NZ  
3896  N N   . HIS A 533  ? 0.2452 0.2644 0.3029 0.0099  0.0111  0.0823  531  HIS A N   
3897  C CA  . HIS A 533  ? 0.2266 0.2404 0.2873 0.0097  0.0090  0.0799  531  HIS A CA  
3898  C C   . HIS A 533  ? 0.2836 0.3012 0.3406 0.0106  0.0092  0.0813  531  HIS A C   
3899  O O   . HIS A 533  ? 0.2849 0.3060 0.3337 0.0118  0.0111  0.0794  531  HIS A O   
3900  C CB  . HIS A 533  ? 0.2618 0.2690 0.3189 0.0101  0.0092  0.0721  531  HIS A CB  
3901  C CG  . HIS A 533  ? 0.2732 0.2746 0.3355 0.0097  0.0068  0.0694  531  HIS A CG  
3902  N ND1 . HIS A 533  ? 0.2817 0.2830 0.3437 0.0102  0.0060  0.0692  531  HIS A ND1 
3903  C CD2 . HIS A 533  ? 0.3444 0.3405 0.4128 0.0089  0.0051  0.0669  531  HIS A CD2 
3904  C CE1 . HIS A 533  ? 0.3698 0.3658 0.4375 0.0098  0.0039  0.0664  531  HIS A CE1 
3905  N NE2 . HIS A 533  ? 0.3869 0.3798 0.4585 0.0091  0.0033  0.0648  531  HIS A NE2 
3906  N N   . ASP A 534  ? 0.2854 0.3023 0.3490 0.0100  0.0070  0.0846  532  ASP A N   
3907  C CA  . ASP A 534  ? 0.2801 0.3009 0.3411 0.0107  0.0069  0.0867  532  ASP A CA  
3908  C C   . ASP A 534  ? 0.2970 0.3146 0.3507 0.0119  0.0075  0.0798  532  ASP A C   
3909  O O   . ASP A 534  ? 0.3628 0.3846 0.4112 0.0129  0.0083  0.0802  532  ASP A O   
3910  C CB  . ASP A 534  ? 0.3456 0.3654 0.4162 0.0097  0.0041  0.0914  532  ASP A CB  
3911  N N   . ARG A 535  ? 0.2639 0.2747 0.3173 0.0118  0.0072  0.0736  533  ARG A N   
3912  C CA  . ARG A 535  ? 0.2788 0.2863 0.3266 0.0127  0.0075  0.0675  533  ARG A CA  
3913  C C   . ARG A 535  ? 0.2673 0.2749 0.3066 0.0135  0.0098  0.0627  533  ARG A C   
3914  O O   . ARG A 535  ? 0.2993 0.3038 0.3342 0.0141  0.0100  0.0573  533  ARG A O   
3915  C CB  . ARG A 535  ? 0.3556 0.3562 0.4087 0.0122  0.0056  0.0636  533  ARG A CB  
3916  N N   . ILE A 536  ? 0.2557 0.2669 0.2928 0.0136  0.0113  0.0645  534  ILE A N   
3917  C CA  . ILE A 536  ? 0.2559 0.2675 0.2855 0.0145  0.0133  0.0603  534  ILE A CA  
3918  C C   . ILE A 536  ? 0.2575 0.2767 0.2823 0.0156  0.0148  0.0629  534  ILE A C   
3919  O O   . ILE A 536  ? 0.2928 0.3173 0.3201 0.0153  0.0152  0.0682  534  ILE A O   
3920  C CB  . ILE A 536  ? 0.2656 0.2746 0.2968 0.0138  0.0137  0.0590  534  ILE A CB  
3921  C CG1 . ILE A 536  ? 0.3136 0.3156 0.3491 0.0129  0.0122  0.0557  534  ILE A CG1 
3922  C CG2 . ILE A 536  ? 0.2610 0.2710 0.2849 0.0148  0.0157  0.0552  534  ILE A CG2 
3923  C CD1 . ILE A 536  ? 0.2999 0.2995 0.3375 0.0122  0.0124  0.0545  534  ILE A CD1 
3924  N N   . ALA A 537  ? 0.2468 0.2672 0.2650 0.0168  0.0156  0.0593  535  ALA A N   
3925  C CA  . ALA A 537  ? 0.2363 0.2644 0.2497 0.0181  0.0169  0.0609  535  ALA A CA  
3926  C C   . ALA A 537  ? 0.2416 0.2720 0.2515 0.0188  0.0186  0.0593  535  ALA A C   
3927  O O   . ALA A 537  ? 0.2314 0.2570 0.2390 0.0188  0.0190  0.0544  535  ALA A O   
3928  C CB  . ALA A 537  ? 0.2762 0.3044 0.2843 0.0192  0.0168  0.0570  535  ALA A CB  
3929  N N   . LEU A 538  ? 0.2388 0.2769 0.2484 0.0192  0.0197  0.0635  536  LEU A N   
3930  C CA  . LEU A 538  ? 0.2379 0.2796 0.2431 0.0204  0.0214  0.0613  536  LEU A CA  
3931  C C   . LEU A 538  ? 0.2712 0.3128 0.2698 0.0220  0.0219  0.0555  536  LEU A C   
3932  O O   . LEU A 538  ? 0.2462 0.2884 0.2431 0.0224  0.0211  0.0549  536  LEU A O   
3933  C CB  . LEU A 538  ? 0.2502 0.3018 0.2556 0.0209  0.0225  0.0668  536  LEU A CB  
3934  C CG  . LEU A 538  ? 0.2573 0.3101 0.2693 0.0194  0.0224  0.0727  536  LEU A CG  
3935  C CD1 . LEU A 538  ? 0.2966 0.3604 0.3084 0.0200  0.0234  0.0785  536  LEU A CD1 
3936  C CD2 . LEU A 538  ? 0.2777 0.3263 0.2904 0.0191  0.0231  0.0700  536  LEU A CD2 
3937  N N   . PRO A 539  ? 0.2285 0.2691 0.2238 0.0229  0.0229  0.0512  537  PRO A N   
3938  C CA  . PRO A 539  ? 0.2229 0.2630 0.2129 0.0243  0.0230  0.0454  537  PRO A CA  
3939  C C   . PRO A 539  ? 0.2246 0.2725 0.2110 0.0259  0.0232  0.0461  537  PRO A C   
3940  O O   . PRO A 539  ? 0.2372 0.2837 0.2210 0.0264  0.0224  0.0429  537  PRO A O   
3941  C CB  . PRO A 539  ? 0.2225 0.2618 0.2108 0.0251  0.0240  0.0420  537  PRO A CB  
3942  C CG  . PRO A 539  ? 0.2289 0.2638 0.2219 0.0234  0.0239  0.0444  537  PRO A CG  
3943  C CD  . PRO A 539  ? 0.2357 0.2744 0.2327 0.0224  0.0236  0.0509  537  PRO A CD  
3944  N N   . ALA A 540  ? 0.2328 0.2895 0.2192 0.0265  0.0242  0.0503  538  ALA A N   
3945  C CA  . ALA A 540  ? 0.2508 0.3163 0.2338 0.0281  0.0244  0.0511  538  ALA A CA  
3946  C C   . ALA A 540  ? 0.2909 0.3557 0.2751 0.0273  0.0230  0.0537  538  ALA A C   
3947  O O   . ALA A 540  ? 0.2800 0.3503 0.2607 0.0286  0.0229  0.0530  538  ALA A O   
3948  C CB  . ALA A 540  ? 0.2881 0.3639 0.2714 0.0286  0.0258  0.0560  538  ALA A CB  
3949  N N   . GLU A 541  ? 0.2707 0.3291 0.2600 0.0254  0.0219  0.0565  539  GLU A N   
3950  C CA  . GLU A 541  ? 0.2872 0.3455 0.2790 0.0246  0.0205  0.0599  539  GLU A CA  
3951  C C   . GLU A 541  ? 0.2749 0.3243 0.2669 0.0240  0.0191  0.0556  539  GLU A C   
3952  O O   . GLU A 541  ? 0.2743 0.3216 0.2697 0.0231  0.0178  0.0580  539  GLU A O   
3953  C CB  . GLU A 541  ? 0.3156 0.3748 0.3140 0.0229  0.0200  0.0671  539  GLU A CB  
3954  C CG  . GLU A 541  ? 0.3849 0.4541 0.3832 0.0234  0.0213  0.0720  539  GLU A CG  
3955  C CD  . GLU A 541  ? 0.5306 0.6011 0.5361 0.0216  0.0207  0.0797  539  GLU A CD  
3956  O OE1 . GLU A 541  ? 0.6681 0.7356 0.6781 0.0205  0.0189  0.0826  539  GLU A OE1 
3957  O OE2 . GLU A 541  ? 0.5928 0.6675 0.6000 0.0214  0.0218  0.0827  539  GLU A OE2 
3958  N N   . LEU A 542  ? 0.2476 0.2922 0.2364 0.0246  0.0195  0.0493  540  LEU A N   
3959  C CA  . LEU A 542  ? 0.2995 0.3361 0.2886 0.0239  0.0183  0.0453  540  LEU A CA  
3960  C C   . LEU A 542  ? 0.2785 0.3166 0.2665 0.0243  0.0173  0.0454  540  LEU A C   
3961  O O   . LEU A 542  ? 0.2988 0.3313 0.2890 0.0234  0.0161  0.0444  540  LEU A O   
3962  C CB  . LEU A 542  ? 0.3103 0.3434 0.2955 0.0246  0.0189  0.0390  540  LEU A CB  
3963  C CG  . LEU A 542  ? 0.3591 0.3867 0.3459 0.0238  0.0193  0.0372  540  LEU A CG  
3964  C CD1 . LEU A 542  ? 0.2947 0.3181 0.2783 0.0243  0.0192  0.0311  540  LEU A CD1 
3965  C CD2 . LEU A 542  ? 0.3384 0.3604 0.3305 0.0220  0.0185  0.0394  540  LEU A CD2 
3966  N N   . PHE A 543  ? 0.2513 0.2973 0.2358 0.0257  0.0176  0.0462  541  PHE A N   
3967  C CA  . PHE A 543  ? 0.2788 0.3267 0.2617 0.0262  0.0165  0.0460  541  PHE A CA  
3968  C C   . PHE A 543  ? 0.2792 0.3331 0.2649 0.0259  0.0160  0.0528  541  PHE A C   
3969  O O   . PHE A 543  ? 0.2823 0.3395 0.2667 0.0264  0.0151  0.0534  541  PHE A O   
3970  C CB  . PHE A 543  ? 0.2745 0.3268 0.2514 0.0282  0.0170  0.0413  541  PHE A CB  
3971  C CG  . PHE A 543  ? 0.2620 0.3090 0.2370 0.0285  0.0174  0.0352  541  PHE A CG  
3972  C CD1 . PHE A 543  ? 0.3196 0.3578 0.2960 0.0274  0.0166  0.0321  541  PHE A CD1 
3973  C CD2 . PHE A 543  ? 0.2487 0.2996 0.2207 0.0299  0.0185  0.0328  541  PHE A CD2 
3974  C CE1 . PHE A 543  ? 0.2888 0.3223 0.2638 0.0275  0.0169  0.0272  541  PHE A CE1 
3975  C CE2 . PHE A 543  ? 0.2425 0.2883 0.2134 0.0301  0.0187  0.0275  541  PHE A CE2 
3976  C CZ  . PHE A 543  ? 0.2653 0.3024 0.2377 0.0289  0.0179  0.0250  541  PHE A CZ  
3977  N N   . GLY A 544  ? 0.2561 0.3116 0.2461 0.0249  0.0163  0.0580  542  GLY A N   
3978  C CA  . GLY A 544  ? 0.3168 0.3774 0.3107 0.0243  0.0155  0.0652  542  GLY A CA  
3979  C C   . GLY A 544  ? 0.2939 0.3652 0.2835 0.0257  0.0160  0.0672  542  GLY A C   
3980  O O   . GLY A 544  ? 0.2979 0.3752 0.2828 0.0271  0.0174  0.0653  542  GLY A O   
3981  N N   . ASP A 545  ? 0.3268 0.4007 0.3180 0.0255  0.0146  0.0708  543  ASP A N   
3982  C CA  . ASP A 545  ? 0.3536 0.4385 0.3413 0.0267  0.0148  0.0737  543  ASP A CA  
3983  C C   . ASP A 545  ? 0.3593 0.4465 0.3400 0.0287  0.0151  0.0670  543  ASP A C   
3984  O O   . ASP A 545  ? 0.3621 0.4594 0.3388 0.0301  0.0155  0.0682  543  ASP A O   
3985  C CB  . ASP A 545  ? 0.4129 0.4996 0.4051 0.0258  0.0130  0.0797  543  ASP A CB  
3986  C CG  . ASP A 545  ? 0.5749 0.6602 0.5751 0.0239  0.0123  0.0869  543  ASP A CG  
3987  O OD1 . ASP A 545  ? 0.5655 0.6533 0.5667 0.0236  0.0136  0.0891  543  ASP A OD1 
3988  O OD2 . ASP A 545  ? 0.7221 0.8038 0.7280 0.0227  0.0104  0.0902  543  ASP A OD2 
3989  N N   . ALA A 546  ? 0.3117 0.3903 0.2909 0.0288  0.0148  0.0603  544  ALA A N   
3990  C CA  . ALA A 546  ? 0.3211 0.4012 0.2945 0.0305  0.0147  0.0540  544  ALA A CA  
3991  C C   . ALA A 546  ? 0.3345 0.4215 0.3031 0.0323  0.0162  0.0511  544  ALA A C   
3992  O O   . ALA A 546  ? 0.3295 0.4246 0.2937 0.0340  0.0162  0.0495  544  ALA A O   
3993  C CB  . ALA A 546  ? 0.2900 0.3594 0.2637 0.0300  0.0140  0.0479  544  ALA A CB  
3994  N N   . ARG A 547  ? 0.2757 0.3601 0.2452 0.0320  0.0175  0.0503  545  ARG A N   
3995  C CA  . ARG A 547  ? 0.3020 0.3925 0.2676 0.0338  0.0189  0.0473  545  ARG A CA  
3996  C C   . ARG A 547  ? 0.2412 0.3279 0.2094 0.0329  0.0201  0.0481  545  ARG A C   
3997  O O   . ARG A 547  ? 0.2591 0.3372 0.2316 0.0310  0.0196  0.0494  545  ARG A O   
3998  C CB  . ARG A 547  ? 0.3530 0.4416 0.3143 0.0354  0.0186  0.0390  545  ARG A CB  
3999  C CG  . ARG A 547  ? 0.3502 0.4271 0.3131 0.0344  0.0181  0.0345  545  ARG A CG  
4000  C CD  . ARG A 547  ? 0.3269 0.4023 0.2863 0.0359  0.0174  0.0271  545  ARG A CD  
4001  N NE  . ARG A 547  ? 0.3015 0.3661 0.2628 0.0345  0.0164  0.0242  545  ARG A NE  
4002  C CZ  . ARG A 547  ? 0.2712 0.3286 0.2336 0.0339  0.0166  0.0208  545  ARG A CZ  
4003  N NH1 . ARG A 547  ? 0.2801 0.3390 0.2419 0.0347  0.0177  0.0193  545  ARG A NH1 
4004  N NH2 . ARG A 547  ? 0.3121 0.3608 0.2764 0.0325  0.0157  0.0191  545  ARG A NH2 
4005  N N   . THR A 548  ? 0.2378 0.3313 0.2035 0.0343  0.0215  0.0471  546  THR A N   
4006  C CA  . THR A 548  ? 0.2286 0.3200 0.1964 0.0338  0.0228  0.0476  546  THR A CA  
4007  C C   . THR A 548  ? 0.2233 0.3070 0.1896 0.0344  0.0227  0.0402  546  THR A C   
4008  O O   . THR A 548  ? 0.2330 0.3192 0.1954 0.0363  0.0226  0.0346  546  THR A O   
4009  C CB  . THR A 548  ? 0.2708 0.3741 0.2366 0.0353  0.0243  0.0498  546  THR A CB  
4010  O OG1 . THR A 548  ? 0.3325 0.4440 0.2996 0.0348  0.0243  0.0571  546  THR A OG1 
4011  C CG2 . THR A 548  ? 0.2709 0.3724 0.2392 0.0347  0.0256  0.0509  546  THR A CG2 
4012  N N   . ASN A 549  ? 0.2182 0.2927 0.1880 0.0327  0.0226  0.0401  547  ASN A N   
4013  C CA  . ASN A 549  ? 0.2115 0.2790 0.1804 0.0330  0.0226  0.0339  547  ASN A CA  
4014  C C   . ASN A 549  ? 0.2383 0.3115 0.2049 0.0348  0.0239  0.0314  547  ASN A C   
4015  O O   . ASN A 549  ? 0.2444 0.3247 0.2117 0.0351  0.0251  0.0353  547  ASN A O   
4016  C CB  . ASN A 549  ? 0.2181 0.2764 0.1913 0.0308  0.0224  0.0354  547  ASN A CB  
4017  C CG  . ASN A 549  ? 0.2221 0.2721 0.1947 0.0307  0.0220  0.0296  547  ASN A CG  
4018  O OD1 . ASN A 549  ? 0.2305 0.2803 0.2003 0.0319  0.0215  0.0245  547  ASN A OD1 
4019  N ND2 . ASN A 549  ? 0.2382 0.2814 0.2141 0.0290  0.0220  0.0305  547  ASN A ND2 
4020  N N   . SER A 550  ? 0.2215 0.2921 0.1860 0.0361  0.0235  0.0248  548  SER A N   
4021  C CA  . SER A 550  ? 0.2068 0.2814 0.1701 0.0378  0.0246  0.0217  548  SER A CA  
4022  C C   . SER A 550  ? 0.2209 0.2909 0.1875 0.0364  0.0254  0.0239  548  SER A C   
4023  O O   . SER A 550  ? 0.2435 0.3051 0.2129 0.0343  0.0248  0.0255  548  SER A O   
4024  C CB  . SER A 550  ? 0.2258 0.2970 0.1874 0.0393  0.0236  0.0142  548  SER A CB  
4025  O OG  . SER A 550  ? 0.2266 0.2868 0.1902 0.0375  0.0226  0.0125  548  SER A OG  
4026  N N   . ALA A 551  ? 0.2403 0.3163 0.2066 0.0377  0.0267  0.0239  549  ALA A N   
4027  C CA  . ALA A 551  ? 0.2592 0.3318 0.2285 0.0367  0.0275  0.0258  549  ALA A CA  
4028  C C   . ALA A 551  ? 0.2366 0.3056 0.2056 0.0378  0.0274  0.0197  549  ALA A C   
4029  O O   . ALA A 551  ? 0.2388 0.3127 0.2054 0.0402  0.0274  0.0150  549  ALA A O   
4030  C CB  . ALA A 551  ? 0.2604 0.3425 0.2303 0.0371  0.0292  0.0308  549  ALA A CB  
4031  N N   . GLY A 552  ? 0.2269 0.2877 0.1987 0.0362  0.0272  0.0198  550  GLY A N   
4032  C CA  . GLY A 552  ? 0.2363 0.2934 0.2087 0.0370  0.0270  0.0151  550  GLY A CA  
4033  C C   . GLY A 552  ? 0.2542 0.3150 0.2282 0.0374  0.0284  0.0171  550  GLY A C   
4034  O O   . GLY A 552  ? 0.2686 0.3372 0.2427 0.0376  0.0297  0.0213  550  GLY A O   
4035  N N   . LEU A 553  ? 0.2414 0.2968 0.2171 0.0373  0.0282  0.0143  551  LEU A N   
4036  C CA  . LEU A 553  ? 0.2315 0.2896 0.2091 0.0376  0.0293  0.0154  551  LEU A CA  
4037  C C   . LEU A 553  ? 0.2413 0.2900 0.2218 0.0356  0.0287  0.0158  551  LEU A C   
4038  O O   . LEU A 553  ? 0.2662 0.3075 0.2468 0.0349  0.0273  0.0128  551  LEU A O   
4039  C CB  . LEU A 553  ? 0.2819 0.3448 0.2584 0.0405  0.0295  0.0101  551  LEU A CB  
4040  C CG  . LEU A 553  ? 0.2603 0.3342 0.2338 0.0429  0.0303  0.0091  551  LEU A CG  
4041  C CD1 . LEU A 553  ? 0.3523 0.4301 0.3254 0.0458  0.0301  0.0027  551  LEU A CD1 
4042  C CD2 . LEU A 553  ? 0.2859 0.3685 0.2597 0.0426  0.0321  0.0152  551  LEU A CD2 
4043  N N   . ASP A 554  ? 0.2349 0.2843 0.2179 0.0346  0.0296  0.0197  552  ASP A N   
4044  C CA  . ASP A 554  ? 0.2580 0.2993 0.2439 0.0326  0.0290  0.0204  552  ASP A CA  
4045  C C   . ASP A 554  ? 0.2169 0.2575 0.2037 0.0338  0.0291  0.0170  552  ASP A C   
4046  O O   . ASP A 554  ? 0.2178 0.2635 0.2059 0.0346  0.0303  0.0184  552  ASP A O   
4047  C CB  . ASP A 554  ? 0.2284 0.2704 0.2171 0.0308  0.0297  0.0263  552  ASP A CB  
4048  C CG  . ASP A 554  ? 0.2291 0.2631 0.2207 0.0287  0.0290  0.0269  552  ASP A CG  
4049  O OD1 . ASP A 554  ? 0.2548 0.2831 0.2459 0.0287  0.0281  0.0230  552  ASP A OD1 
4050  O OD2 . ASP A 554  ? 0.2637 0.2973 0.2581 0.0272  0.0292  0.0312  552  ASP A OD2 
4051  N N   . LEU A 555  ? 0.2175 0.2519 0.2042 0.0339  0.0277  0.0127  553  LEU A N   
4052  C CA  . LEU A 555  ? 0.2056 0.2389 0.1939 0.0350  0.0274  0.0094  553  LEU A CA  
4053  C C   . LEU A 555  ? 0.2247 0.2533 0.2159 0.0333  0.0274  0.0116  553  LEU A C   
4054  O O   . LEU A 555  ? 0.2426 0.2695 0.2356 0.0339  0.0270  0.0092  553  LEU A O   
4055  C CB  . LEU A 555  ? 0.2330 0.2620 0.2207 0.0358  0.0258  0.0042  553  LEU A CB  
4056  C CG  . LEU A 555  ? 0.2414 0.2756 0.2264 0.0378  0.0256  0.0012  553  LEU A CG  
4057  C CD1 . LEU A 555  ? 0.2946 0.3244 0.2802 0.0386  0.0237  -0.0041 553  LEU A CD1 
4058  C CD2 . LEU A 555  ? 0.2895 0.3335 0.2737 0.0403  0.0271  0.0007  553  LEU A CD2 
4059  N N   . SER A 556  ? 0.2084 0.2353 0.2007 0.0312  0.0278  0.0161  554  SER A N   
4060  C CA  . SER A 556  ? 0.2293 0.2534 0.2244 0.0297  0.0279  0.0186  554  SER A CA  
4061  C C   . SER A 556  ? 0.2415 0.2724 0.2382 0.0300  0.0295  0.0223  554  SER A C   
4062  O O   . SER A 556  ? 0.2347 0.2640 0.2340 0.0289  0.0297  0.0246  554  SER A O   
4063  C CB  . SER A 556  ? 0.2327 0.2504 0.2288 0.0271  0.0270  0.0207  554  SER A CB  
4064  O OG  . SER A 556  ? 0.2530 0.2733 0.2494 0.0262  0.0276  0.0246  554  SER A OG  
4065  N N   . ASN A 557  ? 0.1981 0.2366 0.1930 0.0315  0.0306  0.0232  555  ASN A N   
4066  C CA  . ASN A 557  ? 0.2055 0.2513 0.2018 0.0317  0.0321  0.0274  555  ASN A CA  
4067  C C   . ASN A 557  ? 0.2410 0.2930 0.2373 0.0341  0.0331  0.0249  555  ASN A C   
4068  O O   . ASN A 557  ? 0.2171 0.2732 0.2109 0.0364  0.0332  0.0211  555  ASN A O   
4069  C CB  . ASN A 557  ? 0.2262 0.2778 0.2208 0.0318  0.0327  0.0303  555  ASN A CB  
4070  C CG  . ASN A 557  ? 0.2176 0.2775 0.2140 0.0319  0.0342  0.0355  555  ASN A CG  
4071  O OD1 . ASN A 557  ? 0.2420 0.3081 0.2387 0.0334  0.0353  0.0350  555  ASN A OD1 
4072  N ND2 . ASN A 557  ? 0.2514 0.3116 0.2494 0.0301  0.0341  0.0406  555  ASN A ND2 
4073  N N   . GLU A 558  ? 0.2239 0.2766 0.2232 0.0337  0.0337  0.0267  556  GLU A N   
4074  C CA  . GLU A 558  ? 0.2256 0.2838 0.2253 0.0361  0.0345  0.0240  556  GLU A CA  
4075  C C   . GLU A 558  ? 0.2108 0.2803 0.2086 0.0382  0.0361  0.0245  556  GLU A C   
4076  O O   . GLU A 558  ? 0.2424 0.3169 0.2393 0.0409  0.0364  0.0201  556  GLU A O   
4077  C CB  . GLU A 558  ? 0.2429 0.3005 0.2464 0.0352  0.0349  0.0263  556  GLU A CB  
4078  C CG  . GLU A 558  ? 0.2567 0.3044 0.2620 0.0336  0.0334  0.0250  556  GLU A CG  
4079  C CD  . GLU A 558  ? 0.2226 0.2662 0.2273 0.0350  0.0321  0.0192  556  GLU A CD  
4080  O OE1 . GLU A 558  ? 0.2367 0.2850 0.2402 0.0376  0.0324  0.0155  556  GLU A OE1 
4081  O OE2 . GLU A 558  ? 0.2314 0.2670 0.2372 0.0335  0.0307  0.0185  556  GLU A OE2 
4082  N N   . GLU A 559  ? 0.2208 0.2952 0.2185 0.0372  0.0370  0.0298  557  GLU A N   
4083  C CA  . GLU A 559  ? 0.2531 0.3391 0.2487 0.0391  0.0385  0.0306  557  GLU A CA  
4084  C C   . GLU A 559  ? 0.2337 0.3206 0.2253 0.0411  0.0378  0.0256  557  GLU A C   
4085  O O   . GLU A 559  ? 0.2468 0.3417 0.2365 0.0438  0.0385  0.0220  557  GLU A O   
4086  C CB  . GLU A 559  ? 0.2835 0.3737 0.2799 0.0373  0.0392  0.0378  557  GLU A CB  
4087  C CG  . GLU A 559  ? 0.2739 0.3648 0.2749 0.0355  0.0398  0.0435  557  GLU A CG  
4088  C CD  . GLU A 559  ? 0.4009 0.4950 0.4036 0.0335  0.0400  0.0505  557  GLU A CD  
4089  O OE1 . GLU A 559  ? 0.4910 0.5880 0.4909 0.0339  0.0399  0.0511  557  GLU A OE1 
4090  O OE2 . GLU A 559  ? 0.3712 0.4648 0.3783 0.0316  0.0402  0.0556  557  GLU A OE2 
4091  N N   . THR A 560  ? 0.2260 0.3051 0.2165 0.0396  0.0363  0.0249  558  THR A N   
4092  C CA  . THR A 560  ? 0.2474 0.3267 0.2344 0.0412  0.0355  0.0201  558  THR A CA  
4093  C C   . THR A 560  ? 0.2167 0.2940 0.2039 0.0434  0.0347  0.0132  558  THR A C   
4094  O O   . THR A 560  ? 0.2416 0.3246 0.2267 0.0460  0.0347  0.0088  558  THR A O   
4095  C CB  . THR A 560  ? 0.2420 0.3125 0.2285 0.0391  0.0340  0.0208  558  THR A CB  
4096  O OG1 . THR A 560  ? 0.2655 0.3379 0.2527 0.0372  0.0345  0.0272  558  THR A OG1 
4097  C CG2 . THR A 560  ? 0.2688 0.3396 0.2520 0.0406  0.0330  0.0161  558  THR A CG2 
4098  N N   . LEU A 561  ? 0.2303 0.2997 0.2202 0.0423  0.0339  0.0123  559  LEU A N   
4099  C CA  . LEU A 561  ? 0.2014 0.2683 0.1922 0.0442  0.0328  0.0061  559  LEU A CA  
4100  C C   . LEU A 561  ? 0.2175 0.2941 0.2088 0.0471  0.0341  0.0038  559  LEU A C   
4101  O O   . LEU A 561  ? 0.2376 0.3164 0.2286 0.0497  0.0333  -0.0022 559  LEU A O   
4102  C CB  . LEU A 561  ? 0.1990 0.2563 0.1930 0.0423  0.0317  0.0064  559  LEU A CB  
4103  C CG  . LEU A 561  ? 0.1943 0.2420 0.1877 0.0399  0.0302  0.0071  559  LEU A CG  
4104  C CD1 . LEU A 561  ? 0.2056 0.2454 0.2021 0.0380  0.0294  0.0080  559  LEU A CD1 
4105  C CD2 . LEU A 561  ? 0.2340 0.2794 0.2258 0.0411  0.0287  0.0020  559  LEU A CD2 
4106  N N   . ALA A 562  ? 0.2200 0.3028 0.2125 0.0468  0.0358  0.0083  560  ALA A N   
4107  C CA  . ALA A 562  ? 0.2464 0.3392 0.2393 0.0496  0.0372  0.0063  560  ALA A CA  
4108  C C   . ALA A 562  ? 0.2386 0.3420 0.2281 0.0520  0.0380  0.0042  560  ALA A C   
4109  O O   . ALA A 562  ? 0.2496 0.3588 0.2387 0.0552  0.0380  -0.0014 560  ALA A O   
4110  C CB  . ALA A 562  ? 0.2746 0.3719 0.2699 0.0484  0.0389  0.0121  560  ALA A CB  
4111  N N   . SER A 563  ? 0.2286 0.3345 0.2155 0.0507  0.0385  0.0085  561  SER A N   
4112  C CA  A SER A 563  ? 0.2497 0.3659 0.2330 0.0529  0.0391  0.0070  561  SER A CA  
4113  C CA  B SER A 563  ? 0.2494 0.3657 0.2327 0.0530  0.0391  0.0069  561  SER A CA  
4114  C C   . SER A 563  ? 0.2456 0.3583 0.2272 0.0546  0.0373  -0.0002 561  SER A C   
4115  O O   . SER A 563  ? 0.2739 0.3948 0.2537 0.0577  0.0374  -0.0052 561  SER A O   
4116  C CB  A SER A 563  ? 0.2745 0.3931 0.2561 0.0507  0.0398  0.0138  561  SER A CB  
4117  C CB  B SER A 563  ? 0.2753 0.3952 0.2569 0.0510  0.0400  0.0138  561  SER A CB  
4118  O OG  A SER A 563  ? 0.2975 0.4258 0.2754 0.0527  0.0402  0.0126  561  SER A OG  
4119  O OG  B SER A 563  ? 0.3237 0.4332 0.3048 0.0487  0.0384  0.0148  561  SER A OG  
4120  N N   . LEU A 564  ? 0.2512 0.3517 0.2334 0.0527  0.0354  -0.0009 562  LEU A N   
4121  C CA  . LEU A 564  ? 0.2619 0.3582 0.2432 0.0540  0.0335  -0.0074 562  LEU A CA  
4122  C C   . LEU A 564  ? 0.2397 0.3362 0.2234 0.0566  0.0326  -0.0142 562  LEU A C   
4123  O O   . LEU A 564  ? 0.2606 0.3611 0.2434 0.0593  0.0317  -0.0203 562  LEU A O   
4124  C CB  . LEU A 564  ? 0.2598 0.3433 0.2417 0.0510  0.0318  -0.0061 562  LEU A CB  
4125  C CG  . LEU A 564  ? 0.3275 0.4065 0.3082 0.0515  0.0298  -0.0107 562  LEU A CG  
4126  C CD1 . LEU A 564  ? 0.2816 0.3690 0.2583 0.0527  0.0304  -0.0106 562  LEU A CD1 
4127  C CD2 . LEU A 564  ? 0.2933 0.3607 0.2748 0.0483  0.0286  -0.0082 562  LEU A CD2 
4128  N N   . THR A 565  ? 0.2418 0.3346 0.2291 0.0561  0.0327  -0.0134 563  THR A N   
4129  C CA  . THR A 565  ? 0.2544 0.3476 0.2446 0.0587  0.0318  -0.0196 563  THR A CA  
4130  C C   . THR A 565  ? 0.2343 0.3408 0.2232 0.0624  0.0329  -0.0238 563  THR A C   
4131  O O   . THR A 565  ? 0.2603 0.3680 0.2500 0.0652  0.0314  -0.0309 563  THR A O   
4132  C CB  . THR A 565  ? 0.2497 0.3398 0.2437 0.0576  0.0324  -0.0171 563  THR A CB  
4133  O OG1 . THR A 565  ? 0.2719 0.3499 0.2674 0.0544  0.0312  -0.0142 563  THR A OG1 
4134  C CG2 . THR A 565  ? 0.2769 0.3684 0.2744 0.0606  0.0315  -0.0235 563  THR A CG2 
4135  N N   . GLU A 566  ? 0.2717 0.3884 0.2585 0.0626  0.0353  -0.0193 564  GLU A N   
4136  C CA  . GLU A 566  ? 0.2593 0.3902 0.2445 0.0662  0.0365  -0.0228 564  GLU A CA  
4137  C C   . GLU A 566  ? 0.2523 0.3874 0.2339 0.0678  0.0357  -0.0266 564  GLU A C   
4138  O O   . GLU A 566  ? 0.2815 0.4229 0.2631 0.0713  0.0350  -0.0338 564  GLU A O   
4139  C CB  . GLU A 566  ? 0.2979 0.4390 0.2819 0.0656  0.0394  -0.0161 564  GLU A CB  
4140  C CG  . GLU A 566  ? 0.3996 0.5376 0.3875 0.0643  0.0402  -0.0128 564  GLU A CG  
4141  C CD  . GLU A 566  ? 0.4418 0.5789 0.4335 0.0670  0.0393  -0.0197 564  GLU A CD  
4142  O OE1 . GLU A 566  ? 0.4905 0.6373 0.4817 0.0706  0.0395  -0.0256 564  GLU A OE1 
4143  O OE2 . GLU A 566  ? 0.4586 0.5855 0.4538 0.0654  0.0382  -0.0194 564  GLU A OE2 
4144  N N   . ALA A 567  ? 0.2407 0.3722 0.2195 0.0653  0.0355  -0.0222 565  ALA A N   
4145  C CA  . ALA A 567  ? 0.2745 0.4099 0.2498 0.0667  0.0346  -0.0255 565  ALA A CA  
4146  C C   . ALA A 567  ? 0.2310 0.3585 0.2082 0.0680  0.0318  -0.0334 565  ALA A C   
4147  O O   . ALA A 567  ? 0.2555 0.3890 0.2313 0.0708  0.0309  -0.0395 565  ALA A O   
4148  C CB  . ALA A 567  ? 0.2871 0.4192 0.2597 0.0636  0.0349  -0.0189 565  ALA A CB  
4149  N N   . LEU A 568  ? 0.2515 0.3661 0.2322 0.0660  0.0303  -0.0333 566  LEU A N   
4150  C CA  . LEU A 568  ? 0.2179 0.3246 0.2013 0.0669  0.0275  -0.0400 566  LEU A CA  
4151  C C   . LEU A 568  ? 0.2372 0.3492 0.2237 0.0707  0.0267  -0.0475 566  LEU A C   
4152  O O   . LEU A 568  ? 0.2618 0.3753 0.2490 0.0732  0.0248  -0.0546 566  LEU A O   
4153  C CB  . LEU A 568  ? 0.2230 0.3155 0.2095 0.0637  0.0262  -0.0374 566  LEU A CB  
4154  C CG  . LEU A 568  ? 0.2198 0.3060 0.2037 0.0601  0.0264  -0.0312 566  LEU A CG  
4155  C CD1 . LEU A 568  ? 0.2431 0.3172 0.2302 0.0572  0.0254  -0.0286 566  LEU A CD1 
4156  C CD2 . LEU A 568  ? 0.2642 0.3495 0.2458 0.0604  0.0249  -0.0340 566  LEU A CD2 
4157  N N   . ARG A 569  ? 0.2397 0.3548 0.2285 0.0713  0.0281  -0.0463 567  ARG A N   
4158  C CA  . ARG A 569  ? 0.2620 0.3839 0.2538 0.0752  0.0277  -0.0533 567  ARG A CA  
4159  C C   . ARG A 569  ? 0.2463 0.3823 0.2347 0.0786  0.0285  -0.0575 567  ARG A C   
4160  O O   . ARG A 569  ? 0.2899 0.4289 0.2803 0.0819  0.0267  -0.0659 567  ARG A O   
4161  C CB  . ARG A 569  ? 0.2694 0.3940 0.2635 0.0751  0.0296  -0.0502 567  ARG A CB  
4162  C CG  . ARG A 569  ? 0.3296 0.4411 0.3281 0.0725  0.0283  -0.0479 567  ARG A CG  
4163  C CD  . ARG A 569  ? 0.3466 0.4613 0.3473 0.0725  0.0302  -0.0448 567  ARG A CD  
4164  N NE  . ARG A 569  ? 0.3864 0.4891 0.3906 0.0695  0.0292  -0.0413 567  ARG A NE  
4165  C CZ  . ARG A 569  ? 0.5158 0.6187 0.5220 0.0685  0.0306  -0.0373 567  ARG A CZ  
4166  N NH1 . ARG A 569  ? 0.5023 0.6164 0.5075 0.0700  0.0331  -0.0357 567  ARG A NH1 
4167  N NH2 . ARG A 569  ? 0.5469 0.6387 0.5560 0.0659  0.0294  -0.0346 567  ARG A NH2 
4168  N N   . GLU A 570  ? 0.2493 0.3941 0.2327 0.0778  0.0310  -0.0519 568  GLU A N   
4169  C CA  . GLU A 570  ? 0.2532 0.4125 0.2328 0.0809  0.0318  -0.0552 568  GLU A CA  
4170  C C   . GLU A 570  ? 0.3116 0.4685 0.2900 0.0819  0.0294  -0.0607 568  GLU A C   
4171  O O   . GLU A 570  ? 0.3292 0.4952 0.3070 0.0856  0.0287  -0.0679 568  GLU A O   
4172  C CB  . GLU A 570  ? 0.3113 0.4798 0.2864 0.0794  0.0348  -0.0469 568  GLU A CB  
4173  C CG  . GLU A 570  ? 0.3431 0.5181 0.3195 0.0793  0.0373  -0.0426 568  GLU A CG  
4174  C CD  . GLU A 570  ? 0.4715 0.6525 0.4446 0.0768  0.0398  -0.0328 568  GLU A CD  
4175  O OE1 . GLU A 570  ? 0.5774 0.7536 0.5481 0.0743  0.0394  -0.0285 568  GLU A OE1 
4176  O OE2 . GLU A 570  ? 0.6283 0.8189 0.6018 0.0774  0.0422  -0.0295 568  GLU A OE2 
4177  N N   . SER A 571  ? 0.2590 0.4037 0.2370 0.0787  0.0280  -0.0576 569  SER A N   
4178  C CA  . SER A 571  ? 0.2709 0.4127 0.2481 0.0794  0.0256  -0.0626 569  SER A CA  
4179  C C   . SER A 571  ? 0.2953 0.4330 0.2777 0.0820  0.0227  -0.0719 569  SER A C   
4180  O O   . SER A 571  ? 0.3039 0.4450 0.2859 0.0844  0.0208  -0.0785 569  SER A O   
4181  C CB  . SER A 571  ? 0.2614 0.3909 0.2378 0.0753  0.0248  -0.0571 569  SER A CB  
4182  O OG  . SER A 571  ? 0.2734 0.3895 0.2547 0.0736  0.0230  -0.0578 569  SER A OG  
4183  N N   . ALA A 572  ? 0.3016 0.4322 0.2891 0.0817  0.0220  -0.0727 570  ALA A N   
4184  C CA  . ALA A 572  ? 0.3220 0.4483 0.3155 0.0841  0.0190  -0.0812 570  ALA A CA  
4185  C C   . ALA A 572  ? 0.3635 0.5029 0.3581 0.0890  0.0192  -0.0888 570  ALA A C   
4186  O O   . ALA A 572  ? 0.3885 0.5263 0.3880 0.0916  0.0164  -0.0971 570  ALA A O   
4187  C CB  . ALA A 572  ? 0.3411 0.4556 0.3401 0.0821  0.0181  -0.0791 570  ALA A CB  
4188  N N   . ALA A 573  ? 0.3205 0.4728 0.3111 0.0901  0.0223  -0.0861 571  ALA A N   
4189  C CA  . ALA A 573  ? 0.3603 0.5268 0.3511 0.0946  0.0228  -0.0928 571  ALA A CA  
4190  C C   . ALA A 573  ? 0.4180 0.5930 0.4042 0.0952  0.0218  -0.0947 571  ALA A C   
4191  O O   . ALA A 573  ? 0.4530 0.6384 0.4389 0.0971  0.0212  -0.0982 571  ALA A O   
4192  C CB  . ALA A 573  ? 0.3641 0.5396 0.3534 0.0946  0.0261  -0.0876 571  ALA A CB  
4193  N N   . MET A 574  ? 0.3544 0.5256 0.3372 0.0938  0.0216  -0.0926 572  MET A N   
4194  C CA  . MET A 574  ? 0.3663 0.5453 0.3449 0.0942  0.0206  -0.0941 572  MET A CA  
4195  C C   . MET A 574  ? 0.3872 0.5615 0.3698 0.0958  0.0163  -0.1030 572  MET A C   
4196  O O   . MET A 574  ? 0.3357 0.4981 0.3235 0.0955  0.0142  -0.1062 572  MET A O   
4197  C CB  . MET A 574  ? 0.4144 0.5921 0.3874 0.0919  0.0225  -0.0872 572  MET A CB  
4198  C CG  . MET A 574  ? 0.4140 0.5987 0.3829 0.0903  0.0264  -0.0780 572  MET A CG  
4199  S SD  . MET A 574  ? 0.4053 0.5839 0.3697 0.0857  0.0274  -0.0679 572  MET A SD  
4200  C CE  . MET A 574  ? 0.5039 0.6917 0.4657 0.0842  0.0315  -0.0579 572  MET A CE  
4201  N N   . LYS A 575  ? 0.3672 0.5517 0.3481 0.0974  0.0149  -0.1069 573  LYS A N   
4202  C CA  . LYS A 575  ? 0.3974 0.5794 0.3823 0.0990  0.0107  -0.1155 573  LYS A CA  
4203  C C   . LYS A 575  ? 0.3806 0.5593 0.3624 0.0978  0.0096  -0.1148 573  LYS A C   
4204  O O   . LYS A 575  ? 0.3667 0.5540 0.3453 0.0986  0.0087  -0.1164 573  LYS A O   
4205  C CB  . LYS A 575  ? 0.4226 0.6178 0.4079 0.1017  0.0094  -0.1208 573  LYS A CB  
4206  N N   . TRP A 576  ? 0.3335 0.4993 0.3163 0.0958  0.0096  -0.1124 574  TRP A N   
4207  C CA  . TRP A 576  ? 0.3068 0.4681 0.2868 0.0943  0.0089  -0.1110 574  TRP A CA  
4208  C C   . TRP A 576  ? 0.2722 0.4323 0.2558 0.0957  0.0046  -0.1190 574  TRP A C   
4209  O O   . TRP A 576  ? 0.2946 0.4484 0.2853 0.0966  0.0016  -0.1249 574  TRP A O   
4210  C CB  . TRP A 576  ? 0.2864 0.4337 0.2681 0.0922  0.0094  -0.1077 574  TRP A CB  
4211  C CG  . TRP A 576  ? 0.2694 0.4153 0.2483 0.0895  0.0129  -0.0982 574  TRP A CG  
4212  C CD1 . TRP A 576  ? 0.2741 0.4136 0.2566 0.0882  0.0136  -0.0954 574  TRP A CD1 
4213  C CD2 . TRP A 576  ? 0.2688 0.4192 0.2413 0.0872  0.0157  -0.0897 574  TRP A CD2 
4214  N NE1 . TRP A 576  ? 0.2845 0.4243 0.2633 0.0853  0.0167  -0.0859 574  TRP A NE1 
4215  C CE2 . TRP A 576  ? 0.2787 0.4249 0.2515 0.0846  0.0180  -0.0822 574  TRP A CE2 
4216  C CE3 . TRP A 576  ? 0.2576 0.4152 0.2244 0.0871  0.0163  -0.0877 574  TRP A CE3 
4217  C CZ2 . TRP A 576  ? 0.2697 0.4184 0.2379 0.0819  0.0207  -0.0730 574  TRP A CZ2 
4218  C CZ3 . TRP A 576  ? 0.2724 0.4324 0.2345 0.0844  0.0191  -0.0782 574  TRP A CZ3 
4219  C CH2 . TRP A 576  ? 0.3182 0.4738 0.2813 0.0818  0.0212  -0.0710 574  TRP A CH2 
4220  N N   . THR A 577  ? 0.2827 0.4491 0.2619 0.0957  0.0042  -0.1189 575  THR A N   
4221  C CA  . THR A 577  ? 0.2639 0.4294 0.2464 0.0968  0.0001  -0.1260 575  THR A CA  
4222  C C   . THR A 577  ? 0.2948 0.4574 0.2732 0.0952  0.0000  -0.1233 575  THR A C   
4223  O O   . THR A 577  ? 0.3016 0.4668 0.2737 0.0937  0.0031  -0.1162 575  THR A O   
4224  C CB  . THR A 577  ? 0.2843 0.4637 0.2665 0.0995  -0.0012 -0.1310 575  THR A CB  
4225  O OG1 . THR A 577  ? 0.3322 0.5233 0.3069 0.0993  0.0015  -0.1256 575  THR A OG1 
4226  C CG2 . THR A 577  ? 0.3398 0.5230 0.3261 0.1013  -0.0012 -0.1339 575  THR A CG2 
4227  N N   . ALA A 578  ? 0.3049 0.4622 0.2874 0.0955  -0.0038 -0.1291 576  ALA A N   
4228  C CA  . ALA A 578  ? 0.2560 0.4119 0.2353 0.0944  -0.0046 -0.1281 576  ALA A CA  
4229  C C   . ALA A 578  ? 0.2871 0.4483 0.2696 0.0964  -0.0084 -0.1357 576  ALA A C   
4230  O O   . ALA A 578  ? 0.2971 0.4535 0.2870 0.0975  -0.0117 -0.1421 576  ALA A O   
4231  C CB  . ALA A 578  ? 0.2866 0.4273 0.2685 0.0922  -0.0055 -0.1267 576  ALA A CB  
4232  N N   . LEU A 579  ? 0.2775 0.4488 0.2549 0.0970  -0.0081 -0.1350 577  LEU A N   
4233  C CA  . LEU A 579  ? 0.2869 0.4657 0.2667 0.0992  -0.0115 -0.1419 577  LEU A CA  
4234  C C   . LEU A 579  ? 0.3111 0.4892 0.2876 0.0981  -0.0123 -0.1407 577  LEU A C   
4235  O O   . LEU A 579  ? 0.2895 0.4659 0.2601 0.0961  -0.0096 -0.1337 577  LEU A O   
4236  C CB  . LEU A 579  ? 0.3052 0.5004 0.2817 0.1014  -0.0102 -0.1423 577  LEU A CB  
4237  C CG  . LEU A 579  ? 0.3590 0.5582 0.3364 0.1023  -0.0082 -0.1415 577  LEU A CG  
4238  C CD1 . LEU A 579  ? 0.3738 0.5904 0.3475 0.1044  -0.0071 -0.1414 577  LEU A CD1 
4239  C CD2 . LEU A 579  ? 0.3983 0.5905 0.3845 0.1035  -0.0113 -0.1486 577  LEU A CD2 
4240  N N   . PRO A 580  ? 0.3100 0.4896 0.2902 0.0994  -0.0161 -0.1474 578  PRO A N   
4241  C CA  . PRO A 580  ? 0.2839 0.4655 0.2607 0.0988  -0.0168 -0.1464 578  PRO A CA  
4242  C C   . PRO A 580  ? 0.3534 0.5500 0.3228 0.0996  -0.0143 -0.1424 578  PRO A C   
4243  O O   . PRO A 580  ? 0.3698 0.5784 0.3398 0.1021  -0.0153 -0.1464 578  PRO A O   
4244  C CB  . PRO A 580  ? 0.3397 0.5211 0.3234 0.1005  -0.0216 -0.1553 578  PRO A CB  
4245  C CG  . PRO A 580  ? 0.3324 0.5078 0.3240 0.1014  -0.0235 -0.1601 578  PRO A CG  
4246  C CD  . PRO A 580  ? 0.3158 0.4963 0.3041 0.1017  -0.0199 -0.1561 578  PRO A CD  
4247  N N   . GLN A 581  ? 0.2923 0.4885 0.2551 0.0975  -0.0111 -0.1342 579  GLN A N   
4248  C CA  . GLN A 581  ? 0.3038 0.5136 0.2599 0.0978  -0.0084 -0.1287 579  GLN A CA  
4249  C C   . GLN A 581  ? 0.3262 0.5393 0.2794 0.0975  -0.0097 -0.1283 579  GLN A C   
4250  O O   . GLN A 581  ? 0.3248 0.5335 0.2737 0.0953  -0.0082 -0.1223 579  GLN A O   
4251  C CB  . GLN A 581  ? 0.2954 0.5029 0.2467 0.0956  -0.0042 -0.1194 579  GLN A CB  
4252  C CG  . GLN A 581  ? 0.2739 0.4791 0.2278 0.0959  -0.0026 -0.1192 579  GLN A CG  
4253  C CD  . GLN A 581  ? 0.3268 0.5462 0.2805 0.0982  -0.0021 -0.1208 579  GLN A CD  
4254  O OE1 . GLN A 581  ? 0.3340 0.5658 0.2852 0.0996  -0.0026 -0.1214 579  GLN A OE1 
4255  N NE2 . GLN A 581  ? 0.3212 0.5393 0.2776 0.0988  -0.0011 -0.1214 579  GLN A NE2 
4256  N N   . LEU A 582  ? 0.3003 0.5212 0.2560 0.0999  -0.0126 -0.1351 580  LEU A N   
4257  C CA  . LEU A 582  ? 0.3131 0.5389 0.2666 0.1000  -0.0140 -0.1355 580  LEU A CA  
4258  C C   . LEU A 582  ? 0.3060 0.5454 0.2526 0.1000  -0.0112 -0.1286 580  LEU A C   
4259  O O   . LEU A 582  ? 0.3500 0.5968 0.2945 0.1003  -0.0086 -0.1248 580  LEU A O   
4260  C CB  . LEU A 582  ? 0.3109 0.5412 0.2700 0.1027  -0.0181 -0.1452 580  LEU A CB  
4261  C CG  . LEU A 582  ? 0.4049 0.6218 0.3705 0.1022  -0.0218 -0.1511 580  LEU A CG  
4262  C CD1 . LEU A 582  ? 0.3826 0.5865 0.3528 0.1011  -0.0218 -0.1518 580  LEU A CD1 
4263  C CD2 . LEU A 582  ? 0.4653 0.6886 0.4364 0.1050  -0.0258 -0.1602 580  LEU A CD2 
4264  N N   . ALA A 583  ? 0.3193 0.5622 0.2627 0.0995  -0.0118 -0.1268 581  ALA A N   
4265  C CA  . ALA A 583  ? 0.3350 0.5913 0.2727 0.0994  -0.0095 -0.1201 581  ALA A CA  
4266  C C   . ALA A 583  ? 0.3326 0.6045 0.2711 0.1023  -0.0097 -0.1233 581  ALA A C   
4267  O O   . ALA A 583  ? 0.4413 0.7240 0.3759 0.1021  -0.0070 -0.1170 581  ALA A O   
4268  C CB  . ALA A 583  ? 0.3305 0.5886 0.2657 0.0988  -0.0108 -0.1191 581  ALA A CB  
4269  N N   . THR A 584  ? 0.3553 0.6287 0.2991 0.1048  -0.0128 -0.1328 582  THR A N   
4270  C CA  . THR A 584  ? 0.4024 0.6909 0.3477 0.1079  -0.0135 -0.1373 582  THR A CA  
4271  C C   . THR A 584  ? 0.4076 0.6966 0.3548 0.1086  -0.0121 -0.1378 582  THR A C   
4272  O O   . THR A 584  ? 0.4487 0.7510 0.3967 0.1111  -0.0123 -0.1405 582  THR A O   
4273  C CB  . THR A 584  ? 0.4569 0.7467 0.4078 0.1105  -0.0178 -0.1478 582  THR A CB  
4274  O OG1 . THR A 584  ? 0.4459 0.7205 0.4027 0.1100  -0.0200 -0.1529 582  THR A OG1 
4275  C CG2 . THR A 584  ? 0.3909 0.6836 0.3399 0.1103  -0.0192 -0.1477 582  THR A CG2 
4276  N N   . GLY A 585  ? 0.3738 0.6491 0.3220 0.1066  -0.0109 -0.1354 583  GLY A N   
4277  C CA  . GLY A 585  ? 0.3847 0.6594 0.3351 0.1072  -0.0096 -0.1359 583  GLY A CA  
4278  C C   . GLY A 585  ? 0.3985 0.6584 0.3551 0.1070  -0.0117 -0.1417 583  GLY A C   
4279  O O   . GLY A 585  ? 0.4022 0.6531 0.3621 0.1067  -0.0145 -0.1460 583  GLY A O   
4280  N N   . PRO A 586  ? 0.3707 0.6280 0.3294 0.1072  -0.0105 -0.1416 584  PRO A N   
4281  C CA  . PRO A 586  ? 0.3622 0.6057 0.3275 0.1070  -0.0125 -0.1467 584  PRO A CA  
4282  C C   . PRO A 586  ? 0.4449 0.6892 0.4169 0.1094  -0.0171 -0.1569 584  PRO A C   
4283  O O   . PRO A 586  ? 0.4016 0.6590 0.3744 0.1121  -0.0184 -0.1615 584  PRO A O   
4284  C CB  . PRO A 586  ? 0.4675 0.7131 0.4336 0.1075  -0.0104 -0.1454 584  PRO A CB  
4285  C CG  . PRO A 586  ? 0.4664 0.7247 0.4257 0.1072  -0.0068 -0.1379 584  PRO A CG  
4286  C CD  . PRO A 586  ? 0.4010 0.6696 0.3571 0.1080  -0.0077 -0.1380 584  PRO A CD  
4287  N N   . ALA A 587  ? 0.3765 0.6067 0.3535 0.1084  -0.0196 -0.1603 585  ALA A N   
4288  C CA  . ALA A 587  ? 0.4102 0.6390 0.3947 0.1102  -0.0243 -0.1695 585  ALA A CA  
4289  C C   . ALA A 587  ? 0.4187 0.6395 0.4110 0.1108  -0.0261 -0.1743 585  ALA A C   
4290  O O   . ALA A 587  ? 0.4024 0.6141 0.3947 0.1090  -0.0241 -0.1702 585  ALA A O   
4291  C CB  . ALA A 587  ? 0.4338 0.6529 0.4195 0.1086  -0.0264 -0.1700 585  ALA A CB  
4292  N N   . ALA A 588  ? 0.4126 0.6371 0.4119 0.1134  -0.0300 -0.1830 586  ALA A N   
4293  C CA  . ALA A 588  ? 0.3739 0.5906 0.3818 0.1140  -0.0324 -0.1881 586  ALA A CA  
4294  C C   . ALA A 588  ? 0.3716 0.5715 0.3851 0.1117  -0.0349 -0.1887 586  ALA A C   
4295  O O   . ALA A 588  ? 0.4325 0.6287 0.4447 0.1105  -0.0358 -0.1877 586  ALA A O   
4296  C CB  . ALA A 588  ? 0.3761 0.6028 0.3902 0.1175  -0.0361 -0.1974 586  ALA A CB  
4297  N N   . GLY A 589  ? 0.3897 0.5799 0.4099 0.1112  -0.0361 -0.1904 587  GLY A N   
4298  C CA  . GLY A 589  ? 0.3609 0.5356 0.3877 0.1091  -0.0388 -0.1910 587  GLY A CA  
4299  C C   . GLY A 589  ? 0.3900 0.5558 0.4238 0.1087  -0.0397 -0.1920 587  GLY A C   
4300  O O   . GLY A 589  ? 0.4249 0.5969 0.4590 0.1104  -0.0386 -0.1932 587  GLY A O   
4301  N N   . GLU A 590  ? 0.4146 0.5661 0.4544 0.1065  -0.0418 -0.1914 588  GLU A N   
4302  C CA  . GLU A 590  ? 0.3824 0.5241 0.4294 0.1057  -0.0428 -0.1916 588  GLU A CA  
4303  C C   . GLU A 590  ? 0.3382 0.4771 0.3788 0.1042  -0.0380 -0.1842 588  GLU A C   
4304  O O   . GLU A 590  ? 0.3692 0.5038 0.4035 0.1020  -0.0351 -0.1777 588  GLU A O   
4305  C CB  . GLU A 590  ? 0.4709 0.5982 0.5257 0.1034  -0.0462 -0.1918 588  GLU A CB  
4306  N N   . THR A 591  ? 0.3577 0.4993 0.4005 0.1055  -0.0372 -0.1853 589  THR A N   
4307  C CA  . THR A 591  ? 0.3426 0.4833 0.3800 0.1045  -0.0328 -0.1789 589  THR A CA  
4308  C C   . THR A 591  ? 0.3534 0.4816 0.3981 0.1031  -0.0338 -0.1780 589  THR A C   
4309  O O   . THR A 591  ? 0.4011 0.5271 0.4550 0.1043  -0.0375 -0.1836 589  THR A O   
4310  C CB  . THR A 591  ? 0.3930 0.5481 0.4262 0.1071  -0.0306 -0.1802 589  THR A CB  
4311  O OG1 . THR A 591  ? 0.3968 0.5638 0.4226 0.1081  -0.0293 -0.1797 589  THR A OG1 
4312  C CG2 . THR A 591  ? 0.3925 0.5466 0.4214 0.1062  -0.0263 -0.1739 589  THR A CG2 
4313  N N   . ARG A 592  ? 0.3177 0.4380 0.3588 0.1007  -0.0307 -0.1709 590  ARG A N   
4314  C CA  . ARG A 592  ? 0.3666 0.4756 0.4140 0.0993  -0.0312 -0.1690 590  ARG A CA  
4315  C C   . ARG A 592  ? 0.3234 0.4317 0.3639 0.0982  -0.0262 -0.1617 590  ARG A C   
4316  O O   . ARG A 592  ? 0.3364 0.4501 0.3678 0.0977  -0.0227 -0.1573 590  ARG A O   
4317  C CB  . ARG A 592  ? 0.3945 0.4898 0.4481 0.0968  -0.0343 -0.1683 590  ARG A CB  
4318  C CG  . ARG A 592  ? 0.4261 0.5165 0.4729 0.0944  -0.0319 -0.1622 590  ARG A CG  
4319  C CD  . ARG A 592  ? 0.4624 0.5384 0.5158 0.0916  -0.0344 -0.1602 590  ARG A CD  
4320  N NE  . ARG A 592  ? 0.4339 0.5058 0.4812 0.0894  -0.0325 -0.1552 590  ARG A NE  
4321  C CZ  . ARG A 592  ? 0.4391 0.5084 0.4801 0.0880  -0.0285 -0.1487 590  ARG A CZ  
4322  N NH1 . ARG A 592  ? 0.4324 0.5022 0.4724 0.0883  -0.0259 -0.1460 590  ARG A NH1 
4323  N NH2 . ARG A 592  ? 0.4624 0.5286 0.4983 0.0862  -0.0272 -0.1448 590  ARG A NH2 
4324  N N   . THR A 593  ? 0.3328 0.4344 0.3782 0.0977  -0.0261 -0.1603 591  THR A N   
4325  C CA  . THR A 593  ? 0.3285 0.4286 0.3686 0.0966  -0.0217 -0.1535 591  THR A CA  
4326  C C   . THR A 593  ? 0.3586 0.4480 0.3968 0.0936  -0.0207 -0.1477 591  THR A C   
4327  O O   . THR A 593  ? 0.3591 0.4394 0.4024 0.0921  -0.0238 -0.1487 591  THR A O   
4328  C CB  . THR A 593  ? 0.3632 0.4597 0.4096 0.0970  -0.0221 -0.1540 591  THR A CB  
4329  O OG1 . THR A 593  ? 0.3883 0.4730 0.4445 0.0958  -0.0263 -0.1561 591  THR A OG1 
4330  C CG2 . THR A 593  ? 0.3858 0.4938 0.4333 0.1000  -0.0226 -0.1593 591  THR A CG2 
4331  N N   . VAL A 594  ? 0.2746 0.3654 0.3056 0.0927  -0.0162 -0.1413 592  VAL A N   
4332  C CA  . VAL A 594  ? 0.3012 0.3826 0.3301 0.0901  -0.0147 -0.1353 592  VAL A CA  
4333  C C   . VAL A 594  ? 0.2994 0.3751 0.3314 0.0895  -0.0132 -0.1317 592  VAL A C   
4334  O O   . VAL A 594  ? 0.3095 0.3924 0.3380 0.0907  -0.0102 -0.1300 592  VAL A O   
4335  C CB  . VAL A 594  ? 0.3016 0.3895 0.3202 0.0895  -0.0108 -0.1303 592  VAL A CB  
4336  C CG1 . VAL A 594  ? 0.3050 0.3820 0.3216 0.0844  -0.0097 -0.1207 592  VAL A CG1 
4337  C CG2 . VAL A 594  ? 0.3177 0.4118 0.3335 0.0903  -0.0124 -0.1339 592  VAL A CG2 
4338  N N   . LEU A 595  ? 0.3008 0.3638 0.3392 0.0867  -0.0156 -0.1293 593  LEU A N   
4339  C CA  . LEU A 595  ? 0.3024 0.3589 0.3446 0.0851  -0.0150 -0.1251 593  LEU A CA  
4340  C C   . LEU A 595  ? 0.3005 0.3498 0.3381 0.0802  -0.0126 -0.1145 593  LEU A C   
4341  O O   . LEU A 595  ? 0.2997 0.3442 0.3352 0.0775  -0.0131 -0.1113 593  LEU A O   
4342  C CB  . LEU A 595  ? 0.3112 0.3589 0.3648 0.0855  -0.0196 -0.1296 593  LEU A CB  
4343  C CG  . LEU A 595  ? 0.3604 0.4133 0.4198 0.0885  -0.0230 -0.1383 593  LEU A CG  
4344  C CD1 . LEU A 595  ? 0.3804 0.4235 0.4513 0.0874  -0.0276 -0.1402 593  LEU A CD1 
4345  C CD2 . LEU A 595  ? 0.3477 0.4117 0.4045 0.0911  -0.0209 -0.1404 593  LEU A CD2 
4346  N N   . ASN A 596  ? 0.2804 0.3294 0.3168 0.0791  -0.0101 -0.1094 594  ASN A N   
4347  C CA  . ASN A 596  ? 0.2756 0.3176 0.3086 0.0747  -0.0080 -0.0999 594  ASN A CA  
4348  C C   . ASN A 596  ? 0.2605 0.2902 0.3000 0.0718  -0.0112 -0.0982 594  ASN A C   
4349  O O   . ASN A 596  ? 0.2631 0.2885 0.3107 0.0726  -0.0138 -0.1010 594  ASN A O   
4350  C CB  . ASN A 596  ? 0.2616 0.3059 0.2940 0.0748  -0.0055 -0.0965 594  ASN A CB  
4351  C CG  . ASN A 596  ? 0.2760 0.3150 0.3044 0.0706  -0.0030 -0.0869 594  ASN A CG  
4352  O OD1 . ASN A 596  ? 0.2635 0.2938 0.2924 0.0673  -0.0040 -0.0830 594  ASN A OD1 
4353  N ND2 . ASN A 596  ? 0.2854 0.3297 0.3097 0.0707  0.0003  -0.0832 594  ASN A ND2 
4354  N N   . PRO A 597  ? 0.2492 0.2735 0.2860 0.0685  -0.0112 -0.0936 595  PRO A N   
4355  C CA  . PRO A 597  ? 0.2587 0.2722 0.3019 0.0657  -0.0142 -0.0918 595  PRO A CA  
4356  C C   . PRO A 597  ? 0.2813 0.2885 0.3280 0.0636  -0.0140 -0.0867 595  PRO A C   
4357  O O   . PRO A 597  ? 0.2532 0.2526 0.3073 0.0621  -0.0170 -0.0864 595  PRO A O   
4358  C CB  . PRO A 597  ? 0.2585 0.2694 0.2964 0.0627  -0.0133 -0.0870 595  PRO A CB  
4359  C CG  . PRO A 597  ? 0.2626 0.2810 0.2913 0.0629  -0.0092 -0.0837 595  PRO A CG  
4360  C CD  . PRO A 597  ? 0.2365 0.2646 0.2647 0.0672  -0.0085 -0.0896 595  PRO A CD  
4361  N N   . GLY A 598  ? 0.2478 0.2584 0.2897 0.0632  -0.0106 -0.0826 596  GLY A N   
4362  C CA  . GLY A 598  ? 0.2384 0.2440 0.2832 0.0614  -0.0102 -0.0780 596  GLY A CA  
4363  C C   . GLY A 598  ? 0.2646 0.2719 0.3158 0.0643  -0.0116 -0.0825 596  GLY A C   
4364  O O   . GLY A 598  ? 0.2904 0.2929 0.3455 0.0628  -0.0120 -0.0793 596  GLY A O   
4365  N N   . ASP A 599  ? 0.2486 0.2629 0.3012 0.0683  -0.0124 -0.0902 597  ASP A N   
4366  C CA  . ASP A 599  ? 0.2537 0.2704 0.3129 0.0716  -0.0138 -0.0955 597  ASP A CA  
4367  C C   . ASP A 599  ? 0.2545 0.2787 0.3149 0.0759  -0.0153 -0.1047 597  ASP A C   
4368  O O   . ASP A 599  ? 0.2733 0.3075 0.3274 0.0781  -0.0126 -0.1066 597  ASP A O   
4369  C CB  . ASP A 599  ? 0.2624 0.2844 0.3178 0.0721  -0.0103 -0.0924 597  ASP A CB  
4370  C CG  . ASP A 599  ? 0.2799 0.3035 0.3425 0.0750  -0.0118 -0.0971 597  ASP A CG  
4371  O OD1 . ASP A 599  ? 0.3076 0.3310 0.3773 0.0777  -0.0152 -0.1044 597  ASP A OD1 
4372  O OD2 . ASP A 599  ? 0.3235 0.3486 0.3849 0.0747  -0.0096 -0.0935 597  ASP A OD2 
4373  N N   . HIS A 600  ? 0.2645 0.2844 0.3332 0.0770  -0.0196 -0.1103 598  HIS A N   
4374  C CA  . HIS A 600  ? 0.3056 0.3322 0.3760 0.0810  -0.0215 -0.1196 598  HIS A CA  
4375  C C   . HIS A 600  ? 0.3078 0.3442 0.3791 0.0856  -0.0206 -0.1259 598  HIS A C   
4376  O O   . HIS A 600  ? 0.3492 0.3938 0.4192 0.0885  -0.0212 -0.1324 598  HIS A O   
4377  C CB  . HIS A 600  ? 0.3237 0.3428 0.4040 0.0811  -0.0267 -0.1241 598  HIS A CB  
4378  C CG  . HIS A 600  ? 0.3437 0.3561 0.4222 0.0774  -0.0275 -0.1197 598  HIS A CG  
4379  N ND1 . HIS A 600  ? 0.4049 0.4099 0.4920 0.0765  -0.0320 -0.1221 598  HIS A ND1 
4380  C CD2 . HIS A 600  ? 0.3192 0.3315 0.3888 0.0744  -0.0245 -0.1131 598  HIS A CD2 
4381  C CE1 . HIS A 600  ? 0.3959 0.3968 0.4789 0.0731  -0.0315 -0.1170 598  HIS A CE1 
4382  N NE2 . HIS A 600  ? 0.3605 0.3657 0.4330 0.0718  -0.0270 -0.1117 598  HIS A NE2 
4383  N N   . ARG A 601  ? 0.3130 0.3489 0.3861 0.0855  -0.0193 -0.1232 599  ARG A N   
4384  C CA  . ARG A 601  ? 0.3186 0.3646 0.3918 0.0897  -0.0179 -0.1284 599  ARG A CA  
4385  C C   . ARG A 601  ? 0.3487 0.4059 0.4110 0.0905  -0.0133 -0.1263 599  ARG A C   
4386  O O   . ARG A 601  ? 0.3428 0.4105 0.4036 0.0934  -0.0123 -0.1306 599  ARG A O   
4387  C CB  . ARG A 601  ? 0.3055 0.3476 0.3834 0.0891  -0.0177 -0.1253 599  ARG A CB  
4388  C CG  . ARG A 601  ? 0.2908 0.3220 0.3799 0.0880  -0.0223 -0.1263 599  ARG A CG  
4389  C CD  . ARG A 601  ? 0.3499 0.3766 0.4423 0.0865  -0.0217 -0.1211 599  ARG A CD  
4390  N NE  . ARG A 601  ? 0.3317 0.3559 0.4161 0.0824  -0.0180 -0.1112 599  ARG A NE  
4391  C CZ  . ARG A 601  ? 0.3636 0.3843 0.4488 0.0804  -0.0168 -0.1053 599  ARG A CZ  
4392  N NH1 . ARG A 601  ? 0.3678 0.3866 0.4614 0.0820  -0.0189 -0.1077 599  ARG A NH1 
4393  N NH2 . ARG A 601  ? 0.3397 0.3587 0.4173 0.0768  -0.0136 -0.0969 599  ARG A NH2 
4394  N N   . ASP A 602  ? 0.2988 0.3539 0.3533 0.0868  -0.0107 -0.1185 600  ASP A N   
4395  C CA  . ASP A 602  ? 0.3466 0.4116 0.3912 0.0870  -0.0065 -0.1152 600  ASP A CA  
4396  C C   . ASP A 602  ? 0.3459 0.4168 0.3869 0.0886  -0.0071 -0.1198 600  ASP A C   
4397  O O   . ASP A 602  ? 0.3319 0.3973 0.3705 0.0859  -0.0078 -0.1168 600  ASP A O   
4398  C CB  . ASP A 602  ? 0.3196 0.3791 0.3585 0.0823  -0.0037 -0.1047 600  ASP A CB  
4399  C CG  . ASP A 602  ? 0.3364 0.4057 0.3660 0.0823  0.0005  -0.1007 600  ASP A CG  
4400  O OD1 . ASP A 602  ? 0.3404 0.4213 0.3682 0.0859  0.0018  -0.1052 600  ASP A OD1 
4401  O OD2 . ASP A 602  ? 0.3235 0.3892 0.3479 0.0787  0.0025  -0.0931 600  ASP A OD2 
4402  N N   . VAL A 603  ? 0.3195 0.4019 0.3601 0.0931  -0.0070 -0.1273 601  VAL A N   
4403  C CA  . VAL A 603  ? 0.3187 0.4078 0.3550 0.0938  -0.0077 -0.1305 601  VAL A CA  
4404  C C   . VAL A 603  ? 0.3253 0.4228 0.3514 0.0935  -0.0032 -0.1254 601  VAL A C   
4405  O O   . VAL A 603  ? 0.3597 0.4658 0.3821 0.0945  -0.0001 -0.1231 601  VAL A O   
4406  C CB  . VAL A 603  ? 0.3495 0.4471 0.3890 0.0964  -0.0100 -0.1376 601  VAL A CB  
4407  C CG1 . VAL A 603  ? 0.3443 0.4495 0.3793 0.0972  -0.0108 -0.1407 601  VAL A CG1 
4408  C CG2 . VAL A 603  ? 0.3648 0.4539 0.4150 0.0965  -0.0147 -0.1424 601  VAL A CG2 
4409  N N   . VAL A 604  ? 0.2758 0.3702 0.2975 0.0911  -0.0032 -0.1220 602  VAL A N   
4410  C CA  . VAL A 604  ? 0.2927 0.3928 0.3052 0.0893  0.0005  -0.1150 602  VAL A CA  
4411  C C   . VAL A 604  ? 0.2787 0.3928 0.2862 0.0927  0.0013  -0.1197 602  VAL A C   
4412  O O   . VAL A 604  ? 0.3209 0.4450 0.3218 0.0929  0.0047  -0.1158 602  VAL A O   
4413  C CB  . VAL A 604  ? 0.2688 0.3582 0.2794 0.0848  0.0002  -0.1083 602  VAL A CB  
4414  C CG1 . VAL A 604  ? 0.2623 0.3567 0.2643 0.0828  0.0038  -0.1006 602  VAL A CG1 
4415  C CG2 . VAL A 604  ? 0.2773 0.3537 0.2932 0.0817  -0.0008 -0.1041 602  VAL A CG2 
4416  N N   . GLY A 605  ? 0.2758 0.3901 0.2867 0.0938  -0.0023 -0.1263 603  GLY A N   
4417  C CA  . GLY A 605  ? 0.2794 0.4058 0.2859 0.0953  -0.0024 -0.1289 603  GLY A CA  
4418  C C   . GLY A 605  ? 0.2591 0.3837 0.2709 0.0963  -0.0071 -0.1363 603  GLY A C   
4419  O O   . GLY A 605  ? 0.3248 0.4404 0.3447 0.0962  -0.0103 -0.1400 603  GLY A O   
4420  N N   . SER A 606  ? 0.2671 0.4007 0.2747 0.0972  -0.0075 -0.1382 604  SER A N   
4421  C CA  A SER A 606  ? 0.2820 0.4160 0.2943 0.0984  -0.0119 -0.1455 604  SER A CA  
4422  C CA  B SER A 606  ? 0.2823 0.4166 0.2945 0.0984  -0.0119 -0.1455 604  SER A CA  
4423  C C   . SER A 606  ? 0.3110 0.4473 0.3181 0.0976  -0.0119 -0.1442 604  SER A C   
4424  O O   . SER A 606  ? 0.3137 0.4580 0.3128 0.0973  -0.0087 -0.1395 604  SER A O   
4425  C CB  A SER A 606  ? 0.2961 0.4421 0.3102 0.1014  -0.0131 -0.1512 604  SER A CB  
4426  C CB  B SER A 606  ? 0.2958 0.4428 0.3091 0.1014  -0.0128 -0.1509 604  SER A CB  
4427  O OG  A SER A 606  ? 0.3242 0.4671 0.3444 0.1022  -0.0138 -0.1533 604  SER A OG  
4428  O OG  B SER A 606  ? 0.2988 0.4483 0.3157 0.1027  -0.0167 -0.1577 604  SER A OG  
4429  N N   . VAL A 607  ? 0.2801 0.4091 0.2920 0.0971  -0.0157 -0.1481 605  VAL A N   
4430  C CA  . VAL A 607  ? 0.2654 0.3958 0.2734 0.0964  -0.0163 -0.1477 605  VAL A CA  
4431  C C   . VAL A 607  ? 0.2744 0.4100 0.2869 0.0984  -0.0204 -0.1556 605  VAL A C   
4432  O O   . VAL A 607  ? 0.3020 0.4323 0.3232 0.0990  -0.0241 -0.1610 605  VAL A O   
4433  C CB  . VAL A 607  ? 0.2765 0.3934 0.2856 0.0936  -0.0168 -0.1444 605  VAL A CB  
4434  C CG1 . VAL A 607  ? 0.3073 0.4123 0.3266 0.0930  -0.0206 -0.1482 605  VAL A CG1 
4435  C CG2 . VAL A 607  ? 0.2876 0.4064 0.2928 0.0930  -0.0176 -0.1444 605  VAL A CG2 
4436  N N   . THR A 608  ? 0.2852 0.4316 0.2921 0.0994  -0.0199 -0.1560 606  THR A N   
4437  C CA  . THR A 608  ? 0.3050 0.4563 0.3155 0.1011  -0.0238 -0.1630 606  THR A CA  
4438  C C   . THR A 608  ? 0.2990 0.4442 0.3079 0.0993  -0.0248 -0.1614 606  THR A C   
4439  O O   . THR A 608  ? 0.3157 0.4639 0.3167 0.0982  -0.0219 -0.1559 606  THR A O   
4440  C CB  . THR A 608  ? 0.3249 0.4930 0.3304 0.1036  -0.0226 -0.1644 606  THR A CB  
4441  O OG1 . THR A 608  ? 0.3399 0.5135 0.3467 0.1052  -0.0214 -0.1654 606  THR A OG1 
4442  C CG2 . THR A 608  ? 0.3438 0.5177 0.3533 0.1056  -0.0267 -0.1720 606  THR A CG2 
4443  N N   . GLU A 609  ? 0.3235 0.4601 0.3402 0.0989  -0.0289 -0.1659 607  GLU A N   
4444  C CA  . GLU A 609  ? 0.3405 0.4700 0.3566 0.0969  -0.0301 -0.1644 607  GLU A CA  
4445  C C   . GLU A 609  ? 0.3278 0.4664 0.3427 0.0984  -0.0322 -0.1686 607  GLU A C   
4446  O O   . GLU A 609  ? 0.3084 0.4569 0.3256 0.1011  -0.0340 -0.1743 607  GLU A O   
4447  C CB  . GLU A 609  ? 0.3910 0.5057 0.4161 0.0951  -0.0332 -0.1656 607  GLU A CB  
4448  C CG  . GLU A 609  ? 0.4333 0.5392 0.4581 0.0932  -0.0306 -0.1601 607  GLU A CG  
4449  C CD  . GLU A 609  ? 0.4736 0.5648 0.5069 0.0911  -0.0334 -0.1600 607  GLU A CD  
4450  O OE1 . GLU A 609  ? 0.5437 0.6323 0.5860 0.0917  -0.0378 -0.1656 607  GLU A OE1 
4451  O OE2 . GLU A 609  ? 0.4644 0.5471 0.4957 0.0887  -0.0313 -0.1542 607  GLU A OE2 
4452  N N   . THR A 610  ? 0.3355 0.4709 0.3466 0.0967  -0.0319 -0.1656 608  THR A N   
4453  C CA  . THR A 610  ? 0.3167 0.4610 0.3249 0.0979  -0.0331 -0.1680 608  THR A CA  
4454  C C   . THR A 610  ? 0.3593 0.4987 0.3763 0.0982  -0.0382 -0.1746 608  THR A C   
4455  O O   . THR A 610  ? 0.3906 0.5172 0.4129 0.0961  -0.0400 -0.1741 608  THR A O   
4456  C CB  . THR A 610  ? 0.3191 0.4616 0.3192 0.0957  -0.0304 -0.1614 608  THR A CB  
4457  O OG1 . THR A 610  ? 0.3063 0.4516 0.2993 0.0950  -0.0258 -0.1546 608  THR A OG1 
4458  C CG2 . THR A 610  ? 0.3094 0.4626 0.3056 0.0969  -0.0312 -0.1630 608  THR A CG2 
4459  N N   . SER A 611  ? 0.3352 0.4850 0.3541 0.1009  -0.0406 -0.1807 609  SER A N   
4460  C CA  . SER A 611  ? 0.3535 0.5000 0.3803 0.1013  -0.0453 -0.1867 609  SER A CA  
4461  C C   . SER A 611  ? 0.3831 0.5263 0.4060 0.0994  -0.0452 -0.1837 609  SER A C   
4462  O O   . SER A 611  ? 0.3568 0.5049 0.3704 0.0988  -0.0418 -0.1784 609  SER A O   
4463  C CB  . SER A 611  ? 0.3627 0.5225 0.3922 0.1049  -0.0477 -0.1941 609  SER A CB  
4464  O OG  . SER A 611  ? 0.3935 0.5649 0.4149 0.1059  -0.0460 -0.1927 609  SER A OG  
4465  N N   . GLU A 612  ? 0.3892 0.5238 0.4196 0.0984  -0.0491 -0.1867 610  GLU A N   
4466  C CA  . GLU A 612  ? 0.4101 0.5417 0.4373 0.0967  -0.0494 -0.1844 610  GLU A CA  
4467  C C   . GLU A 612  ? 0.4102 0.5556 0.4324 0.0989  -0.0493 -0.1866 610  GLU A C   
4468  O O   . GLU A 612  ? 0.4058 0.5525 0.4213 0.0977  -0.0477 -0.1827 610  GLU A O   
4469  C CB  . GLU A 612  ? 0.5271 0.6472 0.5642 0.0952  -0.0537 -0.1871 610  GLU A CB  
4470  C CG  . GLU A 612  ? 0.5446 0.6506 0.5856 0.0924  -0.0533 -0.1831 610  GLU A CG  
4471  C CD  . GLU A 612  ? 0.6400 0.7352 0.6920 0.0908  -0.0579 -0.1857 610  GLU A CD  
4472  O OE1 . GLU A 612  ? 0.7448 0.8403 0.7988 0.0906  -0.0604 -0.1878 610  GLU A OE1 
4473  O OE2 . GLU A 612  ? 0.5932 0.6802 0.6524 0.0898  -0.0591 -0.1854 610  GLU A OE2 
4474  N N   . GLU A 613  ? 0.3884 0.5445 0.4136 0.1021  -0.0511 -0.1928 611  GLU A N   
4475  C CA  . GLU A 613  ? 0.4236 0.5941 0.4437 0.1044  -0.0507 -0.1947 611  GLU A CA  
4476  C C   . GLU A 613  ? 0.3539 0.5324 0.3627 0.1041  -0.0457 -0.1879 611  GLU A C   
4477  O O   . GLU A 613  ? 0.3366 0.5211 0.3390 0.1039  -0.0444 -0.1850 611  GLU A O   
4478  C CB  . GLU A 613  ? 0.4265 0.6071 0.4528 0.1081  -0.0536 -0.2030 611  GLU A CB  
4479  N N   . ASP A 614  ? 0.3775 0.5563 0.3843 0.1041  -0.0429 -0.1850 612  ASP A N   
4480  C CA  . ASP A 614  ? 0.3137 0.5003 0.3105 0.1038  -0.0382 -0.1781 612  ASP A CA  
4481  C C   . ASP A 614  ? 0.3362 0.5142 0.3271 0.1005  -0.0356 -0.1703 612  ASP A C   
4482  O O   . ASP A 614  ? 0.3169 0.5021 0.2996 0.1000  -0.0325 -0.1647 612  ASP A O   
4483  C CB  . ASP A 614  ? 0.3503 0.5394 0.3470 0.1046  -0.0361 -0.1772 612  ASP A CB  
4484  C CG  . ASP A 614  ? 0.3512 0.5525 0.3516 0.1081  -0.0379 -0.1841 612  ASP A CG  
4485  O OD1 . ASP A 614  ? 0.4037 0.6160 0.4030 0.1101  -0.0393 -0.1874 612  ASP A OD1 
4486  O OD2 . ASP A 614  ? 0.3818 0.5820 0.3862 0.1090  -0.0381 -0.1863 612  ASP A OD2 
4487  N N   . ALA A 615  ? 0.3100 0.4732 0.3053 0.0982  -0.0369 -0.1697 613  ALA A N   
4488  C CA  . ALA A 615  ? 0.3208 0.4759 0.3111 0.0952  -0.0348 -0.1630 613  ALA A CA  
4489  C C   . ALA A 615  ? 0.2978 0.4575 0.2847 0.0951  -0.0358 -0.1628 613  ALA A C   
4490  O O   . ALA A 615  ? 0.3040 0.4665 0.2829 0.0939  -0.0329 -0.1566 613  ALA A O   
4491  C CB  . ALA A 615  ? 0.3040 0.4430 0.3007 0.0929  -0.0365 -0.1630 613  ALA A CB  
4492  N N   . ARG A 616  ? 0.3519 0.5126 0.3449 0.0964  -0.0398 -0.1696 614  ARG A N   
4493  C CA  . ARG A 616  ? 0.3817 0.5477 0.3718 0.0966  -0.0409 -0.1700 614  ARG A CA  
4494  C C   . ARG A 616  ? 0.2806 0.4626 0.2634 0.0985  -0.0386 -0.1682 614  ARG A C   
4495  O O   . ARG A 616  ? 0.3466 0.5328 0.3229 0.0977  -0.0372 -0.1638 614  ARG A O   
4496  C CB  . ARG A 616  ? 0.4063 0.5705 0.4053 0.0978  -0.0459 -0.1779 614  ARG A CB  
4497  C CG  . ARG A 616  ? 0.4709 0.6199 0.4755 0.0951  -0.0482 -0.1778 614  ARG A CG  
4498  C CD  . ARG A 616  ? 0.5509 0.6979 0.5657 0.0963  -0.0533 -0.1855 614  ARG A CD  
4499  N NE  . ARG A 616  ? 0.6225 0.7634 0.6462 0.0967  -0.0554 -0.1892 614  ARG A NE  
4500  C CZ  . ARG A 616  ? 0.5554 0.7035 0.5846 0.0996  -0.0575 -0.1956 614  ARG A CZ  
4501  N NH1 . ARG A 616  ? 0.6125 0.7743 0.6394 0.1025  -0.0580 -0.1995 614  ARG A NH1 
4502  N NH2 . ARG A 616  ? 0.5749 0.7163 0.6122 0.0997  -0.0593 -0.1983 614  ARG A NH2 
4503  N N   . ARG A 617  ? 0.2835 0.4750 0.2674 0.1010  -0.0383 -0.1712 615  ARG A N   
4504  C CA  . ARG A 617  ? 0.3292 0.5366 0.3065 0.1028  -0.0360 -0.1690 615  ARG A CA  
4505  C C   . ARG A 617  ? 0.3387 0.5464 0.3073 0.1007  -0.0314 -0.1593 615  ARG A C   
4506  O O   . ARG A 617  ? 0.3198 0.5370 0.2820 0.1007  -0.0296 -0.1551 615  ARG A O   
4507  C CB  . ARG A 617  ? 0.3698 0.5866 0.3503 0.1057  -0.0365 -0.1740 615  ARG A CB  
4508  C CG  . ARG A 617  ? 0.4287 0.6631 0.4035 0.1078  -0.0345 -0.1724 615  ARG A CG  
4509  C CD  . ARG A 617  ? 0.4817 0.7264 0.4615 0.1113  -0.0367 -0.1802 615  ARG A CD  
4510  N NE  . ARG A 617  ? 0.5044 0.7459 0.4875 0.1117  -0.0361 -0.1813 615  ARG A NE  
4511  C CZ  . ARG A 617  ? 0.5653 0.8147 0.5441 0.1122  -0.0328 -0.1774 615  ARG A CZ  
4512  N NH1 . ARG A 617  ? 0.5165 0.7772 0.4877 0.1121  -0.0299 -0.1716 615  ARG A NH1 
4513  N NH2 . ARG A 617  ? 0.4901 0.7359 0.4726 0.1126  -0.0327 -0.1792 615  ARG A NH2 
4514  N N   . ALA A 618  ? 0.3255 0.5233 0.2942 0.0988  -0.0295 -0.1557 616  ALA A N   
4515  C CA  . ALA A 618  ? 0.2937 0.4914 0.2549 0.0968  -0.0252 -0.1465 616  ALA A CA  
4516  C C   . ALA A 618  ? 0.2626 0.4569 0.2192 0.0947  -0.0247 -0.1417 616  ALA A C   
4517  O O   . ALA A 618  ? 0.2930 0.4943 0.2426 0.0940  -0.0219 -0.1350 616  ALA A O   
4518  C CB  . ALA A 618  ? 0.2946 0.4812 0.2575 0.0953  -0.0235 -0.1442 616  ALA A CB  
4519  N N   . VAL A 619  ? 0.2738 0.4576 0.2345 0.0936  -0.0275 -0.1449 617  VAL A N   
4520  C CA  . VAL A 619  ? 0.2887 0.4693 0.2454 0.0916  -0.0274 -0.1408 617  VAL A CA  
4521  C C   . VAL A 619  ? 0.3114 0.5055 0.2642 0.0931  -0.0277 -0.1407 617  VAL A C   
4522  O O   . VAL A 619  ? 0.3091 0.5068 0.2556 0.0919  -0.0257 -0.1342 617  VAL A O   
4523  C CB  . VAL A 619  ? 0.2795 0.4467 0.2421 0.0902  -0.0306 -0.1446 617  VAL A CB  
4524  C CG1 . VAL A 619  ? 0.3097 0.4741 0.2681 0.0882  -0.0305 -0.1405 617  VAL A CG1 
4525  C CG2 . VAL A 619  ? 0.3068 0.4610 0.2731 0.0886  -0.0300 -0.1437 617  VAL A CG2 
4526  N N   . ARG A 620  ? 0.2954 0.4975 0.2524 0.0958  -0.0303 -0.1479 618  ARG A N   
4527  C CA  . ARG A 620  ? 0.3238 0.5395 0.2775 0.0974  -0.0307 -0.1481 618  ARG A CA  
4528  C C   . ARG A 620  ? 0.3051 0.5329 0.2519 0.0978  -0.0270 -0.1414 618  ARG A C   
4529  O O   . ARG A 620  ? 0.3643 0.5994 0.3058 0.0973  -0.0258 -0.1365 618  ARG A O   
4530  C CB  . ARG A 620  ? 0.3560 0.5782 0.3159 0.1005  -0.0342 -0.1575 618  ARG A CB  
4531  C CG  . ARG A 620  ? 0.3940 0.6067 0.3604 0.1001  -0.0383 -0.1633 618  ARG A CG  
4532  C CD  . ARG A 620  ? 0.5138 0.7338 0.4865 0.1032  -0.0419 -0.1724 618  ARG A CD  
4533  N NE  . ARG A 620  ? 0.5569 0.7681 0.5384 0.1037  -0.0445 -0.1784 618  ARG A NE  
4534  C CZ  . ARG A 620  ? 0.4652 0.6813 0.4503 0.1059  -0.0448 -0.1825 618  ARG A CZ  
4535  N NH1 . ARG A 620  ? 0.5577 0.7881 0.5386 0.1080  -0.0428 -0.1818 618  ARG A NH1 
4536  N NH2 . ARG A 620  ? 0.4932 0.6997 0.4865 0.1059  -0.0473 -0.1872 618  ARG A NH2 
4537  N N   . LEU A 621  ? 0.2830 0.5127 0.2302 0.0984  -0.0251 -0.1407 619  LEU A N   
4538  C CA  . LEU A 621  ? 0.3136 0.5545 0.2550 0.0985  -0.0215 -0.1338 619  LEU A CA  
4539  C C   . LEU A 621  ? 0.2881 0.5236 0.2237 0.0954  -0.0186 -0.1241 619  LEU A C   
4540  O O   . LEU A 621  ? 0.3129 0.5581 0.2432 0.0950  -0.0164 -0.1175 619  LEU A O   
4541  C CB  . LEU A 621  ? 0.3067 0.5496 0.2502 0.0997  -0.0203 -0.1353 619  LEU A CB  
4542  C CG  . LEU A 621  ? 0.3300 0.5801 0.2792 0.1029  -0.0229 -0.1444 619  LEU A CG  
4543  C CD1 . LEU A 621  ? 0.3189 0.5667 0.2708 0.1035  -0.0219 -0.1456 619  LEU A CD1 
4544  C CD2 . LEU A 621  ? 0.3466 0.6146 0.2931 0.1052  -0.0228 -0.1447 619  LEU A CD2 
4545  N N   . ALA A 622  ? 0.3042 0.5248 0.2411 0.0932  -0.0185 -0.1231 620  ALA A N   
4546  C CA  . ALA A 622  ? 0.3156 0.5305 0.2475 0.0904  -0.0161 -0.1145 620  ALA A CA  
4547  C C   . ALA A 622  ? 0.2779 0.4958 0.2067 0.0897  -0.0171 -0.1123 620  ALA A C   
4548  O O   . ALA A 622  ? 0.3066 0.5289 0.2301 0.0883  -0.0149 -0.1042 620  ALA A O   
4549  C CB  . ALA A 622  ? 0.2941 0.4924 0.2287 0.0885  -0.0162 -0.1150 620  ALA A CB  
4550  N N   . ALA A 623  ? 0.3019 0.5173 0.2344 0.0905  -0.0206 -0.1191 621  ALA A N   
4551  C CA  . ALA A 623  ? 0.3158 0.5345 0.2458 0.0901  -0.0218 -0.1177 621  ALA A CA  
4552  C C   . ALA A 623  ? 0.2941 0.5294 0.2200 0.0914  -0.0206 -0.1143 621  ALA A C   
4553  O O   . ALA A 623  ? 0.3360 0.5751 0.2574 0.0901  -0.0196 -0.1078 621  ALA A O   
4554  C CB  . ALA A 623  ? 0.3541 0.5683 0.2897 0.0910  -0.0260 -0.1263 621  ALA A CB  
4555  N N   . ASP A 624  ? 0.2926 0.5382 0.2205 0.0941  -0.0208 -0.1186 622  ASP A N   
4556  C CA  . ASP A 624  ? 0.3640 0.6262 0.2885 0.0954  -0.0196 -0.1155 622  ASP A CA  
4557  C C   . ASP A 624  ? 0.3617 0.6279 0.2812 0.0937  -0.0158 -0.1051 622  ASP A C   
4558  O O   . ASP A 624  ? 0.4199 0.6962 0.3357 0.0934  -0.0147 -0.0992 622  ASP A O   
4559  C CB  . ASP A 624  ? 0.4264 0.6989 0.3545 0.0987  -0.0207 -0.1226 622  ASP A CB  
4560  C CG  . ASP A 624  ? 0.4967 0.7675 0.4304 0.1007  -0.0248 -0.1328 622  ASP A CG  
4561  O OD1 . ASP A 624  ? 0.5683 0.8352 0.5019 0.0999  -0.0266 -0.1337 622  ASP A OD1 
4562  O OD2 . ASP A 624  ? 0.5615 0.8350 0.4999 0.1030  -0.0262 -0.1399 622  ASP A OD2 
4563  N N   . ALA A 625  ? 0.3760 0.6342 0.2958 0.0925  -0.0139 -0.1026 623  ALA A N   
4564  C CA  . ALA A 625  ? 0.4121 0.6728 0.3281 0.0907  -0.0103 -0.0929 623  ALA A CA  
4565  C C   . ALA A 625  ? 0.4064 0.6587 0.3191 0.0877  -0.0092 -0.0852 623  ALA A C   
4566  O O   . ALA A 625  ? 0.4153 0.6702 0.3250 0.0860  -0.0064 -0.0762 623  ALA A O   
4567  C CB  . ALA A 625  ? 0.4277 0.6826 0.3457 0.0907  -0.0088 -0.0938 623  ALA A CB  
4568  N N   . ALA A 626  ? 0.3377 0.5801 0.2513 0.0868  -0.0114 -0.0883 624  ALA A N   
4569  C CA  . ALA A 626  ? 0.3228 0.5561 0.2337 0.0840  -0.0105 -0.0816 624  ALA A CA  
4570  C C   . ALA A 626  ? 0.3741 0.6163 0.2808 0.0828  -0.0091 -0.0722 624  ALA A C   
4571  O O   . ALA A 626  ? 0.3832 0.6218 0.2876 0.0806  -0.0068 -0.0639 624  ALA A O   
4572  C CB  . ALA A 626  ? 0.3509 0.5730 0.2640 0.0835  -0.0135 -0.0872 624  ALA A CB  
4573  N N   . PRO A 627  ? 0.3510 0.6048 0.2568 0.0840  -0.0102 -0.0727 625  PRO A N   
4574  C CA  . PRO A 627  ? 0.3473 0.6089 0.2497 0.0826  -0.0089 -0.0630 625  PRO A CA  
4575  C C   . PRO A 627  ? 0.3410 0.6095 0.2422 0.0819  -0.0057 -0.0550 625  PRO A C   
4576  O O   . PRO A 627  ? 0.3740 0.6417 0.2733 0.0796  -0.0041 -0.0454 625  PRO A O   
4577  C CB  . PRO A 627  ? 0.3526 0.6262 0.2550 0.0846  -0.0108 -0.0667 625  PRO A CB  
4578  C CG  . PRO A 627  ? 0.3734 0.6411 0.2791 0.0863  -0.0138 -0.0779 625  PRO A CG  
4579  C CD  . PRO A 627  ? 0.3612 0.6213 0.2694 0.0867  -0.0129 -0.0816 625  PRO A CD  
4580  N N   . ASP A 628  ? 0.3500 0.6253 0.2527 0.0838  -0.0049 -0.0586 626  ASP A N   
4581  C CA  . ASP A 628  ? 0.3485 0.6313 0.2505 0.0832  -0.0020 -0.0512 626  ASP A CA  
4582  C C   . ASP A 628  ? 0.3606 0.6320 0.2624 0.0807  0.0001  -0.0454 626  ASP A C   
4583  O O   . ASP A 628  ? 0.4074 0.6820 0.3081 0.0789  0.0022  -0.0359 626  ASP A O   
4584  C CB  . ASP A 628  ? 0.3245 0.6160 0.2285 0.0859  -0.0018 -0.0572 626  ASP A CB  
4585  C CG  . ASP A 628  ? 0.4161 0.7213 0.3204 0.0884  -0.0035 -0.0619 626  ASP A CG  
4586  O OD1 . ASP A 628  ? 0.4774 0.7857 0.3802 0.0880  -0.0047 -0.0599 626  ASP A OD1 
4587  O OD2 . ASP A 628  ? 0.5347 0.8477 0.4409 0.0909  -0.0039 -0.0677 626  ASP A OD2 
4588  N N   . TRP A 629  ? 0.3271 0.5851 0.2301 0.0806  -0.0007 -0.0510 627  TRP A N   
4589  C CA  . TRP A 629  ? 0.3321 0.5794 0.2349 0.0784  0.0013  -0.0461 627  TRP A CA  
4590  C C   . TRP A 629  ? 0.3311 0.5716 0.2320 0.0759  0.0012  -0.0392 627  TRP A C   
4591  O O   . TRP A 629  ? 0.3244 0.5623 0.2245 0.0738  0.0033  -0.0306 627  TRP A O   
4592  C CB  . TRP A 629  ? 0.3199 0.5557 0.2252 0.0792  0.0006  -0.0543 627  TRP A CB  
4593  C CG  . TRP A 629  ? 0.2855 0.5105 0.1907 0.0772  0.0027  -0.0497 627  TRP A CG  
4594  C CD1 . TRP A 629  ? 0.2596 0.4679 0.1689 0.0748  0.0016  -0.0503 627  TRP A CD1 
4595  C CD2 . TRP A 629  ? 0.2563 0.4837 0.1611 0.0760  0.0057  -0.0422 627  TRP A CD2 
4596  N NE1 . TRP A 629  ? 0.2592 0.4591 0.1708 0.0723  0.0037  -0.0439 627  TRP A NE1 
4597  C CE2 . TRP A 629  ? 0.2542 0.4652 0.1633 0.0729  0.0062  -0.0390 627  TRP A CE2 
4598  C CE3 . TRP A 629  ? 0.2900 0.5292 0.1946 0.0763  0.0075  -0.0371 627  TRP A CE3 
4599  C CZ2 . TRP A 629  ? 0.2763 0.4847 0.1867 0.0711  0.0087  -0.0318 627  TRP A CZ2 
4600  C CZ3 . TRP A 629  ? 0.2902 0.5277 0.1951 0.0747  0.0102  -0.0300 627  TRP A CZ3 
4601  C CH2 . TRP A 629  ? 0.2862 0.5086 0.1938 0.0722  0.0108  -0.0276 627  TRP A CH2 
4602  N N   . ALA A 630  ? 0.2934 0.5309 0.1937 0.0760  -0.0013 -0.0428 628  ALA A N   
4603  C CA  . ALA A 630  ? 0.3465 0.5777 0.2465 0.0734  -0.0018 -0.0362 628  ALA A CA  
4604  C C   . ALA A 630  ? 0.3620 0.6039 0.2594 0.0725  -0.0004 -0.0259 628  ALA A C   
4605  O O   . ALA A 630  ? 0.3277 0.5628 0.2271 0.0695  0.0001  -0.0176 628  ALA A O   
4606  C CB  . ALA A 630  ? 0.3629 0.5910 0.2633 0.0740  -0.0049 -0.0421 628  ALA A CB  
4607  N N   . ALA A 631  ? 0.3247 0.5804 0.2223 0.0739  0.0000  -0.0257 629  ALA A N   
4608  C CA  . ALA A 631  ? 0.3303 0.5964 0.2275 0.0727  0.0011  -0.0158 629  ALA A CA  
4609  C C   . ALA A 631  ? 0.3372 0.6040 0.2355 0.0712  0.0039  -0.0078 629  ALA A C   
4610  O O   . ALA A 631  ? 0.3477 0.6207 0.2467 0.0696  0.0048  0.0017  629  ALA A O   
4611  C CB  . ALA A 631  ? 0.3328 0.6142 0.2300 0.0749  0.0004  -0.0186 629  ALA A CB  
4612  N N   . VAL A 632  ? 0.3403 0.6008 0.2394 0.0715  0.0052  -0.0111 630  VAL A N   
4613  C CA  . VAL A 632  ? 0.3167 0.5759 0.2170 0.0698  0.0078  -0.0033 630  VAL A CA  
4614  C C   . VAL A 632  ? 0.3022 0.5507 0.2026 0.0670  0.0078  0.0036  630  VAL A C   
4615  O O   . VAL A 632  ? 0.3311 0.5653 0.2340 0.0661  0.0065  -0.0009 630  VAL A O   
4616  C CB  . VAL A 632  ? 0.3219 0.5767 0.2232 0.0709  0.0091  -0.0091 630  VAL A CB  
4617  C CG1 . VAL A 632  ? 0.3244 0.5773 0.2271 0.0690  0.0117  -0.0009 630  VAL A CG1 
4618  C CG2 . VAL A 632  ? 0.3025 0.5685 0.2042 0.0738  0.0086  -0.0162 630  VAL A CG2 
4619  N N   . PRO A 633  ? 0.2793 0.5309 0.1811 0.0648  0.0087  0.0144  631  PRO A N   
4620  C CA  . PRO A 633  ? 0.2904 0.5294 0.1961 0.0616  0.0081  0.0207  631  PRO A CA  
4621  C C   . PRO A 633  ? 0.2820 0.5044 0.1920 0.0599  0.0088  0.0186  631  PRO A C   
4622  O O   . PRO A 633  ? 0.2796 0.5022 0.1898 0.0606  0.0105  0.0167  631  PRO A O   
4623  C CB  . PRO A 633  ? 0.3188 0.5665 0.2254 0.0600  0.0093  0.0326  631  PRO A CB  
4624  C CG  . PRO A 633  ? 0.3447 0.6085 0.2501 0.0618  0.0095  0.0317  631  PRO A CG  
4625  C CD  . PRO A 633  ? 0.2993 0.5642 0.2028 0.0645  0.0099  0.0211  631  PRO A CD  
4626  N N   . PRO A 634  ? 0.2550 0.4632 0.1686 0.0578  0.0075  0.0187  632  PRO A N   
4627  C CA  . PRO A 634  ? 0.2653 0.4581 0.1829 0.0562  0.0081  0.0168  632  PRO A CA  
4628  C C   . PRO A 634  ? 0.2695 0.4618 0.1895 0.0548  0.0103  0.0231  632  PRO A C   
4629  O O   . PRO A 634  ? 0.2513 0.4372 0.1725 0.0548  0.0114  0.0195  632  PRO A O   
4630  C CB  . PRO A 634  ? 0.2552 0.4362 0.1763 0.0538  0.0065  0.0188  632  PRO A CB  
4631  C CG  . PRO A 634  ? 0.2911 0.4796 0.2094 0.0550  0.0046  0.0176  632  PRO A CG  
4632  C CD  . PRO A 634  ? 0.2738 0.4800 0.1878 0.0570  0.0053  0.0201  632  PRO A CD  
4633  N N   . SER A 635  ? 0.2670 0.4660 0.1880 0.0535  0.0109  0.0327  633  SER A N   
4634  C CA  . SER A 635  ? 0.3027 0.5014 0.2266 0.0520  0.0129  0.0392  633  SER A CA  
4635  C C   . SER A 635  ? 0.2958 0.5036 0.2167 0.0542  0.0148  0.0359  633  SER A C   
4636  O O   . SER A 635  ? 0.2820 0.4849 0.2052 0.0534  0.0163  0.0365  633  SER A O   
4637  C CB  . SER A 635  ? 0.4170 0.6232 0.3427 0.0504  0.0129  0.0501  633  SER A CB  
4638  O OG  . SER A 635  ? 0.4775 0.7007 0.3986 0.0525  0.0130  0.0514  633  SER A OG  
4639  N N   . GLU A 636  ? 0.2734 0.4949 0.1892 0.0570  0.0146  0.0322  634  GLU A N   
4640  C CA  . GLU A 636  ? 0.2840 0.5152 0.1970 0.0594  0.0163  0.0282  634  GLU A CA  
4641  C C   . GLU A 636  ? 0.2653 0.4873 0.1785 0.0608  0.0160  0.0178  634  GLU A C   
4642  O O   . GLU A 636  ? 0.2707 0.4929 0.1843 0.0615  0.0176  0.0158  634  GLU A O   
4643  C CB  . GLU A 636  ? 0.2875 0.5368 0.1958 0.0619  0.0161  0.0274  634  GLU A CB  
4644  C CG  . GLU A 636  ? 0.3895 0.6471 0.2980 0.0641  0.0173  0.0223  634  GLU A CG  
4645  C CD  . GLU A 636  ? 0.4971 0.7545 0.4084 0.0627  0.0196  0.0282  634  GLU A CD  
4646  O OE1 . GLU A 636  ? 0.4661 0.7253 0.3801 0.0603  0.0202  0.0383  634  GLU A OE1 
4647  O OE2 . GLU A 636  ? 0.4232 0.6784 0.3344 0.0640  0.0207  0.0226  634  GLU A OE2 
4648  N N   . ARG A 637  ? 0.2698 0.4835 0.1829 0.0611  0.0139  0.0113  635  ARG A N   
4649  C CA  . ARG A 637  ? 0.2483 0.4514 0.1629 0.0618  0.0134  0.0024  635  ARG A CA  
4650  C C   . ARG A 637  ? 0.2482 0.4383 0.1673 0.0593  0.0145  0.0057  635  ARG A C   
4651  O O   . ARG A 637  ? 0.2474 0.4344 0.1674 0.0600  0.0155  0.0017  635  ARG A O   
4652  C CB  . ARG A 637  ? 0.2386 0.4342 0.1533 0.0620  0.0108  -0.0038 635  ARG A CB  
4653  C CG  . ARG A 637  ? 0.2569 0.4656 0.1673 0.0646  0.0094  -0.0073 635  ARG A CG  
4654  C CD  . ARG A 637  ? 0.2854 0.4876 0.1960 0.0654  0.0068  -0.0154 635  ARG A CD  
4655  N NE  . ARG A 637  ? 0.2772 0.4667 0.1909 0.0625  0.0057  -0.0122 635  ARG A NE  
4656  C CZ  . ARG A 637  ? 0.3017 0.4929 0.2146 0.0620  0.0041  -0.0101 635  ARG A CZ  
4657  N NH1 . ARG A 637  ? 0.3029 0.5080 0.2118 0.0639  0.0034  -0.0102 635  ARG A NH1 
4658  N NH2 . ARG A 637  ? 0.2842 0.4630 0.2005 0.0595  0.0031  -0.0081 635  ARG A NH2 
4659  N N   . ALA A 638  ? 0.2647 0.4474 0.1868 0.0563  0.0144  0.0130  636  ALA A N   
4660  C CA  . ALA A 638  ? 0.2432 0.4141 0.1697 0.0538  0.0154  0.0163  636  ALA A CA  
4661  C C   . ALA A 638  ? 0.2565 0.4339 0.1833 0.0540  0.0177  0.0203  636  ALA A C   
4662  O O   . ALA A 638  ? 0.2275 0.3971 0.1568 0.0533  0.0186  0.0192  636  ALA A O   
4663  C CB  . ALA A 638  ? 0.2499 0.4139 0.1797 0.0510  0.0147  0.0235  636  ALA A CB  
4664  N N   . ALA A 639  ? 0.2401 0.4321 0.1645 0.0549  0.0186  0.0253  637  ALA A N   
4665  C CA  . ALA A 639  ? 0.2495 0.4490 0.1742 0.0552  0.0208  0.0292  637  ALA A CA  
4666  C C   . ALA A 639  ? 0.2668 0.4688 0.1896 0.0578  0.0216  0.0208  637  ALA A C   
4667  O O   . ALA A 639  ? 0.2725 0.4734 0.1971 0.0575  0.0232  0.0220  637  ALA A O   
4668  C CB  . ALA A 639  ? 0.2677 0.4835 0.1903 0.0556  0.0215  0.0365  637  ALA A CB  
4669  N N   . CYS A 640  ? 0.2470 0.4520 0.1666 0.0604  0.0203  0.0122  638  CYS A N   
4670  C CA  . CYS A 640  ? 0.2448 0.4502 0.1636 0.0629  0.0206  0.0035  638  CYS A CA  
4671  C C   . CYS A 640  ? 0.2484 0.4376 0.1714 0.0612  0.0205  0.0010  638  CYS A C   
4672  O O   . CYS A 640  ? 0.2433 0.4318 0.1675 0.0619  0.0217  -0.0009 638  CYS A O   
4673  C CB  . CYS A 640  ? 0.2496 0.4594 0.1654 0.0657  0.0187  -0.0056 638  CYS A CB  
4674  S SG  . CYS A 640  ? 0.2832 0.5145 0.1934 0.0684  0.0189  -0.0048 638  CYS A SG  
4675  N N   . LEU A 641  ? 0.2349 0.4113 0.1601 0.0592  0.0189  0.0011  639  LEU A N   
4676  C CA  . LEU A 641  ? 0.2406 0.4020 0.1697 0.0575  0.0187  -0.0010 639  LEU A CA  
4677  C C   . LEU A 641  ? 0.2287 0.3874 0.1606 0.0554  0.0206  0.0060  639  LEU A C   
4678  O O   . LEU A 641  ? 0.2222 0.3750 0.1562 0.0553  0.0213  0.0036  639  LEU A O   
4679  C CB  . LEU A 641  ? 0.2278 0.3776 0.1587 0.0555  0.0169  -0.0011 639  LEU A CB  
4680  C CG  . LEU A 641  ? 0.2516 0.3971 0.1820 0.0569  0.0147  -0.0099 639  LEU A CG  
4681  C CD1 . LEU A 641  ? 0.2823 0.4403 0.2086 0.0598  0.0138  -0.0140 639  LEU A CD1 
4682  C CD2 . LEU A 641  ? 0.2276 0.3614 0.1603 0.0545  0.0132  -0.0088 639  LEU A CD2 
4683  N N   . ASP A 642  ? 0.2260 0.3890 0.1583 0.0538  0.0214  0.0147  640  ASP A N   
4684  C CA  . ASP A 642  ? 0.2264 0.3869 0.1620 0.0518  0.0230  0.0215  640  ASP A CA  
4685  C C   . ASP A 642  ? 0.2253 0.3953 0.1598 0.0535  0.0249  0.0209  640  ASP A C   
4686  O O   . ASP A 642  ? 0.2384 0.4032 0.1756 0.0526  0.0260  0.0219  640  ASP A O   
4687  C CB  . ASP A 642  ? 0.2315 0.3952 0.1686 0.0497  0.0230  0.0310  640  ASP A CB  
4688  C CG  . ASP A 642  ? 0.2462 0.3973 0.1863 0.0472  0.0215  0.0327  640  ASP A CG  
4689  O OD1 . ASP A 642  ? 0.2626 0.4015 0.2045 0.0465  0.0209  0.0282  640  ASP A OD1 
4690  O OD2 . ASP A 642  ? 0.2767 0.4305 0.2177 0.0460  0.0208  0.0388  640  ASP A OD2 
4691  N N   . ARG A 643  ? 0.2340 0.4184 0.1645 0.0562  0.0253  0.0190  641  ARG A N   
4692  C CA  . ARG A 643  ? 0.2382 0.4324 0.1676 0.0582  0.0271  0.0175  641  ARG A CA  
4693  C C   . ARG A 643  ? 0.2494 0.4362 0.1797 0.0597  0.0268  0.0087  641  ARG A C   
4694  O O   . ARG A 643  ? 0.2491 0.4360 0.1811 0.0599  0.0282  0.0087  641  ARG A O   
4695  C CB  . ARG A 643  ? 0.2294 0.4411 0.1540 0.0610  0.0275  0.0163  641  ARG A CB  
4696  C CG  . ARG A 643  ? 0.2528 0.4756 0.1770 0.0598  0.0286  0.0265  641  ARG A CG  
4697  C CD  . ARG A 643  ? 0.2913 0.5327 0.2110 0.0627  0.0291  0.0252  641  ARG A CD  
4698  N NE  . ARG A 643  ? 0.2820 0.5251 0.1987 0.0644  0.0270  0.0188  641  ARG A NE  
4699  C CZ  . ARG A 643  ? 0.2645 0.5110 0.1803 0.0635  0.0257  0.0228  641  ARG A CZ  
4700  N NH1 . ARG A 643  ? 0.3136 0.5609 0.2315 0.0609  0.0261  0.0332  641  ARG A NH1 
4701  N NH2 . ARG A 643  ? 0.3242 0.5730 0.2374 0.0654  0.0238  0.0162  641  ARG A NH2 
4702  N N   . ALA A 644  ? 0.2149 0.3953 0.1446 0.0606  0.0248  0.0012  642  ALA A N   
4703  C CA  . ALA A 644  ? 0.2225 0.3950 0.1539 0.0617  0.0242  -0.0068 642  ALA A CA  
4704  C C   . ALA A 644  ? 0.2282 0.3872 0.1639 0.0590  0.0246  -0.0038 642  ALA A C   
4705  O O   . ALA A 644  ? 0.2410 0.3970 0.1785 0.0597  0.0252  -0.0070 642  ALA A O   
4706  C CB  . ALA A 644  ? 0.2533 0.4208 0.1841 0.0629  0.0217  -0.0145 642  ALA A CB  
4707  N N   . ALA A 645  ? 0.2177 0.3686 0.1551 0.0559  0.0243  0.0022  643  ALA A N   
4708  C CA  . ALA A 645  ? 0.2165 0.3552 0.1579 0.0533  0.0246  0.0050  643  ALA A CA  
4709  C C   . ALA A 645  ? 0.2318 0.3753 0.1746 0.0529  0.0268  0.0100  643  ALA A C   
4710  O O   . ALA A 645  ? 0.2467 0.3833 0.1921 0.0523  0.0272  0.0088  643  ALA A O   
4711  C CB  . ALA A 645  ? 0.2191 0.3498 0.1621 0.0504  0.0237  0.0102  643  ALA A CB  
4712  N N   . GLU A 646  ? 0.2351 0.3904 0.1765 0.0532  0.0280  0.0159  644  GLU A N   
4713  C CA  . GLU A 646  ? 0.2479 0.4094 0.1906 0.0529  0.0300  0.0207  644  GLU A CA  
4714  C C   . GLU A 646  ? 0.2651 0.4311 0.2069 0.0557  0.0309  0.0142  644  GLU A C   
4715  O O   . GLU A 646  ? 0.2750 0.4381 0.2195 0.0551  0.0320  0.0152  644  GLU A O   
4716  C CB  . GLU A 646  ? 0.3128 0.4881 0.2539 0.0530  0.0311  0.0278  644  GLU A CB  
4717  C CG  . GLU A 646  ? 0.3458 0.5175 0.2889 0.0502  0.0303  0.0355  644  GLU A CG  
4718  C CD  . GLU A 646  ? 0.4631 0.6241 0.4114 0.0472  0.0306  0.0406  644  GLU A CD  
4719  O OE1 . GLU A 646  ? 0.5032 0.6654 0.4533 0.0471  0.0320  0.0420  644  GLU A OE1 
4720  O OE2 . GLU A 646  ? 0.4458 0.5973 0.3964 0.0450  0.0292  0.0431  644  GLU A OE2 
4721  N N   . LEU A 647  ? 0.2561 0.4294 0.1946 0.0587  0.0302  0.0073  645  LEU A N   
4722  C CA  . LEU A 647  ? 0.2462 0.4244 0.1842 0.0616  0.0308  0.0004  645  LEU A CA  
4723  C C   . LEU A 647  ? 0.2710 0.4351 0.2124 0.0611  0.0298  -0.0047 645  LEU A C   
4724  O O   . LEU A 647  ? 0.2873 0.4516 0.2306 0.0619  0.0307  -0.0066 645  LEU A O   
4725  C CB  . LEU A 647  ? 0.2541 0.4425 0.1883 0.0650  0.0299  -0.0065 645  LEU A CB  
4726  C CG  . LEU A 647  ? 0.2725 0.4777 0.2029 0.0662  0.0310  -0.0023 645  LEU A CG  
4727  C CD1 . LEU A 647  ? 0.2737 0.4874 0.2004 0.0694  0.0297  -0.0099 645  LEU A CD1 
4728  C CD2 . LEU A 647  ? 0.3208 0.5373 0.2513 0.0671  0.0335  0.0010  645  LEU A CD2 
4729  N N   . MET A 648  ? 0.2377 0.3900 0.1801 0.0596  0.0278  -0.0069 646  MET A N   
4730  C CA  . MET A 648  ? 0.2371 0.3763 0.1829 0.0589  0.0268  -0.0110 646  MET A CA  
4731  C C   . MET A 648  ? 0.2558 0.3880 0.2047 0.0562  0.0280  -0.0051 646  MET A C   
4732  O O   . MET A 648  ? 0.2571 0.3842 0.2086 0.0564  0.0281  -0.0078 646  MET A O   
4733  C CB  . MET A 648  ? 0.2207 0.3495 0.1669 0.0578  0.0245  -0.0139 646  MET A CB  
4734  C CG  . MET A 648  ? 0.2553 0.3885 0.1997 0.0606  0.0229  -0.0218 646  MET A CG  
4735  S SD  . MET A 648  ? 0.2873 0.4064 0.2337 0.0591  0.0201  -0.0259 646  MET A SD  
4736  C CE  . MET A 648  ? 0.3134 0.4410 0.2574 0.0627  0.0182  -0.0344 646  MET A CE  
4737  N N   . GLN A 649  ? 0.2413 0.3735 0.1906 0.0538  0.0288  0.0029  647  GLN A N   
4738  C CA  . GLN A 649  ? 0.2371 0.3634 0.1897 0.0513  0.0298  0.0085  647  GLN A CA  
4739  C C   . GLN A 649  ? 0.2517 0.3859 0.2049 0.0526  0.0317  0.0092  647  GLN A C   
4740  O O   . GLN A 649  ? 0.2780 0.4061 0.2341 0.0519  0.0320  0.0088  647  GLN A O   
4741  C CB  . GLN A 649  ? 0.2669 0.3931 0.2202 0.0488  0.0301  0.0168  647  GLN A CB  
4742  C CG  . GLN A 649  ? 0.2540 0.3730 0.2115 0.0461  0.0307  0.0222  647  GLN A CG  
4743  C CD  . GLN A 649  ? 0.2622 0.3667 0.2219 0.0443  0.0293  0.0197  647  GLN A CD  
4744  O OE1 . GLN A 649  ? 0.2473 0.3459 0.2073 0.0428  0.0282  0.0209  647  GLN A OE1 
4745  N NE2 . GLN A 649  ? 0.2578 0.3570 0.2192 0.0445  0.0295  0.0164  647  GLN A NE2 
4746  N N   . ALA A 650  ? 0.2593 0.4077 0.2099 0.0546  0.0329  0.0104  648  ALA A N   
4747  C CA  . ALA A 650  ? 0.2676 0.4250 0.2187 0.0559  0.0348  0.0114  648  ALA A CA  
4748  C C   . ALA A 650  ? 0.3209 0.4771 0.2725 0.0585  0.0345  0.0030  648  ALA A C   
4749  O O   . ALA A 650  ? 0.3269 0.4842 0.2806 0.0588  0.0357  0.0033  648  ALA A O   
4750  C CB  . ALA A 650  ? 0.2937 0.4677 0.2416 0.0576  0.0361  0.0143  648  ALA A CB  
4751  N N   . ARG A 651  ? 0.2699 0.4237 0.2201 0.0602  0.0327  -0.0045 649  ARG A N   
4752  C CA  . ARG A 651  ? 0.2625 0.4153 0.2138 0.0628  0.0319  -0.0131 649  ARG A CA  
4753  C C   . ARG A 651  ? 0.2582 0.3954 0.2131 0.0612  0.0304  -0.0156 649  ARG A C   
4754  O O   . ARG A 651  ? 0.2597 0.3942 0.2164 0.0631  0.0293  -0.0225 649  ARG A O   
4755  C CB  . ARG A 651  ? 0.2924 0.4517 0.2407 0.0658  0.0305  -0.0202 649  ARG A CB  
4756  C CG  . ARG A 651  ? 0.3605 0.5238 0.3099 0.0694  0.0299  -0.0293 649  ARG A CG  
4757  C CD  . ARG A 651  ? 0.3546 0.5331 0.3004 0.0729  0.0300  -0.0337 649  ARG A CD  
4758  N NE  . ARG A 651  ? 0.3850 0.5668 0.3323 0.0766  0.0290  -0.0433 649  ARG A NE  
4759  C CZ  . ARG A 651  ? 0.4079 0.5963 0.3566 0.0785  0.0304  -0.0450 649  ARG A CZ  
4760  N NH1 . ARG A 651  ? 0.4301 0.6223 0.3789 0.0771  0.0329  -0.0377 649  ARG A NH1 
4761  N NH2 . ARG A 651  ? 0.4249 0.6160 0.3755 0.0820  0.0291  -0.0543 649  ARG A NH2 
4762  N N   . MET A 652  ? 0.2529 0.3802 0.2092 0.0578  0.0302  -0.0101 650  MET A N   
4763  C CA  . MET A 652  ? 0.2557 0.3687 0.2150 0.0561  0.0286  -0.0122 650  MET A CA  
4764  C C   . MET A 652  ? 0.2741 0.3842 0.2366 0.0571  0.0286  -0.0160 650  MET A C   
4765  O O   . MET A 652  ? 0.2512 0.3546 0.2155 0.0578  0.0268  -0.0219 650  MET A O   
4766  C CB  . MET A 652  ? 0.2422 0.3466 0.2029 0.0524  0.0288  -0.0053 650  MET A CB  
4767  C CG  . MET A 652  ? 0.2694 0.3605 0.2333 0.0506  0.0275  -0.0069 650  MET A CG  
4768  S SD  . MET A 652  ? 0.3004 0.3818 0.2658 0.0465  0.0275  0.0001  650  MET A SD  
4769  C CE  . MET A 652  ? 0.2668 0.3475 0.2297 0.0462  0.0261  -0.0004 650  MET A CE  
4770  N N   . PRO A 653  ? 0.2441 0.3591 0.2077 0.0573  0.0305  -0.0130 651  PRO A N   
4771  C CA  . PRO A 653  ? 0.2932 0.4046 0.2602 0.0582  0.0303  -0.0167 651  PRO A CA  
4772  C C   . PRO A 653  ? 0.2780 0.3929 0.2453 0.0617  0.0290  -0.0255 651  PRO A C   
4773  O O   . PRO A 653  ? 0.2668 0.3736 0.2374 0.0619  0.0273  -0.0301 651  PRO A O   
4774  C CB  . PRO A 653  ? 0.2696 0.3885 0.2371 0.0582  0.0327  -0.0117 651  PRO A CB  
4775  C CG  . PRO A 653  ? 0.2956 0.4160 0.2615 0.0556  0.0337  -0.0038 651  PRO A CG  
4776  C CD  . PRO A 653  ? 0.2751 0.3981 0.2377 0.0564  0.0327  -0.0056 651  PRO A CD  
4777  N N   . THR A 654  ? 0.2448 0.3720 0.2091 0.0644  0.0295  -0.0281 652  THR A N   
4778  C CA  . THR A 654  ? 0.2557 0.3869 0.2205 0.0680  0.0281  -0.0371 652  THR A CA  
4779  C C   . THR A 654  ? 0.2473 0.3694 0.2129 0.0676  0.0253  -0.0416 652  THR A C   
4780  O O   . THR A 654  ? 0.2759 0.3933 0.2450 0.0691  0.0233  -0.0482 652  THR A O   
4781  C CB  . THR A 654  ? 0.2535 0.4008 0.2145 0.0709  0.0293  -0.0385 652  THR A CB  
4782  O OG1 . THR A 654  ? 0.2915 0.4475 0.2523 0.0711  0.0319  -0.0339 652  THR A OG1 
4783  C CG2 . THR A 654  ? 0.3078 0.4601 0.2697 0.0749  0.0276  -0.0486 652  THR A CG2 
4784  N N   . LEU A 655  ? 0.2420 0.3616 0.2050 0.0656  0.0250  -0.0380 653  LEU A N   
4785  C CA  . LEU A 655  ? 0.2603 0.3710 0.2242 0.0649  0.0224  -0.0416 653  LEU A CA  
4786  C C   . LEU A 655  ? 0.2908 0.3878 0.2591 0.0628  0.0211  -0.0418 653  LEU A C   
4787  O O   . LEU A 655  ? 0.2719 0.3628 0.2430 0.0635  0.0187  -0.0474 653  LEU A O   
4788  C CB  . LEU A 655  ? 0.2454 0.3556 0.2059 0.0629  0.0226  -0.0367 653  LEU A CB  
4789  C CG  . LEU A 655  ? 0.2397 0.3637 0.1957 0.0648  0.0237  -0.0360 653  LEU A CG  
4790  C CD1 . LEU A 655  ? 0.2635 0.3861 0.2169 0.0625  0.0237  -0.0306 653  LEU A CD1 
4791  C CD2 . LEU A 655  ? 0.3013 0.4320 0.2568 0.0684  0.0221  -0.0447 653  LEU A CD2 
4792  N N   . LEU A 656  ? 0.2687 0.3608 0.2380 0.0603  0.0225  -0.0356 654  LEU A N   
4793  C CA  . LEU A 656  ? 0.2671 0.3473 0.2405 0.0583  0.0214  -0.0355 654  LEU A CA  
4794  C C   . LEU A 656  ? 0.2702 0.3498 0.2476 0.0607  0.0200  -0.0422 654  LEU A C   
4795  O O   . LEU A 656  ? 0.2916 0.3626 0.2724 0.0602  0.0177  -0.0456 654  LEU A O   
4796  C CB  . LEU A 656  ? 0.2720 0.3496 0.2460 0.0559  0.0233  -0.0286 654  LEU A CB  
4797  C CG  . LEU A 656  ? 0.2871 0.3639 0.2587 0.0532  0.0245  -0.0213 654  LEU A CG  
4798  C CD1 . LEU A 656  ? 0.3250 0.3971 0.2987 0.0508  0.0257  -0.0160 654  LEU A CD1 
4799  C CD2 . LEU A 656  ? 0.2922 0.3617 0.2632 0.0515  0.0229  -0.0216 654  LEU A CD2 
4800  N N   . GLY A 657  ? 0.2674 0.3561 0.2448 0.0632  0.0213  -0.0439 655  GLY A N   
4801  C CA  . GLY A 657  ? 0.2807 0.3690 0.2623 0.0656  0.0200  -0.0502 655  GLY A CA  
4802  C C   . GLY A 657  ? 0.2571 0.3447 0.2405 0.0678  0.0172  -0.0580 655  GLY A C   
4803  O O   . GLY A 657  ? 0.2883 0.3692 0.2768 0.0683  0.0149  -0.0623 655  GLY A O   
4804  N N   . LEU A 658  ? 0.2575 0.3523 0.2372 0.0692  0.0172  -0.0599 656  LEU A N   
4805  C CA  . LEU A 658  ? 0.2468 0.3412 0.2282 0.0713  0.0143  -0.0675 656  LEU A CA  
4806  C C   . LEU A 658  ? 0.2235 0.3050 0.2075 0.0686  0.0120  -0.0669 656  LEU A C   
4807  O O   . LEU A 658  ? 0.2646 0.3405 0.2536 0.0694  0.0092  -0.0724 656  LEU A O   
4808  C CB  . LEU A 658  ? 0.2436 0.3493 0.2200 0.0733  0.0149  -0.0693 656  LEU A CB  
4809  C CG  . LEU A 658  ? 0.2759 0.3826 0.2538 0.0757  0.0120  -0.0774 656  LEU A CG  
4810  C CD1 . LEU A 658  ? 0.2876 0.3952 0.2710 0.0789  0.0101  -0.0856 656  LEU A CD1 
4811  C CD2 . LEU A 658  ? 0.2702 0.3893 0.2424 0.0776  0.0129  -0.0784 656  LEU A CD2 
4812  N N   . ILE A 659  ? 0.2381 0.3150 0.2191 0.0653  0.0130  -0.0602 657  ILE A N   
4813  C CA  . ILE A 659  ? 0.2354 0.3008 0.2186 0.0625  0.0111  -0.0591 657  ILE A CA  
4814  C C   . ILE A 659  ? 0.2453 0.3013 0.2339 0.0612  0.0100  -0.0590 657  ILE A C   
4815  O O   . ILE A 659  ? 0.2442 0.2927 0.2370 0.0606  0.0073  -0.0619 657  ILE A O   
4816  C CB  . ILE A 659  ? 0.2372 0.3003 0.2163 0.0594  0.0127  -0.0517 657  ILE A CB  
4817  C CG1 . ILE A 659  ? 0.2686 0.3403 0.2429 0.0606  0.0132  -0.0523 657  ILE A CG1 
4818  C CG2 . ILE A 659  ? 0.2563 0.3078 0.2378 0.0563  0.0111  -0.0500 657  ILE A CG2 
4819  C CD1 . ILE A 659  ? 0.2686 0.3405 0.2391 0.0581  0.0150  -0.0449 657  ILE A CD1 
4820  N N   . ILE A 660  ? 0.2279 0.2845 0.2168 0.0606  0.0119  -0.0553 658  ILE A N   
4821  C CA  . ILE A 660  ? 0.2513 0.2998 0.2452 0.0594  0.0109  -0.0547 658  ILE A CA  
4822  C C   . ILE A 660  ? 0.2551 0.3028 0.2546 0.0620  0.0082  -0.0622 658  ILE A C   
4823  O O   . ILE A 660  ? 0.2798 0.3187 0.2842 0.0607  0.0058  -0.0633 658  ILE A O   
4824  C CB  . ILE A 660  ? 0.2221 0.2733 0.2152 0.0589  0.0135  -0.0502 658  ILE A CB  
4825  C CG1 . ILE A 660  ? 0.2442 0.2925 0.2337 0.0555  0.0154  -0.0425 658  ILE A CG1 
4826  C CG2 . ILE A 660  ? 0.2546 0.3001 0.2533 0.0588  0.0124  -0.0514 658  ILE A CG2 
4827  C CD1 . ILE A 660  ? 0.2904 0.3429 0.2790 0.0552  0.0180  -0.0380 658  ILE A CD1 
4828  N N   . ARG A 661  ? 0.2446 0.3017 0.2437 0.0657  0.0084  -0.0676 659  ARG A N   
4829  C CA  . ARG A 661  ? 0.2594 0.3165 0.2645 0.0685  0.0058  -0.0751 659  ARG A CA  
4830  C C   . ARG A 661  ? 0.3060 0.3613 0.3133 0.0696  0.0027  -0.0809 659  ARG A C   
4831  O O   . ARG A 661  ? 0.2743 0.3239 0.2883 0.0702  -0.0003 -0.0854 659  ARG A O   
4832  C CB  . ARG A 661  ? 0.2739 0.3424 0.2784 0.0722  0.0073  -0.0789 659  ARG A CB  
4833  C CG  . ARG A 661  ? 0.2584 0.3271 0.2634 0.0715  0.0094  -0.0744 659  ARG A CG  
4834  C CD  . ARG A 661  ? 0.2688 0.3496 0.2727 0.0749  0.0113  -0.0774 659  ARG A CD  
4835  N NE  . ARG A 661  ? 0.2897 0.3740 0.2985 0.0788  0.0089  -0.0865 659  ARG A NE  
4836  C CZ  . ARG A 661  ? 0.2752 0.3706 0.2821 0.0824  0.0090  -0.0924 659  ARG A CZ  
4837  N NH1 . ARG A 661  ? 0.2918 0.3960 0.2918 0.0826  0.0113  -0.0898 659  ARG A NH1 
4838  N NH2 . ARG A 661  ? 0.2846 0.3827 0.2969 0.0861  0.0066  -0.1010 659  ARG A NH2 
4839  N N   . GLU A 662  ? 0.2770 0.3369 0.2792 0.0697  0.0033  -0.0808 660  GLU A N   
4840  C CA  . GLU A 662  ? 0.2587 0.3176 0.2629 0.0709  0.0003  -0.0867 660  GLU A CA  
4841  C C   . GLU A 662  ? 0.2599 0.3073 0.2666 0.0674  -0.0016 -0.0838 660  GLU A C   
4842  O O   . GLU A 662  ? 0.2848 0.3274 0.2970 0.0679  -0.0049 -0.0886 660  GLU A O   
4843  C CB  . GLU A 662  ? 0.2976 0.3667 0.2956 0.0725  0.0015  -0.0880 660  GLU A CB  
4844  C CG  . GLU A 662  ? 0.2807 0.3497 0.2808 0.0741  -0.0017 -0.0947 660  GLU A CG  
4845  C CD  . GLU A 662  ? 0.2841 0.3640 0.2780 0.0759  -0.0007 -0.0963 660  GLU A CD  
4846  O OE1 . GLU A 662  ? 0.2809 0.3650 0.2686 0.0745  0.0023  -0.0899 660  GLU A OE1 
4847  O OE2 . GLU A 662  ? 0.3024 0.3866 0.2980 0.0787  -0.0030 -0.1038 660  GLU A OE2 
4848  N N   . ALA A 663  ? 0.2600 0.3030 0.2632 0.0639  0.0004  -0.0760 661  ALA A N   
4849  C CA  . ALA A 663  ? 0.2473 0.2813 0.2513 0.0606  -0.0010 -0.0730 661  ALA A CA  
4850  C C   . ALA A 663  ? 0.2659 0.2905 0.2731 0.0574  -0.0010 -0.0679 661  ALA A C   
4851  O O   . ALA A 663  ? 0.3212 0.3391 0.3284 0.0544  -0.0016 -0.0643 661  ALA A O   
4852  C CB  . ALA A 663  ? 0.2844 0.3212 0.2818 0.0592  0.0008  -0.0689 661  ALA A CB  
4853  N N   . GLY A 664  ? 0.2886 0.3130 0.2983 0.0580  -0.0004 -0.0674 662  GLY A N   
4854  C CA  . GLY A 664  ? 0.3119 0.3277 0.3247 0.0550  -0.0007 -0.0628 662  GLY A CA  
4855  C C   . GLY A 664  ? 0.2806 0.2944 0.2886 0.0518  0.0020  -0.0552 662  GLY A C   
4856  O O   . GLY A 664  ? 0.3304 0.3368 0.3404 0.0489  0.0014  -0.0513 662  GLY A O   
4857  N N   . LYS A 665  ? 0.2429 0.2633 0.2449 0.0523  0.0047  -0.0529 663  LYS A N   
4858  C CA  . LYS A 665  ? 0.2493 0.2681 0.2472 0.0494  0.0069  -0.0461 663  LYS A CA  
4859  C C   . LYS A 665  ? 0.2176 0.2374 0.2153 0.0490  0.0090  -0.0423 663  LYS A C   
4860  O O   . LYS A 665  ? 0.2369 0.2624 0.2351 0.0514  0.0097  -0.0445 663  LYS A O   
4861  C CB  . LYS A 665  ? 0.2691 0.2946 0.2613 0.0501  0.0085  -0.0451 663  LYS A CB  
4862  C CG  . LYS A 665  ? 0.2708 0.2966 0.2627 0.0508  0.0066  -0.0488 663  LYS A CG  
4863  C CD  . LYS A 665  ? 0.3112 0.3279 0.3053 0.0479  0.0050  -0.0471 663  LYS A CD  
4864  C CE  . LYS A 665  ? 0.3378 0.3553 0.3309 0.0483  0.0034  -0.0501 663  LYS A CE  
4865  N NZ  . LYS A 665  ? 0.3557 0.3648 0.3519 0.0458  0.0014  -0.0491 663  LYS A NZ  
4866  N N   . SER A 666  ? 0.2455 0.2599 0.2425 0.0459  0.0099  -0.0367 664  SER A N   
4867  C CA  . SER A 666  ? 0.2430 0.2587 0.2390 0.0451  0.0120  -0.0325 664  SER A CA  
4868  C C   . SER A 666  ? 0.2908 0.3141 0.2819 0.0457  0.0145  -0.0300 664  SER A C   
4869  O O   . SER A 666  ? 0.2587 0.2853 0.2468 0.0462  0.0146  -0.0307 664  SER A O   
4870  C CB  . SER A 666  ? 0.2813 0.2898 0.2778 0.0416  0.0121  -0.0275 664  SER A CB  
4871  O OG  . SER A 666  ? 0.2989 0.3070 0.2917 0.0400  0.0129  -0.0245 664  SER A OG  
4872  N N   . ALA A 667  ? 0.2772 0.3036 0.2678 0.0457  0.0164  -0.0269 665  ALA A N   
4873  C CA  . ALA A 667  ? 0.2510 0.2847 0.2377 0.0460  0.0188  -0.0236 665  ALA A CA  
4874  C C   . ALA A 667  ? 0.2685 0.2995 0.2525 0.0435  0.0192  -0.0193 665  ALA A C   
4875  O O   . ALA A 667  ? 0.2454 0.2817 0.2263 0.0442  0.0199  -0.0186 665  ALA A O   
4876  C CB  . ALA A 667  ? 0.2745 0.3111 0.2620 0.0460  0.0206  -0.0204 665  ALA A CB  
4877  N N   . LEU A 668  ? 0.2615 0.2846 0.2469 0.0408  0.0187  -0.0164 666  LEU A N   
4878  C CA  . LEU A 668  ? 0.2869 0.3072 0.2703 0.0385  0.0190  -0.0128 666  LEU A CA  
4879  C C   . LEU A 668  ? 0.2861 0.3068 0.2679 0.0391  0.0178  -0.0156 666  LEU A C   
4880  O O   . LEU A 668  ? 0.2758 0.2992 0.2548 0.0388  0.0184  -0.0135 666  LEU A O   
4881  C CB  . LEU A 668  ? 0.3189 0.3308 0.3044 0.0357  0.0183  -0.0106 666  LEU A CB  
4882  C CG  . LEU A 668  ? 0.4048 0.4157 0.3911 0.0342  0.0196  -0.0061 666  LEU A CG  
4883  C CD1 . LEU A 668  ? 0.3604 0.3636 0.3486 0.0317  0.0186  -0.0049 666  LEU A CD1 
4884  C CD2 . LEU A 668  ? 0.4196 0.4341 0.4036 0.0335  0.0211  -0.0021 666  LEU A CD2 
4885  N N   . ASN A 669  ? 0.2517 0.2695 0.2356 0.0400  0.0158  -0.0203 667  ASN A N   
4886  C CA  . ASN A 669  ? 0.2598 0.2776 0.2426 0.0405  0.0144  -0.0231 667  ASN A CA  
4887  C C   . ASN A 669  ? 0.2493 0.2760 0.2294 0.0432  0.0150  -0.0256 667  ASN A C   
4888  O O   . ASN A 669  ? 0.2718 0.3005 0.2495 0.0433  0.0147  -0.0257 667  ASN A O   
4889  C CB  . ASN A 669  ? 0.3097 0.3219 0.2963 0.0405  0.0120  -0.0271 667  ASN A CB  
4890  C CG  . ASN A 669  ? 0.3438 0.3479 0.3326 0.0375  0.0113  -0.0242 667  ASN A CG  
4891  O OD1 . ASN A 669  ? 0.4308 0.4305 0.4234 0.0371  0.0098  -0.0257 667  ASN A OD1 
4892  N ND2 . ASN A 669  ? 0.4209 0.4233 0.4074 0.0353  0.0124  -0.0199 667  ASN A ND2 
4893  N N   . ALA A 670  ? 0.2342 0.2668 0.2146 0.0455  0.0157  -0.0275 668  ALA A N   
4894  C CA  . ALA A 670  ? 0.2375 0.2799 0.2151 0.0482  0.0164  -0.0296 668  ALA A CA  
4895  C C   . ALA A 670  ? 0.2423 0.2896 0.2162 0.0473  0.0185  -0.0240 668  ALA A C   
4896  O O   . ALA A 670  ? 0.2471 0.3006 0.2180 0.0484  0.0187  -0.0245 668  ALA A O   
4897  C CB  . ALA A 670  ? 0.2429 0.2907 0.2220 0.0508  0.0169  -0.0329 668  ALA A CB  
4898  N N   . ILE A 671  ? 0.2321 0.2770 0.2065 0.0452  0.0199  -0.0187 669  ILE A N   
4899  C CA  . ILE A 671  ? 0.2409 0.2895 0.2129 0.0441  0.0215  -0.0129 669  ILE A CA  
4900  C C   . ILE A 671  ? 0.2552 0.3006 0.2257 0.0427  0.0206  -0.0120 669  ILE A C   
4901  O O   . ILE A 671  ? 0.2577 0.3090 0.2256 0.0432  0.0211  -0.0103 669  ILE A O   
4902  C CB  . ILE A 671  ? 0.2530 0.2980 0.2268 0.0419  0.0228  -0.0078 669  ILE A CB  
4903  C CG1 . ILE A 671  ? 0.2472 0.2971 0.2221 0.0433  0.0240  -0.0080 669  ILE A CG1 
4904  C CG2 . ILE A 671  ? 0.2938 0.3406 0.2662 0.0402  0.0238  -0.0019 669  ILE A CG2 
4905  C CD1 . ILE A 671  ? 0.2781 0.3230 0.2556 0.0413  0.0247  -0.0041 669  ILE A CD1 
4906  N N   . ALA A 672  ? 0.2330 0.2693 0.2053 0.0408  0.0192  -0.0127 670  ALA A N   
4907  C CA  . ALA A 672  ? 0.2416 0.2746 0.2130 0.0395  0.0183  -0.0121 670  ALA A CA  
4908  C C   . ALA A 672  ? 0.2377 0.2755 0.2071 0.0416  0.0173  -0.0163 670  ALA A C   
4909  O O   . ALA A 672  ? 0.2453 0.2852 0.2126 0.0413  0.0172  -0.0148 670  ALA A O   
4910  C CB  . ALA A 672  ? 0.2565 0.2799 0.2304 0.0375  0.0170  -0.0129 670  ALA A CB  
4911  N N   . GLU A 673  ? 0.2271 0.2669 0.1975 0.0438  0.0163  -0.0217 671  GLU A N   
4912  C CA  . GLU A 673  ? 0.2306 0.2751 0.1996 0.0460  0.0150  -0.0265 671  GLU A CA  
4913  C C   . GLU A 673  ? 0.2574 0.3125 0.2227 0.0476  0.0165  -0.0248 671  GLU A C   
4914  O O   . GLU A 673  ? 0.2309 0.2891 0.1938 0.0480  0.0159  -0.0252 671  GLU A O   
4915  C CB  . GLU A 673  ? 0.2501 0.2951 0.2218 0.0483  0.0137  -0.0328 671  GLU A CB  
4916  C CG  . GLU A 673  ? 0.3049 0.3554 0.2756 0.0510  0.0123  -0.0387 671  GLU A CG  
4917  C CD  . GLU A 673  ? 0.3084 0.3523 0.2810 0.0500  0.0098  -0.0414 671  GLU A CD  
4918  O OE1 . GLU A 673  ? 0.3553 0.3903 0.3301 0.0474  0.0093  -0.0390 671  GLU A OE1 
4919  O OE2 . GLU A 673  ? 0.2821 0.3300 0.2541 0.0519  0.0084  -0.0460 671  GLU A OE2 
4920  N N   . VAL A 674  ? 0.2284 0.2894 0.1931 0.0485  0.0183  -0.0227 672  VAL A N   
4921  C CA  . VAL A 674  ? 0.2180 0.2899 0.1794 0.0499  0.0197  -0.0204 672  VAL A CA  
4922  C C   . VAL A 674  ? 0.2229 0.2943 0.1829 0.0476  0.0205  -0.0138 672  VAL A C   
4923  O O   . VAL A 674  ? 0.2097 0.2876 0.1669 0.0483  0.0206  -0.0127 672  VAL A O   
4924  C CB  . VAL A 674  ? 0.2166 0.2953 0.1781 0.0513  0.0215  -0.0195 672  VAL A CB  
4925  C CG1 . VAL A 674  ? 0.2261 0.3172 0.1843 0.0527  0.0230  -0.0168 672  VAL A CG1 
4926  C CG2 . VAL A 674  ? 0.2429 0.3224 0.2063 0.0538  0.0206  -0.0266 672  VAL A CG2 
4927  N N   . ARG A 675  ? 0.2188 0.2824 0.1808 0.0449  0.0209  -0.0095 673  ARG A N   
4928  C CA  . ARG A 675  ? 0.2182 0.2804 0.1797 0.0428  0.0213  -0.0039 673  ARG A CA  
4929  C C   . ARG A 675  ? 0.2086 0.2689 0.1688 0.0426  0.0197  -0.0058 673  ARG A C   
4930  O O   . ARG A 675  ? 0.2193 0.2840 0.1779 0.0424  0.0199  -0.0026 673  ARG A O   
4931  C CB  . ARG A 675  ? 0.1983 0.2517 0.1627 0.0401  0.0215  -0.0004 673  ARG A CB  
4932  C CG  . ARG A 675  ? 0.2133 0.2688 0.1791 0.0398  0.0231  0.0030  673  ARG A CG  
4933  C CD  . ARG A 675  ? 0.2306 0.2782 0.1993 0.0370  0.0232  0.0068  673  ARG A CD  
4934  N NE  . ARG A 675  ? 0.2262 0.2736 0.1948 0.0355  0.0231  0.0113  673  ARG A NE  
4935  C CZ  . ARG A 675  ? 0.2170 0.2575 0.1879 0.0332  0.0227  0.0139  673  ARG A CZ  
4936  N NH1 . ARG A 675  ? 0.2215 0.2546 0.1943 0.0320  0.0224  0.0125  673  ARG A NH1 
4937  N NH2 . ARG A 675  ? 0.2100 0.2513 0.1814 0.0321  0.0226  0.0179  673  ARG A NH2 
4938  N N   . GLU A 676  ? 0.2145 0.2684 0.1759 0.0426  0.0181  -0.0107 674  GLU A N   
4939  C CA  . GLU A 676  ? 0.2135 0.2654 0.1741 0.0424  0.0165  -0.0126 674  GLU A CA  
4940  C C   . GLU A 676  ? 0.2217 0.2831 0.1792 0.0448  0.0162  -0.0149 674  GLU A C   
4941  O O   . GLU A 676  ? 0.2176 0.2809 0.1735 0.0445  0.0157  -0.0135 674  GLU A O   
4942  C CB  . GLU A 676  ? 0.2076 0.2515 0.1706 0.0420  0.0147  -0.0174 674  GLU A CB  
4943  C CG  . GLU A 676  ? 0.2762 0.3170 0.2388 0.0412  0.0131  -0.0186 674  GLU A CG  
4944  C CD  . GLU A 676  ? 0.4403 0.4719 0.4060 0.0397  0.0116  -0.0210 674  GLU A CD  
4945  O OE1 . GLU A 676  ? 0.5934 0.6219 0.5614 0.0399  0.0113  -0.0231 674  GLU A OE1 
4946  O OE2 . GLU A 676  ? 0.5478 0.5756 0.5137 0.0383  0.0107  -0.0206 674  GLU A OE2 
4947  N N   . ALA A 677  ? 0.2157 0.2838 0.1724 0.0474  0.0165  -0.0186 675  ALA A N   
4948  C CA  . ALA A 677  ? 0.1900 0.2684 0.1436 0.0499  0.0163  -0.0210 675  ALA A CA  
4949  C C   . ALA A 677  ? 0.2235 0.3095 0.1746 0.0495  0.0178  -0.0146 675  ALA A C   
4950  O O   . ALA A 677  ? 0.2162 0.3073 0.1650 0.0500  0.0172  -0.0142 675  ALA A O   
4951  C CB  . ALA A 677  ? 0.2111 0.2957 0.1646 0.0528  0.0164  -0.0263 675  ALA A CB  
4952  N N   . ILE A 678  ? 0.2077 0.2949 0.1596 0.0485  0.0196  -0.0095 676  ILE A N   
4953  C CA  . ILE A 678  ? 0.2089 0.3027 0.1595 0.0477  0.0210  -0.0025 676  ILE A CA  
4954  C C   . ILE A 678  ? 0.2119 0.3004 0.1630 0.0455  0.0201  0.0011  676  ILE A C   
4955  O O   . ILE A 678  ? 0.2267 0.3217 0.1761 0.0457  0.0201  0.0044  676  ILE A O   
4956  C CB  . ILE A 678  ? 0.2125 0.3061 0.1652 0.0466  0.0227  0.0022  676  ILE A CB  
4957  C CG1 . ILE A 678  ? 0.2253 0.3260 0.1772 0.0491  0.0237  -0.0012 676  ILE A CG1 
4958  C CG2 . ILE A 678  ? 0.2263 0.3245 0.1791 0.0452  0.0238  0.0102  676  ILE A CG2 
4959  C CD1 . ILE A 678  ? 0.2165 0.3148 0.1711 0.0481  0.0252  0.0019  676  ILE A CD1 
4960  N N   . ASP A 679  ? 0.2082 0.2854 0.1620 0.0435  0.0193  0.0007  677  ASP A N   
4961  C CA  . ASP A 679  ? 0.2041 0.2759 0.1589 0.0414  0.0185  0.0038  677  ASP A CA  
4962  C C   . ASP A 679  ? 0.2207 0.2943 0.1733 0.0424  0.0169  0.0005  677  ASP A C   
4963  O O   . ASP A 679  ? 0.2132 0.2889 0.1654 0.0417  0.0165  0.0041  677  ASP A O   
4964  C CB  . ASP A 679  ? 0.2032 0.2633 0.1611 0.0393  0.0180  0.0034  677  ASP A CB  
4965  C CG  . ASP A 679  ? 0.2407 0.2985 0.2009 0.0379  0.0194  0.0075  677  ASP A CG  
4966  O OD1 . ASP A 679  ? 0.2526 0.3164 0.2129 0.0379  0.0205  0.0125  677  ASP A OD1 
4967  O OD2 . ASP A 679  ? 0.2780 0.3281 0.2404 0.0368  0.0192  0.0060  677  ASP A OD2 
4968  N N   . PHE A 680  ? 0.2055 0.2786 0.1574 0.0440  0.0158  -0.0063 678  PHE A N   
4969  C CA  . PHE A 680  ? 0.1995 0.2755 0.1495 0.0452  0.0142  -0.0098 678  PHE A CA  
4970  C C   . PHE A 680  ? 0.2127 0.3007 0.1595 0.0468  0.0147  -0.0075 678  PHE A C   
4971  O O   . PHE A 680  ? 0.2148 0.3050 0.1604 0.0465  0.0139  -0.0058 678  PHE A O   
4972  C CB  . PHE A 680  ? 0.2031 0.2782 0.1533 0.0471  0.0128  -0.0176 678  PHE A CB  
4973  C CG  . PHE A 680  ? 0.2275 0.2916 0.1807 0.0456  0.0114  -0.0205 678  PHE A CG  
4974  C CD1 . PHE A 680  ? 0.2078 0.2662 0.1618 0.0437  0.0105  -0.0189 678  PHE A CD1 
4975  C CD2 . PHE A 680  ? 0.2346 0.2946 0.1901 0.0461  0.0110  -0.0247 678  PHE A CD2 
4976  C CE1 . PHE A 680  ? 0.2245 0.2736 0.1814 0.0423  0.0092  -0.0214 678  PHE A CE1 
4977  C CE2 . PHE A 680  ? 0.2273 0.2777 0.1858 0.0447  0.0096  -0.0269 678  PHE A CE2 
4978  C CZ  . PHE A 680  ? 0.2327 0.2779 0.1919 0.0427  0.0087  -0.0252 678  PHE A CZ  
4979  N N   . LEU A 681  ? 0.2027 0.2991 0.1479 0.0486  0.0160  -0.0075 679  LEU A N   
4980  C CA  . LEU A 681  ? 0.1980 0.3071 0.1400 0.0501  0.0167  -0.0051 679  LEU A CA  
4981  C C   . LEU A 681  ? 0.2182 0.3283 0.1607 0.0481  0.0172  0.0031  679  LEU A C   
4982  O O   . LEU A 681  ? 0.2026 0.3184 0.1433 0.0484  0.0165  0.0049  679  LEU A O   
4983  C CB  . LEU A 681  ? 0.2193 0.3371 0.1603 0.0520  0.0183  -0.0055 679  LEU A CB  
4984  C CG  . LEU A 681  ? 0.2240 0.3436 0.1644 0.0547  0.0176  -0.0142 679  LEU A CG  
4985  C CD1 . LEU A 681  ? 0.2226 0.3472 0.1633 0.0560  0.0193  -0.0144 679  LEU A CD1 
4986  C CD2 . LEU A 681  ? 0.2384 0.3676 0.1754 0.0572  0.0164  -0.0185 679  LEU A CD2 
4987  N N   . ARG A 682  ? 0.1984 0.3029 0.1439 0.0459  0.0183  0.0082  680  ARG A N   
4988  C CA  . ARG A 682  ? 0.2171 0.3227 0.1641 0.0440  0.0186  0.0161  680  ARG A CA  
4989  C C   . ARG A 682  ? 0.2080 0.3060 0.1563 0.0424  0.0170  0.0166  680  ARG A C   
4990  O O   . ARG A 682  ? 0.2092 0.3107 0.1576 0.0418  0.0166  0.0215  680  ARG A O   
4991  C CB  . ARG A 682  ? 0.2049 0.3066 0.1552 0.0423  0.0200  0.0210  680  ARG A CB  
4992  C CG  . ARG A 682  ? 0.2271 0.3382 0.1763 0.0437  0.0217  0.0223  680  ARG A CG  
4993  C CD  . ARG A 682  ? 0.2278 0.3342 0.1806 0.0419  0.0229  0.0265  680  ARG A CD  
4994  N NE  . ARG A 682  ? 0.2356 0.3516 0.1875 0.0432  0.0246  0.0283  680  ARG A NE  
4995  C CZ  . ARG A 682  ? 0.2677 0.3815 0.2222 0.0423  0.0258  0.0303  680  ARG A CZ  
4996  N NH1 . ARG A 682  ? 0.2624 0.3649 0.2203 0.0403  0.0254  0.0308  680  ARG A NH1 
4997  N NH2 . ARG A 682  ? 0.2851 0.4089 0.2386 0.0437  0.0274  0.0319  680  ARG A NH2 
4998  N N   . TYR A 683  ? 0.2077 0.2958 0.1572 0.0418  0.0161  0.0118  681  TYR A N   
4999  C CA  . TYR A 683  ? 0.1961 0.2772 0.1470 0.0404  0.0146  0.0119  681  TYR A CA  
5000  C C   . TYR A 683  ? 0.2329 0.3199 0.1811 0.0418  0.0133  0.0096  681  TYR A C   
5001  O O   . TYR A 683  ? 0.2116 0.2994 0.1603 0.0409  0.0126  0.0133  681  TYR A O   
5002  C CB  . TYR A 683  ? 0.2119 0.2821 0.1648 0.0394  0.0140  0.0073  681  TYR A CB  
5003  C CG  . TYR A 683  ? 0.2003 0.2638 0.1547 0.0380  0.0125  0.0070  681  TYR A CG  
5004  C CD1 . TYR A 683  ? 0.2074 0.2660 0.1647 0.0358  0.0126  0.0118  681  TYR A CD1 
5005  C CD2 . TYR A 683  ? 0.2093 0.2715 0.1625 0.0388  0.0110  0.0017  681  TYR A CD2 
5006  C CE1 . TYR A 683  ? 0.2185 0.2716 0.1773 0.0347  0.0114  0.0113  681  TYR A CE1 
5007  C CE2 . TYR A 683  ? 0.2083 0.2650 0.1629 0.0375  0.0098  0.0015  681  TYR A CE2 
5008  C CZ  . TYR A 683  ? 0.2173 0.2695 0.1746 0.0355  0.0100  0.0063  681  TYR A CZ  
5009  O OH  . TYR A 683  ? 0.2264 0.2735 0.1852 0.0343  0.0088  0.0058  681  TYR A OH  
5010  N N   . TYR A 684  ? 0.2065 0.2978 0.1519 0.0440  0.0128  0.0035  682  TYR A N   
5011  C CA  . TYR A 684  ? 0.2029 0.3000 0.1456 0.0455  0.0114  0.0009  682  TYR A CA  
5012  C C   . TYR A 684  ? 0.2385 0.3474 0.1789 0.0463  0.0120  0.0061  682  TYR A C   
5013  O O   . TYR A 684  ? 0.2200 0.3325 0.1592 0.0465  0.0109  0.0072  682  TYR A O   
5014  C CB  . TYR A 684  ? 0.2082 0.3073 0.1492 0.0478  0.0104  -0.0074 682  TYR A CB  
5015  C CG  . TYR A 684  ? 0.2024 0.2902 0.1462 0.0469  0.0094  -0.0122 682  TYR A CG  
5016  C CD1 . TYR A 684  ? 0.2001 0.2791 0.1461 0.0448  0.0084  -0.0111 682  TYR A CD1 
5017  C CD2 . TYR A 684  ? 0.2165 0.3027 0.1609 0.0482  0.0093  -0.0177 682  TYR A CD2 
5018  C CE1 . TYR A 684  ? 0.2164 0.2858 0.1651 0.0438  0.0075  -0.0150 682  TYR A CE1 
5019  C CE2 . TYR A 684  ? 0.2071 0.2833 0.1545 0.0472  0.0082  -0.0215 682  TYR A CE2 
5020  C CZ  . TYR A 684  ? 0.2148 0.2828 0.1642 0.0450  0.0074  -0.0200 682  TYR A CZ  
5021  O OH  . TYR A 684  ? 0.2176 0.2765 0.1700 0.0439  0.0063  -0.0233 682  TYR A OH  
5022  N N   . ALA A 685  ? 0.2033 0.3187 0.1432 0.0467  0.0137  0.0096  683  ALA A N   
5023  C CA  . ALA A 685  ? 0.2214 0.3479 0.1599 0.0470  0.0144  0.0159  683  ALA A CA  
5024  C C   . ALA A 685  ? 0.2200 0.3423 0.1615 0.0446  0.0138  0.0229  683  ALA A C   
5025  O O   . ALA A 685  ? 0.2155 0.3441 0.1558 0.0448  0.0130  0.0260  683  ALA A O   
5026  C CB  . ALA A 685  ? 0.2157 0.3490 0.1541 0.0475  0.0165  0.0190  683  ALA A CB  
5027  N N   . GLU A 686  ? 0.2181 0.3300 0.1637 0.0424  0.0142  0.0252  684  GLU A N   
5028  C CA  . GLU A 686  ? 0.2248 0.3324 0.1740 0.0402  0.0135  0.0314  684  GLU A CA  
5029  C C   . GLU A 686  ? 0.2062 0.3096 0.1553 0.0400  0.0116  0.0288  684  GLU A C   
5030  O O   . GLU A 686  ? 0.2302 0.3365 0.1802 0.0394  0.0107  0.0333  684  GLU A O   
5031  C CB  . GLU A 686  ? 0.2581 0.3559 0.2118 0.0381  0.0142  0.0337  684  GLU A CB  
5032  C CG  . GLU A 686  ? 0.2933 0.3855 0.2516 0.0359  0.0132  0.0390  684  GLU A CG  
5033  C CD  . GLU A 686  ? 0.3264 0.4271 0.2860 0.0356  0.0130  0.0468  684  GLU A CD  
5034  O OE1 . GLU A 686  ? 0.3206 0.4316 0.2781 0.0366  0.0141  0.0495  684  GLU A OE1 
5035  O OE2 . GLU A 686  ? 0.3817 0.4790 0.3450 0.0342  0.0118  0.0506  684  GLU A OE2 
5036  N N   . GLN A 687  ? 0.2006 0.2973 0.1489 0.0404  0.0109  0.0217  685  GLN A N   
5037  C CA  . GLN A 687  ? 0.2081 0.3010 0.1564 0.0402  0.0091  0.0190  685  GLN A CA  
5038  C C   . GLN A 687  ? 0.2269 0.3302 0.1718 0.0419  0.0082  0.0189  685  GLN A C   
5039  O O   . GLN A 687  ? 0.2223 0.3254 0.1678 0.0414  0.0068  0.0205  685  GLN A O   
5040  C CB  . GLN A 687  ? 0.2002 0.2854 0.1484 0.0404  0.0085  0.0115  685  GLN A CB  
5041  C CG  . GLN A 687  ? 0.2071 0.2815 0.1589 0.0384  0.0091  0.0118  685  GLN A CG  
5042  C CD  . GLN A 687  ? 0.2654 0.3341 0.2208 0.0363  0.0086  0.0162  685  GLN A CD  
5043  O OE1 . GLN A 687  ? 0.2510 0.3181 0.2067 0.0361  0.0072  0.0153  685  GLN A OE1 
5044  N NE2 . GLN A 687  ? 0.3026 0.3684 0.2610 0.0349  0.0096  0.0208  685  GLN A NE2 
5045  N N   . THR A 688  ? 0.2133 0.3263 0.1546 0.0440  0.0089  0.0170  686  THR A N   
5046  C CA  . THR A 688  ? 0.1882 0.3127 0.1259 0.0458  0.0081  0.0171  686  THR A CA  
5047  C C   . THR A 688  ? 0.2370 0.3672 0.1758 0.0447  0.0082  0.0259  686  THR A C   
5048  O O   . THR A 688  ? 0.2343 0.3680 0.1725 0.0448  0.0068  0.0275  686  THR A O   
5049  C CB  . THR A 688  ? 0.2226 0.3569 0.1564 0.0483  0.0091  0.0134  686  THR A CB  
5050  O OG1 . THR A 688  ? 0.2284 0.3577 0.1616 0.0495  0.0083  0.0047  686  THR A OG1 
5051  C CG2 . THR A 688  ? 0.2127 0.3607 0.1427 0.0501  0.0085  0.0144  686  THR A CG2 
5052  N N   . ARG A 689  ? 0.2218 0.3533 0.1627 0.0437  0.0097  0.0319  687  ARG A N   
5053  C CA  . ARG A 689  ? 0.2418 0.3789 0.1848 0.0425  0.0097  0.0409  687  ARG A CA  
5054  C C   . ARG A 689  ? 0.2351 0.3636 0.1824 0.0405  0.0082  0.0437  687  ARG A C   
5055  O O   . ARG A 689  ? 0.2641 0.3974 0.2129 0.0399  0.0073  0.0500  687  ARG A O   
5056  C CB  . ARG A 689  ? 0.2404 0.3788 0.1859 0.0415  0.0115  0.0464  687  ARG A CB  
5057  C CG  . ARG A 689  ? 0.2781 0.4282 0.2196 0.0435  0.0130  0.0456  687  ARG A CG  
5058  C CD  . ARG A 689  ? 0.2855 0.4377 0.2300 0.0423  0.0147  0.0523  687  ARG A CD  
5059  N NE  . ARG A 689  ? 0.2995 0.4397 0.2474 0.0410  0.0153  0.0504  687  ARG A NE  
5060  C CZ  . ARG A 689  ? 0.2974 0.4368 0.2439 0.0419  0.0167  0.0461  687  ARG A CZ  
5061  N NH1 . ARG A 689  ? 0.3099 0.4596 0.2520 0.0443  0.0176  0.0428  687  ARG A NH1 
5062  N NH2 . ARG A 689  ? 0.2833 0.4118 0.2332 0.0405  0.0171  0.0450  687  ARG A NH2 
5063  N N   . ARG A 690  ? 0.2180 0.3342 0.1674 0.0396  0.0078  0.0394  688  ARG A N   
5064  C CA  . ARG A 690  ? 0.2308 0.3390 0.1843 0.0379  0.0063  0.0412  688  ARG A CA  
5065  C C   . ARG A 690  ? 0.2513 0.3607 0.2026 0.0388  0.0045  0.0376  688  ARG A C   
5066  O O   . ARG A 690  ? 0.2430 0.3489 0.1974 0.0376  0.0032  0.0403  688  ARG A O   
5067  C CB  . ARG A 690  ? 0.2259 0.3212 0.1824 0.0365  0.0066  0.0379  688  ARG A CB  
5068  C CG  . ARG A 690  ? 0.2600 0.3522 0.2198 0.0352  0.0080  0.0417  688  ARG A CG  
5069  C CD  . ARG A 690  ? 0.2724 0.3638 0.2376 0.0335  0.0074  0.0494  688  ARG A CD  
5070  N NE  . ARG A 690  ? 0.2779 0.3609 0.2467 0.0323  0.0059  0.0487  688  ARG A NE  
5071  C CZ  . ARG A 690  ? 0.3506 0.4358 0.3208 0.0322  0.0044  0.0515  688  ARG A CZ  
5072  N NH1 . ARG A 690  ? 0.3038 0.3994 0.2722 0.0331  0.0040  0.0556  688  ARG A NH1 
5073  N NH2 . ARG A 690  ? 0.2786 0.3560 0.2523 0.0312  0.0031  0.0501  688  ARG A NH2 
5074  N N   . THR A 691  ? 0.2145 0.3286 0.1609 0.0407  0.0044  0.0314  689  THR A N   
5075  C CA  . THR A 691  ? 0.2195 0.3321 0.1648 0.0413  0.0025  0.0268  689  THR A CA  
5076  C C   . THR A 691  ? 0.2701 0.3942 0.2106 0.0435  0.0017  0.0248  689  THR A C   
5077  O O   . THR A 691  ? 0.2854 0.4118 0.2259 0.0436  0.0001  0.0258  689  THR A O   
5078  C CB  . THR A 691  ? 0.2205 0.3235 0.1659 0.0413  0.0024  0.0191  689  THR A CB  
5079  O OG1 . THR A 691  ? 0.2362 0.3423 0.1788 0.0428  0.0034  0.0147  689  THR A OG1 
5080  C CG2 . THR A 691  ? 0.2520 0.3434 0.2021 0.0390  0.0028  0.0207  689  THR A CG2 
5081  N N   . LEU A 692  ? 0.2318 0.3635 0.1685 0.0455  0.0026  0.0216  690  LEU A N   
5082  C CA  . LEU A 692  ? 0.2600 0.4008 0.1922 0.0478  0.0015  0.0166  690  LEU A CA  
5083  C C   . LEU A 692  ? 0.2692 0.4227 0.1993 0.0485  0.0010  0.0224  690  LEU A C   
5084  O O   . LEU A 692  ? 0.2878 0.4484 0.2178 0.0483  0.0023  0.0287  690  LEU A O   
5085  C CB  . LEU A 692  ? 0.2564 0.4010 0.1856 0.0499  0.0024  0.0103  690  LEU A CB  
5086  C CG  . LEU A 692  ? 0.2781 0.4110 0.2092 0.0495  0.0023  0.0036  690  LEU A CG  
5087  C CD1 . LEU A 692  ? 0.3054 0.4433 0.2338 0.0520  0.0026  -0.0035 690  LEU A CD1 
5088  C CD2 . LEU A 692  ? 0.2785 0.4034 0.2113 0.0488  0.0002  0.0000  690  LEU A CD2 
5089  N N   . GLY A 693  ? 0.2667 0.4232 0.1954 0.0492  -0.0009 0.0204  691  GLY A N   
5090  C CA  . GLY A 693  ? 0.2917 0.4605 0.2182 0.0500  -0.0017 0.0253  691  GLY A CA  
5091  C C   . GLY A 693  ? 0.3219 0.4989 0.2437 0.0525  -0.0032 0.0184  691  GLY A C   
5092  O O   . GLY A 693  ? 0.3180 0.4911 0.2387 0.0537  -0.0036 0.0098  691  GLY A O   
5093  N N   . PRO A 694  ? 0.3147 0.5032 0.2341 0.0533  -0.0042 0.0221  692  PRO A N   
5094  C CA  . PRO A 694  ? 0.3318 0.5303 0.2465 0.0559  -0.0056 0.0157  692  PRO A CA  
5095  C C   . PRO A 694  ? 0.3396 0.5295 0.2551 0.0562  -0.0077 0.0077  692  PRO A C   
5096  O O   . PRO A 694  ? 0.4130 0.6073 0.3255 0.0585  -0.0086 -0.0004 692  PRO A O   
5097  C CB  . PRO A 694  ? 0.4086 0.6194 0.3216 0.0561  -0.0064 0.0230  692  PRO A CB  
5098  C CG  . PRO A 694  ? 0.3552 0.5662 0.2713 0.0541  -0.0047 0.0331  692  PRO A CG  
5099  C CD  . PRO A 694  ? 0.3278 0.5221 0.2488 0.0519  -0.0039 0.0326  692  PRO A CD  
5100  N N   . GLY A 695  ? 0.3079 0.4859 0.2278 0.0540  -0.0085 0.0097  693  GLY A N   
5101  C CA  . GLY A 695  ? 0.3618 0.5319 0.2828 0.0540  -0.0104 0.0030  693  GLY A CA  
5102  C C   . GLY A 695  ? 0.3458 0.5051 0.2686 0.0538  -0.0101 -0.0041 693  GLY A C   
5103  O O   . GLY A 695  ? 0.3580 0.5110 0.2821 0.0538  -0.0118 -0.0100 693  GLY A O   
5104  N N   . HIS A 696  ? 0.3345 0.4917 0.2577 0.0536  -0.0080 -0.0036 694  HIS A N   
5105  C CA  . HIS A 696  ? 0.2924 0.4398 0.2174 0.0535  -0.0076 -0.0100 694  HIS A CA  
5106  C C   . HIS A 696  ? 0.3447 0.5006 0.2661 0.0564  -0.0076 -0.0167 694  HIS A C   
5107  O O   . HIS A 696  ? 0.3547 0.5141 0.2750 0.0571  -0.0058 -0.0161 694  HIS A O   
5108  C CB  . HIS A 696  ? 0.3294 0.4681 0.2576 0.0514  -0.0055 -0.0055 694  HIS A CB  
5109  C CG  . HIS A 696  ? 0.2590 0.3922 0.1906 0.0490  -0.0055 0.0019  694  HIS A CG  
5110  N ND1 . HIS A 696  ? 0.2890 0.4254 0.2214 0.0480  -0.0041 0.0101  694  HIS A ND1 
5111  C CD2 . HIS A 696  ? 0.2748 0.3999 0.2094 0.0474  -0.0068 0.0022  694  HIS A CD2 
5112  C CE1 . HIS A 696  ? 0.2685 0.3986 0.2047 0.0459  -0.0047 0.0148  694  HIS A CE1 
5113  N NE2 . HIS A 696  ? 0.2984 0.4219 0.2358 0.0456  -0.0062 0.0101  694  HIS A NE2 
5114  N N   . GLY A 697  ? 0.3272 0.4870 0.2471 0.0581  -0.0098 -0.0232 695  GLY A N   
5115  C CA  . GLY A 697  ? 0.3425 0.5116 0.2593 0.0612  -0.0103 -0.0303 695  GLY A CA  
5116  C C   . GLY A 697  ? 0.2714 0.4322 0.1906 0.0615  -0.0102 -0.0369 695  GLY A C   
5117  O O   . GLY A 697  ? 0.2979 0.4460 0.2211 0.0598  -0.0108 -0.0386 695  GLY A O   
5118  N N   . PRO A 698  ? 0.3130 0.4811 0.2301 0.0638  -0.0093 -0.0407 696  PRO A N   
5119  C CA  . PRO A 698  ? 0.3218 0.4824 0.2417 0.0643  -0.0093 -0.0471 696  PRO A CA  
5120  C C   . PRO A 698  ? 0.2849 0.4416 0.2070 0.0654  -0.0124 -0.0560 696  PRO A C   
5121  O O   . PRO A 698  ? 0.3048 0.4679 0.2251 0.0666  -0.0144 -0.0588 696  PRO A O   
5122  C CB  . PRO A 698  ? 0.3396 0.5117 0.2564 0.0670  -0.0079 -0.0490 696  PRO A CB  
5123  C CG  . PRO A 698  ? 0.4006 0.5875 0.3126 0.0687  -0.0083 -0.0476 696  PRO A CG  
5124  C CD  . PRO A 698  ? 0.3972 0.5813 0.3095 0.0662  -0.0084 -0.0394 696  PRO A CD  
5125  N N   . LEU A 699  ? 0.2799 0.4257 0.2062 0.0646  -0.0128 -0.0601 697  LEU A N   
5126  C CA  . LEU A 699  ? 0.2720 0.4137 0.2014 0.0656  -0.0158 -0.0688 697  LEU A CA  
5127  C C   . LEU A 699  ? 0.3025 0.4556 0.2298 0.0694  -0.0172 -0.0767 697  LEU A C   
5128  O O   . LEU A 699  ? 0.3039 0.4602 0.2315 0.0709  -0.0199 -0.0827 697  LEU A O   
5129  C CB  . LEU A 699  ? 0.2490 0.3773 0.1838 0.0640  -0.0159 -0.0708 697  LEU A CB  
5130  C CG  . LEU A 699  ? 0.3062 0.4223 0.2439 0.0603  -0.0151 -0.0647 697  LEU A CG  
5131  C CD1 . LEU A 699  ? 0.2769 0.3821 0.2195 0.0592  -0.0153 -0.0677 697  LEU A CD1 
5132  C CD2 . LEU A 699  ? 0.3221 0.4360 0.2608 0.0593  -0.0172 -0.0647 697  LEU A CD2 
5133  N N   . GLY A 700  ? 0.2821 0.4418 0.2073 0.0711  -0.0153 -0.0771 698  GLY A N   
5134  C CA  . GLY A 700  ? 0.2637 0.4332 0.1880 0.0749  -0.0165 -0.0856 698  GLY A CA  
5135  C C   . GLY A 700  ? 0.2470 0.4111 0.1745 0.0754  -0.0156 -0.0887 698  GLY A C   
5136  O O   . GLY A 700  ? 0.2738 0.4299 0.2026 0.0730  -0.0134 -0.0829 698  GLY A O   
5137  N N   . PRO A 701  ? 0.2808 0.4489 0.2099 0.0784  -0.0175 -0.0982 699  PRO A N   
5138  C CA  . PRO A 701  ? 0.2693 0.4328 0.2019 0.0791  -0.0168 -0.1015 699  PRO A CA  
5139  C C   . PRO A 701  ? 0.2658 0.4124 0.2041 0.0759  -0.0172 -0.0994 699  PRO A C   
5140  O O   . PRO A 701  ? 0.2710 0.4096 0.2132 0.0747  -0.0197 -0.1020 699  PRO A O   
5141  C CB  . PRO A 701  ? 0.2930 0.4626 0.2278 0.0828  -0.0198 -0.1128 699  PRO A CB  
5142  C CG  . PRO A 701  ? 0.2787 0.4608 0.2102 0.0840  -0.0205 -0.1122 699  PRO A CG  
5143  C CD  . PRO A 701  ? 0.2490 0.4274 0.1768 0.0817  -0.0202 -0.1063 699  PRO A CD  
5144  N N   . ILE A 702  ? 0.2612 0.4029 0.2001 0.0743  -0.0145 -0.0943 700  ILE A N   
5145  C CA  A ILE A 702  ? 0.2549 0.3816 0.1988 0.0713  -0.0146 -0.0919 700  ILE A CA  
5146  C CA  B ILE A 702  ? 0.2548 0.3815 0.1986 0.0713  -0.0145 -0.0917 700  ILE A CA  
5147  C C   . ILE A 702  ? 0.2410 0.3645 0.1889 0.0726  -0.0148 -0.0969 700  ILE A C   
5148  O O   . ILE A 702  ? 0.2465 0.3774 0.1922 0.0744  -0.0129 -0.0970 700  ILE A O   
5149  C CB  A ILE A 702  ? 0.2314 0.3533 0.1734 0.0680  -0.0116 -0.0816 700  ILE A CB  
5150  C CB  B ILE A 702  ? 0.2316 0.3541 0.1733 0.0681  -0.0114 -0.0814 700  ILE A CB  
5151  C CG1 A ILE A 702  ? 0.2454 0.3678 0.1852 0.0664  -0.0121 -0.0774 700  ILE A CG1 
5152  C CG1 B ILE A 702  ? 0.2501 0.3755 0.1885 0.0668  -0.0113 -0.0763 700  ILE A CG1 
5153  C CG2 A ILE A 702  ? 0.2399 0.3478 0.1868 0.0652  -0.0113 -0.0795 700  ILE A CG2 
5154  C CG2 B ILE A 702  ? 0.2399 0.3478 0.1867 0.0651  -0.0113 -0.0792 700  ILE A CG2 
5155  C CD1 A ILE A 702  ? 0.2217 0.3390 0.1605 0.0633  -0.0097 -0.0679 700  ILE A CD1 
5156  C CD1 B ILE A 702  ? 0.2334 0.3510 0.1751 0.0654  -0.0139 -0.0784 700  ILE A CD1 
5157  N N   . VAL A 703  ? 0.2310 0.3441 0.1852 0.0717  -0.0172 -0.1010 701  VAL A N   
5158  C CA  . VAL A 703  ? 0.2520 0.3602 0.2113 0.0726  -0.0179 -0.1054 701  VAL A CA  
5159  C C   . VAL A 703  ? 0.2421 0.3398 0.2030 0.0691  -0.0158 -0.0982 701  VAL A C   
5160  O O   . VAL A 703  ? 0.2432 0.3317 0.2061 0.0661  -0.0162 -0.0943 701  VAL A O   
5161  C CB  . VAL A 703  ? 0.2443 0.3471 0.2103 0.0733  -0.0221 -0.1135 701  VAL A CB  
5162  C CG1 . VAL A 703  ? 0.2645 0.3601 0.2368 0.0735  -0.0230 -0.1168 701  VAL A CG1 
5163  C CG2 . VAL A 703  ? 0.2748 0.3891 0.2392 0.0772  -0.0242 -0.1216 701  VAL A CG2 
5164  N N   . CYS A 704  ? 0.2214 0.3211 0.1813 0.0697  -0.0134 -0.0962 702  CYS A N   
5165  C CA  . CYS A 704  ? 0.2396 0.3302 0.2008 0.0667  -0.0113 -0.0896 702  CYS A CA  
5166  C C   . CYS A 704  ? 0.2712 0.3560 0.2385 0.0674  -0.0127 -0.0943 702  CYS A C   
5167  O O   . CYS A 704  ? 0.2387 0.3299 0.2060 0.0702  -0.0123 -0.0984 702  CYS A O   
5168  C CB  . CYS A 704  ? 0.2294 0.3265 0.1854 0.0666  -0.0077 -0.0831 702  CYS A CB  
5169  S SG  . CYS A 704  ? 0.2410 0.3452 0.1907 0.0657  -0.0063 -0.0769 702  CYS A SG  
5170  N N   . ILE A 705  ? 0.2284 0.3015 0.2009 0.0649  -0.0142 -0.0936 703  ILE A N   
5171  C CA  . ILE A 705  ? 0.2371 0.3034 0.2162 0.0651  -0.0158 -0.0973 703  ILE A CA  
5172  C C   . ILE A 705  ? 0.2305 0.2884 0.2103 0.0618  -0.0136 -0.0901 703  ILE A C   
5173  O O   . ILE A 705  ? 0.2377 0.2897 0.2170 0.0587  -0.0130 -0.0846 703  ILE A O   
5174  C CB  . ILE A 705  ? 0.2514 0.3116 0.2368 0.0648  -0.0198 -0.1026 703  ILE A CB  
5175  C CG1 . ILE A 705  ? 0.2606 0.3297 0.2457 0.0683  -0.0221 -0.1107 703  ILE A CG1 
5176  C CG2 . ILE A 705  ? 0.2595 0.3113 0.2525 0.0642  -0.0215 -0.1048 703  ILE A CG2 
5177  C CD1 . ILE A 705  ? 0.2805 0.3446 0.2710 0.0679  -0.0260 -0.1151 703  ILE A CD1 
5178  N N   . SER A 706  ? 0.2462 0.3042 0.2274 0.0626  -0.0124 -0.0902 704  SER A N   
5179  C CA  . SER A 706  ? 0.2332 0.2853 0.2139 0.0599  -0.0100 -0.0831 704  SER A CA  
5180  C C   . SER A 706  ? 0.2462 0.2906 0.2335 0.0594  -0.0113 -0.0849 704  SER A C   
5181  O O   . SER A 706  ? 0.2454 0.2909 0.2371 0.0618  -0.0137 -0.0918 704  SER A O   
5182  C CB  . SER A 706  ? 0.2380 0.2983 0.2131 0.0609  -0.0066 -0.0795 704  SER A CB  
5183  O OG  . SER A 706  ? 0.2424 0.3106 0.2178 0.0645  -0.0069 -0.0853 704  SER A OG  
5184  N N   . PRO A 707  ? 0.2503 0.2871 0.2386 0.0563  -0.0100 -0.0790 705  PRO A N   
5185  C CA  . PRO A 707  ? 0.2670 0.2963 0.2617 0.0555  -0.0113 -0.0797 705  PRO A CA  
5186  C C   . PRO A 707  ? 0.2220 0.2545 0.2162 0.0569  -0.0095 -0.0796 705  PRO A C   
5187  O O   . PRO A 707  ? 0.2536 0.2932 0.2423 0.0580  -0.0068 -0.0773 705  PRO A O   
5188  C CB  . PRO A 707  ? 0.2526 0.2736 0.2473 0.0514  -0.0104 -0.0727 705  PRO A CB  
5189  C CG  . PRO A 707  ? 0.2330 0.2586 0.2206 0.0507  -0.0072 -0.0674 705  PRO A CG  
5190  C CD  . PRO A 707  ? 0.2361 0.2708 0.2201 0.0534  -0.0075 -0.0712 705  PRO A CD  
5191  N N   . TRP A 708  ? 0.2288 0.2559 0.2291 0.0570  -0.0111 -0.0817 706  TRP A N   
5192  C CA  . TRP A 708  ? 0.2361 0.2661 0.2366 0.0585  -0.0095 -0.0818 706  TRP A CA  
5193  C C   . TRP A 708  ? 0.2356 0.2626 0.2331 0.0558  -0.0065 -0.0739 706  TRP A C   
5194  O O   . TRP A 708  ? 0.2769 0.3085 0.2722 0.0569  -0.0043 -0.0726 706  TRP A O   
5195  C CB  . TRP A 708  ? 0.2311 0.2567 0.2397 0.0596  -0.0124 -0.0867 706  TRP A CB  
5196  C CG  . TRP A 708  ? 0.2571 0.2723 0.2701 0.0561  -0.0132 -0.0822 706  TRP A CG  
5197  C CD1 . TRP A 708  ? 0.2511 0.2592 0.2690 0.0541  -0.0159 -0.0823 706  TRP A CD1 
5198  C CD2 . TRP A 708  ? 0.2476 0.2590 0.2605 0.0542  -0.0112 -0.0766 706  TRP A CD2 
5199  N NE1 . TRP A 708  ? 0.2537 0.2542 0.2742 0.0510  -0.0156 -0.0769 706  TRP A NE1 
5200  C CE2 . TRP A 708  ? 0.2336 0.2360 0.2511 0.0510  -0.0128 -0.0736 706  TRP A CE2 
5201  C CE3 . TRP A 708  ? 0.2441 0.2593 0.2537 0.0548  -0.0083 -0.0739 706  TRP A CE3 
5202  C CZ2 . TRP A 708  ? 0.2258 0.2230 0.2443 0.0486  -0.0116 -0.0681 706  TRP A CZ2 
5203  C CZ3 . TRP A 708  ? 0.2566 0.2661 0.2674 0.0523  -0.0072 -0.0685 706  TRP A CZ3 
5204  C CH2 . TRP A 708  ? 0.2629 0.2635 0.2779 0.0493  -0.0089 -0.0658 706  TRP A CH2 
5205  N N   . ASN A 709  ? 0.2279 0.2478 0.2255 0.0523  -0.0063 -0.0688 707  ASN A N   
5206  C CA  . ASN A 709  ? 0.2431 0.2583 0.2403 0.0498  -0.0044 -0.0626 707  ASN A CA  
5207  C C   . ASN A 709  ? 0.2650 0.2848 0.2558 0.0492  -0.0010 -0.0573 707  ASN A C   
5208  O O   . ASN A 709  ? 0.2563 0.2744 0.2466 0.0480  0.0009  -0.0531 707  ASN A O   
5209  C CB  . ASN A 709  ? 0.2491 0.2553 0.2494 0.0464  -0.0056 -0.0594 707  ASN A CB  
5210  C CG  . ASN A 709  ? 0.2652 0.2713 0.2618 0.0447  -0.0050 -0.0565 707  ASN A CG  
5211  O OD1 . ASN A 709  ? 0.2802 0.2891 0.2762 0.0459  -0.0064 -0.0599 707  ASN A OD1 
5212  N ND2 . ASN A 709  ? 0.2709 0.2740 0.2651 0.0420  -0.0030 -0.0504 707  ASN A ND2 
5213  N N   . PHE A 710  ? 0.2477 0.2730 0.2339 0.0499  -0.0002 -0.0571 708  PHE A N   
5214  C CA  . PHE A 710  ? 0.2548 0.2861 0.2354 0.0498  0.0027  -0.0526 708  PHE A CA  
5215  C C   . PHE A 710  ? 0.2596 0.3011 0.2377 0.0533  0.0027  -0.0571 708  PHE A C   
5216  O O   . PHE A 710  ? 0.2617 0.3079 0.2364 0.0538  0.0027  -0.0573 708  PHE A O   
5217  C CB  . PHE A 710  ? 0.2658 0.2947 0.2435 0.0473  0.0035  -0.0477 708  PHE A CB  
5218  C CG  . PHE A 710  ? 0.3095 0.3293 0.2895 0.0440  0.0035  -0.0436 708  PHE A CG  
5219  C CD1 . PHE A 710  ? 0.3060 0.3223 0.2879 0.0430  0.0044  -0.0412 708  PHE A CD1 
5220  C CD2 . PHE A 710  ? 0.3305 0.3458 0.3108 0.0420  0.0026  -0.0421 708  PHE A CD2 
5221  C CE1 . PHE A 710  ? 0.3085 0.3173 0.2922 0.0400  0.0045  -0.0375 708  PHE A CE1 
5222  C CE2 . PHE A 710  ? 0.3105 0.3184 0.2927 0.0390  0.0027  -0.0385 708  PHE A CE2 
5223  C CZ  . PHE A 710  ? 0.3520 0.3569 0.3359 0.0380  0.0036  -0.0362 708  PHE A CZ  
5224  N N   . PRO A 711  ? 0.2397 0.2854 0.2194 0.0558  0.0027  -0.0610 709  PRO A N   
5225  C CA  . PRO A 711  ? 0.2421 0.2971 0.2207 0.0595  0.0019  -0.0672 709  PRO A CA  
5226  C C   . PRO A 711  ? 0.2516 0.3173 0.2241 0.0607  0.0043  -0.0647 709  PRO A C   
5227  O O   . PRO A 711  ? 0.2482 0.3226 0.2189 0.0636  0.0037  -0.0695 709  PRO A O   
5228  C CB  . PRO A 711  ? 0.2538 0.3093 0.2365 0.0615  0.0013  -0.0714 709  PRO A CB  
5229  C CG  . PRO A 711  ? 0.2503 0.3015 0.2331 0.0593  0.0035  -0.0652 709  PRO A CG  
5230  C CD  . PRO A 711  ? 0.2431 0.2852 0.2260 0.0555  0.0033  -0.0601 709  PRO A CD  
5231  N N   . LEU A 712  ? 0.2494 0.3151 0.2190 0.0587  0.0069  -0.0575 710  LEU A N   
5232  C CA  . LEU A 712  ? 0.2223 0.2977 0.1866 0.0593  0.0090  -0.0539 710  LEU A CA  
5233  C C   . LEU A 712  ? 0.2282 0.3006 0.1900 0.0567  0.0094  -0.0484 710  LEU A C   
5234  O O   . LEU A 712  ? 0.2244 0.3038 0.1828 0.0576  0.0095  -0.0482 710  LEU A O   
5235  C CB  . LEU A 712  ? 0.2200 0.2996 0.1832 0.0594  0.0117  -0.0497 710  LEU A CB  
5236  C CG  . LEU A 712  ? 0.2664 0.3567 0.2246 0.0600  0.0139  -0.0453 710  LEU A CG  
5237  C CD1 . LEU A 712  ? 0.2340 0.3359 0.1899 0.0636  0.0132  -0.0511 710  LEU A CD1 
5238  C CD2 . LEU A 712  ? 0.2829 0.3762 0.2409 0.0594  0.0164  -0.0402 710  LEU A CD2 
5239  N N   . ALA A 713  ? 0.2451 0.3076 0.2089 0.0536  0.0095  -0.0444 711  ALA A N   
5240  C CA  . ALA A 713  ? 0.2246 0.2847 0.1862 0.0512  0.0101  -0.0388 711  ALA A CA  
5241  C C   . ALA A 713  ? 0.2331 0.2927 0.1943 0.0514  0.0081  -0.0417 711  ALA A C   
5242  O O   . ALA A 713  ? 0.2414 0.3066 0.1992 0.0516  0.0085  -0.0397 711  ALA A O   
5243  C CB  . ALA A 713  ? 0.2247 0.2748 0.1888 0.0480  0.0106  -0.0345 711  ALA A CB  
5244  N N   . ILE A 714  ? 0.2222 0.2749 0.1869 0.0511  0.0058  -0.0461 712  ILE A N   
5245  C CA  . ILE A 714  ? 0.2226 0.2744 0.1873 0.0510  0.0038  -0.0487 712  ILE A CA  
5246  C C   . ILE A 714  ? 0.2297 0.2915 0.1923 0.0543  0.0029  -0.0538 712  ILE A C   
5247  O O   . ILE A 714  ? 0.2319 0.2975 0.1918 0.0546  0.0023  -0.0539 712  ILE A O   
5248  C CB  . ILE A 714  ? 0.2384 0.2807 0.2082 0.0498  0.0014  -0.0518 712  ILE A CB  
5249  C CG1 . ILE A 714  ? 0.2759 0.3097 0.2469 0.0463  0.0024  -0.0460 712  ILE A CG1 
5250  C CG2 . ILE A 714  ? 0.2488 0.2912 0.2192 0.0504  -0.0011 -0.0560 712  ILE A CG2 
5251  C CD1 . ILE A 714  ? 0.3633 0.3887 0.3383 0.0445  0.0003  -0.0473 712  ILE A CD1 
5252  N N   . PHE A 715  ? 0.2330 0.2993 0.1966 0.0569  0.0027  -0.0584 713  PHE A N   
5253  C CA  . PHE A 715  ? 0.2184 0.2956 0.1796 0.0603  0.0022  -0.0635 713  PHE A CA  
5254  C C   . PHE A 715  ? 0.2607 0.3471 0.2163 0.0605  0.0042  -0.0587 713  PHE A C   
5255  O O   . PHE A 715  ? 0.2304 0.3226 0.1834 0.0616  0.0033  -0.0604 713  PHE A O   
5256  C CB  . PHE A 715  ? 0.2495 0.3307 0.2124 0.0628  0.0026  -0.0675 713  PHE A CB  
5257  C CG  . PHE A 715  ? 0.2473 0.3408 0.2079 0.0666  0.0022  -0.0731 713  PHE A CG  
5258  C CD1 . PHE A 715  ? 0.2601 0.3547 0.2230 0.0687  -0.0008 -0.0810 713  PHE A CD1 
5259  C CD2 . PHE A 715  ? 0.2465 0.3512 0.2027 0.0680  0.0047  -0.0704 713  PHE A CD2 
5260  C CE1 . PHE A 715  ? 0.2685 0.3750 0.2292 0.0724  -0.0012 -0.0867 713  PHE A CE1 
5261  C CE2 . PHE A 715  ? 0.2464 0.3634 0.2001 0.0716  0.0044  -0.0755 713  PHE A CE2 
5262  C CZ  . PHE A 715  ? 0.2892 0.4074 0.2451 0.0739  0.0015  -0.0840 713  PHE A CZ  
5263  N N   . THR A 716  ? 0.2326 0.3206 0.1865 0.0594  0.0069  -0.0524 714  THR A N   
5264  C CA  . THR A 716  ? 0.2331 0.3299 0.1823 0.0594  0.0088  -0.0470 714  THR A CA  
5265  C C   . THR A 716  ? 0.2325 0.3256 0.1806 0.0572  0.0083  -0.0428 714  THR A C   
5266  O O   . THR A 716  ? 0.2277 0.3288 0.1725 0.0580  0.0083  -0.0416 714  THR A O   
5267  C CB  . THR A 716  ? 0.2610 0.3588 0.2100 0.0583  0.0115  -0.0409 714  THR A CB  
5268  O OG1 . THR A 716  ? 0.2492 0.3515 0.1990 0.0607  0.0120  -0.0449 714  THR A OG1 
5269  C CG2 . THR A 716  ? 0.2626 0.3692 0.2077 0.0580  0.0133  -0.0345 714  THR A CG2 
5270  N N   . GLY A 717  ? 0.2150 0.2967 0.1660 0.0544  0.0078  -0.0407 715  GLY A N   
5271  C CA  . GLY A 717  ? 0.2184 0.2962 0.1687 0.0522  0.0074  -0.0367 715  GLY A CA  
5272  C C   . GLY A 717  ? 0.2204 0.3014 0.1696 0.0535  0.0053  -0.0410 715  GLY A C   
5273  O O   . GLY A 717  ? 0.2392 0.3254 0.1856 0.0534  0.0055  -0.0380 715  GLY A O   
5274  N N   . GLN A 718  ? 0.2201 0.2982 0.1719 0.0546  0.0031  -0.0479 716  GLN A N   
5275  C CA  . GLN A 718  ? 0.2130 0.2936 0.1642 0.0558  0.0008  -0.0524 716  GLN A CA  
5276  C C   . GLN A 718  ? 0.2446 0.3386 0.1915 0.0586  0.0012  -0.0538 716  GLN A C   
5277  O O   . GLN A 718  ? 0.2335 0.3319 0.1779 0.0586  0.0006  -0.0526 716  GLN A O   
5278  C CB  . GLN A 718  ? 0.2146 0.2903 0.1702 0.0567  -0.0018 -0.0599 716  GLN A CB  
5279  C CG  . GLN A 718  ? 0.2107 0.2739 0.1708 0.0539  -0.0024 -0.0584 716  GLN A CG  
5280  C CD  . GLN A 718  ? 0.2571 0.3153 0.2221 0.0546  -0.0054 -0.0652 716  GLN A CD  
5281  O OE1 . GLN A 718  ? 0.2578 0.3084 0.2258 0.0525  -0.0069 -0.0650 716  GLN A OE1 
5282  N NE2 . GLN A 718  ? 0.2440 0.3067 0.2103 0.0574  -0.0063 -0.0712 716  GLN A NE2 
5283  N N   . ILE A 719  ? 0.2374 0.3384 0.1834 0.0609  0.0021  -0.0562 717  ILE A N   
5284  C CA  . ILE A 719  ? 0.2263 0.3413 0.1682 0.0638  0.0025  -0.0580 717  ILE A CA  
5285  C C   . ILE A 719  ? 0.2206 0.3419 0.1585 0.0627  0.0046  -0.0498 717  ILE A C   
5286  O O   . ILE A 719  ? 0.2301 0.3603 0.1646 0.0638  0.0042  -0.0496 717  ILE A O   
5287  C CB  . ILE A 719  ? 0.2614 0.3825 0.2036 0.0665  0.0033  -0.0622 717  ILE A CB  
5288  C CG1 . ILE A 719  ? 0.2357 0.3525 0.1822 0.0682  0.0006  -0.0713 717  ILE A CG1 
5289  C CG2 . ILE A 719  ? 0.2998 0.4366 0.2372 0.0691  0.0045  -0.0622 717  ILE A CG2 
5290  C CD1 . ILE A 719  ? 0.3086 0.4269 0.2571 0.0699  0.0013  -0.0744 717  ILE A CD1 
5291  N N   . ALA A 720  ? 0.2310 0.3479 0.1695 0.0604  0.0067  -0.0430 718  ALA A N   
5292  C CA  . ALA A 720  ? 0.2334 0.3559 0.1691 0.0592  0.0085  -0.0349 718  ALA A CA  
5293  C C   . ALA A 720  ? 0.2125 0.3325 0.1477 0.0577  0.0073  -0.0323 718  ALA A C   
5294  O O   . ALA A 720  ? 0.2177 0.3466 0.1498 0.0582  0.0075  -0.0291 718  ALA A O   
5295  C CB  . ALA A 720  ? 0.2344 0.3508 0.1721 0.0568  0.0106  -0.0285 718  ALA A CB  
5296  N N   . ALA A 721  ? 0.2238 0.3320 0.1621 0.0558  0.0059  -0.0335 719  ALA A N   
5297  C CA  . ALA A 721  ? 0.2058 0.3108 0.1441 0.0543  0.0047  -0.0315 719  ALA A CA  
5298  C C   . ALA A 721  ? 0.2132 0.3265 0.1489 0.0566  0.0029  -0.0361 719  ALA A C   
5299  O O   . ALA A 721  ? 0.2162 0.3355 0.1495 0.0565  0.0028  -0.0324 719  ALA A O   
5300  C CB  . ALA A 721  ? 0.2215 0.3133 0.1638 0.0522  0.0035  -0.0332 719  ALA A CB  
5301  N N   . ALA A 722  ? 0.2142 0.3287 0.1506 0.0588  0.0013  -0.0442 720  ALA A N   
5302  C CA  . ALA A 722  ? 0.2074 0.3297 0.1417 0.0611  -0.0006 -0.0494 720  ALA A CA  
5303  C C   . ALA A 722  ? 0.2439 0.3811 0.1734 0.0631  0.0006  -0.0471 720  ALA A C   
5304  O O   . ALA A 722  ? 0.2311 0.3751 0.1580 0.0636  -0.0003 -0.0460 720  ALA A O   
5305  C CB  . ALA A 722  ? 0.2381 0.3586 0.1751 0.0631  -0.0027 -0.0588 720  ALA A CB  
5306  N N   . LEU A 723  ? 0.2226 0.3656 0.1510 0.0642  0.0026  -0.0460 721  LEU A N   
5307  C CA  . LEU A 723  ? 0.2248 0.3828 0.1488 0.0661  0.0039  -0.0435 721  LEU A CA  
5308  C C   . LEU A 723  ? 0.2355 0.3960 0.1578 0.0640  0.0051  -0.0340 721  LEU A C   
5309  O O   . LEU A 723  ? 0.2231 0.3946 0.1418 0.0651  0.0048  -0.0323 721  LEU A O   
5310  C CB  . LEU A 723  ? 0.2492 0.4116 0.1731 0.0672  0.0061  -0.0432 721  LEU A CB  
5311  C CG  . LEU A 723  ? 0.2279 0.3922 0.1529 0.0701  0.0052  -0.0525 721  LEU A CG  
5312  C CD1 . LEU A 723  ? 0.2470 0.4137 0.1724 0.0704  0.0077  -0.0502 721  LEU A CD1 
5313  C CD2 . LEU A 723  ? 0.2511 0.4293 0.1727 0.0736  0.0039  -0.0584 721  LEU A CD2 
5314  N N   . VAL A 724  ? 0.2447 0.3955 0.1696 0.0610  0.0063  -0.0276 722  VAL A N   
5315  C CA  . VAL A 724  ? 0.2321 0.3856 0.1562 0.0591  0.0073  -0.0185 722  VAL A CA  
5316  C C   . VAL A 724  ? 0.2169 0.3687 0.1408 0.0583  0.0053  -0.0180 722  VAL A C   
5317  O O   . VAL A 724  ? 0.2456 0.4041 0.1678 0.0578  0.0055  -0.0120 722  VAL A O   
5318  C CB  . VAL A 724  ? 0.2185 0.3629 0.1460 0.0563  0.0089  -0.0122 722  VAL A CB  
5319  C CG1 . VAL A 724  ? 0.2506 0.3802 0.1817 0.0538  0.0078  -0.0126 722  VAL A CG1 
5320  C CG2 . VAL A 724  ? 0.2384 0.3897 0.1651 0.0551  0.0104  -0.0028 722  VAL A CG2 
5321  N N   . ALA A 725  ? 0.2291 0.3723 0.1548 0.0582  0.0033  -0.0241 723  ALA A N   
5322  C CA  . ALA A 725  ? 0.2547 0.3973 0.1801 0.0579  0.0013  -0.0248 723  ALA A CA  
5323  C C   . ALA A 725  ? 0.2578 0.4137 0.1792 0.0608  0.0000  -0.0288 723  ALA A C   
5324  O O   . ALA A 725  ? 0.2739 0.4305 0.1948 0.0608  -0.0018 -0.0299 723  ALA A O   
5325  C CB  . ALA A 725  ? 0.2386 0.3686 0.1676 0.0568  -0.0005 -0.0301 723  ALA A CB  
5326  N N   . GLY A 726  ? 0.2405 0.4070 0.1591 0.0633  0.0010  -0.0312 724  GLY A N   
5327  C CA  . GLY A 726  ? 0.2482 0.4289 0.1628 0.0662  0.0000  -0.0349 724  GLY A CA  
5328  C C   . GLY A 726  ? 0.2510 0.4325 0.1659 0.0688  -0.0022 -0.0459 724  GLY A C   
5329  O O   . GLY A 726  ? 0.2701 0.4624 0.1819 0.0712  -0.0036 -0.0498 724  GLY A O   
5330  N N   . ASN A 727  ? 0.2447 0.4154 0.1634 0.0685  -0.0026 -0.0509 725  ASN A N   
5331  C CA  . ASN A 727  ? 0.2552 0.4251 0.1755 0.0708  -0.0050 -0.0613 725  ASN A CA  
5332  C C   . ASN A 727  ? 0.2631 0.4391 0.1830 0.0734  -0.0040 -0.0660 725  ASN A C   
5333  O O   . ASN A 727  ? 0.2660 0.4379 0.1873 0.0723  -0.0019 -0.0625 725  ASN A O   
5334  C CB  . ASN A 727  ? 0.2559 0.4095 0.1816 0.0687  -0.0064 -0.0636 725  ASN A CB  
5335  C CG  . ASN A 727  ? 0.2545 0.4009 0.1811 0.0659  -0.0071 -0.0587 725  ASN A CG  
5336  O OD1 . ASN A 727  ? 0.2751 0.4238 0.2011 0.0664  -0.0092 -0.0613 725  ASN A OD1 
5337  N ND2 . ASN A 727  ? 0.2355 0.3732 0.1638 0.0629  -0.0054 -0.0517 725  ASN A ND2 
5338  N N   . PRO A 728  ? 0.2473 0.4330 0.1659 0.0769  -0.0056 -0.0742 726  PRO A N   
5339  C CA  . PRO A 728  ? 0.2603 0.4497 0.1800 0.0795  -0.0051 -0.0803 726  PRO A CA  
5340  C C   . PRO A 728  ? 0.2617 0.4363 0.1876 0.0786  -0.0067 -0.0852 726  PRO A C   
5341  O O   . PRO A 728  ? 0.2758 0.4406 0.2048 0.0771  -0.0089 -0.0870 726  PRO A O   
5342  C CB  . PRO A 728  ? 0.2511 0.4529 0.1700 0.0828  -0.0072 -0.0873 726  PRO A CB  
5343  C CG  . PRO A 728  ? 0.2656 0.4648 0.1841 0.0822  -0.0097 -0.0890 726  PRO A CG  
5344  C CD  . PRO A 728  ? 0.2561 0.4487 0.1730 0.0787  -0.0082 -0.0793 726  PRO A CD  
5345  N N   . VAL A 729  ? 0.2606 0.4338 0.1885 0.0794  -0.0055 -0.0870 727  VAL A N   
5346  C CA  . VAL A 729  ? 0.2462 0.4051 0.1801 0.0779  -0.0064 -0.0893 727  VAL A CA  
5347  C C   . VAL A 729  ? 0.2508 0.4123 0.1879 0.0812  -0.0080 -0.0991 727  VAL A C   
5348  O O   . VAL A 729  ? 0.2572 0.4301 0.1918 0.0840  -0.0067 -0.1014 727  VAL A O   
5349  C CB  . VAL A 729  ? 0.2315 0.3835 0.1659 0.0751  -0.0034 -0.0810 727  VAL A CB  
5350  C CG1 . VAL A 729  ? 0.2534 0.3929 0.1937 0.0742  -0.0042 -0.0840 727  VAL A CG1 
5351  C CG2 . VAL A 729  ? 0.2596 0.4060 0.1927 0.0716  -0.0026 -0.0724 727  VAL A CG2 
5352  N N   . LEU A 730  ? 0.2439 0.3949 0.1868 0.0809  -0.0108 -0.1047 728  LEU A N   
5353  C CA  . LEU A 730  ? 0.2489 0.3981 0.1969 0.0832  -0.0126 -0.1132 728  LEU A CA  
5354  C C   . LEU A 730  ? 0.2332 0.3687 0.1856 0.0803  -0.0117 -0.1090 728  LEU A C   
5355  O O   . LEU A 730  ? 0.2496 0.3733 0.2052 0.0773  -0.0128 -0.1064 728  LEU A O   
5356  C CB  . LEU A 730  ? 0.2793 0.4258 0.2319 0.0845  -0.0168 -0.1217 728  LEU A CB  
5357  C CG  . LEU A 730  ? 0.2452 0.4030 0.1960 0.0861  -0.0185 -0.1242 728  LEU A CG  
5358  C CD1 . LEU A 730  ? 0.2585 0.4306 0.2065 0.0881  -0.0167 -0.1233 728  LEU A CD1 
5359  C CD2 . LEU A 730  ? 0.2594 0.4179 0.2049 0.0845  -0.0181 -0.1196 728  LEU A CD2 
5360  N N   . ALA A 731  ? 0.2428 0.3804 0.1954 0.0812  -0.0097 -0.1082 729  ALA A N   
5361  C CA  . ALA A 731  ? 0.2459 0.3721 0.2019 0.0785  -0.0084 -0.1035 729  ALA A CA  
5362  C C   . ALA A 731  ? 0.2500 0.3707 0.2130 0.0800  -0.0108 -0.1112 729  ALA A C   
5363  O O   . ALA A 731  ? 0.2788 0.4071 0.2424 0.0833  -0.0109 -0.1168 729  ALA A O   
5364  C CB  . ALA A 731  ? 0.2637 0.3957 0.2158 0.0782  -0.0046 -0.0971 729  ALA A CB  
5365  N N   . LYS A 732  ? 0.2395 0.3471 0.2081 0.0776  -0.0129 -0.1113 730  LYS A N   
5366  C CA  . LYS A 732  ? 0.2517 0.3525 0.2280 0.0786  -0.0156 -0.1177 730  LYS A CA  
5367  C C   . LYS A 732  ? 0.2559 0.3460 0.2351 0.0755  -0.0142 -0.1117 730  LYS A C   
5368  O O   . LYS A 732  ? 0.2504 0.3299 0.2321 0.0721  -0.0149 -0.1077 730  LYS A O   
5369  C CB  . LYS A 732  ? 0.2925 0.3874 0.2738 0.0782  -0.0196 -0.1228 730  LYS A CB  
5370  C CG  . LYS A 732  ? 0.2880 0.3830 0.2765 0.0813  -0.0233 -0.1329 730  LYS A CG  
5371  C CD  . LYS A 732  ? 0.2523 0.3393 0.2469 0.0807  -0.0235 -0.1329 730  LYS A CD  
5372  C CE  . LYS A 732  ? 0.2482 0.3209 0.2475 0.0764  -0.0244 -0.1277 730  LYS A CE  
5373  N NZ  . LYS A 732  ? 0.2831 0.3487 0.2884 0.0759  -0.0247 -0.1274 730  LYS A NZ  
5374  N N   . PRO A 733  ? 0.2445 0.3373 0.2234 0.0765  -0.0122 -0.1108 731  PRO A N   
5375  C CA  . PRO A 733  ? 0.2485 0.3314 0.2302 0.0736  -0.0109 -0.1052 731  PRO A CA  
5376  C C   . PRO A 733  ? 0.2152 0.2886 0.2054 0.0735  -0.0141 -0.1100 731  PRO A C   
5377  O O   . PRO A 733  ? 0.2551 0.3309 0.2497 0.0763  -0.0172 -0.1183 731  PRO A O   
5378  C CB  . PRO A 733  ? 0.2573 0.3480 0.2361 0.0754  -0.0080 -0.1040 731  PRO A CB  
5379  C CG  . PRO A 733  ? 0.2485 0.3504 0.2273 0.0799  -0.0094 -0.1128 731  PRO A CG  
5380  C CD  . PRO A 733  ? 0.2496 0.3551 0.2261 0.0804  -0.0111 -0.1153 731  PRO A CD  
5381  N N   . ALA A 734  ? 0.2462 0.3092 0.2393 0.0702  -0.0136 -0.1045 732  ALA A N   
5382  C CA  . ALA A 734  ? 0.2351 0.2889 0.2367 0.0697  -0.0166 -0.1078 732  ALA A CA  
5383  C C   . ALA A 734  ? 0.2533 0.3115 0.2590 0.0733  -0.0177 -0.1146 732  ALA A C   
5384  O O   . ALA A 734  ? 0.2784 0.3440 0.2804 0.0750  -0.0151 -0.1139 732  ALA A O   
5385  C CB  . ALA A 734  ? 0.2549 0.2988 0.2579 0.0659  -0.0153 -0.1002 732  ALA A CB  
5386  N N   . GLU A 735  ? 0.2652 0.3190 0.2790 0.0745  -0.0216 -0.1212 733  GLU A N   
5387  C CA  . GLU A 735  ? 0.2829 0.3407 0.3015 0.0781  -0.0232 -0.1286 733  GLU A CA  
5388  C C   . GLU A 735  ? 0.2917 0.3467 0.3116 0.0774  -0.0212 -0.1248 733  GLU A C   
5389  O O   . GLU A 735  ? 0.2789 0.3403 0.2999 0.0807  -0.0209 -0.1294 733  GLU A O   
5390  C CB  . GLU A 735  ? 0.3070 0.3593 0.3354 0.0791  -0.0282 -0.1360 733  GLU A CB  
5391  C CG  . GLU A 735  ? 0.3220 0.3609 0.3570 0.0752  -0.0301 -0.1316 733  GLU A CG  
5392  C CD  . GLU A 735  ? 0.3535 0.3882 0.3871 0.0724  -0.0310 -0.1285 733  GLU A CD  
5393  O OE1 . GLU A 735  ? 0.3316 0.3724 0.3571 0.0724  -0.0288 -0.1265 733  GLU A OE1 
5394  O OE2 . GLU A 735  ? 0.3345 0.3599 0.3752 0.0702  -0.0340 -0.1280 733  GLU A OE2 
5395  N N   . GLU A 736  ? 0.2772 0.3234 0.2969 0.0734  -0.0197 -0.1166 734  GLU A N   
5396  C CA  . GLU A 736  ? 0.2496 0.2928 0.2709 0.0726  -0.0181 -0.1130 734  GLU A CA  
5397  C C   . GLU A 736  ? 0.2852 0.3370 0.2988 0.0735  -0.0138 -0.1094 734  GLU A C   
5398  O O   . GLU A 736  ? 0.2874 0.3408 0.3024 0.0746  -0.0127 -0.1095 734  GLU A O   
5399  C CB  . GLU A 736  ? 0.2678 0.2995 0.2912 0.0681  -0.0180 -0.1055 734  GLU A CB  
5400  C CG  . GLU A 736  ? 0.3160 0.3386 0.3480 0.0668  -0.0222 -0.1078 734  GLU A CG  
5401  C CD  . GLU A 736  ? 0.3357 0.3560 0.3661 0.0649  -0.0232 -0.1067 734  GLU A CD  
5402  O OE1 . GLU A 736  ? 0.2996 0.3267 0.3229 0.0657  -0.0215 -0.1065 734  GLU A OE1 
5403  O OE2 . GLU A 736  ? 0.3222 0.3340 0.3585 0.0626  -0.0259 -0.1056 734  GLU A OE2 
5404  N N   . THR A 737  ? 0.2682 0.3256 0.2741 0.0729  -0.0115 -0.1059 735  THR A N   
5405  C CA  . THR A 737  ? 0.2806 0.3448 0.2795 0.0727  -0.0074 -0.1004 735  THR A CA  
5406  C C   . THR A 737  ? 0.2550 0.3320 0.2475 0.0754  -0.0061 -0.1027 735  THR A C   
5407  O O   . THR A 737  ? 0.2685 0.3488 0.2548 0.0738  -0.0037 -0.0969 735  THR A O   
5408  C CB  . THR A 737  ? 0.2427 0.2998 0.2385 0.0684  -0.0054 -0.0911 735  THR A CB  
5409  O OG1 . THR A 737  ? 0.2595 0.3138 0.2539 0.0667  -0.0065 -0.0902 735  THR A OG1 
5410  C CG2 . THR A 737  ? 0.2353 0.2815 0.2367 0.0660  -0.0062 -0.0884 735  THR A CG2 
5411  N N   . PRO A 738  ? 0.2577 0.3429 0.2520 0.0794  -0.0076 -0.1111 736  PRO A N   
5412  C CA  . PRO A 738  ? 0.2448 0.3433 0.2329 0.0821  -0.0065 -0.1135 736  PRO A CA  
5413  C C   . PRO A 738  ? 0.2659 0.3746 0.2483 0.0830  -0.0026 -0.1095 736  PRO A C   
5414  O O   . PRO A 738  ? 0.2645 0.3835 0.2408 0.0839  -0.0010 -0.1081 736  PRO A O   
5415  C CB  . PRO A 738  ? 0.3103 0.4137 0.3032 0.0863  -0.0097 -0.1246 736  PRO A CB  
5416  C CG  . PRO A 738  ? 0.2688 0.3658 0.2690 0.0866  -0.0109 -0.1268 736  PRO A CG  
5417  C CD  . PRO A 738  ? 0.2671 0.3504 0.2692 0.0820  -0.0106 -0.1190 736  PRO A CD  
5418  N N   . LEU A 739  ? 0.2419 0.3486 0.2266 0.0828  -0.0012 -0.1074 737  LEU A N   
5419  C CA  . LEU A 739  ? 0.2501 0.3678 0.2303 0.0842  0.0022  -0.1047 737  LEU A CA  
5420  C C   . LEU A 739  ? 0.2290 0.3477 0.2028 0.0811  0.0053  -0.0948 737  LEU A C   
5421  O O   . LEU A 739  ? 0.2576 0.3882 0.2259 0.0823  0.0075  -0.0929 737  LEU A O   
5422  C CB  . LEU A 739  ? 0.2521 0.3671 0.2367 0.0847  0.0028  -0.1051 737  LEU A CB  
5423  C CG  . LEU A 739  ? 0.2631 0.3772 0.2549 0.0879  -0.0004 -0.1149 737  LEU A CG  
5424  C CD1 . LEU A 739  ? 0.2436 0.3539 0.2397 0.0879  0.0003  -0.1139 737  LEU A CD1 
5425  C CD2 . LEU A 739  ? 0.2757 0.4034 0.2661 0.0916  -0.0012 -0.1216 737  LEU A CD2 
5426  N N   . ILE A 740  ? 0.2298 0.3366 0.2047 0.0771  0.0056  -0.0884 738  ILE A N   
5427  C CA  . ILE A 740  ? 0.2389 0.3462 0.2086 0.0743  0.0083  -0.0792 738  ILE A CA  
5428  C C   . ILE A 740  ? 0.2293 0.3413 0.1947 0.0742  0.0079  -0.0789 738  ILE A C   
5429  O O   . ILE A 740  ? 0.2505 0.3694 0.2108 0.0736  0.0101  -0.0733 738  ILE A O   
5430  C CB  . ILE A 740  ? 0.2750 0.3689 0.2472 0.0702  0.0085  -0.0732 738  ILE A CB  
5431  C CG1 . ILE A 740  ? 0.2547 0.3493 0.2224 0.0674  0.0113  -0.0640 738  ILE A CG1 
5432  C CG2 . ILE A 740  ? 0.2473 0.3309 0.2228 0.0687  0.0056  -0.0754 738  ILE A CG2 
5433  C CD1 . ILE A 740  ? 0.2834 0.3875 0.2483 0.0684  0.0142  -0.0605 738  ILE A CD1 
5434  N N   . ALA A 741  ? 0.2405 0.3491 0.2082 0.0750  0.0048  -0.0848 739  ALA A N   
5435  C CA  . ALA A 741  ? 0.2641 0.3779 0.2280 0.0754  0.0041  -0.0855 739  ALA A CA  
5436  C C   . ALA A 741  ? 0.2502 0.3801 0.2097 0.0790  0.0052  -0.0884 739  ALA A C   
5437  O O   . ALA A 741  ? 0.2778 0.4150 0.2320 0.0786  0.0066  -0.0843 739  ALA A O   
5438  C CB  . ALA A 741  ? 0.2786 0.3857 0.2468 0.0758  0.0004  -0.0920 739  ALA A CB  
5439  N N   . ALA A 742  ? 0.2595 0.3954 0.2213 0.0824  0.0046  -0.0955 740  ALA A N   
5440  C CA  . ALA A 742  ? 0.2236 0.3761 0.1813 0.0860  0.0058  -0.0986 740  ALA A CA  
5441  C C   . ALA A 742  ? 0.2534 0.4132 0.2063 0.0848  0.0096  -0.0900 740  ALA A C   
5442  O O   . ALA A 742  ? 0.2694 0.4417 0.2170 0.0860  0.0111  -0.0881 740  ALA A O   
5443  C CB  . ALA A 742  ? 0.2348 0.3911 0.1972 0.0892  0.0041  -0.1070 740  ALA A CB  
5444  N N   . GLU A 743  ? 0.2429 0.3953 0.1978 0.0825  0.0113  -0.0845 741  GLU A N   
5445  C CA  . GLU A 743  ? 0.2636 0.4218 0.2148 0.0811  0.0147  -0.0759 741  GLU A CA  
5446  C C   . GLU A 743  ? 0.2389 0.3956 0.1862 0.0781  0.0155  -0.0681 741  GLU A C   
5447  O O   . GLU A 743  ? 0.2598 0.4270 0.2028 0.0781  0.0176  -0.0629 741  GLU A O   
5448  C CB  . GLU A 743  ? 0.2624 0.4122 0.2173 0.0793  0.0159  -0.0725 741  GLU A CB  
5449  C CG  . GLU A 743  ? 0.2917 0.4453 0.2439 0.0773  0.0192  -0.0633 741  GLU A CG  
5450  C CD  . GLU A 743  ? 0.2665 0.4369 0.2154 0.0801  0.0214  -0.0633 741  GLU A CD  
5451  O OE1 . GLU A 743  ? 0.2755 0.4555 0.2241 0.0839  0.0205  -0.0710 741  GLU A OE1 
5452  O OE2 . GLU A 743  ? 0.3246 0.4991 0.2715 0.0784  0.0239  -0.0552 741  GLU A OE2 
5453  N N   . GLY A 744  ? 0.2500 0.3941 0.1992 0.0755  0.0137  -0.0672 742  GLY A N   
5454  C CA  . GLY A 744  ? 0.2397 0.3823 0.1857 0.0729  0.0142  -0.0607 742  GLY A CA  
5455  C C   . GLY A 744  ? 0.2311 0.3859 0.1728 0.0751  0.0137  -0.0628 742  GLY A C   
5456  O O   . GLY A 744  ? 0.2668 0.4281 0.2046 0.0740  0.0153  -0.0562 742  GLY A O   
5457  N N   . VAL A 745  ? 0.2450 0.4033 0.1875 0.0781  0.0114  -0.0719 743  VAL A N   
5458  C CA  . VAL A 745  ? 0.2566 0.4278 0.1948 0.0805  0.0109  -0.0748 743  VAL A CA  
5459  C C   . VAL A 745  ? 0.2778 0.4651 0.2121 0.0826  0.0135  -0.0725 743  VAL A C   
5460  O O   . VAL A 745  ? 0.2916 0.4893 0.2211 0.0828  0.0145  -0.0686 743  VAL A O   
5461  C CB  . VAL A 745  ? 0.2700 0.4416 0.2108 0.0836  0.0076  -0.0859 743  VAL A CB  
5462  C CG1 . VAL A 745  ? 0.2947 0.4808 0.2322 0.0860  0.0068  -0.0889 743  VAL A CG1 
5463  C CG2 . VAL A 745  ? 0.3100 0.4676 0.2541 0.0813  0.0050  -0.0871 743  VAL A CG2 
5464  N N   . ARG A 746  ? 0.2841 0.4742 0.2203 0.0841  0.0147  -0.0746 744  ARG A N   
5465  C CA  . ARG A 746  ? 0.2643 0.4676 0.1986 0.0848  0.0166  -0.0708 744  ARG A CA  
5466  C C   . ARG A 746  ? 0.2592 0.4653 0.1897 0.0823  0.0197  -0.0599 744  ARG A C   
5467  O O   . ARG A 746  ? 0.2781 0.4958 0.2059 0.0822  0.0205  -0.0552 744  ARG A O   
5468  C CB  . ARG A 746  ? 0.2887 0.4919 0.2268 0.0861  0.0172  -0.0739 744  ARG A CB  
5469  C CG  . ARG A 746  ? 0.2764 0.4939 0.2134 0.0872  0.0186  -0.0714 744  ARG A CG  
5470  C CD  . ARG A 746  ? 0.2908 0.5069 0.2309 0.0876  0.0201  -0.0716 744  ARG A CD  
5471  N NE  . ARG A 746  ? 0.3101 0.5187 0.2497 0.0852  0.0228  -0.0643 744  ARG A NE  
5472  C CZ  . ARG A 746  ? 0.3050 0.5186 0.2416 0.0832  0.0255  -0.0549 744  ARG A CZ  
5473  N NH1 . ARG A 746  ? 0.3604 0.5866 0.2942 0.0833  0.0259  -0.0511 744  ARG A NH1 
5474  N NH2 . ARG A 746  ? 0.3170 0.5218 0.2545 0.0807  0.0273  -0.0486 744  ARG A NH2 
5475  N N   . ILE A 747  ? 0.2413 0.4340 0.1740 0.0790  0.0203  -0.0544 745  ILE A N   
5476  C CA  . ILE A 747  ? 0.2483 0.4407 0.1795 0.0758  0.0223  -0.0435 745  ILE A CA  
5477  C C   . ILE A 747  ? 0.2430 0.4387 0.1709 0.0748  0.0216  -0.0400 745  ILE A C   
5478  O O   . ILE A 747  ? 0.2574 0.4627 0.1823 0.0742  0.0232  -0.0330 745  ILE A O   
5479  C CB  . ILE A 747  ? 0.2516 0.4280 0.1869 0.0723  0.0225  -0.0393 745  ILE A CB  
5480  C CG1 . ILE A 747  ? 0.2606 0.4373 0.1984 0.0732  0.0239  -0.0403 745  ILE A CG1 
5481  C CG2 . ILE A 747  ? 0.2935 0.4669 0.2279 0.0688  0.0236  -0.0290 745  ILE A CG2 
5482  C CD1 . ILE A 747  ? 0.2705 0.4316 0.2128 0.0705  0.0236  -0.0387 745  ILE A CD1 
5483  N N   . LEU A 748  ? 0.2455 0.4332 0.1741 0.0746  0.0190  -0.0445 746  LEU A N   
5484  C CA  . LEU A 748  ? 0.2575 0.4481 0.1832 0.0738  0.0181  -0.0417 746  LEU A CA  
5485  C C   . LEU A 748  ? 0.2651 0.4737 0.1861 0.0768  0.0185  -0.0434 746  LEU A C   
5486  O O   . LEU A 748  ? 0.2633 0.4796 0.1812 0.0759  0.0193  -0.0369 746  LEU A O   
5487  C CB  . LEU A 748  ? 0.2428 0.4223 0.1705 0.0733  0.0152  -0.0473 746  LEU A CB  
5488  C CG  . LEU A 748  ? 0.2658 0.4291 0.1968 0.0695  0.0150  -0.0425 746  LEU A CG  
5489  C CD1 . LEU A 748  ? 0.2819 0.4340 0.2160 0.0694  0.0122  -0.0493 746  LEU A CD1 
5490  C CD2 . LEU A 748  ? 0.3006 0.4645 0.2296 0.0670  0.0155  -0.0342 746  LEU A CD2 
5491  N N   . ARG A 749  ? 0.2498 0.4650 0.1714 0.0801  0.0176  -0.0518 747  ARG A N   
5492  C CA  . ARG A 749  ? 0.2535 0.4833 0.1741 0.0817  0.0168  -0.0526 747  ARG A CA  
5493  C C   . ARG A 749  ? 0.2726 0.5125 0.1922 0.0809  0.0194  -0.0442 747  ARG A C   
5494  O O   . ARG A 749  ? 0.2998 0.5506 0.2175 0.0806  0.0196  -0.0394 747  ARG A O   
5495  C CB  . ARG A 749  ? 0.2917 0.5239 0.2154 0.0847  0.0146  -0.0630 747  ARG A CB  
5496  C CG  . ARG A 749  ? 0.3566 0.5827 0.2816 0.0857  0.0113  -0.0710 747  ARG A CG  
5497  C CD  . ARG A 749  ? 0.4083 0.6373 0.3373 0.0886  0.0088  -0.0810 747  ARG A CD  
5498  N NE  . ARG A 749  ? 0.3479 0.5734 0.2785 0.0896  0.0054  -0.0882 747  ARG A NE  
5499  C CZ  . ARG A 749  ? 0.3893 0.6194 0.3232 0.0922  0.0027  -0.0967 747  ARG A CZ  
5500  N NH1 . ARG A 749  ? 0.3583 0.5967 0.2940 0.0941  0.0030  -0.0993 747  ARG A NH1 
5501  N NH2 . ARG A 749  ? 0.3534 0.5800 0.2891 0.0929  -0.0004 -0.1027 747  ARG A NH2 
5502  N N   . GLU A 750  ? 0.2541 0.4908 0.1754 0.0803  0.0215  -0.0418 748  GLU A N   
5503  C CA  . GLU A 750  ? 0.3024 0.5478 0.2233 0.0791  0.0239  -0.0332 748  GLU A CA  
5504  C C   . GLU A 750  ? 0.2812 0.5261 0.2001 0.0762  0.0250  -0.0230 748  GLU A C   
5505  O O   . GLU A 750  ? 0.2892 0.5447 0.2075 0.0754  0.0259  -0.0160 748  GLU A O   
5506  C CB  . GLU A 750  ? 0.2643 0.5046 0.1877 0.0787  0.0258  -0.0325 748  GLU A CB  
5507  C CG  . GLU A 750  ? 0.3271 0.5761 0.2508 0.0775  0.0282  -0.0238 748  GLU A CG  
5508  C CD  . GLU A 750  ? 0.3570 0.6005 0.2832 0.0770  0.0301  -0.0227 748  GLU A CD  
5509  O OE1 . GLU A 750  ? 0.4460 0.6822 0.3741 0.0785  0.0294  -0.0304 748  GLU A OE1 
5510  O OE2 . GLU A 750  ? 0.3454 0.5915 0.2722 0.0750  0.0322  -0.0140 748  GLU A OE2 
5511  N N   . ALA A 751  ? 0.2566 0.4894 0.1748 0.0746  0.0249  -0.0220 749  ALA A N   
5512  C CA  . ALA A 751  ? 0.2809 0.5119 0.1979 0.0717  0.0256  -0.0126 749  ALA A CA  
5513  C C   . ALA A 751  ? 0.2888 0.5275 0.2034 0.0720  0.0240  -0.0116 749  ALA A C   
5514  O O   . ALA A 751  ? 0.3040 0.5430 0.2179 0.0698  0.0243  -0.0034 749  ALA A O   
5515  C CB  . ALA A 751  ? 0.2496 0.4611 0.1704 0.0688  0.0242  -0.0122 749  ALA A CB  
5516  N N   . GLY A 752  ? 0.2653 0.5100 0.1794 0.0746  0.0220  -0.0196 750  GLY A N   
5517  C CA  . GLY A 752  ? 0.2910 0.5451 0.2034 0.0751  0.0205  -0.0188 750  GLY A CA  
5518  C C   . GLY A 752  ? 0.2760 0.5252 0.1873 0.0763  0.0178  -0.0264 750  GLY A C   
5519  O O   . GLY A 752  ? 0.3041 0.5610 0.2140 0.0768  0.0164  -0.0262 750  GLY A O   
5520  N N   . ILE A 753  ? 0.2855 0.5225 0.1978 0.0767  0.0170  -0.0330 751  ILE A N   
5521  C CA  . ILE A 753  ? 0.2977 0.5301 0.2097 0.0779  0.0142  -0.0409 751  ILE A CA  
5522  C C   . ILE A 753  ? 0.2673 0.5097 0.1806 0.0809  0.0124  -0.0486 751  ILE A C   
5523  O O   . ILE A 753  ? 0.2837 0.5269 0.1994 0.0824  0.0126  -0.0534 751  ILE A O   
5524  C CB  . ILE A 753  ? 0.2564 0.4734 0.1705 0.0775  0.0135  -0.0461 751  ILE A CB  
5525  C CG1 . ILE A 753  ? 0.2534 0.4573 0.1702 0.0733  0.0144  -0.0374 751  ILE A CG1 
5526  C CG2 . ILE A 753  ? 0.2876 0.5002 0.2022 0.0786  0.0104  -0.0540 751  ILE A CG2 
5527  C CD1 . ILE A 753  ? 0.2615 0.4627 0.1773 0.0712  0.0133  -0.0325 751  ILE A CD1 
5528  N N   . PRO A 754  ? 0.2967 0.5469 0.2087 0.0818  0.0106  -0.0502 752  PRO A N   
5529  C CA  . PRO A 754  ? 0.3022 0.5626 0.2157 0.0848  0.0089  -0.0578 752  PRO A CA  
5530  C C   . PRO A 754  ? 0.2989 0.5507 0.2158 0.0865  0.0066  -0.0685 752  PRO A C   
5531  O O   . PRO A 754  ? 0.2831 0.5220 0.2008 0.0855  0.0056  -0.0709 752  PRO A O   
5532  C CB  . PRO A 754  ? 0.3308 0.5988 0.2422 0.0851  0.0073  -0.0569 752  PRO A CB  
5533  C CG  . PRO A 754  ? 0.2943 0.5587 0.2032 0.0821  0.0087  -0.0471 752  PRO A CG  
5534  C CD  . PRO A 754  ? 0.2659 0.5159 0.1754 0.0803  0.0100  -0.0454 752  PRO A CD  
5535  N N   . ALA A 755  ? 0.3016 0.5608 0.2209 0.0891  0.0057  -0.0748 753  ALA A N   
5536  C CA  . ALA A 755  ? 0.2720 0.5242 0.1956 0.0909  0.0032  -0.0851 753  ALA A CA  
5537  C C   . ALA A 755  ? 0.3037 0.5508 0.2282 0.0912  0.0001  -0.0905 753  ALA A C   
5538  O O   . ALA A 755  ? 0.3157 0.5512 0.2436 0.0913  -0.0018 -0.0966 753  ALA A O   
5539  C CB  . ALA A 755  ? 0.3222 0.5857 0.2482 0.0939  0.0023  -0.0909 753  ALA A CB  
5540  N N   . SER A 756  ? 0.2886 0.5441 0.2102 0.0913  -0.0005 -0.0882 754  SER A N   
5541  C CA  . SER A 756  ? 0.2967 0.5480 0.2192 0.0916  -0.0034 -0.0932 754  SER A CA  
5542  C C   . SER A 756  ? 0.3030 0.5400 0.2244 0.0889  -0.0032 -0.0899 754  SER A C   
5543  O O   . SER A 756  ? 0.3160 0.5449 0.2396 0.0889  -0.0058 -0.0954 754  SER A O   
5544  C CB  . SER A 756  ? 0.3083 0.5730 0.2280 0.0923  -0.0039 -0.0911 754  SER A CB  
5545  O OG  . SER A 756  ? 0.3394 0.6075 0.2549 0.0901  -0.0014 -0.0806 754  SER A OG  
5546  N N   . ALA A 757  ? 0.2927 0.5266 0.2111 0.0866  -0.0003 -0.0811 755  ALA A N   
5547  C CA  . ALA A 757  ? 0.2597 0.4809 0.1769 0.0841  0.0001  -0.0775 755  ALA A CA  
5548  C C   . ALA A 757  ? 0.2999 0.5076 0.2202 0.0835  0.0003  -0.0806 755  ALA A C   
5549  O O   . ALA A 757  ? 0.2786 0.4748 0.1991 0.0818  -0.0001 -0.0800 755  ALA A O   
5550  C CB  . ALA A 757  ? 0.2726 0.4967 0.1857 0.0818  0.0030  -0.0662 755  ALA A CB  
5551  N N   . LEU A 758  ? 0.2452 0.4542 0.1684 0.0849  0.0009  -0.0838 756  LEU A N   
5552  C CA  . LEU A 758  ? 0.2411 0.4377 0.1675 0.0843  0.0012  -0.0862 756  LEU A CA  
5553  C C   . LEU A 758  ? 0.2780 0.4764 0.2094 0.0868  -0.0006 -0.0947 756  LEU A C   
5554  O O   . LEU A 758  ? 0.2981 0.5051 0.2297 0.0880  0.0007  -0.0941 756  LEU A O   
5555  C CB  . LEU A 758  ? 0.2721 0.4673 0.1964 0.0826  0.0048  -0.0782 756  LEU A CB  
5556  C CG  . LEU A 758  ? 0.2783 0.4598 0.2079 0.0812  0.0049  -0.0790 756  LEU A CG  
5557  C CD1 . LEU A 758  ? 0.2693 0.4354 0.2032 0.0791  0.0023  -0.0812 756  LEU A CD1 
5558  C CD2 . LEU A 758  ? 0.2765 0.4553 0.2055 0.0785  0.0080  -0.0693 756  LEU A CD2 
5559  N N   . GLN A 759  ? 0.2646 0.4551 0.2006 0.0874  -0.0038 -0.1023 757  GLN A N   
5560  C CA  . GLN A 759  ? 0.2672 0.4577 0.2090 0.0896  -0.0061 -0.1106 757  GLN A CA  
5561  C C   . GLN A 759  ? 0.2795 0.4556 0.2261 0.0886  -0.0066 -0.1128 757  GLN A C   
5562  O O   . GLN A 759  ? 0.2995 0.4645 0.2467 0.0869  -0.0074 -0.1121 757  GLN A O   
5563  C CB  . GLN A 759  ? 0.2736 0.4674 0.2182 0.0912  -0.0099 -0.1178 757  GLN A CB  
5564  C CG  . GLN A 759  ? 0.2868 0.4958 0.2273 0.0925  -0.0096 -0.1161 757  GLN A CG  
5565  C CD  . GLN A 759  ? 0.2817 0.4936 0.2250 0.0940  -0.0133 -0.1231 757  GLN A CD  
5566  O OE1 . GLN A 759  ? 0.2925 0.5101 0.2398 0.0965  -0.0155 -0.1301 757  GLN A OE1 
5567  N NE2 . GLN A 759  ? 0.2879 0.4957 0.2292 0.0926  -0.0142 -0.1214 757  GLN A NE2 
5568  N N   . LEU A 760  ? 0.2792 0.4555 0.2291 0.0897  -0.0062 -0.1151 758  LEU A N   
5569  C CA  . LEU A 760  ? 0.2793 0.4429 0.2344 0.0890  -0.0067 -0.1172 758  LEU A CA  
5570  C C   . LEU A 760  ? 0.2820 0.4425 0.2446 0.0907  -0.0109 -0.1264 758  LEU A C   
5571  O O   . LEU A 760  ? 0.2778 0.4477 0.2422 0.0930  -0.0122 -0.1309 758  LEU A O   
5572  C CB  . LEU A 760  ? 0.2755 0.4413 0.2302 0.0892  -0.0038 -0.1140 758  LEU A CB  
5573  C CG  . LEU A 760  ? 0.2989 0.4522 0.2594 0.0887  -0.0044 -0.1162 758  LEU A CG  
5574  C CD1 . LEU A 760  ? 0.2838 0.4251 0.2436 0.0853  -0.0031 -0.1095 758  LEU A CD1 
5575  C CD2 . LEU A 760  ? 0.2975 0.4554 0.2594 0.0899  -0.0027 -0.1160 758  LEU A CD2 
5576  N N   . LEU A 761  ? 0.2781 0.4258 0.2454 0.0894  -0.0132 -0.1289 759  LEU A N   
5577  C CA  A LEU A 761  ? 0.2907 0.4341 0.2661 0.0905  -0.0176 -0.1370 759  LEU A CA  
5578  C CA  B LEU A 761  ? 0.2908 0.4342 0.2662 0.0905  -0.0176 -0.1370 759  LEU A CA  
5579  C C   . LEU A 761  ? 0.2865 0.4167 0.2683 0.0894  -0.0184 -0.1378 759  LEU A C   
5580  O O   . LEU A 761  ? 0.2767 0.3956 0.2612 0.0874  -0.0198 -0.1373 759  LEU A O   
5581  C CB  A LEU A 761  ? 0.2861 0.4278 0.2620 0.0900  -0.0204 -0.1394 759  LEU A CB  
5582  C CB  B LEU A 761  ? 0.2862 0.4273 0.2624 0.0900  -0.0204 -0.1394 759  LEU A CB  
5583  C CG  A LEU A 761  ? 0.2779 0.4331 0.2474 0.0911  -0.0194 -0.1379 759  LEU A CG  
5584  C CG  B LEU A 761  ? 0.2766 0.4298 0.2472 0.0910  -0.0203 -0.1390 759  LEU A CG  
5585  C CD1 A LEU A 761  ? 0.2802 0.4326 0.2482 0.0899  -0.0210 -0.1377 759  LEU A CD1 
5586  C CD1 B LEU A 761  ? 0.2661 0.4337 0.2359 0.0938  -0.0199 -0.1415 759  LEU A CD1 
5587  C CD2 A LEU A 761  ? 0.2762 0.4430 0.2482 0.0942  -0.0212 -0.1440 759  LEU A CD2 
5588  C CD2 B LEU A 761  ? 0.2789 0.4330 0.2414 0.0891  -0.0169 -0.1307 759  LEU A CD2 
5589  N N   . PRO A 762  ? 0.2655 0.3970 0.2500 0.0904  -0.0177 -0.1389 760  PRO A N   
5590  C CA  . PRO A 762  ? 0.2892 0.4085 0.2803 0.0894  -0.0186 -0.1396 760  PRO A CA  
5591  C C   . PRO A 762  ? 0.3123 0.4247 0.3125 0.0896  -0.0235 -0.1462 760  PRO A C   
5592  O O   . PRO A 762  ? 0.3088 0.4278 0.3112 0.0913  -0.0262 -0.1517 760  PRO A O   
5593  C CB  . PRO A 762  ? 0.2651 0.3902 0.2569 0.0910  -0.0170 -0.1400 760  PRO A CB  
5594  C CG  . PRO A 762  ? 0.2747 0.4138 0.2585 0.0921  -0.0140 -0.1369 760  PRO A CG  
5595  C CD  . PRO A 762  ? 0.2560 0.4004 0.2374 0.0925  -0.0157 -0.1388 760  PRO A CD  
5596  N N   . GLY A 763  ? 0.2715 0.3710 0.2773 0.0877  -0.0248 -0.1454 761  GLY A N   
5597  C CA  . GLY A 763  ? 0.3062 0.3982 0.3217 0.0875  -0.0295 -0.1508 761  GLY A CA  
5598  C C   . GLY A 763  ? 0.3073 0.3856 0.3259 0.0846  -0.0304 -0.1476 761  GLY A C   
5599  O O   . GLY A 763  ? 0.2790 0.3535 0.2923 0.0829  -0.0273 -0.1416 761  GLY A O   
5600  N N   . ASP A 764  ? 0.3276 0.3989 0.3551 0.0839  -0.0347 -0.1515 762  ASP A N   
5601  C CA  . ASP A 764  ? 0.3486 0.4066 0.3808 0.0810  -0.0361 -0.1486 762  ASP A CA  
5602  C C   . ASP A 764  ? 0.3431 0.3995 0.3726 0.0795  -0.0369 -0.1476 762  ASP A C   
5603  O O   . ASP A 764  ? 0.3010 0.3661 0.3232 0.0806  -0.0354 -0.1477 762  ASP A O   
5604  C CB  . ASP A 764  ? 0.3866 0.4373 0.4308 0.0806  -0.0403 -0.1520 762  ASP A CB  
5605  C CG  . ASP A 764  ? 0.3946 0.4495 0.4450 0.0822  -0.0446 -0.1589 762  ASP A CG  
5606  O OD1 . ASP A 764  ? 0.4176 0.4783 0.4639 0.0828  -0.0449 -0.1605 762  ASP A OD1 
5607  O OD2 . ASP A 764  ? 0.5124 0.5651 0.5720 0.0828  -0.0478 -0.1626 762  ASP A OD2 
5608  N N   . GLY A 765  ? 0.3184 0.3636 0.3540 0.0769  -0.0394 -0.1463 763  GLY A N   
5609  C CA  . GLY A 765  ? 0.3099 0.3529 0.3437 0.0747  -0.0402 -0.1440 763  GLY A CA  
5610  C C   . GLY A 765  ? 0.3324 0.3825 0.3671 0.0771  -0.0430 -0.1510 763  GLY A C   
5611  O O   . GLY A 765  ? 0.3595 0.4114 0.3898 0.0765  -0.0429 -0.1502 763  GLY A O   
5612  N N   . ARG A 766  ? 0.3407 0.3954 0.3814 0.0792  -0.0456 -0.1566 764  ARG A N   
5613  C CA  . ARG A 766  ? 0.3465 0.4092 0.3884 0.0812  -0.0483 -0.1623 764  ARG A CA  
5614  C C   . ARG A 766  ? 0.3463 0.4212 0.3775 0.0830  -0.0451 -0.1617 764  ARG A C   
5615  O O   . ARG A 766  ? 0.3393 0.4195 0.3684 0.0836  -0.0463 -0.1638 764  ARG A O   
5616  C CB  . ARG A 766  ? 0.4191 0.4854 0.4692 0.0835  -0.0513 -0.1686 764  ARG A CB  
5617  C CG  . ARG A 766  ? 0.4607 0.5169 0.5231 0.0821  -0.0556 -0.1703 764  ARG A CG  
5618  C CD  . ARG A 766  ? 0.4399 0.5013 0.5091 0.0848  -0.0580 -0.1763 764  ARG A CD  
5619  N NE  . ARG A 766  ? 0.4895 0.5536 0.5548 0.0858  -0.0547 -0.1744 764  ARG A NE  
5620  C CZ  . ARG A 766  ? 0.5033 0.5767 0.5689 0.0887  -0.0547 -0.1788 764  ARG A CZ  
5621  N NH1 . ARG A 766  ? 0.5729 0.6544 0.6420 0.0912  -0.0577 -0.1855 764  ARG A NH1 
5622  N NH2 . ARG A 766  ? 0.5334 0.6081 0.5958 0.0893  -0.0517 -0.1765 764  ARG A NH2 
5623  N N   . VAL A 767  ? 0.3008 0.3809 0.3255 0.0839  -0.0412 -0.1587 765  VAL A N   
5624  C CA  . VAL A 767  ? 0.3287 0.4206 0.3433 0.0854  -0.0380 -0.1570 765  VAL A CA  
5625  C C   . VAL A 767  ? 0.2903 0.3793 0.2981 0.0832  -0.0360 -0.1516 765  VAL A C   
5626  O O   . VAL A 767  ? 0.3103 0.4068 0.3128 0.0838  -0.0356 -0.1516 765  VAL A O   
5627  C CB  . VAL A 767  ? 0.2775 0.3757 0.2877 0.0867  -0.0344 -0.1548 765  VAL A CB  
5628  C CG1 . VAL A 767  ? 0.3142 0.4255 0.3147 0.0881  -0.0314 -0.1525 765  VAL A CG1 
5629  C CG2 . VAL A 767  ? 0.3313 0.4319 0.3488 0.0888  -0.0368 -0.1605 765  VAL A CG2 
5630  N N   . GLY A 768  ? 0.3118 0.3901 0.3198 0.0807  -0.0347 -0.1469 766  GLY A N   
5631  C CA  . GLY A 768  ? 0.2925 0.3670 0.2958 0.0775  -0.0331 -0.1398 766  GLY A CA  
5632  C C   . GLY A 768  ? 0.2706 0.3433 0.2769 0.0772  -0.0366 -0.1435 766  GLY A C   
5633  O O   . GLY A 768  ? 0.2869 0.3639 0.2873 0.0766  -0.0357 -0.1410 766  GLY A O   
5634  N N   . ALA A 769  ? 0.2961 0.3624 0.3118 0.0775  -0.0408 -0.1494 767  ALA A N   
5635  C CA  . ALA A 769  ? 0.3326 0.3965 0.3523 0.0767  -0.0443 -0.1521 767  ALA A CA  
5636  C C   . ALA A 769  ? 0.2989 0.3751 0.3156 0.0793  -0.0452 -0.1563 767  ALA A C   
5637  O O   . ALA A 769  ? 0.3253 0.4033 0.3393 0.0788  -0.0460 -0.1562 767  ALA A O   
5638  C CB  . ALA A 769  ? 0.3316 0.3866 0.3635 0.0757  -0.0486 -0.1555 767  ALA A CB  
5639  N N   . ALA A 770  ? 0.3051 0.3900 0.3223 0.0820  -0.0451 -0.1600 768  ALA A N   
5640  C CA  . ALA A 770  ? 0.3078 0.4053 0.3223 0.0847  -0.0459 -0.1639 768  ALA A CA  
5641  C C   . ALA A 770  ? 0.3049 0.4100 0.3082 0.0846  -0.0424 -0.1591 768  ALA A C   
5642  O O   . ALA A 770  ? 0.3145 0.4264 0.3152 0.0854  -0.0433 -0.1607 768  ALA A O   
5643  C CB  . ALA A 770  ? 0.3096 0.4154 0.3265 0.0876  -0.0462 -0.1682 768  ALA A CB  
5644  N N   . LEU A 771  ? 0.2894 0.3935 0.2863 0.0836  -0.0383 -0.1531 769  LEU A N   
5645  C CA  . LEU A 771  ? 0.3144 0.4254 0.3011 0.0833  -0.0349 -0.1477 769  LEU A CA  
5646  C C   . LEU A 771  ? 0.3106 0.4154 0.2955 0.0811  -0.0355 -0.1451 769  LEU A C   
5647  O O   . LEU A 771  ? 0.3161 0.4280 0.2957 0.0814  -0.0352 -0.1440 769  LEU A O   
5648  C CB  . LEU A 771  ? 0.2830 0.3938 0.2645 0.0828  -0.0305 -0.1419 769  LEU A CB  
5649  C CG  . LEU A 771  ? 0.2787 0.3973 0.2605 0.0851  -0.0293 -0.1436 769  LEU A CG  
5650  C CD1 . LEU A 771  ? 0.2968 0.4130 0.2745 0.0841  -0.0253 -0.1376 769  LEU A CD1 
5651  C CD2 . LEU A 771  ? 0.3169 0.4507 0.2941 0.0874  -0.0289 -0.1449 769  LEU A CD2 
5652  N N   . VAL A 772  ? 0.2996 0.3913 0.2899 0.0780  -0.0364 -0.1424 770  VAL A N   
5653  C CA  . VAL A 772  ? 0.2898 0.3746 0.2803 0.0747  -0.0370 -0.1376 770  VAL A CA  
5654  C C   . VAL A 772  ? 0.3178 0.4063 0.3104 0.0763  -0.0407 -0.1444 770  VAL A C   
5655  O O   . VAL A 772  ? 0.3410 0.4317 0.3296 0.0751  -0.0405 -0.1414 770  VAL A O   
5656  C CB  . VAL A 772  ? 0.2802 0.3509 0.2775 0.0711  -0.0376 -0.1337 770  VAL A CB  
5657  C CG1 . VAL A 772  ? 0.3092 0.3734 0.3084 0.0680  -0.0390 -0.1306 770  VAL A CG1 
5658  C CG2 . VAL A 772  ? 0.2769 0.3444 0.2708 0.0690  -0.0335 -0.1255 770  VAL A CG2 
5659  N N   . ALA A 773  ? 0.3251 0.4144 0.3248 0.0784  -0.0443 -0.1525 771  ALA A N   
5660  C CA  . ALA A 773  ? 0.3110 0.4027 0.3152 0.0791  -0.0481 -0.1575 771  ALA A CA  
5661  C C   . ALA A 773  ? 0.3782 0.4842 0.3768 0.0818  -0.0476 -0.1594 771  ALA A C   
5662  O O   . ALA A 773  ? 0.4026 0.5116 0.4035 0.0824  -0.0504 -0.1629 771  ALA A O   
5663  C CB  . ALA A 773  ? 0.3648 0.4518 0.3804 0.0797  -0.0521 -0.1633 771  ALA A CB  
5664  N N   . ALA A 774  ? 0.3598 0.4748 0.3516 0.0833  -0.0442 -0.1570 772  ALA A N   
5665  C CA  . ALA A 774  ? 0.3617 0.4912 0.3489 0.0859  -0.0438 -0.1586 772  ALA A CA  
5666  C C   . ALA A 774  ? 0.3342 0.4670 0.3151 0.0849  -0.0432 -0.1552 772  ALA A C   
5667  O O   . ALA A 774  ? 0.3490 0.4768 0.3249 0.0827  -0.0411 -0.1493 772  ALA A O   
5668  C CB  . ALA A 774  ? 0.3758 0.5139 0.3573 0.0873  -0.0401 -0.1558 772  ALA A CB  
5669  N N   . ALA A 775  ? 0.4210 0.5627 0.4024 0.0868  -0.0453 -0.1592 773  ALA A N   
5670  C CA  . ALA A 775  ? 0.4234 0.5670 0.4007 0.0858  -0.0457 -0.1569 773  ALA A CA  
5671  C C   . ALA A 775  ? 0.3382 0.4877 0.3052 0.0851  -0.0417 -0.1492 773  ALA A C   
5672  O O   . ALA A 775  ? 0.3729 0.5194 0.3362 0.0832  -0.0414 -0.1452 773  ALA A O   
5673  C CB  . ALA A 775  ? 0.4098 0.5626 0.3897 0.0882  -0.0487 -0.1629 773  ALA A CB  
5674  N N   . GLU A 776  ? 0.3237 0.4818 0.2864 0.0865  -0.0388 -0.1468 774  GLU A N   
5675  C CA  . GLU A 776  ? 0.3022 0.4669 0.2559 0.0858  -0.0351 -0.1390 774  GLU A CA  
5676  C C   . GLU A 776  ? 0.3110 0.4667 0.2617 0.0834  -0.0322 -0.1327 774  GLU A C   
5677  O O   . GLU A 776  ? 0.3211 0.4813 0.2648 0.0826  -0.0291 -0.1256 774  GLU A O   
5678  C CB  . GLU A 776  ? 0.3387 0.5180 0.2892 0.0883  -0.0333 -0.1387 774  GLU A CB  
5679  C CG  . GLU A 776  ? 0.3701 0.5599 0.3230 0.0909  -0.0359 -0.1448 774  GLU A CG  
5680  C CD  . GLU A 776  ? 0.4649 0.6540 0.4257 0.0931  -0.0385 -0.1532 774  GLU A CD  
5681  O OE1 . GLU A 776  ? 0.3839 0.5630 0.3492 0.0922  -0.0388 -0.1545 774  GLU A OE1 
5682  O OE2 . GLU A 776  ? 0.4783 0.6774 0.4414 0.0956  -0.0405 -0.1585 774  GLU A OE2 
5683  N N   . THR A 777  ? 0.2738 0.4173 0.2299 0.0822  -0.0331 -0.1348 775  THR A N   
5684  C CA  . THR A 777  ? 0.2781 0.4120 0.2336 0.0792  -0.0303 -0.1271 775  THR A CA  
5685  C C   . THR A 777  ? 0.3091 0.4372 0.2633 0.0757  -0.0297 -0.1197 775  THR A C   
5686  O O   . THR A 777  ? 0.3333 0.4553 0.2915 0.0746  -0.0325 -0.1220 775  THR A O   
5687  C CB  . THR A 777  ? 0.2750 0.3970 0.2384 0.0783  -0.0317 -0.1303 775  THR A CB  
5688  O OG1 . THR A 777  ? 0.2897 0.4175 0.2541 0.0814  -0.0316 -0.1360 775  THR A OG1 
5689  C CG2 . THR A 777  ? 0.2621 0.3729 0.2263 0.0742  -0.0291 -0.1212 775  THR A CG2 
5690  N N   . ALA A 778  ? 0.2691 0.3995 0.2179 0.0741  -0.0263 -0.1109 776  ALA A N   
5691  C CA  . ALA A 778  ? 0.2559 0.3829 0.2028 0.0713  -0.0256 -0.1037 776  ALA A CA  
5692  C C   . ALA A 778  ? 0.2677 0.3818 0.2173 0.0675  -0.0238 -0.0968 776  ALA A C   
5693  O O   . ALA A 778  ? 0.2694 0.3790 0.2188 0.0650  -0.0236 -0.0915 776  ALA A O   
5694  C CB  . ALA A 778  ? 0.2735 0.4124 0.2131 0.0721  -0.0233 -0.0984 776  ALA A CB  
5695  N N   . GLY A 779  ? 0.2507 0.3594 0.2029 0.0671  -0.0227 -0.0968 777  GLY A N   
5696  C CA  . GLY A 779  ? 0.2440 0.3410 0.1989 0.0637  -0.0211 -0.0908 777  GLY A CA  
5697  C C   . GLY A 779  ? 0.2367 0.3296 0.1949 0.0641  -0.0206 -0.0931 777  GLY A C   
5698  O O   . GLY A 779  ? 0.2482 0.3486 0.2053 0.0671  -0.0205 -0.0974 777  GLY A O   
5699  N N   . VAL A 780  ? 0.2418 0.3231 0.2044 0.0613  -0.0204 -0.0903 778  VAL A N   
5700  C CA  . VAL A 780  ? 0.2358 0.3116 0.2024 0.0613  -0.0203 -0.0920 778  VAL A CA  
5701  C C   . VAL A 780  ? 0.2310 0.2995 0.1973 0.0582  -0.0175 -0.0840 778  VAL A C   
5702  O O   . VAL A 780  ? 0.2353 0.2971 0.2025 0.0553  -0.0174 -0.0797 778  VAL A O   
5703  C CB  . VAL A 780  ? 0.2590 0.3276 0.2330 0.0612  -0.0238 -0.0982 778  VAL A CB  
5704  C CG1 . VAL A 780  ? 0.2422 0.3057 0.2206 0.0614  -0.0238 -0.0999 778  VAL A CG1 
5705  C CG2 . VAL A 780  ? 0.2559 0.3320 0.2307 0.0644  -0.0269 -0.1066 778  VAL A CG2 
5706  N N   . MET A 781  ? 0.2239 0.2942 0.1887 0.0588  -0.0152 -0.0822 779  MET A N   
5707  C CA  . MET A 781  ? 0.2081 0.2715 0.1733 0.0561  -0.0128 -0.0756 779  MET A CA  
5708  C C   . MET A 781  ? 0.2272 0.2848 0.1975 0.0563  -0.0136 -0.0789 779  MET A C   
5709  O O   . MET A 781  ? 0.2279 0.2908 0.1981 0.0588  -0.0135 -0.0827 779  MET A O   
5710  C CB  . MET A 781  ? 0.2533 0.3236 0.2131 0.0565  -0.0096 -0.0703 779  MET A CB  
5711  C CG  . MET A 781  ? 0.2302 0.3071 0.1853 0.0566  -0.0090 -0.0670 779  MET A CG  
5712  S SD  . MET A 781  ? 0.2420 0.3282 0.1915 0.0573  -0.0056 -0.0610 779  MET A SD  
5713  C CE  . MET A 781  ? 0.2383 0.3142 0.1895 0.0535  -0.0034 -0.0530 779  MET A CE  
5714  N N   . PHE A 782  ? 0.2484 0.2958 0.2235 0.0537  -0.0146 -0.0775 780  PHE A N   
5715  C CA  . PHE A 782  ? 0.2284 0.2695 0.2093 0.0534  -0.0159 -0.0802 780  PHE A CA  
5716  C C   . PHE A 782  ? 0.2398 0.2735 0.2214 0.0504  -0.0138 -0.0736 780  PHE A C   
5717  O O   . PHE A 782  ? 0.2300 0.2590 0.2111 0.0477  -0.0132 -0.0688 780  PHE A O   
5718  C CB  . PHE A 782  ? 0.2318 0.2672 0.2189 0.0529  -0.0195 -0.0847 780  PHE A CB  
5719  C CG  . PHE A 782  ? 0.2335 0.2617 0.2274 0.0522  -0.0210 -0.0865 780  PHE A CG  
5720  C CD1 . PHE A 782  ? 0.2476 0.2786 0.2446 0.0550  -0.0225 -0.0926 780  PHE A CD1 
5721  C CD2 . PHE A 782  ? 0.2441 0.2632 0.2415 0.0488  -0.0210 -0.0818 780  PHE A CD2 
5722  C CE1 . PHE A 782  ? 0.2557 0.2801 0.2594 0.0544  -0.0240 -0.0940 780  PHE A CE1 
5723  C CE2 . PHE A 782  ? 0.2474 0.2603 0.2511 0.0481  -0.0224 -0.0830 780  PHE A CE2 
5724  C CZ  . PHE A 782  ? 0.2373 0.2526 0.2444 0.0509  -0.0240 -0.0889 780  PHE A CZ  
5725  N N   . THR A 783  ? 0.2168 0.2496 0.1996 0.0510  -0.0128 -0.0737 781  THR A N   
5726  C CA  . THR A 783  ? 0.2345 0.2597 0.2194 0.0483  -0.0115 -0.0688 781  THR A CA  
5727  C C   . THR A 783  ? 0.2136 0.2347 0.2047 0.0490  -0.0135 -0.0729 781  THR A C   
5728  O O   . THR A 783  ? 0.2326 0.2586 0.2242 0.0518  -0.0140 -0.0776 781  THR A O   
5729  C CB  . THR A 783  ? 0.2411 0.2693 0.2212 0.0480  -0.0081 -0.0634 781  THR A CB  
5730  O OG1 . THR A 783  ? 0.2331 0.2653 0.2082 0.0475  -0.0066 -0.0597 781  THR A OG1 
5731  C CG2 . THR A 783  ? 0.2453 0.2657 0.2275 0.0451  -0.0069 -0.0585 781  THR A CG2 
5732  N N   . GLY A 784  ? 0.2343 0.2469 0.2304 0.0464  -0.0149 -0.0713 782  GLY A N   
5733  C CA  . GLY A 784  ? 0.2334 0.2417 0.2365 0.0468  -0.0174 -0.0752 782  GLY A CA  
5734  C C   . GLY A 784  ? 0.2107 0.2106 0.2191 0.0437  -0.0192 -0.0729 782  GLY A C   
5735  O O   . GLY A 784  ? 0.2567 0.2541 0.2628 0.0410  -0.0178 -0.0676 782  GLY A O   
5736  N N   . SER A 785  ? 0.2454 0.2417 0.2613 0.0441  -0.0224 -0.0769 783  SER A N   
5737  C CA  . SER A 785  ? 0.2579 0.2465 0.2797 0.0410  -0.0243 -0.0744 783  SER A CA  
5738  C C   . SER A 785  ? 0.2659 0.2543 0.2880 0.0399  -0.0258 -0.0749 783  SER A C   
5739  O O   . SER A 785  ? 0.2611 0.2544 0.2816 0.0422  -0.0268 -0.0795 783  SER A O   
5740  C CB  . SER A 785  ? 0.2969 0.2817 0.3275 0.0416  -0.0276 -0.0783 783  SER A CB  
5741  O OG  . SER A 785  ? 0.2952 0.2831 0.3289 0.0444  -0.0305 -0.0857 783  SER A OG  
5742  N N   . THR A 786  ? 0.2720 0.2550 0.2962 0.0365  -0.0258 -0.0700 784  THR A N   
5743  C CA  . THR A 786  ? 0.2751 0.2574 0.3002 0.0352  -0.0273 -0.0700 784  THR A CA  
5744  C C   . THR A 786  ? 0.2650 0.2469 0.2970 0.0367  -0.0315 -0.0765 784  THR A C   
5745  O O   . THR A 786  ? 0.2695 0.2542 0.3006 0.0375  -0.0327 -0.0794 784  THR A O   
5746  C CB  . THR A 786  ? 0.2873 0.2642 0.3146 0.0313  -0.0267 -0.0638 784  THR A CB  
5747  O OG1 . THR A 786  ? 0.2942 0.2718 0.3153 0.0302  -0.0230 -0.0585 784  THR A OG1 
5748  C CG2 . THR A 786  ? 0.3095 0.2860 0.3377 0.0299  -0.0280 -0.0636 784  THR A CG2 
5749  N N   . GLU A 787  ? 0.3055 0.2840 0.3447 0.0371  -0.0338 -0.0790 785  GLU A N   
5750  C CA  . GLU A 787  ? 0.2778 0.2553 0.3248 0.0384  -0.0383 -0.0852 785  GLU A CA  
5751  C C   . GLU A 787  ? 0.2851 0.2696 0.3292 0.0424  -0.0390 -0.0925 785  GLU A C   
5752  O O   . GLU A 787  ? 0.2808 0.2666 0.3277 0.0434  -0.0418 -0.0972 785  GLU A O   
5753  C CB  . GLU A 787  ? 0.3360 0.3085 0.3917 0.0381  -0.0406 -0.0861 785  GLU A CB  
5754  N N   . VAL A 788  ? 0.2783 0.2678 0.3166 0.0448  -0.0364 -0.0934 786  VAL A N   
5755  C CA  . VAL A 788  ? 0.2676 0.2651 0.3025 0.0487  -0.0368 -0.1000 786  VAL A CA  
5756  C C   . VAL A 788  ? 0.2910 0.2932 0.3188 0.0486  -0.0353 -0.0986 786  VAL A C   
5757  O O   . VAL A 788  ? 0.2689 0.2757 0.2967 0.0507  -0.0373 -0.1041 786  VAL A O   
5758  C CB  . VAL A 788  ? 0.2735 0.2757 0.3045 0.0512  -0.0345 -0.1011 786  VAL A CB  
5759  C CG1 . VAL A 788  ? 0.2892 0.3013 0.3146 0.0549  -0.0340 -0.1064 786  VAL A CG1 
5760  C CG2 . VAL A 788  ? 0.2859 0.2844 0.3252 0.0522  -0.0370 -0.1047 786  VAL A CG2 
5761  N N   . ALA A 789  ? 0.2544 0.2557 0.2765 0.0461  -0.0320 -0.0913 787  ALA A N   
5762  C CA  . ALA A 789  ? 0.2676 0.2727 0.2838 0.0457  -0.0307 -0.0895 787  ALA A CA  
5763  C C   . ALA A 789  ? 0.2432 0.2459 0.2642 0.0448  -0.0341 -0.0920 787  ALA A C   
5764  O O   . ALA A 789  ? 0.2378 0.2456 0.2559 0.0462  -0.0348 -0.0948 787  ALA A O   
5765  C CB  . ALA A 789  ? 0.2172 0.2198 0.2286 0.0428  -0.0272 -0.0813 787  ALA A CB  
5766  N N   . ARG A 790  ? 0.2650 0.2603 0.2938 0.0425  -0.0363 -0.0911 788  ARG A N   
5767  C CA  . ARG A 790  ? 0.2673 0.2601 0.3017 0.0414  -0.0396 -0.0932 788  ARG A CA  
5768  C C   . ARG A 790  ? 0.2569 0.2535 0.2949 0.0447  -0.0432 -0.1020 788  ARG A C   
5769  O O   . ARG A 790  ? 0.2713 0.2700 0.3099 0.0451  -0.0452 -0.1047 788  ARG A O   
5770  C CB  . ARG A 790  ? 0.3107 0.2953 0.3530 0.0382  -0.0412 -0.0897 788  ARG A CB  
5771  C CG  . ARG A 790  ? 0.2871 0.2686 0.3358 0.0364  -0.0445 -0.0905 788  ARG A CG  
5772  C CD  . ARG A 790  ? 0.2994 0.2736 0.3550 0.0327  -0.0454 -0.0853 788  ARG A CD  
5773  N NE  . ARG A 790  ? 0.2828 0.2559 0.3330 0.0300  -0.0415 -0.0776 788  ARG A NE  
5774  C CZ  . ARG A 790  ? 0.2560 0.2261 0.3061 0.0284  -0.0396 -0.0729 788  ARG A CZ  
5775  N NH1 . ARG A 790  ? 0.3210 0.2885 0.3763 0.0291  -0.0411 -0.0746 788  ARG A NH1 
5776  N NH2 . ARG A 790  ? 0.3229 0.2926 0.3678 0.0262  -0.0363 -0.0665 788  ARG A NH2 
5777  N N   . LEU A 791  ? 0.2769 0.2749 0.3176 0.0473  -0.0442 -0.1067 789  LEU A N   
5778  C CA  . LEU A 791  ? 0.2860 0.2888 0.3296 0.0509  -0.0475 -0.1158 789  LEU A CA  
5779  C C   . LEU A 791  ? 0.2764 0.2886 0.3111 0.0535  -0.0457 -0.1180 789  LEU A C   
5780  O O   . LEU A 791  ? 0.2834 0.2997 0.3192 0.0553  -0.0483 -0.1237 789  LEU A O   
5781  C CB  . LEU A 791  ? 0.2738 0.2767 0.3215 0.0533  -0.0484 -0.1201 789  LEU A CB  
5782  C CG  . LEU A 791  ? 0.3316 0.3257 0.3894 0.0513  -0.0509 -0.1190 789  LEU A CG  
5783  C CD1 . LEU A 791  ? 0.3623 0.3573 0.4226 0.0538  -0.0510 -0.1225 789  LEU A CD1 
5784  C CD2 . LEU A 791  ? 0.3554 0.3458 0.4229 0.0509  -0.0559 -0.1234 789  LEU A CD2 
5785  N N   . ILE A 792  ? 0.2577 0.2740 0.2838 0.0536  -0.0415 -0.1135 790  ILE A N   
5786  C CA  . ILE A 792  ? 0.2729 0.2986 0.2906 0.0558  -0.0397 -0.1144 790  ILE A CA  
5787  C C   . ILE A 792  ? 0.2874 0.3128 0.3031 0.0539  -0.0400 -0.1118 790  ILE A C   
5788  O O   . ILE A 792  ? 0.2904 0.3224 0.3036 0.0559  -0.0413 -0.1160 790  ILE A O   
5789  C CB  . ILE A 792  ? 0.2647 0.2941 0.2746 0.0560  -0.0352 -0.1092 790  ILE A CB  
5790  C CG1 . ILE A 792  ? 0.2846 0.3164 0.2963 0.0586  -0.0352 -0.1133 790  ILE A CG1 
5791  C CG2 . ILE A 792  ? 0.3127 0.3511 0.3140 0.0572  -0.0331 -0.1080 790  ILE A CG2 
5792  C CD1 . ILE A 792  ? 0.2596 0.2934 0.2655 0.0583  -0.0310 -0.1079 790  ILE A CD1 
5793  N N   . GLN A 793  ? 0.2586 0.2769 0.2755 0.0502  -0.0390 -0.1052 791  GLN A N   
5794  C CA  . GLN A 793  ? 0.2702 0.2876 0.2861 0.0483  -0.0394 -0.1026 791  GLN A CA  
5795  C C   . GLN A 793  ? 0.2782 0.2957 0.3004 0.0492  -0.0439 -0.1092 791  GLN A C   
5796  O O   . GLN A 793  ? 0.2813 0.3032 0.3007 0.0499  -0.0447 -0.1108 791  GLN A O   
5797  C CB  . GLN A 793  ? 0.2849 0.2943 0.3028 0.0442  -0.0380 -0.0953 791  GLN A CB  
5798  C CG  . GLN A 793  ? 0.2855 0.2930 0.3039 0.0419  -0.0387 -0.0926 791  GLN A CG  
5799  C CD  . GLN A 793  ? 0.3181 0.3177 0.3409 0.0380  -0.0382 -0.0868 791  GLN A CD  
5800  O OE1 . GLN A 793  ? 0.3554 0.3499 0.3845 0.0371  -0.0397 -0.0872 791  GLN A OE1 
5801  N NE2 . GLN A 793  ? 0.3172 0.3162 0.3366 0.0358  -0.0363 -0.0814 791  GLN A NE2 
5802  N N   . ALA A 794  ? 0.2912 0.3038 0.3220 0.0493  -0.0471 -0.1132 792  ALA A N   
5803  C CA  . ALA A 794  ? 0.3323 0.3446 0.3702 0.0502  -0.0517 -0.1198 792  ALA A CA  
5804  C C   . ALA A 794  ? 0.3153 0.3369 0.3501 0.0545  -0.0530 -0.1277 792  ALA A C   
5805  O O   . ALA A 794  ? 0.3467 0.3714 0.3823 0.0553  -0.0555 -0.1316 792  ALA A O   
5806  C CB  . ALA A 794  ? 0.3239 0.3290 0.3725 0.0495  -0.0549 -0.1221 792  ALA A CB  
5807  N N   . GLN A 795  ? 0.3014 0.3282 0.3326 0.0573  -0.0514 -0.1301 793  GLN A N   
5808  C CA  . GLN A 795  ? 0.3060 0.3431 0.3333 0.0615  -0.0521 -0.1372 793  GLN A CA  
5809  C C   . GLN A 795  ? 0.3580 0.4021 0.3769 0.0616  -0.0504 -0.1348 793  GLN A C   
5810  O O   . GLN A 795  ? 0.3560 0.4060 0.3746 0.0637  -0.0528 -0.1406 793  GLN A O   
5811  C CB  . GLN A 795  ? 0.4046 0.4463 0.4280 0.0638  -0.0495 -0.1378 793  GLN A CB  
5812  C CG  . GLN A 795  ? 0.4742 0.5197 0.5023 0.0676  -0.0524 -0.1472 793  GLN A CG  
5813  C CD  . GLN A 795  ? 0.4140 0.4638 0.4380 0.0695  -0.0493 -0.1466 793  GLN A CD  
5814  O OE1 . GLN A 795  ? 0.4720 0.5182 0.4927 0.0672  -0.0458 -0.1391 793  GLN A OE1 
5815  N NE2 . GLN A 795  ? 0.3540 0.4120 0.3782 0.0736  -0.0506 -0.1546 793  GLN A NE2 
5816  N N   . LEU A 796  ? 0.3038 0.3473 0.3161 0.0595  -0.0463 -0.1264 794  LEU A N   
5817  C CA  . LEU A 796  ? 0.3265 0.3765 0.3309 0.0596  -0.0444 -0.1233 794  LEU A CA  
5818  C C   . LEU A 796  ? 0.3051 0.3520 0.3120 0.0576  -0.0465 -0.1225 794  LEU A C   
5819  O O   . LEU A 796  ? 0.3604 0.4137 0.3622 0.0583  -0.0462 -0.1222 794  LEU A O   
5820  C CB  . LEU A 796  ? 0.2933 0.3429 0.2910 0.0578  -0.0397 -0.1145 794  LEU A CB  
5821  C CG  . LEU A 796  ? 0.2775 0.3327 0.2708 0.0599  -0.0371 -0.1144 794  LEU A CG  
5822  C CD1 . LEU A 796  ? 0.2975 0.3514 0.2852 0.0578  -0.0328 -0.1054 794  LEU A CD1 
5823  C CD2 . LEU A 796  ? 0.3079 0.3754 0.2964 0.0637  -0.0376 -0.1198 794  LEU A CD2 
5824  N N   . ALA A 797  ? 0.3273 0.3649 0.3421 0.0550  -0.0486 -0.1218 795  ALA A N   
5825  C CA  . ALA A 797  ? 0.3429 0.3778 0.3603 0.0530  -0.0505 -0.1208 795  ALA A CA  
5826  C C   . ALA A 797  ? 0.3937 0.4345 0.4130 0.0557  -0.0543 -0.1290 795  ALA A C   
5827  O O   . ALA A 797  ? 0.4879 0.5297 0.5068 0.0548  -0.0555 -0.1285 795  ALA A O   
5828  C CB  . ALA A 797  ? 0.3681 0.3925 0.3940 0.0496  -0.0520 -0.1182 795  ALA A CB  
5829  N N   . ASP A 798  ? 0.4095 0.4546 0.4308 0.0590  -0.0563 -0.1367 796  ASP A N   
5830  C CA  . ASP A 798  ? 0.4452 0.4973 0.4676 0.0621  -0.0598 -0.1452 796  ASP A CA  
5831  C C   . ASP A 798  ? 0.4922 0.5556 0.5047 0.0642  -0.0578 -0.1449 796  ASP A C   
5832  O O   . ASP A 798  ? 0.4470 0.5167 0.4593 0.0663  -0.0604 -0.1505 796  ASP A O   
5833  C CB  . ASP A 798  ? 0.3703 0.4247 0.3976 0.0654  -0.0623 -0.1537 796  ASP A CB  
5834  C CG  . ASP A 798  ? 0.5633 0.6074 0.6018 0.0637  -0.0653 -0.1552 796  ASP A CG  
5835  O OD1 . ASP A 798  ? 0.5746 0.6116 0.6185 0.0607  -0.0670 -0.1525 796  ASP A OD1 
5836  O OD2 . ASP A 798  ? 0.6188 0.6620 0.6609 0.0654  -0.0659 -0.1590 796  ASP A OD2 
5837  N N   . ARG A 799  ? 0.3890 0.4550 0.3937 0.0638  -0.0533 -0.1383 797  ARG A N   
5838  C CA  . ARG A 799  ? 0.3685 0.4464 0.3643 0.0664  -0.0512 -0.1384 797  ARG A CA  
5839  C C   . ARG A 799  ? 0.3445 0.4241 0.3340 0.0645  -0.0489 -0.1310 797  ARG A C   
5840  O O   . ARG A 799  ? 0.3331 0.4049 0.3232 0.0611  -0.0471 -0.1238 797  ARG A O   
5841  C CB  . ARG A 799  ? 0.4562 0.5365 0.4482 0.0675  -0.0479 -0.1362 797  ARG A CB  
5842  C CG  . ARG A 799  ? 0.4630 0.5390 0.4619 0.0686  -0.0498 -0.1418 797  ARG A CG  
5843  C CD  . ARG A 799  ? 0.4942 0.5797 0.4936 0.0731  -0.0524 -0.1518 797  ARG A CD  
5844  N NE  . ARG A 799  ? 0.5189 0.6166 0.5089 0.0755  -0.0495 -0.1507 797  ARG A NE  
5845  C CZ  . ARG A 799  ? 0.4645 0.5651 0.4504 0.0761  -0.0461 -0.1476 797  ARG A CZ  
5846  N NH1 . ARG A 799  ? 0.5336 0.6258 0.5236 0.0747  -0.0451 -0.1454 797  ARG A NH1 
5847  N NH2 . ARG A 799  ? 0.5533 0.6658 0.5309 0.0782  -0.0436 -0.1463 797  ARG A NH2 
5848  N N   . LEU A 800  ? 0.3277 0.4181 0.3115 0.0668  -0.0491 -0.1329 798  LEU A N   
5849  C CA  . LEU A 800  ? 0.3467 0.4410 0.3237 0.0655  -0.0466 -0.1257 798  LEU A CA  
5850  C C   . LEU A 800  ? 0.3088 0.4160 0.2779 0.0685  -0.0446 -0.1258 798  LEU A C   
5851  O O   . LEU A 800  ? 0.3660 0.4811 0.3348 0.0719  -0.0462 -0.1332 798  LEU A O   
5852  C CB  . LEU A 800  ? 0.3381 0.4333 0.3163 0.0650  -0.0493 -0.1270 798  LEU A CB  
5853  C CG  . LEU A 800  ? 0.3520 0.4356 0.3376 0.0617  -0.0511 -0.1257 798  LEU A CG  
5854  C CD1 . LEU A 800  ? 0.3680 0.4543 0.3548 0.0618  -0.0542 -0.1286 798  LEU A CD1 
5855  C CD2 . LEU A 800  ? 0.3469 0.4233 0.3310 0.0582  -0.0476 -0.1162 798  LEU A CD2 
5856  N N   . SER A 801  ? 0.3386 0.4482 0.3017 0.0672  -0.0412 -0.1175 799  SER A N   
5857  C CA  . SER A 801  ? 0.3543 0.4766 0.3098 0.0695  -0.0393 -0.1161 799  SER A CA  
5858  C C   . SER A 801  ? 0.4150 0.5472 0.3682 0.0717  -0.0419 -0.1206 799  SER A C   
5859  O O   . SER A 801  ? 0.3930 0.5212 0.3503 0.0709  -0.0449 -0.1235 799  SER A O   
5860  C CB  . SER A 801  ? 0.3857 0.5072 0.3367 0.0671  -0.0357 -0.1056 799  SER A CB  
5861  O OG  . SER A 801  ? 0.3710 0.4906 0.3220 0.0653  -0.0366 -0.1022 799  SER A OG  
5862  N N   . PRO A 802  ? 0.3509 0.4967 0.2978 0.0745  -0.0410 -0.1213 800  PRO A N   
5863  C CA  . PRO A 802  ? 0.3917 0.5479 0.3355 0.0763  -0.0432 -0.1245 800  PRO A CA  
5864  C C   . PRO A 802  ? 0.4170 0.5699 0.3602 0.0737  -0.0433 -0.1181 800  PRO A C   
5865  O O   . PRO A 802  ? 0.4706 0.6274 0.4141 0.0745  -0.0462 -0.1218 800  PRO A O   
5866  C CB  . PRO A 802  ? 0.4344 0.6055 0.3709 0.0791  -0.0411 -0.1235 800  PRO A CB  
5867  C CG  . PRO A 802  ? 0.4297 0.5987 0.3676 0.0799  -0.0394 -0.1251 800  PRO A CG  
5868  C CD  . PRO A 802  ? 0.3604 0.5136 0.3031 0.0763  -0.0383 -0.1204 800  PRO A CD  
5869  N N   . ALA A 803  ? 0.4226 0.5686 0.3650 0.0706  -0.0404 -0.1089 801  ALA A N   
5870  C CA  . ALA A 803  ? 0.4655 0.6068 0.4083 0.0680  -0.0405 -0.1030 801  ALA A CA  
5871  C C   . ALA A 803  ? 0.4918 0.6206 0.4418 0.0657  -0.0427 -0.1054 801  ALA A C   
5872  O O   . ALA A 803  ? 0.4732 0.5974 0.4243 0.0634  -0.0428 -0.1009 801  ALA A O   
5873  C CB  . ALA A 803  ? 0.4982 0.6368 0.4382 0.0657  -0.0367 -0.0927 801  ALA A CB  
5874  N N   . GLY A 804  ? 0.4524 0.5758 0.4077 0.0663  -0.0444 -0.1119 802  GLY A N   
5875  C CA  . GLY A 804  ? 0.3558 0.4676 0.3185 0.0640  -0.0465 -0.1138 802  GLY A CA  
5876  C C   . GLY A 804  ? 0.3870 0.4872 0.3523 0.0604  -0.0441 -0.1068 802  GLY A C   
5877  O O   . GLY A 804  ? 0.4027 0.4951 0.3723 0.0579  -0.0451 -0.1051 802  GLY A O   
5878  N N   . ARG A 805  ? 0.3772 0.4763 0.3401 0.0602  -0.0409 -0.1028 803  ARG A N   
5879  C CA  . ARG A 805  ? 0.3863 0.4753 0.3513 0.0569  -0.0385 -0.0962 803  ARG A CA  
5880  C C   . ARG A 805  ? 0.2981 0.3822 0.2657 0.0571  -0.0377 -0.0982 803  ARG A C   
5881  O O   . ARG A 805  ? 0.3050 0.3952 0.2715 0.0599  -0.0382 -0.1033 803  ARG A O   
5882  C CB  . ARG A 805  ? 0.4066 0.4984 0.3659 0.0560  -0.0351 -0.0877 803  ARG A CB  
5883  C CG  . ARG A 805  ? 0.3912 0.4874 0.3482 0.0556  -0.0359 -0.0849 803  ARG A CG  
5884  C CD  . ARG A 805  ? 0.4037 0.4916 0.3662 0.0533  -0.0378 -0.0852 803  ARG A CD  
5885  N NE  . ARG A 805  ? 0.3593 0.4515 0.3199 0.0531  -0.0388 -0.0830 803  ARG A NE  
5886  C CZ  . ARG A 805  ? 0.4303 0.5275 0.3914 0.0545  -0.0419 -0.0882 803  ARG A CZ  
5887  N NH1 . ARG A 805  ? 0.4212 0.5196 0.3852 0.0563  -0.0445 -0.0963 803  ARG A NH1 
5888  N NH2 . ARG A 805  ? 0.5297 0.6309 0.4890 0.0542  -0.0424 -0.0853 803  ARG A NH2 
5889  N N   . PRO A 806  ? 0.3316 0.4052 0.3032 0.0543  -0.0367 -0.0946 804  PRO A N   
5890  C CA  . PRO A 806  ? 0.3058 0.3745 0.2807 0.0543  -0.0362 -0.0964 804  PRO A CA  
5891  C C   . PRO A 806  ? 0.2820 0.3565 0.2517 0.0559  -0.0333 -0.0945 804  PRO A C   
5892  O O   . PRO A 806  ? 0.2933 0.3718 0.2576 0.0556  -0.0307 -0.0886 804  PRO A O   
5893  C CB  . PRO A 806  ? 0.3057 0.3634 0.2843 0.0506  -0.0350 -0.0910 804  PRO A CB  
5894  C CG  . PRO A 806  ? 0.3322 0.3883 0.3123 0.0490  -0.0365 -0.0897 804  PRO A CG  
5895  C CD  . PRO A 806  ? 0.3303 0.3963 0.3044 0.0509  -0.0363 -0.0893 804  PRO A CD  
5896  N N   . ILE A 807  ? 0.2587 0.3335 0.2304 0.0577  -0.0339 -0.0995 805  ILE A N   
5897  C CA  . ILE A 807  ? 0.2653 0.3448 0.2331 0.0592  -0.0312 -0.0981 805  ILE A CA  
5898  C C   . ILE A 807  ? 0.2515 0.3228 0.2200 0.0563  -0.0284 -0.0911 805  ILE A C   
5899  O O   . ILE A 807  ? 0.2696 0.3317 0.2436 0.0545  -0.0292 -0.0916 805  ILE A O   
5900  C CB  . ILE A 807  ? 0.2663 0.3483 0.2371 0.0620  -0.0330 -0.1060 805  ILE A CB  
5901  C CG1 . ILE A 807  ? 0.3110 0.4012 0.2817 0.0650  -0.0362 -0.1139 805  ILE A CG1 
5902  C CG2 . ILE A 807  ? 0.2921 0.3791 0.2588 0.0634  -0.0301 -0.1043 805  ILE A CG2 
5903  C CD1 . ILE A 807  ? 0.3559 0.4587 0.3190 0.0670  -0.0349 -0.1126 805  ILE A CD1 
5904  N N   . PRO A 808  ? 0.2501 0.3243 0.2134 0.0556  -0.0252 -0.0844 806  PRO A N   
5905  C CA  . PRO A 808  ? 0.2356 0.3021 0.1997 0.0529  -0.0226 -0.0779 806  PRO A CA  
5906  C C   . PRO A 808  ? 0.2412 0.3038 0.2081 0.0533  -0.0222 -0.0801 806  PRO A C   
5907  O O   . PRO A 808  ? 0.2480 0.3168 0.2135 0.0560  -0.0221 -0.0840 806  PRO A O   
5908  C CB  . PRO A 808  ? 0.2633 0.3361 0.2214 0.0530  -0.0197 -0.0716 806  PRO A CB  
5909  C CG  . PRO A 808  ? 0.2870 0.3684 0.2418 0.0546  -0.0210 -0.0731 806  PRO A CG  
5910  C CD  . PRO A 808  ? 0.2643 0.3490 0.2212 0.0572  -0.0240 -0.0820 806  PRO A CD  
5911  N N   . LEU A 809  ? 0.2411 0.2938 0.2122 0.0506  -0.0219 -0.0775 807  LEU A N   
5912  C CA  . LEU A 809  ? 0.2507 0.2985 0.2249 0.0504  -0.0214 -0.0784 807  LEU A CA  
5913  C C   . LEU A 809  ? 0.2546 0.2969 0.2279 0.0477  -0.0185 -0.0709 807  LEU A C   
5914  O O   . LEU A 809  ? 0.2569 0.2933 0.2318 0.0450  -0.0184 -0.0674 807  LEU A O   
5915  C CB  . LEU A 809  ? 0.2614 0.3022 0.2429 0.0497  -0.0245 -0.0829 807  LEU A CB  
5916  C CG  . LEU A 809  ? 0.2569 0.2913 0.2427 0.0489  -0.0243 -0.0830 807  LEU A CG  
5917  C CD1 . LEU A 809  ? 0.2552 0.2955 0.2395 0.0519  -0.0238 -0.0868 807  LEU A CD1 
5918  C CD2 . LEU A 809  ? 0.3006 0.3280 0.2942 0.0477  -0.0276 -0.0865 807  LEU A CD2 
5919  N N   . ILE A 810  ? 0.2262 0.2708 0.1969 0.0483  -0.0161 -0.0687 808  ILE A N   
5920  C CA  . ILE A 810  ? 0.2342 0.2728 0.2054 0.0460  -0.0138 -0.0630 808  ILE A CA  
5921  C C   . ILE A 810  ? 0.2188 0.2523 0.1947 0.0460  -0.0147 -0.0661 808  ILE A C   
5922  O O   . ILE A 810  ? 0.2457 0.2833 0.2214 0.0485  -0.0150 -0.0702 808  ILE A O   
5923  C CB  . ILE A 810  ? 0.2161 0.2600 0.1821 0.0466  -0.0107 -0.0584 808  ILE A CB  
5924  C CG1 . ILE A 810  ? 0.2383 0.2885 0.2001 0.0468  -0.0101 -0.0554 808  ILE A CG1 
5925  C CG2 . ILE A 810  ? 0.2619 0.2992 0.2289 0.0440  -0.0086 -0.0528 808  ILE A CG2 
5926  C CD1 . ILE A 810  ? 0.2803 0.3350 0.2380 0.0468  -0.0072 -0.0496 808  ILE A CD1 
5927  N N   . ALA A 811  ? 0.2245 0.2494 0.2047 0.0434  -0.0153 -0.0643 809  ALA A N   
5928  C CA  . ALA A 811  ? 0.2179 0.2374 0.2034 0.0431  -0.0166 -0.0669 809  ALA A CA  
5929  C C   . ALA A 811  ? 0.2412 0.2546 0.2274 0.0403  -0.0145 -0.0610 809  ALA A C   
5930  O O   . ALA A 811  ? 0.2329 0.2411 0.2209 0.0377  -0.0146 -0.0579 809  ALA A O   
5931  C CB  . ALA A 811  ? 0.2524 0.2679 0.2439 0.0426  -0.0200 -0.0711 809  ALA A CB  
5932  N N   . GLU A 812  ? 0.2072 0.2216 0.1919 0.0410  -0.0126 -0.0597 810  GLU A N   
5933  C CA  . GLU A 812  ? 0.2083 0.2179 0.1930 0.0387  -0.0105 -0.0543 810  GLU A CA  
5934  C C   . GLU A 812  ? 0.2270 0.2318 0.2170 0.0385  -0.0118 -0.0564 810  GLU A C   
5935  O O   . GLU A 812  ? 0.2323 0.2399 0.2229 0.0408  -0.0122 -0.0600 810  GLU A O   
5936  C CB  . GLU A 812  ? 0.2531 0.2676 0.2326 0.0396  -0.0075 -0.0509 810  GLU A CB  
5937  C CG  . GLU A 812  ? 0.2466 0.2658 0.2216 0.0397  -0.0066 -0.0485 810  GLU A CG  
5938  C CD  . GLU A 812  ? 0.3066 0.3208 0.2826 0.0369  -0.0066 -0.0449 810  GLU A CD  
5939  O OE1 . GLU A 812  ? 0.2696 0.2807 0.2452 0.0350  -0.0048 -0.0401 810  GLU A OE1 
5940  O OE2 . GLU A 812  ? 0.2718 0.2853 0.2493 0.0367  -0.0086 -0.0471 810  GLU A OE2 
5941  N N   . THR A 813  ? 0.2254 0.2234 0.2194 0.0358  -0.0125 -0.0541 811  THR A N   
5942  C CA  . THR A 813  ? 0.2164 0.2098 0.2168 0.0354  -0.0147 -0.0566 811  THR A CA  
5943  C C   . THR A 813  ? 0.2403 0.2284 0.2424 0.0330  -0.0135 -0.0520 811  THR A C   
5944  O O   . THR A 813  ? 0.2450 0.2339 0.2430 0.0324  -0.0107 -0.0479 811  THR A O   
5945  C CB  . THR A 813  ? 0.2233 0.2143 0.2285 0.0349  -0.0180 -0.0597 811  THR A CB  
5946  O OG1 . THR A 813  ? 0.2548 0.2441 0.2589 0.0325  -0.0174 -0.0559 811  THR A OG1 
5947  C CG2 . THR A 813  ? 0.2405 0.2372 0.2447 0.0379  -0.0196 -0.0656 811  THR A CG2 
5948  N N   . GLY A 814  ? 0.2405 0.2234 0.2489 0.0316  -0.0156 -0.0524 812  GLY A N   
5949  C CA  . GLY A 814  ? 0.2518 0.2305 0.2624 0.0298  -0.0148 -0.0488 812  GLY A CA  
5950  C C   . GLY A 814  ? 0.2491 0.2252 0.2580 0.0267  -0.0131 -0.0429 812  GLY A C   
5951  O O   . GLY A 814  ? 0.2503 0.2274 0.2569 0.0258  -0.0125 -0.0416 812  GLY A O   
5952  N N   . GLY A 815  ? 0.2449 0.2181 0.2552 0.0251  -0.0122 -0.0396 813  GLY A N   
5953  C CA  . GLY A 815  ? 0.2532 0.2243 0.2623 0.0222  -0.0106 -0.0344 813  GLY A CA  
5954  C C   . GLY A 815  ? 0.2329 0.1997 0.2475 0.0201  -0.0119 -0.0322 813  GLY A C   
5955  O O   . GLY A 815  ? 0.2631 0.2282 0.2821 0.0208  -0.0137 -0.0343 813  GLY A O   
5956  N N   . GLN A 816  ? 0.2277 0.1931 0.2424 0.0173  -0.0112 -0.0281 814  GLN A N   
5957  C CA  . GLN A 816  ? 0.2354 0.1977 0.2541 0.0149  -0.0117 -0.0248 814  GLN A CA  
5958  C C   . GLN A 816  ? 0.2147 0.1779 0.2291 0.0134  -0.0089 -0.0205 814  GLN A C   
5959  O O   . GLN A 816  ? 0.2437 0.2069 0.2583 0.0111  -0.0085 -0.0176 814  GLN A O   
5960  C CB  . GLN A 816  ? 0.2335 0.1939 0.2579 0.0130  -0.0142 -0.0242 814  GLN A CB  
5961  C CG  . GLN A 816  ? 0.2750 0.2327 0.3047 0.0106  -0.0154 -0.0208 814  GLN A CG  
5962  C CD  . GLN A 816  ? 0.2952 0.2508 0.3294 0.0119  -0.0172 -0.0229 814  GLN A CD  
5963  O OE1 . GLN A 816  ? 0.2958 0.2518 0.3276 0.0131  -0.0158 -0.0230 814  GLN A OE1 
5964  N NE2 . GLN A 816  ? 0.3259 0.2793 0.3672 0.0118  -0.0206 -0.0248 814  GLN A NE2 
5965  N N   . ASN A 817  ? 0.2137 0.1782 0.2243 0.0147  -0.0069 -0.0203 815  ASN A N   
5966  C CA  . ASN A 817  ? 0.2040 0.1701 0.2097 0.0140  -0.0042 -0.0175 815  ASN A CA  
5967  C C   . ASN A 817  ? 0.2133 0.1782 0.2202 0.0117  -0.0035 -0.0136 815  ASN A C   
5968  O O   . ASN A 817  ? 0.2105 0.1737 0.2199 0.0115  -0.0041 -0.0129 815  ASN A O   
5969  C CB  . ASN A 817  ? 0.1998 0.1681 0.2016 0.0163  -0.0026 -0.0187 815  ASN A CB  
5970  C CG  . ASN A 817  ? 0.1927 0.1632 0.1936 0.0189  -0.0035 -0.0227 815  ASN A CG  
5971  O OD1 . ASN A 817  ? 0.2034 0.1752 0.2034 0.0190  -0.0039 -0.0237 815  ASN A OD1 
5972  N ND2 . ASN A 817  ? 0.2075 0.1790 0.2089 0.0210  -0.0038 -0.0252 815  ASN A ND2 
5973  N N   . ALA A 818  ? 0.1947 0.1605 0.1997 0.0100  -0.0023 -0.0111 816  ALA A N   
5974  C CA  . ALA A 818  ? 0.2087 0.1743 0.2144 0.0077  -0.0016 -0.0076 816  ALA A CA  
5975  C C   . ALA A 818  ? 0.1795 0.1466 0.1808 0.0079  0.0009  -0.0062 816  ALA A C   
5976  O O   . ALA A 818  ? 0.1918 0.1604 0.1898 0.0093  0.0021  -0.0073 816  ALA A O   
5977  C CB  . ALA A 818  ? 0.1961 0.1624 0.2036 0.0056  -0.0022 -0.0060 816  ALA A CB  
5978  N N   . MET A 819  ? 0.1991 0.1661 0.2009 0.0065  0.0015  -0.0036 817  MET A N   
5979  C CA  . MET A 819  ? 0.1870 0.1556 0.1857 0.0062  0.0036  -0.0021 817  MET A CA  
5980  C C   . MET A 819  ? 0.2066 0.1763 0.2065 0.0037  0.0036  0.0006  817  MET A C   
5981  O O   . MET A 819  ? 0.2104 0.1795 0.2134 0.0024  0.0025  0.0022  817  MET A O   
5982  C CB  . MET A 819  ? 0.2000 0.1680 0.1976 0.0072  0.0044  -0.0018 817  MET A CB  
5983  C CG  . MET A 819  ? 0.2054 0.1749 0.2006 0.0067  0.0062  -0.0002 817  MET A CG  
5984  S SD  . MET A 819  ? 0.2358 0.2047 0.2305 0.0075  0.0070  0.0006  817  MET A SD  
5985  C CE  . MET A 819  ? 0.2707 0.2399 0.2635 0.0103  0.0075  -0.0018 817  MET A CE  
5986  N N   . ILE A 820  ? 0.1953 0.1672 0.1932 0.0031  0.0048  0.0010  818  ILE A N   
5987  C CA  . ILE A 820  ? 0.1902 0.1644 0.1888 0.0010  0.0052  0.0032  818  ILE A CA  
5988  C C   . ILE A 820  ? 0.1891 0.1646 0.1856 0.0010  0.0067  0.0040  818  ILE A C   
5989  O O   . ILE A 820  ? 0.2028 0.1783 0.1970 0.0023  0.0078  0.0028  818  ILE A O   
5990  C CB  . ILE A 820  ? 0.1944 0.1707 0.1928 0.0003  0.0053  0.0028  818  ILE A CB  
5991  C CG1 . ILE A 820  ? 0.2221 0.1971 0.2232 0.0001  0.0035  0.0022  818  ILE A CG1 
5992  C CG2 . ILE A 820  ? 0.2147 0.1945 0.2134 -0.0017 0.0059  0.0048  818  ILE A CG2 
5993  C CD1 . ILE A 820  ? 0.2086 0.1856 0.2100 -0.0005 0.0034  0.0018  818  ILE A CD1 
5994  N N   . VAL A 821  ? 0.2097 0.1864 0.2073 -0.0006 0.0066  0.0062  819  VAL A N   
5995  C CA  . VAL A 821  ? 0.2192 0.1972 0.2151 -0.0007 0.0078  0.0069  819  VAL A CA  
5996  C C   . VAL A 821  ? 0.2201 0.2022 0.2163 -0.0026 0.0081  0.0084  819  VAL A C   
5997  O O   . VAL A 821  ? 0.2477 0.2310 0.2462 -0.0043 0.0071  0.0105  819  VAL A O   
5998  C CB  . VAL A 821  ? 0.2057 0.1818 0.2026 -0.0005 0.0073  0.0080  819  VAL A CB  
5999  C CG1 . VAL A 821  ? 0.2326 0.2104 0.2280 -0.0007 0.0084  0.0087  819  VAL A CG1 
6000  C CG2 . VAL A 821  ? 0.2214 0.1944 0.2182 0.0015  0.0070  0.0062  819  VAL A CG2 
6001  N N   . ASP A 822  ? 0.2179 0.2024 0.2123 -0.0024 0.0093  0.0075  820  ASP A N   
6002  C CA  . ASP A 822  ? 0.2176 0.2070 0.2121 -0.0041 0.0096  0.0085  820  ASP A CA  
6003  C C   . ASP A 822  ? 0.2314 0.2225 0.2251 -0.0044 0.0102  0.0092  820  ASP A C   
6004  O O   . ASP A 822  ? 0.2338 0.2220 0.2271 -0.0034 0.0102  0.0091  820  ASP A O   
6005  C CB  . ASP A 822  ? 0.2366 0.2285 0.2304 -0.0038 0.0103  0.0067  820  ASP A CB  
6006  C CG  . ASP A 822  ? 0.2168 0.2086 0.2091 -0.0023 0.0113  0.0044  820  ASP A CG  
6007  O OD1 . ASP A 822  ? 0.2287 0.2192 0.2204 -0.0017 0.0116  0.0044  820  ASP A OD1 
6008  O OD2 . ASP A 822  ? 0.2421 0.2352 0.2343 -0.0018 0.0116  0.0027  820  ASP A OD2 
6009  N N   . SER A 823  ? 0.2322 0.2284 0.2257 -0.0058 0.0105  0.0099  821  SER A N   
6010  C CA  . SER A 823  ? 0.2427 0.2413 0.2356 -0.0062 0.0108  0.0106  821  SER A CA  
6011  C C   . SER A 823  ? 0.2785 0.2766 0.2700 -0.0047 0.0117  0.0080  821  SER A C   
6012  O O   . SER A 823  ? 0.2939 0.2938 0.2851 -0.0049 0.0119  0.0082  821  SER A O   
6013  C CB  . SER A 823  ? 0.2839 0.2893 0.2770 -0.0081 0.0109  0.0121  821  SER A CB  
6014  O OG  . SER A 823  ? 0.3150 0.3239 0.3076 -0.0079 0.0116  0.0101  821  SER A OG  
6015  N N   . SER A 824  ? 0.2362 0.2322 0.2275 -0.0032 0.0121  0.0057  822  SER A N   
6016  C CA  . SER A 824  ? 0.2326 0.2277 0.2235 -0.0019 0.0127  0.0036  822  SER A CA  
6017  C C   . SER A 824  ? 0.2591 0.2493 0.2499 -0.0006 0.0127  0.0039  822  SER A C   
6018  O O   . SER A 824  ? 0.2587 0.2481 0.2497 0.0003  0.0130  0.0029  822  SER A O   
6019  C CB  . SER A 824  ? 0.2200 0.2157 0.2112 -0.0009 0.0130  0.0012  822  SER A CB  
6020  O OG  . SER A 824  ? 0.2256 0.2175 0.2168 0.0000  0.0128  0.0012  822  SER A OG  
6021  N N   . ALA A 825  ? 0.2585 0.2457 0.2494 -0.0005 0.0122  0.0053  823  ALA A N   
6022  C CA  . ALA A 825  ? 0.2608 0.2441 0.2516 0.0008  0.0122  0.0054  823  ALA A CA  
6023  C C   . ALA A 825  ? 0.2444 0.2275 0.2354 0.0005  0.0122  0.0066  823  ALA A C   
6024  O O   . ALA A 825  ? 0.2769 0.2624 0.2682 -0.0009 0.0119  0.0079  823  ALA A O   
6025  C CB  . ALA A 825  ? 0.2448 0.2256 0.2361 0.0010  0.0115  0.0060  823  ALA A CB  
6026  N N   . LEU A 826  ? 0.2655 0.2463 0.2565 0.0018  0.0126  0.0064  824  LEU A N   
6027  C CA  . LEU A 826  ? 0.2815 0.2619 0.2728 0.0017  0.0126  0.0074  824  LEU A CA  
6028  C C   . LEU A 826  ? 0.2976 0.2758 0.2895 0.0017  0.0119  0.0087  824  LEU A C   
6029  O O   . LEU A 826  ? 0.2713 0.2472 0.2632 0.0030  0.0120  0.0082  824  LEU A O   
6030  C CB  . LEU A 826  ? 0.3279 0.3072 0.3195 0.0029  0.0132  0.0067  824  LEU A CB  
6031  C CG  . LEU A 826  ? 0.4262 0.4054 0.4184 0.0028  0.0132  0.0077  824  LEU A CG  
6032  C CD1 . LEU A 826  ? 0.4477 0.4301 0.4401 0.0014  0.0129  0.0076  824  LEU A CD1 
6033  C CD2 . LEU A 826  ? 0.4955 0.4736 0.4885 0.0041  0.0137  0.0073  824  LEU A CD2 
6034  N N   . ALA A 827  ? 0.2691 0.2484 0.2619 0.0004  0.0113  0.0104  825  ALA A N   
6035  C CA  . ALA A 827  ? 0.2606 0.2380 0.2549 0.0004  0.0104  0.0117  825  ALA A CA  
6036  C C   . ALA A 827  ? 0.2583 0.2327 0.2528 0.0021  0.0106  0.0111  825  ALA A C   
6037  O O   . ALA A 827  ? 0.2477 0.2201 0.2431 0.0030  0.0100  0.0106  825  ALA A O   
6038  C CB  . ALA A 827  ? 0.2849 0.2641 0.2804 -0.0013 0.0096  0.0140  825  ALA A CB  
6039  N N   . GLU A 828  ? 0.2632 0.2379 0.2573 0.0026  0.0113  0.0111  826  GLU A N   
6040  C CA  . GLU A 828  ? 0.2843 0.2571 0.2787 0.0042  0.0116  0.0108  826  GLU A CA  
6041  C C   . GLU A 828  ? 0.2653 0.2372 0.2589 0.0058  0.0121  0.0093  826  GLU A C   
6042  O O   . GLU A 828  ? 0.2611 0.2318 0.2551 0.0071  0.0119  0.0088  826  GLU A O   
6043  C CB  . GLU A 828  ? 0.3035 0.2771 0.2978 0.0044  0.0123  0.0112  826  GLU A CB  
6044  C CG  . GLU A 828  ? 0.3777 0.3523 0.3731 0.0031  0.0118  0.0128  826  GLU A CG  
6045  C CD  . GLU A 828  ? 0.4589 0.4363 0.4539 0.0014  0.0115  0.0132  826  GLU A CD  
6046  O OE1 . GLU A 828  ? 0.4135 0.3921 0.4075 0.0012  0.0117  0.0121  826  GLU A OE1 
6047  O OE2 . GLU A 828  ? 0.5440 0.5228 0.5396 0.0003  0.0109  0.0147  826  GLU A OE2 
6048  N N   . GLN A 829  ? 0.2652 0.2379 0.2575 0.0058  0.0126  0.0085  827  GLN A N   
6049  C CA  . GLN A 829  ? 0.2695 0.2418 0.2609 0.0072  0.0130  0.0073  827  GLN A CA  
6050  C C   . GLN A 829  ? 0.2444 0.2158 0.2360 0.0074  0.0121  0.0065  827  GLN A C   
6051  O O   . GLN A 829  ? 0.2448 0.2156 0.2362 0.0088  0.0121  0.0055  827  GLN A O   
6052  C CB  . GLN A 829  ? 0.3129 0.2864 0.3037 0.0069  0.0135  0.0068  827  GLN A CB  
6053  C CG  . GLN A 829  ? 0.3759 0.3493 0.3658 0.0083  0.0139  0.0061  827  GLN A CG  
6054  C CD  . GLN A 829  ? 0.4309 0.4052 0.4209 0.0081  0.0142  0.0057  827  GLN A CD  
6055  O OE1 . GLN A 829  ? 0.4978 0.4724 0.4877 0.0091  0.0145  0.0056  827  GLN A OE1 
6056  N NE2 . GLN A 829  ? 0.3456 0.3209 0.3362 0.0068  0.0140  0.0055  827  GLN A NE2 
6057  N N   . VAL A 830  ? 0.2449 0.2167 0.2372 0.0058  0.0114  0.0069  828  VAL A N   
6058  C CA  . VAL A 830  ? 0.2422 0.2130 0.2355 0.0057  0.0103  0.0063  828  VAL A CA  
6059  C C   . VAL A 830  ? 0.2313 0.2004 0.2262 0.0066  0.0094  0.0061  828  VAL A C   
6060  O O   . VAL A 830  ? 0.2191 0.1872 0.2144 0.0079  0.0089  0.0045  828  VAL A O   
6061  C CB  . VAL A 830  ? 0.2230 0.1949 0.2173 0.0036  0.0096  0.0075  828  VAL A CB  
6062  C CG1 . VAL A 830  ? 0.2434 0.2141 0.2398 0.0033  0.0081  0.0075  828  VAL A CG1 
6063  C CG2 . VAL A 830  ? 0.2689 0.2429 0.2618 0.0031  0.0103  0.0070  828  VAL A CG2 
6064  N N   . VAL A 831  ? 0.2218 0.1907 0.2180 0.0060  0.0092  0.0076  829  VAL A N   
6065  C CA  . VAL A 831  ? 0.2095 0.1767 0.2080 0.0067  0.0082  0.0074  829  VAL A CA  
6066  C C   . VAL A 831  ? 0.2203 0.1873 0.2180 0.0091  0.0089  0.0055  829  VAL A C   
6067  O O   . VAL A 831  ? 0.2151 0.1812 0.2143 0.0103  0.0079  0.0038  829  VAL A O   
6068  C CB  . VAL A 831  ? 0.2178 0.1851 0.2179 0.0056  0.0079  0.0095  829  VAL A CB  
6069  C CG1 . VAL A 831  ? 0.2316 0.1972 0.2343 0.0067  0.0069  0.0091  829  VAL A CG1 
6070  C CG2 . VAL A 831  ? 0.2460 0.2141 0.2474 0.0033  0.0069  0.0116  829  VAL A CG2 
6071  N N   . GLY A 832  ? 0.2100 0.1782 0.2056 0.0097  0.0104  0.0057  830  GLY A N   
6072  C CA  . GLY A 832  ? 0.2064 0.1755 0.2011 0.0119  0.0111  0.0044  830  GLY A CA  
6073  C C   . GLY A 832  ? 0.2076 0.1771 0.2013 0.0130  0.0108  0.0024  830  GLY A C   
6074  O O   . GLY A 832  ? 0.2226 0.1925 0.2168 0.0148  0.0105  0.0006  830  GLY A O   
6075  N N   . ASP A 833  ? 0.2083 0.1780 0.2009 0.0121  0.0109  0.0025  831  ASP A N   
6076  C CA  . ASP A 833  ? 0.1974 0.1677 0.1890 0.0132  0.0106  0.0007  831  ASP A CA  
6077  C C   . ASP A 833  ? 0.2143 0.1832 0.2081 0.0132  0.0089  -0.0009 831  ASP A C   
6078  O O   . ASP A 833  ? 0.2088 0.1783 0.2024 0.0148  0.0084  -0.0032 831  ASP A O   
6079  C CB  . ASP A 833  ? 0.2202 0.1910 0.2104 0.0121  0.0111  0.0013  831  ASP A CB  
6080  C CG  . ASP A 833  ? 0.2176 0.1899 0.2063 0.0125  0.0125  0.0023  831  ASP A CG  
6081  O OD1 . ASP A 833  ? 0.2672 0.2405 0.2556 0.0137  0.0132  0.0027  831  ASP A OD1 
6082  O OD2 . ASP A 833  ? 0.2378 0.2104 0.2260 0.0116  0.0128  0.0029  831  ASP A OD2 
6083  N N   . VAL A 834  ? 0.2032 0.1704 0.1993 0.0116  0.0079  0.0002  832  VAL A N   
6084  C CA  . VAL A 834  ? 0.2212 0.1867 0.2205 0.0114  0.0059  -0.0009 832  VAL A CA  
6085  C C   . VAL A 834  ? 0.2139 0.1788 0.2153 0.0132  0.0052  -0.0026 832  VAL A C   
6086  O O   . VAL A 834  ? 0.2166 0.1812 0.2195 0.0146  0.0039  -0.0053 832  VAL A O   
6087  C CB  . VAL A 834  ? 0.2118 0.1763 0.2134 0.0089  0.0050  0.0016  832  VAL A CB  
6088  C CG1 . VAL A 834  ? 0.2268 0.1894 0.2330 0.0087  0.0027  0.0011  832  VAL A CG1 
6089  C CG2 . VAL A 834  ? 0.2306 0.1964 0.2306 0.0074  0.0055  0.0026  832  VAL A CG2 
6090  N N   . ILE A 835  ? 0.2192 0.1842 0.2208 0.0133  0.0058  -0.0014 833  ILE A N   
6091  C CA  . ILE A 835  ? 0.2170 0.1818 0.2208 0.0151  0.0052  -0.0031 833  ILE A CA  
6092  C C   . ILE A 835  ? 0.2146 0.1817 0.2164 0.0177  0.0059  -0.0060 833  ILE A C   
6093  O O   . ILE A 835  ? 0.2454 0.2126 0.2493 0.0194  0.0046  -0.0090 833  ILE A O   
6094  C CB  . ILE A 835  ? 0.2262 0.1912 0.2302 0.0148  0.0060  -0.0010 833  ILE A CB  
6095  C CG1 . ILE A 835  ? 0.2478 0.2108 0.2545 0.0125  0.0049  0.0016  833  ILE A CG1 
6096  C CG2 . ILE A 835  ? 0.2655 0.2312 0.2709 0.0171  0.0059  -0.0031 833  ILE A CG2 
6097  C CD1 . ILE A 835  ? 0.2760 0.2369 0.2878 0.0127  0.0025  0.0008  833  ILE A CD1 
6098  N N   . THR A 836  ? 0.2309 0.2002 0.2288 0.0180  0.0077  -0.0053 834  THR A N   
6099  C CA  . THR A 836  ? 0.2559 0.2283 0.2516 0.0202  0.0084  -0.0074 834  THR A CA  
6100  C C   . THR A 836  ? 0.2266 0.1990 0.2226 0.0208  0.0071  -0.0100 834  THR A C   
6101  O O   . THR A 836  ? 0.2381 0.2121 0.2348 0.0228  0.0063  -0.0132 834  THR A O   
6102  C CB  . THR A 836  ? 0.2884 0.2631 0.2807 0.0201  0.0104  -0.0053 834  THR A CB  
6103  O OG1 . THR A 836  ? 0.3433 0.3182 0.3358 0.0198  0.0115  -0.0033 834  THR A OG1 
6104  C CG2 . THR A 836  ? 0.3074 0.2859 0.2973 0.0222  0.0111  -0.0069 834  THR A CG2 
6105  N N   . SER A 837  ? 0.2229 0.1938 0.2186 0.0190  0.0067  -0.0089 835  SER A N   
6106  C CA  . SER A 837  ? 0.2095 0.1806 0.2053 0.0194  0.0056  -0.0111 835  SER A CA  
6107  C C   . SER A 837  ? 0.2118 0.1809 0.2117 0.0199  0.0032  -0.0136 835  SER A C   
6108  O O   . SER A 837  ? 0.2284 0.1985 0.2288 0.0213  0.0022  -0.0168 835  SER A O   
6109  C CB  . SER A 837  ? 0.2341 0.2041 0.2289 0.0173  0.0057  -0.0092 835  SER A CB  
6110  O OG  . SER A 837  ? 0.2274 0.1993 0.2189 0.0172  0.0076  -0.0074 835  SER A OG  
6111  N N   . ALA A 838  ? 0.1982 0.1645 0.2016 0.0185  0.0022  -0.0122 836  ALA A N   
6112  C CA  . ALA A 838  ? 0.1984 0.1626 0.2070 0.0187  -0.0004 -0.0142 836  ALA A CA  
6113  C C   . ALA A 838  ? 0.2182 0.1830 0.2290 0.0211  -0.0011 -0.0173 836  ALA A C   
6114  O O   . ALA A 838  ? 0.2312 0.1953 0.2455 0.0223  -0.0032 -0.0207 836  ALA A O   
6115  C CB  . ALA A 838  ? 0.2307 0.1920 0.2427 0.0160  -0.0014 -0.0110 836  ALA A CB  
6116  N N   . PHE A 839  ? 0.2182 0.1844 0.2274 0.0219  0.0004  -0.0164 837  PHE A N   
6117  C CA  . PHE A 839  ? 0.2169 0.1834 0.2292 0.0239  -0.0004 -0.0189 837  PHE A CA  
6118  C C   . PHE A 839  ? 0.2371 0.2081 0.2461 0.0266  0.0013  -0.0210 837  PHE A C   
6119  O O   . PHE A 839  ? 0.2398 0.2120 0.2514 0.0287  0.0004  -0.0241 837  PHE A O   
6120  C CB  . PHE A 839  ? 0.2224 0.1865 0.2376 0.0225  -0.0007 -0.0160 837  PHE A CB  
6121  C CG  . PHE A 839  ? 0.2145 0.1750 0.2332 0.0198  -0.0024 -0.0134 837  PHE A CG  
6122  C CD1 . PHE A 839  ? 0.2257 0.1841 0.2493 0.0198  -0.0052 -0.0154 837  PHE A CD1 
6123  C CD2 . PHE A 839  ? 0.2259 0.1856 0.2431 0.0173  -0.0014 -0.0090 837  PHE A CD2 
6124  C CE1 . PHE A 839  ? 0.2398 0.1954 0.2669 0.0171  -0.0068 -0.0124 837  PHE A CE1 
6125  C CE2 . PHE A 839  ? 0.2776 0.2352 0.2979 0.0148  -0.0029 -0.0064 837  PHE A CE2 
6126  C CZ  . PHE A 839  ? 0.2433 0.1988 0.2686 0.0146  -0.0055 -0.0078 837  PHE A CZ  
6127  N N   . ASP A 840  ? 0.2385 0.2124 0.2424 0.0265  0.0035  -0.0195 838  ASP A N   
6128  C CA  . ASP A 840  ? 0.2477 0.2267 0.2486 0.0291  0.0049  -0.0213 838  ASP A CA  
6129  C C   . ASP A 840  ? 0.2504 0.2314 0.2527 0.0315  0.0033  -0.0264 838  ASP A C   
6130  O O   . ASP A 840  ? 0.2466 0.2258 0.2502 0.0309  0.0017  -0.0279 838  ASP A O   
6131  C CB  . ASP A 840  ? 0.2841 0.2655 0.2801 0.0284  0.0070  -0.0188 838  ASP A CB  
6132  C CG  . ASP A 840  ? 0.3482 0.3355 0.3410 0.0306  0.0086  -0.0196 838  ASP A CG  
6133  O OD1 . ASP A 840  ? 0.3347 0.3254 0.3264 0.0325  0.0081  -0.0227 838  ASP A OD1 
6134  O OD2 . ASP A 840  ? 0.4229 0.4119 0.4144 0.0305  0.0103  -0.0170 838  ASP A OD2 
6135  N N   . SER A 841  ? 0.2440 0.2291 0.2466 0.0341  0.0036  -0.0294 839  SER A N   
6136  C CA  . SER A 841  ? 0.2333 0.2212 0.2376 0.0368  0.0019  -0.0349 839  SER A CA  
6137  C C   . SER A 841  ? 0.2234 0.2062 0.2337 0.0364  -0.0012 -0.0375 839  SER A C   
6138  O O   . SER A 841  ? 0.2244 0.2079 0.2364 0.0377  -0.0031 -0.0416 839  SER A O   
6139  C CB  . SER A 841  ? 0.2769 0.2687 0.2768 0.0376  0.0025  -0.0360 839  SER A CB  
6140  O OG  . SER A 841  ? 0.3409 0.3372 0.3358 0.0377  0.0053  -0.0329 839  SER A OG  
6141  N N   . ALA A 842  ? 0.2368 0.2148 0.2508 0.0345  -0.0020 -0.0349 840  ALA A N   
6142  C CA  . ALA A 842  ? 0.2052 0.1782 0.2257 0.0335  -0.0051 -0.0360 840  ALA A CA  
6143  C C   . ALA A 842  ? 0.2069 0.1779 0.2275 0.0321  -0.0063 -0.0360 840  ALA A C   
6144  O O   . ALA A 842  ? 0.2488 0.2178 0.2744 0.0325  -0.0092 -0.0392 840  ALA A O   
6145  C CB  . ALA A 842  ? 0.2340 0.2078 0.2599 0.0363  -0.0073 -0.0414 840  ALA A CB  
6146  N N   . GLY A 843  ? 0.2172 0.1888 0.2327 0.0303  -0.0044 -0.0325 841  GLY A N   
6147  C CA  . GLY A 843  ? 0.2195 0.1896 0.2349 0.0289  -0.0053 -0.0322 841  GLY A CA  
6148  C C   . GLY A 843  ? 0.2189 0.1921 0.2333 0.0311  -0.0062 -0.0369 841  GLY A C   
6149  O O   . GLY A 843  ? 0.2192 0.1910 0.2344 0.0302  -0.0075 -0.0374 841  GLY A O   
6150  N N   . GLN A 844  ? 0.2167 0.1947 0.2294 0.0341  -0.0056 -0.0404 842  GLN A N   
6151  C CA  . GLN A 844  ? 0.2117 0.1936 0.2234 0.0365  -0.0065 -0.0454 842  GLN A CA  
6152  C C   . GLN A 844  ? 0.2341 0.2208 0.2389 0.0368  -0.0041 -0.0437 842  GLN A C   
6153  O O   . GLN A 844  ? 0.2470 0.2399 0.2486 0.0393  -0.0031 -0.0462 842  GLN A O   
6154  C CB  . GLN A 844  ? 0.2338 0.2189 0.2483 0.0398  -0.0076 -0.0507 842  GLN A CB  
6155  C CG  . GLN A 844  ? 0.2272 0.2073 0.2498 0.0395  -0.0106 -0.0525 842  GLN A CG  
6156  C CD  . GLN A 844  ? 0.2158 0.1985 0.2413 0.0425  -0.0113 -0.0569 842  GLN A CD  
6157  O OE1 . GLN A 844  ? 0.2327 0.2154 0.2636 0.0445  -0.0141 -0.0624 842  GLN A OE1 
6158  N NE2 . GLN A 844  ? 0.2454 0.2306 0.2679 0.0430  -0.0088 -0.0546 842  GLN A NE2 
6159  N N   . ARG A 845  ? 0.2372 0.2213 0.2399 0.0341  -0.0031 -0.0393 843  ARG A N   
6160  C CA  . ARG A 845  ? 0.2477 0.2350 0.2451 0.0339  -0.0015 -0.0376 843  ARG A CA  
6161  C C   . ARG A 845  ? 0.2280 0.2122 0.2270 0.0323  -0.0031 -0.0376 843  ARG A C   
6162  O O   . ARG A 845  ? 0.2343 0.2133 0.2369 0.0301  -0.0043 -0.0360 843  ARG A O   
6163  C CB  . ARG A 845  ? 0.2513 0.2383 0.2453 0.0321  0.0012  -0.0321 843  ARG A CB  
6164  C CG  . ARG A 845  ? 0.2462 0.2364 0.2386 0.0334  0.0031  -0.0311 843  ARG A CG  
6165  C CD  . ARG A 845  ? 0.3000 0.2892 0.2898 0.0314  0.0053  -0.0258 843  ARG A CD  
6166  N NE  . ARG A 845  ? 0.3508 0.3434 0.3391 0.0325  0.0071  -0.0245 843  ARG A NE  
6167  C CZ  . ARG A 845  ? 0.3975 0.3956 0.3821 0.0337  0.0088  -0.0235 843  ARG A CZ  
6168  N NH1 . ARG A 845  ? 0.4037 0.4047 0.3857 0.0341  0.0089  -0.0238 843  ARG A NH1 
6169  N NH2 . ARG A 845  ? 0.4331 0.4342 0.4170 0.0345  0.0104  -0.0221 843  ARG A NH2 
6170  N N   . CYS A 846  ? 0.2311 0.2187 0.2274 0.0333  -0.0032 -0.0394 844  CYS A N   
6171  C CA  . CYS A 846  ? 0.2219 0.2068 0.2196 0.0317  -0.0047 -0.0393 844  CYS A CA  
6172  C C   . CYS A 846  ? 0.2203 0.2020 0.2168 0.0287  -0.0033 -0.0340 844  CYS A C   
6173  O O   . CYS A 846  ? 0.2024 0.1806 0.2015 0.0267  -0.0046 -0.0331 844  CYS A O   
6174  C CB  . CYS A 846  ? 0.2267 0.2164 0.2213 0.0333  -0.0049 -0.0418 844  CYS A CB  
6175  S SG  . CYS A 846  ? 0.2726 0.2682 0.2601 0.0342  -0.0017 -0.0387 844  CYS A SG  
6176  N N   . SER A 847  ? 0.2009 0.1841 0.1938 0.0283  -0.0008 -0.0306 845  SER A N   
6177  C CA  . SER A 847  ? 0.1889 0.1698 0.1804 0.0258  0.0007  -0.0259 845  SER A CA  
6178  C C   . SER A 847  ? 0.2067 0.1834 0.2011 0.0240  0.0006  -0.0237 845  SER A C   
6179  O O   . SER A 847  ? 0.2071 0.1822 0.2007 0.0219  0.0017  -0.0201 845  SER A O   
6180  C CB  . SER A 847  ? 0.1906 0.1750 0.1777 0.0265  0.0031  -0.0235 845  SER A CB  
6181  O OG  . SER A 847  ? 0.2365 0.2229 0.2235 0.0281  0.0038  -0.0243 845  SER A OG  
6182  N N   . ALA A 848  ? 0.2025 0.1779 0.2005 0.0248  -0.0008 -0.0257 846  ALA A N   
6183  C CA  . ALA A 848  ? 0.1969 0.1691 0.1975 0.0232  -0.0007 -0.0232 846  ALA A CA  
6184  C C   . ALA A 848  ? 0.2092 0.1779 0.2120 0.0203  -0.0015 -0.0205 846  ALA A C   
6185  O O   . ALA A 848  ? 0.2082 0.1760 0.2129 0.0197  -0.0030 -0.0216 846  ALA A O   
6186  C CB  . ALA A 848  ? 0.2148 0.1860 0.2198 0.0247  -0.0025 -0.0262 846  ALA A CB  
6187  N N   . LEU A 849  ? 0.2059 0.1731 0.2086 0.0186  -0.0004 -0.0170 847  LEU A N   
6188  C CA  . LEU A 849  ? 0.2062 0.1712 0.2110 0.0158  -0.0010 -0.0141 847  LEU A CA  
6189  C C   . LEU A 849  ? 0.2142 0.1764 0.2250 0.0151  -0.0036 -0.0149 847  LEU A C   
6190  O O   . LEU A 849  ? 0.2141 0.1752 0.2275 0.0158  -0.0043 -0.0152 847  LEU A O   
6191  C CB  . LEU A 849  ? 0.2176 0.1825 0.2208 0.0144  0.0007  -0.0105 847  LEU A CB  
6192  C CG  . LEU A 849  ? 0.2045 0.1679 0.2098 0.0115  0.0003  -0.0074 847  LEU A CG  
6193  C CD1 . LEU A 849  ? 0.2097 0.1740 0.2137 0.0105  0.0004  -0.0071 847  LEU A CD1 
6194  C CD2 . LEU A 849  ? 0.2225 0.1864 0.2261 0.0104  0.0019  -0.0044 847  LEU A CD2 
6195  N N   . ARG A 850  ? 0.2064 0.1676 0.2198 0.0139  -0.0052 -0.0149 848  ARG A N   
6196  C CA  . ARG A 850  ? 0.2290 0.1875 0.2488 0.0130  -0.0081 -0.0152 848  ARG A CA  
6197  C C   . ARG A 850  ? 0.2273 0.1846 0.2495 0.0098  -0.0084 -0.0107 848  ARG A C   
6198  O O   . ARG A 850  ? 0.2280 0.1832 0.2557 0.0087  -0.0104 -0.0095 848  ARG A O   
6199  C CB  . ARG A 850  ? 0.2366 0.1949 0.2588 0.0138  -0.0101 -0.0186 848  ARG A CB  
6200  C CG  . ARG A 850  ? 0.2321 0.1927 0.2516 0.0169  -0.0099 -0.0232 848  ARG A CG  
6201  C CD  . ARG A 850  ? 0.2412 0.2017 0.2620 0.0190  -0.0101 -0.0253 848  ARG A CD  
6202  N NE  . ARG A 850  ? 0.2283 0.1919 0.2471 0.0221  -0.0101 -0.0301 848  ARG A NE  
6203  C CZ  . ARG A 850  ? 0.2278 0.1928 0.2467 0.0245  -0.0100 -0.0327 848  ARG A CZ  
6204  N NH1 . ARG A 850  ? 0.2183 0.1817 0.2394 0.0241  -0.0099 -0.0311 848  ARG A NH1 
6205  N NH2 . ARG A 850  ? 0.2419 0.2106 0.2586 0.0273  -0.0100 -0.0370 848  ARG A NH2 
6206  N N   . VAL A 851  ? 0.2226 0.1816 0.2412 0.0083  -0.0067 -0.0083 849  VAL A N   
6207  C CA  . VAL A 851  ? 0.2355 0.1947 0.2562 0.0053  -0.0069 -0.0043 849  VAL A CA  
6208  C C   . VAL A 851  ? 0.2197 0.1810 0.2353 0.0045  -0.0042 -0.0019 849  VAL A C   
6209  O O   . VAL A 851  ? 0.2302 0.1933 0.2417 0.0049  -0.0027 -0.0026 849  VAL A O   
6210  C CB  . VAL A 851  ? 0.2730 0.2324 0.2956 0.0040  -0.0082 -0.0043 849  VAL A CB  
6211  C CG1 . VAL A 851  ? 0.3072 0.2675 0.3324 0.0009  -0.0085 0.0002  849  VAL A CG1 
6212  C CG2 . VAL A 851  ? 0.3196 0.2770 0.3471 0.0052  -0.0110 -0.0076 849  VAL A CG2 
6213  N N   . LEU A 852  ? 0.2083 0.1696 0.2246 0.0033  -0.0038 0.0009  850  LEU A N   
6214  C CA  . LEU A 852  ? 0.2020 0.1656 0.2144 0.0024  -0.0016 0.0032  850  LEU A CA  
6215  C C   . LEU A 852  ? 0.2012 0.1667 0.2152 -0.0004 -0.0019 0.0065  850  LEU A C   
6216  O O   . LEU A 852  ? 0.2146 0.1795 0.2332 -0.0020 -0.0037 0.0087  850  LEU A O   
6217  C CB  . LEU A 852  ? 0.2102 0.1733 0.2225 0.0027  -0.0011 0.0043  850  LEU A CB  
6218  C CG  . LEU A 852  ? 0.2039 0.1693 0.2130 0.0016  0.0008  0.0066  850  LEU A CG  
6219  C CD1 . LEU A 852  ? 0.2052 0.1719 0.2095 0.0029  0.0029  0.0049  850  LEU A CD1 
6220  C CD2 . LEU A 852  ? 0.2208 0.1853 0.2308 0.0018  0.0008  0.0079  850  LEU A CD2 
6221  N N   . CYS A 853  ? 0.2168 0.1849 0.2274 -0.0010 -0.0003 0.0068  851  CYS A N   
6222  C CA  . CYS A 853  ? 0.2150 0.1860 0.2267 -0.0034 -0.0004 0.0095  851  CYS A CA  
6223  C C   . CYS A 853  ? 0.1916 0.1656 0.2001 -0.0042 0.0015  0.0112  851  CYS A C   
6224  O O   . CYS A 853  ? 0.2085 0.1835 0.2133 -0.0031 0.0032  0.0095  851  CYS A O   
6225  C CB  . CYS A 853  ? 0.2157 0.1878 0.2265 -0.0034 -0.0003 0.0081  851  CYS A CB  
6226  S SG  . CYS A 853  ? 0.2482 0.2171 0.2618 -0.0020 -0.0023 0.0050  851  CYS A SG  
6227  N N   . LEU A 854  ? 0.2038 0.1795 0.2143 -0.0061 0.0010  0.0144  852  LEU A N   
6228  C CA  . LEU A 854  ? 0.2045 0.1832 0.2124 -0.0067 0.0025  0.0159  852  LEU A CA  
6229  C C   . LEU A 854  ? 0.2129 0.1967 0.2210 -0.0089 0.0028  0.0182  852  LEU A C   
6230  O O   . LEU A 854  ? 0.2309 0.2159 0.2426 -0.0108 0.0014  0.0210  852  LEU A O   
6231  C CB  . LEU A 854  ? 0.2142 0.1917 0.2241 -0.0071 0.0017  0.0179  852  LEU A CB  
6232  C CG  . LEU A 854  ? 0.2343 0.2075 0.2443 -0.0049 0.0014  0.0156  852  LEU A CG  
6233  C CD1 . LEU A 854  ? 0.2186 0.1908 0.2312 -0.0054 0.0004  0.0179  852  LEU A CD1 
6234  C CD2 . LEU A 854  ? 0.2505 0.2238 0.2560 -0.0031 0.0034  0.0131  852  LEU A CD2 
6235  N N   . GLN A 855  ? 0.2117 0.1987 0.2163 -0.0087 0.0046  0.0172  853  GLN A N   
6236  C CA  . GLN A 855  ? 0.2206 0.2134 0.2250 -0.0107 0.0051  0.0191  853  GLN A CA  
6237  C C   . GLN A 855  ? 0.2181 0.2137 0.2242 -0.0125 0.0044  0.0228  853  GLN A C   
6238  O O   . GLN A 855  ? 0.2335 0.2275 0.2390 -0.0120 0.0045  0.0231  853  GLN A O   
6239  C CB  . GLN A 855  ? 0.2102 0.2060 0.2109 -0.0098 0.0069  0.0167  853  GLN A CB  
6240  C CG  . GLN A 855  ? 0.2395 0.2419 0.2401 -0.0114 0.0075  0.0178  853  GLN A CG  
6241  C CD  . GLN A 855  ? 0.2594 0.2651 0.2570 -0.0105 0.0091  0.0152  853  GLN A CD  
6242  O OE1 . GLN A 855  ? 0.2781 0.2810 0.2743 -0.0087 0.0097  0.0122  853  GLN A OE1 
6243  N NE2 . GLN A 855  ? 0.3135 0.3259 0.3107 -0.0119 0.0096  0.0164  853  GLN A NE2 
6244  N N   . GLU A 856  ? 0.2418 0.2416 0.2503 -0.0147 0.0037  0.0260  854  GLU A N   
6245  C CA  . GLU A 856  ? 0.2625 0.2646 0.2738 -0.0168 0.0025  0.0304  854  GLU A CA  
6246  C C   . GLU A 856  ? 0.2798 0.2849 0.2884 -0.0168 0.0036  0.0309  854  GLU A C   
6247  O O   . GLU A 856  ? 0.2944 0.2982 0.3046 -0.0172 0.0026  0.0331  854  GLU A O   
6248  C CB  . GLU A 856  ? 0.2725 0.2803 0.2863 -0.0193 0.0020  0.0339  854  GLU A CB  
6249  C CG  . GLU A 856  ? 0.3131 0.3248 0.3299 -0.0217 0.0008  0.0392  854  GLU A CG  
6250  C CD  . GLU A 856  ? 0.4256 0.4314 0.4472 -0.0218 -0.0015 0.0412  854  GLU A CD  
6251  O OE1 . GLU A 856  ? 0.3545 0.3548 0.3787 -0.0209 -0.0027 0.0395  854  GLU A OE1 
6252  O OE2 . GLU A 856  ? 0.4320 0.4390 0.4550 -0.0228 -0.0022 0.0443  854  GLU A OE2 
6253  N N   . ASP A 857  ? 0.2489 0.2580 0.2536 -0.0161 0.0054  0.0286  855  ASP A N   
6254  C CA  . ASP A 857  ? 0.2954 0.3085 0.2978 -0.0163 0.0062  0.0288  855  ASP A CA  
6255  C C   . ASP A 857  ? 0.3023 0.3101 0.3038 -0.0146 0.0062  0.0274  855  ASP A C   
6256  O O   . ASP A 857  ? 0.3347 0.3449 0.3355 -0.0151 0.0064  0.0286  855  ASP A O   
6257  C CB  . ASP A 857  ? 0.3686 0.3867 0.3677 -0.0157 0.0079  0.0259  855  ASP A CB  
6258  N N   . VAL A 858  ? 0.2505 0.2518 0.2522 -0.0128 0.0062  0.0248  856  VAL A N   
6259  C CA  . VAL A 858  ? 0.2628 0.2595 0.2637 -0.0112 0.0063  0.0235  856  VAL A CA  
6260  C C   . VAL A 858  ? 0.2258 0.2172 0.2300 -0.0108 0.0047  0.0246  856  VAL A C   
6261  O O   . VAL A 858  ? 0.2348 0.2225 0.2388 -0.0094 0.0047  0.0235  856  VAL A O   
6262  C CB  . VAL A 858  ? 0.2690 0.2634 0.2671 -0.0090 0.0076  0.0194  856  VAL A CB  
6263  C CG1 . VAL A 858  ? 0.2925 0.2921 0.2882 -0.0092 0.0089  0.0181  856  VAL A CG1 
6264  C CG2 . VAL A 858  ? 0.2567 0.2483 0.2553 -0.0081 0.0075  0.0176  856  VAL A CG2 
6265  N N   . ALA A 859  ? 0.2449 0.2360 0.2524 -0.0121 0.0033  0.0265  857  ALA A N   
6266  C CA  . ALA A 859  ? 0.2323 0.2181 0.2435 -0.0114 0.0016  0.0265  857  ALA A CA  
6267  C C   . ALA A 859  ? 0.2589 0.2431 0.2722 -0.0116 0.0006  0.0287  857  ALA A C   
6268  O O   . ALA A 859  ? 0.2401 0.2197 0.2545 -0.0099 0.0001  0.0269  857  ALA A O   
6269  C CB  . ALA A 859  ? 0.2388 0.2248 0.2539 -0.0129 0.0000  0.0284  857  ALA A CB  
6270  N N   . ASP A 860  ? 0.2607 0.2492 0.2749 -0.0136 0.0002  0.0324  858  ASP A N   
6271  C CA  . ASP A 860  ? 0.2808 0.2681 0.2976 -0.0139 -0.0010 0.0348  858  ASP A CA  
6272  C C   . ASP A 860  ? 0.2592 0.2445 0.2730 -0.0120 0.0003  0.0322  858  ASP A C   
6273  O O   . ASP A 860  ? 0.2801 0.2614 0.2960 -0.0109 -0.0006 0.0319  858  ASP A O   
6274  C CB  . ASP A 860  ? 0.2932 0.2865 0.3110 -0.0165 -0.0015 0.0396  858  ASP A CB  
6275  C CG  . ASP A 860  ? 0.3657 0.3605 0.3883 -0.0187 -0.0033 0.0433  858  ASP A CG  
6276  O OD1 . ASP A 860  ? 0.4039 0.3938 0.4306 -0.0182 -0.0049 0.0428  858  ASP A OD1 
6277  O OD2 . ASP A 860  ? 0.5466 0.5479 0.5691 -0.0209 -0.0032 0.0469  858  ASP A OD2 
6278  N N   . ARG A 861  ? 0.2543 0.2425 0.2635 -0.0115 0.0022  0.0304  859  ARG A N   
6279  C CA  . ARG A 861  ? 0.2641 0.2507 0.2709 -0.0098 0.0033  0.0282  859  ARG A CA  
6280  C C   . ARG A 861  ? 0.2469 0.2280 0.2537 -0.0075 0.0036  0.0250  859  ARG A C   
6281  O O   . ARG A 861  ? 0.2428 0.2211 0.2502 -0.0062 0.0034  0.0244  859  ARG A O   
6282  C CB  . ARG A 861  ? 0.3466 0.3373 0.3493 -0.0098 0.0051  0.0266  859  ARG A CB  
6283  N N   . ILE A 862  ? 0.2390 0.2190 0.2449 -0.0068 0.0039  0.0229  860  ILE A N   
6284  C CA  . ILE A 862  ? 0.2411 0.2169 0.2467 -0.0045 0.0042  0.0198  860  ILE A CA  
6285  C C   . ILE A 862  ? 0.2306 0.2029 0.2403 -0.0041 0.0024  0.0202  860  ILE A C   
6286  O O   . ILE A 862  ? 0.2163 0.1859 0.2262 -0.0022 0.0024  0.0184  860  ILE A O   
6287  C CB  . ILE A 862  ? 0.2415 0.2174 0.2454 -0.0040 0.0048  0.0176  860  ILE A CB  
6288  C CG1 . ILE A 862  ? 0.2574 0.2362 0.2577 -0.0039 0.0066  0.0164  860  ILE A CG1 
6289  C CG2 . ILE A 862  ? 0.2368 0.2088 0.2408 -0.0018 0.0047  0.0148  860  ILE A CG2 
6290  C CD1 . ILE A 862  ? 0.2819 0.2616 0.2808 -0.0037 0.0071  0.0148  860  ILE A CD1 
6291  N N   . LEU A 863  ? 0.2293 0.2018 0.2427 -0.0057 0.0006  0.0225  861  LEU A N   
6292  C CA  A LEU A 863  ? 0.2319 0.2010 0.2503 -0.0052 -0.0015 0.0228  861  LEU A CA  
6293  C CA  B LEU A 863  ? 0.2318 0.2008 0.2501 -0.0052 -0.0015 0.0228  861  LEU A CA  
6294  C C   . LEU A 863  ? 0.2272 0.1952 0.2471 -0.0049 -0.0019 0.0240  861  LEU A C   
6295  O O   . LEU A 863  ? 0.2224 0.1871 0.2445 -0.0031 -0.0027 0.0221  861  LEU A O   
6296  C CB  A LEU A 863  ? 0.2522 0.2221 0.2751 -0.0074 -0.0035 0.0258  861  LEU A CB  
6297  C CB  B LEU A 863  ? 0.2522 0.2221 0.2750 -0.0074 -0.0035 0.0258  861  LEU A CB  
6298  C CG  A LEU A 863  ? 0.2872 0.2553 0.3119 -0.0071 -0.0044 0.0240  861  LEU A CG  
6299  C CG  B LEU A 863  ? 0.2582 0.2243 0.2871 -0.0070 -0.0061 0.0257  861  LEU A CG  
6300  C CD1 A LEU A 863  ? 0.2530 0.2228 0.2821 -0.0097 -0.0063 0.0278  861  LEU A CD1 
6301  C CD1 B LEU A 863  ? 0.2369 0.1996 0.2651 -0.0043 -0.0059 0.0208  861  LEU A CD1 
6302  C CD2 A LEU A 863  ? 0.2779 0.2415 0.3054 -0.0049 -0.0057 0.0208  861  LEU A CD2 
6303  C CD2 B LEU A 863  ? 0.2874 0.2547 0.3204 -0.0094 -0.0078 0.0287  861  LEU A CD2 
6304  N N   . THR A 864  ? 0.2330 0.2043 0.2518 -0.0064 -0.0015 0.0269  862  THR A N   
6305  C CA  . THR A 864  ? 0.2307 0.2013 0.2508 -0.0061 -0.0018 0.0280  862  THR A CA  
6306  C C   . THR A 864  ? 0.2129 0.1816 0.2302 -0.0036 -0.0003 0.0246  862  THR A C   
6307  O O   . THR A 864  ? 0.2112 0.1773 0.2307 -0.0022 -0.0010 0.0237  862  THR A O   
6308  C CB  . THR A 864  ? 0.2414 0.2166 0.2600 -0.0081 -0.0014 0.0313  862  THR A CB  
6309  O OG1 . THR A 864  ? 0.2739 0.2514 0.2957 -0.0105 -0.0030 0.0351  862  THR A OG1 
6310  C CG2 . THR A 864  ? 0.2534 0.2280 0.2729 -0.0076 -0.0017 0.0324  862  THR A CG2 
6311  N N   . MET A 865  ? 0.2103 0.1804 0.2228 -0.0030 0.0017  0.0226  863  MET A N   
6312  C CA  . MET A 865  ? 0.2176 0.1864 0.2277 -0.0008 0.0032  0.0198  863  MET A CA  
6313  C C   . MET A 865  ? 0.1963 0.1620 0.2078 0.0013  0.0027  0.0170  863  MET A C   
6314  O O   . MET A 865  ? 0.1949 0.1592 0.2067 0.0031  0.0030  0.0156  863  MET A O   
6315  C CB  . MET A 865  ? 0.2353 0.2063 0.2411 -0.0007 0.0051  0.0186  863  MET A CB  
6316  C CG  . MET A 865  ? 0.2812 0.2514 0.2847 0.0012  0.0066  0.0166  863  MET A CG  
6317  S SD  . MET A 865  ? 0.3085 0.2812 0.3082 0.0010  0.0083  0.0154  863  MET A SD  
6318  C CE  . MET A 865  ? 0.2518 0.2282 0.2518 -0.0016 0.0077  0.0180  863  MET A CE  
6319  N N   . LEU A 866  ? 0.2000 0.1650 0.2124 0.0011  0.0019  0.0162  864  LEU A N   
6320  C CA  . LEU A 866  ? 0.2098 0.1724 0.2235 0.0031  0.0013  0.0132  864  LEU A CA  
6321  C C   . LEU A 866  ? 0.1935 0.1538 0.2121 0.0039  -0.0006 0.0131  864  LEU A C   
6322  O O   . LEU A 866  ? 0.2079 0.1670 0.2268 0.0061  -0.0004 0.0103  864  LEU A O   
6323  C CB  . LEU A 866  ? 0.2121 0.1746 0.2266 0.0024  0.0005  0.0126  864  LEU A CB  
6324  C CG  . LEU A 866  ? 0.2633 0.2237 0.2791 0.0044  -0.0003 0.0092  864  LEU A CG  
6325  C CD1 . LEU A 866  ? 0.2680 0.2290 0.2798 0.0067  0.0015  0.0064  864  LEU A CD1 
6326  C CD2 . LEU A 866  ? 0.2923 0.2527 0.3089 0.0035  -0.0012 0.0089  864  LEU A CD2 
6327  N N   . LYS A 867  ? 0.2102 0.1701 0.2328 0.0020  -0.0024 0.0161  865  LYS A N   
6328  C CA  . LYS A 867  ? 0.2278 0.1854 0.2560 0.0026  -0.0045 0.0162  865  LYS A CA  
6329  C C   . LYS A 867  ? 0.2113 0.1691 0.2385 0.0039  -0.0035 0.0160  865  LYS A C   
6330  O O   . LYS A 867  ? 0.2135 0.1695 0.2434 0.0059  -0.0043 0.0138  865  LYS A O   
6331  C CB  . LYS A 867  ? 0.2379 0.1956 0.2708 0.0001  -0.0066 0.0204  865  LYS A CB  
6332  C CG  . LYS A 867  ? 0.2485 0.2057 0.2839 -0.0011 -0.0081 0.0206  865  LYS A CG  
6333  C CD  . LYS A 867  ? 0.2549 0.2130 0.2950 -0.0039 -0.0101 0.0255  865  LYS A CD  
6334  C CE  . LYS A 867  ? 0.3124 0.2703 0.3551 -0.0051 -0.0114 0.0259  865  LYS A CE  
6335  N NZ  . LYS A 867  ? 0.3753 0.3354 0.4218 -0.0083 -0.0130 0.0314  865  LYS A NZ  
6336  N N   . GLY A 868  ? 0.2137 0.1738 0.2373 0.0029  -0.0019 0.0180  866  GLY A N   
6337  C CA  . GLY A 868  ? 0.2189 0.1794 0.2416 0.0040  -0.0009 0.0177  866  GLY A CA  
6338  C C   . GLY A 868  ? 0.2069 0.1671 0.2272 0.0067  0.0006  0.0140  866  GLY A C   
6339  O O   . GLY A 868  ? 0.2160 0.1756 0.2378 0.0084  0.0005  0.0127  866  GLY A O   
6340  N N   . ALA A 869  ? 0.2015 0.1624 0.2180 0.0070  0.0019  0.0123  867  ALA A N   
6341  C CA  . ALA A 869  ? 0.1983 0.1597 0.2124 0.0094  0.0033  0.0092  867  ALA A CA  
6342  C C   . ALA A 869  ? 0.2114 0.1713 0.2287 0.0115  0.0020  0.0062  867  ALA A C   
6343  O O   . ALA A 869  ? 0.2093 0.1700 0.2263 0.0137  0.0026  0.0040  867  ALA A O   
6344  C CB  . ALA A 869  ? 0.2084 0.1710 0.2183 0.0092  0.0048  0.0085  867  ALA A CB  
6345  N N   . LEU A 870  ? 0.2098 0.1680 0.2304 0.0107  -0.0001 0.0061  868  LEU A N   
6346  C CA  . LEU A 870  ? 0.2157 0.1724 0.2402 0.0126  -0.0018 0.0029  868  LEU A CA  
6347  C C   . LEU A 870  ? 0.2350 0.1911 0.2631 0.0140  -0.0026 0.0022  868  LEU A C   
6348  O O   . LEU A 870  ? 0.2315 0.1880 0.2604 0.0166  -0.0027 -0.0015 868  LEU A O   
6349  C CB  . LEU A 870  ? 0.2235 0.1782 0.2524 0.0110  -0.0043 0.0038  868  LEU A CB  
6350  C CG  . LEU A 870  ? 0.2567 0.2094 0.2907 0.0126  -0.0067 0.0003  868  LEU A CG  
6351  C CD1 . LEU A 870  ? 0.2870 0.2407 0.3180 0.0139  -0.0060 -0.0029 868  LEU A CD1 
6352  C CD2 . LEU A 870  ? 0.3008 0.2510 0.3413 0.0107  -0.0096 0.0027  868  LEU A CD2 
6353  N N   . HIS A 871  ? 0.2161 0.1716 0.2462 0.0124  -0.0032 0.0055  869  HIS A N   
6354  C CA  . HIS A 871  ? 0.2440 0.1987 0.2784 0.0136  -0.0042 0.0052  869  HIS A CA  
6355  C C   . HIS A 871  ? 0.2328 0.1896 0.2640 0.0154  -0.0020 0.0040  869  HIS A C   
6356  O O   . HIS A 871  ? 0.2616 0.2183 0.2961 0.0168  -0.0027 0.0031  869  HIS A O   
6357  C CB  . HIS A 871  ? 0.2522 0.2057 0.2903 0.0112  -0.0058 0.0095  869  HIS A CB  
6358  C CG  . HIS A 871  ? 0.2775 0.2289 0.3209 0.0099  -0.0086 0.0105  869  HIS A CG  
6359  N ND1 . HIS A 871  ? 0.3208 0.2697 0.3707 0.0113  -0.0112 0.0081  869  HIS A ND1 
6360  C CD2 . HIS A 871  ? 0.2574 0.2088 0.3009 0.0073  -0.0093 0.0136  869  HIS A CD2 
6361  C CE1 . HIS A 871  ? 0.3237 0.2709 0.3778 0.0095  -0.0135 0.0099  869  HIS A CE1 
6362  N NE2 . HIS A 871  ? 0.3017 0.2506 0.3518 0.0070  -0.0123 0.0134  869  HIS A NE2 
6363  N N   . GLU A 872  ? 0.2022 0.1613 0.2277 0.0155  0.0004  0.0039  870  GLU A N   
6364  C CA  . GLU A 872  ? 0.2385 0.2000 0.2613 0.0172  0.0025  0.0029  870  GLU A CA  
6365  C C   . GLU A 872  ? 0.2461 0.2095 0.2677 0.0199  0.0031  -0.0011 870  GLU A C   
6366  O O   . GLU A 872  ? 0.2290 0.1951 0.2483 0.0215  0.0049  -0.0019 870  GLU A O   
6367  C CB  . GLU A 872  ? 0.2349 0.1979 0.2527 0.0157  0.0046  0.0054  870  GLU A CB  
6368  C CG  . GLU A 872  ? 0.2607 0.2231 0.2793 0.0132  0.0041  0.0091  870  GLU A CG  
6369  C CD  . GLU A 872  ? 0.2542 0.2164 0.2758 0.0135  0.0036  0.0102  870  GLU A CD  
6370  O OE1 . GLU A 872  ? 0.2760 0.2393 0.2979 0.0156  0.0043  0.0084  870  GLU A OE1 
6371  O OE2 . GLU A 872  ? 0.2704 0.2318 0.2940 0.0116  0.0024  0.0130  870  GLU A OE2 
6372  N N   . LEU A 873  ? 0.2205 0.1828 0.2437 0.0206  0.0017  -0.0037 871  LEU A N   
6373  C CA  . LEU A 873  ? 0.2201 0.1849 0.2421 0.0234  0.0022  -0.0078 871  LEU A CA  
6374  C C   . LEU A 873  ? 0.2320 0.1973 0.2584 0.0258  0.0010  -0.0110 871  LEU A C   
6375  O O   . LEU A 873  ? 0.2620 0.2245 0.2940 0.0255  -0.0013 -0.0110 871  LEU A O   
6376  C CB  . LEU A 873  ? 0.2279 0.1916 0.2501 0.0232  0.0010  -0.0097 871  LEU A CB  
6377  C CG  . LEU A 873  ? 0.2405 0.2040 0.2585 0.0210  0.0021  -0.0071 871  LEU A CG  
6378  C CD1 . LEU A 873  ? 0.2583 0.2203 0.2773 0.0207  0.0006  -0.0089 871  LEU A CD1 
6379  C CD2 . LEU A 873  ? 0.2668 0.2336 0.2793 0.0217  0.0048  -0.0068 871  LEU A CD2 
6380  N N   . HIS A 874  ? 0.2320 0.2014 0.2562 0.0284  0.0026  -0.0136 872  HIS A N   
6381  C CA  . HIS A 874  ? 0.2209 0.1921 0.2488 0.0312  0.0017  -0.0174 872  HIS A CA  
6382  C C   . HIS A 874  ? 0.2150 0.1879 0.2434 0.0334  0.0007  -0.0224 872  HIS A C   
6383  O O   . HIS A 874  ? 0.2310 0.2074 0.2546 0.0342  0.0024  -0.0234 872  HIS A O   
6384  C CB  . HIS A 874  ? 0.2405 0.2163 0.2656 0.0326  0.0042  -0.0170 872  HIS A CB  
6385  C CG  . HIS A 874  ? 0.2811 0.2597 0.3096 0.0357  0.0038  -0.0208 872  HIS A CG  
6386  N ND1 . HIS A 874  ? 0.4145 0.3912 0.4490 0.0371  0.0010  -0.0246 872  HIS A ND1 
6387  C CD2 . HIS A 874  ? 0.3538 0.3374 0.3809 0.0376  0.0056  -0.0216 872  HIS A CD2 
6388  C CE1 . HIS A 874  ? 0.3018 0.2823 0.3383 0.0400  0.0012  -0.0278 872  HIS A CE1 
6389  N NE2 . HIS A 874  ? 0.3716 0.3565 0.4035 0.0403  0.0041  -0.0260 872  HIS A NE2 
6390  N N   . ILE A 875  ? 0.2177 0.1881 0.2522 0.0344  -0.0022 -0.0254 873  ILE A N   
6391  C CA  . ILE A 875  ? 0.2416 0.2131 0.2778 0.0365  -0.0037 -0.0307 873  ILE A CA  
6392  C C   . ILE A 875  ? 0.2913 0.2664 0.3308 0.0401  -0.0043 -0.0356 873  ILE A C   
6393  O O   . ILE A 875  ? 0.2655 0.2387 0.3103 0.0404  -0.0056 -0.0357 873  ILE A O   
6394  C CB  . ILE A 875  ? 0.2612 0.2274 0.3030 0.0350  -0.0070 -0.0310 873  ILE A CB  
6395  C CG1 . ILE A 875  ? 0.3178 0.2820 0.3559 0.0321  -0.0065 -0.0273 873  ILE A CG1 
6396  C CG2 . ILE A 875  ? 0.2690 0.2363 0.3144 0.0377  -0.0092 -0.0373 873  ILE A CG2 
6397  C CD1 . ILE A 875  ? 0.3157 0.2787 0.3502 0.0292  -0.0045 -0.0214 873  ILE A CD1 
6398  N N   . GLY A 876  ? 0.2454 0.2260 0.2820 0.0428  -0.0032 -0.0398 874  GLY A N   
6399  C CA  . GLY A 876  ? 0.2453 0.2302 0.2849 0.0463  -0.0037 -0.0450 874  GLY A CA  
6400  C C   . GLY A 876  ? 0.2344 0.2267 0.2695 0.0491  -0.0022 -0.0491 874  GLY A C   
6401  O O   . GLY A 876  ? 0.2403 0.2337 0.2704 0.0482  -0.0012 -0.0480 874  GLY A O   
6402  N N   . ARG A 877  ? 0.2374 0.2349 0.2744 0.0525  -0.0022 -0.0538 875  ARG A N   
6403  C CA  . ARG A 877  ? 0.2372 0.2432 0.2699 0.0553  -0.0006 -0.0576 875  ARG A CA  
6404  C C   . ARG A 877  ? 0.2393 0.2493 0.2643 0.0540  0.0031  -0.0523 875  ARG A C   
6405  O O   . ARG A 877  ? 0.2505 0.2596 0.2748 0.0525  0.0047  -0.0477 875  ARG A O   
6406  C CB  . ARG A 877  ? 0.2937 0.3053 0.3300 0.0591  -0.0010 -0.0630 875  ARG A CB  
6407  C CG  . ARG A 877  ? 0.2872 0.3075 0.3212 0.0627  -0.0006 -0.0691 875  ARG A CG  
6408  C CD  . ARG A 877  ? 0.3216 0.3474 0.3601 0.0665  -0.0013 -0.0750 875  ARG A CD  
6409  N NE  . ARG A 877  ? 0.2994 0.3320 0.3341 0.0673  0.0020  -0.0724 875  ARG A NE  
6410  C CZ  . ARG A 877  ? 0.3863 0.4257 0.4234 0.0707  0.0023  -0.0769 875  ARG A CZ  
6411  N NH1 . ARG A 877  ? 0.3956 0.4357 0.4392 0.0738  -0.0006 -0.0845 875  ARG A NH1 
6412  N NH2 . ARG A 877  ? 0.3649 0.4109 0.3984 0.0711  0.0055  -0.0739 875  ARG A NH2 
6413  N N   . THR A 878  ? 0.2493 0.2636 0.2692 0.0544  0.0042  -0.0528 876  THR A N   
6414  C CA  . THR A 878  ? 0.2323 0.2481 0.2458 0.0522  0.0070  -0.0470 876  THR A CA  
6415  C C   . THR A 878  ? 0.2382 0.2625 0.2479 0.0537  0.0100  -0.0456 876  THR A C   
6416  O O   . THR A 878  ? 0.2435 0.2697 0.2483 0.0521  0.0122  -0.0409 876  THR A O   
6417  C CB  . THR A 878  ? 0.2226 0.2384 0.2326 0.0516  0.0067  -0.0473 876  THR A CB  
6418  O OG1 . THR A 878  ? 0.2873 0.3093 0.2976 0.0549  0.0058  -0.0537 876  THR A OG1 
6419  C CG2 . THR A 878  ? 0.2975 0.3045 0.3106 0.0491  0.0043  -0.0464 876  THR A CG2 
6420  N N   . ASP A 879  ? 0.2251 0.2546 0.2373 0.0567  0.0100  -0.0495 877  ASP A N   
6421  C CA  . ASP A 879  ? 0.2635 0.3016 0.2726 0.0580  0.0129  -0.0479 877  ASP A CA  
6422  C C   . ASP A 879  ? 0.2454 0.2806 0.2555 0.0560  0.0142  -0.0426 877  ASP A C   
6423  O O   . ASP A 879  ? 0.2385 0.2799 0.2484 0.0575  0.0160  -0.0422 877  ASP A O   
6424  C CB  . ASP A 879  ? 0.2403 0.2867 0.2513 0.0622  0.0126  -0.0545 877  ASP A CB  
6425  C CG  . ASP A 879  ? 0.3366 0.3793 0.3546 0.0635  0.0104  -0.0584 877  ASP A CG  
6426  O OD1 . ASP A 879  ? 0.3467 0.3799 0.3687 0.0616  0.0081  -0.0578 877  ASP A OD1 
6427  O OD2 . ASP A 879  ? 0.3130 0.3625 0.3327 0.0665  0.0110  -0.0618 877  ASP A OD2 
6428  N N   . ARG A 880  ? 0.2472 0.2736 0.2583 0.0527  0.0135  -0.0386 878  ARG A N   
6429  C CA  . ARG A 880  ? 0.2377 0.2610 0.2492 0.0505  0.0147  -0.0332 878  ARG A CA  
6430  C C   . ARG A 880  ? 0.2359 0.2548 0.2438 0.0471  0.0154  -0.0278 878  ARG A C   
6431  O O   . ARG A 880  ? 0.2320 0.2456 0.2401 0.0457  0.0138  -0.0283 878  ARG A O   
6432  C CB  . ARG A 880  ? 0.3004 0.3168 0.3176 0.0498  0.0125  -0.0339 878  ARG A CB  
6433  C CG  . ARG A 880  ? 0.3202 0.3403 0.3421 0.0530  0.0117  -0.0387 878  ARG A CG  
6434  C CD  . ARG A 880  ? 0.4192 0.4319 0.4472 0.0519  0.0094  -0.0384 878  ARG A CD  
6435  N NE  . ARG A 880  ? 0.6154 0.6307 0.6487 0.0550  0.0082  -0.0433 878  ARG A NE  
6436  C CZ  . ARG A 880  ? 0.6376 0.6537 0.6737 0.0553  0.0087  -0.0421 878  ARG A CZ  
6437  N NH1 . ARG A 880  ? 0.7019 0.7162 0.7359 0.0528  0.0104  -0.0361 878  ARG A NH1 
6438  N NH2 . ARG A 880  ? 0.6551 0.6738 0.6964 0.0584  0.0074  -0.0471 878  ARG A NH2 
6439  N N   . LEU A 881  ? 0.2231 0.2445 0.2282 0.0458  0.0177  -0.0230 879  LEU A N   
6440  C CA  . LEU A 881  ? 0.2142 0.2319 0.2164 0.0428  0.0184  -0.0181 879  LEU A CA  
6441  C C   . LEU A 881  ? 0.2180 0.2267 0.2226 0.0402  0.0167  -0.0166 879  LEU A C   
6442  O O   . LEU A 881  ? 0.2235 0.2285 0.2263 0.0380  0.0164  -0.0145 879  LEU A O   
6443  C CB  . LEU A 881  ? 0.2278 0.2493 0.2283 0.0419  0.0208  -0.0132 879  LEU A CB  
6444  C CG  . LEU A 881  ? 0.2385 0.2572 0.2366 0.0390  0.0217  -0.0082 879  LEU A CG  
6445  C CD1 . LEU A 881  ? 0.2745 0.2957 0.2690 0.0393  0.0219  -0.0087 879  LEU A CD1 
6446  C CD2 . LEU A 881  ? 0.2776 0.2999 0.2754 0.0384  0.0236  -0.0038 879  LEU A CD2 
6447  N N   . SER A 882  ? 0.2193 0.2251 0.2281 0.0403  0.0156  -0.0175 880  SER A N   
6448  C CA  . SER A 882  ? 0.2314 0.2296 0.2425 0.0378  0.0140  -0.0155 880  SER A CA  
6449  C C   . SER A 882  ? 0.2402 0.2341 0.2530 0.0375  0.0116  -0.0182 880  SER A C   
6450  O O   . SER A 882  ? 0.2507 0.2388 0.2652 0.0352  0.0103  -0.0162 880  SER A O   
6451  C CB  . SER A 882  ? 0.2376 0.2344 0.2531 0.0380  0.0133  -0.0154 880  SER A CB  
6452  O OG  . SER A 882  ? 0.2877 0.2863 0.3068 0.0408  0.0119  -0.0204 880  SER A OG  
6453  N N   . VAL A 883  ? 0.2426 0.2394 0.2551 0.0397  0.0110  -0.0225 881  VAL A N   
6454  C CA  . VAL A 883  ? 0.2446 0.2374 0.2593 0.0394  0.0086  -0.0251 881  VAL A CA  
6455  C C   . VAL A 883  ? 0.2397 0.2309 0.2505 0.0375  0.0090  -0.0229 881  VAL A C   
6456  O O   . VAL A 883  ? 0.2768 0.2724 0.2832 0.0381  0.0107  -0.0225 881  VAL A O   
6457  C CB  . VAL A 883  ? 0.2648 0.2612 0.2816 0.0428  0.0073  -0.0313 881  VAL A CB  
6458  C CG1 . VAL A 883  ? 0.2407 0.2333 0.2592 0.0424  0.0049  -0.0338 881  VAL A CG1 
6459  C CG2 . VAL A 883  ? 0.2445 0.2408 0.2667 0.0445  0.0061  -0.0338 881  VAL A CG2 
6460  N N   . ASP A 884  ? 0.2060 0.1912 0.2185 0.0351  0.0075  -0.0213 882  ASP A N   
6461  C CA  . ASP A 884  ? 0.2282 0.2115 0.2375 0.0331  0.0077  -0.0193 882  ASP A CA  
6462  C C   . ASP A 884  ? 0.2599 0.2428 0.2702 0.0340  0.0059  -0.0230 882  ASP A C   
6463  O O   . ASP A 884  ? 0.3020 0.2864 0.3087 0.0337  0.0066  -0.0229 882  ASP A O   
6464  C CB  . ASP A 884  ? 0.2540 0.2320 0.2646 0.0300  0.0071  -0.0154 882  ASP A CB  
6465  C CG  . ASP A 884  ? 0.2239 0.2022 0.2337 0.0289  0.0086  -0.0119 882  ASP A CG  
6466  O OD1 . ASP A 884  ? 0.2648 0.2463 0.2709 0.0290  0.0108  -0.0101 882  ASP A OD1 
6467  O OD2 . ASP A 884  ? 0.2427 0.2183 0.2560 0.0281  0.0076  -0.0108 882  ASP A OD2 
6468  N N   . VAL A 885  ? 0.2359 0.2165 0.2514 0.0349  0.0035  -0.0262 883  VAL A N   
6469  C CA  . VAL A 885  ? 0.2483 0.2273 0.2660 0.0354  0.0012  -0.0296 883  VAL A CA  
6470  C C   . VAL A 885  ? 0.2306 0.2121 0.2520 0.0386  -0.0003 -0.0353 883  VAL A C   
6471  O O   . VAL A 885  ? 0.2279 0.2081 0.2540 0.0393  -0.0014 -0.0361 883  VAL A O   
6472  C CB  . VAL A 885  ? 0.2589 0.2316 0.2807 0.0327  -0.0010 -0.0274 883  VAL A CB  
6473  C CG1 . VAL A 885  ? 0.2760 0.2470 0.3010 0.0332  -0.0035 -0.0310 883  VAL A CG1 
6474  C CG2 . VAL A 885  ? 0.2721 0.2430 0.2900 0.0296  0.0006  -0.0222 883  VAL A CG2 
6475  N N   . GLY A 886  ? 0.2353 0.2210 0.2549 0.0408  -0.0004 -0.0393 884  GLY A N   
6476  C CA  . GLY A 886  ? 0.2195 0.2085 0.2425 0.0442  -0.0019 -0.0455 884  GLY A CA  
6477  C C   . GLY A 886  ? 0.2161 0.2009 0.2451 0.0443  -0.0055 -0.0492 884  GLY A C   
6478  O O   . GLY A 886  ? 0.2245 0.2033 0.2562 0.0416  -0.0070 -0.0464 884  GLY A O   
6479  N N   . PRO A 887  ? 0.2159 0.2043 0.2476 0.0476  -0.0070 -0.0556 885  PRO A N   
6480  C CA  . PRO A 887  ? 0.2201 0.2046 0.2589 0.0481  -0.0108 -0.0599 885  PRO A CA  
6481  C C   . PRO A 887  ? 0.2261 0.2100 0.2628 0.0472  -0.0116 -0.0606 885  PRO A C   
6482  O O   . PRO A 887  ? 0.2289 0.2163 0.2586 0.0469  -0.0093 -0.0588 885  PRO A O   
6483  C CB  . PRO A 887  ? 0.2193 0.2094 0.2607 0.0524  -0.0118 -0.0671 885  PRO A CB  
6484  C CG  . PRO A 887  ? 0.2508 0.2492 0.2841 0.0540  -0.0083 -0.0670 885  PRO A CG  
6485  C CD  . PRO A 887  ? 0.2374 0.2341 0.2661 0.0511  -0.0053 -0.0595 885  PRO A CD  
6486  N N   . VAL A 888  ? 0.2367 0.2159 0.2801 0.0468  -0.0152 -0.0630 886  VAL A N   
6487  C CA  . VAL A 888  ? 0.2271 0.2069 0.2699 0.0471  -0.0165 -0.0658 886  VAL A CA  
6488  C C   . VAL A 888  ? 0.2359 0.2219 0.2796 0.0513  -0.0176 -0.0738 886  VAL A C   
6489  O O   . VAL A 888  ? 0.2451 0.2334 0.2923 0.0539  -0.0183 -0.0777 886  VAL A O   
6490  C CB  . VAL A 888  ? 0.2535 0.2261 0.3030 0.0446  -0.0199 -0.0646 886  VAL A CB  
6491  C CG1 . VAL A 888  ? 0.2649 0.2329 0.3125 0.0405  -0.0184 -0.0566 886  VAL A CG1 
6492  C CG2 . VAL A 888  ? 0.2860 0.2554 0.3455 0.0459  -0.0236 -0.0685 886  VAL A CG2 
6493  N N   . ILE A 889  ? 0.2441 0.2334 0.2844 0.0520  -0.0177 -0.0763 887  ILE A N   
6494  C CA  . ILE A 889  ? 0.2542 0.2517 0.2922 0.0560  -0.0175 -0.0829 887  ILE A CA  
6495  C C   . ILE A 889  ? 0.2654 0.2629 0.3119 0.0590  -0.0213 -0.0906 887  ILE A C   
6496  O O   . ILE A 889  ? 0.2518 0.2561 0.2980 0.0626  -0.0210 -0.0961 887  ILE A O   
6497  C CB  . ILE A 889  ? 0.2507 0.2523 0.2826 0.0561  -0.0166 -0.0833 887  ILE A CB  
6498  C CG1 . ILE A 889  ? 0.2533 0.2650 0.2817 0.0601  -0.0158 -0.0893 887  ILE A CG1 
6499  C CG2 . ILE A 889  ? 0.2501 0.2463 0.2868 0.0546  -0.0199 -0.0848 887  ILE A CG2 
6500  C CD1 . ILE A 889  ? 0.2686 0.2868 0.2920 0.0614  -0.0123 -0.0873 887  ILE A CD1 
6501  N N   . THR A 890  ? 0.2459 0.2362 0.3004 0.0576  -0.0250 -0.0915 888  THR A N   
6502  C CA  . THR A 890  ? 0.2490 0.2387 0.3125 0.0604  -0.0290 -0.0991 888  THR A CA  
6503  C C   . THR A 890  ? 0.2430 0.2235 0.3161 0.0580  -0.0323 -0.0967 888  THR A C   
6504  O O   . THR A 890  ? 0.2616 0.2365 0.3341 0.0541  -0.0316 -0.0895 888  THR A O   
6505  C CB  . THR A 890  ? 0.2740 0.2660 0.3388 0.0619  -0.0315 -0.1051 888  THR A CB  
6506  O OG1 . THR A 890  ? 0.2890 0.2748 0.3543 0.0582  -0.0325 -0.1005 888  THR A OG1 
6507  C CG2 . THR A 890  ? 0.3069 0.3089 0.3628 0.0645  -0.0288 -0.1081 888  THR A CG2 
6508  N N   . SER A 891  ? 0.2815 0.2609 0.3641 0.0604  -0.0359 -0.1029 889  SER A N   
6509  C CA  A SER A 891  ? 0.3047 0.2756 0.3980 0.0584  -0.0398 -0.1012 889  SER A CA  
6510  C CA  B SER A 891  ? 0.3043 0.2751 0.3974 0.0583  -0.0397 -0.1010 889  SER A CA  
6511  C C   . SER A 891  ? 0.3089 0.2749 0.4047 0.0555  -0.0420 -0.0992 889  SER A C   
6512  O O   . SER A 891  ? 0.3198 0.2788 0.4203 0.0520  -0.0434 -0.0934 889  SER A O   
6513  C CB  A SER A 891  ? 0.3358 0.3069 0.4393 0.0619  -0.0437 -0.1093 889  SER A CB  
6514  C CB  B SER A 891  ? 0.3363 0.3071 0.4396 0.0618  -0.0436 -0.1088 889  SER A CB  
6515  O OG  A SER A 891  ? 0.3552 0.3309 0.4570 0.0646  -0.0418 -0.1112 889  SER A OG  
6516  O OG  B SER A 891  ? 0.3713 0.3468 0.4758 0.0651  -0.0455 -0.1173 889  SER A OG  
6517  N N   . GLU A 892  ? 0.2858 0.2557 0.3787 0.0571  -0.0424 -0.1038 890  GLU A N   
6518  C CA  . GLU A 892  ? 0.3083 0.2741 0.4035 0.0545  -0.0445 -0.1022 890  GLU A CA  
6519  C C   . GLU A 892  ? 0.3435 0.3069 0.4314 0.0503  -0.0412 -0.0931 890  GLU A C   
6520  O O   . GLU A 892  ? 0.3335 0.2910 0.4258 0.0469  -0.0429 -0.0884 890  GLU A O   
6521  C CB  . GLU A 892  ? 0.3318 0.3032 0.4246 0.0573  -0.0454 -0.1094 890  GLU A CB  
6522  C CG  . GLU A 892  ? 0.4045 0.3778 0.5060 0.0614  -0.0495 -0.1193 890  GLU A CG  
6523  C CD  . GLU A 892  ? 0.5242 0.5040 0.6238 0.0653  -0.0480 -0.1241 890  GLU A CD  
6524  O OE1 . GLU A 892  ? 0.3792 0.3646 0.4685 0.0657  -0.0434 -0.1214 890  GLU A OE1 
6525  O OE2 . GLU A 892  ? 0.5597 0.5399 0.6678 0.0674  -0.0513 -0.1295 890  GLU A OE2 
6526  N N   . ALA A 893  ? 0.3039 0.2724 0.3812 0.0506  -0.0366 -0.0904 891  ALA A N   
6527  C CA  . ALA A 893  ? 0.2915 0.2579 0.3623 0.0468  -0.0335 -0.0819 891  ALA A CA  
6528  C C   . ALA A 893  ? 0.3096 0.2701 0.3849 0.0440  -0.0338 -0.0759 891  ALA A C   
6529  O O   . ALA A 893  ? 0.3166 0.2726 0.3927 0.0403  -0.0340 -0.0701 891  ALA A O   
6530  C CB  . ALA A 893  ? 0.2832 0.2561 0.3429 0.0478  -0.0289 -0.0804 891  ALA A CB  
6531  N N   . LYS A 894  ? 0.2722 0.2330 0.3507 0.0457  -0.0341 -0.0774 892  LYS A N   
6532  C CA  . LYS A 894  ? 0.2880 0.2434 0.3714 0.0433  -0.0347 -0.0721 892  LYS A CA  
6533  C C   . LYS A 894  ? 0.3238 0.2728 0.4173 0.0410  -0.0390 -0.0707 892  LYS A C   
6534  O O   . LYS A 894  ? 0.3151 0.2600 0.4095 0.0373  -0.0388 -0.0638 892  LYS A O   
6535  C CB  . LYS A 894  ? 0.2638 0.2209 0.3504 0.0461  -0.0349 -0.0753 892  LYS A CB  
6536  C CG  . LYS A 894  ? 0.2958 0.2476 0.3885 0.0439  -0.0361 -0.0703 892  LYS A CG  
6537  C CD  . LYS A 894  ? 0.3100 0.2640 0.4052 0.0469  -0.0360 -0.0736 892  LYS A CD  
6538  C CE  . LYS A 894  ? 0.3439 0.2926 0.4459 0.0448  -0.0375 -0.0687 892  LYS A CE  
6539  N NZ  . LYS A 894  ? 0.5130 0.4634 0.6192 0.0479  -0.0381 -0.0726 892  LYS A NZ  
6540  N N   . ASP A 895  ? 0.2940 0.2423 0.3953 0.0432  -0.0430 -0.0774 893  ASP A N   
6541  C CA  . ASP A 895  ? 0.3594 0.3016 0.4715 0.0410  -0.0474 -0.0762 893  ASP A CA  
6542  C C   . ASP A 895  ? 0.3140 0.2543 0.4231 0.0375  -0.0469 -0.0712 893  ASP A C   
6543  O O   . ASP A 895  ? 0.3573 0.2928 0.4720 0.0340  -0.0486 -0.0655 893  ASP A O   
6544  C CB  . ASP A 895  ? 0.3394 0.2817 0.4603 0.0443  -0.0518 -0.0851 893  ASP A CB  
6545  C CG  . ASP A 895  ? 0.4008 0.3443 0.5268 0.0478  -0.0531 -0.0903 893  ASP A CG  
6546  O OD1 . ASP A 895  ? 0.4967 0.4389 0.6226 0.0469  -0.0517 -0.0859 893  ASP A OD1 
6547  O OD2 . ASP A 895  ? 0.4536 0.3997 0.5840 0.0515  -0.0556 -0.0989 893  ASP A OD2 
6548  N N   . ASN A 896  ? 0.3037 0.2483 0.4045 0.0383  -0.0446 -0.0731 894  ASN A N   
6549  C CA  . ASN A 896  ? 0.2995 0.2428 0.3973 0.0352  -0.0440 -0.0687 894  ASN A CA  
6550  C C   . ASN A 896  ? 0.3423 0.2842 0.4350 0.0315  -0.0409 -0.0599 894  ASN A C   
6551  O O   . ASN A 896  ? 0.3232 0.2619 0.4188 0.0281  -0.0418 -0.0547 894  ASN A O   
6552  C CB  . ASN A 896  ? 0.3240 0.2727 0.4134 0.0370  -0.0419 -0.0725 894  ASN A CB  
6553  C CG  . ASN A 896  ? 0.4732 0.4211 0.5588 0.0339  -0.0409 -0.0679 894  ASN A CG  
6554  O OD1 . ASN A 896  ? 0.5316 0.4812 0.6086 0.0323  -0.0370 -0.0630 894  ASN A OD1 
6555  N ND2 . ASN A 896  ? 0.4691 0.4143 0.5614 0.0330  -0.0444 -0.0695 894  ASN A ND2 
6556  N N   . ILE A 897  ? 0.3062 0.2510 0.3915 0.0323  -0.0372 -0.0583 895  ILE A N   
6557  C CA  . ILE A 897  ? 0.3070 0.2509 0.3874 0.0291  -0.0342 -0.0505 895  ILE A CA  
6558  C C   . ILE A 897  ? 0.3137 0.2529 0.4024 0.0268  -0.0366 -0.0461 895  ILE A C   
6559  O O   . ILE A 897  ? 0.3045 0.2417 0.3935 0.0232  -0.0363 -0.0397 895  ILE A O   
6560  C CB  . ILE A 897  ? 0.2632 0.2113 0.3349 0.0307  -0.0301 -0.0502 895  ILE A CB  
6561  C CG1 . ILE A 897  ? 0.2978 0.2511 0.3614 0.0328  -0.0279 -0.0537 895  ILE A CG1 
6562  C CG2 . ILE A 897  ? 0.3062 0.2533 0.3736 0.0276  -0.0275 -0.0426 895  ILE A CG2 
6563  C CD1 . ILE A 897  ? 0.2622 0.2204 0.3195 0.0354  -0.0248 -0.0554 895  ILE A CD1 
6564  N N   . GLU A 898  ? 0.2907 0.2284 0.3864 0.0287  -0.0390 -0.0492 896  GLU A N   
6565  C CA  . GLU A 898  ? 0.3062 0.2396 0.4102 0.0266  -0.0413 -0.0448 896  GLU A CA  
6566  C C   . GLU A 898  ? 0.3326 0.2621 0.4452 0.0239  -0.0451 -0.0425 896  GLU A C   
6567  O O   . GLU A 898  ? 0.3319 0.2588 0.4482 0.0206  -0.0459 -0.0358 896  GLU A O   
6568  C CB  . GLU A 898  ? 0.3219 0.2547 0.4320 0.0295  -0.0432 -0.0491 896  GLU A CB  
6569  C CG  . GLU A 898  ? 0.3441 0.2807 0.4463 0.0312  -0.0393 -0.0492 896  GLU A CG  
6570  C CD  . GLU A 898  ? 0.4087 0.3452 0.5170 0.0342  -0.0410 -0.0534 896  GLU A CD  
6571  O OE1 . GLU A 898  ? 0.4810 0.4160 0.5980 0.0362  -0.0449 -0.0591 896  GLU A OE1 
6572  O OE2 . GLU A 898  ? 0.5734 0.5113 0.6780 0.0345  -0.0386 -0.0512 896  GLU A OE2 
6573  N N   . LYS A 899  ? 0.3037 0.2330 0.4197 0.0253  -0.0475 -0.0478 897  LYS A N   
6574  C CA  . LYS A 899  ? 0.3254 0.2511 0.4495 0.0227  -0.0510 -0.0455 897  LYS A CA  
6575  C C   . LYS A 899  ? 0.3445 0.2709 0.4630 0.0188  -0.0486 -0.0382 897  LYS A C   
6576  O O   . LYS A 899  ? 0.3453 0.2691 0.4698 0.0154  -0.0505 -0.0324 897  LYS A O   
6577  C CB  . LYS A 899  ? 0.3574 0.2837 0.4846 0.0250  -0.0536 -0.0529 897  LYS A CB  
6578  N N   . HIS A 900  ? 0.3012 0.2314 0.4081 0.0192  -0.0443 -0.0382 898  HIS A N   
6579  C CA  . HIS A 900  ? 0.3306 0.2620 0.4317 0.0158  -0.0418 -0.0318 898  HIS A CA  
6580  C C   . HIS A 900  ? 0.2990 0.2297 0.3999 0.0132  -0.0405 -0.0247 898  HIS A C   
6581  O O   . HIS A 900  ? 0.3413 0.2712 0.4445 0.0097  -0.0410 -0.0186 898  HIS A O   
6582  C CB  . HIS A 900  ? 0.2870 0.2226 0.3764 0.0172  -0.0376 -0.0336 898  HIS A CB  
6583  C CG  . HIS A 900  ? 0.3071 0.2442 0.3899 0.0141  -0.0346 -0.0274 898  HIS A CG  
6584  N ND1 . HIS A 900  ? 0.3146 0.2514 0.3985 0.0117  -0.0353 -0.0249 898  HIS A ND1 
6585  C CD2 . HIS A 900  ? 0.3130 0.2519 0.3886 0.0132  -0.0310 -0.0233 898  HIS A CD2 
6586  C CE1 . HIS A 900  ? 0.3184 0.2573 0.3958 0.0095  -0.0322 -0.0198 898  HIS A CE1 
6587  N NE2 . HIS A 900  ? 0.2906 0.2306 0.3630 0.0103  -0.0296 -0.0188 898  HIS A NE2 
6588  N N   . ILE A 901  ? 0.2760 0.2074 0.3740 0.0149  -0.0388 -0.0253 899  ILE A N   
6589  C CA  . ILE A 901  ? 0.3157 0.2468 0.4132 0.0126  -0.0376 -0.0189 899  ILE A CA  
6590  C C   . ILE A 901  ? 0.3270 0.2546 0.4357 0.0101  -0.0416 -0.0149 899  ILE A C   
6591  O O   . ILE A 901  ? 0.3612 0.2889 0.4701 0.0067  -0.0412 -0.0080 899  ILE A O   
6592  C CB  . ILE A 901  ? 0.2624 0.1947 0.3563 0.0151  -0.0357 -0.0209 899  ILE A CB  
6593  C CG1 . ILE A 901  ? 0.3179 0.2542 0.4007 0.0169  -0.0316 -0.0236 899  ILE A CG1 
6594  C CG2 . ILE A 901  ? 0.3226 0.2543 0.4173 0.0127  -0.0350 -0.0145 899  ILE A CG2 
6595  C CD1 . ILE A 901  ? 0.2703 0.2084 0.3499 0.0198  -0.0298 -0.0265 899  ILE A CD1 
6596  N N   . GLU A 902  ? 0.3567 0.2813 0.4750 0.0118  -0.0456 -0.0191 900  GLU A N   
6597  C CA  . GLU A 902  ? 0.3700 0.2910 0.5001 0.0096  -0.0498 -0.0152 900  GLU A CA  
6598  C C   . GLU A 902  ? 0.3663 0.2866 0.5002 0.0063  -0.0515 -0.0112 900  GLU A C   
6599  O O   . GLU A 902  ? 0.4424 0.3617 0.5822 0.0030  -0.0532 -0.0044 900  GLU A O   
6600  C CB  . GLU A 902  ? 0.4355 0.3534 0.5757 0.0125  -0.0539 -0.0213 900  GLU A CB  
6601  C CG  . GLU A 902  ? 0.4610 0.3794 0.5994 0.0152  -0.0527 -0.0236 900  GLU A CG  
6602  C CD  . GLU A 902  ? 0.4890 0.4078 0.6255 0.0126  -0.0510 -0.0160 900  GLU A CD  
6603  O OE1 . GLU A 902  ? 0.5097 0.4263 0.6539 0.0095  -0.0536 -0.0100 900  GLU A OE1 
6604  O OE2 . GLU A 902  ? 0.5005 0.4221 0.6277 0.0135  -0.0471 -0.0158 900  GLU A OE2 
6605  N N   . ARG A 903  ? 0.3783 0.2997 0.5091 0.0072  -0.0511 -0.0151 901  ARG A N   
6606  C CA  . ARG A 903  ? 0.3984 0.3199 0.5313 0.0040  -0.0520 -0.0111 901  ARG A CA  
6607  C C   . ARG A 903  ? 0.4521 0.3767 0.5783 0.0006  -0.0487 -0.0033 901  ARG A C   
6608  O O   . ARG A 903  ? 0.4647 0.3891 0.5964 -0.0029 -0.0503 0.0032  901  ARG A O   
6609  C CB  . ARG A 903  ? 0.4396 0.3625 0.5684 0.0056  -0.0515 -0.0167 901  ARG A CB  
6610  N N   . MET A 904  ? 0.4014 0.3291 0.5161 0.0016  -0.0442 -0.0038 902  MET A N   
6611  C CA  . MET A 904  ? 0.4050 0.3359 0.5132 -0.0012 -0.0410 0.0028  902  MET A CA  
6612  C C   . MET A 904  ? 0.3990 0.3293 0.5124 -0.0033 -0.0422 0.0088  902  MET A C   
6613  O O   . MET A 904  ? 0.3989 0.3310 0.5133 -0.0068 -0.0421 0.0156  902  MET A O   
6614  C CB  . MET A 904  ? 0.3492 0.2830 0.4454 0.0007  -0.0364 0.0005  902  MET A CB  
6615  C CG  . MET A 904  ? 0.3322 0.2675 0.4224 0.0025  -0.0348 -0.0043 902  MET A CG  
6616  S SD  . MET A 904  ? 0.4853 0.4226 0.5748 -0.0008 -0.0346 -0.0003 902  MET A SD  
6617  C CE  . MET A 904  ? 0.4966 0.4308 0.5953 0.0001  -0.0390 -0.0049 902  MET A CE  
6618  N N   . ARG A 905  ? 0.3693 0.2973 0.4859 -0.0012 -0.0434 0.0065  903  ARG A N   
6619  C CA  . ARG A 905  ? 0.3776 0.3049 0.4996 -0.0031 -0.0447 0.0121  903  ARG A CA  
6620  C C   . ARG A 905  ? 0.4815 0.4068 0.6153 -0.0059 -0.0491 0.0166  903  ARG A C   
6621  O O   . ARG A 905  ? 0.4245 0.3512 0.5608 -0.0091 -0.0495 0.0240  903  ARG A O   
6622  C CB  . ARG A 905  ? 0.3887 0.3138 0.5130 0.0000  -0.0455 0.0080  903  ARG A CB  
6623  C CG  . ARG A 905  ? 0.4761 0.4016 0.6015 -0.0015 -0.0453 0.0135  903  ARG A CG  
6624  C CD  . ARG A 905  ? 0.4847 0.4074 0.6154 0.0014  -0.0471 0.0095  903  ARG A CD  
6625  N NE  . ARG A 905  ? 0.4526 0.3760 0.5766 0.0054  -0.0448 0.0020  903  ARG A NE  
6626  C CZ  . ARG A 905  ? 0.4254 0.3513 0.5405 0.0066  -0.0411 0.0014  903  ARG A CZ  
6627  N NH1 . ARG A 905  ? 0.4276 0.3556 0.5387 0.0044  -0.0390 0.0074  903  ARG A NH1 
6628  N NH2 . ARG A 905  ? 0.4543 0.3812 0.5648 0.0102  -0.0394 -0.0053 903  ARG A NH2 
6629  N N   . GLY A 906  ? 0.4310 0.3532 0.5722 -0.0049 -0.0525 0.0124  904  GLY A N   
6630  C CA  . GLY A 906  ? 0.5108 0.4308 0.6639 -0.0075 -0.0569 0.0164  904  GLY A CA  
6631  C C   . GLY A 906  ? 0.5420 0.4655 0.6933 -0.0114 -0.0559 0.0229  904  GLY A C   
6632  O O   . GLY A 906  ? 0.6117 0.5348 0.7720 -0.0146 -0.0589 0.0291  904  GLY A O   
6633  N N   . LEU A 907  ? 0.5161 0.4430 0.6563 -0.0112 -0.0519 0.0216  905  LEU A N   
6634  C CA  . LEU A 907  ? 0.5177 0.4486 0.6552 -0.0146 -0.0504 0.0273  905  LEU A CA  
6635  C C   . LEU A 907  ? 0.4979 0.4333 0.6304 -0.0171 -0.0478 0.0344  905  LEU A C   
6636  O O   . LEU A 907  ? 0.5206 0.4603 0.6501 -0.0199 -0.0463 0.0392  905  LEU A O   
6637  C CB  . LEU A 907  ? 0.4799 0.4129 0.6083 -0.0133 -0.0474 0.0228  905  LEU A CB  
6638  C CG  . LEU A 907  ? 0.5258 0.4555 0.6585 -0.0111 -0.0499 0.0160  905  LEU A CG  
6639  C CD1 . LEU A 907  ? 0.5680 0.5004 0.6917 -0.0103 -0.0470 0.0130  905  LEU A CD1 
6640  C CD2 . LEU A 907  ? 0.6059 0.5331 0.7518 -0.0134 -0.0549 0.0189  905  LEU A CD2 
6641  N N   . GLY A 908  ? 0.4481 0.3828 0.5795 -0.0161 -0.0472 0.0348  906  GLY A N   
6642  C CA  . GLY A 908  ? 0.4516 0.3906 0.5783 -0.0182 -0.0449 0.0410  906  GLY A CA  
6643  C C   . GLY A 908  ? 0.3653 0.3074 0.4789 -0.0167 -0.0399 0.0386  906  GLY A C   
6644  O O   . GLY A 908  ? 0.3786 0.3245 0.4878 -0.0182 -0.0379 0.0431  906  GLY A O   
6645  N N   . ARG A 909  ? 0.3796 0.3205 0.4873 -0.0138 -0.0381 0.0318  907  ARG A N   
6646  C CA  . ARG A 909  ? 0.3209 0.2648 0.4169 -0.0125 -0.0336 0.0297  907  ARG A CA  
6647  C C   . ARG A 909  ? 0.3630 0.3062 0.4565 -0.0109 -0.0325 0.0291  907  ARG A C   
6648  O O   . ARG A 909  ? 0.3759 0.3154 0.4750 -0.0091 -0.0348 0.0266  907  ARG A O   
6649  C CB  . ARG A 909  ? 0.3307 0.2735 0.4219 -0.0097 -0.0324 0.0228  907  ARG A CB  
6650  C CG  . ARG A 909  ? 0.3765 0.3194 0.4706 -0.0109 -0.0338 0.0225  907  ARG A CG  
6651  C CD  . ARG A 909  ? 0.4228 0.3706 0.5131 -0.0140 -0.0318 0.0278  907  ARG A CD  
6652  N NE  . ARG A 909  ? 0.4074 0.3556 0.4991 -0.0147 -0.0326 0.0268  907  ARG A NE  
6653  C CZ  . ARG A 909  ? 0.5505 0.4989 0.6503 -0.0174 -0.0354 0.0307  907  ARG A CZ  
6654  N NH1 . ARG A 909  ? 0.5148 0.4630 0.6223 -0.0196 -0.0379 0.0362  907  ARG A NH1 
6655  N NH2 . ARG A 909  ? 0.5212 0.4702 0.6216 -0.0178 -0.0358 0.0294  907  ARG A NH2 
6656  N N   . LYS A 910  ? 0.2854 0.2324 0.3708 -0.0116 -0.0292 0.0313  908  LYS A N   
6657  C CA  . LYS A 910  ? 0.2930 0.2400 0.3755 -0.0102 -0.0278 0.0309  908  LYS A CA  
6658  C C   . LYS A 910  ? 0.2832 0.2280 0.3613 -0.0064 -0.0264 0.0239  908  LYS A C   
6659  O O   . LYS A 910  ? 0.2785 0.2245 0.3499 -0.0053 -0.0240 0.0207  908  LYS A O   
6660  C CB  . LYS A 910  ? 0.3368 0.2887 0.4118 -0.0119 -0.0247 0.0347  908  LYS A CB  
6661  C CG  . LYS A 910  ? 0.4294 0.3845 0.5084 -0.0153 -0.0260 0.0421  908  LYS A CG  
6662  C CD  . LYS A 910  ? 0.4522 0.4124 0.5237 -0.0164 -0.0229 0.0447  908  LYS A CD  
6663  C CE  . LYS A 910  ? 0.4677 0.4263 0.5356 -0.0140 -0.0215 0.0420  908  LYS A CE  
6664  N NZ  . LYS A 910  ? 0.5670 0.5305 0.6295 -0.0153 -0.0193 0.0452  908  LYS A NZ  
6665  N N   . VAL A 911  ? 0.2912 0.2330 0.3732 -0.0044 -0.0278 0.0216  909  VAL A N   
6666  C CA  . VAL A 911  ? 0.2821 0.2223 0.3612 -0.0007 -0.0268 0.0150  909  VAL A CA  
6667  C C   . VAL A 911  ? 0.2984 0.2393 0.3746 0.0004  -0.0252 0.0153  909  VAL A C   
6668  O O   . VAL A 911  ? 0.3153 0.2549 0.3972 -0.0003 -0.0272 0.0180  909  VAL A O   
6669  C CB  . VAL A 911  ? 0.3171 0.2535 0.4047 0.0012  -0.0304 0.0107  909  VAL A CB  
6670  C CG1 . VAL A 911  ? 0.3111 0.2471 0.3953 0.0051  -0.0292 0.0038  909  VAL A CG1 
6671  C CG2 . VAL A 911  ? 0.3082 0.2439 0.3994 -0.0001 -0.0323 0.0105  909  VAL A CG2 
6672  N N   . GLU A 912  ? 0.2648 0.2078 0.3324 0.0020  -0.0218 0.0128  910  GLU A N   
6673  C CA  . GLU A 912  ? 0.2975 0.2412 0.3618 0.0034  -0.0200 0.0124  910  GLU A CA  
6674  C C   . GLU A 912  ? 0.2733 0.2160 0.3367 0.0071  -0.0196 0.0060  910  GLU A C   
6675  O O   . GLU A 912  ? 0.2664 0.2099 0.3258 0.0084  -0.0185 0.0025  910  GLU A O   
6676  C CB  . GLU A 912  ? 0.2915 0.2387 0.3470 0.0024  -0.0165 0.0144  910  GLU A CB  
6677  C CG  . GLU A 912  ? 0.2871 0.2354 0.3395 0.0032  -0.0147 0.0149  910  GLU A CG  
6678  C CD  . GLU A 912  ? 0.3398 0.2883 0.3963 0.0010  -0.0161 0.0200  910  GLU A CD  
6679  O OE1 . GLU A 912  ? 0.3465 0.2951 0.4069 -0.0015 -0.0179 0.0238  910  GLU A OE1 
6680  O OE2 . GLU A 912  ? 0.3281 0.2769 0.3841 0.0018  -0.0155 0.0204  910  GLU A OE2 
6681  N N   . GLN A 913  ? 0.2680 0.2094 0.3352 0.0088  -0.0207 0.0046  911  GLN A N   
6682  C CA  . GLN A 913  ? 0.3042 0.2456 0.3708 0.0124  -0.0204 -0.0015 911  GLN A CA  
6683  C C   . GLN A 913  ? 0.3225 0.2649 0.3874 0.0138  -0.0189 -0.0015 911  GLN A C   
6684  O O   . GLN A 913  ? 0.3295 0.2710 0.3980 0.0124  -0.0200 0.0021  911  GLN A O   
6685  C CB  . GLN A 913  ? 0.2954 0.2339 0.3708 0.0139  -0.0241 -0.0052 911  GLN A CB  
6686  C CG  . GLN A 913  ? 0.3285 0.2659 0.4060 0.0131  -0.0257 -0.0063 911  GLN A CG  
6687  C CD  . GLN A 913  ? 0.3374 0.2724 0.4232 0.0153  -0.0293 -0.0114 911  GLN A CD  
6688  O OE1 . GLN A 913  ? 0.3704 0.3027 0.4649 0.0151  -0.0324 -0.0105 911  GLN A OE1 
6689  N NE2 . GLN A 913  ? 0.3189 0.2550 0.4023 0.0176  -0.0289 -0.0169 911  GLN A NE2 
6690  N N   . ILE A 914  ? 0.3220 0.2667 0.3815 0.0164  -0.0165 -0.0054 912  ILE A N   
6691  C CA  . ILE A 914  ? 0.2954 0.2414 0.3540 0.0182  -0.0153 -0.0064 912  ILE A CA  
6692  C C   . ILE A 914  ? 0.3340 0.2780 0.4009 0.0201  -0.0183 -0.0093 912  ILE A C   
6693  O O   . ILE A 914  ? 0.3226 0.2652 0.3941 0.0215  -0.0206 -0.0132 912  ILE A O   
6694  C CB  . ILE A 914  ? 0.3508 0.3003 0.4024 0.0206  -0.0123 -0.0101 912  ILE A CB  
6695  C CG1 . ILE A 914  ? 0.3820 0.3334 0.4258 0.0188  -0.0094 -0.0071 912  ILE A CG1 
6696  C CG2 . ILE A 914  ? 0.5228 0.4741 0.5744 0.0231  -0.0114 -0.0122 912  ILE A CG2 
6697  C CD1 . ILE A 914  ? 0.3895 0.3443 0.4273 0.0210  -0.0068 -0.0101 912  ILE A CD1 
6698  N N   . GLY A 915  ? 0.3640 0.3077 0.4333 0.0203  -0.0185 -0.0077 913  GLY A N   
6699  C CA  . GLY A 915  ? 0.3491 0.2915 0.4260 0.0227  -0.0210 -0.0113 913  GLY A CA  
6700  C C   . GLY A 915  ? 0.3576 0.3034 0.4310 0.0264  -0.0191 -0.0170 913  GLY A C   
6701  O O   . GLY A 915  ? 0.4426 0.3916 0.5091 0.0268  -0.0158 -0.0163 913  GLY A O   
6702  N N   . LEU A 916  ? 0.3469 0.2924 0.4255 0.0292  -0.0212 -0.0227 914  LEU A N   
6703  C CA  . LEU A 916  ? 0.3712 0.3208 0.4467 0.0329  -0.0197 -0.0286 914  LEU A CA  
6704  C C   . LEU A 916  ? 0.3746 0.3251 0.4547 0.0351  -0.0203 -0.0306 914  LEU A C   
6705  O O   . LEU A 916  ? 0.4155 0.3626 0.5039 0.0348  -0.0234 -0.0299 914  LEU A O   
6706  C CB  . LEU A 916  ? 0.3545 0.3044 0.4329 0.0349  -0.0216 -0.0345 914  LEU A CB  
6707  C CG  . LEU A 916  ? 0.3553 0.3048 0.4292 0.0332  -0.0210 -0.0334 914  LEU A CG  
6708  C CD1 . LEU A 916  ? 0.3994 0.3497 0.4762 0.0356  -0.0230 -0.0399 914  LEU A CD1 
6709  C CD2 . LEU A 916  ? 0.4057 0.3590 0.4691 0.0326  -0.0167 -0.0313 914  LEU A CD2 
6710  N N   . ALA A 917  ? 0.3323 0.2877 0.4072 0.0375  -0.0174 -0.0331 915  ALA A N   
6711  C CA  . ALA A 917  ? 0.3516 0.3089 0.4303 0.0400  -0.0177 -0.0355 915  ALA A CA  
6712  C C   . ALA A 917  ? 0.3731 0.3306 0.4592 0.0434  -0.0207 -0.0426 915  ALA A C   
6713  O O   . ALA A 917  ? 0.3688 0.3268 0.4549 0.0444  -0.0217 -0.0466 915  ALA A O   
6714  C CB  . ALA A 917  ? 0.3945 0.3576 0.4656 0.0415  -0.0137 -0.0360 915  ALA A CB  
6715  N N   . SER A 918  ? 0.3392 0.2964 0.4320 0.0452  -0.0223 -0.0445 916  SER A N   
6716  C CA  . SER A 918  ? 0.3945 0.3519 0.4954 0.0486  -0.0255 -0.0517 916  SER A CA  
6717  C C   . SER A 918  ? 0.3599 0.3241 0.4561 0.0522  -0.0236 -0.0584 916  SER A C   
6718  O O   . SER A 918  ? 0.3410 0.3057 0.4420 0.0546  -0.0261 -0.0647 916  SER A O   
6719  C CB  . SER A 918  ? 0.3812 0.3378 0.4896 0.0500  -0.0272 -0.0524 916  SER A CB  
6720  O OG  . SER A 918  ? 0.4547 0.4162 0.5573 0.0509  -0.0236 -0.0513 916  SER A OG  
6721  N N   . GLU A 919  ? 0.3957 0.3652 0.4828 0.0525  -0.0194 -0.0569 917  GLU A N   
6722  C CA  . GLU A 919  ? 0.3498 0.3269 0.4319 0.0558  -0.0174 -0.0624 917  GLU A CA  
6723  C C   . GLU A 919  ? 0.3629 0.3402 0.4423 0.0557  -0.0179 -0.0648 917  GLU A C   
6724  O O   . GLU A 919  ? 0.3483 0.3315 0.4258 0.0589  -0.0174 -0.0708 917  GLU A O   
6725  C CB  . GLU A 919  ? 0.3785 0.3609 0.4516 0.0554  -0.0128 -0.0588 917  GLU A CB  
6726  C CG  . GLU A 919  ? 0.4337 0.4186 0.5087 0.0567  -0.0117 -0.0583 917  GLU A CG  
6727  C CD  . GLU A 919  ? 0.5399 0.5186 0.6182 0.0536  -0.0126 -0.0522 917  GLU A CD  
6728  O OE1 . GLU A 919  ? 0.4891 0.4620 0.5680 0.0504  -0.0139 -0.0480 917  GLU A OE1 
6729  O OE2 . GLU A 919  ? 0.5954 0.5757 0.6758 0.0545  -0.0120 -0.0515 917  GLU A OE2 
6730  N N   . THR A 920  ? 0.3414 0.3130 0.4205 0.0522  -0.0189 -0.0604 918  THR A N   
6731  C CA  . THR A 920  ? 0.3108 0.2825 0.3876 0.0520  -0.0195 -0.0626 918  THR A CA  
6732  C C   . THR A 920  ? 0.2944 0.2649 0.3797 0.0545  -0.0237 -0.0695 918  THR A C   
6733  O O   . THR A 920  ? 0.2922 0.2645 0.3759 0.0554  -0.0242 -0.0732 918  THR A O   
6734  C CB  . THR A 920  ? 0.3101 0.2764 0.3846 0.0477  -0.0195 -0.0559 918  THR A CB  
6735  O OG1 . THR A 920  ? 0.3249 0.2846 0.4078 0.0457  -0.0228 -0.0533 918  THR A OG1 
6736  C CG2 . THR A 920  ? 0.2953 0.2632 0.3615 0.0455  -0.0155 -0.0497 918  THR A CG2 
6737  N N   . GLY A 921  ? 0.3282 0.2957 0.4229 0.0556  -0.0267 -0.0715 919  GLY A N   
6738  C CA  . GLY A 921  ? 0.3366 0.3021 0.4409 0.0577  -0.0311 -0.0781 919  GLY A CA  
6739  C C   . GLY A 921  ? 0.3011 0.2738 0.4039 0.0621  -0.0310 -0.0868 919  GLY A C   
6740  O O   . GLY A 921  ? 0.3332 0.3049 0.4416 0.0636  -0.0342 -0.0923 919  GLY A O   
6741  N N   . VAL A 922  ? 0.3141 0.2944 0.4097 0.0642  -0.0273 -0.0881 920  VAL A N   
6742  C CA  . VAL A 922  ? 0.3108 0.2993 0.4042 0.0685  -0.0268 -0.0961 920  VAL A CA  
6743  C C   . VAL A 922  ? 0.3097 0.3012 0.3953 0.0678  -0.0252 -0.0962 920  VAL A C   
6744  O O   . VAL A 922  ? 0.3178 0.3161 0.4018 0.0712  -0.0253 -0.1029 920  VAL A O   
6745  C CB  . VAL A 922  ? 0.2882 0.2850 0.3776 0.0713  -0.0236 -0.0977 920  VAL A CB  
6746  C CG1 . VAL A 922  ? 0.2849 0.2796 0.3834 0.0729  -0.0258 -0.0998 920  VAL A CG1 
6747  C CG2 . VAL A 922  ? 0.2980 0.2961 0.3777 0.0684  -0.0191 -0.0897 920  VAL A CG2 
6748  N N   . GLY A 923  ? 0.2730 0.2601 0.3538 0.0638  -0.0239 -0.0890 921  GLY A N   
6749  C CA  . GLY A 923  ? 0.2878 0.2768 0.3621 0.0630  -0.0228 -0.0889 921  GLY A CA  
6750  C C   . GLY A 923  ? 0.2597 0.2407 0.3378 0.0598  -0.0255 -0.0860 921  GLY A C   
6751  O O   . GLY A 923  ? 0.2940 0.2686 0.3811 0.0588  -0.0289 -0.0858 921  GLY A O   
6752  N N   . THR A 924  ? 0.2408 0.2223 0.3124 0.0580  -0.0241 -0.0837 922  THR A N   
6753  C CA  . THR A 924  ? 0.2553 0.2302 0.3299 0.0550  -0.0264 -0.0810 922  THR A CA  
6754  C C   . THR A 924  ? 0.2682 0.2407 0.3360 0.0510  -0.0234 -0.0724 922  THR A C   
6755  O O   . THR A 924  ? 0.2888 0.2647 0.3485 0.0504  -0.0207 -0.0709 922  THR A O   
6756  C CB  . THR A 924  ? 0.2606 0.2381 0.3349 0.0565  -0.0279 -0.0865 922  THR A CB  
6757  O OG1 . THR A 924  ? 0.2667 0.2517 0.3310 0.0579  -0.0244 -0.0872 922  THR A OG1 
6758  C CG2 . THR A 924  ? 0.3122 0.2909 0.3951 0.0603  -0.0317 -0.0952 922  THR A CG2 
6759  N N   . PHE A 925  ? 0.2500 0.2169 0.3214 0.0482  -0.0239 -0.0669 923  PHE A N   
6760  C CA  . PHE A 925  ? 0.2108 0.1757 0.2763 0.0445  -0.0213 -0.0591 923  PHE A CA  
6761  C C   . PHE A 925  ? 0.2572 0.2154 0.3274 0.0410  -0.0237 -0.0549 923  PHE A C   
6762  O O   . PHE A 925  ? 0.2826 0.2366 0.3620 0.0408  -0.0273 -0.0560 923  PHE A O   
6763  C CB  . PHE A 925  ? 0.2201 0.1852 0.2845 0.0441  -0.0193 -0.0553 923  PHE A CB  
6764  C CG  . PHE A 925  ? 0.2611 0.2332 0.3199 0.0469  -0.0163 -0.0577 923  PHE A CG  
6765  C CD1 . PHE A 925  ? 0.2496 0.2252 0.3124 0.0506  -0.0174 -0.0639 923  PHE A CD1 
6766  C CD2 . PHE A 925  ? 0.2304 0.2057 0.2804 0.0458  -0.0124 -0.0537 923  PHE A CD2 
6767  C CE1 . PHE A 925  ? 0.2568 0.2396 0.3145 0.0531  -0.0145 -0.0657 923  PHE A CE1 
6768  C CE2 . PHE A 925  ? 0.2476 0.2297 0.2929 0.0482  -0.0097 -0.0553 923  PHE A CE2 
6769  C CZ  . PHE A 925  ? 0.2311 0.2172 0.2801 0.0518  -0.0107 -0.0612 923  PHE A CZ  
6770  N N   . VAL A 926  ? 0.2525 0.2101 0.3165 0.0382  -0.0216 -0.0499 924  VAL A N   
6771  C CA  . VAL A 926  ? 0.2563 0.2088 0.3231 0.0344  -0.0229 -0.0445 924  VAL A CA  
6772  C C   . VAL A 926  ? 0.2413 0.1939 0.3022 0.0319  -0.0197 -0.0379 924  VAL A C   
6773  O O   . VAL A 926  ? 0.2554 0.2117 0.3083 0.0322  -0.0164 -0.0371 924  VAL A O   
6774  C CB  . VAL A 926  ? 0.2428 0.1949 0.3081 0.0333  -0.0235 -0.0450 924  VAL A CB  
6775  C CG1 . VAL A 926  ? 0.2845 0.2322 0.3519 0.0292  -0.0245 -0.0389 924  VAL A CG1 
6776  C CG2 . VAL A 926  ? 0.2810 0.2329 0.3527 0.0358  -0.0270 -0.0519 924  VAL A CG2 
6777  N N   . PRO A 927  ? 0.2521 0.2012 0.3171 0.0295  -0.0207 -0.0332 925  PRO A N   
6778  C CA  . PRO A 927  ? 0.2713 0.2209 0.3307 0.0272  -0.0179 -0.0274 925  PRO A CA  
6779  C C   . PRO A 927  ? 0.2575 0.2073 0.3115 0.0247  -0.0163 -0.0241 925  PRO A C   
6780  O O   . PRO A 927  ? 0.2702 0.2179 0.3272 0.0233  -0.0183 -0.0238 925  PRO A O   
6781  C CB  . PRO A 927  ? 0.3051 0.2509 0.3714 0.0252  -0.0201 -0.0235 925  PRO A CB  
6782  C CG  . PRO A 927  ? 0.3463 0.2888 0.4211 0.0251  -0.0241 -0.0254 925  PRO A CG  
6783  C CD  . PRO A 927  ? 0.2963 0.2408 0.3713 0.0286  -0.0247 -0.0328 925  PRO A CD  
6784  N N   . PRO A 928  ? 0.2686 0.2210 0.3149 0.0241  -0.0129 -0.0216 926  PRO A N   
6785  C CA  . PRO A 928  ? 0.2516 0.2040 0.2933 0.0215  -0.0115 -0.0179 926  PRO A CA  
6786  C C   . PRO A 928  ? 0.2283 0.1774 0.2747 0.0184  -0.0134 -0.0135 926  PRO A C   
6787  O O   . PRO A 928  ? 0.2541 0.2017 0.3044 0.0174  -0.0144 -0.0109 926  PRO A O   
6788  C CB  . PRO A 928  ? 0.2497 0.2047 0.2848 0.0213  -0.0081 -0.0154 926  PRO A CB  
6789  C CG  . PRO A 928  ? 0.2680 0.2258 0.3021 0.0246  -0.0072 -0.0195 926  PRO A CG  
6790  C CD  . PRO A 928  ? 0.2841 0.2399 0.3259 0.0260  -0.0103 -0.0225 926  PRO A CD  
6791  N N   . THR A 929  ? 0.2294 0.1778 0.2757 0.0167  -0.0141 -0.0127 927  THR A N   
6792  C CA  . THR A 929  ? 0.2544 0.2002 0.3062 0.0139  -0.0165 -0.0091 927  THR A CA  
6793  C C   . THR A 929  ? 0.2384 0.1856 0.2854 0.0114  -0.0148 -0.0056 927  THR A C   
6794  O O   . THR A 929  ? 0.2492 0.1981 0.2913 0.0122  -0.0133 -0.0077 927  THR A O   
6795  C CB  . THR A 929  ? 0.2611 0.2047 0.3198 0.0149  -0.0199 -0.0127 927  THR A CB  
6796  O OG1 . THR A 929  ? 0.2814 0.2241 0.3451 0.0174  -0.0215 -0.0163 927  THR A OG1 
6797  C CG2 . THR A 929  ? 0.2836 0.2247 0.3487 0.0118  -0.0225 -0.0086 927  THR A CG2 
6798  N N   . ILE A 930  ? 0.2337 0.1806 0.2822 0.0085  -0.0151 -0.0004 928  ILE A N   
6799  C CA  . ILE A 930  ? 0.2414 0.1899 0.2866 0.0059  -0.0139 0.0029  928  ILE A CA  
6800  C C   . ILE A 930  ? 0.2570 0.2040 0.3091 0.0036  -0.0168 0.0057  928  ILE A C   
6801  O O   . ILE A 930  ? 0.2730 0.2187 0.3308 0.0025  -0.0187 0.0085  928  ILE A O   
6802  C CB  . ILE A 930  ? 0.2319 0.1827 0.2723 0.0044  -0.0115 0.0068  928  ILE A CB  
6803  C CG1 . ILE A 930  ? 0.2770 0.2294 0.3110 0.0066  -0.0087 0.0043  928  ILE A CG1 
6804  C CG2 . ILE A 930  ? 0.2891 0.2422 0.3272 0.0018  -0.0106 0.0101  928  ILE A CG2 
6805  C CD1 . ILE A 930  ? 0.2846 0.2388 0.3153 0.0055  -0.0067 0.0076  928  ILE A CD1 
6806  N N   . ILE A 931  ? 0.2537 0.2011 0.3058 0.0028  -0.0173 0.0053  929  ILE A N   
6807  C CA  . ILE A 931  ? 0.2701 0.2163 0.3289 0.0004  -0.0201 0.0080  929  ILE A CA  
6808  C C   . ILE A 931  ? 0.2706 0.2199 0.3257 -0.0022 -0.0185 0.0118  929  ILE A C   
6809  O O   . ILE A 931  ? 0.2698 0.2208 0.3193 -0.0016 -0.0165 0.0098  929  ILE A O   
6810  C CB  . ILE A 931  ? 0.2906 0.2345 0.3542 0.0019  -0.0226 0.0036  929  ILE A CB  
6811  C CG1 . ILE A 931  ? 0.2818 0.2232 0.3493 0.0048  -0.0242 -0.0008 929  ILE A CG1 
6812  C CG2 . ILE A 931  ? 0.2992 0.2420 0.3703 -0.0008 -0.0255 0.0069  929  ILE A CG2 
6813  C CD1 . ILE A 931  ? 0.3109 0.2501 0.3839 0.0064  -0.0271 -0.0057 929  ILE A CD1 
6814  N N   . GLU A 932  ? 0.2756 0.2262 0.3339 -0.0051 -0.0193 0.0173  930  GLU A N   
6815  C CA  . GLU A 932  ? 0.2671 0.2216 0.3223 -0.0076 -0.0178 0.0210  930  GLU A CA  
6816  C C   . GLU A 932  ? 0.2598 0.2139 0.3203 -0.0092 -0.0201 0.0220  930  GLU A C   
6817  O O   . GLU A 932  ? 0.2952 0.2476 0.3637 -0.0106 -0.0232 0.0246  930  GLU A O   
6818  C CB  . GLU A 932  ? 0.2506 0.2078 0.3059 -0.0099 -0.0174 0.0265  930  GLU A CB  
6819  C CG  . GLU A 932  ? 0.2825 0.2407 0.3316 -0.0085 -0.0148 0.0255  930  GLU A CG  
6820  C CD  . GLU A 932  ? 0.3301 0.2905 0.3805 -0.0104 -0.0150 0.0304  930  GLU A CD  
6821  O OE1 . GLU A 932  ? 0.3458 0.3102 0.3962 -0.0131 -0.0148 0.0348  930  GLU A OE1 
6822  O OE2 . GLU A 932  ? 0.3154 0.2739 0.3667 -0.0092 -0.0153 0.0298  930  GLU A OE2 
6823  N N   . LEU A 933  ? 0.2787 0.2343 0.3352 -0.0090 -0.0188 0.0201  931  LEU A N   
6824  C CA  . LEU A 933  ? 0.2943 0.2498 0.3555 -0.0104 -0.0207 0.0206  931  LEU A CA  
6825  C C   . LEU A 933  ? 0.3498 0.3101 0.4097 -0.0135 -0.0196 0.0256  931  LEU A C   
6826  O O   . LEU A 933  ? 0.3284 0.2923 0.3821 -0.0139 -0.0169 0.0270  931  LEU A O   
6827  C CB  . LEU A 933  ? 0.3524 0.3067 0.4104 -0.0081 -0.0202 0.0151  931  LEU A CB  
6828  C CG  . LEU A 933  ? 0.3449 0.2955 0.4043 -0.0048 -0.0213 0.0095  931  LEU A CG  
6829  C CD1 . LEU A 933  ? 0.4140 0.3645 0.4705 -0.0030 -0.0209 0.0047  931  LEU A CD1 
6830  C CD2 . LEU A 933  ? 0.4034 0.3505 0.4725 -0.0052 -0.0252 0.0098  931  LEU A CD2 
6831  N N   . GLU A 934  ? 0.3593 0.3199 0.4256 -0.0155 -0.0220 0.0281  932  GLU A N   
6832  C CA  . GLU A 934  ? 0.4487 0.4145 0.5142 -0.0184 -0.0211 0.0326  932  GLU A CA  
6833  C C   . GLU A 934  ? 0.4636 0.4310 0.5241 -0.0176 -0.0192 0.0294  932  GLU A C   
6834  O O   . GLU A 934  ? 0.5359 0.5080 0.5908 -0.0184 -0.0166 0.0306  932  GLU A O   
6835  C CB  . GLU A 934  ? 0.4865 0.4523 0.5615 -0.0212 -0.0245 0.0373  932  GLU A CB  
6836  N N   . LYS A 935  ? 0.4605 0.4243 0.5229 -0.0159 -0.0207 0.0250  933  LYS A N   
6837  C CA  . LYS A 935  ? 0.5150 0.4801 0.5733 -0.0150 -0.0193 0.0219  933  LYS A CA  
6838  C C   . LYS A 935  ? 0.5170 0.4782 0.5728 -0.0116 -0.0193 0.0155  933  LYS A C   
6839  O O   . LYS A 935  ? 0.4590 0.4163 0.5188 -0.0102 -0.0214 0.0134  933  LYS A O   
6840  C CB  . LYS A 935  ? 0.5023 0.4682 0.5667 -0.0170 -0.0215 0.0237  933  LYS A CB  
6841  N N   . LEU A 936  ? 0.4820 0.4447 0.5314 -0.0102 -0.0171 0.0125  934  LEU A N   
6842  C CA  . LEU A 936  ? 0.5150 0.4751 0.5617 -0.0070 -0.0170 0.0068  934  LEU A CA  
6843  C C   . LEU A 936  ? 0.5528 0.5100 0.6059 -0.0064 -0.0203 0.0041  934  LEU A C   
6844  O O   . LEU A 936  ? 0.5323 0.4871 0.5851 -0.0037 -0.0211 -0.0006 934  LEU A O   
6845  C CB  . LEU A 936  ? 0.5144 0.4771 0.5539 -0.0059 -0.0143 0.0049  934  LEU A CB  
6846  C CG  . LEU A 936  ? 0.5695 0.5316 0.6029 -0.0030 -0.0123 0.0014  934  LEU A CG  
6847  C CD1 . LEU A 936  ? 0.4874 0.4525 0.5144 -0.0027 -0.0095 0.0011  934  LEU A CD1 
6848  C CD2 . LEU A 936  ? 0.5231 0.4825 0.5578 -0.0004 -0.0140 -0.0035 934  LEU A CD2 
6849  N N   . SER A 937  ? 0.5821 0.5399 0.6411 -0.0088 -0.0223 0.0069  935  SER A N   
6850  C CA  . SER A 937  ? 0.5640 0.5189 0.6302 -0.0085 -0.0258 0.0045  935  SER A CA  
6851  C C   . SER A 937  ? 0.5142 0.4652 0.5873 -0.0079 -0.0287 0.0037  935  SER A C   
6852  O O   . SER A 937  ? 0.5596 0.5078 0.6388 -0.0070 -0.0319 0.0006  935  SER A O   
6853  C CB  . SER A 937  ? 0.5834 0.5402 0.6545 -0.0116 -0.0272 0.0082  935  SER A CB  
6854  O OG  . SER A 937  ? 0.5913 0.5503 0.6650 -0.0145 -0.0271 0.0145  935  SER A OG  
6855  N N   . ASP A 938  ? 0.5381 0.4889 0.6107 -0.0083 -0.0280 0.0064  936  ASP A N   
6856  C CA  . ASP A 938  ? 0.5039 0.4510 0.5828 -0.0073 -0.0306 0.0053  936  ASP A CA  
6857  C C   . ASP A 938  ? 0.5591 0.5039 0.6361 -0.0035 -0.0309 -0.0017 936  ASP A C   
6858  O O   . ASP A 938  ? 0.5123 0.4540 0.5958 -0.0022 -0.0338 -0.0042 936  ASP A O   
6859  C CB  . ASP A 938  ? 0.5787 0.5265 0.6562 -0.0082 -0.0293 0.0093  936  ASP A CB  
6860  C CG  . ASP A 938  ? 0.5885 0.5392 0.6685 -0.0120 -0.0293 0.0165  936  ASP A CG  
6861  O OD1 . ASP A 938  ? 0.6042 0.5562 0.6878 -0.0140 -0.0305 0.0185  936  ASP A OD1 
6862  O OD2 . ASP A 938  ? 0.5751 0.5273 0.6536 -0.0130 -0.0281 0.0201  936  ASP A OD2 
6863  N N   . LEU A 939  ? 0.4987 0.4455 0.5673 -0.0015 -0.0281 -0.0050 937  LEU A N   
6864  C CA  . LEU A 939  ? 0.4985 0.4444 0.5647 0.0021  -0.0282 -0.0114 937  LEU A CA  
6865  C C   . LEU A 939  ? 0.5674 0.5132 0.6360 0.0029  -0.0301 -0.0154 937  LEU A C   
6866  O O   . LEU A 939  ? 0.5631 0.5105 0.6304 0.0013  -0.0296 -0.0136 937  LEU A O   
6867  C CB  . LEU A 939  ? 0.5017 0.4504 0.5580 0.0037  -0.0242 -0.0124 937  LEU A CB  
6868  C CG  . LEU A 939  ? 0.4879 0.4368 0.5414 0.0035  -0.0223 -0.0096 937  LEU A CG  
6869  C CD1 . LEU A 939  ? 0.4565 0.4075 0.5015 0.0059  -0.0191 -0.0120 937  LEU A CD1 
6870  C CD2 . LEU A 939  ? 0.4808 0.4267 0.5410 0.0042  -0.0248 -0.0104 937  LEU A CD2 
6871  N N   . GLN A 940  ? 0.5036 0.4476 0.5756 0.0056  -0.0325 -0.0210 938  GLN A N   
6872  C CA  . GLN A 940  ? 0.5021 0.4460 0.5767 0.0068  -0.0346 -0.0256 938  GLN A CA  
6873  C C   . GLN A 940  ? 0.5616 0.5081 0.6285 0.0102  -0.0327 -0.0310 938  GLN A C   
6874  O O   . GLN A 940  ? 0.6615 0.6104 0.7237 0.0102  -0.0314 -0.0315 938  GLN A O   
6875  C CB  . GLN A 940  ? 0.5282 0.4685 0.6134 0.0074  -0.0393 -0.0285 938  GLN A CB  
6876  N N   . ARG A 941  ? 0.4923 0.4389 0.5581 0.0130  -0.0326 -0.0347 939  ARG A N   
6877  C CA  . ARG A 941  ? 0.4319 0.3818 0.4908 0.0163  -0.0308 -0.0395 939  ARG A CA  
6878  C C   . ARG A 941  ? 0.3595 0.3108 0.4127 0.0175  -0.0278 -0.0384 939  ARG A C   
6879  O O   . ARG A 941  ? 0.3952 0.3446 0.4506 0.0161  -0.0276 -0.0349 939  ARG A O   
6880  C CB  . ARG A 941  ? 0.4676 0.4175 0.5312 0.0192  -0.0340 -0.0466 939  ARG A CB  
6881  N N   . GLU A 942  ? 0.3567 0.3117 0.4027 0.0199  -0.0256 -0.0412 940  GLU A N   
6882  C CA  . GLU A 942  ? 0.3143 0.2713 0.3551 0.0213  -0.0228 -0.0407 940  GLU A CA  
6883  C C   . GLU A 942  ? 0.2866 0.2418 0.3327 0.0228  -0.0246 -0.0431 940  GLU A C   
6884  O O   . GLU A 942  ? 0.3255 0.2803 0.3767 0.0247  -0.0275 -0.0483 940  GLU A O   
6885  C CB  . GLU A 942  ? 0.2952 0.2569 0.3292 0.0241  -0.0210 -0.0443 940  GLU A CB  
6886  C CG  . GLU A 942  ? 0.2728 0.2373 0.3015 0.0259  -0.0183 -0.0442 940  GLU A CG  
6887  C CD  . GLU A 942  ? 0.2852 0.2550 0.3085 0.0288  -0.0172 -0.0481 940  GLU A CD  
6888  O OE1 . GLU A 942  ? 0.3310 0.3023 0.3570 0.0310  -0.0195 -0.0535 940  GLU A OE1 
6889  O OE2 . GLU A 942  ? 0.2768 0.2495 0.2934 0.0289  -0.0143 -0.0456 940  GLU A OE2 
6890  N N   . VAL A 943  ? 0.2738 0.2280 0.3193 0.0219  -0.0231 -0.0394 941  VAL A N   
6891  C CA  . VAL A 943  ? 0.2571 0.2100 0.3068 0.0234  -0.0243 -0.0413 941  VAL A CA  
6892  C C   . VAL A 943  ? 0.3118 0.2685 0.3544 0.0255  -0.0211 -0.0421 941  VAL A C   
6893  O O   . VAL A 943  ? 0.2612 0.2183 0.2991 0.0241  -0.0183 -0.0376 941  VAL A O   
6894  C CB  . VAL A 943  ? 0.3187 0.2677 0.3738 0.0206  -0.0253 -0.0364 941  VAL A CB  
6895  C CG1 . VAL A 943  ? 0.3136 0.2615 0.3731 0.0223  -0.0265 -0.0383 941  VAL A CG1 
6896  C CG2 . VAL A 943  ? 0.3712 0.3170 0.4338 0.0184  -0.0286 -0.0353 941  VAL A CG2 
6897  N N   . PHE A 944  ? 0.2944 0.2542 0.3362 0.0289  -0.0215 -0.0478 942  PHE A N   
6898  C CA  . PHE A 944  ? 0.2614 0.2261 0.2960 0.0311  -0.0184 -0.0487 942  PHE A CA  
6899  C C   . PHE A 944  ? 0.2730 0.2374 0.3096 0.0321  -0.0180 -0.0487 942  PHE A C   
6900  O O   . PHE A 944  ? 0.2897 0.2562 0.3284 0.0350  -0.0191 -0.0536 942  PHE A O   
6901  C CB  . PHE A 944  ? 0.2552 0.2246 0.2880 0.0342  -0.0190 -0.0548 942  PHE A CB  
6902  C CG  . PHE A 944  ? 0.2509 0.2260 0.2753 0.0358  -0.0157 -0.0545 942  PHE A CG  
6903  C CD1 . PHE A 944  ? 0.2329 0.2090 0.2514 0.0341  -0.0133 -0.0504 942  PHE A CD1 
6904  C CD2 . PHE A 944  ? 0.2410 0.2210 0.2638 0.0390  -0.0150 -0.0583 942  PHE A CD2 
6905  C CE1 . PHE A 944  ? 0.2284 0.2099 0.2401 0.0354  -0.0105 -0.0497 942  PHE A CE1 
6906  C CE2 . PHE A 944  ? 0.2316 0.2176 0.2471 0.0402  -0.0120 -0.0575 942  PHE A CE2 
6907  C CZ  . PHE A 944  ? 0.2343 0.2207 0.2444 0.0384  -0.0098 -0.0530 942  PHE A CZ  
6908  N N   . GLY A 945  ? 0.2587 0.2205 0.2946 0.0296  -0.0166 -0.0431 943  GLY A N   
6909  C CA  . GLY A 945  ? 0.2544 0.2154 0.2925 0.0301  -0.0164 -0.0423 943  GLY A CA  
6910  C C   . GLY A 945  ? 0.2495 0.2090 0.2847 0.0273  -0.0141 -0.0358 943  GLY A C   
6911  O O   . GLY A 945  ? 0.2527 0.2123 0.2838 0.0253  -0.0126 -0.0324 943  GLY A O   
6912  N N   . PRO A 946  ? 0.2347 0.1931 0.2721 0.0273  -0.0139 -0.0343 944  PRO A N   
6913  C CA  . PRO A 946  ? 0.2420 0.1997 0.2761 0.0250  -0.0116 -0.0286 944  PRO A CA  
6914  C C   . PRO A 946  ? 0.2313 0.1850 0.2696 0.0217  -0.0132 -0.0242 944  PRO A C   
6915  O O   . PRO A 946  ? 0.2480 0.1997 0.2897 0.0205  -0.0138 -0.0215 944  PRO A O   
6916  C CB  . PRO A 946  ? 0.2179 0.1766 0.2529 0.0268  -0.0111 -0.0295 944  PRO A CB  
6917  C CG  . PRO A 946  ? 0.2667 0.2238 0.3092 0.0286  -0.0144 -0.0340 944  PRO A CG  
6918  C CD  . PRO A 946  ? 0.2455 0.2037 0.2881 0.0297  -0.0157 -0.0381 944  PRO A CD  
6919  N N   . VAL A 947  ? 0.2326 0.1856 0.2706 0.0200  -0.0138 -0.0233 945  VAL A N   
6920  C CA  . VAL A 947  ? 0.2534 0.2034 0.2959 0.0169  -0.0155 -0.0193 945  VAL A CA  
6921  C C   . VAL A 947  ? 0.2506 0.2020 0.2879 0.0147  -0.0134 -0.0158 945  VAL A C   
6922  O O   . VAL A 947  ? 0.2593 0.2117 0.2944 0.0149  -0.0133 -0.0175 945  VAL A O   
6923  C CB  . VAL A 947  ? 0.2710 0.2186 0.3210 0.0170  -0.0192 -0.0219 945  VAL A CB  
6924  C CG1 . VAL A 947  ? 0.2705 0.2155 0.3257 0.0136  -0.0210 -0.0170 945  VAL A CG1 
6925  C CG2 . VAL A 947  ? 0.2662 0.2128 0.3216 0.0197  -0.0213 -0.0264 945  VAL A CG2 
6926  N N   . LEU A 948  ? 0.2308 0.1823 0.2660 0.0126  -0.0119 -0.0112 946  LEU A N   
6927  C CA  . LEU A 948  ? 0.2318 0.1848 0.2626 0.0105  -0.0100 -0.0079 946  LEU A CA  
6928  C C   . LEU A 948  ? 0.2352 0.1869 0.2708 0.0075  -0.0118 -0.0042 946  LEU A C   
6929  O O   . LEU A 948  ? 0.2667 0.2169 0.3069 0.0064  -0.0133 -0.0017 946  LEU A O   
6930  C CB  . LEU A 948  ? 0.2383 0.1929 0.2644 0.0101  -0.0073 -0.0053 946  LEU A CB  
6931  C CG  . LEU A 948  ? 0.2268 0.1833 0.2489 0.0080  -0.0055 -0.0021 946  LEU A CG  
6932  C CD1 . LEU A 948  ? 0.2630 0.2210 0.2810 0.0089  -0.0044 -0.0044 946  LEU A CD1 
6933  C CD2 . LEU A 948  ? 0.2630 0.2207 0.2816 0.0076  -0.0034 0.0002  946  LEU A CD2 
6934  N N   . HIS A 949  ? 0.2491 0.2017 0.2837 0.0063  -0.0118 -0.0036 947  HIS A N   
6935  C CA  . HIS A 949  ? 0.2440 0.1964 0.2825 0.0032  -0.0131 0.0004  947  HIS A CA  
6936  C C   . HIS A 949  ? 0.2465 0.2019 0.2797 0.0014  -0.0106 0.0038  947  HIS A C   
6937  O O   . HIS A 949  ? 0.2441 0.2012 0.2713 0.0024  -0.0082 0.0023  947  HIS A O   
6938  C CB  . HIS A 949  ? 0.2452 0.1968 0.2871 0.0030  -0.0152 -0.0013 947  HIS A CB  
6939  C CG  . HIS A 949  ? 0.2600 0.2091 0.3068 0.0052  -0.0177 -0.0058 947  HIS A CG  
6940  N ND1 . HIS A 949  ? 0.2769 0.2265 0.3204 0.0082  -0.0171 -0.0109 947  HIS A ND1 
6941  C CD2 . HIS A 949  ? 0.2890 0.2352 0.3440 0.0049  -0.0211 -0.0060 947  HIS A CD2 
6942  C CE1 . HIS A 949  ? 0.3249 0.2725 0.3742 0.0098  -0.0199 -0.0145 947  HIS A CE1 
6943  N NE2 . HIS A 949  ? 0.3001 0.2453 0.3567 0.0079  -0.0224 -0.0117 947  HIS A NE2 
6944  N N   . VAL A 950  ? 0.2425 0.1988 0.2782 -0.0012 -0.0110 0.0084  948  VAL A N   
6945  C CA  . VAL A 950  ? 0.2583 0.2180 0.2894 -0.0029 -0.0087 0.0115  948  VAL A CA  
6946  C C   . VAL A 950  ? 0.2906 0.2523 0.3245 -0.0057 -0.0097 0.0149  948  VAL A C   
6947  O O   . VAL A 950  ? 0.2998 0.2606 0.3399 -0.0073 -0.0121 0.0176  948  VAL A O   
6948  C CB  . VAL A 950  ? 0.2371 0.1975 0.2675 -0.0034 -0.0080 0.0141  948  VAL A CB  
6949  C CG1 . VAL A 950  ? 0.2542 0.2187 0.2803 -0.0052 -0.0058 0.0170  948  VAL A CG1 
6950  C CG2 . VAL A 950  ? 0.2548 0.2136 0.2824 -0.0007 -0.0069 0.0109  948  VAL A CG2 
6951  N N   . ILE A 951  ? 0.2444 0.2090 0.2742 -0.0063 -0.0080 0.0149  949  ILE A N   
6952  C CA  . ILE A 951  ? 0.2853 0.2530 0.3170 -0.0090 -0.0084 0.0183  949  ILE A CA  
6953  C C   . ILE A 951  ? 0.2845 0.2567 0.3109 -0.0099 -0.0058 0.0200  949  ILE A C   
6954  O O   . ILE A 951  ? 0.2588 0.2313 0.2802 -0.0083 -0.0037 0.0178  949  ILE A O   
6955  C CB  . ILE A 951  ? 0.2981 0.2654 0.3312 -0.0089 -0.0093 0.0164  949  ILE A CB  
6956  C CG1 . ILE A 951  ? 0.3182 0.2860 0.3452 -0.0069 -0.0071 0.0126  949  ILE A CG1 
6957  C CG2 . ILE A 951  ? 0.3667 0.3297 0.4057 -0.0080 -0.0122 0.0144  949  ILE A CG2 
6958  C CD1 . ILE A 951  ? 0.4453 0.4129 0.4735 -0.0066 -0.0080 0.0106  949  ILE A CD1 
6959  N N   . ARG A 952  ? 0.2559 0.2321 0.2842 -0.0126 -0.0061 0.0240  950  ARG A N   
6960  C CA  . ARG A 952  ? 0.2510 0.2324 0.2750 -0.0136 -0.0039 0.0257  950  ARG A CA  
6961  C C   . ARG A 952  ? 0.2444 0.2294 0.2678 -0.0147 -0.0033 0.0258  950  ARG A C   
6962  O O   . ARG A 952  ? 0.2786 0.2631 0.3063 -0.0157 -0.0050 0.0268  950  ARG A O   
6963  C CB  . ARG A 952  ? 0.2835 0.2680 0.3099 -0.0158 -0.0045 0.0305  950  ARG A CB  
6964  C CG  . ARG A 952  ? 0.3219 0.3026 0.3506 -0.0151 -0.0057 0.0309  950  ARG A CG  
6965  C CD  . ARG A 952  ? 0.3486 0.3317 0.3818 -0.0176 -0.0073 0.0363  950  ARG A CD  
6966  N NE  . ARG A 952  ? 0.3454 0.3342 0.3749 -0.0187 -0.0056 0.0386  950  ARG A NE  
6967  C CZ  . ARG A 952  ? 0.3484 0.3371 0.3767 -0.0184 -0.0053 0.0395  950  ARG A CZ  
6968  N NH1 . ARG A 952  ? 0.3738 0.3572 0.4044 -0.0170 -0.0064 0.0383  950  ARG A NH1 
6969  N NH2 . ARG A 952  ? 0.3472 0.3417 0.3722 -0.0195 -0.0038 0.0413  950  ARG A NH2 
6970  N N   . TYR A 953  ? 0.2301 0.2188 0.2486 -0.0143 -0.0010 0.0246  951  TYR A N   
6971  C CA  . TYR A 953  ? 0.2389 0.2316 0.2568 -0.0152 -0.0004 0.0245  951  TYR A CA  
6972  C C   . TYR A 953  ? 0.2206 0.2197 0.2351 -0.0161 0.0016  0.0256  951  TYR A C   
6973  O O   . TYR A 953  ? 0.2550 0.2543 0.2662 -0.0151 0.0028  0.0245  951  TYR A O   
6974  C CB  . TYR A 953  ? 0.2352 0.2249 0.2509 -0.0130 0.0002  0.0202  951  TYR A CB  
6975  C CG  . TYR A 953  ? 0.2291 0.2186 0.2396 -0.0110 0.0022  0.0171  951  TYR A CG  
6976  C CD1 . TYR A 953  ? 0.2197 0.2051 0.2287 -0.0092 0.0024  0.0154  951  TYR A CD1 
6977  C CD2 . TYR A 953  ? 0.2456 0.2392 0.2532 -0.0110 0.0039  0.0160  951  TYR A CD2 
6978  C CE1 . TYR A 953  ? 0.2311 0.2164 0.2360 -0.0075 0.0042  0.0131  951  TYR A CE1 
6979  C CE2 . TYR A 953  ? 0.2098 0.2031 0.2136 -0.0092 0.0055  0.0134  951  TYR A CE2 
6980  C CZ  . TYR A 953  ? 0.2361 0.2251 0.2386 -0.0076 0.0056  0.0122  951  TYR A CZ  
6981  O OH  . TYR A 953  ? 0.2350 0.2238 0.2344 -0.0060 0.0070  0.0100  951  TYR A OH  
6982  N N   . ARG A 954  ? 0.2768 0.2813 0.2924 -0.0179 0.0017  0.0276  952  ARG A N   
6983  C CA  . ARG A 954  ? 0.2696 0.2812 0.2822 -0.0185 0.0036  0.0278  952  ARG A CA  
6984  C C   . ARG A 954  ? 0.2537 0.2649 0.2628 -0.0165 0.0051  0.0232  952  ARG A C   
6985  O O   . ARG A 954  ? 0.2581 0.2662 0.2680 -0.0157 0.0046  0.0214  952  ARG A O   
6986  C CB  . ARG A 954  ? 0.3040 0.3223 0.3194 -0.0212 0.0031  0.0317  952  ARG A CB  
6987  N N   . ARG A 955  ? 0.2732 0.2878 0.2787 -0.0157 0.0068  0.0214  953  ARG A N   
6988  C CA  . ARG A 955  ? 0.2537 0.2674 0.2564 -0.0137 0.0081  0.0172  953  ARG A CA  
6989  C C   . ARG A 955  ? 0.2459 0.2618 0.2497 -0.0140 0.0081  0.0164  953  ARG A C   
6990  O O   . ARG A 955  ? 0.2780 0.2903 0.2811 -0.0124 0.0082  0.0135  953  ARG A O   
6991  C CB  . ARG A 955  ? 0.3419 0.3600 0.3417 -0.0131 0.0096  0.0156  953  ARG A CB  
6992  C CG  . ARG A 955  ? 0.4431 0.4612 0.4410 -0.0112 0.0107  0.0113  953  ARG A CG  
6993  C CD  . ARG A 955  ? 0.4884 0.4990 0.4859 -0.0092 0.0103  0.0092  953  ARG A CD  
6994  N NE  . ARG A 955  ? 0.5878 0.5978 0.5840 -0.0074 0.0111  0.0057  953  ARG A NE  
6995  C CZ  . ARG A 955  ? 0.5085 0.5182 0.5053 -0.0069 0.0110  0.0044  953  ARG A CZ  
6996  N NH1 . ARG A 955  ? 0.3808 0.3912 0.3794 -0.0082 0.0102  0.0060  953  ARG A NH1 
6997  N NH2 . ARG A 955  ? 0.5052 0.5139 0.5011 -0.0052 0.0116  0.0014  953  ARG A NH2 
6998  N N   . ASP A 956  ? 0.2588 0.2811 0.2643 -0.0161 0.0080  0.0191  954  ASP A N   
6999  C CA  . ASP A 956  ? 0.2555 0.2804 0.2621 -0.0164 0.0081  0.0183  954  ASP A CA  
7000  C C   . ASP A 956  ? 0.2845 0.3037 0.2939 -0.0163 0.0065  0.0185  954  ASP A C   
7001  O O   . ASP A 956  ? 0.2822 0.3019 0.2922 -0.0160 0.0065  0.0169  954  ASP A O   
7002  C CB  . ASP A 956  ? 0.2868 0.3204 0.2950 -0.0188 0.0084  0.0216  954  ASP A CB  
7003  C CG  . ASP A 956  ? 0.3201 0.3609 0.3255 -0.0186 0.0101  0.0204  954  ASP A CG  
7004  O OD1 . ASP A 956  ? 0.3721 0.4111 0.3748 -0.0165 0.0110  0.0163  954  ASP A OD1 
7005  O OD2 . ASP A 956  ? 0.4240 0.4727 0.4302 -0.0206 0.0103  0.0235  954  ASP A OD2 
7006  N N   . ASP A 957  ? 0.2543 0.2683 0.2656 -0.0165 0.0050  0.0201  955  ASP A N   
7007  C CA  . ASP A 957  ? 0.2694 0.2781 0.2837 -0.0163 0.0032  0.0198  955  ASP A CA  
7008  C C   . ASP A 957  ? 0.2576 0.2598 0.2697 -0.0136 0.0032  0.0159  955  ASP A C   
7009  O O   . ASP A 957  ? 0.2661 0.2635 0.2804 -0.0131 0.0016  0.0153  955  ASP A O   
7010  C CB  . ASP A 957  ? 0.2965 0.3036 0.3152 -0.0181 0.0013  0.0237  955  ASP A CB  
7011  C CG  . ASP A 957  ? 0.3783 0.3921 0.4000 -0.0210 0.0009  0.0283  955  ASP A CG  
7012  O OD1 . ASP A 957  ? 0.3444 0.3632 0.3660 -0.0218 0.0017  0.0283  955  ASP A OD1 
7013  O OD2 . ASP A 957  ? 0.3950 0.4095 0.4193 -0.0226 -0.0001 0.0321  955  ASP A OD2 
7014  N N   . LEU A 958  ? 0.2338 0.2360 0.2418 -0.0119 0.0049  0.0134  956  LEU A N   
7015  C CA  . LEU A 958  ? 0.2341 0.2310 0.2401 -0.0095 0.0050  0.0102  956  LEU A CA  
7016  C C   . LEU A 958  ? 0.2341 0.2288 0.2410 -0.0086 0.0042  0.0082  956  LEU A C   
7017  O O   . LEU A 958  ? 0.2241 0.2142 0.2314 -0.0073 0.0032  0.0068  956  LEU A O   
7018  C CB  . LEU A 958  ? 0.2368 0.2349 0.2392 -0.0080 0.0068  0.0081  956  LEU A CB  
7019  C CG  . LEU A 958  ? 0.2269 0.2204 0.2272 -0.0056 0.0070  0.0053  956  LEU A CG  
7020  C CD1 . LEU A 958  ? 0.2518 0.2407 0.2524 -0.0049 0.0062  0.0057  956  LEU A CD1 
7021  C CD2 . LEU A 958  ? 0.2729 0.2679 0.2706 -0.0045 0.0086  0.0036  956  LEU A CD2 
7022  N N   . ASP A 959  ? 0.2078 0.2063 0.2152 -0.0092 0.0046  0.0080  957  ASP A N   
7023  C CA  . ASP A 959  ? 0.2124 0.2090 0.2205 -0.0083 0.0038  0.0060  957  ASP A CA  
7024  C C   . ASP A 959  ? 0.2219 0.2159 0.2339 -0.0093 0.0016  0.0072  957  ASP A C   
7025  O O   . ASP A 959  ? 0.2281 0.2184 0.2404 -0.0079 0.0005  0.0051  957  ASP A O   
7026  C CB  . ASP A 959  ? 0.2559 0.2574 0.2641 -0.0088 0.0046  0.0056  957  ASP A CB  
7027  C CG  . ASP A 959  ? 0.2756 0.2751 0.2838 -0.0075 0.0040  0.0032  957  ASP A CG  
7028  O OD1 . ASP A 959  ? 0.2689 0.2653 0.2747 -0.0054 0.0043  0.0009  957  ASP A OD1 
7029  O OD2 . ASP A 959  ? 0.3443 0.3457 0.3551 -0.0086 0.0032  0.0038  957  ASP A OD2 
7030  N N   . ARG A 960  ? 0.2224 0.2186 0.2376 -0.0116 0.0008  0.0106  958  ARG A N   
7031  C CA  . ARG A 960  ? 0.2637 0.2571 0.2837 -0.0126 -0.0016 0.0119  958  ARG A CA  
7032  C C   . ARG A 960  ? 0.2627 0.2505 0.2826 -0.0110 -0.0026 0.0104  958  ARG A C   
7033  O O   . ARG A 960  ? 0.2770 0.2612 0.2995 -0.0103 -0.0045 0.0089  958  ARG A O   
7034  C CB  . ARG A 960  ? 0.2687 0.2660 0.2926 -0.0155 -0.0023 0.0165  958  ARG A CB  
7035  C CG  . ARG A 960  ? 0.3148 0.3095 0.3449 -0.0169 -0.0051 0.0185  958  ARG A CG  
7036  C CD  . ARG A 960  ? 0.4771 0.4676 0.5092 -0.0167 -0.0064 0.0194  958  ARG A CD  
7037  N NE  . ARG A 960  ? 0.4829 0.4764 0.5136 -0.0178 -0.0053 0.0224  958  ARG A NE  
7038  C CZ  . ARG A 960  ? 0.4908 0.4814 0.5204 -0.0169 -0.0052 0.0222  958  ARG A CZ  
7039  N NH1 . ARG A 960  ? 0.5244 0.5092 0.5539 -0.0148 -0.0061 0.0190  958  ARG A NH1 
7040  N NH2 . ARG A 960  ? 0.5892 0.5831 0.6177 -0.0181 -0.0043 0.0251  958  ARG A NH2 
7041  N N   . LEU A 961  ? 0.2396 0.2271 0.2567 -0.0104 -0.0014 0.0107  959  LEU A N   
7042  C CA  . LEU A 961  ? 0.2445 0.2272 0.2614 -0.0088 -0.0021 0.0092  959  LEU A CA  
7043  C C   . LEU A 961  ? 0.2629 0.2428 0.2774 -0.0062 -0.0020 0.0052  959  LEU A C   
7044  O O   . LEU A 961  ? 0.2565 0.2328 0.2728 -0.0050 -0.0036 0.0035  959  LEU A O   
7045  C CB  . LEU A 961  ? 0.2275 0.2109 0.2415 -0.0085 -0.0005 0.0102  959  LEU A CB  
7046  C CG  . LEU A 961  ? 0.2387 0.2177 0.2516 -0.0065 -0.0008 0.0084  959  LEU A CG  
7047  C CD1 . LEU A 961  ? 0.3080 0.2841 0.3259 -0.0071 -0.0032 0.0094  959  LEU A CD1 
7048  C CD2 . LEU A 961  ? 0.2777 0.2579 0.2874 -0.0063 0.0010  0.0091  959  LEU A CD2 
7049  N N   . VAL A 962  ? 0.2260 0.2077 0.2368 -0.0052 -0.0003 0.0037  960  VAL A N   
7050  C CA  . VAL A 962  ? 0.2186 0.1982 0.2272 -0.0029 -0.0003 0.0004  960  VAL A CA  
7051  C C   . VAL A 962  ? 0.2725 0.2511 0.2843 -0.0029 -0.0024 -0.0008 960  VAL A C   
7052  O O   . VAL A 962  ? 0.2532 0.2292 0.2648 -0.0012 -0.0034 -0.0034 960  VAL A O   
7053  C CB  . VAL A 962  ? 0.2617 0.2436 0.2666 -0.0020 0.0016  -0.0006 960  VAL A CB  
7054  C CG1 . VAL A 962  ? 0.2894 0.2698 0.2925 0.0002  0.0013  -0.0034 960  VAL A CG1 
7055  C CG2 . VAL A 962  ? 0.2510 0.2333 0.2531 -0.0016 0.0033  0.0001  960  VAL A CG2 
7056  N N   . ASP A 963  ? 0.2558 0.2367 0.2706 -0.0050 -0.0030 0.0010  961  ASP A N   
7057  C CA  . ASP A 963  ? 0.2723 0.2520 0.2911 -0.0054 -0.0053 0.0002  961  ASP A CA  
7058  C C   . ASP A 963  ? 0.2814 0.2574 0.3039 -0.0052 -0.0075 -0.0002 961  ASP A C   
7059  O O   . ASP A 963  ? 0.3195 0.2932 0.3436 -0.0038 -0.0092 -0.0031 961  ASP A O   
7060  C CB  . ASP A 963  ? 0.2995 0.2827 0.3217 -0.0080 -0.0057 0.0030  961  ASP A CB  
7061  C CG  . ASP A 963  ? 0.3723 0.3593 0.3919 -0.0080 -0.0040 0.0026  961  ASP A CG  
7062  O OD1 . ASP A 963  ? 0.4256 0.4119 0.4417 -0.0060 -0.0032 -0.0002 961  ASP A OD1 
7063  O OD2 . ASP A 963  ? 0.4637 0.4548 0.4851 -0.0101 -0.0036 0.0052  961  ASP A OD2 
7064  N N   . ASP A 964  ? 0.2704 0.2461 0.2947 -0.0065 -0.0076 0.0025  962  ASP A N   
7065  C CA  . ASP A 964  ? 0.3065 0.2787 0.3351 -0.0063 -0.0098 0.0023  962  ASP A CA  
7066  C C   . ASP A 964  ? 0.3447 0.3140 0.3706 -0.0033 -0.0098 -0.0016 962  ASP A C   
7067  O O   . ASP A 964  ? 0.3421 0.3087 0.3713 -0.0023 -0.0120 -0.0040 962  ASP A O   
7068  C CB  . ASP A 964  ? 0.3237 0.2965 0.3542 -0.0081 -0.0097 0.0062  962  ASP A CB  
7069  C CG  . ASP A 964  ? 0.3748 0.3508 0.4092 -0.0112 -0.0103 0.0104  962  ASP A CG  
7070  O OD1 . ASP A 964  ? 0.4258 0.4029 0.4626 -0.0120 -0.0113 0.0102  962  ASP A OD1 
7071  O OD2 . ASP A 964  ? 0.4799 0.4578 0.5149 -0.0129 -0.0098 0.0140  962  ASP A OD2 
7072  N N   . VAL A 965  ? 0.2875 0.2577 0.3078 -0.0019 -0.0074 -0.0023 963  VAL A N   
7073  C CA  . VAL A 965  ? 0.2739 0.2423 0.2914 0.0008  -0.0071 -0.0057 963  VAL A CA  
7074  C C   . VAL A 965  ? 0.3152 0.2835 0.3323 0.0024  -0.0081 -0.0091 963  VAL A C   
7075  O O   . VAL A 965  ? 0.3229 0.2895 0.3412 0.0042  -0.0096 -0.0121 963  VAL A O   
7076  C CB  . VAL A 965  ? 0.2408 0.2105 0.2527 0.0017  -0.0044 -0.0052 963  VAL A CB  
7077  C CG1 . VAL A 965  ? 0.2577 0.2265 0.2666 0.0046  -0.0040 -0.0083 963  VAL A CG1 
7078  C CG2 . VAL A 965  ? 0.2619 0.2316 0.2744 0.0004  -0.0037 -0.0023 963  VAL A CG2 
7079  N N   . ASN A 966  ? 0.2663 0.2368 0.2817 0.0019  -0.0073 -0.0088 964  ASN A N   
7080  C CA  . ASN A 966  ? 0.2777 0.2485 0.2927 0.0032  -0.0083 -0.0118 964  ASN A CA  
7081  C C   . ASN A 966  ? 0.3358 0.3049 0.3566 0.0027  -0.0113 -0.0131 964  ASN A C   
7082  O O   . ASN A 966  ? 0.2982 0.2668 0.3193 0.0045  -0.0128 -0.0167 964  ASN A O   
7083  C CB  . ASN A 966  ? 0.2755 0.2491 0.2886 0.0025  -0.0071 -0.0109 964  ASN A CB  
7084  C CG  . ASN A 966  ? 0.2808 0.2559 0.2886 0.0035  -0.0045 -0.0106 964  ASN A CG  
7085  O OD1 . ASN A 966  ? 0.2600 0.2343 0.2651 0.0053  -0.0038 -0.0116 964  ASN A OD1 
7086  N ND2 . ASN A 966  ? 0.2582 0.2357 0.2649 0.0026  -0.0032 -0.0092 964  ASN A ND2 
7087  N N   . ALA A 967  ? 0.3056 0.2741 0.3313 0.0003  -0.0125 -0.0103 965  ALA A N   
7088  C CA  . ALA A 967  ? 0.3443 0.3112 0.3766 -0.0006 -0.0156 -0.0109 965  ALA A CA  
7089  C C   . ALA A 967  ? 0.3186 0.2825 0.3540 0.0011  -0.0179 -0.0142 965  ALA A C   
7090  O O   . ALA A 967  ? 0.3809 0.3433 0.4218 0.0010  -0.0207 -0.0160 965  ALA A O   
7091  C CB  . ALA A 967  ? 0.3769 0.3444 0.4140 -0.0038 -0.0162 -0.0063 965  ALA A CB  
7092  N N   . THR A 968  ? 0.2869 0.2499 0.3194 0.0028  -0.0168 -0.0152 966  THR A N   
7093  C CA  . THR A 968  ? 0.2775 0.2383 0.3128 0.0049  -0.0189 -0.0190 966  THR A CA  
7094  C C   . THR A 968  ? 0.2814 0.2431 0.3151 0.0073  -0.0198 -0.0239 966  THR A C   
7095  O O   . THR A 968  ? 0.3100 0.2703 0.3475 0.0088  -0.0223 -0.0277 966  THR A O   
7096  C CB  . THR A 968  ? 0.3036 0.2640 0.3354 0.0064  -0.0172 -0.0193 966  THR A CB  
7097  O OG1 . THR A 968  ? 0.2818 0.2446 0.3065 0.0083  -0.0147 -0.0207 966  THR A OG1 
7098  C CG2 . THR A 968  ? 0.2762 0.2363 0.3086 0.0042  -0.0160 -0.0145 966  THR A CG2 
7099  N N   . GLY A 969  ? 0.2750 0.2394 0.3035 0.0078  -0.0180 -0.0240 967  GLY A N   
7100  C CA  . GLY A 969  ? 0.2862 0.2522 0.3123 0.0102  -0.0185 -0.0283 967  GLY A CA  
7101  C C   . GLY A 969  ? 0.2658 0.2336 0.2863 0.0129  -0.0168 -0.0304 967  GLY A C   
7102  O O   . GLY A 969  ? 0.2440 0.2142 0.2611 0.0148  -0.0167 -0.0331 967  GLY A O   
7103  N N   . TYR A 970  ? 0.2432 0.2101 0.2626 0.0131  -0.0155 -0.0290 968  TYR A N   
7104  C CA  . TYR A 970  ? 0.2293 0.1982 0.2434 0.0154  -0.0136 -0.0302 968  TYR A CA  
7105  C C   . TYR A 970  ? 0.2191 0.1900 0.2276 0.0149  -0.0107 -0.0271 968  TYR A C   
7106  O O   . TYR A 970  ? 0.2715 0.2421 0.2803 0.0127  -0.0100 -0.0242 968  TYR A O   
7107  C CB  . TYR A 970  ? 0.2484 0.2156 0.2639 0.0158  -0.0134 -0.0298 968  TYR A CB  
7108  C CG  . TYR A 970  ? 0.2566 0.2221 0.2777 0.0169  -0.0164 -0.0335 968  TYR A CG  
7109  C CD1 . TYR A 970  ? 0.2789 0.2464 0.2988 0.0200  -0.0171 -0.0383 968  TYR A CD1 
7110  C CD2 . TYR A 970  ? 0.2822 0.2443 0.3101 0.0149  -0.0187 -0.0322 968  TYR A CD2 
7111  C CE1 . TYR A 970  ? 0.2882 0.2543 0.3138 0.0212  -0.0200 -0.0423 968  TYR A CE1 
7112  C CE2 . TYR A 970  ? 0.2940 0.2542 0.3280 0.0160  -0.0217 -0.0357 968  TYR A CE2 
7113  C CZ  . TYR A 970  ? 0.3215 0.2836 0.3543 0.0193  -0.0224 -0.0410 968  TYR A CZ  
7114  O OH  . TYR A 970  ? 0.3957 0.3561 0.4350 0.0206  -0.0255 -0.0451 968  TYR A OH  
7115  N N   . GLY A 971  ? 0.2099 0.1831 0.2137 0.0168  -0.0089 -0.0277 969  GLY A N   
7116  C CA  . GLY A 971  ? 0.2032 0.1782 0.2025 0.0165  -0.0065 -0.0250 969  GLY A CA  
7117  C C   . GLY A 971  ? 0.2084 0.1859 0.2033 0.0186  -0.0048 -0.0254 969  GLY A C   
7118  O O   . GLY A 971  ? 0.2121 0.1926 0.2036 0.0197  -0.0039 -0.0253 969  GLY A O   
7119  N N   . LEU A 972  ? 0.1989 0.1756 0.1943 0.0192  -0.0045 -0.0255 970  LEU A N   
7120  C CA  . LEU A 972  ? 0.1936 0.1731 0.1853 0.0213  -0.0030 -0.0260 970  LEU A CA  
7121  C C   . LEU A 972  ? 0.2000 0.1793 0.1895 0.0203  -0.0006 -0.0221 970  LEU A C   
7122  O O   . LEU A 972  ? 0.2059 0.1868 0.1927 0.0201  0.0007  -0.0202 970  LEU A O   
7123  C CB  . LEU A 972  ? 0.2113 0.1908 0.2051 0.0230  -0.0042 -0.0290 970  LEU A CB  
7124  C CG  . LEU A 972  ? 0.2152 0.1988 0.2054 0.0255  -0.0029 -0.0302 970  LEU A CG  
7125  C CD1 . LEU A 972  ? 0.2179 0.2061 0.2046 0.0269  -0.0026 -0.0312 970  LEU A CD1 
7126  C CD2 . LEU A 972  ? 0.2472 0.2311 0.2400 0.0273  -0.0044 -0.0341 970  LEU A CD2 
7127  N N   . THR A 973  ? 0.1937 0.1710 0.1845 0.0197  -0.0001 -0.0208 971  THR A N   
7128  C CA  . THR A 973  ? 0.2028 0.1797 0.1919 0.0186  0.0019  -0.0174 971  THR A CA  
7129  C C   . THR A 973  ? 0.1962 0.1703 0.1877 0.0160  0.0018  -0.0151 971  THR A C   
7130  O O   . THR A 973  ? 0.2023 0.1743 0.1972 0.0150  0.0002  -0.0158 971  THR A O   
7131  C CB  . THR A 973  ? 0.1987 0.1762 0.1870 0.0198  0.0028  -0.0172 971  THR A CB  
7132  O OG1 . THR A 973  ? 0.1944 0.1695 0.1862 0.0196  0.0014  -0.0186 971  THR A OG1 
7133  C CG2 . THR A 973  ? 0.2114 0.1930 0.1970 0.0223  0.0033  -0.0190 971  THR A CG2 
7134  N N   . PHE A 974  ? 0.1936 0.1680 0.1834 0.0150  0.0035  -0.0124 972  PHE A N   
7135  C CA  . PHE A 974  ? 0.1889 0.1617 0.1804 0.0127  0.0036  -0.0102 972  PHE A CA  
7136  C C   . PHE A 974  ? 0.1730 0.1463 0.1627 0.0123  0.0055  -0.0080 972  PHE A C   
7137  O O   . PHE A 974  ? 0.2053 0.1802 0.1927 0.0132  0.0066  -0.0076 972  PHE A O   
7138  C CB  . PHE A 974  ? 0.1936 0.1670 0.1855 0.0115  0.0032  -0.0100 972  PHE A CB  
7139  C CG  . PHE A 974  ? 0.1865 0.1596 0.1796 0.0093  0.0037  -0.0078 972  PHE A CG  
7140  C CD1 . PHE A 974  ? 0.1837 0.1556 0.1800 0.0076  0.0026  -0.0070 972  PHE A CD1 
7141  C CD2 . PHE A 974  ? 0.1878 0.1622 0.1792 0.0088  0.0053  -0.0064 972  PHE A CD2 
7142  C CE1 . PHE A 974  ? 0.2100 0.1826 0.2072 0.0056  0.0031  -0.0047 972  PHE A CE1 
7143  C CE2 . PHE A 974  ? 0.1913 0.1663 0.1837 0.0069  0.0057  -0.0047 972  PHE A CE2 
7144  C CZ  . PHE A 974  ? 0.2035 0.1779 0.1984 0.0053  0.0047  -0.0038 972  PHE A CZ  
7145  N N   . GLY A 975  ? 0.1867 0.1587 0.1778 0.0108  0.0056  -0.0064 973  GLY A N   
7146  C CA  . GLY A 975  ? 0.1917 0.1641 0.1816 0.0104  0.0071  -0.0045 973  GLY A CA  
7147  C C   . GLY A 975  ? 0.1879 0.1607 0.1787 0.0082  0.0074  -0.0028 973  GLY A C   
7148  O O   . GLY A 975  ? 0.1835 0.1558 0.1764 0.0068  0.0064  -0.0024 973  GLY A O   
7149  N N   . LEU A 976  ? 0.1766 0.1504 0.1661 0.0080  0.0087  -0.0019 974  LEU A N   
7150  C CA  . LEU A 976  ? 0.1815 0.1566 0.1717 0.0063  0.0091  -0.0007 974  LEU A CA  
7151  C C   . LEU A 976  ? 0.1844 0.1598 0.1739 0.0063  0.0101  0.0002  974  LEU A C   
7152  O O   . LEU A 976  ? 0.1933 0.1687 0.1817 0.0075  0.0109  0.0000  974  LEU A O   
7153  C CB  . LEU A 976  ? 0.1956 0.1722 0.1855 0.0061  0.0093  -0.0014 974  LEU A CB  
7154  C CG  . LEU A 976  ? 0.1996 0.1784 0.1900 0.0047  0.0098  -0.0007 974  LEU A CG  
7155  C CD1 . LEU A 976  ? 0.2211 0.2008 0.2131 0.0028  0.0092  0.0004  974  LEU A CD1 
7156  C CD2 . LEU A 976  ? 0.2248 0.2050 0.2151 0.0050  0.0100  -0.0018 974  LEU A CD2 
7157  N N   . HIS A 977  ? 0.1824 0.1581 0.1728 0.0049  0.0101  0.0015  975  HIS A N   
7158  C CA  . HIS A 977  ? 0.1910 0.1674 0.1810 0.0047  0.0110  0.0022  975  HIS A CA  
7159  C C   . HIS A 977  ? 0.1983 0.1773 0.1886 0.0033  0.0113  0.0025  975  HIS A C   
7160  O O   . HIS A 977  ? 0.1972 0.1775 0.1884 0.0018  0.0108  0.0035  975  HIS A O   
7161  C CB  . HIS A 977  ? 0.2029 0.1781 0.1935 0.0045  0.0108  0.0034  975  HIS A CB  
7162  C CG  . HIS A 977  ? 0.2380 0.2116 0.2279 0.0062  0.0111  0.0030  975  HIS A CG  
7163  N ND1 . HIS A 977  ? 0.3081 0.2818 0.2977 0.0066  0.0119  0.0037  975  HIS A ND1 
7164  C CD2 . HIS A 977  ? 0.3072 0.2797 0.2969 0.0076  0.0107  0.0021  975  HIS A CD2 
7165  C CE1 . HIS A 977  ? 0.2799 0.2527 0.2690 0.0081  0.0121  0.0034  975  HIS A CE1 
7166  N NE2 . HIS A 977  ? 0.2900 0.2622 0.2790 0.0088  0.0114  0.0023  975  HIS A NE2 
7167  N N   . THR A 978  ? 0.1711 0.1513 0.1611 0.0038  0.0119  0.0016  976  THR A N   
7168  C CA  . THR A 978  ? 0.1904 0.1737 0.1809 0.0028  0.0122  0.0011  976  THR A CA  
7169  C C   . THR A 978  ? 0.1879 0.1714 0.1787 0.0038  0.0128  0.0000  976  THR A C   
7170  O O   . THR A 978  ? 0.2204 0.2019 0.2110 0.0051  0.0128  -0.0002 976  THR A O   
7171  C CB  . THR A 978  ? 0.1989 0.1840 0.1898 0.0022  0.0119  0.0005  976  THR A CB  
7172  O OG1 . THR A 978  ? 0.2029 0.1918 0.1942 0.0014  0.0123  -0.0003 976  THR A OG1 
7173  C CG2 . THR A 978  ? 0.2060 0.1897 0.1967 0.0036  0.0119  -0.0007 976  THR A CG2 
7174  N N   . ARG A 979  ? 0.1989 0.1850 0.1903 0.0032  0.0130  -0.0007 977  ARG A N   
7175  C CA  . ARG A 979  ? 0.2203 0.2069 0.2131 0.0040  0.0132  -0.0021 977  ARG A CA  
7176  C C   . ARG A 979  ? 0.2124 0.2013 0.2061 0.0041  0.0131  -0.0039 977  ARG A C   
7177  O O   . ARG A 979  ? 0.2458 0.2351 0.2413 0.0049  0.0130  -0.0054 977  ARG A O   
7178  C CB  . ARG A 979  ? 0.2221 0.2103 0.2155 0.0036  0.0133  -0.0024 977  ARG A CB  
7179  C CG  . ARG A 979  ? 0.2577 0.2435 0.2503 0.0036  0.0134  -0.0007 977  ARG A CG  
7180  C CD  . ARG A 979  ? 0.3713 0.3591 0.3645 0.0030  0.0134  -0.0009 977  ARG A CD  
7181  N NE  . ARG A 979  ? 0.3707 0.3561 0.3638 0.0032  0.0135  0.0006  977  ARG A NE  
7182  C CZ  . ARG A 979  ? 0.4753 0.4616 0.4690 0.0029  0.0134  0.0006  977  ARG A CZ  
7183  N NH1 . ARG A 979  ? 0.3590 0.3488 0.3535 0.0024  0.0133  -0.0011 977  ARG A NH1 
7184  N NH2 . ARG A 979  ? 0.4322 0.4163 0.4259 0.0032  0.0135  0.0021  977  ARG A NH2 
7185  N N   . LEU A 980  ? 0.1844 0.1749 0.1775 0.0033  0.0130  -0.0039 978  LEU A N   
7186  C CA  . LEU A 980  ? 0.1836 0.1777 0.1778 0.0031  0.0130  -0.0056 978  LEU A CA  
7187  C C   . LEU A 980  ? 0.1852 0.1777 0.1798 0.0040  0.0127  -0.0061 978  LEU A C   
7188  O O   . LEU A 980  ? 0.1939 0.1850 0.1875 0.0037  0.0124  -0.0050 978  LEU A O   
7189  C CB  . LEU A 980  ? 0.1940 0.1919 0.1875 0.0014  0.0131  -0.0049 978  LEU A CB  
7190  C CG  . LEU A 980  ? 0.2073 0.2073 0.2002 0.0004  0.0133  -0.0040 978  LEU A CG  
7191  C CD1 . LEU A 980  ? 0.2177 0.2219 0.2103 -0.0014 0.0133  -0.0027 978  LEU A CD1 
7192  C CD2 . LEU A 980  ? 0.2119 0.2143 0.2059 0.0010  0.0135  -0.0063 978  LEU A CD2 
7193  N N   . ASP A 981  ? 0.2023 0.1953 0.1987 0.0050  0.0126  -0.0079 979  ASP A N   
7194  C CA  . ASP A 981  ? 0.1853 0.1770 0.1823 0.0059  0.0122  -0.0082 979  ASP A CA  
7195  C C   . ASP A 981  ? 0.2024 0.1963 0.1990 0.0051  0.0121  -0.0084 979  ASP A C   
7196  O O   . ASP A 981  ? 0.2000 0.1922 0.1961 0.0055  0.0117  -0.0078 979  ASP A O   
7197  C CB  . ASP A 981  ? 0.2253 0.2177 0.2253 0.0070  0.0118  -0.0101 979  ASP A CB  
7198  C CG  . ASP A 981  ? 0.2223 0.2120 0.2236 0.0080  0.0116  -0.0094 979  ASP A CG  
7199  O OD1 . ASP A 981  ? 0.2661 0.2534 0.2657 0.0080  0.0118  -0.0074 979  ASP A OD1 
7200  O OD2 . ASP A 981  ? 0.2684 0.2587 0.2729 0.0087  0.0112  -0.0110 979  ASP A OD2 
7201  N N   . GLU A 982  ? 0.1905 0.1885 0.1873 0.0040  0.0124  -0.0091 980  GLU A N   
7202  C CA  . GLU A 982  ? 0.1989 0.1993 0.1957 0.0031  0.0123  -0.0090 980  GLU A CA  
7203  C C   . GLU A 982  ? 0.1977 0.1957 0.1931 0.0022  0.0119  -0.0067 980  GLU A C   
7204  O O   . GLU A 982  ? 0.2013 0.1986 0.1968 0.0022  0.0114  -0.0065 980  GLU A O   
7205  C CB  . GLU A 982  ? 0.2082 0.2144 0.2055 0.0019  0.0128  -0.0097 980  GLU A CB  
7206  C CG  . GLU A 982  ? 0.2252 0.2343 0.2227 0.0006  0.0127  -0.0089 980  GLU A CG  
7207  C CD  . GLU A 982  ? 0.2803 0.2957 0.2779 -0.0009 0.0132  -0.0085 980  GLU A CD  
7208  O OE1 . GLU A 982  ? 0.3222 0.3382 0.3187 -0.0018 0.0134  -0.0070 980  GLU A OE1 
7209  O OE2 . GLU A 982  ? 0.2508 0.2709 0.2494 -0.0012 0.0134  -0.0097 980  GLU A OE2 
7210  N N   . THR A 983  ? 0.1818 0.1783 0.1761 0.0017  0.0120  -0.0052 981  THR A N   
7211  C CA  . THR A 983  ? 0.1896 0.1837 0.1833 0.0011  0.0115  -0.0033 981  THR A CA  
7212  C C   . THR A 983  ? 0.1914 0.1813 0.1844 0.0026  0.0110  -0.0036 981  THR A C   
7213  O O   . THR A 983  ? 0.1906 0.1792 0.1837 0.0024  0.0103  -0.0032 981  THR A O   
7214  C CB  . THR A 983  ? 0.1999 0.1936 0.1929 0.0003  0.0116  -0.0018 981  THR A CB  
7215  O OG1 . THR A 983  ? 0.2291 0.2277 0.2226 -0.0012 0.0120  -0.0014 981  THR A OG1 
7216  C CG2 . THR A 983  ? 0.2195 0.2103 0.2125 -0.0002 0.0108  -0.0001 981  THR A CG2 
7217  N N   . ILE A 984  ? 0.1876 0.1758 0.1802 0.0039  0.0113  -0.0041 982  ILE A N   
7218  C CA  . ILE A 984  ? 0.1999 0.1852 0.1918 0.0054  0.0110  -0.0041 982  ILE A CA  
7219  C C   . ILE A 984  ? 0.1870 0.1731 0.1795 0.0058  0.0105  -0.0050 982  ILE A C   
7220  O O   . ILE A 984  ? 0.1899 0.1746 0.1818 0.0062  0.0098  -0.0050 982  ILE A O   
7221  C CB  . ILE A 984  ? 0.1868 0.1710 0.1789 0.0066  0.0114  -0.0041 982  ILE A CB  
7222  C CG1 . ILE A 984  ? 0.2084 0.1917 0.1999 0.0063  0.0118  -0.0031 982  ILE A CG1 
7223  C CG2 . ILE A 984  ? 0.2165 0.1990 0.2079 0.0081  0.0111  -0.0038 982  ILE A CG2 
7224  C CD1 . ILE A 984  ? 0.2517 0.2342 0.2439 0.0072  0.0122  -0.0029 982  ILE A CD1 
7225  N N   . ALA A 985  ? 0.1814 0.1698 0.1752 0.0057  0.0106  -0.0061 983  ALA A N   
7226  C CA  . ALA A 985  ? 0.1982 0.1874 0.1928 0.0061  0.0101  -0.0070 983  ALA A CA  
7227  C C   . ALA A 985  ? 0.1927 0.1827 0.1874 0.0050  0.0096  -0.0067 983  ALA A C   
7228  O O   . ALA A 985  ? 0.2123 0.2013 0.2068 0.0055  0.0088  -0.0069 983  ALA A O   
7229  C CB  . ALA A 985  ? 0.2136 0.2056 0.2103 0.0063  0.0104  -0.0085 983  ALA A CB  
7230  N N   . HIS A 986  ? 0.1959 0.1879 0.1909 0.0034  0.0098  -0.0061 984  HIS A N   
7231  C CA  . HIS A 986  ? 0.2145 0.2075 0.2103 0.0020  0.0092  -0.0053 984  HIS A CA  
7232  C C   . HIS A 986  ? 0.2280 0.2174 0.2233 0.0023  0.0083  -0.0047 984  HIS A C   
7233  O O   . HIS A 986  ? 0.2163 0.2049 0.2122 0.0025  0.0073  -0.0052 984  HIS A O   
7234  C CB  . HIS A 986  ? 0.2202 0.2162 0.2166 0.0002  0.0096  -0.0041 984  HIS A CB  
7235  C CG  . HIS A 986  ? 0.2330 0.2300 0.2309 -0.0015 0.0088  -0.0025 984  HIS A CG  
7236  N ND1 . HIS A 986  ? 0.3003 0.3002 0.2989 -0.0033 0.0090  -0.0006 984  HIS A ND1 
7237  C CD2 . HIS A 986  ? 0.2389 0.2346 0.2380 -0.0017 0.0077  -0.0023 984  HIS A CD2 
7238  C CE1 . HIS A 986  ? 0.2921 0.2922 0.2926 -0.0047 0.0080  0.0009  984  HIS A CE1 
7239  N NE2 . HIS A 986  ? 0.2331 0.2305 0.2341 -0.0037 0.0071  -0.0003 984  HIS A NE2 
7240  N N   . VAL A 987  ? 0.2080 0.1954 0.2023 0.0025  0.0084  -0.0039 985  VAL A N   
7241  C CA  . VAL A 987  ? 0.2040 0.1885 0.1982 0.0027  0.0075  -0.0036 985  VAL A CA  
7242  C C   . VAL A 987  ? 0.2060 0.1887 0.1991 0.0046  0.0070  -0.0049 985  VAL A C   
7243  O O   . VAL A 987  ? 0.2143 0.1960 0.2081 0.0049  0.0059  -0.0056 985  VAL A O   
7244  C CB  . VAL A 987  ? 0.1859 0.1689 0.1796 0.0026  0.0078  -0.0025 985  VAL A CB  
7245  C CG1 . VAL A 987  ? 0.2022 0.1824 0.1961 0.0034  0.0068  -0.0027 985  VAL A CG1 
7246  C CG2 . VAL A 987  ? 0.2409 0.2262 0.2359 0.0006  0.0079  -0.0008 985  VAL A CG2 
7247  N N   . THR A 988  ? 0.2082 0.1909 0.2000 0.0059  0.0078  -0.0053 986  THR A N   
7248  C CA  . THR A 988  ? 0.2294 0.2111 0.2200 0.0077  0.0074  -0.0061 986  THR A CA  
7249  C C   . THR A 988  ? 0.2784 0.2613 0.2698 0.0078  0.0066  -0.0071 986  THR A C   
7250  O O   . THR A 988  ? 0.2721 0.2546 0.2628 0.0090  0.0058  -0.0079 986  THR A O   
7251  C CB  . THR A 988  ? 0.2468 0.2284 0.2363 0.0090  0.0083  -0.0056 986  THR A CB  
7252  O OG1 . THR A 988  ? 0.2519 0.2350 0.2425 0.0087  0.0088  -0.0057 986  THR A OG1 
7253  C CG2 . THR A 988  ? 0.2556 0.2361 0.2445 0.0089  0.0089  -0.0047 986  THR A CG2 
7254  N N   . SER A 989  ? 0.2180 0.2029 0.2108 0.0068  0.0068  -0.0071 987  SER A N   
7255  C CA  A SER A 989  ? 0.2575 0.2435 0.2512 0.0069  0.0060  -0.0081 987  SER A CA  
7256  C CA  B SER A 989  ? 0.2578 0.2438 0.2515 0.0068  0.0060  -0.0080 987  SER A CA  
7257  C C   . SER A 989  ? 0.2957 0.2814 0.2907 0.0058  0.0048  -0.0083 987  SER A C   
7258  O O   . SER A 989  ? 0.3638 0.3499 0.3593 0.0062  0.0038  -0.0093 987  SER A O   
7259  C CB  A SER A 989  ? 0.2694 0.2581 0.2646 0.0063  0.0067  -0.0083 987  SER A CB  
7260  C CB  B SER A 989  ? 0.2684 0.2572 0.2637 0.0061  0.0067  -0.0082 987  SER A CB  
7261  O OG  A SER A 989  ? 0.2956 0.2861 0.2920 0.0045  0.0070  -0.0077 987  SER A OG  
7262  O OG  B SER A 989  ? 0.2933 0.2835 0.2898 0.0060  0.0059  -0.0090 987  SER A OG  
7263  N N   . ARG A 990  ? 0.2244 0.2095 0.2203 0.0046  0.0047  -0.0074 988  ARG A N   
7264  C CA  . ARG A 990  ? 0.2516 0.2364 0.2498 0.0033  0.0033  -0.0072 988  ARG A CA  
7265  C C   . ARG A 990  ? 0.2345 0.2164 0.2328 0.0041  0.0021  -0.0079 988  ARG A C   
7266  O O   . ARG A 990  ? 0.2446 0.2259 0.2450 0.0038  0.0005  -0.0087 988  ARG A O   
7267  C CB  . ARG A 990  ? 0.2535 0.2400 0.2535 0.0011  0.0036  -0.0053 988  ARG A CB  
7268  C CG  . ARG A 990  ? 0.3535 0.3436 0.3536 0.0005  0.0048  -0.0051 988  ARG A CG  
7269  C CD  . ARG A 990  ? 0.3821 0.3744 0.3842 -0.0002 0.0041  -0.0055 988  ARG A CD  
7270  N NE  . ARG A 990  ? 0.3429 0.3375 0.3476 -0.0025 0.0037  -0.0036 988  ARG A NE  
7271  C CZ  . ARG A 990  ? 0.3329 0.3297 0.3401 -0.0036 0.0029  -0.0033 988  ARG A CZ  
7272  N NH1 . ARG A 990  ? 0.3843 0.3809 0.3916 -0.0026 0.0024  -0.0050 988  ARG A NH1 
7273  N NH2 . ARG A 990  ? 0.3444 0.3440 0.3541 -0.0058 0.0027  -0.0010 988  ARG A NH2 
7274  N N   . ILE A 991  ? 0.2178 0.1983 0.2142 0.0051  0.0028  -0.0078 989  ILE A N   
7275  C CA  . ILE A 991  ? 0.2165 0.1948 0.2130 0.0061  0.0017  -0.0089 989  ILE A CA  
7276  C C   . ILE A 991  ? 0.2309 0.2095 0.2264 0.0079  0.0009  -0.0110 989  ILE A C   
7277  O O   . ILE A 991  ? 0.2423 0.2223 0.2359 0.0088  0.0016  -0.0112 989  ILE A O   
7278  C CB  . ILE A 991  ? 0.2139 0.1912 0.2087 0.0069  0.0029  -0.0082 989  ILE A CB  
7279  C CG1 . ILE A 991  ? 0.2486 0.2239 0.2443 0.0076  0.0017  -0.0092 989  ILE A CG1 
7280  C CG2 . ILE A 991  ? 0.2301 0.2083 0.2219 0.0085  0.0041  -0.0084 989  ILE A CG2 
7281  C CD1 . ILE A 991  ? 0.2660 0.2401 0.2653 0.0058  0.0005  -0.0082 989  ILE A CD1 
7282  N N   . LYS A 992  ? 0.2124 0.1897 0.2093 0.0085  -0.0008 -0.0128 990  LYS A N   
7283  C CA  . LYS A 992  ? 0.2292 0.2073 0.2251 0.0104  -0.0018 -0.0152 990  LYS A CA  
7284  C C   . LYS A 992  ? 0.2122 0.1895 0.2072 0.0121  -0.0021 -0.0168 990  LYS A C   
7285  O O   . LYS A 992  ? 0.2512 0.2272 0.2488 0.0123  -0.0039 -0.0186 990  LYS A O   
7286  C CB  . LYS A 992  ? 0.2335 0.2115 0.2326 0.0096  -0.0038 -0.0165 990  LYS A CB  
7287  C CG  . LYS A 992  ? 0.2765 0.2558 0.2766 0.0080  -0.0033 -0.0150 990  LYS A CG  
7288  C CD  . LYS A 992  ? 0.4221 0.4015 0.4254 0.0072  -0.0054 -0.0162 990  LYS A CD  
7289  C CE  . LYS A 992  ? 0.4949 0.4722 0.5024 0.0063  -0.0072 -0.0165 990  LYS A CE  
7290  N NZ  . LYS A 992  ? 0.5818 0.5591 0.5930 0.0058  -0.0095 -0.0181 990  LYS A NZ  
7291  N N   . ALA A 993  ? 0.2228 0.2011 0.2145 0.0134  -0.0006 -0.0162 991  ALA A N   
7292  C CA  . ALA A 993  ? 0.1995 0.1780 0.1901 0.0152  -0.0006 -0.0176 991  ALA A CA  
7293  C C   . ALA A 993  ? 0.2154 0.1967 0.2022 0.0169  0.0006  -0.0172 991  ALA A C   
7294  O O   . ALA A 993  ? 0.2377 0.2199 0.2233 0.0165  0.0018  -0.0152 991  ALA A O   
7295  C CB  . ALA A 993  ? 0.2165 0.1931 0.2080 0.0144  0.0001  -0.0162 991  ALA A CB  
7296  N N   . GLY A 994  ? 0.1965 0.1796 0.1819 0.0189  0.0003  -0.0191 992  GLY A N   
7297  C CA  . GLY A 994  ? 0.2098 0.1964 0.1920 0.0206  0.0013  -0.0186 992  GLY A CA  
7298  C C   . GLY A 994  ? 0.1847 0.1718 0.1652 0.0207  0.0032  -0.0159 992  GLY A C   
7299  O O   . GLY A 994  ? 0.1949 0.1845 0.1735 0.0214  0.0041  -0.0141 992  GLY A O   
7300  N N   . ASN A 995  ? 0.1847 0.1696 0.1663 0.0201  0.0037  -0.0154 993  ASN A N   
7301  C CA  . ASN A 995  ? 0.1934 0.1787 0.1738 0.0202  0.0054  -0.0130 993  ASN A CA  
7302  C C   . ASN A 995  ? 0.1950 0.1769 0.1772 0.0182  0.0059  -0.0113 993  ASN A C   
7303  O O   . ASN A 995  ? 0.1940 0.1737 0.1781 0.0175  0.0052  -0.0122 993  ASN A O   
7304  C CB  . ASN A 995  ? 0.1960 0.1830 0.1755 0.0220  0.0055  -0.0143 993  ASN A CB  
7305  C CG  . ASN A 995  ? 0.2010 0.1928 0.1779 0.0240  0.0057  -0.0149 993  ASN A CG  
7306  O OD1 . ASN A 995  ? 0.2114 0.2050 0.1879 0.0251  0.0044  -0.0177 993  ASN A OD1 
7307  N ND2 . ASN A 995  ? 0.2028 0.1971 0.1780 0.0245  0.0072  -0.0122 993  ASN A ND2 
7308  N N   . LEU A 996  ? 0.1738 0.1555 0.1557 0.0172  0.0069  -0.0090 994  LEU A N   
7309  C CA  . LEU A 996  ? 0.1858 0.1654 0.1693 0.0154  0.0075  -0.0076 994  LEU A CA  
7310  C C   . LEU A 996  ? 0.1726 0.1523 0.1553 0.0156  0.0088  -0.0057 994  LEU A C   
7311  O O   . LEU A 996  ? 0.1836 0.1652 0.1651 0.0167  0.0095  -0.0047 994  LEU A O   
7312  C CB  . LEU A 996  ? 0.1924 0.1720 0.1765 0.0142  0.0076  -0.0068 994  LEU A CB  
7313  C CG  . LEU A 996  ? 0.2112 0.1914 0.1959 0.0142  0.0064  -0.0083 994  LEU A CG  
7314  C CD1 . LEU A 996  ? 0.2548 0.2353 0.2404 0.0131  0.0066  -0.0075 994  LEU A CD1 
7315  C CD2 . LEU A 996  ? 0.2248 0.2034 0.2112 0.0135  0.0051  -0.0098 994  LEU A CD2 
7316  N N   . TYR A 997  ? 0.1789 0.1568 0.1628 0.0144  0.0091  -0.0050 995  TYR A N   
7317  C CA  . TYR A 997  ? 0.1872 0.1650 0.1708 0.0145  0.0103  -0.0033 995  TYR A CA  
7318  C C   . TYR A 997  ? 0.1841 0.1606 0.1691 0.0127  0.0106  -0.0023 995  TYR A C   
7319  O O   . TYR A 997  ? 0.2000 0.1754 0.1862 0.0115  0.0100  -0.0026 995  TYR A O   
7320  C CB  . TYR A 997  ? 0.1968 0.1744 0.1804 0.0154  0.0102  -0.0040 995  TYR A CB  
7321  C CG  . TYR A 997  ? 0.1935 0.1732 0.1758 0.0173  0.0098  -0.0056 995  TYR A CG  
7322  C CD1 . TYR A 997  ? 0.1986 0.1778 0.1815 0.0177  0.0084  -0.0081 995  TYR A CD1 
7323  C CD2 . TYR A 997  ? 0.2087 0.1911 0.1893 0.0188  0.0107  -0.0047 995  TYR A CD2 
7324  C CE1 . TYR A 997  ? 0.2307 0.2125 0.2125 0.0197  0.0078  -0.0101 995  TYR A CE1 
7325  C CE2 . TYR A 997  ? 0.2118 0.1972 0.1910 0.0207  0.0103  -0.0063 995  TYR A CE2 
7326  C CZ  . TYR A 997  ? 0.2397 0.2248 0.2194 0.0212  0.0089  -0.0092 995  TYR A CZ  
7327  O OH  . TYR A 997  ? 0.2792 0.2677 0.2574 0.0232  0.0085  -0.0113 995  TYR A OH  
7328  N N   . ILE A 998  ? 0.1713 0.1483 0.1563 0.0125  0.0115  -0.0009 996  ILE A N   
7329  C CA  A ILE A 998  ? 0.1874 0.1640 0.1737 0.0110  0.0118  -0.0003 996  ILE A CA  
7330  C CA  B ILE A 998  ? 0.1873 0.1638 0.1736 0.0110  0.0117  -0.0003 996  ILE A CA  
7331  C C   . ILE A 998  ? 0.1775 0.1537 0.1641 0.0110  0.0125  0.0009  996  ILE A C   
7332  O O   . ILE A 998  ? 0.1901 0.1668 0.1766 0.0118  0.0130  0.0019  996  ILE A O   
7333  C CB  A ILE A 998  ? 0.1912 0.1688 0.1782 0.0108  0.0119  -0.0003 996  ILE A CB  
7334  C CB  B ILE A 998  ? 0.1908 0.1684 0.1779 0.0107  0.0118  -0.0004 996  ILE A CB  
7335  C CG1 A ILE A 998  ? 0.2281 0.2063 0.2149 0.0110  0.0111  -0.0014 996  ILE A CG1 
7336  C CG1 B ILE A 998  ? 0.2302 0.2082 0.2171 0.0106  0.0111  -0.0016 996  ILE A CG1 
7337  C CG2 A ILE A 998  ? 0.2064 0.1843 0.1947 0.0093  0.0121  -0.0004 996  ILE A CG2 
7338  C CG2 B ILE A 998  ? 0.2047 0.1825 0.1931 0.0094  0.0122  -0.0002 996  ILE A CG2 
7339  C CD1 A ILE A 998  ? 0.2182 0.1961 0.2055 0.0098  0.0105  -0.0023 996  ILE A CD1 
7340  C CD1 B ILE A 998  ? 0.2275 0.2066 0.2153 0.0107  0.0110  -0.0018 996  ILE A CD1 
7341  N N   . ASN A 999  ? 0.1771 0.1525 0.1642 0.0099  0.0124  0.0011  997  ASN A N   
7342  C CA  . ASN A 999  ? 0.1886 0.1637 0.1762 0.0096  0.0129  0.0022  997  ASN A CA  
7343  C C   . ASN A 999  ? 0.1835 0.1584 0.1705 0.0110  0.0133  0.0027  997  ASN A C   
7344  O O   . ASN A 999  ? 0.1943 0.1694 0.1817 0.0112  0.0140  0.0038  997  ASN A O   
7345  C CB  . ASN A 999  ? 0.1779 0.1538 0.1665 0.0091  0.0134  0.0025  997  ASN A CB  
7346  C CG  . ASN A 999  ? 0.1853 0.1622 0.1745 0.0078  0.0131  0.0018  997  ASN A CG  
7347  O OD1 . ASN A 999  ? 0.2045 0.1814 0.1935 0.0067  0.0128  0.0018  997  ASN A OD1 
7348  N ND2 . ASN A 999  ? 0.2138 0.1916 0.2039 0.0078  0.0132  0.0012  997  ASN A ND2 
7349  N N   . ARG A 1000 ? 0.1844 0.1591 0.1707 0.0119  0.0128  0.0018  998  ARG A N   
7350  C CA  . ARG A 1000 ? 0.1918 0.1671 0.1775 0.0134  0.0132  0.0018  998  ARG A CA  
7351  C C   . ARG A 1000 ? 0.1941 0.1688 0.1799 0.0139  0.0122  0.0001  998  ARG A C   
7352  O O   . ARG A 1000 ? 0.2152 0.1888 0.2018 0.0130  0.0112  -0.0008 998  ARG A O   
7353  C CB  . ARG A 1000 ? 0.1920 0.1694 0.1766 0.0147  0.0137  0.0024  998  ARG A CB  
7354  C CG  . ARG A 1000 ? 0.1928 0.1709 0.1767 0.0150  0.0132  0.0013  998  ARG A CG  
7355  C CD  . ARG A 1000 ? 0.2009 0.1818 0.1835 0.0167  0.0135  0.0016  998  ARG A CD  
7356  N NE  . ARG A 1000 ? 0.1823 0.1642 0.1639 0.0181  0.0133  0.0002  998  ARG A NE  
7357  C CZ  . ARG A 1000 ? 0.2164 0.2016 0.1966 0.0198  0.0136  0.0001  998  ARG A CZ  
7358  N NH1 . ARG A 1000 ? 0.2280 0.2157 0.2075 0.0202  0.0140  0.0018  998  ARG A NH1 
7359  N NH2 . ARG A 1000 ? 0.2259 0.2123 0.2057 0.0211  0.0133  -0.0018 998  ARG A NH2 
7360  N N   . ASN A 1001 ? 0.1879 0.1635 0.1734 0.0154  0.0123  -0.0005 999  ASN A N   
7361  C CA  . ASN A 1001 ? 0.1917 0.1668 0.1779 0.0163  0.0112  -0.0028 999  ASN A CA  
7362  C C   . ASN A 1001 ? 0.2043 0.1807 0.1895 0.0171  0.0105  -0.0044 999  ASN A C   
7363  O O   . ASN A 1001 ? 0.2050 0.1829 0.1888 0.0172  0.0111  -0.0036 999  ASN A O   
7364  C CB  . ASN A 1001 ? 0.2318 0.2080 0.2182 0.0178  0.0114  -0.0035 999  ASN A CB  
7365  C CG  . ASN A 1001 ? 0.2349 0.2146 0.2193 0.0197  0.0124  -0.0035 999  ASN A CG  
7366  O OD1 . ASN A 1001 ? 0.2373 0.2189 0.2203 0.0205  0.0122  -0.0044 999  ASN A OD1 
7367  N ND2 . ASN A 1001 ? 0.2976 0.2788 0.2819 0.0204  0.0134  -0.0023 999  ASN A ND2 
7368  N N   . ILE A 1002 ? 0.1975 0.1732 0.1838 0.0177  0.0092  -0.0068 1000 ILE A N   
7369  C CA  . ILE A 1002 ? 0.2115 0.1883 0.1973 0.0183  0.0083  -0.0087 1000 ILE A CA  
7370  C C   . ILE A 1002 ? 0.2078 0.1874 0.1926 0.0208  0.0080  -0.0112 1000 ILE A C   
7371  O O   . ILE A 1002 ? 0.2319 0.2122 0.2168 0.0215  0.0068  -0.0135 1000 ILE A O   
7372  C CB  . ILE A 1002 ? 0.1942 0.1684 0.1823 0.0169  0.0067  -0.0095 1000 ILE A CB  
7373  C CG1 . ILE A 1002 ? 0.2113 0.1839 0.2025 0.0172  0.0052  -0.0112 1000 ILE A CG1 
7374  C CG2 . ILE A 1002 ? 0.1955 0.1683 0.1842 0.0146  0.0072  -0.0070 1000 ILE A CG2 
7375  C CD1 . ILE A 1002 ? 0.2091 0.1796 0.2033 0.0159  0.0034  -0.0120 1000 ILE A CD1 
7376  N N   A ILE A 1003 ? 0.2168 0.1984 0.2008 0.0221  0.0090  -0.0109 1001 ILE A N   
7377  N N   B ILE A 1003 ? 0.2165 0.1980 0.2003 0.0220  0.0090  -0.0108 1001 ILE A N   
7378  C CA  A ILE A 1003 ? 0.2418 0.2269 0.2249 0.0245  0.0087  -0.0136 1001 ILE A CA  
7379  C CA  B ILE A 1003 ? 0.2423 0.2273 0.2255 0.0245  0.0088  -0.0134 1001 ILE A CA  
7380  C C   A ILE A 1003 ? 0.2697 0.2595 0.2496 0.0257  0.0100  -0.0124 1001 ILE A C   
7381  C C   B ILE A 1003 ? 0.2161 0.2055 0.1965 0.0257  0.0105  -0.0116 1001 ILE A C   
7382  O O   A ILE A 1003 ? 0.2657 0.2598 0.2444 0.0278  0.0102  -0.0140 1001 ILE A O   
7383  O O   B ILE A 1003 ? 0.2445 0.2338 0.2242 0.0246  0.0117  -0.0083 1001 ILE A O   
7384  C CB  A ILE A 1003 ? 0.2284 0.2134 0.2132 0.0255  0.0086  -0.0148 1001 ILE A CB  
7385  C CB  B ILE A 1003 ? 0.2302 0.2139 0.2160 0.0252  0.0081  -0.0152 1001 ILE A CB  
7386  C CG1 A ILE A 1003 ? 0.2341 0.2190 0.2184 0.0248  0.0102  -0.0116 1001 ILE A CG1 
7387  C CG1 B ILE A 1003 ? 0.1999 0.1829 0.1858 0.0245  0.0094  -0.0124 1001 ILE A CG1 
7388  C CG2 A ILE A 1003 ? 0.2115 0.1922 0.2000 0.0246  0.0067  -0.0164 1001 ILE A CG2 
7389  C CG2 B ILE A 1003 ? 0.2076 0.1871 0.1968 0.0240  0.0061  -0.0166 1001 ILE A CG2 
7390  C CD1 A ILE A 1003 ? 0.2595 0.2450 0.2453 0.0261  0.0103  -0.0128 1001 ILE A CD1 
7391  C CD1 B ILE A 1003 ? 0.2761 0.2594 0.2640 0.0258  0.0090  -0.0142 1001 ILE A CD1 
7392  N N   A GLY A 1004 ? 0.2385 0.2280 0.2174 0.0245  0.0107  -0.0096 1002 GLY A N   
7393  N N   B GLY A 1004 ? 0.2444 0.2383 0.2236 0.0280  0.0105  -0.0138 1002 GLY A N   
7394  C CA  A GLY A 1004 ? 0.2287 0.2225 0.2053 0.0254  0.0118  -0.0077 1002 GLY A CA  
7395  C CA  B GLY A 1004 ? 0.2241 0.2234 0.2008 0.0292  0.0120  -0.0119 1002 GLY A CA  
7396  C C   A GLY A 1004 ? 0.2269 0.2241 0.2019 0.0267  0.0110  -0.0096 1002 GLY A C   
7397  C C   B GLY A 1004 ? 0.2311 0.2322 0.2059 0.0287  0.0125  -0.0096 1002 GLY A C   
7398  O O   A GLY A 1004 ? 0.2283 0.2235 0.2037 0.0260  0.0099  -0.0108 1002 GLY A O   
7399  O O   B GLY A 1004 ? 0.2492 0.2520 0.2233 0.0282  0.0138  -0.0060 1002 GLY A O   
7400  N N   A ALA A 1005 ? 0.2326 0.2353 0.2057 0.0287  0.0116  -0.0101 1003 ALA A N   
7401  N N   B ALA A 1005 ? 0.2374 0.2382 0.2117 0.0288  0.0112  -0.0115 1003 ALA A N   
7402  C CA  A ALA A 1005 ? 0.2288 0.2360 0.2000 0.0302  0.0109  -0.0117 1003 ALA A CA  
7403  C CA  B ALA A 1005 ? 0.2303 0.2331 0.2031 0.0284  0.0115  -0.0095 1003 ALA A CA  
7404  C C   A ALA A 1005 ? 0.2454 0.2588 0.2144 0.0312  0.0122  -0.0088 1003 ALA A C   
7405  C C   B ALA A 1005 ? 0.2295 0.2392 0.2000 0.0301  0.0125  -0.0080 1003 ALA A C   
7406  O O   A ALA A 1005 ? 0.2394 0.2588 0.2063 0.0332  0.0121  -0.0103 1003 ALA A O   
7407  O O   B ALA A 1005 ? 0.2710 0.2850 0.2404 0.0321  0.0125  -0.0104 1003 ALA A O   
7408  C CB  A ALA A 1005 ? 0.2425 0.2512 0.2138 0.0320  0.0096  -0.0167 1003 ALA A CB  
7409  C CB  B ALA A 1005 ? 0.2459 0.2480 0.2187 0.0286  0.0099  -0.0124 1003 ALA A CB  
7410  N N   A VAL A 1006 ? 0.2217 0.2340 0.1913 0.0299  0.0134  -0.0045 1004 VAL A N   
7411  N N   B VAL A 1006 ? 0.2226 0.2335 0.1927 0.0293  0.0134  -0.0039 1004 VAL A N   
7412  C CA  A VAL A 1006 ? 0.2171 0.2350 0.1856 0.0305  0.0146  -0.0007 1004 VAL A CA  
7413  C CA  B VAL A 1006 ? 0.2165 0.2339 0.1849 0.0305  0.0144  -0.0012 1004 VAL A CA  
7414  C C   A VAL A 1006 ? 0.2131 0.2352 0.1798 0.0312  0.0140  -0.0002 1004 VAL A C   
7415  C C   B VAL A 1006 ? 0.2145 0.2361 0.1811 0.0313  0.0138  -0.0011 1004 VAL A C   
7416  O O   A VAL A 1006 ? 0.1886 0.2079 0.1561 0.0300  0.0134  0.0011  1004 VAL A O   
7417  O O   B VAL A 1006 ? 0.2097 0.2283 0.1770 0.0302  0.0130  -0.0008 1004 VAL A O   
7418  C CB  A VAL A 1006 ? 0.2356 0.2506 0.2061 0.0287  0.0155  0.0037  1004 VAL A CB  
7419  C CB  B VAL A 1006 ? 0.2306 0.2468 0.2007 0.0290  0.0156  0.0037  1004 VAL A CB  
7420  C CG1 A VAL A 1006 ? 0.2344 0.2554 0.2044 0.0292  0.0165  0.0080  1004 VAL A CG1 
7421  C CG1 B VAL A 1006 ? 0.2368 0.2599 0.2058 0.0299  0.0165  0.0075  1004 VAL A CG1 
7422  C CG2 A VAL A 1006 ? 0.2366 0.2479 0.2086 0.0281  0.0160  0.0032  1004 VAL A CG2 
7423  C CG2 B VAL A 1006 ? 0.2344 0.2475 0.2060 0.0285  0.0162  0.0036  1004 VAL A CG2 
7424  N N   . VAL A 1007 ? 0.2052 0.2345 0.1696 0.0333  0.0141  -0.0014 1005 VAL A N   
7425  C CA  . VAL A 1007 ? 0.2154 0.2497 0.1777 0.0342  0.0134  -0.0014 1005 VAL A CA  
7426  C C   . VAL A 1007 ? 0.2226 0.2568 0.1859 0.0328  0.0137  0.0039  1005 VAL A C   
7427  O O   . VAL A 1007 ? 0.2260 0.2611 0.1905 0.0321  0.0148  0.0082  1005 VAL A O   
7428  C CB  . VAL A 1007 ? 0.2192 0.2627 0.1789 0.0367  0.0140  -0.0023 1005 VAL A CB  
7429  C CG1 . VAL A 1007 ? 0.2334 0.2832 0.1908 0.0376  0.0134  -0.0015 1005 VAL A CG1 
7430  C CG2 . VAL A 1007 ? 0.2255 0.2688 0.1849 0.0382  0.0133  -0.0083 1005 VAL A CG2 
7431  N N   . GLY A 1008 ? 0.2110 0.2440 0.1742 0.0324  0.0126  0.0035  1006 GLY A N   
7432  C CA  . GLY A 1008 ? 0.2257 0.2585 0.1903 0.0312  0.0125  0.0081  1006 GLY A CA  
7433  C C   . GLY A 1008 ? 0.2195 0.2453 0.1875 0.0291  0.0127  0.0101  1006 GLY A C   
7434  O O   . GLY A 1008 ? 0.2350 0.2601 0.2050 0.0282  0.0125  0.0137  1006 GLY A O   
7435  N N   . VAL A 1009 ? 0.2148 0.2355 0.1837 0.0285  0.0130  0.0079  1007 VAL A N   
7436  C CA  . VAL A 1009 ? 0.2185 0.2330 0.1905 0.0266  0.0133  0.0092  1007 VAL A CA  
7437  C C   . VAL A 1009 ? 0.2167 0.2255 0.1892 0.0257  0.0125  0.0055  1007 VAL A C   
7438  O O   . VAL A 1009 ? 0.2271 0.2321 0.2014 0.0244  0.0120  0.0059  1007 VAL A O   
7439  C CB  . VAL A 1009 ? 0.2164 0.2306 0.1894 0.0263  0.0145  0.0111  1007 VAL A CB  
7440  C CG1 . VAL A 1009 ? 0.2273 0.2354 0.2034 0.0244  0.0145  0.0121  1007 VAL A CG1 
7441  C CG2 . VAL A 1009 ? 0.2353 0.2555 0.2082 0.0270  0.0153  0.0154  1007 VAL A CG2 
7442  N N   . GLN A 1010 ? 0.2035 0.2119 0.1747 0.0265  0.0122  0.0018  1008 GLN A N   
7443  C CA  . GLN A 1010 ? 0.1976 0.2020 0.1693 0.0259  0.0111  -0.0018 1008 GLN A CA  
7444  C C   . GLN A 1010 ? 0.1976 0.2058 0.1672 0.0277  0.0101  -0.0050 1008 GLN A C   
7445  O O   . GLN A 1010 ? 0.2375 0.2462 0.2068 0.0287  0.0098  -0.0080 1008 GLN A O   
7446  C CB  . GLN A 1010 ? 0.2036 0.2037 0.1766 0.0251  0.0112  -0.0033 1008 GLN A CB  
7447  C CG  . GLN A 1010 ? 0.2161 0.2129 0.1910 0.0235  0.0121  -0.0005 1008 GLN A CG  
7448  C CD  . GLN A 1010 ? 0.2337 0.2322 0.2085 0.0240  0.0133  0.0012  1008 GLN A CD  
7449  O OE1 . GLN A 1010 ? 0.2291 0.2297 0.2029 0.0253  0.0134  -0.0005 1008 GLN A OE1 
7450  N NE2 . GLN A 1010 ? 0.2360 0.2337 0.2124 0.0230  0.0140  0.0045  1008 GLN A NE2 
7451  N N   . PRO A 1011 ? 0.2148 0.2261 0.1834 0.0282  0.0095  -0.0046 1009 PRO A N   
7452  C CA  . PRO A 1011 ? 0.2282 0.2427 0.1951 0.0298  0.0082  -0.0082 1009 PRO A CA  
7453  C C   . PRO A 1011 ? 0.2137 0.2235 0.1822 0.0293  0.0071  -0.0122 1009 PRO A C   
7454  O O   . PRO A 1011 ? 0.1940 0.1985 0.1646 0.0274  0.0068  -0.0118 1009 PRO A O   
7455  C CB  . PRO A 1011 ? 0.2134 0.2294 0.1801 0.0295  0.0075  -0.0068 1009 PRO A CB  
7456  C CG  . PRO A 1011 ? 0.2281 0.2446 0.1955 0.0286  0.0087  -0.0017 1009 PRO A CG  
7457  C CD  . PRO A 1011 ? 0.1965 0.2080 0.1658 0.0273  0.0096  -0.0009 1009 PRO A CD  
7458  N N   . PHE A 1012 ? 0.2101 0.2221 0.1781 0.0309  0.0063  -0.0160 1010 PHE A N   
7459  C CA  . PHE A 1012 ? 0.1931 0.2005 0.1635 0.0304  0.0053  -0.0192 1010 PHE A CA  
7460  C C   . PHE A 1012 ? 0.2074 0.2150 0.1785 0.0311  0.0032  -0.0235 1010 PHE A C   
7461  O O   . PHE A 1012 ? 0.2174 0.2303 0.1868 0.0331  0.0026  -0.0258 1010 PHE A O   
7462  C CB  . PHE A 1012 ? 0.2049 0.2136 0.1754 0.0316  0.0059  -0.0206 1010 PHE A CB  
7463  C CG  . PHE A 1012 ? 0.1937 0.1973 0.1673 0.0310  0.0048  -0.0232 1010 PHE A CG  
7464  C CD1 . PHE A 1012 ? 0.2275 0.2259 0.2031 0.0289  0.0054  -0.0208 1010 PHE A CD1 
7465  C CD2 . PHE A 1012 ? 0.2210 0.2253 0.1961 0.0324  0.0030  -0.0280 1010 PHE A CD2 
7466  C CE1 . PHE A 1012 ? 0.2298 0.2237 0.2086 0.0281  0.0042  -0.0225 1010 PHE A CE1 
7467  C CE2 . PHE A 1012 ? 0.2342 0.2336 0.2131 0.0316  0.0017  -0.0300 1010 PHE A CE2 
7468  C CZ  . PHE A 1012 ? 0.2251 0.2194 0.2058 0.0294  0.0023  -0.0270 1010 PHE A CZ  
7469  N N   . GLY A 1013 ? 0.2008 0.2031 0.1749 0.0295  0.0021  -0.0244 1011 GLY A N   
7470  C CA  . GLY A 1013 ? 0.2072 0.2088 0.1830 0.0299  -0.0001 -0.0285 1011 GLY A CA  
7471  C C   . GLY A 1013 ? 0.1988 0.1954 0.1772 0.0276  -0.0009 -0.0275 1011 GLY A C   
7472  O O   . GLY A 1013 ? 0.2241 0.2194 0.2020 0.0261  0.0002  -0.0241 1011 GLY A O   
7473  N N   . GLY A 1014 ? 0.2178 0.2119 0.1995 0.0273  -0.0029 -0.0306 1012 GLY A N   
7474  C CA  . GLY A 1014 ? 0.2514 0.2411 0.2361 0.0249  -0.0037 -0.0296 1012 GLY A CA  
7475  C C   . GLY A 1014 ? 0.2277 0.2179 0.2140 0.0250  -0.0058 -0.0321 1012 GLY A C   
7476  O O   . GLY A 1014 ? 0.2342 0.2284 0.2185 0.0268  -0.0064 -0.0343 1012 GLY A O   
7477  N N   . ARG A 1015 ? 0.2085 0.1949 0.1984 0.0229  -0.0068 -0.0316 1013 ARG A N   
7478  C CA  . ARG A 1015 ? 0.2230 0.2093 0.2149 0.0223  -0.0086 -0.0330 1013 ARG A CA  
7479  C C   . ARG A 1015 ? 0.2202 0.2030 0.2176 0.0213  -0.0109 -0.0349 1013 ARG A C   
7480  O O   . ARG A 1015 ? 0.2101 0.1905 0.2096 0.0209  -0.0109 -0.0347 1013 ARG A O   
7481  C CB  . ARG A 1015 ? 0.2366 0.2222 0.2279 0.0204  -0.0074 -0.0296 1013 ARG A CB  
7482  C CG  . ARG A 1015 ? 0.2420 0.2241 0.2353 0.0180  -0.0065 -0.0265 1013 ARG A CG  
7483  C CD  . ARG A 1015 ? 0.2874 0.2691 0.2814 0.0161  -0.0059 -0.0240 1013 ARG A CD  
7484  N NE  . ARG A 1015 ? 0.3405 0.3235 0.3356 0.0162  -0.0075 -0.0257 1013 ARG A NE  
7485  C CZ  . ARG A 1015 ? 0.3866 0.3682 0.3857 0.0153  -0.0096 -0.0274 1013 ARG A CZ  
7486  N NH1 . ARG A 1015 ? 0.3346 0.3135 0.3374 0.0142  -0.0106 -0.0274 1013 ARG A NH1 
7487  N NH2 . ARG A 1015 ? 0.3305 0.3135 0.3302 0.0156  -0.0110 -0.0290 1013 ARG A NH2 
7488  N N   . GLY A 1016 ? 0.2345 0.2169 0.2346 0.0206  -0.0128 -0.0364 1014 GLY A N   
7489  C CA  . GLY A 1016 ? 0.2328 0.2119 0.2390 0.0195  -0.0153 -0.0379 1014 GLY A CA  
7490  C C   . GLY A 1016 ? 0.2349 0.2142 0.2430 0.0216  -0.0170 -0.0421 1014 GLY A C   
7491  O O   . GLY A 1016 ? 0.2463 0.2293 0.2517 0.0242  -0.0173 -0.0455 1014 GLY A O   
7492  N N   . LEU A 1017 ? 0.2231 0.1989 0.2359 0.0207  -0.0181 -0.0419 1015 LEU A N   
7493  C CA  . LEU A 1017 ? 0.2229 0.1984 0.2384 0.0227  -0.0198 -0.0461 1015 LEU A CA  
7494  C C   . LEU A 1017 ? 0.2370 0.2154 0.2476 0.0249  -0.0177 -0.0466 1015 LEU A C   
7495  O O   . LEU A 1017 ? 0.2420 0.2213 0.2542 0.0270  -0.0189 -0.0504 1015 LEU A O   
7496  C CB  . LEU A 1017 ? 0.2428 0.2137 0.2649 0.0209  -0.0214 -0.0448 1015 LEU A CB  
7497  C CG  . LEU A 1017 ? 0.2483 0.2165 0.2767 0.0186  -0.0239 -0.0442 1015 LEU A CG  
7498  C CD1 . LEU A 1017 ? 0.2598 0.2239 0.2944 0.0166  -0.0251 -0.0417 1015 LEU A CD1 
7499  C CD2 . LEU A 1017 ? 0.2721 0.2413 0.3038 0.0204  -0.0271 -0.0499 1015 LEU A CD2 
7500  N N   . SER A 1018 ? 0.2019 0.1820 0.2070 0.0245  -0.0147 -0.0429 1016 SER A N   
7501  C CA  . SER A 1018 ? 0.2194 0.2022 0.2202 0.0262  -0.0125 -0.0425 1016 SER A CA  
7502  C C   . SER A 1018 ? 0.1964 0.1849 0.1921 0.0286  -0.0117 -0.0443 1016 SER A C   
7503  O O   . SER A 1018 ? 0.2324 0.2241 0.2248 0.0303  -0.0102 -0.0443 1016 SER A O   
7504  C CB  . SER A 1018 ? 0.2073 0.1886 0.2057 0.0243  -0.0098 -0.0372 1016 SER A CB  
7505  O OG  . SER A 1018 ? 0.2121 0.1889 0.2147 0.0223  -0.0105 -0.0354 1016 SER A OG  
7506  N N   . GLY A 1019 ? 0.2079 0.1982 0.2029 0.0287  -0.0127 -0.0454 1017 GLY A N   
7507  C CA  . GLY A 1019 ? 0.2405 0.2370 0.2308 0.0310  -0.0120 -0.0467 1017 GLY A CA  
7508  C C   . GLY A 1019 ? 0.2320 0.2303 0.2213 0.0307  -0.0129 -0.0470 1017 GLY A C   
7509  O O   . GLY A 1019 ? 0.2387 0.2336 0.2300 0.0285  -0.0132 -0.0449 1017 GLY A O   
7510  N N   . THR A 1020 ? 0.2356 0.2397 0.2218 0.0331  -0.0133 -0.0498 1018 THR A N   
7511  C CA  . THR A 1020 ? 0.2298 0.2369 0.2141 0.0332  -0.0138 -0.0495 1018 THR A CA  
7512  C C   . THR A 1020 ? 0.2078 0.2178 0.1872 0.0330  -0.0112 -0.0448 1018 THR A C   
7513  O O   . THR A 1020 ? 0.2339 0.2450 0.2123 0.0324  -0.0112 -0.0430 1018 THR A O   
7514  C CB  . THR A 1020 ? 0.2286 0.2416 0.2118 0.0361  -0.0156 -0.0548 1018 THR A CB  
7515  O OG1 . THR A 1020 ? 0.2199 0.2382 0.1993 0.0383  -0.0142 -0.0554 1018 THR A OG1 
7516  C CG2 . THR A 1020 ? 0.2783 0.2885 0.2671 0.0364  -0.0187 -0.0601 1018 THR A CG2 
7517  N N   . GLY A 1021 ? 0.2306 0.2421 0.2075 0.0337  -0.0091 -0.0427 1019 GLY A N   
7518  C CA  . GLY A 1021 ? 0.2406 0.2562 0.2133 0.0341  -0.0070 -0.0388 1019 GLY A CA  
7519  C C   . GLY A 1021 ? 0.2328 0.2561 0.2024 0.0365  -0.0078 -0.0410 1019 GLY A C   
7520  O O   . GLY A 1021 ? 0.2312 0.2566 0.2018 0.0380  -0.0099 -0.0461 1019 GLY A O   
7521  N N   . PRO A 1022 ? 0.2381 0.2662 0.2040 0.0370  -0.0062 -0.0373 1020 PRO A N   
7522  C CA  . PRO A 1022 ? 0.2394 0.2658 0.2044 0.0355  -0.0038 -0.0315 1020 PRO A CA  
7523  C C   . PRO A 1022 ? 0.2454 0.2710 0.2103 0.0358  -0.0023 -0.0308 1020 PRO A C   
7524  O O   . PRO A 1022 ? 0.2524 0.2801 0.2172 0.0374  -0.0028 -0.0346 1020 PRO A O   
7525  C CB  . PRO A 1022 ? 0.2278 0.2612 0.1894 0.0366  -0.0032 -0.0287 1020 PRO A CB  
7526  C CG  . PRO A 1022 ? 0.2532 0.2936 0.2126 0.0392  -0.0044 -0.0331 1020 PRO A CG  
7527  C CD  . PRO A 1022 ? 0.2180 0.2545 0.1804 0.0393  -0.0067 -0.0386 1020 PRO A CD  
7528  N N   . LYS A 1023 ? 0.2265 0.2491 0.1916 0.0342  -0.0005 -0.0262 1021 LYS A N   
7529  C CA  . LYS A 1023 ? 0.2079 0.2292 0.1733 0.0341  0.0010  -0.0251 1021 LYS A CA  
7530  C C   . LYS A 1023 ? 0.2166 0.2452 0.1789 0.0362  0.0020  -0.0247 1021 LYS A C   
7531  O O   . LYS A 1023 ? 0.2252 0.2589 0.1852 0.0367  0.0027  -0.0216 1021 LYS A O   
7532  C CB  . LYS A 1023 ? 0.2143 0.2314 0.1806 0.0320  0.0025  -0.0202 1021 LYS A CB  
7533  C CG  . LYS A 1023 ? 0.2088 0.2187 0.1783 0.0298  0.0020  -0.0203 1021 LYS A CG  
7534  C CD  . LYS A 1023 ? 0.2097 0.2170 0.1798 0.0280  0.0036  -0.0158 1021 LYS A CD  
7535  C CE  . LYS A 1023 ? 0.2198 0.2208 0.1928 0.0259  0.0034  -0.0157 1021 LYS A CE  
7536  N NZ  . LYS A 1023 ? 0.2127 0.2109 0.1868 0.0256  0.0037  -0.0166 1021 LYS A NZ  
7537  N N   . ALA A 1024 ? 0.2294 0.2587 0.1921 0.0374  0.0021  -0.0275 1022 ALA A N   
7538  C CA  . ALA A 1024 ? 0.2475 0.2832 0.2078 0.0391  0.0036  -0.0263 1022 ALA A CA  
7539  C C   . ALA A 1024 ? 0.2298 0.2640 0.1899 0.0375  0.0056  -0.0203 1022 ALA A C   
7540  O O   . ALA A 1024 ? 0.2334 0.2608 0.1958 0.0354  0.0060  -0.0184 1022 ALA A O   
7541  C CB  . ALA A 1024 ? 0.2308 0.2663 0.1923 0.0404  0.0033  -0.0305 1022 ALA A CB  
7542  N N   . GLY A 1025 ? 0.2208 0.2621 0.1784 0.0385  0.0069  -0.0172 1023 GLY A N   
7543  C CA  . GLY A 1025 ? 0.2178 0.2582 0.1760 0.0372  0.0086  -0.0114 1023 GLY A CA  
7544  C C   . GLY A 1025 ? 0.2168 0.2537 0.1761 0.0353  0.0085  -0.0077 1023 GLY A C   
7545  O O   . GLY A 1025 ? 0.2236 0.2573 0.1846 0.0337  0.0095  -0.0036 1023 GLY A O   
7546  N N   . GLY A 1026 ? 0.2028 0.2402 0.1617 0.0354  0.0070  -0.0093 1024 GLY A N   
7547  C CA  . GLY A 1026 ? 0.2024 0.2372 0.1625 0.0339  0.0067  -0.0062 1024 GLY A CA  
7548  C C   . GLY A 1026 ? 0.2159 0.2575 0.1740 0.0350  0.0059  -0.0052 1024 GLY A C   
7549  O O   . GLY A 1026 ? 0.2084 0.2568 0.1638 0.0370  0.0055  -0.0074 1024 GLY A O   
7550  N N   . PRO A 1027 ? 0.1996 0.2395 0.1591 0.0338  0.0055  -0.0019 1025 PRO A N   
7551  C CA  . PRO A 1027 ? 0.2149 0.2616 0.1729 0.0346  0.0050  0.0007  1025 PRO A CA  
7552  C C   . PRO A 1027 ? 0.1830 0.2320 0.1396 0.0356  0.0032  -0.0032 1025 PRO A C   
7553  O O   . PRO A 1027 ? 0.2058 0.2614 0.1606 0.0366  0.0027  -0.0014 1025 PRO A O   
7554  C CB  . PRO A 1027 ? 0.2202 0.2632 0.1813 0.0328  0.0051  0.0056  1025 PRO A CB  
7555  C CG  . PRO A 1027 ? 0.2283 0.2624 0.1921 0.0312  0.0051  0.0033  1025 PRO A CG  
7556  C CD  . PRO A 1027 ? 0.2035 0.2361 0.1664 0.0316  0.0058  0.0002  1025 PRO A CD  
7557  N N   . LEU A 1028 ? 0.1960 0.2399 0.1535 0.0354  0.0022  -0.0081 1026 LEU A N   
7558  C CA  . LEU A 1028 ? 0.2053 0.2512 0.1618 0.0363  0.0004  -0.0121 1026 LEU A CA  
7559  C C   . LEU A 1028 ? 0.2084 0.2594 0.1626 0.0385  -0.0002 -0.0171 1026 LEU A C   
7560  O O   . LEU A 1028 ? 0.2299 0.2839 0.1832 0.0397  -0.0019 -0.0208 1026 LEU A O   
7561  C CB  . LEU A 1028 ? 0.2145 0.2525 0.1740 0.0348  -0.0007 -0.0147 1026 LEU A CB  
7562  C CG  . LEU A 1028 ? 0.2562 0.2898 0.2182 0.0328  -0.0005 -0.0110 1026 LEU A CG  
7563  C CD1 . LEU A 1028 ? 0.2463 0.2730 0.2110 0.0313  -0.0013 -0.0138 1026 LEU A CD1 
7564  C CD2 . LEU A 1028 ? 0.3797 0.4181 0.3408 0.0333  -0.0013 -0.0087 1026 LEU A CD2 
7565  N N   . TYR A 1029 ? 0.2047 0.2573 0.1581 0.0393  0.0010  -0.0173 1027 TYR A N   
7566  C CA  . TYR A 1029 ? 0.2139 0.2702 0.1660 0.0414  0.0004  -0.0228 1027 TYR A CA  
7567  C C   . TYR A 1029 ? 0.1960 0.2627 0.1446 0.0437  -0.0002 -0.0241 1027 TYR A C   
7568  O O   . TYR A 1029 ? 0.2228 0.2918 0.1709 0.0452  -0.0020 -0.0296 1027 TYR A O   
7569  C CB  . TYR A 1029 ? 0.2204 0.2765 0.1725 0.0416  0.0021  -0.0219 1027 TYR A CB  
7570  C CG  . TYR A 1029 ? 0.2198 0.2761 0.1723 0.0432  0.0015  -0.0278 1027 TYR A CG  
7571  C CD1 . TYR A 1029 ? 0.2230 0.2718 0.1788 0.0424  0.0002  -0.0318 1027 TYR A CD1 
7572  C CD2 . TYR A 1029 ? 0.2056 0.2699 0.1559 0.0455  0.0023  -0.0291 1027 TYR A CD2 
7573  C CE1 . TYR A 1029 ? 0.2261 0.2747 0.1831 0.0439  -0.0006 -0.0370 1027 TYR A CE1 
7574  C CE2 . TYR A 1029 ? 0.2205 0.2848 0.1717 0.0470  0.0017  -0.0347 1027 TYR A CE2 
7575  C CZ  . TYR A 1029 ? 0.2199 0.2762 0.1748 0.0462  0.0001  -0.0387 1027 TYR A CZ  
7576  O OH  . TYR A 1029 ? 0.2440 0.3003 0.2005 0.0479  -0.0007 -0.0441 1027 TYR A OH  
7577  N N   . LEU A 1030 ? 0.2157 0.2892 0.1621 0.0441  0.0011  -0.0189 1028 LEU A N   
7578  C CA  . LEU A 1030 ? 0.2026 0.2873 0.1453 0.0464  0.0006  -0.0198 1028 LEU A CA  
7579  C C   . LEU A 1030 ? 0.2150 0.3011 0.1573 0.0466  -0.0014 -0.0217 1028 LEU A C   
7580  O O   . LEU A 1030 ? 0.2376 0.3314 0.1774 0.0488  -0.0026 -0.0256 1028 LEU A O   
7581  C CB  . LEU A 1030 ? 0.2331 0.3250 0.1740 0.0464  0.0023  -0.0129 1028 LEU A CB  
7582  C CG  . LEU A 1030 ? 0.2374 0.3301 0.1785 0.0463  0.0044  -0.0106 1028 LEU A CG  
7583  C CD1 . LEU A 1030 ? 0.2928 0.3934 0.2325 0.0462  0.0057  -0.0034 1028 LEU A CD1 
7584  C CD2 . LEU A 1030 ? 0.2546 0.3516 0.1941 0.0487  0.0044  -0.0168 1028 LEU A CD2 
7585  N N   . GLY A 1031 ? 0.2209 0.3000 0.1657 0.0445  -0.0020 -0.0191 1029 GLY A N   
7586  C CA  . GLY A 1031 ? 0.2367 0.3170 0.1813 0.0446  -0.0039 -0.0203 1029 GLY A CA  
7587  C C   . GLY A 1031 ? 0.2435 0.3223 0.1887 0.0456  -0.0060 -0.0279 1029 GLY A C   
7588  O O   . GLY A 1031 ? 0.2666 0.3492 0.2109 0.0465  -0.0077 -0.0300 1029 GLY A O   
7589  N N   . ARG A 1032 ? 0.2149 0.2883 0.1621 0.0456  -0.0060 -0.0319 1030 ARG A N   
7590  C CA  . ARG A 1032 ? 0.2194 0.2913 0.1681 0.0467  -0.0082 -0.0392 1030 ARG A CA  
7591  C C   . ARG A 1032 ? 0.2423 0.3241 0.1880 0.0498  -0.0089 -0.0440 1030 ARG A C   
7592  O O   . ARG A 1032 ? 0.2670 0.3495 0.2138 0.0511  -0.0112 -0.0503 1030 ARG A O   
7593  C CB  . ARG A 1032 ? 0.2606 0.3235 0.2129 0.0455  -0.0080 -0.0413 1030 ARG A CB  
7594  C CG  . ARG A 1032 ? 0.2223 0.2813 0.1779 0.0458  -0.0105 -0.0479 1030 ARG A CG  
7595  C CD  . ARG A 1032 ? 0.2356 0.2900 0.1933 0.0441  -0.0119 -0.0473 1030 ARG A CD  
7596  N NE  . ARG A 1032 ? 0.2582 0.3073 0.2202 0.0438  -0.0142 -0.0527 1030 ARG A NE  
7597  C CZ  . ARG A 1032 ? 0.2824 0.3329 0.2457 0.0444  -0.0168 -0.0568 1030 ARG A CZ  
7598  N NH1 . ARG A 1032 ? 0.3083 0.3654 0.2686 0.0455  -0.0174 -0.0565 1030 ARG A NH1 
7599  N NH2 . ARG A 1032 ? 0.2829 0.3281 0.2509 0.0440  -0.0189 -0.0613 1030 ARG A NH2 
7600  N N   . LEU A 1033 ? 0.2211 0.3109 0.1635 0.0510  -0.0072 -0.0412 1031 LEU A N   
7601  C CA  . LEU A 1033 ? 0.2186 0.3184 0.1581 0.0541  -0.0075 -0.0457 1031 LEU A CA  
7602  C C   . LEU A 1033 ? 0.2476 0.3587 0.1830 0.0556  -0.0079 -0.0442 1031 LEU A C   
7603  O O   . LEU A 1033 ? 0.2580 0.3798 0.1903 0.0581  -0.0078 -0.0466 1031 LEU A O   
7604  C CB  . LEU A 1033 ? 0.2275 0.3296 0.1662 0.0547  -0.0052 -0.0439 1031 LEU A CB  
7605  C CG  . LEU A 1033 ? 0.2498 0.3406 0.1925 0.0529  -0.0046 -0.0442 1031 LEU A CG  
7606  C CD1 . LEU A 1033 ? 0.2400 0.3332 0.1817 0.0534  -0.0023 -0.0419 1031 LEU A CD1 
7607  C CD2 . LEU A 1033 ? 0.2737 0.3596 0.2196 0.0537  -0.0069 -0.0519 1031 LEU A CD2 
7608  N N   . VAL A 1034 ? 0.2529 0.3624 0.1885 0.0540  -0.0085 -0.0401 1032 VAL A N   
7609  C CA  . VAL A 1034 ? 0.2549 0.3744 0.1871 0.0552  -0.0093 -0.0384 1032 VAL A CA  
7610  C C   . VAL A 1034 ? 0.2710 0.3862 0.2052 0.0545  -0.0117 -0.0411 1032 VAL A C   
7611  O O   . VAL A 1034 ? 0.2702 0.3746 0.2083 0.0526  -0.0123 -0.0422 1032 VAL A O   
7612  C CB  . VAL A 1034 ? 0.2374 0.3605 0.1682 0.0539  -0.0074 -0.0292 1032 VAL A CB  
7613  C CG1 . VAL A 1034 ? 0.2639 0.3936 0.1925 0.0549  -0.0051 -0.0267 1032 VAL A CG1 
7614  C CG2 . VAL A 1034 ? 0.2544 0.3659 0.1891 0.0508  -0.0068 -0.0243 1032 VAL A CG2 
7615  N N   . THR A 1035 ? 0.2751 0.3994 0.2065 0.0560  -0.0132 -0.0421 1033 THR A N   
7616  C CA  . THR A 1035 ? 0.2809 0.4021 0.2141 0.0556  -0.0157 -0.0451 1033 THR A CA  
7617  C C   . THR A 1035 ? 0.3556 0.4706 0.2907 0.0529  -0.0155 -0.0387 1033 THR A C   
7618  O O   . THR A 1035 ? 0.3965 0.5043 0.3347 0.0517  -0.0170 -0.0407 1033 THR A O   
7619  C CB  . THR A 1035 ? 0.3359 0.4691 0.2655 0.0582  -0.0176 -0.0488 1033 THR A CB  
7620  O OG1 . THR A 1035 ? 0.4215 0.5647 0.3472 0.0586  -0.0163 -0.0423 1033 THR A OG1 
7621  C CG2 . THR A 1035 ? 0.3180 0.4564 0.2467 0.0610  -0.0183 -0.0567 1033 THR A CG2 
7622  N N   . THR A 1036 ? 0.2755 0.3934 0.2093 0.0521  -0.0136 -0.0310 1034 THR A N   
7623  C CA  . THR A 1036 ? 0.3119 0.4241 0.2481 0.0496  -0.0133 -0.0247 1034 THR A CA  
7624  C C   . THR A 1036 ? 0.2979 0.4047 0.2357 0.0480  -0.0108 -0.0196 1034 THR A C   
7625  O O   . THR A 1036 ? 0.3150 0.4282 0.2506 0.0486  -0.0092 -0.0156 1034 THR A O   
7626  C CB  . THR A 1036 ? 0.3854 0.5069 0.3192 0.0502  -0.0139 -0.0198 1034 THR A CB  
7627  O OG1 . THR A 1036 ? 0.4053 0.5324 0.3374 0.0518  -0.0163 -0.0250 1034 THR A OG1 
7628  C CG2 . THR A 1036 ? 0.3916 0.5070 0.3287 0.0478  -0.0137 -0.0135 1034 THR A CG2 
7629  N N   . ALA A 1037 ? 0.2844 0.3798 0.2260 0.0460  -0.0105 -0.0197 1035 ALA A N   
7630  C CA  . ALA A 1037 ? 0.3052 0.3951 0.2485 0.0445  -0.0083 -0.0159 1035 ALA A CA  
7631  C C   . ALA A 1037 ? 0.2747 0.3661 0.2187 0.0433  -0.0073 -0.0078 1035 ALA A C   
7632  O O   . ALA A 1037 ? 0.2822 0.3729 0.2277 0.0425  -0.0084 -0.0054 1035 ALA A O   
7633  C CB  . ALA A 1037 ? 0.3219 0.4000 0.2692 0.0427  -0.0084 -0.0183 1035 ALA A CB  
7634  N N   . PRO A 1038 ? 0.2624 0.3562 0.2059 0.0432  -0.0054 -0.0036 1036 PRO A N   
7635  C CA  . PRO A 1038 ? 0.2515 0.3456 0.1969 0.0419  -0.0046 0.0043  1036 PRO A CA  
7636  C C   . PRO A 1038 ? 0.2597 0.3424 0.2096 0.0396  -0.0042 0.0057  1036 PRO A C   
7637  O O   . PRO A 1038 ? 0.2515 0.3267 0.2028 0.0390  -0.0042 0.0013  1036 PRO A O   
7638  C CB  . PRO A 1038 ? 0.3086 0.4085 0.2522 0.0426  -0.0028 0.0073  1036 PRO A CB  
7639  C CG  . PRO A 1038 ? 0.2929 0.3889 0.2357 0.0432  -0.0021 0.0013  1036 PRO A CG  
7640  C CD  . PRO A 1038 ? 0.2713 0.3668 0.2130 0.0443  -0.0040 -0.0059 1036 PRO A CD  
7641  N N   . VAL A 1039 ? 0.2581 0.3402 0.2108 0.0383  -0.0040 0.0122  1037 VAL A N   
7642  C CA  . VAL A 1039 ? 0.2420 0.3145 0.1993 0.0363  -0.0034 0.0140  1037 VAL A CA  
7643  C C   . VAL A 1039 ? 0.2295 0.3002 0.1872 0.0358  -0.0015 0.0158  1037 VAL A C   
7644  O O   . VAL A 1039 ? 0.2445 0.3206 0.2022 0.0360  -0.0007 0.0211  1037 VAL A O   
7645  C CB  . VAL A 1039 ? 0.2503 0.3227 0.2111 0.0353  -0.0043 0.0197  1037 VAL A CB  
7646  C CG1 . VAL A 1039 ? 0.2713 0.3342 0.2370 0.0334  -0.0038 0.0209  1037 VAL A CG1 
7647  C CG2 . VAL A 1039 ? 0.2988 0.3734 0.2590 0.0358  -0.0063 0.0179  1037 VAL A CG2 
7648  N N   . PRO A 1040 ? 0.2315 0.2951 0.1900 0.0352  -0.0007 0.0121  1038 PRO A N   
7649  C CA  . PRO A 1040 ? 0.2415 0.3036 0.2005 0.0348  0.0010  0.0137  1038 PRO A CA  
7650  C C   . PRO A 1040 ? 0.2155 0.2748 0.1786 0.0333  0.0016  0.0198  1038 PRO A C   
7651  O O   . PRO A 1040 ? 0.2140 0.2697 0.1804 0.0322  0.0006  0.0215  1038 PRO A O   
7652  C CB  . PRO A 1040 ? 0.2491 0.3032 0.2087 0.0342  0.0013  0.0084  1038 PRO A CB  
7653  C CG  . PRO A 1040 ? 0.2716 0.3257 0.2298 0.0349  -0.0002 0.0033  1038 PRO A CG  
7654  C CD  . PRO A 1040 ? 0.2607 0.3181 0.2196 0.0348  -0.0015 0.0062  1038 PRO A CD  
7655  N N   . PRO A 1041 ? 0.2132 0.2741 0.1767 0.0331  0.0030  0.0231  1039 PRO A N   
7656  C CA  . PRO A 1041 ? 0.2007 0.2580 0.1690 0.0315  0.0033  0.0283  1039 PRO A CA  
7657  C C   . PRO A 1041 ? 0.2171 0.2645 0.1886 0.0301  0.0031  0.0257  1039 PRO A C   
7658  O O   . PRO A 1041 ? 0.2257 0.2688 0.1959 0.0300  0.0035  0.0207  1039 PRO A O   
7659  C CB  . PRO A 1041 ? 0.2338 0.2935 0.2014 0.0317  0.0050  0.0304  1039 PRO A CB  
7660  C CG  . PRO A 1041 ? 0.2875 0.3549 0.2498 0.0336  0.0054  0.0277  1039 PRO A CG  
7661  C CD  . PRO A 1041 ? 0.2535 0.3188 0.2136 0.0343  0.0043  0.0215  1039 PRO A CD  
7662  N N   . GLN A 1042 ? 0.2034 0.2477 0.1796 0.0290  0.0024  0.0291  1040 GLN A N   
7663  C CA  . GLN A 1042 ? 0.2101 0.2461 0.1901 0.0276  0.0022  0.0274  1040 GLN A CA  
7664  C C   . GLN A 1042 ? 0.2150 0.2475 0.1938 0.0276  0.0015  0.0221  1040 GLN A C   
7665  O O   . GLN A 1042 ? 0.2229 0.2491 0.2043 0.0265  0.0015  0.0200  1040 GLN A O   
7666  C CB  . GLN A 1042 ? 0.2425 0.2739 0.2234 0.0268  0.0036  0.0267  1040 GLN A CB  
7667  C CG  . GLN A 1042 ? 0.3294 0.3638 0.3120 0.0267  0.0044  0.0318  1040 GLN A CG  
7668  C CD  . GLN A 1042 ? 0.3771 0.4068 0.3608 0.0259  0.0057  0.0308  1040 GLN A CD  
7669  O OE1 . GLN A 1042 ? 0.5339 0.5594 0.5223 0.0247  0.0055  0.0326  1040 GLN A OE1 
7670  N NE2 . GLN A 1042 ? 0.4418 0.4723 0.4215 0.0265  0.0068  0.0276  1040 GLN A NE2 
7671  N N   . HIS A 1043 ? 0.2002 0.2371 0.1755 0.0287  0.0007  0.0199  1041 HIS A N   
7672  C CA  . HIS A 1043 ? 0.1920 0.2260 0.1660 0.0287  0.0000  0.0147  1041 HIS A CA  
7673  C C   . HIS A 1043 ? 0.2009 0.2342 0.1776 0.0284  -0.0015 0.0155  1041 HIS A C   
7674  O O   . HIS A 1043 ? 0.2061 0.2447 0.1816 0.0293  -0.0026 0.0166  1041 HIS A O   
7675  C CB  . HIS A 1043 ? 0.2118 0.2509 0.1811 0.0303  -0.0003 0.0114  1041 HIS A CB  
7676  C CG  . HIS A 1043 ? 0.2250 0.2613 0.1935 0.0303  -0.0012 0.0060  1041 HIS A CG  
7677  N ND1 . HIS A 1043 ? 0.2102 0.2419 0.1785 0.0298  -0.0008 0.0019  1041 HIS A ND1 
7678  C CD2 . HIS A 1043 ? 0.2083 0.2462 0.1766 0.0307  -0.0028 0.0043  1041 HIS A CD2 
7679  C CE1 . HIS A 1043 ? 0.2307 0.2610 0.1989 0.0299  -0.0020 -0.0020 1041 HIS A CE1 
7680  N NE2 . HIS A 1043 ? 0.2214 0.2554 0.1895 0.0304  -0.0032 -0.0008 1041 HIS A NE2 
7681  N N   . SER A 1044 ? 0.2054 0.2326 0.1860 0.0271  -0.0015 0.0150  1042 SER A N   
7682  C CA  . SER A 1044 ? 0.1848 0.2108 0.1685 0.0268  -0.0029 0.0150  1042 SER A CA  
7683  C C   . SER A 1044 ? 0.1873 0.2066 0.1742 0.0254  -0.0024 0.0129  1042 SER A C   
7684  O O   . SER A 1044 ? 0.2135 0.2297 0.2005 0.0248  -0.0012 0.0123  1042 SER A O   
7685  C CB  . SER A 1044 ? 0.2125 0.2415 0.1993 0.0269  -0.0038 0.0204  1042 SER A CB  
7686  O OG  . SER A 1044 ? 0.2094 0.2355 0.2000 0.0261  -0.0031 0.0233  1042 SER A OG  
7687  N N   . SER A 1045 ? 0.1891 0.2068 0.1786 0.0251  -0.0034 0.0118  1043 SER A N   
7688  C CA  . SER A 1045 ? 0.1886 0.2011 0.1815 0.0239  -0.0031 0.0099  1043 SER A CA  
7689  C C   . SER A 1045 ? 0.1817 0.1940 0.1788 0.0239  -0.0044 0.0108  1043 SER A C   
7690  O O   . SER A 1045 ? 0.2001 0.2152 0.1965 0.0244  -0.0056 0.0106  1043 SER A O   
7691  C CB  . SER A 1045 ? 0.2096 0.2197 0.2003 0.0234  -0.0027 0.0053  1043 SER A CB  
7692  O OG  . SER A 1045 ? 0.2246 0.2308 0.2186 0.0222  -0.0023 0.0037  1043 SER A OG  
7693  N N   . VAL A 1046 ? 0.1944 0.2037 0.1962 0.0233  -0.0043 0.0116  1044 VAL A N   
7694  C CA  . VAL A 1046 ? 0.2049 0.2138 0.2115 0.0233  -0.0055 0.0118  1044 VAL A CA  
7695  C C   . VAL A 1046 ? 0.1820 0.1889 0.1890 0.0227  -0.0055 0.0076  1044 VAL A C   
7696  O O   . VAL A 1046 ? 0.2308 0.2377 0.2415 0.0228  -0.0065 0.0072  1044 VAL A O   
7697  C CB  . VAL A 1046 ? 0.2396 0.2464 0.2522 0.0231  -0.0058 0.0140  1044 VAL A CB  
7698  C CG1 . VAL A 1046 ? 0.2418 0.2510 0.2550 0.0235  -0.0062 0.0191  1044 VAL A CG1 
7699  C CG2 . VAL A 1046 ? 0.2285 0.2316 0.2418 0.0222  -0.0045 0.0115  1044 VAL A CG2 
7700  N N   . HIS A 1047 ? 0.1802 0.1858 0.1837 0.0221  -0.0044 0.0046  1045 HIS A N   
7701  C CA  . HIS A 1047 ? 0.2096 0.2137 0.2138 0.0213  -0.0043 0.0010  1045 HIS A CA  
7702  C C   . HIS A 1047 ? 0.2002 0.2063 0.2020 0.0215  -0.0052 -0.0006 1045 HIS A C   
7703  O O   . HIS A 1047 ? 0.2154 0.2235 0.2135 0.0221  -0.0054 -0.0003 1045 HIS A O   
7704  C CB  . HIS A 1047 ? 0.2483 0.2498 0.2508 0.0203  -0.0027 -0.0009 1045 HIS A CB  
7705  C CG  . HIS A 1047 ? 0.2838 0.2835 0.2885 0.0201  -0.0019 0.0005  1045 HIS A CG  
7706  N ND1 . HIS A 1047 ? 0.3310 0.3295 0.3405 0.0199  -0.0020 0.0001  1045 HIS A ND1 
7707  C CD2 . HIS A 1047 ? 0.3213 0.3204 0.3246 0.0202  -0.0011 0.0023  1045 HIS A CD2 
7708  C CE1 . HIS A 1047 ? 0.3164 0.3135 0.3273 0.0198  -0.0014 0.0013  1045 HIS A CE1 
7709  N NE2 . HIS A 1047 ? 0.3355 0.3328 0.3427 0.0199  -0.0008 0.0029  1045 HIS A NE2 
7710  N N   . THR A 1048 ? 0.2026 0.2086 0.2068 0.0211  -0.0058 -0.0024 1046 THR A N   
7711  C CA  . THR A 1048 ? 0.2315 0.2394 0.2343 0.0212  -0.0069 -0.0041 1046 THR A CA  
7712  C C   . THR A 1048 ? 0.2102 0.2164 0.2133 0.0200  -0.0063 -0.0073 1046 THR A C   
7713  O O   . THR A 1048 ? 0.2191 0.2241 0.2252 0.0192  -0.0057 -0.0080 1046 THR A O   
7714  C CB  . THR A 1048 ? 0.2074 0.2172 0.2133 0.0219  -0.0084 -0.0031 1046 THR A CB  
7715  O OG1 . THR A 1048 ? 0.2375 0.2489 0.2442 0.0229  -0.0089 0.0005  1046 THR A OG1 
7716  C CG2 . THR A 1048 ? 0.2275 0.2396 0.2316 0.0221  -0.0097 -0.0047 1046 THR A CG2 
7717  N N   . ASP A 1049 ? 0.2129 0.2194 0.2131 0.0197  -0.0066 -0.0090 1047 ASP A N   
7718  C CA  . ASP A 1049 ? 0.1966 0.2017 0.1974 0.0184  -0.0063 -0.0114 1047 ASP A CA  
7719  C C   . ASP A 1049 ? 0.2066 0.2128 0.2108 0.0179  -0.0070 -0.0124 1047 ASP A C   
7720  O O   . ASP A 1049 ? 0.1993 0.2076 0.2041 0.0187  -0.0084 -0.0123 1047 ASP A O   
7721  C CB  . ASP A 1049 ? 0.1951 0.2004 0.1931 0.0183  -0.0070 -0.0131 1047 ASP A CB  
7722  C CG  . ASP A 1049 ? 0.2265 0.2303 0.2257 0.0168  -0.0069 -0.0151 1047 ASP A CG  
7723  O OD1 . ASP A 1049 ? 0.2131 0.2180 0.2146 0.0162  -0.0077 -0.0162 1047 ASP A OD1 
7724  O OD2 . ASP A 1049 ? 0.2203 0.2222 0.2187 0.0160  -0.0059 -0.0153 1047 ASP A OD2 
7725  N N   . PRO A 1050 ? 0.1826 0.1880 0.1893 0.0167  -0.0060 -0.0133 1048 PRO A N   
7726  C CA  . PRO A 1050 ? 0.1960 0.2032 0.2063 0.0164  -0.0065 -0.0142 1048 PRO A CA  
7727  C C   . PRO A 1050 ? 0.1912 0.1996 0.2017 0.0157  -0.0076 -0.0158 1048 PRO A C   
7728  O O   . PRO A 1050 ? 0.1943 0.2046 0.2073 0.0159  -0.0086 -0.0163 1048 PRO A O   
7729  C CB  . PRO A 1050 ? 0.2191 0.2259 0.2316 0.0154  -0.0050 -0.0149 1048 PRO A CB  
7730  C CG  . PRO A 1050 ? 0.2219 0.2267 0.2315 0.0146  -0.0040 -0.0148 1048 PRO A CG  
7731  C CD  . PRO A 1050 ? 0.2000 0.2036 0.2064 0.0157  -0.0044 -0.0134 1048 PRO A CD  
7732  N N   . VAL A 1051 ? 0.1882 0.1954 0.1965 0.0150  -0.0077 -0.0166 1049 VAL A N   
7733  C CA  . VAL A 1051 ? 0.1878 0.1959 0.1967 0.0143  -0.0091 -0.0181 1049 VAL A CA  
7734  C C   . VAL A 1051 ? 0.1878 0.1973 0.1952 0.0158  -0.0108 -0.0183 1049 VAL A C   
7735  O O   . VAL A 1051 ? 0.2086 0.2199 0.2178 0.0157  -0.0122 -0.0192 1049 VAL A O   
7736  C CB  . VAL A 1051 ? 0.1963 0.2027 0.2044 0.0131  -0.0089 -0.0189 1049 VAL A CB  
7737  C CG1 . VAL A 1051 ? 0.2458 0.2529 0.2555 0.0123  -0.0106 -0.0205 1049 VAL A CG1 
7738  C CG2 . VAL A 1051 ? 0.2191 0.2248 0.2285 0.0116  -0.0072 -0.0184 1049 VAL A CG2 
7739  N N   . LEU A 1052 ? 0.1804 0.1897 0.1847 0.0171  -0.0108 -0.0173 1050 LEU A N   
7740  C CA  . LEU A 1052 ? 0.1869 0.1987 0.1898 0.0186  -0.0122 -0.0169 1050 LEU A CA  
7741  C C   . LEU A 1052 ? 0.2055 0.2190 0.2112 0.0191  -0.0129 -0.0159 1050 LEU A C   
7742  O O   . LEU A 1052 ? 0.1832 0.1990 0.1895 0.0195  -0.0145 -0.0166 1050 LEU A O   
7743  C CB  . LEU A 1052 ? 0.1890 0.2009 0.1884 0.0199  -0.0117 -0.0152 1050 LEU A CB  
7744  C CG  . LEU A 1052 ? 0.1841 0.1995 0.1815 0.0216  -0.0130 -0.0142 1050 LEU A CG  
7745  C CD1 . LEU A 1052 ? 0.1990 0.2160 0.1988 0.0222  -0.0134 -0.0115 1050 LEU A CD1 
7746  C CD2 . LEU A 1052 ? 0.1979 0.2153 0.1944 0.0219  -0.0149 -0.0168 1050 LEU A CD2 
7747  N N   . LEU A 1053 ? 0.1853 0.1980 0.1931 0.0190  -0.0117 -0.0143 1051 LEU A N   
7748  C CA  . LEU A 1053 ? 0.1867 0.2011 0.1980 0.0196  -0.0125 -0.0135 1051 LEU A CA  
7749  C C   . LEU A 1053 ? 0.1839 0.1994 0.1980 0.0187  -0.0131 -0.0154 1051 LEU A C   
7750  O O   . LEU A 1053 ? 0.1968 0.2144 0.2126 0.0193  -0.0146 -0.0153 1051 LEU A O   
7751  C CB  . LEU A 1053 ? 0.2198 0.2330 0.2337 0.0197  -0.0112 -0.0121 1051 LEU A CB  
7752  C CG  . LEU A 1053 ? 0.2074 0.2199 0.2196 0.0206  -0.0109 -0.0095 1051 LEU A CG  
7753  C CD1 . LEU A 1053 ? 0.2275 0.2383 0.2429 0.0205  -0.0097 -0.0088 1051 LEU A CD1 
7754  C CD2 . LEU A 1053 ? 0.2336 0.2486 0.2459 0.0220  -0.0125 -0.0073 1051 LEU A CD2 
7755  N N   . ASP A 1054 ? 0.1808 0.1952 0.1957 0.0172  -0.0122 -0.0169 1052 ASP A N   
7756  C CA  . ASP A 1054 ? 0.2048 0.2208 0.2226 0.0162  -0.0128 -0.0185 1052 ASP A CA  
7757  C C   . ASP A 1054 ? 0.1841 0.2012 0.2008 0.0163  -0.0147 -0.0196 1052 ASP A C   
7758  O O   . ASP A 1054 ? 0.1954 0.2145 0.2146 0.0163  -0.0159 -0.0202 1052 ASP A O   
7759  C CB  . ASP A 1054 ? 0.1885 0.2036 0.2071 0.0144  -0.0114 -0.0194 1052 ASP A CB  
7760  C CG  . ASP A 1054 ? 0.2452 0.2603 0.2657 0.0141  -0.0096 -0.0190 1052 ASP A CG  
7761  O OD1 . ASP A 1054 ? 0.2275 0.2432 0.2496 0.0154  -0.0097 -0.0184 1052 ASP A OD1 
7762  O OD2 . ASP A 1054 ? 0.2964 0.3112 0.3169 0.0128  -0.0084 -0.0194 1052 ASP A OD2 
7763  N N   . PHE A 1055 ? 0.1735 0.1894 0.1867 0.0166  -0.0151 -0.0199 1053 PHE A N   
7764  C CA  . PHE A 1055 ? 0.1874 0.2047 0.1996 0.0170  -0.0172 -0.0215 1053 PHE A CA  
7765  C C   . PHE A 1055 ? 0.1870 0.2070 0.1987 0.0186  -0.0186 -0.0206 1053 PHE A C   
7766  O O   . PHE A 1055 ? 0.1905 0.2126 0.2036 0.0187  -0.0203 -0.0218 1053 PHE A O   
7767  C CB  . PHE A 1055 ? 0.1895 0.2053 0.1982 0.0172  -0.0172 -0.0224 1053 PHE A CB  
7768  C CG  . PHE A 1055 ? 0.1948 0.2121 0.2027 0.0178  -0.0195 -0.0246 1053 PHE A CG  
7769  C CD1 . PHE A 1055 ? 0.2243 0.2418 0.2352 0.0167  -0.0209 -0.0265 1053 PHE A CD1 
7770  C CD2 . PHE A 1055 ? 0.2189 0.2377 0.2229 0.0195  -0.0202 -0.0249 1053 PHE A CD2 
7771  C CE1 . PHE A 1055 ? 0.2499 0.2688 0.2605 0.0172  -0.0232 -0.0289 1053 PHE A CE1 
7772  C CE2 . PHE A 1055 ? 0.2353 0.2560 0.2386 0.0202  -0.0224 -0.0275 1053 PHE A CE2 
7773  C CZ  . PHE A 1055 ? 0.2591 0.2796 0.2657 0.0191  -0.0240 -0.0297 1053 PHE A CZ  
7774  N N   . ALA A 1056 ? 0.1974 0.2177 0.2075 0.0198  -0.0179 -0.0184 1054 ALA A N   
7775  C CA  . ALA A 1056 ? 0.1925 0.2158 0.2026 0.0213  -0.0193 -0.0168 1054 ALA A CA  
7776  C C   . ALA A 1056 ? 0.2162 0.2407 0.2308 0.0211  -0.0201 -0.0168 1054 ALA A C   
7777  O O   . ALA A 1056 ? 0.2225 0.2497 0.2377 0.0217  -0.0219 -0.0170 1054 ALA A O   
7778  C CB  . ALA A 1056 ? 0.2163 0.2396 0.2251 0.0224  -0.0185 -0.0138 1054 ALA A CB  
7779  N N   . LYS A 1057 ? 0.2103 0.2333 0.2282 0.0202  -0.0187 -0.0168 1055 LYS A N   
7780  C CA  . LYS A 1057 ? 0.2345 0.2591 0.2569 0.0200  -0.0193 -0.0172 1055 LYS A CA  
7781  C C   . LYS A 1057 ? 0.2204 0.2462 0.2439 0.0190  -0.0204 -0.0194 1055 LYS A C   
7782  O O   . LYS A 1057 ? 0.2269 0.2550 0.2530 0.0194  -0.0219 -0.0197 1055 LYS A O   
7783  C CB  . LYS A 1057 ? 0.2563 0.2797 0.2820 0.0194  -0.0175 -0.0172 1055 LYS A CB  
7784  C CG  . LYS A 1057 ? 0.2587 0.2813 0.2853 0.0205  -0.0170 -0.0151 1055 LYS A CG  
7785  C CD  . LYS A 1057 ? 0.2483 0.2704 0.2789 0.0201  -0.0156 -0.0158 1055 LYS A CD  
7786  C CE  . LYS A 1057 ? 0.2555 0.2760 0.2844 0.0186  -0.0137 -0.0172 1055 LYS A CE  
7787  N NZ  . LYS A 1057 ? 0.2834 0.3038 0.3155 0.0186  -0.0123 -0.0178 1055 LYS A NZ  
7788  N N   . TRP A 1058 ? 0.2077 0.2320 0.2300 0.0178  -0.0199 -0.0210 1056 TRP A N   
7789  C CA  . TRP A 1058 ? 0.2433 0.2685 0.2671 0.0167  -0.0212 -0.0230 1056 TRP A CA  
7790  C C   . TRP A 1058 ? 0.2231 0.2502 0.2451 0.0178  -0.0236 -0.0237 1056 TRP A C   
7791  O O   . TRP A 1058 ? 0.2489 0.2781 0.2734 0.0177  -0.0252 -0.0247 1056 TRP A O   
7792  C CB  . TRP A 1058 ? 0.2468 0.2698 0.2697 0.0151  -0.0205 -0.0240 1056 TRP A CB  
7793  C CG  . TRP A 1058 ? 0.2564 0.2799 0.2814 0.0139  -0.0221 -0.0259 1056 TRP A CG  
7794  C CD1 . TRP A 1058 ? 0.2890 0.3137 0.3183 0.0123  -0.0221 -0.0263 1056 TRP A CD1 
7795  C CD2 . TRP A 1058 ? 0.2744 0.2978 0.2978 0.0143  -0.0241 -0.0277 1056 TRP A CD2 
7796  N NE1 . TRP A 1058 ? 0.2962 0.3210 0.3269 0.0114  -0.0240 -0.0279 1056 TRP A NE1 
7797  C CE2 . TRP A 1058 ? 0.2933 0.3172 0.3206 0.0127  -0.0254 -0.0291 1056 TRP A CE2 
7798  C CE3 . TRP A 1058 ? 0.2693 0.2925 0.2887 0.0158  -0.0250 -0.0284 1056 TRP A CE3 
7799  C CZ2 . TRP A 1058 ? 0.3003 0.3241 0.3278 0.0127  -0.0277 -0.0314 1056 TRP A CZ2 
7800  C CZ3 . TRP A 1058 ? 0.2971 0.3207 0.3164 0.0159  -0.0272 -0.0310 1056 TRP A CZ3 
7801  C CH2 . TRP A 1058 ? 0.3113 0.3349 0.3348 0.0144  -0.0286 -0.0325 1056 TRP A CH2 
7802  N N   . LEU A 1059 ? 0.2238 0.2509 0.2417 0.0191  -0.0239 -0.0232 1057 LEU A N   
7803  C CA  . LEU A 1059 ? 0.2289 0.2587 0.2447 0.0204  -0.0261 -0.0240 1057 LEU A CA  
7804  C C   . LEU A 1059 ? 0.2457 0.2784 0.2633 0.0213  -0.0273 -0.0226 1057 LEU A C   
7805  O O   . LEU A 1059 ? 0.2612 0.2965 0.2797 0.0217  -0.0294 -0.0238 1057 LEU A O   
7806  C CB  . LEU A 1059 ? 0.2206 0.2507 0.2315 0.0217  -0.0258 -0.0233 1057 LEU A CB  
7807  C CG  . LEU A 1059 ? 0.2182 0.2462 0.2270 0.0211  -0.0255 -0.0255 1057 LEU A CG  
7808  C CD1 . LEU A 1059 ? 0.2076 0.2360 0.2118 0.0225  -0.0247 -0.0243 1057 LEU A CD1 
7809  C CD2 . LEU A 1059 ? 0.2438 0.2733 0.2529 0.0212  -0.0279 -0.0288 1057 LEU A CD2 
7810  N N   . ASP A 1060 ? 0.2216 0.2542 0.2405 0.0219  -0.0262 -0.0199 1058 ASP A N   
7811  C CA  . ASP A 1060 ? 0.2683 0.3034 0.2899 0.0227  -0.0274 -0.0183 1058 ASP A CA  
7812  C C   . ASP A 1060 ? 0.2712 0.3069 0.2974 0.0218  -0.0280 -0.0200 1058 ASP A C   
7813  O O   . ASP A 1060 ? 0.3110 0.3495 0.3387 0.0223  -0.0299 -0.0201 1058 ASP A O   
7814  C CB  . ASP A 1060 ? 0.2635 0.2977 0.2866 0.0234  -0.0262 -0.0154 1058 ASP A CB  
7815  C CG  . ASP A 1060 ? 0.2882 0.3241 0.3082 0.0248  -0.0267 -0.0125 1058 ASP A CG  
7816  O OD1 . ASP A 1060 ? 0.3386 0.3779 0.3564 0.0257  -0.0286 -0.0124 1058 ASP A OD1 
7817  O OD2 . ASP A 1060 ? 0.3673 0.4016 0.3871 0.0251  -0.0254 -0.0103 1058 ASP A OD2 
7818  N N   . GLY A 1061 ? 0.2826 0.3163 0.3110 0.0203  -0.0264 -0.0212 1059 GLY A N   
7819  C CA  . GLY A 1061 ? 0.2659 0.3008 0.2987 0.0192  -0.0269 -0.0226 1059 GLY A CA  
7820  C C   . GLY A 1061 ? 0.3184 0.3547 0.3510 0.0187  -0.0289 -0.0247 1059 GLY A C   
7821  O O   . GLY A 1061 ? 0.3180 0.3565 0.3542 0.0184  -0.0302 -0.0254 1059 GLY A O   
7822  N N   . LYS A 1062 ? 0.3008 0.3359 0.3298 0.0186  -0.0294 -0.0258 1060 LYS A N   
7823  C CA  . LYS A 1062 ? 0.3038 0.3401 0.3327 0.0184  -0.0317 -0.0282 1060 LYS A CA  
7824  C C   . LYS A 1062 ? 0.3267 0.3663 0.3537 0.0201  -0.0339 -0.0282 1060 LYS A C   
7825  O O   . LYS A 1062 ? 0.3789 0.4203 0.4064 0.0201  -0.0361 -0.0304 1060 LYS A O   
7826  C CB  . LYS A 1062 ? 0.3423 0.3762 0.3686 0.0178  -0.0315 -0.0298 1060 LYS A CB  
7827  C CG  . LYS A 1062 ? 0.3094 0.3407 0.3383 0.0157  -0.0300 -0.0302 1060 LYS A CG  
7828  C CD  . LYS A 1062 ? 0.4117 0.4443 0.4458 0.0141  -0.0312 -0.0312 1060 LYS A CD  
7829  C CE  . LYS A 1062 ? 0.4544 0.4852 0.4912 0.0119  -0.0297 -0.0309 1060 LYS A CE  
7830  N NZ  . LYS A 1062 ? 0.5056 0.5381 0.5477 0.0102  -0.0308 -0.0315 1060 LYS A NZ  
7831  N N   . GLY A 1063 ? 0.2814 0.3223 0.3068 0.0216  -0.0336 -0.0256 1061 GLY A N   
7832  C CA  . GLY A 1063 ? 0.3209 0.3656 0.3441 0.0233  -0.0356 -0.0250 1061 GLY A CA  
7833  C C   . GLY A 1063 ? 0.3517 0.3975 0.3695 0.0245  -0.0359 -0.0253 1061 GLY A C   
7834  O O   . GLY A 1063 ? 0.3523 0.4022 0.3679 0.0259  -0.0377 -0.0249 1061 GLY A O   
7835  N N   . ALA A 1064 ? 0.2835 0.3263 0.2990 0.0239  -0.0343 -0.0260 1062 ALA A N   
7836  C CA  . ALA A 1064 ? 0.2787 0.3226 0.2891 0.0251  -0.0344 -0.0266 1062 ALA A CA  
7837  C C   . ALA A 1064 ? 0.2897 0.3345 0.2977 0.0262  -0.0330 -0.0227 1062 ALA A C   
7838  O O   . ALA A 1064 ? 0.2525 0.2948 0.2588 0.0260  -0.0311 -0.0217 1062 ALA A O   
7839  C CB  . ALA A 1064 ? 0.2727 0.3130 0.2825 0.0240  -0.0335 -0.0291 1062 ALA A CB  
7840  N N   . ARG A 1065 ? 0.2842 0.3328 0.2926 0.0273  -0.0342 -0.0202 1063 ARG A N   
7841  C CA  . ARG A 1065 ? 0.2232 0.2724 0.2312 0.0280  -0.0332 -0.0158 1063 ARG A CA  
7842  C C   . ARG A 1065 ? 0.2585 0.3094 0.2613 0.0290  -0.0325 -0.0147 1063 ARG A C   
7843  O O   . ARG A 1065 ? 0.2724 0.3212 0.2749 0.0289  -0.0306 -0.0122 1063 ARG A O   
7844  C CB  . ARG A 1065 ? 0.2842 0.3374 0.2943 0.0289  -0.0350 -0.0133 1063 ARG A CB  
7845  N N   . ALA A 1066 ? 0.2594 0.3146 0.2584 0.0301  -0.0340 -0.0166 1064 ALA A N   
7846  C CA  . ALA A 1066 ? 0.2378 0.2954 0.2319 0.0311  -0.0333 -0.0158 1064 ALA A CA  
7847  C C   . ALA A 1066 ? 0.2332 0.2859 0.2264 0.0303  -0.0312 -0.0177 1064 ALA A C   
7848  O O   . ALA A 1066 ? 0.2466 0.2991 0.2375 0.0306  -0.0296 -0.0154 1064 ALA A O   
7849  C CB  . ALA A 1066 ? 0.2561 0.3198 0.2465 0.0326  -0.0353 -0.0185 1064 ALA A CB  
7850  N N   . GLU A 1067 ? 0.2356 0.2846 0.2309 0.0291  -0.0313 -0.0215 1065 GLU A N   
7851  C CA  . GLU A 1067 ? 0.2249 0.2692 0.2196 0.0282  -0.0296 -0.0231 1065 GLU A CA  
7852  C C   . GLU A 1067 ? 0.2452 0.2854 0.2421 0.0271  -0.0273 -0.0200 1065 GLU A C   
7853  O O   . GLU A 1067 ? 0.2274 0.2654 0.2225 0.0270  -0.0255 -0.0193 1065 GLU A O   
7854  C CB  . GLU A 1067 ? 0.2364 0.2782 0.2336 0.0270  -0.0306 -0.0274 1065 GLU A CB  
7855  C CG  . GLU A 1067 ? 0.2332 0.2784 0.2282 0.0281  -0.0329 -0.0314 1065 GLU A CG  
7856  C CD  . GLU A 1067 ? 0.3080 0.3579 0.3036 0.0290  -0.0353 -0.0319 1065 GLU A CD  
7857  O OE1 . GLU A 1067 ? 0.2636 0.3135 0.2619 0.0285  -0.0353 -0.0294 1065 GLU A OE1 
7858  O OE2 . GLU A 1067 ? 0.3515 0.4054 0.3450 0.0302  -0.0373 -0.0351 1065 GLU A OE2 
7859  N N   . ALA A 1068 ? 0.2261 0.2654 0.2270 0.0265  -0.0273 -0.0183 1066 ALA A N   
7860  C CA  . ALA A 1068 ? 0.2192 0.2551 0.2225 0.0257  -0.0253 -0.0157 1066 ALA A CA  
7861  C C   . ALA A 1068 ? 0.2250 0.2624 0.2262 0.0268  -0.0245 -0.0119 1066 ALA A C   
7862  O O   . ALA A 1068 ? 0.2118 0.2462 0.2130 0.0263  -0.0227 -0.0106 1066 ALA A O   
7863  C CB  . ALA A 1068 ? 0.2410 0.2768 0.2492 0.0252  -0.0259 -0.0149 1066 ALA A CB  
7864  N N   . GLU A 1069 ? 0.2374 0.2797 0.2369 0.0281  -0.0260 -0.0100 1067 GLU A N   
7865  C CA  . GLU A 1069 ? 0.2274 0.2718 0.2250 0.0290  -0.0254 -0.0059 1067 GLU A CA  
7866  C C   . GLU A 1069 ? 0.2418 0.2863 0.2350 0.0293  -0.0241 -0.0070 1067 GLU A C   
7867  O O   . GLU A 1069 ? 0.2506 0.2939 0.2433 0.0293  -0.0226 -0.0043 1067 GLU A O   
7868  C CB  . GLU A 1069 ? 0.2586 0.3092 0.2553 0.0304  -0.0274 -0.0035 1067 GLU A CB  
7869  C CG  . GLU A 1069 ? 0.3145 0.3688 0.3091 0.0313  -0.0269 0.0011  1067 GLU A CG  
7870  C CD  . GLU A 1069 ? 0.4291 0.4808 0.4283 0.0308  -0.0262 0.0056  1067 GLU A CD  
7871  O OE1 . GLU A 1069 ? 0.4791 0.5268 0.4830 0.0300  -0.0262 0.0048  1067 GLU A OE1 
7872  O OE2 . GLU A 1069 ? 0.5589 0.6128 0.5572 0.0313  -0.0258 0.0098  1067 GLU A OE2 
7873  N N   . ALA A 1070 ? 0.2309 0.2769 0.2211 0.0297  -0.0249 -0.0109 1068 ALA A N   
7874  C CA  . ALA A 1070 ? 0.2224 0.2684 0.2088 0.0301  -0.0239 -0.0125 1068 ALA A CA  
7875  C C   . ALA A 1070 ? 0.2088 0.2484 0.1967 0.0287  -0.0219 -0.0131 1068 ALA A C   
7876  O O   . ALA A 1070 ? 0.2248 0.2637 0.2107 0.0288  -0.0204 -0.0122 1068 ALA A O   
7877  C CB  . ALA A 1070 ? 0.2412 0.2896 0.2253 0.0307  -0.0255 -0.0173 1068 ALA A CB  
7878  N N   . ALA A 1071 ? 0.2109 0.2466 0.2026 0.0273  -0.0218 -0.0146 1069 ALA A N   
7879  C CA  . ALA A 1071 ? 0.1848 0.2151 0.1781 0.0259  -0.0199 -0.0150 1069 ALA A CA  
7880  C C   . ALA A 1071 ? 0.1955 0.2245 0.1900 0.0258  -0.0183 -0.0111 1069 ALA A C   
7881  O O   . ALA A 1071 ? 0.1893 0.2160 0.1825 0.0255  -0.0167 -0.0106 1069 ALA A O   
7882  C CB  . ALA A 1071 ? 0.2014 0.2290 0.1987 0.0244  -0.0203 -0.0171 1069 ALA A CB  
7883  N N   . ARG A 1072 ? 0.2055 0.2359 0.2027 0.0261  -0.0190 -0.0084 1070 ARG A N   
7884  C CA  . ARG A 1072 ? 0.2063 0.2356 0.2053 0.0262  -0.0178 -0.0047 1070 ARG A CA  
7885  C C   . ARG A 1072 ? 0.2156 0.2470 0.2109 0.0271  -0.0172 -0.0023 1070 ARG A C   
7886  O O   . ARG A 1072 ? 0.2221 0.2512 0.2178 0.0267  -0.0157 -0.0006 1070 ARG A O   
7887  C CB  . ARG A 1072 ? 0.2305 0.2613 0.2334 0.0265  -0.0191 -0.0022 1070 ARG A CB  
7888  C CG  . ARG A 1072 ? 0.2553 0.2836 0.2626 0.0256  -0.0192 -0.0042 1070 ARG A CG  
7889  C CD  . ARG A 1072 ? 0.2743 0.3039 0.2863 0.0261  -0.0203 -0.0016 1070 ARG A CD  
7890  N NE  . ARG A 1072 ? 0.2893 0.3232 0.3002 0.0271  -0.0224 -0.0008 1070 ARG A NE  
7891  C CZ  . ARG A 1072 ? 0.3027 0.3378 0.3147 0.0269  -0.0237 -0.0031 1070 ARG A CZ  
7892  N NH1 . ARG A 1072 ? 0.3050 0.3374 0.3193 0.0258  -0.0231 -0.0063 1070 ARG A NH1 
7893  N NH2 . ARG A 1072 ? 0.3000 0.3396 0.3109 0.0279  -0.0256 -0.0023 1070 ARG A NH2 
7894  N N   . ASN A 1073 ? 0.2098 0.2463 0.2017 0.0282  -0.0184 -0.0021 1071 ASN A N   
7895  C CA  . ASN A 1073 ? 0.2207 0.2605 0.2090 0.0292  -0.0178 0.0001  1071 ASN A CA  
7896  C C   . ASN A 1073 ? 0.2218 0.2588 0.2075 0.0288  -0.0162 -0.0023 1071 ASN A C   
7897  O O   . ASN A 1073 ? 0.2230 0.2598 0.2077 0.0289  -0.0149 0.0000  1071 ASN A O   
7898  C CB  . ASN A 1073 ? 0.2240 0.2706 0.2088 0.0306  -0.0194 0.0001  1071 ASN A CB  
7899  C CG  . ASN A 1073 ? 0.3125 0.3627 0.2996 0.0311  -0.0209 0.0041  1071 ASN A CG  
7900  O OD1 . ASN A 1073 ? 0.3523 0.4003 0.3436 0.0305  -0.0207 0.0075  1071 ASN A OD1 
7901  N ND2 . ASN A 1073 ? 0.3465 0.4027 0.3313 0.0322  -0.0227 0.0035  1071 ASN A ND2 
7902  N N   . ALA A 1074 ? 0.2066 0.2415 0.1917 0.0283  -0.0165 -0.0069 1072 ALA A N   
7903  C CA  . ALA A 1074 ? 0.2093 0.2410 0.1927 0.0279  -0.0151 -0.0092 1072 ALA A CA  
7904  C C   . ALA A 1074 ? 0.2010 0.2277 0.1870 0.0266  -0.0134 -0.0077 1072 ALA A C   
7905  O O   . ALA A 1074 ? 0.1991 0.2243 0.1836 0.0265  -0.0119 -0.0071 1072 ALA A O   
7906  C CB  . ALA A 1074 ? 0.2514 0.2816 0.2350 0.0274  -0.0161 -0.0140 1072 ALA A CB  
7907  N N   . GLY A 1075 ? 0.1951 0.2193 0.1851 0.0256  -0.0135 -0.0071 1073 GLY A N   
7908  C CA  . GLY A 1075 ? 0.1971 0.2172 0.1898 0.0246  -0.0119 -0.0060 1073 GLY A CA  
7909  C C   . GLY A 1075 ? 0.2011 0.2218 0.1936 0.0251  -0.0110 -0.0021 1073 GLY A C   
7910  O O   . GLY A 1075 ? 0.2143 0.2322 0.2069 0.0245  -0.0095 -0.0018 1073 GLY A O   
7911  N N   . SER A 1076 ? 0.2173 0.2419 0.2099 0.0261  -0.0120 0.0010  1074 SER A N   
7912  C CA  . SER A 1076 ? 0.2043 0.2301 0.1974 0.0265  -0.0114 0.0053  1074 SER A CA  
7913  C C   . SER A 1076 ? 0.2344 0.2626 0.2229 0.0272  -0.0106 0.0056  1074 SER A C   
7914  O O   . SER A 1076 ? 0.2483 0.2753 0.2370 0.0270  -0.0093 0.0077  1074 SER A O   
7915  C CB  . SER A 1076 ? 0.2574 0.2874 0.2523 0.0273  -0.0130 0.0090  1074 SER A CB  
7916  O OG  . SER A 1076 ? 0.3459 0.3735 0.3459 0.0269  -0.0137 0.0093  1074 SER A OG  
7917  N N   . SER A 1077 ? 0.2195 0.2514 0.2042 0.0280  -0.0113 0.0034  1075 SER A N   
7918  C CA  A SER A 1077 ? 0.2334 0.2686 0.2137 0.0290  -0.0107 0.0033  1075 SER A CA  
7919  C CA  B SER A 1077 ? 0.2335 0.2688 0.2138 0.0290  -0.0107 0.0032  1075 SER A CA  
7920  C C   . SER A 1077 ? 0.2146 0.2456 0.1939 0.0283  -0.0092 0.0005  1075 SER A C   
7921  O O   . SER A 1077 ? 0.2377 0.2702 0.2145 0.0288  -0.0081 0.0013  1075 SER A O   
7922  C CB  A SER A 1077 ? 0.2375 0.2782 0.2143 0.0303  -0.0121 0.0009  1075 SER A CB  
7923  C CB  B SER A 1077 ? 0.2372 0.2777 0.2140 0.0302  -0.0122 0.0007  1075 SER A CB  
7924  O OG  A SER A 1077 ? 0.2937 0.3398 0.2707 0.0311  -0.0133 0.0044  1075 SER A OG  
7925  O OG  B SER A 1077 ? 0.2782 0.3221 0.2509 0.0313  -0.0116 -0.0006 1075 SER A OG  
7926  N N   . SER A 1078 ? 0.2016 0.2277 0.1828 0.0272  -0.0091 -0.0025 1076 SER A N   
7927  C CA  . SER A 1078 ? 0.2114 0.2335 0.1920 0.0264  -0.0078 -0.0048 1076 SER A CA  
7928  C C   . SER A 1078 ? 0.2023 0.2224 0.1838 0.0260  -0.0062 -0.0018 1076 SER A C   
7929  O O   . SER A 1078 ? 0.2091 0.2282 0.1936 0.0255  -0.0060 0.0011  1076 SER A O   
7930  C CB  . SER A 1078 ? 0.1897 0.2074 0.1731 0.0250  -0.0080 -0.0075 1076 SER A CB  
7931  O OG  . SER A 1078 ? 0.1857 0.1996 0.1691 0.0241  -0.0068 -0.0090 1076 SER A OG  
7932  N N   . ALA A 1079 ? 0.1845 0.2040 0.1637 0.0261  -0.0051 -0.0027 1077 ALA A N   
7933  C CA  . ALA A 1079 ? 0.1863 0.2035 0.1664 0.0256  -0.0036 -0.0003 1077 ALA A CA  
7934  C C   . ALA A 1079 ? 0.1836 0.1954 0.1653 0.0241  -0.0027 -0.0025 1077 ALA A C   
7935  O O   . ALA A 1079 ? 0.1858 0.1955 0.1679 0.0237  -0.0014 -0.0012 1077 ALA A O   
7936  C CB  . ALA A 1079 ? 0.1990 0.2197 0.1759 0.0267  -0.0028 0.0008  1077 ALA A CB  
7937  N N   . LEU A 1080 ? 0.1818 0.1916 0.1645 0.0234  -0.0034 -0.0054 1078 LEU A N   
7938  C CA  . LEU A 1080 ? 0.1840 0.1894 0.1686 0.0219  -0.0026 -0.0068 1078 LEU A CA  
7939  C C   . LEU A 1080 ? 0.1783 0.1819 0.1657 0.0212  -0.0017 -0.0044 1078 LEU A C   
7940  O O   . LEU A 1080 ? 0.1906 0.1950 0.1802 0.0214  -0.0022 -0.0027 1078 LEU A O   
7941  C CB  . LEU A 1080 ? 0.1768 0.1814 0.1632 0.0211  -0.0037 -0.0092 1078 LEU A CB  
7942  C CG  . LEU A 1080 ? 0.1918 0.1930 0.1805 0.0195  -0.0030 -0.0103 1078 LEU A CG  
7943  C CD1 . LEU A 1080 ? 0.2284 0.2276 0.2158 0.0189  -0.0025 -0.0119 1078 LEU A CD1 
7944  C CD2 . LEU A 1080 ? 0.2002 0.2016 0.1912 0.0187  -0.0040 -0.0118 1078 LEU A CD2 
7945  N N   . GLY A 1081 ? 0.1752 0.1761 0.1627 0.0205  -0.0004 -0.0044 1079 GLY A N   
7946  C CA  . GLY A 1081 ? 0.1893 0.1884 0.1796 0.0199  0.0004  -0.0026 1079 GLY A CA  
7947  C C   . GLY A 1081 ? 0.1980 0.1980 0.1880 0.0205  0.0010  0.0004  1079 GLY A C   
7948  O O   . GLY A 1081 ? 0.2079 0.2063 0.2006 0.0201  0.0016  0.0017  1079 GLY A O   
7949  N N   . LEU A 1082 ? 0.1933 0.1963 0.1804 0.0216  0.0008  0.0014  1080 LEU A N   
7950  C CA  A LEU A 1082 ? 0.1824 0.1867 0.1690 0.0222  0.0016  0.0044  1080 LEU A CA  
7951  C CA  B LEU A 1082 ? 0.1824 0.1867 0.1690 0.0222  0.0016  0.0044  1080 LEU A CA  
7952  C C   . LEU A 1082 ? 0.2006 0.2015 0.1875 0.0213  0.0029  0.0038  1080 LEU A C   
7953  O O   . LEU A 1082 ? 0.2029 0.2020 0.1884 0.0208  0.0032  0.0010  1080 LEU A O   
7954  C CB  A LEU A 1082 ? 0.1869 0.1952 0.1695 0.0234  0.0015  0.0044  1080 LEU A CB  
7955  C CB  B LEU A 1082 ? 0.1868 0.1952 0.1695 0.0234  0.0015  0.0044  1080 LEU A CB  
7956  C CG  A LEU A 1082 ? 0.1930 0.2037 0.1747 0.0240  0.0024  0.0075  1080 LEU A CG  
7957  C CG  B LEU A 1082 ? 0.1932 0.2042 0.1747 0.0241  0.0023  0.0074  1080 LEU A CG  
7958  C CD1 A LEU A 1082 ? 0.1900 0.2020 0.1749 0.0240  0.0020  0.0119  1080 LEU A CD1 
7959  C CD1 B LEU A 1082 ? 0.1798 0.1968 0.1583 0.0256  0.0017  0.0083  1080 LEU A CD1 
7960  C CD2 A LEU A 1082 ? 0.1966 0.2122 0.1742 0.0255  0.0022  0.0069  1080 LEU A CD2 
7961  C CD2 B LEU A 1082 ? 0.1924 0.2013 0.1722 0.0238  0.0035  0.0058  1080 LEU A CD2 
7962  N N   . ASP A 1083 ? 0.2050 0.2051 0.1942 0.0210  0.0034  0.0064  1081 ASP A N   
7963  C CA  . ASP A 1083 ? 0.2231 0.2202 0.2131 0.0202  0.0045  0.0059  1081 ASP A CA  
7964  C C   . ASP A 1083 ? 0.2266 0.2247 0.2178 0.0205  0.0050  0.0094  1081 ASP A C   
7965  O O   . ASP A 1083 ? 0.2710 0.2688 0.2661 0.0203  0.0045  0.0116  1081 ASP A O   
7966  C CB  . ASP A 1083 ? 0.2542 0.2484 0.2475 0.0191  0.0044  0.0044  1081 ASP A CB  
7967  C CG  . ASP A 1083 ? 0.3294 0.3209 0.3234 0.0182  0.0054  0.0036  1081 ASP A CG  
7968  O OD1 . ASP A 1083 ? 0.3790 0.3703 0.3706 0.0182  0.0062  0.0038  1081 ASP A OD1 
7969  O OD2 . ASP A 1083 ? 0.4247 0.4148 0.4217 0.0175  0.0054  0.0025  1081 ASP A OD2 
7970  N N   . LEU A 1084 ? 0.2262 0.2255 0.2146 0.0209  0.0058  0.0099  1082 LEU A N   
7971  C CA  . LEU A 1084 ? 0.2294 0.2308 0.2186 0.0213  0.0063  0.0137  1082 LEU A CA  
7972  C C   . LEU A 1084 ? 0.2441 0.2434 0.2330 0.0208  0.0074  0.0133  1082 LEU A C   
7973  O O   . LEU A 1084 ? 0.2454 0.2429 0.2320 0.0205  0.0079  0.0103  1082 LEU A O   
7974  C CB  . LEU A 1084 ? 0.2509 0.2575 0.2367 0.0226  0.0062  0.0150  1082 LEU A CB  
7975  C CG  . LEU A 1084 ? 0.2837 0.2936 0.2691 0.0233  0.0050  0.0158  1082 LEU A CG  
7976  C CD1 . LEU A 1084 ? 0.2897 0.3053 0.2710 0.0247  0.0052  0.0161  1082 LEU A CD1 
7977  C CD2 . LEU A 1084 ? 0.2655 0.2761 0.2554 0.0231  0.0043  0.0199  1082 LEU A CD2 
7978  N N   . GLU A 1085 ? 0.2305 0.2299 0.2220 0.0206  0.0077  0.0165  1083 GLU A N   
7979  C CA  . GLU A 1085 ? 0.2262 0.2247 0.2173 0.0203  0.0088  0.0169  1083 GLU A CA  
7980  C C   . GLU A 1085 ? 0.2293 0.2325 0.2184 0.0213  0.0093  0.0198  1083 GLU A C   
7981  O O   . GLU A 1085 ? 0.2586 0.2649 0.2495 0.0216  0.0088  0.0235  1083 GLU A O   
7982  C CB  . GLU A 1085 ? 0.2312 0.2268 0.2269 0.0193  0.0088  0.0182  1083 GLU A CB  
7983  C CG  . GLU A 1085 ? 0.2603 0.2553 0.2554 0.0191  0.0099  0.0189  1083 GLU A CG  
7984  C CD  . GLU A 1085 ? 0.3286 0.3204 0.3280 0.0181  0.0098  0.0191  1083 GLU A CD  
7985  O OE1 . GLU A 1085 ? 0.3626 0.3523 0.3652 0.0176  0.0089  0.0180  1083 GLU A OE1 
7986  O OE2 . GLU A 1085 ? 0.3518 0.3434 0.3513 0.0178  0.0105  0.0203  1083 GLU A OE2 
7987  N N   . LEU A 1086 ? 0.2396 0.2437 0.2253 0.0217  0.0102  0.0182  1084 LEU A N   
7988  C CA  . LEU A 1086 ? 0.2265 0.2360 0.2100 0.0229  0.0109  0.0203  1084 LEU A CA  
7989  C C   . LEU A 1086 ? 0.2462 0.2556 0.2315 0.0224  0.0118  0.0231  1084 LEU A C   
7990  O O   . LEU A 1086 ? 0.2440 0.2492 0.2304 0.0216  0.0122  0.0216  1084 LEU A O   
7991  C CB  . LEU A 1086 ? 0.2289 0.2399 0.2080 0.0239  0.0112  0.0165  1084 LEU A CB  
7992  C CG  . LEU A 1086 ? 0.2489 0.2599 0.2263 0.0243  0.0101  0.0135  1084 LEU A CG  
7993  C CD1 . LEU A 1086 ? 0.2689 0.2812 0.2428 0.0254  0.0102  0.0096  1084 LEU A CD1 
7994  C CD2 . LEU A 1086 ? 0.2831 0.2985 0.2606 0.0250  0.0093  0.0161  1084 LEU A CD2 
7995  N N   . PRO A 1087 ? 0.2448 0.2592 0.2307 0.0229  0.0120  0.0273  1085 PRO A N   
7996  C CA  . PRO A 1087 ? 0.2862 0.3011 0.2743 0.0225  0.0129  0.0303  1085 PRO A CA  
7997  C C   . PRO A 1087 ? 0.2347 0.2493 0.2198 0.0229  0.0140  0.0275  1085 PRO A C   
7998  O O   . PRO A 1087 ? 0.2788 0.2961 0.2599 0.0241  0.0144  0.0248  1085 PRO A O   
7999  C CB  . PRO A 1087 ? 0.3085 0.3304 0.2968 0.0232  0.0129  0.0352  1085 PRO A CB  
8000  C CG  . PRO A 1087 ? 0.3192 0.3428 0.3071 0.0236  0.0117  0.0355  1085 PRO A CG  
8001  C CD  . PRO A 1087 ? 0.2434 0.2636 0.2284 0.0238  0.0114  0.0299  1085 PRO A CD  
8002  N N   . GLY A 1088 ? 0.2474 0.2586 0.2349 0.0220  0.0145  0.0279  1086 GLY A N   
8003  C CA  . GLY A 1088 ? 0.2751 0.2857 0.2605 0.0223  0.0155  0.0257  1086 GLY A CA  
8004  C C   . GLY A 1088 ? 0.2221 0.2303 0.2108 0.0212  0.0160  0.0276  1086 GLY A C   
8005  O O   . GLY A 1088 ? 0.2159 0.2242 0.2086 0.0205  0.0156  0.0313  1086 GLY A O   
8006  N N   . PRO A 1089 ? 0.2521 0.2579 0.2396 0.0211  0.0166  0.0251  1087 PRO A N   
8007  C CA  . PRO A 1089 ? 0.2334 0.2373 0.2240 0.0202  0.0170  0.0267  1087 PRO A CA  
8008  C C   . PRO A 1089 ? 0.2392 0.2378 0.2333 0.0188  0.0161  0.0263  1087 PRO A C   
8009  O O   . PRO A 1089 ? 0.2346 0.2305 0.2283 0.0184  0.0154  0.0237  1087 PRO A O   
8010  C CB  . PRO A 1089 ? 0.2739 0.2766 0.2618 0.0206  0.0178  0.0235  1087 PRO A CB  
8011  C CG  . PRO A 1089 ? 0.2759 0.2768 0.2610 0.0209  0.0172  0.0195  1087 PRO A CG  
8012  C CD  . PRO A 1089 ? 0.2430 0.2478 0.2270 0.0218  0.0168  0.0207  1087 PRO A CD  
8013  N N   . VAL A 1090 ? 0.2262 0.2238 0.2242 0.0179  0.0161  0.0286  1088 VAL A N   
8014  C CA  . VAL A 1090 ? 0.2060 0.1990 0.2076 0.0167  0.0153  0.0275  1088 VAL A CA  
8015  C C   . VAL A 1090 ? 0.2154 0.2050 0.2145 0.0163  0.0155  0.0233  1088 VAL A C   
8016  O O   . VAL A 1090 ? 0.2156 0.2058 0.2114 0.0168  0.0163  0.0218  1088 VAL A O   
8017  C CB  . VAL A 1090 ? 0.2243 0.2169 0.2307 0.0159  0.0151  0.0305  1088 VAL A CB  
8018  C CG1 . VAL A 1090 ? 0.2500 0.2461 0.2596 0.0161  0.0146  0.0353  1088 VAL A CG1 
8019  C CG2 . VAL A 1090 ? 0.2292 0.2225 0.2343 0.0160  0.0162  0.0306  1088 VAL A CG2 
8020  N N   . GLY A 1091 ? 0.2192 0.2055 0.2204 0.0154  0.0147  0.0214  1089 GLY A N   
8021  C CA  . GLY A 1091 ? 0.2229 0.2065 0.2223 0.0148  0.0149  0.0180  1089 GLY A CA  
8022  C C   . GLY A 1091 ? 0.2199 0.2035 0.2155 0.0152  0.0150  0.0154  1089 GLY A C   
8023  O O   . GLY A 1091 ? 0.1949 0.1770 0.1887 0.0148  0.0151  0.0131  1089 GLY A O   
8024  N N   . GLU A 1092 ? 0.2016 0.1871 0.1962 0.0159  0.0147  0.0159  1090 GLU A N   
8025  C CA  . GLU A 1092 ? 0.2197 0.2052 0.2111 0.0163  0.0145  0.0135  1090 GLU A CA  
8026  C C   . GLU A 1092 ? 0.2131 0.1996 0.2054 0.0166  0.0138  0.0140  1090 GLU A C   
8027  O O   . GLU A 1092 ? 0.2311 0.2194 0.2254 0.0170  0.0135  0.0169  1090 GLU A O   
8028  C CB  . GLU A 1092 ? 0.2692 0.2573 0.2574 0.0175  0.0151  0.0134  1090 GLU A CB  
8029  C CG  . GLU A 1092 ? 0.3188 0.3060 0.3043 0.0177  0.0149  0.0102  1090 GLU A CG  
8030  C CD  . GLU A 1092 ? 0.3166 0.3062 0.2997 0.0190  0.0154  0.0097  1090 GLU A CD  
8031  O OE1 . GLU A 1092 ? 0.2596 0.2529 0.2414 0.0203  0.0155  0.0105  1090 GLU A OE1 
8032  O OE2 . GLU A 1092 ? 0.3329 0.3213 0.3158 0.0189  0.0157  0.0087  1090 GLU A OE2 
8033  N N   . ARG A 1093 ? 0.2021 0.1874 0.1932 0.0164  0.0133  0.0115  1091 ARG A N   
8034  C CA  . ARG A 1093 ? 0.2111 0.1976 0.2026 0.0168  0.0125  0.0117  1091 ARG A CA  
8035  C C   . ARG A 1093 ? 0.2008 0.1885 0.1887 0.0175  0.0124  0.0098  1091 ARG A C   
8036  O O   . ARG A 1093 ? 0.2110 0.1969 0.1975 0.0170  0.0125  0.0073  1091 ARG A O   
8037  C CB  . ARG A 1093 ? 0.2756 0.2599 0.2697 0.0159  0.0118  0.0102  1091 ARG A CB  
8038  C CG  . ARG A 1093 ? 0.3604 0.3442 0.3590 0.0156  0.0114  0.0121  1091 ARG A CG  
8039  C CD  . ARG A 1093 ? 0.5090 0.4920 0.5104 0.0153  0.0104  0.0106  1091 ARG A CD  
8040  N NE  . ARG A 1093 ? 0.6303 0.6120 0.6305 0.0146  0.0106  0.0073  1091 ARG A NE  
8041  C CZ  . ARG A 1093 ? 0.5867 0.5671 0.5884 0.0138  0.0107  0.0059  1091 ARG A CZ  
8042  N NH1 . ARG A 1093 ? 0.5540 0.5338 0.5589 0.0137  0.0106  0.0071  1091 ARG A NH1 
8043  N NH2 . ARG A 1093 ? 0.5731 0.5533 0.5735 0.0130  0.0109  0.0033  1091 ARG A NH2 
8044  N N   . ASN A 1094 ? 0.1990 0.1899 0.1857 0.0186  0.0123  0.0111  1092 ASN A N   
8045  C CA  . ASN A 1094 ? 0.1883 0.1810 0.1717 0.0195  0.0121  0.0092  1092 ASN A CA  
8046  C C   . ASN A 1094 ? 0.1980 0.1918 0.1815 0.0198  0.0111  0.0090  1092 ASN A C   
8047  O O   . ASN A 1094 ? 0.2138 0.2101 0.1984 0.0203  0.0109  0.0117  1092 ASN A O   
8048  C CB  . ASN A 1094 ? 0.1999 0.1964 0.1813 0.0208  0.0127  0.0104  1092 ASN A CB  
8049  C CG  . ASN A 1094 ? 0.1994 0.1945 0.1804 0.0206  0.0135  0.0097  1092 ASN A CG  
8050  O OD1 . ASN A 1094 ? 0.2115 0.2047 0.1914 0.0205  0.0133  0.0068  1092 ASN A OD1 
8051  N ND2 . ASN A 1094 ? 0.2174 0.2134 0.1998 0.0205  0.0143  0.0124  1092 ASN A ND2 
8052  N N   . LEU A 1095 ? 0.1903 0.1824 0.1733 0.0194  0.0105  0.0062  1093 LEU A N   
8053  C CA  . LEU A 1095 ? 0.1986 0.1911 0.1823 0.0194  0.0096  0.0057  1093 LEU A CA  
8054  C C   . LEU A 1095 ? 0.2017 0.1961 0.1826 0.0203  0.0090  0.0036  1093 LEU A C   
8055  O O   . LEU A 1095 ? 0.2120 0.2059 0.1913 0.0205  0.0090  0.0014  1093 LEU A O   
8056  C CB  . LEU A 1095 ? 0.2165 0.2057 0.2021 0.0180  0.0093  0.0040  1093 LEU A CB  
8057  C CG  . LEU A 1095 ? 0.2437 0.2311 0.2322 0.0172  0.0099  0.0053  1093 LEU A CG  
8058  C CD1 . LEU A 1095 ? 0.3032 0.2885 0.2934 0.0160  0.0096  0.0033  1093 LEU A CD1 
8059  C CD2 . LEU A 1095 ? 0.2871 0.2758 0.2781 0.0176  0.0096  0.0083  1093 LEU A CD2 
8060  N N   . TYR A 1096 ? 0.2070 0.2037 0.1879 0.0209  0.0082  0.0041  1094 TYR A N   
8061  C CA  . TYR A 1096 ? 0.1849 0.1841 0.1634 0.0219  0.0074  0.0021  1094 TYR A CA  
8062  C C   . TYR A 1096 ? 0.1802 0.1790 0.1601 0.0215  0.0063  0.0016  1094 TYR A C   
8063  O O   . TYR A 1096 ? 0.2052 0.2048 0.1869 0.0215  0.0061  0.0040  1094 TYR A O   
8064  C CB  . TYR A 1096 ? 0.2029 0.2072 0.1795 0.0234  0.0075  0.0041  1094 TYR A CB  
8065  C CG  . TYR A 1096 ? 0.2086 0.2165 0.1827 0.0247  0.0065  0.0021  1094 TYR A CG  
8066  C CD1 . TYR A 1096 ? 0.2053 0.2142 0.1772 0.0256  0.0063  -0.0012 1094 TYR A CD1 
8067  C CD2 . TYR A 1096 ? 0.2184 0.2291 0.1927 0.0251  0.0057  0.0035  1094 TYR A CD2 
8068  C CE1 . TYR A 1096 ? 0.2101 0.2228 0.1800 0.0269  0.0052  -0.0035 1094 TYR A CE1 
8069  C CE2 . TYR A 1096 ? 0.2193 0.2338 0.1912 0.0264  0.0047  0.0016  1094 TYR A CE2 
8070  C CZ  . TYR A 1096 ? 0.2066 0.2221 0.1763 0.0273  0.0044  -0.0020 1094 TYR A CZ  
8071  O OH  . TYR A 1096 ? 0.2119 0.2316 0.1796 0.0286  0.0033  -0.0044 1094 TYR A OH  
8072  N N   . THR A 1097 ? 0.1956 0.1930 0.1751 0.0211  0.0056  -0.0015 1095 THR A N   
8073  C CA  . THR A 1097 ? 0.1963 0.1930 0.1775 0.0206  0.0047  -0.0022 1095 THR A CA  
8074  C C   . THR A 1097 ? 0.2255 0.2237 0.2051 0.0212  0.0035  -0.0049 1095 THR A C   
8075  O O   . THR A 1097 ? 0.2134 0.2116 0.1915 0.0216  0.0033  -0.0070 1095 THR A O   
8076  C CB  . THR A 1097 ? 0.2367 0.2297 0.2201 0.0189  0.0050  -0.0031 1095 THR A CB  
8077  O OG1 . THR A 1097 ? 0.2859 0.2772 0.2685 0.0184  0.0051  -0.0052 1095 THR A OG1 
8078  C CG2 . THR A 1097 ? 0.2619 0.2537 0.2472 0.0184  0.0060  -0.0010 1095 THR A CG2 
8079  N N   . LEU A 1098 ? 0.1929 0.1923 0.1732 0.0213  0.0025  -0.0049 1096 LEU A N   
8080  C CA  . LEU A 1098 ? 0.2020 0.2028 0.1815 0.0218  0.0012  -0.0076 1096 LEU A CA  
8081  C C   . LEU A 1098 ? 0.1736 0.1718 0.1556 0.0204  0.0006  -0.0090 1096 LEU A C   
8082  O O   . LEU A 1098 ? 0.1788 0.1766 0.1627 0.0198  0.0007  -0.0078 1096 LEU A O   
8083  C CB  . LEU A 1098 ? 0.1978 0.2030 0.1761 0.0231  0.0003  -0.0065 1096 LEU A CB  
8084  C CG  . LEU A 1098 ? 0.1820 0.1911 0.1576 0.0246  0.0009  -0.0050 1096 LEU A CG  
8085  C CD1 . LEU A 1098 ? 0.2040 0.2182 0.1784 0.0259  -0.0001 -0.0037 1096 LEU A CD1 
8086  C CD2 . LEU A 1098 ? 0.2039 0.2134 0.1774 0.0253  0.0009  -0.0078 1096 LEU A CD2 
8087  N N   . HIS A 1099 ? 0.1869 0.1836 0.1690 0.0198  0.0000  -0.0117 1097 HIS A N   
8088  C CA  . HIS A 1099 ? 0.1860 0.1808 0.1706 0.0184  -0.0006 -0.0129 1097 HIS A CA  
8089  C C   . HIS A 1099 ? 0.1965 0.1925 0.1811 0.0188  -0.0023 -0.0154 1097 HIS A C   
8090  O O   . HIS A 1099 ? 0.2013 0.1996 0.1839 0.0203  -0.0031 -0.0167 1097 HIS A O   
8091  C CB  . HIS A 1099 ? 0.2133 0.2050 0.1988 0.0170  0.0000  -0.0134 1097 HIS A CB  
8092  C CG  . HIS A 1099 ? 0.2324 0.2229 0.2180 0.0166  0.0016  -0.0114 1097 HIS A CG  
8093  N ND1 . HIS A 1099 ? 0.3028 0.2921 0.2904 0.0151  0.0024  -0.0105 1097 HIS A ND1 
8094  C CD2 . HIS A 1099 ? 0.2517 0.2424 0.2356 0.0174  0.0026  -0.0101 1097 HIS A CD2 
8095  C CE1 . HIS A 1099 ? 0.3049 0.2934 0.2921 0.0151  0.0036  -0.0090 1097 HIS A CE1 
8096  N NE2 . HIS A 1099 ? 0.2764 0.2655 0.2616 0.0164  0.0038  -0.0086 1097 HIS A NE2 
8097  N N   . ALA A 1100 ? 0.1973 0.1921 0.1844 0.0175  -0.0030 -0.0164 1098 ALA A N   
8098  C CA  . ALA A 1100 ? 0.2064 0.2018 0.1944 0.0176  -0.0048 -0.0189 1098 ALA A CA  
8099  C C   . ALA A 1100 ? 0.2278 0.2218 0.2158 0.0177  -0.0055 -0.0209 1098 ALA A C   
8100  O O   . ALA A 1100 ? 0.2322 0.2240 0.2204 0.0170  -0.0045 -0.0201 1098 ALA A O   
8101  C CB  . ALA A 1100 ? 0.2114 0.2058 0.2026 0.0158  -0.0053 -0.0191 1098 ALA A CB  
8102  N N   . ARG A 1101 ? 0.2145 0.2098 0.2025 0.0187  -0.0073 -0.0237 1099 ARG A N   
8103  C CA  A ARG A 1101 ? 0.2272 0.2210 0.2162 0.0189  -0.0084 -0.0262 1099 ARG A CA  
8104  C CA  B ARG A 1101 ? 0.2271 0.2210 0.2161 0.0189  -0.0084 -0.0262 1099 ARG A CA  
8105  C C   . ARG A 1101 ? 0.2213 0.2120 0.2145 0.0168  -0.0092 -0.0264 1099 ARG A C   
8106  O O   . ARG A 1101 ? 0.2473 0.2357 0.2422 0.0161  -0.0093 -0.0266 1099 ARG A O   
8107  C CB  A ARG A 1101 ? 0.2603 0.2570 0.2484 0.0209  -0.0102 -0.0295 1099 ARG A CB  
8108  C CB  B ARG A 1101 ? 0.2604 0.2571 0.2485 0.0209  -0.0103 -0.0295 1099 ARG A CB  
8109  C CG  A ARG A 1101 ? 0.2608 0.2614 0.2447 0.0231  -0.0095 -0.0293 1099 ARG A CG  
8110  C CG  B ARG A 1101 ? 0.2622 0.2626 0.2461 0.0231  -0.0095 -0.0294 1099 ARG A CG  
8111  C CD  A ARG A 1101 ? 0.2167 0.2208 0.1997 0.0251  -0.0114 -0.0332 1099 ARG A CD  
8112  C CD  B ARG A 1101 ? 0.2558 0.2568 0.2395 0.0245  -0.0104 -0.0328 1099 ARG A CD  
8113  N NE  A ARG A 1101 ? 0.2209 0.2240 0.2048 0.0258  -0.0121 -0.0361 1099 ARG A NE  
8114  N NE  B ARG A 1101 ? 0.2511 0.2561 0.2310 0.0265  -0.0094 -0.0325 1099 ARG A NE  
8115  C CZ  A ARG A 1101 ? 0.2636 0.2686 0.2449 0.0273  -0.0111 -0.0363 1099 ARG A CZ  
8116  C CZ  B ARG A 1101 ? 0.2624 0.2698 0.2414 0.0284  -0.0102 -0.0357 1099 ARG A CZ  
8117  N NH1 A ARG A 1101 ? 0.2648 0.2730 0.2425 0.0281  -0.0092 -0.0334 1099 ARG A NH1 
8118  N NH1 B ARG A 1101 ? 0.2476 0.2534 0.2295 0.0286  -0.0123 -0.0398 1099 ARG A NH1 
8119  N NH2 A ARG A 1101 ? 0.2686 0.2725 0.2516 0.0280  -0.0119 -0.0393 1099 ARG A NH2 
8120  N NH2 B ARG A 1101 ? 0.2587 0.2705 0.2340 0.0301  -0.0089 -0.0349 1099 ARG A NH2 
8121  N N   . GLY A 1102 ? 0.2191 0.2102 0.2145 0.0157  -0.0099 -0.0262 1100 GLY A N   
8122  C CA  . GLY A 1102 ? 0.2584 0.2473 0.2581 0.0136  -0.0109 -0.0261 1100 GLY A CA  
8123  C C   . GLY A 1102 ? 0.2143 0.2045 0.2164 0.0133  -0.0129 -0.0278 1100 GLY A C   
8124  O O   . GLY A 1102 ? 0.2367 0.2289 0.2377 0.0137  -0.0126 -0.0272 1100 GLY A O   
8125  N N   . ARG A 1103 ? 0.2215 0.2102 0.2273 0.0128  -0.0151 -0.0299 1101 ARG A N   
8126  C CA  . ARG A 1103 ? 0.2145 0.2043 0.2231 0.0126  -0.0173 -0.0317 1101 ARG A CA  
8127  C C   . ARG A 1103 ? 0.2079 0.1993 0.2153 0.0149  -0.0191 -0.0356 1101 ARG A C   
8128  O O   . ARG A 1103 ? 0.2325 0.2226 0.2406 0.0158  -0.0202 -0.0379 1101 ARG A O   
8129  C CB  . ARG A 1103 ? 0.2433 0.2310 0.2579 0.0102  -0.0188 -0.0313 1101 ARG A CB  
8130  C CG  . ARG A 1103 ? 0.2757 0.2647 0.2934 0.0097  -0.0208 -0.0326 1101 ARG A CG  
8131  C CD  . ARG A 1103 ? 0.3087 0.2964 0.3324 0.0069  -0.0219 -0.0310 1101 ARG A CD  
8132  N NE  . ARG A 1103 ? 0.3533 0.3415 0.3769 0.0050  -0.0195 -0.0270 1101 ARG A NE  
8133  C CZ  . ARG A 1103 ? 0.4178 0.4084 0.4417 0.0039  -0.0186 -0.0253 1101 ARG A CZ  
8134  N NH1 . ARG A 1103 ? 0.3218 0.3143 0.3461 0.0045  -0.0197 -0.0268 1101 ARG A NH1 
8135  N NH2 . ARG A 1103 ? 0.4104 0.4018 0.4342 0.0023  -0.0164 -0.0221 1101 ARG A NH2 
8136  N N   . ILE A 1104 ? 0.1986 0.1931 0.2039 0.0161  -0.0196 -0.0365 1102 ILE A N   
8137  C CA  . ILE A 1104 ? 0.2046 0.2018 0.2082 0.0185  -0.0213 -0.0402 1102 ILE A CA  
8138  C C   . ILE A 1104 ? 0.2087 0.2058 0.2168 0.0180  -0.0243 -0.0431 1102 ILE A C   
8139  O O   . ILE A 1104 ? 0.2072 0.2044 0.2174 0.0166  -0.0246 -0.0417 1102 ILE A O   
8140  C CB  . ILE A 1104 ? 0.2146 0.2158 0.2132 0.0201  -0.0201 -0.0392 1102 ILE A CB  
8141  C CG1 . ILE A 1104 ? 0.2208 0.2218 0.2159 0.0203  -0.0172 -0.0358 1102 ILE A CG1 
8142  C CG2 . ILE A 1104 ? 0.2161 0.2212 0.2126 0.0227  -0.0219 -0.0429 1102 ILE A CG2 
8143  C CD1 . ILE A 1104 ? 0.2402 0.2407 0.2335 0.0215  -0.0167 -0.0368 1102 ILE A CD1 
8144  N N   . LEU A 1105 ? 0.1943 0.1914 0.2043 0.0193  -0.0266 -0.0472 1103 LEU A N   
8145  C CA  . LEU A 1105 ? 0.2189 0.2163 0.2332 0.0192  -0.0298 -0.0506 1103 LEU A CA  
8146  C C   . LEU A 1105 ? 0.1887 0.1909 0.1995 0.0211  -0.0305 -0.0524 1103 LEU A C   
8147  O O   . LEU A 1105 ? 0.2265 0.2321 0.2328 0.0236  -0.0302 -0.0542 1103 LEU A O   
8148  C CB  . LEU A 1105 ? 0.2430 0.2389 0.2607 0.0202  -0.0322 -0.0549 1103 LEU A CB  
8149  C CG  . LEU A 1105 ? 0.2551 0.2513 0.2780 0.0204  -0.0360 -0.0593 1103 LEU A CG  
8150  C CD1 . LEU A 1105 ? 0.2697 0.2630 0.2988 0.0173  -0.0370 -0.0569 1103 LEU A CD1 
8151  C CD2 . LEU A 1105 ? 0.2765 0.2716 0.3025 0.0219  -0.0384 -0.0640 1103 LEU A CD2 
8152  N N   . LEU A 1106 ? 0.1983 0.2013 0.2113 0.0201  -0.0315 -0.0519 1104 LEU A N   
8153  C CA  . LEU A 1106 ? 0.2165 0.2240 0.2269 0.0217  -0.0326 -0.0536 1104 LEU A CA  
8154  C C   . LEU A 1106 ? 0.2629 0.2708 0.2778 0.0221  -0.0363 -0.0584 1104 LEU A C   
8155  O O   . LEU A 1106 ? 0.2307 0.2357 0.2516 0.0200  -0.0377 -0.0582 1104 LEU A O   
8156  C CB  . LEU A 1106 ? 0.2103 0.2187 0.2201 0.0205  -0.0313 -0.0499 1104 LEU A CB  
8157  C CG  . LEU A 1106 ? 0.2815 0.2894 0.2877 0.0200  -0.0279 -0.0453 1104 LEU A CG  
8158  C CD1 . LEU A 1106 ? 0.2356 0.2456 0.2412 0.0196  -0.0271 -0.0428 1104 LEU A CD1 
8159  C CD2 . LEU A 1106 ? 0.2777 0.2874 0.2787 0.0220  -0.0264 -0.0452 1104 LEU A CD2 
8160  N N   . VAL A 1107 ? 0.2200 0.2321 0.2324 0.0247  -0.0378 -0.0625 1105 VAL A N   
8161  C CA  . VAL A 1107 ? 0.2127 0.2260 0.2292 0.0255  -0.0416 -0.0677 1105 VAL A CA  
8162  C C   . VAL A 1107 ? 0.2234 0.2425 0.2361 0.0271  -0.0422 -0.0686 1105 VAL A C   
8163  O O   . VAL A 1107 ? 0.2346 0.2587 0.2431 0.0298  -0.0427 -0.0716 1105 VAL A O   
8164  C CB  . VAL A 1107 ? 0.2278 0.2411 0.2456 0.0273  -0.0434 -0.0728 1105 VAL A CB  
8165  C CG1 . VAL A 1107 ? 0.2583 0.2719 0.2819 0.0278  -0.0477 -0.0784 1105 VAL A CG1 
8166  C CG2 . VAL A 1107 ? 0.2535 0.2614 0.2740 0.0258  -0.0421 -0.0708 1105 VAL A CG2 
8167  N N   . PRO A 1108 ? 0.2082 0.2273 0.2222 0.0256  -0.0421 -0.0659 1106 PRO A N   
8168  C CA  . PRO A 1108 ? 0.2460 0.2705 0.2565 0.0270  -0.0427 -0.0662 1106 PRO A CA  
8169  C C   . PRO A 1108 ? 0.2562 0.2829 0.2702 0.0278  -0.0466 -0.0716 1106 PRO A C   
8170  O O   . PRO A 1108 ? 0.2546 0.2779 0.2748 0.0268  -0.0489 -0.0745 1106 PRO A O   
8171  C CB  . PRO A 1108 ? 0.2394 0.2622 0.2510 0.0248  -0.0411 -0.0612 1106 PRO A CB  
8172  C CG  . PRO A 1108 ? 0.2379 0.2550 0.2558 0.0221  -0.0414 -0.0605 1106 PRO A CG  
8173  C CD  . PRO A 1108 ? 0.2574 0.2719 0.2754 0.0225  -0.0410 -0.0618 1106 PRO A CD  
8174  N N   . ALA A 1109 ? 0.2123 0.2450 0.2226 0.0297  -0.0475 -0.0728 1107 ALA A N   
8175  C CA  . ALA A 1109 ? 0.2546 0.2901 0.2678 0.0305  -0.0512 -0.0776 1107 ALA A CA  
8176  C C   . ALA A 1109 ? 0.2967 0.3343 0.3101 0.0297  -0.0515 -0.0752 1107 ALA A C   
8177  O O   . ALA A 1109 ? 0.3034 0.3408 0.3218 0.0290  -0.0543 -0.0777 1107 ALA A O   
8178  C CB  . ALA A 1109 ? 0.2527 0.2949 0.2617 0.0339  -0.0527 -0.0826 1107 ALA A CB  
8179  N N   . THR A 1110 ? 0.2375 0.2772 0.2462 0.0298  -0.0488 -0.0703 1108 THR A N   
8180  C CA  . THR A 1110 ? 0.2382 0.2800 0.2469 0.0292  -0.0490 -0.0677 1108 THR A CA  
8181  C C   . THR A 1110 ? 0.2374 0.2755 0.2464 0.0271  -0.0458 -0.0617 1108 THR A C   
8182  O O   . THR A 1110 ? 0.2259 0.2611 0.2332 0.0267  -0.0432 -0.0593 1108 THR A O   
8183  C CB  . THR A 1110 ? 0.2539 0.3032 0.2568 0.0317  -0.0492 -0.0676 1108 THR A CB  
8184  O OG1 . THR A 1110 ? 0.2477 0.2981 0.2452 0.0325  -0.0461 -0.0639 1108 THR A OG1 
8185  C CG2 . THR A 1110 ? 0.2574 0.3115 0.2594 0.0340  -0.0522 -0.0740 1108 THR A CG2 
8186  N N   . GLU A 1111 ? 0.2566 0.2950 0.2679 0.0260  -0.0461 -0.0596 1109 GLU A N   
8187  C CA  . GLU A 1111 ? 0.2261 0.2618 0.2378 0.0243  -0.0432 -0.0543 1109 GLU A CA  
8188  C C   . GLU A 1111 ? 0.2437 0.2814 0.2497 0.0256  -0.0406 -0.0508 1109 GLU A C   
8189  O O   . GLU A 1111 ? 0.2380 0.2724 0.2435 0.0246  -0.0380 -0.0477 1109 GLU A O   
8190  C CB  . GLU A 1111 ? 0.2682 0.3052 0.2832 0.0233  -0.0443 -0.0531 1109 GLU A CB  
8191  C CG  . GLU A 1111 ? 0.2638 0.2994 0.2788 0.0222  -0.0415 -0.0482 1109 GLU A CG  
8192  C CD  . GLU A 1111 ? 0.2969 0.3336 0.3158 0.0212  -0.0425 -0.0473 1109 GLU A CD  
8193  O OE1 . GLU A 1111 ? 0.3424 0.3768 0.3665 0.0193  -0.0434 -0.0483 1109 GLU A OE1 
8194  O OE2 . GLU A 1111 ? 0.3651 0.4051 0.3822 0.0222  -0.0425 -0.0454 1109 GLU A OE2 
8195  N N   . SER A 1112 ? 0.2394 0.2828 0.2413 0.0278  -0.0415 -0.0511 1110 SER A N   
8196  C CA  . SER A 1112 ? 0.2314 0.2771 0.2284 0.0289  -0.0392 -0.0473 1110 SER A CA  
8197  C C   . SER A 1112 ? 0.2445 0.2885 0.2389 0.0294  -0.0376 -0.0478 1110 SER A C   
8198  O O   . SER A 1112 ? 0.2399 0.2820 0.2325 0.0290  -0.0350 -0.0441 1110 SER A O   
8199  C CB  . SER A 1112 ? 0.2880 0.3409 0.2812 0.0311  -0.0406 -0.0474 1110 SER A CB  
8200  O OG  . SER A 1112 ? 0.2707 0.3259 0.2601 0.0319  -0.0385 -0.0429 1110 SER A OG  
8201  N N   . GLY A 1113 ? 0.2280 0.2724 0.2224 0.0303  -0.0392 -0.0526 1111 GLY A N   
8202  C CA  . GLY A 1113 ? 0.2077 0.2503 0.2003 0.0307  -0.0379 -0.0534 1111 GLY A CA  
8203  C C   . GLY A 1113 ? 0.1993 0.2350 0.1949 0.0284  -0.0358 -0.0510 1111 GLY A C   
8204  O O   . GLY A 1113 ? 0.2158 0.2500 0.2091 0.0284  -0.0334 -0.0485 1111 GLY A O   
8205  N N   . LEU A 1114 ? 0.2145 0.2465 0.2154 0.0264  -0.0368 -0.0516 1112 LEU A N   
8206  C CA  . LEU A 1114 ? 0.2231 0.2495 0.2270 0.0241  -0.0349 -0.0490 1112 LEU A CA  
8207  C C   . LEU A 1114 ? 0.2003 0.2263 0.2021 0.0236  -0.0320 -0.0440 1112 LEU A C   
8208  O O   . LEU A 1114 ? 0.1963 0.2193 0.1974 0.0229  -0.0298 -0.0419 1112 LEU A O   
8209  C CB  . LEU A 1114 ? 0.2228 0.2465 0.2328 0.0220  -0.0365 -0.0499 1112 LEU A CB  
8210  C CG  . LEU A 1114 ? 0.2374 0.2565 0.2505 0.0194  -0.0345 -0.0468 1112 LEU A CG  
8211  C CD1 . LEU A 1114 ? 0.2549 0.2708 0.2675 0.0192  -0.0333 -0.0470 1112 LEU A CD1 
8212  C CD2 . LEU A 1114 ? 0.2730 0.2906 0.2924 0.0174  -0.0362 -0.0476 1112 LEU A CD2 
8213  N N   . TYR A 1115 ? 0.2147 0.2437 0.2159 0.0240  -0.0322 -0.0422 1113 TYR A N   
8214  C CA  . TYR A 1115 ? 0.2179 0.2466 0.2181 0.0236  -0.0299 -0.0377 1113 TYR A CA  
8215  C C   . TYR A 1115 ? 0.2120 0.2418 0.2075 0.0250  -0.0281 -0.0358 1113 TYR A C   
8216  O O   . TYR A 1115 ? 0.2024 0.2298 0.1977 0.0243  -0.0258 -0.0328 1113 TYR A O   
8217  C CB  . TYR A 1115 ? 0.2076 0.2395 0.2084 0.0240  -0.0308 -0.0363 1113 TYR A CB  
8218  C CG  . TYR A 1115 ? 0.2027 0.2335 0.2085 0.0225  -0.0321 -0.0373 1113 TYR A CG  
8219  C CD1 . TYR A 1115 ? 0.2211 0.2480 0.2308 0.0205  -0.0319 -0.0383 1113 TYR A CD1 
8220  C CD2 . TYR A 1115 ? 0.2456 0.2797 0.2524 0.0230  -0.0337 -0.0371 1113 TYR A CD2 
8221  C CE1 . TYR A 1115 ? 0.2528 0.2793 0.2673 0.0190  -0.0331 -0.0389 1113 TYR A CE1 
8222  C CE2 . TYR A 1115 ? 0.2330 0.2665 0.2446 0.0216  -0.0348 -0.0379 1113 TYR A CE2 
8223  C CZ  . TYR A 1115 ? 0.2709 0.3006 0.2863 0.0195  -0.0345 -0.0388 1113 TYR A CZ  
8224  O OH  . TYR A 1115 ? 0.2674 0.2970 0.2877 0.0180  -0.0356 -0.0394 1113 TYR A OH  
8225  N N   . HIS A 1116 ? 0.2079 0.2420 0.1998 0.0270  -0.0292 -0.0376 1114 HIS A N   
8226  C CA  . HIS A 1116 ? 0.2089 0.2448 0.1965 0.0283  -0.0276 -0.0358 1114 HIS A CA  
8227  C C   . HIS A 1116 ? 0.2070 0.2388 0.1946 0.0277  -0.0262 -0.0366 1114 HIS A C   
8228  O O   . HIS A 1116 ? 0.2103 0.2410 0.1962 0.0276  -0.0240 -0.0337 1114 HIS A O   
8229  C CB  . HIS A 1116 ? 0.2348 0.2773 0.2186 0.0306  -0.0292 -0.0378 1114 HIS A CB  
8230  C CG  . HIS A 1116 ? 0.2408 0.2885 0.2231 0.0316  -0.0298 -0.0351 1114 HIS A CG  
8231  N ND1 . HIS A 1116 ? 0.2742 0.3241 0.2583 0.0316  -0.0320 -0.0364 1114 HIS A ND1 
8232  C CD2 . HIS A 1116 ? 0.2571 0.3083 0.2366 0.0325  -0.0286 -0.0308 1114 HIS A CD2 
8233  C CE1 . HIS A 1116 ? 0.2780 0.3325 0.2603 0.0326  -0.0322 -0.0330 1114 HIS A CE1 
8234  N NE2 . HIS A 1116 ? 0.3147 0.3701 0.2944 0.0330  -0.0302 -0.0295 1114 HIS A NE2 
8235  N N   . GLN A 1117 ? 0.1910 0.2205 0.1810 0.0272  -0.0276 -0.0406 1115 GLN A N   
8236  C CA  . GLN A 1117 ? 0.2081 0.2336 0.1988 0.0265  -0.0265 -0.0413 1115 GLN A CA  
8237  C C   . GLN A 1117 ? 0.1787 0.1994 0.1715 0.0243  -0.0244 -0.0379 1115 GLN A C   
8238  O O   . GLN A 1117 ? 0.1955 0.2142 0.1870 0.0241  -0.0224 -0.0361 1115 GLN A O   
8239  C CB  . GLN A 1117 ? 0.2106 0.2343 0.2047 0.0261  -0.0288 -0.0459 1115 GLN A CB  
8240  C CG  . GLN A 1117 ? 0.2108 0.2389 0.2029 0.0285  -0.0310 -0.0504 1115 GLN A CG  
8241  C CD  . GLN A 1117 ? 0.2503 0.2761 0.2470 0.0281  -0.0335 -0.0551 1115 GLN A CD  
8242  O OE1 . GLN A 1117 ? 0.2301 0.2513 0.2316 0.0259  -0.0339 -0.0546 1115 GLN A OE1 
8243  N NE2 . GLN A 1117 ? 0.2230 0.2522 0.2184 0.0302  -0.0354 -0.0598 1115 GLN A NE2 
8244  N N   . LEU A 1118 ? 0.1824 0.2018 0.1787 0.0228  -0.0248 -0.0371 1116 LEU A N   
8245  C CA  A LEU A 1118 ? 0.1988 0.2147 0.1974 0.0209  -0.0228 -0.0341 1116 LEU A CA  
8246  C CA  B LEU A 1118 ? 0.1989 0.2148 0.1975 0.0209  -0.0228 -0.0341 1116 LEU A CA  
8247  C C   . LEU A 1118 ? 0.1810 0.1977 0.1769 0.0214  -0.0207 -0.0304 1116 LEU A C   
8248  O O   . LEU A 1118 ? 0.1950 0.2090 0.1910 0.0206  -0.0187 -0.0285 1116 LEU A O   
8249  C CB  A LEU A 1118 ? 0.2068 0.2223 0.2097 0.0193  -0.0239 -0.0342 1116 LEU A CB  
8250  C CB  B LEU A 1118 ? 0.2076 0.2233 0.2103 0.0194  -0.0238 -0.0340 1116 LEU A CB  
8251  C CG  A LEU A 1118 ? 0.2121 0.2247 0.2182 0.0171  -0.0222 -0.0320 1116 LEU A CG  
8252  C CG  B LEU A 1118 ? 0.2039 0.2176 0.2109 0.0179  -0.0255 -0.0365 1116 LEU A CG  
8253  C CD1 A LEU A 1118 ? 0.2179 0.2271 0.2246 0.0160  -0.0213 -0.0321 1116 LEU A CD1 
8254  C CD1 B LEU A 1118 ? 0.1937 0.2087 0.2042 0.0170  -0.0266 -0.0363 1116 LEU A CD1 
8255  C CD2 A LEU A 1118 ? 0.2289 0.2420 0.2395 0.0158  -0.0238 -0.0330 1116 LEU A CD2 
8256  C CD2 B LEU A 1118 ? 0.2186 0.2284 0.2275 0.0161  -0.0239 -0.0351 1116 LEU A CD2 
8257  N N   . ALA A 1119 ? 0.2038 0.2244 0.1978 0.0229  -0.0212 -0.0294 1117 ALA A N   
8258  C CA  . ALA A 1119 ? 0.2160 0.2374 0.2083 0.0234  -0.0195 -0.0256 1117 ALA A CA  
8259  C C   . ALA A 1119 ? 0.2166 0.2375 0.2058 0.0241  -0.0180 -0.0248 1117 ALA A C   
8260  O O   . ALA A 1119 ? 0.2045 0.2232 0.1939 0.0235  -0.0161 -0.0222 1117 ALA A O   
8261  C CB  . ALA A 1119 ? 0.2356 0.2618 0.2266 0.0248  -0.0206 -0.0244 1117 ALA A CB  
8262  N N   . ALA A 1120 ? 0.1992 0.2223 0.1858 0.0254  -0.0189 -0.0273 1118 ALA A N   
8263  C CA  . ALA A 1120 ? 0.1981 0.2213 0.1818 0.0262  -0.0176 -0.0267 1118 ALA A CA  
8264  C C   . ALA A 1120 ? 0.2044 0.2222 0.1898 0.0246  -0.0161 -0.0268 1118 ALA A C   
8265  O O   . ALA A 1120 ? 0.1900 0.2065 0.1743 0.0244  -0.0142 -0.0243 1118 ALA A O   
8266  C CB  . ALA A 1120 ? 0.1898 0.2166 0.1709 0.0279  -0.0190 -0.0302 1118 ALA A CB  
8267  N N   . ALA A 1121 ? 0.1871 0.2022 0.1756 0.0233  -0.0172 -0.0293 1119 ALA A N   
8268  C CA  . ALA A 1121 ? 0.1861 0.1967 0.1764 0.0218  -0.0161 -0.0292 1119 ALA A CA  
8269  C C   . ALA A 1121 ? 0.1815 0.1899 0.1734 0.0203  -0.0142 -0.0260 1119 ALA A C   
8270  O O   . ALA A 1121 ? 0.1881 0.1942 0.1797 0.0196  -0.0125 -0.0245 1119 ALA A O   
8271  C CB  . ALA A 1121 ? 0.2046 0.2132 0.1985 0.0207  -0.0179 -0.0323 1119 ALA A CB  
8272  N N   . LEU A 1122 ? 0.1829 0.1921 0.1768 0.0197  -0.0146 -0.0251 1120 LEU A N   
8273  C CA  . LEU A 1122 ? 0.1755 0.1832 0.1713 0.0185  -0.0130 -0.0227 1120 LEU A CA  
8274  C C   . LEU A 1122 ? 0.1878 0.1962 0.1816 0.0194  -0.0115 -0.0199 1120 LEU A C   
8275  O O   . LEU A 1122 ? 0.1904 0.1967 0.1850 0.0186  -0.0099 -0.0183 1120 LEU A O   
8276  C CB  . LEU A 1122 ? 0.2028 0.2118 0.2016 0.0179  -0.0139 -0.0227 1120 LEU A CB  
8277  C CG  . LEU A 1122 ? 0.2008 0.2090 0.2026 0.0165  -0.0154 -0.0249 1120 LEU A CG  
8278  C CD1 . LEU A 1122 ? 0.2198 0.2300 0.2243 0.0162  -0.0162 -0.0247 1120 LEU A CD1 
8279  C CD2 . LEU A 1122 ? 0.2261 0.2314 0.2299 0.0146  -0.0142 -0.0246 1120 LEU A CD2 
8280  N N   . ALA A 1123 ? 0.1866 0.1981 0.1781 0.0211  -0.0121 -0.0191 1121 ALA A N   
8281  C CA  . ALA A 1123 ? 0.1718 0.1843 0.1620 0.0219  -0.0110 -0.0160 1121 ALA A CA  
8282  C C   . ALA A 1123 ? 0.1892 0.1998 0.1775 0.0218  -0.0094 -0.0154 1121 ALA A C   
8283  O O   . ALA A 1123 ? 0.1909 0.2010 0.1793 0.0219  -0.0081 -0.0128 1121 ALA A O   
8284  C CB  . ALA A 1123 ? 0.1842 0.2012 0.1718 0.0237  -0.0121 -0.0152 1121 ALA A CB  
8285  N N   . THR A 1124 ? 0.1805 0.1900 0.1676 0.0217  -0.0097 -0.0179 1122 THR A N   
8286  C CA  . THR A 1124 ? 0.1726 0.1803 0.1582 0.0217  -0.0083 -0.0176 1122 THR A CA  
8287  C C   . THR A 1124 ? 0.1863 0.1900 0.1743 0.0199  -0.0075 -0.0182 1122 THR A C   
8288  O O   . THR A 1124 ? 0.1939 0.1958 0.1811 0.0196  -0.0068 -0.0185 1122 THR A O   
8289  C CB  . THR A 1124 ? 0.1964 0.2064 0.1792 0.0231  -0.0092 -0.0198 1122 THR A CB  
8290  O OG1 . THR A 1124 ? 0.1917 0.2019 0.1757 0.0231  -0.0111 -0.0231 1122 THR A OG1 
8291  C CG2 . THR A 1124 ? 0.2140 0.2288 0.1940 0.0249  -0.0093 -0.0181 1122 THR A CG2 
8292  N N   . GLY A 1125 ? 0.1795 0.1823 0.1705 0.0186  -0.0077 -0.0181 1123 GLY A N   
8293  C CA  . GLY A 1125 ? 0.2008 0.2008 0.1940 0.0167  -0.0067 -0.0179 1123 GLY A CA  
8294  C C   . GLY A 1125 ? 0.1784 0.1769 0.1732 0.0156  -0.0077 -0.0200 1123 GLY A C   
8295  O O   . GLY A 1125 ? 0.2060 0.2026 0.2026 0.0140  -0.0069 -0.0195 1123 GLY A O   
8296  N N   . ASN A 1126 ? 0.1897 0.1891 0.1841 0.0164  -0.0095 -0.0222 1124 ASN A N   
8297  C CA  . ASN A 1126 ? 0.1979 0.1956 0.1944 0.0154  -0.0107 -0.0242 1124 ASN A CA  
8298  C C   . ASN A 1126 ? 0.1798 0.1776 0.1801 0.0139  -0.0118 -0.0247 1124 ASN A C   
8299  O O   . ASN A 1126 ? 0.2077 0.2074 0.2086 0.0140  -0.0121 -0.0244 1124 ASN A O   
8300  C CB  . ASN A 1126 ? 0.1820 0.1811 0.1771 0.0171  -0.0124 -0.0270 1124 ASN A CB  
8301  C CG  . ASN A 1126 ? 0.1892 0.1889 0.1807 0.0187  -0.0114 -0.0267 1124 ASN A CG  
8302  O OD1 . ASN A 1126 ? 0.2206 0.2180 0.2121 0.0182  -0.0105 -0.0264 1124 ASN A OD1 
8303  N ND2 . ASN A 1126 ? 0.1917 0.1948 0.1802 0.0205  -0.0114 -0.0265 1124 ASN A ND2 
8304  N N   . SER A 1127 ? 0.2003 0.1961 0.2036 0.0124  -0.0125 -0.0254 1125 SER A N   
8305  C CA  . SER A 1127 ? 0.2042 0.2003 0.2114 0.0111  -0.0143 -0.0263 1125 SER A CA  
8306  C C   . SER A 1127 ? 0.1988 0.1951 0.2066 0.0122  -0.0168 -0.0296 1125 SER A C   
8307  O O   . SER A 1127 ? 0.2064 0.2027 0.2115 0.0140  -0.0170 -0.0311 1125 SER A O   
8308  C CB  . SER A 1127 ? 0.2209 0.2153 0.2317 0.0087  -0.0140 -0.0249 1125 SER A CB  
8309  O OG  . SER A 1127 ? 0.2853 0.2772 0.2965 0.0086  -0.0145 -0.0256 1125 SER A OG  
8310  N N   . VAL A 1128 ? 0.2140 0.2108 0.2255 0.0114  -0.0188 -0.0309 1126 VAL A N   
8311  C CA  . VAL A 1128 ? 0.2085 0.2057 0.2211 0.0125  -0.0215 -0.0344 1126 VAL A CA  
8312  C C   . VAL A 1128 ? 0.2319 0.2273 0.2506 0.0106  -0.0236 -0.0353 1126 VAL A C   
8313  O O   . VAL A 1128 ? 0.2381 0.2334 0.2600 0.0084  -0.0232 -0.0330 1126 VAL A O   
8314  C CB  . VAL A 1128 ? 0.2338 0.2344 0.2445 0.0141  -0.0225 -0.0358 1126 VAL A CB  
8315  C CG1 . VAL A 1128 ? 0.2272 0.2298 0.2325 0.0159  -0.0206 -0.0345 1126 VAL A CG1 
8316  C CG2 . VAL A 1128 ? 0.2352 0.2368 0.2491 0.0125  -0.0227 -0.0345 1126 VAL A CG2 
8317  N N   . ALA A 1129 ? 0.2142 0.2087 0.2347 0.0115  -0.0260 -0.0386 1127 ALA A N   
8318  C CA  . ALA A 1129 ? 0.2174 0.2108 0.2443 0.0101  -0.0289 -0.0403 1127 ALA A CA  
8319  C C   . ALA A 1129 ? 0.2089 0.2046 0.2353 0.0121  -0.0313 -0.0444 1127 ALA A C   
8320  O O   . ALA A 1129 ? 0.2440 0.2406 0.2675 0.0145  -0.0319 -0.0474 1127 ALA A O   
8321  C CB  . ALA A 1129 ? 0.2841 0.2741 0.3148 0.0094  -0.0301 -0.0410 1127 ALA A CB  
8322  N N   . ILE A 1130 ? 0.2215 0.2187 0.2506 0.0113  -0.0326 -0.0445 1128 ILE A N   
8323  C CA  . ILE A 1130 ? 0.2240 0.2240 0.2527 0.0131  -0.0350 -0.0482 1128 ILE A CA  
8324  C C   . ILE A 1130 ? 0.2807 0.2790 0.3159 0.0125  -0.0386 -0.0516 1128 ILE A C   
8325  O O   . ILE A 1130 ? 0.2669 0.2631 0.3081 0.0100  -0.0395 -0.0499 1128 ILE A O   
8326  C CB  . ILE A 1130 ? 0.2172 0.2199 0.2451 0.0127  -0.0345 -0.0466 1128 ILE A CB  
8327  C CG1 . ILE A 1130 ? 0.2435 0.2473 0.2664 0.0129  -0.0310 -0.0429 1128 ILE A CG1 
8328  C CG2 . ILE A 1130 ? 0.2386 0.2447 0.2650 0.0149  -0.0368 -0.0504 1128 ILE A CG2 
8329  C CD1 . ILE A 1130 ? 0.2466 0.2526 0.2699 0.0123  -0.0305 -0.0410 1128 ILE A CD1 
8330  N N   . ASP A 1131 ? 0.2493 0.2489 0.2837 0.0149  -0.0408 -0.0564 1129 ASP A N   
8331  C CA  . ASP A 1131 ? 0.2582 0.2565 0.2994 0.0147  -0.0447 -0.0605 1129 ASP A CA  
8332  C C   . ASP A 1131 ? 0.2692 0.2681 0.3153 0.0130  -0.0466 -0.0601 1129 ASP A C   
8333  O O   . ASP A 1131 ? 0.2657 0.2681 0.3092 0.0140  -0.0469 -0.0610 1129 ASP A O   
8334  C CB  . ASP A 1131 ? 0.2523 0.2535 0.2908 0.0180  -0.0467 -0.0663 1129 ASP A CB  
8335  C CG  . ASP A 1131 ? 0.3486 0.3486 0.3943 0.0181  -0.0510 -0.0712 1129 ASP A CG  
8336  O OD1 . ASP A 1131 ? 0.2744 0.2702 0.3271 0.0159  -0.0523 -0.0701 1129 ASP A OD1 
8337  O OD2 . ASP A 1131 ? 0.2993 0.3027 0.3438 0.0205  -0.0532 -0.0763 1129 ASP A OD2 
8338  N N   . ALA A 1132 ? 0.2763 0.2720 0.3297 0.0102  -0.0479 -0.0583 1130 ALA A N   
8339  C CA  . ALA A 1132 ? 0.3240 0.3205 0.3829 0.0083  -0.0497 -0.0575 1130 ALA A CA  
8340  C C   . ALA A 1132 ? 0.3427 0.3405 0.4050 0.0098  -0.0537 -0.0631 1130 ALA A C   
8341  O O   . ALA A 1132 ? 0.3280 0.3278 0.3924 0.0091  -0.0550 -0.0633 1130 ALA A O   
8342  C CB  . ALA A 1132 ? 0.3318 0.3251 0.3982 0.0049  -0.0501 -0.0539 1130 ALA A CB  
8343  N N   . ALA A 1133 ? 0.2988 0.2958 0.3616 0.0118  -0.0558 -0.0680 1131 ALA A N   
8344  C CA  . ALA A 1133 ? 0.3142 0.3130 0.3801 0.0136  -0.0599 -0.0741 1131 ALA A CA  
8345  C C   . ALA A 1133 ? 0.3381 0.3422 0.3970 0.0161  -0.0594 -0.0762 1131 ALA A C   
8346  O O   . ALA A 1133 ? 0.3353 0.3419 0.3962 0.0175  -0.0626 -0.0811 1131 ALA A O   
8347  C CB  . ALA A 1133 ? 0.3440 0.3410 0.4126 0.0153  -0.0622 -0.0791 1131 ALA A CB  
8348  N N   . SER A 1134 ? 0.3208 0.3271 0.3719 0.0166  -0.0556 -0.0726 1132 SER A N   
8349  C CA  . SER A 1134 ? 0.2840 0.2955 0.3289 0.0187  -0.0551 -0.0736 1132 SER A CA  
8350  C C   . SER A 1134 ? 0.2894 0.3024 0.3374 0.0173  -0.0563 -0.0725 1132 SER A C   
8351  O O   . SER A 1134 ? 0.2929 0.3104 0.3375 0.0191  -0.0570 -0.0743 1132 SER A O   
8352  C CB  . SER A 1134 ? 0.2908 0.3036 0.3279 0.0193  -0.0508 -0.0692 1132 SER A CB  
8353  O OG  . SER A 1134 ? 0.2842 0.2948 0.3226 0.0166  -0.0484 -0.0637 1132 SER A OG  
8354  N N   . GLY A 1135 ? 0.3185 0.3283 0.3727 0.0143  -0.0564 -0.0694 1133 GLY A N   
8355  C CA  . GLY A 1135 ? 0.3011 0.3125 0.3586 0.0128  -0.0573 -0.0679 1133 GLY A CA  
8356  C C   . GLY A 1135 ? 0.3175 0.3318 0.3691 0.0130  -0.0542 -0.0642 1133 GLY A C   
8357  O O   . GLY A 1135 ? 0.3297 0.3465 0.3829 0.0126  -0.0551 -0.0638 1133 GLY A O   
8358  N N   . LEU A 1136 ? 0.2729 0.2870 0.3185 0.0137  -0.0507 -0.0614 1134 LEU A N   
8359  C CA  . LEU A 1136 ? 0.2947 0.3116 0.3349 0.0143  -0.0480 -0.0581 1134 LEU A CA  
8360  C C   . LEU A 1136 ? 0.2961 0.3115 0.3380 0.0118  -0.0453 -0.0530 1134 LEU A C   
8361  O O   . LEU A 1136 ? 0.2857 0.3026 0.3234 0.0122  -0.0427 -0.0502 1134 LEU A O   
8362  C CB  . LEU A 1136 ? 0.2926 0.3112 0.3253 0.0167  -0.0461 -0.0582 1134 LEU A CB  
8363  C CG  . LEU A 1136 ? 0.2760 0.2983 0.3056 0.0196  -0.0484 -0.0629 1134 LEU A CG  
8364  C CD1 . LEU A 1136 ? 0.2740 0.2980 0.2966 0.0217  -0.0462 -0.0624 1134 LEU A CD1 
8365  C CD2 . LEU A 1136 ? 0.3107 0.3374 0.3398 0.0204  -0.0499 -0.0636 1134 LEU A CD2 
8366  N N   . GLN A 1137 ? 0.3033 0.3159 0.3515 0.0092  -0.0459 -0.0519 1135 GLN A N   
8367  C CA  . GLN A 1137 ? 0.3328 0.3448 0.3827 0.0068  -0.0433 -0.0472 1135 GLN A CA  
8368  C C   . GLN A 1137 ? 0.2924 0.3077 0.3412 0.0068  -0.0422 -0.0453 1135 GLN A C   
8369  O O   . GLN A 1137 ? 0.3193 0.3352 0.3656 0.0064  -0.0392 -0.0420 1135 GLN A O   
8370  C CB  . GLN A 1137 ? 0.3250 0.3349 0.3828 0.0039  -0.0448 -0.0461 1135 GLN A CB  
8371  C CG  . GLN A 1137 ? 0.3266 0.3327 0.3860 0.0033  -0.0450 -0.0462 1135 GLN A CG  
8372  C CD  . GLN A 1137 ? 0.3285 0.3332 0.3898 0.0048  -0.0485 -0.0512 1135 GLN A CD  
8373  O OE1 . GLN A 1137 ? 0.3666 0.3735 0.4269 0.0066  -0.0505 -0.0548 1135 GLN A OE1 
8374  N NE2 . GLN A 1137 ? 0.3894 0.3907 0.4539 0.0041  -0.0493 -0.0516 1135 GLN A NE2 
8375  N N   . ALA A 1138 ? 0.2970 0.3147 0.3479 0.0073  -0.0448 -0.0475 1136 ALA A N   
8376  C CA  . ALA A 1138 ? 0.2965 0.3174 0.3471 0.0073  -0.0440 -0.0459 1136 ALA A CA  
8377  C C   . ALA A 1138 ? 0.3370 0.3598 0.3807 0.0096  -0.0420 -0.0449 1136 ALA A C   
8378  O O   . ALA A 1138 ? 0.3920 0.4171 0.4355 0.0096  -0.0409 -0.0430 1136 ALA A O   
8379  C CB  . ALA A 1138 ? 0.3210 0.3440 0.3755 0.0074  -0.0474 -0.0485 1136 ALA A CB  
8380  N N   . SER A 1139 ? 0.3145 0.3366 0.3532 0.0115  -0.0415 -0.0461 1137 SER A N   
8381  C CA  . SER A 1139 ? 0.3055 0.3296 0.3382 0.0135  -0.0396 -0.0447 1137 SER A CA  
8382  C C   . SER A 1139 ? 0.2907 0.3132 0.3217 0.0127  -0.0361 -0.0410 1137 SER A C   
8383  O O   . SER A 1139 ? 0.3190 0.3429 0.3461 0.0141  -0.0346 -0.0392 1137 SER A O   
8384  C CB  . SER A 1139 ? 0.3091 0.3338 0.3369 0.0158  -0.0404 -0.0473 1137 SER A CB  
8385  O OG  . SER A 1139 ? 0.3403 0.3676 0.3689 0.0170  -0.0437 -0.0510 1137 SER A OG  
8386  N N   . LEU A 1140 ? 0.2754 0.2952 0.3094 0.0106  -0.0350 -0.0397 1138 LEU A N   
8387  C CA  . LEU A 1140 ? 0.3075 0.3260 0.3400 0.0099  -0.0318 -0.0365 1138 LEU A CA  
8388  C C   . LEU A 1140 ? 0.3293 0.3484 0.3663 0.0076  -0.0308 -0.0344 1138 LEU A C   
8389  O O   . LEU A 1140 ? 0.3935 0.4113 0.4314 0.0061  -0.0289 -0.0324 1138 LEU A O   
8390  C CB  . LEU A 1140 ? 0.3539 0.3692 0.3848 0.0097  -0.0310 -0.0366 1138 LEU A CB  
8391  C CG  . LEU A 1140 ? 0.4017 0.4166 0.4271 0.0119  -0.0306 -0.0377 1138 LEU A CG  
8392  C CD1 . LEU A 1140 ? 0.3709 0.3826 0.3955 0.0112  -0.0290 -0.0367 1138 LEU A CD1 
8393  C CD2 . LEU A 1140 ? 0.3036 0.3207 0.3248 0.0136  -0.0290 -0.0359 1138 LEU A CD2 
8394  N N   . LYS A 1141 ? 0.3348 0.3567 0.3747 0.0074  -0.0319 -0.0346 1139 LYS A N   
8395  C CA  . LYS A 1141 ? 0.4012 0.4246 0.4456 0.0053  -0.0310 -0.0326 1139 LYS A CA  
8396  C C   . LYS A 1141 ? 0.3775 0.4024 0.4200 0.0058  -0.0281 -0.0305 1139 LYS A C   
8397  O O   . LYS A 1141 ? 0.3576 0.3832 0.3967 0.0078  -0.0277 -0.0305 1139 LYS A O   
8398  C CB  . LYS A 1141 ? 0.3868 0.4129 0.4352 0.0049  -0.0333 -0.0338 1139 LYS A CB  
8399  N N   . ASN A 1142 ? 0.3506 0.3762 0.3955 0.0039  -0.0262 -0.0285 1140 ASN A N   
8400  C CA  . ASN A 1142 ? 0.3355 0.3632 0.3798 0.0042  -0.0237 -0.0270 1140 ASN A CA  
8401  C C   . ASN A 1142 ? 0.3359 0.3614 0.3752 0.0058  -0.0219 -0.0265 1140 ASN A C   
8402  O O   . ASN A 1142 ? 0.3120 0.3388 0.3503 0.0071  -0.0208 -0.0260 1140 ASN A O   
8403  C CB  . ASN A 1142 ? 0.3953 0.4262 0.4414 0.0052  -0.0244 -0.0274 1140 ASN A CB  
8404  C CG  . ASN A 1142 ? 0.4932 0.5263 0.5443 0.0037  -0.0263 -0.0279 1140 ASN A CG  
8405  O OD1 . ASN A 1142 ? 0.5065 0.5402 0.5582 0.0046  -0.0286 -0.0294 1140 ASN A OD1 
8406  N ND2 . ASN A 1142 ? 0.4618 0.4967 0.5169 0.0014  -0.0254 -0.0266 1140 ASN A ND2 
8407  N N   . LEU A 1143 ? 0.3424 0.3648 0.3793 0.0057  -0.0218 -0.0265 1141 LEU A N   
8408  C CA  . LEU A 1143 ? 0.3145 0.3351 0.3470 0.0070  -0.0200 -0.0259 1141 LEU A CA  
8409  C C   . LEU A 1143 ? 0.3426 0.3645 0.3758 0.0063  -0.0174 -0.0243 1141 LEU A C   
8410  O O   . LEU A 1143 ? 0.3225 0.3462 0.3589 0.0044  -0.0167 -0.0235 1141 LEU A O   
8411  C CB  . LEU A 1143 ? 0.3026 0.3199 0.3330 0.0067  -0.0202 -0.0262 1141 LEU A CB  
8412  C CG  . LEU A 1143 ? 0.3180 0.3339 0.3461 0.0081  -0.0222 -0.0282 1141 LEU A CG  
8413  C CD1 . LEU A 1143 ? 0.2961 0.3089 0.3230 0.0076  -0.0221 -0.0285 1141 LEU A CD1 
8414  C CD2 . LEU A 1143 ? 0.3046 0.3213 0.3287 0.0105  -0.0220 -0.0282 1141 LEU A CD2 
8415  N N   . PRO A 1144 ? 0.3052 0.3267 0.3358 0.0079  -0.0161 -0.0238 1142 PRO A N   
8416  C CA  . PRO A 1144 ? 0.2916 0.3139 0.3226 0.0074  -0.0137 -0.0227 1142 PRO A CA  
8417  C C   . PRO A 1144 ? 0.2921 0.3127 0.3223 0.0058  -0.0128 -0.0220 1142 PRO A C   
8418  O O   . PRO A 1144 ? 0.2703 0.2880 0.2984 0.0059  -0.0136 -0.0222 1142 PRO A O   
8419  C CB  . PRO A 1144 ? 0.3514 0.3724 0.3795 0.0095  -0.0131 -0.0224 1142 PRO A CB  
8420  C CG  . PRO A 1144 ? 0.3545 0.3755 0.3816 0.0110  -0.0151 -0.0229 1142 PRO A CG  
8421  C CD  . PRO A 1144 ? 0.3303 0.3507 0.3576 0.0101  -0.0168 -0.0240 1142 PRO A CD  
8422  N N   . GLN A 1145 ? 0.3045 0.3274 0.3366 0.0045  -0.0110 -0.0211 1143 GLN A N   
8423  C CA  . GLN A 1145 ? 0.3240 0.3459 0.3557 0.0028  -0.0101 -0.0200 1143 GLN A CA  
8424  C C   . GLN A 1145 ? 0.2905 0.3086 0.3181 0.0038  -0.0095 -0.0198 1143 GLN A C   
8425  O O   . GLN A 1145 ? 0.2709 0.2867 0.2978 0.0029  -0.0098 -0.0193 1143 GLN A O   
8426  C CB  . GLN A 1145 ? 0.3762 0.4021 0.4099 0.0016  -0.0081 -0.0191 1143 GLN A CB  
8427  N N   . THR A 1146 ? 0.2858 0.3032 0.3111 0.0057  -0.0087 -0.0201 1144 THR A N   
8428  C CA  . THR A 1146 ? 0.2995 0.3136 0.3211 0.0067  -0.0081 -0.0197 1144 THR A CA  
8429  C C   . THR A 1146 ? 0.2687 0.2801 0.2882 0.0073  -0.0098 -0.0203 1144 THR A C   
8430  O O   . THR A 1146 ? 0.2798 0.2887 0.2971 0.0072  -0.0095 -0.0201 1144 THR A O   
8431  C CB  . THR A 1146 ? 0.3086 0.3227 0.3289 0.0086  -0.0074 -0.0197 1144 THR A CB  
8432  O OG1 . THR A 1146 ? 0.2920 0.3071 0.3132 0.0098  -0.0089 -0.0203 1144 THR A OG1 
8433  C CG2 . THR A 1146 ? 0.2913 0.3076 0.3134 0.0082  -0.0057 -0.0196 1144 THR A CG2 
8434  N N   . VAL A 1147 ? 0.2619 0.2741 0.2822 0.0080  -0.0116 -0.0214 1145 VAL A N   
8435  C CA  . VAL A 1147 ? 0.2551 0.2655 0.2736 0.0087  -0.0134 -0.0225 1145 VAL A CA  
8436  C C   . VAL A 1147 ? 0.2582 0.2678 0.2792 0.0069  -0.0145 -0.0231 1145 VAL A C   
8437  O O   . VAL A 1147 ? 0.2422 0.2494 0.2620 0.0070  -0.0152 -0.0237 1145 VAL A O   
8438  C CB  . VAL A 1147 ? 0.2421 0.2541 0.2604 0.0102  -0.0151 -0.0235 1145 VAL A CB  
8439  C CG1 . VAL A 1147 ? 0.2415 0.2525 0.2575 0.0113  -0.0168 -0.0251 1145 VAL A CG1 
8440  C CG2 . VAL A 1147 ? 0.2671 0.2802 0.2840 0.0118  -0.0141 -0.0225 1145 VAL A CG2 
8441  N N   . GLY A 1148 ? 0.2370 0.2487 0.2621 0.0052  -0.0148 -0.0227 1146 GLY A N   
8442  C CA  . GLY A 1148 ? 0.2355 0.2465 0.2639 0.0032  -0.0160 -0.0226 1146 GLY A CA  
8443  C C   . GLY A 1148 ? 0.2738 0.2826 0.3015 0.0022  -0.0149 -0.0214 1146 GLY A C   
8444  O O   . GLY A 1148 ? 0.2764 0.2831 0.3057 0.0015  -0.0164 -0.0218 1146 GLY A O   
8445  N N   . LEU A 1149 ? 0.2485 0.2578 0.2742 0.0022  -0.0125 -0.0199 1147 LEU A N   
8446  C CA  . LEU A 1149 ? 0.2895 0.2969 0.3143 0.0013  -0.0115 -0.0187 1147 LEU A CA  
8447  C C   . LEU A 1149 ? 0.2667 0.2705 0.2887 0.0027  -0.0124 -0.0199 1147 LEU A C   
8448  O O   . LEU A 1149 ? 0.3048 0.3065 0.3274 0.0018  -0.0125 -0.0193 1147 LEU A O   
8449  C CB  . LEU A 1149 ? 0.3033 0.3121 0.3262 0.0015  -0.0089 -0.0175 1147 LEU A CB  
8450  C CG  . LEU A 1149 ? 0.4182 0.4313 0.4439 -0.0001 -0.0077 -0.0162 1147 LEU A CG  
8451  C CD1 . LEU A 1149 ? 0.4299 0.4443 0.4535 0.0006  -0.0054 -0.0159 1147 LEU A CD1 
8452  C CD2 . LEU A 1149 ? 0.4130 0.4269 0.4418 -0.0026 -0.0081 -0.0144 1147 LEU A CD2 
8453  N N   . ARG A 1150 ? 0.2596 0.2630 0.2789 0.0048  -0.0130 -0.0215 1148 ARG A N   
8454  C CA  . ARG A 1150 ? 0.2508 0.2517 0.2672 0.0064  -0.0137 -0.0229 1148 ARG A CA  
8455  C C   . ARG A 1150 ? 0.2363 0.2366 0.2545 0.0067  -0.0164 -0.0252 1148 ARG A C   
8456  O O   . ARG A 1150 ? 0.2512 0.2499 0.2674 0.0079  -0.0172 -0.0268 1148 ARG A O   
8457  C CB  . ARG A 1150 ? 0.2241 0.2257 0.2364 0.0086  -0.0129 -0.0230 1148 ARG A CB  
8458  C CG  . ARG A 1150 ? 0.2731 0.2747 0.2837 0.0087  -0.0105 -0.0212 1148 ARG A CG  
8459  C CD  . ARG A 1150 ? 0.2579 0.2583 0.2646 0.0105  -0.0100 -0.0212 1148 ARG A CD  
8460  N NE  . ARG A 1150 ? 0.2484 0.2489 0.2536 0.0109  -0.0080 -0.0195 1148 ARG A NE  
8461  C CZ  . ARG A 1150 ? 0.2436 0.2444 0.2462 0.0126  -0.0076 -0.0189 1148 ARG A CZ  
8462  N NH1 . ARG A 1150 ? 0.2143 0.2159 0.2150 0.0141  -0.0088 -0.0198 1148 ARG A NH1 
8463  N NH2 . ARG A 1150 ? 0.2301 0.2309 0.2324 0.0128  -0.0060 -0.0174 1148 ARG A NH2 
8464  N N   . VAL A 1151 ? 0.2361 0.2378 0.2581 0.0056  -0.0179 -0.0256 1149 VAL A N   
8465  C CA  . VAL A 1151 ? 0.2424 0.2439 0.2664 0.0061  -0.0208 -0.0283 1149 VAL A CA  
8466  C C   . VAL A 1151 ? 0.3046 0.3047 0.3341 0.0038  -0.0223 -0.0279 1149 VAL A C   
8467  O O   . VAL A 1151 ? 0.3194 0.3208 0.3522 0.0017  -0.0217 -0.0257 1149 VAL A O   
8468  C CB  . VAL A 1151 ? 0.2626 0.2669 0.2871 0.0068  -0.0218 -0.0292 1149 VAL A CB  
8469  C CG1 . VAL A 1151 ? 0.2697 0.2739 0.2970 0.0070  -0.0249 -0.0321 1149 VAL A CG1 
8470  C CG2 . VAL A 1151 ? 0.2480 0.2536 0.2676 0.0091  -0.0207 -0.0293 1149 VAL A CG2 
8471  N N   . SER A 1152 ? 0.2530 0.2509 0.2839 0.0042  -0.0243 -0.0301 1150 SER A N   
8472  C CA  . SER A 1152 ? 0.2952 0.2917 0.3324 0.0023  -0.0266 -0.0302 1150 SER A CA  
8473  C C   . SER A 1152 ? 0.2856 0.2817 0.3244 0.0037  -0.0298 -0.0343 1150 SER A C   
8474  O O   . SER A 1152 ? 0.2799 0.2765 0.3143 0.0062  -0.0300 -0.0370 1150 SER A O   
8475  C CB  . SER A 1152 ? 0.3140 0.3076 0.3526 0.0011  -0.0262 -0.0288 1150 SER A CB  
8476  O OG  . SER A 1152 ? 0.3694 0.3611 0.4047 0.0033  -0.0264 -0.0311 1150 SER A OG  
8477  N N   . TRP A 1153 ? 0.2690 0.2645 0.3143 0.0021  -0.0324 -0.0348 1151 TRP A N   
8478  C CA  . TRP A 1153 ? 0.2840 0.2789 0.3321 0.0032  -0.0358 -0.0391 1151 TRP A CA  
8479  C C   . TRP A 1153 ? 0.3125 0.3040 0.3657 0.0024  -0.0379 -0.0400 1151 TRP A C   
8480  O O   . TRP A 1153 ? 0.3543 0.3444 0.4119 -0.0002 -0.0377 -0.0366 1151 TRP A O   
8481  C CB  . TRP A 1153 ? 0.2999 0.2968 0.3524 0.0021  -0.0377 -0.0393 1151 TRP A CB  
8482  C CG  . TRP A 1153 ? 0.2916 0.2918 0.3395 0.0034  -0.0363 -0.0393 1151 TRP A CG  
8483  C CD1 . TRP A 1153 ? 0.3180 0.3204 0.3639 0.0026  -0.0336 -0.0360 1151 TRP A CD1 
8484  C CD2 . TRP A 1153 ? 0.2776 0.2798 0.3225 0.0059  -0.0377 -0.0429 1151 TRP A CD2 
8485  N NE1 . TRP A 1153 ? 0.3164 0.3215 0.3587 0.0043  -0.0334 -0.0372 1151 TRP A NE1 
8486  C CE2 . TRP A 1153 ? 0.2999 0.3050 0.3413 0.0063  -0.0358 -0.0412 1151 TRP A CE2 
8487  C CE3 . TRP A 1153 ? 0.2585 0.2606 0.3034 0.0078  -0.0405 -0.0475 1151 TRP A CE3 
8488  C CZ2 . TRP A 1153 ? 0.2678 0.2757 0.3059 0.0085  -0.0367 -0.0433 1151 TRP A CZ2 
8489  C CZ3 . TRP A 1153 ? 0.2920 0.2974 0.3332 0.0100  -0.0412 -0.0499 1151 TRP A CZ3 
8490  C CH2 . TRP A 1153 ? 0.3071 0.3153 0.3449 0.0103  -0.0393 -0.0476 1151 TRP A CH2 
8491  N N   . SER A 1154 ? 0.2942 0.2846 0.3470 0.0045  -0.0400 -0.0445 1152 SER A N   
8492  C CA  . SER A 1154 ? 0.2977 0.2847 0.3551 0.0043  -0.0420 -0.0458 1152 SER A CA  
8493  C C   . SER A 1154 ? 0.3371 0.3235 0.4002 0.0050  -0.0463 -0.0507 1152 SER A C   
8494  O O   . SER A 1154 ? 0.3046 0.2930 0.3645 0.0077  -0.0474 -0.0552 1152 SER A O   
8495  C CB  . SER A 1154 ? 0.2880 0.2740 0.3397 0.0065  -0.0403 -0.0471 1152 SER A CB  
8496  O OG  . SER A 1154 ? 0.3133 0.2961 0.3701 0.0063  -0.0425 -0.0487 1152 SER A OG  
8497  N N   . LYS A 1155 ? 0.3420 0.3260 0.4138 0.0026  -0.0489 -0.0497 1153 LYS A N   
8498  C CA  . LYS A 1155 ? 0.3509 0.3336 0.4295 0.0032  -0.0534 -0.0544 1153 LYS A CA  
8499  C C   . LYS A 1155 ? 0.3712 0.3507 0.4525 0.0044  -0.0551 -0.0573 1153 LYS A C   
8500  O O   . LYS A 1155 ? 0.5098 0.4890 0.5940 0.0064  -0.0584 -0.0631 1153 LYS A O   
8501  C CB  . LYS A 1155 ? 0.3567 0.3386 0.4447 0.0000  -0.0558 -0.0519 1153 LYS A CB  
8502  N N   . ASP A 1156 ? 0.3434 0.3207 0.4239 0.0033  -0.0529 -0.0536 1154 ASP A N   
8503  C CA  . ASP A 1156 ? 0.3560 0.3302 0.4393 0.0042  -0.0543 -0.0556 1154 ASP A CA  
8504  C C   . ASP A 1156 ? 0.3572 0.3322 0.4315 0.0058  -0.0503 -0.0544 1154 ASP A C   
8505  O O   . ASP A 1156 ? 0.3277 0.3019 0.4007 0.0040  -0.0477 -0.0492 1154 ASP A O   
8506  C CB  . ASP A 1156 ? 0.4098 0.3806 0.5022 0.0009  -0.0558 -0.0514 1154 ASP A CB  
8507  C CG  . ASP A 1156 ? 0.5076 0.4747 0.6041 0.0017  -0.0576 -0.0533 1154 ASP A CG  
8508  O OD1 . ASP A 1156 ? 0.4960 0.4635 0.5883 0.0050  -0.0576 -0.0583 1154 ASP A OD1 
8509  O OD2 . ASP A 1156 ? 0.5047 0.4690 0.6089 -0.0009 -0.0590 -0.0497 1154 ASP A OD2 
8510  N N   . TRP A 1157 ? 0.3465 0.3237 0.4147 0.0092  -0.0500 -0.0590 1155 TRP A N   
8511  C CA  . TRP A 1157 ? 0.2976 0.2761 0.3571 0.0107  -0.0462 -0.0577 1155 TRP A CA  
8512  C C   . TRP A 1157 ? 0.3307 0.3059 0.3918 0.0100  -0.0453 -0.0555 1155 TRP A C   
8513  O O   . TRP A 1157 ? 0.3214 0.2969 0.3775 0.0094  -0.0418 -0.0514 1155 TRP A O   
8514  C CB  . TRP A 1157 ? 0.3174 0.2991 0.3714 0.0145  -0.0465 -0.0632 1155 TRP A CB  
8515  C CG  . TRP A 1157 ? 0.2901 0.2756 0.3419 0.0156  -0.0474 -0.0656 1155 TRP A CG  
8516  C CD1 . TRP A 1157 ? 0.2647 0.2512 0.3178 0.0138  -0.0474 -0.0631 1155 TRP A CD1 
8517  C CD2 . TRP A 1157 ? 0.2533 0.2427 0.3015 0.0189  -0.0487 -0.0712 1155 TRP A CD2 
8518  N NE1 . TRP A 1157 ? 0.2902 0.2805 0.3406 0.0157  -0.0486 -0.0667 1155 TRP A NE1 
8519  C CE2 . TRP A 1157 ? 0.2813 0.2737 0.3286 0.0189  -0.0494 -0.0716 1155 TRP A CE2 
8520  C CE3 . TRP A 1157 ? 0.2745 0.2657 0.3201 0.0220  -0.0492 -0.0759 1155 TRP A CE3 
8521  C CZ2 . TRP A 1157 ? 0.2965 0.2936 0.3402 0.0217  -0.0507 -0.0764 1155 TRP A CZ2 
8522  C CZ3 . TRP A 1157 ? 0.2760 0.2723 0.3180 0.0248  -0.0504 -0.0808 1155 TRP A CZ3 
8523  C CH2 . TRP A 1157 ? 0.3141 0.3133 0.3552 0.0247  -0.0512 -0.0809 1155 TRP A CH2 
8524  N N   . ALA A 1158 ? 0.3254 0.2977 0.3939 0.0100  -0.0486 -0.0582 1156 ALA A N   
8525  C CA  . ALA A 1158 ? 0.3569 0.3260 0.4273 0.0094  -0.0480 -0.0562 1156 ALA A CA  
8526  C C   . ALA A 1158 ? 0.4072 0.3747 0.4799 0.0058  -0.0464 -0.0492 1156 ALA A C   
8527  O O   . ALA A 1158 ? 0.4833 0.4494 0.5545 0.0053  -0.0445 -0.0463 1156 ALA A O   
8528  C CB  . ALA A 1158 ? 0.3856 0.3517 0.4646 0.0102  -0.0524 -0.0607 1156 ALA A CB  
8529  N N   . ALA A 1159 ? 0.3525 0.3207 0.4288 0.0033  -0.0470 -0.0464 1157 ALA A N   
8530  C CA  . ALA A 1159 ? 0.4036 0.3715 0.4820 -0.0001 -0.0454 -0.0397 1157 ALA A CA  
8531  C C   . ALA A 1159 ? 0.4126 0.3834 0.4823 -0.0003 -0.0409 -0.0362 1157 ALA A C   
8532  O O   . ALA A 1159 ? 0.4148 0.3857 0.4844 -0.0025 -0.0389 -0.0311 1157 ALA A O   
8533  C CB  . ALA A 1159 ? 0.3903 0.3585 0.4762 -0.0027 -0.0479 -0.0380 1157 ALA A CB  
8534  N N   . ASP A 1160 ? 0.3918 0.3652 0.4545 0.0020  -0.0393 -0.0388 1158 ASP A N   
8535  C CA  . ASP A 1160 ? 0.3842 0.3604 0.4397 0.0018  -0.0355 -0.0358 1158 ASP A CA  
8536  C C   . ASP A 1160 ? 0.3287 0.3054 0.3765 0.0041  -0.0327 -0.0364 1158 ASP A C   
8537  O O   . ASP A 1160 ? 0.3456 0.3245 0.3874 0.0043  -0.0298 -0.0345 1158 ASP A O   
8538  C CB  . ASP A 1160 ? 0.3678 0.3470 0.4219 0.0023  -0.0358 -0.0372 1158 ASP A CB  
8539  C CG  . ASP A 1160 ? 0.4315 0.4105 0.4933 -0.0002 -0.0384 -0.0360 1158 ASP A CG  
8540  O OD1 . ASP A 1160 ? 0.4998 0.4776 0.5669 -0.0029 -0.0387 -0.0322 1158 ASP A OD1 
8541  O OD2 . ASP A 1160 ? 0.3808 0.3613 0.4437 0.0005  -0.0401 -0.0387 1158 ASP A OD2 
8542  N N   . GLY A 1161 ? 0.3051 0.2798 0.3532 0.0057  -0.0337 -0.0390 1159 GLY A N   
8543  C CA  . GLY A 1161 ? 0.3415 0.3167 0.3830 0.0076  -0.0312 -0.0393 1159 GLY A CA  
8544  C C   . GLY A 1161 ? 0.3478 0.3214 0.3888 0.0058  -0.0289 -0.0347 1159 GLY A C   
8545  O O   . GLY A 1161 ? 0.4189 0.3921 0.4639 0.0030  -0.0289 -0.0309 1159 GLY A O   
8546  N N   . PRO A 1162 ? 0.3337 0.3072 0.3699 0.0074  -0.0270 -0.0349 1160 PRO A N   
8547  C CA  . PRO A 1162 ? 0.3188 0.2937 0.3502 0.0106  -0.0266 -0.0388 1160 PRO A CA  
8548  C C   . PRO A 1162 ? 0.3442 0.3226 0.3695 0.0118  -0.0248 -0.0387 1160 PRO A C   
8549  O O   . PRO A 1162 ? 0.3205 0.2998 0.3435 0.0104  -0.0226 -0.0352 1160 PRO A O   
8550  C CB  . PRO A 1162 ? 0.3290 0.3027 0.3578 0.0110  -0.0247 -0.0372 1160 PRO A CB  
8551  C CG  . PRO A 1162 ? 0.3781 0.3512 0.4070 0.0083  -0.0227 -0.0319 1160 PRO A CG  
8552  C CD  . PRO A 1162 ? 0.3514 0.3237 0.3868 0.0058  -0.0248 -0.0307 1160 PRO A CD  
8553  N N   . PHE A 1163 ? 0.2726 0.2533 0.2956 0.0143  -0.0258 -0.0428 1161 PHE A N   
8554  C CA  . PHE A 1163 ? 0.2336 0.2179 0.2505 0.0157  -0.0241 -0.0425 1161 PHE A CA  
8555  C C   . PHE A 1163 ? 0.2247 0.2104 0.2360 0.0176  -0.0219 -0.0424 1161 PHE A C   
8556  O O   . PHE A 1163 ? 0.2742 0.2584 0.2862 0.0182  -0.0219 -0.0432 1161 PHE A O   
8557  C CB  . PHE A 1163 ? 0.2195 0.2064 0.2371 0.0172  -0.0265 -0.0466 1161 PHE A CB  
8558  C CG  . PHE A 1163 ? 0.2460 0.2314 0.2697 0.0152  -0.0289 -0.0468 1161 PHE A CG  
8559  C CD1 . PHE A 1163 ? 0.2532 0.2386 0.2776 0.0130  -0.0277 -0.0430 1161 PHE A CD1 
8560  C CD2 . PHE A 1163 ? 0.2404 0.2246 0.2697 0.0156  -0.0324 -0.0509 1161 PHE A CD2 
8561  C CE1 . PHE A 1163 ? 0.2778 0.2622 0.3081 0.0110  -0.0299 -0.0429 1161 PHE A CE1 
8562  C CE2 . PHE A 1163 ? 0.2849 0.2677 0.3205 0.0136  -0.0347 -0.0507 1161 PHE A CE2 
8563  C CZ  . PHE A 1163 ? 0.2673 0.2504 0.3033 0.0113  -0.0334 -0.0465 1161 PHE A CZ  
8564  N N   . ALA A 1164 ? 0.2307 0.2194 0.2368 0.0184  -0.0199 -0.0409 1162 ALA A N   
8565  C CA  . ALA A 1164 ? 0.2240 0.2146 0.2250 0.0201  -0.0178 -0.0401 1162 ALA A CA  
8566  C C   . ALA A 1164 ? 0.2228 0.2182 0.2199 0.0227  -0.0182 -0.0425 1162 ALA A C   
8567  O O   . ALA A 1164 ? 0.2495 0.2474 0.2421 0.0241  -0.0164 -0.0414 1162 ALA A O   
8568  C CB  . ALA A 1164 ? 0.2609 0.2509 0.2594 0.0188  -0.0149 -0.0354 1162 ALA A CB  
8569  N N   . GLY A 1165 ? 0.2161 0.2130 0.2149 0.0233  -0.0206 -0.0457 1163 GLY A N   
8570  C CA  . GLY A 1165 ? 0.2148 0.2169 0.2102 0.0258  -0.0214 -0.0484 1163 GLY A CA  
8571  C C   . GLY A 1165 ? 0.2038 0.2066 0.2021 0.0255  -0.0239 -0.0508 1163 GLY A C   
8572  O O   . GLY A 1165 ? 0.2139 0.2133 0.2168 0.0234  -0.0249 -0.0500 1163 GLY A O   
8573  N N   . ALA A 1166 ? 0.2054 0.2133 0.2012 0.0277  -0.0251 -0.0536 1164 ALA A N   
8574  C CA  . ALA A 1166 ? 0.1997 0.2087 0.1982 0.0277  -0.0277 -0.0563 1164 ALA A CA  
8575  C C   . ALA A 1166 ? 0.2006 0.2159 0.1943 0.0296  -0.0277 -0.0566 1164 ALA A C   
8576  O O   . ALA A 1166 ? 0.2411 0.2606 0.2302 0.0316  -0.0265 -0.0568 1164 ALA A O   
8577  C CB  . ALA A 1166 ? 0.2294 0.2376 0.2325 0.0285  -0.0309 -0.0619 1164 ALA A CB  
8578  N N   . LEU A 1167 ? 0.1933 0.2093 0.1884 0.0288  -0.0288 -0.0563 1165 LEU A N   
8579  C CA  . LEU A 1167 ? 0.1944 0.2165 0.1860 0.0305  -0.0295 -0.0570 1165 LEU A CA  
8580  C C   . LEU A 1167 ? 0.2236 0.2467 0.2188 0.0309  -0.0329 -0.0618 1165 LEU A C   
8581  O O   . LEU A 1167 ? 0.2291 0.2481 0.2294 0.0289  -0.0342 -0.0618 1165 LEU A O   
8582  C CB  . LEU A 1167 ? 0.2089 0.2312 0.1990 0.0293  -0.0278 -0.0520 1165 LEU A CB  
8583  C CG  . LEU A 1167 ? 0.2048 0.2257 0.1920 0.0287  -0.0245 -0.0471 1165 LEU A CG  
8584  C CD1 . LEU A 1167 ? 0.2353 0.2559 0.2224 0.0274  -0.0233 -0.0428 1165 LEU A CD1 
8585  C CD2 . LEU A 1167 ? 0.2469 0.2729 0.2291 0.0311  -0.0235 -0.0472 1165 LEU A CD2 
8586  N N   . VAL A 1168 ? 0.2163 0.2452 0.2089 0.0336  -0.0345 -0.0659 1166 VAL A N   
8587  C CA  . VAL A 1168 ? 0.2166 0.2471 0.2127 0.0344  -0.0381 -0.0714 1166 VAL A CA  
8588  C C   . VAL A 1168 ? 0.2252 0.2628 0.2174 0.0361  -0.0389 -0.0720 1166 VAL A C   
8589  O O   . VAL A 1168 ? 0.2223 0.2655 0.2087 0.0378  -0.0374 -0.0706 1166 VAL A O   
8590  C CB  . VAL A 1168 ? 0.2177 0.2489 0.2153 0.0363  -0.0399 -0.0773 1166 VAL A CB  
8591  C CG1 . VAL A 1168 ? 0.2332 0.2659 0.2353 0.0372  -0.0440 -0.0835 1166 VAL A CG1 
8592  C CG2 . VAL A 1168 ? 0.2482 0.2726 0.2497 0.0346  -0.0390 -0.0761 1166 VAL A CG2 
8593  N N   . GLU A 1169 ? 0.2008 0.2385 0.1964 0.0354  -0.0414 -0.0738 1167 GLU A N   
8594  C CA  . GLU A 1169 ? 0.2101 0.2546 0.2028 0.0370  -0.0428 -0.0751 1167 GLU A CA  
8595  C C   . GLU A 1169 ? 0.2598 0.3063 0.2560 0.0384  -0.0467 -0.0823 1167 GLU A C   
8596  O O   . GLU A 1169 ? 0.2451 0.2862 0.2478 0.0368  -0.0487 -0.0844 1167 GLU A O   
8597  C CB  . GLU A 1169 ? 0.2169 0.2599 0.2108 0.0351  -0.0424 -0.0709 1167 GLU A CB  
8598  C CG  . GLU A 1169 ? 0.2052 0.2551 0.1966 0.0366  -0.0441 -0.0720 1167 GLU A CG  
8599  C CD  . GLU A 1169 ? 0.2280 0.2758 0.2221 0.0346  -0.0443 -0.0688 1167 GLU A CD  
8600  O OE1 . GLU A 1169 ? 0.2334 0.2747 0.2317 0.0321  -0.0434 -0.0665 1167 GLU A OE1 
8601  O OE2 . GLU A 1169 ? 0.2470 0.3001 0.2391 0.0355  -0.0453 -0.0685 1167 GLU A OE2 
8602  N N   . GLY A 1170 ? 0.2233 0.2776 0.2155 0.0413  -0.0479 -0.0860 1168 GLY A N   
8603  C CA  . GLY A 1170 ? 0.2631 0.3202 0.2587 0.0427  -0.0519 -0.0931 1168 GLY A CA  
8604  C C   . GLY A 1170 ? 0.2640 0.3305 0.2543 0.0463  -0.0526 -0.0974 1168 GLY A C   
8605  O O   . GLY A 1170 ? 0.2623 0.3330 0.2467 0.0475  -0.0500 -0.0947 1168 GLY A O   
8606  N N   . ASP A 1171 ? 0.2541 0.3242 0.2470 0.0479  -0.0564 -0.1044 1169 ASP A N   
8607  C CA  . ASP A 1171 ? 0.2686 0.3481 0.2574 0.0515  -0.0575 -0.1098 1169 ASP A CA  
8608  C C   . ASP A 1171 ? 0.2700 0.3477 0.2600 0.0527  -0.0571 -0.1134 1169 ASP A C   
8609  O O   . ASP A 1171 ? 0.2552 0.3244 0.2495 0.0507  -0.0562 -0.1116 1169 ASP A O   
8610  C CB  . ASP A 1171 ? 0.2849 0.3697 0.2757 0.0531  -0.0617 -0.1163 1169 ASP A CB  
8611  C CG  . ASP A 1171 ? 0.3403 0.4187 0.3403 0.0524  -0.0654 -0.1223 1169 ASP A CG  
8612  O OD1 . ASP A 1171 ? 0.3089 0.3800 0.3135 0.0512  -0.0650 -0.1226 1169 ASP A OD1 
8613  O OD2 . ASP A 1171 ? 0.3908 0.4716 0.3938 0.0529  -0.0689 -0.1267 1169 ASP A OD2 
8614  N N   . ALA A 1172 ? 0.2711 0.3577 0.2572 0.0561  -0.0577 -0.1184 1170 ALA A N   
8615  C CA  . ALA A 1172 ? 0.2891 0.3755 0.2754 0.0576  -0.0569 -0.1213 1170 ALA A CA  
8616  C C   . ALA A 1172 ? 0.2955 0.3734 0.2908 0.0568  -0.0596 -0.1262 1170 ALA A C   
8617  O O   . ALA A 1172 ? 0.2845 0.3564 0.2820 0.0558  -0.0581 -0.1247 1170 ALA A O   
8618  C CB  . ALA A 1172 ? 0.2965 0.3950 0.2777 0.0616  -0.0576 -0.1269 1170 ALA A CB  
8619  N N   . GLU A 1173 ? 0.3063 0.3836 0.3073 0.0570  -0.0637 -0.1319 1171 GLU A N   
8620  C CA  . GLU A 1173 ? 0.3148 0.3843 0.3253 0.0562  -0.0667 -0.1365 1171 GLU A CA  
8621  C C   . GLU A 1173 ? 0.2974 0.3559 0.3130 0.0520  -0.0656 -0.1300 1171 GLU A C   
8622  O O   . GLU A 1173 ? 0.3202 0.3716 0.3418 0.0509  -0.0661 -0.1307 1171 GLU A O   
8623  C CB  . GLU A 1173 ? 0.3586 0.4310 0.3745 0.0579  -0.0717 -0.1451 1171 GLU A CB  
8624  C CG  . GLU A 1173 ? 0.4002 0.4833 0.4124 0.0623  -0.0731 -0.1529 1171 GLU A CG  
8625  C CD  . GLU A 1173 ? 0.4133 0.4963 0.4254 0.0640  -0.0718 -0.1552 1171 GLU A CD  
8626  O OE1 . GLU A 1173 ? 0.4327 0.5065 0.4518 0.0624  -0.0724 -0.1550 1171 GLU A OE1 
8627  O OE2 . GLU A 1173 ? 0.4361 0.5287 0.4412 0.0670  -0.0703 -0.1571 1171 GLU A OE2 
8628  N N   . ARG A 1174 ? 0.2627 0.3200 0.2760 0.0498  -0.0640 -0.1238 1172 ARG A N   
8629  C CA  . ARG A 1174 ? 0.2888 0.3369 0.3057 0.0459  -0.0623 -0.1171 1172 ARG A CA  
8630  C C   . ARG A 1174 ? 0.2907 0.3359 0.3042 0.0453  -0.0584 -0.1123 1172 ARG A C   
8631  O O   . ARG A 1174 ? 0.2603 0.2978 0.2790 0.0432  -0.0581 -0.1104 1172 ARG A O   
8632  C CB  . ARG A 1174 ? 0.2831 0.3318 0.2974 0.0441  -0.0611 -0.1116 1172 ARG A CB  
8633  C CG  . ARG A 1174 ? 0.2830 0.3236 0.3000 0.0403  -0.0589 -0.1045 1172 ARG A CG  
8634  C CD  . ARG A 1174 ? 0.3326 0.3659 0.3595 0.0382  -0.0617 -0.1064 1172 ARG A CD  
8635  N NE  . ARG A 1174 ? 0.2805 0.3071 0.3097 0.0346  -0.0595 -0.0995 1172 ARG A NE  
8636  C CZ  . ARG A 1174 ? 0.3155 0.3352 0.3523 0.0323  -0.0605 -0.0987 1172 ARG A CZ  
8637  N NH1 . ARG A 1174 ? 0.3118 0.3294 0.3552 0.0330  -0.0640 -0.1042 1172 ARG A NH1 
8638  N NH2 . ARG A 1174 ? 0.2968 0.3119 0.3347 0.0292  -0.0582 -0.0922 1172 ARG A NH2 
8639  N N   . ILE A 1175 ? 0.2562 0.3078 0.2615 0.0471  -0.0555 -0.1103 1173 ILE A N   
8640  C CA  . ILE A 1175 ? 0.2426 0.2921 0.2446 0.0467  -0.0519 -0.1058 1173 ILE A CA  
8641  C C   . ILE A 1175 ? 0.2519 0.2986 0.2582 0.0478  -0.0531 -0.1106 1173 ILE A C   
8642  O O   . ILE A 1175 ? 0.2613 0.3014 0.2701 0.0460  -0.0515 -0.1073 1173 ILE A O   
8643  C CB  . ILE A 1175 ? 0.2624 0.3202 0.2553 0.0487  -0.0491 -0.1033 1173 ILE A CB  
8644  C CG1 . ILE A 1175 ? 0.2672 0.3261 0.2567 0.0471  -0.0475 -0.0971 1173 ILE A CG1 
8645  C CG2 . ILE A 1175 ? 0.2609 0.3176 0.2509 0.0488  -0.0458 -0.1002 1173 ILE A CG2 
8646  C CD1 . ILE A 1175 ? 0.2823 0.3504 0.2638 0.0490  -0.0456 -0.0946 1173 ILE A CD1 
8647  N N   . ARG A 1176 ? 0.2910 0.3430 0.2986 0.0508  -0.0560 -0.1186 1174 ARG A N   
8648  C CA  . ARG A 1176 ? 0.2774 0.3271 0.2897 0.0521  -0.0576 -0.1237 1174 ARG A CA  
8649  C C   . ARG A 1176 ? 0.2366 0.2761 0.2585 0.0493  -0.0597 -0.1234 1174 ARG A C   
8650  O O   . ARG A 1176 ? 0.2735 0.3074 0.2985 0.0484  -0.0587 -0.1219 1174 ARG A O   
8651  C CB  . ARG A 1176 ? 0.2570 0.3146 0.2697 0.0560  -0.0608 -0.1331 1174 ARG A CB  
8652  C CG  . ARG A 1176 ? 0.3251 0.3826 0.3407 0.0582  -0.0616 -0.1384 1174 ARG A CG  
8653  C CD  . ARG A 1176 ? 0.3563 0.4201 0.3751 0.0617  -0.0658 -0.1488 1174 ARG A CD  
8654  N NE  . ARG A 1176 ? 0.3295 0.4045 0.3409 0.0642  -0.0656 -0.1509 1174 ARG A NE  
8655  C CZ  . ARG A 1176 ? 0.3786 0.4633 0.3826 0.0672  -0.0636 -0.1523 1174 ARG A CZ  
8656  N NH1 . ARG A 1176 ? 0.3865 0.4711 0.3893 0.0681  -0.0614 -0.1517 1174 ARG A NH1 
8657  N NH2 . ARG A 1176 ? 0.3874 0.4829 0.3855 0.0694  -0.0640 -0.1544 1174 ARG A NH2 
8658  N N   . ALA A 1177 ? 0.2699 0.3071 0.2969 0.0478  -0.0624 -0.1243 1175 ALA A N   
8659  C CA  . ALA A 1177 ? 0.2952 0.3234 0.3319 0.0449  -0.0646 -0.1235 1175 ALA A CA  
8660  C C   . ALA A 1177 ? 0.2601 0.2817 0.2961 0.0415  -0.0611 -0.1149 1175 ALA A C   
8661  O O   . ALA A 1177 ? 0.2776 0.2928 0.3194 0.0399  -0.0615 -0.1137 1175 ALA A O   
8662  C CB  . ALA A 1177 ? 0.2771 0.3050 0.3184 0.0439  -0.0679 -0.1253 1175 ALA A CB  
8663  N N   . VAL A 1178 ? 0.2604 0.2839 0.2897 0.0404  -0.0578 -0.1088 1176 VAL A N   
8664  C CA  . VAL A 1178 ? 0.2412 0.2593 0.2696 0.0373  -0.0544 -0.1010 1176 VAL A CA  
8665  C C   . VAL A 1178 ? 0.2660 0.2830 0.2918 0.0381  -0.0519 -0.0997 1176 VAL A C   
8666  O O   . VAL A 1178 ? 0.2663 0.2771 0.2955 0.0358  -0.0509 -0.0960 1176 VAL A O   
8667  C CB  . VAL A 1178 ? 0.2333 0.2542 0.2551 0.0364  -0.0516 -0.0955 1176 VAL A CB  
8668  C CG1 . VAL A 1178 ? 0.2469 0.2633 0.2671 0.0338  -0.0479 -0.0880 1176 VAL A CG1 
8669  C CG2 . VAL A 1178 ? 0.2604 0.2811 0.2859 0.0351  -0.0540 -0.0959 1176 VAL A CG2 
8670  N N   . ASN A 1179 ? 0.2756 0.2990 0.2953 0.0412  -0.0509 -0.1025 1177 ASN A N   
8671  C CA  . ASN A 1179 ? 0.2641 0.2872 0.2813 0.0421  -0.0485 -0.1014 1177 ASN A CA  
8672  C C   . ASN A 1179 ? 0.2861 0.3037 0.3113 0.0419  -0.0510 -0.1050 1177 ASN A C   
8673  O O   . ASN A 1179 ? 0.2670 0.2802 0.2932 0.0406  -0.0492 -0.1016 1177 ASN A O   
8674  C CB  . ASN A 1179 ? 0.3123 0.3445 0.3224 0.0457  -0.0476 -0.1047 1177 ASN A CB  
8675  C CG  . ASN A 1179 ? 0.3640 0.3975 0.3682 0.0460  -0.0436 -0.1002 1177 ASN A CG  
8676  O OD1 . ASN A 1179 ? 0.4259 0.4540 0.4299 0.0434  -0.0411 -0.0940 1177 ASN A OD1 
8677  N ND2 . ASN A 1179 ? 0.4068 0.4479 0.4061 0.0491  -0.0429 -0.1034 1177 ASN A ND2 
8678  N N   . LYS A 1180 ? 0.2930 0.3109 0.3246 0.0431  -0.0553 -0.1117 1178 LYS A N   
8679  C CA  . LYS A 1180 ? 0.3036 0.3159 0.3443 0.0428  -0.0581 -0.1151 1178 LYS A CA  
8680  C C   . LYS A 1180 ? 0.2712 0.2750 0.3179 0.0386  -0.0581 -0.1092 1178 LYS A C   
8681  O O   . LYS A 1180 ? 0.2871 0.2859 0.3378 0.0375  -0.0578 -0.1074 1178 LYS A O   
8682  C CB  . LYS A 1180 ? 0.3204 0.3349 0.3672 0.0449  -0.0630 -0.1237 1178 LYS A CB  
8683  C CG  . LYS A 1180 ? 0.3429 0.3662 0.3847 0.0493  -0.0634 -0.1306 1178 LYS A CG  
8684  C CD  . LYS A 1180 ? 0.3395 0.3665 0.3861 0.0515  -0.0682 -0.1391 1178 LYS A CD  
8685  C CE  . LYS A 1180 ? 0.4392 0.4594 0.4982 0.0509  -0.0727 -0.1435 1178 LYS A CE  
8686  N NZ  . LYS A 1180 ? 0.5009 0.5247 0.5649 0.0531  -0.0776 -0.1523 1178 LYS A NZ  
8687  N N   . ALA A 1181 ? 0.2717 0.2744 0.3192 0.0363  -0.0583 -0.1059 1179 ALA A N   
8688  C CA  . ALA A 1181 ? 0.2807 0.2765 0.3335 0.0324  -0.0580 -0.1000 1179 ALA A CA  
8689  C C   . ALA A 1181 ? 0.2796 0.2734 0.3273 0.0308  -0.0536 -0.0929 1179 ALA A C   
8690  O O   . ALA A 1181 ? 0.2683 0.2566 0.3207 0.0283  -0.0533 -0.0893 1179 ALA A O   
8691  C CB  . ALA A 1181 ? 0.2578 0.2538 0.3117 0.0305  -0.0589 -0.0980 1179 ALA A CB  
8692  N N   . ILE A 1182 ? 0.2565 0.2550 0.2948 0.0320  -0.0501 -0.0909 1180 ILE A N   
8693  C CA  . ILE A 1182 ? 0.2647 0.2615 0.2983 0.0307  -0.0460 -0.0846 1180 ILE A CA  
8694  C C   . ILE A 1182 ? 0.2732 0.2681 0.3081 0.0317  -0.0456 -0.0858 1180 ILE A C   
8695  O O   . ILE A 1182 ? 0.2683 0.2587 0.3046 0.0295  -0.0440 -0.0812 1180 ILE A O   
8696  C CB  . ILE A 1182 ? 0.2527 0.2550 0.2768 0.0319  -0.0427 -0.0822 1180 ILE A CB  
8697  C CG1 . ILE A 1182 ? 0.2495 0.2526 0.2729 0.0303  -0.0427 -0.0795 1180 ILE A CG1 
8698  C CG2 . ILE A 1182 ? 0.2714 0.2725 0.2908 0.0312  -0.0388 -0.0769 1180 ILE A CG2 
8699  C CD1 . ILE A 1182 ? 0.2901 0.2987 0.3051 0.0315  -0.0401 -0.0773 1180 ILE A CD1 
8700  N N   . ALA A 1183 ? 0.2533 0.2519 0.2878 0.0349  -0.0472 -0.0921 1181 ALA A N   
8701  C CA  . ALA A 1183 ? 0.2676 0.2647 0.3034 0.0361  -0.0469 -0.0937 1181 ALA A CA  
8702  C C   . ALA A 1183 ? 0.2983 0.2883 0.3439 0.0340  -0.0495 -0.0934 1181 ALA A C   
8703  O O   . ALA A 1183 ? 0.2974 0.2843 0.3445 0.0335  -0.0485 -0.0915 1181 ALA A O   
8704  C CB  . ALA A 1183 ? 0.2905 0.2937 0.3249 0.0402  -0.0485 -0.1013 1181 ALA A CB  
8705  N N   . ALA A 1184 ? 0.2643 0.2518 0.3169 0.0326  -0.0528 -0.0947 1182 ALA A N   
8706  C CA  . ALA A 1184 ? 0.2842 0.2652 0.3471 0.0304  -0.0556 -0.0941 1182 ALA A CA  
8707  C C   . ALA A 1184 ? 0.2995 0.2760 0.3631 0.0264  -0.0534 -0.0858 1182 ALA A C   
8708  O O   . ALA A 1184 ? 0.2847 0.2561 0.3563 0.0243  -0.0552 -0.0840 1182 ALA A O   
8709  C CB  . ALA A 1184 ? 0.2862 0.2664 0.3571 0.0302  -0.0603 -0.0986 1182 ALA A CB  
8710  N N   . LEU A 1185 ? 0.2572 0.2357 0.3130 0.0254  -0.0496 -0.0809 1183 LEU A N   
8711  C CA  . LEU A 1185 ? 0.2650 0.2401 0.3212 0.0219  -0.0474 -0.0735 1183 LEU A CA  
8712  C C   . LEU A 1185 ? 0.2849 0.2573 0.3415 0.0215  -0.0459 -0.0709 1183 LEU A C   
8713  O O   . LEU A 1185 ? 0.2912 0.2656 0.3431 0.0239  -0.0444 -0.0731 1183 LEU A O   
8714  C CB  . LEU A 1185 ? 0.2315 0.2098 0.2794 0.0213  -0.0437 -0.0693 1183 LEU A CB  
8715  C CG  . LEU A 1185 ? 0.2627 0.2440 0.3097 0.0216  -0.0449 -0.0711 1183 LEU A CG  
8716  C CD1 . LEU A 1185 ? 0.2549 0.2392 0.2938 0.0213  -0.0412 -0.0670 1183 LEU A CD1 
8717  C CD2 . LEU A 1185 ? 0.2821 0.2602 0.3377 0.0189  -0.0478 -0.0701 1183 LEU A CD2 
8718  N N   . PRO A 1186 ? 0.2923 0.2603 0.3544 0.0183  -0.0461 -0.0662 1184 PRO A N   
8719  C CA  . PRO A 1186 ? 0.2828 0.2482 0.3453 0.0178  -0.0447 -0.0634 1184 PRO A CA  
8720  C C   . PRO A 1186 ? 0.2534 0.2211 0.3063 0.0179  -0.0400 -0.0596 1184 PRO A C   
8721  O O   . PRO A 1186 ? 0.2879 0.2579 0.3355 0.0172  -0.0378 -0.0570 1184 PRO A O   
8722  C CB  . PRO A 1186 ? 0.3295 0.2909 0.3996 0.0140  -0.0460 -0.0583 1184 PRO A CB  
8723  C CG  . PRO A 1186 ? 0.3891 0.3520 0.4585 0.0122  -0.0458 -0.0563 1184 PRO A CG  
8724  C CD  . PRO A 1186 ? 0.2936 0.2597 0.3611 0.0151  -0.0474 -0.0626 1184 PRO A CD  
8725  N N   . GLY A 1187 ? 0.2563 0.2233 0.3074 0.0190  -0.0387 -0.0594 1185 GLY A N   
8726  C CA  . GLY A 1187 ? 0.3231 0.2913 0.3669 0.0186  -0.0345 -0.0550 1185 GLY A CA  
8727  C C   . GLY A 1187 ? 0.2660 0.2387 0.3017 0.0216  -0.0324 -0.0576 1185 GLY A C   
8728  O O   . GLY A 1187 ? 0.2847 0.2592 0.3203 0.0244  -0.0335 -0.0625 1185 GLY A O   
8729  N N   . PRO A 1188 ? 0.2549 0.2299 0.2840 0.0211  -0.0293 -0.0541 1186 PRO A N   
8730  C CA  . PRO A 1188 ? 0.2370 0.2163 0.2586 0.0235  -0.0269 -0.0550 1186 PRO A CA  
8731  C C   . PRO A 1188 ? 0.2403 0.2241 0.2600 0.0262  -0.0284 -0.0601 1186 PRO A C   
8732  O O   . PRO A 1188 ? 0.2455 0.2296 0.2678 0.0258  -0.0305 -0.0618 1186 PRO A O   
8733  C CB  . PRO A 1188 ? 0.2880 0.2679 0.3046 0.0218  -0.0237 -0.0496 1186 PRO A CB  
8734  C CG  . PRO A 1188 ? 0.2943 0.2724 0.3149 0.0194  -0.0250 -0.0479 1186 PRO A CG  
8735  C CD  . PRO A 1188 ? 0.2706 0.2448 0.2992 0.0182  -0.0280 -0.0492 1186 PRO A CD  
8736  N N   . LEU A 1189 ? 0.2383 0.2260 0.2535 0.0290  -0.0274 -0.0626 1187 LEU A N   
8737  C CA  . LEU A 1189 ? 0.2377 0.2312 0.2493 0.0315  -0.0280 -0.0664 1187 LEU A CA  
8738  C C   . LEU A 1189 ? 0.2397 0.2354 0.2463 0.0305  -0.0260 -0.0625 1187 LEU A C   
8739  O O   . LEU A 1189 ? 0.2834 0.2782 0.2868 0.0292  -0.0231 -0.0575 1187 LEU A O   
8740  C CB  . LEU A 1189 ? 0.2557 0.2539 0.2630 0.0345  -0.0267 -0.0688 1187 LEU A CB  
8741  C CG  . LEU A 1189 ? 0.2622 0.2603 0.2741 0.0366  -0.0293 -0.0749 1187 LEU A CG  
8742  C CD1 . LEU A 1189 ? 0.2874 0.2793 0.3049 0.0350  -0.0297 -0.0732 1187 LEU A CD1 
8743  C CD2 . LEU A 1189 ? 0.3363 0.3412 0.3431 0.0400  -0.0281 -0.0779 1187 LEU A CD2 
8744  N N   . LEU A 1190 ? 0.2373 0.2356 0.2439 0.0311  -0.0277 -0.0649 1188 LEU A N   
8745  C CA  . LEU A 1190 ? 0.2530 0.2534 0.2557 0.0303  -0.0262 -0.0616 1188 LEU A CA  
8746  C C   . LEU A 1190 ? 0.2230 0.2305 0.2195 0.0330  -0.0253 -0.0630 1188 LEU A C   
8747  O O   . LEU A 1190 ? 0.2646 0.2761 0.2611 0.0355  -0.0272 -0.0683 1188 LEU A O   
8748  C CB  . LEU A 1190 ? 0.2632 0.2622 0.2701 0.0289  -0.0286 -0.0626 1188 LEU A CB  
8749  C CG  . LEU A 1190 ? 0.2535 0.2463 0.2668 0.0260  -0.0296 -0.0605 1188 LEU A CG  
8750  C CD1 . LEU A 1190 ? 0.3240 0.3164 0.3404 0.0245  -0.0313 -0.0604 1188 LEU A CD1 
8751  C CD2 . LEU A 1190 ? 0.2691 0.2592 0.2806 0.0239  -0.0264 -0.0547 1188 LEU A CD2 
8752  N N   . LEU A 1191 ? 0.2354 0.2447 0.2269 0.0326  -0.0225 -0.0583 1189 LEU A N   
8753  C CA  . LEU A 1191 ? 0.2337 0.2501 0.2197 0.0347  -0.0217 -0.0584 1189 LEU A CA  
8754  C C   . LEU A 1191 ? 0.2297 0.2479 0.2162 0.0346  -0.0234 -0.0594 1189 LEU A C   
8755  O O   . LEU A 1191 ? 0.2425 0.2584 0.2293 0.0326  -0.0226 -0.0556 1189 LEU A O   
8756  C CB  . LEU A 1191 ? 0.2408 0.2579 0.2225 0.0341  -0.0184 -0.0527 1189 LEU A CB  
8757  C CG  . LEU A 1191 ? 0.2311 0.2557 0.2072 0.0364  -0.0171 -0.0521 1189 LEU A CG  
8758  C CD1 . LEU A 1191 ? 0.2417 0.2657 0.2151 0.0356  -0.0141 -0.0465 1189 LEU A CD1 
8759  C CD2 . LEU A 1191 ? 0.2598 0.2891 0.2338 0.0370  -0.0181 -0.0521 1189 LEU A CD2 
8760  N N   . VAL A 1192 ? 0.2316 0.2542 0.2182 0.0367  -0.0258 -0.0647 1190 VAL A N   
8761  C CA  . VAL A 1192 ? 0.2121 0.2367 0.1997 0.0368  -0.0280 -0.0665 1190 VAL A CA  
8762  C C   . VAL A 1192 ? 0.2236 0.2560 0.2053 0.0386  -0.0271 -0.0656 1190 VAL A C   
8763  O O   . VAL A 1192 ? 0.2550 0.2931 0.2329 0.0410  -0.0265 -0.0673 1190 VAL A O   
8764  C CB  . VAL A 1192 ? 0.2735 0.2982 0.2658 0.0380  -0.0316 -0.0734 1190 VAL A CB  
8765  C CG1 . VAL A 1192 ? 0.2786 0.3056 0.2720 0.0381  -0.0340 -0.0755 1190 VAL A CG1 
8766  C CG2 . VAL A 1192 ? 0.2881 0.3051 0.2870 0.0360  -0.0326 -0.0738 1190 VAL A CG2 
8767  N N   . GLN A 1193 ? 0.2248 0.2579 0.2057 0.0376  -0.0271 -0.0628 1191 GLN A N   
8768  C CA  . GLN A 1193 ? 0.2080 0.2486 0.1841 0.0393  -0.0270 -0.0621 1191 GLN A CA  
8769  C C   . GLN A 1193 ? 0.2177 0.2598 0.1961 0.0394  -0.0299 -0.0654 1191 GLN A C   
8770  O O   . GLN A 1193 ? 0.2329 0.2698 0.2154 0.0373  -0.0307 -0.0645 1191 GLN A O   
8771  C CB  . GLN A 1193 ? 0.1985 0.2390 0.1720 0.0380  -0.0244 -0.0553 1191 GLN A CB  
8772  C CG  . GLN A 1193 ? 0.2598 0.2987 0.2315 0.0376  -0.0216 -0.0516 1191 GLN A CG  
8773  C CD  . GLN A 1193 ? 0.2437 0.2840 0.2126 0.0369  -0.0194 -0.0454 1191 GLN A CD  
8774  O OE1 . GLN A 1193 ? 0.2626 0.3098 0.2277 0.0384  -0.0192 -0.0440 1191 GLN A OE1 
8775  N NE2 . GLN A 1193 ? 0.2429 0.2771 0.2140 0.0345  -0.0180 -0.0416 1191 GLN A NE2 
8776  N N   . ALA A 1194 ? 0.2020 0.2517 0.1777 0.0420  -0.0315 -0.0692 1192 ALA A N   
8777  C CA  . ALA A 1194 ? 0.2056 0.2575 0.1832 0.0425  -0.0345 -0.0731 1192 ALA A CA  
8778  C C   . ALA A 1194 ? 0.2145 0.2745 0.1871 0.0438  -0.0343 -0.0711 1192 ALA A C   
8779  O O   . ALA A 1194 ? 0.2377 0.3038 0.2053 0.0453  -0.0326 -0.0690 1192 ALA A O   
8780  C CB  . ALA A 1194 ? 0.2260 0.2800 0.2061 0.0445  -0.0374 -0.0808 1192 ALA A CB  
8781  N N   . ALA A 1195 ? 0.2123 0.2728 0.1867 0.0433  -0.0363 -0.0718 1193 ALA A N   
8782  C CA  . ALA A 1195 ? 0.2211 0.2895 0.1914 0.0445  -0.0367 -0.0703 1193 ALA A CA  
8783  C C   . ALA A 1195 ? 0.2200 0.2893 0.1934 0.0447  -0.0400 -0.0746 1193 ALA A C   
8784  O O   . ALA A 1195 ? 0.2409 0.3034 0.2199 0.0429  -0.0414 -0.0761 1193 ALA A O   
8785  C CB  . ALA A 1195 ? 0.2399 0.3068 0.2086 0.0428  -0.0342 -0.0626 1193 ALA A CB  
8786  N N   . SER A 1196 ? 0.2262 0.3043 0.1961 0.0467  -0.0414 -0.0763 1194 SER A N   
8787  C CA  . SER A 1196 ? 0.2479 0.3274 0.2204 0.0468  -0.0445 -0.0795 1194 SER A CA  
8788  C C   . SER A 1196 ? 0.2341 0.3113 0.2071 0.0447  -0.0437 -0.0735 1194 SER A C   
8789  O O   . SER A 1196 ? 0.2329 0.3095 0.2035 0.0438  -0.0409 -0.0672 1194 SER A O   
8790  C CB  . SER A 1196 ? 0.2857 0.3763 0.2540 0.0498  -0.0464 -0.0835 1194 SER A CB  
8791  O OG  . SER A 1196 ? 0.2674 0.3645 0.2300 0.0504  -0.0444 -0.0778 1194 SER A OG  
8792  N N   . SER A 1197 ? 0.2436 0.3197 0.2204 0.0440  -0.0463 -0.0757 1195 SER A N   
8793  C CA  . SER A 1197 ? 0.2591 0.3341 0.2364 0.0424  -0.0458 -0.0706 1195 SER A CA  
8794  C C   . SER A 1197 ? 0.2353 0.3186 0.2069 0.0438  -0.0448 -0.0666 1195 SER A C   
8795  O O   . SER A 1197 ? 0.2511 0.3331 0.2220 0.0426  -0.0429 -0.0603 1195 SER A O   
8796  C CB  . SER A 1197 ? 0.2625 0.3365 0.2445 0.0417  -0.0490 -0.0742 1195 SER A CB  
8797  O OG  . SER A 1197 ? 0.2825 0.3491 0.2705 0.0402  -0.0501 -0.0774 1195 SER A OG  
8798  N N   . GLY A 1198 ? 0.2574 0.3498 0.2252 0.0465  -0.0463 -0.0702 1196 GLY A N   
8799  C CA  . GLY A 1198 ? 0.2765 0.3777 0.2388 0.0479  -0.0455 -0.0661 1196 GLY A CA  
8800  C C   . GLY A 1198 ? 0.3008 0.4021 0.2599 0.0477  -0.0421 -0.0604 1196 GLY A C   
8801  O O   . GLY A 1198 ? 0.2818 0.3858 0.2389 0.0473  -0.0408 -0.0540 1196 GLY A O   
8802  N N   . GLU A 1199 ? 0.2588 0.3570 0.2178 0.0479  -0.0408 -0.0625 1197 GLU A N   
8803  C CA  . GLU A 1199 ? 0.2854 0.3831 0.2419 0.0476  -0.0376 -0.0572 1197 GLU A CA  
8804  C C   . GLU A 1199 ? 0.2773 0.3668 0.2367 0.0449  -0.0357 -0.0511 1197 GLU A C   
8805  O O   . GLU A 1199 ? 0.2710 0.3619 0.2284 0.0445  -0.0336 -0.0449 1197 GLU A O   
8806  C CB  . GLU A 1199 ? 0.2449 0.3400 0.2015 0.0483  -0.0369 -0.0613 1197 GLU A CB  
8807  C CG  . GLU A 1199 ? 0.3240 0.4199 0.2777 0.0484  -0.0338 -0.0570 1197 GLU A CG  
8808  C CD  . GLU A 1199 ? 0.4440 0.5387 0.3978 0.0495  -0.0335 -0.0619 1197 GLU A CD  
8809  O OE1 . GLU A 1199 ? 0.4117 0.5056 0.3681 0.0503  -0.0359 -0.0689 1197 GLU A OE1 
8810  O OE2 . GLU A 1199 ? 0.5660 0.6607 0.5179 0.0495  -0.0310 -0.0590 1197 GLU A OE2 
8811  N N   . ILE A 1200 ? 0.2519 0.3330 0.2162 0.0430  -0.0364 -0.0528 1198 ILE A N   
8812  C CA  . ILE A 1200 ? 0.2642 0.3384 0.2316 0.0406  -0.0347 -0.0477 1198 ILE A CA  
8813  C C   . ILE A 1200 ? 0.2865 0.3647 0.2531 0.0405  -0.0350 -0.0430 1198 ILE A C   
8814  O O   . ILE A 1200 ? 0.2763 0.3525 0.2431 0.0395  -0.0331 -0.0373 1198 ILE A O   
8815  C CB  . ILE A 1200 ? 0.2428 0.3089 0.2157 0.0386  -0.0357 -0.0506 1198 ILE A CB  
8816  C CG1 . ILE A 1200 ? 0.2509 0.3123 0.2251 0.0384  -0.0351 -0.0537 1198 ILE A CG1 
8817  C CG2 . ILE A 1200 ? 0.2622 0.3227 0.2382 0.0363  -0.0344 -0.0457 1198 ILE A CG2 
8818  C CD1 . ILE A 1200 ? 0.2644 0.3189 0.2443 0.0366  -0.0365 -0.0568 1198 ILE A CD1 
8819  N N   . ALA A 1201 ? 0.2576 0.3416 0.2234 0.0417  -0.0376 -0.0456 1199 ALA A N   
8820  C CA  . ALA A 1201 ? 0.2783 0.3664 0.2437 0.0417  -0.0382 -0.0412 1199 ALA A CA  
8821  C C   . ALA A 1201 ? 0.2974 0.3927 0.2583 0.0430  -0.0368 -0.0362 1199 ALA A C   
8822  O O   . ALA A 1201 ? 0.2963 0.3920 0.2578 0.0423  -0.0360 -0.0302 1199 ALA A O   
8823  C CB  . ALA A 1201 ? 0.3015 0.3945 0.2672 0.0427  -0.0414 -0.0454 1199 ALA A CB  
8824  N N   . ARG A 1202 ? 0.2590 0.3603 0.2157 0.0448  -0.0366 -0.0385 1200 ARG A N   
8825  C CA  . ARG A 1202 ? 0.2783 0.3882 0.2306 0.0462  -0.0356 -0.0339 1200 ARG A CA  
8826  C C   . ARG A 1202 ? 0.3097 0.4160 0.2616 0.0452  -0.0325 -0.0289 1200 ARG A C   
8827  O O   . ARG A 1202 ? 0.3088 0.4191 0.2596 0.0452  -0.0315 -0.0225 1200 ARG A O   
8828  C CB  . ARG A 1202 ? 0.2575 0.3769 0.2052 0.0488  -0.0367 -0.0388 1200 ARG A CB  
8829  C CG  . ARG A 1202 ? 0.2659 0.3915 0.2131 0.0501  -0.0399 -0.0429 1200 ARG A CG  
8830  C CD  . ARG A 1202 ? 0.2970 0.4334 0.2393 0.0529  -0.0409 -0.0476 1200 ARG A CD  
8831  N NE  . ARG A 1202 ? 0.3305 0.4635 0.2733 0.0535  -0.0405 -0.0536 1200 ARG A NE  
8832  C CZ  . ARG A 1202 ? 0.3221 0.4530 0.2672 0.0542  -0.0428 -0.0615 1200 ARG A CZ  
8833  N NH1 . ARG A 1202 ? 0.2933 0.4261 0.2400 0.0545  -0.0457 -0.0648 1200 ARG A NH1 
8834  N NH2 . ARG A 1202 ? 0.3590 0.4857 0.3054 0.0545  -0.0423 -0.0661 1200 ARG A NH2 
8835  N N   . ASN A 1203 ? 0.2731 0.3723 0.2265 0.0445  -0.0312 -0.0316 1201 ASN A N   
8836  C CA  . ASN A 1203 ? 0.2818 0.3788 0.2344 0.0440  -0.0285 -0.0278 1201 ASN A CA  
8837  C C   . ASN A 1203 ? 0.3448 0.4310 0.3019 0.0416  -0.0270 -0.0258 1201 ASN A C   
8838  O O   . ASN A 1203 ? 0.3063 0.3858 0.2657 0.0407  -0.0272 -0.0301 1201 ASN A O   
8839  C CB  . ASN A 1203 ? 0.2899 0.3890 0.2399 0.0454  -0.0280 -0.0327 1201 ASN A CB  
8840  C CG  . ASN A 1203 ? 0.3337 0.4312 0.2827 0.0450  -0.0252 -0.0290 1201 ASN A CG  
8841  O OD1 . ASN A 1203 ? 0.3503 0.4456 0.3004 0.0438  -0.0237 -0.0226 1201 ASN A OD1 
8842  N ND2 . ASN A 1203 ? 0.3683 0.4670 0.3155 0.0462  -0.0246 -0.0330 1201 ASN A ND2 
8843  N N   . PRO A 1204 ? 0.3162 0.4006 0.2747 0.0404  -0.0257 -0.0195 1202 PRO A N   
8844  C CA  . PRO A 1204 ? 0.3678 0.4425 0.3304 0.0383  -0.0243 -0.0179 1202 PRO A CA  
8845  C C   . PRO A 1204 ? 0.3427 0.4127 0.3050 0.0379  -0.0225 -0.0197 1202 PRO A C   
8846  O O   . PRO A 1204 ? 0.3373 0.3995 0.3029 0.0362  -0.0217 -0.0204 1202 PRO A O   
8847  C CB  . PRO A 1204 ? 0.4126 0.4883 0.3765 0.0377  -0.0234 -0.0107 1202 PRO A CB  
8848  C CG  . PRO A 1204 ? 0.4422 0.5271 0.4037 0.0392  -0.0250 -0.0088 1202 PRO A CG  
8849  C CD  . PRO A 1204 ? 0.3616 0.4529 0.3186 0.0410  -0.0256 -0.0134 1202 PRO A CD  
8850  N N   . ASP A 1205 ? 0.3342 0.4092 0.2927 0.0394  -0.0218 -0.0205 1203 ASP A N   
8851  C CA  . ASP A 1205 ? 0.3262 0.3974 0.2844 0.0392  -0.0202 -0.0223 1203 ASP A CA  
8852  C C   . ASP A 1205 ? 0.3299 0.4017 0.2873 0.0403  -0.0215 -0.0294 1203 ASP A C   
8853  O O   . ASP A 1205 ? 0.3726 0.4447 0.3286 0.0410  -0.0205 -0.0313 1203 ASP A O   
8854  C CB  . ASP A 1205 ? 0.4020 0.4780 0.3572 0.0400  -0.0183 -0.0182 1203 ASP A CB  
8855  C CG  . ASP A 1205 ? 0.4334 0.5081 0.3905 0.0388  -0.0172 -0.0111 1203 ASP A CG  
8856  O OD1 . ASP A 1205 ? 0.4079 0.4760 0.3688 0.0371  -0.0172 -0.0100 1203 ASP A OD1 
8857  O OD2 . ASP A 1205 ? 0.5085 0.5890 0.4635 0.0395  -0.0163 -0.0068 1203 ASP A OD2 
8858  N N   . ALA A 1206 ? 0.2871 0.3593 0.2458 0.0405  -0.0238 -0.0333 1204 ALA A N   
8859  C CA  . ALA A 1206 ? 0.2860 0.3582 0.2451 0.0415  -0.0255 -0.0403 1204 ALA A CA  
8860  C C   . ALA A 1206 ? 0.2869 0.3513 0.2486 0.0403  -0.0244 -0.0421 1204 ALA A C   
8861  O O   . ALA A 1206 ? 0.3186 0.3840 0.2795 0.0416  -0.0247 -0.0463 1204 ALA A O   
8862  C CB  . ALA A 1206 ? 0.2795 0.3508 0.2413 0.0411  -0.0281 -0.0434 1204 ALA A CB  
8863  N N   . TYR A 1207 ? 0.2714 0.3282 0.2363 0.0380  -0.0233 -0.0391 1205 TYR A N   
8864  C CA  . TYR A 1207 ? 0.2772 0.3270 0.2442 0.0367  -0.0218 -0.0393 1205 TYR A CA  
8865  C C   . TYR A 1207 ? 0.2806 0.3297 0.2461 0.0361  -0.0191 -0.0337 1205 TYR A C   
8866  O O   . TYR A 1207 ? 0.3522 0.4001 0.3187 0.0350  -0.0184 -0.0293 1205 TYR A O   
8867  C CB  . TYR A 1207 ? 0.2447 0.2872 0.2166 0.0345  -0.0225 -0.0400 1205 TYR A CB  
8868  C CG  . TYR A 1207 ? 0.2368 0.2796 0.2111 0.0348  -0.0253 -0.0452 1205 TYR A CG  
8869  C CD1 . TYR A 1207 ? 0.2455 0.2890 0.2202 0.0360  -0.0268 -0.0506 1205 TYR A CD1 
8870  C CD2 . TYR A 1207 ? 0.2457 0.2881 0.2222 0.0339  -0.0267 -0.0449 1205 TYR A CD2 
8871  C CE1 . TYR A 1207 ? 0.2207 0.2643 0.1983 0.0363  -0.0297 -0.0555 1205 TYR A CE1 
8872  C CE2 . TYR A 1207 ? 0.2671 0.3099 0.2463 0.0341  -0.0295 -0.0497 1205 TYR A CE2 
8873  C CZ  . TYR A 1207 ? 0.2410 0.2842 0.2207 0.0353  -0.0310 -0.0549 1205 TYR A CZ  
8874  O OH  . TYR A 1207 ? 0.2446 0.2879 0.2276 0.0355  -0.0340 -0.0598 1205 TYR A OH  
8875  N N   . CYS A 1208 ? 0.2419 0.2917 0.2055 0.0369  -0.0178 -0.0340 1206 CYS A N   
8876  C CA  . CYS A 1208 ? 0.2458 0.2957 0.2081 0.0365  -0.0154 -0.0289 1206 CYS A CA  
8877  C C   . CYS A 1208 ? 0.2384 0.2799 0.2039 0.0343  -0.0140 -0.0273 1206 CYS A C   
8878  O O   . CYS A 1208 ? 0.2313 0.2683 0.1986 0.0338  -0.0141 -0.0304 1206 CYS A O   
8879  C CB  . CYS A 1208 ? 0.2804 0.3353 0.2393 0.0384  -0.0146 -0.0301 1206 CYS A CB  
8880  S SG  . CYS A 1208 ? 0.3373 0.3927 0.2948 0.0380  -0.0117 -0.0240 1206 CYS A SG  
8881  N N   . LEU A 1209 ? 0.2085 0.2481 0.1750 0.0331  -0.0128 -0.0224 1207 LEU A N   
8882  C CA  . LEU A 1209 ? 0.2104 0.2429 0.1800 0.0311  -0.0115 -0.0208 1207 LEU A CA  
8883  C C   . LEU A 1209 ? 0.2163 0.2468 0.1851 0.0310  -0.0097 -0.0201 1207 LEU A C   
8884  O O   . LEU A 1209 ? 0.2279 0.2526 0.1990 0.0294  -0.0088 -0.0200 1207 LEU A O   
8885  C CB  . LEU A 1209 ? 0.2218 0.2533 0.1933 0.0301  -0.0109 -0.0163 1207 LEU A CB  
8886  C CG  . LEU A 1209 ? 0.2140 0.2473 0.1867 0.0301  -0.0127 -0.0167 1207 LEU A CG  
8887  C CD1 . LEU A 1209 ? 0.2391 0.2708 0.2143 0.0291  -0.0121 -0.0124 1207 LEU A CD1 
8888  C CD2 . LEU A 1209 ? 0.2535 0.2832 0.2285 0.0292  -0.0140 -0.0209 1207 LEU A CD2 
8889  N N   . ASN A 1210 ? 0.2373 0.2730 0.2029 0.0326  -0.0091 -0.0196 1208 ASN A N   
8890  C CA  . ASN A 1210 ? 0.2435 0.2777 0.2084 0.0327  -0.0075 -0.0192 1208 ASN A CA  
8891  C C   . ASN A 1210 ? 0.2422 0.2715 0.2088 0.0321  -0.0079 -0.0235 1208 ASN A C   
8892  O O   . ASN A 1210 ? 0.2656 0.2906 0.2333 0.0311  -0.0066 -0.0227 1208 ASN A O   
8893  C CB  . ASN A 1210 ? 0.2751 0.3166 0.2362 0.0348  -0.0071 -0.0191 1208 ASN A CB  
8894  C CG  . ASN A 1210 ? 0.2969 0.3437 0.2564 0.0352  -0.0064 -0.0138 1208 ASN A CG  
8895  O OD1 . ASN A 1210 ? 0.4042 0.4496 0.3656 0.0341  -0.0066 -0.0106 1208 ASN A OD1 
8896  N ND2 . ASN A 1210 ? 0.4093 0.4629 0.3658 0.0368  -0.0057 -0.0128 1208 ASN A ND2 
8897  N N   . TRP A 1211 ? 0.2388 0.2689 0.2059 0.0328  -0.0099 -0.0280 1209 TRP A N   
8898  C CA  . TRP A 1211 ? 0.2345 0.2608 0.2038 0.0325  -0.0108 -0.0322 1209 TRP A CA  
8899  C C   . TRP A 1211 ? 0.2368 0.2567 0.2101 0.0303  -0.0115 -0.0325 1209 TRP A C   
8900  O O   . TRP A 1211 ? 0.2839 0.3004 0.2598 0.0298  -0.0125 -0.0356 1209 TRP A O   
8901  C CB  . TRP A 1211 ? 0.2495 0.2803 0.2177 0.0346  -0.0128 -0.0374 1209 TRP A CB  
8902  C CG  . TRP A 1211 ? 0.2551 0.2942 0.2190 0.0369  -0.0124 -0.0368 1209 TRP A CG  
8903  C CD1 . TRP A 1211 ? 0.2478 0.2934 0.2095 0.0385  -0.0138 -0.0384 1209 TRP A CD1 
8904  C CD2 . TRP A 1211 ? 0.2377 0.2797 0.1989 0.0377  -0.0103 -0.0342 1209 TRP A CD2 
8905  N NE1 . TRP A 1211 ? 0.2750 0.3281 0.2328 0.0403  -0.0127 -0.0367 1209 TRP A NE1 
8906  C CE2 . TRP A 1211 ? 0.2512 0.3021 0.2087 0.0398  -0.0106 -0.0340 1209 TRP A CE2 
8907  C CE3 . TRP A 1211 ? 0.2474 0.2859 0.2091 0.0368  -0.0083 -0.0317 1209 TRP A CE3 
8908  C CZ2 . TRP A 1211 ? 0.2699 0.3263 0.2243 0.0409  -0.0088 -0.0313 1209 TRP A CZ2 
8909  C CZ3 . TRP A 1211 ? 0.2734 0.3170 0.2321 0.0380  -0.0067 -0.0293 1209 TRP A CZ3 
8910  C CH2 . TRP A 1211 ? 0.2768 0.3293 0.2321 0.0400  -0.0069 -0.0290 1209 TRP A CH2 
8911  N N   . LEU A 1212 ? 0.2108 0.2294 0.1851 0.0290  -0.0110 -0.0293 1210 LEU A N   
8912  C CA  . LEU A 1212 ? 0.2145 0.2282 0.1925 0.0269  -0.0113 -0.0292 1210 LEU A CA  
8913  C C   . LEU A 1212 ? 0.1983 0.2079 0.1773 0.0252  -0.0093 -0.0256 1210 LEU A C   
8914  O O   . LEU A 1212 ? 0.1954 0.2015 0.1773 0.0234  -0.0093 -0.0251 1210 LEU A O   
8915  C CB  . LEU A 1212 ? 0.1940 0.2094 0.1727 0.0267  -0.0126 -0.0289 1210 LEU A CB  
8916  C CG  . LEU A 1212 ? 0.2077 0.2259 0.1866 0.0279  -0.0150 -0.0332 1210 LEU A CG  
8917  C CD1 . LEU A 1212 ? 0.2216 0.2434 0.2000 0.0284  -0.0161 -0.0324 1210 LEU A CD1 
8918  C CD2 . LEU A 1212 ? 0.2514 0.2651 0.2346 0.0264  -0.0164 -0.0360 1210 LEU A CD2 
8919  N N   . VAL A 1213 ? 0.2015 0.2121 0.1784 0.0258  -0.0076 -0.0233 1211 VAL A N   
8920  C CA  . VAL A 1213 ? 0.2098 0.2168 0.1877 0.0244  -0.0058 -0.0206 1211 VAL A CA  
8921  C C   . VAL A 1213 ? 0.2098 0.2153 0.1871 0.0246  -0.0052 -0.0218 1211 VAL A C   
8922  O O   . VAL A 1213 ? 0.2216 0.2296 0.1973 0.0262  -0.0059 -0.0243 1211 VAL A O   
8923  C CB  . VAL A 1213 ? 0.2034 0.2119 0.1802 0.0246  -0.0044 -0.0165 1211 VAL A CB  
8924  C CG1 . VAL A 1213 ? 0.2218 0.2310 0.2001 0.0241  -0.0050 -0.0152 1211 VAL A CG1 
8925  C CG2 . VAL A 1213 ? 0.2397 0.2531 0.2132 0.0265  -0.0041 -0.0156 1211 VAL A CG2 
8926  N N   . GLU A 1214 ? 0.2103 0.2118 0.1891 0.0231  -0.0039 -0.0202 1212 GLU A N   
8927  C CA  . GLU A 1214 ? 0.2342 0.2338 0.2130 0.0231  -0.0033 -0.0209 1212 GLU A CA  
8928  C C   . GLU A 1214 ? 0.2025 0.2021 0.1799 0.0230  -0.0013 -0.0175 1212 GLU A C   
8929  O O   . GLU A 1214 ? 0.1980 0.1961 0.1766 0.0219  -0.0004 -0.0150 1212 GLU A O   
8930  C CB  . GLU A 1214 ? 0.2795 0.2746 0.2615 0.0211  -0.0036 -0.0215 1212 GLU A CB  
8931  C CG  . GLU A 1214 ? 0.3773 0.3701 0.3602 0.0209  -0.0034 -0.0224 1212 GLU A CG  
8932  C CD  . GLU A 1214 ? 0.4133 0.4025 0.3998 0.0190  -0.0044 -0.0231 1212 GLU A CD  
8933  O OE1 . GLU A 1214 ? 0.4463 0.4353 0.4349 0.0190  -0.0063 -0.0257 1212 GLU A OE1 
8934  O OE2 . GLU A 1214 ? 0.4596 0.4466 0.4472 0.0173  -0.0032 -0.0208 1212 GLU A OE2 
8935  N N   . GLU A 1215 ? 0.2077 0.2093 0.1832 0.0243  -0.0006 -0.0175 1213 GLU A N   
8936  C CA  . GLU A 1215 ? 0.1952 0.1968 0.1699 0.0242  0.0012  -0.0144 1213 GLU A CA  
8937  C C   . GLU A 1215 ? 0.1932 0.1904 0.1696 0.0228  0.0019  -0.0143 1213 GLU A C   
8938  O O   . GLU A 1215 ? 0.2092 0.2047 0.1865 0.0227  0.0012  -0.0168 1213 GLU A O   
8939  C CB  . GLU A 1215 ? 0.1988 0.2048 0.1708 0.0262  0.0016  -0.0145 1213 GLU A CB  
8940  C CG  . GLU A 1215 ? 0.2037 0.2154 0.1735 0.0277  0.0009  -0.0142 1213 GLU A CG  
8941  C CD  . GLU A 1215 ? 0.1831 0.1999 0.1502 0.0298  0.0011  -0.0154 1213 GLU A CD  
8942  O OE1 . GLU A 1215 ? 0.2284 0.2459 0.1953 0.0308  0.0000  -0.0196 1213 GLU A OE1 
8943  O OE2 . GLU A 1215 ? 0.2229 0.2431 0.1885 0.0304  0.0023  -0.0122 1213 GLU A OE2 
8944  N N   . VAL A 1216 ? 0.1965 0.1920 0.1737 0.0217  0.0032  -0.0114 1214 VAL A N   
8945  C CA  . VAL A 1216 ? 0.2057 0.1977 0.1842 0.0205  0.0040  -0.0109 1214 VAL A CA  
8946  C C   . VAL A 1216 ? 0.1969 0.1897 0.1746 0.0208  0.0055  -0.0081 1214 VAL A C   
8947  O O   . VAL A 1216 ? 0.2177 0.2117 0.1955 0.0208  0.0060  -0.0058 1214 VAL A O   
8948  C CB  . VAL A 1216 ? 0.2038 0.1928 0.1846 0.0185  0.0040  -0.0106 1214 VAL A CB  
8949  C CG1 . VAL A 1216 ? 0.2189 0.2053 0.2008 0.0173  0.0049  -0.0098 1214 VAL A CG1 
8950  C CG2 . VAL A 1216 ? 0.2444 0.2329 0.2265 0.0181  0.0024  -0.0130 1214 VAL A CG2 
8951  N N   . SER A 1217 ? 0.1960 0.1882 0.1731 0.0211  0.0061  -0.0084 1215 SER A N   
8952  C CA  . SER A 1217 ? 0.2014 0.1939 0.1782 0.0211  0.0075  -0.0058 1215 SER A CA  
8953  C C   . SER A 1217 ? 0.1869 0.1756 0.1656 0.0195  0.0081  -0.0053 1215 SER A C   
8954  O O   . SER A 1217 ? 0.2039 0.1905 0.1834 0.0188  0.0075  -0.0071 1215 SER A O   
8955  C CB  . SER A 1217 ? 0.2116 0.2067 0.1866 0.0227  0.0078  -0.0065 1215 SER A CB  
8956  O OG  . SER A 1217 ? 0.2363 0.2310 0.2116 0.0225  0.0091  -0.0043 1215 SER A OG  
8957  N N   . ALA A 1218 ? 0.1784 0.1665 0.1581 0.0188  0.0090  -0.0029 1216 ALA A N   
8958  C CA  . ALA A 1218 ? 0.1912 0.1765 0.1724 0.0174  0.0096  -0.0024 1216 ALA A CA  
8959  C C   . ALA A 1218 ? 0.2086 0.1944 0.1899 0.0177  0.0106  -0.0001 1216 ALA A C   
8960  O O   . ALA A 1218 ? 0.2234 0.2107 0.2052 0.0181  0.0109  0.0019  1216 ALA A O   
8961  C CB  . ALA A 1218 ? 0.2042 0.1882 0.1873 0.0161  0.0094  -0.0023 1216 ALA A CB  
8962  N N   . SER A 1219 ? 0.1983 0.1828 0.1796 0.0174  0.0111  -0.0003 1217 SER A N   
8963  C CA  . SER A 1219 ? 0.2084 0.1932 0.1901 0.0175  0.0121  0.0018  1217 SER A CA  
8964  C C   . SER A 1219 ? 0.1838 0.1659 0.1672 0.0160  0.0124  0.0020  1217 SER A C   
8965  O O   . SER A 1219 ? 0.2074 0.1878 0.1908 0.0153  0.0122  0.0007  1217 SER A O   
8966  C CB  . SER A 1219 ? 0.2048 0.1910 0.1850 0.0187  0.0124  0.0013  1217 SER A CB  
8967  O OG  . SER A 1219 ? 0.2093 0.1961 0.1901 0.0187  0.0134  0.0036  1217 SER A OG  
8968  N N   . ILE A 1220 ? 0.1891 0.1711 0.1743 0.0155  0.0127  0.0036  1218 ILE A N   
8969  C CA  . ILE A 1220 ? 0.1831 0.1633 0.1701 0.0142  0.0129  0.0035  1218 ILE A CA  
8970  C C   . ILE A 1220 ? 0.1937 0.1738 0.1815 0.0143  0.0136  0.0053  1218 ILE A C   
8971  O O   . ILE A 1220 ? 0.1991 0.1804 0.1881 0.0148  0.0137  0.0072  1218 ILE A O   
8972  C CB  . ILE A 1220 ? 0.2384 0.2185 0.2273 0.0136  0.0125  0.0033  1218 ILE A CB  
8973  C CG1 . ILE A 1220 ? 0.2644 0.2449 0.2526 0.0136  0.0118  0.0018  1218 ILE A CG1 
8974  C CG2 . ILE A 1220 ? 0.2537 0.2327 0.2443 0.0124  0.0127  0.0028  1218 ILE A CG2 
8975  C CD1 . ILE A 1220 ? 0.3784 0.3594 0.3685 0.0135  0.0114  0.0016  1218 ILE A CD1 
8976  N N   . ASN A 1221 ? 0.1896 0.1685 0.1774 0.0136  0.0139  0.0049  1219 ASN A N   
8977  C CA  . ASN A 1221 ? 0.2093 0.1881 0.1983 0.0135  0.0144  0.0064  1219 ASN A CA  
8978  C C   . ASN A 1221 ? 0.1900 0.1681 0.1816 0.0126  0.0142  0.0065  1219 ASN A C   
8979  O O   . ASN A 1221 ? 0.2532 0.2305 0.2452 0.0115  0.0141  0.0052  1219 ASN A O   
8980  C CB  . ASN A 1221 ? 0.2248 0.2026 0.2128 0.0131  0.0146  0.0059  1219 ASN A CB  
8981  C CG  . ASN A 1221 ? 0.2169 0.1944 0.2063 0.0129  0.0151  0.0073  1219 ASN A CG  
8982  O OD1 . ASN A 1221 ? 0.2039 0.1821 0.1950 0.0131  0.0153  0.0088  1219 ASN A OD1 
8983  N ND2 . ASN A 1221 ? 0.2409 0.2176 0.2300 0.0123  0.0152  0.0069  1219 ASN A ND2 
8984  N N   . THR A 1222 ? 0.1955 0.1742 0.1892 0.0130  0.0141  0.0081  1220 THR A N   
8985  C CA  . THR A 1222 ? 0.2237 0.2018 0.2208 0.0123  0.0136  0.0078  1220 THR A CA  
8986  C C   . THR A 1222 ? 0.2690 0.2465 0.2680 0.0119  0.0138  0.0086  1220 THR A C   
8987  O O   . THR A 1222 ? 0.3148 0.2920 0.3172 0.0115  0.0132  0.0081  1220 THR A O   
8988  C CB  . THR A 1222 ? 0.2691 0.2479 0.2686 0.0130  0.0130  0.0091  1220 THR A CB  
8989  O OG1 . THR A 1222 ? 0.2576 0.2376 0.2575 0.0137  0.0133  0.0120  1220 THR A OG1 
8990  C CG2 . THR A 1222 ? 0.2645 0.2439 0.2622 0.0133  0.0127  0.0080  1220 THR A CG2 
8991  N N   . ALA A 1223 ? 0.2251 0.2027 0.2226 0.0121  0.0145  0.0097  1221 ALA A N   
8992  C CA  . ALA A 1223 ? 0.2875 0.2645 0.2864 0.0116  0.0146  0.0102  1221 ALA A CA  
8993  C C   . ALA A 1223 ? 0.3079 0.2842 0.3053 0.0107  0.0147  0.0085  1221 ALA A C   
8994  O O   . ALA A 1223 ? 0.3706 0.3466 0.3688 0.0102  0.0149  0.0088  1221 ALA A O   
8995  C CB  . ALA A 1223 ? 0.2723 0.2504 0.2709 0.0123  0.0153  0.0126  1221 ALA A CB  
8996  N N   . ALA A 1224 ? 0.3185 0.2948 0.3138 0.0104  0.0146  0.0068  1222 ALA A N   
8997  C CA  . ALA A 1224 ? 0.3635 0.3395 0.3573 0.0095  0.0146  0.0059  1222 ALA A CA  
8998  C C   . ALA A 1224 ? 0.4037 0.3802 0.3992 0.0084  0.0144  0.0050  1222 ALA A C   
8999  O O   . ALA A 1224 ? 0.4047 0.3812 0.3995 0.0077  0.0144  0.0051  1222 ALA A O   
9000  C CB  . ALA A 1224 ? 0.3563 0.3324 0.3483 0.0092  0.0144  0.0047  1222 ALA A CB  
9001  N N   . ALA A 1225 ? 0.3515 0.3285 0.3492 0.0084  0.0140  0.0041  1223 ALA A N   
9002  C CA  . ALA A 1225 ? 0.4294 0.4075 0.4289 0.0076  0.0136  0.0027  1223 ALA A CA  
9003  C C   . ALA A 1225 ? 0.4450 0.4226 0.4462 0.0076  0.0136  0.0037  1223 ALA A C   
9004  O O   . ALA A 1225 ? 0.4445 0.4231 0.4468 0.0069  0.0132  0.0025  1223 ALA A O   
9005  C CB  . ALA A 1225 ? 0.4288 0.4077 0.4308 0.0078  0.0130  0.0009  1223 ALA A CB  
9006  N N   . GLY A 1226 ? 0.3811 0.3575 0.3824 0.0083  0.0139  0.0058  1224 GLY A N   
9007  C CA  . GLY A 1226 ? 0.4151 0.3912 0.4182 0.0082  0.0140  0.0071  1224 GLY A CA  
9008  C C   . GLY A 1226 ? 0.4469 0.4226 0.4534 0.0088  0.0137  0.0088  1224 GLY A C   
9009  O O   . GLY A 1226 ? 0.3964 0.3720 0.4047 0.0088  0.0138  0.0103  1224 GLY A O   
9010  N N   . GLY A 1227 ? 0.3320 0.3077 0.3397 0.0093  0.0134  0.0088  1225 GLY A N   
9011  C CA  . GLY A 1227 ? 0.4065 0.3821 0.4180 0.0098  0.0130  0.0110  1225 GLY A CA  
9012  C C   . GLY A 1227 ? 0.3904 0.3663 0.4019 0.0105  0.0128  0.0115  1225 GLY A C   
9013  O O   . GLY A 1227 ? 0.3722 0.3483 0.3811 0.0105  0.0129  0.0098  1225 GLY A O   
9014  N N   . ASN A 1228 ? 0.3317 0.3078 0.3464 0.0109  0.0124  0.0142  1226 ASN A N   
9015  C CA  . ASN A 1228 ? 0.3327 0.3095 0.3479 0.0115  0.0121  0.0155  1226 ASN A CA  
9016  C C   . ASN A 1228 ? 0.3967 0.3727 0.4179 0.0114  0.0106  0.0151  1226 ASN A C   
9017  O O   . ASN A 1228 ? 0.3757 0.3514 0.4017 0.0112  0.0098  0.0171  1226 ASN A O   
9018  C CB  . ASN A 1228 ? 0.3595 0.3381 0.3742 0.0121  0.0128  0.0194  1226 ASN A CB  
9019  C CG  . ASN A 1228 ? 0.3941 0.3742 0.4085 0.0128  0.0126  0.0210  1226 ASN A CG  
9020  O OD1 . ASN A 1228 ? 0.4010 0.3804 0.4184 0.0128  0.0115  0.0205  1226 ASN A OD1 
9021  N ND2 . ASN A 1228 ? 0.4146 0.3971 0.4256 0.0135  0.0135  0.0229  1226 ASN A ND2 
9022  N N   . ALA A 1229 ? 0.3769 0.3526 0.3980 0.0115  0.0100  0.0125  1227 ALA A N   
9023  C CA  . ALA A 1229 ? 0.3670 0.3420 0.3941 0.0115  0.0085  0.0114  1227 ALA A CA  
9024  C C   . ALA A 1229 ? 0.3669 0.3421 0.3983 0.0119  0.0076  0.0152  1227 ALA A C   
9025  O O   . ALA A 1229 ? 0.4001 0.3745 0.4380 0.0118  0.0062  0.0160  1227 ALA A O   
9026  C CB  . ALA A 1229 ? 0.3739 0.3492 0.3998 0.0117  0.0082  0.0080  1227 ALA A CB  
9027  N N   . SER A 1230 ? 0.3920 0.3686 0.4202 0.0124  0.0083  0.0177  1228 SER A N   
9028  C CA  . SER A 1230 ? 0.4059 0.3835 0.4380 0.0128  0.0075  0.0218  1228 SER A CA  
9029  C C   . SER A 1230 ? 0.4531 0.4312 0.4886 0.0124  0.0074  0.0255  1228 SER A C   
9030  O O   . SER A 1230 ? 0.4263 0.4042 0.4684 0.0122  0.0059  0.0282  1228 SER A O   
9031  C CB  . SER A 1230 ? 0.4517 0.4315 0.4790 0.0134  0.0083  0.0235  1228 SER A CB  
9032  N N   . LEU A 1231 ? 0.3820 0.3608 0.4137 0.0122  0.0088  0.0258  1229 LEU A N   
9033  C CA  . LEU A 1231 ? 0.4533 0.4329 0.4881 0.0118  0.0088  0.0293  1229 LEU A CA  
9034  C C   . LEU A 1231 ? 0.4575 0.4349 0.4984 0.0111  0.0075  0.0280  1229 LEU A C   
9035  O O   . LEU A 1231 ? 0.4824 0.4602 0.5274 0.0107  0.0071  0.0312  1229 LEU A O   
9036  C CB  . LEU A 1231 ? 0.4166 0.3979 0.4456 0.0120  0.0107  0.0299  1229 LEU A CB  
9037  C CG  . LEU A 1231 ? 0.4268 0.4117 0.4516 0.0128  0.0119  0.0327  1229 LEU A CG  
9038  C CD1 . LEU A 1231 ? 0.3834 0.3699 0.4038 0.0131  0.0135  0.0328  1229 LEU A CD1 
9039  C CD2 . LEU A 1231 ? 0.4879 0.4753 0.5172 0.0129  0.0112  0.0378  1229 LEU A CD2 
9040  N N   . MET A 1232 ? 0.4641 0.4394 0.5058 0.0110  0.0067  0.0234  1230 MET A N   
9041  C CA  . MET A 1232 ? 0.4332 0.4067 0.4814 0.0105  0.0050  0.0217  1230 MET A CA  
9042  C C   . MET A 1232 ? 0.4450 0.4179 0.5016 0.0105  0.0030  0.0245  1230 MET A C   
9043  O O   . MET A 1232 ? 0.4539 0.4257 0.5172 0.0100  0.0015  0.0247  1230 MET A O   
9044  C CB  . MET A 1232 ? 0.4625 0.4350 0.5098 0.0106  0.0046  0.0160  1230 MET A CB  
9045  C CG  . MET A 1232 ? 0.4110 0.3840 0.4517 0.0103  0.0062  0.0134  1230 MET A CG  
9046  S SD  . MET A 1232 ? 0.5232 0.4963 0.5626 0.0104  0.0057  0.0073  1230 MET A SD  
9047  C CE  . MET A 1232 ? 0.4956 0.4679 0.5435 0.0102  0.0035  0.0049  1230 MET A CE  
9048  N N   . ALA A 1233 ? 0.4590 0.4328 0.5160 0.0109  0.0027  0.0268  1231 ALA A N   
9049  C CA  . ALA A 1233 ? 0.4873 0.4608 0.5524 0.0109  0.0007  0.0301  1231 ALA A CA  
9050  C C   . ALA A 1233 ? 0.5711 0.5471 0.6377 0.0105  0.0011  0.0368  1231 ALA A C   
9051  O O   . ALA A 1233 ? 0.5415 0.5176 0.6155 0.0102  -0.0007 0.0406  1231 ALA A O   
9052  C CB  . ALA A 1233 ? 0.4608 0.4344 0.5260 0.0115  0.0000  0.0293  1231 ALA A CB  
9053  N N   . ILE A 1234 ? 0.5717 0.5498 0.6317 0.0105  0.0033  0.0383  1232 ILE A N   
9054  C CA  . ILE A 1234 ? 0.5516 0.5332 0.6122 0.0103  0.0039  0.0444  1232 ILE A CA  
9055  C C   . ILE A 1234 ? 0.5279 0.5090 0.5916 0.0095  0.0039  0.0455  1232 ILE A C   
9056  O O   . ILE A 1234 ? 0.4047 0.3859 0.4634 0.0095  0.0054  0.0433  1232 ILE A O   
9057  C CB  . ILE A 1234 ? 0.5122 0.4972 0.5639 0.0110  0.0063  0.0453  1232 ILE A CB  
9058  C CG1 . ILE A 1234 ? 0.5221 0.5076 0.5715 0.0117  0.0060  0.0445  1232 ILE A CG1 
9059  C CG2 . ILE A 1234 ? 0.4418 0.4313 0.4940 0.0109  0.0071  0.0513  1232 ILE A CG2 
9060  C CD1 . ILE A 1234 ? 0.4815 0.4716 0.5251 0.0124  0.0075  0.0474  1232 ILE A CD1 
9061  N N   . GLY A 1235 ? 0.5148 0.4957 0.5875 0.0088  0.0020  0.0492  1233 GLY A N   
9062  C CA  . GLY A 1235 ? 0.4432 0.4240 0.5201 0.0080  0.0017  0.0511  1233 GLY A CA  
9063  C C   . GLY A 1235 ? 0.4237 0.4077 0.5063 0.0073  0.0010  0.0585  1233 GLY A C   
9064  O O   . GLY A 1235 ? 0.4682 0.4529 0.5549 0.0074  -0.0003 0.0615  1233 GLY A O   
9065  O OXT . GLY A 1235 ? 0.3023 0.2886 0.3860 0.0068  0.0017  0.0620  1233 GLY A OXT 
9066  N N   . ALA B 16   ? 0.5809 0.4692 0.5453 0.0663  -0.0310 -0.0308 14   ALA B N   
9067  C CA  . ALA B 16   ? 0.5504 0.4439 0.5173 0.0604  -0.0298 -0.0294 14   ALA B CA  
9068  C C   . ALA B 16   ? 0.5419 0.4268 0.5021 0.0555  -0.0310 -0.0291 14   ALA B C   
9069  O O   . ALA B 16   ? 0.6014 0.4793 0.5562 0.0564  -0.0313 -0.0306 14   ALA B O   
9070  C CB  . ALA B 16   ? 0.4926 0.3962 0.4651 0.0603  -0.0265 -0.0303 14   ALA B CB  
9071  N N   . PRO B 17   ? 0.5297 0.4152 0.4900 0.0505  -0.0316 -0.0270 15   PRO B N   
9072  C CA  . PRO B 17   ? 0.4905 0.3690 0.4450 0.0455  -0.0326 -0.0265 15   PRO B CA  
9073  C C   . PRO B 17   ? 0.4657 0.3470 0.4204 0.0435  -0.0304 -0.0277 15   PRO B C   
9074  O O   . PRO B 17   ? 0.4699 0.3607 0.4304 0.0436  -0.0279 -0.0280 15   PRO B O   
9075  C CB  . PRO B 17   ? 0.5380 0.4195 0.4943 0.0410  -0.0331 -0.0240 15   PRO B CB  
9076  C CG  . PRO B 17   ? 0.5867 0.4791 0.5508 0.0429  -0.0314 -0.0237 15   PRO B CG  
9077  C CD  . PRO B 17   ? 0.5287 0.4214 0.4943 0.0491  -0.0315 -0.0252 15   PRO B CD  
9078  N N   . ALA B 18   ? 0.4422 0.3150 0.3903 0.0416  -0.0315 -0.0285 16   ALA B N   
9079  C CA  . ALA B 18   ? 0.4031 0.2777 0.3506 0.0396  -0.0299 -0.0297 16   ALA B CA  
9080  C C   . ALA B 18   ? 0.3613 0.2437 0.3129 0.0345  -0.0284 -0.0281 16   ALA B C   
9081  O O   . ALA B 18   ? 0.3701 0.2519 0.3215 0.0310  -0.0294 -0.0261 16   ALA B O   
9082  C CB  . ALA B 18   ? 0.4294 0.2928 0.3688 0.0376  -0.0319 -0.0305 16   ALA B CB  
9083  N N   . PRO B 19   ? 0.3440 0.2337 0.2992 0.0342  -0.0259 -0.0289 17   PRO B N   
9084  C CA  . PRO B 19   ? 0.3186 0.2159 0.2780 0.0299  -0.0244 -0.0275 17   PRO B CA  
9085  C C   . PRO B 19   ? 0.3172 0.2098 0.2723 0.0245  -0.0258 -0.0263 17   PRO B C   
9086  O O   . PRO B 19   ? 0.3361 0.2222 0.2859 0.0231  -0.0268 -0.0272 17   PRO B O   
9087  C CB  . PRO B 19   ? 0.3337 0.2372 0.2959 0.0310  -0.0218 -0.0289 17   PRO B CB  
9088  C CG  . PRO B 19   ? 0.3602 0.2631 0.3228 0.0367  -0.0214 -0.0307 17   PRO B CG  
9089  C CD  . PRO B 19   ? 0.3590 0.2512 0.3153 0.0382  -0.0241 -0.0311 17   PRO B CD  
9090  N N   . PHE B 20   ? 0.3061 0.2021 0.2635 0.0212  -0.0258 -0.0243 18   PHE B N   
9091  C CA  . PHE B 20   ? 0.2999 0.1939 0.2546 0.0158  -0.0267 -0.0228 18   PHE B CA  
9092  C C   . PHE B 20   ? 0.3646 0.2477 0.3123 0.0143  -0.0295 -0.0223 18   PHE B C   
9093  O O   . PHE B 20   ? 0.3660 0.2465 0.3107 0.0096  -0.0303 -0.0212 18   PHE B O   
9094  C CB  . PHE B 20   ? 0.3125 0.2099 0.2676 0.0130  -0.0253 -0.0234 18   PHE B CB  
9095  C CG  . PHE B 20   ? 0.2741 0.1818 0.2357 0.0140  -0.0226 -0.0236 18   PHE B CG  
9096  C CD1 . PHE B 20   ? 0.2662 0.1806 0.2320 0.0119  -0.0216 -0.0220 18   PHE B CD1 
9097  C CD2 . PHE B 20   ? 0.2961 0.2064 0.2591 0.0169  -0.0211 -0.0254 18   PHE B CD2 
9098  C CE1 . PHE B 20   ? 0.2780 0.2010 0.2493 0.0126  -0.0194 -0.0221 18   PHE B CE1 
9099  C CE2 . PHE B 20   ? 0.2897 0.2090 0.2584 0.0175  -0.0187 -0.0254 18   PHE B CE2 
9100  C CZ  . PHE B 20   ? 0.2686 0.1940 0.2414 0.0154  -0.0179 -0.0238 18   PHE B CZ  
9101  N N   . ALA B 21   ? 0.3829 0.2596 0.3279 0.0182  -0.0310 -0.0230 19   ALA B N   
9102  C CA  . ALA B 21   ? 0.4047 0.2702 0.3427 0.0170  -0.0339 -0.0225 19   ALA B CA  
9103  C C   . ALA B 21   ? 0.4469 0.3110 0.3838 0.0133  -0.0352 -0.0198 19   ALA B C   
9104  O O   . ALA B 21   ? 0.4844 0.3399 0.4154 0.0105  -0.0374 -0.0189 19   ALA B O   
9105  C CB  . ALA B 21   ? 0.4633 0.3224 0.3988 0.0226  -0.0352 -0.0239 19   ALA B CB  
9106  N N   . ASP B 22   ? 0.3525 0.2247 0.2947 0.0131  -0.0339 -0.0186 20   ASP B N   
9107  C CA  . ASP B 22   ? 0.3665 0.2384 0.3078 0.0096  -0.0348 -0.0161 20   ASP B CA  
9108  C C   . ASP B 22   ? 0.3169 0.1989 0.2633 0.0065  -0.0325 -0.0151 20   ASP B C   
9109  O O   . ASP B 22   ? 0.3479 0.2340 0.2967 0.0060  -0.0322 -0.0137 20   ASP B O   
9110  C CB  . ASP B 22   ? 0.4435 0.3134 0.3849 0.0128  -0.0361 -0.0153 20   ASP B CB  
9111  N N   . PHE B 23   ? 0.2881 0.1738 0.2358 0.0047  -0.0310 -0.0160 21   PHE B N   
9112  C CA  . PHE B 23   ? 0.2730 0.1688 0.2262 0.0028  -0.0287 -0.0155 21   PHE B CA  
9113  C C   . PHE B 23   ? 0.2615 0.1585 0.2138 -0.0017 -0.0289 -0.0131 21   PHE B C   
9114  O O   . PHE B 23   ? 0.2703 0.1733 0.2262 -0.0016 -0.0279 -0.0122 21   PHE B O   
9115  C CB  . PHE B 23   ? 0.2618 0.1607 0.2160 0.0016  -0.0273 -0.0167 21   PHE B CB  
9116  C CG  . PHE B 23   ? 0.2707 0.1791 0.2298 -0.0005 -0.0251 -0.0161 21   PHE B CG  
9117  C CD1 . PHE B 23   ? 0.2564 0.1721 0.2210 0.0022  -0.0234 -0.0164 21   PHE B CD1 
9118  C CD2 . PHE B 23   ? 0.2727 0.1829 0.2309 -0.0051 -0.0248 -0.0151 21   PHE B CD2 
9119  C CE1 . PHE B 23   ? 0.2386 0.1625 0.2074 0.0005  -0.0215 -0.0158 21   PHE B CE1 
9120  C CE2 . PHE B 23   ? 0.2713 0.1903 0.2341 -0.0066 -0.0228 -0.0145 21   PHE B CE2 
9121  C CZ  . PHE B 23   ? 0.2491 0.1745 0.2169 -0.0037 -0.0212 -0.0149 21   PHE B CZ  
9122  N N   . ALA B 24   ? 0.2811 0.1728 0.2287 -0.0057 -0.0303 -0.0121 22   ALA B N   
9123  C CA  . ALA B 24   ? 0.2904 0.1839 0.2372 -0.0101 -0.0303 -0.0098 22   ALA B CA  
9124  C C   . ALA B 24   ? 0.2768 0.1615 0.2171 -0.0139 -0.0326 -0.0085 22   ALA B C   
9125  O O   . ALA B 24   ? 0.3009 0.1872 0.2404 -0.0184 -0.0323 -0.0075 22   ALA B O   
9126  C CB  . ALA B 24   ? 0.3034 0.2061 0.2544 -0.0127 -0.0280 -0.0096 22   ALA B CB  
9127  N N   . PRO B 25   ? 0.3041 0.1797 0.2398 -0.0122 -0.0348 -0.0083 23   PRO B N   
9128  C CA  . PRO B 25   ? 0.3470 0.2133 0.2761 -0.0159 -0.0372 -0.0070 23   PRO B CA  
9129  C C   . PRO B 25   ? 0.3454 0.2141 0.2737 -0.0208 -0.0371 -0.0042 23   PRO B C   
9130  O O   . PRO B 25   ? 0.3345 0.2078 0.2652 -0.0201 -0.0362 -0.0031 23   PRO B O   
9131  C CB  . PRO B 25   ? 0.4144 0.2714 0.3395 -0.0121 -0.0395 -0.0074 23   PRO B CB  
9132  C CG  . PRO B 25   ? 0.3768 0.2398 0.3067 -0.0078 -0.0383 -0.0077 23   PRO B CG  
9133  C CD  . PRO B 25   ? 0.3279 0.2014 0.2643 -0.0070 -0.0355 -0.0091 23   PRO B CD  
9134  N N   . PRO B 26   ? 0.3228 0.1889 0.2479 -0.0261 -0.0378 -0.0030 24   PRO B N   
9135  C CA  . PRO B 26   ? 0.3340 0.2030 0.2584 -0.0309 -0.0375 -0.0001 24   PRO B CA  
9136  C C   . PRO B 26   ? 0.3552 0.2166 0.2747 -0.0310 -0.0395 0.0018  24   PRO B C   
9137  O O   . PRO B 26   ? 0.3587 0.2106 0.2741 -0.0285 -0.0417 0.0012  24   PRO B O   
9138  C CB  . PRO B 26   ? 0.3772 0.2442 0.2989 -0.0363 -0.0382 0.0006  24   PRO B CB  
9139  C CG  . PRO B 26   ? 0.3871 0.2448 0.3049 -0.0344 -0.0402 -0.0014 24   PRO B CG  
9140  C CD  . PRO B 26   ? 0.3548 0.2151 0.2764 -0.0278 -0.0391 -0.0041 24   PRO B CD  
9141  N N   . VAL B 27   ? 0.3465 0.2123 0.2665 -0.0339 -0.0387 0.0042  25   VAL B N   
9142  C CA  . VAL B 27   ? 0.3312 0.1904 0.2464 -0.0346 -0.0405 0.0064  25   VAL B CA  
9143  C C   . VAL B 27   ? 0.3676 0.2151 0.2757 -0.0377 -0.0434 0.0076  25   VAL B C   
9144  O O   . VAL B 27   ? 0.3999 0.2380 0.3031 -0.0359 -0.0457 0.0081  25   VAL B O   
9145  C CB  . VAL B 27   ? 0.3430 0.2094 0.2595 -0.0378 -0.0389 0.0089  25   VAL B CB  
9146  C CG1 . VAL B 27   ? 0.3815 0.2402 0.2919 -0.0395 -0.0410 0.0116  25   VAL B CG1 
9147  C CG2 . VAL B 27   ? 0.3561 0.2318 0.2786 -0.0339 -0.0367 0.0076  25   VAL B CG2 
9148  N N   . ARG B 28   ? 0.3521 0.1998 0.2593 -0.0423 -0.0433 0.0079  26   ARG B N   
9149  C CA  . ARG B 28   ? 0.3814 0.2179 0.2816 -0.0459 -0.0461 0.0090  26   ARG B CA  
9150  C C   . ARG B 28   ? 0.4223 0.2597 0.3233 -0.0483 -0.0460 0.0075  26   ARG B C   
9151  O O   . ARG B 28   ? 0.3618 0.2097 0.2686 -0.0484 -0.0436 0.0065  26   ARG B O   
9152  C CB  . ARG B 28   ? 0.4121 0.2473 0.3087 -0.0518 -0.0467 0.0127  26   ARG B CB  
9153  C CG  . ARG B 28   ? 0.4092 0.2550 0.3096 -0.0569 -0.0444 0.0141  26   ARG B CG  
9154  C CD  . ARG B 28   ? 0.4244 0.2704 0.3218 -0.0621 -0.0445 0.0179  26   ARG B CD  
9155  N NE  . ARG B 28   ? 0.4479 0.2975 0.3465 -0.0593 -0.0434 0.0188  26   ARG B NE  
9156  C CZ  . ARG B 28   ? 0.4939 0.3353 0.3876 -0.0578 -0.0453 0.0200  26   ARG B CZ  
9157  N NH1 . ARG B 28   ? 0.5040 0.3327 0.3912 -0.0587 -0.0485 0.0207  26   ARG B NH1 
9158  N NH2 . ARG B 28   ? 0.4669 0.3127 0.3622 -0.0552 -0.0442 0.0206  26   ARG B NH2 
9159  N N   . PRO B 29   ? 0.3956 0.2221 0.2907 -0.0500 -0.0487 0.0072  27   PRO B N   
9160  C CA  . PRO B 29   ? 0.4049 0.2321 0.3001 -0.0532 -0.0489 0.0061  27   PRO B CA  
9161  C C   . PRO B 29   ? 0.3947 0.2307 0.2925 -0.0596 -0.0475 0.0085  27   PRO B C   
9162  O O   . PRO B 29   ? 0.4115 0.2469 0.3071 -0.0635 -0.0478 0.0116  27   PRO B O   
9163  C CB  . PRO B 29   ? 0.4240 0.2362 0.3110 -0.0548 -0.0525 0.0061  27   PRO B CB  
9164  C CG  . PRO B 29   ? 0.4835 0.2880 0.3676 -0.0495 -0.0539 0.0058  27   PRO B CG  
9165  C CD  . PRO B 29   ? 0.4220 0.2346 0.3098 -0.0490 -0.0519 0.0078  27   PRO B CD  
9166  N N   . GLN B 30   ? 0.3872 0.2317 0.2897 -0.0604 -0.0458 0.0072  28   GLN B N   
9167  C CA  . GLN B 30   ? 0.3837 0.2385 0.2899 -0.0656 -0.0440 0.0092  28   GLN B CA  
9168  C C   . GLN B 30   ? 0.3616 0.2107 0.2631 -0.0725 -0.0463 0.0109  28   GLN B C   
9169  O O   . GLN B 30   ? 0.3943 0.2387 0.2938 -0.0732 -0.0479 0.0092  28   GLN B O   
9170  C CB  . GLN B 30   ? 0.3461 0.2121 0.2592 -0.0635 -0.0415 0.0071  28   GLN B CB  
9171  C CG  . GLN B 30   ? 0.3437 0.2149 0.2613 -0.0569 -0.0394 0.0054  28   GLN B CG  
9172  C CD  . GLN B 30   ? 0.3444 0.2219 0.2644 -0.0570 -0.0376 0.0074  28   GLN B CD  
9173  O OE1 . GLN B 30   ? 0.3426 0.2303 0.2667 -0.0593 -0.0355 0.0086  28   GLN B OE1 
9174  N NE2 . GLN B 30   ? 0.3360 0.2074 0.2531 -0.0542 -0.0386 0.0079  28   GLN B NE2 
9175  N N   . SER B 31   ? 0.3816 0.2313 0.2813 -0.0776 -0.0465 0.0143  29   SER B N   
9176  C CA  . SER B 31   ? 0.3810 0.2265 0.2766 -0.0848 -0.0485 0.0165  29   SER B CA  
9177  C C   . SER B 31   ? 0.3717 0.2279 0.2725 -0.0882 -0.0471 0.0162  29   SER B C   
9178  O O   . SER B 31   ? 0.3559 0.2231 0.2632 -0.0851 -0.0444 0.0147  29   SER B O   
9179  C CB  . SER B 31   ? 0.3975 0.2435 0.2910 -0.0894 -0.0484 0.0204  29   SER B CB  
9180  O OG  . SER B 31   ? 0.3835 0.2439 0.2834 -0.0899 -0.0450 0.0216  29   SER B OG  
9181  N N   . THR B 32   ? 0.4157 0.2683 0.3133 -0.0947 -0.0492 0.0177  30   THR B N   
9182  C CA  . THR B 32   ? 0.3760 0.2389 0.2782 -0.0988 -0.0482 0.0179  30   THR B CA  
9183  C C   . THR B 32   ? 0.3506 0.2284 0.2593 -0.0996 -0.0447 0.0198  30   THR B C   
9184  O O   . THR B 32   ? 0.3508 0.2398 0.2658 -0.0982 -0.0425 0.0186  30   THR B O   
9185  C CB  . THR B 32   ? 0.3993 0.2557 0.2966 -0.1064 -0.0512 0.0199  30   THR B CB  
9186  O OG1 . THR B 32   ? 0.4909 0.3335 0.3820 -0.1050 -0.0544 0.0176  30   THR B OG1 
9187  C CG2 . THR B 32   ? 0.4422 0.3101 0.3445 -0.1111 -0.0503 0.0205  30   THR B CG2 
9188  N N   . LEU B 33   ? 0.3734 0.2512 0.2805 -0.1016 -0.0441 0.0228  31   LEU B N   
9189  C CA  . LEU B 33   ? 0.3619 0.2534 0.2746 -0.1023 -0.0407 0.0246  31   LEU B CA  
9190  C C   . LEU B 33   ? 0.3273 0.2255 0.2451 -0.0950 -0.0380 0.0222  31   LEU B C   
9191  O O   . LEU B 33   ? 0.3190 0.2299 0.2430 -0.0943 -0.0352 0.0221  31   LEU B O   
9192  C CB  . LEU B 33   ? 0.3399 0.2292 0.2489 -0.1062 -0.0408 0.0283  31   LEU B CB  
9193  C CG  . LEU B 33   ? 0.3479 0.2340 0.2533 -0.1145 -0.0429 0.0312  31   LEU B CG  
9194  C CD1 . LEU B 33   ? 0.4034 0.2856 0.3043 -0.1181 -0.0432 0.0349  31   LEU B CD1 
9195  C CD2 . LEU B 33   ? 0.4137 0.3134 0.3253 -0.1184 -0.0411 0.0320  31   LEU B CD2 
9196  N N   . ARG B 34   ? 0.3165 0.2064 0.2317 -0.0896 -0.0388 0.0204  32   ARG B N   
9197  C CA  . ARG B 34   ? 0.3304 0.2265 0.2505 -0.0829 -0.0364 0.0181  32   ARG B CA  
9198  C C   . ARG B 34   ? 0.2926 0.1944 0.2174 -0.0806 -0.0356 0.0153  32   ARG B C   
9199  O O   . ARG B 34   ? 0.2958 0.2081 0.2265 -0.0777 -0.0329 0.0144  32   ARG B O   
9200  C CB  . ARG B 34   ? 0.3122 0.1986 0.2287 -0.0777 -0.0377 0.0168  32   ARG B CB  
9201  C CG  . ARG B 34   ? 0.3341 0.2165 0.2468 -0.0786 -0.0380 0.0194  32   ARG B CG  
9202  C CD  . ARG B 34   ? 0.3103 0.2036 0.2276 -0.0769 -0.0349 0.0202  32   ARG B CD  
9203  N NE  . ARG B 34   ? 0.3265 0.2230 0.2478 -0.0701 -0.0335 0.0174  32   ARG B NE  
9204  C CZ  . ARG B 34   ? 0.3338 0.2252 0.2534 -0.0656 -0.0341 0.0167  32   ARG B CZ  
9205  N NH1 . ARG B 34   ? 0.3522 0.2347 0.2660 -0.0668 -0.0360 0.0186  32   ARG B NH1 
9206  N NH2 . ARG B 34   ? 0.3415 0.2367 0.2654 -0.0599 -0.0328 0.0141  32   ARG B NH2 
9207  N N   . ARG B 35   ? 0.3166 0.2114 0.2385 -0.0819 -0.0379 0.0140  33   ARG B N   
9208  C CA  . ARG B 35   ? 0.3168 0.2165 0.2426 -0.0799 -0.0373 0.0114  33   ARG B CA  
9209  C C   . ARG B 35   ? 0.3031 0.2156 0.2343 -0.0835 -0.0355 0.0126  33   ARG B C   
9210  O O   . ARG B 35   ? 0.2995 0.2203 0.2360 -0.0806 -0.0337 0.0109  33   ARG B O   
9211  C CB  . ARG B 35   ? 0.3416 0.2307 0.2624 -0.0810 -0.0404 0.0098  33   ARG B CB  
9212  C CG  . ARG B 35   ? 0.3925 0.2706 0.3093 -0.0757 -0.0418 0.0077  33   ARG B CG  
9213  C CD  . ARG B 35   ? 0.4708 0.3376 0.3819 -0.0767 -0.0449 0.0061  33   ARG B CD  
9214  N NE  . ARG B 35   ? 0.5319 0.3883 0.4390 -0.0714 -0.0462 0.0042  33   ARG B NE  
9215  C CZ  . ARG B 35   ? 0.6348 0.4925 0.5444 -0.0650 -0.0450 0.0013  33   ARG B CZ  
9216  N NH1 . ARG B 35   ? 0.6668 0.5348 0.5823 -0.0632 -0.0427 -0.0001 33   ARG B NH1 
9217  N NH2 . ARG B 35   ? 0.5851 0.4335 0.4911 -0.0604 -0.0461 -0.0001 33   ARG B NH2 
9218  N N   . ALA B 36   ? 0.3046 0.2189 0.2346 -0.0898 -0.0360 0.0156  34   ALA B N   
9219  C CA  . ALA B 36   ? 0.3265 0.2537 0.2618 -0.0933 -0.0343 0.0170  34   ALA B CA  
9220  C C   . ALA B 36   ? 0.3120 0.2504 0.2530 -0.0898 -0.0307 0.0172  34   ALA B C   
9221  O O   . ALA B 36   ? 0.2978 0.2473 0.2445 -0.0892 -0.0288 0.0167  34   ALA B O   
9222  C CB  . ALA B 36   ? 0.3021 0.2290 0.2349 -0.1010 -0.0355 0.0204  34   ALA B CB  
9223  N N   . ILE B 37   ? 0.2745 0.2099 0.2137 -0.0872 -0.0299 0.0178  35   ILE B N   
9224  C CA  . ILE B 37   ? 0.2735 0.2182 0.2174 -0.0832 -0.0267 0.0175  35   ILE B CA  
9225  C C   . ILE B 37   ? 0.2944 0.2419 0.2424 -0.0773 -0.0257 0.0142  35   ILE B C   
9226  O O   . ILE B 37   ? 0.2486 0.2067 0.2021 -0.0759 -0.0234 0.0137  35   ILE B O   
9227  C CB  . ILE B 37   ? 0.2715 0.2108 0.2120 -0.0814 -0.0266 0.0185  35   ILE B CB  
9228  C CG1 . ILE B 37   ? 0.2708 0.2091 0.2077 -0.0875 -0.0272 0.0221  35   ILE B CG1 
9229  C CG2 . ILE B 37   ? 0.2749 0.2222 0.2198 -0.0765 -0.0237 0.0176  35   ILE B CG2 
9230  C CD1 . ILE B 37   ? 0.2853 0.2150 0.2171 -0.0863 -0.0281 0.0233  35   ILE B CD1 
9231  N N   . THR B 38   ? 0.2646 0.2026 0.2097 -0.0738 -0.0274 0.0121  36   THR B N   
9232  C CA  . THR B 38   ? 0.2713 0.2115 0.2199 -0.0681 -0.0263 0.0091  36   THR B CA  
9233  C C   . THR B 38   ? 0.2757 0.2228 0.2280 -0.0692 -0.0259 0.0081  36   THR B C   
9234  O O   . THR B 38   ? 0.2563 0.2109 0.2135 -0.0657 -0.0239 0.0068  36   THR B O   
9235  C CB  . THR B 38   ? 0.2789 0.2076 0.2234 -0.0647 -0.0283 0.0071  36   THR B CB  
9236  O OG1 . THR B 38   ? 0.2793 0.2017 0.2200 -0.0642 -0.0290 0.0084  36   THR B OG1 
9237  C CG2 . THR B 38   ? 0.3054 0.2368 0.2536 -0.0587 -0.0270 0.0043  36   THR B CG2 
9238  N N   . ALA B 39   ? 0.2818 0.2261 0.2317 -0.0741 -0.0279 0.0090  37   ALA B N   
9239  C CA  . ALA B 39   ? 0.2931 0.2433 0.2461 -0.0754 -0.0280 0.0081  37   ALA B CA  
9240  C C   . ALA B 39   ? 0.2877 0.2517 0.2469 -0.0760 -0.0253 0.0092  37   ALA B C   
9241  O O   . ALA B 39   ? 0.2820 0.2527 0.2452 -0.0747 -0.0245 0.0080  37   ALA B O   
9242  C CB  . ALA B 39   ? 0.2924 0.2368 0.2412 -0.0812 -0.0309 0.0090  37   ALA B CB  
9243  N N   . ALA B 40   ? 0.2535 0.2220 0.2135 -0.0777 -0.0239 0.0115  38   ALA B N   
9244  C CA  . ALA B 40   ? 0.2781 0.2597 0.2436 -0.0784 -0.0213 0.0128  38   ALA B CA  
9245  C C   . ALA B 40   ? 0.2318 0.2188 0.2011 -0.0726 -0.0186 0.0114  38   ALA B C   
9246  O O   . ALA B 40   ? 0.2544 0.2522 0.2284 -0.0722 -0.0163 0.0121  38   ALA B O   
9247  C CB  . ALA B 40   ? 0.2850 0.2693 0.2492 -0.0835 -0.0209 0.0160  38   ALA B CB  
9248  N N   . TYR B 41   ? 0.2313 0.2112 0.1988 -0.0680 -0.0188 0.0096  39   TYR B N   
9249  C CA  . TYR B 41   ? 0.2308 0.2144 0.2009 -0.0630 -0.0166 0.0087  39   TYR B CA  
9250  C C   . TYR B 41   ? 0.2284 0.2230 0.2045 -0.0608 -0.0143 0.0079  39   TYR B C   
9251  O O   . TYR B 41   ? 0.2294 0.2313 0.2082 -0.0598 -0.0121 0.0087  39   TYR B O   
9252  C CB  . TYR B 41   ? 0.2289 0.2037 0.1969 -0.0585 -0.0176 0.0065  39   TYR B CB  
9253  C CG  . TYR B 41   ? 0.2244 0.1988 0.1929 -0.0542 -0.0162 0.0059  39   TYR B CG  
9254  C CD1 . TYR B 41   ? 0.2210 0.2041 0.1932 -0.0526 -0.0137 0.0063  39   TYR B CD1 
9255  C CD2 . TYR B 41   ? 0.2496 0.2150 0.2150 -0.0515 -0.0175 0.0048  39   TYR B CD2 
9256  C CE1 . TYR B 41   ? 0.2133 0.1956 0.1858 -0.0488 -0.0127 0.0056  39   TYR B CE1 
9257  C CE2 . TYR B 41   ? 0.2403 0.2054 0.2063 -0.0476 -0.0165 0.0042  39   TYR B CE2 
9258  C CZ  . TYR B 41   ? 0.2220 0.1954 0.1915 -0.0464 -0.0142 0.0046  39   TYR B CZ  
9259  O OH  . TYR B 41   ? 0.2291 0.2020 0.1989 -0.0428 -0.0134 0.0040  39   TYR B OH  
9260  N N   . ARG B 42   ? 0.2363 0.2319 0.2142 -0.0600 -0.0149 0.0064  40   ARG B N   
9261  C CA  . ARG B 42   ? 0.2247 0.2299 0.2079 -0.0576 -0.0131 0.0056  40   ARG B CA  
9262  C C   . ARG B 42   ? 0.2336 0.2439 0.2186 -0.0612 -0.0139 0.0062  40   ARG B C   
9263  O O   . ARG B 42   ? 0.2450 0.2596 0.2331 -0.0591 -0.0135 0.0050  40   ARG B O   
9264  C CB  . ARG B 42   ? 0.2495 0.2523 0.2340 -0.0520 -0.0126 0.0031  40   ARG B CB  
9265  C CG  . ARG B 42   ? 0.2425 0.2420 0.2260 -0.0487 -0.0117 0.0027  40   ARG B CG  
9266  C CD  . ARG B 42   ? 0.2279 0.2247 0.2125 -0.0436 -0.0113 0.0004  40   ARG B CD  
9267  N NE  . ARG B 42   ? 0.2227 0.2144 0.2053 -0.0415 -0.0112 0.0002  40   ARG B NE  
9268  C CZ  . ARG B 42   ? 0.2265 0.2220 0.2107 -0.0394 -0.0095 0.0004  40   ARG B CZ  
9269  N NH1 . ARG B 42   ? 0.2329 0.2371 0.2210 -0.0386 -0.0075 0.0006  40   ARG B NH1 
9270  N NH2 . ARG B 42   ? 0.2249 0.2151 0.2068 -0.0379 -0.0099 0.0004  40   ARG B NH2 
9271  N N   . ARG B 43   ? 0.2222 0.2322 0.2052 -0.0666 -0.0151 0.0083  41   ARG B N   
9272  C CA  . ARG B 43   ? 0.2483 0.2627 0.2327 -0.0707 -0.0163 0.0091  41   ARG B CA  
9273  C C   . ARG B 43   ? 0.2575 0.2849 0.2480 -0.0695 -0.0141 0.0094  41   ARG B C   
9274  O O   . ARG B 43   ? 0.2279 0.2616 0.2208 -0.0680 -0.0117 0.0103  41   ARG B O   
9275  C CB  . ARG B 43   ? 0.2278 0.2404 0.2092 -0.0771 -0.0177 0.0116  41   ARG B CB  
9276  C CG  . ARG B 43   ? 0.2208 0.2384 0.2037 -0.0822 -0.0191 0.0128  41   ARG B CG  
9277  C CD  . ARG B 43   ? 0.2577 0.2699 0.2362 -0.0885 -0.0211 0.0150  41   ARG B CD  
9278  N NE  . ARG B 43   ? 0.2873 0.2854 0.2597 -0.0883 -0.0237 0.0137  41   ARG B NE  
9279  C CZ  . ARG B 43   ? 0.3143 0.3037 0.2815 -0.0916 -0.0252 0.0151  41   ARG B CZ  
9280  N NH1 . ARG B 43   ? 0.2897 0.2827 0.2567 -0.0955 -0.0245 0.0180  41   ARG B NH1 
9281  N NH2 . ARG B 43   ? 0.3085 0.2852 0.2702 -0.0907 -0.0276 0.0135  41   ARG B NH2 
9282  N N   . PRO B 44   ? 0.2364 0.2679 0.2294 -0.0696 -0.0148 0.0087  42   PRO B N   
9283  C CA  . PRO B 44   ? 0.2279 0.2718 0.2267 -0.0683 -0.0129 0.0091  42   PRO B CA  
9284  C C   . PRO B 44   ? 0.2248 0.2772 0.2258 -0.0719 -0.0116 0.0117  42   PRO B C   
9285  O O   . PRO B 44   ? 0.2234 0.2739 0.2220 -0.0773 -0.0130 0.0136  42   PRO B O   
9286  C CB  . PRO B 44   ? 0.2680 0.3134 0.2679 -0.0697 -0.0148 0.0083  42   PRO B CB  
9287  C CG  . PRO B 44   ? 0.2910 0.3243 0.2861 -0.0682 -0.0167 0.0063  42   PRO B CG  
9288  C CD  . PRO B 44   ? 0.2654 0.2902 0.2558 -0.0703 -0.0173 0.0071  42   PRO B CD  
9289  N N   . GLU B 45   ? 0.2347 0.2963 0.2399 -0.0687 -0.0089 0.0119  43   GLU B N   
9290  C CA  . GLU B 45   ? 0.2245 0.2951 0.2320 -0.0713 -0.0072 0.0143  43   GLU B CA  
9291  C C   . GLU B 45   ? 0.2341 0.3115 0.2436 -0.0768 -0.0084 0.0162  43   GLU B C   
9292  O O   . GLU B 45   ? 0.2548 0.3353 0.2639 -0.0815 -0.0083 0.0187  43   GLU B O   
9293  C CB  . GLU B 45   ? 0.2804 0.3594 0.2921 -0.0661 -0.0042 0.0137  43   GLU B CB  
9294  C CG  . GLU B 45   ? 0.2945 0.3792 0.3067 -0.0668 -0.0019 0.0154  43   GLU B CG  
9295  C CD  . GLU B 45   ? 0.2053 0.2919 0.2188 -0.0609 0.0007  0.0141  43   GLU B CD  
9296  O OE1 . GLU B 45   ? 0.1993 0.2820 0.2130 -0.0563 0.0006  0.0118  43   GLU B OE1 
9297  O OE2 . GLU B 45   ? 0.2107 0.3027 0.2247 -0.0610 0.0028  0.0154  43   GLU B OE2 
9298  N N   . THR B 46   ? 0.2451 0.3250 0.2569 -0.0766 -0.0098 0.0153  44   THR B N   
9299  C CA  . THR B 46   ? 0.2350 0.3213 0.2488 -0.0820 -0.0113 0.0170  44   THR B CA  
9300  C C   . THR B 46   ? 0.2258 0.3035 0.2347 -0.0881 -0.0142 0.0180  44   THR B C   
9301  O O   . THR B 46   ? 0.2699 0.3528 0.2799 -0.0938 -0.0153 0.0201  44   THR B O   
9302  C CB  . THR B 46   ? 0.2544 0.3442 0.2711 -0.0801 -0.0124 0.0155  44   THR B CB  
9303  O OG1 . THR B 46   ? 0.2627 0.3412 0.2755 -0.0775 -0.0140 0.0131  44   THR B OG1 
9304  C CG2 . THR B 46   ? 0.2604 0.3607 0.2826 -0.0749 -0.0097 0.0151  44   THR B CG2 
9305  N N   . GLU B 47   ? 0.2461 0.3106 0.2494 -0.0871 -0.0155 0.0166  45   GLU B N   
9306  C CA  . GLU B 47   ? 0.2507 0.3059 0.2487 -0.0927 -0.0182 0.0176  45   GLU B CA  
9307  C C   . GLU B 47   ? 0.2504 0.3043 0.2461 -0.0953 -0.0171 0.0199  45   GLU B C   
9308  O O   . GLU B 47   ? 0.2946 0.3457 0.2876 -0.1013 -0.0189 0.0219  45   GLU B O   
9309  C CB  . GLU B 47   ? 0.2678 0.3094 0.2606 -0.0903 -0.0202 0.0151  45   GLU B CB  
9310  C CG  . GLU B 47   ? 0.3500 0.3915 0.3439 -0.0884 -0.0216 0.0130  45   GLU B CG  
9311  C CD  . GLU B 47   ? 0.3958 0.4242 0.3845 -0.0856 -0.0232 0.0104  45   GLU B CD  
9312  O OE1 . GLU B 47   ? 0.4390 0.4575 0.4226 -0.0874 -0.0244 0.0107  45   GLU B OE1 
9313  O OE2 . GLU B 47   ? 0.4639 0.4922 0.4537 -0.0816 -0.0232 0.0083  45   GLU B OE2 
9314  N N   . CYS B 48   ? 0.2201 0.2761 0.2169 -0.0909 -0.0144 0.0196  46   CYS B N   
9315  C CA  . CYS B 48   ? 0.2426 0.2970 0.2368 -0.0929 -0.0133 0.0217  46   CYS B CA  
9316  C C   . CYS B 48   ? 0.2344 0.3005 0.2320 -0.0974 -0.0119 0.0247  46   CYS B C   
9317  O O   . CYS B 48   ? 0.2455 0.3096 0.2402 -0.1024 -0.0124 0.0271  46   CYS B O   
9318  C CB  . CYS B 48   ? 0.2351 0.2888 0.2294 -0.0869 -0.0108 0.0204  46   CYS B CB  
9319  S SG  . CYS B 48   ? 0.2425 0.2825 0.2326 -0.0819 -0.0121 0.0174  46   CYS B SG  
9320  N N   . LEU B 49   ? 0.2366 0.3152 0.2403 -0.0956 -0.0101 0.0246  47   LEU B N   
9321  C CA  . LEU B 49   ? 0.2375 0.3286 0.2449 -0.0985 -0.0080 0.0273  47   LEU B CA  
9322  C C   . LEU B 49   ? 0.2611 0.3558 0.2688 -0.1063 -0.0098 0.0301  47   LEU B C   
9323  O O   . LEU B 49   ? 0.2469 0.3462 0.2545 -0.1102 -0.0086 0.0329  47   LEU B O   
9324  C CB  . LEU B 49   ? 0.2436 0.3474 0.2575 -0.0936 -0.0053 0.0265  47   LEU B CB  
9325  C CG  . LEU B 49   ? 0.2231 0.3289 0.2372 -0.0884 -0.0020 0.0259  47   LEU B CG  
9326  C CD1 . LEU B 49   ? 0.2461 0.3561 0.2591 -0.0920 -0.0003 0.0288  47   LEU B CD1 
9327  C CD2 . LEU B 49   ? 0.2316 0.3245 0.2411 -0.0842 -0.0027 0.0236  47   LEU B CD2 
9328  N N   . PRO B 50   ? 0.2644 0.3577 0.2726 -0.1091 -0.0126 0.0296  48   PRO B N   
9329  C CA  . PRO B 50   ? 0.2893 0.3874 0.2984 -0.1169 -0.0143 0.0324  48   PRO B CA  
9330  C C   . PRO B 50   ? 0.2958 0.3860 0.2993 -0.1226 -0.0154 0.0348  48   PRO B C   
9331  O O   . PRO B 50   ? 0.2924 0.3905 0.2976 -0.1276 -0.0145 0.0379  48   PRO B O   
9332  C CB  . PRO B 50   ? 0.2643 0.3584 0.2731 -0.1181 -0.0177 0.0307  48   PRO B CB  
9333  C CG  . PRO B 50   ? 0.2440 0.3401 0.2556 -0.1104 -0.0164 0.0278  48   PRO B CG  
9334  C CD  . PRO B 50   ? 0.2392 0.3298 0.2484 -0.1051 -0.0140 0.0267  48   PRO B CD  
9335  N N   . PRO B 51   ? 0.2966 0.3715 0.2934 -0.1220 -0.0173 0.0335  49   PRO B N   
9336  C CA  . PRO B 51   ? 0.3012 0.3688 0.2926 -0.1274 -0.0183 0.0361  49   PRO B CA  
9337  C C   . PRO B 51   ? 0.2723 0.3455 0.2643 -0.1266 -0.0149 0.0381  49   PRO B C   
9338  O O   . PRO B 51   ? 0.3035 0.3774 0.2934 -0.1325 -0.0150 0.0413  49   PRO B O   
9339  C CB  . PRO B 51   ? 0.3395 0.3898 0.3240 -0.1255 -0.0208 0.0339  49   PRO B CB  
9340  C CG  . PRO B 51   ? 0.3544 0.4043 0.3410 -0.1177 -0.0198 0.0304  49   PRO B CG  
9341  C CD  . PRO B 51   ? 0.2824 0.3458 0.2760 -0.1171 -0.0188 0.0301  49   PRO B CD  
9342  N N   . LEU B 52   ? 0.2782 0.3555 0.2725 -0.1197 -0.0119 0.0364  50   LEU B N   
9343  C CA  . LEU B 52   ? 0.2500 0.3334 0.2448 -0.1186 -0.0086 0.0381  50   LEU B CA  
9344  C C   . LEU B 52   ? 0.2719 0.3716 0.2726 -0.1219 -0.0065 0.0407  50   LEU B C   
9345  O O   . LEU B 52   ? 0.2689 0.3725 0.2686 -0.1257 -0.0050 0.0437  50   LEU B O   
9346  C CB  . LEU B 52   ? 0.2564 0.3399 0.2523 -0.1103 -0.0062 0.0353  50   LEU B CB  
9347  C CG  . LEU B 52   ? 0.2413 0.3100 0.2321 -0.1064 -0.0079 0.0327  50   LEU B CG  
9348  C CD1 . LEU B 52   ? 0.2472 0.3182 0.2404 -0.0985 -0.0056 0.0300  50   LEU B CD1 
9349  C CD2 . LEU B 52   ? 0.2762 0.3352 0.2606 -0.1091 -0.0087 0.0345  50   LEU B CD2 
9350  N N   . VAL B 53   ? 0.2649 0.3743 0.2716 -0.1205 -0.0063 0.0397  51   VAL B N   
9351  C CA  . VAL B 53   ? 0.2631 0.3886 0.2758 -0.1237 -0.0045 0.0422  51   VAL B CA  
9352  C C   . VAL B 53   ? 0.3243 0.4483 0.3345 -0.1315 -0.0064 0.0453  51   VAL B C   
9353  O O   . VAL B 53   ? 0.2799 0.4113 0.2909 -0.1331 -0.0046 0.0477  51   VAL B O   
9354  C CB  . VAL B 53   ? 0.2584 0.3927 0.2774 -0.1212 -0.0048 0.0406  51   VAL B CB  
9355  C CG1 . VAL B 53   ? 0.2933 0.4413 0.3173 -0.1243 -0.0042 0.0429  51   VAL B CG1 
9356  C CG2 . VAL B 53   ? 0.2732 0.4109 0.2949 -0.1126 -0.0022 0.0378  51   VAL B CG2 
9357  N N   . GLU B 54   ? 0.3019 0.4147 0.3081 -0.1350 -0.0104 0.0448  52   GLU B N   
9358  C CA  . GLU B 54   ? 0.3108 0.4198 0.3134 -0.1409 -0.0126 0.0472  52   GLU B CA  
9359  C C   . GLU B 54   ? 0.3117 0.4151 0.3091 -0.1432 -0.0117 0.0495  52   GLU B C   
9360  O O   . GLU B 54   ? 0.3185 0.4271 0.3159 -0.1465 -0.0110 0.0522  52   GLU B O   
9361  C CB  . GLU B 54   ? 0.3656 0.4622 0.3641 -0.1435 -0.0171 0.0459  52   GLU B CB  
9362  N N   . ALA B 55   ? 0.3052 0.3981 0.2982 -0.1413 -0.0116 0.0484  53   ALA B N   
9363  C CA  . ALA B 55   ? 0.3645 0.4512 0.3519 -0.1432 -0.0109 0.0505  53   ALA B CA  
9364  C C   . ALA B 55   ? 0.3148 0.4142 0.3055 -0.1415 -0.0067 0.0522  53   ALA B C   
9365  O O   . ALA B 55   ? 0.3567 0.4553 0.3441 -0.1443 -0.0060 0.0548  53   ALA B O   
9366  C CB  . ALA B 55   ? 0.3535 0.4264 0.3356 -0.1409 -0.0119 0.0489  53   ALA B CB  
9367  N N   . ALA B 56   ? 0.2991 0.4100 0.2960 -0.1366 -0.0038 0.0508  54   ALA B N   
9368  C CA  . ALA B 56   ? 0.3233 0.4460 0.3231 -0.1340 0.0005  0.0519  54   ALA B CA  
9369  C C   . ALA B 56   ? 0.3077 0.4439 0.3124 -0.1358 0.0015  0.0537  54   ALA B C   
9370  O O   . ALA B 56   ? 0.3528 0.4989 0.3596 -0.1339 0.0049  0.0547  54   ALA B O   
9371  C CB  . ALA B 56   ? 0.3237 0.4517 0.3274 -0.1270 0.0031  0.0491  54   ALA B CB  
9372  N N   . THR B 57   ? 0.3080 0.4445 0.3141 -0.1392 -0.0013 0.0540  55   THR B N   
9373  C CA  . THR B 57   ? 0.3763 0.5261 0.3875 -0.1407 -0.0004 0.0556  55   THR B CA  
9374  C C   . THR B 57   ? 0.3622 0.5139 0.3707 -0.1448 0.0005  0.0588  55   THR B C   
9375  O O   . THR B 57   ? 0.3820 0.5225 0.3843 -0.1490 -0.0015 0.0602  55   THR B O   
9376  C CB  . THR B 57   ? 0.3821 0.5304 0.3946 -0.1439 -0.0040 0.0552  55   THR B CB  
9377  O OG1 . THR B 57   ? 0.3724 0.5216 0.3884 -0.1396 -0.0045 0.0523  55   THR B OG1 
9378  C CG2 . THR B 57   ? 0.3492 0.5103 0.3664 -0.1464 -0.0035 0.0573  55   THR B CG2 
9379  N N   . GLN B 58   ? 0.3870 0.5529 0.4002 -0.1433 0.0036  0.0600  56   GLN B N   
9380  C CA  . GLN B 58   ? 0.3723 0.5423 0.3840 -0.1470 0.0048  0.0631  56   GLN B CA  
9381  C C   . GLN B 58   ? 0.4123 0.5963 0.4300 -0.1483 0.0053  0.0644  56   GLN B C   
9382  O O   . GLN B 58   ? 0.3614 0.5539 0.3850 -0.1448 0.0059  0.0628  56   GLN B O   
9383  C CB  . GLN B 58   ? 0.4040 0.5772 0.4144 -0.1434 0.0087  0.0634  56   GLN B CB  
9384  C CG  . GLN B 58   ? 0.3733 0.5339 0.3783 -0.1411 0.0086  0.0619  56   GLN B CG  
9385  C CD  . GLN B 58   ? 0.4401 0.6002 0.4411 -0.1403 0.0113  0.0633  56   GLN B CD  
9386  O OE1 . GLN B 58   ? 0.4819 0.6384 0.4788 -0.1449 0.0106  0.0659  56   GLN B OE1 
9387  N NE2 . GLN B 58   ? 0.4471 0.6108 0.4493 -0.1344 0.0144  0.0615  56   GLN B NE2 
9388  N N   . SER B 59   ? 0.4417 0.6279 0.4579 -0.1535 0.0051  0.0675  57   SER B N   
9389  C CA  . SER B 59   ? 0.4044 0.6035 0.4259 -0.1556 0.0054  0.0692  57   SER B CA  
9390  C C   . SER B 59   ? 0.4296 0.6438 0.4572 -0.1498 0.0097  0.0685  57   SER B C   
9391  O O   . SER B 59   ? 0.3825 0.5971 0.4092 -0.1453 0.0126  0.0675  57   SER B O   
9392  C CB  . SER B 59   ? 0.4310 0.6295 0.4492 -0.1619 0.0049  0.0727  57   SER B CB  
9393  O OG  . SER B 59   ? 0.4669 0.6672 0.4829 -0.1604 0.0082  0.0738  57   SER B OG  
9394  N N   . LYS B 60   ? 0.4154 0.6419 0.4491 -0.1500 0.0098  0.0691  58   LYS B N   
9395  C CA  . LYS B 60   ? 0.4108 0.6520 0.4503 -0.1447 0.0137  0.0688  58   LYS B CA  
9396  C C   . LYS B 60   ? 0.4111 0.6559 0.4484 -0.1449 0.0170  0.0707  58   LYS B C   
9397  O O   . LYS B 60   ? 0.4250 0.6759 0.4640 -0.1391 0.0205  0.0695  58   LYS B O   
9398  C CB  . LYS B 60   ? 0.3717 0.6251 0.4175 -0.1460 0.0131  0.0697  58   LYS B CB  
9399  N N   . GLU B 61   ? 0.4105 0.6511 0.4437 -0.1514 0.0157  0.0736  59   GLU B N   
9400  C CA  . GLU B 61   ? 0.4255 0.6693 0.4563 -0.1522 0.0186  0.0757  59   GLU B CA  
9401  C C   . GLU B 61   ? 0.4319 0.6674 0.4579 -0.1482 0.0204  0.0742  59   GLU B C   
9402  O O   . GLU B 61   ? 0.4025 0.6446 0.4293 -0.1438 0.0241  0.0738  59   GLU B O   
9403  C CB  . GLU B 61   ? 0.4977 0.7368 0.5245 -0.1603 0.0164  0.0791  59   GLU B CB  
9404  N N   . ILE B 62   ? 0.4232 0.6440 0.4440 -0.1497 0.0177  0.0732  60   ILE B N   
9405  C CA  . ILE B 62   ? 0.3801 0.5923 0.3960 -0.1462 0.0190  0.0718  60   ILE B CA  
9406  C C   . ILE B 62   ? 0.3758 0.5938 0.3957 -0.1383 0.0217  0.0687  60   ILE B C   
9407  O O   . ILE B 62   ? 0.4352 0.6541 0.4534 -0.1341 0.0247  0.0679  60   ILE B O   
9408  C CB  . ILE B 62   ? 0.4529 0.6480 0.4626 -0.1494 0.0153  0.0714  60   ILE B CB  
9409  N N   . ARG B 63   ? 0.3586 0.5807 0.3838 -0.1361 0.0205  0.0668  61   ARG B N   
9410  C CA  . ARG B 63   ? 0.3760 0.6032 0.4050 -0.1286 0.0227  0.0638  61   ARG B CA  
9411  C C   . ARG B 63   ? 0.3829 0.6238 0.4157 -0.1242 0.0268  0.0639  61   ARG B C   
9412  O O   . ARG B 63   ? 0.3974 0.6398 0.4301 -0.1182 0.0296  0.0620  61   ARG B O   
9413  C CB  . ARG B 63   ? 0.4038 0.6320 0.4372 -0.1275 0.0203  0.0619  61   ARG B CB  
9414  C CG  . ARG B 63   ? 0.4262 0.6401 0.4557 -0.1301 0.0167  0.0609  61   ARG B CG  
9415  C CD  . ARG B 63   ? 0.4662 0.6812 0.4999 -0.1281 0.0147  0.0587  61   ARG B CD  
9416  N NE  . ARG B 63   ? 0.3781 0.5980 0.4149 -0.1325 0.0123  0.0602  61   ARG B NE  
9417  C CZ  . ARG B 63   ? 0.4472 0.6792 0.4904 -0.1302 0.0130  0.0599  61   ARG B CZ  
9418  N NH1 . ARG B 63   ? 0.4802 0.7208 0.5276 -0.1234 0.0160  0.0581  61   ARG B NH1 
9419  N NH2 . ARG B 63   ? 0.4688 0.7040 0.5141 -0.1347 0.0105  0.0613  61   ARG B NH2 
9420  N N   . ASP B 64   ? 0.3315 0.5826 0.3677 -0.1271 0.0272  0.0662  62   ASP B N   
9421  C CA  . ASP B 64   ? 0.3668 0.6308 0.4063 -0.1233 0.0311  0.0665  62   ASP B CA  
9422  C C   . ASP B 64   ? 0.3069 0.5677 0.3410 -0.1230 0.0337  0.0675  62   ASP B C   
9423  O O   . ASP B 64   ? 0.3729 0.6388 0.4075 -0.1171 0.0371  0.0661  62   ASP B O   
9424  C CB  . ASP B 64   ? 0.3916 0.6667 0.4354 -0.1271 0.0308  0.0691  62   ASP B CB  
9425  C CG  . ASP B 64   ? 0.4450 0.7250 0.4946 -0.1267 0.0287  0.0681  62   ASP B CG  
9426  O OD1 . ASP B 64   ? 0.4095 0.6887 0.4612 -0.1213 0.0287  0.0652  62   ASP B OD1 
9427  O OD2 . ASP B 64   ? 0.4677 0.7526 0.5196 -0.1318 0.0270  0.0703  62   ASP B OD2 
9428  N N   . ALA B 65   ? 0.3167 0.5687 0.3452 -0.1293 0.0319  0.0699  63   ALA B N   
9429  C CA  . ALA B 65   ? 0.3309 0.5792 0.3537 -0.1294 0.0341  0.0710  63   ALA B CA  
9430  C C   . ALA B 65   ? 0.4085 0.6489 0.4277 -0.1241 0.0352  0.0683  63   ALA B C   
9431  O O   . ALA B 65   ? 0.4250 0.6671 0.4417 -0.1206 0.0384  0.0680  63   ALA B O   
9432  C CB  . ALA B 65   ? 0.3488 0.5879 0.3662 -0.1373 0.0315  0.0740  63   ALA B CB  
9433  N N   . ALA B 66   ? 0.4014 0.6332 0.4203 -0.1233 0.0327  0.0663  64   ALA B N   
9434  C CA  . ALA B 66   ? 0.3721 0.5964 0.3877 -0.1183 0.0336  0.0637  64   ALA B CA  
9435  C C   . ALA B 66   ? 0.3711 0.6047 0.3912 -0.1104 0.0367  0.0609  64   ALA B C   
9436  O O   . ALA B 66   ? 0.3908 0.6226 0.4080 -0.1057 0.0391  0.0594  64   ALA B O   
9437  C CB  . ALA B 66   ? 0.3413 0.5535 0.3551 -0.1201 0.0299  0.0625  64   ALA B CB  
9438  N N   . ALA B 67   ? 0.3650 0.6083 0.3919 -0.1087 0.0366  0.0602  65   ALA B N   
9439  C CA  . ALA B 67   ? 0.3525 0.6045 0.3837 -0.1010 0.0394  0.0576  65   ALA B CA  
9440  C C   . ALA B 67   ? 0.4225 0.6826 0.4530 -0.0982 0.0433  0.0583  65   ALA B C   
9441  O O   . ALA B 67   ? 0.3866 0.6486 0.4168 -0.0916 0.0459  0.0560  65   ALA B O   
9442  C CB  . ALA B 67   ? 0.3991 0.6598 0.4375 -0.1002 0.0382  0.0571  65   ALA B CB  
9443  N N   . SER B 68   ? 0.4366 0.7011 0.4666 -0.1032 0.0436  0.0614  66   SER B N   
9444  C CA  . SER B 68   ? 0.4052 0.6769 0.4340 -0.1012 0.0473  0.0624  66   SER B CA  
9445  C C   . SER B 68   ? 0.4309 0.6934 0.4522 -0.1002 0.0486  0.0620  66   SER B C   
9446  O O   . SER B 68   ? 0.4480 0.7136 0.4680 -0.0946 0.0518  0.0605  66   SER B O   
9447  C CB  . SER B 68   ? 0.4391 0.7175 0.4691 -0.1074 0.0471  0.0660  66   SER B CB  
9448  N N   . THR B 69   ? 0.4081 0.6588 0.4242 -0.1056 0.0460  0.0635  67   THR B N   
9449  C CA  . THR B 69   ? 0.3768 0.6178 0.3855 -0.1048 0.0468  0.0632  67   THR B CA  
9450  C C   . THR B 69   ? 0.4101 0.6478 0.4182 -0.0976 0.0479  0.0595  67   THR B C   
9451  O O   . THR B 69   ? 0.3830 0.6196 0.3870 -0.0937 0.0504  0.0585  67   THR B O   
9452  C CB  . THR B 69   ? 0.3814 0.6094 0.3849 -0.1114 0.0432  0.0651  67   THR B CB  
9453  O OG1 . THR B 69   ? 0.4093 0.6397 0.4123 -0.1179 0.0424  0.0686  67   THR B OG1 
9454  C CG2 . THR B 69   ? 0.3462 0.5634 0.3419 -0.1101 0.0437  0.0646  67   THR B CG2 
9455  N N   . ALA B 70   ? 0.3577 0.5936 0.3695 -0.0960 0.0459  0.0575  68   ALA B N   
9456  C CA  . ALA B 70   ? 0.4002 0.6335 0.4119 -0.0892 0.0469  0.0539  68   ALA B CA  
9457  C C   . ALA B 70   ? 0.3908 0.6346 0.4054 -0.0822 0.0505  0.0521  68   ALA B C   
9458  O O   . ALA B 70   ? 0.3779 0.6191 0.3893 -0.0769 0.0525  0.0498  68   ALA B O   
9459  C CB  . ALA B 70   ? 0.3711 0.6016 0.3868 -0.0890 0.0441  0.0523  68   ALA B CB  
9460  N N   . ARG B 71   ? 0.4370 0.6924 0.4573 -0.0821 0.0514  0.0529  69   ARG B N   
9461  C CA  A ARG B 71   ? 0.4048 0.6701 0.4278 -0.0755 0.0548  0.0513  69   ARG B CA  
9462  C CA  B ARG B 71   ? 0.4051 0.6703 0.4280 -0.0754 0.0548  0.0513  69   ARG B CA  
9463  C C   . ARG B 71   ? 0.2830 0.5482 0.3004 -0.0742 0.0578  0.0519  69   ARG B C   
9464  O O   . ARG B 71   ? 0.4001 0.6658 0.4158 -0.0677 0.0602  0.0493  69   ARG B O   
9465  C CB  A ARG B 71   ? 0.4030 0.6808 0.4328 -0.0766 0.0550  0.0527  69   ARG B CB  
9466  C CB  B ARG B 71   ? 0.4033 0.6810 0.4332 -0.0762 0.0550  0.0525  69   ARG B CB  
9467  C CG  A ARG B 71   ? 0.3818 0.6705 0.4138 -0.0709 0.0587  0.0519  69   ARG B CG  
9468  C CG  B ARG B 71   ? 0.3828 0.6709 0.4150 -0.0698 0.0586  0.0512  69   ARG B CG  
9469  C CD  A ARG B 71   ? 0.3742 0.6686 0.4119 -0.0644 0.0590  0.0491  69   ARG B CD  
9470  C CD  B ARG B 71   ? 0.3678 0.6682 0.4074 -0.0697 0.0586  0.0521  69   ARG B CD  
9471  N NE  A ARG B 71   ? 0.3859 0.6856 0.4297 -0.0676 0.0566  0.0502  69   ARG B NE  
9472  N NE  B ARG B 71   ? 0.3868 0.6875 0.4312 -0.0665 0.0568  0.0499  69   ARG B NE  
9473  C CZ  A ARG B 71   ? 0.3784 0.6824 0.4274 -0.0632 0.0559  0.0483  69   ARG B CZ  
9474  C CZ  B ARG B 71   ? 0.3946 0.6971 0.4407 -0.0588 0.0581  0.0467  69   ARG B CZ  
9475  N NH1 A ARG B 71   ? 0.4027 0.7064 0.4518 -0.0555 0.0575  0.0451  69   ARG B NH1 
9476  N NH1 B ARG B 71   ? 0.3574 0.6613 0.4007 -0.0533 0.0613  0.0452  69   ARG B NH1 
9477  N NH2 A ARG B 71   ? 0.3749 0.6834 0.4289 -0.0668 0.0536  0.0496  69   ARG B NH2 
9478  N NH2 B ARG B 71   ? 0.4162 0.7187 0.4665 -0.0566 0.0562  0.0451  69   ARG B NH2 
9479  N N   . LYS B 72   ? 0.3367 0.6007 0.3509 -0.0805 0.0575  0.0552  70   LYS B N   
9480  C CA  . LYS B 72   ? 0.3657 0.6293 0.3742 -0.0799 0.0602  0.0561  70   LYS B CA  
9481  C C   . LYS B 72   ? 0.3884 0.6412 0.3902 -0.0767 0.0604  0.0540  70   LYS B C   
9482  O O   . LYS B 72   ? 0.4230 0.6769 0.4212 -0.0722 0.0632  0.0527  70   LYS B O   
9483  C CB  . LYS B 72   ? 0.3862 0.6486 0.3923 -0.0879 0.0591  0.0601  70   LYS B CB  
9484  C CG  . LYS B 72   ? 0.4232 0.6850 0.4231 -0.0882 0.0617  0.0615  70   LYS B CG  
9485  C CD  . LYS B 72   ? 0.3695 0.6306 0.3675 -0.0963 0.0605  0.0657  70   LYS B CD  
9486  C CE  . LYS B 72   ? 0.4612 0.7202 0.4523 -0.0970 0.0627  0.0673  70   LYS B CE  
9487  N NZ  . LYS B 72   ? 0.4028 0.6729 0.3953 -0.0921 0.0669  0.0666  70   LYS B NZ  
9488  N N   . LEU B 73   ? 0.3997 0.6421 0.3996 -0.0789 0.0574  0.0535  71   LEU B N   
9489  C CA  . LEU B 73   ? 0.3889 0.6210 0.3825 -0.0760 0.0574  0.0516  71   LEU B CA  
9490  C C   . LEU B 73   ? 0.3526 0.5870 0.3481 -0.0678 0.0590  0.0475  71   LEU B C   
9491  O O   . LEU B 73   ? 0.3954 0.6262 0.3860 -0.0634 0.0607  0.0457  71   LEU B O   
9492  C CB  . LEU B 73   ? 0.3508 0.5714 0.3421 -0.0807 0.0538  0.0522  71   LEU B CB  
9493  C CG  . LEU B 73   ? 0.3587 0.5741 0.3469 -0.0888 0.0516  0.0560  71   LEU B CG  
9494  C CD1 . LEU B 73   ? 0.3372 0.5419 0.3245 -0.0927 0.0477  0.0562  71   LEU B CD1 
9495  C CD2 . LEU B 73   ? 0.3958 0.6066 0.3763 -0.0898 0.0530  0.0575  71   LEU B CD2 
9496  N N   . ILE B 74   ? 0.3822 0.6223 0.3848 -0.0655 0.0584  0.0461  72   ILE B N   
9497  C CA  . ILE B 74   ? 0.3526 0.5939 0.3572 -0.0578 0.0595  0.0423  72   ILE B CA  
9498  C C   . ILE B 74   ? 0.4444 0.6939 0.4492 -0.0520 0.0630  0.0410  72   ILE B C   
9499  O O   . ILE B 74   ? 0.3911 0.6380 0.3929 -0.0459 0.0645  0.0381  72   ILE B O   
9500  C CB  . ILE B 74   ? 0.3514 0.5955 0.3630 -0.0574 0.0574  0.0413  72   ILE B CB  
9501  C CG1 . ILE B 74   ? 0.3720 0.6058 0.3821 -0.0616 0.0541  0.0416  72   ILE B CG1 
9502  C CG2 . ILE B 74   ? 0.3614 0.6089 0.3760 -0.0491 0.0588  0.0377  72   ILE B CG2 
9503  C CD1 . ILE B 74   ? 0.3597 0.5959 0.3762 -0.0637 0.0516  0.0418  72   ILE B CD1 
9504  N N   . GLU B 75   ? 0.4082 0.6677 0.4165 -0.0539 0.0643  0.0431  73   GLU B N   
9505  C CA  . GLU B 75   ? 0.4626 0.7298 0.4706 -0.0489 0.0677  0.0422  73   GLU B CA  
9506  C C   . GLU B 75   ? 0.4502 0.7115 0.4499 -0.0480 0.0695  0.0420  73   GLU B C   
9507  O O   . GLU B 75   ? 0.5041 0.7654 0.5012 -0.0416 0.0717  0.0393  73   GLU B O   
9508  C CB  . GLU B 75   ? 0.4222 0.7008 0.4349 -0.0522 0.0687  0.0450  73   GLU B CB  
9509  N N   . ALA B 76   ? 0.4053 0.6607 0.4005 -0.0545 0.0683  0.0449  74   ALA B N   
9510  C CA  . ALA B 76   ? 0.4170 0.6656 0.4037 -0.0541 0.0696  0.0449  74   ALA B CA  
9511  C C   . ALA B 76   ? 0.4328 0.6724 0.4153 -0.0490 0.0691  0.0414  74   ALA B C   
9512  O O   . ALA B 76   ? 0.4708 0.7087 0.4482 -0.0444 0.0712  0.0395  74   ALA B O   
9513  C CB  . ALA B 76   ? 0.3889 0.6315 0.3716 -0.0622 0.0677  0.0486  74   ALA B CB  
9514  N N   . LEU B 77   ? 0.4219 0.6555 0.4062 -0.0499 0.0664  0.0405  75   LEU B N   
9515  C CA  . LEU B 77   ? 0.4648 0.6901 0.4455 -0.0453 0.0658  0.0372  75   LEU B CA  
9516  C C   . LEU B 77   ? 0.4668 0.6968 0.4495 -0.0369 0.0679  0.0335  75   LEU B C   
9517  O O   . LEU B 77   ? 0.4950 0.7204 0.4722 -0.0322 0.0690  0.0310  75   LEU B O   
9518  C CB  . LEU B 77   ? 0.4017 0.6211 0.3850 -0.0479 0.0625  0.0370  75   LEU B CB  
9519  C CG  . LEU B 77   ? 0.4165 0.6265 0.3954 -0.0548 0.0599  0.0396  75   LEU B CG  
9520  C CD1 . LEU B 77   ? 0.3687 0.5743 0.3512 -0.0570 0.0570  0.0393  75   LEU B CD1 
9521  C CD2 . LEU B 77   ? 0.4310 0.6318 0.4010 -0.0533 0.0602  0.0387  75   LEU B CD2 
9522  N N   . ARG B 78   ? 0.3960 0.6348 0.3863 -0.0350 0.0683  0.0330  76   ARG B N   
9523  C CA  . ARG B 78   ? 0.4494 0.6922 0.4418 -0.0270 0.0700  0.0296  76   ARG B CA  
9524  C C   . ARG B 78   ? 0.4443 0.6930 0.4344 -0.0237 0.0732  0.0293  76   ARG B C   
9525  O O   . ARG B 78   ? 0.4759 0.7260 0.4659 -0.0167 0.0747  0.0262  76   ARG B O   
9526  C CB  . ARG B 78   ? 0.4601 0.7100 0.4612 -0.0259 0.0691  0.0293  76   ARG B CB  
9527  C CG  . ARG B 78   ? 0.4552 0.6989 0.4585 -0.0266 0.0662  0.0282  76   ARG B CG  
9528  C CD  . ARG B 78   ? 0.4541 0.7048 0.4656 -0.0258 0.0652  0.0281  76   ARG B CD  
9529  N NE  . ARG B 78   ? 0.4667 0.7118 0.4799 -0.0230 0.0632  0.0256  76   ARG B NE  
9530  C CZ  . ARG B 78   ? 0.5273 0.7763 0.5470 -0.0221 0.0618  0.0252  76   ARG B CZ  
9531  N NH1 . ARG B 78   ? 0.5288 0.7874 0.5540 -0.0239 0.0619  0.0271  76   ARG B NH1 
9532  N NH2 . ARG B 78   ? 0.4978 0.7410 0.5183 -0.0192 0.0603  0.0228  76   ARG B NH2 
9533  N N   . GLY B 79   ? 0.4585 0.7101 0.4463 -0.0285 0.0743  0.0324  77   GLY B N   
9534  C CA  . GLY B 79   ? 0.4945 0.7516 0.4797 -0.0256 0.0775  0.0323  77   GLY B CA  
9535  C C   . GLY B 79   ? 0.5539 0.8032 0.5301 -0.0229 0.0786  0.0307  77   GLY B C   
9536  O O   . GLY B 79   ? 0.4300 0.6831 0.4035 -0.0193 0.0814  0.0299  77   GLY B O   
9537  N N   . LYS B 80   ? 0.5574 0.7959 0.5287 -0.0244 0.0765  0.0301  78   LYS B N   
9538  C CA  . LYS B 80   ? 0.5418 0.7722 0.5039 -0.0229 0.0771  0.0290  78   LYS B CA  
9539  C C   . LYS B 80   ? 0.5811 0.8027 0.5406 -0.0180 0.0757  0.0252  78   LYS B C   
9540  O O   . LYS B 80   ? 0.5693 0.7908 0.5340 -0.0162 0.0742  0.0236  78   LYS B O   
9541  C CB  . LYS B 80   ? 0.5783 0.8036 0.5355 -0.0302 0.0760  0.0327  78   LYS B CB  
9542  C CG  . LYS B 80   ? 0.4939 0.7138 0.4533 -0.0358 0.0726  0.0344  78   LYS B CG  
9543  C CD  . LYS B 80   ? 0.5069 0.7240 0.4628 -0.0436 0.0716  0.0387  78   LYS B CD  
9544  C CE  . LYS B 80   ? 0.3750 0.5843 0.3314 -0.0489 0.0680  0.0402  78   LYS B CE  
9545  N NZ  . LYS B 80   ? 0.4248 0.6309 0.3780 -0.0565 0.0668  0.0444  78   LYS B NZ  
9546  N N   . HIS B 81   ? 0.7396 0.9537 0.6907 -0.0160 0.0760  0.0237  79   HIS B N   
9547  C CA  . HIS B 81   ? 0.7310 0.9363 0.6782 -0.0110 0.0747  0.0198  79   HIS B CA  
9548  C C   . HIS B 81   ? 0.6708 0.8796 0.6215 -0.0034 0.0759  0.0160  79   HIS B C   
9549  O O   . HIS B 81   ? 0.6768 0.8868 0.6241 0.0013  0.0780  0.0141  79   HIS B O   
9550  C CB  . HIS B 81   ? 0.6385 0.8370 0.5868 -0.0144 0.0715  0.0202  79   HIS B CB  
9551  N N   . GLY B 85   ? 0.5556 0.6983 0.4802 0.0124  0.0618  -0.0012 83   GLY B N   
9552  C CA  . GLY B 85   ? 0.4800 0.6106 0.3975 0.0138  0.0592  -0.0035 83   GLY B CA  
9553  C C   . GLY B 85   ? 0.5251 0.6489 0.4431 0.0193  0.0575  -0.0078 83   GLY B C   
9554  O O   . GLY B 85   ? 0.4589 0.5823 0.3724 0.0245  0.0590  -0.0107 83   GLY B O   
9555  N N   . VAL B 86   ? 0.5193 0.6377 0.4426 0.0182  0.0544  -0.0081 84   VAL B N   
9556  C CA  . VAL B 86   ? 0.4834 0.5960 0.4082 0.0231  0.0528  -0.0118 84   VAL B CA  
9557  C C   . VAL B 86   ? 0.4597 0.5812 0.3879 0.0281  0.0560  -0.0133 84   VAL B C   
9558  O O   . VAL B 86   ? 0.4563 0.5744 0.3825 0.0335  0.0560  -0.0168 84   VAL B O   
9559  C CB  . VAL B 86   ? 0.4502 0.5560 0.3802 0.0206  0.0491  -0.0115 84   VAL B CB  
9560  N N   . GLU B 87   ? 0.4843 0.6174 0.4177 0.0262  0.0586  -0.0107 85   GLU B N   
9561  C CA  . GLU B 87   ? 0.5203 0.6630 0.4575 0.0310  0.0616  -0.0119 85   GLU B CA  
9562  C C   . GLU B 87   ? 0.4552 0.6006 0.3861 0.0360  0.0646  -0.0141 85   GLU B C   
9563  O O   . GLU B 87   ? 0.4618 0.6077 0.3927 0.0421  0.0656  -0.0172 85   GLU B O   
9564  C CB  . GLU B 87   ? 0.5808 0.7362 0.5247 0.0274  0.0638  -0.0083 85   GLU B CB  
9565  N N   . GLY B 88   ? 0.4600 0.6069 0.3850 0.0338  0.0661  -0.0126 86   GLY B N   
9566  C CA  . GLY B 88   ? 0.4623 0.6115 0.3804 0.0385  0.0690  -0.0148 86   GLY B CA  
9567  C C   . GLY B 88   ? 0.3889 0.5259 0.3008 0.0430  0.0668  -0.0190 86   GLY B C   
9568  O O   . GLY B 88   ? 0.4015 0.5388 0.3105 0.0486  0.0684  -0.0219 86   GLY B O   
9569  N N   . LEU B 89   ? 0.4289 0.5542 0.3395 0.0402  0.0626  -0.0193 87   LEU B N   
9570  C CA  . LEU B 89   ? 0.4247 0.5382 0.3302 0.0439  0.0600  -0.0232 87   LEU B CA  
9571  C C   . LEU B 89   ? 0.3362 0.4486 0.2461 0.0490  0.0596  -0.0261 87   LEU B C   
9572  O O   . LEU B 89   ? 0.3725 0.4810 0.2778 0.0545  0.0599  -0.0296 87   LEU B O   
9573  C CB  . LEU B 89   ? 0.4417 0.5441 0.3459 0.0394  0.0555  -0.0224 87   LEU B CB  
9574  C CG  . LEU B 89   ? 0.4574 0.5473 0.3573 0.0422  0.0522  -0.0261 87   LEU B CG  
9575  C CD1 . LEU B 89   ? 0.5110 0.5987 0.4016 0.0458  0.0535  -0.0285 87   LEU B CD1 
9576  C CD2 . LEU B 89   ? 0.5058 0.5867 0.4058 0.0373  0.0480  -0.0247 87   LEU B CD2 
9577  N N   . VAL B 90   ? 0.3705 0.4860 0.2887 0.0471  0.0587  -0.0245 88   VAL B N   
9578  C CA  . VAL B 90   ? 0.3852 0.5000 0.3079 0.0516  0.0583  -0.0268 88   VAL B CA  
9579  C C   . VAL B 90   ? 0.4324 0.5562 0.3547 0.0575  0.0622  -0.0283 88   VAL B C   
9580  O O   . VAL B 90   ? 0.4284 0.5482 0.3492 0.0632  0.0621  -0.0317 88   VAL B O   
9581  C CB  . VAL B 90   ? 0.4119 0.5295 0.3437 0.0480  0.0569  -0.0244 88   VAL B CB  
9582  C CG1 . VAL B 90   ? 0.4506 0.5699 0.3873 0.0528  0.0570  -0.0262 88   VAL B CG1 
9583  C CG2 . VAL B 90   ? 0.3815 0.4887 0.3133 0.0435  0.0527  -0.0236 88   VAL B CG2 
9584  N N   . GLN B 91   ? 0.4242 0.5595 0.3479 0.0560  0.0657  -0.0258 89   GLN B N   
9585  C CA  . GLN B 91   ? 0.4340 0.5751 0.3594 0.0600  0.0680  -0.0264 89   GLN B CA  
9586  C C   . GLN B 91   ? 0.4063 0.5412 0.3234 0.0640  0.0685  -0.0294 89   GLN B C   
9587  O O   . GLN B 91   ? 0.4546 0.5878 0.3714 0.0693  0.0688  -0.0319 89   GLN B O   
9588  C CB  . GLN B 91   ? 0.4839 0.6377 0.4140 0.0564  0.0708  -0.0225 89   GLN B CB  
9589  N N   . GLU B 92   ? 0.3919 0.5229 0.3017 0.0614  0.0683  -0.0291 90   GLU B N   
9590  C CA  . GLU B 92   ? 0.4028 0.5284 0.3043 0.0647  0.0688  -0.0317 90   GLU B CA  
9591  C C   . GLU B 92   ? 0.4017 0.5156 0.2996 0.0694  0.0662  -0.0360 90   GLU B C   
9592  O O   . GLU B 92   ? 0.4358 0.5469 0.3302 0.0740  0.0668  -0.0386 90   GLU B O   
9593  C CB  . GLU B 92   ? 0.4532 0.5764 0.3475 0.0608  0.0687  -0.0303 90   GLU B CB  
9594  C CG  . GLU B 92   ? 0.4771 0.5945 0.3625 0.0640  0.0691  -0.0330 90   GLU B CG  
9595  C CD  . GLU B 92   ? 0.4845 0.5986 0.3622 0.0601  0.0687  -0.0317 90   GLU B CD  
9596  O OE1 . GLU B 92   ? 0.5712 0.6875 0.4504 0.0549  0.0680  -0.0286 90   GLU B OE1 
9597  O OE2 . GLU B 92   ? 0.5046 0.6137 0.3745 0.0623  0.0688  -0.0338 90   GLU B OE2 
9598  N N   . TYR B 93   ? 0.4107 0.5176 0.3093 0.0682  0.0631  -0.0367 91   TYR B N   
9599  C CA  . TYR B 93   ? 0.4007 0.4958 0.2959 0.0721  0.0603  -0.0407 91   TYR B CA  
9600  C C   . TYR B 93   ? 0.3859 0.4810 0.2883 0.0746  0.0594  -0.0415 91   TYR B C   
9601  O O   . TYR B 93   ? 0.3961 0.4812 0.2966 0.0770  0.0566  -0.0443 91   TYR B O   
9602  C CB  . TYR B 93   ? 0.3561 0.4415 0.2458 0.0694  0.0571  -0.0415 91   TYR B CB  
9603  C CG  . TYR B 93   ? 0.3732 0.4566 0.2544 0.0681  0.0576  -0.0415 91   TYR B CG  
9604  C CD1 . TYR B 93   ? 0.3552 0.4307 0.2290 0.0716  0.0568  -0.0448 91   TYR B CD1 
9605  C CD2 . TYR B 93   ? 0.4150 0.5034 0.2960 0.0627  0.0584  -0.0379 91   TYR B CD2 
9606  C CE1 . TYR B 93   ? 0.3674 0.4410 0.2333 0.0704  0.0572  -0.0448 91   TYR B CE1 
9607  C CE2 . TYR B 93   ? 0.4067 0.4935 0.2793 0.0618  0.0590  -0.0378 91   TYR B CE2 
9608  C CZ  . TYR B 93   ? 0.4084 0.4878 0.2736 0.0656  0.0584  -0.0413 91   TYR B CZ  
9609  O OH  . TYR B 93   ? 0.4421 0.5194 0.2991 0.0644  0.0587  -0.0412 91   TYR B OH  
9610  N N   . SER B 94   ? 0.3483 0.4541 0.2586 0.0741  0.0614  -0.0390 92   SER B N   
9611  C CA  . SER B 94   ? 0.3243 0.4310 0.2415 0.0766  0.0607  -0.0394 92   SER B CA  
9612  C C   . SER B 94   ? 0.3612 0.4594 0.2791 0.0755  0.0574  -0.0404 92   SER B C   
9613  O O   . SER B 94   ? 0.3598 0.4507 0.2780 0.0789  0.0555  -0.0429 92   SER B O   
9614  C CB  . SER B 94   ? 0.3849 0.4890 0.3007 0.0826  0.0611  -0.0421 92   SER B CB  
9615  O OG  . SER B 94   ? 0.4236 0.5358 0.3385 0.0837  0.0642  -0.0413 92   SER B OG  
9616  N N   . LEU B 95   ? 0.2965 0.3944 0.2155 0.0697  0.0561  -0.0381 93   LEU B N   
9617  C CA  . LEU B 95   ? 0.2887 0.3767 0.2101 0.0667  0.0519  -0.0380 93   LEU B CA  
9618  C C   . LEU B 95   ? 0.3046 0.3971 0.2350 0.0658  0.0515  -0.0364 93   LEU B C   
9619  O O   . LEU B 95   ? 0.3227 0.4262 0.2583 0.0643  0.0538  -0.0338 93   LEU B O   
9620  C CB  . LEU B 95   ? 0.2914 0.3764 0.2114 0.0602  0.0501  -0.0356 93   LEU B CB  
9621  C CG  . LEU B 95   ? 0.3392 0.4193 0.2502 0.0601  0.0500  -0.0368 93   LEU B CG  
9622  C CD1 . LEU B 95   ? 0.3232 0.3994 0.2338 0.0537  0.0475  -0.0344 93   LEU B CD1 
9623  C CD2 . LEU B 95   ? 0.3446 0.4142 0.2497 0.0646  0.0482  -0.0410 93   LEU B CD2 
9624  N N   . SER B 96   ? 0.2794 0.3633 0.2116 0.0667  0.0485  -0.0378 94   SER B N   
9625  C CA  . SER B 96   ? 0.2937 0.3799 0.2339 0.0645  0.0473  -0.0359 94   SER B CA  
9626  C C   . SER B 96   ? 0.2924 0.3774 0.2350 0.0576  0.0454  -0.0330 94   SER B C   
9627  O O   . SER B 96   ? 0.2705 0.3511 0.2083 0.0548  0.0445  -0.0328 94   SER B O   
9628  C CB  . SER B 96   ? 0.2751 0.3518 0.2160 0.0672  0.0446  -0.0382 94   SER B CB  
9629  O OG  . SER B 96   ? 0.2567 0.3222 0.1939 0.0645  0.0413  -0.0391 94   SER B OG  
9630  N N   . SER B 97   ? 0.2559 0.3446 0.2057 0.0549  0.0447  -0.0308 95   SER B N   
9631  C CA  . SER B 97   ? 0.2628 0.3496 0.2148 0.0486  0.0427  -0.0282 95   SER B CA  
9632  C C   . SER B 97   ? 0.2621 0.3366 0.2107 0.0472  0.0392  -0.0296 95   SER B C   
9633  O O   . SER B 97   ? 0.2579 0.3292 0.2036 0.0435  0.0381  -0.0285 95   SER B O   
9634  C CB  . SER B 97   ? 0.3135 0.4050 0.2735 0.0465  0.0423  -0.0262 95   SER B CB  
9635  O OG  . SER B 97   ? 0.3900 0.4938 0.3534 0.0467  0.0453  -0.0244 95   SER B OG  
9636  N N   . GLN B 98   ? 0.2462 0.3136 0.1949 0.0502  0.0374  -0.0319 96   GLN B N   
9637  C CA  . GLN B 98   ? 0.2374 0.2934 0.1833 0.0488  0.0340  -0.0332 96   GLN B CA  
9638  C C   . GLN B 98   ? 0.2324 0.2838 0.1703 0.0495  0.0339  -0.0348 96   GLN B C   
9639  O O   . GLN B 98   ? 0.2388 0.2837 0.1744 0.0464  0.0314  -0.0346 96   GLN B O   
9640  C CB  . GLN B 98   ? 0.2418 0.2914 0.1890 0.0520  0.0323  -0.0354 96   GLN B CB  
9641  C CG  . GLN B 98   ? 0.2315 0.2829 0.1861 0.0504  0.0314  -0.0337 96   GLN B CG  
9642  C CD  . GLN B 98   ? 0.2455 0.2936 0.2023 0.0450  0.0290  -0.0318 96   GLN B CD  
9643  O OE1 . GLN B 98   ? 0.3014 0.3546 0.2599 0.0413  0.0297  -0.0294 96   GLN B OE1 
9644  N NE2 . GLN B 98   ? 0.2456 0.2849 0.2025 0.0444  0.0261  -0.0328 96   GLN B NE2 
9645  N N   . GLU B 99   ? 0.2345 0.2893 0.1683 0.0536  0.0365  -0.0364 97   GLU B N   
9646  C CA  . GLU B 99   ? 0.2344 0.2854 0.1602 0.0543  0.0365  -0.0379 97   GLU B CA  
9647  C C   . GLU B 99   ? 0.2950 0.3501 0.2197 0.0497  0.0372  -0.0351 97   GLU B C   
9648  O O   . GLU B 99   ? 0.2705 0.3196 0.1902 0.0477  0.0354  -0.0354 97   GLU B O   
9649  C CB  . GLU B 99   ? 0.2820 0.3362 0.2036 0.0600  0.0394  -0.0403 97   GLU B CB  
9650  C CG  . GLU B 99   ? 0.2601 0.3070 0.1803 0.0648  0.0381  -0.0436 97   GLU B CG  
9651  C CD  . GLU B 99   ? 0.2809 0.3323 0.1982 0.0710  0.0412  -0.0457 97   GLU B CD  
9652  O OE1 . GLU B 99   ? 0.2930 0.3539 0.2097 0.0715  0.0446  -0.0445 97   GLU B OE1 
9653  O OE2 . GLU B 99   ? 0.2924 0.3376 0.2076 0.0754  0.0403  -0.0486 97   GLU B OE2 
9654  N N   . GLY B 100  ? 0.2489 0.3142 0.1780 0.0479  0.0397  -0.0324 98   GLY B N   
9655  C CA  . GLY B 100  ? 0.2823 0.3511 0.2106 0.0430  0.0402  -0.0295 98   GLY B CA  
9656  C C   . GLY B 100  ? 0.2688 0.3306 0.1985 0.0383  0.0366  -0.0281 98   GLY B C   
9657  O O   . GLY B 100  ? 0.2674 0.3258 0.1928 0.0355  0.0355  -0.0273 98   GLY B O   
9658  N N   . VAL B 101  ? 0.2504 0.3099 0.1860 0.0376  0.0347  -0.0279 99   VAL B N   
9659  C CA  . VAL B 101  ? 0.2496 0.3025 0.1868 0.0335  0.0314  -0.0268 99   VAL B CA  
9660  C C   . VAL B 101  ? 0.2565 0.2993 0.1881 0.0343  0.0287  -0.0290 99   VAL B C   
9661  O O   . VAL B 101  ? 0.2640 0.3027 0.1931 0.0310  0.0268  -0.0280 99   VAL B O   
9662  C CB  . VAL B 101  ? 0.2295 0.2821 0.1739 0.0331  0.0302  -0.0264 99   VAL B CB  
9663  C CG1 . VAL B 101  ? 0.2722 0.3173 0.2179 0.0297  0.0267  -0.0257 99   VAL B CG1 
9664  C CG2 . VAL B 101  ? 0.2502 0.3126 0.2000 0.0314  0.0324  -0.0238 99   VAL B CG2 
9665  N N   . ALA B 102  ? 0.2455 0.2841 0.1751 0.0385  0.0283  -0.0321 100  ALA B N   
9666  C CA  . ALA B 102  ? 0.2531 0.2821 0.1776 0.0392  0.0256  -0.0343 100  ALA B CA  
9667  C C   . ALA B 102  ? 0.2528 0.2812 0.1701 0.0386  0.0260  -0.0344 100  ALA B C   
9668  O O   . ALA B 102  ? 0.2652 0.2871 0.1792 0.0365  0.0233  -0.0345 100  ALA B O   
9669  C CB  . ALA B 102  ? 0.2544 0.2795 0.1773 0.0441  0.0255  -0.0376 100  ALA B CB  
9670  N N   . LEU B 103  ? 0.2372 0.2726 0.1518 0.0404  0.0295  -0.0342 101  LEU B N   
9671  C CA  . LEU B 103  ? 0.2589 0.2943 0.1662 0.0399  0.0303  -0.0341 101  LEU B CA  
9672  C C   . LEU B 103  ? 0.2946 0.3304 0.2023 0.0346  0.0291  -0.0309 101  LEU B C   
9673  O O   . LEU B 103  ? 0.2798 0.3104 0.1819 0.0332  0.0273  -0.0311 101  LEU B O   
9674  C CB  . LEU B 103  ? 0.2720 0.3163 0.1773 0.0428  0.0346  -0.0342 101  LEU B CB  
9675  C CG  . LEU B 103  ? 0.2789 0.3248 0.1768 0.0422  0.0360  -0.0337 101  LEU B CG  
9676  C CD1 . LEU B 103  ? 0.3362 0.3728 0.2263 0.0445  0.0339  -0.0369 101  LEU B CD1 
9677  C CD2 . LEU B 103  ? 0.2840 0.3403 0.1814 0.0448  0.0406  -0.0333 101  LEU B CD2 
9678  N N   . MET B 104  ? 0.2602 0.3017 0.1742 0.0316  0.0299  -0.0281 102  MET B N   
9679  C CA  . MET B 104  ? 0.2815 0.3228 0.1956 0.0266  0.0287  -0.0250 102  MET B CA  
9680  C C   . MET B 104  ? 0.2823 0.3145 0.1969 0.0247  0.0245  -0.0253 102  MET B C   
9681  O O   . MET B 104  ? 0.2929 0.3216 0.2042 0.0219  0.0228  -0.0240 102  MET B O   
9682  C CB  . MET B 104  ? 0.2914 0.3405 0.2120 0.0238  0.0304  -0.0220 102  MET B CB  
9683  C CG  . MET B 104  ? 0.3137 0.3730 0.2341 0.0252  0.0346  -0.0211 102  MET B CG  
9684  S SD  . MET B 104  ? 0.4093 0.4707 0.3209 0.0247  0.0365  -0.0204 102  MET B SD  
9685  C CE  . MET B 104  ? 0.4968 0.5573 0.4092 0.0180  0.0349  -0.0162 102  MET B CE  
9686  N N   . CYS B 105  ? 0.2537 0.2820 0.1724 0.0262  0.0228  -0.0270 103  CYS B N   
9687  C CA  . CYS B 105  ? 0.2768 0.2967 0.1959 0.0247  0.0189  -0.0276 103  CYS B CA  
9688  C C   . CYS B 105  ? 0.2679 0.2815 0.1796 0.0259  0.0172  -0.0296 103  CYS B C   
9689  O O   . CYS B 105  ? 0.2948 0.3036 0.2046 0.0234  0.0145  -0.0288 103  CYS B O   
9690  C CB  . CYS B 105  ? 0.2339 0.2511 0.1581 0.0265  0.0178  -0.0292 103  CYS B CB  
9691  S SG  . CYS B 105  ? 0.2641 0.2870 0.1971 0.0246  0.0187  -0.0269 103  CYS B SG  
9692  N N   . LEU B 106  ? 0.2623 0.2755 0.1697 0.0298  0.0186  -0.0322 104  LEU B N   
9693  C CA  . LEU B 106  ? 0.2604 0.2677 0.1600 0.0309  0.0171  -0.0343 104  LEU B CA  
9694  C C   . LEU B 106  ? 0.2865 0.2957 0.1812 0.0285  0.0176  -0.0322 104  LEU B C   
9695  O O   . LEU B 106  ? 0.3236 0.3270 0.2138 0.0271  0.0149  -0.0324 104  LEU B O   
9696  C CB  . LEU B 106  ? 0.2685 0.2760 0.1640 0.0358  0.0190  -0.0374 104  LEU B CB  
9697  C CG  . LEU B 106  ? 0.2907 0.2925 0.1772 0.0372  0.0177  -0.0396 104  LEU B CG  
9698  C CD1 . LEU B 106  ? 0.3596 0.3520 0.2456 0.0365  0.0133  -0.0413 104  LEU B CD1 
9699  C CD2 . LEU B 106  ? 0.3288 0.3322 0.2105 0.0421  0.0204  -0.0424 104  LEU B CD2 
9700  N N   . ALA B 107  ? 0.2822 0.2995 0.1774 0.0278  0.0210  -0.0301 105  ALA B N   
9701  C CA  . ALA B 107  ? 0.3047 0.3241 0.1949 0.0253  0.0217  -0.0279 105  ALA B CA  
9702  C C   . ALA B 107  ? 0.3286 0.3444 0.2208 0.0209  0.0188  -0.0253 105  ALA B C   
9703  O O   . ALA B 107  ? 0.3499 0.3617 0.2367 0.0193  0.0170  -0.0247 105  ALA B O   
9704  C CB  . ALA B 107  ? 0.3077 0.3370 0.1991 0.0251  0.0260  -0.0258 105  ALA B CB  
9705  N N   . GLU B 108  ? 0.3181 0.3352 0.2178 0.0190  0.0182  -0.0238 106  GLU B N   
9706  C CA  . GLU B 108  ? 0.3205 0.3338 0.2225 0.0152  0.0153  -0.0217 106  GLU B CA  
9707  C C   . GLU B 108  ? 0.3792 0.3840 0.2782 0.0155  0.0114  -0.0234 106  GLU B C   
9708  O O   . GLU B 108  ? 0.3670 0.3684 0.2631 0.0132  0.0092  -0.0219 106  GLU B O   
9709  C CB  . GLU B 108  ? 0.3317 0.3469 0.2423 0.0141  0.0151  -0.0208 106  GLU B CB  
9710  C CG  . GLU B 108  ? 0.3648 0.3750 0.2783 0.0111  0.0117  -0.0193 106  GLU B CG  
9711  C CD  . GLU B 108  ? 0.4061 0.4169 0.3275 0.0109  0.0112  -0.0192 106  GLU B CD  
9712  O OE1 . GLU B 108  ? 0.3646 0.3804 0.2895 0.0125  0.0135  -0.0198 106  GLU B OE1 
9713  O OE2 . GLU B 108  ? 0.4330 0.4394 0.3571 0.0093  0.0084  -0.0187 106  GLU B OE2 
9714  N N   . ALA B 109  ? 0.3203 0.3215 0.2200 0.0184  0.0103  -0.0264 107  ALA B N   
9715  C CA  . ALA B 109  ? 0.3445 0.3379 0.2418 0.0186  0.0065  -0.0281 107  ALA B CA  
9716  C C   . ALA B 109  ? 0.3424 0.3332 0.2309 0.0190  0.0059  -0.0288 107  ALA B C   
9717  O O   . ALA B 109  ? 0.3749 0.3608 0.2607 0.0174  0.0028  -0.0284 107  ALA B O   
9718  C CB  . ALA B 109  ? 0.3699 0.3601 0.2697 0.0213  0.0056  -0.0311 107  ALA B CB  
9719  N N   . LEU B 110  ? 0.3341 0.3283 0.2178 0.0214  0.0089  -0.0299 108  LEU B N   
9720  C CA  . LEU B 110  ? 0.3387 0.3307 0.2133 0.0220  0.0087  -0.0306 108  LEU B CA  
9721  C C   . LEU B 110  ? 0.3623 0.3557 0.2345 0.0185  0.0085  -0.0272 108  LEU B C   
9722  O O   . LEU B 110  ? 0.3917 0.3809 0.2575 0.0179  0.0064  -0.0273 108  LEU B O   
9723  C CB  . LEU B 110  ? 0.3588 0.3549 0.2291 0.0255  0.0124  -0.0325 108  LEU B CB  
9724  C CG  . LEU B 110  ? 0.3393 0.3318 0.2095 0.0295  0.0120  -0.0363 108  LEU B CG  
9725  C CD1 . LEU B 110  ? 0.3536 0.3518 0.2216 0.0331  0.0162  -0.0377 108  LEU B CD1 
9726  C CD2 . LEU B 110  ? 0.3790 0.3632 0.2427 0.0302  0.0085  -0.0389 108  LEU B CD2 
9727  N N   . LEU B 111  ? 0.3671 0.3660 0.2441 0.0162  0.0104  -0.0242 109  LEU B N   
9728  C CA  . LEU B 111  ? 0.4227 0.4224 0.2974 0.0126  0.0101  -0.0208 109  LEU B CA  
9729  C C   . LEU B 111  ? 0.4357 0.4292 0.3121 0.0101  0.0058  -0.0197 109  LEU B C   
9730  O O   . LEU B 111  ? 0.4844 0.4767 0.3575 0.0075  0.0048  -0.0171 109  LEU B O   
9731  C CB  . LEU B 111  ? 0.4200 0.4273 0.2992 0.0106  0.0133  -0.0179 109  LEU B CB  
9732  C CG  . LEU B 111  ? 0.3816 0.3961 0.2579 0.0125  0.0177  -0.0183 109  LEU B CG  
9733  C CD1 . LEU B 111  ? 0.3981 0.4203 0.2804 0.0106  0.0205  -0.0157 109  LEU B CD1 
9734  C CD2 . LEU B 111  ? 0.4503 0.4647 0.3177 0.0120  0.0185  -0.0174 109  LEU B CD2 
9735  N N   . ARG B 112  ? 0.4172 0.4070 0.2987 0.0110  0.0034  -0.0214 110  ARG B N   
9736  C CA  . ARG B 112  ? 0.4551 0.4389 0.3376 0.0092  -0.0008 -0.0208 110  ARG B CA  
9737  C C   . ARG B 112  ? 0.4612 0.4397 0.3365 0.0100  -0.0035 -0.0222 110  ARG B C   
9738  O O   . ARG B 112  ? 0.5007 0.4748 0.3755 0.0084  -0.0070 -0.0213 110  ARG B O   
9739  C CB  . ARG B 112  ? 0.4583 0.4404 0.3485 0.0098  -0.0025 -0.0220 110  ARG B CB  
9740  C CG  . ARG B 112  ? 0.4831 0.4698 0.3806 0.0086  -0.0005 -0.0203 110  ARG B CG  
9741  C CD  . ARG B 112  ? 0.5860 0.5703 0.4906 0.0086  -0.0026 -0.0210 110  ARG B CD  
9742  N NE  . ARG B 112  ? 0.5354 0.5195 0.4423 0.0113  -0.0021 -0.0239 110  ARG B NE  
9743  C CZ  . ARG B 112  ? 0.5625 0.5508 0.4741 0.0124  0.0004  -0.0242 110  ARG B CZ  
9744  N NH1 . ARG B 112  ? 0.5869 0.5804 0.5016 0.0108  0.0027  -0.0219 110  ARG B NH1 
9745  N NH2 . ARG B 112  ? 0.6132 0.6002 0.5263 0.0149  0.0005  -0.0268 110  ARG B NH2 
9746  N N   . ILE B 113  ? 0.4353 0.4141 0.3047 0.0125  -0.0020 -0.0245 111  ILE B N   
9747  C CA  . ILE B 113  ? 0.4342 0.4083 0.2953 0.0131  -0.0042 -0.0257 111  ILE B CA  
9748  C C   . ILE B 113  ? 0.4701 0.4465 0.3255 0.0112  -0.0028 -0.0228 111  ILE B C   
9749  O O   . ILE B 113  ? 0.5124 0.4940 0.3650 0.0119  0.0011  -0.0224 111  ILE B O   
9750  C CB  . ILE B 113  ? 0.4412 0.4142 0.2979 0.0166  -0.0033 -0.0295 111  ILE B CB  
9751  C CG1 . ILE B 113  ? 0.4356 0.4058 0.2980 0.0182  -0.0047 -0.0320 111  ILE B CG1 
9752  C CG2 . ILE B 113  ? 0.4722 0.4402 0.3196 0.0171  -0.0056 -0.0307 111  ILE B CG2 
9753  C CD1 . ILE B 113  ? 0.4511 0.4197 0.3095 0.0218  -0.0037 -0.0358 111  ILE B CD1 
9754  N N   . PRO B 114  ? 0.5779 0.5509 0.4313 0.0088  -0.0058 -0.0207 112  PRO B N   
9755  C CA  . PRO B 114  ? 0.5186 0.4936 0.3670 0.0066  -0.0044 -0.0174 112  PRO B CA  
9756  C C   . PRO B 114  ? 0.5077 0.4825 0.3462 0.0079  -0.0034 -0.0183 112  PRO B C   
9757  O O   . PRO B 114  ? 0.5647 0.5437 0.3994 0.0068  -0.0004 -0.0161 112  PRO B O   
9758  C CB  . PRO B 114  ? 0.4946 0.4649 0.3440 0.0041  -0.0085 -0.0152 112  PRO B CB  
9759  C CG  . PRO B 114  ? 0.5531 0.5183 0.4044 0.0056  -0.0123 -0.0180 112  PRO B CG  
9760  C CD  . PRO B 114  ? 0.5181 0.4854 0.3743 0.0079  -0.0105 -0.0209 112  PRO B CD  
9761  N N   . ASP B 115  ? 0.5383 0.5085 0.3724 0.0101  -0.0056 -0.0215 113  ASP B N   
9762  C CA  . ASP B 115  ? 0.6067 0.5759 0.4306 0.0114  -0.0050 -0.0226 113  ASP B CA  
9763  C C   . ASP B 115  ? 0.5929 0.5669 0.4153 0.0144  -0.0006 -0.0248 113  ASP B C   
9764  O O   . ASP B 115  ? 0.5824 0.5555 0.4079 0.0169  -0.0005 -0.0280 113  ASP B O   
9765  C CB  . ASP B 115  ? 0.5817 0.5438 0.4015 0.0125  -0.0095 -0.0252 113  ASP B CB  
9766  C CG  . ASP B 115  ? 0.6593 0.6197 0.4682 0.0142  -0.0090 -0.0268 113  ASP B CG  
9767  O OD1 . ASP B 115  ? 0.7533 0.7160 0.5564 0.0129  -0.0074 -0.0243 113  ASP B OD1 
9768  O OD2 . ASP B 115  ? 0.7011 0.6580 0.5071 0.0167  -0.0104 -0.0305 113  ASP B OD2 
9769  N N   . THR B 116  ? 0.5787 0.5577 0.3961 0.0141  0.0031  -0.0231 114  THR B N   
9770  C CA  . THR B 116  ? 0.6109 0.5954 0.4267 0.0171  0.0076  -0.0250 114  THR B CA  
9771  C C   . THR B 116  ? 0.6230 0.6031 0.4331 0.0210  0.0067  -0.0295 114  THR B C   
9772  O O   . THR B 116  ? 0.5689 0.5507 0.3816 0.0241  0.0086  -0.0323 114  THR B O   
9773  C CB  . THR B 116  ? 0.6505 0.6410 0.4609 0.0160  0.0114  -0.0222 114  THR B CB  
9774  O OG1 . THR B 116  ? 0.7317 0.7265 0.5481 0.0123  0.0125  -0.0181 114  THR B OG1 
9775  C CG2 . THR B 116  ? 0.6593 0.6560 0.4677 0.0195  0.0162  -0.0243 114  THR B CG2 
9776  N N   . ALA B 117  ? 0.6226 0.5967 0.4250 0.0209  0.0035  -0.0304 115  ALA B N   
9777  C CA  . ALA B 117  ? 0.6135 0.5829 0.4096 0.0244  0.0024  -0.0348 115  ALA B CA  
9778  C C   . ALA B 117  ? 0.5448 0.5097 0.3471 0.0257  -0.0004 -0.0377 115  ALA B C   
9779  O O   . ALA B 117  ? 0.6195 0.5834 0.4206 0.0291  0.0008  -0.0413 115  ALA B O   
9780  C CB  . ALA B 117  ? 0.5664 0.5301 0.3531 0.0236  -0.0009 -0.0349 115  ALA B CB  
9781  N N   . THR B 118  ? 0.5510 0.5130 0.3598 0.0230  -0.0039 -0.0362 116  THR B N   
9782  C CA  . THR B 118  ? 0.5480 0.5062 0.3632 0.0238  -0.0065 -0.0386 116  THR B CA  
9783  C C   . THR B 118  ? 0.5548 0.5178 0.3769 0.0256  -0.0029 -0.0392 116  THR B C   
9784  O O   . THR B 118  ? 0.5518 0.5122 0.3756 0.0280  -0.0034 -0.0424 116  THR B O   
9785  C CB  . THR B 118  ? 0.5545 0.5099 0.3757 0.0206  -0.0105 -0.0364 116  THR B CB  
9786  O OG1 . THR B 118  ? 0.6325 0.5831 0.4472 0.0193  -0.0142 -0.0362 116  THR B OG1 
9787  C CG2 . THR B 118  ? 0.5511 0.5034 0.3795 0.0212  -0.0128 -0.0385 116  THR B CG2 
9788  N N   . ARG B 119  ? 0.5277 0.4977 0.3538 0.0242  0.0005  -0.0362 117  ARG B N   
9789  C CA  . ARG B 119  ? 0.5090 0.4844 0.3420 0.0257  0.0039  -0.0364 117  ARG B CA  
9790  C C   . ARG B 119  ? 0.5209 0.4986 0.3488 0.0299  0.0073  -0.0393 117  ARG B C   
9791  O O   . ARG B 119  ? 0.4695 0.4465 0.3004 0.0327  0.0079  -0.0419 117  ARG B O   
9792  C CB  . ARG B 119  ? 0.4742 0.4567 0.3119 0.0230  0.0066  -0.0323 117  ARG B CB  
9793  C CG  . ARG B 119  ? 0.4425 0.4309 0.2882 0.0240  0.0097  -0.0321 117  ARG B CG  
9794  C CD  . ARG B 119  ? 0.4551 0.4511 0.3031 0.0215  0.0129  -0.0283 117  ARG B CD  
9795  N NE  . ARG B 119  ? 0.4760 0.4698 0.3257 0.0173  0.0103  -0.0251 117  ARG B NE  
9796  C CZ  . ARG B 119  ? 0.5706 0.5672 0.4172 0.0146  0.0114  -0.0218 117  ARG B CZ  
9797  N NH1 . ARG B 119  ? 0.4816 0.4836 0.3232 0.0153  0.0151  -0.0211 117  ARG B NH1 
9798  N NH2 . ARG B 119  ? 0.5907 0.5843 0.4390 0.0111  0.0086  -0.0191 117  ARG B NH2 
9799  N N   . ASP B 120  ? 0.4906 0.4709 0.3106 0.0305  0.0096  -0.0388 118  ASP B N   
9800  C CA  . ASP B 120  ? 0.5225 0.5052 0.3370 0.0347  0.0130  -0.0416 118  ASP B CA  
9801  C C   . ASP B 120  ? 0.5797 0.5544 0.3896 0.0379  0.0104  -0.0461 118  ASP B C   
9802  O O   . ASP B 120  ? 0.5298 0.5051 0.3388 0.0419  0.0125  -0.0490 118  ASP B O   
9803  C CB  . ASP B 120  ? 0.5566 0.5434 0.3630 0.0345  0.0158  -0.0400 118  ASP B CB  
9804  C CG  . ASP B 120  ? 0.6381 0.6340 0.4491 0.0319  0.0193  -0.0357 118  ASP B CG  
9805  O OD1 . ASP B 120  ? 0.6374 0.6366 0.4577 0.0308  0.0199  -0.0344 118  ASP B OD1 
9806  O OD2 . ASP B 120  ? 0.6835 0.6832 0.4888 0.0308  0.0215  -0.0337 118  ASP B OD2 
9807  N N   . ALA B 121  ? 0.5699 0.5368 0.3766 0.0362  0.0056  -0.0468 119  ALA B N   
9808  C CA  . ALA B 121  ? 0.6070 0.5659 0.4096 0.0387  0.0027  -0.0511 119  ALA B CA  
9809  C C   . ALA B 121  ? 0.5584 0.5153 0.3692 0.0396  0.0016  -0.0526 119  ALA B C   
9810  O O   . ALA B 121  ? 0.5698 0.5230 0.3783 0.0430  0.0017  -0.0562 119  ALA B O   
9811  C CB  . ALA B 121  ? 0.5622 0.5140 0.3598 0.0364  -0.0023 -0.0512 119  ALA B CB  
9812  N N   . LEU B 122  ? 0.5392 0.4979 0.3593 0.0365  0.0005  -0.0499 120  LEU B N   
9813  C CA  . LEU B 122  ? 0.5271 0.4844 0.3552 0.0372  -0.0003 -0.0510 120  LEU B CA  
9814  C C   . LEU B 122  ? 0.4983 0.4609 0.3287 0.0406  0.0042  -0.0520 120  LEU B C   
9815  O O   . LEU B 122  ? 0.5170 0.4764 0.3491 0.0432  0.0038  -0.0547 120  LEU B O   
9816  C CB  . LEU B 122  ? 0.5169 0.4760 0.3541 0.0333  -0.0019 -0.0477 120  LEU B CB  
9817  C CG  . LEU B 122  ? 0.5315 0.4888 0.3770 0.0335  -0.0031 -0.0486 120  LEU B CG  
9818  C CD1 . LEU B 122  ? 0.5770 0.5258 0.4207 0.0334  -0.0077 -0.0512 120  LEU B CD1 
9819  C CD2 . LEU B 122  ? 0.4874 0.4487 0.3420 0.0303  -0.0032 -0.0451 120  LEU B CD2 
9820  N N   . ILE B 123  ? 0.4548 0.4256 0.2852 0.0407  0.0083  -0.0498 121  ILE B N   
9821  C CA  . ILE B 123  ? 0.4970 0.4739 0.3295 0.0441  0.0128  -0.0505 121  ILE B CA  
9822  C C   . ILE B 123  ? 0.5616 0.5349 0.3863 0.0490  0.0136  -0.0547 121  ILE B C   
9823  O O   . ILE B 123  ? 0.5335 0.5058 0.3604 0.0523  0.0144  -0.0570 121  ILE B O   
9824  C CB  . ILE B 123  ? 0.4643 0.4510 0.2977 0.0428  0.0169  -0.0471 121  ILE B CB  
9825  C CG1 . ILE B 123  ? 0.3969 0.3870 0.2391 0.0384  0.0162  -0.0432 121  ILE B CG1 
9826  C CG2 . ILE B 123  ? 0.4722 0.4658 0.3061 0.0469  0.0216  -0.0481 121  ILE B CG2 
9827  C CD1 . ILE B 123  ? 0.3982 0.3967 0.2407 0.0362  0.0194  -0.0395 121  ILE B CD1 
9828  N N   . ARG B 124  ? 0.5013 0.4724 0.3164 0.0495  0.0134  -0.0557 122  ARG B N   
9829  C CA  . ARG B 124  ? 0.5915 0.5599 0.3982 0.0544  0.0148  -0.0596 122  ARG B CA  
9830  C C   . ARG B 124  ? 0.5981 0.5559 0.4026 0.0559  0.0107  -0.0635 122  ARG B C   
9831  O O   . ARG B 124  ? 0.6989 0.6542 0.5005 0.0603  0.0118  -0.0669 122  ARG B O   
9832  C CB  . ARG B 124  ? 0.6292 0.5982 0.4258 0.0544  0.0157  -0.0595 122  ARG B CB  
9833  N N   . ASP B 125  ? 0.6207 0.5723 0.4267 0.0523  0.0059  -0.0629 123  ASP B N   
9834  C CA  . ASP B 125  ? 0.6857 0.6271 0.4888 0.0531  0.0016  -0.0664 123  ASP B CA  
9835  C C   . ASP B 125  ? 0.6751 0.6140 0.4873 0.0522  -0.0003 -0.0665 123  ASP B C   
9836  O O   . ASP B 125  ? 0.7126 0.6437 0.5228 0.0537  -0.0029 -0.0696 123  ASP B O   
9837  C CB  . ASP B 125  ? 0.7096 0.6453 0.5076 0.0499  -0.0028 -0.0662 123  ASP B CB  
9838  C CG  . ASP B 125  ? 0.7723 0.7100 0.5608 0.0504  -0.0012 -0.0660 123  ASP B CG  
9839  O OD1 . ASP B 125  ? 0.7702 0.7111 0.5536 0.0543  0.0027  -0.0675 123  ASP B OD1 
9840  O OD2 . ASP B 125  ? 0.8501 0.7863 0.6361 0.0472  -0.0039 -0.0642 123  ASP B OD2 
9841  N N   . LYS B 126  ? 0.5792 0.5240 0.4009 0.0497  0.0008  -0.0631 124  LYS B N   
9842  C CA  . LYS B 126  ? 0.6315 0.5739 0.4616 0.0486  -0.0012 -0.0630 124  LYS B CA  
9843  C C   . LYS B 126  ? 0.6267 0.5763 0.4647 0.0499  0.0025  -0.0615 124  LYS B C   
9844  O O   . LYS B 126  ? 0.6526 0.5996 0.4942 0.0517  0.0022  -0.0630 124  LYS B O   
9845  C CB  . LYS B 126  ? 0.6387 0.5794 0.4737 0.0437  -0.0051 -0.0605 124  LYS B CB  
9846  N N   . ILE B 127  ? 0.5415 0.4999 0.3822 0.0489  0.0059  -0.0584 125  ILE B N   
9847  C CA  . ILE B 127  ? 0.5216 0.4872 0.3704 0.0495  0.0090  -0.0567 125  ILE B CA  
9848  C C   . ILE B 127  ? 0.5632 0.5317 0.4093 0.0547  0.0127  -0.0589 125  ILE B C   
9849  O O   . ILE B 127  ? 0.5273 0.4965 0.3785 0.0568  0.0136  -0.0596 125  ILE B O   
9850  C CB  . ILE B 127  ? 0.4638 0.4377 0.3169 0.0461  0.0109  -0.0524 125  ILE B CB  
9851  C CG1 . ILE B 127  ? 0.5068 0.4773 0.3615 0.0414  0.0072  -0.0504 125  ILE B CG1 
9852  C CG2 . ILE B 127  ? 0.4523 0.4329 0.3143 0.0463  0.0135  -0.0506 125  ILE B CG2 
9853  C CD1 . ILE B 127  ? 0.5434 0.5087 0.4043 0.0400  0.0037  -0.0507 125  ILE B CD1 
9854  N N   . ALA B 128  ? 0.4847 0.4552 0.3228 0.0570  0.0150  -0.0600 126  ALA B N   
9855  C CA  . ALA B 128  ? 0.4958 0.4700 0.3311 0.0622  0.0189  -0.0620 126  ALA B CA  
9856  C C   . ALA B 128  ? 0.5960 0.5620 0.4285 0.0662  0.0173  -0.0662 126  ALA B C   
9857  O O   . ALA B 128  ? 0.5544 0.5232 0.3875 0.0706  0.0201  -0.0677 126  ALA B O   
9858  C CB  . ALA B 128  ? 0.5294 0.5072 0.3561 0.0637  0.0215  -0.0624 126  ALA B CB  
9859  N N   . ASP B 129  ? 0.6089 0.5648 0.4384 0.0647  0.0127  -0.0680 127  ASP B N   
9860  C CA  . ASP B 129  ? 0.7368 0.6838 0.5641 0.0677  0.0105  -0.0716 127  ASP B CA  
9861  C C   . ASP B 129  ? 0.7749 0.7206 0.6116 0.0663  0.0090  -0.0706 127  ASP B C   
9862  O O   . ASP B 129  ? 0.8898 0.8267 0.7256 0.0668  0.0058  -0.0729 127  ASP B O   
9863  C CB  . ASP B 129  ? 0.7372 0.6739 0.5566 0.0665  0.0062  -0.0741 127  ASP B CB  
9864  N N   . GLY B 130  ? 0.7622 0.7164 0.6075 0.0644  0.0111  -0.0672 128  GLY B N   
9865  C CA  . GLY B 130  ? 0.7625 0.7164 0.6165 0.0635  0.0102  -0.0661 128  GLY B CA  
9866  C C   . GLY B 130  ? 0.7707 0.7202 0.6294 0.0585  0.0061  -0.0646 128  GLY B C   
9867  O O   . GLY B 130  ? 0.7432 0.6960 0.6104 0.0564  0.0061  -0.0622 128  GLY B O   
9868  N N   . ASN B 131  ? 0.8420 0.7844 0.6954 0.0567  0.0026  -0.0658 129  ASN B N   
9869  C CA  . ASN B 131  ? 0.8349 0.7731 0.6926 0.0522  -0.0016 -0.0646 129  ASN B CA  
9870  C C   . ASN B 131  ? 0.7945 0.7395 0.6579 0.0481  -0.0011 -0.0606 129  ASN B C   
9871  O O   . ASN B 131  ? 0.8593 0.8028 0.7207 0.0451  -0.0034 -0.0597 129  ASN B O   
9872  C CB  . ASN B 131  ? 0.8377 0.7672 0.6879 0.0513  -0.0055 -0.0669 129  ASN B CB  
9873  N N   . TRP B 132  ? 0.6792 0.6317 0.5496 0.0481  0.0019  -0.0583 130  TRP B N   
9874  C CA  . TRP B 132  ? 0.5949 0.5539 0.4704 0.0444  0.0026  -0.0545 130  TRP B CA  
9875  C C   . TRP B 132  ? 0.6025 0.5597 0.4854 0.0408  -0.0003 -0.0528 130  TRP B C   
9876  O O   . TRP B 132  ? 0.6871 0.6467 0.5725 0.0374  -0.0012 -0.0502 130  TRP B O   
9877  C CB  . TRP B 132  ? 0.5535 0.5220 0.4326 0.0458  0.0071  -0.0527 130  TRP B CB  
9878  C CG  . TRP B 132  ? 0.4603 0.4307 0.3460 0.0476  0.0084  -0.0528 130  TRP B CG  
9879  C CD1 . TRP B 132  ? 0.4524 0.4232 0.3368 0.0520  0.0105  -0.0549 130  TRP B CD1 
9880  C CD2 . TRP B 132  ? 0.4125 0.3848 0.3070 0.0450  0.0076  -0.0505 130  TRP B CD2 
9881  N NE1 . TRP B 132  ? 0.4142 0.3869 0.3059 0.0523  0.0109  -0.0540 130  TRP B NE1 
9882  C CE2 . TRP B 132  ? 0.3750 0.3487 0.2729 0.0480  0.0092  -0.0514 130  TRP B CE2 
9883  C CE3 . TRP B 132  ? 0.3888 0.3615 0.2881 0.0406  0.0056  -0.0480 130  TRP B CE3 
9884  C CZ2 . TRP B 132  ? 0.3558 0.3313 0.2618 0.0465  0.0089  -0.0497 130  TRP B CZ2 
9885  C CZ3 . TRP B 132  ? 0.3815 0.3561 0.2888 0.0394  0.0055  -0.0464 130  TRP B CZ3 
9886  C CH2 . TRP B 132  ? 0.3717 0.3476 0.2821 0.0422  0.0071  -0.0473 130  TRP B CH2 
9887  N N   . LYS B 133  ? 0.6388 0.5918 0.5251 0.0416  -0.0017 -0.0541 131  LYS B N   
9888  C CA  . LYS B 133  ? 0.6775 0.6293 0.5711 0.0384  -0.0042 -0.0524 131  LYS B CA  
9889  C C   . LYS B 133  ? 0.7799 0.7270 0.6717 0.0352  -0.0081 -0.0522 131  LYS B C   
9890  O O   . LYS B 133  ? 0.7857 0.7345 0.6827 0.0320  -0.0095 -0.0499 131  LYS B O   
9891  C CB  . LYS B 133  ? 0.6328 0.5807 0.5296 0.0399  -0.0049 -0.0539 131  LYS B CB  
9892  N N   . SER B 134  ? 0.8408 0.7819 0.7249 0.0362  -0.0100 -0.0548 132  SER B N   
9893  C CA  . SER B 134  ? 0.8045 0.7409 0.6867 0.0334  -0.0141 -0.0549 132  SER B CA  
9894  C C   . SER B 134  ? 0.8524 0.7929 0.7336 0.0311  -0.0140 -0.0525 132  SER B C   
9895  O O   . SER B 134  ? 0.8692 0.8099 0.7544 0.0280  -0.0163 -0.0505 132  SER B O   
9896  C CB  . SER B 134  ? 0.7469 0.6758 0.6208 0.0352  -0.0162 -0.0584 132  SER B CB  
9897  N N   . HIS B 135  ? 0.8681 0.8118 0.7436 0.0328  -0.0113 -0.0525 133  HIS B N   
9898  C CA  . HIS B 135  ? 0.8646 0.8108 0.7373 0.0307  -0.0115 -0.0504 133  HIS B CA  
9899  C C   . HIS B 135  ? 0.8709 0.8232 0.7508 0.0281  -0.0103 -0.0467 133  HIS B C   
9900  O O   . HIS B 135  ? 0.8929 0.8456 0.7725 0.0255  -0.0119 -0.0447 133  HIS B O   
9901  C CB  . HIS B 135  ? 0.8192 0.7676 0.6840 0.0332  -0.0086 -0.0513 133  HIS B CB  
9902  N N   . LEU B 136  ? 0.8232 0.7799 0.7094 0.0288  -0.0077 -0.0458 134  LEU B N   
9903  C CA  . LEU B 136  ? 0.7470 0.7094 0.6395 0.0265  -0.0064 -0.0425 134  LEU B CA  
9904  C C   . LEU B 136  ? 0.7149 0.6778 0.6158 0.0260  -0.0066 -0.0420 134  LEU B C   
9905  O O   . LEU B 136  ? 0.7520 0.7136 0.6576 0.0236  -0.0091 -0.0407 134  LEU B O   
9906  C CB  . LEU B 136  ? 0.6619 0.6312 0.5531 0.0275  -0.0021 -0.0412 134  LEU B CB  
9907  C CG  . LEU B 136  ? 0.6183 0.5881 0.5008 0.0284  -0.0010 -0.0416 134  LEU B CG  
9908  C CD1 . LEU B 136  ? 0.5072 0.4844 0.3893 0.0299  0.0036  -0.0406 134  LEU B CD1 
9909  C CD2 . LEU B 136  ? 0.6408 0.6091 0.5209 0.0253  -0.0033 -0.0396 134  LEU B CD2 
9910  N N   . ARG B 140  ? 0.4943 0.4597 0.4271 0.0160  -0.0132 -0.0342 138  ARG B N   
9911  C CA  . ARG B 140  ? 0.5874 0.5582 0.5233 0.0159  -0.0101 -0.0324 138  ARG B CA  
9912  C C   . ARG B 140  ? 0.5786 0.5519 0.5120 0.0184  -0.0069 -0.0336 138  ARG B C   
9913  O O   . ARG B 140  ? 0.4668 0.4391 0.3939 0.0197  -0.0065 -0.0348 138  ARG B O   
9914  C CB  . ARG B 140  ? 0.5510 0.5240 0.4856 0.0139  -0.0099 -0.0300 138  ARG B CB  
9915  N N   . SER B 141  ? 0.4375 0.4141 0.3756 0.0192  -0.0049 -0.0332 139  SER B N   
9916  C CA  . SER B 141  ? 0.3707 0.3502 0.3071 0.0218  -0.0019 -0.0342 139  SER B CA  
9917  C C   . SER B 141  ? 0.3950 0.3786 0.3270 0.0218  0.0003  -0.0332 139  SER B C   
9918  O O   . SER B 141  ? 0.3895 0.3757 0.3223 0.0194  0.0005  -0.0309 139  SER B O   
9919  C CB  . SER B 141  ? 0.3996 0.3832 0.3424 0.0221  -0.0001 -0.0332 139  SER B CB  
9920  O OG  . SER B 141  ? 0.3914 0.3788 0.3331 0.0247  0.0029  -0.0339 139  SER B OG  
9921  N N   . LEU B 142  ? 0.3262 0.3101 0.2533 0.0245  0.0020  -0.0350 140  LEU B N   
9922  C CA  . LEU B 142  ? 0.3232 0.3121 0.2466 0.0249  0.0047  -0.0341 140  LEU B CA  
9923  C C   . LEU B 142  ? 0.2774 0.2734 0.2059 0.0240  0.0074  -0.0318 140  LEU B C   
9924  O O   . LEU B 142  ? 0.2896 0.2903 0.2164 0.0228  0.0092  -0.0301 140  LEU B O   
9925  C CB  . LEU B 142  ? 0.3209 0.3096 0.2394 0.0287  0.0064  -0.0367 140  LEU B CB  
9926  C CG  . LEU B 142  ? 0.3719 0.3629 0.2837 0.0291  0.0081  -0.0365 140  LEU B CG  
9927  C CD1 . LEU B 142  ? 0.4215 0.4065 0.3282 0.0276  0.0050  -0.0370 140  LEU B CD1 
9928  C CD2 . LEU B 142  ? 0.3793 0.3714 0.2871 0.0332  0.0104  -0.0389 140  LEU B CD2 
9929  N N   . PHE B 143  ? 0.2711 0.2682 0.2057 0.0243  0.0075  -0.0317 141  PHE B N   
9930  C CA  . PHE B 143  ? 0.2573 0.2612 0.1964 0.0242  0.0102  -0.0301 141  PHE B CA  
9931  C C   . PHE B 143  ? 0.2610 0.2661 0.2054 0.0208  0.0092  -0.0276 141  PHE B C   
9932  O O   . PHE B 143  ? 0.2699 0.2798 0.2190 0.0205  0.0107  -0.0264 141  PHE B O   
9933  C CB  . PHE B 143  ? 0.2569 0.2618 0.1984 0.0275  0.0114  -0.0318 141  PHE B CB  
9934  C CG  . PHE B 143  ? 0.2581 0.2609 0.1940 0.0311  0.0121  -0.0344 141  PHE B CG  
9935  C CD1 . PHE B 143  ? 0.2562 0.2631 0.1875 0.0323  0.0145  -0.0344 141  PHE B CD1 
9936  C CD2 . PHE B 143  ? 0.2449 0.2414 0.1798 0.0333  0.0104  -0.0369 141  PHE B CD2 
9937  C CE1 . PHE B 143  ? 0.2675 0.2723 0.1932 0.0358  0.0153  -0.0370 141  PHE B CE1 
9938  C CE2 . PHE B 143  ? 0.2639 0.2578 0.1930 0.0367  0.0110  -0.0395 141  PHE B CE2 
9939  C CZ  . PHE B 143  ? 0.2544 0.2525 0.1790 0.0381  0.0135  -0.0397 141  PHE B CZ  
9940  N N   . VAL B 144  ? 0.2806 0.2816 0.2242 0.0184  0.0066  -0.0269 142  VAL B N   
9941  C CA  . VAL B 144  ? 0.2833 0.2846 0.2314 0.0154  0.0055  -0.0247 142  VAL B CA  
9942  C C   . VAL B 144  ? 0.2828 0.2904 0.2325 0.0137  0.0078  -0.0224 142  VAL B C   
9943  O O   . VAL B 144  ? 0.3058 0.3154 0.2605 0.0124  0.0079  -0.0211 142  VAL B O   
9944  C CB  . VAL B 144  ? 0.3135 0.3097 0.2595 0.0135  0.0025  -0.0243 142  VAL B CB  
9945  C CG1 . VAL B 144  ? 0.3644 0.3611 0.3143 0.0106  0.0016  -0.0219 142  VAL B CG1 
9946  C CG2 . VAL B 144  ? 0.3625 0.3531 0.3086 0.0147  0.0000  -0.0263 142  VAL B CG2 
9947  N N   . ASN B 145  ? 0.2882 0.2990 0.2336 0.0136  0.0096  -0.0217 143  ASN B N   
9948  C CA  . ASN B 145  ? 0.2985 0.3154 0.2452 0.0115  0.0117  -0.0193 143  ASN B CA  
9949  C C   . ASN B 145  ? 0.2768 0.3005 0.2245 0.0136  0.0149  -0.0197 143  ASN B C   
9950  O O   . ASN B 145  ? 0.2917 0.3213 0.2391 0.0123  0.0171  -0.0179 143  ASN B O   
9951  C CB  . ASN B 145  ? 0.3618 0.3783 0.3033 0.0093  0.0115  -0.0177 143  ASN B CB  
9952  C CG  . ASN B 145  ? 0.4277 0.4390 0.3694 0.0066  0.0086  -0.0164 143  ASN B CG  
9953  O OD1 . ASN B 145  ? 0.4381 0.4488 0.3845 0.0052  0.0076  -0.0155 143  ASN B OD1 
9954  N ND2 . ASN B 145  ? 0.4081 0.4154 0.3445 0.0062  0.0071  -0.0164 143  ASN B ND2 
9955  N N   . ALA B 146  ? 0.2625 0.2857 0.2118 0.0169  0.0153  -0.0219 144  ALA B N   
9956  C CA  . ALA B 146  ? 0.2855 0.3150 0.2354 0.0195  0.0183  -0.0225 144  ALA B CA  
9957  C C   . ALA B 146  ? 0.2780 0.3143 0.2335 0.0180  0.0198  -0.0204 144  ALA B C   
9958  O O   . ALA B 146  ? 0.2893 0.3326 0.2452 0.0192  0.0226  -0.0200 144  ALA B O   
9959  C CB  . ALA B 146  ? 0.2784 0.3048 0.2285 0.0235  0.0180  -0.0253 144  ALA B CB  
9960  N N   . ALA B 147  ? 0.2897 0.3242 0.2494 0.0155  0.0181  -0.0192 145  ALA B N   
9961  C CA  . ALA B 147  ? 0.2740 0.3148 0.2385 0.0137  0.0194  -0.0172 145  ALA B CA  
9962  C C   . ALA B 147  ? 0.3082 0.3541 0.2707 0.0109  0.0210  -0.0149 145  ALA B C   
9963  O O   . ALA B 147  ? 0.3044 0.3579 0.2693 0.0106  0.0232  -0.0137 145  ALA B O   
9964  C CB  . ALA B 147  ? 0.3205 0.3578 0.2891 0.0115  0.0172  -0.0164 145  ALA B CB  
9965  N N   . THR B 148  ? 0.2883 0.3302 0.2465 0.0089  0.0198  -0.0142 146  THR B N   
9966  C CA  . THR B 148  ? 0.2923 0.3382 0.2479 0.0061  0.0211  -0.0119 146  THR B CA  
9967  C C   . THR B 148  ? 0.2881 0.3401 0.2408 0.0084  0.0242  -0.0124 146  THR B C   
9968  O O   . THR B 148  ? 0.3071 0.3668 0.2610 0.0071  0.0265  -0.0107 146  THR B O   
9969  C CB  . THR B 148  ? 0.4128 0.4523 0.3641 0.0037  0.0189  -0.0110 146  THR B CB  
9970  O OG1 . THR B 148  ? 0.4204 0.4550 0.3748 0.0018  0.0163  -0.0105 146  THR B OG1 
9971  C CG2 . THR B 148  ? 0.4268 0.4700 0.3749 0.0006  0.0203  -0.0084 146  THR B CG2 
9972  N N   . TRP B 149  ? 0.2856 0.3343 0.2344 0.0119  0.0241  -0.0149 147  TRP B N   
9973  C CA  . TRP B 149  ? 0.2824 0.3365 0.2281 0.0147  0.0271  -0.0158 147  TRP B CA  
9974  C C   . TRP B 149  ? 0.2558 0.3171 0.2064 0.0171  0.0293  -0.0163 147  TRP B C   
9975  O O   . TRP B 149  ? 0.2657 0.3347 0.2156 0.0182  0.0323  -0.0158 147  TRP B O   
9976  C CB  . TRP B 149  ? 0.2674 0.3157 0.2076 0.0180  0.0263  -0.0186 147  TRP B CB  
9977  C CG  . TRP B 149  ? 0.2828 0.3255 0.2175 0.0157  0.0245  -0.0180 147  TRP B CG  
9978  C CD1 . TRP B 149  ? 0.3115 0.3457 0.2446 0.0154  0.0212  -0.0191 147  TRP B CD1 
9979  C CD2 . TRP B 149  ? 0.3150 0.3606 0.2455 0.0133  0.0257  -0.0159 147  TRP B CD2 
9980  N NE1 . TRP B 149  ? 0.3010 0.3324 0.2289 0.0131  0.0202  -0.0179 147  TRP B NE1 
9981  C CE2 . TRP B 149  ? 0.3112 0.3492 0.2372 0.0118  0.0230  -0.0159 147  TRP B CE2 
9982  C CE3 . TRP B 149  ? 0.3416 0.3956 0.2715 0.0122  0.0289  -0.0139 147  TRP B CE3 
9983  C CZ2 . TRP B 149  ? 0.3592 0.3974 0.2800 0.0093  0.0232  -0.0139 147  TRP B CZ2 
9984  C CZ3 . TRP B 149  ? 0.3490 0.4033 0.2737 0.0095  0.0293  -0.0119 147  TRP B CZ3 
9985  C CH2 . TRP B 149  ? 0.4083 0.4544 0.3283 0.0081  0.0264  -0.0120 147  TRP B CH2 
9986  N N   . GLY B 150  ? 0.2604 0.3196 0.2158 0.0181  0.0280  -0.0171 148  GLY B N   
9987  C CA  . GLY B 150  ? 0.2784 0.3445 0.2388 0.0201  0.0298  -0.0172 148  GLY B CA  
9988  C C   . GLY B 150  ? 0.2599 0.3346 0.2236 0.0168  0.0315  -0.0143 148  GLY B C   
9989  O O   . GLY B 150  ? 0.2824 0.3657 0.2479 0.0184  0.0342  -0.0139 148  GLY B O   
9990  N N   . LEU B 151  ? 0.2987 0.3713 0.2632 0.0122  0.0299  -0.0121 149  LEU B N   
9991  C CA  A LEU B 151  ? 0.3261 0.4060 0.2930 0.0084  0.0313  -0.0091 149  LEU B CA  
9992  C CA  B LEU B 151  ? 0.3261 0.4061 0.2931 0.0084  0.0313  -0.0091 149  LEU B CA  
9993  C C   . LEU B 151  ? 0.3284 0.4144 0.2914 0.0081  0.0340  -0.0081 149  LEU B C   
9994  O O   . LEU B 151  ? 0.3662 0.4616 0.3318 0.0074  0.0364  -0.0065 149  LEU B O   
9995  C CB  A LEU B 151  ? 0.3362 0.4111 0.3036 0.0036  0.0288  -0.0072 149  LEU B CB  
9996  C CB  B LEU B 151  ? 0.3363 0.4110 0.3036 0.0037  0.0287  -0.0072 149  LEU B CB  
9997  C CG  A LEU B 151  ? 0.3247 0.3998 0.2978 0.0020  0.0274  -0.0065 149  LEU B CG  
9998  C CG  B LEU B 151  ? 0.3503 0.4305 0.3210 -0.0007 0.0291  -0.0043 149  LEU B CG  
9999  C CD1 A LEU B 151  ? 0.3938 0.4628 0.3662 -0.0023 0.0249  -0.0048 149  LEU B CD1 
10000 C CD1 B LEU B 151  ? 0.3382 0.4259 0.3148 0.0007  0.0305  -0.0044 149  LEU B CD1 
10001 C CD2 A LEU B 151  ? 0.3389 0.4242 0.3162 0.0010  0.0296  -0.0049 149  LEU B CD2 
10002 C CD2 B LEU B 151  ? 0.3592 0.4321 0.3304 -0.0041 0.0261  -0.0033 149  LEU B CD2 
10003 N N   . VAL B 152  ? 0.3251 0.4061 0.2820 0.0085  0.0336  -0.0088 150  VAL B N   
10004 C CA  . VAL B 152  ? 0.3360 0.4223 0.2884 0.0083  0.0362  -0.0078 150  VAL B CA  
10005 C C   . VAL B 152  ? 0.3198 0.4136 0.2728 0.0129  0.0393  -0.0094 150  VAL B C   
10006 O O   . VAL B 152  ? 0.3549 0.4579 0.3081 0.0123  0.0423  -0.0078 150  VAL B O   
10007 C CB  . VAL B 152  ? 0.2855 0.3640 0.2307 0.0082  0.0348  -0.0085 150  VAL B CB  
10008 C CG1 . VAL B 152  ? 0.3752 0.4591 0.3153 0.0088  0.0377  -0.0080 150  VAL B CG1 
10009 C CG2 . VAL B 152  ? 0.3657 0.4380 0.3102 0.0035  0.0320  -0.0065 150  VAL B CG2 
10010 N N   . VAL B 153  ? 0.3107 0.4007 0.2638 0.0176  0.0387  -0.0125 151  VAL B N   
10011 C CA  . VAL B 153  ? 0.3092 0.4047 0.2616 0.0227  0.0415  -0.0144 151  VAL B CA  
10012 C C   . VAL B 153  ? 0.3246 0.4289 0.2840 0.0238  0.0431  -0.0138 151  VAL B C   
10013 O O   . VAL B 153  ? 0.3156 0.4292 0.2756 0.0258  0.0462  -0.0135 151  VAL B O   
10014 C CB  . VAL B 153  ? 0.3168 0.4036 0.2657 0.0272  0.0400  -0.0180 151  VAL B CB  
10015 C CG1 . VAL B 153  ? 0.3255 0.4172 0.2740 0.0329  0.0426  -0.0203 151  VAL B CG1 
10016 C CG2 . VAL B 153  ? 0.2886 0.3682 0.2303 0.0262  0.0387  -0.0186 151  VAL B CG2 
10017 N N   . THR B 154  ? 0.3052 0.4068 0.2697 0.0227  0.0410  -0.0136 152  THR B N   
10018 C CA  . THR B 154  ? 0.3171 0.4258 0.2879 0.0243  0.0420  -0.0133 152  THR B CA  
10019 C C   . THR B 154  ? 0.3664 0.4805 0.3424 0.0193  0.0417  -0.0102 152  THR B C   
10020 O O   . THR B 154  ? 0.4079 0.5299 0.3892 0.0200  0.0428  -0.0095 152  THR B O   
10021 C CB  . THR B 154  ? 0.3494 0.4513 0.3224 0.0274  0.0398  -0.0157 152  THR B CB  
10022 O OG1 . THR B 154  ? 0.3298 0.4252 0.3046 0.0236  0.0368  -0.0147 152  THR B OG1 
10023 C CG2 . THR B 154  ? 0.3576 0.4519 0.3250 0.0316  0.0394  -0.0188 152  THR B CG2 
10024 N N   . GLY B 155  ? 0.3254 0.4352 0.2999 0.0142  0.0399  -0.0083 153  GLY B N   
10025 C CA  . GLY B 155  ? 0.3374 0.4504 0.3163 0.0094  0.0391  -0.0056 153  GLY B CA  
10026 C C   . GLY B 155  ? 0.3677 0.4761 0.3510 0.0092  0.0366  -0.0062 153  GLY B C   
10027 O O   . GLY B 155  ? 0.4072 0.5182 0.3943 0.0055  0.0358  -0.0042 153  GLY B O   
10028 N N   . LYS B 156  ? 0.3336 0.4352 0.3162 0.0130  0.0353  -0.0089 154  LYS B N   
10029 C CA  . LYS B 156  ? 0.3649 0.4620 0.3513 0.0132  0.0330  -0.0095 154  LYS B CA  
10030 C C   . LYS B 156  ? 0.3613 0.4471 0.3447 0.0125  0.0303  -0.0106 154  LYS B C   
10031 O O   . LYS B 156  ? 0.3707 0.4517 0.3491 0.0141  0.0301  -0.0120 154  LYS B O   
10032 C CB  . LYS B 156  ? 0.4601 0.5593 0.4489 0.0185  0.0338  -0.0116 154  LYS B CB  
10033 N N   . LEU B 157  ? 0.3406 0.4224 0.3268 0.0101  0.0280  -0.0100 155  LEU B N   
10034 C CA  . LEU B 157  ? 0.3724 0.4442 0.3565 0.0092  0.0253  -0.0108 155  LEU B CA  
10035 C C   . LEU B 157  ? 0.4463 0.5140 0.4330 0.0121  0.0241  -0.0127 155  LEU B C   
10036 O O   . LEU B 157  ? 0.4579 0.5292 0.4491 0.0124  0.0242  -0.0123 155  LEU B O   
10037 C CB  . LEU B 157  ? 0.4067 0.4764 0.3916 0.0043  0.0237  -0.0087 155  LEU B CB  
10038 C CG  . LEU B 157  ? 0.4712 0.5312 0.4548 0.0035  0.0208  -0.0094 155  LEU B CG  
10039 C CD1 . LEU B 157  ? 0.4510 0.5059 0.4292 0.0040  0.0203  -0.0101 155  LEU B CD1 
10040 C CD2 . LEU B 157  ? 0.4669 0.5253 0.4520 -0.0008 0.0193  -0.0074 155  LEU B CD2 
10041 N N   . THR B 158  ? 0.4590 0.5193 0.4428 0.0141  0.0228  -0.0146 156  THR B N   
10042 C CA  . THR B 158  ? 0.4718 0.5268 0.4578 0.0158  0.0210  -0.0160 156  THR B CA  
10043 C C   . THR B 158  ? 0.4464 0.4937 0.4311 0.0133  0.0185  -0.0158 156  THR B C   
10044 O O   . THR B 158  ? 0.4396 0.4844 0.4207 0.0116  0.0180  -0.0154 156  THR B O   
10045 C CB  . THR B 158  ? 0.5284 0.5808 0.5123 0.0203  0.0214  -0.0185 156  THR B CB  
10046 O OG1 . THR B 158  ? 0.5454 0.5922 0.5242 0.0204  0.0206  -0.0195 156  THR B OG1 
10047 C CG2 . THR B 158  ? 0.5225 0.5824 0.5066 0.0232  0.0241  -0.0188 156  THR B CG2 
10048 N N   . SER B 159  ? 0.3906 0.4345 0.3784 0.0132  0.0169  -0.0161 157  SER B N   
10049 C CA  A SER B 159  ? 0.4091 0.4462 0.3963 0.0112  0.0145  -0.0160 157  SER B CA  
10050 C CA  B SER B 159  ? 0.4090 0.4461 0.3961 0.0112  0.0145  -0.0160 157  SER B CA  
10051 C C   . SER B 159  ? 0.4275 0.4584 0.4115 0.0131  0.0133  -0.0179 157  SER B C   
10052 O O   . SER B 159  ? 0.3961 0.4225 0.3777 0.0115  0.0117  -0.0178 157  SER B O   
10053 C CB  A SER B 159  ? 0.4063 0.4423 0.3979 0.0106  0.0134  -0.0158 157  SER B CB  
10054 C CB  B SER B 159  ? 0.4061 0.4420 0.3976 0.0105  0.0133  -0.0157 157  SER B CB  
10055 O OG  A SER B 159  ? 0.3992 0.4380 0.3932 0.0134  0.0144  -0.0166 157  SER B OG  
10056 O OG  B SER B 159  ? 0.3679 0.3977 0.3589 0.0088  0.0112  -0.0156 157  SER B OG  
10057 N N   . THR B 160  ? 0.3506 0.3811 0.3344 0.0165  0.0139  -0.0197 158  THR B N   
10058 C CA  . THR B 160  ? 0.2745 0.2990 0.2551 0.0183  0.0127  -0.0216 158  THR B CA  
10059 C C   . THR B 160  ? 0.2807 0.3073 0.2581 0.0214  0.0145  -0.0230 158  THR B C   
10060 O O   . THR B 160  ? 0.3057 0.3387 0.2840 0.0225  0.0167  -0.0225 158  THR B O   
10061 C CB  . THR B 160  ? 0.3338 0.3537 0.3170 0.0193  0.0111  -0.0226 158  THR B CB  
10062 O OG1 . THR B 160  ? 0.3676 0.3910 0.3538 0.0213  0.0124  -0.0228 158  THR B OG1 
10063 C CG2 . THR B 160  ? 0.3559 0.3734 0.3417 0.0164  0.0093  -0.0214 158  THR B CG2 
10064 N N   . VAL B 161  ? 0.2241 0.2452 0.1977 0.0230  0.0134  -0.0248 159  VAL B N   
10065 C CA  . VAL B 161  ? 0.2678 0.2893 0.2366 0.0256  0.0146  -0.0263 159  VAL B CA  
10066 C C   . VAL B 161  ? 0.2422 0.2597 0.2105 0.0291  0.0142  -0.0286 159  VAL B C   
10067 O O   . VAL B 161  ? 0.2247 0.2361 0.1936 0.0287  0.0119  -0.0294 159  VAL B O   
10068 C CB  . VAL B 161  ? 0.3208 0.3383 0.2848 0.0240  0.0133  -0.0265 159  VAL B CB  
10069 C CG1 . VAL B 161  ? 0.3661 0.3811 0.3247 0.0269  0.0137  -0.0288 159  VAL B CG1 
10070 C CG2 . VAL B 161  ? 0.4216 0.4436 0.3851 0.0210  0.0143  -0.0242 159  VAL B CG2 
10071 N N   . ASN B 162  ? 0.2299 0.2509 0.1971 0.0324  0.0162  -0.0296 160  ASN B N   
10072 C CA  . ASN B 162  ? 0.2211 0.2372 0.1866 0.0360  0.0157  -0.0320 160  ASN B CA  
10073 C C   . ASN B 162  ? 0.2278 0.2390 0.1869 0.0370  0.0150  -0.0339 160  ASN B C   
10074 O O   . ASN B 162  ? 0.2352 0.2488 0.1904 0.0395  0.0168  -0.0349 160  ASN B O   
10075 C CB  . ASN B 162  ? 0.2345 0.2556 0.2015 0.0396  0.0180  -0.0324 160  ASN B CB  
10076 C CG  . ASN B 162  ? 0.2398 0.2552 0.2051 0.0432  0.0172  -0.0347 160  ASN B CG  
10077 O OD1 . ASN B 162  ? 0.2373 0.2452 0.1989 0.0434  0.0153  -0.0364 160  ASN B OD1 
10078 N ND2 . ASN B 162  ? 0.2625 0.2809 0.2303 0.0461  0.0184  -0.0349 160  ASN B ND2 
10079 N N   . ASP B 163  ? 0.2271 0.2315 0.1851 0.0351  0.0122  -0.0344 161  ASP B N   
10080 C CA  . ASP B 163  ? 0.2135 0.2129 0.1654 0.0355  0.0111  -0.0361 161  ASP B CA  
10081 C C   . ASP B 163  ? 0.2292 0.2242 0.1771 0.0395  0.0111  -0.0389 161  ASP B C   
10082 O O   . ASP B 163  ? 0.2371 0.2299 0.1791 0.0408  0.0111  -0.0404 161  ASP B O   
10083 C CB  . ASP B 163  ? 0.2324 0.2263 0.1845 0.0323  0.0080  -0.0357 161  ASP B CB  
10084 C CG  . ASP B 163  ? 0.2572 0.2472 0.2136 0.0317  0.0061  -0.0357 161  ASP B CG  
10085 O OD1 . ASP B 163  ? 0.2340 0.2273 0.1953 0.0317  0.0071  -0.0346 161  ASP B OD1 
10086 O OD2 . ASP B 163  ? 0.2976 0.2813 0.2524 0.0309  0.0035  -0.0368 161  ASP B OD2 
10087 N N   . ARG B 164  ? 0.2163 0.2097 0.1669 0.0415  0.0110  -0.0395 162  ARG B N   
10088 C CA  . ARG B 164  ? 0.2207 0.2098 0.1670 0.0457  0.0111  -0.0422 162  ARG B CA  
10089 C C   . ARG B 164  ? 0.2182 0.2133 0.1623 0.0491  0.0143  -0.0428 162  ARG B C   
10090 O O   . ARG B 164  ? 0.2139 0.2062 0.1521 0.0521  0.0147  -0.0451 162  ARG B O   
10091 C CB  . ARG B 164  ? 0.2327 0.2180 0.1823 0.0469  0.0101  -0.0426 162  ARG B CB  
10092 C CG  . ARG B 164  ? 0.2336 0.2127 0.1851 0.0436  0.0069  -0.0423 162  ARG B CG  
10093 C CD  . ARG B 164  ? 0.3257 0.2988 0.2722 0.0423  0.0047  -0.0437 162  ARG B CD  
10094 N NE  . ARG B 164  ? 0.4233 0.3916 0.3635 0.0458  0.0046  -0.0465 162  ARG B NE  
10095 C CZ  . ARG B 164  ? 0.4710 0.4356 0.4052 0.0458  0.0036  -0.0481 162  ARG B CZ  
10096 N NH1 . ARG B 164  ? 0.4762 0.4417 0.4100 0.0425  0.0025  -0.0470 162  ARG B NH1 
10097 N NH2 . ARG B 164  ? 0.4198 0.3796 0.3480 0.0493  0.0036  -0.0508 162  ARG B NH2 
10098 N N   . SER B 165  ? 0.2274 0.2310 0.1761 0.0489  0.0166  -0.0408 163  SER B N   
10099 C CA  . SER B 165  ? 0.1994 0.2102 0.1466 0.0519  0.0198  -0.0409 163  SER B CA  
10100 C C   . SER B 165  ? 0.2149 0.2275 0.1571 0.0510  0.0207  -0.0410 163  SER B C   
10101 O O   . SER B 165  ? 0.2155 0.2296 0.1531 0.0543  0.0225  -0.0426 163  SER B O   
10102 C CB  . SER B 165  ? 0.2025 0.2222 0.1561 0.0508  0.0216  -0.0384 163  SER B CB  
10103 O OG  . SER B 165  ? 0.2339 0.2619 0.1867 0.0528  0.0247  -0.0381 163  SER B OG  
10104 N N   . LEU B 166  ? 0.2265 0.2387 0.1693 0.0465  0.0194  -0.0393 164  LEU B N   
10105 C CA  . LEU B 166  ? 0.2235 0.2372 0.1615 0.0452  0.0201  -0.0390 164  LEU B CA  
10106 C C   . LEU B 166  ? 0.2432 0.2490 0.1741 0.0470  0.0185  -0.0418 164  LEU B C   
10107 O O   . LEU B 166  ? 0.2449 0.2522 0.1703 0.0485  0.0200  -0.0427 164  LEU B O   
10108 C CB  . LEU B 166  ? 0.2307 0.2451 0.1711 0.0402  0.0188  -0.0364 164  LEU B CB  
10109 C CG  . LEU B 166  ? 0.2226 0.2456 0.1685 0.0383  0.0207  -0.0337 164  LEU B CG  
10110 C CD1 . LEU B 166  ? 0.2823 0.3046 0.2307 0.0335  0.0191  -0.0314 164  LEU B CD1 
10111 C CD2 . LEU B 166  ? 0.2358 0.2667 0.1796 0.0395  0.0240  -0.0331 164  LEU B CD2 
10112 N N   . ALA B 167  ? 0.2231 0.2206 0.1538 0.0465  0.0155  -0.0431 165  ALA B N   
10113 C CA  . ALA B 167  ? 0.2192 0.2088 0.1432 0.0482  0.0137  -0.0459 165  ALA B CA  
10114 C C   . ALA B 167  ? 0.2386 0.2280 0.1584 0.0534  0.0156  -0.0484 165  ALA B C   
10115 O O   . ALA B 167  ? 0.2646 0.2520 0.1776 0.0553  0.0160  -0.0503 165  ALA B O   
10116 C CB  . ALA B 167  ? 0.2658 0.2471 0.1914 0.0466  0.0101  -0.0466 165  ALA B CB  
10117 N N   . ALA B 168  ? 0.2346 0.2262 0.1584 0.0560  0.0168  -0.0485 166  ALA B N   
10118 C CA  . ALA B 168  ? 0.2276 0.2196 0.1480 0.0614  0.0188  -0.0508 166  ALA B CA  
10119 C C   . ALA B 168  ? 0.2144 0.2147 0.1321 0.0631  0.0223  -0.0505 166  ALA B C   
10120 O O   . ALA B 168  ? 0.2519 0.2507 0.1633 0.0667  0.0234  -0.0529 166  ALA B O   
10121 C CB  . ALA B 168  ? 0.2469 0.2409 0.1729 0.0635  0.0195  -0.0504 166  ALA B CB  
10122 N N   . ALA B 169  ? 0.2305 0.2396 0.1530 0.0603  0.0240  -0.0474 167  ALA B N   
10123 C CA  . ALA B 169  ? 0.2248 0.2428 0.1456 0.0612  0.0275  -0.0466 167  ALA B CA  
10124 C C   . ALA B 169  ? 0.2661 0.2814 0.1797 0.0603  0.0272  -0.0474 167  ALA B C   
10125 O O   . ALA B 169  ? 0.2564 0.2750 0.1650 0.0632  0.0296  -0.0486 167  ALA B O   
10126 C CB  . ALA B 169  ? 0.2437 0.2706 0.1713 0.0575  0.0288  -0.0430 167  ALA B CB  
10127 N N   . LEU B 170  ? 0.2640 0.2735 0.1767 0.0562  0.0241  -0.0468 168  LEU B N   
10128 C CA  . LEU B 170  ? 0.2202 0.2268 0.1259 0.0551  0.0235  -0.0474 168  LEU B CA  
10129 C C   . LEU B 170  ? 0.2709 0.2702 0.1690 0.0592  0.0228  -0.0512 168  LEU B C   
10130 O O   . LEU B 170  ? 0.2714 0.2719 0.1629 0.0610  0.0243  -0.0524 168  LEU B O   
10131 C CB  . LEU B 170  ? 0.2626 0.2645 0.1695 0.0500  0.0202  -0.0459 168  LEU B CB  
10132 C CG  . LEU B 170  ? 0.2569 0.2567 0.1571 0.0483  0.0194  -0.0459 168  LEU B CG  
10133 C CD1 . LEU B 170  ? 0.2946 0.3032 0.1932 0.0480  0.0229  -0.0440 168  LEU B CD1 
10134 C CD2 . LEU B 170  ? 0.3037 0.2992 0.2061 0.0437  0.0160  -0.0443 168  LEU B CD2 
10135 N N   . THR B 171  ? 0.2743 0.2659 0.1730 0.0606  0.0203  -0.0532 169  THR B N   
10136 C CA  . THR B 171  ? 0.2705 0.2546 0.1620 0.0647  0.0196  -0.0569 169  THR B CA  
10137 C C   . THR B 171  ? 0.2802 0.2698 0.1690 0.0700  0.0234  -0.0583 169  THR B C   
10138 O O   . THR B 171  ? 0.2939 0.2813 0.1749 0.0729  0.0242  -0.0607 169  THR B O   
10139 C CB  . THR B 171  ? 0.2874 0.2632 0.1811 0.0652  0.0166  -0.0584 169  THR B CB  
10140 O OG1 . THR B 171  ? 0.3372 0.3081 0.2329 0.0603  0.0131  -0.0572 169  THR B OG1 
10141 C CG2 . THR B 171  ? 0.3006 0.2682 0.1868 0.0695  0.0157  -0.0623 169  THR B CG2 
10142 N N   . ARG B 172  ? 0.2713 0.2685 0.1665 0.0714  0.0258  -0.0568 170  ARG B N   
10143 C CA  . ARG B 172  ? 0.2671 0.2702 0.1606 0.0768  0.0294  -0.0581 170  ARG B CA  
10144 C C   . ARG B 172  ? 0.2846 0.2951 0.1741 0.0768  0.0324  -0.0574 170  ARG B C   
10145 O O   . ARG B 172  ? 0.2887 0.2993 0.1717 0.0812  0.0343  -0.0598 170  ARG B O   
10146 C CB  . ARG B 172  ? 0.2760 0.2863 0.1777 0.0778  0.0311  -0.0563 170  ARG B CB  
10147 C CG  . ARG B 172  ? 0.2535 0.2688 0.1539 0.0841  0.0344  -0.0580 170  ARG B CG  
10148 C CD  . ARG B 172  ? 0.2509 0.2748 0.1599 0.0845  0.0361  -0.0557 170  ARG B CD  
10149 N NE  . ARG B 172  ? 0.2345 0.2534 0.1490 0.0820  0.0332  -0.0547 170  ARG B NE  
10150 C CZ  . ARG B 172  ? 0.2344 0.2568 0.1554 0.0769  0.0323  -0.0516 170  ARG B CZ  
10151 N NH1 . ARG B 172  ? 0.2439 0.2743 0.1666 0.0735  0.0340  -0.0491 170  ARG B NH1 
10152 N NH2 . ARG B 172  ? 0.2395 0.2570 0.1649 0.0752  0.0298  -0.0510 170  ARG B NH2 
10153 N N   . LEU B 173  ? 0.2832 0.2999 0.1763 0.0719  0.0330  -0.0540 171  LEU B N   
10154 C CA  . LEU B 173  ? 0.2587 0.2833 0.1485 0.0717  0.0361  -0.0529 171  LEU B CA  
10155 C C   . LEU B 173  ? 0.2856 0.3037 0.1659 0.0719  0.0349  -0.0549 171  LEU B C   
10156 O O   . LEU B 173  ? 0.2909 0.3131 0.1656 0.0745  0.0377  -0.0558 171  LEU B O   
10157 C CB  . LEU B 173  ? 0.2730 0.3053 0.1687 0.0663  0.0368  -0.0487 171  LEU B CB  
10158 C CG  . LEU B 173  ? 0.2741 0.3014 0.1702 0.0605  0.0335  -0.0469 171  LEU B CG  
10159 C CD1 . LEU B 173  ? 0.3070 0.3348 0.1961 0.0589  0.0341  -0.0464 171  LEU B CD1 
10160 C CD2 . LEU B 173  ? 0.2918 0.3249 0.1963 0.0563  0.0336  -0.0433 171  LEU B CD2 
10161 N N   . ILE B 174  ? 0.2885 0.2967 0.1668 0.0691  0.0308  -0.0556 172  ILE B N   
10162 C CA  . ILE B 174  ? 0.2764 0.2782 0.1456 0.0692  0.0294  -0.0576 172  ILE B CA  
10163 C C   . ILE B 174  ? 0.3288 0.3251 0.1911 0.0751  0.0298  -0.0619 172  ILE B C   
10164 O O   . ILE B 174  ? 0.3545 0.3507 0.2088 0.0774  0.0312  -0.0635 172  ILE B O   
10165 C CB  . ILE B 174  ? 0.2935 0.2867 0.1627 0.0647  0.0247  -0.0572 172  ILE B CB  
10166 C CG1 . ILE B 174  ? 0.3264 0.3249 0.2013 0.0591  0.0245  -0.0530 172  ILE B CG1 
10167 C CG2 . ILE B 174  ? 0.3459 0.3317 0.2053 0.0652  0.0229  -0.0596 172  ILE B CG2 
10168 C CD1 . ILE B 174  ? 0.3458 0.3368 0.2222 0.0549  0.0200  -0.0524 172  ILE B CD1 
10169 N N   . SER B 175  ? 0.3118 0.3030 0.1766 0.0777  0.0284  -0.0637 173  SER B N   
10170 C CA  . SER B 175  ? 0.3275 0.3127 0.1857 0.0833  0.0286  -0.0677 173  SER B CA  
10171 C C   . SER B 175  ? 0.3282 0.3223 0.1874 0.0867  0.0328  -0.0671 173  SER B C   
10172 O O   . SER B 175  ? 0.3843 0.3752 0.2387 0.0896  0.0332  -0.0691 173  SER B O   
10173 C CB  . SER B 175  ? 0.3435 0.3212 0.2052 0.0847  0.0260  -0.0691 173  SER B CB  
10174 O OG  . SER B 175  ? 0.4052 0.3745 0.2675 0.0804  0.0217  -0.0690 173  SER B OG  
10175 N N   . ARG B 176  ? 0.3098 0.3153 0.1755 0.0862  0.0360  -0.0643 174  ARG B N   
10176 C CA  . ARG B 176  ? 0.2922 0.3071 0.1596 0.0891  0.0400  -0.0635 174  ARG B CA  
10177 C C   . ARG B 176  ? 0.3281 0.3490 0.1910 0.0877  0.0424  -0.0624 174  ARG B C   
10178 O O   . ARG B 176  ? 0.3658 0.3888 0.2254 0.0906  0.0444  -0.0633 174  ARG B O   
10179 C CB  . ARG B 176  ? 0.3220 0.3467 0.1988 0.0890  0.0421  -0.0609 174  ARG B CB  
10180 C CG  . ARG B 176  ? 0.3193 0.3539 0.1991 0.0922  0.0458  -0.0600 174  ARG B CG  
10181 C CD  . ARG B 176  ? 0.3010 0.3444 0.1903 0.0919  0.0472  -0.0575 174  ARG B CD  
10182 N NE  . ARG B 176  ? 0.3102 0.3625 0.2032 0.0875  0.0487  -0.0543 174  ARG B NE  
10183 C CZ  . ARG B 176  ? 0.3390 0.3914 0.2363 0.0842  0.0473  -0.0528 174  ARG B CZ  
10184 N NH1 . ARG B 176  ? 0.3091 0.3536 0.2083 0.0848  0.0444  -0.0541 174  ARG B NH1 
10185 N NH2 . ARG B 176  ? 0.3500 0.4103 0.2503 0.0797  0.0485  -0.0496 174  ARG B NH2 
10186 N N   . CYS B 177  ? 0.3347 0.3582 0.1971 0.0834  0.0421  -0.0603 175  CYS B N   
10187 C CA  . CYS B 177  ? 0.3359 0.3668 0.1953 0.0815  0.0448  -0.0583 175  CYS B CA  
10188 C C   . CYS B 177  ? 0.3794 0.4035 0.2305 0.0789  0.0426  -0.0590 175  CYS B C   
10189 O O   . CYS B 177  ? 0.4048 0.4333 0.2517 0.0780  0.0446  -0.0579 175  CYS B O   
10190 C CB  . CYS B 177  ? 0.3319 0.3741 0.1980 0.0782  0.0471  -0.0544 175  CYS B CB  
10191 S SG  . CYS B 177  ? 0.4251 0.4770 0.3016 0.0805  0.0497  -0.0530 175  CYS B SG  
10192 N N   . GLY B 178  ? 0.3683 0.3819 0.2171 0.0777  0.0384  -0.0607 176  GLY B N   
10193 C CA  . GLY B 178  ? 0.3813 0.3875 0.2220 0.0757  0.0358  -0.0617 176  GLY B CA  
10194 C C   . GLY B 178  ? 0.3822 0.3924 0.2235 0.0700  0.0357  -0.0579 176  GLY B C   
10195 O O   . GLY B 178  ? 0.3652 0.3818 0.2142 0.0664  0.0363  -0.0543 176  GLY B O   
10196 N N   . GLU B 179  ? 0.4022 0.4082 0.2348 0.0694  0.0346  -0.0589 177  GLU B N   
10197 C CA  . GLU B 179  ? 0.4149 0.4235 0.2466 0.0643  0.0342  -0.0555 177  GLU B CA  
10198 C C   . GLU B 179  ? 0.3307 0.3517 0.1659 0.0629  0.0386  -0.0519 177  GLU B C   
10199 O O   . GLU B 179  ? 0.3506 0.3745 0.1904 0.0577  0.0378  -0.0482 177  GLU B O   
10200 C CB  . GLU B 179  ? 0.4589 0.4609 0.2797 0.0645  0.0325  -0.0574 177  GLU B CB  
10201 C CG  . GLU B 179  ? 0.4967 0.5003 0.3160 0.0593  0.0316  -0.0539 177  GLU B CG  
10202 C CD  . GLU B 179  ? 0.6373 0.6332 0.4462 0.0591  0.0291  -0.0557 177  GLU B CD  
10203 O OE1 . GLU B 179  ? 0.7006 0.6898 0.5033 0.0630  0.0280  -0.0598 177  GLU B OE1 
10204 O OE2 . GLU B 179  ? 0.7158 0.7122 0.5226 0.0551  0.0280  -0.0530 177  GLU B OE2 
10205 N N   . PRO B 180  ? 0.3483 0.3773 0.1819 0.0670  0.0431  -0.0526 178  PRO B N   
10206 C CA  . PRO B 180  ? 0.3637 0.4051 0.2009 0.0650  0.0472  -0.0489 178  PRO B CA  
10207 C C   . PRO B 180  ? 0.3803 0.4269 0.2285 0.0612  0.0469  -0.0455 178  PRO B C   
10208 O O   . PRO B 180  ? 0.3767 0.4295 0.2275 0.0568  0.0480  -0.0416 178  PRO B O   
10209 C CB  . PRO B 180  ? 0.4203 0.4676 0.2576 0.0695  0.0510  -0.0502 178  PRO B CB  
10210 C CG  . PRO B 180  ? 0.4252 0.4623 0.2551 0.0726  0.0489  -0.0541 178  PRO B CG  
10211 C CD  . PRO B 180  ? 0.3877 0.4141 0.2174 0.0722  0.0442  -0.0561 178  PRO B CD  
10212 N N   . VAL B 181  ? 0.3243 0.3681 0.1788 0.0627  0.0454  -0.0467 179  VAL B N   
10213 C CA  . VAL B 181  ? 0.3276 0.3763 0.1921 0.0591  0.0452  -0.0435 179  VAL B CA  
10214 C C   . VAL B 181  ? 0.3214 0.3640 0.1877 0.0533  0.0412  -0.0413 179  VAL B C   
10215 O O   . VAL B 181  ? 0.3343 0.3818 0.2064 0.0490  0.0415  -0.0377 179  VAL B O   
10216 C CB  . VAL B 181  ? 0.3326 0.3815 0.2036 0.0625  0.0452  -0.0451 179  VAL B CB  
10217 C CG1 . VAL B 181  ? 0.3397 0.3763 0.2100 0.0630  0.0408  -0.0478 179  VAL B CG1 
10218 C CG2 . VAL B 181  ? 0.3501 0.4066 0.2309 0.0591  0.0460  -0.0416 179  VAL B CG2 
10219 N N   . ILE B 182  ? 0.3243 0.3561 0.1858 0.0533  0.0375  -0.0435 180  ILE B N   
10220 C CA  . ILE B 182  ? 0.3363 0.3621 0.1989 0.0483  0.0336  -0.0417 180  ILE B CA  
10221 C C   . ILE B 182  ? 0.3678 0.3976 0.2271 0.0445  0.0346  -0.0385 180  ILE B C   
10222 O O   . ILE B 182  ? 0.3633 0.3945 0.2271 0.0398  0.0335  -0.0352 180  ILE B O   
10223 C CB  . ILE B 182  ? 0.3504 0.3645 0.2080 0.0493  0.0294  -0.0449 180  ILE B CB  
10224 C CG1 . ILE B 182  ? 0.3344 0.3442 0.1957 0.0525  0.0283  -0.0477 180  ILE B CG1 
10225 C CG2 . ILE B 182  ? 0.3486 0.3574 0.2074 0.0443  0.0255  -0.0429 180  ILE B CG2 
10226 C CD1 . ILE B 182  ? 0.3781 0.3770 0.2331 0.0545  0.0249  -0.0514 180  ILE B CD1 
10227 N N   . ARG B 183  ? 0.3813 0.4127 0.2324 0.0465  0.0367  -0.0395 181  ARG B N   
10228 C CA  A ARG B 183  ? 0.4196 0.4549 0.2667 0.0431  0.0379  -0.0364 181  ARG B CA  
10229 C CA  B ARG B 183  ? 0.4196 0.4549 0.2666 0.0431  0.0379  -0.0364 181  ARG B CA  
10230 C C   . ARG B 183  ? 0.4050 0.4508 0.2587 0.0403  0.0410  -0.0325 181  ARG B C   
10231 O O   . ARG B 183  ? 0.4188 0.4656 0.2742 0.0353  0.0401  -0.0290 181  ARG B O   
10232 C CB  A ARG B 183  ? 0.4190 0.4551 0.2561 0.0464  0.0402  -0.0384 181  ARG B CB  
10233 C CB  B ARG B 183  ? 0.4184 0.4546 0.2556 0.0464  0.0403  -0.0384 181  ARG B CB  
10234 C CG  A ARG B 183  ? 0.4766 0.5209 0.3104 0.0442  0.0436  -0.0352 181  ARG B CG  
10235 C CG  B ARG B 183  ? 0.4769 0.5212 0.3108 0.0441  0.0436  -0.0351 181  ARG B CG  
10236 C CD  A ARG B 183  ? 0.5285 0.5685 0.3586 0.0392  0.0410  -0.0324 181  ARG B CD  
10237 C CD  B ARG B 183  ? 0.5345 0.5734 0.3623 0.0402  0.0410  -0.0333 181  ARG B CD  
10238 N NE  A ARG B 183  ? 0.4998 0.5283 0.3269 0.0388  0.0359  -0.0345 181  ARG B NE  
10239 N NE  B ARG B 183  ? 0.4737 0.5096 0.3073 0.0351  0.0377  -0.0304 181  ARG B NE  
10240 C CZ  A ARG B 183  ? 0.5053 0.5287 0.3364 0.0348  0.0321  -0.0327 181  ARG B CZ  
10241 C CZ  B ARG B 183  ? 0.4995 0.5259 0.3321 0.0334  0.0330  -0.0311 181  ARG B CZ  
10242 N NH1 A ARG B 183  ? 0.4764 0.5046 0.3143 0.0308  0.0326  -0.0288 181  ARG B NH1 
10243 N NH1 B ARG B 183  ? 0.5043 0.5228 0.3304 0.0361  0.0306  -0.0345 181  ARG B NH1 
10244 N NH2 A ARG B 183  ? 0.5202 0.5338 0.3486 0.0349  0.0277  -0.0347 181  ARG B NH2 
10245 N NH2 B ARG B 183  ? 0.5070 0.5317 0.3451 0.0290  0.0305  -0.0282 181  ARG B NH2 
10246 N N   . ARG B 184  ? 0.3935 0.4473 0.2513 0.0434  0.0445  -0.0331 182  ARG B N   
10247 C CA  . ARG B 184  ? 0.3871 0.4515 0.2517 0.0407  0.0474  -0.0294 182  ARG B CA  
10248 C C   . ARG B 184  ? 0.4024 0.4646 0.2752 0.0365  0.0446  -0.0272 182  ARG B C   
10249 O O   . ARG B 184  ? 0.3993 0.4661 0.2753 0.0319  0.0451  -0.0235 182  ARG B O   
10250 C CB  . ARG B 184  ? 0.4380 0.5111 0.3059 0.0453  0.0513  -0.0308 182  ARG B CB  
10251 C CG  . ARG B 184  ? 0.4805 0.5596 0.3414 0.0487  0.0554  -0.0317 182  ARG B CG  
10252 C CD  . ARG B 184  ? 0.5243 0.6149 0.3869 0.0452  0.0589  -0.0275 182  ARG B CD  
10253 N NE  . ARG B 184  ? 0.4707 0.5722 0.3413 0.0464  0.0620  -0.0264 182  ARG B NE  
10254 C CZ  . ARG B 184  ? 0.4645 0.5719 0.3429 0.0419  0.0622  -0.0229 182  ARG B CZ  
10255 N NH1 . ARG B 184  ? 0.5179 0.6212 0.3972 0.0360  0.0595  -0.0199 182  ARG B NH1 
10256 N NH2 . ARG B 184  ? 0.4674 0.5849 0.3528 0.0435  0.0650  -0.0222 182  ARG B NH2 
10257 N N   . GLY B 185  ? 0.3832 0.4384 0.2593 0.0381  0.0416  -0.0295 183  GLY B N   
10258 C CA  . GLY B 185  ? 0.3539 0.4067 0.2373 0.0344  0.0389  -0.0277 183  GLY B CA  
10259 C C   . GLY B 185  ? 0.3763 0.4237 0.2575 0.0295  0.0359  -0.0254 183  GLY B C   
10260 O O   . GLY B 185  ? 0.3505 0.4000 0.2365 0.0253  0.0354  -0.0223 183  GLY B O   
10261 N N   . VAL B 186  ? 0.3374 0.3775 0.2111 0.0302  0.0339  -0.0271 184  VAL B N   
10262 C CA  . VAL B 186  ? 0.3854 0.4200 0.2563 0.0260  0.0308  -0.0250 184  VAL B CA  
10263 C C   . VAL B 186  ? 0.3785 0.4196 0.2480 0.0224  0.0331  -0.0211 184  VAL B C   
10264 O O   . VAL B 186  ? 0.3721 0.4126 0.2446 0.0180  0.0316  -0.0181 184  VAL B O   
10265 C CB  . VAL B 186  ? 0.3664 0.3927 0.2291 0.0278  0.0284  -0.0277 184  VAL B CB  
10266 C CG1 . VAL B 186  ? 0.3990 0.4213 0.2575 0.0237  0.0259  -0.0252 184  VAL B CG1 
10267 C CG2 . VAL B 186  ? 0.3725 0.3911 0.2375 0.0299  0.0251  -0.0308 184  VAL B CG2 
10268 N N   . ASP B 187  ? 0.3723 0.4198 0.2371 0.0242  0.0369  -0.0212 185  ASP B N   
10269 C CA  . ASP B 187  ? 0.4039 0.4583 0.2673 0.0207  0.0394  -0.0173 185  ASP B CA  
10270 C C   . ASP B 187  ? 0.4196 0.4807 0.2917 0.0176  0.0406  -0.0144 185  ASP B C   
10271 O O   . ASP B 187  ? 0.4041 0.4666 0.2769 0.0128  0.0403  -0.0107 185  ASP B O   
10272 C CB  . ASP B 187  ? 0.4101 0.4713 0.2676 0.0237  0.0436  -0.0182 185  ASP B CB  
10273 C CG  . ASP B 187  ? 0.4757 0.5300 0.3233 0.0261  0.0424  -0.0207 185  ASP B CG  
10274 O OD1 . ASP B 187  ? 0.5127 0.5579 0.3577 0.0244  0.0383  -0.0209 185  ASP B OD1 
10275 O OD2 . ASP B 187  ? 0.4821 0.5403 0.3245 0.0298  0.0455  -0.0226 185  ASP B OD2 
10276 N N   . MET B 188  ? 0.4076 0.4727 0.2862 0.0202  0.0418  -0.0159 186  MET B N   
10277 C CA  . MET B 188  ? 0.4022 0.4738 0.2892 0.0175  0.0429  -0.0133 186  MET B CA  
10278 C C   . MET B 188  ? 0.3821 0.4472 0.2732 0.0135  0.0390  -0.0117 186  MET B C   
10279 O O   . MET B 188  ? 0.4097 0.4777 0.3036 0.0090  0.0391  -0.0082 186  MET B O   
10280 C CB  . MET B 188  ? 0.4182 0.4945 0.3109 0.0217  0.0446  -0.0156 186  MET B CB  
10281 C CG  . MET B 188  ? 0.4566 0.5400 0.3580 0.0193  0.0457  -0.0132 186  MET B CG  
10282 S SD  . MET B 188  ? 0.6680 0.7635 0.5695 0.0157  0.0497  -0.0091 186  MET B SD  
10283 C CE  . MET B 188  ? 0.5487 0.6503 0.4441 0.0213  0.0538  -0.0115 186  MET B CE  
10284 N N   . ALA B 189  ? 0.3924 0.4486 0.2837 0.0151  0.0355  -0.0142 187  ALA B N   
10285 C CA  . ALA B 189  ? 0.3851 0.4351 0.2803 0.0118  0.0319  -0.0129 187  ALA B CA  
10286 C C   . ALA B 189  ? 0.4042 0.4506 0.2947 0.0077  0.0302  -0.0102 187  ALA B C   
10287 O O   . ALA B 189  ? 0.3834 0.4287 0.2772 0.0037  0.0287  -0.0075 187  ALA B O   
10288 C CB  . ALA B 189  ? 0.4005 0.4422 0.2965 0.0145  0.0287  -0.0162 187  ALA B CB  
10289 N N   . MET B 190  ? 0.3745 0.4187 0.2569 0.0087  0.0304  -0.0108 188  MET B N   
10290 C CA  . MET B 190  ? 0.4096 0.4504 0.2868 0.0050  0.0289  -0.0081 188  MET B CA  
10291 C C   . MET B 190  ? 0.4379 0.4856 0.3167 0.0008  0.0312  -0.0040 188  MET B C   
10292 O O   . MET B 190  ? 0.4194 0.4640 0.2989 -0.0034 0.0292  -0.0012 188  MET B O   
10293 C CB  . MET B 190  ? 0.4425 0.4810 0.3103 0.0071  0.0293  -0.0096 188  MET B CB  
10294 C CG  . MET B 190  ? 0.5072 0.5400 0.3691 0.0039  0.0268  -0.0074 188  MET B CG  
10295 S SD  . MET B 190  ? 0.5688 0.6001 0.4191 0.0063  0.0277  -0.0089 188  MET B SD  
10296 C CE  . MET B 190  ? 0.5010 0.5273 0.3511 0.0119  0.0262  -0.0144 188  MET B CE  
10297 N N   . ARG B 191  ? 0.3869 0.4441 0.2664 0.0018  0.0355  -0.0036 189  ARG B N   
10298 C CA  . ARG B 191  ? 0.4112 0.4758 0.2926 -0.0024 0.0378  0.0004  189  ARG B CA  
10299 C C   . ARG B 191  ? 0.4283 0.4935 0.3181 -0.0053 0.0365  0.0020  189  ARG B C   
10300 O O   . ARG B 191  ? 0.4219 0.4867 0.3124 -0.0100 0.0357  0.0054  189  ARG B O   
10301 C CB  . ARG B 191  ? 0.4024 0.4779 0.2834 -0.0004 0.0427  0.0003  189  ARG B CB  
10302 N N   . MET B 192  ? 0.3780 0.4439 0.2739 -0.0023 0.0363  -0.0005 190  MET B N   
10303 C CA  . MET B 192  ? 0.3780 0.4448 0.2818 -0.0047 0.0352  0.0007  190  MET B CA  
10304 C C   . MET B 192  ? 0.4089 0.4663 0.3126 -0.0077 0.0310  0.0018  190  MET B C   
10305 O O   . MET B 192  ? 0.3838 0.4414 0.2901 -0.0120 0.0302  0.0047  190  MET B O   
10306 C CB  . MET B 192  ? 0.3986 0.4671 0.3081 -0.0006 0.0356  -0.0023 190  MET B CB  
10307 C CG  . MET B 192  ? 0.4656 0.5437 0.3760 0.0027  0.0397  -0.0034 190  MET B CG  
10308 S SD  . MET B 192  ? 0.5770 0.6572 0.4951 0.0068  0.0398  -0.0062 190  MET B SD  
10309 C CE  . MET B 192  ? 0.4494 0.5340 0.3753 0.0018  0.0394  -0.0029 190  MET B CE  
10310 N N   . MET B 193  ? 0.3867 0.4357 0.2876 -0.0054 0.0282  -0.0006 191  MET B N   
10311 C CA  A MET B 193  ? 0.4060 0.4463 0.3072 -0.0075 0.0241  0.0001  191  MET B CA  
10312 C CA  B MET B 193  ? 0.4056 0.4461 0.3070 -0.0076 0.0242  0.0002  191  MET B CA  
10313 C C   . MET B 193  ? 0.4204 0.4572 0.3156 -0.0110 0.0229  0.0029  191  MET B C   
10314 O O   . MET B 193  ? 0.4127 0.4436 0.3086 -0.0137 0.0200  0.0045  191  MET B O   
10315 C CB  A MET B 193  ? 0.4390 0.4721 0.3396 -0.0040 0.0214  -0.0034 191  MET B CB  
10316 C CB  B MET B 193  ? 0.4394 0.4728 0.3409 -0.0042 0.0214  -0.0033 191  MET B CB  
10317 C CG  A MET B 193  ? 0.3985 0.4338 0.3043 -0.0003 0.0223  -0.0064 191  MET B CG  
10318 C CG  B MET B 193  ? 0.4147 0.4499 0.3233 -0.0017 0.0217  -0.0055 191  MET B CG  
10319 S SD  A MET B 193  ? 0.3949 0.4217 0.2991 0.0035  0.0192  -0.0104 191  MET B SD  
10320 S SD  B MET B 193  ? 0.4265 0.4526 0.3361 0.0010  0.0179  -0.0087 191  MET B SD  
10321 C CE  A MET B 193  ? 0.4907 0.5123 0.4017 0.0016  0.0157  -0.0098 191  MET B CE  
10322 C CE  B MET B 193  ? 0.4206 0.4450 0.3225 0.0047  0.0185  -0.0115 191  MET B CE  
10323 N N   . GLY B 194  ? 0.4081 0.4482 0.2970 -0.0109 0.0252  0.0037  192  GLY B N   
10324 C CA  . GLY B 194  ? 0.4367 0.4731 0.3191 -0.0141 0.0240  0.0065  192  GLY B CA  
10325 C C   . GLY B 194  ? 0.3817 0.4240 0.2640 -0.0186 0.0263  0.0105  192  GLY B C   
10326 O O   . GLY B 194  ? 0.4145 0.4526 0.2930 -0.0222 0.0247  0.0135  192  GLY B O   
10327 N N   . GLU B 195  ? 0.3830 0.4349 0.2693 -0.0184 0.0299  0.0108  193  GLU B N   
10328 C CA  . GLU B 195  ? 0.4222 0.4811 0.3080 -0.0226 0.0326  0.0146  193  GLU B CA  
10329 C C   . GLU B 195  ? 0.4002 0.4658 0.2942 -0.0245 0.0340  0.0158  193  GLU B C   
10330 O O   . GLU B 195  ? 0.3670 0.4362 0.2614 -0.0292 0.0349  0.0194  193  GLU B O   
10331 C CB  . GLU B 195  ? 0.4373 0.5037 0.3181 -0.0210 0.0365  0.0146  193  GLU B CB  
10332 C CG  . GLU B 195  ? 0.5445 0.6050 0.4163 -0.0192 0.0355  0.0136  193  GLU B CG  
10333 C CD  . GLU B 195  ? 0.5880 0.6558 0.4552 -0.0165 0.0396  0.0127  193  GLU B CD  
10334 O OE1 . GLU B 195  ? 0.6527 0.7303 0.5215 -0.0182 0.0433  0.0148  193  GLU B OE1 
10335 O OE2 . GLU B 195  ? 0.6687 0.7326 0.5307 -0.0126 0.0390  0.0097  193  GLU B OE2 
10336 N N   . GLN B 196  ? 0.3838 0.4512 0.2841 -0.0213 0.0340  0.0130  194  GLN B N   
10337 C CA  . GLN B 196  ? 0.3801 0.4541 0.2881 -0.0230 0.0353  0.0140  194  GLN B CA  
10338 C C   . GLN B 196  ? 0.3994 0.4667 0.3121 -0.0244 0.0317  0.0138  194  GLN B C   
10339 O O   . GLN B 196  ? 0.4441 0.5124 0.3597 -0.0287 0.0312  0.0165  194  GLN B O   
10340 C CB  . GLN B 196  ? 0.4029 0.4850 0.3148 -0.0184 0.0382  0.0113  194  GLN B CB  
10341 N N   . PHE B 197  ? 0.3742 0.4346 0.2877 -0.0209 0.0293  0.0107  195  PHE B N   
10342 C CA  . PHE B 197  ? 0.3896 0.4437 0.3076 -0.0220 0.0260  0.0105  195  PHE B CA  
10343 C C   . PHE B 197  ? 0.4090 0.4554 0.3233 -0.0259 0.0232  0.0129  195  PHE B C   
10344 O O   . PHE B 197  ? 0.4042 0.4469 0.3219 -0.0282 0.0210  0.0139  195  PHE B O   
10345 C CB  . PHE B 197  ? 0.4222 0.4711 0.3417 -0.0174 0.0242  0.0067  195  PHE B CB  
10346 C CG  . PHE B 197  ? 0.4002 0.4554 0.3235 -0.0134 0.0266  0.0041  195  PHE B CG  
10347 C CD1 . PHE B 197  ? 0.4414 0.5058 0.3693 -0.0142 0.0293  0.0051  195  PHE B CD1 
10348 C CD2 . PHE B 197  ? 0.4274 0.4790 0.3496 -0.0088 0.0259  0.0006  195  PHE B CD2 
10349 C CE1 . PHE B 197  ? 0.4775 0.5475 0.4088 -0.0102 0.0314  0.0028  195  PHE B CE1 
10350 C CE2 . PHE B 197  ? 0.4664 0.5230 0.3918 -0.0050 0.0279  -0.0018 195  PHE B CE2 
10351 C CZ  . PHE B 197  ? 0.4189 0.4848 0.3489 -0.0055 0.0307  -0.0007 195  PHE B CZ  
10352 N N   . VAL B 198  ? 0.3881 0.4316 0.2952 -0.0263 0.0230  0.0139  196  VAL B N   
10353 C CA  . VAL B 198  ? 0.3672 0.4037 0.2700 -0.0300 0.0204  0.0166  196  VAL B CA  
10354 C C   . VAL B 198  ? 0.3579 0.3984 0.2548 -0.0326 0.0227  0.0194  196  VAL B C   
10355 O O   . VAL B 198  ? 0.3871 0.4336 0.2816 -0.0304 0.0256  0.0185  196  VAL B O   
10356 C CB  . VAL B 198  ? 0.3381 0.3647 0.2375 -0.0278 0.0168  0.0149  196  VAL B CB  
10357 C CG1 . VAL B 198  ? 0.3919 0.4147 0.2972 -0.0256 0.0146  0.0124  196  VAL B CG1 
10358 C CG2 . VAL B 198  ? 0.4075 0.4348 0.3017 -0.0243 0.0179  0.0128  196  VAL B CG2 
10359 N N   . THR B 199  ? 0.3835 0.4205 0.2777 -0.0373 0.0214  0.0230  197  THR B N   
10360 C CA  A THR B 199  ? 0.3771 0.4164 0.2648 -0.0400 0.0231  0.0260  197  THR B CA  
10361 C CA  B THR B 199  ? 0.3769 0.4163 0.2646 -0.0400 0.0231  0.0259  197  THR B CA  
10362 C C   . THR B 199  ? 0.3829 0.4160 0.2630 -0.0379 0.0215  0.0251  197  THR B C   
10363 O O   . THR B 199  ? 0.4176 0.4538 0.2918 -0.0385 0.0236  0.0265  197  THR B O   
10364 C CB  A THR B 199  ? 0.3739 0.4109 0.2610 -0.0459 0.0219  0.0301  197  THR B CB  
10365 C CB  B THR B 199  ? 0.3737 0.4110 0.2606 -0.0459 0.0221  0.0302  197  THR B CB  
10366 O OG1 A THR B 199  ? 0.3557 0.3973 0.2503 -0.0476 0.0226  0.0304  197  THR B OG1 
10367 O OG1 B THR B 199  ? 0.3992 0.4383 0.2793 -0.0488 0.0237  0.0333  197  THR B OG1 
10368 C CG2 A THR B 199  ? 0.3948 0.4367 0.2764 -0.0494 0.0245  0.0336  197  THR B CG2 
10369 C CG2 B THR B 199  ? 0.3382 0.3641 0.2244 -0.0466 0.0176  0.0303  197  THR B CG2 
10370 N N   . GLY B 200  ? 0.3426 0.3672 0.2228 -0.0355 0.0180  0.0230  198  GLY B N   
10371 C CA  . GLY B 200  ? 0.3737 0.3923 0.2473 -0.0333 0.0161  0.0219  198  GLY B CA  
10372 C C   . GLY B 200  ? 0.3788 0.3897 0.2551 -0.0306 0.0123  0.0192  198  GLY B C   
10373 O O   . GLY B 200  ? 0.3563 0.3654 0.2386 -0.0312 0.0109  0.0190  198  GLY B O   
10374 N N   . GLU B 201  ? 0.3962 0.4029 0.2679 -0.0276 0.0108  0.0172  199  GLU B N   
10375 C CA  . GLU B 201  ? 0.4255 0.4251 0.2995 -0.0251 0.0070  0.0148  199  GLU B CA  
10376 C C   . GLU B 201  ? 0.4143 0.4058 0.2863 -0.0274 0.0033  0.0171  199  GLU B C   
10377 O O   . GLU B 201  ? 0.5015 0.4880 0.3774 -0.0263 0.0004  0.0159  199  GLU B O   
10378 C CB  . GLU B 201  ? 0.5043 0.5022 0.3742 -0.0212 0.0064  0.0118  199  GLU B CB  
10379 C CG  . GLU B 201  ? 0.5989 0.6031 0.4713 -0.0179 0.0094  0.0087  199  GLU B CG  
10380 C CD  . GLU B 201  ? 0.7256 0.7266 0.5943 -0.0141 0.0081  0.0054  199  GLU B CD  
10381 O OE1 . GLU B 201  ? 0.6272 0.6220 0.4906 -0.0143 0.0052  0.0058  199  GLU B OE1 
10382 O OE2 . GLU B 201  ? 0.7614 0.7659 0.6323 -0.0109 0.0098  0.0024  199  GLU B OE2 
10383 N N   . THR B 202  ? 0.3645 0.3543 0.2301 -0.0305 0.0033  0.0204  200  THR B N   
10384 C CA  . THR B 202  ? 0.3815 0.3634 0.2444 -0.0328 -0.0002 0.0230  200  THR B CA  
10385 C C   . THR B 202  ? 0.3936 0.3773 0.2553 -0.0376 0.0012  0.0270  200  THR B C   
10386 O O   . THR B 202  ? 0.3673 0.3584 0.2285 -0.0392 0.0050  0.0281  200  THR B O   
10387 C CB  . THR B 202  ? 0.4258 0.4026 0.2804 -0.0320 -0.0023 0.0235  200  THR B CB  
10388 O OG1 . THR B 202  ? 0.4161 0.3971 0.2645 -0.0339 0.0005  0.0256  200  THR B OG1 
10389 C CG2 . THR B 202  ? 0.4846 0.4606 0.3395 -0.0275 -0.0035 0.0195  200  THR B CG2 
10390 N N   . ILE B 203  ? 0.3365 0.3131 0.1976 -0.0400 -0.0017 0.0293  201  ILE B N   
10391 C CA  . ILE B 203  ? 0.3633 0.3404 0.2231 -0.0450 -0.0008 0.0333  201  ILE B CA  
10392 C C   . ILE B 203  ? 0.4158 0.3946 0.2675 -0.0473 0.0009  0.0361  201  ILE B C   
10393 O O   . ILE B 203  ? 0.3605 0.3449 0.2115 -0.0509 0.0038  0.0387  201  ILE B O   
10394 C CB  . ILE B 203  ? 0.3513 0.3195 0.2118 -0.0468 -0.0045 0.0349  201  ILE B CB  
10395 C CG1 . ILE B 203  ? 0.3615 0.3304 0.2213 -0.0521 -0.0035 0.0387  201  ILE B CG1 
10396 C CG2 . ILE B 203  ? 0.3943 0.3538 0.2484 -0.0457 -0.0082 0.0357  201  ILE B CG2 
10397 C CD1 . ILE B 203  ? 0.3361 0.3132 0.2031 -0.0534 -0.0005 0.0381  201  ILE B CD1 
10398 N N   . ARG B 204  ? 0.3914 0.3660 0.2369 -0.0452 -0.0008 0.0356  202  ARG B N   
10399 C CA  . ARG B 204  ? 0.4386 0.4148 0.2758 -0.0468 0.0008  0.0379  202  ARG B CA  
10400 C C   . ARG B 204  ? 0.3743 0.3614 0.2124 -0.0467 0.0058  0.0373  202  ARG B C   
10401 O O   . ARG B 204  ? 0.4029 0.3944 0.2377 -0.0503 0.0084  0.0405  202  ARG B O   
10402 C CB  . ARG B 204  ? 0.4942 0.4654 0.3261 -0.0432 -0.0018 0.0361  202  ARG B CB  
10403 C CG  . ARG B 204  ? 0.6284 0.5960 0.4506 -0.0452 -0.0025 0.0392  202  ARG B CG  
10404 C CD  . ARG B 204  ? 0.5222 0.4833 0.3401 -0.0417 -0.0062 0.0373  202  ARG B CD  
10405 N NE  . ARG B 204  ? 0.4462 0.4116 0.2643 -0.0376 -0.0048 0.0334  202  ARG B NE  
10406 C CZ  . ARG B 204  ? 0.5197 0.4900 0.3320 -0.0372 -0.0019 0.0333  202  ARG B CZ  
10407 N NH1 . ARG B 204  ? 0.5115 0.4842 0.3182 -0.0407 0.0004  0.0370  202  ARG B NH1 
10408 N NH2 . ARG B 204  ? 0.4798 0.4525 0.2920 -0.0332 -0.0012 0.0293  202  ARG B NH2 
10409 N N   . GLU B 205  ? 0.3806 0.3721 0.2231 -0.0425 0.0071  0.0332  203  GLU B N   
10410 C CA  . GLU B 205  ? 0.3888 0.3905 0.2323 -0.0415 0.0117  0.0321  203  GLU B CA  
10411 C C   . GLU B 205  ? 0.3860 0.3946 0.2354 -0.0448 0.0144  0.0340  203  GLU B C   
10412 O O   . GLU B 205  ? 0.3990 0.4154 0.2469 -0.0468 0.0181  0.0358  203  GLU B O   
10413 C CB  . GLU B 205  ? 0.4101 0.4136 0.2574 -0.0362 0.0119  0.0272  203  GLU B CB  
10414 C CG  . GLU B 205  ? 0.4180 0.4313 0.2658 -0.0342 0.0165  0.0256  203  GLU B CG  
10415 C CD  . GLU B 205  ? 0.5636 0.5772 0.4139 -0.0288 0.0163  0.0207  203  GLU B CD  
10416 O OE1 . GLU B 205  ? 0.5300 0.5419 0.3872 -0.0273 0.0147  0.0186  203  GLU B OE1 
10417 O OE2 . GLU B 205  ? 0.6919 0.7071 0.5369 -0.0261 0.0176  0.0190  203  GLU B OE2 
10418 N N   . ALA B 206  ? 0.3367 0.3427 0.1929 -0.0454 0.0125  0.0335  204  ALA B N   
10419 C CA  . ALA B 206  ? 0.3245 0.3364 0.1865 -0.0486 0.0146  0.0351  204  ALA B CA  
10420 C C   . ALA B 206  ? 0.3557 0.3680 0.2132 -0.0543 0.0154  0.0400  204  ALA B C   
10421 O O   . ALA B 206  ? 0.3518 0.3730 0.2109 -0.0569 0.0189  0.0417  204  ALA B O   
10422 C CB  . ALA B 206  ? 0.3338 0.3406 0.2023 -0.0484 0.0117  0.0340  204  ALA B CB  
10423 N N   . LEU B 207  ? 0.3406 0.3436 0.1926 -0.0563 0.0121  0.0423  205  LEU B N   
10424 C CA  . LEU B 207  ? 0.3623 0.3644 0.2093 -0.0619 0.0125  0.0471  205  LEU B CA  
10425 C C   . LEU B 207  ? 0.4003 0.4098 0.2417 -0.0628 0.0163  0.0487  205  LEU B C   
10426 O O   . LEU B 207  ? 0.4024 0.4178 0.2434 -0.0672 0.0189  0.0521  205  LEU B O   
10427 C CB  . LEU B 207  ? 0.3857 0.3756 0.2272 -0.0631 0.0080  0.0490  205  LEU B CB  
10428 C CG  . LEU B 207  ? 0.4254 0.4079 0.2718 -0.0635 0.0045  0.0485  205  LEU B CG  
10429 C CD1 . LEU B 207  ? 0.4249 0.3955 0.2660 -0.0630 -0.0001 0.0494  205  LEU B CD1 
10430 C CD2 . LEU B 207  ? 0.3800 0.3648 0.2292 -0.0689 0.0055  0.0516  205  LEU B CD2 
10431 N N   . LYS B 208  ? 0.3547 0.3641 0.1918 -0.0587 0.0166  0.0464  206  LYS B N   
10432 C CA  . LYS B 208  ? 0.3867 0.4031 0.2180 -0.0590 0.0203  0.0476  206  LYS B CA  
10433 C C   . LYS B 208  ? 0.3870 0.4162 0.2239 -0.0587 0.0251  0.0468  206  LYS B C   
10434 O O   . LYS B 208  ? 0.4188 0.4554 0.2533 -0.0618 0.0285  0.0497  206  LYS B O   
10435 C CB  . LYS B 208  ? 0.4321 0.4454 0.2577 -0.0542 0.0194  0.0448  206  LYS B CB  
10436 N N   . ARG B 209  ? 0.3929 0.4250 0.2375 -0.0552 0.0253  0.0431  207  ARG B N   
10437 C CA  . ARG B 209  ? 0.3815 0.4256 0.2318 -0.0544 0.0296  0.0421  207  ARG B CA  
10438 C C   . ARG B 209  ? 0.4360 0.4849 0.2915 -0.0596 0.0307  0.0453  207  ARG B C   
10439 O O   . ARG B 209  ? 0.4242 0.4841 0.2837 -0.0600 0.0345  0.0455  207  ARG B O   
10440 C CB  . ARG B 209  ? 0.4013 0.4463 0.2578 -0.0489 0.0293  0.0371  207  ARG B CB  
10441 C CG  . ARG B 209  ? 0.4328 0.4748 0.2846 -0.0437 0.0288  0.0337  207  ARG B CG  
10442 C CD  . ARG B 209  ? 0.4326 0.4752 0.2907 -0.0387 0.0284  0.0290  207  ARG B CD  
10443 N NE  . ARG B 209  ? 0.5480 0.5886 0.4018 -0.0337 0.0283  0.0255  207  ARG B NE  
10444 C CZ  . ARG B 209  ? 0.5556 0.5950 0.4132 -0.0292 0.0275  0.0213  207  ARG B CZ  
10445 N NH1 . ARG B 209  ? 0.4491 0.4891 0.3150 -0.0288 0.0267  0.0201  207  ARG B NH1 
10446 N NH2 . ARG B 209  ? 0.6096 0.6470 0.4625 -0.0250 0.0273  0.0183  207  ARG B NH2 
10447 N N   . SER B 210  ? 0.3654 0.4062 0.2206 -0.0636 0.0274  0.0478  208  SER B N   
10448 C CA  . SER B 210  ? 0.3664 0.4106 0.2263 -0.0688 0.0279  0.0508  208  SER B CA  
10449 C C   . SER B 210  ? 0.4031 0.4523 0.2585 -0.0744 0.0304  0.0556  208  SER B C   
10450 O O   . SER B 210  ? 0.3947 0.4497 0.2542 -0.0788 0.0318  0.0581  208  SER B O   
10451 C CB  . SER B 210  ? 0.3334 0.3664 0.1947 -0.0707 0.0232  0.0513  208  SER B CB  
10452 O OG  . SER B 210  ? 0.4004 0.4303 0.2671 -0.0658 0.0214  0.0469  208  SER B OG  
10453 N N   . LYS B 211  ? 0.3831 0.4303 0.2299 -0.0744 0.0309  0.0570  209  LYS B N   
10454 C CA  . LYS B 211  ? 0.3880 0.4390 0.2297 -0.0800 0.0330  0.0620  209  LYS B CA  
10455 C C   . LYS B 211  ? 0.3790 0.4451 0.2252 -0.0812 0.0381  0.0628  209  LYS B C   
10456 O O   . LYS B 211  ? 0.4278 0.4986 0.2746 -0.0872 0.0395  0.0670  209  LYS B O   
10457 C CB  . LYS B 211  ? 0.4373 0.4841 0.2690 -0.0790 0.0329  0.0630  209  LYS B CB  
10458 C CG  . LYS B 211  ? 0.5125 0.5455 0.3400 -0.0765 0.0279  0.0615  209  LYS B CG  
10459 C CD  . LYS B 211  ? 0.5199 0.5429 0.3481 -0.0806 0.0238  0.0640  209  LYS B CD  
10460 C CE  . LYS B 211  ? 0.6191 0.6290 0.4429 -0.0779 0.0190  0.0627  209  LYS B CE  
10461 N NZ  . LYS B 211  ? 0.5827 0.5823 0.4078 -0.0807 0.0147  0.0643  209  LYS B NZ  
10462 N N   . GLU B 212  ? 0.4069 0.4808 0.2566 -0.0757 0.0408  0.0589  210  GLU B N   
10463 C CA  . GLU B 212  ? 0.4538 0.5426 0.3070 -0.0760 0.0459  0.0595  210  GLU B CA  
10464 C C   . GLU B 212  ? 0.4096 0.5042 0.2711 -0.0805 0.0464  0.0614  210  GLU B C   
10465 O O   . GLU B 212  ? 0.4041 0.5063 0.2671 -0.0846 0.0487  0.0647  210  GLU B O   
10466 C CB  . GLU B 212  ? 0.4885 0.5829 0.3445 -0.0687 0.0481  0.0544  210  GLU B CB  
10467 C CG  . GLU B 212  ? 0.6101 0.7202 0.4704 -0.0681 0.0534  0.0545  210  GLU B CG  
10468 C CD  . GLU B 212  ? 0.7174 0.8320 0.5820 -0.0608 0.0549  0.0493  210  GLU B CD  
10469 O OE1 . GLU B 212  ? 0.8328 0.9394 0.6940 -0.0560 0.0528  0.0458  210  GLU B OE1 
10470 O OE2 . GLU B 212  ? 0.8027 0.9287 0.6742 -0.0600 0.0580  0.0487  210  GLU B OE2 
10471 N N   . LEU B 213  ? 0.3754 0.4656 0.2433 -0.0789 0.0436  0.0589  211  LEU B N   
10472 C CA  . LEU B 213  ? 0.3697 0.4651 0.2453 -0.0829 0.0437  0.0604  211  LEU B CA  
10473 C C   . LEU B 213  ? 0.3910 0.4787 0.2643 -0.0900 0.0408  0.0647  211  LEU B C   
10474 O O   . LEU B 213  ? 0.3687 0.4626 0.2460 -0.0952 0.0418  0.0676  211  LEU B O   
10475 C CB  . LEU B 213  ? 0.3270 0.4217 0.2106 -0.0785 0.0423  0.0561  211  LEU B CB  
10476 C CG  . LEU B 213  ? 0.3945 0.4988 0.2816 -0.0722 0.0457  0.0522  211  LEU B CG  
10477 C CD1 . LEU B 213  ? 0.3972 0.5012 0.2923 -0.0686 0.0443  0.0485  211  LEU B CD1 
10478 C CD2 . LEU B 213  ? 0.4155 0.5349 0.3045 -0.0741 0.0506  0.0545  211  LEU B CD2 
10479 N N   . GLU B 214  ? 0.3578 0.4322 0.2246 -0.0903 0.0371  0.0652  212  GLU B N   
10480 C CA  . GLU B 214  ? 0.3424 0.4090 0.2058 -0.0970 0.0344  0.0696  212  GLU B CA  
10481 C C   . GLU B 214  ? 0.3849 0.4586 0.2457 -0.1020 0.0372  0.0739  212  GLU B C   
10482 O O   . GLU B 214  ? 0.3900 0.4637 0.2537 -0.1072 0.0363  0.0767  212  GLU B O   
10483 C CB  . GLU B 214  ? 0.3841 0.4355 0.2406 -0.0958 0.0301  0.0694  212  GLU B CB  
10484 C CG  . GLU B 214  ? 0.3573 0.4003 0.2181 -0.0919 0.0264  0.0655  212  GLU B CG  
10485 C CD  . GLU B 214  ? 0.3988 0.4270 0.2534 -0.0913 0.0219  0.0657  212  GLU B CD  
10486 O OE1 . GLU B 214  ? 0.4465 0.4713 0.2931 -0.0918 0.0218  0.0677  212  GLU B OE1 
10487 O OE2 . GLU B 214  ? 0.4001 0.4204 0.2578 -0.0900 0.0184  0.0639  212  GLU B OE2 
10488 N N   . GLU B 215  ? 0.3897 0.4686 0.2467 -0.0990 0.0402  0.0735  213  GLU B N   
10489 C CA  . GLU B 215  ? 0.3962 0.4816 0.2528 -0.1019 0.0427  0.0764  213  GLU B CA  
10490 C C   . GLU B 215  ? 0.4104 0.5086 0.2764 -0.1037 0.0453  0.0767  213  GLU B C   
10491 O O   . GLU B 215  ? 0.4099 0.5120 0.2770 -0.1081 0.0462  0.0798  213  GLU B O   
10492 C CB  . GLU B 215  ? 0.4242 0.5133 0.2752 -0.0978 0.0455  0.0754  213  GLU B CB  
10493 C CG  . GLU B 215  ? 0.4615 0.5383 0.3024 -0.0970 0.0428  0.0760  213  GLU B CG  
10494 C CD  . GLU B 215  ? 0.5937 0.6742 0.4288 -0.0931 0.0457  0.0750  213  GLU B CD  
10495 O OE1 . GLU B 215  ? 0.7220 0.8118 0.5584 -0.0939 0.0492  0.0763  213  GLU B OE1 
10496 O OE2 . GLU B 215  ? 0.6954 0.7693 0.5244 -0.0891 0.0442  0.0728  213  GLU B OE2 
10497 N N   . LYS B 216  ? 0.3742 0.4790 0.2469 -0.1003 0.0465  0.0735  214  LYS B N   
10498 C CA  . LYS B 216  ? 0.3909 0.5075 0.2729 -0.1016 0.0487  0.0736  214  LYS B CA  
10499 C C   . LYS B 216  ? 0.4380 0.5506 0.3246 -0.1069 0.0455  0.0752  214  LYS B C   
10500 O O   . LYS B 216  ? 0.4132 0.5348 0.3070 -0.1092 0.0466  0.0760  214  LYS B O   
10501 C CB  . LYS B 216  ? 0.3958 0.5217 0.2832 -0.0954 0.0514  0.0694  214  LYS B CB  
10502 N N   . GLY B 217  ? 0.3656 0.4649 0.2480 -0.1087 0.0414  0.0757  215  GLY B N   
10503 C CA  . GLY B 217  ? 0.3468 0.4406 0.2326 -0.1134 0.0381  0.0770  215  GLY B CA  
10504 C C   . GLY B 217  ? 0.3878 0.4767 0.2761 -0.1111 0.0360  0.0742  215  GLY B C   
10505 O O   . GLY B 217  ? 0.3816 0.4662 0.2731 -0.1146 0.0333  0.0750  215  GLY B O   
10506 N N   . PHE B 218  ? 0.3450 0.4345 0.2323 -0.1051 0.0371  0.0708  216  PHE B N   
10507 C CA  . PHE B 218  ? 0.3329 0.4145 0.2240 -0.1008 0.0339  0.0668  216  PHE B CA  
10508 C C   . PHE B 218  ? 0.3373 0.4026 0.2220 -0.1012 0.0293  0.0671  216  PHE B C   
10509 O O   . PHE B 218  ? 0.3366 0.3968 0.2136 -0.1030 0.0289  0.0696  216  PHE B O   
10510 C CB  . PHE B 218  ? 0.3331 0.4188 0.2266 -0.0928 0.0356  0.0619  216  PHE B CB  
10511 C CG  . PHE B 218  ? 0.3519 0.4526 0.2525 -0.0910 0.0396  0.0607  216  PHE B CG  
10512 C CD1 . PHE B 218  ? 0.3525 0.4650 0.2518 -0.0917 0.0440  0.0625  216  PHE B CD1 
10513 C CD2 . PHE B 218  ? 0.3545 0.4576 0.2630 -0.0884 0.0389  0.0577  216  PHE B CD2 
10514 C CE1 . PHE B 218  ? 0.3768 0.5033 0.2828 -0.0895 0.0476  0.0613  216  PHE B CE1 
10515 C CE2 . PHE B 218  ? 0.3745 0.4913 0.2895 -0.0864 0.0423  0.0566  216  PHE B CE2 
10516 C CZ  . PHE B 218  ? 0.3722 0.5008 0.2862 -0.0869 0.0467  0.0583  216  PHE B CZ  
10517 N N   . SER B 219  ? 0.3127 0.3700 0.2008 -0.0993 0.0259  0.0645  217  SER B N   
10518 C CA  . SER B 219  ? 0.3489 0.3913 0.2322 -0.0977 0.0217  0.0637  217  SER B CA  
10519 C C   . SER B 219  ? 0.3024 0.3426 0.1897 -0.0907 0.0206  0.0585  217  SER B C   
10520 O O   . SER B 219  ? 0.2910 0.3404 0.1842 -0.0873 0.0231  0.0559  217  SER B O   
10521 C CB  . SER B 219  ? 0.3260 0.3592 0.2088 -0.1030 0.0181  0.0661  217  SER B CB  
10522 O OG  . SER B 219  ? 0.3547 0.3915 0.2453 -0.1034 0.0177  0.0645  217  SER B OG  
10523 N N   . TYR B 220  ? 0.3162 0.3439 0.2003 -0.0884 0.0169  0.0572  218  TYR B N   
10524 C CA  . TYR B 220  ? 0.2919 0.3170 0.1789 -0.0818 0.0158  0.0525  218  TYR B CA  
10525 C C   . TYR B 220  ? 0.2872 0.3008 0.1752 -0.0813 0.0115  0.0514  218  TYR B C   
10526 O O   . TYR B 220  ? 0.3113 0.3160 0.1950 -0.0849 0.0087  0.0540  218  TYR B O   
10527 C CB  . TYR B 220  ? 0.2775 0.3002 0.1587 -0.0777 0.0160  0.0513  218  TYR B CB  
10528 C CG  . TYR B 220  ? 0.2832 0.3176 0.1652 -0.0753 0.0204  0.0503  218  TYR B CG  
10529 C CD1 . TYR B 220  ? 0.2968 0.3381 0.1750 -0.0789 0.0234  0.0536  218  TYR B CD1 
10530 C CD2 . TYR B 220  ? 0.2853 0.3241 0.1718 -0.0696 0.0217  0.0460  218  TYR B CD2 
10531 C CE1 . TYR B 220  ? 0.3172 0.3696 0.1961 -0.0765 0.0276  0.0526  218  TYR B CE1 
10532 C CE2 . TYR B 220  ? 0.3166 0.3659 0.2036 -0.0671 0.0256  0.0449  218  TYR B CE2 
10533 C CZ  . TYR B 220  ? 0.2847 0.3408 0.1679 -0.0705 0.0286  0.0482  218  TYR B CZ  
10534 O OH  . TYR B 220  ? 0.3685 0.4351 0.2521 -0.0677 0.0327  0.0470  218  TYR B OH  
10535 N N   . SER B 221  ? 0.2700 0.2839 0.1636 -0.0766 0.0109  0.0474  219  SER B N   
10536 C CA  . SER B 221  ? 0.2740 0.2777 0.1686 -0.0744 0.0071  0.0454  219  SER B CA  
10537 C C   . SER B 221  ? 0.2880 0.2918 0.1843 -0.0678 0.0071  0.0413  219  SER B C   
10538 O O   . SER B 221  ? 0.2951 0.3069 0.1965 -0.0650 0.0094  0.0388  219  SER B O   
10539 C CB  . SER B 221  ? 0.2917 0.2963 0.1927 -0.0760 0.0064  0.0447  219  SER B CB  
10540 O OG  . SER B 221  ? 0.2850 0.2798 0.1867 -0.0736 0.0028  0.0427  219  SER B OG  
10541 N N   . TYR B 222  ? 0.2810 0.2759 0.1727 -0.0655 0.0044  0.0407  220  TYR B N   
10542 C CA  . TYR B 222  ? 0.2699 0.2646 0.1622 -0.0597 0.0043  0.0371  220  TYR B CA  
10543 C C   . TYR B 222  ? 0.2956 0.2858 0.1931 -0.0563 0.0020  0.0340  220  TYR B C   
10544 O O   . TYR B 222  ? 0.2856 0.2680 0.1829 -0.0576 -0.0009 0.0346  220  TYR B O   
10545 C CB  . TYR B 222  ? 0.2659 0.2544 0.1507 -0.0588 0.0027  0.0381  220  TYR B CB  
10546 C CG  . TYR B 222  ? 0.2551 0.2490 0.1349 -0.0615 0.0055  0.0408  220  TYR B CG  
10547 C CD1 . TYR B 222  ? 0.2814 0.2844 0.1618 -0.0592 0.0090  0.0393  220  TYR B CD1 
10548 C CD2 . TYR B 222  ? 0.2784 0.2686 0.1528 -0.0666 0.0048  0.0450  220  TYR B CD2 
10549 C CE1 . TYR B 222  ? 0.2841 0.2929 0.1601 -0.0616 0.0118  0.0418  220  TYR B CE1 
10550 C CE2 . TYR B 222  ? 0.2806 0.2764 0.1504 -0.0693 0.0075  0.0477  220  TYR B CE2 
10551 C CZ  . TYR B 222  ? 0.2884 0.2937 0.1591 -0.0667 0.0111  0.0461  220  TYR B CZ  
10552 O OH  . TYR B 222  ? 0.3101 0.3216 0.1764 -0.0693 0.0141  0.0488  220  TYR B OH  
10553 N N   . ASP B 223  ? 0.2772 0.2723 0.1789 -0.0520 0.0034  0.0306  221  ASP B N   
10554 C CA  . ASP B 223  ? 0.2983 0.2907 0.2053 -0.0484 0.0017  0.0274  221  ASP B CA  
10555 C C   . ASP B 223  ? 0.2925 0.2820 0.1976 -0.0438 0.0006  0.0249  221  ASP B C   
10556 O O   . ASP B 223  ? 0.3176 0.3127 0.2227 -0.0414 0.0028  0.0233  221  ASP B O   
10557 C CB  . ASP B 223  ? 0.3007 0.3019 0.2144 -0.0475 0.0043  0.0257  221  ASP B CB  
10558 C CG  . ASP B 223  ? 0.3448 0.3447 0.2637 -0.0431 0.0033  0.0221  221  ASP B CG  
10559 O OD1 . ASP B 223  ? 0.3401 0.3322 0.2587 -0.0418 0.0003  0.0212  221  ASP B OD1 
10560 O OD2 . ASP B 223  ? 0.3868 0.3939 0.3101 -0.0410 0.0056  0.0201  221  ASP B OD2 
10561 N N   . MET B 224  ? 0.2936 0.2743 0.1970 -0.0427 -0.0028 0.0246  222  MET B N   
10562 C CA  . MET B 224  ? 0.3479 0.3254 0.2495 -0.0387 -0.0043 0.0224  222  MET B CA  
10563 C C   . MET B 224  ? 0.3516 0.3307 0.2593 -0.0346 -0.0044 0.0187  222  MET B C   
10564 O O   . MET B 224  ? 0.3717 0.3475 0.2789 -0.0314 -0.0062 0.0168  222  MET B O   
10565 C CB  . MET B 224  ? 0.3363 0.3041 0.2334 -0.0390 -0.0081 0.0237  222  MET B CB  
10566 C CG  . MET B 224  ? 0.3122 0.2773 0.2024 -0.0429 -0.0083 0.0276  222  MET B CG  
10567 S SD  . MET B 224  ? 0.3728 0.3450 0.2581 -0.0436 -0.0049 0.0285  222  MET B SD  
10568 C CE  . MET B 224  ? 0.4194 0.3888 0.3026 -0.0385 -0.0067 0.0254  222  MET B CE  
10569 N N   . LEU B 225  ? 0.3448 0.3291 0.2584 -0.0349 -0.0027 0.0178  223  LEU B N   
10570 C CA  . LEU B 225  ? 0.3299 0.3174 0.2495 -0.0314 -0.0020 0.0146  223  LEU B CA  
10571 C C   . LEU B 225  ? 0.4060 0.3877 0.3291 -0.0297 -0.0049 0.0131  223  LEU B C   
10572 O O   . LEU B 225  ? 0.4016 0.3855 0.3296 -0.0270 -0.0044 0.0106  223  LEU B O   
10573 C CB  . LEU B 225  ? 0.4017 0.3925 0.3203 -0.0280 -0.0007 0.0123  223  LEU B CB  
10574 C CG  . LEU B 225  ? 0.4247 0.4218 0.3398 -0.0290 0.0024  0.0133  223  LEU B CG  
10575 C CD1 . LEU B 225  ? 0.4978 0.4969 0.4115 -0.0252 0.0032  0.0107  223  LEU B CD1 
10576 C CD2 . LEU B 225  ? 0.3648 0.3696 0.2839 -0.0309 0.0053  0.0142  223  LEU B CD2 
10577 N N   . GLY B 226  ? 0.3480 0.3223 0.2685 -0.0310 -0.0076 0.0146  224  GLY B N   
10578 C CA  . GLY B 226  ? 0.3827 0.3520 0.3066 -0.0290 -0.0102 0.0131  224  GLY B CA  
10579 C C   . GLY B 226  ? 0.3224 0.2941 0.2518 -0.0297 -0.0093 0.0125  224  GLY B C   
10580 O O   . GLY B 226  ? 0.3176 0.2913 0.2470 -0.0330 -0.0081 0.0143  224  GLY B O   
10581 N N   . GLU B 227  ? 0.2975 0.2691 0.2318 -0.0267 -0.0099 0.0100  225  GLU B N   
10582 C CA  . GLU B 227  ? 0.2893 0.2632 0.2288 -0.0270 -0.0091 0.0092  225  GLU B CA  
10583 C C   . GLU B 227  ? 0.2541 0.2262 0.1979 -0.0235 -0.0104 0.0067  225  GLU B C   
10584 O O   . GLU B 227  ? 0.2746 0.2471 0.2187 -0.0208 -0.0107 0.0051  225  GLU B O   
10585 C CB  . GLU B 227  ? 0.3102 0.2927 0.2524 -0.0274 -0.0059 0.0088  225  GLU B CB  
10586 C CG  . GLU B 227  ? 0.3614 0.3470 0.3087 -0.0278 -0.0050 0.0080  225  GLU B CG  
10587 C CD  . GLU B 227  ? 0.4054 0.3997 0.3549 -0.0284 -0.0018 0.0081  225  GLU B CD  
10588 O OE1 . GLU B 227  ? 0.3556 0.3532 0.3020 -0.0290 -0.0003 0.0089  225  GLU B OE1 
10589 O OE2 . GLU B 227  ? 0.4116 0.4093 0.3656 -0.0282 -0.0010 0.0072  225  GLU B OE2 
10590 N N   . ALA B 228  ? 0.2417 0.2119 0.1887 -0.0237 -0.0112 0.0064  226  ALA B N   
10591 C CA  . ALA B 228  ? 0.2491 0.2191 0.2009 -0.0207 -0.0118 0.0040  226  ALA B CA  
10592 C C   . ALA B 228  ? 0.2517 0.2180 0.2028 -0.0179 -0.0138 0.0029  226  ALA B C   
10593 O O   . ALA B 228  ? 0.2706 0.2395 0.2242 -0.0154 -0.0134 0.0010  226  ALA B O   
10594 C CB  . ALA B 228  ? 0.2738 0.2507 0.2299 -0.0195 -0.0093 0.0024  226  ALA B CB  
10595 N N   . ALA B 229  ? 0.2433 0.2034 0.1907 -0.0184 -0.0162 0.0043  227  ALA B N   
10596 C CA  . ALA B 229  ? 0.2352 0.1917 0.1823 -0.0157 -0.0185 0.0034  227  ALA B CA  
10597 C C   . ALA B 229  ? 0.2159 0.1735 0.1689 -0.0130 -0.0188 0.0012  227  ALA B C   
10598 O O   . ALA B 229  ? 0.2391 0.1964 0.1948 -0.0133 -0.0185 0.0009  227  ALA B O   
10599 C CB  . ALA B 229  ? 0.2516 0.2010 0.1948 -0.0165 -0.0211 0.0051  227  ALA B CB  
10600 N N   . THR B 230  ? 0.2322 0.1912 0.1869 -0.0106 -0.0193 -0.0004 228  THR B N   
10601 C CA  . THR B 230  ? 0.2256 0.1857 0.1856 -0.0081 -0.0196 -0.0024 228  THR B CA  
10602 C C   . THR B 230  ? 0.2453 0.2009 0.2055 -0.0063 -0.0225 -0.0024 228  THR B C   
10603 O O   . THR B 230  ? 0.2360 0.1913 0.2002 -0.0047 -0.0230 -0.0034 228  THR B O   
10604 C CB  . THR B 230  ? 0.2436 0.2079 0.2057 -0.0066 -0.0185 -0.0041 228  THR B CB  
10605 O OG1 . THR B 230  ? 0.2879 0.2565 0.2494 -0.0080 -0.0159 -0.0040 228  THR B OG1 
10606 C CG2 . THR B 230  ? 0.2351 0.2011 0.2030 -0.0045 -0.0185 -0.0059 228  THR B CG2 
10607 N N   . THR B 231  ? 0.2301 0.1824 0.1859 -0.0064 -0.0243 -0.0013 229  THR B N   
10608 C CA  . THR B 231  ? 0.2245 0.1730 0.1804 -0.0044 -0.0272 -0.0013 229  THR B CA  
10609 C C   . THR B 231  ? 0.2286 0.1715 0.1789 -0.0057 -0.0289 0.0009  229  THR B C   
10610 O O   . THR B 231  ? 0.2350 0.1774 0.1811 -0.0083 -0.0279 0.0024  229  THR B O   
10611 C CB  . THR B 231  ? 0.2413 0.1912 0.1973 -0.0028 -0.0284 -0.0023 229  THR B CB  
10612 O OG1 . THR B 231  ? 0.2514 0.2004 0.2017 -0.0043 -0.0285 -0.0011 229  THR B OG1 
10613 C CG2 . THR B 231  ? 0.2561 0.2111 0.2166 -0.0020 -0.0266 -0.0043 229  THR B CG2 
10614 N N   . ALA B 232  ? 0.2338 0.1725 0.1841 -0.0039 -0.0315 0.0011  230  ALA B N   
10615 C CA  . ALA B 232  ? 0.2591 0.1917 0.2038 -0.0048 -0.0335 0.0033  230  ALA B CA  
10616 C C   . ALA B 232  ? 0.2546 0.1870 0.1941 -0.0060 -0.0339 0.0045  230  ALA B C   
10617 O O   . ALA B 232  ? 0.2691 0.1982 0.2032 -0.0083 -0.0341 0.0066  230  ALA B O   
10618 C CB  . ALA B 232  ? 0.2800 0.2088 0.2259 -0.0019 -0.0364 0.0031  230  ALA B CB  
10619 N N   . ALA B 233  ? 0.2580 0.1940 0.1990 -0.0047 -0.0341 0.0031  231  ALA B N   
10620 C CA  . ALA B 233  ? 0.2654 0.2013 0.2012 -0.0056 -0.0345 0.0040  231  ALA B CA  
10621 C C   . ALA B 233  ? 0.2513 0.1897 0.1842 -0.0085 -0.0316 0.0048  231  ALA B C   
10622 O O   . ALA B 233  ? 0.2633 0.1997 0.1903 -0.0103 -0.0317 0.0066  231  ALA B O   
10623 C CB  . ALA B 233  ? 0.2824 0.2215 0.2204 -0.0037 -0.0352 0.0021  231  ALA B CB  
10624 N N   . ASP B 234  ? 0.2414 0.1843 0.1784 -0.0090 -0.0289 0.0036  232  ASP B N   
10625 C CA  . ASP B 234  ? 0.2465 0.1925 0.1814 -0.0116 -0.0260 0.0044  232  ASP B CA  
10626 C C   . ASP B 234  ? 0.2385 0.1807 0.1694 -0.0143 -0.0262 0.0070  232  ASP B C   
10627 O O   . ASP B 234  ? 0.2541 0.1963 0.1800 -0.0166 -0.0254 0.0087  232  ASP B O   
10628 C CB  . ASP B 234  ? 0.2518 0.2028 0.1922 -0.0115 -0.0235 0.0028  232  ASP B CB  
10629 C CG  . ASP B 234  ? 0.3071 0.2623 0.2511 -0.0093 -0.0227 0.0004  232  ASP B CG  
10630 O OD1 . ASP B 234  ? 0.3215 0.2770 0.2630 -0.0085 -0.0233 -0.0001 232  ASP B OD1 
10631 O OD2 . ASP B 234  ? 0.3048 0.2628 0.2540 -0.0085 -0.0215 -0.0010 232  ASP B OD2 
10632 N N   . ALA B 235  ? 0.2385 0.1772 0.1713 -0.0142 -0.0273 0.0073  233  ALA B N   
10633 C CA  . ALA B 235  ? 0.2468 0.1813 0.1760 -0.0170 -0.0276 0.0096  233  ALA B CA  
10634 C C   . ALA B 235  ? 0.2503 0.1792 0.1729 -0.0177 -0.0299 0.0118  233  ALA B C   
10635 O O   . ALA B 235  ? 0.2579 0.1850 0.1758 -0.0209 -0.0294 0.0142  233  ALA B O   
10636 C CB  . ALA B 235  ? 0.2528 0.1839 0.1851 -0.0161 -0.0287 0.0090  233  ALA B CB  
10637 N N   . GLU B 236  ? 0.2555 0.1818 0.1778 -0.0149 -0.0324 0.0112  234  GLU B N   
10638 C CA  . GLU B 236  ? 0.2669 0.1879 0.1829 -0.0154 -0.0348 0.0134  234  GLU B CA  
10639 C C   . GLU B 236  ? 0.2681 0.1921 0.1796 -0.0172 -0.0333 0.0143  234  GLU B C   
10640 O O   . GLU B 236  ? 0.2845 0.2050 0.1898 -0.0197 -0.0338 0.0169  234  GLU B O   
10641 C CB  . GLU B 236  ? 0.2979 0.2165 0.2152 -0.0118 -0.0378 0.0123  234  GLU B CB  
10642 C CG  . GLU B 236  ? 0.3496 0.2615 0.2606 -0.0118 -0.0408 0.0146  234  GLU B CG  
10643 C CD  . GLU B 236  ? 0.4689 0.3789 0.3817 -0.0081 -0.0440 0.0137  234  GLU B CD  
10644 O OE1 . GLU B 236  ? 0.4855 0.3997 0.4045 -0.0057 -0.0437 0.0112  234  GLU B OE1 
10645 O OE2 . GLU B 236  ? 0.4983 0.4027 0.4064 -0.0076 -0.0468 0.0155  234  GLU B OE2 
10646 N N   . ARG B 237  ? 0.2710 0.2011 0.1853 -0.0162 -0.0315 0.0123  235  ARG B N   
10647 C CA  . ARG B 237  ? 0.2834 0.2167 0.1935 -0.0175 -0.0299 0.0129  235  ARG B CA  
10648 C C   . ARG B 237  ? 0.2766 0.2120 0.1845 -0.0212 -0.0271 0.0147  235  ARG B C   
10649 O O   . ARG B 237  ? 0.2789 0.2133 0.1809 -0.0234 -0.0268 0.0169  235  ARG B O   
10650 C CB  . ARG B 237  ? 0.3094 0.2485 0.2231 -0.0155 -0.0284 0.0100  235  ARG B CB  
10651 C CG  . ARG B 237  ? 0.3465 0.2888 0.2556 -0.0164 -0.0267 0.0103  235  ARG B CG  
10652 C CD  . ARG B 237  ? 0.4223 0.3700 0.3346 -0.0145 -0.0250 0.0075  235  ARG B CD  
10653 N NE  . ARG B 237  ? 0.4792 0.4294 0.3862 -0.0153 -0.0235 0.0079  235  ARG B NE  
10654 C CZ  . ARG B 237  ? 0.5049 0.4582 0.4118 -0.0136 -0.0226 0.0057  235  ARG B CZ  
10655 N NH1 . ARG B 237  ? 0.5481 0.5026 0.4602 -0.0112 -0.0232 0.0030  235  ARG B NH1 
10656 N NH2 . ARG B 237  ? 0.5202 0.4754 0.4216 -0.0143 -0.0211 0.0061  235  ARG B NH2 
10657 N N   . TYR B 238  ? 0.2567 0.1953 0.1695 -0.0219 -0.0252 0.0139  236  TYR B N   
10658 C CA  . TYR B 238  ? 0.2518 0.1931 0.1632 -0.0256 -0.0226 0.0157  236  TYR B CA  
10659 C C   . TYR B 238  ? 0.2677 0.2027 0.1739 -0.0285 -0.0242 0.0189  236  TYR B C   
10660 O O   . TYR B 238  ? 0.2644 0.2005 0.1663 -0.0317 -0.0228 0.0212  236  TYR B O   
10661 C CB  . TYR B 238  ? 0.2455 0.1907 0.1631 -0.0257 -0.0208 0.0143  236  TYR B CB  
10662 C CG  . TYR B 238  ? 0.2807 0.2325 0.2031 -0.0234 -0.0187 0.0115  236  TYR B CG  
10663 C CD1 . TYR B 238  ? 0.3075 0.2634 0.2279 -0.0226 -0.0173 0.0109  236  TYR B CD1 
10664 C CD2 . TYR B 238  ? 0.2788 0.2325 0.2074 -0.0219 -0.0183 0.0096  236  TYR B CD2 
10665 C CE1 . TYR B 238  ? 0.3520 0.3132 0.2765 -0.0204 -0.0156 0.0083  236  TYR B CE1 
10666 C CE2 . TYR B 238  ? 0.2888 0.2481 0.2217 -0.0198 -0.0166 0.0072  236  TYR B CE2 
10667 C CZ  . TYR B 238  ? 0.3478 0.3106 0.2786 -0.0191 -0.0153 0.0065  236  TYR B CZ  
10668 O OH  . TYR B 238  ? 0.3638 0.3314 0.2985 -0.0169 -0.0137 0.0041  236  TYR B OH  
10669 N N   . TYR B 239  ? 0.2666 0.1948 0.1729 -0.0273 -0.0271 0.0191  237  TYR B N   
10670 C CA  . TYR B 239  ? 0.2744 0.1954 0.1752 -0.0298 -0.0291 0.0220  237  TYR B CA  
10671 C C   . TYR B 239  ? 0.2924 0.2114 0.1862 -0.0307 -0.0298 0.0241  237  TYR B C   
10672 O O   . TYR B 239  ? 0.2971 0.2145 0.1859 -0.0344 -0.0293 0.0270  237  TYR B O   
10673 C CB  . TYR B 239  ? 0.2831 0.1969 0.1849 -0.0274 -0.0323 0.0215  237  TYR B CB  
10674 C CG  . TYR B 239  ? 0.3005 0.2058 0.1959 -0.0294 -0.0348 0.0246  237  TYR B CG  
10675 C CD1 . TYR B 239  ? 0.3138 0.2156 0.2079 -0.0326 -0.0346 0.0262  237  TYR B CD1 
10676 C CD2 . TYR B 239  ? 0.4032 0.3037 0.2935 -0.0283 -0.0373 0.0259  237  TYR B CD2 
10677 C CE1 . TYR B 239  ? 0.3306 0.2240 0.2186 -0.0346 -0.0369 0.0290  237  TYR B CE1 
10678 C CE2 . TYR B 239  ? 0.4060 0.2982 0.2900 -0.0301 -0.0396 0.0289  237  TYR B CE2 
10679 C CZ  . TYR B 239  ? 0.3810 0.2695 0.2639 -0.0333 -0.0394 0.0304  237  TYR B CZ  
10680 O OH  . TYR B 239  ? 0.4792 0.3589 0.3556 -0.0353 -0.0417 0.0334  237  TYR B OH  
10681 N N   . ARG B 240  ? 0.2920 0.2110 0.1854 -0.0276 -0.0313 0.0228  238  ARG B N   
10682 C CA  . ARG B 240  ? 0.3098 0.2267 0.1963 -0.0282 -0.0323 0.0246  238  ARG B CA  
10683 C C   . ARG B 240  ? 0.2917 0.2146 0.1755 -0.0307 -0.0290 0.0255  238  ARG B C   
10684 O O   . ARG B 240  ? 0.3193 0.2404 0.1967 -0.0331 -0.0290 0.0282  238  ARG B O   
10685 C CB  . ARG B 240  ? 0.3188 0.2352 0.2059 -0.0242 -0.0345 0.0227  238  ARG B CB  
10686 C CG  . ARG B 240  ? 0.3501 0.2605 0.2390 -0.0216 -0.0381 0.0223  238  ARG B CG  
10687 C CD  . ARG B 240  ? 0.3823 0.2844 0.2650 -0.0233 -0.0405 0.0255  238  ARG B CD  
10688 N NE  . ARG B 240  ? 0.4457 0.3423 0.3304 -0.0204 -0.0438 0.0250  238  ARG B NE  
10689 C CZ  . ARG B 240  ? 0.5195 0.4081 0.4002 -0.0209 -0.0463 0.0273  238  ARG B CZ  
10690 N NH1 . ARG B 240  ? 0.4698 0.3545 0.3440 -0.0247 -0.0460 0.0304  238  ARG B NH1 
10691 N NH2 . ARG B 240  ? 0.5776 0.4618 0.4607 -0.0177 -0.0491 0.0264  238  ARG B NH2 
10692 N N   . ASP B 241  ? 0.2965 0.2269 0.1854 -0.0301 -0.0260 0.0232  239  ASP B N   
10693 C CA  . ASP B 241  ? 0.3147 0.2517 0.2017 -0.0321 -0.0226 0.0238  239  ASP B CA  
10694 C C   . ASP B 241  ? 0.2839 0.2209 0.1687 -0.0367 -0.0211 0.0269  239  ASP B C   
10695 O O   . ASP B 241  ? 0.2994 0.2382 0.1791 -0.0393 -0.0196 0.0291  239  ASP B O   
10696 C CB  . ASP B 241  ? 0.3540 0.2986 0.2472 -0.0302 -0.0199 0.0207  239  ASP B CB  
10697 C CG  . ASP B 241  ? 0.4054 0.3510 0.2995 -0.0263 -0.0209 0.0179  239  ASP B CG  
10698 O OD1 . ASP B 241  ? 0.4377 0.3788 0.3273 -0.0252 -0.0235 0.0184  239  ASP B OD1 
10699 O OD2 . ASP B 241  ? 0.4956 0.4462 0.3948 -0.0243 -0.0193 0.0153  239  ASP B OD2 
10700 N N   . TYR B 242  ? 0.2809 0.2157 0.1693 -0.0379 -0.0216 0.0271  240  TYR B N   
10701 C CA  . TYR B 242  ? 0.2784 0.2123 0.1645 -0.0426 -0.0207 0.0302  240  TYR B CA  
10702 C C   . TYR B 242  ? 0.2880 0.2142 0.1664 -0.0447 -0.0231 0.0335  240  TYR B C   
10703 O O   . TYR B 242  ? 0.2864 0.2133 0.1603 -0.0487 -0.0218 0.0365  240  TYR B O   
10704 C CB  . TYR B 242  ? 0.2757 0.2073 0.1665 -0.0432 -0.0215 0.0296  240  TYR B CB  
10705 C CG  . TYR B 242  ? 0.2595 0.1986 0.1574 -0.0423 -0.0189 0.0271  240  TYR B CG  
10706 C CD1 . TYR B 242  ? 0.2782 0.2264 0.1776 -0.0434 -0.0154 0.0269  240  TYR B CD1 
10707 C CD2 . TYR B 242  ? 0.2646 0.2018 0.1677 -0.0404 -0.0200 0.0251  240  TYR B CD2 
10708 C CE1 . TYR B 242  ? 0.2801 0.2348 0.1860 -0.0424 -0.0132 0.0247  240  TYR B CE1 
10709 C CE2 . TYR B 242  ? 0.2665 0.2102 0.1759 -0.0397 -0.0179 0.0230  240  TYR B CE2 
10710 C CZ  . TYR B 242  ? 0.2827 0.2350 0.1935 -0.0407 -0.0146 0.0228  240  TYR B CZ  
10711 O OH  . TYR B 242  ? 0.2777 0.2360 0.1948 -0.0398 -0.0127 0.0208  240  TYR B OH  
10712 N N   . GLU B 243  ? 0.2838 0.2025 0.1607 -0.0421 -0.0266 0.0331  241  GLU B N   
10713 C CA  . GLU B 243  ? 0.2983 0.2088 0.1678 -0.0437 -0.0293 0.0363  241  GLU B CA  
10714 C C   . GLU B 243  ? 0.2878 0.2008 0.1512 -0.0449 -0.0281 0.0379  241  GLU B C   
10715 O O   . GLU B 243  ? 0.3027 0.2132 0.1602 -0.0487 -0.0280 0.0414  241  GLU B O   
10716 C CB  . GLU B 243  ? 0.3142 0.2177 0.1840 -0.0398 -0.0332 0.0350  241  GLU B CB  
10717 C CG  . GLU B 243  ? 0.3803 0.2748 0.2425 -0.0406 -0.0364 0.0380  241  GLU B CG  
10718 C CD  . GLU B 243  ? 0.4052 0.2942 0.2682 -0.0360 -0.0401 0.0366  241  GLU B CD  
10719 O OE1 . GLU B 243  ? 0.4381 0.3317 0.3057 -0.0324 -0.0399 0.0335  241  GLU B OE1 
10720 O OE2 . GLU B 243  ? 0.4667 0.3471 0.3258 -0.0360 -0.0432 0.0385  241  GLU B OE2 
10721 N N   . SER B 244  ? 0.2988 0.2167 0.1636 -0.0416 -0.0273 0.0355  242  SER B N   
10722 C CA  A SER B 244  ? 0.3058 0.2264 0.1647 -0.0422 -0.0261 0.0366  242  SER B CA  
10723 C CA  B SER B 244  ? 0.3060 0.2266 0.1649 -0.0423 -0.0261 0.0366  242  SER B CA  
10724 C C   . SER B 244  ? 0.2899 0.2173 0.1478 -0.0461 -0.0222 0.0383  242  SER B C   
10725 O O   . SER B 244  ? 0.3021 0.2290 0.1532 -0.0489 -0.0215 0.0412  242  SER B O   
10726 C CB  A SER B 244  ? 0.3234 0.2482 0.1849 -0.0379 -0.0259 0.0330  242  SER B CB  
10727 C CB  B SER B 244  ? 0.3236 0.2482 0.1847 -0.0380 -0.0260 0.0332  242  SER B CB  
10728 O OG  A SER B 244  ? 0.3708 0.2984 0.2266 -0.0381 -0.0247 0.0337  242  SER B OG  
10729 O OG  B SER B 244  ? 0.2976 0.2162 0.1590 -0.0347 -0.0299 0.0321  242  SER B OG  
10730 N N   . ALA B 245  ? 0.2953 0.2292 0.1596 -0.0464 -0.0195 0.0366  243  ALA B N   
10731 C CA  . ALA B 245  ? 0.3059 0.2471 0.1699 -0.0500 -0.0157 0.0382  243  ALA B CA  
10732 C C   . ALA B 245  ? 0.3184 0.2555 0.1787 -0.0552 -0.0161 0.0423  243  ALA B C   
10733 O O   . ALA B 245  ? 0.3172 0.2578 0.1733 -0.0587 -0.0139 0.0450  243  ALA B O   
10734 C CB  . ALA B 245  ? 0.2972 0.2460 0.1693 -0.0490 -0.0131 0.0356  243  ALA B CB  
10735 N N   . ILE B 246  ? 0.3080 0.2376 0.1695 -0.0558 -0.0190 0.0429  244  ILE B N   
10736 C CA  . ILE B 246  ? 0.3223 0.2468 0.1796 -0.0609 -0.0198 0.0468  244  ILE B CA  
10737 C C   . ILE B 246  ? 0.3365 0.2562 0.1849 -0.0627 -0.0210 0.0501  244  ILE B C   
10738 O O   . ILE B 246  ? 0.3535 0.2740 0.1977 -0.0675 -0.0196 0.0536  244  ILE B O   
10739 C CB  . ILE B 246  ? 0.3137 0.2299 0.1733 -0.0607 -0.0230 0.0464  244  ILE B CB  
10740 C CG1 . ILE B 246  ? 0.3172 0.2389 0.1848 -0.0603 -0.0213 0.0440  244  ILE B CG1 
10741 C CG2 . ILE B 246  ? 0.3376 0.2463 0.1913 -0.0656 -0.0246 0.0506  244  ILE B CG2 
10742 C CD1 . ILE B 246  ? 0.3464 0.2606 0.2167 -0.0592 -0.0242 0.0429  244  ILE B CD1 
10743 N N   . HIS B 247  ? 0.3378 0.2524 0.1831 -0.0591 -0.0236 0.0492  245  HIS B N   
10744 C CA  . HIS B 247  ? 0.3321 0.2424 0.1686 -0.0605 -0.0247 0.0523  245  HIS B CA  
10745 C C   . HIS B 247  ? 0.3388 0.2578 0.1725 -0.0624 -0.0208 0.0534  245  HIS B C   
10746 O O   . HIS B 247  ? 0.3647 0.2825 0.1920 -0.0665 -0.0202 0.0572  245  HIS B O   
10747 C CB  . HIS B 247  ? 0.3457 0.2504 0.1799 -0.0559 -0.0281 0.0508  245  HIS B CB  
10748 C CG  . HIS B 247  ? 0.3725 0.2673 0.2072 -0.0545 -0.0323 0.0509  245  HIS B CG  
10749 N ND1 . HIS B 247  ? 0.3724 0.2583 0.2014 -0.0576 -0.0346 0.0546  245  HIS B ND1 
10750 C CD2 . HIS B 247  ? 0.3880 0.2803 0.2279 -0.0502 -0.0345 0.0478  245  HIS B CD2 
10751 C CE1 . HIS B 247  ? 0.4051 0.2833 0.2358 -0.0550 -0.0381 0.0536  245  HIS B CE1 
10752 N NE2 . HIS B 247  ? 0.4142 0.2966 0.2517 -0.0505 -0.0380 0.0495  245  HIS B NE2 
10753 N N   . ALA B 248  ? 0.3110 0.2389 0.1494 -0.0596 -0.0181 0.0501  246  ALA B N   
10754 C CA  . ALA B 248  ? 0.3322 0.2685 0.1679 -0.0607 -0.0143 0.0508  246  ALA B CA  
10755 C C   . ALA B 248  ? 0.3245 0.2668 0.1615 -0.0658 -0.0111 0.0533  246  ALA B C   
10756 O O   . ALA B 248  ? 0.3369 0.2820 0.1685 -0.0692 -0.0091 0.0564  246  ALA B O   
10757 C CB  . ALA B 248  ? 0.3384 0.2820 0.1788 -0.0561 -0.0124 0.0464  246  ALA B CB  
10758 N N   . ILE B 249  ? 0.3232 0.2677 0.1674 -0.0664 -0.0105 0.0520  247  ILE B N   
10759 C CA  . ILE B 249  ? 0.3219 0.2725 0.1682 -0.0712 -0.0077 0.0542  247  ILE B CA  
10760 C C   . ILE B 249  ? 0.3234 0.2668 0.1638 -0.0767 -0.0094 0.0589  247  ILE B C   
10761 O O   . ILE B 249  ? 0.3450 0.2931 0.1829 -0.0813 -0.0069 0.0622  247  ILE B O   
10762 C CB  . ILE B 249  ? 0.3018 0.2555 0.1570 -0.0704 -0.0072 0.0517  247  ILE B CB  
10763 C CG1 . ILE B 249  ? 0.2988 0.2601 0.1596 -0.0654 -0.0052 0.0473  247  ILE B CG1 
10764 C CG2 . ILE B 249  ? 0.3361 0.2952 0.1934 -0.0759 -0.0049 0.0543  247  ILE B CG2 
10765 C CD1 . ILE B 249  ? 0.2992 0.2605 0.1680 -0.0633 -0.0061 0.0443  247  ILE B CD1 
10766 N N   . GLY B 250  ? 0.3477 0.2798 0.1859 -0.0761 -0.0136 0.0594  248  GLY B N   
10767 C CA  . GLY B 250  ? 0.3690 0.2929 0.2013 -0.0810 -0.0156 0.0638  248  GLY B CA  
10768 C C   . GLY B 250  ? 0.4128 0.3357 0.2363 -0.0832 -0.0152 0.0672  248  GLY B C   
10769 O O   . GLY B 250  ? 0.4033 0.3258 0.2226 -0.0887 -0.0143 0.0713  248  GLY B O   
10770 N N   . LYS B 251  ? 0.3777 0.3001 0.1981 -0.0789 -0.0158 0.0657  249  LYS B N   
10771 C CA  . LYS B 251  ? 0.4223 0.3442 0.2341 -0.0807 -0.0152 0.0688  249  LYS B CA  
10772 C C   . LYS B 251  ? 0.3783 0.3120 0.1902 -0.0836 -0.0102 0.0700  249  LYS B C   
10773 O O   . LYS B 251  ? 0.4168 0.3508 0.2225 -0.0882 -0.0090 0.0742  249  LYS B O   
10774 C CB  . LYS B 251  ? 0.4229 0.3420 0.2315 -0.0754 -0.0171 0.0665  249  LYS B CB  
10775 N N   . ALA B 252  ? 0.3950 0.3388 0.2140 -0.0810 -0.0071 0.0665  250  ALA B N   
10776 C CA  . ALA B 252  ? 0.3786 0.3344 0.1984 -0.0832 -0.0022 0.0674  250  ALA B CA  
10777 C C   . ALA B 252  ? 0.3956 0.3541 0.2172 -0.0895 -0.0007 0.0708  250  ALA B C   
10778 O O   . ALA B 252  ? 0.4312 0.3965 0.2499 -0.0934 0.0025  0.0738  250  ALA B O   
10779 C CB  . ALA B 252  ? 0.3805 0.3456 0.2077 -0.0785 0.0004  0.0626  250  ALA B CB  
10780 N N   . SER B 253  ? 0.3791 0.3326 0.2054 -0.0907 -0.0030 0.0704  251  SER B N   
10781 C CA  . SER B 253  ? 0.3943 0.3491 0.2218 -0.0971 -0.0023 0.0738  251  SER B CA  
10782 C C   . SER B 253  ? 0.3911 0.3405 0.2098 -0.1024 -0.0030 0.0791  251  SER B C   
10783 O O   . SER B 253  ? 0.4321 0.3877 0.2499 -0.1079 -0.0003 0.0825  251  SER B O   
10784 C CB  . SER B 253  ? 0.3805 0.3279 0.2126 -0.0971 -0.0055 0.0725  251  SER B CB  
10785 O OG  . SER B 253  ? 0.4071 0.3552 0.2400 -0.1035 -0.0051 0.0757  251  SER B OG  
10786 N N   . ALA B 254  ? 0.3934 0.3314 0.2053 -0.1010 -0.0067 0.0800  252  ALA B N   
10787 C CA  . ALA B 254  ? 0.4437 0.3756 0.2461 -0.1054 -0.0077 0.0850  252  ALA B CA  
10788 C C   . ALA B 254  ? 0.4648 0.3942 0.2664 -0.1127 -0.0080 0.0893  252  ALA B C   
10789 O O   . ALA B 254  ? 0.4881 0.4216 0.2879 -0.1164 -0.0061 0.0920  252  ALA B O   
10790 C CB  . ALA B 254  ? 0.4656 0.4058 0.2632 -0.1053 -0.0041 0.0862  252  ALA B CB  
10791 N N   . GLY B 255  ? 0.4765 0.4004 0.2828 -0.1131 -0.0104 0.0880  253  GLY B N   
10792 C CA  . GLY B 255  ? 0.4583 0.3788 0.2651 -0.1192 -0.0114 0.0910  253  GLY B CA  
10793 C C   . GLY B 255  ? 0.4813 0.4146 0.2949 -0.1230 -0.0076 0.0913  253  GLY B C   
10794 O O   . GLY B 255  ? 0.5104 0.4426 0.3252 -0.1279 -0.0081 0.0934  253  GLY B O   
10795 N N   . ARG B 256  ? 0.4236 0.3690 0.2418 -0.1208 -0.0038 0.0891  254  ARG B N   
10796 C CA  . ARG B 256  ? 0.4378 0.3960 0.2632 -0.1239 -0.0001 0.0892  254  ARG B CA  
10797 C C   . ARG B 256  ? 0.4211 0.3768 0.2521 -0.1262 -0.0019 0.0884  254  ARG B C   
10798 O O   . ARG B 256  ? 0.4332 0.3978 0.2700 -0.1297 0.0002  0.0890  254  ARG B O   
10799 C CB  . ARG B 256  ? 0.4219 0.3934 0.2510 -0.1203 0.0042  0.0867  254  ARG B CB  
10800 C CG  . ARG B 256  ? 0.4071 0.3863 0.2327 -0.1200 0.0075  0.0880  254  ARG B CG  
10801 C CD  . ARG B 256  ? 0.4001 0.3917 0.2291 -0.1159 0.0117  0.0852  254  ARG B CD  
10802 N NE  . ARG B 256  ? 0.4066 0.3931 0.2354 -0.1087 0.0098  0.0809  254  ARG B NE  
10803 C CZ  . ARG B 256  ? 0.3970 0.3914 0.2306 -0.1031 0.0120  0.0766  254  ARG B CZ  
10804 N NH1 . ARG B 256  ? 0.4175 0.4250 0.2570 -0.1034 0.0161  0.0758  254  ARG B NH1 
10805 N NH2 . ARG B 256  ? 0.4282 0.4171 0.2607 -0.0970 0.0100  0.0730  254  ARG B NH2 
10806 N N   . GLY B 257  ? 0.4280 0.3722 0.2585 -0.1235 -0.0058 0.0865  255  GLY B N   
10807 C CA  . GLY B 257  ? 0.4224 0.3633 0.2581 -0.1251 -0.0078 0.0853  255  GLY B CA  
10808 C C   . GLY B 257  ? 0.3847 0.3352 0.2300 -0.1207 -0.0058 0.0807  255  GLY B C   
10809 O O   . GLY B 257  ? 0.4007 0.3608 0.2489 -0.1166 -0.0028 0.0783  255  GLY B O   
10810 N N   . ILE B 258  ? 0.3928 0.3404 0.2427 -0.1218 -0.0076 0.0793  256  ILE B N   
10811 C CA  . ILE B 258  ? 0.3725 0.3263 0.2309 -0.1171 -0.0067 0.0747  256  ILE B CA  
10812 C C   . ILE B 258  ? 0.3536 0.3231 0.2185 -0.1187 -0.0023 0.0745  256  ILE B C   
10813 O O   . ILE B 258  ? 0.3659 0.3424 0.2375 -0.1140 -0.0008 0.0706  256  ILE B O   
10814 C CB  . ILE B 258  ? 0.4119 0.3565 0.2726 -0.1172 -0.0103 0.0731  256  ILE B CB  
10815 C CG1 . ILE B 258  ? 0.4131 0.3573 0.2735 -0.1250 -0.0108 0.0765  256  ILE B CG1 
10816 C CG2 . ILE B 258  ? 0.4194 0.3489 0.2742 -0.1146 -0.0145 0.0728  256  ILE B CG2 
10817 C CD1 . ILE B 258  ? 0.4354 0.3714 0.2981 -0.1254 -0.0140 0.0749  256  ILE B CD1 
10818 N N   . TYR B 259  ? 0.3600 0.3356 0.2233 -0.1250 -0.0003 0.0786  257  TYR B N   
10819 C CA  . TYR B 259  ? 0.3730 0.3642 0.2429 -0.1267 0.0038  0.0786  257  TYR B CA  
10820 C C   . TYR B 259  ? 0.3694 0.3712 0.2384 -0.1242 0.0080  0.0787  257  TYR B C   
10821 O O   . TYR B 259  ? 0.3592 0.3709 0.2339 -0.1197 0.0107  0.0754  257  TYR B O   
10822 C CB  . TYR B 259  ? 0.3977 0.3907 0.2676 -0.1350 0.0037  0.0827  257  TYR B CB  
10823 C CG  . TYR B 259  ? 0.3884 0.3699 0.2583 -0.1373 -0.0006 0.0825  257  TYR B CG  
10824 C CD1 . TYR B 259  ? 0.3922 0.3747 0.2687 -0.1347 -0.0014 0.0790  257  TYR B CD1 
10825 C CD2 . TYR B 259  ? 0.4455 0.4150 0.3097 -0.1405 -0.0042 0.0847  257  TYR B CD2 
10826 C CE1 . TYR B 259  ? 0.4048 0.3765 0.2809 -0.1365 -0.0054 0.0785  257  TYR B CE1 
10827 C CE2 . TYR B 259  ? 0.3788 0.3372 0.2427 -0.1422 -0.0082 0.0841  257  TYR B CE2 
10828 C CZ  . TYR B 259  ? 0.4423 0.4017 0.3115 -0.1407 -0.0086 0.0814  257  TYR B CZ  
10829 O OH  . TYR B 259  ? 0.4321 0.3807 0.3009 -0.1420 -0.0126 0.0806  257  TYR B OH  
10830 N N   . GLU B 260  ? 0.3707 0.3704 0.2322 -0.1272 0.0085  0.0824  258  GLU B N   
10831 C CA  . GLU B 260  ? 0.4083 0.4172 0.2679 -0.1247 0.0123  0.0824  258  GLU B CA  
10832 C C   . GLU B 260  ? 0.4400 0.4445 0.2982 -0.1169 0.0114  0.0784  258  GLU B C   
10833 O O   . GLU B 260  ? 0.4369 0.4505 0.2974 -0.1124 0.0146  0.0759  258  GLU B O   
10834 C CB  . GLU B 260  ? 0.4161 0.4230 0.2699 -0.1282 0.0124  0.0861  258  GLU B CB  
10835 C CG  . GLU B 260  ? 0.5487 0.5636 0.3996 -0.1253 0.0160  0.0860  258  GLU B CG  
10836 C CD  . GLU B 260  ? 0.5418 0.5543 0.3871 -0.1285 0.0160  0.0895  258  GLU B CD  
10837 O OE1 . GLU B 260  ? 0.5927 0.5997 0.4374 -0.1335 0.0137  0.0920  258  GLU B OE1 
10838 O OE2 . GLU B 260  ? 0.6070 0.6229 0.4480 -0.1260 0.0182  0.0896  258  GLU B OE2 
10839 N N   . GLY B 261  ? 0.3828 0.3733 0.2372 -0.1152 0.0072  0.0776  259  GLY B N   
10840 C CA  . GLY B 261  ? 0.3731 0.3584 0.2250 -0.1086 0.0059  0.0745  259  GLY B CA  
10841 C C   . GLY B 261  ? 0.3508 0.3376 0.2100 -0.1026 0.0054  0.0693  259  GLY B C   
10842 O O   . GLY B 261  ? 0.3522 0.3408 0.2177 -0.1035 0.0051  0.0681  259  GLY B O   
10843 N N   . PRO B 262  ? 0.3392 0.3247 0.1974 -0.0966 0.0053  0.0662  260  PRO B N   
10844 C CA  . PRO B 262  ? 0.3389 0.3262 0.2038 -0.0907 0.0050  0.0613  260  PRO B CA  
10845 C C   . PRO B 262  ? 0.3565 0.3325 0.2227 -0.0896 0.0007  0.0598  260  PRO B C   
10846 O O   . PRO B 262  ? 0.3659 0.3312 0.2268 -0.0917 -0.0025 0.0621  260  PRO B O   
10847 C CB  . PRO B 262  ? 0.3497 0.3375 0.2113 -0.0854 0.0057  0.0591  260  PRO B CB  
10848 C CG  . PRO B 262  ? 0.3680 0.3479 0.2204 -0.0879 0.0040  0.0626  260  PRO B CG  
10849 C CD  . PRO B 262  ? 0.3485 0.3313 0.1990 -0.0950 0.0054  0.0672  260  PRO B CD  
10850 N N   . GLY B 263  ? 0.3142 0.2929 0.1875 -0.0859 0.0007  0.0560  261  GLY B N   
10851 C CA  . GLY B 263  ? 0.3219 0.2911 0.1971 -0.0837 -0.0029 0.0540  261  GLY B CA  
10852 C C   . GLY B 263  ? 0.2812 0.2519 0.1608 -0.0770 -0.0030 0.0494  261  GLY B C   
10853 O O   . GLY B 263  ? 0.3016 0.2792 0.1817 -0.0740 -0.0005 0.0478  261  GLY B O   
10854 N N   . ILE B 264  ? 0.2890 0.2530 0.1715 -0.0748 -0.0058 0.0472  262  ILE B N   
10855 C CA  . ILE B 264  ? 0.2703 0.2350 0.1573 -0.0688 -0.0061 0.0430  262  ILE B CA  
10856 C C   . ILE B 264  ? 0.2849 0.2509 0.1788 -0.0683 -0.0064 0.0409  262  ILE B C   
10857 O O   . ILE B 264  ? 0.2951 0.2571 0.1891 -0.0719 -0.0078 0.0425  262  ILE B O   
10858 C CB  . ILE B 264  ? 0.2987 0.2533 0.1817 -0.0655 -0.0096 0.0422  262  ILE B CB  
10859 C CG1 . ILE B 264  ? 0.2839 0.2407 0.1710 -0.0595 -0.0095 0.0380  262  ILE B CG1 
10860 C CG2 . ILE B 264  ? 0.3178 0.2622 0.2000 -0.0668 -0.0132 0.0430  262  ILE B CG2 
10861 C CD1 . ILE B 264  ? 0.3113 0.2596 0.1948 -0.0561 -0.0128 0.0372  262  ILE B CD1 
10862 N N   . SER B 265  ? 0.2492 0.2207 0.1487 -0.0639 -0.0051 0.0374  263  SER B N   
10863 C CA  . SER B 265  ? 0.2584 0.2310 0.1645 -0.0626 -0.0054 0.0350  263  SER B CA  
10864 C C   . SER B 265  ? 0.2648 0.2325 0.1726 -0.0573 -0.0075 0.0318  263  SER B C   
10865 O O   . SER B 265  ? 0.3197 0.2886 0.2265 -0.0538 -0.0070 0.0303  263  SER B O   
10866 C CB  . SER B 265  ? 0.2784 0.2628 0.1900 -0.0622 -0.0019 0.0338  263  SER B CB  
10867 O OG  . SER B 265  ? 0.2914 0.2809 0.2029 -0.0674 -0.0002 0.0367  263  SER B OG  
10868 N N   . ILE B 266  ? 0.2451 0.2074 0.1556 -0.0567 -0.0097 0.0307  264  ILE B N   
10869 C CA  . ILE B 266  ? 0.2583 0.2160 0.1709 -0.0519 -0.0116 0.0277  264  ILE B CA  
10870 C C   . ILE B 266  ? 0.2487 0.2095 0.1681 -0.0505 -0.0111 0.0253  264  ILE B C   
10871 O O   . ILE B 266  ? 0.2580 0.2217 0.1794 -0.0536 -0.0102 0.0262  264  ILE B O   
10872 C CB  . ILE B 266  ? 0.2740 0.2205 0.1823 -0.0517 -0.0153 0.0287  264  ILE B CB  
10873 C CG1 . ILE B 266  ? 0.3136 0.2550 0.2219 -0.0549 -0.0168 0.0299  264  ILE B CG1 
10874 C CG2 . ILE B 266  ? 0.2971 0.2402 0.1983 -0.0533 -0.0160 0.0313  264  ILE B CG2 
10875 C CD1 . ILE B 266  ? 0.3507 0.2809 0.2559 -0.0537 -0.0205 0.0300  264  ILE B CD1 
10876 N N   . LYS B 267  ? 0.2414 0.2015 0.1639 -0.0459 -0.0118 0.0224  265  LYS B N   
10877 C CA  . LYS B 267  ? 0.2372 0.1989 0.1657 -0.0440 -0.0117 0.0200  265  LYS B CA  
10878 C C   . LYS B 267  ? 0.2328 0.1859 0.1610 -0.0416 -0.0148 0.0189  265  LYS B C   
10879 O O   . LYS B 267  ? 0.2493 0.1991 0.1759 -0.0387 -0.0162 0.0181  265  LYS B O   
10880 C CB  . LYS B 267  ? 0.2373 0.2066 0.1704 -0.0406 -0.0095 0.0174  265  LYS B CB  
10881 C CG  . LYS B 267  ? 0.2632 0.2418 0.1980 -0.0425 -0.0063 0.0181  265  LYS B CG  
10882 C CD  . LYS B 267  ? 0.3189 0.3041 0.2576 -0.0388 -0.0043 0.0155  265  LYS B CD  
10883 C CE  . LYS B 267  ? 0.3118 0.3066 0.2524 -0.0403 -0.0010 0.0161  265  LYS B CE  
10884 N NZ  . LYS B 267  ? 0.3317 0.3283 0.2674 -0.0433 0.0001  0.0188  265  LYS B NZ  
10885 N N   . LEU B 268  ? 0.2317 0.1812 0.1613 -0.0429 -0.0160 0.0188  266  LEU B N   
10886 C CA  . LEU B 268  ? 0.2416 0.1832 0.1710 -0.0403 -0.0188 0.0176  266  LEU B CA  
10887 C C   . LEU B 268  ? 0.2431 0.1871 0.1770 -0.0354 -0.0186 0.0146  266  LEU B C   
10888 O O   . LEU B 268  ? 0.2440 0.1827 0.1771 -0.0325 -0.0207 0.0139  266  LEU B O   
10889 C CB  . LEU B 268  ? 0.2352 0.1729 0.1653 -0.0422 -0.0198 0.0178  266  LEU B CB  
10890 C CG  . LEU B 268  ? 0.2537 0.1879 0.1790 -0.0474 -0.0205 0.0209  266  LEU B CG  
10891 C CD1 . LEU B 268  ? 0.3038 0.2334 0.2295 -0.0491 -0.0219 0.0207  266  LEU B CD1 
10892 C CD2 . LEU B 268  ? 0.2971 0.2238 0.2161 -0.0479 -0.0226 0.0229  266  LEU B CD2 
10893 N N   . SER B 269  ? 0.2285 0.1805 0.1671 -0.0343 -0.0162 0.0130  267  SER B N   
10894 C CA  . SER B 269  ? 0.2308 0.1848 0.1734 -0.0299 -0.0160 0.0103  267  SER B CA  
10895 C C   . SER B 269  ? 0.2240 0.1773 0.1643 -0.0278 -0.0167 0.0101  267  SER B C   
10896 O O   . SER B 269  ? 0.2348 0.1876 0.1776 -0.0243 -0.0174 0.0082  267  SER B O   
10897 C CB  . SER B 269  ? 0.2414 0.2037 0.1891 -0.0292 -0.0134 0.0088  267  SER B CB  
10898 O OG  . SER B 269  ? 0.2397 0.2075 0.1860 -0.0302 -0.0113 0.0095  267  SER B OG  
10899 N N   . ALA B 270  ? 0.2148 0.1680 0.1503 -0.0299 -0.0163 0.0121  268  ALA B N   
10900 C CA  . ALA B 270  ? 0.2302 0.1819 0.1627 -0.0280 -0.0173 0.0121  268  ALA B CA  
10901 C C   . ALA B 270  ? 0.2497 0.1932 0.1797 -0.0268 -0.0206 0.0125  268  ALA B C   
10902 O O   . ALA B 270  ? 0.2511 0.1930 0.1798 -0.0243 -0.0219 0.0119  268  ALA B O   
10903 C CB  . ALA B 270  ? 0.2543 0.2079 0.1818 -0.0308 -0.0161 0.0143  268  ALA B CB  
10904 N N   . LEU B 271  ? 0.2315 0.1694 0.1602 -0.0283 -0.0221 0.0137  269  LEU B N   
10905 C CA  . LEU B 271  ? 0.2682 0.1978 0.1932 -0.0275 -0.0252 0.0147  269  LEU B CA  
10906 C C   . LEU B 271  ? 0.2420 0.1685 0.1707 -0.0240 -0.0270 0.0127  269  LEU B C   
10907 O O   . LEU B 271  ? 0.2696 0.1893 0.1957 -0.0227 -0.0297 0.0132  269  LEU B O   
10908 C CB  . LEU B 271  ? 0.2741 0.1982 0.1940 -0.0314 -0.0261 0.0175  269  LEU B CB  
10909 C CG  . LEU B 271  ? 0.2780 0.2048 0.1936 -0.0348 -0.0247 0.0199  269  LEU B CG  
10910 C CD1 . LEU B 271  ? 0.3260 0.2479 0.2374 -0.0393 -0.0254 0.0227  269  LEU B CD1 
10911 C CD2 . LEU B 271  ? 0.2806 0.2053 0.1921 -0.0332 -0.0259 0.0205  269  LEU B CD2 
10912 N N   . HIS B 272  ? 0.2476 0.1789 0.1821 -0.0224 -0.0255 0.0104  270  HIS B N   
10913 C CA  . HIS B 272  ? 0.2490 0.1780 0.1871 -0.0190 -0.0269 0.0085  270  HIS B CA  
10914 C C   . HIS B 272  ? 0.2287 0.1648 0.1730 -0.0172 -0.0248 0.0061  270  HIS B C   
10915 O O   . HIS B 272  ? 0.2476 0.1885 0.1935 -0.0191 -0.0225 0.0060  270  HIS B O   
10916 C CB  . HIS B 272  ? 0.2789 0.2024 0.2161 -0.0201 -0.0280 0.0090  270  HIS B CB  
10917 C CG  . HIS B 272  ? 0.2666 0.1861 0.2058 -0.0164 -0.0300 0.0075  270  HIS B CG  
10918 N ND1 . HIS B 272  ? 0.2860 0.2093 0.2309 -0.0138 -0.0291 0.0051  270  HIS B ND1 
10919 C CD2 . HIS B 272  ? 0.3345 0.2469 0.2707 -0.0148 -0.0327 0.0081  270  HIS B CD2 
10920 C CE1 . HIS B 272  ? 0.2921 0.2111 0.2377 -0.0107 -0.0311 0.0043  270  HIS B CE1 
10921 N NE2 . HIS B 272  ? 0.3375 0.2499 0.2780 -0.0111 -0.0334 0.0061  270  HIS B NE2 
10922 N N   . PRO B 273  ? 0.2370 0.1739 0.1848 -0.0137 -0.0256 0.0042  271  PRO B N   
10923 C CA  . PRO B 273  ? 0.2306 0.1738 0.1840 -0.0121 -0.0237 0.0021  271  PRO B CA  
10924 C C   . PRO B 273  ? 0.2249 0.1687 0.1819 -0.0119 -0.0229 0.0011  271  PRO B C   
10925 O O   . PRO B 273  ? 0.2367 0.1859 0.1981 -0.0111 -0.0211 -0.0004 271  PRO B O   
10926 C CB  . PRO B 273  ? 0.2507 0.1938 0.2062 -0.0087 -0.0253 0.0008  271  PRO B CB  
10927 C CG  . PRO B 273  ? 0.2760 0.2124 0.2284 -0.0079 -0.0280 0.0019  271  PRO B CG  
10928 C CD  . PRO B 273  ? 0.2521 0.1848 0.1986 -0.0111 -0.0283 0.0042  271  PRO B CD  
10929 N N   . ARG B 274  ? 0.2256 0.1640 0.1807 -0.0126 -0.0242 0.0018  272  ARG B N   
10930 C CA  . ARG B 274  ? 0.2310 0.1696 0.1889 -0.0125 -0.0236 0.0008  272  ARG B CA  
10931 C C   . ARG B 274  ? 0.2538 0.1894 0.2082 -0.0161 -0.0235 0.0024  272  ARG B C   
10932 O O   . ARG B 274  ? 0.2532 0.1835 0.2062 -0.0162 -0.0248 0.0024  272  ARG B O   
10933 C CB  . ARG B 274  ? 0.2428 0.1773 0.2022 -0.0092 -0.0254 -0.0004 272  ARG B CB  
10934 C CG  . ARG B 274  ? 0.2507 0.1887 0.2143 -0.0058 -0.0254 -0.0020 272  ARG B CG  
10935 C CD  . ARG B 274  ? 0.2471 0.1922 0.2155 -0.0056 -0.0230 -0.0034 272  ARG B CD  
10936 N NE  . ARG B 274  ? 0.2441 0.1902 0.2147 -0.0060 -0.0218 -0.0042 272  ARG B NE  
10937 C CZ  . ARG B 274  ? 0.2408 0.1862 0.2143 -0.0036 -0.0221 -0.0055 272  ARG B CZ  
10938 N NH1 . ARG B 274  ? 0.2450 0.1886 0.2195 -0.0007 -0.0236 -0.0061 272  ARG B NH1 
10939 N NH2 . ARG B 274  ? 0.2509 0.1976 0.2260 -0.0041 -0.0209 -0.0062 272  ARG B NH2 
10940 N N   . TYR B 275  ? 0.2315 0.1706 0.1844 -0.0192 -0.0220 0.0037  273  TYR B N   
10941 C CA  . TYR B 275  ? 0.2357 0.1731 0.1857 -0.0232 -0.0218 0.0054  273  TYR B CA  
10942 C C   . TYR B 275  ? 0.2379 0.1793 0.1918 -0.0237 -0.0203 0.0042  273  TYR B C   
10943 O O   . TYR B 275  ? 0.2356 0.1841 0.1923 -0.0245 -0.0181 0.0039  273  TYR B O   
10944 C CB  . TYR B 275  ? 0.2453 0.1857 0.1924 -0.0261 -0.0207 0.0073  273  TYR B CB  
10945 C CG  . TYR B 275  ? 0.2346 0.1746 0.1793 -0.0306 -0.0202 0.0092  273  TYR B CG  
10946 C CD1 . TYR B 275  ? 0.2548 0.1873 0.1962 -0.0324 -0.0223 0.0103  273  TYR B CD1 
10947 C CD2 . TYR B 275  ? 0.2359 0.1831 0.1817 -0.0331 -0.0178 0.0100  273  TYR B CD2 
10948 C CE1 . TYR B 275  ? 0.2636 0.1956 0.2027 -0.0369 -0.0220 0.0121  273  TYR B CE1 
10949 C CE2 . TYR B 275  ? 0.2299 0.1775 0.1740 -0.0374 -0.0174 0.0118  273  TYR B CE2 
10950 C CZ  . TYR B 275  ? 0.2547 0.1946 0.1955 -0.0395 -0.0196 0.0129  273  TYR B CZ  
10951 O OH  . TYR B 275  ? 0.2678 0.2078 0.2068 -0.0442 -0.0194 0.0148  273  TYR B OH  
10952 N N   . SER B 276  ? 0.2206 0.1575 0.1747 -0.0230 -0.0215 0.0034  274  SER B N   
10953 C CA  A SER B 276  ? 0.2261 0.1662 0.1835 -0.0233 -0.0203 0.0022  274  SER B CA  
10954 C CA  B SER B 276  ? 0.2269 0.1670 0.1845 -0.0232 -0.0203 0.0021  274  SER B CA  
10955 C C   . SER B 276  ? 0.2339 0.1668 0.1891 -0.0236 -0.0222 0.0019  274  SER B C   
10956 O O   . SER B 276  ? 0.2442 0.1702 0.1965 -0.0221 -0.0243 0.0021  274  SER B O   
10957 C CB  A SER B 276  ? 0.2606 0.2058 0.2234 -0.0197 -0.0191 -0.0001 274  SER B CB  
10958 C CB  B SER B 276  ? 0.2600 0.2047 0.2228 -0.0194 -0.0192 -0.0002 274  SER B CB  
10959 O OG  A SER B 276  ? 0.2585 0.1994 0.2218 -0.0163 -0.0206 -0.0013 274  SER B OG  
10960 O OG  B SER B 276  ? 0.2679 0.2138 0.2333 -0.0191 -0.0186 -0.0015 274  SER B OG  
10961 N N   . ARG B 277  ? 0.2179 0.1524 0.1742 -0.0255 -0.0215 0.0016  275  ARG B N   
10962 C CA  . ARG B 277  ? 0.2337 0.1614 0.1877 -0.0257 -0.0232 0.0011  275  ARG B CA  
10963 C C   . ARG B 277  ? 0.2294 0.1543 0.1850 -0.0210 -0.0240 -0.0010 275  ARG B C   
10964 O O   . ARG B 277  ? 0.2462 0.1634 0.1986 -0.0201 -0.0260 -0.0012 275  ARG B O   
10965 C CB  . ARG B 277  ? 0.2326 0.1636 0.1880 -0.0283 -0.0223 0.0008  275  ARG B CB  
10966 C CG  . ARG B 277  ? 0.2485 0.1730 0.2018 -0.0284 -0.0239 -0.0002 275  ARG B CG  
10967 C CD  . ARG B 277  ? 0.2495 0.1645 0.1966 -0.0305 -0.0264 0.0012  275  ARG B CD  
10968 N NE  . ARG B 277  ? 0.2531 0.1612 0.1977 -0.0304 -0.0280 0.0001  275  ARG B NE  
10969 C CZ  . ARG B 277  ? 0.2544 0.1569 0.1981 -0.0263 -0.0292 -0.0016 275  ARG B CZ  
10970 N NH1 . ARG B 277  ? 0.2782 0.1819 0.2241 -0.0221 -0.0289 -0.0023 275  ARG B NH1 
10971 N NH2 . ARG B 277  ? 0.2720 0.1677 0.2126 -0.0265 -0.0308 -0.0025 275  ARG B NH2 
10972 N N   . ALA B 278  ? 0.2287 0.1596 0.1892 -0.0181 -0.0225 -0.0025 276  ALA B N   
10973 C CA  . ALA B 278  ? 0.2393 0.1686 0.2019 -0.0137 -0.0230 -0.0043 276  ALA B CA  
10974 C C   . ALA B 278  ? 0.2477 0.1713 0.2076 -0.0117 -0.0250 -0.0038 276  ALA B C   
10975 O O   . ALA B 278  ? 0.2683 0.1882 0.2283 -0.0084 -0.0261 -0.0050 276  ALA B O   
10976 C CB  . ALA B 278  ? 0.2476 0.1847 0.2158 -0.0114 -0.0210 -0.0056 276  ALA B CB  
10977 N N   . GLN B 279  ? 0.2319 0.1548 0.1892 -0.0134 -0.0255 -0.0020 277  GLN B N   
10978 C CA  . GLN B 279  ? 0.2409 0.1584 0.1953 -0.0117 -0.0276 -0.0013 277  GLN B CA  
10979 C C   . GLN B 279  ? 0.2446 0.1548 0.1927 -0.0149 -0.0293 0.0008  277  GLN B C   
10980 O O   . GLN B 279  ? 0.2520 0.1594 0.1971 -0.0152 -0.0306 0.0023  277  GLN B O   
10981 C CB  . GLN B 279  ? 0.2510 0.1733 0.2074 -0.0105 -0.0270 -0.0010 277  GLN B CB  
10982 C CG  . GLN B 279  ? 0.2402 0.1690 0.2025 -0.0075 -0.0255 -0.0030 277  GLN B CG  
10983 C CD  . GLN B 279  ? 0.2897 0.2158 0.2538 -0.0036 -0.0267 -0.0045 277  GLN B CD  
10984 O OE1 . GLN B 279  ? 0.3252 0.2449 0.2862 -0.0023 -0.0288 -0.0040 277  GLN B OE1 
10985 N NE2 . GLN B 279  ? 0.2517 0.1827 0.2207 -0.0016 -0.0252 -0.0062 277  GLN B NE2 
10986 N N   . ALA B 280  ? 0.2658 0.1727 0.2118 -0.0173 -0.0296 0.0009  278  ALA B N   
10987 C CA  . ALA B 280  ? 0.2761 0.1764 0.2162 -0.0211 -0.0312 0.0031  278  ALA B CA  
10988 C C   . ALA B 280  ? 0.2816 0.1732 0.2172 -0.0192 -0.0339 0.0039  278  ALA B C   
10989 O O   . ALA B 280  ? 0.2862 0.1739 0.2173 -0.0217 -0.0350 0.0061  278  ALA B O   
10990 C CB  . ALA B 280  ? 0.2939 0.1913 0.2325 -0.0237 -0.0314 0.0028  278  ALA B CB  
10991 N N   . ALA B 281  ? 0.2734 0.1620 0.2103 -0.0147 -0.0349 0.0021  279  ALA B N   
10992 C CA  . ALA B 281  ? 0.3006 0.1810 0.2334 -0.0125 -0.0376 0.0028  279  ALA B CA  
10993 C C   . ALA B 281  ? 0.2822 0.1648 0.2147 -0.0120 -0.0379 0.0042  279  ALA B C   
10994 O O   . ALA B 281  ? 0.3015 0.1777 0.2288 -0.0131 -0.0399 0.0062  279  ALA B O   
10995 C CB  . ALA B 281  ? 0.3091 0.1873 0.2439 -0.0072 -0.0384 0.0005  279  ALA B CB  
10996 N N   . ARG B 282  ? 0.2703 0.1615 0.2080 -0.0105 -0.0361 0.0032  280  ARG B N   
10997 C CA  . ARG B 282  ? 0.2634 0.1569 0.2007 -0.0101 -0.0364 0.0044  280  ARG B CA  
10998 C C   . ARG B 282  ? 0.2648 0.1589 0.1984 -0.0149 -0.0358 0.0068  280  ARG B C   
10999 O O   . ARG B 282  ? 0.2876 0.1791 0.2175 -0.0155 -0.0370 0.0086  280  ARG B O   
11000 C CB  . ARG B 282  ? 0.2951 0.1973 0.2385 -0.0076 -0.0347 0.0027  280  ARG B CB  
11001 C CG  . ARG B 282  ? 0.2967 0.1990 0.2439 -0.0028 -0.0354 0.0007  280  ARG B CG  
11002 C CD  . ARG B 282  ? 0.3194 0.2298 0.2720 -0.0009 -0.0341 -0.0004 280  ARG B CD  
11003 N NE  . ARG B 282  ? 0.3162 0.2267 0.2669 -0.0010 -0.0352 0.0009  280  ARG B NE  
11004 C CZ  . ARG B 282  ? 0.2777 0.1944 0.2313 -0.0006 -0.0342 0.0005  280  ARG B CZ  
11005 N NH1 . ARG B 282  ? 0.2957 0.2191 0.2544 -0.0002 -0.0321 -0.0011 280  ARG B NH1 
11006 N NH2 . ARG B 282  ? 0.2892 0.2051 0.2402 -0.0007 -0.0355 0.0017  280  ARG B NH2 
11007 N N   . VAL B 283  ? 0.2583 0.1561 0.1929 -0.0183 -0.0338 0.0069  281  VAL B N   
11008 C CA  . VAL B 283  ? 0.2771 0.1761 0.2084 -0.0230 -0.0330 0.0093  281  VAL B CA  
11009 C C   . VAL B 283  ? 0.2762 0.1657 0.2007 -0.0253 -0.0355 0.0116  281  VAL B C   
11010 O O   . VAL B 283  ? 0.2897 0.1776 0.2103 -0.0271 -0.0361 0.0138  281  VAL B O   
11011 C CB  . VAL B 283  ? 0.2556 0.1605 0.1898 -0.0260 -0.0307 0.0089  281  VAL B CB  
11012 C CG1 . VAL B 283  ? 0.2891 0.1944 0.2196 -0.0312 -0.0301 0.0115  281  VAL B CG1 
11013 C CG2 . VAL B 283  ? 0.2677 0.1821 0.2078 -0.0239 -0.0283 0.0071  281  VAL B CG2 
11014 N N   . MET B 284  ? 0.2842 0.1667 0.2068 -0.0252 -0.0371 0.0111  282  MET B N   
11015 C CA  . MET B 284  ? 0.2945 0.1669 0.2101 -0.0275 -0.0396 0.0133  282  MET B CA  
11016 C C   . MET B 284  ? 0.3234 0.1901 0.2360 -0.0242 -0.0420 0.0139  282  MET B C   
11017 O O   . MET B 284  ? 0.3474 0.2080 0.2541 -0.0265 -0.0436 0.0165  282  MET B O   
11018 C CB  . MET B 284  ? 0.3123 0.1782 0.2264 -0.0279 -0.0408 0.0123  282  MET B CB  
11019 C CG  . MET B 284  ? 0.3091 0.1802 0.2256 -0.0316 -0.0388 0.0119  282  MET B CG  
11020 S SD  . MET B 284  ? 0.3543 0.2287 0.2682 -0.0385 -0.0376 0.0152  282  MET B SD  
11021 C CE  . MET B 284  ? 0.4058 0.2666 0.3111 -0.0416 -0.0410 0.0176  282  MET B CE  
11022 N N   . GLY B 285  ? 0.3127 0.1814 0.2292 -0.0190 -0.0422 0.0118  283  GLY B N   
11023 C CA  . GLY B 285  ? 0.3349 0.1985 0.2490 -0.0156 -0.0447 0.0123  283  GLY B CA  
11024 C C   . GLY B 285  ? 0.3319 0.1997 0.2457 -0.0157 -0.0444 0.0136  283  GLY B C   
11025 O O   . GLY B 285  ? 0.3622 0.2244 0.2717 -0.0149 -0.0467 0.0152  283  GLY B O   
11026 N N   . GLU B 286  ? 0.2995 0.1769 0.2177 -0.0167 -0.0417 0.0129  284  GLU B N   
11027 C CA  . GLU B 286  ? 0.2798 0.1621 0.1985 -0.0161 -0.0413 0.0134  284  GLU B CA  
11028 C C   . GLU B 286  ? 0.3273 0.2142 0.2443 -0.0205 -0.0392 0.0151  284  GLU B C   
11029 O O   . GLU B 286  ? 0.3565 0.2430 0.2700 -0.0215 -0.0398 0.0169  284  GLU B O   
11030 C CB  . GLU B 286  ? 0.3120 0.2017 0.2375 -0.0123 -0.0401 0.0108  284  GLU B CB  
11031 C CG  . GLU B 286  ? 0.3301 0.2169 0.2582 -0.0077 -0.0417 0.0090  284  GLU B CG  
11032 C CD  . GLU B 286  ? 0.3580 0.2527 0.2934 -0.0047 -0.0402 0.0064  284  GLU B CD  
11033 O OE1 . GLU B 286  ? 0.3542 0.2556 0.2919 -0.0053 -0.0386 0.0062  284  GLU B OE1 
11034 O OE2 . GLU B 286  ? 0.3735 0.2675 0.3119 -0.0016 -0.0405 0.0047  284  GLU B OE2 
11035 N N   . LEU B 287  ? 0.2994 0.1911 0.2190 -0.0232 -0.0368 0.0146  285  LEU B N   
11036 C CA  . LEU B 287  ? 0.3052 0.2022 0.2237 -0.0272 -0.0346 0.0162  285  LEU B CA  
11037 C C   . LEU B 287  ? 0.3360 0.2266 0.2479 -0.0317 -0.0357 0.0193  285  LEU B C   
11038 O O   . LEU B 287  ? 0.3037 0.1951 0.2119 -0.0339 -0.0354 0.0214  285  LEU B O   
11039 C CB  . LEU B 287  ? 0.2922 0.1968 0.2159 -0.0283 -0.0318 0.0147  285  LEU B CB  
11040 C CG  . LEU B 287  ? 0.3013 0.2146 0.2264 -0.0306 -0.0289 0.0152  285  LEU B CG  
11041 C CD1 . LEU B 287  ? 0.2913 0.2115 0.2222 -0.0305 -0.0266 0.0132  285  LEU B CD1 
11042 C CD2 . LEU B 287  ? 0.3059 0.2181 0.2261 -0.0356 -0.0285 0.0182  285  LEU B CD2 
11043 N N   . LEU B 288  ? 0.3019 0.1863 0.2121 -0.0330 -0.0370 0.0195  286  LEU B N   
11044 C CA  . LEU B 288  ? 0.3083 0.1861 0.2122 -0.0376 -0.0381 0.0225  286  LEU B CA  
11045 C C   . LEU B 288  ? 0.3308 0.2025 0.2286 -0.0377 -0.0403 0.0249  286  LEU B C   
11046 O O   . LEU B 288  ? 0.3201 0.1921 0.2139 -0.0419 -0.0397 0.0276  286  LEU B O   
11047 C CB  . LEU B 288  ? 0.3568 0.2276 0.2597 -0.0384 -0.0397 0.0219  286  LEU B CB  
11048 C CG  . LEU B 288  ? 0.3796 0.2414 0.2754 -0.0428 -0.0416 0.0249  286  LEU B CG  
11049 C CD1 . LEU B 288  ? 0.3613 0.2286 0.2561 -0.0487 -0.0395 0.0273  286  LEU B CD1 
11050 C CD2 . LEU B 288  ? 0.4544 0.3086 0.3490 -0.0428 -0.0434 0.0239  286  LEU B CD2 
11051 N N   . PRO B 289  ? 0.3306 0.1970 0.2274 -0.0334 -0.0427 0.0242  287  PRO B N   
11052 C CA  . PRO B 289  ? 0.3348 0.1954 0.2254 -0.0336 -0.0448 0.0267  287  PRO B CA  
11053 C C   . PRO B 289  ? 0.3260 0.1936 0.2160 -0.0350 -0.0430 0.0279  287  PRO B C   
11054 O O   . PRO B 289  ? 0.3394 0.2033 0.2234 -0.0375 -0.0439 0.0308  287  PRO B O   
11055 C CB  . PRO B 289  ? 0.3968 0.2534 0.2885 -0.0277 -0.0473 0.0250  287  PRO B CB  
11056 C CG  . PRO B 289  ? 0.4021 0.2575 0.2978 -0.0258 -0.0473 0.0225  287  PRO B CG  
11057 C CD  . PRO B 289  ? 0.3564 0.2209 0.2569 -0.0283 -0.0439 0.0214  287  PRO B CD  
11058 N N   . ARG B 290  ? 0.3064 0.1838 0.2023 -0.0334 -0.0405 0.0257  288  ARG B N   
11059 C CA  A ARG B 290  ? 0.3202 0.2043 0.2154 -0.0347 -0.0386 0.0266  288  ARG B CA  
11060 C CA  B ARG B 290  ? 0.3201 0.2043 0.2153 -0.0347 -0.0386 0.0266  288  ARG B CA  
11061 C C   . ARG B 290  ? 0.2966 0.1836 0.1893 -0.0403 -0.0364 0.0289  288  ARG B C   
11062 O O   . ARG B 290  ? 0.3127 0.2000 0.2008 -0.0426 -0.0361 0.0313  288  ARG B O   
11063 C CB  A ARG B 290  ? 0.3284 0.2214 0.2303 -0.0314 -0.0366 0.0236  288  ARG B CB  
11064 C CB  B ARG B 290  ? 0.3282 0.2213 0.2301 -0.0315 -0.0365 0.0236  288  ARG B CB  
11065 C CG  A ARG B 290  ? 0.3574 0.2482 0.2616 -0.0262 -0.0388 0.0216  288  ARG B CG  
11066 C CG  B ARG B 290  ? 0.3643 0.2558 0.2678 -0.0264 -0.0386 0.0219  288  ARG B CG  
11067 C CD  A ARG B 290  ? 0.3709 0.2694 0.2824 -0.0232 -0.0370 0.0184  288  ARG B CD  
11068 C CD  B ARG B 290  ? 0.3663 0.2657 0.2770 -0.0234 -0.0369 0.0187  288  ARG B CD  
11069 N NE  A ARG B 290  ? 0.3581 0.2544 0.2720 -0.0186 -0.0392 0.0167  288  ARG B NE  
11070 N NE  B ARG B 290  ? 0.3531 0.2530 0.2650 -0.0195 -0.0385 0.0175  288  ARG B NE  
11071 C CZ  A ARG B 290  ? 0.3596 0.2605 0.2799 -0.0155 -0.0384 0.0140  288  ARG B CZ  
11072 C CZ  B ARG B 290  ? 0.3788 0.2845 0.2964 -0.0165 -0.0376 0.0149  288  ARG B CZ  
11073 N NH1 A ARG B 290  ? 0.2841 0.1915 0.2088 -0.0164 -0.0357 0.0126  288  ARG B NH1 
11074 N NH1 B ARG B 290  ? 0.3611 0.2727 0.2839 -0.0168 -0.0350 0.0132  288  ARG B NH1 
11075 N NH2 A ARG B 290  ? 0.3682 0.2673 0.2904 -0.0115 -0.0405 0.0128  288  ARG B NH2 
11076 N NH2 B ARG B 290  ? 0.4040 0.3097 0.3222 -0.0134 -0.0393 0.0141  288  ARG B NH2 
11077 N N   . VAL B 291  ? 0.3195 0.2088 0.2153 -0.0425 -0.0350 0.0284  289  VAL B N   
11078 C CA  . VAL B 291  ? 0.3017 0.1941 0.1955 -0.0480 -0.0331 0.0307  289  VAL B CA  
11079 C C   . VAL B 291  ? 0.3069 0.1902 0.1931 -0.0516 -0.0353 0.0342  289  VAL B C   
11080 O O   . VAL B 291  ? 0.3283 0.2133 0.2106 -0.0555 -0.0342 0.0370  289  VAL B O   
11081 C CB  . VAL B 291  ? 0.3280 0.2243 0.2265 -0.0498 -0.0315 0.0295  289  VAL B CB  
11082 C CG1 . VAL B 291  ? 0.3625 0.2637 0.2597 -0.0554 -0.0293 0.0320  289  VAL B CG1 
11083 C CG2 . VAL B 291  ? 0.3315 0.2356 0.2372 -0.0459 -0.0296 0.0261  289  VAL B CG2 
11084 N N   . LYS B 292  ? 0.3182 0.1914 0.2020 -0.0503 -0.0384 0.0341  290  LYS B N   
11085 C CA  . LYS B 292  ? 0.3314 0.1948 0.2077 -0.0535 -0.0409 0.0375  290  LYS B CA  
11086 C C   . LYS B 292  ? 0.3423 0.2046 0.2136 -0.0533 -0.0415 0.0397  290  LYS B C   
11087 O O   . LYS B 292  ? 0.3559 0.2158 0.2215 -0.0578 -0.0415 0.0431  290  LYS B O   
11088 C CB  . LYS B 292  ? 0.3710 0.2234 0.2455 -0.0509 -0.0443 0.0366  290  LYS B CB  
11089 C CG  . LYS B 292  ? 0.4108 0.2517 0.2771 -0.0544 -0.0470 0.0400  290  LYS B CG  
11090 C CD  . LYS B 292  ? 0.5249 0.3594 0.3859 -0.0521 -0.0496 0.0416  290  LYS B CD  
11091 C CE  . LYS B 292  ? 0.5130 0.3360 0.3655 -0.0561 -0.0522 0.0453  290  LYS B CE  
11092 N NZ  . LYS B 292  ? 0.5170 0.3297 0.3679 -0.0552 -0.0549 0.0445  290  LYS B NZ  
11093 N N   . ALA B 293  ? 0.3331 0.1972 0.2062 -0.0483 -0.0420 0.0378  291  ALA B N   
11094 C CA  . ALA B 293  ? 0.3474 0.2106 0.2156 -0.0478 -0.0428 0.0397  291  ALA B CA  
11095 C C   . ALA B 293  ? 0.3676 0.2392 0.2349 -0.0515 -0.0395 0.0413  291  ALA B C   
11096 O O   . ALA B 293  ? 0.3637 0.2326 0.2246 -0.0544 -0.0399 0.0444  291  ALA B O   
11097 C CB  . ALA B 293  ? 0.3639 0.2288 0.2352 -0.0419 -0.0438 0.0370  291  ALA B CB  
11098 N N   . LEU B 294  ? 0.3149 0.1966 0.1884 -0.0513 -0.0363 0.0391  292  LEU B N   
11099 C CA  . LEU B 294  ? 0.3326 0.2228 0.2056 -0.0545 -0.0330 0.0404  292  LEU B CA  
11100 C C   . LEU B 294  ? 0.3282 0.2168 0.1975 -0.0608 -0.0324 0.0438  292  LEU B C   
11101 O O   . LEU B 294  ? 0.3426 0.2334 0.2075 -0.0641 -0.0311 0.0466  292  LEU B O   
11102 C CB  . LEU B 294  ? 0.3004 0.2013 0.1810 -0.0528 -0.0299 0.0373  292  LEU B CB  
11103 C CG  . LEU B 294  ? 0.3158 0.2192 0.2002 -0.0471 -0.0303 0.0340  292  LEU B CG  
11104 C CD1 . LEU B 294  ? 0.2995 0.2124 0.1912 -0.0458 -0.0273 0.0312  292  LEU B CD1 
11105 C CD2 . LEU B 294  ? 0.3329 0.2370 0.2130 -0.0459 -0.0305 0.0349  292  LEU B CD2 
11106 N N   . ALA B 295  ? 0.3268 0.2117 0.1978 -0.0626 -0.0332 0.0436  293  ALA B N   
11107 C CA  . ALA B 295  ? 0.3408 0.2238 0.2085 -0.0688 -0.0329 0.0469  293  ALA B CA  
11108 C C   . ALA B 295  ? 0.3817 0.2550 0.2408 -0.0713 -0.0354 0.0506  293  ALA B C   
11109 O O   . ALA B 295  ? 0.3625 0.2369 0.2175 -0.0765 -0.0343 0.0540  293  ALA B O   
11110 C CB  . ALA B 295  ? 0.3620 0.2419 0.2329 -0.0699 -0.0338 0.0456  293  ALA B CB  
11111 N N   . LEU B 296  ? 0.3651 0.2290 0.2213 -0.0676 -0.0388 0.0500  294  LEU B N   
11112 C CA  . LEU B 296  ? 0.3912 0.2453 0.2389 -0.0694 -0.0415 0.0535  294  LEU B CA  
11113 C C   . LEU B 296  ? 0.3937 0.2527 0.2377 -0.0704 -0.0399 0.0556  294  LEU B C   
11114 O O   . LEU B 296  ? 0.4058 0.2613 0.2432 -0.0749 -0.0402 0.0595  294  LEU B O   
11115 C CB  . LEU B 296  ? 0.4199 0.2644 0.2662 -0.0642 -0.0453 0.0521  294  LEU B CB  
11116 C CG  . LEU B 296  ? 0.4719 0.3045 0.3094 -0.0652 -0.0487 0.0555  294  LEU B CG  
11117 C CD1 . LEU B 296  ? 0.4983 0.3244 0.3310 -0.0716 -0.0494 0.0588  294  LEU B CD1 
11118 C CD2 . LEU B 296  ? 0.5502 0.3743 0.3877 -0.0595 -0.0524 0.0535  294  LEU B CD2 
11119 N N   . LEU B 297  ? 0.3649 0.2320 0.2127 -0.0664 -0.0381 0.0530  295  LEU B N   
11120 C CA  . LEU B 297  ? 0.3754 0.2479 0.2198 -0.0673 -0.0363 0.0547  295  LEU B CA  
11121 C C   . LEU B 297  ? 0.3716 0.2520 0.2159 -0.0728 -0.0327 0.0569  295  LEU B C   
11122 O O   . LEU B 297  ? 0.3721 0.2521 0.2102 -0.0764 -0.0321 0.0603  295  LEU B O   
11123 C CB  . LEU B 297  ? 0.3595 0.2394 0.2085 -0.0619 -0.0351 0.0511  295  LEU B CB  
11124 C CG  . LEU B 297  ? 0.4363 0.3103 0.2846 -0.0565 -0.0384 0.0494  295  LEU B CG  
11125 C CD1 . LEU B 297  ? 0.4196 0.3022 0.2734 -0.0521 -0.0367 0.0458  295  LEU B CD1 
11126 C CD2 . LEU B 297  ? 0.4724 0.3394 0.3121 -0.0572 -0.0407 0.0526  295  LEU B CD2 
11127 N N   . ALA B 298  ? 0.3615 0.2493 0.2125 -0.0737 -0.0303 0.0549  296  ALA B N   
11128 C CA  . ALA B 298  ? 0.3466 0.2425 0.1983 -0.0789 -0.0269 0.0570  296  ALA B CA  
11129 C C   . ALA B 298  ? 0.3991 0.2879 0.2449 -0.0851 -0.0283 0.0613  296  ALA B C   
11130 O O   . ALA B 298  ? 0.3950 0.2878 0.2373 -0.0897 -0.0264 0.0646  296  ALA B O   
11131 C CB  . ALA B 298  ? 0.3390 0.2430 0.1990 -0.0785 -0.0247 0.0542  296  ALA B CB  
11132 N N   . LYS B 299  ? 0.3761 0.2543 0.2206 -0.0853 -0.0317 0.0614  297  LYS B N   
11133 C CA  . LYS B 299  ? 0.3996 0.2694 0.2379 -0.0911 -0.0335 0.0655  297  LYS B CA  
11134 C C   . LYS B 299  ? 0.4462 0.3108 0.2760 -0.0926 -0.0346 0.0691  297  LYS B C   
11135 O O   . LYS B 299  ? 0.4530 0.3175 0.2782 -0.0985 -0.0338 0.0731  297  LYS B O   
11136 C CB  . LYS B 299  ? 0.4497 0.3078 0.2875 -0.0900 -0.0373 0.0645  297  LYS B CB  
11137 C CG  . LYS B 299  ? 0.4837 0.3304 0.3136 -0.0953 -0.0400 0.0687  297  LYS B CG  
11138 C CD  . LYS B 299  ? 0.5902 0.4233 0.4177 -0.0924 -0.0444 0.0676  297  LYS B CD  
11139 C CE  . LYS B 299  ? 0.5907 0.4124 0.4109 -0.0981 -0.0470 0.0715  297  LYS B CE  
11140 N NZ  . LYS B 299  ? 0.6330 0.4522 0.4456 -0.1014 -0.0471 0.0760  297  LYS B NZ  
11141 N N   . ASN B 300  ? 0.4219 0.2823 0.2495 -0.0873 -0.0365 0.0678  298  ASN B N   
11142 C CA  . ASN B 300  ? 0.4397 0.2944 0.2588 -0.0883 -0.0380 0.0712  298  ASN B CA  
11143 C C   . ASN B 300  ? 0.4493 0.3141 0.2666 -0.0914 -0.0342 0.0733  298  ASN B C   
11144 O O   . ASN B 300  ? 0.4664 0.3275 0.2763 -0.0954 -0.0345 0.0775  298  ASN B O   
11145 C CB  . ASN B 300  ? 0.4645 0.3142 0.2826 -0.0817 -0.0407 0.0690  298  ASN B CB  
11146 C CG  . ASN B 300  ? 0.5085 0.3465 0.3263 -0.0790 -0.0449 0.0679  298  ASN B CG  
11147 O OD1 . ASN B 300  ? 0.5995 0.4301 0.4149 -0.0827 -0.0464 0.0698  298  ASN B OD1 
11148 N ND2 . ASN B 300  ? 0.6156 0.4518 0.4357 -0.0726 -0.0467 0.0649  298  ASN B ND2 
11149 N N   . TYR B 301  ? 0.4032 0.2805 0.2271 -0.0896 -0.0306 0.0706  299  TYR B N   
11150 C CA  . TYR B 301  ? 0.4000 0.2877 0.2227 -0.0922 -0.0266 0.0722  299  TYR B CA  
11151 C C   . TYR B 301  ? 0.3645 0.2589 0.1897 -0.0983 -0.0238 0.0742  299  TYR B C   
11152 O O   . TYR B 301  ? 0.4258 0.3292 0.2500 -0.1010 -0.0203 0.0760  299  TYR B O   
11153 C CB  . TYR B 301  ? 0.3763 0.2741 0.2043 -0.0870 -0.0240 0.0682  299  TYR B CB  
11154 C CG  . TYR B 301  ? 0.3888 0.2825 0.2136 -0.0817 -0.0261 0.0667  299  TYR B CG  
11155 C CD1 . TYR B 301  ? 0.3891 0.2812 0.2061 -0.0826 -0.0262 0.0695  299  TYR B CD1 
11156 C CD2 . TYR B 301  ? 0.3973 0.2893 0.2270 -0.0759 -0.0279 0.0627  299  TYR B CD2 
11157 C CE1 . TYR B 301  ? 0.3864 0.2749 0.2004 -0.0779 -0.0283 0.0681  299  TYR B CE1 
11158 C CE2 . TYR B 301  ? 0.4004 0.2891 0.2275 -0.0712 -0.0300 0.0613  299  TYR B CE2 
11159 C CZ  . TYR B 301  ? 0.3957 0.2827 0.2151 -0.0722 -0.0302 0.0640  299  TYR B CZ  
11160 O OH  . TYR B 301  ? 0.4187 0.3026 0.2354 -0.0677 -0.0325 0.0627  299  TYR B OH  
11161 N N   . ASP B 302  ? 0.3747 0.2651 0.2030 -0.1003 -0.0253 0.0739  300  ASP B N   
11162 C CA  . ASP B 302  ? 0.4085 0.3054 0.2404 -0.1058 -0.0230 0.0753  300  ASP B CA  
11163 C C   . ASP B 302  ? 0.3655 0.2779 0.2043 -0.1045 -0.0184 0.0730  300  ASP B C   
11164 O O   . ASP B 302  ? 0.3959 0.3172 0.2346 -0.1087 -0.0152 0.0754  300  ASP B O   
11165 C CB  . ASP B 302  ? 0.4102 0.3036 0.2353 -0.1132 -0.0231 0.0807  300  ASP B CB  
11166 C CG  . ASP B 302  ? 0.4413 0.3373 0.2698 -0.1190 -0.0224 0.0820  300  ASP B CG  
11167 O OD1 . ASP B 302  ? 0.4597 0.3551 0.2941 -0.1172 -0.0234 0.0789  300  ASP B OD1 
11168 O OD2 . ASP B 302  ? 0.5168 0.4160 0.3424 -0.1254 -0.0209 0.0861  300  ASP B OD2 
11169 N N   . ILE B 303  ? 0.3434 0.2587 0.1882 -0.0985 -0.0182 0.0684  301  ILE B N   
11170 C CA  . ILE B 303  ? 0.3344 0.2632 0.1865 -0.0966 -0.0144 0.0658  301  ILE B CA  
11171 C C   . ILE B 303  ? 0.3635 0.2929 0.2228 -0.0957 -0.0150 0.0629  301  ILE B C   
11172 O O   . ILE B 303  ? 0.3451 0.2646 0.2040 -0.0948 -0.0184 0.0621  301  ILE B O   
11173 C CB  . ILE B 303  ? 0.3400 0.2732 0.1929 -0.0904 -0.0132 0.0627  301  ILE B CB  
11174 C CG1 . ILE B 303  ? 0.3537 0.2798 0.2091 -0.0847 -0.0162 0.0590  301  ILE B CG1 
11175 C CG2 . ILE B 303  ? 0.3450 0.2762 0.1900 -0.0911 -0.0130 0.0654  301  ILE B CG2 
11176 C CD1 . ILE B 303  ? 0.3787 0.3097 0.2362 -0.0787 -0.0151 0.0556  301  ILE B CD1 
11177 N N   . GLY B 304  ? 0.3234 0.2648 0.1894 -0.0955 -0.0117 0.0613  302  GLY B N   
11178 C CA  . GLY B 304  ? 0.3127 0.2558 0.1858 -0.0940 -0.0120 0.0583  302  GLY B CA  
11179 C C   . GLY B 304  ? 0.3142 0.2564 0.1910 -0.0869 -0.0127 0.0538  302  GLY B C   
11180 O O   . GLY B 304  ? 0.3236 0.2695 0.2000 -0.0831 -0.0114 0.0524  302  GLY B O   
11181 N N   . LEU B 305  ? 0.2838 0.2208 0.1640 -0.0851 -0.0149 0.0516  303  LEU B N   
11182 C CA  . LEU B 305  ? 0.3112 0.2482 0.1959 -0.0788 -0.0155 0.0473  303  LEU B CA  
11183 C C   . LEU B 305  ? 0.3103 0.2517 0.2019 -0.0789 -0.0147 0.0452  303  LEU B C   
11184 O O   . LEU B 305  ? 0.3187 0.2540 0.2101 -0.0814 -0.0168 0.0458  303  LEU B O   
11185 C CB  . LEU B 305  ? 0.3197 0.2445 0.2009 -0.0758 -0.0194 0.0466  303  LEU B CB  
11186 C CG  . LEU B 305  ? 0.3279 0.2528 0.2138 -0.0694 -0.0200 0.0424  303  LEU B CG  
11187 C CD1 . LEU B 305  ? 0.3671 0.2848 0.2488 -0.0657 -0.0225 0.0421  303  LEU B CD1 
11188 C CD2 . LEU B 305  ? 0.3751 0.2964 0.2652 -0.0686 -0.0216 0.0404  303  LEU B CD2 
11189 N N   . ASN B 306  ? 0.2737 0.2253 0.1712 -0.0762 -0.0119 0.0428  304  ASN B N   
11190 C CA  . ASN B 306  ? 0.2686 0.2261 0.1727 -0.0764 -0.0107 0.0410  304  ASN B CA  
11191 C C   . ASN B 306  ? 0.2552 0.2118 0.1640 -0.0706 -0.0115 0.0369  304  ASN B C   
11192 O O   . ASN B 306  ? 0.2765 0.2345 0.1856 -0.0661 -0.0109 0.0351  304  ASN B O   
11193 C CB  . ASN B 306  ? 0.2867 0.2574 0.1943 -0.0776 -0.0068 0.0414  304  ASN B CB  
11194 C CG  . ASN B 306  ? 0.2791 0.2566 0.1939 -0.0770 -0.0056 0.0393  304  ASN B CG  
11195 O OD1 . ASN B 306  ? 0.3018 0.2796 0.2179 -0.0811 -0.0060 0.0406  304  ASN B OD1 
11196 N ND2 . ASN B 306  ? 0.2781 0.2606 0.1974 -0.0719 -0.0042 0.0360  304  ASN B ND2 
11197 N N   . ILE B 307  ? 0.2694 0.2235 0.1815 -0.0707 -0.0128 0.0356  305  ILE B N   
11198 C CA  . ILE B 307  ? 0.2560 0.2101 0.1730 -0.0656 -0.0132 0.0319  305  ILE B CA  
11199 C C   . ILE B 307  ? 0.2644 0.2297 0.1879 -0.0651 -0.0103 0.0304  305  ILE B C   
11200 O O   . ILE B 307  ? 0.2515 0.2198 0.1773 -0.0685 -0.0099 0.0311  305  ILE B O   
11201 C CB  . ILE B 307  ? 0.2802 0.2250 0.1969 -0.0655 -0.0163 0.0311  305  ILE B CB  
11202 C CG1 . ILE B 307  ? 0.3004 0.2339 0.2107 -0.0653 -0.0193 0.0325  305  ILE B CG1 
11203 C CG2 . ILE B 307  ? 0.2950 0.2412 0.2173 -0.0605 -0.0163 0.0273  305  ILE B CG2 
11204 C CD1 . ILE B 307  ? 0.3440 0.2678 0.2533 -0.0651 -0.0224 0.0318  305  ILE B CD1 
11205 N N   . ASP B 308  ? 0.2577 0.2290 0.1839 -0.0610 -0.0084 0.0283  306  ASP B N   
11206 C CA  . ASP B 308  ? 0.2485 0.2299 0.1808 -0.0598 -0.0057 0.0266  306  ASP B CA  
11207 C C   . ASP B 308  ? 0.2519 0.2317 0.1887 -0.0582 -0.0068 0.0244  306  ASP B C   
11208 O O   . ASP B 308  ? 0.2541 0.2259 0.1901 -0.0561 -0.0093 0.0231  306  ASP B O   
11209 C CB  . ASP B 308  ? 0.2427 0.2290 0.1763 -0.0551 -0.0039 0.0246  306  ASP B CB  
11210 C CG  . ASP B 308  ? 0.2586 0.2485 0.1881 -0.0564 -0.0021 0.0265  306  ASP B CG  
11211 O OD1 . ASP B 308  ? 0.2687 0.2597 0.1954 -0.0610 -0.0016 0.0296  306  ASP B OD1 
11212 O OD2 . ASP B 308  ? 0.2524 0.2441 0.1815 -0.0527 -0.0012 0.0249  306  ASP B OD2 
11213 N N   . ALA B 309  ? 0.2254 0.2132 0.1671 -0.0591 -0.0050 0.0239  307  ALA B N   
11214 C CA  . ALA B 309  ? 0.2115 0.1987 0.1575 -0.0578 -0.0059 0.0218  307  ALA B CA  
11215 C C   . ALA B 309  ? 0.2059 0.1979 0.1564 -0.0526 -0.0044 0.0188  307  ALA B C   
11216 O O   . ALA B 309  ? 0.2248 0.2245 0.1769 -0.0513 -0.0019 0.0186  307  ALA B O   
11217 C CB  . ALA B 309  ? 0.2345 0.2272 0.1829 -0.0620 -0.0051 0.0231  307  ALA B CB  
11218 N N   . GLU B 310  ? 0.2150 0.2023 0.1674 -0.0496 -0.0060 0.0166  308  GLU B N   
11219 C CA  . GLU B 310  ? 0.1993 0.1898 0.1556 -0.0447 -0.0050 0.0138  308  GLU B CA  
11220 C C   . GLU B 310  ? 0.1944 0.1878 0.1556 -0.0438 -0.0047 0.0122  308  GLU B C   
11221 O O   . GLU B 310  ? 0.1986 0.1971 0.1616 -0.0467 -0.0038 0.0132  308  GLU B O   
11222 C CB  . GLU B 310  ? 0.1992 0.1823 0.1533 -0.0414 -0.0068 0.0126  308  GLU B CB  
11223 C CG  . GLU B 310  ? 0.2286 0.2096 0.1777 -0.0421 -0.0069 0.0142  308  GLU B CG  
11224 C CD  . GLU B 310  ? 0.2322 0.2067 0.1793 -0.0388 -0.0088 0.0131  308  GLU B CD  
11225 O OE1 . GLU B 310  ? 0.2537 0.2312 0.2031 -0.0352 -0.0079 0.0111  308  GLU B OE1 
11226 O OE2 . GLU B 310  ? 0.2440 0.2107 0.1874 -0.0397 -0.0112 0.0142  308  GLU B OE2 
11227 N N   . GLU B 311  ? 0.1943 0.1848 0.1578 -0.0401 -0.0055 0.0098  309  GLU B N   
11228 C CA  . GLU B 311  ? 0.1800 0.1737 0.1481 -0.0390 -0.0051 0.0082  309  GLU B CA  
11229 C C   . GLU B 311  ? 0.2126 0.2024 0.1798 -0.0422 -0.0068 0.0090  309  GLU B C   
11230 O O   . GLU B 311  ? 0.2077 0.1902 0.1707 -0.0443 -0.0088 0.0102  309  GLU B O   
11231 C CB  . GLU B 311  ? 0.1929 0.1839 0.1631 -0.0344 -0.0057 0.0057  309  GLU B CB  
11232 C CG  . GLU B 311  ? 0.2401 0.2352 0.2117 -0.0311 -0.0041 0.0045  309  GLU B CG  
11233 C CD  . GLU B 311  ? 0.2610 0.2513 0.2289 -0.0300 -0.0051 0.0048  309  GLU B CD  
11234 O OE1 . GLU B 311  ? 0.2392 0.2240 0.2030 -0.0323 -0.0067 0.0064  309  GLU B OE1 
11235 O OE2 . GLU B 311  ? 0.3267 0.3184 0.2957 -0.0268 -0.0045 0.0034  309  GLU B OE2 
11236 N N   . ALA B 312  ? 0.1901 0.1846 0.1611 -0.0426 -0.0062 0.0083  310  ALA B N   
11237 C CA  . ALA B 312  ? 0.1922 0.1836 0.1623 -0.0459 -0.0077 0.0090  310  ALA B CA  
11238 C C   . ALA B 312  ? 0.2095 0.1910 0.1771 -0.0446 -0.0102 0.0079  310  ALA B C   
11239 O O   . ALA B 312  ? 0.2114 0.1871 0.1758 -0.0477 -0.0121 0.0090  310  ALA B O   
11240 C CB  . ALA B 312  ? 0.1922 0.1904 0.1670 -0.0458 -0.0067 0.0081  310  ALA B CB  
11241 N N   . ASP B 313  ? 0.2007 0.1801 0.1697 -0.0401 -0.0103 0.0059  311  ASP B N   
11242 C CA  . ASP B 313  ? 0.2147 0.1853 0.1817 -0.0385 -0.0125 0.0048  311  ASP B CA  
11243 C C   . ASP B 313  ? 0.2340 0.1971 0.1961 -0.0389 -0.0142 0.0059  311  ASP B C   
11244 O O   . ASP B 313  ? 0.2333 0.1890 0.1936 -0.0372 -0.0160 0.0051  311  ASP B O   
11245 C CB  . ASP B 313  ? 0.2267 0.1981 0.1973 -0.0337 -0.0121 0.0023  311  ASP B CB  
11246 C CG  . ASP B 313  ? 0.2456 0.2193 0.2174 -0.0305 -0.0110 0.0016  311  ASP B CG  
11247 O OD1 . ASP B 313  ? 0.2414 0.2155 0.2110 -0.0315 -0.0107 0.0030  311  ASP B OD1 
11248 O OD2 . ASP B 313  ? 0.2756 0.2506 0.2506 -0.0270 -0.0106 -0.0002 311  ASP B OD2 
11249 N N   . ARG B 314  ? 0.2072 0.1720 0.1671 -0.0411 -0.0136 0.0079  312  ARG B N   
11250 C CA  . ARG B 314  ? 0.2261 0.1838 0.1808 -0.0421 -0.0152 0.0094  312  ARG B CA  
11251 C C   . ARG B 314  ? 0.2259 0.1810 0.1767 -0.0474 -0.0161 0.0120  312  ARG B C   
11252 O O   . ARG B 314  ? 0.2497 0.1977 0.1957 -0.0486 -0.0178 0.0135  312  ARG B O   
11253 C CB  . ARG B 314  ? 0.2069 0.1676 0.1612 -0.0405 -0.0141 0.0098  312  ARG B CB  
11254 C CG  . ARG B 314  ? 0.2156 0.1754 0.1721 -0.0355 -0.0143 0.0075  312  ARG B CG  
11255 C CD  . ARG B 314  ? 0.2145 0.1797 0.1720 -0.0336 -0.0126 0.0073  312  ARG B CD  
11256 N NE  . ARG B 314  ? 0.2189 0.1812 0.1771 -0.0295 -0.0135 0.0056  312  ARG B NE  
11257 C CZ  . ARG B 314  ? 0.2119 0.1775 0.1710 -0.0272 -0.0126 0.0049  312  ARG B CZ  
11258 N NH1 . ARG B 314  ? 0.2294 0.2015 0.1890 -0.0281 -0.0105 0.0054  312  ARG B NH1 
11259 N NH2 . ARG B 314  ? 0.2523 0.2146 0.2117 -0.0240 -0.0139 0.0037  312  ARG B NH2 
11260 N N   . LEU B 315  ? 0.2202 0.1808 0.1730 -0.0506 -0.0151 0.0127  313  LEU B N   
11261 C CA  . LEU B 315  ? 0.2328 0.1921 0.1823 -0.0561 -0.0158 0.0153  313  LEU B CA  
11262 C C   . LEU B 315  ? 0.2498 0.1977 0.1945 -0.0576 -0.0188 0.0158  313  LEU B C   
11263 O O   . LEU B 315  ? 0.2515 0.1937 0.1912 -0.0601 -0.0201 0.0179  313  LEU B O   
11264 C CB  . LEU B 315  ? 0.2247 0.1921 0.1780 -0.0589 -0.0144 0.0156  313  LEU B CB  
11265 C CG  . LEU B 315  ? 0.2468 0.2173 0.1985 -0.0648 -0.0141 0.0186  313  LEU B CG  
11266 C CD1 . LEU B 315  ? 0.2455 0.2251 0.2020 -0.0666 -0.0127 0.0184  313  LEU B CD1 
11267 C CD2 . LEU B 315  ? 0.2814 0.2419 0.2275 -0.0688 -0.0169 0.0202  313  LEU B CD2 
11268 N N   . GLU B 316  ? 0.2481 0.1926 0.1940 -0.0561 -0.0200 0.0138  314  GLU B N   
11269 C CA  . GLU B 316  ? 0.2512 0.1849 0.1923 -0.0579 -0.0229 0.0141  314  GLU B CA  
11270 C C   . GLU B 316  ? 0.2577 0.1827 0.1950 -0.0548 -0.0246 0.0139  314  GLU B C   
11271 O O   . GLU B 316  ? 0.2753 0.1916 0.2071 -0.0571 -0.0268 0.0155  314  GLU B O   
11272 C CB  . GLU B 316  ? 0.2567 0.1892 0.1997 -0.0570 -0.0237 0.0120  314  GLU B CB  
11273 C CG  . GLU B 316  ? 0.2369 0.1766 0.1824 -0.0612 -0.0227 0.0128  314  GLU B CG  
11274 C CD  . GLU B 316  ? 0.2842 0.2226 0.2311 -0.0608 -0.0236 0.0108  314  GLU B CD  
11275 O OE1 . GLU B 316  ? 0.2900 0.2188 0.2332 -0.0603 -0.0260 0.0099  314  GLU B OE1 
11276 O OE2 . GLU B 316  ? 0.2929 0.2400 0.2445 -0.0610 -0.0220 0.0102  314  GLU B OE2 
11277 N N   . LEU B 317  ? 0.2600 0.1872 0.2001 -0.0497 -0.0237 0.0121  315  LEU B N   
11278 C CA  . LEU B 317  ? 0.2649 0.1854 0.2019 -0.0468 -0.0252 0.0121  315  LEU B CA  
11279 C C   . LEU B 317  ? 0.2706 0.1890 0.2030 -0.0499 -0.0256 0.0151  315  LEU B C   
11280 O O   . LEU B 317  ? 0.2904 0.1997 0.2177 -0.0503 -0.0280 0.0162  315  LEU B O   
11281 C CB  . LEU B 317  ? 0.2848 0.2101 0.2261 -0.0416 -0.0239 0.0101  315  LEU B CB  
11282 C CG  . LEU B 317  ? 0.2934 0.2129 0.2324 -0.0383 -0.0254 0.0099  315  LEU B CG  
11283 C CD1 . LEU B 317  ? 0.3319 0.2410 0.2672 -0.0372 -0.0282 0.0094  315  LEU B CD1 
11284 C CD2 . LEU B 317  ? 0.3037 0.2285 0.2474 -0.0336 -0.0241 0.0077  315  LEU B CD2 
11285 N N   . SER B 318  ? 0.2492 0.1760 0.1833 -0.0522 -0.0234 0.0165  316  SER B N   
11286 C CA  . SER B 318  ? 0.2583 0.1838 0.1880 -0.0551 -0.0235 0.0193  316  SER B CA  
11287 C C   . SER B 318  ? 0.2606 0.1788 0.1850 -0.0602 -0.0255 0.0218  316  SER B C   
11288 O O   . SER B 318  ? 0.2759 0.1885 0.1950 -0.0619 -0.0268 0.0240  316  SER B O   
11289 C CB  . SER B 318  ? 0.2553 0.1917 0.1877 -0.0565 -0.0204 0.0202  316  SER B CB  
11290 O OG  . SER B 318  ? 0.2588 0.2005 0.1929 -0.0607 -0.0193 0.0212  316  SER B OG  
11291 N N   . LEU B 319  ? 0.2665 0.1844 0.1920 -0.0628 -0.0260 0.0214  317  LEU B N   
11292 C CA  . LEU B 319  ? 0.2693 0.1798 0.1897 -0.0679 -0.0281 0.0236  317  LEU B CA  
11293 C C   . LEU B 319  ? 0.3005 0.1979 0.2155 -0.0660 -0.0313 0.0234  317  LEU B C   
11294 O O   . LEU B 319  ? 0.3030 0.1927 0.2122 -0.0697 -0.0332 0.0259  317  LEU B O   
11295 C CB  . LEU B 319  ? 0.2833 0.1961 0.2061 -0.0706 -0.0282 0.0229  317  LEU B CB  
11296 C CG  . LEU B 319  ? 0.2792 0.2047 0.2070 -0.0731 -0.0253 0.0235  317  LEU B CG  
11297 C CD1 . LEU B 319  ? 0.2861 0.2129 0.2163 -0.0751 -0.0258 0.0224  317  LEU B CD1 
11298 C CD2 . LEU B 319  ? 0.3216 0.2504 0.2471 -0.0782 -0.0244 0.0270  317  LEU B CD2 
11299 N N   . ASP B 320  ? 0.3045 0.1993 0.2213 -0.0604 -0.0319 0.0206  318  ASP B N   
11300 C CA  . ASP B 320  ? 0.3442 0.2270 0.2561 -0.0580 -0.0349 0.0203  318  ASP B CA  
11301 C C   . ASP B 320  ? 0.3048 0.1843 0.2127 -0.0577 -0.0356 0.0224  318  ASP B C   
11302 O O   . ASP B 320  ? 0.3531 0.2221 0.2551 -0.0584 -0.0383 0.0237  318  ASP B O   
11303 C CB  . ASP B 320  ? 0.3276 0.2098 0.2429 -0.0520 -0.0350 0.0169  318  ASP B CB  
11304 C CG  . ASP B 320  ? 0.3272 0.2084 0.2440 -0.0525 -0.0354 0.0150  318  ASP B CG  
11305 O OD1 . ASP B 320  ? 0.3585 0.2315 0.2707 -0.0556 -0.0376 0.0159  318  ASP B OD1 
11306 O OD2 . ASP B 320  ? 0.3544 0.2429 0.2768 -0.0500 -0.0336 0.0128  318  ASP B OD2 
11307 N N   . LEU B 321  ? 0.2897 0.1777 0.2004 -0.0567 -0.0333 0.0228  319  LEU B N   
11308 C CA  . LEU B 321  ? 0.3116 0.1970 0.2181 -0.0569 -0.0339 0.0250  319  LEU B CA  
11309 C C   . LEU B 321  ? 0.3060 0.1899 0.2078 -0.0633 -0.0340 0.0286  319  LEU B C   
11310 O O   . LEU B 321  ? 0.3476 0.2231 0.2432 -0.0647 -0.0362 0.0308  319  LEU B O   
11311 C CB  . LEU B 321  ? 0.3318 0.2263 0.2421 -0.0539 -0.0315 0.0241  319  LEU B CB  
11312 C CG  . LEU B 321  ? 0.3136 0.2077 0.2272 -0.0476 -0.0320 0.0212  319  LEU B CG  
11313 C CD1 . LEU B 321  ? 0.3379 0.2382 0.2579 -0.0455 -0.0304 0.0183  319  LEU B CD1 
11314 C CD2 . LEU B 321  ? 0.3460 0.2444 0.2600 -0.0452 -0.0310 0.0213  319  LEU B CD2 
11315 N N   . LEU B 322  ? 0.3127 0.2047 0.2173 -0.0673 -0.0319 0.0293  320  LEU B N   
11316 C CA  . LEU B 322  ? 0.3212 0.2128 0.2219 -0.0737 -0.0318 0.0329  320  LEU B CA  
11317 C C   . LEU B 322  ? 0.3200 0.1991 0.2147 -0.0767 -0.0352 0.0343  320  LEU B C   
11318 O O   . LEU B 322  ? 0.3477 0.2211 0.2365 -0.0804 -0.0365 0.0375  320  LEU B O   
11319 C CB  . LEU B 322  ? 0.3030 0.2055 0.2086 -0.0772 -0.0292 0.0331  320  LEU B CB  
11320 C CG  . LEU B 322  ? 0.3355 0.2394 0.2379 -0.0842 -0.0289 0.0369  320  LEU B CG  
11321 C CD1 . LEU B 322  ? 0.3296 0.2360 0.2290 -0.0848 -0.0276 0.0393  320  LEU B CD1 
11322 C CD2 . LEU B 322  ? 0.3176 0.2324 0.2255 -0.0872 -0.0266 0.0367  320  LEU B CD2 
11323 N N   . GLU B 323  ? 0.3417 0.2162 0.2376 -0.0752 -0.0367 0.0320  321  GLU B N   
11324 C CA  . GLU B 323  ? 0.3264 0.1880 0.2164 -0.0774 -0.0401 0.0327  321  GLU B CA  
11325 C C   . GLU B 323  ? 0.3439 0.1948 0.2277 -0.0753 -0.0426 0.0339  321  GLU B C   
11326 O O   . GLU B 323  ? 0.3948 0.2373 0.2722 -0.0795 -0.0447 0.0368  321  GLU B O   
11327 C CB  . GLU B 323  ? 0.3952 0.2540 0.2877 -0.0745 -0.0411 0.0293  321  GLU B CB  
11328 C CG  . GLU B 323  ? 0.4426 0.2872 0.3288 -0.0756 -0.0447 0.0294  321  GLU B CG  
11329 C CD  . GLU B 323  ? 0.4654 0.3084 0.3499 -0.0822 -0.0455 0.0308  321  GLU B CD  
11330 O OE1 . GLU B 323  ? 0.4156 0.2694 0.3048 -0.0853 -0.0432 0.0311  321  GLU B OE1 
11331 O OE2 . GLU B 323  ? 0.4610 0.2919 0.3392 -0.0845 -0.0486 0.0317  321  GLU B OE2 
11332 N N   . VAL B 324  ? 0.3422 0.1931 0.2278 -0.0690 -0.0426 0.0318  322  VAL B N   
11333 C CA  . VAL B 324  ? 0.3850 0.2261 0.2652 -0.0664 -0.0451 0.0328  322  VAL B CA  
11334 C C   . VAL B 324  ? 0.3532 0.1950 0.2292 -0.0699 -0.0448 0.0365  322  VAL B C   
11335 O O   . VAL B 324  ? 0.3972 0.2288 0.2663 -0.0719 -0.0473 0.0390  322  VAL B O   
11336 C CB  . VAL B 324  ? 0.3859 0.2287 0.2698 -0.0589 -0.0450 0.0298  322  VAL B CB  
11337 C CG1 . VAL B 324  ? 0.3874 0.2217 0.2660 -0.0563 -0.0475 0.0311  322  VAL B CG1 
11338 C CG2 . VAL B 324  ? 0.4180 0.2581 0.3046 -0.0555 -0.0458 0.0264  322  VAL B CG2 
11339 N N   . LEU B 325  ? 0.3449 0.1985 0.2248 -0.0708 -0.0416 0.0370  323  LEU B N   
11340 C CA  . LEU B 325  ? 0.3768 0.2318 0.2528 -0.0737 -0.0410 0.0404  323  LEU B CA  
11341 C C   . LEU B 325  ? 0.3388 0.1892 0.2095 -0.0810 -0.0418 0.0440  323  LEU B C   
11342 O O   . LEU B 325  ? 0.3608 0.2049 0.2251 -0.0832 -0.0433 0.0471  323  LEU B O   
11343 C CB  . LEU B 325  ? 0.3511 0.2200 0.2324 -0.0731 -0.0372 0.0398  323  LEU B CB  
11344 C CG  . LEU B 325  ? 0.3675 0.2404 0.2531 -0.0663 -0.0365 0.0366  323  LEU B CG  
11345 C CD1 . LEU B 325  ? 0.3773 0.2636 0.2686 -0.0659 -0.0328 0.0356  323  LEU B CD1 
11346 C CD2 . LEU B 325  ? 0.3659 0.2324 0.2467 -0.0636 -0.0384 0.0377  323  LEU B CD2 
11347 N N   . CYS B 326  ? 0.3701 0.2235 0.2433 -0.0849 -0.0411 0.0438  324  CYS B N   
11348 C CA  . CYS B 326  ? 0.3580 0.2077 0.2266 -0.0923 -0.0420 0.0474  324  CYS B CA  
11349 C C   . CYS B 326  ? 0.3938 0.2275 0.2551 -0.0933 -0.0461 0.0484  324  CYS B C   
11350 O O   . CYS B 326  ? 0.3934 0.2216 0.2491 -0.0991 -0.0474 0.0520  324  CYS B O   
11351 C CB  . CYS B 326  ? 0.3539 0.2117 0.2274 -0.0963 -0.0403 0.0469  324  CYS B CB  
11352 S SG  . CYS B 326  ? 0.3974 0.2738 0.2781 -0.0965 -0.0354 0.0468  324  CYS B SG  
11353 N N   . LEU B 327  ? 0.3892 0.2156 0.2506 -0.0878 -0.0483 0.0454  325  LEU B N   
11354 C CA  . LEU B 327  ? 0.4236 0.2343 0.2780 -0.0878 -0.0523 0.0460  325  LEU B CA  
11355 C C   . LEU B 327  ? 0.4569 0.2600 0.3065 -0.0838 -0.0542 0.0469  325  LEU B C   
11356 O O   . LEU B 327  ? 0.4704 0.2599 0.3137 -0.0833 -0.0577 0.0476  325  LEU B O   
11357 C CB  . LEU B 327  ? 0.4103 0.2168 0.2670 -0.0841 -0.0536 0.0422  325  LEU B CB  
11358 C CG  . LEU B 327  ? 0.4546 0.2660 0.3147 -0.0885 -0.0526 0.0414  325  LEU B CG  
11359 C CD1 . LEU B 327  ? 0.5251 0.3334 0.3878 -0.0841 -0.0535 0.0373  325  LEU B CD1 
11360 C CD2 . LEU B 327  ? 0.5432 0.3470 0.3971 -0.0961 -0.0546 0.0448  325  LEU B CD2 
11361 N N   . ASP B 328  ? 0.4296 0.2408 0.2817 -0.0811 -0.0521 0.0471  326  ASP B N   
11362 C CA  . ASP B 328  ? 0.4558 0.2609 0.3039 -0.0769 -0.0539 0.0477  326  ASP B CA  
11363 C C   . ASP B 328  ? 0.4293 0.2286 0.2698 -0.0820 -0.0551 0.0524  326  ASP B C   
11364 O O   . ASP B 328  ? 0.4461 0.2537 0.2870 -0.0857 -0.0526 0.0547  326  ASP B O   
11365 C CB  . ASP B 328  ? 0.4237 0.2401 0.2777 -0.0722 -0.0513 0.0458  326  ASP B CB  
11366 C CG  . ASP B 328  ? 0.5100 0.3210 0.3610 -0.0671 -0.0533 0.0458  326  ASP B CG  
11367 O OD1 . ASP B 328  ? 0.4776 0.2778 0.3212 -0.0684 -0.0561 0.0485  326  ASP B OD1 
11368 O OD2 . ASP B 328  ? 0.5192 0.3366 0.3752 -0.0618 -0.0522 0.0432  326  ASP B OD2 
11369 N N   . GLY B 329  ? 0.4824 0.2672 0.3157 -0.0821 -0.0589 0.0538  327  GLY B N   
11370 C CA  . GLY B 329  ? 0.4907 0.2683 0.3158 -0.0870 -0.0604 0.0585  327  GLY B CA  
11371 C C   . GLY B 329  ? 0.4833 0.2656 0.3070 -0.0857 -0.0593 0.0604  327  GLY B C   
11372 O O   . GLY B 329  ? 0.4836 0.2643 0.3018 -0.0908 -0.0593 0.0645  327  GLY B O   
11373 N N   . ASP B 330  ? 0.4748 0.2629 0.3030 -0.0792 -0.0584 0.0576  328  ASP B N   
11374 C CA  . ASP B 330  ? 0.4583 0.2519 0.2854 -0.0780 -0.0572 0.0591  328  ASP B CA  
11375 C C   . ASP B 330  ? 0.5109 0.3168 0.3404 -0.0830 -0.0532 0.0607  328  ASP B C   
11376 O O   . ASP B 330  ? 0.5203 0.3290 0.3465 -0.0843 -0.0523 0.0633  328  ASP B O   
11377 C CB  . ASP B 330  ? 0.4859 0.2845 0.3183 -0.0704 -0.0568 0.0554  328  ASP B CB  
11378 C CG  . ASP B 330  ? 0.5473 0.3344 0.3768 -0.0650 -0.0608 0.0543  328  ASP B CG  
11379 O OD1 . ASP B 330  ? 0.5728 0.3476 0.3948 -0.0669 -0.0639 0.0569  328  ASP B OD1 
11380 O OD2 . ASP B 330  ? 0.5363 0.3267 0.3708 -0.0588 -0.0608 0.0509  328  ASP B OD2 
11381 N N   . LEU B 331  ? 0.4405 0.2539 0.2754 -0.0857 -0.0509 0.0594  329  LEU B N   
11382 C CA  . LEU B 331  ? 0.4571 0.2827 0.2948 -0.0903 -0.0471 0.0609  329  LEU B CA  
11383 C C   . LEU B 331  ? 0.4023 0.2250 0.2359 -0.0984 -0.0473 0.0647  329  LEU B C   
11384 O O   . LEU B 331  ? 0.4462 0.2793 0.2832 -0.1026 -0.0442 0.0656  329  LEU B O   
11385 C CB  . LEU B 331  ? 0.4160 0.2535 0.2631 -0.0879 -0.0441 0.0571  329  LEU B CB  
11386 C CG  . LEU B 331  ? 0.3923 0.2332 0.2438 -0.0803 -0.0439 0.0534  329  LEU B CG  
11387 C CD1 . LEU B 331  ? 0.3936 0.2450 0.2538 -0.0782 -0.0412 0.0497  329  LEU B CD1 
11388 C CD2 . LEU B 331  ? 0.3912 0.2367 0.2406 -0.0789 -0.0427 0.0547  329  LEU B CD2 
11389 N N   . SER B 332  ? 0.4649 0.2735 0.2912 -0.1004 -0.0510 0.0669  330  SER B N   
11390 C CA  . SER B 332  ? 0.4854 0.2890 0.3072 -0.1082 -0.0519 0.0705  330  SER B CA  
11391 C C   . SER B 332  ? 0.4864 0.3006 0.3083 -0.1137 -0.0486 0.0737  330  SER B C   
11392 O O   . SER B 332  ? 0.5103 0.3266 0.3290 -0.1132 -0.0477 0.0757  330  SER B O   
11393 C CB  . SER B 332  ? 0.5642 0.3547 0.3795 -0.1071 -0.0558 0.0712  330  SER B CB  
11394 O OG  . SER B 332  ? 0.6010 0.3896 0.4143 -0.1128 -0.0565 0.0729  330  SER B OG  
11395 N N   . GLY B 333  ? 0.4628 0.2840 0.2884 -0.1189 -0.0469 0.0741  331  GLY B N   
11396 C CA  . GLY B 333  ? 0.5131 0.3445 0.3393 -0.1244 -0.0440 0.0770  331  GLY B CA  
11397 C C   . GLY B 333  ? 0.4885 0.3334 0.3185 -0.1240 -0.0397 0.0774  331  GLY B C   
11398 O O   . GLY B 333  ? 0.5338 0.3882 0.3644 -0.1280 -0.0369 0.0797  331  GLY B O   
11399 N N   . TRP B 334  ? 0.4699 0.3188 0.3047 -0.1172 -0.0388 0.0734  332  TRP B N   
11400 C CA  . TRP B 334  ? 0.4576 0.3211 0.2979 -0.1145 -0.0347 0.0719  332  TRP B CA  
11401 C C   . TRP B 334  ? 0.3877 0.2626 0.2360 -0.1162 -0.0320 0.0701  332  TRP B C   
11402 O O   . TRP B 334  ? 0.4228 0.2962 0.2755 -0.1137 -0.0331 0.0668  332  TRP B O   
11403 C CB  . TRP B 334  ? 0.4815 0.3440 0.3237 -0.1063 -0.0353 0.0682  332  TRP B CB  
11404 C CG  . TRP B 334  ? 0.4433 0.3194 0.2913 -0.1027 -0.0316 0.0659  332  TRP B CG  
11405 C CD1 . TRP B 334  ? 0.4303 0.3153 0.2772 -0.1042 -0.0285 0.0678  332  TRP B CD1 
11406 C CD2 . TRP B 334  ? 0.4135 0.2952 0.2687 -0.0969 -0.0306 0.0613  332  TRP B CD2 
11407 N NE1 . TRP B 334  ? 0.3989 0.2944 0.2519 -0.0994 -0.0258 0.0644  332  TRP B NE1 
11408 C CE2 . TRP B 334  ? 0.3850 0.2786 0.2433 -0.0950 -0.0270 0.0605  332  TRP B CE2 
11409 C CE3 . TRP B 334  ? 0.3949 0.2727 0.2542 -0.0930 -0.0323 0.0577  332  TRP B CE3 
11410 C CZ2 . TRP B 334  ? 0.3513 0.2525 0.2164 -0.0896 -0.0253 0.0564  332  TRP B CZ2 
11411 C CZ3 . TRP B 334  ? 0.4243 0.3102 0.2905 -0.0878 -0.0305 0.0538  332  TRP B CZ3 
11412 C CH2 . TRP B 334  ? 0.3956 0.2928 0.2647 -0.0862 -0.0271 0.0532  332  TRP B CH2 
11413 N N   . ASN B 335  ? 0.4039 0.2903 0.2540 -0.1204 -0.0286 0.0723  333  ASN B N   
11414 C CA  . ASN B 335  ? 0.4102 0.3084 0.2680 -0.1222 -0.0259 0.0709  333  ASN B CA  
11415 C C   . ASN B 335  ? 0.3735 0.2845 0.2378 -0.1169 -0.0224 0.0678  333  ASN B C   
11416 O O   . ASN B 335  ? 0.3795 0.3024 0.2500 -0.1183 -0.0195 0.0671  333  ASN B O   
11417 C CB  . ASN B 335  ? 0.4252 0.3284 0.2816 -0.1305 -0.0245 0.0752  333  ASN B CB  
11418 C CG  . ASN B 335  ? 0.4961 0.3869 0.3474 -0.1358 -0.0283 0.0776  333  ASN B CG  
11419 O OD1 . ASN B 335  ? 0.4390 0.3201 0.2900 -0.1340 -0.0313 0.0755  333  ASN B OD1 
11420 N ND2 . ASN B 335  ? 0.4847 0.3773 0.3336 -0.1405 -0.0280 0.0805  333  ASN B ND2 
11421 N N   . GLY B 336  ? 0.3716 0.2805 0.2346 -0.1110 -0.0226 0.0659  334  GLY B N   
11422 C CA  . GLY B 336  ? 0.3744 0.2945 0.2426 -0.1060 -0.0195 0.0631  334  GLY B CA  
11423 C C   . GLY B 336  ? 0.3425 0.2640 0.2173 -0.1003 -0.0197 0.0584  334  GLY B C   
11424 O O   . GLY B 336  ? 0.3344 0.2646 0.2134 -0.0961 -0.0172 0.0559  334  GLY B O   
11425 N N   . MET B 337  ? 0.3625 0.2758 0.2380 -0.1000 -0.0226 0.0570  335  MET B N   
11426 C CA  . MET B 337  ? 0.3363 0.2516 0.2181 -0.0947 -0.0226 0.0526  335  MET B CA  
11427 C C   . MET B 337  ? 0.3349 0.2631 0.2237 -0.0961 -0.0194 0.0516  335  MET B C   
11428 O O   . MET B 337  ? 0.3309 0.2613 0.2203 -0.1016 -0.0192 0.0535  335  MET B O   
11429 C CB  . MET B 337  ? 0.3864 0.2903 0.2670 -0.0945 -0.0262 0.0515  335  MET B CB  
11430 C CG  . MET B 337  ? 0.3868 0.2922 0.2735 -0.0890 -0.0263 0.0470  335  MET B CG  
11431 S SD  . MET B 337  ? 0.5339 0.4358 0.4204 -0.0812 -0.0273 0.0443  335  MET B SD  
11432 C CE  . MET B 337  ? 0.4281 0.3448 0.3222 -0.0776 -0.0232 0.0415  335  MET B CE  
11433 N N   . GLY B 338  ? 0.2990 0.2356 0.1930 -0.0912 -0.0171 0.0486  336  GLY B N   
11434 C CA  . GLY B 338  ? 0.3154 0.2647 0.2162 -0.0915 -0.0140 0.0474  336  GLY B CA  
11435 C C   . GLY B 338  ? 0.3032 0.2535 0.2100 -0.0868 -0.0143 0.0433  336  GLY B C   
11436 O O   . GLY B 338  ? 0.2957 0.2403 0.2023 -0.0818 -0.0158 0.0409  336  GLY B O   
11437 N N   . PHE B 339  ? 0.2791 0.2370 0.1913 -0.0884 -0.0129 0.0426  337  PHE B N   
11438 C CA  . PHE B 339  ? 0.2747 0.2335 0.1923 -0.0844 -0.0132 0.0390  337  PHE B CA  
11439 C C   . PHE B 339  ? 0.2604 0.2322 0.1845 -0.0851 -0.0102 0.0383  337  PHE B C   
11440 O O   . PHE B 339  ? 0.2850 0.2616 0.2096 -0.0903 -0.0094 0.0407  337  PHE B O   
11441 C CB  . PHE B 339  ? 0.2957 0.2445 0.2117 -0.0862 -0.0165 0.0388  337  PHE B CB  
11442 C CG  . PHE B 339  ? 0.2977 0.2450 0.2180 -0.0816 -0.0173 0.0350  337  PHE B CG  
11443 C CD1 . PHE B 339  ? 0.3049 0.2448 0.2239 -0.0764 -0.0190 0.0328  337  PHE B CD1 
11444 C CD2 . PHE B 339  ? 0.2690 0.2225 0.1945 -0.0824 -0.0165 0.0337  337  PHE B CD2 
11445 C CE1 . PHE B 339  ? 0.2969 0.2359 0.2199 -0.0723 -0.0196 0.0295  337  PHE B CE1 
11446 C CE2 . PHE B 339  ? 0.2935 0.2456 0.2227 -0.0783 -0.0172 0.0304  337  PHE B CE2 
11447 C CZ  . PHE B 339  ? 0.3110 0.2559 0.2389 -0.0733 -0.0186 0.0283  337  PHE B CZ  
11448 N N   . VAL B 340  ? 0.2523 0.2296 0.1811 -0.0798 -0.0086 0.0352  338  VAL B N   
11449 C CA  . VAL B 340  ? 0.2449 0.2345 0.1799 -0.0794 -0.0057 0.0343  338  VAL B CA  
11450 C C   . VAL B 340  ? 0.2502 0.2393 0.1893 -0.0796 -0.0070 0.0326  338  VAL B C   
11451 O O   . VAL B 340  ? 0.2363 0.2177 0.1752 -0.0767 -0.0091 0.0305  338  VAL B O   
11452 C CB  . VAL B 340  ? 0.2667 0.2619 0.2045 -0.0736 -0.0036 0.0318  338  VAL B CB  
11453 C CG1 . VAL B 340  ? 0.2489 0.2562 0.1930 -0.0727 -0.0008 0.0307  338  VAL B CG1 
11454 C CG2 . VAL B 340  ? 0.2528 0.2481 0.1860 -0.0733 -0.0025 0.0333  338  VAL B CG2 
11455 N N   . VAL B 341  ? 0.2418 0.2396 0.1847 -0.0828 -0.0055 0.0335  339  VAL B N   
11456 C CA  A VAL B 341  ? 0.2447 0.2445 0.1923 -0.0825 -0.0062 0.0317  339  VAL B CA  
11457 C CA  B VAL B 341  ? 0.2447 0.2444 0.1923 -0.0824 -0.0062 0.0317  339  VAL B CA  
11458 C C   . VAL B 341  ? 0.2195 0.2325 0.1733 -0.0806 -0.0030 0.0307  339  VAL B C   
11459 O O   . VAL B 341  ? 0.2268 0.2485 0.1813 -0.0828 -0.0007 0.0327  339  VAL B O   
11460 C CB  A VAL B 341  ? 0.2598 0.2561 0.2059 -0.0886 -0.0083 0.0338  339  VAL B CB  
11461 C CB  B VAL B 341  ? 0.2598 0.2560 0.2058 -0.0886 -0.0083 0.0337  339  VAL B CB  
11462 C CG1 A VAL B 341  ? 0.2802 0.2624 0.2199 -0.0898 -0.0116 0.0343  339  VAL B CG1 
11463 C CG1 B VAL B 341  ? 0.2443 0.2383 0.1934 -0.0873 -0.0099 0.0313  339  VAL B CG1 
11464 C CG2 A VAL B 341  ? 0.2895 0.2940 0.2356 -0.0942 -0.0065 0.0372  339  VAL B CG2 
11465 C CG2 B VAL B 341  ? 0.2854 0.2697 0.2243 -0.0914 -0.0109 0.0357  339  VAL B CG2 
11466 N N   . GLN B 342  ? 0.2140 0.2286 0.1721 -0.0765 -0.0030 0.0278  340  GLN B N   
11467 C CA  . GLN B 342  ? 0.2165 0.2423 0.1803 -0.0734 -0.0003 0.0263  340  GLN B CA  
11468 C C   . GLN B 342  ? 0.2228 0.2550 0.1910 -0.0763 -0.0003 0.0267  340  GLN B C   
11469 O O   . GLN B 342  ? 0.2242 0.2521 0.1936 -0.0759 -0.0022 0.0252  340  GLN B O   
11470 C CB  . GLN B 342  ? 0.2080 0.2313 0.1737 -0.0670 -0.0003 0.0229  340  GLN B CB  
11471 C CG  . GLN B 342  ? 0.1876 0.2058 0.1495 -0.0640 -0.0002 0.0225  340  GLN B CG  
11472 C CD  . GLN B 342  ? 0.2118 0.2226 0.1739 -0.0593 -0.0018 0.0196  340  GLN B CD  
11473 O OE1 . GLN B 342  ? 0.2226 0.2269 0.1843 -0.0597 -0.0040 0.0189  340  GLN B OE1 
11474 N NE2 . GLN B 342  ? 0.2096 0.2216 0.1722 -0.0548 -0.0006 0.0180  340  GLN B NE2 
11475 N N   . ALA B 343  ? 0.2034 0.2463 0.1741 -0.0790 0.0019  0.0286  341  ALA B N   
11476 C CA  . ALA B 343  ? 0.1839 0.2340 0.1589 -0.0822 0.0018  0.0293  341  ALA B CA  
11477 C C   . ALA B 343  ? 0.1924 0.2479 0.1730 -0.0776 0.0026  0.0265  341  ALA B C   
11478 O O   . ALA B 343  ? 0.2061 0.2652 0.1900 -0.0796 0.0018  0.0265  341  ALA B O   
11479 C CB  . ALA B 343  ? 0.2112 0.2720 0.1876 -0.0863 0.0041  0.0323  341  ALA B CB  
11480 N N   . TYR B 344  ? 0.2051 0.2608 0.1867 -0.0716 0.0040  0.0241  342  TYR B N   
11481 C CA  . TYR B 344  ? 0.1829 0.2419 0.1692 -0.0675 0.0042  0.0215  342  TYR B CA  
11482 C C   . TYR B 344  ? 0.1936 0.2430 0.1788 -0.0669 0.0014  0.0198  342  TYR B C   
11483 O O   . TYR B 344  ? 0.2033 0.2547 0.1921 -0.0640 0.0013  0.0178  342  TYR B O   
11484 C CB  . TYR B 344  ? 0.1946 0.2572 0.1826 -0.0614 0.0065  0.0195  342  TYR B CB  
11485 C CG  . TYR B 344  ? 0.1862 0.2397 0.1710 -0.0573 0.0058  0.0176  342  TYR B CG  
11486 C CD1 . TYR B 344  ? 0.1922 0.2345 0.1724 -0.0587 0.0033  0.0178  342  TYR B CD1 
11487 C CD2 . TYR B 344  ? 0.1902 0.2466 0.1765 -0.0521 0.0076  0.0157  342  TYR B CD2 
11488 C CE1 . TYR B 344  ? 0.1914 0.2264 0.1691 -0.0549 0.0027  0.0162  342  TYR B CE1 
11489 C CE2 . TYR B 344  ? 0.2047 0.2535 0.1883 -0.0487 0.0069  0.0141  342  TYR B CE2 
11490 C CZ  . TYR B 344  ? 0.1974 0.2360 0.1770 -0.0501 0.0045  0.0144  342  TYR B CZ  
11491 O OH  . TYR B 344  ? 0.1871 0.2190 0.1644 -0.0466 0.0038  0.0128  342  TYR B OH  
11492 N N   . GLY B 345  ? 0.1983 0.2375 0.1786 -0.0694 -0.0009 0.0206  343  GLY B N   
11493 C CA  . GLY B 345  ? 0.2090 0.2384 0.1877 -0.0685 -0.0036 0.0189  343  GLY B CA  
11494 C C   . GLY B 345  ? 0.2214 0.2499 0.2000 -0.0735 -0.0056 0.0200  343  GLY B C   
11495 O O   . GLY B 345  ? 0.2152 0.2454 0.1923 -0.0788 -0.0059 0.0226  343  GLY B O   
11496 N N   . LYS B 346  ? 0.2049 0.2304 0.1849 -0.0719 -0.0071 0.0179  344  LYS B N   
11497 C CA  . LYS B 346  ? 0.2181 0.2425 0.1980 -0.0763 -0.0091 0.0185  344  LYS B CA  
11498 C C   . LYS B 346  ? 0.2388 0.2522 0.2127 -0.0804 -0.0118 0.0198  344  LYS B C   
11499 O O   . LYS B 346  ? 0.2338 0.2466 0.2068 -0.0855 -0.0135 0.0211  344  LYS B O   
11500 C CB  . LYS B 346  ? 0.2259 0.2490 0.2081 -0.0730 -0.0100 0.0158  344  LYS B CB  
11501 C CG  . LYS B 346  ? 0.2218 0.2556 0.2098 -0.0694 -0.0076 0.0148  344  LYS B CG  
11502 C CD  . LYS B 346  ? 0.2286 0.2605 0.2184 -0.0659 -0.0084 0.0122  344  LYS B CD  
11503 C CE  . LYS B 346  ? 0.2158 0.2587 0.2113 -0.0630 -0.0063 0.0116  344  LYS B CE  
11504 N NZ  . LYS B 346  ? 0.2068 0.2479 0.2039 -0.0592 -0.0068 0.0092  344  LYS B NZ  
11505 N N   . ARG B 347  ? 0.2216 0.2262 0.1914 -0.0782 -0.0125 0.0194  345  ARG B N   
11506 C CA  . ARG B 347  ? 0.2462 0.2396 0.2100 -0.0816 -0.0151 0.0205  345  ARG B CA  
11507 C C   . ARG B 347  ? 0.2335 0.2278 0.1944 -0.0865 -0.0148 0.0239  345  ARG B C   
11508 O O   . ARG B 347  ? 0.2638 0.2492 0.2196 -0.0902 -0.0171 0.0253  345  ARG B O   
11509 C CB  . ARG B 347  ? 0.2402 0.2234 0.2007 -0.0771 -0.0162 0.0186  345  ARG B CB  
11510 C CG  . ARG B 347  ? 0.2293 0.2098 0.1916 -0.0731 -0.0170 0.0155  345  ARG B CG  
11511 C CD  . ARG B 347  ? 0.2205 0.1944 0.1814 -0.0676 -0.0172 0.0136  345  ARG B CD  
11512 N NE  . ARG B 347  ? 0.2121 0.1930 0.1763 -0.0638 -0.0146 0.0131  345  ARG B NE  
11513 C CZ  . ARG B 347  ? 0.2160 0.1930 0.1793 -0.0595 -0.0144 0.0118  345  ARG B CZ  
11514 N NH1 . ARG B 347  ? 0.2327 0.1994 0.1923 -0.0581 -0.0165 0.0110  345  ARG B NH1 
11515 N NH2 . ARG B 347  ? 0.2118 0.1952 0.1780 -0.0564 -0.0121 0.0114  345  ARG B NH2 
11516 N N   . CYS B 348  ? 0.2364 0.2415 0.2005 -0.0865 -0.0119 0.0252  346  CYS B N   
11517 C CA  . CYS B 348  ? 0.2503 0.2568 0.2116 -0.0903 -0.0111 0.0283  346  CYS B CA  
11518 C C   . CYS B 348  ? 0.2623 0.2646 0.2200 -0.0975 -0.0132 0.0311  346  CYS B C   
11519 O O   . CYS B 348  ? 0.2810 0.2750 0.2332 -0.0996 -0.0145 0.0328  346  CYS B O   
11520 C CB  . CYS B 348  ? 0.2412 0.2614 0.2071 -0.0894 -0.0075 0.0291  346  CYS B CB  
11521 S SG  . CYS B 348  ? 0.2988 0.3206 0.2608 -0.0924 -0.0059 0.0325  346  CYS B SG  
11522 N N   . PRO B 349  ? 0.2639 0.2713 0.2244 -0.1015 -0.0139 0.0318  347  PRO B N   
11523 C CA  . PRO B 349  ? 0.2821 0.2849 0.2388 -0.1088 -0.0161 0.0346  347  PRO B CA  
11524 C C   . PRO B 349  ? 0.2545 0.2416 0.2049 -0.1093 -0.0197 0.0338  347  PRO B C   
11525 O O   . PRO B 349  ? 0.2794 0.2593 0.2246 -0.1141 -0.0214 0.0362  347  PRO B O   
11526 C CB  . PRO B 349  ? 0.2994 0.3114 0.2611 -0.1122 -0.0162 0.0349  347  PRO B CB  
11527 C CG  . PRO B 349  ? 0.2949 0.3115 0.2614 -0.1062 -0.0151 0.0316  347  PRO B CG  
11528 C CD  . PRO B 349  ? 0.2716 0.2885 0.2384 -0.0999 -0.0129 0.0301  347  PRO B CD  
11529 N N   . PHE B 350  ? 0.2693 0.2508 0.2201 -0.1044 -0.0208 0.0304  348  PHE B N   
11530 C CA  . PHE B 350  ? 0.2862 0.2528 0.2310 -0.1040 -0.0241 0.0293  348  PHE B CA  
11531 C C   . PHE B 350  ? 0.2747 0.2332 0.2148 -0.1015 -0.0242 0.0298  348  PHE B C   
11532 O O   . PHE B 350  ? 0.2969 0.2438 0.2310 -0.1037 -0.0268 0.0307  348  PHE B O   
11533 C CB  . PHE B 350  ? 0.2646 0.2290 0.2115 -0.0994 -0.0249 0.0257  348  PHE B CB  
11534 C CG  . PHE B 350  ? 0.2892 0.2625 0.2410 -0.1014 -0.0246 0.0253  348  PHE B CG  
11535 C CD1 . PHE B 350  ? 0.3138 0.2837 0.2635 -0.1072 -0.0272 0.0262  348  PHE B CD1 
11536 C CD2 . PHE B 350  ? 0.2681 0.2533 0.2264 -0.0980 -0.0218 0.0241  348  PHE B CD2 
11537 C CE1 . PHE B 350  ? 0.3382 0.3167 0.2924 -0.1093 -0.0271 0.0260  348  PHE B CE1 
11538 C CE2 . PHE B 350  ? 0.2941 0.2878 0.2569 -0.0998 -0.0216 0.0239  348  PHE B CE2 
11539 C CZ  . PHE B 350  ? 0.3051 0.2958 0.2660 -0.1055 -0.0243 0.0249  348  PHE B CZ  
11540 N N   . VAL B 351  ? 0.2782 0.2429 0.2211 -0.0970 -0.0215 0.0292  349  VAL B N   
11541 C CA  . VAL B 351  ? 0.2601 0.2186 0.1987 -0.0950 -0.0215 0.0299  349  VAL B CA  
11542 C C   . VAL B 351  ? 0.2717 0.2292 0.2062 -0.1010 -0.0217 0.0338  349  VAL B C   
11543 O O   . VAL B 351  ? 0.2908 0.2378 0.2193 -0.1019 -0.0237 0.0351  349  VAL B O   
11544 C CB  . VAL B 351  ? 0.2447 0.2108 0.1872 -0.0893 -0.0185 0.0285  349  VAL B CB  
11545 C CG1 . VAL B 351  ? 0.2774 0.2376 0.2153 -0.0876 -0.0186 0.0295  349  VAL B CG1 
11546 C CG2 . VAL B 351  ? 0.2706 0.2362 0.2164 -0.0836 -0.0185 0.0248  349  VAL B CG2 
11547 N N   . LEU B 352  ? 0.2741 0.2427 0.2120 -0.1051 -0.0198 0.0359  350  LEU B N   
11548 C CA  . LEU B 352  ? 0.2938 0.2625 0.2281 -0.1114 -0.0199 0.0399  350  LEU B CA  
11549 C C   . LEU B 352  ? 0.2951 0.2522 0.2239 -0.1166 -0.0236 0.0413  350  LEU B C   
11550 O O   . LEU B 352  ? 0.3246 0.2739 0.2475 -0.1197 -0.0249 0.0439  350  LEU B O   
11551 C CB  . LEU B 352  ? 0.2811 0.2647 0.2206 -0.1148 -0.0171 0.0418  350  LEU B CB  
11552 C CG  . LEU B 352  ? 0.2835 0.2781 0.2271 -0.1103 -0.0133 0.0411  350  LEU B CG  
11553 C CD1 . LEU B 352  ? 0.3007 0.3101 0.2497 -0.1136 -0.0107 0.0428  350  LEU B CD1 
11554 C CD2 . LEU B 352  ? 0.3232 0.3139 0.2618 -0.1098 -0.0126 0.0429  350  LEU B CD2 
11555 N N   . ASP B 353  ? 0.3171 0.2725 0.2475 -0.1177 -0.0254 0.0397  351  ASP B N   
11556 C CA  . ASP B 353  ? 0.3201 0.2632 0.2449 -0.1222 -0.0292 0.0405  351  ASP B CA  
11557 C C   . ASP B 353  ? 0.2893 0.2177 0.2076 -0.1190 -0.0314 0.0396  351  ASP B C   
11558 O O   . ASP B 353  ? 0.3315 0.2496 0.2434 -0.1230 -0.0339 0.0419  351  ASP B O   
11559 C CB  . ASP B 353  ? 0.3239 0.2669 0.2512 -0.1224 -0.0308 0.0381  351  ASP B CB  
11560 C CG  . ASP B 353  ? 0.3486 0.3045 0.2814 -0.1269 -0.0295 0.0394  351  ASP B CG  
11561 O OD1 . ASP B 353  ? 0.3659 0.3286 0.2993 -0.1318 -0.0282 0.0428  351  ASP B OD1 
11562 O OD2 . ASP B 353  ? 0.4209 0.3805 0.3577 -0.1255 -0.0298 0.0371  351  ASP B OD2 
11563 N N   . PHE B 354  ? 0.3314 0.2584 0.2513 -0.1116 -0.0308 0.0364  352  PHE B N   
11564 C CA  . PHE B 354  ? 0.3135 0.2277 0.2279 -0.1078 -0.0327 0.0355  352  PHE B CA  
11565 C C   . PHE B 354  ? 0.3044 0.2163 0.2147 -0.1092 -0.0323 0.0385  352  PHE B C   
11566 O O   . PHE B 354  ? 0.3350 0.2348 0.2386 -0.1106 -0.0349 0.0398  352  PHE B O   
11567 C CB  . PHE B 354  ? 0.3211 0.2369 0.2392 -0.0999 -0.0316 0.0317  352  PHE B CB  
11568 C CG  . PHE B 354  ? 0.3117 0.2170 0.2253 -0.0954 -0.0330 0.0309  352  PHE B CG  
11569 C CD1 . PHE B 354  ? 0.3364 0.2289 0.2455 -0.0940 -0.0361 0.0294  352  PHE B CD1 
11570 C CD2 . PHE B 354  ? 0.3170 0.2252 0.2306 -0.0926 -0.0313 0.0316  352  PHE B CD2 
11571 C CE1 . PHE B 354  ? 0.3308 0.2139 0.2359 -0.0897 -0.0375 0.0287  352  PHE B CE1 
11572 C CE2 . PHE B 354  ? 0.3664 0.2651 0.2759 -0.0887 -0.0328 0.0310  352  PHE B CE2 
11573 C CZ  . PHE B 354  ? 0.3456 0.2321 0.2512 -0.0872 -0.0359 0.0296  352  PHE B CZ  
11574 N N   . ILE B 355  ? 0.3134 0.2368 0.2273 -0.1087 -0.0290 0.0396  353  ILE B N   
11575 C CA  . ILE B 355  ? 0.3181 0.2402 0.2281 -0.1096 -0.0282 0.0423  353  ILE B CA  
11576 C C   . ILE B 355  ? 0.3263 0.2446 0.2314 -0.1174 -0.0296 0.0464  353  ILE B C   
11577 O O   . ILE B 355  ? 0.3386 0.2475 0.2372 -0.1188 -0.0313 0.0485  353  ILE B O   
11578 C CB  . ILE B 355  ? 0.3088 0.2445 0.2237 -0.1071 -0.0243 0.0423  353  ILE B CB  
11579 C CG1 . ILE B 355  ? 0.3349 0.2722 0.2535 -0.0993 -0.0233 0.0385  353  ILE B CG1 
11580 C CG2 . ILE B 355  ? 0.3140 0.2494 0.2245 -0.1092 -0.0234 0.0456  353  ILE B CG2 
11581 C CD1 . ILE B 355  ? 0.3164 0.2673 0.2405 -0.0968 -0.0195 0.0379  353  ILE B CD1 
11582 N N   . ILE B 356  ? 0.3387 0.2646 0.2469 -0.1228 -0.0290 0.0478  354  ILE B N   
11583 C CA  . ILE B 356  ? 0.3583 0.2813 0.2623 -0.1309 -0.0303 0.0518  354  ILE B CA  
11584 C C   . ILE B 356  ? 0.3599 0.2659 0.2567 -0.1327 -0.0347 0.0520  354  ILE B C   
11585 O O   . ILE B 356  ? 0.3581 0.2560 0.2484 -0.1367 -0.0363 0.0551  354  ILE B O   
11586 C CB  . ILE B 356  ? 0.3651 0.2999 0.2745 -0.1360 -0.0290 0.0529  354  ILE B CB  
11587 C CG1 . ILE B 356  ? 0.3778 0.3289 0.2930 -0.1349 -0.0246 0.0537  354  ILE B CG1 
11588 C CG2 . ILE B 356  ? 0.3667 0.2965 0.2716 -0.1447 -0.0312 0.0567  354  ILE B CG2 
11589 C CD1 . ILE B 356  ? 0.3712 0.3357 0.2936 -0.1375 -0.0230 0.0535  354  ILE B CD1 
11590 N N   . ASP B 357  ? 0.3584 0.2586 0.2559 -0.1295 -0.0366 0.0485  355  ASP B N   
11591 C CA  . ASP B 357  ? 0.3781 0.2617 0.2687 -0.1304 -0.0408 0.0482  355  ASP B CA  
11592 C C   . ASP B 357  ? 0.3528 0.2261 0.2379 -0.1260 -0.0419 0.0482  355  ASP B C   
11593 O O   . ASP B 357  ? 0.3566 0.2176 0.2345 -0.1290 -0.0447 0.0503  355  ASP B O   
11594 C CB  . ASP B 357  ? 0.3605 0.2410 0.2532 -0.1273 -0.0423 0.0442  355  ASP B CB  
11595 C CG  . ASP B 357  ? 0.3863 0.2493 0.2717 -0.1264 -0.0464 0.0432  355  ASP B CG  
11596 O OD1 . ASP B 357  ? 0.4233 0.2807 0.3047 -0.1306 -0.0487 0.0445  355  ASP B OD1 
11597 O OD2 . ASP B 357  ? 0.3990 0.2562 0.2836 -0.1196 -0.0468 0.0404  355  ASP B OD2 
11598 N N   . LEU B 358  ? 0.3479 0.2258 0.2364 -0.1190 -0.0398 0.0458  356  LEU B N   
11599 C CA  . LEU B 358  ? 0.3255 0.1949 0.2094 -0.1147 -0.0407 0.0459  356  LEU B CA  
11600 C C   . LEU B 358  ? 0.3354 0.2035 0.2145 -0.1193 -0.0406 0.0503  356  LEU B C   
11601 O O   . LEU B 358  ? 0.3802 0.2359 0.2522 -0.1196 -0.0432 0.0518  356  LEU B O   
11602 C CB  . LEU B 358  ? 0.3287 0.2059 0.2179 -0.1073 -0.0382 0.0430  356  LEU B CB  
11603 C CG  . LEU B 358  ? 0.3383 0.2091 0.2239 -0.1024 -0.0388 0.0429  356  LEU B CG  
11604 C CD1 . LEU B 358  ? 0.3827 0.2378 0.2624 -0.1003 -0.0426 0.0419  356  LEU B CD1 
11605 C CD2 . LEU B 358  ? 0.3407 0.2204 0.2324 -0.0957 -0.0362 0.0399  356  LEU B CD2 
11606 N N   . ALA B 359  ? 0.3508 0.2316 0.2333 -0.1229 -0.0375 0.0525  357  ALA B N   
11607 C CA  . ALA B 359  ? 0.3551 0.2358 0.2331 -0.1276 -0.0370 0.0569  357  ALA B CA  
11608 C C   . ALA B 359  ? 0.3890 0.2584 0.2604 -0.1343 -0.0403 0.0598  357  ALA B C   
11609 O O   . ALA B 359  ? 0.4175 0.2787 0.2826 -0.1346 -0.0420 0.0618  357  ALA B O   
11610 C CB  . ALA B 359  ? 0.4014 0.2986 0.2849 -0.1305 -0.0330 0.0586  357  ALA B CB  
11611 N N   . ARG B 360  ? 0.3794 0.2505 0.2533 -0.1370 -0.0414 0.0587  358  ARG B N   
11612 C CA  A ARG B 360  ? 0.4048 0.2688 0.2742 -0.1409 -0.0443 0.0599  358  ARG B CA  
11613 C CA  B ARG B 360  ? 0.4047 0.2687 0.2742 -0.1409 -0.0443 0.0600  358  ARG B CA  
11614 C C   . ARG B 360  ? 0.3809 0.2280 0.2434 -0.1375 -0.0481 0.0587  358  ARG B C   
11615 O O   . ARG B 360  ? 0.4169 0.2563 0.2734 -0.1395 -0.0501 0.0608  358  ARG B O   
11616 C CB  A ARG B 360  ? 0.4210 0.2898 0.2945 -0.1437 -0.0448 0.0586  358  ARG B CB  
11617 C CB  B ARG B 360  ? 0.4208 0.2900 0.2944 -0.1439 -0.0447 0.0587  358  ARG B CB  
11618 C CG  A ARG B 360  ? 0.4344 0.3194 0.3141 -0.1481 -0.0417 0.0604  358  ARG B CG  
11619 C CG  B ARG B 360  ? 0.4634 0.3407 0.3380 -0.1504 -0.0440 0.0618  358  ARG B CG  
11620 C CD  A ARG B 360  ? 0.4765 0.3636 0.3580 -0.1521 -0.0432 0.0600  358  ARG B CD  
11621 C CD  B ARG B 360  ? 0.4795 0.3600 0.3573 -0.1532 -0.0451 0.0605  358  ARG B CD  
11622 N NE  A ARG B 360  ? 0.4705 0.3726 0.3571 -0.1566 -0.0406 0.0623  358  ARG B NE  
11623 N NE  B ARG B 360  ? 0.4727 0.3666 0.3586 -0.1524 -0.0423 0.0590  358  ARG B NE  
11624 C CZ  A ARG B 360  ? 0.4814 0.3959 0.3754 -0.1568 -0.0385 0.0611  358  ARG B CZ  
11625 C CZ  B ARG B 360  ? 0.4865 0.3951 0.3779 -0.1559 -0.0396 0.0608  358  ARG B CZ  
11626 N NH1 A ARG B 360  ? 0.5168 0.4304 0.4138 -0.1531 -0.0388 0.0577  358  ARG B NH1 
11627 N NH1 B ARG B 360  ? 0.5340 0.4464 0.4239 -0.1605 -0.0390 0.0642  358  ARG B NH1 
11628 N NH2 A ARG B 360  ? 0.4992 0.4274 0.3977 -0.1607 -0.0361 0.0634  358  ARG B NH2 
11629 N NH2 B ARG B 360  ? 0.5124 0.4323 0.4111 -0.1546 -0.0374 0.0591  358  ARG B NH2 
11630 N N   . ARG B 361  ? 0.3940 0.2355 0.2573 -0.1322 -0.0491 0.0552  359  ARG B N   
11631 C CA  . ARG B 361  ? 0.4500 0.2760 0.3071 -0.1286 -0.0527 0.0537  359  ARG B CA  
11632 C C   . ARG B 361  ? 0.4058 0.2253 0.2586 -0.1248 -0.0531 0.0547  359  ARG B C   
11633 O O   . ARG B 361  ? 0.4322 0.2393 0.2789 -0.1228 -0.0561 0.0544  359  ARG B O   
11634 C CB  . ARG B 361  ? 0.5076 0.3294 0.3666 -0.1242 -0.0539 0.0495  359  ARG B CB  
11635 C CG  . ARG B 361  ? 0.4855 0.3120 0.3493 -0.1194 -0.0518 0.0472  359  ARG B CG  
11636 C CD  . ARG B 361  ? 0.4017 0.2255 0.2679 -0.1160 -0.0529 0.0431  359  ARG B CD  
11637 N NE  . ARG B 361  ? 0.3873 0.2237 0.2615 -0.1111 -0.0496 0.0404  359  ARG B NE  
11638 C CZ  . ARG B 361  ? 0.3704 0.2072 0.2466 -0.1037 -0.0488 0.0379  359  ARG B CZ  
11639 N NH1 . ARG B 361  ? 0.4074 0.2327 0.2783 -0.1000 -0.0510 0.0376  359  ARG B NH1 
11640 N NH2 . ARG B 361  ? 0.3549 0.2039 0.2386 -0.0998 -0.0457 0.0356  359  ARG B NH2 
11641 N N   . SER B 362  ? 0.3959 0.2234 0.2513 -0.1239 -0.0502 0.0559  360  SER B N   
11642 C CA  . SER B 362  ? 0.4105 0.2323 0.2619 -0.1201 -0.0506 0.0568  360  SER B CA  
11643 C C   . SER B 362  ? 0.4137 0.2375 0.2614 -0.1240 -0.0499 0.0609  360  SER B C   
11644 O O   . SER B 362  ? 0.4402 0.2582 0.2835 -0.1213 -0.0507 0.0620  360  SER B O   
11645 C CB  . SER B 362  ? 0.4301 0.2613 0.2876 -0.1139 -0.0477 0.0542  360  SER B CB  
11646 O OG  . SER B 362  ? 0.3996 0.2461 0.2624 -0.1163 -0.0438 0.0554  360  SER B OG  
11647 N N   . GLY B 363  ? 0.4066 0.2386 0.2559 -0.1301 -0.0484 0.0631  361  GLY B N   
11648 C CA  . GLY B 363  ? 0.4207 0.2554 0.2668 -0.1338 -0.0475 0.0669  361  GLY B CA  
11649 C C   . GLY B 363  ? 0.4147 0.2584 0.2627 -0.1324 -0.0441 0.0682  361  GLY B C   
11650 O O   . GLY B 363  ? 0.4467 0.2883 0.2901 -0.1325 -0.0440 0.0706  361  GLY B O   
11651 N N   . ARG B 364  ? 0.3893 0.2429 0.2435 -0.1309 -0.0413 0.0666  362  ARG B N   
11652 C CA  . ARG B 364  ? 0.4344 0.2991 0.2919 -0.1279 -0.0377 0.0665  362  ARG B CA  
11653 C C   . ARG B 364  ? 0.4281 0.3086 0.2925 -0.1312 -0.0341 0.0669  362  ARG B C   
11654 O O   . ARG B 364  ? 0.4397 0.3243 0.3095 -0.1310 -0.0339 0.0644  362  ARG B O   
11655 C CB  . ARG B 364  ? 0.4224 0.2880 0.2841 -0.1191 -0.0374 0.0618  362  ARG B CB  
11656 C CG  . ARG B 364  ? 0.4112 0.2627 0.2676 -0.1144 -0.0408 0.0607  362  ARG B CG  
11657 C CD  . ARG B 364  ? 0.4133 0.2624 0.2647 -0.1133 -0.0408 0.0630  362  ARG B CD  
11658 N NE  . ARG B 364  ? 0.4304 0.2653 0.2763 -0.1093 -0.0445 0.0624  362  ARG B NE  
11659 C CZ  . ARG B 364  ? 0.3897 0.2235 0.2380 -0.1018 -0.0450 0.0589  362  ARG B CZ  
11660 N NH1 . ARG B 364  ? 0.4051 0.2504 0.2606 -0.0976 -0.0421 0.0559  362  ARG B NH1 
11661 N NH2 . ARG B 364  ? 0.4509 0.2716 0.2940 -0.0986 -0.0485 0.0586  362  ARG B NH2 
11662 N N   . ARG B 365  ? 0.4097 0.2994 0.2739 -0.1341 -0.0312 0.0698  363  ARG B N   
11663 C CA  . ARG B 365  ? 0.3819 0.2883 0.2537 -0.1350 -0.0272 0.0693  363  ARG B CA  
11664 C C   . ARG B 365  ? 0.3499 0.2628 0.2267 -0.1269 -0.0251 0.0653  363  ARG B C   
11665 O O   . ARG B 365  ? 0.3631 0.2743 0.2371 -0.1231 -0.0247 0.0652  363  ARG B O   
11666 C CB  . ARG B 365  ? 0.4094 0.3240 0.2794 -0.1404 -0.0245 0.0737  363  ARG B CB  
11667 C CG  . ARG B 365  ? 0.4143 0.3458 0.2920 -0.1425 -0.0208 0.0736  363  ARG B CG  
11668 C CD  . ARG B 365  ? 0.4363 0.3757 0.3132 -0.1472 -0.0189 0.0771  363  ARG B CD  
11669 N NE  . ARG B 365  ? 0.4563 0.4115 0.3408 -0.1496 -0.0158 0.0771  363  ARG B NE  
11670 C CZ  . ARG B 365  ? 0.4282 0.3968 0.3153 -0.1497 -0.0118 0.0783  363  ARG B CZ  
11671 N NH1 . ARG B 365  ? 0.4136 0.3821 0.2964 -0.1479 -0.0102 0.0797  363  ARG B NH1 
11672 N NH2 . ARG B 365  ? 0.3751 0.3576 0.2693 -0.1515 -0.0094 0.0782  363  ARG B NH2 
11673 N N   . ILE B 366  ? 0.3532 0.2724 0.2369 -0.1242 -0.0242 0.0619  364  ILE B N   
11674 C CA  . ILE B 366  ? 0.3418 0.2673 0.2307 -0.1168 -0.0223 0.0580  364  ILE B CA  
11675 C C   . ILE B 366  ? 0.3731 0.3147 0.2673 -0.1174 -0.0180 0.0585  364  ILE B C   
11676 O O   . ILE B 366  ? 0.3443 0.2937 0.2419 -0.1221 -0.0168 0.0598  364  ILE B O   
11677 C CB  . ILE B 366  ? 0.3397 0.2622 0.2327 -0.1131 -0.0239 0.0540  364  ILE B CB  
11678 C CG1 . ILE B 366  ? 0.3801 0.2864 0.2674 -0.1124 -0.0281 0.0537  364  ILE B CG1 
11679 C CG2 . ILE B 366  ? 0.3183 0.2478 0.2168 -0.1059 -0.0218 0.0502  364  ILE B CG2 
11680 C CD1 . ILE B 366  ? 0.3929 0.2954 0.2833 -0.1093 -0.0298 0.0500  364  ILE B CD1 
11681 N N   . MET B 367  ? 0.3385 0.2853 0.2334 -0.1127 -0.0158 0.0574  365  MET B N   
11682 C CA  . MET B 367  ? 0.3403 0.3022 0.2403 -0.1121 -0.0116 0.0572  365  MET B CA  
11683 C C   . MET B 367  ? 0.3343 0.3020 0.2418 -0.1075 -0.0107 0.0531  365  MET B C   
11684 O O   . MET B 367  ? 0.3324 0.2951 0.2406 -0.1018 -0.0119 0.0499  365  MET B O   
11685 C CB  . MET B 367  ? 0.3116 0.2756 0.2088 -0.1088 -0.0098 0.0574  365  MET B CB  
11686 C CG  . MET B 367  ? 0.3081 0.2638 0.1970 -0.1123 -0.0113 0.0612  365  MET B CG  
11687 S SD  . MET B 367  ? 0.3580 0.3170 0.2432 -0.1086 -0.0091 0.0616  365  MET B SD  
11688 C CE  . MET B 367  ? 0.4150 0.3864 0.2997 -0.1144 -0.0052 0.0656  365  MET B CE  
11689 N N   . VAL B 368  ? 0.2918 0.2702 0.2048 -0.1099 -0.0088 0.0532  366  VAL B N   
11690 C CA  . VAL B 368  ? 0.2945 0.2780 0.2144 -0.1062 -0.0082 0.0496  366  VAL B CA  
11691 C C   . VAL B 368  ? 0.2979 0.2960 0.2231 -0.1039 -0.0042 0.0489  366  VAL B C   
11692 O O   . VAL B 368  ? 0.2973 0.3052 0.2246 -0.1081 -0.0020 0.0512  366  VAL B O   
11693 C CB  . VAL B 368  ? 0.3167 0.2992 0.2389 -0.1104 -0.0100 0.0499  366  VAL B CB  
11694 C CG1 . VAL B 368  ? 0.3070 0.2950 0.2360 -0.1062 -0.0093 0.0462  366  VAL B CG1 
11695 C CG2 . VAL B 368  ? 0.3384 0.3055 0.2547 -0.1124 -0.0141 0.0504  366  VAL B CG2 
11696 N N   . ARG B 369  ? 0.2744 0.2742 0.2017 -0.0973 -0.0031 0.0457  367  ARG B N   
11697 C CA  . ARG B 369  ? 0.2602 0.2729 0.1924 -0.0944 0.0006  0.0445  367  ARG B CA  
11698 C C   . ARG B 369  ? 0.2563 0.2747 0.1954 -0.0929 0.0009  0.0421  367  ARG B C   
11699 O O   . ARG B 369  ? 0.2608 0.2740 0.2016 -0.0888 -0.0006 0.0391  367  ARG B O   
11700 C CB  . ARG B 369  ? 0.2445 0.2563 0.1754 -0.0883 0.0016  0.0423  367  ARG B CB  
11701 C CG  . ARG B 369  ? 0.2795 0.3043 0.2147 -0.0855 0.0055  0.0413  367  ARG B CG  
11702 C CD  . ARG B 369  ? 0.2596 0.2830 0.1948 -0.0788 0.0060  0.0382  367  ARG B CD  
11703 N NE  . ARG B 369  ? 0.2594 0.2766 0.1880 -0.0785 0.0054  0.0394  367  ARG B NE  
11704 C CZ  . ARG B 369  ? 0.2671 0.2780 0.1937 -0.0738 0.0042  0.0371  367  ARG B CZ  
11705 N NH1 . ARG B 369  ? 0.2609 0.2710 0.1915 -0.0690 0.0036  0.0337  367  ARG B NH1 
11706 N NH2 . ARG B 369  ? 0.2813 0.2868 0.2016 -0.0740 0.0035  0.0386  367  ARG B NH2 
11707 N N   . LEU B 370  ? 0.2515 0.2809 0.1947 -0.0961 0.0029  0.0435  368  LEU B N   
11708 C CA  . LEU B 370  ? 0.2516 0.2881 0.2017 -0.0945 0.0035  0.0414  368  LEU B CA  
11709 C C   . LEU B 370  ? 0.2373 0.2836 0.1913 -0.0890 0.0068  0.0393  368  LEU B C   
11710 O O   . LEU B 370  ? 0.2538 0.3087 0.2079 -0.0897 0.0097  0.0409  368  LEU B O   
11711 C CB  . LEU B 370  ? 0.2429 0.2865 0.1956 -0.1008 0.0038  0.0440  368  LEU B CB  
11712 C CG  . LEU B 370  ? 0.2582 0.3087 0.2178 -0.0996 0.0040  0.0421  368  LEU B CG  
11713 C CD1 . LEU B 370  ? 0.2841 0.3240 0.2432 -0.0982 0.0006  0.0397  368  LEU B CD1 
11714 C CD2 . LEU B 370  ? 0.2645 0.3243 0.2269 -0.1059 0.0047  0.0450  368  LEU B CD2 
11715 N N   . VAL B 371  ? 0.2198 0.2643 0.1767 -0.0836 0.0064  0.0358  369  VAL B N   
11716 C CA  . VAL B 371  ? 0.2240 0.2765 0.1848 -0.0781 0.0091  0.0335  369  VAL B CA  
11717 C C   . VAL B 371  ? 0.2200 0.2774 0.1870 -0.0765 0.0090  0.0315  369  VAL B C   
11718 O O   . VAL B 371  ? 0.2400 0.2929 0.2077 -0.0790 0.0066  0.0315  369  VAL B O   
11719 C CB  . VAL B 371  ? 0.2142 0.2596 0.1723 -0.0725 0.0085  0.0310  369  VAL B CB  
11720 C CG1 . VAL B 371  ? 0.2445 0.2838 0.1959 -0.0743 0.0081  0.0330  369  VAL B CG1 
11721 C CG2 . VAL B 371  ? 0.2463 0.2825 0.2050 -0.0703 0.0057  0.0286  369  VAL B CG2 
11722 N N   . LYS B 372  ? 0.2064 0.2724 0.1776 -0.0722 0.0115  0.0297  370  LYS B N   
11723 C CA  . LYS B 372  ? 0.2276 0.2965 0.2042 -0.0697 0.0111  0.0274  370  LYS B CA  
11724 C C   . LYS B 372  ? 0.2073 0.2668 0.1832 -0.0651 0.0092  0.0244  370  LYS B C   
11725 O O   . LYS B 372  ? 0.2208 0.2739 0.1969 -0.0660 0.0067  0.0237  370  LYS B O   
11726 C CB  . LYS B 372  ? 0.2213 0.3035 0.2031 -0.0673 0.0143  0.0270  370  LYS B CB  
11727 C CG  . LYS B 372  ? 0.2238 0.3153 0.2070 -0.0728 0.0156  0.0302  370  LYS B CG  
11728 C CD  . LYS B 372  ? 0.2254 0.3310 0.2139 -0.0708 0.0188  0.0302  370  LYS B CD  
11729 C CE  . LYS B 372  ? 0.2440 0.3586 0.2333 -0.0767 0.0202  0.0338  370  LYS B CE  
11730 N NZ  . LYS B 372  ? 0.2338 0.3628 0.2279 -0.0742 0.0237  0.0338  370  LYS B NZ  
11731 N N   . GLY B 373  ? 0.2091 0.2673 0.1838 -0.0604 0.0103  0.0226  371  GLY B N   
11732 C CA  . GLY B 373  ? 0.1955 0.2444 0.1689 -0.0565 0.0084  0.0201  371  GLY B CA  
11733 C C   . GLY B 373  ? 0.2086 0.2607 0.1838 -0.0507 0.0102  0.0176  371  GLY B C   
11734 O O   . GLY B 373  ? 0.2215 0.2825 0.2004 -0.0488 0.0124  0.0170  371  GLY B O   
11735 N N   . ALA B 374  ? 0.1875 0.2317 0.1597 -0.0477 0.0090  0.0162  372  ALA B N   
11736 C CA  . ALA B 374  ? 0.2087 0.2546 0.1811 -0.0428 0.0105  0.0141  372  ALA B CA  
11737 C C   . ALA B 374  ? 0.1980 0.2413 0.1735 -0.0385 0.0097  0.0112  372  ALA B C   
11738 O O   . ALA B 374  ? 0.2335 0.2778 0.2094 -0.0344 0.0107  0.0093  372  ALA B O   
11739 C CB  . ALA B 374  ? 0.2299 0.2698 0.1968 -0.0424 0.0099  0.0145  372  ALA B CB  
11740 N N   . TYR B 375  ? 0.1910 0.2308 0.1686 -0.0393 0.0079  0.0107  373  TYR B N   
11741 C CA  . TYR B 375  ? 0.1844 0.2204 0.1643 -0.0354 0.0069  0.0081  373  TYR B CA  
11742 C C   . TYR B 375  ? 0.1832 0.2245 0.1681 -0.0346 0.0074  0.0072  373  TYR B C   
11743 O O   . TYR B 375  ? 0.1893 0.2268 0.1759 -0.0329 0.0061  0.0057  373  TYR B O   
11744 C CB  . TYR B 375  ? 0.2026 0.2285 0.1800 -0.0360 0.0041  0.0079  373  TYR B CB  
11745 C CG  . TYR B 375  ? 0.2205 0.2404 0.1928 -0.0366 0.0031  0.0088  373  TYR B CG  
11746 C CD1 . TYR B 375  ? 0.2116 0.2308 0.1803 -0.0408 0.0029  0.0114  373  TYR B CD1 
11747 C CD2 . TYR B 375  ? 0.2408 0.2555 0.2118 -0.0332 0.0022  0.0071  373  TYR B CD2 
11748 C CE1 . TYR B 375  ? 0.2204 0.2339 0.1842 -0.0413 0.0019  0.0123  373  TYR B CE1 
11749 C CE2 . TYR B 375  ? 0.2700 0.2793 0.2364 -0.0336 0.0011  0.0080  373  TYR B CE2 
11750 C CZ  . TYR B 375  ? 0.2414 0.2499 0.2040 -0.0376 0.0010  0.0106  373  TYR B CZ  
11751 O OH  . TYR B 375  ? 0.2692 0.2721 0.2269 -0.0380 -0.0002 0.0115  373  TYR B OH  
11752 N N   . TRP B 376  ? 0.1845 0.2348 0.1718 -0.0358 0.0094  0.0082  374  TRP B N   
11753 C CA  . TRP B 376  ? 0.1703 0.2255 0.1620 -0.0361 0.0094  0.0080  374  TRP B CA  
11754 C C   . TRP B 376  ? 0.1795 0.2341 0.1742 -0.0315 0.0094  0.0054  374  TRP B C   
11755 O O   . TRP B 376  ? 0.1824 0.2341 0.1788 -0.0314 0.0080  0.0047  374  TRP B O   
11756 C CB  . TRP B 376  ? 0.1650 0.2309 0.1591 -0.0377 0.0116  0.0095  374  TRP B CB  
11757 C CG  . TRP B 376  ? 0.1946 0.2656 0.1933 -0.0382 0.0114  0.0093  374  TRP B CG  
11758 C CD1 . TRP B 376  ? 0.1755 0.2457 0.1749 -0.0422 0.0097  0.0105  374  TRP B CD1 
11759 C CD2 . TRP B 376  ? 0.1894 0.2665 0.1924 -0.0344 0.0127  0.0079  374  TRP B CD2 
11760 N NE1 . TRP B 376  ? 0.1731 0.2490 0.1770 -0.0412 0.0099  0.0099  374  TRP B NE1 
11761 C CE2 . TRP B 376  ? 0.1795 0.2598 0.1857 -0.0364 0.0118  0.0083  374  TRP B CE2 
11762 C CE3 . TRP B 376  ? 0.2199 0.3001 0.2240 -0.0295 0.0145  0.0062  374  TRP B CE3 
11763 C CZ2 . TRP B 376  ? 0.1694 0.2557 0.1799 -0.0335 0.0125  0.0073  374  TRP B CZ2 
11764 C CZ3 . TRP B 376  ? 0.2157 0.3015 0.2240 -0.0267 0.0153  0.0052  374  TRP B CZ3 
11765 C CH2 . TRP B 376  ? 0.2108 0.2999 0.2224 -0.0287 0.0143  0.0058  374  TRP B CH2 
11766 N N   . ASP B 377  ? 0.1886 0.2458 0.1839 -0.0276 0.0111  0.0041  375  ASP B N   
11767 C CA  A ASP B 377  ? 0.2168 0.2734 0.2147 -0.0233 0.0111  0.0018  375  ASP B CA  
11768 C CA  B ASP B 377  ? 0.2167 0.2735 0.2148 -0.0234 0.0111  0.0019  375  ASP B CA  
11769 C C   . ASP B 377  ? 0.1854 0.2330 0.1823 -0.0225 0.0089  0.0007  375  ASP B C   
11770 O O   . ASP B 377  ? 0.1909 0.2375 0.1903 -0.0209 0.0083  -0.0005 375  ASP B O   
11771 C CB  A ASP B 377  ? 0.2485 0.3070 0.2457 -0.0195 0.0128  0.0006  375  ASP B CB  
11772 C CB  B ASP B 377  ? 0.2536 0.3140 0.2519 -0.0194 0.0131  0.0006  375  ASP B CB  
11773 C CG  A ASP B 377  ? 0.3120 0.3800 0.3106 -0.0191 0.0153  0.0013  375  ASP B CG  
11774 C CG  B ASP B 377  ? 0.2656 0.3222 0.2596 -0.0190 0.0132  0.0006  375  ASP B CG  
11775 O OD1 A ASP B 377  ? 0.4015 0.4757 0.4039 -0.0196 0.0158  0.0018  375  ASP B OD1 
11776 O OD1 B ASP B 377  ? 0.3206 0.3693 0.3123 -0.0190 0.0114  0.0001  375  ASP B OD1 
11777 O OD2 A ASP B 377  ? 0.4347 0.5042 0.4309 -0.0181 0.0167  0.0013  375  ASP B OD2 
11778 O OD2 B ASP B 377  ? 0.3725 0.4341 0.3654 -0.0184 0.0152  0.0010  375  ASP B OD2 
11779 N N   . ALA B 378  ? 0.1800 0.2212 0.1730 -0.0235 0.0078  0.0010  376  ALA B N   
11780 C CA  . ALA B 378  ? 0.1687 0.2017 0.1607 -0.0224 0.0058  -0.0001 376  ALA B CA  
11781 C C   . ALA B 378  ? 0.1778 0.2080 0.1705 -0.0249 0.0042  0.0004  376  ALA B C   
11782 O O   . ALA B 378  ? 0.1803 0.2064 0.1741 -0.0232 0.0030  -0.0009 376  ALA B O   
11783 C CB  . ALA B 378  ? 0.2010 0.2283 0.1888 -0.0229 0.0049  0.0003  376  ALA B CB  
11784 N N   . GLU B 379  ? 0.1759 0.2082 0.1678 -0.0288 0.0040  0.0023  377  GLU B N   
11785 C CA  . GLU B 379  ? 0.1665 0.1958 0.1586 -0.0313 0.0023  0.0027  377  GLU B CA  
11786 C C   . GLU B 379  ? 0.1980 0.2317 0.1942 -0.0300 0.0027  0.0017  377  GLU B C   
11787 O O   . GLU B 379  ? 0.1803 0.2100 0.1769 -0.0299 0.0013  0.0009  377  GLU B O   
11788 C CB  . GLU B 379  ? 0.1842 0.2147 0.1742 -0.0363 0.0020  0.0050  377  GLU B CB  
11789 C CG  . GLU B 379  ? 0.2050 0.2303 0.1903 -0.0381 0.0013  0.0064  377  GLU B CG  
11790 C CD  . GLU B 379  ? 0.2323 0.2475 0.2146 -0.0377 -0.0011 0.0058  377  GLU B CD  
11791 O OE1 . GLU B 379  ? 0.2359 0.2474 0.2194 -0.0362 -0.0022 0.0043  377  GLU B OE1 
11792 O OE2 . GLU B 379  ? 0.2296 0.2404 0.2078 -0.0390 -0.0017 0.0069  377  GLU B OE2 
11793 N N   . ILE B 380  ? 0.1666 0.2085 0.1658 -0.0288 0.0047  0.0017  378  ILE B N   
11794 C CA  . ILE B 380  ? 0.1659 0.2119 0.1689 -0.0272 0.0050  0.0008  378  ILE B CA  
11795 C C   . ILE B 380  ? 0.1767 0.2180 0.1804 -0.0233 0.0045  -0.0013 378  ILE B C   
11796 O O   . ILE B 380  ? 0.1655 0.2048 0.1704 -0.0230 0.0035  -0.0020 378  ILE B O   
11797 C CB  . ILE B 380  ? 0.1614 0.2169 0.1673 -0.0260 0.0072  0.0011  378  ILE B CB  
11798 C CG1 . ILE B 380  ? 0.1654 0.2266 0.1710 -0.0300 0.0078  0.0033  378  ILE B CG1 
11799 C CG2 . ILE B 380  ? 0.1746 0.2340 0.1843 -0.0240 0.0073  0.0002  378  ILE B CG2 
11800 C CD1 . ILE B 380  ? 0.1838 0.2447 0.1897 -0.0342 0.0061  0.0045  378  ILE B CD1 
11801 N N   . LYS B 381  ? 0.1728 0.2125 0.1756 -0.0205 0.0052  -0.0022 379  LYS B N   
11802 C CA  . LYS B 381  ? 0.1539 0.1896 0.1576 -0.0170 0.0048  -0.0040 379  LYS B CA  
11803 C C   . LYS B 381  ? 0.1640 0.1923 0.1662 -0.0178 0.0029  -0.0044 379  LYS B C   
11804 O O   . LYS B 381  ? 0.1716 0.1981 0.1754 -0.0162 0.0024  -0.0055 379  LYS B O   
11805 C CB  . LYS B 381  ? 0.1675 0.2022 0.1700 -0.0145 0.0056  -0.0048 379  LYS B CB  
11806 C CG  . LYS B 381  ? 0.1766 0.2070 0.1799 -0.0113 0.0051  -0.0065 379  LYS B CG  
11807 C CD  . LYS B 381  ? 0.1573 0.1872 0.1594 -0.0090 0.0058  -0.0073 379  LYS B CD  
11808 C CE  . LYS B 381  ? 0.1857 0.2121 0.1892 -0.0061 0.0053  -0.0089 379  LYS B CE  
11809 N NZ  . LYS B 381  ? 0.1710 0.1964 0.1731 -0.0040 0.0057  -0.0098 379  LYS B NZ  
11810 N N   . ARG B 382  ? 0.1763 0.2002 0.1752 -0.0201 0.0018  -0.0035 380  ARG B N   
11811 C CA  A ARG B 382  ? 0.1711 0.1875 0.1682 -0.0203 -0.0001 -0.0039 380  ARG B CA  
11812 C CA  B ARG B 382  ? 0.1716 0.1880 0.1687 -0.0204 -0.0001 -0.0039 380  ARG B CA  
11813 C C   . ARG B 382  ? 0.1649 0.1806 0.1629 -0.0217 -0.0010 -0.0040 380  ARG B C   
11814 O O   . ARG B 382  ? 0.1808 0.1927 0.1793 -0.0201 -0.0018 -0.0052 380  ARG B O   
11815 C CB  A ARG B 382  ? 0.1987 0.2105 0.1919 -0.0226 -0.0011 -0.0028 380  ARG B CB  
11816 C CB  B ARG B 382  ? 0.1984 0.2104 0.1915 -0.0228 -0.0011 -0.0026 380  ARG B CB  
11817 C CG  A ARG B 382  ? 0.2446 0.2484 0.2357 -0.0226 -0.0032 -0.0032 380  ARG B CG  
11818 C CG  B ARG B 382  ? 0.2485 0.2524 0.2394 -0.0223 -0.0030 -0.0032 380  ARG B CG  
11819 C CD  A ARG B 382  ? 0.2148 0.2161 0.2073 -0.0188 -0.0033 -0.0049 380  ARG B CD  
11820 C CD  B ARG B 382  ? 0.3076 0.3095 0.2992 -0.0187 -0.0029 -0.0046 380  ARG B CD  
11821 N NE  A ARG B 382  ? 0.2726 0.2667 0.2631 -0.0184 -0.0052 -0.0053 380  ARG B NE  
11822 N NE  B ARG B 382  ? 0.2918 0.2923 0.2858 -0.0163 -0.0033 -0.0061 380  ARG B NE  
11823 C CZ  A ARG B 382  ? 0.3554 0.3450 0.3430 -0.0184 -0.0062 -0.0048 380  ARG B CZ  
11824 C CZ  B ARG B 382  ? 0.2953 0.2952 0.2909 -0.0133 -0.0031 -0.0073 380  ARG B CZ  
11825 N NH1 A ARG B 382  ? 0.3072 0.2983 0.2933 -0.0189 -0.0057 -0.0040 380  ARG B NH1 
11826 N NH1 B ARG B 382  ? 0.2572 0.2578 0.2523 -0.0121 -0.0026 -0.0074 380  ARG B NH1 
11827 N NH2 A ARG B 382  ? 0.3844 0.3677 0.3705 -0.0177 -0.0079 -0.0053 380  ARG B NH2 
11828 N NH2 B ARG B 382  ? 0.3091 0.3079 0.3068 -0.0115 -0.0033 -0.0085 380  ARG B NH2 
11829 N N   . ALA B 383  ? 0.1679 0.1875 0.1661 -0.0247 -0.0009 -0.0028 381  ALA B N   
11830 C CA  . ALA B 383  ? 0.1488 0.1678 0.1475 -0.0263 -0.0020 -0.0029 381  ALA B CA  
11831 C C   . ALA B 383  ? 0.1706 0.1927 0.1727 -0.0235 -0.0013 -0.0042 381  ALA B C   
11832 O O   . ALA B 383  ? 0.1788 0.1976 0.1808 -0.0230 -0.0023 -0.0050 381  ALA B O   
11833 C CB  . ALA B 383  ? 0.1733 0.1966 0.1718 -0.0304 -0.0020 -0.0011 381  ALA B CB  
11834 N N   . GLN B 384  ? 0.1594 0.1874 0.1641 -0.0214 0.0004  -0.0043 382  GLN B N   
11835 C CA  . GLN B 384  ? 0.1564 0.1869 0.1641 -0.0185 0.0011  -0.0055 382  GLN B CA  
11836 C C   . GLN B 384  ? 0.1640 0.1890 0.1714 -0.0157 0.0006  -0.0069 382  GLN B C   
11837 O O   . GLN B 384  ? 0.1815 0.2051 0.1898 -0.0146 0.0002  -0.0077 382  GLN B O   
11838 C CB  . GLN B 384  ? 0.1594 0.1968 0.1696 -0.0166 0.0029  -0.0054 382  GLN B CB  
11839 C CG  . GLN B 384  ? 0.1555 0.2000 0.1671 -0.0189 0.0035  -0.0041 382  GLN B CG  
11840 C CD  . GLN B 384  ? 0.1643 0.2157 0.1784 -0.0165 0.0053  -0.0041 382  GLN B CD  
11841 O OE1 . GLN B 384  ? 0.1980 0.2483 0.2120 -0.0136 0.0062  -0.0050 382  GLN B OE1 
11842 N NE2 . GLN B 384  ? 0.1574 0.2160 0.1738 -0.0177 0.0058  -0.0031 382  GLN B NE2 
11843 N N   . LEU B 385  ? 0.1604 0.1823 0.1665 -0.0145 0.0008  -0.0072 383  LEU B N   
11844 C CA  . LEU B 385  ? 0.1650 0.1821 0.1711 -0.0120 0.0003  -0.0084 383  LEU B CA  
11845 C C   . LEU B 385  ? 0.1812 0.1930 0.1859 -0.0128 -0.0012 -0.0088 383  LEU B C   
11846 O O   . LEU B 385  ? 0.1746 0.1844 0.1803 -0.0108 -0.0014 -0.0098 383  LEU B O   
11847 C CB  . LEU B 385  ? 0.1906 0.2050 0.1951 -0.0112 0.0002  -0.0085 383  LEU B CB  
11848 C CG  . LEU B 385  ? 0.2223 0.2405 0.2278 -0.0095 0.0017  -0.0087 383  LEU B CG  
11849 C CD1 . LEU B 385  ? 0.2292 0.2439 0.2324 -0.0093 0.0012  -0.0087 383  LEU B CD1 
11850 C CD2 . LEU B 385  ? 0.2588 0.2783 0.2670 -0.0065 0.0023  -0.0098 383  LEU B CD2 
11851 N N   . ASP B 386  ? 0.1854 0.1947 0.1874 -0.0157 -0.0023 -0.0079 384  ASP B N   
11852 C CA  . ASP B 386  ? 0.1733 0.1765 0.1732 -0.0163 -0.0039 -0.0083 384  ASP B CA  
11853 C C   . ASP B 386  ? 0.1911 0.1951 0.1913 -0.0174 -0.0043 -0.0085 384  ASP B C   
11854 O O   . ASP B 386  ? 0.2019 0.2009 0.2001 -0.0178 -0.0056 -0.0091 384  ASP B O   
11855 C CB  . ASP B 386  ? 0.2060 0.2047 0.2022 -0.0187 -0.0051 -0.0073 384  ASP B CB  
11856 C CG  . ASP B 386  ? 0.2555 0.2518 0.2508 -0.0172 -0.0051 -0.0073 384  ASP B CG  
11857 O OD1 . ASP B 386  ? 0.2640 0.2614 0.2614 -0.0143 -0.0043 -0.0083 384  ASP B OD1 
11858 O OD2 . ASP B 386  ? 0.2883 0.2814 0.2806 -0.0191 -0.0060 -0.0063 384  ASP B OD2 
11859 N N   . GLY B 387  ? 0.1654 0.1756 0.1679 -0.0179 -0.0034 -0.0081 385  GLY B N   
11860 C CA  . GLY B 387  ? 0.1798 0.1913 0.1827 -0.0189 -0.0039 -0.0084 385  GLY B CA  
11861 C C   . GLY B 387  ? 0.2031 0.2115 0.2030 -0.0225 -0.0056 -0.0077 385  GLY B C   
11862 O O   . GLY B 387  ? 0.2150 0.2204 0.2135 -0.0230 -0.0067 -0.0083 385  GLY B O   
11863 N N   . LEU B 388  ? 0.1980 0.2067 0.1965 -0.0252 -0.0058 -0.0063 386  LEU B N   
11864 C CA  . LEU B 388  ? 0.2063 0.2109 0.2014 -0.0289 -0.0075 -0.0056 386  LEU B CA  
11865 C C   . LEU B 388  ? 0.2079 0.2178 0.2041 -0.0320 -0.0078 -0.0047 386  LEU B C   
11866 O O   . LEU B 388  ? 0.2037 0.2210 0.2033 -0.0312 -0.0065 -0.0044 386  LEU B O   
11867 C CB  . LEU B 388  ? 0.2060 0.2074 0.1985 -0.0305 -0.0079 -0.0044 386  LEU B CB  
11868 C CG  . LEU B 388  ? 0.2009 0.1967 0.1923 -0.0274 -0.0080 -0.0054 386  LEU B CG  
11869 C CD1 . LEU B 388  ? 0.2373 0.2296 0.2258 -0.0289 -0.0085 -0.0042 386  LEU B CD1 
11870 C CD2 . LEU B 388  ? 0.2437 0.2329 0.2333 -0.0260 -0.0094 -0.0069 386  LEU B CD2 
11871 N N   . ALA B 389  ? 0.2115 0.2174 0.2046 -0.0355 -0.0096 -0.0041 387  ALA B N   
11872 C CA  . ALA B 389  ? 0.2091 0.2192 0.2031 -0.0385 -0.0103 -0.0036 387  ALA B CA  
11873 C C   . ALA B 389  ? 0.2094 0.2285 0.2064 -0.0405 -0.0091 -0.0018 387  ALA B C   
11874 O O   . ALA B 389  ? 0.2486 0.2744 0.2484 -0.0411 -0.0088 -0.0015 387  ALA B O   
11875 C CB  . ALA B 389  ? 0.2729 0.2761 0.2626 -0.0422 -0.0128 -0.0033 387  ALA B CB  
11876 N N   . ASP B 390  ? 0.2106 0.2299 0.2067 -0.0416 -0.0084 -0.0006 388  ASP B N   
11877 C CA  . ASP B 390  ? 0.1915 0.2193 0.1901 -0.0435 -0.0071 0.0012  388  ASP B CA  
11878 C C   . ASP B 390  ? 0.1773 0.2037 0.1746 -0.0427 -0.0060 0.0018  388  ASP B C   
11879 O O   . ASP B 390  ? 0.1993 0.2184 0.1941 -0.0409 -0.0065 0.0010  388  ASP B O   
11880 C CB  . ASP B 390  ? 0.2067 0.2360 0.2043 -0.0490 -0.0085 0.0028  388  ASP B CB  
11881 C CG  . ASP B 390  ? 0.2243 0.2648 0.2259 -0.0506 -0.0072 0.0043  388  ASP B CG  
11882 O OD1 . ASP B 390  ? 0.2146 0.2606 0.2182 -0.0491 -0.0051 0.0049  388  ASP B OD1 
11883 O OD2 . ASP B 390  ? 0.2804 0.3242 0.2831 -0.0534 -0.0084 0.0048  388  ASP B OD2 
11884 N N   . PHE B 391  ? 0.1831 0.2167 0.1821 -0.0441 -0.0045 0.0033  389  PHE B N   
11885 C CA  . PHE B 391  ? 0.1711 0.2039 0.1684 -0.0439 -0.0034 0.0042  389  PHE B CA  
11886 C C   . PHE B 391  ? 0.1886 0.2161 0.1817 -0.0484 -0.0050 0.0059  389  PHE B C   
11887 O O   . PHE B 391  ? 0.2093 0.2368 0.2017 -0.0524 -0.0063 0.0069  389  PHE B O   
11888 C CB  . PHE B 391  ? 0.1902 0.2332 0.1908 -0.0434 -0.0011 0.0051  389  PHE B CB  
11889 C CG  . PHE B 391  ? 0.1666 0.2144 0.1711 -0.0390 0.0003  0.0036  389  PHE B CG  
11890 C CD1 . PHE B 391  ? 0.1705 0.2152 0.1748 -0.0347 0.0010  0.0020  389  PHE B CD1 
11891 C CD2 . PHE B 391  ? 0.1814 0.2363 0.1895 -0.0392 0.0005  0.0037  389  PHE B CD2 
11892 C CE1 . PHE B 391  ? 0.1711 0.2193 0.1786 -0.0307 0.0021  0.0007  389  PHE B CE1 
11893 C CE2 . PHE B 391  ? 0.1773 0.2358 0.1885 -0.0350 0.0016  0.0023  389  PHE B CE2 
11894 C CZ  . PHE B 391  ? 0.1668 0.2218 0.1776 -0.0308 0.0024  0.0008  389  PHE B CZ  
11895 N N   . PRO B 392  ? 0.1832 0.2058 0.1733 -0.0478 -0.0049 0.0062  390  PRO B N   
11896 C CA  . PRO B 392  ? 0.1743 0.1921 0.1602 -0.0522 -0.0062 0.0081  390  PRO B CA  
11897 C C   . PRO B 392  ? 0.1980 0.2231 0.1844 -0.0549 -0.0046 0.0104  390  PRO B C   
11898 O O   . PRO B 392  ? 0.2047 0.2265 0.1875 -0.0586 -0.0053 0.0123  390  PRO B O   
11899 C CB  . PRO B 392  ? 0.2034 0.2128 0.1859 -0.0495 -0.0068 0.0073  390  PRO B CB  
11900 C CG  . PRO B 392  ? 0.2011 0.2154 0.1867 -0.0449 -0.0047 0.0060  390  PRO B CG  
11901 C CD  . PRO B 392  ? 0.1828 0.2033 0.1729 -0.0433 -0.0039 0.0048  390  PRO B CD  
11902 N N   . VAL B 393  ? 0.1985 0.2333 0.1892 -0.0530 -0.0023 0.0102  391  VAL B N   
11903 C CA  . VAL B 393  ? 0.1994 0.2428 0.1913 -0.0551 -0.0004 0.0122  391  VAL B CA  
11904 C C   . VAL B 393  ? 0.1899 0.2432 0.1867 -0.0557 0.0005  0.0124  391  VAL B C   
11905 O O   . VAL B 393  ? 0.1787 0.2323 0.1780 -0.0534 0.0000  0.0107  391  VAL B O   
11906 C CB  . VAL B 393  ? 0.2008 0.2466 0.1926 -0.0514 0.0018  0.0117  391  VAL B CB  
11907 C CG1 . VAL B 393  ? 0.1855 0.2218 0.1724 -0.0510 0.0008  0.0117  391  VAL B CG1 
11908 C CG2 . VAL B 393  ? 0.1931 0.2416 0.1885 -0.0461 0.0029  0.0093  391  VAL B CG2 
11909 N N   . PHE B 394  ? 0.1821 0.2438 0.1803 -0.0587 0.0019  0.0145  392  PHE B N   
11910 C CA  . PHE B 394  ? 0.1739 0.2464 0.1772 -0.0588 0.0031  0.0148  392  PHE B CA  
11911 C C   . PHE B 394  ? 0.1849 0.2628 0.1915 -0.0529 0.0053  0.0130  392  PHE B C   
11912 O O   . PHE B 394  ? 0.1890 0.2637 0.1938 -0.0495 0.0063  0.0120  392  PHE B O   
11913 C CB  . PHE B 394  ? 0.1783 0.2589 0.1824 -0.0636 0.0040  0.0177  392  PHE B CB  
11914 C CG  . PHE B 394  ? 0.1833 0.2581 0.1840 -0.0697 0.0016  0.0195  392  PHE B CG  
11915 C CD1 . PHE B 394  ? 0.2068 0.2797 0.2083 -0.0722 -0.0007 0.0192  392  PHE B CD1 
11916 C CD2 . PHE B 394  ? 0.1960 0.2663 0.1924 -0.0727 0.0015  0.0213  392  PHE B CD2 
11917 C CE1 . PHE B 394  ? 0.2085 0.2750 0.2064 -0.0777 -0.0031 0.0207  392  PHE B CE1 
11918 C CE2 . PHE B 394  ? 0.1934 0.2573 0.1862 -0.0782 -0.0009 0.0229  392  PHE B CE2 
11919 C CZ  . PHE B 394  ? 0.2269 0.2888 0.2205 -0.0807 -0.0033 0.0226  392  PHE B CZ  
11920 N N   . THR B 395  ? 0.1822 0.2678 0.1934 -0.0517 0.0058  0.0126  393  THR B N   
11921 C CA  . THR B 395  ? 0.1733 0.2642 0.1877 -0.0462 0.0077  0.0110  393  THR B CA  
11922 C C   . THR B 395  ? 0.1565 0.2598 0.1747 -0.0460 0.0101  0.0122  393  THR B C   
11923 O O   . THR B 395  ? 0.1879 0.2954 0.2082 -0.0413 0.0119  0.0110  393  THR B O   
11924 C CB  . THR B 395  ? 0.1793 0.2686 0.1960 -0.0436 0.0065  0.0092  393  THR B CB  
11925 O OG1 . THR B 395  ? 0.1910 0.2855 0.2102 -0.0469 0.0054  0.0103  393  THR B OG1 
11926 C CG2 . THR B 395  ? 0.1955 0.2730 0.2087 -0.0430 0.0045  0.0077  393  THR B CG2 
11927 N N   . ARG B 396  ? 0.1784 0.2877 0.1975 -0.0510 0.0101  0.0146  394  ARG B N   
11928 C CA  . ARG B 396  ? 0.1964 0.3180 0.2189 -0.0511 0.0125  0.0161  394  ARG B CA  
11929 C C   . ARG B 396  ? 0.1928 0.3144 0.2120 -0.0542 0.0136  0.0180  394  ARG B C   
11930 O O   . ARG B 396  ? 0.2026 0.3186 0.2186 -0.0592 0.0119  0.0195  394  ARG B O   
11931 C CB  . ARG B 396  ? 0.1921 0.3226 0.2189 -0.0545 0.0118  0.0176  394  ARG B CB  
11932 C CG  . ARG B 396  ? 0.2141 0.3458 0.2442 -0.0514 0.0108  0.0159  394  ARG B CG  
11933 C CD  . ARG B 396  ? 0.2458 0.3883 0.2806 -0.0544 0.0104  0.0175  394  ARG B CD  
11934 N NE  . ARG B 396  ? 0.2683 0.4104 0.3055 -0.0524 0.0088  0.0161  394  ARG B NE  
11935 C CZ  . ARG B 396  ? 0.3110 0.4628 0.3531 -0.0498 0.0095  0.0159  394  ARG B CZ  
11936 N NH1 . ARG B 396  ? 0.3278 0.4915 0.3736 -0.0493 0.0118  0.0173  394  ARG B NH1 
11937 N NH2 . ARG B 396  ? 0.2861 0.4358 0.3295 -0.0476 0.0080  0.0145  394  ARG B NH2 
11938 N N   . LYS B 397  ? 0.1945 0.3222 0.2142 -0.0513 0.0165  0.0180  395  LYS B N   
11939 C CA  . LYS B 397  ? 0.2103 0.3376 0.2264 -0.0536 0.0177  0.0197  395  LYS B CA  
11940 C C   . LYS B 397  ? 0.1969 0.3300 0.2137 -0.0603 0.0175  0.0229  395  LYS B C   
11941 O O   . LYS B 397  ? 0.2245 0.3529 0.2372 -0.0644 0.0169  0.0247  395  LYS B O   
11942 C CB  . LYS B 397  ? 0.2516 0.3852 0.2683 -0.0489 0.0209  0.0189  395  LYS B CB  
11943 C CG  . LYS B 397  ? 0.2414 0.3724 0.2533 -0.0499 0.0222  0.0200  395  LYS B CG  
11944 C CD  . LYS B 397  ? 0.2614 0.4027 0.2745 -0.0538 0.0241  0.0229  395  LYS B CD  
11945 C CE  . LYS B 397  ? 0.2595 0.3981 0.2673 -0.0546 0.0255  0.0239  395  LYS B CE  
11946 N NZ  . LYS B 397  ? 0.2445 0.3934 0.2533 -0.0589 0.0275  0.0270  395  LYS B NZ  
11947 N N   . ILE B 398  ? 0.2227 0.3660 0.2448 -0.0615 0.0178  0.0238  396  ILE B N   
11948 C CA  . ILE B 398  ? 0.2639 0.4135 0.2872 -0.0682 0.0174  0.0269  396  ILE B CA  
11949 C C   . ILE B 398  ? 0.1718 0.3110 0.1916 -0.0735 0.0140  0.0277  396  ILE B C   
11950 O O   . ILE B 398  ? 0.2239 0.3637 0.2421 -0.0796 0.0134  0.0304  396  ILE B O   
11951 C CB  . ILE B 398  ? 0.2690 0.4319 0.2992 -0.0678 0.0182  0.0273  396  ILE B CB  
11952 C CG1 . ILE B 398  ? 0.3373 0.5097 0.3695 -0.0741 0.0187  0.0308  396  ILE B CG1 
11953 C CG2 . ILE B 398  ? 0.2490 0.4079 0.2811 -0.0673 0.0154  0.0258  396  ILE B CG2 
11954 C CD1 . ILE B 398  ? 0.3501 0.5379 0.3892 -0.0728 0.0205  0.0314  396  ILE B CD1 
11955 N N   . HIS B 399  ? 0.2048 0.3339 0.2231 -0.0713 0.0117  0.0254  397  HIS B N   
11956 C CA  . HIS B 399  ? 0.2013 0.3197 0.2157 -0.0757 0.0084  0.0258  397  HIS B CA  
11957 C C   . HIS B 399  ? 0.1945 0.3037 0.2028 -0.0775 0.0082  0.0267  397  HIS B C   
11958 O O   . HIS B 399  ? 0.2214 0.3258 0.2265 -0.0831 0.0064  0.0287  397  HIS B O   
11959 C CB  . HIS B 399  ? 0.1999 0.3103 0.2141 -0.0723 0.0064  0.0230  397  HIS B CB  
11960 C CG  . HIS B 399  ? 0.2190 0.3368 0.2384 -0.0716 0.0059  0.0223  397  HIS B CG  
11961 N ND1 . HIS B 399  ? 0.2103 0.3236 0.2305 -0.0679 0.0046  0.0198  397  HIS B ND1 
11962 C CD2 . HIS B 399  ? 0.2377 0.3673 0.2618 -0.0741 0.0065  0.0240  397  HIS B CD2 
11963 C CE1 . HIS B 399  ? 0.2336 0.3552 0.2585 -0.0681 0.0043  0.0199  397  HIS B CE1 
11964 N NE2 . HIS B 399  ? 0.2379 0.3696 0.2654 -0.0718 0.0054  0.0224  397  HIS B NE2 
11965 N N   . THR B 400  ? 0.2041 0.3104 0.2105 -0.0726 0.0098  0.0252  398  THR B N   
11966 C CA  . THR B 400  ? 0.2039 0.3027 0.2046 -0.0740 0.0098  0.0262  398  THR B CA  
11967 C C   . THR B 400  ? 0.1800 0.2858 0.1801 -0.0789 0.0113  0.0296  398  THR B C   
11968 O O   . THR B 400  ? 0.2285 0.3278 0.2239 -0.0834 0.0100  0.0315  398  THR B O   
11969 C CB  . THR B 400  ? 0.2007 0.2971 0.2001 -0.0677 0.0114  0.0241  398  THR B CB  
11970 O OG1 . THR B 400  ? 0.1902 0.2782 0.1893 -0.0642 0.0096  0.0213  398  THR B OG1 
11971 C CG2 . THR B 400  ? 0.2328 0.3233 0.2266 -0.0689 0.0117  0.0253  398  THR B CG2 
11972 N N   . ASP B 401  ? 0.2128 0.3321 0.2175 -0.0783 0.0140  0.0304  399  ASP B N   
11973 C CA  . ASP B 401  ? 0.2404 0.3678 0.2451 -0.0830 0.0157  0.0337  399  ASP B CA  
11974 C C   . ASP B 401  ? 0.1963 0.3227 0.2007 -0.0905 0.0133  0.0363  399  ASP B C   
11975 O O   . ASP B 401  ? 0.2309 0.3553 0.2318 -0.0957 0.0130  0.0391  399  ASP B O   
11976 C CB  . ASP B 401  ? 0.2544 0.3971 0.2647 -0.0805 0.0190  0.0339  399  ASP B CB  
11977 C CG  . ASP B 401  ? 0.3189 0.4628 0.3284 -0.0739 0.0217  0.0319  399  ASP B CG  
11978 O OD1 . ASP B 401  ? 0.2757 0.4104 0.2798 -0.0727 0.0215  0.0314  399  ASP B OD1 
11979 O OD2 . ASP B 401  ? 0.2789 0.4328 0.2930 -0.0698 0.0239  0.0309  399  ASP B OD2 
11980 N N   . VAL B 402  ? 0.2104 0.3380 0.2185 -0.0913 0.0114  0.0354  400  VAL B N   
11981 C CA  . VAL B 402  ? 0.2375 0.3632 0.2451 -0.0984 0.0087  0.0375  400  VAL B CA  
11982 C C   . VAL B 402  ? 0.1891 0.2991 0.1898 -0.1009 0.0058  0.0376  400  VAL B C   
11983 O O   . VAL B 402  ? 0.2344 0.3414 0.2320 -0.1073 0.0045  0.0404  400  VAL B O   
11984 C CB  . VAL B 402  ? 0.2249 0.3546 0.2374 -0.0981 0.0070  0.0362  400  VAL B CB  
11985 C CG1 . VAL B 402  ? 0.2800 0.4054 0.2911 -0.1053 0.0037  0.0380  400  VAL B CG1 
11986 C CG2 . VAL B 402  ? 0.2512 0.3974 0.2707 -0.0963 0.0098  0.0367  400  VAL B CG2 
11987 N N   . SER B 403  ? 0.2233 0.3231 0.2215 -0.0959 0.0047  0.0347  401  SER B N   
11988 C CA  . SER B 403  ? 0.2621 0.3469 0.2538 -0.0973 0.0021  0.0345  401  SER B CA  
11989 C C   . SER B 403  ? 0.2019 0.2842 0.1888 -0.0998 0.0031  0.0369  401  SER B C   
11990 O O   . SER B 403  ? 0.2401 0.3142 0.2223 -0.1048 0.0009  0.0388  401  SER B O   
11991 C CB  . SER B 403  ? 0.2251 0.3017 0.2157 -0.0907 0.0015  0.0309  401  SER B CB  
11992 O OG  . SER B 403  ? 0.2336 0.2964 0.2181 -0.0915 -0.0008 0.0307  401  SER B OG  
11993 N N   . TYR B 404  ? 0.2407 0.3297 0.2285 -0.0964 0.0063  0.0369  402  TYR B N   
11994 C CA  . TYR B 404  ? 0.2513 0.3386 0.2344 -0.0985 0.0074  0.0393  402  TYR B CA  
11995 C C   . TYR B 404  ? 0.2319 0.3242 0.2148 -0.1063 0.0074  0.0432  402  TYR B C   
11996 O O   . TYR B 404  ? 0.2576 0.3421 0.2349 -0.1107 0.0059  0.0455  402  TYR B O   
11997 C CB  . TYR B 404  ? 0.2483 0.3438 0.2331 -0.0934 0.0111  0.0384  402  TYR B CB  
11998 C CG  . TYR B 404  ? 0.2321 0.3243 0.2114 -0.0940 0.0123  0.0401  402  TYR B CG  
11999 C CD1 . TYR B 404  ? 0.2704 0.3686 0.2484 -0.0993 0.0137  0.0437  402  TYR B CD1 
12000 C CD2 . TYR B 404  ? 0.2361 0.3194 0.2114 -0.0893 0.0120  0.0381  402  TYR B CD2 
12001 C CE1 . TYR B 404  ? 0.2704 0.3656 0.2430 -0.0998 0.0149  0.0453  402  TYR B CE1 
12002 C CE2 . TYR B 404  ? 0.2415 0.3217 0.2115 -0.0898 0.0129  0.0396  402  TYR B CE2 
12003 C CZ  . TYR B 404  ? 0.2776 0.3637 0.2461 -0.0950 0.0144  0.0432  402  TYR B CZ  
12004 O OH  . TYR B 404  ? 0.2839 0.3671 0.2468 -0.0956 0.0153  0.0448  402  TYR B OH  
12005 N N   . ILE B 405  ? 0.2732 0.3786 0.2620 -0.1081 0.0088  0.0442  403  ILE B N   
12006 C CA  . ILE B 405  ? 0.2801 0.3919 0.2693 -0.1156 0.0089  0.0481  403  ILE B CA  
12007 C C   . ILE B 405  ? 0.2475 0.3492 0.2337 -0.1216 0.0049  0.0492  403  ILE B C   
12008 O O   . ILE B 405  ? 0.2870 0.3852 0.2692 -0.1279 0.0039  0.0524  403  ILE B O   
12009 C CB  . ILE B 405  ? 0.2917 0.4207 0.2886 -0.1157 0.0114  0.0488  403  ILE B CB  
12010 C CG1 . ILE B 405  ? 0.3060 0.4442 0.3046 -0.1102 0.0156  0.0481  403  ILE B CG1 
12011 C CG2 . ILE B 405  ? 0.2831 0.4189 0.2811 -0.1240 0.0112  0.0529  403  ILE B CG2 
12012 C CD1 . ILE B 405  ? 0.3982 0.5527 0.4046 -0.1081 0.0181  0.0479  403  ILE B CD1 
12013 N N   . ALA B 406  ? 0.2641 0.3602 0.2515 -0.1197 0.0023  0.0465  404  ALA B N   
12014 C CA  . ALA B 406  ? 0.2996 0.3848 0.2834 -0.1247 -0.0017 0.0471  404  ALA B CA  
12015 C C   . ALA B 406  ? 0.2750 0.3451 0.2510 -0.1254 -0.0035 0.0475  404  ALA B C   
12016 O O   . ALA B 406  ? 0.3134 0.3763 0.2850 -0.1316 -0.0060 0.0498  404  ALA B O   
12017 C CB  . ALA B 406  ? 0.2686 0.3505 0.2549 -0.1213 -0.0037 0.0437  404  ALA B CB  
12018 N N   . CYS B 407  ? 0.2581 0.3230 0.2319 -0.1191 -0.0025 0.0453  405  CYS B N   
12019 C CA  . CYS B 407  ? 0.2986 0.3496 0.2651 -0.1190 -0.0042 0.0456  405  CYS B CA  
12020 C C   . CYS B 407  ? 0.2549 0.3079 0.2179 -0.1232 -0.0028 0.0493  405  CYS B C   
12021 O O   . CYS B 407  ? 0.3125 0.3546 0.2692 -0.1269 -0.0050 0.0511  405  CYS B O   
12022 C CB  . CYS B 407  ? 0.2601 0.3060 0.2260 -0.1111 -0.0036 0.0421  405  CYS B CB  
12023 S SG  . CYS B 407  ? 0.3279 0.3674 0.2959 -0.1071 -0.0062 0.0381  405  CYS B SG  
12024 N N   . ALA B 408  ? 0.2809 0.3475 0.2477 -0.1228 0.0009  0.0506  406  ALA B N   
12025 C CA  . ALA B 408  ? 0.3068 0.3769 0.2706 -0.1275 0.0025  0.0544  406  ALA B CA  
12026 C C   . ALA B 408  ? 0.2794 0.3488 0.2420 -0.1363 0.0004  0.0579  406  ALA B C   
12027 O O   . ALA B 408  ? 0.3449 0.4082 0.3019 -0.1410 -0.0004 0.0609  406  ALA B O   
12028 C CB  . ALA B 408  ? 0.3281 0.4143 0.2969 -0.1253 0.0069  0.0549  406  ALA B CB  
12029 N N   . ALA B 409  ? 0.3116 0.3867 0.2794 -0.1386 -0.0006 0.0575  407  ALA B N   
12030 C CA  . ALA B 409  ? 0.3446 0.4177 0.3112 -0.1450 -0.0033 0.0597  407  ALA B CA  
12031 C C   . ALA B 409  ? 0.3114 0.3666 0.2706 -0.1476 -0.0073 0.0598  407  ALA B C   
12032 O O   . ALA B 409  ? 0.3826 0.4324 0.3373 -0.1519 -0.0090 0.0621  407  ALA B O   
12033 C CB  . ALA B 409  ? 0.3067 0.3881 0.2799 -0.1453 -0.0040 0.0584  407  ALA B CB  
12034 N N   . LYS B 410  ? 0.3262 0.3717 0.2838 -0.1441 -0.0089 0.0570  408  LYS B N   
12035 C CA  . LYS B 410  ? 0.3107 0.3387 0.2610 -0.1454 -0.0127 0.0567  408  LYS B CA  
12036 C C   . LYS B 410  ? 0.3673 0.3883 0.3111 -0.1458 -0.0123 0.0588  408  LYS B C   
12037 O O   . LYS B 410  ? 0.3877 0.3982 0.3254 -0.1498 -0.0149 0.0607  408  LYS B O   
12038 C CB  . LYS B 410  ? 0.3302 0.3504 0.2807 -0.1385 -0.0142 0.0522  408  LYS B CB  
12039 C CG  . LYS B 410  ? 0.3613 0.3636 0.3047 -0.1391 -0.0182 0.0514  408  LYS B CG  
12040 C CD  . LYS B 410  ? 0.3827 0.3782 0.3264 -0.1317 -0.0191 0.0470  408  LYS B CD  
12041 C CE  . LYS B 410  ? 0.3812 0.3819 0.3303 -0.1305 -0.0197 0.0445  408  LYS B CE  
12042 N NZ  . LYS B 410  ? 0.3997 0.3925 0.3460 -0.1359 -0.0234 0.0449  408  LYS B NZ  
12043 N N   . LEU B 411  ? 0.3533 0.3796 0.2981 -0.1404 -0.0091 0.0580  409  LEU B N   
12044 C CA  . LEU B 411  ? 0.3771 0.3972 0.3156 -0.1404 -0.0086 0.0599  409  LEU B CA  
12045 C C   . LEU B 411  ? 0.3779 0.4031 0.3146 -0.1475 -0.0077 0.0646  409  LEU B C   
12046 O O   . LEU B 411  ? 0.3681 0.3833 0.2982 -0.1499 -0.0095 0.0665  409  LEU B O   
12047 C CB  . LEU B 411  ? 0.3328 0.3582 0.2730 -0.1330 -0.0055 0.0578  409  LEU B CB  
12048 C CG  . LEU B 411  ? 0.3478 0.3642 0.2874 -0.1257 -0.0069 0.0536  409  LEU B CG  
12049 C CD1 . LEU B 411  ? 0.3367 0.3610 0.2796 -0.1189 -0.0037 0.0513  409  LEU B CD1 
12050 C CD2 . LEU B 411  ? 0.3434 0.3438 0.2751 -0.1259 -0.0099 0.0541  409  LEU B CD2 
12051 N N   . LEU B 412  ? 0.3687 0.4093 0.3117 -0.1484 -0.0051 0.0652  410  LEU B N   
12052 C CA  . LEU B 412  ? 0.3360 0.3823 0.2782 -0.1525 -0.0043 0.0683  410  LEU B CA  
12053 C C   . LEU B 412  ? 0.3589 0.3966 0.2977 -0.1579 -0.0083 0.0697  410  LEU B C   
12054 O O   . LEU B 412  ? 0.4171 0.4534 0.3523 -0.1617 -0.0086 0.0725  410  LEU B O   
12055 C CB  . LEU B 412  ? 0.4007 0.4654 0.3506 -0.1518 -0.0008 0.0685  410  LEU B CB  
12056 C CG  . LEU B 412  ? 0.3720 0.4462 0.3241 -0.1469 0.0037  0.0679  410  LEU B CG  
12057 C CD1 . LEU B 412  ? 0.4497 0.5413 0.4101 -0.1452 0.0067  0.0673  410  LEU B CD1 
12058 C CD2 . LEU B 412  ? 0.4189 0.4911 0.3653 -0.1478 0.0051  0.0704  410  LEU B CD2 
12059 N N   . ALA B 413  ? 0.3905 0.4223 0.3302 -0.1583 -0.0112 0.0677  411  ALA B N   
12060 C CA  . ALA B 413  ? 0.4249 0.4466 0.3605 -0.1629 -0.0153 0.0686  411  ALA B CA  
12061 C C   . ALA B 413  ? 0.4409 0.4448 0.3680 -0.1627 -0.0182 0.0687  411  ALA B C   
12062 O O   . ALA B 413  ? 0.4591 0.4530 0.3816 -0.1662 -0.0217 0.0695  411  ALA B O   
12063 C CB  . ALA B 413  ? 0.4153 0.4373 0.3547 -0.1631 -0.0175 0.0663  411  ALA B CB  
12064 N N   . ALA B 414  ? 0.3845 0.3840 0.3092 -0.1586 -0.0170 0.0679  412  ALA B N   
12065 C CA  . ALA B 414  ? 0.3586 0.3413 0.2754 -0.1577 -0.0198 0.0679  412  ALA B CA  
12066 C C   . ALA B 414  ? 0.4307 0.4123 0.3431 -0.1568 -0.0179 0.0700  412  ALA B C   
12067 O O   . ALA B 414  ? 0.4310 0.4008 0.3379 -0.1542 -0.0193 0.0695  412  ALA B O   
12068 C CB  . ALA B 414  ? 0.4301 0.4047 0.3468 -0.1531 -0.0211 0.0644  412  ALA B CB  
12069 N N   . THR B 415  ? 0.4028 0.3966 0.3175 -0.1587 -0.0148 0.0724  413  THR B N   
12070 C CA  . THR B 415  ? 0.3999 0.3936 0.3105 -0.1576 -0.0128 0.0743  413  THR B CA  
12071 C C   . THR B 415  ? 0.4120 0.3912 0.3141 -0.1600 -0.0160 0.0763  413  THR B C   
12072 O O   . THR B 415  ? 0.4275 0.4025 0.3247 -0.1583 -0.0153 0.0774  413  THR B O   
12073 C CB  . THR B 415  ? 0.3916 0.4013 0.3062 -0.1591 -0.0089 0.0763  413  THR B CB  
12074 O OG1 . THR B 415  ? 0.4444 0.4560 0.3590 -0.1648 -0.0102 0.0786  413  THR B OG1 
12075 C CG2 . THR B 415  ? 0.4209 0.4453 0.3439 -0.1561 -0.0057 0.0743  413  THR B CG2 
12076 N N   . ASP B 416  ? 0.4605 0.4319 0.3604 -0.1638 -0.0196 0.0767  414  ASP B N   
12077 C CA  . ASP B 416  ? 0.4569 0.4132 0.3486 -0.1655 -0.0230 0.0781  414  ASP B CA  
12078 C C   . ASP B 416  ? 0.4315 0.3734 0.3187 -0.1610 -0.0254 0.0758  414  ASP B C   
12079 O O   . ASP B 416  ? 0.5154 0.4444 0.3955 -0.1612 -0.0280 0.0768  414  ASP B O   
12080 C CB  . ASP B 416  ? 0.4181 0.3704 0.3087 -0.1707 -0.0261 0.0790  414  ASP B CB  
12081 N N   . VAL B 417  ? 0.4378 0.3816 0.3291 -0.1569 -0.0246 0.0728  415  VAL B N   
12082 C CA  . VAL B 417  ? 0.3955 0.3259 0.2835 -0.1527 -0.0273 0.0702  415  VAL B CA  
12083 C C   . VAL B 417  ? 0.4169 0.3499 0.3061 -0.1475 -0.0249 0.0690  415  VAL B C   
12084 O O   . VAL B 417  ? 0.4046 0.3261 0.2891 -0.1439 -0.0266 0.0680  415  VAL B O   
12085 C CB  . VAL B 417  ? 0.4640 0.3926 0.3554 -0.1528 -0.0294 0.0675  415  VAL B CB  
12086 C CG1 . VAL B 417  ? 0.3939 0.3093 0.2824 -0.1481 -0.0319 0.0646  415  VAL B CG1 
12087 C CG2 . VAL B 417  ? 0.4563 0.3815 0.3458 -0.1580 -0.0320 0.0688  415  VAL B CG2 
12088 N N   . VAL B 418  ? 0.3829 0.3308 0.2783 -0.1468 -0.0209 0.0688  416  VAL B N   
12089 C CA  . VAL B 418  ? 0.3696 0.3226 0.2677 -0.1393 -0.0184 0.0660  416  VAL B CA  
12090 C C   . VAL B 418  ? 0.3919 0.3586 0.2920 -0.1406 -0.0143 0.0683  416  VAL B C   
12091 O O   . VAL B 418  ? 0.3675 0.3419 0.2689 -0.1469 -0.0130 0.0715  416  VAL B O   
12092 C CB  . VAL B 418  ? 0.3646 0.3224 0.2697 -0.1337 -0.0179 0.0614  416  VAL B CB  
12093 C CG1 . VAL B 418  ? 0.3447 0.2886 0.2473 -0.1313 -0.0218 0.0588  416  VAL B CG1 
12094 C CG2 . VAL B 418  ? 0.3652 0.3356 0.2769 -0.1375 -0.0163 0.0618  416  VAL B CG2 
12095 N N   . PHE B 419  ? 0.3479 0.3177 0.2483 -0.1346 -0.0122 0.0667  417  PHE B N   
12096 C CA  . PHE B 419  ? 0.3432 0.3259 0.2453 -0.1348 -0.0080 0.0683  417  PHE B CA  
12097 C C   . PHE B 419  ? 0.3229 0.3176 0.2330 -0.1293 -0.0052 0.0646  417  PHE B C   
12098 O O   . PHE B 419  ? 0.3132 0.3060 0.2242 -0.1224 -0.0050 0.0613  417  PHE B O   
12099 C CB  . PHE B 419  ? 0.3690 0.3463 0.2648 -0.1320 -0.0078 0.0692  417  PHE B CB  
12100 C CG  . PHE B 419  ? 0.3626 0.3524 0.2595 -0.1314 -0.0035 0.0704  417  PHE B CG  
12101 C CD1 . PHE B 419  ? 0.3703 0.3696 0.2678 -0.1375 -0.0012 0.0741  417  PHE B CD1 
12102 C CD2 . PHE B 419  ? 0.3670 0.3591 0.2642 -0.1245 -0.0019 0.0677  417  PHE B CD2 
12103 C CE1 . PHE B 419  ? 0.3764 0.3875 0.2747 -0.1365 0.0029  0.0751  417  PHE B CE1 
12104 C CE2 . PHE B 419  ? 0.3497 0.3527 0.2474 -0.1236 0.0020  0.0686  417  PHE B CE2 
12105 C CZ  . PHE B 419  ? 0.3406 0.3533 0.2388 -0.1294 0.0045  0.0722  417  PHE B CZ  
12106 N N   . PRO B 420  ? 0.3206 0.3275 0.2368 -0.1321 -0.0032 0.0651  418  PRO B N   
12107 C CA  . PRO B 420  ? 0.2834 0.3009 0.2072 -0.1267 -0.0009 0.0616  418  PRO B CA  
12108 C C   . PRO B 420  ? 0.3005 0.3275 0.2252 -0.1227 0.0030  0.0612  418  PRO B C   
12109 O O   . PRO B 420  ? 0.3013 0.3340 0.2237 -0.1260 0.0052  0.0644  418  PRO B O   
12110 C CB  . PRO B 420  ? 0.3232 0.3507 0.2525 -0.1318 -0.0002 0.0630  418  PRO B CB  
12111 C CG  . PRO B 420  ? 0.3295 0.3481 0.2541 -0.1393 -0.0033 0.0663  418  PRO B CG  
12112 C CD  . PRO B 420  ? 0.3134 0.3240 0.2301 -0.1402 -0.0036 0.0687  418  PRO B CD  
12113 N N   . GLN B 421  ? 0.2982 0.3265 0.2259 -0.1155 0.0038  0.0573  419  GLN B N   
12114 C CA  . GLN B 421  ? 0.3089 0.3451 0.2373 -0.1107 0.0072  0.0561  419  GLN B CA  
12115 C C   . GLN B 421  ? 0.2793 0.3258 0.2155 -0.1064 0.0092  0.0530  419  GLN B C   
12116 O O   . GLN B 421  ? 0.2628 0.3049 0.2015 -0.1019 0.0078  0.0495  419  GLN B O   
12117 C CB  . GLN B 421  ? 0.2843 0.3101 0.2077 -0.1058 0.0058  0.0544  419  GLN B CB  
12118 C CG  . GLN B 421  ? 0.2942 0.3085 0.2096 -0.1098 0.0033  0.0575  419  GLN B CG  
12119 C CD  . GLN B 421  ? 0.2983 0.3005 0.2095 -0.1051 0.0008  0.0554  419  GLN B CD  
12120 O OE1 . GLN B 421  ? 0.3127 0.3087 0.2259 -0.1019 -0.0015 0.0525  419  GLN B OE1 
12121 N NE2 . GLN B 421  ? 0.2929 0.2919 0.1982 -0.1045 0.0011  0.0569  419  GLN B NE2 
12122 N N   . PHE B 422  ? 0.2845 0.3449 0.2249 -0.1079 0.0126  0.0543  420  PHE B N   
12123 C CA  . PHE B 422  ? 0.2465 0.3174 0.1945 -0.1046 0.0143  0.0518  420  PHE B CA  
12124 C C   . PHE B 422  ? 0.2494 0.3257 0.1984 -0.0978 0.0172  0.0492  420  PHE B C   
12125 O O   . PHE B 422  ? 0.2704 0.3568 0.2199 -0.0977 0.0206  0.0504  420  PHE B O   
12126 C CB  . PHE B 422  ? 0.2747 0.3576 0.2270 -0.1101 0.0160  0.0545  420  PHE B CB  
12127 C CG  . PHE B 422  ? 0.3074 0.3843 0.2586 -0.1171 0.0129  0.0570  420  PHE B CG  
12128 C CD1 . PHE B 422  ? 0.3180 0.3884 0.2712 -0.1167 0.0098  0.0549  420  PHE B CD1 
12129 C CD2 . PHE B 422  ? 0.3124 0.3898 0.2600 -0.1240 0.0129  0.0613  420  PHE B CD2 
12130 C CE1 . PHE B 422  ? 0.3382 0.4025 0.2898 -0.1230 0.0068  0.0569  420  PHE B CE1 
12131 C CE2 . PHE B 422  ? 0.3488 0.4199 0.2948 -0.1306 0.0098  0.0635  420  PHE B CE2 
12132 C CZ  . PHE B 422  ? 0.3356 0.4000 0.2836 -0.1300 0.0067  0.0612  420  PHE B CZ  
12133 N N   . ALA B 423  ? 0.2479 0.3173 0.1972 -0.0921 0.0158  0.0456  421  ALA B N   
12134 C CA  . ALA B 423  ? 0.2632 0.3360 0.2133 -0.0854 0.0179  0.0427  421  ALA B CA  
12135 C C   . ALA B 423  ? 0.2503 0.3343 0.2079 -0.0825 0.0200  0.0407  421  ALA B C   
12136 O O   . ALA B 423  ? 0.2890 0.3709 0.2505 -0.0812 0.0183  0.0387  421  ALA B O   
12137 C CB  . ALA B 423  ? 0.2447 0.3054 0.1923 -0.0810 0.0153  0.0398  421  ALA B CB  
12138 N N   . THR B 424  ? 0.2955 0.3912 0.2550 -0.0813 0.0236  0.0412  422  THR B N   
12139 C CA  . THR B 424  ? 0.2552 0.3616 0.2215 -0.0778 0.0257  0.0392  422  THR B CA  
12140 C C   . THR B 424  ? 0.2502 0.3671 0.2164 -0.0752 0.0298  0.0394  422  THR B C   
12141 O O   . THR B 424  ? 0.2837 0.4033 0.2461 -0.0783 0.0313  0.0422  422  THR B O   
12142 C CB  . THR B 424  ? 0.2990 0.4124 0.2706 -0.0825 0.0254  0.0410  422  THR B CB  
12143 O OG1 . THR B 424  ? 0.2756 0.3992 0.2539 -0.0785 0.0272  0.0390  422  THR B OG1 
12144 C CG2 . THR B 424  ? 0.2949 0.4155 0.2654 -0.0888 0.0270  0.0452  422  THR B CG2 
12145 N N   . HIS B 425  ? 0.2631 0.3853 0.2331 -0.0692 0.0314  0.0363  423  HIS B N   
12146 C CA  . HIS B 425  ? 0.2682 0.4014 0.2391 -0.0660 0.0354  0.0360  423  HIS B CA  
12147 C C   . HIS B 425  ? 0.2883 0.4353 0.2662 -0.0665 0.0375  0.0367  423  HIS B C   
12148 O O   . HIS B 425  ? 0.3033 0.4606 0.2829 -0.0634 0.0410  0.0362  423  HIS B O   
12149 C CB  . HIS B 425  ? 0.2773 0.4070 0.2470 -0.0586 0.0359  0.0321  423  HIS B CB  
12150 C CG  . HIS B 425  ? 0.2673 0.3849 0.2301 -0.0577 0.0341  0.0315  423  HIS B CG  
12151 N ND1 . HIS B 425  ? 0.3072 0.4154 0.2692 -0.0534 0.0320  0.0283  423  HIS B ND1 
12152 C CD2 . HIS B 425  ? 0.2925 0.4059 0.2490 -0.0607 0.0340  0.0337  423  HIS B CD2 
12153 C CE1 . HIS B 425  ? 0.3025 0.4017 0.2582 -0.0536 0.0306  0.0285  423  HIS B CE1 
12154 N NE2 . HIS B 425  ? 0.2838 0.3857 0.2358 -0.0579 0.0318  0.0318  423  HIS B NE2 
12155 N N   . ASN B 426  ? 0.2885 0.4360 0.2706 -0.0703 0.0355  0.0377  424  ASN B N   
12156 C CA  . ASN B 426  ? 0.2793 0.4394 0.2686 -0.0707 0.0369  0.0381  424  ASN B CA  
12157 C C   . ASN B 426  ? 0.2964 0.4657 0.2864 -0.0772 0.0385  0.0423  424  ASN B C   
12158 O O   . ASN B 426  ? 0.2785 0.4428 0.2666 -0.0836 0.0363  0.0449  424  ASN B O   
12159 C CB  . ASN B 426  ? 0.2755 0.4307 0.2686 -0.0715 0.0336  0.0369  424  ASN B CB  
12160 C CG  . ASN B 426  ? 0.2873 0.4547 0.2880 -0.0705 0.0348  0.0366  424  ASN B CG  
12161 O OD1 . ASN B 426  ? 0.3007 0.4801 0.3044 -0.0735 0.0369  0.0391  424  ASN B OD1 
12162 N ND2 . ASN B 426  ? 0.2996 0.4642 0.3035 -0.0663 0.0334  0.0337  424  ASN B ND2 
12163 N N   . ALA B 427  ? 0.3139 0.4967 0.3064 -0.0755 0.0424  0.0430  425  ALA B N   
12164 C CA  . ALA B 427  ? 0.3225 0.5155 0.3157 -0.0815 0.0443  0.0471  425  ALA B CA  
12165 C C   . ALA B 427  ? 0.2588 0.4552 0.2576 -0.0863 0.0420  0.0487  425  ALA B C   
12166 O O   . ALA B 427  ? 0.2968 0.4934 0.2948 -0.0920 0.0410  0.0516  425  ALA B O   
12167 C CB  . ALA B 427  ? 0.3444 0.5488 0.3397 -0.0767 0.0481  0.0464  425  ALA B CB  
12168 N N   . GLN B 428  ? 0.2761 0.4747 0.2804 -0.0840 0.0410  0.0466  426  GLN B N   
12169 C CA  . GLN B 428  ? 0.3127 0.5131 0.3216 -0.0885 0.0383  0.0479  426  GLN B CA  
12170 C C   . GLN B 428  ? 0.2978 0.4860 0.3024 -0.0948 0.0348  0.0495  426  GLN B C   
12171 O O   . GLN B 428  ? 0.2839 0.4715 0.2885 -0.1007 0.0329  0.0520  426  GLN B O   
12172 C CB  . GLN B 428  ? 0.2942 0.4996 0.3096 -0.0842 0.0379  0.0453  426  GLN B CB  
12173 C CG  . GLN B 428  ? 0.3095 0.5203 0.3304 -0.0878 0.0358  0.0465  426  GLN B CG  
12174 C CD  . GLN B 428  ? 0.3094 0.5104 0.3286 -0.0937 0.0319  0.0474  426  GLN B CD  
12175 O OE1 . GLN B 428  ? 0.3300 0.5203 0.3460 -0.0929 0.0303  0.0459  426  GLN B OE1 
12176 N NE2 . GLN B 428  ? 0.3352 0.5384 0.3561 -0.0992 0.0299  0.0497  426  GLN B NE2 
12177 N N   . THR B 429  ? 0.2997 0.4742 0.3000 -0.0918 0.0327  0.0470  427  THR B N   
12178 C CA  . THR B 429  ? 0.3301 0.4905 0.3257 -0.0963 0.0289  0.0478  427  THR B CA  
12179 C C   . THR B 429  ? 0.2780 0.4364 0.2682 -0.1022 0.0293  0.0516  427  THR B C   
12180 O O   . THR B 429  ? 0.2886 0.4431 0.2774 -0.1090 0.0270  0.0542  427  THR B O   
12181 C CB  . THR B 429  ? 0.2655 0.4124 0.2572 -0.0909 0.0271  0.0444  427  THR B CB  
12182 O OG1 . THR B 429  ? 0.2723 0.4220 0.2688 -0.0849 0.0273  0.0410  427  THR B OG1 
12183 C CG2 . THR B 429  ? 0.3347 0.4675 0.3224 -0.0948 0.0230  0.0448  427  THR B CG2 
12184 N N   . LEU B 430  ? 0.3114 0.4721 0.2981 -0.0997 0.0322  0.0519  428  LEU B N   
12185 C CA  . LEU B 430  ? 0.2853 0.4445 0.2665 -0.1049 0.0329  0.0555  428  LEU B CA  
12186 C C   . LEU B 430  ? 0.2969 0.4643 0.2815 -0.1098 0.0328  0.0583  428  LEU B C   
12187 O O   . LEU B 430  ? 0.3057 0.4667 0.2870 -0.1158 0.0305  0.0608  428  LEU B O   
12188 C CB  . LEU B 430  ? 0.3405 0.5030 0.3183 -0.1002 0.0363  0.0548  428  LEU B CB  
12189 C CG  . LEU B 430  ? 0.3671 0.5260 0.3376 -0.1034 0.0373  0.0577  428  LEU B CG  
12190 C CD1 . LEU B 430  ? 0.3434 0.5045 0.3111 -0.0970 0.0403  0.0557  428  LEU B CD1 
12191 C CD2 . LEU B 430  ? 0.3972 0.5629 0.3693 -0.1078 0.0377  0.0607  428  LEU B CD2 
12192 N N   . ALA B 431  ? 0.3583 0.5391 0.3494 -0.1069 0.0351  0.0575  429  ALA B N   
12193 C CA  . ALA B 431  ? 0.3377 0.5268 0.3323 -0.1108 0.0350  0.0598  429  ALA B CA  
12194 C C   . ALA B 431  ? 0.3427 0.5269 0.3389 -0.1165 0.0310  0.0609  429  ALA B C   
12195 O O   . ALA B 431  ? 0.3670 0.5507 0.3619 -0.1223 0.0296  0.0637  429  ALA B O   
12196 C CB  . ALA B 431  ? 0.3498 0.5536 0.3515 -0.1060 0.0378  0.0584  429  ALA B CB  
12197 N N   . ALA B 432  ? 0.3394 0.5195 0.3378 -0.1151 0.0290  0.0587  430  ALA B N   
12198 C CA  . ALA B 432  ? 0.3045 0.4790 0.3038 -0.1201 0.0251  0.0594  430  ALA B CA  
12199 C C   . ALA B 432  ? 0.3407 0.5017 0.3327 -0.1257 0.0224  0.0615  430  ALA B C   
12200 O O   . ALA B 432  ? 0.3610 0.5198 0.3524 -0.1314 0.0199  0.0636  430  ALA B O   
12201 C CB  . ALA B 432  ? 0.3285 0.5002 0.3308 -0.1171 0.0237  0.0565  430  ALA B CB  
12202 N N   . ILE B 433  ? 0.3482 0.4997 0.3343 -0.1241 0.0227  0.0610  431  ILE B N   
12203 C CA  . ILE B 433  ? 0.3742 0.5118 0.3529 -0.1289 0.0199  0.0629  431  ILE B CA  
12204 C C   . ILE B 433  ? 0.3045 0.4444 0.2801 -0.1325 0.0209  0.0661  431  ILE B C   
12205 O O   . ILE B 433  ? 0.3327 0.4650 0.3045 -0.1380 0.0181  0.0683  431  ILE B O   
12206 C CB  . ILE B 433  ? 0.3306 0.4574 0.3040 -0.1258 0.0198  0.0614  431  ILE B CB  
12207 C CG1 . ILE B 433  ? 0.4032 0.5254 0.3797 -0.1218 0.0177  0.0577  431  ILE B CG1 
12208 C CG2 . ILE B 433  ? 0.3982 0.5108 0.3634 -0.1301 0.0171  0.0636  431  ILE B CG2 
12209 C CD1 . ILE B 433  ? 0.4198 0.5306 0.3922 -0.1156 0.0169  0.0546  431  ILE B CD1 
12210 N N   . TYR B 434  ? 0.3495 0.4992 0.3261 -0.1292 0.0247  0.0662  432  TYR B N   
12211 C CA  . TYR B 434  ? 0.3197 0.4728 0.2937 -0.1323 0.0260  0.0692  432  TYR B CA  
12212 C C   . TYR B 434  ? 0.3492 0.5070 0.3264 -0.1378 0.0244  0.0714  432  TYR B C   
12213 O O   . TYR B 434  ? 0.3577 0.5101 0.3306 -0.1432 0.0228  0.0742  432  TYR B O   
12214 C CB  . TYR B 434  ? 0.3799 0.5448 0.3560 -0.1270 0.0306  0.0684  432  TYR B CB  
12215 C CG  . TYR B 434  ? 0.3518 0.5237 0.3269 -0.1296 0.0326  0.0712  432  TYR B CG  
12216 C CD1 . TYR B 434  ? 0.3858 0.5502 0.3535 -0.1320 0.0326  0.0734  432  TYR B CD1 
12217 C CD2 . TYR B 434  ? 0.3699 0.5560 0.3514 -0.1293 0.0346  0.0718  432  TYR B CD2 
12218 C CE1 . TYR B 434  ? 0.4230 0.5939 0.3897 -0.1343 0.0346  0.0760  432  TYR B CE1 
12219 C CE2 . TYR B 434  ? 0.3761 0.5690 0.3568 -0.1316 0.0366  0.0744  432  TYR B CE2 
12220 C CZ  . TYR B 434  ? 0.4148 0.6001 0.3881 -0.1342 0.0366  0.0765  432  TYR B CZ  
12221 O OH  . TYR B 434  ? 0.4161 0.6083 0.3887 -0.1365 0.0386  0.0791  432  TYR B OH  
12222 N N   . HIS B 435  ? 0.3839 0.5511 0.3684 -0.1368 0.0244  0.0702  433  HIS B N   
12223 C CA  . HIS B 435  ? 0.4089 0.5809 0.3965 -0.1420 0.0227  0.0722  433  HIS B CA  
12224 C C   . HIS B 435  ? 0.3661 0.5261 0.3513 -0.1467 0.0180  0.0724  433  HIS B C   
12225 O O   . HIS B 435  ? 0.3923 0.5496 0.3757 -0.1526 0.0158  0.0749  433  HIS B O   
12226 C CB  . HIS B 435  ? 0.4313 0.6185 0.4273 -0.1390 0.0246  0.0711  433  HIS B CB  
12227 C CG  . HIS B 435  ? 0.3919 0.5913 0.3899 -0.1359 0.0289  0.0717  433  HIS B CG  
12228 N ND1 . HIS B 435  ? 0.3847 0.5904 0.3825 -0.1398 0.0299  0.0747  433  HIS B ND1 
12229 C CD2 . HIS B 435  ? 0.3757 0.5817 0.3755 -0.1292 0.0324  0.0696  433  HIS B CD2 
12230 C CE1 . HIS B 435  ? 0.4636 0.6794 0.4632 -0.1356 0.0339  0.0745  433  HIS B CE1 
12231 N NE2 . HIS B 435  ? 0.3458 0.5618 0.3465 -0.1290 0.0355  0.0713  433  HIS B NE2 
12232 N N   . MET B 436  ? 0.3619 0.5143 0.3468 -0.1440 0.0164  0.0698  434  MET B N   
12233 C CA  . MET B 436  ? 0.3710 0.5106 0.3528 -0.1480 0.0120  0.0697  434  MET B CA  
12234 C C   . MET B 436  ? 0.3447 0.4719 0.3185 -0.1525 0.0100  0.0721  434  MET B C   
12235 O O   . MET B 436  ? 0.4175 0.5368 0.3887 -0.1575 0.0064  0.0732  434  MET B O   
12236 C CB  . MET B 436  ? 0.3719 0.5045 0.3538 -0.1439 0.0110  0.0665  434  MET B CB  
12237 C CG  . MET B 436  ? 0.3923 0.5106 0.3703 -0.1472 0.0065  0.0661  434  MET B CG  
12238 S SD  . MET B 436  ? 0.4516 0.5618 0.4291 -0.1420 0.0060  0.0625  434  MET B SD  
12239 C CE  . MET B 436  ? 0.3775 0.5019 0.3647 -0.1385 0.0073  0.0602  434  MET B CE  
12240 N N   . ALA B 437  ? 0.3534 0.4784 0.3228 -0.1507 0.0121  0.0728  435  ALA B N   
12241 C CA  . ALA B 437  ? 0.3953 0.5082 0.3568 -0.1545 0.0103  0.0751  435  ALA B CA  
12242 C C   . ALA B 437  ? 0.4495 0.5667 0.4104 -0.1600 0.0101  0.0784  435  ALA B C   
12243 O O   . ALA B 437  ? 0.4502 0.5569 0.4048 -0.1642 0.0078  0.0805  435  ALA B O   
12244 C CB  . ALA B 437  ? 0.4256 0.5353 0.3825 -0.1507 0.0127  0.0749  435  ALA B CB  
12245 N N   . GLY B 438  ? 0.4547 0.5871 0.4220 -0.1600 0.0125  0.0791  436  GLY B N   
12246 C CA  . GLY B 438  ? 0.4091 0.5466 0.3764 -0.1654 0.0124  0.0823  436  GLY B CA  
12247 C C   . GLY B 438  ? 0.5254 0.6659 0.4893 -0.1655 0.0153  0.0845  436  GLY B C   
12248 O O   . GLY B 438  ? 0.4982 0.6379 0.4598 -0.1610 0.0177  0.0835  436  GLY B O   
12249 N N   . LYS B 439  ? 0.4720 0.6158 0.4352 -0.1709 0.0149  0.0877  437  LYS B N   
12250 C CA  . LYS B 439  ? 0.4676 0.6164 0.4283 -0.1715 0.0179  0.0901  437  LYS B CA  
12251 C C   . LYS B 439  ? 0.4930 0.6273 0.4445 -0.1732 0.0164  0.0915  437  LYS B C   
12252 O O   . LYS B 439  ? 0.5840 0.7205 0.5325 -0.1718 0.0192  0.0927  437  LYS B O   
12253 C CB  . LYS B 439  ? 0.4674 0.6260 0.4312 -0.1767 0.0182  0.0931  437  LYS B CB  
12254 N N   . ASP B 440  ? 0.4486 0.5682 0.3956 -0.1761 0.0121  0.0915  438  ASP B N   
12255 C CA  . ASP B 440  ? 0.5135 0.6190 0.4517 -0.1781 0.0103  0.0931  438  ASP B CA  
12256 C C   . ASP B 440  ? 0.5218 0.6199 0.4566 -0.1724 0.0110  0.0908  438  ASP B C   
12257 O O   . ASP B 440  ? 0.5560 0.6498 0.4924 -0.1694 0.0097  0.0879  438  ASP B O   
12258 C CB  . ASP B 440  ? 0.5132 0.6054 0.4476 -0.1832 0.0052  0.0938  438  ASP B CB  
12259 N N   . PHE B 441  ? 0.4656 0.5626 0.3957 -0.1710 0.0131  0.0920  439  PHE B N   
12260 C CA  . PHE B 441  ? 0.4281 0.5181 0.3544 -0.1657 0.0138  0.0900  439  PHE B CA  
12261 C C   . PHE B 441  ? 0.4747 0.5565 0.3927 -0.1666 0.0137  0.0922  439  PHE B C   
12262 O O   . PHE B 441  ? 0.4584 0.5455 0.3751 -0.1693 0.0154  0.0949  439  PHE B O   
12263 C CB  . PHE B 441  ? 0.4350 0.5374 0.3665 -0.1595 0.0180  0.0875  439  PHE B CB  
12264 C CG  . PHE B 441  ? 0.4452 0.5400 0.3725 -0.1542 0.0184  0.0854  439  PHE B CG  
12265 C CD1 . PHE B 441  ? 0.4016 0.4887 0.3294 -0.1519 0.0162  0.0828  439  PHE B CD1 
12266 C CD2 . PHE B 441  ? 0.4182 0.5131 0.3406 -0.1518 0.0208  0.0862  439  PHE B CD2 
12267 C CE1 . PHE B 441  ? 0.3977 0.4777 0.3216 -0.1473 0.0164  0.0810  439  PHE B CE1 
12268 C CE2 . PHE B 441  ? 0.4145 0.5021 0.3328 -0.1471 0.0209  0.0843  439  PHE B CE2 
12269 C CZ  . PHE B 441  ? 0.4178 0.4981 0.3369 -0.1450 0.0186  0.0818  439  PHE B CZ  
12270 N N   . HIS B 442  ? 0.4758 0.5444 0.3882 -0.1641 0.0118  0.0910  440  HIS B N   
12271 C CA  . HIS B 442  ? 0.4571 0.5179 0.3616 -0.1633 0.0120  0.0925  440  HIS B CA  
12272 C C   . HIS B 442  ? 0.4311 0.4853 0.3332 -0.1575 0.0119  0.0897  440  HIS B C   
12273 O O   . HIS B 442  ? 0.4381 0.4896 0.3432 -0.1555 0.0105  0.0871  440  HIS B O   
12274 C CB  . HIS B 442  ? 0.4603 0.5072 0.3582 -0.1683 0.0079  0.0950  440  HIS B CB  
12275 C CG  . HIS B 442  ? 0.5238 0.5582 0.4208 -0.1691 0.0035  0.0934  440  HIS B CG  
12276 N ND1 . HIS B 442  ? 0.5497 0.5716 0.4422 -0.1655 0.0014  0.0916  440  HIS B ND1 
12277 C CD2 . HIS B 442  ? 0.5270 0.5597 0.4268 -0.1728 0.0008  0.0933  440  HIS B CD2 
12278 C CE1 . HIS B 442  ? 0.5234 0.5365 0.4162 -0.1669 -0.0023 0.0904  440  HIS B CE1 
12279 N NE2 . HIS B 442  ? 0.5575 0.5767 0.4545 -0.1713 -0.0028 0.0914  440  HIS B NE2 
12280 N N   . VAL B 443  ? 0.4290 0.4807 0.3256 -0.1549 0.0134  0.0903  441  VAL B N   
12281 C CA  . VAL B 443  ? 0.4550 0.4986 0.3480 -0.1498 0.0128  0.0880  441  VAL B CA  
12282 C C   . VAL B 443  ? 0.4160 0.4427 0.3045 -0.1514 0.0078  0.0879  441  VAL B C   
12283 O O   . VAL B 443  ? 0.4307 0.4486 0.3144 -0.1555 0.0051  0.0904  441  VAL B O   
12284 C CB  . VAL B 443  ? 0.4896 0.5329 0.3766 -0.1471 0.0149  0.0889  441  VAL B CB  
12285 C CG1 . VAL B 443  ? 0.4636 0.4957 0.3455 -0.1427 0.0132  0.0870  441  VAL B CG1 
12286 C CG2 . VAL B 443  ? 0.4721 0.5318 0.3638 -0.1441 0.0200  0.0880  441  VAL B CG2 
12287 N N   . GLY B 444  ? 0.4259 0.4482 0.3161 -0.1480 0.0065  0.0851  442  GLY B N   
12288 C CA  . GLY B 444  ? 0.4155 0.4227 0.3025 -0.1490 0.0020  0.0845  442  GLY B CA  
12289 C C   . GLY B 444  ? 0.4308 0.4392 0.3236 -0.1512 0.0002  0.0832  442  GLY B C   
12290 O O   . GLY B 444  ? 0.3957 0.3924 0.2867 -0.1510 -0.0033 0.0820  442  GLY B O   
12291 N N   . LYS B 445  ? 0.4037 0.4259 0.3033 -0.1533 0.0025  0.0835  443  LYS B N   
12292 C CA  . LYS B 445  ? 0.3830 0.4072 0.2883 -0.1551 0.0010  0.0822  443  LYS B CA  
12293 C C   . LYS B 445  ? 0.4013 0.4286 0.3113 -0.1502 0.0020  0.0787  443  LYS B C   
12294 O O   . LYS B 445  ? 0.3903 0.4091 0.3004 -0.1497 -0.0009 0.0769  443  LYS B O   
12295 C CB  . LYS B 445  ? 0.3750 0.4129 0.2860 -0.1588 0.0029  0.0837  443  LYS B CB  
12296 C CG  . LYS B 445  ? 0.4036 0.4432 0.3198 -0.1612 0.0008  0.0826  443  LYS B CG  
12297 C CD  . LYS B 445  ? 0.4792 0.5314 0.4002 -0.1653 0.0022  0.0846  443  LYS B CD  
12298 C CE  . LYS B 445  ? 0.5378 0.5914 0.4636 -0.1677 -0.0001 0.0835  443  LYS B CE  
12299 N NZ  . LYS B 445  ? 0.5132 0.5785 0.4433 -0.1720 0.0009  0.0857  443  LYS B NZ  
12300 N N   . TYR B 446  ? 0.3471 0.3865 0.2607 -0.1464 0.0061  0.0777  444  TYR B N   
12301 C CA  . TYR B 446  ? 0.3509 0.3936 0.2682 -0.1413 0.0075  0.0745  444  TYR B CA  
12302 C C   . TYR B 446  ? 0.3389 0.3914 0.2564 -0.1372 0.0118  0.0742  444  TYR B C   
12303 O O   . TYR B 446  ? 0.3364 0.3945 0.2524 -0.1385 0.0138  0.0763  444  TYR B O   
12304 C CB  . TYR B 446  ? 0.3523 0.4036 0.2779 -0.1417 0.0077  0.0728  444  TYR B CB  
12305 C CG  . TYR B 446  ? 0.4202 0.4881 0.3520 -0.1425 0.0109  0.0737  444  TYR B CG  
12306 C CD1 . TYR B 446  ? 0.3447 0.4254 0.2811 -0.1379 0.0150  0.0721  444  TYR B CD1 
12307 C CD2 . TYR B 446  ? 0.3669 0.4376 0.2999 -0.1479 0.0098  0.0759  444  TYR B CD2 
12308 C CE1 . TYR B 446  ? 0.4556 0.5512 0.3976 -0.1382 0.0179  0.0728  444  TYR B CE1 
12309 C CE2 . TYR B 446  ? 0.4225 0.5084 0.3613 -0.1486 0.0127  0.0768  444  TYR B CE2 
12310 C CZ  . TYR B 446  ? 0.4006 0.4989 0.3438 -0.1436 0.0167  0.0752  444  TYR B CZ  
12311 O OH  . TYR B 446  ? 0.5045 0.6178 0.4534 -0.1439 0.0195  0.0759  444  TYR B OH  
12312 N N   . GLU B 447  ? 0.3326 0.3863 0.2529 -0.1300 0.0126  0.0702  445  GLU B N   
12313 C CA  . GLU B 447  ? 0.3328 0.3959 0.2540 -0.1251 0.0165  0.0689  445  GLU B CA  
12314 C C   . GLU B 447  ? 0.2830 0.3535 0.2117 -0.1190 0.0179  0.0646  445  GLU B C   
12315 O O   . GLU B 447  ? 0.2865 0.3528 0.2187 -0.1178 0.0155  0.0623  445  GLU B O   
12316 C CB  . GLU B 447  ? 0.3098 0.3633 0.2239 -0.1212 0.0158  0.0682  445  GLU B CB  
12317 C CG  . GLU B 447  ? 0.2787 0.3211 0.1927 -0.1157 0.0127  0.0643  445  GLU B CG  
12318 C CD  . GLU B 447  ? 0.2969 0.3295 0.2038 -0.1125 0.0115  0.0639  445  GLU B CD  
12319 O OE1 . GLU B 447  ? 0.3300 0.3626 0.2313 -0.1152 0.0126  0.0670  445  GLU B OE1 
12320 O OE2 . GLU B 447  ? 0.3043 0.3294 0.2115 -0.1072 0.0095  0.0604  445  GLU B OE2 
12321 N N   . PHE B 448  ? 0.3015 0.3827 0.2322 -0.1150 0.0217  0.0636  446  PHE B N   
12322 C CA  . PHE B 448  ? 0.2804 0.3666 0.2167 -0.1080 0.0229  0.0592  446  PHE B CA  
12323 C C   . PHE B 448  ? 0.2458 0.3236 0.1777 -0.1018 0.0222  0.0564  446  PHE B C   
12324 O O   . PHE B 448  ? 0.2919 0.3627 0.2169 -0.1027 0.0216  0.0580  446  PHE B O   
12325 C CB  . PHE B 448  ? 0.3439 0.4468 0.2852 -0.1068 0.0274  0.0594  446  PHE B CB  
12326 C CG  . PHE B 448  ? 0.3009 0.4134 0.2475 -0.1123 0.0280  0.0618  446  PHE B CG  
12327 C CD1 . PHE B 448  ? 0.3362 0.4518 0.2896 -0.1112 0.0269  0.0597  446  PHE B CD1 
12328 C CD2 . PHE B 448  ? 0.3283 0.4466 0.2732 -0.1187 0.0294  0.0662  446  PHE B CD2 
12329 C CE1 . PHE B 448  ? 0.3017 0.4263 0.2602 -0.1165 0.0272  0.0620  446  PHE B CE1 
12330 C CE2 . PHE B 448  ? 0.3712 0.4968 0.3220 -0.1222 0.0290  0.0673  446  PHE B CE2 
12331 C CZ  . PHE B 448  ? 0.3339 0.4630 0.2912 -0.1215 0.0280  0.0654  446  PHE B CZ  
12332 N N   . GLN B 449  ? 0.2800 0.3583 0.2160 -0.0956 0.0222  0.0522  447  GLN B N   
12333 C CA  . GLN B 449  ? 0.2589 0.3308 0.1918 -0.0894 0.0218  0.0493  447  GLN B CA  
12334 C C   . GLN B 449  ? 0.2552 0.3362 0.1932 -0.0833 0.0245  0.0459  447  GLN B C   
12335 O O   . GLN B 449  ? 0.2615 0.3504 0.2060 -0.0830 0.0255  0.0450  447  GLN B O   
12336 C CB  . GLN B 449  ? 0.2578 0.3156 0.1888 -0.0879 0.0176  0.0474  447  GLN B CB  
12337 C CG  . GLN B 449  ? 0.2675 0.3150 0.1932 -0.0934 0.0146  0.0505  447  GLN B CG  
12338 C CD  . GLN B 449  ? 0.2742 0.3079 0.1964 -0.0905 0.0111  0.0486  447  GLN B CD  
12339 O OE1 . GLN B 449  ? 0.3176 0.3498 0.2426 -0.0850 0.0106  0.0450  447  GLN B OE1 
12340 N NE2 . GLN B 449  ? 0.2717 0.2953 0.1877 -0.0941 0.0085  0.0512  447  GLN B NE2 
12341 N N   . CYS B 450  ? 0.2587 0.3383 0.1934 -0.0785 0.0256  0.0440  448  CYS B N   
12342 C CA  . CYS B 450  ? 0.2431 0.3294 0.1817 -0.0723 0.0278  0.0405  448  CYS B CA  
12343 C C   . CYS B 450  ? 0.2507 0.3284 0.1852 -0.0671 0.0265  0.0378  448  CYS B C   
12344 O O   . CYS B 450  ? 0.2714 0.3396 0.2000 -0.0684 0.0244  0.0388  448  CYS B O   
12345 C CB  . CYS B 450  ? 0.2691 0.3689 0.2087 -0.0721 0.0322  0.0416  448  CYS B CB  
12346 S SG  . CYS B 450  ? 0.2990 0.3980 0.2301 -0.0719 0.0341  0.0432  448  CYS B SG  
12347 N N   . LEU B 451  ? 0.2598 0.3410 0.1974 -0.0613 0.0278  0.0343  449  LEU B N   
12348 C CA  . LEU B 451  ? 0.2712 0.3454 0.2056 -0.0562 0.0267  0.0313  449  LEU B CA  
12349 C C   . LEU B 451  ? 0.3099 0.3887 0.2398 -0.0542 0.0296  0.0314  449  LEU B C   
12350 O O   . LEU B 451  ? 0.3189 0.4087 0.2509 -0.0537 0.0331  0.0318  449  LEU B O   
12351 C CB  . LEU B 451  ? 0.2880 0.3631 0.2280 -0.0512 0.0265  0.0275  449  LEU B CB  
12352 C CG  . LEU B 451  ? 0.3532 0.4210 0.2913 -0.0459 0.0250  0.0242  449  LEU B CG  
12353 C CD1 . LEU B 451  ? 0.3448 0.4003 0.2789 -0.0474 0.0213  0.0247  449  LEU B CD1 
12354 C CD2 . LEU B 451  ? 0.3872 0.4570 0.3315 -0.0419 0.0249  0.0210  449  LEU B CD2 
12355 N N   . HIS B 452  ? 0.2681 0.3386 0.1917 -0.0529 0.0281  0.0310  450  HIS B N   
12356 C CA  . HIS B 452  ? 0.3371 0.4108 0.2558 -0.0504 0.0304  0.0306  450  HIS B CA  
12357 C C   . HIS B 452  ? 0.3073 0.3878 0.2295 -0.0447 0.0328  0.0271  450  HIS B C   
12358 O O   . HIS B 452  ? 0.3132 0.3908 0.2393 -0.0413 0.0314  0.0241  450  HIS B O   
12359 C CB  . HIS B 452  ? 0.2968 0.3594 0.2091 -0.0489 0.0277  0.0297  450  HIS B CB  
12360 C CG  . HIS B 452  ? 0.3048 0.3692 0.2120 -0.0453 0.0296  0.0283  450  HIS B CG  
12361 N ND1 . HIS B 452  ? 0.3397 0.4073 0.2410 -0.0475 0.0316  0.0309  450  HIS B ND1 
12362 C CD2 . HIS B 452  ? 0.3091 0.3730 0.2163 -0.0396 0.0299  0.0246  450  HIS B CD2 
12363 C CE1 . HIS B 452  ? 0.3648 0.4334 0.2622 -0.0432 0.0330  0.0287  450  HIS B CE1 
12364 N NE2 . HIS B 452  ? 0.3276 0.3938 0.2285 -0.0384 0.0319  0.0248  450  HIS B NE2 
12365 N N   . GLY B 453  ? 0.3859 0.4755 0.3064 -0.0437 0.0365  0.0275  451  GLY B N   
12366 C CA  . GLY B 453  ? 0.4839 0.5795 0.4068 -0.0380 0.0389  0.0242  451  GLY B CA  
12367 C C   . GLY B 453  ? 0.4987 0.6011 0.4298 -0.0367 0.0398  0.0230  451  GLY B C   
12368 O O   . GLY B 453  ? 0.4926 0.5972 0.4262 -0.0315 0.0407  0.0197  451  GLY B O   
12369 N N   . MET B 454  ? 0.3923 0.4977 0.3276 -0.0415 0.0393  0.0256  452  MET B N   
12370 C CA  . MET B 454  ? 0.3726 0.4857 0.3157 -0.0409 0.0403  0.0249  452  MET B CA  
12371 C C   . MET B 454  ? 0.3675 0.4895 0.3129 -0.0465 0.0420  0.0288  452  MET B C   
12372 O O   . MET B 454  ? 0.4050 0.5386 0.3548 -0.0457 0.0449  0.0291  452  MET B O   
12373 C CB  . MET B 454  ? 0.3298 0.4350 0.2767 -0.0407 0.0367  0.0234  452  MET B CB  
12374 C CG  . MET B 454  ? 0.3551 0.4675 0.3097 -0.0411 0.0372  0.0234  452  MET B CG  
12375 S SD  . MET B 454  ? 0.4725 0.5965 0.4310 -0.0352 0.0410  0.0209  452  MET B SD  
12376 C CE  . MET B 454  ? 0.4583 0.5724 0.4148 -0.0287 0.0392  0.0164  452  MET B CE  
12377 N N   . GLY B 455  ? 0.2981 0.4146 0.2403 -0.0522 0.0401  0.0319  453  GLY B N   
12378 C CA  . GLY B 455  ? 0.3314 0.4545 0.2759 -0.0584 0.0409  0.0358  453  GLY B CA  
12379 C C   . GLY B 455  ? 0.3815 0.5121 0.3222 -0.0613 0.0440  0.0389  453  GLY B C   
12380 O O   . GLY B 455  ? 0.3575 0.4960 0.3010 -0.0663 0.0452  0.0421  453  GLY B O   
12381 N N   . GLU B 456  ? 0.3634 0.4920 0.2978 -0.0586 0.0453  0.0382  454  GLU B N   
12382 C CA  . GLU B 456  ? 0.3873 0.5227 0.3174 -0.0615 0.0483  0.0413  454  GLU B CA  
12383 C C   . GLU B 456  ? 0.3722 0.5236 0.3074 -0.0614 0.0525  0.0423  454  GLU B C   
12384 O O   . GLU B 456  ? 0.3989 0.5571 0.3340 -0.0669 0.0541  0.0462  454  GLU B O   
12385 C CB  . GLU B 456  ? 0.4623 0.5924 0.3844 -0.0581 0.0488  0.0401  454  GLU B CB  
12386 C CG  . GLU B 456  ? 0.4790 0.5944 0.3954 -0.0595 0.0448  0.0403  454  GLU B CG  
12387 C CD  . GLU B 456  ? 0.5000 0.6066 0.4174 -0.0542 0.0421  0.0361  454  GLU B CD  
12388 O OE1 . GLU B 456  ? 0.4534 0.5638 0.3774 -0.0512 0.0424  0.0336  454  GLU B OE1 
12389 O OE2 . GLU B 456  ? 0.4293 0.5256 0.3411 -0.0530 0.0397  0.0353  454  GLU B OE2 
12390 N N   . PRO B 457  ? 0.3753 0.5335 0.3150 -0.0555 0.0545  0.0390  455  PRO B N   
12391 C CA  . PRO B 457  ? 0.3895 0.5636 0.3344 -0.0553 0.0585  0.0400  455  PRO B CA  
12392 C C   . PRO B 457  ? 0.4169 0.5973 0.3677 -0.0616 0.0580  0.0434  455  PRO B C   
12393 O O   . PRO B 457  ? 0.3825 0.5715 0.3353 -0.0642 0.0599  0.0458  455  PRO B O   
12394 C CB  . PRO B 457  ? 0.3716 0.5484 0.3208 -0.0478 0.0593  0.0356  455  PRO B CB  
12395 C CG  . PRO B 457  ? 0.4302 0.5945 0.3736 -0.0436 0.0572  0.0324  455  PRO B CG  
12396 C CD  . PRO B 457  ? 0.4036 0.5556 0.3433 -0.0485 0.0533  0.0343  455  PRO B CD  
12397 N N   . LEU B 458  ? 0.3938 0.5671 0.3481 -0.0634 0.0544  0.0428  456  LEU B N   
12398 C CA  . LEU B 458  ? 0.3742 0.5521 0.3333 -0.0698 0.0534  0.0460  456  LEU B CA  
12399 C C   . LEU B 458  ? 0.3528 0.5273 0.3067 -0.0771 0.0528  0.0504  456  LEU B C   
12400 O O   . LEU B 458  ? 0.3447 0.5260 0.3016 -0.0807 0.0535  0.0529  456  LEU B O   
12401 C CB  . LEU B 458  ? 0.3465 0.5163 0.3096 -0.0698 0.0495  0.0442  456  LEU B CB  
12402 C CG  . LEU B 458  ? 0.3181 0.4912 0.2858 -0.0765 0.0480  0.0472  456  LEU B CG  
12403 C CD1 . LEU B 458  ? 0.3752 0.5646 0.3497 -0.0768 0.0510  0.0483  456  LEU B CD1 
12404 C CD2 . LEU B 458  ? 0.3501 0.5146 0.3210 -0.0758 0.0441  0.0451  456  LEU B CD2 
12405 N N   . TYR B 459  ? 0.3186 0.4795 0.2657 -0.0777 0.0501  0.0503  457  TYR B N   
12406 C CA  . TYR B 459  ? 0.3227 0.4781 0.2648 -0.0848 0.0487  0.0545  457  TYR B CA  
12407 C C   . TYR B 459  ? 0.3272 0.4869 0.2643 -0.0858 0.0514  0.0567  457  TYR B C   
12408 O O   . TYR B 459  ? 0.3276 0.4843 0.2622 -0.0915 0.0502  0.0601  457  TYR B O   
12409 C CB  . TYR B 459  ? 0.3477 0.4860 0.2852 -0.0850 0.0441  0.0535  457  TYR B CB  
12410 C CG  . TYR B 459  ? 0.3403 0.4744 0.2831 -0.0867 0.0409  0.0527  457  TYR B CG  
12411 C CD1 . TYR B 459  ? 0.3025 0.4366 0.2466 -0.0939 0.0394  0.0562  457  TYR B CD1 
12412 C CD2 . TYR B 459  ? 0.2942 0.4249 0.2408 -0.0811 0.0395  0.0485  457  TYR B CD2 
12413 C CE1 . TYR B 459  ? 0.3099 0.4403 0.2586 -0.0955 0.0364  0.0554  457  TYR B CE1 
12414 C CE2 . TYR B 459  ? 0.3089 0.4361 0.2602 -0.0827 0.0366  0.0479  457  TYR B CE2 
12415 C CZ  . TYR B 459  ? 0.2667 0.3937 0.2189 -0.0897 0.0351  0.0512  457  TYR B CZ  
12416 O OH  . TYR B 459  ? 0.2795 0.4027 0.2359 -0.0912 0.0322  0.0504  457  TYR B OH  
12417 N N   . GLU B 460  ? 0.3529 0.5185 0.2890 -0.0799 0.0546  0.0544  458  GLU B N   
12418 C CA  . GLU B 460  ? 0.3819 0.5534 0.3156 -0.0800 0.0573  0.0560  458  GLU B CA  
12419 C C   . GLU B 460  ? 0.4472 0.6295 0.3879 -0.0831 0.0585  0.0581  458  GLU B C   
12420 O O   . GLU B 460  ? 0.4242 0.6100 0.3630 -0.0859 0.0598  0.0607  458  GLU B O   
12421 C CB  . GLU B 460  ? 0.3966 0.5723 0.3283 -0.0725 0.0604  0.0527  458  GLU B CB  
12422 N N   . GLU B 461  ? 0.3955 0.5831 0.3442 -0.0829 0.0578  0.0571  459  GLU B N   
12423 C CA  . GLU B 461  ? 0.4206 0.6181 0.3762 -0.0862 0.0582  0.0591  459  GLU B CA  
12424 C C   . GLU B 461  ? 0.4289 0.6207 0.3849 -0.0940 0.0548  0.0622  459  GLU B C   
12425 O O   . GLU B 461  ? 0.3742 0.5731 0.3360 -0.0972 0.0545  0.0638  459  GLU B O   
12426 C CB  . GLU B 461  ? 0.3604 0.5666 0.3244 -0.0818 0.0591  0.0563  459  GLU B CB  
12427 C CG  . GLU B 461  ? 0.3512 0.5610 0.3148 -0.0736 0.0619  0.0526  459  GLU B CG  
12428 C CD  . GLU B 461  ? 0.4909 0.7085 0.4529 -0.0712 0.0654  0.0530  459  GLU B CD  
12429 O OE1 . GLU B 461  ? 0.4939 0.7171 0.4574 -0.0757 0.0660  0.0561  459  GLU B OE1 
12430 O OE2 . GLU B 461  ? 0.5161 0.7341 0.4752 -0.0650 0.0676  0.0502  459  GLU B OE2 
12431 N N   . VAL B 462  ? 0.3890 0.5678 0.3388 -0.0968 0.0521  0.0631  460  VAL B N   
12432 C CA  . VAL B 462  ? 0.3404 0.5115 0.2897 -0.1037 0.0483  0.0657  460  VAL B CA  
12433 C C   . VAL B 462  ? 0.3921 0.5545 0.3334 -0.1081 0.0472  0.0688  460  VAL B C   
12434 O O   . VAL B 462  ? 0.4074 0.5698 0.3488 -0.1140 0.0460  0.0720  460  VAL B O   
12435 C CB  . VAL B 462  ? 0.3708 0.5331 0.3207 -0.1032 0.0453  0.0638  460  VAL B CB  
12436 C CG1 . VAL B 462  ? 0.3366 0.4894 0.2850 -0.1101 0.0413  0.0663  460  VAL B CG1 
12437 C CG2 . VAL B 462  ? 0.3328 0.5039 0.2910 -0.0993 0.0463  0.0610  460  VAL B CG2 
12438 N N   . VAL B 463  ? 0.3434 0.4979 0.2774 -0.1054 0.0474  0.0680  461  VAL B N   
12439 C CA  . VAL B 463  ? 0.3389 0.4844 0.2647 -0.1090 0.0462  0.0708  461  VAL B CA  
12440 C C   . VAL B 463  ? 0.3695 0.5239 0.2945 -0.1095 0.0493  0.0727  461  VAL B C   
12441 O O   . VAL B 463  ? 0.4296 0.5939 0.3569 -0.1047 0.0529  0.0709  461  VAL B O   
12442 C CB  . VAL B 463  ? 0.3553 0.4903 0.2736 -0.1054 0.0453  0.0691  461  VAL B CB  
12443 C CG1 . VAL B 463  ? 0.3891 0.5145 0.2988 -0.1089 0.0438  0.0721  461  VAL B CG1 
12444 C CG2 . VAL B 463  ? 0.3743 0.5011 0.2937 -0.1049 0.0422  0.0673  461  VAL B CG2 
12445 N N   . GLY B 464  ? 0.4488 0.5993 0.3704 -0.1154 0.0480  0.0764  462  GLY B N   
12446 C CA  . GLY B 464  ? 0.4243 0.5821 0.3444 -0.1165 0.0509  0.0785  462  GLY B CA  
12447 C C   . GLY B 464  ? 0.4781 0.6437 0.4036 -0.1219 0.0509  0.0813  462  GLY B C   
12448 O O   . GLY B 464  ? 0.4650 0.6366 0.3979 -0.1223 0.0504  0.0803  462  GLY B O   
12449 N N   . ARG B 465  ? 0.4798 0.6452 0.4014 -0.1261 0.0513  0.0847  463  ARG B N   
12450 C CA  . ARG B 465  ? 0.4955 0.6687 0.4217 -0.1315 0.0515  0.0875  463  ARG B CA  
12451 C C   . ARG B 465  ? 0.5162 0.7057 0.4504 -0.1281 0.0551  0.0861  463  ARG B C   
12452 O O   . ARG B 465  ? 0.5572 0.7539 0.4978 -0.1314 0.0545  0.0872  463  ARG B O   
12453 C CB  . ARG B 465  ? 0.6004 0.7713 0.5206 -0.1358 0.0519  0.0913  463  ARG B CB  
12454 N N   . GLY B 466  ? 0.4963 0.6913 0.4300 -0.1215 0.0585  0.0835  464  GLY B N   
12455 C CA  . GLY B 466  ? 0.5328 0.7424 0.4737 -0.1173 0.0618  0.0817  464  GLY B CA  
12456 C C   . GLY B 466  ? 0.5448 0.7569 0.4923 -0.1136 0.0610  0.0784  464  GLY B C   
12457 O O   . GLY B 466  ? 0.4963 0.7201 0.4499 -0.1094 0.0636  0.0766  464  GLY B O   
12458 N N   . LYS B 467  ? 0.5114 0.7128 0.4578 -0.1148 0.0574  0.0775  465  LYS B N   
12459 C CA  . LYS B 467  ? 0.4670 0.6698 0.4194 -0.1118 0.0563  0.0746  465  LYS B CA  
12460 C C   . LYS B 467  ? 0.4798 0.6783 0.4353 -0.1179 0.0524  0.0762  465  LYS B C   
12461 O O   . LYS B 467  ? 0.4660 0.6693 0.4239 -0.1230 0.0520  0.0790  465  LYS B O   
12462 C CB  . LYS B 467  ? 0.4139 0.6078 0.3621 -0.1067 0.0558  0.0714  465  LYS B CB  
12463 C CG  . LYS B 467  ? 0.4884 0.6859 0.4334 -0.1003 0.0594  0.0694  465  LYS B CG  
12464 C CD  . LYS B 467  ? 0.5129 0.7241 0.4649 -0.0952 0.0625  0.0672  465  LYS B CD  
12465 C CE  . LYS B 467  ? 0.5219 0.7361 0.4701 -0.0887 0.0661  0.0649  465  LYS B CE  
12466 N NZ  . LYS B 467  ? 0.5414 0.7670 0.4963 -0.0827 0.0687  0.0621  465  LYS B NZ  
12467 N N   . LEU B 468  ? 0.4079 0.5972 0.3630 -0.1174 0.0495  0.0745  466  LEU B N   
12468 C CA  . LEU B 468  ? 0.3861 0.5697 0.3431 -0.1231 0.0456  0.0759  466  LEU B CA  
12469 C C   . LEU B 468  ? 0.3381 0.5084 0.2876 -0.1286 0.0427  0.0786  466  LEU B C   
12470 O O   . LEU B 468  ? 0.3822 0.5469 0.3323 -0.1339 0.0393  0.0801  466  LEU B O   
12471 C CB  . LEU B 468  ? 0.3824 0.5625 0.3429 -0.1203 0.0437  0.0728  466  LEU B CB  
12472 C CG  . LEU B 468  ? 0.4133 0.6062 0.3817 -0.1150 0.0462  0.0702  466  LEU B CG  
12473 C CD1 . LEU B 468  ? 0.4151 0.6047 0.3873 -0.1132 0.0440  0.0676  466  LEU B CD1 
12474 C CD2 . LEU B 468  ? 0.4145 0.6197 0.3887 -0.1179 0.0472  0.0722  466  LEU B CD2 
12475 N N   . ASP B 469  ? 0.3786 0.5435 0.3208 -0.1274 0.0438  0.0793  467  ASP B N   
12476 C CA  . ASP B 469  ? 0.4648 0.6168 0.3993 -0.1321 0.0410  0.0819  467  ASP B CA  
12477 C C   . ASP B 469  ? 0.3796 0.5182 0.3121 -0.1336 0.0368  0.0811  467  ASP B C   
12478 O O   . ASP B 469  ? 0.3851 0.5146 0.3147 -0.1390 0.0334  0.0833  467  ASP B O   
12479 C CB  . ASP B 469  ? 0.4404 0.5954 0.3749 -0.1386 0.0406  0.0857  467  ASP B CB  
12480 C CG  . ASP B 469  ? 0.5337 0.6792 0.4594 -0.1416 0.0398  0.0885  467  ASP B CG  
12481 O OD1 . ASP B 469  ? 0.5130 0.6503 0.4327 -0.1383 0.0397  0.0874  467  ASP B OD1 
12482 O OD2 . ASP B 469  ? 0.6115 0.7578 0.5363 -0.1471 0.0392  0.0918  467  ASP B OD2 
12483 N N   . ARG B 470  ? 0.4113 0.5484 0.3453 -0.1285 0.0369  0.0777  468  ARG B N   
12484 C CA  . ARG B 470  ? 0.3768 0.5014 0.3087 -0.1288 0.0333  0.0765  468  ARG B CA  
12485 C C   . ARG B 470  ? 0.3792 0.4962 0.3051 -0.1241 0.0336  0.0747  468  ARG B C   
12486 O O   . ARG B 470  ? 0.3702 0.4944 0.2971 -0.1187 0.0368  0.0726  468  ARG B O   
12487 C CB  . ARG B 470  ? 0.3769 0.5067 0.3167 -0.1273 0.0328  0.0741  468  ARG B CB  
12488 C CG  . ARG B 470  ? 0.3738 0.5096 0.3192 -0.1322 0.0316  0.0757  468  ARG B CG  
12489 C CD  . ARG B 470  ? 0.3459 0.4702 0.2865 -0.1388 0.0278  0.0786  468  ARG B CD  
12490 N NE  . ARG B 470  ? 0.3989 0.5284 0.3443 -0.1438 0.0265  0.0801  468  ARG B NE  
12491 C CZ  . ARG B 470  ? 0.4794 0.6163 0.4256 -0.1473 0.0277  0.0828  468  ARG B CZ  
12492 N NH1 . ARG B 470  ? 0.4193 0.5597 0.3621 -0.1463 0.0305  0.0842  468  ARG B NH1 
12493 N NH2 . ARG B 470  ? 0.4751 0.6160 0.4255 -0.1519 0.0261  0.0842  468  ARG B NH2 
12494 N N   . PRO B 471  ? 0.3465 0.4489 0.2661 -0.1259 0.0303  0.0754  469  PRO B N   
12495 C CA  . PRO B 471  ? 0.3395 0.4341 0.2528 -0.1217 0.0302  0.0739  469  PRO B CA  
12496 C C   . PRO B 471  ? 0.3280 0.4222 0.2450 -0.1166 0.0299  0.0700  469  PRO B C   
12497 O O   . PRO B 471  ? 0.3052 0.4007 0.2283 -0.1172 0.0286  0.0687  469  PRO B O   
12498 C CB  . PRO B 471  ? 0.3185 0.3972 0.2247 -0.1256 0.0260  0.0761  469  PRO B CB  
12499 C CG  . PRO B 471  ? 0.3970 0.4737 0.3074 -0.1304 0.0234  0.0770  469  PRO B CG  
12500 C CD  . PRO B 471  ? 0.3677 0.4595 0.2850 -0.1318 0.0261  0.0777  469  PRO B CD  
12501 N N   . CYS B 472  ? 0.3348 0.4261 0.2491 -0.1101 0.0305  0.0670  470  CYS B N   
12502 C CA  . CYS B 472  ? 0.3062 0.3945 0.2244 -0.1033 0.0294  0.0621  470  CYS B CA  
12503 C C   . CYS B 472  ? 0.2974 0.3731 0.2092 -0.0993 0.0271  0.0603  470  CYS B C   
12504 O O   . CYS B 472  ? 0.3212 0.3968 0.2273 -0.0983 0.0286  0.0612  470  CYS B O   
12505 C CB  . CYS B 472  ? 0.3234 0.4250 0.2469 -0.0982 0.0333  0.0596  470  CYS B CB  
12506 S SG  . CYS B 472  ? 0.3455 0.4433 0.2737 -0.0904 0.0319  0.0538  470  CYS B SG  
12507 N N   . ARG B 473  ? 0.3063 0.3716 0.2191 -0.0972 0.0235  0.0579  471  ARG B N   
12508 C CA  . ARG B 473  ? 0.3205 0.3743 0.2285 -0.0929 0.0211  0.0558  471  ARG B CA  
12509 C C   . ARG B 473  ? 0.3050 0.3619 0.2170 -0.0856 0.0221  0.0510  471  ARG B C   
12510 O O   . ARG B 473  ? 0.3042 0.3643 0.2229 -0.0838 0.0219  0.0487  471  ARG B O   
12511 C CB  . ARG B 473  ? 0.2757 0.3160 0.1821 -0.0947 0.0165  0.0559  471  ARG B CB  
12512 C CG  . ARG B 473  ? 0.2997 0.3284 0.2009 -0.0906 0.0138  0.0541  471  ARG B CG  
12513 C CD  . ARG B 473  ? 0.2897 0.3052 0.1888 -0.0926 0.0094  0.0547  471  ARG B CD  
12514 N NE  . ARG B 473  ? 0.3053 0.3186 0.2012 -0.0998 0.0086  0.0591  471  ARG B NE  
12515 C CZ  . ARG B 473  ? 0.3366 0.3452 0.2252 -0.1030 0.0081  0.0625  471  ARG B CZ  
12516 N NH1 . ARG B 473  ? 0.3444 0.3494 0.2278 -0.0997 0.0081  0.0620  471  ARG B NH1 
12517 N NH2 . ARG B 473  ? 0.3575 0.3650 0.2438 -0.1100 0.0076  0.0666  471  ARG B NH2 
12518 N N   . ILE B 474  ? 0.2867 0.3426 0.1946 -0.0815 0.0230  0.0497  472  ILE B N   
12519 C CA  . ILE B 474  ? 0.2760 0.3345 0.1868 -0.0747 0.0240  0.0453  472  ILE B CA  
12520 C C   . ILE B 474  ? 0.2933 0.3397 0.2031 -0.0713 0.0202  0.0427  472  ILE B C   
12521 O O   . ILE B 474  ? 0.2921 0.3293 0.1957 -0.0716 0.0180  0.0436  472  ILE B O   
12522 C CB  . ILE B 474  ? 0.2874 0.3513 0.1940 -0.0720 0.0271  0.0451  472  ILE B CB  
12523 C CG1 . ILE B 474  ? 0.2880 0.3651 0.1962 -0.0750 0.0312  0.0476  472  ILE B CG1 
12524 C CG2 . ILE B 474  ? 0.2953 0.3601 0.2041 -0.0650 0.0276  0.0405  472  ILE B CG2 
12525 C CD1 . ILE B 474  ? 0.3006 0.3828 0.2036 -0.0730 0.0343  0.0479  472  ILE B CD1 
12526 N N   . TYR B 475  ? 0.2638 0.3104 0.1796 -0.0682 0.0194  0.0396  473  TYR B N   
12527 C CA  . TYR B 475  ? 0.2616 0.2987 0.1776 -0.0642 0.0164  0.0366  473  TYR B CA  
12528 C C   . TYR B 475  ? 0.2783 0.3164 0.1922 -0.0588 0.0175  0.0340  473  TYR B C   
12529 O O   . TYR B 475  ? 0.2807 0.3271 0.1982 -0.0556 0.0202  0.0319  473  TYR B O   
12530 C CB  . TYR B 475  ? 0.2588 0.2972 0.1821 -0.0628 0.0156  0.0344  473  TYR B CB  
12531 C CG  . TYR B 475  ? 0.2582 0.2868 0.1821 -0.0596 0.0123  0.0318  473  TYR B CG  
12532 C CD1 . TYR B 475  ? 0.2919 0.3200 0.2171 -0.0539 0.0124  0.0283  473  TYR B CD1 
12533 C CD2 . TYR B 475  ? 0.2687 0.2886 0.1918 -0.0622 0.0091  0.0329  473  TYR B CD2 
12534 C CE1 . TYR B 475  ? 0.2932 0.3131 0.2194 -0.0512 0.0095  0.0261  473  TYR B CE1 
12535 C CE2 . TYR B 475  ? 0.2473 0.2589 0.1712 -0.0591 0.0062  0.0305  473  TYR B CE2 
12536 C CZ  . TYR B 475  ? 0.2769 0.2889 0.2026 -0.0537 0.0065  0.0272  473  TYR B CZ  
12537 O OH  . TYR B 475  ? 0.2928 0.2973 0.2195 -0.0507 0.0038  0.0250  473  TYR B OH  
12538 N N   . ALA B 476  ? 0.2800 0.3097 0.1880 -0.0578 0.0155  0.0341  474  ALA B N   
12539 C CA  . ALA B 476  ? 0.2875 0.3178 0.1916 -0.0538 0.0165  0.0323  474  ALA B CA  
12540 C C   . ALA B 476  ? 0.2967 0.3189 0.2010 -0.0494 0.0136  0.0292  474  ALA B C   
12541 O O   . ALA B 476  ? 0.3023 0.3152 0.2026 -0.0501 0.0105  0.0300  474  ALA B O   
12542 C CB  . ALA B 476  ? 0.3151 0.3435 0.2114 -0.0567 0.0168  0.0355  474  ALA B CB  
12543 N N   . PRO B 477  ? 0.2905 0.3159 0.1994 -0.0449 0.0144  0.0256  475  PRO B N   
12544 C CA  . PRO B 477  ? 0.2859 0.3042 0.1947 -0.0408 0.0118  0.0226  475  PRO B CA  
12545 C C   . PRO B 477  ? 0.2921 0.3071 0.1940 -0.0392 0.0113  0.0225  475  PRO B C   
12546 O O   . PRO B 477  ? 0.2988 0.3194 0.1975 -0.0390 0.0140  0.0229  475  PRO B O   
12547 C CB  . PRO B 477  ? 0.2976 0.3217 0.2124 -0.0369 0.0135  0.0193  475  PRO B CB  
12548 C CG  . PRO B 477  ? 0.3196 0.3522 0.2387 -0.0393 0.0161  0.0206  475  PRO B CG  
12549 C CD  . PRO B 477  ? 0.2923 0.3277 0.2068 -0.0435 0.0175  0.0243  475  PRO B CD  
12550 N N   . VAL B 478  ? 0.2826 0.2887 0.1824 -0.0379 0.0079  0.0217  476  VAL B N   
12551 C CA  . VAL B 478  ? 0.2835 0.2853 0.1767 -0.0363 0.0067  0.0215  476  VAL B CA  
12552 C C   . VAL B 478  ? 0.3246 0.3213 0.2198 -0.0322 0.0041  0.0182  476  VAL B C   
12553 O O   . VAL B 478  ? 0.3435 0.3348 0.2417 -0.0322 0.0014  0.0179  476  VAL B O   
12554 C CB  . VAL B 478  ? 0.2949 0.2900 0.1821 -0.0399 0.0045  0.0250  476  VAL B CB  
12555 C CG1 . VAL B 478  ? 0.3395 0.3305 0.2198 -0.0382 0.0032  0.0248  476  VAL B CG1 
12556 C CG2 . VAL B 478  ? 0.3107 0.3107 0.1963 -0.0447 0.0069  0.0286  476  VAL B CG2 
12557 N N   . GLY B 479  ? 0.3583 0.3567 0.2518 -0.0287 0.0048  0.0157  477  GLY B N   
12558 C CA  . GLY B 479  ? 0.4059 0.3995 0.3010 -0.0252 0.0023  0.0127  477  GLY B CA  
12559 C C   . GLY B 479  ? 0.4336 0.4309 0.3284 -0.0214 0.0039  0.0096  477  GLY B C   
12560 O O   . GLY B 479  ? 0.3657 0.3695 0.2590 -0.0212 0.0072  0.0096  477  GLY B O   
12561 N N   . THR B 480  ? 0.4687 0.4619 0.3653 -0.0184 0.0016  0.0069  478  THR B N   
12562 C CA  . THR B 480  ? 0.5448 0.5392 0.4402 -0.0148 0.0021  0.0037  478  THR B CA  
12563 C C   . THR B 480  ? 0.5574 0.5574 0.4588 -0.0128 0.0046  0.0016  478  THR B C   
12564 O O   . THR B 480  ? 0.5260 0.5290 0.4328 -0.0142 0.0056  0.0024  478  THR B O   
12565 C CB  . THR B 480  ? 0.5081 0.4956 0.4033 -0.0128 -0.0017 0.0019  478  THR B CB  
12566 O OG1 . THR B 480  ? 0.6175 0.6033 0.5196 -0.0126 -0.0032 0.0013  478  THR B OG1 
12567 C CG2 . THR B 480  ? 0.4956 0.4775 0.3850 -0.0146 -0.0043 0.0041  478  THR B CG2 
12568 N N   . HIS B 481  ? 0.5950 0.5962 0.4952 -0.0094 0.0054  -0.0014 479  HIS B N   
12569 C CA  . HIS B 481  ? 0.5439 0.5497 0.4494 -0.0070 0.0075  -0.0036 479  HIS B CA  
12570 C C   . HIS B 481  ? 0.6215 0.6246 0.5338 -0.0065 0.0055  -0.0047 479  HIS B C   
12571 O O   . HIS B 481  ? 0.5657 0.5729 0.4836 -0.0066 0.0070  -0.0047 479  HIS B O   
12572 C CB  . HIS B 481  ? 0.5496 0.5555 0.4516 -0.0034 0.0082  -0.0066 479  HIS B CB  
12573 C CG  . HIS B 481  ? 0.5868 0.5960 0.4820 -0.0034 0.0105  -0.0059 479  HIS B CG  
12574 N ND1 . HIS B 481  ? 0.6279 0.6376 0.5189 -0.0002 0.0116  -0.0085 479  HIS B ND1 
12575 C CD2 . HIS B 481  ? 0.5605 0.5727 0.4522 -0.0063 0.0121  -0.0029 479  HIS B CD2 
12576 C CE1 . HIS B 481  ? 0.6456 0.6588 0.5308 -0.0008 0.0139  -0.0072 479  HIS B CE1 
12577 N NE2 . HIS B 481  ? 0.6805 0.6954 0.5661 -0.0047 0.0143  -0.0037 479  HIS B NE2 
12578 N N   . GLU B 482  ? 0.5948 0.5914 0.5068 -0.0061 0.0020  -0.0054 480  GLU B N   
12579 C CA  . GLU B 482  ? 0.5573 0.5514 0.4755 -0.0055 0.0001  -0.0064 480  GLU B CA  
12580 C C   . GLU B 482  ? 0.5446 0.5397 0.4668 -0.0083 0.0003  -0.0040 480  GLU B C   
12581 O O   . GLU B 482  ? 0.6230 0.6198 0.5511 -0.0079 0.0007  -0.0047 480  GLU B O   
12582 C CB  . GLU B 482  ? 0.6094 0.5969 0.5264 -0.0047 -0.0036 -0.0073 480  GLU B CB  
12583 N N   . THR B 483  ? 0.6089 0.6026 0.5275 -0.0111 -0.0002 -0.0013 481  THR B N   
12584 C CA  . THR B 483  ? 0.6344 0.6280 0.5560 -0.0140 -0.0004 0.0010  481  THR B CA  
12585 C C   . THR B 483  ? 0.5858 0.5866 0.5104 -0.0151 0.0029  0.0018  481  THR B C   
12586 O O   . THR B 483  ? 0.6069 0.6089 0.5367 -0.0159 0.0031  0.0019  481  THR B O   
12587 C CB  . THR B 483  ? 0.6551 0.6446 0.5715 -0.0167 -0.0020 0.0038  481  THR B CB  
12588 N N   . LEU B 484  ? 0.5682 0.5741 0.4895 -0.0152 0.0056  0.0022  482  LEU B N   
12589 C CA  . LEU B 484  ? 0.5667 0.5801 0.4907 -0.0165 0.0088  0.0032  482  LEU B CA  
12590 C C   . LEU B 484  ? 0.5319 0.5490 0.4620 -0.0138 0.0100  0.0008  482  LEU B C   
12591 O O   . LEU B 484  ? 0.5448 0.5664 0.4795 -0.0150 0.0113  0.0015  482  LEU B O   
12592 C CB  . LEU B 484  ? 0.5385 0.5570 0.4576 -0.0170 0.0116  0.0043  482  LEU B CB  
12593 C CG  . LEU B 484  ? 0.5442 0.5653 0.4609 -0.0132 0.0133  0.0017  482  LEU B CG  
12594 C CD1 . LEU B 484  ? 0.5165 0.5454 0.4378 -0.0112 0.0163  0.0003  482  LEU B CD1 
12595 C CD2 . LEU B 484  ? 0.5088 0.5309 0.4181 -0.0140 0.0145  0.0030  482  LEU B CD2 
12596 N N   . LEU B 485  ? 0.5187 0.5339 0.4488 -0.0102 0.0094  -0.0021 483  LEU B N   
12597 C CA  . LEU B 485  ? 0.5860 0.6041 0.5214 -0.0075 0.0104  -0.0044 483  LEU B CA  
12598 C C   . LEU B 485  ? 0.5403 0.5560 0.4814 -0.0082 0.0087  -0.0043 483  LEU B C   
12599 O O   . LEU B 485  ? 0.4967 0.5160 0.4426 -0.0070 0.0098  -0.0053 483  LEU B O   
12600 C CB  . LEU B 485  ? 0.5546 0.5699 0.4881 -0.0037 0.0097  -0.0074 483  LEU B CB  
12601 C CG  . LEU B 485  ? 0.5257 0.5444 0.4543 -0.0018 0.0120  -0.0083 483  LEU B CG  
12602 C CD1 . LEU B 485  ? 0.5284 0.5425 0.4547 0.0015  0.0105  -0.0113 483  LEU B CD1 
12603 C CD2 . LEU B 485  ? 0.5277 0.5545 0.4591 -0.0008 0.0155  -0.0084 483  LEU B CD2 
12604 N N   . ALA B 486  ? 0.5507 0.5606 0.4911 -0.0101 0.0060  -0.0032 484  ALA B N   
12605 C CA  . ALA B 486  ? 0.4794 0.4864 0.4248 -0.0102 0.0041  -0.0035 484  ALA B CA  
12606 C C   . ALA B 486  ? 0.5912 0.6025 0.5408 -0.0122 0.0055  -0.0023 484  ALA B C   
12607 O O   . ALA B 486  ? 0.6183 0.6292 0.5727 -0.0114 0.0050  -0.0032 484  ALA B O   
12608 C CB  . ALA B 486  ? 0.5504 0.5504 0.4936 -0.0116 0.0011  -0.0025 484  ALA B CB  
12609 N N   . TYR B 487  ? 0.5507 0.5661 0.4985 -0.0148 0.0073  -0.0001 485  TYR B N   
12610 C CA  . TYR B 487  ? 0.5190 0.5389 0.4709 -0.0169 0.0085  0.0012  485  TYR B CA  
12611 C C   . TYR B 487  ? 0.5160 0.5443 0.4677 -0.0175 0.0117  0.0021  485  TYR B C   
12612 O O   . TYR B 487  ? 0.4281 0.4605 0.3818 -0.0204 0.0127  0.0040  485  TYR B O   
12613 C CB  . TYR B 487  ? 0.5319 0.5478 0.4831 -0.0206 0.0067  0.0035  485  TYR B CB  
12614 C CG  . TYR B 487  ? 0.5998 0.6087 0.5526 -0.0197 0.0038  0.0025  485  TYR B CG  
12615 C CD1 . TYR B 487  ? 0.6393 0.6487 0.5974 -0.0189 0.0035  0.0014  485  TYR B CD1 
12616 C CD2 . TYR B 487  ? 0.6081 0.6101 0.5573 -0.0197 0.0013  0.0028  485  TYR B CD2 
12617 C CE1 . TYR B 487  ? 0.6660 0.6696 0.6257 -0.0180 0.0011  0.0005  485  TYR B CE1 
12618 C CE2 . TYR B 487  ? 0.6313 0.6276 0.5824 -0.0187 -0.0012 0.0020  485  TYR B CE2 
12619 C CZ  . TYR B 487  ? 0.7000 0.6972 0.6563 -0.0179 -0.0012 0.0008  485  TYR B CZ  
12620 O OH  . TYR B 487  ? 0.7415 0.7335 0.6996 -0.0168 -0.0035 0.0000  485  TYR B OH  
12621 N N   . LEU B 488  ? 0.5489 0.5799 0.4983 -0.0149 0.0134  0.0007  486  LEU B N   
12622 C CA  . LEU B 488  ? 0.4941 0.5337 0.4435 -0.0149 0.0166  0.0014  486  LEU B CA  
12623 C C   . LEU B 488  ? 0.5032 0.5489 0.4588 -0.0139 0.0181  0.0007  486  LEU B C   
12624 O O   . LEU B 488  ? 0.3931 0.4464 0.3503 -0.0154 0.0203  0.0022  486  LEU B O   
12625 C CB  . LEU B 488  ? 0.5005 0.5411 0.4457 -0.0118 0.0180  -0.0002 486  LEU B CB  
12626 C CG  . LEU B 488  ? 0.4719 0.5216 0.4165 -0.0114 0.0216  0.0004  486  LEU B CG  
12627 C CD1 . LEU B 488  ? 0.5810 0.6344 0.5246 -0.0161 0.0225  0.0039  486  LEU B CD1 
12628 C CD2 . LEU B 488  ? 0.3783 0.4275 0.3174 -0.0085 0.0225  -0.0011 486  LEU B CD2 
12629 N N   . VAL B 489  ? 0.4931 0.5359 0.4522 -0.0114 0.0168  -0.0014 487  VAL B N   
12630 C CA  . VAL B 489  ? 0.4076 0.4556 0.3724 -0.0103 0.0179  -0.0020 487  VAL B CA  
12631 C C   . VAL B 489  ? 0.4539 0.5052 0.4213 -0.0143 0.0180  0.0005  487  VAL B C   
12632 O O   . VAL B 489  ? 0.5375 0.5968 0.5075 -0.0150 0.0201  0.0013  487  VAL B O   
12633 C CB  . VAL B 489  ? 0.4387 0.4819 0.4065 -0.0076 0.0161  -0.0043 487  VAL B CB  
12634 C CG1 . VAL B 489  ? 0.4503 0.4982 0.4238 -0.0071 0.0169  -0.0045 487  VAL B CG1 
12635 C CG2 . VAL B 489  ? 0.4704 0.5115 0.4359 -0.0036 0.0164  -0.0068 487  VAL B CG2 
12636 N N   . ARG B 490  ? 0.5163 0.5615 0.4832 -0.0171 0.0156  0.0016  488  ARG B N   
12637 C CA  . ARG B 490  ? 0.5077 0.5548 0.4765 -0.0212 0.0153  0.0038  488  ARG B CA  
12638 C C   . ARG B 490  ? 0.4892 0.5419 0.4556 -0.0243 0.0172  0.0064  488  ARG B C   
12639 O O   . ARG B 490  ? 0.4894 0.5483 0.4587 -0.0268 0.0182  0.0079  488  ARG B O   
12640 C CB  . ARG B 490  ? 0.5047 0.5431 0.4722 -0.0232 0.0123  0.0044  488  ARG B CB  
12641 C CG  . ARG B 490  ? 0.4974 0.5361 0.4663 -0.0275 0.0115  0.0066  488  ARG B CG  
12642 C CD  . ARG B 490  ? 0.4468 0.4763 0.4132 -0.0293 0.0086  0.0072  488  ARG B CD  
12643 N NE  . ARG B 490  ? 0.4431 0.4689 0.4038 -0.0305 0.0081  0.0086  488  ARG B NE  
12644 C CZ  . ARG B 490  ? 0.4263 0.4439 0.3840 -0.0301 0.0057  0.0084  488  ARG B CZ  
12645 N NH1 . ARG B 490  ? 0.3790 0.3914 0.3388 -0.0283 0.0037  0.0068  488  ARG B NH1 
12646 N NH2 . ARG B 490  ? 0.3724 0.3871 0.3248 -0.0315 0.0053  0.0099  488  ARG B NH2 
12647 N N   . ARG B 491  ? 0.4580 0.5092 0.4193 -0.0243 0.0176  0.0068  489  ARG B N   
12648 C CA  . ARG B 491  ? 0.5359 0.5922 0.4944 -0.0275 0.0194  0.0095  489  ARG B CA  
12649 C C   . ARG B 491  ? 0.5450 0.6122 0.5065 -0.0262 0.0227  0.0093  489  ARG B C   
12650 O O   . ARG B 491  ? 0.4953 0.5691 0.4579 -0.0295 0.0242  0.0117  489  ARG B O   
12651 C CB  . ARG B 491  ? 0.5138 0.5659 0.4659 -0.0272 0.0192  0.0098  489  ARG B CB  
12652 N N   . LEU B 492  ? 0.5737 0.6428 0.5366 -0.0213 0.0238  0.0066  490  LEU B N   
12653 C CA  . LEU B 492  ? 0.5948 0.6739 0.5600 -0.0191 0.0270  0.0062  490  LEU B CA  
12654 C C   . LEU B 492  ? 0.5972 0.6819 0.5689 -0.0191 0.0274  0.0061  490  LEU B C   
12655 O O   . LEU B 492  ? 0.4283 0.5226 0.4026 -0.0199 0.0297  0.0074  490  LEU B O   
12656 C CB  . LEU B 492  ? 0.5391 0.6169 0.5023 -0.0137 0.0278  0.0032  490  LEU B CB  
12657 N N   . LEU B 493  ? 0.5620 0.6414 0.5366 -0.0182 0.0252  0.0048  491  LEU B N   
12658 C CA  . LEU B 493  ? 0.3902 0.4744 0.3708 -0.0181 0.0253  0.0046  491  LEU B CA  
12659 C C   . LEU B 493  ? 0.5250 0.6131 0.5073 -0.0234 0.0251  0.0076  491  LEU B C   
12660 O O   . LEU B 493  ? 0.6002 0.6969 0.5865 -0.0240 0.0266  0.0084  491  LEU B O   
12661 C CB  . LEU B 493  ? 0.4769 0.5538 0.4595 -0.0163 0.0228  0.0027  491  LEU B CB  
12662 N N   . ALA B 497  ? 0.4720 0.5834 0.4665 -0.0133 0.0306  0.0043  495  ALA B N   
12663 C CA  . ALA B 497  ? 0.5308 0.6477 0.5309 -0.0146 0.0302  0.0051  495  ALA B CA  
12664 C C   . ALA B 497  ? 0.4427 0.5725 0.4461 -0.0148 0.0330  0.0065  495  ALA B C   
12665 O O   . ALA B 497  ? 0.4812 0.6158 0.4828 -0.0175 0.0345  0.0085  495  ALA B O   
12666 C CB  . ALA B 497  ? 0.4148 0.5271 0.4150 -0.0200 0.0278  0.0069  495  ALA B CB  
12667 N N   . ASN B 498  ? 0.4762 0.6117 0.4844 -0.0119 0.0335  0.0056  496  ASN B N   
12668 C CA  . ASN B 498  ? 0.4916 0.6400 0.5036 -0.0115 0.0360  0.0068  496  ASN B CA  
12669 C C   . ASN B 498  ? 0.4507 0.6050 0.4650 -0.0177 0.0357  0.0100  496  ASN B C   
12670 O O   . ASN B 498  ? 0.4590 0.6240 0.4751 -0.0189 0.0380  0.0117  496  ASN B O   
12671 C CB  . ASN B 498  ? 0.4501 0.6024 0.4668 -0.0070 0.0361  0.0052  496  ASN B CB  
12672 N N   . SER B 499  ? 0.4116 0.5590 0.4257 -0.0218 0.0329  0.0108  497  SER B N   
12673 C CA  . SER B 499  ? 0.3627 0.5142 0.3785 -0.0281 0.0321  0.0137  497  SER B CA  
12674 C C   . SER B 499  ? 0.3504 0.5004 0.3617 -0.0325 0.0326  0.0159  497  SER B C   
12675 O O   . SER B 499  ? 0.3435 0.4972 0.3558 -0.0381 0.0322  0.0186  497  SER B O   
12676 C CB  . SER B 499  ? 0.4031 0.5467 0.4197 -0.0306 0.0287  0.0135  497  SER B CB  
12677 O OG  . SER B 499  ? 0.4200 0.5511 0.4318 -0.0298 0.0271  0.0121  497  SER B OG  
12678 N N   . SER B 500  ? 0.3362 0.4807 0.3425 -0.0303 0.0334  0.0149  498  SER B N   
12679 C CA  . SER B 500  ? 0.3384 0.4801 0.3397 -0.0343 0.0336  0.0169  498  SER B CA  
12680 C C   . SER B 500  ? 0.3925 0.5461 0.3944 -0.0353 0.0369  0.0189  498  SER B C   
12681 O O   . SER B 500  ? 0.4328 0.5942 0.4368 -0.0308 0.0395  0.0176  498  SER B O   
12682 C CB  . SER B 500  ? 0.3876 0.5191 0.3832 -0.0313 0.0330  0.0150  498  SER B CB  
12683 N N   . PHE B 501  ? 0.3165 0.4713 0.3165 -0.0412 0.0369  0.0220  499  PHE B N   
12684 C CA  . PHE B 501  ? 0.3654 0.5307 0.3650 -0.0426 0.0402  0.0241  499  PHE B CA  
12685 C C   . PHE B 501  ? 0.4345 0.5985 0.4293 -0.0379 0.0424  0.0224  499  PHE B C   
12686 O O   . PHE B 501  ? 0.5320 0.7062 0.5278 -0.0355 0.0457  0.0226  499  PHE B O   
12687 C CB  . PHE B 501  ? 0.3567 0.5209 0.3537 -0.0501 0.0394  0.0278  499  PHE B CB  
12688 C CG  . PHE B 501  ? 0.3863 0.5631 0.3842 -0.0528 0.0426  0.0306  499  PHE B CG  
12689 C CD1 . PHE B 501  ? 0.4549 0.6329 0.4478 -0.0517 0.0451  0.0311  499  PHE B CD1 
12690 C CD2 . PHE B 501  ? 0.3655 0.5529 0.3690 -0.0566 0.0431  0.0329  499  PHE B CD2 
12691 C CE1 . PHE B 501  ? 0.4229 0.6129 0.4166 -0.0543 0.0483  0.0339  499  PHE B CE1 
12692 C CE2 . PHE B 501  ? 0.4351 0.6348 0.4398 -0.0593 0.0462  0.0357  499  PHE B CE2 
12693 C CZ  . PHE B 501  ? 0.4267 0.6278 0.4264 -0.0581 0.0489  0.0362  499  PHE B CZ  
12694 N N   . VAL B 502  ? 0.5057 0.6574 0.4956 -0.0362 0.0405  0.0207  500  VAL B N   
12695 C CA  . VAL B 502  ? 0.5559 0.7051 0.5407 -0.0319 0.0421  0.0190  500  VAL B CA  
12696 C C   . VAL B 502  ? 0.5869 0.7423 0.5746 -0.0253 0.0443  0.0162  500  VAL B C   
12697 O O   . VAL B 502  ? 0.6080 0.7682 0.5932 -0.0222 0.0471  0.0155  500  VAL B O   
12698 C CB  . VAL B 502  ? 0.5040 0.6389 0.4837 -0.0313 0.0392  0.0175  500  VAL B CB  
12699 N N   . HIS B 503  ? 0.4914 0.6464 0.4840 -0.0229 0.0429  0.0145  501  HIS B N   
12700 C CA  . HIS B 503  ? 0.5113 0.6717 0.5067 -0.0166 0.0447  0.0120  501  HIS B CA  
12701 C C   . HIS B 503  ? 0.5588 0.7339 0.5596 -0.0169 0.0474  0.0135  501  HIS B C   
12702 O O   . HIS B 503  ? 0.5143 0.6966 0.5158 -0.0121 0.0501  0.0123  501  HIS B O   
12703 C CB  . HIS B 503  ? 0.5165 0.6699 0.5145 -0.0138 0.0421  0.0095  501  HIS B CB  
12704 C CG  . HIS B 503  ? 0.5175 0.6774 0.5198 -0.0084 0.0435  0.0076  501  HIS B CG  
12705 N ND1 . HIS B 503  ? 0.5405 0.7096 0.5492 -0.0092 0.0439  0.0088  501  HIS B ND1 
12706 C CD2 . HIS B 503  ? 0.5305 0.6887 0.5317 -0.0021 0.0444  0.0047  501  HIS B CD2 
12707 C CE1 . HIS B 503  ? 0.5621 0.7349 0.5733 -0.0034 0.0450  0.0067  501  HIS B CE1 
12708 N NE2 . HIS B 503  ? 0.5561 0.7223 0.5628 0.0009  0.0454  0.0042  501  HIS B NE2 
12709 N N   . ARG B 504  ? 0.4846 0.6644 0.4892 -0.0224 0.0465  0.0163  502  ARG B N   
12710 C CA  . ARG B 504  ? 0.4455 0.6395 0.4562 -0.0227 0.0486  0.0178  502  ARG B CA  
12711 C C   . ARG B 504  ? 0.4697 0.6744 0.4793 -0.0237 0.0522  0.0198  502  ARG B C   
12712 O O   . ARG B 504  ? 0.4729 0.6897 0.4866 -0.0209 0.0549  0.0198  502  ARG B O   
12713 C CB  . ARG B 504  ? 0.4210 0.6163 0.4360 -0.0285 0.0462  0.0200  502  ARG B CB  
12714 C CG  . ARG B 504  ? 0.4503 0.6387 0.4679 -0.0265 0.0433  0.0179  502  ARG B CG  
12715 C CD  . ARG B 504  ? 0.3893 0.5747 0.4088 -0.0327 0.0403  0.0199  502  ARG B CD  
12716 N NE  . ARG B 504  ? 0.3752 0.5729 0.3995 -0.0369 0.0412  0.0227  502  ARG B NE  
12717 C CZ  . ARG B 504  ? 0.4020 0.6100 0.4324 -0.0350 0.0420  0.0226  502  ARG B CZ  
12718 N NH1 . ARG B 504  ? 0.3861 0.5938 0.4186 -0.0286 0.0422  0.0198  502  ARG B NH1 
12719 N NH2 . ARG B 504  ? 0.3837 0.6026 0.4184 -0.0396 0.0425  0.0255  502  ARG B NH2 
12720 N N   . ILE B 505  ? 0.4417 0.6423 0.4459 -0.0275 0.0524  0.0215  503  ILE B N   
12721 C CA  . ILE B 505  ? 0.4798 0.6902 0.4823 -0.0287 0.0559  0.0236  503  ILE B CA  
12722 C C   . ILE B 505  ? 0.5185 0.7330 0.5194 -0.0213 0.0590  0.0209  503  ILE B C   
12723 O O   . ILE B 505  ? 0.4728 0.6974 0.4751 -0.0200 0.0618  0.0217  503  ILE B O   
12724 C CB  . ILE B 505  ? 0.4838 0.6873 0.4798 -0.0340 0.0552  0.0258  503  ILE B CB  
12725 N N   . ASN B 506  ? 0.5032 0.7076 0.5011 -0.0161 0.0577  0.0174  504  ASN B N   
12726 C CA  . ASN B 506  ? 0.5757 0.7817 0.5712 -0.0090 0.0601  0.0144  504  ASN B CA  
12727 C C   . ASN B 506  ? 0.5783 0.7887 0.5792 -0.0032 0.0604  0.0120  504  ASN B C   
12728 O O   . ASN B 506  ? 0.5887 0.7992 0.5876 0.0032  0.0621  0.0092  504  ASN B O   
12729 C CB  . ASN B 506  ? 0.5780 0.7702 0.5661 -0.0068 0.0586  0.0121  504  ASN B CB  
12730 C CG  . ASN B 506  ? 0.5967 0.7865 0.5785 -0.0108 0.0593  0.0142  504  ASN B CG  
12731 O OD1 . ASN B 506  ? 0.5934 0.7931 0.5745 -0.0120 0.0625  0.0161  504  ASN B OD1 
12732 N ND2 . ASN B 506  ? 0.6513 0.8283 0.6284 -0.0129 0.0563  0.0138  504  ASN B ND2 
12733 N N   . ASP B 507  ? 0.5111 0.7248 0.5184 -0.0053 0.0588  0.0130  505  ASP B N   
12734 C CA  . ASP B 507  ? 0.5523 0.7707 0.5649 -0.0001 0.0590  0.0111  505  ASP B CA  
12735 C C   . ASP B 507  ? 0.6133 0.8439 0.6309 0.0000  0.0606  0.0128  505  ASP B C   
12736 O O   . ASP B 507  ? 0.5658 0.8016 0.5875 -0.0056 0.0596  0.0157  505  ASP B O   
12737 C CB  . ASP B 507  ? 0.5714 0.7834 0.5876 -0.0020 0.0553  0.0109  505  ASP B CB  
12738 C CG  . ASP B 507  ? 0.6219 0.8334 0.6413 0.0044  0.0548  0.0081  505  ASP B CG  
12739 O OD1 . ASP B 507  ? 0.6960 0.9169 0.7176 0.0092  0.0574  0.0073  505  ASP B OD1 
12740 O OD2 . ASP B 507  ? 0.7447 0.9462 0.7640 0.0047  0.0518  0.0067  505  ASP B OD2 
12741 N N   . PRO B 508  ? 0.6489 0.8832 0.6663 0.0059  0.0625  0.0111  506  PRO B N   
12742 C CA  . PRO B 508  ? 0.5984 0.8436 0.6204 0.0059  0.0638  0.0128  506  PRO B CA  
12743 C C   . PRO B 508  ? 0.6189 0.8693 0.6483 0.0057  0.0620  0.0134  506  PRO B C   
12744 O O   . PRO B 508  ? 0.6783 0.9381 0.7121 0.0037  0.0625  0.0155  506  PRO B O   
12745 C CB  . PRO B 508  ? 0.6919 0.9379 0.7112 0.0131  0.0660  0.0102  506  PRO B CB  
12746 C CG  . PRO B 508  ? 0.6893 0.9248 0.7014 0.0154  0.0662  0.0078  506  PRO B CG  
12747 C CD  . PRO B 508  ? 0.6104 0.8388 0.6229 0.0127  0.0636  0.0076  506  PRO B CD  
12748 N N   . LYS B 509  ? 0.6327 0.8775 0.6635 0.0076  0.0600  0.0116  507  LYS B N   
12749 C CA  . LYS B 509  ? 0.6188 0.8677 0.6562 0.0072  0.0581  0.0122  507  LYS B CA  
12750 C C   . LYS B 509  ? 0.6659 0.9172 0.7061 -0.0008 0.0563  0.0154  507  LYS B C   
12751 O O   . LYS B 509  ? 0.7234 0.9786 0.7690 -0.0019 0.0546  0.0162  507  LYS B O   
12752 C CB  . LYS B 509  ? 0.5489 0.7904 0.5864 0.0115  0.0565  0.0094  507  LYS B CB  
12753 N N   . VAL B 510  ? 0.6629 0.9117 0.6995 -0.0063 0.0566  0.0172  508  VAL B N   
12754 C CA  . VAL B 510  ? 0.6027 0.8524 0.6411 -0.0143 0.0548  0.0203  508  VAL B CA  
12755 C C   . VAL B 510  ? 0.5816 0.8388 0.6200 -0.0180 0.0563  0.0230  508  VAL B C   
12756 O O   . VAL B 510  ? 0.6332 0.8892 0.6668 -0.0177 0.0583  0.0232  508  VAL B O   
12757 C CB  . VAL B 510  ? 0.5517 0.7915 0.5855 -0.0182 0.0535  0.0204  508  VAL B CB  
12758 C CG1 . VAL B 510  ? 0.5732 0.8130 0.6089 -0.0263 0.0513  0.0234  508  VAL B CG1 
12759 C CG2 . VAL B 510  ? 0.5255 0.7578 0.5587 -0.0137 0.0524  0.0174  508  VAL B CG2 
12760 N N   . SER B 511  ? 0.5490 0.8138 0.5927 -0.0215 0.0553  0.0253  509  SER B N   
12761 C CA  . SER B 511  ? 0.5739 0.8466 0.6182 -0.0251 0.0566  0.0280  509  SER B CA  
12762 C C   . SER B 511  ? 0.5746 0.8430 0.6156 -0.0330 0.0556  0.0307  509  SER B C   
12763 O O   . SER B 511  ? 0.5631 0.8234 0.6025 -0.0363 0.0534  0.0308  509  SER B O   
12764 C CB  . SER B 511  ? 0.5874 0.8700 0.6386 -0.0260 0.0557  0.0294  509  SER B CB  
12765 O OG  . SER B 511  ? 0.5626 0.8431 0.6162 -0.0317 0.0526  0.0309  509  SER B OG  
12766 N N   . ILE B 512  ? 0.5184 0.7920 0.5582 -0.0361 0.0572  0.0331  510  ILE B N   
12767 C CA  . ILE B 512  ? 0.5275 0.7978 0.5648 -0.0441 0.0560  0.0361  510  ILE B CA  
12768 C C   . ILE B 512  ? 0.5707 0.8425 0.6124 -0.0497 0.0529  0.0380  510  ILE B C   
12769 O O   . ILE B 512  ? 0.5380 0.8034 0.5774 -0.0561 0.0508  0.0398  510  ILE B O   
12770 C CB  . ILE B 512  ? 0.4042 0.6799 0.4391 -0.0461 0.0584  0.0383  510  ILE B CB  
12771 N N   . ASP B 513  ? 0.5195 0.7991 0.5674 -0.0474 0.0524  0.0376  511  ASP B N   
12772 C CA  . ASP B 513  ? 0.5093 0.7900 0.5613 -0.0523 0.0493  0.0390  511  ASP B CA  
12773 C C   . ASP B 513  ? 0.4490 0.7195 0.4998 -0.0531 0.0467  0.0376  511  ASP B C   
12774 O O   . ASP B 513  ? 0.4509 0.7166 0.5010 -0.0595 0.0440  0.0393  511  ASP B O   
12775 C CB  . ASP B 513  ? 0.5271 0.8182 0.5856 -0.0490 0.0493  0.0387  511  ASP B CB  
12776 C CG  . ASP B 513  ? 0.5415 0.8435 0.6024 -0.0512 0.0508  0.0411  511  ASP B CG  
12777 O OD1 . ASP B 513  ? 0.5407 0.8420 0.5991 -0.0572 0.0508  0.0437  511  ASP B OD1 
12778 O OD2 . ASP B 513  ? 0.6302 0.9414 0.6954 -0.0468 0.0520  0.0406  511  ASP B OD2 
12779 N N   . GLU B 514  ? 0.4500 0.7169 0.5003 -0.0467 0.0473  0.0345  512  GLU B N   
12780 C CA  . GLU B 514  ? 0.5118 0.7691 0.5608 -0.0472 0.0450  0.0331  512  GLU B CA  
12781 C C   . GLU B 514  ? 0.4563 0.7040 0.4993 -0.0520 0.0445  0.0341  512  GLU B C   
12782 O O   . GLU B 514  ? 0.4330 0.6736 0.4752 -0.0561 0.0419  0.0345  512  GLU B O   
12783 C CB  . GLU B 514  ? 0.4648 0.7200 0.5140 -0.0391 0.0461  0.0296  512  GLU B CB  
12784 C CG  . GLU B 514  ? 0.5843 0.8480 0.6387 -0.0336 0.0467  0.0284  512  GLU B CG  
12785 C CD  . GLU B 514  ? 0.6136 0.8740 0.6673 -0.0257 0.0477  0.0250  512  GLU B CD  
12786 O OE1 . GLU B 514  ? 0.7032 0.9554 0.7554 -0.0251 0.0463  0.0234  512  GLU B OE1 
12787 O OE2 . GLU B 514  ? 0.6548 0.9204 0.7093 -0.0200 0.0498  0.0238  512  GLU B OE2 
12788 N N   . LEU B 515  ? 0.4389 0.6860 0.4774 -0.0515 0.0469  0.0346  513  LEU B N   
12789 C CA  . LEU B 515  ? 0.4391 0.6767 0.4712 -0.0555 0.0464  0.0355  513  LEU B CA  
12790 C C   . LEU B 515  ? 0.3984 0.6343 0.4297 -0.0640 0.0444  0.0389  513  LEU B C   
12791 O O   . LEU B 515  ? 0.4080 0.6344 0.4350 -0.0683 0.0427  0.0398  513  LEU B O   
12792 C CB  . LEU B 515  ? 0.3810 0.6184 0.4081 -0.0523 0.0495  0.0350  513  LEU B CB  
12793 C CG  . LEU B 515  ? 0.3542 0.5900 0.3801 -0.0442 0.0513  0.0314  513  LEU B CG  
12794 C CD1 . LEU B 515  ? 0.4490 0.6859 0.4701 -0.0415 0.0543  0.0312  513  LEU B CD1 
12795 C CD2 . LEU B 515  ? 0.3828 0.6068 0.4057 -0.0435 0.0493  0.0295  513  LEU B CD2 
12796 N N   . ILE B 516  ? 0.3615 0.6062 0.3966 -0.0665 0.0444  0.0409  514  ILE B N   
12797 C CA  . ILE B 516  ? 0.3212 0.5648 0.3556 -0.0745 0.0423  0.0442  514  ILE B CA  
12798 C C   . ILE B 516  ? 0.3234 0.5663 0.3619 -0.0778 0.0389  0.0445  514  ILE B C   
12799 O O   . ILE B 516  ? 0.3628 0.6047 0.4011 -0.0844 0.0369  0.0470  514  ILE B O   
12800 C CB  . ILE B 516  ? 0.3855 0.6383 0.4208 -0.0763 0.0442  0.0466  514  ILE B CB  
12801 C CG1 . ILE B 516  ? 0.3750 0.6399 0.4174 -0.0734 0.0448  0.0462  514  ILE B CG1 
12802 C CG2 . ILE B 516  ? 0.3972 0.6503 0.4281 -0.0729 0.0476  0.0461  514  ILE B CG2 
12803 C CD1 . ILE B 516  ? 0.3907 0.6659 0.4346 -0.0749 0.0468  0.0485  514  ILE B CD1 
12804 N N   . ALA B 517  ? 0.3831 0.6263 0.4250 -0.0734 0.0383  0.0419  515  ALA B N   
12805 C CA  . ALA B 517  ? 0.4021 0.6437 0.4472 -0.0762 0.0350  0.0419  515  ALA B CA  
12806 C C   . ALA B 517  ? 0.3529 0.5828 0.3935 -0.0826 0.0321  0.0431  515  ALA B C   
12807 O O   . ALA B 517  ? 0.3515 0.5726 0.3873 -0.0822 0.0324  0.0423  515  ALA B O   
12808 C CB  . ALA B 517  ? 0.3312 0.5727 0.3794 -0.0700 0.0348  0.0388  515  ALA B CB  
12809 N N   . ASP B 518  ? 0.3387 0.5683 0.3806 -0.0884 0.0293  0.0449  516  ASP B N   
12810 C CA  . ASP B 518  ? 0.3573 0.5756 0.3949 -0.0949 0.0262  0.0461  516  ASP B CA  
12811 C C   . ASP B 518  ? 0.2904 0.5014 0.3284 -0.0936 0.0239  0.0438  516  ASP B C   
12812 O O   . ASP B 518  ? 0.3146 0.5290 0.3570 -0.0934 0.0221  0.0431  516  ASP B O   
12813 C CB  . ASP B 518  ? 0.3237 0.5447 0.3623 -0.1014 0.0240  0.0488  516  ASP B CB  
12814 C CG  . ASP B 518  ? 0.3904 0.5989 0.4237 -0.1081 0.0208  0.0502  516  ASP B CG  
12815 O OD1 . ASP B 518  ? 0.3267 0.5245 0.3560 -0.1078 0.0199  0.0490  516  ASP B OD1 
12816 O OD2 . ASP B 518  ? 0.4056 0.6149 0.4387 -0.1138 0.0190  0.0525  516  ASP B OD2 
12817 N N   . PRO B 519  ? 0.2514 0.4523 0.2850 -0.0929 0.0238  0.0427  517  PRO B N   
12818 C CA  . PRO B 519  ? 0.2910 0.4816 0.3239 -0.0902 0.0209  0.0398  517  PRO B CA  
12819 C C   . PRO B 519  ? 0.2823 0.4690 0.3157 -0.0962 0.0172  0.0408  517  PRO B C   
12820 O O   . PRO B 519  ? 0.2723 0.4572 0.3081 -0.0941 0.0152  0.0388  517  PRO B O   
12821 C CB  . PRO B 519  ? 0.2954 0.4717 0.3213 -0.0877 0.0205  0.0382  517  PRO B CB  
12822 C CG  . PRO B 519  ? 0.3234 0.5004 0.3455 -0.0920 0.0220  0.0411  517  PRO B CG  
12823 C CD  . PRO B 519  ? 0.2523 0.4464 0.2796 -0.0930 0.0252  0.0433  517  PRO B CD  
12824 N N   . VAL B 520  ? 0.2813 0.4665 0.3122 -0.1037 0.0160  0.0439  518  VAL B N   
12825 C CA  . VAL B 520  ? 0.2925 0.4720 0.3227 -0.1092 0.0120  0.0446  518  VAL B CA  
12826 C C   . VAL B 520  ? 0.3109 0.5003 0.3473 -0.1084 0.0112  0.0443  518  VAL B C   
12827 O O   . VAL B 520  ? 0.2891 0.4752 0.3268 -0.1089 0.0085  0.0430  518  VAL B O   
12828 C CB  . VAL B 520  ? 0.3157 0.4898 0.3410 -0.1157 0.0108  0.0475  518  VAL B CB  
12829 C CG1 . VAL B 520  ? 0.3523 0.5184 0.3758 -0.1211 0.0064  0.0479  518  VAL B CG1 
12830 C CG2 . VAL B 520  ? 0.3067 0.4718 0.3258 -0.1158 0.0119  0.0479  518  VAL B CG2 
12831 N N   . GLU B 521  ? 0.2924 0.4939 0.3325 -0.1070 0.0135  0.0455  519  GLU B N   
12832 C CA  . GLU B 521  ? 0.3082 0.5195 0.3540 -0.1063 0.0128  0.0454  519  GLU B CA  
12833 C C   . GLU B 521  ? 0.3064 0.5216 0.3565 -0.0996 0.0136  0.0426  519  GLU B C   
12834 O O   . GLU B 521  ? 0.3136 0.5317 0.3671 -0.0994 0.0116  0.0419  519  GLU B O   
12835 C CB  . GLU B 521  ? 0.3247 0.5477 0.3732 -0.1068 0.0149  0.0476  519  GLU B CB  
12836 C CG  . GLU B 521  ? 0.3482 0.5679 0.3930 -0.1139 0.0137  0.0506  519  GLU B CG  
12837 C CD  . GLU B 521  ? 0.4109 0.6232 0.4540 -0.1198 0.0094  0.0512  519  GLU B CD  
12838 O OE1 . GLU B 521  ? 0.4134 0.6286 0.4602 -0.1189 0.0076  0.0501  519  GLU B OE1 
12839 O OE2 . GLU B 521  ? 0.4911 0.6944 0.5289 -0.1252 0.0077  0.0528  519  GLU B OE2 
12840 N N   . VAL B 522  ? 0.2998 0.5149 0.3494 -0.0941 0.0163  0.0410  520  VAL B N   
12841 C CA  . VAL B 522  ? 0.2850 0.5027 0.3382 -0.0877 0.0169  0.0383  520  VAL B CA  
12842 C C   . VAL B 522  ? 0.3526 0.5607 0.4045 -0.0891 0.0137  0.0367  520  VAL B C   
12843 O O   . VAL B 522  ? 0.3201 0.5311 0.3757 -0.0869 0.0123  0.0354  520  VAL B O   
12844 C CB  . VAL B 522  ? 0.3197 0.5388 0.3722 -0.0815 0.0205  0.0368  520  VAL B CB  
12845 C CG1 . VAL B 522  ? 0.3326 0.5526 0.3880 -0.0746 0.0208  0.0338  520  VAL B CG1 
12846 C CG2 . VAL B 522  ? 0.3983 0.6274 0.4522 -0.0798 0.0236  0.0381  520  VAL B CG2 
12847 N N   . VAL B 523  ? 0.2787 0.4728 0.3242 -0.0916 0.0121  0.0364  521  VAL B N   
12848 C CA  . VAL B 523  ? 0.2638 0.4452 0.3063 -0.0916 0.0086  0.0344  521  VAL B CA  
12849 C C   . VAL B 523  ? 0.2759 0.4601 0.3207 -0.0975 0.0055  0.0357  521  VAL B C   
12850 O O   . VAL B 523  ? 0.2719 0.4534 0.3178 -0.0958 0.0033  0.0339  521  VAL B O   
12851 C CB  . VAL B 523  ? 0.3021 0.4680 0.3371 -0.0927 0.0074  0.0339  521  VAL B CB  
12852 C CG1 . VAL B 523  ? 0.2830 0.4367 0.3149 -0.0941 0.0036  0.0323  521  VAL B CG1 
12853 C CG2 . VAL B 523  ? 0.3289 0.4907 0.3617 -0.0859 0.0099  0.0318  521  VAL B CG2 
12854 N N   . ARG B 524  ? 0.2934 0.4816 0.3381 -0.1040 0.0050  0.0387  522  ARG B N   
12855 C CA  . ARG B 524  ? 0.3471 0.5348 0.3922 -0.1086 0.0017  0.0396  522  ARG B CA  
12856 C C   . ARG B 524  ? 0.3322 0.5301 0.3835 -0.1052 0.0015  0.0387  522  ARG B C   
12857 O O   . ARG B 524  ? 0.3582 0.5536 0.4099 -0.1072 -0.0016 0.0381  522  ARG B O   
12858 C CB  . ARG B 524  ? 0.3243 0.5141 0.3678 -0.1140 0.0016  0.0426  522  ARG B CB  
12859 C CG  . ARG B 524  ? 0.3484 0.5372 0.3918 -0.1193 -0.0020 0.0437  522  ARG B CG  
12860 C CD  . ARG B 524  ? 0.3714 0.5671 0.4154 -0.1234 -0.0014 0.0467  522  ARG B CD  
12861 N NE  . ARG B 524  ? 0.3779 0.5691 0.4175 -0.1255 0.0001  0.0483  522  ARG B NE  
12862 C CZ  . ARG B 524  ? 0.4182 0.5968 0.4515 -0.1301 -0.0020 0.0491  522  ARG B CZ  
12863 N NH1 . ARG B 524  ? 0.4154 0.5840 0.4458 -0.1331 -0.0058 0.0482  522  ARG B NH1 
12864 N NH2 . ARG B 524  ? 0.4015 0.5771 0.4311 -0.1316 -0.0004 0.0507  522  ARG B NH2 
12865 N N   . ALA B 525  ? 0.3031 0.5118 0.3587 -0.0999 0.0047  0.0384  523  ALA B N   
12866 C CA  . ALA B 525  ? 0.3614 0.5804 0.4227 -0.0964 0.0048  0.0379  523  ALA B CA  
12867 C C   . ALA B 525  ? 0.3768 0.5948 0.4402 -0.0906 0.0047  0.0350  523  ALA B C   
12868 O O   . ALA B 525  ? 0.3757 0.6015 0.4436 -0.0873 0.0046  0.0344  523  ALA B O   
12869 C CB  . ALA B 525  ? 0.3698 0.6012 0.4348 -0.0936 0.0080  0.0391  523  ALA B CB  
12870 N N   . MET B 526  ? 0.3422 0.5509 0.4023 -0.0894 0.0048  0.0334  524  MET B N   
12871 C CA  A MET B 526  ? 0.3603 0.5648 0.4208 -0.0830 0.0045  0.0304  524  MET B CA  
12872 C CA  B MET B 526  ? 0.3604 0.5650 0.4209 -0.0830 0.0045  0.0304  524  MET B CA  
12873 C C   . MET B 526  ? 0.3410 0.5423 0.4019 -0.0852 0.0007  0.0297  524  MET B C   
12874 O O   . MET B 526  ? 0.3459 0.5421 0.4041 -0.0916 -0.0020 0.0308  524  MET B O   
12875 C CB  A MET B 526  ? 0.3812 0.5712 0.4354 -0.0797 0.0049  0.0283  524  MET B CB  
12876 C CB  B MET B 526  ? 0.3811 0.5716 0.4356 -0.0794 0.0050  0.0283  524  MET B CB  
12877 C CG  A MET B 526  ? 0.4128 0.6053 0.4664 -0.0761 0.0085  0.0284  524  MET B CG  
12878 C CG  B MET B 526  ? 0.4176 0.6116 0.4725 -0.0737 0.0088  0.0276  524  MET B CG  
12879 S SD  A MET B 526  ? 0.4498 0.6553 0.5095 -0.0685 0.0116  0.0274  524  MET B SD  
12880 S SD  B MET B 526  ? 0.4483 0.6265 0.4958 -0.0714 0.0093  0.0259  524  MET B SD  
12881 C CE  A MET B 526  ? 0.4066 0.6022 0.4648 -0.0623 0.0100  0.0239  524  MET B CE  
12882 C CE  B MET B 526  ? 0.4669 0.6497 0.5162 -0.0627 0.0128  0.0240  524  MET B CE  
12883 N N   . PRO B 527  ? 0.3624 0.5662 0.4261 -0.0799 0.0004  0.0278  525  PRO B N   
12884 C CA  . PRO B 527  ? 0.4387 0.6399 0.5026 -0.0819 -0.0031 0.0272  525  PRO B CA  
12885 C C   . PRO B 527  ? 0.4121 0.5970 0.4692 -0.0840 -0.0058 0.0257  525  PRO B C   
12886 O O   . PRO B 527  ? 0.3589 0.5407 0.4145 -0.0893 -0.0090 0.0262  525  PRO B O   
12887 C CB  . PRO B 527  ? 0.4561 0.6619 0.5235 -0.0747 -0.0023 0.0253  525  PRO B CB  
12888 C CG  . PRO B 527  ? 0.4863 0.6899 0.5526 -0.0687 0.0010  0.0241  525  PRO B CG  
12889 C CD  . PRO B 527  ? 0.4531 0.6609 0.5192 -0.0719 0.0031  0.0262  525  PRO B CD  
12890 N N   . VAL B 528  ? 0.3602 0.5346 0.4129 -0.0800 -0.0046 0.0239  526  VAL B N   
12891 C CA  . VAL B 528  ? 0.3259 0.4849 0.3721 -0.0815 -0.0067 0.0225  526  VAL B CA  
12892 C C   . VAL B 528  ? 0.2860 0.4396 0.3285 -0.0828 -0.0051 0.0233  526  VAL B C   
12893 O O   . VAL B 528  ? 0.3334 0.4855 0.3753 -0.0778 -0.0026 0.0223  526  VAL B O   
12894 C CB  . VAL B 528  ? 0.3163 0.4673 0.3606 -0.0754 -0.0069 0.0195  526  VAL B CB  
12895 C CG1 . VAL B 528  ? 0.3057 0.4411 0.3434 -0.0766 -0.0088 0.0181  526  VAL B CG1 
12896 C CG2 . VAL B 528  ? 0.3291 0.4853 0.3767 -0.0742 -0.0086 0.0189  526  VAL B CG2 
12897 N N   . VAL B 529  ? 0.2830 0.4336 0.3228 -0.0896 -0.0066 0.0252  527  VAL B N   
12898 C CA  . VAL B 529  ? 0.2730 0.4188 0.3092 -0.0912 -0.0052 0.0264  527  VAL B CA  
12899 C C   . VAL B 529  ? 0.2755 0.4073 0.3062 -0.0872 -0.0054 0.0240  527  VAL B C   
12900 O O   . VAL B 529  ? 0.2888 0.4103 0.3160 -0.0877 -0.0080 0.0224  527  VAL B O   
12901 C CB  . VAL B 529  ? 0.2345 0.3787 0.2684 -0.0995 -0.0072 0.0289  527  VAL B CB  
12902 C CG1 . VAL B 529  ? 0.2401 0.3770 0.2691 -0.1010 -0.0061 0.0300  527  VAL B CG1 
12903 C CG2 . VAL B 529  ? 0.2638 0.4234 0.3036 -0.1034 -0.0065 0.0316  527  VAL B CG2 
12904 N N   . GLY B 530  ? 0.2401 0.3717 0.2702 -0.0832 -0.0026 0.0236  528  GLY B N   
12905 C CA  . GLY B 530  ? 0.2572 0.3762 0.2823 -0.0797 -0.0027 0.0216  528  GLY B CA  
12906 C C   . GLY B 530  ? 0.2321 0.3481 0.2581 -0.0733 -0.0025 0.0187  528  GLY B C   
12907 O O   . GLY B 530  ? 0.2283 0.3332 0.2503 -0.0711 -0.0033 0.0169  528  GLY B O   
12908 N N   . ALA B 531  ? 0.2268 0.3523 0.2579 -0.0703 -0.0016 0.0182  529  ALA B N   
12909 C CA  . ALA B 531  ? 0.2120 0.3347 0.2438 -0.0642 -0.0013 0.0157  529  ALA B CA  
12910 C C   . ALA B 531  ? 0.2089 0.3274 0.2390 -0.0593 0.0009  0.0144  529  ALA B C   
12911 O O   . ALA B 531  ? 0.2425 0.3661 0.2733 -0.0590 0.0032  0.0155  529  ALA B O   
12912 C CB  . ALA B 531  ? 0.2783 0.4127 0.3160 -0.0617 -0.0005 0.0157  529  ALA B CB  
12913 N N   . LYS B 532  ? 0.1996 0.3091 0.2273 -0.0556 0.0002  0.0122  530  LYS B N   
12914 C CA  . LYS B 532  ? 0.2235 0.3287 0.2497 -0.0508 0.0020  0.0108  530  LYS B CA  
12915 C C   . LYS B 532  ? 0.2098 0.3249 0.2402 -0.0466 0.0047  0.0107  530  LYS B C   
12916 O O   . LYS B 532  ? 0.2179 0.3416 0.2524 -0.0459 0.0049  0.0110  530  LYS B O   
12917 C CB  . LYS B 532  ? 0.2500 0.3459 0.2742 -0.0475 0.0008  0.0085  530  LYS B CB  
12918 C CG  . LYS B 532  ? 0.2594 0.3512 0.2827 -0.0422 0.0024  0.0068  530  LYS B CG  
12919 C CD  . LYS B 532  ? 0.2615 0.3459 0.2837 -0.0393 0.0011  0.0047  530  LYS B CD  
12920 C CE  . LYS B 532  ? 0.2361 0.3260 0.2618 -0.0372 0.0009  0.0041  530  LYS B CE  
12921 N NZ  . LYS B 532  ? 0.2359 0.3332 0.2651 -0.0329 0.0032  0.0039  530  LYS B NZ  
12922 N N   . HIS B 533  ? 0.1856 0.2992 0.2146 -0.0437 0.0067  0.0102  531  HIS B N   
12923 C CA  . HIS B 533  ? 0.2044 0.3254 0.2365 -0.0389 0.0092  0.0097  531  HIS B CA  
12924 C C   . HIS B 533  ? 0.2039 0.3250 0.2383 -0.0347 0.0087  0.0079  531  HIS B C   
12925 O O   . HIS B 533  ? 0.2147 0.3270 0.2469 -0.0333 0.0073  0.0064  531  HIS B O   
12926 C CB  . HIS B 533  ? 0.2030 0.3191 0.2320 -0.0361 0.0108  0.0088  531  HIS B CB  
12927 C CG  . HIS B 533  ? 0.2464 0.3706 0.2777 -0.0322 0.0135  0.0086  531  HIS B CG  
12928 N ND1 . HIS B 533  ? 0.2346 0.3621 0.2688 -0.0272 0.0143  0.0072  531  HIS B ND1 
12929 C CD2 . HIS B 533  ? 0.3088 0.4379 0.3396 -0.0325 0.0156  0.0097  531  HIS B CD2 
12930 C CE1 . HIS B 533  ? 0.3069 0.4410 0.3422 -0.0244 0.0168  0.0073  531  HIS B CE1 
12931 N NE2 . HIS B 533  ? 0.4015 0.5370 0.4349 -0.0275 0.0177  0.0087  531  HIS B NE2 
12932 N N   . ASP B 534  ? 0.2198 0.3510 0.2586 -0.0325 0.0098  0.0083  532  ASP B N   
12933 C CA  . ASP B 534  ? 0.2540 0.3861 0.2952 -0.0285 0.0093  0.0070  532  ASP B CA  
12934 C C   . ASP B 534  ? 0.2558 0.3812 0.2952 -0.0232 0.0102  0.0049  532  ASP B C   
12935 O O   . ASP B 534  ? 0.2822 0.4045 0.3220 -0.0205 0.0093  0.0037  532  ASP B O   
12936 C CB  . ASP B 534  ? 0.2834 0.4281 0.3295 -0.0268 0.0106  0.0078  532  ASP B CB  
12937 C CG  . ASP B 534  ? 0.4496 0.6015 0.4984 -0.0317 0.0092  0.0097  532  ASP B CG  
12938 O OD1 . ASP B 534  ? 0.5041 0.6508 0.5514 -0.0348 0.0068  0.0097  532  ASP B OD1 
12939 O OD2 . ASP B 534  ? 0.5593 0.7222 0.6116 -0.0324 0.0106  0.0112  532  ASP B OD2 
12940 N N   . ARG B 535  ? 0.1979 0.3211 0.2352 -0.0218 0.0119  0.0045  533  ARG B N   
12941 C CA  . ARG B 535  ? 0.2313 0.3493 0.2672 -0.0168 0.0128  0.0027  533  ARG B CA  
12942 C C   . ARG B 535  ? 0.2423 0.3491 0.2739 -0.0175 0.0119  0.0017  533  ARG B C   
12943 O O   . ARG B 535  ? 0.2584 0.3608 0.2884 -0.0139 0.0127  0.0003  533  ARG B O   
12944 C CB  . ARG B 535  ? 0.2810 0.4051 0.3178 -0.0136 0.0153  0.0026  533  ARG B CB  
12945 N N   . ILE B 536  ? 0.1962 0.2984 0.2257 -0.0219 0.0102  0.0024  534  ILE B N   
12946 C CA  . ILE B 536  ? 0.1725 0.2642 0.1980 -0.0225 0.0091  0.0016  534  ILE B CA  
12947 C C   . ILE B 536  ? 0.1820 0.2686 0.2071 -0.0239 0.0069  0.0011  534  ILE B C   
12948 O O   . ILE B 536  ? 0.2124 0.3010 0.2379 -0.0277 0.0056  0.0022  534  ILE B O   
12949 C CB  . ILE B 536  ? 0.1857 0.2755 0.2084 -0.0264 0.0091  0.0029  534  ILE B CB  
12950 C CG1 . ILE B 536  ? 0.2000 0.2951 0.2228 -0.0249 0.0114  0.0034  534  ILE B CG1 
12951 C CG2 . ILE B 536  ? 0.2068 0.2856 0.2255 -0.0268 0.0077  0.0021  534  ILE B CG2 
12952 C CD1 . ILE B 536  ? 0.2683 0.3625 0.2882 -0.0287 0.0116  0.0049  534  ILE B CD1 
12953 N N   . ALA B 537  ? 0.1787 0.2591 0.2030 -0.0208 0.0064  -0.0005 535  ALA B N   
12954 C CA  . ALA B 537  ? 0.1891 0.2649 0.2129 -0.0215 0.0046  -0.0011 535  ALA B CA  
12955 C C   . ALA B 537  ? 0.1712 0.2389 0.1912 -0.0246 0.0031  -0.0011 535  ALA B C   
12956 O O   . ALA B 537  ? 0.1777 0.2404 0.1953 -0.0242 0.0034  -0.0014 535  ALA B O   
12957 C CB  . ALA B 537  ? 0.2089 0.2811 0.2331 -0.0171 0.0049  -0.0028 535  ALA B CB  
12958 N N   . LEU B 538  ? 0.1782 0.2447 0.1976 -0.0277 0.0013  -0.0007 536  LEU B N   
12959 C CA  . LEU B 538  ? 0.1772 0.2346 0.1928 -0.0295 -0.0004 -0.0011 536  LEU B CA  
12960 C C   . LEU B 538  ? 0.1946 0.2458 0.2094 -0.0257 -0.0002 -0.0029 536  LEU B C   
12961 O O   . LEU B 538  ? 0.1916 0.2450 0.2085 -0.0224 0.0005  -0.0037 536  LEU B O   
12962 C CB  . LEU B 538  ? 0.2008 0.2573 0.2158 -0.0325 -0.0024 -0.0010 536  LEU B CB  
12963 C CG  . LEU B 538  ? 0.2160 0.2764 0.2308 -0.0375 -0.0032 0.0008  536  LEU B CG  
12964 C CD1 . LEU B 538  ? 0.2614 0.3211 0.2758 -0.0400 -0.0053 0.0007  536  LEU B CD1 
12965 C CD2 . LEU B 538  ? 0.2355 0.2903 0.2468 -0.0404 -0.0037 0.0017  536  LEU B CD2 
12966 N N   . PRO B 539  ? 0.1753 0.2186 0.1868 -0.0260 -0.0010 -0.0034 537  PRO B N   
12967 C CA  . PRO B 539  ? 0.1769 0.2147 0.1879 -0.0225 -0.0010 -0.0050 537  PRO B CA  
12968 C C   . PRO B 539  ? 0.1679 0.2056 0.1800 -0.0211 -0.0015 -0.0059 537  PRO B C   
12969 O O   . PRO B 539  ? 0.1743 0.2122 0.1879 -0.0176 -0.0006 -0.0068 537  PRO B O   
12970 C CB  . PRO B 539  ? 0.2058 0.2357 0.2131 -0.0240 -0.0022 -0.0051 537  PRO B CB  
12971 C CG  . PRO B 539  ? 0.1857 0.2177 0.1919 -0.0272 -0.0021 -0.0035 537  PRO B CG  
12972 C CD  . PRO B 539  ? 0.1814 0.2208 0.1898 -0.0294 -0.0019 -0.0024 537  PRO B CD  
12973 N N   . ALA B 540  ? 0.1689 0.2064 0.1801 -0.0237 -0.0029 -0.0057 538  ALA B N   
12974 C CA  . ALA B 540  ? 0.1867 0.2240 0.1985 -0.0223 -0.0034 -0.0065 538  ALA B CA  
12975 C C   . ALA B 540  ? 0.1975 0.2421 0.2129 -0.0201 -0.0023 -0.0063 538  ALA B C   
12976 O O   . ALA B 540  ? 0.1963 0.2405 0.2123 -0.0179 -0.0023 -0.0071 538  ALA B O   
12977 C CB  . ALA B 540  ? 0.2046 0.2404 0.2144 -0.0258 -0.0054 -0.0063 538  ALA B CB  
12978 N N   . GLU B 541  ? 0.1933 0.2444 0.2110 -0.0204 -0.0012 -0.0053 539  GLU B N   
12979 C CA  . GLU B 541  ? 0.1828 0.2414 0.2038 -0.0185 -0.0003 -0.0049 539  GLU B CA  
12980 C C   . GLU B 541  ? 0.1687 0.2289 0.1914 -0.0148 0.0016  -0.0053 539  GLU B C   
12981 O O   . GLU B 541  ? 0.1942 0.2609 0.2196 -0.0131 0.0025  -0.0049 539  GLU B O   
12982 C CB  . GLU B 541  ? 0.2151 0.2809 0.2377 -0.0217 -0.0006 -0.0034 539  GLU B CB  
12983 C CG  . GLU B 541  ? 0.2573 0.3210 0.2782 -0.0253 -0.0028 -0.0033 539  GLU B CG  
12984 C CD  . GLU B 541  ? 0.3597 0.4297 0.3818 -0.0294 -0.0036 -0.0017 539  GLU B CD  
12985 O OE1 . GLU B 541  ? 0.3652 0.4423 0.3899 -0.0296 -0.0023 -0.0006 539  GLU B OE1 
12986 O OE2 . GLU B 541  ? 0.4077 0.4755 0.4280 -0.0327 -0.0056 -0.0016 539  GLU B OE2 
12987 N N   . LEU B 542  ? 0.1594 0.2137 0.1804 -0.0133 0.0020  -0.0061 540  LEU B N   
12988 C CA  . LEU B 542  ? 0.1864 0.2416 0.2085 -0.0101 0.0035  -0.0066 540  LEU B CA  
12989 C C   . LEU B 542  ? 0.1809 0.2387 0.2053 -0.0067 0.0041  -0.0070 540  LEU B C   
12990 O O   . LEU B 542  ? 0.2056 0.2665 0.2314 -0.0042 0.0054  -0.0071 540  LEU B O   
12991 C CB  . LEU B 542  ? 0.1968 0.2449 0.2169 -0.0090 0.0035  -0.0075 540  LEU B CB  
12992 C CG  . LEU B 542  ? 0.2250 0.2699 0.2427 -0.0110 0.0032  -0.0072 540  LEU B CG  
12993 C CD1 . LEU B 542  ? 0.1932 0.2321 0.2097 -0.0090 0.0033  -0.0082 540  LEU B CD1 
12994 C CD2 . LEU B 542  ? 0.2211 0.2714 0.2394 -0.0117 0.0044  -0.0063 540  LEU B CD2 
12995 N N   . PHE B 543  ? 0.1704 0.2266 0.1947 -0.0065 0.0032  -0.0073 541  PHE B N   
12996 C CA  . PHE B 543  ? 0.1780 0.2357 0.2040 -0.0034 0.0036  -0.0076 541  PHE B CA  
12997 C C   . PHE B 543  ? 0.1790 0.2431 0.2068 -0.0038 0.0032  -0.0068 541  PHE B C   
12998 O O   . PHE B 543  ? 0.2025 0.2678 0.2315 -0.0015 0.0033  -0.0069 541  PHE B O   
12999 C CB  . PHE B 543  ? 0.1725 0.2240 0.1971 -0.0024 0.0032  -0.0085 541  PHE B CB  
13000 C CG  . PHE B 543  ? 0.1933 0.2390 0.2162 -0.0022 0.0034  -0.0092 541  PHE B CG  
13001 C CD1 . PHE B 543  ? 0.2200 0.2655 0.2434 -0.0004 0.0044  -0.0094 541  PHE B CD1 
13002 C CD2 . PHE B 543  ? 0.1801 0.2207 0.2009 -0.0039 0.0024  -0.0096 541  PHE B CD2 
13003 C CE1 . PHE B 543  ? 0.2201 0.2607 0.2421 -0.0004 0.0044  -0.0100 541  PHE B CE1 
13004 C CE2 . PHE B 543  ? 0.1975 0.2331 0.2170 -0.0036 0.0025  -0.0102 541  PHE B CE2 
13005 C CZ  . PHE B 543  ? 0.2084 0.2442 0.2286 -0.0020 0.0034  -0.0103 541  PHE B CZ  
13006 N N   . GLY B 544  ? 0.1875 0.2558 0.2158 -0.0068 0.0027  -0.0059 542  GLY B N   
13007 C CA  . GLY B 544  ? 0.1890 0.2644 0.2194 -0.0074 0.0022  -0.0050 542  GLY B CA  
13008 C C   . GLY B 544  ? 0.2222 0.2959 0.2520 -0.0075 0.0009  -0.0052 542  GLY B C   
13009 O O   . GLY B 544  ? 0.2405 0.3084 0.2677 -0.0092 -0.0002 -0.0058 542  GLY B O   
13010 N N   . ASP B 545  ? 0.2320 0.3108 0.2640 -0.0055 0.0009  -0.0048 543  ASP B N   
13011 C CA  . ASP B 545  ? 0.2429 0.3210 0.2742 -0.0057 -0.0005 -0.0049 543  ASP B CA  
13012 C C   . ASP B 545  ? 0.2636 0.3349 0.2929 -0.0034 -0.0003 -0.0058 543  ASP B C   
13013 O O   . ASP B 545  ? 0.2667 0.3361 0.2946 -0.0038 -0.0014 -0.0060 543  ASP B O   
13014 C CB  . ASP B 545  ? 0.2762 0.3619 0.3103 -0.0039 -0.0006 -0.0040 543  ASP B CB  
13015 C CG  . ASP B 545  ? 0.4577 0.5515 0.4944 -0.0062 -0.0009 -0.0029 543  ASP B CG  
13016 O OD1 . ASP B 545  ? 0.4826 0.5758 0.5182 -0.0102 -0.0018 -0.0026 543  ASP B OD1 
13017 O OD2 . ASP B 545  ? 0.6024 0.7030 0.6421 -0.0040 -0.0002 -0.0022 543  ASP B OD2 
13018 N N   . ALA B 546  ? 0.2189 0.2865 0.2480 -0.0012 0.0010  -0.0064 544  ALA B N   
13019 C CA  . ALA B 546  ? 0.1956 0.2575 0.2233 0.0009  0.0013  -0.0071 544  ALA B CA  
13020 C C   . ALA B 546  ? 0.2074 0.2635 0.2323 -0.0011 0.0004  -0.0079 544  ALA B C   
13021 O O   . ALA B 546  ? 0.2096 0.2630 0.2332 -0.0004 0.0001  -0.0082 544  ALA B O   
13022 C CB  . ALA B 546  ? 0.2473 0.3066 0.2754 0.0033  0.0027  -0.0076 544  ALA B CB  
13023 N N   . ARG B 547  ? 0.1959 0.2498 0.2196 -0.0035 0.0002  -0.0081 545  ARG B N   
13024 C CA  . ARG B 547  ? 0.1995 0.2474 0.2203 -0.0051 -0.0006 -0.0089 545  ARG B CA  
13025 C C   . ARG B 547  ? 0.1915 0.2381 0.2113 -0.0080 -0.0011 -0.0089 545  ARG B C   
13026 O O   . ARG B 547  ? 0.1821 0.2319 0.2033 -0.0084 -0.0005 -0.0083 545  ARG B O   
13027 C CB  . ARG B 547  ? 0.2537 0.2963 0.2738 -0.0028 0.0002  -0.0098 545  ARG B CB  
13028 C CG  . ARG B 547  ? 0.2005 0.2419 0.2215 -0.0018 0.0013  -0.0099 545  ARG B CG  
13029 C CD  . ARG B 547  ? 0.2172 0.2538 0.2376 0.0003  0.0019  -0.0106 545  ARG B CD  
13030 N NE  . ARG B 547  ? 0.1932 0.2299 0.2151 0.0019  0.0029  -0.0106 545  ARG B NE  
13031 C CZ  . ARG B 547  ? 0.1976 0.2310 0.2189 0.0016  0.0031  -0.0111 545  ARG B CZ  
13032 N NH1 . ARG B 547  ? 0.1966 0.2263 0.2160 0.0001  0.0024  -0.0115 545  ARG B NH1 
13033 N NH2 . ARG B 547  ? 0.2156 0.2494 0.2379 0.0031  0.0039  -0.0111 545  ARG B NH2 
13034 N N   . THR B 548  ? 0.1700 0.2118 0.1869 -0.0099 -0.0022 -0.0095 546  THR B N   
13035 C CA  . THR B 548  ? 0.1708 0.2099 0.1860 -0.0127 -0.0029 -0.0094 546  THR B CA  
13036 C C   . THR B 548  ? 0.1603 0.1940 0.1745 -0.0113 -0.0022 -0.0101 546  THR B C   
13037 O O   . THR B 548  ? 0.1653 0.1950 0.1786 -0.0094 -0.0020 -0.0110 546  THR B O   
13038 C CB  . THR B 548  ? 0.1834 0.2191 0.1955 -0.0152 -0.0047 -0.0098 546  THR B CB  
13039 O OG1 . THR B 548  ? 0.2358 0.2769 0.2490 -0.0166 -0.0056 -0.0092 546  THR B OG1 
13040 C CG2 . THR B 548  ? 0.2175 0.2498 0.2275 -0.0183 -0.0056 -0.0096 546  THR B CG2 
13041 N N   . ASN B 549  ? 0.1570 0.1911 0.1714 -0.0122 -0.0018 -0.0096 547  ASN B N   
13042 C CA  . ASN B 549  ? 0.1545 0.1838 0.1680 -0.0110 -0.0013 -0.0101 547  ASN B CA  
13043 C C   . ASN B 549  ? 0.1694 0.1922 0.1797 -0.0123 -0.0026 -0.0108 547  ASN B C   
13044 O O   . ASN B 549  ? 0.1847 0.2065 0.1931 -0.0151 -0.0039 -0.0106 547  ASN B O   
13045 C CB  . ASN B 549  ? 0.1680 0.1995 0.1821 -0.0121 -0.0008 -0.0093 547  ASN B CB  
13046 C CG  . ASN B 549  ? 0.1570 0.1845 0.1704 -0.0106 -0.0003 -0.0098 547  ASN B CG  
13047 O OD1 . ASN B 549  ? 0.1695 0.1938 0.1830 -0.0083 0.0000  -0.0107 547  ASN B OD1 
13048 N ND2 . ASN B 549  ? 0.1667 0.1945 0.1794 -0.0120 -0.0001 -0.0092 547  ASN B ND2 
13049 N N   . SER B 550  ? 0.1567 0.1749 0.1663 -0.0103 -0.0023 -0.0117 548  SER B N   
13050 C CA  . SER B 550  ? 0.1677 0.1796 0.1742 -0.0111 -0.0035 -0.0124 548  SER B CA  
13051 C C   . SER B 550  ? 0.1873 0.1974 0.1921 -0.0137 -0.0043 -0.0117 548  SER B C   
13052 O O   . SER B 550  ? 0.1843 0.1971 0.1903 -0.0141 -0.0036 -0.0109 548  SER B O   
13053 C CB  . SER B 550  ? 0.1553 0.1636 0.1621 -0.0083 -0.0029 -0.0133 548  SER B CB  
13054 O OG  . SER B 550  ? 0.1659 0.1750 0.1741 -0.0075 -0.0022 -0.0129 548  SER B OG  
13055 N N   . ALA B 551  ? 0.1925 0.1974 0.1939 -0.0155 -0.0058 -0.0120 549  ALA B N   
13056 C CA  . ALA B 551  ? 0.2238 0.2257 0.2228 -0.0182 -0.0069 -0.0113 549  ALA B CA  
13057 C C   . ALA B 551  ? 0.1995 0.1949 0.1965 -0.0167 -0.0073 -0.0120 549  ALA B C   
13058 O O   . ALA B 551  ? 0.2035 0.1953 0.1997 -0.0146 -0.0075 -0.0132 549  ALA B O   
13059 C CB  . ALA B 551  ? 0.2083 0.2085 0.2046 -0.0216 -0.0085 -0.0110 549  ALA B CB  
13060 N N   . GLY B 552  ? 0.1946 0.1886 0.1908 -0.0177 -0.0075 -0.0112 550  GLY B N   
13061 C CA  . GLY B 552  ? 0.2148 0.2025 0.2087 -0.0168 -0.0083 -0.0116 550  GLY B CA  
13062 C C   . GLY B 552  ? 0.1999 0.1818 0.1895 -0.0196 -0.0102 -0.0112 550  GLY B C   
13063 O O   . GLY B 552  ? 0.2318 0.2136 0.2200 -0.0221 -0.0111 -0.0111 550  GLY B O   
13064 N N   . LEU B 553  ? 0.2220 0.1986 0.2094 -0.0192 -0.0110 -0.0111 551  LEU B N   
13065 C CA  . LEU B 553  ? 0.2288 0.1988 0.2117 -0.0217 -0.0129 -0.0106 551  LEU B CA  
13066 C C   . LEU B 553  ? 0.2190 0.1881 0.2010 -0.0228 -0.0131 -0.0092 551  LEU B C   
13067 O O   . LEU B 553  ? 0.2513 0.2215 0.2350 -0.0203 -0.0122 -0.0094 551  LEU B O   
13068 C CB  . LEU B 553  ? 0.2560 0.2188 0.2364 -0.0193 -0.0141 -0.0121 551  LEU B CB  
13069 C CG  . LEU B 553  ? 0.2632 0.2257 0.2434 -0.0183 -0.0141 -0.0136 551  LEU B CG  
13070 C CD1 . LEU B 553  ? 0.3037 0.2601 0.2819 -0.0151 -0.0148 -0.0151 551  LEU B CD1 
13071 C CD2 . LEU B 553  ? 0.2917 0.2528 0.2691 -0.0221 -0.0155 -0.0132 551  LEU B CD2 
13072 N N   . ASP B 554  ? 0.2244 0.1913 0.2034 -0.0266 -0.0143 -0.0078 552  ASP B N   
13073 C CA  . ASP B 554  ? 0.2350 0.2014 0.2127 -0.0281 -0.0143 -0.0062 552  ASP B CA  
13074 C C   . ASP B 554  ? 0.2320 0.1895 0.2057 -0.0273 -0.0161 -0.0064 552  ASP B C   
13075 O O   . ASP B 554  ? 0.2407 0.1921 0.2104 -0.0297 -0.0179 -0.0060 552  ASP B O   
13076 C CB  . ASP B 554  ? 0.2536 0.2228 0.2304 -0.0328 -0.0145 -0.0044 552  ASP B CB  
13077 C CG  . ASP B 554  ? 0.2604 0.2297 0.2357 -0.0345 -0.0143 -0.0026 552  ASP B CG  
13078 O OD1 . ASP B 554  ? 0.2597 0.2265 0.2345 -0.0321 -0.0143 -0.0028 552  ASP B OD1 
13079 O OD2 . ASP B 554  ? 0.2720 0.2442 0.2467 -0.0384 -0.0143 -0.0009 552  ASP B OD2 
13080 N N   . LEU B 555  ? 0.2335 0.1902 0.2081 -0.0241 -0.0157 -0.0069 553  LEU B N   
13081 C CA  . LEU B 555  ? 0.2523 0.2010 0.2235 -0.0227 -0.0174 -0.0070 553  LEU B CA  
13082 C C   . LEU B 555  ? 0.2624 0.2079 0.2301 -0.0254 -0.0184 -0.0051 553  LEU B C   
13083 O O   . LEU B 555  ? 0.2580 0.1972 0.2229 -0.0241 -0.0199 -0.0050 553  LEU B O   
13084 C CB  . LEU B 555  ? 0.2558 0.2051 0.2296 -0.0181 -0.0168 -0.0083 553  LEU B CB  
13085 C CG  . LEU B 555  ? 0.2455 0.1977 0.2226 -0.0153 -0.0157 -0.0101 553  LEU B CG  
13086 C CD1 . LEU B 555  ? 0.3014 0.2537 0.2807 -0.0112 -0.0154 -0.0111 553  LEU B CD1 
13087 C CD2 . LEU B 555  ? 0.2928 0.2400 0.2672 -0.0157 -0.0169 -0.0111 553  LEU B CD2 
13088 N N   . SER B 556  ? 0.2429 0.1929 0.2108 -0.0290 -0.0177 -0.0034 554  SER B N   
13089 C CA  . SER B 556  ? 0.2498 0.1965 0.2138 -0.0324 -0.0187 -0.0013 554  SER B CA  
13090 C C   . SER B 556  ? 0.2698 0.2132 0.2307 -0.0367 -0.0201 -0.0004 554  SER B C   
13091 O O   . SER B 556  ? 0.2671 0.2073 0.2244 -0.0401 -0.0211 0.0016  554  SER B O   
13092 C CB  . SER B 556  ? 0.2560 0.2101 0.2220 -0.0337 -0.0169 0.0001  554  SER B CB  
13093 O OG  . SER B 556  ? 0.2629 0.2239 0.2313 -0.0362 -0.0156 0.0006  554  SER B OG  
13094 N N   . ASN B 557  ? 0.2451 0.1889 0.2070 -0.0368 -0.0203 -0.0016 555  ASN B N   
13095 C CA  . ASN B 557  ? 0.2418 0.1827 0.2008 -0.0411 -0.0217 -0.0009 555  ASN B CA  
13096 C C   . ASN B 557  ? 0.2670 0.1971 0.2213 -0.0402 -0.0242 -0.0020 555  ASN B C   
13097 O O   . ASN B 557  ? 0.2602 0.1884 0.2153 -0.0365 -0.0242 -0.0041 555  ASN B O   
13098 C CB  . ASN B 557  ? 0.2414 0.1894 0.2043 -0.0415 -0.0206 -0.0018 555  ASN B CB  
13099 C CG  . ASN B 557  ? 0.2667 0.2125 0.2270 -0.0461 -0.0222 -0.0012 555  ASN B CG  
13100 O OD1 . ASN B 557  ? 0.2775 0.2145 0.2333 -0.0469 -0.0244 -0.0017 555  ASN B OD1 
13101 N ND2 . ASN B 557  ? 0.2692 0.2232 0.2324 -0.0491 -0.0212 -0.0001 555  ASN B ND2 
13102 N N   . GLU B 558  ? 0.2764 0.1994 0.2257 -0.0436 -0.0261 -0.0004 556  GLU B N   
13103 C CA  . GLU B 558  ? 0.3050 0.2168 0.2491 -0.0425 -0.0286 -0.0013 556  GLU B CA  
13104 C C   . GLU B 558  ? 0.3045 0.2137 0.2477 -0.0425 -0.0295 -0.0032 556  GLU B C   
13105 O O   . GLU B 558  ? 0.3131 0.2154 0.2539 -0.0392 -0.0307 -0.0051 556  GLU B O   
13106 C CB  . GLU B 558  ? 0.3476 0.2517 0.2860 -0.0465 -0.0307 0.0009  556  GLU B CB  
13107 C CG  . GLU B 558  ? 0.3317 0.2356 0.2695 -0.0459 -0.0304 0.0026  556  GLU B CG  
13108 C CD  . GLU B 558  ? 0.3482 0.2481 0.2858 -0.0403 -0.0307 0.0012  556  GLU B CD  
13109 O OE1 . GLU B 558  ? 0.3204 0.2159 0.2576 -0.0366 -0.0315 -0.0010 556  GLU B OE1 
13110 O OE2 . GLU B 558  ? 0.3212 0.2226 0.2591 -0.0395 -0.0302 0.0024  556  GLU B OE2 
13111 N N   . GLU B 559  ? 0.2899 0.2045 0.2348 -0.0461 -0.0291 -0.0028 557  GLU B N   
13112 C CA  . GLU B 559  ? 0.2838 0.1966 0.2279 -0.0460 -0.0299 -0.0047 557  GLU B CA  
13113 C C   . GLU B 559  ? 0.2915 0.2078 0.2393 -0.0404 -0.0283 -0.0070 557  GLU B C   
13114 O O   . GLU B 559  ? 0.3113 0.2222 0.2570 -0.0378 -0.0292 -0.0091 557  GLU B O   
13115 C CB  . GLU B 559  ? 0.3634 0.2831 0.3096 -0.0505 -0.0296 -0.0037 557  GLU B CB  
13116 C CG  . GLU B 559  ? 0.4050 0.3219 0.3478 -0.0567 -0.0314 -0.0014 557  GLU B CG  
13117 C CD  . GLU B 559  ? 0.5030 0.4279 0.4485 -0.0609 -0.0310 -0.0005 557  GLU B CD  
13118 O OE1 . GLU B 559  ? 0.5459 0.4748 0.4940 -0.0591 -0.0304 -0.0023 557  GLU B OE1 
13119 O OE2 . GLU B 559  ? 0.4807 0.4081 0.4259 -0.0659 -0.0313 0.0019  557  GLU B OE2 
13120 N N   . THR B 560  ? 0.2649 0.1905 0.2182 -0.0386 -0.0258 -0.0067 558  THR B N   
13121 C CA  . THR B 560  ? 0.2560 0.1853 0.2130 -0.0337 -0.0242 -0.0087 558  THR B CA  
13122 C C   . THR B 560  ? 0.2643 0.1870 0.2195 -0.0294 -0.0248 -0.0099 558  THR B C   
13123 O O   . THR B 560  ? 0.2670 0.1879 0.2222 -0.0259 -0.0247 -0.0120 558  THR B O   
13124 C CB  . THR B 560  ? 0.2452 0.1847 0.2079 -0.0328 -0.0217 -0.0080 558  THR B CB  
13125 O OG1 . THR B 560  ? 0.2691 0.2150 0.2335 -0.0366 -0.0211 -0.0068 558  THR B OG1 
13126 C CG2 . THR B 560  ? 0.2774 0.2206 0.2438 -0.0281 -0.0201 -0.0099 558  THR B CG2 
13127 N N   . LEU B 561  ? 0.2501 0.1693 0.2035 -0.0294 -0.0254 -0.0086 559  LEU B N   
13128 C CA  . LEU B 561  ? 0.2462 0.1596 0.1981 -0.0252 -0.0261 -0.0097 559  LEU B CA  
13129 C C   . LEU B 561  ? 0.2906 0.1942 0.2374 -0.0245 -0.0283 -0.0111 559  LEU B C   
13130 O O   . LEU B 561  ? 0.2688 0.1698 0.2156 -0.0200 -0.0283 -0.0129 559  LEU B O   
13131 C CB  . LEU B 561  ? 0.2710 0.1821 0.2215 -0.0257 -0.0267 -0.0079 559  LEU B CB  
13132 C CG  . LEU B 561  ? 0.2412 0.1613 0.1966 -0.0251 -0.0246 -0.0070 559  LEU B CG  
13133 C CD1 . LEU B 561  ? 0.2708 0.1881 0.2238 -0.0262 -0.0254 -0.0051 559  LEU B CD1 
13134 C CD2 . LEU B 561  ? 0.2637 0.1877 0.2234 -0.0201 -0.0231 -0.0088 559  LEU B CD2 
13135 N N   . ALA B 562  ? 0.2782 0.1766 0.2206 -0.0288 -0.0301 -0.0102 560  ALA B N   
13136 C CA  . ALA B 562  ? 0.2944 0.1828 0.2312 -0.0282 -0.0324 -0.0116 560  ALA B CA  
13137 C C   . ALA B 562  ? 0.3321 0.2223 0.2701 -0.0261 -0.0317 -0.0141 560  ALA B C   
13138 O O   . ALA B 562  ? 0.3206 0.2052 0.2563 -0.0223 -0.0323 -0.0161 560  ALA B O   
13139 C CB  . ALA B 562  ? 0.3021 0.1844 0.2338 -0.0339 -0.0346 -0.0100 560  ALA B CB  
13140 N N   . SER B 563  ? 0.2853 0.1836 0.2268 -0.0284 -0.0303 -0.0139 561  SER B N   
13141 C CA  . SER B 563  ? 0.2791 0.1793 0.2215 -0.0264 -0.0297 -0.0160 561  SER B CA  
13142 C C   . SER B 563  ? 0.2887 0.1933 0.2352 -0.0209 -0.0276 -0.0174 561  SER B C   
13143 O O   . SER B 563  ? 0.2964 0.1986 0.2418 -0.0175 -0.0275 -0.0196 561  SER B O   
13144 C CB  . SER B 563  ? 0.3166 0.2242 0.2614 -0.0303 -0.0290 -0.0153 561  SER B CB  
13145 O OG  . SER B 563  ? 0.3508 0.2684 0.3015 -0.0302 -0.0267 -0.0140 561  SER B OG  
13146 N N   . LEU B 564  ? 0.2581 0.1692 0.2092 -0.0198 -0.0259 -0.0163 562  LEU B N   
13147 C CA  . LEU B 564  ? 0.2556 0.1710 0.2109 -0.0150 -0.0240 -0.0174 562  LEU B CA  
13148 C C   . LEU B 564  ? 0.2823 0.1904 0.2349 -0.0109 -0.0250 -0.0187 562  LEU B C   
13149 O O   . LEU B 564  ? 0.2870 0.1958 0.2408 -0.0069 -0.0240 -0.0204 562  LEU B O   
13150 C CB  . LEU B 564  ? 0.2793 0.2023 0.2395 -0.0151 -0.0223 -0.0159 562  LEU B CB  
13151 C CG  . LEU B 564  ? 0.2877 0.2159 0.2526 -0.0107 -0.0204 -0.0167 562  LEU B CG  
13152 C CD1 . LEU B 564  ? 0.2849 0.2174 0.2521 -0.0092 -0.0190 -0.0182 562  LEU B CD1 
13153 C CD2 . LEU B 564  ? 0.2974 0.2320 0.2662 -0.0115 -0.0191 -0.0152 562  LEU B CD2 
13154 N N   . THR B 565  ? 0.2828 0.1839 0.2315 -0.0119 -0.0269 -0.0177 563  THR B N   
13155 C CA  . THR B 565  ? 0.2769 0.1705 0.2226 -0.0080 -0.0281 -0.0188 563  THR B CA  
13156 C C   . THR B 565  ? 0.3093 0.1980 0.2519 -0.0059 -0.0287 -0.0212 563  THR B C   
13157 O O   . THR B 565  ? 0.3000 0.1883 0.2434 -0.0011 -0.0280 -0.0228 563  THR B O   
13158 C CB  . THR B 565  ? 0.2941 0.1793 0.2347 -0.0103 -0.0305 -0.0173 563  THR B CB  
13159 O OG1 . THR B 565  ? 0.3003 0.1898 0.2437 -0.0116 -0.0300 -0.0152 563  THR B OG1 
13160 C CG2 . THR B 565  ? 0.3193 0.1959 0.2563 -0.0060 -0.0321 -0.0186 563  THR B CG2 
13161 N N   . GLU B 566  ? 0.2885 0.1738 0.2273 -0.0095 -0.0299 -0.0213 564  GLU B N   
13162 C CA  . GLU B 566  ? 0.2929 0.1729 0.2279 -0.0078 -0.0306 -0.0237 564  GLU B CA  
13163 C C   . GLU B 566  ? 0.2852 0.1728 0.2244 -0.0048 -0.0282 -0.0252 564  GLU B C   
13164 O O   . GLU B 566  ? 0.2969 0.1821 0.2350 -0.0005 -0.0278 -0.0273 564  GLU B O   
13165 C CB  . GLU B 566  ? 0.3383 0.2132 0.2684 -0.0128 -0.0327 -0.0234 564  GLU B CB  
13166 C CG  . GLU B 566  ? 0.4221 0.2873 0.3466 -0.0154 -0.0354 -0.0222 564  GLU B CG  
13167 C CD  . GLU B 566  ? 0.5431 0.4008 0.4649 -0.0107 -0.0363 -0.0231 564  GLU B CD  
13168 O OE1 . GLU B 566  ? 0.6217 0.4749 0.5410 -0.0067 -0.0366 -0.0255 564  GLU B OE1 
13169 O OE2 . GLU B 566  ? 0.5331 0.3896 0.4553 -0.0108 -0.0368 -0.0213 564  GLU B OE2 
13170 N N   . ALA B 567  ? 0.2583 0.1553 0.2026 -0.0069 -0.0264 -0.0242 565  ALA B N   
13171 C CA  . ALA B 567  ? 0.3002 0.2045 0.2485 -0.0043 -0.0241 -0.0253 565  ALA B CA  
13172 C C   . ALA B 567  ? 0.2700 0.1772 0.2220 0.0007  -0.0225 -0.0259 565  ALA B C   
13173 O O   . ALA B 567  ? 0.2639 0.1731 0.2170 0.0042  -0.0211 -0.0275 565  ALA B O   
13174 C CB  . ALA B 567  ? 0.2829 0.1963 0.2358 -0.0074 -0.0227 -0.0239 565  ALA B CB  
13175 N N   . LEU B 568  ? 0.2495 0.1573 0.2034 0.0011  -0.0226 -0.0245 566  LEU B N   
13176 C CA  . LEU B 568  ? 0.2494 0.1602 0.2070 0.0056  -0.0213 -0.0249 566  LEU B CA  
13177 C C   . LEU B 568  ? 0.2751 0.1789 0.2292 0.0097  -0.0222 -0.0267 566  LEU B C   
13178 O O   . LEU B 568  ? 0.2656 0.1723 0.2220 0.0138  -0.0207 -0.0281 566  LEU B O   
13179 C CB  . LEU B 568  ? 0.2466 0.1593 0.2067 0.0048  -0.0215 -0.0230 566  LEU B CB  
13180 C CG  . LEU B 568  ? 0.2351 0.1556 0.1992 0.0015  -0.0202 -0.0214 566  LEU B CG  
13181 C CD1 . LEU B 568  ? 0.2643 0.1849 0.2293 0.0004  -0.0208 -0.0196 566  LEU B CD1 
13182 C CD2 . LEU B 568  ? 0.2674 0.1964 0.2370 0.0035  -0.0177 -0.0219 566  LEU B CD2 
13183 N N   . ARG B 569  ? 0.2757 0.1701 0.2240 0.0087  -0.0247 -0.0267 567  ARG B N   
13184 C CA  . ARG B 569  ? 0.2990 0.1857 0.2431 0.0127  -0.0258 -0.0286 567  ARG B CA  
13185 C C   . ARG B 569  ? 0.3069 0.1939 0.2496 0.0147  -0.0248 -0.0308 567  ARG B C   
13186 O O   . ARG B 569  ? 0.3217 0.2089 0.2650 0.0195  -0.0238 -0.0325 567  ARG B O   
13187 C CB  . ARG B 569  ? 0.3271 0.2030 0.2644 0.0105  -0.0288 -0.0282 567  ARG B CB  
13188 C CG  . ARG B 569  ? 0.4188 0.2932 0.3568 0.0100  -0.0299 -0.0262 567  ARG B CG  
13189 C CD  . ARG B 569  ? 0.4144 0.2777 0.3454 0.0076  -0.0329 -0.0255 567  ARG B CD  
13190 N NE  . ARG B 569  ? 0.4540 0.3166 0.3856 0.0064  -0.0338 -0.0233 567  ARG B NE  
13191 C CZ  . ARG B 569  ? 0.5114 0.3660 0.4378 0.0033  -0.0362 -0.0219 567  ARG B CZ  
13192 N NH1 . ARG B 569  ? 0.5406 0.3871 0.4610 0.0006  -0.0381 -0.0224 567  ARG B NH1 
13193 N NH2 . ARG B 569  ? 0.5714 0.4261 0.4986 0.0026  -0.0369 -0.0198 567  ARG B NH2 
13194 N N   . GLU B 570  ? 0.2897 0.1770 0.2306 0.0109  -0.0250 -0.0309 568  GLU B N   
13195 C CA  . GLU B 570  ? 0.2943 0.1818 0.2334 0.0124  -0.0242 -0.0330 568  GLU B CA  
13196 C C   . GLU B 570  ? 0.3142 0.2113 0.2593 0.0155  -0.0212 -0.0334 568  GLU B C   
13197 O O   . GLU B 570  ? 0.3201 0.2171 0.2642 0.0190  -0.0202 -0.0353 568  GLU B O   
13198 C CB  . GLU B 570  ? 0.3205 0.2075 0.2572 0.0074  -0.0251 -0.0327 568  GLU B CB  
13199 C CG  . GLU B 570  ? 0.3634 0.2398 0.2931 0.0043  -0.0283 -0.0327 568  GLU B CG  
13200 C CD  . GLU B 570  ? 0.5007 0.3784 0.4297 -0.0019 -0.0293 -0.0313 568  GLU B CD  
13201 O OE1 . GLU B 570  ? 0.4749 0.3614 0.4083 -0.0034 -0.0277 -0.0307 568  GLU B OE1 
13202 O OE2 . GLU B 570  ? 0.5444 0.4144 0.4685 -0.0053 -0.0319 -0.0307 568  GLU B OE2 
13203 N N   . SER B 571  ? 0.2917 0.1970 0.2429 0.0142  -0.0197 -0.0316 569  SER B N   
13204 C CA  . SER B 571  ? 0.2652 0.1793 0.2220 0.0168  -0.0170 -0.0317 569  SER B CA  
13205 C C   . SER B 571  ? 0.3305 0.2444 0.2886 0.0221  -0.0162 -0.0328 569  SER B C   
13206 O O   . SER B 571  ? 0.3272 0.2456 0.2875 0.0251  -0.0142 -0.0338 569  SER B O   
13207 C CB  . SER B 571  ? 0.2874 0.2095 0.2501 0.0144  -0.0159 -0.0296 569  SER B CB  
13208 O OG  . SER B 571  ? 0.2729 0.1951 0.2380 0.0154  -0.0162 -0.0286 569  SER B OG  
13209 N N   . ALA B 572  ? 0.3047 0.2134 0.2614 0.0233  -0.0178 -0.0325 570  ALA B N   
13210 C CA  . ALA B 572  ? 0.2953 0.2042 0.2536 0.0285  -0.0172 -0.0334 570  ALA B CA  
13211 C C   . ALA B 572  ? 0.3502 0.2534 0.3036 0.0321  -0.0174 -0.0359 570  ALA B C   
13212 O O   . ALA B 572  ? 0.3914 0.2968 0.3467 0.0369  -0.0162 -0.0369 570  ALA B O   
13213 C CB  . ALA B 572  ? 0.3256 0.2311 0.2840 0.0288  -0.0189 -0.0322 570  ALA B CB  
13214 N N   . ALA B 573  ? 0.3167 0.2127 0.2638 0.0300  -0.0189 -0.0368 571  ALA B N   
13215 C CA  . ALA B 573  ? 0.3758 0.2658 0.3176 0.0334  -0.0192 -0.0394 571  ALA B CA  
13216 C C   . ALA B 573  ? 0.3637 0.2592 0.3064 0.0342  -0.0170 -0.0406 571  ALA B C   
13217 O O   . ALA B 573  ? 0.3797 0.2714 0.3183 0.0375  -0.0167 -0.0429 571  ALA B O   
13218 C CB  . ALA B 573  ? 0.3819 0.2608 0.3159 0.0307  -0.0222 -0.0400 571  ALA B CB  
13219 N N   . MET B 574  ? 0.3182 0.2223 0.2659 0.0315  -0.0153 -0.0392 572  MET B N   
13220 C CA  . MET B 574  ? 0.2878 0.1971 0.2362 0.0321  -0.0132 -0.0401 572  MET B CA  
13221 C C   . MET B 574  ? 0.3011 0.2170 0.2541 0.0368  -0.0105 -0.0405 572  MET B C   
13222 O O   . MET B 574  ? 0.3121 0.2319 0.2700 0.0383  -0.0099 -0.0394 572  MET B O   
13223 C CB  . MET B 574  ? 0.3078 0.2238 0.2600 0.0276  -0.0125 -0.0382 572  MET B CB  
13224 C CG  . MET B 574  ? 0.3282 0.2391 0.2763 0.0226  -0.0149 -0.0377 572  MET B CG  
13225 S SD  . MET B 574  ? 0.3455 0.2647 0.2989 0.0178  -0.0142 -0.0352 572  MET B SD  
13226 C CE  . MET B 574  ? 0.3500 0.2624 0.2977 0.0125  -0.0172 -0.0350 572  MET B CE  
13227 N N   . LYS B 575  ? 0.2837 0.2013 0.2351 0.0390  -0.0089 -0.0421 573  LYS B N   
13228 C CA  . LYS B 575  ? 0.2712 0.1962 0.2270 0.0431  -0.0061 -0.0424 573  LYS B CA  
13229 C C   . LYS B 575  ? 0.2615 0.1958 0.2232 0.0405  -0.0041 -0.0405 573  LYS B C   
13230 O O   . LYS B 575  ? 0.2723 0.2086 0.2327 0.0387  -0.0034 -0.0406 573  LYS B O   
13231 C CB  . LYS B 575  ? 0.2996 0.2220 0.2506 0.0466  -0.0051 -0.0449 573  LYS B CB  
13232 C CG  . LYS B 575  ? 0.3415 0.2718 0.2968 0.0509  -0.0019 -0.0452 573  LYS B CG  
13233 C CD  . LYS B 575  ? 0.4210 0.3482 0.3708 0.0547  -0.0010 -0.0478 573  LYS B CD  
13234 C CE  . LYS B 575  ? 0.5766 0.5111 0.5305 0.0596  0.0021  -0.0482 573  LYS B CE  
13235 N NZ  . LYS B 575  ? 0.5799 0.5235 0.5377 0.0586  0.0049  -0.0470 573  LYS B NZ  
13236 N N   . TRP B 576  ? 0.2626 0.2026 0.2307 0.0403  -0.0035 -0.0387 574  TRP B N   
13237 C CA  . TRP B 576  ? 0.2317 0.1801 0.2055 0.0381  -0.0018 -0.0369 574  TRP B CA  
13238 C C   . TRP B 576  ? 0.2220 0.1776 0.1999 0.0415  0.0010  -0.0370 574  TRP B C   
13239 O O   . TRP B 576  ? 0.2494 0.2063 0.2295 0.0449  0.0016  -0.0373 574  TRP B O   
13240 C CB  . TRP B 576  ? 0.2337 0.1840 0.2118 0.0360  -0.0027 -0.0349 574  TRP B CB  
13241 C CG  . TRP B 576  ? 0.2252 0.1701 0.2002 0.0321  -0.0051 -0.0343 574  TRP B CG  
13242 C CD1 . TRP B 576  ? 0.2594 0.1979 0.2320 0.0319  -0.0073 -0.0343 574  TRP B CD1 
13243 C CD2 . TRP B 576  ? 0.2388 0.1843 0.2129 0.0279  -0.0056 -0.0335 574  TRP B CD2 
13244 N NE1 . TRP B 576  ? 0.2678 0.2030 0.2379 0.0276  -0.0091 -0.0335 574  TRP B NE1 
13245 C CE2 . TRP B 576  ? 0.2629 0.2027 0.2341 0.0251  -0.0080 -0.0330 574  TRP B CE2 
13246 C CE3 . TRP B 576  ? 0.2342 0.1847 0.2096 0.0262  -0.0042 -0.0331 574  TRP B CE3 
13247 C CZ2 . TRP B 576  ? 0.2724 0.2120 0.2425 0.0207  -0.0090 -0.0321 574  TRP B CZ2 
13248 C CZ3 . TRP B 576  ? 0.2451 0.1952 0.2193 0.0221  -0.0053 -0.0322 574  TRP B CZ3 
13249 C CH2 . TRP B 576  ? 0.2611 0.2060 0.2328 0.0194  -0.0076 -0.0317 574  TRP B CH2 
13250 N N   . THR B 577  ? 0.2331 0.1934 0.2118 0.0404  0.0028  -0.0366 575  THR B N   
13251 C CA  . THR B 577  ? 0.2145 0.1818 0.1967 0.0431  0.0056  -0.0365 575  THR B CA  
13252 C C   . THR B 577  ? 0.2201 0.1942 0.2068 0.0402  0.0069  -0.0345 575  THR B C   
13253 O O   . THR B 577  ? 0.2183 0.1914 0.2041 0.0366  0.0059  -0.0337 575  THR B O   
13254 C CB  . THR B 577  ? 0.2498 0.2153 0.2271 0.0457  0.0068  -0.0385 575  THR B CB  
13255 O OG1 . THR B 577  ? 0.2913 0.2552 0.2649 0.0427  0.0063  -0.0385 575  THR B OG1 
13256 C CG2 . THR B 577  ? 0.2762 0.2338 0.2481 0.0488  0.0053  -0.0407 575  THR B CG2 
13257 N N   . ALA B 578  ? 0.2069 0.1882 0.1985 0.0418  0.0093  -0.0337 576  ALA B N   
13258 C CA  . ALA B 578  ? 0.2124 0.1999 0.2077 0.0395  0.0108  -0.0319 576  ALA B CA  
13259 C C   . ALA B 578  ? 0.1944 0.1871 0.1909 0.0422  0.0136  -0.0320 576  ALA B C   
13260 O O   . ALA B 578  ? 0.2216 0.2169 0.2207 0.0452  0.0146  -0.0323 576  ALA B O   
13261 C CB  . ALA B 578  ? 0.1954 0.1867 0.1968 0.0378  0.0105  -0.0300 576  ALA B CB  
13262 N N   . LEU B 579  ? 0.2067 0.2010 0.2011 0.0412  0.0147  -0.0318 577  LEU B N   
13263 C CA  . LEU B 579  ? 0.2070 0.2057 0.2013 0.0436  0.0174  -0.0321 577  LEU B CA  
13264 C C   . LEU B 579  ? 0.1986 0.2031 0.1962 0.0412  0.0189  -0.0299 577  LEU B C   
13265 O O   . LEU B 579  ? 0.1929 0.1966 0.1909 0.0380  0.0177  -0.0288 577  LEU B O   
13266 C CB  . LEU B 579  ? 0.2430 0.2371 0.2301 0.0449  0.0173  -0.0341 577  LEU B CB  
13267 C CG  . LEU B 579  ? 0.2851 0.2711 0.2670 0.0464  0.0152  -0.0364 577  LEU B CG  
13268 C CD1 . LEU B 579  ? 0.3213 0.3024 0.2956 0.0472  0.0149  -0.0384 577  LEU B CD1 
13269 C CD2 . LEU B 579  ? 0.2716 0.2587 0.2557 0.0504  0.0160  -0.0372 577  LEU B CD2 
13270 N N   . PRO B 580  ? 0.1886 0.1989 0.1884 0.0428  0.0216  -0.0292 578  PRO B N   
13271 C CA  . PRO B 580  ? 0.1846 0.1995 0.1860 0.0406  0.0230  -0.0273 578  PRO B CA  
13272 C C   . PRO B 580  ? 0.1786 0.1900 0.1738 0.0398  0.0226  -0.0281 578  PRO B C   
13273 O O   . PRO B 580  ? 0.2157 0.2266 0.2067 0.0421  0.0238  -0.0294 578  PRO B O   
13274 C CB  . PRO B 580  ? 0.2085 0.2300 0.2130 0.0429  0.0260  -0.0266 578  PRO B CB  
13275 C CG  . PRO B 580  ? 0.2174 0.2387 0.2236 0.0461  0.0259  -0.0279 578  PRO B CG  
13276 C CD  . PRO B 580  ? 0.2054 0.2187 0.2062 0.0467  0.0235  -0.0301 578  PRO B CD  
13277 N N   . GLN B 581  ? 0.1784 0.1873 0.1728 0.0367  0.0208  -0.0274 579  GLN B N   
13278 C CA  . GLN B 581  ? 0.2034 0.2090 0.1922 0.0356  0.0198  -0.0281 579  GLN B CA  
13279 C C   . GLN B 581  ? 0.2182 0.2282 0.2080 0.0341  0.0212  -0.0262 579  GLN B C   
13280 O O   . GLN B 581  ? 0.2098 0.2207 0.2019 0.0314  0.0203  -0.0246 579  GLN B O   
13281 C CB  . GLN B 581  ? 0.2093 0.2101 0.1968 0.0330  0.0169  -0.0284 579  GLN B CB  
13282 C CG  . GLN B 581  ? 0.2273 0.2229 0.2132 0.0342  0.0153  -0.0302 579  GLN B CG  
13283 C CD  . GLN B 581  ? 0.2728 0.2635 0.2520 0.0362  0.0148  -0.0326 579  GLN B CD  
13284 O OE1 . GLN B 581  ? 0.2741 0.2652 0.2496 0.0366  0.0158  -0.0331 579  GLN B OE1 
13285 N NE2 . GLN B 581  ? 0.3446 0.3298 0.3216 0.0373  0.0132  -0.0343 579  GLN B NE2 
13286 N N   . LEU B 582  ? 0.2051 0.2176 0.1928 0.0360  0.0234  -0.0263 580  LEU B N   
13287 C CA  . LEU B 582  ? 0.2117 0.2279 0.1995 0.0347  0.0248  -0.0244 580  LEU B CA  
13288 C C   . LEU B 582  ? 0.2388 0.2515 0.2207 0.0336  0.0234  -0.0252 580  LEU B C   
13289 O O   . LEU B 582  ? 0.2426 0.2502 0.2202 0.0338  0.0215  -0.0272 580  LEU B O   
13290 C CB  . LEU B 582  ? 0.2315 0.2527 0.2201 0.0370  0.0280  -0.0239 580  LEU B CB  
13291 C CG  . LEU B 582  ? 0.2580 0.2845 0.2538 0.0369  0.0295  -0.0221 580  LEU B CG  
13292 C CD1 . LEU B 582  ? 0.2644 0.2899 0.2634 0.0381  0.0285  -0.0232 580  LEU B CD1 
13293 C CD2 . LEU B 582  ? 0.3147 0.3469 0.3113 0.0385  0.0327  -0.0211 580  LEU B CD2 
13294 N N   . ALA B 583  ? 0.2175 0.2330 0.1992 0.0322  0.0241  -0.0233 581  ALA B N   
13295 C CA  . ALA B 583  ? 0.2449 0.2577 0.2214 0.0310  0.0226  -0.0238 581  ALA B CA  
13296 C C   . ALA B 583  ? 0.2876 0.2974 0.2575 0.0332  0.0229  -0.0262 581  ALA B C   
13297 O O   . ALA B 583  ? 0.3215 0.3270 0.2865 0.0324  0.0207  -0.0277 581  ALA B O   
13298 C CB  . ALA B 583  ? 0.2885 0.3051 0.2656 0.0297  0.0236  -0.0213 581  ALA B CB  
13299 N N   . THR B 584  ? 0.2526 0.2647 0.2222 0.0360  0.0254  -0.0267 582  THR B N   
13300 C CA  . THR B 584  ? 0.2809 0.2906 0.2440 0.0386  0.0262  -0.0290 582  THR B CA  
13301 C C   . THR B 584  ? 0.2482 0.2531 0.2095 0.0405  0.0251  -0.0318 582  THR B C   
13302 O O   . THR B 584  ? 0.2649 0.2670 0.2206 0.0431  0.0255  -0.0340 582  THR B O   
13303 C CB  . THR B 584  ? 0.2980 0.3132 0.2618 0.0408  0.0297  -0.0281 582  THR B CB  
13304 O OG1 . THR B 584  ? 0.3085 0.3279 0.2793 0.0413  0.0312  -0.0268 582  THR B OG1 
13305 C CG2 . THR B 584  ? 0.3988 0.4172 0.3619 0.0390  0.0306  -0.0258 582  THR B CG2 
13306 N N   . GLY B 585  ? 0.2593 0.2627 0.2248 0.0396  0.0235  -0.0317 583  GLY B N   
13307 C CA  . GLY B 585  ? 0.2586 0.2571 0.2224 0.0414  0.0223  -0.0340 583  GLY B CA  
13308 C C   . GLY B 585  ? 0.2492 0.2508 0.2194 0.0427  0.0234  -0.0333 583  GLY B C   
13309 O O   . GLY B 585  ? 0.2636 0.2713 0.2394 0.0421  0.0252  -0.0311 583  GLY B O   
13310 N N   . PRO B 586  ? 0.2389 0.2362 0.2083 0.0444  0.0222  -0.0351 584  PRO B N   
13311 C CA  . PRO B 586  ? 0.2109 0.2111 0.1862 0.0459  0.0230  -0.0346 584  PRO B CA  
13312 C C   . PRO B 586  ? 0.2429 0.2486 0.2198 0.0494  0.0262  -0.0346 584  PRO B C   
13313 O O   . PRO B 586  ? 0.2642 0.2686 0.2360 0.0521  0.0274  -0.0364 584  PRO B O   
13314 C CB  . PRO B 586  ? 0.2573 0.2504 0.2299 0.0469  0.0206  -0.0367 584  PRO B CB  
13315 C CG  . PRO B 586  ? 0.3071 0.2944 0.2715 0.0478  0.0198  -0.0390 584  PRO B CG  
13316 C CD  . PRO B 586  ? 0.2864 0.2756 0.2493 0.0449  0.0198  -0.0377 584  PRO B CD  
13317 N N   . ALA B 587  ? 0.2340 0.2458 0.2179 0.0492  0.0276  -0.0326 585  ALA B N   
13318 C CA  . ALA B 587  ? 0.2164 0.2347 0.2032 0.0521  0.0307  -0.0322 585  ALA B CA  
13319 C C   . ALA B 587  ? 0.2297 0.2477 0.2189 0.0552  0.0305  -0.0335 585  ALA B C   
13320 O O   . ALA B 587  ? 0.2302 0.2445 0.2210 0.0543  0.0281  -0.0338 585  ALA B O   
13321 C CB  . ALA B 587  ? 0.2406 0.2662 0.2339 0.0497  0.0323  -0.0291 585  ALA B CB  
13322 N N   . ALA B 588  ? 0.2414 0.2635 0.2308 0.0590  0.0331  -0.0342 586  ALA B N   
13323 C CA  . ALA B 588  ? 0.2335 0.2569 0.2261 0.0624  0.0333  -0.0351 586  ALA B CA  
13324 C C   . ALA B 588  ? 0.2326 0.2626 0.2339 0.0606  0.0337  -0.0326 586  ALA B C   
13325 O O   . ALA B 588  ? 0.2508 0.2859 0.2558 0.0577  0.0348  -0.0302 586  ALA B O   
13326 C CB  . ALA B 588  ? 0.2278 0.2552 0.2189 0.0670  0.0364  -0.0364 586  ALA B CB  
13327 N N   . GLY B 589  ? 0.2421 0.2716 0.2465 0.0625  0.0325  -0.0332 587  GLY B N   
13328 C CA  . GLY B 589  ? 0.2429 0.2786 0.2555 0.0612  0.0327  -0.0310 587  GLY B CA  
13329 C C   . GLY B 589  ? 0.2433 0.2781 0.2582 0.0642  0.0315  -0.0321 587  GLY B C   
13330 O O   . GLY B 589  ? 0.2678 0.2975 0.2780 0.0677  0.0308  -0.0346 587  GLY B O   
13331 N N   . GLU B 590  ? 0.2434 0.2830 0.2653 0.0628  0.0310  -0.0303 588  GLU B N   
13332 C CA  . GLU B 590  ? 0.2500 0.2892 0.2748 0.0653  0.0295  -0.0310 588  GLU B CA  
13333 C C   . GLU B 590  ? 0.2403 0.2704 0.2617 0.0638  0.0260  -0.0318 588  GLU B C   
13334 O O   . GLU B 590  ? 0.2279 0.2560 0.2498 0.0595  0.0246  -0.0306 588  GLU B O   
13335 C CB  . GLU B 590  ? 0.2997 0.3472 0.3331 0.0640  0.0301  -0.0286 588  GLU B CB  
13336 C CG  . GLU B 590  ? 0.4154 0.4727 0.4528 0.0659  0.0336  -0.0277 588  GLU B CG  
13337 C CD  . GLU B 590  ? 0.4547 0.5134 0.4910 0.0717  0.0348  -0.0297 588  GLU B CD  
13338 O OE1 . GLU B 590  ? 0.5298 0.5851 0.5662 0.0742  0.0328  -0.0310 588  GLU B OE1 
13339 O OE2 . GLU B 590  ? 0.5898 0.6529 0.6250 0.0740  0.0378  -0.0301 588  GLU B OE2 
13340 N N   . THR B 591  ? 0.2444 0.2690 0.2624 0.0672  0.0246  -0.0339 589  THR B N   
13341 C CA  . THR B 591  ? 0.2731 0.2884 0.2868 0.0659  0.0213  -0.0349 589  THR B CA  
13342 C C   . THR B 591  ? 0.2472 0.2620 0.2644 0.0673  0.0194  -0.0347 589  THR B C   
13343 O O   . THR B 591  ? 0.2615 0.2801 0.2814 0.0714  0.0203  -0.0352 589  THR B O   
13344 C CB  . THR B 591  ? 0.2588 0.2661 0.2642 0.0684  0.0208  -0.0376 589  THR B CB  
13345 O OG1 . THR B 591  ? 0.2925 0.3004 0.2945 0.0670  0.0225  -0.0377 589  THR B OG1 
13346 C CG2 . THR B 591  ? 0.2879 0.2855 0.2889 0.0666  0.0174  -0.0383 589  THR B CG2 
13347 N N   . ARG B 592  ? 0.2419 0.2524 0.2592 0.0640  0.0168  -0.0339 590  ARG B N   
13348 C CA  . ARG B 592  ? 0.2807 0.2894 0.3002 0.0651  0.0145  -0.0338 590  ARG B CA  
13349 C C   . ARG B 592  ? 0.2475 0.2468 0.2621 0.0626  0.0115  -0.0342 590  ARG B C   
13350 O O   . ARG B 592  ? 0.2416 0.2374 0.2526 0.0593  0.0112  -0.0341 590  ARG B O   
13351 C CB  . ARG B 592  ? 0.2782 0.2946 0.3056 0.0632  0.0147  -0.0315 590  ARG B CB  
13352 C CG  . ARG B 592  ? 0.2830 0.2997 0.3116 0.0579  0.0142  -0.0298 590  ARG B CG  
13353 C CD  . ARG B 592  ? 0.3518 0.3733 0.3868 0.0562  0.0134  -0.0280 590  ARG B CD  
13354 N NE  . ARG B 592  ? 0.3404 0.3627 0.3766 0.0514  0.0132  -0.0264 590  ARG B NE  
13355 C CZ  . ARG B 592  ? 0.3346 0.3515 0.3686 0.0485  0.0110  -0.0261 590  ARG B CZ  
13356 N NH1 . ARG B 592  ? 0.3292 0.3392 0.3594 0.0494  0.0088  -0.0272 590  ARG B NH1 
13357 N NH2 . ARG B 592  ? 0.3373 0.3557 0.3728 0.0447  0.0112  -0.0247 590  ARG B NH2 
13358 N N   . THR B 593  ? 0.2850 0.2804 0.2994 0.0641  0.0092  -0.0345 591  THR B N   
13359 C CA  . THR B 593  ? 0.2697 0.2566 0.2797 0.0617  0.0063  -0.0346 591  THR B CA  
13360 C C   . THR B 593  ? 0.2500 0.2391 0.2637 0.0571  0.0054  -0.0325 591  THR B C   
13361 O O   . THR B 593  ? 0.2727 0.2693 0.2928 0.0566  0.0063  -0.0310 591  THR B O   
13362 C CB  . THR B 593  ? 0.3052 0.2866 0.3132 0.0650  0.0042  -0.0355 591  THR B CB  
13363 O OG1 . THR B 593  ? 0.3510 0.3387 0.3656 0.0665  0.0041  -0.0344 591  THR B OG1 
13364 C CG2 . THR B 593  ? 0.3674 0.3454 0.3709 0.0698  0.0050  -0.0379 591  THR B CG2 
13365 N N   . VAL B 594  ? 0.2319 0.2147 0.2416 0.0538  0.0036  -0.0324 592  VAL B N   
13366 C CA  . VAL B 594  ? 0.2269 0.2103 0.2389 0.0497  0.0023  -0.0306 592  VAL B CA  
13367 C C   . VAL B 594  ? 0.2473 0.2239 0.2566 0.0500  -0.0005 -0.0308 592  VAL B C   
13368 O O   . VAL B 594  ? 0.2571 0.2260 0.2604 0.0503  -0.0019 -0.0320 592  VAL B O   
13369 C CB  . VAL B 594  ? 0.2279 0.2098 0.2373 0.0457  0.0026  -0.0303 592  VAL B CB  
13370 C CG1 . VAL B 594  ? 0.2448 0.2273 0.2564 0.0418  0.0014  -0.0286 592  VAL B CG1 
13371 C CG2 . VAL B 594  ? 0.2617 0.2497 0.2732 0.0458  0.0054  -0.0301 592  VAL B CG2 
13372 N N   . LEU B 595  ? 0.2389 0.2183 0.2524 0.0498  -0.0015 -0.0296 593  LEU B N   
13373 C CA  . LEU B 595  ? 0.2339 0.2077 0.2454 0.0505  -0.0042 -0.0295 593  LEU B CA  
13374 C C   . LEU B 595  ? 0.2256 0.1979 0.2371 0.0461  -0.0057 -0.0280 593  LEU B C   
13375 O O   . LEU B 595  ? 0.2684 0.2461 0.2838 0.0435  -0.0047 -0.0268 593  LEU B O   
13376 C CB  . LEU B 595  ? 0.2549 0.2331 0.2711 0.0539  -0.0044 -0.0292 593  LEU B CB  
13377 C CG  . LEU B 595  ? 0.2750 0.2560 0.2921 0.0587  -0.0028 -0.0306 593  LEU B CG  
13378 C CD1 . LEU B 595  ? 0.3039 0.2901 0.3264 0.0619  -0.0032 -0.0301 593  LEU B CD1 
13379 C CD2 . LEU B 595  ? 0.2664 0.2389 0.2765 0.0612  -0.0035 -0.0325 593  LEU B CD2 
13380 N N   . ASN B 596  ? 0.2162 0.1810 0.2232 0.0454  -0.0080 -0.0281 594  ASN B N   
13381 C CA  . ASN B 596  ? 0.2200 0.1832 0.2265 0.0415  -0.0094 -0.0267 594  ASN B CA  
13382 C C   . ASN B 596  ? 0.2029 0.1713 0.2148 0.0418  -0.0099 -0.0254 594  ASN B C   
13383 O O   . ASN B 596  ? 0.2110 0.1790 0.2239 0.0449  -0.0110 -0.0256 594  ASN B O   
13384 C CB  . ASN B 596  ? 0.2199 0.1738 0.2203 0.0413  -0.0119 -0.0269 594  ASN B CB  
13385 C CG  . ASN B 596  ? 0.2287 0.1802 0.2276 0.0372  -0.0133 -0.0255 594  ASN B CG  
13386 O OD1 . ASN B 596  ? 0.2239 0.1801 0.2266 0.0355  -0.0131 -0.0243 594  ASN B OD1 
13387 N ND2 . ASN B 596  ? 0.2563 0.2002 0.2493 0.0354  -0.0147 -0.0257 594  ASN B ND2 
13388 N N   . PRO B 597  ? 0.1904 0.1638 0.2058 0.0389  -0.0092 -0.0243 595  PRO B N   
13389 C CA  . PRO B 597  ? 0.1983 0.1764 0.2186 0.0390  -0.0098 -0.0233 595  PRO B CA  
13390 C C   . PRO B 597  ? 0.1993 0.1728 0.2175 0.0391  -0.0124 -0.0227 595  PRO B C   
13391 O O   . PRO B 597  ? 0.2015 0.1779 0.2231 0.0404  -0.0134 -0.0221 595  PRO B O   
13392 C CB  . PRO B 597  ? 0.2018 0.1841 0.2246 0.0354  -0.0087 -0.0223 595  PRO B CB  
13393 C CG  . PRO B 597  ? 0.1967 0.1748 0.2149 0.0329  -0.0083 -0.0226 595  PRO B CG  
13394 C CD  . PRO B 597  ? 0.1914 0.1660 0.2062 0.0353  -0.0079 -0.0239 595  PRO B CD  
13395 N N   . GLY B 598  ? 0.2044 0.1706 0.2168 0.0375  -0.0137 -0.0227 596  GLY B N   
13396 C CA  . GLY B 598  ? 0.2092 0.1704 0.2190 0.0374  -0.0163 -0.0220 596  GLY B CA  
13397 C C   . GLY B 598  ? 0.2304 0.1868 0.2377 0.0413  -0.0177 -0.0228 596  GLY B C   
13398 O O   . GLY B 598  ? 0.2460 0.1984 0.2514 0.0419  -0.0200 -0.0221 596  GLY B O   
13399 N N   . ASP B 599  ? 0.2238 0.1803 0.2309 0.0442  -0.0165 -0.0242 597  ASP B N   
13400 C CA  . ASP B 599  ? 0.2386 0.1906 0.2433 0.0485  -0.0177 -0.0251 597  ASP B CA  
13401 C C   . ASP B 599  ? 0.2511 0.2063 0.2572 0.0515  -0.0154 -0.0267 597  ASP B C   
13402 O O   . ASP B 599  ? 0.2432 0.1949 0.2455 0.0509  -0.0145 -0.0277 597  ASP B O   
13403 C CB  . ASP B 599  ? 0.2414 0.1829 0.2385 0.0474  -0.0196 -0.0253 597  ASP B CB  
13404 C CG  . ASP B 599  ? 0.2718 0.2074 0.2658 0.0517  -0.0213 -0.0262 597  ASP B CG  
13405 O OD1 . ASP B 599  ? 0.2580 0.1976 0.2553 0.0561  -0.0205 -0.0271 597  ASP B OD1 
13406 O OD2 . ASP B 599  ? 0.3108 0.2376 0.2989 0.0508  -0.0235 -0.0259 597  ASP B OD2 
13407 N N   . HIS B 600  ? 0.2295 0.1915 0.2410 0.0548  -0.0146 -0.0268 598  HIS B N   
13408 C CA  . HIS B 600  ? 0.2535 0.2197 0.2668 0.0576  -0.0121 -0.0281 598  HIS B CA  
13409 C C   . HIS B 600  ? 0.2424 0.2016 0.2502 0.0612  -0.0125 -0.0299 598  HIS B C   
13410 O O   . HIS B 600  ? 0.2784 0.2398 0.2862 0.0632  -0.0104 -0.0312 598  HIS B O   
13411 C CB  . HIS B 600  ? 0.2582 0.2339 0.2789 0.0601  -0.0110 -0.0276 598  HIS B CB  
13412 C CG  . HIS B 600  ? 0.2462 0.2292 0.2722 0.0564  -0.0100 -0.0262 598  HIS B CG  
13413 N ND1 . HIS B 600  ? 0.2995 0.2914 0.3325 0.0574  -0.0092 -0.0255 598  HIS B ND1 
13414 C CD2 . HIS B 600  ? 0.2463 0.2288 0.2715 0.0517  -0.0098 -0.0254 598  HIS B CD2 
13415 C CE1 . HIS B 600  ? 0.3378 0.3336 0.3737 0.0535  -0.0086 -0.0243 598  HIS B CE1 
13416 N NE2 . HIS B 600  ? 0.2709 0.2612 0.3021 0.0502  -0.0089 -0.0243 598  HIS B NE2 
13417 N N   . ARG B 601  ? 0.2629 0.2135 0.2657 0.0621  -0.0152 -0.0300 599  ARG B N   
13418 C CA  . ARG B 601  ? 0.2718 0.2144 0.2685 0.0651  -0.0158 -0.0318 599  ARG B CA  
13419 C C   . ARG B 601  ? 0.2682 0.2058 0.2596 0.0618  -0.0152 -0.0325 599  ARG B C   
13420 O O   . ARG B 601  ? 0.3073 0.2396 0.2940 0.0642  -0.0150 -0.0343 599  ARG B O   
13421 C CB  . ARG B 601  ? 0.3086 0.2427 0.3011 0.0665  -0.0190 -0.0315 599  ARG B CB  
13422 C CG  . ARG B 601  ? 0.3237 0.2624 0.3210 0.0701  -0.0199 -0.0308 599  ARG B CG  
13423 C CD  . ARG B 601  ? 0.3694 0.2999 0.3626 0.0705  -0.0233 -0.0299 599  ARG B CD  
13424 N NE  . ARG B 601  ? 0.3455 0.2731 0.3367 0.0648  -0.0245 -0.0283 599  ARG B NE  
13425 C CZ  . ARG B 601  ? 0.4046 0.3245 0.3914 0.0637  -0.0274 -0.0273 599  ARG B CZ  
13426 N NH1 . ARG B 601  ? 0.3895 0.3034 0.3733 0.0679  -0.0295 -0.0276 599  ARG B NH1 
13427 N NH2 . ARG B 601  ? 0.3448 0.2629 0.3299 0.0584  -0.0280 -0.0258 599  ARG B NH2 
13428 N N   . ASP B 602  ? 0.2587 0.1978 0.2507 0.0566  -0.0149 -0.0313 600  ASP B N   
13429 C CA  . ASP B 602  ? 0.2670 0.2020 0.2544 0.0531  -0.0146 -0.0317 600  ASP B CA  
13430 C C   . ASP B 602  ? 0.2699 0.2121 0.2605 0.0531  -0.0116 -0.0323 600  ASP B C   
13431 O O   . ASP B 602  ? 0.2701 0.2197 0.2657 0.0508  -0.0102 -0.0311 600  ASP B O   
13432 C CB  . ASP B 602  ? 0.2910 0.2246 0.2778 0.0479  -0.0158 -0.0299 600  ASP B CB  
13433 C CG  . ASP B 602  ? 0.3132 0.2428 0.2955 0.0441  -0.0157 -0.0302 600  ASP B CG  
13434 O OD1 . ASP B 602  ? 0.3287 0.2537 0.3067 0.0455  -0.0155 -0.0319 600  ASP B OD1 
13435 O OD2 . ASP B 602  ? 0.3181 0.2495 0.3014 0.0397  -0.0157 -0.0288 600  ASP B OD2 
13436 N N   . VAL B 603  ? 0.2604 0.2003 0.2478 0.0559  -0.0106 -0.0342 601  VAL B N   
13437 C CA  . VAL B 603  ? 0.2662 0.2123 0.2558 0.0560  -0.0078 -0.0348 601  VAL B CA  
13438 C C   . VAL B 603  ? 0.2786 0.2222 0.2648 0.0513  -0.0078 -0.0346 601  VAL B C   
13439 O O   . VAL B 603  ? 0.3027 0.2380 0.2825 0.0504  -0.0093 -0.0356 601  VAL B O   
13440 C CB  . VAL B 603  ? 0.2839 0.2286 0.2710 0.0610  -0.0067 -0.0370 601  VAL B CB  
13441 C CG1 . VAL B 603  ? 0.2935 0.2446 0.2824 0.0609  -0.0037 -0.0375 601  VAL B CG1 
13442 C CG2 . VAL B 603  ? 0.2846 0.2324 0.2755 0.0659  -0.0068 -0.0371 601  VAL B CG2 
13443 N N   . VAL B 604  ? 0.2423 0.1928 0.2328 0.0483  -0.0062 -0.0334 602  VAL B N   
13444 C CA  . VAL B 604  ? 0.2338 0.1830 0.2219 0.0440  -0.0062 -0.0330 602  VAL B CA  
13445 C C   . VAL B 604  ? 0.2312 0.1812 0.2171 0.0447  -0.0045 -0.0343 602  VAL B C   
13446 O O   . VAL B 604  ? 0.2503 0.1955 0.2313 0.0426  -0.0052 -0.0350 602  VAL B O   
13447 C CB  . VAL B 604  ? 0.2183 0.1737 0.2115 0.0405  -0.0056 -0.0310 602  VAL B CB  
13448 C CG1 . VAL B 604  ? 0.2273 0.1811 0.2179 0.0361  -0.0059 -0.0305 602  VAL B CG1 
13449 C CG2 . VAL B 604  ? 0.2342 0.1888 0.2293 0.0401  -0.0074 -0.0298 602  VAL B CG2 
13450 N N   . GLY B 605  ? 0.2297 0.1860 0.2191 0.0477  -0.0021 -0.0347 603  GLY B N   
13451 C CA  . GLY B 605  ? 0.2429 0.2006 0.2303 0.0484  -0.0003 -0.0359 603  GLY B CA  
13452 C C   . GLY B 605  ? 0.2299 0.1954 0.2219 0.0517  0.0024  -0.0360 603  GLY B C   
13453 O O   . GLY B 605  ? 0.2458 0.2144 0.2417 0.0544  0.0025  -0.0356 603  GLY B O   
13454 N N   . SER B 606  ? 0.2244 0.1936 0.2162 0.0514  0.0045  -0.0362 604  SER B N   
13455 C CA  A SER B 606  ? 0.2393 0.2160 0.2349 0.0544  0.0072  -0.0362 604  SER B CA  
13456 C CA  B SER B 606  ? 0.2392 0.2159 0.2348 0.0544  0.0072  -0.0363 604  SER B CA  
13457 C CA  C SER B 606  ? 0.2391 0.2157 0.2345 0.0544  0.0073  -0.0363 604  SER B CA  
13458 C C   . SER B 606  ? 0.2332 0.2160 0.2315 0.0515  0.0091  -0.0349 604  SER B C   
13459 O O   . SER B 606  ? 0.2615 0.2416 0.2563 0.0486  0.0087  -0.0349 604  SER B O   
13460 C CB  A SER B 606  ? 0.2904 0.2642 0.2813 0.0586  0.0082  -0.0386 604  SER B CB  
13461 C CB  B SER B 606  ? 0.2905 0.2642 0.2812 0.0586  0.0081  -0.0386 604  SER B CB  
13462 C CB  C SER B 606  ? 0.2900 0.2629 0.2800 0.0582  0.0080  -0.0387 604  SER B CB  
13463 O OG  A SER B 606  ? 0.2862 0.2563 0.2716 0.0570  0.0082  -0.0396 604  SER B OG  
13464 O OG  B SER B 606  ? 0.3373 0.3053 0.3257 0.0618  0.0065  -0.0399 604  SER B OG  
13465 O OG  C SER B 606  ? 0.2799 0.2601 0.2725 0.0605  0.0111  -0.0388 604  SER B OG  
13466 N N   . VAL B 607  ? 0.2048 0.1959 0.2092 0.0522  0.0111  -0.0336 605  VAL B N   
13467 C CA  . VAL B 607  ? 0.1900 0.1871 0.1972 0.0497  0.0130  -0.0322 605  VAL B CA  
13468 C C   . VAL B 607  ? 0.2007 0.2039 0.2097 0.0526  0.0160  -0.0324 605  VAL B C   
13469 O O   . VAL B 607  ? 0.1999 0.2068 0.2122 0.0558  0.0168  -0.0325 605  VAL B O   
13470 C CB  . VAL B 607  ? 0.1893 0.1906 0.2024 0.0466  0.0126  -0.0299 605  VAL B CB  
13471 C CG1 . VAL B 607  ? 0.1919 0.1976 0.2105 0.0487  0.0127  -0.0294 605  VAL B CG1 
13472 C CG2 . VAL B 607  ? 0.1973 0.2041 0.2127 0.0443  0.0145  -0.0285 605  VAL B CG2 
13473 N N   . THR B 608  ? 0.1992 0.2036 0.2057 0.0517  0.0175  -0.0324 606  THR B N   
13474 C CA  . THR B 608  ? 0.1996 0.2106 0.2079 0.0537  0.0206  -0.0322 606  THR B CA  
13475 C C   . THR B 608  ? 0.1984 0.2156 0.2116 0.0504  0.0218  -0.0297 606  THR B C   
13476 O O   . THR B 608  ? 0.1997 0.2150 0.2111 0.0471  0.0211  -0.0290 606  THR B O   
13477 C CB  . THR B 608  ? 0.2276 0.2351 0.2291 0.0551  0.0214  -0.0339 606  THR B CB  
13478 O OG1 . THR B 608  ? 0.2392 0.2401 0.2360 0.0583  0.0201  -0.0363 606  THR B OG1 
13479 C CG2 . THR B 608  ? 0.2378 0.2522 0.2407 0.0571  0.0247  -0.0336 606  THR B CG2 
13480 N N   . GLU B 609  ? 0.2015 0.2260 0.2208 0.0511  0.0233  -0.0283 607  GLU B N   
13481 C CA  . GLU B 609  ? 0.2157 0.2454 0.2398 0.0478  0.0241  -0.0259 607  GLU B CA  
13482 C C   . GLU B 609  ? 0.1868 0.2214 0.2107 0.0478  0.0269  -0.0251 607  GLU B C   
13483 O O   . GLU B 609  ? 0.2193 0.2554 0.2410 0.0508  0.0288  -0.0262 607  GLU B O   
13484 C CB  . GLU B 609  ? 0.2490 0.2833 0.2800 0.0477  0.0236  -0.0247 607  GLU B CB  
13485 C CG  . GLU B 609  ? 0.2522 0.2809 0.2826 0.0471  0.0206  -0.0253 607  GLU B CG  
13486 C CD  . GLU B 609  ? 0.3165 0.3490 0.3531 0.0466  0.0197  -0.0240 607  GLU B CD  
13487 O OE1 . GLU B 609  ? 0.3693 0.4084 0.4105 0.0483  0.0213  -0.0234 607  GLU B OE1 
13488 O OE2 . GLU B 609  ? 0.2930 0.3222 0.3300 0.0443  0.0175  -0.0236 607  GLU B OE2 
13489 N N   . THR B 610  ? 0.1860 0.2228 0.2119 0.0443  0.0272  -0.0230 608  THR B N   
13490 C CA  . THR B 610  ? 0.1878 0.2277 0.2124 0.0435  0.0294  -0.0220 608  THR B CA  
13491 C C   . THR B 610  ? 0.1943 0.2425 0.2244 0.0439  0.0319  -0.0203 608  THR B C   
13492 O O   . THR B 610  ? 0.2003 0.2518 0.2361 0.0424  0.0315  -0.0188 608  THR B O   
13493 C CB  . THR B 610  ? 0.1890 0.2270 0.2133 0.0395  0.0283  -0.0205 608  THR B CB  
13494 O OG1 . THR B 610  ? 0.1849 0.2159 0.2050 0.0387  0.0258  -0.0219 608  THR B OG1 
13495 C CG2 . THR B 610  ? 0.1962 0.2364 0.2181 0.0387  0.0303  -0.0195 608  THR B CG2 
13496 N N   . SER B 611  ? 0.1934 0.2451 0.2218 0.0458  0.0346  -0.0204 609  SER B N   
13497 C CA  . SER B 611  ? 0.1991 0.2592 0.2326 0.0456  0.0372  -0.0184 609  SER B CA  
13498 C C   . SER B 611  ? 0.2348 0.2963 0.2700 0.0414  0.0373  -0.0158 609  SER B C   
13499 O O   . SER B 611  ? 0.1954 0.2521 0.2265 0.0396  0.0363  -0.0157 609  SER B O   
13500 C CB  . SER B 611  ? 0.2258 0.2892 0.2564 0.0487  0.0402  -0.0191 609  SER B CB  
13501 O OG  . SER B 611  ? 0.2318 0.2929 0.2572 0.0474  0.0409  -0.0189 609  SER B OG  
13502 N N   . GLU B 612  ? 0.2165 0.2845 0.2577 0.0400  0.0386  -0.0135 610  GLU B N   
13503 C CA  . GLU B 612  ? 0.2296 0.2988 0.2723 0.0361  0.0388  -0.0110 610  GLU B CA  
13504 C C   . GLU B 612  ? 0.2407 0.3098 0.2785 0.0360  0.0407  -0.0104 610  GLU B C   
13505 O O   . GLU B 612  ? 0.2402 0.3065 0.2761 0.0333  0.0400  -0.0092 610  GLU B O   
13506 C CB  . GLU B 612  ? 0.2789 0.3551 0.3287 0.0345  0.0398  -0.0087 610  GLU B CB  
13507 C CG  . GLU B 612  ? 0.3066 0.3823 0.3611 0.0338  0.0374  -0.0089 610  GLU B CG  
13508 C CD  . GLU B 612  ? 0.3923 0.4753 0.4539 0.0323  0.0382  -0.0068 610  GLU B CD  
13509 O OE1 . GLU B 612  ? 0.5835 0.6712 0.6466 0.0306  0.0404  -0.0046 610  GLU B OE1 
13510 O OE2 . GLU B 612  ? 0.4295 0.5136 0.4953 0.0326  0.0367  -0.0071 610  GLU B OE2 
13511 N N   . GLU B 613  ? 0.2366 0.3085 0.2720 0.0391  0.0431  -0.0114 611  GLU B N   
13512 C CA  . GLU B 613  ? 0.2361 0.3076 0.2661 0.0392  0.0448  -0.0111 611  GLU B CA  
13513 C C   . GLU B 613  ? 0.2291 0.2926 0.2527 0.0390  0.0426  -0.0128 611  GLU B C   
13514 O O   . GLU B 613  ? 0.2452 0.3070 0.2655 0.0371  0.0427  -0.0117 611  GLU B O   
13515 C CB  . GLU B 613  ? 0.2698 0.3459 0.2983 0.0429  0.0478  -0.0121 611  GLU B CB  
13516 N N   . ASP B 614  ? 0.2120 0.2706 0.2337 0.0408  0.0406  -0.0153 612  ASP B N   
13517 C CA  . ASP B 614  ? 0.2033 0.2547 0.2192 0.0402  0.0384  -0.0168 612  ASP B CA  
13518 C C   . ASP B 614  ? 0.2065 0.2550 0.2241 0.0366  0.0361  -0.0154 612  ASP B C   
13519 O O   . ASP B 614  ? 0.2048 0.2492 0.2183 0.0352  0.0349  -0.0156 612  ASP B O   
13520 C CB  . ASP B 614  ? 0.2198 0.2664 0.2327 0.0430  0.0369  -0.0198 612  ASP B CB  
13521 C CG  . ASP B 614  ? 0.2728 0.3200 0.2812 0.0467  0.0389  -0.0217 612  ASP B CG  
13522 O OD1 . ASP B 614  ? 0.3328 0.3822 0.3383 0.0467  0.0409  -0.0210 612  ASP B OD1 
13523 O OD2 . ASP B 614  ? 0.2758 0.3210 0.2832 0.0497  0.0385  -0.0239 612  ASP B OD2 
13524 N N   . ALA B 615  ? 0.1992 0.2499 0.2228 0.0351  0.0354  -0.0142 613  ALA B N   
13525 C CA  . ALA B 615  ? 0.1779 0.2264 0.2031 0.0318  0.0336  -0.0127 613  ALA B CA  
13526 C C   . ALA B 615  ? 0.1960 0.2460 0.2201 0.0298  0.0348  -0.0105 613  ALA B C   
13527 O O   . ALA B 615  ? 0.1949 0.2412 0.2163 0.0282  0.0334  -0.0102 613  ALA B O   
13528 C CB  . ALA B 615  ? 0.2014 0.2523 0.2331 0.0306  0.0329  -0.0117 613  ALA B CB  
13529 N N   . ARG B 616  ? 0.2260 0.2816 0.2521 0.0299  0.0374  -0.0089 614  ARG B N   
13530 C CA  . ARG B 616  ? 0.2071 0.2640 0.2318 0.0281  0.0386  -0.0066 614  ARG B CA  
13531 C C   . ARG B 616  ? 0.1989 0.2527 0.2166 0.0291  0.0387  -0.0077 614  ARG B C   
13532 O O   . ARG B 616  ? 0.2140 0.2657 0.2293 0.0274  0.0381  -0.0064 614  ARG B O   
13533 C CB  . ARG B 616  ? 0.2436 0.3073 0.2718 0.0279  0.0414  -0.0046 614  ARG B CB  
13534 C CG  . ARG B 616  ? 0.2676 0.3340 0.3025 0.0256  0.0409  -0.0028 614  ARG B CG  
13535 C CD  . ARG B 616  ? 0.3347 0.4080 0.3731 0.0247  0.0436  -0.0004 614  ARG B CD  
13536 N NE  . ARG B 616  ? 0.3542 0.4326 0.3944 0.0276  0.0455  -0.0015 614  ARG B NE  
13537 C CZ  . ARG B 616  ? 0.3670 0.4481 0.4123 0.0283  0.0450  -0.0021 614  ARG B CZ  
13538 N NH1 . ARG B 616  ? 0.3426 0.4217 0.3915 0.0262  0.0426  -0.0017 614  ARG B NH1 
13539 N NH2 . ARG B 616  ? 0.3459 0.4319 0.3926 0.0313  0.0468  -0.0032 614  ARG B NH2 
13540 N N   . ARG B 617  ? 0.1970 0.2504 0.2113 0.0321  0.0395  -0.0099 615  ARG B N   
13541 C CA  . ARG B 617  ? 0.2174 0.2674 0.2248 0.0331  0.0393  -0.0112 615  ARG B CA  
13542 C C   . ARG B 617  ? 0.2046 0.2487 0.2097 0.0315  0.0362  -0.0120 615  ARG B C   
13543 O O   . ARG B 617  ? 0.2138 0.2557 0.2148 0.0306  0.0356  -0.0115 615  ARG B O   
13544 C CB  . ARG B 617  ? 0.2523 0.3019 0.2563 0.0367  0.0403  -0.0139 615  ARG B CB  
13545 C CG  . ARG B 617  ? 0.2889 0.3350 0.2852 0.0377  0.0402  -0.0154 615  ARG B CG  
13546 C CD  . ARG B 617  ? 0.3530 0.4002 0.3459 0.0415  0.0421  -0.0176 615  ARG B CD  
13547 N NE  . ARG B 617  ? 0.4034 0.4470 0.3961 0.0436  0.0406  -0.0203 615  ARG B NE  
13548 C CZ  . ARG B 617  ? 0.4796 0.5168 0.4668 0.0445  0.0385  -0.0228 615  ARG B CZ  
13549 N NH1 . ARG B 617  ? 0.4533 0.4870 0.4349 0.0433  0.0375  -0.0230 615  ARG B NH1 
13550 N NH2 . ARG B 617  ? 0.4805 0.5145 0.4677 0.0464  0.0373  -0.0251 615  ARG B NH2 
13551 N N   . ALA B 618  ? 0.1965 0.2380 0.2041 0.0313  0.0342  -0.0131 616  ALA B N   
13552 C CA  . ALA B 618  ? 0.1742 0.2107 0.1799 0.0298  0.0314  -0.0138 616  ALA B CA  
13553 C C   . ALA B 618  ? 0.1885 0.2253 0.1954 0.0271  0.0308  -0.0114 616  ALA B C   
13554 O O   . ALA B 618  ? 0.1921 0.2260 0.1957 0.0261  0.0293  -0.0115 616  ALA B O   
13555 C CB  . ALA B 618  ? 0.1849 0.2192 0.1936 0.0298  0.0295  -0.0150 616  ALA B CB  
13556 N N   . VAL B 619  ? 0.1975 0.2377 0.2093 0.0258  0.0318  -0.0093 617  VAL B N   
13557 C CA  . VAL B 619  ? 0.1787 0.2186 0.1915 0.0234  0.0311  -0.0070 617  VAL B CA  
13558 C C   . VAL B 619  ? 0.1924 0.2327 0.2008 0.0234  0.0322  -0.0059 617  VAL B C   
13559 O O   . VAL B 619  ? 0.2189 0.2570 0.2253 0.0222  0.0309  -0.0051 617  VAL B O   
13560 C CB  . VAL B 619  ? 0.1764 0.2193 0.1950 0.0220  0.0318  -0.0050 617  VAL B CB  
13561 C CG1 . VAL B 619  ? 0.2133 0.2551 0.2324 0.0197  0.0311  -0.0027 617  VAL B CG1 
13562 C CG2 . VAL B 619  ? 0.2086 0.2507 0.2310 0.0220  0.0305  -0.0062 617  VAL B CG2 
13563 N N   . ARG B 620  ? 0.2131 0.2565 0.2199 0.0248  0.0346  -0.0058 618  ARG B N   
13564 C CA  . ARG B 620  ? 0.2379 0.2817 0.2399 0.0250  0.0357  -0.0049 618  ARG B CA  
13565 C C   . ARG B 620  ? 0.2028 0.2424 0.1992 0.0256  0.0338  -0.0068 618  ARG B C   
13566 O O   . ARG B 620  ? 0.2176 0.2559 0.2110 0.0247  0.0331  -0.0057 618  ARG B O   
13567 C CB  . ARG B 620  ? 0.2592 0.3072 0.2603 0.0267  0.0387  -0.0048 618  ARG B CB  
13568 C CG  . ARG B 620  ? 0.4785 0.5299 0.4796 0.0255  0.0408  -0.0018 618  ARG B CG  
13569 C CD  . ARG B 620  ? 0.4456 0.5019 0.4462 0.0273  0.0441  -0.0017 618  ARG B CD  
13570 N NE  . ARG B 620  ? 0.4621 0.5218 0.4682 0.0281  0.0449  -0.0023 618  ARG B NE  
13571 C CZ  . ARG B 620  ? 0.5075 0.5679 0.5129 0.0309  0.0456  -0.0048 618  ARG B CZ  
13572 N NH1 . ARG B 620  ? 0.4949 0.5527 0.4941 0.0332  0.0457  -0.0071 618  ARG B NH1 
13573 N NH2 . ARG B 620  ? 0.3842 0.4479 0.3950 0.0316  0.0462  -0.0051 618  ARG B NH2 
13574 N N   . LEU B 621  ? 0.2015 0.2388 0.1965 0.0271  0.0329  -0.0095 619  LEU B N   
13575 C CA  . LEU B 621  ? 0.2129 0.2460 0.2027 0.0274  0.0309  -0.0114 619  LEU B CA  
13576 C C   . LEU B 621  ? 0.2188 0.2495 0.2097 0.0253  0.0283  -0.0107 619  LEU B C   
13577 O O   . LEU B 621  ? 0.2343 0.2631 0.2214 0.0247  0.0270  -0.0108 619  LEU B O   
13578 C CB  . LEU B 621  ? 0.2217 0.2523 0.2101 0.0292  0.0302  -0.0144 619  LEU B CB  
13579 C CG  . LEU B 621  ? 0.2388 0.2711 0.2246 0.0320  0.0326  -0.0157 619  LEU B CG  
13580 C CD1 . LEU B 621  ? 0.2697 0.2992 0.2551 0.0339  0.0318  -0.0185 619  LEU B CD1 
13581 C CD2 . LEU B 621  ? 0.2954 0.3269 0.2745 0.0327  0.0331  -0.0161 619  LEU B CD2 
13582 N N   . ALA B 622  ? 0.2038 0.2347 0.2000 0.0242  0.0276  -0.0101 620  ALA B N   
13583 C CA  . ALA B 622  ? 0.2096 0.2387 0.2072 0.0224  0.0254  -0.0093 620  ALA B CA  
13584 C C   . ALA B 622  ? 0.1944 0.2247 0.1914 0.0213  0.0257  -0.0068 620  ALA B C   
13585 O O   . ALA B 622  ? 0.1989 0.2276 0.1940 0.0205  0.0240  -0.0065 620  ALA B O   
13586 C CB  . ALA B 622  ? 0.1999 0.2291 0.2029 0.0216  0.0248  -0.0092 620  ALA B CB  
13587 N N   . ALA B 623  ? 0.1875 0.2207 0.1861 0.0212  0.0279  -0.0049 621  ALA B N   
13588 C CA  . ALA B 623  ? 0.1937 0.2274 0.1914 0.0202  0.0282  -0.0023 621  ALA B CA  
13589 C C   . ALA B 623  ? 0.2133 0.2463 0.2051 0.0208  0.0279  -0.0026 621  ALA B C   
13590 O O   . ALA B 623  ? 0.2259 0.2578 0.2161 0.0201  0.0266  -0.0014 621  ALA B O   
13591 C CB  . ALA B 623  ? 0.2113 0.2483 0.2117 0.0198  0.0306  -0.0002 621  ALA B CB  
13592 N N   . ASP B 624  ? 0.2248 0.2582 0.2131 0.0223  0.0291  -0.0042 622  ASP B N   
13593 C CA  . ASP B 624  ? 0.2342 0.2668 0.2163 0.0230  0.0288  -0.0046 622  ASP B CA  
13594 C C   . ASP B 624  ? 0.2570 0.2866 0.2370 0.0224  0.0258  -0.0058 622  ASP B C   
13595 O O   . ASP B 624  ? 0.3325 0.3617 0.3091 0.0220  0.0249  -0.0050 622  ASP B O   
13596 C CB  . ASP B 624  ? 0.2988 0.3318 0.2775 0.0250  0.0304  -0.0067 622  ASP B CB  
13597 C CG  . ASP B 624  ? 0.3731 0.4100 0.3531 0.0257  0.0336  -0.0054 622  ASP B CG  
13598 O OD1 . ASP B 624  ? 0.4430 0.4821 0.4253 0.0245  0.0346  -0.0025 622  ASP B OD1 
13599 O OD2 . ASP B 624  ? 0.4297 0.4675 0.4083 0.0276  0.0351  -0.0071 622  ASP B OD2 
13600 N N   . ALA B 625  ? 0.3078 0.3356 0.2899 0.0222  0.0243  -0.0076 623  ALA B N   
13601 C CA  . ALA B 625  ? 0.3621 0.3874 0.3425 0.0214  0.0215  -0.0088 623  ALA B CA  
13602 C C   . ALA B 625  ? 0.3048 0.3302 0.2891 0.0200  0.0200  -0.0074 623  ALA B C   
13603 O O   . ALA B 625  ? 0.2887 0.3129 0.2723 0.0192  0.0178  -0.0081 623  ALA B O   
13604 C CB  . ALA B 625  ? 0.4417 0.4648 0.4218 0.0219  0.0207  -0.0116 623  ALA B CB  
13605 N N   . ALA B 626  ? 0.2395 0.2665 0.2278 0.0196  0.0212  -0.0054 624  ALA B N   
13606 C CA  . ALA B 626  ? 0.2281 0.2548 0.2198 0.0185  0.0198  -0.0042 624  ALA B CA  
13607 C C   . ALA B 626  ? 0.2289 0.2554 0.2181 0.0182  0.0181  -0.0033 624  ALA B C   
13608 O O   . ALA B 626  ? 0.2401 0.2660 0.2307 0.0176  0.0161  -0.0037 624  ALA B O   
13609 C CB  . ALA B 626  ? 0.2182 0.2460 0.2139 0.0181  0.0212  -0.0022 624  ALA B CB  
13610 N N   . PRO B 627  ? 0.2294 0.2566 0.2150 0.0186  0.0186  -0.0020 625  PRO B N   
13611 C CA  . PRO B 627  ? 0.2416 0.2687 0.2249 0.0184  0.0167  -0.0011 625  PRO B CA  
13612 C C   . PRO B 627  ? 0.2427 0.2691 0.2238 0.0181  0.0145  -0.0032 625  PRO B C   
13613 O O   . PRO B 627  ? 0.2429 0.2698 0.2248 0.0176  0.0126  -0.0029 625  PRO B O   
13614 C CB  . PRO B 627  ? 0.2683 0.2962 0.2476 0.0189  0.0179  0.0005  625  PRO B CB  
13615 C CG  . PRO B 627  ? 0.3409 0.3695 0.3218 0.0191  0.0206  0.0013  625  PRO B CG  
13616 C CD  . PRO B 627  ? 0.2530 0.2813 0.2366 0.0192  0.0210  -0.0010 625  PRO B CD  
13617 N N   . ASP B 628  ? 0.2407 0.2661 0.2191 0.0183  0.0148  -0.0054 626  ASP B N   
13618 C CA  . ASP B 628  ? 0.2645 0.2888 0.2403 0.0177  0.0126  -0.0073 626  ASP B CA  
13619 C C   . ASP B 628  ? 0.2520 0.2759 0.2318 0.0167  0.0111  -0.0081 626  ASP B C   
13620 O O   . ASP B 628  ? 0.2662 0.2904 0.2456 0.0158  0.0089  -0.0085 626  ASP B O   
13621 C CB  . ASP B 628  ? 0.2689 0.2913 0.2405 0.0184  0.0131  -0.0096 626  ASP B CB  
13622 C CG  . ASP B 628  ? 0.3671 0.3900 0.3338 0.0194  0.0144  -0.0090 626  ASP B CG  
13623 O OD1 . ASP B 628  ? 0.3860 0.4102 0.3512 0.0192  0.0138  -0.0072 626  ASP B OD1 
13624 O OD2 . ASP B 628  ? 0.4562 0.4783 0.4205 0.0205  0.0159  -0.0103 626  ASP B OD2 
13625 N N   . TRP B 629  ? 0.2107 0.2342 0.1944 0.0168  0.0123  -0.0083 627  TRP B N   
13626 C CA  . TRP B 629  ? 0.2110 0.2342 0.1983 0.0159  0.0110  -0.0090 627  TRP B CA  
13627 C C   . TRP B 629  ? 0.2022 0.2271 0.1925 0.0155  0.0102  -0.0072 627  TRP B C   
13628 O O   . TRP B 629  ? 0.2046 0.2300 0.1960 0.0147  0.0085  -0.0075 627  TRP B O   
13629 C CB  . TRP B 629  ? 0.2023 0.2244 0.1925 0.0162  0.0124  -0.0098 627  TRP B CB  
13630 C CG  . TRP B 629  ? 0.1677 0.1894 0.1612 0.0153  0.0111  -0.0104 627  TRP B CG  
13631 C CD1 . TRP B 629  ? 0.1855 0.2076 0.1833 0.0152  0.0116  -0.0096 627  TRP B CD1 
13632 C CD2 . TRP B 629  ? 0.1812 0.2017 0.1735 0.0142  0.0092  -0.0118 627  TRP B CD2 
13633 N NE1 . TRP B 629  ? 0.1835 0.2050 0.1830 0.0142  0.0102  -0.0105 627  TRP B NE1 
13634 C CE2 . TRP B 629  ? 0.1675 0.1881 0.1638 0.0135  0.0088  -0.0118 627  TRP B CE2 
13635 C CE3 . TRP B 629  ? 0.2030 0.2223 0.1913 0.0135  0.0077  -0.0131 627  TRP B CE3 
13636 C CZ2 . TRP B 629  ? 0.1823 0.2020 0.1786 0.0122  0.0070  -0.0128 627  TRP B CZ2 
13637 C CZ3 . TRP B 629  ? 0.2053 0.2236 0.1938 0.0120  0.0058  -0.0142 627  TRP B CZ3 
13638 C CH2 . TRP B 629  ? 0.2098 0.2285 0.2023 0.0113  0.0056  -0.0139 627  TRP B CH2 
13639 N N   . ALA B 630  ? 0.1995 0.2253 0.1909 0.0162  0.0115  -0.0052 628  ALA B N   
13640 C CA  . ALA B 630  ? 0.2095 0.2363 0.2033 0.0162  0.0107  -0.0034 628  ALA B CA  
13641 C C   . ALA B 630  ? 0.2045 0.2327 0.1960 0.0161  0.0087  -0.0032 628  ALA B C   
13642 O O   . ALA B 630  ? 0.2406 0.2701 0.2343 0.0160  0.0075  -0.0026 628  ALA B O   
13643 C CB  . ALA B 630  ? 0.2306 0.2574 0.2249 0.0169  0.0122  -0.0013 628  ALA B CB  
13644 N N   . ALA B 631  ? 0.2174 0.2456 0.2045 0.0161  0.0084  -0.0037 629  ALA B N   
13645 C CA  . ALA B 631  ? 0.2267 0.2564 0.2115 0.0159  0.0064  -0.0034 629  ALA B CA  
13646 C C   . ALA B 631  ? 0.2348 0.2650 0.2199 0.0146  0.0044  -0.0051 629  ALA B C   
13647 O O   . ALA B 631  ? 0.2513 0.2834 0.2355 0.0141  0.0024  -0.0048 629  ALA B O   
13648 C CB  . ALA B 631  ? 0.2566 0.2858 0.2360 0.0163  0.0066  -0.0034 629  ALA B CB  
13649 N N   . VAL B 632  ? 0.2113 0.2399 0.1977 0.0138  0.0047  -0.0068 630  VAL B N   
13650 C CA  . VAL B 632  ? 0.2026 0.2315 0.1896 0.0123  0.0028  -0.0081 630  VAL B CA  
13651 C C   . VAL B 632  ? 0.2195 0.2510 0.2109 0.0122  0.0022  -0.0070 630  VAL B C   
13652 O O   . VAL B 632  ? 0.2237 0.2548 0.2184 0.0129  0.0035  -0.0064 630  VAL B O   
13653 C CB  . VAL B 632  ? 0.2240 0.2501 0.2110 0.0117  0.0034  -0.0101 630  VAL B CB  
13654 C CG1 . VAL B 632  ? 0.2113 0.2376 0.1991 0.0098  0.0014  -0.0111 630  VAL B CG1 
13655 C CG2 . VAL B 632  ? 0.2203 0.2438 0.2026 0.0122  0.0040  -0.0114 630  VAL B CG2 
13656 N N   . PRO B 633  ? 0.2116 0.2458 0.2032 0.0114  0.0002  -0.0067 631  PRO B N   
13657 C CA  . PRO B 633  ? 0.2331 0.2703 0.2289 0.0118  -0.0002 -0.0055 631  PRO B CA  
13658 C C   . PRO B 633  ? 0.2068 0.2431 0.2059 0.0112  0.0005  -0.0063 631  PRO B C   
13659 O O   . PRO B 633  ? 0.1957 0.2302 0.1941 0.0099  0.0002  -0.0079 631  PRO B O   
13660 C CB  . PRO B 633  ? 0.2264 0.2670 0.2216 0.0106  -0.0026 -0.0056 631  PRO B CB  
13661 C CG  . PRO B 633  ? 0.2459 0.2855 0.2363 0.0104  -0.0033 -0.0059 631  PRO B CG  
13662 C CD  . PRO B 633  ? 0.2029 0.2380 0.1909 0.0104  -0.0017 -0.0072 631  PRO B CD  
13663 N N   . PRO B 634  ? 0.1943 0.2315 0.1968 0.0124  0.0012  -0.0053 632  PRO B N   
13664 C CA  . PRO B 634  ? 0.2001 0.2366 0.2056 0.0119  0.0018  -0.0060 632  PRO B CA  
13665 C C   . PRO B 634  ? 0.1992 0.2370 0.2051 0.0099  0.0005  -0.0071 632  PRO B C   
13666 O O   . PRO B 634  ? 0.1882 0.2238 0.1946 0.0090  0.0009  -0.0082 632  PRO B O   
13667 C CB  . PRO B 634  ? 0.2207 0.2587 0.2292 0.0135  0.0022  -0.0046 632  PRO B CB  
13668 C CG  . PRO B 634  ? 0.2538 0.2914 0.2607 0.0150  0.0026  -0.0032 632  PRO B CG  
13669 C CD  . PRO B 634  ? 0.2183 0.2568 0.2217 0.0142  0.0015  -0.0035 632  PRO B CD  
13670 N N   . SER B 635  ? 0.2066 0.2480 0.2125 0.0092  -0.0012 -0.0068 633  SER B N   
13671 C CA  . SER B 635  ? 0.2189 0.2617 0.2253 0.0069  -0.0024 -0.0076 633  SER B CA  
13672 C C   . SER B 635  ? 0.1986 0.2377 0.2016 0.0052  -0.0030 -0.0092 633  SER B C   
13673 O O   . SER B 635  ? 0.1960 0.2338 0.1992 0.0035  -0.0034 -0.0101 633  SER B O   
13674 C CB  . SER B 635  ? 0.2517 0.2997 0.2589 0.0063  -0.0042 -0.0068 633  SER B CB  
13675 O OG  . SER B 635  ? 0.3616 0.4095 0.3654 0.0062  -0.0053 -0.0067 633  SER B OG  
13676 N N   . GLU B 636  ? 0.2015 0.2385 0.2009 0.0057  -0.0029 -0.0095 634  GLU B N   
13677 C CA  . GLU B 636  ? 0.1900 0.2230 0.1857 0.0045  -0.0033 -0.0111 634  GLU B CA  
13678 C C   . GLU B 636  ? 0.1952 0.2243 0.1913 0.0054  -0.0015 -0.0119 634  GLU B C   
13679 O O   . GLU B 636  ? 0.1886 0.2145 0.1831 0.0043  -0.0019 -0.0133 634  GLU B O   
13680 C CB  . GLU B 636  ? 0.2008 0.2330 0.1922 0.0050  -0.0038 -0.0113 634  GLU B CB  
13681 C CG  . GLU B 636  ? 0.3615 0.3892 0.3486 0.0042  -0.0041 -0.0132 634  GLU B CG  
13682 C CD  . GLU B 636  ? 0.4181 0.4445 0.4047 0.0015  -0.0058 -0.0144 634  GLU B CD  
13683 O OE1 . GLU B 636  ? 0.3914 0.4212 0.3790 -0.0003 -0.0077 -0.0138 634  GLU B OE1 
13684 O OE2 . GLU B 636  ? 0.3709 0.3930 0.3563 0.0013  -0.0054 -0.0157 634  GLU B OE2 
13685 N N   . ARG B 637  ? 0.1644 0.1935 0.1624 0.0073  0.0003  -0.0110 635  ARG B N   
13686 C CA  . ARG B 637  ? 0.1757 0.2020 0.1749 0.0080  0.0018  -0.0117 635  ARG B CA  
13687 C C   . ARG B 637  ? 0.1652 0.1914 0.1668 0.0068  0.0013  -0.0121 635  ARG B C   
13688 O O   . ARG B 637  ? 0.1817 0.2048 0.1827 0.0063  0.0014  -0.0132 635  ARG B O   
13689 C CB  . ARG B 637  ? 0.1732 0.1999 0.1743 0.0099  0.0035  -0.0104 635  ARG B CB  
13690 C CG  . ARG B 637  ? 0.1794 0.2062 0.1778 0.0110  0.0041  -0.0097 635  ARG B CG  
13691 C CD  . ARG B 637  ? 0.1834 0.2098 0.1834 0.0125  0.0060  -0.0086 635  ARG B CD  
13692 N NE  . ARG B 637  ? 0.1895 0.2175 0.1930 0.0129  0.0061  -0.0073 635  ARG B NE  
13693 C CZ  . ARG B 637  ? 0.1964 0.2256 0.2003 0.0140  0.0064  -0.0056 635  ARG B CZ  
13694 N NH1 . ARG B 637  ? 0.2604 0.2899 0.2613 0.0145  0.0064  -0.0049 635  ARG B NH1 
13695 N NH2 . ARG B 637  ? 0.1971 0.2267 0.2039 0.0146  0.0066  -0.0047 635  ARG B NH2 
13696 N N   . ALA B 638  ? 0.1523 0.1820 0.1567 0.0064  0.0007  -0.0111 636  ALA B N   
13697 C CA  . ALA B 638  ? 0.1612 0.1913 0.1677 0.0052  0.0003  -0.0113 636  ALA B CA  
13698 C C   . ALA B 638  ? 0.1592 0.1879 0.1635 0.0028  -0.0012 -0.0124 636  ALA B C   
13699 O O   . ALA B 638  ? 0.1614 0.1881 0.1661 0.0018  -0.0013 -0.0131 636  ALA B O   
13700 C CB  . ALA B 638  ? 0.1578 0.1924 0.1673 0.0056  0.0001  -0.0101 636  ALA B CB  
13701 N N   . ALA B 639  ? 0.1719 0.2014 0.1736 0.0018  -0.0025 -0.0126 637  ALA B N   
13702 C CA  . ALA B 639  ? 0.1753 0.2029 0.1745 -0.0007 -0.0042 -0.0137 637  ALA B CA  
13703 C C   . ALA B 639  ? 0.1727 0.1944 0.1690 -0.0005 -0.0038 -0.0152 637  ALA B C   
13704 O O   . ALA B 639  ? 0.1754 0.1945 0.1705 -0.0023 -0.0048 -0.0160 637  ALA B O   
13705 C CB  . ALA B 639  ? 0.1749 0.2042 0.1715 -0.0018 -0.0059 -0.0136 637  ALA B CB  
13706 N N   . CYS B 640  ? 0.1711 0.1910 0.1664 0.0017  -0.0024 -0.0155 638  CYS B N   
13707 C CA  . CYS B 640  ? 0.1705 0.1854 0.1636 0.0025  -0.0018 -0.0169 638  CYS B CA  
13708 C C   . CYS B 640  ? 0.1536 0.1674 0.1495 0.0024  -0.0012 -0.0169 638  CYS B C   
13709 O O   . CYS B 640  ? 0.1740 0.1839 0.1682 0.0017  -0.0018 -0.0180 638  CYS B O   
13710 C CB  . CYS B 640  ? 0.1537 0.1681 0.1462 0.0050  0.0000  -0.0169 638  CYS B CB  
13711 S SG  . CYS B 640  ? 0.1992 0.2138 0.1873 0.0053  -0.0005 -0.0172 638  CYS B SG  
13712 N N   . LEU B 641  ? 0.1506 0.1674 0.1504 0.0032  -0.0001 -0.0157 639  LEU B N   
13713 C CA  . LEU B 641  ? 0.1607 0.1766 0.1630 0.0032  0.0003  -0.0157 639  LEU B CA  
13714 C C   . LEU B 641  ? 0.1581 0.1736 0.1599 0.0007  -0.0012 -0.0158 639  LEU B C   
13715 O O   . LEU B 641  ? 0.1627 0.1751 0.1641 0.0001  -0.0015 -0.0165 639  LEU B O   
13716 C CB  . LEU B 641  ? 0.1624 0.1815 0.1685 0.0044  0.0015  -0.0144 639  LEU B CB  
13717 C CG  . LEU B 641  ? 0.1675 0.1859 0.1749 0.0065  0.0032  -0.0142 639  LEU B CG  
13718 C CD1 . LEU B 641  ? 0.2215 0.2399 0.2269 0.0077  0.0038  -0.0141 639  LEU B CD1 
13719 C CD2 . LEU B 641  ? 0.1532 0.1742 0.1641 0.0073  0.0039  -0.0130 639  LEU B CD2 
13720 N N   . ASP B 642  ? 0.1563 0.1754 0.1585 -0.0009 -0.0022 -0.0151 640  ASP B N   
13721 C CA  . ASP B 642  ? 0.1664 0.1857 0.1684 -0.0036 -0.0037 -0.0151 640  ASP B CA  
13722 C C   . ASP B 642  ? 0.1590 0.1733 0.1568 -0.0052 -0.0051 -0.0163 640  ASP B C   
13723 O O   . ASP B 642  ? 0.1694 0.1812 0.1665 -0.0069 -0.0058 -0.0166 640  ASP B O   
13724 C CB  . ASP B 642  ? 0.1694 0.1942 0.1727 -0.0049 -0.0045 -0.0140 640  ASP B CB  
13725 C CG  . ASP B 642  ? 0.1959 0.2254 0.2033 -0.0037 -0.0034 -0.0128 640  ASP B CG  
13726 O OD1 . ASP B 642  ? 0.1910 0.2194 0.2001 -0.0028 -0.0024 -0.0127 640  ASP B OD1 
13727 O OD2 . ASP B 642  ? 0.1983 0.2326 0.2072 -0.0037 -0.0038 -0.0119 640  ASP B OD2 
13728 N N   . ARG B 643  ? 0.1700 0.1823 0.1647 -0.0046 -0.0055 -0.0172 641  ARG B N   
13729 C CA  . ARG B 643  ? 0.1951 0.2018 0.1853 -0.0058 -0.0068 -0.0187 641  ARG B CA  
13730 C C   . ARG B 643  ? 0.1778 0.1797 0.1674 -0.0044 -0.0060 -0.0195 641  ARG B C   
13731 O O   . ARG B 643  ? 0.1804 0.1779 0.1678 -0.0058 -0.0071 -0.0203 641  ARG B O   
13732 C CB  . ARG B 643  ? 0.1916 0.1969 0.1781 -0.0051 -0.0072 -0.0196 641  ARG B CB  
13733 C CG  . ARG B 643  ? 0.2106 0.2189 0.1961 -0.0075 -0.0091 -0.0191 641  ARG B CG  
13734 C CD  . ARG B 643  ? 0.2362 0.2423 0.2171 -0.0071 -0.0099 -0.0203 641  ARG B CD  
13735 N NE  . ARG B 643  ? 0.2368 0.2445 0.2182 -0.0041 -0.0080 -0.0200 641  ARG B NE  
13736 C CZ  . ARG B 643  ? 0.2383 0.2511 0.2214 -0.0035 -0.0078 -0.0188 641  ARG B CZ  
13737 N NH1 . ARG B 643  ? 0.2516 0.2687 0.2363 -0.0055 -0.0092 -0.0177 641  ARG B NH1 
13738 N NH2 . ARG B 643  ? 0.2698 0.2833 0.2530 -0.0008 -0.0061 -0.0185 641  ARG B NH2 
13739 N N   . ALA B 644  ? 0.1597 0.1624 0.1515 -0.0016 -0.0040 -0.0194 642  ALA B N   
13740 C CA  . ALA B 644  ? 0.1695 0.1685 0.1613 -0.0001 -0.0033 -0.0201 642  ALA B CA  
13741 C C   . ALA B 644  ? 0.1794 0.1780 0.1730 -0.0015 -0.0038 -0.0195 642  ALA B C   
13742 O O   . ALA B 644  ? 0.1732 0.1673 0.1652 -0.0017 -0.0044 -0.0203 642  ALA B O   
13743 C CB  . ALA B 644  ? 0.1705 0.1714 0.1649 0.0028  -0.0012 -0.0198 642  ALA B CB  
13744 N N   . ALA B 645  ? 0.1699 0.1732 0.1668 -0.0026 -0.0036 -0.0182 643  ALA B N   
13745 C CA  . ALA B 645  ? 0.1660 0.1693 0.1644 -0.0040 -0.0040 -0.0176 643  ALA B CA  
13746 C C   . ALA B 645  ? 0.1559 0.1560 0.1512 -0.0069 -0.0059 -0.0179 643  ALA B C   
13747 O O   . ALA B 645  ? 0.1847 0.1815 0.1793 -0.0077 -0.0064 -0.0179 643  ALA B O   
13748 C CB  . ALA B 645  ? 0.1733 0.1825 0.1754 -0.0043 -0.0033 -0.0162 643  ALA B CB  
13749 N N   . GLU B 646  ? 0.1727 0.1735 0.1659 -0.0087 -0.0071 -0.0180 644  GLU B N   
13750 C CA  . GLU B 646  ? 0.1928 0.1902 0.1828 -0.0118 -0.0091 -0.0182 644  GLU B CA  
13751 C C   . GLU B 646  ? 0.1882 0.1780 0.1742 -0.0111 -0.0098 -0.0197 644  GLU B C   
13752 O O   . GLU B 646  ? 0.1954 0.1811 0.1794 -0.0130 -0.0111 -0.0197 644  GLU B O   
13753 C CB  . GLU B 646  ? 0.2175 0.2169 0.2058 -0.0137 -0.0105 -0.0183 644  GLU B CB  
13754 C CG  . GLU B 646  ? 0.2664 0.2733 0.2583 -0.0149 -0.0103 -0.0168 644  GLU B CG  
13755 C CD  . GLU B 646  ? 0.3631 0.3723 0.3571 -0.0173 -0.0106 -0.0155 644  GLU B CD  
13756 O OE1 . GLU B 646  ? 0.4363 0.4419 0.4277 -0.0201 -0.0121 -0.0156 644  GLU B OE1 
13757 O OE2 . GLU B 646  ? 0.3660 0.3804 0.3640 -0.0163 -0.0092 -0.0145 644  GLU B OE2 
13758 N N   . LEU B 647  ? 0.1970 0.1848 0.1816 -0.0083 -0.0090 -0.0209 645  LEU B N   
13759 C CA  . LEU B 647  ? 0.2076 0.1884 0.1884 -0.0070 -0.0095 -0.0225 645  LEU B CA  
13760 C C   . LEU B 647  ? 0.1956 0.1745 0.1782 -0.0057 -0.0088 -0.0222 645  LEU B C   
13761 O O   . LEU B 647  ? 0.2163 0.1895 0.1960 -0.0063 -0.0100 -0.0228 645  LEU B O   
13762 C CB  . LEU B 647  ? 0.1968 0.1769 0.1762 -0.0040 -0.0085 -0.0237 645  LEU B CB  
13763 C CG  . LEU B 647  ? 0.2106 0.1917 0.1873 -0.0050 -0.0093 -0.0242 645  LEU B CG  
13764 C CD1 . LEU B 647  ? 0.2228 0.2033 0.1981 -0.0017 -0.0079 -0.0253 645  LEU B CD1 
13765 C CD2 . LEU B 647  ? 0.2527 0.2285 0.2246 -0.0078 -0.0118 -0.0250 645  LEU B CD2 
13766 N N   . MET B 648  ? 0.1771 0.1605 0.1641 -0.0040 -0.0071 -0.0214 646  MET B N   
13767 C CA  . MET B 648  ? 0.1706 0.1525 0.1592 -0.0030 -0.0066 -0.0211 646  MET B CA  
13768 C C   . MET B 648  ? 0.1872 0.1680 0.1754 -0.0059 -0.0079 -0.0202 646  MET B C   
13769 O O   . MET B 648  ? 0.2133 0.1898 0.2002 -0.0058 -0.0085 -0.0203 646  MET B O   
13770 C CB  . MET B 648  ? 0.2099 0.1969 0.2032 -0.0010 -0.0047 -0.0203 646  MET B CB  
13771 C CG  . MET B 648  ? 0.1950 0.1825 0.1890 0.0020  -0.0033 -0.0210 646  MET B CG  
13772 S SD  . MET B 648  ? 0.2103 0.2022 0.2096 0.0038  -0.0015 -0.0200 646  MET B SD  
13773 C CE  . MET B 648  ? 0.2500 0.2429 0.2495 0.0067  0.0001  -0.0207 646  MET B CE  
13774 N N   . GLN B 649  ? 0.1881 0.1729 0.1773 -0.0086 -0.0083 -0.0191 647  GLN B N   
13775 C CA  . GLN B 649  ? 0.2027 0.1870 0.1916 -0.0116 -0.0094 -0.0181 647  GLN B CA  
13776 C C   . GLN B 649  ? 0.1873 0.1645 0.1712 -0.0136 -0.0115 -0.0188 647  GLN B C   
13777 O O   . GLN B 649  ? 0.2253 0.1987 0.2078 -0.0146 -0.0123 -0.0184 647  GLN B O   
13778 C CB  . GLN B 649  ? 0.1864 0.1770 0.1774 -0.0140 -0.0094 -0.0168 647  GLN B CB  
13779 C CG  . GLN B 649  ? 0.2054 0.1969 0.1966 -0.0171 -0.0101 -0.0155 647  GLN B CG  
13780 C CD  . GLN B 649  ? 0.1922 0.1856 0.1862 -0.0158 -0.0088 -0.0148 647  GLN B CD  
13781 O OE1 . GLN B 649  ? 0.2035 0.2027 0.2011 -0.0147 -0.0074 -0.0141 647  GLN B OE1 
13782 N NE2 . GLN B 649  ? 0.2092 0.1974 0.2013 -0.0156 -0.0093 -0.0149 647  GLN B NE2 
13783 N N   . ALA B 650  ? 0.2077 0.1829 0.1885 -0.0141 -0.0124 -0.0198 648  ALA B N   
13784 C CA  . ALA B 650  ? 0.2286 0.1966 0.2043 -0.0162 -0.0146 -0.0205 648  ALA B CA  
13785 C C   . ALA B 650  ? 0.2479 0.2088 0.2209 -0.0135 -0.0148 -0.0218 648  ALA B C   
13786 O O   . ALA B 650  ? 0.2717 0.2261 0.2410 -0.0150 -0.0165 -0.0220 648  ALA B O   
13787 C CB  . ALA B 650  ? 0.2501 0.2175 0.2230 -0.0171 -0.0157 -0.0215 648  ALA B CB  
13788 N N   . ARG B 651  ? 0.2208 0.1830 0.1957 -0.0095 -0.0131 -0.0226 649  ARG B N   
13789 C CA  . ARG B 651  ? 0.2111 0.1677 0.1840 -0.0065 -0.0131 -0.0238 649  ARG B CA  
13790 C C   . ARG B 651  ? 0.2324 0.1900 0.2085 -0.0051 -0.0122 -0.0230 649  ARG B C   
13791 O O   . ARG B 651  ? 0.2337 0.1881 0.2093 -0.0021 -0.0119 -0.0238 649  ARG B O   
13792 C CB  . ARG B 651  ? 0.2404 0.1977 0.2131 -0.0031 -0.0118 -0.0253 649  ARG B CB  
13793 C CG  . ARG B 651  ? 0.2506 0.2059 0.2194 -0.0045 -0.0129 -0.0263 649  ARG B CG  
13794 C CD  . ARG B 651  ? 0.2553 0.2125 0.2239 -0.0015 -0.0115 -0.0274 649  ARG B CD  
13795 N NE  . ARG B 651  ? 0.2717 0.2279 0.2368 -0.0033 -0.0127 -0.0282 649  ARG B NE  
13796 C CZ  . ARG B 651  ? 0.2616 0.2196 0.2257 -0.0015 -0.0117 -0.0291 649  ARG B CZ  
13797 N NH1 . ARG B 651  ? 0.2495 0.2101 0.2158 0.0022  -0.0095 -0.0294 649  ARG B NH1 
13798 N NH2 . ARG B 651  ? 0.2642 0.2215 0.2250 -0.0035 -0.0131 -0.0296 649  ARG B NH2 
13799 N N   . MET B 652  ? 0.2088 0.1711 0.1881 -0.0070 -0.0118 -0.0213 650  MET B N   
13800 C CA  . MET B 652  ? 0.2092 0.1726 0.1913 -0.0058 -0.0111 -0.0205 650  MET B CA  
13801 C C   . MET B 652  ? 0.2264 0.1827 0.2054 -0.0050 -0.0124 -0.0210 650  MET B C   
13802 O O   . MET B 652  ? 0.2351 0.1913 0.2159 -0.0020 -0.0116 -0.0213 650  MET B O   
13803 C CB  . MET B 652  ? 0.2103 0.1785 0.1949 -0.0085 -0.0108 -0.0188 650  MET B CB  
13804 C CG  . MET B 652  ? 0.2099 0.1789 0.1968 -0.0074 -0.0102 -0.0180 650  MET B CG  
13805 S SD  . MET B 652  ? 0.2431 0.2178 0.2325 -0.0103 -0.0097 -0.0162 650  MET B SD  
13806 C CE  . MET B 652  ? 0.2050 0.1873 0.1989 -0.0086 -0.0077 -0.0162 650  MET B CE  
13807 N N   . PRO B 653  ? 0.2165 0.1667 0.1910 -0.0073 -0.0144 -0.0210 651  PRO B N   
13808 C CA  . PRO B 653  ? 0.2578 0.2010 0.2294 -0.0062 -0.0157 -0.0213 651  PRO B CA  
13809 C C   . PRO B 653  ? 0.2577 0.1980 0.2286 -0.0018 -0.0152 -0.0231 651  PRO B C   
13810 O O   . PRO B 653  ? 0.2432 0.1819 0.2149 0.0006  -0.0152 -0.0231 651  PRO B O   
13811 C CB  . PRO B 653  ? 0.2606 0.1975 0.2270 -0.0097 -0.0180 -0.0211 651  PRO B CB  
13812 C CG  . PRO B 653  ? 0.2390 0.1817 0.2071 -0.0136 -0.0177 -0.0198 651  PRO B CG  
13813 C CD  . PRO B 653  ? 0.2354 0.1852 0.2076 -0.0115 -0.0157 -0.0204 651  PRO B CD  
13814 N N   . THR B 654  ? 0.2357 0.1759 0.2053 -0.0006 -0.0148 -0.0245 652  THR B N   
13815 C CA  . THR B 654  ? 0.2474 0.1856 0.2163 0.0037  -0.0141 -0.0262 652  THR B CA  
13816 C C   . THR B 654  ? 0.2571 0.2021 0.2318 0.0065  -0.0119 -0.0258 652  THR B C   
13817 O O   . THR B 654  ? 0.2404 0.1845 0.2161 0.0098  -0.0115 -0.0264 652  THR B O   
13818 C CB  . THR B 654  ? 0.2572 0.1938 0.2229 0.0040  -0.0142 -0.0277 652  THR B CB  
13819 O OG1 . THR B 654  ? 0.2947 0.2244 0.2550 0.0012  -0.0165 -0.0281 652  THR B OG1 
13820 C CG2 . THR B 654  ? 0.2807 0.2157 0.2458 0.0087  -0.0132 -0.0295 652  THR B CG2 
13821 N N   . LEU B 655  ? 0.2257 0.1777 0.2042 0.0052  -0.0105 -0.0249 653  LEU B N   
13822 C CA  . LEU B 655  ? 0.2209 0.1791 0.2046 0.0074  -0.0085 -0.0244 653  LEU B CA  
13823 C C   . LEU B 655  ? 0.2366 0.1945 0.2223 0.0079  -0.0088 -0.0235 653  LEU B C   
13824 O O   . LEU B 655  ? 0.2319 0.1918 0.2205 0.0107  -0.0079 -0.0237 653  LEU B O   
13825 C CB  . LEU B 655  ? 0.2109 0.1756 0.1977 0.0056  -0.0073 -0.0234 653  LEU B CB  
13826 C CG  . LEU B 655  ? 0.2511 0.2167 0.2360 0.0051  -0.0071 -0.0241 653  LEU B CG  
13827 C CD1 . LEU B 655  ? 0.2466 0.2186 0.2347 0.0034  -0.0061 -0.0229 653  LEU B CD1 
13828 C CD2 . LEU B 655  ? 0.2941 0.2596 0.2788 0.0085  -0.0058 -0.0254 653  LEU B CD2 
13829 N N   . LEU B 656  ? 0.2343 0.1900 0.2186 0.0051  -0.0102 -0.0225 654  LEU B N   
13830 C CA  . LEU B 656  ? 0.2340 0.1890 0.2195 0.0054  -0.0107 -0.0216 654  LEU B CA  
13831 C C   . LEU B 656  ? 0.2544 0.2046 0.2384 0.0086  -0.0114 -0.0226 654  LEU B C   
13832 O O   . LEU B 656  ? 0.2557 0.2078 0.2427 0.0107  -0.0110 -0.0224 654  LEU B O   
13833 C CB  . LEU B 656  ? 0.2779 0.2299 0.2607 0.0019  -0.0123 -0.0204 654  LEU B CB  
13834 C CG  . LEU B 656  ? 0.3307 0.2872 0.3148 -0.0015 -0.0118 -0.0193 654  LEU B CG  
13835 C CD1 . LEU B 656  ? 0.3132 0.2671 0.2950 -0.0046 -0.0132 -0.0179 654  LEU B CD1 
13836 C CD2 . LEU B 656  ? 0.2810 0.2447 0.2702 -0.0005 -0.0099 -0.0188 654  LEU B CD2 
13837 N N   . GLY B 657  ? 0.2411 0.1849 0.2204 0.0089  -0.0127 -0.0237 655  GLY B N   
13838 C CA  . GLY B 657  ? 0.2771 0.2159 0.2545 0.0122  -0.0135 -0.0247 655  GLY B CA  
13839 C C   . GLY B 657  ? 0.2673 0.2106 0.2485 0.0161  -0.0118 -0.0255 655  GLY B C   
13840 O O   . GLY B 657  ? 0.2595 0.2027 0.2424 0.0188  -0.0119 -0.0256 655  GLY B O   
13841 N N   . LEU B 658  ? 0.2364 0.1841 0.2192 0.0164  -0.0101 -0.0261 656  LEU B N   
13842 C CA  . LEU B 658  ? 0.2058 0.1582 0.1923 0.0198  -0.0082 -0.0267 656  LEU B CA  
13843 C C   . LEU B 658  ? 0.2147 0.1731 0.2068 0.0199  -0.0073 -0.0254 656  LEU B C   
13844 O O   . LEU B 658  ? 0.2224 0.1826 0.2172 0.0227  -0.0069 -0.0255 656  LEU B O   
13845 C CB  . LEU B 658  ? 0.2238 0.1793 0.2102 0.0198  -0.0067 -0.0274 656  LEU B CB  
13846 C CG  . LEU B 658  ? 0.2043 0.1645 0.1940 0.0232  -0.0046 -0.0279 656  LEU B CG  
13847 C CD1 . LEU B 658  ? 0.2257 0.1826 0.2141 0.0271  -0.0049 -0.0292 656  LEU B CD1 
13848 C CD2 . LEU B 658  ? 0.2077 0.1701 0.1964 0.0228  -0.0033 -0.0285 656  LEU B CD2 
13849 N N   . ILE B 659  ? 0.2086 0.1700 0.2023 0.0168  -0.0071 -0.0241 657  ILE B N   
13850 C CA  . ILE B 659  ? 0.1875 0.1542 0.1861 0.0168  -0.0063 -0.0230 657  ILE B CA  
13851 C C   . ILE B 659  ? 0.1944 0.1586 0.1931 0.0176  -0.0077 -0.0226 657  ILE B C   
13852 O O   . ILE B 659  ? 0.2066 0.1741 0.2091 0.0193  -0.0073 -0.0223 657  ILE B O   
13853 C CB  . ILE B 659  ? 0.1888 0.1587 0.1884 0.0135  -0.0060 -0.0219 657  ILE B CB  
13854 C CG1 . ILE B 659  ? 0.1983 0.1715 0.1986 0.0133  -0.0045 -0.0222 657  ILE B CG1 
13855 C CG2 . ILE B 659  ? 0.2298 0.2036 0.2333 0.0132  -0.0056 -0.0208 657  ILE B CG2 
13856 C CD1 . ILE B 659  ? 0.2085 0.1834 0.2083 0.0102  -0.0045 -0.0213 657  ILE B CD1 
13857 N N   . ILE B 660  ? 0.1973 0.1557 0.1919 0.0162  -0.0096 -0.0224 658  ILE B N   
13858 C CA  . ILE B 660  ? 0.1946 0.1499 0.1887 0.0169  -0.0111 -0.0219 658  ILE B CA  
13859 C C   . ILE B 660  ? 0.2184 0.1733 0.2138 0.0210  -0.0111 -0.0228 658  ILE B C   
13860 O O   . ILE B 660  ? 0.2358 0.1927 0.2340 0.0224  -0.0115 -0.0223 658  ILE B O   
13861 C CB  . ILE B 660  ? 0.2088 0.1571 0.1974 0.0147  -0.0131 -0.0216 658  ILE B CB  
13862 C CG1 . ILE B 660  ? 0.2362 0.1864 0.2246 0.0107  -0.0131 -0.0202 658  ILE B CG1 
13863 C CG2 . ILE B 660  ? 0.2360 0.1797 0.2231 0.0163  -0.0149 -0.0213 658  ILE B CG2 
13864 C CD1 . ILE B 660  ? 0.2489 0.1927 0.2321 0.0080  -0.0148 -0.0198 658  ILE B CD1 
13865 N N   . ARG B 661  ? 0.2071 0.1595 0.2002 0.0230  -0.0109 -0.0242 659  ARG B N   
13866 C CA  . ARG B 661  ? 0.2047 0.1563 0.1985 0.0271  -0.0109 -0.0252 659  ARG B CA  
13867 C C   . ARG B 661  ? 0.2141 0.1732 0.2134 0.0293  -0.0088 -0.0254 659  ARG B C   
13868 O O   . ARG B 661  ? 0.2268 0.1877 0.2287 0.0323  -0.0088 -0.0255 659  ARG B O   
13869 C CB  . ARG B 661  ? 0.2281 0.1730 0.2166 0.0287  -0.0117 -0.0267 659  ARG B CB  
13870 C CG  . ARG B 661  ? 0.2682 0.2049 0.2516 0.0274  -0.0142 -0.0264 659  ARG B CG  
13871 C CD  . ARG B 661  ? 0.3111 0.2405 0.2886 0.0284  -0.0152 -0.0279 659  ARG B CD  
13872 N NE  . ARG B 661  ? 0.2753 0.2039 0.2528 0.0333  -0.0147 -0.0294 659  ARG B NE  
13873 C CZ  . ARG B 661  ? 0.2949 0.2237 0.2711 0.0352  -0.0135 -0.0311 659  ARG B CZ  
13874 N NH1 . ARG B 661  ? 0.3120 0.2416 0.2867 0.0326  -0.0127 -0.0314 659  ARG B NH1 
13875 N NH2 . ARG B 661  ? 0.2968 0.2249 0.2729 0.0400  -0.0130 -0.0325 659  ARG B NH2 
13876 N N   . GLU B 662  ? 0.2141 0.1775 0.2149 0.0279  -0.0070 -0.0253 660  GLU B N   
13877 C CA  . GLU B 662  ? 0.2048 0.1751 0.2105 0.0298  -0.0050 -0.0254 660  GLU B CA  
13878 C C   . GLU B 662  ? 0.2073 0.1829 0.2181 0.0286  -0.0047 -0.0240 660  GLU B C   
13879 O O   . GLU B 662  ? 0.2122 0.1924 0.2273 0.0306  -0.0039 -0.0239 660  GLU B O   
13880 C CB  . GLU B 662  ? 0.2298 0.2022 0.2348 0.0289  -0.0032 -0.0258 660  GLU B CB  
13881 C CG  . GLU B 662  ? 0.2319 0.2113 0.2416 0.0306  -0.0010 -0.0256 660  GLU B CG  
13882 C CD  . GLU B 662  ? 0.2119 0.1933 0.2206 0.0299  0.0007  -0.0260 660  GLU B CD  
13883 O OE1 . GLU B 662  ? 0.2279 0.2078 0.2344 0.0272  0.0004  -0.0257 660  GLU B OE1 
13884 O OE2 . GLU B 662  ? 0.2270 0.2118 0.2374 0.0323  0.0024  -0.0264 660  GLU B OE2 
13885 N N   . ALA B 663  ? 0.1864 0.1616 0.1968 0.0254  -0.0053 -0.0230 661  ALA B N   
13886 C CA  . ALA B 663  ? 0.1891 0.1693 0.2038 0.0241  -0.0048 -0.0219 661  ALA B CA  
13887 C C   . ALA B 663  ? 0.2108 0.1892 0.2254 0.0232  -0.0066 -0.0211 661  ALA B C   
13888 O O   . ALA B 663  ? 0.2729 0.2545 0.2902 0.0218  -0.0065 -0.0203 661  ALA B O   
13889 C CB  . ALA B 663  ? 0.2132 0.1959 0.2282 0.0215  -0.0037 -0.0214 661  ALA B CB  
13890 N N   . GLY B 664  ? 0.2294 0.2023 0.2406 0.0240  -0.0084 -0.0214 662  GLY B N   
13891 C CA  . GLY B 664  ? 0.2459 0.2170 0.2567 0.0233  -0.0101 -0.0205 662  GLY B CA  
13892 C C   . GLY B 664  ? 0.2450 0.2151 0.2540 0.0198  -0.0105 -0.0196 662  GLY B C   
13893 O O   . GLY B 664  ? 0.2511 0.2217 0.2608 0.0189  -0.0115 -0.0188 662  GLY B O   
13894 N N   . LYS B 665  ? 0.2114 0.1805 0.2180 0.0178  -0.0099 -0.0197 663  LYS B N   
13895 C CA  . LYS B 665  ? 0.2110 0.1801 0.2163 0.0146  -0.0100 -0.0188 663  LYS B CA  
13896 C C   . LYS B 665  ? 0.1908 0.1539 0.1912 0.0131  -0.0117 -0.0184 663  LYS B C   
13897 O O   . LYS B 665  ? 0.2074 0.1658 0.2046 0.0139  -0.0126 -0.0190 663  LYS B O   
13898 C CB  . LYS B 665  ? 0.2124 0.1841 0.2179 0.0131  -0.0085 -0.0190 663  LYS B CB  
13899 C CG  . LYS B 665  ? 0.2379 0.2150 0.2475 0.0143  -0.0067 -0.0192 663  LYS B CG  
13900 C CD  . LYS B 665  ? 0.2465 0.2273 0.2597 0.0141  -0.0065 -0.0186 663  LYS B CD  
13901 C CE  . LYS B 665  ? 0.2663 0.2521 0.2834 0.0149  -0.0048 -0.0187 663  LYS B CE  
13902 N NZ  . LYS B 665  ? 0.2911 0.2800 0.3114 0.0147  -0.0048 -0.0181 663  LYS B NZ  
13903 N N   . SER B 666  ? 0.2280 0.1913 0.2276 0.0108  -0.0123 -0.0173 664  SER B N   
13904 C CA  . SER B 666  ? 0.2271 0.1854 0.2221 0.0085  -0.0136 -0.0166 664  SER B CA  
13905 C C   . SER B 666  ? 0.2271 0.1855 0.2204 0.0061  -0.0129 -0.0166 664  SER B C   
13906 O O   . SER B 666  ? 0.2326 0.1955 0.2284 0.0061  -0.0114 -0.0170 664  SER B O   
13907 C CB  . SER B 666  ? 0.2753 0.2346 0.2701 0.0067  -0.0141 -0.0153 664  SER B CB  
13908 O OG  . SER B 666  ? 0.2830 0.2473 0.2797 0.0050  -0.0125 -0.0150 664  SER B OG  
13909 N N   . ALA B 667  ? 0.2354 0.1888 0.2243 0.0040  -0.0142 -0.0161 665  ALA B N   
13910 C CA  . ALA B 667  ? 0.2284 0.1819 0.2155 0.0014  -0.0139 -0.0160 665  ALA B CA  
13911 C C   . ALA B 667  ? 0.2321 0.1919 0.2219 -0.0006 -0.0124 -0.0153 665  ALA B C   
13912 O O   . ALA B 667  ? 0.2130 0.1760 0.2040 -0.0012 -0.0113 -0.0157 665  ALA B O   
13913 C CB  . ALA B 667  ? 0.2636 0.2107 0.2456 -0.0011 -0.0157 -0.0152 665  ALA B CB  
13914 N N   . LEU B 668  ? 0.2305 0.1923 0.2211 -0.0015 -0.0123 -0.0142 666  LEU B N   
13915 C CA  . LEU B 668  ? 0.2462 0.2139 0.2391 -0.0030 -0.0109 -0.0137 666  LEU B CA  
13916 C C   . LEU B 668  ? 0.2148 0.1873 0.2119 -0.0009 -0.0093 -0.0145 666  LEU B C   
13917 O O   . LEU B 668  ? 0.2195 0.1961 0.2182 -0.0018 -0.0081 -0.0145 666  LEU B O   
13918 C CB  . LEU B 668  ? 0.2724 0.2410 0.2650 -0.0039 -0.0110 -0.0126 666  LEU B CB  
13919 C CG  . LEU B 668  ? 0.3546 0.3206 0.3434 -0.0071 -0.0119 -0.0112 666  LEU B CG  
13920 C CD1 . LEU B 668  ? 0.3807 0.3478 0.3692 -0.0074 -0.0120 -0.0103 666  LEU B CD1 
13921 C CD2 . LEU B 668  ? 0.3628 0.3321 0.3516 -0.0098 -0.0111 -0.0107 666  LEU B CD2 
13922 N N   . ASN B 669  ? 0.2056 0.1779 0.2047 0.0018  -0.0093 -0.0152 667  ASN B N   
13923 C CA  . ASN B 669  ? 0.2015 0.1784 0.2045 0.0035  -0.0078 -0.0158 667  ASN B CA  
13924 C C   . ASN B 669  ? 0.2136 0.1906 0.2167 0.0042  -0.0072 -0.0166 667  ASN B C   
13925 O O   . ASN B 669  ? 0.2206 0.2016 0.2262 0.0046  -0.0058 -0.0168 667  ASN B O   
13926 C CB  . ASN B 669  ? 0.2780 0.2554 0.2835 0.0057  -0.0080 -0.0161 667  ASN B CB  
13927 C CG  . ASN B 669  ? 0.3003 0.2784 0.3057 0.0049  -0.0085 -0.0153 667  ASN B CG  
13928 O OD1 . ASN B 669  ? 0.3955 0.3716 0.4007 0.0059  -0.0097 -0.0152 667  ASN B OD1 
13929 N ND2 . ASN B 669  ? 0.3112 0.2920 0.3166 0.0031  -0.0077 -0.0148 667  ASN B ND2 
13930 N N   . ALA B 670  ? 0.1970 0.1694 0.1971 0.0044  -0.0082 -0.0171 668  ALA B N   
13931 C CA  . ALA B 670  ? 0.1914 0.1634 0.1907 0.0049  -0.0077 -0.0180 668  ALA B CA  
13932 C C   . ALA B 670  ? 0.1897 0.1636 0.1880 0.0022  -0.0074 -0.0175 668  ALA B C   
13933 O O   . ALA B 670  ? 0.1963 0.1729 0.1957 0.0025  -0.0064 -0.0179 668  ALA B O   
13934 C CB  . ALA B 670  ? 0.2051 0.1710 0.2008 0.0059  -0.0091 -0.0188 668  ALA B CB  
13935 N N   . ILE B 671  ? 0.1931 0.1658 0.1894 -0.0005 -0.0082 -0.0166 669  ILE B N   
13936 C CA  . ILE B 671  ? 0.1940 0.1696 0.1900 -0.0031 -0.0079 -0.0159 669  ILE B CA  
13937 C C   . ILE B 671  ? 0.1861 0.1680 0.1861 -0.0025 -0.0062 -0.0157 669  ILE B C   
13938 O O   . ILE B 671  ? 0.1966 0.1817 0.1975 -0.0029 -0.0054 -0.0158 669  ILE B O   
13939 C CB  . ILE B 671  ? 0.1827 0.1567 0.1764 -0.0061 -0.0089 -0.0147 669  ILE B CB  
13940 C CG1 . ILE B 671  ? 0.2138 0.1812 0.2031 -0.0073 -0.0107 -0.0149 669  ILE B CG1 
13941 C CG2 . ILE B 671  ? 0.2228 0.2019 0.2175 -0.0085 -0.0081 -0.0139 669  ILE B CG2 
13942 C CD1 . ILE B 671  ? 0.2503 0.2149 0.2368 -0.0100 -0.0118 -0.0136 669  ILE B CD1 
13943 N N   . ALA B 672  ? 0.1861 0.1698 0.1883 -0.0014 -0.0057 -0.0154 670  ALA B N   
13944 C CA  . ALA B 672  ? 0.1989 0.1878 0.2044 -0.0007 -0.0043 -0.0152 670  ALA B CA  
13945 C C   . ALA B 672  ? 0.1970 0.1875 0.2045 0.0012  -0.0033 -0.0159 670  ALA B C   
13946 O O   . ALA B 672  ? 0.1988 0.1931 0.2081 0.0013  -0.0023 -0.0158 670  ALA B O   
13947 C CB  . ALA B 672  ? 0.2206 0.2101 0.2276 0.0001  -0.0042 -0.0149 670  ALA B CB  
13948 N N   . GLU B 673  ? 0.1866 0.1743 0.1938 0.0030  -0.0037 -0.0167 671  GLU B N   
13949 C CA  . GLU B 673  ? 0.1872 0.1765 0.1961 0.0049  -0.0026 -0.0173 671  GLU B CA  
13950 C C   . GLU B 673  ? 0.1788 0.1688 0.1863 0.0040  -0.0024 -0.0176 671  GLU B C   
13951 O O   . GLU B 673  ? 0.1834 0.1768 0.1926 0.0045  -0.0013 -0.0175 671  GLU B O   
13952 C CB  . GLU B 673  ? 0.2124 0.1984 0.2207 0.0069  -0.0031 -0.0181 671  GLU B CB  
13953 C CG  . GLU B 673  ? 0.2144 0.2024 0.2247 0.0090  -0.0019 -0.0187 671  GLU B CG  
13954 C CD  . GLU B 673  ? 0.2178 0.2094 0.2321 0.0101  -0.0009 -0.0183 671  GLU B CD  
13955 O OE1 . GLU B 673  ? 0.2448 0.2367 0.2603 0.0097  -0.0014 -0.0179 671  GLU B OE1 
13956 O OE2 . GLU B 673  ? 0.1992 0.1933 0.2152 0.0112  0.0003  -0.0185 671  GLU B OE2 
13957 N N   . VAL B 674  ? 0.1651 0.1515 0.1690 0.0026  -0.0036 -0.0178 672  VAL B N   
13958 C CA  . VAL B 674  ? 0.1645 0.1513 0.1668 0.0016  -0.0036 -0.0181 672  VAL B CA  
13959 C C   . VAL B 674  ? 0.1598 0.1511 0.1635 -0.0003 -0.0032 -0.0171 672  VAL B C   
13960 O O   . VAL B 674  ? 0.1632 0.1573 0.1675 -0.0001 -0.0025 -0.0171 672  VAL B O   
13961 C CB  . VAL B 674  ? 0.1820 0.1633 0.1799 0.0003  -0.0052 -0.0186 672  VAL B CB  
13962 C CG1 . VAL B 674  ? 0.1796 0.1612 0.1756 -0.0009 -0.0055 -0.0190 672  VAL B CG1 
13963 C CG2 . VAL B 674  ? 0.2046 0.1816 0.2012 0.0027  -0.0056 -0.0197 672  VAL B CG2 
13964 N N   . ARG B 675  ? 0.1651 0.1573 0.1691 -0.0018 -0.0035 -0.0163 673  ARG B N   
13965 C CA  . ARG B 675  ? 0.1669 0.1639 0.1724 -0.0032 -0.0029 -0.0154 673  ARG B CA  
13966 C C   . ARG B 675  ? 0.1585 0.1595 0.1672 -0.0013 -0.0015 -0.0153 673  ARG B C   
13967 O O   . ARG B 675  ? 0.1565 0.1611 0.1661 -0.0016 -0.0010 -0.0150 673  ARG B O   
13968 C CB  . ARG B 675  ? 0.1665 0.1641 0.1720 -0.0047 -0.0032 -0.0145 673  ARG B CB  
13969 C CG  . ARG B 675  ? 0.1835 0.1780 0.1858 -0.0074 -0.0046 -0.0141 673  ARG B CG  
13970 C CD  . ARG B 675  ? 0.1691 0.1656 0.1717 -0.0089 -0.0044 -0.0130 673  ARG B CD  
13971 N NE  . ARG B 675  ? 0.1714 0.1739 0.1761 -0.0097 -0.0035 -0.0123 673  ARG B NE  
13972 C CZ  . ARG B 675  ? 0.1726 0.1787 0.1785 -0.0101 -0.0028 -0.0115 673  ARG B CZ  
13973 N NH1 . ARG B 675  ? 0.1918 0.1959 0.1968 -0.0101 -0.0029 -0.0112 673  ARG B NH1 
13974 N NH2 . ARG B 675  ? 0.1715 0.1833 0.1794 -0.0105 -0.0019 -0.0110 673  ARG B NH2 
13975 N N   . GLU B 676  ? 0.1521 0.1526 0.1625 0.0007  -0.0009 -0.0156 674  GLU B N   
13976 C CA  . GLU B 676  ? 0.1525 0.1562 0.1658 0.0023  0.0003  -0.0154 674  GLU B CA  
13977 C C   . GLU B 676  ? 0.1498 0.1544 0.1632 0.0032  0.0009  -0.0157 674  GLU B C   
13978 O O   . GLU B 676  ? 0.1454 0.1532 0.1602 0.0036  0.0017  -0.0153 674  GLU B O   
13979 C CB  . GLU B 676  ? 0.1770 0.1797 0.1920 0.0038  0.0006  -0.0156 674  GLU B CB  
13980 C CG  . GLU B 676  ? 0.1882 0.1936 0.2060 0.0052  0.0017  -0.0154 674  GLU B CG  
13981 C CD  . GLU B 676  ? 0.3346 0.3419 0.3534 0.0048  0.0019  -0.0149 674  GLU B CD  
13982 O OE1 . GLU B 676  ? 0.3546 0.3620 0.3720 0.0034  0.0014  -0.0146 674  GLU B OE1 
13983 O OE2 . GLU B 676  ? 0.3204 0.3290 0.3411 0.0059  0.0025  -0.0147 674  GLU B OE2 
13984 N N   . ALA B 677  ? 0.1452 0.1467 0.1566 0.0037  0.0005  -0.0165 675  ALA B N   
13985 C CA  . ALA B 677  ? 0.1515 0.1537 0.1624 0.0045  0.0010  -0.0169 675  ALA B CA  
13986 C C   . ALA B 677  ? 0.1555 0.1597 0.1652 0.0029  0.0006  -0.0165 675  ALA B C   
13987 O O   . ALA B 677  ? 0.1550 0.1619 0.1655 0.0035  0.0013  -0.0162 675  ALA B O   
13988 C CB  . ALA B 677  ? 0.1672 0.1654 0.1757 0.0053  0.0005  -0.0179 675  ALA B CB  
13989 N N   . ILE B 678  ? 0.1414 0.1443 0.1492 0.0007  -0.0006 -0.0164 676  ILE B N   
13990 C CA  . ILE B 678  ? 0.1387 0.1440 0.1456 -0.0012 -0.0012 -0.0160 676  ILE B CA  
13991 C C   . ILE B 678  ? 0.1400 0.1505 0.1499 -0.0009 -0.0003 -0.0150 676  ILE B C   
13992 O O   . ILE B 678  ? 0.1517 0.1652 0.1620 -0.0008 -0.0001 -0.0147 676  ILE B O   
13993 C CB  . ILE B 678  ? 0.1409 0.1441 0.1456 -0.0039 -0.0026 -0.0158 676  ILE B CB  
13994 C CG1 . ILE B 678  ? 0.1616 0.1590 0.1626 -0.0041 -0.0037 -0.0169 676  ILE B CG1 
13995 C CG2 . ILE B 678  ? 0.1600 0.1672 0.1648 -0.0062 -0.0032 -0.0150 676  ILE B CG2 
13996 C CD1 . ILE B 678  ? 0.1621 0.1559 0.1608 -0.0063 -0.0051 -0.0167 676  ILE B CD1 
13997 N N   . ASP B 679  ? 0.1419 0.1533 0.1537 -0.0004 0.0002  -0.0146 677  ASP B N   
13998 C CA  . ASP B 679  ? 0.1410 0.1568 0.1553 0.0001  0.0010  -0.0138 677  ASP B CA  
13999 C C   . ASP B 679  ? 0.1420 0.1591 0.1579 0.0022  0.0020  -0.0137 677  ASP B C   
14000 O O   . ASP B 679  ? 0.1524 0.1730 0.1694 0.0026  0.0024  -0.0131 677  ASP B O   
14001 C CB  . ASP B 679  ? 0.1463 0.1621 0.1617 0.0001  0.0013  -0.0135 677  ASP B CB  
14002 C CG  . ASP B 679  ? 0.1696 0.1852 0.1835 -0.0022 0.0005  -0.0132 677  ASP B CG  
14003 O OD1 . ASP B 679  ? 0.1919 0.2094 0.2050 -0.0040 -0.0001 -0.0128 677  ASP B OD1 
14004 O OD2 . ASP B 679  ? 0.1932 0.2068 0.2068 -0.0024 0.0003  -0.0132 677  ASP B OD2 
14005 N N   . PHE B 680  ? 0.1381 0.1527 0.1542 0.0036  0.0025  -0.0142 678  PHE B N   
14006 C CA  . PHE B 680  ? 0.1339 0.1496 0.1512 0.0053  0.0035  -0.0140 678  PHE B CA  
14007 C C   . PHE B 680  ? 0.1498 0.1669 0.1658 0.0051  0.0033  -0.0139 678  PHE B C   
14008 O O   . PHE B 680  ? 0.1410 0.1606 0.1579 0.0059  0.0038  -0.0132 678  PHE B O   
14009 C CB  . PHE B 680  ? 0.1294 0.1425 0.1470 0.0066  0.0039  -0.0145 678  PHE B CB  
14010 C CG  . PHE B 680  ? 0.1478 0.1604 0.1674 0.0073  0.0043  -0.0144 678  PHE B CG  
14011 C CD1 . PHE B 680  ? 0.1478 0.1623 0.1694 0.0079  0.0049  -0.0138 678  PHE B CD1 
14012 C CD2 . PHE B 680  ? 0.1590 0.1690 0.1785 0.0075  0.0040  -0.0150 678  PHE B CD2 
14013 C CE1 . PHE B 680  ? 0.1564 0.1699 0.1796 0.0085  0.0050  -0.0138 678  PHE B CE1 
14014 C CE2 . PHE B 680  ? 0.1498 0.1594 0.1713 0.0081  0.0042  -0.0149 678  PHE B CE2 
14015 C CZ  . PHE B 680  ? 0.1612 0.1725 0.1844 0.0085  0.0046  -0.0143 678  PHE B CZ  
14016 N N   . LEU B 681  ? 0.1381 0.1531 0.1515 0.0041  0.0025  -0.0145 679  LEU B N   
14017 C CA  . LEU B 681  ? 0.1313 0.1473 0.1429 0.0038  0.0021  -0.0146 679  LEU B CA  
14018 C C   . LEU B 681  ? 0.1382 0.1582 0.1506 0.0028  0.0017  -0.0137 679  LEU B C   
14019 O O   . LEU B 681  ? 0.1454 0.1679 0.1582 0.0036  0.0019  -0.0131 679  LEU B O   
14020 C CB  . LEU B 681  ? 0.1418 0.1543 0.1501 0.0026  0.0010  -0.0156 679  LEU B CB  
14021 C CG  . LEU B 681  ? 0.1415 0.1503 0.1487 0.0041  0.0015  -0.0165 679  LEU B CG  
14022 C CD1 . LEU B 681  ? 0.1507 0.1553 0.1547 0.0030  0.0003  -0.0176 679  LEU B CD1 
14023 C CD2 . LEU B 681  ? 0.1642 0.1739 0.1707 0.0056  0.0024  -0.0166 679  LEU B CD2 
14024 N N   . ARG B 682  ? 0.1435 0.1645 0.1563 0.0012  0.0010  -0.0135 680  ARG B N   
14025 C CA  . ARG B 682  ? 0.1250 0.1506 0.1388 0.0002  0.0005  -0.0127 680  ARG B CA  
14026 C C   . ARG B 682  ? 0.1432 0.1720 0.1598 0.0020  0.0016  -0.0119 680  ARG B C   
14027 O O   . ARG B 682  ? 0.1412 0.1739 0.1587 0.0023  0.0014  -0.0112 680  ARG B O   
14028 C CB  . ARG B 682  ? 0.1354 0.1614 0.1488 -0.0023 -0.0004 -0.0125 680  ARG B CB  
14029 C CG  . ARG B 682  ? 0.1470 0.1697 0.1572 -0.0044 -0.0018 -0.0132 680  ARG B CG  
14030 C CD  . ARG B 682  ? 0.1598 0.1825 0.1696 -0.0070 -0.0026 -0.0129 680  ARG B CD  
14031 N NE  . ARG B 682  ? 0.1674 0.1868 0.1739 -0.0093 -0.0042 -0.0134 680  ARG B NE  
14032 C CZ  . ARG B 682  ? 0.1802 0.1972 0.1851 -0.0117 -0.0052 -0.0133 680  ARG B CZ  
14033 N NH1 . ARG B 682  ? 0.1892 0.2069 0.1955 -0.0121 -0.0046 -0.0127 680  ARG B NH1 
14034 N NH2 . ARG B 682  ? 0.2193 0.2325 0.2207 -0.0138 -0.0068 -0.0139 680  ARG B NH2 
14035 N N   . TYR B 683  ? 0.1349 0.1622 0.1528 0.0033  0.0024  -0.0120 681  TYR B N   
14036 C CA  . TYR B 683  ? 0.1354 0.1649 0.1555 0.0051  0.0033  -0.0114 681  TYR B CA  
14037 C C   . TYR B 683  ? 0.1321 0.1617 0.1524 0.0068  0.0038  -0.0110 681  TYR B C   
14038 O O   . TYR B 683  ? 0.1435 0.1761 0.1648 0.0078  0.0040  -0.0102 681  TYR B O   
14039 C CB  . TYR B 683  ? 0.1347 0.1619 0.1557 0.0057  0.0039  -0.0117 681  TYR B CB  
14040 C CG  . TYR B 683  ? 0.1309 0.1593 0.1537 0.0076  0.0047  -0.0113 681  TYR B CG  
14041 C CD1 . TYR B 683  ? 0.1483 0.1800 0.1721 0.0079  0.0048  -0.0109 681  TYR B CD1 
14042 C CD2 . TYR B 683  ? 0.1337 0.1601 0.1571 0.0091  0.0053  -0.0112 681  TYR B CD2 
14043 C CE1 . TYR B 683  ? 0.1555 0.1878 0.1806 0.0099  0.0054  -0.0107 681  TYR B CE1 
14044 C CE2 . TYR B 683  ? 0.1414 0.1680 0.1660 0.0107  0.0058  -0.0108 681  TYR B CE2 
14045 C CZ  . TYR B 683  ? 0.1401 0.1694 0.1654 0.0112  0.0058  -0.0107 681  TYR B CZ  
14046 O OH  . TYR B 683  ? 0.1761 0.2053 0.2023 0.0131  0.0063  -0.0104 681  TYR B OH  
14047 N N   . TYR B 684  ? 0.1270 0.1536 0.1463 0.0071  0.0041  -0.0114 682  TYR B N   
14048 C CA  . TYR B 684  ? 0.1283 0.1551 0.1475 0.0086  0.0047  -0.0108 682  TYR B CA  
14049 C C   . TYR B 684  ? 0.1445 0.1737 0.1623 0.0082  0.0040  -0.0104 682  TYR B C   
14050 O O   . TYR B 684  ? 0.1458 0.1766 0.1640 0.0094  0.0042  -0.0096 682  TYR B O   
14051 C CB  . TYR B 684  ? 0.1359 0.1595 0.1544 0.0091  0.0054  -0.0113 682  TYR B CB  
14052 C CG  . TYR B 684  ? 0.1337 0.1556 0.1540 0.0096  0.0060  -0.0114 682  TYR B CG  
14053 C CD1 . TYR B 684  ? 0.1449 0.1674 0.1670 0.0104  0.0063  -0.0109 682  TYR B CD1 
14054 C CD2 . TYR B 684  ? 0.1274 0.1467 0.1474 0.0094  0.0061  -0.0122 682  TYR B CD2 
14055 C CE1 . TYR B 684  ? 0.1394 0.1601 0.1629 0.0107  0.0066  -0.0111 682  TYR B CE1 
14056 C CE2 . TYR B 684  ? 0.1287 0.1466 0.1504 0.0098  0.0064  -0.0124 682  TYR B CE2 
14057 C CZ  . TYR B 684  ? 0.1449 0.1635 0.1683 0.0103  0.0066  -0.0118 682  TYR B CZ  
14058 O OH  . TYR B 684  ? 0.1470 0.1641 0.1718 0.0105  0.0067  -0.0120 682  TYR B OH  
14059 N N   . ALA B 685  ? 0.1244 0.1537 0.1406 0.0064  0.0029  -0.0110 683  ALA B N   
14060 C CA  . ALA B 685  ? 0.1324 0.1643 0.1474 0.0057  0.0020  -0.0107 683  ALA B CA  
14061 C C   . ALA B 685  ? 0.1370 0.1735 0.1542 0.0061  0.0018  -0.0097 683  ALA B C   
14062 O O   . ALA B 685  ? 0.1530 0.1918 0.1702 0.0072  0.0016  -0.0089 683  ALA B O   
14063 C CB  . ALA B 685  ? 0.1474 0.1782 0.1602 0.0033  0.0007  -0.0115 683  ALA B CB  
14064 N N   . GLU B 686  ? 0.1387 0.1766 0.1576 0.0056  0.0018  -0.0097 684  GLU B N   
14065 C CA  . GLU B 686  ? 0.1574 0.2001 0.1784 0.0063  0.0018  -0.0088 684  GLU B CA  
14066 C C   . GLU B 686  ? 0.1699 0.2126 0.1922 0.0091  0.0027  -0.0082 684  GLU B C   
14067 O O   . GLU B 686  ? 0.1490 0.1949 0.1719 0.0103  0.0025  -0.0073 684  GLU B O   
14068 C CB  . GLU B 686  ? 0.1909 0.2352 0.2132 0.0053  0.0019  -0.0089 684  GLU B CB  
14069 C CG  . GLU B 686  ? 0.1915 0.2411 0.2162 0.0065  0.0021  -0.0081 684  GLU B CG  
14070 C CD  . GLU B 686  ? 0.2512 0.3060 0.2764 0.0059  0.0011  -0.0074 684  GLU B CD  
14071 O OE1 . GLU B 686  ? 0.2328 0.2872 0.2563 0.0040  0.0000  -0.0075 684  GLU B OE1 
14072 O OE2 . GLU B 686  ? 0.2682 0.3275 0.2954 0.0075  0.0013  -0.0067 684  GLU B OE2 
14073 N N   . GLN B 687  ? 0.1377 0.1766 0.1601 0.0100  0.0037  -0.0085 685  GLN B N   
14074 C CA  . GLN B 687  ? 0.1394 0.1776 0.1627 0.0124  0.0044  -0.0079 685  GLN B CA  
14075 C C   . GLN B 687  ? 0.1481 0.1864 0.1702 0.0132  0.0042  -0.0071 685  GLN B C   
14076 O O   . GLN B 687  ? 0.1679 0.2075 0.1906 0.0150  0.0043  -0.0062 685  GLN B O   
14077 C CB  . GLN B 687  ? 0.1473 0.1815 0.1709 0.0128  0.0052  -0.0083 685  GLN B CB  
14078 C CG  . GLN B 687  ? 0.1656 0.1996 0.1902 0.0124  0.0054  -0.0090 685  GLN B CG  
14079 C CD  . GLN B 687  ? 0.1696 0.2065 0.1955 0.0139  0.0055  -0.0086 685  GLN B CD  
14080 O OE1 . GLN B 687  ? 0.1965 0.2328 0.2228 0.0158  0.0058  -0.0081 685  GLN B OE1 
14081 N NE2 . GLN B 687  ? 0.2226 0.2628 0.2490 0.0129  0.0053  -0.0087 685  GLN B NE2 
14082 N N   . THR B 688  ? 0.1379 0.1747 0.1581 0.0120  0.0040  -0.0075 686  THR B N   
14083 C CA  . THR B 688  ? 0.1498 0.1870 0.1684 0.0126  0.0038  -0.0068 686  THR B CA  
14084 C C   . THR B 688  ? 0.1541 0.1957 0.1729 0.0128  0.0027  -0.0060 686  THR B C   
14085 O O   . THR B 688  ? 0.1585 0.2012 0.1773 0.0145  0.0026  -0.0050 686  THR B O   
14086 C CB  . THR B 688  ? 0.1263 0.1613 0.1424 0.0113  0.0036  -0.0075 686  THR B CB  
14087 O OG1 . THR B 688  ? 0.1594 0.1908 0.1756 0.0116  0.0047  -0.0080 686  THR B OG1 
14088 C CG2 . THR B 688  ? 0.1629 0.1985 0.1768 0.0118  0.0033  -0.0069 686  THR B CG2 
14089 N N   . ARG B 689  ? 0.1411 0.1853 0.1602 0.0111  0.0017  -0.0065 687  ARG B N   
14090 C CA  . ARG B 689  ? 0.1448 0.1940 0.1645 0.0111  0.0006  -0.0058 687  ARG B CA  
14091 C C   . ARG B 689  ? 0.1518 0.2039 0.1740 0.0134  0.0009  -0.0049 687  ARG B C   
14092 O O   . ARG B 689  ? 0.1800 0.2359 0.2027 0.0144  0.0001  -0.0040 687  ARG B O   
14093 C CB  . ARG B 689  ? 0.1733 0.2249 0.1932 0.0084  -0.0005 -0.0064 687  ARG B CB  
14094 C CG  . ARG B 689  ? 0.1906 0.2396 0.2075 0.0063  -0.0013 -0.0072 687  ARG B CG  
14095 C CD  . ARG B 689  ? 0.1929 0.2443 0.2098 0.0035  -0.0026 -0.0076 687  ARG B CD  
14096 N NE  . ARG B 689  ? 0.1936 0.2443 0.2119 0.0025  -0.0020 -0.0080 687  ARG B NE  
14097 C CZ  . ARG B 689  ? 0.2078 0.2542 0.2244 0.0010  -0.0020 -0.0090 687  ARG B CZ  
14098 N NH1 . ARG B 689  ? 0.1962 0.2386 0.2098 0.0003  -0.0024 -0.0098 687  ARG B NH1 
14099 N NH2 . ARG B 689  ? 0.2040 0.2500 0.2218 0.0002  -0.0015 -0.0092 687  ARG B NH2 
14100 N N   . ARG B 690  ? 0.1525 0.2029 0.1761 0.0143  0.0020  -0.0052 688  ARG B N   
14101 C CA  . ARG B 690  ? 0.1404 0.1927 0.1658 0.0168  0.0024  -0.0046 688  ARG B CA  
14102 C C   . ARG B 690  ? 0.1677 0.2173 0.1925 0.0192  0.0028  -0.0037 688  ARG B C   
14103 O O   . ARG B 690  ? 0.1646 0.2157 0.1904 0.0215  0.0028  -0.0030 688  ARG B O   
14104 C CB  . ARG B 690  ? 0.1586 0.2097 0.1853 0.0168  0.0033  -0.0053 688  ARG B CB  
14105 C CG  . ARG B 690  ? 0.1822 0.2365 0.2098 0.0147  0.0030  -0.0059 688  ARG B CG  
14106 C CD  . ARG B 690  ? 0.2153 0.2763 0.2449 0.0155  0.0026  -0.0052 688  ARG B CD  
14107 N NE  . ARG B 690  ? 0.2552 0.3169 0.2862 0.0185  0.0034  -0.0050 688  ARG B NE  
14108 C CZ  . ARG B 690  ? 0.2507 0.3144 0.2823 0.0212  0.0032  -0.0042 688  ARG B CZ  
14109 N NH1 . ARG B 690  ? 0.2273 0.2933 0.2585 0.0212  0.0021  -0.0034 688  ARG B NH1 
14110 N NH2 . ARG B 690  ? 0.2151 0.2783 0.2474 0.0241  0.0039  -0.0042 688  ARG B NH2 
14111 N N   . THR B 691  ? 0.1624 0.2077 0.1853 0.0187  0.0032  -0.0037 689  THR B N   
14112 C CA  . THR B 691  ? 0.1628 0.2048 0.1851 0.0206  0.0038  -0.0029 689  THR B CA  
14113 C C   . THR B 691  ? 0.1853 0.2259 0.2055 0.0206  0.0036  -0.0019 689  THR B C   
14114 O O   . THR B 691  ? 0.2238 0.2638 0.2434 0.0225  0.0035  -0.0007 689  THR B O   
14115 C CB  . THR B 691  ? 0.1661 0.2037 0.1889 0.0204  0.0048  -0.0035 689  THR B CB  
14116 O OG1 . THR B 691  ? 0.1775 0.2134 0.1994 0.0183  0.0051  -0.0043 689  THR B OG1 
14117 C CG2 . THR B 691  ? 0.1878 0.2262 0.2123 0.0209  0.0050  -0.0042 689  THR B CG2 
14118 N N   . LEU B 692  ? 0.1708 0.2103 0.1893 0.0188  0.0037  -0.0025 690  LEU B N   
14119 C CA  . LEU B 692  ? 0.1659 0.2032 0.1823 0.0190  0.0041  -0.0017 690  LEU B CA  
14120 C C   . LEU B 692  ? 0.1837 0.2235 0.1983 0.0196  0.0030  -0.0007 690  LEU B C   
14121 O O   . LEU B 692  ? 0.2168 0.2597 0.2310 0.0185  0.0019  -0.0012 690  LEU B O   
14122 C CB  . LEU B 692  ? 0.1822 0.2172 0.1972 0.0172  0.0047  -0.0027 690  LEU B CB  
14123 C CG  . LEU B 692  ? 0.2040 0.2363 0.2206 0.0168  0.0057  -0.0035 690  LEU B CG  
14124 C CD1 . LEU B 692  ? 0.2335 0.2638 0.2487 0.0156  0.0064  -0.0043 690  LEU B CD1 
14125 C CD2 . LEU B 692  ? 0.2151 0.2451 0.2328 0.0182  0.0065  -0.0025 690  LEU B CD2 
14126 N N   . GLY B 693  ? 0.1876 0.2259 0.2012 0.0211  0.0032  0.0008  691  GLY B N   
14127 C CA  . GLY B 693  ? 0.1996 0.2397 0.2112 0.0219  0.0022  0.0020  691  GLY B CA  
14128 C C   . GLY B 693  ? 0.2262 0.2632 0.2351 0.0220  0.0030  0.0030  691  GLY B C   
14129 O O   . GLY B 693  ? 0.2292 0.2630 0.2379 0.0213  0.0044  0.0027  691  GLY B O   
14130 N N   . PRO B 694  ? 0.2368 0.2748 0.2435 0.0229  0.0022  0.0044  692  PRO B N   
14131 C CA  . PRO B 694  ? 0.2591 0.2946 0.2626 0.0227  0.0030  0.0054  692  PRO B CA  
14132 C C   . PRO B 694  ? 0.2754 0.3069 0.2792 0.0233  0.0044  0.0066  692  PRO B C   
14133 O O   . PRO B 694  ? 0.3090 0.3384 0.3111 0.0224  0.0056  0.0069  692  PRO B O   
14134 C CB  . PRO B 694  ? 0.3190 0.3567 0.3202 0.0238  0.0014  0.0068  692  PRO B CB  
14135 C CG  . PRO B 694  ? 0.3475 0.3885 0.3514 0.0251  0.0000  0.0068  692  PRO B CG  
14136 C CD  . PRO B 694  ? 0.2562 0.2983 0.2631 0.0239  0.0004  0.0050  692  PRO B CD  
14137 N N   . GLY B 695  ? 0.2653 0.2958 0.2712 0.0247  0.0042  0.0072  693  GLY B N   
14138 C CA  . GLY B 695  ? 0.2628 0.2891 0.2689 0.0250  0.0053  0.0083  693  GLY B CA  
14139 C C   . GLY B 695  ? 0.2520 0.2762 0.2600 0.0236  0.0065  0.0071  693  GLY B C   
14140 O O   . GLY B 695  ? 0.3061 0.3269 0.3145 0.0236  0.0073  0.0080  693  GLY B O   
14141 N N   . HIS B 696  ? 0.2437 0.2699 0.2531 0.0225  0.0066  0.0051  694  HIS B N   
14142 C CA  . HIS B 696  ? 0.2040 0.2286 0.2153 0.0212  0.0077  0.0040  694  HIS B CA  
14143 C C   . HIS B 696  ? 0.2068 0.2314 0.2166 0.0198  0.0087  0.0035  694  HIS B C   
14144 O O   . HIS B 696  ? 0.2777 0.3038 0.2875 0.0189  0.0086  0.0019  694  HIS B O   
14145 C CB  . HIS B 696  ? 0.2197 0.2460 0.2333 0.0210  0.0071  0.0022  694  HIS B CB  
14146 C CG  . HIS B 696  ? 0.1827 0.2099 0.1974 0.0227  0.0061  0.0025  694  HIS B CG  
14147 N ND1 . HIS B 696  ? 0.2124 0.2436 0.2276 0.0232  0.0050  0.0021  694  HIS B ND1 
14148 C CD2 . HIS B 696  ? 0.2212 0.2460 0.2366 0.0242  0.0061  0.0033  694  HIS B CD2 
14149 C CE1 . HIS B 696  ? 0.2251 0.2567 0.2414 0.0251  0.0045  0.0025  694  HIS B CE1 
14150 N NE2 . HIS B 696  ? 0.2469 0.2744 0.2632 0.0258  0.0051  0.0032  694  HIS B NE2 
14151 N N   . GLY B 697  ? 0.2409 0.2638 0.2493 0.0197  0.0097  0.0050  695  GLY B N   
14152 C CA  . GLY B 697  ? 0.2269 0.2501 0.2336 0.0187  0.0109  0.0048  695  GLY B CA  
14153 C C   . GLY B 697  ? 0.2043 0.2269 0.2132 0.0176  0.0119  0.0035  695  GLY B C   
14154 O O   . GLY B 697  ? 0.2334 0.2545 0.2449 0.0175  0.0121  0.0035  695  GLY B O   
14155 N N   . PRO B 698  ? 0.2225 0.2462 0.2302 0.0171  0.0126  0.0023  696  PRO B N   
14156 C CA  . PRO B 698  ? 0.2139 0.2371 0.2236 0.0163  0.0136  0.0011  696  PRO B CA  
14157 C C   . PRO B 698  ? 0.2097 0.2320 0.2204 0.0159  0.0152  0.0025  696  PRO B C   
14158 O O   . PRO B 698  ? 0.2178 0.2398 0.2270 0.0160  0.0158  0.0044  696  PRO B O   
14159 C CB  . PRO B 698  ? 0.2982 0.3226 0.3056 0.0162  0.0138  -0.0004 696  PRO B CB  
14160 C CG  . PRO B 698  ? 0.3393 0.3643 0.3431 0.0166  0.0138  0.0007  696  PRO B CG  
14161 C CD  . PRO B 698  ? 0.2852 0.3102 0.2893 0.0172  0.0124  0.0020  696  PRO B CD  
14162 N N   . LEU B 699  ? 0.1816 0.2037 0.1951 0.0153  0.0157  0.0017  697  LEU B N   
14163 C CA  . LEU B 699  ? 0.1793 0.2012 0.1943 0.0146  0.0172  0.0029  697  LEU B CA  
14164 C C   . LEU B 699  ? 0.1793 0.2030 0.1923 0.0147  0.0188  0.0030  697  LEU B C   
14165 O O   . LEU B 699  ? 0.1978 0.2221 0.2105 0.0142  0.0201  0.0048  697  LEU B O   
14166 C CB  . LEU B 699  ? 0.1857 0.2072 0.2043 0.0139  0.0172  0.0019  697  LEU B CB  
14167 C CG  . LEU B 699  ? 0.2168 0.2364 0.2373 0.0139  0.0158  0.0016  697  LEU B CG  
14168 C CD1 . LEU B 699  ? 0.2053 0.2248 0.2288 0.0132  0.0158  0.0005  697  LEU B CD1 
14169 C CD2 . LEU B 699  ? 0.2633 0.2809 0.2837 0.0137  0.0157  0.0036  697  LEU B CD2 
14170 N N   . GLY B 700  ? 0.1763 0.2010 0.1880 0.0152  0.0188  0.0010  698  GLY B N   
14171 C CA  . GLY B 700  ? 0.1893 0.2157 0.1995 0.0155  0.0203  0.0006  698  GLY B CA  
14172 C C   . GLY B 700  ? 0.1752 0.2019 0.1873 0.0157  0.0205  -0.0014 698  GLY B C   
14173 O O   . GLY B 700  ? 0.1763 0.2018 0.1900 0.0155  0.0191  -0.0026 698  GLY B O   
14174 N N   . PRO B 701  ? 0.1824 0.2107 0.1943 0.0162  0.0221  -0.0018 699  PRO B N   
14175 C CA  . PRO B 701  ? 0.1594 0.1879 0.1729 0.0168  0.0222  -0.0038 699  PRO B CA  
14176 C C   . PRO B 701  ? 0.1616 0.1896 0.1795 0.0160  0.0215  -0.0037 699  PRO B C   
14177 O O   . PRO B 701  ? 0.1735 0.2024 0.1941 0.0151  0.0221  -0.0021 699  PRO B O   
14178 C CB  . PRO B 701  ? 0.1788 0.2098 0.1920 0.0176  0.0244  -0.0036 699  PRO B CB  
14179 C CG  . PRO B 701  ? 0.1835 0.2151 0.1929 0.0177  0.0252  -0.0022 699  PRO B CG  
14180 C CD  . PRO B 701  ? 0.1863 0.2166 0.1966 0.0165  0.0241  -0.0004 699  PRO B CD  
14181 N N   . ILE B 702  ? 0.1583 0.1848 0.1766 0.0161  0.0201  -0.0055 700  ILE B N   
14182 C CA  A ILE B 702  ? 0.1542 0.1801 0.1763 0.0154  0.0193  -0.0057 700  ILE B CA  
14183 C CA  B ILE B 702  ? 0.1543 0.1802 0.1763 0.0154  0.0192  -0.0057 700  ILE B CA  
14184 C C   . ILE B 702  ? 0.1693 0.1956 0.1925 0.0162  0.0195  -0.0072 700  ILE B C   
14185 O O   . ILE B 702  ? 0.1633 0.1886 0.1840 0.0171  0.0191  -0.0089 700  ILE B O   
14186 C CB  A ILE B 702  ? 0.1356 0.1594 0.1573 0.0149  0.0174  -0.0062 700  ILE B CB  
14187 C CB  B ILE B 702  ? 0.1366 0.1603 0.1581 0.0149  0.0173  -0.0063 700  ILE B CB  
14188 C CG1 A ILE B 702  ? 0.1543 0.1777 0.1759 0.0144  0.0171  -0.0044 700  ILE B CG1 
14189 C CG1 B ILE B 702  ? 0.1560 0.1793 0.1763 0.0146  0.0170  -0.0048 700  ILE B CG1 
14190 C CG2 A ILE B 702  ? 0.1483 0.1712 0.1730 0.0145  0.0165  -0.0070 700  ILE B CG2 
14191 C CG2 B ILE B 702  ? 0.1508 0.1737 0.1757 0.0144  0.0165  -0.0066 700  ILE B CG2 
14192 C CD1 A ILE B 702  ? 0.1561 0.1781 0.1775 0.0142  0.0155  -0.0048 700  ILE B CD1 
14193 C CD1 B ILE B 702  ? 0.1622 0.1856 0.1847 0.0139  0.0175  -0.0029 700  ILE B CD1 
14194 N N   . VAL B 703  ? 0.1442 0.1719 0.1712 0.0159  0.0200  -0.0067 701  VAL B N   
14195 C CA  . VAL B 703  ? 0.1519 0.1803 0.1806 0.0167  0.0201  -0.0080 701  VAL B CA  
14196 C C   . VAL B 703  ? 0.1372 0.1633 0.1673 0.0161  0.0182  -0.0089 701  VAL B C   
14197 O O   . VAL B 703  ? 0.1456 0.1714 0.1779 0.0149  0.0176  -0.0079 701  VAL B O   
14198 C CB  . VAL B 703  ? 0.1437 0.1754 0.1760 0.0165  0.0216  -0.0068 701  VAL B CB  
14199 C CG1 . VAL B 703  ? 0.1604 0.1930 0.1953 0.0174  0.0213  -0.0081 701  VAL B CG1 
14200 C CG2 . VAL B 703  ? 0.1693 0.2036 0.1999 0.0173  0.0236  -0.0061 701  VAL B CG2 
14201 N N   . CYS B 704  ? 0.1376 0.1619 0.1660 0.0169  0.0173  -0.0106 702  CYS B N   
14202 C CA  . CYS B 704  ? 0.1435 0.1656 0.1727 0.0163  0.0155  -0.0114 702  CYS B CA  
14203 C C   . CYS B 704  ? 0.1586 0.1811 0.1897 0.0172  0.0154  -0.0123 702  CYS B C   
14204 O O   . CYS B 704  ? 0.1434 0.1656 0.1728 0.0186  0.0157  -0.0135 702  CYS B O   
14205 C CB  . CYS B 704  ? 0.1429 0.1626 0.1686 0.0162  0.0143  -0.0125 702  CYS B CB  
14206 S SG  . CYS B 704  ? 0.1531 0.1727 0.1766 0.0153  0.0142  -0.0115 702  CYS B SG  
14207 N N   . ILE B 705  ? 0.1270 0.1502 0.1616 0.0165  0.0149  -0.0118 703  ILE B N   
14208 C CA  . ILE B 705  ? 0.1446 0.1687 0.1816 0.0173  0.0147  -0.0124 703  ILE B CA  
14209 C C   . ILE B 705  ? 0.1354 0.1569 0.1726 0.0167  0.0127  -0.0130 703  ILE B C   
14210 O O   . ILE B 705  ? 0.1426 0.1632 0.1804 0.0153  0.0120  -0.0124 703  ILE B O   
14211 C CB  . ILE B 705  ? 0.1469 0.1746 0.1881 0.0169  0.0156  -0.0111 703  ILE B CB  
14212 C CG1 . ILE B 705  ? 0.1633 0.1941 0.2043 0.0177  0.0178  -0.0104 703  ILE B CG1 
14213 C CG2 . ILE B 705  ? 0.1495 0.1782 0.1937 0.0174  0.0149  -0.0115 703  ILE B CG2 
14214 C CD1 . ILE B 705  ? 0.1663 0.2006 0.2109 0.0166  0.0189  -0.0086 703  ILE B CD1 
14215 N N   . SER B 706  ? 0.1449 0.1647 0.1809 0.0177  0.0119  -0.0143 704  SER B N   
14216 C CA  . SER B 706  ? 0.1593 0.1760 0.1943 0.0170  0.0101  -0.0150 704  SER B CA  
14217 C C   . SER B 706  ? 0.1559 0.1726 0.1928 0.0179  0.0092  -0.0155 704  SER B C   
14218 O O   . SER B 706  ? 0.1606 0.1791 0.1989 0.0194  0.0099  -0.0157 704  SER B O   
14219 C CB  . SER B 706  ? 0.1606 0.1744 0.1913 0.0171  0.0096  -0.0159 704  SER B CB  
14220 O OG  . SER B 706  ? 0.1496 0.1629 0.1786 0.0188  0.0101  -0.0169 704  SER B OG  
14221 N N   . PRO B 707  ? 0.1486 0.1632 0.1855 0.0170  0.0077  -0.0156 705  PRO B N   
14222 C CA  . PRO B 707  ? 0.1573 0.1716 0.1958 0.0177  0.0065  -0.0160 705  PRO B CA  
14223 C C   . PRO B 707  ? 0.1657 0.1768 0.2012 0.0188  0.0056  -0.0171 705  PRO B C   
14224 O O   . PRO B 707  ? 0.1719 0.1805 0.2039 0.0185  0.0055  -0.0176 705  PRO B O   
14225 C CB  . PRO B 707  ? 0.1776 0.1909 0.2167 0.0160  0.0053  -0.0156 705  PRO B CB  
14226 C CG  . PRO B 707  ? 0.1589 0.1702 0.1949 0.0150  0.0053  -0.0156 705  PRO B CG  
14227 C CD  . PRO B 707  ? 0.1603 0.1732 0.1958 0.0153  0.0069  -0.0153 705  PRO B CD  
14228 N N   . TRP B 708  ? 0.1441 0.1550 0.1808 0.0200  0.0047  -0.0175 706  TRP B N   
14229 C CA  . TRP B 708  ? 0.1594 0.1666 0.1930 0.0212  0.0037  -0.0185 706  TRP B CA  
14230 C C   . TRP B 708  ? 0.1631 0.1664 0.1939 0.0197  0.0021  -0.0186 706  TRP B C   
14231 O O   . TRP B 708  ? 0.1676 0.1671 0.1948 0.0199  0.0013  -0.0193 706  TRP B O   
14232 C CB  . TRP B 708  ? 0.1636 0.1718 0.1994 0.0234  0.0032  -0.0189 706  TRP B CB  
14233 C CG  . TRP B 708  ? 0.1605 0.1687 0.1982 0.0227  0.0016  -0.0184 706  TRP B CG  
14234 C CD1 . TRP B 708  ? 0.1873 0.1992 0.2292 0.0221  0.0016  -0.0176 706  TRP B CD1 
14235 C CD2 . TRP B 708  ? 0.1693 0.1732 0.2044 0.0223  -0.0004 -0.0187 706  TRP B CD2 
14236 N NE1 . TRP B 708  ? 0.1861 0.1964 0.2281 0.0215  -0.0003 -0.0175 706  TRP B NE1 
14237 C CE2 . TRP B 708  ? 0.1596 0.1650 0.1974 0.0216  -0.0015 -0.0181 706  TRP B CE2 
14238 C CE3 . TRP B 708  ? 0.1798 0.1787 0.2104 0.0223  -0.0013 -0.0193 706  TRP B CE3 
14239 C CZ2 . TRP B 708  ? 0.1725 0.1748 0.2086 0.0211  -0.0034 -0.0181 706  TRP B CZ2 
14240 C CZ3 . TRP B 708  ? 0.1879 0.1837 0.2169 0.0216  -0.0032 -0.0191 706  TRP B CZ3 
14241 C CH2 . TRP B 708  ? 0.1770 0.1745 0.2086 0.0211  -0.0042 -0.0185 706  TRP B CH2 
14242 N N   . ASN B 709  ? 0.1540 0.1580 0.1863 0.0181  0.0015  -0.0179 707  ASN B N   
14243 C CA  . ASN B 709  ? 0.1648 0.1656 0.1950 0.0170  -0.0002 -0.0179 707  ASN B CA  
14244 C C   . ASN B 709  ? 0.1868 0.1853 0.2135 0.0154  -0.0003 -0.0180 707  ASN B C   
14245 O O   . ASN B 709  ? 0.1889 0.1842 0.2129 0.0147  -0.0015 -0.0181 707  ASN B O   
14246 C CB  . ASN B 709  ? 0.1660 0.1683 0.1987 0.0161  -0.0009 -0.0173 707  ASN B CB  
14247 C CG  . ASN B 709  ? 0.1674 0.1713 0.2008 0.0146  0.0000  -0.0168 707  ASN B CG  
14248 O OD1 . ASN B 709  ? 0.2013 0.2078 0.2366 0.0147  0.0013  -0.0165 707  ASN B OD1 
14249 N ND2 . ASN B 709  ? 0.1962 0.1985 0.2278 0.0132  -0.0007 -0.0166 707  ASN B ND2 
14250 N N   . PHE B 710  ? 0.1693 0.1696 0.1960 0.0148  0.0010  -0.0178 708  PHE B N   
14251 C CA  . PHE B 710  ? 0.1671 0.1658 0.1906 0.0134  0.0010  -0.0178 708  PHE B CA  
14252 C C   . PHE B 710  ? 0.1757 0.1747 0.1982 0.0144  0.0020  -0.0183 708  PHE B C   
14253 O O   . PHE B 710  ? 0.1768 0.1781 0.1998 0.0141  0.0032  -0.0180 708  PHE B O   
14254 C CB  . PHE B 710  ? 0.1736 0.1743 0.1979 0.0120  0.0015  -0.0171 708  PHE B CB  
14255 C CG  . PHE B 710  ? 0.1865 0.1869 0.2115 0.0112  0.0006  -0.0168 708  PHE B CG  
14256 C CD1 . PHE B 710  ? 0.2114 0.2091 0.2345 0.0108  -0.0007 -0.0169 708  PHE B CD1 
14257 C CD2 . PHE B 710  ? 0.2142 0.2168 0.2414 0.0108  0.0011  -0.0163 708  PHE B CD2 
14258 C CE1 . PHE B 710  ? 0.2153 0.2128 0.2387 0.0100  -0.0015 -0.0166 708  PHE B CE1 
14259 C CE2 . PHE B 710  ? 0.2251 0.2271 0.2524 0.0102  0.0003  -0.0161 708  PHE B CE2 
14260 C CZ  . PHE B 710  ? 0.2503 0.2499 0.2756 0.0098  -0.0010 -0.0163 708  PHE B CZ  
14261 N N   . PRO B 711  ? 0.1866 0.1831 0.2072 0.0157  0.0015  -0.0191 709  PRO B N   
14262 C CA  . PRO B 711  ? 0.1796 0.1767 0.1996 0.0172  0.0026  -0.0198 709  PRO B CA  
14263 C C   . PRO B 711  ? 0.1801 0.1762 0.1969 0.0163  0.0029  -0.0200 709  PRO B C   
14264 O O   . PRO B 711  ? 0.1770 0.1740 0.1932 0.0174  0.0040  -0.0205 709  PRO B O   
14265 C CB  . PRO B 711  ? 0.1829 0.1768 0.2014 0.0191  0.0018  -0.0207 709  PRO B CB  
14266 C CG  . PRO B 711  ? 0.1842 0.1743 0.2004 0.0176  0.0000  -0.0206 709  PRO B CG  
14267 C CD  . PRO B 711  ? 0.1758 0.1685 0.1946 0.0160  0.0000  -0.0195 709  PRO B CD  
14268 N N   . LEU B 712  ? 0.1595 0.1538 0.1742 0.0142  0.0019  -0.0198 710  LEU B N   
14269 C CA  . LEU B 712  ? 0.1658 0.1600 0.1781 0.0130  0.0021  -0.0199 710  LEU B CA  
14270 C C   . LEU B 712  ? 0.1666 0.1641 0.1806 0.0115  0.0026  -0.0188 710  LEU B C   
14271 O O   . LEU B 712  ? 0.1652 0.1647 0.1790 0.0113  0.0034  -0.0186 710  LEU B O   
14272 C CB  . LEU B 712  ? 0.1751 0.1649 0.1833 0.0117  0.0005  -0.0204 710  LEU B CB  
14273 C CG  . LEU B 712  ? 0.1509 0.1407 0.1565 0.0102  0.0004  -0.0206 710  LEU B CG  
14274 C CD1 . LEU B 712  ? 0.1786 0.1685 0.1829 0.0119  0.0013  -0.0214 710  LEU B CD1 
14275 C CD2 . LEU B 712  ? 0.2149 0.2004 0.2168 0.0083  -0.0014 -0.0209 710  LEU B CD2 
14276 N N   . ALA B 713  ? 0.1581 0.1562 0.1737 0.0106  0.0021  -0.0182 711  ALA B N   
14277 C CA  . ALA B 713  ? 0.1707 0.1715 0.1874 0.0093  0.0024  -0.0173 711  ALA B CA  
14278 C C   . ALA B 713  ? 0.1588 0.1628 0.1782 0.0102  0.0038  -0.0168 711  ALA B C   
14279 O O   . ALA B 713  ? 0.1672 0.1731 0.1864 0.0099  0.0044  -0.0164 711  ALA B O   
14280 C CB  . ALA B 713  ? 0.1821 0.1825 0.1993 0.0083  0.0016  -0.0169 711  ALA B CB  
14281 N N   . ILE B 714  ? 0.1678 0.1725 0.1898 0.0112  0.0042  -0.0166 712  ILE B N   
14282 C CA  . ILE B 714  ? 0.1596 0.1671 0.1841 0.0118  0.0054  -0.0159 712  ILE B CA  
14283 C C   . ILE B 714  ? 0.1717 0.1800 0.1955 0.0127  0.0064  -0.0161 712  ILE B C   
14284 O O   . ILE B 714  ? 0.1570 0.1672 0.1812 0.0126  0.0073  -0.0154 712  ILE B O   
14285 C CB  . ILE B 714  ? 0.1590 0.1671 0.1865 0.0123  0.0054  -0.0157 712  ILE B CB  
14286 C CG1 . ILE B 714  ? 0.1967 0.2041 0.2244 0.0112  0.0045  -0.0155 712  ILE B CG1 
14287 C CG2 . ILE B 714  ? 0.1671 0.1777 0.1970 0.0127  0.0066  -0.0149 712  ILE B CG2 
14288 C CD1 . ILE B 714  ? 0.2865 0.2945 0.3169 0.0114  0.0043  -0.0152 712  ILE B CD1 
14289 N N   . PHE B 715  ? 0.1478 0.1546 0.1703 0.0137  0.0063  -0.0169 713  PHE B N   
14290 C CA  . PHE B 715  ? 0.1519 0.1593 0.1731 0.0147  0.0073  -0.0173 713  PHE B CA  
14291 C C   . PHE B 715  ? 0.1523 0.1599 0.1710 0.0137  0.0073  -0.0171 713  PHE B C   
14292 O O   . PHE B 715  ? 0.1505 0.1602 0.1694 0.0140  0.0084  -0.0165 713  PHE B O   
14293 C CB  . PHE B 715  ? 0.1555 0.1601 0.1745 0.0159  0.0068  -0.0185 713  PHE B CB  
14294 C CG  . PHE B 715  ? 0.1395 0.1442 0.1564 0.0172  0.0078  -0.0192 713  PHE B CG  
14295 C CD1 . PHE B 715  ? 0.1442 0.1516 0.1631 0.0188  0.0094  -0.0189 713  PHE B CD1 
14296 C CD2 . PHE B 715  ? 0.1648 0.1670 0.1776 0.0167  0.0071  -0.0199 713  PHE B CD2 
14297 C CE1 . PHE B 715  ? 0.1699 0.1775 0.1865 0.0201  0.0104  -0.0195 713  PHE B CE1 
14298 C CE2 . PHE B 715  ? 0.1718 0.1739 0.1822 0.0179  0.0080  -0.0207 713  PHE B CE2 
14299 C CZ  . PHE B 715  ? 0.1593 0.1640 0.1714 0.0197  0.0097  -0.0205 713  PHE B CZ  
14300 N N   . THR B 716  ? 0.1445 0.1501 0.1609 0.0124  0.0060  -0.0175 714  THR B N   
14301 C CA  . THR B 716  ? 0.1557 0.1618 0.1700 0.0114  0.0057  -0.0173 714  THR B CA  
14302 C C   . THR B 716  ? 0.1573 0.1664 0.1735 0.0108  0.0062  -0.0161 714  THR B C   
14303 O O   . THR B 716  ? 0.1516 0.1622 0.1670 0.0108  0.0066  -0.0157 714  THR B O   
14304 C CB  . THR B 716  ? 0.1549 0.1584 0.1666 0.0098  0.0042  -0.0179 714  THR B CB  
14305 O OG1 . THR B 716  ? 0.1736 0.1736 0.1829 0.0105  0.0036  -0.0190 714  THR B OG1 
14306 C CG2 . THR B 716  ? 0.1744 0.1791 0.1844 0.0084  0.0037  -0.0176 714  THR B CG2 
14307 N N   . GLY B 717  ? 0.1451 0.1547 0.1636 0.0105  0.0060  -0.0156 715  GLY B N   
14308 C CA  . GLY B 717  ? 0.1508 0.1628 0.1709 0.0102  0.0064  -0.0146 715  GLY B CA  
14309 C C   . GLY B 717  ? 0.1438 0.1575 0.1651 0.0112  0.0076  -0.0138 715  GLY B C   
14310 O O   . GLY B 717  ? 0.1522 0.1674 0.1730 0.0111  0.0078  -0.0132 715  GLY B O   
14311 N N   . GLN B 718  ? 0.1334 0.1469 0.1562 0.0120  0.0083  -0.0138 716  GLN B N   
14312 C CA  . GLN B 718  ? 0.1375 0.1527 0.1615 0.0126  0.0096  -0.0128 716  GLN B CA  
14313 C C   . GLN B 718  ? 0.1457 0.1615 0.1673 0.0130  0.0101  -0.0128 716  GLN B C   
14314 O O   . GLN B 718  ? 0.1404 0.1575 0.1616 0.0130  0.0106  -0.0119 716  GLN B O   
14315 C CB  . GLN B 718  ? 0.1272 0.1428 0.1535 0.0133  0.0103  -0.0128 716  GLN B CB  
14316 C CG  . GLN B 718  ? 0.1334 0.1484 0.1622 0.0128  0.0096  -0.0128 716  GLN B CG  
14317 C CD  . GLN B 718  ? 0.1451 0.1610 0.1766 0.0133  0.0102  -0.0125 716  GLN B CD  
14318 O OE1 . GLN B 718  ? 0.1619 0.1783 0.1957 0.0128  0.0102  -0.0118 716  GLN B OE1 
14319 N NE2 . GLN B 718  ? 0.1611 0.1776 0.1924 0.0142  0.0108  -0.0130 716  GLN B NE2 
14320 N N   . ILE B 719  ? 0.1367 0.1512 0.1561 0.0133  0.0099  -0.0140 717  ILE B N   
14321 C CA  . ILE B 719  ? 0.1444 0.1591 0.1609 0.0138  0.0103  -0.0142 717  ILE B CA  
14322 C C   . ILE B 719  ? 0.1427 0.1578 0.1573 0.0128  0.0095  -0.0139 717  ILE B C   
14323 O O   . ILE B 719  ? 0.1493 0.1657 0.1627 0.0131  0.0099  -0.0132 717  ILE B O   
14324 C CB  . ILE B 719  ? 0.1638 0.1763 0.1780 0.0144  0.0101  -0.0157 717  ILE B CB  
14325 C CG1 . ILE B 719  ? 0.1587 0.1716 0.1749 0.0158  0.0112  -0.0159 717  ILE B CG1 
14326 C CG2 . ILE B 719  ? 0.2149 0.2269 0.2253 0.0146  0.0101  -0.0163 717  ILE B CG2 
14327 C CD1 . ILE B 719  ? 0.2490 0.2593 0.2634 0.0166  0.0106  -0.0175 717  ILE B CD1 
14328 N N   . ALA B 720  ? 0.1396 0.1539 0.1541 0.0117  0.0081  -0.0143 718  ALA B N   
14329 C CA  . ALA B 720  ? 0.1450 0.1604 0.1580 0.0107  0.0072  -0.0140 718  ALA B CA  
14330 C C   . ALA B 720  ? 0.1449 0.1628 0.1597 0.0110  0.0077  -0.0126 718  ALA B C   
14331 O O   . ALA B 720  ? 0.1460 0.1653 0.1593 0.0110  0.0075  -0.0121 718  ALA B O   
14332 C CB  . ALA B 720  ? 0.1630 0.1777 0.1762 0.0093  0.0059  -0.0145 718  ALA B CB  
14333 N N   . ALA B 721  ? 0.1375 0.1556 0.1550 0.0114  0.0082  -0.0120 719  ALA B N   
14334 C CA  . ALA B 721  ? 0.1486 0.1683 0.1674 0.0119  0.0085  -0.0107 719  ALA B CA  
14335 C C   . ALA B 721  ? 0.1358 0.1561 0.1539 0.0126  0.0095  -0.0099 719  ALA B C   
14336 O O   . ALA B 721  ? 0.1447 0.1663 0.1620 0.0129  0.0094  -0.0089 719  ALA B O   
14337 C CB  . ALA B 721  ? 0.1561 0.1752 0.1777 0.0120  0.0087  -0.0104 719  ALA B CB  
14338 N N   . ALA B 722  ? 0.1341 0.1536 0.1524 0.0131  0.0105  -0.0101 720  ALA B N   
14339 C CA  . ALA B 722  ? 0.1248 0.1452 0.1423 0.0137  0.0117  -0.0091 720  ALA B CA  
14340 C C   . ALA B 722  ? 0.1488 0.1696 0.1629 0.0138  0.0114  -0.0093 720  ALA B C   
14341 O O   . ALA B 722  ? 0.1509 0.1727 0.1639 0.0141  0.0116  -0.0082 720  ALA B O   
14342 C CB  . ALA B 722  ? 0.1359 0.1561 0.1544 0.0141  0.0129  -0.0094 720  ALA B CB  
14343 N N   . LEU B 723  ? 0.1440 0.1638 0.1561 0.0134  0.0106  -0.0108 721  LEU B N   
14344 C CA  . LEU B 723  ? 0.1532 0.1731 0.1616 0.0133  0.0101  -0.0112 721  LEU B CA  
14345 C C   . LEU B 723  ? 0.1623 0.1838 0.1704 0.0128  0.0089  -0.0104 721  LEU B C   
14346 O O   . LEU B 723  ? 0.1542 0.1768 0.1603 0.0130  0.0089  -0.0097 721  LEU B O   
14347 C CB  . LEU B 723  ? 0.1514 0.1693 0.1578 0.0128  0.0091  -0.0130 721  LEU B CB  
14348 C CG  . LEU B 723  ? 0.1580 0.1742 0.1635 0.0138  0.0101  -0.0141 721  LEU B CG  
14349 C CD1 . LEU B 723  ? 0.1665 0.1799 0.1702 0.0132  0.0089  -0.0158 721  LEU B CD1 
14350 C CD2 . LEU B 723  ? 0.1801 0.1968 0.1828 0.0148  0.0112  -0.0140 721  LEU B CD2 
14351 N N   . VAL B 724  ? 0.1469 0.1688 0.1570 0.0120  0.0080  -0.0105 722  VAL B N   
14352 C CA  . VAL B 724  ? 0.1370 0.1611 0.1469 0.0116  0.0068  -0.0098 722  VAL B CA  
14353 C C   . VAL B 724  ? 0.1537 0.1792 0.1648 0.0127  0.0074  -0.0082 722  VAL B C   
14354 O O   . VAL B 724  ? 0.1646 0.1920 0.1748 0.0129  0.0067  -0.0074 722  VAL B O   
14355 C CB  . VAL B 724  ? 0.1304 0.1551 0.1419 0.0105  0.0058  -0.0103 722  VAL B CB  
14356 C CG1 . VAL B 724  ? 0.1608 0.1858 0.1755 0.0111  0.0063  -0.0097 722  VAL B CG1 
14357 C CG2 . VAL B 724  ? 0.1533 0.1805 0.1639 0.0096  0.0044  -0.0101 722  VAL B CG2 
14358 N N   . ALA B 725  ? 0.1642 0.1888 0.1772 0.0134  0.0086  -0.0075 723  ALA B N   
14359 C CA  . ALA B 725  ? 0.1585 0.1835 0.1720 0.0143  0.0091  -0.0059 723  ALA B CA  
14360 C C   . ALA B 725  ? 0.1823 0.2074 0.1932 0.0148  0.0098  -0.0051 723  ALA B C   
14361 O O   . ALA B 725  ? 0.1958 0.2210 0.2066 0.0155  0.0102  -0.0036 723  ALA B O   
14362 C CB  . ALA B 725  ? 0.1577 0.1812 0.1739 0.0146  0.0100  -0.0055 723  ALA B CB  
14363 N N   . GLY B 726  ? 0.1549 0.1797 0.1634 0.0144  0.0099  -0.0062 724  GLY B N   
14364 C CA  . GLY B 726  ? 0.1654 0.1904 0.1708 0.0149  0.0105  -0.0057 724  GLY B CA  
14365 C C   . GLY B 726  ? 0.1827 0.2070 0.1880 0.0153  0.0123  -0.0055 724  GLY B C   
14366 O O   . GLY B 726  ? 0.1907 0.2154 0.1935 0.0158  0.0131  -0.0046 724  GLY B O   
14367 N N   . ASN B 727  ? 0.1544 0.1778 0.1620 0.0152  0.0130  -0.0063 725  ASN B N   
14368 C CA  . ASN B 727  ? 0.1612 0.1846 0.1694 0.0156  0.0147  -0.0061 725  ASN B CA  
14369 C C   . ASN B 727  ? 0.1573 0.1801 0.1639 0.0159  0.0150  -0.0080 725  ASN B C   
14370 O O   . ASN B 727  ? 0.1729 0.1944 0.1799 0.0155  0.0139  -0.0094 725  ASN B O   
14371 C CB  . ASN B 727  ? 0.1663 0.1894 0.1786 0.0153  0.0152  -0.0056 725  ASN B CB  
14372 C CG  . ASN B 727  ? 0.1876 0.2107 0.2015 0.0151  0.0147  -0.0040 725  ASN B CG  
14373 O OD1 . ASN B 727  ? 0.1748 0.1981 0.1884 0.0152  0.0155  -0.0023 725  ASN B OD1 
14374 N ND2 . ASN B 727  ? 0.1527 0.1752 0.1679 0.0148  0.0134  -0.0045 725  ASN B ND2 
14375 N N   . PRO B 728  ? 0.1467 0.1700 0.1513 0.0167  0.0164  -0.0080 726  PRO B N   
14376 C CA  . PRO B 728  ? 0.1658 0.1882 0.1693 0.0174  0.0169  -0.0099 726  PRO B CA  
14377 C C   . PRO B 728  ? 0.1794 0.2021 0.1870 0.0175  0.0176  -0.0100 726  PRO B C   
14378 O O   . PRO B 728  ? 0.1722 0.1962 0.1829 0.0171  0.0183  -0.0084 726  PRO B O   
14379 C CB  . PRO B 728  ? 0.1844 0.2079 0.1849 0.0185  0.0186  -0.0096 726  PRO B CB  
14380 C CG  . PRO B 728  ? 0.1985 0.2239 0.2007 0.0181  0.0196  -0.0071 726  PRO B CG  
14381 C CD  . PRO B 728  ? 0.1679 0.1927 0.1716 0.0170  0.0179  -0.0062 726  PRO B CD  
14382 N N   . VAL B 729  ? 0.1478 0.1691 0.1552 0.0180  0.0171  -0.0118 727  VAL B N   
14383 C CA  . VAL B 729  ? 0.1451 0.1664 0.1563 0.0181  0.0172  -0.0121 727  VAL B CA  
14384 C C   . VAL B 729  ? 0.1663 0.1880 0.1773 0.0196  0.0185  -0.0131 727  VAL B C   
14385 O O   . VAL B 729  ? 0.1622 0.1823 0.1696 0.0206  0.0184  -0.0147 727  VAL B O   
14386 C CB  . VAL B 729  ? 0.1492 0.1682 0.1608 0.0172  0.0153  -0.0131 727  VAL B CB  
14387 C CG1 . VAL B 729  ? 0.1601 0.1786 0.1746 0.0175  0.0152  -0.0137 727  VAL B CG1 
14388 C CG2 . VAL B 729  ? 0.1704 0.1898 0.1832 0.0159  0.0143  -0.0119 727  VAL B CG2 
14389 N N   . LEU B 730  ? 0.1443 0.1680 0.1593 0.0198  0.0195  -0.0124 728  LEU B N   
14390 C CA  . LEU B 730  ? 0.1436 0.1683 0.1597 0.0214  0.0205  -0.0134 728  LEU B CA  
14391 C C   . LEU B 730  ? 0.1402 0.1634 0.1591 0.0210  0.0191  -0.0140 728  LEU B C   
14392 O O   . LEU B 730  ? 0.1613 0.1856 0.1838 0.0199  0.0188  -0.0128 728  LEU B O   
14393 C CB  . LEU B 730  ? 0.1571 0.1858 0.1761 0.0217  0.0226  -0.0119 728  LEU B CB  
14394 C CG  . LEU B 730  ? 0.1741 0.2048 0.1906 0.0220  0.0244  -0.0108 728  LEU B CG  
14395 C CD1 . LEU B 730  ? 0.1863 0.2151 0.1974 0.0235  0.0244  -0.0126 728  LEU B CD1 
14396 C CD2 . LEU B 730  ? 0.1771 0.2076 0.1934 0.0203  0.0240  -0.0089 728  LEU B CD2 
14397 N N   . ALA B 731  ? 0.1500 0.1704 0.1669 0.0218  0.0180  -0.0158 729  ALA B N   
14398 C CA  . ALA B 731  ? 0.1474 0.1659 0.1661 0.0214  0.0164  -0.0164 729  ALA B CA  
14399 C C   . ALA B 731  ? 0.1630 0.1826 0.1840 0.0231  0.0170  -0.0170 729  ALA B C   
14400 O O   . ALA B 731  ? 0.1491 0.1678 0.1678 0.0250  0.0175  -0.0184 729  ALA B O   
14401 C CB  . ALA B 731  ? 0.1833 0.1976 0.1982 0.0209  0.0146  -0.0178 729  ALA B CB  
14402 N N   . LYS B 732  ? 0.1491 0.1708 0.1746 0.0225  0.0170  -0.0160 730  LYS B N   
14403 C CA  . LYS B 732  ? 0.1456 0.1693 0.1742 0.0240  0.0174  -0.0164 730  LYS B CA  
14404 C C   . LYS B 732  ? 0.1365 0.1576 0.1662 0.0235  0.0154  -0.0169 730  LYS B C   
14405 O O   . LYS B 732  ? 0.1515 0.1735 0.1842 0.0220  0.0148  -0.0159 730  LYS B O   
14406 C CB  . LYS B 732  ? 0.1436 0.1721 0.1765 0.0235  0.0190  -0.0146 730  LYS B CB  
14407 C CG  . LYS B 732  ? 0.1541 0.1864 0.1895 0.0256  0.0204  -0.0148 730  LYS B CG  
14408 C CD  . LYS B 732  ? 0.1529 0.1841 0.1898 0.0269  0.0191  -0.0160 730  LYS B CD  
14409 C CE  . LYS B 732  ? 0.1610 0.1934 0.2023 0.0252  0.0179  -0.0149 730  LYS B CE  
14410 N NZ  . LYS B 732  ? 0.1505 0.1817 0.1929 0.0266  0.0165  -0.0160 730  LYS B NZ  
14411 N N   . PRO B 733  ? 0.1447 0.1624 0.1718 0.0247  0.0143  -0.0185 731  PRO B N   
14412 C CA  . PRO B 733  ? 0.1606 0.1757 0.1884 0.0242  0.0124  -0.0188 731  PRO B CA  
14413 C C   . PRO B 733  ? 0.1453 0.1629 0.1771 0.0254  0.0125  -0.0187 731  PRO B C   
14414 O O   . PRO B 733  ? 0.1500 0.1709 0.1835 0.0272  0.0139  -0.0187 731  PRO B O   
14415 C CB  . PRO B 733  ? 0.1830 0.1933 0.2061 0.0251  0.0113  -0.0205 731  PRO B CB  
14416 C CG  . PRO B 733  ? 0.1765 0.1879 0.1979 0.0275  0.0129  -0.0213 731  PRO B CG  
14417 C CD  . PRO B 733  ? 0.1506 0.1662 0.1735 0.0266  0.0148  -0.0199 731  PRO B CD  
14418 N N   . ALA B 734  ? 0.1542 0.1703 0.1874 0.0245  0.0108  -0.0185 732  ALA B N   
14419 C CA  . ALA B 734  ? 0.1558 0.1741 0.1927 0.0256  0.0104  -0.0184 732  ALA B CA  
14420 C C   . ALA B 734  ? 0.1619 0.1796 0.1977 0.0286  0.0106  -0.0196 732  ALA B C   
14421 O O   . ALA B 734  ? 0.1764 0.1899 0.2078 0.0295  0.0101  -0.0209 732  ALA B O   
14422 C CB  . ALA B 734  ? 0.1667 0.1824 0.2039 0.0243  0.0083  -0.0183 732  ALA B CB  
14423 N N   . GLU B 735  ? 0.1585 0.1805 0.1983 0.0302  0.0113  -0.0193 733  GLU B N   
14424 C CA  . GLU B 735  ? 0.1785 0.2005 0.2176 0.0336  0.0117  -0.0205 733  GLU B CA  
14425 C C   . GLU B 735  ? 0.1743 0.1910 0.2108 0.0346  0.0095  -0.0217 733  GLU B C   
14426 O O   . GLU B 735  ? 0.1796 0.1936 0.2131 0.0372  0.0094  -0.0230 733  GLU B O   
14427 C CB  . GLU B 735  ? 0.1878 0.2165 0.2323 0.0350  0.0129  -0.0198 733  GLU B CB  
14428 C CG  . GLU B 735  ? 0.2232 0.2541 0.2723 0.0336  0.0115  -0.0187 733  GLU B CG  
14429 C CD  . GLU B 735  ? 0.2363 0.2706 0.2886 0.0305  0.0122  -0.0170 733  GLU B CD  
14430 O OE1 . GLU B 735  ? 0.2361 0.2688 0.2861 0.0287  0.0128  -0.0167 733  GLU B OE1 
14431 O OE2 . GLU B 735  ? 0.2622 0.3008 0.3195 0.0299  0.0119  -0.0160 733  GLU B OE2 
14432 N N   . GLU B 736  ? 0.1707 0.1854 0.2078 0.0326  0.0076  -0.0211 734  GLU B N   
14433 C CA  . GLU B 736  ? 0.1703 0.1798 0.2048 0.0334  0.0054  -0.0219 734  GLU B CA  
14434 C C   . GLU B 736  ? 0.1729 0.1762 0.2015 0.0327  0.0047  -0.0229 734  GLU B C   
14435 O O   . GLU B 736  ? 0.2017 0.2001 0.2272 0.0340  0.0032  -0.0238 734  GLU B O   
14436 C CB  . GLU B 736  ? 0.1611 0.1705 0.1977 0.0313  0.0037  -0.0209 734  GLU B CB  
14437 C CG  . GLU B 736  ? 0.1980 0.2130 0.2404 0.0318  0.0038  -0.0201 734  GLU B CG  
14438 C CD  . GLU B 736  ? 0.2001 0.2195 0.2458 0.0294  0.0050  -0.0188 734  GLU B CD  
14439 O OE1 . GLU B 736  ? 0.1943 0.2136 0.2384 0.0282  0.0064  -0.0186 734  GLU B OE1 
14440 O OE2 . GLU B 736  ? 0.2726 0.2954 0.3225 0.0287  0.0045  -0.0179 734  GLU B OE2 
14441 N N   . THR B 737  ? 0.1728 0.1758 0.1996 0.0306  0.0055  -0.0226 735  THR B N   
14442 C CA  . THR B 737  ? 0.1860 0.1836 0.2077 0.0291  0.0044  -0.0232 735  THR B CA  
14443 C C   . THR B 737  ? 0.1785 0.1761 0.1975 0.0290  0.0058  -0.0237 735  THR B C   
14444 O O   . THR B 737  ? 0.1905 0.1874 0.2079 0.0266  0.0057  -0.0233 735  THR B O   
14445 C CB  . THR B 737  ? 0.1618 0.1585 0.1838 0.0260  0.0032  -0.0222 735  THR B CB  
14446 O OG1 . THR B 737  ? 0.1699 0.1714 0.1954 0.0246  0.0045  -0.0210 735  THR B OG1 
14447 C CG2 . THR B 737  ? 0.1883 0.1835 0.2114 0.0262  0.0015  -0.0219 735  THR B CG2 
14448 N N   . PRO B 738  ? 0.1595 0.1578 0.1776 0.0317  0.0070  -0.0246 736  PRO B N   
14449 C CA  . PRO B 738  ? 0.1717 0.1702 0.1869 0.0317  0.0083  -0.0251 736  PRO B CA  
14450 C C   . PRO B 738  ? 0.1793 0.1715 0.1886 0.0310  0.0069  -0.0263 736  PRO B C   
14451 O O   . PRO B 738  ? 0.1770 0.1690 0.1838 0.0300  0.0075  -0.0265 736  PRO B O   
14452 C CB  . PRO B 738  ? 0.1792 0.1805 0.1954 0.0352  0.0101  -0.0259 736  PRO B CB  
14453 C CG  . PRO B 738  ? 0.1910 0.1899 0.2075 0.0373  0.0087  -0.0266 736  PRO B CG  
14454 C CD  . PRO B 738  ? 0.1830 0.1823 0.2026 0.0351  0.0073  -0.0254 736  PRO B CD  
14455 N N   . LEU B 739  ? 0.1708 0.1576 0.1775 0.0315  0.0050  -0.0272 737  LEU B N   
14456 C CA  . LEU B 739  ? 0.1883 0.1688 0.1890 0.0310  0.0037  -0.0284 737  LEU B CA  
14457 C C   . LEU B 739  ? 0.1854 0.1649 0.1847 0.0272  0.0028  -0.0276 737  LEU B C   
14458 O O   . LEU B 739  ? 0.1868 0.1645 0.1825 0.0262  0.0027  -0.0282 737  LEU B O   
14459 C CB  . LEU B 739  ? 0.1818 0.1565 0.1800 0.0325  0.0018  -0.0294 737  LEU B CB  
14460 C CG  . LEU B 739  ? 0.1836 0.1592 0.1830 0.0367  0.0027  -0.0303 737  LEU B CG  
14461 C CD1 . LEU B 739  ? 0.2050 0.1743 0.2018 0.0379  0.0005  -0.0310 737  LEU B CD1 
14462 C CD2 . LEU B 739  ? 0.2174 0.1930 0.2139 0.0391  0.0042  -0.0318 737  LEU B CD2 
14463 N N   . ILE B 740  ? 0.1783 0.1589 0.1802 0.0251  0.0020  -0.0263 738  ILE B N   
14464 C CA  . ILE B 740  ? 0.1796 0.1598 0.1805 0.0217  0.0013  -0.0255 738  ILE B CA  
14465 C C   . ILE B 740  ? 0.1751 0.1601 0.1776 0.0209  0.0029  -0.0249 738  ILE B C   
14466 O O   . ILE B 740  ? 0.1813 0.1659 0.1817 0.0189  0.0025  -0.0247 738  ILE B O   
14467 C CB  . ILE B 740  ? 0.2132 0.1934 0.2161 0.0198  0.0001  -0.0244 738  ILE B CB  
14468 C CG1 . ILE B 740  ? 0.2075 0.1871 0.2088 0.0164  -0.0007 -0.0237 738  ILE B CG1 
14469 C CG2 . ILE B 740  ? 0.2032 0.1887 0.2114 0.0204  0.0013  -0.0233 738  ILE B CG2 
14470 C CD1 . ILE B 740  ? 0.2346 0.2086 0.2306 0.0152  -0.0023 -0.0245 738  ILE B CD1 
14471 N N   . ALA B 741  ? 0.1533 0.1431 0.1596 0.0225  0.0047  -0.0243 739  ALA B N   
14472 C CA  . ALA B 741  ? 0.1606 0.1546 0.1682 0.0219  0.0062  -0.0236 739  ALA B CA  
14473 C C   . ALA B 741  ? 0.1718 0.1641 0.1751 0.0227  0.0066  -0.0247 739  ALA B C   
14474 O O   . ALA B 741  ? 0.1763 0.1694 0.1781 0.0211  0.0067  -0.0244 739  ALA B O   
14475 C CB  . ALA B 741  ? 0.1805 0.1795 0.1927 0.0233  0.0080  -0.0228 739  ALA B CB  
14476 N N   . ALA B 742  ? 0.1733 0.1632 0.1744 0.0252  0.0068  -0.0262 740  ALA B N   
14477 C CA  . ALA B 742  ? 0.1761 0.1638 0.1725 0.0262  0.0071  -0.0275 740  ALA B CA  
14478 C C   . ALA B 742  ? 0.1781 0.1613 0.1702 0.0236  0.0051  -0.0279 740  ALA B C   
14479 O O   . ALA B 742  ? 0.1849 0.1680 0.1741 0.0228  0.0052  -0.0282 740  ALA B O   
14480 C CB  . ALA B 742  ? 0.2069 0.1918 0.2011 0.0295  0.0074  -0.0292 740  ALA B CB  
14481 N N   . GLU B 743  ? 0.1962 0.1759 0.1878 0.0222  0.0032  -0.0279 741  GLU B N   
14482 C CA  . GLU B 743  ? 0.1945 0.1704 0.1825 0.0194  0.0013  -0.0281 741  GLU B CA  
14483 C C   . GLU B 743  ? 0.1832 0.1632 0.1731 0.0167  0.0015  -0.0266 741  GLU B C   
14484 O O   . GLU B 743  ? 0.1967 0.1758 0.1836 0.0150  0.0007  -0.0268 741  GLU B O   
14485 C CB  . GLU B 743  ? 0.2035 0.1749 0.1906 0.0185  -0.0006 -0.0281 741  GLU B CB  
14486 C CG  . GLU B 743  ? 0.2099 0.1774 0.1934 0.0153  -0.0026 -0.0281 741  GLU B CG  
14487 C CD  . GLU B 743  ? 0.2436 0.2058 0.2212 0.0155  -0.0036 -0.0298 741  GLU B CD  
14488 O OE1 . GLU B 743  ? 0.2387 0.1995 0.2144 0.0185  -0.0028 -0.0312 741  GLU B OE1 
14489 O OE2 . GLU B 743  ? 0.2881 0.2477 0.2628 0.0124  -0.0054 -0.0297 741  GLU B OE2 
14490 N N   . GLY B 744  ? 0.1831 0.1678 0.1779 0.0165  0.0025  -0.0252 742  GLY B N   
14491 C CA  . GLY B 744  ? 0.1913 0.1800 0.1880 0.0146  0.0029  -0.0238 742  GLY B CA  
14492 C C   . GLY B 744  ? 0.1593 0.1501 0.1546 0.0151  0.0040  -0.0240 742  GLY B C   
14493 O O   . GLY B 744  ? 0.1721 0.1639 0.1662 0.0133  0.0034  -0.0235 742  GLY B O   
14494 N N   . VAL B 745  ? 0.1692 0.1610 0.1647 0.0177  0.0055  -0.0245 743  VAL B N   
14495 C CA  . VAL B 745  ? 0.1638 0.1576 0.1575 0.0183  0.0067  -0.0245 743  VAL B CA  
14496 C C   . VAL B 745  ? 0.1850 0.1747 0.1730 0.0178  0.0053  -0.0260 743  VAL B C   
14497 O O   . VAL B 745  ? 0.1852 0.1760 0.1714 0.0167  0.0052  -0.0257 743  VAL B O   
14498 C CB  . VAL B 745  ? 0.1905 0.1868 0.1858 0.0210  0.0089  -0.0246 743  VAL B CB  
14499 C CG1 . VAL B 745  ? 0.1790 0.1762 0.1711 0.0220  0.0100  -0.0250 743  VAL B CG1 
14500 C CG2 . VAL B 745  ? 0.1877 0.1886 0.1885 0.0208  0.0100  -0.0228 743  VAL B CG2 
14501 N N   . ARG B 746  ? 0.1865 0.1710 0.1715 0.0185  0.0042  -0.0275 744  ARG B N   
14502 C CA  . ARG B 746  ? 0.1968 0.1765 0.1760 0.0176  0.0026  -0.0290 744  ARG B CA  
14503 C C   . ARG B 746  ? 0.1760 0.1561 0.1547 0.0141  0.0009  -0.0281 744  ARG B C   
14504 O O   . ARG B 746  ? 0.1871 0.1665 0.1623 0.0130  0.0001  -0.0286 744  ARG B O   
14505 C CB  . ARG B 746  ? 0.1963 0.1695 0.1724 0.0184  0.0011  -0.0305 744  ARG B CB  
14506 C CG  . ARG B 746  ? 0.2247 0.1966 0.2000 0.0222  0.0024  -0.0319 744  ARG B CG  
14507 C CD  . ARG B 746  ? 0.2162 0.1809 0.1878 0.0228  0.0006  -0.0334 744  ARG B CD  
14508 N NE  . ARG B 746  ? 0.2342 0.1984 0.2061 0.0268  0.0019  -0.0345 744  ARG B NE  
14509 C CZ  . ARG B 746  ? 0.2069 0.1723 0.1827 0.0283  0.0023  -0.0339 744  ARG B CZ  
14510 N NH1 . ARG B 746  ? 0.2222 0.1878 0.2008 0.0261  0.0012  -0.0326 744  ARG B NH1 
14511 N NH2 . ARG B 746  ? 0.2349 0.2018 0.2117 0.0321  0.0039  -0.0347 744  ARG B NH2 
14512 N N   . ILE B 747  ? 0.1831 0.1644 0.1652 0.0123  0.0002  -0.0269 745  ILE B N   
14513 C CA  . ILE B 747  ? 0.1764 0.1586 0.1584 0.0090  -0.0013 -0.0260 745  ILE B CA  
14514 C C   . ILE B 747  ? 0.1926 0.1802 0.1766 0.0085  -0.0004 -0.0248 745  ILE B C   
14515 O O   . ILE B 747  ? 0.1747 0.1628 0.1567 0.0066  -0.0016 -0.0247 745  ILE B O   
14516 C CB  . ILE B 747  ? 0.1772 0.1592 0.1620 0.0076  -0.0020 -0.0251 745  ILE B CB  
14517 C CG1 . ILE B 747  ? 0.2083 0.1839 0.1897 0.0073  -0.0036 -0.0262 745  ILE B CG1 
14518 C CG2 . ILE B 747  ? 0.1893 0.1746 0.1756 0.0045  -0.0029 -0.0237 745  ILE B CG2 
14519 C CD1 . ILE B 747  ? 0.2218 0.1968 0.2057 0.0064  -0.0041 -0.0254 745  ILE B CD1 
14520 N N   . LEU B 748  ? 0.1727 0.1644 0.1606 0.0101  0.0015  -0.0238 746  LEU B N   
14521 C CA  . LEU B 748  ? 0.1653 0.1618 0.1548 0.0099  0.0023  -0.0225 746  LEU B CA  
14522 C C   . LEU B 748  ? 0.1776 0.1735 0.1630 0.0106  0.0024  -0.0233 746  LEU B C   
14523 O O   . LEU B 748  ? 0.1737 0.1718 0.1584 0.0093  0.0018  -0.0227 746  LEU B O   
14524 C CB  . LEU B 748  ? 0.1737 0.1738 0.1676 0.0114  0.0043  -0.0213 746  LEU B CB  
14525 C CG  . LEU B 748  ? 0.2031 0.2051 0.2011 0.0103  0.0041  -0.0201 746  LEU B CG  
14526 C CD1 . LEU B 748  ? 0.2229 0.2269 0.2248 0.0119  0.0057  -0.0194 746  LEU B CD1 
14527 C CD2 . LEU B 748  ? 0.2370 0.2424 0.2360 0.0088  0.0036  -0.0189 746  LEU B CD2 
14528 N N   . ARG B 749  ? 0.1741 0.1673 0.1569 0.0127  0.0032  -0.0247 747  ARG B N   
14529 C CA  . ARG B 749  ? 0.1845 0.1768 0.1628 0.0134  0.0033  -0.0256 747  ARG B CA  
14530 C C   . ARG B 749  ? 0.1853 0.1741 0.1592 0.0111  0.0008  -0.0266 747  ARG B C   
14531 O O   . ARG B 749  ? 0.1911 0.1810 0.1626 0.0103  0.0002  -0.0266 747  ARG B O   
14532 C CB  . ARG B 749  ? 0.1803 0.1704 0.1565 0.0164  0.0047  -0.0271 747  ARG B CB  
14533 C CG  . ARG B 749  ? 0.1916 0.1861 0.1715 0.0184  0.0073  -0.0260 747  ARG B CG  
14534 C CD  . ARG B 749  ? 0.2267 0.2196 0.2041 0.0214  0.0088  -0.0275 747  ARG B CD  
14535 N NE  . ARG B 749  ? 0.2200 0.2176 0.2008 0.0231  0.0114  -0.0263 747  ARG B NE  
14536 C CZ  . ARG B 749  ? 0.2730 0.2711 0.2522 0.0258  0.0132  -0.0271 747  ARG B CZ  
14537 N NH1 . ARG B 749  ? 0.2776 0.2714 0.2515 0.0273  0.0127  -0.0293 747  ARG B NH1 
14538 N NH2 . ARG B 749  ? 0.2740 0.2769 0.2568 0.0270  0.0155  -0.0257 747  ARG B NH2 
14539 N N   . GLU B 750  ? 0.1760 0.1605 0.1488 0.0100  -0.0008 -0.0275 748  GLU B N   
14540 C CA  . GLU B 750  ? 0.1906 0.1716 0.1593 0.0074  -0.0033 -0.0283 748  GLU B CA  
14541 C C   . GLU B 750  ? 0.1765 0.1619 0.1474 0.0046  -0.0043 -0.0267 748  GLU B C   
14542 O O   . GLU B 750  ? 0.2072 0.1920 0.1748 0.0028  -0.0060 -0.0271 748  GLU B O   
14543 C CB  . GLU B 750  ? 0.1959 0.1717 0.1635 0.0064  -0.0048 -0.0291 748  GLU B CB  
14544 C CG  . GLU B 750  ? 0.2242 0.1958 0.1875 0.0034  -0.0075 -0.0299 748  GLU B CG  
14545 C CD  . GLU B 750  ? 0.2503 0.2157 0.2117 0.0026  -0.0090 -0.0307 748  GLU B CD  
14546 O OE1 . GLU B 750  ? 0.2526 0.2168 0.2157 0.0049  -0.0078 -0.0309 748  GLU B OE1 
14547 O OE2 . GLU B 750  ? 0.2940 0.2559 0.2523 -0.0004 -0.0114 -0.0310 748  GLU B OE2 
14548 N N   . ALA B 751  ? 0.1824 0.1724 0.1586 0.0044  -0.0033 -0.0250 749  ALA B N   
14549 C CA  . ALA B 751  ? 0.1776 0.1723 0.1565 0.0023  -0.0041 -0.0234 749  ALA B CA  
14550 C C   . ALA B 751  ? 0.2045 0.2033 0.1836 0.0031  -0.0033 -0.0226 749  ALA B C   
14551 O O   . ALA B 751  ? 0.2114 0.2143 0.1924 0.0016  -0.0040 -0.0213 749  ALA B O   
14552 C CB  . ALA B 751  ? 0.1888 0.1864 0.1730 0.0023  -0.0031 -0.0220 749  ALA B CB  
14553 N N   . GLY B 752  ? 0.1943 0.1924 0.1713 0.0055  -0.0019 -0.0232 750  GLY B N   
14554 C CA  . GLY B 752  ? 0.1953 0.1966 0.1715 0.0062  -0.0014 -0.0225 750  GLY B CA  
14555 C C   . GLY B 752  ? 0.1976 0.2016 0.1764 0.0086  0.0011  -0.0214 750  GLY B C   
14556 O O   . GLY B 752  ? 0.2099 0.2163 0.1876 0.0093  0.0017  -0.0207 750  GLY B O   
14557 N N   . ILE B 753  ? 0.1898 0.1937 0.1718 0.0099  0.0026  -0.0212 751  ILE B N   
14558 C CA  . ILE B 753  ? 0.1866 0.1931 0.1710 0.0119  0.0049  -0.0202 751  ILE B CA  
14559 C C   . ILE B 753  ? 0.2053 0.2101 0.1859 0.0138  0.0061  -0.0213 751  ILE B C   
14560 O O   . ILE B 753  ? 0.2067 0.2079 0.1853 0.0147  0.0061  -0.0230 751  ILE B O   
14561 C CB  . ILE B 753  ? 0.1607 0.1676 0.1497 0.0125  0.0060  -0.0197 751  ILE B CB  
14562 C CG1 . ILE B 753  ? 0.1873 0.1957 0.1796 0.0107  0.0049  -0.0187 751  ILE B CG1 
14563 C CG2 . ILE B 753  ? 0.2032 0.2129 0.1947 0.0142  0.0083  -0.0185 751  ILE B CG2 
14564 C CD1 . ILE B 753  ? 0.1749 0.1872 0.1692 0.0103  0.0049  -0.0170 751  ILE B CD1 
14565 N N   . PRO B 754  ? 0.2080 0.2151 0.1874 0.0147  0.0072  -0.0205 752  PRO B N   
14566 C CA  . PRO B 754  ? 0.2009 0.2067 0.1762 0.0166  0.0084  -0.0216 752  PRO B CA  
14567 C C   . PRO B 754  ? 0.1943 0.2001 0.1717 0.0187  0.0106  -0.0219 752  PRO B C   
14568 O O   . PRO B 754  ? 0.2040 0.2119 0.1864 0.0187  0.0115  -0.0207 752  PRO B O   
14569 C CB  . PRO B 754  ? 0.2329 0.2419 0.2074 0.0169  0.0093  -0.0200 752  PRO B CB  
14570 C CG  . PRO B 754  ? 0.2662 0.2774 0.2430 0.0149  0.0076  -0.0185 752  PRO B CG  
14571 C CD  . PRO B 754  ? 0.1919 0.2027 0.1730 0.0140  0.0071  -0.0185 752  PRO B CD  
14572 N N   . ALA B 755  ? 0.2327 0.2360 0.2063 0.0205  0.0113  -0.0237 753  ALA B N   
14573 C CA  . ALA B 755  ? 0.2521 0.2558 0.2277 0.0227  0.0132  -0.0241 753  ALA B CA  
14574 C C   . ALA B 755  ? 0.2139 0.2225 0.1933 0.0234  0.0157  -0.0221 753  ALA B C   
14575 O O   . ALA B 755  ? 0.2418 0.2522 0.2256 0.0242  0.0169  -0.0215 753  ALA B O   
14576 C CB  . ALA B 755  ? 0.2986 0.2991 0.2689 0.0249  0.0137  -0.0264 753  ALA B CB  
14577 N N   . SER B 756  ? 0.2028 0.2136 0.1805 0.0231  0.0162  -0.0208 754  SER B N   
14578 C CA  . SER B 756  ? 0.2089 0.2240 0.1899 0.0235  0.0184  -0.0186 754  SER B CA  
14579 C C   . SER B 756  ? 0.2043 0.2212 0.1908 0.0218  0.0179  -0.0167 754  SER B C   
14580 O O   . SER B 756  ? 0.2105 0.2303 0.2006 0.0220  0.0195  -0.0150 754  SER B O   
14581 C CB  . SER B 756  ? 0.2439 0.2605 0.2213 0.0236  0.0191  -0.0176 754  SER B CB  
14582 O OG  . SER B 756  ? 0.2901 0.3059 0.2662 0.0218  0.0168  -0.0172 754  SER B OG  
14583 N N   . ALA B 757  ? 0.1775 0.1927 0.1645 0.0202  0.0156  -0.0170 755  ALA B N   
14584 C CA  . ALA B 757  ? 0.1575 0.1742 0.1493 0.0189  0.0151  -0.0155 755  ALA B CA  
14585 C C   . ALA B 757  ? 0.1680 0.1838 0.1633 0.0189  0.0150  -0.0161 755  ALA B C   
14586 O O   . ALA B 757  ? 0.1759 0.1930 0.1753 0.0182  0.0149  -0.0149 755  ALA B O   
14587 C CB  . ALA B 757  ? 0.1699 0.1861 0.1608 0.0172  0.0129  -0.0152 755  ALA B CB  
14588 N N   . LEU B 758  ? 0.1723 0.1856 0.1659 0.0199  0.0148  -0.0180 756  LEU B N   
14589 C CA  . LEU B 758  ? 0.1669 0.1792 0.1638 0.0200  0.0145  -0.0185 756  LEU B CA  
14590 C C   . LEU B 758  ? 0.1679 0.1792 0.1636 0.0222  0.0156  -0.0200 756  LEU B C   
14591 O O   . LEU B 758  ? 0.1916 0.1995 0.1831 0.0229  0.0147  -0.0219 756  LEU B O   
14592 C CB  . LEU B 758  ? 0.1673 0.1767 0.1634 0.0184  0.0121  -0.0193 756  LEU B CB  
14593 C CG  . LEU B 758  ? 0.1671 0.1750 0.1658 0.0186  0.0117  -0.0200 756  LEU B CG  
14594 C CD1 . LEU B 758  ? 0.1679 0.1787 0.1719 0.0184  0.0126  -0.0184 756  LEU B CD1 
14595 C CD2 . LEU B 758  ? 0.1793 0.1844 0.1767 0.0167  0.0094  -0.0206 756  LEU B CD2 
14596 N N   . GLN B 759  ? 0.1619 0.1760 0.1611 0.0233  0.0174  -0.0192 757  GLN B N   
14597 C CA  . GLN B 759  ? 0.1621 0.1764 0.1612 0.0257  0.0187  -0.0204 757  GLN B CA  
14598 C C   . GLN B 759  ? 0.1680 0.1825 0.1715 0.0258  0.0183  -0.0203 757  GLN B C   
14599 O O   . GLN B 759  ? 0.1776 0.1940 0.1852 0.0244  0.0181  -0.0188 757  GLN B O   
14600 C CB  . GLN B 759  ? 0.1596 0.1781 0.1593 0.0269  0.0212  -0.0193 757  GLN B CB  
14601 C CG  . GLN B 759  ? 0.1777 0.1958 0.1723 0.0270  0.0217  -0.0194 757  GLN B CG  
14602 C CD  . GLN B 759  ? 0.1795 0.2020 0.1749 0.0278  0.0243  -0.0179 757  GLN B CD  
14603 O OE1 . GLN B 759  ? 0.2136 0.2373 0.2073 0.0299  0.0260  -0.0188 757  GLN B OE1 
14604 N NE2 . GLN B 759  ? 0.1819 0.2068 0.1799 0.0261  0.0246  -0.0156 757  GLN B NE2 
14605 N N   . LEU B 760  ? 0.1671 0.1793 0.1694 0.0276  0.0180  -0.0221 758  LEU B N   
14606 C CA  . LEU B 760  ? 0.1608 0.1729 0.1669 0.0280  0.0174  -0.0222 758  LEU B CA  
14607 C C   . LEU B 760  ? 0.1774 0.1931 0.1860 0.0305  0.0195  -0.0222 758  LEU B C   
14608 O O   . LEU B 760  ? 0.1846 0.1999 0.1902 0.0328  0.0205  -0.0235 758  LEU B O   
14609 C CB  . LEU B 760  ? 0.1736 0.1801 0.1763 0.0285  0.0154  -0.0241 758  LEU B CB  
14610 C CG  . LEU B 760  ? 0.1656 0.1714 0.1715 0.0291  0.0146  -0.0243 758  LEU B CG  
14611 C CD1 . LEU B 760  ? 0.2035 0.2094 0.2123 0.0264  0.0132  -0.0230 758  LEU B CD1 
14612 C CD2 . LEU B 760  ? 0.2047 0.2051 0.2068 0.0306  0.0132  -0.0263 758  LEU B CD2 
14613 N N   . LEU B 761  ? 0.1669 0.1862 0.1809 0.0300  0.0200  -0.0208 759  LEU B N   
14614 C CA  . LEU B 761  ? 0.1606 0.1845 0.1781 0.0320  0.0219  -0.0204 759  LEU B CA  
14615 C C   . LEU B 761  ? 0.1510 0.1747 0.1722 0.0325  0.0207  -0.0207 759  LEU B C   
14616 O O   . LEU B 761  ? 0.1649 0.1911 0.1906 0.0309  0.0205  -0.0192 759  LEU B O   
14617 C CB  . LEU B 761  ? 0.1758 0.2050 0.1968 0.0307  0.0237  -0.0182 759  LEU B CB  
14618 C CG  . LEU B 761  ? 0.1857 0.2159 0.2035 0.0302  0.0251  -0.0175 759  LEU B CG  
14619 C CD1 . LEU B 761  ? 0.2081 0.2368 0.2207 0.0327  0.0260  -0.0193 759  LEU B CD1 
14620 C CD2 . LEU B 761  ? 0.2083 0.2357 0.2243 0.0277  0.0235  -0.0168 759  LEU B CD2 
14621 N N   . PRO B 762  ? 0.1620 0.1824 0.1811 0.0346  0.0198  -0.0225 760  PRO B N   
14622 C CA  . PRO B 762  ? 0.1599 0.1802 0.1823 0.0353  0.0187  -0.0226 760  PRO B CA  
14623 C C   . PRO B 762  ? 0.1692 0.1961 0.1970 0.0366  0.0204  -0.0217 760  PRO B C   
14624 O O   . PRO B 762  ? 0.1742 0.2049 0.2021 0.0381  0.0227  -0.0215 760  PRO B O   
14625 C CB  . PRO B 762  ? 0.1734 0.1886 0.1916 0.0377  0.0176  -0.0248 760  PRO B CB  
14626 C CG  . PRO B 762  ? 0.1857 0.1971 0.1980 0.0372  0.0174  -0.0258 760  PRO B CG  
14627 C CD  . PRO B 762  ? 0.1675 0.1836 0.1807 0.0365  0.0196  -0.0245 760  PRO B CD  
14628 N N   . GLY B 763  ? 0.1659 0.1941 0.1979 0.0361  0.0193  -0.0210 761  GLY B N   
14629 C CA  . GLY B 763  ? 0.1598 0.1941 0.1972 0.0373  0.0206  -0.0202 761  GLY B CA  
14630 C C   . GLY B 763  ? 0.1547 0.1908 0.1969 0.0348  0.0194  -0.0186 761  GLY B C   
14631 O O   . GLY B 763  ? 0.1814 0.2136 0.2224 0.0326  0.0176  -0.0185 761  GLY B O   
14632 N N   . ASP B 764  ? 0.1915 0.2338 0.2391 0.0352  0.0204  -0.0175 762  ASP B N   
14633 C CA  . ASP B 764  ? 0.1843 0.2284 0.2365 0.0330  0.0191  -0.0163 762  ASP B CA  
14634 C C   . ASP B 764  ? 0.1947 0.2413 0.2488 0.0299  0.0200  -0.0143 762  ASP B C   
14635 O O   . ASP B 764  ? 0.1842 0.2300 0.2355 0.0292  0.0213  -0.0140 762  ASP B O   
14636 C CB  . ASP B 764  ? 0.2030 0.2518 0.2599 0.0351  0.0191  -0.0163 762  ASP B CB  
14637 C CG  . ASP B 764  ? 0.2512 0.3074 0.3117 0.0361  0.0217  -0.0153 762  ASP B CG  
14638 O OD1 . ASP B 764  ? 0.2195 0.2777 0.2794 0.0347  0.0236  -0.0142 762  ASP B OD1 
14639 O OD2 . ASP B 764  ? 0.3316 0.3922 0.3956 0.0384  0.0220  -0.0155 762  ASP B OD2 
14640 N N   . GLY B 765  ? 0.1881 0.2376 0.2469 0.0280  0.0193  -0.0130 763  GLY B N   
14641 C CA  . GLY B 765  ? 0.1820 0.2329 0.2424 0.0249  0.0198  -0.0112 763  GLY B CA  
14642 C C   . GLY B 765  ? 0.1808 0.2364 0.2421 0.0249  0.0225  -0.0100 763  GLY B C   
14643 O O   . GLY B 765  ? 0.1800 0.2351 0.2406 0.0226  0.0231  -0.0086 763  GLY B O   
14644 N N   . ARG B 766  ? 0.1815 0.2416 0.2442 0.0274  0.0242  -0.0103 764  ARG B N   
14645 C CA  . ARG B 766  ? 0.1780 0.2428 0.2412 0.0276  0.0270  -0.0091 764  ARG B CA  
14646 C C   . ARG B 766  ? 0.1638 0.2247 0.2210 0.0278  0.0279  -0.0097 764  ARG B C   
14647 O O   . ARG B 766  ? 0.1786 0.2415 0.2353 0.0264  0.0296  -0.0082 764  ARG B O   
14648 C CB  . ARG B 766  ? 0.1671 0.2374 0.2325 0.0308  0.0287  -0.0097 764  ARG B CB  
14649 C CG  . ARG B 766  ? 0.2290 0.3045 0.3008 0.0308  0.0280  -0.0090 764  ARG B CG  
14650 C CD  . ARG B 766  ? 0.3116 0.3918 0.3850 0.0348  0.0293  -0.0101 764  ARG B CD  
14651 N NE  . ARG B 766  ? 0.3842 0.4585 0.4529 0.0380  0.0282  -0.0126 764  ARG B NE  
14652 C CZ  . ARG B 766  ? 0.4592 0.5352 0.5273 0.0421  0.0291  -0.0141 764  ARG B CZ  
14653 N NH1 . ARG B 766  ? 0.4490 0.5331 0.5213 0.0439  0.0313  -0.0135 764  ARG B NH1 
14654 N NH2 . ARG B 766  ? 0.4634 0.5328 0.5266 0.0445  0.0277  -0.0163 764  ARG B NH2 
14655 N N   . VAL B 767  ? 0.1604 0.2158 0.2130 0.0294  0.0266  -0.0117 765  VAL B N   
14656 C CA  . VAL B 767  ? 0.1701 0.2216 0.2170 0.0294  0.0271  -0.0122 765  VAL B CA  
14657 C C   . VAL B 767  ? 0.1564 0.2052 0.2027 0.0262  0.0260  -0.0110 765  VAL B C   
14658 O O   . VAL B 767  ? 0.1696 0.2185 0.2137 0.0252  0.0271  -0.0100 765  VAL B O   
14659 C CB  . VAL B 767  ? 0.1609 0.2072 0.2033 0.0316  0.0258  -0.0147 765  VAL B CB  
14660 C CG1 . VAL B 767  ? 0.1667 0.2090 0.2032 0.0313  0.0260  -0.0153 765  VAL B CG1 
14661 C CG2 . VAL B 767  ? 0.1832 0.2320 0.2260 0.0352  0.0270  -0.0160 765  VAL B CG2 
14662 N N   . GLY B 768  ? 0.1509 0.1973 0.1990 0.0246  0.0239  -0.0109 766  GLY B N   
14663 C CA  . GLY B 768  ? 0.1620 0.2061 0.2098 0.0218  0.0229  -0.0097 766  GLY B CA  
14664 C C   . GLY B 768  ? 0.1572 0.2051 0.2077 0.0200  0.0244  -0.0074 766  GLY B C   
14665 O O   . GLY B 768  ? 0.1631 0.2096 0.2115 0.0186  0.0248  -0.0064 766  GLY B O   
14666 N N   . ALA B 769  ? 0.1662 0.2191 0.2214 0.0199  0.0252  -0.0066 767  ALA B N   
14667 C CA  . ALA B 769  ? 0.1658 0.2223 0.2238 0.0177  0.0265  -0.0042 767  ALA B CA  
14668 C C   . ALA B 769  ? 0.1559 0.2144 0.2113 0.0183  0.0289  -0.0034 767  ALA B C   
14669 O O   . ALA B 769  ? 0.1760 0.2343 0.2307 0.0163  0.0296  -0.0015 767  ALA B O   
14670 C CB  . ALA B 769  ? 0.1718 0.2339 0.2357 0.0174  0.0268  -0.0034 767  ALA B CB  
14671 N N   . ALA B 770  ? 0.1628 0.2228 0.2161 0.0212  0.0303  -0.0047 768  ALA B N   
14672 C CA  . ALA B 770  ? 0.1622 0.2240 0.2125 0.0219  0.0326  -0.0042 768  ALA B CA  
14673 C C   . ALA B 770  ? 0.1684 0.2250 0.2136 0.0211  0.0319  -0.0042 768  ALA B C   
14674 O O   . ALA B 770  ? 0.2008 0.2583 0.2441 0.0201  0.0333  -0.0026 768  ALA B O   
14675 C CB  . ALA B 770  ? 0.1799 0.2435 0.2285 0.0255  0.0340  -0.0060 768  ALA B CB  
14676 N N   . LEU B 771  ? 0.1598 0.2112 0.2026 0.0213  0.0297  -0.0058 769  LEU B N   
14677 C CA  . LEU B 771  ? 0.1596 0.2066 0.1980 0.0205  0.0288  -0.0058 769  LEU B CA  
14678 C C   . LEU B 771  ? 0.1611 0.2074 0.2011 0.0177  0.0283  -0.0037 769  LEU B C   
14679 O O   . LEU B 771  ? 0.1900 0.2354 0.2273 0.0169  0.0288  -0.0025 769  LEU B O   
14680 C CB  . LEU B 771  ? 0.1621 0.2042 0.1982 0.0211  0.0266  -0.0079 769  LEU B CB  
14681 C CG  . LEU B 771  ? 0.1595 0.2005 0.1924 0.0238  0.0268  -0.0101 769  LEU B CG  
14682 C CD1 . LEU B 771  ? 0.1934 0.2298 0.2248 0.0240  0.0244  -0.0119 769  LEU B CD1 
14683 C CD2 . LEU B 771  ? 0.1753 0.2159 0.2033 0.0246  0.0280  -0.0103 769  LEU B CD2 
14684 N N   . VAL B 772  ? 0.1610 0.2073 0.2050 0.0163  0.0270  -0.0032 770  VAL B N   
14685 C CA  . VAL B 772  ? 0.1552 0.2002 0.2006 0.0138  0.0263  -0.0014 770  VAL B CA  
14686 C C   . VAL B 772  ? 0.2072 0.2554 0.2534 0.0125  0.0282  0.0010  770  VAL B C   
14687 O O   . VAL B 772  ? 0.2153 0.2614 0.2599 0.0110  0.0280  0.0026  770  VAL B O   
14688 C CB  . VAL B 772  ? 0.1666 0.2114 0.2161 0.0127  0.0247  -0.0015 770  VAL B CB  
14689 C CG1 . VAL B 772  ? 0.1840 0.2278 0.2353 0.0100  0.0241  0.0005  770  VAL B CG1 
14690 C CG2 . VAL B 772  ? 0.1758 0.2166 0.2238 0.0135  0.0226  -0.0035 770  VAL B CG2 
14691 N N   . ALA B 773  ? 0.1820 0.2354 0.2307 0.0131  0.0301  0.0015  771  ALA B N   
14692 C CA  . ALA B 773  ? 0.1952 0.2523 0.2451 0.0116  0.0321  0.0040  771  ALA B CA  
14693 C C   . ALA B 773  ? 0.2456 0.3028 0.2908 0.0126  0.0339  0.0045  771  ALA B C   
14694 O O   . ALA B 773  ? 0.2483 0.3078 0.2937 0.0111  0.0355  0.0069  771  ALA B O   
14695 C CB  . ALA B 773  ? 0.2219 0.2854 0.2766 0.0119  0.0336  0.0044  771  ALA B CB  
14696 N N   . ALA B 774  ? 0.1981 0.2529 0.2391 0.0148  0.0336  0.0025  772  ALA B N   
14697 C CA  . ALA B 774  ? 0.2024 0.2576 0.2387 0.0160  0.0352  0.0027  772  ALA B CA  
14698 C C   . ALA B 774  ? 0.2267 0.2793 0.2606 0.0141  0.0349  0.0048  772  ALA B C   
14699 O O   . ALA B 774  ? 0.2271 0.2758 0.2611 0.0128  0.0329  0.0050  772  ALA B O   
14700 C CB  . ALA B 774  ? 0.2319 0.2842 0.2641 0.0184  0.0344  -0.0001 772  ALA B CB  
14701 N N   . ALA B 775  ? 0.2630 0.3180 0.2944 0.0141  0.0370  0.0063  773  ALA B N   
14702 C CA  . ALA B 775  ? 0.2738 0.3269 0.3033 0.0122  0.0370  0.0088  773  ALA B CA  
14703 C C   . ALA B 775  ? 0.2318 0.2795 0.2575 0.0125  0.0348  0.0080  773  ALA B C   
14704 O O   . ALA B 775  ? 0.2695 0.3143 0.2952 0.0109  0.0336  0.0096  773  ALA B O   
14705 C CB  . ALA B 775  ? 0.3168 0.3733 0.3435 0.0126  0.0397  0.0103  773  ALA B CB  
14706 N N   . GLU B 776  ? 0.2295 0.2758 0.2521 0.0145  0.0341  0.0056  774  GLU B N   
14707 C CA  . GLU B 776  ? 0.2082 0.2502 0.2270 0.0148  0.0322  0.0050  774  GLU B CA  
14708 C C   . GLU B 776  ? 0.1955 0.2344 0.2161 0.0146  0.0298  0.0035  774  GLU B C   
14709 O O   . GLU B 776  ? 0.1953 0.2311 0.2133 0.0148  0.0281  0.0029  774  GLU B O   
14710 C CB  . GLU B 776  ? 0.2236 0.2656 0.2374 0.0168  0.0327  0.0033  774  GLU B CB  
14711 C CG  . GLU B 776  ? 0.2804 0.3253 0.2914 0.0172  0.0352  0.0047  774  GLU B CG  
14712 C CD  . GLU B 776  ? 0.3593 0.4086 0.3721 0.0185  0.0375  0.0039  774  GLU B CD  
14713 O OE1 . GLU B 776  ? 0.3017 0.3517 0.3182 0.0190  0.0370  0.0024  774  GLU B OE1 
14714 O OE2 . GLU B 776  ? 0.4141 0.4663 0.4246 0.0191  0.0398  0.0048  774  GLU B OE2 
14715 N N   . THR B 777  ? 0.1814 0.2212 0.2063 0.0143  0.0295  0.0028  775  THR B N   
14716 C CA  . THR B 777  ? 0.1815 0.2182 0.2079 0.0140  0.0272  0.0015  775  THR B CA  
14717 C C   . THR B 777  ? 0.1804 0.2144 0.2070 0.0125  0.0260  0.0031  775  THR B C   
14718 O O   . THR B 777  ? 0.1909 0.2255 0.2194 0.0110  0.0265  0.0052  775  THR B O   
14719 C CB  . THR B 777  ? 0.1843 0.2229 0.2153 0.0138  0.0272  0.0008  775  THR B CB  
14720 O OG1 . THR B 777  ? 0.2167 0.2571 0.2469 0.0157  0.0281  -0.0010 775  THR B OG1 
14721 C CG2 . THR B 777  ? 0.1822 0.2177 0.2147 0.0133  0.0250  -0.0002 775  THR B CG2 
14722 N N   . ALA B 778  ? 0.1475 0.1786 0.1720 0.0130  0.0242  0.0022  776  ALA B N   
14723 C CA  . ALA B 778  ? 0.1628 0.1912 0.1868 0.0122  0.0230  0.0035  776  ALA B CA  
14724 C C   . ALA B 778  ? 0.1684 0.1945 0.1946 0.0118  0.0212  0.0025  776  ALA B C   
14725 O O   . ALA B 778  ? 0.1860 0.2097 0.2121 0.0113  0.0202  0.0035  776  ALA B O   
14726 C CB  . ALA B 778  ? 0.1649 0.1922 0.1846 0.0131  0.0224  0.0034  776  ALA B CB  
14727 N N   . GLY B 779  ? 0.1548 0.1814 0.1828 0.0121  0.0208  0.0007  777  GLY B N   
14728 C CA  . GLY B 779  ? 0.1710 0.1956 0.2009 0.0118  0.0192  -0.0002 777  GLY B CA  
14729 C C   . GLY B 779  ? 0.1408 0.1665 0.1725 0.0122  0.0191  -0.0020 777  GLY B C   
14730 O O   . GLY B 779  ? 0.1564 0.1838 0.1869 0.0132  0.0199  -0.0029 777  GLY B O   
14731 N N   . VAL B 780  ? 0.1477 0.1724 0.1820 0.0116  0.0180  -0.0025 778  VAL B N   
14732 C CA  . VAL B 780  ? 0.1384 0.1639 0.1744 0.0120  0.0177  -0.0040 778  VAL B CA  
14733 C C   . VAL B 780  ? 0.1502 0.1732 0.1862 0.0119  0.0159  -0.0052 778  VAL B C   
14734 O O   . VAL B 780  ? 0.1534 0.1746 0.1901 0.0111  0.0151  -0.0046 778  VAL B O   
14735 C CB  . VAL B 780  ? 0.1527 0.1805 0.1925 0.0113  0.0184  -0.0033 778  VAL B CB  
14736 C CG1 . VAL B 780  ? 0.1657 0.1942 0.2072 0.0120  0.0178  -0.0049 778  VAL B CG1 
14737 C CG2 . VAL B 780  ? 0.1640 0.1950 0.2039 0.0114  0.0204  -0.0020 778  VAL B CG2 
14738 N N   . MET B 781  ? 0.1361 0.1587 0.1710 0.0127  0.0153  -0.0068 779  MET B N   
14739 C CA  . MET B 781  ? 0.1442 0.1648 0.1791 0.0125  0.0137  -0.0079 779  MET B CA  
14740 C C   . MET B 781  ? 0.1455 0.1667 0.1825 0.0128  0.0135  -0.0089 779  MET B C   
14741 O O   . MET B 781  ? 0.1523 0.1742 0.1884 0.0138  0.0139  -0.0097 779  MET B O   
14742 C CB  . MET B 781  ? 0.1453 0.1648 0.1772 0.0130  0.0131  -0.0089 779  MET B CB  
14743 C CG  . MET B 781  ? 0.1597 0.1792 0.1896 0.0130  0.0134  -0.0079 779  MET B CG  
14744 S SD  . MET B 781  ? 0.1542 0.1731 0.1807 0.0133  0.0126  -0.0089 779  MET B SD  
14745 C CE  . MET B 781  ? 0.1574 0.1751 0.1847 0.0127  0.0111  -0.0095 779  MET B CE  
14746 N N   . PHE B 782  ? 0.1372 0.1580 0.1766 0.0120  0.0127  -0.0087 780  PHE B N   
14747 C CA  . PHE B 782  ? 0.1399 0.1614 0.1815 0.0123  0.0122  -0.0093 780  PHE B CA  
14748 C C   . PHE B 782  ? 0.1207 0.1399 0.1621 0.0119  0.0105  -0.0102 780  PHE B C   
14749 O O   . PHE B 782  ? 0.1468 0.1645 0.1881 0.0111  0.0098  -0.0099 780  PHE B O   
14750 C CB  . PHE B 782  ? 0.1459 0.1696 0.1911 0.0114  0.0127  -0.0082 780  PHE B CB  
14751 C CG  . PHE B 782  ? 0.1293 0.1542 0.1773 0.0115  0.0120  -0.0087 780  PHE B CG  
14752 C CD1 . PHE B 782  ? 0.1461 0.1733 0.1948 0.0129  0.0127  -0.0093 780  PHE B CD1 
14753 C CD2 . PHE B 782  ? 0.1466 0.1701 0.1960 0.0105  0.0105  -0.0088 780  PHE B CD2 
14754 C CE1 . PHE B 782  ? 0.1623 0.1907 0.2135 0.0133  0.0119  -0.0098 780  PHE B CE1 
14755 C CE2 . PHE B 782  ? 0.1565 0.1813 0.2085 0.0107  0.0096  -0.0093 780  PHE B CE2 
14756 C CZ  . PHE B 782  ? 0.1412 0.1686 0.1942 0.0121  0.0103  -0.0097 780  PHE B CZ  
14757 N N   . THR B 783  ? 0.1261 0.1449 0.1672 0.0126  0.0099  -0.0114 781  THR B N   
14758 C CA  . THR B 783  ? 0.1524 0.1693 0.1936 0.0123  0.0083  -0.0121 781  THR B CA  
14759 C C   . THR B 783  ? 0.1567 0.1749 0.2001 0.0129  0.0079  -0.0125 781  THR B C   
14760 O O   . THR B 783  ? 0.1543 0.1733 0.1973 0.0142  0.0085  -0.0130 781  THR B O   
14761 C CB  . THR B 783  ? 0.1497 0.1644 0.1876 0.0124  0.0076  -0.0130 781  THR B CB  
14762 O OG1 . THR B 783  ? 0.1585 0.1728 0.1948 0.0120  0.0080  -0.0125 781  THR B OG1 
14763 C CG2 . THR B 783  ? 0.1670 0.1799 0.2049 0.0119  0.0061  -0.0135 781  THR B CG2 
14764 N N   . GLY B 784  ? 0.1471 0.1652 0.1926 0.0122  0.0069  -0.0123 782  GLY B N   
14765 C CA  . GLY B 784  ? 0.1460 0.1661 0.1943 0.0128  0.0065  -0.0125 782  GLY B CA  
14766 C C   . GLY B 784  ? 0.1635 0.1840 0.2145 0.0115  0.0054  -0.0119 782  GLY B C   
14767 O O   . GLY B 784  ? 0.1658 0.1843 0.2159 0.0104  0.0047  -0.0118 782  GLY B O   
14768 N N   . SER B 785  ? 0.1684 0.1919 0.2228 0.0117  0.0053  -0.0116 783  SER B N   
14769 C CA  . SER B 785  ? 0.1860 0.2100 0.2431 0.0103  0.0040  -0.0112 783  SER B CA  
14770 C C   . SER B 785  ? 0.1947 0.2194 0.2531 0.0086  0.0047  -0.0100 783  SER B C   
14771 O O   . SER B 785  ? 0.1754 0.2018 0.2341 0.0086  0.0064  -0.0091 783  SER B O   
14772 C CB  . SER B 785  ? 0.1956 0.2233 0.2565 0.0110  0.0035  -0.0111 783  SER B CB  
14773 O OG  . SER B 785  ? 0.1916 0.2235 0.2549 0.0115  0.0053  -0.0103 783  SER B OG  
14774 N N   . THR B 786  ? 0.1903 0.2132 0.2492 0.0070  0.0032  -0.0098 784  THR B N   
14775 C CA  . THR B 786  ? 0.1946 0.2172 0.2545 0.0052  0.0035  -0.0086 784  THR B CA  
14776 C C   . THR B 786  ? 0.1856 0.2130 0.2497 0.0045  0.0045  -0.0073 784  THR B C   
14777 O O   . THR B 786  ? 0.2113 0.2394 0.2758 0.0035  0.0058  -0.0061 784  THR B O   
14778 C CB  . THR B 786  ? 0.2064 0.2260 0.2659 0.0038  0.0014  -0.0090 784  THR B CB  
14779 O OG1 . THR B 786  ? 0.2355 0.2514 0.2913 0.0047  0.0007  -0.0102 784  THR B OG1 
14780 C CG2 . THR B 786  ? 0.2745 0.2925 0.3342 0.0020  0.0016  -0.0079 784  THR B CG2 
14781 N N   . GLU B 787  ? 0.2210 0.2518 0.2881 0.0050  0.0040  -0.0075 785  GLU B N   
14782 C CA  . GLU B 787  ? 0.2057 0.2420 0.2773 0.0044  0.0050  -0.0062 785  GLU B CA  
14783 C C   . GLU B 787  ? 0.1961 0.2348 0.2671 0.0055  0.0076  -0.0056 785  GLU B C   
14784 O O   . GLU B 787  ? 0.2028 0.2441 0.2758 0.0042  0.0089  -0.0041 785  GLU B O   
14785 C CB  . GLU B 787  ? 0.2581 0.2980 0.3330 0.0054  0.0040  -0.0067 785  GLU B CB  
14786 N N   . VAL B 788  ? 0.1759 0.2134 0.2440 0.0078  0.0083  -0.0068 786  VAL B N   
14787 C CA  . VAL B 788  ? 0.1839 0.2233 0.2509 0.0091  0.0106  -0.0064 786  VAL B CA  
14788 C C   . VAL B 788  ? 0.1554 0.1921 0.2197 0.0079  0.0114  -0.0056 786  VAL B C   
14789 O O   . VAL B 788  ? 0.1724 0.2114 0.2371 0.0076  0.0132  -0.0044 786  VAL B O   
14790 C CB  . VAL B 788  ? 0.1952 0.2332 0.2594 0.0117  0.0107  -0.0080 786  VAL B CB  
14791 C CG1 . VAL B 788  ? 0.1758 0.2146 0.2377 0.0128  0.0129  -0.0079 786  VAL B CG1 
14792 C CG2 . VAL B 788  ? 0.1971 0.2384 0.2642 0.0132  0.0102  -0.0086 786  VAL B CG2 
14793 N N   . ALA B 789  ? 0.1616 0.1936 0.2232 0.0073  0.0101  -0.0061 787  ALA B N   
14794 C CA  . ALA B 789  ? 0.1558 0.1852 0.2149 0.0064  0.0106  -0.0053 787  ALA B CA  
14795 C C   . ALA B 789  ? 0.1531 0.1840 0.2147 0.0043  0.0111  -0.0035 787  ALA B C   
14796 O O   . ALA B 789  ? 0.1720 0.2028 0.2323 0.0039  0.0125  -0.0023 787  ALA B O   
14797 C CB  . ALA B 789  ? 0.1422 0.1668 0.1986 0.0062  0.0090  -0.0062 787  ALA B CB  
14798 N N   . ARG B 790  ? 0.1702 0.2022 0.2350 0.0027  0.0099  -0.0031 788  ARG B N   
14799 C CA  . ARG B 790  ? 0.1711 0.2044 0.2383 0.0003  0.0102  -0.0012 788  ARG B CA  
14800 C C   . ARG B 790  ? 0.1935 0.2320 0.2628 0.0004  0.0125  0.0002  788  ARG B C   
14801 O O   . ARG B 790  ? 0.2077 0.2465 0.2771 -0.0012 0.0135  0.0020  788  ARG B O   
14802 C CB  . ARG B 790  ? 0.2380 0.2722 0.3087 -0.0015 0.0084  -0.0011 788  ARG B CB  
14803 C CG  . ARG B 790  ? 0.2737 0.3027 0.3425 -0.0022 0.0061  -0.0020 788  ARG B CG  
14804 C CD  . ARG B 790  ? 0.3227 0.3529 0.3950 -0.0045 0.0044  -0.0016 788  ARG B CD  
14805 N NE  . ARG B 790  ? 0.4276 0.4531 0.4978 -0.0046 0.0020  -0.0030 788  ARG B NE  
14806 C CZ  . ARG B 790  ? 0.4196 0.4396 0.4868 -0.0055 0.0011  -0.0031 788  ARG B CZ  
14807 N NH1 . ARG B 790  ? 0.3671 0.3852 0.4331 -0.0066 0.0020  -0.0018 788  ARG B NH1 
14808 N NH2 . ARG B 790  ? 0.4758 0.4920 0.5409 -0.0053 -0.0009 -0.0046 788  ARG B NH2 
14809 N N   . LEU B 791  ? 0.1887 0.2313 0.2595 0.0023  0.0134  -0.0005 789  LEU B N   
14810 C CA  . LEU B 791  ? 0.1889 0.2368 0.2614 0.0028  0.0158  0.0006  789  LEU B CA  
14811 C C   . LEU B 791  ? 0.1933 0.2395 0.2618 0.0036  0.0175  0.0010  789  LEU B C   
14812 O O   . LEU B 791  ? 0.2008 0.2494 0.2697 0.0027  0.0192  0.0027  789  LEU B O   
14813 C CB  . LEU B 791  ? 0.1830 0.2351 0.2574 0.0052  0.0163  -0.0006 789  LEU B CB  
14814 C CG  . LEU B 791  ? 0.2431 0.2977 0.3217 0.0047  0.0146  -0.0009 789  LEU B CG  
14815 C CD1 . LEU B 791  ? 0.2236 0.2817 0.3034 0.0077  0.0152  -0.0022 789  LEU B CD1 
14816 C CD2 . LEU B 791  ? 0.2564 0.3151 0.3396 0.0018  0.0148  0.0012  789  LEU B CD2 
14817 N N   . ILE B 792  ? 0.1850 0.2271 0.2494 0.0053  0.0169  -0.0006 790  ILE B N   
14818 C CA  . ILE B 792  ? 0.1878 0.2281 0.2482 0.0061  0.0182  -0.0004 790  ILE B CA  
14819 C C   . ILE B 792  ? 0.1748 0.2124 0.2341 0.0041  0.0180  0.0013  790  ILE B C   
14820 O O   . ILE B 792  ? 0.1903 0.2287 0.2482 0.0038  0.0196  0.0027  790  ILE B O   
14821 C CB  . ILE B 792  ? 0.1555 0.1921 0.2123 0.0079  0.0172  -0.0024 790  ILE B CB  
14822 C CG1 . ILE B 792  ? 0.1674 0.2064 0.2246 0.0101  0.0176  -0.0039 790  ILE B CG1 
14823 C CG2 . ILE B 792  ? 0.1764 0.2106 0.2290 0.0084  0.0179  -0.0021 790  ILE B CG2 
14824 C CD1 . ILE B 792  ? 0.1752 0.2105 0.2293 0.0115  0.0163  -0.0058 790  ILE B CD1 
14825 N N   . GLN B 793  ? 0.1715 0.2055 0.2311 0.0027  0.0161  0.0012  791  GLN B N   
14826 C CA  . GLN B 793  ? 0.1805 0.2111 0.2389 0.0009  0.0156  0.0027  791  GLN B CA  
14827 C C   . GLN B 793  ? 0.1894 0.2230 0.2502 -0.0012 0.0168  0.0050  791  GLN B C   
14828 O O   . GLN B 793  ? 0.1986 0.2308 0.2575 -0.0020 0.0177  0.0066  791  GLN B O   
14829 C CB  . GLN B 793  ? 0.1971 0.2238 0.2558 -0.0001 0.0133  0.0019  791  GLN B CB  
14830 C CG  . GLN B 793  ? 0.2188 0.2412 0.2761 -0.0018 0.0125  0.0031  791  GLN B CG  
14831 C CD  . GLN B 793  ? 0.2582 0.2778 0.3167 -0.0033 0.0103  0.0026  791  GLN B CD  
14832 O OE1 . GLN B 793  ? 0.2672 0.2895 0.3291 -0.0042 0.0097  0.0024  791  GLN B OE1 
14833 N NE2 . GLN B 793  ? 0.2923 0.3063 0.3479 -0.0034 0.0090  0.0024  791  GLN B NE2 
14834 N N   . ALA B 794  ? 0.2016 0.2397 0.2668 -0.0021 0.0170  0.0054  792  ALA B N   
14835 C CA  . ALA B 794  ? 0.2196 0.2615 0.2876 -0.0044 0.0183  0.0078  792  ALA B CA  
14836 C C   . ALA B 794  ? 0.2133 0.2587 0.2800 -0.0032 0.0210  0.0087  792  ALA B C   
14837 O O   . ALA B 794  ? 0.2368 0.2824 0.3030 -0.0049 0.0221  0.0110  792  ALA B O   
14838 C CB  . ALA B 794  ? 0.2448 0.2916 0.3181 -0.0055 0.0178  0.0078  792  ALA B CB  
14839 N N   . GLN B 795  ? 0.1995 0.2473 0.2653 -0.0004 0.0220  0.0071  793  GLN B N   
14840 C CA  . GLN B 795  ? 0.2108 0.2613 0.2746 0.0010  0.0245  0.0077  793  GLN B CA  
14841 C C   . GLN B 795  ? 0.2049 0.2509 0.2641 0.0007  0.0246  0.0086  793  GLN B C   
14842 O O   . GLN B 795  ? 0.2206 0.2682 0.2787 -0.0001 0.0263  0.0105  793  GLN B O   
14843 C CB  . GLN B 795  ? 0.2597 0.3114 0.3220 0.0042  0.0250  0.0053  793  GLN B CB  
14844 C CG  . GLN B 795  ? 0.3004 0.3572 0.3664 0.0055  0.0254  0.0044  793  GLN B CG  
14845 C CD  . GLN B 795  ? 0.3314 0.3880 0.3948 0.0089  0.0258  0.0021  793  GLN B CD  
14846 O OE1 . GLN B 795  ? 0.3267 0.3796 0.3887 0.0099  0.0240  0.0002  793  GLN B OE1 
14847 N NE2 . GLN B 795  ? 0.2772 0.3374 0.3397 0.0105  0.0281  0.0022  793  GLN B NE2 
14848 N N   . LEU B 796  ? 0.1915 0.2322 0.2479 0.0014  0.0228  0.0073  794  LEU B N   
14849 C CA  . LEU B 796  ? 0.1910 0.2277 0.2430 0.0017  0.0228  0.0079  794  LEU B CA  
14850 C C   . LEU B 796  ? 0.2222 0.2566 0.2742 -0.0008 0.0226  0.0103  794  LEU B C   
14851 O O   . LEU B 796  ? 0.2429 0.2760 0.2918 -0.0008 0.0234  0.0118  794  LEU B O   
14852 C CB  . LEU B 796  ? 0.1804 0.2126 0.2299 0.0031  0.0210  0.0059  794  LEU B CB  
14853 C CG  . LEU B 796  ? 0.1942 0.2276 0.2423 0.0056  0.0212  0.0037  794  LEU B CG  
14854 C CD1 . LEU B 796  ? 0.1955 0.2245 0.2413 0.0064  0.0193  0.0021  794  LEU B CD1 
14855 C CD2 . LEU B 796  ? 0.1886 0.2238 0.2338 0.0068  0.0230  0.0040  794  LEU B CD2 
14856 N N   . ALA B 797  ? 0.2237 0.2572 0.2787 -0.0029 0.0213  0.0109  795  ALA B N   
14857 C CA  . ALA B 797  ? 0.2545 0.2847 0.3091 -0.0055 0.0207  0.0131  795  ALA B CA  
14858 C C   . ALA B 797  ? 0.2868 0.3207 0.3423 -0.0072 0.0228  0.0158  795  ALA B C   
14859 O O   . ALA B 797  ? 0.3108 0.3418 0.3650 -0.0091 0.0226  0.0180  795  ALA B O   
14860 C CB  . ALA B 797  ? 0.2686 0.2970 0.3262 -0.0075 0.0187  0.0128  795  ALA B CB  
14861 N N   . ASP B 798  ? 0.2702 0.3105 0.3277 -0.0064 0.0248  0.0157  796  ASP B N   
14862 C CA  . ASP B 798  ? 0.3147 0.3592 0.3728 -0.0077 0.0271  0.0183  796  ASP B CA  
14863 C C   . ASP B 798  ? 0.3141 0.3569 0.3671 -0.0063 0.0284  0.0189  796  ASP B C   
14864 O O   . ASP B 798  ? 0.3533 0.3978 0.4055 -0.0077 0.0301  0.0214  796  ASP B O   
14865 C CB  . ASP B 798  ? 0.2920 0.3442 0.3537 -0.0069 0.0290  0.0178  796  ASP B CB  
14866 N N   . ARG B 799  ? 0.2558 0.2951 0.3053 -0.0037 0.0275  0.0169  797  ARG B N   
14867 C CA  . ARG B 799  ? 0.3319 0.3705 0.3768 -0.0020 0.0285  0.0171  797  ARG B CA  
14868 C C   . ARG B 799  ? 0.2928 0.3248 0.3341 -0.0019 0.0267  0.0175  797  ARG B C   
14869 O O   . ARG B 799  ? 0.2569 0.2849 0.2989 -0.0024 0.0246  0.0167  797  ARG B O   
14870 C CB  . ARG B 799  ? 0.3540 0.3946 0.3976 0.0010  0.0290  0.0144  797  ARG B CB  
14871 C CG  . ARG B 799  ? 0.4296 0.4765 0.4764 0.0017  0.0307  0.0137  797  ARG B CG  
14872 C CD  . ARG B 799  ? 0.3892 0.4377 0.4329 0.0047  0.0318  0.0118  797  ARG B CD  
14873 N NE  . ARG B 799  ? 0.3764 0.4223 0.4194 0.0066  0.0300  0.0089  797  ARG B NE  
14874 C CZ  . ARG B 799  ? 0.4205 0.4626 0.4595 0.0078  0.0290  0.0078  797  ARG B CZ  
14875 N NH1 . ARG B 799  ? 0.3659 0.4064 0.4012 0.0078  0.0294  0.0091  797  ARG B NH1 
14876 N NH2 . ARG B 799  ? 0.3527 0.3928 0.3913 0.0091  0.0274  0.0054  797  ARG B NH2 
14877 N N   . LEU B 800  ? 0.2769 0.3080 0.3141 -0.0011 0.0275  0.0185  798  LEU B N   
14878 C CA  . LEU B 800  ? 0.2729 0.2986 0.3062 -0.0001 0.0260  0.0186  798  LEU B CA  
14879 C C   . LEU B 800  ? 0.2940 0.3210 0.3236 0.0023  0.0267  0.0176  798  LEU B C   
14880 O O   . LEU B 800  ? 0.3024 0.3338 0.3317 0.0028  0.0287  0.0176  798  LEU B O   
14881 C CB  . LEU B 800  ? 0.2984 0.3209 0.3300 -0.0020 0.0259  0.0217  798  LEU B CB  
14882 C CG  . LEU B 800  ? 0.3174 0.3371 0.3516 -0.0047 0.0248  0.0230  798  LEU B CG  
14883 C CD1 . LEU B 800  ? 0.3775 0.3940 0.4092 -0.0066 0.0250  0.0263  798  LEU B CD1 
14884 C CD2 . LEU B 800  ? 0.2718 0.2868 0.3062 -0.0038 0.0223  0.0210  798  LEU B CD2 
14885 N N   . SER B 801  ? 0.2931 0.3165 0.3201 0.0038  0.0251  0.0165  799  SER B N   
14886 C CA  . SER B 801  ? 0.3068 0.3309 0.3299 0.0058  0.0254  0.0159  799  SER B CA  
14887 C C   . SER B 801  ? 0.3572 0.3813 0.3772 0.0051  0.0266  0.0187  799  SER B C   
14888 O O   . SER B 801  ? 0.3594 0.3820 0.3801 0.0032  0.0269  0.0211  799  SER B O   
14889 C CB  . SER B 801  ? 0.3262 0.3465 0.3475 0.0072  0.0232  0.0148  799  SER B CB  
14890 O OG  . SER B 801  ? 0.3114 0.3278 0.3313 0.0065  0.0224  0.0169  799  SER B OG  
14891 N N   . PRO B 802  ? 0.3861 0.4118 0.4025 0.0066  0.0274  0.0185  800  PRO B N   
14892 C CA  . PRO B 802  ? 0.4094 0.4346 0.4222 0.0062  0.0283  0.0212  800  PRO B CA  
14893 C C   . PRO B 802  ? 0.3979 0.4180 0.4090 0.0058  0.0266  0.0230  800  PRO B C   
14894 O O   . PRO B 802  ? 0.4224 0.4414 0.4315 0.0046  0.0273  0.0259  800  PRO B O   
14895 C CB  . PRO B 802  ? 0.3860 0.4132 0.3949 0.0082  0.0288  0.0199  800  PRO B CB  
14896 C CG  . PRO B 802  ? 0.3933 0.4233 0.4045 0.0091  0.0292  0.0169  800  PRO B CG  
14897 C CD  . PRO B 802  ? 0.3346 0.3625 0.3498 0.0086  0.0276  0.0158  800  PRO B CD  
14898 N N   . ALA B 803  ? 0.3842 0.4012 0.3959 0.0068  0.0245  0.0215  801  ALA B N   
14899 C CA  . ALA B 803  ? 0.3890 0.4010 0.3996 0.0067  0.0227  0.0230  801  ALA B CA  
14900 C C   . ALA B 803  ? 0.3910 0.4004 0.4045 0.0045  0.0224  0.0242  801  ALA B C   
14901 O O   . ALA B 803  ? 0.4517 0.4561 0.4641 0.0044  0.0210  0.0254  801  ALA B O   
14902 C CB  . ALA B 803  ? 0.4148 0.4251 0.4252 0.0088  0.0207  0.0207  801  ALA B CB  
14903 N N   . GLY B 804  ? 0.3371 0.3495 0.3541 0.0028  0.0237  0.0240  802  GLY B N   
14904 C CA  . GLY B 804  ? 0.3461 0.3562 0.3659 0.0004  0.0233  0.0252  802  GLY B CA  
14905 C C   . GLY B 804  ? 0.3316 0.3387 0.3537 0.0007  0.0213  0.0231  802  GLY B C   
14906 O O   . GLY B 804  ? 0.3413 0.3441 0.3640 -0.0008 0.0201  0.0242  802  GLY B O   
14907 N N   . ARG B 805  ? 0.3300 0.3391 0.3532 0.0025  0.0209  0.0203  803  ARG B N   
14908 C CA  . ARG B 805  ? 0.2796 0.2861 0.3045 0.0030  0.0191  0.0182  803  ARG B CA  
14909 C C   . ARG B 805  ? 0.2595 0.2698 0.2879 0.0028  0.0195  0.0161  803  ARG B C   
14910 O O   . ARG B 805  ? 0.2573 0.2722 0.2862 0.0032  0.0210  0.0156  803  ARG B O   
14911 C CB  . ARG B 805  ? 0.3194 0.3240 0.3418 0.0057  0.0177  0.0169  803  ARG B CB  
14912 C CG  . ARG B 805  ? 0.3776 0.3782 0.3965 0.0063  0.0170  0.0189  803  ARG B CG  
14913 C CD  . ARG B 805  ? 0.4286 0.4238 0.4478 0.0048  0.0159  0.0203  803  ARG B CD  
14914 N NE  . ARG B 805  ? 0.4753 0.4662 0.4909 0.0056  0.0151  0.0223  803  ARG B NE  
14915 C CZ  . ARG B 805  ? 0.3928 0.3821 0.4067 0.0040  0.0158  0.0253  803  ARG B CZ  
14916 N NH1 . ARG B 805  ? 0.4138 0.4058 0.4295 0.0013  0.0174  0.0266  803  ARG B NH1 
14917 N NH2 . ARG B 805  ? 0.4932 0.4784 0.5035 0.0051  0.0149  0.0270  803  ARG B NH2 
14918 N N   . PRO B 806  ? 0.2521 0.2605 0.2828 0.0024  0.0181  0.0147  804  PRO B N   
14919 C CA  . PRO B 806  ? 0.2271 0.2389 0.2611 0.0023  0.0183  0.0127  804  PRO B CA  
14920 C C   . PRO B 806  ? 0.2082 0.2227 0.2412 0.0045  0.0187  0.0106  804  PRO B C   
14921 O O   . PRO B 806  ? 0.2277 0.2406 0.2582 0.0062  0.0179  0.0098  804  PRO B O   
14922 C CB  . PRO B 806  ? 0.2465 0.2547 0.2819 0.0018  0.0164  0.0117  804  PRO B CB  
14923 C CG  . PRO B 806  ? 0.2938 0.2971 0.3276 0.0007  0.0156  0.0137  804  PRO B CG  
14924 C CD  . PRO B 806  ? 0.2844 0.2872 0.3146 0.0020  0.0163  0.0149  804  PRO B CD  
14925 N N   . ILE B 807  ? 0.1997 0.2185 0.2349 0.0045  0.0198  0.0097  805  ILE B N   
14926 C CA  . ILE B 807  ? 0.1956 0.2165 0.2300 0.0063  0.0199  0.0075  805  ILE B CA  
14927 C C   . ILE B 807  ? 0.1979 0.2166 0.2333 0.0068  0.0181  0.0055  805  ILE B C   
14928 O O   . ILE B 807  ? 0.1970 0.2157 0.2354 0.0057  0.0176  0.0051  805  ILE B O   
14929 C CB  . ILE B 807  ? 0.1891 0.2145 0.2254 0.0063  0.0215  0.0071  805  ILE B CB  
14930 C CG1 . ILE B 807  ? 0.2523 0.2802 0.2877 0.0057  0.0235  0.0092  805  ILE B CG1 
14931 C CG2 . ILE B 807  ? 0.2020 0.2286 0.2371 0.0082  0.0214  0.0047  805  ILE B CG2 
14932 C CD1 . ILE B 807  ? 0.2885 0.3159 0.3196 0.0070  0.0240  0.0096  805  ILE B CD1 
14933 N N   . PRO B 808  ? 0.1723 0.1897 0.2055 0.0083  0.0172  0.0042  806  PRO B N   
14934 C CA  . PRO B 808  ? 0.1818 0.1974 0.2158 0.0088  0.0157  0.0024  806  PRO B CA  
14935 C C   . PRO B 808  ? 0.1870 0.2049 0.2231 0.0088  0.0157  0.0008  806  PRO B C   
14936 O O   . PRO B 808  ? 0.1681 0.1886 0.2038 0.0094  0.0167  0.0002  806  PRO B O   
14937 C CB  . PRO B 808  ? 0.1917 0.2066 0.2228 0.0103  0.0151  0.0017  806  PRO B CB  
14938 C CG  . PRO B 808  ? 0.2427 0.2575 0.2715 0.0105  0.0157  0.0035  806  PRO B CG  
14939 C CD  . PRO B 808  ? 0.1809 0.1981 0.2107 0.0095  0.0174  0.0046  806  PRO B CD  
14940 N N   . LEU B 809  ? 0.1583 0.1748 0.1964 0.0082  0.0146  0.0000  807  LEU B N   
14941 C CA  . LEU B 809  ? 0.1673 0.1852 0.2072 0.0083  0.0143  -0.0016 807  LEU B CA  
14942 C C   . LEU B 809  ? 0.1534 0.1689 0.1926 0.0088  0.0127  -0.0030 807  LEU B C   
14943 O O   . LEU B 809  ? 0.1713 0.1842 0.2106 0.0083  0.0118  -0.0027 807  LEU B O   
14944 C CB  . LEU B 809  ? 0.1650 0.1842 0.2084 0.0069  0.0144  -0.0009 807  LEU B CB  
14945 C CG  . LEU B 809  ? 0.1630 0.1833 0.2085 0.0070  0.0136  -0.0023 807  LEU B CG  
14946 C CD1 . LEU B 809  ? 0.1678 0.1909 0.2130 0.0084  0.0146  -0.0034 807  LEU B CD1 
14947 C CD2 . LEU B 809  ? 0.1996 0.2212 0.2487 0.0053  0.0135  -0.0014 807  LEU B CD2 
14948 N N   . ILE B 810  ? 0.1475 0.1638 0.1857 0.0098  0.0125  -0.0045 808  ILE B N   
14949 C CA  . ILE B 810  ? 0.1581 0.1728 0.1961 0.0100  0.0112  -0.0059 808  ILE B CA  
14950 C C   . ILE B 810  ? 0.1533 0.1691 0.1935 0.0097  0.0109  -0.0067 808  ILE B C   
14951 O O   . ILE B 810  ? 0.1676 0.1854 0.2080 0.0102  0.0116  -0.0071 808  ILE B O   
14952 C CB  . ILE B 810  ? 0.1514 0.1661 0.1869 0.0110  0.0109  -0.0068 808  ILE B CB  
14953 C CG1 . ILE B 810  ? 0.1613 0.1758 0.1949 0.0115  0.0112  -0.0059 808  ILE B CG1 
14954 C CG2 . ILE B 810  ? 0.1924 0.2057 0.2278 0.0111  0.0096  -0.0080 808  ILE B CG2 
14955 C CD1 . ILE B 810  ? 0.1709 0.1859 0.2024 0.0122  0.0108  -0.0068 808  ILE B CD1 
14956 N N   . ALA B 811  ? 0.1599 0.1745 0.2017 0.0089  0.0098  -0.0069 809  ALA B N   
14957 C CA  . ALA B 811  ? 0.1469 0.1626 0.1910 0.0086  0.0094  -0.0075 809  ALA B CA  
14958 C C   . ALA B 811  ? 0.1778 0.1914 0.2212 0.0086  0.0079  -0.0087 809  ALA B C   
14959 O O   . ALA B 811  ? 0.1709 0.1824 0.2145 0.0079  0.0069  -0.0086 809  ALA B O   
14960 C CB  . ALA B 811  ? 0.1766 0.1936 0.2237 0.0073  0.0096  -0.0063 809  ALA B CB  
14961 N N   . GLU B 812  ? 0.1471 0.1610 0.1895 0.0094  0.0076  -0.0098 810  GLU B N   
14962 C CA  . GLU B 812  ? 0.1579 0.1699 0.1992 0.0095  0.0063  -0.0109 810  GLU B CA  
14963 C C   . GLU B 812  ? 0.1672 0.1800 0.2103 0.0094  0.0055  -0.0114 810  GLU B C   
14964 O O   . GLU B 812  ? 0.1748 0.1891 0.2182 0.0101  0.0060  -0.0117 810  GLU B O   
14965 C CB  . GLU B 812  ? 0.1811 0.1927 0.2196 0.0102  0.0064  -0.0115 810  GLU B CB  
14966 C CG  . GLU B 812  ? 0.1772 0.1887 0.2143 0.0104  0.0071  -0.0109 810  GLU B CG  
14967 C CD  . GLU B 812  ? 0.1874 0.1969 0.2243 0.0102  0.0065  -0.0107 810  GLU B CD  
14968 O OE1 . GLU B 812  ? 0.2012 0.2096 0.2368 0.0103  0.0057  -0.0115 810  GLU B OE1 
14969 O OE2 . GLU B 812  ? 0.2052 0.2142 0.2431 0.0098  0.0067  -0.0098 810  GLU B OE2 
14970 N N   . THR B 813  ? 0.1605 0.1722 0.2048 0.0086  0.0043  -0.0115 811  THR B N   
14971 C CA  . THR B 813  ? 0.1527 0.1658 0.1996 0.0083  0.0036  -0.0116 811  THR B CA  
14972 C C   . THR B 813  ? 0.1585 0.1699 0.2045 0.0083  0.0019  -0.0126 811  THR B C   
14973 O O   . THR B 813  ? 0.1632 0.1728 0.2064 0.0088  0.0017  -0.0133 811  THR B O   
14974 C CB  . THR B 813  ? 0.1615 0.1758 0.2113 0.0071  0.0037  -0.0105 811  THR B CB  
14975 O OG1 . THR B 813  ? 0.1624 0.1739 0.2110 0.0063  0.0032  -0.0103 811  THR B OG1 
14976 C CG2 . THR B 813  ? 0.1986 0.2154 0.2493 0.0074  0.0056  -0.0095 811  THR B CG2 
14977 N N   . GLY B 814  ? 0.1704 0.1823 0.2187 0.0077  0.0008  -0.0126 812  GLY B N   
14978 C CA  . GLY B 814  ? 0.1820 0.1927 0.2294 0.0079  -0.0008 -0.0134 812  GLY B CA  
14979 C C   . GLY B 814  ? 0.1749 0.1824 0.2199 0.0073  -0.0019 -0.0140 812  GLY B C   
14980 O O   . GLY B 814  ? 0.1964 0.2025 0.2403 0.0069  -0.0015 -0.0138 812  GLY B O   
14981 N N   . GLY B 815  ? 0.1788 0.1852 0.2227 0.0075  -0.0033 -0.0147 813  GLY B N   
14982 C CA  . GLY B 815  ? 0.1685 0.1721 0.2098 0.0070  -0.0044 -0.0153 813  GLY B CA  
14983 C C   . GLY B 815  ? 0.1701 0.1732 0.2121 0.0066  -0.0064 -0.0157 813  GLY B C   
14984 O O   . GLY B 815  ? 0.2048 0.2099 0.2491 0.0069  -0.0070 -0.0155 813  GLY B O   
14985 N N   . GLN B 816  ? 0.1615 0.1621 0.2016 0.0060  -0.0075 -0.0162 814  GLN B N   
14986 C CA  . GLN B 816  ? 0.1714 0.1710 0.2110 0.0056  -0.0096 -0.0167 814  GLN B CA  
14987 C C   . GLN B 816  ? 0.1496 0.1462 0.1847 0.0059  -0.0099 -0.0176 814  GLN B C   
14988 O O   . GLN B 816  ? 0.1795 0.1739 0.2129 0.0054  -0.0108 -0.0182 814  GLN B O   
14989 C CB  . GLN B 816  ? 0.1669 0.1665 0.2089 0.0042  -0.0110 -0.0166 814  GLN B CB  
14990 C CG  . GLN B 816  ? 0.1764 0.1759 0.2187 0.0038  -0.0133 -0.0170 814  GLN B CG  
14991 C CD  . GLN B 816  ? 0.1758 0.1784 0.2208 0.0045  -0.0136 -0.0165 814  GLN B CD  
14992 O OE1 . GLN B 816  ? 0.1962 0.1985 0.2393 0.0057  -0.0133 -0.0166 814  GLN B OE1 
14993 N NE2 . GLN B 816  ? 0.1863 0.1921 0.2358 0.0039  -0.0141 -0.0158 814  GLN B NE2 
14994 N N   . ASN B 817  ? 0.1456 0.1423 0.1786 0.0066  -0.0092 -0.0176 815  ASN B N   
14995 C CA  . ASN B 817  ? 0.1479 0.1429 0.1771 0.0070  -0.0086 -0.0181 815  ASN B CA  
14996 C C   . ASN B 817  ? 0.1586 0.1516 0.1848 0.0068  -0.0101 -0.0187 815  ASN B C   
14997 O O   . ASN B 817  ? 0.1712 0.1643 0.1974 0.0068  -0.0112 -0.0186 815  ASN B O   
14998 C CB  . ASN B 817  ? 0.1664 0.1626 0.1947 0.0075  -0.0071 -0.0177 815  ASN B CB  
14999 C CG  . ASN B 817  ? 0.1494 0.1475 0.1804 0.0077  -0.0058 -0.0171 815  ASN B CG  
15000 O OD1 . ASN B 817  ? 0.1519 0.1503 0.1839 0.0077  -0.0050 -0.0170 815  ASN B OD1 
15001 N ND2 . ASN B 817  ? 0.1498 0.1492 0.1819 0.0081  -0.0056 -0.0168 815  ASN B ND2 
15002 N N   . ALA B 818  ? 0.1580 0.1491 0.1814 0.0069  -0.0100 -0.0194 816  ALA B N   
15003 C CA  . ALA B 818  ? 0.1558 0.1449 0.1758 0.0068  -0.0114 -0.0201 816  ALA B CA  
15004 C C   . ALA B 818  ? 0.1434 0.1324 0.1598 0.0073  -0.0102 -0.0203 816  ALA B C   
15005 O O   . ALA B 818  ? 0.1603 0.1505 0.1766 0.0078  -0.0084 -0.0201 816  ALA B O   
15006 C CB  . ALA B 818  ? 0.1705 0.1573 0.1897 0.0065  -0.0125 -0.0210 816  ALA B CB  
15007 N N   . MET B 819  ? 0.1560 0.1437 0.1693 0.0072  -0.0112 -0.0205 817  MET B N   
15008 C CA  . MET B 819  ? 0.1637 0.1512 0.1730 0.0075  -0.0102 -0.0207 817  MET B CA  
15009 C C   . MET B 819  ? 0.1657 0.1508 0.1716 0.0075  -0.0116 -0.0217 817  MET B C   
15010 O O   . MET B 819  ? 0.1803 0.1641 0.1860 0.0070  -0.0136 -0.0217 817  MET B O   
15011 C CB  . MET B 819  ? 0.1684 0.1568 0.1766 0.0070  -0.0101 -0.0198 817  MET B CB  
15012 C CG  . MET B 819  ? 0.1951 0.1837 0.1992 0.0071  -0.0090 -0.0198 817  MET B CG  
15013 S SD  . MET B 819  ? 0.2141 0.2028 0.2162 0.0061  -0.0092 -0.0186 817  MET B SD  
15014 C CE  . MET B 819  ? 0.2281 0.2192 0.2333 0.0059  -0.0076 -0.0178 817  MET B CE  
15015 N N   . ILE B 820  ? 0.1670 0.1514 0.1702 0.0083  -0.0106 -0.0226 818  ILE B N   
15016 C CA  . ILE B 820  ? 0.1698 0.1517 0.1691 0.0086  -0.0117 -0.0237 818  ILE B CA  
15017 C C   . ILE B 820  ? 0.1680 0.1507 0.1632 0.0089  -0.0107 -0.0235 818  ILE B C   
15018 O O   . ILE B 820  ? 0.1884 0.1735 0.1835 0.0094  -0.0087 -0.0231 818  ILE B O   
15019 C CB  . ILE B 820  ? 0.1784 0.1585 0.1770 0.0096  -0.0114 -0.0249 818  ILE B CB  
15020 C CG1 . ILE B 820  ? 0.1923 0.1714 0.1947 0.0089  -0.0126 -0.0249 818  ILE B CG1 
15021 C CG2 . ILE B 820  ? 0.1986 0.1758 0.1922 0.0101  -0.0125 -0.0263 818  ILE B CG2 
15022 C CD1 . ILE B 820  ? 0.2199 0.1964 0.2216 0.0096  -0.0125 -0.0260 818  ILE B CD1 
15023 N N   . VAL B 821  ? 0.1882 0.1693 0.1803 0.0084  -0.0123 -0.0237 819  VAL B N   
15024 C CA  . VAL B 821  ? 0.2033 0.1851 0.1913 0.0083  -0.0115 -0.0232 819  VAL B CA  
15025 C C   . VAL B 821  ? 0.1976 0.1769 0.1808 0.0089  -0.0124 -0.0246 819  VAL B C   
15026 O O   . VAL B 821  ? 0.2157 0.1924 0.1983 0.0085  -0.0147 -0.0252 819  VAL B O   
15027 C CB  . VAL B 821  ? 0.1918 0.1736 0.1799 0.0071  -0.0127 -0.0219 819  VAL B CB  
15028 C CG1 . VAL B 821  ? 0.2214 0.2036 0.2048 0.0067  -0.0119 -0.0212 819  VAL B CG1 
15029 C CG2 . VAL B 821  ? 0.1907 0.1744 0.1832 0.0067  -0.0120 -0.0208 819  VAL B CG2 
15030 N N   . ASP B 822  ? 0.1991 0.1793 0.1791 0.0100  -0.0106 -0.0252 820  ASP B N   
15031 C CA  . ASP B 822  ? 0.2187 0.1965 0.1934 0.0108  -0.0112 -0.0265 820  ASP B CA  
15032 C C   . ASP B 822  ? 0.2443 0.2228 0.2148 0.0101  -0.0111 -0.0257 820  ASP B C   
15033 O O   . ASP B 822  ? 0.2293 0.2099 0.2008 0.0090  -0.0105 -0.0240 820  ASP B O   
15034 C CB  . ASP B 822  ? 0.2257 0.2032 0.1991 0.0127  -0.0098 -0.0281 820  ASP B CB  
15035 C CG  . ASP B 822  ? 0.2514 0.2327 0.2236 0.0137  -0.0068 -0.0277 820  ASP B CG  
15036 O OD1 . ASP B 822  ? 0.2254 0.2094 0.1969 0.0127  -0.0059 -0.0262 820  ASP B OD1 
15037 O OD2 . ASP B 822  ? 0.2499 0.2315 0.2217 0.0155  -0.0055 -0.0288 820  ASP B OD2 
15038 N N   . SER B 823  ? 0.2358 0.2122 0.2010 0.0109  -0.0116 -0.0269 821  SER B N   
15039 C CA  . SER B 823  ? 0.2447 0.2214 0.2053 0.0102  -0.0116 -0.0261 821  SER B CA  
15040 C C   . SER B 823  ? 0.2687 0.2494 0.2278 0.0105  -0.0085 -0.0252 821  SER B C   
15041 O O   . SER B 823  ? 0.3036 0.2851 0.2590 0.0096  -0.0082 -0.0241 821  SER B O   
15042 C CB  . SER B 823  ? 0.2559 0.2291 0.2109 0.0109  -0.0131 -0.0277 821  SER B CB  
15043 O OG  . SER B 823  ? 0.3051 0.2780 0.2579 0.0129  -0.0116 -0.0296 821  SER B OG  
15044 N N   . SER B 824  ? 0.2274 0.2110 0.1893 0.0115  -0.0064 -0.0254 822  SER B N   
15045 C CA  . SER B 824  ? 0.2347 0.2229 0.1959 0.0115  -0.0036 -0.0244 822  SER B CA  
15046 C C   . SER B 824  ? 0.2627 0.2535 0.2278 0.0096  -0.0031 -0.0223 822  SER B C   
15047 O O   . SER B 824  ? 0.2643 0.2589 0.2287 0.0089  -0.0011 -0.0210 822  SER B O   
15048 C CB  . SER B 824  ? 0.2483 0.2387 0.2101 0.0138  -0.0014 -0.0257 822  SER B CB  
15049 O OG  . SER B 824  ? 0.2266 0.2178 0.1939 0.0140  -0.0012 -0.0255 822  SER B OG  
15050 N N   . ALA B 825  ? 0.2234 0.2123 0.1923 0.0087  -0.0048 -0.0219 823  ALA B N   
15051 C CA  . ALA B 825  ? 0.2318 0.2227 0.2044 0.0072  -0.0044 -0.0201 823  ALA B CA  
15052 C C   . ALA B 825  ? 0.2520 0.2424 0.2217 0.0053  -0.0050 -0.0184 823  ALA B C   
15053 O O   . ALA B 825  ? 0.2638 0.2516 0.2298 0.0051  -0.0065 -0.0185 823  ALA B O   
15054 C CB  . ALA B 825  ? 0.2437 0.2325 0.2206 0.0071  -0.0061 -0.0203 823  ALA B CB  
15055 N N   . LEU B 826  ? 0.2625 0.2553 0.2339 0.0038  -0.0040 -0.0168 824  LEU B N   
15056 C CA  . LEU B 826  ? 0.2526 0.2446 0.2214 0.0018  -0.0046 -0.0150 824  LEU B CA  
15057 C C   . LEU B 826  ? 0.2554 0.2438 0.2262 0.0011  -0.0070 -0.0145 824  LEU B C   
15058 O O   . LEU B 826  ? 0.2453 0.2342 0.2204 0.0010  -0.0070 -0.0143 824  LEU B O   
15059 C CB  . LEU B 826  ? 0.2987 0.2946 0.2682 0.0003  -0.0025 -0.0134 824  LEU B CB  
15060 C CG  . LEU B 826  ? 0.3708 0.3656 0.3372 -0.0022 -0.0030 -0.0113 824  LEU B CG  
15061 C CD1 . LEU B 826  ? 0.4098 0.4035 0.3706 -0.0022 -0.0033 -0.0112 824  LEU B CD1 
15062 C CD2 . LEU B 826  ? 0.4583 0.4574 0.4258 -0.0039 -0.0010 -0.0098 824  LEU B CD2 
15063 N N   . ALA B 827  ? 0.2617 0.2467 0.2294 0.0008  -0.0091 -0.0142 825  ALA B N   
15064 C CA  . ALA B 827  ? 0.2279 0.2097 0.1977 0.0008  -0.0116 -0.0140 825  ALA B CA  
15065 C C   . ALA B 827  ? 0.2519 0.2337 0.2240 -0.0005 -0.0115 -0.0125 825  ALA B C   
15066 O O   . ALA B 827  ? 0.2318 0.2128 0.2079 0.0001  -0.0123 -0.0128 825  ALA B O   
15067 C CB  . ALA B 827  ? 0.2459 0.2244 0.2114 0.0005  -0.0138 -0.0136 825  ALA B CB  
15068 N N   . GLU B 828  ? 0.2505 0.2330 0.2200 -0.0022 -0.0104 -0.0109 826  GLU B N   
15069 C CA  . GLU B 828  ? 0.2522 0.2339 0.2232 -0.0036 -0.0105 -0.0096 826  GLU B CA  
15070 C C   . GLU B 828  ? 0.2492 0.2337 0.2252 -0.0030 -0.0092 -0.0103 826  GLU B C   
15071 O O   . GLU B 828  ? 0.2415 0.2245 0.2200 -0.0031 -0.0100 -0.0101 826  GLU B O   
15072 C CB  . GLU B 828  ? 0.2930 0.2755 0.2603 -0.0059 -0.0095 -0.0077 826  GLU B CB  
15073 C CG  . GLU B 828  ? 0.3214 0.3003 0.2837 -0.0068 -0.0111 -0.0064 826  GLU B CG  
15074 C CD  . GLU B 828  ? 0.3273 0.3068 0.2857 -0.0061 -0.0109 -0.0070 826  GLU B CD  
15075 O OE1 . GLU B 828  ? 0.3422 0.3248 0.3018 -0.0047 -0.0095 -0.0086 826  GLU B OE1 
15076 O OE2 . GLU B 828  ? 0.3725 0.3493 0.3264 -0.0070 -0.0121 -0.0058 826  GLU B OE2 
15077 N N   . GLN B 829  ? 0.2259 0.2141 0.2029 -0.0023 -0.0072 -0.0112 827  GLN B N   
15078 C CA  . GLN B 829  ? 0.2296 0.2204 0.2110 -0.0018 -0.0060 -0.0118 827  GLN B CA  
15079 C C   . GLN B 829  ? 0.2319 0.2212 0.2168 -0.0001 -0.0072 -0.0131 827  GLN B C   
15080 O O   . GLN B 829  ? 0.2149 0.2041 0.2031 0.0000  -0.0073 -0.0130 827  GLN B O   
15081 C CB  . GLN B 829  ? 0.2910 0.2862 0.2725 -0.0012 -0.0037 -0.0123 827  GLN B CB  
15082 N N   . VAL B 830  ? 0.2187 0.2066 0.2027 0.0011  -0.0081 -0.0142 828  VAL B N   
15083 C CA  . VAL B 830  ? 0.1998 0.1863 0.1870 0.0024  -0.0095 -0.0152 828  VAL B CA  
15084 C C   . VAL B 830  ? 0.2191 0.2033 0.2078 0.0020  -0.0112 -0.0144 828  VAL B C   
15085 O O   . VAL B 830  ? 0.2040 0.1885 0.1965 0.0026  -0.0113 -0.0147 828  VAL B O   
15086 C CB  . VAL B 830  ? 0.2001 0.1849 0.1853 0.0032  -0.0107 -0.0163 828  VAL B CB  
15087 C CG1 . VAL B 830  ? 0.2220 0.2053 0.2105 0.0040  -0.0125 -0.0170 828  VAL B CG1 
15088 C CG2 . VAL B 830  ? 0.2268 0.2134 0.2107 0.0041  -0.0091 -0.0174 828  VAL B CG2 
15089 N N   . VAL B 831  ? 0.2155 0.1972 0.2009 0.0012  -0.0125 -0.0134 829  VAL B N   
15090 C CA  . VAL B 831  ? 0.1926 0.1717 0.1790 0.0012  -0.0143 -0.0128 829  VAL B CA  
15091 C C   . VAL B 831  ? 0.2162 0.1958 0.2048 0.0007  -0.0134 -0.0123 829  VAL B C   
15092 O O   . VAL B 831  ? 0.2144 0.1934 0.2061 0.0017  -0.0141 -0.0126 829  VAL B O   
15093 C CB  . VAL B 831  ? 0.2059 0.1819 0.1877 0.0005  -0.0160 -0.0117 829  VAL B CB  
15094 C CG1 . VAL B 831  ? 0.2165 0.1895 0.1988 0.0005  -0.0176 -0.0108 829  VAL B CG1 
15095 C CG2 . VAL B 831  ? 0.2290 0.2041 0.2094 0.0013  -0.0175 -0.0125 829  VAL B CG2 
15096 N N   . GLY B 832  ? 0.2104 0.1912 0.1973 -0.0007 -0.0119 -0.0115 830  GLY B N   
15097 C CA  . GLY B 832  ? 0.2001 0.1813 0.1889 -0.0013 -0.0112 -0.0111 830  GLY B CA  
15098 C C   . GLY B 832  ? 0.2016 0.1853 0.1949 -0.0001 -0.0102 -0.0122 830  GLY B C   
15099 O O   . GLY B 832  ? 0.2224 0.2054 0.2180 0.0004  -0.0105 -0.0123 830  GLY B O   
15100 N N   . ASP B 833  ? 0.1858 0.1722 0.1802 0.0006  -0.0090 -0.0130 831  ASP B N   
15101 C CA  . ASP B 833  ? 0.2177 0.2063 0.2161 0.0017  -0.0081 -0.0140 831  ASP B CA  
15102 C C   . ASP B 833  ? 0.1944 0.1817 0.1955 0.0031  -0.0095 -0.0146 831  ASP B C   
15103 O O   . ASP B 833  ? 0.1925 0.1808 0.1970 0.0037  -0.0090 -0.0150 831  ASP B O   
15104 C CB  . ASP B 833  ? 0.2093 0.2007 0.2078 0.0022  -0.0066 -0.0146 831  ASP B CB  
15105 C CG  . ASP B 833  ? 0.1979 0.1919 0.1948 0.0011  -0.0049 -0.0139 831  ASP B CG  
15106 O OD1 . ASP B 833  ? 0.2346 0.2284 0.2312 -0.0002 -0.0049 -0.0130 831  ASP B OD1 
15107 O OD2 . ASP B 833  ? 0.2261 0.2223 0.2221 0.0015  -0.0038 -0.0143 831  ASP B OD2 
15108 N N   . VAL B 834  ? 0.1866 0.1719 0.1864 0.0034  -0.0111 -0.0148 832  VAL B N   
15109 C CA  . VAL B 834  ? 0.1936 0.1782 0.1962 0.0045  -0.0126 -0.0153 832  VAL B CA  
15110 C C   . VAL B 834  ? 0.1954 0.1787 0.1991 0.0048  -0.0133 -0.0147 832  VAL B C   
15111 O O   . VAL B 834  ? 0.1935 0.1776 0.2008 0.0057  -0.0134 -0.0151 832  VAL B O   
15112 C CB  . VAL B 834  ? 0.1830 0.1660 0.1837 0.0047  -0.0144 -0.0156 832  VAL B CB  
15113 C CG1 . VAL B 834  ? 0.1951 0.1775 0.1986 0.0056  -0.0162 -0.0157 832  VAL B CG1 
15114 C CG2 . VAL B 834  ? 0.2148 0.1990 0.2151 0.0049  -0.0137 -0.0165 832  VAL B CG2 
15115 N N   . ILE B 835  ? 0.1969 0.1778 0.1974 0.0040  -0.0139 -0.0138 833  ILE B N   
15116 C CA  . ILE B 835  ? 0.2340 0.2128 0.2350 0.0044  -0.0148 -0.0134 833  ILE B CA  
15117 C C   . ILE B 835  ? 0.2306 0.2110 0.2340 0.0046  -0.0133 -0.0136 833  ILE B C   
15118 O O   . ILE B 835  ? 0.2580 0.2386 0.2643 0.0059  -0.0135 -0.0140 833  ILE B O   
15119 C CB  . ILE B 835  ? 0.2390 0.2144 0.2355 0.0033  -0.0158 -0.0122 833  ILE B CB  
15120 C CG1 . ILE B 835  ? 0.2952 0.2688 0.2895 0.0036  -0.0177 -0.0120 833  ILE B CG1 
15121 C CG2 . ILE B 835  ? 0.2926 0.2654 0.2892 0.0038  -0.0164 -0.0119 833  ILE B CG2 
15122 C CD1 . ILE B 835  ? 0.3320 0.3017 0.3218 0.0027  -0.0188 -0.0107 833  ILE B CD1 
15123 N N   . THR B 836  ? 0.2030 0.1849 0.2055 0.0033  -0.0117 -0.0135 834  THR B N   
15124 C CA  . THR B 836  ? 0.2083 0.1919 0.2129 0.0034  -0.0103 -0.0137 834  THR B CA  
15125 C C   . THR B 836  ? 0.2265 0.2125 0.2352 0.0048  -0.0097 -0.0146 834  THR B C   
15126 O O   . THR B 836  ? 0.2774 0.2638 0.2884 0.0057  -0.0094 -0.0148 834  THR B O   
15127 C CB  . THR B 836  ? 0.2356 0.2212 0.2387 0.0019  -0.0087 -0.0133 834  THR B CB  
15128 O OG1 . THR B 836  ? 0.3041 0.2877 0.3036 0.0002  -0.0092 -0.0123 834  THR B OG1 
15129 C CG2 . THR B 836  ? 0.2744 0.2622 0.2797 0.0019  -0.0074 -0.0136 834  THR B CG2 
15130 N N   . SER B 837  ? 0.1792 0.1669 0.1888 0.0050  -0.0094 -0.0150 835  SER B N   
15131 C CA  . SER B 837  ? 0.1760 0.1659 0.1892 0.0060  -0.0087 -0.0157 835  SER B CA  
15132 C C   . SER B 837  ? 0.1736 0.1632 0.1895 0.0071  -0.0099 -0.0159 835  SER B C   
15133 O O   . SER B 837  ? 0.1825 0.1739 0.2017 0.0078  -0.0093 -0.0161 835  SER B O   
15134 C CB  . SER B 837  ? 0.1811 0.1722 0.1941 0.0059  -0.0083 -0.0161 835  SER B CB  
15135 O OG  . SER B 837  ? 0.1806 0.1728 0.1915 0.0051  -0.0070 -0.0159 835  SER B OG  
15136 N N   . ALA B 838  ? 0.1746 0.1624 0.1894 0.0073  -0.0117 -0.0158 836  ALA B N   
15137 C CA  . ALA B 838  ? 0.1764 0.1647 0.1941 0.0083  -0.0130 -0.0160 836  ALA B CA  
15138 C C   . ALA B 838  ? 0.1837 0.1709 0.2019 0.0094  -0.0136 -0.0157 836  ALA B C   
15139 O O   . ALA B 838  ? 0.2091 0.1980 0.2308 0.0106  -0.0138 -0.0159 836  ALA B O   
15140 C CB  . ALA B 838  ? 0.1727 0.1598 0.1890 0.0082  -0.0149 -0.0160 836  ALA B CB  
15141 N N   . PHE B 839  ? 0.2057 0.1900 0.2204 0.0090  -0.0140 -0.0152 837  PHE B N   
15142 C CA  . PHE B 839  ? 0.2230 0.2053 0.2375 0.0102  -0.0151 -0.0150 837  PHE B CA  
15143 C C   . PHE B 839  ? 0.2456 0.2263 0.2587 0.0102  -0.0142 -0.0149 837  PHE B C   
15144 O O   . PHE B 839  ? 0.2508 0.2301 0.2643 0.0116  -0.0147 -0.0151 837  PHE B O   
15145 C CB  . PHE B 839  ? 0.2294 0.2085 0.2407 0.0101  -0.0171 -0.0144 837  PHE B CB  
15146 C CG  . PHE B 839  ? 0.2173 0.1977 0.2297 0.0103  -0.0184 -0.0145 837  PHE B CG  
15147 C CD1 . PHE B 839  ? 0.2130 0.1959 0.2296 0.0116  -0.0191 -0.0149 837  PHE B CD1 
15148 C CD2 . PHE B 839  ? 0.2460 0.2252 0.2551 0.0090  -0.0189 -0.0143 837  PHE B CD2 
15149 C CE1 . PHE B 839  ? 0.2032 0.1872 0.2209 0.0114  -0.0205 -0.0151 837  PHE B CE1 
15150 C CE2 . PHE B 839  ? 0.2441 0.2241 0.2538 0.0091  -0.0203 -0.0145 837  PHE B CE2 
15151 C CZ  . PHE B 839  ? 0.2260 0.2083 0.2400 0.0102  -0.0212 -0.0150 837  PHE B CZ  
15152 N N   . ASP B 840  ? 0.2512 0.2322 0.2626 0.0086  -0.0128 -0.0148 838  ASP B N   
15153 C CA  . ASP B 840  ? 0.2644 0.2444 0.2749 0.0084  -0.0119 -0.0149 838  ASP B CA  
15154 C C   . ASP B 840  ? 0.2691 0.2514 0.2833 0.0100  -0.0111 -0.0156 838  ASP B C   
15155 O O   . ASP B 840  ? 0.2377 0.2233 0.2551 0.0105  -0.0104 -0.0158 838  ASP B O   
15156 C CB  . ASP B 840  ? 0.3506 0.3319 0.3597 0.0064  -0.0105 -0.0146 838  ASP B CB  
15157 C CG  . ASP B 840  ? 0.4280 0.4086 0.4360 0.0058  -0.0098 -0.0146 838  ASP B CG  
15158 O OD1 . ASP B 840  ? 0.4711 0.4533 0.4814 0.0068  -0.0089 -0.0152 838  ASP B OD1 
15159 O OD2 . ASP B 840  ? 0.5268 0.5051 0.5314 0.0041  -0.0101 -0.0140 838  ASP B OD2 
15160 N N   . SER B 841  ? 0.2419 0.2221 0.2551 0.0109  -0.0111 -0.0158 839  SER B N   
15161 C CA  . SER B 841  ? 0.2408 0.2230 0.2570 0.0128  -0.0103 -0.0165 839  SER B CA  
15162 C C   . SER B 841  ? 0.2119 0.1962 0.2317 0.0145  -0.0109 -0.0166 839  SER B C   
15163 O O   . SER B 841  ? 0.1903 0.1780 0.2136 0.0157  -0.0099 -0.0169 839  SER B O   
15164 C CB  . SER B 841  ? 0.2615 0.2470 0.2795 0.0121  -0.0083 -0.0167 839  SER B CB  
15165 O OG  . SER B 841  ? 0.2900 0.2740 0.3050 0.0104  -0.0079 -0.0165 839  SER B OG  
15166 N N   . ALA B 842  ? 0.1969 0.1796 0.2158 0.0147  -0.0127 -0.0162 840  ALA B N   
15167 C CA  . ALA B 842  ? 0.1772 0.1621 0.1994 0.0161  -0.0137 -0.0162 840  ALA B CA  
15168 C C   . ALA B 842  ? 0.1762 0.1656 0.2021 0.0154  -0.0127 -0.0163 840  ALA B C   
15169 O O   . ALA B 842  ? 0.1766 0.1691 0.2064 0.0166  -0.0126 -0.0164 840  ALA B O   
15170 C CB  . ALA B 842  ? 0.1991 0.1840 0.2228 0.0187  -0.0141 -0.0166 840  ALA B CB  
15171 N N   . GLY B 843  ? 0.1728 0.1623 0.1974 0.0135  -0.0118 -0.0162 841  GLY B N   
15172 C CA  . GLY B 843  ? 0.1717 0.1645 0.1992 0.0128  -0.0110 -0.0163 841  GLY B CA  
15173 C C   . GLY B 843  ? 0.1642 0.1599 0.1946 0.0133  -0.0093 -0.0165 841  GLY B C   
15174 O O   . GLY B 843  ? 0.1731 0.1715 0.2064 0.0129  -0.0087 -0.0164 841  GLY B O   
15175 N N   . GLN B 844  ? 0.1590 0.1540 0.1886 0.0142  -0.0084 -0.0167 842  GLN B N   
15176 C CA  . GLN B 844  ? 0.1623 0.1600 0.1943 0.0149  -0.0067 -0.0168 842  GLN B CA  
15177 C C   . GLN B 844  ? 0.1735 0.1713 0.2040 0.0136  -0.0052 -0.0168 842  GLN B C   
15178 O O   . GLN B 844  ? 0.1829 0.1804 0.2123 0.0139  -0.0043 -0.0170 842  GLN B O   
15179 C CB  . GLN B 844  ? 0.1604 0.1574 0.1923 0.0168  -0.0067 -0.0172 842  GLN B CB  
15180 C CG  . GLN B 844  ? 0.1585 0.1565 0.1927 0.0184  -0.0080 -0.0172 842  GLN B CG  
15181 C CD  . GLN B 844  ? 0.1671 0.1635 0.2005 0.0207  -0.0084 -0.0176 842  GLN B CD  
15182 O OE1 . GLN B 844  ? 0.1645 0.1639 0.2010 0.0226  -0.0079 -0.0178 842  GLN B OE1 
15183 N NE2 . GLN B 844  ? 0.1969 0.1885 0.2258 0.0206  -0.0092 -0.0178 842  GLN B NE2 
15184 N N   . ARG B 845  ? 0.1723 0.1706 0.2028 0.0122  -0.0052 -0.0165 843  ARG B N   
15185 C CA  A ARG B 845  ? 0.1633 0.1625 0.1931 0.0112  -0.0039 -0.0164 843  ARG B CA  
15186 C CA  B ARG B 845  ? 0.1633 0.1626 0.1932 0.0112  -0.0039 -0.0164 843  ARG B CA  
15187 C C   . ARG B 845  ? 0.1446 0.1459 0.1771 0.0109  -0.0036 -0.0162 843  ARG B C   
15188 O O   . ARG B 845  ? 0.1528 0.1539 0.1861 0.0106  -0.0047 -0.0162 843  ARG B O   
15189 C CB  A ARG B 845  ? 0.1922 0.1896 0.2188 0.0100  -0.0042 -0.0163 843  ARG B CB  
15190 C CB  B ARG B 845  ? 0.1923 0.1896 0.2187 0.0100  -0.0042 -0.0163 843  ARG B CB  
15191 C CG  A ARG B 845  ? 0.2069 0.2018 0.2303 0.0097  -0.0046 -0.0163 843  ARG B CG  
15192 C CG  B ARG B 845  ? 0.2038 0.1984 0.2271 0.0098  -0.0048 -0.0164 843  ARG B CG  
15193 C CD  A ARG B 845  ? 0.2513 0.2459 0.2722 0.0082  -0.0043 -0.0161 843  ARG B CD  
15194 C CD  B ARG B 845  ? 0.2304 0.2239 0.2507 0.0083  -0.0050 -0.0161 843  ARG B CD  
15195 N NE  A ARG B 845  ? 0.2716 0.2639 0.2893 0.0073  -0.0047 -0.0159 843  ARG B NE  
15196 N NE  B ARG B 845  ? 0.2345 0.2255 0.2517 0.0075  -0.0054 -0.0159 843  ARG B NE  
15197 C CZ  A ARG B 845  ? 0.2609 0.2506 0.2760 0.0066  -0.0059 -0.0156 843  ARG B CZ  
15198 C CZ  B ARG B 845  ? 0.2930 0.2843 0.3090 0.0067  -0.0046 -0.0158 843  ARG B CZ  
15199 N NH1 A ARG B 845  ? 0.2668 0.2560 0.2822 0.0069  -0.0069 -0.0155 843  ARG B NH1 
15200 N NH1 B ARG B 845  ? 0.2970 0.2912 0.3147 0.0067  -0.0033 -0.0159 843  ARG B NH1 
15201 N NH2 A ARG B 845  ? 0.2933 0.2808 0.3055 0.0055  -0.0063 -0.0153 843  ARG B NH2 
15202 N NH2 B ARG B 845  ? 0.3488 0.3374 0.3619 0.0058  -0.0053 -0.0156 843  ARG B NH2 
15203 N N   . CYS B 846  ? 0.1620 0.1651 0.1957 0.0108  -0.0022 -0.0160 844  CYS B N   
15204 C CA  . CYS B 846  ? 0.1619 0.1663 0.1978 0.0102  -0.0020 -0.0157 844  CYS B CA  
15205 C C   . CYS B 846  ? 0.1338 0.1365 0.1677 0.0094  -0.0027 -0.0159 844  CYS B C   
15206 O O   . CYS B 846  ? 0.1649 0.1676 0.1999 0.0090  -0.0033 -0.0159 844  CYS B O   
15207 C CB  . CYS B 846  ? 0.1731 0.1790 0.2097 0.0103  -0.0003 -0.0153 844  CYS B CB  
15208 S SG  . CYS B 846  ? 0.1690 0.1744 0.2025 0.0101  0.0006  -0.0154 844  CYS B SG  
15209 N N   . SER B 847  ? 0.1501 0.1517 0.1810 0.0092  -0.0025 -0.0161 845  SER B N   
15210 C CA  . SER B 847  ? 0.1501 0.1505 0.1787 0.0086  -0.0029 -0.0163 845  SER B CA  
15211 C C   . SER B 847  ? 0.1536 0.1523 0.1808 0.0084  -0.0045 -0.0165 845  SER B C   
15212 O O   . SER B 847  ? 0.1548 0.1525 0.1799 0.0080  -0.0048 -0.0167 845  SER B O   
15213 C CB  . SER B 847  ? 0.1546 0.1552 0.1809 0.0083  -0.0020 -0.0162 845  SER B CB  
15214 O OG  . SER B 847  ? 0.1713 0.1710 0.1966 0.0082  -0.0024 -0.0161 845  SER B OG  
15215 N N   . ALA B 848  ? 0.1548 0.1532 0.1831 0.0088  -0.0054 -0.0165 846  ALA B N   
15216 C CA  . ALA B 848  ? 0.1530 0.1494 0.1795 0.0087  -0.0070 -0.0166 846  ALA B CA  
15217 C C   . ALA B 848  ? 0.1554 0.1513 0.1818 0.0083  -0.0081 -0.0169 846  ALA B C   
15218 O O   . ALA B 848  ? 0.1571 0.1542 0.1860 0.0082  -0.0081 -0.0170 846  ALA B O   
15219 C CB  . ALA B 848  ? 0.1608 0.1572 0.1889 0.0096  -0.0080 -0.0165 846  ALA B CB  
15220 N N   . LEU B 849  ? 0.1558 0.1499 0.1792 0.0079  -0.0091 -0.0169 847  LEU B N   
15221 C CA  . LEU B 849  ? 0.1675 0.1606 0.1900 0.0076  -0.0103 -0.0173 847  LEU B CA  
15222 C C   . LEU B 849  ? 0.1567 0.1502 0.1818 0.0079  -0.0121 -0.0173 847  LEU B C   
15223 O O   . LEU B 849  ? 0.1820 0.1750 0.2070 0.0083  -0.0131 -0.0170 847  LEU B O   
15224 C CB  . LEU B 849  ? 0.1739 0.1652 0.1922 0.0071  -0.0109 -0.0173 847  LEU B CB  
15225 C CG  . LEU B 849  ? 0.1672 0.1571 0.1838 0.0069  -0.0124 -0.0178 847  LEU B CG  
15226 C CD1 . LEU B 849  ? 0.1868 0.1769 0.2037 0.0069  -0.0118 -0.0185 847  LEU B CD1 
15227 C CD2 . LEU B 849  ? 0.1854 0.1736 0.1976 0.0065  -0.0127 -0.0176 847  LEU B CD2 
15228 N N   . ARG B 850  ? 0.1582 0.1525 0.1856 0.0076  -0.0124 -0.0176 848  ARG B N   
15229 C CA  . ARG B 850  ? 0.1456 0.1409 0.1759 0.0075  -0.0141 -0.0176 848  ARG B CA  
15230 C C   . ARG B 850  ? 0.1641 0.1577 0.1927 0.0069  -0.0161 -0.0181 848  ARG B C   
15231 O O   . ARG B 850  ? 0.1741 0.1682 0.2041 0.0070  -0.0180 -0.0179 848  ARG B O   
15232 C CB  . ARG B 850  ? 0.1631 0.1608 0.1976 0.0073  -0.0133 -0.0174 848  ARG B CB  
15233 C CG  . ARG B 850  ? 0.1617 0.1611 0.1977 0.0079  -0.0113 -0.0169 848  ARG B CG  
15234 C CD  . ARG B 850  ? 0.1580 0.1579 0.1943 0.0090  -0.0115 -0.0167 848  ARG B CD  
15235 N NE  . ARG B 850  ? 0.1598 0.1614 0.1976 0.0096  -0.0096 -0.0164 848  ARG B NE  
15236 C CZ  . ARG B 850  ? 0.1584 0.1600 0.1959 0.0107  -0.0094 -0.0163 848  ARG B CZ  
15237 N NH1 . ARG B 850  ? 0.1783 0.1783 0.2142 0.0113  -0.0108 -0.0163 848  ARG B NH1 
15238 N NH2 . ARG B 850  ? 0.1628 0.1658 0.2013 0.0113  -0.0077 -0.0161 848  ARG B NH2 
15239 N N   . VAL B 851  ? 0.1644 0.1561 0.1900 0.0064  -0.0157 -0.0187 849  VAL B N   
15240 C CA  . VAL B 851  ? 0.1659 0.1557 0.1895 0.0058  -0.0175 -0.0194 849  VAL B CA  
15241 C C   . VAL B 851  ? 0.1837 0.1713 0.2022 0.0060  -0.0170 -0.0198 849  VAL B C   
15242 O O   . VAL B 851  ? 0.1835 0.1708 0.2006 0.0062  -0.0154 -0.0202 849  VAL B O   
15243 C CB  . VAL B 851  ? 0.1851 0.1747 0.2105 0.0051  -0.0178 -0.0198 849  VAL B CB  
15244 C CG1 . VAL B 851  ? 0.2233 0.2106 0.2464 0.0044  -0.0201 -0.0207 849  VAL B CG1 
15245 C CG2 . VAL B 851  ? 0.2206 0.2131 0.2514 0.0047  -0.0179 -0.0191 849  VAL B CG2 
15246 N N   . LEU B 852  ? 0.1867 0.1730 0.2023 0.0060  -0.0184 -0.0198 850  LEU B N   
15247 C CA  . LEU B 852  ? 0.1810 0.1655 0.1915 0.0060  -0.0180 -0.0201 850  LEU B CA  
15248 C C   . LEU B 852  ? 0.1732 0.1556 0.1812 0.0057  -0.0196 -0.0211 850  LEU B C   
15249 O O   . LEU B 852  ? 0.1810 0.1628 0.1895 0.0054  -0.0219 -0.0212 850  LEU B O   
15250 C CB  . LEU B 852  ? 0.1866 0.1705 0.1950 0.0061  -0.0187 -0.0192 850  LEU B CB  
15251 C CG  . LEU B 852  ? 0.1800 0.1623 0.1830 0.0059  -0.0183 -0.0193 850  LEU B CG  
15252 C CD1 . LEU B 852  ? 0.2015 0.1849 0.2034 0.0060  -0.0157 -0.0194 850  LEU B CD1 
15253 C CD2 . LEU B 852  ? 0.2091 0.1903 0.2100 0.0057  -0.0192 -0.0182 850  LEU B CD2 
15254 N N   . CYS B 853  ? 0.1756 0.1569 0.1812 0.0060  -0.0184 -0.0220 851  CYS B N   
15255 C CA  . CYS B 853  ? 0.1902 0.1690 0.1930 0.0058  -0.0198 -0.0232 851  CYS B CA  
15256 C C   . CYS B 853  ? 0.1856 0.1631 0.1827 0.0063  -0.0194 -0.0236 851  CYS B C   
15257 O O   . CYS B 853  ? 0.2032 0.1815 0.1985 0.0069  -0.0172 -0.0236 851  CYS B O   
15258 C CB  . CYS B 853  ? 0.1900 0.1680 0.1937 0.0061  -0.0188 -0.0241 851  CYS B CB  
15259 S SG  . CYS B 853  ? 0.2210 0.2011 0.2312 0.0054  -0.0188 -0.0233 851  CYS B SG  
15260 N N   . LEU B 854  ? 0.1942 0.1700 0.1884 0.0059  -0.0215 -0.0238 852  LEU B N   
15261 C CA  . LEU B 854  ? 0.2084 0.1832 0.1971 0.0062  -0.0212 -0.0238 852  LEU B CA  
15262 C C   . LEU B 854  ? 0.2013 0.1733 0.1859 0.0064  -0.0224 -0.0254 852  LEU B C   
15263 O O   . LEU B 854  ? 0.2153 0.1856 0.2005 0.0058  -0.0249 -0.0260 852  LEU B O   
15264 C CB  . LEU B 854  ? 0.2110 0.1857 0.1989 0.0056  -0.0227 -0.0226 852  LEU B CB  
15265 C CG  . LEU B 854  ? 0.1917 0.1685 0.1832 0.0055  -0.0218 -0.0212 852  LEU B CG  
15266 C CD1 . LEU B 854  ? 0.2247 0.2005 0.2150 0.0053  -0.0239 -0.0202 852  LEU B CD1 
15267 C CD2 . LEU B 854  ? 0.2316 0.2096 0.2216 0.0057  -0.0191 -0.0207 852  LEU B CD2 
15268 N N   . GLN B 855  ? 0.2121 0.1835 0.1924 0.0072  -0.0207 -0.0261 853  GLN B N   
15269 C CA  . GLN B 855  ? 0.2150 0.1833 0.1904 0.0076  -0.0218 -0.0278 853  GLN B CA  
15270 C C   . GLN B 855  ? 0.2560 0.2229 0.2285 0.0069  -0.0244 -0.0275 853  GLN B C   
15271 O O   . GLN B 855  ? 0.2338 0.2019 0.2056 0.0065  -0.0242 -0.0260 853  GLN B O   
15272 C CB  . GLN B 855  ? 0.2217 0.1904 0.1927 0.0089  -0.0193 -0.0284 853  GLN B CB  
15273 C CG  . GLN B 855  ? 0.2671 0.2324 0.2332 0.0098  -0.0202 -0.0305 853  GLN B CG  
15274 C CD  . GLN B 855  ? 0.2996 0.2656 0.2614 0.0115  -0.0175 -0.0312 853  GLN B CD  
15275 O OE1 . GLN B 855  ? 0.3121 0.2809 0.2762 0.0123  -0.0150 -0.0308 853  GLN B OE1 
15276 N NE2 . GLN B 855  ? 0.3387 0.3026 0.2944 0.0122  -0.0181 -0.0324 853  GLN B NE2 
15277 N N   . GLU B 856  ? 0.2443 0.2083 0.2151 0.0066  -0.0269 -0.0288 854  GLU B N   
15278 C CA  . GLU B 856  ? 0.2683 0.2311 0.2376 0.0057  -0.0299 -0.0285 854  GLU B CA  
15279 C C   . GLU B 856  ? 0.2592 0.2217 0.2229 0.0060  -0.0295 -0.0278 854  GLU B C   
15280 O O   . GLU B 856  ? 0.2861 0.2490 0.2498 0.0054  -0.0311 -0.0265 854  GLU B O   
15281 C CB  . GLU B 856  ? 0.3117 0.2711 0.2791 0.0053  -0.0326 -0.0302 854  GLU B CB  
15282 N N   . ASP B 857  ? 0.2798 0.2420 0.2388 0.0069  -0.0273 -0.0285 855  ASP B N   
15283 C CA  . ASP B 857  ? 0.3105 0.2723 0.2635 0.0071  -0.0269 -0.0280 855  ASP B CA  
15284 C C   . ASP B 857  ? 0.2934 0.2579 0.2477 0.0065  -0.0254 -0.0257 855  ASP B C   
15285 O O   . ASP B 857  ? 0.3328 0.2969 0.2828 0.0061  -0.0257 -0.0247 855  ASP B O   
15286 C CB  . ASP B 857  ? 0.3952 0.3565 0.3431 0.0084  -0.0248 -0.0295 855  ASP B CB  
15287 N N   . VAL B 858  ? 0.2387 0.2057 0.1985 0.0064  -0.0239 -0.0249 856  VAL B N   
15288 C CA  . VAL B 858  ? 0.2458 0.2148 0.2069 0.0057  -0.0226 -0.0228 856  VAL B CA  
15289 C C   . VAL B 858  ? 0.1971 0.1664 0.1634 0.0051  -0.0242 -0.0217 856  VAL B C   
15290 O O   . VAL B 858  ? 0.2302 0.2006 0.1975 0.0046  -0.0236 -0.0201 856  VAL B O   
15291 C CB  . VAL B 858  ? 0.2500 0.2219 0.2121 0.0061  -0.0191 -0.0225 856  VAL B CB  
15292 C CG1 . VAL B 858  ? 0.2958 0.2681 0.2525 0.0068  -0.0174 -0.0233 856  VAL B CG1 
15293 C CG2 . VAL B 858  ? 0.2500 0.2230 0.2175 0.0067  -0.0184 -0.0235 856  VAL B CG2 
15294 N N   . ALA B 859  ? 0.2193 0.1879 0.1890 0.0052  -0.0263 -0.0226 857  ALA B N   
15295 C CA  . ALA B 859  ? 0.2336 0.2034 0.2090 0.0049  -0.0274 -0.0216 857  ALA B CA  
15296 C C   . ALA B 859  ? 0.2196 0.1886 0.1938 0.0046  -0.0290 -0.0200 857  ALA B C   
15297 O O   . ALA B 859  ? 0.2346 0.2047 0.2116 0.0046  -0.0284 -0.0188 857  ALA B O   
15298 C CB  . ALA B 859  ? 0.2384 0.2078 0.2173 0.0049  -0.0294 -0.0227 857  ALA B CB  
15299 N N   . ASP B 860  ? 0.2512 0.2181 0.2210 0.0045  -0.0312 -0.0201 858  ASP B N   
15300 C CA  . ASP B 860  ? 0.2526 0.2184 0.2212 0.0043  -0.0332 -0.0185 858  ASP B CA  
15301 C C   . ASP B 860  ? 0.2392 0.2049 0.2055 0.0039  -0.0312 -0.0169 858  ASP B C   
15302 O O   . ASP B 860  ? 0.2398 0.2053 0.2080 0.0040  -0.0318 -0.0155 858  ASP B O   
15303 C CB  . ASP B 860  ? 0.2479 0.2113 0.2115 0.0042  -0.0358 -0.0188 858  ASP B CB  
15304 C CG  . ASP B 860  ? 0.3317 0.2951 0.2980 0.0043  -0.0385 -0.0201 858  ASP B CG  
15305 O OD1 . ASP B 860  ? 0.3854 0.3507 0.3579 0.0044  -0.0390 -0.0200 858  ASP B OD1 
15306 O OD2 . ASP B 860  ? 0.3966 0.3581 0.3585 0.0041  -0.0402 -0.0211 858  ASP B OD2 
15307 N N   . ARG B 861  ? 0.2349 0.2008 0.1971 0.0036  -0.0289 -0.0171 859  ARG B N   
15308 C CA  . ARG B 861  ? 0.2587 0.2248 0.2186 0.0028  -0.0271 -0.0154 859  ARG B CA  
15309 C C   . ARG B 861  ? 0.2380 0.2060 0.2030 0.0027  -0.0254 -0.0149 859  ARG B C   
15310 O O   . ARG B 861  ? 0.2457 0.2130 0.2108 0.0022  -0.0253 -0.0133 859  ARG B O   
15311 C CB  . ARG B 861  ? 0.3049 0.2716 0.2597 0.0025  -0.0249 -0.0157 859  ARG B CB  
15312 C CG  . ARG B 861  ? 0.4006 0.3681 0.3532 0.0013  -0.0230 -0.0138 859  ARG B CG  
15313 C CD  . ARG B 861  ? 0.4981 0.4663 0.4449 0.0008  -0.0212 -0.0137 859  ARG B CD  
15314 N NE  . ARG B 861  ? 0.6088 0.5784 0.5545 -0.0006 -0.0192 -0.0118 859  ARG B NE  
15315 C CZ  . ARG B 861  ? 0.5460 0.5190 0.4943 -0.0009 -0.0164 -0.0118 859  ARG B CZ  
15316 N NH1 . ARG B 861  ? 0.5015 0.4767 0.4533 0.0004  -0.0152 -0.0136 859  ARG B NH1 
15317 N NH2 . ARG B 861  ? 0.5475 0.5215 0.4949 -0.0026 -0.0150 -0.0099 859  ARG B NH2 
15318 N N   . ILE B 862  ? 0.2198 0.1900 0.1889 0.0033  -0.0240 -0.0162 860  ILE B N   
15319 C CA  . ILE B 862  ? 0.2303 0.2023 0.2042 0.0033  -0.0225 -0.0157 860  ILE B CA  
15320 C C   . ILE B 862  ? 0.2066 0.1778 0.1841 0.0037  -0.0244 -0.0151 860  ILE B C   
15321 O O   . ILE B 862  ? 0.2212 0.1924 0.2001 0.0034  -0.0238 -0.0140 860  ILE B O   
15322 C CB  . ILE B 862  ? 0.2231 0.1974 0.2002 0.0039  -0.0207 -0.0172 860  ILE B CB  
15323 C CG1 . ILE B 862  ? 0.2517 0.2272 0.2251 0.0037  -0.0183 -0.0175 860  ILE B CG1 
15324 C CG2 . ILE B 862  ? 0.2086 0.1847 0.1910 0.0040  -0.0196 -0.0169 860  ILE B CG2 
15325 C CD1 . ILE B 862  ? 0.2799 0.2570 0.2554 0.0046  -0.0168 -0.0191 860  ILE B CD1 
15326 N N   . LEU B 863  ? 0.2229 0.1936 0.2021 0.0043  -0.0268 -0.0158 861  LEU B N   
15327 C CA  . LEU B 863  ? 0.2255 0.1962 0.2086 0.0050  -0.0285 -0.0153 861  LEU B CA  
15328 C C   . LEU B 863  ? 0.2388 0.2069 0.2188 0.0049  -0.0299 -0.0137 861  LEU B C   
15329 O O   . LEU B 863  ? 0.2241 0.1919 0.2065 0.0054  -0.0301 -0.0129 861  LEU B O   
15330 C CB  . LEU B 863  ? 0.2282 0.1993 0.2137 0.0055  -0.0309 -0.0162 861  LEU B CB  
15331 C CG  . LEU B 863  ? 0.2580 0.2314 0.2476 0.0055  -0.0298 -0.0176 861  LEU B CG  
15332 C CD1 . LEU B 863  ? 0.2778 0.2511 0.2686 0.0055  -0.0323 -0.0185 861  LEU B CD1 
15333 C CD2 . LEU B 863  ? 0.2744 0.2500 0.2694 0.0059  -0.0284 -0.0172 861  LEU B CD2 
15334 N N   . THR B 864  ? 0.2252 0.1912 0.1996 0.0043  -0.0308 -0.0132 862  THR B N   
15335 C CA  . THR B 864  ? 0.2343 0.1974 0.2052 0.0041  -0.0321 -0.0115 862  THR B CA  
15336 C C   . THR B 864  ? 0.2505 0.2133 0.2210 0.0033  -0.0299 -0.0104 862  THR B C   
15337 O O   . THR B 864  ? 0.2512 0.2120 0.2222 0.0036  -0.0307 -0.0093 862  THR B O   
15338 C CB  . THR B 864  ? 0.2818 0.2428 0.2462 0.0034  -0.0330 -0.0110 862  THR B CB  
15339 O OG1 . THR B 864  ? 0.3109 0.2718 0.2755 0.0041  -0.0356 -0.0120 862  THR B OG1 
15340 C CG2 . THR B 864  ? 0.3280 0.2857 0.2882 0.0029  -0.0341 -0.0089 862  THR B CG2 
15341 N N   . MET B 865  ? 0.2143 0.1790 0.1841 0.0023  -0.0272 -0.0107 863  MET B N   
15342 C CA  . MET B 865  ? 0.2216 0.1863 0.1910 0.0012  -0.0252 -0.0097 863  MET B CA  
15343 C C   . MET B 865  ? 0.2263 0.1920 0.2011 0.0020  -0.0248 -0.0100 863  MET B C   
15344 O O   . MET B 865  ? 0.2236 0.1874 0.1981 0.0016  -0.0247 -0.0090 863  MET B O   
15345 C CB  . MET B 865  ? 0.2323 0.1997 0.2003 0.0003  -0.0224 -0.0101 863  MET B CB  
15346 C CG  . MET B 865  ? 0.2508 0.2187 0.2180 -0.0013 -0.0205 -0.0089 863  MET B CG  
15347 S SD  . MET B 865  ? 0.2771 0.2491 0.2430 -0.0021 -0.0173 -0.0093 863  MET B SD  
15348 C CE  . MET B 865  ? 0.3099 0.2807 0.2695 -0.0024 -0.0180 -0.0091 863  MET B CE  
15349 N N   . LEU B 866  ? 0.2123 0.1806 0.1917 0.0031  -0.0244 -0.0115 864  LEU B N   
15350 C CA  . LEU B 866  ? 0.2071 0.1766 0.1916 0.0039  -0.0239 -0.0118 864  LEU B CA  
15351 C C   . LEU B 866  ? 0.2194 0.1865 0.2047 0.0050  -0.0261 -0.0111 864  LEU B C   
15352 O O   . LEU B 866  ? 0.2200 0.1862 0.2064 0.0052  -0.0257 -0.0106 864  LEU B O   
15353 C CB  . LEU B 866  ? 0.2169 0.1893 0.2058 0.0048  -0.0236 -0.0133 864  LEU B CB  
15354 C CG  . LEU B 866  ? 0.2013 0.1754 0.1956 0.0058  -0.0232 -0.0137 864  LEU B CG  
15355 C CD1 . LEU B 866  ? 0.2327 0.2074 0.2275 0.0052  -0.0210 -0.0133 864  LEU B CD1 
15356 C CD2 . LEU B 866  ? 0.2364 0.2132 0.2345 0.0062  -0.0230 -0.0150 864  LEU B CD2 
15357 N N   . LYS B 867  ? 0.2141 0.1802 0.1987 0.0058  -0.0286 -0.0111 865  LYS B N   
15358 C CA  . LYS B 867  ? 0.2280 0.1922 0.2136 0.0072  -0.0308 -0.0104 865  LYS B CA  
15359 C C   . LYS B 867  ? 0.2382 0.1982 0.2193 0.0066  -0.0312 -0.0089 865  LYS B C   
15360 O O   . LYS B 867  ? 0.2296 0.1878 0.2118 0.0076  -0.0318 -0.0084 865  LYS B O   
15361 C CB  . LYS B 867  ? 0.2412 0.2056 0.2271 0.0081  -0.0335 -0.0107 865  LYS B CB  
15362 C CG  . LYS B 867  ? 0.2803 0.2486 0.2716 0.0086  -0.0333 -0.0121 865  LYS B CG  
15363 C CD  . LYS B 867  ? 0.3275 0.2962 0.3184 0.0088  -0.0358 -0.0125 865  LYS B CD  
15364 C CE  . LYS B 867  ? 0.3680 0.3403 0.3638 0.0088  -0.0355 -0.0139 865  LYS B CE  
15365 N NZ  . LYS B 867  ? 0.4185 0.3910 0.4137 0.0086  -0.0381 -0.0143 865  LYS B NZ  
15366 N N   . GLY B 868  ? 0.2321 0.1904 0.2079 0.0048  -0.0308 -0.0080 866  GLY B N   
15367 C CA  . GLY B 868  ? 0.2384 0.1927 0.2097 0.0038  -0.0310 -0.0064 866  GLY B CA  
15368 C C   . GLY B 868  ? 0.2388 0.1930 0.2114 0.0030  -0.0291 -0.0062 866  GLY B C   
15369 O O   . GLY B 868  ? 0.2567 0.2073 0.2280 0.0031  -0.0298 -0.0053 866  GLY B O   
15370 N N   . ALA B 869  ? 0.2371 0.1952 0.2124 0.0024  -0.0266 -0.0072 867  ALA B N   
15371 C CA  . ALA B 869  ? 0.2362 0.1948 0.2131 0.0017  -0.0248 -0.0072 867  ALA B CA  
15372 C C   . ALA B 869  ? 0.2213 0.1796 0.2023 0.0037  -0.0255 -0.0079 867  ALA B C   
15373 O O   . ALA B 869  ? 0.2217 0.1775 0.2022 0.0035  -0.0253 -0.0075 867  ALA B O   
15374 C CB  . ALA B 869  ? 0.2450 0.2082 0.2238 0.0008  -0.0222 -0.0081 867  ALA B CB  
15375 N N   . LEU B 870  ? 0.2092 0.1698 0.1942 0.0056  -0.0263 -0.0090 868  LEU B N   
15376 C CA  . LEU B 870  ? 0.2333 0.1942 0.2223 0.0077  -0.0267 -0.0096 868  LEU B CA  
15377 C C   . LEU B 870  ? 0.2284 0.1847 0.2152 0.0088  -0.0289 -0.0087 868  LEU B C   
15378 O O   . LEU B 870  ? 0.2418 0.1970 0.2302 0.0102  -0.0288 -0.0090 868  LEU B O   
15379 C CB  . LEU B 870  ? 0.2418 0.2065 0.2355 0.0092  -0.0274 -0.0107 868  LEU B CB  
15380 C CG  . LEU B 870  ? 0.2512 0.2201 0.2482 0.0086  -0.0253 -0.0118 868  LEU B CG  
15381 C CD1 . LEU B 870  ? 0.2678 0.2398 0.2687 0.0096  -0.0262 -0.0126 868  LEU B CD1 
15382 C CD2 . LEU B 870  ? 0.2827 0.2528 0.2822 0.0088  -0.0234 -0.0121 868  LEU B CD2 
15383 N N   . HIS B 871  ? 0.2176 0.1709 0.2003 0.0085  -0.0308 -0.0076 869  HIS B N   
15384 C CA  A HIS B 871  ? 0.2433 0.1916 0.2234 0.0098  -0.0330 -0.0067 869  HIS B CA  
15385 C CA  B HIS B 871  ? 0.2434 0.1916 0.2234 0.0097  -0.0330 -0.0066 869  HIS B CA  
15386 C C   . HIS B 871  ? 0.2577 0.2017 0.2344 0.0085  -0.0323 -0.0058 869  HIS B C   
15387 O O   . HIS B 871  ? 0.2802 0.2196 0.2552 0.0098  -0.0339 -0.0053 869  HIS B O   
15388 C CB  A HIS B 871  ? 0.2626 0.2085 0.2388 0.0096  -0.0353 -0.0056 869  HIS B CB  
15389 C CB  B HIS B 871  ? 0.2614 0.2072 0.2370 0.0092  -0.0351 -0.0055 869  HIS B CB  
15390 C CG  A HIS B 871  ? 0.3053 0.2537 0.2848 0.0118  -0.0372 -0.0062 869  HIS B CG  
15391 C CG  B HIS B 871  ? 0.2962 0.2366 0.2687 0.0106  -0.0377 -0.0043 869  HIS B CG  
15392 N ND1 A HIS B 871  ? 0.2977 0.2500 0.2788 0.0113  -0.0371 -0.0070 869  HIS B ND1 
15393 N ND1 B HIS B 871  ? 0.3573 0.2978 0.3327 0.0137  -0.0398 -0.0046 869  HIS B ND1 
15394 C CD2 A HIS B 871  ? 0.3324 0.2801 0.3140 0.0145  -0.0394 -0.0062 869  HIS B CD2 
15395 C CD2 B HIS B 871  ? 0.3490 0.2836 0.3158 0.0094  -0.0386 -0.0026 869  HIS B CD2 
15396 C CE1 A HIS B 871  ? 0.3282 0.2822 0.3123 0.0133  -0.0392 -0.0073 869  HIS B CE1 
15397 C CE1 B HIS B 871  ? 0.3221 0.2569 0.2936 0.0146  -0.0419 -0.0034 869  HIS B CE1 
15398 N NE2 A HIS B 871  ? 0.3042 0.2558 0.2889 0.0153  -0.0406 -0.0068 869  HIS B NE2 
15399 N NE2 B HIS B 871  ? 0.3677 0.2985 0.3337 0.0119  -0.0413 -0.0021 869  HIS B NE2 
15400 N N   . GLU B 872  ? 0.2255 0.1708 0.2012 0.0060  -0.0301 -0.0058 870  GLU B N   
15401 C CA  . GLU B 872  ? 0.2453 0.1868 0.2179 0.0043  -0.0296 -0.0049 870  GLU B CA  
15402 C C   . GLU B 872  ? 0.2360 0.1787 0.2120 0.0051  -0.0282 -0.0061 870  GLU B C   
15403 O O   . GLU B 872  ? 0.2524 0.1920 0.2259 0.0036  -0.0278 -0.0056 870  GLU B O   
15404 C CB  . GLU B 872  ? 0.2446 0.1872 0.2141 0.0009  -0.0280 -0.0040 870  GLU B CB  
15405 C CG  . GLU B 872  ? 0.2615 0.2028 0.2269 0.0000  -0.0292 -0.0028 870  GLU B CG  
15406 C CD  . GLU B 872  ? 0.2744 0.2090 0.2352 0.0003  -0.0317 -0.0012 870  GLU B CD  
15407 O OE1 . GLU B 872  ? 0.3130 0.2434 0.2725 0.0001  -0.0322 -0.0008 870  GLU B OE1 
15408 O OE2 . GLU B 872  ? 0.2964 0.2296 0.2546 0.0007  -0.0334 -0.0005 870  GLU B OE2 
15409 N N   . LEU B 873  ? 0.2343 0.1813 0.2156 0.0072  -0.0275 -0.0076 871  LEU B N   
15410 C CA  . LEU B 873  ? 0.2351 0.1835 0.2194 0.0080  -0.0261 -0.0087 871  LEU B CA  
15411 C C   . LEU B 873  ? 0.2513 0.1957 0.2354 0.0105  -0.0276 -0.0089 871  LEU B C   
15412 O O   . LEU B 873  ? 0.2701 0.2131 0.2544 0.0127  -0.0295 -0.0088 871  LEU B O   
15413 C CB  . LEU B 873  ? 0.2354 0.1900 0.2253 0.0091  -0.0247 -0.0100 871  LEU B CB  
15414 C CG  . LEU B 873  ? 0.2608 0.2194 0.2512 0.0071  -0.0231 -0.0100 871  LEU B CG  
15415 C CD1 . LEU B 873  ? 0.2817 0.2455 0.2776 0.0082  -0.0217 -0.0113 871  LEU B CD1 
15416 C CD2 . LEU B 873  ? 0.2475 0.2054 0.2352 0.0044  -0.0216 -0.0095 871  LEU B CD2 
15417 N N   . HIS B 874  ? 0.2457 0.1884 0.2295 0.0104  -0.0267 -0.0094 872  HIS B N   
15418 C CA  . HIS B 874  ? 0.2643 0.2033 0.2479 0.0130  -0.0277 -0.0100 872  HIS B CA  
15419 C C   . HIS B 874  ? 0.2268 0.1707 0.2156 0.0151  -0.0261 -0.0116 872  HIS B C   
15420 O O   . HIS B 874  ? 0.2311 0.1778 0.2213 0.0137  -0.0241 -0.0121 872  HIS B O   
15421 C CB  . HIS B 874  ? 0.2711 0.2041 0.2498 0.0112  -0.0280 -0.0095 872  HIS B CB  
15422 C CG  . HIS B 874  ? 0.2720 0.2001 0.2494 0.0139  -0.0291 -0.0102 872  HIS B CG  
15423 N ND1 . HIS B 874  ? 0.3598 0.2815 0.3326 0.0126  -0.0296 -0.0100 872  HIS B ND1 
15424 C CD2 . HIS B 874  ? 0.3199 0.2484 0.3000 0.0178  -0.0297 -0.0112 872  HIS B CD2 
15425 C CE1 . HIS B 874  ? 0.3509 0.2689 0.3232 0.0158  -0.0306 -0.0109 872  HIS B CE1 
15426 N NE2 . HIS B 874  ? 0.3761 0.2984 0.3530 0.0191  -0.0306 -0.0117 872  HIS B NE2 
15427 N N   . ILE B 875  ? 0.2307 0.1760 0.2226 0.0184  -0.0270 -0.0122 873  ILE B N   
15428 C CA  . ILE B 875  ? 0.2452 0.1954 0.2424 0.0206  -0.0256 -0.0135 873  ILE B CA  
15429 C C   . ILE B 875  ? 0.2479 0.1942 0.2438 0.0233  -0.0261 -0.0142 873  ILE B C   
15430 O O   . ILE B 875  ? 0.2575 0.1995 0.2512 0.0253  -0.0282 -0.0138 873  ILE B O   
15431 C CB  . ILE B 875  ? 0.2557 0.2111 0.2576 0.0223  -0.0261 -0.0136 873  ILE B CB  
15432 C CG1 . ILE B 875  ? 0.3189 0.2772 0.3212 0.0197  -0.0259 -0.0130 873  ILE B CG1 
15433 C CG2 . ILE B 875  ? 0.2701 0.2307 0.2773 0.0244  -0.0245 -0.0148 873  ILE B CG2 
15434 C CD1 . ILE B 875  ? 0.3648 0.3252 0.3691 0.0208  -0.0276 -0.0127 873  ILE B CD1 
15435 N N   . GLY B 876  ? 0.2144 0.1618 0.2113 0.0237  -0.0243 -0.0153 874  GLY B N   
15436 C CA  . GLY B 876  ? 0.2210 0.1648 0.2167 0.0266  -0.0248 -0.0162 874  GLY B CA  
15437 C C   . GLY B 876  ? 0.2163 0.1611 0.2122 0.0262  -0.0227 -0.0173 874  GLY B C   
15438 O O   . GLY B 876  ? 0.2247 0.1740 0.2229 0.0242  -0.0209 -0.0174 874  GLY B O   
15439 N N   . ARG B 877  ? 0.2452 0.1853 0.2385 0.0285  -0.0232 -0.0182 875  ARG B N   
15440 C CA  . ARG B 877  ? 0.2281 0.1681 0.2208 0.0285  -0.0215 -0.0194 875  ARG B CA  
15441 C C   . ARG B 877  ? 0.2315 0.1691 0.2207 0.0242  -0.0212 -0.0188 875  ARG B C   
15442 O O   . ARG B 877  ? 0.2509 0.1830 0.2358 0.0222  -0.0228 -0.0178 875  ARG B O   
15443 C CB  . ARG B 877  ? 0.2728 0.2069 0.2623 0.0318  -0.0225 -0.0206 875  ARG B CB  
15444 C CG  . ARG B 877  ? 0.2886 0.2242 0.2785 0.0330  -0.0206 -0.0221 875  ARG B CG  
15445 C CD  . ARG B 877  ? 0.3581 0.2879 0.3448 0.0369  -0.0216 -0.0234 875  ARG B CD  
15446 N NE  . ARG B 877  ? 0.3335 0.2542 0.3134 0.0352  -0.0231 -0.0235 875  ARG B NE  
15447 C CZ  . ARG B 877  ? 0.4107 0.3247 0.3863 0.0380  -0.0241 -0.0248 875  ARG B CZ  
15448 N NH1 . ARG B 877  ? 0.3800 0.2956 0.3576 0.0429  -0.0236 -0.0261 875  ARG B NH1 
15449 N NH2 . ARG B 877  ? 0.4262 0.3318 0.3955 0.0358  -0.0255 -0.0249 875  ARG B NH2 
15450 N N   . THR B 878  ? 0.2159 0.1579 0.2071 0.0227  -0.0192 -0.0193 876  THR B N   
15451 C CA  . THR B 878  ? 0.2357 0.1782 0.2254 0.0185  -0.0186 -0.0185 876  THR B CA  
15452 C C   . THR B 878  ? 0.2246 0.1612 0.2092 0.0166  -0.0192 -0.0187 876  THR B C   
15453 O O   . THR B 878  ? 0.2419 0.1795 0.2255 0.0132  -0.0186 -0.0181 876  THR B O   
15454 C CB  . THR B 878  ? 0.2243 0.1743 0.2187 0.0178  -0.0163 -0.0187 876  THR B CB  
15455 O OG1 . THR B 878  ? 0.2592 0.2109 0.2551 0.0202  -0.0151 -0.0200 876  THR B OG1 
15456 C CG2 . THR B 878  ? 0.2627 0.2178 0.2614 0.0184  -0.0161 -0.0181 876  THR B CG2 
15457 N N   . ASP B 879  ? 0.2231 0.1535 0.2042 0.0188  -0.0204 -0.0196 877  ASP B N   
15458 C CA  . ASP B 879  ? 0.2496 0.1737 0.2254 0.0168  -0.0212 -0.0199 877  ASP B CA  
15459 C C   . ASP B 879  ? 0.2554 0.1729 0.2264 0.0143  -0.0234 -0.0185 877  ASP B C   
15460 O O   . ASP B 879  ? 0.2752 0.1852 0.2410 0.0136  -0.0249 -0.0188 877  ASP B O   
15461 C CB  . ASP B 879  ? 0.2816 0.2016 0.2553 0.0203  -0.0214 -0.0218 877  ASP B CB  
15462 C CG  . ASP B 879  ? 0.3061 0.2216 0.2786 0.0240  -0.0231 -0.0220 877  ASP B CG  
15463 O OD1 . ASP B 879  ? 0.3444 0.2630 0.3200 0.0251  -0.0234 -0.0211 877  ASP B OD1 
15464 O OD2 . ASP B 879  ? 0.3151 0.2239 0.2834 0.0260  -0.0242 -0.0232 877  ASP B OD2 
15465 N N   . ARG B 880  ? 0.2653 0.1854 0.2378 0.0127  -0.0236 -0.0170 878  ARG B N   
15466 C CA  . ARG B 880  ? 0.2763 0.1916 0.2446 0.0097  -0.0253 -0.0153 878  ARG B CA  
15467 C C   . ARG B 880  ? 0.2325 0.1539 0.2031 0.0062  -0.0240 -0.0140 878  ARG B C   
15468 O O   . ARG B 880  ? 0.2474 0.1754 0.2227 0.0073  -0.0227 -0.0141 878  ARG B O   
15469 C CB  . ARG B 880  ? 0.3009 0.2126 0.2680 0.0119  -0.0272 -0.0145 878  ARG B CB  
15470 C CG  . ARG B 880  ? 0.3697 0.2739 0.3335 0.0152  -0.0290 -0.0155 878  ARG B CG  
15471 C CD  . ARG B 880  ? 0.4522 0.3536 0.4151 0.0172  -0.0309 -0.0144 878  ARG B CD  
15472 N NE  . ARG B 880  ? 0.6367 0.5323 0.5976 0.0215  -0.0324 -0.0155 878  ARG B NE  
15473 C CZ  . ARG B 880  ? 0.7053 0.5914 0.6601 0.0215  -0.0347 -0.0151 878  ARG B CZ  
15474 N NH1 . ARG B 880  ? 0.7278 0.6089 0.6779 0.0172  -0.0359 -0.0134 878  ARG B NH1 
15475 N NH2 . ARG B 880  ? 0.6676 0.5488 0.6208 0.0260  -0.0359 -0.0163 878  ARG B NH2 
15476 N N   . LEU B 881  ? 0.2408 0.1599 0.2080 0.0021  -0.0243 -0.0129 879  LEU B N   
15477 C CA  . LEU B 881  ? 0.2392 0.1642 0.2083 -0.0011 -0.0230 -0.0117 879  LEU B CA  
15478 C C   . LEU B 881  ? 0.2331 0.1602 0.2034 -0.0006 -0.0233 -0.0106 879  LEU B C   
15479 O O   . LEU B 881  ? 0.2435 0.1770 0.2170 -0.0014 -0.0218 -0.0103 879  LEU B O   
15480 C CB  . LEU B 881  ? 0.2576 0.1794 0.2225 -0.0055 -0.0237 -0.0104 879  LEU B CB  
15481 C CG  . LEU B 881  ? 0.2514 0.1793 0.2179 -0.0090 -0.0223 -0.0091 879  LEU B CG  
15482 C CD1 . LEU B 881  ? 0.2769 0.2123 0.2481 -0.0086 -0.0201 -0.0102 879  LEU B CD1 
15483 C CD2 . LEU B 881  ? 0.2916 0.2158 0.2537 -0.0135 -0.0232 -0.0076 879  LEU B CD2 
15484 N N   . SER B 882  ? 0.2299 0.1514 0.1974 0.0010  -0.0253 -0.0101 880  SER B N   
15485 C CA  . SER B 882  ? 0.2301 0.1530 0.1982 0.0013  -0.0258 -0.0090 880  SER B CA  
15486 C C   . SER B 882  ? 0.2465 0.1753 0.2199 0.0046  -0.0249 -0.0101 880  SER B C   
15487 O O   . SER B 882  ? 0.2608 0.1914 0.2350 0.0049  -0.0254 -0.0093 880  SER B O   
15488 C CB  . SER B 882  ? 0.2686 0.1836 0.2320 0.0022  -0.0284 -0.0081 880  SER B CB  
15489 O OG  . SER B 882  ? 0.2986 0.2111 0.2630 0.0064  -0.0292 -0.0095 880  SER B OG  
15490 N N   . VAL B 883  ? 0.2384 0.1701 0.2154 0.0069  -0.0238 -0.0117 881  VAL B N   
15491 C CA  . VAL B 883  ? 0.2464 0.1837 0.2286 0.0098  -0.0230 -0.0125 881  VAL B CA  
15492 C C   . VAL B 883  ? 0.2348 0.1792 0.2206 0.0081  -0.0210 -0.0125 881  VAL B C   
15493 O O   . VAL B 883  ? 0.2618 0.2082 0.2479 0.0064  -0.0195 -0.0128 881  VAL B O   
15494 C CB  . VAL B 883  ? 0.2508 0.1883 0.2353 0.0132  -0.0226 -0.0141 881  VAL B CB  
15495 C CG1 . VAL B 883  ? 0.2548 0.1993 0.2452 0.0153  -0.0214 -0.0148 881  VAL B CG1 
15496 C CG2 . VAL B 883  ? 0.2610 0.1920 0.2424 0.0156  -0.0247 -0.0142 881  VAL B CG2 
15497 N N   . ASP B 884  ? 0.2305 0.1782 0.2184 0.0086  -0.0211 -0.0121 882  ASP B N   
15498 C CA  . ASP B 884  ? 0.2357 0.1893 0.2266 0.0073  -0.0194 -0.0121 882  ASP B CA  
15499 C C   . ASP B 884  ? 0.2634 0.2222 0.2597 0.0096  -0.0183 -0.0133 882  ASP B C   
15500 O O   . ASP B 884  ? 0.3095 0.2726 0.3081 0.0087  -0.0165 -0.0137 882  ASP B O   
15501 C CB  . ASP B 884  ? 0.2466 0.2005 0.2363 0.0064  -0.0203 -0.0111 882  ASP B CB  
15502 C CG  . ASP B 884  ? 0.2603 0.2095 0.2446 0.0039  -0.0213 -0.0097 882  ASP B CG  
15503 O OD1 . ASP B 884  ? 0.2518 0.2012 0.2345 0.0014  -0.0203 -0.0093 882  ASP B OD1 
15504 O OD2 . ASP B 884  ? 0.2525 0.1979 0.2342 0.0045  -0.0233 -0.0089 882  ASP B OD2 
15505 N N   . VAL B 885  ? 0.2344 0.1930 0.2326 0.0124  -0.0193 -0.0137 883  VAL B N   
15506 C CA  . VAL B 885  ? 0.2263 0.1900 0.2297 0.0143  -0.0184 -0.0146 883  VAL B CA  
15507 C C   . VAL B 885  ? 0.2173 0.1799 0.2218 0.0171  -0.0186 -0.0154 883  VAL B C   
15508 O O   . VAL B 885  ? 0.2208 0.1795 0.2234 0.0189  -0.0203 -0.0153 883  VAL B O   
15509 C CB  . VAL B 885  ? 0.2458 0.2116 0.2512 0.0150  -0.0196 -0.0142 883  VAL B CB  
15510 C CG1 . VAL B 885  ? 0.2537 0.2249 0.2647 0.0167  -0.0188 -0.0150 883  VAL B CG1 
15511 C CG2 . VAL B 885  ? 0.3072 0.2738 0.3109 0.0124  -0.0194 -0.0136 883  VAL B CG2 
15512 N N   . GLY B 886  ? 0.2168 0.1826 0.2239 0.0178  -0.0168 -0.0163 884  GLY B N   
15513 C CA  . GLY B 886  ? 0.2125 0.1779 0.2207 0.0206  -0.0165 -0.0172 884  GLY B CA  
15514 C C   . GLY B 886  ? 0.1982 0.1686 0.2117 0.0230  -0.0163 -0.0175 884  GLY B C   
15515 O O   . GLY B 886  ? 0.1919 0.1653 0.2078 0.0225  -0.0168 -0.0170 884  GLY B O   
15516 N N   . PRO B 887  ? 0.1903 0.1618 0.2054 0.0255  -0.0155 -0.0184 885  PRO B N   
15517 C CA  . PRO B 887  ? 0.1856 0.1622 0.2058 0.0280  -0.0152 -0.0186 885  PRO B CA  
15518 C C   . PRO B 887  ? 0.1801 0.1630 0.2047 0.0267  -0.0133 -0.0185 885  PRO B C   
15519 O O   . PRO B 887  ? 0.1763 0.1596 0.1999 0.0246  -0.0119 -0.0185 885  PRO B O   
15520 C CB  . PRO B 887  ? 0.1845 0.1598 0.2041 0.0310  -0.0146 -0.0196 885  PRO B CB  
15521 C CG  . PRO B 887  ? 0.1846 0.1564 0.2002 0.0292  -0.0136 -0.0201 885  PRO B CG  
15522 C CD  . PRO B 887  ? 0.2121 0.1799 0.2240 0.0262  -0.0149 -0.0192 885  PRO B CD  
15523 N N   . VAL B 888  ? 0.1706 0.1585 0.2000 0.0282  -0.0133 -0.0184 886  VAL B N   
15524 C CA  . VAL B 888  ? 0.1854 0.1790 0.2191 0.0275  -0.0113 -0.0184 886  VAL B CA  
15525 C C   . VAL B 888  ? 0.1745 0.1697 0.2091 0.0298  -0.0096 -0.0192 886  VAL B C   
15526 O O   . VAL B 888  ? 0.1808 0.1735 0.2138 0.0324  -0.0101 -0.0198 886  VAL B O   
15527 C CB  . VAL B 888  ? 0.2043 0.2029 0.2430 0.0275  -0.0120 -0.0178 886  VAL B CB  
15528 C CG1 . VAL B 888  ? 0.1961 0.1927 0.2331 0.0252  -0.0137 -0.0172 886  VAL B CG1 
15529 C CG2 . VAL B 888  ? 0.2784 0.2789 0.3197 0.0306  -0.0130 -0.0179 886  VAL B CG2 
15530 N N   . ILE B 889  ? 0.1667 0.1657 0.2034 0.0288  -0.0075 -0.0191 887  ILE B N   
15531 C CA  . ILE B 889  ? 0.1695 0.1685 0.2052 0.0302  -0.0058 -0.0199 887  ILE B CA  
15532 C C   . ILE B 889  ? 0.1771 0.1793 0.2156 0.0337  -0.0053 -0.0203 887  ILE B C   
15533 O O   . ILE B 889  ? 0.1808 0.1810 0.2170 0.0359  -0.0046 -0.0213 887  ILE B O   
15534 C CB  . ILE B 889  ? 0.1629 0.1649 0.1996 0.0282  -0.0037 -0.0196 887  ILE B CB  
15535 C CG1 . ILE B 889  ? 0.1764 0.1779 0.2112 0.0295  -0.0020 -0.0204 887  ILE B CG1 
15536 C CG2 . ILE B 889  ? 0.1928 0.2011 0.2351 0.0277  -0.0030 -0.0188 887  ILE B CG2 
15537 C CD1 . ILE B 889  ? 0.2010 0.1961 0.2301 0.0296  -0.0029 -0.0212 887  ILE B CD1 
15538 N N   . THR B 890  ? 0.1524 0.1599 0.1960 0.0343  -0.0055 -0.0197 888  THR B N   
15539 C CA  . THR B 890  ? 0.1891 0.2008 0.2361 0.0376  -0.0049 -0.0200 888  THR B CA  
15540 C C   . THR B 890  ? 0.1802 0.1949 0.2311 0.0384  -0.0067 -0.0194 888  THR B C   
15541 O O   . THR B 890  ? 0.1707 0.1851 0.2223 0.0360  -0.0081 -0.0186 888  THR B O   
15542 C CB  . THR B 890  ? 0.1908 0.2092 0.2420 0.0373  -0.0023 -0.0196 888  THR B CB  
15543 O OG1 . THR B 890  ? 0.2109 0.2326 0.2654 0.0342  -0.0025 -0.0185 888  THR B OG1 
15544 C CG2 . THR B 890  ? 0.2076 0.2239 0.2553 0.0369  -0.0003 -0.0203 888  THR B CG2 
15545 N N   . SER B 891  ? 0.1881 0.2061 0.2418 0.0418  -0.0066 -0.0197 889  SER B N   
15546 C CA  A SER B 891  ? 0.1719 0.1942 0.2302 0.0428  -0.0082 -0.0190 889  SER B CA  
15547 C CA  B SER B 891  ? 0.1719 0.1941 0.2301 0.0427  -0.0082 -0.0190 889  SER B CA  
15548 C CA  C SER B 891  ? 0.1723 0.1945 0.2305 0.0428  -0.0082 -0.0190 889  SER B CA  
15549 C C   . SER B 891  ? 0.1791 0.2079 0.2427 0.0400  -0.0076 -0.0179 889  SER B C   
15550 O O   . SER B 891  ? 0.1871 0.2175 0.2531 0.0388  -0.0095 -0.0172 889  SER B O   
15551 C CB  A SER B 891  ? 0.2096 0.2352 0.2702 0.0473  -0.0078 -0.0196 889  SER B CB  
15552 C CB  B SER B 891  ? 0.2099 0.2350 0.2703 0.0473  -0.0080 -0.0196 889  SER B CB  
15553 C CB  C SER B 891  ? 0.2098 0.2351 0.2703 0.0473  -0.0079 -0.0196 889  SER B CB  
15554 O OG  A SER B 891  ? 0.2303 0.2492 0.2859 0.0501  -0.0090 -0.0206 889  SER B OG  
15555 O OG  B SER B 891  ? 0.2055 0.2367 0.2692 0.0483  -0.0052 -0.0197 889  SER B OG  
15556 O OG  C SER B 891  ? 0.2137 0.2431 0.2786 0.0484  -0.0098 -0.0189 889  SER B OG  
15557 N N   . GLU B 892  ? 0.1709 0.2034 0.2362 0.0390  -0.0050 -0.0177 890  GLU B N   
15558 C CA  . GLU B 892  ? 0.1952 0.2332 0.2652 0.0362  -0.0044 -0.0166 890  GLU B CA  
15559 C C   . GLU B 892  ? 0.1804 0.2145 0.2483 0.0326  -0.0058 -0.0161 890  GLU B C   
15560 O O   . GLU B 892  ? 0.1963 0.2331 0.2673 0.0306  -0.0071 -0.0153 890  GLU B O   
15561 C CB  . GLU B 892  ? 0.2308 0.2722 0.3019 0.0357  -0.0014 -0.0164 890  GLU B CB  
15562 N N   . ALA B 893  ? 0.1832 0.2111 0.2456 0.0316  -0.0057 -0.0167 891  ALA B N   
15563 C CA  . ALA B 893  ? 0.1768 0.2010 0.2368 0.0286  -0.0069 -0.0164 891  ALA B CA  
15564 C C   . ALA B 893  ? 0.1772 0.1996 0.2369 0.0287  -0.0097 -0.0163 891  ALA B C   
15565 O O   . ALA B 893  ? 0.1881 0.2111 0.2490 0.0265  -0.0109 -0.0158 891  ALA B O   
15566 C CB  . ALA B 893  ? 0.2064 0.2249 0.2607 0.0278  -0.0062 -0.0170 891  ALA B CB  
15567 N N   . LYS B 894  ? 0.1710 0.1907 0.2286 0.0314  -0.0108 -0.0168 892  LYS B N   
15568 C CA  A LYS B 894  ? 0.1789 0.1968 0.2360 0.0319  -0.0136 -0.0166 892  LYS B CA  
15569 C CA  B LYS B 894  ? 0.1786 0.1965 0.2358 0.0319  -0.0136 -0.0166 892  LYS B CA  
15570 C C   . LYS B 894  ? 0.1903 0.2145 0.2533 0.0316  -0.0147 -0.0159 892  LYS B C   
15571 O O   . LYS B 894  ? 0.1846 0.2081 0.2477 0.0299  -0.0166 -0.0155 892  LYS B O   
15572 C CB  A LYS B 894  ? 0.1863 0.2009 0.2409 0.0353  -0.0145 -0.0172 892  LYS B CB  
15573 C CB  B LYS B 894  ? 0.1860 0.2004 0.2405 0.0353  -0.0145 -0.0172 892  LYS B CB  
15574 C CG  A LYS B 894  ? 0.2004 0.2133 0.2546 0.0363  -0.0175 -0.0169 892  LYS B CG  
15575 C CG  B LYS B 894  ? 0.1991 0.2115 0.2528 0.0361  -0.0175 -0.0169 892  LYS B CG  
15576 C CD  A LYS B 894  ? 0.2393 0.2486 0.2909 0.0401  -0.0183 -0.0174 892  LYS B CD  
15577 C CD  B LYS B 894  ? 0.2393 0.2469 0.2895 0.0394  -0.0184 -0.0174 892  LYS B CD  
15578 C CE  A LYS B 894  ? 0.2842 0.2932 0.3365 0.0417  -0.0212 -0.0169 892  LYS B CE  
15579 C CE  B LYS B 894  ? 0.2538 0.2596 0.3034 0.0405  -0.0215 -0.0169 892  LYS B CE  
15580 N NZ  A LYS B 894  ? 0.2864 0.2905 0.3348 0.0392  -0.0233 -0.0164 892  LYS B NZ  
15581 N NZ  B LYS B 894  ? 0.3454 0.3448 0.3903 0.0432  -0.0227 -0.0173 892  LYS B NZ  
15582 N N   . ASP B 895  ? 0.1805 0.2109 0.2485 0.0333  -0.0133 -0.0157 893  ASP B N   
15583 C CA  . ASP B 895  ? 0.1876 0.2247 0.2617 0.0328  -0.0143 -0.0149 893  ASP B CA  
15584 C C   . ASP B 895  ? 0.1800 0.2183 0.2554 0.0288  -0.0143 -0.0143 893  ASP B C   
15585 O O   . ASP B 895  ? 0.1963 0.2367 0.2743 0.0274  -0.0163 -0.0137 893  ASP B O   
15586 C CB  . ASP B 895  ? 0.2199 0.2640 0.2990 0.0351  -0.0124 -0.0147 893  ASP B CB  
15587 C CG  . ASP B 895  ? 0.2399 0.2836 0.3184 0.0395  -0.0128 -0.0154 893  ASP B CG  
15588 O OD1 . ASP B 895  ? 0.2727 0.3116 0.3481 0.0407  -0.0151 -0.0157 893  ASP B OD1 
15589 O OD2 . ASP B 895  ? 0.2813 0.3296 0.3625 0.0419  -0.0108 -0.0156 893  ASP B OD2 
15590 N N   . ASN B 896  ? 0.1703 0.2071 0.2439 0.0270  -0.0122 -0.0143 894  ASN B N   
15591 C CA  . ASN B 896  ? 0.1781 0.2154 0.2525 0.0235  -0.0120 -0.0138 894  ASN B CA  
15592 C C   . ASN B 896  ? 0.1839 0.2161 0.2546 0.0217  -0.0143 -0.0140 894  ASN B C   
15593 O O   . ASN B 896  ? 0.1871 0.2205 0.2597 0.0196  -0.0159 -0.0136 894  ASN B O   
15594 C CB  . ASN B 896  ? 0.2010 0.2370 0.2734 0.0226  -0.0093 -0.0139 894  ASN B CB  
15595 C CG  . ASN B 896  ? 0.2901 0.3260 0.3629 0.0192  -0.0089 -0.0134 894  ASN B CG  
15596 O OD1 . ASN B 896  ? 0.3097 0.3421 0.3802 0.0174  -0.0105 -0.0135 894  ASN B OD1 
15597 N ND2 . ASN B 896  ? 0.3497 0.3892 0.4251 0.0185  -0.0068 -0.0127 894  ASN B ND2 
15598 N N   . ILE B 897  ? 0.1753 0.2016 0.2406 0.0226  -0.0146 -0.0147 895  ILE B N   
15599 C CA  . ILE B 897  ? 0.1790 0.2004 0.2403 0.0211  -0.0166 -0.0148 895  ILE B CA  
15600 C C   . ILE B 897  ? 0.1748 0.1976 0.2379 0.0218  -0.0194 -0.0146 895  ILE B C   
15601 O O   . ILE B 897  ? 0.1893 0.2113 0.2520 0.0198  -0.0212 -0.0144 895  ILE B O   
15602 C CB  . ILE B 897  ? 0.1814 0.1969 0.2369 0.0220  -0.0163 -0.0154 895  ILE B CB  
15603 C CG1 . ILE B 897  ? 0.1746 0.1890 0.2284 0.0210  -0.0137 -0.0156 895  ILE B CG1 
15604 C CG2 . ILE B 897  ? 0.2050 0.2159 0.2563 0.0208  -0.0183 -0.0154 895  ILE B CG2 
15605 C CD1 . ILE B 897  ? 0.1866 0.1967 0.2360 0.0224  -0.0130 -0.0161 895  ILE B CD1 
15606 N N   . GLU B 898  ? 0.1875 0.2121 0.2523 0.0247  -0.0200 -0.0146 896  GLU B N   
15607 C CA  . GLU B 898  ? 0.1802 0.2061 0.2466 0.0256  -0.0229 -0.0142 896  GLU B CA  
15608 C C   . GLU B 898  ? 0.1887 0.2207 0.2609 0.0240  -0.0237 -0.0136 896  GLU B C   
15609 O O   . GLU B 898  ? 0.1834 0.2156 0.2560 0.0232  -0.0264 -0.0134 896  GLU B O   
15610 C CB  . GLU B 898  ? 0.1991 0.2255 0.2660 0.0295  -0.0232 -0.0144 896  GLU B CB  
15611 C CG  . GLU B 898  ? 0.2257 0.2446 0.2860 0.0305  -0.0235 -0.0148 896  GLU B CG  
15612 C CD  . GLU B 898  ? 0.3180 0.3361 0.3780 0.0345  -0.0239 -0.0151 896  GLU B CD  
15613 O OE1 . GLU B 898  ? 0.3279 0.3518 0.3929 0.0367  -0.0235 -0.0150 896  GLU B OE1 
15614 O OE2 . GLU B 898  ? 0.3980 0.4096 0.4526 0.0353  -0.0248 -0.0153 896  GLU B OE2 
15615 N N   . LYS B 899  ? 0.1751 0.2121 0.2515 0.0233  -0.0216 -0.0133 897  LYS B N   
15616 C CA  . LYS B 899  ? 0.1839 0.2266 0.2658 0.0213  -0.0225 -0.0126 897  LYS B CA  
15617 C C   . LYS B 899  ? 0.1651 0.2042 0.2444 0.0178  -0.0238 -0.0127 897  LYS B C   
15618 O O   . LYS B 899  ? 0.1763 0.2172 0.2577 0.0164  -0.0262 -0.0124 897  LYS B O   
15619 C CB  . LYS B 899  ? 0.2257 0.2738 0.3120 0.0208  -0.0197 -0.0121 897  LYS B CB  
15620 C CG  . LYS B 899  ? 0.2364 0.2903 0.3283 0.0183  -0.0206 -0.0111 897  LYS B CG  
15621 C CD  . LYS B 899  ? 0.3199 0.3802 0.4166 0.0182  -0.0179 -0.0103 897  LYS B CD  
15622 C CE  . LYS B 899  ? 0.3180 0.3754 0.4123 0.0160  -0.0155 -0.0103 897  LYS B CE  
15623 N NZ  . LYS B 899  ? 0.3149 0.3787 0.4144 0.0145  -0.0137 -0.0091 897  LYS B NZ  
15624 N N   . HIS B 900  ? 0.1604 0.1943 0.2350 0.0167  -0.0224 -0.0132 898  HIS B N   
15625 C CA  . HIS B 900  ? 0.1761 0.2062 0.2477 0.0139  -0.0235 -0.0134 898  HIS B CA  
15626 C C   . HIS B 900  ? 0.1775 0.2041 0.2456 0.0142  -0.0264 -0.0138 898  HIS B C   
15627 O O   . HIS B 900  ? 0.1776 0.2041 0.2459 0.0124  -0.0285 -0.0138 898  HIS B O   
15628 C CB  . HIS B 900  ? 0.1659 0.1916 0.2331 0.0132  -0.0213 -0.0139 898  HIS B CB  
15629 C CG  . HIS B 900  ? 0.1881 0.2091 0.2511 0.0111  -0.0223 -0.0144 898  HIS B CG  
15630 N ND1 . HIS B 900  ? 0.2235 0.2450 0.2878 0.0086  -0.0230 -0.0143 898  HIS B ND1 
15631 C CD2 . HIS B 900  ? 0.1875 0.2032 0.2449 0.0112  -0.0228 -0.0150 898  HIS B CD2 
15632 C CE1 . HIS B 900  ? 0.2013 0.2180 0.2609 0.0075  -0.0238 -0.0150 898  HIS B CE1 
15633 N NE2 . HIS B 900  ? 0.1915 0.2049 0.2469 0.0090  -0.0237 -0.0153 898  HIS B NE2 
15634 N N   . ILE B 901  ? 0.1862 0.2098 0.2510 0.0165  -0.0265 -0.0140 899  ILE B N   
15635 C CA  . ILE B 901  ? 0.1899 0.2098 0.2510 0.0169  -0.0292 -0.0142 899  ILE B CA  
15636 C C   . ILE B 901  ? 0.1982 0.2222 0.2634 0.0171  -0.0319 -0.0137 899  ILE B C   
15637 O O   . ILE B 901  ? 0.1976 0.2200 0.2610 0.0156  -0.0344 -0.0138 899  ILE B O   
15638 C CB  . ILE B 901  ? 0.1846 0.2007 0.2419 0.0194  -0.0288 -0.0143 899  ILE B CB  
15639 C CG1 . ILE B 901  ? 0.1691 0.1809 0.2219 0.0186  -0.0265 -0.0147 899  ILE B CG1 
15640 C CG2 . ILE B 901  ? 0.2065 0.2194 0.2604 0.0199  -0.0318 -0.0141 899  ILE B CG2 
15641 C CD1 . ILE B 901  ? 0.2200 0.2283 0.2694 0.0208  -0.0260 -0.0148 899  ILE B CD1 
15642 N N   . GLU B 902  ? 0.2018 0.2315 0.2724 0.0189  -0.0316 -0.0132 900  GLU B N   
15643 C CA  . GLU B 902  ? 0.2017 0.2363 0.2768 0.0193  -0.0343 -0.0127 900  GLU B CA  
15644 C C   . GLU B 902  ? 0.1922 0.2300 0.2707 0.0160  -0.0352 -0.0125 900  GLU B C   
15645 O O   . GLU B 902  ? 0.2108 0.2503 0.2907 0.0152  -0.0382 -0.0122 900  GLU B O   
15646 C CB  . GLU B 902  ? 0.2152 0.2555 0.2954 0.0224  -0.0336 -0.0122 900  GLU B CB  
15647 C CG  . GLU B 902  ? 0.2953 0.3318 0.3719 0.0260  -0.0335 -0.0125 900  GLU B CG  
15648 C CD  . GLU B 902  ? 0.3564 0.3877 0.4282 0.0263  -0.0365 -0.0125 900  GLU B CD  
15649 O OE1 . GLU B 902  ? 0.3518 0.3859 0.4259 0.0260  -0.0394 -0.0121 900  GLU B OE1 
15650 O OE2 . GLU B 902  ? 0.3960 0.4207 0.4617 0.0267  -0.0361 -0.0129 900  GLU B OE2 
15651 N N   . ARG B 903  ? 0.2093 0.2477 0.2888 0.0140  -0.0329 -0.0125 901  ARG B N   
15652 C CA  . ARG B 903  ? 0.2169 0.2570 0.2986 0.0105  -0.0338 -0.0123 901  ARG B CA  
15653 C C   . ARG B 903  ? 0.2469 0.2810 0.3232 0.0087  -0.0360 -0.0130 901  ARG B C   
15654 O O   . ARG B 903  ? 0.2589 0.2942 0.3365 0.0069  -0.0387 -0.0130 901  ARG B O   
15655 C CB  . ARG B 903  ? 0.2448 0.2856 0.3278 0.0089  -0.0308 -0.0121 901  ARG B CB  
15656 C CG  . ARG B 903  ? 0.3440 0.3870 0.4300 0.0054  -0.0318 -0.0117 901  ARG B CG  
15657 C CD  . ARG B 903  ? 0.4376 0.4808 0.5245 0.0039  -0.0289 -0.0114 901  ARG B CD  
15658 N NE  . ARG B 903  ? 0.5074 0.5440 0.5889 0.0021  -0.0287 -0.0121 901  ARG B NE  
15659 C CZ  . ARG B 903  ? 0.4365 0.4715 0.5178 -0.0010 -0.0302 -0.0122 901  ARG B CZ  
15660 N NH1 . ARG B 903  ? 0.5046 0.5441 0.5908 -0.0030 -0.0321 -0.0115 901  ARG B NH1 
15661 N NH2 . ARG B 903  ? 0.5395 0.5681 0.6154 -0.0020 -0.0298 -0.0131 901  ARG B NH2 
15662 N N   . MET B 904  ? 0.2156 0.2435 0.2856 0.0092  -0.0349 -0.0137 902  MET B N   
15663 C CA  . MET B 904  ? 0.2068 0.2291 0.2712 0.0079  -0.0366 -0.0145 902  MET B CA  
15664 C C   . MET B 904  ? 0.2565 0.2787 0.3200 0.0088  -0.0399 -0.0143 902  MET B C   
15665 O O   . MET B 904  ? 0.2475 0.2682 0.3094 0.0071  -0.0424 -0.0147 902  MET B O   
15666 C CB  . MET B 904  ? 0.2115 0.2282 0.2699 0.0085  -0.0345 -0.0150 902  MET B CB  
15667 C CG  . MET B 904  ? 0.2187 0.2351 0.2774 0.0076  -0.0314 -0.0152 902  MET B CG  
15668 S SD  . MET B 904  ? 0.3346 0.3497 0.3932 0.0043  -0.0321 -0.0156 902  MET B SD  
15669 C CE  . MET B 904  ? 0.3806 0.4025 0.4470 0.0033  -0.0312 -0.0146 902  MET B CE  
15670 N N   . ARG B 905  ? 0.2263 0.2496 0.2904 0.0117  -0.0400 -0.0139 903  ARG B N   
15671 C CA  . ARG B 905  ? 0.2353 0.2586 0.2986 0.0129  -0.0433 -0.0136 903  ARG B CA  
15672 C C   . ARG B 905  ? 0.2753 0.3042 0.3441 0.0117  -0.0459 -0.0132 903  ARG B C   
15673 O O   . ARG B 905  ? 0.2753 0.3030 0.3423 0.0106  -0.0490 -0.0133 903  ARG B O   
15674 C CB  . ARG B 905  ? 0.2747 0.2985 0.3383 0.0164  -0.0428 -0.0132 903  ARG B CB  
15675 C CG  . ARG B 905  ? 0.3823 0.4031 0.4423 0.0180  -0.0458 -0.0129 903  ARG B CG  
15676 C CD  . ARG B 905  ? 0.3830 0.4049 0.4443 0.0217  -0.0456 -0.0124 903  ARG B CD  
15677 N NE  . ARG B 905  ? 0.3424 0.3615 0.4016 0.0228  -0.0424 -0.0126 903  ARG B NE  
15678 C CZ  . ARG B 905  ? 0.3067 0.3193 0.3595 0.0232  -0.0418 -0.0128 903  ARG B CZ  
15679 N NH1 . ARG B 905  ? 0.3741 0.3820 0.4215 0.0224  -0.0438 -0.0127 903  ARG B NH1 
15680 N NH2 . ARG B 905  ? 0.3716 0.3824 0.4232 0.0244  -0.0392 -0.0130 903  ARG B NH2 
15681 N N   . GLY B 906  ? 0.2486 0.2839 0.3242 0.0115  -0.0447 -0.0127 904  GLY B N   
15682 C CA  . GLY B 906  ? 0.2803 0.3218 0.3618 0.0102  -0.0471 -0.0121 904  GLY B CA  
15683 C C   . GLY B 906  ? 0.2753 0.3151 0.3558 0.0063  -0.0486 -0.0125 904  GLY B C   
15684 O O   . GLY B 906  ? 0.3210 0.3643 0.4047 0.0048  -0.0516 -0.0122 904  GLY B O   
15685 N N   . LEU B 907  ? 0.2807 0.3153 0.3569 0.0046  -0.0467 -0.0133 905  LEU B N   
15686 C CA  . LEU B 907  ? 0.3391 0.3705 0.4130 0.0013  -0.0480 -0.0139 905  LEU B CA  
15687 C C   . LEU B 907  ? 0.3096 0.3350 0.3766 0.0011  -0.0504 -0.0148 905  LEU B C   
15688 O O   . LEU B 907  ? 0.3205 0.3424 0.3846 -0.0013 -0.0517 -0.0157 905  LEU B O   
15689 C CB  . LEU B 907  ? 0.3413 0.3697 0.4135 -0.0001 -0.0449 -0.0143 905  LEU B CB  
15690 C CG  . LEU B 907  ? 0.4164 0.4504 0.4949 -0.0009 -0.0427 -0.0134 905  LEU B CG  
15691 C CD1 . LEU B 907  ? 0.4523 0.4824 0.5282 -0.0022 -0.0399 -0.0138 905  LEU B CD1 
15692 C CD2 . LEU B 907  ? 0.4301 0.4695 0.5144 -0.0034 -0.0451 -0.0127 905  LEU B CD2 
15693 N N   . GLY B 908  ? 0.2846 0.3085 0.3488 0.0038  -0.0511 -0.0147 906  GLY B N   
15694 C CA  . GLY B 908  ? 0.2902 0.3088 0.3478 0.0038  -0.0534 -0.0154 906  GLY B CA  
15695 C C   . GLY B 908  ? 0.3415 0.3534 0.3919 0.0041  -0.0513 -0.0161 906  GLY B C   
15696 O O   . GLY B 908  ? 0.3172 0.3246 0.3617 0.0039  -0.0529 -0.0167 906  GLY B O   
15697 N N   . ARG B 909  ? 0.2603 0.2717 0.3110 0.0046  -0.0477 -0.0162 907  ARG B N   
15698 C CA  . ARG B 909  ? 0.2546 0.2603 0.2989 0.0049  -0.0457 -0.0168 907  ARG B CA  
15699 C C   . ARG B 909  ? 0.2607 0.2643 0.3015 0.0072  -0.0458 -0.0163 907  ARG B C   
15700 O O   . ARG B 909  ? 0.2964 0.3029 0.3405 0.0092  -0.0462 -0.0155 907  ARG B O   
15701 C CB  . ARG B 909  ? 0.2556 0.2618 0.3015 0.0049  -0.0420 -0.0168 907  ARG B CB  
15702 C CG  . ARG B 909  ? 0.3136 0.3212 0.3625 0.0025  -0.0415 -0.0171 907  ARG B CG  
15703 C CD  . ARG B 909  ? 0.4093 0.4121 0.4532 0.0007  -0.0424 -0.0183 907  ARG B CD  
15704 N NE  . ARG B 909  ? 0.4701 0.4735 0.5164 -0.0015 -0.0421 -0.0186 907  ARG B NE  
15705 C CZ  . ARG B 909  ? 0.5562 0.5611 0.6051 -0.0036 -0.0447 -0.0186 907  ARG B CZ  
15706 N NH1 . ARG B 909  ? 0.5737 0.5802 0.6233 -0.0037 -0.0479 -0.0185 907  ARG B NH1 
15707 N NH2 . ARG B 909  ? 0.5859 0.5906 0.6367 -0.0058 -0.0442 -0.0187 907  ARG B NH2 
15708 N N   . LYS B 910  ? 0.2383 0.2366 0.2723 0.0071  -0.0456 -0.0168 908  LYS B N   
15709 C CA  . LYS B 910  ? 0.2572 0.2528 0.2873 0.0089  -0.0456 -0.0162 908  LYS B CA  
15710 C C   . LYS B 910  ? 0.2356 0.2314 0.2667 0.0102  -0.0424 -0.0158 908  LYS B C   
15711 O O   . LYS B 910  ? 0.2458 0.2405 0.2759 0.0093  -0.0398 -0.0163 908  LYS B O   
15712 C CB  . LYS B 910  ? 0.2958 0.2862 0.3184 0.0081  -0.0460 -0.0167 908  LYS B CB  
15713 C CG  . LYS B 910  ? 0.3807 0.3680 0.3987 0.0095  -0.0464 -0.0159 908  LYS B CG  
15714 C CD  . LYS B 910  ? 0.4400 0.4226 0.4504 0.0086  -0.0463 -0.0163 908  LYS B CD  
15715 C CE  . LYS B 910  ? 0.5813 0.5607 0.5871 0.0097  -0.0471 -0.0152 908  LYS B CE  
15716 N NZ  . LYS B 910  ? 0.5823 0.5576 0.5807 0.0087  -0.0464 -0.0154 908  LYS B NZ  
15717 N N   . VAL B 911  ? 0.2174 0.2145 0.2504 0.0123  -0.0428 -0.0150 909  VAL B N   
15718 C CA  . VAL B 911  ? 0.2168 0.2139 0.2507 0.0137  -0.0401 -0.0147 909  VAL B CA  
15719 C C   . VAL B 911  ? 0.2397 0.2327 0.2689 0.0153  -0.0408 -0.0141 909  VAL B C   
15720 O O   . VAL B 911  ? 0.2557 0.2490 0.2851 0.0167  -0.0435 -0.0135 909  VAL B O   
15721 C CB  . VAL B 911  ? 0.2179 0.2205 0.2588 0.0151  -0.0397 -0.0144 909  VAL B CB  
15722 C CG1 . VAL B 911  ? 0.2302 0.2323 0.2713 0.0169  -0.0373 -0.0142 909  VAL B CG1 
15723 C CG2 . VAL B 911  ? 0.2328 0.2392 0.2781 0.0131  -0.0390 -0.0148 909  VAL B CG2 
15724 N N   . GLU B 912  ? 0.2192 0.2087 0.2444 0.0151  -0.0387 -0.0141 910  GLU B N   
15725 C CA  . GLU B 912  ? 0.2351 0.2203 0.2557 0.0162  -0.0392 -0.0133 910  GLU B CA  
15726 C C   . GLU B 912  ? 0.2443 0.2289 0.2654 0.0171  -0.0366 -0.0133 910  GLU B C   
15727 O O   . GLU B 912  ? 0.2329 0.2182 0.2546 0.0160  -0.0341 -0.0138 910  GLU B O   
15728 C CB  . GLU B 912  ? 0.2884 0.2693 0.3023 0.0145  -0.0393 -0.0132 910  GLU B CB  
15729 C CG  . GLU B 912  ? 0.3378 0.3186 0.3501 0.0138  -0.0420 -0.0133 910  GLU B CG  
15730 C CD  . GLU B 912  ? 0.4776 0.4547 0.4834 0.0121  -0.0416 -0.0134 910  GLU B CD  
15731 O OE1 . GLU B 912  ? 0.5056 0.4790 0.5064 0.0123  -0.0422 -0.0125 910  GLU B OE1 
15732 O OE2 . GLU B 912  ? 0.5726 0.5505 0.5782 0.0106  -0.0407 -0.0144 910  GLU B OE2 
15733 N N   . GLN B 913  ? 0.2221 0.2051 0.2428 0.0192  -0.0374 -0.0127 911  GLN B N   
15734 C CA  . GLN B 913  ? 0.2333 0.2147 0.2536 0.0202  -0.0354 -0.0127 911  GLN B CA  
15735 C C   . GLN B 913  ? 0.2837 0.2591 0.2980 0.0204  -0.0362 -0.0119 911  GLN B C   
15736 O O   . GLN B 913  ? 0.3080 0.2813 0.3202 0.0215  -0.0388 -0.0111 911  GLN B O   
15737 C CB  . GLN B 913  ? 0.2585 0.2435 0.2842 0.0228  -0.0353 -0.0128 911  GLN B CB  
15738 C CG  . GLN B 913  ? 0.2647 0.2558 0.2964 0.0221  -0.0343 -0.0134 911  GLN B CG  
15739 C CD  . GLN B 913  ? 0.3002 0.2954 0.3371 0.0246  -0.0336 -0.0136 911  GLN B CD  
15740 O OE1 . GLN B 913  ? 0.4156 0.4120 0.4543 0.0269  -0.0355 -0.0132 911  GLN B OE1 
15741 N NE2 . GLN B 913  ? 0.2708 0.2684 0.3103 0.0242  -0.0309 -0.0140 911  GLN B NE2 
15742 N N   . ILE B 914  ? 0.2774 0.2501 0.2888 0.0194  -0.0342 -0.0119 912  ILE B N   
15743 C CA  . ILE B 914  ? 0.3547 0.3216 0.3600 0.0188  -0.0347 -0.0110 912  ILE B CA  
15744 C C   . ILE B 914  ? 0.3199 0.2843 0.3245 0.0197  -0.0334 -0.0110 912  ILE B C   
15745 O O   . ILE B 914  ? 0.3021 0.2684 0.3083 0.0188  -0.0310 -0.0117 912  ILE B O   
15746 C CB  . ILE B 914  ? 0.3577 0.3233 0.3588 0.0159  -0.0337 -0.0107 912  ILE B CB  
15747 C CG1 . ILE B 914  ? 0.3892 0.3561 0.3898 0.0152  -0.0354 -0.0107 912  ILE B CG1 
15748 C CG2 . ILE B 914  ? 0.3542 0.3142 0.3493 0.0149  -0.0339 -0.0096 912  ILE B CG2 
15749 C CD1 . ILE B 914  ? 0.3358 0.3029 0.3336 0.0127  -0.0340 -0.0110 912  ILE B CD1 
15750 N N   . LEU B 916  ? 0.5990 0.5570 0.6064 0.0313  -0.0364 -0.0116 914  LEU B N   
15751 C CA  . LEU B 916  ? 0.4920 0.4481 0.4990 0.0327  -0.0347 -0.0124 914  LEU B CA  
15752 C C   . LEU B 916  ? 0.5655 0.5152 0.5688 0.0354  -0.0367 -0.0121 914  LEU B C   
15753 O O   . LEU B 916  ? 0.5075 0.4573 0.5118 0.0382  -0.0389 -0.0117 914  LEU B O   
15754 C CB  . LEU B 916  ? 0.5322 0.4952 0.5458 0.0346  -0.0331 -0.0135 914  LEU B CB  
15755 C CG  . LEU B 916  ? 0.4877 0.4568 0.5054 0.0323  -0.0307 -0.0140 914  LEU B CG  
15756 C CD1 . LEU B 916  ? 0.4586 0.4332 0.4818 0.0346  -0.0291 -0.0149 914  LEU B CD1 
15757 C CD2 . LEU B 916  ? 0.4870 0.4533 0.5010 0.0291  -0.0290 -0.0140 914  LEU B CD2 
15758 N N   . ALA B 917  ? 0.4945 0.4384 0.4934 0.0348  -0.0359 -0.0123 915  ALA B N   
15759 C CA  . ALA B 917  ? 0.5306 0.4675 0.5255 0.0375  -0.0376 -0.0122 915  ALA B CA  
15760 C C   . ALA B 917  ? 0.5619 0.5018 0.5610 0.0420  -0.0372 -0.0135 915  ALA B C   
15761 O O   . ALA B 917  ? 0.5225 0.4691 0.5268 0.0425  -0.0351 -0.0145 915  ALA B O   
15762 C CB  . ALA B 917  ? 0.4769 0.4071 0.4661 0.0352  -0.0368 -0.0122 915  ALA B CB  
15763 N N   . SER B 918  ? 0.5585 0.4934 0.5551 0.0455  -0.0394 -0.0134 916  SER B N   
15764 C CA  . SER B 918  ? 0.5816 0.5190 0.5817 0.0503  -0.0390 -0.0146 916  SER B CA  
15765 C C   . SER B 918  ? 0.5424 0.4796 0.5424 0.0505  -0.0364 -0.0161 916  SER B C   
15766 O O   . SER B 918  ? 0.4922 0.4350 0.4970 0.0534  -0.0349 -0.0173 916  SER B O   
15767 C CB  . SER B 918  ? 0.5776 0.5083 0.5741 0.0541  -0.0419 -0.0142 916  SER B CB  
15768 O OG  . SER B 918  ? 0.6588 0.5794 0.6477 0.0527  -0.0427 -0.0139 916  SER B OG  
15769 N N   . GLU B 919  ? 0.5048 0.4357 0.4994 0.0475  -0.0359 -0.0161 917  GLU B N   
15770 C CA  . GLU B 919  ? 0.5276 0.4577 0.5213 0.0473  -0.0337 -0.0175 917  GLU B CA  
15771 C C   . GLU B 919  ? 0.5082 0.4476 0.5081 0.0464  -0.0308 -0.0182 917  GLU B C   
15772 O O   . GLU B 919  ? 0.4792 0.4196 0.4797 0.0474  -0.0289 -0.0195 917  GLU B O   
15773 C CB  . GLU B 919  ? 0.5202 0.4432 0.5076 0.0433  -0.0337 -0.0170 917  GLU B CB  
15774 C CG  . GLU B 919  ? 0.6743 0.5867 0.6547 0.0442  -0.0362 -0.0167 917  GLU B CG  
15775 C CD  . GLU B 919  ? 0.6825 0.5918 0.6608 0.0439  -0.0389 -0.0149 917  GLU B CD  
15776 O OE1 . GLU B 919  ? 0.6227 0.5370 0.6035 0.0415  -0.0387 -0.0138 917  GLU B OE1 
15777 O OE2 . GLU B 919  ? 0.6778 0.5794 0.6515 0.0462  -0.0412 -0.0145 917  GLU B OE2 
15778 N N   . THR B 920  ? 0.4409 0.3866 0.4449 0.0444  -0.0306 -0.0174 918  THR B N   
15779 C CA  . THR B 920  ? 0.3806 0.3346 0.3903 0.0434  -0.0280 -0.0179 918  THR B CA  
15780 C C   . THR B 920  ? 0.3979 0.3580 0.4131 0.0475  -0.0271 -0.0188 918  THR B C   
15781 O O   . THR B 920  ? 0.3593 0.3251 0.3782 0.0471  -0.0247 -0.0194 918  THR B O   
15782 C CB  . THR B 920  ? 0.4376 0.3960 0.4498 0.0401  -0.0282 -0.0168 918  THR B CB  
15783 O OG1 . THR B 920  ? 0.4079 0.3677 0.4219 0.0418  -0.0305 -0.0160 918  THR B OG1 
15784 C CG2 . THR B 920  ? 0.3370 0.2906 0.3441 0.0360  -0.0284 -0.0160 918  THR B CG2 
15785 N N   . GLY B 921  ? 0.3869 0.3458 0.4024 0.0514  -0.0290 -0.0188 919  GLY B N   
15786 C CA  . GLY B 921  ? 0.3827 0.3484 0.4040 0.0554  -0.0282 -0.0195 919  GLY B CA  
15787 C C   . GLY B 921  ? 0.3631 0.3302 0.3850 0.0573  -0.0257 -0.0210 919  GLY B C   
15788 O O   . GLY B 921  ? 0.4199 0.3947 0.4475 0.0593  -0.0241 -0.0214 919  GLY B O   
15789 N N   . VAL B 922  ? 0.2863 0.2460 0.3022 0.0566  -0.0253 -0.0217 920  VAL B N   
15790 C CA  . VAL B 922  ? 0.2746 0.2347 0.2901 0.0583  -0.0229 -0.0233 920  VAL B CA  
15791 C C   . VAL B 922  ? 0.2769 0.2422 0.2948 0.0549  -0.0202 -0.0233 920  VAL B C   
15792 O O   . VAL B 922  ? 0.2451 0.2123 0.2635 0.0561  -0.0180 -0.0245 920  VAL B O   
15793 C CB  . VAL B 922  ? 0.3004 0.2500 0.3081 0.0588  -0.0239 -0.0241 920  VAL B CB  
15794 C CG1 . VAL B 922  ? 0.2949 0.2390 0.3000 0.0631  -0.0264 -0.0242 920  VAL B CG1 
15795 C CG2 . VAL B 922  ? 0.3274 0.2714 0.3304 0.0537  -0.0247 -0.0231 920  VAL B CG2 
15796 N N   . GLY B 923  ? 0.2322 0.1997 0.2514 0.0507  -0.0203 -0.0221 921  GLY B N   
15797 C CA  . GLY B 923  ? 0.2418 0.2143 0.2636 0.0476  -0.0180 -0.0221 921  GLY B CA  
15798 C C   . GLY B 923  ? 0.2430 0.2229 0.2706 0.0462  -0.0179 -0.0210 921  GLY B C   
15799 O O   . GLY B 923  ? 0.2546 0.2369 0.2851 0.0480  -0.0194 -0.0205 921  GLY B O   
15800 N N   . THR B 924  ? 0.2004 0.1839 0.2299 0.0429  -0.0162 -0.0207 922  THR B N   
15801 C CA  . THR B 924  ? 0.1935 0.1838 0.2284 0.0412  -0.0161 -0.0198 922  THR B CA  
15802 C C   . THR B 924  ? 0.2043 0.1918 0.2367 0.0373  -0.0170 -0.0190 922  THR B C   
15803 O O   . THR B 924  ? 0.2064 0.1933 0.2373 0.0347  -0.0155 -0.0190 922  THR B O   
15804 C CB  . THR B 924  ? 0.1789 0.1758 0.2182 0.0409  -0.0134 -0.0200 922  THR B CB  
15805 O OG1 . THR B 924  ? 0.2023 0.1965 0.2382 0.0392  -0.0117 -0.0205 922  THR B OG1 
15806 C CG2 . THR B 924  ? 0.2104 0.2114 0.2529 0.0450  -0.0125 -0.0206 922  THR B CG2 
15807 N N   . PHE B 925  ? 0.2000 0.1861 0.2319 0.0370  -0.0193 -0.0182 923  PHE B N   
15808 C CA  . PHE B 925  ? 0.2045 0.1878 0.2336 0.0336  -0.0202 -0.0175 923  PHE B CA  
15809 C C   . PHE B 925  ? 0.1977 0.1857 0.2308 0.0327  -0.0213 -0.0168 923  PHE B C   
15810 O O   . PHE B 925  ? 0.2101 0.2012 0.2465 0.0348  -0.0225 -0.0166 923  PHE B O   
15811 C CB  . PHE B 925  ? 0.2056 0.1816 0.2290 0.0337  -0.0224 -0.0171 923  PHE B CB  
15812 C CG  . PHE B 925  ? 0.2110 0.1812 0.2295 0.0338  -0.0217 -0.0177 923  PHE B CG  
15813 C CD1 . PHE B 925  ? 0.2177 0.1859 0.2355 0.0371  -0.0217 -0.0185 923  PHE B CD1 
15814 C CD2 . PHE B 925  ? 0.2037 0.1706 0.2183 0.0305  -0.0211 -0.0174 923  PHE B CD2 
15815 C CE1 . PHE B 925  ? 0.2334 0.1957 0.2464 0.0371  -0.0213 -0.0191 923  PHE B CE1 
15816 C CE2 . PHE B 925  ? 0.2129 0.1746 0.2231 0.0302  -0.0208 -0.0179 923  PHE B CE2 
15817 C CZ  . PHE B 925  ? 0.2130 0.1720 0.2222 0.0334  -0.0210 -0.0188 923  PHE B CZ  
15818 N N   . VAL B 926  ? 0.1934 0.1818 0.2258 0.0294  -0.0208 -0.0164 924  VAL B N   
15819 C CA  . VAL B 926  ? 0.2041 0.1949 0.2384 0.0279  -0.0222 -0.0158 924  VAL B CA  
15820 C C   . VAL B 926  ? 0.1921 0.1778 0.2211 0.0256  -0.0232 -0.0154 924  VAL B C   
15821 O O   . VAL B 926  ? 0.1937 0.1773 0.2198 0.0238  -0.0217 -0.0155 924  VAL B O   
15822 C CB  . VAL B 926  ? 0.1876 0.1839 0.2262 0.0262  -0.0206 -0.0159 924  VAL B CB  
15823 C CG1 . VAL B 926  ? 0.1971 0.1949 0.2369 0.0244  -0.0222 -0.0155 924  VAL B CG1 
15824 C CG2 . VAL B 926  ? 0.2188 0.2207 0.2628 0.0283  -0.0195 -0.0161 924  VAL B CG2 
15825 N N   . PRO B 927  ? 0.2285 0.2123 0.2558 0.0256  -0.0255 -0.0148 925  PRO B N   
15826 C CA  . PRO B 927  ? 0.2254 0.2046 0.2473 0.0234  -0.0263 -0.0143 925  PRO B CA  
15827 C C   . PRO B 927  ? 0.2060 0.1876 0.2286 0.0207  -0.0254 -0.0143 925  PRO B C   
15828 O O   . PRO B 927  ? 0.2086 0.1949 0.2357 0.0206  -0.0252 -0.0146 925  PRO B O   
15829 C CB  . PRO B 927  ? 0.2617 0.2387 0.2821 0.0246  -0.0292 -0.0136 925  PRO B CB  
15830 C CG  . PRO B 927  ? 0.2365 0.2191 0.2627 0.0262  -0.0300 -0.0138 925  PRO B CG  
15831 C CD  . PRO B 927  ? 0.2449 0.2312 0.2752 0.0275  -0.0277 -0.0145 925  PRO B CD  
15832 N N   . PRO B 928  ? 0.2162 0.1947 0.2345 0.0185  -0.0249 -0.0141 926  PRO B N   
15833 C CA  . PRO B 928  ? 0.2176 0.1977 0.2356 0.0163  -0.0244 -0.0142 926  PRO B CA  
15834 C C   . PRO B 928  ? 0.2119 0.1940 0.2319 0.0165  -0.0265 -0.0141 926  PRO B C   
15835 O O   . PRO B 928  ? 0.2143 0.1945 0.2326 0.0174  -0.0287 -0.0136 926  PRO B O   
15836 C CB  . PRO B 928  ? 0.2342 0.2101 0.2465 0.0146  -0.0244 -0.0136 926  PRO B CB  
15837 C CG  . PRO B 928  ? 0.2692 0.2421 0.2796 0.0151  -0.0237 -0.0134 926  PRO B CG  
15838 C CD  . PRO B 928  ? 0.2501 0.2234 0.2632 0.0179  -0.0248 -0.0136 926  PRO B CD  
15839 N N   . THR B 929  ? 0.2040 0.1899 0.2274 0.0156  -0.0258 -0.0146 927  THR B N   
15840 C CA  . THR B 929  ? 0.1905 0.1789 0.2165 0.0156  -0.0276 -0.0147 927  THR B CA  
15841 C C   . THR B 929  ? 0.1895 0.1780 0.2141 0.0135  -0.0272 -0.0151 927  THR B C   
15842 O O   . THR B 929  ? 0.2032 0.1923 0.2281 0.0125  -0.0251 -0.0155 927  THR B O   
15843 C CB  . THR B 929  ? 0.1892 0.1825 0.2215 0.0168  -0.0272 -0.0149 927  THR B CB  
15844 O OG1 . THR B 929  ? 0.2031 0.1963 0.2363 0.0192  -0.0275 -0.0146 927  THR B OG1 
15845 C CG2 . THR B 929  ? 0.2023 0.1987 0.2377 0.0164  -0.0293 -0.0148 927  THR B CG2 
15846 N N   . ILE B 930  ? 0.1957 0.1833 0.2186 0.0129  -0.0294 -0.0150 928  ILE B N   
15847 C CA  . ILE B 930  ? 0.2116 0.1987 0.2327 0.0111  -0.0294 -0.0156 928  ILE B CA  
15848 C C   . ILE B 930  ? 0.2132 0.2030 0.2377 0.0109  -0.0315 -0.0159 928  ILE B C   
15849 O O   . ILE B 930  ? 0.2009 0.1909 0.2259 0.0117  -0.0339 -0.0155 928  ILE B O   
15850 C CB  . ILE B 930  ? 0.2131 0.1964 0.2280 0.0104  -0.0301 -0.0154 928  ILE B CB  
15851 C CG1 . ILE B 930  ? 0.2267 0.2077 0.2384 0.0102  -0.0281 -0.0149 928  ILE B CG1 
15852 C CG2 . ILE B 930  ? 0.2346 0.2175 0.2475 0.0089  -0.0300 -0.0162 928  ILE B CG2 
15853 C CD1 . ILE B 930  ? 0.2893 0.2667 0.2949 0.0094  -0.0287 -0.0144 928  ILE B CD1 
15854 N N   . ILE B 931  ? 0.2064 0.1981 0.2334 0.0097  -0.0307 -0.0165 929  ILE B N   
15855 C CA  . ILE B 931  ? 0.1856 0.1799 0.2162 0.0090  -0.0325 -0.0167 929  ILE B CA  
15856 C C   . ILE B 931  ? 0.2089 0.2010 0.2364 0.0073  -0.0328 -0.0176 929  ILE B C   
15857 O O   . ILE B 931  ? 0.2141 0.2053 0.2406 0.0066  -0.0307 -0.0181 929  ILE B O   
15858 C CB  . ILE B 931  ? 0.2000 0.1986 0.2367 0.0091  -0.0313 -0.0166 929  ILE B CB  
15859 C CG1 . ILE B 931  ? 0.2239 0.2245 0.2632 0.0112  -0.0307 -0.0159 929  ILE B CG1 
15860 C CG2 . ILE B 931  ? 0.1979 0.1994 0.2385 0.0079  -0.0335 -0.0167 929  ILE B CG2 
15861 C CD1 . ILE B 931  ? 0.2218 0.2274 0.2674 0.0115  -0.0296 -0.0156 929  ILE B CD1 
15862 N N   . GLU B 932  ? 0.1995 0.1906 0.2253 0.0067  -0.0355 -0.0179 930  GLU B N   
15863 C CA  . GLU B 932  ? 0.2200 0.2087 0.2426 0.0052  -0.0360 -0.0189 930  GLU B CA  
15864 C C   . GLU B 932  ? 0.2156 0.2066 0.2427 0.0038  -0.0366 -0.0193 930  GLU B C   
15865 O O   . GLU B 932  ? 0.2229 0.2170 0.2542 0.0036  -0.0386 -0.0189 930  GLU B O   
15866 C CB  . GLU B 932  ? 0.2770 0.2631 0.2949 0.0050  -0.0387 -0.0191 930  GLU B CB  
15867 C CG  . GLU B 932  ? 0.3136 0.2970 0.3265 0.0060  -0.0380 -0.0186 930  GLU B CG  
15868 C CD  . GLU B 932  ? 0.5030 0.4831 0.5098 0.0055  -0.0398 -0.0190 930  GLU B CD  
15869 O OE1 . GLU B 932  ? 0.5298 0.5098 0.5365 0.0047  -0.0422 -0.0197 930  GLU B OE1 
15870 O OE2 . GLU B 932  ? 0.4295 0.4072 0.4315 0.0058  -0.0387 -0.0186 930  GLU B OE2 
15871 N N   . LEU B 933  ? 0.2437 0.2333 0.2699 0.0029  -0.0349 -0.0200 931  LEU B N   
15872 C CA  . LEU B 933  ? 0.2190 0.2099 0.2488 0.0013  -0.0355 -0.0203 931  LEU B CA  
15873 C C   . LEU B 933  ? 0.2813 0.2685 0.3068 0.0000  -0.0373 -0.0216 931  LEU B C   
15874 O O   . LEU B 933  ? 0.3201 0.3037 0.3399 0.0005  -0.0369 -0.0224 931  LEU B O   
15875 C CB  . LEU B 933  ? 0.2436 0.2351 0.2752 0.0012  -0.0325 -0.0202 931  LEU B CB  
15876 C CG  . LEU B 933  ? 0.2821 0.2770 0.3173 0.0025  -0.0304 -0.0192 931  LEU B CG  
15877 C CD1 . LEU B 933  ? 0.3255 0.3203 0.3616 0.0022  -0.0277 -0.0192 931  LEU B CD1 
15878 C CD2 . LEU B 933  ? 0.3632 0.3626 0.4042 0.0026  -0.0317 -0.0183 931  LEU B CD2 
15879 N N   . GLU B 934  ? 0.2987 0.2868 0.3272 -0.0017 -0.0393 -0.0218 932  GLU B N   
15880 C CA  . GLU B 934  ? 0.3227 0.3067 0.3473 -0.0031 -0.0410 -0.0231 932  GLU B CA  
15881 C C   . GLU B 934  ? 0.3332 0.3147 0.3567 -0.0035 -0.0387 -0.0238 932  GLU B C   
15882 O O   . GLU B 934  ? 0.3863 0.3633 0.4045 -0.0035 -0.0388 -0.0251 932  GLU B O   
15883 C CB  . GLU B 934  ? 0.3867 0.3723 0.4145 -0.0050 -0.0443 -0.0231 932  GLU B CB  
15884 N N   . LYS B 935  ? 0.3072 0.2916 0.3355 -0.0036 -0.0367 -0.0229 933  LYS B N   
15885 C CA  . LYS B 935  ? 0.3041 0.2864 0.3319 -0.0040 -0.0348 -0.0232 933  LYS B CA  
15886 C C   . LYS B 935  ? 0.2701 0.2559 0.3016 -0.0030 -0.0318 -0.0220 933  LYS B C   
15887 O O   . LYS B 935  ? 0.2937 0.2839 0.3298 -0.0028 -0.0318 -0.0209 933  LYS B O   
15888 C CB  . LYS B 935  ? 0.3741 0.3556 0.4042 -0.0064 -0.0366 -0.0234 933  LYS B CB  
15889 N N   . LEU B 936  ? 0.2772 0.2611 0.3068 -0.0023 -0.0294 -0.0223 934  LEU B N   
15890 C CA  . LEU B 936  ? 0.2899 0.2767 0.3226 -0.0014 -0.0267 -0.0212 934  LEU B CA  
15891 C C   . LEU B 936  ? 0.3005 0.2910 0.3392 -0.0028 -0.0267 -0.0201 934  LEU B C   
15892 O O   . LEU B 936  ? 0.2889 0.2833 0.3312 -0.0020 -0.0252 -0.0190 934  LEU B O   
15893 C CB  . LEU B 936  ? 0.3134 0.2976 0.3430 -0.0005 -0.0244 -0.0217 934  LEU B CB  
15894 C CG  . LEU B 936  ? 0.3253 0.3112 0.3546 0.0011  -0.0217 -0.0212 934  LEU B CG  
15895 C CD1 . LEU B 936  ? 0.3369 0.3198 0.3615 0.0022  -0.0202 -0.0220 934  LEU B CD1 
15896 C CD2 . LEU B 936  ? 0.3463 0.3355 0.3803 0.0010  -0.0201 -0.0200 934  LEU B CD2 
15897 N N   . SER B 937  ? 0.2598 0.2490 0.2996 -0.0048 -0.0285 -0.0203 935  SER B N   
15898 C CA  . SER B 937  ? 0.2914 0.2843 0.3370 -0.0065 -0.0286 -0.0190 935  SER B CA  
15899 C C   . SER B 937  ? 0.2929 0.2913 0.3431 -0.0064 -0.0297 -0.0181 935  SER B C   
15900 O O   . SER B 937  ? 0.2898 0.2925 0.3454 -0.0075 -0.0293 -0.0169 935  SER B O   
15901 C CB  . SER B 937  ? 0.3001 0.2900 0.3454 -0.0090 -0.0305 -0.0193 935  SER B CB  
15902 O OG  . SER B 937  ? 0.3518 0.3397 0.3949 -0.0099 -0.0336 -0.0203 935  SER B OG  
15903 N N   . ASP B 938  ? 0.2632 0.2616 0.3115 -0.0052 -0.0310 -0.0186 936  ASP B N   
15904 C CA  . ASP B 938  ? 0.2816 0.2852 0.3341 -0.0044 -0.0318 -0.0177 936  ASP B CA  
15905 C C   . ASP B 938  ? 0.2496 0.2566 0.3049 -0.0028 -0.0289 -0.0168 936  ASP B C   
15906 O O   . ASP B 938  ? 0.2894 0.3015 0.3495 -0.0023 -0.0290 -0.0158 936  ASP B O   
15907 C CB  . ASP B 938  ? 0.3367 0.3387 0.3856 -0.0030 -0.0334 -0.0183 936  ASP B CB  
15908 C CG  . ASP B 938  ? 0.4238 0.4231 0.4701 -0.0045 -0.0367 -0.0192 936  ASP B CG  
15909 O OD1 . ASP B 938  ? 0.4051 0.4041 0.4531 -0.0068 -0.0380 -0.0193 936  ASP B OD1 
15910 O OD2 . ASP B 938  ? 0.4878 0.4850 0.5302 -0.0034 -0.0379 -0.0198 936  ASP B OD2 
15911 N N   . LEU B 939  ? 0.2460 0.2506 0.2983 -0.0018 -0.0264 -0.0170 937  LEU B N   
15912 C CA  . LEU B 939  ? 0.2868 0.2939 0.3408 -0.0001 -0.0238 -0.0163 937  LEU B CA  
15913 C C   . LEU B 939  ? 0.2820 0.2906 0.3388 -0.0013 -0.0220 -0.0156 937  LEU B C   
15914 O O   . LEU B 939  ? 0.3673 0.3725 0.4217 -0.0022 -0.0215 -0.0160 937  LEU B O   
15915 C CB  . LEU B 939  ? 0.2712 0.2747 0.3200 0.0014  -0.0224 -0.0170 937  LEU B CB  
15916 C CG  . LEU B 939  ? 0.3353 0.3402 0.3842 0.0032  -0.0200 -0.0166 937  LEU B CG  
15917 C CD1 . LEU B 939  ? 0.3263 0.3345 0.3780 0.0046  -0.0207 -0.0161 937  LEU B CD1 
15918 C CD2 . LEU B 939  ? 0.2764 0.2774 0.3198 0.0041  -0.0194 -0.0173 937  LEU B CD2 
15919 N N   . GLN B 940  ? 0.2361 0.2499 0.2980 -0.0011 -0.0211 -0.0145 938  GLN B N   
15920 C CA  . GLN B 940  ? 0.2985 0.3144 0.3636 -0.0025 -0.0196 -0.0135 938  GLN B CA  
15921 C C   . GLN B 940  ? 0.2647 0.2827 0.3307 -0.0010 -0.0166 -0.0129 938  GLN B C   
15922 O O   . GLN B 940  ? 0.2714 0.2907 0.3393 -0.0020 -0.0151 -0.0120 938  GLN B O   
15923 C CB  . GLN B 940  ? 0.3787 0.3996 0.4496 -0.0041 -0.0210 -0.0125 938  GLN B CB  
15924 N N   . ARG B 941  ? 0.2125 0.2304 0.2767 0.0014  -0.0157 -0.0134 939  ARG B N   
15925 C CA  . ARG B 941  ? 0.2155 0.2352 0.2802 0.0028  -0.0131 -0.0129 939  ARG B CA  
15926 C C   . ARG B 941  ? 0.1824 0.1990 0.2427 0.0047  -0.0126 -0.0138 939  ARG B C   
15927 O O   . ARG B 941  ? 0.1782 0.1928 0.2363 0.0052  -0.0142 -0.0144 939  ARG B O   
15928 C CB  . ARG B 941  ? 0.2529 0.2785 0.3226 0.0037  -0.0125 -0.0121 939  ARG B CB  
15929 C CG  . ARG B 941  ? 0.2317 0.2588 0.3021 0.0055  -0.0140 -0.0125 939  ARG B CG  
15930 C CD  . ARG B 941  ? 0.2408 0.2744 0.3168 0.0063  -0.0136 -0.0116 939  ARG B CD  
15931 N NE  . ARG B 941  ? 0.2493 0.2843 0.3260 0.0084  -0.0150 -0.0120 939  ARG B NE  
15932 C CZ  . ARG B 941  ? 0.2400 0.2748 0.3154 0.0111  -0.0139 -0.0123 939  ARG B CZ  
15933 N NH1 . ARG B 941  ? 0.2508 0.2839 0.3238 0.0119  -0.0116 -0.0126 939  ARG B NH1 
15934 N NH2 . ARG B 941  ? 0.2415 0.2778 0.3180 0.0132  -0.0153 -0.0125 939  ARG B NH2 
15935 N N   . GLU B 942  ? 0.1930 0.2094 0.2521 0.0056  -0.0103 -0.0137 940  GLU B N   
15936 C CA  . GLU B 942  ? 0.1765 0.1905 0.2318 0.0072  -0.0097 -0.0143 940  GLU B CA  
15937 C C   . GLU B 942  ? 0.1916 0.2078 0.2484 0.0090  -0.0101 -0.0143 940  GLU B C   
15938 O O   . GLU B 942  ? 0.2390 0.2589 0.2991 0.0098  -0.0091 -0.0138 940  GLU B O   
15939 C CB  . GLU B 942  ? 0.1943 0.2080 0.2483 0.0076  -0.0073 -0.0141 940  GLU B CB  
15940 C CG  . GLU B 942  ? 0.1919 0.2035 0.2423 0.0090  -0.0066 -0.0147 940  GLU B CG  
15941 C CD  . GLU B 942  ? 0.1919 0.2041 0.2418 0.0094  -0.0044 -0.0144 940  GLU B CD  
15942 O OE1 . GLU B 942  ? 0.2311 0.2463 0.2838 0.0096  -0.0033 -0.0138 940  GLU B OE1 
15943 O OE2 . GLU B 942  ? 0.1763 0.1861 0.2227 0.0095  -0.0038 -0.0148 940  GLU B OE2 
15944 N N   . VAL B 943  ? 0.1589 0.1727 0.2131 0.0097  -0.0116 -0.0149 941  VAL B N   
15945 C CA  . VAL B 943  ? 0.1643 0.1790 0.2190 0.0116  -0.0123 -0.0149 941  VAL B CA  
15946 C C   . VAL B 943  ? 0.1794 0.1909 0.2300 0.0127  -0.0113 -0.0154 941  VAL B C   
15947 O O   . VAL B 943  ? 0.1663 0.1742 0.2129 0.0122  -0.0120 -0.0157 941  VAL B O   
15948 C CB  . VAL B 943  ? 0.1875 0.2017 0.2423 0.0115  -0.0150 -0.0151 941  VAL B CB  
15949 C CG1 . VAL B 943  ? 0.1987 0.2137 0.2540 0.0138  -0.0158 -0.0151 941  VAL B CG1 
15950 C CG2 . VAL B 943  ? 0.2400 0.2574 0.2989 0.0100  -0.0161 -0.0147 941  VAL B CG2 
15951 N N   . PHE B 944  ? 0.1713 0.1844 0.2228 0.0141  -0.0097 -0.0153 942  PHE B N   
15952 C CA  . PHE B 944  ? 0.1661 0.1764 0.2139 0.0146  -0.0085 -0.0157 942  PHE B CA  
15953 C C   . PHE B 944  ? 0.1634 0.1713 0.2090 0.0162  -0.0096 -0.0160 942  PHE B C   
15954 O O   . PHE B 944  ? 0.1873 0.1956 0.2331 0.0180  -0.0090 -0.0162 942  PHE B O   
15955 C CB  . PHE B 944  ? 0.1661 0.1788 0.2155 0.0151  -0.0063 -0.0155 942  PHE B CB  
15956 C CG  . PHE B 944  ? 0.1628 0.1730 0.2085 0.0149  -0.0049 -0.0158 942  PHE B CG  
15957 C CD1 . PHE B 944  ? 0.1649 0.1738 0.2091 0.0133  -0.0045 -0.0157 942  PHE B CD1 
15958 C CD2 . PHE B 944  ? 0.1638 0.1730 0.2078 0.0164  -0.0042 -0.0162 942  PHE B CD2 
15959 C CE1 . PHE B 944  ? 0.1823 0.1895 0.2235 0.0131  -0.0033 -0.0158 942  PHE B CE1 
15960 C CE2 . PHE B 944  ? 0.1756 0.1826 0.2163 0.0159  -0.0032 -0.0164 942  PHE B CE2 
15961 C CZ  . PHE B 944  ? 0.1922 0.1986 0.2317 0.0142  -0.0028 -0.0162 942  PHE B CZ  
15962 N N   . GLY B 945  ? 0.1573 0.1623 0.2003 0.0156  -0.0114 -0.0161 943  GLY B N   
15963 C CA  . GLY B 945  ? 0.1889 0.1911 0.2294 0.0169  -0.0128 -0.0162 943  GLY B CA  
15964 C C   . GLY B 945  ? 0.1810 0.1798 0.2178 0.0156  -0.0143 -0.0161 943  GLY B C   
15965 O O   . GLY B 945  ? 0.1794 0.1779 0.2152 0.0139  -0.0139 -0.0162 943  GLY B O   
15966 N N   . PRO B 946  ? 0.1717 0.1676 0.2060 0.0165  -0.0159 -0.0160 944  PRO B N   
15967 C CA  . PRO B 946  ? 0.1733 0.1656 0.2033 0.0153  -0.0170 -0.0158 944  PRO B CA  
15968 C C   . PRO B 946  ? 0.1675 0.1605 0.1982 0.0147  -0.0189 -0.0157 944  PRO B C   
15969 O O   . PRO B 946  ? 0.2003 0.1914 0.2292 0.0152  -0.0209 -0.0154 944  PRO B O   
15970 C CB  . PRO B 946  ? 0.1846 0.1733 0.2115 0.0165  -0.0179 -0.0156 944  PRO B CB  
15971 C CG  . PRO B 946  ? 0.1936 0.1845 0.2241 0.0189  -0.0185 -0.0158 944  PRO B CG  
15972 C CD  . PRO B 946  ? 0.1727 0.1683 0.2077 0.0189  -0.0165 -0.0160 944  PRO B CD  
15973 N N   . VAL B 947  ? 0.1771 0.1728 0.2105 0.0136  -0.0185 -0.0159 945  VAL B N   
15974 C CA  . VAL B 947  ? 0.1680 0.1649 0.2028 0.0130  -0.0203 -0.0159 945  VAL B CA  
15975 C C   . VAL B 947  ? 0.1999 0.1954 0.2323 0.0112  -0.0199 -0.0163 945  VAL B C   
15976 O O   . VAL B 947  ? 0.2024 0.1995 0.2365 0.0104  -0.0184 -0.0165 945  VAL B O   
15977 C CB  . VAL B 947  ? 0.1826 0.1840 0.2230 0.0135  -0.0205 -0.0158 945  VAL B CB  
15978 C CG1 . VAL B 947  ? 0.1935 0.1958 0.2351 0.0126  -0.0229 -0.0158 945  VAL B CG1 
15979 C CG2 . VAL B 947  ? 0.2005 0.2036 0.2433 0.0157  -0.0205 -0.0156 945  VAL B CG2 
15980 N N   . LEU B 948  ? 0.1725 0.1651 0.2008 0.0106  -0.0211 -0.0163 946  LEU B N   
15981 C CA  . LEU B 948  ? 0.1778 0.1690 0.2032 0.0092  -0.0208 -0.0168 946  LEU B CA  
15982 C C   . LEU B 948  ? 0.1799 0.1714 0.2061 0.0086  -0.0229 -0.0171 946  LEU B C   
15983 O O   . LEU B 948  ? 0.2035 0.1945 0.2293 0.0090  -0.0250 -0.0169 946  LEU B O   
15984 C CB  . LEU B 948  ? 0.1797 0.1676 0.1997 0.0089  -0.0208 -0.0166 946  LEU B CB  
15985 C CG  . LEU B 948  ? 0.1924 0.1790 0.2091 0.0078  -0.0203 -0.0171 946  LEU B CG  
15986 C CD1 . LEU B 948  ? 0.1938 0.1818 0.2118 0.0075  -0.0180 -0.0175 946  LEU B CD1 
15987 C CD2 . LEU B 948  ? 0.2387 0.2227 0.2503 0.0074  -0.0204 -0.0167 946  LEU B CD2 
15988 N N   . HIS B 949  ? 0.1689 0.1611 0.1962 0.0076  -0.0223 -0.0177 947  HIS B N   
15989 C CA  . HIS B 949  ? 0.1663 0.1582 0.1938 0.0067  -0.0243 -0.0182 947  HIS B CA  
15990 C C   . HIS B 949  ? 0.2057 0.1944 0.2279 0.0061  -0.0244 -0.0189 947  HIS B C   
15991 O O   . HIS B 949  ? 0.2208 0.2085 0.2407 0.0061  -0.0224 -0.0191 947  HIS B O   
15992 C CB  . HIS B 949  ? 0.1920 0.1863 0.2238 0.0059  -0.0239 -0.0183 947  HIS B CB  
15993 C CG  . HIS B 949  ? 0.1729 0.1709 0.2099 0.0066  -0.0234 -0.0176 947  HIS B CG  
15994 N ND1 . HIS B 949  ? 0.1781 0.1773 0.2163 0.0073  -0.0210 -0.0172 947  HIS B ND1 
15995 C CD2 . HIS B 949  ? 0.1835 0.1845 0.2245 0.0068  -0.0249 -0.0171 947  HIS B CD2 
15996 C CE1 . HIS B 949  ? 0.1799 0.1826 0.2226 0.0081  -0.0210 -0.0167 947  HIS B CE1 
15997 N NE2 . HIS B 949  ? 0.1895 0.1936 0.2341 0.0078  -0.0233 -0.0165 947  HIS B NE2 
15998 N N   . VAL B 950  ? 0.2006 0.1878 0.2207 0.0056  -0.0268 -0.0192 948  VAL B N   
15999 C CA  . VAL B 950  ? 0.2261 0.2102 0.2406 0.0053  -0.0269 -0.0199 948  VAL B CA  
16000 C C   . VAL B 950  ? 0.2144 0.1974 0.2286 0.0043  -0.0285 -0.0210 948  VAL B C   
16001 O O   . VAL B 950  ? 0.2149 0.1988 0.2315 0.0038  -0.0308 -0.0209 948  VAL B O   
16002 C CB  . VAL B 950  ? 0.2187 0.2010 0.2292 0.0056  -0.0283 -0.0195 948  VAL B CB  
16003 C CG1 . VAL B 950  ? 0.2589 0.2383 0.2636 0.0052  -0.0286 -0.0203 948  VAL B CG1 
16004 C CG2 . VAL B 950  ? 0.2299 0.2124 0.2399 0.0064  -0.0267 -0.0185 948  VAL B CG2 
16005 N N   . ILE B 951  ? 0.1976 0.1787 0.2089 0.0041  -0.0272 -0.0219 949  ILE B N   
16006 C CA  . ILE B 951  ? 0.2171 0.1960 0.2267 0.0033  -0.0286 -0.0231 949  ILE B CA  
16007 C C   . ILE B 951  ? 0.2040 0.1798 0.2070 0.0037  -0.0285 -0.0240 949  ILE B C   
16008 O O   . ILE B 951  ? 0.2229 0.1987 0.2236 0.0045  -0.0262 -0.0238 949  ILE B O   
16009 C CB  . ILE B 951  ? 0.2501 0.2290 0.2619 0.0030  -0.0270 -0.0235 949  ILE B CB  
16010 C CG1 . ILE B 951  ? 0.3167 0.2987 0.3348 0.0023  -0.0273 -0.0226 949  ILE B CG1 
16011 C CG2 . ILE B 951  ? 0.3451 0.3204 0.3536 0.0024  -0.0281 -0.0250 949  ILE B CG2 
16012 C CD1 . ILE B 951  ? 0.4099 0.3918 0.4302 0.0018  -0.0258 -0.0228 949  ILE B CD1 
16013 N N   . ARG B 952  ? 0.2156 0.1891 0.2156 0.0032  -0.0308 -0.0249 950  ARG B N   
16014 C CA  A ARG B 952  ? 0.2308 0.2013 0.2243 0.0036  -0.0307 -0.0259 950  ARG B CA  
16015 C CA  B ARG B 952  ? 0.2311 0.2016 0.2246 0.0036  -0.0307 -0.0259 950  ARG B CA  
16016 C C   . ARG B 952  ? 0.2328 0.2006 0.2247 0.0035  -0.0308 -0.0275 950  ARG B C   
16017 O O   . ARG B 952  ? 0.2911 0.2584 0.2858 0.0024  -0.0325 -0.0279 950  ARG B O   
16018 C CB  A ARG B 952  ? 0.2385 0.2077 0.2288 0.0033  -0.0335 -0.0259 950  ARG B CB  
16019 C CB  B ARG B 952  ? 0.2386 0.2078 0.2290 0.0033  -0.0336 -0.0259 950  ARG B CB  
16020 C CG  A ARG B 952  ? 0.2628 0.2339 0.2542 0.0036  -0.0338 -0.0242 950  ARG B CG  
16021 C CG  B ARG B 952  ? 0.2659 0.2372 0.2581 0.0035  -0.0342 -0.0243 950  ARG B CG  
16022 C CD  A ARG B 952  ? 0.3091 0.2798 0.3001 0.0032  -0.0372 -0.0240 950  ARG B CD  
16023 C CD  B ARG B 952  ? 0.3082 0.2784 0.2983 0.0031  -0.0375 -0.0242 950  ARG B CD  
16024 N NE  A ARG B 952  ? 0.3291 0.3014 0.3216 0.0037  -0.0376 -0.0224 950  ARG B NE  
16025 N NE  B ARG B 952  ? 0.3215 0.2888 0.3044 0.0034  -0.0377 -0.0248 950  ARG B NE  
16026 C CZ  A ARG B 952  ? 0.3196 0.2904 0.3075 0.0041  -0.0381 -0.0217 950  ARG B CZ  
16027 C CZ  B ARG B 952  ? 0.3231 0.2900 0.3027 0.0038  -0.0377 -0.0237 950  ARG B CZ  
16028 N NH1 A ARG B 952  ? 0.3283 0.2965 0.3099 0.0040  -0.0379 -0.0224 950  ARG B NH1 
16029 N NH1 B ARG B 952  ? 0.3241 0.2927 0.3065 0.0041  -0.0377 -0.0221 950  ARG B NH1 
16030 N NH2 A ARG B 952  ? 0.3201 0.2918 0.3095 0.0047  -0.0387 -0.0202 950  ARG B NH2 
16031 N NH2 B ARG B 952  ? 0.2939 0.2584 0.2668 0.0039  -0.0377 -0.0243 950  ARG B NH2 
16032 N N   . TYR B 953  ? 0.2234 0.1895 0.2108 0.0045  -0.0289 -0.0284 951  TYR B N   
16033 C CA  . TYR B 953  ? 0.2403 0.2033 0.2258 0.0047  -0.0289 -0.0300 951  TYR B CA  
16034 C C   . TYR B 953  ? 0.2472 0.2073 0.2256 0.0058  -0.0286 -0.0315 951  TYR B C   
16035 O O   . TYR B 953  ? 0.2603 0.2217 0.2357 0.0066  -0.0272 -0.0310 951  TYR B O   
16036 C CB  . TYR B 953  ? 0.2393 0.2034 0.2279 0.0054  -0.0263 -0.0298 951  TYR B CB  
16037 C CG  . TYR B 953  ? 0.2055 0.1712 0.1919 0.0069  -0.0233 -0.0296 951  TYR B CG  
16038 C CD1 . TYR B 953  ? 0.1940 0.1632 0.1827 0.0070  -0.0218 -0.0280 951  TYR B CD1 
16039 C CD2 . TYR B 953  ? 0.2072 0.1708 0.1893 0.0084  -0.0220 -0.0310 951  TYR B CD2 
16040 C CE1 . TYR B 953  ? 0.2106 0.1816 0.1975 0.0080  -0.0191 -0.0277 951  TYR B CE1 
16041 C CE2 . TYR B 953  ? 0.2438 0.2095 0.2243 0.0097  -0.0192 -0.0307 951  TYR B CE2 
16042 C CZ  . TYR B 953  ? 0.2426 0.2122 0.2257 0.0094  -0.0178 -0.0290 951  TYR B CZ  
16043 O OH  . TYR B 953  ? 0.2362 0.2081 0.2177 0.0104  -0.0152 -0.0286 951  TYR B OH  
16044 N N   . ARG B 954  ? 0.2899 0.2460 0.2654 0.0058  -0.0300 -0.0333 952  ARG B N   
16045 C CA  . ARG B 954  ? 0.3298 0.2828 0.2983 0.0073  -0.0295 -0.0350 952  ARG B CA  
16046 C C   . ARG B 954  ? 0.2806 0.2337 0.2488 0.0090  -0.0264 -0.0355 952  ARG B C   
16047 O O   . ARG B 954  ? 0.2713 0.2243 0.2435 0.0088  -0.0260 -0.0353 952  ARG B O   
16048 C CB  . ARG B 954  ? 0.3189 0.2669 0.2841 0.0066  -0.0325 -0.0369 952  ARG B CB  
16049 N N   . ARG B 955  ? 0.3038 0.2575 0.2675 0.0108  -0.0243 -0.0360 953  ARG B N   
16050 C CA  . ARG B 955  ? 0.3266 0.2813 0.2903 0.0127  -0.0213 -0.0363 953  ARG B CA  
16051 C C   . ARG B 955  ? 0.3321 0.2825 0.2951 0.0135  -0.0218 -0.0380 953  ARG B C   
16052 O O   . ARG B 955  ? 0.3193 0.2705 0.2851 0.0144  -0.0201 -0.0377 953  ARG B O   
16053 C CB  . ARG B 955  ? 0.4051 0.3613 0.3636 0.0145  -0.0191 -0.0367 953  ARG B CB  
16054 C CG  . ARG B 955  ? 0.4356 0.3938 0.3943 0.0167  -0.0159 -0.0369 953  ARG B CG  
16055 C CD  . ARG B 955  ? 0.3979 0.3600 0.3632 0.0161  -0.0144 -0.0351 953  ARG B CD  
16056 N NE  . ARG B 955  ? 0.4301 0.3944 0.3955 0.0182  -0.0115 -0.0353 953  ARG B NE  
16057 C CZ  . ARG B 955  ? 0.4587 0.4203 0.4235 0.0200  -0.0112 -0.0366 953  ARG B CZ  
16058 N NH1 . ARG B 955  ? 0.4380 0.3943 0.4020 0.0195  -0.0135 -0.0379 953  ARG B NH1 
16059 N NH2 . ARG B 955  ? 0.3925 0.3568 0.3574 0.0221  -0.0085 -0.0366 953  ARG B NH2 
16060 N N   . ASP B 956  ? 0.3206 0.2660 0.2796 0.0131  -0.0244 -0.0397 954  ASP B N   
16061 C CA  A ASP B 956  ? 0.3468 0.2871 0.3047 0.0136  -0.0253 -0.0414 954  ASP B CA  
16062 C CA  B ASP B 956  ? 0.3467 0.2871 0.3046 0.0137  -0.0252 -0.0413 954  ASP B CA  
16063 C C   . ASP B 956  ? 0.3525 0.2930 0.3168 0.0117  -0.0262 -0.0402 954  ASP B C   
16064 O O   . ASP B 956  ? 0.3774 0.3142 0.3416 0.0122  -0.0265 -0.0411 954  ASP B O   
16065 C CB  A ASP B 956  ? 0.3521 0.2867 0.3041 0.0133  -0.0282 -0.0435 954  ASP B CB  
16066 C CB  B ASP B 956  ? 0.3507 0.2852 0.3021 0.0139  -0.0277 -0.0437 954  ASP B CB  
16067 C CG  A ASP B 956  ? 0.4181 0.3519 0.3630 0.0156  -0.0270 -0.0450 954  ASP B CG  
16068 C CG  B ASP B 956  ? 0.3382 0.2717 0.2901 0.0112  -0.0312 -0.0435 954  ASP B CG  
16069 O OD1 A ASP B 956  ? 0.4426 0.3789 0.3865 0.0179  -0.0238 -0.0449 954  ASP B OD1 
16070 O OD1 B ASP B 956  ? 0.4011 0.3381 0.3590 0.0091  -0.0320 -0.0416 954  ASP B OD1 
16071 O OD2 A ASP B 956  ? 0.4402 0.3711 0.3803 0.0150  -0.0293 -0.0461 954  ASP B OD2 
16072 O OD2 B ASP B 956  ? 0.4270 0.3564 0.3730 0.0113  -0.0332 -0.0452 954  ASP B OD2 
16073 N N   . ASP B 957  ? 0.2924 0.2369 0.2620 0.0098  -0.0268 -0.0383 955  ASP B N   
16074 C CA  . ASP B 957  ? 0.3157 0.2613 0.2916 0.0079  -0.0275 -0.0370 955  ASP B CA  
16075 C C   . ASP B 957  ? 0.2652 0.2154 0.2456 0.0087  -0.0245 -0.0353 955  ASP B C   
16076 O O   . ASP B 957  ? 0.2709 0.2232 0.2569 0.0072  -0.0247 -0.0339 955  ASP B O   
16077 C CB  . ASP B 957  ? 0.3422 0.2898 0.3214 0.0055  -0.0300 -0.0359 955  ASP B CB  
16078 C CG  . ASP B 957  ? 0.4503 0.3934 0.4264 0.0041  -0.0335 -0.0374 955  ASP B CG  
16079 O OD1 . ASP B 957  ? 0.4491 0.3870 0.4220 0.0044  -0.0343 -0.0390 955  ASP B OD1 
16080 O OD2 . ASP B 957  ? 0.4842 0.4287 0.4608 0.0027  -0.0356 -0.0369 955  ASP B OD2 
16081 N N   . LEU B 958  ? 0.2521 0.2043 0.2304 0.0108  -0.0219 -0.0354 956  LEU B N   
16082 C CA  . LEU B 958  ? 0.2324 0.1892 0.2147 0.0114  -0.0192 -0.0337 956  LEU B CA  
16083 C C   . LEU B 958  ? 0.2481 0.2040 0.2341 0.0113  -0.0188 -0.0333 956  LEU B C   
16084 O O   . LEU B 958  ? 0.2331 0.1923 0.2241 0.0103  -0.0181 -0.0317 956  LEU B O   
16085 C CB  . LEU B 958  ? 0.2503 0.2089 0.2293 0.0137  -0.0166 -0.0341 956  LEU B CB  
16086 C CG  . LEU B 958  ? 0.2329 0.1963 0.2156 0.0144  -0.0139 -0.0326 956  LEU B CG  
16087 C CD1 . LEU B 958  ? 0.2623 0.2295 0.2491 0.0126  -0.0141 -0.0307 956  LEU B CD1 
16088 C CD2 . LEU B 958  ? 0.2777 0.2432 0.2570 0.0165  -0.0116 -0.0330 956  LEU B CD2 
16089 N N   . ASP B 959  ? 0.2380 0.1891 0.2210 0.0122  -0.0192 -0.0348 957  ASP B N   
16090 C CA  . ASP B 959  ? 0.2145 0.1643 0.2004 0.0122  -0.0188 -0.0343 957  ASP B CA  
16091 C C   . ASP B 959  ? 0.2235 0.1735 0.2142 0.0093  -0.0207 -0.0331 957  ASP B C   
16092 O O   . ASP B 959  ? 0.2347 0.1871 0.2300 0.0087  -0.0197 -0.0316 957  ASP B O   
16093 C CB  . ASP B 959  ? 0.2354 0.1792 0.2168 0.0139  -0.0192 -0.0362 957  ASP B CB  
16094 C CG  . ASP B 959  ? 0.2682 0.2112 0.2517 0.0148  -0.0179 -0.0355 957  ASP B CG  
16095 O OD1 . ASP B 959  ? 0.2560 0.2037 0.2422 0.0158  -0.0155 -0.0342 957  ASP B OD1 
16096 O OD2 . ASP B 959  ? 0.2674 0.2049 0.2496 0.0144  -0.0194 -0.0362 957  ASP B OD2 
16097 N N   . ARG B 960  ? 0.2265 0.1744 0.2163 0.0075  -0.0234 -0.0337 958  ARG B N   
16098 C CA  . ARG B 960  ? 0.2305 0.1795 0.2251 0.0046  -0.0252 -0.0325 958  ARG B CA  
16099 C C   . ARG B 960  ? 0.2282 0.1836 0.2278 0.0041  -0.0241 -0.0306 958  ARG B C   
16100 O O   . ARG B 960  ? 0.2197 0.1775 0.2244 0.0026  -0.0241 -0.0292 958  ARG B O   
16101 C CB  . ARG B 960  ? 0.2797 0.2257 0.2722 0.0029  -0.0285 -0.0336 958  ARG B CB  
16102 N N   . LEU B 961  ? 0.2076 0.1656 0.2055 0.0052  -0.0232 -0.0306 959  LEU B N   
16103 C CA  . LEU B 961  ? 0.2047 0.1680 0.2066 0.0049  -0.0221 -0.0289 959  LEU B CA  
16104 C C   . LEU B 961  ? 0.2034 0.1692 0.2086 0.0056  -0.0196 -0.0278 959  LEU B C   
16105 O O   . LEU B 961  ? 0.2098 0.1791 0.2198 0.0047  -0.0192 -0.0264 959  LEU B O   
16106 C CB  . LEU B 961  ? 0.1992 0.1641 0.1981 0.0060  -0.0215 -0.0291 959  LEU B CB  
16107 C CG  . LEU B 961  ? 0.2153 0.1850 0.2175 0.0059  -0.0202 -0.0275 959  LEU B CG  
16108 C CD1 . LEU B 961  ? 0.2466 0.2180 0.2528 0.0043  -0.0222 -0.0265 959  LEU B CD1 
16109 C CD2 . LEU B 961  ? 0.2441 0.2146 0.2425 0.0069  -0.0193 -0.0276 959  LEU B CD2 
16110 N N   . VAL B 962  ? 0.1864 0.1509 0.1891 0.0074  -0.0178 -0.0284 960  VAL B N   
16111 C CA  . VAL B 962  ? 0.1931 0.1598 0.1986 0.0081  -0.0156 -0.0273 960  VAL B CA  
16112 C C   . VAL B 962  ? 0.2026 0.1684 0.2118 0.0065  -0.0164 -0.0265 960  VAL B C   
16113 O O   . VAL B 962  ? 0.1987 0.1678 0.2120 0.0060  -0.0153 -0.0251 960  VAL B O   
16114 C CB  . VAL B 962  ? 0.2122 0.1775 0.2142 0.0105  -0.0139 -0.0282 960  VAL B CB  
16115 C CG1 . VAL B 962  ? 0.2242 0.1912 0.2291 0.0111  -0.0120 -0.0271 960  VAL B CG1 
16116 C CG2 . VAL B 962  ? 0.2236 0.1914 0.2230 0.0118  -0.0126 -0.0285 960  VAL B CG2 
16117 N N   . ASP B 963  ? 0.2041 0.1653 0.2118 0.0056  -0.0184 -0.0274 961  ASP B N   
16118 C CA  . ASP B 963  ? 0.2234 0.1839 0.2347 0.0035  -0.0194 -0.0265 961  ASP B CA  
16119 C C   . ASP B 963  ? 0.2130 0.1782 0.2294 0.0017  -0.0200 -0.0251 961  ASP B C   
16120 O O   . ASP B 963  ? 0.2365 0.2042 0.2571 0.0007  -0.0193 -0.0236 961  ASP B O   
16121 C CB  . ASP B 963  ? 0.2418 0.1967 0.2506 0.0022  -0.0220 -0.0277 961  ASP B CB  
16122 C CG  . ASP B 963  ? 0.3027 0.2522 0.3068 0.0040  -0.0216 -0.0290 961  ASP B CG  
16123 O OD1 . ASP B 963  ? 0.3079 0.2584 0.3120 0.0059  -0.0193 -0.0286 961  ASP B OD1 
16124 O OD2 . ASP B 963  ? 0.3209 0.2651 0.3214 0.0035  -0.0237 -0.0305 961  ASP B OD2 
16125 N N   . ASP B 964  ? 0.1972 0.1636 0.2130 0.0013  -0.0214 -0.0255 962  ASP B N   
16126 C CA  . ASP B 964  ? 0.2132 0.1840 0.2336 -0.0001 -0.0221 -0.0243 962  ASP B CA  
16127 C C   . ASP B 964  ? 0.2187 0.1941 0.2420 0.0009  -0.0197 -0.0230 962  ASP B C   
16128 O O   . ASP B 964  ? 0.2157 0.1945 0.2437 -0.0001 -0.0194 -0.0217 962  ASP B O   
16129 C CB  . ASP B 964  ? 0.2151 0.1861 0.2336 -0.0002 -0.0239 -0.0250 962  ASP B CB  
16130 C CG  . ASP B 964  ? 0.2683 0.2352 0.2844 -0.0016 -0.0268 -0.0262 962  ASP B CG  
16131 O OD1 . ASP B 964  ? 0.2767 0.2409 0.2934 -0.0028 -0.0276 -0.0263 962  ASP B OD1 
16132 O OD2 . ASP B 964  ? 0.3510 0.3172 0.3644 -0.0014 -0.0284 -0.0270 962  ASP B OD2 
16133 N N   . VAL B 965  ? 0.1836 0.1593 0.2043 0.0028  -0.0178 -0.0233 963  VAL B N   
16134 C CA  . VAL B 965  ? 0.1697 0.1492 0.1927 0.0036  -0.0156 -0.0222 963  VAL B CA  
16135 C C   . VAL B 965  ? 0.1869 0.1669 0.2126 0.0034  -0.0143 -0.0213 963  VAL B C   
16136 O O   . VAL B 965  ? 0.1974 0.1808 0.2269 0.0029  -0.0135 -0.0201 963  VAL B O   
16137 C CB  . VAL B 965  ? 0.1805 0.1601 0.1999 0.0054  -0.0141 -0.0227 963  VAL B CB  
16138 C CG1 . VAL B 965  ? 0.1835 0.1667 0.2051 0.0061  -0.0120 -0.0216 963  VAL B CG1 
16139 C CG2 . VAL B 965  ? 0.2121 0.1915 0.2289 0.0055  -0.0153 -0.0233 963  VAL B CG2 
16140 N N   . ASN B 966  ? 0.1882 0.1646 0.2116 0.0037  -0.0142 -0.0219 964  ASN B N   
16141 C CA  . ASN B 966  ? 0.1937 0.1701 0.2192 0.0035  -0.0131 -0.0208 964  ASN B CA  
16142 C C   . ASN B 966  ? 0.1988 0.1761 0.2284 0.0012  -0.0142 -0.0198 964  ASN B C   
16143 O O   . ASN B 966  ? 0.2298 0.2090 0.2623 0.0007  -0.0130 -0.0185 964  ASN B O   
16144 C CB  . ASN B 966  ? 0.1880 0.1598 0.2100 0.0044  -0.0130 -0.0217 964  ASN B CB  
16145 C CG  . ASN B 966  ? 0.1963 0.1683 0.2151 0.0069  -0.0113 -0.0224 964  ASN B CG  
16146 O OD1 . ASN B 966  ? 0.2074 0.1833 0.2273 0.0077  -0.0098 -0.0218 964  ASN B OD1 
16147 N ND2 . ASN B 966  ? 0.2186 0.1865 0.2335 0.0082  -0.0115 -0.0236 964  ASN B ND2 
16148 N N   . ALA B 967  ? 0.1975 0.1735 0.2272 -0.0003 -0.0165 -0.0204 965  ALA B N   
16149 C CA  . ALA B 967  ? 0.2127 0.1895 0.2461 -0.0028 -0.0179 -0.0194 965  ALA B CA  
16150 C C   . ALA B 967  ? 0.2060 0.1887 0.2446 -0.0034 -0.0171 -0.0179 965  ALA B C   
16151 O O   . ALA B 967  ? 0.2183 0.2027 0.2606 -0.0053 -0.0176 -0.0168 965  ALA B O   
16152 C CB  . ALA B 967  ? 0.2122 0.1864 0.2444 -0.0043 -0.0208 -0.0204 965  ALA B CB  
16153 N N   . THR B 968  ? 0.1772 0.1631 0.2160 -0.0017 -0.0158 -0.0179 966  THR B N   
16154 C CA  . THR B 968  ? 0.1958 0.1870 0.2391 -0.0019 -0.0149 -0.0166 966  THR B CA  
16155 C C   . THR B 968  ? 0.1882 0.1809 0.2336 -0.0020 -0.0128 -0.0153 966  THR B C   
16156 O O   . THR B 968  ? 0.2060 0.2030 0.2555 -0.0025 -0.0121 -0.0142 966  THR B O   
16157 C CB  . THR B 968  ? 0.1881 0.1815 0.2307 -0.0001 -0.0140 -0.0169 966  THR B CB  
16158 O OG1 . THR B 968  ? 0.1903 0.1830 0.2306 0.0014  -0.0119 -0.0170 966  THR B OG1 
16159 C CG2 . THR B 968  ? 0.2070 0.1985 0.2466 0.0003  -0.0158 -0.0181 966  THR B CG2 
16160 N N   . GLY B 969  ? 0.1963 0.1858 0.2389 -0.0014 -0.0119 -0.0155 967  GLY B N   
16161 C CA  . GLY B 969  ? 0.1950 0.1855 0.2388 -0.0012 -0.0099 -0.0143 967  GLY B CA  
16162 C C   . GLY B 969  ? 0.1914 0.1843 0.2346 0.0008  -0.0078 -0.0142 967  GLY B C   
16163 O O   . GLY B 969  ? 0.1845 0.1777 0.2277 0.0012  -0.0062 -0.0134 967  GLY B O   
16164 N N   . TYR B 970  ? 0.1815 0.1759 0.2240 0.0018  -0.0080 -0.0150 968  TYR B N   
16165 C CA  A TYR B 970  ? 0.1637 0.1597 0.2050 0.0035  -0.0063 -0.0150 968  TYR B CA  
16166 C CA  B TYR B 970  ? 0.1641 0.1601 0.2054 0.0035  -0.0063 -0.0150 968  TYR B CA  
16167 C C   . TYR B 970  ? 0.1689 0.1620 0.2061 0.0047  -0.0059 -0.0159 968  TYR B C   
16168 O O   . TYR B 970  ? 0.1977 0.1874 0.2326 0.0046  -0.0070 -0.0167 968  TYR B O   
16169 C CB  A TYR B 970  ? 0.1683 0.1668 0.2105 0.0040  -0.0066 -0.0153 968  TYR B CB  
16170 C CB  B TYR B 970  ? 0.1684 0.1667 0.2104 0.0040  -0.0067 -0.0153 968  TYR B CB  
16171 C CG  A TYR B 970  ? 0.1859 0.1882 0.2322 0.0036  -0.0063 -0.0143 968  TYR B CG  
16172 C CG  B TYR B 970  ? 0.1716 0.1734 0.2178 0.0033  -0.0069 -0.0145 968  TYR B CG  
16173 C CD1 A TYR B 970  ? 0.1740 0.1788 0.2215 0.0042  -0.0044 -0.0135 968  TYR B CD1 
16174 C CD1 B TYR B 970  ? 0.1808 0.1858 0.2290 0.0039  -0.0053 -0.0137 968  TYR B CD1 
16175 C CD2 A TYR B 970  ? 0.1866 0.1904 0.2355 0.0026  -0.0079 -0.0142 968  TYR B CD2 
16176 C CD2 B TYR B 970  ? 0.1612 0.1634 0.2094 0.0021  -0.0088 -0.0145 968  TYR B CD2 
16177 C CE1 A TYR B 970  ? 0.2010 0.2095 0.2520 0.0041  -0.0039 -0.0128 968  TYR B CE1 
16178 C CE1 B TYR B 970  ? 0.2112 0.2198 0.2633 0.0036  -0.0053 -0.0130 968  TYR B CE1 
16179 C CE2 A TYR B 970  ? 0.1897 0.1977 0.2426 0.0025  -0.0074 -0.0134 968  TYR B CE2 
16180 C CE2 B TYR B 970  ? 0.2160 0.2221 0.2684 0.0016  -0.0090 -0.0137 968  TYR B CE2 
16181 C CZ  A TYR B 970  ? 0.2072 0.2174 0.2610 0.0034  -0.0053 -0.0127 968  TYR B CZ  
16182 C CZ  B TYR B 970  ? 0.2131 0.2225 0.2675 0.0024  -0.0071 -0.0130 968  TYR B CZ  
16183 O OH  A TYR B 970  ? 0.2096 0.2242 0.2672 0.0035  -0.0047 -0.0119 968  TYR B OH  
16184 O OH  B TYR B 970  ? 0.2355 0.2493 0.2941 0.0022  -0.0071 -0.0122 968  TYR B OH  
16185 N N   . GLY B 971  ? 0.1618 0.1565 0.1981 0.0059  -0.0044 -0.0158 969  GLY B N   
16186 C CA  . GLY B 971  ? 0.1688 0.1618 0.2016 0.0072  -0.0038 -0.0165 969  GLY B CA  
16187 C C   . GLY B 971  ? 0.1464 0.1419 0.1788 0.0081  -0.0024 -0.0162 969  GLY B C   
16188 O O   . GLY B 971  ? 0.1566 0.1523 0.1882 0.0089  -0.0012 -0.0159 969  GLY B O   
16189 N N   . LEU B 972  ? 0.1416 0.1387 0.1743 0.0080  -0.0026 -0.0163 970  LEU B N   
16190 C CA  . LEU B 972  ? 0.1473 0.1465 0.1795 0.0086  -0.0014 -0.0161 970  LEU B CA  
16191 C C   . LEU B 972  ? 0.1388 0.1375 0.1680 0.0091  -0.0015 -0.0167 970  LEU B C   
16192 O O   . LEU B 972  ? 0.1536 0.1523 0.1813 0.0098  -0.0007 -0.0168 970  LEU B O   
16193 C CB  . LEU B 972  ? 0.1642 0.1652 0.1985 0.0083  -0.0015 -0.0157 970  LEU B CB  
16194 C CG  . LEU B 972  ? 0.1422 0.1449 0.1760 0.0088  -0.0004 -0.0154 970  LEU B CG  
16195 C CD1 . LEU B 972  ? 0.1818 0.1855 0.2158 0.0091  0.0010  -0.0149 970  LEU B CD1 
16196 C CD2 . LEU B 972  ? 0.1708 0.1748 0.2065 0.0088  -0.0006 -0.0152 970  LEU B CD2 
16197 N N   . THR B 973  ? 0.1411 0.1395 0.1695 0.0087  -0.0024 -0.0171 971  THR B N   
16198 C CA  . THR B 973  ? 0.1424 0.1405 0.1678 0.0089  -0.0024 -0.0175 971  THR B CA  
16199 C C   . THR B 973  ? 0.1284 0.1243 0.1520 0.0088  -0.0036 -0.0183 971  THR B C   
16200 O O   . THR B 973  ? 0.1572 0.1519 0.1820 0.0083  -0.0049 -0.0184 971  THR B O   
16201 C CB  . THR B 973  ? 0.1315 0.1304 0.1562 0.0085  -0.0024 -0.0172 971  THR B CB  
16202 O OG1 . THR B 973  ? 0.1476 0.1459 0.1735 0.0082  -0.0037 -0.0172 971  THR B OG1 
16203 C CG2 . THR B 973  ? 0.1676 0.1685 0.1934 0.0086  -0.0012 -0.0166 971  THR B CG2 
16204 N N   . PHE B 974  ? 0.1398 0.1354 0.1605 0.0092  -0.0033 -0.0187 972  PHE B N   
16205 C CA  . PHE B 974  ? 0.1436 0.1370 0.1619 0.0093  -0.0044 -0.0196 972  PHE B CA  
16206 C C   . PHE B 974  ? 0.1501 0.1443 0.1652 0.0095  -0.0038 -0.0197 972  PHE B C   
16207 O O   . PHE B 974  ? 0.1534 0.1495 0.1680 0.0101  -0.0023 -0.0195 972  PHE B O   
16208 C CB  . PHE B 974  ? 0.1354 0.1269 0.1531 0.0100  -0.0044 -0.0203 972  PHE B CB  
16209 C CG  . PHE B 974  ? 0.1497 0.1387 0.1641 0.0103  -0.0054 -0.0213 972  PHE B CG  
16210 C CD1 . PHE B 974  ? 0.1776 0.1645 0.1920 0.0094  -0.0073 -0.0218 972  PHE B CD1 
16211 C CD2 . PHE B 974  ? 0.1622 0.1514 0.1735 0.0115  -0.0044 -0.0219 972  PHE B CD2 
16212 C CE1 . PHE B 974  ? 0.1804 0.1648 0.1912 0.0097  -0.0083 -0.0229 972  PHE B CE1 
16213 C CE2 . PHE B 974  ? 0.1733 0.1602 0.1811 0.0119  -0.0052 -0.0230 972  PHE B CE2 
16214 C CZ  . PHE B 974  ? 0.1756 0.1599 0.1830 0.0110  -0.0072 -0.0235 972  PHE B CZ  
16215 N N   . GLY B 975  ? 0.1529 0.1457 0.1658 0.0090  -0.0049 -0.0200 973  GLY B N   
16216 C CA  . GLY B 975  ? 0.1523 0.1459 0.1619 0.0090  -0.0043 -0.0200 973  GLY B CA  
16217 C C   . GLY B 975  ? 0.1595 0.1511 0.1657 0.0096  -0.0050 -0.0210 973  GLY B C   
16218 O O   . GLY B 975  ? 0.1657 0.1548 0.1718 0.0094  -0.0065 -0.0217 973  GLY B O   
16219 N N   . LEU B 976  ? 0.1598 0.1527 0.1633 0.0101  -0.0037 -0.0212 974  LEU B N   
16220 C CA  . LEU B 976  ? 0.1668 0.1580 0.1665 0.0108  -0.0041 -0.0222 974  LEU B CA  
16221 C C   . LEU B 976  ? 0.1818 0.1750 0.1786 0.0103  -0.0033 -0.0216 974  LEU B C   
16222 O O   . LEU B 976  ? 0.1814 0.1779 0.1788 0.0103  -0.0016 -0.0209 974  LEU B O   
16223 C CB  . LEU B 976  ? 0.1881 0.1791 0.1870 0.0126  -0.0031 -0.0232 974  LEU B CB  
16224 C CG  . LEU B 976  ? 0.2053 0.1948 0.1997 0.0137  -0.0031 -0.0245 974  LEU B CG  
16225 C CD1 . LEU B 976  ? 0.2272 0.2125 0.2200 0.0132  -0.0054 -0.0254 974  LEU B CD1 
16226 C CD2 . LEU B 976  ? 0.2096 0.1989 0.2034 0.0159  -0.0019 -0.0255 974  LEU B CD2 
16227 N N   . HIS B 977  ? 0.1674 0.1588 0.1613 0.0097  -0.0045 -0.0217 975  HIS B N   
16228 C CA  . HIS B 977  ? 0.1838 0.1767 0.1743 0.0091  -0.0037 -0.0211 975  HIS B CA  
16229 C C   . HIS B 977  ? 0.1899 0.1815 0.1762 0.0103  -0.0036 -0.0223 975  HIS B C   
16230 O O   . HIS B 977  ? 0.1929 0.1812 0.1772 0.0103  -0.0054 -0.0232 975  HIS B O   
16231 C CB  . HIS B 977  ? 0.2015 0.1930 0.1913 0.0074  -0.0052 -0.0200 975  HIS B CB  
16232 C CG  . HIS B 977  ? 0.2030 0.1963 0.1951 0.0062  -0.0046 -0.0186 975  HIS B CG  
16233 N ND1 . HIS B 977  ? 0.2934 0.2881 0.2833 0.0049  -0.0039 -0.0174 975  HIS B ND1 
16234 C CD2 . HIS B 977  ? 0.2630 0.2567 0.2590 0.0060  -0.0047 -0.0182 975  HIS B CD2 
16235 C CE1 . HIS B 977  ? 0.2596 0.2552 0.2521 0.0040  -0.0038 -0.0164 975  HIS B CE1 
16236 N NE2 . HIS B 977  ? 0.2801 0.2752 0.2761 0.0047  -0.0042 -0.0170 975  HIS B NE2 
16237 N N   . THR B 978  ? 0.1871 0.1817 0.1720 0.0113  -0.0016 -0.0225 976  THR B N   
16238 C CA  . THR B 978  ? 0.1868 0.1807 0.1673 0.0128  -0.0010 -0.0238 976  THR B CA  
16239 C C   . THR B 978  ? 0.1939 0.1927 0.1736 0.0135  0.0016  -0.0233 976  THR B C   
16240 O O   . THR B 978  ? 0.2113 0.2135 0.1944 0.0133  0.0028  -0.0224 976  THR B O   
16241 C CB  . THR B 978  ? 0.2182 0.2092 0.1987 0.0148  -0.0016 -0.0256 976  THR B CB  
16242 O OG1 . THR B 978  ? 0.2181 0.2083 0.1939 0.0164  -0.0010 -0.0270 976  THR B OG1 
16243 C CG2 . THR B 978  ? 0.2337 0.2268 0.2177 0.0159  -0.0002 -0.0256 976  THR B CG2 
16244 N N   . ARG B 979  ? 0.2183 0.2177 0.1936 0.0142  0.0023  -0.0238 977  ARG B N   
16245 C CA  . ARG B 979  ? 0.2209 0.2255 0.1954 0.0152  0.0050  -0.0234 977  ARG B CA  
16246 C C   . ARG B 979  ? 0.2315 0.2361 0.2048 0.0184  0.0060  -0.0253 977  ARG B C   
16247 O O   . ARG B 979  ? 0.2334 0.2426 0.2061 0.0197  0.0083  -0.0252 977  ARG B O   
16248 C CB  . ARG B 979  ? 0.2616 0.2678 0.2319 0.0140  0.0056  -0.0226 977  ARG B CB  
16249 C CG  . ARG B 979  ? 0.3486 0.3553 0.3200 0.0109  0.0049  -0.0205 977  ARG B CG  
16250 C CD  . ARG B 979  ? 0.4160 0.4230 0.3827 0.0096  0.0050  -0.0196 977  ARG B CD  
16251 N NE  . ARG B 979  ? 0.5189 0.5269 0.4866 0.0067  0.0047  -0.0173 977  ARG B NE  
16252 C CZ  . ARG B 979  ? 0.5594 0.5680 0.5234 0.0049  0.0049  -0.0159 977  ARG B CZ  
16253 N NH1 . ARG B 979  ? 0.4671 0.4757 0.4262 0.0058  0.0055  -0.0165 977  ARG B NH1 
16254 N NH2 . ARG B 979  ? 0.4963 0.5051 0.4613 0.0022  0.0045  -0.0138 977  ARG B NH2 
16255 N N   . LEU B 980  ? 0.2009 0.2004 0.1738 0.0196  0.0045  -0.0269 978  LEU B N   
16256 C CA  . LEU B 980  ? 0.1971 0.1950 0.1673 0.0227  0.0050  -0.0290 978  LEU B CA  
16257 C C   . LEU B 980  ? 0.2148 0.2126 0.1887 0.0243  0.0054  -0.0294 978  LEU B C   
16258 O O   . LEU B 980  ? 0.2095 0.2040 0.1861 0.0234  0.0037  -0.0294 978  LEU B O   
16259 C CB  . LEU B 980  ? 0.2101 0.2016 0.1765 0.0228  0.0028  -0.0306 978  LEU B CB  
16260 C CG  . LEU B 980  ? 0.2427 0.2336 0.2054 0.0212  0.0019  -0.0301 978  LEU B CG  
16261 C CD1 . LEU B 980  ? 0.2670 0.2515 0.2261 0.0213  -0.0006 -0.0318 978  LEU B CD1 
16262 C CD2 . LEU B 980  ? 0.2528 0.2480 0.2118 0.0222  0.0044  -0.0300 978  LEU B CD2 
16263 N N   . ASP B 981  ? 0.1979 0.1994 0.1717 0.0268  0.0076  -0.0298 979  ASP B N   
16264 C CA  . ASP B 981  ? 0.1987 0.2005 0.1759 0.0285  0.0080  -0.0299 979  ASP B CA  
16265 C C   . ASP B 981  ? 0.2149 0.2098 0.1910 0.0297  0.0061  -0.0316 979  ASP B C   
16266 O O   . ASP B 981  ? 0.2081 0.2016 0.1876 0.0297  0.0055  -0.0313 979  ASP B O   
16267 C CB  . ASP B 981  ? 0.2234 0.2304 0.2003 0.0314  0.0105  -0.0302 979  ASP B CB  
16268 C CG  . ASP B 981  ? 0.2293 0.2439 0.2087 0.0300  0.0123  -0.0283 979  ASP B CG  
16269 O OD1 . ASP B 981  ? 0.2501 0.2656 0.2322 0.0269  0.0116  -0.0266 979  ASP B OD1 
16270 O OD2 . ASP B 981  ? 0.2792 0.2989 0.2577 0.0320  0.0145  -0.0284 979  ASP B OD2 
16271 N N   . GLU B 982  ? 0.2191 0.2095 0.1903 0.0308  0.0052  -0.0334 980  GLU B N   
16272 C CA  . GLU B 982  ? 0.2262 0.2096 0.1962 0.0316  0.0033  -0.0350 980  GLU B CA  
16273 C C   . GLU B 982  ? 0.2117 0.1922 0.1849 0.0285  0.0010  -0.0341 980  GLU B C   
16274 O O   . GLU B 982  ? 0.2193 0.1963 0.1945 0.0285  -0.0002 -0.0343 980  GLU B O   
16275 C CB  . GLU B 982  ? 0.2445 0.2234 0.2083 0.0331  0.0025  -0.0372 980  GLU B CB  
16276 C CG  . GLU B 982  ? 0.2968 0.2680 0.2590 0.0336  0.0002  -0.0389 980  GLU B CG  
16277 C CD  . GLU B 982  ? 0.3510 0.3169 0.3072 0.0339  -0.0014 -0.0409 980  GLU B CD  
16278 O OE1 . GLU B 982  ? 0.3859 0.3528 0.3405 0.0320  -0.0020 -0.0405 980  GLU B OE1 
16279 O OE2 . GLU B 982  ? 0.3326 0.2931 0.2854 0.0361  -0.0022 -0.0429 980  GLU B OE2 
16280 N N   . THR B 983  ? 0.1976 0.1795 0.1712 0.0259  0.0003  -0.0330 981  THR B N   
16281 C CA  . THR B 983  ? 0.2031 0.1829 0.1799 0.0232  -0.0018 -0.0321 981  THR B CA  
16282 C C   . THR B 983  ? 0.2023 0.1852 0.1846 0.0224  -0.0010 -0.0305 981  THR B C   
16283 O O   . THR B 983  ? 0.2011 0.1815 0.1863 0.0215  -0.0023 -0.0302 981  THR B O   
16284 C CB  . THR B 983  ? 0.2295 0.2101 0.2051 0.0210  -0.0026 -0.0313 981  THR B CB  
16285 O OG1 . THR B 983  ? 0.2285 0.2056 0.1987 0.0217  -0.0037 -0.0329 981  THR B OG1 
16286 C CG2 . THR B 983  ? 0.2204 0.1996 0.1996 0.0185  -0.0047 -0.0303 981  THR B CG2 
16287 N N   . ILE B 984  ? 0.1832 0.1716 0.1670 0.0229  0.0011  -0.0294 982  ILE B N   
16288 C CA  . ILE B 984  ? 0.1864 0.1778 0.1749 0.0224  0.0019  -0.0280 982  ILE B CA  
16289 C C   . ILE B 984  ? 0.1938 0.1828 0.1834 0.0242  0.0019  -0.0287 982  ILE B C   
16290 O O   . ILE B 984  ? 0.1920 0.1797 0.1848 0.0232  0.0011  -0.0280 982  ILE B O   
16291 C CB  . ILE B 984  ? 0.1893 0.1871 0.1787 0.0225  0.0041  -0.0268 982  ILE B CB  
16292 C CG1 . ILE B 984  ? 0.2359 0.2355 0.2244 0.0201  0.0039  -0.0258 982  ILE B CG1 
16293 C CG2 . ILE B 984  ? 0.2079 0.2085 0.2018 0.0222  0.0048  -0.0256 982  ILE B CG2 
16294 C CD1 . ILE B 984  ? 0.2386 0.2441 0.2271 0.0200  0.0059  -0.0247 982  ILE B CD1 
16295 N N   . ALA B 985  ? 0.1922 0.1802 0.1788 0.0271  0.0027  -0.0301 983  ALA B N   
16296 C CA  . ALA B 985  ? 0.2025 0.1877 0.1897 0.0290  0.0026  -0.0307 983  ALA B CA  
16297 C C   . ALA B 985  ? 0.1996 0.1783 0.1867 0.0278  0.0002  -0.0313 983  ALA B C   
16298 O O   . ALA B 985  ? 0.2155 0.1926 0.2053 0.0274  -0.0003 -0.0307 983  ALA B O   
16299 C CB  . ALA B 985  ? 0.1995 0.1844 0.1830 0.0326  0.0038  -0.0323 983  ALA B CB  
16300 N N   . HIS B 986  ? 0.2036 0.1787 0.1875 0.0270  -0.0013 -0.0324 984  HIS B N   
16301 C CA  . HIS B 986  ? 0.2288 0.1980 0.2125 0.0256  -0.0037 -0.0330 984  HIS B CA  
16302 C C   . HIS B 986  ? 0.2079 0.1785 0.1966 0.0227  -0.0045 -0.0313 984  HIS B C   
16303 O O   . HIS B 986  ? 0.2148 0.1833 0.2059 0.0222  -0.0052 -0.0308 984  HIS B O   
16304 C CB  . HIS B 986  ? 0.2391 0.2051 0.2185 0.0250  -0.0052 -0.0344 984  HIS B CB  
16305 C CG  . HIS B 986  ? 0.2312 0.1918 0.2107 0.0230  -0.0080 -0.0349 984  HIS B CG  
16306 N ND1 . HIS B 986  ? 0.3075 0.2643 0.2829 0.0225  -0.0099 -0.0363 984  HIS B ND1 
16307 C CD2 . HIS B 986  ? 0.2641 0.2227 0.2471 0.0213  -0.0093 -0.0341 984  HIS B CD2 
16308 C CE1 . HIS B 986  ? 0.3115 0.2645 0.2883 0.0204  -0.0123 -0.0364 984  HIS B CE1 
16309 N NE2 . HIS B 986  ? 0.2668 0.2209 0.2483 0.0197  -0.0119 -0.0350 984  HIS B NE2 
16310 N N   . VAL B 987  ? 0.1914 0.1658 0.1816 0.0210  -0.0043 -0.0302 985  VAL B N   
16311 C CA  . VAL B 987  ? 0.1944 0.1697 0.1888 0.0185  -0.0052 -0.0288 985  VAL B CA  
16312 C C   . VAL B 987  ? 0.2063 0.1843 0.2046 0.0187  -0.0040 -0.0275 985  VAL B C   
16313 O O   . VAL B 987  ? 0.2255 0.2022 0.2268 0.0175  -0.0048 -0.0268 985  VAL B O   
16314 C CB  . VAL B 987  ? 0.2001 0.1784 0.1947 0.0169  -0.0054 -0.0280 985  VAL B CB  
16315 C CG1 . VAL B 987  ? 0.2243 0.2042 0.2234 0.0149  -0.0060 -0.0265 985  VAL B CG1 
16316 C CG2 . VAL B 987  ? 0.2093 0.1844 0.2001 0.0165  -0.0071 -0.0292 985  VAL B CG2 
16317 N N   . THR B 988  ? 0.1960 0.1778 0.1944 0.0202  -0.0019 -0.0271 986  THR B N   
16318 C CA  . THR B 988  ? 0.2020 0.1864 0.2040 0.0203  -0.0009 -0.0258 986  THR B CA  
16319 C C   . THR B 988  ? 0.2212 0.2020 0.2231 0.0217  -0.0012 -0.0262 986  THR B C   
16320 O O   . THR B 988  ? 0.2892 0.2706 0.2942 0.0211  -0.0010 -0.0251 986  THR B O   
16321 C CB  . THR B 988  ? 0.2311 0.2209 0.2335 0.0212  0.0011  -0.0251 986  THR B CB  
16322 O OG1 . THR B 988  ? 0.2503 0.2404 0.2497 0.0238  0.0021  -0.0262 986  THR B OG1 
16323 C CG2 . THR B 988  ? 0.2434 0.2363 0.2459 0.0195  0.0012  -0.0244 986  THR B CG2 
16324 N N   . SER B 989  ? 0.2246 0.2015 0.2230 0.0234  -0.0017 -0.0278 987  SER B N   
16325 C CA  . SER B 989  ? 0.2554 0.2278 0.2533 0.0246  -0.0022 -0.0281 987  SER B CA  
16326 C C   . SER B 989  ? 0.2699 0.2382 0.2693 0.0222  -0.0042 -0.0278 987  SER B C   
16327 O O   . SER B 989  ? 0.3402 0.3057 0.3405 0.0223  -0.0046 -0.0274 987  SER B O   
16328 C CB  . SER B 989  ? 0.2836 0.2524 0.2769 0.0274  -0.0022 -0.0300 987  SER B CB  
16329 O OG  . SER B 989  ? 0.3689 0.3337 0.3589 0.0267  -0.0038 -0.0315 987  SER B OG  
16330 N N   . ARG B 990  ? 0.2225 0.1907 0.2223 0.0200  -0.0055 -0.0279 988  ARG B N   
16331 C CA  . ARG B 990  ? 0.2175 0.1820 0.2185 0.0177  -0.0076 -0.0278 988  ARG B CA  
16332 C C   . ARG B 990  ? 0.2023 0.1703 0.2079 0.0153  -0.0077 -0.0261 988  ARG B C   
16333 O O   . ARG B 990  ? 0.2140 0.1802 0.2218 0.0135  -0.0089 -0.0255 988  ARG B O   
16334 C CB  . ARG B 990  ? 0.2553 0.2163 0.2528 0.0171  -0.0094 -0.0293 988  ARG B CB  
16335 C CG  . ARG B 990  ? 0.3654 0.3229 0.3577 0.0197  -0.0093 -0.0313 988  ARG B CG  
16336 C CD  . ARG B 990  ? 0.3298 0.2810 0.3204 0.0204  -0.0103 -0.0320 988  ARG B CD  
16337 N NE  . ARG B 990  ? 0.2629 0.2089 0.2516 0.0185  -0.0130 -0.0330 988  ARG B NE  
16338 C CZ  . ARG B 990  ? 0.2650 0.2048 0.2522 0.0182  -0.0145 -0.0337 988  ARG B CZ  
16339 N NH1 . ARG B 990  ? 0.3069 0.2446 0.2941 0.0197  -0.0137 -0.0333 988  ARG B NH1 
16340 N NH2 . ARG B 990  ? 0.2871 0.2223 0.2723 0.0163  -0.0171 -0.0347 988  ARG B NH2 
16341 N N   . ILE B 991  ? 0.1934 0.1663 0.2004 0.0151  -0.0066 -0.0254 989  ILE B N   
16342 C CA  . ILE B 991  ? 0.1884 0.1645 0.1995 0.0132  -0.0066 -0.0240 989  ILE B CA  
16343 C C   . ILE B 991  ? 0.2002 0.1775 0.2141 0.0133  -0.0055 -0.0227 989  ILE B C   
16344 O O   . ILE B 991  ? 0.2175 0.1949 0.2304 0.0151  -0.0042 -0.0227 989  ILE B O   
16345 C CB  . ILE B 991  ? 0.1933 0.1734 0.2044 0.0131  -0.0057 -0.0236 989  ILE B CB  
16346 C CG1 . ILE B 991  ? 0.2326 0.2151 0.2473 0.0113  -0.0062 -0.0225 989  ILE B CG1 
16347 C CG2 . ILE B 991  ? 0.2348 0.2181 0.2458 0.0147  -0.0037 -0.0232 989  ILE B CG2 
16348 C CD1 . ILE B 991  ? 0.2680 0.2484 0.2830 0.0098  -0.0083 -0.0229 989  ILE B CD1 
16349 N N   . LYS B 992  ? 0.1899 0.1682 0.2073 0.0116  -0.0059 -0.0216 990  LYS B N   
16350 C CA  . LYS B 992  ? 0.1882 0.1677 0.2081 0.0115  -0.0049 -0.0203 990  LYS B CA  
16351 C C   . LYS B 992  ? 0.1908 0.1749 0.2138 0.0106  -0.0041 -0.0192 990  LYS B C   
16352 O O   . LYS B 992  ? 0.2440 0.2289 0.2698 0.0090  -0.0047 -0.0185 990  LYS B O   
16353 C CB  . LYS B 992  ? 0.2074 0.1835 0.2284 0.0101  -0.0062 -0.0199 990  LYS B CB  
16354 C CG  . LYS B 992  ? 0.2492 0.2199 0.2667 0.0110  -0.0071 -0.0211 990  LYS B CG  
16355 C CD  . LYS B 992  ? 0.3459 0.3129 0.3645 0.0091  -0.0085 -0.0206 990  LYS B CD  
16356 C CE  . LYS B 992  ? 0.4199 0.3887 0.4416 0.0084  -0.0075 -0.0187 990  LYS B CE  
16357 N NZ  . LYS B 992  ? 0.4819 0.4481 0.5053 0.0059  -0.0089 -0.0178 990  LYS B NZ  
16358 N N   . ALA B 993  ? 0.1890 0.1759 0.2113 0.0116  -0.0029 -0.0192 991  ALA B N   
16359 C CA  . ALA B 993  ? 0.1645 0.1552 0.1891 0.0109  -0.0022 -0.0183 991  ALA B CA  
16360 C C   . ALA B 993  ? 0.1665 0.1597 0.1908 0.0121  -0.0006 -0.0178 991  ALA B C   
16361 O O   . ALA B 993  ? 0.1813 0.1742 0.2035 0.0135  0.0000  -0.0183 991  ALA B O   
16362 C CB  . ALA B 993  ? 0.1920 0.1835 0.2158 0.0104  -0.0028 -0.0188 991  ALA B CB  
16363 N N   . GLY B 994  ? 0.1467 0.1424 0.1731 0.0115  0.0002  -0.0169 992  GLY B N   
16364 C CA  . GLY B 994  ? 0.1590 0.1571 0.1852 0.0124  0.0015  -0.0163 992  GLY B CA  
16365 C C   . GLY B 994  ? 0.1371 0.1375 0.1619 0.0127  0.0020  -0.0166 992  GLY B C   
16366 O O   . GLY B 994  ? 0.1432 0.1456 0.1675 0.0135  0.0029  -0.0164 992  GLY B O   
16367 N N   . ASN B 995  ? 0.1458 0.1462 0.1701 0.0118  0.0013  -0.0170 993  ASN B N   
16368 C CA  . ASN B 995  ? 0.1393 0.1417 0.1622 0.0116  0.0017  -0.0171 993  ASN B CA  
16369 C C   . ASN B 995  ? 0.1396 0.1405 0.1604 0.0115  0.0009  -0.0178 993  ASN B C   
16370 O O   . ASN B 995  ? 0.1567 0.1559 0.1777 0.0107  -0.0003 -0.0180 993  ASN B O   
16371 C CB  . ASN B 995  ? 0.1421 0.1458 0.1661 0.0105  0.0016  -0.0165 993  ASN B CB  
16372 C CG  . ASN B 995  ? 0.1402 0.1459 0.1653 0.0107  0.0026  -0.0158 993  ASN B CG  
16373 O OD1 . ASN B 995  ? 0.1477 0.1531 0.1743 0.0109  0.0028  -0.0154 993  ASN B OD1 
16374 N ND2 . ASN B 995  ? 0.1570 0.1649 0.1810 0.0106  0.0032  -0.0156 993  ASN B ND2 
16375 N N   . LEU B 996  ? 0.1463 0.1479 0.1649 0.0123  0.0015  -0.0183 994  LEU B N   
16376 C CA  . LEU B 996  ? 0.1527 0.1530 0.1687 0.0124  0.0009  -0.0190 994  LEU B CA  
16377 C C   . LEU B 996  ? 0.1497 0.1526 0.1644 0.0117  0.0015  -0.0186 994  LEU B C   
16378 O O   . LEU B 996  ? 0.1529 0.1588 0.1682 0.0117  0.0025  -0.0180 994  LEU B O   
16379 C CB  . LEU B 996  ? 0.1618 0.1613 0.1762 0.0141  0.0013  -0.0199 994  LEU B CB  
16380 C CG  . LEU B 996  ? 0.1801 0.1768 0.1955 0.0149  0.0009  -0.0201 994  LEU B CG  
16381 C CD1 . LEU B 996  ? 0.2033 0.1984 0.2163 0.0169  0.0012  -0.0211 994  LEU B CD1 
16382 C CD2 . LEU B 996  ? 0.1884 0.1821 0.2047 0.0136  -0.0006 -0.0203 994  LEU B CD2 
16383 N N   . TYR B 997  ? 0.1445 0.1462 0.1572 0.0110  0.0007  -0.0189 995  TYR B N   
16384 C CA  . TYR B 997  ? 0.1624 0.1659 0.1735 0.0100  0.0011  -0.0183 995  TYR B CA  
16385 C C   . TYR B 997  ? 0.1467 0.1492 0.1545 0.0103  0.0008  -0.0190 995  TYR B C   
16386 O O   . TYR B 997  ? 0.1730 0.1724 0.1799 0.0102  -0.0005 -0.0196 995  TYR B O   
16387 C CB  . TYR B 997  ? 0.1601 0.1627 0.1719 0.0084  0.0001  -0.0177 995  TYR B CB  
16388 C CG  . TYR B 997  ? 0.1636 0.1667 0.1783 0.0083  0.0003  -0.0172 995  TYR B CG  
16389 C CD1 . TYR B 997  ? 0.1577 0.1592 0.1745 0.0087  -0.0004 -0.0175 995  TYR B CD1 
16390 C CD2 . TYR B 997  ? 0.1762 0.1817 0.1915 0.0077  0.0011  -0.0165 995  TYR B CD2 
16391 C CE1 . TYR B 997  ? 0.1835 0.1858 0.2027 0.0087  0.0000  -0.0171 995  TYR B CE1 
16392 C CE2 . TYR B 997  ? 0.1580 0.1638 0.1755 0.0077  0.0012  -0.0162 995  TYR B CE2 
16393 C CZ  . TYR B 997  ? 0.1747 0.1790 0.1941 0.0083  0.0007  -0.0165 995  TYR B CZ  
16394 O OH  . TYR B 997  ? 0.1911 0.1959 0.2125 0.0083  0.0011  -0.0161 995  TYR B OH  
16395 N N   . ILE B 998  ? 0.1532 0.1585 0.1592 0.0105  0.0020  -0.0188 996  ILE B N   
16396 C CA  . ILE B 998  ? 0.1583 0.1631 0.1609 0.0110  0.0021  -0.0194 996  ILE B CA  
16397 C C   . ILE B 998  ? 0.1781 0.1844 0.1789 0.0092  0.0023  -0.0184 996  ILE B C   
16398 O O   . ILE B 998  ? 0.1722 0.1822 0.1737 0.0085  0.0035  -0.0175 996  ILE B O   
16399 C CB  . ILE B 998  ? 0.1737 0.1807 0.1754 0.0130  0.0036  -0.0201 996  ILE B CB  
16400 C CG1 . ILE B 998  ? 0.2275 0.2325 0.2309 0.0147  0.0034  -0.0209 996  ILE B CG1 
16401 C CG2 . ILE B 998  ? 0.2043 0.2107 0.2020 0.0137  0.0038  -0.0209 996  ILE B CG2 
16402 C CD1 . ILE B 998  ? 0.2745 0.2748 0.2772 0.0148  0.0018  -0.0219 996  ILE B CD1 
16403 N N   . ASN B 999  ? 0.1668 0.1704 0.1653 0.0084  0.0010  -0.0185 997  ASN B N   
16404 C CA  . ASN B 999  ? 0.1768 0.1810 0.1727 0.0067  0.0010  -0.0174 997  ASN B CA  
16405 C C   . ASN B 999  ? 0.1757 0.1806 0.1733 0.0049  0.0008  -0.0161 997  ASN B C   
16406 O O   . ASN B 999  ? 0.1822 0.1891 0.1785 0.0034  0.0014  -0.0150 997  ASN B O   
16407 C CB  . ASN B 999  ? 0.1607 0.1684 0.1542 0.0072  0.0027  -0.0174 997  ASN B CB  
16408 C CG  . ASN B 999  ? 0.1859 0.1919 0.1765 0.0089  0.0027  -0.0188 997  ASN B CG  
16409 O OD1 . ASN B 999  ? 0.1923 0.1943 0.1815 0.0089  0.0010  -0.0194 997  ASN B OD1 
16410 N ND2 . ASN B 999  ? 0.1979 0.2070 0.1875 0.0105  0.0044  -0.0193 997  ASN B ND2 
16411 N N   . ARG B 1000 ? 0.1747 0.1777 0.1750 0.0049  -0.0002 -0.0162 998  ARG B N   
16412 C CA  . ARG B 1000 ? 0.1518 0.1546 0.1535 0.0035  -0.0006 -0.0153 998  ARG B CA  
16413 C C   . ARG B 1000 ? 0.1721 0.1719 0.1757 0.0040  -0.0020 -0.0157 998  ARG B C   
16414 O O   . ARG B 1000 ? 0.1929 0.1911 0.1971 0.0051  -0.0027 -0.0166 998  ARG B O   
16415 C CB  . ARG B 1000 ? 0.1636 0.1699 0.1674 0.0034  0.0008  -0.0149 998  ARG B CB  
16416 C CG  . ARG B 1000 ? 0.1620 0.1694 0.1682 0.0053  0.0015  -0.0157 998  ARG B CG  
16417 C CD  . ARG B 1000 ? 0.1637 0.1734 0.1725 0.0051  0.0022  -0.0153 998  ARG B CD  
16418 N NE  . ARG B 1000 ? 0.1525 0.1599 0.1624 0.0042  0.0011  -0.0150 998  ARG B NE  
16419 C CZ  . ARG B 1000 ? 0.1624 0.1711 0.1739 0.0038  0.0014  -0.0146 998  ARG B CZ  
16420 N NH1 . ARG B 1000 ? 0.1712 0.1834 0.1836 0.0039  0.0026  -0.0143 998  ARG B NH1 
16421 N NH2 . ARG B 1000 ? 0.1845 0.1907 0.1965 0.0032  0.0005  -0.0145 998  ARG B NH2 
16422 N N   . ASN B 1001 ? 0.1584 0.1574 0.1632 0.0031  -0.0025 -0.0150 999  ASN B N   
16423 C CA  . ASN B 1001 ? 0.1616 0.1586 0.1687 0.0037  -0.0036 -0.0154 999  ASN B CA  
16424 C C   . ASN B 1001 ? 0.1684 0.1669 0.1786 0.0049  -0.0028 -0.0160 999  ASN B C   
16425 O O   . ASN B 1001 ? 0.1680 0.1690 0.1786 0.0053  -0.0014 -0.0160 999  ASN B O   
16426 C CB  . ASN B 1001 ? 0.1813 0.1767 0.1882 0.0028  -0.0043 -0.0147 999  ASN B CB  
16427 C CG  . ASN B 1001 ? 0.1968 0.1942 0.2048 0.0022  -0.0032 -0.0143 999  ASN B CG  
16428 O OD1 . ASN B 1001 ? 0.1914 0.1908 0.2018 0.0031  -0.0023 -0.0147 999  ASN B OD1 
16429 N ND2 . ASN B 1001 ? 0.3167 0.3134 0.3229 0.0007  -0.0035 -0.0135 999  ASN B ND2 
16430 N N   . ILE B 1002 ? 0.1561 0.1533 0.1685 0.0056  -0.0036 -0.0163 1000 ILE B N   
16431 C CA  . ILE B 1002 ? 0.1617 0.1600 0.1770 0.0065  -0.0029 -0.0167 1000 ILE B CA  
16432 C C   . ILE B 1002 ? 0.1808 0.1798 0.1983 0.0066  -0.0026 -0.0164 1000 ILE B C   
16433 O O   . ILE B 1002 ? 0.1865 0.1860 0.2065 0.0072  -0.0024 -0.0166 1000 ILE B O   
16434 C CB  . ILE B 1002 ? 0.1593 0.1561 0.1755 0.0072  -0.0039 -0.0174 1000 ILE B CB  
16435 C CG1 . ILE B 1002 ? 0.1593 0.1548 0.1769 0.0070  -0.0054 -0.0173 1000 ILE B CG1 
16436 C CG2 . ILE B 1002 ? 0.1702 0.1660 0.1835 0.0072  -0.0043 -0.0179 1000 ILE B CG2 
16437 C CD1 . ILE B 1002 ? 0.1658 0.1605 0.1853 0.0074  -0.0063 -0.0178 1000 ILE B CD1 
16438 N N   . ILE B 1003 ? 0.1850 0.1840 0.2015 0.0058  -0.0025 -0.0159 1001 ILE B N   
16439 C CA  . ILE B 1003 ? 0.1960 0.1952 0.2142 0.0060  -0.0023 -0.0157 1001 ILE B CA  
16440 C C   . ILE B 1003 ? 0.2522 0.2535 0.2702 0.0055  -0.0011 -0.0154 1001 ILE B C   
16441 O O   . ILE B 1003 ? 0.2593 0.2606 0.2780 0.0055  -0.0009 -0.0153 1001 ILE B O   
16442 C CB  . ILE B 1003 ? 0.2082 0.2050 0.2254 0.0057  -0.0034 -0.0156 1001 ILE B CB  
16443 C CG1 . ILE B 1003 ? 0.3008 0.2964 0.3148 0.0044  -0.0039 -0.0151 1001 ILE B CG1 
16444 C CG2 . ILE B 1003 ? 0.2084 0.2039 0.2268 0.0065  -0.0047 -0.0159 1001 ILE B CG2 
16445 C CD1 . ILE B 1003 ? 0.3738 0.3666 0.3864 0.0041  -0.0050 -0.0149 1001 ILE B CD1 
16446 N N   . GLY B 1004 ? 0.2132 0.2165 0.2305 0.0054  -0.0003 -0.0153 1002 GLY B N   
16447 C CA  . GLY B 1004 ? 0.2194 0.2252 0.2368 0.0050  0.0007  -0.0150 1002 GLY B CA  
16448 C C   . GLY B 1004 ? 0.2173 0.2244 0.2369 0.0060  0.0014  -0.0150 1002 GLY B C   
16449 O O   . GLY B 1004 ? 0.2334 0.2406 0.2542 0.0071  0.0017  -0.0153 1002 GLY B O   
16450 N N   . ALA B 1005 ? 0.2025 0.2101 0.2223 0.0056  0.0016  -0.0148 1003 ALA B N   
16451 C CA  . ALA B 1005 ? 0.2329 0.2418 0.2544 0.0064  0.0023  -0.0147 1003 ALA B CA  
16452 C C   . ALA B 1005 ? 0.2313 0.2423 0.2521 0.0056  0.0027  -0.0143 1003 ALA B C   
16453 O O   . ALA B 1005 ? 0.2113 0.2226 0.2325 0.0058  0.0029  -0.0143 1003 ALA B O   
16454 C CB  . ALA B 1005 ? 0.2026 0.2099 0.2253 0.0070  0.0021  -0.0150 1003 ALA B CB  
16455 N N   . VAL B 1006 ? 0.1638 0.1766 0.1834 0.0047  0.0028  -0.0140 1004 VAL B N   
16456 C CA  . VAL B 1006 ? 0.1899 0.2050 0.2090 0.0036  0.0029  -0.0136 1004 VAL B CA  
16457 C C   . VAL B 1006 ? 0.1639 0.1815 0.1846 0.0048  0.0036  -0.0134 1004 VAL B C   
16458 O O   . VAL B 1006 ? 0.1591 0.1784 0.1808 0.0060  0.0043  -0.0134 1004 VAL B O   
16459 C CB  . VAL B 1006 ? 0.1759 0.1933 0.1939 0.0023  0.0030  -0.0131 1004 VAL B CB  
16460 C CG1 . VAL B 1006 ? 0.1894 0.2099 0.2073 0.0010  0.0030  -0.0125 1004 VAL B CG1 
16461 C CG2 . VAL B 1006 ? 0.1993 0.2136 0.2153 0.0009  0.0021  -0.0131 1004 VAL B CG2 
16462 N N   . VAL B 1007 ? 0.1758 0.1933 0.1963 0.0044  0.0035  -0.0134 1005 VAL B N   
16463 C CA  . VAL B 1007 ? 0.1619 0.1813 0.1836 0.0056  0.0040  -0.0131 1005 VAL B CA  
16464 C C   . VAL B 1007 ? 0.1661 0.1896 0.1884 0.0058  0.0045  -0.0126 1005 VAL B C   
16465 O O   . VAL B 1007 ? 0.1560 0.1817 0.1776 0.0044  0.0042  -0.0123 1005 VAL B O   
16466 C CB  . VAL B 1007 ? 0.1644 0.1831 0.1851 0.0049  0.0037  -0.0132 1005 VAL B CB  
16467 C CG1 . VAL B 1007 ? 0.1739 0.1948 0.1954 0.0059  0.0042  -0.0128 1005 VAL B CG1 
16468 C CG2 . VAL B 1007 ? 0.1903 0.2055 0.2106 0.0052  0.0034  -0.0138 1005 VAL B CG2 
16469 N N   . GLY B 1008 ? 0.1533 0.1777 0.1769 0.0076  0.0051  -0.0124 1006 GLY B N   
16470 C CA  . GLY B 1008 ? 0.1654 0.1936 0.1897 0.0085  0.0055  -0.0120 1006 GLY B CA  
16471 C C   . GLY B 1008 ? 0.1750 0.2047 0.1991 0.0085  0.0058  -0.0121 1006 GLY B C   
16472 O O   . GLY B 1008 ? 0.1926 0.2260 0.2174 0.0094  0.0063  -0.0118 1006 GLY B O   
16473 N N   . VAL B 1009 ? 0.1548 0.1818 0.1780 0.0077  0.0055  -0.0126 1007 VAL B N   
16474 C CA  . VAL B 1009 ? 0.1706 0.1986 0.1931 0.0077  0.0058  -0.0127 1007 VAL B CA  
16475 C C   . VAL B 1009 ? 0.1672 0.1916 0.1894 0.0089  0.0058  -0.0134 1007 VAL B C   
16476 O O   . VAL B 1009 ? 0.1654 0.1904 0.1874 0.0104  0.0063  -0.0138 1007 VAL B O   
16477 C CB  . VAL B 1009 ? 0.1707 0.1990 0.1918 0.0052  0.0054  -0.0124 1007 VAL B CB  
16478 C CG1 . VAL B 1009 ? 0.1762 0.2057 0.1963 0.0052  0.0058  -0.0125 1007 VAL B CG1 
16479 C CG2 . VAL B 1009 ? 0.1685 0.2002 0.1899 0.0037  0.0052  -0.0117 1007 VAL B CG2 
16480 N N   . GLN B 1010 ? 0.1618 0.1824 0.1837 0.0083  0.0051  -0.0137 1008 GLN B N   
16481 C CA  . GLN B 1010 ? 0.1588 0.1762 0.1811 0.0094  0.0049  -0.0143 1008 GLN B CA  
16482 C C   . GLN B 1010 ? 0.1589 0.1751 0.1826 0.0098  0.0049  -0.0141 1008 GLN B C   
16483 O O   . GLN B 1010 ? 0.1728 0.1870 0.1967 0.0091  0.0044  -0.0142 1008 GLN B O   
16484 C CB  . GLN B 1010 ? 0.1806 0.1953 0.2018 0.0085  0.0042  -0.0147 1008 GLN B CB  
16485 C CG  . GLN B 1010 ? 0.1824 0.1982 0.2019 0.0079  0.0042  -0.0147 1008 GLN B CG  
16486 C CD  . GLN B 1010 ? 0.1849 0.2013 0.2032 0.0059  0.0039  -0.0142 1008 GLN B CD  
16487 O OE1 . GLN B 1010 ? 0.1838 0.1981 0.2020 0.0050  0.0032  -0.0141 1008 GLN B OE1 
16488 N NE2 . GLN B 1010 ? 0.1803 0.1995 0.1976 0.0052  0.0044  -0.0138 1008 GLN B NE2 
16489 N N   . PRO B 1011 ? 0.1542 0.1717 0.1788 0.0110  0.0054  -0.0138 1009 PRO B N   
16490 C CA  . PRO B 1011 ? 0.1753 0.1914 0.2009 0.0115  0.0055  -0.0135 1009 PRO B CA  
16491 C C   . PRO B 1011 ? 0.1445 0.1574 0.1706 0.0114  0.0050  -0.0139 1009 PRO B C   
16492 O O   . PRO B 1011 ? 0.1368 0.1484 0.1626 0.0118  0.0048  -0.0144 1009 PRO B O   
16493 C CB  . PRO B 1011 ? 0.1489 0.1661 0.1750 0.0130  0.0060  -0.0131 1009 PRO B CB  
16494 C CG  . PRO B 1011 ? 0.1629 0.1834 0.1884 0.0132  0.0063  -0.0130 1009 PRO B CG  
16495 C CD  . PRO B 1011 ? 0.1665 0.1868 0.1911 0.0122  0.0060  -0.0136 1009 PRO B CD  
16496 N N   . PHE B 1012 ? 0.1318 0.1438 0.1588 0.0108  0.0049  -0.0138 1010 PHE B N   
16497 C CA  . PHE B 1012 ? 0.1382 0.1480 0.1657 0.0104  0.0043  -0.0142 1010 PHE B CA  
16498 C C   . PHE B 1012 ? 0.1451 0.1539 0.1743 0.0108  0.0044  -0.0138 1010 PHE B C   
16499 O O   . PHE B 1012 ? 0.1587 0.1684 0.1886 0.0109  0.0050  -0.0133 1010 PHE B O   
16500 C CB  . PHE B 1012 ? 0.1492 0.1586 0.1763 0.0096  0.0038  -0.0144 1010 PHE B CB  
16501 C CG  . PHE B 1012 ? 0.1380 0.1456 0.1657 0.0094  0.0030  -0.0148 1010 PHE B CG  
16502 C CD1 . PHE B 1012 ? 0.1692 0.1757 0.1958 0.0090  0.0023  -0.0152 1010 PHE B CD1 
16503 C CD2 . PHE B 1012 ? 0.1568 0.1640 0.1863 0.0095  0.0030  -0.0147 1010 PHE B CD2 
16504 C CE1 . PHE B 1012 ? 0.1575 0.1623 0.1846 0.0089  0.0013  -0.0155 1010 PHE B CE1 
16505 C CE2 . PHE B 1012 ? 0.1683 0.1743 0.1988 0.0094  0.0022  -0.0150 1010 PHE B CE2 
16506 C CZ  . PHE B 1012 ? 0.1657 0.1704 0.1949 0.0091  0.0012  -0.0154 1010 PHE B CZ  
16507 N N   . GLY B 1013 ? 0.1388 0.1459 0.1687 0.0108  0.0039  -0.0141 1011 GLY B N   
16508 C CA  . GLY B 1013 ? 0.1482 0.1544 0.1799 0.0107  0.0039  -0.0136 1011 GLY B CA  
16509 C C   . GLY B 1013 ? 0.1351 0.1390 0.1667 0.0108  0.0032  -0.0139 1011 GLY B C   
16510 O O   . GLY B 1013 ? 0.1546 0.1578 0.1846 0.0115  0.0032  -0.0143 1011 GLY B O   
16511 N N   . GLY B 1014 ? 0.1540 0.1570 0.1874 0.0101  0.0027  -0.0137 1012 GLY B N   
16512 C CA  . GLY B 1014 ? 0.1842 0.1846 0.2174 0.0099  0.0018  -0.0141 1012 GLY B CA  
16513 C C   . GLY B 1014 ? 0.1797 0.1788 0.2141 0.0095  0.0019  -0.0132 1012 GLY B C   
16514 O O   . GLY B 1014 ? 0.2025 0.2027 0.2375 0.0096  0.0029  -0.0123 1012 GLY B O   
16515 N N   . ARG B 1015 ? 0.1722 0.1688 0.2067 0.0088  0.0007  -0.0136 1013 ARG B N   
16516 C CA  . ARG B 1015 ? 0.1845 0.1788 0.2196 0.0082  0.0004  -0.0128 1013 ARG B CA  
16517 C C   . ARG B 1015 ? 0.1821 0.1762 0.2194 0.0064  -0.0007 -0.0127 1013 ARG B C   
16518 O O   . ARG B 1015 ? 0.1682 0.1640 0.2066 0.0061  -0.0012 -0.0132 1013 ARG B O   
16519 C CB  . ARG B 1015 ? 0.1788 0.1693 0.2110 0.0091  -0.0001 -0.0136 1013 ARG B CB  
16520 C CG  . ARG B 1015 ? 0.1924 0.1812 0.2230 0.0092  -0.0014 -0.0150 1013 ARG B CG  
16521 C CD  . ARG B 1015 ? 0.2587 0.2428 0.2871 0.0094  -0.0025 -0.0157 1013 ARG B CD  
16522 N NE  . ARG B 1015 ? 0.2925 0.2747 0.3227 0.0074  -0.0037 -0.0152 1013 ARG B NE  
16523 C CZ  . ARG B 1015 ? 0.2797 0.2620 0.3110 0.0059  -0.0051 -0.0156 1013 ARG B CZ  
16524 N NH1 . ARG B 1015 ? 0.2727 0.2563 0.3032 0.0064  -0.0054 -0.0166 1013 ARG B NH1 
16525 N NH2 . ARG B 1015 ? 0.2925 0.2737 0.3258 0.0039  -0.0061 -0.0149 1013 ARG B NH2 
16526 N N   . GLY B 1016 ? 0.1852 0.1772 0.2233 0.0053  -0.0011 -0.0119 1014 GLY B N   
16527 C CA  . GLY B 1016 ? 0.1759 0.1682 0.2166 0.0034  -0.0023 -0.0116 1014 GLY B CA  
16528 C C   . GLY B 1016 ? 0.1811 0.1781 0.2251 0.0029  -0.0014 -0.0108 1014 GLY B C   
16529 O O   . GLY B 1016 ? 0.1903 0.1895 0.2349 0.0033  0.0001  -0.0098 1014 GLY B O   
16530 N N   . LEU B 1017 ? 0.1676 0.1664 0.2136 0.0021  -0.0025 -0.0112 1015 LEU B N   
16531 C CA  . LEU B 1017 ? 0.1839 0.1871 0.2329 0.0021  -0.0017 -0.0106 1015 LEU B CA  
16532 C C   . LEU B 1017 ? 0.1677 0.1727 0.2155 0.0039  -0.0006 -0.0111 1015 LEU B C   
16533 O O   . LEU B 1017 ? 0.1686 0.1770 0.2185 0.0042  0.0002  -0.0108 1015 LEU B O   
16534 C CB  . LEU B 1017 ? 0.1764 0.1810 0.2278 0.0011  -0.0034 -0.0110 1015 LEU B CB  
16535 C CG  . LEU B 1017 ? 0.1940 0.1973 0.2471 -0.0011 -0.0048 -0.0104 1015 LEU B CG  
16536 C CD1 . LEU B 1017 ? 0.2163 0.2211 0.2714 -0.0019 -0.0067 -0.0109 1015 LEU B CD1 
16537 C CD2 . LEU B 1017 ? 0.2255 0.2316 0.2816 -0.0023 -0.0035 -0.0086 1015 LEU B CD2 
16538 N N   . SER B 1018 ? 0.1424 0.1452 0.1869 0.0050  -0.0005 -0.0119 1016 SER B N   
16539 C CA  . SER B 1018 ? 0.1424 0.1465 0.1855 0.0063  0.0004  -0.0124 1016 SER B CA  
16540 C C   . SER B 1018 ? 0.1490 0.1541 0.1912 0.0071  0.0020  -0.0118 1016 SER B C   
16541 O O   . SER B 1018 ? 0.1536 0.1601 0.1950 0.0079  0.0027  -0.0121 1016 SER B O   
16542 C CB  . SER B 1018 ? 0.1503 0.1523 0.1904 0.0070  -0.0004 -0.0136 1016 SER B CB  
16543 O OG  . SER B 1018 ? 0.1537 0.1549 0.1942 0.0064  -0.0020 -0.0142 1016 SER B OG  
16544 N N   . GLY B 1019 ? 0.1493 0.1535 0.1916 0.0067  0.0025  -0.0109 1017 GLY B N   
16545 C CA  . GLY B 1019 ? 0.1661 0.1712 0.2073 0.0076  0.0039  -0.0103 1017 GLY B CA  
16546 C C   . GLY B 1019 ? 0.1558 0.1594 0.1966 0.0073  0.0043  -0.0092 1017 GLY B C   
16547 O O   . GLY B 1019 ? 0.1739 0.1745 0.2142 0.0068  0.0034  -0.0093 1017 GLY B O   
16548 N N   . THR B 1020 ? 0.1696 0.1747 0.2103 0.0077  0.0056  -0.0083 1018 THR B N   
16549 C CA  . THR B 1020 ? 0.1601 0.1636 0.1996 0.0078  0.0061  -0.0072 1018 THR B CA  
16550 C C   . THR B 1020 ? 0.1595 0.1622 0.1964 0.0094  0.0061  -0.0077 1018 THR B C   
16551 O O   . THR B 1020 ? 0.1764 0.1768 0.2119 0.0099  0.0060  -0.0072 1018 THR B O   
16552 C CB  . THR B 1020 ? 0.1555 0.1615 0.1959 0.0076  0.0075  -0.0058 1018 THR B CB  
16553 O OG1 . THR B 1020 ? 0.1593 0.1679 0.1990 0.0085  0.0083  -0.0064 1018 THR B OG1 
16554 C CG2 . THR B 1020 ? 0.1625 0.1699 0.2058 0.0060  0.0077  -0.0050 1018 THR B CG2 
16555 N N   . GLY B 1021 ? 0.1692 0.1737 0.2053 0.0102  0.0063  -0.0087 1019 GLY B N   
16556 C CA  . GLY B 1021 ? 0.1585 0.1635 0.1926 0.0114  0.0066  -0.0089 1019 GLY B CA  
16557 C C   . GLY B 1021 ? 0.1625 0.1691 0.1963 0.0117  0.0076  -0.0077 1019 GLY B C   
16558 O O   . GLY B 1021 ? 0.1550 0.1622 0.1900 0.0109  0.0082  -0.0068 1019 GLY B O   
16559 N N   . PRO B 1022 ? 0.1488 0.1564 0.1810 0.0128  0.0079  -0.0077 1020 PRO B N   
16560 C CA  . PRO B 1022 ? 0.1548 0.1628 0.1858 0.0136  0.0074  -0.0087 1020 PRO B CA  
16561 C C   . PRO B 1022 ? 0.1669 0.1764 0.1980 0.0131  0.0072  -0.0097 1020 PRO B C   
16562 O O   . PRO B 1022 ? 0.1818 0.1922 0.2136 0.0124  0.0075  -0.0098 1020 PRO B O   
16563 C CB  . PRO B 1022 ? 0.1964 0.2059 0.2261 0.0147  0.0078  -0.0080 1020 PRO B CB  
16564 C CG  . PRO B 1022 ? 0.1821 0.1929 0.2121 0.0141  0.0085  -0.0072 1020 PRO B CG  
16565 C CD  . PRO B 1022 ? 0.1545 0.1636 0.1859 0.0131  0.0087  -0.0066 1020 PRO B CD  
16566 N N   . LYS B 1023 ? 0.1505 0.1603 0.1808 0.0134  0.0067  -0.0106 1021 LYS B N   
16567 C CA  . LYS B 1023 ? 0.1546 0.1654 0.1847 0.0127  0.0064  -0.0115 1021 LYS B CA  
16568 C C   . LYS B 1023 ? 0.1520 0.1649 0.1814 0.0125  0.0068  -0.0114 1021 LYS B C   
16569 O O   . LYS B 1023 ? 0.1549 0.1695 0.1836 0.0130  0.0070  -0.0110 1021 LYS B O   
16570 C CB  . LYS B 1023 ? 0.1424 0.1533 0.1714 0.0132  0.0060  -0.0122 1021 LYS B CB  
16571 C CG  . LYS B 1023 ? 0.1393 0.1477 0.1683 0.0134  0.0055  -0.0127 1021 LYS B CG  
16572 C CD  . LYS B 1023 ? 0.1292 0.1384 0.1567 0.0140  0.0054  -0.0134 1021 LYS B CD  
16573 C CE  . LYS B 1023 ? 0.1598 0.1666 0.1867 0.0142  0.0047  -0.0142 1021 LYS B CE  
16574 N NZ  . LYS B 1023 ? 0.1498 0.1562 0.1767 0.0130  0.0041  -0.0147 1021 LYS B NZ  
16575 N N   . ALA B 1024 ? 0.1569 0.1698 0.1866 0.0117  0.0067  -0.0118 1022 ALA B N   
16576 C CA  . ALA B 1024 ? 0.1481 0.1622 0.1765 0.0113  0.0067  -0.0120 1022 ALA B CA  
16577 C C   . ALA B 1024 ? 0.1619 0.1770 0.1891 0.0109  0.0062  -0.0124 1022 ALA B C   
16578 O O   . ALA B 1024 ? 0.1590 0.1735 0.1863 0.0109  0.0058  -0.0128 1022 ALA B O   
16579 C CB  . ALA B 1024 ? 0.1730 0.1862 0.2017 0.0108  0.0065  -0.0126 1022 ALA B CB  
16580 N N   . GLY B 1025 ? 0.1379 0.1547 0.1640 0.0106  0.0062  -0.0123 1023 GLY B N   
16581 C CA  . GLY B 1025 ? 0.1622 0.1806 0.1874 0.0100  0.0058  -0.0124 1023 GLY B CA  
16582 C C   . GLY B 1025 ? 0.1471 0.1672 0.1729 0.0110  0.0060  -0.0121 1023 GLY B C   
16583 O O   . GLY B 1025 ? 0.1511 0.1727 0.1765 0.0107  0.0059  -0.0122 1023 GLY B O   
16584 N N   . GLY B 1026 ? 0.1538 0.1735 0.1803 0.0122  0.0064  -0.0116 1024 GLY B N   
16585 C CA  . GLY B 1026 ? 0.1499 0.1707 0.1767 0.0136  0.0066  -0.0113 1024 GLY B CA  
16586 C C   . GLY B 1026 ? 0.1572 0.1793 0.1840 0.0146  0.0069  -0.0104 1024 GLY B C   
16587 O O   . GLY B 1026 ? 0.1487 0.1707 0.1752 0.0141  0.0070  -0.0100 1024 GLY B O   
16588 N N   . PRO B 1027 ? 0.1558 0.1791 0.1827 0.0161  0.0070  -0.0101 1025 PRO B N   
16589 C CA  . PRO B 1027 ? 0.1447 0.1700 0.1715 0.0171  0.0070  -0.0092 1025 PRO B CA  
16590 C C   . PRO B 1027 ? 0.1424 0.1650 0.1691 0.0180  0.0072  -0.0084 1025 PRO B C   
16591 O O   . PRO B 1027 ? 0.1442 0.1681 0.1705 0.0187  0.0071  -0.0075 1025 PRO B O   
16592 C CB  . PRO B 1027 ? 0.1565 0.1842 0.1835 0.0188  0.0070  -0.0092 1025 PRO B CB  
16593 C CG  . PRO B 1027 ? 0.1823 0.2075 0.2093 0.0191  0.0071  -0.0100 1025 PRO B CG  
16594 C CD  . PRO B 1027 ? 0.1603 0.1840 0.1872 0.0170  0.0070  -0.0106 1025 PRO B CD  
16595 N N   . LEU B 1028 ? 0.1487 0.1678 0.1757 0.0178  0.0073  -0.0085 1026 LEU B N   
16596 C CA  . LEU B 1028 ? 0.1485 0.1651 0.1754 0.0181  0.0075  -0.0076 1026 LEU B CA  
16597 C C   . LEU B 1028 ? 0.1610 0.1775 0.1880 0.0168  0.0079  -0.0073 1026 LEU B C   
16598 O O   . LEU B 1028 ? 0.1771 0.1922 0.2040 0.0169  0.0083  -0.0062 1026 LEU B O   
16599 C CB  . LEU B 1028 ? 0.1568 0.1697 0.1840 0.0184  0.0074  -0.0078 1026 LEU B CB  
16600 C CG  . LEU B 1028 ? 0.2046 0.2169 0.2312 0.0201  0.0071  -0.0083 1026 LEU B CG  
16601 C CD1 . LEU B 1028 ? 0.2202 0.2281 0.2467 0.0202  0.0067  -0.0086 1026 LEU B CD1 
16602 C CD2 . LEU B 1028 ? 0.2675 0.2810 0.2935 0.0219  0.0070  -0.0074 1026 LEU B CD2 
16603 N N   . TYR B 1029 ? 0.1379 0.1556 0.1649 0.0156  0.0079  -0.0080 1027 TYR B N   
16604 C CA  . TYR B 1029 ? 0.1408 0.1580 0.1680 0.0146  0.0083  -0.0081 1027 TYR B CA  
16605 C C   . TYR B 1029 ? 0.1378 0.1561 0.1640 0.0147  0.0087  -0.0071 1027 TYR B C   
16606 O O   . TYR B 1029 ? 0.1414 0.1587 0.1678 0.0146  0.0094  -0.0064 1027 TYR B O   
16607 C CB  . TYR B 1029 ? 0.1426 0.1605 0.1696 0.0136  0.0080  -0.0092 1027 TYR B CB  
16608 C CG  . TYR B 1029 ? 0.1492 0.1661 0.1766 0.0128  0.0083  -0.0096 1027 TYR B CG  
16609 C CD1 . TYR B 1029 ? 0.1359 0.1512 0.1648 0.0126  0.0083  -0.0097 1027 TYR B CD1 
16610 C CD2 . TYR B 1029 ? 0.1538 0.1715 0.1800 0.0123  0.0083  -0.0100 1027 TYR B CD2 
16611 C CE1 . TYR B 1029 ? 0.1519 0.1668 0.1814 0.0121  0.0085  -0.0101 1027 TYR B CE1 
16612 C CE2 . TYR B 1029 ? 0.1403 0.1571 0.1668 0.0120  0.0086  -0.0105 1027 TYR B CE2 
16613 C CZ  . TYR B 1029 ? 0.1289 0.1446 0.1573 0.0120  0.0087  -0.0106 1027 TYR B CZ  
16614 O OH  . TYR B 1029 ? 0.1599 0.1752 0.1887 0.0119  0.0089  -0.0111 1027 TYR B OH  
16615 N N   . LEU B 1030 ? 0.1384 0.1589 0.1634 0.0150  0.0084  -0.0071 1028 LEU B N   
16616 C CA  . LEU B 1030 ? 0.1386 0.1601 0.1622 0.0150  0.0086  -0.0064 1028 LEU B CA  
16617 C C   . LEU B 1030 ? 0.1561 0.1766 0.1794 0.0160  0.0090  -0.0049 1028 LEU B C   
16618 O O   . LEU B 1030 ? 0.1554 0.1758 0.1778 0.0159  0.0096  -0.0042 1028 LEU B O   
16619 C CB  . LEU B 1030 ? 0.1529 0.1771 0.1753 0.0150  0.0079  -0.0066 1028 LEU B CB  
16620 C CG  . LEU B 1030 ? 0.1728 0.1978 0.1948 0.0137  0.0074  -0.0078 1028 LEU B CG  
16621 C CD1 . LEU B 1030 ? 0.2062 0.2342 0.2271 0.0134  0.0065  -0.0077 1028 LEU B CD1 
16622 C CD2 . LEU B 1030 ? 0.1952 0.2186 0.2163 0.0130  0.0078  -0.0084 1028 LEU B CD2 
16623 N N   . GLY B 1031 ? 0.1653 0.1848 0.1893 0.0170  0.0087  -0.0045 1029 GLY B N   
16624 C CA  . GLY B 1031 ? 0.1606 0.1785 0.1841 0.0179  0.0089  -0.0030 1029 GLY B CA  
16625 C C   . GLY B 1031 ? 0.1629 0.1783 0.1869 0.0170  0.0096  -0.0023 1029 GLY B C   
16626 O O   . GLY B 1031 ? 0.1834 0.1975 0.2065 0.0174  0.0099  -0.0008 1029 GLY B O   
16627 N N   . ARG B 1032 ? 0.1464 0.1614 0.1717 0.0159  0.0099  -0.0032 1030 ARG B N   
16628 C CA  . ARG B 1032 ? 0.1362 0.1499 0.1624 0.0150  0.0107  -0.0025 1030 ARG B CA  
16629 C C   . ARG B 1032 ? 0.1640 0.1794 0.1893 0.0145  0.0116  -0.0021 1030 ARG B C   
16630 O O   . ARG B 1032 ? 0.1763 0.1913 0.2022 0.0138  0.0125  -0.0011 1030 ARG B O   
16631 C CB  . ARG B 1032 ? 0.1581 0.1710 0.1863 0.0141  0.0105  -0.0037 1030 ARG B CB  
16632 C CG  . ARG B 1032 ? 0.1738 0.1856 0.2036 0.0130  0.0111  -0.0030 1030 ARG B CG  
16633 C CD  . ARG B 1032 ? 0.1837 0.1925 0.2135 0.0130  0.0107  -0.0019 1030 ARG B CD  
16634 N NE  . ARG B 1032 ? 0.1911 0.1989 0.2228 0.0115  0.0110  -0.0013 1030 ARG B NE  
16635 C CZ  . ARG B 1032 ? 0.2243 0.2309 0.2561 0.0107  0.0114  0.0005  1030 ARG B CZ  
16636 N NH1 . ARG B 1032 ? 0.2313 0.2372 0.2611 0.0114  0.0117  0.0018  1030 ARG B NH1 
16637 N NH2 . ARG B 1032 ? 0.2329 0.2391 0.2667 0.0091  0.0115  0.0010  1030 ARG B NH2 
16638 N N   . LEU B 1033 ? 0.1603 0.1777 0.1842 0.0148  0.0115  -0.0027 1031 LEU B N   
16639 C CA  . LEU B 1033 ? 0.1565 0.1754 0.1790 0.0146  0.0123  -0.0028 1031 LEU B CA  
16640 C C   . LEU B 1033 ? 0.1559 0.1756 0.1760 0.0152  0.0124  -0.0016 1031 LEU B C   
16641 O O   . LEU B 1033 ? 0.1712 0.1921 0.1893 0.0152  0.0128  -0.0018 1031 LEU B O   
16642 C CB  . LEU B 1033 ? 0.1619 0.1818 0.1840 0.0143  0.0119  -0.0046 1031 LEU B CB  
16643 C CG  . LEU B 1033 ? 0.1560 0.1750 0.1803 0.0138  0.0115  -0.0057 1031 LEU B CG  
16644 C CD1 . LEU B 1033 ? 0.1639 0.1834 0.1873 0.0135  0.0110  -0.0072 1031 LEU B CD1 
16645 C CD2 . LEU B 1033 ? 0.1799 0.1983 0.2059 0.0134  0.0124  -0.0053 1031 LEU B CD2 
16646 N N   . VAL B 1034 ? 0.1606 0.1793 0.1804 0.0159  0.0119  -0.0004 1032 VAL B N   
16647 C CA  . VAL B 1034 ? 0.1796 0.1987 0.1971 0.0166  0.0118  0.0011  1032 VAL B CA  
16648 C C   . VAL B 1034 ? 0.2010 0.2176 0.2187 0.0167  0.0121  0.0029  1032 VAL B C   
16649 O O   . VAL B 1034 ? 0.2168 0.2315 0.2365 0.0164  0.0120  0.0028  1032 VAL B O   
16650 C CB  . VAL B 1034 ? 0.1772 0.1978 0.1938 0.0176  0.0105  0.0007  1032 VAL B CB  
16651 C CG1 . VAL B 1034 ? 0.2011 0.2239 0.2169 0.0170  0.0101  -0.0008 1032 VAL B CG1 
16652 C CG2 . VAL B 1034 ? 0.1897 0.2094 0.2082 0.0182  0.0097  0.0003  1032 VAL B CG2 
16653 N N   . THR B 1035 ? 0.2101 0.2266 0.2257 0.0171  0.0123  0.0046  1033 THR B N   
16654 C CA  . THR B 1035 ? 0.2484 0.2621 0.2639 0.0169  0.0127  0.0065  1033 THR B CA  
16655 C C   . THR B 1035 ? 0.2448 0.2562 0.2602 0.0183  0.0114  0.0071  1033 THR B C   
16656 O O   . THR B 1035 ? 0.3030 0.3110 0.3187 0.0181  0.0114  0.0083  1033 THR B O   
16657 C CB  . THR B 1035 ? 0.3015 0.3155 0.3145 0.0167  0.0136  0.0084  1033 THR B CB  
16658 O OG1 . THR B 1035 ? 0.3509 0.3668 0.3614 0.0178  0.0129  0.0083  1033 THR B OG1 
16659 C CG2 . THR B 1035 ? 0.3341 0.3498 0.3476 0.0154  0.0152  0.0081  1033 THR B CG2 
16660 N N   . THR B 1036 ? 0.2011 0.2142 0.2161 0.0197  0.0103  0.0062  1034 THR B N   
16661 C CA  . THR B 1036 ? 0.2577 0.2692 0.2729 0.0214  0.0092  0.0064  1034 THR B CA  
16662 C C   . THR B 1036 ? 0.2505 0.2644 0.2674 0.0217  0.0086  0.0043  1034 THR B C   
16663 O O   . THR B 1036 ? 0.2277 0.2451 0.2443 0.0216  0.0084  0.0035  1034 THR B O   
16664 C CB  . THR B 1036 ? 0.3052 0.3175 0.3181 0.0230  0.0084  0.0078  1034 THR B CB  
16665 O OG1 . THR B 1036 ? 0.3894 0.3998 0.4003 0.0224  0.0090  0.0098  1034 THR B OG1 
16666 C CG2 . THR B 1036 ? 0.3500 0.3605 0.3631 0.0252  0.0073  0.0080  1034 THR B CG2 
16667 N N   . ALA B 1037 ? 0.2301 0.2420 0.2486 0.0219  0.0084  0.0034  1035 ALA B N   
16668 C CA  . ALA B 1037 ? 0.2042 0.2183 0.2242 0.0220  0.0081  0.0015  1035 ALA B CA  
16669 C C   . ALA B 1037 ? 0.2117 0.2283 0.2314 0.0240  0.0072  0.0014  1035 ALA B C   
16670 O O   . ALA B 1037 ? 0.2236 0.2387 0.2426 0.0258  0.0067  0.0024  1035 ALA B O   
16671 C CB  . ALA B 1037 ? 0.2413 0.2525 0.2628 0.0217  0.0081  0.0007  1035 ALA B CB  
16672 N N   . PRO B 1038 ? 0.1772 0.1978 0.1975 0.0236  0.0069  0.0003  1036 PRO B N   
16673 C CA  . PRO B 1038 ? 0.1870 0.2108 0.2077 0.0253  0.0061  0.0001  1036 PRO B CA  
16674 C C   . PRO B 1038 ? 0.1737 0.1966 0.1958 0.0264  0.0061  -0.0008 1036 PRO B C   
16675 O O   . PRO B 1038 ? 0.1818 0.2017 0.2043 0.0256  0.0065  -0.0015 1036 PRO B O   
16676 C CB  . PRO B 1038 ? 0.1959 0.2239 0.2170 0.0238  0.0059  -0.0008 1036 PRO B CB  
16677 C CG  . PRO B 1038 ? 0.2160 0.2422 0.2375 0.0218  0.0066  -0.0018 1036 PRO B CG  
16678 C CD  . PRO B 1038 ? 0.1840 0.2062 0.2049 0.0216  0.0073  -0.0008 1036 PRO B CD  
16679 N N   . VAL B 1039 ? 0.1835 0.2093 0.2060 0.0283  0.0055  -0.0009 1037 VAL B N   
16680 C CA  . VAL B 1039 ? 0.1834 0.2095 0.2070 0.0296  0.0055  -0.0019 1037 VAL B CA  
16681 C C   . VAL B 1039 ? 0.1908 0.2207 0.2156 0.0278  0.0057  -0.0032 1037 VAL B C   
16682 O O   . VAL B 1039 ? 0.1762 0.2110 0.2016 0.0275  0.0053  -0.0031 1037 VAL B O   
16683 C CB  . VAL B 1039 ? 0.1939 0.2221 0.2175 0.0327  0.0050  -0.0014 1037 VAL B CB  
16684 C CG1 . VAL B 1039 ? 0.2293 0.2581 0.2538 0.0341  0.0052  -0.0027 1037 VAL B CG1 
16685 C CG2 . VAL B 1039 ? 0.2281 0.2518 0.2500 0.0344  0.0046  0.0000  1037 VAL B CG2 
16686 N N   . PRO B 1040 ? 0.1773 0.2053 0.2026 0.0266  0.0062  -0.0043 1038 PRO B N   
16687 C CA  . PRO B 1040 ? 0.1752 0.2063 0.2014 0.0247  0.0063  -0.0054 1038 PRO B CA  
16688 C C   . PRO B 1040 ? 0.1589 0.1947 0.1861 0.0259  0.0062  -0.0057 1038 PRO B C   
16689 O O   . PRO B 1040 ? 0.1638 0.1996 0.1911 0.0285  0.0062  -0.0056 1038 PRO B O   
16690 C CB  . PRO B 1040 ? 0.1932 0.2206 0.2195 0.0236  0.0067  -0.0063 1038 PRO B CB  
16691 C CG  . PRO B 1040 ? 0.2240 0.2466 0.2496 0.0240  0.0068  -0.0056 1038 PRO B CG  
16692 C CD  . PRO B 1040 ? 0.1947 0.2173 0.2196 0.0264  0.0065  -0.0046 1038 PRO B CD  
16693 N N   . PRO B 1041 ? 0.1769 0.2166 0.2049 0.0242  0.0060  -0.0061 1039 PRO B N   
16694 C CA  . PRO B 1041 ? 0.1780 0.2226 0.2071 0.0249  0.0061  -0.0064 1039 PRO B CA  
16695 C C   . PRO B 1041 ? 0.1561 0.1987 0.1852 0.0263  0.0067  -0.0073 1039 PRO B C   
16696 O O   . PRO B 1041 ? 0.1907 0.2290 0.2191 0.0253  0.0070  -0.0080 1039 PRO B O   
16697 C CB  . PRO B 1041 ? 0.1839 0.2311 0.2134 0.0219  0.0059  -0.0068 1039 PRO B CB  
16698 C CG  . PRO B 1041 ? 0.2253 0.2701 0.2536 0.0202  0.0055  -0.0065 1039 PRO B CG  
16699 C CD  . PRO B 1041 ? 0.1998 0.2393 0.2273 0.0213  0.0059  -0.0064 1039 PRO B CD  
16700 N N   . GLN B 1042 ? 0.1667 0.2125 0.1966 0.0288  0.0069  -0.0073 1040 GLN B N   
16701 C CA  . GLN B 1042 ? 0.1884 0.2330 0.2180 0.0305  0.0076  -0.0082 1040 GLN B CA  
16702 C C   . GLN B 1042 ? 0.1764 0.2140 0.2044 0.0319  0.0076  -0.0086 1040 GLN B C   
16703 O O   . GLN B 1042 ? 0.1812 0.2166 0.2084 0.0330  0.0079  -0.0096 1040 GLN B O   
16704 C CB  . GLN B 1042 ? 0.2121 0.2579 0.2418 0.0283  0.0080  -0.0091 1040 GLN B CB  
16705 C CG  . GLN B 1042 ? 0.2643 0.3167 0.2955 0.0264  0.0080  -0.0087 1040 GLN B CG  
16706 C CD  . GLN B 1042 ? 0.3201 0.3726 0.3509 0.0240  0.0084  -0.0094 1040 GLN B CD  
16707 O OE1 . GLN B 1042 ? 0.4861 0.5431 0.5176 0.0242  0.0090  -0.0095 1040 GLN B OE1 
16708 N NE2 . GLN B 1042 ? 0.4205 0.4684 0.4503 0.0219  0.0081  -0.0098 1040 GLN B NE2 
16709 N N   . HIS B 1043 ? 0.1685 0.2026 0.1959 0.0318  0.0071  -0.0078 1041 HIS B N   
16710 C CA  . HIS B 1043 ? 0.1719 0.1991 0.1978 0.0323  0.0070  -0.0080 1041 HIS B CA  
16711 C C   . HIS B 1043 ? 0.1683 0.1936 0.1933 0.0357  0.0067  -0.0076 1041 HIS B C   
16712 O O   . HIS B 1043 ? 0.1932 0.2176 0.2178 0.0367  0.0063  -0.0064 1041 HIS B O   
16713 C CB  . HIS B 1043 ? 0.1825 0.2071 0.2082 0.0302  0.0067  -0.0071 1041 HIS B CB  
16714 C CG  . HIS B 1043 ? 0.1854 0.2035 0.2100 0.0301  0.0066  -0.0070 1041 HIS B CG  
16715 N ND1 . HIS B 1043 ? 0.2002 0.2153 0.2248 0.0283  0.0067  -0.0079 1041 HIS B ND1 
16716 C CD2 . HIS B 1043 ? 0.2027 0.2169 0.2262 0.0313  0.0062  -0.0061 1041 HIS B CD2 
16717 C CE1 . HIS B 1043 ? 0.1831 0.1929 0.2068 0.0283  0.0064  -0.0075 1041 HIS B CE1 
16718 N NE2 . HIS B 1043 ? 0.1843 0.1933 0.2072 0.0300  0.0061  -0.0064 1041 HIS B NE2 
16719 N N   . SER B 1044 ? 0.1543 0.1789 0.1787 0.0378  0.0070  -0.0087 1042 SER B N   
16720 C CA  . SER B 1044 ? 0.1594 0.1811 0.1825 0.0414  0.0067  -0.0087 1042 SER B CA  
16721 C C   . SER B 1044 ? 0.1561 0.1755 0.1779 0.0427  0.0071  -0.0104 1042 SER B C   
16722 O O   . SER B 1044 ? 0.1683 0.1896 0.1905 0.0410  0.0076  -0.0114 1042 SER B O   
16723 C CB  . SER B 1044 ? 0.1740 0.2015 0.1981 0.0441  0.0067  -0.0080 1042 SER B CB  
16724 O OG  . SER B 1044 ? 0.1847 0.2184 0.2102 0.0445  0.0075  -0.0088 1042 SER B OG  
16725 N N   . SER B 1045 ? 0.1649 0.1800 0.1848 0.0458  0.0068  -0.0107 1043 SER B N   
16726 C CA  . SER B 1045 ? 0.1561 0.1686 0.1742 0.0476  0.0071  -0.0125 1043 SER B CA  
16727 C C   . SER B 1045 ? 0.1807 0.1917 0.1974 0.0522  0.0069  -0.0126 1043 SER B C   
16728 O O   . SER B 1045 ? 0.1916 0.1994 0.2076 0.0534  0.0061  -0.0115 1043 SER B O   
16729 C CB  . SER B 1045 ? 0.1800 0.1849 0.1964 0.0456  0.0064  -0.0131 1043 SER B CB  
16730 O OG  . SER B 1045 ? 0.1947 0.1961 0.2087 0.0476  0.0065  -0.0148 1043 SER B OG  
16731 N N   . VAL B 1046 ? 0.1728 0.1861 0.1888 0.0550  0.0076  -0.0140 1044 VAL B N   
16732 C CA  . VAL B 1046 ? 0.1925 0.2039 0.2067 0.0598  0.0074  -0.0145 1044 VAL B CA  
16733 C C   . VAL B 1046 ? 0.2173 0.2188 0.2278 0.0610  0.0066  -0.0157 1044 VAL B C   
16734 O O   . VAL B 1046 ? 0.2244 0.2223 0.2326 0.0651  0.0063  -0.0161 1044 VAL B O   
16735 C CB  . VAL B 1046 ? 0.2244 0.2431 0.2396 0.0629  0.0087  -0.0154 1044 VAL B CB  
16736 C CG1 . VAL B 1046 ? 0.2625 0.2910 0.2815 0.0615  0.0092  -0.0141 1044 VAL B CG1 
16737 C CG2 . VAL B 1046 ? 0.2316 0.2497 0.2454 0.0620  0.0095  -0.0172 1044 VAL B CG2 
16738 N N   . HIS B 1047 ? 0.2071 0.2039 0.2167 0.0575  0.0062  -0.0162 1045 HIS B N   
16739 C CA  A HIS B 1047 ? 0.2308 0.2184 0.2368 0.0581  0.0053  -0.0174 1045 HIS B CA  
16740 C CA  B HIS B 1047 ? 0.2311 0.2187 0.2372 0.0578  0.0053  -0.0174 1045 HIS B CA  
16741 C C   . HIS B 1047 ? 0.2083 0.1890 0.2133 0.0570  0.0040  -0.0160 1045 HIS B C   
16742 O O   . HIS B 1047 ? 0.2285 0.2109 0.2357 0.0541  0.0038  -0.0143 1045 HIS B O   
16743 C CB  A HIS B 1047 ? 0.2290 0.2154 0.2345 0.0550  0.0054  -0.0187 1045 HIS B CB  
16744 C CB  B HIS B 1047 ? 0.2228 0.2092 0.2288 0.0540  0.0053  -0.0183 1045 HIS B CB  
16745 C CG  A HIS B 1047 ? 0.2032 0.1969 0.2097 0.0556  0.0068  -0.0197 1045 HIS B CG  
16746 C CG  B HIS B 1047 ? 0.2331 0.2100 0.2362 0.0529  0.0040  -0.0191 1045 HIS B CG  
16747 N ND1 A HIS B 1047 ? 0.2504 0.2446 0.2547 0.0594  0.0075  -0.0214 1045 HIS B ND1 
16748 N ND1 B HIS B 1047 ? 0.2662 0.2373 0.2655 0.0556  0.0035  -0.0210 1045 HIS B ND1 
16749 C CD2 A HIS B 1047 ? 0.2475 0.2482 0.2568 0.0529  0.0077  -0.0193 1045 HIS B CD2 
16750 C CD2 B HIS B 1047 ? 0.2408 0.2132 0.2441 0.0492  0.0030  -0.0183 1045 HIS B CD2 
16751 C CE1 A HIS B 1047 ? 0.2905 0.2921 0.2964 0.0588  0.0088  -0.0218 1045 HIS B CE1 
16752 C CE1 B HIS B 1047 ? 0.2644 0.2276 0.2617 0.0534  0.0021  -0.0212 1045 HIS B CE1 
16753 N NE2 A HIS B 1047 ? 0.2686 0.2740 0.2775 0.0548  0.0089  -0.0205 1045 HIS B NE2 
16754 N NE2 B HIS B 1047 ? 0.2758 0.2400 0.2758 0.0495  0.0018  -0.0196 1045 HIS B NE2 
16755 N N   . THR B 1048 ? 0.1970 0.1697 0.1985 0.0595  0.0030  -0.0167 1046 THR B N   
16756 C CA  . THR B 1048 ? 0.2299 0.1949 0.2298 0.0585  0.0016  -0.0153 1046 THR B CA  
16757 C C   . THR B 1048 ? 0.2247 0.1814 0.2218 0.0567  0.0005  -0.0166 1046 THR B C   
16758 O O   . THR B 1048 ? 0.2398 0.1930 0.2340 0.0592  0.0003  -0.0186 1046 THR B O   
16759 C CB  . THR B 1048 ? 0.2630 0.2250 0.2609 0.0630  0.0010  -0.0147 1046 THR B CB  
16760 O OG1 . THR B 1048 ? 0.2379 0.2085 0.2385 0.0650  0.0020  -0.0138 1046 THR B OG1 
16761 C CG2 . THR B 1048 ? 0.2845 0.2393 0.2811 0.0613  -0.0003 -0.0128 1046 THR B CG2 
16762 N N   . ASP B 1049 ? 0.2305 0.1841 0.2284 0.0525  -0.0002 -0.0154 1047 ASP B N   
16763 C CA  . ASP B 1049 ? 0.2332 0.1792 0.2287 0.0503  -0.0014 -0.0165 1047 ASP B CA  
16764 C C   . ASP B 1049 ? 0.2255 0.1622 0.2165 0.0534  -0.0027 -0.0171 1047 ASP B C   
16765 O O   . ASP B 1049 ? 0.2364 0.1702 0.2266 0.0549  -0.0033 -0.0156 1047 ASP B O   
16766 C CB  . ASP B 1049 ? 0.2163 0.1611 0.2138 0.0455  -0.0019 -0.0147 1047 ASP B CB  
16767 C CG  . ASP B 1049 ? 0.2343 0.1722 0.2301 0.0428  -0.0033 -0.0156 1047 ASP B CG  
16768 O OD1 . ASP B 1049 ? 0.2407 0.1703 0.2334 0.0432  -0.0047 -0.0154 1047 ASP B OD1 
16769 O OD2 . ASP B 1049 ? 0.2409 0.1816 0.2381 0.0404  -0.0030 -0.0166 1047 ASP B OD2 
16770 N N   . PRO B 1050 ? 0.2560 0.1876 0.2437 0.0546  -0.0034 -0.0195 1048 PRO B N   
16771 C CA  . PRO B 1050 ? 0.2748 0.1972 0.2577 0.0580  -0.0047 -0.0204 1048 PRO B CA  
16772 C C   . PRO B 1050 ? 0.2619 0.1752 0.2431 0.0551  -0.0066 -0.0190 1048 PRO B C   
16773 O O   . PRO B 1050 ? 0.2861 0.1921 0.2639 0.0577  -0.0077 -0.0186 1048 PRO B O   
16774 C CB  . PRO B 1050 ? 0.3080 0.2281 0.2879 0.0595  -0.0048 -0.0234 1048 PRO B CB  
16775 C CG  . PRO B 1050 ? 0.2956 0.2204 0.2782 0.0552  -0.0044 -0.0236 1048 PRO B CG  
16776 C CD  . PRO B 1050 ? 0.2703 0.2047 0.2581 0.0536  -0.0029 -0.0215 1048 PRO B CD  
16777 N N   . VAL B 1051 ? 0.2660 0.1794 0.2493 0.0499  -0.0070 -0.0181 1049 VAL B N   
16778 C CA  . VAL B 1051 ? 0.2631 0.1686 0.2452 0.0467  -0.0087 -0.0165 1049 VAL B CA  
16779 C C   . VAL B 1051 ? 0.2467 0.1540 0.2305 0.0465  -0.0083 -0.0136 1049 VAL B C   
16780 O O   . VAL B 1051 ? 0.2724 0.1720 0.2536 0.0466  -0.0096 -0.0123 1049 VAL B O   
16781 C CB  . VAL B 1051 ? 0.2913 0.1973 0.2755 0.0413  -0.0092 -0.0165 1049 VAL B CB  
16782 C CG1 . VAL B 1051 ? 0.3196 0.2182 0.3029 0.0377  -0.0109 -0.0146 1049 VAL B CG1 
16783 C CG2 . VAL B 1051 ? 0.3141 0.2178 0.2959 0.0417  -0.0099 -0.0195 1049 VAL B CG2 
16784 N N   . LEU B 1052 ? 0.2412 0.1581 0.2291 0.0463  -0.0066 -0.0125 1050 LEU B N   
16785 C CA  . LEU B 1052 ? 0.2289 0.1480 0.2179 0.0470  -0.0061 -0.0100 1050 LEU B CA  
16786 C C   . LEU B 1052 ? 0.2703 0.1846 0.2557 0.0521  -0.0068 -0.0101 1050 LEU B C   
16787 O O   . LEU B 1052 ? 0.2608 0.1699 0.2445 0.0522  -0.0077 -0.0081 1050 LEU B O   
16788 C CB  . LEU B 1052 ? 0.2344 0.1648 0.2278 0.0469  -0.0043 -0.0095 1050 LEU B CB  
16789 C CG  . LEU B 1052 ? 0.2183 0.1528 0.2133 0.0475  -0.0037 -0.0070 1050 LEU B CG  
16790 C CD1 . LEU B 1052 ? 0.2449 0.1797 0.2381 0.0529  -0.0037 -0.0071 1050 LEU B CD1 
16791 C CD2 . LEU B 1052 ? 0.2269 0.1563 0.2213 0.0443  -0.0045 -0.0045 1050 LEU B CD2 
16792 N N   . LEU B 1053 ? 0.2659 0.1817 0.2500 0.0564  -0.0064 -0.0124 1051 LEU B N   
16793 C CA  . LEU B 1053 ? 0.2899 0.2015 0.2706 0.0618  -0.0070 -0.0126 1051 LEU B CA  
16794 C C   . LEU B 1053 ? 0.2894 0.1882 0.2652 0.0618  -0.0091 -0.0126 1051 LEU B C   
16795 O O   . LEU B 1053 ? 0.3088 0.2027 0.2824 0.0641  -0.0100 -0.0111 1051 LEU B O   
16796 C CB  . LEU B 1053 ? 0.3145 0.2302 0.2947 0.0663  -0.0060 -0.0153 1051 LEU B CB  
16797 C CG  . LEU B 1053 ? 0.3428 0.2709 0.3273 0.0674  -0.0040 -0.0150 1051 LEU B CG  
16798 C CD1 . LEU B 1053 ? 0.3429 0.2749 0.3269 0.0709  -0.0030 -0.0177 1051 LEU B CD1 
16799 C CD2 . LEU B 1053 ? 0.3578 0.2889 0.3434 0.0701  -0.0039 -0.0129 1051 LEU B CD2 
16800 N N   . ASP B 1054 ? 0.2924 0.1855 0.2663 0.0593  -0.0100 -0.0142 1052 ASP B N   
16801 C CA  . ASP B 1054 ? 0.3218 0.2023 0.2908 0.0588  -0.0123 -0.0142 1052 ASP B CA  
16802 C C   . ASP B 1054 ? 0.2829 0.1601 0.2528 0.0548  -0.0131 -0.0109 1052 ASP B C   
16803 O O   . ASP B 1054 ? 0.3284 0.1963 0.2944 0.0557  -0.0147 -0.0098 1052 ASP B O   
16804 C CB  . ASP B 1054 ? 0.3417 0.2177 0.3090 0.0562  -0.0132 -0.0165 1052 ASP B CB  
16805 C CG  . ASP B 1054 ? 0.4149 0.2914 0.3798 0.0606  -0.0128 -0.0198 1052 ASP B CG  
16806 O OD1 . ASP B 1054 ? 0.3877 0.2662 0.3515 0.0660  -0.0120 -0.0204 1052 ASP B OD1 
16807 O OD2 . ASP B 1054 ? 0.4282 0.3030 0.3921 0.0586  -0.0133 -0.0219 1052 ASP B OD2 
16808 N N   . PHE B 1055 ? 0.2911 0.1759 0.2657 0.0505  -0.0120 -0.0092 1053 PHE B N   
16809 C CA  . PHE B 1055 ? 0.2885 0.1714 0.2641 0.0467  -0.0124 -0.0060 1053 PHE B CA  
16810 C C   . PHE B 1055 ? 0.2872 0.1704 0.2619 0.0499  -0.0122 -0.0039 1053 PHE B C   
16811 O O   . PHE B 1055 ? 0.3122 0.1881 0.2844 0.0491  -0.0134 -0.0017 1053 PHE B O   
16812 C CB  . PHE B 1055 ? 0.2947 0.1865 0.2756 0.0421  -0.0110 -0.0051 1053 PHE B CB  
16813 C CG  . PHE B 1055 ? 0.2773 0.1681 0.2595 0.0378  -0.0111 -0.0018 1053 PHE B CG  
16814 C CD1 . PHE B 1055 ? 0.3043 0.1859 0.2839 0.0346  -0.0129 -0.0008 1053 PHE B CD1 
16815 C CD2 . PHE B 1055 ? 0.2609 0.1601 0.2466 0.0368  -0.0095 0.0001  1053 PHE B CD2 
16816 C CE1 . PHE B 1055 ? 0.3280 0.2093 0.3090 0.0306  -0.0128 0.0023  1053 PHE B CE1 
16817 C CE2 . PHE B 1055 ? 0.2934 0.1920 0.2802 0.0330  -0.0094 0.0031  1053 PHE B CE2 
16818 C CZ  . PHE B 1055 ? 0.3008 0.1907 0.2853 0.0299  -0.0110 0.0042  1053 PHE B CZ  
16819 N N   . ALA B 1056 ? 0.2841 0.1755 0.2608 0.0537  -0.0107 -0.0045 1054 ALA B N   
16820 C CA  . ALA B 1056 ? 0.3015 0.1939 0.2776 0.0571  -0.0107 -0.0025 1054 ALA B CA  
16821 C C   . ALA B 1056 ? 0.3027 0.1845 0.2733 0.0613  -0.0125 -0.0028 1054 ALA B C   
16822 O O   . ALA B 1056 ? 0.3254 0.2025 0.2939 0.0619  -0.0134 -0.0004 1054 ALA B O   
16823 C CB  . ALA B 1056 ? 0.3206 0.2242 0.3000 0.0603  -0.0090 -0.0033 1054 ALA B CB  
16824 N N   . LYS B 1057 ? 0.3274 0.2049 0.2952 0.0642  -0.0130 -0.0058 1055 LYS B N   
16825 C CA  . LYS B 1057 ? 0.3507 0.2172 0.3128 0.0682  -0.0149 -0.0063 1055 LYS B CA  
16826 C C   . LYS B 1057 ? 0.3912 0.2462 0.3499 0.0643  -0.0169 -0.0045 1055 LYS B C   
16827 O O   . LYS B 1057 ? 0.4082 0.2550 0.3630 0.0664  -0.0184 -0.0030 1055 LYS B O   
16828 C CB  . LYS B 1057 ? 0.3795 0.2435 0.3390 0.0719  -0.0150 -0.0100 1055 LYS B CB  
16829 C CG  . LYS B 1057 ? 0.4447 0.3183 0.4063 0.0771  -0.0132 -0.0116 1055 LYS B CG  
16830 C CD  . LYS B 1057 ? 0.3875 0.2585 0.3461 0.0806  -0.0132 -0.0152 1055 LYS B CD  
16831 C CE  . LYS B 1057 ? 0.4103 0.2808 0.3696 0.0758  -0.0132 -0.0169 1055 LYS B CE  
16832 N NZ  . LYS B 1057 ? 0.4534 0.3242 0.4105 0.0794  -0.0127 -0.0204 1055 LYS B NZ  
16833 N N   . TRP B 1058 ? 0.3613 0.2156 0.3215 0.0586  -0.0171 -0.0046 1056 TRP B N   
16834 C CA  . TRP B 1058 ? 0.3932 0.2377 0.3508 0.0541  -0.0189 -0.0027 1056 TRP B CA  
16835 C C   . TRP B 1058 ? 0.3724 0.2180 0.3312 0.0522  -0.0187 0.0012  1056 TRP B C   
16836 O O   . TRP B 1058 ? 0.4144 0.2501 0.3691 0.0520  -0.0204 0.0031  1056 TRP B O   
16837 C CB  . TRP B 1058 ? 0.3662 0.2121 0.3263 0.0482  -0.0189 -0.0035 1056 TRP B CB  
16838 C CG  . TRP B 1058 ? 0.3851 0.2225 0.3435 0.0428  -0.0207 -0.0015 1056 TRP B CG  
16839 C CD1 . TRP B 1058 ? 0.4774 0.3021 0.4305 0.0422  -0.0231 -0.0022 1056 TRP B CD1 
16840 C CD2 . TRP B 1058 ? 0.3726 0.2138 0.3346 0.0372  -0.0200 0.0016  1056 TRP B CD2 
16841 N NE1 . TRP B 1058 ? 0.4660 0.2866 0.4195 0.0362  -0.0242 0.0005  1056 TRP B NE1 
16842 C CE2 . TRP B 1058 ? 0.4347 0.2656 0.3937 0.0331  -0.0222 0.0028  1056 TRP B CE2 
16843 C CE3 . TRP B 1058 ? 0.3785 0.2308 0.3458 0.0352  -0.0179 0.0034  1056 TRP B CE3 
16844 C CZ2 . TRP B 1058 ? 0.4058 0.2377 0.3672 0.0272  -0.0221 0.0059  1056 TRP B CZ2 
16845 C CZ3 . TRP B 1058 ? 0.4031 0.2562 0.3725 0.0296  -0.0178 0.0063  1056 TRP B CZ3 
16846 C CH2 . TRP B 1058 ? 0.4000 0.2433 0.3667 0.0256  -0.0198 0.0076  1056 TRP B CH2 
16847 N N   . LEU B 1059 ? 0.3365 0.1935 0.3003 0.0509  -0.0167 0.0025  1057 LEU B N   
16848 C CA  . LEU B 1059 ? 0.3641 0.2230 0.3288 0.0497  -0.0163 0.0061  1057 LEU B CA  
16849 C C   . LEU B 1059 ? 0.4098 0.2642 0.3708 0.0553  -0.0172 0.0070  1057 LEU B C   
16850 O O   . LEU B 1059 ? 0.4073 0.2553 0.3655 0.0544  -0.0183 0.0099  1057 LEU B O   
16851 C CB  . LEU B 1059 ? 0.3356 0.2078 0.3060 0.0482  -0.0140 0.0067  1057 LEU B CB  
16852 C CG  . LEU B 1059 ? 0.3055 0.1824 0.2797 0.0425  -0.0131 0.0065  1057 LEU B CG  
16853 C CD1 . LEU B 1059 ? 0.3281 0.2178 0.3074 0.0421  -0.0109 0.0066  1057 LEU B CD1 
16854 C CD2 . LEU B 1059 ? 0.3869 0.2583 0.3604 0.0372  -0.0139 0.0093  1057 LEU B CD2 
16855 N N   . ASP B 1060 ? 0.3767 0.2347 0.3376 0.0610  -0.0168 0.0047  1058 ASP B N   
16856 C CA  . ASP B 1060 ? 0.4179 0.2717 0.3753 0.0670  -0.0177 0.0052  1058 ASP B CA  
16857 C C   . ASP B 1060 ? 0.4591 0.2978 0.4102 0.0673  -0.0202 0.0058  1058 ASP B C   
16858 O O   . ASP B 1060 ? 0.4904 0.3234 0.4385 0.0687  -0.0214 0.0083  1058 ASP B O   
16859 C CB  . ASP B 1060 ? 0.4360 0.2942 0.3937 0.0729  -0.0171 0.0019  1058 ASP B CB  
16860 C CG  . ASP B 1060 ? 0.4875 0.3601 0.4506 0.0742  -0.0149 0.0017  1058 ASP B CG  
16861 O OD1 . ASP B 1060 ? 0.4560 0.3341 0.4215 0.0728  -0.0143 0.0044  1058 ASP B OD1 
16862 O OD2 . ASP B 1060 ? 0.4699 0.3481 0.4345 0.0768  -0.0139 -0.0011 1058 ASP B OD2 
16863 N N   . GLY B 1061 ? 0.4504 0.2823 0.3992 0.0661  -0.0212 0.0033  1059 GLY B N   
16864 C CA  . GLY B 1061 ? 0.4896 0.3065 0.4319 0.0668  -0.0238 0.0034  1059 GLY B CA  
16865 C C   . GLY B 1061 ? 0.5140 0.3240 0.4547 0.0616  -0.0250 0.0071  1059 GLY B C   
16866 O O   . GLY B 1061 ? 0.5152 0.3140 0.4507 0.0631  -0.0270 0.0085  1059 GLY B O   
16867 N N   . LYS B 1062 ? 0.4730 0.2896 0.4182 0.0554  -0.0238 0.0088  1060 LYS B N   
16868 C CA  . LYS B 1062 ? 0.5229 0.3342 0.4671 0.0501  -0.0246 0.0125  1060 LYS B CA  
16869 C C   . LYS B 1062 ? 0.5618 0.3784 0.5073 0.0508  -0.0237 0.0160  1060 LYS B C   
16870 O O   . LYS B 1062 ? 0.6033 0.4178 0.5487 0.0461  -0.0239 0.0194  1060 LYS B O   
16871 C CB  . LYS B 1062 ? 0.5516 0.3659 0.4993 0.0429  -0.0241 0.0127  1060 LYS B CB  
16872 C CG  . LYS B 1062 ? 0.5465 0.3754 0.5009 0.0408  -0.0214 0.0128  1060 LYS B CG  
16873 C CD  . LYS B 1062 ? 0.4872 0.3181 0.4448 0.0342  -0.0211 0.0127  1060 LYS B CD  
16874 C CE  . LYS B 1062 ? 0.4979 0.3209 0.4535 0.0289  -0.0225 0.0160  1060 LYS B CE  
16875 N NZ  . LYS B 1062 ? 0.5693 0.3916 0.5268 0.0231  -0.0230 0.0154  1060 LYS B NZ  
16876 N N   . GLY B 1063 ? 0.5034 0.3267 0.4500 0.0563  -0.0227 0.0153  1061 GLY B N   
16877 C CA  . GLY B 1063 ? 0.5260 0.3536 0.4732 0.0575  -0.0222 0.0184  1061 GLY B CA  
16878 C C   . GLY B 1063 ? 0.5268 0.3666 0.4796 0.0536  -0.0199 0.0199  1061 GLY B C   
16879 O O   . GLY B 1063 ? 0.5016 0.3449 0.4547 0.0539  -0.0194 0.0227  1061 GLY B O   
16880 N N   . ALA B 1064 ? 0.4643 0.3106 0.4214 0.0500  -0.0185 0.0181  1062 ALA B N   
16881 C CA  . ALA B 1064 ? 0.4502 0.3080 0.4125 0.0464  -0.0163 0.0191  1062 ALA B CA  
16882 C C   . ALA B 1064 ? 0.4258 0.2944 0.3912 0.0507  -0.0149 0.0177  1062 ALA B C   
16883 O O   . ALA B 1064 ? 0.3693 0.2457 0.3384 0.0507  -0.0136 0.0152  1062 ALA B O   
16884 C CB  . ALA B 1064 ? 0.4514 0.3117 0.4169 0.0413  -0.0156 0.0178  1062 ALA B CB  
16885 N N   . ARG B 1065 ? 0.4451 0.3139 0.4087 0.0544  -0.0153 0.0196  1063 ARG B N   
16886 C CA  . ARG B 1065 ? 0.4229 0.3005 0.3887 0.0593  -0.0145 0.0182  1063 ARG B CA  
16887 C C   . ARG B 1065 ? 0.4049 0.2950 0.3759 0.0567  -0.0124 0.0181  1063 ARG B C   
16888 O O   . ARG B 1065 ? 0.3871 0.2852 0.3613 0.0586  -0.0114 0.0157  1063 ARG B O   
16889 C CB  . ARG B 1065 ? 0.4893 0.3639 0.4519 0.0636  -0.0157 0.0205  1063 ARG B CB  
16890 N N   . ALA B 1066 ? 0.3601 0.2522 0.3320 0.0524  -0.0117 0.0208  1064 ALA B N   
16891 C CA  . ALA B 1066 ? 0.3506 0.2539 0.3271 0.0499  -0.0098 0.0206  1064 ALA B CA  
16892 C C   . ALA B 1066 ? 0.3438 0.2507 0.3237 0.0474  -0.0088 0.0179  1064 ALA B C   
16893 O O   . ALA B 1066 ? 0.3434 0.2594 0.3269 0.0480  -0.0075 0.0161  1064 ALA B O   
16894 C CB  . ALA B 1066 ? 0.4123 0.3160 0.3886 0.0457  -0.0092 0.0239  1064 ALA B CB  
16895 N N   . GLU B 1067 ? 0.3234 0.2232 0.3021 0.0445  -0.0094 0.0175  1065 GLU B N   
16896 C CA  . GLU B 1067 ? 0.3383 0.2412 0.3200 0.0419  -0.0086 0.0150  1065 GLU B CA  
16897 C C   . GLU B 1067 ? 0.3044 0.2089 0.2865 0.0460  -0.0087 0.0116  1065 GLU B C   
16898 O O   . GLU B 1067 ? 0.2950 0.2065 0.2804 0.0453  -0.0075 0.0096  1065 GLU B O   
16899 C CB  . GLU B 1067 ? 0.3329 0.2278 0.3132 0.0377  -0.0095 0.0156  1065 GLU B CB  
16900 C CG  . GLU B 1067 ? 0.3560 0.2512 0.3369 0.0329  -0.0089 0.0188  1065 GLU B CG  
16901 C CD  . GLU B 1067 ? 0.3983 0.2873 0.3753 0.0337  -0.0099 0.0220  1065 GLU B CD  
16902 O OE1 . GLU B 1067 ? 0.4021 0.2850 0.3754 0.0380  -0.0114 0.0218  1065 GLU B OE1 
16903 O OE2 . GLU B 1067 ? 0.3958 0.2860 0.3732 0.0301  -0.0092 0.0248  1065 GLU B OE2 
16904 N N   . ALA B 1068 ? 0.3085 0.2062 0.2868 0.0504  -0.0101 0.0111  1066 ALA B N   
16905 C CA  . ALA B 1068 ? 0.3449 0.2446 0.3233 0.0547  -0.0101 0.0079  1066 ALA B CA  
16906 C C   . ALA B 1068 ? 0.3251 0.2363 0.3071 0.0571  -0.0086 0.0074  1066 ALA B C   
16907 O O   . ALA B 1068 ? 0.2826 0.1996 0.2670 0.0579  -0.0076 0.0049  1066 ALA B O   
16908 C CB  . ALA B 1068 ? 0.3205 0.2109 0.2940 0.0595  -0.0118 0.0077  1066 ALA B CB  
16909 N N   . GLU B 1069 ? 0.2926 0.2071 0.2749 0.0579  -0.0085 0.0098  1067 GLU B N   
16910 C CA  . GLU B 1069 ? 0.3243 0.2499 0.3101 0.0595  -0.0073 0.0095  1067 GLU B CA  
16911 C C   . GLU B 1069 ? 0.3253 0.2585 0.3151 0.0552  -0.0057 0.0088  1067 GLU B C   
16912 O O   . GLU B 1069 ? 0.2939 0.2351 0.2867 0.0561  -0.0047 0.0070  1067 GLU B O   
16913 C CB  . GLU B 1069 ? 0.3378 0.2646 0.3226 0.0608  -0.0078 0.0124  1067 GLU B CB  
16914 C CG  . GLU B 1069 ? 0.4076 0.3457 0.3958 0.0617  -0.0068 0.0125  1067 GLU B CG  
16915 C CD  . GLU B 1069 ? 0.4900 0.4329 0.4793 0.0669  -0.0068 0.0106  1067 GLU B CD  
16916 O OE1 . GLU B 1069 ? 0.4834 0.4205 0.4704 0.0703  -0.0076 0.0093  1067 GLU B OE1 
16917 O OE2 . GLU B 1069 ? 0.5388 0.4913 0.5312 0.0674  -0.0061 0.0104  1067 GLU B OE2 
16918 N N   . ALA B 1070 ? 0.3132 0.2442 0.3032 0.0504  -0.0054 0.0103  1068 ALA B N   
16919 C CA  . ALA B 1070 ? 0.3069 0.2445 0.3006 0.0464  -0.0040 0.0095  1068 ALA B CA  
16920 C C   . ALA B 1070 ? 0.2397 0.1776 0.2347 0.0463  -0.0038 0.0066  1068 ALA B C   
16921 O O   . ALA B 1070 ? 0.2768 0.2221 0.2749 0.0454  -0.0026 0.0051  1068 ALA B O   
16922 C CB  . ALA B 1070 ? 0.3259 0.2606 0.3195 0.0416  -0.0038 0.0116  1068 ALA B CB  
16923 N N   . ALA B 1071 ? 0.2582 0.1876 0.2503 0.0472  -0.0049 0.0056  1069 ALA B N   
16924 C CA  . ALA B 1071 ? 0.2504 0.1796 0.2430 0.0472  -0.0048 0.0027  1069 ALA B CA  
16925 C C   . ALA B 1071 ? 0.2571 0.1927 0.2510 0.0512  -0.0041 0.0007  1069 ALA B C   
16926 O O   . ALA B 1071 ? 0.2366 0.1781 0.2330 0.0502  -0.0031 -0.0010 1069 ALA B O   
16927 C CB  . ALA B 1071 ? 0.2645 0.1829 0.2533 0.0476  -0.0065 0.0021  1069 ALA B CB  
16928 N N   . ARG B 1072 ? 0.2489 0.1838 0.2410 0.0558  -0.0047 0.0011  1070 ARG B N   
16929 C CA  A ARG B 1072 ? 0.2547 0.1964 0.2482 0.0598  -0.0039 -0.0006 1070 ARG B CA  
16930 C CA  B ARG B 1072 ? 0.2547 0.1965 0.2483 0.0598  -0.0039 -0.0006 1070 ARG B CA  
16931 C C   . ARG B 1072 ? 0.2706 0.2231 0.2683 0.0581  -0.0026 -0.0002 1070 ARG B C   
16932 O O   . ARG B 1072 ? 0.2444 0.2033 0.2444 0.0585  -0.0016 -0.0021 1070 ARG B O   
16933 C CB  A ARG B 1072 ? 0.2646 0.2042 0.2558 0.0651  -0.0048 0.0001  1070 ARG B CB  
16934 C CB  B ARG B 1072 ? 0.2651 0.2044 0.2562 0.0651  -0.0048 -0.0001 1070 ARG B CB  
16935 C CG  A ARG B 1072 ? 0.3015 0.2309 0.2883 0.0680  -0.0061 -0.0011 1070 ARG B CG  
16936 C CG  B ARG B 1072 ? 0.3004 0.2283 0.2868 0.0671  -0.0063 -0.0008 1070 ARG B CG  
16937 C CD  A ARG B 1072 ? 0.3062 0.2345 0.2910 0.0738  -0.0069 -0.0006 1070 ARG B CD  
16938 C CD  B ARG B 1072 ? 0.3065 0.2328 0.2907 0.0735  -0.0070 -0.0013 1070 ARG B CD  
16939 N NE  A ARG B 1072 ? 0.3175 0.2436 0.3013 0.0734  -0.0077 0.0025  1070 ARG B NE  
16940 N NE  B ARG B 1072 ? 0.3172 0.2314 0.2964 0.0752  -0.0086 -0.0018 1070 ARG B NE  
16941 C CZ  A ARG B 1072 ? 0.3689 0.2845 0.3486 0.0735  -0.0093 0.0040  1070 ARG B CZ  
16942 C CZ  B ARG B 1072 ? 0.3213 0.2309 0.2984 0.0760  -0.0088 -0.0045 1070 ARG B CZ  
16943 N NH1 A ARG B 1072 ? 0.3499 0.2559 0.3260 0.0740  -0.0103 0.0025  1070 ARG B NH1 
16944 N NH1 B ARG B 1072 ? 0.3729 0.2891 0.3524 0.0757  -0.0074 -0.0068 1070 ARG B NH1 
16945 N NH2 A ARG B 1072 ? 0.3165 0.2310 0.2953 0.0730  -0.0099 0.0069  1070 ARG B NH2 
16946 N NH2 B ARG B 1072 ? 0.3371 0.2348 0.3093 0.0771  -0.0105 -0.0048 1070 ARG B NH2 
16947 N N   . ASN B 1073 ? 0.2544 0.2089 0.2530 0.0560  -0.0025 0.0021  1071 ASN B N   
16948 C CA  . ASN B 1073 ? 0.2619 0.2258 0.2639 0.0542  -0.0014 0.0025  1071 ASN B CA  
16949 C C   . ASN B 1073 ? 0.2569 0.2236 0.2612 0.0503  -0.0004 0.0011  1071 ASN B C   
16950 O O   . ASN B 1073 ? 0.2628 0.2370 0.2698 0.0500  0.0005  0.0000  1071 ASN B O   
16951 C CB  . ASN B 1073 ? 0.2859 0.2503 0.2876 0.0526  -0.0016 0.0052  1071 ASN B CB  
16952 C CG  . ASN B 1073 ? 0.3615 0.3259 0.3617 0.0567  -0.0025 0.0066  1071 ASN B CG  
16953 O OD1 . ASN B 1073 ? 0.3682 0.3350 0.3686 0.0607  -0.0027 0.0054  1071 ASN B OD1 
16954 N ND2 . ASN B 1073 ? 0.3967 0.3587 0.3953 0.0558  -0.0030 0.0091  1071 ASN B ND2 
16955 N N   . ALA B 1074 ? 0.2325 0.1931 0.2358 0.0473  -0.0007 0.0012  1072 ALA B N   
16956 C CA  . ALA B 1074 ? 0.2473 0.2102 0.2528 0.0439  0.0001  -0.0001 1072 ALA B CA  
16957 C C   . ALA B 1074 ? 0.2095 0.1738 0.2152 0.0457  0.0003  -0.0027 1072 ALA B C   
16958 O O   . ALA B 1074 ? 0.2184 0.1883 0.2265 0.0442  0.0012  -0.0039 1072 ALA B O   
16959 C CB  . ALA B 1074 ? 0.2544 0.2106 0.2589 0.0405  -0.0005 0.0006  1072 ALA B CB  
16960 N N   . GLY B 1075 ? 0.2175 0.1762 0.2205 0.0489  -0.0006 -0.0037 1073 GLY B N   
16961 C CA  . GLY B 1075 ? 0.2402 0.2002 0.2429 0.0509  -0.0002 -0.0062 1073 GLY B CA  
16962 C C   . GLY B 1075 ? 0.2348 0.2043 0.2401 0.0527  0.0009  -0.0068 1073 GLY B C   
16963 O O   . GLY B 1075 ? 0.2375 0.2111 0.2441 0.0522  0.0017  -0.0085 1073 GLY B O   
16964 N N   . SER B 1076 ? 0.2408 0.2140 0.2468 0.0545  0.0009  -0.0053 1074 SER B N   
16965 C CA  . SER B 1076 ? 0.2285 0.2110 0.2370 0.0561  0.0018  -0.0056 1074 SER B CA  
16966 C C   . SER B 1076 ? 0.2275 0.2164 0.2390 0.0522  0.0026  -0.0051 1074 SER B C   
16967 O O   . SER B 1076 ? 0.2449 0.2401 0.2584 0.0518  0.0035  -0.0063 1074 SER B O   
16968 C CB  . SER B 1076 ? 0.2549 0.2392 0.2631 0.0597  0.0013  -0.0042 1074 SER B CB  
16969 O OG  . SER B 1076 ? 0.2884 0.2682 0.2941 0.0642  0.0007  -0.0051 1074 SER B OG  
16970 N N   . SER B 1077 ? 0.2245 0.2117 0.2362 0.0492  0.0024  -0.0035 1075 SER B N   
16971 C CA  A SER B 1077 ? 0.2541 0.2471 0.2684 0.0458  0.0031  -0.0031 1075 SER B CA  
16972 C CA  B SER B 1077 ? 0.2540 0.2472 0.2683 0.0459  0.0031  -0.0032 1075 SER B CA  
16973 C C   . SER B 1077 ? 0.2243 0.2170 0.2395 0.0428  0.0037  -0.0045 1075 SER B C   
16974 O O   . SER B 1077 ? 0.2610 0.2592 0.2783 0.0407  0.0043  -0.0048 1075 SER B O   
16975 C CB  A SER B 1077 ? 0.2848 0.2759 0.2985 0.0439  0.0028  -0.0009 1075 SER B CB  
16976 C CB  B SER B 1077 ? 0.2921 0.2848 0.3062 0.0442  0.0029  -0.0010 1075 SER B CB  
16977 O OG  A SER B 1077 ? 0.2912 0.2820 0.3037 0.0467  0.0022  0.0005  1075 SER B OG  
16978 O OG  B SER B 1077 ? 0.2751 0.2615 0.2880 0.0418  0.0027  -0.0004 1075 SER B OG  
16979 N N   . SER B 1078 ? 0.1968 0.1830 0.2104 0.0424  0.0032  -0.0053 1076 SER B N   
16980 C CA  . SER B 1078 ? 0.2052 0.1910 0.2196 0.0397  0.0035  -0.0067 1076 SER B CA  
16981 C C   . SER B 1078 ? 0.1890 0.1809 0.2048 0.0404  0.0043  -0.0082 1076 SER B C   
16982 O O   . SER B 1078 ? 0.1972 0.1911 0.2125 0.0436  0.0044  -0.0089 1076 SER B O   
16983 C CB  . SER B 1078 ? 0.2063 0.1845 0.2183 0.0403  0.0027  -0.0076 1076 SER B CB  
16984 O OG  . SER B 1078 ? 0.1922 0.1703 0.2048 0.0382  0.0028  -0.0091 1076 SER B OG  
16985 N N   . ALA B 1079 ? 0.1710 0.1659 0.1885 0.0374  0.0048  -0.0086 1077 ALA B N   
16986 C CA  . ALA B 1079 ? 0.1807 0.1808 0.1992 0.0375  0.0054  -0.0099 1077 ALA B CA  
16987 C C   . ALA B 1079 ? 0.1743 0.1712 0.1919 0.0368  0.0053  -0.0115 1077 ALA B C   
16988 O O   . ALA B 1079 ? 0.1675 0.1680 0.1857 0.0361  0.0058  -0.0125 1077 ALA B O   
16989 C CB  . ALA B 1079 ? 0.1924 0.1982 0.2132 0.0350  0.0060  -0.0093 1077 ALA B CB  
16990 N N   . LEU B 1080 ? 0.1654 0.1554 0.1811 0.0368  0.0045  -0.0118 1078 LEU B N   
16991 C CA  . LEU B 1080 ? 0.1662 0.1526 0.1804 0.0364  0.0041  -0.0135 1078 LEU B CA  
16992 C C   . LEU B 1080 ? 0.1710 0.1602 0.1843 0.0392  0.0047  -0.0149 1078 LEU B C   
16993 O O   . LEU B 1080 ? 0.1877 0.1772 0.1999 0.0426  0.0049  -0.0150 1078 LEU B O   
16994 C CB  . LEU B 1080 ? 0.1734 0.1517 0.1853 0.0369  0.0030  -0.0135 1078 LEU B CB  
16995 C CG  . LEU B 1080 ? 0.1735 0.1472 0.1832 0.0370  0.0023  -0.0154 1078 LEU B CG  
16996 C CD1 . LEU B 1080 ? 0.1902 0.1643 0.2012 0.0334  0.0020  -0.0157 1078 LEU B CD1 
16997 C CD2 . LEU B 1080 ? 0.1953 0.1608 0.2021 0.0382  0.0010  -0.0154 1078 LEU B CD2 
16998 N N   . GLY B 1081 ? 0.1575 0.1488 0.1709 0.0379  0.0051  -0.0161 1079 GLY B N   
16999 C CA  . GLY B 1081 ? 0.1802 0.1747 0.1927 0.0402  0.0058  -0.0174 1079 GLY B CA  
17000 C C   . GLY B 1081 ? 0.1859 0.1887 0.2007 0.0399  0.0069  -0.0169 1079 GLY B C   
17001 O O   . GLY B 1081 ? 0.2031 0.2095 0.2174 0.0414  0.0078  -0.0178 1079 GLY B O   
17002 N N   . LEU B 1082 ? 0.1723 0.1782 0.1895 0.0379  0.0070  -0.0154 1080 LEU B N   
17003 C CA  A LEU B 1082 ? 0.1716 0.1847 0.1908 0.0368  0.0078  -0.0150 1080 LEU B CA  
17004 C CA  B LEU B 1082 ? 0.1713 0.1845 0.1905 0.0368  0.0078  -0.0150 1080 LEU B CA  
17005 C C   . LEU B 1082 ? 0.1748 0.1892 0.1937 0.0350  0.0081  -0.0160 1080 LEU B C   
17006 O O   . LEU B 1082 ? 0.1879 0.1981 0.2060 0.0331  0.0075  -0.0165 1080 LEU B O   
17007 C CB  A LEU B 1082 ? 0.1725 0.1869 0.1936 0.0343  0.0075  -0.0135 1080 LEU B CB  
17008 C CB  B LEU B 1082 ? 0.1723 0.1868 0.1934 0.0344  0.0075  -0.0135 1080 LEU B CB  
17009 C CG  A LEU B 1082 ? 0.1680 0.1889 0.1910 0.0325  0.0080  -0.0130 1080 LEU B CG  
17010 C CG  B LEU B 1082 ? 0.1676 0.1886 0.1906 0.0326  0.0080  -0.0129 1080 LEU B CG  
17011 C CD1 A LEU B 1082 ? 0.2250 0.2518 0.2488 0.0348  0.0086  -0.0127 1080 LEU B CD1 
17012 C CD1 B LEU B 1082 ? 0.1858 0.2077 0.2100 0.0316  0.0077  -0.0115 1080 LEU B CD1 
17013 C CD2 A LEU B 1082 ? 0.1955 0.2166 0.2197 0.0304  0.0077  -0.0117 1080 LEU B CD2 
17014 C CD2 B LEU B 1082 ? 0.1707 0.1918 0.1939 0.0296  0.0081  -0.0135 1080 LEU B CD2 
17015 N N   . ASP B 1083 ? 0.1912 0.2114 0.2106 0.0356  0.0090  -0.0162 1081 ASP B N   
17016 C CA  . ASP B 1083 ? 0.2349 0.2563 0.2535 0.0342  0.0094  -0.0171 1081 ASP B CA  
17017 C C   . ASP B 1083 ? 0.2024 0.2314 0.2228 0.0333  0.0103  -0.0164 1081 ASP B C   
17018 O O   . ASP B 1083 ? 0.2546 0.2882 0.2752 0.0355  0.0112  -0.0165 1081 ASP B O   
17019 C CB  . ASP B 1083 ? 0.2543 0.2732 0.2703 0.0369  0.0097  -0.0186 1081 ASP B CB  
17020 C CG  . ASP B 1083 ? 0.3996 0.4189 0.4141 0.0355  0.0100  -0.0196 1081 ASP B CG  
17021 O OD1 . ASP B 1083 ? 0.4238 0.4442 0.4393 0.0324  0.0098  -0.0190 1081 ASP B OD1 
17022 O OD2 . ASP B 1083 ? 0.4509 0.4693 0.4630 0.0378  0.0105  -0.0208 1081 ASP B OD2 
17023 N N   . LEU B 1084 ? 0.1934 0.2238 0.2151 0.0301  0.0100  -0.0156 1082 LEU B N   
17024 C CA  . LEU B 1084 ? 0.2100 0.2469 0.2334 0.0286  0.0105  -0.0147 1082 LEU B CA  
17025 C C   . LEU B 1084 ? 0.2041 0.2418 0.2269 0.0259  0.0106  -0.0149 1082 LEU B C   
17026 O O   . LEU B 1084 ? 0.1944 0.2274 0.2161 0.0244  0.0100  -0.0154 1082 LEU B O   
17027 C CB  . LEU B 1084 ? 0.2349 0.2723 0.2600 0.0270  0.0098  -0.0136 1082 LEU B CB  
17028 C CG  . LEU B 1084 ? 0.2872 0.3245 0.3130 0.0292  0.0096  -0.0129 1082 LEU B CG  
17029 C CD1 . LEU B 1084 ? 0.3004 0.3378 0.3273 0.0272  0.0089  -0.0119 1082 LEU B CD1 
17030 C CD2 . LEU B 1084 ? 0.3099 0.3532 0.3366 0.0317  0.0102  -0.0127 1082 LEU B CD2 
17031 N N   . GLU B 1085 ? 0.1830 0.2267 0.2066 0.0251  0.0113  -0.0144 1083 GLU B N   
17032 C CA  . GLU B 1085 ? 0.1676 0.2125 0.1910 0.0218  0.0112  -0.0141 1083 GLU B CA  
17033 C C   . GLU B 1085 ? 0.1798 0.2269 0.2048 0.0195  0.0106  -0.0130 1083 GLU B C   
17034 O O   . GLU B 1085 ? 0.2072 0.2591 0.2339 0.0201  0.0108  -0.0122 1083 GLU B O   
17035 C CB  . GLU B 1085 ? 0.1978 0.2477 0.2207 0.0220  0.0123  -0.0141 1083 GLU B CB  
17036 C CG  . GLU B 1085 ? 0.2228 0.2728 0.2449 0.0184  0.0120  -0.0136 1083 GLU B CG  
17037 C CD  . GLU B 1085 ? 0.2857 0.3399 0.3068 0.0180  0.0131  -0.0135 1083 GLU B CD  
17038 O OE1 . GLU B 1085 ? 0.3153 0.3719 0.3359 0.0208  0.0142  -0.0141 1083 GLU B OE1 
17039 O OE2 . GLU B 1085 ? 0.2872 0.3421 0.3077 0.0149  0.0129  -0.0128 1083 GLU B OE2 
17040 N N   . LEU B 1086 ? 0.1818 0.2255 0.2063 0.0169  0.0098  -0.0129 1084 LEU B N   
17041 C CA  . LEU B 1086 ? 0.1739 0.2186 0.1993 0.0147  0.0091  -0.0121 1084 LEU B CA  
17042 C C   . LEU B 1086 ? 0.2062 0.2543 0.2314 0.0119  0.0091  -0.0115 1084 LEU B C   
17043 O O   . LEU B 1086 ? 0.2168 0.2641 0.2407 0.0110  0.0094  -0.0117 1084 LEU B O   
17044 C CB  . LEU B 1086 ? 0.2017 0.2406 0.2265 0.0136  0.0082  -0.0124 1084 LEU B CB  
17045 C CG  . LEU B 1086 ? 0.1943 0.2296 0.2193 0.0158  0.0082  -0.0128 1084 LEU B CG  
17046 C CD1 . LEU B 1086 ? 0.2211 0.2518 0.2459 0.0145  0.0074  -0.0129 1084 LEU B CD1 
17047 C CD2 . LEU B 1086 ? 0.2501 0.2882 0.2764 0.0174  0.0083  -0.0122 1084 LEU B CD2 
17048 N N   . PRO B 1087 ? 0.1831 0.2349 0.2095 0.0104  0.0088  -0.0106 1085 PRO B N   
17049 C CA  . PRO B 1087 ? 0.1988 0.2536 0.2250 0.0073  0.0086  -0.0099 1085 PRO B CA  
17050 C C   . PRO B 1087 ? 0.1979 0.2473 0.2221 0.0050  0.0078  -0.0101 1085 PRO B C   
17051 O O   . PRO B 1087 ? 0.2169 0.2616 0.2406 0.0050  0.0070  -0.0106 1085 PRO B O   
17052 C CB  . PRO B 1087 ? 0.2244 0.2828 0.2521 0.0063  0.0079  -0.0091 1085 PRO B CB  
17053 C CG  . PRO B 1087 ? 0.2564 0.3164 0.2856 0.0095  0.0083  -0.0092 1085 PRO B CG  
17054 C CD  . PRO B 1087 ? 0.2009 0.2550 0.2289 0.0116  0.0085  -0.0102 1085 PRO B CD  
17055 N N   . GLY B 1088 ? 0.1987 0.2488 0.2216 0.0031  0.0079  -0.0098 1086 GLY B N   
17056 C CA  . GLY B 1088 ? 0.2158 0.2609 0.2367 0.0010  0.0071  -0.0099 1086 GLY B CA  
17057 C C   . GLY B 1088 ? 0.1789 0.2260 0.1985 -0.0015 0.0072  -0.0091 1086 GLY B C   
17058 O O   . GLY B 1088 ? 0.1957 0.2488 0.2164 -0.0023 0.0079  -0.0083 1086 GLY B O   
17059 N N   . PRO B 1089 ? 0.1862 0.2286 0.2036 -0.0028 0.0066  -0.0092 1087 PRO B N   
17060 C CA  . PRO B 1089 ? 0.1963 0.2399 0.2120 -0.0055 0.0066  -0.0083 1087 PRO B CA  
17061 C C   . PRO B 1089 ? 0.1792 0.2268 0.1947 -0.0043 0.0081  -0.0082 1087 PRO B C   
17062 O O   . PRO B 1089 ? 0.1965 0.2437 0.2123 -0.0013 0.0088  -0.0091 1087 PRO B O   
17063 C CB  . PRO B 1089 ? 0.2117 0.2484 0.2249 -0.0064 0.0055  -0.0086 1087 PRO B CB  
17064 C CG  . PRO B 1089 ? 0.2401 0.2733 0.2539 -0.0034 0.0055  -0.0099 1087 PRO B CG  
17065 C CD  . PRO B 1089 ? 0.2069 0.2428 0.2232 -0.0019 0.0058  -0.0101 1087 PRO B CD  
17066 N N   . VAL B 1090 ? 0.1725 0.2237 0.1872 -0.0068 0.0085  -0.0069 1088 VAL B N   
17067 C CA  . VAL B 1090 ? 0.1865 0.2411 0.2004 -0.0059 0.0100  -0.0068 1088 VAL B CA  
17068 C C   . VAL B 1090 ? 0.1830 0.2317 0.1939 -0.0051 0.0097  -0.0076 1088 VAL B C   
17069 O O   . VAL B 1090 ? 0.1812 0.2237 0.1907 -0.0060 0.0082  -0.0078 1088 VAL B O   
17070 C CB  . VAL B 1090 ? 0.1933 0.2532 0.2068 -0.0091 0.0106  -0.0051 1088 VAL B CB  
17071 C CG1 . VAL B 1090 ? 0.1885 0.2549 0.2052 -0.0100 0.0108  -0.0043 1088 VAL B CG1 
17072 C CG2 . VAL B 1090 ? 0.2120 0.2669 0.2227 -0.0127 0.0092  -0.0042 1088 VAL B CG2 
17073 N N   . GLY B 1091 ? 0.1908 0.2414 0.2007 -0.0031 0.0110  -0.0080 1089 GLY B N   
17074 C CA  . GLY B 1091 ? 0.1924 0.2378 0.1994 -0.0024 0.0106  -0.0087 1089 GLY B CA  
17075 C C   . GLY B 1091 ? 0.1848 0.2249 0.1921 0.0001  0.0097  -0.0103 1089 GLY B C   
17076 O O   . GLY B 1091 ? 0.1793 0.2143 0.1844 0.0003  0.0089  -0.0108 1089 GLY B O   
17077 N N   . GLU B 1092 ? 0.1806 0.2217 0.1906 0.0018  0.0098  -0.0108 1090 GLU B N   
17078 C CA  . GLU B 1092 ? 0.1689 0.2055 0.1795 0.0041  0.0091  -0.0121 1090 GLU B CA  
17079 C C   . GLU B 1092 ? 0.1782 0.2181 0.1909 0.0068  0.0101  -0.0127 1090 GLU B C   
17080 O O   . GLU B 1092 ? 0.2082 0.2533 0.2228 0.0065  0.0107  -0.0119 1090 GLU B O   
17081 C CB  . GLU B 1092 ? 0.2261 0.2590 0.2376 0.0027  0.0077  -0.0120 1090 GLU B CB  
17082 C CG  . GLU B 1092 ? 0.3044 0.3311 0.3148 0.0031  0.0064  -0.0127 1090 GLU B CG  
17083 C CD  . GLU B 1092 ? 0.2749 0.2987 0.2861 0.0017  0.0052  -0.0125 1090 GLU B CD  
17084 O OE1 . GLU B 1092 ? 0.2309 0.2559 0.2442 0.0021  0.0053  -0.0124 1090 GLU B OE1 
17085 O OE2 . GLU B 1092 ? 0.2907 0.3109 0.3002 0.0003  0.0042  -0.0122 1090 GLU B OE2 
17086 N N   . ARG B 1093 ? 0.1769 0.2138 0.1893 0.0094  0.0100  -0.0139 1091 ARG B N   
17087 C CA  . ARG B 1093 ? 0.1647 0.2031 0.1790 0.0121  0.0106  -0.0145 1091 ARG B CA  
17088 C C   . ARG B 1093 ? 0.1688 0.2021 0.1839 0.0125  0.0094  -0.0150 1091 ARG B C   
17089 O O   . ARG B 1093 ? 0.1790 0.2074 0.1928 0.0127  0.0086  -0.0157 1091 ARG B O   
17090 C CB  . ARG B 1093 ? 0.2053 0.2445 0.2182 0.0150  0.0116  -0.0155 1091 ARG B CB  
17091 C CG  . ARG B 1093 ? 0.3076 0.3535 0.3204 0.0153  0.0132  -0.0149 1091 ARG B CG  
17092 C CD  . ARG B 1093 ? 0.4079 0.4552 0.4200 0.0191  0.0143  -0.0160 1091 ARG B CD  
17093 N NE  . ARG B 1093 ? 0.4554 0.4971 0.4645 0.0205  0.0139  -0.0175 1091 ARG B NE  
17094 C CZ  . ARG B 1093 ? 0.5608 0.6025 0.5668 0.0204  0.0145  -0.0179 1091 ARG B CZ  
17095 N NH1 . ARG B 1093 ? 0.5589 0.6063 0.5646 0.0192  0.0157  -0.0169 1091 ARG B NH1 
17096 N NH2 . ARG B 1093 ? 0.5294 0.5655 0.5326 0.0215  0.0137  -0.0193 1091 ARG B NH2 
17097 N N   . ASN B 1094 ? 0.1448 0.1794 0.1621 0.0126  0.0093  -0.0145 1092 ASN B N   
17098 C CA  . ASN B 1094 ? 0.1572 0.1877 0.1755 0.0127  0.0083  -0.0147 1092 ASN B CA  
17099 C C   . ASN B 1094 ? 0.1703 0.2013 0.1898 0.0154  0.0087  -0.0150 1092 ASN B C   
17100 O O   . ASN B 1094 ? 0.1788 0.2139 0.1997 0.0160  0.0093  -0.0144 1092 ASN B O   
17101 C CB  . ASN B 1094 ? 0.1585 0.1895 0.1778 0.0104  0.0077  -0.0139 1092 ASN B CB  
17102 C CG  . ASN B 1094 ? 0.1655 0.1942 0.1833 0.0081  0.0070  -0.0137 1092 ASN B CG  
17103 O OD1 . ASN B 1094 ? 0.1608 0.1851 0.1779 0.0081  0.0062  -0.0142 1092 ASN B OD1 
17104 N ND2 . ASN B 1094 ? 0.1719 0.2034 0.1890 0.0061  0.0071  -0.0129 1092 ASN B ND2 
17105 N N   . LEU B 1095 ? 0.1537 0.1803 0.1725 0.0169  0.0084  -0.0159 1093 LEU B N   
17106 C CA  . LEU B 1095 ? 0.1562 0.1822 0.1753 0.0196  0.0087  -0.0163 1093 LEU B CA  
17107 C C   . LEU B 1095 ? 0.1444 0.1666 0.1645 0.0195  0.0079  -0.0161 1093 LEU B C   
17108 O O   . LEU B 1095 ? 0.1600 0.1791 0.1802 0.0179  0.0071  -0.0162 1093 LEU B O   
17109 C CB  . LEU B 1095 ? 0.1776 0.2010 0.1944 0.0214  0.0088  -0.0175 1093 LEU B CB  
17110 C CG  . LEU B 1095 ? 0.2180 0.2450 0.2333 0.0214  0.0097  -0.0177 1093 LEU B CG  
17111 C CD1 . LEU B 1095 ? 0.2770 0.3009 0.2896 0.0234  0.0098  -0.0191 1093 LEU B CD1 
17112 C CD2 . LEU B 1095 ? 0.2269 0.2605 0.2436 0.0224  0.0109  -0.0170 1093 LEU B CD2 
17113 N N   . TYR B 1096 ? 0.1471 0.1698 0.1681 0.0213  0.0081  -0.0158 1094 TYR B N   
17114 C CA  . TYR B 1096 ? 0.1565 0.1762 0.1785 0.0213  0.0076  -0.0154 1094 TYR B CA  
17115 C C   . TYR B 1096 ? 0.1467 0.1643 0.1681 0.0239  0.0076  -0.0157 1094 TYR B C   
17116 O O   . TYR B 1096 ? 0.1560 0.1767 0.1775 0.0260  0.0082  -0.0156 1094 TYR B O   
17117 C CB  . TYR B 1096 ? 0.1677 0.1906 0.1913 0.0202  0.0077  -0.0143 1094 TYR B CB  
17118 C CG  . TYR B 1096 ? 0.1562 0.1768 0.1807 0.0204  0.0073  -0.0137 1094 TYR B CG  
17119 C CD1 . TYR B 1096 ? 0.1603 0.1782 0.1852 0.0187  0.0068  -0.0135 1094 TYR B CD1 
17120 C CD2 . TYR B 1096 ? 0.1751 0.1966 0.1999 0.0223  0.0075  -0.0131 1094 TYR B CD2 
17121 C CE1 . TYR B 1096 ? 0.1675 0.1839 0.1932 0.0187  0.0067  -0.0128 1094 TYR B CE1 
17122 C CE2 . TYR B 1096 ? 0.1701 0.1896 0.1955 0.0224  0.0073  -0.0123 1094 TYR B CE2 
17123 C CZ  . TYR B 1096 ? 0.1611 0.1782 0.1869 0.0205  0.0070  -0.0122 1094 TYR B CZ  
17124 O OH  . TYR B 1096 ? 0.1712 0.1865 0.1973 0.0205  0.0069  -0.0113 1094 TYR B OH  
17125 N N   . THR B 1097 ? 0.1566 0.1689 0.1774 0.0240  0.0069  -0.0161 1095 THR B N   
17126 C CA  . THR B 1097 ? 0.1614 0.1704 0.1809 0.0264  0.0067  -0.0165 1095 THR B CA  
17127 C C   . THR B 1097 ? 0.1552 0.1600 0.1753 0.0257  0.0060  -0.0159 1095 THR B C   
17128 O O   . THR B 1097 ? 0.1695 0.1730 0.1905 0.0235  0.0056  -0.0156 1095 THR B O   
17129 C CB  . THR B 1097 ? 0.1986 0.2045 0.2158 0.0271  0.0064  -0.0180 1095 THR B CB  
17130 O OG1 . THR B 1097 ? 0.2537 0.2565 0.2708 0.0248  0.0056  -0.0183 1095 THR B OG1 
17131 C CG2 . THR B 1097 ? 0.2162 0.2264 0.2325 0.0277  0.0073  -0.0185 1095 THR B CG2 
17132 N N   . LEU B 1098 ? 0.1648 0.1675 0.1842 0.0278  0.0059  -0.0156 1096 LEU B N   
17133 C CA  . LEU B 1098 ? 0.1480 0.1464 0.1677 0.0272  0.0053  -0.0148 1096 LEU B CA  
17134 C C   . LEU B 1098 ? 0.1495 0.1419 0.1670 0.0283  0.0045  -0.0157 1096 LEU B C   
17135 O O   . LEU B 1098 ? 0.1695 0.1608 0.1851 0.0311  0.0045  -0.0164 1096 LEU B O   
17136 C CB  . LEU B 1098 ? 0.1499 0.1499 0.1703 0.0284  0.0056  -0.0135 1096 LEU B CB  
17137 C CG  . LEU B 1098 ? 0.1505 0.1559 0.1727 0.0270  0.0062  -0.0126 1096 LEU B CG  
17138 C CD1 . LEU B 1098 ? 0.1670 0.1737 0.1896 0.0284  0.0063  -0.0113 1096 LEU B CD1 
17139 C CD2 . LEU B 1098 ? 0.1728 0.1778 0.1963 0.0241  0.0060  -0.0123 1096 LEU B CD2 
17140 N N   . HIS B 1099 ? 0.1556 0.1442 0.1732 0.0262  0.0036  -0.0157 1097 HIS B N   
17141 C CA  . HIS B 1099 ? 0.1735 0.1559 0.1890 0.0265  0.0025  -0.0166 1097 HIS B CA  
17142 C C   . HIS B 1099 ? 0.1715 0.1502 0.1877 0.0253  0.0019  -0.0153 1097 HIS B C   
17143 O O   . HIS B 1099 ? 0.1753 0.1566 0.1936 0.0241  0.0024  -0.0138 1097 HIS B O   
17144 C CB  . HIS B 1099 ? 0.1925 0.1738 0.2079 0.0246  0.0018  -0.0177 1097 HIS B CB  
17145 C CG  . HIS B 1099 ? 0.2158 0.2007 0.2304 0.0253  0.0024  -0.0188 1097 HIS B CG  
17146 N ND1 . HIS B 1099 ? 0.2522 0.2349 0.2639 0.0269  0.0021  -0.0204 1097 HIS B ND1 
17147 C CD2 . HIS B 1099 ? 0.2524 0.2427 0.2685 0.0245  0.0033  -0.0184 1097 HIS B CD2 
17148 C CE1 . HIS B 1099 ? 0.2692 0.2563 0.2808 0.0270  0.0029  -0.0208 1097 HIS B CE1 
17149 N NE2 . HIS B 1099 ? 0.2553 0.2468 0.2695 0.0255  0.0036  -0.0197 1097 HIS B NE2 
17150 N N   . ALA B 1100 ? 0.1912 0.1637 0.2054 0.0255  0.0007  -0.0158 1098 ALA B N   
17151 C CA  . ALA B 1100 ? 0.1992 0.1680 0.2141 0.0236  0.0000  -0.0144 1098 ALA B CA  
17152 C C   . ALA B 1100 ? 0.1989 0.1700 0.2166 0.0203  -0.0001 -0.0138 1098 ALA B C   
17153 O O   . ALA B 1100 ? 0.2136 0.1865 0.2318 0.0194  -0.0003 -0.0149 1098 ALA B O   
17154 C CB  . ALA B 1100 ? 0.2224 0.1836 0.2344 0.0239  -0.0015 -0.0152 1098 ALA B CB  
17155 N N   . ARG B 1101 ? 0.1949 0.1660 0.2144 0.0186  0.0000  -0.0121 1099 ARG B N   
17156 C CA  . ARG B 1101 ? 0.1994 0.1723 0.2217 0.0155  -0.0001 -0.0115 1099 ARG B CA  
17157 C C   . ARG B 1101 ? 0.1953 0.1638 0.2171 0.0138  -0.0017 -0.0122 1099 ARG B C   
17158 O O   . ARG B 1101 ? 0.2134 0.1838 0.2369 0.0120  -0.0021 -0.0127 1099 ARG B O   
17159 C CB  . ARG B 1101 ? 0.2297 0.2038 0.2537 0.0143  0.0006  -0.0093 1099 ARG B CB  
17160 C CG  . ARG B 1101 ? 0.2399 0.2197 0.2653 0.0150  0.0020  -0.0087 1099 ARG B CG  
17161 C CD  . ARG B 1101 ? 0.2337 0.2178 0.2617 0.0132  0.0025  -0.0088 1099 ARG B CD  
17162 N NE  . ARG B 1101 ? 0.2428 0.2316 0.2716 0.0137  0.0037  -0.0083 1099 ARG B NE  
17163 C CZ  . ARG B 1101 ? 0.2187 0.2107 0.2495 0.0124  0.0044  -0.0077 1099 ARG B CZ  
17164 N NH1 . ARG B 1101 ? 0.1984 0.1904 0.2312 0.0104  0.0041  -0.0074 1099 ARG B NH1 
17165 N NH2 . ARG B 1101 ? 0.2511 0.2468 0.2821 0.0131  0.0054  -0.0073 1099 ARG B NH2 
17166 N N   . GLY B 1102 ? 0.1839 0.1463 0.2032 0.0142  -0.0028 -0.0123 1100 GLY B N   
17167 C CA  . GLY B 1102 ? 0.2219 0.1797 0.2407 0.0121  -0.0046 -0.0128 1100 GLY B CA  
17168 C C   . GLY B 1102 ? 0.2240 0.1765 0.2419 0.0110  -0.0054 -0.0114 1100 GLY B C   
17169 O O   . GLY B 1102 ? 0.2318 0.1805 0.2470 0.0131  -0.0054 -0.0112 1100 GLY B O   
17170 N N   . ARG B 1103 ? 0.2187 0.1710 0.2390 0.0076  -0.0060 -0.0102 1101 ARG B N   
17171 C CA  . ARG B 1103 ? 0.2205 0.1682 0.2403 0.0060  -0.0068 -0.0085 1101 ARG B CA  
17172 C C   . ARG B 1103 ? 0.2137 0.1660 0.2364 0.0047  -0.0052 -0.0061 1101 ARG B C   
17173 O O   . ARG B 1103 ? 0.2280 0.1861 0.2543 0.0031  -0.0044 -0.0057 1101 ARG B O   
17174 C CB  . ARG B 1103 ? 0.2307 0.1746 0.2508 0.0027  -0.0088 -0.0087 1101 ARG B CB  
17175 C CG  . ARG B 1103 ? 0.2520 0.1903 0.2712 0.0007  -0.0097 -0.0068 1101 ARG B CG  
17176 C CD  . ARG B 1103 ? 0.3250 0.2580 0.3435 -0.0023 -0.0122 -0.0073 1101 ARG B CD  
17177 N NE  . ARG B 1103 ? 0.4018 0.3276 0.4154 -0.0002 -0.0137 -0.0095 1101 ARG B NE  
17178 C CZ  . ARG B 1103 ? 0.4605 0.3851 0.4727 0.0000  -0.0150 -0.0118 1101 ARG B CZ  
17179 N NH1 . ARG B 1103 ? 0.5633 0.4935 0.5790 -0.0018 -0.0151 -0.0122 1101 ARG B NH1 
17180 N NH2 . ARG B 1103 ? 0.4124 0.3302 0.4197 0.0023  -0.0163 -0.0138 1101 ARG B NH2 
17181 N N   . ILE B 1104 ? 0.1998 0.1496 0.2209 0.0057  -0.0047 -0.0046 1102 ILE B N   
17182 C CA  . ILE B 1104 ? 0.1929 0.1466 0.2160 0.0049  -0.0032 -0.0024 1102 ILE B CA  
17183 C C   . ILE B 1104 ? 0.1961 0.1463 0.2197 0.0017  -0.0039 -0.0002 1102 ILE B C   
17184 O O   . ILE B 1104 ? 0.2114 0.1543 0.2319 0.0016  -0.0054 0.0000  1102 ILE B O   
17185 C CB  . ILE B 1104 ? 0.1837 0.1377 0.2048 0.0081  -0.0021 -0.0019 1102 ILE B CB  
17186 C CG1 . ILE B 1104 ? 0.2077 0.1650 0.2282 0.0111  -0.0016 -0.0040 1102 ILE B CG1 
17187 C CG2 . ILE B 1104 ? 0.1975 0.1560 0.2203 0.0073  -0.0005 0.0003  1102 ILE B CG2 
17188 C CD1 . ILE B 1104 ? 0.2154 0.1797 0.2390 0.0104  -0.0005 -0.0046 1102 ILE B CD1 
17189 N N   . LEU B 1105 ? 0.1867 0.1418 0.2138 -0.0009 -0.0029 0.0014  1103 LEU B N   
17190 C CA  . LEU B 1105 ? 0.2107 0.1637 0.2386 -0.0041 -0.0032 0.0038  1103 LEU B CA  
17191 C C   . LEU B 1105 ? 0.1907 0.1422 0.2165 -0.0030 -0.0022 0.0058  1103 LEU B C   
17192 O O   . LEU B 1105 ? 0.1920 0.1485 0.2184 -0.0013 -0.0005 0.0063  1103 LEU B O   
17193 C CB  . LEU B 1105 ? 0.2099 0.1698 0.2425 -0.0069 -0.0022 0.0048  1103 LEU B CB  
17194 C CG  . LEU B 1105 ? 0.2129 0.1728 0.2471 -0.0105 -0.0020 0.0077  1103 LEU B CG  
17195 C CD1 . LEU B 1105 ? 0.2202 0.1733 0.2534 -0.0132 -0.0043 0.0079  1103 LEU B CD1 
17196 C CD2 . LEU B 1105 ? 0.2171 0.1854 0.2562 -0.0123 -0.0005 0.0084  1103 LEU B CD2 
17197 N N   . LEU B 1106 ? 0.1986 0.1428 0.2214 -0.0037 -0.0035 0.0070  1104 LEU B N   
17198 C CA  . LEU B 1106 ? 0.2106 0.1524 0.2310 -0.0027 -0.0028 0.0092  1104 LEU B CA  
17199 C C   . LEU B 1106 ? 0.2113 0.1528 0.2331 -0.0067 -0.0026 0.0121  1104 LEU B C   
17200 O O   . LEU B 1106 ? 0.2325 0.1696 0.2544 -0.0097 -0.0042 0.0126  1104 LEU B O   
17201 C CB  . LEU B 1106 ? 0.2299 0.1630 0.2455 -0.0003 -0.0045 0.0085  1104 LEU B CB  
17202 C CG  . LEU B 1106 ? 0.2899 0.2238 0.3034 0.0045  -0.0040 0.0068  1104 LEU B CG  
17203 C CD1 . LEU B 1106 ? 0.3006 0.2412 0.3166 0.0058  -0.0031 0.0044  1104 LEU B CD1 
17204 C CD2 . LEU B 1106 ? 0.2360 0.1612 0.2450 0.0069  -0.0058 0.0057  1104 LEU B CD2 
17205 N N   . VAL B 1107 ? 0.1899 0.1361 0.2127 -0.0069 -0.0007 0.0142  1105 VAL B N   
17206 C CA  . VAL B 1107 ? 0.2181 0.1647 0.2421 -0.0106 -0.0001 0.0173  1105 VAL B CA  
17207 C C   . VAL B 1107 ? 0.2118 0.1550 0.2321 -0.0092 0.0004  0.0194  1105 VAL B C   
17208 O O   . VAL B 1107 ? 0.2275 0.1759 0.2483 -0.0083 0.0023  0.0206  1105 VAL B O   
17209 C CB  . VAL B 1107 ? 0.2034 0.1594 0.2320 -0.0123 0.0019  0.0179  1105 VAL B CB  
17210 C CG1 . VAL B 1107 ? 0.2290 0.1856 0.2593 -0.0166 0.0024  0.0211  1105 VAL B CG1 
17211 C CG2 . VAL B 1107 ? 0.2102 0.1699 0.2421 -0.0126 0.0014  0.0154  1105 VAL B CG2 
17212 N N   . PRO B 1108 ? 0.2043 0.1386 0.2206 -0.0087 -0.0014 0.0199  1106 PRO B N   
17213 C CA  . PRO B 1108 ? 0.2410 0.1715 0.2535 -0.0071 -0.0012 0.0220  1106 PRO B CA  
17214 C C   . PRO B 1108 ? 0.2503 0.1800 0.2630 -0.0111 -0.0007 0.0257  1106 PRO B C   
17215 O O   . PRO B 1108 ? 0.2800 0.2102 0.2952 -0.0152 -0.0010 0.0266  1106 PRO B O   
17216 C CB  . PRO B 1108 ? 0.2495 0.1703 0.2578 -0.0051 -0.0036 0.0209  1106 PRO B CB  
17217 C CG  . PRO B 1108 ? 0.2561 0.1738 0.2658 -0.0083 -0.0052 0.0199  1106 PRO B CG  
17218 C CD  . PRO B 1108 ? 0.2480 0.1750 0.2626 -0.0090 -0.0039 0.0182  1106 PRO B CD  
17219 N N   . ALA B 1109 ? 0.2470 0.1754 0.2568 -0.0098 0.0000  0.0279  1107 ALA B N   
17220 C CA  . ALA B 1109 ? 0.2671 0.1929 0.2756 -0.0132 0.0003  0.0317  1107 ALA B CA  
17221 C C   . ALA B 1109 ? 0.3068 0.2220 0.3099 -0.0122 -0.0017 0.0331  1107 ALA B C   
17222 O O   . ALA B 1109 ? 0.3280 0.2375 0.3297 -0.0157 -0.0027 0.0356  1107 ALA B O   
17223 C CB  . ALA B 1109 ? 0.2719 0.2050 0.2812 -0.0128 0.0028  0.0336  1107 ALA B CB  
17224 N N   . THR B 1110 ? 0.2861 0.1984 0.2862 -0.0074 -0.0024 0.0315  1108 THR B N   
17225 C CA  . THR B 1110 ? 0.2951 0.1977 0.2899 -0.0055 -0.0042 0.0328  1108 THR B CA  
17226 C C   . THR B 1110 ? 0.2888 0.1860 0.2816 -0.0018 -0.0061 0.0295  1108 THR B C   
17227 O O   . THR B 1110 ? 0.2770 0.1792 0.2723 0.0001  -0.0056 0.0264  1108 THR B O   
17228 C CB  . THR B 1110 ? 0.3137 0.2181 0.3060 -0.0025 -0.0032 0.0346  1108 THR B CB  
17229 O OG1 . THR B 1110 ? 0.3021 0.2126 0.2957 0.0018  -0.0024 0.0318  1108 THR B OG1 
17230 C CG2 . THR B 1110 ? 0.3384 0.2487 0.3323 -0.0058 -0.0010 0.0377  1108 THR B CG2 
17231 N N   . GLU B 1111 ? 0.3030 0.1897 0.2909 -0.0006 -0.0081 0.0303  1109 GLU B N   
17232 C CA  . GLU B 1111 ? 0.3111 0.1921 0.2966 0.0033  -0.0099 0.0273  1109 GLU B CA  
17233 C C   . GLU B 1111 ? 0.3153 0.2021 0.3012 0.0087  -0.0089 0.0252  1109 GLU B C   
17234 O O   . GLU B 1111 ? 0.2961 0.1852 0.2833 0.0109  -0.0090 0.0219  1109 GLU B O   
17235 C CB  . GLU B 1111 ? 0.3164 0.1849 0.2961 0.0040  -0.0122 0.0287  1109 GLU B CB  
17236 C CG  . GLU B 1111 ? 0.3542 0.2166 0.3305 0.0091  -0.0139 0.0258  1109 GLU B CG  
17237 C CD  . GLU B 1111 ? 0.4014 0.2506 0.3717 0.0097  -0.0164 0.0271  1109 GLU B CD  
17238 O OE1 . GLU B 1111 ? 0.4012 0.2432 0.3702 0.0061  -0.0180 0.0271  1109 GLU B OE1 
17239 O OE2 . GLU B 1111 ? 0.4452 0.2912 0.4121 0.0136  -0.0167 0.0282  1109 GLU B OE2 
17240 N N   . SER B 1112 ? 0.3056 0.1949 0.2903 0.0106  -0.0080 0.0271  1110 SER B N   
17241 C CA  . SER B 1112 ? 0.2883 0.1838 0.2737 0.0154  -0.0071 0.0254  1110 SER B CA  
17242 C C   . SER B 1112 ? 0.2890 0.1947 0.2794 0.0146  -0.0053 0.0233  1110 SER B C   
17243 O O   . SER B 1112 ? 0.2896 0.1989 0.2811 0.0178  -0.0052 0.0205  1110 SER B O   
17244 C CB  . SER B 1112 ? 0.3417 0.2387 0.3252 0.0170  -0.0065 0.0281  1110 SER B CB  
17245 O OG  . SER B 1112 ? 0.3456 0.2485 0.3299 0.0215  -0.0059 0.0264  1110 SER B OG  
17246 N N   . GLY B 1113 ? 0.2767 0.1875 0.2702 0.0103  -0.0039 0.0247  1111 GLY B N   
17247 C CA  . GLY B 1113 ? 0.2537 0.1736 0.2517 0.0096  -0.0024 0.0227  1111 GLY B CA  
17248 C C   . GLY B 1113 ? 0.2556 0.1744 0.2550 0.0097  -0.0033 0.0196  1111 GLY B C   
17249 O O   . GLY B 1113 ? 0.2430 0.1673 0.2444 0.0118  -0.0026 0.0171  1111 GLY B O   
17250 N N   . LEU B 1114 ? 0.2577 0.1691 0.2558 0.0074  -0.0049 0.0197  1112 LEU B N   
17251 C CA  . LEU B 1114 ? 0.2480 0.1573 0.2467 0.0076  -0.0060 0.0168  1112 LEU B CA  
17252 C C   . LEU B 1114 ? 0.2561 0.1635 0.2524 0.0128  -0.0067 0.0142  1112 LEU B C   
17253 O O   . LEU B 1114 ? 0.2355 0.1466 0.2335 0.0141  -0.0065 0.0114  1112 LEU B O   
17254 C CB  . LEU B 1114 ? 0.2711 0.1716 0.2679 0.0043  -0.0080 0.0175  1112 LEU B CB  
17255 C CG  . LEU B 1114 ? 0.2663 0.1625 0.2623 0.0047  -0.0097 0.0145  1112 LEU B CG  
17256 C CD1 . LEU B 1114 ? 0.2769 0.1814 0.2775 0.0035  -0.0086 0.0124  1112 LEU B CD1 
17257 C CD2 . LEU B 1114 ? 0.3308 0.2176 0.3245 0.0012  -0.0118 0.0155  1112 LEU B CD2 
17258 N N   . TYR B 1115 ? 0.2629 0.1648 0.2553 0.0158  -0.0075 0.0152  1113 TYR B N   
17259 C CA  . TYR B 1115 ? 0.2645 0.1652 0.2548 0.0211  -0.0081 0.0129  1113 TYR B CA  
17260 C C   . TYR B 1115 ? 0.2607 0.1717 0.2541 0.0234  -0.0063 0.0117  1113 TYR B C   
17261 O O   . TYR B 1115 ? 0.2565 0.1698 0.2505 0.0260  -0.0062 0.0089  1113 TYR B O   
17262 C CB  . TYR B 1115 ? 0.2841 0.1776 0.2699 0.0241  -0.0092 0.0145  1113 TYR B CB  
17263 C CG  . TYR B 1115 ? 0.2730 0.1548 0.2547 0.0227  -0.0114 0.0153  1113 TYR B CG  
17264 C CD1 . TYR B 1115 ? 0.2907 0.1685 0.2726 0.0196  -0.0124 0.0140  1113 TYR B CD1 
17265 C CD2 . TYR B 1115 ? 0.3520 0.2264 0.3294 0.0245  -0.0125 0.0174  1113 TYR B CD2 
17266 C CE1 . TYR B 1115 ? 0.3290 0.1955 0.3069 0.0180  -0.0146 0.0147  1113 TYR B CE1 
17267 C CE2 . TYR B 1115 ? 0.3640 0.2269 0.3373 0.0232  -0.0146 0.0182  1113 TYR B CE2 
17268 C CZ  . TYR B 1115 ? 0.3886 0.2475 0.3621 0.0199  -0.0157 0.0168  1113 TYR B CZ  
17269 O OH  . TYR B 1115 ? 0.4157 0.2628 0.3849 0.0183  -0.0180 0.0176  1113 TYR B OH  
17270 N N   . HIS B 1116 ? 0.2355 0.1526 0.2308 0.0222  -0.0048 0.0136  1114 HIS B N   
17271 C CA  . HIS B 1116 ? 0.2393 0.1658 0.2374 0.0239  -0.0032 0.0125  1114 HIS B CA  
17272 C C   . HIS B 1116 ? 0.2468 0.1787 0.2486 0.0218  -0.0024 0.0105  1114 HIS B C   
17273 O O   . HIS B 1116 ? 0.2480 0.1852 0.2513 0.0239  -0.0018 0.0083  1114 HIS B O   
17274 C CB  . HIS B 1116 ? 0.2443 0.1756 0.2431 0.0229  -0.0020 0.0151  1114 HIS B CB  
17275 C CG  . HIS B 1116 ? 0.2875 0.2164 0.2832 0.0261  -0.0026 0.0167  1114 HIS B CG  
17276 N ND1 . HIS B 1116 ? 0.3071 0.2285 0.2994 0.0256  -0.0036 0.0192  1114 HIS B ND1 
17277 C CD2 . HIS B 1116 ? 0.2764 0.2095 0.2718 0.0299  -0.0023 0.0162  1114 HIS B CD2 
17278 C CE1 . HIS B 1116 ? 0.3311 0.2521 0.3211 0.0291  -0.0040 0.0202  1114 HIS B CE1 
17279 N NE2 . HIS B 1116 ? 0.3212 0.2496 0.3132 0.0318  -0.0033 0.0184  1114 HIS B NE2 
17280 N N   . GLN B 1117 ? 0.2289 0.1599 0.2323 0.0176  -0.0024 0.0111  1115 GLN B N   
17281 C CA  . GLN B 1117 ? 0.2113 0.1470 0.2181 0.0157  -0.0019 0.0092  1115 GLN B CA  
17282 C C   . GLN B 1117 ? 0.2058 0.1382 0.2114 0.0176  -0.0031 0.0064  1115 GLN B C   
17283 O O   . GLN B 1117 ? 0.2138 0.1513 0.2214 0.0185  -0.0025 0.0042  1115 GLN B O   
17284 C CB  . GLN B 1117 ? 0.2218 0.1568 0.2304 0.0110  -0.0019 0.0106  1115 GLN B CB  
17285 C CG  . GLN B 1117 ? 0.2135 0.1535 0.2240 0.0089  -0.0003 0.0131  1115 GLN B CG  
17286 C CD  . GLN B 1117 ? 0.2240 0.1637 0.2365 0.0042  -0.0003 0.0145  1115 GLN B CD  
17287 O OE1 . GLN B 1117 ? 0.2383 0.1729 0.2504 0.0024  -0.0018 0.0141  1115 GLN B OE1 
17288 N NE2 . GLN B 1117 ? 0.2326 0.1780 0.2473 0.0023  0.0014  0.0163  1115 GLN B NE2 
17289 N N   . LEU B 1118 ? 0.2182 0.1419 0.2204 0.0181  -0.0048 0.0063  1116 LEU B N   
17290 C CA  . LEU B 1118 ? 0.2245 0.1444 0.2249 0.0202  -0.0059 0.0035  1116 LEU B CA  
17291 C C   . LEU B 1118 ? 0.2322 0.1558 0.2320 0.0250  -0.0052 0.0019  1116 LEU B C   
17292 O O   . LEU B 1118 ? 0.2440 0.1701 0.2445 0.0262  -0.0051 -0.0006 1116 LEU B O   
17293 C CB  . LEU B 1118 ? 0.2528 0.1619 0.2489 0.0205  -0.0080 0.0039  1116 LEU B CB  
17294 C CG  . LEU B 1118 ? 0.3196 0.2239 0.3159 0.0157  -0.0092 0.0046  1116 LEU B CG  
17295 C CD1 . LEU B 1118 ? 0.3161 0.2094 0.3078 0.0160  -0.0112 0.0056  1116 LEU B CD1 
17296 C CD2 . LEU B 1118 ? 0.2953 0.2009 0.2931 0.0147  -0.0097 0.0019  1116 LEU B CD2 
17297 N N   . ALA B 1119 ? 0.2478 0.1720 0.2464 0.0275  -0.0049 0.0033  1117 ALA B N   
17298 C CA  . ALA B 1119 ? 0.2377 0.1662 0.2362 0.0319  -0.0043 0.0020  1117 ALA B CA  
17299 C C   . ALA B 1119 ? 0.2446 0.1825 0.2468 0.0312  -0.0027 0.0008  1117 ALA B C   
17300 O O   . ALA B 1119 ? 0.2177 0.1584 0.2203 0.0333  -0.0025 -0.0015 1117 ALA B O   
17301 C CB  . ALA B 1119 ? 0.2450 0.1737 0.2421 0.0343  -0.0041 0.0041  1117 ALA B CB  
17302 N N   . ALA B 1120 ? 0.2026 0.1453 0.2076 0.0281  -0.0017 0.0023  1118 ALA B N   
17303 C CA  . ALA B 1120 ? 0.1891 0.1401 0.1973 0.0274  -0.0004 0.0013  1118 ALA B CA  
17304 C C   . ALA B 1120 ? 0.1985 0.1497 0.2079 0.0261  -0.0006 -0.0009 1118 ALA B C   
17305 O O   . ALA B 1120 ? 0.2110 0.1668 0.2215 0.0275  -0.0001 -0.0027 1118 ALA B O   
17306 C CB  . ALA B 1120 ? 0.2145 0.1696 0.2250 0.0243  0.0006  0.0032  1118 ALA B CB  
17307 N N   . ALA B 1121 ? 0.1850 0.1311 0.1941 0.0234  -0.0016 -0.0008 1119 ALA B N   
17308 C CA  . ALA B 1121 ? 0.1839 0.1303 0.1940 0.0219  -0.0020 -0.0028 1119 ALA B CA  
17309 C C   . ALA B 1121 ? 0.1794 0.1224 0.1868 0.0250  -0.0028 -0.0051 1119 ALA B C   
17310 O O   . ALA B 1121 ? 0.1897 0.1360 0.1980 0.0254  -0.0025 -0.0070 1119 ALA B O   
17311 C CB  . ALA B 1121 ? 0.2231 0.1653 0.2337 0.0181  -0.0029 -0.0019 1119 ALA B CB  
17312 N N   . LEU B 1122 ? 0.1988 0.1351 0.2028 0.0273  -0.0038 -0.0050 1120 LEU B N   
17313 C CA  . LEU B 1122 ? 0.2011 0.1340 0.2022 0.0305  -0.0045 -0.0074 1120 LEU B CA  
17314 C C   . LEU B 1122 ? 0.2011 0.1406 0.2029 0.0341  -0.0032 -0.0084 1120 LEU B C   
17315 O O   . LEU B 1122 ? 0.2088 0.1497 0.2101 0.0356  -0.0030 -0.0106 1120 LEU B O   
17316 C CB  . LEU B 1122 ? 0.2251 0.1488 0.2219 0.0325  -0.0060 -0.0070 1120 LEU B CB  
17317 C CG  . LEU B 1122 ? 0.2505 0.1666 0.2460 0.0289  -0.0076 -0.0062 1120 LEU B CG  
17318 C CD1 . LEU B 1122 ? 0.2622 0.1693 0.2534 0.0310  -0.0089 -0.0054 1120 LEU B CD1 
17319 C CD2 . LEU B 1122 ? 0.2656 0.1794 0.2607 0.0273  -0.0085 -0.0084 1120 LEU B CD2 
17320 N N   . ALA B 1123 ? 0.1960 0.1398 0.1990 0.0352  -0.0023 -0.0067 1121 ALA B N   
17321 C CA  . ALA B 1123 ? 0.1906 0.1411 0.1946 0.0383  -0.0012 -0.0075 1121 ALA B CA  
17322 C C   . ALA B 1123 ? 0.2018 0.1592 0.2086 0.0367  -0.0002 -0.0087 1121 ALA B C   
17323 O O   . ALA B 1123 ? 0.1915 0.1537 0.1987 0.0390  0.0006  -0.0099 1121 ALA B O   
17324 C CB  . ALA B 1123 ? 0.1985 0.1527 0.2036 0.0390  -0.0006 -0.0053 1121 ALA B CB  
17325 N N   . THR B 1124 ? 0.1758 0.1340 0.1845 0.0328  -0.0001 -0.0083 1122 THR B N   
17326 C CA  . THR B 1124 ? 0.1712 0.1352 0.1825 0.0311  0.0007  -0.0093 1122 THR B CA  
17327 C C   . THR B 1124 ? 0.1619 0.1225 0.1722 0.0301  -0.0001 -0.0112 1122 THR B C   
17328 O O   . THR B 1124 ? 0.2048 0.1690 0.2170 0.0280  0.0002  -0.0118 1122 THR B O   
17329 C CB  . THR B 1124 ? 0.1904 0.1583 0.2045 0.0281  0.0014  -0.0077 1122 THR B CB  
17330 O OG1 . THR B 1124 ? 0.1849 0.1480 0.1987 0.0258  0.0007  -0.0063 1122 THR B OG1 
17331 C CG2 . THR B 1124 ? 0.1758 0.1487 0.1908 0.0295  0.0023  -0.0065 1122 THR B CG2 
17332 N N   . GLY B 1125 ? 0.1764 0.1301 0.1835 0.0315  -0.0013 -0.0120 1123 GLY B N   
17333 C CA  . GLY B 1125 ? 0.1881 0.1385 0.1936 0.0311  -0.0022 -0.0141 1123 GLY B CA  
17334 C C   . GLY B 1125 ? 0.2043 0.1510 0.2104 0.0273  -0.0033 -0.0138 1123 GLY B C   
17335 O O   . GLY B 1125 ? 0.2013 0.1456 0.2062 0.0266  -0.0042 -0.0155 1123 GLY B O   
17336 N N   . ASN B 1126 ? 0.1924 0.1386 0.2002 0.0248  -0.0034 -0.0117 1124 ASN B N   
17337 C CA  . ASN B 1126 ? 0.1809 0.1255 0.1903 0.0208  -0.0043 -0.0111 1124 ASN B CA  
17338 C C   . ASN B 1126 ? 0.2088 0.1446 0.2154 0.0200  -0.0061 -0.0110 1124 ASN B C   
17339 O O   . ASN B 1126 ? 0.2158 0.1465 0.2194 0.0221  -0.0066 -0.0107 1124 ASN B O   
17340 C CB  . ASN B 1126 ? 0.1857 0.1346 0.1984 0.0184  -0.0033 -0.0088 1124 ASN B CB  
17341 C CG  . ASN B 1126 ? 0.1595 0.1164 0.1748 0.0190  -0.0017 -0.0089 1124 ASN B CG  
17342 O OD1 . ASN B 1126 ? 0.1955 0.1557 0.2123 0.0180  -0.0016 -0.0101 1124 ASN B OD1 
17343 N ND2 . ASN B 1126 ? 0.1888 0.1487 0.2043 0.0206  -0.0006 -0.0078 1124 ASN B ND2 
17344 N N   . SER B 1127 ? 0.2140 0.1480 0.2215 0.0166  -0.0073 -0.0113 1125 SER B N   
17345 C CA  . SER B 1127 ? 0.2165 0.1431 0.2224 0.0144  -0.0091 -0.0105 1125 SER B CA  
17346 C C   . SER B 1127 ? 0.2193 0.1487 0.2286 0.0111  -0.0084 -0.0077 1125 SER B C   
17347 O O   . SER B 1127 ? 0.2172 0.1540 0.2298 0.0107  -0.0068 -0.0069 1125 SER B O   
17348 C CB  . SER B 1127 ? 0.2488 0.1721 0.2539 0.0124  -0.0108 -0.0122 1125 SER B CB  
17349 O OG  . SER B 1127 ? 0.2819 0.2117 0.2910 0.0099  -0.0104 -0.0121 1125 SER B OG  
17350 N N   . VAL B 1128 ? 0.2370 0.1604 0.2452 0.0087  -0.0098 -0.0063 1126 VAL B N   
17351 C CA  . VAL B 1128 ? 0.2215 0.1473 0.2326 0.0056  -0.0091 -0.0035 1126 VAL B CA  
17352 C C   . VAL B 1128 ? 0.2283 0.1503 0.2402 0.0012  -0.0108 -0.0027 1126 VAL B C   
17353 O O   . VAL B 1128 ? 0.2586 0.1732 0.2674 0.0009  -0.0129 -0.0039 1126 VAL B O   
17354 C CB  . VAL B 1128 ? 0.2327 0.1560 0.2419 0.0071  -0.0085 -0.0014 1126 VAL B CB  
17355 C CG1 . VAL B 1128 ? 0.2316 0.1597 0.2406 0.0111  -0.0068 -0.0020 1126 VAL B CG1 
17356 C CG2 . VAL B 1128 ? 0.2594 0.1723 0.2639 0.0078  -0.0105 -0.0016 1126 VAL B CG2 
17357 N N   . ALA B 1129 ? 0.2243 0.1515 0.2403 -0.0021 -0.0100 -0.0007 1127 ALA B N   
17358 C CA  . ALA B 1129 ? 0.2422 0.1666 0.2594 -0.0066 -0.0113 0.0010  1127 ALA B CA  
17359 C C   . ALA B 1129 ? 0.2074 0.1326 0.2253 -0.0077 -0.0100 0.0041  1127 ALA B C   
17360 O O   . ALA B 1129 ? 0.2151 0.1478 0.2359 -0.0073 -0.0078 0.0052  1127 ALA B O   
17361 C CB  . ALA B 1129 ? 0.2611 0.1918 0.2830 -0.0095 -0.0113 0.0007  1127 ALA B CB  
17362 N N   . ILE B 1130 ? 0.2226 0.1399 0.2374 -0.0090 -0.0113 0.0056  1128 ILE B N   
17363 C CA  . ILE B 1130 ? 0.2237 0.1407 0.2383 -0.0100 -0.0103 0.0088  1128 ILE B CA  
17364 C C   . ILE B 1130 ? 0.2299 0.1485 0.2477 -0.0154 -0.0105 0.0111  1128 ILE B C   
17365 O O   . ILE B 1130 ? 0.2383 0.1521 0.2558 -0.0184 -0.0126 0.0109  1128 ILE B O   
17366 C CB  . ILE B 1130 ? 0.2332 0.1405 0.2422 -0.0081 -0.0115 0.0093  1128 ILE B CB  
17367 C CG1 . ILE B 1130 ? 0.2401 0.1459 0.2461 -0.0026 -0.0115 0.0067  1128 ILE B CG1 
17368 C CG2 . ILE B 1130 ? 0.2414 0.1493 0.2502 -0.0086 -0.0102 0.0126  1128 ILE B CG2 
17369 C CD1 . ILE B 1130 ? 0.2542 0.1494 0.2546 -0.0005 -0.0132 0.0065  1128 ILE B CD1 
17370 N N   . ASP B 1131 ? 0.2212 0.1464 0.2420 -0.0166 -0.0084 0.0135  1129 ASP B N   
17371 C CA  . ASP B 1131 ? 0.2242 0.1522 0.2484 -0.0215 -0.0082 0.0161  1129 ASP B CA  
17372 C C   . ASP B 1131 ? 0.2449 0.1635 0.2659 -0.0245 -0.0101 0.0180  1129 ASP B C   
17373 O O   . ASP B 1131 ? 0.2431 0.1570 0.2606 -0.0235 -0.0099 0.0198  1129 ASP B O   
17374 C CB  . ASP B 1131 ? 0.2207 0.1563 0.2473 -0.0215 -0.0054 0.0183  1129 ASP B CB  
17375 C CG  . ASP B 1131 ? 0.2296 0.1688 0.2597 -0.0264 -0.0048 0.0212  1129 ASP B CG  
17376 O OD1 . ASP B 1131 ? 0.2511 0.1905 0.2838 -0.0296 -0.0062 0.0209  1129 ASP B OD1 
17377 O OD2 . ASP B 1131 ? 0.2518 0.1936 0.2820 -0.0269 -0.0029 0.0238  1129 ASP B OD2 
17378 N N   . ALA B 1132 ? 0.2575 0.1734 0.2796 -0.0283 -0.0122 0.0178  1130 ALA B N   
17379 C CA  . ALA B 1132 ? 0.2449 0.1513 0.2639 -0.0315 -0.0144 0.0196  1130 ALA B CA  
17380 C C   . ALA B 1132 ? 0.2664 0.1749 0.2867 -0.0349 -0.0130 0.0237  1130 ALA B C   
17381 O O   . ALA B 1132 ? 0.2931 0.1933 0.3096 -0.0363 -0.0142 0.0258  1130 ALA B O   
17382 C CB  . ALA B 1132 ? 0.2576 0.1616 0.2779 -0.0353 -0.0170 0.0185  1130 ALA B CB  
17383 N N   . ALA B 1133 ? 0.2586 0.1778 0.2840 -0.0360 -0.0105 0.0250  1131 ALA B N   
17384 C CA  . ALA B 1133 ? 0.3069 0.2287 0.3336 -0.0391 -0.0089 0.0290  1131 ALA B CA  
17385 C C   . ALA B 1133 ? 0.3130 0.2314 0.3353 -0.0361 -0.0077 0.0305  1131 ALA B C   
17386 O O   . ALA B 1133 ? 0.3196 0.2382 0.3416 -0.0386 -0.0067 0.0340  1131 ALA B O   
17387 C CB  . ALA B 1133 ? 0.2824 0.2168 0.3154 -0.0406 -0.0064 0.0298  1131 ALA B CB  
17388 N N   . SER B 1134 ? 0.2672 0.1828 0.2861 -0.0309 -0.0078 0.0280  1132 SER B N   
17389 C CA  . SER B 1134 ? 0.2939 0.2056 0.3085 -0.0279 -0.0071 0.0294  1132 SER B CA  
17390 C C   . SER B 1134 ? 0.2561 0.1563 0.2658 -0.0297 -0.0093 0.0314  1132 SER B C   
17391 O O   . SER B 1134 ? 0.3025 0.1997 0.3089 -0.0286 -0.0087 0.0337  1132 SER B O   
17392 C CB  . SER B 1134 ? 0.2745 0.1858 0.2868 -0.0220 -0.0071 0.0263  1132 SER B CB  
17393 O OG  . SER B 1134 ? 0.2864 0.1896 0.2958 -0.0207 -0.0097 0.0238  1132 SER B OG  
17394 N N   . GLY B 1135 ? 0.2914 0.1846 0.3000 -0.0322 -0.0120 0.0305  1133 GLY B N   
17395 C CA  . GLY B 1135 ? 0.2873 0.1685 0.2908 -0.0338 -0.0144 0.0321  1133 GLY B CA  
17396 C C   . GLY B 1135 ? 0.3286 0.2011 0.3260 -0.0286 -0.0155 0.0307  1133 GLY B C   
17397 O O   . GLY B 1135 ? 0.3698 0.2324 0.3624 -0.0291 -0.0171 0.0325  1133 GLY B O   
17398 N N   . LEU B 1136 ? 0.3111 0.1869 0.3086 -0.0234 -0.0148 0.0274  1134 LEU B N   
17399 C CA  . LEU B 1136 ? 0.3018 0.1716 0.2943 -0.0178 -0.0154 0.0261  1134 LEU B CA  
17400 C C   . LEU B 1136 ? 0.3441 0.2055 0.3331 -0.0157 -0.0180 0.0228  1134 LEU B C   
17401 O O   . LEU B 1136 ? 0.3438 0.2023 0.3296 -0.0103 -0.0182 0.0208  1134 LEU B O   
17402 C CB  . LEU B 1136 ? 0.3011 0.1802 0.2957 -0.0134 -0.0129 0.0249  1134 LEU B CB  
17403 C CG  . LEU B 1136 ? 0.3108 0.1973 0.3075 -0.0144 -0.0104 0.0280  1134 LEU B CG  
17404 C CD1 . LEU B 1136 ? 0.3107 0.2064 0.3097 -0.0104 -0.0083 0.0263  1134 LEU B CD1 
17405 C CD2 . LEU B 1136 ? 0.3462 0.2252 0.3382 -0.0141 -0.0110 0.0310  1134 LEU B CD2 
17406 N N   . GLN B 1137 ? 0.3258 0.1836 0.3154 -0.0197 -0.0199 0.0221  1135 GLN B N   
17407 C CA  . GLN B 1137 ? 0.3349 0.1851 0.3212 -0.0178 -0.0224 0.0187  1135 GLN B CA  
17408 C C   . GLN B 1137 ? 0.4113 0.2494 0.3905 -0.0141 -0.0241 0.0184  1135 GLN B C   
17409 O O   . GLN B 1137 ? 0.4135 0.2483 0.3898 -0.0094 -0.0248 0.0151  1135 GLN B O   
17410 C CB  . GLN B 1137 ? 0.4008 0.2479 0.3883 -0.0235 -0.0245 0.0186  1135 GLN B CB  
17411 C CG  . GLN B 1137 ? 0.3664 0.2248 0.3606 -0.0261 -0.0232 0.0178  1135 GLN B CG  
17412 C CD  . GLN B 1137 ? 0.3475 0.2146 0.3469 -0.0303 -0.0212 0.0214  1135 GLN B CD  
17413 O OE1 . GLN B 1137 ? 0.3440 0.2101 0.3422 -0.0308 -0.0202 0.0244  1135 GLN B OE1 
17414 N NE2 . GLN B 1137 ? 0.3670 0.2428 0.3721 -0.0333 -0.0206 0.0209  1135 GLN B NE2 
17415 N N   . ALA B 1138 ? 0.3737 0.2054 0.3500 -0.0159 -0.0247 0.0218  1136 ALA B N   
17416 C CA  . ALA B 1138 ? 0.4082 0.2279 0.3776 -0.0124 -0.0266 0.0217  1136 ALA B CA  
17417 C C   . ALA B 1138 ? 0.4443 0.2669 0.4123 -0.0055 -0.0250 0.0205  1136 ALA B C   
17418 O O   . ALA B 1138 ? 0.4528 0.2664 0.4153 -0.0012 -0.0265 0.0195  1136 ALA B O   
17419 C CB  . ALA B 1138 ? 0.4129 0.2253 0.3796 -0.0162 -0.0275 0.0260  1136 ALA B CB  
17420 N N   . SER B 1139 ? 0.3938 0.2288 0.3666 -0.0043 -0.0222 0.0207  1137 SER B N   
17421 C CA  . SER B 1139 ? 0.3772 0.2162 0.3494 0.0019  -0.0207 0.0197  1137 SER B CA  
17422 C C   . SER B 1139 ? 0.4114 0.2502 0.3825 0.0066  -0.0212 0.0154  1137 SER B C   
17423 O O   . SER B 1139 ? 0.3945 0.2340 0.3638 0.0122  -0.0206 0.0143  1137 SER B O   
17424 C CB  . SER B 1139 ? 0.3829 0.2349 0.3604 0.0013  -0.0177 0.0210  1137 SER B CB  
17425 O OG  . SER B 1139 ? 0.4094 0.2616 0.3870 -0.0019 -0.0171 0.0250  1137 SER B OG  
17426 N N   . LEU B 1140 ? 0.4092 0.2476 0.3814 0.0045  -0.0221 0.0130  1138 LEU B N   
17427 C CA  . LEU B 1140 ? 0.4133 0.2515 0.3844 0.0086  -0.0225 0.0089  1138 LEU B CA  
17428 C C   . LEU B 1140 ? 0.4432 0.2684 0.4084 0.0091  -0.0255 0.0071  1138 LEU B C   
17429 O O   . LEU B 1140 ? 0.4954 0.3196 0.4598 0.0104  -0.0263 0.0038  1138 LEU B O   
17430 C CB  . LEU B 1140 ? 0.3868 0.2349 0.3632 0.0066  -0.0213 0.0071  1138 LEU B CB  
17431 C CG  . LEU B 1140 ? 0.3973 0.2582 0.3790 0.0072  -0.0184 0.0081  1138 LEU B CG  
17432 C CD1 . LEU B 1140 ? 0.3640 0.2335 0.3501 0.0061  -0.0174 0.0059  1138 LEU B CD1 
17433 C CD2 . LEU B 1140 ? 0.4221 0.2847 0.4020 0.0130  -0.0172 0.0078  1138 LEU B CD2 
17434 N N   . LYS B 1141 ? 0.4961 0.3109 0.4570 0.0082  -0.0273 0.0093  1139 LYS B N   
17435 C CA  . LYS B 1141 ? 0.5324 0.3336 0.4869 0.0090  -0.0303 0.0076  1139 LYS B CA  
17436 C C   . LYS B 1141 ? 0.5534 0.3521 0.5042 0.0164  -0.0303 0.0044  1139 LYS B C   
17437 O O   . LYS B 1141 ? 0.5381 0.3410 0.4891 0.0210  -0.0287 0.0050  1139 LYS B O   
17438 C CB  . LYS B 1141 ? 0.5367 0.3273 0.4871 0.0066  -0.0320 0.0110  1139 LYS B CB  
17439 N N   . ASN B 1142 ? 0.5630 0.3552 0.5103 0.0177  -0.0320 0.0010  1140 ASN B N   
17440 C CA  . ASN B 1142 ? 0.5334 0.3222 0.4765 0.0247  -0.0322 -0.0023 1140 ASN B CA  
17441 C C   . ASN B 1142 ? 0.5297 0.3316 0.4772 0.0286  -0.0293 -0.0039 1140 ASN B C   
17442 O O   . ASN B 1142 ? 0.4900 0.2922 0.4353 0.0349  -0.0286 -0.0056 1140 ASN B O   
17443 C CB  . ASN B 1142 ? 0.5901 0.3689 0.5274 0.0289  -0.0334 -0.0012 1140 ASN B CB  
17444 N N   . LEU B 1143 ? 0.5033 0.3162 0.4570 0.0250  -0.0276 -0.0035 1141 LEU B N   
17445 C CA  . LEU B 1143 ? 0.4507 0.2755 0.4084 0.0281  -0.0251 -0.0052 1141 LEU B CA  
17446 C C   . LEU B 1143 ? 0.4602 0.2827 0.4149 0.0320  -0.0256 -0.0093 1141 LEU B C   
17447 O O   . LEU B 1143 ? 0.5313 0.3468 0.4832 0.0298  -0.0276 -0.0110 1141 LEU B O   
17448 C CB  . LEU B 1143 ? 0.4257 0.2609 0.3899 0.0230  -0.0237 -0.0042 1141 LEU B CB  
17449 C CG  . LEU B 1143 ? 0.4254 0.2739 0.3947 0.0248  -0.0208 -0.0045 1141 LEU B CG  
17450 C CD1 . LEU B 1143 ? 0.3989 0.2513 0.3693 0.0269  -0.0193 -0.0020 1141 LEU B CD1 
17451 C CD2 . LEU B 1143 ? 0.3712 0.2273 0.3459 0.0195  -0.0201 -0.0039 1141 LEU B CD2 
17452 N N   . PRO B 1144 ? 0.4620 0.2901 0.4168 0.0376  -0.0239 -0.0110 1142 PRO B N   
17453 C CA  . PRO B 1144 ? 0.5073 0.3347 0.4596 0.0412  -0.0240 -0.0149 1142 PRO B CA  
17454 C C   . PRO B 1144 ? 0.4724 0.3050 0.4278 0.0372  -0.0238 -0.0163 1142 PRO B C   
17455 O O   . PRO B 1144 ? 0.4001 0.2417 0.3612 0.0335  -0.0225 -0.0147 1142 PRO B O   
17456 C CB  . PRO B 1144 ? 0.4885 0.3246 0.4426 0.0469  -0.0216 -0.0155 1142 PRO B CB  
17457 C CG  . PRO B 1144 ? 0.4896 0.3267 0.4449 0.0474  -0.0211 -0.0122 1142 PRO B CG  
17458 C CD  . PRO B 1144 ? 0.4499 0.2859 0.4075 0.0408  -0.0218 -0.0093 1142 PRO B CD  
17459 N N   . GLN B 1145 ? 0.4781 0.3048 0.4296 0.0380  -0.0253 -0.0194 1143 GLN B N   
17460 C CA  . GLN B 1145 ? 0.4415 0.2722 0.3953 0.0343  -0.0255 -0.0209 1143 GLN B CA  
17461 C C   . GLN B 1145 ? 0.3863 0.2305 0.3454 0.0352  -0.0228 -0.0213 1143 GLN B C   
17462 O O   . GLN B 1145 ? 0.3919 0.2422 0.3552 0.0310  -0.0224 -0.0208 1143 GLN B O   
17463 C CB  . GLN B 1145 ? 0.4962 0.3183 0.4440 0.0361  -0.0275 -0.0245 1143 GLN B CB  
17464 N N   . THR B 1146 ? 0.4151 0.2642 0.3742 0.0405  -0.0208 -0.0220 1144 THR B N   
17465 C CA  . THR B 1146 ? 0.4136 0.2754 0.3777 0.0411  -0.0183 -0.0220 1144 THR B CA  
17466 C C   . THR B 1146 ? 0.3872 0.2561 0.3571 0.0368  -0.0173 -0.0189 1144 THR B C   
17467 O O   . THR B 1146 ? 0.4190 0.2962 0.3932 0.0344  -0.0161 -0.0189 1144 THR B O   
17468 C CB  . THR B 1146 ? 0.4216 0.2875 0.3850 0.0472  -0.0165 -0.0227 1144 THR B CB  
17469 O OG1 . THR B 1146 ? 0.4815 0.3434 0.4437 0.0490  -0.0168 -0.0206 1144 THR B OG1 
17470 C CG2 . THR B 1146 ? 0.5123 0.3736 0.4705 0.0518  -0.0169 -0.0262 1144 THR B CG2 
17471 N N   . VAL B 1147 ? 0.3607 0.2265 0.3306 0.0361  -0.0176 -0.0163 1145 VAL B N   
17472 C CA  . VAL B 1147 ? 0.3269 0.1991 0.3020 0.0321  -0.0166 -0.0133 1145 VAL B CA  
17473 C C   . VAL B 1147 ? 0.3485 0.2183 0.3250 0.0261  -0.0180 -0.0125 1145 VAL B C   
17474 O O   . VAL B 1147 ? 0.3473 0.2249 0.3287 0.0227  -0.0170 -0.0116 1145 VAL B O   
17475 C CB  . VAL B 1147 ? 0.3161 0.1865 0.2906 0.0334  -0.0163 -0.0106 1145 VAL B CB  
17476 C CG1 . VAL B 1147 ? 0.3538 0.2320 0.3335 0.0297  -0.0149 -0.0077 1145 VAL B CG1 
17477 C CG2 . VAL B 1147 ? 0.3353 0.2078 0.3082 0.0396  -0.0152 -0.0115 1145 VAL B CG2 
17478 N N   . GLY B 1148 ? 0.3569 0.2159 0.3292 0.0247  -0.0205 -0.0129 1146 GLY B N   
17479 C CA  . GLY B 1148 ? 0.3493 0.2061 0.3231 0.0188  -0.0220 -0.0120 1146 GLY B CA  
17480 C C   . GLY B 1148 ? 0.3737 0.2364 0.3503 0.0168  -0.0218 -0.0139 1146 GLY B C   
17481 O O   . GLY B 1148 ? 0.3629 0.2293 0.3435 0.0120  -0.0221 -0.0126 1146 GLY B O   
17482 N N   . LEU B 1149 ? 0.3779 0.2418 0.3526 0.0205  -0.0214 -0.0169 1147 LEU B N   
17483 C CA  . LEU B 1149 ? 0.3455 0.2151 0.3225 0.0189  -0.0213 -0.0186 1147 LEU B CA  
17484 C C   . LEU B 1149 ? 0.3505 0.2318 0.3339 0.0172  -0.0191 -0.0170 1147 LEU B C   
17485 O O   . LEU B 1149 ? 0.3712 0.2570 0.3574 0.0144  -0.0192 -0.0176 1147 LEU B O   
17486 C CB  . LEU B 1149 ? 0.4964 0.3656 0.4698 0.0236  -0.0209 -0.0219 1147 LEU B CB  
17487 N N   . ARG B 1150 ? 0.3174 0.2034 0.3029 0.0188  -0.0171 -0.0151 1148 ARG B N   
17488 C CA  . ARG B 1150 ? 0.2987 0.1951 0.2898 0.0172  -0.0151 -0.0136 1148 ARG B CA  
17489 C C   . ARG B 1150 ? 0.2768 0.1741 0.2711 0.0129  -0.0152 -0.0105 1148 ARG B C   
17490 O O   . ARG B 1150 ? 0.2755 0.1810 0.2742 0.0115  -0.0135 -0.0092 1148 ARG B O   
17491 C CB  . ARG B 1150 ? 0.2898 0.1915 0.2814 0.0213  -0.0129 -0.0132 1148 ARG B CB  
17492 C CG  . ARG B 1150 ? 0.3421 0.2464 0.3321 0.0254  -0.0121 -0.0158 1148 ARG B CG  
17493 C CD  . ARG B 1150 ? 0.3270 0.2419 0.3212 0.0258  -0.0099 -0.0154 1148 ARG B CD  
17494 N NE  . ARG B 1150 ? 0.3061 0.2241 0.2989 0.0301  -0.0089 -0.0173 1148 ARG B NE  
17495 C CZ  . ARG B 1150 ? 0.2998 0.2235 0.2939 0.0328  -0.0072 -0.0167 1148 ARG B CZ  
17496 N NH1 . ARG B 1150 ? 0.2619 0.1890 0.2587 0.0318  -0.0064 -0.0143 1148 ARG B NH1 
17497 N NH2 . ARG B 1150 ? 0.2647 0.1911 0.2575 0.0365  -0.0063 -0.0184 1148 ARG B NH2 
17498 N N   . VAL B 1151 ? 0.3050 0.1939 0.2968 0.0108  -0.0170 -0.0094 1149 VAL B N   
17499 C CA  . VAL B 1151 ? 0.2904 0.1797 0.2847 0.0069  -0.0169 -0.0062 1149 VAL B CA  
17500 C C   . VAL B 1151 ? 0.2994 0.1861 0.2949 0.0018  -0.0188 -0.0060 1149 VAL B C   
17501 O O   . VAL B 1151 ? 0.3466 0.2249 0.3383 0.0013  -0.0212 -0.0074 1149 VAL B O   
17502 C CB  . VAL B 1151 ? 0.3069 0.1887 0.2975 0.0083  -0.0175 -0.0045 1149 VAL B CB  
17503 C CG1 . VAL B 1151 ? 0.3460 0.2272 0.3386 0.0036  -0.0177 -0.0011 1149 VAL B CG1 
17504 C CG2 . VAL B 1151 ? 0.3424 0.2280 0.3325 0.0131  -0.0156 -0.0044 1149 VAL B CG2 
17505 N N   . SER B 1152 ? 0.2779 0.1717 0.2786 -0.0018 -0.0179 -0.0042 1150 SER B N   
17506 C CA  . SER B 1152 ? 0.2810 0.1729 0.2835 -0.0071 -0.0196 -0.0031 1150 SER B CA  
17507 C C   . SER B 1152 ? 0.2850 0.1803 0.2907 -0.0102 -0.0184 0.0005  1150 SER B C   
17508 O O   . SER B 1152 ? 0.2821 0.1828 0.2894 -0.0083 -0.0161 0.0018  1150 SER B O   
17509 C CB  . SER B 1152 ? 0.3163 0.2142 0.3223 -0.0089 -0.0199 -0.0047 1150 SER B CB  
17510 O OG  . SER B 1152 ? 0.3835 0.2918 0.3942 -0.0083 -0.0175 -0.0040 1150 SER B OG  
17511 N N   . TRP B 1153 ? 0.2986 0.1906 0.3051 -0.0149 -0.0200 0.0021  1151 TRP B N   
17512 C CA  . TRP B 1153 ? 0.2886 0.1841 0.2985 -0.0186 -0.0190 0.0056  1151 TRP B CA  
17513 C C   . TRP B 1153 ? 0.2967 0.1997 0.3122 -0.0226 -0.0189 0.0060  1151 TRP B C   
17514 O O   . TRP B 1153 ? 0.3311 0.2317 0.3467 -0.0247 -0.0211 0.0046  1151 TRP B O   
17515 C CB  . TRP B 1153 ? 0.2913 0.1769 0.2976 -0.0212 -0.0209 0.0076  1151 TRP B CB  
17516 C CG  . TRP B 1153 ? 0.2906 0.1695 0.2917 -0.0171 -0.0207 0.0078  1151 TRP B CG  
17517 C CD1 . TRP B 1153 ? 0.3585 0.2292 0.3541 -0.0132 -0.0222 0.0053  1151 TRP B CD1 
17518 C CD2 . TRP B 1153 ? 0.2981 0.1784 0.2990 -0.0161 -0.0189 0.0105  1151 TRP B CD2 
17519 N NE1 . TRP B 1153 ? 0.3482 0.2152 0.3404 -0.0099 -0.0214 0.0064  1151 TRP B NE1 
17520 C CE2 . TRP B 1153 ? 0.3060 0.1786 0.3013 -0.0116 -0.0195 0.0096  1151 TRP B CE2 
17521 C CE3 . TRP B 1153 ? 0.3032 0.1904 0.3078 -0.0184 -0.0168 0.0136  1151 TRP B CE3 
17522 C CZ2 . TRP B 1153 ? 0.3237 0.1955 0.3173 -0.0096 -0.0183 0.0118  1151 TRP B CZ2 
17523 C CZ3 . TRP B 1153 ? 0.2964 0.1825 0.2990 -0.0165 -0.0156 0.0157  1151 TRP B CZ3 
17524 C CH2 . TRP B 1153 ? 0.3267 0.2052 0.3238 -0.0122 -0.0164 0.0149  1151 TRP B CH2 
17525 N N   . SER B 1154 ? 0.2387 0.1509 0.2589 -0.0234 -0.0165 0.0079  1152 SER B N   
17526 C CA  . SER B 1154 ? 0.2449 0.1655 0.2709 -0.0265 -0.0161 0.0083  1152 SER B CA  
17527 C C   . SER B 1154 ? 0.2403 0.1638 0.2697 -0.0310 -0.0155 0.0118  1152 SER B C   
17528 O O   . SER B 1154 ? 0.2419 0.1679 0.2715 -0.0304 -0.0134 0.0140  1152 SER B O   
17529 C CB  . SER B 1154 ? 0.2660 0.1961 0.2952 -0.0235 -0.0138 0.0071  1152 SER B CB  
17530 O OG  . SER B 1154 ? 0.2356 0.1735 0.2704 -0.0265 -0.0134 0.0077  1152 SER B OG  
17531 N N   . LYS B 1155 ? 0.2492 0.1725 0.2810 -0.0356 -0.0173 0.0124  1153 LYS B N   
17532 C CA  . LYS B 1155 ? 0.2633 0.1917 0.2996 -0.0403 -0.0166 0.0157  1153 LYS B CA  
17533 C C   . LYS B 1155 ? 0.2625 0.2023 0.3053 -0.0412 -0.0153 0.0155  1153 LYS B C   
17534 O O   . LYS B 1155 ? 0.2735 0.2187 0.3208 -0.0453 -0.0149 0.0179  1153 LYS B O   
17535 C CB  . LYS B 1155 ? 0.3178 0.2388 0.3528 -0.0453 -0.0196 0.0168  1153 LYS B CB  
17536 N N   . ASP B 1156 ? 0.2156 0.1591 0.2589 -0.0376 -0.0148 0.0127  1154 ASP B N   
17537 C CA  . ASP B 1156 ? 0.2142 0.1677 0.2632 -0.0380 -0.0139 0.0122  1154 ASP B CA  
17538 C C   . ASP B 1156 ? 0.2197 0.1761 0.2676 -0.0328 -0.0124 0.0097  1154 ASP B C   
17539 O O   . ASP B 1156 ? 0.2200 0.1739 0.2661 -0.0310 -0.0139 0.0070  1154 ASP B O   
17540 C CB  . ASP B 1156 ? 0.2130 0.1656 0.2637 -0.0410 -0.0168 0.0111  1154 ASP B CB  
17541 C CG  . ASP B 1156 ? 0.2184 0.1816 0.2755 -0.0420 -0.0161 0.0111  1154 ASP B CG  
17542 O OD1 . ASP B 1156 ? 0.2004 0.1703 0.2594 -0.0388 -0.0137 0.0106  1154 ASP B OD1 
17543 O OD2 . ASP B 1156 ? 0.2291 0.1935 0.2892 -0.0459 -0.0181 0.0116  1154 ASP B OD2 
17544 N N   . TRP B 1157 ? 0.1772 0.1388 0.2261 -0.0307 -0.0095 0.0108  1155 TRP B N   
17545 C CA  . TRP B 1157 ? 0.1816 0.1451 0.2289 -0.0260 -0.0082 0.0087  1155 TRP B CA  
17546 C C   . TRP B 1157 ? 0.2256 0.1945 0.2758 -0.0252 -0.0085 0.0066  1155 TRP B C   
17547 O O   . TRP B 1157 ? 0.2161 0.1832 0.2639 -0.0222 -0.0090 0.0041  1155 TRP B O   
17548 C CB  . TRP B 1157 ? 0.2153 0.1839 0.2633 -0.0243 -0.0052 0.0102  1155 TRP B CB  
17549 C CG  . TRP B 1157 ? 0.1965 0.1604 0.2415 -0.0247 -0.0046 0.0124  1155 TRP B CG  
17550 C CD1 . TRP B 1157 ? 0.2083 0.1633 0.2495 -0.0260 -0.0065 0.0130  1155 TRP B CD1 
17551 C CD2 . TRP B 1157 ? 0.1875 0.1552 0.2327 -0.0238 -0.0021 0.0144  1155 TRP B CD2 
17552 N NE1 . TRP B 1157 ? 0.2119 0.1650 0.2512 -0.0259 -0.0052 0.0154  1155 TRP B NE1 
17553 C CE2 . TRP B 1157 ? 0.1856 0.1467 0.2273 -0.0247 -0.0025 0.0163  1155 TRP B CE2 
17554 C CE3 . TRP B 1157 ? 0.1975 0.1734 0.2453 -0.0224 0.0005  0.0146  1155 TRP B CE3 
17555 C CZ2 . TRP B 1157 ? 0.2134 0.1758 0.2540 -0.0242 -0.0005 0.0185  1155 TRP B CZ2 
17556 C CZ3 . TRP B 1157 ? 0.2184 0.1957 0.2651 -0.0219 0.0025  0.0167  1155 TRP B CZ3 
17557 C CH2 . TRP B 1157 ? 0.2196 0.1904 0.2628 -0.0228 0.0020  0.0187  1155 TRP B CH2 
17558 N N   . ALA B 1158 ? 0.1954 0.1711 0.2509 -0.0277 -0.0083 0.0076  1156 ALA B N   
17559 C CA  . ALA B 1158 ? 0.1927 0.1741 0.2512 -0.0267 -0.0085 0.0059  1156 ALA B CA  
17560 C C   . ALA B 1158 ? 0.2159 0.1925 0.2727 -0.0273 -0.0115 0.0038  1156 ALA B C   
17561 O O   . ALA B 1158 ? 0.2757 0.2540 0.3324 -0.0251 -0.0119 0.0016  1156 ALA B O   
17562 C CB  . ALA B 1158 ? 0.1810 0.1711 0.2457 -0.0292 -0.0076 0.0077  1156 ALA B CB  
17563 N N   . ALA B 1159 ? 0.2068 0.1773 0.2622 -0.0304 -0.0138 0.0044  1157 ALA B N   
17564 C CA  . ALA B 1159 ? 0.2203 0.1856 0.2735 -0.0310 -0.0168 0.0022  1157 ALA B CA  
17565 C C   . ALA B 1159 ? 0.2591 0.2169 0.3060 -0.0275 -0.0173 -0.0001 1157 ALA B C   
17566 O O   . ALA B 1159 ? 0.2771 0.2323 0.3221 -0.0266 -0.0191 -0.0024 1157 ALA B O   
17567 C CB  . ALA B 1159 ? 0.2429 0.2039 0.2964 -0.0357 -0.0192 0.0036  1157 ALA B CB  
17568 N N   . ASP B 1160 ? 0.2516 0.2063 0.2955 -0.0254 -0.0157 0.0006  1158 ASP B N   
17569 C CA  . ASP B 1160 ? 0.2675 0.2147 0.3055 -0.0222 -0.0162 -0.0013 1158 ASP B CA  
17570 C C   . ASP B 1160 ? 0.2574 0.2081 0.2945 -0.0178 -0.0143 -0.0028 1158 ASP B C   
17571 O O   . ASP B 1160 ? 0.3058 0.2516 0.3384 -0.0148 -0.0144 -0.0044 1158 ASP B O   
17572 C CB  . ASP B 1160 ? 0.2638 0.2045 0.2986 -0.0226 -0.0161 0.0004  1158 ASP B CB  
17573 C CG  . ASP B 1160 ? 0.2720 0.2071 0.3065 -0.0270 -0.0186 0.0015  1158 ASP B CG  
17574 O OD1 . ASP B 1160 ? 0.3316 0.2666 0.3673 -0.0293 -0.0207 0.0005  1158 ASP B OD1 
17575 O OD2 . ASP B 1160 ? 0.3056 0.2365 0.3385 -0.0284 -0.0185 0.0036  1158 ASP B OD2 
17576 N N   . GLY B 1161 ? 0.2329 0.1919 0.2740 -0.0174 -0.0125 -0.0023 1159 GLY B N   
17577 C CA  . GLY B 1161 ? 0.2782 0.2407 0.3187 -0.0137 -0.0109 -0.0038 1159 GLY B CA  
17578 C C   . GLY B 1161 ? 0.2999 0.2624 0.3397 -0.0128 -0.0123 -0.0062 1159 GLY B C   
17579 O O   . GLY B 1161 ? 0.3209 0.2796 0.3598 -0.0146 -0.0147 -0.0071 1159 GLY B O   
17580 N N   . PRO B 1162 ? 0.3189 0.2856 0.3589 -0.0101 -0.0110 -0.0073 1160 PRO B N   
17581 C CA  . PRO B 1162 ? 0.2648 0.2362 0.3058 -0.0081 -0.0085 -0.0065 1160 PRO B CA  
17582 C C   . PRO B 1162 ? 0.2644 0.2319 0.3016 -0.0057 -0.0076 -0.0066 1160 PRO B C   
17583 O O   . PRO B 1162 ? 0.2860 0.2483 0.3193 -0.0041 -0.0085 -0.0081 1160 PRO B O   
17584 C CB  . PRO B 1162 ? 0.3309 0.3065 0.3727 -0.0064 -0.0082 -0.0081 1160 PRO B CB  
17585 C CG  . PRO B 1162 ? 0.3553 0.3261 0.3939 -0.0059 -0.0102 -0.0102 1160 PRO B CG  
17586 C CD  . PRO B 1162 ? 0.3637 0.3303 0.4024 -0.0090 -0.0122 -0.0096 1160 PRO B CD  
17587 N N   . PHE B 1163 ? 0.2032 0.1734 0.2414 -0.0053 -0.0057 -0.0049 1161 PHE B N   
17588 C CA  . PHE B 1163 ? 0.2020 0.1700 0.2371 -0.0028 -0.0046 -0.0048 1161 PHE B CA  
17589 C C   . PHE B 1163 ? 0.1827 0.1557 0.2181 -0.0002 -0.0030 -0.0057 1161 PHE B C   
17590 O O   . PHE B 1163 ? 0.1982 0.1758 0.2360 -0.0005 -0.0027 -0.0062 1161 PHE B O   
17591 C CB  . PHE B 1163 ? 0.2165 0.1840 0.2521 -0.0040 -0.0037 -0.0023 1161 PHE B CB  
17592 C CG  . PHE B 1163 ? 0.2065 0.1692 0.2420 -0.0070 -0.0053 -0.0012 1161 PHE B CG  
17593 C CD1 . PHE B 1163 ? 0.2693 0.2244 0.3010 -0.0066 -0.0072 -0.0023 1161 PHE B CD1 
17594 C CD2 . PHE B 1163 ? 0.2300 0.1956 0.2690 -0.0103 -0.0051 0.0008  1161 PHE B CD2 
17595 C CE1 . PHE B 1163 ? 0.2716 0.2215 0.3028 -0.0095 -0.0090 -0.0014 1161 PHE B CE1 
17596 C CE2 . PHE B 1163 ? 0.2364 0.1975 0.2753 -0.0134 -0.0067 0.0019  1161 PHE B CE2 
17597 C CZ  . PHE B 1163 ? 0.2358 0.1887 0.2707 -0.0131 -0.0088 0.0008  1161 PHE B CZ  
17598 N N   . ALA B 1164 ? 0.2121 0.1838 0.2448 0.0023  -0.0022 -0.0058 1162 ALA B N   
17599 C CA  . ALA B 1164 ? 0.2155 0.1915 0.2482 0.0046  -0.0008 -0.0065 1162 ALA B CA  
17600 C C   . ALA B 1164 ? 0.2189 0.1970 0.2515 0.0055  0.0008  -0.0050 1162 ALA B C   
17601 O O   . ALA B 1164 ? 0.2273 0.2081 0.2592 0.0075  0.0018  -0.0055 1162 ALA B O   
17602 C CB  . ALA B 1164 ? 0.2241 0.1980 0.2538 0.0070  -0.0013 -0.0085 1162 ALA B CB  
17603 N N   . GLY B 1165 ? 0.1870 0.1636 0.2201 0.0040  0.0010  -0.0031 1163 GLY B N   
17604 C CA  . GLY B 1165 ? 0.1935 0.1717 0.2261 0.0046  0.0024  -0.0014 1163 GLY B CA  
17605 C C   . GLY B 1165 ? 0.1894 0.1639 0.2216 0.0028  0.0020  0.0006  1163 GLY B C   
17606 O O   . GLY B 1165 ? 0.1862 0.1565 0.2182 0.0012  0.0005  0.0005  1163 GLY B O   
17607 N N   . ALA B 1166 ? 0.1964 0.1723 0.2283 0.0030  0.0032  0.0024  1164 ALA B N   
17608 C CA  . ALA B 1166 ? 0.1786 0.1508 0.2098 0.0011  0.0030  0.0047  1164 ALA B CA  
17609 C C   . ALA B 1166 ? 0.1939 0.1657 0.2228 0.0028  0.0039  0.0061  1164 ALA B C   
17610 O O   . ALA B 1166 ? 0.2121 0.1885 0.2413 0.0042  0.0052  0.0061  1164 ALA B O   
17611 C CB  . ALA B 1166 ? 0.2003 0.1762 0.2349 -0.0021 0.0037  0.0062  1164 ALA B CB  
17612 N N   . LEU B 1167 ? 0.1817 0.1474 0.2079 0.0027  0.0030  0.0074  1165 LEU B N   
17613 C CA  . LEU B 1167 ? 0.1819 0.1465 0.2057 0.0040  0.0037  0.0093  1165 LEU B CA  
17614 C C   . LEU B 1167 ? 0.2200 0.1825 0.2440 0.0009  0.0038  0.0120  1165 LEU B C   
17615 O O   . LEU B 1167 ? 0.2159 0.1736 0.2397 -0.0012 0.0024  0.0124  1165 LEU B O   
17616 C CB  . LEU B 1167 ? 0.1987 0.1576 0.2189 0.0069  0.0024  0.0086  1165 LEU B CB  
17617 C CG  . LEU B 1167 ? 0.1841 0.1449 0.2040 0.0098  0.0022  0.0058  1165 LEU B CG  
17618 C CD1 . LEU B 1167 ? 0.2235 0.1789 0.2400 0.0129  0.0011  0.0053  1165 LEU B CD1 
17619 C CD2 . LEU B 1167 ? 0.2326 0.2005 0.2539 0.0111  0.0038  0.0056  1165 LEU B CD2 
17620 N N   . VAL B 1168 ? 0.2035 0.1697 0.2277 0.0005  0.0054  0.0140  1166 VAL B N   
17621 C CA  . VAL B 1168 ? 0.2163 0.1821 0.2410 -0.0026 0.0060  0.0168  1166 VAL B CA  
17622 C C   . VAL B 1168 ? 0.2192 0.1827 0.2405 -0.0015 0.0064  0.0190  1166 VAL B C   
17623 O O   . VAL B 1168 ? 0.2211 0.1878 0.2414 0.0012  0.0073  0.0186  1166 VAL B O   
17624 C CB  . VAL B 1168 ? 0.2123 0.1857 0.2409 -0.0046 0.0078  0.0172  1166 VAL B CB  
17625 C CG1 . VAL B 1168 ? 0.2153 0.1889 0.2446 -0.0079 0.0086  0.0203  1166 VAL B CG1 
17626 C CG2 . VAL B 1168 ? 0.2017 0.1776 0.2337 -0.0053 0.0072  0.0149  1166 VAL B CG2 
17627 N N   . GLU B 1169 ? 0.2148 0.1729 0.2344 -0.0034 0.0057  0.0214  1167 GLU B N   
17628 C CA  . GLU B 1169 ? 0.2277 0.1833 0.2439 -0.0029 0.0061  0.0240  1167 GLU B CA  
17629 C C   . GLU B 1169 ? 0.2499 0.2073 0.2673 -0.0068 0.0073  0.0270  1167 GLU B C   
17630 O O   . GLU B 1169 ? 0.2513 0.2069 0.2705 -0.0101 0.0066  0.0277  1167 GLU B O   
17631 C CB  . GLU B 1169 ? 0.2299 0.1763 0.2422 -0.0016 0.0040  0.0244  1167 GLU B CB  
17632 C CG  . GLU B 1169 ? 0.2423 0.1854 0.2509 -0.0010 0.0041  0.0273  1167 GLU B CG  
17633 C CD  . GLU B 1169 ? 0.2766 0.2095 0.2812 -0.0004 0.0019  0.0280  1167 GLU B CD  
17634 O OE1 . GLU B 1169 ? 0.2724 0.2008 0.2772 -0.0011 0.0003  0.0264  1167 GLU B OE1 
17635 O OE2 . GLU B 1169 ? 0.2965 0.2258 0.2976 0.0008  0.0016  0.0302  1167 GLU B OE2 
17636 N N   . GLY B 1170 ? 0.2410 0.2022 0.2575 -0.0064 0.0090  0.0288  1168 GLY B N   
17637 C CA  . GLY B 1170 ? 0.2560 0.2190 0.2732 -0.0100 0.0103  0.0319  1168 GLY B CA  
17638 C C   . GLY B 1170 ? 0.3051 0.2742 0.3217 -0.0090 0.0126  0.0330  1168 GLY B C   
17639 O O   . GLY B 1170 ? 0.2707 0.2428 0.2866 -0.0058 0.0130  0.0312  1168 GLY B O   
17640 N N   . ASP B 1171 ? 0.2966 0.2676 0.3133 -0.0119 0.0140  0.0360  1169 ASP B N   
17641 C CA  . ASP B 1171 ? 0.2954 0.2727 0.3116 -0.0113 0.0164  0.0370  1169 ASP B CA  
17642 C C   . ASP B 1171 ? 0.2673 0.2529 0.2879 -0.0114 0.0180  0.0349  1169 ASP B C   
17643 O O   . ASP B 1171 ? 0.2619 0.2482 0.2860 -0.0121 0.0173  0.0330  1169 ASP B O   
17644 C CB  . ASP B 1171 ? 0.2971 0.2736 0.3114 -0.0142 0.0175  0.0411  1169 ASP B CB  
17645 C CG  . ASP B 1171 ? 0.3293 0.3075 0.3472 -0.0187 0.0182  0.0427  1169 ASP B CG  
17646 O OD1 . ASP B 1171 ? 0.3146 0.2956 0.3368 -0.0196 0.0179  0.0408  1169 ASP B OD1 
17647 O OD2 . ASP B 1171 ? 0.4195 0.3965 0.4359 -0.0215 0.0190  0.0463  1169 ASP B OD2 
17648 N N   . ALA B 1172 ? 0.2844 0.2759 0.3045 -0.0104 0.0202  0.0353  1170 ALA B N   
17649 C CA  . ALA B 1172 ? 0.2923 0.2911 0.3159 -0.0098 0.0217  0.0330  1170 ALA B CA  
17650 C C   . ALA B 1172 ? 0.2733 0.2751 0.3017 -0.0129 0.0222  0.0333  1170 ALA B C   
17651 O O   . ALA B 1172 ? 0.2837 0.2881 0.3155 -0.0124 0.0218  0.0308  1170 ALA B O   
17652 C CB  . ALA B 1172 ? 0.3005 0.3047 0.3223 -0.0087 0.0240  0.0338  1170 ALA B CB  
17653 N N   . GLU B 1173 ? 0.2712 0.2729 0.3001 -0.0163 0.0229  0.0365  1171 GLU B N   
17654 C CA  . GLU B 1173 ? 0.2888 0.2945 0.3228 -0.0194 0.0235  0.0369  1171 GLU B CA  
17655 C C   . GLU B 1173 ? 0.2687 0.2695 0.3046 -0.0206 0.0208  0.0355  1171 GLU B C   
17656 O O   . GLU B 1173 ? 0.2631 0.2677 0.3035 -0.0217 0.0207  0.0342  1171 GLU B O   
17657 C CB  . GLU B 1173 ? 0.3809 0.3888 0.4152 -0.0230 0.0252  0.0407  1171 GLU B CB  
17658 C CG  . GLU B 1173 ? 0.4581 0.4734 0.4919 -0.0220 0.0283  0.0415  1171 GLU B CG  
17659 C CD  . GLU B 1173 ? 0.4509 0.4734 0.4882 -0.0197 0.0295  0.0384  1171 GLU B CD  
17660 O OE1 . GLU B 1173 ? 0.4442 0.4697 0.4863 -0.0209 0.0291  0.0373  1171 GLU B OE1 
17661 O OE2 . GLU B 1173 ? 0.5020 0.5269 0.5368 -0.0166 0.0307  0.0371  1171 GLU B OE2 
17662 N N   . ARG B 1174 ? 0.2600 0.2524 0.2924 -0.0202 0.0186  0.0358  1172 ARG B N   
17663 C CA  . ARG B 1174 ? 0.2568 0.2440 0.2902 -0.0207 0.0160  0.0341  1172 ARG B CA  
17664 C C   . ARG B 1174 ? 0.2204 0.2100 0.2553 -0.0176 0.0155  0.0302  1172 ARG B C   
17665 O O   . ARG B 1174 ? 0.2413 0.2320 0.2796 -0.0186 0.0146  0.0286  1172 ARG B O   
17666 C CB  . ARG B 1174 ? 0.2699 0.2476 0.2986 -0.0202 0.0140  0.0350  1172 ARG B CB  
17667 C CG  . ARG B 1174 ? 0.2729 0.2443 0.3016 -0.0200 0.0112  0.0329  1172 ARG B CG  
17668 C CD  . ARG B 1174 ? 0.3003 0.2718 0.3325 -0.0243 0.0105  0.0336  1172 ARG B CD  
17669 N NE  . ARG B 1174 ? 0.2924 0.2574 0.3240 -0.0242 0.0077  0.0316  1172 ARG B NE  
17670 C CZ  . ARG B 1174 ? 0.2647 0.2301 0.2997 -0.0269 0.0065  0.0309  1172 ARG B CZ  
17671 N NH1 . ARG B 1174 ? 0.2892 0.2614 0.3287 -0.0301 0.0078  0.0322  1172 ARG B NH1 
17672 N NH2 . ARG B 1174 ? 0.2951 0.2541 0.3287 -0.0264 0.0040  0.0288  1172 ARG B NH2 
17673 N N   . ILE B 1175 ? 0.2199 0.2104 0.2523 -0.0140 0.0161  0.0289  1173 ILE B N   
17674 C CA  . ILE B 1175 ? 0.2228 0.2157 0.2564 -0.0112 0.0158  0.0255  1173 ILE B CA  
17675 C C   . ILE B 1175 ? 0.2126 0.2128 0.2508 -0.0121 0.0171  0.0245  1173 ILE B C   
17676 O O   . ILE B 1175 ? 0.2122 0.2131 0.2529 -0.0117 0.0160  0.0222  1173 ILE B O   
17677 C CB  . ILE B 1175 ? 0.2219 0.2153 0.2521 -0.0077 0.0163  0.0247  1173 ILE B CB  
17678 C CG1 . ILE B 1175 ? 0.2390 0.2251 0.2652 -0.0062 0.0146  0.0251  1173 ILE B CG1 
17679 C CG2 . ILE B 1175 ? 0.2172 0.2145 0.2490 -0.0053 0.0164  0.0215  1173 ILE B CG2 
17680 C CD1 . ILE B 1175 ? 0.2576 0.2443 0.2803 -0.0033 0.0151  0.0251  1173 ILE B CD1 
17681 N N   . ARG B 1176 ? 0.2325 0.2384 0.2718 -0.0130 0.0194  0.0261  1174 ARG B N   
17682 C CA  . ARG B 1176 ? 0.2195 0.2326 0.2632 -0.0134 0.0207  0.0252  1174 ARG B CA  
17683 C C   . ARG B 1176 ? 0.2191 0.2324 0.2669 -0.0164 0.0195  0.0253  1174 ARG B C   
17684 O O   . ARG B 1176 ? 0.2147 0.2308 0.2657 -0.0159 0.0191  0.0232  1174 ARG B O   
17685 C CB  . ARG B 1176 ? 0.2476 0.2666 0.2915 -0.0141 0.0235  0.0272  1174 ARG B CB  
17686 C CG  . ARG B 1176 ? 0.2931 0.3199 0.3410 -0.0135 0.0252  0.0259  1174 ARG B CG  
17687 C CD  . ARG B 1176 ? 0.3281 0.3612 0.3770 -0.0148 0.0280  0.0283  1174 ARG B CD  
17688 N NE  . ARG B 1176 ? 0.3360 0.3680 0.3801 -0.0137 0.0293  0.0297  1174 ARG B NE  
17689 C CZ  . ARG B 1176 ? 0.3752 0.4098 0.4169 -0.0107 0.0307  0.0284  1174 ARG B CZ  
17690 N NH1 . ARG B 1176 ? 0.3856 0.4236 0.4290 -0.0084 0.0309  0.0255  1174 ARG B NH1 
17691 N NH2 . ARG B 1176 ? 0.3849 0.4185 0.4223 -0.0102 0.0318  0.0300  1174 ARG B NH2 
17692 N N   . ALA B 1177 ? 0.2237 0.2335 0.2713 -0.0196 0.0189  0.0279  1175 ALA B N   
17693 C CA  . ALA B 1177 ? 0.2270 0.2368 0.2785 -0.0229 0.0176  0.0282  1175 ALA B CA  
17694 C C   . ALA B 1177 ? 0.2047 0.2096 0.2560 -0.0218 0.0149  0.0255  1175 ALA B C   
17695 O O   . ALA B 1177 ? 0.2148 0.2223 0.2699 -0.0228 0.0140  0.0242  1175 ALA B O   
17696 C CB  . ALA B 1177 ? 0.2386 0.2444 0.2891 -0.0267 0.0171  0.0316  1175 ALA B CB  
17697 N N   . VAL B 1178 ? 0.2233 0.2213 0.2701 -0.0198 0.0136  0.0246  1176 VAL B N   
17698 C CA  . VAL B 1178 ? 0.2058 0.1992 0.2521 -0.0185 0.0112  0.0220  1176 VAL B CA  
17699 C C   . VAL B 1178 ? 0.1973 0.1954 0.2453 -0.0158 0.0116  0.0191  1176 VAL B C   
17700 O O   . VAL B 1178 ? 0.2161 0.2143 0.2661 -0.0160 0.0102  0.0172  1176 VAL B O   
17701 C CB  . VAL B 1178 ? 0.2413 0.2267 0.2824 -0.0166 0.0099  0.0218  1176 VAL B CB  
17702 C CG1 . VAL B 1178 ? 0.2339 0.2154 0.2740 -0.0146 0.0079  0.0188  1176 VAL B CG1 
17703 C CG2 . VAL B 1178 ? 0.2407 0.2202 0.2798 -0.0195 0.0090  0.0246  1176 VAL B CG2 
17704 N N   . ASN B 1179 ? 0.2029 0.2049 0.2499 -0.0134 0.0135  0.0188  1177 ASN B N   
17705 C CA  . ASN B 1179 ? 0.2188 0.2249 0.2671 -0.0109 0.0139  0.0161  1177 ASN B CA  
17706 C C   . ASN B 1179 ? 0.1988 0.2108 0.2520 -0.0124 0.0143  0.0158  1177 ASN B C   
17707 O O   . ASN B 1179 ? 0.2132 0.2261 0.2680 -0.0114 0.0133  0.0136  1177 ASN B O   
17708 C CB  . ASN B 1179 ? 0.2056 0.2146 0.2517 -0.0084 0.0158  0.0162  1177 ASN B CB  
17709 C CG  . ASN B 1179 ? 0.2450 0.2556 0.2907 -0.0055 0.0157  0.0133  1177 ASN B CG  
17710 O OD1 . ASN B 1179 ? 0.2586 0.2665 0.3042 -0.0047 0.0140  0.0114  1177 ASN B OD1 
17711 N ND2 . ASN B 1179 ? 0.2308 0.2456 0.2759 -0.0039 0.0174  0.0131  1177 ASN B ND2 
17712 N N   . LYS B 1180 ? 0.2084 0.2245 0.2641 -0.0147 0.0157  0.0181  1178 LYS B N   
17713 C CA  . LYS B 1180 ? 0.2103 0.2324 0.2711 -0.0162 0.0161  0.0180  1178 LYS B CA  
17714 C C   . LYS B 1180 ? 0.1822 0.2013 0.2450 -0.0183 0.0135  0.0173  1178 LYS B C   
17715 O O   . LYS B 1180 ? 0.2184 0.2405 0.2841 -0.0179 0.0128  0.0156  1178 LYS B O   
17716 C CB  . LYS B 1180 ? 0.2344 0.2617 0.2976 -0.0187 0.0181  0.0209  1178 LYS B CB  
17717 C CG  . LYS B 1180 ? 0.3052 0.3369 0.3669 -0.0166 0.0209  0.0214  1178 LYS B CG  
17718 C CD  . LYS B 1180 ? 0.3510 0.3889 0.4156 -0.0190 0.0231  0.0241  1178 LYS B CD  
17719 C CE  . LYS B 1180 ? 0.4665 0.5121 0.5366 -0.0190 0.0239  0.0234  1178 LYS B CE  
17720 N NZ  . LYS B 1180 ? 0.4625 0.5115 0.5320 -0.0151 0.0251  0.0209  1178 LYS B NZ  
17721 N N   . ALA B 1181 ? 0.2033 0.2159 0.2640 -0.0204 0.0119  0.0185  1179 ALA B N   
17722 C CA  . ALA B 1181 ? 0.2024 0.2114 0.2644 -0.0224 0.0093  0.0177  1179 ALA B CA  
17723 C C   . ALA B 1181 ? 0.1979 0.2039 0.2582 -0.0196 0.0078  0.0145  1179 ALA B C   
17724 O O   . ALA B 1181 ? 0.2125 0.2193 0.2751 -0.0202 0.0062  0.0131  1179 ALA B O   
17725 C CB  . ALA B 1181 ? 0.2026 0.2042 0.2618 -0.0250 0.0079  0.0195  1179 ALA B CB  
17726 N N   . ILE B 1182 ? 0.1929 0.1958 0.2491 -0.0165 0.0081  0.0135  1180 ILE B N   
17727 C CA  . ILE B 1182 ? 0.2098 0.2103 0.2643 -0.0139 0.0069  0.0106  1180 ILE B CA  
17728 C C   . ILE B 1182 ? 0.1953 0.2021 0.2528 -0.0125 0.0076  0.0090  1180 ILE B C   
17729 O O   . ILE B 1182 ? 0.2097 0.2159 0.2679 -0.0120 0.0061  0.0071  1180 ILE B O   
17730 C CB  . ILE B 1182 ? 0.2166 0.2134 0.2666 -0.0110 0.0073  0.0101  1180 ILE B CB  
17731 C CG1 . ILE B 1182 ? 0.2182 0.2075 0.2650 -0.0119 0.0059  0.0111  1180 ILE B CG1 
17732 C CG2 . ILE B 1182 ? 0.2424 0.2388 0.2911 -0.0081 0.0067  0.0073  1180 ILE B CG2 
17733 C CD1 . ILE B 1182 ? 0.2168 0.2028 0.2593 -0.0092 0.0064  0.0111  1180 ILE B CD1 
17734 N N   . ALA B 1183 ? 0.2177 0.2304 0.2767 -0.0118 0.0099  0.0098  1181 ALA B N   
17735 C CA  . ALA B 1183 ? 0.2334 0.2516 0.2951 -0.0103 0.0105  0.0083  1181 ALA B CA  
17736 C C   . ALA B 1183 ? 0.2303 0.2515 0.2964 -0.0123 0.0093  0.0082  1181 ALA B C   
17737 O O   . ALA B 1183 ? 0.2673 0.2909 0.3350 -0.0110 0.0088  0.0065  1181 ALA B O   
17738 C CB  . ALA B 1183 ? 0.2293 0.2530 0.2915 -0.0091 0.0131  0.0091  1181 ALA B CB  
17739 N N   . ALA B 1184 ? 0.2106 0.2314 0.2786 -0.0156 0.0087  0.0101  1182 ALA B N   
17740 C CA  . ALA B 1184 ? 0.2444 0.2681 0.3168 -0.0179 0.0074  0.0102  1182 ALA B CA  
17741 C C   . ALA B 1184 ? 0.2289 0.2468 0.3000 -0.0187 0.0044  0.0087  1182 ALA B C   
17742 O O   . ALA B 1184 ? 0.2385 0.2583 0.3129 -0.0207 0.0029  0.0087  1182 ALA B O   
17743 C CB  . ALA B 1184 ? 0.2559 0.2827 0.3314 -0.0215 0.0081  0.0131  1182 ALA B CB  
17744 N N   . LEU B 1185 ? 0.2080 0.2191 0.2743 -0.0172 0.0035  0.0075  1183 LEU B N   
17745 C CA  . LEU B 1185 ? 0.1977 0.2034 0.2625 -0.0177 0.0008  0.0060  1183 LEU B CA  
17746 C C   . LEU B 1185 ? 0.2254 0.2338 0.2915 -0.0160 0.0001  0.0037  1183 LEU B C   
17747 O O   . LEU B 1185 ? 0.2543 0.2657 0.3201 -0.0132 0.0015  0.0028  1183 LEU B O   
17748 C CB  . LEU B 1185 ? 0.1977 0.1959 0.2570 -0.0161 0.0003  0.0052  1183 LEU B CB  
17749 C CG  . LEU B 1185 ? 0.2156 0.2098 0.2729 -0.0176 0.0007  0.0073  1183 LEU B CG  
17750 C CD1 . LEU B 1185 ? 0.2128 0.2004 0.2648 -0.0151 0.0003  0.0062  1183 LEU B CD1 
17751 C CD2 . LEU B 1185 ? 0.2225 0.2140 0.2812 -0.0216 -0.0012 0.0086  1183 LEU B CD2 
17752 N N   . PRO B 1186 ? 0.2358 0.2428 0.3030 -0.0175 -0.0023 0.0029  1184 PRO B N   
17753 C CA  . PRO B 1186 ? 0.2366 0.2452 0.3043 -0.0157 -0.0033 0.0008  1184 PRO B CA  
17754 C C   . PRO B 1186 ? 0.2148 0.2183 0.2776 -0.0130 -0.0036 -0.0012 1184 PRO B C   
17755 O O   . PRO B 1186 ? 0.2651 0.2632 0.3242 -0.0127 -0.0037 -0.0012 1184 PRO B O   
17756 C CB  . PRO B 1186 ? 0.3058 0.3135 0.3755 -0.0185 -0.0060 0.0006  1184 PRO B CB  
17757 C CG  . PRO B 1186 ? 0.3147 0.3163 0.3821 -0.0209 -0.0069 0.0016  1184 PRO B CG  
17758 C CD  . PRO B 1186 ? 0.2730 0.2758 0.3402 -0.0209 -0.0044 0.0037  1184 PRO B CD  
17759 N N   . GLY B 1187 ? 0.2303 0.2358 0.2931 -0.0110 -0.0039 -0.0029 1185 GLY B N   
17760 C CA  . GLY B 1187 ? 0.2158 0.2171 0.2743 -0.0086 -0.0043 -0.0047 1185 GLY B CA  
17761 C C   . GLY B 1187 ? 0.2189 0.2214 0.2756 -0.0061 -0.0021 -0.0048 1185 GLY B C   
17762 O O   . GLY B 1187 ? 0.2501 0.2575 0.3089 -0.0054 -0.0004 -0.0042 1185 GLY B O   
17763 N N   . PRO B 1188 ? 0.1909 0.1890 0.2435 -0.0046 -0.0021 -0.0057 1186 PRO B N   
17764 C CA  . PRO B 1188 ? 0.2055 0.2048 0.2563 -0.0022 -0.0003 -0.0059 1186 PRO B CA  
17765 C C   . PRO B 1188 ? 0.2173 0.2187 0.2689 -0.0025 0.0016  -0.0041 1186 PRO B C   
17766 O O   . PRO B 1188 ? 0.2144 0.2144 0.2666 -0.0043 0.0015  -0.0026 1186 PRO B O   
17767 C CB  . PRO B 1188 ? 0.2549 0.2490 0.3014 -0.0009 -0.0009 -0.0069 1186 PRO B CB  
17768 C CG  . PRO B 1188 ? 0.3086 0.2982 0.3545 -0.0027 -0.0026 -0.0067 1186 PRO B CG  
17769 C CD  . PRO B 1188 ? 0.2195 0.2115 0.2690 -0.0049 -0.0037 -0.0064 1186 PRO B CD  
17770 N N   . LEU B 1189 ? 0.1806 0.1852 0.2321 -0.0008 0.0032  -0.0042 1187 LEU B N   
17771 C CA  . LEU B 1189 ? 0.1715 0.1777 0.2228 -0.0006 0.0050  -0.0027 1187 LEU B CA  
17772 C C   . LEU B 1189 ? 0.1860 0.1880 0.2337 0.0004  0.0050  -0.0025 1187 LEU B C   
17773 O O   . LEU B 1189 ? 0.2187 0.2192 0.2640 0.0022  0.0048  -0.0039 1187 LEU B O   
17774 C CB  . LEU B 1189 ? 0.1958 0.2060 0.2473 0.0012  0.0065  -0.0032 1187 LEU B CB  
17775 C CG  . LEU B 1189 ? 0.2134 0.2287 0.2685 0.0007  0.0071  -0.0029 1187 LEU B CG  
17776 C CD1 . LEU B 1189 ? 0.3064 0.3222 0.3631 0.0007  0.0056  -0.0042 1187 LEU B CD1 
17777 C CD2 . LEU B 1189 ? 0.2365 0.2548 0.2909 0.0024  0.0089  -0.0030 1187 LEU B CD2 
17778 N N   . LEU B 1190 ? 0.1789 0.1789 0.2261 -0.0009 0.0053  -0.0009 1188 LEU B N   
17779 C CA  . LEU B 1190 ? 0.1987 0.1941 0.2425 0.0002  0.0050  -0.0006 1188 LEU B CA  
17780 C C   . LEU B 1190 ? 0.1968 0.1940 0.2390 0.0019  0.0066  0.0000  1188 LEU B C   
17781 O O   . LEU B 1190 ? 0.1971 0.1977 0.2406 0.0013  0.0080  0.0013  1188 LEU B O   
17782 C CB  . LEU B 1190 ? 0.1830 0.1745 0.2265 -0.0018 0.0043  0.0010  1188 LEU B CB  
17783 C CG  . LEU B 1190 ? 0.1841 0.1730 0.2288 -0.0039 0.0024  0.0005  1188 LEU B CG  
17784 C CD1 . LEU B 1190 ? 0.2006 0.1841 0.2437 -0.0055 0.0015  0.0020  1188 LEU B CD1 
17785 C CD2 . LEU B 1190 ? 0.2167 0.2035 0.2599 -0.0024 0.0010  -0.0019 1188 LEU B CD2 
17786 N N   . LEU B 1191 ? 0.1957 0.1908 0.2350 0.0039  0.0063  -0.0010 1189 LEU B N   
17787 C CA  . LEU B 1191 ? 0.1814 0.1775 0.2189 0.0055  0.0074  -0.0003 1189 LEU B CA  
17788 C C   . LEU B 1191 ? 0.1852 0.1778 0.2212 0.0049  0.0074  0.0016  1189 LEU B C   
17789 O O   . LEU B 1191 ? 0.2138 0.2017 0.2479 0.0054  0.0062  0.0014  1189 LEU B O   
17790 C CB  . LEU B 1191 ? 0.1869 0.1825 0.2223 0.0077  0.0070  -0.0019 1189 LEU B CB  
17791 C CG  . LEU B 1191 ? 0.1898 0.1881 0.2239 0.0093  0.0081  -0.0016 1189 LEU B CG  
17792 C CD1 . LEU B 1191 ? 0.1980 0.1969 0.2308 0.0110  0.0077  -0.0033 1189 LEU B CD1 
17793 C CD2 . LEU B 1191 ? 0.1852 0.1815 0.2173 0.0098  0.0084  0.0000  1189 LEU B CD2 
17794 N N   . VAL B 1192 ? 0.1879 0.1827 0.2245 0.0039  0.0086  0.0034  1190 VAL B N   
17795 C CA  . VAL B 1192 ? 0.2011 0.1929 0.2365 0.0029  0.0087  0.0056  1190 VAL B CA  
17796 C C   . VAL B 1192 ? 0.2024 0.1942 0.2351 0.0049  0.0094  0.0064  1190 VAL B C   
17797 O O   . VAL B 1192 ? 0.2123 0.2081 0.2448 0.0058  0.0106  0.0062  1190 VAL B O   
17798 C CB  . VAL B 1192 ? 0.1918 0.1865 0.2297 0.0004  0.0098  0.0074  1190 VAL B CB  
17799 C CG1 . VAL B 1192 ? 0.2013 0.1929 0.2377 -0.0010 0.0100  0.0100  1190 VAL B CG1 
17800 C CG2 . VAL B 1192 ? 0.2126 0.2081 0.2538 -0.0016 0.0090  0.0068  1190 VAL B CG2 
17801 N N   . GLN B 1193 ? 0.1882 0.1750 0.2182 0.0054  0.0086  0.0074  1191 GLN B N   
17802 C CA  . GLN B 1193 ? 0.1746 0.1610 0.2020 0.0071  0.0090  0.0086  1191 GLN B CA  
17803 C C   . GLN B 1193 ? 0.1998 0.1827 0.2260 0.0055  0.0090  0.0112  1191 GLN B C   
17804 O O   . GLN B 1193 ? 0.2107 0.1886 0.2365 0.0043  0.0078  0.0116  1191 GLN B O   
17805 C CB  . GLN B 1193 ? 0.2023 0.1858 0.2274 0.0098  0.0078  0.0073  1191 GLN B CB  
17806 C CG  . GLN B 1193 ? 0.2101 0.1965 0.2363 0.0111  0.0077  0.0048  1191 GLN B CG  
17807 C CD  . GLN B 1193 ? 0.2213 0.2067 0.2454 0.0140  0.0071  0.0040  1191 GLN B CD  
17808 O OE1 . GLN B 1193 ? 0.2230 0.2099 0.2457 0.0154  0.0075  0.0048  1191 GLN B OE1 
17809 N NE2 . GLN B 1193 ? 0.2080 0.1908 0.2317 0.0149  0.0060  0.0024  1191 GLN B NE2 
17810 N N   . ALA B 1194 ? 0.2085 0.1937 0.2338 0.0053  0.0103  0.0130  1192 ALA B N   
17811 C CA  . ALA B 1194 ? 0.2131 0.1956 0.2372 0.0035  0.0105  0.0158  1192 ALA B CA  
17812 C C   . ALA B 1194 ? 0.2363 0.2175 0.2569 0.0055  0.0107  0.0172  1192 ALA B C   
17813 O O   . ALA B 1194 ? 0.2584 0.2432 0.2783 0.0075  0.0112  0.0163  1192 ALA B O   
17814 C CB  . ALA B 1194 ? 0.2327 0.2197 0.2592 0.0009  0.0122  0.0171  1192 ALA B CB  
17815 N N   . ALA B 1195 ? 0.2335 0.2094 0.2518 0.0047  0.0100  0.0194  1193 ALA B N   
17816 C CA  . ALA B 1195 ? 0.2359 0.2102 0.2507 0.0064  0.0100  0.0211  1193 ALA B CA  
17817 C C   . ALA B 1195 ? 0.2721 0.2419 0.2853 0.0041  0.0099  0.0242  1193 ALA B C   
17818 O O   . ALA B 1195 ? 0.2581 0.2242 0.2723 0.0018  0.0091  0.0246  1193 ALA B O   
17819 C CB  . ALA B 1195 ? 0.2575 0.2282 0.2702 0.0097  0.0084  0.0199  1193 ALA B CB  
17820 N N   . SER B 1196 ? 0.2622 0.2323 0.2728 0.0044  0.0106  0.0265  1194 SER B N   
17821 C CA  . SER B 1196 ? 0.2679 0.2329 0.2761 0.0025  0.0103  0.0297  1194 SER B CA  
17822 C C   . SER B 1196 ? 0.2803 0.2375 0.2852 0.0046  0.0081  0.0299  1194 SER B C   
17823 O O   . SER B 1196 ? 0.2894 0.2463 0.2935 0.0080  0.0072  0.0279  1194 SER B O   
17824 C CB  . SER B 1196 ? 0.3068 0.2747 0.3128 0.0024  0.0117  0.0321  1194 SER B CB  
17825 O OG  . SER B 1196 ? 0.3273 0.2955 0.3307 0.0060  0.0111  0.0315  1194 SER B OG  
17826 N N   . SER B 1197 ? 0.2951 0.2459 0.2979 0.0026  0.0073  0.0324  1195 SER B N   
17827 C CA  . SER B 1197 ? 0.2974 0.2400 0.2964 0.0048  0.0052  0.0330  1195 SER B CA  
17828 C C   . SER B 1197 ? 0.2983 0.2419 0.2944 0.0085  0.0051  0.0335  1195 SER B C   
17829 O O   . SER B 1197 ? 0.3176 0.2581 0.3121 0.0120  0.0036  0.0321  1195 SER B O   
17830 C CB  . SER B 1197 ? 0.3259 0.2615 0.3227 0.0017  0.0045  0.0361  1195 SER B CB  
17831 O OG  . SER B 1197 ? 0.3328 0.2677 0.3325 -0.0020 0.0044  0.0357  1195 SER B OG  
17832 N N   . GLY B 1198 ? 0.3187 0.2667 0.3140 0.0078  0.0066  0.0354  1196 GLY B N   
17833 C CA  . GLY B 1198 ? 0.3636 0.3130 0.3561 0.0111  0.0064  0.0358  1196 GLY B CA  
17834 C C   . GLY B 1198 ? 0.3791 0.3338 0.3735 0.0143  0.0063  0.0326  1196 GLY B C   
17835 O O   . GLY B 1198 ? 0.3544 0.3081 0.3470 0.0178  0.0051  0.0321  1196 GLY B O   
17836 N N   . GLU B 1199 ? 0.3126 0.2729 0.3108 0.0130  0.0075  0.0304  1197 GLU B N   
17837 C CA  . GLU B 1199 ? 0.3501 0.3153 0.3503 0.0155  0.0074  0.0273  1197 GLU B CA  
17838 C C   . GLU B 1199 ? 0.3618 0.3230 0.3620 0.0179  0.0057  0.0254  1197 GLU B C   
17839 O O   . GLU B 1199 ? 0.3309 0.2940 0.3308 0.0211  0.0050  0.0240  1197 GLU B O   
17840 C CB  . GLU B 1199 ? 0.3613 0.3323 0.3652 0.0133  0.0090  0.0256  1197 GLU B CB  
17841 C CG  . GLU B 1199 ? 0.4590 0.4356 0.4647 0.0152  0.0092  0.0228  1197 GLU B CG  
17842 C CD  . GLU B 1199 ? 0.4896 0.4713 0.4987 0.0131  0.0106  0.0214  1197 GLU B CD  
17843 O OE1 . GLU B 1199 ? 0.4765 0.4582 0.4864 0.0103  0.0117  0.0228  1197 GLU B OE1 
17844 O OE2 . GLU B 1199 ? 0.5862 0.5718 0.5968 0.0142  0.0107  0.0190  1197 GLU B OE2 
17845 N N   . ILE B 1200 ? 0.2976 0.2533 0.2982 0.0164  0.0050  0.0253  1198 ILE B N   
17846 C CA  . ILE B 1200 ? 0.3040 0.2551 0.3040 0.0188  0.0033  0.0235  1198 ILE B CA  
17847 C C   . ILE B 1200 ? 0.3445 0.2914 0.3409 0.0222  0.0020  0.0247  1198 ILE B C   
17848 O O   . ILE B 1200 ? 0.3311 0.2780 0.3272 0.0257  0.0011  0.0229  1198 ILE B O   
17849 C CB  . ILE B 1200 ? 0.2781 0.2234 0.2786 0.0161  0.0026  0.0235  1198 ILE B CB  
17850 C CG1 . ILE B 1200 ? 0.2877 0.2380 0.2923 0.0134  0.0037  0.0219  1198 ILE B CG1 
17851 C CG2 . ILE B 1200 ? 0.2824 0.2215 0.2812 0.0188  0.0008  0.0219  1198 ILE B CG2 
17852 C CD1 . ILE B 1200 ? 0.2928 0.2382 0.2981 0.0102  0.0030  0.0221  1198 ILE B CD1 
17853 N N   . ALA B 1201 ? 0.3461 0.2896 0.3396 0.0214  0.0018  0.0278  1199 ALA B N   
17854 C CA  . ALA B 1201 ? 0.3840 0.3229 0.3737 0.0247  0.0004  0.0292  1199 ALA B CA  
17855 C C   . ALA B 1201 ? 0.3790 0.3244 0.3688 0.0278  0.0006  0.0287  1199 ALA B C   
17856 O O   . ALA B 1201 ? 0.4490 0.3930 0.4374 0.0317  -0.0007 0.0281  1199 ALA B O   
17857 C CB  . ALA B 1201 ? 0.3825 0.3157 0.3688 0.0227  0.0001  0.0328  1199 ALA B CB  
17858 N N   . ARG B 1202 ? 0.4074 0.3600 0.3988 0.0262  0.0021  0.0288  1200 ARG B N   
17859 C CA  . ARG B 1202 ? 0.3964 0.3549 0.3875 0.0285  0.0022  0.0286  1200 ARG B CA  
17860 C C   . ARG B 1202 ? 0.4164 0.3808 0.4105 0.0302  0.0023  0.0254  1200 ARG B C   
17861 O O   . ARG B 1202 ? 0.4262 0.3937 0.4200 0.0333  0.0016  0.0249  1200 ARG B O   
17862 C CB  . ARG B 1202 ? 0.4295 0.3925 0.4203 0.0260  0.0038  0.0301  1200 ARG B CB  
17863 C CG  . ARG B 1202 ? 0.5573 0.5159 0.5447 0.0242  0.0040  0.0337  1200 ARG B CG  
17864 C CD  . ARG B 1202 ? 0.6033 0.5672 0.5902 0.0222  0.0057  0.0349  1200 ARG B CD  
17865 N NE  . ARG B 1202 ? 0.5853 0.5549 0.5759 0.0201  0.0073  0.0327  1200 ARG B NE  
17866 C CZ  . ARG B 1202 ? 0.5889 0.5587 0.5811 0.0167  0.0088  0.0333  1200 ARG B CZ  
17867 N NH1 . ARG B 1202 ? 0.6111 0.5759 0.6016 0.0145  0.0089  0.0361  1200 ARG B NH1 
17868 N NH2 . ARG B 1202 ? 0.5225 0.4975 0.5180 0.0154  0.0101  0.0312  1200 ARG B NH2 
17869 N N   . ASN B 1203 ? 0.3449 0.3111 0.3421 0.0283  0.0032  0.0233  1201 ASN B N   
17870 C CA  . ASN B 1203 ? 0.3576 0.3302 0.3578 0.0291  0.0036  0.0206  1201 ASN B CA  
17871 C C   . ASN B 1203 ? 0.3300 0.3003 0.3317 0.0303  0.0029  0.0183  1201 ASN B C   
17872 O O   . ASN B 1203 ? 0.3403 0.3079 0.3432 0.0281  0.0032  0.0177  1201 ASN B O   
17873 C CB  . ASN B 1203 ? 0.3583 0.3356 0.3606 0.0259  0.0053  0.0200  1201 ASN B CB  
17874 C CG  . ASN B 1203 ? 0.3640 0.3472 0.3691 0.0264  0.0057  0.0172  1201 ASN B CG  
17875 O OD1 . ASN B 1203 ? 0.4270 0.4118 0.4326 0.0290  0.0048  0.0159  1201 ASN B OD1 
17876 N ND2 . ASN B 1203 ? 0.4131 0.3997 0.4201 0.0239  0.0070  0.0164  1201 ASN B ND2 
17877 N N   . PRO B 1204 ? 0.3740 0.3456 0.3756 0.0338  0.0020  0.0171  1202 PRO B N   
17878 C CA  . PRO B 1204 ? 0.3843 0.3540 0.3871 0.0351  0.0015  0.0148  1202 PRO B CA  
17879 C C   . PRO B 1204 ? 0.3408 0.3144 0.3468 0.0329  0.0025  0.0126  1202 PRO B C   
17880 O O   . PRO B 1204 ? 0.3676 0.3387 0.3743 0.0330  0.0023  0.0109  1202 PRO B O   
17881 C CB  . PRO B 1204 ? 0.4414 0.4140 0.4440 0.0393  0.0007  0.0140  1202 PRO B CB  
17882 C CG  . PRO B 1204 ? 0.4356 0.4086 0.4360 0.0404  0.0002  0.0165  1202 PRO B CG  
17883 C CD  . PRO B 1204 ? 0.3747 0.3496 0.3752 0.0367  0.0014  0.0178  1202 PRO B CD  
17884 N N   . ASP B 1205 ? 0.3244 0.3038 0.3320 0.0310  0.0036  0.0125  1203 ASP B N   
17885 C CA  . ASP B 1205 ? 0.3382 0.3212 0.3485 0.0290  0.0045  0.0105  1203 ASP B CA  
17886 C C   . ASP B 1205 ? 0.3402 0.3224 0.3512 0.0254  0.0055  0.0114  1203 ASP B C   
17887 O O   . ASP B 1205 ? 0.3279 0.3143 0.3410 0.0237  0.0064  0.0104  1203 ASP B O   
17888 C CB  . ASP B 1205 ? 0.3851 0.3752 0.3968 0.0296  0.0049  0.0094  1203 ASP B CB  
17889 C CG  . ASP B 1205 ? 0.4267 0.4187 0.4386 0.0328  0.0041  0.0083  1203 ASP B CG  
17890 O OD1 . ASP B 1205 ? 0.3979 0.3860 0.4092 0.0345  0.0035  0.0076  1203 ASP B OD1 
17891 O OD2 . ASP B 1205 ? 0.4934 0.4908 0.5058 0.0337  0.0041  0.0080  1203 ASP B OD2 
17892 N N   . ALA B 1206 ? 0.3210 0.2979 0.3303 0.0244  0.0053  0.0134  1204 ALA B N   
17893 C CA  . ALA B 1206 ? 0.3012 0.2776 0.3115 0.0209  0.0062  0.0144  1204 ALA B CA  
17894 C C   . ALA B 1206 ? 0.2673 0.2448 0.2805 0.0192  0.0065  0.0124  1204 ALA B C   
17895 O O   . ALA B 1206 ? 0.3003 0.2812 0.3155 0.0170  0.0076  0.0122  1204 ALA B O   
17896 C CB  . ALA B 1206 ? 0.3266 0.2964 0.3348 0.0199  0.0056  0.0167  1204 ALA B CB  
17897 N N   . TYR B 1207 ? 0.2526 0.2270 0.2659 0.0205  0.0055  0.0108  1205 TYR B N   
17898 C CA  . TYR B 1207 ? 0.2483 0.2240 0.2639 0.0194  0.0055  0.0086  1205 TYR B CA  
17899 C C   . TYR B 1207 ? 0.2510 0.2304 0.2672 0.0218  0.0054  0.0065  1205 TYR B C   
17900 O O   . TYR B 1207 ? 0.3310 0.3092 0.3456 0.0246  0.0047  0.0063  1205 TYR B O   
17901 C CB  . TYR B 1207 ? 0.2400 0.2094 0.2551 0.0188  0.0044  0.0082  1205 TYR B CB  
17902 C CG  . TYR B 1207 ? 0.2343 0.2000 0.2490 0.0159  0.0044  0.0104  1205 TYR B CG  
17903 C CD1 . TYR B 1207 ? 0.2228 0.1920 0.2399 0.0129  0.0055  0.0111  1205 TYR B CD1 
17904 C CD2 . TYR B 1207 ? 0.2510 0.2097 0.2629 0.0162  0.0033  0.0119  1205 TYR B CD2 
17905 C CE1 . TYR B 1207 ? 0.2136 0.1802 0.2308 0.0100  0.0056  0.0132  1205 TYR B CE1 
17906 C CE2 . TYR B 1207 ? 0.2538 0.2091 0.2654 0.0132  0.0032  0.0141  1205 TYR B CE2 
17907 C CZ  . TYR B 1207 ? 0.2365 0.1961 0.2509 0.0100  0.0045  0.0148  1205 TYR B CZ  
17908 O OH  . TYR B 1207 ? 0.2324 0.1895 0.2468 0.0068  0.0046  0.0171  1205 TYR B OH  
17909 N N   . CYS B 1208 ? 0.2006 0.1847 0.2191 0.0208  0.0061  0.0050  1206 CYS B N   
17910 C CA  . CYS B 1208 ? 0.1923 0.1805 0.2114 0.0225  0.0061  0.0033  1206 CYS B CA  
17911 C C   . CYS B 1208 ? 0.2062 0.1927 0.2259 0.0228  0.0056  0.0013  1206 CYS B C   
17912 O O   . CYS B 1208 ? 0.1971 0.1828 0.2182 0.0208  0.0056  0.0006  1206 CYS B O   
17913 C CB  . CYS B 1208 ? 0.2313 0.2249 0.2520 0.0210  0.0071  0.0029  1206 CYS B CB  
17914 S SG  . CYS B 1208 ? 0.2633 0.2621 0.2847 0.0225  0.0071  0.0010  1206 CYS B SG  
17915 N N   . LEU B 1209 ? 0.1925 0.1787 0.2112 0.0255  0.0050  0.0004  1207 LEU B N   
17916 C CA  . LEU B 1209 ? 0.1791 0.1636 0.1978 0.0262  0.0045  -0.0016 1207 LEU B CA  
17917 C C   . LEU B 1209 ? 0.1740 0.1632 0.1947 0.0251  0.0051  -0.0031 1207 LEU B C   
17918 O O   . LEU B 1209 ? 0.1789 0.1669 0.1998 0.0249  0.0048  -0.0046 1207 LEU B O   
17919 C CB  . LEU B 1209 ? 0.1685 0.1518 0.1855 0.0297  0.0040  -0.0021 1207 LEU B CB  
17920 C CG  . LEU B 1209 ? 0.2187 0.1968 0.2334 0.0312  0.0032  -0.0006 1207 LEU B CG  
17921 C CD1 . LEU B 1209 ? 0.2292 0.2061 0.2423 0.0350  0.0027  -0.0016 1207 LEU B CD1 
17922 C CD2 . LEU B 1209 ? 0.2442 0.2157 0.2580 0.0291  0.0026  -0.0001 1207 LEU B CD2 
17923 N N   . ASN B 1210 ? 0.1762 0.1705 0.1980 0.0244  0.0058  -0.0028 1208 ASN B N   
17924 C CA  . ASN B 1210 ? 0.2197 0.2179 0.2431 0.0233  0.0062  -0.0041 1208 ASN B CA  
17925 C C   . ASN B 1210 ? 0.1828 0.1792 0.2073 0.0210  0.0062  -0.0047 1208 ASN B C   
17926 O O   . ASN B 1210 ? 0.2086 0.2061 0.2338 0.0205  0.0061  -0.0061 1208 ASN B O   
17927 C CB  . ASN B 1210 ? 0.2454 0.2484 0.2694 0.0226  0.0068  -0.0036 1208 ASN B CB  
17928 C CG  . ASN B 1210 ? 0.2368 0.2425 0.2599 0.0247  0.0067  -0.0031 1208 ASN B CG  
17929 O OD1 . ASN B 1210 ? 0.2980 0.3021 0.3201 0.0268  0.0062  -0.0029 1208 ASN B OD1 
17930 N ND2 . ASN B 1210 ? 0.2996 0.3096 0.3231 0.0240  0.0070  -0.0029 1208 ASN B ND2 
17931 N N   . TRP B 1211 ? 0.1815 0.1751 0.2062 0.0195  0.0062  -0.0035 1209 TRP B N   
17932 C CA  . TRP B 1211 ? 0.1691 0.1619 0.1954 0.0172  0.0061  -0.0037 1209 TRP B CA  
17933 C C   . TRP B 1211 ? 0.1922 0.1801 0.2178 0.0170  0.0051  -0.0043 1209 TRP B C   
17934 O O   . TRP B 1211 ? 0.2157 0.2028 0.2428 0.0150  0.0048  -0.0046 1209 TRP B O   
17935 C CB  . TRP B 1211 ? 0.1995 0.1930 0.2267 0.0155  0.0069  -0.0021 1209 TRP B CB  
17936 C CG  . TRP B 1211 ? 0.2067 0.2039 0.2335 0.0160  0.0077  -0.0013 1209 TRP B CG  
17937 C CD1 . TRP B 1211 ? 0.2217 0.2187 0.2475 0.0161  0.0082  0.0004  1209 TRP B CD1 
17938 C CD2 . TRP B 1211 ? 0.1891 0.1905 0.2162 0.0166  0.0081  -0.0024 1209 TRP B CD2 
17939 N NE1 . TRP B 1211 ? 0.2347 0.2355 0.2600 0.0167  0.0087  0.0005  1209 TRP B NE1 
17940 C CE2 . TRP B 1211 ? 0.2080 0.2115 0.2341 0.0169  0.0087  -0.0012 1209 TRP B CE2 
17941 C CE3 . TRP B 1211 ? 0.2087 0.2120 0.2365 0.0166  0.0079  -0.0040 1209 TRP B CE3 
17942 C CZ2 . TRP B 1211 ? 0.2168 0.2241 0.2427 0.0173  0.0089  -0.0019 1209 TRP B CZ2 
17943 C CZ3 . TRP B 1211 ? 0.2063 0.2133 0.2339 0.0168  0.0082  -0.0045 1209 TRP B CZ3 
17944 C CH2 . TRP B 1211 ? 0.2211 0.2300 0.2477 0.0171  0.0087  -0.0035 1209 TRP B CH2 
17945 N N   . LEU B 1212 ? 0.1763 0.1609 0.1999 0.0190  0.0045  -0.0045 1210 LEU B N   
17946 C CA  . LEU B 1212 ? 0.1586 0.1377 0.1810 0.0189  0.0034  -0.0052 1210 LEU B CA  
17947 C C   . LEU B 1212 ? 0.1781 0.1571 0.1996 0.0204  0.0029  -0.0073 1210 LEU B C   
17948 O O   . LEU B 1212 ? 0.1710 0.1454 0.1909 0.0208  0.0020  -0.0081 1210 LEU B O   
17949 C CB  . LEU B 1212 ? 0.1670 0.1413 0.1871 0.0203  0.0028  -0.0040 1210 LEU B CB  
17950 C CG  . LEU B 1212 ? 0.1628 0.1358 0.1834 0.0182  0.0030  -0.0017 1210 LEU B CG  
17951 C CD1 . LEU B 1212 ? 0.2095 0.1786 0.2276 0.0199  0.0026  -0.0003 1210 LEU B CD1 
17952 C CD2 . LEU B 1212 ? 0.2004 0.1702 0.2220 0.0153  0.0023  -0.0017 1210 LEU B CD2 
17953 N N   . VAL B 1213 ? 0.1669 0.1510 0.1892 0.0211  0.0037  -0.0081 1211 VAL B N   
17954 C CA  . VAL B 1213 ? 0.1756 0.1605 0.1974 0.0220  0.0035  -0.0099 1211 VAL B CA  
17955 C C   . VAL B 1213 ? 0.1627 0.1508 0.1864 0.0198  0.0037  -0.0104 1211 VAL B C   
17956 O O   . VAL B 1213 ? 0.1818 0.1725 0.2072 0.0184  0.0043  -0.0095 1211 VAL B O   
17957 C CB  . VAL B 1213 ? 0.1656 0.1538 0.1865 0.0246  0.0041  -0.0104 1211 VAL B CB  
17958 C CG1 . VAL B 1213 ? 0.1906 0.1751 0.2093 0.0272  0.0036  -0.0102 1211 VAL B CG1 
17959 C CG2 . VAL B 1213 ? 0.1794 0.1728 0.2018 0.0242  0.0049  -0.0093 1211 VAL B CG2 
17960 N N   . GLU B 1214 ? 0.1623 0.1497 0.1854 0.0197  0.0032  -0.0119 1212 GLU B N   
17961 C CA  . GLU B 1214 ? 0.1841 0.1743 0.2086 0.0181  0.0033  -0.0125 1212 GLU B CA  
17962 C C   . GLU B 1214 ? 0.1603 0.1542 0.1842 0.0193  0.0039  -0.0134 1212 GLU B C   
17963 O O   . GLU B 1214 ? 0.1715 0.1647 0.1937 0.0211  0.0038  -0.0143 1212 GLU B O   
17964 C CB  . GLU B 1214 ? 0.2325 0.2194 0.2568 0.0169  0.0021  -0.0135 1212 GLU B CB  
17965 C CG  . GLU B 1214 ? 0.2581 0.2477 0.2838 0.0153  0.0021  -0.0140 1212 GLU B CG  
17966 C CD  . GLU B 1214 ? 0.2983 0.2851 0.3234 0.0144  0.0008  -0.0150 1212 GLU B CD  
17967 O OE1 . GLU B 1214 ? 0.2912 0.2738 0.3156 0.0141  -0.0002 -0.0152 1212 GLU B OE1 
17968 O OE2 . GLU B 1214 ? 0.3331 0.3218 0.3584 0.0138  0.0006  -0.0157 1212 GLU B OE2 
17969 N N   . GLU B 1215 ? 0.1499 0.1477 0.1752 0.0183  0.0044  -0.0131 1213 GLU B N   
17970 C CA  . GLU B 1215 ? 0.1586 0.1600 0.1835 0.0187  0.0049  -0.0137 1213 GLU B CA  
17971 C C   . GLU B 1215 ? 0.1480 0.1487 0.1724 0.0178  0.0043  -0.0148 1213 GLU B C   
17972 O O   . GLU B 1215 ? 0.1622 0.1616 0.1876 0.0162  0.0038  -0.0148 1213 GLU B O   
17973 C CB  . GLU B 1215 ? 0.1644 0.1694 0.1906 0.0177  0.0055  -0.0129 1213 GLU B CB  
17974 C CG  . GLU B 1215 ? 0.1676 0.1739 0.1942 0.0184  0.0059  -0.0117 1213 GLU B CG  
17975 C CD  . GLU B 1215 ? 0.1566 0.1655 0.1842 0.0171  0.0063  -0.0112 1213 GLU B CD  
17976 O OE1 . GLU B 1215 ? 0.1691 0.1768 0.1976 0.0160  0.0063  -0.0108 1213 GLU B OE1 
17977 O OE2 . GLU B 1215 ? 0.1765 0.1886 0.2038 0.0173  0.0066  -0.0112 1213 GLU B OE2 
17978 N N   . VAL B 1216 ? 0.1524 0.1542 0.1753 0.0188  0.0045  -0.0156 1214 VAL B N   
17979 C CA  . VAL B 1216 ? 0.1569 0.1585 0.1790 0.0179  0.0041  -0.0165 1214 VAL B CA  
17980 C C   . VAL B 1216 ? 0.1379 0.1436 0.1595 0.0179  0.0048  -0.0165 1214 VAL B C   
17981 O O   . VAL B 1216 ? 0.1577 0.1658 0.1788 0.0195  0.0055  -0.0165 1214 VAL B O   
17982 C CB  . VAL B 1216 ? 0.1573 0.1553 0.1772 0.0189  0.0034  -0.0177 1214 VAL B CB  
17983 C CG1 . VAL B 1216 ? 0.1867 0.1849 0.2054 0.0181  0.0030  -0.0186 1214 VAL B CG1 
17984 C CG2 . VAL B 1216 ? 0.1957 0.1893 0.2161 0.0184  0.0025  -0.0176 1214 VAL B CG2 
17985 N N   . SER B 1217 ? 0.1370 0.1438 0.1591 0.0162  0.0046  -0.0165 1215 SER B N   
17986 C CA  . SER B 1217 ? 0.1429 0.1531 0.1644 0.0156  0.0050  -0.0164 1215 SER B CA  
17987 C C   . SER B 1217 ? 0.1399 0.1489 0.1595 0.0153  0.0046  -0.0172 1215 SER B C   
17988 O O   . SER B 1217 ? 0.1610 0.1670 0.1804 0.0146  0.0037  -0.0176 1215 SER B O   
17989 C CB  . SER B 1217 ? 0.1648 0.1761 0.1874 0.0139  0.0049  -0.0157 1215 SER B CB  
17990 O OG  . SER B 1217 ? 0.1858 0.1989 0.2075 0.0127  0.0049  -0.0157 1215 SER B OG  
17991 N N   . ALA B 1218 ? 0.1391 0.1507 0.1573 0.0158  0.0053  -0.0174 1216 ALA B N   
17992 C CA  . ALA B 1218 ? 0.1607 0.1715 0.1767 0.0154  0.0050  -0.0180 1216 ALA B CA  
17993 C C   . ALA B 1218 ? 0.1620 0.1767 0.1776 0.0142  0.0057  -0.0174 1216 ALA B C   
17994 O O   . ALA B 1218 ? 0.1827 0.2013 0.1988 0.0149  0.0067  -0.0170 1216 ALA B O   
17995 C CB  . ALA B 1218 ? 0.1868 0.1964 0.2008 0.0175  0.0053  -0.0190 1216 ALA B CB  
17996 N N   . SER B 1219 ? 0.1528 0.1664 0.1675 0.0124  0.0050  -0.0172 1217 SER B N   
17997 C CA  . SER B 1219 ? 0.1486 0.1651 0.1625 0.0109  0.0054  -0.0165 1217 SER B CA  
17998 C C   . SER B 1219 ? 0.1500 0.1660 0.1611 0.0107  0.0054  -0.0169 1217 SER B C   
17999 O O   . SER B 1219 ? 0.1609 0.1733 0.1708 0.0102  0.0043  -0.0173 1217 SER B O   
18000 C CB  . SER B 1219 ? 0.1764 0.1918 0.1910 0.0089  0.0046  -0.0158 1217 SER B CB  
18001 O OG  . SER B 1219 ? 0.1773 0.1949 0.1909 0.0072  0.0048  -0.0150 1217 SER B OG  
18002 N N   . ILE B 1220 ? 0.1670 0.1867 0.1770 0.0112  0.0066  -0.0167 1218 ILE B N   
18003 C CA  . ILE B 1220 ? 0.1669 0.1867 0.1740 0.0112  0.0069  -0.0170 1218 ILE B CA  
18004 C C   . ILE B 1220 ? 0.1710 0.1937 0.1773 0.0089  0.0072  -0.0158 1218 ILE B C   
18005 O O   . ILE B 1220 ? 0.1765 0.2038 0.1841 0.0084  0.0082  -0.0150 1218 ILE B O   
18006 C CB  . ILE B 1220 ? 0.2038 0.2258 0.2100 0.0138  0.0081  -0.0179 1218 ILE B CB  
18007 C CG1 . ILE B 1220 ? 0.2464 0.2648 0.2532 0.0160  0.0076  -0.0190 1218 ILE B CG1 
18008 C CG2 . ILE B 1220 ? 0.2188 0.2411 0.2216 0.0140  0.0086  -0.0183 1218 ILE B CG2 
18009 C CD1 . ILE B 1220 ? 0.3823 0.4031 0.3893 0.0188  0.0088  -0.0196 1218 ILE B CD1 
18010 N N   . ASN B 1221 ? 0.1730 0.1930 0.1770 0.0074  0.0063  -0.0156 1219 ASN B N   
18011 C CA  . ASN B 1221 ? 0.1709 0.1930 0.1734 0.0050  0.0066  -0.0143 1219 ASN B CA  
18012 C C   . ASN B 1221 ? 0.1970 0.2228 0.1974 0.0058  0.0081  -0.0143 1219 ASN B C   
18013 O O   . ASN B 1221 ? 0.2120 0.2358 0.2096 0.0066  0.0080  -0.0150 1219 ASN B O   
18014 C CB  . ASN B 1221 ? 0.1837 0.2011 0.1841 0.0035  0.0050  -0.0140 1219 ASN B CB  
18015 C CG  . ASN B 1221 ? 0.1936 0.2122 0.1918 0.0009  0.0051  -0.0126 1219 ASN B CG  
18016 O OD1 . ASN B 1221 ? 0.1864 0.2096 0.1849 -0.0001 0.0063  -0.0117 1219 ASN B OD1 
18017 N ND2 . ASN B 1221 ? 0.2265 0.2409 0.2223 -0.0002 0.0037  -0.0123 1219 ASN B ND2 
18018 N N   . THR B 1222 ? 0.1838 0.2154 0.1856 0.0055  0.0096  -0.0136 1220 THR B N   
18019 C CA  . THR B 1222 ? 0.1904 0.2266 0.1906 0.0065  0.0113  -0.0135 1220 THR B CA  
18020 C C   . THR B 1222 ? 0.2344 0.2727 0.2325 0.0036  0.0117  -0.0120 1220 THR B C   
18021 O O   . THR B 1222 ? 0.2980 0.3411 0.2949 0.0040  0.0134  -0.0117 1220 THR B O   
18022 C CB  . THR B 1222 ? 0.2148 0.2568 0.2179 0.0081  0.0128  -0.0135 1220 THR B CB  
18023 O OG1 . THR B 1222 ? 0.2429 0.2878 0.2485 0.0057  0.0126  -0.0121 1220 THR B OG1 
18024 C CG2 . THR B 1222 ? 0.2464 0.2859 0.2511 0.0111  0.0124  -0.0149 1220 THR B CG2 
18025 N N   . ALA B 1223 ? 0.2144 0.2492 0.2117 0.0009  0.0102  -0.0111 1221 ALA B N   
18026 C CA  . ALA B 1223 ? 0.2691 0.3043 0.2637 -0.0019 0.0102  -0.0096 1221 ALA B CA  
18027 C C   . ALA B 1223 ? 0.3320 0.3617 0.3229 -0.0019 0.0091  -0.0100 1221 ALA B C   
18028 O O   . ALA B 1223 ? 0.4144 0.4434 0.4025 -0.0042 0.0088  -0.0087 1221 ALA B O   
18029 C CB  . ALA B 1223 ? 0.2954 0.3298 0.2911 -0.0051 0.0092  -0.0081 1221 ALA B CB  
18030 N N   . ALA B 1224 ? 0.3491 0.3750 0.3398 0.0006  0.0084  -0.0117 1222 ALA B N   
18031 C CA  . ALA B 1224 ? 0.3964 0.4167 0.3840 0.0006  0.0068  -0.0121 1222 ALA B CA  
18032 C C   . ALA B 1224 ? 0.4659 0.4872 0.4492 0.0004  0.0075  -0.0119 1222 ALA B C   
18033 O O   . ALA B 1224 ? 0.4176 0.4347 0.3978 -0.0006 0.0062  -0.0115 1222 ALA B O   
18034 C CB  . ALA B 1224 ? 0.3410 0.3575 0.3297 0.0030  0.0057  -0.0140 1222 ALA B CB  
18035 N N   . ALA B 1225 ? 0.4150 0.4416 0.3979 0.0014  0.0097  -0.0120 1223 ALA B N   
18036 C CA  . ALA B 1225 ? 0.4123 0.4404 0.3909 0.0013  0.0107  -0.0116 1223 ALA B CA  
18037 C C   . ALA B 1225 ? 0.4877 0.5177 0.4646 -0.0022 0.0110  -0.0093 1223 ALA B C   
18038 O O   . ALA B 1225 ? 0.4828 0.5135 0.4557 -0.0028 0.0117  -0.0087 1223 ALA B O   
18039 C CB  . ALA B 1225 ? 0.4580 0.4915 0.4366 0.0040  0.0131  -0.0126 1223 ALA B CB  
18040 N N   . GLY B 1226 ? 0.4589 0.4894 0.4384 -0.0046 0.0105  -0.0079 1224 GLY B N   
18041 C CA  . GLY B 1226 ? 0.4252 0.4567 0.4030 -0.0083 0.0105  -0.0056 1224 GLY B CA  
18042 C C   . GLY B 1226 ? 0.4909 0.5290 0.4716 -0.0102 0.0120  -0.0042 1224 GLY B C   
18043 O O   . GLY B 1226 ? 0.4489 0.4882 0.4282 -0.0136 0.0120  -0.0021 1224 GLY B O   
18044 N N   . GLY B 1227 ? 0.4125 0.4550 0.3970 -0.0081 0.0131  -0.0052 1225 GLY B N   
18045 C CA  . GLY B 1227 ? 0.3807 0.4301 0.3684 -0.0097 0.0143  -0.0039 1225 GLY B CA  
18046 C C   . GLY B 1227 ? 0.4554 0.5078 0.4472 -0.0067 0.0150  -0.0054 1225 GLY B C   
18047 O O   . GLY B 1227 ? 0.4330 0.4821 0.4249 -0.0035 0.0146  -0.0073 1225 GLY B O   
18048 N N   . ASN B 1228 ? 0.3851 0.4439 0.3802 -0.0078 0.0160  -0.0044 1226 ASN B N   
18049 C CA  . ASN B 1228 ? 0.4197 0.4819 0.4189 -0.0053 0.0165  -0.0054 1226 ASN B CA  
18050 C C   . ASN B 1228 ? 0.4946 0.5654 0.4950 -0.0035 0.0189  -0.0053 1226 ASN B C   
18051 O O   . ASN B 1228 ? 0.5389 0.6160 0.5400 -0.0060 0.0200  -0.0035 1226 ASN B O   
18052 C CB  . ASN B 1228 ? 0.4107 0.4733 0.4128 -0.0079 0.0153  -0.0044 1226 ASN B CB  
18053 C CG  . ASN B 1228 ? 0.4581 0.5227 0.4640 -0.0053 0.0153  -0.0055 1226 ASN B CG  
18054 O OD1 . ASN B 1228 ? 0.4540 0.5232 0.4614 -0.0023 0.0168  -0.0062 1226 ASN B OD1 
18055 N ND2 . ASN B 1228 ? 0.3784 0.4393 0.3858 -0.0065 0.0136  -0.0055 1226 ASN B ND2 
18056 N N   . ALA B 1229 ? 0.4633 0.5343 0.4639 0.0008  0.0198  -0.0072 1227 ALA B N   
18057 C CA  . ALA B 1229 ? 0.5105 0.5895 0.5122 0.0033  0.0222  -0.0073 1227 ALA B CA  
18058 C C   . ALA B 1229 ? 0.5559 0.6422 0.5624 0.0026  0.0227  -0.0063 1227 ALA B C   
18059 O O   . ALA B 1229 ? 0.5066 0.6013 0.5144 0.0018  0.0244  -0.0050 1227 ALA B O   
18060 C CB  . ALA B 1229 ? 0.4282 0.5045 0.4290 0.0082  0.0226  -0.0097 1227 ALA B CB  
18061 N N   . SER B 1230 ? 0.5575 0.6410 0.5666 0.0030  0.0212  -0.0067 1228 SER B N   
18062 C CA  . SER B 1230 ? 0.5285 0.6186 0.5420 0.0029  0.0215  -0.0059 1228 SER B CA  
18063 C C   . SER B 1230 ? 0.6324 0.7273 0.6471 -0.0020 0.0213  -0.0036 1228 SER B C   
18064 O O   . SER B 1230 ? 0.6643 0.7680 0.6819 -0.0024 0.0225  -0.0025 1228 SER B O   
18065 C CB  . SER B 1230 ? 0.5070 0.5923 0.5225 0.0040  0.0197  -0.0069 1228 SER B CB  
18066 N N   . LEU B 1231 ? 0.5718 0.6610 0.5842 -0.0057 0.0198  -0.0028 1229 LEU B N   
18067 C CA  . LEU B 1231 ? 0.5799 0.6724 0.5929 -0.0106 0.0194  -0.0006 1229 LEU B CA  
18068 C C   . LEU B 1231 ? 0.6175 0.7158 0.6289 -0.0124 0.0213  0.0009  1229 LEU B C   
18069 O O   . LEU B 1231 ? 0.6286 0.7312 0.6410 -0.0166 0.0212  0.0030  1229 LEU B O   
18070 C CB  . LEU B 1231 ? 0.5498 0.6337 0.5606 -0.0138 0.0170  -0.0003 1229 LEU B CB  
18071 C CG  . LEU B 1231 ? 0.4101 0.4891 0.4225 -0.0136 0.0151  -0.0011 1229 LEU B CG  
18072 C CD1 . LEU B 1231 ? 0.3362 0.4078 0.3459 -0.0172 0.0130  -0.0004 1229 LEU B CD1 
18073 C CD2 . LEU B 1231 ? 0.4518 0.5374 0.4683 -0.0142 0.0151  -0.0004 1229 LEU B CD2 
18074 N N   . MET B 1232 ? 0.5688 0.6672 0.5777 -0.0095 0.0228  0.0000  1230 MET B N   
18075 C CA  . MET B 1232 ? 0.5497 0.6550 0.5574 -0.0107 0.0250  0.0014  1230 MET B CA  
18076 C C   . MET B 1232 ? 0.6086 0.7253 0.6208 -0.0104 0.0267  0.0024  1230 MET B C   
18077 O O   . MET B 1232 ? 0.4955 0.6193 0.5082 -0.0135 0.0279  0.0045  1230 MET B O   
18078 C CB  . MET B 1232 ? 0.5206 0.6236 0.5246 -0.0069 0.0264  -0.0002 1230 MET B CB  
18079 N N   . ALA B 1233 ? 0.6753 0.7944 0.6909 -0.0066 0.0268  0.0010  1231 ALA B N   
18080 C CA  . ALA B 1233 ? 0.7731 0.9031 0.7934 -0.0059 0.0282  0.0018  1231 ALA B CA  
18081 C C   . ALA B 1233 ? 0.7766 0.9090 0.8003 -0.0100 0.0265  0.0034  1231 ALA B C   
18082 O O   . ALA B 1233 ? 0.7905 0.9320 0.8185 -0.0096 0.0272  0.0042  1231 ALA B O   
18083 C CB  . ALA B 1233 ? 0.6882 0.8193 0.7103 0.0001  0.0289  -0.0003 1231 ALA B CB  
18084 N N   . ILE B 1234 ? 0.7086 0.8332 0.7305 -0.0137 0.0242  0.0039  1232 ILE B N   
18085 C CA  . ILE B 1234 ? 0.6880 0.8132 0.7123 -0.0175 0.0223  0.0051  1232 ILE B CA  
18086 C C   . ILE B 1234 ? 0.6014 0.7279 0.6242 -0.0234 0.0220  0.0075  1232 ILE B C   
18087 O O   . ILE B 1234 ? 0.5359 0.6543 0.5546 -0.0257 0.0210  0.0078  1232 ILE B O   
18088 C CB  . ILE B 1234 ? 0.6139 0.7290 0.6372 -0.0170 0.0199  0.0037  1232 ILE B CB  
18089 C CG1 . ILE B 1234 ? 0.6488 0.7642 0.6744 -0.0118 0.0201  0.0018  1232 ILE B CG1 
18090 C CG2 . ILE B 1234 ? 0.5299 0.6440 0.5543 -0.0216 0.0177  0.0050  1232 ILE B CG2 
18091 C CD1 . ILE B 1234 ? 0.4975 0.6065 0.5237 -0.0117 0.0178  0.0009  1232 ILE B CD1 
18092 N N   . GLY B 1235 ? 0.5836 0.7202 0.6097 -0.0260 0.0229  0.0094  1233 GLY B N   
18093 C CA  . GLY B 1235 ? 0.4214 0.5601 0.4466 -0.0321 0.0225  0.0120  1233 GLY B CA  
18094 C C   . GLY B 1235 ? 0.3789 0.5230 0.4081 -0.0356 0.0211  0.0134  1233 GLY B C   
18095 O O   . GLY B 1235 ? 0.5670 0.7186 0.6007 -0.0333 0.0216  0.0131  1233 GLY B O   
18096 O OXT . GLY B 1235 ? 0.2777 0.4185 0.3056 -0.0410 0.0193  0.0149  1233 GLY B OXT 
# 
